Browse entries in the PDBbind-CN Database
HEADER HYDROLASE/HYDROLASE INHIBITOR 03-DEC-18 6N9D TITLE COMPLEX OF TISSUE INHIBITOR OF METALLOPROTEINASES-1 (TIMP-1) MUTANT TITLE 2 (L34G/L133P/L151C/G154A) WITH MATRIX METALLOPROTEINASE-3 CATALYTIC TITLE 3 DOMAIN (MMP-3CD) COMPND MOL_ID: 1; COMPND 2 MOLECULE: STROMELYSIN-1; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: SL-1,MATRIX METALLOPROTEINASE-3,MMP-3,TRANSIN-1; COMPND 5 EC: 3.4.24.17; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: METALLOPROTEINASE INHIBITOR 1; COMPND 9 CHAIN: B; COMPND 10 SYNONYM: ERYTHROID-POTENTIATING ACTIVITY,EPA,FIBROBLAST COLLAGENASE COMPND 11 INHIBITOR,COLLAGENASE INHIBITOR,TISSUE INHIBITOR OF COMPND 12 METALLOPROTEINASES 1,TIMP-1; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: MMP3, STMY1; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_COMMON: HUMAN; SOURCE 12 ORGANISM_TAXID: 9606; SOURCE 13 GENE: TIMP1, CLGI, TIMP; SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 15 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS TISSUE INHIBITOR OF METALLOPROTEINASES, MATRIX METALLOPROTEINASE, KEYWDS 2 HYDROLASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR M.RAEESZADEH-SARMAZDEH,E.S.RADISKY,B.SANKARAN REVDAT 3 04-DEC-19 6N9D 1 REMARK REVDAT 2 26-JUN-19 6N9D 1 JRNL REVDAT 1 15-MAY-19 6N9D 0 JRNL AUTH M.RAEESZADEH-SARMAZDEH,K.A.GREENE,B.SANKARAN,G.P.DOWNEY, JRNL AUTH 2 D.C.RADISKY,E.S.RADISKY JRNL TITL DIRECTED EVOLUTION OF THE METALLOPROTEINASE INHIBITOR TIMP-1 JRNL TITL 2 REVEALS THAT ITS N- AND C-TERMINAL DOMAINS COOPERATE IN JRNL TITL 3 MATRIX METALLOPROTEINASE RECOGNITION. JRNL REF J.BIOL.CHEM. V. 294 9476 2019 JRNL REFN ESSN 1083-351X JRNL PMID 31040180 JRNL DOI 10.1074/JBC.RA119.008321 REMARK 2 REMARK 2 RESOLUTION. 2.67 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.9_1692 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) : 2.67 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.99 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 14140 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.189 REMARK 3 R VALUE (WORKING SET) : 0.184 REMARK 3 FREE R VALUE : 0.258 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.350 REMARK 3 FREE R VALUE TEST SET COUNT : 1039 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 43.9963 - 5.1052 1.00 2069 162 0.1680 0.2409 REMARK 3 2 5.1052 - 4.0531 1.00 1904 151 0.1412 0.2140 REMARK 3 3 4.0531 - 3.5410 1.00 1857 148 0.1648 0.2305 REMARK 3 4 3.5410 - 3.2174 1.00 1840 146 0.2120 0.3155 REMARK 3 5 3.2174 - 2.9868 1.00 1834 146 0.2207 0.3261 REMARK 3 6 2.9868 - 2.8107 1.00 1799 143 0.2549 0.2659 REMARK 3 7 2.8107 - 2.6700 0.99 1798 143 0.3221 0.4075 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) : 0.400 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.200 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 55.93 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.11 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 : 0.009 2706 REMARK 3 ANGLE : 1.304 3680 REMARK 3 CHIRALITY : 0.049 402 REMARK 3 PLANARITY : 0.007 476 REMARK 3 DIHEDRAL : 16.368 949 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 5 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 87 THROUGH 147 ) REMARK 3 ORIGIN FOR THE GROUP (A): 25.4035 27.1386 10.2626 REMARK 3 T TENSOR REMARK 3 T11: 0.3339 T22: 0.5127 REMARK 3 T33: 0.5186 T12: 0.0236 REMARK 3 T13: -0.0328 T23: -0.0911 REMARK 3 L TENSOR REMARK 3 L11: 3.6401 L22: 5.9231 REMARK 3 L33: 4.5513 L12: 2.0652 REMARK 3 L13: 0.1833 L23: -2.1618 REMARK 3 S TENSOR REMARK 3 S11: 0.1169 S12: -0.2328 S13: -0.1394 REMARK 3 S21: 0.2511 S22: -0.3101 S23: -1.0575 REMARK 3 S31: 0.1399 S32: 0.6620 S33: 0.1443 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 148 THROUGH 207 ) REMARK 3 ORIGIN FOR THE GROUP (A): 14.7458 20.6886 13.7329 REMARK 3 T TENSOR REMARK 3 T11: 0.5081 T22: 0.2821 REMARK 3 T33: 0.3635 T12: -0.0444 REMARK 3 T13: -0.0433 T23: -0.0490 REMARK 3 L TENSOR REMARK 3 L11: 4.0548 L22: 2.7607 REMARK 3 L33: 4.5577 L12: 0.1535 REMARK 3 L13: -0.1441 L23: 0.5903 REMARK 3 S TENSOR REMARK 3 S11: 0.0761 S12: -0.0320 S13: -0.7159 REMARK 3 S21: 0.4231 S22: -0.3094 S23: -0.2601 REMARK 3 S31: 0.8346 S32: -0.2583 S33: 0.2354 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 208 THROUGH 247 ) REMARK 3 ORIGIN FOR THE GROUP (A): 11.1675 29.5753 0.5633 REMARK 3 T TENSOR REMARK 3 T11: 0.3632 T22: 0.4182 REMARK 3 T33: 0.4755 T12: 0.0455 REMARK 3 T13: -0.0582 T23: -0.1341 REMARK 3 L TENSOR REMARK 3 L11: 5.8107 L22: 2.6802 REMARK 3 L33: 3.0647 L12: 2.8080 REMARK 3 L13: -0.5366 L23: -2.1117 REMARK 3 S TENSOR REMARK 3 S11: -0.0055 S12: 0.6196 S13: 0.0606 REMARK 3 S21: -0.2623 S22: -0.0039 S23: 0.7312 REMARK 3 S31: 0.2527 S32: -0.3108 S33: 0.0455 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 90 ) REMARK 3 ORIGIN FOR THE GROUP (A): -5.8736 23.6341 20.7732 REMARK 3 T TENSOR REMARK 3 T11: 0.5745 T22: 0.3144 REMARK 3 T33: 0.3100 T12: -0.0607 REMARK 3 T13: 0.0442 T23: -0.0747 REMARK 3 L TENSOR REMARK 3 L11: 5.3852 L22: 3.3491 REMARK 3 L33: 4.1670 L12: 1.4013 REMARK 3 L13: 0.2489 L23: 1.1305 REMARK 3 S TENSOR REMARK 3 S11: 0.1652 S12: -0.3803 S13: 0.4206 REMARK 3 S21: 0.7122 S22: -0.2779 S23: 0.2628 REMARK 3 S31: 0.3489 S32: -0.4264 S33: 0.0686 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 91 THROUGH 179 ) REMARK 3 ORIGIN FOR THE GROUP (A): -5.7266 9.3658 8.1272 REMARK 3 T TENSOR REMARK 3 T11: 0.4813 T22: 0.3146 REMARK 3 T33: 0.3257 T12: -0.0965 REMARK 3 T13: 0.0211 T23: -0.0277 REMARK 3 L TENSOR REMARK 3 L11: 1.0151 L22: 5.2375 REMARK 3 L33: 3.3935 L12: -1.1303 REMARK 3 L13: -0.4156 L23: 3.3570 REMARK 3 S TENSOR REMARK 3 S11: 0.0545 S12: 0.2083 S13: 0.0059 REMARK 3 S21: 0.2424 S22: -0.0611 S23: 0.0467 REMARK 3 S31: 0.3439 S32: 0.0098 S33: -0.0069 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 6N9D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-DEC-18. REMARK 100 THE DEPOSITION ID IS D_1000238376. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 22-MAY-18 REMARK 200 TEMPERATURE (KELVIN) : 80 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ALS REMARK 200 BEAMLINE : 8.2.1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2 REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14162 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.670 REMARK 200 RESOLUTION RANGE LOW (A) : 43.990 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 20.40 REMARK 200 R MERGE (I) : 0.24690 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.1100 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.67 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.77 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 21.10 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.160 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: 1UEA REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 57.30 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM ACETATE, 0.1 M SODIUM REMARK 280 CACODYLATE: HCL, PH 6.5 18 % (W/V) PEG 8000, VAPOR DIFFUSION, REMARK 280 HANGING DROP, TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+2/3 REMARK 290 3555 -X+Y,-X,Z+1/3 REMARK 290 4555 -X,-Y,Z+1/2 REMARK 290 5555 Y,-X+Y,Z+1/6 REMARK 290 6555 X-Y,X,Z+5/6 REMARK 290 7555 Y,X,-Z+2/3 REMARK 290 8555 X-Y,-Y,-Z REMARK 290 9555 -X,-X+Y,-Z+1/3 REMARK 290 10555 -Y,-X,-Z+1/6 REMARK 290 11555 -X+Y,Y,-Z+1/2 REMARK 290 12555 X,X-Y,-Z+5/6 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 213.00800 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 106.50400 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 159.75600 REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 53.25200 REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 266.26000 REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 213.00800 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 106.50400 REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 53.25200 REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 159.75600 REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 266.26000 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: 2680 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 15820 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -81.0 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 HOH B 220 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 PHE A 83 REMARK 465 ARG A 84 REMARK 465 THR A 85 REMARK 465 PHE A 86 REMARK 465 GLY B 53 REMARK 465 ASP B 54 REMARK 465 ALA B 55 REMARK 465 ALA B 56 REMARK 465 ARG B 180 REMARK 465 SER B 181 REMARK 465 GLN B 182 REMARK 465 ILE B 183 REMARK 465 ALA B 184 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 ARG A 233 CD NE CZ NH1 NH2 REMARK 470 ARG B 59 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 75 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 114 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 118 CG CD CE NZ REMARK 470 LYS B 138 CG CD CE NZ REMARK 470 LYS B 157 CG CD CE NZ REMARK 480 REMARK 480 ZERO OCCUPANCY ATOM REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 480 M RES C SSEQI ATOMS REMARK 480 GLN B 31 CG CD OE1 NE2 REMARK 480 GLU B 126 CG CD OE1 OE2 REMARK 480 GLU B 156 CG CD OE1 OE2 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 O ALA A 167 OG SER B 68 2.03 REMARK 500 O ASN B 78 O HOH B 201 2.04 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 LEU B 52 CA - CB - CG ANGL. DEV. = 14.0 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 LYS A 110 38.55 -75.12 REMARK 500 ASP A 111 -48.72 -156.73 REMARK 500 ARG A 149 -107.07 43.44 REMARK 500 HIS A 151 -50.55 72.60 REMARK 500 ASN A 162 -107.74 52.05 REMARK 500 ASP A 189 -147.10 -98.38 REMARK 500 LEU A 229 -33.07 79.83 REMARK 500 ASN B 30 75.60 49.20 REMARK 500 CYS B 70 31.65 81.61 REMARK 500 ASN B 78 -111.54 65.24 REMARK 500 LYS B 118 -62.43 -133.72 REMARK 500 PRO B 133 -88.69 -71.02 REMARK 500 GLN B 153 50.78 -101.75 REMARK 500 HIS B 163 -13.56 -140.05 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 GLU A 150 HIS A 151 139.41 REMARK 500 HIS B 77 ASN B 78 136.38 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 302 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 107 OD1 REMARK 620 2 ASP A 107 OD2 52.4 REMARK 620 3 ASP A 182 O 177.1 125.3 REMARK 620 4 ASP A 182 OD1 105.9 88.1 71.8 REMARK 620 5 GLU A 184 O 109.1 61.3 69.6 93.3 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 305 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 141 O REMARK 620 2 GLY A 173 O 164.7 REMARK 620 3 ASN A 175 O 93.5 81.5 REMARK 620 4 ASP A 177 OD1 86.2 78.8 81.7 REMARK 620 5 HOH A 406 O 111.2 70.1 149.9 83.2 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 303 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 151 NE2 REMARK 620 2 ASP A 153 OD2 115.5 REMARK 620 3 HIS A 166 NE2 133.4 107.6 REMARK 620 4 HIS A 179 ND1 80.4 100.2 109.1 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 301 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 158 OD1 REMARK 620 2 GLY A 159 O 85.5 REMARK 620 3 GLY A 161 O 82.9 99.2 REMARK 620 4 VAL A 163 O 92.4 171.3 88.9 REMARK 620 5 ASP A 181 OD2 93.6 77.7 175.5 94.0 REMARK 620 6 GLU A 184 OE2 175.2 95.6 101.6 85.9 82.1 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 304 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 201 NE2 REMARK 620 2 HIS A 205 NE2 90.4 REMARK 620 3 HIS A 211 NE2 117.9 93.7 REMARK 620 4 CYS B 1 N 110.6 91.4 131.1 REMARK 620 5 CYS B 1 O 82.0 164.3 102.0 78.6 REMARK 620 N 1 2 3 4 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 303 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 304 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 305 DBREF 6N9D A 83 247 UNP P08254 MMP3_HUMAN 100 264 DBREF 6N9D B 1 184 UNP P01033 TIMP1_HUMAN 24 207 SEQADV 6N9D GLY B 34 UNP P01033 LEU 57 ENGINEERED MUTATION SEQADV 6N9D PRO B 133 UNP P01033 LEU 156 ENGINEERED MUTATION SEQADV 6N9D CYS B 151 UNP P01033 LEU 174 ENGINEERED MUTATION SEQADV 6N9D ALA B 154 UNP P01033 GLY 177 ENGINEERED MUTATION SEQRES 1 A 165 PHE ARG THR PHE PRO GLY ILE PRO LYS TRP ARG LYS THR SEQRES 2 A 165 HIS LEU THR TYR ARG ILE VAL ASN TYR THR PRO ASP LEU SEQRES 3 A 165 PRO LYS ASP ALA VAL ASP SER ALA VAL GLU LYS ALA LEU SEQRES 4 A 165 LYS VAL TRP GLU GLU VAL THR PRO LEU THR PHE SER ARG SEQRES 5 A 165 LEU TYR GLU GLY GLU ALA ASP ILE MET ILE SER PHE ALA SEQRES 6 A 165 VAL ARG GLU HIS GLY ASP PHE TYR PRO PHE ASP GLY PRO SEQRES 7 A 165 GLY ASN VAL LEU ALA HIS ALA TYR ALA PRO GLY PRO GLY SEQRES 8 A 165 ILE ASN GLY ASP ALA HIS PHE ASP ASP ASP GLU GLN TRP SEQRES 9 A 165 THR LYS ASP THR THR GLY THR ASN LEU PHE LEU VAL ALA SEQRES 10 A 165 ALA HIS GLU ILE GLY HIS SER LEU GLY LEU PHE HIS SER SEQRES 11 A 165 ALA ASN THR GLU ALA LEU MET TYR PRO LEU TYR HIS SER SEQRES 12 A 165 LEU THR ASP LEU THR ARG PHE ARG LEU SER GLN ASP ASP SEQRES 13 A 165 ILE ASN GLY ILE GLN SER LEU TYR GLY SEQRES 1 B 184 CYS THR CYS VAL PRO PRO HIS PRO GLN THR ALA PHE CYS SEQRES 2 B 184 ASN SER ASP LEU VAL ILE ARG ALA LYS PHE VAL GLY THR SEQRES 3 B 184 PRO GLU VAL ASN GLN THR THR GLY TYR GLN ARG TYR GLU SEQRES 4 B 184 ILE LYS MET THR LYS MET TYR LYS GLY PHE GLN ALA LEU SEQRES 5 B 184 GLY ASP ALA ALA ASP ILE ARG PHE VAL TYR THR PRO ALA SEQRES 6 B 184 MET GLU SER VAL CYS GLY TYR PHE HIS ARG SER HIS ASN SEQRES 7 B 184 ARG SER GLU GLU PHE LEU ILE ALA GLY LYS LEU GLN ASP SEQRES 8 B 184 GLY LEU LEU HIS ILE THR THR CYS SER PHE VAL ALA PRO SEQRES 9 B 184 TRP ASN SER LEU SER LEU ALA GLN ARG ARG GLY PHE THR SEQRES 10 B 184 LYS THR TYR THR VAL GLY CYS GLU GLU CYS THR VAL PHE SEQRES 11 B 184 PRO CYS PRO SER ILE PRO CYS LYS LEU GLN SER GLY THR SEQRES 12 B 184 HIS CYS LEU TRP THR ASP GLN CYS LEU GLN ALA SER GLU SEQRES 13 B 184 LYS GLY PHE GLN SER ARG HIS LEU ALA CYS LEU PRO ARG SEQRES 14 B 184 GLU PRO GLY LEU CYS THR TRP GLN SER LEU ARG SER GLN SEQRES 15 B 184 ILE ALA HET CA A 301 1 HET CA A 302 1 HET ZN A 303 1 HET ZN A 304 1 HET CA A 305 1 HETNAM CA CALCIUM ION HETNAM ZN ZINC ION FORMUL 3 CA 3(CA 2+) FORMUL 5 ZN 2(ZN 2+) FORMUL 8 HOH *46(H2 O) HELIX 1 AA1 ASP A 111 GLU A 126 1 16 HELIX 2 AA2 LEU A 195 GLY A 208 1 14 HELIX 3 AA3 SER A 235 GLY A 247 1 13 HELIX 4 AA4 HIS B 7 SER B 15 1 9 HELIX 5 AA5 MET B 66 CYS B 70 5 5 HELIX 6 AA6 ASN B 106 LEU B 108 5 3 HELIX 7 AA7 SER B 109 THR B 117 1 9 HELIX 8 AA8 TYR B 120 GLU B 125 1 6 HELIX 9 AA9 GLN B 153 GLY B 158 1 6 HELIX 10 AB1 GLY B 158 HIS B 163 1 6 SHEET 1 AA1 6 THR A 131 ARG A 134 0 SHEET 2 AA1 6 HIS A 96 ILE A 101 1 N LEU A 97 O THR A 131 SHEET 3 AA1 6 ILE A 142 ALA A 147 1 O ILE A 144 N ARG A 100 SHEET 4 AA1 6 ALA A 178 ASP A 181 1 O PHE A 180 N ALA A 147 SHEET 5 AA1 6 ASN A 162 ALA A 167 -1 N HIS A 166 O HIS A 179 SHEET 6 AA1 6 THR B 2 VAL B 4 -1 O THR B 2 N LEU A 164 SHEET 1 AA2 2 TRP A 186 THR A 187 0 SHEET 2 AA2 2 THR A 193 ASN A 194 1 O THR A 193 N THR A 187 SHEET 1 AA3 7 PHE B 101 PRO B 104 0 SHEET 2 AA3 7 PHE B 83 GLN B 90 -1 N LEU B 84 O ALA B 103 SHEET 3 AA3 7 LEU B 93 HIS B 95 -1 O HIS B 95 N LYS B 88 SHEET 4 AA3 7 PHE B 60 PRO B 64 1 N TYR B 62 O LEU B 94 SHEET 5 AA3 7 TYR B 35 LYS B 47 -1 N GLN B 36 O THR B 63 SHEET 6 AA3 7 LEU B 17 PHE B 23 -1 N ARG B 20 O THR B 43 SHEET 7 AA3 7 PHE B 83 GLN B 90 -1 O ILE B 85 N ILE B 19 SHEET 1 AA4 2 THR B 128 PRO B 131 0 SHEET 2 AA4 2 HIS B 144 TRP B 147 1 O CYS B 145 N THR B 128 SHEET 1 AA5 2 LEU B 164 GLU B 170 0 SHEET 2 AA5 2 LEU B 173 SER B 178 -1 O GLN B 177 N ALA B 165 SSBOND 1 CYS B 1 CYS B 70 1555 1555 2.04 SSBOND 2 CYS B 3 CYS B 99 1555 1555 2.03 SSBOND 3 CYS B 13 CYS B 124 1555 1555 2.04 SSBOND 4 CYS B 127 CYS B 174 1555 1555 2.06 SSBOND 5 CYS B 132 CYS B 137 1555 1555 2.04 SSBOND 6 CYS B 145 CYS B 166 1555 1555 2.04 LINK OD1 ASP A 107 CA CA A 302 1555 1555 2.56 LINK OD2 ASP A 107 CA CA A 302 1555 1555 2.43 LINK O ASP A 141 CA CA A 305 1555 1555 2.36 LINK NE2 HIS A 151 ZN ZN A 303 1555 1555 2.30 LINK OD2 ASP A 153 ZN ZN A 303 1555 1555 2.37 LINK OD1 ASP A 158 CA CA A 301 1555 1555 2.37 LINK O GLY A 159 CA CA A 301 1555 1555 2.27 LINK O GLY A 161 CA CA A 301 1555 1555 2.45 LINK O VAL A 163 CA CA A 301 1555 1555 2.22 LINK NE2 HIS A 166 ZN ZN A 303 1555 1555 2.09 LINK O GLY A 173 CA CA A 305 1555 1555 2.39 LINK O ASN A 175 CA CA A 305 1555 1555 2.32 LINK OD1 ASP A 177 CA CA A 305 1555 1555 2.74 LINK ND1 HIS A 179 ZN ZN A 303 1555 1555 1.99 LINK OD2 ASP A 181 CA CA A 301 1555 1555 2.52 LINK O ASP A 182 CA CA A 302 1555 1555 2.42 LINK OD1 ASP A 182 CA CA A 302 1555 1555 2.54 LINK O GLU A 184 CA CA A 302 1555 1555 3.11 LINK OE2 GLU A 184 CA CA A 301 1555 1555 2.46 LINK NE2 HIS A 201 ZN ZN A 304 1555 1555 2.03 LINK NE2 HIS A 205 ZN ZN A 304 1555 1555 2.24 LINK NE2 HIS A 211 ZN ZN A 304 1555 1555 1.99 LINK N CYS B 1 ZN ZN A 304 1555 1555 2.18 LINK O CYS B 1 ZN ZN A 304 1555 1555 2.36 LINK CA CA A 305 O HOH A 406 1555 1555 2.49 CISPEP 1 ASN B 78 ARG B 79 0 -22.11 CISPEP 2 ILE B 135 PRO B 136 0 2.73 SITE 1 AC1 6 ASP A 158 GLY A 159 GLY A 161 VAL A 163 SITE 2 AC1 6 ASP A 181 GLU A 184 SITE 1 AC2 4 THR A 105 ASP A 107 ASP A 182 GLU A 184 SITE 1 AC3 4 HIS A 151 ASP A 153 HIS A 166 HIS A 179 SITE 1 AC4 4 HIS A 201 HIS A 205 HIS A 211 CYS B 1 SITE 1 AC5 6 ALA A 140 ASP A 141 GLY A 173 ASN A 175 SITE 2 AC5 6 ASP A 177 HOH A 406 CRYST1 70.031 70.031 319.512 90.00 90.00 120.00 P 65 2 2 12 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 0.014279 0.008244 0.000000 0.00000 SCALE2 0.000000 0.016488 0.000000 0.00000 SCALE3 0.000000 0.000000 0.003130 0.00000 ATOM 1 N PRO A 87 7.821 46.970 18.178 1.00101.82 N ANISOU 1 N PRO A 87 14196 10082 14409 2128 3554 -3327 N ATOM 2 CA PRO A 87 7.074 45.754 17.833 1.00103.45 C ANISOU 2 CA PRO A 87 13948 10687 14671 2196 3601 -3066 C ATOM 3 C PRO A 87 8.021 44.580 17.543 1.00103.30 C ANISOU 3 C PRO A 87 13915 10957 14377 1881 3293 -3012 C ATOM 4 O PRO A 87 7.614 43.412 17.567 1.00 92.64 O ANISOU 4 O PRO A 87 12317 9962 12920 1847 3315 -2876 O ATOM 5 CB PRO A 87 6.277 46.174 16.596 1.00103.30 C ANISOU 5 CB PRO A 87 13479 10545 15225 2477 3592 -2730 C ATOM 6 CG PRO A 87 6.212 47.680 16.675 1.00105.12 C ANISOU 6 CG PRO A 87 13939 10310 15690 2655 3701 -2859 C ATOM 7 CD PRO A 87 7.517 48.088 17.271 1.00102.21 C ANISOU 7 CD PRO A 87 14119 9761 14954 2363 3545 -3186 C ATOM 8 N GLY A 88 9.281 44.916 17.270 1.00109.64 N ANISOU 8 N GLY A 88 14980 11596 15082 1644 3007 -3118 N ATOM 9 CA GLY A 88 10.371 43.958 17.278 1.00103.45 C ANISOU 9 CA GLY A 88 14284 11046 13976 1312 2723 -3150 C ATOM 10 C GLY A 88 10.562 43.108 16.041 1.00100.34 C ANISOU 10 C GLY A 88 13508 10837 13779 1274 2519 -2900 C ATOM 11 O GLY A 88 9.945 42.051 15.914 1.00103.82 O ANISOU 11 O GLY A 88 13660 11585 14203 1324 2576 -2747 O ATOM 12 N ILE A 89 11.431 43.554 15.135 1.00 87.49 N ANISOU 12 N ILE A 89 11881 9039 12324 1159 2258 -2844 N ATOM 13 CA ILE A 89 11.830 42.719 14.003 1.00 73.77 C ANISOU 13 CA ILE A 89 9819 7588 10621 1036 1909 -2515 C ATOM 14 C ILE A 89 13.265 42.215 14.132 1.00 62.38 C ANISOU 14 C ILE A 89 8539 6305 8860 694 1582 -2569 C ATOM 15 O ILE A 89 14.224 42.937 13.843 1.00 53.50 O ANISOU 15 O ILE A 89 7559 4995 7775 534 1392 -2602 O ATOM 16 CB ILE A 89 11.725 43.450 12.671 1.00 70.69 C ANISOU 16 CB ILE A 89 9218 7010 10629 1133 1772 -2252 C ATOM 17 CG1 ILE A 89 10.480 44.322 12.637 1.00 74.82 C ANISOU 17 CG1 ILE A 89 9630 7251 11549 1485 2079 -2214 C ATOM 18 CG2 ILE A 89 11.740 42.438 11.522 1.00 61.01 C ANISOU 18 CG2 ILE A 89 7651 6118 9413 1053 1512 -1911 C ATOM 19 CD1 ILE A 89 10.379 45.135 11.376 1.00 79.82 C ANISOU 19 CD1 ILE A 89 10086 7659 12581 1569 1913 -1926 C ATOM 20 N PRO A 90 13.411 40.950 14.523 1.00 62.18 N ANISOU 20 N PRO A 90 8453 6622 8549 581 1504 -2541 N ATOM 21 CA PRO A 90 14.719 40.366 14.803 1.00 58.01 C ANISOU 21 CA PRO A 90 8044 6257 7740 291 1212 -2574 C ATOM 22 C PRO A 90 15.568 40.197 13.550 1.00 55.63 C ANISOU 22 C PRO A 90 7525 6029 7583 191 926 -2339 C ATOM 23 O PRO A 90 15.131 39.665 12.526 1.00 63.04 O ANISOU 23 O PRO A 90 8186 7101 8665 290 895 -2104 O ATOM 24 CB PRO A 90 14.365 39.009 15.391 1.00 64.75 C ANISOU 24 CB PRO A 90 8834 7432 8338 271 1240 -2540 C ATOM 25 CG PRO A 90 13.103 38.631 14.649 1.00 69.40 C ANISOU 25 CG PRO A 90 9103 8110 9157 503 1396 -2332 C ATOM 26 CD PRO A 90 12.346 39.933 14.504 1.00 71.15 C ANISOU 26 CD PRO A 90 9336 8020 9677 721 1640 -2395 C ATOM 27 N LYS A 91 16.792 40.682 13.645 1.00 48.22 N ANISOU 27 N LYS A 91 6730 5002 6590 -29 724 -2403 N ATOM 28 CA LYS A 91 17.800 40.409 12.654 1.00 45.15 C ANISOU 28 CA LYS A 91 6144 4730 6279 -161 481 -2201 C ATOM 29 C LYS A 91 19.124 40.449 13.386 1.00 43.95 C ANISOU 29 C LYS A 91 6143 4607 5948 -438 260 -2298 C ATOM 30 O LYS A 91 19.262 41.146 14.392 1.00 46.76 O ANISOU 30 O LYS A 91 6807 4784 6176 -556 271 -2519 O ATOM 31 CB LYS A 91 17.756 41.420 11.499 1.00 49.87 C ANISOU 31 CB LYS A 91 6655 5116 7176 -116 476 -2064 C ATOM 32 CG LYS A 91 18.090 42.848 11.899 1.00 54.45 C ANISOU 32 CG LYS A 91 7504 5335 7849 -210 478 -2224 C ATOM 33 CD LYS A 91 18.278 43.753 10.698 1.00 57.11 C ANISOU 33 CD LYS A 91 7748 5482 8470 -226 410 -2032 C ATOM 34 CE LYS A 91 19.755 43.950 10.388 1.00 70.89 C ANISOU 34 CE LYS A 91 9475 7275 10186 -531 166 -1958 C ATOM 35 NZ LYS A 91 20.007 45.005 9.354 1.00 85.09 N ANISOU 35 NZ LYS A 91 11247 8847 12235 -602 104 -1784 N ATOM 36 N TRP A 92 20.078 39.665 12.905 1.00 42.10 N ANISOU 36 N TRP A 92 5697 4598 5701 -546 65 -2129 N ATOM 37 CA TRP A 92 21.441 39.742 13.388 1.00 43.38 C ANISOU 37 CA TRP A 92 5895 4805 5783 -816 -188 -2134 C ATOM 38 C TRP A 92 21.964 41.155 13.185 1.00 45.80 C ANISOU 38 C TRP A 92 6328 4840 6232 -982 -257 -2178 C ATOM 39 O TRP A 92 21.694 41.785 12.168 1.00 45.47 O ANISOU 39 O TRP A 92 6198 4664 6414 -896 -171 -2079 O ATOM 40 CB TRP A 92 22.314 38.726 12.657 1.00 44.96 C ANISOU 40 CB TRP A 92 5769 5267 6048 -832 -320 -1906 C ATOM 41 CG TRP A 92 22.063 37.314 13.099 1.00 51.56 C ANISOU 41 CG TRP A 92 6540 6328 6723 -734 -322 -1874 C ATOM 42 CD1 TRP A 92 21.422 36.336 12.402 1.00 48.36 C ANISOU 42 CD1 TRP A 92 5982 6050 6342 -537 -200 -1770 C ATOM 43 CD2 TRP A 92 22.437 36.732 14.354 1.00 44.15 C ANISOU 43 CD2 TRP A 92 5722 5493 5559 -859 -479 -1931 C ATOM 44 NE1 TRP A 92 21.387 35.177 13.137 1.00 36.94 N ANISOU 44 NE1 TRP A 92 4548 4761 4726 -521 -259 -1761 N ATOM 45 CE2 TRP A 92 22.000 35.397 14.341 1.00 40.79 C ANISOU 45 CE2 TRP A 92 5196 5245 5059 -710 -432 -1846 C ATOM 46 CE3 TRP A 92 23.104 37.209 15.479 1.00 43.85 C ANISOU 46 CE3 TRP A 92 5893 5408 5358 -1114 -681 -2031 C ATOM 47 CZ2 TRP A 92 22.206 34.539 15.420 1.00 39.92 C ANISOU 47 CZ2 TRP A 92 5172 5263 4735 -791 -576 -1840 C ATOM 48 CZ3 TRP A 92 23.312 36.366 16.523 1.00 44.69 C ANISOU 48 CZ3 TRP A 92 6086 5662 5230 -1208 -836 -2022 C ATOM 49 CH2 TRP A 92 22.864 35.047 16.498 1.00 42.71 C ANISOU 49 CH2 TRP A 92 5718 5585 4926 -1039 -780 -1919 C ATOM 50 N ARG A 93 22.710 41.662 14.153 1.00 56.23 N ANISOU 50 N ARG A 93 7881 6069 7415 -1250 -437 -2309 N ATOM 51 CA ARG A 93 23.282 42.998 14.015 1.00 55.36 C ANISOU 51 CA ARG A 93 7926 5676 7431 -1464 -540 -2349 C ATOM 52 C ARG A 93 24.668 42.992 13.350 1.00 60.06 C ANISOU 52 C ARG A 93 8228 6414 8177 -1700 -792 -2104 C ATOM 53 O ARG A 93 25.125 44.015 12.888 1.00 61.30 O ANISOU 53 O ARG A 93 8421 6373 8499 -1865 -861 -2055 O ATOM 54 CB ARG A 93 23.328 43.671 15.377 1.00 59.53 C ANISOU 54 CB ARG A 93 8917 5986 7717 -1678 -604 -2635 C ATOM 55 CG ARG A 93 21.963 44.220 15.793 1.00 68.62 C ANISOU 55 CG ARG A 93 10385 6860 8827 -1434 -264 -2894 C ATOM 56 CD ARG A 93 21.780 44.244 17.310 1.00 88.08 C ANISOU 56 CD ARG A 93 13297 9258 10911 -1572 -234 -3198 C ATOM 57 NE ARG A 93 23.009 44.581 18.026 1.00101.76 N ANISOU 57 NE ARG A 93 15250 10966 12448 -2019 -596 -3245 N ATOM 58 CZ ARG A 93 23.330 44.114 19.233 1.00107.38 C ANISOU 58 CZ ARG A 93 16139 11850 12810 -2186 -757 -3298 C ATOM 59 NH1 ARG A 93 22.508 43.282 19.864 1.00103.63 N ANISOU 59 NH1 ARG A 93 15717 11551 12108 -1994 -558 -3366 N ATOM 60 NH2 ARG A 93 24.474 44.478 19.810 1.00111.82 N ANISOU 60 NH2 ARG A 93 16780 12436 13272 -2535 -1117 -3232 N ATOM 61 N LYS A 94 25.315 41.834 13.270 1.00 63.59 N ANISOU 61 N LYS A 94 8371 7198 8595 -1701 -904 -1935 N ATOM 62 CA LYS A 94 26.538 41.682 12.483 1.00 59.26 C ANISOU 62 CA LYS A 94 7454 6823 8241 -1841 -1050 -1672 C ATOM 63 C LYS A 94 26.176 41.000 11.150 1.00 57.76 C ANISOU 63 C LYS A 94 6970 6783 8192 -1564 -823 -1507 C ATOM 64 O LYS A 94 25.127 40.373 11.055 1.00 53.41 O ANISOU 64 O LYS A 94 6470 6265 7558 -1305 -642 -1573 O ATOM 65 CB LYS A 94 27.583 40.874 13.266 1.00 56.73 C ANISOU 65 CB LYS A 94 6968 6748 7838 -2014 -1322 -1572 C ATOM 66 CG LYS A 94 26.980 39.706 14.051 1.00 65.42 C ANISOU 66 CG LYS A 94 8145 7997 8714 -1838 -1291 -1654 C ATOM 67 CD LYS A 94 28.008 38.933 14.866 1.00 70.14 C ANISOU 67 CD LYS A 94 8589 8815 9248 -2014 -1604 -1514 C ATOM 68 CE LYS A 94 27.315 38.135 15.972 1.00 72.06 C ANISOU 68 CE LYS A 94 9078 9117 9182 -1947 -1620 -1642 C ATOM 69 NZ LYS A 94 28.243 37.446 16.923 1.00 76.16 N ANISOU 69 NZ LYS A 94 9512 9822 9602 -2153 -1981 -1491 N ATOM 70 N THR A 95 27.011 41.129 10.119 1.00 66.75 N ANISOU 70 N THR A 95 7823 8015 9524 -1642 -824 -1291 N ATOM 71 CA THR A 95 26.731 40.448 8.840 1.00 62.58 C ANISOU 71 CA THR A 95 7074 7634 9068 -1419 -601 -1150 C ATOM 72 C THR A 95 27.555 39.172 8.702 1.00 53.94 C ANISOU 72 C THR A 95 5661 6834 8000 -1348 -604 -1017 C ATOM 73 O THR A 95 27.199 38.267 7.948 1.00 52.49 O ANISOU 73 O THR A 95 5376 6771 7796 -1131 -416 -970 O ATOM 74 CB THR A 95 27.006 41.348 7.604 1.00 66.06 C ANISOU 74 CB THR A 95 7433 7992 9676 -1522 -520 -990 C ATOM 75 OG1 THR A 95 28.410 41.356 7.297 1.00 68.55 O ANISOU 75 OG1 THR A 95 7449 8471 10128 -1725 -601 -802 O ATOM 76 CG2 THR A 95 26.504 42.762 7.844 1.00 70.81 C ANISOU 76 CG2 THR A 95 8334 8248 10322 -1641 -577 -1088 C ATOM 77 N HIS A 96 28.658 39.104 9.437 1.00 53.15 N ANISOU 77 N HIS A 96 5410 6830 7954 -1538 -828 -947 N ATOM 78 CA HIS A 96 29.420 37.874 9.529 1.00 46.47 C ANISOU 78 CA HIS A 96 4255 6229 7172 -1438 -856 -813 C ATOM 79 C HIS A 96 28.950 36.994 10.711 1.00 55.35 C ANISOU 79 C HIS A 96 5535 7387 8108 -1344 -983 -925 C ATOM 80 O HIS A 96 29.060 37.377 11.878 1.00 63.80 O ANISOU 80 O HIS A 96 6786 8398 9056 -1543 -1231 -1003 O ATOM 81 CB HIS A 96 30.905 38.194 9.651 1.00 49.87 C ANISOU 81 CB HIS A 96 4358 6776 7814 -1689 -1054 -605 C ATOM 82 CG HIS A 96 31.773 36.979 9.694 1.00 66.10 C ANISOU 82 CG HIS A 96 6029 9068 10020 -1554 -1070 -424 C ATOM 83 ND1 HIS A 96 31.854 36.087 8.645 1.00 71.65 N ANISOU 83 ND1 HIS A 96 6511 9887 10827 -1276 -759 -346 N ATOM 84 CD2 HIS A 96 32.578 36.492 10.667 1.00 66.61 C ANISOU 84 CD2 HIS A 96 5904 9250 10154 -1648 -1361 -298 C ATOM 85 CE1 HIS A 96 32.677 35.107 8.969 1.00 77.37 C ANISOU 85 CE1 HIS A 96 6915 10769 11715 -1169 -827 -191 C ATOM 86 NE2 HIS A 96 33.132 35.330 10.190 1.00 73.90 N ANISOU 86 NE2 HIS A 96 6463 10343 11272 -1391 -1211 -135 N ATOM 87 N LEU A 97 28.416 35.817 10.409 1.00 48.47 N ANISOU 87 N LEU A 97 4630 6601 7186 -1069 -817 -932 N ATOM 88 CA LEU A 97 27.980 34.897 11.455 1.00 46.41 C ANISOU 88 CA LEU A 97 4502 6379 6750 -988 -927 -999 C ATOM 89 C LEU A 97 28.870 33.676 11.558 1.00 48.79 C ANISOU 89 C LEU A 97 4502 6848 7187 -881 -1007 -814 C ATOM 90 O LEU A 97 29.653 33.390 10.660 1.00 53.51 O ANISOU 90 O LEU A 97 4786 7531 8015 -791 -883 -665 O ATOM 91 CB LEU A 97 26.531 34.425 11.228 1.00 39.91 C ANISOU 91 CB LEU A 97 3914 5493 5756 -774 -712 -1142 C ATOM 92 CG LEU A 97 25.285 35.319 11.378 1.00 38.98 C ANISOU 92 CG LEU A 97 4108 5205 5499 -784 -609 -1329 C ATOM 93 CD1 LEU A 97 25.598 36.621 12.057 1.00 41.29 C ANISOU 93 CD1 LEU A 97 4562 5354 5771 -1027 -756 -1420 C ATOM 94 CD2 LEU A 97 24.586 35.557 10.041 1.00 37.26 C ANISOU 94 CD2 LEU A 97 3868 4930 5359 -647 -373 -1308 C ATOM 95 N THR A 98 28.719 32.946 12.657 1.00 57.51 N ANISOU 95 N THR A 98 5713 7988 8151 -880 -1194 -818 N ATOM 96 CA THR A 98 29.373 31.652 12.827 1.00 61.13 C ANISOU 96 CA THR A 98 5925 8560 8743 -730 -1276 -634 C ATOM 97 C THR A 98 28.369 30.534 13.085 1.00 43.08 C ANISOU 97 C THR A 98 3851 6243 6275 -534 -1188 -710 C ATOM 98 O THR A 98 27.248 30.780 13.507 1.00 42.24 O ANISOU 98 O THR A 98 4071 6070 5909 -574 -1142 -885 O ATOM 99 CB THR A 98 30.391 31.668 13.983 1.00 59.52 C ANISOU 99 CB THR A 98 5585 8445 8584 -956 -1683 -460 C ATOM 100 OG1 THR A 98 29.824 32.341 15.114 1.00 60.88 O ANISOU 100 OG1 THR A 98 6147 8555 8432 -1213 -1881 -619 O ATOM 101 CG2 THR A 98 31.665 32.363 13.551 1.00 51.31 C ANISOU 101 CG2 THR A 98 4172 7482 7841 -1108 -1773 -278 C ATOM 102 N TYR A 99 28.791 29.305 12.822 1.00 43.56 N ANISOU 102 N TYR A 99 3714 6340 6497 -320 -1150 -566 N ATOM 103 CA TYR A 99 27.942 28.130 12.989 1.00 48.22 C ANISOU 103 CA TYR A 99 4493 6879 6950 -146 -1081 -604 C ATOM 104 C TYR A 99 28.774 26.914 13.401 1.00 50.29 C ANISOU 104 C TYR A 99 4541 7163 7403 -11 -1243 -380 C ATOM 105 O TYR A 99 29.960 26.775 13.054 1.00 46.80 O ANISOU 105 O TYR A 99 3731 6767 7283 71 -1263 -201 O ATOM 106 CB TYR A 99 27.151 27.818 11.700 1.00 43.78 C ANISOU 106 CB TYR A 99 4019 6240 6373 47 -726 -724 C ATOM 107 CG TYR A 99 27.951 27.178 10.584 1.00 40.64 C ANISOU 107 CG TYR A 99 3368 5832 6240 262 -515 -633 C ATOM 108 CD1 TYR A 99 28.687 27.951 9.698 1.00 44.21 C ANISOU 108 CD1 TYR A 99 3598 6334 6866 237 -366 -603 C ATOM 109 CD2 TYR A 99 27.979 25.796 10.426 1.00 48.25 C ANISOU 109 CD2 TYR A 99 4335 6720 7278 487 -441 -579 C ATOM 110 CE1 TYR A 99 29.432 27.364 8.678 1.00 54.29 C ANISOU 110 CE1 TYR A 99 4653 7611 8366 440 -108 -533 C ATOM 111 CE2 TYR A 99 28.717 25.197 9.406 1.00 56.36 C ANISOU 111 CE2 TYR A 99 5166 7706 8544 709 -188 -529 C ATOM 112 CZ TYR A 99 29.437 25.987 8.532 1.00 59.33 C ANISOU 112 CZ TYR A 99 5315 8158 9070 689 -2 -513 C ATOM 113 OH TYR A 99 30.167 25.407 7.517 1.00 60.65 O ANISOU 113 OH TYR A 99 5299 8294 9451 913 311 -479 O ATOM 114 N ARG A 100 28.147 26.033 14.159 1.00 44.08 N ANISOU 114 N ARG A 100 3969 6339 6440 14 -1354 -367 N ATOM 115 CA ARG A 100 28.822 24.830 14.569 1.00 48.65 C ANISOU 115 CA ARG A 100 4384 6895 7206 155 -1521 -136 C ATOM 116 C ARG A 100 27.840 23.686 14.553 1.00 50.69 C ANISOU 116 C ARG A 100 4906 7033 7318 298 -1414 -188 C ATOM 117 O ARG A 100 26.703 23.829 15.000 1.00 43.10 O ANISOU 117 O ARG A 100 4266 6078 6033 166 -1403 -326 O ATOM 118 CB ARG A 100 29.444 24.991 15.955 1.00 51.09 C ANISOU 118 CB ARG A 100 4652 7304 7457 -83 -1965 53 C ATOM 119 CG ARG A 100 29.805 23.659 16.586 1.00 56.62 C ANISOU 119 CG ARG A 100 5281 7957 8275 39 -2188 309 C ATOM 120 CD ARG A 100 30.811 23.787 17.702 1.00 67.93 C ANISOU 120 CD ARG A 100 6530 9505 9775 -175 -2663 594 C ATOM 121 NE ARG A 100 30.955 22.510 18.390 1.00 75.77 N ANISOU 121 NE ARG A 100 7525 10433 10831 -77 -2904 852 N ATOM 122 CZ ARG A 100 30.910 22.370 19.710 1.00 76.70 C ANISOU 122 CZ ARG A 100 7836 10623 10684 -348 -3312 1008 C ATOM 123 NH1 ARG A 100 30.737 23.436 20.478 1.00 73.96 N ANISOU 123 NH1 ARG A 100 7717 10407 9975 -730 -3497 895 N ATOM 124 NH2 ARG A 100 31.030 21.168 20.258 1.00 73.46 N ANISOU 124 NH2 ARG A 100 7428 10133 10352 -249 -3529 1275 N ATOM 125 N ILE A 101 28.275 22.561 14.003 1.00 52.28 N ANISOU 125 N ILE A 101 4970 7114 7778 570 -1310 -77 N ATOM 126 CA ILE A 101 27.479 21.356 14.049 1.00 52.12 C ANISOU 126 CA ILE A 101 5207 6944 7653 685 -1260 -87 C ATOM 127 C ILE A 101 27.943 20.606 15.267 1.00 54.08 C ANISOU 127 C ILE A 101 5418 7182 7948 650 -1626 175 C ATOM 128 O ILE A 101 28.995 19.969 15.265 1.00 64.22 O ANISOU 128 O ILE A 101 6418 8398 9585 840 -1722 399 O ATOM 129 CB ILE A 101 27.633 20.499 12.790 1.00 55.35 C ANISOU 129 CB ILE A 101 5578 7169 8284 988 -939 -138 C ATOM 130 CG1 ILE A 101 27.214 21.294 11.556 1.00 52.82 C ANISOU 130 CG1 ILE A 101 5310 6880 7878 975 -608 -369 C ATOM 131 CG2 ILE A 101 26.809 19.234 12.912 1.00 53.07 C ANISOU 131 CG2 ILE A 101 5596 6690 7879 1059 -934 -139 C ATOM 132 CD1 ILE A 101 27.810 20.756 10.283 1.00 56.71 C ANISOU 132 CD1 ILE A 101 5693 7243 8612 1243 -276 -408 C ATOM 133 N VAL A 102 27.144 20.696 16.312 1.00 49.20 N ANISOU 133 N VAL A 102 5084 6634 6975 406 -1820 163 N ATOM 134 CA VAL A 102 27.537 20.218 17.616 1.00 59.40 C ANISOU 134 CA VAL A 102 6393 7964 8211 272 -2219 421 C ATOM 135 C VAL A 102 27.332 18.723 17.746 1.00 68.87 C ANISOU 135 C VAL A 102 7702 8970 9497 440 -2271 587 C ATOM 136 O VAL A 102 27.715 18.106 18.733 1.00 74.60 O ANISOU 136 O VAL A 102 8429 9685 10230 371 -2615 860 O ATOM 137 CB VAL A 102 26.725 20.930 18.694 1.00 58.32 C ANISOU 137 CB VAL A 102 6574 7982 7602 -79 -2357 320 C ATOM 138 CG1 VAL A 102 27.445 20.867 20.024 1.00 63.78 C ANISOU 138 CG1 VAL A 102 7251 8775 8208 -305 -2818 586 C ATOM 139 CG2 VAL A 102 26.485 22.378 18.279 1.00 50.61 C ANISOU 139 CG2 VAL A 102 5607 7109 6515 -197 -2167 55 C ATOM 140 N ASN A 103 26.747 18.132 16.722 1.00 71.48 N ANISOU 140 N ASN A 103 8142 9126 9890 644 -1948 435 N ATOM 141 CA ASN A 103 26.012 16.909 16.929 1.00 61.72 C ANISOU 141 CA ASN A 103 7183 7709 8560 678 -1969 501 C ATOM 142 C ASN A 103 25.738 16.207 15.620 1.00 60.27 C ANISOU 142 C ASN A 103 7073 7284 8541 933 -1630 353 C ATOM 143 O ASN A 103 25.526 16.866 14.611 1.00 59.85 O ANISOU 143 O ASN A 103 6993 7274 8473 972 -1341 121 O ATOM 144 CB ASN A 103 24.707 17.258 17.623 1.00 56.13 C ANISOU 144 CB ASN A 103 6806 7143 7380 369 -1990 390 C ATOM 145 CG ASN A 103 24.134 16.117 18.332 1.00 52.16 C ANISOU 145 CG ASN A 103 6555 6528 6736 291 -2150 562 C ATOM 146 OD1 ASN A 103 24.841 15.177 18.651 1.00 55.13 O ANISOU 146 OD1 ASN A 103 6864 6742 7342 418 -2363 819 O ATOM 147 ND2 ASN A 103 22.845 16.176 18.610 1.00 52.67 N ANISOU 147 ND2 ASN A 103 6896 6673 6445 80 -2053 452 N ATOM 148 N TYR A 104 25.715 14.882 15.615 1.00 63.66 N ANISOU 148 N TYR A 104 7636 7445 9107 1086 -1668 481 N ATOM 149 CA TYR A 104 25.484 14.189 14.354 1.00 62.01 C ANISOU 149 CA TYR A 104 7566 6970 9025 1306 -1341 311 C ATOM 150 C TYR A 104 24.426 13.098 14.402 1.00 57.60 C ANISOU 150 C TYR A 104 7410 6191 8284 1222 -1356 308 C ATOM 151 O TYR A 104 24.456 12.237 15.267 1.00 56.18 O ANISOU 151 O TYR A 104 7328 5884 8136 1198 -1612 544 O ATOM 152 CB TYR A 104 26.795 13.602 13.845 1.00 55.30 C ANISOU 152 CB TYR A 104 6447 5903 8662 1687 -1244 420 C ATOM 153 CG TYR A 104 27.688 14.644 13.228 1.00 55.07 C ANISOU 153 CG TYR A 104 6044 6058 8822 1789 -1064 342 C ATOM 154 CD1 TYR A 104 28.794 15.133 13.908 1.00 59.58 C ANISOU 154 CD1 TYR A 104 6204 6797 9637 1809 -1301 580 C ATOM 155 CD2 TYR A 104 27.411 15.160 11.975 1.00 56.50 C ANISOU 155 CD2 TYR A 104 6289 6258 8919 1822 -686 56 C ATOM 156 CE1 TYR A 104 29.611 16.091 13.352 1.00 62.92 C ANISOU 156 CE1 TYR A 104 6272 7395 10242 1865 -1147 534 C ATOM 157 CE2 TYR A 104 28.223 16.127 11.409 1.00 64.39 C ANISOU 157 CE2 TYR A 104 6954 7432 10080 1885 -518 7 C ATOM 158 CZ TYR A 104 29.323 16.587 12.102 1.00 66.70 C ANISOU 158 CZ TYR A 104 6823 7883 10637 1907 -741 246 C ATOM 159 OH TYR A 104 30.132 17.550 11.543 1.00 71.64 O ANISOU 159 OH TYR A 104 7103 8685 11432 1935 -583 221 O ATOM 160 N THR A 105 23.495 13.134 13.454 1.00 52.58 N ANISOU 160 N THR A 105 7009 5508 7459 1150 -1104 64 N ATOM 161 CA THR A 105 22.560 12.032 13.289 1.00 50.05 C ANISOU 161 CA THR A 105 7069 4939 7008 1064 -1104 57 C ATOM 162 C THR A 105 23.249 10.796 12.694 1.00 61.90 C ANISOU 162 C THR A 105 8681 6007 8833 1377 -1002 81 C ATOM 163 O THR A 105 24.124 10.908 11.825 1.00 60.46 O ANISOU 163 O THR A 105 8343 5723 8906 1659 -752 -35 O ATOM 164 CB THR A 105 21.376 12.419 12.396 1.00 51.46 C ANISOU 164 CB THR A 105 7456 5193 6903 868 -903 -181 C ATOM 165 OG1 THR A 105 20.448 11.331 12.338 1.00 57.05 O ANISOU 165 OG1 THR A 105 8526 5673 7478 723 -960 -149 O ATOM 166 CG2 THR A 105 21.841 12.760 10.982 1.00 49.66 C ANISOU 166 CG2 THR A 105 7187 4890 6791 1054 -585 -411 C ATOM 167 N PRO A 106 22.866 9.606 13.184 1.00 66.28 N ANISOU 167 N PRO A 106 9510 6288 9385 1332 -1176 238 N ATOM 168 CA PRO A 106 23.343 8.313 12.678 1.00 65.88 C ANISOU 168 CA PRO A 106 9659 5745 9629 1613 -1083 254 C ATOM 169 C PRO A 106 22.747 7.917 11.326 1.00 59.69 C ANISOU 169 C PRO A 106 9244 4713 8723 1605 -772 -53 C ATOM 170 O PRO A 106 23.201 6.942 10.738 1.00 67.74 O ANISOU 170 O PRO A 106 10468 5296 9975 1863 -613 -115 O ATOM 171 CB PRO A 106 22.888 7.322 13.761 1.00 61.83 C ANISOU 171 CB PRO A 106 9366 5063 9064 1455 -1425 541 C ATOM 172 CG PRO A 106 22.597 8.141 14.950 1.00 59.69 C ANISOU 172 CG PRO A 106 8905 5227 8548 1173 -1693 715 C ATOM 173 CD PRO A 106 22.097 9.446 14.427 1.00 59.20 C ANISOU 173 CD PRO A 106 8725 5536 8233 1018 -1492 454 C ATOM 174 N ASP A 107 21.756 8.662 10.849 1.00 56.13 N ANISOU 174 N ASP A 107 8889 4523 7916 1309 -695 -234 N ATOM 175 CA ASP A 107 21.064 8.332 9.613 1.00 56.17 C ANISOU 175 CA ASP A 107 9272 4334 7734 1205 -477 -492 C ATOM 176 C ASP A 107 21.871 8.705 8.384 1.00 56.90 C ANISOU 176 C ASP A 107 9305 4363 7953 1470 -102 -742 C ATOM 177 O ASP A 107 21.451 8.470 7.246 1.00 63.43 O ANISOU 177 O ASP A 107 10474 5023 8603 1394 109 -978 O ATOM 178 CB ASP A 107 19.718 9.041 9.559 1.00 52.56 C ANISOU 178 CB ASP A 107 8879 4205 6888 791 -561 -538 C ATOM 179 CG ASP A 107 18.998 9.036 10.886 1.00 63.80 C ANISOU 179 CG ASP A 107 10236 5832 8174 535 -867 -288 C ATOM 180 OD1 ASP A 107 19.375 8.239 11.779 1.00 75.29 O ANISOU 180 OD1 ASP A 107 11723 7108 9775 609 -1057 -72 O ATOM 181 OD2 ASP A 107 18.049 9.836 11.027 1.00 52.34 O ANISOU 181 OD2 ASP A 107 8700 4715 6470 260 -904 -297 O ATOM 182 N LEU A 108 23.026 9.304 8.628 1.00 57.22 N ANISOU 182 N LEU A 108 8913 4553 8276 1746 -28 -673 N ATOM 183 CA LEU A 108 23.871 9.852 7.578 1.00 57.85 C ANISOU 183 CA LEU A 108 8832 4663 8484 1982 341 -867 C ATOM 184 C LEU A 108 25.324 9.778 7.997 1.00 60.76 C ANISOU 184 C LEU A 108 8777 4981 9326 2378 391 -702 C ATOM 185 O LEU A 108 25.616 9.721 9.188 1.00 61.14 O ANISOU 185 O LEU A 108 8581 5115 9536 2390 70 -421 O ATOM 186 CB LEU A 108 23.500 11.307 7.278 1.00 53.73 C ANISOU 186 CB LEU A 108 8109 4587 7719 1756 373 -955 C ATOM 187 CG LEU A 108 22.269 11.579 6.421 1.00 54.87 C ANISOU 187 CG LEU A 108 8594 4799 7456 1428 428 -1142 C ATOM 188 CD1 LEU A 108 22.113 13.080 6.168 1.00 58.06 C ANISOU 188 CD1 LEU A 108 8726 5614 7719 1281 463 -1185 C ATOM 189 CD2 LEU A 108 22.412 10.835 5.125 1.00 54.58 C ANISOU 189 CD2 LEU A 108 8949 4418 7370 1533 748 -1382 C ATOM 190 N PRO A 109 26.240 9.757 7.019 1.00 67.89 N ANISOU 190 N PRO A 109 9591 5753 10453 2691 796 -856 N ATOM 191 CA PRO A 109 27.665 9.941 7.307 1.00 71.23 C ANISOU 191 CA PRO A 109 9485 6223 11357 3055 878 -679 C ATOM 192 C PRO A 109 27.942 11.316 7.899 1.00 69.32 C ANISOU 192 C PRO A 109 8768 6479 11090 2884 676 -535 C ATOM 193 O PRO A 109 27.180 12.254 7.666 1.00 68.55 O ANISOU 193 O PRO A 109 8754 6664 10626 2569 648 -665 O ATOM 194 CB PRO A 109 28.318 9.785 5.936 1.00 72.37 C ANISOU 194 CB PRO A 109 9697 6177 11624 3343 1438 -939 C ATOM 195 CG PRO A 109 27.403 8.865 5.213 1.00 71.10 C ANISOU 195 CG PRO A 109 10209 5644 11163 3236 1576 -1196 C ATOM 196 CD PRO A 109 26.021 9.257 5.650 1.00 67.26 C ANISOU 196 CD PRO A 109 9954 5382 10219 2745 1199 -1178 C ATOM 197 N LYS A 110 29.028 11.431 8.654 1.00 76.03 N ANISOU 197 N LYS A 110 9130 7416 12342 3085 520 -255 N ATOM 198 CA LYS A 110 29.349 12.652 9.388 1.00 83.16 C ANISOU 198 CA LYS A 110 9616 8752 13230 2889 254 -89 C ATOM 199 C LYS A 110 29.866 13.715 8.436 1.00 88.34 C ANISOU 199 C LYS A 110 10023 9639 13905 2909 587 -243 C ATOM 200 O LYS A 110 30.760 14.488 8.772 1.00104.30 O ANISOU 200 O LYS A 110 11565 11907 16156 2928 500 -71 O ATOM 201 CB LYS A 110 30.389 12.353 10.474 1.00 88.58 C ANISOU 201 CB LYS A 110 9870 9440 14345 3063 -64 297 C ATOM 202 CG LYS A 110 31.521 11.437 9.996 1.00 96.53 C ANISOU 202 CG LYS A 110 10642 10125 15911 3564 213 394 C ATOM 203 CD LYS A 110 32.511 11.107 