HEADER MEMBRANE PROTEIN 19-JAN-18 6FJ3 TITLE HIGH RESOLUTION CRYSTAL STRUCTURE OF PARATHYROID HORMONE 1 RECEPTOR IN TITLE 2 COMPLEX WITH A PEPTIDE AGONIST. CAVEAT 6FJ3 FUC C 6 HAS WRONG CHIRALITY AT ATOM C1 FUC D 4 HAS WRONG CAVEAT 2 6FJ3 CHIRALITY AT ATOM C1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: PARATHYROID HORMONE/PARATHYROID HORMONE-RELATED PEPTIDE COMPND 3 RECEPTOR,PARATHYROID HORMONE/PARATHYROID HORMONE-RELATED PEPTIDE COMPND 4 RECEPTOR,GLGA GLYCOGEN SYNTHASE,PARATHYROID HORMONE/PARATHYROID COMPND 5 HORMONE-RELATED PEPTIDE RECEPTOR; COMPND 6 CHAIN: A; COMPND 7 SYNONYM: PTH/PTHRP TYPE I RECEPTOR,PTH/PTHR RECEPTOR,PARATHYROID COMPND 8 HORMONE 1 RECEPTOR,PTH1 RECEPTOR,PTH/PTHRP TYPE I RECEPTOR,PTH/PTHR COMPND 9 RECEPTOR,PARATHYROID HORMONE 1 RECEPTOR,PTH1 RECEPTOR,GLYCOGEN COMPND 10 SYNTHASE,PTH/PTHRP TYPE I RECEPTOR,PTH/PTHR RECEPTOR,PARATHYROID COMPND 11 HORMONE 1 RECEPTOR,PTH1 RECEPTOR; COMPND 12 ENGINEERED: YES; COMPND 13 MUTATION: YES; COMPND 14 MOL_ID: 2; COMPND 15 MOLECULE: PARATHYROID HORMONE; COMPND 16 CHAIN: B; COMPND 17 SYNONYM: PTH,PARATHYRIN; COMPND 18 ENGINEERED: YES; COMPND 19 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, PYROCOCCUS ABYSSI (STRAIN GE5 / SOURCE 3 ORSAY); SOURCE 4 ORGANISM_COMMON: HUMAN; SOURCE 5 ORGANISM_TAXID: 9606, 272844; SOURCE 6 STRAIN: GE5 / ORSAY; SOURCE 7 GENE: PTH1R, PTHR, PTHR1, PAB2292; SOURCE 8 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 9 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS EXPRESSION VECTOR SOURCE 11 PFASTBAC1-HM; SOURCE 12 MOL_ID: 2; SOURCE 13 ORGANISM_SCIENTIFIC: EQUUS CABALLUS; SOURCE 14 ORGANISM_COMMON: HORSE; SOURCE 15 ORGANISM_TAXID: 9796; SOURCE 16 GENE: PTH; SOURCE 17 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 18 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS EXPRESSION VECTOR SOURCE 20 PFASTBAC1-HM KEYWDS GPCR, CELL SIGNALLING, 7TM, MEMBRANE PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR J.EHRENMANN,J.SCHOPPE,C.KLENK,M.RAPPAS,L.KUMMER,A.S.DORE,A.PLUCKTHUN REVDAT 4 29-JUL-20 6FJ3 1 CAVEAT COMPND REMARK HETNAM REVDAT 4 2 1 LINK SITE ATOM REVDAT 3 19-DEC-18 6FJ3 1 JRNL REVDAT 2 28-NOV-18 6FJ3 1 JRNL REVDAT 1 21-NOV-18 6FJ3 0 JRNL AUTH J.EHRENMANN,J.SCHOPPE,C.KLENK,M.RAPPAS,L.KUMMER,A.S.DORE, JRNL AUTH 2 A.PLUCKTHUN JRNL TITL HIGH-RESOLUTION CRYSTAL STRUCTURE OF PARATHYROID HORMONE 1 JRNL TITL 2 RECEPTOR IN COMPLEX WITH A PEPTIDE AGONIST. JRNL REF NAT. STRUCT. MOL. BIOL. V. 25 1086 2018 JRNL REFN ESSN 1545-9985 JRNL PMID 30455434 JRNL DOI 10.1038/S41594-018-0151-4 REMARK 2 REMARK 2 RESOLUTION. 2.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.13_2998: ???) 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 : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.39 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.970 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 3 NUMBER OF REFLECTIONS : 33645 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.211 REMARK 3 R VALUE (WORKING SET) : 0.209 REMARK 3 FREE R VALUE : 0.248 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.920 REMARK 3 FREE R VALUE TEST SET COUNT : 1657 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 49.3955 - 5.7211 1.00 2683 135 0.1955 0.2587 REMARK 3 2 5.7211 - 4.5420 1.00 2665 135 0.1826 0.2135 REMARK 3 3 4.5420 - 3.9681 1.00 2672 120 0.1728 0.1645 REMARK 3 4 3.9681 - 3.6054 1.00 2675 142 0.1748 0.2009 REMARK 3 5 3.6054 - 3.3471 1.00 2663 150 0.2050 0.2478 REMARK 3 6 3.3471 - 3.1498 1.00 2649 134 0.2234 0.2728 REMARK 3 7 3.1498 - 2.9921 0.99 2694 136 0.2325 0.2733 REMARK 3 8 2.9921 - 2.8618 1.00 2669 146 0.2485 0.3115 REMARK 3 9 2.8618 - 2.7517 1.00 2638 136 0.2668 0.3510 REMARK 3 10 2.7517 - 2.6567 1.00 2660 148 0.2817 0.3187 REMARK 3 11 2.6567 - 2.5737 1.00 2660 130 0.3080 0.3545 REMARK 3 12 2.5737 - 2.5001 0.99 2660 145 0.3570 0.3937 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL 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) : 0.380 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.730 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 50.93 REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.002 5310 REMARK 3 ANGLE : 0.506 7147 REMARK 3 CHIRALITY : 0.038 801 REMARK 3 PLANARITY : 0.003 856 REMARK 3 DIHEDRAL : 13.816 3146 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 4 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 31 THROUGH 162 ) REMARK 3 ORIGIN FOR THE GROUP (A): 56.5263-116.8187 248.7511 REMARK 3 T TENSOR REMARK 3 T11: 0.3642 T22: 0.3282 REMARK 3 T33: 0.4235 T12: -0.0345 REMARK 3 T13: -0.0283 T23: 0.0841 REMARK 3 L TENSOR REMARK 3 L11: 3.6676 L22: 5.9585 REMARK 3 L33: 4.3386 L12: 0.4077 REMARK 3 L13: -0.2575 L23: 0.4031 REMARK 3 S TENSOR REMARK 3 S11: 0.0559 S12: 0.3170 S13: 0.3081 REMARK 3 S21: -0.0037 S22: 0.1429 S23: 0.0920 REMARK 3 S31: -0.4497 S32: 0.4464 S33: -0.1965 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 163 THROUGH 211 ) REMARK 3 ORIGIN FOR THE GROUP (A): 52.2381-126.6211 212.3274 REMARK 3 T TENSOR REMARK 3 T11: 1.5131 T22: 1.0779 REMARK 3 T33: 0.6428 T12: 0.1376 REMARK 3 T13: 0.0137 T23: 0.1680 REMARK 3 L TENSOR REMARK 3 L11: 0.3120 L22: 0.0107 REMARK 3 L33: 4.2341 L12: -0.3164 REMARK 3 L13: -1.3435 L23: 0.8801 REMARK 3 S TENSOR REMARK 3 S11: -0.2549 S12: 0.5358 S13: -0.1250 REMARK 3 S21: -0.3632 S22: -0.3832 S23: 0.2084 REMARK 3 S31: 1.8862 S32: -0.8520 S33: -0.3294 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 212 THROUGH 480 ) REMARK 3 ORIGIN FOR THE GROUP (A): 46.5901-111.2984 170.6847 REMARK 3 T TENSOR REMARK 3 T11: 0.5759 T22: 0.5160 REMARK 3 T33: 0.3659 T12: 0.0528 REMARK 3 T13: 0.0342 T23: -0.0056 REMARK 3 L TENSOR REMARK 3 L11: 1.2328 L22: 0.8306 REMARK 3 L33: 3.8228 L12: -0.0736 REMARK 3 L13: 0.5005 L23: -0.6154 REMARK 3 S TENSOR REMARK 3 S11: -0.0276 S12: -0.3740 S13: -0.0386 REMARK 3 S21: 0.3459 S22: -0.0916 S23: -0.0194 REMARK 3 S31: 0.3351 S32: 0.5727 S33: 0.1002 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 2 THROUGH 34 ) REMARK 3 ORIGIN FOR THE GROUP (A): 56.2808-122.4542 225.5416 REMARK 3 T TENSOR REMARK 3 T11: 1.0358 T22: 1.2162 REMARK 3 T33: 0.4526 T12: 0.0746 REMARK 3 T13: -0.0156 T23: 0.0124 REMARK 3 L TENSOR REMARK 3 L11: 0.5240 L22: 0.4626 REMARK 3 L33: 2.1384 L12: -0.4268 REMARK 3 L13: 1.0669 L23: -0.9001 REMARK 3 S TENSOR REMARK 3 S11: 0.2755 S12: 1.2053 S13: -0.0911 REMARK 3 S21: -0.7917 S22: 0.0193 S23: -0.2271 REMARK 3 S31: 0.8530 S32: 0.2489 S33: -0.3575 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 6FJ3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-JAN-18. REMARK 100 THE DEPOSITION ID IS D_1200008418. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 04-SEP-17 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SLS REMARK 200 BEAMLINE : X06SA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.000 REMARK 200 MONOCHROMATOR : LN2 COOLED FIXED EXIT SI(111) REMARK 200 MONOCHROMATOR REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33759 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500 REMARK 200 RESOLUTION RANGE LOW (A) : 49.390 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 200 DATA REDUNDANCY : 5.300 REMARK 200 R MERGE (I) : 0.15300 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.60 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3 REMARK 200 DATA REDUNDANCY IN SHELL : 4.70 REMARK 200 R MERGE FOR SHELL (I) : 1.66200 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.900 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 5EE7, 3C4M REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 64.53 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.47 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CITRATE PH 6.0, 0.3 M REMARK 280 SODIUM ACETATE, 31% PEG400, 20 UM E-PTH(1-34), LIPIDIC CUBIC REMARK 280 PHASE, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 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: 11370 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 33160 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 27.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY A 22 REMARK 465 PRO A 23 REMARK 465 ALA A 24 REMARK 465 LEU A 25 REMARK 465 VAL A 26 REMARK 465 ASP A 27 REMARK 465 ALA A 28 REMARK 465 ASP A 29 REMARK 465 ASP A 30 REMARK 465 GLY A 247 REMARK 465 ALA A 248 REMARK 465 THR A 249 REMARK 465 LEU A 250 REMARK 465 ASP A 251 REMARK 465 GLU A 252 REMARK 465 ALA A 253 REMARK 465 GLU A 254 REMARK 465 ARG A 255 REMARK 465 LEU A 256 REMARK 465 THR A 257 REMARK 465 GLU A 258 REMARK 465 GLU A 259 REMARK 465 GLU A 260 REMARK 465 LEU A 261 REMARK 465 ARG A 262 REMARK 465 ALA A 263 REMARK 465 ILE A 264 REMARK 465 ALA A 265 REMARK 465 GLN A 266 REMARK 465 ALA A 267 REMARK 465 PRO A 268 REMARK 465 PRO A 269 REMARK 465 PRO A 270 REMARK 465 PRO A 271 REMARK 465 ALA A 272 REMARK 465 THR A 273 REMARK 465 ALA A 274 REMARK 465 ALA A 275 REMARK 465 ALA A 276 REMARK 465 GLY A 277 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 O4 NAG E 2 O5 BMA E 3 2.03 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 TYR B 34 C NH2 B 35 N -0.272 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 HIS A 114 -10.43 84.28 REMARK 500 ILE A 115 -50.16 -126.47 REMARK 500 PHE A 173 31.47 -87.67 REMARK 500 GLU A 177 -129.27 58.44 REMARK 500 ALA A 347 -156.08 -163.88 REMARK 500 THR A 349 -165.20 -79.98 REMARK 500 ASP A 353 56.25 -96.00 REMARK 500 GLN A1262 -77.60 -133.92 REMARK 500 PRO A1335 49.50 -92.41 REMARK 500 CYS A 460 -60.76 -140.75 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A1740 DISTANCE = 5.81 ANGSTROMS REMARK 525 HOH A1741 DISTANCE = 5.93 ANGSTROMS REMARK 525 HOH A1742 DISTANCE = 5.99 ANGSTROMS REMARK 525 HOH A1743 DISTANCE = 6.09 ANGSTROMS REMARK 525 HOH A1744 DISTANCE = 6.89 ANGSTROMS REMARK 525 HOH A1745 DISTANCE = 8.22 ANGSTROMS REMARK 525 HOH A1746 DISTANCE = 9.14 ANGSTROMS REMARK 525 HOH A1747 DISTANCE = 9.21 ANGSTROMS REMARK 525 HOH A1748 DISTANCE = 10.28 ANGSTROMS REMARK 525 HOH B 108 DISTANCE = 6.85 ANGSTROMS REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 MAN A 1511 REMARK 610 MAN A 1516 REMARK 610 MAN A 1517 REMARK 610 OLA A 1518 REMARK 610 OLA A 1519 REMARK 610 OLA A 1520 REMARK 610 OLA A 1523 REMARK 610 OLA A 1524 DBREF 6FJ3 A 24 60 UNP Q03431 PTH1R_HUMAN 24 60 DBREF 6FJ3 A 105 388 UNP Q03431 PTH1R_HUMAN 105 388 DBREF 6FJ3 A 1218 1413 UNP Q9V2J8 Q9V2J8_PYRAB 218 413 DBREF 6FJ3 A 398 480 UNP Q03431 PTH1R_HUMAN 398 480 DBREF 6FJ3 B 1 34 UNP Q27IM2 PTHY_HORSE 32 65 SEQADV 6FJ3 GLY A 22 UNP Q03431 EXPRESSION TAG SEQADV 6FJ3 PRO A 23 UNP Q03431 EXPRESSION TAG SEQADV 6FJ3 CYS A 191 UNP Q03431 TYR 191 ENGINEERED MUTATION SEQADV 6FJ3 MET A 240 UNP Q03431 LYS 240 ENGINEERED MUTATION SEQADV 6FJ3 ALA A 300 UNP Q03431 LEU 300 ENGINEERED MUTATION SEQADV 6FJ3 LYS A 312 UNP Q03431 MET 312 ENGINEERED MUTATION SEQADV 6FJ3 ILE A 334 UNP Q03431 VAL 334 ENGINEERED MUTATION SEQADV 6FJ3 ASN A 359 UNP Q03431 LYS 359 ENGINEERED MUTATION SEQADV 6FJ3 ALA A 407 UNP Q03431 LEU 407 ENGINEERED MUTATION SEQADV 6FJ3 LEU A 426 UNP Q03431 ALA 426 ENGINEERED MUTATION SEQADV 6FJ3 ARG A 440 UNP Q03431 GLN 440 ENGINEERED MUTATION SEQADV 6FJ3 ALA A 458 UNP Q03431 ILE 458 ENGINEERED MUTATION SEQADV 6FJ3 AC5 B 1 UNP Q27IM2 SER 32 CONFLICT SEQADV 6FJ3 AIB B 3 UNP Q27IM2 SER 34 CONFLICT SEQADV 6FJ3 GLN B 10 UNP Q27IM2 ASN 41 ENGINEERED MUTATION SEQADV 6FJ3 HRG B 11 UNP Q27IM2 LEU 42 CONFLICT SEQADV 6FJ3 ALA B 12 UNP Q27IM2 GLY 43 ENGINEERED MUTATION SEQADV 6FJ3 TRP B 14 UNP Q27IM2 HIS 45 ENGINEERED MUTATION SEQADV 6FJ3 NLE B 18 UNP Q27IM2 VAL 49 CONFLICT SEQADV 6FJ3 TYR B 34 UNP Q27IM2 PHE 65 ENGINEERED MUTATION SEQADV 6FJ3 NH2 B 35 UNP Q27IM2 AMIDATION SEQRES 1 A 602 GLY PRO ALA LEU VAL ASP ALA ASP ASP VAL MET THR LYS SEQRES 2 A 602 GLU GLU GLN ILE PHE LEU LEU HIS ARG ALA GLN ALA GLN SEQRES 3 A 602 CYS GLU LYS ARG LEU LYS GLU VAL LEU GLN ARG PRO ALA SEQRES 4 A 602 GLY ARG PRO CYS LEU PRO GLU TRP ASP HIS ILE LEU CYS SEQRES 5 A 602 TRP PRO LEU GLY ALA PRO GLY GLU VAL VAL ALA VAL PRO SEQRES 6 A 602 CYS PRO ASP TYR ILE TYR ASP PHE ASN HIS LYS GLY HIS SEQRES 7 A 602 ALA TYR ARG ARG CYS ASP ARG ASN GLY SER TRP GLU LEU SEQRES 8 A 602 VAL PRO GLY HIS ASN ARG THR TRP ALA ASN TYR SER GLU SEQRES 9 A 602 CYS VAL LYS PHE LEU THR ASN GLU THR ARG GLU ARG GLU SEQRES 10 A 602 VAL PHE ASP ARG LEU GLY MET ILE CYS THR VAL GLY TYR SEQRES 11 A 602 SER VAL SER LEU ALA SER LEU THR VAL ALA VAL LEU ILE SEQRES 12 A 602 LEU ALA TYR PHE ARG ARG LEU HIS CYS THR ARG ASN TYR SEQRES 13 A 602 ILE HIS MET HIS LEU PHE LEU SER PHE MET LEU ARG ALA SEQRES 14 A 602 VAL SER ILE PHE VAL MET ASP ALA VAL LEU TYR SER GLY SEQRES 15 A 602 ALA THR LEU ASP GLU ALA GLU ARG LEU THR GLU GLU GLU SEQRES 16 A 602 LEU ARG ALA ILE ALA GLN ALA PRO PRO PRO PRO ALA THR SEQRES 17 A 602 ALA ALA ALA GLY TYR ALA GLY CYS ARG VAL ALA VAL THR SEQRES 18 A 602 PHE PHE LEU TYR PHE LEU ALA THR ASN TYR TYR TRP ILE SEQRES 19 A 602 ALA VAL GLU GLY LEU TYR LEU HIS SER LEU ILE PHE LYS SEQRES 20 A 602 ALA PHE PHE SER GLU LYS LYS TYR LEU TRP GLY PHE THR SEQRES 21 A 602 VAL PHE GLY TRP GLY LEU PRO ALA ILE PHE VAL ALA VAL SEQRES 22 A 602 TRP VAL SER VAL ARG ALA THR LEU ALA ASN THR GLY CYS SEQRES 23 A 602 TRP ASP LEU SER SER GLY ASN ASN LYS TRP ILE ILE GLN SEQRES 24 A 602 VAL PRO ILE LEU ALA SER ILE VAL LEU ASN PHE ILE LEU SEQRES 25 A 602 PHE ILE ASN ILE VAL ARG VAL LEU ALA THR LYS GLY ILE SEQRES 26 A 602 ASP YCM SER PHE TRP ASN GLU SER TYR LEU THR GLY SER SEQRES 27 A 602 ARG ASP GLU ARG LYS LYS SER LEU LEU SER LYS PHE GLY SEQRES 28 A 602 MET ASP GLU GLY VAL THR PHE MET PHE ILE GLY ARG PHE SEQRES 29 A 602 ASP ARG GLY GLN LYS GLY VAL ASP VAL LEU LEU LYS ALA SEQRES 30 A 602 ILE GLU ILE LEU SER SER LYS LYS GLU PHE GLN GLU MET SEQRES 31 A 602 ARG PHE ILE ILE ILE GLY LYS GLY ASP PRO GLU LEU GLU SEQRES 32 A 602 GLY TRP ALA ARG SER LEU GLU GLU LYS HIS GLY ASN VAL SEQRES 33 A 602 LYS VAL ILE THR GLU MET LEU SER ARG GLU PHE VAL ARG SEQRES 34 A 602 GLU LEU TYR GLY SER VAL ASP PHE VAL ILE ILE PRO SER SEQRES 35 A 602 TYR PHE GLU PRO PHE GLY LEU VAL ALA LEU GLU ALA MET SEQRES 36 A 602 CYS LEU GLY ALA ILE PRO ILE ALA SER ALA VAL GLY GLY SEQRES 37 A 602 LEU ARG ASP ILE ILE THR ASN GLU THR GLY ILE LEU VAL SEQRES 38 A 602 LYS ALA GLY ASP PRO GLY GLU LEU ALA ASN ALA ILE LEU SEQRES 39 A 602 LYS ALA LEU GLU LEU SER ARG SER ASP LEU SER LYS PHE SEQRES 40 A 602 ARG GLU ASN CYS LYS LYS ARG ALA MET SER PHE SER ASP SEQRES 41 A 602 THR ARG GLN GLN TYR ARG LYS LEU ALA LYS SER THR LEU SEQRES 42 A 602 VAL LEU MET PRO LEU PHE GLY VAL HIS TYR ILE VAL PHE SEQRES 43 A 602 MET LEU THR PRO TYR THR GLU VAL SER GLY THR LEU TRP SEQRES 44 A 602 GLN VAL ARG MET HIS TYR GLU MET LEU PHE ASN SER PHE SEQRES 45 A 602 GLN GLY PHE PHE VAL ALA ILE ALA TYR CYS PHE CYS ASN SEQRES 46 A 602 GLY GLU VAL GLN ALA GLU ILE LYS LYS SER TRP SER ARG SEQRES 47 A 602 TRP THR LEU ALA SEQRES 1 B 35 AC5 VAL AIB GLU ILE GLN LEU MET HIS GLN HRG ALA LYS SEQRES 2 B 35 TRP LEU ASN SER NLE GLU ARG VAL GLU TRP LEU ARG LYS SEQRES 3 B 35 LYS LEU GLN ASP VAL HIS ASN TYR NH2 MODRES 6FJ3 YCM A 1221 CYS MODIFIED RESIDUE HET YCM A1221 10 HET AC5 B 1 8 HET AIB B 3 6 HET HRG B 11 12 HET NLE B 18 8 HET NH2 B 35 1 HET NAG C 1 14 HET NAG C 2 14 HET BMA C 3 11 HET MAN C 4 11 HET MAN C 5 11 HET FUC C 6 10 HET NAG D 1 14 HET NAG D 2 14 HET BMA D 3 11 HET FUC D 4 10 HET NAG E 1 14 HET NAG E 2 14 HET BMA E 3 11 HET MAN E 4 11 HET MAN A1511 11 HET MAN A1516 11 HET MAN A1517 11 HET OLA A1518 9 HET OLA A1519 11 HET OLA A1520 7 HET OLA A1521 20 HET OLA A1522 20 HET OLA A1523 7 HET OLA A1524 13 HET OLA A1525 20 HET OLA A1526 20 HET ACY A1527 4 HET PG4 A1528 13 HET CL A1529 1 HETNAM YCM S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE HETNAM AC5 1-AMINOCYCLOPENTANECARBOXYLIC ACID HETNAM AIB ALPHA-AMINOISOBUTYRIC ACID HETNAM HRG L-HOMOARGININE HETNAM NLE NORLEUCINE HETNAM NH2 AMINO GROUP HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETNAM FUC ALPHA-L-FUCOPYRANOSE HETNAM OLA OLEIC ACID HETNAM ACY ACETIC ACID HETNAM PG4 TETRAETHYLENE GLYCOL HETNAM CL CHLORIDE ION HETSYN YCM CYSTEINE-S-ACETAMIDE HETSYN AC5 CYCLO-LEUCINE FORMUL 1 YCM C5 H10 N2 O3 S FORMUL 2 AC5 C6 H11 N O2 FORMUL 2 AIB C4 H9 N O2 FORMUL 2 HRG C7 H16 N4 O2 FORMUL 2 NLE C6 H13 N O2 FORMUL 2 NH2 H2 N FORMUL 3 NAG 6(C8 H15 N O6) FORMUL 3 BMA 3(C6 H12 O6) FORMUL 3 MAN 6(C6 H12 O6) FORMUL 3 FUC 2(C6 H12 O5) FORMUL 9 OLA 9(C18 H34 O2) FORMUL 18 ACY C2 H4 O2 FORMUL 19 PG4 C8 H18 O5 FORMUL 20 CL CL 1- FORMUL 21 HOH *156(H2 O) HELIX 1 AA1 THR A 33 GLN A 57 1 25 HELIX 2 AA2 ARG A 179 PHE A 212 1 34 HELIX 3 AA3 ARG A 213 HIS A 216 5 4 HELIX 4 AA4 CYS A 217 SER A 246 1 30 HELIX 5 AA5 ALA A 279 LYS A 312 1 34 HELIX 6 AA6 SER A 316 ALA A 347 1 32 HELIX 7 AA7 GLY A 357 ASN A 359 5 3 HELIX 8 AA8 LYS A 360 ARG A 383 1 24 HELIX 9 AA9 ASN A 1225 LEU A 1229 5 5 HELIX 10 AB1 SER A 1232 PHE A 1244 1 13 HELIX 11 AB2 GLY A 1264 SER A 1277 1 14 HELIX 12 AB3 LYS A 1278 GLN A 1282 5 5 HELIX 13 AB4 ASP A 1293 HIS A 1307 1 15 HELIX 14 AB5 SER A 1318 GLY A 1327 1 10 HELIX 15 AB6 GLY A 1342 LEU A 1351 1 10 HELIX 16 AB7 VAL A 1360 ILE A 1367 1 8 HELIX 17 AB8 ASP A 1379 ARG A 1395 1 17 HELIX 18 AB9 LEU A 1398 THR A 427 1 46 HELIX 19 AC1 GLY A 434 PHE A 450 1 17 HELIX 20 AC2 PHE A 450 CYS A 460 1 11 HELIX 21 AC3 ASN A 463 THR A 478 1 16 HELIX 22 AC4 VAL B 2 TYR B 34 1 33 SHEET 1 AA1 2 VAL A 126 PRO A 130 0 SHEET 2 AA1 2 HIS A 143 ARG A 147 -1 O ALA A 144 N VAL A 129 SHEET 1 AA2 6 VAL A1310 ILE A1313 0 SHEET 2 AA2 6 MET A1284 ILE A1289 1 N ILE A1288 O LYS A1311 SHEET 3 AA2 6 VAL A1250 ILE A1255 1 N PHE A1252 O ARG A1285 SHEET 4 AA2 6 PHE A1331 ILE A1334 1 O ILE A1333 N MET A1253 SHEET 5 AA2 6 ILE A1354 SER A1358 1 O ILE A1356 N VAL A1332 SHEET 6 AA2 6 ILE A1373 VAL A1375 1 O ILE A1373 N ALA A1357 SSBOND 1 CYS A 48 CYS A 117 1555 1555 2.03 SSBOND 2 CYS A 108 CYS A 148 1555 1555 2.03 SSBOND 3 CYS A 131 CYS A 170 1555 1555 2.03 SSBOND 4 CYS A 281 CYS A 351 1555 1555 2.03 LINK ND2 ASN A 151 C1 NAG E 1 1555 1555 1.43 LINK ND2 ASN A 161 C1 NAG C 1 1555 1555 1.46 LINK ND2 ASN A 166 C1 NAG D 1 1555 1555 1.46 LINK C ASP A1220 N YCM A1221 1555 1555 1.33 LINK C YCM A1221 N SER A1222 1555 1555 1.33 LINK C AC5 B 1 N VAL B 2 1555 1555 1.28 LINK C VAL B 2 N AIB B 3 1555 1555 1.33 LINK C AIB B 3 N GLU B 4 1555 1555 1.33 LINK C GLN B 10 N HRG B 11 1555 1555 1.33 LINK C HRG B 11 N ALA B 12 1555 1555 1.33 LINK C SER B 17 N NLE B 18 1555 1555 1.33 LINK C NLE B 18 N GLU B 19 1555 1555 1.33 LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.41 LINK O6 NAG C 1 C1 FUC C 6 1555 1555 1.41 LINK O4 NAG C 2 C1 BMA C 3 1555 1555 1.41 LINK O3 BMA C 3 C1 MAN C 4 1555 1555 1.48 LINK O6 BMA C 3 C1 MAN C 5 1555 1555 1.44 LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.44 LINK O6 NAG D 1 C1 FUC D 4 1555 1555 1.47 LINK O4 NAG D 2 C1 BMA D 3 1555 1555 1.43 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.47 LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.45 LINK O6 BMA E 3 C1 MAN E 4 1555 1555 1.46 CRYST1 44.115 52.864 111.874 80.63 83.76 79.16 P 1 1 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 0.022668 -0.004342 -0.001865 0.00000 SCALE2 0.000000 0.019260 -0.002840 0.00000 SCALE3 0.000000 0.000000 0.009089 0.00000 ATOM 1 N VAL A 31 56.821-112.776 222.620 1.00129.10 N ANISOU 1 N VAL A 31 20977 18132 9943 -1526 -394 3300 N ATOM 2 CA VAL A 31 57.663-111.648 222.997 1.00126.46 C ANISOU 2 CA VAL A 31 20613 17625 9813 -1682 -2 3535 C ATOM 3 C VAL A 31 58.431-111.976 224.274 1.00111.63 C ANISOU 3 C VAL A 31 18348 15721 8345 -1794 292 3321 C ATOM 4 O VAL A 31 59.596-111.607 224.422 1.00109.38 O ANISOU 4 O VAL A 31 17978 15463 8118 -1998 780 3312 O ATOM 5 CB VAL A 31 56.829-110.366 223.172 1.00126.63 C ANISOU 5 CB VAL A 31 20712 17314 10090 -1562 -304 3935 C ATOM 6 CG1 VAL A 31 57.739-109.160 223.357 1.00126.96 C ANISOU 6 CG1 VAL A 31 20793 17166 10280 -1750 114 4174 C ATOM 7 CG2 VAL A 31 55.904-110.169 221.982 1.00128.57 C ANISOU 7 CG2 VAL A 31 21286 17608 9956 -1411 -687 4129 C ATOM 8 N MET A 32 57.770-112.676 225.193 1.00100.19 N ANISOU 8 N MET A 32 16641 14231 7194 -1665 -15 3151 N ATOM 9 CA MET A 32 58.378-113.084 226.455 1.00 92.72 C ANISOU 9 CA MET A 32 15324 13283 6622 -1751 198 2950 C ATOM 10 C MET A 32 59.074-114.425 226.250 1.00 86.29 C ANISOU 10 C MET A 32 14419 12798 5567 -1806 450 2545 C ATOM 11 O MET A 32 58.420-115.438 225.985 1.00 79.50 O ANISOU 11 O MET A 32 13578 12046 4582 -1653 163 2319 O ATOM 12 CB MET A 32 57.325-113.173 227.557 1.00 92.22 C ANISOU 12 CB MET A 32 15018 13009 7012 -1570 -235 2973 C ATOM 13 CG MET A 32 57.856-113.672 228.894 1.00 93.07 C ANISOU 13 CG MET A 32 14611 13081 7671 -1524 -46 2663 C ATOM 14 SD MET A 32 59.015-112.529 229.670 1.00 96.22 S ANISOU 14 SD MET A 32 14860 13323 8375 -1752 391 2795 S ATOM 15 CE MET A 32 57.968-111.095 229.909 1.00 97.86 C ANISOU 15 CE MET A 32 15289 13125 8770 -1689 65 3247 C ATOM 16 N THR A 33 60.397-114.430 226.373 1.00 84.98 N ANISOU 16 N THR A 33 14092 12768 5430 -1983 989 2409 N ATOM 17 CA THR A 33 61.179-115.643 226.199 1.00 92.12 C ANISOU 17 CA THR A 33 14810 13945 6247 -1956 1290 1976 C ATOM 18 C THR A 33 61.344-116.376 227.527 1.00 92.62 C ANISOU 18 C THR A 33 14322 13941 6928 -1786 1247 1667 C ATOM 19 O THR A 33 61.112-115.826 228.607 1.00 86.86 O ANISOU 19 O THR A 33 13346 12985 6670 -1750 1099 1785 O ATOM 20 CB THR A 33 62.554-115.324 225.609 1.00 95.05 C ANISOU 20 CB THR A 33 15204 14499 6411 -2181 1904 1956 C ATOM 21 OG1 THR A 33 63.198-114.323 226.407 1.00 95.85 O ANISOU 21 OG1 THR A 33 15055 14446 6917 -2347 2120 2137 O ATOM 22 CG2 THR A 33 62.419-114.820 224.180 1.00 95.25 C ANISOU 22 CG2 THR A 33 15675 14550 5965 -2197 1923 2158 C ATOM 23 N LYS A 34 61.747-117.645 227.429 1.00 94.41 N ANISOU 23 N LYS A 34 14392 14353 7126 -1672 1379 1265 N ATOM 24 CA LYS A 34 62.043-118.424 228.626 1.00 87.93 C ANISOU 24 CA LYS A 34 13081 13479 6847 -1506 1373 976 C ATOM 25 C LYS A 34 63.224-117.833 229.384 1.00 90.55 C ANISOU 25 C LYS A 34 13056 13822 7528 -1637 1737 996 C ATOM 26 O LYS A 34 63.245-117.839 230.621 1.00 90.24 O ANISOU 26 O LYS A 34 12666 13638 7983 -1550 1612 951 O ATOM 27 CB LYS A 34 62.311-119.880 228.242 1.00 87.22 C ANISOU 27 CB LYS A 34 12946 13562 6631 -1355 1473 553 C ATOM 28 CG LYS A 34 62.972-120.718 229.324 1.00 85.64 C ANISOU 28 CG LYS A 34 12260 13344 6935 -1192 1585 252 C ATOM 29 CD LYS A 34 63.101-122.168 228.883 1.00 89.08 C ANISOU 29 CD LYS A 34 12715 13886 7246 -1015 1647 -154 C ATOM 30 CE LYS A 34 64.093-122.927 229.748 1.00 90.33 C ANISOU 30 CE LYS A 34 12410 14068 7845 -857 1872 -436 C ATOM 31 NZ LYS A 34 65.481-122.419 229.568 1.00 94.87 N ANISOU 31 NZ LYS A 34 12768 14851 8426 -992 2381 -444 N ATOM 32 N GLU A 35 64.212-117.305 228.657 1.00 92.11 N ANISOU 32 N GLU A 35 13342 14194 7463 -1865 2189 1065 N ATOM 33 CA GLU A 35 65.358-116.676 229.305 1.00 93.65 C ANISOU 33 CA GLU A 35 13176 14411 7996 -2040 2533 1089 C ATOM 34 C GLU A 35 64.941-115.435 230.085 1.00 88.09 C ANISOU 34 C GLU A 35 12477 13421 7572 -2156 2319 1417 C ATOM 35 O GLU A 35 65.478-115.161 231.166 1.00 79.52 O ANISOU 35 O GLU A 35 11014 12257 6942 -2194 2356 1364 O ATOM 36 CB GLU A 35 66.418-116.323 228.261 1.00105.16 C ANISOU 36 CB GLU A 35 14751 16111 9093 -2298 3089 1118 C ATOM 37 CG GLU A 35 67.563-115.479 228.795 1.00114.63 C ANISOU 37 CG GLU A 35 15602 17328 10624 -2558 3448 1194 C ATOM 38 CD GLU A 35 68.520-115.041 227.704 1.00130.24 C ANISOU 38 CD GLU A 35 17689 19463 12334 -2765 3949 1256 C ATOM 39 OE1 GLU A 35 68.572-115.712 226.652 1.00136.55 O ANISOU 39 OE1 GLU A 35 18713 20435 12736 -2660 4105 1116 O ATOM 40 OE2 GLU A 35 69.217-114.022 227.898 1.00135.83 O ANISOU 40 OE2 GLU A 35 18248 20069 13290 -2981 4134 1433 O ATOM 41 N GLU A 36 63.983-114.672 229.554 1.00 91.64 N ANISOU 41 N GLU A 36 13362 13702 7755 -2202 2080 1749 N ATOM 42 CA GLU A 36 63.528-113.470 230.246 1.00 91.71 C ANISOU 42 CA GLU A 36 13414 13397 8034 -2282 1886 2056 C ATOM 43 C GLU A 36 62.820-113.816 231.551 1.00 82.07 C ANISOU 43 C GLU A 36 11912 11984 7289 -2044 1510 1936 C ATOM 44 O GLU A 36 62.992-113.122 232.560 1.00 77.04 O ANISOU 44 O GLU A 36 11086 11153 7033 -2109 1492 1999 O ATOM 45 CB GLU A 36 62.613-112.656 229.332 1.00 99.60 C ANISOU 45 CB GLU A 36 14947 14250 8645 -2327 1684 2443 C ATOM 46 CG GLU A 36 63.147-111.275 228.989 1.00112.24 C ANISOU 46 CG GLU A 36 16760 15705 10180 -2613 1948 2777 C ATOM 47 CD GLU A 36 62.348-110.598 227.892 1.00123.03 C ANISOU 47 CD GLU A 36 18600 16929 11218 -2522 1734 3088 C ATOM 48 OE1 GLU A 36 61.675-111.312 227.119 1.00124.72 O ANISOU 48 OE1 GLU A 36 19037 17288 11064 -2362 1512 3040 O ATOM 49 OE2 GLU A 36 62.392-109.353 227.803 1.00127.77 O ANISOU 49 OE2 GLU A 36 19341 17269 11935 -2606 1775 3371 O ATOM 50 N GLN A 37 62.020-114.886 231.552 1.00 76.81 N ANISOU 50 N GLN A 37 11231 11359 6593 -1786 1221 1754 N ATOM 51 CA GLN A 37 61.365-115.316 232.783 1.00 75.87 C ANISOU 51 CA GLN A 37 10849 11073 6907 -1573 915 1632 C ATOM 52 C GLN A 37 62.374-115.808 233.811 1.00 74.10 C ANISOU 52 C GLN A 37 10190 10922 7041 -1560 1101 1365 C ATOM 53 O GLN A 37 62.171-115.620 235.016 1.00 65.17 O ANISOU 53 O GLN A 37 8859 9615 6287 -1496 950 1352 O ATOM 54 CB GLN A 37 60.341-116.410 232.482 1.00 76.99 C ANISOU 54 CB GLN A 37 11069 11247 6938 -1344 597 1489 C ATOM 55 CG GLN A 37 59.145-115.940 231.673 1.00 82.44 C ANISOU 55 CG GLN A 37 12126 11841 7355 -1314 281 1753 C ATOM 56 CD GLN A 37 58.243-115.005 232.453 1.00 79.59 C ANISOU 56 CD GLN A 37 11747 11176 7319 -1251 15 2004 C ATOM 57 OE1 GLN A 37 57.382-115.448 233.213 1.00 61.87 O ANISOU 57 OE1 GLN A 37 9325 8809 5375 -1070 -253 1921 O ATOM 58 NE2 GLN A 37 58.434-113.703 232.266 1.00 88.94 N ANISOU 58 NE2 GLN A 37 13122 12220 8451 -1402 114 2311 N ATOM 59 N ILE A 38 63.460-116.439 233.358 1.00 78.54 N ANISOU 59 N ILE A 38 10606 11747 7488 -1608 1425 1148 N ATOM 60 CA ILE A 38 64.490-116.904 234.281 1.00 79.67 C ANISOU 60 CA ILE A 38 10306 11981 7985 -1577 1579 905 C ATOM 61 C ILE A 38 65.160-115.723 234.971 1.00 82.59 C ANISOU 61 C ILE A 38 10517 12257 8604 -1812 1704 1050 C ATOM 62 O ILE A 38 65.418-115.755 236.181 1.00 83.40 O ANISOU 62 O ILE A 38 10330 12282 9077 -1765 1593 951 O ATOM 63 CB ILE A 38 65.512-117.786 233.538 1.00 80.22 C ANISOU 63 CB ILE A 38 10237 12353 7890 -1558 1926 643 C ATOM 64 CG1 ILE A 38 64.849-119.080 233.062 1.00 77.95 C ANISOU 64 CG1 ILE A 38 10090 12109 7420 -1305 1766 434 C ATOM 65 CG2 ILE A 38 66.708-118.092 234.426 1.00 78.88 C ANISOU 65 CG2 ILE A 38 9568 12293 8110 -1539 2093 431 C ATOM 66 CD1 ILE A 38 65.765-119.978 232.261 1.00 80.15 C ANISOU 66 CD1 ILE A 38 10287 12653 7512 -1254 2120 149 C ATOM 67 N PHE A 39 65.443-114.658 234.217 1.00 84.98 N ANISOU 67 N PHE A 39 11040 12553 8696 -2085 1927 1287 N ATOM 68 CA PHE A 39 66.059-113.474 234.809 1.00 85.76 C ANISOU 68 CA PHE A 39 11027 12524 9035 -2355 2051 1426 C ATOM 69 C PHE A 39 65.120-112.801 235.803 1.00 84.44 C ANISOU 69 C PHE A 39 10959 12013 9112 -2290 1704 1572 C ATOM 70 O PHE A 39 65.552-112.370 236.879 1.00 84.04 O ANISOU 70 O PHE A 39 10677 11856 9396 -2376 1675 1512 O ATOM 71 CB PHE A 39 66.474-112.495 233.711 1.00 89.46 C ANISOU 71 CB PHE A 39 11774 13017 9200 -2673 2377 1681 C ATOM 72 CG PHE A 39 67.062-111.214 234.229 1.00 91.99 C ANISOU 72 CG PHE A 39 12030 13159 9765 -2995 2513 1840 C ATOM 73 CD1 PHE A 39 68.378-111.163 234.657 1.00 97.00 C ANISOU 73 CD1 PHE A 39 12232 13961 10664 -3205 2790 1663 C ATOM 74 CD2 PHE A 39 66.301-110.057 234.281 1.00 91.05 C ANISOU 74 CD2 PHE A 39 12272 12690 9634 -3089 2355 2158 C ATOM 75 CE1 PHE A 39 68.923-109.985 235.133 1.00 99.73 C ANISOU 75 CE1 PHE A 39 12517 14130 11245 -3541 2900 1787 C ATOM 76 CE2 PHE A 39 66.840-108.876 234.755 1.00 94.98 C ANISOU 76 CE2 PHE A 39 12744 12979 10365 -3402 2485 2286 C ATOM 77 CZ PHE A 39 68.153-108.840 235.181 1.00 98.92 C ANISOU 77 CZ PHE A 39 12819 13645 11122 -3633 2747 2088 C ATOM 78 N LEU A 40 63.833-112.702 235.462 1.00 81.60 N ANISOU 78 N LEU A 40 10933 11480 8591 -2134 1437 1749 N ATOM 79 CA LEU A 40 62.870-112.096 236.374 1.00 73.07 C ANISOU 79 CA LEU A 40 9932 10073 7758 -2035 1139 1872 C ATOM 80 C LEU A 40 62.677-112.939 237.628 1.00 70.09 C ANISOU 80 C LEU A 40 9256 9685 7690 -1818 945 1619 C ATOM 81 O LEU A 40 62.451-112.391 238.713 1.00 70.30 O ANISOU 81 O LEU A 40 9227 9491 7992 -1817 829 1631 O ATOM 82 CB LEU A 40 61.532-111.889 235.663 1.00 69.22 C ANISOU 82 CB LEU A 40 9807 9437 7055 -1889 888 2108 C ATOM 83 CG LEU A 40 61.537-110.903 234.493 1.00 73.53 C ANISOU 83 CG LEU A 40 10740 9922 7275 -2081 1011 2435 C ATOM 84 CD1 LEU A 40 60.216-110.955 233.744 1.00 68.71 C ANISOU 84 CD1 LEU A 40 10445 9231 6430 -1884 689 2633 C ATOM 85 CD2 LEU A 40 61.822-109.492 234.984 1.00 60.74 C ANISOU 85 CD2 LEU A 40 9207 8004 5866 -2299 1113 2642 C ATOM 86 N LEU A 41 62.761-114.265 237.502 1.00 70.44 N ANISOU 86 N LEU A 41 9140 9944 7678 -1635 916 1389 N ATOM 87 CA LEU A 41 62.612-115.125 238.670 1.00 65.30 C ANISOU 87 CA LEU A 41 8242 9270 7297 -1432 742 1175 C ATOM 88 C LEU A 41 63.835-115.055 239.575 1.00 74.37 C ANISOU 88 C LEU A 41 9066 10503 8689 -1540 869 1018 C ATOM 89 O LEU A 41 63.704-115.159 240.800 1.00 75.71 O ANISOU 89 O LEU A 41 9109 10557 9099 -1454 705 936 O ATOM 90 CB LEU A 41 62.352-116.566 238.230 1.00 55.36 C ANISOU 90 CB LEU A 41 6942 8173 5919 -1212 675 984 C ATOM 91 CG LEU A 41 61.845-117.523 239.309 1.00 51.33 C ANISOU 91 CG LEU A 41 6282 7576 5647 -979 454 824 C ATOM 92 CD1 LEU A 41 60.501-117.055 239.845 1.00 53.40 C ANISOU 92 CD1 LEU A 41 6699 7573 6019 -905 211 983 C ATOM 93 CD2 LEU A 41 61.747-118.941 238.771 1.00 43.76 C ANISOU 93 CD2 LEU A 41 5300 6753 4574 -799 428 622 C ATOM 94 N HIS A 42 65.025-114.882 238.995 1.00 79.74 N ANISOU 94 N HIS A 42 9602 11393 9303 -1734 1157 972 N ATOM 95 CA HIS A 42 66.227-114.719 239.807 1.00 79.29 C ANISOU 95 CA HIS A 42 9189 11433 9505 -1866 1253 830 C ATOM 96 C HIS A 42 66.174-113.430 240.617 1.00 73.98 C ANISOU 96 C HIS A 42 8587 10512 9008 -2079 1183 961 C ATOM 97 O HIS A 42 66.614-113.398 241.772 1.00 75.14 O ANISOU 97 O HIS A 42 8515 10633 9401 -2094 1064 831 O ATOM 98 CB HIS A 42 67.471-114.741 238.920 1.00 86.94 C ANISOU 98 CB HIS A 42 9959 12685 10389 -2052 1618 761 C ATOM 99 CG HIS A 42 67.909-116.117 238.525 1.00 94.27 C ANISOU 99 CG HIS A 42 10675 13872 11270 -1821 1706 521 C ATOM 100 ND1 HIS A 42 67.686-117.224 239.314 1.00 94.40 N ANISOU 100 ND1 HIS A 42 10541 13881 11447 -1516 1466 337 N ATOM 101 CD2 HIS A 42 68.558-116.564 237.424 1.00 99.54 C ANISOU 101 CD2 HIS A 42 11283 14791 11746 -1846 2029 429 C ATOM 102 CE1 HIS A 42 68.179-118.295 238.717 1.00 95.67 C ANISOU 102 CE1 HIS A 42 10553 14253 11544 -1350 1620 140 C ATOM 103 NE2 HIS A 42 68.713-117.921 237.568 1.00 99.50 N ANISOU 103 NE2 HIS A 42 11085 14909 11813 -1540 1970 175 N ATOM 104 N ARG A 43 65.643-112.357 240.027 1.00 70.80 N ANISOU 104 N ARG A 43 8516 9913 8474 -2240 1242 1215 N ATOM 105 CA ARG A 43 65.521-111.100 240.758 1.00 70.71 C ANISOU 105 CA ARG A 43 8623 9606 8636 -2429 1186 1332 C ATOM 106 C ARG A 43 64.533-111.227 241.910 1.00 67.71 C ANISOU 106 C ARG A 43 8315 9000 8411 -2200 888 1286 C ATOM 107 O ARG A 43 64.764-110.684 242.996 1.00 63.30 O ANISOU 107 O ARG A 43 7699 8295 8058 -2296 811 1211 O ATOM 108 CB ARG A 43 65.106-109.978 239.807 1.00 72.29 C ANISOU 108 CB ARG A 43 9201 9606 8661 -2608 1309 1640 C ATOM 109 CG ARG A 43 64.788-108.660 240.496 1.00 74.43 C ANISOU 109 CG ARG A 43 9670 9493 9117 -2761 1242 1774 C ATOM 110 CD ARG A 43 65.224-107.480 239.646 1.00 82.74 C ANISOU 110 CD ARG A 43 10952 10412 10072 -3100 1492 2023 C ATOM 111 NE ARG A 43 64.704-107.560 238.285 1.00 91.00 N ANISOU 111 NE ARG A 43 12291 11510 10775 -3033 1560 2263 N ATOM 112 CZ ARG A 43 65.055-106.737 237.303 1.00103.60 C ANISOU 112 CZ ARG A 43 14138 13043 12181 -3302 1802 2517 C ATOM 113 NH1 ARG A 43 65.932-105.768 237.530 1.00106.45 N ANISOU 113 NH1 ARG A 43 14438 13268 12739 -3591 1992 2519 N ATOM 114 NH2 ARG A 43 64.533-106.882 236.093 1.00108.01 N ANISOU 114 NH2 ARG A 43 14998 13666 12374 -3216 1820 2732 N ATOM 115 N ALA A 44 63.430-111.948 241.693 1.00 66.47 N ANISOU 115 N ALA A 44 8287 8817 8153 -1913 727 1317 N ATOM 116 CA ALA A 44 62.457-112.148 242.762 1.00 62.38 C ANISOU 116 CA ALA A 44 7815 8102 7785 -1698 494 1271 C ATOM 117 C ALA A 44 63.048-112.969 243.900 1.00 66.59 C ANISOU 117 C ALA A 44 8074 8762 8467 -1616 408 1023 C ATOM 118 O ALA A 44 62.736-112.729 245.073 1.00 66.80 O ANISOU 118 O ALA A 44 8128 8617 8635 -1576 284 967 O ATOM 119 CB ALA A 44 61.202-112.822 242.209 1.00 56.04 C ANISOU 119 CB ALA A 44 7152 7275 6866 -1440 351 1347 C ATOM 120 N GLN A 45 63.905-113.939 243.575 1.00 68.02 N ANISOU 120 N GLN A 45 8004 9233 8607 -1576 474 874 N ATOM 121 CA GLN A 45 64.529-114.751 244.614 1.00 65.96 C ANISOU 121 CA GLN A 45 7480 9091 8489 -1471 362 663 C ATOM 122 C GLN A 45 65.506-113.928 245.444 1.00 62.50 C ANISOU 122 C GLN A 45 6891 8646 8209 -1711 364 593 C ATOM 123 O GLN A 45 65.591-114.103 246.665 1.00 62.48 O ANISOU 123 O GLN A 45 6828 8596 8315 -1649 183 482 O ATOM 124 CB GLN A 45 65.232-115.955 243.986 1.00 69.18 C ANISOU 124 CB GLN A 45 7649 9789 8847 -1343 443 521 C ATOM 125 CG GLN A 45 65.818-116.933 244.992 1.00 74.48 C ANISOU 125 CG GLN A 45 8062 10566 9671 -1169 291 329 C ATOM 126 CD GLN A 45 66.346-118.194 244.337 1.00 77.58 C ANISOU 126 CD GLN A 45 8256 11184 10037 -979 371 187 C ATOM 127 OE1 GLN A 45 66.294-118.343 243.117 1.00 81.63 O ANISOU 127 OE1 GLN A 45 8833 11793 10390 -995 559 207 O ATOM 128 NE2 GLN A 45 66.856-119.113 245.149 1.00 78.33 N ANISOU 128 NE2 GLN A 45 8136 11351 10276 -787 225 40 N ATOM 129 N ALA A 46 66.247-113.023 244.801 1.00 60.89 N ANISOU 129 N ALA A 46 6644 8486 8006 -2006 564 658 N ATOM 130 CA ALA A 46 67.182-112.177 245.537 1.00 61.13 C ANISOU 130 CA ALA A 46 6521 8497 8208 -2289 560 581 C ATOM 131 C ALA A 46 66.447-111.213 246.460 1.00 66.79 C ANISOU 131 C ALA A 46 7529 8866 8981 -2355 426 633 C ATOM 132 O ALA A 46 66.909-110.938 247.574 1.00 72.65 O ANISOU 132 O ALA A 46 8187 9571 9847 -2454 282 492 O ATOM 133 CB ALA A 46 68.078-111.412 244.563 1.00 54.99 C ANISOU 133 CB ALA A 46 5647 7819 7430 -2625 848 656 C ATOM 134 N GLN A 47 65.303-110.687 246.015 1.00 66.22 N ANISOU 134 N GLN A 47 7804 8537 8819 -2290 462 824 N ATOM 135 CA GLN A 47 64.511-109.810 246.871 1.00 69.36 C ANISOU 135 CA GLN A 47 8481 8583 9290 -2298 367 860 C ATOM 136 C GLN A 47 63.971-110.557 248.083 1.00 66.38 C ANISOU 136 C GLN A 47 8101 8183 8937 -2047 163 715 C ATOM 137 O GLN A 47 63.843-109.974 249.166 1.00 69.30 O ANISOU 137 O GLN A 47 8599 8358 9375 -2107 80 628 O ATOM 138 CB GLN A 47 63.363-109.192 246.072 1.00 72.72 C ANISOU 138 CB GLN A 47 9232 8752 9645 -2221 435 1106 C ATOM 139 CG GLN A 47 63.813-108.297 244.928 1.00 90.44 C ANISOU 139 CG GLN A 47 11582 10953 11830 -2486 638 1299 C ATOM 140 CD GLN A 47 62.668-107.880 244.023 1.00 99.98 C ANISOU 140 CD GLN A 47 13106 11953 12929 -2351 647 1570 C ATOM 141 OE1 GLN A 47 61.522-108.283 244.224 1.00103.43 O ANISOU 141 OE1 GLN A 47 13632 12299 13369 -2057 499 1598 O ATOM 142 NE2 GLN A 47 62.975-107.069 243.017 1.00102.07 N ANISOU 142 NE2 GLN A 47 13536 12145 13103 -2571 816 1782 N ATOM 143 N CYS A 48 63.658-111.844 247.922 1.00 64.23 N ANISOU 143 N CYS A 48 7715 8095 8594 -1779 95 684 N ATOM 144 CA CYS A 48 63.135-112.625 249.037 1.00 66.60 C ANISOU 144 CA CYS A 48 8037 8366 8900 -1551 -72 577 C ATOM 145 C CYS A 48 64.219-112.909 250.068 1.00 72.29 C ANISOU 145 C CYS A 48 8562 9238 9666 -1625 -211 386 C ATOM 146 O CYS A 48 63.949-112.919 251.275 1.00 72.92 O ANISOU 146 O CYS A 48 8764 9208 9735 -1568 -344 301 O ATOM 147 CB CYS A 48 62.531-113.928 248.518 1.00 66.47 C ANISOU 147 CB CYS A 48 7966 8475 8815 -1276 -102 603 C ATOM 148 SG CYS A 48 61.497-114.812 249.702 1.00 64.77 S ANISOU 148 SG CYS A 48 7866 8140 8605 -1006 -243 550 S ATOM 149 N GLU A 49 65.451-113.146 249.612 1.00 78.56 N ANISOU 149 N GLU A 49 9048 10296 10505 -1746 -184 316 N ATOM 150 CA GLU A 49 66.547-113.404 250.541 1.00 82.32 C ANISOU 150 CA GLU A 49 9279 10942 11055 -1809 -362 140 C ATOM 151 C GLU A 49 66.854-112.176 251.388 1.00 84.75 C ANISOU 151 C GLU A 49 9703 11083 11416 -2096 -430 68 C ATOM 152 O GLU A 49 67.134-112.296 252.586 1.00 86.42 O ANISOU 152 O GLU A 49 9920 11303 11611 -2088 -655 -67 O ATOM 153 CB GLU A 49 67.788-113.856 249.771 1.00 89.49 C ANISOU 153 CB GLU A 49 9777 12172 12053 -1875 -284 77 C ATOM 154 CG GLU A 49 67.595-115.157 249.006 1.00 98.75 C ANISOU 154 CG GLU A 49 10843 13506 13171 -1580 -223 93 C ATOM 155 CD GLU A 49 68.755-115.472 248.083 1.00110.21 C ANISOU 155 CD GLU A 49 11914 15255 14707 -1648 -57 25 C ATOM 156 OE1 GLU A 49 69.658-114.619 247.946 1.00115.80 O ANISOU 156 OE1 GLU A 49 12429 16047 15523 -1953 40 -5 O ATOM 157 OE2 GLU A 49 68.763-116.572 247.492 1.00112.32 O ANISOU 157 OE2 GLU A 49 12074 15661 14941 -1404 -1 -10 O ATOM 158 N LYS A 50 66.801-110.985 250.786 1.00 84.41 N ANISOU 158 N LYS A 50 9787 10868 11417 -2356 -248 158 N ATOM 159 CA LYS A 50 67.023-109.764 251.554 1.00 81.25 C ANISOU 159 CA LYS A 50 9547 10246 11079 -2644 -297 76 C ATOM 160 C LYS A 50 65.894-109.525 252.548 1.00 75.48 C ANISOU 160 C LYS A 50 9200 9219 10258 -2490 -377 55 C ATOM 161 O LYS A 50 66.136-109.068 253.672 1.00 75.03 O ANISOU 161 O LYS A 50 9256 9063 10187 -2615 -525 -107 O ATOM 162 CB LYS A 50 67.172-108.568 250.613 1.00 80.87 C ANISOU 162 CB LYS A 50 9588 10030 11108 -2948 -59 207 C ATOM 163 CG LYS A 50 67.345-107.239 251.332 1.00 85.79 C ANISOU 163 CG LYS A 50 10423 10354 11818 -3265 -85 120 C ATOM 164 CD LYS A 50 67.550-106.091 250.358 1.00 90.45 C ANISOU 164 CD LYS A 50 11116 10751 12500 -3580 163 278 C ATOM 165 CE LYS A 50 67.740-104.776 251.097 1.00 96.22 C ANISOU 165 CE LYS A 50 12080 11137 13341 -3909 135 169 C ATOM 166 NZ LYS A 50 68.002-103.642 250.168 1.00102.27 N ANISOU 166 NZ LYS A 50 12969 11676 14213 -4246 383 340 N ATOM 167 N ARG A 51 64.655-109.832 252.156 1.00 69.07 N ANISOU 167 N ARG A 51 8586 8272 9384 -2225 -277 202 N ATOM 168 CA ARG A 51 63.523-109.622 253.053 1.00 70.34 C ANISOU 168 CA ARG A 51 9075 8161 9491 -2065 -295 182 C ATOM 169 C ARG A 51 63.600-110.538 254.268 1.00 69.35 C ANISOU 169 C ARG A 51 8937 8163 9250 -1910 -490 35 C ATOM 170 O ARG A 51 63.285-110.118 255.388 1.00 71.31 O ANISOU 170 O ARG A 51 9437 8234 9425 -1930 -542 -81 O ATOM 171 CB ARG A 51 62.211-109.836 252.300 1.00 72.45 C ANISOU 171 CB ARG A 51 9469 8298 9760 -1816 -160 374 C ATOM 172 CG ARG A 51 60.965-109.655 253.154 1.00 74.69 C ANISOU 172 CG ARG A 51 10033 8313 10035 -1630 -127 358 C ATOM 173 CD ARG A 51 60.892-108.251 253.731 1.00 82.66 C ANISOU 173 CD ARG A 51 11312 8990 11106 -1812 -57 284 C ATOM 174 NE ARG A 51 60.935-107.230 252.688 1.00 89.43 N ANISOU 174 NE ARG A 51 12228 9672 12082 -1964 66 439 N ATOM 175 CZ ARG A 51 59.864-106.770 252.049 1.00 93.00 C ANISOU 175 CZ ARG A 51 12829 9886 12620 -1809 181 624 C ATOM 176 NH1 ARG A 51 58.660-107.240 252.344 1.00 88.42 N ANISOU 176 NH1 ARG A 51 12306 9235 12056 -1508 203 653 N ATOM 177 NH2 ARG A 51 59.998-105.840 251.112 1.00 98.75 N ANISOU 177 NH2 ARG A 51 13645 10447 13427 -1958 270 790 N ATOM 178 N LEU A 52 64.019-111.790 254.070 1.00 64.61 N ANISOU 178 N LEU A 52 8079 7853 8616 -1749 -593 38 N ATOM 179 CA LEU A 52 64.114-112.721 255.190 1.00 60.10 C ANISOU 179 CA LEU A 52 7524 7389 7925 -1585 -795 -61 C ATOM 180 C LEU A 52 65.205-112.300 256.167 1.00 64.67 C ANISOU 180 C LEU A 52 8055 8051 8468 -1800 -1020 -244 C ATOM 181 O LEU A 52 65.056-112.469 257.383 1.00 65.35 O ANISOU 181 O LEU A 52 8348 8089 8393 -1744 -1174 -338 O ATOM 182 CB LEU A 52 64.364-114.138 254.674 1.00 56.91 C ANISOU 182 CB LEU A 52 6859 7235 7527 -1356 -855 -9 C ATOM 183 CG LEU A 52 64.483-115.244 255.727 1.00 62.42 C ANISOU 183 CG LEU A 52 7581 8028 8106 -1153 -1072 -63 C ATOM 184 CD1 LEU A 52 63.277-115.240 256.657 1.00 60.35 C ANISOU 184 CD1 LEU A 52 7701 7528 7702 -1041 -1019 -37 C ATOM 185 CD2 LEU A 52 64.646-116.604 255.063 1.00 58.24 C ANISOU 185 CD2 LEU A 52 6823 7680 7625 -914 -1093 -5 C ATOM 186 N LYS A 53 66.307-111.745 255.657 1.00 70.36 N ANISOU 186 N LYS A 53 8507 8902 9325 -2063 -1041 -297 N ATOM 187 CA LYS A 53 67.382-111.298 256.537 1.00 76.49 C ANISOU 187 CA LYS A 53 9189 9771 10104 -2306 -1288 -487 C ATOM 188 C LYS A 53 66.967-110.085 257.360 1.00 82.33 C ANISOU 188 C LYS A 53 10321 10196 10766 -2515 -1276 -597 C ATOM 189 O LYS A 53 67.394-109.945 258.512 1.00 84.95 O ANISOU 189 O LYS A 53 10758 10547 10972 -2613 -1527 -774 O ATOM 190 CB LYS A 53 68.634-110.991 255.715 1.00 79.62 C ANISOU 190 CB LYS A 53 9154 10385 10715 -2565 -1271 -518 C ATOM 191 CG LYS A 53 69.246-112.222 255.064 1.00 84.41 C ANISOU 191 CG LYS A 53 9340 11328 11402 -2352 -1302 -472 C ATOM 192 CD LYS A 53 70.191-111.854 253.933 1.00 91.28 C ANISOU 192 CD LYS A 53 9823 12375 12485 -2589 -1120 -460 C ATOM 193 CE LYS A 53 70.677-113.099 253.205 1.00 92.87 C ANISOU 193 CE LYS A 53 9644 12882 12761 -2334 -1084 -431 C ATOM 194 NZ LYS A 53 71.435-112.768 251.967 1.00 94.58 N ANISOU 194 NZ LYS A 53 9530 13260 13144 -2544 -808 -404 N ATOM 195 N GLU A 54 66.135-109.206 256.795 1.00 85.27 N ANISOU 195 N GLU A 54 10931 10267 11201 -2570 -1001 -503 N ATOM 196 CA GLU A 54 65.636-108.068 257.560 1.00 88.42 C ANISOU 196 CA GLU A 54 11734 10314 11547 -2720 -949 -618 C ATOM 197 C GLU A 54 64.688-108.509 258.667 1.00 83.56 C ANISOU 197 C GLU A 54 11455 9588 10706 -2466 -978 -675 C ATOM 198 O GLU A 54 64.553-107.813 259.680 1.00 89.50 O ANISOU 198 O GLU A 54 12533 10140 11335 -2584 -1019 -854 O ATOM 199 CB GLU A 54 64.933-107.076 256.632 1.00 97.52 C ANISOU 199 CB GLU A 54 13053 11150 12852 -2783 -650 -472 C ATOM 200 CG GLU A 54 65.834-106.451 255.581 1.00110.80 C ANISOU 200 CG GLU A 54 14493 12881 14724 -3090 -569 -402 C ATOM 201 CD GLU A 54 65.077-105.529 254.644 1.00121.79 C ANISOU 201 CD GLU A 54 16103 13940 16231 -3115 -294 -208 C ATOM 202 OE1 GLU A 54 63.850-105.374 254.823 1.00124.08 O ANISOU 202 OE1 GLU A 54 16688 13969 16487 -2873 -187 -142 O ATOM 203 OE2 GLU A 54 65.707-104.961 253.728 1.00127.02 O ANISOU 203 OE2 GLU A 54 16637 14600 17023 -3374 -182 -110 O ATOM 204 N VAL A 55 64.027-109.654 258.496 1.00 69.06 N ANISOU 204 N VAL A 55 9564 7871 8806 -2137 -937 -535 N ATOM 205 CA VAL A 55 63.090-110.134 259.505 1.00 62.21 C ANISOU 205 CA VAL A 55 9005 6901 7730 -1911 -912 -562 C ATOM 206 C VAL A 55 63.823-110.867 260.622 1.00 69.55 C ANISOU 206 C VAL A 55 9946 8052 8428 -1899 -1226 -685 C ATOM 207 O VAL A 55 63.483-110.721 261.802 1.00 71.37 O ANISOU 207 O VAL A 55 10531 8168 8418 -1891 -1265 -808 O ATOM 208 CB VAL A 55 62.017-111.021 258.847 1.00 54.69 C ANISOU 208 CB VAL A 55 7996 5950 6833 -1600 -727 -356 C ATOM 209 CG1 VAL A 55 61.108-111.636 259.897 1.00 55.12 C ANISOU 209 CG1 VAL A 55 8329 5927 6688 -1390 -675 -372 C ATOM 210 CG2 VAL A 55 61.204-110.214 257.849 1.00 54.53 C ANISOU 210 CG2 VAL A 55 8010 5696 7015 -1595 -466 -232 C ATOM 211 N LEU A 56 64.844-111.656 260.275 1.00 70.31 N ANISOU 211 N LEU A 56 9668 8464 8584 -1887 -1455 -654 N ATOM 212 CA LEU A 56 65.554-112.436 261.284 1.00 68.16 C ANISOU 212 CA LEU A 56 9380 8407 8109 -1827 -1803 -734 C ATOM 213 C LEU A 56 66.348-111.553 262.238 1.00 76.77 C ANISOU 213 C LEU A 56 10601 9491 9075 -2124 -2057 -967 C ATOM 214 O LEU A 56 66.605-111.953 263.379 1.00 76.25 O ANISOU 214 O LEU A 56 10723 9512 8736 -2082 -2334 -1053 O ATOM 215 CB LEU A 56 66.484-113.448 260.614 1.00 61.31 C ANISOU 215 CB LEU A 56 8037 7863 7397 -1714 -1980 -653 C ATOM 216 CG LEU A 56 65.828-114.594 259.842 1.00 57.85 C ANISOU 216 CG LEU A 56 7492 7461 7028 -1399 -1812 -458 C ATOM 217 CD1 LEU A 56 66.879-115.589 259.375 1.00 57.79 C ANISOU 217 CD1 LEU A 56 7047 7758 7155 -1276 -2014 -431 C ATOM 218 CD2 LEU A 56 64.773-115.282 260.692 1.00 54.83 C ANISOU 218 CD2 LEU A 56 7487 6936 6410 -1169 -1764 -385 C ATOM 219 N GLN A 57 66.750-110.359 261.797 1.00 81.77 N ANISOU 219 N GLN A 57 11164 10014 9892 -2439 -1982 -1069 N ATOM 220 CA GLN A 57 67.519-109.478 262.668 1.00 90.56 C ANISOU 220 CA GLN A 57 12398 11100 10912 -2768 -2234 -1320 C ATOM 221 C GLN A 57 66.659-108.849 263.755 1.00 89.75 C ANISOU 221 C GLN A 57 12887 10692 10521 -2787 -2143 -1466 C ATOM 222 O GLN A 57 67.203-108.361 264.752 1.00 93.58 O ANISOU 222 O GLN A 57 13573 11173 10810 -3007 -2409 -1699 O ATOM 223 CB GLN A 57 68.207-108.387 261.844 1.00101.14 C ANISOU 223 CB GLN A 57 13495 12377 12559 -3133 -2152 -1382 C ATOM 224 CG GLN A 57 67.266-107.332 261.286 1.00108.96 C ANISOU 224 CG GLN A 57 14770 12965 13663 -3207 -1753 -1332 C ATOM 225 CD GLN A 57 67.972-106.343 260.377 1.00116.55 C ANISOU 225 CD GLN A 57 15502 13854 14927 -3568 -1654 -1338 C ATOM 226 OE1 GLN A 57 68.935-106.689 259.692 1.00119.25 O ANISOU 226 OE1 GLN A 57 15372 14487 15452 -3672 -1740 -1285 O ATOM 227 NE2 GLN A 57 67.498-105.102 260.371 1.00118.33 N ANISOU 227 NE2 GLN A 57 16069 13676 15214 -3760 -1448 -1402 N ATOM 228 N ARG A 58 65.337-108.851 263.591 1.00 86.92 N ANISOU 228 N ARG A 58 12802 10086 10136 -2566 -1775 -1351 N ATOM 229 CA ARG A 58 64.408-108.294 264.575 1.00 85.74 C ANISOU 229 CA ARG A 58 13200 9639 9738 -2539 -1601 -1490 C ATOM 230 C ARG A 58 63.253-109.266 264.787 1.00 82.14 C ANISOU 230 C ARG A 58 12903 9168 9137 -2171 -1385 -1320 C ATOM 231 O ARG A 58 62.122-109.013 264.353 1.00 84.05 O ANISOU 231 O ARG A 58 13248 9174 9513 -2023 -1014 -1225 O ATOM 232 CB ARG A 58 63.893-106.926 264.126 1.00 84.58 C ANISOU 232 CB ARG A 58 13228 9106 9803 -2697 -1292 -1561 C ATOM 233 CG ARG A 58 64.980-105.888 263.924 1.00 88.86 C ANISOU 233 CG ARG A 58 13654 9602 10507 -3109 -1463 -1729 C ATOM 234 CD ARG A 58 64.393-104.578 263.444 1.00 87.65 C ANISOU 234 CD ARG A 58 13719 9010 10575 -3233 -1136 -1759 C ATOM 235 NE ARG A 58 63.354-104.091 264.345 1.00 87.18 N ANISOU 235 NE ARG A 58 14184 8617 10322 -3111 -914 -1912 N ATOM 236 CZ ARG A 58 63.590-103.358 265.428 1.00 89.36 C ANISOU 236 CZ ARG A 58 14855 8719 10381 -3329 -1013 -2230 C ATOM 237 NH1 ARG A 58 64.833-103.026 265.749 1.00 91.11 N ANISOU 237 NH1 ARG A 58 14983 9072 10561 -3697 -1373 -2424 N ATOM 238 NH2 ARG A 58 62.585-102.957 266.192 1.00 91.76 N ANISOU 238 NH2 ARG A 58 15636 8718 10509 -3183 -746 -2372 N ATOM 239 N PRO A 59 63.502-110.389 265.459 1.00 80.25 N ANISOU 239 N PRO A 59 12683 9168 8640 -2021 -1619 -1269 N ATOM 240 CA PRO A 59 62.426-111.358 265.695 1.00 76.24 C ANISOU 240 CA PRO A 59 12337 8632 8000 -1709 -1401 -1098 C ATOM 241 C PRO A 59 61.497-110.905 266.810 1.00 79.83 C ANISOU 241 C PRO A 59 13340 8842 8151 -1689 -1160 -1235 C ATOM 242 O PRO A 59 61.923-110.307 267.802 1.00 82.81 O ANISOU 242 O PRO A 59 14046 9179 8241 -1873 -1319 -1467 O ATOM 243 CB PRO A 59 63.185-112.631 266.087 1.00 77.57 C ANISOU 243 CB PRO A 59 12372 9112 7990 -1588 -1771 -1001 C ATOM 244 CG PRO A 59 64.425-112.121 266.738 1.00 81.64 C ANISOU 244 CG PRO A 59 12896 9767 8357 -1842 -2191 -1211 C ATOM 245 CD PRO A 59 64.788-110.846 266.017 1.00 83.90 C ANISOU 245 CD PRO A 59 13003 9931 8944 -2125 -2107 -1348 C ATOM 246 N ALA A 60 60.209-111.201 266.637 1.00 73.67 N ANISOU 246 N ALA A 60 12648 7903 7439 -1469 -764 -1104 N ATOM 247 CA ALA A 60 59.201-110.833 267.624 1.00 68.82 C ANISOU 247 CA ALA A 60 12513 7058 6579 -1415 -440 -1223 C ATOM 248 C ALA A 60 58.007-111.764 267.480 1.00 64.44 C ANISOU 248 C ALA A 60 11926 6475 6082 -1146 -113 -1007 C ATOM 249 O ALA A 60 57.527-111.988 266.365 1.00 64.57 O ANISOU 249 O ALA A 60 11588 6475 6470 -1027 26 -833 O ATOM 250 CB ALA A 60 58.766-109.373 267.452 1.00 65.72 C ANISOU 250 CB ALA A 60 12262 6337 6370 -1529 -173 -1410 C ATOM 251 N GLY A 105 57.535-112.301 268.603 1.00 59.58 N ANISOU 251 N GLY A 105 11694 5856 5090 -1070 7 -1019 N ATOM 252 CA GLY A 105 56.390-113.188 268.581 1.00 57.39 C ANISOU 252 CA GLY A 105 11404 5539 4863 -858 345 -824 C ATOM 253 C GLY A 105 56.721-114.548 267.983 1.00 63.45 C ANISOU 253 C GLY A 105 11850 6525 5733 -740 118 -563 C ATOM 254 O GLY A 105 57.883-114.945 267.851 1.00 67.26 O ANISOU 254 O GLY A 105 12187 7215 6155 -790 -312 -536 O ATOM 255 N ARG A 106 55.661-115.268 267.612 1.00 73.98 N ANISOU 255 N ARG A 106 13058 7798 7254 -579 421 -383 N ATOM 256 CA ARG A 106 55.761-116.580 266.975 1.00 78.33 C ANISOU 256 CA ARG A 106 13323 8491 7947 -457 278 -147 C ATOM 257 C ARG A 106 55.057-116.556 265.621 1.00 78.36 C ANISOU 257 C ARG A 106 12900 8438 8435 -376 454 -47 C ATOM 258 O ARG A 106 54.022-117.212 265.441 1.00 83.47 O ANISOU 258 O ARG A 106 13473 9014 9227 -270 718 83 O ATOM 259 CB ARG A 106 55.156-117.673 267.854 1.00 93.40 C ANISOU 259 CB ARG A 106 15520 10378 9590 -369 442 -6 C ATOM 260 CG ARG A 106 56.086-118.277 268.889 1.00110.87 C ANISOU 260 CG ARG A 106 18066 12722 11336 -391 103 19 C ATOM 261 CD ARG A 106 55.454-119.537 269.464 1.00124.08 C ANISOU 261 CD ARG A 106 19966 14350 12828 -289 271 238 C ATOM 262 NE ARG A 106 56.265-120.162 270.503 1.00137.71 N ANISOU 262 NE ARG A 106 22070 16179 14075 -283 -60 306 N ATOM 263 CZ ARG A 106 55.964-121.320 271.082 1.00146.38 C ANISOU 263 CZ ARG A 106 23429 17236 14952 -201 -3 529 C ATOM 264 NH1 ARG A 106 54.872-121.979 270.718 1.00147.42 N ANISOU 264 NH1 ARG A 106 23459 17230 15326 -148 390 683 N ATOM 265 NH2 ARG A 106 56.754-121.821 272.021 1.00150.72 N ANISOU 265 NH2 ARG A 106 24345 17874 15047 -180 -354 607 N ATOM 266 N PRO A 107 55.591-115.819 264.640 1.00 69.54 N ANISOU 266 N PRO A 107 11501 7353 7568 -440 305 -99 N ATOM 267 CA PRO A 107 54.944-115.796 263.325 1.00 58.13 C ANISOU 267 CA PRO A 107 9689 5865 6530 -362 432 11 C ATOM 268 C PRO A 107 55.556-116.801 262.364 1.00 56.05 C ANISOU 268 C PRO A 107 9102 5798 6397 -310 176 147 C ATOM 269 O PRO A 107 56.679-117.269 262.577 1.00 61.33 O ANISOU 269 O PRO A 107 9762 6635 6906 -341 -127 135 O ATOM 270 CB PRO A 107 55.189-114.360 262.859 1.00 59.60 C ANISOU 270 CB PRO A 107 9833 5946 6867 -472 439 -113 C ATOM 271 CG PRO A 107 56.556-114.060 263.407 1.00 61.93 C ANISOU 271 CG PRO A 107 10254 6363 6914 -639 124 -248 C ATOM 272 CD PRO A 107 56.710-114.860 264.694 1.00 68.17 C ANISOU 272 CD PRO A 107 11353 7228 7319 -611 49 -265 C ATOM 273 N CYS A 108 54.826-117.143 261.307 1.00 53.06 N ANISOU 273 N CYS A 108 8452 5398 6312 -222 287 264 N ATOM 274 CA CYS A 108 55.409-117.924 260.226 1.00 49.41 C ANISOU 274 CA CYS A 108 7688 5103 5983 -183 71 352 C ATOM 275 C CYS A 108 56.410-117.065 259.463 1.00 42.81 C ANISOU 275 C CYS A 108 6684 4363 5218 -297 -102 286 C ATOM 276 O CYS A 108 56.095-115.946 259.048 1.00 47.37 O ANISOU 276 O CYS A 108 7248 4824 5925 -362 13 255 O ATOM 277 CB CYS A 108 54.317-118.437 259.291 1.00 52.95 C ANISOU 277 CB CYS A 108 7924 5497 6698 -86 221 469 C ATOM 278 SG CYS A 108 53.384-119.834 259.950 1.00 54.22 S ANISOU 278 SG CYS A 108 8190 5585 6825 9 377 573 S ATOM 279 N LEU A 109 57.622-117.582 259.290 1.00 43.61 N ANISOU 279 N LEU A 109 6654 4663 5251 -318 -367 270 N ATOM 280 CA LEU A 109 58.681-116.777 258.701 1.00 45.24 C ANISOU 280 CA LEU A 109 6693 4979 5516 -464 -508 195 C ATOM 281 C LEU A 109 58.583-116.771 257.176 1.00 47.82 C ANISOU 281 C LEU A 109 6742 5362 6067 -451 -458 279 C ATOM 282 O LEU A 109 58.054-117.709 256.574 1.00 48.00 O ANISOU 282 O LEU A 109 6655 5412 6170 -315 -422 370 O ATOM 283 CB LEU A 109 60.048-117.302 259.125 1.00 48.06 C ANISOU 283 CB LEU A 109 6966 5550 5746 -489 -807 133 C ATOM 284 CG LEU A 109 60.365-117.228 260.619 1.00 51.53 C ANISOU 284 CG LEU A 109 7699 5972 5907 -529 -942 45 C ATOM 285 CD1 LEU A 109 61.818-117.590 260.873 1.00 52.49 C ANISOU 285 CD1 LEU A 109 7656 6330 5960 -559 -1299 -17 C ATOM 286 CD2 LEU A 109 60.047-115.845 261.165 1.00 52.46 C ANISOU 286 CD2 LEU A 109 8062 5914 5957 -701 -811 -82 C ATOM 287 N PRO A 110 59.076-115.713 256.532 1.00 49.47 N ANISOU 287 N PRO A 110 6862 5574 6359 -608 -452 250 N ATOM 288 CA PRO A 110 59.114-115.699 255.067 1.00 46.90 C ANISOU 288 CA PRO A 110 6313 5326 6182 -613 -413 339 C ATOM 289 C PRO A 110 60.047-116.772 254.531 1.00 51.77 C ANISOU 289 C PRO A 110 6684 6196 6788 -556 -554 329 C ATOM 290 O PRO A 110 61.035-117.141 255.169 1.00 55.44 O ANISOU 290 O PRO A 110 7087 6798 7180 -571 -721 244 O ATOM 291 CB PRO A 110 59.633-114.294 254.737 1.00 43.82 C ANISOU 291 CB PRO A 110 5937 4869 5843 -832 -376 309 C ATOM 292 CG PRO A 110 59.366-113.481 255.965 1.00 43.40 C ANISOU 292 CG PRO A 110 6158 4614 5719 -902 -338 207 C ATOM 293 CD PRO A 110 59.520-114.433 257.108 1.00 49.10 C ANISOU 293 CD PRO A 110 6964 5425 6268 -805 -457 136 C ATOM 294 N GLU A 111 59.720-117.279 253.344 1.00 48.86 N ANISOU 294 N GLU A 111 6178 5888 6498 -477 -498 408 N ATOM 295 CA GLU A 111 60.557-118.282 252.701 1.00 51.85 C ANISOU 295 CA GLU A 111 6332 6486 6881 -405 -583 376 C ATOM 296 C GLU A 111 60.274-118.291 251.206 1.00 50.43 C ANISOU 296 C GLU A 111 6053 6359 6747 -408 -483 442 C ATOM 297 O GLU A 111 59.225-117.832 250.749 1.00 52.15 O ANISOU 297 O GLU A 111 6379 6437 6997 -408 -397 539 O ATOM 298 CB GLU A 111 60.339-119.673 253.309 1.00 51.75 C ANISOU 298 CB GLU A 111 6354 6471 6836 -203 -672 368 C ATOM 299 CG GLU A 111 58.899-120.148 253.295 1.00 59.06 C ANISOU 299 CG GLU A 111 7422 7221 7797 -99 -572 452 C ATOM 300 CD GLU A 111 58.724-121.473 254.010 1.00 72.31 C ANISOU 300 CD GLU A 111 9176 8855 9442 59 -639 459 C ATOM 301 OE1 GLU A 111 59.631-121.862 254.776 1.00 77.71 O ANISOU 301 OE1 GLU A 111 9867 9615 10045 104 -785 415 O ATOM 302 OE2 GLU A 111 57.680-122.128 253.806 1.00 74.92 O ANISOU 302 OE2 GLU A 111 9560 9070 9837 132 -561 516 O ATOM 303 N TRP A 112 61.233-118.823 250.454 1.00 49.85 N ANISOU 303 N TRP A 112 5773 6498 6672 -399 -499 386 N ATOM 304 CA TRP A 112 61.180-118.881 248.998 1.00 45.65 C ANISOU 304 CA TRP A 112 5167 6058 6119 -417 -397 424 C ATOM 305 C TRP A 112 60.865-120.311 248.577 1.00 44.60 C ANISOU 305 C TRP A 112 4999 5969 5980 -217 -432 379 C ATOM 306 O TRP A 112 61.609-121.238 248.918 1.00 52.65 O ANISOU 306 O TRP A 112 5895 7084 7026 -99 -502 279 O ATOM 307 CB TRP A 112 62.507-118.411 248.400 1.00 47.51 C ANISOU 307 CB TRP A 112 5203 6499 6350 -573 -326 369 C ATOM 308 CG TRP A 112 62.574-118.464 246.906 1.00 55.43 C ANISOU 308 CG TRP A 112 6167 7622 7274 -608 -185 403 C ATOM 309 CD1 TRP A 112 63.220-119.397 246.147 1.00 56.99 C ANISOU 309 CD1 TRP A 112 6199 8017 7437 -516 -126 301 C ATOM 310 CD2 TRP A 112 61.984-117.537 245.987 1.00 55.37 C ANISOU 310 CD2 TRP A 112 6318 7537 7183 -737 -83 550 C ATOM 311 NE1 TRP A 112 63.066-119.109 244.812 1.00 57.94 N ANISOU 311 NE1 TRP A 112 6388 8206 7423 -600 21 362 N ATOM 312 CE2 TRP A 112 62.309-117.975 244.687 1.00 55.25 C ANISOU 312 CE2 TRP A 112 6251 7701 7043 -735 30 533 C ATOM 313 CE3 TRP A 112 61.209-116.383 246.136 1.00 54.88 C ANISOU 313 CE3 TRP A 112 6455 7259 7138 -836 -79 695 C ATOM 314 CZ2 TRP A 112 61.886-117.299 243.545 1.00 57.15 C ANISOU 314 CZ2 TRP A 112 6655 7924 7135 -843 123 679 C ATOM 315 CZ3 TRP A 112 60.790-115.714 245.000 1.00 57.96 C ANISOU 315 CZ3 TRP A 112 6981 7613 7428 -919 1 850 C ATOM 316 CH2 TRP A 112 61.130-116.173 243.722 1.00 58.79 C ANISOU 316 CH2 TRP A 112 7054 7913 7371 -930 89 851 C ATOM 317 N ASP A 113 59.767-120.489 247.841 1.00 40.49 N ANISOU 317 N ASP A 113 4583 5362 5439 -177 -405 449 N ATOM 318 CA ASP A 113 59.303-121.811 247.437 1.00 41.51 C ANISOU 318 CA ASP A 113 4715 5485 5572 -23 -447 393 C ATOM 319 C ASP A 113 59.535-122.081 245.951 1.00 44.06 C ANISOU 319 C ASP A 113 4995 5958 5789 -36 -386 347 C ATOM 320 O ASP A 113 58.815-122.879 245.347 1.00 48.63 O ANISOU 320 O ASP A 113 5636 6497 6345 39 -426 316 O ATOM 321 CB ASP A 113 57.825-121.993 247.787 1.00 43.57 C ANISOU 321 CB ASP A 113 5110 5541 5903 24 -486 475 C ATOM 322 CG ASP A 113 56.909-121.055 247.013 1.00 52.91 C ANISOU 322 CG ASP A 113 6355 6670 7077 -60 -465 595 C ATOM 323 OD1 ASP A 113 57.409-120.202 246.250 1.00 55.12 O ANISOU 323 OD1 ASP A 113 6632 7046 7266 -166 -417 639 O ATOM 324 OD2 ASP A 113 55.676-121.176 247.170 1.00 53.28 O ANISOU 324 OD2 ASP A 113 6450 6574 7220 -19 -499 656 O ATOM 325 N HIS A 114 60.526-121.410 245.360 1.00 47.48 N ANISOU 325 N HIS A 114 5335 6559 6145 -153 -279 334 N ATOM 326 CA HIS A 114 60.999-121.488 243.980 1.00 46.31 C ANISOU 326 CA HIS A 114 5160 6590 5846 -201 -157 289 C ATOM 327 C HIS A 114 60.194-120.608 243.020 1.00 48.83 C ANISOU 327 C HIS A 114 5660 6872 6022 -325 -138 446 C ATOM 328 O HIS A 114 60.620-120.438 241.877 1.00 56.10 O ANISOU 328 O HIS A 114 6612 7944 6761 -406 -17 444 O ATOM 329 CB HIS A 114 61.032-122.923 243.414 1.00 42.43 C ANISOU 329 CB HIS A 114 4651 6154 5318 -31 -164 124 C ATOM 330 CG HIS A 114 61.848-123.877 244.229 1.00 52.82 C ANISOU 330 CG HIS A 114 5802 7486 6780 135 -196 -16 C ATOM 331 ND1 HIS A 114 61.286-124.918 244.938 1.00 55.28 N ANISOU 331 ND1 HIS A 114 6178 7626 7198 299 -329 -52 N ATOM 332 CD2 HIS A 114 63.182-123.949 244.448 1.00 55.82 C ANISOU 332 CD2 HIS A 114 5948 8029 7232 168 -125 -115 C ATOM 333 CE1 HIS A 114 62.240-125.590 245.558 1.00 54.78 C ANISOU 333 CE1 HIS A 114 5964 7603 7246 447 -355 -150 C ATOM 334 NE2 HIS A 114 63.399-125.023 245.278 1.00 56.05 N ANISOU 334 NE2 HIS A 114 5917 7978 7401 380 -246 -198 N ATOM 335 N ILE A 115 59.059-120.040 243.428 1.00 49.45 N ANISOU 335 N ILE A 115 5863 6755 6170 -331 -245 588 N ATOM 336 CA ILE A 115 58.277-119.214 242.512 1.00 46.98 C ANISOU 336 CA ILE A 115 5712 6395 5744 -409 -272 758 C ATOM 337 C ILE A 115 57.995-117.840 243.109 1.00 49.26 C ANISOU 337 C ILE A 115 6070 6509 6136 -501 -261 924 C ATOM 338 O ILE A 115 58.226-116.817 242.454 1.00 56.79 O ANISOU 338 O ILE A 115 7126 7463 6989 -637 -188 1061 O ATOM 339 CB ILE A 115 56.973-119.922 242.098 1.00 43.41 C ANISOU 339 CB ILE A 115 5334 5870 5292 -296 -441 767 C ATOM 340 CG1 ILE A 115 57.259-120.913 240.968 1.00 42.43 C ANISOU 340 CG1 ILE A 115 5239 5919 4963 -269 -436 627 C ATOM 341 CG2 ILE A 115 55.925-118.910 241.656 1.00 51.97 C ANISOU 341 CG2 ILE A 115 6544 6833 6368 -328 -544 980 C ATOM 342 CD1 ILE A 115 56.020-121.477 240.307 1.00 41.43 C ANISOU 342 CD1 ILE A 115 5206 5744 4792 -216 -634 631 C ATOM 343 N LEU A 116 57.495-117.789 244.344 1.00 45.38 N ANISOU 343 N LEU A 116 5557 5850 5836 -433 -313 913 N ATOM 344 CA LEU A 116 57.181-116.507 244.963 1.00 53.87 C ANISOU 344 CA LEU A 116 6723 6728 7019 -501 -285 1032 C ATOM 345 C LEU A 116 57.631-116.500 246.418 1.00 52.76 C ANISOU 345 C LEU A 116 6533 6520 6992 -506 -259 921 C ATOM 346 O LEU A 116 57.994-117.530 246.992 1.00 50.80 O ANISOU 346 O LEU A 116 6188 6360 6755 -426 -294 789 O ATOM 347 CB LEU A 116 55.685-116.169 244.844 1.00 57.80 C ANISOU 347 CB LEU A 116 7306 7036 7619 -395 -380 1169 C ATOM 348 CG LEU A 116 54.599-117.025 245.502 1.00 55.66 C ANISOU 348 CG LEU A 116 6966 6679 7503 -238 -457 1114 C ATOM 349 CD1 LEU A 116 54.372-116.624 246.948 1.00 66.44 C ANISOU 349 CD1 LEU A 116 8352 7866 9028 -212 -376 1080 C ATOM 350 CD2 LEU A 116 53.303-116.915 244.716 1.00 48.00 C ANISOU 350 CD2 LEU A 116 6004 5642 6593 -154 -589 1243 C ATOM 351 N CYS A 117 57.597-115.308 247.008 1.00 51.24 N ANISOU 351 N CYS A 117 6440 6154 6873 -599 -208 978 N ATOM 352 CA CYS A 117 58.060-115.070 248.368 1.00 48.99 C ANISOU 352 CA CYS A 117 6167 5799 6649 -643 -194 868 C ATOM 353 C CYS A 117 56.860-114.901 249.290 1.00 48.99 C ANISOU 353 C CYS A 117 6284 5569 6762 -522 -187 886 C ATOM 354 O CYS A 117 55.990-114.061 249.038 1.00 48.32 O ANISOU 354 O CYS A 117 6299 5295 6767 -495 -148 1001 O ATOM 355 CB CYS A 117 58.944-113.823 248.418 1.00 60.09 C ANISOU 355 CB CYS A 117 7621 7158 8054 -869 -124 877 C ATOM 356 SG CYS A 117 59.892-113.591 249.939 1.00 68.38 S ANISOU 356 SG CYS A 117 8657 8201 9125 -986 -164 694 S ATOM 357 N TRP A 118 56.822-115.687 250.348 1.00 45.57 N ANISOU 357 N TRP A 118 5842 5146 6328 -441 -211 780 N ATOM 358 CA TRP A 118 55.679-115.588 251.243 1.00 37.89 C ANISOU 358 CA TRP A 118 4978 3970 5448 -336 -146 788 C ATOM 359 C TRP A 118 55.979-114.637 252.396 1.00 38.22 C ANISOU 359 C TRP A 118 5187 3864 5471 -426 -79 707 C ATOM 360 O TRP A 118 57.122-114.541 252.850 1.00 43.78 O ANISOU 360 O TRP A 118 5895 4667 6073 -550 -142 608 O ATOM 361 CB TRP A 118 55.310-116.964 251.784 1.00 34.68 C ANISOU 361 CB TRP A 118 4529 3618 5030 -210 -175 740 C ATOM 362 CG TRP A 118 54.826-117.866 250.705 1.00 36.99 C ANISOU 362 CG TRP A 118 4689 4001 5363 -131 -238 793 C ATOM 363 CD1 TRP A 118 55.586-118.661 249.897 1.00 38.20 C ANISOU 363 CD1 TRP A 118 4738 4346 5430 -135 -325 753 C ATOM 364 CD2 TRP A 118 53.470-118.052 250.292 1.00 39.55 C ANISOU 364 CD2 TRP A 118 4966 4229 5830 -43 -226 873 C ATOM 365 NE1 TRP A 118 54.783-119.339 249.011 1.00 41.14 N ANISOU 365 NE1 TRP A 118 5047 4736 5850 -66 -374 791 N ATOM 366 CE2 TRP A 118 53.479-118.983 249.234 1.00 37.99 C ANISOU 366 CE2 TRP A 118 4665 4170 5599 -18 -336 870 C ATOM 367 CE3 TRP A 118 52.246-117.528 250.719 1.00 37.88 C ANISOU 367 CE3 TRP A 118 4772 3832 5790 22 -130 931 C ATOM 368 CZ2 TRP A 118 52.313-119.397 248.596 1.00 32.62 C ANISOU 368 CZ2 TRP A 118 3901 3454 5038 41 -395 923 C ATOM 369 CZ3 TRP A 118 51.091-117.940 250.085 1.00 40.56 C ANISOU 369 CZ3 TRP A 118 4978 4147 6285 99 -176 997 C ATOM 370 CH2 TRP A 118 51.132-118.866 249.034 1.00 38.89 C ANISOU 370 CH2 TRP A 118 4669 4083 6026 95 -329 994 C ATOM 371 N PRO A 119 54.970-113.918 252.884 1.00 38.03 N ANISOU 371 N PRO A 119 5293 3603 5555 -365 44 730 N ATOM 372 CA PRO A 119 55.217-112.915 253.926 1.00 40.13 C ANISOU 372 CA PRO A 119 5765 3695 5790 -458 127 624 C ATOM 373 C PRO A 119 55.223-113.514 255.322 1.00 47.84 C ANISOU 373 C PRO A 119 6864 4680 6633 -425 155 496 C ATOM 374 O PRO A 119 55.191-114.738 255.481 1.00 50.62 O ANISOU 374 O PRO A 119 7137 5176 6921 -342 98 506 O ATOM 375 CB PRO A 119 54.046-111.947 253.742 1.00 43.43 C ANISOU 375 CB PRO A 119 6261 3838 6401 -360 271 704 C ATOM 376 CG PRO A 119 52.927-112.847 253.320 1.00 45.90 C ANISOU 376 CG PRO A 119 6408 4200 6831 -174 281 801 C ATOM 377 CD PRO A 119 53.553-113.945 252.479 1.00 40.52 C ANISOU 377 CD PRO A 119 5556 3793 6046 -205 114 839 C ATOM 378 N LEU A 120 55.270-112.658 256.340 1.00 50.18 N ANISOU 378 N LEU A 120 7392 4806 6868 -494 243 375 N ATOM 379 CA LEU A 120 55.059-113.124 257.702 1.00 44.73 C ANISOU 379 CA LEU A 120 6891 4092 6012 -452 308 267 C ATOM 380 C LEU A 120 53.633-113.637 257.852 1.00 45.79 C ANISOU 380 C LEU A 120 7004 4126 6266 -264 514 340 C ATOM 381 O LEU A 120 52.685-113.048 257.325 1.00 52.46 O ANISOU 381 O LEU A 120 7780 4813 7341 -173 651 408 O ATOM 382 CB LEU A 120 55.325-112.000 258.704 1.00 50.94 C ANISOU 382 CB LEU A 120 7970 4697 6689 -574 378 96 C ATOM 383 CG LEU A 120 56.778-111.612 258.982 1.00 56.73 C ANISOU 383 CG LEU A 120 8750 5540 7265 -801 155 -30 C ATOM 384 CD1 LEU A 120 56.834-110.372 259.861 1.00 62.73 C ANISOU 384 CD1 LEU A 120 9826 6058 7952 -934 244 -216 C ATOM 385 CD2 LEU A 120 57.519-112.761 259.640 1.00 53.55 C ANISOU 385 CD2 LEU A 120 8327 5387 6633 -796 -50 -64 C ATOM 386 N GLY A 121 53.485-114.746 258.568 1.00 45.36 N ANISOU 386 N GLY A 121 6998 4161 6075 -208 528 338 N ATOM 387 CA GLY A 121 52.177-115.337 258.764 1.00 48.12 C ANISOU 387 CA GLY A 121 7306 4429 6550 -72 744 405 C ATOM 388 C GLY A 121 51.725-115.323 260.208 1.00 56.49 C ANISOU 388 C GLY A 121 8655 5374 7435 -60 977 311 C ATOM 389 O GLY A 121 52.450-115.777 261.098 1.00 58.38 O ANISOU 389 O GLY A 121 9112 5696 7375 -124 884 254 O ATOM 390 N ALA A 122 50.527-114.797 260.455 1.00 60.52 N ANISOU 390 N ALA A 122 9176 5697 8123 31 1283 294 N ATOM 391 CA ALA A 122 49.982-114.807 261.804 1.00 59.12 C ANISOU 391 CA ALA A 122 9279 5409 7773 47 1582 198 C ATOM 392 C ALA A 122 49.479-116.206 262.155 1.00 60.34 C ANISOU 392 C ALA A 122 9400 5649 7877 75 1675 307 C ATOM 393 O ALA A 122 48.906-116.890 261.302 1.00 59.27 O ANISOU 393 O ALA A 122 8955 5561 8004 130 1646 435 O ATOM 394 CB ALA A 122 48.845-113.798 261.934 1.00 55.74 C ANISOU 394 CB ALA A 122 8835 4747 7596 158 1924 132 C ATOM 395 N PRO A 123 49.685-116.653 263.393 1.00 62.96 N ANISOU 395 N PRO A 123 10071 5988 7862 25 1775 262 N ATOM 396 CA PRO A 123 49.277-118.014 263.768 1.00 62.80 C ANISOU 396 CA PRO A 123 10074 6017 7771 31 1866 393 C ATOM 397 C PRO A 123 47.781-118.231 263.585 1.00 63.44 C ANISOU 397 C PRO A 123 9922 5992 8192 97 2232 455 C ATOM 398 O PRO A 123 46.957-117.446 264.060 1.00 63.49 O ANISOU 398 O PRO A 123 9972 5861 8292 145 2584 361 O ATOM 399 CB PRO A 123 49.687-118.112 265.242 1.00 63.19 C ANISOU 399 CB PRO A 123 10611 6053 7344 -34 1953 324 C ATOM 400 CG PRO A 123 50.770-117.101 265.401 1.00 67.06 C ANISOU 400 CG PRO A 123 11269 6575 7636 -98 1704 164 C ATOM 401 CD PRO A 123 50.409-115.973 264.480 1.00 68.18 C ANISOU 401 CD PRO A 123 11143 6617 8144 -59 1761 96 C ATOM 402 N GLY A 124 47.439-119.311 262.885 1.00 59.97 N ANISOU 402 N GLY A 124 9215 5612 7959 99 2148 599 N ATOM 403 CA GLY A 124 46.057-119.681 262.663 1.00 62.00 C ANISOU 403 CA GLY A 124 9194 5793 8570 127 2444 664 C ATOM 404 C GLY A 124 45.347-118.929 261.561 1.00 63.56 C ANISOU 404 C GLY A 124 8979 5964 9208 221 2420 654 C ATOM 405 O GLY A 124 44.126-119.067 261.428 1.00 66.16 O ANISOU 405 O GLY A 124 9031 6232 9874 257 2669 686 O ATOM 406 N GLU A 125 46.063-118.146 260.760 1.00 57.90 N ANISOU 406 N GLU A 125 8203 5289 8506 257 2124 622 N ATOM 407 CA GLU A 125 45.455-117.326 