11.110 1.00 95.08 C ANISOU 203 CD LYS A 110 9996 9942 16187 3726 -170 843 C ATOM 204 CE LYS A 110 33.841 10.618 10.548 1.00 91.56 C ANISOU 204 CE LYS A 110 9159 9346 16284 4187 151 942 C ATOM 205 NZ LYS A 110 34.907 10.613 11.584 1.00 89.23 N ANISOU 205 NZ LYS A 110 8373 9233 16296 4203 -256 1374 N ATOM 206 N ASP A 111 29.266 13.771 7.258 1.00 78.31 N ANISOU 206 N ASP A 111 9097 8294 12362 2856 937 -550 N ATOM 207 CA ASP A 111 29.959 14.269 6.089 1.00 82.24 C ANISOU 207 CA ASP A 111 9434 8856 12956 3003 1388 -701 C ATOM 208 C ASP A 111 28.956 14.761 5.064 1.00 75.06 C ANISOU 208 C ASP A 111 8938 8012 11570 2737 1582 -993 C ATOM 209 O ASP A 111 29.082 15.851 4.506 1.00 68.98 O ANISOU 209 O ASP A 111 8021 7503 10687 2602 1716 -1057 O ATOM 210 CB ASP A 111 30.831 13.146 5.516 1.00 91.07 C ANISOU 210 CB ASP A 111 10532 9613 14459 3457 1769 -728 C ATOM 211 CG ASP A 111 31.499 13.525 4.223 1.00100.56 C ANISOU 211 CG ASP A 111 11649 10886 15672 3579 2285 -912 C ATOM 212 OD1 ASP A 111 30.801 13.554 3.186 1.00102.66 O ANISOU 212 OD1 ASP A 111 12374 11103 15529 3416 2529 -1203 O ATOM 213 OD2 ASP A 111 32.727 13.769 4.238 1.00106.32 O ANISOU 213 OD2 ASP A 111 11892 11790 16714 3738 2350 -742 O ATOM 214 N ALA A 112 27.966 13.922 4.806 1.00 73.15 N ANISOU 214 N ALA A 112 9219 7516 11060 2647 1574 -1145 N ATOM 215 CA ALA A 112 26.815 14.329 4.036 1.00 55.98 C ANISOU 215 CA ALA A 112 7444 5415 8413 2323 1617 -1355 C ATOM 216 C ALA A 112 26.091 15.365 4.863 1.00 51.50 C ANISOU 216 C ALA A 112 6726 5181 7660 2004 1238 -1233 C ATOM 217 O ALA A 112 25.602 16.376 4.346 1.00 53.70 O ANISOU 217 O ALA A 112 7024 5684 7696 1778 1269 -1314 O ATOM 218 CB ALA A 112 25.920 13.144 3.731 1.00 57.63 C ANISOU 218 CB ALA A 112 8218 5275 8404 2257 1615 -1493 C ATOM 219 N VAL A 113 26.032 15.095 6.163 1.00 54.17 N ANISOU 219 N VAL A 113 6932 5534 8115 1992 887 -1031 N ATOM 220 CA VAL A 113 25.477 16.033 7.129 1.00 55.61 C ANISOU 220 CA VAL A 113 6968 6015 8148 1725 554 -917 C ATOM 221 C VAL A 113 26.099 17.416 6.961 1.00 54.84 C ANISOU 221 C VAL A 113 6513 6208 8116 1680 615 -906 C ATOM 222 O VAL A 113 25.385 18.420 6.904 1.00 45.87 O ANISOU 222 O VAL A 113 5412 5274 6743 1436 548 -964 O ATOM 223 CB VAL A 113 25.695 15.538 8.573 1.00 58.77 C ANISOU 223 CB VAL A 113 7237 6395 8698 1752 204 -677 C ATOM 224 CG1 VAL A 113 25.276 16.604 9.577 1.00 45.66 C ANISOU 224 CG1 VAL A 113 5436 5047 6866 1483 -83 -589 C ATOM 225 CG2 VAL A 113 24.933 14.232 8.797 1.00 62.65 C ANISOU 225 CG2 VAL A 113 8114 6601 9090 1733 108 -664 C ATOM 226 N ASP A 114 27.426 17.456 6.855 1.00 59.89 N ANISOU 226 N ASP A 114 6798 6852 9105 1920 749 -816 N ATOM 227 CA ASP A 114 28.139 18.718 6.664 1.00 61.03 C ANISOU 227 CA ASP A 114 6583 7258 9349 1863 808 -777 C ATOM 228 C ASP A 114 27.686 19.406 5.365 1.00 62.01 C ANISOU 228 C ASP A 114 6888 7447 9224 1738 1101 -981 C ATOM 229 O ASP A 114 27.333 20.587 5.376 1.00 59.15 O ANISOU 229 O ASP A 114 6470 7294 8711 1509 1007 -991 O ATOM 230 CB ASP A 114 29.660 18.492 6.664 1.00 64.50 C ANISOU 230 CB ASP A 114 6577 7682 10248 2154 937 -616 C ATOM 231 CG ASP A 114 30.222 18.156 8.061 1.00 68.92 C ANISOU 231 CG ASP A 114 6860 8258 11069 2206 542 -333 C ATOM 232 OD1 ASP A 114 29.500 18.363 9.056 1.00 68.28 O ANISOU 232 OD1 ASP A 114 6923 8257 10761 1967 181 -282 O ATOM 233 OD2 ASP A 114 31.393 17.694 8.167 1.00 58.69 O ANISOU 233 OD2 ASP A 114 5193 6901 10205 2480 595 -146 O ATOM 234 N SER A 115 27.664 18.661 4.262 1.00 60.88 N ANISOU 234 N SER A 115 7003 7107 9023 1875 1444 -1140 N ATOM 235 CA SER A 115 27.239 19.211 2.975 1.00 60.51 C ANISOU 235 CA SER A 115 7182 7114 8694 1728 1707 -1316 C ATOM 236 C SER A 115 25.844 19.793 3.076 1.00 50.63 C ANISOU 236 C SER A 115 6184 5965 7090 1401 1457 -1354 C ATOM 237 O SER A 115 25.604 20.907 2.625 1.00 51.08 O ANISOU 237 O SER A 115 6192 6203 7011 1217 1469 -1364 O ATOM 238 CB SER A 115 27.271 18.149 1.874 1.00 69.81 C ANISOU 238 CB SER A 115 8723 8020 9780 1881 2080 -1507 C ATOM 239 OG SER A 115 28.496 17.443 1.880 1.00 78.79 O ANISOU 239 OG SER A 115 9627 9009 11300 2246 2336 -1467 O ATOM 240 N ALA A 116 24.936 19.038 3.684 1.00 44.77 N ANISOU 240 N ALA A 116 5685 5099 6226 1335 1232 -1351 N ATOM 241 CA ALA A 116 23.570 19.503 3.875 1.00 40.59 C ANISOU 241 CA ALA A 116 5339 4670 5412 1049 1003 -1354 C ATOM 242 C ALA A 116 23.551 20.887 4.485 1.00 42.56 C ANISOU 242 C ALA A 116 5298 5176 5697 923 839 -1264 C ATOM 243 O ALA A 116 23.020 21.830 3.885 1.00 44.16 O ANISOU 243 O ALA A 116 5535 5496 5746 754 864 -1295 O ATOM 244 CB ALA A 116 22.804 18.551 4.733 1.00 40.19 C ANISOU 244 CB ALA A 116 5473 4494 5303 1007 772 -1304 C ATOM 245 N VAL A 117 24.145 21.017 5.667 1.00 48.92 N ANISOU 245 N VAL A 117 5840 6047 6700 993 658 -1145 N ATOM 246 CA VAL A 117 24.191 22.307 6.357 1.00 46.83 C ANISOU 246 CA VAL A 117 5351 5985 6456 858 492 -1082 C ATOM 247 C VAL A 117 24.848 23.342 5.469 1.00 39.65 C ANISOU 247 C VAL A 117 4271 5178 5617 837 676 -1104 C ATOM 248 O VAL A 117 24.305 24.429 5.285 1.00 41.11 O ANISOU 248 O VAL A 117 4470 5462 5686 667 637 -1124 O ATOM 249 CB VAL A 117 24.961 22.230 7.695 1.00 47.67 C ANISOU 249 CB VAL A 117 5221 6139 6753 911 261 -943 C ATOM 250 CG1 VAL A 117 25.063 23.615 8.357 1.00 42.27 C ANISOU 250 CG1 VAL A 117 4370 5635 6056 737 101 -913 C ATOM 251 CG2 VAL A 117 24.301 21.258 8.620 1.00 44.32 C ANISOU 251 CG2 VAL A 117 4981 5627 6232 897 68 -893 C ATOM 252 N GLU A 118 26.007 22.990 4.911 1.00 47.62 N ANISOU 252 N GLU A 118 5112 6150 6831 1017 893 -1085 N ATOM 253 CA GLU A 118 26.745 23.905 4.033 1.00 56.94 C ANISOU 253 CA GLU A 118 6106 7440 8086 989 1106 -1080 C ATOM 254 C GLU A 118 25.856 24.470 2.922 1.00 47.84 C ANISOU 254 C GLU A 118 5223 6307 6648 813 1229 -1179 C ATOM 255 O GLU A 118 25.749 25.688 2.769 1.00 40.68 O ANISOU 255 O GLU A 118 4230 5517 5707 647 1176 -1140 O ATOM 256 CB GLU A 118 27.971 23.212 3.433 1.00 69.74 C ANISOU 256 CB GLU A 118 7548 9001 9949 1238 1415 -1062 C ATOM 257 CG GLU A 118 29.071 22.902 4.450 1.00 87.50 C ANISOU 257 CG GLU A 118 9404 11272 12568 1405 1272 -885 C ATOM 258 CD GLU A 118 30.250 22.141 3.850 1.00109.96 C ANISOU 258 CD GLU A 118 12025 14036 15717 1709 1617 -848 C ATOM 259 OE1 GLU A 118 30.161 21.715 2.675 1.00120.09 O ANISOU 259 OE1 GLU A 118 13538 15213 16876 1800 1999 -1006 O ATOM 260 OE2 GLU A 118 31.265 21.960 4.559 1.00115.44 O ANISOU 260 OE2 GLU A 118 12317 14769 16777 1855 1510 -653 O ATOM 261 N LYS A 119 25.189 23.596 2.180 1.00 39.71 N ANISOU 261 N LYS A 119 4534 5144 5410 825 1357 -1288 N ATOM 262 CA LYS A 119 24.288 24.050 1.134 1.00 47.15 C ANISOU 262 CA LYS A 119 5747 6108 6060 622 1412 -1344 C ATOM 263 C LYS A 119 23.163 24.927 1.693 1.00 49.90 C ANISOU 263 C LYS A 119 6104 6541 6314 429 1118 -1280 C ATOM 264 O LYS A 119 22.790 25.940 1.090 1.00 44.12 O ANISOU 264 O LYS A 119 5387 5889 5490 270 1110 -1239 O ATOM 265 CB LYS A 119 23.703 22.859 0.363 1.00 57.86 C ANISOU 265 CB LYS A 119 7513 7290 7182 622 1535 -1468 C ATOM 266 CG LYS A 119 24.708 22.140 -0.530 1.00 66.15 C ANISOU 266 CG LYS A 119 8644 8227 8263 800 1928 -1577 C ATOM 267 CD LYS A 119 25.678 23.145 -1.138 1.00 73.08 C ANISOU 267 CD LYS A 119 9261 9271 9234 797 2158 -1526 C ATOM 268 CE LYS A 119 25.767 23.044 -2.645 1.00 77.61 C ANISOU 268 CE LYS A 119 10143 9817 9527 713 2510 -1642 C ATOM 269 NZ LYS A 119 26.499 24.237 -3.144 1.00 77.81 N ANISOU 269 NZ LYS A 119 9906 10045 9615 629 2663 -1541 N ATOM 270 N ALA A 120 22.633 24.559 2.851 1.00 47.12 N ANISOU 270 N ALA A 120 5739 6166 5999 449 894 -1258 N ATOM 271 CA ALA A 120 21.512 25.309 3.402 1.00 32.43 C ANISOU 271 CA ALA A 120 3888 4373 4059 300 681 -1213 C ATOM 272 C ALA A 120 21.939 26.699 3.843 1.00 38.42 C ANISOU 272 C ALA A 120 4409 5232 4956 255 621 -1165 C ATOM 273 O ALA A 120 21.163 27.635 3.755 1.00 44.40 O ANISOU 273 O ALA A 120 5184 6021 5664 139 548 -1135 O ATOM 274 CB ALA A 120 20.895 24.568 4.536 1.00 31.63 C ANISOU 274 CB ALA A 120 3840 4237 3941 321 507 -1202 C ATOM 275 N LEU A 121 23.167 26.843 4.328 1.00 40.31 N ANISOU 275 N LEU A 121 4424 5504 5388 341 636 -1142 N ATOM 276 CA LEU A 121 23.681 28.173 4.632 1.00 40.91 C ANISOU 276 CA LEU A 121 4304 5652 5586 252 572 -1097 C ATOM 277 C LEU A 121 23.913 28.944 3.337 1.00 50.80 C ANISOU 277 C LEU A 121 5550 6931 6818 168 742 -1067 C ATOM 278 O LEU A 121 23.811 30.169 3.280 1.00 51.17 O ANISOU 278 O LEU A 121 5548 6996 6900 42 683 -1025 O ATOM 279 CB LEU A 121 24.981 28.089 5.412 1.00 35.22 C ANISOU 279 CB LEU A 121 3323 4976 5081 319 509 -1040 C ATOM 280 CG LEU A 121 24.920 27.553 6.836 1.00 37.27 C ANISOU 280 CG LEU A 121 3575 5229 5357 349 282 -1026 C ATOM 281 CD1 LEU A 121 26.326 27.219 7.248 1.00 36.79 C ANISOU 281 CD1 LEU A 121 3232 5211 5537 434 235 -915 C ATOM 282 CD2 LEU A 121 24.299 28.585 7.787 1.00 33.35 C ANISOU 282 CD2 LEU A 121 3144 4753 4773 190 95 -1063 C ATOM 283 N LYS A 122 24.222 28.199 2.286 1.00 46.36 N ANISOU 283 N LYS A 122 5074 6354 6186 229 966 -1090 N ATOM 284 CA LYS A 122 24.664 28.797 1.052 1.00 41.05 C ANISOU 284 CA LYS A 122 4399 5729 5468 143 1170 -1052 C ATOM 285 C LYS A 122 23.488 29.425 0.290 1.00 43.45 C ANISOU 285 C LYS A 122 4932 6019 5559 -35 1104 -1020 C ATOM 286 O LYS A 122 23.659 30.424 -0.400 1.00 41.67 O ANISOU 286 O LYS A 122 4677 5834 5323 -170 1148 -935 O ATOM 287 CB LYS A 122 25.397 27.734 0.221 1.00 41.10 C ANISOU 287 CB LYS A 122 4460 5713 5444 277 1478 -1113 C ATOM 288 CG LYS A 122 25.919 28.196 -1.118 1.00 51.72 C ANISOU 288 CG LYS A 122 5839 7123 6690 184 1761 -1087 C ATOM 289 CD LYS A 122 27.420 27.985 -1.223 1.00 74.33 C ANISOU 289 CD LYS A 122 8398 10049 9793 337 2037 -1058 C ATOM 290 CE LYS A 122 28.170 28.818 -0.183 1.00 86.34 C ANISOU 290 CE LYS A 122 9513 11661 11631 317 1835 -924 C ATOM 291 NZ LYS A 122 29.576 29.116 -0.603 1.00 95.37 N ANISOU 291 NZ LYS A 122 10309 12927 13001 348 2094 -817 N ATOM 292 N VAL A 123 22.287 28.872 0.436 1.00 42.92 N ANISOU 292 N VAL A 123 5069 5896 5344 -52 973 -1052 N ATOM 293 CA VAL A 123 21.153 29.420 -0.303 1.00 36.99 C ANISOU 293 CA VAL A 123 4487 5141 4428 -221 877 -971 C ATOM 294 C VAL A 123 20.881 30.831 0.171 1.00 45.26 C ANISOU 294 C VAL A 123 5375 6189 5633 -280 728 -878 C ATOM 295 O VAL A 123 20.498 31.702 -0.621 1.00 46.08 O ANISOU 295 O VAL A 123 5527 6290 5693 -414 695 -759 O ATOM 296 CB VAL A 123 19.854 28.573 -0.161 1.00 41.80 C ANISOU 296 CB VAL A 123 5289 5706 4888 -251 733 -982 C ATOM 297 CG1 VAL A 123 20.056 27.144 -0.659 1.00 34.00 C ANISOU 297 CG1 VAL A 123 4533 4658 3728 -216 868 -1090 C ATOM 298 CG2 VAL A 123 19.352 28.566 1.261 1.00 42.46 C ANISOU 298 CG2 VAL A 123 5239 5780 5112 -162 571 -998 C ATOM 299 N TRP A 124 21.105 31.063 1.462 1.00 47.55 N ANISOU 299 N TRP A 124 5505 6464 6097 -188 635 -929 N ATOM 300 CA TRP A 124 20.869 32.375 2.052 1.00 43.28 C ANISOU 300 CA TRP A 124 4867 5876 5704 -232 515 -888 C ATOM 301 C TRP A 124 22.044 33.343 1.832 1.00 37.82 C ANISOU 301 C TRP A 124 4035 5189 5147 -309 568 -842 C ATOM 302 O TRP A 124 21.844 34.532 1.616 1.00 44.25 O ANISOU 302 O TRP A 124 4844 5931 6037 -405 510 -763 O ATOM 303 CB TRP A 124 20.558 32.222 3.535 1.00 37.65 C ANISOU 303 CB TRP A 124 4111 5137 5056 -145 403 -981 C ATOM 304 CG TRP A 124 19.287 31.464 3.769 1.00 36.44 C ANISOU 304 CG TRP A 124 4068 4987 4792 -105 351 -989 C ATOM 305 CD1 TRP A 124 19.160 30.251 4.369 1.00 38.06 C ANISOU 305 CD1 TRP A 124 4322 5222 4917 -39 335 -1048 C ATOM 306 CD2 TRP A 124 17.965 31.867 3.399 1.00 32.14 C ANISOU 306 CD2 TRP A 124 3570 4414 4229 -144 295 -897 C ATOM 307 NE1 TRP A 124 17.845 29.868 4.390 1.00 33.35 N ANISOU 307 NE1 TRP A 124 3806 4629 4237 -59 281 -1007 N ATOM 308 CE2 TRP A 124 17.089 30.845 3.805 1.00 34.23 C ANISOU 308 CE2 TRP A 124 3894 4716 4398 -116 255 -908 C ATOM 309 CE3 TRP A 124 17.436 32.997 2.765 1.00 35.09 C ANISOU 309 CE3 TRP A 124 3921 4727 4686 -201 261 -776 C ATOM 310 CZ2 TRP A 124 15.709 30.911 3.592 1.00 41.51 C ANISOU 310 CZ2 TRP A 124 4815 5645 5313 -152 185 -794 C ATOM 311 CZ3 TRP A 124 16.068 33.062 2.552 1.00 35.64 C ANISOU 311 CZ3 TRP A 124 3988 4787 4765 -209 184 -657 C ATOM 312 CH2 TRP A 124 15.218 32.027 2.965 1.00 37.74 C ANISOU 312 CH2 TRP A 124 4276 5119 4945 -188 149 -663 C ATOM 313 N GLU A 125 23.262 32.827 1.852 1.00 33.98 N ANISOU 313 N GLU A 125 3419 4777 4713 -268 678 -867 N ATOM 314 CA GLU A 125 24.432 33.655 1.633 1.00 38.92 C ANISOU 314 CA GLU A 125 3864 5438 5485 -365 733 -792 C ATOM 315 C GLU A 125 24.512 34.190 0.191 1.00 46.84 C ANISOU 315 C GLU A 125 4934 6467 6396 -500 881 -675 C ATOM 316 O GLU A 125 25.083 35.251 -0.055 1.00 52.69 O ANISOU 316 O GLU A 125 5576 7200 7244 -643 876 -571 O ATOM 317 CB GLU A 125 25.693 32.859 1.975 1.00 41.85 C ANISOU 317 CB GLU A 125 4021 5905 5977 -266 828 -807 C ATOM 318 CG GLU A 125 26.971 33.624 1.754 1.00 60.00 C ANISOU 318 CG GLU A 125 6065 8276 8457 -380 890 -694 C ATOM 319 CD GLU A 125 27.951 32.866 0.904 1.00 80.85 C ANISOU 319 CD GLU A 125 8555 11030 11132 -292 1190 -652 C ATOM 320 OE1 GLU A 125 28.185 31.679 1.216 1.00 87.46 O ANISOU 320 OE1 GLU A 125 9348 11880 12003 -94 1260 -716 O ATOM 321 OE2 GLU A 125 28.475 33.453 -0.073 1.00 88.46 O ANISOU 321 OE2 GLU A 125 9458 12060 12093 -417 1373 -552 O ATOM 322 N GLU A 126 23.937 33.455 -0.758 1.00 47.10 N ANISOU 322 N GLU A 126 5165 6524 6207 -489 995 -682 N ATOM 323 CA GLU A 126 24.063 33.792 -2.178 1.00 38.88 C ANISOU 323 CA GLU A 126 4240 5529 5003 -644 1150 -572 C ATOM 324 C GLU A 126 23.265 35.014 -2.584 1.00 46.19 C ANISOU 324 C GLU A 126 5256 6374 5918 -811 976 -416 C ATOM 325 O GLU A 126 23.540 35.620 -3.616 1.00 46.24 O ANISOU 325 O GLU A 126 5321 6414 5834 -984 1059 -275 O ATOM 326 CB GLU A 126 23.613 32.636 -3.051 1.00 45.64 C ANISOU 326 CB GLU A 126 5355 6413 5572 -627 1292 -638 C ATOM 327 CG GLU A 126 24.640 31.576 -3.300 1.00 63.22 C ANISOU 327 CG GLU A 126 7548 8700 7774 -497 1595 -754 C ATOM 328 CD GLU A 126 24.029 30.395 -4.007 1.00 79.68 C ANISOU 328 CD GLU A 126 9971 10745 9560 -485 1700 -862 C ATOM 329 OE1 GLU A 126 22.778 30.335 -4.055 1.00 76.27 O ANISOU 329 OE1 GLU A 126 9741 10259 8979 -577 1470 -835 O ATOM 330 OE2 GLU A 126 24.793 29.542 -4.510 1.00 90.40 O ANISOU 330 OE2 GLU A 126 11389 12113 10845 -388 2013 -969 O ATOM 331 N VAL A 127 22.268 35.368 -1.782 1.00 47.98 N ANISOU 331 N VAL A 127 5496 6490 6244 -753 750 -427 N ATOM 332 CA VAL A 127 21.395 36.488 -2.114 1.00 47.02 C ANISOU 332 CA VAL A 127 5441 6252 6173 -855 582 -264 C ATOM 333 C VAL A 127 21.517 37.666 -1.139 1.00 40.12 C ANISOU 333 C VAL A 127 4446 5223 5574 -835 459 -271 C ATOM 334 O VAL A 127 20.774 38.636 -1.237 1.00 40.46 O ANISOU 334 O VAL A 127 4534 5114 5726 -867 328 -152 O ATOM 335 CB VAL A 127 19.949 36.020 -2.149 1.00 50.16 C ANISOU 335 CB VAL A 127 5958 6622 6480 -803 443 -236 C ATOM 336 CG1 VAL A 127 19.751 35.021 -3.293 1.00 37.35 C ANISOU 336 CG1 VAL A 127 4536 5114 4542 -905 521 -205 C ATOM 337 CG2 VAL A 127 19.573 35.414 -0.791 1.00 46.56 C ANISOU 337 CG2 VAL A 127 5425 6146 6121 -614 398 -411 C ATOM 338 N THR A 128 22.455 37.574 -0.197 1.00 38.77 N ANISOU 338 N THR A 128 4137 5073 5519 -788 491 -404 N ATOM 339 CA THR A 128 22.621 38.588 0.838 1.00 39.29 C ANISOU 339 CA THR A 128 4152 4980 5795 -803 365 -455 C ATOM 340 C THR A 128 24.086 38.921 1.059 1.00 41.86 C ANISOU 340 C THR A 128 4317 5360 6227 -930 395 -448 C ATOM 341 O THR A 128 24.958 38.284 0.498 1.00 41.38 O ANISOU 341 O THR A 128 4137 5475 6111 -955 545 -408 O ATOM 342 CB THR A 128 22.018 38.137 2.195 1.00 47.41 C ANISOU 342 CB THR A 128 5204 5965 6844 -639 289 -641 C ATOM 343 OG1 THR A 128 22.748 37.014 2.703 1.00 54.54 O ANISOU 343 OG1 THR A 128 6013 7027 7682 -576 338 -743 O ATOM 344 CG2 THR A 128 20.587 37.759 2.037 1.00 36.50 C ANISOU 344 CG2 THR A 128 3920 4559 5390 -522 269 -623 C ATOM 345 N PRO A 129 24.358 39.950 1.867 1.00 47.08 N ANISOU 345 N PRO A 129 4977 5859 7053 -1020 258 -480 N ATOM 346 CA PRO A 129 25.732 40.177 2.322 1.00 50.45 C ANISOU 346 CA PRO A 129 5226 6350 7594 -1167 222 -470 C ATOM 347 C PRO A 129 26.195 39.234 3.436 1.00 51.21 C ANISOU 347 C PRO A 129 5210 6565 7681 -1070 169 -608 C ATOM 348 O PRO A 129 27.343 39.336 3.866 1.00 56.44 O ANISOU 348 O PRO A 129 5685 7304 8456 -1197 99 -567 O ATOM 349 CB PRO A 129 25.695 41.619 2.836 1.00 50.41 C ANISOU 349 CB PRO A 129 5340 6079 7735 -1328 55 -472 C ATOM 350 CG PRO A 129 24.254 41.940 3.027 1.00 49.86 C ANISOU 350 CG PRO A 129 5494 5804 7649 -1171 27 -550 C ATOM 351 CD PRO A 129 23.533 41.163 1.991 1.00 52.01 C ANISOU 351 CD PRO A 129 5762 6212 7786 -1047 148 -454 C ATOM 352 N LEU A 130 25.333 38.335 3.894 1.00 54.31 N ANISOU 352 N LEU A 130 5703 6981 7953 -872 180 -734 N ATOM 353 CA LEU A 130 25.695 37.439 4.997 1.00 51.91 C ANISOU 353 CA LEU A 130 5326 6771 7627 -791 101 -838 C ATOM 354 C LEU A 130 26.927 36.593 4.678 1.00 55.09 C ANISOU 354 C LEU A 130 5456 7374 8101 -773 186 -742 C ATOM 355 O LEU A 130 27.210 36.310 3.517 1.00 67.00 O ANISOU 355 O LEU A 130 6884 8972 9601 -747 390 -649 O ATOM 356 CB LEU A 130 24.518 36.529 5.353 1.00 38.25 C ANISOU 356 CB LEU A 130 3747 5043 5745 -596 129 -950 C ATOM 357 CG LEU A 130 23.402 37.212 6.130 1.00 41.34 C ANISOU 357 CG LEU A 130 4347 5260 6103 -575 53 -1068 C ATOM 358 CD1 LEU A 130 22.339 36.229 6.561 1.00 46.90 C ANISOU 358 CD1 LEU A 130 5142 6009 6669 -407 89 -1149 C ATOM 359 CD2 LEU A 130 24.002 37.880 7.334 1.00 38.66 C ANISOU 359 CD2 LEU A 130 4051 4836 5803 -711 -107 -1162 C ATOM 360 N THR A 131 27.667 36.212 5.711 1.00 49.33 N ANISOU 360 N THR A 131 4586 6710 7444 -788 37 -753 N ATOM 361 CA THR A 131 28.789 35.306 5.543 1.00 52.44 C ANISOU 361 CA THR A 131 4677 7281 7968 -713 112 -642 C ATOM 362 C THR A 131 28.857 34.365 6.724 1.00 64.37 C ANISOU 362 C THR A 131 6164 8830 9464 -610 -57 -688 C ATOM 363 O THR A 131 28.385 34.697 7.808 1.00 70.24 O ANISOU 363 O THR A 131 7089 9492 10106 -694 -272 -785 O ATOM 364 CB THR A 131 30.101 36.055 5.422 1.00 56.65 C ANISOU 364 CB THR A 131 4917 7891 8719 -921 59 -474 C ATOM 365 OG1 THR A 131 29.861 37.298 4.759 1.00 60.82 O ANISOU 365 OG1 THR A 131 5564 8311 9232 -1107 92 -444 O ATOM 366 CG2 THR A 131 31.078 35.241 4.604 1.00 65.02 C ANISOU 366 CG2 THR A 131 5645 9130 9930 -793 311 -335 C ATOM 367 N PHE A 132 29.456 33.197 6.517 1.00 62.77 N ANISOU 367 N PHE A 132 5755 8737 9359 -427 54 -614 N ATOM 368 CA PHE A 132 29.484 32.166 7.545 1.00 46.99 C ANISOU 368 CA PHE A 132 3743 6758 7353 -308 -107 -620 C ATOM 369 C PHE A 132 30.857 31.545 7.752 1.00 45.42 C ANISOU 369 C PHE A 132 3141 6681 7434 -242 -154 -426 C ATOM 370 O PHE A 132 31.443 31.007 6.820 1.00 60.53 O ANISOU 370 O PHE A 132 4842 8651 9505 -76 120 -351 O ATOM 371 CB PHE A 132 28.477 31.076 7.192 1.00 40.15 C ANISOU 371 CB PHE A 132 3104 5834 6319 -87 57 -732 C ATOM 372 CG PHE A 132 27.059 31.566 7.132 1.00 42.76 C ANISOU 372 CG PHE A 132 3770 6063 6412 -139 65 -878 C ATOM 373 CD1 PHE A 132 26.296 31.679 8.289 1.00 41.03 C ANISOU 373 CD1 PHE A 132 3747 5794 6051 -194 -126 -969 C ATOM 374 CD2 PHE A 132 26.480 31.924 5.917 1.00 47.96 C ANISOU 374 CD2 PHE A 132 4542 6686 6993 -138 270 -905 C ATOM 375 CE1 PHE A 132 24.966 32.136 8.235 1.00 41.27 C ANISOU 375 CE1 PHE A 132 4030 5734 5915 -208 -81 -1084 C ATOM 376 CE2 PHE A 132 25.155 32.376 5.858 1.00 39.95 C ANISOU 376 CE2 PHE A 132 3780 5582 5816 -171 254 -990 C ATOM 377 CZ PHE A 132 24.402 32.485 7.022 1.00 34.80 C ANISOU 377 CZ PHE A 132 3269 4877 5076 -188 94 -1079 C ATOM 378 N SER A 133 31.370 31.626 8.977 1.00 51.17 N ANISOU 378 N SER A 133 3767 7448 8225 -375 -498 -335 N ATOM 379 CA SER A 133 32.555 30.856 9.387 1.00 50.17 C ANISOU 379 CA SER A 133 3244 7433 8386 -288 -620 -107 C ATOM 380 C SER A 133 32.103 29.661 10.213 1.00 49.47 C ANISOU 380 C SER A 133 3298 7294 8204 -121 -756 -122 C ATOM 381 O SER A 133 31.127 29.759 10.952 1.00 54.26 O ANISOU 381 O SER A 133 4268 7829 8518 -214 -904 -269 O ATOM 382 CB SER A 133 33.531 31.712 10.196 1.00 54.64 C ANISOU 382 CB SER A 133 3573 8093 9096 -601 -982 71 C ATOM 383 OG SER A 133 34.500 32.331 9.367 1.00 66.02 O ANISOU 383 OG SER A 133 4648 9636 10803 -684 -839 227 O ATOM 384 N ARG A 134 32.788 28.531 10.083 1.00 51.52 N ANISOU 384 N ARG A 134 3280 7577 8720 134 -684 36 N ATOM 385 CA ARG A 134 32.419 27.342 10.852 1.00 51.33 C ANISOU 385 CA ARG A 134 3389 7478 8636 291 -830 61 C ATOM 386 C ARG A 134 33.290 27.175 12.103 1.00 60.92 C ANISOU 386 C ARG A 134 4357 8779 10010 166 -1277 326 C ATOM 387 O ARG A 134 34.499 27.406 12.056 1.00 58.11 O ANISOU 387 O ARG A 134 3549 8539 9993 132 -1369 564 O ATOM 388 CB ARG A 134 32.518 26.084 9.992 1.00 51.91 C ANISOU 388 CB ARG A 134 3388 7454 8883 668 -491 64 C ATOM 389 CG ARG A 134 31.966 24.870 10.694 1.00 56.13 C ANISOU 389 CG ARG A 134 4138 7863 9328 812 -628 72 C ATOM 390 CD ARG A 134 32.125 23.589 9.915 1.00 64.42 C ANISOU 390 CD ARG A 134 5151 8758 10570 1182 -312 71 C ATOM 391 NE ARG A 134 31.680 22.448 10.716 1.00 71.45 N ANISOU 391 NE ARG A 134 6237 9508 11404 1284 -508 127 N ATOM 392 CZ ARG A 134 31.709 21.183 10.307 1.00 73.76 C ANISOU 392 CZ ARG A 134 6582 9598 11846 1593 -313 132 C ATOM 393 NH1 ARG A 134 32.165 20.884 9.096 1.00 63.15 N ANISOU 393 NH1 ARG A 134 5125 8172 10697 1844 119 56 N ATOM 394 NH2 ARG A 134 31.284 20.214 11.113 1.00 80.48 N ANISOU 394 NH2 ARG A 134 7628 10313 12637 1640 -537 210 N ATOM 395 N LEU A 135 32.673 26.774 13.217 1.00 58.39 N ANISOU 395 N LEU A 135 4327 8419 9441 75 -1564 308 N ATOM 396 CA LEU A 135 33.418 26.487 14.440 1.00 57.36 C ANISOU 396 CA LEU A 135 4022 8365 9405 -64 -2029 582 C ATOM 397 C LEU A 135 33.286 25.028 14.855 1.00 58.20 C ANISOU 397 C LEU A 135 4160 8377 9578 184 -2100 714 C ATOM 398 O LEU A 135 32.223 24.439 14.709 1.00 60.68 O ANISOU 398 O LEU A 135 4833 8567 9658 307 -1917 526 O ATOM 399 CB LEU A 135 32.947 27.391 15.567 1.00 56.95 C ANISOU 399 CB LEU A 135 4318 8357 8961 -471 -2367 483 C ATOM 400 CG LEU A 135 33.179 28.870 15.286 1.00 59.11 C ANISOU 400 CG LEU A 135 4580 8680 9200 -746 -2360 379 C ATOM 401 CD1 LEU A 135 32.737 29.741 16.446 1.00 58.18 C ANISOU 401 CD1 LEU A 135 4864 8557 8686 -1141 -2672 250 C ATOM 402 CD2 LEU A 135 34.637 29.091 14.973 1.00 60.82 C ANISOU 402 CD2 LEU A 135 4231 9023 9853 -786 -2476 679 C ATOM 403 N TYR A 136 34.370 24.449 15.369 1.00 62.47 N ANISOU 403 N TYR A 136 4308 8967 10461 246 -2386 1067 N ATOM 404 CA TYR A 136 34.364 23.045 15.789 1.00 69.88 C ANISOU 404 CA TYR A 136 5245 9780 11525 493 -2490 1248 C ATOM 405 C TYR A 136 34.476 22.892 17.307 1.00 75.92 C ANISOU 405 C TYR A 136 6117 10618 12113 207 -3067 1484 C ATOM 406 O TYR A 136 34.485 21.777 17.839 1.00 82.83 O ANISOU 406 O TYR A 136 7012 11392 13067 351 -3246 1688 O ATOM 407 CB TYR A 136 35.505 22.268 15.127 1.00 67.91 C ANISOU 407 CB TYR A 136 4447 9479 11875 879 -2329 1509 C ATOM 408 CG TYR A 136 35.492 22.270 13.618 1.00 69.81 C ANISOU 408 CG TYR A 136 4602 9644 12279 1173 -1728 1292 C ATOM 409 CD1 TYR A 136 34.860 21.259 12.906 1.00 69.86 C ANISOU 409 CD1 TYR A 136 4861 9419 12262 1503 -1355 1111 C ATOM 410 CD2 TYR A 136 36.140 23.271 12.902 1.00 72.49 C ANISOU 410 CD2 TYR A 136 4629 10137 12776 1088 -1545 1281 C ATOM 411 CE1 TYR A 136 34.860 21.254 11.522 1.00 73.14 C ANISOU 411 CE1 TYR A 136 5256 9767 12768 1732 -811 904 C ATOM 412 CE2 TYR A 136 36.147 23.274 11.519 1.00 73.83 C ANISOU 412 CE2 TYR A 136 4749 10254 13050 1325 -989 1096 C ATOM 413 CZ TYR A 136 35.508 22.264 10.835 1.00 78.94 C ANISOU 413 CZ TYR A 136 5682 10677 13634 1644 -623 901 C ATOM 414 OH TYR A 136 35.517 22.272 9.460 1.00 88.50 O ANISOU 414 OH TYR A 136 6901 11837 14887 1839 -77 708 O ATOM 415 N GLU A 137 34.580 24.015 18.000 1.00 75.02 N ANISOU 415 N GLU A 137 6099 10660 11745 -216 -3367 1464 N ATOM 416 CA GLU A 137 34.599 24.011 19.453 1.00 78.37 C ANISOU 416 CA GLU A 137 6731 11165 11880 -568 -3908 1639 C ATOM 417 C GLU A 137 34.203 25.391 19.951 1.00 83.42 C ANISOU 417 C GLU A 137 7720 11900 12076 -1018 -4024 1394 C ATOM 418 O GLU A 137 34.546 26.406 19.344 1.00 87.02 O ANISOU 418 O GLU A 137 8023 12403 12639 -1110 -3892 1286 O ATOM 419 CB GLU A 137 35.974 23.614 19.981 1.00 79.30 C ANISOU 419 CB GLU A 137 6491 11330 12310 -565 -4174 2036 C ATOM 420 CG GLU A 137 37.067 24.618 19.679 1.00 87.96 C ANISOU 420 CG GLU A 137 7257 12545 13617 -715 -4167 2106 C ATOM 421 CD GLU A 137 38.441 24.127 20.091 1.00103.59 C ANISOU 421 CD GLU A 137 8846 14557 15956 -668 -4383 2512 C ATOM 422 OE1 GLU A 137 38.549 22.960 20.532 1.00114.03 O ANISOU 422 OE1 GLU A 137 10134 15789 17404 -477 -4508 2736 O ATOM 423 OE2 GLU A 137 39.411 24.909 19.973 1.00104.86 O ANISOU 423 OE2 GLU A 137 8732 14824 16285 -830 -4437 2623 O ATOM 424 N GLY A 138 33.455 25.426 21.045 1.00 74.01 N ANISOU 424 N GLY A 138 7025 10717 10379 -1296 -4242 1299 N ATOM 425 CA GLY A 138 32.986 26.686 21.582 1.00 74.58 C ANISOU 425 CA GLY A 138 7524 10820 9992 -1681 -4266 1011 C ATOM 426 C GLY A 138 31.571 27.008 21.140 1.00 76.37 C ANISOU 426 C GLY A 138 8161 10946 9911 -1585 -3819 589 C ATOM 427 O GLY A 138 30.895 26.173 20.534 1.00 76.62 O ANISOU 427 O GLY A 138 8207 10890 10016 -1251 -3497 521 O ATOM 428 N GLU A 139 31.130 28.228 21.446 1.00 76.61 N ANISOU 428 N GLU A 139 8535 10964 9608 -1872 -3778 307 N ATOM 429 CA GLU A 139 29.772 28.673 21.156 1.00 64.64 C ANISOU 429 CA GLU A 139 7410 9345 7806 -1790 -3350 -81 C ATOM 430 C GLU A 139 29.718 29.499 19.880 1.00 60.47 C ANISOU 430 C GLU A 139 6708 8738 7529 -1632 -3000 -256 C ATOM 431 O GLU A 139 30.405 30.513 19.754 1.00 63.66 O ANISOU 431 O GLU A 139 7010 9145 8032 -1835 -3117 -260 O ATOM 432 CB GLU A 139 29.221 29.495 22.323 1.00 69.59 C ANISOU 432 CB GLU A 139 8571 9966 7905 -2169 -3467 -302 C ATOM 433 CG GLU A 139 28.882 28.698 23.564 1.00 82.29 C ANISOU 433 CG GLU A 139 10487 11649 9130 -2332 -3698 -201 C ATOM 434 CD GLU A 139 27.413 28.360 23.641 1.00 88.37 C ANISOU 434 CD GLU A 139 11599 12371 9608 -2181 -3301 -442 C ATOM 435 OE1 GLU A 139 26.646 28.882 22.798 1.00 78.46 O ANISOU 435 OE1 GLU A 139 10358 11019 8434 -1979 -2879 -700 O ATOM 436 OE2 GLU A 139 27.028 27.582 24.546 1.00 99.43 O ANISOU 436 OE2 GLU A 139 13237 13837 10705 -2283 -3425 -345 O ATOM 437 N ALA A 140 28.892 29.059 18.940 1.00 52.11 N ANISOU 437 N ALA A 140 5635 7608 6556 -1304 -2596 -382 N ATOM 438 CA ALA A 140 28.671 29.776 17.693 1.00 53.46 C ANISOU 438 CA ALA A 140 5698 7704 6910 -1159 -2254 -539 C ATOM 439 C ALA A 140 27.360 30.544 17.749 1.00 52.97 C ANISOU 439 C ALA A 140 6033 7541 6552 -1195 -1995 -857 C ATOM 440 O ALA A 140 26.535 30.326 18.641 1.00 62.83 O ANISOU 440 O ALA A 140 7612 8789 7473 -1268 -1999 -963 O ATOM 441 CB ALA A 140 28.667 28.812 16.523 1.00 53.99 C ANISOU 441 CB ALA A 140 5493 7752 7267 -795 -1989 -454 C ATOM 442 N ASP A 141 27.170 31.449 16.799 1.00 45.97 N ANISOU 442 N ASP A 141 5102 6571 5795 -1141 -1761 -987 N ATOM 443 CA ASP A 141 25.927 32.197 16.715 1.00 47.20 C ANISOU 443 CA ASP A 141 5566 6606 5761 -1119 -1497 -1251 C ATOM 444 C ASP A 141 24.808 31.229 16.456 1.00 48.92 C ANISOU 444 C ASP A 141 5850 6837 5899 -882 -1267 -1282 C ATOM 445 O ASP A 141 23.774 31.250 17.129 1.00 50.34 O ANISOU 445 O ASP A 141 6312 6996 5819 -905 -1165 -1423 O ATOM 446 CB ASP A 141 25.985 33.243 15.606 1.00 49.80 C ANISOU 446 CB ASP A 141 5791 6833 6298 -1085 -1316 -1315 C ATOM 447 CG ASP A 141 27.025 34.304 15.867 1.00 55.91 C ANISOU 447 CG ASP A 141 6527 7571 7145 -1366 -1546 -1287 C ATOM 448 OD1 ASP A 141 27.021 34.890 16.975 1.00 57.37 O ANISOU 448 OD1 ASP A 141 7009 7698 7089 -1620 -1726 -1405 O ATOM 449 OD2 ASP A 141 27.853 34.538 14.965 1.00 56.62 O ANISOU 449 OD2 ASP A 141 6306 7690 7517 -1357 -1541 -1146 O ATOM 450 N ILE A 142 25.045 30.362 15.477 1.00 46.32 N ANISOU 450 N ILE A 142 5263 6541 5797 -667 -1177 -1144 N ATOM 451 CA ILE A 142 24.090 29.330 15.090 1.00 46.52 C ANISOU 451 CA ILE A 142 5340 6563 5773 -468 -994 -1145 C ATOM 452 C ILE A 142 24.588 27.932 15.495 1.00 45.92 C ANISOU 452 C ILE A 142 5176 6541 5733 -399 -1162 -956 C ATOM 453 O ILE A 142 25.490 27.371 14.858 1.00 48.11 O ANISOU 453 O ILE A 142 5191 6818 6271 -267 -1184 -810 O ATOM 454 CB ILE A 142 23.836 29.385 13.574 1.00 41.41 C ANISOU 454 CB ILE A 142 4555 5865 5312 -291 -740 -1160 C ATOM 455 CG1 ILE A 142 23.445 30.798 13.166 1.00 41.52 C ANISOU 455 CG1 ILE A 142 4636 5806 5336 -361 -618 -1293 C ATOM 456 CG2 ILE A 142 22.777 28.387 13.151 1.00 40.22 C ANISOU 456 CG2 ILE A 142 4498 5699 5086 -143 -583 -1166 C ATOM 457 CD1 ILE A 142 23.493 31.004 11.678 1.00 43.69 C ANISOU 457 CD1 ILE A 142 4762 6049 5789 -252 -434 -1259 C ATOM 458 N MET A 143 24.007 27.377 16.557 1.00 40.68 N ANISOU 458 N MET A 143 4732 5910 4816 -481 -1262 -949 N ATOM 459 CA MET A 143 24.354 26.026 17.001 1.00 43.45 C ANISOU 459 CA MET A 143 5041 6278 5191 -423 -1439 -747 C ATOM 460 C MET A 143 23.408 24.969 16.409 1.00 41.91 C ANISOU 460 C MET A 143 4919 6017 4988 -245 -1240 -749 C ATOM 461 O MET A 143 22.188 25.058 16.565 1.00 44.54 O ANISOU 461 O MET A 143 5455 6360 5108 -289 -1086 -866 O ATOM 462 CB MET A 143 24.345 25.952 18.528 1.00 43.31 C ANISOU 462 CB MET A 143 5245 6337 4873 -664 -1704 -693 C ATOM 463 CG MET A 143 25.337 26.880 19.224 1.00 48.69 C ANISOU 463 CG MET A 143 5903 7077 5521 -907 -1980 -666 C ATOM 464 SD MET A 143 27.084 26.380 19.164 1.00 51.35 S ANISOU 464 SD MET A 143 5822 7456 6233 -882 -2339 -329 S ATOM 465 CE MET A 143 27.200 25.105 20.421 1.00 51.61 C ANISOU 465 CE MET A 143 5976 7536 6098 -973 -2692 -60 C ATOM 466 N ILE A 144 23.971 23.978 15.722 1.00 39.29 N ANISOU 466 N ILE A 144 4421 5607 4902 -49 -1234 -617 N ATOM 467 CA ILE A 144 23.154 22.952 15.074 1.00 46.29 C ANISOU 467 CA ILE A 144 5416 6392 5781 90 -1065 -627 C ATOM 468 C ILE A 144 23.268 21.601 15.751 1.00 52.18 C ANISOU 468 C ILE A 144 6238 7068 6519 121 -1249 -440 C ATOM 469 O ILE A 144 24.362 21.028 15.854 1.00 55.64 O ANISOU 469 O ILE A 144 6500 7450 7193 234 -1406 -265 O ATOM 470 CB ILE A 144 23.515 22.728 13.599 1.00 45.67 C ANISOU 470 CB ILE A 144 5193 6211 5948 298 -847 -665 C ATOM 471 CG1 ILE A 144 23.644 24.048 12.848 1.00 44.48 C ANISOU 471 CG1 ILE A 144 4932 6120 5847 265 -696 -793 C ATOM 472 CG2 ILE A 144 22.438 21.876 12.955 1.00 38.13 C ANISOU 472 CG2 ILE A 144 4440 5152 4897 354 -688 -718 C ATOM 473 CD1 ILE A 144 22.384 24.860 12.890 1.00 49.55 C ANISOU 473 CD1 ILE A 144 5751 6807 6270 140 -593 -939 C ATOM 474 N SER A 145 22.124 21.077 16.174 1.00 41.77 N ANISOU 474 N SER A 145 5161 5747 4961 28 -1222 -451 N ATOM 475 CA SER A 145 22.109 19.864 16.969 1.00 44.16 C ANISOU 475 CA SER A 145 5587 5987 5207 -1 -1420 -254 C ATOM 476 C SER A 145 20.933 18.964 16.624 1.00 42.57 C ANISOU 476 C SER A 145 5588 5689 4896 -6 -1290 -267 C ATOM 477 O SER A 145 19.888 19.404 16.126 1.00 38.04 O ANISOU 477 O SER A 145 5083 5168 4202 -62 -1082 -415 O ATOM 478 CB SER A 145 22.086 20.215 18.465 1.00 46.73 C ANISOU 478 CB SER A 145 6038 6467 5250 -251 -1649 -177 C ATOM 479 OG SER A 145 21.039 21.125 18.787 1.00 42.41 O ANISOU 479 OG SER A 145 5649 6054 4413 -416 -1474 -368 O ATOM 480 N PHE A 146 21.127 17.684 16.885 1.00 50.76 N ANISOU 480 N PHE A 146 6711 6572 6004 45 -1436 -82 N ATOM 481 CA PHE A 146 20.074 16.705 16.711 1.00 48.56 C ANISOU 481 CA PHE A 146 6656 6181 5615 -13 -1376 -50 C ATOM 482 C PHE A 146 19.633 16.247 18.077 1.00 44.72 C ANISOU 482 C PHE A 146 6341 5777 4871 -235 -1575 130 C ATOM 483 O PHE A 146 20.459 16.039 18.963 1.00 47.04 O ANISOU 483 O PHE A 146 6610 6082 5182 -258 -1831 310 O ATOM 484 CB PHE A 146 20.560 15.528 15.870 1.00 51.45 C ANISOU 484 CB PHE A 146 7054 6245 6251 206 -1362 9 C ATOM 485 CG PHE A 146 20.857 15.893 14.454 1.00 49.50 C ANISOU 485 CG PHE A 146 6703 5918 6185 391 -1113 -184 C ATOM 486 CD1 PHE A 146 22.070 16.458 14.116 1.00 47.55 C ANISOU 486 CD1 PHE A 146 6194 5691 6181 576 -1077 -207 C ATOM 487 CD2 PHE A 146 19.920 15.675 13.457 1.00 51.03 C ANISOU 487 CD2 PHE A 146 7065 6032 6291 348 -927 -320 C ATOM 488 CE1 PHE A 146 22.353 16.807 12.804 1.00 44.17 C ANISOU 488 CE1 PHE A 146 5687 5208 5888 724 -819 -376 C ATOM 489 CE2 PHE A 146 20.194 16.022 12.143 1.00 52.85 C ANISOU 489 CE2 PHE A 146 7246 6200 6633 481 -704 -490 C ATOM 490 CZ PHE A 146 21.420 16.591 11.818 1.00 44.22 C ANISOU 490 CZ PHE A 146 5905 5132 5765 675 -631 -523 C ATOM 491 N ALA A 147 18.330 16.108 18.266 1.00 44.04 N ANISOU 491 N ALA A 147 6420 5770 4542 -420 -1464 107 N ATOM 492 CA ALA A 147 17.845 15.650 19.553 1.00 46.86 C ANISOU 492 CA ALA A 147 6959 6226 4620 -658 -1609 285 C ATOM 493 C ALA A 147 16.558 14.849 19.445 1.00 49.29 C ANISOU 493 C ALA A 147 7433 6499 4797 -810 -1516 351 C ATOM 494 O ALA A 147 15.877 14.823 18.412 1.00 54.78 O ANISOU 494 O ALA A 147 8101 7136 5579 -770 -1339 239 O ATOM 495 CB ALA A 147 17.649 16.830 20.500 1.00 52.22 C ANISOU 495 CB ALA A 147 7645 7182 5014 -829 -1558 188 C ATOM 496 N VAL A 148 16.247 14.198 20.554 1.00 49.01 N ANISOU 496 N VAL A 148 9178 3440 6004 -826 -781 1092 N ATOM 497 CA VAL A 148 15.044 13.415 20.697 1.00 60.13 C ANISOU 497 CA VAL A 148 10782 4703 7364 -1164 -594 1076 C ATOM 498 C VAL A 148 14.311 13.884 21.944 1.00 58.43 C ANISOU 498 C VAL A 148 10641 4739 6820 -1421 -558 1219 C ATOM 499 O VAL A 148 14.941 14.292 22.918 1.00 51.32 O ANISOU 499 O VAL A 148 9791 3951 5758 -1315 -716 1439 O ATOM 500 CB VAL A 148 15.380 11.915 20.775 1.00 65.27 C ANISOU 500 CB VAL A 148 11754 4834 8213 -1132 -602 1266 C ATOM 501 CG1 VAL A 148 14.787 11.284 22.023 1.00 66.89 C ANISOU 501 CG1 VAL A 148 12279 4907 8229 -1412 -556 1566 C ATOM 502 CG2 VAL A 148 14.927 11.214 19.503 1.00 64.13 C ANISOU 502 CG2 VAL A 148 11596 4461 8309 -1199 -447 977 C ATOM 503 N ARG A 149 12.985 13.861 21.866 1.00 57.39 N ANISOU 503 N ARG A 149 10489 4733 6586 -1755 -348 1066 N ATOM 504 CA ARG A 149 12.092 14.110 22.991 1.00 56.08 C ANISOU 504 CA ARG A 149 10402 4795 6111 -2050 -248 1173 C ATOM 505 C ARG A 149 12.499 15.295 23.878 1.00 60.59 C ANISOU 505 C ARG A 149 10877 5718 6428 -1931 -379 1246 C ATOM 506 O ARG A 149 12.376 16.437 23.453 1.00 57.92 O ANISOU 506 O ARG A 149 10265 5684 6059 -1842 -382 1009 O ATOM 507 CB ARG A 149 11.966 12.844 23.846 1.00 56.69 C ANISOU 507 CB ARG A 149 10860 4531 6147 -2249 -206 1497 C ATOM 508 CG ARG A 149 11.459 11.632 23.106 1.00 58.94 C ANISOU 508 CG ARG A 149 11287 4431 6676 -2434 -59 1422 C ATOM 509 CD ARG A 149 10.083 11.838 22.515 1.00 58.08 C ANISOU 509 CD ARG A 149 10972 4559 6535 -2762 172 1099 C ATOM 510 NE ARG A 149 9.626 10.617 21.852 1.00 61.61 N ANISOU 510 NE ARG A 149 11570 4624 7216 -2972 301 1015 N ATOM 511 CZ ARG A 149 8.367 10.375 21.501 1.00 67.78 C ANISOU 511 CZ ARG A 149 12222 5545 7987 -3317 506 787 C ATOM 512 NH1 ARG A 149 7.422 11.273 21.748 1.00 60.30 N ANISOU 512 NH1 ARG A 149 11050 5058 6804 -3535 623 648 N ATOM 513 NH2 ARG A 149 8.050 9.227 20.909 1.00 72.02 N ANISOU 513 NH2 ARG A 149 12809 5799 8756 -3412 586 683 N ATOM 514 N GLU A 150 13.005 14.999 25.084 1.00 66.46 N ANISOU 514 N GLU A 150 11859 6400 6993 -1923 -496 1574 N ATOM 515 CA GLU A 150 13.094 15.953 26.193 1.00 64.95 C ANISOU 515 CA GLU A 150 11644 6561 6474 -1929 -577 1648 C ATOM 516 C GLU A 150 14.217 16.972 26.051 1.00 69.96 C ANISOU 516 C GLU A 150 12083 7346 7154 -1607 -808 1581 C ATOM 517 O GLU A 150 14.094 18.083 26.555 1.00 92.38 O ANISOU 517 O GLU A 150 14799 10521 9780 -1620 -835 1472 O ATOM 518 CB GLU A 150 13.233 15.206 27.513 1.00 89.48 C ANISOU 518 CB GLU A 150 15093 9564 9343 -2047 -629 2035 C ATOM 519 CG GLU A 150 11.977 14.431 27.930 1.00106.28 C ANISOU 519 CG GLU A 150 17410 11642 11330 -2451 -364 2114 C ATOM 520 CD GLU A 150 12.170 12.915 27.919 1.00114.42 C ANISOU 520 CD GLU A 150 18693 12211 12569 -2466 -352 2353 C ATOM 521 OE1 GLU A 150 12.713 12.383 26.924 1.00112.49 O ANISOU 521 OE1 GLU A 150 18443 11629 12669 -2281 -414 2295 O ATOM 522 OE2 GLU A 150 11.793 12.260 28.918 1.00118.09 O ANISOU 522 OE2 GLU A 150 19317 12679 12874 -2623 -273 2562 O ATOM 523 N HIS A 151 15.328 16.603 25.430 1.00 50.20 N ANISOU 523 N HIS A 151 9554 4600 4920 -1328 -972 1643 N ATOM 524 CA HIS A 151 15.965 17.561 24.515 1.00 61.93 C ANISOU 524 CA HIS A 151 10735 6215 6579 -1096 -1056 1412 C ATOM 525 C HIS A 151 16.706 18.795 25.105 1.00 62.00 C ANISOU 525 C HIS A 151 10601 6516 6440 -969 -1245 1398 C ATOM 526 O HIS A 151 17.844 19.054 24.730 1.00 64.51 O ANISOU 526 O HIS A 151 10782 6803 6924 -724 -1419 1410 O ATOM 527 CB HIS A 151 14.834 17.940 23.553 1.00 63.48 C ANISOU 527 CB HIS A 151 10758 6527 6835 -1244 -827 1095 C ATOM 528 CG HIS A 151 15.140 18.998 22.554 1.00 44.20 C ANISOU 528 CG HIS A 151 8021 4247 4527 -1071 -852 845 C ATOM 529 ND1 HIS A 151 14.180 19.432 21.669 1.00 39.12 N ANISOU 529 ND1 HIS A 151 7207 3740 3919 -1160 -682 575 N ATOM 530 CD2 HIS A 151 16.240 19.749 22.322 1.00 45.39 C ANISOU 530 CD2 HIS A 151 8015 4466 4766 -835 -1021 832 C ATOM 531 CE1 HIS A 151 14.679 20.403 20.926 1.00 43.92 C ANISOU 531 CE1 HIS A 151 7594 4469 4624 -975 -744 429 C ATOM 532 NE2 HIS A 151 15.926 20.618 21.303 1.00 43.25 N ANISOU 532 NE2 HIS A 151 7512 4343 4580 -794 -938 576 N ATOM 533 N GLY A 152 16.104 19.570 25.998 1.00 63.19 N ANISOU 533 N GLY A 152 10769 6953 6289 -1135 -1208 1352 N ATOM 534 CA GLY A 152 16.895 20.569 26.717 1.00 52.86 C ANISOU 534 CA GLY A 152 9385 5871 4826 -1034 -1414 1360 C ATOM 535 C GLY A 152 16.508 22.039 26.623 1.00 50.32 C ANISOU 535 C GLY A 152 8866 5836 4418 -1071 -1363 1069 C ATOM 536 O GLY A 152 17.235 22.927 27.100 1.00 44.67 O ANISOU 536 O GLY A 152 8077 5278 3619 -994 -1539 1036 O ATOM 537 N ASP A 153 15.376 22.306 25.982 1.00 47.43 N ANISOU 537 N ASP A 153 8408 5528 4084 -1183 -1133 849 N ATOM 538 CA ASP A 153 14.751 23.614 26.048 1.00 39.88 C ANISOU 538 CA ASP A 153 7313 4832 3010 -1227 -1053 588 C ATOM 539 C ASP A 153 13.271 23.448 26.394 1.00 44.21 C ANISOU 539 C ASP A 153 7911 5525 3363 -1454 -805 494 C ATOM 540 O ASP A 153 12.852 22.382 26.869 1.00 43.02 O ANISOU 540 O ASP A 153 7939 5298 3108 -1618 -721 671 O ATOM 541 CB ASP A 153 14.938 24.399 24.738 1.00 37.95 C ANISOU 541 CB ASP A 153 6825 4562 3031 -1070 -1040 379 C ATOM 542 CG ASP A 153 14.411 23.668 23.505 1.00 44.74 C ANISOU 542 CG ASP A 153 7615 5276 4108 -1066 -891 322 C ATOM 543 OD1 ASP A 153 13.786 22.598 23.624 1.00 37.23 O ANISOU 543 OD1 ASP A 153 6791 4231 3125 -1209 -777 406 O ATOM 544 OD2 ASP A 153 14.622 24.186 22.388 1.00 50.46 O ANISOU 544 OD2 ASP A 153 8160 5982 5029 -931 -885 186 O ATOM 545 N PHE A 154 12.484 24.494 26.159 1.00 49.87 N ANISOU 545 N PHE A 154 8466 6446 4037 -1462 -685 224 N ATOM 546 CA PHE A 154 11.067 24.492 26.532 1.00 46.83 C ANISOU 546 CA PHE A 154 8068 6267 3457 -1658 -447 98 C ATOM 547 C PHE A 154 10.212 23.636 25.631 1.00 42.27 C ANISOU 547 C PHE A 154 7421 5606 3035 -1765 -270 61 C ATOM 548 O PHE A 154 9.101 23.289 25.990 1.00 43.97 O ANISOU 548 O PHE A 154 7640 5968 3101 -1979 -71 15 O ATOM 549 CB PHE A 154 10.502 25.908 26.504 1.00 48.97 C ANISOU 549 CB PHE A 154 8167 6774 3664 -1582 -384 -197 C ATOM 550 CG PHE A 154 10.847 26.716 27.700 1.00 52.67 C ANISOU 550 CG PHE A 154 8732 7404 3875 -1580 -474 -230 C ATOM 551 CD1 PHE A 154 11.173 28.059 27.567 1.00 51.15 C ANISOU 551 CD1 PHE A 154 8438 7260 3735 -1421 -560 -435 C ATOM 552 CD2 PHE A 154 10.838 26.138 28.958 1.00 49.50 C ANISOU 552 CD2 PHE A 154 8540 7101 3167 -1748 -471 -59 C ATOM 553 CE1 PHE A 154 11.494 28.811 28.663 1.00 46.79 C ANISOU 553 CE1 PHE A 154 7966 6841 2971 -1421 -642 -502 C ATOM 554 CE2 PHE A 154 11.148 26.873 30.055 1.00 45.30 C ANISOU 554 CE2 PHE A 154 8077 6737 2397 -1738 -555 -112 C ATOM 555 CZ PHE A 154 11.484 28.219 29.915 1.00 51.39 C ANISOU 555 CZ PHE A 154 8700 7537 3290 -1554 -635 -348 C ATOM 556 N TYR A 155 10.719 23.322 24.446 1.00 45.95 N ANISOU 556 N TYR A 155 7806 5859 3793 -1629 -334 59 N ATOM 557 CA TYR A 155 9.878 22.759 23.400 1.00 44.23 C ANISOU 557 