259.724 1.00 62.49 C ANISOU 407 CA GLU A 125 8459 5826 9459 361 2069 639 C ATOM 408 C GLU A 125 45.858-117.819 258.341 1.00 57.96 C ANISOU 408 C GLU A 125 7643 5393 8985 342 1679 737 C ATOM 409 O GLU A 125 46.937-118.391 258.154 1.00 55.45 O ANISOU 409 O GLU A 125 7447 5199 8423 265 1431 748 O ATOM 410 CB GLU A 125 45.853-115.855 259.884 1.00 75.41 C ANISOU 410 CB GLU A 125 10269 7345 11040 414 2090 532 C ATOM 411 CG GLU A 125 45.605-115.286 261.274 1.00 92.19 C ANISOU 411 CG GLU A 125 12709 9321 12996 426 2467 385 C ATOM 412 CD GLU A 125 44.131-115.162 261.612 1.00105.44 C ANISOU 412 CD GLU A 125 14190 10873 14999 547 2886 371 C ATOM 413 OE1 GLU A 125 43.306-115.080 260.678 1.00108.08 O ANISOU 413 OE1 GLU A 125 14115 11198 15754 655 2839 459 O ATOM 414 OE2 GLU A 125 43.799-115.149 262.817 1.00111.11 O ANISOU 414 OE2 GLU A 125 15156 11512 15547 534 3264 268 O ATOM 415 N VAL A 126 44.977-117.592 257.373 1.00 56.06 N ANISOU 415 N VAL A 126 7057 5139 9103 425 1624 803 N ATOM 416 CA VAL A 126 45.252-117.900 255.976 1.00 49.99 C ANISOU 416 CA VAL A 126 6085 4500 8411 414 1263 885 C ATOM 417 C VAL A 126 45.978-116.720 255.349 1.00 47.84 C ANISOU 417 C VAL A 126 5897 4215 8066 449 1083 891 C ATOM 418 O VAL A 126 45.625-115.558 255.585 1.00 47.17 O ANISOU 418 O VAL A 126 5849 3973 8100 542 1223 869 O ATOM 419 CB VAL A 126 43.947-118.221 255.224 1.00 53.86 C ANISOU 419 CB VAL A 126 6178 4992 9294 472 1241 957 C ATOM 420 CG1 VAL A 126 44.229-118.498 253.754 1.00 57.76 C ANISOU 420 CG1 VAL A 126 6516 5625 9806 454 849 1027 C ATOM 421 CG2 VAL A 126 43.243-119.408 255.863 1.00 53.42 C ANISOU 421 CG2 VAL A 126 6035 4931 9332 388 1447 951 C ATOM 422 N VAL A 127 47.005-117.012 254.557 1.00 43.55 N ANISOU 422 N VAL A 127 5394 3818 7336 372 800 916 N ATOM 423 CA VAL A 127 47.826-115.993 253.911 1.00 43.03 C ANISOU 423 CA VAL A 127 5419 3754 7175 355 643 937 C ATOM 424 C VAL A 127 47.615-116.092 252.406 1.00 46.62 C ANISOU 424 C VAL A 127 5667 4309 7736 380 390 1053 C ATOM 425 O VAL A 127 47.800-117.163 251.815 1.00 44.63 O ANISOU 425 O VAL A 127 5322 4216 7418 330 233 1060 O ATOM 426 CB VAL A 127 49.308-116.152 254.274 1.00 40.86 C ANISOU 426 CB VAL A 127 5364 3586 6575 227 554 860 C ATOM 427 CG1 VAL A 127 50.161-115.202 253.453 1.00 41.45 C ANISOU 427 CG1 VAL A 127 5485 3683 6582 166 403 893 C ATOM 428 CG2 VAL A 127 49.516-115.904 255.760 1.00 39.48 C ANISOU 428 CG2 VAL A 127 5438 3310 6251 199 759 744 C ATOM 429 N ALA A 128 47.228-114.978 251.789 1.00 49.54 N ANISOU 429 N ALA A 128 5998 4570 8253 463 343 1143 N ATOM 430 CA ALA A 128 46.972-114.915 250.357 1.00 49.88 C ANISOU 430 CA ALA A 128 5897 4697 8360 497 84 1278 C ATOM 431 C ALA A 128 47.964-113.965 249.703 1.00 52.54 C ANISOU 431 C ALA A 128 6423 5025 8516 429 -18 1346 C ATOM 432 O ALA A 128 48.122-112.823 250.147 1.00 64.48 O ANISOU 432 O ALA A 128 8090 6344 10068 447 103 1350 O ATOM 433 CB ALA A 128 45.537-114.463 250.071 1.00 53.84 C ANISOU 433 CB ALA A 128 6166 5074 9218 674 76 1374 C ATOM 434 N VAL A 129 48.627-114.439 248.654 1.00 46.12 N ANISOU 434 N VAL A 129 5610 4407 7506 338 -216 1390 N ATOM 435 CA VAL A 129 49.583-113.652 247.887 1.00 43.19 C ANISOU 435 CA VAL A 129 5401 4058 6949 239 -292 1472 C ATOM 436 C VAL A 129 49.067-113.566 246.458 1.00 51.11 C ANISOU 436 C VAL A 129 6344 5128 7947 293 -521 1644 C ATOM 437 O VAL A 129 48.754-114.599 245.864 1.00 59.12 O ANISOU 437 O VAL A 129 7227 6317 8918 298 -668 1621 O ATOM 438 CB VAL A 129 50.998-114.260 247.908 1.00 41.11 C ANISOU 438 CB VAL A 129 5212 3995 6413 70 -286 1360 C ATOM 439 CG1 VAL A 129 51.945-113.451 247.037 1.00 33.59 C ANISOU 439 CG1 VAL A 129 4391 3080 5291 -59 -323 1453 C ATOM 440 CG2 VAL A 129 51.521-114.339 249.332 1.00 31.85 C ANISOU 440 CG2 VAL A 129 4115 2768 5217 22 -122 1204 C ATOM 441 N PRO A 130 48.948-112.373 245.873 1.00 52.61 N ANISOU 441 N PRO A 130 6652 5170 8169 332 -574 1819 N ATOM 442 CA PRO A 130 48.519-112.286 244.472 1.00 51.15 C ANISOU 442 CA PRO A 130 6460 5062 7912 380 -829 2008 C ATOM 443 C PRO A 130 49.521-112.973 243.558 1.00 50.67 C ANISOU 443 C PRO A 130 6486 5271 7496 209 -906 1979 C ATOM 444 O PRO A 130 50.726-112.969 243.815 1.00 52.18 O ANISOU 444 O PRO A 130 6782 5530 7512 50 -754 1889 O ATOM 445 CB PRO A 130 48.454-110.776 244.212 1.00 45.53 C ANISOU 445 CB PRO A 130 5937 4091 7273 435 -822 2210 C ATOM 446 CG PRO A 130 49.373-110.178 245.224 1.00 48.47 C ANISOU 446 CG PRO A 130 6465 4322 7628 307 -559 2092 C ATOM 447 CD PRO A 130 49.253-111.049 246.443 1.00 51.68 C ANISOU 447 CD PRO A 130 6721 4790 8127 320 -415 1855 C ATOM 448 N CYS A 131 49.003-113.585 242.496 1.00 48.47 N ANISOU 448 N CYS A 131 6147 5151 7120 245 -1145 2038 N ATOM 449 CA CYS A 131 49.853-114.354 241.595 1.00 56.21 C ANISOU 449 CA CYS A 131 7213 6391 7753 104 -1196 1974 C ATOM 450 C CYS A 131 50.939-113.450 241.016 1.00 57.79 C ANISOU 450 C CYS A 131 7663 6597 7699 -38 -1092 2097 C ATOM 451 O CYS A 131 50.629-112.358 240.518 1.00 59.38 O ANISOU 451 O CYS A 131 8015 6645 7901 -3 -1164 2330 O ATOM 452 CB CYS A 131 49.024-114.987 240.477 1.00 57.69 C ANISOU 452 CB CYS A 131 7350 6720 7852 160 -1499 2022 C ATOM 453 SG CYS A 131 47.707-116.087 241.066 1.00 60.92 S ANISOU 453 SG CYS A 131 7428 7119 8598 273 -1624 1877 S ATOM 454 N PRO A 132 52.207-113.859 241.068 1.00 56.22 N ANISOU 454 N PRO A 132 7502 6558 7302 -199 -917 1957 N ATOM 455 CA PRO A 132 53.304-112.919 240.798 1.00 58.27 C ANISOU 455 CA PRO A 132 7942 6796 7400 -373 -746 2052 C ATOM 456 C PRO A 132 53.294-112.390 239.370 1.00 66.29 C ANISOU 456 C PRO A 132 9187 7864 8138 -429 -843 2283 C ATOM 457 O PRO A 132 52.966-113.105 238.419 1.00 65.32 O ANISOU 457 O PRO A 132 9090 7925 7803 -394 -1006 2283 O ATOM 458 CB PRO A 132 54.560-113.753 241.079 1.00 53.73 C ANISOU 458 CB PRO A 132 7269 6441 6703 -502 -574 1821 C ATOM 459 CG PRO A 132 54.120-115.177 240.949 1.00 52.99 C ANISOU 459 CG PRO A 132 7036 6510 6588 -393 -696 1657 C ATOM 460 CD PRO A 132 52.699-115.199 241.429 1.00 51.61 C ANISOU 460 CD PRO A 132 6774 6163 6674 -223 -860 1706 C ATOM 461 N ASP A 133 53.664-111.112 239.232 1.00 72.67 N ANISOU 461 N ASP A 133 10194 8487 8929 -530 -740 2482 N ATOM 462 CA ASP A 133 53.702-110.484 237.915 1.00 78.15 C ANISOU 462 CA ASP A 133 11168 9193 9332 -599 -808 2751 C ATOM 463 C ASP A 133 54.798-111.082 237.045 1.00 73.08 C ANISOU 463 C ASP A 133 10597 8862 8306 -796 -654 2670 C ATOM 464 O ASP A 133 54.596-111.291 235.844 1.00 75.54 O ANISOU 464 O ASP A 133 11091 9320 8289 -799 -775 2788 O ATOM 465 CB ASP A 133 53.906-108.974 238.048 1.00 90.42 C ANISOU 465 CB ASP A 133 12943 10429 10983 -683 -698 2987 C ATOM 466 CG ASP A 133 52.629-108.238 238.391 1.00101.37 C ANISOU 466 CG ASP A 133 14351 11493 12674 -437 -897 3156 C ATOM 467 OD1 ASP A 133 51.544-108.851 238.305 1.00105.55 O ANISOU 467 OD1 ASP A 133 14721 12080 13301 -215 -1146 3135 O ATOM 468 OD2 ASP A 133 52.711-107.044 238.750 1.00106.78 O ANISOU 468 OD2 ASP A 133 15197 11853 13523 -467 -796 3298 O ATOM 469 N TYR A 134 55.962-111.370 237.631 1.00 62.00 N ANISOU 469 N TYR A 134 9049 7571 6936 -952 -389 2460 N ATOM 470 CA TYR A 134 57.099-111.861 236.859 1.00 57.15 C ANISOU 470 CA TYR A 134 8458 7246 6009 -1132 -179 2368 C ATOM 471 C TYR A 134 56.873-113.247 236.265 1.00 62.54 C ANISOU 471 C TYR A 134 9071 8198 6494 -1020 -289 2181 C ATOM 472 O TYR A 134 57.740-113.726 235.524 1.00 72.35 O ANISOU 472 O TYR A 134 10349 9685 7455 -1137 -104 2083 O ATOM 473 CB TYR A 134 58.362-111.862 237.724 1.00 56.00 C ANISOU 473 CB TYR A 134 8099 7157 6021 -1296 92 2173 C ATOM 474 CG TYR A 134 58.169-112.423 239.114 1.00 50.94 C ANISOU 474 CG TYR A 134 7193 6455 5705 -1160 18 1949 C ATOM 475 CD1 TYR A 134 58.296-113.784 239.358 1.00 49.72 C ANISOU 475 CD1 TYR A 134 6830 6504 5557 -1042 -17 1698 C ATOM 476 CD2 TYR A 134 57.871-111.589 240.186 1.00 49.25 C ANISOU 476 CD2 TYR A 134 6976 5962 5774 -1151 -3 1989 C ATOM 477 CE1 TYR A 134 58.125-114.300 240.628 1.00 48.91 C ANISOU 477 CE1 TYR A 134 6534 6334 5716 -925 -80 1527 C ATOM 478 CE2 TYR A 134 57.697-112.097 241.461 1.00 46.50 C ANISOU 478 CE2 TYR A 134 6436 5568 5665 -1038 -53 1792 C ATOM 479 CZ TYR A 134 57.828-113.454 241.676 1.00 48.33 C ANISOU 479 CZ TYR A 134 6473 6011 5878 -930 -94 1579 C ATOM 480 OH TYR A 134 57.657-113.968 242.939 1.00 53.62 O ANISOU 480 OH TYR A 134 6999 6625 6752 -824 -139 1416 O ATOM 481 N ILE A 135 55.754-113.898 236.564 1.00 55.32 N ANISOU 481 N ILE A 135 8055 7234 5729 -812 -560 2114 N ATOM 482 CA ILE A 135 55.357-115.135 235.904 1.00 55.18 C ANISOU 482 CA ILE A 135 8020 7417 5526 -723 -715 1954 C ATOM 483 C ILE A 135 54.335-114.763 234.838 1.00 58.25 C ANISOU 483 C ILE A 135 8651 7782 5700 -665 -1007 2188 C ATOM 484 O ILE A 135 53.193-114.410 235.152 1.00 60.21 O ANISOU 484 O ILE A 135 8847 7846 6183 -520 -1265 2319 O ATOM 485 CB ILE A 135 54.789-116.156 236.898 1.00 58.88 C ANISOU 485 CB ILE A 135 8219 7847 6307 -568 -829 1729 C ATOM 486 CG1 ILE A 135 55.805-116.441 238.005 1.00 53.81 C ANISOU 486 CG1 ILE A 135 7371 7215 5858 -608 -585 1537 C ATOM 487 CG2 ILE A 135 54.424-117.440 236.178 1.00 57.17 C ANISOU 487 CG2 ILE A 135 8008 7803 5909 -510 -982 1547 C ATOM 488 CD1 ILE A 135 57.118-116.997 237.498 1.00 53.78 C ANISOU 488 CD1 ILE A 135 7350 7455 5631 -714 -348 1370 C ATOM 489 N TYR A 136 54.750-114.846 233.571 1.00 60.75 N ANISOU 489 N TYR A 136 9228 8291 5562 -773 -968 2239 N ATOM 490 CA TYR A 136 53.942-114.315 232.477 1.00 63.00 C ANISOU 490 CA TYR A 136 9814 8560 5562 -744 -1251 2513 C ATOM 491 C TYR A 136 52.658-115.110 232.266 1.00 66.17 C ANISOU 491 C TYR A 136 10128 8993 6020 -575 -1672 2433 C ATOM 492 O TYR A 136 51.623-114.532 231.918 1.00 66.52 O ANISOU 492 O TYR A 136 10260 8923 6091 -466 -2010 2677 O ATOM 493 CB TYR A 136 54.771-114.288 231.192 1.00 68.77 C ANISOU 493 CB TYR A 136 10883 9515 5733 -922 -1068 2564 C ATOM 494 CG TYR A 136 54.052-113.705 229.998 1.00 73.14 C ANISOU 494 CG TYR A 136 11823 10066 5901 -910 -1363 2877 C ATOM 495 CD1 TYR A 136 53.969-112.332 229.818 1.00 75.05 C ANISOU 495 CD1 TYR A 136 12301 10094 6121 -949 -1371 3270 C ATOM 496 CD2 TYR A 136 53.470-114.528 229.043 1.00 78.58 C ANISOU 496 CD2 TYR A 136 12667 10953 6235 -863 -1653 2783 C ATOM 497 CE1 TYR A 136 53.317-111.793 228.725 1.00 83.14 C ANISOU 497 CE1 TYR A 136 13617 11098 6873 -864 -1615 3499 C ATOM 498 CE2 TYR A 136 52.816-113.999 227.947 1.00 82.04 C ANISOU 498 CE2 TYR A 136 13444 11400 6326 -828 -1948 3047 C ATOM 499 CZ TYR A 136 52.743-112.631 227.793 1.00 84.88 C ANISOU 499 CZ TYR A 136 13939 11542 6769 -791 -1897 3375 C ATOM 500 OH TYR A 136 52.093-112.100 226.702 1.00 89.60 O ANISOU 500 OH TYR A 136 14781 12139 7122 -685 -2136 3572 O ATOM 501 N ASP A 137 52.698-116.424 232.469 1.00 72.70 N ANISOU 501 N ASP A 137 10773 9958 6890 -550 -1670 2099 N ATOM 502 CA ASP A 137 51.571-117.287 232.138 1.00 76.62 C ANISOU 502 CA ASP A 137 11203 10504 7406 -450 -2055 1987 C ATOM 503 C ASP A 137 50.573-117.448 233.277 1.00 74.71 C ANISOU 503 C ASP A 137 10606 10069 7712 -305 -2218 1952 C ATOM 504 O ASP A 137 49.616-118.215 233.133 1.00 80.26 O ANISOU 504 O ASP A 137 11183 10799 8512 -246 -2518 1840 O ATOM 505 CB ASP A 137 52.076-118.666 231.702 1.00 84.27 C ANISOU 505 CB ASP A 137 12199 11684 8138 -512 -1966 1632 C ATOM 506 CG ASP A 137 53.067-118.586 230.560 1.00 96.27 C ANISOU 506 CG ASP A 137 14063 13415 9099 -652 -1748 1627 C ATOM 507 OD1 ASP A 137 54.222-118.180 230.805 1.00 99.52 O ANISOU 507 OD1 ASP A 137 14474 13854 9485 -740 -1348 1637 O ATOM 508 OD2 ASP A 137 52.694-118.928 229.417 1.00104.11 O ANISOU 508 OD2 ASP A 137 15327 14557 9675 -685 -1970 1604 O ATOM 509 N PHE A 138 50.762-116.751 234.394 1.00 64.76 N ANISOU 509 N PHE A 138 9187 8616 6803 -264 -2018 2033 N ATOM 510 CA PHE A 138 49.847-116.872 235.519 1.00 62.27 C ANISOU 510 CA PHE A 138 8557 8119 6982 -132 -2104 1994 C ATOM 511 C PHE A 138 48.625-115.980 235.334 1.00 62.07 C ANISOU 511 C PHE A 138 8500 7942 7141 9 -2412 2265 C ATOM 512 O PHE A 138 48.669-114.958 234.645 1.00 62.89 O ANISOU 512 O PHE A 138 8843 8000 7052 15 -2491 2537 O ATOM 513 CB PHE A 138 50.547-116.507 236.830 1.00 62.61 C ANISOU 513 CB PHE A 138 8476 8020 7294 -142 -1765 1943 C ATOM 514 CG PHE A 138 51.221-117.667 237.504 1.00 60.26 C ANISOU 514 CG PHE A 138 8036 7809 7052 -184 -1569 1644 C ATOM 515 CD1 PHE A 138 51.146-118.942 236.966 1.00 62.97 C ANISOU 515 CD1 PHE A 138 8368 8306 7252 -201 -1672 1432 C ATOM 516 CD2 PHE A 138 51.919-117.484 238.686 1.00 54.35 C ANISOU 516 CD2 PHE A 138 7184 6967 6499 -199 -1306 1574 C ATOM 517 CE1 PHE A 138 51.764-120.010 237.591 1.00 56.58 C ANISOU 517 CE1 PHE A 138 7447 7533 6516 -210 -1501 1176 C ATOM 518 CE2 PHE A 138 52.537-118.548 239.315 1.00 48.58 C ANISOU 518 CE2 PHE A 138 6335 6305 5819 -209 -1166 1330 C ATOM 519 CZ PHE A 138 52.459-119.812 238.767 1.00 47.86 C ANISOU 519 CZ PHE A 138 6234 6343 5608 -202 -1256 1141 C ATOM 520 N ASN A 139 47.523-116.384 235.962 1.00 61.84 N ANISOU 520 N ASN A 139 8165 7826 7507 128 -2576 2198 N ATOM 521 CA ASN A 139 46.330-115.547 236.058 1.00 63.35 C ANISOU 521 CA ASN A 139 8216 7847 8009 306 -2820 2425 C ATOM 522 C ASN A 139 46.603-114.470 237.100 1.00 68.98 C ANISOU 522 C ASN A 139 8910 8304 8993 377 -2528 2535 C ATOM 523 O ASN A 139 46.566-114.730 238.305 1.00 71.52 O ANISOU 523 O ASN A 139 9021 8525 9627 400 -2302 2379 O ATOM 524 CB ASN A 139 45.112-116.385 236.429 1.00 66.97 C ANISOU 524 CB ASN A 139 8302 8310 8832 384 -3034 2286 C ATOM 525 CG ASN A 139 43.918-115.540 236.827 1.00 75.75 C ANISOU 525 CG ASN A 139 9169 9232 10379 593 -3161 2455 C ATOM 526 OD1 ASN A 139 43.722-114.438 236.314 1.00 81.94 O ANISOU 526 OD1 ASN A 139 10106 9936 11091 697 -3221 2655 O ATOM 527 ND2 ASN A 139 43.116-116.051 237.753 1.00 78.53 N ANISOU 527 ND2 ASN A 139 9151 9515 11172 647 -3098 2313 N ATOM 528 N HIS A 140 46.881-113.253 236.640 1.00 66.77 N ANISOU 528 N HIS A 140 8887 7904 8578 400 -2531 2805 N ATOM 529 CA HIS A 140 47.310-112.180 237.527 1.00 63.14 C ANISOU 529 CA HIS A 140 8487 7183 8321 423 -2240 2890 C ATOM 530 C HIS A 140 46.155-111.497 238.247 1.00 66.28 C ANISOU 530 C HIS A 140 8664 7320 9199 662 -2298 2969 C ATOM 531 O HIS A 140 46.364-110.444 238.858 1.00 71.68 O ANISOU 531 O HIS A 140 9444 7752 10038 707 -2079 3035 O ATOM 532 CB HIS A 140 48.130-111.154 236.743 1.00 60.74 C ANISOU 532 CB HIS A 140 8572 6820 7687 317 -2177 3136 C ATOM 533 CG HIS A 140 49.365-111.728 236.122 1.00 72.24 C ANISOU 533 CG HIS A 140 10222 8533 8692 74 -2009 3025 C ATOM 534 ND1 HIS A 140 49.433-112.086 234.793 1.00 78.62 N ANISOU 534 ND1 HIS A 140 11244 9563 9064 6 -2204 3102 N ATOM 535 CD2 HIS A 140 50.574-112.025 236.654 1.00 71.65 C ANISOU 535 CD2 HIS A 140 10143 8539 8543 -106 -1663 2827 C ATOM 536 CE1 HIS A 140 50.635-112.567 234.530 1.00 78.17 C ANISOU 536 CE1 HIS A 140 11304 9705 8694 -200 -1938 2948 C ATOM 537 NE2 HIS A 140 51.347-112.543 235.643 1.00 74.17 N ANISOU 537 NE2 HIS A 140 10642 9119 8421 -264 -1621 2786 N ATOM 538 N LYS A 141 44.953-112.066 238.196 1.00 64.36 N ANISOU 538 N LYS A 141 8123 7152 9181 797 -2513 2880 N ATOM 539 CA LYS A 141 43.835-111.586 238.995 1.00 69.64 C ANISOU 539 CA LYS A 141 8513 7632 10315 1007 -2459 2845 C ATOM 540 C LYS A 141 43.535-112.492 240.181 1.00 65.58 C ANISOU 540 C LYS A 141 7676 7119 10124 997 -2287 2625 C ATOM 541 O LYS A 141 42.649-112.172 240.980 1.00 66.54 O ANISOU 541 O LYS A 141 7557 7095 10630 1149 -2169 2569 O ATOM 542 CB LYS A 141 42.583-111.440 238.124 1.00 78.66 C ANISOU 542 CB LYS A 141 9513 8845 11529 1168 -2798 2922 C ATOM 543 CG LYS A 141 42.801-110.610 236.871 1.00 92.65 C ANISOU 543 CG LYS A 141 11629 10628 12948 1195 -2992 3158 C ATOM 544 CD LYS A 141 41.491-110.062 236.329 1.00107.29 C ANISOU 544 CD LYS A 141 13333 12450 14982 1434 -3272 3269 C ATOM 545 CE LYS A 141 40.885-109.047 237.286 1.00110.82 C ANISOU 545 CE LYS A 141 13634 12602 15868 1657 -3077 3295 C ATOM 546 NZ LYS A 141 39.644-108.431 236.738 1.00112.43 N ANISOU 546 NZ LYS A 141 13693 12769 16255 1919 -3353 3425 N ATOM 547 N GLY A 142 44.254-113.608 240.319 1.00 60.89 N ANISOU 547 N GLY A 142 7088 6687 9359 821 -2235 2480 N ATOM 548 CA GLY A 142 44.038-114.538 241.403 1.00 59.13 C ANISOU 548 CA GLY A 142 6622 6480 9363 781 -2025 2238 C ATOM 549 C GLY A 142 45.111-114.446 242.479 1.00 58.58 C ANISOU 549 C GLY A 142 6709 6333 9214 680 -1632 2106 C ATOM 550 O GLY A 142 46.024-113.626 242.434 1.00 60.18 O ANISOU 550 O GLY A 142 7174 6465 9228 625 -1511 2182 O ATOM 551 N HIS A 143 44.982-115.330 243.467 1.00 57.52 N ANISOU 551 N HIS A 143 6414 6212 9228 638 -1445 1909 N ATOM 552 CA HIS A 143 45.890-115.354 244.604 1.00 53.56 C ANISOU 552 CA HIS A 143 6042 5649 8660 556 -1117 1775 C ATOM 553 C HIS A 143 46.316-116.783 244.902 1.00 54.15 C ANISOU 553 C HIS A 143 6079 5878 8617 430 -1063 1581 C ATOM 554 O HIS A 143 45.545-117.730 244.723 1.00 56.26 O ANISOU 554 O HIS A 143 6152 6212 9014 426 -1180 1519 O ATOM 555 CB HIS A 143 45.247-114.746 245.859 1.00 53.29 C ANISOU 555 CB HIS A 143 5911 5386 8952 678 -869 1753 C ATOM 556 CG HIS A 143 45.000-113.273 245.763 1.00 60.49 C ANISOU 556 CG HIS A 143 6910 6079 9993 818 -859 1915 C ATOM 557 ND1 HIS A 143 44.041-112.731 244.935 1.00 64.61 N ANISOU 557 ND1 HIS A 143 7300 6543 10706 986 -1104 2098 N ATOM 558 CD2 HIS A 143 45.583-112.229 246.397 1.00 59.86 C ANISOU 558 CD2 HIS A 143 7050 5801 9893 818 -650 1919 C ATOM 559 CE1 HIS A 143 44.047-111.416 245.060 1.00 65.74 C ANISOU 559 CE1 HIS A 143 7588 6439 10949 1104 -1031 2224 C ATOM 560 NE2 HIS A 143 44.973-111.086 245.942 1.00 63.99 N ANISOU 560 NE2 HIS A 143 7589 6121 10603 991 -745 2106 N ATOM 561 N ALA A 144 47.559-116.926 245.353 1.00 44.55 N ANISOU 561 N ALA A 144 5045 4707 7176 326 -899 1486 N ATOM 562 CA ALA A 144 48.036-118.164 245.948 1.00 44.08 C ANISOU 562 CA ALA A 144 4974 4729 7045 249 -805 1313 C ATOM 563 C ALA A 144 47.817-118.112 247.455 1.00 44.68 C ANISOU 563 C ALA A 144 5036 4653 7289 281 -554 1251 C ATOM 564 O ALA A 144 47.760-117.034 248.053 1.00 44.08 O ANISOU 564 O ALA A 144 5026 4431 7292 331 -418 1299 O ATOM 565 CB ALA A 144 49.515-118.388 245.631 1.00 31.87 C ANISOU 565 CB ALA A 144 3597 3327 5184 146 -783 1243 C ATOM 566 N TYR A 145 47.691-119.287 248.070 1.00 45.71 N ANISOU 566 N TYR A 145 5113 4799 7457 248 -484 1143 N ATOM 567 CA TYR A 145 47.270-119.375 249.461 1.00 47.76 C ANISOU 567 CA TYR A 145 5371 4919 7858 271 -240 1101 C ATOM 568 C TYR A 145 48.211-120.254 250.273 1.00 48.67 C ANISOU 568 C TYR A 145 5643 5068 7780 207 -149 1000 C ATOM 569 O TYR A 145 48.814-121.199 249.757 1.00 47.85 O ANISOU 569 O TYR A 145 5560 5077 7545 163 -274 944 O ATOM 570 CB TYR A 145 45.839-119.922 249.578 1.00 55.46 C ANISOU 570 CB TYR A 145 6101 5829 9144 300 -209 1113 C ATOM 571 CG TYR A 145 44.807-119.097 248.845 1.00 64.56 C ANISOU 571 CG TYR A 145 7042 6947 10539 400 -333 1220 C ATOM 572 CD1 TYR A 145 44.272-117.950 249.417 1.00 67.41 C ANISOU 572 CD1 TYR A 145 7369 7153 11090 522 -165 1276 C ATOM 573 CD2 TYR A 145 44.364-119.467 247.582 1.00 74.15 C ANISOU 573 CD2 TYR A 145 8106 8277 11792 386 -636 1258 C ATOM 574 CE1 TYR A 145 43.328-117.192 248.751 1.00 72.28 C ANISOU 574 CE1 TYR A 145 7779 7721 11964 655 -302 1389 C ATOM 575 CE2 TYR A 145 43.420-118.714 246.906 1.00 79.63 C ANISOU 575 CE2 TYR A 145 8604 8946 12705 498 -806 1377 C ATOM 576 CZ TYR A 145 42.905-117.579 247.497 1.00 76.22 C ANISOU 576 CZ TYR A 145 8115 8351 12496 646 -641 1453 C ATOM 577 OH TYR A 145 41.965-116.826 246.831 1.00 74.03 O ANISOU 577 OH TYR A 145 7629 8031 12469 798 -831 1586 O ATOM 578 N ARG A 146 48.323-119.922 251.557 1.00 47.35 N ANISOU 578 N ARG A 146 5604 4795 7592 216 65 973 N ATOM 579 CA ARG A 146 49.014-120.742 252.542 1.00 36.76 C ANISOU 579 CA ARG A 146 4427 3458 6083 177 146 906 C ATOM 580 C ARG A 146 48.284-120.611 253.871 1.00 44.99 C ANISOU 580 C ARG A 146 5546 4347 7200 193 417 903 C ATOM 581 O ARG A 146 47.427-119.742 254.051 1.00 48.74 O ANISOU 581 O ARG A 146 5946 4719 7854 244 562 927 O ATOM 582 CB ARG A 146 50.483-120.334 252.707 1.00 32.58 C ANISOU 582 CB ARG A 146 4063 3019 5296 145 73 858 C ATOM 583 CG ARG A 146 51.474-121.103 251.852 1.00 31.15 C ANISOU 583 CG ARG A 146 3847 3003 4983 126 -118 819 C ATOM 584 CD ARG A 146 52.888-120.881 252.370 1.00 30.98 C ANISOU 584 CD ARG A 146 3946 3069 4757 96 -156 758 C ATOM 585 NE ARG A 146 53.913-121.428 251.485 1.00 33.30 N ANISOU 585 NE ARG A 146 4162 3534 4954 93 -300 708 N ATOM 586 CZ ARG A 146 55.211-121.449 251.776 1.00 38.79 C ANISOU 586 CZ ARG A 146 4877 4343 5517 79 -362 645 C ATOM 587 NH1 ARG A 146 55.640-120.961 252.934 1.00 27.55 N ANISOU 587 NH1 ARG A 146 3574 2881 4015 50 -336 624 N ATOM 588 NH2 ARG A 146 56.080-121.962 250.916 1.00 33.24 N ANISOU 588 NH2 ARG A 146 4067 3799 4763 95 -449 587 N ATOM 589 N ARG A 147 48.635-121.486 254.810 1.00 47.88 N ANISOU 589 N ARG A 147 6078 4692 7421 161 497 878 N ATOM 590 CA ARG A 147 48.109-121.423 256.165 1.00 51.09 C ANISOU 590 CA ARG A 147 6638 4969 7804 157 781 875 C ATOM 591 C ARG A 147 49.254-121.501 257.163 1.00 51.16 C ANISOU 591 C ARG A 147 6959 5003 7477 136 760 835 C ATOM 592 O ARG A 147 50.252-122.191 256.940 1.00 49.31 O ANISOU 592 O ARG A 147 6775 4867 7092 133 548 830 O ATOM 593 CB ARG A 147 47.103-122.544 256.445 1.00 61.04 C ANISOU 593 CB ARG A 147 7814 6148 9230 116 933 923 C ATOM 594 CG ARG A 147 45.805-122.414 255.674 1.00 71.33 C ANISOU 594 CG ARG A 147 8774 7423 10905 124 970 950 C ATOM 595 CD ARG A 147 44.738-123.337 256.236 1.00 81.31 C ANISOU 595 CD ARG A 147 9950 8584 12362 47 1209 985 C ATOM 596 NE ARG A 147 43.523-123.312 255.429 1.00 86.83 N ANISOU 596 NE ARG A 147 10256 9282 13453 39 1187 1000 N ATOM 597 CZ ARG A 147 43.267-124.164 254.443 1.00 90.47 C ANISOU 597 CZ ARG A 147 10524 9791 14061 -33 954 1000 C ATOM 598 NH1 ARG A 147 44.141-125.116 254.143 1.00 87.75 N ANISOU 598 NH1 ARG A 147 10354 9476 13512 -86 764 978 N ATOM 599 NH2 ARG A 147 42.136-124.067 253.759 1.00 96.32 N ANISOU 599 NH2 ARG A 147 10892 10545 15159 -45 898 1008 N ATOM 600 N CYS A 148 49.091-120.784 258.270 1.00 56.61 N ANISOU 600 N CYS A 148 7853 5603 8054 132 975 795 N ATOM 601 CA CYS A 148 50.085-120.716 259.332 1.00 57.24 C ANISOU 601 CA CYS A 148 8256 5705 7789 103 939 745 C ATOM 602 C CYS A 148 49.546-121.433 260.564 1.00 59.21 C ANISOU 602 C CYS A 148 8745 5855 7900 84 1183 788 C ATOM 603 O CYS A 148 48.398-121.207 260.963 1.00 58.38 O ANISOU 603 O CYS A 148 8615 5632 7934 84 1507 792 O ATOM 604 CB CYS A 148 50.426-119.256 259.651 1.00 54.27 C ANISOU 604 CB CYS A 148 7999 5293 7327 84 977 640 C ATOM 605 SG CYS A 148 51.757-119.013 260.845 1.00 60.58 S ANISOU 605 SG CYS A 148 9170 6149 7698 14 841 542 S ATOM 606 N ASP A 149 50.366-122.302 261.153 1.00 66.82 N ANISOU 606 N ASP A 149 9932 6860 8595 76 1036 829 N ATOM 607 CA ASP A 149 49.942-123.071 262.315 1.00 75.46 C ANISOU 607 CA ASP A 149 11316 7851 9504 49 1250 909 C ATOM 608 C ASP A 149 49.690-122.163 263.513 1.00 71.85 C ANISOU 608 C ASP A 149 11163 7329 8809 16 1513 828 C ATOM 609 O ASP A 149 50.135-121.014 263.564 1.00 70.44 O ANISOU 609 O ASP A 149 11026 7183 8555 14 1453 698 O ATOM 610 CB ASP A 149 50.992-124.116 262.699 1.00 85.55 C ANISOU 610 CB ASP A 149 12807 9177 10522 79 979 989 C ATOM 611 CG ASP A 149 50.904-125.370 261.859 1.00 97.98 C ANISOU 611 CG ASP A 149 14189 10723 12314 110 859 1082 C ATOM 612 OD1 ASP A 149 49.812-125.655 261.325 1.00104.45 O ANISOU 612 OD1 ASP A 149 14798 11458 13428 64 1050 1110 O ATOM 613 OD2 ASP A 149 51.927-126.078 261.743 1.00102.38 O ANISOU 613 OD2 ASP A 149 14801 11337 12761 183 566 1114 O ATOM 614 N ARG A 150 48.973-122.709 264.498 1.00 75.56 N ANISOU 614 N ARG A 150 11873 7689 9146 -24 1829 902 N ATOM 615 CA ARG A 150 48.780-121.996 265.754 1.00 75.25 C ANISOU 615 CA ARG A 150 12205 7590 8796 -57 2107 816 C ATOM 616 C ARG A 150 50.103-121.774 266.473 1.00 65.28 C ANISOU 616 C ARG A 150 11307 6420 7077 -67 1793 760 C ATOM 617 O ARG A 150 50.244-120.809 267.233 1.00 73.74 O ANISOU 617 O ARG A 150 12643 7473 7900 -101 1892 612 O ATOM 618 CB ARG A 150 47.810-122.768 266.648 1.00 90.59 C ANISOU 618 CB ARG A 150 14358 9411 10650 -117 2525 930 C ATOM 619 CG ARG A 150 46.516-123.171 265.959 1.00100.09 C ANISOU 619 CG ARG A 150 15155 10536 12341 -137 2805 995 C ATOM 620 CD ARG A 150 45.709-124.131 266.822 1.00114.24 C ANISOU 620 CD ARG A 150 17153 12208 14044 -239 3198 1137 C ATOM 621 NE ARG A 150 46.392-125.409 267.012 1.00120.94 N ANISOU 621 NE ARG A 150 18245 13037 14671 -272 2951 1316 N ATOM 622 CZ ARG A 150 46.118-126.513 266.324 1.00121.18 C ANISOU 622 CZ ARG A 150 18056 13003 14985 -314 2867 1444 C ATOM 623 NH1 ARG A 150 45.169-126.502 265.398 1.00121.10 N ANISOU 623 NH1 ARG A 150 17565 12974 15474 -350 2987 1408 N ATOM 624 NH2 ARG A 150 46.791-127.630 266.563 1.00120.22 N ANISOU 624 NH2 ARG A 150 18202 12823 14653 -315 2645 1602 N ATOM 625 N ASN A 151 51.083-122.651 266.244 1.00 68.42 N ANISOU 625 N ASN A 151 11711 6911 7374 -34 1403 862 N ATOM 626 CA ASN A 151 52.401-122.474 266.843 1.00 81.33 C ANISOU 626 CA ASN A 151 13608 8664 8630 -32 1035 812 C ATOM 627 C ASN A 151 53.216-121.427 266.096 1.00 70.63 C ANISOU 627 C ASN A 151 12000 7428 7410 -46 767 646 C ATOM 628 O ASN A 151 53.979-120.675 266.712 1.00 77.75 O ANISOU 628 O ASN A 151 13112 8392 8038 -104 601 514 O ATOM 629 CB ASN A 151 53.155-123.803 266.862 1.00101.70 C ANISOU 629 CB ASN A 151 16249 11289 11103 44 714 986 C ATOM 630 CG ASN A 151 52.366-124.912 267.522 1.00120.61 C ANISOU 630 CG ASN A 151 18909 13527 13388 38 978 1184 C ATOM 631 OD1 ASN A 151 51.690-124.699 268.528 1.00113.09 O ANISOU 631 OD1 ASN A 151 18299 12485 12183 -36 1319 1193 O ATOM 632 ND2 ASN A 151 52.447-126.108 266.954 1.00143.25 N ANISOU 632 ND2 ASN A 151 21638 16345 16447 104 846 1338 N ATOM 633 N GLY A 152 53.073-121.369 264.776 1.00 66.02 N ANISOU 633 N GLY A 152 10984 6873 7228 -14 719 652 N ATOM 634 CA GLY A 152 53.841-120.441 263.972 1.00 55.89 C ANISOU 634 CA GLY A 152 9462 5693 6080 -44 495 530 C ATOM 635 C GLY A 152 54.669-121.140 262.914 1.00 54.84 C ANISOU 635 C GLY A 152 9018 5705 6116 13 177 591 C ATOM 636 O GLY A 152 55.781-120.709 262.597 1.00 56.67 O ANISOU 636 O GLY A 152 9135 6075 6322 -20 -98 511 O ATOM 637 N SER A 153 54.136-122.228 262.367 1.00 48.83 N ANISOU 637 N SER A 153 8115 4905 5535 87 232 717 N ATOM 638 CA SER A 153 54.783-122.990 261.309 1.00 51.87 C ANISOU 638 CA SER A 153 8222 5397 6090 159 -12 754 C ATOM 639 C SER A 153 53.853-123.070 260.106 1.00 46.03 C ANISOU 639 C SER A 153 7191 4610 5687 162 134 777 C ATOM 640 O SER A 153 52.630-123.136 260.258 1.00 45.63 O ANISOU 640 O SER A 153 7159 4425 5755 140 404 823 O ATOM 641 CB SER A 153 55.155-124.400 261.784 1.00 59.45 C ANISOU 641 CB SER A 153 9332 6332 6926 258 -152 873 C ATOM 642 OG SER A 153 56.107-124.353 262.832 1.00 70.04 O ANISOU 642 OG SER A 153 10926 7742 7943 276 -368 867 O ATOM 643 N TRP A 154 54.431-123.044 258.909 1.00 40.79 N ANISOU 643 N TRP A 154 6253 4069 5174 182 -43 739 N ATOM 644 CA TRP A 154 53.622-123.147 257.701 1.00 39.80 C ANISOU 644 CA TRP A 154 5878 3923 5321 182 33 758 C ATOM 645 C TRP A 154 52.968-124.522 257.630 1.00 38.60 C ANISOU 645 C TRP A 154 5728 3667 5269 224 84 837 C ATOM 646 O TRP A 154 53.617-125.542 257.882 1.00 37.73 O ANISOU 646 O TRP A 154 5712 3556 5067 292 -51 867 O ATOM 647 CB TRP A 154 54.475-122.894 256.459 1.00 35.22 C ANISOU 647 CB TRP A 154 5065 3508 4810 185 -157 701 C ATOM 648 CG TRP A 154 54.922-121.466 256.312 1.00 33.62 C ANISOU 648 CG TRP A 154 4831 3367 4575 101 -166 641 C ATOM 649 CD1 TRP A 154 56.200-120.994 256.388 1.00 34.17 C ANISOU 649 CD1 TRP A 154 4882 3573 4528 53 -325 570 C ATOM 650 CD2 TRP A 154 54.087-120.327 256.067 1.00 31.46 C ANISOU 650 CD2 TRP A 154 4537 2998 4418 49 -11 649 C ATOM 651 NE1 TRP A 154 56.214-119.633 256.202 1.00 33.68 N ANISOU 651 NE1 TRP A 154 4817 3488 4493 -55 -265 533 N ATOM 652 CE2 TRP A 154 54.929-119.199 256.003 1.00 32.87 C ANISOU 652 CE2 TRP A 154 4730 3232 4529 -40 -75 586 C ATOM 653 CE3 TRP A 154 52.711-120.153 255.895 1.00 32.12 C ANISOU 653 CE3 TRP A 154 4571 2946 4686 76 171 704 C ATOM 654 CZ2 TRP A 154 54.439-117.914 255.777 1.00 34.21 C ANISOU 654 CZ2 TRP A 154 4916 3289 4795 -93 40 587 C ATOM 655 CZ3 TRP A 154 52.226-118.878 255.670 1.00 37.43 C ANISOU 655 CZ3 TRP A 154 5223 3532 5466 56 271 703 C ATOM 656 CH2 TRP A 154 53.088-117.775 255.612 1.00 37.81 C ANISOU 656 CH2 TRP A 154 5336 3602 5429 -22 208 651 C ATOM 657 N GLU A 155 51.677-124.544 257.303 1.00 34.85 N ANISOU 657 N GLU A 155 5144 3089 5008 182 272 871 N ATOM 658 CA GLU A 155 50.929-125.795 257.256 1.00 36.07 C ANISOU 658 CA GLU A 155 5289 3118 5296 170 345 936 C ATOM 659 C GLU A 155 51.540-126.750 256.238 1.00 36.24 C ANISOU 659 C GLU A 155 5198 3193 5378 222 116 901 C ATOM 660 O GLU A 155 51.871-126.354 255.117 1.00 42.92 O ANISOU 660 O GLU A 155 5851 4172 6285 234 -19 828 O ATOM 661 CB GLU A 155 49.465-125.513 256.921 1.00 48.57 C ANISOU 661 CB GLU A 155 6680 4620 7152 101 551 954 C ATOM 662 CG GLU A 155 48.598-126.751 256.778 1.00 63.17 C ANISOU 662 CG GLU A 155 8469 6337 9197 37 630 1005 C ATOM 663 CD GLU A 155 47.117-126.427 256.805 1.00 73.47 C ANISOU 663 CD GLU A 155 9572 7562 10779 -43 876 1028 C ATOM 664 OE1 GLU A 155 46.709-125.582 257.630 1.00 71.66 O ANISOU 664 OE1 GLU A 155 9407 7302 10517 -38 1115 1039 O ATOM 665 OE2 GLU A 155 46.364-127.008 255.996 1.00 77.21 O ANISOU 665 OE2 GLU A 155 9813 8006 11517 -110 827 1018 O ATOM 666 N LEU A 156 51.689-128.010 256.634 1.00 44.65 N ANISOU 666 N LEU A 156 6413 4137 6415 256 91 953 N ATOM 667 CA LEU A 156 52.401-129.010 255.851 1.00 38.99 C ANISOU 667 CA LEU A 156 5647 3432 5737 341 -111 900 C ATOM 668 C LEU A 156 51.446-129.847 255.008 1.00 40.82 C ANISOU 668 C LEU A 156 5757 3541 6212 265 -74 874 C ATOM 669 O LEU A 156 50.237-129.897 255.249 1.00 42.09 O ANISOU 669 O LEU A 156 5885 3582 6524 143 108 928 O ATOM 670 CB LEU A 156 53.211-129.934 256.764 1.00 33.99 C ANISOU 670 CB LEU A 156 5270 2699 4944 454 -199 975 C ATOM 671 CG LEU A 156 54.164-129.282 257.765 1.00 38.72 C ANISOU 671 CG LEU A 156 6023 3409 5279 520 -288 1006 C ATOM 672 CD1 LEU A 156 54.871-130.346 258.589 1.00 36.60 C ANISOU 672 CD1 LEU A 156 6008 3027 4872 656 -426 1107 C ATOM 673 CD2 LEU A 156 55.167-128.406 257.050 1.00 32.97 C ANISOU 673 CD2 LEU A 156 5073 2928 4527 558 -455 880 C ATOM 674 N VAL A 157 52.014-130.514 254.013 1.00 42.35 N ANISOU 674 N VAL A 157 5874 3768 6449 332 -245 771 N ATOM 675 CA VAL A 157 51.265-131.487 253.216 1.00 41.72 C ANISOU 675 CA VAL A 157 5731 3550 6572 256 -258 710 C ATOM 676 C VAL A 157 51.130-132.776 254.022 1.00 42.28 C ANISOU 676 C VAL A 157 6039 3340 6684 260 -193 797 C ATOM 677 O VAL A 157 52.134-133.265 254.562 1.00 54.34 O ANISOU 677 O VAL A 157 7750 4822 8075 416 -278 836 O ATOM 678 CB VAL A 157 51.965-131.744 251.885 1.00 40.90 C ANISOU 678 CB VAL A 157 5515 3569 6456 331 -439 544 C ATOM 679 CG1 VAL A 157 51.272-132.865 251.125 1.00 34.67 C ANISOU 679 CG1 VAL A 157 4719 2609 5846 247 -476 448 C ATOM 680 CG2 VAL A 157 51.999-130.474 251.053 1.00 31.54 C ANISOU 680 CG2 VAL A 157 4134 2635 5214 297 -483 496 C ATOM 681 N PRO A 158 49.930-133.344 254.137 1.00 42.73 N ANISOU 681 N PRO A 158 6095 3201 6939 91 -53 841 N ATOM 682 CA PRO A 158 49.769-134.564 254.939 1.00 43.90 C ANISOU 682 CA PRO A 158 6510 3045 7127 64 40 953 C ATOM 683 C PRO A 158 50.588-135.718 254.381 1.00 42.35 C ANISOU 683 C PRO A 158 6432 2708 6952 199 -143 862 C ATOM 684 O PRO A 158 50.620-135.958 253.172 1.00 44.96 O ANISOU 684 O PRO A 158 6610 3085 7386 193 -271 677 O ATOM 685 CB PRO A 158 48.265-134.849 254.850 1.00 49.78 C ANISOU 685 CB PRO A 158 7129 3641 8145 -190 224 973 C ATOM 686 CG PRO A 158 47.649-133.528 254.521 1.00 49.66 C ANISOU 686 CG PRO A 158 6819 3869 8180 -248 273 935 C ATOM 687 CD PRO A 158 48.642-132.833 253.642 1.00 47.43 C ANISOU 687 CD PRO A 158 6437 3839 7745 -89 38 813 C ATOM 688 N GLY A 159 51.260-136.434 255.284 1.00 42.36 N ANISOU 688 N GLY A 159 6729 2528 6840 336 -159 992 N ATOM 689 CA GLY A 159 52.051-137.590 254.924 1.00 44.03 C ANISOU 689 CA GLY A 159 7082 2548 7098 509 -315 927 C ATOM 690 C GLY A 159 53.483-137.299 254.532 1.00 42.97 C ANISOU 690 C GLY A 159 6861 2636 6830 783 -524 819 C ATOM 691 O GLY A 159 54.256-138.245 254.336 1.00 44.77 O ANISOU 691 O GLY A 159 7199 2707 7105 984 -645 767 O ATOM 692 N HIS A 160 53.863-136.029 254.404 1.00 40.51 N ANISOU 692 N HIS A 160 6343 2668 6379 797 -557 778 N ATOM 693 CA HIS A 160 55.218-135.661 254.023 1.00 44.62 C ANISOU 693 CA HIS A 160 6728 3427 6797 1015 -726 672 C ATOM 694 C HIS A 160 55.618-134.392 254.761 1.00 42.78 C ANISOU 694 C HIS A 160 6440 3448 6367 1007 -738 759 C ATOM 695 O HIS A 160 54.773-133.614 255.207 1.00 37.48 O ANISOU 695 O HIS A 160 5779 2813 5650 829 -598 839 O ATOM 696 CB HIS A 160 55.350-135.443 252.508 1.00 46.03 C ANISOU 696 CB HIS A 160 6658 3784 7048 998 -759 436 C ATOM 697 CG HIS A 160 54.788-136.559 251.685 1.00 54.08 C ANISOU 697 CG HIS A 160 7739 4566 8242 949 -746 304 C ATOM 698 ND1 HIS A 160 53.454-136.636 251.350 1.00 57.13 N ANISOU 698 ND1 HIS A 160 8110 4846 8753 697 -660 294 N ATOM 699 CD2 HIS A 160 55.378-137.646 251.135 1.00 60.12 C ANISOU 699 CD2 HIS A 160 8580 5168 9095 1116 -813 159 C ATOM 700 CE1 HIS A 160 53.246-137.722 250.627 1.00 62.90 C ANISOU 700 CE1 HIS A 160 8918 5359 9624 682 -694 142 C ATOM 701 NE2 HIS A 160 54.397-138.353 250.482 1.00 64.09 N ANISOU 701 NE2 HIS A 160 9146 5458 9748 941 -773 53 N ATOM 702 N ASN A 161 56.928-134.190 254.878 1.00 42.65 N ANISOU 702 N ASN A 161 6348 3601 6255 1202 -905 723 N ATOM 703 CA ASN A 161 57.469-132.976 255.487 1.00 37.75 C ANISOU 703 CA ASN A 161 5657 3230 5456 1180 -956 763 C ATOM 704 C ASN A 161 57.727-131.919 254.410 1.00 40.17 C ANISOU 704 C ASN A 161 5660 3821 5782 1098 -935 605 C ATOM 705 O ASN A 161 58.854-131.501 254.150 1.00 43.93 O ANISOU 705 O ASN A 161 5954 4514 6223 1191 -1046 520 O ATOM 706 CB ASN A 161 58.733-133.301 256.274 1.00 44.80 C ANISOU 706 CB ASN A 161 6611 4160 6250 1408 -1180 821 C ATOM 707 CG ASN A 161 59.202-132.144 257.135 1.00 50.14 C ANISOU 707 CG ASN A 161 7283 5048 6719 1349 -1260 869 C ATOM 708 OD1 ASN A 161 58.506-131.141 257.288 1.00 44.99 O ANISOU 708 OD1 ASN A 161 6641 4463 5989 1146 -1113 875 O ATOM 709 ND2 ASN A 161 60.387-132.286 257.710 1.00 63.51 N ANISOU 709 ND2 ASN A 161 8958 6837 8336 1534 -1509 892 N ATOM 710 N ARG A 162 56.636-131.502 253.769 1.00 41.58 N ANISOU 710 N ARG A 162 5781 3989 6028 915 -789 577 N ATOM 711 CA ARG A 162 56.658-130.464 252.751 1.00 38.07 C ANISOU 711 CA ARG A 162 5112 3771 5580 816 -758 474 C ATOM 712 C ARG A 162 55.648-129.386 253.113 1.00 43.88 C ANISOU 712 C ARG A 162 5864 4512 6296 638 -633 561 C ATOM 713 O ARG A 162 54.601-129.669 253.700 1.00 46.42 O ANISOU 713 O ARG A 162 6311 4651 6675 563 -522 653 O ATOM 714 CB ARG A 162 56.320-131.015 251.358 1.00 37.05 C ANISOU 714 CB ARG A 162 4885 3634 5557 798 -746 338 C ATOM 715 CG ARG A 162 57.079-132.261 250.958 1.00 44.59 C ANISOU 715 CG ARG A 162 5863 4508 6571 983 -821 223 C ATOM 716 CD ARG A 162 56.509-132.834 249.669 1.00 54.36 C ANISOU 716 CD ARG A 162 7075 5694 7885 925 -796 70 C ATOM 717 NE ARG A 162 57.051-134.154 249.364 1.00 63.13 N ANISOU 717 NE ARG A 162 8264 6643 9078 1102 -837 -57 N ATOM 718 CZ ARG A 162 56.583-134.949 248.408 1.00 67.28 C ANISOU 718 CZ ARG A 162 8844 7046 9675 1066 -829 -216 C ATOM 719 NH1 ARG A 162 55.558-134.558 247.663 1.00 64.31 N ANISOU 719 NH1 ARG A 162 8431 6717 9287 854 -816 -254 N ATOM 720 NH2 ARG A 162 57.135-136.137 248.200 1.00 73.32 N ANISOU 720 NH2 ARG A 162 9704 7627 10525 1250 -852 -346 N ATOM 721 N THR A 163 55.965-128.147 252.747 1.00 59.79 N ANISOU 721 N THR A 163 10755 5620 6343 3172 1924 2341 N ATOM 722 CA THR A 163 55.043-127.046 252.982 1.00 62.47 C ANISOU 722 CA THR A 163 10640 6061 7034 2858 1700 2417 C ATOM 723 C THR A 163 53.897-127.089 251.976 1.00 67.33 C ANISOU 723 C THR A 163 11513 6432 7636 2513 1660 2456 C ATOM 724 O THR A 163 54.104-127.335 250.785 1.00 58.74 O ANISOU 724 O THR A 163 10630 5300 6390 2556 1684 2462 O ATOM 725 CB THR A 163 55.780-125.709 252.890 1.00 61.02 C ANISOU 725 CB THR A 163 9725 6352 7107 2954 1497 2463 C ATOM 726 OG1 THR A 163 56.898-125.717 253.787 1.00 62.30 O ANISOU 726 OG1 THR A 163 9708 6750 7213 3203 1571 2407 O ATOM 727 CG2 THR A 163 54.856-124.563 253.258 1.00 55.88 C ANISOU 727 CG2 THR A 163 8592 5828 6811 2659 1280 2523 C ATOM 728 N TRP A 164 52.681-126.855 252.464 1.00 56.66 N ANISOU 728 N TRP A 164 10163 4934 6431 2138 1613 2476 N ATOM 729 CA TRP A 164 51.491-126.874 251.627 1.00 57.38 C ANISOU 729 CA TRP A 164 10420 4887 6494 1661 1570 2416 C ATOM 730 C TRP A 164 51.197-125.486 251.070 1.00 59.83 C ANISOU 730 C TRP A 164 9977 5629 7127 1509 1264 2445 C ATOM 731 O TRP A 164 51.432-124.467 251.725 1.00 55.71 O ANISOU 731 O TRP A 164 8882 5383 6902 1635 1117 2553 O ATOM 732 CB TRP A 164 50.281-127.382 252.415 1.00 58.38 C ANISOU 732 CB TRP A 164 10774 4799 6607 1165 1628 2223 C ATOM 733 CG TRP A 164 48.988-127.336 251.645 1.00 80.67 C ANISOU 733 CG TRP A 164 13550 7677 9425 552 1512 2004 C ATOM 734 CD1 TRP A 164 48.496-128.297 250.807 1.00 83.01 C ANISOU 734 CD1 TRP A 164 14406 7724 9408 258 1656 1833 C ATOM 735 CD2 TRP A 164 48.024-126.273 251.642 1.00 73.48 C ANISOU 735 CD2 TRP A 164 11991 7117 8811 169 1234 1924 C ATOM 736 NE1 TRP A 164 47.289-127.898 250.284 1.00 75.49 N ANISOU 736 NE1 TRP A 164 13167 6979 8537 -291 1480 1642 N ATOM 737 CE2 TRP A 164 46.977-126.660 250.780 1.00 71.22 C ANISOU 737 CE2 TRP A 164 11888 6809 8363 -336 1217 1699 C ATOM 738 CE3 TRP A 164 47.946-125.032 252.283 1.00 66.66 C ANISOU 738 CE3 TRP A 164 10420 6591 8317 212 1007 2019 C ATOM 739 CZ2 TRP A 164 45.867-125.852 250.546 1.00 57.83 C ANISOU 739 CZ2 TRP A 164 9678 5446 6850 -765 972 1568 C ATOM 740 CZ3 TRP A 164 46.841-124.231 252.048 1.00 56.71 C ANISOU 740 CZ3 TRP A 164 8683 5621 7242 -211 772 1899 C ATOM 741 CH2 TRP A 164 45.817-124.645 251.188 1.00 54.55 C ANISOU 741 CH2 TRP A 164 8592 5346 6789 -678 752 1677 C ATOM 742 N ALA A 165 50.678-125.459 249.844 1.00 62.07 N ANISOU 742 N ALA A 165 10286 5963 7334 1240 1182 2345 N ATOM 743 CA ALA A 165 50.278-124.217 249.200 1.00 55.35 C ANISOU 743 CA ALA A 165 8796 5495 6740 1077 907 2354 C ATOM 744 C ALA A 165 49.168-124.516 248.205 1.00 62.76 C ANISOU 744 C ALA A 165 9883 6418 7543 594 851 2148 C ATOM 745 O ALA A 165 48.991-125.654 247.764 1.00 72.37 O ANISOU 745 O ALA A 165 11706 7340 8451 459 1036 2028 O ATOM 746 CB ALA A 165 51.458-123.531 248.501 1.00 51.85 C ANISOU 746 CB ALA A 165 8078 5267 6354 1528 848 2548 C ATOM 747 N ASN A 166 48.417-123.473 247.856 1.00 63.57 N ANISOU 747 N ASN A 166 9434 6857 7864 341 602 2103 N ATOM 748 CA ASN A 166 47.309-123.572 246.910 1.00 54.74 C ANISOU 748 CA ASN A 166 8334 5833 6634 -110 509 1902 C ATOM 749 C ASN A 166 47.596-122.631 245.748 1.00 53.55 C ANISOU 749 C ASN A 166 7794 5980 6572 46 328 1996 C ATOM 750 O ASN A 166 47.576-121.406 245.915 1.00 50.96 O ANISOU 750 O ASN A 166 6889 5955 6519 129 133 2095 O ATOM 751 CB ASN A 166 45.981-123.234 247.588 1.00 54.25 C ANISOU 751 CB ASN A 166 7979 5927 6707 -579 377 1732 C ATOM 752 CG ASN A 166 44.778-123.666 246.770 1.00 68.38 C ANISOU 752 CG ASN A 166 9908 7782 8293 -1090 343 1470 C ATOM 753 OD1 ASN A 166 44.844-123.764 245.546 1.00 61.11 O ANISOU 753 OD1 ASN A 166 9081 6919 7219 -1088 325 1441 O ATOM 754 ND2 ASN A 166 43.666-123.925 247.449 1.00 86.51 N ANISOU 754 ND2 ASN A 166 12205 10091 10573 -1539 337 1268 N ATOM 755 N TYR A 167 47.862-123.203 244.572 1.00 55.53 N ANISOU 755 N TYR A 167 8387 6131 6580 87 406 1964 N ATOM 756 CA TYR A 167 48.185-122.447 243.368 1.00 54.78 C ANISOU 756 CA TYR A 167 8010 6278 6525 247 264 2049 C ATOM 757 C TYR A 167 47.114-122.579 242.290 1.00 56.58 C ANISOU 757 C TYR A 167 8263 6635 6601 -156 172 1846 C ATOM 758 O TYR A 167 47.382-122.284 241.121 1.00 56.80 O ANISOU 758 O TYR A 167 8226 6787 6570 -38 105 1887 O ATOM 759 CB TYR A 167 49.535-122.895 242.806 1.00 55.42 C ANISOU 759 CB TYR A 167 8415 6186 6456 697 417 2205 C ATOM 760 CG TYR A 167 50.732-122.145 243.342 1.00 55.44 C ANISOU 760 CG TYR A 167 8108 6298 6658 1172 404 2442 C ATOM 761 CD1 TYR A 167 51.271-122.451 244.586 1.00 58.85 C ANISOU 761 CD1 TYR A 167 8641 6588 7133 1376 531 2518 C ATOM 762 CD2 TYR A 167 51.337-121.142 242.594 1.00 51.41 C ANISOU 762 CD2 TYR A 167 7215 6045 6273 1411 278 2579 C ATOM 763 CE1 TYR A 167 52.371-121.772 245.074 1.00 60.31 C ANISOU 763 CE1 TYR A 167 8521 6917 7477 1794 526 2714 C ATOM 764 CE2 TYR A 167 52.437-120.457 243.073 1.00 49.43 C ANISOU 764 CE2 TYR A 167 6680 5919 6183 1806 283 2772 C ATOM 765 CZ TYR A 167 52.950-120.777 244.313 1.00 68.34 C ANISOU 765 CZ TYR A 167 9152 8203 8613 1991 405 2833 C ATOM 766 OH TYR A 167 54.045-120.101 244.796 1.00 66.34 O ANISOU 766 OH TYR A 167 8578 8137 8492 2253 405 2858 O ATOM 767 N SER A 168 45.907-123.016 242.657 1.00 57.99 N ANISOU 767 N SER A 168 8524 6810 6701 -633 170 1618 N ATOM 768 CA SER A 168 44.896-123.327 241.651 1.00 60.29 C ANISOU 768 CA SER A 168 8895 7229 6784 -1040 118 1390 C ATOM 769 C SER A 168 44.443-122.089 240.885 1.00 67.38 C ANISOU 769 C SER A 168 9202 8571 7828 -1040 -153 1411 C ATOM 770 O SER A 168 44.122-122.185 239.695 1.00 66.25 O ANISOU 770 O SER A 168 9104 8554 7512 -1155 -199 1315 O ATOM 771 CB SER A 168 43.697-124.009 242.305 1.00 62.17 C ANISOU 771 CB SER A 168 9309 7413 6901 -1572 180 1124 C ATOM 772 OG SER A 168 43.047-123.129 243.203 1.00 72.14 O ANISOU 772 OG SER A 168 10053 8936 8421 -1691 2 1118 O ATOM 773 N GLU A 169 44.411-120.924 241.537 1.00 58.89 N ANISOU 773 N GLU A 169 7590 7733 7054 -904 -324 1536 N ATOM 774 CA GLU A 169 43.953-119.719 240.852 1.00 55.12 C ANISOU 774 CA GLU A 169 6585 7662 6695 -882 -567 1562 C ATOM 775 C GLU A 169 44.992-119.213 239.858 1.00 59.64 C ANISOU 775 C GLU A 169 7112 8259 7291 -471 -585 1759 C ATOM 776 O GLU A 169 44.635-118.706 238.788 1.00 65.53 O ANISOU 776 O GLU A 169 7670 9253 7977 -488 -716 1729 O ATOM 777 CB GLU A 169 43.607-118.629 241.866 1.00 54.49 C ANISOU 777 CB GLU A 169 5988 7802 6913 -858 -724 1637 C ATOM 778 CG GLU A 169 42.390-118.933 242.723 1.00 65.88 C ANISOU 778 CG GLU A 169 7372 9319 8339 -1296 -756 1423 C ATOM 779 CD GLU A 169 41.894-117.714 243.477 1.00 73.46 C ANISOU 779 CD GLU A 169 7765 10575 9572 -1278 -953 1486 C ATOM 780 OE1 GLU A 169 42.159-116.583 243.019 1.00 73.62 O ANISOU 780 OE1 GLU A 169 7418 10818 9735 -1014 -1096 1639 O ATOM 781 OE2 GLU A 169 41.243-117.883 244.529 1.00 78.47 O ANISOU 781 OE2 GLU A 169 8338 11207 10270 -1528 -955 1383 O ATOM 782 N CYS A 170 46.280-119.338 240.189 1.00 62.15 N ANISOU 782 N CYS A 170 7592 8344 7678 -94 -452 1957 N ATOM 783 CA CYS A 170 47.317-118.845 239.287 1.00 64.29 C ANISOU 783 CA CYS A 170 7809 8653 7966 289 -459 2139 C ATOM 784 C CYS A 170 47.442-119.713 238.041 1.00 63.63 C ANISOU 784 C CYS A 170 8141 8446 7591 255 -369 2056 C ATOM 785 O CYS A 170 47.859-119.224 236.986 1.00 68.12 O ANISOU 785 O CYS A 170 8607 9136 8138 450 -432 2141 O ATOM 786 CB CYS A 170 48.662-118.771 240.011 1.00 64.38 C ANISOU 786 CB CYS A 170 7859 8500 8101 692 -335 2350 C ATOM 787 SG CYS A 170 48.643-117.825 241.551 1.00 64.22 S ANISOU 787 SG CYS A 170 7382 8600 8417 743 -411 2451 S ATOM 788 N VAL A 171 47.091-120.990 238.143 1.00 62.21 N ANISOU 788 N VAL A 171 8447 8014 7176 6 -212 1890 N ATOM 789 CA VAL A 171 47.204-121.924 237.032 1.00 67.21 C ANISOU 789 CA VAL A 171 9535 8491 7511 -51 -96 1800 C ATOM 790 C VAL A 171 45.842-122.170 236.373 1.00 79.97 C ANISOU 790 C VAL A 171 11142 10291 8953 -532 -181 1534 C ATOM 791 O VAL A 171 45.685-123.114 235.598 1.00 64.56 O ANISOU 791 O VAL A 171 9611 8197 6720 -706 -64 1396 O ATOM 792 CB VAL A 171 47.869-123.237 237.484 1.00 72.80 C ANISOU 792 CB VAL A 171 10871 8766 8025 35 177 1801 C ATOM 793 CG1 VAL A 171 46.891-124.110 238.272 1.00 63.22 C ANISOU 793 CG1 VAL A 171 9943 7391 6688 -408 282 1578 C ATOM 794 CG2 VAL A 171 48.492-123.990 236.308 1.00 84.15 C ANISOU 794 CG2 VAL A 171 12752 10025 9197 179 306 1811 C ATOM 795 N LYS A 172 44.862-121.305 236.648 1.00 77.56 N ANISOU 795 N LYS A 172 10347 10328 8794 -741 -383 1458 N ATOM 796 CA LYS A 172 43.489-121.537 236.207 1.00 81.52 C ANISOU 796 CA LYS A 172 10791 11068 9117 -1217 -465 1180 C ATOM 797 C LYS A 172 43.395-121.608 234.687 1.00 87.91 C ANISOU 797 C LYS A 172 11662 12020 9720 -1226 -509 1116 C ATOM 798 O LYS A 172 42.959-122.618 234.124 1.00 91.86 O ANISOU 798 O LYS A 172 12544 12426 9931 -1534 -394 909 O ATOM 799 CB LYS A 172 42.582-120.437 236.763 1.00 84.45 C ANISOU 799 CB LYS A 172 10571 11827 9691 -1336 -692 1149 C ATOM 800 CG LYS A 172 41.099-120.658 236.533 1.00 93.00 C ANISOU 800 CG LYS A 172 11538 13213 10585 -1839 -781 842 C ATOM 801 CD LYS A 172 40.271-119.811 237.489 1.00 97.17 C ANISOU 801 CD LYS A 172 11576 14035 11311 -1962 -952 810 C ATOM 802 CE LYS A 172 40.665-118.345 237.415 1.00 98.76 C ANISOU 802 CE LYS A 172 11279 14465 11780 -1551 -1141 1054 C ATOM 803 NZ LYS A 172 39.948-117.522 238.428 1.00100.64 N ANISOU 803 NZ LYS A 172 11073 14948 12217 -1634 -1290 1046 N ATOM 804 N PHE A 173 43.802-120.538 234.001 1.00 90.60 N ANISOU 804 N PHE A 173 11644 12583 10195 -897 -665 1288 N ATOM 805 CA PHE A 173 43.792-120.502 232.542 1.00 91.51 C ANISOU 805 CA PHE A 173 11793 12841 10133 -851 -716 1255 C ATOM 806 C PHE A 173 45.077-121.053 231.934 1.00 95.59 C ANISOU 806 C PHE A 173 12718 13031 10571 -531 -552 1410 C ATOM 807 O PHE A 173 45.493-120.604 230.859 1.00 90.95 O ANISOU 807 O PHE A 173 12045 12554 9958 -302 -618 1503 O ATOM 808 CB PHE A 173 43.546-119.075 232.051 1.00 83.06 C ANISOU 808 CB PHE A 173 10168 12173 9218 -653 -953 1357 C ATOM 809 CG PHE A 173 42.423-118.375 232.762 1.00 78.73 C ANISOU 809 CG PHE A 173 9181 11957 8776 -868 -1122 1254 C ATOM 810 CD1 PHE A 173 41.107-118.758 232.557 1.00 81.06 C ANISOU 810 CD1 PHE A 173 9418 12521 8859 -1304 -1186 965 C ATOM 811 CD2 PHE A 173 42.683-117.329 233.632 1.00 73.56 C ANISOU 811 CD2 PHE A 173 8166 11367 8418 -638 -1211 1437 C ATOM 812 CE1 PHE A 173 40.073-118.116 233.211 1.00 82.07 C ANISOU 812 CE1 PHE A 173 9130 12987 9067 -1485 -1344 866 C ATOM 813 CE2 PHE A 173 41.654-116.682 234.288 1.00 74.53 C ANISOU 813 CE2 PHE A 173 7895 11793 8631 -817 -1365 1349 C ATOM 814 CZ PHE A 173 40.347-117.075 234.077 1.00 80.46 C ANISOU 814 CZ PHE A 173 8584 12822 9166 -1229 -1436 1065 C ATOM 815 N LEU A 174 45.718-122.019 232.591 1.00102.52 N ANISOU 815 N LEU A 174 14047 13514 11393 -493 -336 1438 N ATOM 816 CA LEU A 174 46.989-122.575 232.140 1.00116.25 C ANISOU 816 CA LEU A 174 16182 14945 13041 -149 -169 1592 C ATOM 817 C LEU A 174 46.882-124.077 231.884 1.00132.42 C ANISOU 817 C LEU A 174 18882 16667 14763 -387 58 1423 C ATOM 818 O LEU A 174 47.827-124.833 232.118 1.00139.27 O ANISOU 818 O LEU A 174 20192 17181 15542 -153 259 1524 O ATOM 819 CB LEU A 174 48.095-122.267 233.148 1.00115.32 C ANISOU 819 CB LEU A 174 16014 14662 13140 241 -102 1828 C ATOM 820 CG LEU A 174 49.544-122.322 232.664 1.00112.94 C ANISOU 820 CG LEU A 174 15892 14202 12818 716 -2 2043 C ATOM 821 CD1 LEU A 174 49.737-121.430 231.451 1.00113.06 C ANISOU 821 CD1 LEU A 174 15607 14475 12875 882 -154 2125 C ATOM 822 CD2 LEU A 174 50.480-121.923 233.785 1.00110.74 C ANISOU 822 CD2 LEU A 174 15472 13853 12751 1052 46 2240 C ATOM 823 N THR A 175 45.726-124.523 231.405 1.00142.57 N ANISOU 823 N THR A 175 20243 18081 15846 -853 38 1156 N ATOM 824 CA THR A 175 45.524-125.899 230.965 1.00154.06 C ANISOU 824 CA THR A 175 22320 19259 16958 -1138 257 964 C ATOM 825 C THR A 175 45.267-125.937 229.462 1.00162.31 C ANISOU 825 C THR A 175 23374 20488 17810 -1225 194 869 C ATOM 826 O THR A 175 44.385-126.650 228.977 1.00166.95 O ANISOU 826 O THR A 175 24182 21120 18133 -1671 255 601 O ATOM 827 CB THR A 175 44.375-126.560 231.722 1.00156.27 C ANISOU 827 CB THR A 175 22753 19512 17113 -1683 337 690 C ATOM 828 OG1 THR A 175 43.148-125.885 231.418 1.00156.09 O ANISOU 828 OG1 THR A 175 22232 19966 17109 -2020 117 505 O ATOM 829 CG2 THR A 175 44.623-126.494 233.223 1.00152.88 C ANISOU 829 CG2 THR A 175 22304 18901 16881 -1584 395 790 C ATOM 830 N ASN A 176 46.054-125.162 228.713 1.00165.55 N ANISOU 830 N ASN A 176 23544 21015 18342 -804 78 1081 N ATOM 831 CA ASN A 176 45.797-124.983 227.287 1.00172.85 C ANISOU 831 CA ASN A 176 24381 22171 19123 -843 -20 1013 C ATOM 832 C ASN A 176 46.078-126.255 226.498 1.00176.84 C ANISOU 832 C ASN A 176 25518 22371 19301 -948 197 912 C ATOM 833 O ASN A 176 45.320-126.602 225.584 1.00183.25 O ANISOU 833 O ASN A 176 26396 23345 19885 -1271 180 699 O ATOM 834 CB ASN A 176 46.636-123.819 226.757 1.00174.28 C ANISOU 834 CB ASN A 176 24178 22518 19521 -354 -176 1278 C ATOM 835 CG ASN A 176 48.073-123.861 227.253 1.00173.42 C ANISOU 835 CG ASN A 176 24252 22099 19541 108 -52 1543 C ATOM 836 OD1 ASN A 176 48.620-124.931 227.522 1.00174.48 O ANISOU 836 OD1 ASN A 176 24911 21864 19520 145 169 1543 O ATOM 837 ND2 ASN A 176 48.687-122.691 227.382 1.00170.36 N ANISOU 837 ND2 ASN A 176 23438 21874 19416 467 -182 1762 N ATOM 838 N GLU A 177 47.155-126.960 226.838 1.00174.76 N ANISOU 838 N GLU A 177 25726 21683 18993 -670 408 1059 N ATOM 839 CA GLU A 177 47.609-128.156 226.112 1.00172.79 C ANISOU 839 CA GLU A 177 26127 21096 18431 -678 635 1007 C ATOM 840 C GLU A 177 47.861-127.727 224.667 1.00171.58 C ANISOU 840 C GLU A 177 25814 21148 18230 -511 514 1060 C ATOM 841 O GLU A 177 48.564-126.727 224.449 1.00173.25 O ANISOU 841 O GLU A 177 25642 21520 18667 -98 365 1286 O ATOM 842 CB GLU A 177 46.612-129.295 226.304 1.00174.83 C ANISOU 842 CB GLU A 177 26828 21198 18400 -1251 814 697 C ATOM 843 CG GLU A 177 46.298-129.623 227.761 1.00171.91 C ANISOU 843 CG GLU A 177 26580 20647 18091 -1428 922 642 C ATOM 844 CD GLU A 177 47.446-130.307 228.487 1.00168.43 C ANISOU 844 CD GLU A 177 26648 19728 17620 -1051 1158 832 C ATOM 845 OE1 GLU A 177 48.480-130.601 227.849 1.00167.73 O ANISOU 845 OE1 GLU A 177 26845 19446 17437 -665 1250 993 O ATOM 846 OE2 GLU A 177 47.311-130.556 229.704 1.00166.16 O ANISOU 846 OE2 GLU A 177 26473 19273 17389 -1129 1254 816 O ATOM 847 N THR A 178 47.321-128.422 223.665 1.00174.86 N ANISOU 847 N THR A 178 26509 21572 18358 -821 577 855 N ATOM 848 CA THR A 178 47.588-128.093 222.266 1.00175.67 C ANISOU 848 CA THR A 178 26500 21848 18396 -654 476 903 C ATOM 849 C THR A 178 46.301-128.209 221.461 1.00170.55 C ANISOU 849 C THR A 178 25729 21524 17548 -1147 392 606 C ATOM 850 O THR A 178 45.791-129.314 221.254 1.00174.71 O ANISOU 850 O THR A 178 26718 21888 17776 -1550 574 370 O ATOM 851 CB THR A 178 48.669-129.002 221.675 1.00181.35 C ANISOU 851 CB THR A 178 27814 22172 18918 -386 690 1010 C ATOM 852 OG1 THR A 178 48.348-130.372 221.946 1.00185.75 O ANISOU 852 OG1 THR A 178 29021 22376 19178 -730 958 816 O ATOM 853 CG2 THR A 178 50.034-128.673 222.261 1.00178.34 C ANISOU 853 CG2 THR A 178 27432 21597 18733 184 728 1321 C ATOM 854 N ARG A 179 45.781-127.069 221.009 1.00162.22 N ANISOU 854 N ARG A 179 24063 20938 16635 -1110 128 611 N ATOM 855 CA ARG A 179 44.751-127.025 219.979 1.00154.78 C ANISOU 855 CA ARG A 179 22940 20377 15490 -1444 17 370 C ATOM 856 C ARG A 179 45.238-126.385 218.689 1.00146.98 C ANISOU 856 C ARG A 179 21757 19571 14519 -1101 -116 510 C ATOM 857 O ARG A 179 44.778-126.765 217.609 1.00148.79 O ANISOU 857 O ARG A 179 22081 19952 14500 -1309 -116 337 O ATOM 858 CB ARG A 179 43.513-126.270 220.488 1.00155.64 C ANISOU 858 CB ARG A 179 22497 20954 15687 -1726 -182 210 C ATOM 859 CG ARG A 179 42.442-126.020 219.430 1.00157.35 C ANISOU 859 CG ARG A 179 22411 21674 15699 -1998 -335 -25 C ATOM 860 CD ARG A 179 41.139-125.528 220.042 1.00156.90 C ANISOU 860 CD ARG A 179 21892 22068 15655 -2339 -489 -234 C ATOM 861 NE ARG A 179 40.334-124.771 219.084 1.00157.21 N ANISOU 861 NE ARG A 179 21452 22685 15595 -2358 -714 -345 N ATOM 862 CZ ARG A 179 39.525-125.318 218.182 1.00159.03 C ANISOU 862 CZ ARG A 179 21735 23195 15492 -2731 -701 -637 C ATOM 863 NH1 ARG A 179 39.409-126.636 218.099 1.00161.30 N ANISOU 863 NH1 ARG A 179 22559 23212 15516 -3148 -461 -853 N ATOM 864 NH2 ARG A 179 38.832-124.543 217.357 1.00159.05 N ANISOU 864 NH2 ARG A 179 21267 23757 15410 -2681 -918 -718 N ATOM 865 N GLU A 180 46.184-125.448 218.780 1.00135.19 N ANISOU 865 N GLU A 180 20011 18057 13297 -592 -214 813 N ATOM 866 CA GLU A 180 46.779-124.811 217.613 1.00122.64 C ANISOU 866 CA GLU A 180 18266 16594 11736 -233 -320 971 C ATOM 867 C GLU A 180 47.656-125.756 216.802 1.00118.21 C ANISOU 867 C GLU A 180 18246 15689 10979 -105 -136 1018 C ATOM 868 O GLU A 180 47.993-125.426 215.660 1.00117.42 O ANISOU 868 O GLU A 180 18077 15703 10833 103 -208 1090 O ATOM 869 CB GLU A 180 47.610-123.599 218.043 1.00119.28 C ANISOU 869 CB GLU A 180 17471 16206 11643 244 -435 1272 C ATOM 870 CG GLU A 180 46.992-122.752 219.152 1.00122.69 C ANISOU 870 CG GLU A 180 17459 16856 12303 174 -568 1275 C ATOM 871 CD GLU A 180 47.325-123.263 220.545 1.00127.64 C ANISOU 871 CD GLU A 180 18296 17166 13036 130 -422 1313 C ATOM 872 OE1 GLU A 180 47.197-124.483 220.785 1.00130.77 O ANISOU 872 OE1 GLU A 180 19163 17291 13233 -136 -234 1166 O ATOM 873 OE2 GLU A 180 47.725-122.444 221.398 1.00123.83 O ANISOU 873 OE2 GLU A 180 17526 16701 12825 366 -484 1490 O ATOM 874 N ARG A 181 48.039-126.909 217.359 1.00119.22 N ANISOU 874 N ARG A 181 18923 15397 10980 -204 104 984 N ATOM 875 CA ARG A 181 48.871-127.850 216.615 1.00120.15 C ANISOU 875 CA ARG A 181 19594 15173 10885 -64 294 1030 C ATOM 876 C ARG A 181 48.161-128.376 215.377 1.00115.44 C ANISOU 876 C ARG A 181 19147 14720 9996 -391 301 799 C ATOM 877 O ARG A 181 48.810-128.653 214.362 1.00115.63 O ANISOU 877 O ARG A 181 19402 14632 9898 -188 350 874 O ATOM 878 CB ARG A 181 49.286-129.020 217.507 1.00125.83 C ANISOU 878 CB ARG A 181 20911 15416 11481 -124 567 1017 C ATOM 879 CG ARG A 181 50.553-128.786 218.307 1.00131.39 C ANISOU 879 CG ARG A 181 21658 15879 12385 379 627 1307 C ATOM 880 CD ARG A 181 50.980-130.048 219.041 1.00140.90 C ANISOU 880 CD ARG A 181 23527 16606 13402 361 918 1290 C ATOM 881 NE ARG A 181 51.207-131.165 218.129 1.00149.47 N ANISOU 881 NE ARG A 181 25219 17421 14152 294 1114 1207 N ATOM 882 CZ ARG A 181 52.382-131.455 217.581 1.00151.62 C ANISOU 882 CZ ARG A 181 25781 17482 14344 728 1209 1395 C ATOM 883 NH1 ARG A 181 53.445-130.709 217.852 1.00149.73 N ANISOU 883 NH1 ARG A 181 25265 17295 14330 1245 1128 1665 N ATOM 884 NH2 ARG A 181 52.496-132.491 216.762 1.00154.18 N ANISOU 884 NH2 ARG A 181 26674 17557 14350 637 1392 1304 N ATOM 885 N GLU A 182 46.837-128.528 215.441 1.00112.35 N ANISOU 885 N GLU A 182 18616 14597 9474 -900 254 509 N ATOM 886 CA GLU A 182 46.097-129.059 214.301 1.00117.23 C ANISOU 886 CA GLU A 182 19358 15397 9786 -1255 269 255 C ATOM 887 C GLU A 182 46.173-128.117 213.106 1.00108.61 C ANISOU 887 C GLU A 182 17848 14669 8750 -985 49 346 C ATOM 888 O GLU A 182 46.337-128.563 211.964 1.00106.74 O ANISOU 888 O GLU A 182 17840 14408 8308 -992 98 296 O ATOM 889 CB GLU A 182 44.642-129.310 214.698 1.00125.89 C ANISOU 889 CB GLU A 182 20316 16784 10733 -1858 252 -88 C ATOM 890 CG GLU A 182 44.482-130.222 215.902 1.00133.36 C ANISOU 890 CG GLU A 182 21683 17376 11614 -2163 478 -198 C ATOM 891 CD GLU A 182 43.063-130.238 216.436 1.00138.92 C ANISOU 891 CD GLU A 182 22133 18425 12225 -2727 427 -515 C ATOM 892 OE1 GLU A 182 42.231-129.449 215.941 1.00140.33 O ANISOU 892 OE1 GLU A 182 21758 19152 12409 -2828 195 -629 O ATOM 893 OE2 GLU A 182 42.780-131.038 217.353 1.00140.46 O ANISOU 893 OE2 GLU A 182 22689 18356 12325 -3058 624 -653 O ATOM 894 N VAL A 183 46.064-126.810 213.350 1.00101.25 N ANISOU 894 N VAL A 183 16324 14061 8085 -738 -184 484 N ATOM 895 CA VAL A 183 46.100-125.845 212.257 1.00100.07 C ANISOU 895 CA VAL A 183 15785 14256 7981 -465 -386 575 C ATOM 896 C VAL A 183 47.517-125.697 211.716 1.00 97.27 C ANISOU 896 C VAL A 183 15618 13613 7728 39 -336 868 C ATOM 897 O VAL A 183 47.731-125.678 210.497 1.00 97.26 O ANISOU 897 O VAL A 183 15659 13691 7604 160 -369 882 O ATOM 898 CB VAL A 183 45.523-124.496 212.722 1.00 97.79 C ANISOU 898 CB VAL A 183 14855 14382 7921 -354 -626 630 C ATOM 899 CG1 VAL A 183 45.624-123.463 211.613 1.00 98.96 C ANISOU 899 CG1 VAL A 183 14647 14847 8106 -24 -814 747 C ATOM 900 CG2 VAL A 183 44.077-124.664 213.164 1.00100.36 C ANISOU 900 CG2 VAL A 183 14973 15050 8107 -857 -683 319 C ATOM 901 N PHE A 184 48.508-125.597 212.606 1.00 91.05 N ANISOU 901 N PHE A 184 14936 12510 7151 339 -255 1096 N ATOM 902 CA PHE A 184 49.884-125.406 212.160 1.00 89.87 C ANISOU 902 CA PHE A 184 14921 12134 7090 824 -209 1367 C ATOM 903 C PHE A 184 50.424-126.630 211.430 1.00 95.83 C ANISOU 903 C PHE A 184 16270 12562 7579 802 -9 1326 C ATOM 904 O PHE A 184 51.249-126.490 210.520 1.00 97.64 O ANISOU 904 O PHE A 184 16571 12737 7789 1121 -12 1473 O ATOM 905 CB PHE A 184 50.781-125.059 213.348 1.00 87.75 C ANISOU 905 CB PHE A 184 14611 11652 7078 1125 -159 1593 C ATOM 906 CG PHE A 184 50.555-123.679 213.896 1.00 88.61 C ANISOU 906 CG PHE A 184 14136 12058 7474 1264 -353 1700 C ATOM 907 CD1 PHE A 184 50.045-122.674 213.090 1.00 83.69 C ANISOU 907 CD1 PHE A 184 13096 11813 6888 1319 -552 1696 C ATOM 908 CD2 PHE A 184 50.850-123.387 215.218 1.00 89.61 C ANISOU 908 CD2 PHE A 184 14150 12081 7818 1352 -328 1807 C ATOM 909 CE1 PHE A 184 49.835-121.403 213.591 1.00 84.76 C ANISOU 909 CE1 PHE A 184 12741 12198 7266 1460 -711 1800 C ATOM 910 CE2 PHE A 184 50.642-122.118 215.725 1.00 85.45 C ANISOU 910 CE2 PHE A 184 13109 11812 7547 1470 -493 1904 C ATOM 911 CZ PHE A 184 50.134-121.125 214.911 1.00 85.62 C ANISOU 911 CZ PHE A 184 12747 12189 7596 1525 -680 1903 C ATOM 912 N ASP A 185 49.977-127.831 211.807 1.00 96.49 N ANISOU 912 N ASP A 185 16802 12417 7444 429 176 1126 N ATOM 913 CA ASP A 185 50.438-129.032 211.119 1.00 99.08 C ANISOU 913 CA ASP A 185 17743 12414 7490 391 387 1076 C ATOM 914 C ASP A 185 49.782-129.180 209.751 1.00100.29 C ANISOU 914 C ASP A 185 17875 12810 7420 160 324 893 C ATOM 915 O ASP A 185 50.426-129.636 208.800 1.00100.46 O ANISOU 915 O ASP A 185 18208 12669 7294 325 405 951 O ATOM 916 CB ASP A 185 50.173-130.270 211.976 1.00107.16 C ANISOU 916 CB ASP A 185 19306 13083 8327 61 636 919 C ATOM 917 CG ASP A 185 51.093-130.353 213.180 1.00108.40 C ANISOU 917 CG ASP A 185 19626 12919 8644 381 749 1129 C ATOM 918 OD1 ASP A 185 52.249-129.889 213.081 1.00107.08 O ANISOU 918 OD1 ASP A 185 19382 12679 8623 888 720 1396 O ATOM 919 OD2 ASP A 185 50.662-130.885 214.225 1.00108.77 O ANISOU 919 OD2 ASP A 185 19872 12801 8655 122 871 1018 O ATOM 920 N ARG A 186 48.507-128.804 209.631 1.00104.19 N ANISOU 920 N ARG A 186 17997 13718 7871 -212 178 666 N ATOM 921 CA ARG A 186 47.835-128.885 208.338 1.00112.47 C ANISOU 921 CA ARG A 186 18970 15068 8695 -424 104 478 C ATOM 922 C ARG A 186 48.410-127.872 207.355 1.00104.90 C ANISOU 922 C ARG A 186 17672 14315 7871 28 -79 689 C ATOM 923 O ARG A 186 48.727-128.214 206.210 1.00103.05 O ANISOU 923 O ARG A 186 17641 14042 7470 102 -44 686 O ATOM 924 CB ARG A 186 46.329-128.673 208.502 1.00121.74 C ANISOU 924 CB ARG A 186 19780 16701 9775 -903 -15 179 C ATOM 925 CG ARG A 186 45.582-129.868 209.074 1.00131.06 C ANISOU 925 CG ARG A 186 21361 17727 10707 -1479 193 -119 C ATOM 926 CD ARG A 186 44.099-129.799 208.733 1.00137.51 C ANISOU 926 CD ARG A 186 21849 19079 11320 -1985 84 -469 C ATOM 927 NE ARG A 186 43.440-128.644 209.337 1.00137.57 N ANISOU 927 NE ARG A 186 21208 19522 11541 -1930 -156 -454 N ATOM 928 CZ ARG A 186 42.668-128.706 210.417 1.00136.82 C ANISOU 928 CZ ARG A 186 20990 19526 11469 -2263 -147 -611 C ATOM 929 NH1 ARG A 186 42.450-129.870 211.013 1.00137.95 N ANISOU 929 NH1 ARG A 186 21628 19356 11433 -2692 99 -800 N ATOM 930 NH2 ARG A 186 42.108-127.604 210.899 1.00134.50 N ANISOU 930 NH2 ARG A 186 20100 19638 11366 -2167 -375 -580 N ATOM 931 N LEU A 187 48.551-126.617 207.788 1.00100.75 N ANISOU 931 N LEU A 187 16645 13997 7636 329 -263 872 N ATOM 932 CA LEU A 187 49.079-125.585 206.902 1.00 96.57 C ANISOU 932 CA LEU A 187 15806 13655 7232 751 -422 1071 C ATOM 933 C LEU A 187 50.538-125.848 206.551 1.00 95.46 C ANISOU 933 C LEU A 187 16005 13133 7134 1154 -298 1316 C ATOM 934 O LEU A 187 50.960-125.612 205.413 1.00 98.18 O ANISOU 934 O LEU A 187 16343 13539 7423 1375 -346 1395 O ATOM 935 CB LEU A 187 48.921-124.210 207.550 1.00 91.19 C ANISOU 935 CB LEU A 187 14572 13237 6839 964 -610 1209 C ATOM 936 CG LEU A 187 47.492-123.778 207.880 1.00 92.14 C ANISOU 936 CG LEU A 187 14288 13797 6923 637 -760 990 C ATOM 937 CD1 LEU A 187 47.500-122.455 208.627 1.00 87.66 C ANISOU 937 CD1 LEU A 187 13246 13408 6651 896 -915 1163 C ATOM 938 CD2 LEU A 187 46.654-123.681 206.616 1.00 92.14 C ANISOU 938 CD2 LEU A 187 14122 14202 6683 500 -876 804 C ATOM 939 N GLY A 188 51.324-126.333 207.514 1.00 90.66 N ANISOU 939 N GLY A 188 15690 12148 6609 1268 -140 1435 N ATOM 940 CA GLY A 188 52.705-126.678 207.226 1.00 88.99 C ANISOU 940 CA GLY A 188 15815 11603 6396 1653 -10 1649 C ATOM 941 C GLY A 188 52.836-127.850 206.277 1.00 97.98 C ANISOU 941 C GLY A 188 17475 12530 7225 1530 144 1538 C ATOM 942 O GLY A 188 53.771-127.900 205.472 1.00 98.62 O ANISOU 942 O GLY A 188 17715 12491 7266 1850 178 1688 O ATOM 943 N MET A 189 51.910-128.809 206.357 1.00 94.54 N ANISOU 943 N MET A 189 17322 12045 6553 1053 249 1270 N ATOM 944 CA MET A 189 51.907-129.913 205.404 1.00104.67 C ANISOU 944 CA MET A 189 19105 13148 7518 877 402 1134 C ATOM 945 C MET A 189 51.531-129.429 204.009 1.00106.78 C ANISOU 945 C MET A 189 19106 13758 7706 873 242 1073 C ATOM 946 O MET A 189 52.108-129.879 203.012 1.00106.68 O ANISOU 946 O MET A 189 19387 13605 7543 1014 313 1118 O ATOM 947 CB MET A 189 50.946-131.005 205.873 1.00111.74 C ANISOU 947 CB MET A 189 20361 13927 8169 317 570 837 C ATOM 948 CG MET A 189 50.834-132.188 204.929 1.00123.51 C ANISOU 948 CG MET A 189 22400 15228 9302 62 754 662 C ATOM 949 SD MET A 189 49.589-133.374 205.470 1.00139.25 S ANISOU 949 SD MET A 189 24786 17131 10991 -673 962 274 S ATOM 950 CE MET A 189 48.134-132.330 205.531 1.00140.14 C ANISOU 950 CE MET A 189 24122 17917 11209 -1014 677 62 C ATOM 951 N ILE A 190 50.566-128.510 203.921 1.00111.07 N ANISOU 951 N ILE A 190 19101 14764 8338 733 27 973 N ATOM 952 CA ILE A 190 50.193-127.937 202.632 1.00 98.25 C ANISOU 952 CA ILE A 190 17184 13507 6641 781 -139 928 C ATOM 953 C ILE A 190 51.372-127.188 202.022 1.00 97.08 C ANISOU 953 C ILE A 190 16931 13292 6661 1333 -208 1230 C ATOM 954 O ILE A 190 51.581-127.215 200.803 1.00101.51 O ANISOU 954 O ILE A 190 17551 13919 7098 1445 -236 1240 O ATOM 955 CB ILE A 190 48.958-127.029 202.795 1.00101.16 C ANISOU 955 CB ILE A 190 16971 14397 7066 587 -355 782 C ATOM 956 CG1 ILE A 190 47.730-127.861 203.170 1.00101.08 C ANISOU 956 CG1 ILE A 190 17071 14512 6823 -15 -279 433 C ATOM 957 CG2 ILE A 190 48.698-126.229 201.528 1.00100.02 C ANISOU 957 CG2 ILE A 190 16481 14647 6876 761 -542 790 C ATOM 958 CD1 ILE A 190 46.475-127.042 203.379 1.00101.31 C ANISOU 958 CD1 ILE A 190 16528 15094 6871 -215 -486 266 C ATOM 959 N CYS A 191 52.170-126.525 202.861 1.00 93.90 N ANISOU 959 N CYS A 191 16380 12765 6533 1671 -226 1471 N ATOM 960 CA CYS A 191 53.336-125.800 202.366 1.00 95.90 C ANISOU 960 CA CYS A 191 16535 12962 6940 2170 -270 1747 C ATOM 961 C CYS A 191 54.366-126.753 201.776 1.00101.68 C ANISOU 961 C CYS A 191 17786 13334 7513 2338 -93 1827 C ATOM 962 O CYS A 191 54.840-126.553 200.651 1.00100.01 O ANISOU 962 O CYS A 191 17586 13167 7246 2555 -131 1907 O ATOM 963 CB CYS A 191 53.960-124.977 203.492 1.00 96.63 C ANISOU 963 CB CYS A 191 16379 13002 7334 2442 -298 1957 C ATOM 964 SG CYS A 191 55.264-123.850 202.949 1.00 94.13 S ANISOU 964 SG CYS A 191 15842 12708 7216 3001 -364 2267 S ATOM 965 N THR A 192 54.730-127.795 202.526 1.00105.34 N ANISOU 965 N THR A 192 18700 13437 7888 2259 109 1809 N ATOM 966 CA THR A 192 55.764-128.713 202.060 1.00103.90 C ANISOU 966 CA THR A 192 19039 12899 7537 2467 292 1901 C ATOM 967 C THR A 192 55.289-129.529 200.864 1.00105.11 C ANISOU 967 C THR A 192 19502 13042 7392 2215 347 1716 C ATOM 968 O THR A 192 56.065-129.787 199.938 1.00102.85 O ANISOU 968 O THR A 192 19440 12634 7003 2459 395 1815 O ATOM 969 CB THR A 192 56.204-129.633 203.199 1.00102.55 C ANISOU 969 CB THR A 192 19301 12350 7314 2462 506 1922 C ATOM 970 OG1 THR A 192 55.049-130.201 203.829 1.00104.61 O ANISOU 970 OG1 THR A 192 19669 12607 7471 1970 561 1675 O ATOM 971 CG2 THR A 192 57.010-128.854 204.229 1.00 96.90 C ANISOU 971 CG2 THR A 192 18312 11628 6877 2819 469 2148 C ATOM 972 N VAL A 193 54.019-129.941 200.862 1.00 98.82 N ANISOU 972 N VAL A 193 18713 12393 6442 1718 344 1437 N ATOM 973 CA VAL A 193 53.490-130.705 199.735 1.00111.18 C ANISOU 973 CA VAL A 193 20547 13990 7707 1429 400 1230 C ATOM 974 C VAL A 193 53.417-129.832 198.488 1.00101.25 C ANISOU 974 C VAL A 193 18901 13084 6485 1604 198 1274 C ATOM 975 O VAL A 193 53.831-130.242 197.398 1.00102.42 O ANISOU 975 O VAL A 193 19295 13148 6471 1700 246 1288 O ATOM 976 CB VAL A 193 52.117-131.304 200.087 1.00105.97 C ANISOU 976 CB VAL A 193 