CA TYR A 155 7473 5604 3730 -1708 -180 -62 C ATOM 558 C TYR A 155 10.393 21.395 22.931 1.00 48.43 C ANISOU 558 C TYR A 155 8146 5806 4448 -1737 -214 111 C ATOM 559 O TYR A 155 11.181 21.292 21.990 1.00 41.17 O ANISOU 559 O TYR A 155 7171 4714 3759 -1549 -315 103 O ATOM 560 CB TYR A 155 9.775 23.762 22.248 1.00 41.46 C ANISOU 560 CB TYR A 155 6872 5348 3535 -1512 -192 -295 C ATOM 561 CG TYR A 155 9.502 25.169 22.745 1.00 46.06 C ANISOU 561 CG TYR A 155 7357 6172 3973 -1427 -195 -446 C ATOM 562 CD1 TYR A 155 8.246 25.528 23.234 1.00 48.39 C ANISOU 562 CD1 TYR A 155 7568 6735 4084 -1549 -23 -605 C ATOM 563 CD2 TYR A 155 10.505 26.126 22.764 1.00 46.57 C ANISOU 563 CD2 TYR A 155 7413 6190 4091 -1233 -363 -440 C ATOM 564 CE1 TYR A 155 7.995 26.805 23.705 1.00 46.91 C ANISOU 564 CE1 TYR A 155 7306 6741 3775 -1444 -18 -766 C ATOM 565 CE2 TYR A 155 10.261 27.408 23.232 1.00 42.74 C ANISOU 565 CE2 TYR A 155 6872 5877 3492 -1162 -364 -597 C ATOM 566 CZ TYR A 155 9.009 27.744 23.699 1.00 42.79 C ANISOU 566 CZ TYR A 155 6812 6125 3321 -1250 -193 -764 C ATOM 567 OH TYR A 155 8.778 29.021 24.167 1.00 43.34 O ANISOU 567 OH TYR A 155 6839 6338 3292 -1151 -189 -943 O ATOM 568 N PRO A 156 9.943 20.331 23.610 1.00 62.81 N ANISOU 568 N PRO A 156 10164 7534 6167 -1978 -117 270 N ATOM 569 CA PRO A 156 10.409 18.971 23.330 1.00 64.31 C ANISOU 569 CA PRO A 156 10548 7356 6532 -2013 -144 455 C ATOM 570 C PRO A 156 9.932 18.476 21.975 1.00 59.55 C ANISOU 570 C PRO A 156 9817 6643 6165 -2043 -45 257 C ATOM 571 O PRO A 156 8.884 18.896 21.484 1.00 51.52 O ANISOU 571 O PRO A 156 8595 5863 5116 -2150 93 17 O ATOM 572 CB PRO A 156 9.779 18.136 24.455 1.00 46.76 C ANISOU 572 CB PRO A 156 8564 5105 4098 -2318 -22 657 C ATOM 573 CG PRO A 156 9.225 19.103 25.405 1.00 46.91 C ANISOU 573 CG PRO A 156 8515 5499 3809 -2398 38 594 C ATOM 574 CD PRO A 156 8.916 20.340 24.659 1.00 51.51 C ANISOU 574 CD PRO A 156 8788 6332 4450 -2241 49 280 C ATOM 575 N PHE A 157 10.696 17.580 21.374 1.00 53.25 N ANISOU 575 N PHE A 157 9134 5501 5597 -1936 -120 342 N ATOM 576 CA PHE A 157 10.250 16.995 20.133 1.00 52.04 C ANISOU 576 CA PHE A 157 8895 5233 5646 -1987 -24 139 C ATOM 577 C PHE A 157 9.226 15.911 20.457 1.00 54.54 C ANISOU 577 C PHE A 157 9366 5430 5928 -2356 155 167 C ATOM 578 O PHE A 157 8.919 15.678 21.628 1.00 48.12 O ANISOU 578 O PHE A 157 8722 4636 4926 -2550 208 366 O ATOM 579 CB PHE A 157 11.439 16.483 19.340 1.00 45.78 C ANISOU 579 CB PHE A 157 8155 4132 5108 -1724 -151 178 C ATOM 580 CG PHE A 157 12.175 17.572 18.637 1.00 44.61 C ANISOU 580 CG PHE A 157 7775 4155 5018 -1428 -263 64 C ATOM 581 CD1 PHE A 157 11.473 18.530 17.912 1.00 53.88 C ANISOU 581 CD1 PHE A 157 8693 5637 6140 -1426 -196 -183 C ATOM 582 CD2 PHE A 157 13.560 17.670 18.714 1.00 48.21 C ANISOU 582 CD2 PHE A 157 8261 4480 5578 -1153 -436 216 C ATOM 583 CE1 PHE A 157 12.147 19.568 17.250 1.00 51.62 C ANISOU 583 CE1 PHE A 157 8219 5489 5904 -1171 -289 -260 C ATOM 584 CE2 PHE A 157 14.244 18.712 18.058 1.00 43.66 C ANISOU 584 CE2 PHE A 157 7462 4071 5056 -920 -521 117 C ATOM 585 CZ PHE A 157 13.535 19.658 17.329 1.00 43.25 C ANISOU 585 CZ PHE A 157 7193 4290 4950 -939 -441 -109 C ATOM 586 N ASP A 158 8.686 15.267 19.430 1.00 48.63 N ANISOU 586 N ASP A 158 8557 4575 5343 -2475 252 -37 N ATOM 587 CA ASP A 158 7.472 14.485 19.606 1.00 56.54 C ANISOU 587 CA ASP A 158 9612 5567 6303 -2882 448 -95 C ATOM 588 C ASP A 158 7.522 13.075 19.018 1.00 66.29 C ANISOU 588 C ASP A 158 11054 6357 7775 -3023 496 -110 C ATOM 589 O ASP A 158 6.476 12.447 18.809 1.00 71.64 O ANISOU 589 O ASP A 158 11719 7031 8471 -3377 659 -249 O ATOM 590 CB ASP A 158 6.278 15.248 19.004 1.00 53.97 C ANISOU 590 CB ASP A 158 8932 5683 5891 -2998 560 -419 C ATOM 591 CG ASP A 158 6.576 15.863 17.618 1.00 54.31 C ANISOU 591 CG ASP A 158 8731 5840 6064 -2717 465 -672 C ATOM 592 OD1 ASP A 158 7.466 15.381 16.878 1.00 44.83 O ANISOU 592 OD1 ASP A 158 7626 4351 5057 -2531 374 -674 O ATOM 593 OD2 ASP A 158 5.875 16.829 17.254 1.00 55.90 O ANISOU 593 OD2 ASP A 158 8642 6435 6164 -2679 492 -872 O ATOM 594 N GLY A 159 8.725 12.564 18.771 1.00 62.80 N ANISOU 594 N GLY A 159 10798 5540 7522 -2754 359 19 N ATOM 595 CA GLY A 159 8.854 11.278 18.109 1.00 62.78 C ANISOU 595 CA GLY A 159 10995 5085 7773 -2828 398 -39 C ATOM 596 C GLY A 159 8.727 11.496 16.612 1.00 63.46 C ANISOU 596 C GLY A 159 10830 5293 7989 -2721 403 -420 C ATOM 597 O GLY A 159 8.821 12.635 16.158 1.00 57.82 O ANISOU 597 O GLY A 159 9830 4954 7185 -2516 341 -553 O ATOM 598 N PRO A 160 8.508 10.414 15.840 1.00 62.17 N ANISOU 598 N PRO A 160 10785 4809 8026 -2864 476 -597 N ATOM 599 CA PRO A 160 8.492 10.441 14.369 1.00 59.59 C ANISOU 599 CA PRO A 160 10254 4573 7816 -2741 470 -961 C ATOM 600 C PRO A 160 7.258 11.131 13.789 1.00 59.83 C ANISOU 600 C PRO A 160 9940 5104 7688 -2944 548 -1256 C ATOM 601 O PRO A 160 6.157 10.853 14.243 1.00 65.88 O ANISOU 601 O PRO A 160 10651 6011 8370 -3267 661 -1262 O ATOM 602 CB PRO A 160 8.513 8.956 13.998 1.00 58.81 C ANISOU 602 CB PRO A 160 10321 4071 7954 -2787 510 -1002 C ATOM 603 CG PRO A 160 8.999 8.256 15.216 1.00 61.40 C ANISOU 603 CG PRO A 160 10964 4030 8334 -2787 490 -613 C ATOM 604 CD PRO A 160 8.427 9.039 16.348 1.00 63.82 C ANISOU 604 CD PRO A 160 11247 4630 8370 -2994 529 -416 C ATOM 605 N GLY A 161 7.437 12.019 12.813 1.00 50.47 N ANISOU 605 N GLY A 161 8493 4228 6456 -2709 480 -1468 N ATOM 606 CA GLY A 161 6.313 12.765 12.275 1.00 49.41 C ANISOU 606 CA GLY A 161 8023 4590 6160 -2844 523 -1721 C ATOM 607 C GLY A 161 5.992 14.066 12.999 1.00 64.57 C ANISOU 607 C GLY A 161 9742 6922 7871 -2764 500 -1594 C ATOM 608 O GLY A 161 6.699 14.472 13.920 1.00 62.65 O ANISOU 608 O GLY A 161 9615 6601 7587 -2606 442 -1319 O ATOM 609 N ASN A 162 4.918 14.722 12.569 1.00 60.66 N ANISOU 609 N ASN A 162 8937 6871 7239 -2864 537 -1813 N ATOM 610 CA ASN A 162 4.530 16.030 13.095 1.00 51.43 C ANISOU 610 CA ASN A 162 7550 6107 5884 -2750 520 -1754 C ATOM 611 C ASN A 162 5.689 17.046 13.055 1.00 49.02 C ANISOU 611 C ASN A 162 7247 5806 5571 -2331 381 -1602 C ATOM 612 O ASN A 162 6.028 17.503 11.966 1.00 49.59 O ANISOU 612 O ASN A 162 7186 5986 5669 -2101 306 -1730 O ATOM 613 CB ASN A 162 3.937 15.867 14.502 1.00 52.40 C ANISOU 613 CB ASN A 162 7761 6247 5900 -3025 634 -1582 C ATOM 614 CG ASN A 162 2.581 15.154 14.473 1.00 57.04 C ANISOU 614 CG ASN A 162 8238 6970 6463 -3465 792 -1768 C ATOM 615 OD1 ASN A 162 2.484 14.020 14.000 1.00 54.15 O ANISOU 615 OD1 ASN A 162 7991 6343 6240 -3644 833 -1843 O ATOM 616 ND2 ASN A 162 1.527 15.829 14.950 1.00 54.92 N ANISOU 616 ND2 ASN A 162 7712 7131 6024 -3590 879 -1840 N ATOM 617 N VAL A 163 6.289 17.415 14.194 1.00 40.09 N ANISOU 617 N VAL A 163 6259 4581 4393 -2246 347 -1339 N ATOM 618 CA VAL A 163 7.393 18.379 14.173 1.00 37.34 C ANISOU 618 CA VAL A 163 5898 4239 4049 -1890 213 -1212 C ATOM 619 C VAL A 163 8.707 17.718 13.765 1.00 37.31 C ANISOU 619 C VAL A 163 6074 3872 4228 -1709 130 -1114 C ATOM 620 O VAL A 163 9.074 16.693 14.295 1.00 45.89 O ANISOU 620 O VAL A 163 7402 4628 5406 -1808 143 -976 O ATOM 621 CB VAL A 163 7.603 19.053 15.530 1.00 41.33 C ANISOU 621 CB VAL A 163 6477 4802 4425 -1865 186 -1000 C ATOM 622 CG1 VAL A 163 8.738 20.090 15.443 1.00 34.20 C ANISOU 622 CG1 VAL A 163 5542 3910 3543 -1531 42 -901 C ATOM 623 CG2 VAL A 163 6.334 19.707 15.999 1.00 37.15 C ANISOU 623 CG2 VAL A 163 5767 4634 3716 -2017 287 -1111 C ATOM 624 N LEU A 164 9.415 18.303 12.814 1.00 35.44 N ANISOU 624 N LEU A 164 5719 3701 4044 -1436 53 -1178 N ATOM 625 CA LEU A 164 10.636 17.685 12.314 1.00 38.70 C ANISOU 625 CA LEU A 164 6252 3819 4633 -1247 -4 -1126 C ATOM 626 C LEU A 164 11.847 18.445 12.820 1.00 38.71 C ANISOU 626 C LEU A 164 6262 3794 4652 -993 -124 -908 C ATOM 627 O LEU A 164 12.897 17.862 13.051 1.00 41.33 O ANISOU 627 O LEU A 164 6733 3855 5116 -867 -185 -766 O ATOM 628 CB LEU A 164 10.656 17.647 10.780 1.00 35.46 C ANISOU 628 CB LEU A 164 5701 3508 4267 -1138 15 -1370 C ATOM 629 CG LEU A 164 9.479 16.967 10.094 1.00 37.31 C ANISOU 629 CG LEU A 164 5883 3821 4473 -1384 109 -1640 C ATOM 630 CD1 LEU A 164 9.636 16.974 8.583 1.00 37.26 C ANISOU 630 CD1 LEU A 164 5749 3938 4471 -1247 108 -1876 C ATOM 631 CD2 LEU A 164 9.306 15.572 10.606 1.00 45.40 C ANISOU 631 CD2 LEU A 164 7152 4477 5619 -1624 177 -1623 C ATOM 632 N ALA A 165 11.691 19.755 12.971 1.00 36.73 N ANISOU 632 N ALA A 165 5853 3825 4275 -916 -161 -895 N ATOM 633 CA ALA A 165 12.766 20.598 13.453 1.00 33.06 C ANISOU 633 CA ALA A 165 5377 3363 3821 -720 -276 -719 C ATOM 634 C ALA A 165 12.210 21.920 13.973 1.00 36.81 C ANISOU 634 C ALA A 165 5743 4107 4137 -732 -290 -721 C ATOM 635 O ALA A 165 11.023 22.225 13.797 1.00 39.13 O ANISOU 635 O ALA A 165 5935 4609 4323 -843 -211 -867 O ATOM 636 CB ALA A 165 13.767 20.826 12.359 1.00 33.15 C ANISOU 636 CB ALA A 165 5284 3361 3949 -485 -314 -754 C ATOM 637 N HIS A 166 13.049 22.691 14.652 1.00 36.47 N ANISOU 637 N HIS A 166 5716 4060 4083 -620 -395 -574 N ATOM 638 CA HIS A 166 12.683 24.070 14.985 1.00 30.61 C ANISOU 638 CA HIS A 166 4875 3534 3223 -587 -414 -606 C ATOM 639 C HIS A 166 13.916 24.911 15.237 1.00 34.08 C ANISOU 639 C HIS A 166 5300 3933 3717 -433 -541 -483 C ATOM 640 O HIS A 166 15.024 24.390 15.379 1.00 41.84 O ANISOU 640 O HIS A 166 6339 4751 4805 -365 -623 -354 O ATOM 641 CB HIS A 166 11.716 24.140 16.183 1.00 28.09 C ANISOU 641 CB HIS A 166 4623 3317 2731 -770 -363 -610 C ATOM 642 CG HIS A 166 12.222 23.542 17.465 1.00 29.45 C ANISOU 642 CG HIS A 166 4993 3343 2853 -863 -420 -423 C ATOM 643 ND1 HIS A 166 11.401 22.826 18.315 1.00 42.02 N ANISOU 643 ND1 HIS A 166 6705 4940 4319 -1086 -330 -392 N ATOM 644 CD2 HIS A 166 13.424 23.610 18.083 1.00 36.33 C ANISOU 644 CD2 HIS A 166 5954 4092 3758 -769 -562 -249 C ATOM 645 CE1 HIS A 166 12.083 22.457 19.384 1.00 42.18 C ANISOU 645 CE1 HIS A 166 6908 4835 4285 -1114 -418 -187 C ATOM 646 NE2 HIS A 166 13.313 22.929 19.276 1.00 36.17 N ANISOU 646 NE2 HIS A 166 6121 4004 3617 -915 -571 -105 N ATOM 647 N ALA A 167 13.729 26.220 15.267 1.00 34.38 N ANISOU 647 N ALA A 167 5254 4116 3695 -376 -559 -531 N ATOM 648 CA ALA A 167 14.859 27.130 15.355 1.00 33.85 C ANISOU 648 CA ALA A 167 5154 4011 3696 -262 -669 -442 C ATOM 649 C ALA A 167 14.457 28.374 16.119 1.00 44.10 C ANISOU 649 C ALA A 167 6461 5409 4884 -281 -695 -488 C ATOM 650 O ALA A 167 13.275 28.597 16.361 1.00 46.26 O ANISOU 650 O ALA A 167 6730 5808 5039 -337 -612 -603 O ATOM 651 CB ALA A 167 15.371 27.489 13.950 1.00 24.29 C ANISOU 651 CB ALA A 167 3810 2815 2604 -121 -648 -463 C ATOM 652 N TYR A 168 15.431 29.187 16.509 1.00 40.59 N ANISOU 652 N TYR A 168 6021 4917 4486 -239 -806 -420 N ATOM 653 CA TYR A 168 15.107 30.413 17.228 1.00 36.29 C ANISOU 653 CA TYR A 168 5506 4430 3851 -255 -832 -495 C ATOM 654 C TYR A 168 15.553 31.611 16.427 1.00 37.58 C ANISOU 654 C TYR A 168 5589 4559 4129 -150 -851 -506 C ATOM 655 O TYR A 168 16.576 31.545 15.733 1.00 34.84 O ANISOU 655 O TYR A 168 5173 4145 3920 -103 -890 -409 O ATOM 656 CB TYR A 168 15.770 30.435 18.609 1.00 31.53 C ANISOU 656 CB TYR A 168 5013 3799 3168 -345 -958 -429 C ATOM 657 CG TYR A 168 15.292 29.343 19.524 1.00 32.70 C ANISOU 657 CG TYR A 168 5278 3980 3166 -462 -936 -383 C ATOM 658 CD1 TYR A 168 15.890 28.094 19.504 1.00 33.97 C ANISOU 658 CD1 TYR A 168 5483 4037 3387 -472 -979 -233 C ATOM 659 CD2 TYR A 168 14.242 29.563 20.421 1.00 33.77 C ANISOU 659 CD2 TYR A 168 5488 4243 3098 -558 -860 -485 C ATOM 660 CE1 TYR A 168 15.458 27.080 20.346 1.00 38.71 C ANISOU 660 CE1 TYR A 168 6225 4629 3853 -591 -955 -155 C ATOM 661 CE2 TYR A 168 13.799 28.560 21.274 1.00 31.30 C ANISOU 661 CE2 TYR A 168 5295 3968 2629 -697 -820 -416 C ATOM 662 CZ TYR A 168 14.414 27.314 21.225 1.00 41.91 C ANISOU 662 CZ TYR A 168 6707 5175 4041 -720 -871 -236 C ATOM 663 OH TYR A 168 13.987 26.288 22.037 1.00 49.07 O ANISOU 663 OH TYR A 168 7765 6078 4803 -866 -827 -132 O ATOM 664 N ALA A 169 14.792 32.701 16.534 1.00 37.13 N ANISOU 664 N ALA A 169 5543 4545 4018 -110 -814 -619 N ATOM 665 CA ALA A 169 15.157 33.979 15.912 1.00 29.34 C ANISOU 665 CA ALA A 169 4529 3480 3138 -21 -834 -613 C ATOM 666 C ALA A 169 16.525 34.501 16.407 1.00 35.19 C ANISOU 666 C ALA A 169 5299 4098 3975 -94 -960 -535 C ATOM 667 O ALA A 169 16.978 34.118 17.482 1.00 36.99 O ANISOU 667 O ALA A 169 5583 4331 4142 -196 -1050 -525 O ATOM 668 CB ALA A 169 14.073 34.989 16.171 1.00 25.17 C ANISOU 668 CB ALA A 169 4039 2988 2538 51 -784 -757 C ATOM 669 N PRO A 170 17.197 35.362 15.608 1.00 34.08 N ANISOU 669 N PRO A 170 5113 3861 3976 -57 -969 -470 N ATOM 670 CA PRO A 170 18.513 35.950 15.932 1.00 31.27 C ANISOU 670 CA PRO A 170 4745 3402 3736 -156 -1078 -405 C ATOM 671 C PRO A 170 18.649 36.549 17.329 1.00 37.09 C ANISOU 671 C PRO A 170 5591 4097 4406 -268 -1190 -512 C ATOM 672 O PRO A 170 17.792 37.296 17.786 1.00 45.32 O ANISOU 672 O PRO A 170 6740 5108 5371 -242 -1158 -653 O ATOM 673 CB PRO A 170 18.661 37.060 14.899 1.00 34.78 C ANISOU 673 CB PRO A 170 5173 3740 4303 -105 -1021 -355 C ATOM 674 CG PRO A 170 17.919 36.545 13.717 1.00 38.51 C ANISOU 674 CG PRO A 170 5585 4309 4738 35 -901 -317 C ATOM 675 CD PRO A 170 16.745 35.759 14.262 1.00 29.27 C ANISOU 675 CD PRO A 170 4449 3260 3414 71 -870 -437 C ATOM 676 N GLY A 171 19.753 36.241 17.991 1.00 32.02 N ANISOU 676 N GLY A 171 4911 3468 3788 -381 -1325 -458 N ATOM 677 CA GLY A 171 19.973 36.721 19.336 1.00 29.96 C ANISOU 677 CA GLY A 171 4748 3205 3429 -502 -1454 -566 C ATOM 678 C GLY A 171 21.082 35.930 19.995 1.00 38.50 C ANISOU 678 C GLY A 171 5756 4375 4496 -585 -1617 -468 C ATOM 679 O GLY A 171 21.660 35.010 19.402 1.00 44.55 O ANISOU 679 O GLY A 171 6396 5180 5350 -528 -1618 -321 O ATOM 680 N PRO A 172 21.388 36.277 21.242 1.00 32.61 N ANISOU 680 N PRO A 172 5089 3672 3631 -705 -1764 -557 N ATOM 681 CA PRO A 172 22.441 35.566 21.957 1.00 39.31 C ANISOU 681 CA PRO A 172 5864 4633 4440 -767 -1955 -455 C ATOM 682 C PRO A 172 21.877 34.266 22.504 1.00 41.68 C ANISOU 682 C PRO A 172 6249 5037 4552 -703 -1946 -370 C ATOM 683 O PRO A 172 20.665 34.070 22.446 1.00 39.75 O ANISOU 683 O PRO A 172 6113 4792 4198 -659 -1791 -429 O ATOM 684 CB PRO A 172 22.819 36.538 23.055 1.00 36.08 C ANISOU 684 CB PRO A 172 5528 4242 3938 -927 -2111 -612 C ATOM 685 CG PRO A 172 21.548 37.231 23.349 1.00 35.86 C ANISOU 685 CG PRO A 172 5687 4157 3782 -912 -1979 -804 C ATOM 686 CD PRO A 172 20.778 37.329 22.070 1.00 34.49 C ANISOU 686 CD PRO A 172 5487 3871 3748 -773 -1770 -770 C ATOM 687 N GLY A 173 22.734 33.378 22.986 1.00 34.52 N ANISOU 687 N GLY A 173 5284 4213 3619 -697 -2105 -223 N ATOM 688 CA GLY A 173 22.274 32.118 23.535 1.00 34.69 C ANISOU 688 CA GLY A 173 5418 4290 3471 -648 -2104 -105 C ATOM 689 C GLY A 173 21.616 31.105 22.616 1.00 41.63 C ANISOU 689 C GLY A 173 6300 5089 4430 -533 -1923 -18 C ATOM 690 O GLY A 173 22.079 30.870 21.502 1.00 51.23 O ANISOU 690 O GLY A 173 7369 6233 5862 -437 -1869 38 O ATOM 691 N ILE A 174 20.543 30.487 23.116 1.00 44.09 N ANISOU 691 N ILE A 174 6776 5426 4549 -562 -1826 -19 N ATOM 692 CA ILE A 174 19.728 29.506 22.390 1.00 31.62 C ANISOU 692 CA ILE A 174 5226 3777 3011 -504 -1650 28 C ATOM 693 C ILE A 174 19.268 30.128 21.079 1.00 39.66 C ANISOU 693 C ILE A 174 6131 4748 4192 -443 -1491 -93 C ATOM 694 O ILE A 174 18.908 29.432 20.134 1.00 46.97 O ANISOU 694 O ILE A 174 7014 5618 5213 -375 -1370 -71 O ATOM 695 CB ILE A 174 18.474 29.069 23.237 1.00 42.90 C ANISOU 695 CB ILE A 174 6840 5279 4182 -610 -1544 -2 C ATOM 696 CG1 ILE A 174 17.724 27.864 22.655 1.00 45.01 C ANISOU 696 CG1 ILE A 174 7148 5467 4488 -601 -1387 63 C ATOM 697 CG2 ILE A 174 17.472 30.209 23.376 1.00 32.56 C ANISOU 697 CG2 ILE A 174 5546 4062 2764 -664 -1425 -227 C ATOM 698 CD1 ILE A 174 18.392 26.539 22.818 1.00 48.31 C ANISOU 698 CD1 ILE A 174 7635 5766 4957 -559 -1476 283 C ATOM 699 N ASN A 175 19.268 31.459 21.025 1.00 43.54 N ANISOU 699 N ASN A 175 6586 5255 4703 -467 -1496 -224 N ATOM 700 CA ASN A 175 18.799 32.147 19.839 1.00 40.92 C ANISOU 700 CA ASN A 175 6173 4877 4498 -396 -1358 -310 C ATOM 701 C ASN A 175 19.775 31.999 18.707 1.00 44.87 C ANISOU 701 C ASN A 175 6515 5315 5217 -317 -1366 -209 C ATOM 702 O ASN A 175 20.982 32.085 18.898 1.00 53.92 O ANISOU 702 O ASN A 175 7579 6453 6456 -337 -1499 -131 O ATOM 703 CB ASN A 175 18.564 33.612 20.118 1.00 28.40 C ANISOU 703 CB ASN A 175 4624 3276 2891 -431 -1364 -459 C ATOM 704 CG ASN A 175 17.300 33.852 20.877 1.00 38.27 C ANISOU 704 CG ASN A 175 5996 4606 3938 -458 -1280 -609 C ATOM 705 OD1 ASN A 175 17.041 33.202 21.889 1.00 43.96 O ANISOU 705 OD1 ASN A 175 6811 5421 4471 -535 -1306 -598 O ATOM 706 ND2 ASN A 175 16.495 34.803 20.403 1.00 40.30 N ANISOU 706 ND2 ASN A 175 6252 4836 4225 -386 -1175 -744 N ATOM 707 N GLY A 176 19.239 31.779 17.520 1.00 34.53 N ANISOU 707 N GLY A 176 5150 3994 3976 -231 -1221 -222 N ATOM 708 CA GLY A 176 20.076 31.497 16.380 1.00 40.16 C ANISOU 708 CA GLY A 176 5718 4680 4862 -149 -1194 -138 C ATOM 709 C GLY A 176 20.174 30.002 16.166 1.00 38.95 C ANISOU 709 C GLY A 176 5558 4511 4730 -88 -1172 -73 C ATOM 710 O GLY A 176 20.464 29.536 15.068 1.00 38.80 O ANISOU 710 O GLY A 176 5440 4483 4817 3 -1092 -55 O ATOM 711 N ASP A 177 19.913 29.234 17.213 1.00 29.16 N ANISOU 711 N ASP A 177 4441 3257 3380 -140 -1233 -40 N ATOM 712 CA ASP A 177 20.118 27.799 17.106 1.00 28.68 C ANISOU 712 CA ASP A 177 4409 3121 3366 -82 -1229 44 C ATOM 713 C ASP A 177 19.034 27.072 16.306 1.00 32.21 C ANISOU 713 C ASP A 177 4899 3545 3796 -75 -1060 -41 C ATOM 714 O ASP A 177 17.894 27.535 16.167 1.00 36.17 O ANISOU 714 O ASP A 177 5428 4123 4192 -136 -961 -156 O ATOM 715 CB ASP A 177 20.238 27.196 18.499 1.00 33.36 C ANISOU 715 CB ASP A 177 5145 3690 3839 -145 -1356 148 C ATOM 716 CG ASP A 177 21.360 27.842 19.322 1.00 42.16 C ANISOU 716 CG ASP A 177 6203 4864 4954 -157 -1556 219 C ATOM 717 OD1 ASP A 177 21.907 28.895 18.907 1.00 42.49 O ANISOU 717 OD1 ASP A 177 6106 4952 5085 -160 -1579 164 O ATOM 718 OD2 ASP A 177 21.684 27.293 20.393 1.00 45.42 O ANISOU 718 OD2 ASP A 177 6713 5279 5267 -177 -1696 334 O ATOM 719 N ALA A 178 19.414 25.921 15.773 1.00 29.27 N ANISOU 719 N ALA A 178 4519 3070 3534 6 -1033 0 N ATOM 720 CA ALA A 178 18.496 25.092 15.015 1.00 34.49 C ANISOU 720 CA ALA A 178 5223 3690 4190 -10 -889 -99 C ATOM 721 C ALA A 178 18.529 23.659 15.546 1.00 46.07 C ANISOU 721 C ALA A 178 6845 4976 5685 -29 -907 -16 C ATOM 722 O ALA A 178 19.603 23.083 15.758 1.00 53.66 O ANISOU 722 O ALA A 178 7806 5819 6762 87 -1007 107 O ATOM 723 CB ALA A 178 18.845 25.132 13.555 1.00 36.65 C ANISOU 723 CB ALA A 178 5351 3996 4577 111 -803 -178 C ATOM 724 N HIS A 179 17.351 23.093 15.790 1.00 42.73 N ANISOU 724 N HIS A 179 6549 4527 5159 -176 -814 -73 N ATOM 725 CA HIS A 179 17.274 21.762 16.379 1.00 38.47 C ANISOU 725 CA HIS A 179 6200 3780 4637 -236 -819 29 C ATOM 726 C HIS A 179 16.584 20.813 15.417 1.00 37.65 C ANISOU 726 C HIS A 179 6127 3569 4609 -283 -674 -114 C ATOM 727 O HIS A 179 15.584 21.171 14.786 1.00 35.62 O ANISOU 727 O HIS A 179 5790 3465 4281 -376 -562 -289 O ATOM 728 CB HIS A 179 16.525 21.791 17.712 1.00 36.98 C ANISOU 728 CB HIS A 179 6168 3637 4246 -427 -829 112 C ATOM 729 CG HIS A 179 17.204 22.595 18.776 1.00 39.19 C ANISOU 729 CG HIS A 179 6451 4015 4423 -398 -986 236 C ATOM 730 ND1 HIS A 179 16.572 22.959 19.948 1.00 44.08 N ANISOU 730 ND1 HIS A 179 7179 4754 4816 -555 -992 270 N ATOM 731 CD2 HIS A 179 18.461 23.092 18.854 1.00 36.36 C ANISOU 731 CD2 HIS A 179 5992 3674 4148 -247 -1142 316 C ATOM 732 CE1 HIS A 179 17.409 23.655 20.698 1.00 46.27 C ANISOU 732 CE1 HIS A 179 7438 5110 5033 -499 -1156 353 C ATOM 733 NE2 HIS A 179 18.558 23.759 20.052 1.00 41.87 N ANISOU 733 NE2 HIS A 179 6746 4494 4670 -322 -1254 384 N ATOM 734 N PHE A 180 17.110 19.603 15.297 1.00 34.71 N ANISOU 734 N PHE A 180 5870 2935 4383 -212 -685 -51 N ATOM 735 CA PHE A 180 16.503 18.641 14.385 1.00 44.79 C ANISOU 735 CA PHE A 180 7198 4076 5744 -272 -551 -218 C ATOM 736 C PHE A 180 16.118 17.372 15.132 1.00 44.03 C ANISOU 736 C PHE A 180 7366 3691 5670 -420 -529 -110 C ATOM 737 O PHE A 180 16.911 16.799 15.896 1.00 38.50 O ANISOU 737 O PHE A 180 6814 2777 5037 -323 -636 108 O ATOM 738 CB PHE A 180 17.442 18.345 13.211 1.00 39.22 C ANISOU 738 CB PHE A 180 6384 3298 5222 -38 -541 -313 C ATOM 739 CG PHE A 180 17.719 19.547 12.362 1.00 38.26 C ANISOU 739 CG PHE A 180 6018 3458 5062 68 -530 -409 C ATOM 740 CD1 PHE A 180 18.514 20.582 12.837 1.00 39.68 C ANISOU 740 CD1 PHE A 180 6083 3772 5220 159 -640 -273 C ATOM 741 CD2 PHE A 180 17.164 19.666 11.102 1.00 45.59 C ANISOU 741 CD2 PHE A 180 6840 4521 5961 57 -414 -630 C ATOM 742 CE1 PHE A 180 18.748 21.718 12.065 1.00 43.24 C ANISOU 742 CE1 PHE A 180 6337 4450 5642 228 -618 -338 C ATOM 743 CE2 PHE A 180 17.410 20.791 10.313 1.00 49.78 C ANISOU 743 CE2 PHE A 180 7172 5304 6437 153 -401 -679 C ATOM 744 CZ PHE A 180 18.196 21.820 10.797 1.00 43.60 C ANISOU 744 CZ PHE A 180 6296 4616 5653 232 -495 -523 C ATOM 745 N ASP A 181 14.868 16.973 14.937 1.00 41.92 N ANISOU 745 N ASP A 181 7155 3435 5338 -667 -393 -252 N ATOM 746 CA ASP A 181 14.329 15.792 15.579 1.00 48.74 C ANISOU 746 CA ASP A 181 8277 4025 6218 -877 -335 -162 C ATOM 747 C ASP A 181 14.921 14.529 14.952 1.00 57.22 C ANISOU 747 C ASP A 181 9496 4712 7533 -761 -323 -194 C ATOM 748 O ASP A 181 14.591 14.154 13.821 1.00 58.84 O ANISOU 748 O ASP A 181 9642 4886 7829 -781 -226 -451 O ATOM 749 CB ASP A 181 12.807 15.788 15.478 1.00 41.51 C ANISOU 749 CB ASP A 181 7327 3273 5173 -1201 -183 -335 C ATOM 750 CG ASP A 181 12.175 14.699 16.307 1.00 45.27 C ANISOU 750 CG ASP A 181 8067 3501 5633 -1484 -104 -210 C ATOM 751 OD1 ASP A 181 12.899 13.800 16.783 1.00 45.59 O ANISOU 751 OD1 ASP A 181 8352 3179 5792 -1411 -165 0 O ATOM 752 OD2 ASP A 181 10.945 14.740 16.469 1.00 45.61 O ANISOU 752 OD2 ASP A 181 8067 3714 5549 -1779 23 -315 O ATOM 753 N ASP A 182 15.785 13.862 15.706 1.00 48.69 N ANISOU 753 N ASP A 182 8612 3337 6549 -627 -428 61 N ATOM 754 CA ASP A 182 16.485 12.717 15.179 1.00 49.51 C ANISOU 754 CA ASP A 182 8856 3048 6906 -447 -432 44 C ATOM 755 C ASP A 182 15.600 11.475 15.152 1.00 58.20 C ANISOU 755 C ASP A 182 10225 3804 8084 -714 -301 -16 C ATOM 756 O ASP A 182 16.057 10.380 14.812 1.00 63.58 O ANISOU 756 O ASP A 182 11091 4077 8991 -596 -291 -33 O ATOM 757 CB ASP A 182 17.741 12.449 15.989 1.00 54.22 C ANISOU 757 CB ASP A 182 9555 3457 7590 -171 -611 349 C ATOM 758 CG ASP A 182 18.834 11.846 15.156 1.00 58.90 C ANISOU 758 CG ASP A 182 10107 3823 8448 174 -643 268 C ATOM 759 OD1 ASP A 182 18.572 11.572 13.968 1.00 59.74 O ANISOU 759 OD1 ASP A 182 10146 3896 8655 173 -511 -32 O ATOM 760 OD2 ASP A 182 19.943 11.633 15.686 1.00 67.48 O ANISOU 760 OD2 ASP A 182 11222 4785 9633 451 -799 492 O ATOM 761 N ASP A 183 14.332 11.642 15.506 1.00 50.68 N ANISOU 761 N ASP A 183 9289 3009 6957 -1080 -194 -61 N ATOM 762 CA ASP A 183 13.390 10.543 15.383 1.00 55.38 C ANISOU 762 CA ASP A 183 10096 3322 7624 -1399 -49 -159 C ATOM 763 C ASP A 183 12.783 10.508 13.967 1.00 59.64 C ANISOU 763 C ASP A 183 10457 3981 8221 -1482 65 -576 C ATOM 764 O ASP A 183 11.889 9.722 13.676 1.00 54.66 O ANISOU 764 O ASP A 183 9936 3192 7641 -1786 189 -743 O ATOM 765 CB ASP A 183 12.301 10.639 16.452 1.00 58.35 C ANISOU 765 CB ASP A 183 10560 3827 7785 -1781 31 -13 C ATOM 766 CG ASP A 183 12.577 9.743 17.651 1.00 66.59 C ANISOU 766 CG ASP A 183 11971 4484 8846 -1850 -4 362 C ATOM 767 OD1 ASP A 183 13.484 8.889 17.566 1.00 69.65 O ANISOU 767 OD1 ASP A 183 12511 4500 9453 -1597 -81 476 O ATOM 768 OD2 ASP A 183 11.879 9.877 18.675 1.00 74.76 O ANISOU 768 OD2 ASP A 183 13090 5647 9669 -2126 52 541 O ATOM 769 N GLU A 184 13.280 11.372 13.090 1.00 59.92 N ANISOU 769 N GLU A 184 10217 4312 8237 -1225 17 -741 N ATOM 770 CA GLU A 184 13.043 11.211 11.670 1.00 52.03 C ANISOU 770 CA GLU A 184 9085 3383 7302 -1209 94 -1108 C ATOM 771 C GLU A 184 14.244 10.496 11.080 1.00 62.07 C ANISOU 771 C GLU A 184 10455 4320 8809 -882 60 -1148 C ATOM 772 O GLU A 184 15.316 10.461 11.698 1.00 58.72 O ANISOU 772 O GLU A 184 10104 3733 8474 -618 -47 -889 O ATOM 773 CB GLU A 184 12.835 12.553 10.963 1.00 48.03 C ANISOU 773 CB GLU A 184 8233 3401 6616 -1123 80 -1261 C ATOM 774 CG GLU A 184 12.205 13.643 11.807 1.00 56.14 C ANISOU 774 CG GLU A 184 9130 4778 7424 -1250 54 -1117 C ATOM 775 CD GLU A 184 10.850 13.266 12.396 1.00 68.13 C ANISOU 775 CD GLU A 184 10718 6323 8845 -1654 156 -1145 C ATOM 776 OE1 GLU A 184 10.214 12.290 11.930 1.00 75.08 O ANISOU 776 OE1 GLU A 184 11694 7023 9811 -1884 252 -1335 O ATOM 777 OE2 GLU A 184 10.418 13.963 13.343 1.00 65.43 O ANISOU 777 OE2 GLU A 184 10328 6195 8336 -1754 148 -989 O ATOM 778 N GLN A 185 14.063 9.916 9.895 1.00 60.93 N ANISOU 778 N GLN A 185 10301 4093 8757 -894 148 -1488 N ATOM 779 CA GLN A 185 15.188 9.405 9.136 1.00 56.18 C ANISOU 779 CA GLN A 185 9725 3269 8350 -546 141 -1599 C ATOM 780 C GLN A 185 15.671 10.490 8.181 1.00 57.02 C ANISOU 780 C GLN A 185 9499 3830 8335 -313 129 -1738 C ATOM 781 O GLN A 185 14.992 10.832 7.207 1.00 57.22 O ANISOU 781 O GLN A 185 9365 4152 8223 -431 197 -2021 O ATOM 782 CB GLN A 185 14.815 8.144 8.376 1.00 57.79 C ANISOU 782 CB GLN A 185 10054 3188 8717 -650 224 -1883 C ATOM 783 CG GLN A 185 15.996 7.466 7.697 1.00 65.75 C ANISOU 783 CG GLN A 185 11088 3945 9949 -268 213 -1992 C ATOM 784 CD GLN A 185 16.797 6.586 8.642 1.00 73.19 C ANISOU 784 CD GLN A 185 12236 4429 11145 -87 146 -1689 C ATOM 785 OE1 GLN A 185 16.272 6.087 9.643 1.00 77.06 O ANISOU 785 OE1 GLN A 185 12904 4711 11663 -313 127 -1452 O ATOM 786 NE2 GLN A 185 18.077 6.384 8.324 1.00 69.41 N ANISOU 786 NE2 GLN A 185 11704 3824 10844 329 126 -1687 N ATOM 787 N TRP A 186 16.840 11.045 8.482 1.00 54.48 N ANISOU 787 N TRP A 186 9070 3579 8053 5 36 -1524 N ATOM 788 CA TRP A 186 17.397 12.124 7.682 1.00 52.91 C ANISOU 788 CA TRP A 186 8565 3793 7744 209 31 -1598 C ATOM 789 C TRP A 186 18.174 11.572 6.502 1.00 55.00 C ANISOU 789 C TRP A 186 8784 3976 8136 466 112 -1851 C ATOM 790 O TRP A 186 19.037 10.707 6.656 1.00 69.25 O ANISOU 790 O TRP A 186 10718 5426 10167 692 100 -1813 O ATOM 791 CB TRP A 186 18.285 13.024 8.543 1.00 57.62 C ANISOU 791 CB TRP A 186 9042 4529 8322 388 -99 -1271 C ATOM 792 CG TRP A 186 17.506 13.747 9.579 1.00 50.50 C ANISOU 792 CG TRP A 186 8153 3787 7249 149 -161 -1076 C ATOM 793 CD1 TRP A 186 17.444 13.454 10.902 1.00 50.64 C ANISOU 793 CD1 TRP A 186 8357 3606 7280 58 -244 -809 C ATOM 794 CD2 TRP A 186 16.642 14.867 9.371 1.00 45.14 C ANISOU 794 CD2 TRP A 186 7298 3505 6347 -19 -139 -1142 C ATOM 795 NE1 TRP A 186 16.604 14.324 11.537 1.00 48.74 N ANISOU 795 NE1 TRP A 186 8059 3629 6830 -164 -259 -729 N ATOM 796 CE2 TRP A 186 16.100 15.208 10.620 1.00 42.06 C ANISOU 796 CE2 TRP A 186 6988 3139 5854 -201 -198 -933 C ATOM 797 CE3 TRP A 186 16.274 15.616 8.245 1.00 46.55 C ANISOU 797 CE3 TRP A 186 7267 4027 6394 -15 -77 -1352 C ATOM 798 CZ2 TRP A 186 15.209 16.259 10.784 1.00 37.16 C ANISOU 798 CZ2 TRP A 186 6235 2856 5030 -362 -189 -952 C ATOM 799 CZ3 TRP A 186 15.395 16.666 8.404 1.00 40.79 C ANISOU 799 CZ3 TRP A 186 6413 3618 5465 -165 -87 -1338 C ATOM 800 CH2 TRP A 186 14.870 16.979 9.665 1.00 41.90 C ANISOU 800 CH2 TRP A 186 6627 3759 5533 -329 -139 -1152 C ATOM 801 N THR A 187 17.860 12.066 5.315 1.00 48.03 N ANISOU 801 N THR A 187 7717 3433 7097 448 194 -2113 N ATOM 802 CA THR A 187 18.454 11.514 4.107 1.00 50.26 C ANISOU 802 CA THR A 187 7963 3683 7451 656 299 -2408 C ATOM 803 C THR A 187 19.081 12.574 3.202 1.00 48.41 C ANISOU 803 C THR A 187 7430 3903 7060 847 337 -2445 C ATOM 804 O THR A 187 18.794 13.771 3.308 1.00 47.55 O ANISOU 804 O THR A 187 7153 4150 6763 765 290 -2298 O ATOM 805 CB THR A 187 17.410 10.714 3.309 1.00 52.46 C ANISOU 805 CB THR A 187 8369 3881 7683 418 395 -2783 C ATOM 806 OG1 THR A 187 16.233 11.506 3.143 1.00 50.18 O ANISOU 806 OG1 THR A 187 7957 3971 7137 137 380 -2828 O ATOM 807 CG2 THR A 187 17.032 9.460 4.055 1.00 55.43 C ANISOU 807 CG2 THR A 187 9066 3737 8258 261 381 -2750 C ATOM 808 N LYS A 188 19.958 12.117 2.319 1.00 56.84 N ANISOU 808 N LYS A 188 8441 4942 8212 1106 433 -2640 N ATOM 809 CA LYS A 188 20.518 12.975 1.296 1.00 56.80 C ANISOU 809 CA LYS A 188 8171 5369 8041 1260 511 -2713 C ATOM 810 C LYS A 188 19.445 13.314 0.270 1.00 56.91 C ANISOU 810 C LYS A 188 8140 5713 7770 1052 573 -2967 C ATOM 811 O LYS A 188 19.308 14.472 -0.122 1.00 61.84 O ANISOU 811 O LYS A 188 8577 6749 8171 1025 567 -2873 O ATOM 812 CB LYS A 188 21.726 12.310 0.631 1.00 67.88 C ANISOU 812 CB LYS A 188 9519 6670 9602 1595 622 -2880 C ATOM 813 CG LYS A 188 23.047 13.007 0.958 1.00 79.28 C ANISOU 813 CG LYS A 188 10727 8265 11131 1853 593 -2615 C ATOM 814 CD LYS A 188 23.049 14.437 0.404 1.00 84.34 C ANISOU 814 CD LYS A 188 11116 9423 11506 1782 624 -2516 C ATOM 815 CE LYS A 188 23.780 15.421 1.318 1.00 79.75 C ANISOU 815 CE LYS A 188 10370 8947 10986 1828 508 -2142 C ATOM 816 NZ LYS A 188 23.545 16.839 0.912 1.00 69.54 N ANISOU 816 NZ LYS A 188 8903 8074 9445 1695 522 -2024 N ATOM 817 N ASP A 189 18.661 12.316 -0.134 1.00 57.49 N ANISOU 817 N ASP A 189 8393 5615 7834 889 614 -3226 N ATOM 818 CA ASP A 189 17.624 12.522 -1.149 1.00 57.97 C ANISOU 818 CA ASP A 189 8403 6028 7596 682 634 -3395 C ATOM 819 C ASP A 189 16.206 12.729 -0.589 1.00 64.00 C ANISOU 819 C ASP A 189 9212 6841 8265 348 537 -3356 C ATOM 820 O ASP A 189 16.012 13.302 0.490 1.00 57.16 O ANISOU 820 O ASP A 189 8336 5919 7463 273 466 -3169 O ATOM 821 CB ASP A 189 17.613 11.348 -2.138 1.00 55.87 C ANISOU 821 CB ASP A 189 8264 5648 7315 694 716 -3656 C ATOM 822 CG ASP A 189 17.471 10.001 -1.451 1.00 74.37 C ANISOU 822 CG ASP A 189 10893 7452 9914 624 692 -3701 C ATOM 823 OD1 ASP A 189 17.078 9.953 -0.262 1.00 76.53 O ANISOU 823 OD1 ASP A 189 11274 7477 10328 482 608 -3529 O ATOM 824 OD2 ASP A 189 17.746 8.976 -2.110 1.00 86.02 O ANISOU 824 OD2 ASP A 189 12501 8743 11439 706 759 -3902 O ATOM 825 N THR A 190 15.227 12.251 -1.354 1.00 69.86 N ANISOU 825 N THR A 190 9983 7707 8854 153 534 -3540 N ATOM 826 CA THR A 190 13.812 12.501 -1.111 1.00 65.97 C ANISOU 826 CA THR A 190 9450 7383 8233 -148 451 -3528 C ATOM 827 C THR A 190 13.178 11.313 -0.402 1.00 61.99 C ANISOU 827 C THR A 190 9162 6477 7915 -381 428 -3581 C ATOM 828 O THR A 190 12.067 11.397 0.109 1.00 65.69 O ANISOU 828 O THR A 190 9604 7014 8343 -646 374 -3539 O ATOM 829 CB THR A 190 13.055 12.765 -2.447 1.00 95.49 C ANISOU 829 CB THR A 190 13037 11555 11692 -216 441 -3685 C ATOM 830 OG1 THR A 190 13.878 13.537 -3.328 1.00 99.41 O ANISOU 830 OG1 THR A 190 13393 12345 12033 26 493 -3658 O ATOM 831 CG2 THR A 190 11.758 13.508 -2.216 1.00 92.84 C ANISOU 831 CG2 THR A 190 12550 11522 11201 -425 347 -3601 C ATOM 832 N THR A 191 13.896 10.201 -0.367 1.00 56.51 N ANISOU 832 N THR A 191 8677 5364 7432 -273 475 -3660 N ATOM 833 CA THR A 191 13.327 8.953 0.123 1.00 61.99 C ANISOU 833 CA THR A 191 9600 5650 8301 -488 454 -3722 C ATOM 834 C THR A 191 12.950 9.024 1.592 1.00 66.54 C ANISOU 834 C THR A 191 10265 6002 9016 -668 405 -3472 C ATOM 835 O THR A 191 12.084 8.285 2.053 1.00 74.51 O ANISOU 835 O THR A 191 11389 6819 10103 -948 386 -3483 O ATOM 836 CB THR A 191 14.296 7.798 -0.078 1.00 63.17 C ANISOU 836 CB THR A 191 9977 5362 8665 -277 502 -3821 C ATOM 837 OG1 THR A 191 15.390 7.936 0.840 1.00 66.34 O ANISOU 837 OG1 THR A 191 10450 5488 9268 -36 501 -3583 O ATOM 838 CG2 THR A 191 14.806 7.802 -1.515 1.00 64.66 C ANISOU 838 CG2 THR A 191 10070 5801 8696 -76 581 -4058 C ATOM 839 N GLY A 192 13.600 9.920 2.324 1.00 54.97 N ANISOU 839 N GLY A 192 8738 4571 7575 -519 393 -3245 N ATOM 840 CA GLY A 192 13.286 10.128 3.725 1.00 53.52 C ANISOU 840 CA GLY A 192 8636 4220 7477 -684 357 -2988 C ATOM 841 C GLY A 192 12.938 11.571 3.990 1.00 49.55 C ANISOU 841 C GLY A 192 7914 4139 6774 -723 331 -2878 C ATOM 842 O GLY A 192 12.234 12.204 3.215 1.00 58.44 O ANISOU 842 O GLY A 192 8830 5700 7677 -784 318 -3000 O ATOM 843 N THR A 193 13.421 12.104 5.098 1.00 47.54 N ANISOU 843 N THR A 193 7691 3800 6574 -648 283 -2565 N ATOM 844 CA THR A 193 13.245 13.523 5.337 1.00 57.43 C ANISOU 844 CA THR A 193 8716 5473 7630 -607 219 -2387 C ATOM 845 C THR A 193 14.563 14.194 4.976 1.00 55.30 C ANISOU 845 C THR A 193 8324 5307 7379 -249 190 -2268 C ATOM 846 O THR A 193 15.612 13.869 5.528 1.00 59.14 O ANISOU 846 O THR A 193 8904 5524 8041 -60 158 -2088 O ATOM 847 CB THR A 193 12.826 13.843 6.796 1.00 52.91 C ANISOU 847 CB THR A 193 8211 4849 7044 -768 166 -2093 C ATOM 848 OG1 THR A 193 11.682 13.051 7.160 1.00 44.94 O ANISOU 848 OG1 THR A 193 7328 3706 6043 -1124 223 -2197 O ATOM 849 CG2 THR A 193 12.496 15.348 6.938 1.00 39.58 C ANISOU 849 CG2 THR A 193 6288 3602 5149 -733 110 -1978 C ATOM 850 N ASN A 194 14.501 15.113 4.023 1.00 45.04 N ANISOU 850 N ASN A 194 6808 4409 5895 -161 200 -2364 N ATOM 851 CA ASN A 194 15.701 15.653 3.425 1.00 44.78 C ANISOU 851 CA ASN A 194 6647 4498 5867 138 212 -2305 C ATOM 852 C ASN A 194 16.362 16.677 4.323 1.00 47.78 C ANISOU 852 C ASN A 194 6947 4942 6265 248 126 -1966 C ATOM 853 O ASN A 194 15.790 17.736 4.572 1.00 39.94 O ANISOU 853 O ASN A 194 5852 4202 5121 166 78 -1859 O ATOM 854 CB ASN A 194 15.385 16.278 2.074 1.00 41.04 C ANISOU 854 CB ASN A 194 5996 4435 5164 174 260 -2500 C ATOM 855 CG ASN A 194 16.631 16.780 1.376 1.00 52.94 C ANISOU 855 CG ASN A 194 7371 6081 6661 453 308 -2445 C ATOM 856 OD1 ASN A 194 16.957 17.972 1.438 1.00 54.42 O ANISOU 856 OD1 ASN A 194 7416 6501 6758 532 273 -2233 O ATOM 857 ND2 ASN A 194 17.362 15.862 0.734 1.00 49.80 N ANISOU 857 ND2 ASN A 194 7022 5528 6371 601 399 -2637 N ATOM 858 N LEU A 195 17.569 16.367 4.794 1.00 51.93 N ANISOU 858 N LEU A 195 7512 5241 6979 443 99 -1814 N ATOM 859 CA LEU A 195 18.224 17.215 5.776 1.00 46.11 C ANISOU 859 CA LEU A 195 6711 4537 6273 517 -4 -1506 C ATOM 860 C LEU A 195 18.444 18.610 5.200 1.00 42.26 C ANISOU 860 C LEU A 195 6003 4422 5633 583 0 -1450 C ATOM 861 O LEU A 195 18.230 19.616 5.878 1.00 33.55 O ANISOU 861 O LEU A 195 4854 3441 4454 514 -77 -1273 O ATOM 862 CB LEU A 195 19.549 16.611 6.236 1.00 47.59 C ANISOU 862 CB LEU A 195 6933 4464 6684 743 -47 -1377 C ATOM 863 CG LEU A 195 20.168 17.442 7.368 1.00 43.66 C ANISOU 863 CG LEU A 195 6372 4011 6204 782 -183 -1070 C ATOM 864 CD1 LEU A 195 19.119 17.635 8.461 1.00 39.37 C ANISOU 864 CD1 LEU A 195 5972 3431 5557 534 -252 -956 C ATOM 865 CD2 LEU A 195 21.454 16.845 7.948 1.00 38.68 C ANISOU 865 CD2 LEU A 195 5753 3156 5789 1011 -264 -918 C ATOM 866 N PHE A 196 18.825 18.671 3.932 1.00 47.16 N ANISOU 866 N PHE A 196 6505 5216 6197 707 98 -1607 N ATOM 867 CA PHE A 196 19.100 19.957 3.312 1.00 50.06 C ANISOU 867 CA PHE A 196 6687 5915 6420 767 118 -1524 C ATOM 868 C PHE A 196 17.879 20.866 3.320 1.00 46.88 C ANISOU 868 C PHE A 196 6269 5728 5816 604 78 -1506 C ATOM 869 O PHE A 196 17.963 22.017 3.787 1.00 40.75 O ANISOU 869 O PHE A 196 5428 5056 4998 596 16 -1308 O ATOM 870 CB PHE A 196 19.590 19.783 1.879 1.00 51.52 C ANISOU 870 CB PHE A 196 6766 6280 6529 905 252 -1707 C ATOM 871 CG PHE A 196 19.453 21.022 1.054 1.00 51.49 C ANISOU 871 CG PHE A 196 6622 6637 6306 907 288 -1647 C ATOM 872 CD1 PHE A 196 20.302 22.100 1.253 1.00 48.58 C ANISOU 872 CD1 PHE A 196 6126 6371 5962 970 274 -1405 C ATOM 873 CD2 PHE A 196 18.467 21.122 0.085 1.00 54.30 C ANISOU 873 CD2 PHE A 196 6976 7227 6427 837 327 -1822 C ATOM 874 CE1 PHE A 196 20.174 23.257 0.494 1.00 45.97 C ANISOU 874 CE1 PHE A 196 5701 6330 5437 963 313 -1317 C ATOM 875 CE2 PHE A 196 18.333 22.276 -0.680 1.00 46.40 C ANISOU 875 CE2 PHE A 196 5869 6550 5212 860 348 -1727 C ATOM 876 CZ PHE A 196 19.189 23.343 -0.475 1.00 41.72 C ANISOU 876 CZ PHE A 196 5181 6014 4657 923 348 -1464 C ATOM 877 N LEU A 197 16.757 20.350 2.805 1.00 37.06 N ANISOU 877 N LEU A 197 5077 4548 4456 481 109 -1726 N ATOM 878 CA LEU A 197 15.506 21.115 2.777 1.00 32.55 C ANISOU 878 CA LEU A 197 4461 4207 3697 349 65 -1737 C ATOM 879 C LEU A 197 15.141 21.694 4.130 1.00 39.18 C ANISOU 879 C LEU A 197 5343 4964 4581 253 -26 -1541 C ATOM 880 O LEU A 197 14.997 22.906 4.257 1.00 49.65 O ANISOU 880 O LEU A 197 6589 6455 5819 285 -69 -1405 O ATOM 881 CB LEU A 197 14.349 20.266 2.269 1.00 38.54 C ANISOU 881 CB LEU A 197 5260 5017 4366 192 92 -2016 C ATOM 882 CG LEU A 197 14.441 20.021 0.754 1.00 53.71 C ANISOU 882 CG LEU A 197 7113 7151 6142 276 168 -2242 C ATOM 883 CD1 LEU A 197 13.162 19.414 0.175 1.00 57.25 C ANISOU 883 CD1 LEU A 197 7561 7741 6453 97 166 -2536 C ATOM 884 CD2 LEU A 197 14.815 21.304 0.021 1.00 46.75 C ANISOU 884 CD2 LEU A 197 6092 6581 5090 429 171 -2097 C ATOM 885 N VAL A 198 15.019 20.845 5.144 1.00 39.91 N ANISOU 885 N VAL A 198 5573 4791 4801 142 -49 -1523 N ATOM 886 CA VAL A 198 14.554 21.321 6.439 1.00 36.23 C ANISOU 886 CA VAL A 198 5154 4281 4329 28 -119 -1366 C ATOM 887 C VAL A 198 15.530 22.321 7.054 1.00 37.32 C ANISOU 887 C VAL A 198 5252 4412 4516 150 -190 -1129 C ATOM 888 O VAL A 198 15.116 23.332 7.621 1.00 36.86 O ANISOU 888 O VAL A 198 5162 4465 4378 112 -239 -1036 O ATOM 889 CB VAL A 198 14.326 20.176 7.412 1.00 34.03 C ANISOU 889 CB VAL A 198 5055 3716 4159 -122 -122 -1356 C ATOM 890 CG1 VAL A 198 13.796 20.739 8.743 1.00 29.63 C ANISOU 890 CG1 VAL A 198 4540 3175 3543 -247 -178 -1200 C ATOM 891 CG2 VAL A 198 13.357 19.153 6.804 1.00 32.47 C ANISOU 891 CG2 VAL A 198 4904 3497 3936 -289 -45 -1610 C ATOM 892 N ALA A 199 16.821 22.042 6.917 1.00 39.85 N ANISOU 892 N ALA A 199 5560 4609 4971 295 -194 -1055 N ATOM 893 CA ALA A 199 17.857 22.943 7.414 1.00 38.35 C ANISOU 893 CA ALA A 199 5299 4431 4842 391 -264 -851 C ATOM 894 C ALA A 199 17.743 24.320 6.789 1.00 40.46 C ANISOU 894 C ALA A 199 5441 4940 4992 423 -250 -813 C ATOM 895 O ALA A 199 17.922 25.325 7.458 1.00 40.67 O ANISOU 895 O ALA A 199 5452 4987 5014 404 -320 -674 O ATOM 896 CB ALA A 199 19.233 22.375 7.142 1.00 28.98 C ANISOU 896 CB ALA A 199 4061 3133 3818 555 -253 -814 C ATOM 897 N ALA A 200 17.450 24.371 5.498 1.00 46.82 N ANISOU 897 N ALA A 200 6175 5920 5695 473 -163 -937 N ATOM 898 CA ALA A 200 17.432 25.657 4.824 1.00 41.72 C ANISOU 898 CA ALA A 200 5433 5484 4935 524 -148 -860 C ATOM 899 C ALA A 200 16.325 26.502 5.423 1.00 38.37 C ANISOU 899 C ALA A 200 5044 5122 4415 445 -213 -829 C ATOM 900 O ALA A 200 16.560 27.659 5.765 1.00 41.21 O ANISOU 900 O ALA A 200 5388 5492 4779 463 -257 -685 O ATOM 901 CB ALA A 200 17.257 25.486 3.333 1.00 27.44 C ANISOU 901 CB ALA A 200 3556 3879 2990 595 -50 -991 C ATOM 902 N HIS A 201 15.141 25.904 5.584 1.00 35.17 N ANISOU 902 N HIS A 201 4680 4747 3935 350 -213 -978 N ATOM 903 CA HIS A 201 14.015 26.552 6.262 1.00 34.54 C ANISOU 903 CA HIS A 201 4609 4741 3771 279 -260 -981 C ATOM 904 C HIS A 201 14.377 27.012 7.668 1.00 36.65 C ANISOU 904 C HIS A 201 4951 4850 4123 231 -328 -843 C ATOM 905 O HIS A 201 14.041 28.140 8.059 1.00 34.58 O ANISOU 905 O HIS A 201 4679 4642 3816 254 -367 -782 O ATOM 906 CB HIS A 201 12.804 25.619 6.351 1.00 36.68 C ANISOU 906 CB HIS A 201 4894 5064 3979 141 -234 -1170 C ATOM 907 CG HIS A 201 11.675 26.162 7.179 1.00 40.09 C ANISOU 907 CG HIS A 201 5308 5587 4336 61 -262 -1188 C ATOM 908 ND1 HIS A 201 10.492 26.612 6.623 1.00 34.50 N ANISOU 908 ND1 HIS A 201 4481 5139 3488 81 -263 -1302 N ATOM 909 CD2 HIS A 201 11.546 26.332 8.521 1.00 35.81 C ANISOU 909 CD2 HIS A 201 4840 4940 3826 -24 -288 -1115 C ATOM 910 CE1 HIS A 201 9.688 27.028 7.584 1.00 33.88 C ANISOU 910 CE1 HIS A 201 4389 5105 3379 19 -274 -1309 C ATOM 911 NE2 HIS A 201 10.305 26.871 8.745 1.00 37.52 N ANISOU 911 NE2 HIS A 201 4975 5348 3931 -54 -282 -1201 N ATOM 912 N GLU A 202 15.040 26.153 8.439 1.00 33.38 N ANISOU 912 N GLU A 202 4621 4241 3823 176 -349 -799 N ATOM 913 CA GLU A 202 15.296 26.504 9.838 1.00 40.59 C ANISOU 913 CA GLU A 202 5612 5039 