19945 13457 6861 820 450 896 C ATOM 977 CG1 VAL A 193 51.399-131.770 198.828 1.00111.80 C ANISOU 977 CG1 VAL A 193 20773 14394 7312 502 448 658 C ATOM 978 CG2 VAL A 193 52.280-132.460 201.059 1.00105.80 C ANISOU 978 CG2 VAL A 193 20495 12991 6711 628 715 835 C ATOM 979 N GLY A 194 52.896-128.612 198.632 1.00103.07 N ANISOU 979 N GLY A 194 18539 13705 6918 1665 -22 1300 N ATOM 980 CA GLY A 194 52.755-127.737 197.479 1.00 99.16 C ANISOU 980 CA GLY A 194 17683 13553 6439 1844 -208 1338 C ATOM 981 C GLY A 194 54.086-127.320 196.885 1.00 97.33 C ANISOU 981 C GLY A 194 17505 13155 6322 2352 -210 1621 C ATOM 982 O GLY A 194 54.249-127.298 195.662 1.00 98.15 O ANISOU 982 O GLY A 194 17644 13340 6309 2459 -248 1628 O ATOM 983 N TYR A 195 55.058-126.984 197.737 1.00 94.95 N ANISOU 983 N TYR A 195 17200 12638 6237 2663 -164 1848 N ATOM 984 CA TYR A 195 56.358-126.561 197.229 1.00100.18 C ANISOU 984 CA TYR A 195 17890 13176 6999 3132 -157 2105 C ATOM 985 C TYR A 195 57.170-127.736 196.698 1.00102.98 C ANISOU 985 C TYR A 195 18807 13181 7139 3212 31 2129 C ATOM 986 O TYR A 195 58.009-127.552 195.809 1.00107.02 O ANISOU 986 O TYR A 195 19372 13657 7636 3521 25 2272 O ATOM 987 CB TYR A 195 57.135-125.816 198.314 1.00 90.48 C ANISOU 987 CB TYR A 195 16453 11878 6046 3422 -161 2319 C ATOM 988 CG TYR A 195 56.841-124.333 198.354 1.00 94.74 C ANISOU 988 CG TYR A 195 16435 12750 6813 3555 -354 2403 C ATOM 989 CD1 TYR A 195 57.465-123.461 197.471 1.00 97.59 C ANISOU 989 CD1 TYR A 195 16613 13222 7244 3883 -432 2562 C ATOM 990 CD2 TYR A 195 55.939-123.805 199.267 1.00 87.82 C ANISOU 990 CD2 TYR A 195 15238 12064 6064 3356 -445 2321 C ATOM 991 CE1 TYR A 195 57.202-122.104 197.497 1.00 85.80 C ANISOU 991 CE1 TYR A 195 14667 12001 5933 4013 -581 2641 C ATOM 992 CE2 TYR A 195 55.668-122.448 199.302 1.00 92.26 C ANISOU 992 CE2 TYR A 195 15328 12913 6812 3499 -606 2402 C ATOM 993 CZ TYR A 195 56.302-121.603 198.413 1.00 90.35 C ANISOU 993 CZ TYR A 195 14946 12756 6626 3829 -667 2564 C ATOM 994 OH TYR A 195 56.038-120.253 198.442 1.00 83.81 O ANISOU 994 OH TYR A 195 13702 12184 5959 3979 -802 2647 O ATOM 995 N SER A 196 56.938-128.943 197.220 1.00100.24 N ANISOU 995 N SER A 196 18905 12568 6613 2943 209 1992 N ATOM 996 CA SER A 196 57.638-130.111 196.692 1.00101.68 C ANISOU 996 CA SER A 196 19674 12406 6554 3013 404 2004 C ATOM 997 C SER A 196 57.139-130.467 195.298 1.00103.00 C ANISOU 997 C SER A 196 19951 12689 6497 2829 377 1854 C ATOM 998 O SER A 196 57.940-130.757 194.402 1.00101.20 O ANISOU 998 O SER A 196 19961 12324 6165 3075 430 1956 O ATOM 999 CB SER A 196 57.474-131.300 197.638 1.00100.83 C ANISOU 999 CB SER A 196 20059 11963 6290 2769 624 1891 C ATOM 1000 OG SER A 196 57.924-130.976 198.942 1.00 98.34 O ANISOU 1000 OG SER A 196 19633 11556 6175 2949 647 2027 O ATOM 1001 N VAL A 197 55.819-130.453 195.097 1.00102.34 N ANISOU 1001 N VAL A 197 19684 12879 6322 2398 296 1603 N ATOM 1002 CA VAL A 197 55.266-130.717 193.771 1.00111.67 C ANISOU 1002 CA VAL A 197 20905 14240 7283 2209 256 1440 C ATOM 1003 C VAL A 197 55.691-129.629 192.795 1.00111.04 C ANISOU 1003 C VAL A 197 20442 14410 7337 2583 69 1608 C ATOM 1004 O VAL A 197 55.976-129.900 191.622 1.00103.92 O ANISOU 1004 O VAL A 197 19704 13494 6286 2668 80 1611 O ATOM 1005 CB VAL A 197 53.733-130.848 193.848 1.00106.61 C ANISOU 1005 CB VAL A 197 20080 13918 6508 1670 200 1121 C ATOM 1006 CG1 VAL A 197 53.137-131.009 192.457 1.00113.82 C ANISOU 1006 CG1 VAL A 197 20960 15095 7191 1491 140 945 C ATOM 1007 CG2 VAL A 197 53.345-132.023 194.729 1.00108.66 C ANISOU 1007 CG2 VAL A 197 20796 13892 6599 1265 421 938 C ATOM 1008 N SER A 198 55.751-128.381 193.266 1.00107.56 N ANISOU 1008 N SER A 198 19509 14187 7171 2810 -93 1751 N ATOM 1009 CA SER A 198 56.192-127.289 192.405 1.00109.26 C ANISOU 1009 CA SER A 198 19391 14610 7512 3175 -249 1920 C ATOM 1010 C SER A 198 57.658-127.443 192.023 1.00110.73 C ANISOU 1010 C SER A 198 19845 14500 7728 3584 -152 2156 C ATOM 1011 O SER A 198 58.025-127.251 190.858 1.00115.90 O ANISOU 1011 O SER A 198 20504 15215 8318 3771 -196 2217 O ATOM 1012 CB SER A 198 55.955-125.945 193.095 1.00104.25 C ANISOU 1012 CB SER A 198 18229 14232 7150 3316 -409 2021 C ATOM 1013 OG SER A 198 54.574-125.716 193.307 1.00 97.32 O ANISOU 1013 OG SER A 198 17061 13693 6224 2978 -521 1802 O ATOM 1014 N LEU A 199 58.511-127.797 192.987 1.00105.09 N ANISOU 1014 N LEU A 199 19349 13485 7095 3736 -18 2287 N ATOM 1015 CA LEU A 199 59.932-127.944 192.691 1.00102.08 C ANISOU 1015 CA LEU A 199 19035 12855 6896 4049 83 2421 C ATOM 1016 C LEU A 199 60.192-129.160 191.811 1.00103.65 C ANISOU 1016 C LEU A 199 19720 12819 6842 3987 221 2340 C ATOM 1017 O LEU A 199 61.048-129.115 190.920 1.00106.45 O ANISOU 1017 O LEU A 199 20019 13113 7313 4191 235 2388 O ATOM 1018 CB LEU A 199 60.733-128.036 193.989 1.00 98.94 C ANISOU 1018 CB LEU A 199 18592 12242 6757 4155 195 2485 C ATOM 1019 CG LEU A 199 62.255-128.082 193.838 1.00 96.92 C ANISOU 1019 CG LEU A 199 18245 11813 6767 4433 298 2541 C ATOM 1020 CD1 LEU A 199 62.746-126.905 193.011 1.00 96.18 C ANISOU 1020 CD1 LEU A 199 17696 11937 6911 4604 183 2600 C ATOM 1021 CD2 LEU A 199 62.928-128.098 195.201 1.00 97.37 C ANISOU 1021 CD2 LEU A 199 18207 11751 7040 4521 393 2569 C ATOM 1022 N ALA A 200 59.462-130.254 192.040 1.00104.27 N ANISOU 1022 N ALA A 200 20287 12760 6573 3677 340 2196 N ATOM 1023 CA ALA A 200 59.638-131.442 191.212 1.00106.56 C ANISOU 1023 CA ALA A 200 21064 12809 6615 3573 492 2096 C ATOM 1024 C ALA A 200 59.169-131.196 189.782 1.00104.16 C ANISOU 1024 C ALA A 200 20693 12756 6127 3523 375 2035 C ATOM 1025 O ALA A 200 59.811-131.646 188.827 1.00110.85 O ANISOU 1025 O ALA A 200 21700 13459 6961 3643 434 2049 O ATOM 1026 CB ALA A 200 58.895-132.627 191.825 1.00105.69 C ANISOU 1026 CB ALA A 200 21485 12487 6184 3177 674 1911 C ATOM 1027 N SER A 201 58.054-130.481 189.616 1.00104.17 N ANISOU 1027 N SER A 201 20291 13143 6145 3299 202 1906 N ATOM 1028 CA SER A 201 57.542-130.219 188.275 1.00105.32 C ANISOU 1028 CA SER A 201 20271 13569 6175 3233 82 1808 C ATOM 1029 C SER A 201 58.377-129.174 187.545 1.00103.17 C ANISOU 1029 C SER A 201 19719 13413 6070 3699 -49 2045 C ATOM 1030 O SER A 201 58.474-129.213 186.314 1.00112.15 O ANISOU 1030 O SER A 201 20902 14626 7083 3775 -86 2036 O ATOM 1031 CB SER A 201 56.081-129.776 188.346 1.00106.24 C ANISOU 1031 CB SER A 201 19990 14104 6272 2863 -62 1574 C ATOM 1032 OG SER A 201 55.941-128.594 189.115 1.00103.79 O ANISOU 1032 OG SER A 201 19195 14005 6235 3017 -210 1682 O ATOM 1033 N LEU A 202 58.981-128.236 188.277 1.00103.63 N ANISOU 1033 N LEU A 202 19450 13480 6445 3973 -107 2230 N ATOM 1034 CA LEU A 202 59.836-127.241 187.642 1.00 98.52 C ANISOU 1034 CA LEU A 202 18401 12892 6138 4285 -185 2365 C ATOM 1035 C LEU A 202 61.188-127.818 187.245 1.00102.24 C ANISOU 1035 C LEU A 202 19048 13040 6760 4463 -37 2418 C ATOM 1036 O LEU A 202 61.781-127.370 186.258 1.00101.90 O ANISOU 1036 O LEU A 202 18833 13040 6845 4638 -71 2460 O ATOM 1037 CB LEU A 202 60.032-126.040 188.568 1.00 95.84 C ANISOU 1037 CB LEU A 202 17593 12663 6157 4416 -262 2469 C ATOM 1038 CG LEU A 202 58.869-125.053 188.676 1.00 95.52 C ANISOU 1038 CG LEU A 202 17211 13013 6068 4354 -450 2444 C ATOM 1039 CD1 LEU A 202 59.168-123.994 189.721 1.00 92.94 C ANISOU 1039 CD1 LEU A 202 16484 12716 6113 4458 -481 2541 C ATOM 1040 CD2 LEU A 202 58.591-124.411 187.330 1.00 96.08 C ANISOU 1040 CD2 LEU A 202 17075 13336 6096 4454 -573 2429 C ATOM 1041 N THR A 203 61.691-128.803 187.995 1.00 99.70 N ANISOU 1041 N THR A 203 19061 12407 6414 4428 133 2402 N ATOM 1042 CA THR A 203 62.972-129.411 187.647 1.00101.93 C ANISOU 1042 CA THR A 203 19503 12418 6806 4619 275 2425 C ATOM 1043 C THR A 203 62.875-130.203 186.350 1.00107.11 C ANISOU 1043 C THR A 203 20498 12997 7201 4566 312 2360 C ATOM 1044 O THR A 203 63.769-130.123 185.501 1.00107.33 O ANISOU 1044 O THR A 203 20453 12980 7349 4765 329 2395 O ATOM 1045 CB THR A 203 63.461-130.306 188.785 1.00103.97 C ANISOU 1045 CB THR A 203 20046 12382 7077 4617 449 2407 C ATOM 1046 OG1 THR A 203 62.368-131.083 189.291 1.00108.87 O ANISOU 1046 OG1 THR A 203 21050 12926 7391 4312 501 2313 O ATOM 1047 CG2 THR A 203 64.055-129.468 189.909 1.00100.88 C ANISOU 1047 CG2 THR A 203 19252 12059 7020 4759 433 2479 C ATOM 1048 N VAL A 204 61.800-130.977 186.178 1.00112.31 N ANISOU 1048 N VAL A 204 21530 13655 7487 4268 338 2240 N ATOM 1049 CA VAL A 204 61.617-131.703 184.928 1.00120.46 C ANISOU 1049 CA VAL A 204 22874 14643 8250 4170 376 2153 C ATOM 1050 C VAL A 204 61.235-130.765 183.790 1.00115.84 C ANISOU 1050 C VAL A 204 21945 14406 7662 4238 187 2169 C ATOM 1051 O VAL A 204 61.464-131.093 182.621 1.00117.75 O ANISOU 1051 O VAL A 204 22314 14623 7805 4280 198 2146 O ATOM 1052 CB VAL A 204 60.568-132.819 185.090 1.00130.73 C ANISOU 1052 CB VAL A 204 24675 15860 9136 3753 492 1960 C ATOM 1053 CG1 VAL A 204 61.057-133.866 186.079 1.00133.73 C ANISOU 1053 CG1 VAL A 204 25459 15827 9524 3712 712 1942 C ATOM 1054 CG2 VAL A 204 59.236-132.241 185.538 1.00133.74 C ANISOU 1054 CG2 VAL A 204 24866 16599 9350 3484 364 1854 C ATOM 1055 N ALA A 205 60.665-129.598 184.100 1.00110.38 N ANISOU 1055 N ALA A 205 20818 14036 7085 4265 18 2208 N ATOM 1056 CA ALA A 205 60.313-128.649 183.049 1.00107.15 C ANISOU 1056 CA ALA A 205 20062 13956 6692 4366 -156 2222 C ATOM 1057 C ALA A 205 61.550-127.954 182.494 1.00104.52 C ANISOU 1057 C ALA A 205 19450 13538 6724 4686 -159 2355 C ATOM 1058 O ALA A 205 61.687-127.801 181.275 1.00108.30 O ANISOU 1058 O ALA A 205 19886 14095 7167 4774 -204 2352 O ATOM 1059 CB ALA A 205 59.311-127.624 183.578 1.00109.00 C ANISOU 1059 CB ALA A 205 19919 14559 6937 4311 -324 2207 C ATOM 1060 N VAL A 206 62.461-127.525 183.372 1.00102.30 N ANISOU 1060 N VAL A 206 18972 13120 6779 4834 -100 2444 N ATOM 1061 CA VAL A 206 63.674-126.861 182.905 1.00100.93 C ANISOU 1061 CA VAL A 206 18532 12900 6918 5072 -73 2514 C ATOM 1062 C VAL A 206 64.606-127.858 182.226 1.00105.66 C ANISOU 1062 C VAL A 206 19445 13249 7452 5156 60 2493 C ATOM 1063 O VAL A 206 65.374-127.488 181.328 1.00106.24 O ANISOU 1063 O VAL A 206 19378 13336 7650 5310 65 2514 O ATOM 1064 CB VAL A 206 64.367-126.128 184.072 1.00 99.90 C ANISOU 1064 CB VAL A 206 18095 12748 7116 5154 -32 2569 C ATOM 1065 CG1 VAL A 206 64.825-127.113 185.137 1.00108.85 C ANISOU 1065 CG1 VAL A 206 19500 13633 8226 5126 111 2553 C ATOM 1066 CG2 VAL A 206 65.538-125.295 183.569 1.00 94.07 C ANISOU 1066 CG2 VAL A 206 17059 12032 6650 5332 2 2602 C ATOM 1067 N LEU A 207 64.550-129.133 182.620 1.00107.08 N ANISOU 1067 N LEU A 207 20067 13192 7425 5053 181 2441 N ATOM 1068 CA LEU A 207 65.381-130.138 181.966 1.00108.29 C ANISOU 1068 CA LEU A 207 20549 13098 7498 5142 314 2413 C ATOM 1069 C LEU A 207 64.870-130.453 180.565 1.00109.13 C ANISOU 1069 C LEU A 207 20833 13267 7364 5072 261 2369 C ATOM 1070 O LEU A 207 65.666-130.666 179.643 1.00110.32 O ANISOU 1070 O LEU A 207 21031 13332 7553 5219 304 2377 O ATOM 1071 CB LEU A 207 65.442-131.408 182.815 1.00109.72 C ANISOU 1071 CB LEU A 207 21182 12982 7525 5052 480 2360 C ATOM 1072 CG LEU A 207 66.354-131.356 184.043 1.00107.85 C ANISOU 1072 CG LEU A 207 20824 12632 7521 5201 576 2392 C ATOM 1073 CD1 LEU A 207 66.337-132.686 184.782 1.00108.22 C ANISOU 1073 CD1 LEU A 207 21369 12365 7384 5122 750 2330 C ATOM 1074 CD2 LEU A 207 67.771-130.978 183.641 1.00104.59 C ANISOU 1074 CD2 LEU A 207 20163 12239 7339 5472 618 2421 C ATOM 1075 N ILE A 208 63.548-130.483 180.384 1.00113.38 N ANISOU 1075 N ILE A 208 21457 13989 7633 4837 170 2304 N ATOM 1076 CA ILE A 208 62.984-130.756 179.066 1.00107.30 C ANISOU 1076 CA ILE A 208 20829 13340 6600 4745 116 2234 C ATOM 1077 C ILE A 208 63.305-129.623 178.099 1.00118.94 C ANISOU 1077 C ILE A 208 21884 15032 8277 4962 -16 2307 C ATOM 1078 O ILE A 208 63.670-129.861 176.940 1.00117.74 O ANISOU 1078 O ILE A 208 21819 14845 8072 5041 -7 2300 O ATOM 1079 CB ILE A 208 61.467-131.000 179.174 1.00109.19 C ANISOU 1079 CB ILE A 208 21206 13810 6470 4407 56 2092 C ATOM 1080 CG1 ILE A 208 61.189-132.387 179.758 1.00111.43 C ANISOU 1080 CG1 ILE A 208 22035 13818 6486 4120 244 1966 C ATOM 1081 CG2 ILE A 208 60.795-130.849 177.817 1.00115.63 C ANISOU 1081 CG2 ILE A 208 21972 14909 7054 4341 -55 2006 C ATOM 1082 CD1 ILE A 208 59.717-132.683 179.952 1.00113.50 C ANISOU 1082 CD1 ILE A 208 22436 14321 6369 3704 223 1756 C ATOM 1083 N LEU A 209 63.186-128.373 178.556 1.00114.86 N ANISOU 1083 N LEU A 209 20920 14723 7997 5052 -126 2371 N ATOM 1084 CA LEU A 209 63.471-127.240 177.682 1.00115.76 C ANISOU 1084 CA LEU A 209 20656 15017 8309 5235 -223 2424 C ATOM 1085 C LEU A 209 64.947-127.164 177.316 1.00120.01 C ANISOU 1085 C LEU A 209 21138 15357 9103 5435 -116 2475 C ATOM 1086 O LEU A 209 65.294-126.632 176.255 1.00123.27 O ANISOU 1086 O LEU A 209 21398 15847 9591 5554 -151 2489 O ATOM 1087 CB LEU A 209 63.021-125.937 178.343 1.00112.48 C ANISOU 1087 CB LEU A 209 19814 14834 8090 5264 -332 2465 C ATOM 1088 CG LEU A 209 61.521-125.796 178.607 1.00113.48 C ANISOU 1088 CG LEU A 209 19897 15256 7962 5093 -466 2397 C ATOM 1089 CD1 LEU A 209 61.203-124.418 179.164 1.00114.44 C ANISOU 1089 CD1 LEU A 209 19572 15590 8320 5171 -565 2447 C ATOM 1090 CD2 LEU A 209 60.724-126.063 177.339 1.00112.44 C ANISOU 1090 CD2 LEU A 209 19862 15350 7511 5031 -554 2304 C ATOM 1091 N ALA A 210 65.827-127.685 178.170 1.00121.52 N ANISOU 1091 N ALA A 210 21443 15319 9409 5473 18 2486 N ATOM 1092 CA ALA A 210 67.255-127.680 177.890 1.00125.25 C ANISOU 1092 CA ALA A 210 21855 15661 10074 5651 127 2502 C ATOM 1093 C ALA A 210 67.723-128.924 177.147 1.00131.61 C ANISOU 1093 C ALA A 210 23057 16251 10696 5689 226 2462 C ATOM 1094 O ALA A 210 68.785-128.888 176.515 1.00134.03 O ANISOU 1094 O ALA A 210 23309 16510 11107 5843 288 2463 O ATOM 1095 CB ALA A 210 68.050-127.540 179.192 1.00122.07 C ANISOU 1095 CB ALA A 210 21325 15181 9874 5699 222 2517 C ATOM 1096 N TYR A 211 66.959-130.016 177.203 1.00135.74 N ANISOU 1096 N TYR A 211 23992 16649 10933 5535 254 2415 N ATOM 1097 CA TYR A 211 67.362-131.251 176.539 1.00134.47 C ANISOU 1097 CA TYR A 211 24257 16251 10585 5551 369 2368 C ATOM 1098 C TYR A 211 67.031-131.215 175.051 1.00136.37 C ANISOU 1098 C TYR A 211 24534 16595 10685 5542 291 2352 C ATOM 1099 O TYR A 211 67.920-131.346 174.202 1.00135.11 O ANISOU 1099 O TYR A 211 24383 16360 10591 5700 336 2359 O ATOM 1100 CB TYR A 211 66.691-132.450 177.216 1.00133.87 C ANISOU 1100 CB TYR A 211 24653 15970 10241 5345 466 2304 C ATOM 1101 CG TYR A 211 66.933-133.770 176.521 1.00136.34 C ANISOU 1101 CG TYR A 211 25463 16016 10325 5316 599 2240 C ATOM 1102 CD1 TYR A 211 68.155-134.420 176.630 1.00138.34 C ANISOU 1102 CD1 TYR A 211 25872 16021 10669 5525 746 2242 C ATOM 1103 CD2 TYR A 211 65.935-134.372 175.767 1.00138.71 C ANISOU 1103 CD2 TYR A 211 26075 16334 10296 5068 586 2159 C ATOM 1104 CE1 TYR A 211 68.380-135.629 175.999 1.00143.17 C ANISOU 1104 CE1 TYR A 211 26952 16370 11075 5515 874 2184 C ATOM 1105 CE2 TYR A 211 66.149-135.581 175.134 1.00143.58 C ANISOU 1105 CE2 TYR A 211 27163 16687 10704 5016 724 2093 C ATOM 1106 CZ TYR A 211 67.373-136.205 175.253 1.00145.93 C ANISOU 1106 CZ TYR A 211 27625 16700 11121 5253 865 2116 C ATOM 1107 OH TYR A 211 67.590-137.409 174.623 1.00148.74 O ANISOU 1107 OH TYR A 211 28463 16777 11273 5218 1007 2052 O ATOM 1108 N PHE A 212 65.754-131.041 174.718 1.00117.10 N ANISOU 1108 N PHE A 212 16544 17305 10643 6852 -92 1877 N ATOM 1109 CA PHE A 212 65.334-131.003 173.322 1.00123.40 C ANISOU 1109 CA PHE A 212 17430 17929 11530 6849 -31 1765 C ATOM 1110 C PHE A 212 65.884-129.753 172.646 1.00130.52 C ANISOU 1110 C PHE A 212 17856 19272 12464 6722 -29 1741 C ATOM 1111 O PHE A 212 65.637-128.631 173.101 1.00132.28 O ANISOU 1111 O PHE A 212 17833 19666 12761 6412 -90 1767 O ATOM 1112 CB PHE A 212 63.811-131.040 173.227 1.00120.55 C ANISOU 1112 CB PHE A 212 17422 17053 11328 6581 -37 1717 C ATOM 1113 CG PHE A 212 63.204-132.329 173.703 1.00123.97 C ANISOU 1113 CG PHE A 212 18352 17017 11733 6672 -34 1733 C ATOM 1114 CD1 PHE A 212 63.052-133.398 172.836 1.00125.35 C ANISOU 1114 CD1 PHE A 212 18875 16872 11880 6871 16 1656 C ATOM 1115 CD2 PHE A 212 62.785-132.471 175.016 1.00123.80 C ANISOU 1115 CD2 PHE A 212 18458 16881 11701 6537 -86 1827 C ATOM 1116 CE1 PHE A 212 62.494-134.587 173.270 1.00125.90 C ANISOU 1116 CE1 PHE A 212 19411 16507 11918 6922 7 1673 C ATOM 1117 CE2 PHE A 212 62.226-133.657 175.455 1.00123.26 C ANISOU 1117 CE2 PHE A 212 18844 16386 11605 6594 -87 1852 C ATOM 1118 CZ PHE A 212 62.080-134.716 174.580 1.00123.87 C ANISOU 1118 CZ PHE A 212 19266 16138 11661 6780 -43 1775 C ATOM 1119 N ARG A 213 66.631-129.947 171.556 1.00134.40 N ANISOU 1119 N ARG A 213 18230 19953 12883 6950 38 1691 N ATOM 1120 CA ARG A 213 67.216-128.820 170.841 1.00133.70 C ANISOU 1120 CA ARG A 213 17691 20298 12812 6828 46 1677 C ATOM 1121 C ARG A 213 66.175-128.009 170.082 1.00131.70 C ANISOU 1121 C ARG A 213 17456 19840 12745 6527 40 1600 C ATOM 1122 O ARG A 213 66.420-126.835 169.787 1.00132.38 O ANISOU 1122 O ARG A 213 17170 20250 12879 6308 14 1604 O ATOM 1123 CB ARG A 213 68.296-129.312 169.877 1.00137.65 C ANISOU 1123 CB ARG A 213 18080 21065 13157 7162 130 1655 C ATOM 1124 CG ARG A 213 69.483-129.970 170.560 1.00143.08 C ANISOU 1124 CG ARG A 213 18673 22054 13637 7472 141 1740 C ATOM 1125 CD ARG A 213 70.526-130.415 169.548 1.00148.41 C ANISOU 1125 CD ARG A 213 19241 23016 14132 7802 232 1720 C ATOM 1126 NE ARG A 213 71.698-131.000 170.194 1.00155.59 N ANISOU 1126 NE ARG A 213 20036 24252 14828 8109 247 1808 N ATOM 1127 CZ ARG A 213 72.753-131.474 169.540 1.00159.30 C ANISOU 1127 CZ ARG A 213 20406 25031 15089 8442 324 1816 C ATOM 1128 NH1 ARG A 213 72.786-131.436 168.215 1.00158.76 N ANISOU 1128 NH1 ARG A 213 20342 24985 14995 8504 391 1740 N ATOM 1129 NH2 ARG A 213 73.775-131.988 170.210 1.00162.69 N ANISOU 1129 NH2 ARG A 213 20733 25759 15324 8719 334 1905 N ATOM 1130 N ARG A 214 65.024-128.603 169.762 1.00131.70 N ANISOU 1130 N ARG A 214 17882 19312 12845 6495 59 1533 N ATOM 1131 CA ARG A 214 63.976-127.882 169.052 1.00130.67 C ANISOU 1131 CA ARG A 214 17791 18968 12890 6218 56 1462 C ATOM 1132 C ARG A 214 63.265-126.861 169.930 1.00126.02 C ANISOU 1132 C ARG A 214 17099 18382 12402 5856 -22 1507 C ATOM 1133 O ARG A 214 62.508-126.038 169.402 1.00120.95 O ANISOU 1133 O ARG A 214 16412 17655 11888 5609 -33 1460 O ATOM 1134 CB ARG A 214 62.954-128.870 168.483 1.00131.52 C ANISOU 1134 CB ARG A 214 18396 18511 13064 6270 99 1380 C ATOM 1135 CG ARG A 214 63.570-130.038 167.730 1.00136.55 C ANISOU 1135 CG ARG A 214 19230 19087 13565 6627 165 1330 C ATOM 1136 CD ARG A 214 64.393-129.568 166.541 1.00139.34 C ANISOU 1136 CD ARG A 214 19271 19807 13863 6736 214 1286 C ATOM 1137 NE ARG A 214 65.067-130.679 165.876 1.00144.22 N ANISOU 1137 NE ARG A 214 20075 20416 14307 7097 274 1247 N ATOM 1138 CZ ARG A 214 64.541-131.385 164.880 1.00144.23 C ANISOU 1138 CZ ARG A 214 20414 20075 14311 7170 309 1148 C ATOM 1139 NH1 ARG A 214 63.328-131.096 164.428 1.00140.65 N ANISOU 1139 NH1 ARG A 214 20137 19264 14042 6899 296 1079 N ATOM 1140 NH2 ARG A 214 65.228-132.380 164.335 1.00146.82 N ANISOU 1140 NH2 ARG A 214 20910 20427 14447 7509 351 1120 N ATOM 1141 N LEU A 215 63.488-126.891 171.244 1.00124.54 N ANISOU 1141 N LEU A 215 16881 18297 12141 5821 -77 1593 N ATOM 1142 CA LEU A 215 62.836-125.988 172.181 1.00119.96 C ANISOU 1142 CA LEU A 215 16239 17730 11612 5482 -150 1631 C ATOM 1143 C LEU A 215 63.749-124.851 172.629 1.00123.40 C ANISOU 1143 C LEU A 215 16199 18704 11982 5329 -218 1677 C ATOM 1144 O LEU A 215 63.478-124.213 173.652 1.00132.22 O ANISOU 1144 O LEU A 215 17256 19899 13082 5084 -287 1714 O ATOM 1145 CB LEU A 215 62.333-126.768 173.397 1.00120.19 C ANISOU 1145 CB LEU A 215 16590 17479 11596 5492 -168 1692 C ATOM 1146 CG LEU A 215 61.395-127.945 173.121 1.00117.07 C ANISOU 1146 CG LEU A 215 16696 16530 11257 5584 -114 1658 C ATOM 1147 CD1 LEU A 215 61.081-128.693 174.407 1.00116.84 C ANISOU 1147 CD1 LEU A 215 16935 16296 11161 5587 -138 1739 C ATOM 1148 CD2 LEU A 215 60.117-127.468 172.451 1.00113.30 C ANISOU 1148 CD2 LEU A 215 16375 15741 10933 5324 -92 1589 C ATOM 1149 N HIS A 216 64.822-124.585 171.888 1.00110.01 N ANISOU 1149 N HIS A 216 14176 17385 10240 5447 -197 1672 N ATOM 1150 CA HIS A 216 65.801-123.564 172.253 1.00 99.21 C ANISOU 1150 CA HIS A 216 12349 16544 8803 5285 -261 1720 C ATOM 1151 C HIS A 216 65.479-122.283 171.491 1.00 96.93 C ANISOU 1151 C HIS A 216 11838 16376 8617 4969 -289 1667 C ATOM 1152 O HIS A 216 65.776-122.165 170.299 1.00101.46 O ANISOU 1152 O HIS A 216 12285 17045 9222 5041 -236 1628 O ATOM 1153 CB HIS A 216 67.218-124.044 171.959 1.00 95.68 C ANISOU 1153 CB HIS A 216 11668 16468 8217 5583 -213 1764 C ATOM 1154 CG HIS A 216 67.628-125.245 172.752 1.00 95.52 C ANISOU 1154 CG HIS A 216 11846 16371 8076 5896 -193 1821 C ATOM 1155 ND1 HIS A 216 68.800-125.930 172.514 1.00 98.33 N ANISOU 1155 ND1 HIS A 216 12086 16994 8281 6232 -134 1858 N ATOM 1156 CD2 HIS A 216 67.022-125.883 173.781 1.00 94.38 C ANISOU 1156 CD2 HIS A 216 12016 15920 7926 5920 -223 1853 C ATOM 1157 CE1 HIS A 216 68.898-126.938 173.362 1.00 99.14 C ANISOU 1157 CE1 HIS A 216 12425 16947 8295 6459 -135 1907 C ATOM 1158 NE2 HIS A 216 67.832-126.932 174.142 1.00 98.31 N ANISOU 1158 NE2 HIS A 216 12582 16489 8280 6267 -190 1907 N ATOM 1159 N CYS A 217 64.873-121.322 172.184 1.00 90.54 N ANISOU 1159 N CYS A 217 10992 15565 7843 4616 -372 1661 N ATOM 1160 CA CYS A 217 64.589-120.016 171.604 1.00 88.18 C ANISOU 1160 CA CYS A 217 10488 15344 7673 4226 -386 1576 C ATOM 1161 C CYS A 217 64.453-119.008 172.737 1.00 87.25 C ANISOU 1161 C CYS A 217 10262 15329 7562 3832 -467 1558 C ATOM 1162 O CYS A 217 64.411-119.370 173.915 1.00 86.51 O ANISOU 1162 O CYS A 217 10284 15210 7376 3871 -507 1609 O ATOM 1163 CB CYS A 217 63.330-120.048 170.730 1.00 86.54 C ANISOU 1163 CB CYS A 217 10548 14643 7691 4084 -289 1435 C ATOM 1164 SG CYS A 217 61.833-120.614 171.571 1.00 84.09 S ANISOU 1164 SG CYS A 217 10699 13752 7499 3957 -241 1366 S ATOM 1165 N THR A 218 64.387-117.729 172.357 1.00 86.94 N ANISOU 1165 N THR A 218 10014 15397 7624 3454 -495 1483 N ATOM 1166 CA THR A 218 64.314-116.658 173.348 1.00 90.16 C ANISOU 1166 CA THR A 218 10322 15908 8027 3068 -582 1451 C ATOM 1167 C THR A 218 63.073-116.794 174.223 1.00 84.13 C ANISOU 1167 C THR A 218 9897 14708 7362 2920 -544 1364 C ATOM 1168 O THR A 218 63.115-116.500 175.424 1.00 80.86 O ANISOU 1168 O THR A 218 9486 14375 6862 2783 -611 1379 O ATOM 1169 CB THR A 218 64.333-115.296 172.648 1.00 94.46 C ANISOU 1169 CB THR A 218 10652 16560 8680 2693 -611 1375 C ATOM 1170 OG1 THR A 218 65.542-115.166 171.889 1.00102.89 O ANISOU 1170 OG1 THR A 218 11377 18084 9631 2813 -649 1476 O ATOM 1171 CG2 THR A 218 64.258-114.163 173.663 1.00 91.07 C ANISOU 1171 CG2 THR A 218 10159 16209 8235 2294 -710 1329 C ATOM 1172 N ARG A 219 61.960-117.248 173.640 1.00 80.60 N ANISOU 1172 N ARG A 219 9729 13813 7081 2943 -437 1277 N ATOM 1173 CA ARG A 219 60.730-117.404 174.411 1.00 78.19 C ANISOU 1173 CA ARG A 219 9729 13115 6866 2799 -391 1205 C ATOM 1174 C ARG A 219 60.904-118.423 175.530 1.00 84.39 C ANISOU 1174 C ARG A 219 10676 13895 7493 3033 -410 1311 C ATOM 1175 O ARG A 219 60.418-118.217 176.649 1.00 82.64 O ANISOU 1175 O ARG A 219 10562 13593 7247 2866 -429 1293 O ATOM 1176 CB ARG A 219 59.583-117.813 173.487 1.00 75.21 C ANISOU 1176 CB ARG A 219 9598 12301 6676 2799 -279 1114 C ATOM 1177 CG ARG A 219 58.216-117.791 174.149 1.00 79.77 C ANISOU 1177 CG ARG A 219 10444 12503 7362 2590 -225 1032 C ATOM 1178 CD ARG A 219 57.153-118.434 173.270 1.00 81.65 C ANISOU 1178 CD ARG A 219 10933 12337 7753 2630 -123 973 C ATOM 1179 NE ARG A 219 57.236-119.892 173.281 1.00 92.44 N ANISOU 1179 NE ARG A 219 12536 13553 9034 2962 -95 1065 N ATOM 1180 CZ ARG A 219 57.847-120.618 172.349 1.00 93.78 C ANISOU 1180 CZ ARG A 219 12712 13758 9162 3263 -84 1109 C ATOM 1181 NH1 ARG A 219 58.432-120.024 171.319 1.00 90.09 N ANISOU 1181 NH1 ARG A 219 12001 13500 8729 3266 -92 1078 N ATOM 1182 NH2 ARG A 219 57.869-121.940 172.446 1.00 98.50 N ANISOU 1182 NH2 ARG A 219 13573 14178 9672 3564 -66 1187 N ATOM 1183 N ASN A 220 61.597-119.529 175.251 1.00 86.53 N ANISOU 1183 N ASN A 220 10978 14253 7645 3435 -405 1424 N ATOM 1184 CA ASN A 220 61.824-120.540 176.276 1.00 84.57 C ANISOU 1184 CA ASN A 220 10898 13999 7234 3688 -430 1541 C ATOM 1185 C ASN A 220 62.928-120.139 177.245 1.00 87.37 C ANISOU 1185 C ASN A 220 10984 14823 7390 3696 -547 1640 C ATOM 1186 O ASN A 220 62.930-120.595 178.394 1.00 94.30 O ANISOU 1186 O ASN A 220 11984 15700 8145 3764 -582 1714 O ATOM 1187 CB ASN A 220 62.154-121.885 175.629 1.00 86.48 C ANISOU 1187 CB ASN A 220 11309 14139 7410 4141 -388 1623 C ATOM 1188 CG ASN A 220 60.953-122.513 174.950 1.00 86.21 C ANISOU 1188 CG ASN A 220 11630 13585 7542 4133 -286 1540 C ATOM 1189 OD1 ASN A 220 59.809-122.262 175.332 1.00 86.18 O ANISOU 1189 OD1 ASN A 220 11804 13277 7663 3845 -246 1461 O ATOM 1190 ND2 ASN A 220 61.207-123.337 173.941 1.00 89.62 N ANISOU 1190 ND2 ASN A 220 12165 13926 7962 4452 -246 1558 N ATOM 1191 N TYR A 221 63.870-119.300 176.807 1.00 81.32 N ANISOU 1191 N TYR A 221 9851 14469 6577 3615 -612 1652 N ATOM 1192 CA TYR A 221 64.882-118.792 177.728 1.00 84.26 C ANISOU 1192 CA TYR A 221 9948 15307 6760 3553 -737 1741 C ATOM 1193 C TYR A 221 64.249-117.924 178.809 1.00 80.44 C ANISOU 1193 C TYR A 221 9528 14730 6306 3159 -780 1657 C ATOM 1194 O TYR A 221 64.652-117.984 179.976 1.00 76.88 O ANISOU 1194 O TYR A 221 9048 14474 5689 3165 -861 1730 O ATOM 1195 CB TYR A 221 65.949-118.006 176.965 1.00 91.51 C ANISOU 1195 CB TYR A 221 10459 16656 7653 3472 -788 1759 C ATOM 1196 CG TYR A 221 66.674-118.808 175.908 1.00100.43 C ANISOU 1196 CG TYR A 221 11494 17864 8800 3820 -703 1800 C ATOM 1197 CD1 TYR A 221 66.817-120.185 176.025 1.00104.61 C ANISOU 1197 CD1 TYR A 221 12227 18232 9290 4221 -630 1852 C ATOM 1198 CD2 TYR A 221 67.216-118.186 174.790 1.00103.65 C ANISOU 1198 CD2 TYR A 221 11625 18504 9253 3742 -691 1782 C ATOM 1199 CE1 TYR A 221 67.479-120.920 175.059 1.00108.90 C ANISOU 1199 CE1 TYR A 221 12709 18844 9825 4548 -543 1869 C ATOM 1200 CE2 TYR A 221 67.878-118.912 173.819 1.00107.21 C ANISOU 1200 CE2 TYR A 221 11996 19044 9697 4065 -598 1809 C ATOM 1201 CZ TYR A 221 68.007-120.277 173.958 1.00112.51 C ANISOU 1201 CZ TYR A 221 12881 19551 10315 4474 -523 1846 C ATOM 1202 OH TYR A 221 68.667-121.001 172.993 1.00118.33 O ANISOU 1202 OH TYR A 221 13567 20375 11020 4802 -423 1856 O ATOM 1203 N ILE A 222 63.256-117.113 178.437 1.00 79.44 N ANISOU 1203 N ILE A 222 9494 14312 6378 2828 -728 1502 N ATOM 1204 CA ILE A 222 62.531-116.320 179.424 1.00 77.32 C ANISOU 1204 CA ILE A 222 9327 13912 6140 2486 -752 1405 C ATOM 1205 C ILE A 222 61.753-117.228 180.367 1.00 79.86 C ANISOU 1205 C ILE A 222 9966 13950 6428 2604 -698 1431 C ATOM 1206 O ILE A 222 61.624-116.934 181.563 1.00 84.34 O ANISOU 1206 O ILE A 222 10578 14570 6897 2462 -748 1426 O ATOM 1207 CB ILE A 222 61.610-115.306 178.718 1.00 71.44 C ANISOU 1207 CB ILE A 222 8622 12908 5614 2157 -699 1237 C ATOM 1208 CG1 ILE A 222 62.428-114.391 177.806 1.00 72.16 C ANISOU 1208 CG1 ILE A 222 8405 13291 5724 2020 -762 1229 C ATOM 1209 CG2 ILE A 222 60.826-114.484 179.732 1.00 61.14 C ANISOU 1209 CG2 ILE A 222 7441 11462 4328 1839 -716 1127 C ATOM 1210 CD1 ILE A 222 61.597-113.381 177.042 1.00 68.98 C ANISOU 1210 CD1 ILE A 222 8040 12640 5527 1717 -719 1078 C ATOM 1211 N HIS A 223 61.236-118.347 179.854 1.00 73.12 N ANISOU 1211 N HIS A 223 9345 12795 5642 2857 -600 1462 N ATOM 1212 CA HIS A 223 60.537-119.301 180.707 1.00 78.31 C ANISOU 1212 CA HIS A 223 10316 13185 6255 2969 -553 1511 C ATOM 1213 C HIS A 223 61.486-119.944 181.712 1.00 80.72 C ANISOU 1213 C HIS A 223 10579 13774 6317 3214 -640 1671 C ATOM 1214 O HIS A 223 61.111-120.174 182.867 1.00 71.07 O ANISOU 1214 O HIS A 223 9513 12484 5005 3166 -650 1705 O ATOM 1215 CB HIS A 223 59.856-120.370 179.853 1.00 80.44 C ANISOU 1215 CB HIS A 223 10854 13071 6639 3174 -446 1517 C ATOM 1216 CG HIS A 223 58.742-119.846 179.001 1.00 83.65 C ANISOU 1216 CG HIS A 223 11342 13166 7277 2927 -357 1368 C ATOM 1217 ND1 HIS A 223 58.257-118.561 179.116 1.00 83.16 N ANISOU 1217 ND1 HIS A 223 11165 13119 7314 2567 -361 1238 N ATOM 1218 CD2 HIS A 223 58.016-120.435 178.021 1.00 82.83 C ANISOU 1218 CD2 HIS A 223 11429 12727 7315 2996 -267 1329 C ATOM 1219 CE1 HIS A 223 57.281-118.380 178.243 1.00 80.05 C ANISOU 1219 CE1 HIS A 223 10872 12428 7114 2438 -274 1132 C ATOM 1220 NE2 HIS A 223 57.116-119.502 177.566 1.00 81.07 N ANISOU 1220 NE2 HIS A 223 11181 12349 7274 2681 -218 1185 N ATOM 1221 N MET A 224 62.718-120.242 181.291 1.00 84.94 N ANISOU 1221 N MET A 224 10895 14648 6731 3486 -701 1778 N ATOM 1222 CA MET A 224 63.676-120.865 182.198 1.00 88.80 C ANISOU 1222 CA MET A 224 11317 15417 7006 3731 -780 1928 C ATOM 1223 C MET A 224 64.114-119.908 183.301 1.00 87.12 C ANISOU 1223 C MET A 224 10898 15522 6682 3455 -888 1917 C ATOM 1224 O MET A 224 64.398-120.347 184.422 1.00 86.66 O ANISOU 1224 O MET A 224 10888 15526 6514 3517 -924 1988 O ATOM 1225 CB MET A 224 64.882-121.382 181.411 1.00 92.17 C ANISOU 1225 CB MET A 224 11522 16062 7436 4024 -770 1982 C ATOM 1226 CG MET A 224 64.543-122.545 180.484 1.00 94.34 C ANISOU 1226 CG MET A 224 12053 16002 7792 4348 -666 1992 C ATOM 1227 SD MET A 224 65.817-122.932 179.265 1.00 97.91 S ANISOU 1227 SD MET A 224 12238 16714 8250 4661 -625 2009 S ATOM 1228 CE MET A 224 67.097-123.636 180.297 1.00 98.58 C ANISOU 1228 CE MET A 224 12186 17105 8164 4911 -663 2127 C ATOM 1229 N HIS A 225 64.171-118.606 183.009 1.00 83.75 N ANISOU 1229 N HIS A 225 10256 15279 6287 3136 -942 1824 N ATOM 1230 CA HIS A 225 64.411-117.626 184.064 1.00 82.27 C ANISOU 1230 CA HIS A 225 9937 15333 5989 2830 -1051 1790 C ATOM 1231 C HIS A 225 63.253-117.594 185.052 1.00 80.29 C ANISOU 1231 C HIS A 225 9984 14754 5770 2653 -1000 1711 C ATOM 1232 O HIS A 225 63.467-117.540 186.269 1.00 73.03 O ANISOU 1232 O HIS A 225 9074 13996 4677 2605 -1075 1757 O ATOM 1233 CB HIS A 225 64.631-116.239 183.461 1.00 87.12 C ANISOU 1233 CB HIS A 225 10308 16103 6691 2480 -1103 1676 C ATOM 1234 CG HIS A 225 66.004-116.028 182.906 1.00 94.10 C ANISOU 1234 CG HIS A 225 10825 17400 7529 2537 -1173 1751 C ATOM 1235 ND1 HIS A 225 66.989-115.355 183.597 1.00 96.22 N ANISOU 1235 ND1 HIS A 225 10838 18023 7698 2340 -1287 1773 N ATOM 1236 CD2 HIS A 225 66.556-116.393 181.725 1.00 94.47 C ANISOU 1236 CD2 HIS A 225 10719 17526 7650 2740 -1120 1793 C ATOM 1237 CE1 HIS A 225 68.089-115.317 182.867 1.00 97.57 C ANISOU 1237 CE1 HIS A 225 10704 18487 7881 2414 -1296 1835 C ATOM 1238 NE2 HIS A 225 67.853-115.941 181.727 1.00 97.46 N ANISOU 1238 NE2 HIS A 225 10742 18320 7969 2663 -1191 1845 N ATOM 1239 N LEU A 226 62.019-117.622 184.545 1.00 79.01 N ANISOU 1239 N LEU A 226 10053 14153 5814 2552 -874 1596 N ATOM 1240 CA LEU A 226 60.855-117.645 185.423 1.00 81.85 C ANISOU 1240 CA LEU A 226 10684 14215 6201 2398 -809 1530 C ATOM 1241 C LEU A 226 60.798-118.938 186.225 1.00 83.56 C ANISOU 1241 C LEU A 226 11115 14354 6279 2672 -790 1679 C ATOM 1242 O LEU A 226 60.379-118.936 187.389 1.00 85.31 O ANISOU 1242 O LEU A 226 11467 14548 6399 2574 -797 1686 O ATOM 1243 CB LEU A 226 59.579-117.461 184.600 1.00 77.08 C ANISOU 1243 CB LEU A 226 10250 13194 5843 2254 -677 1394 C ATOM 1244 CG LEU A 226 58.257-117.373 185.362 1.00 75.02 C ANISOU 1244 CG LEU A 226 10239 12638 5628 2070 -593 1312 C ATOM 1245 CD1 LEU A 226 58.276-116.206 186.331 1.00 76.70 C ANISOU 1245 CD1 LEU A 226 10369 13025 5749 1790 -665 1216 C ATOM 1246 CD2 LEU A 226 57.100-117.238 184.391 1.00 71.80 C ANISOU 1246 CD2 LEU A 226 9954 11868 5459 1958 -470 1196 C ATOM 1247 N PHE A 227 61.216-120.053 185.621 1.00 84.80 N ANISOU 1247 N PHE A 227 11328 14472 6422 3024 -767 1802 N ATOM 1248 CA PHE A 227 61.264-121.315 186.351 1.00 86.46 C ANISOU 1248 CA PHE A 227 11761 14605 6486 3309 -764 1961 C ATOM 1249 C PHE A 227 62.292-121.261 187.474 1.00 89.56 C ANISOU 1249 C PHE A 227 11979 15367 6684 3352 -880 2050 C ATOM 1250 O PHE A 227 62.025-121.719 188.592 1.00 91.73 O ANISOU 1250 O PHE A 227 12421 15572 6860 3356 -883 2110 O ATOM 1251 CB PHE A 227 61.585-122.468 185.399 1.00 85.11 C ANISOU 1251 CB PHE A 227 11691 14298 6349 3686 -722 2053 C ATOM 1252 CG PHE A 227 60.492-122.770 184.411 1.00 77.82 C ANISOU 1252 CG PHE A 227 10998 12929 5640 3636 -599 1964 C ATOM 1253 CD1 PHE A 227 