4770 115 -429 -680 C ATOM 914 C GLU A 202 16.377 27.589 9.978 1.00 35.41 C ANISOU 914 C GLU A 202 4912 4361 4181 195 -492 -536 C ATOM 915 O GLU A 202 16.276 28.444 10.853 1.00 36.35 O ANISOU 915 O GLU A 202 5069 4469 4274 155 -554 -484 O ATOM 916 CB GLU A 202 15.663 25.259 10.663 1.00 39.43 C ANISOU 916 CB GLU A 202 5582 4696 4703 40 -453 -644 C ATOM 917 CG GLU A 202 14.613 24.137 10.636 1.00 34.15 C ANISOU 917 CG GLU A 202 4985 4000 3990 -93 -382 -777 C ATOM 918 CD GLU A 202 13.251 24.522 11.237 1.00 40.57 C ANISOU 918 CD GLU A 202 5801 4953 4660 -234 -354 -847 C ATOM 919 OE1 GLU A 202 13.082 25.665 11.726 1.00 37.90 O ANISOU 919 OE1 GLU A 202 5427 4718 4255 -204 -393 -803 O ATOM 920 OE2 GLU A 202 12.335 23.663 11.215 1.00 38.48 O ANISOU 920 OE2 GLU A 202 5567 4696 4358 -381 -286 -962 O ATOM 921 N ILE A 203 17.396 27.556 9.121 1.00 27.67 N ANISOU 921 N ILE A 203 3848 3381 3284 291 -467 -489 N ATOM 922 CA ILE A 203 18.376 28.637 9.054 1.00 34.55 C ANISOU 922 CA ILE A 203 4648 4259 4221 333 -502 -360 C ATOM 923 C ILE A 203 17.704 29.980 8.731 1.00 42.53 C ANISOU 923 C ILE A 203 5657 5362 5141 343 -490 -348 C ATOM 924 O ILE A 203 18.086 31.038 9.278 1.00 41.31 O ANISOU 924 O ILE A 203 5519 5148 5027 313 -549 -261 O ATOM 925 CB ILE A 203 19.458 28.349 8.007 1.00 37.35 C ANISOU 925 CB ILE A 203 4882 4652 4656 427 -434 -329 C ATOM 926 CG1 ILE A 203 20.336 27.191 8.472 1.00 38.68 C ANISOU 926 CG1 ILE A 203 5042 4698 4957 462 -470 -318 C ATOM 927 CG2 ILE A 203 20.328 29.579 7.782 1.00 30.93 C ANISOU 927 CG2 ILE A 203 3981 3876 3895 428 -441 -195 C ATOM 928 CD1 ILE A 203 21.029 27.476 9.760 1.00 35.38 C ANISOU 928 CD1 ILE A 203 4638 4183 4621 412 -609 -198 C ATOM 929 N GLY A 204 16.704 29.931 7.850 1.00 33.79 N ANISOU 929 N GLY A 204 4534 4391 3914 389 -423 -440 N ATOM 930 CA GLY A 204 15.854 31.083 7.607 1.00 36.51 C ANISOU 930 CA GLY A 204 4886 4820 4164 436 -427 -433 C ATOM 931 C GLY A 204 15.340 31.688 8.907 1.00 39.49 C ANISOU 931 C GLY A 204 5344 5117 4544 379 -496 -448 C ATOM 932 O GLY A 204 15.323 32.905 9.074 1.00 45.06 O ANISOU 932 O GLY A 204 6082 5776 5262 416 -525 -388 O ATOM 933 N HIS A 205 14.934 30.841 9.845 1.00 41.22 N ANISOU 933 N HIS A 205 5610 5308 4746 285 -513 -529 N ATOM 934 CA HIS A 205 14.505 31.330 11.154 1.00 40.62 C ANISOU 934 CA HIS A 205 5611 5182 4639 220 -563 -554 C ATOM 935 C HIS A 205 15.647 31.947 11.958 1.00 36.38 C ANISOU 935 C HIS A 205 5128 4499 4196 178 -650 -449 C ATOM 936 O HIS A 205 15.453 32.970 12.600 1.00 50.65 O ANISOU 936 O HIS A 205 6990 6266 5988 172 -689 -467 O ATOM 937 CB HIS A 205 13.852 30.208 11.950 1.00 39.80 C ANISOU 937 CB HIS A 205 5553 5096 4471 102 -544 -638 C ATOM 938 CG HIS A 205 12.464 29.901 11.504 1.00 33.79 C ANISOU 938 CG HIS A 205 4729 4507 3604 96 -469 -780 C ATOM 939 ND1 HIS A 205 11.552 30.887 11.202 1.00 38.51 N ANISOU 939 ND1 HIS A 205 5260 5242 4130 196 -455 -847 N ATOM 940 CD2 HIS A 205 11.832 28.725 11.279 1.00 43.08 C ANISOU 940 CD2 HIS A 205 5884 5744 4741 2 -410 -876 C ATOM 941 CE1 HIS A 205 10.414 30.331 10.829 1.00 45.36 C ANISOU 941 CE1 HIS A 205 6038 6288 4909 166 -399 -981 C ATOM 942 NE2 HIS A 205 10.559 29.019 10.866 1.00 43.60 N ANISOU 942 NE2 HIS A 205 5844 6017 4705 27 -367 -1007 N ATOM 943 N SER A 206 16.832 31.351 11.889 1.00 30.61 N ANISOU 943 N SER A 206 4367 3698 3566 156 -683 -359 N ATOM 944 CA SER A 206 18.016 31.880 12.565 1.00 33.69 C ANISOU 944 CA SER A 206 4759 3989 4051 105 -782 -265 C ATOM 945 C SER A 206 18.461 33.241 12.048 1.00 41.17 C ANISOU 945 C SER A 206 5676 4901 5066 125 -780 -206 C ATOM 946 O SER A 206 19.217 33.943 12.725 1.00 50.37 O ANISOU 946 O SER A 206 6855 5982 6299 47 -866 -166 O ATOM 947 CB SER A 206 19.189 30.921 12.423 1.00 23.73 C ANISOU 947 CB SER A 206 3423 2696 2897 116 -812 -183 C ATOM 948 OG SER A 206 18.801 29.635 12.793 1.00 34.76 O ANISOU 948 OG SER A 206 4879 4075 4254 106 -807 -217 O ATOM 949 N LEU A 207 18.044 33.588 10.834 1.00 28.65 N ANISOU 949 N LEU A 207 4051 3378 3458 217 -687 -193 N ATOM 950 CA LEU A 207 18.456 34.848 10.226 1.00 34.40 C ANISOU 950 CA LEU A 207 4775 4050 4247 234 -668 -97 C ATOM 951 C LEU A 207 17.374 35.892 10.447 1.00 35.64 C ANISOU 951 C LEU A 207 5038 4162 4342 292 -673 -154 C ATOM 952 O LEU A 207 17.615 37.091 10.321 1.00 45.79 O ANISOU 952 O LEU A 207 6382 5323 5693 291 -681 -85 O ATOM 953 CB LEU A 207 18.759 34.663 8.735 1.00 42.79 C ANISOU 953 CB LEU A 207 5742 5216 5299 311 -564 -13 C ATOM 954 CG LEU A 207 19.833 33.587 8.502 1.00 47.13 C ANISOU 954 CG LEU A 207 6171 5816 5922 288 -542 12 C ATOM 955 CD1 LEU A 207 20.111 33.318 6.997 1.00 33.61 C ANISOU 955 CD1 LEU A 207 4361 4243 4166 370 -414 58 C ATOM 956 CD2 LEU A 207 21.132 33.892 9.290 1.00 32.25 C ANISOU 956 CD2 LEU A 207 4231 3836 4187 175 -626 87 C ATOM 957 N GLY A 208 16.182 35.430 10.802 1.00 31.20 N ANISOU 957 N GLY A 208 4171 3728 3955 -603 900 -1313 N ATOM 958 CA GLY A 208 15.145 36.327 11.273 1.00 32.81 C ANISOU 958 CA GLY A 208 4351 3754 4362 -624 1122 -1573 C ATOM 959 C GLY A 208 13.857 36.282 10.486 1.00 33.19 C ANISOU 959 C GLY A 208 4212 3642 4757 -351 1099 -1647 C ATOM 960 O GLY A 208 12.997 37.135 10.676 1.00 36.90 O ANISOU 960 O GLY A 208 4617 3925 5477 -299 1280 -1822 O ATOM 961 N LEU A 209 13.730 35.292 9.608 1.00 31.78 N ANISOU 961 N LEU A 209 3937 3533 4604 -190 887 -1511 N ATOM 962 CA LEU A 209 12.537 35.122 8.794 1.00 32.31 C ANISOU 962 CA LEU A 209 3817 3507 4953 21 817 -1537 C ATOM 963 C LEU A 209 11.385 34.440 9.542 1.00 36.92 C ANISOU 963 C LEU A 209 4272 4101 5654 -53 951 -1667 C ATOM 964 O LEU A 209 11.583 33.515 10.325 1.00 39.90 O ANISOU 964 O LEU A 209 4690 4609 5862 -230 984 -1665 O ATOM 965 CB LEU A 209 12.879 34.329 7.527 1.00 30.86 C ANISOU 965 CB LEU A 209 3608 3415 4704 169 544 -1375 C ATOM 966 CG LEU A 209 13.731 35.104 6.509 1.00 34.03 C ANISOU 966 CG LEU A 209 4065 3824 5039 283 396 -1233 C ATOM 967 CD1 LEU A 209 14.277 34.184 5.462 1.00 32.65 C ANISOU 967 CD1 LEU A 209 3903 3791 4710 369 185 -1118 C ATOM 968 CD2 LEU A 209 12.952 36.224 5.836 1.00 31.85 C ANISOU 968 CD2 LEU A 209 3653 3401 5046 429 375 -1213 C ATOM 969 N PHE A 210 10.175 34.915 9.290 1.00 36.79 N ANISOU 969 N PHE A 210 4073 3956 5949 81 1023 -1742 N ATOM 970 CA PHE A 210 8.974 34.259 9.781 1.00 40.91 C ANISOU 970 CA PHE A 210 4424 4505 6613 43 1118 -1826 C ATOM 971 C PHE A 210 8.386 33.378 8.683 1.00 40.55 C ANISOU 971 C PHE A 210 4238 4508 6660 170 858 -1695 C ATOM 972 O PHE A 210 8.885 33.374 7.552 1.00 57.72 O ANISOU 972 O PHE A 210 6450 6697 8782 285 632 -1568 O ATOM 973 CB PHE A 210 7.959 35.299 10.251 1.00 50.14 C ANISOU 973 CB PHE A 210 5446 5511 8094 105 1393 -1983 C ATOM 974 CG PHE A 210 8.417 36.106 11.438 1.00 61.84 C ANISOU 974 CG PHE A 210 7085 6943 9467 -77 1700 -2191 C ATOM 975 CD1 PHE A 210 8.483 35.532 12.701 1.00 73.56 C ANISOU 975 CD1 PHE A 210 8642 8599 10709 -357 1874 -2318 C ATOM 976 CD2 PHE A 210 8.766 37.440 11.298 1.00 59.55 C ANISOU 976 CD2 PHE A 210 6872 6442 9311 -3 1813 -2256 C ATOM 977 CE1 PHE A 210 8.896 36.277 13.808 1.00 68.86 C ANISOU 977 CE1 PHE A 210 8205 8002 9958 -588 2163 -2532 C ATOM 978 CE2 PHE A 210 9.175 38.189 12.395 1.00 56.74 C ANISOU 978 CE2 PHE A 210 6689 6031 8839 -215 2111 -2491 C ATOM 979 CZ PHE A 210 9.238 37.598 13.652 1.00 63.42 C ANISOU 979 CZ PHE A 210 7617 7086 9392 -522 2289 -2642 C ATOM 980 N HIS A 211 7.340 32.624 9.006 1.00 36.67 N ANISOU 980 N HIS A 211 3590 4064 6280 119 887 -1728 N ATOM 981 CA HIS A 211 6.718 31.721 8.023 1.00 46.10 C ANISOU 981 CA HIS A 211 4661 5312 7541 178 638 -1622 C ATOM 982 C HIS A 211 6.052 32.471 6.870 1.00 52.81 C ANISOU 982 C HIS A 211 5328 6107 8629 364 510 -1513 C ATOM 983 O HIS A 211 5.600 33.614 7.010 1.00 51.59 O ANISOU 983 O HIS A 211 5045 5834 8722 473 663 -1517 O ATOM 984 CB HIS A 211 5.693 30.785 8.687 1.00 37.75 C ANISOU 984 CB HIS A 211 3460 4322 6562 49 693 -1659 C ATOM 985 CG HIS A 211 6.319 29.693 9.503 1.00 39.46 C ANISOU 985 CG HIS A 211 3822 4620 6550 -151 703 -1671 C ATOM 986 ND1 HIS A 211 5.635 29.003 10.477 1.00 45.56 N ANISOU 986 ND1 HIS A 211 4495 5472 7344 -326 811 -1698 N ATOM 987 CD2 HIS A 211 7.571 29.171 9.487 1.00 34.93 C ANISOU 987 CD2 HIS A 211 3456 4068 5748 -206 616 -1617 C ATOM 988 CE1 HIS A 211 6.437 28.104 11.022 1.00 38.43 C ANISOU 988 CE1 HIS A 211 3730 4627 6244 -488 771 -1640 C ATOM 989 NE2 HIS A 211 7.615 28.187 10.438 1.00 35.09 N ANISOU 989 NE2 HIS A 211 3488 4161 5685 -406 660 -1588 N ATOM 990 N SER A 212 6.023 31.818 5.716 1.00 50.17 N ANISOU 990 N SER A 212 4979 5861 8223 383 232 -1407 N ATOM 991 CA SER A 212 5.397 32.397 4.544 1.00 41.79 C ANISOU 991 CA SER A 212 3723 4820 7335 500 56 -1246 C ATOM 992 C SER A 212 4.053 31.759 4.300 1.00 40.85 C ANISOU 992 C SER A 212 3360 4779 7381 444 -42 -1182 C ATOM 993 O SER A 212 3.875 30.562 4.504 1.00 46.03 O ANISOU 993 O SER A 212 4073 5502 7915 301 -100 -1253 O ATOM 994 CB SER A 212 6.276 32.228 3.315 1.00 43.91 C ANISOU 994 CB SER A 212 4129 5193 7363 515 -194 -1164 C ATOM 995 OG SER A 212 5.632 32.803 2.199 1.00 54.32 O ANISOU 995 OG SER A 212 5233 6582 8825 580 -384 -967 O ATOM 996 N ALA A 213 3.098 32.552 3.845 1.00 43.17 N ANISOU 996 N ALA A 213 3365 5060 7977 548 -71 -1014 N ATOM 997 CA ALA A 213 1.790 32.000 3.524 1.00 56.40 C ANISOU 997 CA ALA A 213 4768 6847 9814 478 -195 -893 C ATOM 998 C ALA A 213 1.829 31.378 2.137 1.00 64.72 C ANISOU 998 C ALA A 213 5841 8090 10659 367 -555 -772 C ATOM 999 O ALA A 213 0.866 30.743 1.710 1.00 68.81 O ANISOU 999 O ALA A 213 6180 8743 11221 239 -723 -673 O ATOM 1000 CB ALA A 213 0.718 33.066 3.607 1.00 48.26 C ANISOU 1000 CB ALA A 213 3371 5737 9227 633 -75 -718 C ATOM 1001 N ASN A 214 2.961 31.563 1.454 1.00 60.35 N ANISOU 1001 N ASN A 214 5508 7566 9858 391 -663 -788 N ATOM 1002 CA ASN A 214 3.158 31.078 0.094 1.00 52.94 C ANISOU 1002 CA ASN A 214 4619 6831 8664 270 -968 -715 C ATOM 1003 C ASN A 214 3.774 29.673 0.034 1.00 57.52 C ANISOU 1003 C ASN A 214 5491 7445 8921 113 -1016 -955 C ATOM 1004 O ASN A 214 4.904 29.440 0.485 1.00 57.45 O ANISOU 1004 O ASN A 214 5742 7337 8748 160 -887 -1114 O ATOM 1005 CB ASN A 214 4.020 32.071 -0.680 1.00 52.32 C ANISOU 1005 CB ASN A 214 4589 6793 8497 376 -1048 -586 C ATOM 1006 CG ASN A 214 4.278 31.633 -2.108 1.00 66.03 C ANISOU 1006 CG ASN A 214 6377 8793 9917 224 -1343 -523 C ATOM 1007 OD1 ASN A 214 3.617 30.731 -2.622 1.00 67.49 O ANISOU 1007 OD1 ASN A 214 6519 9130 9995 30 -1506 -548 O ATOM 1008 ND2 ASN A 214 5.243 32.278 -2.762 1.00 73.98 N ANISOU 1008 ND2 ASN A 214 7481 9873 10755 282 -1407 -448 N ATOM 1009 N THR A 215 3.015 28.750 -0.551 1.00 44.93 N ANISOU 1009 N THR A 215 3835 5980 7258 -83 -1204 -959 N ATOM 1010 CA THR A 215 3.405 27.357 -0.686 1.00 44.55 C ANISOU 1010 CA THR A 215 4036 5917 6974 -249 -1249 -1192 C ATOM 1011 C THR A 215 4.638 27.145 -1.585 1.00 55.02 C ANISOU 1011 C THR A 215 5625 7304 7974 -252 -1311 -1320 C ATOM 1012 O THR A 215 5.289 26.096 -1.538 1.00 50.85 O ANISOU 1012 O THR A 215 5342 6684 7296 -314 -1260 -1543 O ATOM 1013 CB THR A 215 2.224 26.546 -1.235 1.00 57.66 C ANISOU 1013 CB THR A 215 5559 7712 8639 -497 -1457 -1159 C ATOM 1014 OG1 THR A 215 1.823 27.058 -2.517 1.00 64.10 O ANISOU 1014 OG1 THR A 215 6216 8784 9354 -593 -1706 -970 O ATOM 1015 CG2 THR A 215 1.044 26.615 -0.270 1.00 48.17 C ANISOU 1015 CG2 THR A 215 4088 6458 7756 -497 -1370 -1037 C ATOM 1016 N GLU A 216 4.955 28.149 -2.398 1.00 63.06 N ANISOU 1016 N GLU A 216 6575 8474 8911 -180 -1408 -1162 N ATOM 1017 CA GLU A 216 6.163 28.146 -3.224 1.00 61.30 C ANISOU 1017 CA GLU A 216 6565 8349 8375 -165 -1441 -1251 C ATOM 1018 C GLU A 216 7.423 28.430 -2.402 1.00 56.65 C ANISOU 1018 C GLU A 216 6161 7582 7780 34 -1216 -1324 C ATOM 1019 O GLU A 216 8.537 28.117 -2.823 1.00 51.42 O ANISOU 1019 O GLU A 216 5704 6953 6880 59 -1182 -1442 O ATOM 1020 CB GLU A 216 6.054 29.191 -4.343 1.00 69.67 C ANISOU 1020 CB GLU A 216 7453 9666 9351 -182 -1642 -996 C ATOM 1021 CG GLU A 216 4.713 29.216 -5.083 1.00 92.32 C ANISOU 1021 CG GLU A 216 10047 12755 12276 -383 -1892 -795 C ATOM 1022 CD GLU A 216 4.482 28.009 -5.989 1.00104.79 C ANISOU 1022 CD GLU A 216 11754 14524 13537 -690 -2053 -993 C ATOM 1023 OE1 GLU A 216 4.446 28.193 -7.228 1.00110.31 O ANISOU 1023 OE1 GLU A 216 12401 15546 13967 -879 -2272 -891 O ATOM 1024 OE2 GLU A 216 4.314 26.884 -5.466 1.00104.27 O ANISOU 1024 OE2 GLU A 216 11839 14292 13488 -771 -1963 -1246 O ATOM 1025 N ALA A 217 7.244 29.037 -1.233 1.00 53.80 N ANISOU 1025 N ALA A 217 5717 7052 7671 158 -1052 -1251 N ATOM 1026 CA ALA A 217 8.381 29.502 -0.455 1.00 44.34 C ANISOU 1026 CA ALA A 217 4666 5730 6450 298 -863 -1272 C ATOM 1027 C ALA A 217 8.999 28.407 0.391 1.00 42.82 C ANISOU 1027 C ALA A 217 4666 5401 6203 269 -715 -1445 C ATOM 1028 O ALA A 217 8.337 27.471 0.824 1.00 46.85 O ANISOU 1028 O ALA A 217 5158 5837 6805 165 -702 -1533 O ATOM 1029 CB ALA A 217 7.980 30.654 0.418 1.00 44.64 C ANISOU 1029 CB ALA A 217 4557 5654 6752 402 -730 -1152 C ATOM 1030 N LEU A 218 10.293 28.539 0.618 1.00 46.52 N ANISOU 1030 N LEU A 218 5297 5842 6536 352 -616 -1452 N ATOM 1031 CA LEU A 218 10.967 27.703 1.576 1.00 40.00 C ANISOU 1031 CA LEU A 218 4604 4886 5706 337 -468 -1523 C ATOM 1032 C LEU A 218 10.389 27.971 2.970 1.00 39.01 C ANISOU 1032 C LEU A 218 4392 4666 5766 291 -328 -1488 C ATOM 1033 O LEU A 218 10.255 27.070 3.777 1.00 41.44 O ANISOU 1033 O LEU A 218 4720 4890 6136 202 -256 -1529 O ATOM 1034 CB LEU A 218 12.458 27.972 1.527 1.00 31.72 C ANISOU 1034 CB LEU A 218 3697 3870 4486 431 -401 -1470 C ATOM 1035 CG LEU A 218 13.330 27.187 2.494 1.00 42.08 C ANISOU 1035 CG LEU A 218 5112 5076 5802 418 -261 -1459 C ATOM 1036 CD1 LEU A 218 13.163 25.676 2.331 1.00 32.73 C ANISOU 1036 CD1 LEU A 218 3978 3773 4684 366 -268 -1586 C ATOM 1037 CD2 LEU A 218 14.774 27.596 2.278 1.00 37.65 C ANISOU 1037 CD2 LEU A 218 4644 4592 5069 514 -220 -1357 C ATOM 1038 N MET A 219 10.003 29.207 3.246 1.00 35.04 N ANISOU 1038 N MET A 219 3779 4171 5364 340 -277 -1413 N ATOM 1039 CA MET A 219 9.546 29.533 4.590 1.00 40.93 C ANISOU 1039 CA MET A 219 4460 4841 6252 285 -91 -1428 C ATOM 1040 C MET A 219 8.067 29.171 4.802 1.00 49.00 C ANISOU 1040 C MET A 219 5288 5849 7480 219 -97 -1459 C ATOM 1041 O MET A 219 7.411 29.624 5.746 1.00 43.26 O ANISOU 1041 O MET A 219 4447 5084 6905 190 70 -1479 O ATOM 1042 CB MET A 219 9.803 31.014 4.889 1.00 34.90 C ANISOU 1042 CB MET A 219 3679 4042 5538 360 22 -1380 C ATOM 1043 CG MET A 219 11.278 31.337 4.970 1.00 31.98 C ANISOU 1043 CG MET A 219 3498 3700 4954 373 47 -1330 C ATOM 1044 SD MET A 219 12.185 30.136 5.967 1.00 47.44 S ANISOU 1044 SD MET A 219 5601 5681 6745 236 131 -1336 S ATOM 1045 CE MET A 219 11.724 30.684 7.610 1.00 48.89 C ANISOU 1045 CE MET A 219 5749 5835 6993 73 373 -1398 C ATOM 1046 N TYR A 220 7.536 28.345 3.919 1.00 48.67 N ANISOU 1046 N TYR A 220 5206 5853 7434 176 -279 -1472 N ATOM 1047 CA TYR A 220 6.258 27.733 4.196 1.00 47.32 C ANISOU 1047 CA TYR A 220 4869 5684 7426 68 -302 -1484 C ATOM 1048 C TYR A 220 6.542 26.615 5.210 1.00 54.92 C ANISOU 1048 C TYR A 220 5935 6578 8355 -60 -209 -1546 C ATOM 1049 O TYR A 220 7.544 25.906 5.099 1.00 61.18 O ANISOU 1049 O TYR A 220 6913 7320 9013 -70 -231 -1577 O ATOM 1050 CB TYR A 220 5.619 27.220 2.909 1.00 42.93 C ANISOU 1050 CB TYR A 220 4249 5218 6846 7 -546 -1470 C ATOM 1051 CG TYR A 220 4.181 26.777 3.046 1.00 48.25 C ANISOU 1051 CG TYR A 220 4704 5930 7700 -117 -608 -1429 C ATOM 1052 CD1 TYR A 220 3.168 27.692 3.339 1.00 50.51 C ANISOU 1052 CD1 TYR A 220 4713 6252 8225 -55 -543 -1303 C ATOM 1053 CD2 TYR A 220 3.831 25.445 2.858 1.00 46.61 C ANISOU 1053 CD2 TYR A 220 4552 5708 7449 -296 -725 -1508 C ATOM 1054 CE1 TYR A 220 1.845 27.284 3.456 1.00 51.40 C ANISOU 1054 CE1 TYR A 220 4590 6429 8512 -167 -599 -1230 C ATOM 1055 CE2 TYR A 220 2.516 25.029 2.969 1.00 54.43 C ANISOU 1055 CE2 TYR A 220 5334 6756 8593 -438 -802 -1445 C ATOM 1056 CZ TYR A 220 1.527 25.949 3.266 1.00 54.67 C ANISOU 1056 CZ TYR A 220 5069 6864 8841 -372 -743 -1293 C ATOM 1057 OH TYR A 220 0.227 25.514 3.372 1.00 53.75 O ANISOU 1057 OH TYR A 220 4715 6829 8881 -513 -819 -1199 O ATOM 1058 N PRO A 221 5.684 26.483 6.231 1.00 49.27 N ANISOU 1058 N PRO A 221 5077 5865 7780 -158 -91 -1538 N ATOM 1059 CA PRO A 221 5.959 25.586 7.359 1.00 49.49 C ANISOU 1059 CA PRO A 221 5166 5861 7776 -306 7 -1539 C ATOM 1060 C PRO A 221 5.663 24.102 7.119 1.00 51.72 C ANISOU 1060 C PRO A 221 5474 6078 8098 -441 -140 -1543 C ATOM 1061 O PRO A 221 6.126 23.284 7.923 1.00 51.96 O ANISOU 1061 O PRO A 221 5571 6055 8117 -552 -89 -1497 O ATOM 1062 CB PRO A 221 5.054 26.138 8.461 1.00 37.67 C ANISOU 1062 CB PRO A 221 3482 4433 6398 -374 201 -1537 C ATOM 1063 CG PRO A 221 3.936 26.757 7.741 1.00 42.18 C ANISOU 1063 CG PRO A 221 3846 5033 7148 -279 143 -1521 C ATOM 1064 CD PRO A 221 4.515 27.340 6.487 1.00 47.26 C ANISOU 1064 CD PRO A 221 4576 5655 7727 -122 -4 -1503 C ATOM 1065 N LEU A 222 4.916 23.749 6.070 1.00 44.65 N ANISOU 1065 N LEU A 222 4522 5188 7253 -461 -322 -1578 N ATOM 1066 CA LEU A 222 4.792 22.336 5.711 1.00 40.07 C ANISOU 1066 CA LEU A 222 4025 4502 6699 -603 -460 -1628 C ATOM 1067 C LEU A 222 6.050 21.878 4.959 1.00 45.87 C ANISOU 1067 C LEU A 222 5003 5119 7306 -520 -497 -1721 C ATOM 1068 O LEU A 222 6.673 22.651 4.218 1.00 42.10 O ANISOU 1068 O LEU A 222 4595 4707 6693 -376 -507 -1752 O ATOM 1069 CB LEU A 222 3.546 22.091 4.884 1.00 47.15 C ANISOU 1069 CB LEU A 222 4785 5469 7661 -714 -643 -1642 C ATOM 1070 CG LEU A 222 2.246 22.585 5.534 1.00 57.09 C ANISOU 1070 CG LEU A 222 5753 6859 9080 -768 -594 -1524 C ATOM 1071 CD1 LEU A 222 1.039 22.119 4.752 1.00 53.40 C ANISOU 1071 CD1 LEU A 222 5135 6474 8681 -926 -807 -1489 C ATOM 1072 CD2 LEU A 222 2.156 22.144 6.983 1.00 64.54 C ANISOU 1072 CD2 LEU A 222 6645 7778 10100 -872 -432 -1471 C ATOM 1073 N TYR A 223 6.457 20.636 5.180 1.00 49.56 N ANISOU 1073 N TYR A 223 5583 5405 7840 -605 -501 -1749 N ATOM 1074 CA TYR A 223 7.669 20.129 4.538 1.00 53.12 C ANISOU 1074 CA TYR A 223 6244 5714 8226 -504 -485 -1842 C ATOM 1075 C TYR A 223 7.365 19.751 3.090 1.00 57.80 C ANISOU 1075 C TYR A 223 6930 6295 8735 -546 -624 -2050 C ATOM 1076 O TYR A 223 6.440 18.977 2.833 1.00 48.17 O ANISOU 1076 O TYR A 223 5688 5017 7599 -732 -738 -2126 O ATOM 1077 CB TYR A 223 8.221 18.942 5.320 1.00 49.62 C ANISOU 1077 CB TYR A 223 5858 5043 7952 -564 -417 -1768 C ATOM 1078 CG TYR A 223 9.197 18.074 4.575 1.00 47.55 C ANISOU 1078 CG TYR A 223 5782 4554 7730 -478 -390 -1895 C ATOM 1079 CD1 TYR A 223 8.831 16.798 4.161 1.00 50.19 C ANISOU 1079 CD1 TYR A 223 6197 4640 8234 -601 -446 -2038 C ATOM 1080 CD2 TYR A 223 10.486 18.512 4.295 1.00 46.37 C ANISOU 1080 CD2 TYR A 223 5724 4425 7469 -280 -289 -1879 C ATOM 1081 CE1 TYR A 223 9.714 15.982 3.481 1.00 46.06 C ANISOU 1081 CE1 TYR A 223 5848 3866 7788 -511 -371 -2198 C ATOM 1082 CE2 TYR A 223 11.383 17.699 3.614 1.00 46.13 C ANISOU 1082 CE2 TYR A 223 5842 4182 7505 -180 -220 -2006 C ATOM 1083 CZ TYR A 223 10.985 16.428 3.215 1.00 44.91 C ANISOU 1083 CZ TYR A 223 5771 3752 7542 -288 -245 -2182 C ATOM 1084 OH TYR A 223 11.849 15.600 2.545 1.00 46.98 O ANISOU 1084 OH TYR A 223 6182 3758 7909 -181 -129 -2351 O ATOM 1085 N HIS A 224 8.109 20.335 2.151 1.00 60.87 N ANISOU 1085 N HIS A 224 7419 6775 8933 -411 -623 -2132 N ATOM 1086 CA HIS A 224 7.858 20.103 0.723 1.00 72.90 C ANISOU 1086 CA HIS A 224 9031 8368 10301 -492 -752 -2333 C ATOM 1087 C HIS A 224 8.349 18.720 0.319 1.00 64.05 C ANISOU 1087 C HIS A 224 8113 6985 9238 -553 -701 -2559 C ATOM 1088 O HIS A 224 9.455 18.580 -0.184 1.00 46.55 O ANISOU 1088 O HIS A 224 6045 4707 6937 -420 -591 -2672 O ATOM 1089 CB HIS A 224 8.540 21.170 -0.150 1.00 81.82 C ANISOU 1089 CB HIS A 224 10190 9712 11188 -350 -762 -2330 C ATOM 1090 CG HIS A 224 8.005 22.557 0.043 1.00 86.85 C ANISOU 1090 CG HIS A 224 10629 10563 11809 -292 -819 -2124 C ATOM 1091 ND1 HIS A 224 8.425 23.385 1.065 1.00 88.98 N ANISOU 1091 ND1 HIS A 224 10832 10822 12153 -149 -689 -1958 N ATOM 1092 CD2 HIS A 224 7.090 23.267 -0.662 1.00 84.90 C ANISOU 1092 CD2 HIS A 224 10225 10529 11504 -365 -983 -2049 C ATOM 1093 CE1 HIS A 224 7.790 24.541 0.981 1.00 85.41 C ANISOU 1093 CE1 HIS A 224 10208 10523 11721 -115 -744 -1827 C ATOM 1094 NE2 HIS A 224 6.971 24.494 -0.056 1.00 82.24 N ANISOU 1094 NE2 HIS A 224 9727 10257 11261 -230 -929 -1849 N ATOM 1095 N SER A 225 7.522 17.703 0.527 1.00 82.02 N ANISOU 1095 N SER A 225 10388 9094 11682 -756 -768 -2625 N ATOM 1096 CA SER A 225 7.985 16.325 0.422 1.00 89.41 C ANISOU 1096 CA SER A 225 11505 9683 12784 -804 -683 -2813 C ATOM 1097 C SER A 225 8.406 15.955 -0.998 1.00 92.04 C ANISOU 1097 C SER A 225 12050 9997 12923 -841 -664 -3156 C ATOM 1098 O SER A 225 9.089 14.953 -1.203 1.00 89.80 O ANISOU 1098 O SER A 225 11940 9401 12779 -807 -520 -3356 O ATOM 1099 CB SER A 225 6.900 15.370 0.920 1.00 93.21 C ANISOU 1099 CB SER A 225 11932 9996 13487 -1053 -786 -2796 C ATOM 1100 OG SER A 225 5.837 15.290 -0.004 1.00104.98 O ANISOU 1100 OG SER A 225 13426 11635 14825 -1302 -973 -2951 O ATOM 1101 N LEU A 226 8.032 16.785 -1.967 1.00 96.52 N ANISOU 1101 N LEU A 226 12591 10905 13178 -911 -794 -3212 N ATOM 1102 CA LEU A 226 8.169 16.415 -3.371 1.00106.67 C ANISOU 1102 CA LEU A 226 14064 12257 14208 -1054 -811 -3552 C ATOM 1103 C LEU A 226 9.157 17.215 -4.197 1.00102.03 C ANISOU 1103 C LEU A 226 13533 11907 13326 -889 -734 -3606 C ATOM 1104 O LEU A 226 9.153 17.103 -5.425 1.00118.70 O ANISOU 1104 O LEU A 226 15769 14192 15141 -1049 -771 -3846 O ATOM 1105 CB LEU A 226 6.824 16.515 -4.071 1.00110.00 C ANISOU 1105 CB LEU A 226 14412 12936 14448 -1388 -1071 -3585 C ATOM 1106 CG LEU A 226 5.729 15.561 -3.650 1.00108.23 C ANISOU 1106 CG LEU A 226 14165 12522 14434 -1654 -1183 -3608 C ATOM 1107 CD1 LEU A 226 4.528 15.942 -4.460 1.00103.31 C ANISOU 1107 CD1 LEU A 226 13422 12262 13568 -1966 -1456 -3569 C ATOM 1108 CD2 LEU A 226 6.183 14.146 -3.940 1.00110.14 C ANISOU 1108 CD2 LEU A 226 14702 12397 14748 -1704 -1020 -3826 C ATOM 1109 N THR A 227 9.980 18.032 -3.558 1.00 73.75 N ANISOU 1109 N THR A 227 9861 8371 9789 -607 -636 -3362 N ATOM 1110 CA THR A 227 11.044 18.688 -4.296 1.00 71.32 C ANISOU 1110 CA THR A 227 9612 8262 9226 -447 -547 -3401 C ATOM 1111 C THR A 227 11.984 17.607 -4.846 1.00 87.28 C ANISOU 1111 C THR A 227 11857 10039 11267 -396 -317 -3739 C ATOM 1112 O THR A 227 12.295 16.644 -4.145 1.00 91.03 O ANISOU 1112 O THR A 227 12389 10140 12059 -313 -165 -3723 O ATOM 1113 CB THR A 227 11.798 19.685 -3.405 1.00 69.20 C ANISOU 1113 CB THR A 227 9217 8049 9029 -180 -478 -3070 C ATOM 1114 OG1 THR A 227 10.856 20.563 -2.781 1.00 72.09 O ANISOU 1114 OG1 THR A 227 9386 8557 9450 -227 -636 -2809 O ATOM 1115 CG2 THR A 227 12.762 20.519 -4.209 1.00 63.12 C ANISOU 1115 CG2 THR A 227 8471 7539 7972 -49 -436 -3056 C ATOM 1116 N ASP A 228 12.402 17.742 -6.104 1.00100.26 N ANISOU 1116 N ASP A 228 13614 11913 12566 -447 -278 -3904 N ATOM 1117 CA ASP A 228 13.296 16.757 -6.720 1.00115.13 C ANISOU 1117 CA ASP A 228 15707 13595 14440 -375 -21 -4105 C ATOM 1118 C ASP A 228 14.762 17.084 -6.426 1.00110.29 C ANISOU 1118 C ASP A 228 15064 12947 13896 -38 204 -3993 C ATOM 1119 O ASP A 228 15.638 16.233 -6.624 1.00118.00 O ANISOU 1119 O ASP A 228 16159 13685 14991 101 452 -4099 O ATOM 1120 CB ASP A 228 13.078 16.695 -8.231 1.00122.38 C ANISOU 1120 CB ASP A 228 16765 14794 14942 -609 -68 -4342 C ATOM 1121 CG ASP A 228 13.615 17.924 -8.942 1.00124.08 C ANISOU 1121 CG ASP A 228 16893 15464 14788 -564 -119 -4262 C ATOM 1122 OD1 ASP A 228 14.013 17.800 -10.120 1.00125.13 O ANISOU 1122 OD1 ASP A 228 17148 15792 14606 -654 -45 -4437 O ATOM 1123 OD2 ASP A 228 13.651 19.012 -8.315 1.00119.18 O ANISOU 1123 OD2 ASP A 228 16078 15010 14195 -438 -238 -4021 O ATOM 1124 N LEU A 229 14.996 18.332 -5.996 1.00 91.59 N ANISOU 1124 N LEU A 229 12524 10826 11448 86 104 -3775 N ATOM 1125 CA LEU A 229 16.296 18.861 -5.539 1.00 79.47 C ANISOU 1125 CA LEU A 229 10916 9312 9969 387 258 -3589 C ATOM 1126 C LEU A 229 17.222 19.244 -6.674 1.00 79.24 C ANISOU 1126 C LEU A 229 10942 9566 9599 451 370 -3687 C ATOM 1127 O LEU A 229 18.030 20.155 -6.548 1.00 73.28 O ANISOU 1127 O LEU A 229 10087 9021 8736 620 382 -3463 O ATOM 1128 CB LEU A 229 17.030 17.865 -4.642 1.00 74.51 C ANISOU 1128 CB LEU A 229 10300 8253 9758 578 485 -3509 C ATOM 1129 CG LEU A 229 16.456 17.559 -3.271 1.00 62.54 C ANISOU 1129 CG LEU A 229 8685 6475 8604 558 407 -3293 C ATOM 1130 CD1 LEU A 229 17.285 16.447 -2.632 1.00 63.02 C ANISOU 1130 CD1 LEU A 229 8751 6123 9069 727 637 -3224 C ATOM 1131 CD2 LEU A 229 16.436 18.826 -2.415 1.00 48.69 C ANISOU 1131 CD2 LEU A 229 6763 4967 6771 605 262 -2890 C ATOM 1132 N THR A 230 17.125 18.507 -7.767 1.00 86.70 N ANISOU 1132 N THR A 230 12053 10515 10374 299 455 -3954 N ATOM 1133 CA THR A 230 17.925 18.771 -8.946 1.00 87.55 C ANISOU 1133 CA THR A 230 12223 10912 10131 311 571 -4068 C ATOM 1134 C THR A 230 17.770 20.223 -9.388 1.00 95.23 C ANISOU 1134 C THR A 230 13056 12395 10730 230 337 -3907 C ATOM 1135 O THR A 230 18.761 20.918 -9.607 1.00 94.05 O ANISOU 1135 O THR A 230 12838 12478 10419 390 412 -3783 O ATOM 1136 CB THR A 230 17.524 17.830 -10.084 1.00 82.06 C ANISOU 1136 CB THR A 230 11731 10186 9260 80 630 -4401 C ATOM 1137 OG1 THR A 230 17.680 16.472 -9.643 1.00 81.21 O ANISOU 1137 OG1 THR A 230 11745 9581 9531 179 832 -4536 O ATOM 1138 CG2 THR A 230 18.371 18.090 -11.320 1.00 79.83 C ANISOU 1138 CG2 THR A 230 11507 10224 8601 78 765 -4525 C ATOM 1139 N ARG A 231 16.522 20.681 -9.479 1.00 99.82 N ANISOU 1139 N ARG A 231 13574 13153 11200 -12 42 -3868 N ATOM 1140 CA ARG A 231 16.223 22.018 -9.985 1.00 96.69 C ANISOU 1140 CA ARG A 231 13024 13242 10471 -118 -221 -3675 C ATOM 1141 C ARG A 231 15.689 22.954 -8.895 1.00 82.03 C ANISOU 1141 C ARG A 231 10978 11322 8867 -21 -415 -3240 C ATOM 1142 O ARG A 231 14.960 23.901 -9.185 1.00 76.35 O ANISOU 1142 O ARG A 231 10113 10875 8023 -153 -671 -3010 O ATOM 1143 CB ARG A 231 15.220 21.930 -11.142 1.00102.18 C ANISOU 1143 CB ARG A 231 13753 14212 10859 -496 -416 -3771 C ATOM 1144 CG ARG A 231 15.763 21.250 -12.397 1.00108.07 C ANISOU 1144 CG ARG A 231 14683 15052 11327 -618 -234 -4019 C ATOM 1145 CD ARG A 231 14.704 21.184 -13.485 1.00114.06 C ANISOU 1145 CD ARG A 231 15461 16099 11778 -1018 -459 -4076 C ATOM 1146 NE ARG A 231 14.278 22.523 -13.891 1.00114.53 N ANISOU 1146 NE ARG A 231 15293 16632 11592 -1150 -770 -3727 N ATOM 1147 CZ ARG A 231 14.875 23.260 -14.825 1.00112.97 C ANISOU 1147 CZ ARG A 231 15032 16831 11061 -1198 -800 -3584 C ATOM 1148 NH1 ARG A 231 15.928 22.793 -15.486 1.00113.73 N ANISOU 1148 NH1 ARG A 231 15276 16946 10989 -1134 -526 -3803 N ATOM 1149 NH2 ARG A 231 14.402 24.465 -15.108 1.00110.03 N ANISOU 1149 NH2 ARG A 231 14427 16826 10553 -1309 -1103 -3192 N ATOM 1150 N PHE A 232 16.071 22.695 -7.648 1.00 77.03 N ANISOU 1150 N PHE A 232 10335 10338 8595 200 -281 -3121 N ATOM 1151 CA PHE A 232 15.680 23.563 -6.539 1.00 71.29 C ANISOU 1151 CA PHE A 232 9452 9548 8088 284 -405 -2760 C ATOM 1152 C PHE A 232 16.283 24.951 -6.630 1.00 71.48 C ANISOU 1152 C PHE A 232 9362 9836 7962 388 -482 -2450 C ATOM 1153 O PHE A 232 17.489 25.098 -6.774 1.00 75.95 O ANISOU 1153 O PHE A 232 9961 10471 8425 537 -343 -2408 O ATOM 1154 CB PHE A 232 16.085 22.963 -5.199 1.00 73.13 C ANISOU 1154 CB PHE A 232 9702 9406 8678 451 -237 -2692 C ATOM 1155 CG PHE A 232 15.871 23.901 -4.028 1.00 68.90 C ANISOU 1155 CG PHE A 232 9028 8842 8309 518 -314 -2355 C ATOM 1156 CD1 PHE A 232 14.595 24.116 -3.511 1.00 72.78 C ANISOU 1156 CD1 PHE A 232 9422 9285 8944 395 -457 -2287 C ATOM 1157 CD2 PHE A 232 16.939 24.557 -3.439 1.00 55.73 C ANISOU 1157 CD2 PHE A 232 7325 7201 6649 685 -228 -2119 C ATOM 1158 CE1 PHE A 232 14.391 24.978 -2.423 1.00 62.84 C ANISOU 1158 CE1 PHE A 232 8047 7992 7838 448 -478 -2033 C ATOM 1159 CE2 PHE A 232 16.737 25.435 -2.355 1.00 56.36 C ANISOU 1159 CE2 PHE A 232 7306 7253 6854 702 -276 -1861 C ATOM 1160 CZ PHE A 232 15.466 25.640 -1.845 1.00 52.41 C ANISOU 1160 CZ PHE A 232 6725 6689 6500 590 -382 -1841 C ATOM 1161 N ARG A 233 15.430 25.963 -6.515 1.00 66.88 N ANISOU 1161 N ARG A 233 8629 9379 7404 312 -695 -2215 N ATOM 1162 CA ARG A 233 15.852 27.358 -6.497 1.00 63.05 C ANISOU 1162 CA ARG A 233 8025 9077 6854 397 -784 -1897 C ATOM 1163 C ARG A 233 15.182 28.068 -5.316 1.00 62.19 C ANISOU 1163 C ARG A 233 7798 8781 7052 447 -833 -1678 C ATOM 1164 O ARG A 233 14.149 27.628 -4.816 1.00 57.50 O ANISOU 1164 O ARG A 233 7165 8028 6655 372 -863 -1744 O ATOM 1165 CB ARG A 233 15.505 28.062 -7.825 1.00 63.09 C ANISOU 1165 CB ARG A 233 7935 9471 6565 234 -998 -1810 C ATOM 1166 CG ARG A 233 16.549 27.922 -8.949 1.00 63.48 C ANISOU 1166 CG ARG A 233 8069 9814 6238 212 -931 -1922 C ATOM 1167 N LEU A 234 15.780 29.156 -4.852 1.00 62.60 N ANISOU 1167 N LEU A 234 7795 8849 7139 558 -825 -1432 N ATOM 1168 CA LEU A 234 15.189 29.915 -3.765 1.00 48.86 C ANISOU 1168 CA LEU A 234 5959 6933 5672 591 -830 -1270 C ATOM 1169 C LEU A 234 14.010 30.687 -4.339 1.00 51.01 C ANISOU 1169 C LEU A 234 6049 7318 6016 503 -1031 -1138 C ATOM 1170 O LEU A 234 14.107 31.237 -5.422 1.00 59.88 O ANISOU 1170 O LEU A 234 7103 8694 6955 450 -1184 -1018 O ATOM 1171 CB LEU A 234 16.237 30.836 -3.124 1.00 40.16 C ANISOU 1171 CB LEU A 234 4881 5806 4573 698 -749 -1077 C ATOM 1172 CG LEU A 234 15.961 31.399 -1.734 1.00 40.93 C ANISOU 1172 CG LEU A 234 4953 5682 4918 715 -657 -995 C ATOM 1173 CD1 LEU A 234 15.421 30.311 -0.823 1.00 38.12 C ANISOU 1173 CD1 LEU A 234 4631 5134 4719 676 -546 -1158 C ATOM 1174 CD2 LEU A 234 17.223 32.033 -1.123 1.00 41.74 C ANISOU 1174 CD2 LEU A 234 5130 5783 4947 764 -564 -846 C ATOM 1175 N SER A 235 12.890 30.698 -3.629 1.00 53.29 N ANISOU 1175 N SER A 235 6234 7440 6575 476 -1032 -1134 N ATOM 1176 CA SER A 235 11.668 31.374 -4.080 1.00 46.53 C ANISOU 1176 CA SER A 235 5152 6663 5864 409 -1209 -968 C ATOM 1177 C SER A 235 11.784 32.899 -4.018 1.00 40.92 C ANISOU 1177 C SER A 235 4305 5941 5300 505 -1249 -687 C ATOM 1178 O SER A 235 12.576 33.418 -3.250 1.00 44.17 O ANISOU 1178 O SER A 235 4809 6212 5761 608 -1106 -665 O ATOM 1179 CB SER A 235 10.487 30.877 -3.233 1.00 48.84 C ANISOU 1179 CB SER A 235 5359 6769 6429 371 -1156 -1048 C ATOM 1180 OG SER A 235 9.510 31.866 -2.987 1.00 46.77 O ANISOU 1180 OG SER A 235 4856 6452 6461 408 -1201 -841 O ATOM 1181 N GLN A 236 10.994 33.620 -4.815 1.00 49.01 N ANISOU 1181 N GLN A 236 5103 7106 6413 454 -1449 -453 N ATOM 1182 CA GLN A 236 11.061 35.091 -4.831 1.00 53.51 C ANISOU 1182 CA GLN A 236 5521 7620 7190 549 -1495 -155 C ATOM 1183 C GLN A 236 10.566 35.737 -3.518 1.00 56.31 C ANISOU 1183 C GLN A 236 5813 7620 7961 679 -1295 -158 C ATOM 1184 O GLN A 236 11.153 36.704 -3.038 1.00 55.12 O ANISOU 1184 O GLN A 236 5702 7312 7931 772 -1197 -77 O ATOM 1185 CB GLN A 236 10.268 35.650 -6.021 1.00 55.19 C ANISOU 1185 CB GLN A 236 5457 8073 7441 450 -1774 156 C ATOM 1186 CG GLN A 236 10.559 37.132 -6.356 1.00 58.97 C ANISOU 1186 CG GLN A 236 5778 8537 8091 528 -1871 519 C ATOM 1187 CD GLN A 236 12.000 37.379 -6.806 1.00 63.88 C ANISOU 1187 CD GLN A 236 6580 9323 8370 521 -1888 542 C ATOM 1188 OE1 GLN A 236 12.460 36.809 -7.793 1.00 66.47 O ANISOU 1188 OE1 GLN A 236 6970 9996 8288 386 -2011 506 O ATOM 1189 NE2 GLN A 236 12.717 38.228 -6.076 1.00 64.49 N ANISOU 1189 NE2 GLN A 236 6740 9163 8602 649 -1752 591 N ATOM 1190 N ASP A 237 9.485 35.204 -2.956 1.00 56.66 N ANISOU 1190 N ASP A 237 5762 7554 8212 662 -1227 -264 N ATOM 1191 CA ASP A 237 9.034 35.573 -1.621 1.00 63.29 C ANISOU 1191 CA ASP A 237 6572 8092 9383 756 -983 -352 C ATOM 1192 C ASP A 237 10.159 35.403 -0.595 1.00 54.51 C ANISOU 1192 C ASP A 237 5738 6853 8119 773 -765 -555 C ATOM 1193 O ASP A 237 10.274 36.170 0.355 1.00 53.94 O ANISOU 1193 O ASP A 237 5692 6567 8234 829 -570 -587 O ATOM 1194 CB ASP A 237 7.819 34.723 -1.221 1.00 76.24 C ANISOU 1194 CB ASP A 237 8092 9708 11170 696 -949 -459 C ATOM 1195 CG ASP A 237 7.167 35.187 0.076 1.00 93.83 C ANISOU 1195 CG ASP A 237 10229 11669 13754 782 -685 -534 C ATOM 1196 OD1 ASP A 237 7.843 35.243 1.130 1.00 98.52 O ANISOU 1196 OD1 ASP A 237 11017 12117 14299 796 -460 -713 O ATOM 1197 OD2 ASP A 237 5.958 35.496 0.043 1.00101.55 O ANISOU 1197 OD2 ASP A 237 10924 12604 15056 819 -695 -404 O ATOM 1198 N ASP A 238 10.992 34.394 -0.785 1.00 49.05 N ANISOU 1198 N ASP A 238 5246 6294 7096 710 -788 -687 N ATOM 1199 CA ASP A 238 12.034 34.111 0.190 1.00 55.37 C ANISOU 1199 CA ASP A 238 6267 7007 7763 706 -605 -819 C ATOM 1200 C ASP A 238 13.184 35.112 0.068 1.00 59.32 C ANISOU 1200 C ASP A 238 6857 7525 8158 749 -604 -684 C ATOM 1201 O ASP A 238 13.742 35.557 1.070 1.00 60.41 O ANISOU 1201 O ASP A 238 7101 7533 8317 734 -440 -719 O ATOM 1202 CB ASP A 238 12.550 32.671 0.024 1.00 65.38 C ANISOU 1202 CB ASP A 238 7683 8374 8784 649 -615 -969 C ATOM 1203 CG ASP A 238 11.527 31.608 0.463 1.00 69.53 C ANISOU 1203 CG ASP A 238 8160 8829 9431 575 -583 -1116 C ATOM 1204 OD1 ASP A 238 10.879 31.771 1.526 1.00 63.82 O ANISOU 1204 OD1 ASP A 238 7371 7963 8913 558 -445 -1153 O ATOM 1205 OD2 ASP A 238 11.378 30.601 -0.264 1.00 70.45 O ANISOU 1205 OD2 ASP A 238 8308 9037 9425 514 -686 -1207 O ATOM 1206 N ILE A 239 13.530 35.475 -1.162 1.00 60.05 N ANISOU 1206 N ILE A 239 6900 7803 8112 766 -796 -521 N ATOM 1207 CA ILE A 239 14.619 36.419 -1.398 1.00 51.56 C ANISOU 1207 CA ILE A 239 5889 6774 6927 790 -827 -354 C ATOM 1208 C ILE A 239 14.239 37.828 -0.929 1.00 43.15 C ANISOU 1208 C ILE A 239 4729 5477 6187 831 -773 -228 C ATOM 1209 O ILE A 239 15.044 38.517 -0.288 1.00 39.96 O ANISOU 1209 O ILE A 239 4449 4962 5774 815 -666 -209 O ATOM 1210 CB ILE A 239 15.025 36.441 -2.895 1.00 47.46 C ANISOU 1210 CB ILE A 239 5315 6559 6159 772 -1052 -194 C ATOM 1211 CG1 ILE A 239 15.555 35.061 -3.313 1.00 38.31 C ANISOU 1211 CG1 ILE A 239 4285 5587 4682 736 -1038 -381 C ATOM 1212 CG2 ILE A 239 16.074 37.530 -3.157 1.00 43.54 C ANISOU 1212 CG2 ILE A 239 4849 6120 5575 785 -1104 29 C ATOM 1213 CD1 ILE A 239 15.665 34.854 -4.803 1.00 36.22 C ANISOU 1213 CD1 ILE A 239 3965 5651 4148 672 -1227 -317 C ATOM 1214 N ASN A 240 13.013 38.246 -1.240 1.00 36.54 N ANISOU 1214 N ASN A 240 3666 4558 5659 876 -836 -136 N ATOM 1215 CA ASN A 240 12.479 39.510 -0.730 1.00 40.44 C ANISOU 1215 CA ASN A 240 4042 4758 6567 947 -731 -47 C ATOM 1216 C ASN A 240 12.526 39.564 0.798 1.00 45.70 C ANISOU 1216 C ASN A 240 4858 5170 7335 924 -422 -309 C ATOM 1217 O ASN A 240 12.826 40.593 1.385 1.00 59.39 O ANISOU 1217 O ASN A 240 6651 6678 9235 926 -282 -315 O ATOM 1218 CB ASN A 240 11.027 39.736 -1.177 1.00 44.79 C ANISOU 1218 CB ASN A 240 4282 5254 7484 1014 -812 94 C ATOM 1219 CG ASN A 240 10.874 39.888 -2.677 1.00 50.29 C ANISOU 1219 CG ASN A 240 4785 6223 8101 987 -1135 413 C ATOM 1220 OD1 ASN A 240 11.779 40.341 -3.370 1.00 52.49 O ANISOU 1220 OD1 ASN A 240 5117 6647 8180 956 -1279 587 O ATOM 1221 ND2 ASN A 240 9.702 39.515 -3.183 1.00 61.69 N ANISOU 1221 ND2 ASN A 240 5986 7768 9685 970 -1261 514 N ATOM 1222 N GLY A 241 12.212 38.448 1.438 1.00 38.85 N ANISOU 1222 N GLY A 241 4052 4348 6362 871 -317 -526 N ATOM 1223 CA GLY A 241 12.207 38.384 2.882 1.00 44.51 C ANISOU 1223 CA GLY A 241 4892 4900 7121 799 -38 -759 C ATOM 1224 C GLY A 241 13.591 38.601 3.456 1.00 50.70 C ANISOU 1224 C GLY A 241 5924 5708 7632 689 34 -790 C ATOM 1225 O GLY A 241 13.781 39.471 4.309 1.00 54.30 O ANISOU 1225 O GLY A 241 6466 5978 8189 623 221 -875 O ATOM 1226 N ILE A 242 14.563 37.821 2.990 1.00 37.77 N ANISOU 1226 N ILE A 242 4395 4300 5654 655 -103 -722 N ATOM 1227 CA ILE A 242 15.900 37.891 3.568 1.00 39.57 C ANISOU 1227 CA ILE A 242 4823 4594 5616 538 -46 -704 C ATOM 1228 C ILE A 242 16.571 39.211 3.174 1.00 45.61 C ANISOU 1228 C ILE A 242 5622 5304 6404 540 -109 -536 C ATOM 1229 O ILE A 242 17.386 39.747 3.917 1.00 49.34 O ANISOU 1229 O ILE A 242 6246 5732 6770 405 -11 -542 O ATOM 1230 CB ILE A 242 16.772 36.665 3.149 1.00 37.74 C ANISOU 1230 CB ILE A 242 4661 4605 5073 536 -148 -652 C ATOM 1231 CG1 ILE A 242 17.920 36.459 4.133 1.00 33.56 C ANISOU 1231 CG1 ILE A 242 4290 4138 4323 389 -43 -630 C ATOM 1232 CG2 ILE A 242 17.255 36.769 1.710 1.00 36.79 C ANISOU 1232 CG2 ILE A 242 4492 4665 4823 635 -359 -481 C ATOM 1233 CD1 ILE A 242 17.445 36.212 5.534 1.00 35.83 C ANISOU 1233 CD1 ILE A 242 4619 4324 4672 238 154 -793 C ATOM 1234 N GLN A 243 16.193 39.763 2.027 1.00 50.72 N ANISOU 1234 N GLN A 243 6118 5959 7196 661 -283 -365 N ATOM 1235 CA GLN A 243 16.782 41.021 1.598 1.00 51.37 C ANISOU 1235 CA GLN A 243 6206 5976 7336 658 -368 -163 C ATOM 1236 C GLN A 243 16.091 42.229 2.236 1.00 50.32 C ANISOU 1236 C GLN A 243 6035 5471 7615 666 -201 -229 C ATOM 1237 O GLN A 243 16.590 43.346 2.164 1.00 37.28 O ANISOU 1237 O GLN A 243 4426 3677 6062 631 -218 -105 O ATOM 1238 CB GLN A 243 16.747 41.143 0.072 1.00 49.49 C ANISOU 1238 CB GLN A 243 5803 5937 7063 751 -642 100 C ATOM 1239 CG GLN A 243 17.822 40.341 -0.644 1.00 42.77 C ANISOU 1239 CG GLN A 243 5027 5442 5780 724 -776 180 C ATOM 1240 CD GLN A 243 17.905 40.677 -2.129 1.00 42.66 C ANISOU 1240 CD GLN A 243 4863 5665 5682 759 -1033 447 C ATOM 1241 OE1 GLN A 243 17.197 41.559 -2.629 1.00 37.97 O ANISOU 1241 OE1 GLN A 243 4092 4969 5366 795 -1144 631 O ATOM 1242 NE2 GLN A 243 18.780 39.983 -2.837 1.00 40.03 N ANISOU 1242 NE2 GLN A 243 4580 5658 4973 740 -1118 486 N ATOM 1243 N SER A 244 14.934 42.029 2.855 1.00 55.19 N ANISOU 1243 N SER A 244 6561 5911 8496 712 -24 -427 N ATOM 1244 CA SER A 244 14.328 43.147 3.573 1.00 52.53 C ANISOU 1244 CA SER A 244 6199 5194 8565 725 209 -545 C ATOM 1245 C SER A 244 15.065 43.303 4.892 1.00 51.17 C ANISOU 1245 C SER A 244 6299 4950 8193 507 448 -791 C ATOM 1246 O SER A 244 15.236 44.404 5.368 1.00 55.70 O ANISOU 1246 O SER A 244 6964 5251 8948 437 601 -865 O ATOM 1247 CB SER A 244 12.830 42.951 3.794 1.00 53.85 C ANISOU 1247 CB SER A 244 6147 5211 9103 853 347 -662 C ATOM 1248 OG SER A 244 12.551 41.664 4.314 1.00 70.15 O ANISOU 1248 OG SER A 244 8248 7468 10937 789 406 -843 O ATOM 1249 N LEU A 245 15.535 42.190 5.449 1.00 51.63 N ANISOU 1249 N LEU A 245 6482 5259 7875 377 468 -894 N ATOM 1250 CA LEU A 245 16.356 42.212 6.657 1.00 52.48 C ANISOU 1250 CA LEU A 245 6830 5400 7709 112 641 -1054 C ATOM 1251 C LEU A 245 17.786 42.719 6.438 1.00 52.89 C ANISOU 1251 C LEU A 245 7043 5561 7492 -22 503 -861 C ATOM 1252 O LEU A 245 18.201 43.679 7.095 1.00 58.05 O ANISOU 1252 O LEU A 245 7852 6045 8158 -205 637 -950 O ATOM 1253 CB LEU A 245 16.413 40.819 7.292 1.00 45.90 C ANISOU 1253 CB LEU A 245 6031 4816 6592 9 674 -1141 C ATOM 1254 CG LEU A 245 15.087 40.268 7.826 1.00 41.78 C ANISOU 1254 CG LEU A 245 5382 4217 6274 57 846 -1353 C ATOM 1255 CD1 LEU A 245 15.307 39.008 8.664 1.00 42.49 C ANISOU 1255 CD1 LEU A 245 5534 4539 6072 -115 891 -1416 C ATOM 1256 CD2 LEU A 245 14.344 41.321 8.619 1.00 39.80 C ANISOU 1256 CD2 LEU A 245 5136 3665 6322 12 1147 -1601 C ATOM 1257 N TYR A 246 18.536 42.089 5.532 1.00 46.73 N ANISOU 1257 N TYR A 246 6226 5061 6466 51 253 -612 N ATOM 1258 CA TYR A 246 19.954 42.431 5.363 1.00 46.04 C ANISOU 1258 CA TYR A 246 6265 5139 6090 -83 127 -401 C ATOM 1259 C TYR A 246 20.308 43.152 4.052 1.00 39.96 C ANISOU 1259 C TYR A 246 5402 4393 5389 50 -105 -120 C ATOM 1260 O TYR A 246 21.480 43.512 3.836 1.00 37.33 O ANISOU 1260 O TYR A 246 5150 4209 4826 -58 -220 86 O ATOM 1261 CB TYR A 246 20.808 41.170 5.493 1.00 41.49 C ANISOU 1261 CB TYR A 246 5723 4900 5143 -140 60 -307 C ATOM 1262 CG TYR A 246 20.555 40.425 6.765 1.00 42.45 C ANISOU 1262 CG TYR A 246 5912 5043 5176 -305 249 -504 C ATOM 1263 CD1 TYR A 246 21.109 40.858 7.948 1.00 36.42 C ANISOU 1263 CD1 TYR A 246 5312 4281 4244 -615 387 -571 C ATOM 1264 CD2 TYR A 246 19.739 39.295 6.789 1.00 47.47 C ANISOU 1264 CD2 TYR A 246 6443 5713 5881 -190 281 -614 C ATOM 1265 CE1 TYR A 246 20.873 40.191 9.136 1.00 42.52 C ANISOU 1265 CE1 TYR A 246 6130 5124 4901 -813 550 -723 C ATOM 1266 CE2 TYR A 246 19.490 38.618 7.976 1.00 49.19 C ANISOU 1266 CE2 TYR A 246 6702 5969 6020 -365 441 -759 C ATOM 1267 CZ TYR A 246 20.066 39.078 9.153 1.00 48.54 C ANISOU 1267 CZ TYR A 246 6770 5921 5750 -681 575 -804 C ATOM 1268 OH TYR A 246 19.851 38.437 10.357 1.00 47.88 O ANISOU 1268 OH TYR A 246 6716 5931 5545 -907 724 -916 O ATOM 1269 N GLY A 247 19.316 43.357 3.187 1.00 37.43 N ANISOU 1269 N GLY A 247 4890 3962 5370 259 -187 -73 N ATOM 1270 CA GLY A 247 19.491 44.177 1.990 1.00 44.47 C ANISOU 1270 CA GLY A 247 5660 4864 6372 352 -408 222 C ATOM 1271 C GLY A 247 20.608 43.806 1.028 1.00 47.08 C ANISOU 1271 C GLY A 247 5981 5577 6331 348 -639 489 C ATOM 1272 O GLY A 247 20.632 42.707 0.483 1.00 50.57 O ANISOU 1272 O GLY A 247 6363 6292 6560 431 -713 487 O TER 1273 GLY A 247 ATOM 1274 N CYS B 1 10.318 26.127 12.120 1.00 40.13 N ANISOU 1274 N CYS B 1 5015 5087 5146 -97 -473 -290 N ATOM 1275 CA CYS B 1 9.384 25.037 12.372 1.00 46.15 C ANISOU 1275 CA CYS B 1 5988 5741 5807 53 -497 -323 C ATOM 1276 C CYS B 1 8.993 24.336 11.084 1.00 44.77 C ANISOU 1276 C CYS B 1 5771 5718 5523 65 -367 -326 C ATOM 1277 O CYS B 1 8.619 24.971 10.112 1.00 45.08 O ANISOU 1277 O CYS B 1 5747 5872 5509 -75 -255 -200 O ATOM 1278 CB CYS B 1 8.122 25.534 13.078 1.00 40.67 C ANISOU 1278 CB CYS B 1 5523 4832 5097 9 -508 -229 C ATOM 1279 SG CYS B 1 7.122 24.155 13.715 1.00 41.10 S ANISOU 1279 SG CYS B 1 5839 4748 5029 152 -549 -286 S ATOM 1280 N THR B 2 9.056 23.014 11.098 1.00 43.97 N ANISOU 1280 N THR B 2 5718 5606 5383 229 -396 -468 N ATOM 1281 CA THR B 2 8.814 22.221 9.903 1.00 39.73 C ANISOU 1281 CA THR B 2 5129 5223 4745 244 -273 -546 C ATOM 1282 C THR B 2 7.906 21.058 10.224 1.00 41.38 C ANISOU 1282 C THR B 2 5568 5248 4906 352 -306 -610 C ATOM 1283 O THR B 2 8.248 20.218 11.063 1.00 39.91 O ANISOU 1283 O THR B 2 5481 4892 4793 512 -424 -698 O ATOM 1284 CB THR B 2 10.114 21.665 9.316 1.00 44.86 C ANISOU 1284 CB THR B 2 5526 6076 5441 332 -235 -742 C ATOM 1285 OG1 THR B 2 10.977 22.743 8.949 1.00 48.00 O ANISOU 1285 OG1 THR B 2 5689 6678 5873 183 -177 -684 O ATOM 1286 CG2 THR B 2 9.817 20.821 8.101 1.00 41.17 C ANISOU 1286 CG2 THR B 2 5016 5773 4852 336 -92 -876 C ATOM 1287 N CYS B 3 6.772 20.991 9.533 1.00 38.99 N ANISOU 1287 N CYS B 3 5345 4987 4483 253 -213 -555 N ATOM 1288 CA CYS B 3 5.722 20.047 9.882 1.00 36.66 C ANISOU 1288 CA CYS B 3 5274 4512 4143 291 -229 -594 C ATOM 1289 C CYS B 3 5.392 19.068 8.786 1.00 37.04 C ANISOU 1289 C CYS B 3 5300 4675 4098 282 -131 -747 C ATOM 1290 O CYS B 3 5.409 19.420 7.614 1.00 43.68 O ANISOU 1290 O CYS B 3 5983 5786 4828 179 -28 -750 O ATOM 1291 CB CYS B 3 4.436 20.797 10.244 1.00 38.73 C ANISOU 1291 CB CYS B 3 5656 4700 4360 171 -220 -425 C ATOM 1292 SG CYS B 3 4.616 21.906 11.606 1.00 74.53 S ANISOU 1292 SG CYS B 3 10249 9073 8997 164 -314 -308 S ATOM 1293 N VAL B 4 5.078 17.839 9.189 1.00 41.96 N ANISOU 1293 N VAL B 4 6100 5088 4757 371 -167 -870 N ATOM 1294 CA VAL B 4 4.284 16.916 8.377 1.00 41.83 C ANISOU 1294 CA VAL B 4 6141 5101 4650 310 -80 -1010 C ATOM 1295 C VAL B 4 2.975 16.672 9.121 1.00 44.44 C ANISOU 1295 C VAL B 4 6705 5225 4953 224 -107 -914 C ATOM 1296 O VAL B 4 2.883 15.756 9.942 1.00 50.02 O ANISOU 1296 O VAL B 4 7616 5652 5737 290 -168 -953 O ATOM 1297 CB VAL B 4 5.006 15.582 8.123 1.00 39.96 C ANISOU 1297 CB VAL B 4 5910 4757 4514 467 -76 -1275 C ATOM 1298 CG1 VAL B 4 4.082 14.593 7.423 1.00 40.65 C ANISOU 1298 CG1 VAL B 4 6099 4821 4527 374 9 -1446 C ATOM 1299 CG2 VAL B 4 6.264 15.813 7.315 1.00 36.97 C ANISOU 1299 CG2 VAL B 4 5251 4640 4155 540 -13 -1416 C ATOM 1300 N PRO B 5 1.972 17.524 8.878 1.00 37.91 N ANISOU 1300 N PRO B 5 5842 4535 4026 74 -66 -773 N ATOM 1301 CA PRO B 5 0.736 17.382 9.653 1.00 38.84 C ANISOU 1301 CA PRO B 5 6135 4493 4130 -14 -72 -702 C ATOM 1302 C PRO B 5 0.096 16.037 9.362 1.00 42.71 C ANISOU 1302 C PRO B 5 6752 4887 4589 -76 -28 -868 C ATOM 1303 O PRO B 5 0.180 15.536 8.243 1.00 46.88 O ANISOU 1303 O PRO B 5 7186 5570 5058 -104 29 -1029 O ATOM 1304 CB PRO B 5 -0.139 18.561 9.186 1.00 37.26 C ANISOU 1304 CB PRO B 5 5799 4498 3860 -127 -39 -552 C ATOM 1305 CG PRO B 5 0.493 19.069 7.935 1.00 36.59 C ANISOU 1305 CG PRO B 5 5507 4690 3705 -138 -12 -540 C ATOM 1306 CD PRO B 5 1.951 18.677 7.965 1.00 31.95 C ANISOU 1306 CD PRO B 5 4884 4071 3185 -14 -22 -654 C ATOM 1307 N PRO B 6 -0.513 15.435 10.384 1.00 42.98 N ANISOU 1307 N PRO B 6 7009 4667 4656 -118 -46 -842 N ATOM 1308 CA PRO B 6 -0.907 14.034 10.290 1.00 38.91 C ANISOU 1308 CA PRO B 6 6660 3962 4160 -175 -17 -996 C ATOM 1309 C PRO B 6 -2.201 13.819 9.535 1.00 40.12 C ANISOU 1309 C PRO B 6 6760 4274 4210 -385 75 -1080 C ATOM 1310 O PRO B 6 -3.020 14.719 9.418 1.00 33.75 O ANISOU 1310 O PRO B 6 5827 3671 3325 -481 100 -974 O ATOM 1311 CB PRO B 6 -1.091 13.644 11.759 1.00 35.67 C ANISOU 1311 CB PRO B 6 6516 3245 3793 -183 -73 -873 C ATOM 1312 CG PRO B 6 -1.612 14.905 12.369 1.00 31.37 C ANISOU 1312 CG PRO B 6 5901 2838 3180 -244 -60 -708 C ATOM 1313 CD PRO B 6 -0.884 16.021 11.689 1.00 30.27 C ANISOU 1313 CD PRO B 6 5515 2934 3054 -141 -81 -678 C ATOM 1314 N HIS B 7 -2.398 12.602 9.052 1.00 48.44 N ANISOU 1314 N HIS B 7 7906 5215 5284 -452 115 -1283 N ATOM 1315 CA HIS B 7 -3.702 12.209 8.568 1.00 41.53 C ANISOU 1315 CA HIS B 7 7015 4442 4322 -688 189 -1381 C ATOM 1316 C HIS B 7 -4.722 12.308 9.712 1.00 45.01 C ANISOU 1316 C HIS B 7 7590 4749 4763 -830 210 -1229 C ATOM 1317 O HIS B 7 -4.410 11.987 10.872 1.00 35.65 O ANISOU 1317 O HIS B 7 6630 3269 3648 -784 178 -1122 O ATOM 1318 CB HIS B 7 -3.634 10.806 8.007 1.00 38.59 C ANISOU 1318 CB HIS B 7 6757 3897 4007 -743 228 -1654 C ATOM 1319 CG HIS B 7 -4.869 10.389 7.278 1.00 40.44 C ANISOU 1319 CG HIS B 7 6930 4297 4138 -1008 299 -1813 C ATOM 1320 ND1 HIS B 7 -6.059 10.129 7.921 1.00 46.96 N ANISOU 1320 ND1 HIS B 7 7855 5028 4961 -1227 339 -1755 N ATOM 1321 CD2 HIS B 7 -5.095 10.180 5.959 1.00 42.34 C ANISOU 1321 CD2 HIS B 7 7004 4827 4258 -1108 338 -2043 C ATOM 1322 CE1 HIS B 7 -6.971 9.782 7.025 1.00 53.50 C ANISOU 1322 CE1 HIS B 7 8562 6072 5693 -1445 387 -1946 C ATOM 1323 NE2 HIS B 7 -6.410 9.800 5.830 1.00 47.83 N ANISOU 1323 NE2 HIS B 7 7693 5589 4892 -1377 378 -2121 N ATOM 1324 N PRO B 8 -5.940 12.767 9.392 1.00 47.31 N ANISOU 1324 N PRO B 8 7727 5287 4962 -1005 262 -1220 N ATOM 1325 CA PRO B 8 -7.015 12.920 10.384 1.00 41.87 C ANISOU 1325 CA PRO B 8 7100 4545 4265 -1161 319 -1122 C ATOM 1326 C PRO B 8 -7.184 11.697 11.308 1.00 41.15 C ANISOU 1326 C PRO B 8 7323 4089 4222 -1296 363 -1144 C ATOM 1327 O PRO B 8 -7.322 11.862 12.535 1.00 38.50 O ANISOU 1327 O PRO B 8 7138 3612 3878 -1326 382 -994 O ATOM 1328 CB PRO B 8 -8.262 13.107 9.518 1.00 44.76 C ANISOU 1328 CB PRO B 8 7227 5231 4550 -1343 360 -1215 C ATOM 1329 CG PRO B 8 -7.771 13.625 8.212 1.00 35.62 C ANISOU 1329 CG PRO B 8 5856 4357 3322 -1233 293 -1249 C ATOM 1330 CD PRO B 8 -6.365 13.142 8.028 1.00 35.64 C ANISOU 1330 CD PRO B 8 5988 4184 3369 -1068 264 -1313 C ATOM 1331 N GLN B 9 -7.174 10.491 10.733 1.00 38.99 N ANISOU 1331 N GLN B 9 7161 3660 3994 -1390 381 -1328 N ATOM 1332 CA GLN B 9 -7.278 9.269 11.539 1.00 42.65 C ANISOU 1332 CA GLN B 9 7956 3713 4535 -1523 409 -1324 C ATOM 1333 C GLN B 9 -6.106 9.163 12.510 1.00 45.32 C ANISOU 1333 C GLN B 9 8528 3743 4947 -1296 303 -1147 C ATOM 1334 O GLN B 9 -6.296 8.838 13.675 1.00 45.62 O ANISOU 1334 O GLN B 9 8814 3551 4968 -1390 307 -979 O ATOM 1335 CB GLN B 9 -7.346 8.018 10.666 1.00 43.84 C ANISOU 1335 CB GLN B 9 8185 3702 4769 -1634 435 -1585 C ATOM 1336 CG GLN B 9 -7.208 6.724 11.461 1.00 46.60 C ANISOU 1336 CG GLN B 9 8893 3554 5261 -1706 429 -1537 C ATOM 1337 CD GLN B 9 -7.649 5.488 10.680 1.00 52.55 C ANISOU 1337 CD GLN B 9 9629 4207 6131 -1850 474 -1763 C ATOM 1338 OE1 GLN B 9 -8.558 5.554 9.860 1.00 50.13 O ANISOU 1338 OE1 GLN B 9 9117 4192 5739 -2056 549 -1942 O ATOM 1339 NE2 GLN B 9 -7.004 4.351 10.940 1.00 57.73 N ANISOU 1339 NE2 GLN B 9 10489 4449 6994 -1736 410 -1758 N ATOM 1340 N THR B 10 -4.897 9.445 12.031 1.00 46.29 N ANISOU 1340 N THR B 10 8558 3895 5136 -1013 206 -1182 N ATOM 1341 CA THR B 10 -3.737 9.460 12.906 1.00 43.23 C ANISOU 1341 CA THR B 10 8327 3278 4822 -777 77 -1023 C ATOM 1342 C THR B 10 -3.940 10.489 14.001 1.00 44.36 C ANISOU 1342 C THR B 10 8472 3539 4845 -795 66 -794 C ATOM 1343 O THR B 10 -3.725 10.207 15.169 1.00 51.94 O ANISOU 1343 O THR B 10 9678 4273 5783 -794 3 -622 O ATOM 1344 CB THR B 10 -2.432 9.788 12.163 1.00 43.23 C ANISOU 1344 CB THR B 10 8140 3380 4904 -485 -6 -1121 C ATOM 1345 OG1 THR B 10 -2.227 8.864 11.087 1.00 47.69 O ANISOU 1345 OG1 THR B 10 8674 3875 5569 -465 29 -1392 O ATOM 1346 CG2 THR B 10 -1.272 9.685 13.115 1.00 39.96 C ANISOU 1346 CG2 THR B 10 7872 2727 4586 -249 -162 -970 C ATOM 1347 N ALA B 11 -4.361 11.685 13.609 1.00 45.92 N ANISOU 1347 N ALA B 11 8398 4088 4960 -812 122 -797 N ATOM 1348 CA ALA B 11 -4.612 12.758 14.554 1.00 40.25 C ANISOU 1348 CA ALA B 11 7647 3491 4155 -825 132 -642 C ATOM 1349 C ALA B 11 -5.601 12.322 15.643 1.00 49.30 C ANISOU 1349 C ALA B 11 9005 4522 5205 -1070 224 -562 C ATOM 1350 O ALA B 11 -5.416 12.625 16.819 1.00 51.51 O ANISOU 1350 O ALA B 11 9428 4740 5402 -1069 198 -422 O ATOM 1351 CB ALA B 11 -5.122 13.963 13.835 1.00 33.01 C ANISOU 1351 CB ALA B 11 6414 2916 3213 -825 186 -675 C ATOM 1352 N PHE B 12 -6.646 11.605 15.252 1.00 43.30 N ANISOU 1352 N PHE B 12 8258 3758 4435 -1306 337 -663 N ATOM 1353 CA PHE B 12 -7.613 11.113 16.220 1.00 41.31 C ANISOU 1353 CA PHE B 12 8196 3414 4087 -1587 454 -596 C ATOM 1354 C PHE B 12 -6.950 10.142 17.179 1.00 53.15 C ANISOU 1354 C PHE B 12 10086 4531 5575 -1588 367 -433 C ATOM 1355 O PHE B 12 -7.052 10.278 18.406 1.00 63.45 O ANISOU 1355 O PHE B 12 11572 5796 6739 -1680 383 -267 O ATOM 1356 CB PHE B 12 -8.785 10.424 15.517 1.00 46.62 C ANISOU 1356 CB PHE B 12 8793 4145 4776 -1862 582 -757 C ATOM 1357 CG PHE B 12 -9.872 9.975 16.449 1.00 54.15 C ANISOU 1357 CG PHE B 12 9892 5055 5626 -2202 738 -705 C ATOM 1358 CD1 PHE B 12 -9.833 8.725 17.040 1.00 56.01 C ANISOU 1358 CD1 PHE B 12 10496 4926 5860 -2385 748 -613 C ATOM 1359 CD2 PHE B 12 -10.945 10.804 16.736 1.00 62.25 C ANISOU 1359 CD2 PHE B 12 10680 6404 6566 -2344 881 -747 C ATOM 1360 CE1 PHE B 12 -10.844 8.312 17.910 1.00 60.75 C ANISOU 1360 CE1 PHE B 12 11238 5508 6337 -2748 915 -545 C ATOM 1361 CE2 PHE B 12 -11.964 10.387 17.599 1.00 64.73 C ANISOU 1361 CE2 PHE B 12 11099 6725 6771 -2687 1059 -724 C ATOM 1362 CZ PHE B 12 -11.906 9.142 18.185 1.00 61.70 C ANISOU 1362 CZ PHE B 12 11095 6000 6349 -2909 1083 -614 C ATOM 1363 N CYS B 13 -6.272 9.153 16.611 1.00 49.62 N ANISOU 1363 N CYS B 13 9770 3807 5275 -1483 269 -486 N ATOM 1364 CA CYS B 13 -5.755 8.042 17.396 1.00 52.49 C ANISOU 1364 CA CYS B 13 10520 3742 5680 -1486 168 -323 C ATOM 1365 C CYS B 13 -4.646 8.449 18.356 1.00 56.73 C ANISOU 1365 C CYS B 13 11177 4210 6165 -1246 -13 -112 C ATOM 1366 O CYS B 13 -4.491 7.858 19.425 1.00 66.05 O ANISOU 1366 O CYS B 13 12643 5183 7269 -1299 -90 111 O ATOM 1367 CB CYS B 13 -5.266 6.932 16.463 1.00 47.36 C ANISOU 1367 CB CYS B 13 9875 2860 5260 -1359 103 -470 C ATOM 1368 SG CYS B 13 -6.624 6.124 15.581 1.00 73.56 S ANISOU 1368 SG CYS B 13 13099 6229 8624 -1694 292 -691 S ATOM 1369 N ASN B 14 -3.880 9.467 17.985 1.00 46.58 N ANISOU 1369 N ASN B 14 9629 3161 4908 -989 -87 -173 N ATOM 1370 CA ASN B 14 -2.681 9.791 18.742 1.00 53.00 C ANISOU 1370 CA ASN B 14 10515 3915 5708 -744 -286 -19 C ATOM 1371 C ASN B 14 -2.846 10.993 19.638 1.00 53.46 C ANISOU 1371 C ASN B 14 10503 4243 5566 -796 -259 71 C ATOM 1372 O ASN B 14 -1.979 11.282 20.461 1.00 64.15 O ANISOU 1372 O ASN B 14 11941 5577 6856 -656 -422 204 O ATOM 1373 CB ASN B 14 -1.504 10.008 17.797 1.00 54.68 C ANISOU 1373 CB ASN B 14 10496 4170 6111 -421 -402 -158 C ATOM 1374 CG ASN B 14 -0.980 8.706 17.219 1.00 61.52 C ANISOU 1374 CG ASN B 14 11485 4694 7196 -292 -483 -245 C ATOM 1375 OD1 ASN B 14 -1.581 7.638 17.398 1.00 58.79 O ANISOU 1375 OD1 ASN B 14 11378 4075 6883 -459 -443 -207 O ATOM 1376 ND2 ASN B 14 0.161 8.784 16.539 1.00 65.93 N ANISOU 1376 ND2 ASN B 14 11850 5279 7921 3 -585 -374 N ATOM 1377 N SER B 15 -3.958 11.694 19.476 1.00 43.87 N ANISOU 1377 N SER B 15 9118 3286 4264 -992 -60 -24 N ATOM 1378 CA SER B 15 -4.249 12.804 20.354 1.00 46.74 C ANISOU 1378 CA SER B 15 9417 3882 4460 -1058 -1 13 C ATOM 1379 C SER B 15 -4.902 12.292 21.620 1.00 57.13 C ANISOU 1379 C SER B 15 11033 5125 5550 -1325 72 159 C ATOM 1380 O SER B 15 -5.578 11.265 21.603 1.00 64.03 O ANISOU 1380 O SER B 15 12087 5832 6408 -1537 155 199 O ATOM 1381 CB SER B 15 -5.132 13.826 19.652 1.00 40.03 C ANISOU 1381 CB SER B 15 8232 3327 3651 -1113 166 -155 C ATOM 1382 OG SER B 15 -4.356 14.534 18.705 1.00 34.68 O ANISOU 1382 OG SER B 15 7304 2748 3125 -872 77 -229 O ATOM 1383 N ASP B 16 -4.677 12.992 22.726 1.00 53.71 N ANISOU 1383 N ASP B 16 10663 4819 4926 -1340 43 234 N ATOM 1384 CA ASP B 16 -5.310 12.607 23.984 1.00 52.47 C ANISOU 1384 CA ASP B 16 10785 4663 4487 -1627 135 370 C ATOM 1385 C ASP B 16 -6.705 13.215 24.057 1.00 48.26 C ANISOU 1385 C ASP B 16 10063 4403 3870 -1879 430 200 C ATOM 1386 O ASP B 16 -7.607 12.615 24.622 1.00 53.12 O ANISOU 1386 O ASP B 16 10845 5021 4318 -2191 594 255 O ATOM 1387 CB ASP B 16 -4.458 13.029 25.182 1.00 56.22 C ANISOU 1387 CB ASP B 16 11420 5193 4747 -1558 -29 505 C ATOM 1388 CG ASP B 16 -3.125 12.300 25.236 1.00 70.82 C ANISOU 1388 CG ASP B 16 13458 6773 6676 -1314 -344 697 C ATOM 1389 OD1 ASP B 16 -3.125 11.061 25.099 1.00 80.25 O ANISOU 1389 OD1 ASP B 16 14893 7663 7936 -1352 -409 848 O ATOM 1390 OD2 ASP B 16 -2.077 12.965 25.407 1.00 72.66 O ANISOU 1390 OD2 ASP B 16 13587 7089 6932 -1083 -531 685 O ATOM 1391 N LEU B 17 -6.886 14.397 23.468 1.00 50.53 N ANISOU 1391 N LEU B 17 9993 4913 4292 -1743 496 -1 N ATOM 1392 CA LEU B 17 -8.207 15.036 23.419 1.00 48.94 C ANISOU 1392 CA LEU B 17 9548 4968 4081 -1917 754 -187 C ATOM 1393 C LEU B 17 -8.602 15.331 21.985 1.00 52.59 C ANISOU 1393 C LEU B 17 9678 5496 4807 -1798 777 -329 C ATOM 1394 O LEU B 17 -7.769 15.731 21.159 1.00 48.77 O ANISOU 1394 O LEU B 17 9064 4973 4493 -1536 622 -334 O ATOM 1395 CB LEU B 17 -8.249 16.347 24.226 1.00 41.38 C ANISOU 1395 CB LEU B 17 8459 4235 3029 -1879 825 -308 C ATOM 1396 CG LEU B 17 -8.125 16.374 25.759 1.00 47.83 C ANISOU 1396 CG LEU B 17 9536 5126 3513 -2050 861 -244 C ATOM 1397 CD1 LEU B 17 -8.399 17.779 26.266 1.00 54.74 C ANISOU 1397 CD1 LEU B 17 10185 6244 4371 -2010 984 -477 C ATOM 1398 CD2 LEU B 17 -9.057 15.407 26.425 1.00 47.05 C ANISOU 1398 CD2 LEU B 17 9657 5048 3174 -2416 1046 -162 C ATOM 1399 N VAL B 18 -9.877 15.133 21.681 1.00 53.58 N ANISOU 1399 N VAL B 18 9656 5755 4949 -2008 970 -441 N ATOM 1400 CA VAL B 18 -10.405 15.544 20.391 1.00 46.05 C ANISOU 1400 CA VAL B 18 8354 4936 4206 -1913 986 -578 C ATOM 1401 C VAL B 18 -11.736 16.197 20.634 1.00 46.24 C ANISOU 1401 C VAL B 18 8108 5231 4229 -2057 1201 -742 C ATOM 1402 O VAL B 18 -12.665 15.539 21.133 1.00 42.31 O ANISOU 1402 O VAL B 18 7673 4794 3611 -2360 1381 -779 O ATOM 1403 CB VAL B 18 -10.573 14.378 19.422 1.00 41.61 C ANISOU 1403 CB VAL B 18 7842 4251 3718 -2006 953 -575 C ATOM 1404 CG1 VAL B 18 -11.247 14.866 18.151 1.00 38.32 C ANISOU 1404 CG1 VAL B 18 7048 4054 3459 -1946 968 -720 C ATOM 1405 CG2 VAL B 18 -9.226 13.731 19.125 1.00 38.68 C ANISOU 1405 CG2 VAL B 18 7701 3603 3394 -1823 746 -455 C ATOM 1406 N ILE B 19 -11.806 17.492 20.307 1.00 41.20 N ANISOU 1406 N ILE B 19 7170 4744 3742 -1841 1183 -839 N ATOM 1407 CA ILE B 19 -12.968 18.325 20.615 1.00 49.71 C ANISOU 1407 CA ILE B 19 7952 6064 4873 -1896 1369 -1021 C ATOM 1408 C ILE B 19 -13.265 19.351 19.556 1.00 43.04 C ANISOU 1408 C ILE B 19 6727 5339 4289 -1655 1291 -1089 C ATOM 1409 O ILE B 19 -12.383 19.751 18.795 1.00 36.66 O ANISOU 1409 O ILE B 19 5904 4433 3591 -1427 1102 -986 O ATOM 1410 CB ILE B 19 -12.813 19.129 21.942 1.00 41.38 C ANISOU 1410 CB ILE B 19 6965 5051 3706 -1890 1470 -1098 C ATOM 1411 CG1 ILE B 19 -11.601 20.068 21.862 1.00 44.74 C ANISOU 1411 CG1 ILE B 19 7414 5351 4235 -1594 1279 -1041 C ATOM 1412 CG2 ILE B 19 -12.719 18.209 23.134 1.00 48.42 C ANISOU 1412 CG2 ILE B 19 8220 5896 4284 -2171 1567 -1019 C ATOM 1413 CD1 ILE B 19 -11.581 21.153 22.920 1.00 45.43 C ANISOU 1413 CD1 ILE B 19 7463 5507 4292 -1551 1374 -1196 C ATOM 1414 N ARG B 20 -14.527 19.771 19.544 1.00 42.68 N ANISOU 1414 N ARG B 20 6367 5513 4335 -1717 1442 -1256 N ATOM 1415 CA ARG B 20 -14.957 21.000 18.897 1.00 47.37 C ANISOU 1415 CA ARG B 20 6584 6221 5192 -1468 1385 -1328 C ATOM 1416 C ARG B 20 -14.956 22.164 19.877 1.00 48.42 C ANISOU 1416 C ARG B 20 6649 6346 5402 -1344 1484 -1464 C ATOM 1417 O ARG B 20 -15.533 22.063 20.969 1.00 48.62 O ANISOU 1417 O ARG B 20 6699 6476 5299 -1527 1706 -1629 O ATOM 1418 CB ARG B 20 -16.364 20.856 18.333 1.00 57.41 C ANISOU 1418 CB ARG B 20 7499 7748 6565 -1566 1471 -1458 C ATOM 1419 CG ARG B 20 -16.492 20.014 17.098 1.00 65.23 C ANISOU 1419 CG ARG B 20 8447 8793 7543 -1640 1341 -1372 C ATOM 1420 CD ARG B 20 -17.751 20.444 16.384 1.00 67.42 C ANISOU 1420 CD ARG B 20 8266 9351 7998 -1602 1339 -1487 C ATOM 1421 NE ARG B 20 -18.667 19.350 16.108 1.00 65.51 N ANISOU 1421 NE ARG B 20 7939 9288 7663 -1912 1431 -1588 N ATOM 1422 CZ ARG B 20 -19.979 19.509 16.018 1.00 68.23 C ANISOU 1422 CZ ARG B 20 7889 9920 8113 -1995 1526 -1763 C ATOM 1423 NH1 ARG B 20 -20.507 20.714 16.212 1.00 69.37 N ANISOU 1423 NH1 ARG B 20 7700 10180 8478 -1754 1542 -1855 N ATOM 1424 NH2 ARG B 20 -20.757 18.466 15.752 1.00 70.79 N ANISOU 1424 NH2 ARG B 20 8144 10406 8349 -2317 1607 -1862 N ATOM 1425 N ALA B 21 -14.356 23.283 19.479 1.00 42.65 N ANISOU 1425 N ALA B 21 5823 5501 4879 -1057 1334 -1413 N ATOM 1426 CA ALA B 21 -14.368 24.457 20.344 1.00 42.80 C ANISOU 1426 CA ALA B 21 5763 5477 5020 -930 1423 -1582 C ATOM 1427 C ALA B 21 -14.345 25.783 19.584 1.00 44.90 C ANISOU 1427 C ALA B 21 5764 5652 5642 -613 1280 -1556 C ATOM 1428 O ALA B 21 -13.938 25.836 18.431 1.00 44.75 O ANISOU 1428 O ALA B 21 5707 5580 5717 -490 1078 -1343 O ATOM 1429 CB ALA B 21 -13.208 24.388 21.297 1.00 43.99 C ANISOU 1429 CB ALA B 21 6269 5477 4968 -982 1406 -1548 C ATOM 1430 N LYS B 22 -14.803 26.850 20.240 1.00 53.42 N ANISOU 1430 N LYS B 22 6666 6711 6919 -492 1395 -1778 N ATOM 1431 CA LYS B 22 -14.699 28.214 19.707 1.00 51.85 C ANISOU 1431 CA LYS B 22 6264 6340 7097 -184 1260 -1753 C ATOM 1432 C LYS B 22 -13.533 28.963 20.372 1.00 48.27 C ANISOU 1432 C LYS B 22 6038 5639 6663 -120 1222 -1779 C ATOM 1433 O LYS B 22 -13.242 28.728 21.538 1.00 51.10 O ANISOU 1433 O LYS B 22 6596 6022 6797 -278 1365 -1947 O ATOM 1434 CB LYS B 22 -16.008 28.976 19.918 1.00 47.15 C ANISOU 1434 CB LYS B 22 5283 5841 6792 -50 1396 -2013 C ATOM 1435 CG LYS B 22 -17.218 28.349 19.242 1.00 48.40 C ANISOU 1435 CG LYS B 22 5146 6275 6967 -105 1416 -2012 C ATOM 1436 CD LYS B 22 -18.417 29.282 19.273 1.00 59.37 C ANISOU 1436 CD LYS B 22 6089 7736 8732 113 1488 -2243 C ATOM 1437 CE LYS B 22 -19.555 28.739 20.150 1.00 76.49 C ANISOU 1437 CE LYS B 22 8069 10211 10782 -100 1800 -2582 C ATOM 1438 NZ LYS B 22 -19.743 29.469 21.451 1.00 82.28 N ANISOU 1438 NZ LYS B 22 8761 10911 11590 -74 2059 -2959 N ATOM 1439 N PHE B 23 -12.855 29.841 19.636 1.00 42.29 N ANISOU 1439 N PHE B 23 5257 4660 6151 84 1025 -1603 N ATOM 1440 CA PHE B 23 -11.754 30.625 20.215 1.00 42.01 C ANISOU 1440 CA PHE B 23 5405 4384 6171 127 983 -1644 C ATOM 1441 C PHE B 23 -12.242 31.971 20.683 1.00 48.42 C ANISOU 1441 C PHE B 23 6025 5025 7346 308 1062 -1893 C ATOM 1442 O PHE B 23 -12.739 32.772 19.886 1.00 50.40 O ANISOU 1442 O PHE B 23 6037 5152 7960 531 963 -1808 O ATOM 1443 CB PHE B 23 -10.619 30.838 19.218 1.00 39.91 C ANISOU 1443 CB PHE B 23 5241 3958 5966 201 747 -1323 C ATOM 1444 CG PHE B 23 -9.724 29.661 19.067 1.00 37.47 C ANISOU 1444 CG PHE B 23 5178 3746 5313 36 680 -1156 C ATOM 1445 CD1 PHE B 23 -8.418 29.717 19.504 1.00 36.10 C ANISOU 1445 CD1 PHE B 23 5228 3458 5032 -16 609 -1125 C ATOM 1446 CD2 PHE B 23 -10.194 28.488 18.487 1.00 43.53 C ANISOU 1446 CD2 PHE B 23 5937 4714 5887 -63 681 -1052 C ATOM 1447 CE1 PHE B 23 -7.595 28.631 19.366 1.00 34.10 C ANISOU 1447 CE1 PHE B 23 5172 3280 4505 -128 534 -984 C ATOM 1448 CE2 PHE B 23 -9.373 27.392 18.346 1.00 34.24 C ANISOU 1448 CE2 PHE B 23 4986 3582 4442 -189 619 -923 C ATOM 1449 CZ PHE B 23 -8.076 27.457 18.790 1.00 33.20 C ANISOU 1449 CZ PHE B 23 5064 3328 4224 -204 543 -886 C ATOM 1450 N VAL B 24 -12.071 32.252 21.967 1.00 46.39 N ANISOU 1450 N VAL B 24 5878 4747 7000 219 1226 -2203 N ATOM 1451 CA VAL B 24 -12.819 33.359 22.531 1.00 51.55 C ANISOU 1451 CA VAL B 24 6311 5292 7985 373 1369 -2545 C ATOM 1452 C VAL B 24 -12.001 34.625 22.789 1.00 62.09 C ANISOU 1452 C VAL B 24 7717 6273 9602 493 1294 -2639 C ATOM 1453 O VAL B 24 -12.536 35.722 22.715 1.00 66.27 O ANISOU 1453 O VAL B 24 8030 6582 10567 716 1315 -2801 O ATOM 1454 CB VAL B 24 -13.512 32.913 23.815 1.00 51.98 C ANISOU 1454 CB VAL B 24 6364 5612 7776 185 1665 -2924 C ATOM 1455 CG1 VAL B 24 -14.133 31.547 23.608 1.00 50.77 C ANISOU 1455 CG1 VAL B 24 6208 5783 7300 -9 1734 -2796 C ATOM 1456 CG2 VAL B 24 -12.532 32.840 24.924 1.00 57.84 C ANISOU 1456 CG2 VAL B 24 7421 6351 8206 -10 1715 -3061 C ATOM 1457 N GLY B 25 -10.709 34.489 23.058 1.00 65.83 N ANISOU 1457 N GLY B 25 8476 6673 9864 354 1196 -2539 N ATOM 1458 CA GLY B 25 -9.915 35.647 23.422 1.00 57.77 C ANISOU 1458 CA GLY B 25 7526 5337 9085 409 1145 -2675 C ATOM 1459 C GLY B 25 -8.617 35.729 22.658 1.00 49.64 C ANISOU 1459 C GLY B 25 6654 4142 8065 386 906 -2323 C ATOM 1460 O GLY B 25 -8.398 34.996 21.705 1.00 62.52 O ANISOU 1460 O GLY B 25 8306 5881 9566 373 776 -1969 O ATOM 1461 N THR B 26 -7.770 36.653 23.073 1.00 53.47 N ANISOU 1461 N THR B 26 7231 4372 8715 367 862 -2451 N ATOM 1462 CA THR B 26 -6.414 36.779 22.571 1.00 58.56 C ANISOU 1462 CA THR B 26 8019 4887 9343 290 668 -2187 C ATOM 1463 C THR B 26 -5.556 35.897 23.450 1.00 58.26 C ANISOU 1463 C THR B 26 8202 5099 8836 65 669 -2268 C ATOM 1464 O THR B 26 -5.854 35.740 24.632 1.00 68.76 O ANISOU 1464 O THR B 26 9597 6574 9955 -34 816 -2599 O ATOM 1465 CB THR B 26 -5.922 38.234 22.650 1.00 69.91 C ANISOU 1465 CB THR B 26 9442 5914 11207 346 622 -2308 C ATOM 1466 OG1 THR B 26 -7.028 39.115 22.434 1.00 72.95 O ANISOU 1466 OG1 THR B 26 9624 6069 12026 573 688 -2416 O ATOM 1467 CG2 THR B 26 -4.827 38.522 21.626 1.00 72.49 C ANISOU 1467 CG2 THR B 26 9822 6071 11649 310 419 -1923 C ATOM 1468 N PRO B 27 -4.492 35.311 22.899 1.00 50.30 N ANISOU 1468 N PRO B 27 7301 4159 7651 -14 503 -1973 N ATOM 1469 CA PRO B 27 -3.641 34.498 23.771 1.00 52.58 C ANISOU 1469 CA PRO B 27 7788 4665 7525 -193 467 -2041 C ATOM 1470 C PRO B 27 -2.894 35.336 24.805 1.00 53.93 C ANISOU 1470 C PRO B 27 8037 4733 7721 -302 459 -2344 C ATOM 1471 O PRO B 27 -2.626 36.508 24.553 1.00 49.37 O ANISOU 1471 O PRO B 27 7382 3863 7513 -256 431 -2408 O ATOM 1472 CB PRO B 27 -2.663 33.840 22.792 1.00 51.61 C ANISOU 1472 CB PRO B 27 7700 4597 7313 -204 285 -1675 C ATOM 1473 CG PRO B 27 -2.659 34.743 21.612 1.00 51.81 C ANISOU 1473 CG PRO B 27 7576 4382 7728 -90 225 -1477 C ATOM 1474 CD PRO B 27 -4.062 35.246 21.498 1.00 51.54 C ANISOU 1474 CD PRO B 27 7400 4249 7935 53 350 -1576 C ATOM 1475 N GLU B 28 -2.592 34.745 25.959 1.00 51.39 N ANISOU 1475 N GLU B 28 7876 4646 7005 -457 479 -2524 N ATOM 1476 CA GLU B 28 -1.748 35.389 26.956 1.00 49.05 C ANISOU 1476 CA GLU B 28 7665 4326 6645 -595 433 -2805 C ATOM 1477 C GLU B 28 -0.396 34.689 26.921 1.00 52.87 C ANISOU 1477 C GLU B 28 8257 4956 6876 -689 207 -2588 C ATOM 1478 O GLU B 28 -0.340 33.468 26.810 1.00 49.85 O ANISOU 1478 O GLU B 28 7964 4783 6196 -691 148 -2361 O ATOM 1479 CB GLU B 28 -2.363 35.310 28.351 1.00 53.59 C ANISOU 1479 CB GLU B 28 8314 5132 6916 -695 581 -3127 C ATOM 1480 CG GLU B 28 -3.813 35.725 28.456 1.00 63.09 C ANISOU 1480 CG GLU B 28 9367 6313 8292 -581 807 -3291 C ATOM 1481 CD GLU B 28 -4.458 35.229 29.752 1.00 77.08 C ANISOU 1481 CD GLU B 28 11208 8429 9650 -710 961 -3493 C ATOM 1482 OE1 GLU B 28 -5.111 34.157 29.734 1.00 77.99 O ANISOU 1482 OE1 GLU B 28 11372 8754 9508 -761 1055 -3386 O ATOM 1483 OE2 GLU B 28 -4.302 35.909 30.791 1.00 83.82 O ANISOU 1483 OE2 GLU B 28 12072 9346 10430 -780 991 -3748 O ATOM 1484 N VAL B 29 0.688 35.447 27.040 1.00 69.97 N ANISOU 1484 N VAL B 29 10404 7005 9177 -767 80 -2673 N ATOM 1485 CA VAL B 29 2.000 34.927 26.661 1.00 82.73 C ANISOU 1485 CA VAL B 29 12029 8721 10683 -809 -142 -2431 C ATOM 1486 C VAL B 29 2.748 34.114 27.735 1.00 82.41 C ANISOU 1486 C VAL B 29 12138 8985 10190 -932 -287 -2494 C ATOM 1487 O VAL B 29 3.495 33.222 27.366 1.00 88.42 O ANISOU 1487 O VAL B 29 12912 9879 10806 -898 -453 -2236 O ATOM 1488 CB VAL B 29 2.930 36.071 26.187 1.00 93.79 C ANISOU 1488 CB VAL B 29 13310 9880 12447 -864 -229 -2455 C ATOM 1489 CG1 VAL B 29 4.029 35.516 25.291 1.00 83.15 C ANISOU 1489 CG1 VAL B 29 11888 8619 11085 -855 -401 -2131 C ATOM 1490 CG2 VAL B 29 2.135 37.136 25.442 1.00102.14 C ANISOU 1490 CG2 VAL B 29 14259 10583 13965 -765 -93 -2454 C ATOM 1491 N ASN B 30 2.585 34.415 29.027 1.00 73.31 N ANISOU 1491 N ASN B 30 11091 7950 8815 -1069 -238 -2831 N ATOM 1492 CA ASN B 30 3.221 33.615 30.102 1.00 77.08 C ANISOU 1492 CA ASN B 30 11731 8749 8806 -1193 -400 -2856 C ATOM 1493 C ASN B 30 4.725 33.340 29.912 1.00 77.32 C ANISOU 1493 C ASN B 30 11709 8866 8803 -1208 -694 -2691 C ATOM 1494 O ASN B 30 5.094 32.209 29.577 1.00 67.78 O ANISOU 1494 O ASN B 30 10541 7780 7431 -1117 -833 -2384 O ATOM 1495 CB ASN B 30 2.484 32.264 30.242 1.00 74.52 C ANISOU 1495 CB ASN B 30 11564 8613 8138 -1152 -350 -2634 C ATOM 1496 CG ASN B 30 2.894 31.456 31.503 1.00 82.31 C ANISOU 1496 CG ASN B 30 12769 9922 8583 -1295 -495 -2645 C ATOM 1497 OD1 ASN B 30 4.013 31.562 32.016 1.00 64.34 O ANISOU 1497 OD1 ASN B 30 10501 7769 6177 -1366 -729 -2687 O ATOM 1498 ND2 ASN B 30 1.968 30.624 31.984 1.00 93.65 N ANISOU 1498 ND2 ASN B 30 14340 11513 9728 -1323 -365 -2555 N ATOM 1499 N GLN B 31 5.589 34.334 30.149 1.00 80.21 N ANISOU 1499 N GLN B 31 11972 9170 9332 -1324 -787 -2911 N ATOM 1500 CA GLN B 31 7.004 34.195 29.767 1.00 80.50 C ANISOU 1500 CA GLN B 31 11881 9277 9430 -1333 -1041 -2762 C ATOM 1501 C GLN B 31 7.797 33.370 30.788 1.00 79.71 C ANISOU 1501 C GLN B 31 11881 9526 8878 -1397 -1302 -2755 C ATOM 1502 O GLN B 31 8.958 33.033 30.574 1.00 76.40 O ANISOU 1502 O GLN B 31 11342 9224 8462 -1372 -1542 -2622 O ATOM 1503 CB GLN B 31 7.651 35.582 29.542 1.00 76.24 C ANISOU 1503 CB GLN B 31 11172 8526 9270 -1464 -1041 -2982 C ATOM 1504 CG GLN B 31 9.152 35.594 29.160 0.00 70.72 C ANISOU 1504 CG GLN B 31 10286 7920 8664 -1522 -1278 -2881 C ATOM 1505 CD GLN B 31 9.600 34.370 28.359 0.00 65.01 C ANISOU 1505 CD GLN B 31 9500 7341 7860 -1341 -1400 -2496 C ATOM 1506 OE1 GLN B 31 8.971 33.984 27.376 0.00 62.00 O ANISOU 1506 OE1 GLN B 31 9116 6832 7609 -1191 -1265 -2252 O ATOM 1507 NE2 GLN B 31 10.683 33.738 28.809 0.00 65.96 N ANISOU 1507 NE2 GLN B 31 9562 7738 7763 -1348 -1666 -2460 N ATOM 1508 N THR B 32 7.176 32.979 31.888 1.00 82.50 N ANISOU 1508 N THR B 32 12447 10070 8828 -1474 -1267 -2873 N ATOM 1509 CA THR B 32 7.908 32.081 32.765 1.00 78.47 C ANISOU 1509 CA THR B 32 12056 9887 7874 -1512 -1550 -2771 C ATOM 1510 C THR B 32 8.051 30.686 32.095 1.00 80.24 C ANISOU 1510 C THR B 32 12317 10127 8042 -1300 -1672 -2327 C ATOM 1511 O THR B 32 9.135 30.110 32.130 1.00 79.34 O ANISOU 1511 O THR B 32 12141 10154 7851 -1231 -1965 -2169 O ATOM 1512 CB THR B 32 7.261 31.996 34.181 1.00 82.01 C ANISOU 1512 CB THR B 32 12646 10585 7929 -1601 -1462 -2920 C ATOM 1513 OG1 THR B 32 8.264 31.625 35.128 1.00 90.18 O ANISOU 1513 OG1 THR B 32 13694 11935 8634 -1653 -1765 -2893 O ATOM 1514 CG2 THR B 32 6.087 31.015 34.265 1.00 77.80 C ANISOU 1514 CG2 THR B 32 12308 10086 7168 -1545 -1284 -2708 C ATOM 1515 N THR B 33 7.002 30.185 31.431 1.00 74.96 N ANISOU 1515 N THR B 33 11721 9303 7458 -1190 -1453 -2153 N ATOM 1516 CA THR B 33 7.003 28.832 30.850 1.00 65.90 C ANISOU 1516 CA THR B 33 10642 8146 6253 -1012 -1538 -1780 C ATOM 1517 C THR B 33 7.473 28.732 29.384 1.00 65.79 C ANISOU 1517 C THR B 33 10401 7956 6640 -832 -1545 -1600 C ATOM 1518 O THR B 33 8.042 27.717 28.981 1.00 69.08 O ANISOU 1518 O THR B 33 10806 8403 7037 -681 -1713 -1358 O ATOM 1519 CB THR B 33 5.591 28.192 30.923 1.00 82.86 C ANISOU 1519 CB THR B 33 12993 10251 8238 -1022 -1301 -1689 C ATOM 1520 OG1 THR B 33 5.631 26.864 30.388 1.00 80.53 O ANISOU 1520 OG1 THR B 33 12781 9914 7901 -872 -1393 -1348 O ATOM 1521 CG2 THR B 33 4.586 28.990 30.115 1.00 73.36 C ANISOU 1521 CG2 THR B 33 11663 8837 7374 -1003 -992 -1814 C ATOM 1522 N GLY B 34 7.224 29.766 28.585 1.00 55.06 N ANISOU 1522 N GLY B 34 8868 6413 5639 -849 -1362 -1714 N ATOM 1523 CA GLY B 34 7.534 29.727 27.165 1.00 45.43 C ANISOU 1523 CA GLY B 34 7451 5058 4750 -718 -1330 -1537 C ATOM 1524 C GLY B 34 6.319 29.448 26.292 1.00 47.22 C ANISOU 1524 C GLY B 34 7716 5135 5090 -633 -1098 -1405 C ATOM 1525 O GLY B 34 6.431 29.322 25.074 1.00 45.68 O ANISOU 1525 O GLY B 34 7383 4859 5115 -534 -1057 -1246 O ATOM 1526 N TYR B 35 5.151 29.361 26.918 1.00 46.11 N ANISOU 1526 N TYR B 35 7747 4991 4781 -688 -942 -1486 N ATOM 1527 CA TYR B 35 3.922 29.024 26.213 1.00 40.28 C ANISOU 1527 CA TYR B 35 7031 4153 4119 -621 -735 -1381 C ATOM 1528 C TYR B 35 2.865 30.107 26.305 1.00 48.60 C ANISOU 1528 C TYR B 35 8039 5085 5342 -676 -508 -1589 C ATOM 1529 O TYR B 35 2.741 30.778 27.310 1.00 64.78 O ANISOU 1529 O TYR B 35 10140 7166 7306 -791 -465 -1849 O ATOM 1530 CB TYR B 35 3.339 27.709 26.749 1.00 39.37 C ANISOU 1530 CB TYR B 35 7141 4145 3671 -626 -732 -1257 C ATOM 1531 CG TYR B 35 4.138 26.497 26.334 1.00 38.66 C ANISOU 1531 CG TYR B 35 7088 4087 3514 -507 -928 -1010 C ATOM 1532 CD1 TYR B 35 5.318 26.174 26.972 1.00 40.39 C ANISOU 1532 CD1 TYR B 35 7342 4416 3587 -490 -1189 -980 C ATOM 1533 CD2 TYR B 35 3.739 25.709 25.273 1.00 36.64 C ANISOU 1533 CD2 TYR B 35 6807 3750 3366 -399 -863 -832 C ATOM 1534 CE1 TYR B 35 6.051 25.091 26.594 1.00 40.22 C ANISOU 1534 CE1 TYR B 35 7328 4397 3557 -343 -1373 -778 C ATOM 1535 CE2 TYR B 35 4.476 24.633 24.878 1.00 36.42 C ANISOU 1535 CE2 TYR B 35 6800 3720 3318 -274 -1028 -656 C ATOM 1536 CZ TYR B 35 5.632 24.323 25.541 1.00 38.25 C ANISOU 1536 CZ TYR B 35 7061 4034 3436 -230 -1282 -628 C ATOM 1537 OH TYR B 35 6.376 23.219 25.162 1.00 40.12 O ANISOU 1537 OH TYR B 35 7301 4246 3696 -66 -1457 -468 O ATOM 1538 N GLN B 36 2.087 30.259 25.245 1.00 51.09 N ANISOU 1538 N GLN B 36 8246 5270 5898 -585 -370 -1485 N ATOM 1539 CA GLN B 36 0.923 31.130 25.256 1.00 45.65 C ANISOU 1539 CA GLN B 36 7493 4457 5396 -584 -163 -1652 C ATOM 1540 C GLN B 36 -0.329 30.264 25.286 1.00 49.31 C ANISOU 1540 C GLN B 36 8028 5013 5695 -570 -13 -1603 C ATOM 1541 O GLN B 36 -0.309 29.126 24.784 1.00 36.54 O ANISOU 1541 O GLN B 36 6468 3471 3946 -533 -66 -1377 O ATOM 1542 CB GLN B 36 0.924 32.015 24.022 1.00 43.91 C ANISOU 1542 CB GLN B 36 7079 4025 5580 -492 -143 -1547 C ATOM 1543 CG GLN B 36 1.395 31.226 22.812 1.00 52.66 C ANISOU 1543 CG GLN B 36 8129 5184 6696 -413 -237 -1236 C ATOM 1544 CD GLN B 36 0.927 31.790 21.502 1.00 47.59 C ANISOU 1544 CD GLN B 36 7328 4404 6350 -327 -179 -1072 C ATOM 1545 OE1 GLN B 36 0.072 32.672 21.452 1.00 52.53 O ANISOU 1545 OE1 GLN B 36 7887 4875 7199 -291 -75 -1156 O ATOM 1546 NE2 GLN B 36 1.486 31.280 20.424 1.00 41.28 N ANISOU 1546 NE2 GLN B 36 6463 3670 5553 -289 -254 -838 N ATOM 1547 N ARG B 37 -1.416 30.782 25.859 1.00 42.27 N ANISOU 1547 N ARG B 37 7118 4115 4827 -606 182 -1835 N ATOM 1548 CA ARG B 37 -2.644 29.996 25.903 1.00 39.53 C ANISOU 1548 CA ARG B 37 6802 3883 4333 -625 345 -1811 C ATOM 1549 C ARG B 37 -3.834 30.761 25.370 1.00 41.34 C ANISOU 1549 C ARG B 37 6823 4005 4880 -526 521 -1920 C ATOM 1550 O ARG B 37 -3.949 31.968 25.558 1.00 47.79 O ANISOU 1550 O ARG B 37 7530 4671 5958 -479 578 -2136 O ATOM 1551 CB ARG B 37 -2.946 29.507 27.327 1.00 41.67 C ANISOU 1551 CB ARG B 37 7269 4362 4200 -805 434 -1985 C ATOM 1552 CG ARG B 37 -3.203 30.608 28.322 1.00 44.59 C ANISOU 1552 CG ARG B 37 7608 4743 4590 -880 567 -2370 C ATOM 1553 CD ARG B 37 -3.817 30.086 29.587 1.00 48.88 C ANISOU 1553 CD ARG B 37 8317 5546 4709 -1078 722 -2543 C ATOM 1554 NE ARG B 37 -4.008 31.175 30.544 1.00 64.15 N ANISOU 1554 NE ARG B 37 10151 7530 6693 -1110 826 -2887 N ATOM 1555 CZ ARG B 37 -4.798 31.116 31.611 1.00 68.92 C ANISOU 1555 CZ ARG B 37 10752 8369 7065 -1225 1005 -3053 C ATOM 1556 NH1 ARG B 37 -5.495 30.019 31.870 1.00 67.25 N ANISOU 1556 NH1 ARG B 37 10640 8358 6554 -1349 1114 -2910 N ATOM 1557 NH2 ARG B 37 -4.899 32.162 32.414 1.00 75.81 N ANISOU 1557 NH2 ARG B 37 11526 9265 8014 -1231 1083 -3362 N ATOM 1558 N TYR B 38 -4.709 30.031 24.690 1.00 38.82 N ANISOU 1558 N TYR B 38 6443 3753 4554 -489 591 -1771 N ATOM 1559 CA TYR B 38 -5.977 30.554 24.227 1.00 39.63 C ANISOU 1559 CA TYR B 38 6325 3814 4917 -391 744 -1861 C ATOM 1560 C TYR B 38 -7.115 30.059 25.109 1.00 45.34 C ANISOU 1560 C TYR B 38 7065 4742 5419 -516 970 -2068 C ATOM 1561 O TYR B 38 -7.152 28.902 25.523 1.00 46.02 O ANISOU 1561 O TYR B 38 7329 5000 5156 -673 992 -1980 O ATOM 1562 CB TYR B 38 -6.263 30.132 22.790 1.00 37.60 C ANISOU 1562 CB TYR B 38 5942 3539 4806 -281 666 -1574 C ATOM 1563 CG TYR B 38 -5.255 30.554 21.758 1.00 36.14 C ANISOU 1563 CG TYR B 38 5717 3202 4812 -182 475 -1344 C ATOM 1564 CD1 TYR B 38 -4.166 29.745 21.453 1.00 40.42 C ANISOU 1564 CD1 TYR B 38 6393 3797 5168 -228 331 -1152 C ATOM 1565 CD2 TYR B 38 -5.417 31.737 21.041 1.00 36.99 C ANISOU 1565 CD2 TYR B 38 5644 3115 5295 -42 443 -1307 C ATOM 1566 CE1 TYR B 38 -3.248 30.113 20.466 1.00 47.95 C ANISOU 1566 CE1 TYR B 38 7282 4658 6279 -162 188 -958 C ATOM 1567 CE2 TYR B 38 -4.508 32.116 20.061 1.00 39.49 C ANISOU 1567 CE2 TYR B 38 5931 3316 5757 5 287 -1068 C ATOM 1568 CZ TYR B 38 -3.428 31.301 19.776 1.00 49.41 C ANISOU 1568 CZ TYR B 38 7303 4674 6797 -67 175 -908 C ATOM 1569 OH TYR B 38 -2.521 31.675 18.811 1.00 50.23 O ANISOU 1569 OH TYR B 38 7353 4707 7025 -46 53 -696 O ATOM 1570 N GLU B 39 -8.069 30.928 25.369 1.00 43.67 N ANISOU 1570 N GLU B 39 6659 4504 5431 -450 1143 -2340 N ATOM 1571 CA GLU B 39 -9.244 30.500 26.057 1.00 45.63 C ANISOU 1571 CA GLU B 39 6855 4976 5504 -569 1388 -2549 C ATOM 1572 C GLU B 39 -10.234 30.034 24.995 1.00 50.45 C ANISOU 1572 C GLU B 39 7257 5641 6270 -488 1413 -2388 C ATOM 1573 O GLU B 39 -10.331 30.612 23.917 1.00 53.07 O ANISOU 1573 O GLU B 39 7397 5814 6953 -282 1297 -2257 O ATOM 1574 CB GLU B 39 -9.764 31.639 26.921 1.00 52.47 C ANISOU 1574 CB GLU B 39 7586 5816 6532 -535 1580 -2980 C ATOM 1575 CG GLU B 39 -11.086 31.457 27.607 1.00 57.18 C ANISOU 1575 CG GLU B 39 8043 6659 7023 -635 1880 -3277 C ATOM 1576 CD GLU B 39 -11.559 32.784 28.188 1.00 73.36 C ANISOU 1576 CD GLU B 39 9879 8624 9372 -506 2014 -3663 C ATOM 1577 OE1 GLU B 39 -10.895 33.825 27.912 1.00 69.63 O ANISOU 1577 OE1 GLU B 39 9382 7850 9225 -335 1867 -3680 O ATOM 1578 OE2 GLU B 39 -12.592 32.788 28.898 1.00 81.66 O ANISOU 1578 OE2 GLU B 39 10771 9906 10350 -578 2234 -3887 O ATOM 1579 N ILE B 40 -10.925 28.947 25.290 1.00 53.35 N ANISOU 1579 N ILE B 40 7676 6243 6350 -676 1547 -2375 N ATOM 1580 CA ILE B 40 -11.829 28.328 24.345 1.00 58.40 C ANISOU 1580 CA ILE B 40 8136 6977 7078 -657 1565 -2236 C ATOM 1581 C ILE B 40 -13.096 27.867 25.052 1.00 62.18 C ANISOU 1581 C ILE B 40 8507 7722 7396 -846 1849 -2467 C ATOM 1582 O ILE B 40 -13.059 27.510 26.239 1.00 52.67 O ANISOU 1582 O ILE B 40 7497 6660 5855 -1072 2005 -2610 O ATOM 1583 CB ILE B 40 -11.180 27.118 23.643 1.00 46.79 C ANISOU 1583 CB ILE B 40 6870 5497 5409 -738 1391 -1891 C ATOM 1584 CG1 ILE B 40 -10.528 26.196 24.670 1.00 41.61 C ANISOU 1584 CG1 ILE B 40 6571 4906 4334 -970 1405 -1846 C ATOM 1585 CG2 ILE B 40 -10.142 27.577 22.642 1.00 47.88 C ANISOU 1585 CG2 ILE B 40 7010 5427 5754 -541 1138 -1668 C ATOM 1586 CD1 ILE B 40 -10.598 24.729 24.306 1.00 40.58 C ANISOU 1586 CD1 ILE B 40 6605 4829 3986 -1129 1370 -1617 C ATOM 1587 N LYS B 41 -14.216 27.903 24.334 1.00 47.81 N ANISOU 1587 N LYS B 41 6366 5995 5805 -766 1913 -2504 N ATOM 1588 CA LYS B 41 -15.418 27.263 24.819 1.00 57.69 C ANISOU 1588 CA LYS B 41 7489 7533 6897 -983 2175 -2682 C ATOM 1589 C LYS B 41 -15.571 26.008 24.018 1.00 57.42 C ANISOU 1589 C LYS B 41 7525 7569 6723 -1127 2088 -2406 C ATOM 1590 O LYS B 41 -15.629 26.056 22.798 1.00 64.33 O ANISOU 1590 O LYS B 41 8241 8375 7825 -959 1906 -2232 O ATOM 1591 CB LYS B 41 -16.669 28.134 24.677 1.00 65.75 C ANISOU 1591 CB LYS B 41 8050 8654 8278 -812 2327 -2975 C ATOM 1592 CG LYS B 41 -17.905 27.481 25.306 1.00 77.36 C ANISOU 1592 CG LYS B 41 9359 10472 9561 -1079 2641 -3208 C ATOM 1593 CD LYS B 41 -19.129 27.499 24.387 1.00 86.25 C ANISOU 1593 CD LYS B 41 10033 11748 10992 -966 2652 -3250 C ATOM 1594 CE LYS B 41 -20.249 26.613 24.935 1.00 89.81 C ANISOU 1594 CE LYS B 41 10352 12566 11207 -1310 2956 -3433 C ATOM 1595 NZ LYS B 41 -20.386 26.708 26.425 1.00 95.93 N ANISOU 1595 NZ LYS B 41 11236 13511 11702 -1538 3284 -3750 N ATOM 1596 N MET B 42 -15.613 24.881 24.705 1.00 56.49 N ANISOU 1596 N MET B 42 7662 7580 6222 -1452 2213 -2362 N ATOM 1597 CA MET B 42 -15.784 23.610 24.042 1.00 58.40 C ANISOU 1597 CA MET B 42 8000 7855 6336 -1626 2155 -2136 C ATOM 1598 C MET B 42 -17.254 23.470 23.676 1.00 55.81 C ANISOU 1598 C MET B 42 7292 7771 6141 -1711 2330 -2303 C ATOM 1599 O MET B 42 -18.112 23.869 24.456 1.00 54.69 O ANISOU 1599 O MET B 42 6950 7832 5996 -1796 2588 -2592 O ATOM 1600 CB MET B 42 -15.326 22.486 24.957 1.00 55.90 C ANISOU 1600 CB MET B 42 8106 7541 5592 -1944 2218 -2012 C ATOM 1601 CG MET B 42 -15.159 21.171 24.303 1.00 47.12 C ANISOU 1601 CG MET B 42 7186 6343 4374 -2092 2107 -1753 C ATOM 1602 SD MET B 42 -15.262 19.938 25.583 1.00 77.26 S ANISOU 1602 SD MET B 42 11403 10227 7726 -2534 2290 -1674 S ATOM 1603 CE MET B 42 -17.043 19.841 25.762 1.00 65.31 C ANISOU 1603 CE MET B 42 9527 9059 6228 -2806 2647 -1948 C ATOM 1604 N THR B 43 -17.542 22.934 22.492 1.00 52.91 N ANISOU 1604 N THR B 43 6798 7413 5891 -1689 2192 -2151 N ATOM 1605 CA THR B 43 -18.924 22.763 22.055 1.00 53.73 C ANISOU 1605 CA THR B 43 6509 7776 6128 -1776 2320 -2304 C ATOM 1606 C THR B 43 -19.291 21.282 21.984 1.00 57.83 C ANISOU 1606 C THR B 43 7189 8388 6395 -2158 2402 -2213 C ATOM 1607 O THR B 43 -20.460 20.925 22.066 1.00 65.59 O ANISOU 1607 O THR B 43 7915 9628 7378 -2374 2598 -2383 O ATOM 1608 CB THR B 43 -19.180 23.436 20.686 1.00 52.71 C ANISOU 1608 CB THR B 43 6030 7641 6358 -1455 2088 -2238 C ATOM 1609 OG1 THR B 43 -18.558 22.682 19.638 1.00 53.35 O ANISOU 1609 OG1 THR B 43 6287 7614 6368 -1471 1857 -1967 O ATOM 1610 CG2 THR B 43 -18.611 24.840 20.685 1.00 60.70 C ANISOU 1610 CG2 THR B 43 6970 8461 7631 -1087 1967 -2253 C ATOM 1611 N LYS B 44 -18.283 20.428 21.855 1.00 55.35 N ANISOU 1611 N LYS B 44 7292 7850 5889 -2244 2256 -1960 N ATOM 1612 CA LYS B 44 -18.478 18.993 21.736 1.00 58.30 C ANISOU 1612 CA LYS B 44 7876 8212 6063 -2586 2300 -1851 C ATOM 1613 C LYS B 44 -17.167 18.321 22.072 1.00 60.77 C ANISOU 1613 C LYS B 44 8696 8225 6167 -2615 2162 -1603 C ATOM 1614 O LYS B 44 -16.109 18.938 21.946 1.00 62.09 O ANISOU 1614 O LYS B 44 8969 8223 6399 -2332 1973 -1505 O ATOM 1615 CB LYS B 44 -18.917 18.596 20.318 1.00 69.69 C ANISOU 1615 CB LYS B 44 9087 9712 7681 -2554 2153 -1817 C ATOM 1616 CG LYS B 44 -20.380 18.872 19.985 1.00 86.77 C ANISOU 1616 CG LYS B 44 10747 12212 10010 -2621 2286 -2047 C ATOM 1617 CD LYS B 44 -21.050 17.739 19.223 1.00 94.79 C ANISOU 1617 CD LYS B 44 11690 13335 10993 -2908 2284 -2052 C ATOM 1618 CE LYS B 44 -22.371 18.215 18.607 1.00101.00 C ANISOU 1618 CE LYS B 44 11895 14479 12002 -2871 2315 -2263 C ATOM 1619 NZ LYS B 44 -22.893 17.391 