59.216-122.260 184.583 1.00 71.18 C ANISOU 1253 CD1 PHE A 227 10295 11805 4944 3301 -520 1838 C ATOM 1254 CD2 PHE A 227 60.744-123.574 183.312 1.00 77.28 C ANISOU 1254 CD2 PHE A 227 11006 12734 5624 3929 -562 2004 C ATOM 1255 CE1 PHE A 227 58.215-122.543 183.673 1.00 68.75 C ANISOU 1255 CE1 PHE A 227 10179 11112 4832 3241 -413 1762 C ATOM 1256 CE2 PHE A 227 59.747-123.860 182.401 1.00 75.64 C ANISOU 1256 CE2 PHE A 227 11012 12117 5610 3864 -458 1917 C ATOM 1257 CZ PHE A 227 58.481-123.343 182.582 1.00 73.10 C ANISOU 1257 CZ PHE A 227 10809 11531 5434 3510 -386 1801 C ATOM 1258 N LEU A 228 63.471-120.699 187.196 1.00 89.52 N ANISOU 1258 N LEU A 228 11625 15730 6659 3345 -965 2046 N ATOM 1259 CA LEU A 228 64.535-120.654 188.192 1.00 88.43 C ANISOU 1259 CA LEU A 228 11289 15928 6382 3358 -1067 2115 C ATOM 1260 C LEU A 228 64.163-119.777 189.381 1.00 87.76 C ANISOU 1260 C LEU A 228 11220 15934 6191 3035 -1132 2054 C ATOM 1261 O LEU A 228 64.550-120.080 190.516 1.00 93.12 O ANISOU 1261 O LEU A 228 11910 16733 6740 3067 -1187 2124 O ATOM 1262 CB LEU A 228 65.828-120.159 187.546 1.00 90.56 C ANISOU 1262 CB LEU A 228 11169 16580 6658 3378 -1132 2121 C ATOM 1263 CG LEU A 228 67.079-120.087 188.423 1.00 98.21 C ANISOU 1263 CG LEU A 228 11885 17945 7487 3396 -1235 2199 C ATOM 1264 CD1 LEU A 228 67.446-121.463 188.961 1.00 99.83 C ANISOU 1264 CD1 LEU A 228 12223 18090 7617 3763 -1206 2333 C ATOM 1265 CD2 LEU A 228 68.236-119.482 187.640 1.00 99.25 C ANISOU 1265 CD2 LEU A 228 11626 18449 7637 3362 -1281 2198 C ATOM 1266 N SER A 229 63.417-118.695 189.146 1.00 80.21 N ANISOU 1266 N SER A 229 10278 14920 5279 2731 -1127 1916 N ATOM 1267 CA SER A 229 63.034-117.812 190.243 1.00 79.23 C ANISOU 1267 CA SER A 229 10188 14867 5047 2427 -1182 1831 C ATOM 1268 C SER A 229 62.084-118.510 191.211 1.00 80.55 C ANISOU 1268 C SER A 229 10676 14786 5145 2476 -1109 1869 C ATOM 1269 O SER A 229 62.190-118.330 192.429 1.00 83.19 O ANISOU 1269 O SER A 229 11031 15239 5341 2370 -1165 1876 O ATOM 1270 CB SER A 229 62.399-116.536 189.694 1.00 74.26 C ANISOU 1270 CB SER A 229 9527 14153 4534 2094 -1167 1644 C ATOM 1271 OG SER A 229 61.168-116.816 189.051 1.00 71.84 O ANISOU 1271 OG SER A 229 9450 13397 4448 2083 -1009 1560 O ATOM 1272 N PHE A 230 61.149-119.308 190.688 1.00 81.62 N ANISOU 1272 N PHE A 230 11065 14561 5386 2614 -979 1893 N ATOM 1273 CA PHE A 230 60.241-120.044 191.561 1.00 81.68 C ANISOU 1273 CA PHE A 230 11377 14318 5340 2643 -901 1947 C ATOM 1274 C PHE A 230 60.933-121.227 192.227 1.00 85.72 C ANISOU 1274 C PHE A 230 11943 14877 5748 2915 -940 2123 C ATOM 1275 O PHE A 230 60.540-121.634 193.326 1.00 79.53 O ANISOU 1275 O PHE A 230 11333 14028 4858 2891 -928 2180 O ATOM 1276 CB PHE A 230 59.018-120.516 190.773 1.00 73.49 C ANISOU 1276 CB PHE A 230 10579 12820 4525 2626 -745 1892 C ATOM 1277 CG PHE A 230 57.973-119.455 190.583 1.00 72.63 C ANISOU 1277 CG PHE A 230 10481 12536 4579 2285 -668 1689 C ATOM 1278 CD1 PHE A 230 57.004-119.239 191.549 1.00 70.88 C ANISOU 1278 CD1 PHE A 230 10421 12201 4310 2098 -607 1637 C ATOM 1279 CD2 PHE A 230 57.959-118.672 189.439 1.00 69.16 C ANISOU 1279 CD2 PHE A 230 9890 12057 4328 2165 -653 1556 C ATOM 1280 CE1 PHE A 230 56.041-118.263 191.381 1.00 73.91 C ANISOU 1280 CE1 PHE A 230 10815 12438 4830 1822 -533 1450 C ATOM 1281 CE2 PHE A 230 56.997-117.694 189.265 1.00 68.41 C ANISOU 1281 CE2 PHE A 230 9818 11798 4376 1877 -585 1374 C ATOM 1282 CZ PHE A 230 56.038-117.489 190.236 1.00 72.60 C ANISOU 1282 CZ PHE A 230 10510 12219 4856 1717 -525 1319 C ATOM 1283 N MET A 231 61.957-121.791 191.581 1.00 82.19 N ANISOU 1283 N MET A 231 11349 14536 5344 3170 -977 2201 N ATOM 1284 CA MET A 231 62.701-122.886 192.195 1.00 86.54 C ANISOU 1284 CA MET A 231 11934 15137 5810 3439 -1011 2351 C ATOM 1285 C MET A 231 63.521-122.397 193.382 1.00 89.94 C ANISOU 1285 C MET A 231 12169 15925 6078 3335 -1129 2373 C ATOM 1286 O MET A 231 63.572-123.061 194.424 1.00 86.81 O ANISOU 1286 O MET A 231 11902 15514 5566 3418 -1147 2473 O ATOM 1287 CB MET A 231 63.602-123.556 191.158 1.00 91.26 C ANISOU 1287 CB MET A 231 12412 15778 6486 3754 -1007 2409 C ATOM 1288 CG MET A 231 62.849-124.361 190.113 1.00 94.65 C ANISOU 1288 CG MET A 231 13100 15808 7056 3916 -895 2411 C ATOM 1289 SD MET A 231 63.888-124.870 188.729 1.00 97.40 S ANISOU 1289 SD MET A 231 13272 16240 7494 4251 -882 2428 S ATOM 1290 CE MET A 231 65.097-125.890 189.568 1.00100.11 C ANISOU 1290 CE MET A 231 13563 16781 7693 4575 -938 2576 C ATOM 1291 N LEU A 232 64.168-121.237 193.245 1.00 89.95 N ANISOU 1291 N LEU A 232 11869 16242 6064 3138 -1216 2283 N ATOM 1292 CA LEU A 232 64.939-120.688 194.355 1.00 91.49 C ANISOU 1292 CA LEU A 232 11885 16771 6105 3000 -1337 2291 C ATOM 1293 C LEU A 232 64.035-120.230 195.492 1.00 90.62 C ANISOU 1293 C LEU A 232 11968 16572 5892 2750 -1335 2227 C ATOM 1294 O LEU A 232 64.434-120.290 196.661 1.00 89.49 O ANISOU 1294 O LEU A 232 11811 16592 5598 2722 -1408 2278 O ATOM 1295 CB LEU A 232 65.814-119.534 193.866 1.00 91.58 C ANISOU 1295 CB LEU A 232 11548 17114 6133 2811 -1432 2208 C ATOM 1296 CG LEU A 232 66.891-119.897 192.842 1.00 96.77 C ANISOU 1296 CG LEU A 232 11953 17953 6862 3046 -1437 2277 C ATOM 1297 CD1 LEU A 232 67.747-118.686 192.505 1.00 98.07 C ANISOU 1297 CD1 LEU A 232 11769 18468 7025 2798 -1536 2206 C ATOM 1298 CD2 LEU A 232 67.753-121.044 193.350 1.00 91.00 C ANISOU 1298 CD2 LEU A 232 11195 17341 6039 3381 -1452 2437 C ATOM 1299 N ARG A 233 62.824-119.767 195.172 1.00 90.31 N ANISOU 1299 N ARG A 233 12102 16286 5924 2574 -1247 2114 N ATOM 1300 CA ARG A 233 61.861-119.432 196.216 1.00 91.85 C ANISOU 1300 CA ARG A 233 12501 16380 6019 2370 -1213 2051 C ATOM 1301 C ARG A 233 61.478-120.668 197.020 1.00 92.34 C ANISOU 1301 C ARG A 233 12811 16266 6007 2550 -1157 2199 C ATOM 1302 O ARG A 233 61.299-120.594 198.241 1.00 92.07 O ANISOU 1302 O ARG A 233 12859 16297 5826 2447 -1183 2210 O ATOM 1303 CB ARG A 233 60.620-118.791 195.597 1.00 89.13 C ANISOU 1303 CB ARG A 233 12288 15804 5774 2188 -1107 1906 C ATOM 1304 CG ARG A 233 59.566-118.364 196.605 1.00 88.92 C ANISOU 1304 CG ARG A 233 12455 15687 5644 1980 -1051 1821 C ATOM 1305 CD ARG A 233 58.205-118.239 195.943 1.00 87.60 C ANISOU 1305 CD ARG A 233 12464 15178 5643 1883 -892 1717 C ATOM 1306 NE ARG A 233 57.220-117.604 196.812 1.00 92.36 N ANISOU 1306 NE ARG A 233 13196 15702 6194 1650 -827 1589 N ATOM 1307 CZ ARG A 233 55.928-117.502 196.522 1.00 91.81 C ANISOU 1307 CZ ARG A 233 13278 15324 6282 1533 -675 1489 C ATOM 1308 NH1 ARG A 233 55.463-118.000 195.384 1.00 89.07 N ANISOU 1308 NH1 ARG A 233 12979 14706 6158 1607 -580 1504 N ATOM 1309 NH2 ARG A 233 55.099-116.907 197.369 1.00 89.18 N ANISOU 1309 NH2 ARG A 233 13044 14970 5872 1350 -618 1377 N ATOM 1310 N ALA A 234 61.349-121.815 196.349 1.00 91.54 N ANISOU 1310 N ALA A 234 12845 15932 6004 2812 -1084 2312 N ATOM 1311 CA ALA A 234 61.043-123.056 197.052 1.00 94.62 C ANISOU 1311 CA ALA A 234 13488 16133 6330 2980 -1042 2464 C ATOM 1312 C ALA A 234 62.204-123.505 197.928 1.00105.35 C ANISOU 1312 C ALA A 234 14727 17751 7551 3133 -1155 2583 C ATOM 1313 O ALA A 234 61.985-124.085 198.998 1.00114.88 O ANISOU 1313 O ALA A 234 16101 18913 8637 3152 -1156 2678 O ATOM 1314 CB ALA A 234 60.677-124.151 196.051 1.00 90.99 C ANISOU 1314 CB ALA A 234 13221 15339 6013 3213 -950 2543 C ATOM 1315 N VAL A 235 63.441-123.252 197.494 1.00103.96 N ANISOU 1315 N VAL A 235 14257 17857 7385 3239 -1246 2586 N ATOM 1316 CA VAL A 235 64.594-123.604 198.315 1.00105.99 C ANISOU 1316 CA VAL A 235 14368 18400 7505 3380 -1353 2695 C ATOM 1317 C VAL A 235 64.678-122.698 199.537 1.00106.29 C ANISOU 1317 C VAL A 235 14326 18676 7382 3106 -1441 2634 C ATOM 1318 O VAL A 235 65.123-123.127 200.608 1.00111.34 O ANISOU 1318 O VAL A 235 14984 19447 7874 3173 -1503 2734 O ATOM 1319 CB VAL A 235 65.882-123.548 197.471 1.00101.24 C ANISOU 1319 CB VAL A 235 13451 18062 6955 3557 -1412 2713 C ATOM 1320 CG1 VAL A 235 67.102-123.874 198.322 1.00103.32 C ANISOU 1320 CG1 VAL A 235 13537 18654 7067 3702 -1517 2826 C ATOM 1321 CG2 VAL A 235 65.784-124.505 196.294 1.00 98.70 C ANISOU 1321 CG2 VAL A 235 13239 17487 6777 3852 -1318 2763 C ATOM 1322 N SER A 236 64.235-121.444 199.409 1.00102.76 N ANISOU 1322 N SER A 236 13809 18277 6956 2797 -1448 2466 N ATOM 1323 CA SER A 236 64.334-120.508 200.524 1.00105.25 C ANISOU 1323 CA SER A 236 14064 18807 7117 2529 -1537 2382 C ATOM 1324 C SER A 236 63.420-120.908 201.676 1.00106.74 C ANISOU 1324 C SER A 236 14536 18833 7186 2476 -1482 2416 C ATOM 1325 O SER A 236 63.831-120.863 202.842 1.00109.90 O ANISOU 1325 O SER A 236 14921 19418 7418 2430 -1563 2454 O ATOM 1326 CB SER A 236 64.011-119.091 200.051 1.00106.66 C ANISOU 1326 CB SER A 236 14143 19028 7353 2218 -1552 2181 C ATOM 1327 OG SER A 236 62.683-119.007 199.564 1.00111.32 O ANISOU 1327 OG SER A 236 14951 19303 8041 2143 -1417 2096 O ATOM 1328 N ILE A 237 62.179-121.303 201.376 1.00104.36 N ANISOU 1328 N ILE A 237 14490 18198 6963 2473 -1341 2408 N ATOM 1329 CA ILE A 237 61.260-121.679 202.446 1.00109.56 C ANISOU 1329 CA ILE A 237 15407 18715 7506 2403 -1275 2447 C ATOM 1330 C ILE A 237 61.690-122.989 203.092 1.00110.89 C ANISOU 1330 C ILE A 237 15682 18860 7591 2648 -1298 2657 C ATOM 1331 O ILE A 237 61.445-123.209 204.285 1.00110.76 O ANISOU 1331 O ILE A 237 15791 18874 7418 2590 -1307 2712 O ATOM 1332 CB ILE A 237 59.811-121.752 201.925 1.00107.25 C ANISOU 1332 CB ILE A 237 15341 18090 7320 2318 -1111 2391 C ATOM 1333 CG1 ILE A 237 59.680-122.780 200.801 1.00111.21 C ANISOU 1333 CG1 ILE A 237 15937 18329 7988 2552 -1039 2496 C ATOM 1334 CG2 ILE A 237 59.343-120.388 201.457 1.00102.29 C ANISOU 1334 CG2 ILE A 237 14621 17497 6746 2068 -1090 2173 C ATOM 1335 CD1 ILE A 237 58.984-124.054 201.223 1.00115.88 C ANISOU 1335 CD1 ILE A 237 16826 18648 8556 2664 -954 2658 C ATOM 1336 N PHE A 238 62.332-123.878 202.330 1.00109.69 N ANISOU 1336 N PHE A 238 15492 18652 7533 2931 -1307 2774 N ATOM 1337 CA PHE A 238 62.883-125.090 202.928 1.00108.01 C ANISOU 1337 CA PHE A 238 15369 18436 7235 3186 -1344 2967 C ATOM 1338 C PHE A 238 64.052-124.771 203.849 1.00110.05 C ANISOU 1338 C PHE A 238 15406 19078 7329 3194 -1488 2998 C ATOM 1339 O PHE A 238 64.345-125.544 204.768 1.00112.09 O ANISOU 1339 O PHE A 238 15758 19373 7457 3322 -1527 3139 O ATOM 1340 CB PHE A 238 63.311-126.072 201.837 1.00111.29 C ANISOU 1340 CB PHE A 238 15803 18694 7788 3504 -1315 3060 C ATOM 1341 CG PHE A 238 62.161-126.759 201.155 1.00112.80 C ANISOU 1341 CG PHE A 238 16291 18458 8111 3533 -1181 3081 C ATOM 1342 CD1 PHE A 238 60.951-126.925 201.808 1.00113.43 C ANISOU 1342 CD1 PHE A 238 16634 18320 8143 3352 -1099 3098 C ATOM 1343 CD2 PHE A 238 62.292-127.241 199.864 1.00112.39 C ANISOU 1343 CD2 PHE A 238 16251 18228 8223 3732 -1135 3083 C ATOM 1344 CE1 PHE A 238 59.891-127.557 201.184 1.00111.37 C ANISOU 1344 CE1 PHE A 238 16638 17675 8001 3350 -979 3125 C ATOM 1345 CE2 PHE A 238 61.235-127.874 199.235 1.00111.12 C ANISOU 1345 CE2 PHE A 238 16376 17664 8181 3740 -1020 3099 C ATOM 1346 CZ PHE A 238 60.034-128.032 199.896 1.00109.90 C ANISOU 1346 CZ PHE A 238 16477 17297 7982 3539 -944 3124 C ATOM 1347 N VAL A 239 64.726-123.644 203.622 1.00109.35 N ANISOU 1347 N VAL A 239 15030 19275 7241 3048 -1573 2873 N ATOM 1348 CA VAL A 239 65.775-123.204 204.535 1.00112.01 C ANISOU 1348 CA VAL A 239 15157 19987 7417 2997 -1714 2887 C ATOM 1349 C VAL A 239 65.171-122.529 205.761 1.00110.43 C ANISOU 1349 C VAL A 239 15071 19829 7059 2719 -1735 2806 C ATOM 1350 O VAL A 239 65.680-122.677 206.878 1.00113.05 O ANISOU 1350 O VAL A 239 15385 20350 7217 2727 -1821 2878 O ATOM 1351 CB VAL A 239 66.761-122.280 203.796 1.00108.59 C ANISOU 1351 CB VAL A 239 14374 19842 7043 2926 -1801 2794 C ATOM 1352 CG1 VAL A 239 67.706-121.600 204.775 1.00106.60 C ANISOU 1352 CG1 VAL A 239 13912 19971 6619 2783 -1951 2779 C ATOM 1353 CG2 VAL A 239 67.549-123.068 202.762 1.00104.64 C ANISOU 1353 CG2 VAL A 239 13736 19365 6656 3249 -1785 2898 C ATOM 1354 N MET A 240 64.069-121.797 205.580 1.00111.61 N ANISOU 1354 N MET A 240 15345 19804 7259 2482 -1651 2653 N ATOM 1355 CA MET A 240 63.461-121.083 206.698 1.00116.41 C ANISOU 1355 CA MET A 240 16065 20453 7714 2225 -1657 2551 C ATOM 1356 C MET A 240 62.864-122.048 207.716 1.00117.60 C ANISOU 1356 C MET A 240 16472 20468 7742 2304 -1598 2689 C ATOM 1357 O MET A 240 63.105-121.918 208.922 1.00121.97 O ANISOU 1357 O MET A 240 17044 21191 8108 2233 -1668 2708 O ATOM 1358 CB MET A 240 62.396-120.111 206.190 1.00115.53 C ANISOU 1358 CB MET A 240 16028 20180 7690 1985 -1564 2351 C ATOM 1359 CG MET A 240 62.945-118.966 205.356 1.00116.09 C ANISOU 1359 CG MET A 240 15862 20396 7853 1841 -1639 2195 C ATOM 1360 SD MET A 240 61.771-117.607 205.204 1.00116.24 S ANISOU 1360 SD MET A 240 15987 20280 7900 1518 -1565 1934 S ATOM 1361 CE MET A 240 60.326-118.473 204.599 1.00115.96 C ANISOU 1361 CE MET A 240 16205 19859 7994 1631 -1351 1987 C ATOM 1362 N ASP A 241 62.076-123.021 207.256 1.00117.65 N ANISOU 1362 N ASP A 241 16687 20167 7847 2439 -1472 2790 N ATOM 1363 CA ASP A 241 61.485-123.974 208.188 1.00121.65 C ANISOU 1363 CA ASP A 241 17448 20534 8240 2491 -1417 2937 C ATOM 1364 C ASP A 241 62.500-124.975 208.722 1.00125.02 C ANISOU 1364 C ASP A 241 17850 21078 8573 2742 -1516 3135 C ATOM 1365 O ASP A 241 62.208-125.660 209.708 1.00129.50 O ANISOU 1365 O ASP A 241 18602 21597 9006 2765 -1505 3261 O ATOM 1366 CB ASP A 241 60.314-124.713 207.532 1.00123.74 C ANISOU 1366 CB ASP A 241 17955 20423 8637 2525 -1259 2991 C ATOM 1367 CG ASP A 241 60.764-125.851 206.638 1.00129.32 C ANISOU 1367 CG ASP A 241 18699 20960 9478 2820 -1256 3140 C ATOM 1368 OD1 ASP A 241 61.753-125.679 205.898 1.00132.15 O ANISOU 1368 OD1 ASP A 241 18838 21458 9917 2961 -1331 3116 O ATOM 1369 OD2 ASP A 241 60.123-126.923 206.677 1.00131.15 O ANISOU 1369 OD2 ASP A 241 19184 20916 9729 2906 -1178 3279 O ATOM 1370 N ALA A 242 63.678-125.077 208.101 1.00123.56 N ANISOU 1370 N ALA A 242 17438 21058 8450 2932 -1606 3169 N ATOM 1371 CA ALA A 242 64.725-125.938 208.640 1.00124.77 C ANISOU 1371 CA ALA A 242 17537 21368 8501 3183 -1703 3346 C ATOM 1372 C ALA A 242 65.357-125.316 209.879 1.00134.48 C ANISOU 1372 C ALA A 242 18636 22937 9522 3051 -1828 3323 C ATOM 1373 O ALA A 242 65.533-125.988 210.902 1.00140.96 O ANISOU 1373 O ALA A 242 19565 23806 10188 3138 -1868 3462 O ATOM 1374 CB ALA A 242 65.785-126.211 207.573 1.00122.31 C ANISOU 1374 CB ALA A 242 17004 21156 8313 3437 -1747 3381 C ATOM 1375 N VAL A 243 65.704-124.028 209.806 1.00133.47 N ANISOU 1375 N VAL A 243 18288 23039 9384 2832 -1896 3150 N ATOM 1376 CA VAL A 243 66.239-123.343 210.976 1.00141.80 C ANISOU 1376 CA VAL A 243 19241 24397 10238 2670 -2017 3106 C ATOM 1377 C VAL A 243 65.158-123.116 212.023 1.00146.77 C ANISOU 1377 C VAL A 243 20122 24910 10734 2465 -1958 3052 C ATOM 1378 O VAL A 243 65.474-122.858 213.191 1.00151.01 O ANISOU 1378 O VAL A 243 20654 25648 11075 2377 -2044 3056 O ATOM 1379 CB VAL A 243 66.901-122.011 210.573 1.00144.37 C ANISOU 1379 CB VAL A 243 19284 24977 10593 2468 -2114 2932 C ATOM 1380 CG1 VAL A 243 67.844-122.220 209.397 1.00144.55 C ANISOU 1380 CG1 VAL A 243 19054 25105 10765 2659 -2144 2980 C ATOM 1381 CG2 VAL A 243 65.850-120.961 210.247 1.00142.77 C ANISOU 1381 CG2 VAL A 243 19179 24608 10458 2184 -2037 2718 C ATOM 1382 N LEU A 244 63.884-123.209 211.635 1.00150.64 N ANISOU 1382 N LEU A 244 20828 25091 11319 2389 -1807 3004 N ATOM 1383 CA LEU A 244 62.793-123.109 212.597 1.00150.63 C ANISOU 1383 CA LEU A 244 21064 24978 11189 2217 -1724 2969 C ATOM 1384 C LEU A 244 62.601-124.407 213.371 1.00161.11 C ANISOU 1384 C LEU A 244 22599 26204 12412 2376 -1697 3193 C ATOM 1385 O LEU A 244 62.251-124.371 214.556 1.00162.09 O ANISOU 1385 O LEU A 244 22848 26390 12350 2268 -1697 3208 O ATOM 1386 CB LEU A 244 61.500-122.718 211.875 1.00138.63 C ANISOU 1386 CB LEU A 244 19674 23192 9807 2073 -1565 2839 C ATOM 1387 CG LEU A 244 60.188-122.683 212.663 1.00132.00 C ANISOU 1387 CG LEU A 244 19079 22210 8866 1908 -1436 2805 C ATOM 1388 CD1 LEU A 244 59.370-121.466 212.268 1.00128.34 C ANISOU 1388 CD1 LEU A 244 18607 21694 8464 1680 -1355 2562 C ATOM 1389 CD2 LEU A 244 59.383-123.954 212.434 1.00128.63 C ANISOU 1389 CD2 LEU A 244 18875 21491 8506 2027 -1310 2987 C ATOM 1390 N TYR A 245 62.831-125.554 212.726 1.00177.85 N ANISOU 1390 N TYR A 245 24770 28163 14643 2632 -1675 3364 N ATOM 1391 CA TYR A 245 62.661-126.841 213.391 1.00187.05 C ANISOU 1391 CA TYR A 245 26155 29197 15717 2786 -1657 3586 C ATOM 1392 C TYR A 245 63.708-127.088 214.469 1.00187.51 C ANISOU 1392 C TYR A 245 26128 29539 15578 2890 -1801 3696 C ATOM 1393 O TYR A 245 63.476-127.913 215.359 1.00192.13 O ANISOU 1393 O TYR A 245 26908 30063 16030 2942 -1797 3855 O ATOM 1394 CB TYR A 245 62.706-127.973 212.363 1.00197.82 C ANISOU 1394 CB TYR A 245 27610 30299 17254 3045 -1609 3725 C ATOM 1395 CG TYR A 245 61.379-128.261 211.695 1.00204.01 C ANISOU 1395 CG TYR A 245 28618 30719 18176 2951 -1449 3710 C ATOM 1396 CD1 TYR A 245 60.184-128.119 212.389 1.00206.79 C ANISOU 1396 CD1 TYR A 245 29163 30966 18443 2716 -1349 3690 C ATOM 1397 CD2 TYR A 245 61.322-128.678 210.371 1.00206.16 C ANISOU 1397 CD2 TYR A 245 28903 30768 18661 3098 -1395 3716 C ATOM 1398 CE1 TYR A 245 58.970-128.385 211.783 1.00206.90 C ANISOU 1398 CE1 TYR A 245 29361 30674 18579 2618 -1200 3684 C ATOM 1399 CE2 TYR A 245 60.113-128.944 209.757 1.00205.97 C ANISOU 1399 CE2 TYR A 245 29082 30416 18760 3000 -1254 3705 C ATOM 1400 CZ TYR A 245 58.941-128.796 210.467 1.00206.57 C ANISOU 1400 CZ TYR A 245 29332 30406 18750 2755 -1158 3693 C ATOM 1401 OH TYR A 245 57.737-129.061 209.857 1.00205.77 O ANISOU 1401 OH TYR A 245 29413 30003 18769 2645 -1016 3690 O ATOM 1402 N SER A 246 64.845-126.402 214.413 1.00181.05 N ANISOU 1402 N SER A 246 25023 29033 14735 2910 -1930 3623 N ATOM 1403 CA SER A 246 65.905-126.596 215.396 1.00179.33 C ANISOU 1403 CA SER A 246 24693 29114 14330 3009 -2073 3726 C ATOM 1404 C SER A 246 65.477-126.103 216.775 1.00178.21 C ANISOU 1404 C SER A 246 24659 29085 13966 2783 -2094 3678 C ATOM 1405 O SER A 246 65.496-126.857 217.748 1.00178.96 O ANISOU 1405 O SER A 246 24898 29194 13903 2863 -2118 3835 O ATOM 1406 CB SER A 246 67.184-125.879 214.957 1.00178.02 C ANISOU 1406 CB SER A 246 24170 29276 14192 3042 -2200 3649 C ATOM 1407 OG SER A 246 66.980-124.480 214.875 1.00174.74 O ANISOU 1407 OG SER A 246 23640 28970 13785 2742 -2217 3421 O ATOM 1408 N TYR A 278 70.722-116.370 214.966 1.00144.47 N ANISOU 1408 N TYR A 278 18540 26635 9717 1156 -2969 2374 N ATOM 1409 CA TYR A 278 69.761-115.288 214.784 1.00143.51 C ANISOU 1409 CA TYR A 278 18597 26292 9638 887 -2921 2136 C ATOM 1410 C TYR A 278 69.969-114.594 213.443 1.00135.74 C ANISOU 1410 C TYR A 278 17440 25280 8857 775 -2923 2039 C ATOM 1411 O TYR A 278 69.019-114.394 212.686 1.00128.40 O ANISOU 1411 O TYR A 278 16644 24068 8074 744 -2800 1937 O ATOM 1412 CB TYR A 278 69.866-114.277 215.927 1.00152.98 C ANISOU 1412 CB TYR A 278 19879 27621 10626 614 -3044 1985 C ATOM 1413 CG TYR A 278 68.966-113.075 215.758 1.00157.61 C ANISOU 1413 CG TYR A 278 20653 27989 11243 346 -3008 1722 C ATOM 1414 CD1 TYR A 278 67.590-113.187 215.908 1.00158.25 C ANISOU 1414 CD1 TYR A 278 21029 27764 11335 371 -2844 1640 C ATOM 1415 CD2 TYR A 278 69.493-111.826 215.456 1.00161.72 C ANISOU 1415 CD2 TYR A 278 21059 28610 11777 66 -3136 1560 C ATOM 1416 CE1 TYR A 278 66.763-112.090 215.756 1.00158.87 C ANISOU 1416 CE1 TYR A 278 21280 27647 11436 154 -2803 1395 C ATOM 1417 CE2 TYR A 278 68.673-110.724 215.305 1.00162.40 C ANISOU 1417 CE2 TYR A 278 21340 28476 11889 -162 -3107 1315 C ATOM 1418 CZ TYR A 278 67.310-110.861 215.455 1.00160.57 C ANISOU 1418 CZ TYR A 278 21397 27946 11665 -103 -2938 1229 C ATOM 1419 OH TYR A 278 66.492-109.764 215.304 1.00158.86 O ANISOU 1419 OH TYR A 278 21375 27516 11469 -302 -2903 981 O ATOM 1420 N ALA A 279 71.218-114.225 213.154 1.00134.16 N ANISOU 1420 N ALA A 279 16931 25385 8658 706 -3061 2076 N ATOM 1421 CA ALA A 279 71.527-113.623 211.863 1.00130.10 C ANISOU 1421 CA ALA A 279 16223 24877 8331 601 -3067 2010 C ATOM 1422 C ALA A 279 71.295-114.596 210.713 1.00130.69 C ANISOU 1422 C ALA A 279 16249 24799 8607 894 -2925 2133 C ATOM 1423 O ALA A 279 71.052-114.159 209.584 1.00117.25 O ANISOU 1423 O ALA A 279 14496 22973 7082 822 -2874 2050 O ATOM 1424 CB ALA A 279 72.970-113.119 211.845 1.00130.41 C ANISOU 1424 CB ALA A 279 15923 25312 8314 469 -3236 2054 C ATOM 1425 N GLY A 280 71.388-115.904 210.973 1.00131.26 N ANISOU 1425 N GLY A 280 16347 24874 8653 1224 -2866 2328 N ATOM 1426 CA GLY A 280 71.107-116.884 209.939 1.00131.64 C ANISOU 1426 CA GLY A 280 16399 24738 8880 1516 -2731 2439 C ATOM 1427 C GLY A 280 69.656-116.894 209.518 1.00134.15 C ANISOU 1427 C GLY A 280 17008 24650 9313 1490 -2576 2337 C ATOM 1428 O GLY A 280 69.334-117.325 208.409 1.00128.67 O ANISOU 1428 O GLY A 280 16311 23777 8800 1637 -2470 2366 O ATOM 1429 N CYS A 281 68.765-116.419 210.390 1.00141.78 N ANISOU 1429 N CYS A 281 18225 25476 10168 1307 -2555 2216 N ATOM 1430 CA CYS A 281 67.365-116.285 210.025 1.00145.07 C ANISOU 1430 CA CYS A 281 18900 25540 10680 1249 -2403 2101 C ATOM 1431 C CYS A 281 67.128-115.059 209.158 1.00139.75 C ANISOU 1431 C CYS A 281 18172 24800 10128 999 -2411 1897 C ATOM 1432 O CYS A 281 66.276-115.095 208.266 1.00138.23 O ANISOU 1432 O CYS A 281 18075 24352 10093 1023 -2283 1843 O ATOM 1433 CB CYS A 281 66.501-116.217 211.284 1.00154.03 C ANISOU 1433 CB CYS A 281 20311 26573 11641 1158 -2364 2045 C ATOM 1434 SG CYS A 281 64.720-116.275 210.954 1.00159.84 S ANISOU 1434 SG CYS A 281 21360 26900 12472 1130 -2148 1943 S ATOM 1435 N ARG A 282 67.871-113.977 209.404 1.00138.71 N ANISOU 1435 N ARG A 282 17894 24888 9923 751 -2562 1788 N ATOM 1436 CA ARG A 282 67.675-112.748 208.644 1.00136.40 C ANISOU 1436 CA ARG A 282 17572 24521 9734 486 -2585 1590 C ATOM 1437 C ARG A 282 68.043-112.939 207.179 1.00130.05 C ANISOU 1437 C ARG A 282 16557 23713 9143 582 -2550 1649 C ATOM 1438 O ARG A 282 67.329-112.469 206.286 1.00127.68 O ANISOU 1438 O ARG A 282 16328 23197 8989 496 -2471 1531 O ATOM 1439 CB ARG A 282 68.500-111.623 209.262 1.00140.39 C ANISOU 1439 CB ARG A 282 17973 25265 10106 197 -2771 1483 C ATOM 1440 CG ARG A 282 68.623-111.711 210.772 1.00147.14 C ANISOU 1440 CG ARG A 282 18943 26242 10722 174 -2842 1498 C ATOM 1441 CD ARG A 282 67.705-110.729 211.474 1.00150.07 C ANISOU 1441 CD ARG A 282 19599 26432 10988 -57 -2835 1268 C ATOM 1442 NE ARG A 282 68.077-109.346 211.193 1.00151.20 N ANISOU 1442 NE ARG A 282 19689 26615 11144 -374 -2960 1083 N ATOM 1443 CZ ARG A 282 69.074-108.703 211.793 1.00152.96 C ANISOU 1443 CZ ARG A 282 19792 27092 11234 -568 -3143 1060 C ATOM 1444 NH1 ARG A 282 69.338-107.444 211.475 1.00154.51 N ANISOU 1444 NH1 ARG A 282 19971 27281 11456 -871 -3251 892 N ATOM 1445 NH2 ARG A 282 69.811-109.319 212.707 1.00151.97 N ANISOU 1445 NH2 ARG A 282 19570 27223 10949 -466 -3221 1209 N ATOM 1446 N VAL A 283 69.156-113.626 206.912 1.00124.50 N ANISOU 1446 N VAL A 283 15594 23256 8456 770 -2603 1830 N ATOM 1447 CA VAL A 283 69.556-113.879 205.534 1.00118.29 C ANISOU 1447 CA VAL A 283 14600 22485 7859 893 -2561 1895 C ATOM 1448 C VAL A 283 68.617-114.864 204.853 1.00111.39 C ANISOU 1448 C VAL A 283 13897 21304 7123 1159 -2385 1957 C ATOM 1449 O VAL A 283 68.515-114.866 203.621 1.00107.25 O ANISOU 1449 O VAL A 283 13293 20683 6774 1212 -2321 1946 O ATOM 1450 CB VAL A 283 71.011-114.380 205.479 1.00119.34 C ANISOU 1450 CB VAL A 283 14405 22984 7953 1050 -2652 2071 C ATOM 1451 CG1 VAL A 283 71.958-113.309 205.997 1.00117.67 C ANISOU 1451 CG1 VAL A 283 14002 23086 7622 744 -2827 2007 C ATOM 1452 CG2 VAL A 283 71.163-115.662 206.283 1.00122.16 C ANISOU 1452 CG2 VAL A 283 14831 23382 8203 1365 -2624 2252 C ATOM 1453 N ALA A 284 67.918-115.700 205.623 1.00111.10 N ANISOU 1453 N ALA A 284 14101 21105 7008 1317 -2305 2026 N ATOM 1454 CA ALA A 284 66.975-116.639 205.026 1.00107.83 C ANISOU 1454 CA ALA A 284 13875 20378 6717 1541 -2140 2089 C ATOM 1455 C ALA A 284 65.721-115.922 204.541 1.00105.28 C ANISOU 1455 C ALA A 284 13739 19774 6490 1351 -2038 1908 C ATOM 1456 O ALA A 284 65.242-116.173 203.429 1.00104.17 O ANISOU 1456 O ALA A 284 13619 19441 6520 1443 -1936 1905 O ATOM 1457 CB ALA A 284 66.618-117.737 206.028 1.00104.08 C ANISOU 1457 CB ALA A 284 13606 19816 6122 1736 -2089 2228 C ATOM 1458 N VAL A 285 65.172-115.024 205.363 1.00106.10 N ANISOU 1458 N VAL A 285 13984 19851 6479 1097 -2062 1750 N ATOM 1459 CA VAL A 285 63.982-114.286 204.958 1.00109.65 C ANISOU 1459 CA VAL A 285 14610 20050 7004 925 -1962 1564 C ATOM 1460 C VAL A 285 64.311-113.214 203.929 1.00111.57 C ANISOU 1460 C VAL A 285 14689 20331 7371 731 -2023 1428 C ATOM 1461 O VAL A 285 63.430-112.806 203.163 1.00115.30 O ANISOU 1461 O VAL A 285 15258 20585 7964 659 -1927 1310 O ATOM 1462 CB VAL A 285 63.278-113.669 206.181 1.00117.25 C ANISOU 1462 CB VAL A 285 15788 20967 7793 740 -1958 1428 C ATOM 1463 CG1 VAL A 285 62.917-114.752 207.184 1.00121.68 C ANISOU 1463 CG1 VAL A 285 16512 21491 8231 918 -1891 1575 C ATOM 1464 CG2 VAL A 285 64.152-112.605 206.827 1.00122.91 C ANISOU 1464 CG2 VAL A 285 16395 21924 8380 504 -2140 1322 C ATOM 1465 N THR A 286 65.559-112.742 203.887 1.00109.05 N ANISOU 1465 N THR A 286 14119 20291 7023 635 -2180 1447 N ATOM 1466 CA THR A 286 65.949-111.788 202.854 1.00105.09 C ANISOU 1466 CA THR A 286 13448 19835 6646 445 -2241 1345 C ATOM 1467 C THR A 286 65.994-112.453 201.484 1.00 98.05 C ANISOU 1467 C THR A 286 12434 18873 5949 654 -2151 1445 C ATOM 1468 O THR A 286 65.492-111.897 200.500 1.00 92.32 O ANISOU 1468 O THR A 286 11722 17992 5362 550 -2101 1338 O ATOM 1469 CB THR A 286 67.303-111.165 203.196 1.00107.27 C ANISOU 1469 CB THR A 286 13477 20447 6833 276 -2427 1362 C ATOM 1470 OG1 THR A 286 67.166-110.323 204.348 1.00110.45 O ANISOU 1470 OG1 THR A 286 14026 20873 7067 34 -2517 1225 O ATOM 1471 CG2 THR A 286 67.828-110.340 202.029 1.00102.89 C ANISOU 1471 CG2 THR A 286 12715 19960 6419 97 -2484 1302 C ATOM 1472 N PHE A 287 66.585-113.648 201.404 1.00 97.91 N ANISOU 1472 N PHE A 287 12307 18955 5938 960 -2129 1647 N ATOM 1473 CA PHE A 287 66.599-114.382 200.144 1.00 96.64 C ANISOU 1473 CA PHE A 287 12065 18704 5952 1198 -2035 1740 C ATOM 1474 C PHE A 287 65.192-114.746 199.692 1.00 95.62 C ANISOU 1474 C PHE A 287 12203 18204 5923 1274 -1869 1691 C ATOM 1475 O PHE A 287 64.912-114.753 198.488 1.00 96.51 O ANISOU 1475 O PHE A 287 12283 18188 6198 1323 -1799 1670 O ATOM 1476 CB PHE A 287 67.460-115.639 200.277 1.00103.48 C ANISOU 1476 CB PHE A 287 12810 19722 6784 1538 -2039 1955 C ATOM 1477 CG PHE A 287 68.914-115.413 199.974 1.00113.10 C ANISOU 1477 CG PHE A 287 13674 21308 7992 1538 -2154 2025 C ATOM 1478 CD1 PHE A 287 69.680-114.571 200.763 1.00117.54 C ANISOU 1478 CD1 PHE A 287 14091 22151 8418 1290 -2302 1983 C ATOM 1479 CD2 PHE A 287 69.518-116.050 198.901 1.00116.30 C ANISOU 1479 CD2 PHE A 287 13892 21783 8512 1787 -2108 2132 C ATOM 1480 CE1 PHE A 287 71.018-114.363 200.486 1.00121.79 C ANISOU 1480 CE1 PHE A 287 14289 23048 8939 1273 -2399 2058 C ATOM 1481 CE2 PHE A 287 70.856-115.846 198.619 1.00119.19 C ANISOU 1481 CE2 PHE A 287 13913 22516 8857 1790 -2196 2202 C ATOM 1482 CZ PHE A 287 71.607-115.002 199.412 1.00122.45 C ANISOU 1482 CZ PHE A 287 14168 23221 9135 1525 -2340 2171 C ATOM 1483 N PHE A 288 64.292-115.041 200.633 1.00 93.92 N ANISOU 1483 N PHE A 288 12250 17826 5611 1278 -1802 1676 N ATOM 1484 CA PHE A 288 62.920-115.366 200.256 1.00 91.88 C ANISOU 1484 CA PHE A 288 12238 17233 5438 1327 -1636 1634 C ATOM 1485 C PHE A 288 62.214-114.156 199.656 1.00 86.49 C ANISOU 1485 C PHE A 288 11591 16436 4835 1068 -1610 1423 C ATOM 1486 O PHE A 288 61.536-114.268 198.628 1.00 84.57 O ANISOU 1486 O PHE A 288 11400 15991 4740 1119 -1502 1394 O ATOM 1487 CB PHE A 288 62.137-115.891 201.459 1.00 88.97 C ANISOU 1487 CB PHE A 288 12122 16749 4935 1360 -1568 1669 C ATOM 1488 CG PHE A 288 60.662-116.013 201.202 1.00 88.93 C ANISOU 1488 CG PHE A 288 12360 16432 4996 1343 -1396 1604 C ATOM 1489 CD1 PHE A 288 60.160-117.084 200.484 1.00 89.39 C ANISOU 1489 CD1 PHE A 288 12522 16265 5176 1564 -1273 1725 C ATOM 1490 CD2 PHE A 288 59.780-115.047 201.658 1.00 88.38 C ANISOU 1490 CD2 PHE A 288 12419 16293 4867 1108 -1354 1416 C ATOM 1491 CE1 PHE A 288 58.806-117.194 200.233 1.00 84.24 C ANISOU 1491 CE1 PHE A 288 12082 15339 4587 1532 -1113 1673 C ATOM 1492 CE2 PHE A 288 58.426-115.153 201.409 1.00 84.80 C ANISOU 1492 CE2 PHE A 288 12164 15582 4475 1098 -1185 1358 C ATOM 1493 CZ PHE A 288 57.939-116.230 200.697 1.00 82.51 C ANISOU 1493 CZ PHE A 288 11958 15085 4308 1301 -1064 1493 C ATOM 1494 N LEU A 289 62.349-112.992 200.294 1.00 86.72 N ANISOU 1494 N LEU A 289 11611 16576 4761 789 -1709 1269 N ATOM 1495 CA LEU A 289 61.690-111.796 199.781 1.00 88.78 C ANISOU 1495 CA LEU A 289 11933 16712 5089 540 -1692 1055 C ATOM 1496 C LEU A 289 62.276-111.362 198.444 1.00 92.77 C ANISOU 1496 C LEU A 289 12223 17271 5753 486 -1742 1041 C ATOM 1497 O LEU A 289 61.559-110.795 197.611 1.00 94.90 O ANISOU 1497 O LEU A 289 12553 17366 6138 384 -1677 916 O ATOM 1498 CB LEU A 289 61.785-110.663 200.802 1.00 90.64 C ANISOU 1498 CB LEU A 289 12235 17033 5172 264 -1801 891 C ATOM 1499 CG LEU A 289 61.041-110.902 202.118 1.00 95.26 C ANISOU 1499 CG LEU A 289 13054 17549 5592 286 -1738 865 C ATOM 1500 CD1 LEU A 289 61.203-109.714 203.051 1.00 95.98 C ANISOU 1500 CD1 LEU A 289 13218 17717 5533 23 -1855 687 C ATOM 1501 CD2 LEU A 289 59.569-111.195 201.864 1.00 94.05 C ANISOU 1501 CD2 LEU A 289 13116 17117 5503 360 -1537 811 C ATOM 1502 N TYR A 290 63.566-111.619 198.219 1.00 92.97 N ANISOU 1502 N TYR A 290 11993 17547 5785 555 -1851 1171 N ATOM 1503 CA TYR A 290 64.155-111.331 196.916 1.00 89.91 C ANISOU 1503 CA TYR A 290 11382 17231 5547 532 -1882 1184 C ATOM 1504 C TYR A 290 63.570-112.239 195.842 1.00 88.67 C ANISOU 1504 C TYR A 290 11270 16877 5545 793 -1734 1262 C ATOM 1505 O TYR A 290 63.152-111.768 194.778 1.00 87.50 O ANISOU 1505 O TYR A 290 11111 16606 5531 714 -1689 1177 O ATOM 1506 CB TYR A 290 65.676-111.478 196.979 1.00 92.60 C ANISOU 1506 CB TYR A 290 11423 17915 5846 570 -2013 1316 C ATOM 1507 CG TYR A 290 66.344-111.418 195.623 1.00 91.89 C ANISOU 1507 CG TYR A 290 11080 17928 5905 608 -2020 1368 C ATOM 1508 CD1 TYR A 290 66.490-110.212 194.952 1.00 90.61 C ANISOU 1508 CD1 TYR A 290 10822 17789 5815 305 -2088 1244 C ATOM 1509 CD2 TYR A 290 66.829-112.569 195.015 1.00 91.60 C ANISOU 1509 CD2 TYR A 290 10914 17955 5933 949 -1957 1540 C ATOM 1510 CE1 TYR A 290 67.098-110.153 193.712 1.00 92.06 C ANISOU 1510 CE1 TYR A 290 10770 18080 6130 331 -2088 1300 C ATOM 1511 CE2 TYR A 290 67.439-112.520 193.775 1.00 90.58 C ANISOU 1511 CE2 TYR A 290 10553 17933 5931 998 -1952 1584 C ATOM 1512 CZ TYR A 290 67.571-111.309 193.129 1.00 91.65 C ANISOU 1512 CZ TYR A 290 10577 18112 6133 682 -2016 1468 C ATOM 1513 OH TYR A 290 68.178-111.251 191.895 1.00 91.82 O ANISOU 1513 OH TYR A 290 10361 18252 6274 721 -2005 1518 O ATOM 1514 N PHE A 291 63.530-113.547 196.107 1.00 82.70 N ANISOU 1514 N PHE A 291 10583 16072 4769 1103 -1659 1423 N ATOM 1515 CA PHE A 291 62.965-114.480 195.137 1.00 80.80 C ANISOU 1515 CA PHE A 291 10427 15607 4667 1358 -1521 1500 C ATOM 1516 C PHE A 291 61.478-114.233 194.924 1.00 90.70 C ANISOU 1516 C PHE A 291 11933 16551 5976 1271 -1387 1376 C ATOM 1517 O PHE A 291 60.978-114.394 193.805 1.00 85.31 O ANISOU 1517 O PHE A 291 11278 15628 5508 1326 -1282 1345 O ATOM 1518 CB PHE A 291 63.214-115.919 195.588 1.00 82.35 C ANISOU 1518 CB PHE A 291 10693 15779 4818 1688 -1479 1692 C ATOM 1519 CG PHE A 291 64.667-116.290 195.644 1.00 87.11 C ANISOU 1519 CG PHE A 291 11034 16686 5378 1833 -1585 1822 C ATOM 1520 CD1 PHE A 291 65.565-115.757 194.734 1.00 87.74 C ANISOU 1520 CD1 PHE A 291 10829 16973 5534 1782 -1651 1809 C ATOM 1521 CD2 PHE A 291 65.139-117.163 196.612 1.00 89.61 C ANISOU 1521 CD2 PHE A 291 11382 17094 5572 2018 -1614 1960 C ATOM 1522 CE1 PHE A 291 66.904-116.090 194.782 1.00 89.40 C ANISOU 1522 CE1 PHE A 291 10777 17493 5697 1919 -1733 1930 C ATOM 1523 CE2 PHE A 291 66.478-117.499 196.667 1.00 94.92 C ANISOU 1523 CE2 PHE A 291 11802 18066 6197 2166 -1702 2077 C ATOM 1524 CZ PHE A 291 67.361-116.962 195.750 1.00 97.89 C ANISOU 1524 CZ PHE A 291 11882 18664 6648 2119 -1757 2061 C ATOM 1525 N LEU A 292 60.759-113.840 195.978 1.00 78.46 N ANISOU 1525 N LEU A 292 10563 14938 4309 1120 -1368 1283 N ATOM 1526 CA LEU A 292 59.355-113.473 195.818 1.00 76.25 C ANISOU 