17.469 1.00103.73 N ANISOU 1619 NZ LYS B 44 12089 14951 12374 -3039 2200 -2266 N ATOM 1620 N MET B 45 -17.221 17.059 22.486 1.00 62.61 N ANISOU 1620 N MET B 45 9237 8382 6171 -2955 2245 -1495 N ATOM 1621 CA MET B 45 -15.995 16.288 22.685 1.00 59.19 C ANISOU 1621 CA MET B 45 9273 7633 5585 -2955 2073 -1239 C ATOM 1622 C MET B 45 -16.133 14.892 22.072 1.00 63.00 C ANISOU 1622 C MET B 45 9929 7959 6050 -3183 2035 -1127 C ATOM 1623 O MET B 45 -17.162 14.252 22.224 1.00 66.72 O ANISOU 1623 O MET B 45 10340 8553 6457 -3525 2233 -1206 O ATOM 1624 CB MET B 45 -15.656 16.200 24.175 1.00 53.52 C ANISOU 1624 CB MET B 45 8879 6897 4558 -3126 2186 -1172 C ATOM 1625 CG MET B 45 -14.532 15.235 24.513 1.00 50.20 C ANISOU 1625 CG MET B 45 8952 6159 3962 -3167 2006 -881 C ATOM 1626 SD MET B 45 -14.182 15.199 26.287 1.00 69.54 S ANISOU 1626 SD MET B 45 11774 8654 5994 -3380 2107 -776 S ATOM 1627 CE MET B 45 -12.859 16.387 26.405 1.00 50.09 C ANISOU 1627 CE MET B 45 9298 6131 3604 -2952 1864 -784 C ATOM 1628 N TYR B 46 -15.102 14.422 21.379 1.00 52.47 N ANISOU 1628 N TYR B 46 8795 6352 4788 -3006 1794 -971 N ATOM 1629 CA TYR B 46 -15.177 13.128 20.704 1.00 50.04 C ANISOU 1629 CA TYR B 46 8644 5858 4511 -3188 1749 -912 C ATOM 1630 C TYR B 46 -14.240 12.111 21.332 1.00 53.03 C ANISOU 1630 C TYR B 46 9527 5871 4752 -3263 1654 -676 C ATOM 1631 O TYR B 46 -14.601 10.944 21.516 1.00 59.15 O ANISOU 1631 O TYR B 46 10538 6476 5459 -3578 1730 -606 O ATOM 1632 CB TYR B 46 -14.862 13.287 19.212 1.00 46.57 C ANISOU 1632 CB TYR B 46 7987 5417 4290 -2934 1558 -972 C ATOM 1633 CG TYR B 46 -15.882 14.143 18.500 1.00 48.73 C ANISOU 1633 CG TYR B 46 7771 6042 4701 -2880 1614 -1163 C ATOM 1634 CD1 TYR B 46 -17.206 13.724 18.400 1.00 48.29 C ANISOU 1634 CD1 TYR B 46 7504 6197 4647 -3190 1789 -1316 C ATOM 1635 CD2 TYR B 46 -15.535 15.373 17.941 1.00 43.37 C ANISOU 1635 CD2 TYR B 46 6834 5481 4164 -2527 1481 -1178 C ATOM 1636 CE1 TYR B 46 -18.160 14.502 17.764 1.00 48.66 C ANISOU 1636 CE1 TYR B 46 7070 6582 4836 -3117 1811 -1486 C ATOM 1637 CE2 TYR B 46 -16.489 16.161 17.292 1.00 43.80 C ANISOU 1637 CE2 TYR B 46 6443 5835 4365 -2452 1498 -1316 C ATOM 1638 CZ TYR B 46 -17.803 15.711 17.208 1.00 51.54 C ANISOU 1638 CZ TYR B 46 7197 7039 5348 -2734 1653 -1473 C ATOM 1639 OH TYR B 46 -18.778 16.455 16.577 1.00 55.21 O ANISOU 1639 OH TYR B 46 7190 7816 5970 -2645 1644 -1609 O ATOM 1640 N LYS B 47 -13.034 12.564 21.658 1.00 47.46 N ANISOU 1640 N LYS B 47 8977 5034 4021 -2974 1474 -549 N ATOM 1641 CA LYS B 47 -12.094 11.750 22.414 1.00 49.76 C ANISOU 1641 CA LYS B 47 9723 5008 4175 -2997 1350 -304 C ATOM 1642 C LYS B 47 -11.667 12.480 23.704 1.00 55.37 C ANISOU 1642 C LYS B 47 10557 5821 4658 -2957 1356 -220 C ATOM 1643 O LYS B 47 -11.454 13.692 23.715 1.00 50.43 O ANISOU 1643 O LYS B 47 9693 5389 4079 -2734 1338 -339 O ATOM 1644 CB LYS B 47 -10.885 11.399 21.540 1.00 46.52 C ANISOU 1644 CB LYS B 47 9396 4326 3952 -2684 1085 -236 C ATOM 1645 CG LYS B 47 -9.982 10.329 22.121 1.00 48.45 C ANISOU 1645 CG LYS B 47 10089 4187 4133 -2686 927 11 C ATOM 1646 CD LYS B 47 -8.917 9.831 21.130 1.00 47.24 C ANISOU 1646 CD LYS B 47 9968 3766 4214 -2389 701 11 C ATOM 1647 CE LYS B 47 -8.029 8.814 21.816 1.00 49.73 C ANISOU 1647 CE LYS B 47 10714 3683 4499 -2352 523 265 C ATOM 1648 NZ LYS B 47 -6.747 8.576 21.157 1.00 48.73 N ANISOU 1648 NZ LYS B 47 10590 3341 4584 -1982 282 264 N ATOM 1649 N GLY B 48 -11.580 11.744 24.803 1.00 63.73 N ANISOU 1649 N GLY B 48 11998 6756 5463 -3197 1384 -16 N ATOM 1650 CA GLY B 48 -10.978 12.284 26.009 1.00 57.68 C ANISOU 1650 CA GLY B 48 11405 6072 4438 -3157 1334 89 C ATOM 1651 C GLY B 48 -11.899 12.463 27.193 1.00 63.64 C ANISOU 1651 C GLY B 48 12124 7101 4956 -3447 1552 10 C ATOM 1652 O GLY B 48 -11.918 13.515 27.815 1.00 72.41 O ANISOU 1652 O GLY B 48 13087 8464 5963 -3390 1625 -128 O ATOM 1653 N PHE B 49 -12.647 11.426 27.528 1.00 67.81 N ANISOU 1653 N PHE B 49 12764 7576 5422 -3743 1642 73 N ATOM 1654 CA PHE B 49 -13.588 11.503 28.625 1.00 62.56 C ANISOU 1654 CA PHE B 49 12041 7182 4546 -4039 1855 -10 C ATOM 1655 C PHE B 49 -12.931 10.995 29.895 1.00 78.89 C ANISOU 1655 C PHE B 49 14459 9161 6357 -4098 1699 246 C ATOM 1656 O PHE B 49 -13.540 10.975 30.968 1.00 84.76 O ANISOU 1656 O PHE B 49 15220 10115 6870 -4355 1845 228 O ATOM 1657 CB PHE B 49 -14.834 10.716 28.282 1.00 64.90 C ANISOU 1657 CB PHE B 49 12238 7519 4903 -4351 2053 -98 C ATOM 1658 CG PHE B 49 -15.361 11.019 26.920 1.00 67.41 C ANISOU 1658 CG PHE B 49 12229 7895 5488 -4285 2145 -307 C ATOM 1659 CD1 PHE B 49 -16.288 12.038 26.737 1.00 63.72 C ANISOU 1659 CD1 PHE B 49 11328 7793 5092 -4307 2371 -604 C ATOM 1660 CD2 PHE B 49 -14.902 10.307 25.806 1.00 67.54 C ANISOU 1660 CD2 PHE B 49 12345 7609 5707 -4177 1989 -217 C ATOM 1661 CE1 PHE B 49 -16.769 12.332 25.471 1.00 65.87 C ANISOU 1661 CE1 PHE B 49 11269 8150 5608 -4238 2431 -778 C ATOM 1662 CE2 PHE B 49 -15.367 10.594 24.546 1.00 63.31 C ANISOU 1662 CE2 PHE B 49 11496 7155 5403 -4137 2058 -406 C ATOM 1663 CZ PHE B 49 -16.306 11.609 24.374 1.00 67.52 C ANISOU 1663 CZ PHE B 49 11595 8078 5982 -4175 2275 -670 C ATOM 1664 N GLN B 50 -11.671 10.594 29.766 1.00 79.99 N ANISOU 1664 N GLN B 50 14854 9003 6538 -3851 1394 481 N ATOM 1665 CA GLN B 50 -10.840 10.317 30.926 1.00 88.55 C ANISOU 1665 CA GLN B 50 16219 10033 7394 -3826 1192 726 C ATOM 1666 C GLN B 50 -9.946 11.526 31.201 1.00 98.61 C ANISOU 1666 C GLN B 50 17395 11457 8614 -3562 1074 650 C ATOM 1667 O GLN B 50 -8.738 11.507 30.951 1.00 90.40 O ANISOU 1667 O GLN B 50 16468 10222 7656 -3270 790 789 O ATOM 1668 CB GLN B 50 -10.023 9.050 30.714 1.00 82.53 C ANISOU 1668 CB GLN B 50 15767 8858 6732 -3707 911 1030 C ATOM 1669 CG GLN B 50 -10.878 7.814 30.401 1.00 81.19 C ANISOU 1669 CG GLN B 50 15698 8507 6644 -3963 1022 1093 C ATOM 1670 CD GLN B 50 -11.863 7.460 31.504 1.00 82.20 C ANISOU 1670 CD GLN B 50 15906 8834 6494 -4369 1226 1139 C ATOM 1671 OE1 GLN B 50 -12.904 8.105 31.668 1.00 78.69 O ANISOU 1671 OE1 GLN B 50 15217 8721 5959 -4588 1512 893 O ATOM 1672 NE2 GLN B 50 -11.538 6.421 32.267 1.00 89.24 N ANISOU 1672 NE2 GLN B 50 17125 9523 7260 -4467 1077 1458 N ATOM 1673 N ALA B 51 -10.598 12.585 31.684 1.00114.21 N ANISOU 1673 N ALA B 51 19126 13788 10481 -3664 1304 396 N ATOM 1674 CA ALA B 51 -9.981 13.813 32.180 1.00115.32 C ANISOU 1674 CA ALA B 51 19144 14132 10539 -3484 1253 262 C ATOM 1675 C ALA B 51 -11.001 14.509 33.081 1.00132.03 C ANISOU 1675 C ALA B 51 21059 16624 12484 -3720 1550 15 C ATOM 1676 O ALA B 51 -12.206 14.288 32.927 1.00139.22 O ANISOU 1676 O ALA B 51 21821 17644 13434 -3949 1809 -117 O ATOM 1677 CB ALA B 51 -9.562 14.717 31.052 1.00 99.31 C ANISOU 1677 CB ALA B 51 16893 12067 8774 -3175 1211 91 C ATOM 1678 N LEU B 52 -10.499 15.342 33.999 1.00135.13 N ANISOU 1678 N LEU B 52 21428 17215 12699 -3660 1507 -68 N ATOM 1679 CA LEU B 52 -11.259 16.038 35.060 1.00130.21 C ANISOU 1679 CA LEU B 52 20644 16954 11875 -3860 1756 -309 C ATOM 1680 C LEU B 52 -12.560 15.355 35.484 1.00129.24 C ANISOU 1680 C LEU B 52 20508 16969 11629 -4234 2023 -330 C ATOM 1681 O LEU B 52 -12.903 15.337 36.671 1.00131.54 O ANISOU 1681 O LEU B 52 20860 17496 11622 -4473 2135 -348 O ATOM 1682 CB LEU B 52 -11.555 17.500 34.653 1.00125.87 C ANISOU 1682 CB LEU B 52 19705 16578 11544 -3667 1916 -707 C ATOM 1683 CG LEU B 52 -12.703 18.062 33.781 1.00126.95 C ANISOU 1683 CG LEU B 52 19456 16804 11976 -3641 2184 -1013 C ATOM 1684 CD1 LEU B 52 -13.180 17.170 32.606 1.00136.95 C ANISOU 1684 CD1 LEU B 52 20721 17874 13440 -3681 2200 -889 C ATOM 1685 CD2 LEU B 52 -13.878 18.535 34.658 1.00129.10 C ANISOU 1685 CD2 LEU B 52 19497 17415 12143 -3868 2503 -1304 C ATOM 1686 N ASP B 57 -14.938 19.805 31.805 1.00 90.51 N ANISOU 1686 N ASP B 57 13867 12419 8104 -3389 2666 -1739 N ATOM 1687 CA ASP B 57 -14.778 20.649 30.633 1.00 87.58 C ANISOU 1687 CA ASP B 57 13250 11949 8079 -3057 2610 -1882 C ATOM 1688 C ASP B 57 -13.439 21.411 30.710 1.00 91.08 C ANISOU 1688 C ASP B 57 13825 12241 8539 -2786 2376 -1854 C ATOM 1689 O ASP B 57 -12.951 21.714 31.800 1.00 90.83 O ANISOU 1689 O ASP B 57 13922 12287 8302 -2832 2339 -1876 O ATOM 1690 CB ASP B 57 -15.965 21.611 30.521 1.00 96.39 C ANISOU 1690 CB ASP B 57 13899 13282 9442 -2993 2863 -2269 C ATOM 1691 CG ASP B 57 -16.020 22.337 29.185 1.00108.91 C ANISOU 1691 CG ASP B 57 15203 14764 11412 -2672 2815 -2395 C ATOM 1692 OD1 ASP B 57 -14.966 22.500 28.533 1.00118.41 O ANISOU 1692 OD1 ASP B 57 16563 15741 12688 -2457 2589 -2255 O ATOM 1693 OD2 ASP B 57 -17.132 22.734 28.773 1.00110.02 O ANISOU 1693 OD2 ASP B 57 14952 15060 11789 -2634 2994 -2635 O ATOM 1694 N ILE B 58 -12.855 21.700 29.543 1.00 92.46 N ANISOU 1694 N ILE B 58 13962 12217 8953 -2522 2215 -1813 N ATOM 1695 CA ILE B 58 -11.564 22.397 29.430 1.00 87.83 C ANISOU 1695 CA ILE B 58 13478 11463 8431 -2270 1975 -1787 C ATOM 1696 C ILE B 58 -11.744 23.811 28.858 1.00 73.35 C ANISOU 1696 C ILE B 58 11311 9598 6960 -2001 2026 -2092 C ATOM 1697 O ILE B 58 -12.562 24.038 27.951 1.00 63.25 O ANISOU 1697 O ILE B 58 9724 8315 5992 -1888 2099 -2166 O ATOM 1698 CB ILE B 58 -10.555 21.597 28.542 1.00 76.85 C ANISOU 1698 CB ILE B 58 12322 9816 7061 -2161 1695 -1465 C ATOM 1699 CG1 ILE B 58 -9.138 22.186 28.633 1.00 83.87 C ANISOU 1699 CG1 ILE B 58 13313 10563 7992 -1942 1423 -1407 C ATOM 1700 CG2 ILE B 58 -11.031 21.520 27.104 1.00 65.21 C ANISOU 1700 CG2 ILE B 58 10577 8240 5958 -2000 1664 -1427 C ATOM 1701 CD1 ILE B 58 -8.536 22.183 30.054 1.00 89.38 C ANISOU 1701 CD1 ILE B 58 14241 11374 8346 -2077 1367 -1387 C ATOM 1702 N ARG B 59 -10.980 24.761 29.398 1.00 65.20 N ANISOU 1702 N ARG B 59 10290 8520 5963 -1872 1930 -2213 N ATOM 1703 CA ARG B 59 -11.172 26.173 29.071 1.00 61.98 C ANISOU 1703 CA ARG B 59 9584 8039 5927 -1637 1985 -2517 C ATOM 1704 C ARG B 59 -10.014 26.799 28.274 1.00 51.35 C ANISOU 1704 C ARG B 59 8231 6414 4866 -1367 1696 -2381 C ATOM 1705 O ARG B 59 -10.088 27.948 27.847 1.00 52.03 O ANISOU 1705 O ARG B 59 8078 6365 5326 -1152 1688 -2543 O ATOM 1706 CB ARG B 59 -11.398 26.973 30.366 1.00 59.70 C ANISOU 1706 CB ARG B 59 9212 7909 5563 -1695 2114 -2787 C ATOM 1707 N PHE B 60 -8.940 26.051 28.083 1.00 45.68 N ANISOU 1707 N PHE B 60 7765 5601 3991 -1377 1455 -2077 N ATOM 1708 CA PHE B 60 -7.753 26.614 27.475 1.00 50.32 C ANISOU 1708 CA PHE B 60 8342 5975 4801 -1167 1198 -1963 C ATOM 1709 C PHE B 60 -6.994 25.606 26.642 1.00 53.46 C ANISOU 1709 C PHE B 60 8870 6267 5174 -1115 975 -1609 C ATOM 1710 O PHE B 60 -7.022 24.404 26.924 1.00 54.37 O ANISOU 1710 O PHE B 60 9204 6442 5012 -1267 963 -1441 O ATOM 1711 CB PHE B 60 -6.814 27.178 28.544 1.00 55.60 C ANISOU 1711 CB PHE B 60 9170 6668 5289 -1221 1119 -2106 C ATOM 1712 CG PHE B 60 -7.399 28.308 29.338 1.00 59.97 C ANISOU 1712 CG PHE B 60 9589 7295 5903 -1252 1331 -2516 C ATOM 1713 CD1 PHE B 60 -7.322 29.617 28.873 1.00 62.66 C ANISOU 1713 CD1 PHE B 60 9699 7435 6673 -1050 1318 -2696 C ATOM 1714 CD2 PHE B 60 -8.011 28.072 30.559 1.00 52.74 C ANISOU 1714 CD2 PHE B 60 8708 6640 4689 -1442 1496 -2634 C ATOM 1715 CE1 PHE B 60 -7.854 30.667 29.609 1.00 60.18 C ANISOU 1715 CE1 PHE B 60 9223 7156 6486 -1032 1481 -3048 C ATOM 1716 CE2 PHE B 60 -8.545 29.119 31.288 1.00 54.03 C ANISOU 1716 CE2 PHE B 60 8681 6882 4966 -1424 1660 -2971 C ATOM 1717 CZ PHE B 60 -8.465 30.414 30.818 1.00 53.98 C ANISOU 1717 CZ PHE B 60 8463 6654 5391 -1209 1648 -3186 C ATOM 1718 N VAL B 61 -6.307 26.125 25.626 1.00 44.94 N ANISOU 1718 N VAL B 61 7659 5020 4394 -909 806 -1507 N ATOM 1719 CA VAL B 61 -5.362 25.362 24.815 1.00 41.67 C ANISOU 1719 CA VAL B 61 7334 4511 3989 -829 590 -1230 C ATOM 1720 C VAL B 61 -4.000 26.021 24.892 1.00 38.88 C ANISOU 1720 C VAL B 61 6997 4064 3711 -729 395 -1217 C ATOM 1721 O VAL B 61 -3.894 27.231 24.767 1.00 40.17 O ANISOU 1721 O VAL B 61 7000 4152 4111 -648 408 -1354 O ATOM 1722 CB VAL B 61 -5.782 25.310 23.343 1.00 44.98 C ANISOU 1722 CB VAL B 61 7545 4871 4674 -702 579 -1111 C ATOM 1723 CG1 VAL B 61 -4.938 24.297 22.588 1.00 42.14 C ANISOU 1723 CG1 VAL B 61 7291 4453 4267 -657 405 -876 C ATOM 1724 CG2 VAL B 61 -7.251 24.977 23.225 1.00 51.95 C ANISOU 1724 CG2 VAL B 61 8317 5867 5553 -792 779 -1187 C ATOM 1725 N TYR B 62 -2.949 25.244 25.080 1.00 42.45 N ANISOU 1725 N TYR B 62 7628 4509 3992 -733 206 -1057 N ATOM 1726 CA TYR B 62 -1.622 25.838 25.127 1.00 43.62 C ANISOU 1726 CA TYR B 62 7750 4604 4220 -650 14 -1057 C ATOM 1727 C TYR B 62 -0.786 25.483 23.893 1.00 41.47 C ANISOU 1727 C TYR B 62 7381 4248 4128 -503 -138 -861 C ATOM 1728 O TYR B 62 -1.020 24.453 23.249 1.00 32.74 O ANISOU 1728 O TYR B 62 6317 3131 2992 -476 -141 -713 O ATOM 1729 CB TYR B 62 -0.890 25.400 26.387 1.00 37.60 C ANISOU 1729 CB TYR B 62 7218 3937 3131 -749 -119 -1059 C ATOM 1730 CG TYR B 62 -1.534 25.832 27.677 1.00 40.11 C ANISOU 1730 CG TYR B 62 7636 4390 3215 -923 28 -1283 C ATOM 1731 CD1 TYR B 62 -0.919 26.767 28.503 1.00 41.85 C ANISOU 1731 CD1 TYR B 62 7852 4666 3384 -972 -32 -1492 C ATOM 1732 CD2 TYR B 62 -2.747 25.286 28.090 1.00 41.51 C ANISOU 1732 CD2 TYR B 62 7906 4664 3203 -1066 238 -1311 C ATOM 1733 CE1 TYR B 62 -1.504 27.151 29.699 1.00 44.58 C ANISOU 1733 CE1 TYR B 62 8289 5169 3482 -1147 121 -1741 C ATOM 1734 CE2 TYR B 62 -3.333 25.659 29.272 1.00 43.85 C ANISOU 1734 CE2 TYR B 62 8281 5128 3254 -1245 403 -1541 C ATOM 1735 CZ TYR B 62 -2.711 26.588 30.080 1.00 48.49 C ANISOU 1735 CZ TYR B 62 8870 5778 3775 -1281 346 -1764 C ATOM 1736 OH TYR B 62 -3.299 26.953 31.275 1.00 50.03 O ANISOU 1736 OH TYR B 62 9085 6177 3746 -1444 517 -1996 O ATOM 1737 N THR B 63 0.193 26.340 23.601 1.00 33.49 N ANISOU 1737 N THR B 63 6240 3189 3296 -433 -249 -888 N ATOM 1738 CA THR B 63 1.059 26.219 22.446 1.00 32.09 C ANISOU 1738 CA THR B 63 5929 2973 3290 -318 -362 -743 C ATOM 1739 C THR B 63 2.282 27.105 22.618 1.00 32.83 C ANISOU 1739 C THR B 63 5924 3052 3496 -312 -493 -806 C ATOM 1740 O THR B 63 2.209 28.123 23.295 1.00 43.24 O ANISOU 1740 O THR B 63 7227 4338 4865 -385 -455 -976 O ATOM 1741 CB THR B 63 0.315 26.614 21.150 1.00 40.85 C ANISOU 1741 CB THR B 63 6860 4036 4627 -264 -245 -677 C ATOM 1742 OG1 THR B 63 1.243 26.710 20.068 1.00 45.90 O ANISOU 1742 OG1 THR B 63 7359 4674 5408 -189 -336 -558 O ATOM 1743 CG2 THR B 63 -0.336 27.942 21.312 1.00 31.57 C ANISOU 1743 CG2 THR B 63 5576 2781 3638 -283 -134 -808 C ATOM 1744 N PRO B 64 3.414 26.718 22.010 1.00 33.65 N ANISOU 1744 N PRO B 64 5946 3188 3652 -235 -637 -699 N ATOM 1745 CA PRO B 64 4.660 27.509 21.978 1.00 35.18 C ANISOU 1745 CA PRO B 64 5992 3395 3979 -248 -756 -749 C ATOM 1746 C PRO B 64 4.431 28.986 21.667 1.00 41.44 C ANISOU 1746 C PRO B 64 6652 4074 5021 -319 -654 -829 C ATOM 1747 O PRO B 64 3.587 29.308 20.833 1.00 34.55 O ANISOU 1747 O PRO B 64 5717 3121 4290 -293 -523 -754 O ATOM 1748 CB PRO B 64 5.459 26.854 20.855 1.00 32.38 C ANISOU 1748 CB PRO B 64 5503 3097 3702 -144 -824 -610 C ATOM 1749 CG PRO B 64 4.996 25.411 20.866 1.00 32.46 C ANISOU 1749 CG PRO B 64 5674 3121 3540 -62 -834 -522 C ATOM 1750 CD PRO B 64 3.592 25.377 21.417 1.00 31.57 C ANISOU 1750 CD PRO B 64 5728 2955 3311 -140 -692 -554 C ATOM 1751 N ALA B 65 5.174 29.867 22.330 1.00 47.25 N ANISOU 1751 N ALA B 65 7345 4790 5817 -409 -729 -976 N ATOM 1752 CA ALA B 65 4.901 31.295 22.260 1.00 49.87 C ANISOU 1752 CA ALA B 65 7596 4949 6405 -489 -633 -1086 C ATOM 1753 C ALA B 65 5.430 31.916 20.971 1.00 48.43 C ANISOU 1753 C ALA B 65 7225 4687 6489 -497 -623 -927 C ATOM 1754 O ALA B 65 5.074 33.031 20.614 1.00 43.38 O ANISOU 1754 O ALA B 65 6527 3852 6103 -542 -541 -931 O ATOM 1755 CB ALA B 65 5.489 31.999 23.462 1.00 45.67 C ANISOU 1755 CB ALA B 65 7098 4418 5836 -616 -711 -1337 C ATOM 1756 N MET B 66 6.279 31.183 20.273 1.00 46.85 N ANISOU 1756 N MET B 66 6933 4636 6232 -456 -703 -786 N ATOM 1757 CA MET B 66 6.860 31.683 19.043 1.00 44.80 C ANISOU 1757 CA MET B 66 6491 4368 6164 -499 -677 -633 C ATOM 1758 C MET B 66 6.484 30.817 17.853 1.00 38.37 C ANISOU 1758 C MET B 66 5641 3661 5278 -398 -617 -436 C ATOM 1759 O MET B 66 6.359 29.600 17.978 1.00 36.71 O ANISOU 1759 O MET B 66 5505 3567 4877 -292 -650 -437 O ATOM 1760 CB MET B 66 8.377 31.762 19.176 1.00 44.94 C ANISOU 1760 CB MET B 66 6361 4514 6202 -580 -802 -694 C ATOM 1761 CG MET B 66 8.832 32.992 19.925 1.00 51.23 C ANISOU 1761 CG MET B 66 7130 5180 7155 -748 -838 -867 C ATOM 1762 SD MET B 66 10.263 32.658 20.953 1.00 59.06 S ANISOU 1762 SD MET B 66 8035 6389 8015 -804 -1055 -1060 S ATOM 1763 CE MET B 66 9.529 31.629 22.227 1.00 95.09 C ANISOU 1763 CE MET B 66 12855 11026 12248 -673 -1135 -1153 C ATOM 1764 N GLU B 67 6.299 31.457 16.704 1.00 37.39 N ANISOU 1764 N GLU B 67 5414 3488 5303 -443 -535 -265 N ATOM 1765 CA GLU B 67 5.950 30.756 15.479 1.00 41.11 C ANISOU 1765 CA GLU B 67 5837 4096 5686 -380 -476 -92 C ATOM 1766 C GLU B 67 7.088 29.838 15.083 1.00 45.18 C ANISOU 1766 C GLU B 67 6242 4840 6086 -356 -523 -111 C ATOM 1767 O GLU B 67 6.881 28.694 14.674 1.00 44.52 O ANISOU 1767 O GLU B 67 6181 4881 5854 -252 -512 -103 O ATOM 1768 CB GLU B 67 5.652 31.768 14.389 1.00 36.59 C ANISOU 1768 CB GLU B 67 5179 3446 5276 -463 -407 118 C ATOM 1769 CG GLU B 67 5.477 31.230 13.006 1.00 49.18 C ANISOU 1769 CG GLU B 67 6697 5236 6753 -450 -354 306 C ATOM 1770 CD GLU B 67 5.480 32.346 11.972 1.00 63.11 C ANISOU 1770 CD GLU B 67 8379 6946 8655 -575 -317 557 C ATOM 1771 OE1 GLU B 67 6.525 32.550 11.320 1.00 69.33 O ANISOU 1771 OE1 GLU B 67 9041 7870 9432 -710 -294 637 O ATOM 1772 OE2 GLU B 67 4.447 33.034 11.822 1.00 70.58 O ANISOU 1772 OE2 GLU B 67 9379 7712 9727 -542 -314 682 O ATOM 1773 N SER B 68 8.296 30.358 15.265 1.00 46.84 N ANISOU 1773 N SER B 68 6318 5091 6387 -454 -578 -168 N ATOM 1774 CA SER B 68 9.533 29.707 14.872 1.00 45.50 C ANISOU 1774 CA SER B 68 5970 5151 6168 -437 -619 -214 C ATOM 1775 C SER B 68 9.683 28.334 15.499 1.00 49.28 C ANISOU 1775 C SER B 68 6522 5707 6496 -250 -724 -333 C ATOM 1776 O SER B 68 10.363 27.423 14.980 1.00 47.00 O ANISOU 1776 O SER B 68 6111 5590 6159 -153 -740 -369 O ATOM 1777 CB SER B 68 10.704 30.602 15.263 1.00 45.13 C ANISOU 1777 CB SER B 68 5764 5118 6264 -593 -678 -294 C ATOM 1778 OG SER B 68 11.796 29.821 15.687 1.00 56.51 O ANISOU 1778 OG SER B 68 7075 6745 7650 -509 -800 -440 O ATOM 1779 N VAL B 69 9.029 28.182 16.631 1.00 33.49 N ANISOU 1779 N VAL B 69 4728 3570 4427 -201 -791 -397 N ATOM 1780 CA VAL B 69 9.290 27.024 17.432 1.00 33.59 C ANISOU 1780 CA VAL B 69 4839 3622 4302 -56 -928 -477 C ATOM 1781 C VAL B 69 7.981 26.256 17.560 1.00 38.06 C ANISOU 1781 C VAL B 69 5637 4088 4734 15 -865 -426 C ATOM 1782 O VAL B 69 7.747 25.527 18.517 1.00 39.45 O ANISOU 1782 O VAL B 69 5995 4217 4775 79 -955 -459 O ATOM 1783 CB VAL B 69 9.935 27.439 18.786 1.00 43.18 C ANISOU 1783 CB VAL B 69 6080 4828 5498 -102 -1094 -601 C ATOM 1784 CG1 VAL B 69 8.907 28.007 19.764 1.00 50.07 C ANISOU 1784 CG1 VAL B 69 7172 5550 6304 -183 -1060 -651 C ATOM 1785 CG2 VAL B 69 10.721 26.287 19.379 1.00 49.50 C ANISOU 1785 CG2 VAL B 69 6887 5729 6194 59 -1293 -643 C ATOM 1786 N CYS B 70 7.155 26.418 16.528 1.00 40.92 N ANISOU 1786 N CYS B 70 5979 4441 5128 -15 -713 -332 N ATOM 1787 CA CYS B 70 5.968 25.592 16.270 1.00 39.16 C ANISOU 1787 CA CYS B 70 5904 4178 4798 37 -635 -288 C ATOM 1788 C CYS B 70 4.772 26.036 17.095 1.00 45.66 C ANISOU 1788 C CYS B 70 6890 4871 5589 -20 -582 -304 C ATOM 1789 O CYS B 70 3.914 25.232 17.460 1.00 49.72 O ANISOU 1789 O CYS B 70 7563 5349 5978 3 -551 -313 O ATOM 1790 CB CYS B 70 6.252 24.100 16.513 1.00 29.89 C ANISOU 1790 CB CYS B 70 4830 3016 3512 167 -718 -329 C ATOM 1791 SG CYS B 70 7.615 23.410 15.551 1.00 55.02 S ANISOU 1791 SG CYS B 70 7791 6353 6759 282 -763 -378 S ATOM 1792 N GLY B 71 4.707 27.330 17.366 1.00 42.95 N ANISOU 1792 N GLY B 71 6495 4452 5373 -104 -557 -324 N ATOM 1793 CA GLY B 71 3.543 27.880 18.011 1.00 29.77 C ANISOU 1793 CA GLY B 71 4928 2666 3719 -143 -477 -378 C ATOM 1794 C GLY B 71 2.370 28.023 17.066 1.00 37.82 C ANISOU 1794 C GLY B 71 5898 3672 4801 -127 -360 -275 C ATOM 1795 O GLY B 71 2.491 28.593 15.980 1.00 45.98 O ANISOU 1795 O GLY B 71 6792 4721 5957 -139 -340 -145 O ATOM 1796 N TYR B 72 1.220 27.510 17.487 1.00 33.96 N ANISOU 1796 N TYR B 72 5515 3174 4214 -118 -288 -323 N ATOM 1797 CA TYR B 72 -0.029 27.745 16.768 1.00 32.39 C ANISOU 1797 CA TYR B 72 5242 2976 4090 -102 -192 -257 C ATOM 1798 C TYR B 72 -0.559 29.152 16.970 1.00 41.09 C ANISOU 1798 C TYR B 72 6263 3932 5417 -98 -148 -289 C ATOM 1799 O TYR B 72 -0.930 29.537 18.085 1.00 51.08 O ANISOU 1799 O TYR B 72 7597 5114 6699 -118 -99 -463 O ATOM 1800 CB TYR B 72 -1.096 26.750 17.202 1.00 32.05 C ANISOU 1800 CB TYR B 72 5308 2984 3885 -119 -116 -324 C ATOM 1801 CG TYR B 72 -2.460 27.018 16.614 1.00 38.61 C ANISOU 1801 CG TYR B 72 6025 3845 4799 -106 -26 -295 C ATOM 1802 CD1 TYR B 72 -2.785 26.552 15.343 1.00 38.89 C ANISOU 1802 CD1 TYR B 72 5964 4001 4812 -92 -36 -170 C ATOM 1803 CD2 TYR B 72 -3.438 27.717 17.335 1.00 35.30 C ANISOU 1803 CD2 TYR B 72 5575 3360 4479 -105 66 -418 C ATOM 1804 CE1 TYR B 72 -4.037 26.778 14.793 1.00 35.26 C ANISOU 1804 CE1 TYR B 72 5374 3602 4419 -77 13 -138 C ATOM 1805 CE2 TYR B 72 -4.698 27.944 16.795 1.00 35.14 C ANISOU 1805 CE2 TYR B 72 5406 3385 4560 -68 131 -401 C ATOM 1806 CZ TYR B 72 -4.988 27.471 15.519 1.00 43.18 C ANISOU 1806 CZ TYR B 72 6326 4532 5550 -54 88 -245 C ATOM 1807 OH TYR B 72 -6.227 27.680 14.957 1.00 48.54 O ANISOU 1807 OH TYR B 72 6832 5289 6320 -15 118 -220 O ATOM 1808 N PHE B 73 -0.618 29.905 15.879 1.00 36.03 N ANISOU 1808 N PHE B 73 5483 3259 4948 -74 -163 -122 N ATOM 1809 CA PHE B 73 -1.260 31.207 15.877 1.00 35.50 C ANISOU 1809 CA PHE B 73 5333 3005 5149 -36 -137 -111 C ATOM 1810 C PHE B 73 -2.588 31.113 15.153 1.00 31.75 C ANISOU 1810 C PHE B 73 4758 2592 4715 42 -104 -15 C ATOM 1811 O PHE B 73 -2.663 30.624 14.032 1.00 38.02 O ANISOU 1811 O PHE B 73 5491 3545 5412 41 -142 165 O ATOM 1812 CB PHE B 73 -0.353 32.272 15.247 1.00 35.50 C ANISOU 1812 CB PHE B 73 5263 2880 5347 -78 -203 45 C ATOM 1813 CG PHE B 73 0.781 32.679 16.144 1.00 47.31 C ANISOU 1813 CG PHE B 73 6818 4280 6878 -164 -233 -106 C ATOM 1814 CD1 PHE B 73 1.852 31.815 16.374 1.00 49.65 C ANISOU 1814 CD1 PHE B 73 7155 4742 6965 -217 -285 -153 C ATOM 1815 CD2 PHE B 73 0.760 33.900 16.802 1.00 60.95 C ANISOU 1815 CD2 PHE B 73 8549 5749 8858 -185 -221 -229 C ATOM 1816 CE1 PHE B 73 2.898 32.176 17.223 1.00 47.03 C ANISOU 1816 CE1 PHE B 73 6850 4362 6656 -298 -341 -299 C ATOM 1817 CE2 PHE B 73 1.802 34.271 17.653 1.00 55.35 C ANISOU 1817 CE2 PHE B 73 7886 4979 8166 -292 -259 -400 C ATOM 1818 CZ PHE B 73 2.872 33.406 17.863 1.00 46.58 C ANISOU 1818 CZ PHE B 73 6798 4077 6822 -352 -328 -427 C ATOM 1819 N HIS B 74 -3.633 31.588 15.816 1.00 34.02 N ANISOU 1819 N HIS B 74 5010 2777 5140 105 -32 -163 N ATOM 1820 CA HIS B 74 -5.011 31.441 15.347 1.00 39.06 C ANISOU 1820 CA HIS B 74 5517 3501 5823 187 2 -131 C ATOM 1821 C HIS B 74 -5.396 32.581 14.414 1.00 40.18 C ANISOU 1821 C HIS B 74 5502 3507 6256 299 -84 81 C ATOM 1822 O HIS B 74 -5.498 33.719 14.847 1.00 45.51 O ANISOU 1822 O HIS B 74 6144 3922 7224 374 -80 17 O ATOM 1823 CB HIS B 74 -5.940 31.395 16.552 1.00 39.61 C ANISOU 1823 CB HIS B 74 5590 3553 5906 199 138 -419 C ATOM 1824 CG HIS B 74 -7.362 31.088 16.224 1.00 40.28 C ANISOU 1824 CG HIS B 74 5513 3776 6017 259 193 -441 C ATOM 1825 ND1 HIS B 74 -7.767 29.861 15.748 1.00 40.04 N ANISOU 1825 ND1 HIS B 74 5484 3986 5743 180 204 -388 N ATOM 1826 CD2 HIS B 74 -8.483 31.837 16.342 1.00 47.13 C ANISOU 1826 CD2 HIS B 74 6190 4576 7140 387 241 -539 C ATOM 1827 CE1 HIS B 74 -9.076 29.870 15.575 1.00 42.39 C ANISOU 1827 CE1 HIS B 74 5592 4385 6129 235 253 -445 C ATOM 1828 NE2 HIS B 74 -9.535 31.059 15.922 1.00 49.84 N ANISOU 1828 NE2 HIS B 74 6403 5154 7379 376 273 -534 N ATOM 1829 N ARG B 75 -5.606 32.284 13.138 1.00 47.96 N ANISOU 1829 N ARG B 75 6401 4659 7162 308 -172 333 N ATOM 1830 CA ARG B 75 -5.783 33.346 12.150 1.00 62.05 C ANISOU 1830 CA ARG B 75 8071 6327 9178 393 -293 618 C ATOM 1831 C ARG B 75 -7.224 33.866 12.110 1.00 61.31 C ANISOU 1831 C ARG B 75 7795 6176 9325 570 -318 605 C ATOM 1832 O ARG B 75 -7.462 35.080 12.019 1.00 63.88 O ANISOU 1832 O ARG B 75 8049 6226 9996 701 -388 708 O ATOM 1833 CB ARG B 75 -5.350 32.862 10.760 1.00 64.03 C ANISOU 1833 CB ARG B 75 8304 6826 9198 309 -386 907 C ATOM 1834 N SER B 76 -8.178 32.948 12.186 1.00 56.96 N ANISOU 1834 N SER B 76 7156 5870 8615 575 -263 470 N ATOM 1835 CA SER B 76 -9.595 33.304 12.169 1.00 64.18 C ANISOU 1835 CA SER B 76 7843 6797 9743 739 -278 416 C ATOM 1836 C SER B 76 -9.997 34.232 13.330 1.00 76.87 C ANISOU 1836 C SER B 76 9403 8113 11689 870 -175 148 C ATOM 1837 O SER B 76 -9.475 34.107 14.444 1.00 82.17 O ANISOU 1837 O SER B 76 10226 8700 12294 779 -33 -112 O ATOM 1838 CB SER B 76 -10.442 32.029 12.197 1.00 50.13 C ANISOU 1838 CB SER B 76 5988 5355 7705 656 -199 261 C ATOM 1839 OG SER B 76 -11.729 32.282 12.728 1.00 47.69 O ANISOU 1839 OG SER B 76 5464 5057 7600 778 -128 56 O ATOM 1840 N HIS B 77 -10.913 35.167 13.070 1.00 77.27 N ANISOU 1840 N HIS B 77 9239 8017 12101 1091 -255 201 N ATOM 1841 CA HIS B 77 -11.439 36.014 14.142 1.00 83.10 C ANISOU 1841 CA HIS B 77 9891 8494 13190 1240 -137 -116 C ATOM 1842 C HIS B 77 -12.935 35.751 14.304 1.00 81.95 C ANISOU 1842 C HIS B 77 9453 8548 13136 1370 -72 -314 C ATOM 1843 O HIS B 77 -13.699 36.556 14.852 1.00 61.72 O ANISOU 1843 O HIS B 77 6703 5805 10942 1571 -12 -538 O ATOM 1844 CB HIS B 77 -11.107 37.489 13.895 1.00 95.71 C ANISOU 1844 CB HIS B 77 11490 9646 15228 1407 -265 49 C ATOM 1845 CG HIS B 77 -9.654 37.801 14.102 1.00110.42 C ANISOU 1845 CG HIS B 77 13622 11303 17031 1238 -261 113 C ATOM 1846 ND1 HIS B 77 -8.960 37.394 15.225 1.00113.46 N ANISOU 1846 ND1 HIS B 77 14179 11713 17216 1067 -93 -203 N ATOM 1847 CD2 HIS B 77 -8.755 38.451 13.324 1.00114.31 C ANISOU 1847 CD2 HIS B 77 14225 11591 17614 1192 -409 461 C ATOM 1848 CE1 HIS B 77 -7.702 37.786 15.133 1.00111.05 C ANISOU 1848 CE1 HIS B 77 14055 11235 16905 939 -146 -75 C ATOM 1849 NE2 HIS B 77 -7.551 38.431 13.989 1.00115.16 N ANISOU 1849 NE2 HIS B 77 14540 11611 17603 998 -321 321 N ATOM 1850 N ASN B 78 -13.324 34.596 13.774 1.00100.16 N ANISOU 1850 N ASN B 78 11707 11237 15112 1245 -84 -241 N ATOM 1851 CA ASN B 78 -14.241 33.701 14.465 1.00113.60 C ANISOU 1851 CA ASN B 78 13289 13223 16650 1153 109 -561 C ATOM 1852 C ASN B 78 -15.666 34.340 14.638 1.00 73.17 C ANISOU 1852 C ASN B 78 7787 8111 11903 1395 135 -751 C ATOM 1853 O ASN B 78 -16.339 34.455 13.607 1.00 58.68 O ANISOU 1853 O ASN B 78 5718 6398 10182 1533 -61 -524 O ATOM 1854 CB ASN B 78 -13.500 33.264 15.743 1.00118.41 C ANISOU 1854 CB ASN B 78 14170 13786 17035 954 327 -835 C ATOM 1855 CG ASN B 78 -13.799 31.838 16.144 1.00121.22 C ANISOU 1855 CG ASN B 78 14595 14468 16997 710 479 -978 C ATOM 1856 OD1 ASN B 78 -14.916 31.350 15.973 1.00131.48 O ANISOU 1856 OD1 ASN B 78 15667 16012 18278 696 531 -1065 O ATOM 1857 ND2 ASN B 78 -12.794 31.160 16.687 1.00110.28 N ANISOU 1857 ND2 ASN B 78 13518 13075 15307 511 542 -998 N ATOM 1858 N ARG B 79 -16.208 34.720 15.813 1.00 80.76 N ANISOU 1858 N ARG B 79 8641 8995 13049 1456 356 -1157 N ATOM 1859 CA ARG B 79 -15.900 34.294 17.181 1.00 73.54 C ANISOU 1859 CA ARG B 79 7915 8117 11911 1250 636 -1520 C ATOM 1860 C ARG B 79 -16.757 33.067 17.449 1.00 69.58 C ANISOU 1860 C ARG B 79 7304 8029 11104 1046 805 -1688 C ATOM 1861 O ARG B 79 -16.624 32.390 18.462 1.00 66.48 O ANISOU 1861 O ARG B 79 7078 7761 10419 811 1031 -1923 O ATOM 1862 CB ARG B 79 -16.172 35.407 18.191 1.00 77.11 C ANISOU 1862 CB ARG B 79 8266 8310 12724 1421 788 -1886 C ATOM 1863 CG ARG B 79 -15.411 35.265 19.507 1.00 81.20 C ANISOU 1863 CG ARG B 79 9071 8781 13000 1207 1006 -2181 C ATOM 1864 CD ARG B 79 -14.046 35.961 19.466 1.00 89.80 C ANISOU 1864 CD ARG B 79 10443 9514 14161 1210 871 -2023 C ATOM 1865 NE ARG B 79 -14.164 37.412 19.319 1.00104.18 N ANISOU 1865 NE ARG B 79 12129 10928 16529 1493 787 -2063 N ATOM 1866 CZ ARG B 79 -14.356 38.266 20.326 1.00115.01 C ANISOU 1866 CZ ARG B 79 13447 12088 18162 1583 954 -2482 C ATOM 1867 NH1 ARG B 79 -14.457 39.570 20.088 1.00116.31 N ANISOU 1867 NH1 ARG B 79 13497 11824 18872 1855 854 -2493 N ATOM 1868 NH2 ARG B 79 -14.451 37.823 21.572 1.00118.64 N ANISOU 1868 NH2 ARG B 79 13977 12760 18340 1392 1222 -2893 N ATOM 1869 N SER B 80 -17.618 32.774 16.483 1.00 69.97 N ANISOU 1869 N SER B 80 7080 8296 11210 1117 675 -1538 N ATOM 1870 CA SER B 80 -18.613 31.717 16.589 1.00 67.30 C ANISOU 1870 CA SER B 80 6560 8350 10661 933 816 -1700 C ATOM 1871 C SER B 80 -18.263 30.466 15.763 1.00 64.48 C ANISOU 1871 C SER B 80 6373 8211 9916 690 709 -1444 C ATOM 1872 O SER B 80 -18.961 29.450 15.807 1.00 59.51 O ANISOU 1872 O SER B 80 5652 7883 9077 476 820 -1557 O ATOM 1873 CB SER B 80 -19.954 32.276 16.142 1.00 68.42 C ANISOU 1873 CB SER B 80 6207 8618 11170 1184 748 -1781 C ATOM 1874 OG SER B 80 -19.753 33.112 15.014 1.00 76.46 O ANISOU 1874 OG SER B 80 7146 9447 12460 1461 421 -1426 O ATOM 1875 N GLU B 81 -17.183 30.552 14.998 1.00 68.75 N ANISOU 1875 N GLU B 81 7152 8595 10374 711 504 -1119 N ATOM 1876 CA GLU B 81 -16.773 29.451 14.139 1.00 63.31 C ANISOU 1876 CA GLU B 81 6616 8091 9347 512 400 -905 C ATOM 1877 C GLU B 81 -16.223 28.318 14.984 1.00 53.28 C ANISOU 1877 C GLU B 81 5663 6856 7724 217 596 -1044 C ATOM 1878 O GLU B 81 -15.261 28.501 15.725 1.00 44.71 O ANISOU 1878 O GLU B 81 4850 5559 6577 189 659 -1072 O ATOM 1879 CB GLU B 81 -15.724 29.921 13.131 1.00 64.50 C ANISOU 1879 CB GLU B 81 6919 8083 9506 612 157 -547 C ATOM 1880 CG GLU B 81 -15.495 28.961 11.990 1.00 68.56 C ANISOU 1880 CG GLU B 81 7493 8834 9723 459 24 -341 C ATOM 1881 CD GLU B 81 -14.476 29.468 10.986 1.00 69.16 C ANISOU 1881 CD GLU B 81 7697 8801 9780 535 -185 1 C ATOM 1882 OE1 GLU B 81 -13.807 30.489 11.265 1.00 59.77 O ANISOU 1882 OE1 GLU B 81 6599 7315 8796 670 -215 88 O ATOM 1883 OE2 GLU B 81 -14.347 28.833 9.917 1.00 71.74 O ANISOU 1883 OE2 GLU B 81 8029 9352 9875 433 -306 165 O ATOM 1884 N GLU B 82 -16.843 27.149 14.888 1.00 51.02 N ANISOU 1884 N GLU B 82 5342 6828 7217 -10 679 -1125 N ATOM 1885 CA GLU B 82 -16.324 25.987 15.589 1.00 46.39 C ANISOU 1885 CA GLU B 82 5082 6241 6303 -293 831 -1199 C ATOM 1886 C GLU B 82 -15.110 25.392 14.861 1.00 47.86 C ANISOU 1886 C GLU B 82 5556 6335 6293 -345 676 -962 C ATOM 1887 O GLU B 82 -15.078 25.278 13.632 1.00 43.41 O ANISOU 1887 O GLU B 82 4900 5874 5719 -301 499 -790 O ATOM 1888 CB GLU B 82 -17.410 24.931 15.766 1.00 44.05 C ANISOU 1888 CB GLU B 82 4664 6210 5862 -549 989 -1369 C ATOM 1889 CG GLU B 82 -18.668 25.454 16.441 1.00 57.31 C ANISOU 1889 CG GLU B 82 6001 8043 7731 -515 1169 -1638 C ATOM 1890 CD GLU B 82 -19.627 24.343 16.834 1.00 71.68 C ANISOU 1890 CD GLU B 82 7744 10123 9368 -845 1379 -1824 C ATOM 1891 OE1 GLU B 82 -19.213 23.162 16.837 1.00 74.76 O ANISOU 1891 OE1 GLU B 82 8430 10498 9478 -1114 1409 -1751 O ATOM 1892 OE2 GLU B 82 -20.801 24.647 17.131 1.00 81.66 O ANISOU 1892 OE2 GLU B 82 8641 11597 10789 -839 1517 -2051 O ATOM 1893 N PHE B 83 -14.106 25.039 15.652 1.00 46.73 N ANISOU 1893 N PHE B 83 5746 6020 5988 -433 741 -970 N ATOM 1894 CA PHE B 83 -12.889 24.427 15.164 1.00 42.35 C ANISOU 1894 CA PHE B 83 5457 5369 5264 -473 624 -799 C ATOM 1895 C PHE B 83 -12.737 23.034 15.766 1.00 46.78 C ANISOU 1895 C PHE B 83 6283 5928 5563 -721 736 -870 C ATOM 1896 O PHE B 83 -13.096 22.798 16.923 1.00 47.28 O ANISOU 1896 O PHE B 83 6439 5983 5543 -853 906 -1011 O ATOM 1897 CB PHE B 83 -11.673 25.282 15.523 1.00 37.60 C ANISOU 1897 CB PHE B 83 5009 4539 4739 -330 555 -718 C ATOM 1898 CG PHE B 83 -11.537 26.515 14.705 1.00 37.09 C ANISOU 1898 CG PHE B 83 4760 4414 4918 -113 407 -568 C ATOM 1899 CD1 PHE B 83 -12.317 27.618 14.958 1.00 49.20 C ANISOU 1899 CD1 PHE B 83 6066 5902 6725 40 431 -647 C ATOM 1900 CD2 PHE B 83 -10.622 26.573 13.671 1.00 33.73 C ANISOU 1900 CD2 PHE B 83 4389 3970 4458 -66 246 -347 C ATOM 1901 CE1 PHE B 83 -12.190 28.759 14.188 1.00 47.34 C ANISOU 1901 CE1 PHE B 83 5686 5559 6740 242 273 -465 C ATOM 1902 CE2 PHE B 83 -10.489 27.695 12.911 1.00 34.58 C ANISOU 1902 CE2 PHE B 83 4355 4017 4768 97 109 -163 C ATOM 1903 CZ PHE B 83 -11.272 28.790 13.164 1.00 39.43 C ANISOU 1903 CZ PHE B 83 4770 4541 5670 254 109 -201 C ATOM 1904 N LEU B 84 -12.217 22.105 14.976 1.00 43.88 N ANISOU 1904 N LEU B 84 6042 5566 5064 -792 645 -772 N ATOM 1905 CA LEU B 84 -11.830 20.831 15.531 1.00 43.56 C ANISOU 1905 CA LEU B 84 6301 5428 4823 -984 712 -800 C ATOM 1906 C LEU B 84 -10.381 20.927 15.994 1.00 49.72 C ANISOU 1906 C LEU B 84 7339 5997 5556 -882 630 -705 C ATOM 1907 O LEU B 84 -9.494 21.299 15.220 1.00 51.71 O ANISOU 1907 O LEU B 84 7569 6213 5866 -732 491 -597 O ATOM 1908 CB LEU B 84 -11.998 19.703 14.518 1.00 38.85 C ANISOU 1908 CB LEU B 84 5716 4907 4137 -1111 666 -795 C ATOM 1909 CG LEU B 84 -11.619 18.385 15.188 1.00 39.28 C ANISOU 1909 CG LEU B 84 6107 4785 4033 -1299 733 -815 C ATOM 1910 CD1 LEU B 84 -12.675 17.349 14.956 1.00 38.17 C ANISOU 1910 CD1 LEU B 84 5932 4740 3830 -1562 833 -925 C ATOM 1911 CD2 LEU B 84 -10.245 17.897 14.751 1.00 35.07 C ANISOU 1911 CD2 LEU B 84 5782 4079 3465 -1191 597 -724 C ATOM 1912 N ILE B 85 -10.155 20.600 17.262 1.00 46.42 N ANISOU 1912 N ILE B 85 7152 5469 5016 -980 715 -744 N ATOM 1913 CA ILE B 85 -8.810 20.566 17.839 1.00 41.20 C ANISOU 1913 CA ILE B 85 6736 4631 4287 -902 619 -662 C ATOM 1914 C ILE B 85 -8.439 19.135 18.206 1.00 36.46 C ANISOU 1914 C ILE B 85 6436 3904 3512 -1043 609 -610 C ATOM 1915 O ILE B 85 -9.230 18.432 18.853 1.00 36.82 O ANISOU 1915 O ILE B 85 6593 3962 3434 -1258 740 -652 O ATOM 1916 CB ILE B 85 -8.701 21.429 19.111 1.00 42.95 C ANISOU 1916 CB ILE B 85 7006 4826 4485 -887 683 -735 C ATOM 1917 CG1 ILE B 85 -9.403 22.768 18.919 1.00 32.79 C ANISOU 1917 CG1 ILE B 85 5423 3628 3410 -773 738 -833 C ATOM 1918 CG2 ILE B 85 -7.245 21.585 19.537 1.00 40.66 C ANISOU 1918 CG2 ILE B 85 6901 4394 4152 -782 537 -653 C ATOM 1919 CD1 ILE B 85 -9.225 23.669 20.043 1.00 33.65 C ANISOU 1919 CD1 ILE B 85 5564 3693 3528 -745 800 -952 C ATOM 1920 N ALA B 86 -7.256 18.702 17.779 1.00 34.55 N ANISOU 1920 N ALA B 86 6316 3534 3279 -926 457 -520 N ATOM 1921 CA ALA B 86 -6.714 17.402 18.161 1.00 34.54 C ANISOU 1921 CA ALA B 86 6610 3345 3167 -996 405 -455 C ATOM 1922 C ALA B 86 -5.382 17.621 18.862 1.00 39.45 C ANISOU 1922 C ALA B 86 7384 3847 3758 -849 259 -370 C ATOM 1923 O ALA B 86 -4.384 17.939 18.210 1.00 43.28 O ANISOU 1923 O ALA B 86 7775 4319 4350 -665 135 -350 O ATOM 1924 CB ALA B 86 -6.541 16.502 16.947 1.00 32.00 C ANISOU 1924 CB ALA B 86 6269 2977 2912 -976 353 -473 C ATOM 1925 N GLY B 87 -5.354 17.465 20.183 1.00 34.59 N ANISOU 1925 N GLY B 87 6989 3176 2979 -948 273 -324 N ATOM 1926 CA GLY B 87 -4.123 17.734 20.906 1.00 41.18 C ANISOU 1926 CA GLY B 87 7943 3939 3763 -819 109 -251 C ATOM 1927 C GLY B 87 -3.751 16.793 22.026 1.00 45.90 C ANISOU 1927 C GLY B 87 8882 4396 4162 -904 24 -115 C ATOM 1928 O GLY B 87 -4.579 15.995 22.477 1.00 55.64 O ANISOU 1928 O GLY B 87 10299 5584 5259 -1118 133 -68 O ATOM 1929 N LYS B 88 -2.500 16.896 22.483 1.00 43.71 N ANISOU 1929 N LYS B 88 8683 4060 3864 -748 -181 -39 N ATOM 1930 CA LYS B 88 -1.990 16.026 23.542 1.00 45.03 C ANISOU 1930 CA LYS B 88 9176 4093 3841 -788 -328 136 C ATOM 1931 C LYS B 88 -2.179 16.665 24.915 1.00 46.54 C ANISOU 1931 C LYS B 88 9480 4442 3760 -937 -296 135 C ATOM 1932 O LYS B 88 -2.272 17.888 25.037 1.00 45.17 O ANISOU 1932 O LYS B 88 9109 4445 3608 -926 -220 -26 O ATOM 1933 CB LYS B 88 -0.520 15.679 23.301 1.00 43.51 C ANISOU 1933 CB LYS B 88 8988 3770 3774 -524 -599 217 C ATOM 1934 CG LYS B 88 -0.330 14.344 22.562 1.00 63.86 C ANISOU 1934 CG LYS B 88 11670 6090 6503 -438 -665 286 C ATOM 1935 CD LYS B 88 0.865 14.396 21.610 1.00 76.61 C ANISOU 1935 CD LYS B 88 13067 7677 8366 -148 -811 211 C ATOM 1936 CE LYS B 88 0.759 13.362 20.486 1.00 82.20 C ANISOU 1936 CE LYS B 88 13765 8202 9265 -86 -772 148 C ATOM 1937 NZ LYS B 88 1.267 13.902 19.173 1.00 71.22 N ANISOU 1937 NZ LYS B 88 12036 6958 8066 71 -736 -30 N ATOM 1938 N LEU B 89 -2.265 15.824 25.939 1.00 48.10 N ANISOU 1938 N LEU B 89 10007 4570 3699 -1091 -347 313 N ATOM 1939 CA LEU B 89 -2.479 16.293 27.303 1.00 49.10 C ANISOU 1939 CA LEU B 89 10279 4885 3493 -1278 -305 314 C ATOM 1940 C LEU B 89 -1.199 16.265 28.113 1.00 50.28 C ANISOU 1940 C LEU B 89 10577 5030 3496 -1154 -610 454 C ATOM 1941 O LEU B 89 -0.805 15.218 28.607 1.00 62.45 O ANISOU 1941 O LEU B 89 12410 6416 4902 -1164 -793 712 O ATOM 1942 CB LEU B 89 -3.534 15.442 27.988 1.00 58.07 C ANISOU 1942 CB LEU B 89 11688 6013 4365 -1598 -134 434 C ATOM 1943 CG LEU B 89 -4.537 16.230 28.812 1.00 63.15 C ANISOU 1943 CG LEU B 89 12281 6949 4763 -1857 138 254 C ATOM 1944 CD1 LEU B 89 -5.208 17.249 27.915 1.00 59.16 C ANISOU 1944 CD1 LEU B 89 11380 6558 4541 -1776 340 -39 C ATOM 1945 CD2 LEU B 89 -5.564 15.282 29.422 1.00 61.39 C ANISOU 1945 CD2 LEU B 89 12269 6728 4328 -2192 320 375 C ATOM 1946 N GLN B 90 -0.547 17.416 28.230 1.00 52.36 N ANISOU 1946 N GLN B 90 10634 5454 3805 -1038 -681 288 N ATOM 1947 CA GLN B 90 0.662 17.553 29.031 1.00 61.58 C ANISOU 1947 CA GLN B 90 11886 6684 4827 -939 -977 372 C ATOM 1948 C GLN B 90 0.298 18.099 30.395 1.00 62.67 C ANISOU 1948 C GLN B 90 12171 7075 4564 -1185 -908 304 C ATOM 1949 O GLN B 90 -0.187 19.231 30.496 1.00 56.13 O ANISOU 1949 O GLN B 90 11158 6420 3748 -1268 -707 27 O ATOM 1950 CB GLN B 90 1.671 18.489 28.364 1.00 75.94 C ANISOU 1950 CB GLN B 90 13383 8541 6931 -703 -1099 211 C ATOM 1951 CG GLN B 90 2.234 18.009 27.029 1.00 94.06 C ANISOU 1951 CG GLN B 90 15506 10645 9587 -456 -1179 252 C ATOM 1952 CD GLN B 90 3.589 18.638 26.713 1.00106.13 C ANISOU 1952 CD GLN B 90 16790 12233 11304 -242 -1389 176 C ATOM 1953 OE1 GLN B 90 4.298 19.101 27.618 1.00118.33 O ANISOU 1953 OE1 GLN B 90 18353 13917 12690 -253 -1567 159 O ATOM 1954 NE2 GLN B 90 3.949 18.669 25.427 1.00 92.55 N ANISOU 1954 NE2 GLN B 90 14826 10437 9902 -72 -1362 115 N ATOM 1955 N ASP B 91 0.523 17.294 31.434 1.00 69.33 N ANISOU 1955 N ASP B 91 13281 6346 6714 1474 -2057 -1261 N ATOM 1956 CA ASP B 91 0.322 17.719 32.819 1.00 72.33 C ANISOU 1956 CA ASP B 91 14003 6603 6878 1631 -2111 -1219 C ATOM 1957 C ASP B 91 -1.063 18.324 33.014 1.00 63.77 C ANISOU 1957 C ASP B 91 13057 5458 5713 1334 -1699 -1055 C ATOM 1958 O ASP B 91 -1.229 19.329 33.720 1.00 60.65 O ANISOU 1958 O ASP B 91 12650 5061 5332 1346 -1714 -1097 O ATOM 1959 CB ASP B 91 1.403 18.723 33.240 1.00 85.57 C ANISOU 1959 CB ASP B 91 15341 8393 8780 1838 -2481 -1479 C ATOM 1960 CG ASP B 91 2.790 18.093 33.336 1.00100.84 C ANISOU 1960 CG ASP B 91 17176 10363 10777 2195 -2911 -1674 C ATOM 1961 OD1 ASP B 91 2.908 17.016 33.956 1.00111.19 O ANISOU 1961 OD1 ASP B 91 18954 11507 11786 2451 -3029 -1569 O ATOM 1962 OD2 ASP B 91 3.759 18.665 32.786 1.00100.70 O ANISOU 1962 OD2 ASP B 91 16616 10524 11123 2219 -3118 -1939 O ATOM 1963 N GLY B 92 -2.048 17.721 32.352 1.00 58.00 N ANISOU 1963 N GLY B 92 12422 4687 4927 1066 -1332 -891 N ATOM 1964 CA GLY B 92 -3.436 18.100 32.535 1.00 54.28 C ANISOU 1964 CA GLY B 92 12084 4151 4387 783 -906 -752 C ATOM 1965 C GLY B 92 -3.874 19.306 31.742 1.00 54.82 C ANISOU 1965 C GLY B 92 11691 4361 4775 528 -776 -822 C ATOM 1966 O GLY B 92 -4.955 19.845 31.980 1.00 51.42 O ANISOU 1966 O GLY B 92 11306 3896 4334 328 -470 -753 O ATOM 1967 N LEU B 93 -3.038 19.719 30.793 1.00 56.23 N ANISOU 1967 N LEU B 93 11384 4715 5264 529 -991 -937 N ATOM 1968 CA LEU B 93 -3.344 20.854 29.925 1.00 55.68 C ANISOU 1968 CA LEU B 93 10734 4861 5562 286 -859 -900 C ATOM 1969 C LEU B 93 -3.331 20.481 28.449 1.00 52.67 C ANISOU 1969 C LEU B 93 9956 4647 5410 108 -757 -824 C ATOM 1970 O LEU B 93 -2.397 19.844 27.965 1.00 44.16 O ANISOU 1970 O LEU B 93 8791 3609 4377 223 -954 -905 O ATOM 1971 CB LEU B 93 -2.349 21.983 30.151 1.00 51.36 C ANISOU 1971 CB LEU B 93 9894 4394 5228 410 -1152 -1087 C ATOM 1972 CG LEU B 93 -2.201 22.408 31.598 1.00 52.01 C ANISOU 1972 CG LEU B 93 10347 4320 5095 631 -1326 -1202 C ATOM 1973 CD1 LEU B 93 -1.046 23.388 31.704 1.00 47.79 C ANISOU 1973 CD1 LEU B 93 9465 3873 4820 762 -1656 -1446 C ATOM 1974 CD2 LEU B 93 -3.516 23.003 32.093 1.00 46.44 C ANISOU 1974 CD2 LEU B 93 9791 3557 4296 455 -999 -1061 C ATOM 1975 N LEU B 94 -4.352 20.925 27.730 1.00 48.73 N ANISOU 1975 N LEU B 94 9209 4248 5059 -150 -468 -694 N ATOM 1976 CA LEU B 94 -4.443 20.648 26.309 1.00 44.51 C ANISOU 1976 CA LEU B 94 8330 3864 4717 -306 -370 -620 C ATOM 1977 C LEU B 94 -3.353 21.386 25.521 1.00 40.34 C ANISOU 1977 C LEU B 94 7379 3480 4469 -290 -550 -712 C ATOM 1978 O LEU B 94 -3.259 22.609 25.565 1.00 44.05 O ANISOU 1978 O LEU B 94 7636 3995 5105 -334 -565 -750 O ATOM 1979 CB LEU B 94 -5.826 21.023 25.790 1.00 47.82 C ANISOU 1979 CB LEU B 94 8604 4346 5220 -540 -63 -502 C ATOM 1980 CG LEU B 94 -6.021 20.606 24.337 1.00 43.46 C ANISOU 1980 CG LEU B 94 7768 3929 4816 -669 25 -432 C ATOM 1981 CD1 LEU B 94 -5.737 19.124 24.219 1.00 39.03 C ANISOU 1981 CD1 LEU B 94 7432 3301 4096 -615 6 -424 C ATOM 1982 CD2 LEU B 94 -7.415 20.932 23.872 1.00 41.01 C ANISOU 1982 CD2 LEU B 94 7321 3675 4584 -851 275 -369 C ATOM 1983 N HIS B 95 -2.524 20.631 24.806 1.00 40.98 N ANISOU 1983 N HIS B 95 7351 3617 4604 -235 -663 -762 N ATOM 1984 CA HIS B 95 -1.417 21.222 24.064 1.00 36.39 C ANISOU 1984 CA HIS B 95 6379 3153 4294 -239 -787 -887 C ATOM 1985 C HIS B 95 -1.508 20.962 22.578 1.00 36.20 C ANISOU 1985 C HIS B 95 6096 3251 4407 -399 -631 -792 C ATOM 1986 O HIS B 95 -1.784 19.836 22.140 1.00 34.59 O ANISOU 1986 O HIS B 95 6007 3048 4086 -400 -579 -719 O ATOM 1987 CB HIS B 95 -0.077 20.693 24.569 1.00 38.37 C ANISOU 1987 CB HIS B 95 6675 3371 4535 7 -1105 -1119 C ATOM 1988 CG HIS B 95 0.549 21.554 25.613 1.00 54.24 C ANISOU 1988 CG HIS B 95 8686 5328 6596 152 -1324 -1314 C ATOM 1989 ND1 HIS B 95 0.240 21.443 26.951 1.00 57.62 N ANISOU 1989 ND1 HIS B 95 9528 5606 6760 329 -1440 -1332 N ATOM 1990 CD2 HIS B 95 1.452 22.555 25.513 1.00 57.93 C ANISOU 1990 CD2 HIS B 95 8802 5860 7350 141 -1432 -1516 C ATOM 1991 CE1 HIS B 95 0.936 22.336 27.633 1.00 58.21 C ANISOU 1991 CE1 HIS B 95 9495 5668 6952 445 -1650 -1540 C ATOM 1992 NE2 HIS B 95 1.678 23.022 26.785 1.00 59.35 N ANISOU 1992 NE2 HIS B 95 9159 5944 7449 323 -1647 -1665 N ATOM 1993 N ILE B 96 -1.249 22.005 21.801 1.00 34.41 N ANISOU 1993 N ILE B 96 5552 3107 4414 -528 -552 -801 N ATOM 1994 CA ILE B 96 -1.116 21.842 20.368 1.00 33.55 C ANISOU 1994 CA ILE B 96 5227 3097 4424 -651 -420 -738 C ATOM 1995 C ILE B 96 0.083 22.602 19.854 1.00 38.61 C ANISOU 1995 C ILE B 96 5568 3781 5321 -697 -441 -896 C ATOM 1996 O ILE B 96 0.646 23.471 20.532 1.00 35.60 O ANISOU 1996 O ILE B 96 5102 3361 5065 -669 -531 -1044 O ATOM 1997 CB ILE B 96 -2.360 22.313 19.603 1.00 32.10 C ANISOU 1997 CB ILE B 96 5025 2945 4228 -807 -199 -542 C ATOM 1998 CG1 ILE B 96 -2.545 23.818 19.741 1.00 33.07 C ANISOU 1998 CG1 ILE B 96 5051 3040 4472 -878 -140 -534 C ATOM 1999 CG2 ILE B 96 -3.607 21.590 20.090 1.00 31.56 C ANISOU 1999 CG2 ILE B 96 5195 2836 3960 -801 -132 -438 C ATOM 2000 CD1 ILE B 96 -3.802 24.303 19.118 1.00 34.67 C ANISOU 2000 CD1 ILE B 96 5267 3260 4645 -969 19 -377 C ATOM 2001 N THR B 97 0.472 22.228 18.646 1.00 34.29 N ANISOU 2001 N THR B 97 4867 3307 4856 -775 -339 -884 N ATOM 2002 CA THR B 97 1.435 22.967 17.856 1.00 35.30 C ANISOU 2002 CA THR B 97 4719 3462 5230 -891 -235 -1005 C ATOM 2003 C THR B 97 0.814 23.328 16.524 1.00 34.32 C ANISOU 2003 C THR B 97 4590 3357 5094 -1054 21 -806 C ATOM 2004 O THR B 97 -0.296 22.923 16.215 1.00 35.33 O ANISOU 2004 O THR B 97 4876 3500 5048 -1051 69 -613 O ATOM 2005 CB THR B 97 2.679 22.166 17.568 1.00 36.68 C ANISOU 2005 CB THR B 97 4719 3695 5521 -819 -334 -1228 C ATOM 2006 OG1 THR B 97 2.326 21.089 16.680 1.00 40.54 O ANISOU 2006 OG1 THR B 97 5285 4241 5878 -821 -266 -1094 O ATOM 2007 CG2 THR B 97 3.274 21.635 18.868 1.00 38.00 C ANISOU 2007 CG2 THR B 97 4950 3834 5654 -585 -655 -1444 C ATOM 2008 N THR B 98 1.565 24.061 15.720 1.00 45.79 N ANISOU 2008 N THR B 98 5871 4796 6732 -1190 190 -880 N ATOM 2009 CA THR B 98 1.136 24.393 14.383 1.00 55.06 C ANISOU 2009 CA THR B 98 7100 5957 7862 -1316 430 -707 C ATOM 2010 C THR B 98 1.067 23.116 13.502 1.00 57.52 C ANISOU 2010 C THR B 98 7440 6357 8059 -1275 441 -647 C ATOM 2011 O THR B 98 0.447 23.118 12.441 1.00 50.40 O ANISOU 2011 O THR B 98 6648 5455 7045 -1321 579 -481 O ATOM 2012 CB THR B 98 2.071 25.478 13.780 1.00 51.75 C ANISOU 2012 CB THR B 98 6546 5459 7660 -1492 659 -819 C ATOM 2013 OG1 THR B 98 1.667 25.789 12.441 1.00 62.55 O ANISOU 2013 OG1 THR B 98 8059 6777 8929 -1591 902 -639 O ATOM 2014 CG2 THR B 98 3.513 25.025 13.796 1.00 43.02 C ANISOU 2014 CG2 THR B 98 5166 4401 6777 -1513 647 -1116 C ATOM 2015 N CYS B 99 1.667 22.020 13.965 1.00 55.03 N ANISOU 2015 N CYS B 99 7054 6104 7752 -1162 269 -790 N ATOM 2016 CA CYS B 99 1.571 20.741 13.262 1.00 44.43 C ANISOU 2016 CA CYS B 99 5755 4834 6293 -1108 254 -742 C ATOM 2017 C CYS B 99 0.311 19.952 13.604 1.00 43.82 C ANISOU 2017 C CYS B 99 5897 4762 5989 -1024 158 -573 C ATOM 2018 O CYS B 99 -0.023 18.990 12.930 1.00 49.29 O ANISOU 2018 O CYS B 99 6652 5501 6576 -1002 172 -504 O ATOM 2019 CB CYS B 99 2.792 19.867 13.564 1.00 38.00 C ANISOU 2019 CB CYS B 99 4786 4068 5584 -1003 102 -992 C ATOM 2020 SG CYS B 99 4.362 20.639 13.168 1.00118.77 S ANISOU 2020 SG CYS B 99 14675 14305 16148 -1120 237 -1289 S ATOM 2021 N SER B 100 -0.368 20.333 14.673 1.00 43.67 N ANISOU 2021 N SER B 100 5992 4690 5911 -986 76 -533 N ATOM 2022 CA SER B 100 -1.534 19.588 15.127 1.00 34.57 C ANISOU 2022 CA SER B 100 5040 3522 4572 -937 33 -419 C ATOM 2023 C SER B 100 -2.622 19.657 14.092 1.00 30.00 C ANISOU 2023 C SER B 100 4489 2979 3929 -1013 169 -265 C ATOM 2024 O SER B 100 -2.606 20.525 13.255 1.00 37.30 O ANISOU 2024 O SER B 100 5348 3911 4914 -1078 276 -215 O ATOM 2025 CB SER B 100 -2.056 20.147 16.455 1.00 34.62 C ANISOU 2025 CB SER B 100 5165 3454 4537 -902 -31 -421 C ATOM 2026 OG SER B 100 -1.102 20.006 17.488 1.00 41.83 O ANISOU 2026 OG SER B 100 6098 4322 5473 -785 -206 -583 O ATOM 2027 N PHE B 101 -3.586 18.751 14.167 1.00 37.88 N ANISOU 2027 N PHE B 101 5607 3983 4802 -996 164 -209 N ATOM 2028 CA PHE B 101 -4.779 18.863 13.345 1.00 37.84 C ANISOU 2028 CA PHE B 101 5607 4015 4756 -1041 250 -117 C ATOM 2029 C PHE B 101 -5.769 19.845 13.955 1.00 43.59 C ANISOU 2029 C PHE B 101 6358 4708 5498 -1061 277 -90 C ATOM 2030 O PHE B 101 -6.535 19.500 14.848 1.00 45.39 O ANISOU 2030 O PHE B 101 6669 4901 5677 -1068 284 -113 O ATOM 2031 CB PHE B 101 -5.464 17.511 13.158 1.00 41.80 C ANISOU 2031 CB PHE B 101 6184 4535 5163 -1038 253 -118 C ATOM 2032 CG PHE B 101 -6.383 17.477 11.976 1.00 43.81 C ANISOU 2032 CG PHE B 101 6389 4854 5404 -1055 300 -79 C ATOM 2033 CD1 PHE B 101 -7.684 17.932 12.079 1.00 44.37 C ANISOU 2033 CD1 PHE B 101 6442 4928 5487 -1072 327 -89 C ATOM 2034 CD2 PHE B 101 -5.928 17.031 10.744 1.00 44.24 C ANISOU 2034 CD2 PHE B 101 6410 4964 5437 -1034 303 -62 C ATOM 2035 CE1 PHE B 101 -8.527 17.917 10.980 1.00 45.00 C ANISOU 2035 CE1 PHE B 101 6468 5068 5560 -1042 316 -100 C ATOM 2036 CE2 PHE B 101 -6.761 17.018 9.640 1.00 41.18 C ANISOU 2036 CE2 PHE B 101 6007 4626 5013 -1012 310 -44 C ATOM 2037 CZ PHE B 101 -8.061 17.463 9.757 1.00 41.86 C ANISOU 2037 CZ PHE B 101 6072 4717 5114 -1003 296 -71 C ATOM 2038 N VAL B 102 -5.742 21.076 13.465 1.00 45.95 N ANISOU 2038 N VAL B 102 6605 4998 5857 -1074 312 -50 N ATOM 2039 CA VAL B 102 -6.707 22.088 13.864 1.00 37.38 C ANISOU 2039 CA VAL B 102 5535 3881 4787 -1069 322 -32 C ATOM 2040 C VAL B 102 -7.347 22.673 12.606 1.00 37.09 C ANISOU 2040 C VAL B 102 5502 3862 4728 -1033 342 24 C ATOM 2041 O VAL B 102 -6.655 23.142 11.705 1.00 36.91 O ANISOU 2041 O VAL B 102 5509 3812 4703 -1036 388 76 O ATOM 2042 CB VAL B 102 -6.045 23.215 14.681 1.00 35.15 C ANISOU 2042 CB VAL B 102 5246 3526 4585 -1083 313 -53 C ATOM 2043 CG1 VAL B 102 -7.071 24.269 15.048 1.00 42.73 C ANISOU 2043 CG1 VAL B 102 6229 4451 5557 -1064 319 -38 C ATOM 2044 CG2 VAL B 102 -5.367 22.654 15.908 1.00 29.45 C ANISOU 2044 CG2 VAL B 102 4553 2777 3860 -1066 243 -134 C ATOM 2045 N ALA B 103 -8.667 22.657 12.542 1.00 43.23 N ANISOU 2045 N ALA B 103 6268 4672 5488 -989 312 -9 N ATOM 2046 CA ALA B 103 -9.353 23.077 11.334 1.00 42.02 C ANISOU 2046 CA ALA B 103 6142 4534 5289 -896 270 8 C ATOM 2047 C ALA B 103 -10.782 23.473 11.643 1.00 43.51 C ANISOU 2047 C ALA B 103 6271 4744 5515 -828 208 -91 C ATOM 2048 O ALA B 103 -11.391 22.948 12.580 1.00 38.29 O ANISOU 2048 O ALA B 103 5525 4112 4910 -889 242 -185 O ATOM 2049 CB ALA B 103 -9.327 21.956 10.300 1.00 42.30 C ANISOU 2049 CB ALA B 103 6174 4638 5261 -876 255 3 C ATOM 2050 N PRO B 104 -11.333 24.390 10.841 1.00 45.50 N ANISOU 2050 N PRO B 104 6587 4970 5730 -693 123 -88 N ATOM 2051 CA PRO B 104 -12.737 24.765 11.000 1.00 44.26 C ANISOU 2051 CA PRO B 104 6339 4849 5631 -588 26 -236 C ATOM 2052 C PRO B 104 -13.642 23.578 10.732 1.00 40.35 C ANISOU 2052 C PRO B 104 5684 4464 5183 -588 -7 -398 C ATOM 2053 O PRO B 104 -13.515 22.972 9.680 1.00 42.08 O ANISOU 2053 O PRO B 104 5939 4718 5331 -534 -61 -386 O ATOM 2054 CB PRO B 104 -12.928 25.852 9.943 1.00 40.89 C ANISOU 2054 CB PRO B 104 6083 4348 5104 -395 -95 -192 C ATOM 2055 CG PRO B 104 -11.530 26.316 9.622 1.00 33.89 C ANISOU 2055 CG PRO B 104 5392 3350 4135 -469 20 1 C ATOM 2056 CD PRO B 104 -10.704 25.101 9.718 1.00 32.62 C ANISOU 2056 CD PRO B 104 5146 3257 3992 -617 119 30 C ATOM 2057 N TRP B 105 -14.525 23.251 11.672 1.00 41.78 N ANISOU 2057 N TRP B 105 5701 4686 5487 -663 52 -561 N ATOM 2058 CA TRP B 105 -15.424 22.109 11.528 1.00 39.70 C ANISOU 2058 CA TRP B 105 5265 4507 5310 -712 75 -757 C ATOM 2059 C TRP B 105 -16.134 22.074 10.165 1.00 40.97 C ANISOU 2059 C TRP B 105 5363 4738 5467 -521 -124 -887 C ATOM 2060 O TRP B 105 -16.176 21.035 9.498 1.00 42.85 O ANISOU 2060 O TRP B 105 5558 5028 5695 -540 -139 -940 O ATOM 2061 CB TRP B 105 -16.453 22.109 12.664 1.00 41.10 C ANISOU 2061 CB TRP B 105 5278 4696 5642 -809 194 -960 C ATOM 2062 CG TRP B 105 -17.384 20.951 12.626 1.00 36.02 C ANISOU 2062 CG TRP B 105 4447 4114 5124 -912 284 -1197 C ATOM 2063 CD1 TRP B 105 -18.691 20.964 12.240 1.00 39.24 C ANISOU 2063 CD1 TRP B 105 4601 4605 5703 -839 210 -1505 C ATOM 2064 CD2 TRP B 105 -17.078 19.592 12.962 1.00 40.77 C ANISOU 2064 CD2 TRP B 105 5101 4684 5707 -1105 468 -1179 C ATOM 2065 NE1 TRP B 105 -19.225 19.694 12.322 1.00 41.85 N ANISOU 2065 NE1 TRP B 105 4796 4960 6146 -1010 367 -1691 N ATOM 2066 CE2 TRP B 105 -18.253 18.834 12.762 1.00 44.56 C ANISOU 2066 CE2 TRP B 105 5353 5220 6358 -1176 534 -1475 C ATOM 2067 CE3 TRP B 105 -15.926 18.940 13.416 1.00 39.83 C ANISOU 2067 CE3 TRP B 105 5203 4485 5447 -1210 570 -966 C ATOM 2068 CZ2 TRP B 105 -18.306 17.457 12.998 1.00 46.19 C ANISOU 2068 CZ2 TRP B 105 5582 5382 6584 -1375 735 -1536 C ATOM 2069 CZ3 TRP B 105 -15.982 17.567 13.646 1.00 39.42 C ANISOU 2069 CZ3 TRP B 105 5194 4391 5391 -1368 731 -1020 C ATOM 2070 CH2 TRP B 105 -17.163 16.847 13.442 1.00 40.76 C ANISOU 2070 CH2 TRP B 105 5170 4596 5719 -1462 830 -1288 C ATOM 2071 N ASN B 106 -16.672 23.211 9.745 1.00 43.45 N ANISOU 2071 N ASN B 106 5700 5039 5772 -312 -298 -946 N ATOM 2072 CA ASN B 106 -17.408 23.280 8.489 1.00 48.97 C ANISOU 2072 CA ASN B 106 6380 5786 6439 -66 -542 -1100 C ATOM 2073 C ASN B 106 -16.549 22.954 7.267 1.00 45.33 C ANISOU 2073 C ASN B 106 6154 5294 5775 12 -602 -917 C ATOM 2074 O ASN B 106 -17.036 22.411 6.281 1.00 39.59 O ANISOU 2074 O ASN B 106 5397 4627 5020 152 -759 -1053 O ATOM 2075 CB ASN B 106 -18.031 24.665 8.318 1.00 50.69 C ANISOU 2075 CB ASN B 106 6662 5958 6641 185 -740 -1177 C ATOM 2076 CG ASN B 106 -19.144 24.922 9.303 1.00 50.66 C ANISOU 2076 CG ASN B 106 6369 6014 6866 157 -720 -1450 C ATOM 2077 OD1 ASN B 106 -19.568 24.014 10.018 1.00 46.81 O ANISOU 2077 OD1 ASN B 106 5637 5600 6551 -53 -544 -1608 O ATOM 2078 ND2 ASN B 106 -19.632 26.164 9.344 1.00 57.93 N ANISOU 2078 ND2 ASN B 106 7339 6888 7785 368 -882 -1518 N ATOM 2079 N SER B 107 -15.266 23.278 7.343 1.00 45.40 N ANISOU 2079 N SER B 107 6387 5209 5655 -81 -469 -637 N ATOM 2080 CA SER B 107 -14.391 23.121 6.194 1.00 43.55 C ANISOU 2080 CA SER B 107 6396 4925 5227 -20 -477 -469 C ATOM 2081 C SER B 107 -13.980 21.655 5.974 1.00 45.52 C ANISOU 2081 C SER B 107 6549 5255 5490 -158 -392 -473 C ATOM 2082 O SER B 107 -13.420 21.306 4.933 1.00 47.64 O ANISOU 2082 O SER B 107 6978 5510 5613 -98 -409 -386 O ATOM 2083 CB SER B 107 -13.161 24.007 6.357 1.00 36.24 C ANISOU 2083 CB SER B 107 5701 3864 4204 -97 -328 -223 C ATOM 2084 OG SER B 107 -12.188 23.337 7.118 1.00 53.42 O ANISOU 2084 OG SER B 107 7785 6061 6452 -335 -138 -136 O ATOM 2085 N LEU B 108 -14.282 20.800 6.947 1.00 47.13 N ANISOU 2085 N LEU B 108 6527 5526 5856 -338 -290 -579 N ATOM 2086 CA LEU B 108 -14.010 19.364 6.837 1.00 44.66 C ANISOU 2086 CA LEU B 108 6141 5267 5560 -466 -211 -603 C ATOM 2087 C LEU B 108 -14.930 18.680 5.842 1.00 40.61 C ANISOU 2087 C LEU B 108 5527 4836 5066 -341 -369 -809 C ATOM 2088 O LEU B 108 -16.042 19.142 5.595 1.00 38.51 O ANISOU 2088 O LEU B 108 5150 4609 4873 -187 -533 -1014 O ATOM 2089 CB LEU B 108 -14.153 18.682 8.201 1.00 36.64 C ANISOU 2089 CB LEU B 108 4990 4250 4681 -684 -39 -664 C ATOM 2090 CG LEU B 108 -13.091 19.162 9.176 1.00 39.52 C ANISOU 2090 CG LEU B 108 5472 4536 5010 -787 85 -477 C ATOM 2091 CD1 LEU B 108 -13.360 18.659 10.596 1.00 39.42 C ANISOU 2091 CD1 LEU B 108 5403 4490 5085 -956 238 -544 C ATOM 2092 CD2 LEU B 108 -11.722 18.758 8.677 1.00 31.12 C ANISOU 2092 CD2 LEU B 108 4543 3450 3833 -809 119 -308 C ATOM 2093 N SER B 109 -14.478 17.559 5.287 1.00 39.49 N ANISOU 2093 N SER B 109 5408 4723 4873 -394 -337 -785 N ATOM 2094 CA SER B 109 -15.340 16.765 4.413 1.00 41.98 C ANISOU 2094 CA SER B 109 5605 5118 5230 -297 -483 -1010 C ATOM 2095 C SER B 109 -16.387 16.012 5.231 1.00 51.58 C ANISOU 2095 C SER B 109 6533 6378 6686 -456 -400 -1277 C ATOM 2096 O SER B 109 -16.305 15.967 6.460 1.00 49.95 O ANISOU 2096 O SER B 109 6284 6126 6568 -652 -202 -1243 O ATOM 2097 CB SER B 109 -14.515 15.788 3.587 1.00 36.33 C ANISOU 2097 CB SER B 109 5009 4409 4385 -312 -461 -908 C ATOM 2098 OG SER B 109 -13.984 14.766 4.398 1.00 41.33 O ANISOU 2098 OG SER B 109 5595 5025 5085 -545 -265 -859 O ATOM 2099 N LEU B 110 -17.382 15.437 4.560 1.00 60.58 N ANISOU 2099 N LEU B 110 7489 7595 7934 -375 -539 -1566 N ATOM 2100 CA LEU B 110 -18.381 14.648 5.266 1.00 59.74 C ANISOU 2100 CA LEU B 110 7097 7515 8087 -567 -406 -1862 C ATOM 2101 C LEU B 110 -17.681 13.448 5.871 1.00 54.92 C ANISOU 2101 C LEU B 110 6577 6833 7459 -835 -144 -1731 C ATOM 2102 O LEU B 110 -17.832 13.156 7.064 1.00 53.77 O ANISOU 2102 O LEU B 110 6400 6616 7412 -1062 104 -1753 O ATOM 2103 CB LEU B 110 -19.510 14.194 4.343 1.00 69.12 C ANISOU 2103 CB LEU B 110 8041 8799 9422 -431 -616 -2242 C ATOM 2104 CG LEU B 110 -20.543 13.316 5.060 1.00 69.56 C ANISOU 2104 CG LEU B 110 7773 8866 9789 -682 -416 -2595 C ATOM 2105 CD1 LEU B 110 -21.390 14.155 6.010 1.00 80.04 C ANISOU 2105 CD1 LEU B 110 8896 10202 11313 -728 -335 -2782 C ATOM 2106 CD2 LEU B 110 -21.410 12.561 4.097 1.00 61.06 C ANISOU 2106 CD2 LEU B 110 6455 7877 8869 -594 -595 -2971 C ATOM 2107 N ALA B 111 -16.889 12.776 5.040 1.00 45.83 N ANISOU 2107 N ALA B 111 5577 5684 6155 -787 -201 -1594 N ATOM 2108 CA ALA B 111 -16.116 11.623 5.478 1.00 40.98 C ANISOU 2108 CA ALA B 111 5088 4993 5490 -983 -4 -1465 C ATOM 2109 C ALA B 111 -15.160 11.966 6.617 1.00 49.60 C ANISOU 2109 C ALA B 111 6364 5991 6492 -1093 164 -1208 C ATOM 2110 O ALA B 111 -14.736 11.088 7.340 1.00 52.15 O ANISOU 2110 O ALA B 111 6798 6222 6795 -1256 337 -1151 O ATOM 2111 CB ALA B 111 -15.341 11.049 4.331 1.00 36.72 C ANISOU 2111 CB ALA B 111 4680 4482 4790 -870 -121 -1356 C ATOM 2112 N GLN B 112 -14.785 13.230 6.762 1.00 46.32 N ANISOU 2112 N GLN B 112 6007 5581 6009 -986 98 -1063 N ATOM 2113 CA GLN B 112 -13.902 13.602 7.857 1.00 42.89 C ANISOU 2113 CA GLN B 112 5721 5064 5512 -1075 228 -863 C ATOM 2114 C GLN B 112 -14.704 13.816 9.147 1.00 47.56 C ANISOU 2114 C GLN B 112 6240 5601 6231 -1215 384 -978 C ATOM 2115 O GLN B 112 -14.239 13.484 10.231 1.00 48.43 O ANISOU 2115 O GLN B 112 6493 5609 6299 -1342 542 -892 O ATOM 2116 CB GLN B 112 -13.100 14.847 7.502 1.00 38.34 C ANISOU 2116 CB GLN B 112 5244 4496 4826 -934 127 -674 C ATOM 2117 CG GLN B 112 -11.765 14.556 6.837 1.00 38.24 C ANISOU 2117 CG GLN B 112 5380 4478 4673 -892 112 -497 C ATOM 2118 CD GLN B 112 -11.144 15.779 6.157 1.00 34.29 C ANISOU 2118 CD GLN B 112 4981 3973 4075 -764 48 -360 C ATOM 2119 OE1 GLN B 112 -11.828 16.766 5.864 1.00 33.63 O ANISOU 2119 OE1 GLN B 112 4892 3893 3992 -651 -42 -397 O ATOM 2120 NE2 GLN B 112 -9.846 15.705 5.893 1.00 32.80 N ANISOU 2120 NE2 GLN B 112 4898 3759 3803 -779 106 -221 N ATOM 2121 N ARG B 113 -15.921 14.335 9.033 1.00 48.76 N ANISOU 2121 N ARG B 113 6182 5811 6532 -1177 337 -1198 N ATOM 2122 CA ARG B 113 -16.750 14.521 10.217 1.00 50.69 C ANISOU 2122 CA ARG B 113 6335 6008 6917 -1324 521 -1346 C ATOM 2123 C ARG B 113 -17.295 13.171 10.703 1.00 58.37 C ANISOU 2123 C ARG B 113 7286 6905 7987 -1557 764 -1518 C ATOM 2124 O ARG B 113 -17.133 12.831 11.876 1.00 65.28 O ANISOU 2124 O ARG B 113 8330 7648 8825 -1728 1002 -1463 O ATOM 2125 CB ARG B 113 -17.877 15.518 9.942 1.00 47.36 C ANISOU 2125 CB ARG B 113 5667 5677 6649 -1197 389 -1572 C ATOM 2126 CG ARG B 113 -17.383 16.936 9.643 1.00 47.96 C ANISOU 2126 CG ARG B 113 5838 5774 6612 -983 193 -1393 C ATOM 2127 CD ARG B 113 -18.549 17.890 9.380 1.00 57.64 C ANISOU 2127 CD ARG B 113 6851 7073 7977 -817 29 -1640 C ATOM 2128 NE ARG B 113 -18.477 18.503 8.058 1.00 64.87 N ANISOU 2128 NE ARG B 113 7833 8037 8780 -530 -271 -1611 N ATOM 2129 CZ ARG B 113 -19.187 18.109 7.007 1.00 69.66 C ANISOU 2129 CZ ARG B 113 8306 8723 9438 -378 -469 -1842 C ATOM 2130 NH1 ARG B 113 -20.046 17.105 7.123 1.00 82.85 N ANISOU 2130 NH1 ARG B 113 9712 10448 11319 -511 -386 -2145 N ATOM 2131 NH2 ARG B 113 -19.049 18.729 5.843 1.00 62.46 N ANISOU 2131 NH2 ARG B 113 7548 7820 8363 -89 -742 -1787 N ATOM 2132 N ARG B 114 -17.929 12.396 9.823 1.00 58.47 N ANISOU 2132 N ARG B 114 7129 6977 8112 -1563 713 -1733 N ATOM 2133 CA ARG B 114 -18.121 10.979 10.129 1.00 65.61 C ANISOU 2133 CA ARG B 114 8092 7774 9062 -1789 949 -1837 C ATOM 2134 C ARG B 114 -16.687 10.539 10.284 1.00 64.69 C ANISOU 2134 C ARG B 114 8314 7571 8693 -1764 941 -1504 C ATOM 2135 O ARG B 114 -15.833 11.000 9.552 1.00 67.33 O ANISOU 2135 O ARG B 114 8699 7983 8899 -1576 721 -1320 O ATOM 2136 CB ARG B 114 -18.869 10.199 9.021 1.00 52.37 C ANISOU 2136 CB ARG B 114 6178 6179 7540 -1779 856 -2117 C ATOM 2137 N GLY B 115 -16.361 9.723 11.261 1.00 57.32 N ANISOU 2137 N GLY B 115 7638 6465 7678 -1936 1179 -1433 N ATOM 2138 CA GLY B 115 -14.947 9.452 11.407 1.00 58.17 C ANISOU 2138 CA GLY B 115 8041 6506 7553 -1849 1102 -1151 C ATOM 2139 C GLY B 115 -14.368 10.152 12.604 1.00 53.56 C ANISOU 2139 C GLY B 115 7660 5835 6855 -1836 1157 -988 C ATOM 2140 O GLY B 115 -13.892 9.480 13.509 1.00 54.62 O ANISOU 2140 O GLY B 115 8106 5796 6850 -1905 1291 -906 O ATOM 2141 N PHE B 116 -14.400 11.483 12.638 1.00 45.38 N ANISOU 2141 N PHE B 116 6485 4898 5859 -1733 1042 -948 N ATOM 2142 CA PHE B 116 -14.065 12.142 13.899 1.00 43.49 C ANISOU 2142 CA PHE B 116 6419 4565 5540 -1745 1120 -846 C ATOM 2143 C PHE B 116 -15.119 11.727 14.928 1.00 51.77 C ANISOU 2143 C PHE B 116 7538 5478 6653 -1955 1428 -1013 C ATOM 2144 O PHE B 116 -14.801 11.401 16.064 1.00 51.26 O ANISOU 2144 O PHE B 116 7794 5237 6445 -2022 1587 -939 O ATOM 2145 CB PHE B 116 -13.974 13.667 13.755 1.00 36.39 C ANISOU 2145 CB PHE B 116 5361 3779 4686 -1611 960 -789 C ATOM 2146 CG PHE B 116 -12.598 14.154 13.388 1.00 44.95 C ANISOU 2146 CG PHE B 116 6525 4900 5655 -1458 768 -584 C ATOM 2147 CD1 PHE B 116 -11.479 13.714 14.098 1.00 42.73 C ANISOU 2147 CD1 PHE B 116 6487 4515 5232 -1441 767 -462 C ATOM 2148 CD2 PHE B 116 -12.407 15.029 12.319 1.00 37.94 C ANISOU 2148 CD2 PHE B 116 5484 4133 4799 -1325 594 -540 C ATOM 2149 CE1 PHE B 116 -10.192 14.148 13.750 1.00 30.13 C ANISOU 2149 CE1 PHE B 116 4906 2962 3582 -1316 605 -335 C ATOM 2150 CE2 PHE B 116 -11.121 15.450 11.965 1.00 38.98 C ANISOU 2150 CE2 PHE B 116 5684 4279 4847 -1228 483 -380 C ATOM 2151 CZ PHE B 116 -10.016 15.001 12.677 1.00 29.54 C ANISOU 2151 CZ PHE B 116 4656 3005 3564 -1235 493 -297 C ATOM 2152 N THR B 117 -16.369 11.683 14.489 1.00 55.54 N ANISOU 2152 N THR B 117 7729 6027 7345 -2053 1517 -1264 N ATOM 2153 CA THR B 117 -17.484 11.303 15.340 1.00 61.83 C ANISOU 2153 CA THR B 117 8524 6706 8263 -2290 1861 -1489 C ATOM 2154 C THR B 117 -17.521 9.809 15.705 1.00 70.55 C ANISOU 2154 C THR B 117 9899 7625 9279 -2460 2121 -1513 C ATOM 2155 O THR B 117 -17.691 9.464 16.873 1.00 79.48 O ANISOU 2155 O THR B 117 11299 8623 10277 -2520 2376 -1482 O ATOM 2156 CB THR B 117 -18.793 11.673 14.663 1.00 66.18 C ANISOU 2156 CB THR B 117 8621 7411 9112 -2319 1846 -1814 C ATOM 2157 OG1 THR B 117 -18.762 11.178 13.322 1.00 80.18 O ANISOU 2157 OG1 THR B 117 10218 9303 10943 -2223 1631 -1874 O ATOM 2158 CG2 THR B 117 -18.947 13.195 14.607 1.00 59.26 C ANISOU 2158 CG2 THR B 117 7544 6677 8294 -2136 1638 -1806 C ATOM 2159 N LYS B 118 -17.369 8.924 14.721 1.00 68.56 N ANISOU 2159 N LYS B 118 9592 7401 9055 -2460 2032 -1547 N ATOM 2160 CA LYS B 118 -17.492 7.481 14.971 1.00 63.40 C ANISOU 2160 CA LYS B 118 9162 6620 8306 -2546 2247 -1562 C ATOM 2161 C LYS B 118 -16.381 6.671 14.341 1.00 68.22 C ANISOU 2161 C LYS B 118 9991 7172 8758 -2468 2071 -1393 C ATOM 2162 O LYS B 118 -15.607 6.025 15.036 1.00 80.48 O ANISOU 2162 O LYS B 118 11954 8560 10065 -2427 2125 -1218 O ATOM 2163 CB LYS B 118 -18.837 6.937 14.458 1.00 57.89 C ANISOU 2163 CB LYS B 118 8124 6005 7868 -2670 2406 -1883 C ATOM 2164 N THR B 119 -16.308 6.721 13.018 1.00 61.30 N ANISOU 2164 N THR B 119 8846 6437 8007 -2414 1842 -1465 N ATOM 2165 CA THR B 119 -15.520 5.775 12.235 1.00 57.52 C ANISOU 2165 CA THR B 119 8490 5949 7415 -2328 1698 -1368 C ATOM 2166 C THR B 119 -14.044 5.619 12.637 1.00 48.71 C ANISOU 2166 C THR B 119 7737 4749 6023 -2163 1562 -1081 C ATOM 2167 O THR B 119 -13.562 4.499 12.779 1.00 48.41 O ANISOU 2167 O THR B 119 8001 4547 5847 -2185 1620 -1032 O ATOM 2168 CB THR B 119 -15.591 6.154 10.738 1.00 62.65 C ANISOU 2168 CB THR B 119 8773 6850 8180 -2161 1400 -1433 C ATOM 2169 OG1 THR B 119 -16.959 6.116 10.305 1.00 73.56 O ANISOU 2169 OG1 THR B 119 9816 8305 9829 -2280 1478 -1760 O ATOM 2170 CG2 THR B 119 -14.728 5.218 9.865 1.00 48.82 C ANISOU 2170 CG2 THR B 119 7140 5104 6307 -2060 1250 -1335 C ATOM 2171 N TYR B 120 -13.325 6.717 12.826 1.00 47.76 N ANISOU 2171 N TYR B 120 7584 4729 5833 -1993 1376 -922 N ATOM 2172 CA TYR B 120 -11.878 6.625 13.073 1.00 52.22 C ANISOU 2172 CA TYR B 120 8401 5250 6190 -1813 1203 -716 C ATOM 2173 C TYR B 120 -11.471 5.652 14.184 1.00 59.43 C ANISOU 2173 C TYR B 120 9797 5889 6896 -1847 1341 -661 C ATOM 2174 O TYR B 120 -10.514 4.896 14.028 1.00 57.55 O ANISOU 2174 O TYR B 120 9764 5587 6514 -1721 1210 -585 O ATOM 2175 CB TYR B 120 -11.303 8.003 13.399 1.00 42.95 C ANISOU 2175 CB TYR B 120 7136 4180 5003 -1678 1053 -602 C ATOM 2176 CG TYR B 120 -11.155 8.874 12.185 1.00 41.18 C ANISOU 2176 CG TYR B 120 6575 4186 4888 -1565 856 -586 C ATOM 2177 CD1 TYR B 120 -10.950 8.308 10.933 1.00 36.38 C ANISOU 2177 CD1 TYR B 120 5854 3672 4296 -1509 748 -606 C ATOM 2178 CD2 TYR B 120 -11.188 10.259 12.285 1.00 37.87 C ANISOU 2178 CD2 TYR B 120 5999 3863 4526 -1505 784 -545 C ATOM 2179 CE1 TYR B 120 -10.806 9.094 9.814 1.00 33.58 C ANISOU 2179 CE1 TYR B 120 5276 3492 3993 -1395 590 -583 C ATOM 2180 CE2 TYR B 120 -11.039 11.056 11.168 1.00 38.85 C ANISOU 2180 CE2 TYR B 120 5903 4150 4708 -1395 627 -519 C ATOM 2181 CZ TYR B 120 -10.852 10.460 9.938 1.00 39.33 C ANISOU 2181 CZ TYR B 120 5893 4289 4761 -1339 538 -535 C ATOM 2182 OH TYR B 120 -10.714 11.232 8.819 1.00 47.11 O ANISOU 2182 OH TYR B 120 6739 5402 5760 -1221 404 -503 O ATOM 2183 N THR B 121 -12.200 5.663 15.294 1.00 61.47 N ANISOU 2183 N THR B 121 10262 5971 7125 -2004 1607 -712 N ATOM 2184 CA THR B 121 -11.789 4.912 16.472 1.00 58.19 C ANISOU 2184 CA THR B 121 10364 5300 6446 -1969 1720 -633 C ATOM 2185 C THR B 121 -11.694 3.386 16.196 1.00 55.40 C ANISOU 2185 C THR B 121 10239 4829 5982 -1976 1786 -648 C ATOM 2186 O THR B 121 -10.983 2.657 16.894 1.00 57.26 O ANISOU 2186 O THR B 121 10919 4886 5954 -1846 1754 -554 O ATOM 2187 CB THR B 121 -12.754 5.217 17.651 1.00 55.32 C ANISOU 2187 CB THR B 121 10084 4885 6050 -2075 2010 -689 C ATOM 2188 OG1 THR B 121 -12.169 4.798 18.893 1.00 65.06 O ANISOU 2188 OG1 THR B 121 11840 5914 6965 -1957 2047 -584 O ATOM 2189 CG2 THR B 121 -14.104 4.537 17.451 1.00 48.13 C ANISOU 2189 CG2 THR B 121 9006 3996 5286 -2285 2321 -879 C ATOM 2190 N VAL B 122 -12.381 2.911 15.159 1.00 48.31 N ANISOU 2190 N VAL B 122 9050 4027 5279 -2107 1850 -778 N ATOM 2191 CA VAL B 122 -12.254 1.520 14.728 1.00 51.70 C ANISOU 2191 CA VAL B 122 9653 4358 5634 -2117 1887 -799 C ATOM 2192 C VAL B 122 -10.819 1.138 14.318 1.00 58.04 C ANISOU 2192 C VAL B 122 10673 5099 6282 -1903 1583 -679 C ATOM 2193 O VAL B 122 -10.389 -0.023 14.464 1.00 65.11 O ANISOU 2193 O VAL B 122 11899 5841 6998 -1829 1584 -640 O ATOM 2194 CB VAL B 122 -13.183 1.222 13.538 1.00 45.90 C ANISOU 2194 CB VAL B 122 8507 3762 5170 -2271 1946 -988 C ATOM 2195 CG1 VAL B 122 -13.264 -0.293 13.267 1.00 45.22 C ANISOU 2195 CG1 VAL B 122 8617 3549 5016 -2319 2055 -1031 C ATOM 2196 CG2 VAL B 122 -14.553 1.804 13.789 1.00 46.21 C ANISOU 2196 CG2 VAL B 122 8234 3901 5423 -2440 2173 -1163 C ATOM 2197 N GLY B 123 -10.080 2.116 13.809 1.00 45.55 N ANISOU 2197 N GLY B 123 8830 3716 4760 -1745 1307 -619 N ATOM 2198 CA GLY B 123 -8.783 1.848 13.221 1.00 49.84 C ANISOU 2198 CA GLY B 123 9373 4347 5218 -1497 1006 -544 C ATOM 2199 C GLY B 123 -7.627 2.098 14.157 1.00 49.35 C ANISOU 2199 C GLY B 123 9592 4196 4963 -1268 822 -449 C ATOM 2200 O GLY B 123 -6.497 1.713 13.869 1.00 56.21 O ANISOU 2200 O GLY B 123 10515 5090 5752 -1051 583 -433 O ATOM 2201 N CYS B 124 -7.916 2.722 15.291 1.00 45.17 N ANISOU 2201 N CYS B 124 9238 3559 4365 -1304 926 -418 N ATOM 2202 CA CYS B 124 -6.879 3.111 16.246 1.00 43.14 C ANISOU 2202 CA CYS B 124 9228 3228 3937 -1066 721 -360 C ATOM 2203 C CYS B 124 -6.083 1.926 16.790 1.00 46.83 C ANISOU 2203 C CYS B 124 10223 3436 4135 -868 603 -355 C ATOM 2204 O CYS B 124 -4.868 1.868 16.630 1.00 51.43 O ANISOU 2204 O CYS B 124 10778 4087 4676 -601 290 -376 O ATOM 2205 CB CYS B 124 -7.513 3.908 17.387 1.00 39.92 C ANISOU 2205 CB CYS B 124 8962 2723 3485 -1160 892 -338 C ATOM 2206 SG CYS B 124 -8.117 5.511 16.834 1.00107.10 S ANISOU 2206 SG CYS B 124 16861 11545 12288 -1282 912 -349 S ATOM 2207 N GLU B 125 -6.769 0.972 17.408 1.00 55.25 N ANISOU 2207 N GLU B 125 11693 4271 5029 -976 853 -330 N ATOM 2208 CA GLU B 125 -6.099 -0.186 17.994 1.00 72.52 C ANISOU 2208 CA GLU B 125 14358 6274 6922 -756 745 -279 C ATOM 2209 C GLU B 125 -5.289 -1.025 16.992 1.00 73.61 C ANISOU 2209 C GLU B 125 14440 6439 7092 -606 515 -329 C ATOM 2210 O GLU B 125 -4.136 -1.366 17.253 1.00 75.44 O ANISOU 2210 O GLU B 125 14861 6624 7179 -289 202 -336 O ATOM 2211 CB GLU B 125 -7.128 -1.075 18.701 1.00 87.03 C ANISOU 2211 CB GLU B 125 16542 7953 8572 -941 1121 -240 C ATOM 2212 CG GLU B 125 -6.907 -1.162 20.215 1.00106.48 C ANISOU 2212 CG GLU B 125 19547 10237 10674 -785 1136 -162 C ATOM 2213 CD GLU B 125 -8.199 -1.363 20.999 1.00122.56 C ANISOU 2213 CD GLU B 125 21784 12185 12597 -1050 1606 -194 C ATOM 2214 OE1 GLU B 125 -9.221 -1.724 20.377 1.00130.22 O ANISOU 2214 OE1 GLU B 125 22505 13209 13765 -1330 1907 -282 O ATOM 2215 OE2 GLU B 125 -8.198 -1.151 22.235 1.00124.69 O ANISOU 2215 OE2 GLU B 125 22450 12336 12591 -967 1671 -162 O ATOM 2216 N GLU B 126 -5.864 -1.342 15.839 1.00 69.03 N ANISOU 2216 N GLU B 126 13571 5949 6707 -810 645 -386 N ATOM 2217 CA GLU B 126 -5.224 -2.330 14.983 1.00 60.07 C ANISOU 2217 CA GLU B 126 12454 4811 5558 -682 478 -432 C ATOM 2218 C GLU B 126 -4.582 -1.801 13.699 1.00 50.48 C ANISOU 2218 C GLU B 126 10714 3902 4565 -607 254 -502 C ATOM 2219 O GLU B 126 -3.914 -2.565 13.007 1.00 52.39 O ANISOU 2219 O GLU B 126 10944 4171 4790 -465 93 -551 O ATOM 2220 CB GLU B 126 -6.237 -3.435 14.637 1.00 58.72 C ANISOU 2220 CB GLU B 126 12364 4552 5395 -918 775 -433 C ATOM 2221 CG GLU B 126 -6.464 -4.419 15.782 0.00 61.35 C ANISOU 2221 CG GLU B 126 13240 4645 5426 -894 944 -344 C ATOM 2222 CD GLU B 126 -7.931 -4.632 16.101 0.00 62.17 C ANISOU 2222 CD GLU B 126 13347 4705 5570 -1235 1395 -374 C ATOM 2223 OE1 GLU B 126 -8.377 -4.181 17.178 0.00 63.26 O ANISOU 2223 OE1 GLU B 126 13666 4785 5585 -1293 1577 -341 O ATOM 2224 OE2 GLU B 126 -8.637 -5.255 15.281 0.00 62.35 O ANISOU 2224 OE2 GLU B 126 13177 4757 5756 -1434 1567 -460 O ATOM 2225 N CYS B 127 -4.745 -0.517 13.385 1.00 47.98 N ANISOU 2225 N CYS B 127 9933 3850 4446 -681 251 -485 N ATOM 2226 CA CYS B 127 -4.289 0.005 12.083 1.00 38.31 C ANISOU 2226 CA CYS B 127 8184 2947 3426 -644 114 -514 C ATOM 2227 C CYS B 127 -3.446 1.294 12.153 1.00 50.38 C ANISOU 2227 C CYS B 127 9411 4679 5052 -514 -60 -509 C ATOM 2228 O CYS B 127 -3.539 2.070 13.107 1.00 56.54 O ANISOU 2228 O CYS B 127 10267 5412 5805 -514 -46 -475 O ATOM 2229 CB CYS B 127 -5.497 0.238 11.177 1.00 37.32 C ANISOU 2229 CB CYS B 127 7746 2956 3479 -901 319 -524 C ATOM 2230 SG CYS B 127 -6.515 -1.262 10.855 1.00 55.24 S ANISOU 2230 SG CYS B 127 10252 5021 5717 -1096 541 -595 S ATOM 2231 N THR B 128 -2.624 1.531 11.137 1.00 47.86 N ANISOU 2231 N THR B 128 8756 4575 4853 -418 -200 -555 N ATOM 2232 CA THR B 128 -1.746 2.698 11.157 1.00 42.52 C ANISOU 2232 CA THR B 128 7796 4069 4293 -321 -326 -583 C ATOM 2233 C THR B 128 -1.625 3.420 9.813 1.00 44.19 C ANISOU 2233 C THR B 128 7578 4530 4681 -397 -279 -580 C ATOM 2234 O THR B 128 -1.263 2.820 8.806 1.00 41.03 O ANISOU 2234 O THR B 128 7080 4209 4302 -359 -304 -626 O ATOM 2235 CB THR B 128 -0.334 2.308 11.615 1.00 47.38 C ANISOU 2235 CB THR B 128 8511 4639 4853 -41 -589 -711 C ATOM 2236 OG1 THR B 128 -0.362 1.978 13.014 1.00 47.84 O ANISOU 2236 OG1 THR B 128 9005 4454 4717 77 -668 -710 O ATOM 2237 CG2 THR B 128 0.648 3.468 11.378 1.00 36.30 C ANISOU 2237 CG2 THR B 128 6716 3436 3638 23 -686 -800 C ATOM 2238 N VAL B 129 -1.916 4.717 9.805 1.00 44.68 N ANISOU 2238 N VAL B 129 7429 4700 4850 -494 -204 -527 N ATOM 2239 CA VAL B 129 -1.725 5.519 8.606 1.00 32.07 C ANISOU 2239 CA VAL B 129 5510 3296 3379 -546 -149 -515 C ATOM 2240 C VAL B 129 -0.282 6.009 8.514 1.00 38.07 C ANISOU 2240 C VAL B 129 6087 4141 4236 -428 -246 -618 C ATOM 2241 O VAL B 129 0.128 6.904 9.230 1.00 46.07 O ANISOU 2241 O VAL B 129 7033 5154 5317 -409 -281 -645 O ATOM 2242 CB VAL B 129 -2.691 6.713 8.567 1.00 31.08 C ANISOU 2242 CB VAL B 129 5268 3224 3315 -688 -26 -423 C ATOM 2243 CG1 VAL B 129 -2.419 7.568 7.349 1.00 30.64 C ANISOU 2243 CG1 VAL B 129 4978 3322 3343 -712 30 -402 C ATOM 2244 CG2 VAL B 129 -4.130 6.223 8.544 1.00 30.97 C ANISOU 2244 CG2 VAL B 129 5357 3150 3261 -811 76 -391 C ATOM 2245 N PHE B 130 0.487 5.400 7.620 1.00 43.87 N ANISOU 2245 N PHE B 130 6725 4949 4996 -354 -278 -706 N ATOM 2246 CA PHE B 130 1.911 5.695 7.475 1.00 46.94 C ANISOU 2246 CA PHE B 130 6904 5420 5513 -250 -346 -871 C ATOM 2247 C PHE B 130 2.178 6.681 6.334 1.00 50.65 C ANISOU 2247 C PHE B 130 7116 6028 6100 -370 -158 -858 C ATOM 2248 O PHE B 130 1.833 6.413 5.195 1.00 40.41 O ANISOU 2248 O PHE B 130 5812 4788 4755 -424 -51 -799 O ATOM 2249 CB PHE B 130 2.673 4.398 7.238 1.00 48.44 C ANISOU 2249 CB PHE B 130 7151 5591 5664 -82 -484 -1014 C ATOM 2250 CG PHE B 130 4.146 4.574 7.105 1.00 60.12 C ANISOU 2250 CG PHE B 130 8377 7160 7308 40 -565 -1251 C ATOM 2251 CD1 PHE B 130 4.963 4.563 8.231 1.00 64.95 C ANISOU 2251 CD1 PHE B 130 9000 7711 7966 226 -792 -1431 C ATOM 2252 CD2 PHE B 130 4.728 4.724 5.854 1.00 62.23 C ANISOU 2252 CD2 PHE B 130 8398 7563 7684 -21 -414 -1327 C ATOM 2253 CE1 PHE B 130 6.334 4.718 8.114 1.00 66.50 C ANISOU 2253 CE1 PHE B 130 8902 8001 8362 345 -881 -1720 C ATOM 2254 CE2 PHE B 130 6.102 4.884 5.728 1.00 68.98 C ANISOU 2254 CE2 PHE B 130 8976 8501 8732 65 -447 -1597 C ATOM 2255 CZ PHE B 130 6.905 4.881 6.858 1.00 69.19 C ANISOU 2255 CZ PHE B 130 8953 8487 8851 247 -689 -1812 C ATOM 2256 N PRO B 131 2.800 7.829 6.644 1.00 55.36 N ANISOU 2256 N PRO B 131 7534 6658 6841 -410 -111 -921 N ATOM 2257 CA PRO B 131 3.048 8.888 5.658 1.00 54.62 C ANISOU 2257 CA PRO B 131 7267 6645 6843 -546 115 -899 C ATOM 2258 C PRO B 131 4.105 8.529 4.621 1.00 62.45 C ANISOU 2258 C PRO B 131 8094 7718 7917 -532 217 -1056 C ATOM 2259 O PRO B 131 5.246 8.236 4.975 1.00 65.72 O ANISOU 2259 O PRO B 131 8339 8158 8473 -437 126 -1293 O ATOM 2260 CB PRO B 131 3.526 10.061 6.519 1.00 56.15 C ANISOU 2260 CB PRO B 131 7331 6818 7187 -587 120 -970 C ATOM 2261 CG PRO B 131 3.046 9.743 7.907 1.00 55.62 C ANISOU 2261 CG PRO B 131 7430 6660 7043 -488 -93 -944 C ATOM 2262 CD PRO B 131 3.169 8.254 7.998 1.00 52.95 C ANISOU 2262 CD PRO B 131 7234 6289 6596 -336 -257 -1006 C ATOM 2263 N CYS B 132 3.707 8.565 3.351 1.00 69.56 N ANISOU 2263 N CYS B 132 9051 8655 8725 -610 396 -947 N ATOM 2264 CA CYS B 132 4.595 8.324 2.223 1.00 68.32 C ANISOU 2264 CA CYS B 132 8779 8564 8614 -624 560 -1072 C ATOM 2265 C CYS B 132 5.069 9.631 1.606 1.00 79.02 C ANISOU 2265 C CYS B 132 10046 9917 10063 -787 862 -1081 C ATOM 2266 O CYS B 132 4.315 10.274 0.875 1.00 80.94 O ANISOU 2266 O CYS B 132 10467 10122 10163 -867 1014 -890 O ATOM 2267 CB CYS B 132 3.889 7.482 1.153 1.00 56.39 C ANISOU 2267 CB CYS B 132 7444 7073 6909 -592 576 -957 C ATOM 2268 SG CYS B 132 4.284 5.731 1.216 1.00111.33 S ANISOU 2268 SG CYS B 132 14411 14053 13837 -417 363 -1102 S ATOM 2269 N PRO B 133 6.325 10.021 1.886 1.00 91.35 N ANISOU 2269 N PRO B 133 11345 11501 11864 -828 952 -1328 N ATOM 2270 CA PRO B 133 6.891 11.236 1.282 1.00102.32 C ANISOU 2270 CA PRO B 133 12653 12857 13367 -1022 1305 -1374 C ATOM 2271 C PRO B 133 7.170 11.049 -0.218 1.00105.79 C ANISOU 2271 C PRO B 133 13180 13306 13709 -1093 1603 -1369 C ATOM 2272 O PRO B 133 6.322 11.338 -1.067 1.00111.97 O ANISOU 2272 O PRO B 133 14256 14035 14254 -1124 1721 -1131 O ATOM 2273 CB PRO B 133 8.189 11.450 2.071 1.00 99.63 C ANISOU 2273 CB PRO B 133 11953 12550 13352 -1030 1281 -1718 C ATOM 2274 CG PRO B 133 8.574 10.086 2.563 1.00 95.48 C ANISOU 2274 CG PRO B 133 11328 12098 12852 -804 956 -1894 C ATOM 2275 CD PRO B 133 7.303 9.294 2.718 1.00 93.26 C ANISOU 2275 CD PRO B 133 11361 11789 12285 -684 729 -1614 C ATOM 2276 N SER B 134 8.360 10.568 -0.537 1.00 91.71 N ANISOU 2276 N SER B 134 11151 11588 12106 -1098 1713 -1656 N ATOM 2277 CA SER B 134 8.678 10.212 -1.900 1.00 83.40 C ANISOU 2277 CA SER B 134 10183 10549 10955 -1145 1986 -1680 C ATOM 2278 C SER B 134 8.180 8.801 -2.179 1.00 79.50 C ANISOU 2278 C SER B 134 9805 10124 10278 -947 1721 -1615 C ATOM 2279 O SER B 134 8.357 7.905 -1.353 1.00 84.05 O ANISOU 2279 O SER B 134 10242 10757 10937 -786 1401 -1740 O ATOM 2280 CB SER B 134 10.188 10.318 -2.131 1.00 86.28 C ANISOU 2280 CB SER B 134 10198 10956 11627 -1256 2257 -2061 C ATOM 2281 OG SER B 134 10.611 9.622 -3.290 1.00 93.68 O ANISOU 2281 OG SER B 134 11169 11935 12492 -1252 2458 -2147 O ATOM 2282 N ILE B 135 7.532 8.604 -3.322 1.00 64.23 N ANISOU 2282 N ILE B 135 8159 8166 8081 -944 1840 -1426 N ATOM 2283 CA ILE B 135 7.426 7.257 -3.871 1.00 61.90 C ANISOU 2283 CA ILE B 135 7918 7939 7663 -793 1692 -1455 C ATOM 2284 C ILE B 135 8.746 6.942 -4.595 1.00 60.78 C ANISOU 2284 C ILE B 135 7574 7854 7668 -837 1955 -1740 C ATOM 2285 O ILE B 135 9.312 7.791 -5.276 1.00 50.91 O ANISOU 2285 O ILE B 135 6328 6555 6461 -1014 2357 -1797 O ATOM 2286 CB ILE B 135 6.220 7.088 -4.825 1.00 57.75 C ANISOU 2286 CB ILE B 135 7760 7374 6806 -743 1676 -1189 C ATOM 2287 CG1 ILE B 135 6.073 8.304 -5.737 1.00 74.67 C ANISOU 2287 CG1 ILE B 135 10149 9418 8805 -875 2023 -1052 C ATOM 2288 CG2 ILE B 135 4.932 6.899 -4.033 1.00 48.05 C ANISOU 2288 CG2 ILE B 135 6646 6127 5485 -658 1344 -1003 C ATOM 2289 CD1 ILE B 135 6.662 8.118 -7.139 1.00 84.54 C ANISOU 2289 CD1 ILE B 135 11542 10653 9926 -907 2348 -1118 C ATOM 2290 N PRO B 136 9.264 5.722 -4.425 1.00 59.40 N ANISOU 2290 N PRO B 136 7226 7766 7578 -680 1747 -1942 N ATOM 2291 CA PRO B 136 8.700 4.603 -3.666 1.00 60.90 C ANISOU 2291 CA PRO B 136 7463 7974 7700 -475 1312 -1897 C ATOM 2292 C PRO B 136 8.746 4.803 -2.153 1.00 63.33 C ANISOU 2292 C PRO B 136 7636 8261 8166 -415 1040 -1953 C ATOM 2293 O PRO B 136 9.668 5.457 -1.654 1.00 70.24 O ANISOU 2293 O PRO B 136 8239 9156 9294 -474 1122 -2174 O ATOM 2294 CB PRO B 136 9.596 3.421 -4.067 1.00 59.67 C ANISOU 2294 CB PRO B 136 7150 7898 7622 -338 1258 -2166 C ATOM 2295 CG PRO B 136 10.478 3.921 -5.154 1.00 57.84 C ANISOU 2295 CG PRO B 136 6803 7700 7473 -488 1692 -2326 C ATOM 2296 CD PRO B 136 10.577 5.384 -4.985 1.00 53.99 C ANISOU 2296 CD PRO B 136 6279 7151 7084 -704 1968 -2277 C ATOM 2297 N CYS B 137 7.745 4.259 -1.457 1.00 61.28 N ANISOU 2297 N CYS B 137 7577 7949 7756 -309 741 -1769 N ATOM 2298 CA CYS B 137 7.746 4.140 0.004 1.00 57.71 C ANISOU 2298 CA CYS B 137 7087 7453 7389 -201 446 -1821 C ATOM 2299 C CYS B 137 7.861 2.663 0.357 1.00 62.31 C ANISOU 2299 C CYS B 137 7752 8014 7908 23 148 -1923 C ATOM 2300 O CYS B 137 7.370 1.818 -0.388 1.00 62.39 O ANISOU 2300 O CYS B 137 7926 8021 7756 56 144 -1832 O ATOM 2301 CB CYS B 137 6.470 4.701 0.624 1.00 40.68 C ANISOU 2301 CB CYS B 137 5146 5213 5097 -272 380 -1537 C ATOM 2302 SG CYS B 137 5.602 5.970 -0.320 1.00137.89 S ANISOU 2302 SG CYS B 137 17586 17512 17292 -480 684 -1281 S ATOM 2303 N LYS B 138 8.496 2.334 1.476 1.00 60.79 N ANISOU 2303 N LYS B 138 7480 7791 7827 195 -116 -2119 N ATOM 2304 CA LYS B 138 8.468 0.947 1.932 1.00 53.52 C ANISOU 2304 CA LYS B 138 6749 6795 6790 429 -419 -2177 C ATOM 2305 C LYS B 138 7.225 0.760 2.812 1.00 48.34 C ANISOU 2305 C LYS B 138 6444 5990 5932 422 -557 -1910 C ATOM 2306 O LYS B 138 6.921 1.597 3.665 1.00 48.08 O ANISOU 2306 O LYS B 138 6430 5914 5925 361 -573 -1830 O ATOM 2307 CB LYS B 138 9.757 0.568 2.678 1.00 46.76 C ANISOU 2307 CB LYS B 138 5702 5951 6112 676 -676 -2545 C ATOM 2308 N LEU B 139 6.481 -0.313 2.558 1.00 45.69 N ANISOU 2308 N LEU B 139 6380 5572 5407 461 -622 -1786 N ATOM 2309 CA LEU B 139 5.373 -0.709 3.417 1.00 48.34 C ANISOU 2309 CA LEU B 139 7061 5740 5568 451 -725 -1592 C ATOM 2310 C LEU B 139 5.919 -1.585 4.534 1.00 58.67 C ANISOU 2310 C LEU B 139 8580 6898 6816 710 -1023 -1737 C ATOM 2311 O LEU B 139 6.315 -2.719 4.282 1.00 54.81 O ANISOU 2311 O LEU B 139 8200 6360 6265 879 -1155 -1853 O ATOM 2312 CB LEU B 139 4.304 -1.467 2.627 1.00 47.02 C ANISOU 2312 CB LEU B 139 7083 5532 5249 354 -636 -1432 C ATOM 2313 CG LEU B 139 3.213 -2.072 3.512 1.00 43.81 C ANISOU 2313 CG LEU B 139 7034 4925 4688 326 -704 -1291 C ATOM 2314 CD1 LEU B 139 2.192 -1.014 3.904 1.00 44.53 C ANISOU 2314 CD1 LEU B 139 7118 5012 4788 127 -567 -1114 C ATOM 2315 CD2 LEU B 139 2.537 -3.269 2.866 1.00 38.99 C ANISOU 2315 CD2 LEU B 139 6617 4238 3960 305 -688 -1255 C ATOM 2316 N GLN B 140 5.950 -1.070 5.761 1.00 69.41 N ANISOU 2316 N GLN B 140 10031 8170 8173 767 -1142 -1737 N ATOM 2317 CA GLN B 140 6.635 -1.774 6.848 1.00 67.48 C ANISOU 2317 CA GLN B 140 10009 7774 7855 1071 -1463 -1913 C ATOM 2318 C GLN B 140 5.805 -2.897 7.478 1.00 52.03 C ANISOU 2318 C GLN B 140 8593 5554 5621 1138 -1548 -1766 C ATOM 2319 O GLN B 140 6.350 -3.747 8.172 1.00 49.77 O ANISOU 2319 O GLN B 140 8593 5104 5213 1425 -1817 -1902 O ATOM 2320 CB GLN B 140 7.075 -0.781 7.927 1.00 73.34 C