1526 CA LEU A 292 10496 14284 4192 991 -1213 1121 C ATOM 1527 C LEU A 292 59.204-112.281 194.881 1.00 77.34 C ANISOU 1527 C LEU A 292 10555 14318 4514 761 -1221 935 C ATOM 1528 O LEU A 292 58.272-112.231 194.071 1.00 72.26 O ANISOU 1528 O LEU A 292 10004 13358 4094 747 -1086 852 O ATOM 1529 CB LEU A 292 58.734-113.164 197.179 1.00 79.53 C ANISOU 1529 CB LEU A 292 11091 14702 4426 871 -1199 1046 C ATOM 1530 CG LEU A 292 57.291-112.654 197.169 1.00 80.32 C ANISOU 1530 CG LEU A 292 11390 14473 4653 734 -1043 868 C ATOM 1531 CD1 LEU A 292 56.327-113.766 196.787 1.00 80.56 C ANISOU 1531 CD1 LEU A 292 11568 14217 4825 910 -864 965 C ATOM 1532 CD2 LEU A 292 56.920-112.049 198.514 1.00 85.76 C ANISOU 1532 CD2 LEU A 292 12212 15250 5125 589 -1065 762 C ATOM 1533 N ALA A 293 60.117-111.312 194.975 1.00 75.74 N ANISOU 1533 N ALA A 293 10185 14380 4213 567 -1387 876 N ATOM 1534 CA ALA A 293 60.040-110.138 194.113 1.00 74.77 C ANISOU 1534 CA ALA A 293 10002 14158 4248 329 -1414 711 C ATOM 1535 C ALA A 293 60.430-110.476 192.679 1.00 73.38 C ANISOU 1535 C ALA A 293 9656 13955 4271 442 -1386 788 C ATOM 1536 O ALA A 293 59.843-109.944 191.730 1.00 71.05 O ANISOU 1536 O ALA A 293 9390 13415 4189 343 -1312 672 O ATOM 1537 CB ALA A 293 60.927-109.022 194.665 1.00 76.45 C ANISOU 1537 CB ALA A 293 10108 14662 4279 59 -1614 637 C ATOM 1538 N THR A 294 61.419-111.357 192.499 1.00 74.35 N ANISOU 1538 N THR A 294 9599 14334 4316 666 -1442 983 N ATOM 1539 CA THR A 294 61.807-111.753 191.149 1.00 75.01 C ANISOU 1539 CA THR A 294 9525 14409 4567 811 -1407 1060 C ATOM 1540 C THR A 294 60.703-112.542 190.457 1.00 72.02 C ANISOU 1540 C THR A 294 9335 13628 4401 988 -1215 1054 C ATOM 1541 O THR A 294 60.597-112.503 189.226 1.00 76.58 O ANISOU 1541 O THR A 294 9850 14073 5172 1013 -1158 1030 O ATOM 1542 CB THR A 294 63.098-112.573 191.178 1.00 79.50 C ANISOU 1542 CB THR A 294 9869 15358 4977 1057 -1504 1273 C ATOM 1543 OG1 THR A 294 62.906-113.747 191.976 1.00 80.35 O ANISOU 1543 OG1 THR A 294 10126 15431 4971 1325 -1453 1403 O ATOM 1544 CG2 THR A 294 64.241-111.750 191.751 1.00 77.94 C ANISOU 1544 CG2 THR A 294 9452 15514 4648 838 -1682 1270 C ATOM 1545 N ASN A 295 59.877-113.258 191.223 1.00 70.95 N ANISOU 1545 N ASN A 295 9429 13306 4224 1096 -1118 1080 N ATOM 1546 CA ASN A 295 58.760-113.984 190.629 1.00 71.08 C ANISOU 1546 CA ASN A 295 9637 12941 4430 1218 -943 1076 C ATOM 1547 C ASN A 295 57.772-113.026 189.978 1.00 72.82 C ANISOU 1547 C ASN A 295 9922 12890 4856 992 -861 880 C ATOM 1548 O ASN A 295 57.377-113.213 188.821 1.00 73.01 O ANISOU 1548 O ASN A 295 9947 12707 5086 1042 -775 861 O ATOM 1549 CB ASN A 295 58.061-114.834 191.690 1.00 73.30 C ANISOU 1549 CB ASN A 295 10147 13105 4601 1324 -867 1148 C ATOM 1550 CG ASN A 295 58.944-115.939 192.226 1.00 80.74 C ANISOU 1550 CG ASN A 295 11062 14260 5356 1594 -934 1361 C ATOM 1551 OD1 ASN A 295 59.700-116.563 191.482 1.00 88.21 O ANISOU 1551 OD1 ASN A 295 11894 15292 6328 1811 -963 1477 O ATOM 1552 ND2 ASN A 295 58.859-116.182 193.526 1.00 80.94 N ANISOU 1552 ND2 ASN A 295 11195 14379 5178 1598 -959 1415 N ATOM 1553 N TYR A 296 57.367-111.983 190.707 1.00 73.32 N ANISOU 1553 N TYR A 296 10049 12953 4857 753 -888 730 N ATOM 1554 CA TYR A 296 56.385-111.048 190.171 1.00 71.39 C ANISOU 1554 CA TYR A 296 9886 12447 4790 564 -810 542 C ATOM 1555 C TYR A 296 56.979-110.156 189.089 1.00 70.91 C ANISOU 1555 C TYR A 296 9652 12440 4851 427 -889 474 C ATOM 1556 O TYR A 296 56.251-109.691 188.204 1.00 65.05 O ANISOU 1556 O TYR A 296 8952 11455 4309 350 -809 367 O ATOM 1557 CB TYR A 296 55.796-110.203 191.299 1.00 67.41 C ANISOU 1557 CB TYR A 296 9525 11927 4161 383 -817 397 C ATOM 1558 CG TYR A 296 54.808-110.956 192.159 1.00 65.86 C ANISOU 1558 CG TYR A 296 9524 11603 3899 485 -689 432 C ATOM 1559 CD1 TYR A 296 53.469-111.032 191.802 1.00 64.02 C ANISOU 1559 CD1 TYR A 296 9427 11075 3822 483 -524 360 C ATOM 1560 CD2 TYR A 296 55.213-111.594 193.324 1.00 71.25 C ANISOU 1560 CD2 TYR A 296 10243 12478 4352 577 -735 550 C ATOM 1561 CE1 TYR A 296 52.559-111.720 192.580 1.00 64.36 C ANISOU 1561 CE1 TYR A 296 9632 11028 3794 552 -406 407 C ATOM 1562 CE2 TYR A 296 54.309-112.286 194.110 1.00 71.68 C ANISOU 1562 CE2 TYR A 296 10475 12424 4335 654 -617 596 C ATOM 1563 CZ TYR A 296 52.983-112.344 193.732 1.00 69.43 C ANISOU 1563 CZ TYR A 296 10318 11856 4208 633 -452 527 C ATOM 1564 OH TYR A 296 52.076-113.030 194.506 1.00 70.75 O ANISOU 1564 OH TYR A 296 10646 11942 4295 686 -334 587 O ATOM 1565 N TYR A 297 58.289-109.906 189.135 1.00 72.24 N ANISOU 1565 N TYR A 297 9618 12935 4894 388 -1048 544 N ATOM 1566 CA TYR A 297 58.908-109.072 188.112 1.00 70.67 C ANISOU 1566 CA TYR A 297 9241 12817 4793 237 -1128 502 C ATOM 1567 C TYR A 297 59.212-109.854 186.842 1.00 72.79 C ANISOU 1567 C TYR A 297 9378 13071 5209 441 -1070 616 C ATOM 1568 O TYR A 297 59.202-109.275 185.750 1.00 75.10 O ANISOU 1568 O TYR A 297 9591 13286 5659 339 -1064 557 O ATOM 1569 CB TYR A 297 60.175-108.417 188.660 1.00 72.63 C ANISOU 1569 CB TYR A 297 9309 13449 4836 72 -1328 533 C ATOM 1570 CG TYR A 297 59.934-107.016 189.171 1.00 76.57 C ANISOU 1570 CG TYR A 297 9914 13895 5286 -257 -1413 348 C ATOM 1571 CD1 TYR A 297 59.163-106.792 190.304 1.00 76.08 C ANISOU 1571 CD1 TYR A 297 10079 13706 5122 -307 -1380 240 C ATOM 1572 CD2 TYR A 297 60.468-105.915 188.513 1.00 77.48 C ANISOU 1572 CD2 TYR A 297 9917 14078 5444 -514 -1526 282 C ATOM 1573 CE1 TYR A 297 58.933-105.512 190.771 1.00 76.37 C ANISOU 1573 CE1 TYR A 297 10244 13674 5098 -582 -1457 58 C ATOM 1574 CE2 TYR A 297 60.245-104.631 188.973 1.00 78.74 C ANISOU 1574 CE2 TYR A 297 10217 14152 5549 -812 -1613 109 C ATOM 1575 CZ TYR A 297 59.477-104.436 190.101 1.00 78.14 C ANISOU 1575 CZ TYR A 297 10382 13937 5370 -832 -1578 -10 C ATOM 1576 OH TYR A 297 59.252-103.159 190.562 1.00 81.15 O ANISOU 1576 OH TYR A 297 10932 14218 5684 -1104 -1665 -194 O ATOM 1577 N TRP A 298 59.477-111.157 186.953 1.00 74.40 N ANISOU 1577 N TRP A 298 9575 13338 5355 734 -1029 777 N ATOM 1578 CA TRP A 298 59.607-111.984 185.761 1.00 64.07 C ANISOU 1578 CA TRP A 298 8201 11959 4182 961 -955 868 C ATOM 1579 C TRP A 298 58.260-112.310 185.133 1.00 68.11 C ANISOU 1579 C TRP A 298 8921 12049 4909 996 -788 791 C ATOM 1580 O TRP A 298 58.208-112.615 183.937 1.00 71.03 O ANISOU 1580 O TRP A 298 9247 12310 5432 1093 -730 807 O ATOM 1581 CB TRP A 298 60.362-113.274 186.082 1.00 65.84 C ANISOU 1581 CB TRP A 298 8380 12376 4261 1285 -975 1064 C ATOM 1582 CG TRP A 298 61.848-113.111 186.033 1.00 67.97 C ANISOU 1582 CG TRP A 298 8354 13096 4375 1324 -1124 1173 C ATOM 1583 CD1 TRP A 298 62.701-113.030 187.094 1.00 70.40 C ANISOU 1583 CD1 TRP A 298 8552 13751 4446 1306 -1256 1252 C ATOM 1584 CD2 TRP A 298 62.658-112.993 184.857 1.00 71.35 C ANISOU 1584 CD2 TRP A 298 8540 13709 4862 1377 -1157 1223 C ATOM 1585 NE1 TRP A 298 63.993-112.876 186.652 1.00 72.04 N ANISOU 1585 NE1 TRP A 298 8451 14360 4561 1343 -1372 1353 N ATOM 1586 CE2 TRP A 298 63.993-112.850 185.283 1.00 71.91 C ANISOU 1586 CE2 TRP A 298 8345 14257 4720 1389 -1309 1338 C ATOM 1587 CE3 TRP A 298 62.383-112.997 183.486 1.00 68.32 C ANISOU 1587 CE3 TRP A 298 8129 13151 4678 1415 -1072 1185 C ATOM 1588 CZ2 TRP A 298 65.051-112.713 184.387 1.00 75.19 C ANISOU 1588 CZ2 TRP A 298 8458 14995 5114 1438 -1372 1423 C ATOM 1589 CZ3 TRP A 298 63.435-112.861 182.598 1.00 71.57 C ANISOU 1589 CZ3 TRP A 298 8257 13868 5068 1470 -1133 1263 C ATOM 1590 CH2 TRP A 298 64.752-112.720 183.052 1.00 75.65 C ANISOU 1590 CH2 TRP A 298 8501 14874 5370 1481 -1279 1383 C ATOM 1591 N ILE A 299 57.175-112.258 185.908 1.00 64.26 N ANISOU 1591 N ILE A 299 8649 11344 4423 919 -711 712 N ATOM 1592 CA ILE A 299 55.845-112.307 185.309 1.00 67.30 C ANISOU 1592 CA ILE A 299 9197 11364 5008 887 -563 620 C ATOM 1593 C ILE A 299 55.602-111.055 184.476 1.00 64.10 C ANISOU 1593 C ILE A 299 8724 10877 4757 666 -574 468 C ATOM 1594 O ILE A 299 55.014-111.118 183.389 1.00 64.54 O ANISOU 1594 O ILE A 299 8799 10719 5003 682 -488 430 O ATOM 1595 CB ILE A 299 54.770-112.489 186.396 1.00 71.03 C ANISOU 1595 CB ILE A 299 9886 11680 5420 849 -479 580 C ATOM 1596 CG1 ILE A 299 54.885-113.872 187.039 1.00 72.64 C ANISOU 1596 CG1 ILE A 299 10192 11907 5500 1078 -452 751 C ATOM 1597 CG2 ILE A 299 53.377-112.295 185.814 1.00 56.97 C ANISOU 1597 CG2 ILE A 299 8236 9575 3835 770 -339 470 C ATOM 1598 CD1 ILE A 299 54.652-115.012 186.076 1.00 74.39 C ANISOU 1598 CD1 ILE A 299 10482 11934 5851 1281 -368 850 C ATOM 1599 N ALA A 300 56.061-109.901 184.966 1.00 64.67 N ANISOU 1599 N ALA A 300 8726 11109 4737 451 -688 380 N ATOM 1600 CA ALA A 300 55.979-108.676 184.179 1.00 60.99 C ANISOU 1600 CA ALA A 300 8204 10572 4396 235 -723 251 C ATOM 1601 C ALA A 300 56.866-108.745 182.943 1.00 67.56 C ANISOU 1601 C ALA A 300 8825 11536 5309 276 -770 330 C ATOM 1602 O ALA A 300 56.542-108.137 181.916 1.00 69.87 O ANISOU 1602 O ALA A 300 9096 11684 5768 175 -743 255 O ATOM 1603 CB ALA A 300 56.356-107.470 185.039 1.00 60.24 C ANISOU 1603 CB ALA A 300 8114 10615 4158 -12 -854 148 C ATOM 1604 N VAL A 301 57.983-109.470 183.022 1.00 66.99 N ANISOU 1604 N VAL A 301 8591 11751 5110 436 -839 486 N ATOM 1605 CA VAL A 301 58.820-109.674 181.842 1.00 64.26 C ANISOU 1605 CA VAL A 301 8035 11560 4822 525 -866 575 C ATOM 1606 C VAL A 301 58.067-110.481 180.793 1.00 62.38 C ANISOU 1606 C VAL A 301 7886 11043 4771 713 -720 585 C ATOM 1607 O VAL A 301 58.123-110.177 179.595 1.00 66.36 O ANISOU 1607 O VAL A 301 8299 11505 5411 680 -702 563 O ATOM 1608 CB VAL A 301 60.145-110.352 182.235 1.00 68.81 C ANISOU 1608 CB VAL A 301 8419 12528 5199 701 -964 746 C ATOM 1609 CG1 VAL A 301 60.887-110.825 180.993 1.00 70.75 C ANISOU 1609 CG1 VAL A 301 8464 12920 5496 878 -955 850 C ATOM 1610 CG2 VAL A 301 61.010-109.398 183.044 1.00 66.15 C ANISOU 1610 CG2 VAL A 301 7945 12508 4683 460 -1132 737 C ATOM 1611 N GLU A 302 57.350-111.521 181.227 1.00 60.10 N ANISOU 1611 N GLU A 302 7788 10564 4484 898 -619 622 N ATOM 1612 CA GLU A 302 56.524-112.291 180.303 1.00 60.60 C ANISOU 1612 CA GLU A 302 7974 10334 4716 1043 -487 623 C ATOM 1613 C GLU A 302 55.483-111.407 179.630 1.00 61.79 C ANISOU 1613 C GLU A 302 8191 10225 5061 838 -422 471 C ATOM 1614 O GLU A 302 55.216-111.552 178.431 1.00 55.02 O ANISOU 1614 O GLU A 302 7318 9232 4357 882 -363 459 O ATOM 1615 CB GLU A 302 55.846-113.447 181.041 1.00 59.57 C ANISOU 1615 CB GLU A 302 8064 10033 4538 1210 -404 687 C ATOM 1616 CG GLU A 302 56.797-114.525 181.546 1.00 65.97 C ANISOU 1616 CG GLU A 302 8847 11047 5170 1475 -455 855 C ATOM 1617 CD GLU A 302 57.193-115.520 180.468 1.00 72.90 C ANISOU 1617 CD GLU A 302 9710 11891 6100 1746 -419 950 C ATOM 1618 OE1 GLU A 302 56.921-115.260 179.277 1.00 73.98 O ANISOU 1618 OE1 GLU A 302 9807 11902 6398 1707 -373 886 O ATOM 1619 OE2 GLU A 302 57.773-116.570 180.815 1.00 77.40 O ANISOU 1619 OE2 GLU A 302 10319 12552 6537 2011 -439 1087 O ATOM 1620 N GLY A 303 54.888-110.481 180.384 1.00 62.08 N ANISOU 1620 N GLY A 303 8310 10195 5084 626 -432 353 N ATOM 1621 CA GLY A 303 53.928-109.566 179.789 1.00 61.73 C ANISOU 1621 CA GLY A 303 8328 9919 5207 452 -377 208 C ATOM 1622 C GLY A 303 54.579-108.560 178.860 1.00 58.62 C ANISOU 1622 C GLY A 303 7769 9623 4879 302 -461 168 C ATOM 1623 O GLY A 303 54.028-108.228 177.807 1.00 54.94 O ANISOU 1623 O GLY A 303 7310 8980 4584 256 -406 110 O ATOM 1624 N LEU A 304 55.760-108.060 179.234 1.00 63.23 N ANISOU 1624 N LEU A 304 8202 10503 5321 211 -600 209 N ATOM 1625 CA LEU A 304 56.464-107.109 178.379 1.00 60.72 C ANISOU 1625 CA LEU A 304 7717 10309 5045 39 -691 193 C ATOM 1626 C LEU A 304 56.933-107.767 177.087 1.00 63.50 C ANISOU 1626 C LEU A 304 7919 10728 5482 202 -655 293 C ATOM 1627 O LEU A 304 56.894-107.145 176.019 1.00 63.30 O ANISOU 1627 O LEU A 304 7826 10645 5578 95 -655 257 O ATOM 1628 CB LEU A 304 57.648-106.503 179.131 1.00 61.86 C ANISOU 1628 CB LEU A 304 7724 10787 4995 -114 -857 232 C ATOM 1629 CG LEU A 304 57.317-105.410 180.147 1.00 62.74 C ANISOU 1629 CG LEU A 304 7978 10833 5028 -360 -929 98 C ATOM 1630 CD1 LEU A 304 58.537-105.071 180.985 1.00 62.97 C ANISOU 1630 CD1 LEU A 304 7874 11217 4835 -486 -1098 159 C ATOM 1631 CD2 LEU A 304 56.793-104.173 179.434 1.00 59.02 C ANISOU 1631 CD2 LEU A 304 7580 10149 4698 -587 -940 -35 C ATOM 1632 N TYR A 305 57.379-109.023 177.164 1.00 65.48 N ANISOU 1632 N TYR A 305 8128 11094 5657 474 -624 421 N ATOM 1633 CA TYR A 305 57.819-109.722 175.962 1.00 59.73 C ANISOU 1633 CA TYR A 305 7281 10425 4989 670 -583 509 C ATOM 1634 C TYR A 305 56.657-109.967 175.008 1.00 58.39 C ANISOU 1634 C TYR A 305 7260 9900 5024 711 -454 436 C ATOM 1635 O TYR A 305 56.797-109.791 173.792 1.00 61.28 O ANISOU 1635 O TYR A 305 7530 10263 5491 710 -437 436 O ATOM 1636 CB TYR A 305 58.494-111.041 176.338 1.00 57.85 C ANISOU 1636 CB TYR A 305 7012 10357 4610 983 -579 653 C ATOM 1637 CG TYR A 305 58.915-111.869 175.146 1.00 57.30 C ANISOU 1637 CG TYR A 305 6859 10332 4582 1235 -528 736 C ATOM 1638 CD1 TYR A 305 59.945-111.449 174.315 1.00 58.62 C ANISOU 1638 CD1 TYR A 305 6761 10797 4716 1218 -591 792 C ATOM 1639 CD2 TYR A 305 58.288-113.074 174.856 1.00 56.99 C ANISOU 1639 CD2 TYR A 305 7012 10042 4600 1486 -420 760 C ATOM 1640 CE1 TYR A 305 60.336-112.202 173.225 1.00 62.21 C ANISOU 1640 CE1 TYR A 305 7139 11308 5190 1471 -539 862 C ATOM 1641 CE2 TYR A 305 58.673-113.836 173.767 1.00 61.85 C ANISOU 1641 CE2 TYR A 305 7580 10683 5237 1731 -378 823 C ATOM 1642 CZ TYR A 305 59.698-113.394 172.954 1.00 64.62 C ANISOU 1642 CZ TYR A 305 7661 11342 5551 1737 -433 870 C ATOM 1643 OH TYR A 305 60.088-114.144 171.868 1.00 64.21 O ANISOU 1643 OH TYR A 305 7561 11332 5503 2001 -384 926 O ATOM 1644 N LEU A 306 55.502-110.371 175.540 1.00 56.84 N ANISOU 1644 N LEU A 306 7291 9425 4882 737 -363 379 N ATOM 1645 CA LEU A 306 54.331-110.578 174.695 1.00 55.22 C ANISOU 1645 CA LEU A 306 7220 8899 4862 749 -248 312 C ATOM 1646 C LEU A 306 53.815-109.257 174.136 1.00 55.06 C ANISOU 1646 C LEU A 306 7179 8769 4972 503 -257 188 C ATOM 1647 O LEU A 306 53.427-109.182 172.964 1.00 48.20 O ANISOU 1647 O LEU A 306 6298 7769 4246 501 -207 161 O ATOM 1648 CB LEU A 306 53.236-111.294 175.484 1.00 56.65 C ANISOU 1648 CB LEU A 306 7627 8850 5047 808 -156 296 C ATOM 1649 CG LEU A 306 51.895-111.487 174.774 1.00 65.94 C ANISOU 1649 CG LEU A 306 8946 9710 6400 785 -40 228 C ATOM 1650 CD1 LEU A 306 52.062-112.305 173.494 1.00 44.68 C ANISOU 1650 CD1 LEU A 306 6237 6952 3786 950 -1 285 C ATOM 1651 CD2 LEU A 306 50.889-112.138 175.713 1.00 45.23 C ANISOU 1651 CD2 LEU A 306 6520 6920 3747 808 39 231 C ATOM 1652 N HIS A 307 53.799-108.207 174.961 1.00 53.06 N ANISOU 1652 N HIS A 307 6940 8559 4663 300 -324 111 N ATOM 1653 CA HIS A 307 53.367-106.898 174.484 1.00 52.85 C ANISOU 1653 CA HIS A 307 6922 8416 4742 75 -347 -5 C ATOM 1654 C HIS A 307 54.310-106.354 173.421 1.00 61.31 C ANISOU 1654 C HIS A 307 7802 9655 5841 -7 -425 38 C ATOM 1655 O HIS A 307 53.875-105.630 172.518 1.00 64.81 O ANISOU 1655 O HIS A 307 8251 9958 6418 -122 -412 -25 O ATOM 1656 CB HIS A 307 53.266-105.925 175.659 1.00 55.71 C ANISOU 1656 CB HIS A 307 7368 8793 5007 -108 -417 -97 C ATOM 1657 CG HIS A 307 52.779-104.561 175.280 1.00 55.15 C ANISOU 1657 CG HIS A 307 7356 8568 5029 -322 -446 -225 C ATOM 1658 ND1 HIS A 307 53.615-103.578 174.797 1.00 55.82 N ANISOU 1658 ND1 HIS A 307 7332 8775 5100 -513 -566 -224 N ATOM 1659 CD2 HIS A 307 51.542-104.012 175.329 1.00 52.09 C ANISOU 1659 CD2 HIS A 307 7134 7920 4739 -370 -374 -349 C ATOM 1660 CE1 HIS A 307 52.913-102.484 174.558 1.00 53.67 C ANISOU 1660 CE1 HIS A 307 7182 8292 4916 -666 -571 -346 C ATOM 1661 NE2 HIS A 307 51.653-102.721 174.873 1.00 53.97 N ANISOU 1661 NE2 HIS A 307 7381 8103 5023 -567 -453 -427 N ATOM 1662 N SER A 308 55.598-106.694 173.507 1.00 62.77 N ANISOU 1662 N SER A 308 7805 10155 5890 54 -507 155 N ATOM 1663 CA SER A 308 56.553-106.217 172.513 1.00 59.59 C ANISOU 1663 CA SER A 308 7189 9963 5488 -27 -578 215 C ATOM 1664 C SER A 308 56.394-106.955 171.190 1.00 65.13 C ANISOU 1664 C SER A 308 7846 10596 6305 160 -484 260 C ATOM 1665 O SER A 308 56.489-106.344 170.120 1.00 67.85 O ANISOU 1665 O SER A 308 8103 10941 6737 53 -495 251 O ATOM 1666 CB SER A 308 57.977-106.362 173.044 1.00 57.04 C ANISOU 1666 CB SER A 308 6661 10046 4967 -12 -693 336 C ATOM 1667 OG SER A 308 58.216-105.448 174.099 1.00 59.45 O ANISOU 1667 OG SER A 308 6994 10431 5164 -249 -806 286 O ATOM 1668 N LEU A 309 56.152-108.268 171.237 1.00 62.03 N ANISOU 1668 N LEU A 309 7528 10137 5905 433 -397 310 N ATOM 1669 CA LEU A 309 55.962-109.019 170.001 1.00 56.02 C ANISOU 1669 CA LEU A 309 6761 9284 5239 617 -311 340 C ATOM 1670 C LEU A 309 54.786-108.486 169.194 1.00 56.46 C ANISOU 1670 C LEU A 309 6933 9033 5488 491 -243 231 C ATOM 1671 O LEU A 309 54.826-108.492 167.959 1.00 60.52 O ANISOU 1671 O LEU A 309 7379 9533 6084 522 -215 242 O ATOM 1672 CB LEU A 309 55.757-110.503 170.307 1.00 50.48 C ANISOU 1672 CB LEU A 309 6190 8496 4492 910 -236 397 C ATOM 1673 CG LEU A 309 56.968-111.289 170.813 1.00 59.47 C ANISOU 1673 CG LEU A 309 7213 9942 5442 1129 -289 528 C ATOM 1674 CD1 LEU A 309 56.588-112.736 171.082 1.00 65.43 C ANISOU 1674 CD1 LEU A 309 8165 10530 6167 1411 -212 575 C ATOM 1675 CD2 LEU A 309 58.114-111.212 169.819 1.00 53.50 C ANISOU 1675 CD2 LEU A 309 6205 9490 4631 1210 -330 609 C ATOM 1676 N ILE A 310 53.747-108.002 169.869 1.00 52.41 N ANISOU 1676 N ILE A 310 6585 8294 5036 358 -217 130 N ATOM 1677 CA ILE A 310 52.530-107.565 169.194 1.00 51.87 C ANISOU 1677 CA ILE A 310 6629 7939 5140 269 -146 32 C ATOM 1678 C ILE A 310 52.631-106.119 168.722 1.00 58.81 C ANISOU 1678 C ILE A 310 7441 8828 6078 29 -216 -28 C ATOM 1679 O ILE A 310 52.239-105.801 167.597 1.00 57.93 O ANISOU 1679 O ILE A 310 7315 8606 6090 -10 -186 -53 O ATOM 1680 CB ILE A 310 51.321-107.773 170.128 1.00 49.09 C ANISOU 1680 CB ILE A 310 6477 7362 4814 266 -75 -41 C ATOM 1681 CG1 ILE A 310 51.078-109.268 170.353 1.00 46.95 C ANISOU 1681 CG1 ILE A 310 6302 7028 4507 487 1 29 C ATOM 1682 CG2 ILE A 310 50.078-107.095 169.569 1.00 48.57 C ANISOU 1682 CG2 ILE A 310 6500 7047 4906 154 -16 -146 C ATOM 1683 CD1 ILE A 310 49.849-109.569 171.178 1.00 48.89 C ANISOU 1683 CD1 ILE A 310 6730 7071 4774 473 80 -21 C ATOM 1684 N PHE A 311 53.160-105.223 169.557 1.00 60.58 N ANISOU 1684 N PHE A 311 7637 9174 6205 -144 -317 -49 N ATOM 1685 CA PHE A 311 53.145-103.799 169.249 1.00 58.86 C ANISOU 1685 CA PHE A 311 7419 8910 6035 -393 -393 -116 C ATOM 1686 C PHE A 311 54.445-103.281 168.649 1.00 61.14 C ANISOU 1686 C PHE A 311 7499 9474 6256 -519 -503 -28 C ATOM 1687 O PHE A 311 54.446-102.188 168.074 1.00 60.52 O ANISOU 1687 O PHE A 311 7418 9341 6234 -724 -560 -61 O ATOM 1688 CB PHE A 311 52.811-102.991 170.509 1.00 61.17 C ANISOU 1688 CB PHE A 311 7856 9126 6261 -539 -445 -214 C ATOM 1689 CG PHE A 311 51.405-103.193 170.996 1.00 71.15 C ANISOU 1689 CG PHE A 311 9316 10122 7598 -458 -335 -313 C ATOM 1690 CD1 PHE A 311 50.365-102.437 170.481 1.00 73.66 C ANISOU 1690 CD1 PHE A 311 9744 10195 8049 -526 -292 -412 C ATOM 1691 CD2 PHE A 311 51.121-104.145 171.960 1.00 77.77 C ANISOU 1691 CD2 PHE A 311 10220 10969 8361 -311 -275 -295 C ATOM 1692 CE1 PHE A 311 49.069-102.623 170.923 1.00 76.16 C ANISOU 1692 CE1 PHE A 311 10209 10308 8418 -445 -188 -493 C ATOM 1693 CE2 PHE A 311 49.827-104.335 172.407 1.00 75.29 C ANISOU 1693 CE2 PHE A 311 10064 10443 8100 -252 -171 -372 C ATOM 1694 CZ PHE A 311 48.800-103.573 171.887 1.00 76.19 C ANISOU 1694 CZ PHE A 311 10263 10342 8343 -318 -125 -471 C ATOM 1695 N LYS A 312 55.544-104.022 168.766 1.00 61.41 N ANISOU 1695 N LYS A 312 7360 9810 6163 -401 -535 91 N ATOM 1696 CA LYS A 312 56.800-103.661 168.120 1.00 66.37 C ANISOU 1696 CA LYS A 312 7749 10756 6714 -497 -626 197 C ATOM 1697 C LYS A 312 56.926-104.449 166.824 1.00 73.71 C ANISOU 1697 C LYS A 312 8567 11735 7705 -296 -542 268 C ATOM 1698 O LYS A 312 57.003-105.682 166.846 1.00 72.94 O ANISOU 1698 O LYS A 312 8461 11679 7572 -17 -469 317 O ATOM 1699 CB LYS A 312 57.995-103.932 169.034 1.00 70.19 C ANISOU 1699 CB LYS A 312 8079 11595 6995 -484 -719 293 C ATOM 1700 CG LYS A 312 58.371-102.770 169.928 1.00 78.60 C ANISOU 1700 CG LYS A 312 9165 12733 7964 -790 -860 255 C ATOM 1701 CD LYS A 312 59.272-101.789 169.198 1.00 85.42 C ANISOU 1701 CD LYS A 312 9848 13815 8792 -1054 -975 322 C ATOM 1702 CE LYS A 312 59.565-100.583 170.067 1.00 92.62 C ANISOU 1702 CE LYS A 312 10833 14749 9611 -1392 -1128 272 C ATOM 1703 NZ LYS A 312 59.905-100.994 171.457 1.00 95.80 N ANISOU 1703 NZ LYS A 312 11250 15294 9854 -1337 -1175 276 N ATOM 1704 N ALA A 313 56.944-103.732 165.698 1.00 71.47 N ANISOU 1704 N ALA A 313 8217 11435 7505 -435 -555 271 N ATOM 1705 CA ALA A 313 57.035-104.390 164.400 1.00 68.37 C ANISOU 1705 CA ALA A 313 7725 11087 7165 -256 -476 327 C ATOM 1706 C ALA A 313 58.341-105.153 164.242 1.00 66.85 C ANISOU 1706 C ALA A 313 7291 11296 6812 -77 -496 466 C ATOM 1707 O ALA A 313 58.387-106.165 163.533 1.00 62.04 O ANISOU 1707 O ALA A 313 6652 10713 6206 193 -409 505 O ATOM 1708 CB ALA A 313 56.899-103.359 163.282 1.00 71.81 C ANISOU 1708 CB ALA A 313 8122 11464 7698 -468 -502 317 C ATOM 1709 N PHE A 314 59.405-104.694 164.899 1.00 70.62 N ANISOU 1709 N PHE A 314 7600 12094 7137 -216 -610 542 N ATOM 1710 CA PHE A 314 60.740-105.215 164.644 1.00 67.19 C ANISOU 1710 CA PHE A 314 6884 12110 6537 -75 -641 690 C ATOM 1711 C PHE A 314 61.715-104.757 165.723 1.00 72.53 C ANISOU 1711 C PHE A 314 7416 13103 7039 -242 -775 758 C ATOM 1712 O PHE A 314 61.906-103.553 165.927 1.00 78.42 O ANISOU 1712 O PHE A 314 8140 13883 7774 -593 -886 745 O ATOM 1713 CB PHE A 314 61.192-104.778 163.245 1.00 55.34 C ANISOU 1713 CB PHE A 314 5196 10775 5057 -153 -639 757 C ATOM 1714 CG PHE A 314 62.671-104.610 163.098 1.00 52.82 C ANISOU 1714 CG PHE A 314 4537 10984 4548 -204 -724 914 C ATOM 1715 CD1 PHE A 314 63.499-105.710 162.964 1.00 54.19 C ANISOU 1715 CD1 PHE A 314 4525 11483 4581 136 -681 1020 C ATOM 1716 CD2 PHE A 314 63.231-103.344 163.062 1.00 54.08 C ANISOU 1716 CD2 PHE A 314 4564 11321 4662 -592 -851 963 C ATOM 1717 CE1 PHE A 314 64.861-105.549 162.819 1.00 61.94 C ANISOU 1717 CE1 PHE A 314 5162 12998 5375 101 -755 1176 C ATOM 1718 CE2 PHE A 314 64.590-103.177 162.916 1.00 56.66 C ANISOU 1718 CE2 PHE A 314 4555 12170 4804 -667 -933 1122 C ATOM 1719 CZ PHE A 314 65.406-104.279 162.789 1.00 59.97 C ANISOU 1719 CZ PHE A 314 4757 12949 5081 -315 -881 1231 C ATOM 1720 N PHE A 315 62.322-105.708 166.429 1.00 64.89 N ANISOU 1720 N PHE A 315 6367 12360 5929 6 -774 832 N ATOM 1721 CA PHE A 315 63.277-105.388 167.481 1.00 69.08 C ANISOU 1721 CA PHE A 315 6746 13225 6276 -126 -905 906 C ATOM 1722 C PHE A 315 64.275-106.530 167.608 1.00 73.43 C ANISOU 1722 C PHE A 315 7087 14161 6652 220 -889 1045 C ATOM 1723 O PHE A 315 64.139-107.579 166.973 1.00 83.92 O ANISOU 1723 O PHE A 315 8439 15440 8007 568 -776 1065 O ATOM 1724 CB PHE A 315 62.576-105.122 168.821 1.00 70.74 C ANISOU 1724 CB PHE A 315 7204 13175 6500 -245 -940 796 C ATOM 1725 CG PHE A 315 61.869-106.323 169.395 1.00 67.48 C ANISOU 1725 CG PHE A 315 6991 12533 6115 81 -832 755 C ATOM 1726 CD1 PHE A 315 62.531-107.196 170.245 1.00 67.04 C ANISOU 1726 CD1 PHE A 315 6862 12718 5894 304 -854 844 C ATOM 1727 CD2 PHE A 315 60.538-106.569 169.097 1.00 62.42 C ANISOU 1727 CD2 PHE A 315 6614 11445 5657 151 -716 636 C ATOM 1728 CE1 PHE A 315 61.885-108.298 170.774 1.00 62.48 C ANISOU 1728 CE1 PHE A 315 6490 11915 5334 585 -762 818 C ATOM 1729 CE2 PHE A 315 59.885-107.668 169.626 1.00 57.52 C ANISOU 1729 CE2 PHE A 315 6182 10619 5052 413 -624 611 C ATOM 1730 CZ PHE A 315 60.560-108.533 170.466 1.00 57.51 C ANISOU 1730 CZ PHE A 315 6126 10837 4886 626 -648 704 C ATOM 1731 N SER A 316 65.285-106.311 168.445 1.00 66.22 N ANISOU 1731 N SER A 316 5977 13633 5549 125 -1011 1140 N ATOM 1732 CA SER A 316 66.314-107.309 168.704 1.00 67.46 C ANISOU 1732 CA SER A 316 5914 14204 5513 451 -1015 1283 C ATOM 1733 C SER A 316 65.939-108.107 169.947 1.00 76.98 C ANISOU 1733 C SER A 316 7322 15251 6674 653 -1000 1250 C ATOM 1734 O SER A 316 65.836-107.546 171.044 1.00 75.43 O ANISOU 1734 O SER A 316 7205 15020 6434 422 -1092 1207 O ATOM 1735 CB SER A 316 67.678-106.644 168.883 1.00 68.19 C ANISOU 1735 CB SER A 316 5641 14862 5405 232 -1163 1427 C ATOM 1736 OG SER A 316 68.669-107.597 169.224 1.00 67.22 O ANISOU 1736 OG SER A 316 5313 15122 5105 561 -1150 1559 O ATOM 1737 N GLU A 317 65.733-109.416 169.776 1.00 83.74 N ANISOU 1737 N GLU A 317 8279 16005 7533 1080 -887 1271 N ATOM 1738 CA GLU A 317 65.390-110.261 170.915 1.00 86.07 C ANISOU 1738 CA GLU A 317 8776 16149 7777 1286 -869 1260 C ATOM 1739 C GLU A 317 66.577-110.462 171.847 1.00 86.52 C ANISOU 1739 C GLU A 317 8603 16680 7590 1364 -981 1398 C ATOM 1740 O GLU A 317 66.390-110.590 173.062 1.00 87.51 O ANISOU 1740 O GLU A 317 8858 16741 7652 1341 -1026 1382 O ATOM 1741 CB GLU A 317 64.864-111.613 170.435 1.00 90.60 C ANISOU 1741 CB GLU A 317 9549 16465 8411 1707 -730 1253 C ATOM 1742 CG GLU A 317 63.420-111.591 169.967 1.00 90.91 C ANISOU 1742 CG GLU A 317 9901 15960 8683 1630 -624 1103 C ATOM 1743 CD GLU A 317 62.876-112.982 169.710 1.00 94.20 C ANISOU 1743 CD GLU A 317 10553 16102 9135 2011 -508 1099 C ATOM 1744 OE1 GLU A 317 63.681-113.893 169.421 1.00 98.88 O ANISOU 1744 OE1 GLU A 317 11046 16927 9596 2363 -492 1206 O ATOM 1745 OE2 GLU A 317 61.644-113.168 169.804 1.00 93.80 O ANISOU 1745 OE2 GLU A 317 10794 15611 9233 1960 -435 993 O ATOM 1746 N LYS A 318 67.795-110.500 171.303 1.00 88.05 N ANISOU 1746 N LYS A 318 8447 17374 7635 1460 -1027 1540 N ATOM 1747 CA LYS A 318 68.978-110.657 172.144 1.00 92.67 C ANISOU 1747 CA LYS A 318 8814 18339 8057 1497 -1080 1647 C ATOM 1748 C LYS A 318 69.139-109.471 173.086 1.00 92.12 C ANISOU 1748 C LYS A 318 8701 18355 7945 1036 -1224 1616 C ATOM 1749 O LYS A 318 69.405-109.642 174.281 1.00 98.60 O ANISOU 1749 O LYS A 318 9551 19246 8667 1037 -1279 1635 O ATOM 1750 CB LYS A 318 70.223-110.823 171.272 1.00 96.88 C ANISOU 1750 CB LYS A 318 9023 19245 8540 1617 -1007 1752 C ATOM 1751 CG LYS A 318 71.529-110.741 172.045 1.00107.49 C ANISOU 1751 CG LYS A 318 10111 20998 9733 1562 -1046 1856 C ATOM 1752 CD LYS A 318 72.729-110.828 171.117 1.00117.19 C ANISOU 1752 CD LYS A 318 11020 22621 10884 1657 -958 1963 C ATOM 1753 CE LYS A 318 72.745-112.145 170.361 1.00121.32 C ANISOU 1753 CE LYS A 318 11604 23096 11397 2183 -805 1979 C ATOM 1754 NZ LYS A 318 73.944-112.265 169.486 1.00125.26 N ANISOU 1754 NZ LYS A 318 11803 24009 11782 2298 -706 2080 N ATOM 1755 N LYS A 319 68.977-108.256 172.561 1.00 86.12 N ANISOU 1755 N LYS A 319 7893 17573 7258 635 -1288 1564 N ATOM 1756 CA LYS A 319 69.129-107.069 173.395 1.00 91.34 C ANISOU 1756 CA LYS A 319 8554 18271 7882 178 -1428 1521 C ATOM 1757 C LYS A 319 67.974-106.934 174.379 1.00 89.34 C ANISOU 1757 C LYS A 319 8633 17674 7637 94 -1481 1392 C ATOM 1758 O LYS A 319 68.171-106.503 175.521 1.00 86.08 O ANISOU 1758 O LYS A 319 8261 17315 7130 -104 -1580 1370 O ATOM 1759 CB LYS A 319 69.234-105.827 172.515 1.00 95.32 C ANISOU 1759 CB LYS A 319 8962 18787 8466 -222 -1475 1500 C ATOM 1760 CG LYS A 319 69.787-104.615 173.230 1.00104.08 C ANISOU 1760 CG LYS A 319 10024 20004 9518 -687 -1611 1492 C ATOM 1761 CD LYS A 319 69.434-103.350 172.484 1.00108.35 C ANISOU 1761 CD LYS A 319 10624 20378 10165 -1094 -1667 1427 C ATOM 1762 CE LYS A 319 69.853-103.411 171.026 1.00110.31 C ANISOU 1762 CE LYS A 319 10665 20774 10474 -1024 -1573 1516 C ATOM 1763 NZ LYS A 319 71.332-103.408 170.876 1.00116.01 N ANISOU 1763 NZ LYS A 319 11057 21946 11074 -1051 -1549 1678 N ATOM 1764 N TYR A 320 66.760-107.291 173.952 1.00 85.24 N ANISOU 1764 N TYR A 320 8406 16654 7326 228 -1335 1268 N ATOM 1765 CA TYR A 320 65.617-107.255 174.859 1.00 81.80 C ANISOU 1765 CA TYR A 320 8321 15781 6978 175 -1298 1123 C ATOM 1766 C TYR A 320 65.762-108.285 175.972 1.00 85.22 C ANISOU 1766 C TYR A 320 8814 16293 7271 457 -1293 1183 C ATOM 1767 O TYR A 320 65.390-108.020 177.121 1.00 85.81 O ANISOU 1767 O TYR A 320 9054 16253 7297 325 -1341 1115 O ATOM 1768 CB TYR A 320 64.322-107.480 174.080 1.00 77.69 C ANISOU 1768 CB TYR A 320 8060 14760 6698 267 -1142 1000 C ATOM 1769 CG TYR A 320 63.644-106.206 173.628 1.00 77.69 C ANISOU 1769 CG TYR A 320 8172 14494 6852 -97 -1161 869 C ATOM 1770 CD1 TYR A 320 64.353-105.217 172.957 1.00 80.13 C ANISOU 1770 CD1 TYR A 320 8273 15034 7138 -378 -1258 911 C ATOM 1771 CD2 TYR A 320 62.291-105.997 173.862 1.00 74.30 C ANISOU 1771 CD2 TYR A 320 8059 13591 6581 -154 -1081 711 C ATOM 1772 CE1 TYR A 320 63.735-104.052 172.542 1.00 79.46 C ANISOU 1772 CE1 TYR A 320 8320 14683 7188 -700 -1281 797 C ATOM 1773 CE2 TYR A 320 61.664-104.837 173.448 1.00 74.75 C ANISOU 1773 CE2 TYR A 320 8229 13402 6769 -451 -1098 593 C ATOM 1774 CZ TYR A 320 62.390-103.869 172.789 1.00 79.82 C ANISOU 1774 CZ TYR A 320 8690 14249 7390 -719 -1201 635 C ATOM 1775 OH TYR A 320 61.768-102.713 172.376 1.00 81.68 O ANISOU 1775 OH TYR A 320 9066 14217 7751 -1004 -1225 523 O ATOM 1776 N LEU A 321 66.300-109.465 175.652 1.00 84.08 N ANISOU 1776 N LEU A 321 8554 16340 7053 857 -1234 1310 N ATOM 1777 CA LEU A 321 66.549-110.465 176.685 1.00 83.49 C ANISOU 1777 CA LEU A 321 8529 16367 6825 1142 -1241 1391 C ATOM 1778 C LEU A 321 67.585-109.978 177.688 1.00 88.57 C ANISOU 1778 C LEU A 321 8953 17456 7244 971 -1409 1476 C ATOM 1779 O LEU A 321 67.490-110.290 178.880 1.00 88.84 O ANISOU 1779 O LEU A 321 9109 17463 7183 1015 -1440 1478 O ATOM 1780 CB LEU A 321 66.998-111.782 176.050 1.00 83.40 C ANISOU 1780 CB LEU A 321 8443 16479 6768 1622 -1154 1513 C ATOM 1781 CG LEU A 321 67.361-112.921 177.007 1.00 85.61 C ANISOU 1781 CG LEU A 321 8778 16861 6891 1967 -1154 1616 C ATOM 1782 CD1 LEU A 321 66.182-113.276 177.902 1.00 82.30 C ANISOU 1782 CD1 LEU A 321 8734 16002 6535 1967 -1102 1525 C ATOM 1783 CD2 LEU A 321 67.843-114.142 176.238 1.00 84.41 C ANISOU 1783 CD2 LEU A 321 8583 16739 6751 2419 -1038 1700 C ATOM 1784 N TRP A 322 68.576-109.212 177.227 1.00 95.28 N ANISOU 1784 N TRP A 322 9513 18598 8093 742 -1464 1520 N ATOM 1785 CA TRP A 322 69.548-108.630 178.145 1.00100.40 C ANISOU 1785 CA TRP A 322 9990 19531 8627 501 -1573 1563 C ATOM 1786 C TRP A 322 68.892-107.596 179.051 1.00 97.89 C ANISOU 1786 C TRP A 322 9879 19027 8289 111 -1690 1433 C ATOM 1787 O TRP A 322 69.206-107.518 180.245 1.00 99.91 O ANISOU 1787 O TRP A 322 10158 19373 8429 32 -1765 1437 O ATOM 1788 CB TRP A 322 70.701-108.007 177.358 1.00107.79 C ANISOU 1788 CB TRP A 322 10589 20806 9562 317 -1590 1646 C ATOM 1789 CG TRP A 322 71.881-107.636 178.202 1.00116.18 C ANISOU 1789 CG TRP A 322 11436 22221 10485 140 -1678 1727 C ATOM 1790 CD1 TRP A 322 72.934-108.438 178.535 1.00122.03 C ANISOU 1790 CD1 TRP A 322 11961 23297 11108 405 -1640 1859 C ATOM 1791 CD2 TRP A 322 72.134-106.366 178.817 1.00120.72 C ANISOU 1791 CD2 TRP A 322 12005 22846 11018 -341 -1819 1681 C ATOM 1792 NE1 TRP A 322 73.825-107.748 179.321 1.00126.98 N ANISOU 1792 NE1 TRP A 322 12427 24203 11618 112 -1749 1906 N ATOM 1793 CE2 TRP A 322 73.357-106.474 179.509 1.00126.85 C ANISOU 1793 CE2 TRP A 322 12545 24008 11646 -352 -1862 1797 C ATOM 1794 CE3 TRP A 322 71.444-105.150 178.851 1.00118.67 C ANISOU 1794 CE3 TRP A 322 11936 22330 10824 -757 -1911 1548 C ATOM 1795 CZ2 TRP A 322 73.905-105.413 180.226 1.00129.10 C ANISOU 1795 CZ2 TRP A 322 12779 24425 11847 -775 -1998 1790 C ATOM 1796 CZ3 TRP A 322 71.990-104.098 179.564 1.00121.50 C ANISOU 1796 CZ3 TRP A 322 12267 22794 11104 -1165 -2044 1533 C ATOM 1797 CH2 TRP A 322 73.208-104.236 180.241 1.00126.55 C ANISOU 1797 CH2 TRP A 322 12670 23819 11596 -1177 -2088 1655 C ATOM 1798 N GLY A 323 67.974-106.796 178.503 1.00 93.04 N ANISOU 1798 N GLY A 323 9427 18147 7778 -127 -1704 1310 N ATOM 1799 CA GLY A 323 67.243-105.850 179.327 1.00 91.11 C ANISOU 1799 CA GLY A 323 9428 17672 7518 -462 -1792 1161 C ATOM 1800 C GLY A 323 66.234-106.516 180.240 1.00 85.34 C ANISOU 1800 C GLY A 323 9014 16590 6823 -264 -1695 1072 C ATOM 1801 O GLY A 323 65.941-106.004 181.324 1.00 84.08 O ANISOU 1801 O GLY A 323 9017 16345 6586 -456 -1766 982 O ATOM 1802 N PHE A 324 65.688-107.660 179.819 1.00 79.42 N ANISOU 1802 N PHE A 324 8363 15636 6179 112 -1534 1096 N ATOM 1803 CA PHE A 324 64.761-108.394 180.674 1.00 77.57 C ANISOU 1803 CA PHE A 324 8415 15093 5963 301 -1441 1040 C ATOM 1804 C PHE A 324 65.479-109.045 181.850 1.00 82.03 C ANISOU 1804 C PHE A 324 8907 15968 6292 458 -1520 1159 C ATOM 1805 O PHE A 324 64.909-109.144 182.943 1.00 80.76 O ANISOU 