ANISOU 2320 CB GLN B 140 10661 8515 8690 1139 -1581 -2004 C ATOM 2321 CG GLN B 140 8.466 -0.172 7.693 1.00 85.03 C ANISOU 2321 CG GLN B 140 11668 10181 10457 1244 -1658 -2336 C ATOM 2322 CD GLN B 140 9.608 -1.166 7.923 1.00101.81 C ANISOU 2322 CD GLN B 140 13802 12275 12607 1612 -1996 -2675 C ATOM 2323 OE1 GLN B 140 9.464 -2.145 8.660 1.00105.38 O ANISOU 2323 OE1 GLN B 140 14693 12519 12826 1855 -2252 -2664 O ATOM 2324 NE2 GLN B 140 10.749 -0.910 7.291 1.00111.23 N ANISOU 2324 NE2 GLN B 140 14524 13657 14080 1659 -1986 -2996 N ATOM 2325 N SER B 141 4.504 -2.926 7.197 1.00 51.60 N ANISOU 2325 N SER B 141 8688 5446 5473 880 -1314 -1516 N ATOM 2326 CA SER B 141 3.598 -3.899 7.808 1.00 47.75 C ANISOU 2326 CA SER B 141 8706 4686 4751 867 -1306 -1384 C ATOM 2327 C SER B 141 2.267 -4.009 7.072 1.00 49.59 C ANISOU 2327 C SER B 141 8943 4928 4971 564 -1028 -1201 C ATOM 2328 O SER B 141 1.843 -3.064 6.413 1.00 56.38 O ANISOU 2328 O SER B 141 9481 5978 5965 368 -860 -1126 O ATOM 2329 CB SER B 141 3.336 -3.522 9.265 1.00 55.20 C ANISOU 2329 CB SER B 141 9962 5441 5570 914 -1369 -1322 C ATOM 2330 OG SER B 141 2.174 -4.161 9.757 1.00 58.49 O ANISOU 2330 OG SER B 141 10826 5606 5792 773 -1214 -1156 O ATOM 2331 N GLY B 142 1.597 -5.151 7.209 1.00 47.87 N ANISOU 2331 N GLY B 142 9107 4487 4593 534 -987 -1149 N ATOM 2332 CA GLY B 142 0.319 -5.384 6.548 1.00 41.29 C ANISOU 2332 CA GLY B 142 8267 3646 3774 258 -745 -1040 C ATOM 2333 C GLY B 142 -0.838 -4.602 7.147 1.00 47.71 C ANISOU 2333 C GLY B 142 9104 4416 4607 15 -542 -910 C ATOM 2334 O GLY B 142 -1.882 -4.425 6.514 1.00 58.70 O ANISOU 2334 O GLY B 142 10342 5878 6082 -213 -359 -863 O ATOM 2335 N THR B 143 -0.647 -4.127 8.374 1.00 44.31 N ANISOU 2335 N THR B 143 8861 3871 4105 84 -593 -879 N ATOM 2336 CA THR B 143 -1.606 -3.239 9.029 1.00 46.20 C ANISOU 2336 CA THR B 143 9096 4087 4373 -122 -411 -773 C ATOM 2337 C THR B 143 -1.292 -1.761 8.795 1.00 39.54 C ANISOU 2337 C THR B 143 7823 3504 3698 -142 -434 -756 C ATOM 2338 O THR B 143 -1.907 -0.885 9.405 1.00 38.79 O ANISOU 2338 O THR B 143 7703 3405 3632 -267 -326 -682 O ATOM 2339 CB THR B 143 -1.651 -3.478 10.541 1.00 50.28 C ANISOU 2339 CB THR B 143 10104 4311 4691 -46 -426 -740 C ATOM 2340 OG1 THR B 143 -0.412 -3.046 11.121 1.00 49.12 O ANISOU 2340 OG1 THR B 143 9948 4202 4513 237 -699 -814 O ATOM 2341 CG2 THR B 143 -1.887 -4.958 10.845 1.00 51.43 C ANISOU 2341 CG2 THR B 143 10773 4138 4631 -15 -384 -752 C ATOM 2342 N HIS B 144 -0.323 -1.482 7.928 1.00 38.77 N ANISOU 2342 N HIS B 144 7408 3615 3709 -26 -550 -835 N ATOM 2343 CA HIS B 144 -0.087 -0.113 7.480 1.00 44.67 C ANISOU 2343 CA HIS B 144 7763 4589 4619 -88 -508 -818 C ATOM 2344 C HIS B 144 -0.860 0.228 6.219 1.00 49.26 C ANISOU 2344 C HIS B 144 8107 5328 5283 -264 -348 -758 C ATOM 2345 O HIS B 144 -0.893 -0.541 5.259 1.00 55.41 O ANISOU 2345 O HIS B 144 8865 6143 6045 -254 -342 -796 O ATOM 2346 CB HIS B 144 1.392 0.144 7.216 1.00 50.83 C ANISOU 2346 CB HIS B 144 8318 5501 5496 101 -664 -966 C ATOM 2347 CG HIS B 144 2.222 0.213 8.448 1.00 58.23 C ANISOU 2347 CG HIS B 144 9392 6334 6400 303 -867 -1070 C ATOM 2348 ND1 HIS B 144 1.674 0.311 9.708 1.00 59.83 N ANISOU 2348 ND1 HIS B 144 9906 6352 6476 302 -884 -992 N ATOM 2349 CD2 HIS B 144 3.562 0.237 8.617 1.00 68.15 C ANISOU 2349 CD2 HIS B 144 10509 7647 7738 528 -1073 -1277 C ATOM 2350 CE1 HIS B 144 2.641 0.366 10.601 1.00 63.34 C ANISOU 2350 CE1 HIS B 144 10437 6733 6895 542 -1119 -1131 C ATOM 2351 NE2 HIS B 144 3.798 0.328 9.965 1.00 67.96 N ANISOU 2351 NE2 HIS B 144 10726 7471 7624 687 -1251 -1323 N ATOM 2352 N CYS B 145 -1.482 1.396 6.232 1.00 47.07 N ANISOU 2352 N CYS B 145 7672 5132 5080 -398 -240 -675 N ATOM 2353 CA CYS B 145 -2.016 1.966 5.018 1.00 45.33 C ANISOU 2353 CA CYS B 145 7230 5070 4923 -497 -140 -636 C ATOM 2354 C CYS B 145 -1.091 3.089 4.617 1.00 39.97 C ANISOU 2354 C CYS B 145 6321 4534 4331 -456 -130 -642 C ATOM 2355 O CYS B 145 -0.851 3.990 5.414 1.00 32.67 O ANISOU 2355 O CYS B 145 5353 3601 3461 -466 -133 -622 O ATOM 2356 CB CYS B 145 -3.441 2.472 5.211 1.00 46.39 C ANISOU 2356 CB CYS B 145 7363 5183 5081 -659 -31 -570 C ATOM 2357 SG CYS B 145 -4.611 1.156 5.558 1.00 86.94 S ANISOU 2357 SG CYS B 145 12730 10140 10165 -771 39 -616 S ATOM 2358 N LEU B 146 -0.557 3.009 3.397 1.00 33.19 N ANISOU 2358 N LEU B 146 5336 3791 3485 -420 -97 -683 N ATOM 2359 CA LEU B 146 0.311 4.039 2.871 1.00 34.71 C ANISOU 2359 CA LEU B 146 5333 4095 3760 -420 -15 -703 C ATOM 2360 C LEU B 146 -0.534 5.249 2.506 1.00 43.30 C ANISOU 2360 C LEU B 146 6384 5221 4846 -531 100 -579 C ATOM 2361 O LEU B 146 -1.564 5.135 1.843 1.00 41.60 O ANISOU 2361 O LEU B 146 6228 5020 4559 -564 117 -522 O ATOM 2362 CB LEU B 146 1.104 3.537 1.662 1.00 39.78 C ANISOU 2362 CB LEU B 146 5897 4823 4393 -358 31 -793 C ATOM 2363 CG LEU B 146 2.068 2.365 1.906 1.00 40.17 C ANISOU 2363 CG LEU B 146 5958 4847 4458 -213 -100 -953 C ATOM 2364 CD1 LEU B 146 2.788 2.017 0.647 1.00 36.49 C ANISOU 2364 CD1 LEU B 146 5389 4480 3996 -172 -16 -1049 C ATOM 2365 CD2 LEU B 146 3.064 2.670 2.990 1.00 43.32 C ANISOU 2365 CD2 LEU B 146 6269 5221 4972 -128 -202 -1078 C ATOM 2366 N TRP B 147 -0.104 6.401 3.003 1.00 47.81 N ANISOU 2366 N TRP B 147 6862 5800 5504 -570 155 -563 N ATOM 2367 CA TRP B 147 -0.745 7.675 2.742 1.00 45.00 C ANISOU 2367 CA TRP B 147 6493 5459 5146 -653 257 -453 C ATOM 2368 C TRP B 147 0.020 8.311 1.591 1.00 46.09 C ANISOU 2368 C TRP B 147 6574 5654 5285 -669 421 -463 C ATOM 2369 O TRP B 147 1.172 8.727 1.747 1.00 49.68 O ANISOU 2369 O TRP B 147 6901 6120 5854 -691 506 -554 O ATOM 2370 CB TRP B 147 -0.722 8.538 4.000 1.00 47.03 C ANISOU 2370 CB TRP B 147 6714 5664 5489 -694 235 -434 C ATOM 2371 CG TRP B 147 -1.455 9.818 3.914 1.00 40.72 C ANISOU 2371 CG TRP B 147 5922 4860 4689 -765 314 -327 C ATOM 2372 CD1 TRP B 147 -2.435 10.142 3.036 1.00 36.91 C ANISOU 2372 CD1 TRP B 147 5510 4397 4117 -769 345 -249 C ATOM 2373 CD2 TRP B 147 -1.259 10.968 4.748 1.00 39.72 C ANISOU 2373 CD2 TRP B 147 5742 4698 4651 -814 344 -307 C ATOM 2374 NE1 TRP B 147 -2.867 11.432 3.262 1.00 35.29 N ANISOU 2374 NE1 TRP B 147 5313 4164 3931 -808 390 -175 N ATOM 2375 CE2 TRP B 147 -2.160 11.959 4.312 1.00 35.21 C ANISOU 2375 CE2 TRP B 147 5224 4119 4033 -850 405 -201 C ATOM 2376 CE3 TRP B 147 -0.403 11.257 5.819 1.00 31.37 C ANISOU 2376 CE3 TRP B 147 4602 3610 3707 -808 302 -390 C ATOM 2377 CZ2 TRP B 147 -2.248 13.213 4.921 1.00 30.81 C ANISOU 2377 CZ2 TRP B 147 4649 3520 3539 -899 446 -157 C ATOM 2378 CZ3 TRP B 147 -0.485 12.506 6.417 1.00 34.85 C ANISOU 2378 CZ3 TRP B 147 5007 4016 4217 -866 344 -353 C ATOM 2379 CH2 TRP B 147 -1.404 13.470 5.965 1.00 30.89 C ANISOU 2379 CH2 TRP B 147 4568 3502 3668 -920 428 -228 C ATOM 2380 N THR B 148 -0.611 8.353 0.423 1.00 45.10 N ANISOU 2380 N THR B 148 6554 5551 5030 -656 474 -395 N ATOM 2381 CA THR B 148 0.113 8.641 -0.804 1.00 40.35 C ANISOU 2381 CA THR B 148 5984 4976 4371 -656 653 -409 C ATOM 2382 C THR B 148 -0.277 9.976 -1.424 1.00 46.12 C ANISOU 2382 C THR B 148 6853 5659 5010 -691 793 -291 C ATOM 2383 O THR B 148 0.323 10.384 -2.404 1.00 50.49 O ANISOU 2383 O THR B 148 7500 6193 5491 -711 996 -287 O ATOM 2384 CB THR B 148 -0.069 7.498 -1.850 1.00 36.62 C ANISOU 2384 CB THR B 148 5597 4547 3770 -570 608 -445 C ATOM 2385 OG1 THR B 148 -1.381 6.936 -1.759 1.00 46.74 O ANISOU 2385 OG1 THR B 148 6953 5824 4983 -525 429 -410 O ATOM 2386 CG2 THR B 148 0.918 6.386 -1.586 1.00 42.03 C ANISOU 2386 CG2 THR B 148 6160 5266 4544 -532 565 -591 C ATOM 2387 N ASP B 149 -1.277 10.647 -0.864 1.00 52.14 N ANISOU 2387 N ASP B 149 7659 6386 5766 -694 699 -205 N ATOM 2388 CA ASP B 149 -1.571 12.030 -1.232 1.00 50.23 C ANISOU 2388 CA ASP B 149 7563 6073 5450 -710 810 -101 C ATOM 2389 C ASP B 149 -0.251 12.779 -1.269 1.00 54.80 C ANISOU 2389 C ASP B 149 8096 6603 6121 -827 1069 -132 C ATOM 2390 O ASP B 149 0.447 12.836 -0.257 1.00 61.09 O ANISOU 2390 O ASP B 149 8685 7414 7114 -903 1071 -218 O ATOM 2391 CB ASP B 149 -2.511 12.702 -0.205 1.00 54.88 C ANISOU 2391 CB ASP B 149 8115 6633 6102 -720 682 -50 C ATOM 2392 CG ASP B 149 -3.852 11.956 -0.003 1.00 67.48 C ANISOU 2392 CG ASP B 149 9696 8273 7670 -645 461 -77 C ATOM 2393 OD1 ASP B 149 -4.232 11.109 -0.857 1.00 63.54 O ANISOU 2393 OD1 ASP B 149 9256 7816 7072 -563 388 -118 O ATOM 2394 OD2 ASP B 149 -4.518 12.240 1.035 1.00 63.79 O ANISOU 2394 OD2 ASP B 149 9151 7793 7294 -679 379 -78 O ATOM 2395 N GLN B 150 0.133 13.325 -2.409 1.00 69.67 N ANISOU 2395 N GLN B 150 10179 8420 7872 -844 1297 -92 N ATOM 2396 CA GLN B 150 1.311 14.165 -2.366 1.00 86.62 C ANISOU 2396 CA GLN B 150 12272 10497 10145 -1000 1594 -148 C ATOM 2397 C GLN B 150 0.939 15.593 -2.712 1.00 87.24 C ANISOU 2397 C GLN B 150 12628 10421 10100 -1035 1752 -10 C ATOM 2398 O GLN B 150 1.715 16.305 -3.326 1.00 87.84 O ANISOU 2398 O GLN B 150 12841 10381 10152 -1152 2084 -17 O ATOM 2399 CB GLN B 150 2.416 13.652 -3.275 1.00 96.88 C ANISOU 2399 CB GLN B 150 13554 11812 11445 -1054 1840 -265 C ATOM 2400 CG GLN B 150 2.469 12.151 -3.446 1.00 98.09 C ANISOU 2400 CG GLN B 150 13586 12094 11592 -948 1661 -357 C ATOM 2401 CD GLN B 150 3.881 11.659 -3.719 1.00107.98 C ANISOU 2401 CD GLN B 150 14637 13392 12998 -1027 1869 -564 C ATOM 2402 OE1 GLN B 150 4.278 11.428 -4.865 1.00117.12 O ANISOU 2402 OE1 GLN B 150 15934 14535 14033 -1033 2082 -590 O ATOM 2403 NE2 GLN B 150 4.649 11.482 -2.643 1.00107.07 N ANISOU 2403 NE2 GLN B 150 14192 13334 13156 -1070 1794 -740 N ATOM 2404 N CYS B 151 -0.270 15.999 -2.339 1.00 88.91 N ANISOU 2404 N CYS B 151 12940 10614 10229 -931 1527 100 N ATOM 2405 CA CYS B 151 -0.594 17.406 -2.216 1.00 84.54 C ANISOU 2405 CA CYS B 151 12580 9916 9626 -958 1614 205 C ATOM 2406 C CYS B 151 0.445 18.023 -1.285 1.00 79.82 C ANISOU 2406 C CYS B 151 11746 9286 9296 -1157 1795 115 C ATOM 2407 O CYS B 151 0.978 17.347 -0.406 1.00 79.81 O ANISOU 2407 O CYS B 151 11412 9400 9513 -1205 1700 -19 O ATOM 2408 CB CYS B 151 -2.012 17.575 -1.661 1.00 78.74 C ANISOU 2408 CB CYS B 151 11862 9211 8846 -814 1297 269 C ATOM 2409 SG CYS B 151 -3.321 18.049 -2.849 1.00132.65 S ANISOU 2409 SG CYS B 151 19121 15946 15334 -564 1151 379 S ATOM 2410 N LEU B 152 0.762 19.292 -1.477 1.00 75.78 N ANISOU 2410 N LEU B 152 11423 8604 8767 -1263 2048 168 N ATOM 2411 CA LEU B 152 1.548 19.966 -0.463 1.00 75.81 C ANISOU 2411 CA LEU B 152 11180 8577 9048 -1440 2164 61 C ATOM 2412 C LEU B 152 0.771 19.976 0.855 1.00 76.35 C ANISOU 2412 C LEU B 152 11060 8728 9221 -1362 1833 75 C ATOM 2413 O LEU B 152 1.342 19.717 1.915 1.00 73.55 O ANISOU 2413 O LEU B 152 10390 8453 9102 -1424 1754 -64 O ATOM 2414 CB LEU B 152 1.895 21.390 -0.877 1.00 71.46 C ANISOU 2414 CB LEU B 152 10902 7796 8454 -1579 2504 121 C ATOM 2415 CG LEU B 152 2.646 22.088 0.255 1.00 73.15 C ANISOU 2415 CG LEU B 152 10820 7986 8989 -1760 2590 -23 C ATOM 2416 CD1 LEU B 152 3.849 21.259 0.703 1.00 80.35 C ANISOU 2416 CD1 LEU B 152 11290 9042 10196 -1863 2627 -288 C ATOM 2417 CD2 LEU B 152 3.092 23.448 -0.164 1.00 71.91 C ANISOU 2417 CD2 LEU B 152 10924 7579 8820 -1939 2978 8 C ATOM 2418 N GLN B 153 -0.526 20.279 0.774 1.00 68.38 N ANISOU 2418 N GLN B 153 10260 7692 8029 -1213 1640 220 N ATOM 2419 CA GLN B 153 -1.408 20.311 1.942 1.00 59.57 C ANISOU 2419 CA GLN B 153 8998 6643 6992 -1144 1364 229 C ATOM 2420 C GLN B 153 -2.256 19.037 1.997 1.00 55.48 C ANISOU 2420 C GLN B 153 8394 6272 6415 -1010 1101 213 C ATOM 2421 O GLN B 153 -3.491 19.079 2.118 1.00 46.16 O ANISOU 2421 O GLN B 153 7275 5111 5153 -890 906 257 O ATOM 2422 CB GLN B 153 -2.291 21.550 1.901 1.00 50.39 C ANISOU 2422 CB GLN B 153 8080 5351 5714 -1076 1336 348 C ATOM 2423 CG GLN B 153 -1.508 22.822 1.722 1.00 49.67 C ANISOU 2423 CG GLN B 153 8147 5071 5653 -1218 1631 374 C ATOM 2424 CD GLN B 153 -2.270 23.867 0.957 1.00 57.53 C ANISOU 2424 CD GLN B 153 9572 5884 6402 -1100 1660 520 C ATOM 2425 OE1 GLN B 153 -2.154 23.970 -0.262 1.00 58.23 O ANISOU 2425 OE1 GLN B 153 9999 5858 6268 -1055 1818 590 O ATOM 2426 NE2 GLN B 153 -3.062 24.655 1.668 1.00 69.81 N ANISOU 2426 NE2 GLN B 153 11148 7399 7978 -1029 1501 558 N ATOM 2427 N ALA B 154 -1.560 17.909 1.889 1.00 49.86 N ANISOU 2427 N ALA B 154 7531 5654 5761 -1036 1111 121 N ATOM 2428 CA ALA B 154 -2.168 16.589 1.899 1.00 50.10 C ANISOU 2428 CA ALA B 154 7490 5799 5748 -940 908 87 C ATOM 2429 C ALA B 154 -3.161 16.424 3.035 1.00 53.76 C ANISOU 2429 C ALA B 154 7857 6298 6272 -906 701 81 C ATOM 2430 O ALA B 154 -4.223 15.830 2.857 1.00 50.55 O ANISOU 2430 O ALA B 154 7477 5938 5793 -822 555 79 O ATOM 2431 CB ALA B 154 -1.085 15.518 1.990 1.00 46.62 C ANISOU 2431 CB ALA B 154 6875 5431 5407 -982 941 -34 C ATOM 2432 N SER B 155 -2.811 16.959 4.201 1.00 60.90 N ANISOU 2432 N SER B 155 8647 7174 7317 -979 704 54 N ATOM 2433 CA SER B 155 -3.649 16.805 5.375 1.00 54.18 C ANISOU 2433 CA SER B 155 7731 6339 6517 -964 553 40 C ATOM 2434 C SER B 155 -4.961 17.557 5.166 1.00 44.90 C ANISOU 2434 C SER B 155 6655 5137 5268 -900 492 102 C ATOM 2435 O SER B 155 -6.048 17.006 5.349 1.00 41.45 O ANISOU 2435 O SER B 155 6192 4744 4814 -853 374 65 O ATOM 2436 CB SER B 155 -2.914 17.289 6.629 1.00 58.61 C ANISOU 2436 CB SER B 155 8183 6863 7222 -1030 562 -12 C ATOM 2437 OG SER B 155 -3.627 16.947 7.812 1.00 50.51 O ANISOU 2437 OG SER B 155 7139 5838 6214 -1013 438 -32 O ATOM 2438 N GLU B 156 -4.870 18.816 4.765 1.00 45.51 N ANISOU 2438 N GLU B 156 6851 5132 5310 -896 578 171 N ATOM 2439 CA GLU B 156 -6.090 19.576 4.558 1.00 57.19 C ANISOU 2439 CA GLU B 156 8440 6577 6712 -790 482 205 C ATOM 2440 C GLU B 156 -6.811 19.148 3.265 1.00 68.68 C ANISOU 2440 C GLU B 156 10033 8061 8003 -643 392 201 C ATOM 2441 O GLU B 156 -8.033 18.966 3.275 1.00 76.13 O ANISOU 2441 O GLU B 156 10936 9052 8937 -539 222 129 O ATOM 2442 CB GLU B 156 -5.799 21.085 4.549 1.00 46.80 C ANISOU 2442 CB GLU B 156 7268 5129 5384 -808 589 282 C ATOM 2443 CG GLU B 156 -4.560 21.468 5.338 0.00 49.93 C ANISOU 2443 CG GLU B 156 7553 5483 5935 -969 739 264 C ATOM 2444 CD GLU B 156 -4.296 22.959 5.319 0.00 53.03 C ANISOU 2444 CD GLU B 156 8093 5724 6333 -1012 870 323 C ATOM 2445 OE1 GLU B 156 -5.272 23.734 5.213 0.00 54.04 O ANISOU 2445 OE1 GLU B 156 8373 5790 6371 -902 782 378 O ATOM 2446 OE2 GLU B 156 -3.117 23.359 5.424 0.00 54.44 O ANISOU 2446 OE2 GLU B 156 8228 5836 6619 -1154 1060 291 O ATOM 2447 N LYS B 157 -6.062 18.942 2.178 1.00 57.98 N ANISOU 2447 N LYS B 157 8822 6678 6530 -634 505 246 N ATOM 2448 CA LYS B 157 -6.674 18.891 0.852 1.00 50.60 C ANISOU 2448 CA LYS B 157 8115 5724 5387 -458 423 259 C ATOM 2449 C LYS B 157 -6.553 17.557 0.083 1.00 49.55 C ANISOU 2449 C LYS B 157 7953 5682 5190 -422 386 202 C ATOM 2450 O LYS B 157 -6.995 17.465 -1.062 1.00 53.64 O ANISOU 2450 O LYS B 157 8678 6184 5520 -259 306 199 O ATOM 2451 CB LYS B 157 -6.093 20.032 -0.005 1.00 43.77 C ANISOU 2451 CB LYS B 157 7589 4689 4352 -433 605 377 C ATOM 2452 N GLY B 158 -5.987 16.521 0.695 1.00 44.69 N ANISOU 2452 N GLY B 158 7114 5153 4714 -546 420 147 N ATOM 2453 CA GLY B 158 -5.721 15.282 -0.032 1.00 40.11 C ANISOU 2453 CA GLY B 158 6522 4643 4076 -521 406 96 C ATOM 2454 C GLY B 158 -6.896 14.312 -0.154 1.00 45.27 C ANISOU 2454 C GLY B 158 7090 5382 4731 -430 193 -16 C ATOM 2455 O GLY B 158 -7.763 14.266 0.724 1.00 49.77 O ANISOU 2455 O GLY B 158 7512 5977 5422 -454 91 -85 O ATOM 2456 N PHE B 159 -6.926 13.520 -1.228 1.00 36.60 N ANISOU 2456 N PHE B 159 6076 4320 3511 -338 146 -57 N ATOM 2457 CA PHE B 159 -8.028 12.576 -1.423 1.00 35.27 C ANISOU 2457 CA PHE B 159 5808 4225 3367 -262 -50 -203 C ATOM 2458 C PHE B 159 -8.196 11.566 -0.276 1.00 34.62 C ANISOU 2458 C PHE B 159 5494 4183 3478 -412 -51 -287 C ATOM 2459 O PHE B 159 -9.270 11.478 0.315 1.00 40.18 O ANISOU 2459 O PHE B 159 6069 4903 4295 -432 -140 -397 O ATOM 2460 CB PHE B 159 -7.877 11.792 -2.734 1.00 36.42 C ANISOU 2460 CB PHE B 159 6085 4400 3353 -147 -94 -242 C ATOM 2461 CG PHE B 159 -9.057 10.894 -3.020 1.00 36.96 C ANISOU 2461 CG PHE B 159 6041 4538 3464 -61 -308 -431 C ATOM 2462 CD1 PHE B 159 -10.151 11.373 -3.733 1.00 39.52 C ANISOU 2462 CD1 PHE B 159 6446 4868 3701 148 -522 -540 C ATOM 2463 CD2 PHE B 159 -9.098 9.599 -2.530 1.00 36.07 C ANISOU 2463 CD2 PHE B 159 5747 4469 3489 -183 -304 -528 C ATOM 2464 CE1 PHE B 159 -11.258 10.564 -3.973 1.00 42.61 C ANISOU 2464 CE1 PHE B 159 6677 5330 4181 221 -727 -776 C ATOM 2465 CE2 PHE B 159 -10.206 8.782 -2.759 1.00 42.53 C ANISOU 2465 CE2 PHE B 159 6441 5334 4383 -142 -465 -736 C ATOM 2466 CZ PHE B 159 -11.280 9.262 -3.486 1.00 44.91 C ANISOU 2466 CZ PHE B 159 6764 5664 4637 53 -676 -876 C ATOM 2467 N GLN B 160 -7.160 10.767 -0.019 1.00 33.07 N ANISOU 2467 N GLN B 160 5268 3989 3308 -506 52 -258 N ATOM 2468 CA GLN B 160 -7.143 9.823 1.101 1.00 35.34 C ANISOU 2468 CA GLN B 160 5435 4267 3726 -626 64 -314 C ATOM 2469 C GLN B 160 -7.412 10.512 2.446 1.00 39.76 C ANISOU 2469 C GLN B 160 5930 4781 4397 -716 98 -289 C ATOM 2470 O GLN B 160 -8.183 10.015 3.251 1.00 31.09 O ANISOU 2470 O GLN B 160 4771 3658 3385 -790 85 -368 O ATOM 2471 CB GLN B 160 -5.801 9.087 1.165 1.00 32.84 C ANISOU 2471 CB GLN B 160 5133 3944 3399 -659 141 -289 C ATOM 2472 CG GLN B 160 -5.533 8.191 -0.027 1.00 45.42 C ANISOU 2472 CG GLN B 160 6783 5581 4894 -584 119 -333 C ATOM 2473 CD GLN B 160 -4.179 7.513 0.033 1.00 47.81 C ANISOU 2473 CD GLN B 160 7074 5885 5207 -597 188 -342 C ATOM 2474 OE1 GLN B 160 -3.189 8.115 0.437 1.00 40.99 O ANISOU 2474 OE1 GLN B 160 6171 5010 4395 -631 279 -309 O ATOM 2475 NE2 GLN B 160 -4.132 6.250 -0.370 1.00 57.61 N ANISOU 2475 NE2 GLN B 160 8334 7139 6416 -565 135 -418 N ATOM 2476 N SER B 161 -6.776 11.654 2.689 1.00 37.10 N ANISOU 2476 N SER B 161 5621 4417 4058 -721 165 -190 N ATOM 2477 CA SER B 161 -7.080 12.411 3.889 1.00 33.66 C ANISOU 2477 CA SER B 161 5135 3939 3715 -786 182 -171 C ATOM 2478 C SER B 161 -8.545 12.804 3.959 1.00 37.64 C ANISOU 2478 C SER B 161 5590 4455 4256 -758 103 -246 C ATOM 2479 O SER B 161 -9.155 12.728 5.018 1.00 37.15 O ANISOU 2479 O SER B 161 5459 4367 4291 -839 122 -302 O ATOM 2480 CB SER B 161 -6.222 13.665 3.971 1.00 33.51 C ANISOU 2480 CB SER B 161 5153 3883 3696 -793 265 -74 C ATOM 2481 OG SER B 161 -6.728 14.535 4.955 1.00 35.10 O ANISOU 2481 OG SER B 161 5320 4047 3971 -828 258 -61 O ATOM 2482 N ARG B 162 -9.120 13.206 2.831 1.00 44.92 N ANISOU 2482 N ARG B 162 6559 5410 5099 -627 13 -272 N ATOM 2483 CA ARG B 162 -10.476 13.738 2.846 1.00 42.87 C ANISOU 2483 CA ARG B 162 6228 5168 4891 -555 -103 -388 C ATOM 2484 C ARG B 162 -11.580 12.706 2.653 1.00 38.43 C ANISOU 2484 C ARG B 162 5526 4662 4416 -556 -192 -598 C ATOM 2485 O ARG B 162 -12.755 13.050 2.757 1.00 42.61 O ANISOU 2485 O ARG B 162 5932 5218 5041 -507 -286 -762 O ATOM 2486 CB ARG B 162 -10.626 14.828 1.780 1.00 48.58 C ANISOU 2486 CB ARG B 162 7112 5874 5471 -363 -200 -341 C ATOM 2487 CG ARG B 162 -10.162 16.196 2.241 1.00 48.29 C ANISOU 2487 CG ARG B 162 7175 5758 5416 -374 -121 -203 C ATOM 2488 CD ARG B 162 -10.389 17.253 1.181 1.00 53.11 C ANISOU 2488 CD ARG B 162 8026 6305 5850 -171 -207 -156 C ATOM 2489 NE ARG B 162 -11.771 17.732 1.112 1.00 56.64 N ANISOU 2489 NE ARG B 162 8423 6772 6324 0 -423 -311 N ATOM 2490 CZ ARG B 162 -12.313 18.589 1.976 1.00 56.38 C ANISOU 2490 CZ ARG B 162 8306 6717 6398 -8 -447 -344 C ATOM 2491 NH1 ARG B 162 -11.606 19.052 2.998 1.00 56.04 N ANISOU 2491 NH1 ARG B 162 8233 6625 6434 -180 -274 -220 N ATOM 2492 NH2 ARG B 162 -13.569 18.979 1.827 1.00 52.19 N ANISOU 2492 NH2 ARG B 162 7707 6215 5907 173 -661 -530 N ATOM 2493 N HIS B 163 -11.238 11.450 2.378 1.00 38.84 N ANISOU 2493 N HIS B 163 5578 4726 4455 -612 -161 -628 N ATOM 2494 CA HIS B 163 -12.299 10.482 2.069 1.00 46.16 C ANISOU 2494 CA HIS B 163 6370 5692 5476 -621 -236 -856 C ATOM 2495 C HIS B 163 -12.122 9.092 2.653 1.00 40.09 C ANISOU 2495 C HIS B 163 5581 4876 4776 -797 -111 -902 C ATOM 2496 O HIS B 163 -13.065 8.305 2.630 1.00 37.06 O ANISOU 2496 O HIS B 163 5073 4496 4514 -864 -115 -1114 O ATOM 2497 CB HIS B 163 -12.463 10.326 0.550 1.00 44.58 C ANISOU 2497 CB HIS B 163 6233 5552 5153 -422 -412 -923 C ATOM 2498 CG HIS B 163 -12.907 11.572 -0.144 1.00 50.37 C ANISOU 2498 CG HIS B 163 7047 6301 5791 -203 -574 -928 C ATOM 2499 ND1 HIS B 163 -12.227 12.101 -1.219 1.00 52.80 N ANISOU 2499 ND1 HIS B 163 7610 6586 5866 -33 -620 -784 N ATOM 2500 CD2 HIS B 163 -13.957 12.395 0.081 1.00 62.64 C ANISOU 2500 CD2 HIS B 163 8495 7871 7435 -113 -697 -1069 C ATOM 2501 CE1 HIS B 163 -12.840 13.199 -1.627 1.00 67.11 C ANISOU 2501 CE1 HIS B 163 9518 8380 7602 165 -774 -818 C ATOM 2502 NE2 HIS B 163 -13.891 13.401 -0.853 1.00 71.99 N ANISOU 2502 NE2 HIS B 163 9900 9031 8421 133 -844 -998 N ATOM 2503 N LEU B 164 -10.932 8.764 3.150 1.00 32.93 N ANISOU 2503 N LEU B 164 4802 3912 3796 -862 -5 -735 N ATOM 2504 CA LEU B 164 -10.645 7.357 3.441 1.00 35.12 C ANISOU 2504 CA LEU B 164 5138 4127 4080 -965 70 -772 C ATOM 2505 C LEU B 164 -10.127 7.095 4.856 1.00 45.16 C ANISOU 2505 C LEU B 164 6522 5279 5359 -1088 205 -691 C ATOM 2506 O LEU B 164 -9.358 7.882 5.420 1.00 43.85 O ANISOU 2506 O LEU B 164 6406 5100 5154 -1061 218 -559 O ATOM 2507 CB LEU B 164 -9.629 6.797 2.421 1.00 36.81 C ANISOU 2507 CB LEU B 164 5444 4379 4165 -862 14 -701 C ATOM 2508 CG LEU B 164 -9.951 6.847 0.921 1.00 39.55 C ANISOU 2508 CG LEU B 164 5769 4818 4439 -712 -121 -768 C ATOM 2509 CD1 LEU B 164 -8.892 6.096 0.134 1.00 40.61 C ANISOU 2509 CD1 LEU B 164 6010 4967 4452 -649 -122 -708 C ATOM 2510 CD2 LEU B 164 -11.353 6.303 0.621 1.00 38.25 C ANISOU 2510 CD2 LEU B 164 5467 4676 4391 -727 -202 -1009 C ATOM 2511 N ALA B 165 -10.535 5.962 5.417 1.00 43.26 N ANISOU 2511 N ALA B 165 6350 4931 5156 -1215 307 -785 N ATOM 2512 CA ALA B 165 -10.016 5.543 6.706 1.00 45.00 C ANISOU 2512 CA ALA B 165 6777 4999 5324 -1294 419 -712 C ATOM 2513 C ALA B 165 -9.208 4.263 6.548 1.00 45.65 C ANISOU 2513 C ALA B 165 7040 5000 5304 -1262 402 -692 C ATOM 2514 O ALA B 165 -9.426 3.498 5.611 1.00 45.78 O ANISOU 2514 O ALA B 165 7011 5053 5331 -1252 364 -776 O ATOM 2515 CB ALA B 165 -11.146 5.345 7.697 1.00 49.54 C ANISOU 2515 CB ALA B 165 7379 5453 5990 -1478 604 -828 C ATOM 2516 N CYS B 166 -8.279 4.030 7.468 1.00 41.83 N ANISOU 2516 N CYS B 166 6772 4403 4719 -1222 406 -601 N ATOM 2517 CA CYS B 166 -7.455 2.831 7.421 1.00 36.75 C ANISOU 2517 CA CYS B 166 6330 3664 3967 -1152 358 -598 C ATOM 2518 C CYS B 166 -8.000 1.812 8.406 1.00 44.04 C ANISOU 2518 C CYS B 166 7554 4346 4832 -1275 512 -645 C ATOM 2519 O CYS B 166 -7.707 1.875 9.593 1.00 48.68 O ANISOU 2519 O CYS B 166 8387 4784 5324 -1262 551 -589 O ATOM 2520 CB CYS B 166 -5.995 3.163 7.732 1.00 39.69 C ANISOU 2520 CB CYS B 166 6758 4059 4264 -981 223 -516 C ATOM 2521 SG CYS B 166 -4.846 1.806 7.478 1.00 65.51 S ANISOU 2521 SG CYS B 166 10215 7255 7422 -828 102 -553 S ATOM 2522 N LEU B 167 -8.784 0.869 7.884 1.00 51.40 N ANISOU 2522 N LEU B 167 8490 5225 5814 -1393 606 -759 N ATOM 2523 CA LEU B 167 -9.577 -0.066 8.675 1.00 41.86 C ANISOU 2523 CA LEU B 167 7548 3768 4588 -1580 835 -840 C ATOM 2524 C LEU B 167 -9.217 -1.524 8.420 1.00 53.34 C ANISOU 2524 C LEU B 167 9264 5063 5941 -1561 836 -874 C ATOM 2525 O LEU B 167 -8.739 -1.871 7.338 1.00 53.50 O ANISOU 2525 O LEU B 167 9147 5212 5969 -1445 676 -892 O ATOM 2526 CB LEU B 167 -11.050 0.146 8.375 1.00 38.54 C ANISOU 2526 CB LEU B 167 6867 3400 4378 -1792 1000 -1016 C ATOM 2527 CG LEU B 167 -11.483 1.590 8.580 1.00 41.54 C ANISOU 2527 CG LEU B 167 6988 3933 4862 -1791 981 -1004 C ATOM 2528 CD1 LEU B 167 -12.962 1.757 8.254 1.00 38.85 C ANISOU 2528 CD1 LEU B 167 6356 3651 4753 -1966 1109 -1238 C ATOM 2529 CD2 LEU B 167 -11.153 2.026 10.006 1.00 40.10 C ANISOU 2529 CD2 LEU B 167 7070 3602 4563 -1802 1080 -884 C ATOM 2530 N PRO B 168 -9.443 -2.391 9.423 1.00 56.61 N ANISOU 2530 N PRO B 168 10098 5171 6238 -1670 1032 -883 N ATOM 2531 CA PRO B 168 -9.140 -3.814 9.207 1.00 51.65 C ANISOU 2531 CA PRO B 168 9774 4352 5500 -1650 1042 -917 C ATOM 2532 C PRO B 168 -10.134 -4.498 8.289 1.00 51.76 C ANISOU 2532 C PRO B 168 9591 4385 5692 -1845 1170 -1100 C ATOM 2533 O PRO B 168 -11.326 -4.248 8.417 1.00 55.95 O ANISOU 2533 O PRO B 168 9941 4918 6400 -2075 1387 -1232 O ATOM 2534 CB PRO B 168 -9.216 -4.408 10.616 1.00 46.99 C ANISOU 2534 CB PRO B 168 9692 3449 4715 -1693 1240 -846 C ATOM 2535 CG PRO B 168 -10.020 -3.412 11.412 1.00 46.58 C ANISOU 2535 CG PRO B 168 9512 3443 4742 -1835 1427 -837 C ATOM 2536 CD PRO B 168 -9.760 -2.085 10.834 1.00 41.86 C ANISOU 2536 CD PRO B 168 8523 3098 4282 -1767 1227 -835 C ATOM 2537 N ARG B 169 -9.648 -5.328 7.368 1.00 57.23 N ANISOU 2537 N ARG B 169 10280 5110 6354 -1737 1025 -1132 N ATOM 2538 CA ARG B 169 -10.519 -6.169 6.546 1.00 55.37 C ANISOU 2538 CA ARG B 169 9917 4850 6269 -1909 1132 -1328 C ATOM 2539 C ARG B 169 -10.548 -7.543 7.185 1.00 59.42 C ANISOU 2539 C ARG B 169 10839 5082 6657 -1960 1308 -1297 C ATOM 2540 O ARG B 169 -11.514 -8.299 7.032 1.00 56.11 O ANISOU 2540 O ARG B 169 10342 4609 6367 -2144 1513 -1425 O ATOM 2541 CB ARG B 169 -10.034 -6.272 5.096 1.00 43.57 C ANISOU 2541 CB ARG B 169 8139 3605 4811 -1727 865 -1360 C ATOM 2542 CG ARG B 169 -10.035 -4.966 4.324 1.00 53.02 C ANISOU 2542 CG ARG B 169 8902 5137 6105 -1612 685 -1338 C ATOM 2543 CD ARG B 169 -11.336 -4.727 3.536 1.00 64.30 C ANISOU 2543 CD ARG B 169 9967 6700 7764 -1748 719 -1561 C ATOM 2544 NE ARG B 169 -11.194 -3.606 2.598 1.00 67.30 N ANISOU 2544 NE ARG B 169 10027 7374 8169 -1569 498 -1529 N ATOM 2545 CZ ARG B 169 -12.171 -3.101 1.842 1.00 65.00 C ANISOU 2545 CZ ARG B 169 9418 7241 8039 -1583 431 -1708 C ATOM 2546 NH1 ARG B 169 -13.396 -3.608 1.894 1.00 63.22 N ANISOU 2546 NH1 ARG B 169 9065 6938 8015 -1786 566 -1975 N ATOM 2547 NH2 ARG B 169 -11.915 -2.081 1.023 1.00 63.73 N ANISOU 2547 NH2 ARG B 169 9079 7301 7835 -1386 228 -1643 N ATOM 2548 N GLU B 170 -9.464 -7.842 7.899 1.00 61.46 N ANISOU 2548 N GLU B 170 11500 5193 6658 -1757 1203 -1126 N ATOM 2549 CA GLU B 170 -9.278 -9.105 8.606 1.00 66.87 C ANISOU 2549 CA GLU B 170 12637 5627 7146 -1721 1314 -1044 C ATOM 2550 C GLU B 170 -8.036 -8.959 9.471 1.00 64.38 C ANISOU 2550 C GLU B 170 12690 5213 6558 -1437 1114 -873 C ATOM 2551 O GLU B 170 -7.293 -7.996 9.303 1.00 68.98 O ANISOU 2551 O GLU B 170 13121 5937 7150 -1277 882 -853 O ATOM 2552 CB GLU B 170 -9.137 -10.278 7.626 1.00 70.92 C ANISOU 2552 CB GLU B 170 13163 6101 7681 -1693 1243 -1135 C ATOM 2553 CG GLU B 170 -7.760 -10.389 6.994 1.00 70.54 C ANISOU 2553 CG GLU B 170 13178 6114 7511 -1385 888 -1102 C ATOM 2554 CD GLU B 170 -7.449 -11.815 6.585 1.00 77.45 C ANISOU 2554 CD GLU B 170 14279 6849 8299 -1304 846 -1128 C ATOM 2555 OE1 GLU B 170 -8.380 -12.654 6.641 1.00 83.73 O ANISOU 2555 OE1 GLU B 170 15140 7516 9158 -1521 1098 -1186 O ATOM 2556 OE2 GLU B 170 -6.283 -12.099 6.219 1.00 70.76 O ANISOU 2556 OE2 GLU B 170 13529 6028 7331 -1024 569 -1108 O ATOM 2557 N PRO B 171 -7.812 -9.889 10.413 1.00 71.40 N ANISOU 2557 N PRO B 171 14068 5864 7197 -1362 1195 -769 N ATOM 2558 CA PRO B 171 -6.621 -9.770 11.267 1.00 72.45 C ANISOU 2558 CA PRO B 171 14552 5911 7066 -1045 950 -637 C ATOM 2559 C PRO B 171 -5.307 -9.786 10.504 1.00 68.25 C ANISOU 2559 C PRO B 171 13914 5487 6530 -732 552 -674 C ATOM 2560 O PRO B 171 -5.114 -10.636 9.631 1.00 69.20 O ANISOU 2560 O PRO B 171 13998 5609 6685 -693 480 -743 O ATOM 2561 CB PRO B 171 -6.726 -10.990 12.179 1.00 62.73 C ANISOU 2561 CB PRO B 171 13885 4403 5547 -1029 1110 -550 C ATOM 2562 CG PRO B 171 -8.186 -11.193 12.302 1.00 69.64 C ANISOU 2562 CG PRO B 171 14681 5236 6541 -1407 1549 -618 C ATOM 2563 CD PRO B 171 -8.744 -10.903 10.933 1.00 73.02 C ANISOU 2563 CD PRO B 171 14537 5875 7334 -1577 1545 -779 C ATOM 2564 N GLY B 172 -4.428 -8.841 10.845 1.00 57.32 N ANISOU 2564 N GLY B 172 12459 4205 5116 -513 309 -652 N ATOM 2565 CA GLY B 172 -3.132 -8.706 10.206 1.00 50.50 C ANISOU 2565 CA GLY B 172 11428 3489 4270 -209 -52 -733 C ATOM 2566 C GLY B 172 -3.218 -7.839 8.964 1.00 53.69 C ANISOU 2566 C GLY B 172 11322 4173 4906 -314 -83 -846 C ATOM 2567 O GLY B 172 -2.205 -7.495 8.355 1.00 57.70 O ANISOU 2567 O GLY B 172 11523 4920 5481 -103 -324 -891 O ATOM 2568 N LEU B 173 -4.439 -7.461 8.599 1.00 54.92 N ANISOU 2568 N LEU B 173 11237 4406 5225 -627 174 -841 N ATOM 2569 CA LEU B 173 -4.669 -6.767 7.345 1.00 52.66 C ANISOU 2569 CA LEU B 173 10376 4468 5162 -704 150 -876 C ATOM 2570 C LEU B 173 -5.526 -5.518 7.468 1.00 57.67 C ANISOU 2570 C LEU B 173 10704 5259 5951 -896 291 -842 C ATOM 2571 O LEU B 173 -6.691 -5.587 7.871 1.00 62.01 O ANISOU 2571 O LEU B 173 11327 5679 6554 -1143 538 -872 O ATOM 2572 CB LEU B 173 -5.332 -7.700 6.347 1.00 50.72 C ANISOU 2572 CB LEU B 173 10072 4206 4992 -841 244 -976 C ATOM 2573 CG LEU B 173 -5.627 -7.024 5.015 1.00 45.41 C ANISOU 2573 CG LEU B 173 8874 3870 4510 -886 197 -1023 C ATOM 2574 CD1 LEU B 173 -4.326 -6.541 4.416 1.00 40.45 C ANISOU 2574 CD1 LEU B 173 8037 3470 3862 -629 -39 -992 C ATOM 2575 CD2 LEU B 173 -6.327 -7.999 4.094 1.00 47.06 C ANISOU 2575 CD2 LEU B 173 9048 4044 4788 -1006 267 -1153 C ATOM 2576 N CYS B 174 -4.949 -4.385 7.080 1.00 53.00 N ANISOU 2576 N CYS B 174 9758 4937 5442 -786 148 -801 N ATOM 2577 CA CYS B 174 -5.713 -3.149 6.975 1.00 51.74 C ANISOU 2577 CA CYS B 174 9280 4950 5430 -932 244 -775 C ATOM 2578 C CYS B 174 -5.616 -2.560 5.555 1.00 46.27 C ANISOU 2578 C CYS B 174 8173 4550 4859 -891 151 -799 C ATOM 2579 O CYS B 174 -4.600 -2.703 4.870 1.00 40.52 O ANISOU 2579 O CYS B 174 7366 3932 4099 -721 5 -804 O ATOM 2580 CB CYS B 174 -5.234 -2.136 8.021 1.00 46.26 C ANISOU 2580 CB CYS B 174 8625 4255 4696 -857 199 -688 C ATOM 2581 SG CYS B 174 -5.521 -2.666 9.726 1.00 65.56 S ANISOU 2581 SG CYS B 174 11619 6335 6956 -902 334 -653 S ATOM 2582 N THR B 175 -6.694 -1.925 5.107 1.00 42.58 N ANISOU 2582 N THR B 175 7465 4193 4520 -1038 242 -835 N ATOM 2583 CA THR B 175 -6.693 -1.213 3.834 1.00 50.70 C ANISOU 2583 CA THR B 175 8178 5468 5618 -976 152 -846 C ATOM 2584 C THR B 175 -7.514 0.056 3.950 1.00 54.63 C ANISOU 2584 C THR B 175 8473 6066 6217 -1057 202 -832 C ATOM 2585 O THR B 175 -8.385 0.173 4.823 1.00 57.67 O ANISOU 2585 O THR B 175 8903 6345 6663 -1206 332 -867 O ATOM 2586 CB THR B 175 -7.275 -2.055 2.656 1.00 53.03 C ANISOU 2586 CB THR B 175 8396 5804 5949 -1000 132 -974 C ATOM 2587 OG1 THR B 175 -8.594 -2.511 2.991 1.00 52.97 O ANISOU 2587 OG1 THR B 175 8401 5679 6046 -1201 273 -1104 O ATOM 2588 CG2 THR B 175 -6.369 -3.247 2.294 1.00 50.51 C ANISOU 2588 CG2 THR B 175 8248 5418 5527 -886 56 -992 C ATOM 2589 N TRP B 176 -7.224 0.996 3.056 1.00 49.01 N ANISOU 2589 N TRP B 176 7566 5542 5513 -955 113 -790 N ATOM 2590 CA TRP B 176 -8.039 2.183 2.857 1.00 38.68 C ANISOU 2590 CA TRP B 176 6076 4338 4284 -985 116 -795 C ATOM 2591 C TRP B 176 -9.485 1.839 2.499 1.00 35.13 C ANISOU 2591 C TRP B 176 5513 3888 3947 -1085 139 -973 C ATOM 2592 O TRP B 176 -9.725 1.081 1.566 1.00 51.71 O ANISOU 2592 O TRP B 176 7583 6020 6046 -1053 78 -1082 O ATOM 2593 CB TRP B 176 -7.442 3.046 1.747 1.00 34.47 C ANISOU 2593 CB TRP B 176 5444 3963 3692 -839 27 -727 C ATOM 2594 CG TRP B 176 -6.166 3.720 2.070 1.00 39.45 C ANISOU 2594 CG TRP B 176 6100 4613 4277 -775 39 -601 C ATOM 2595 CD1 TRP B 176 -4.966 3.523 1.464 1.00 44.29 C ANISOU 2595 CD1 TRP B 176 6727 5275 4828 -677 20 -577 C ATOM 2596 CD2 TRP B 176 -5.959 4.743 3.055 1.00 49.03 C ANISOU 2596 CD2 TRP B 176 7296 5802 5531 -809 80 -521 C ATOM 2597 NE1 TRP B 176 -4.018 4.354 2.014 1.00 48.27 N ANISOU 2597 NE1 TRP B 176 7198 5787 5356 -659 53 -510 N ATOM 2598 CE2 TRP B 176 -4.604 5.110 2.996 1.00 48.90 C ANISOU 2598 CE2 TRP B 176 7269 5821 5491 -733 77 -468 C ATOM 2599 CE3 TRP B 176 -6.790 5.381 3.986 1.00 52.33 C ANISOU 2599 CE3 TRP B 176 7695 6173 6016 -899 126 -513 C ATOM 2600 CZ2 TRP B 176 -4.055 6.082 3.835 1.00 41.88 C ANISOU 2600 CZ2 TRP B 176 6347 4917 4649 -743 102 -413 C ATOM 2601 CZ3 TRP B 176 -6.243 6.353 4.815 1.00 43.44 C ANISOU 2601 CZ3 TRP B 176 6565 5032 4909 -897 147 -431 C ATOM 2602 CH2 TRP B 176 -4.888 6.688 4.733 1.00 39.33 C ANISOU 2602 CH2 TRP B 176 6031 4543 4368 -819 126 -384 C ATOM 2603 N GLN B 177 -10.444 2.404 3.228 1.00 43.60 N ANISOU 2603 N GLN B 177 6502 4930 5132 -1201 224 -1035 N ATOM 2604 CA GLN B 177 -11.870 2.219 2.916 1.00 51.03 C ANISOU 2604 CA GLN B 177 7262 5891 6237 -1297 244 -1271 C ATOM 2605 C GLN B 177 -12.608 3.554 2.906 1.00 48.27 C ANISOU 2605 C GLN B 177 6716 5650 5976 -1253 185 -1316 C ATOM 2606 O GLN B 177 -12.142 4.553 3.470 1.00 47.24 O ANISOU 2606 O GLN B 177 6625 5532 5794 -1215 196 -1155 O ATOM 2607 CB GLN B 177 -12.542 1.256 3.909 1.00 46.32 C ANISOU 2607 CB GLN B 177 6758 5101 5740 -1535 469 -1398 C ATOM 2608 CG GLN B 177 -11.735 -0.024 4.143 1.00 51.52 C ANISOU 2608 CG GLN B 177 7703 5598 6273 -1560 532 -1324 C ATOM 2609 CD GLN B 177 -12.460 -1.070 4.977 1.00 57.15 C ANISOU 2609 CD GLN B 177 8581 6075 7059 -1805 788 -1460 C ATOM 2610 OE1 GLN B 177 -13.686 -1.042 5.120 1.00 67.14 O ANISOU 2610 OE1 GLN B 177 9671 7319 8520 -1984 931 -1678 O ATOM 2611 NE2 GLN B 177 -11.697 -2.010 5.526 1.00 50.36 N ANISOU 2611 NE2 GLN B 177 8074 5018 6042 -1809 856 -1354 N ATOM 2612 N SER B 178 -13.765 3.547 2.257 1.00 51.08 N ANISOU 2612 N SER B 178 6855 6078 6473 -1245 106 -1565 N ATOM 2613 CA SER B 178 -14.592 4.733 2.080 1.00 59.59 C ANISOU 2613 CA SER B 178 7736 7263 7641 -1153 -6 -1671 C ATOM 2614 C SER B 178 -15.684 4.841 3.155 1.00 64.28 C ANISOU 2614 C SER B 178 8174 7792 8458 -1357 173 -1865 C ATOM 2615 O SER B 178 -16.364 3.860 3.473 1.00 69.03 O ANISOU 2615 O SER B 178 8709 8304 9216 -1557 336 -2079 O ATOM 2616 CB SER B 178 -15.219 4.726 0.678 1.00 64.20 C ANISOU 2616 CB SER B 178 8176 7973 8245 -961 -256 -1877 C ATOM 2617 OG SER B 178 -15.857 5.962 0.390 1.00 72.41 O ANISOU 2617 OG SER B 178 9091 9106 9314 -793 -425 -1957 O ATOM 2618 N LEU B 179 -15.850 6.044 3.701 1.00 64.67 N ANISOU 2618 N LEU B 179 8171 7875 8524 -1318 168 -1803 N ATOM 2619 CA LEU B 179 -16.831 6.298 4.749 1.00 74.86 C ANISOU 2619 CA LEU B 179 9316 9112 10016 -1501 354 -1981 C ATOM 2620 C LEU B 179 -18.181 6.751 4.184 1.00 80.59 C ANISOU 2620 C LEU B 179 9694 9959 10968 -1423 207 -2343 C ATOM 2621 O LEU B 179 -18.796 6.052 3.367 1.00 85.48 O ANISOU 2621 O LEU B 179 10146 10626 11706 -1401 108 -2611 O ATOM 2622 CB LEU B 179 -16.301 7.347 5.720 1.00 78.27 C ANISOU 2622 CB LEU B 179 9873 9510 10355 -1494 423 -1746 C ATOM 2623 CG LEU B 179 -15.021 7.062 6.516 1.00 74.50 C ANISOU 2623 CG LEU B 179 9713 8909 9685 -1550 546 -1442 C ATOM 2624 CD1 LEU B 179 -13.780 7.196 5.672 1.00 75.43 C ANISOU 2624 CD1 LEU B 179 9958 9093 9610 -1360 365 -1218 C ATOM 2625 CD2 LEU B 179 -14.931 7.999 7.690 1.00 66.10 C ANISOU 2625 CD2 LEU B 179 8711 7794 8609 -1595 650 -1333 C TER 2626 LEU B 179 HETATM 2627 CA CA A 301 8.838 14.637 15.097 1.00 47.42 CA HETATM 2628 CA CA A 302 17.658 9.285 13.365 1.00 74.88 CA HETATM 2629 ZN ZN A 303 14.781 22.523 20.708 1.00 50.31 ZN HETATM 2630 ZN ZN A 304 9.331 27.184 10.494 1.00 36.61 ZN HETATM 2631 CA CA A 305 23.111 31.304 19.392 1.00 48.78 CA HETATM 2632 O HOH A 401 21.815 44.900 7.851 1.00 43.57 O HETATM 2633 O HOH A 402 10.878 13.637 1.151 1.00 43.91 O HETATM 2634 O HOH A 403 11.756 12.991 19.007 1.00 37.81 O HETATM 2635 O HOH A 404 5.767 42.614 19.427 1.00 51.46 O HETATM 2636 O HOH A 405 20.269 16.637 2.690 1.00 50.79 O HETATM 2637 O HOH A 406 24.627 29.926 20.809 1.00 54.39 O HETATM 2638 O HOH A 407 13.079 20.180 24.902 1.00 29.72 O HETATM 2639 O HOH A 408 19.906 30.912 -3.618 1.00 32.00 O HETATM 2640 O HOH A 409 12.759 34.221 12.960 1.00 39.81 O HETATM 2641 O HOH A 410 9.587 9.949 29.124 1.00 61.08 O HETATM 2642 O HOH A 411 25.274 34.204 19.606 1.00 42.53 O HETATM 2643 O HOH A 412 23.263 43.779 10.088 1.00 63.47 O HETATM 2644 O HOH A 413 28.231 37.530 0.212 1.00 47.40 O HETATM 2645 O HOH A 414 26.119 34.241 22.311 1.00 35.95 O HETATM 2646 O HOH A 415 6.505 36.537 5.018 1.00 35.07 O HETATM 2647 O HOH A 416 18.344 31.895 -5.361 1.00 37.67 O HETATM 2648 O HOH A 417 31.703 41.385 5.019 1.00 55.75 O HETATM 2649 O HOH A 418 -0.735 28.278 6.564 1.00 54.69 O HETATM 2650 O HOH A 419 16.106 9.743 25.849 1.00 50.27 O HETATM 2651 O HOH A 420 32.973 17.239 16.005 1.00 54.37 O HETATM 2652 O HOH A 421 32.813 16.048 17.954 1.00 81.70 O HETATM 2653 O HOH B 201 -18.201 34.006 12.917 1.00 65.66 O HETATM 2654 O HOH B 202 -22.443 23.462 18.401 1.00 70.47 O HETATM 2655 O HOH B 203 -0.702 -1.343 12.859 1.00 33.92 O HETATM 2656 O HOH B 204 -19.242 21.340 6.282 1.00 40.03 O HETATM 2657 O HOH B 205 -10.386 10.495 6.448 1.00 37.87 O HETATM 2658 O HOH B 206 8.619 23.031 19.026 1.00 47.98 O HETATM 2659 O HOH B 207 -5.093 4.843 12.856 1.00 43.31 O HETATM 2660 O HOH B 208 -19.528 22.046 27.559 1.00 74.78 O HETATM 2661 O HOH B 209 -2.412 6.147 12.162 1.00 34.07 O HETATM 2662 O HOH B 210 -1.182 15.257 18.825 1.00 48.70 O HETATM 2663 O HOH B 211 2.209 22.289 22.621 1.00 49.92 O HETATM 2664 O HOH B 212 -0.362 10.283 9.435 1.00 30.46 O HETATM 2665 O HOH B 213 -14.471 -1.262 -0.138 1.00 51.46 O HETATM 2666 O HOH B 214 0.011 28.762 13.246 1.00 45.73 O HETATM 2667 O HOH B 215 -2.155 3.992 -1.369 1.00 69.19 O HETATM 2668 O HOH B 216 -2.039 -2.278 3.002 1.00 61.03 O HETATM 2669 O HOH B 217 2.989 12.732 10.662 1.00 45.85 O HETATM 2670 O HOH B 218 -15.985 9.137 1.543 1.00 51.28 O HETATM 2671 O HOH B 219 -3.708 7.786 22.629 1.00 44.18 O HETATM 2672 O HOH B 220 -5.972 0.000 0.000 0.50 57.87 O HETATM 2673 O HOH B 221 -3.928 -0.086 2.093 1.00 50.61 O HETATM 2674 O HOH B 222 12.986 -3.458 8.932 1.00 53.39 O HETATM 2675 O HOH B 223 -1.411 7.567 21.672 1.00 68.05 O HETATM 2676 O HOH B 224 -12.649 -1.917 18.360 1.00 40.48 O HETATM 2677 O HOH B 225 0.152 27.628 8.879 1.00 42.18 O CONECT 180 2628 CONECT 181 2628 CONECT 445 2631 CONECT 532 2629 CONECT 544 2629 CONECT 592 2627 CONECT 597 2627 CONECT 608 2627 CONECT 620 2627 CONECT 646 2629 CONECT 690 2631 CONECT 702 2631 CONECT 717 2631 CONECT 730 2629 CONECT 752 2627 CONECT 756 2628 CONECT 759 2628 CONECT 772 2628 CONECT 777 2627 CONECT 911 2630 CONECT 942 2630 CONECT 989 2630 CONECT 1274 2630 CONECT 1277 2630 CONECT 1279 1791 CONECT 1292 2020 CONECT 1368 2206 CONECT 1791 1279 CONECT 2020 1292 CONECT 2206 1368 CONECT 2230 2581 CONECT 2268 2302 CONECT 2302 2268 CONECT 2357 2521 CONECT 2521 2357 CONECT 2581 2230 CONECT 2627 592 597 608 620 CONECT 2627 752 777 CONECT 2628 180 181 756 759 CONECT 2628 772 CONECT 2629 532 544 646 730 CONECT 2630 911 942 989 1274 CONECT 2630 1277 CONECT 2631 445 690 702 717 CONECT 2631 2637 CONECT 2637 2631 MASTER 506 0 5 10 19 0 7 6 2675 2 46 28 END
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Related entries of code: 6n9d
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RCSB PDB
PDBbind
161aa, >2JT5_1|Chain... at 100%
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RCSB PDB
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RCSB PDB
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Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
No complexes with the same small molecule ligand are found!
Entry Information
PDB ID
6n9d
Complex Type
Protein-Protein
PDBbind Subset
general set
Protein Name
matrix metalloproteinase-3 catalytic domain (MMP-3cd)
Ligand Name
tissue inhibitor of metalloproteinase-1 (TIMP-1) C1 mutant (L34G/L133P/L151C/G154A)
EC.Number
E.C.3.4.24.17
Resolution
2.67(Å)
Affinity (Kd/Ki/IC50)
Ki=17.8pM
Release Year
2019
Protein/NA Sequence
Check fasta file
Primary Reference
(2019) J.Biol.Chem. Vol. 294: pp. 9476-9488
Links to External Databases
RCSB PDB
The mother database
PDBsum
Enhanced annotations on PDB entries
Pubchem
Comprehensive collection of chemical and biological data
UniProtKB AC
UniProt accession number (AC):
P01033
P08254
Entrez Gene ID
NCBI Entrez Gene ID:
7076
4314
ASD
Information of known allosteric effects of PDB entries
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