1805 O PHE A 324 8960 15650 6077 441 -1516 1100 O ATOM 1806 CB PHE A 324 64.016-109.450 179.857 1.00 76.33 C ANISOU 1806 CB PHE A 324 8394 14634 5975 630 -1262 1045 C ATOM 1807 CG PHE A 324 63.028-108.878 178.878 1.00 79.09 C ANISOU 1807 CG PHE A 324 8880 14606 6563 485 -1169 908 C ATOM 1808 CD1 PHE A 324 62.542-107.589 179.033 1.00 80.28 C ANISOU 1808 CD1 PHE A 324 9125 14598 6779 121 -1220 766 C ATOM 1809 CD2 PHE A 324 62.584-109.632 177.803 1.00 75.51 C ANISOU 1809 CD2 PHE A 324 8475 13955 6261 723 -1035 921 C ATOM 1810 CE1 PHE A 324 61.633-107.063 178.133 1.00 76.07 C ANISOU 1810 CE1 PHE A 324 8717 13729 6459 10 -1137 649 C ATOM 1811 CE2 PHE A 324 61.675-109.111 176.902 1.00 74.22 C ANISOU 1811 CE2 PHE A 324 8427 13465 6308 591 -955 803 C ATOM 1812 CZ PHE A 324 61.199-107.825 177.067 1.00 74.31 C ANISOU 1812 CZ PHE A 324 8516 13334 6385 241 -1005 671 C ATOM 1813 N THR A 325 66.719-109.497 181.647 1.00 78.58 N ANISOU 1813 N THR A 325 8165 15989 5701 624 -1592 1332 N ATOM 1814 CA THR A 325 67.482-110.081 182.745 1.00 82.00 C ANISOU 1814 CA THR A 325 8524 16645 5986 765 -1636 1431 C ATOM 1815 C THR A 325 67.796-109.039 183.812 1.00 87.49 C ANISOU 1815 C THR A 325 9208 17454 6580 387 -1777 1366 C ATOM 1816 O THR A 325 67.673-109.314 185.012 1.00 90.57 O ANISOU 1816 O THR A 325 9727 17829 6858 423 -1806 1363 O ATOM 1817 CB THR A 325 68.771-110.712 182.215 1.00 82.16 C ANISOU 1817 CB THR A 325 8231 16994 5992 1002 -1610 1584 C ATOM 1818 OG1 THR A 325 68.449-111.777 181.312 1.00 75.23 O ANISOU 1818 OG1 THR A 325 7414 15973 5196 1389 -1477 1632 O ATOM 1819 CG2 THR A 325 69.608-111.265 183.360 1.00 85.11 C ANISOU 1819 CG2 THR A 325 8517 17603 6220 1134 -1654 1682 C ATOM 1820 N VAL A 326 68.199-107.838 183.394 1.00 86.88 N ANISOU 1820 N VAL A 326 8997 17475 6538 17 -1865 1315 N ATOM 1821 CA VAL A 326 68.459-106.765 184.349 1.00 87.65 C ANISOU 1821 CA VAL A 326 9127 17629 6545 -367 -2004 1238 C ATOM 1822 C VAL A 326 67.169-106.347 185.045 1.00 88.02 C ANISOU 1822 C VAL A 326 9535 17332 6576 -501 -2009 1066 C ATOM 1823 O VAL A 326 67.167-106.022 186.238 1.00 93.97 O ANISOU 1823 O VAL A 326 10404 18088 7211 -638 -2085 1010 O ATOM 1824 CB VAL A 326 69.134-105.577 183.639 1.00 86.61 C ANISOU 1824 CB VAL A 326 8809 17630 6467 -739 -2088 1226 C ATOM 1825 CG1 VAL A 326 69.404-104.446 184.620 1.00 86.22 C ANISOU 1825 CG1 VAL A 326 8834 17601 6325 -1142 -2236 1142 C ATOM 1826 CG2 VAL A 326 70.422-106.025 182.964 1.00 89.68 C ANISOU 1826 CG2 VAL A 326 8827 18397 6850 -594 -2059 1402 C ATOM 1827 N PHE A 327 66.052-106.359 184.316 1.00 82.91 N ANISOU 1827 N PHE A 327 9074 16370 6057 -452 -1909 973 N ATOM 1828 CA PHE A 327 64.773-105.987 184.911 1.00 81.68 C ANISOU 1828 CA PHE A 327 9275 15769 5991 -547 -1835 787 C ATOM 1829 C PHE A 327 64.311-107.028 185.925 1.00 85.37 C ANISOU 1829 C PHE A 327 9902 16157 6377 -269 -1756 819 C ATOM 1830 O PHE A 327 63.812-106.677 187.001 1.00 79.93 O ANISOU 1830 O PHE A 327 9415 15352 5601 -388 -1781 717 O ATOM 1831 CB PHE A 327 63.726-105.801 183.810 1.00 74.43 C ANISOU 1831 CB PHE A 327 8506 14427 5347 -536 -1686 677 C ATOM 1832 CG PHE A 327 62.399-105.294 184.304 1.00 74.56 C ANISOU 1832 CG PHE A 327 8859 14011 5458 -643 -1608 483 C ATOM 1833 CD1 PHE A 327 62.171-103.935 184.448 1.00 76.55 C ANISOU 1833 CD1 PHE A 327 9231 14137 5715 -992 -1697 331 C ATOM 1834 CD2 PHE A 327 61.372-106.175 184.606 1.00 72.07 C ANISOU 1834 CD2 PHE A 327 8746 13420 5217 -391 -1447 458 C ATOM 1835 CE1 PHE A 327 60.950-103.465 184.895 1.00 75.88 C ANISOU 1835 CE1 PHE A 327 9452 13674 5704 -1051 -1619 151 C ATOM 1836 CE2 PHE A 327 60.149-105.711 185.053 1.00 70.52 C ANISOU 1836 CE2 PHE A 327 8829 12871 5094 -477 -1369 290 C ATOM 1837 CZ PHE A 327 59.937-104.354 185.198 1.00 72.94 C ANISOU 1837 CZ PHE A 327 9243 13070 5401 -789 -1451 133 C ATOM 1838 N GLY A 328 64.481-108.309 185.607 1.00 89.42 N ANISOU 1838 N GLY A 328 10342 16731 6903 103 -1664 962 N ATOM 1839 CA GLY A 328 63.980-109.378 186.448 1.00 80.90 C ANISOU 1839 CA GLY A 328 9442 15532 5763 376 -1579 1007 C ATOM 1840 C GLY A 328 64.818-109.669 187.676 1.00 81.32 C ANISOU 1840 C GLY A 328 9404 15950 5543 422 -1707 1117 C ATOM 1841 O GLY A 328 64.272-109.924 188.753 1.00 88.22 O ANISOU 1841 O GLY A 328 10482 16708 6330 452 -1684 1085 O ATOM 1842 N TRP A 329 66.142-109.644 187.532 1.00 77.08 N ANISOU 1842 N TRP A 329 8566 15777 4945 422 -1806 1234 N ATOM 1843 CA TRP A 329 67.037-109.956 188.639 1.00 80.65 C ANISOU 1843 CA TRP A 329 8915 16476 5253 470 -1884 1326 C ATOM 1844 C TRP A 329 67.653-108.727 189.289 1.00 84.92 C ANISOU 1844 C TRP A 329 9368 17191 5709 74 -2040 1252 C ATOM 1845 O TRP A 329 68.022-108.785 190.467 1.00 92.73 O ANISOU 1845 O TRP A 329 10375 18303 6557 45 -2110 1274 O ATOM 1846 CB TRP A 329 68.165-110.884 188.171 1.00 81.01 C ANISOU 1846 CB TRP A 329 8688 16787 5305 773 -1860 1507 C ATOM 1847 CG TRP A 329 67.698-112.235 187.722 1.00 79.83 C ANISOU 1847 CG TRP A 329 8658 16459 5215 1201 -1719 1592 C ATOM 1848 CD1 TRP A 329 67.727-112.731 186.452 1.00 84.54 C ANISOU 1848 CD1 TRP A 329 9180 17007 5934 1414 -1627 1638 C ATOM 1849 CD2 TRP A 329 67.131-113.265 188.542 1.00 84.25 C ANISOU 1849 CD2 TRP A 329 9457 16842 5710 1456 -1654 1640 C ATOM 1850 NE1 TRP A 329 67.215-114.006 186.430 1.00 83.04 N ANISOU 1850 NE1 TRP A 329 9186 16603 5763 1788 -1515 1705 N ATOM 1851 CE2 TRP A 329 66.841-114.357 187.700 1.00 84.57 C ANISOU 1851 CE2 TRP A 329 9575 16712 5847 1812 -1529 1714 C ATOM 1852 CE3 TRP A 329 66.841-113.370 189.906 1.00 81.07 C ANISOU 1852 CE3 TRP A 329 9224 16403 5177 1412 -1689 1630 C ATOM 1853 CZ2 TRP A 329 66.275-115.538 188.177 1.00 84.70 C ANISOU 1853 CZ2 TRP A 329 9843 16504 5837 2105 -1443 1782 C ATOM 1854 CZ3 TRP A 329 66.278-114.543 190.377 1.00 80.70 C ANISOU 1854 CZ3 TRP A 329 9405 16157 5101 1706 -1598 1704 C ATOM 1855 CH2 TRP A 329 66.002-115.611 189.515 1.00 79.70 C ANISOU 1855 CH2 TRP A 329 9362 15845 5077 2040 -1479 1782 C ATOM 1856 N GLY A 330 67.774-107.621 188.560 1.00 84.93 N ANISOU 1856 N GLY A 330 9290 17190 5788 -236 -2098 1169 N ATOM 1857 CA GLY A 330 68.435-106.443 189.087 1.00 89.68 C ANISOU 1857 CA GLY A 330 9819 17937 6318 -625 -2249 1109 C ATOM 1858 C GLY A 330 67.563-105.588 189.981 1.00 88.95 C ANISOU 1858 C GLY A 330 10039 17596 6161 -884 -2302 920 C ATOM 1859 O GLY A 330 67.925-105.317 191.130 1.00 91.62 O ANISOU 1859 O GLY A 330 10417 18035 6358 -1003 -2396 900 O ATOM 1860 N LEU A 331 66.414-105.152 189.464 1.00 88.18 N ANISOU 1860 N LEU A 331 10168 17176 6160 -964 -2239 775 N ATOM 1861 CA LEU A 331 65.541-104.277 190.243 1.00 91.09 C ANISOU 1861 CA LEU A 331 10848 17291 6470 -1198 -2273 575 C ATOM 1862 C LEU A 331 65.067-104.901 191.552 1.00 91.31 C ANISOU 1862 C LEU A 331 11061 17282 6352 -1031 -2235 562 C ATOM 1863 O LEU A 331 65.061-104.185 192.569 1.00 88.40 O ANISOU 1863 O LEU A 331 10837 16887 5866 -1239 -2325 452 O ATOM 1864 CB LEU A 331 64.346-103.830 189.390 1.00 88.63 C ANISOU 1864 CB LEU A 331 10738 16647 6290 -1262 -2185 429 C ATOM 1865 CG LEU A 331 64.524-102.555 188.562 1.00 91.05 C ANISOU 1865 CG LEU A 331 11028 16863 6705 -1605 -2269 335 C ATOM 1866 CD1 LEU A 331 65.530-102.758 187.438 1.00 95.08 C ANISOU 1866 CD1 LEU A 331 11198 17614 7312 -1578 -2286 499 C ATOM 1867 CD2 LEU A 331 63.187-102.083 188.012 1.00 92.39 C ANISOU 1867 CD2 LEU A 331 11471 16549 7082 -1625 -2134 155 C ATOM 1868 N PRO A 332 64.654-106.175 191.613 1.00 92.41 N ANISOU 1868 N PRO A 332 11227 17401 6486 -673 -2107 668 N ATOM 1869 CA PRO A 332 64.337-106.755 192.930 1.00 92.49 C ANISOU 1869 CA PRO A 332 11397 17402 6345 -537 -2082 680 C ATOM 1870 C PRO A 332 65.488-106.671 193.914 1.00 99.10 C ANISOU 1870 C PRO A 332 12089 18527 7037 -612 -2222 755 C ATOM 1871 O PRO A 332 65.262-106.404 195.099 1.00101.60 O ANISOU 1871 O PRO A 332 12575 18817 7213 -701 -2265 678 O ATOM 1872 CB PRO A 332 63.974-108.205 192.589 1.00 91.47 C ANISOU 1872 CB PRO A 332 11268 17225 6262 -136 -1933 828 C ATOM 1873 CG PRO A 332 63.429-108.122 191.217 1.00 92.40 C ANISOU 1873 CG PRO A 332 11384 17127 6598 -111 -1830 785 C ATOM 1874 CD PRO A 332 64.271-107.089 190.520 1.00 92.86 C ANISOU 1874 CD PRO A 332 11231 17379 6673 -388 -1970 759 C ATOM 1875 N ALA A 333 66.724-106.874 193.453 1.00102.68 N ANISOU 1875 N ALA A 333 12231 19269 7515 -578 -2289 902 N ATOM 1876 CA ALA A 333 67.875-106.736 194.336 1.00105.10 C ANISOU 1876 CA ALA A 333 12372 19880 7682 -671 -2422 977 C ATOM 1877 C ALA A 333 68.087-105.299 194.792 1.00107.74 C ANISOU 1877 C ALA A 333 12774 20206 7956 -1095 -2567 825 C ATOM 1878 O ALA A 333 68.766-105.078 195.801 1.00112.99 O ANISOU 1878 O ALA A 333 13398 21060 8473 -1205 -2679 843 O ATOM 1879 CB ALA A 333 69.137-107.253 193.644 1.00103.44 C ANISOU 1879 CB ALA A 333 11794 19996 7513 -535 -2441 1166 C ATOM 1880 N ILE A 334 67.522-104.323 194.082 1.00103.68 N ANISOU 1880 N ILE A 334 12379 19465 7550 -1332 -2569 676 N ATOM 1881 CA ILE A 334 67.729-102.923 194.439 1.00105.60 C ANISOU 1881 CA ILE A 334 12720 19653 7748 -1734 -2708 529 C ATOM 1882 C ILE A 334 66.897-102.547 195.659 1.00104.78 C ANISOU 1882 C ILE A 334 12956 19341 7515 -1799 -2720 358 C ATOM 1883 O ILE A 334 67.437-102.159 196.701 1.00113.79 O ANISOU 1883 O ILE A 334 14121 20609 8506 -1942 -2838 336 O ATOM 1884 CB ILE A 334 67.419-102.007 193.241 1.00108.77 C ANISOU 1884 CB ILE A 334 13153 19857 8316 -1955 -2706 432 C ATOM 1885 CG1 ILE A 334 68.424-102.247 192.114 1.00105.38 C ANISOU 1885 CG1 ILE A 334 12362 19686 7989 -1933 -2711 606 C ATOM 1886 CG2 ILE A 334 67.435-100.547 193.669 1.00113.42 C ANISOU 1886 CG2 ILE A 334 13933 20298 8863 -2353 -2839 258 C ATOM 1887 CD1 ILE A 334 68.240-101.333 190.926 1.00102.59 C ANISOU 1887 CD1 ILE A 334 12019 19167 7794 -2168 -2717 534 C ATOM 1888 N PHE A 335 65.570-102.657 195.554 1.00 96.17 N ANISOU 1888 N PHE A 335 12129 17940 6472 -1690 -2592 235 N ATOM 1889 CA PHE A 335 64.723-102.251 196.669 1.00 99.67 C ANISOU 1889 CA PHE A 335 12897 18184 6788 -1742 -2582 61 C ATOM 1890 C PHE A 335 64.701-103.266 197.806 1.00 99.00 C ANISOU 1890 C PHE A 335 12834 18234 6547 -1498 -2541 157 C ATOM 1891 O PHE A 335 64.214-102.937 198.893 1.00 99.16 O ANISOU 1891 O PHE A 335 13090 18158 6429 -1547 -2552 33 O ATOM 1892 CB PHE A 335 63.292-101.961 196.193 1.00 99.75 C ANISOU 1892 CB PHE A 335 13177 17829 6894 -1717 -2446 -110 C ATOM 1893 CG PHE A 335 62.677-103.052 195.360 1.00100.40 C ANISOU 1893 CG PHE A 335 13193 17864 7090 -1427 -2275 -5 C ATOM 1894 CD1 PHE A 335 62.142-104.183 195.955 1.00102.96 C ANISOU 1894 CD1 PHE A 335 13580 18201 7339 -1137 -2151 77 C ATOM 1895 CD2 PHE A 335 62.596-102.925 193.983 1.00 98.92 C ANISOU 1895 CD2 PHE A 335 12902 17602 7083 -1451 -2237 10 C ATOM 1896 CE1 PHE A 335 61.563-105.179 195.190 1.00100.93 C ANISOU 1896 CE1 PHE A 335 13288 17868 7195 -873 -1992 175 C ATOM 1897 CE2 PHE A 335 62.018-103.917 193.213 1.00 97.07 C ANISOU 1897 CE2 PHE A 335 12624 17270 6988 -1170 -2068 99 C ATOM 1898 CZ PHE A 335 61.497-105.043 193.818 1.00 99.46 C ANISOU 1898 CZ PHE A 335 13001 17535 7255 -876 -1936 178 C ATOM 1899 N VAL A 336 65.213-104.479 197.594 1.00100.06 N ANISOU 1899 N VAL A 336 12744 18576 6697 -1227 -2492 372 N ATOM 1900 CA VAL A 336 65.421-105.389 198.716 1.00 96.51 C ANISOU 1900 CA VAL A 336 12297 18279 6092 -1023 -2484 485 C ATOM 1901 C VAL A 336 66.654-104.976 199.509 1.00 93.86 C ANISOU 1901 C VAL A 336 11812 18232 5620 -1194 -2663 530 C ATOM 1902 O VAL A 336 66.659-105.033 200.744 1.00 95.74 O ANISOU 1902 O VAL A 336 12167 18524 5687 -1193 -2706 508 O ATOM 1903 CB VAL A 336 65.516-106.845 198.220 1.00 91.85 C ANISOU 1903 CB VAL A 336 11558 17771 5571 -654 -2368 696 C ATOM 1904 CG1 VAL A 336 66.195-107.728 199.256 1.00 91.65 C ANISOU 1904 CG1 VAL A 336 11452 17977 5396 -471 -2406 854 C ATOM 1905 CG2 VAL A 336 64.130-107.383 197.901 1.00 86.22 C ANISOU 1905 CG2 VAL A 336 11069 16760 4930 -472 -2182 650 C ATOM 1906 N ALA A 337 67.710-104.537 198.818 1.00 97.11 N ANISOU 1906 N ALA A 337 11959 18842 6098 -1352 -2765 595 N ATOM 1907 CA ALA A 337 68.881-104.015 199.515 1.00104.73 C ANISOU 1907 CA ALA A 337 12774 20085 6933 -1563 -2937 630 C ATOM 1908 C ALA A 337 68.533-102.760 200.305 1.00110.28 C ANISOU 1908 C ALA A 337 13746 20620 7535 -1881 -3039 413 C ATOM 1909 O ALA A 337 69.016-102.570 201.428 1.00116.80 O ANISOU 1909 O ALA A 337 14599 21592 8186 -1971 -3147 405 O ATOM 1910 CB ALA A 337 70.004-103.730 198.519 1.00 99.56 C ANISOU 1910 CB ALA A 337 11784 19668 6377 -1693 -3004 742 C ATOM 1911 N VAL A 338 67.695-101.891 199.733 1.00104.99 N ANISOU 1911 N VAL A 338 13289 19634 6970 -2043 -3007 231 N ATOM 1912 CA VAL A 338 67.210-100.727 200.470 1.00108.09 C ANISOU 1912 CA VAL A 338 13991 19806 7271 -2293 -3082 3 C ATOM 1913 C VAL A 338 66.367-101.166 201.658 1.00111.88 C ANISOU 1913 C VAL A 338 14725 20185 7600 -2112 -3010 -72 C ATOM 1914 O VAL A 338 66.363-100.510 202.708 1.00117.22 O ANISOU 1914 O VAL A 338 15588 20831 8119 -2257 -3101 -199 O ATOM 1915 CB VAL A 338 66.426 -99.791 199.528 1.00104.04 C ANISOU 1915 CB VAL A 338 13661 18954 6918 -2454 -3042 -170 C ATOM 1916 CG1 VAL A 338 65.901 -98.579 200.283 1.00104.04 C ANISOU 1916 CG1 VAL A 338 14007 18696 6826 -2676 -3113 -417 C ATOM 1917 CG2 VAL A 338 67.303 -99.356 198.365 1.00103.82 C ANISOU 1917 CG2 VAL A 338 13376 19040 7032 -2646 -3114 -80 C ATOM 1918 N TRP A 339 65.652-102.285 201.522 1.00107.23 N ANISOU 1918 N TRP A 339 14150 19545 7047 -1795 -2844 11 N ATOM 1919 CA TRP A 339 64.860-102.805 202.632 1.00103.73 C ANISOU 1919 CA TRP A 339 13928 19027 6457 -1616 -2757 -28 C ATOM 1920 C TRP A 339 65.756-103.263 203.776 1.00102.41 C ANISOU 1920 C TRP A 339 13654 19154 6104 -1575 -2861 94 C ATOM 1921 O TRP A 339 65.501-102.943 204.943 1.00101.84 O ANISOU 1921 O TRP A 339 13784 19053 5857 -1626 -2899 -10 O ATOM 1922 CB TRP A 339 63.970-103.947 202.142 1.00103.00 C ANISOU 1922 CB TRP A 339 13855 18824 6458 -1303 -2554 64 C ATOM 1923 CG TRP A 339 63.073-104.516 203.195 1.00101.46 C ANISOU 1923 CG TRP A 339 13884 18541 6126 -1126 -2441 40 C ATOM 1924 CD1 TRP A 339 61.924-103.963 203.677 1.00100.43 C ANISOU 1924 CD1 TRP A 339 14056 18165 5938 -1164 -2356 -160 C ATOM 1925 CD2 TRP A 339 63.244-105.758 203.888 1.00104.83 C ANISOU 1925 CD2 TRP A 339 14251 19123 6456 -876 -2392 229 C ATOM 1926 NE1 TRP A 339 61.371-104.780 204.633 1.00105.89 N ANISOU 1926 NE1 TRP A 339 14865 18870 6499 -966 -2253 -101 N ATOM 1927 CE2 TRP A 339 62.162-105.889 204.781 1.00107.85 C ANISOU 1927 CE2 TRP A 339 14905 19350 6723 -796 -2278 139 C ATOM 1928 CE3 TRP A 339 64.208-106.770 203.842 1.00105.93 C ANISOU 1928 CE3 TRP A 339 14139 19514 6594 -702 -2430 467 C ATOM 1929 CZ2 TRP A 339 62.018-106.991 205.622 1.00109.16 C ANISOU 1929 CZ2 TRP A 339 15103 19596 6776 -576 -2206 289 C ATOM 1930 CZ3 TRP A 339 64.063-107.863 204.677 1.00107.67 C ANISOU 1930 CZ3 TRP A 339 14408 19797 6706 -467 -2364 606 C ATOM 1931 CH2 TRP A 339 62.976-107.964 205.555 1.00109.28 C ANISOU 1931 CH2 TRP A 339 14889 19834 6799 -419 -2256 521 C ATOM 1932 N VAL A 340 66.815-104.011 203.460 1.00103.80 N ANISOU 1932 N VAL A 340 13510 19621 6307 -1472 -2905 315 N ATOM 1933 CA VAL A 340 67.744-104.461 204.492 1.00109.42 C ANISOU 1933 CA VAL A 340 14093 20634 6846 -1428 -3008 443 C ATOM 1934 C VAL A 340 68.482-103.279 205.108 1.00119.44 C ANISOU 1934 C VAL A 340 15372 22014 7995 -1770 -3201 334 C ATOM 1935 O VAL A 340 68.796-103.287 206.305 1.00127.73 O ANISOU 1935 O VAL A 340 16480 23199 8853 -1795 -3284 334 O ATOM 1936 CB VAL A 340 68.722-105.499 203.908 1.00111.93 C ANISOU 1936 CB VAL A 340 14059 21237 7233 -1220 -3001 698 C ATOM 1937 CG1 VAL A 340 69.663-106.019 204.988 1.00117.07 C ANISOU 1937 CG1 VAL A 340 14575 22206 7702 -1149 -3099 837 C ATOM 1938 CG2 VAL A 340 67.956-106.647 203.266 1.00101.44 C ANISOU 1938 CG2 VAL A 340 12758 19757 6026 -882 -2813 796 C ATOM 1939 N SER A 341 68.761-102.243 204.312 1.00117.49 N ANISOU 1939 N SER A 341 15083 21704 7856 -2045 -3276 243 N ATOM 1940 CA SER A 341 69.468-101.077 204.833 1.00122.16 C ANISOU 1940 CA SER A 341 15700 22375 8342 -2395 -3462 143 C ATOM 1941 C SER A 341 68.608-100.302 205.825 1.00124.23 C ANISOU 1941 C SER A 341 16355 22379 8470 -2498 -3482 -95 C ATOM 1942 O SER A 341 69.105 -99.839 206.858 1.00125.16 O ANISOU 1942 O SER A 341 16534 22615 8407 -2651 -3618 -144 O ATOM 1943 CB SER A 341 69.903-100.172 203.680 1.00120.48 C ANISOU 1943 CB SER A 341 15371 22120 8287 -2666 -3524 114 C ATOM 1944 OG SER A 341 70.570 -99.017 204.158 1.00126.00 O ANISOU 1944 OG SER A 341 16117 22871 8887 -3027 -3703 22 O ATOM 1945 N VAL A 342 67.317-100.144 205.526 1.00120.21 N ANISOU 1945 N VAL A 342 16111 21524 8039 -2407 -3344 -249 N ATOM 1946 CA VAL A 342 66.428 -99.423 206.431 1.00124.40 C ANISOU 1946 CA VAL A 342 17017 21806 8442 -2461 -3338 -484 C ATOM 1947 C VAL A 342 66.091-100.270 207.652 1.00126.90 C ANISOU 1947 C VAL A 342 17426 22219 8572 -2228 -3278 -438 C ATOM 1948 O VAL A 342 65.852 -99.737 208.743 1.00131.76 O ANISOU 1948 O VAL A 342 18275 22781 9008 -2295 -3333 -584 O ATOM 1949 CB VAL A 342 65.162 -98.986 205.668 1.00124.10 C ANISOU 1949 CB VAL A 342 17210 21388 8552 -2424 -3196 -657 C ATOM 1950 CG1 VAL A 342 64.102 -98.437 206.617 1.00125.33 C ANISOU 1950 CG1 VAL A 342 17748 21300 8573 -2389 -3144 -890 C ATOM 1951 CG2 VAL A 342 65.514 -97.949 204.611 1.00126.80 C ANISOU 1951 CG2 VAL A 342 17514 21609 9056 -2699 -3282 -727 C ATOM 1952 N ARG A 343 66.116-101.595 207.507 1.00123.26 N ANISOU 1952 N ARG A 343 16786 21903 8143 -1953 -3170 -228 N ATOM 1953 CA AARG A 343 65.687-102.486 208.580 0.65121.12 C ANISOU 1953 CA AARG A 343 16618 21689 7714 -1718 -3088 -164 C ATOM 1954 CA BARG A 343 65.685-102.483 208.582 0.35121.14 C ANISOU 1954 CA BARG A 343 16621 21691 7717 -1718 -3088 -165 C ATOM 1955 C ARG A 343 66.743-102.606 209.674 1.00126.07 C ANISOU 1955 C ARG A 343 17137 22623 8142 -1778 -3248 -73 C ATOM 1956 O ARG A 343 66.485-102.291 210.840 1.00131.32 O ANISOU 1956 O ARG A 343 18014 23270 8612 -1811 -3286 -182 O ATOM 1957 CB AARG A 343 65.354-103.863 208.002 0.65116.47 C ANISOU 1957 CB AARG A 343 15895 21119 7239 -1408 -2921 36 C ATOM 1958 CB BARG A 343 65.346-103.859 208.007 0.35116.51 C ANISOU 1958 CB BARG A 343 15903 21122 7243 -1408 -2920 34 C ATOM 1959 CG AARG A 343 65.016-104.917 209.036 0.65115.78 C ANISOU 1959 CG AARG A 343 15887 21102 7004 -1165 -2836 149 C ATOM 1960 CG BARG A 343 64.798-104.845 209.020 0.35115.43 C ANISOU 1960 CG BARG A 343 15888 21005 6964 -1165 -2814 118 C ATOM 1961 CD AARG A 343 64.702-106.241 208.364 0.65112.31 C ANISOU 1961 CD AARG A 343 15334 20643 6695 -872 -2677 347 C ATOM 1962 CD BARG A 343 64.603-106.207 208.384 0.35112.07 C ANISOU 1962 CD BARG A 343 15327 20592 6663 -874 -2668 333 C ATOM 1963 NE AARG A 343 64.289-107.263 209.320 0.65110.89 N ANISOU 1963 NE AARG A 343 15259 20490 6385 -650 -2585 461 N ATOM 1964 NE BARG A 343 65.876-106.812 208.001 0.35111.67 N ANISOU 1964 NE BARG A 343 14949 20822 6657 -809 -2763 545 N ATOM 1965 CZ AARG A 343 63.043-107.415 209.756 0.65109.17 C ANISOU 1965 CZ AARG A 343 15299 20062 6120 -566 -2430 379 C ATOM 1966 CZ BARG A 343 66.420-107.856 208.618 0.35111.69 C ANISOU 1966 CZ BARG A 343 14843 21029 6566 -610 -2774 745 C ATOM 1967 NH1AARG A 343 62.084-106.605 209.327 0.65102.36 N ANISOU 1967 NH1AARG A 343 14614 18951 5328 -666 -2347 174 N ATOM 1968 NH1BARG A 343 65.794-108.420 209.641 0.35112.53 N ANISOU 1968 NH1BARG A 343 15144 21080 6532 -476 -2699 767 N ATOM 1969 NH2AARG A 343 62.754-108.375 210.624 0.65110.66 N ANISOU 1969 NH2AARG A 343 15565 20293 6189 -382 -2353 508 N ATOM 1970 NH2BARG A 343 67.583-108.341 208.205 0.35113.08 N ANISOU 1970 NH2BARG A 343 14714 21465 6788 -537 -2854 925 N ATOM 1971 N ALA A 344 67.944-103.066 209.311 1.00127.61 N ANISOU 1971 N ALA A 344 16994 23115 8376 -1781 -3337 129 N ATOM 1972 CA ALA A 344 68.971-103.347 210.312 1.00135.75 C ANISOU 1972 CA ALA A 344 17885 24472 9222 -1800 -3474 248 C ATOM 1973 C ALA A 344 69.382-102.104 211.092 1.00148.18 C ANISOU 1973 C ALA A 344 19588 26075 10640 -2122 -3655 76 C ATOM 1974 O ALA A 344 69.856-102.216 212.229 1.00152.36 O ANISOU 1974 O ALA A 344 20127 26798 10965 -2136 -3752 108 O ATOM 1975 CB ALA A 344 70.193-103.978 209.643 1.00135.00 C ANISOU 1975 CB ALA A 344 17384 24697 9212 -1744 -3527 486 C ATOM 1976 N THR A 345 69.206-100.916 210.512 1.00153.73 N ANISOU 1976 N THR A 345 20402 26578 11430 -2381 -3706 -107 N ATOM 1977 CA THR A 345 69.669 -99.702 211.178 1.00167.03 C ANISOU 1977 CA THR A 345 22215 28275 12976 -2702 -3889 -266 C ATOM 1978 C THR A 345 68.752 -99.308 212.330 1.00175.37 C ANISOU 1978 C THR A 345 23654 29129 13849 -2665 -3867 -473 C ATOM 1979 O THR A 345 69.229 -98.924 213.405 1.00181.81 O ANISOU 1979 O THR A 345 24543 30079 14458 -2790 -4005 -523 O ATOM 1980 CB THR A 345 69.781 -98.556 210.174 1.00169.68 C ANISOU 1980 CB THR A 345 22567 28436 13467 -2991 -3950 -386 C ATOM 1981 OG1 THR A 345 68.569 -98.464 209.415 1.00166.61 O ANISOU 1981 OG1 THR A 345 22371 27695 13239 -2873 -3786 -507 O ATOM 1982 CG2 THR A 345 70.957 -98.779 209.235 1.00171.45 C ANISOU 1982 CG2 THR A 345 22387 28939 13817 -3092 -4013 -177 C ATOM 1983 N LEU A 346 67.435 -99.401 212.131 1.00176.35 N ANISOU 1983 N LEU A 346 24020 28948 14038 -2489 -3690 -594 N ATOM 1984 CA LEU A 346 66.503 -98.852 213.112 1.00182.04 C ANISOU 1984 CA LEU A 346 25114 29459 14594 -2461 -3656 -820 C ATOM 1985 C LEU A 346 66.548 -99.630 214.424 1.00191.26 C ANISOU 1985 C LEU A 346 26316 30821 15534 -2290 -3650 -733 C ATOM 1986 O LEU A 346 66.594 -99.033 215.506 1.00193.31 O ANISOU 1986 O LEU A 346 26770 31096 15583 -2384 -3749 -870 O ATOM 1987 CB LEU A 346 65.084 -98.818 212.534 1.00175.17 C ANISOU 1987 CB LEU A 346 24459 28247 13851 -2298 -3450 -952 C ATOM 1988 CG LEU A 346 64.330-100.098 212.159 1.00169.76 C ANISOU 1988 CG LEU A 346 23704 27538 13258 -1985 -3231 -798 C ATOM 1989 CD1 LEU A 346 63.451-100.574 213.307 1.00169.30 C ANISOU 1989 CD1 LEU A 346 23870 27442 13012 -1776 -3111 -838 C ATOM 1990 CD2 LEU A 346 63.494 -99.880 210.909 1.00165.23 C ANISOU 1990 CD2 LEU A 346 23176 26689 12914 -1953 -3093 -876 C ATOM 1991 N ALA A 347 66.547-100.957 214.352 1.00194.44 N ANISOU 1991 N ALA A 347 26541 31368 15971 -2039 -3538 -504 N ATOM 1992 CA ALA A 347 66.570-101.785 215.552 1.00201.02 C ANISOU 1992 CA ALA A 347 27404 32374 16599 -1866 -3521 -396 C ATOM 1993 C ALA A 347 66.965-103.205 215.152 1.00204.02 C ANISOU 1993 C ALA A 347 27501 32945 17071 -1636 -3443 -102 C ATOM 1994 O ALA A 347 67.612-103.412 214.119 1.00203.96 O ANISOU 1994 O ALA A 347 27226 33031 17241 -1659 -3468 22 O ATOM 1995 CB ALA A 347 65.211-101.735 216.273 1.00199.48 C ANISOU 1995 CB ALA A 347 27559 31944 16290 -1718 -3366 -555 C ATOM 1996 N ASN A 348 66.573-104.186 215.977 1.00207.06 N ANISOU 1996 N ASN A 348 27955 33385 17334 -1406 -3346 11 N ATOM 1997 CA ASN A 348 66.878-105.592 215.754 1.00206.37 C ANISOU 1997 CA ASN A 348 27651 33450 17311 -1157 -3269 288 C ATOM 1998 C ASN A 348 65.667-106.405 216.224 1.00199.92 C ANISOU 1998 C ASN A 348 27050 32461 16448 -920 -3065 318 C ATOM 1999 O ASN A 348 65.717-107.157 217.197 1.00202.63 O ANISOU 1999 O ASN A 348 27429 32929 16633 -786 -3052 440 O ATOM 2000 CB ASN A 348 68.160-106.007 216.482 1.00217.26 C ANISOU 2000 CB ASN A 348 28814 35192 18545 -1163 -3433 460 C ATOM 2001 CG ASN A 348 68.776-107.266 215.907 1.00220.74 C ANISOU 2001 CG ASN A 348 28964 35808 19101 -931 -3391 739 C ATOM 2002 OD1 ASN A 348 68.530-107.622 214.754 1.00219.98 O ANISOU 2002 OD1 ASN A 348 28771 35594 19218 -830 -3285 795 O ATOM 2003 ND2 ASN A 348 69.590-107.944 216.707 1.00223.96 N ANISOU 2003 ND2 ASN A 348 29237 36497 19362 -834 -3475 912 N ATOM 2004 N THR A 349 64.553-106.248 215.514 1.00174.30 N ANISOU 2004 N THR A 349 23950 28931 13344 -877 -2900 210 N ATOM 2005 CA THR A 349 63.294-106.871 215.902 1.00158.09 C ANISOU 2005 CA THR A 349 22111 26702 11255 -692 -2692 216 C ATOM 2006 C THR A 349 63.281-108.339 215.473 1.00144.61 C ANISOU 2006 C THR A 349 20256 25032 9658 -445 -2575 486 C ATOM 2007 O THR A 349 64.313-108.927 215.135 1.00134.41 O ANISOU 2007 O THR A 349 18713 23934 8423 -382 -2667 671 O ATOM 2008 CB THR A 349 62.118-106.100 215.309 1.00150.15 C ANISOU 2008 CB THR A 349 21304 25393 10351 -744 -2560 -6 C ATOM 2009 OG1 THR A 349 62.223-106.081 213.880 1.00145.16 O ANISOU 2009 OG1 THR A 349 20509 24675 9970 -759 -2535 22 O ATOM 2010 CG2 THR A 349 62.103-104.670 215.830 1.00148.60 C ANISOU 2010 CG2 THR A 349 21298 25136 10028 -958 -2677 -278 C ATOM 2011 N GLY A 350 62.101-108.947 215.484 1.00137.60 N ANISOU 2011 N GLY A 350 19527 23954 8800 -296 -2369 510 N ATOM 2012 CA GLY A 350 61.968-110.350 215.142 1.00136.69 C ANISOU 2012 CA GLY A 350 19326 23830 8780 -63 -2253 758 C ATOM 2013 C GLY A 350 62.330-110.630 213.694 1.00143.23 C ANISOU 2013 C GLY A 350 19947 24617 9857 -7 -2244 841 C ATOM 2014 O GLY A 350 62.484-109.737 212.860 1.00146.54 O ANISOU 2014 O GLY A 350 20300 24984 10395 -153 -2296 701 O ATOM 2015 N CYS A 351 62.463-111.925 213.396 1.00153.44 N ANISOU 2015 N CYS A 351 21148 25925 11226 219 -2177 1079 N ATOM 2016 CA CYS A 351 62.895-112.340 212.067 1.00153.59 C ANISOU 2016 CA CYS A 351 20966 25924 11465 317 -2170 1182 C ATOM 2017 C CYS A 351 61.740-112.395 211.072 1.00148.12 C ANISOU 2017 C CYS A 351 20376 24948 10956 353 -1988 1119 C ATOM 2018 O CYS A 351 61.957-112.189 209.871 1.00145.08 O ANISOU 2018 O CYS A 351 19854 24516 10755 343 -1993 1101 O ATOM 2019 CB CYS A 351 63.594-113.701 212.147 1.00160.03 C ANISOU 2019 CB CYS A 351 21655 26866 12283 568 -2186 1457 C ATOM 2020 SG CYS A 351 64.183-114.353 210.560 1.00165.87 S ANISOU 2020 SG CYS A 351 22155 27592 13277 747 -2171 1599 S ATOM 2021 N TRP A 352 60.516-112.649 211.539 1.00141.27 N ANISOU 2021 N TRP A 352 19736 23902 10038 388 -1825 1087 N ATOM 2022 CA TRP A 352 59.384-112.882 210.649 1.00132.07 C ANISOU 2022 CA TRP A 352 18658 22482 9039 445 -1637 1061 C ATOM 2023 C TRP A 352 58.257-111.868 210.812 1.00125.20 C ANISOU 2023 C TRP A 352 17973 21459 8139 292 -1537 816 C ATOM 2024 O TRP A 352 57.187-112.052 210.216 1.00124.97 O ANISOU 2024 O TRP A 352 18028 21230 8226 335 -1364 790 O ATOM 2025 CB TRP A 352 58.829-114.295 210.857 1.00132.36 C ANISOU 2025 CB TRP A 352 18786 22423 9080 650 -1499 1279 C ATOM 2026 CG TRP A 352 59.663-115.379 210.246 1.00128.78 C ANISOU 2026 CG TRP A 352 18183 22017 8732 852 -1547 1508 C ATOM 2027 CD1 TRP A 352 59.821-115.637 208.916 1.00122.63 C ANISOU 2027 CD1 TRP A 352 17286 21146 8162 942 -1522 1552 C ATOM 2028 CD2 TRP A 352 60.440-116.362 210.941 1.00127.07 C ANISOU 2028 CD2 TRP A 352 17927 21944 8410 1010 -1623 1721 C ATOM 2029 NE1 TRP A 352 60.654-116.715 208.739 1.00122.15 N ANISOU 2029 NE1 TRP A 352 17120 21159 8132 1157 -1575 1772 N ATOM 2030 CE2 TRP A 352 61.048-117.179 209.966 1.00125.94 C ANISOU 2030 CE2 TRP A 352 17647 21782 8424 1205 -1638 1880 C ATOM 2031 CE3 TRP A 352 60.685-116.629 212.292 1.00125.23 C ANISOU 2031 CE3 TRP A 352 17767 21854 7962 1015 -1680 1789 C ATOM 2032 CZ2 TRP A 352 61.884-118.244 210.299 1.00127.48 C ANISOU 2032 CZ2 TRP A 352 17780 22089 8569 1415 -1706 2100 C ATOM 2033 CZ3 TRP A 352 61.516-117.688 212.621 1.00125.65 C ANISOU 2033 CZ3 TRP A 352 17752 22024 7966 1208 -1752 2016 C ATOM 2034 CH2 TRP A 352 62.104-118.482 211.628 1.00126.94 C ANISOU 2034 CH2 TRP A 352 17783 22159 8291 1411 -1764 2166 C ATOM 2035 N ASP A 353 58.454-110.810 211.594 1.00122.51 N ANISOU 2035 N ASP A 353 17703 21201 7645 126 -1638 636 N ATOM 2036 CA ASP A 353 57.398-109.820 211.804 1.00118.97 C ANISOU 2036 CA ASP A 353 17450 20599 7154 11 -1544 391 C ATOM 2037 C ASP A 353 57.572-108.637 210.850 1.00122.04 C ANISOU 2037 C ASP A 353 17793 20905 7671 -146 -1619 191 C ATOM 2038 O ASP A 353 57.665-107.477 211.247 1.00123.31 O ANISOU 2038 O ASP A 353 18052 21060 7739 -306 -1711 -19 O ATOM 2039 CB ASP A 353 57.377-109.376 213.261 1.00118.11 C ANISOU 2039 CB ASP A 353 17497 20589 6789 -55 -1596 300 C ATOM 2040 CG ASP A 353 58.764-109.239 213.847 1.00123.46 C ANISOU 2040 CG ASP A 353 18057 21506 7345 -122 -1823 355 C ATOM 2041 OD1 ASP A 353 59.717-109.020 213.075 1.00125.68 O ANISOU 2041 OD1 ASP A 353 18146 21867 7741 -181 -1958 382 O ATOM 2042 OD2 ASP A 353 58.903-109.372 215.083 1.00127.38 O ANISOU 2042 OD2 ASP A 353 18644 22127 7630 -115 -1865 381 O ATOM 2043 N LEU A 354 57.609-108.970 209.558 1.00124.27 N ANISOU 2043 N LEU A 354 17937 21110 8171 -95 -1577 262 N ATOM 2044 CA LEU A 354 57.753-107.950 208.527 1.00128.05 C ANISOU 2044 CA LEU A 354 18360 21501 8792 -242 -1638 98 C ATOM 2045 C LEU A 354 56.499-107.094 208.414 1.00133.78 C ANISOU 2045 C LEU A 354 19292 22003 9536 -305 -1507 -138 C ATOM 2046 O LEU A 354 56.583-105.910 208.064 1.00133.85 O ANISOU 2046 O LEU A 354 19348 21931 9579 -469 -1588 -342 O ATOM 2047 CB LEU A 354 58.059-108.608 207.179 1.00122.61 C ANISOU 2047 CB LEU A 354 17473 20791 8323 -148 -1613 246 C ATOM 2048 CG LEU A 354 58.541-110.061 207.135 1.00121.27 C ANISOU 2048 CG LEU A 354 17173 20725 8179 70 -1593 530 C ATOM 2049 CD1 LEU A 354 58.486-110.564 205.699 1.00114.83 C ANISOU 2049 CD1 LEU A 354 16230 19811 7591 176 -1525 620 C ATOM 2050 CD2 LEU A 354 59.949-110.209 207.699 1.00123.31 C ANISOU 2050 CD2 LEU A 354 17270 21250 8332 58 -1787 644 C ATOM 2051 N SER A 355 55.332-107.672 208.705 1.00139.32 N ANISOU 2051 N SER A 355 20117 22599 10217 -175 -1303 -111 N ATOM 2052 CA SER A 355 54.071-106.984 208.477 1.00140.61 C ANISOU 2052 CA SER A 355 20444 22561 10421 -194 -1148 -313 C ATOM 2053 C SER A 355 53.774-105.940 209.541 1.00141.11 C ANISOU 2053 C SER A 355 20717 22608 10292 -280 -1181 -535 C ATOM 2054 O SER A 355 52.819-105.175 209.379 1.00142.54 O ANISOU 2054 O SER A 355 21044 22620 10495 -291 -1075 -735 O ATOM 2055 CB SER A 355 52.926-107.997 208.432 1.00145.14 C ANISOU 2055 CB SER A 355 21053 23052 11040 -32 -913 -189 C ATOM 2056 OG SER A 355 51.724-107.396 207.981 1.00146.66 O ANISOU 2056 OG SER A 355 21349 23063 11311 -35 -754 -366 O ATOM 2057 N SER A 356 54.555-105.893 210.623 1.00136.54 N ANISOU 2057 N SER A 356 20162 22196 9521 -323 -1323 -506 N ATOM 2058 CA SER A 356 54.178-105.066 211.762 1.00134.35 C ANISOU 2058 CA SER A 356 20109 21904 9033 -365 -1335 -698 C ATOM 2059 C SER A 356 54.469-103.590 211.503 1.00132.64 C ANISOU 2059 C SER A 356 19991 21583 8823 -524 -1477 -959 C ATOM 2060 O SER A 356 53.696-102.718 211.920 1.00134.31 O ANISOU 2060 O SER A 356 20423 21661 8948 -516 -1420 -1181 O ATOM 2061 CB SER A 356 54.907-105.559 213.008 1.00134.20 C ANISOU 2061 CB SER A 356 20086 22103 8802 -354 -1440 -572 C ATOM 2062 OG SER A 356 54.280-105.068 214.174 1.00135.05 O ANISOU 2062 OG SER A 356 20421 22196 8694 -341 -1389 -717 O ATOM 2063 N GLY A 357 55.572-103.284 210.818 1.00129.84 N ANISOU 2063 N GLY A 357 19478 21284 8573 -664 -1663 -933 N ATOM 2064 CA GLY A 357 55.981-101.920 210.580 1.00128.69 C ANISOU 2064 CA GLY A 357 19412 21045 8441 -849 -1823 -1153 C ATOM 2065 C GLY A 357 55.791-101.497 209.133 1.00129.16 C ANISOU 2065 C GLY A 357 19401 20925 8747 -916 -1797 -1215 C ATOM 2066 O GLY A 357 55.483-102.292 208.245 1.00125.13 O ANISOU 2066 O GLY A 357 18751 20391 8400 -824 -1674 -1076 O ATOM 2067 N ASN A 358 55.986-100.198 208.914 1.00133.24 N ANISOU 2067 N ASN A 358 20029 21307 9287 -1084 -1920 -1430 N ATOM 2068 CA ASN A 358 55.898 -99.615 207.584 1.00134.45 C ANISOU 2068 CA ASN A 358 20141 21275 9668 -1186 -1925 -1506 C ATOM 2069 C ASN A 358 57.043-100.034 206.675 1.00133.08 C ANISOU 2069 C ASN A 358 19681 21245 9640 -1305 -2049 -1312 C ATOM 2070 O ASN A 358 57.056 -99.626 205.508 1.00129.12 O ANISOU 2070 O ASN A 358 19120 20608 9331 -1399 -2058 -1347 O ATOM 2071 CB ASN A 358 55.852 -98.087 207.679 1.00142.32 C ANISOU 2071 CB ASN A 358 21352 22077 10646 -1342 -2036 -1779 C ATOM 2072 CG ASN A 358 54.480 -97.566 208.069 1.00144.85 C ANISOU 2072 CG ASN A 358 21934 22194 10910 -1180 -1867 -1997 C ATOM 2073 OD1 ASN A 358 53.603 -98.330 208.473 1.00144.93 O ANISOU 2073 OD1 ASN A 358 21971 22242 10853 -968 -1675 -1943 O ATOM 2074 ND2 ASN A 358 54.289 -96.257 207.946 1.00146.99 N ANISOU 2074 ND2 ASN A 358 22387 22252 11208 -1278 -1933 -2239 N ATOM 2075 N ASN A 359 57.997-100.825 207.172 1.00135.39 N ANISOU 2075 N ASN A 359 19789 21810 9843 -1290 -2141 -1108 N ATOM 2076 CA ASN A 359 59.111-101.277 206.349 1.00130.61 C ANISOU 2076 CA ASN A 359 18884 21377 9363 -1361 -2249 -913 C ATOM 2077 C ASN A 359 58.667-102.202 205.222 1.00114.92 C ANISOU 2077 C ASN A 359 16751 19347 7568 -1203 -2092 -769 C ATOM 2078 O ASN A 359 59.401-102.357 204.239 1.00108.79 O ANISOU 2078 O ASN A 359 15750 18648 6937 -1260 -2160 -655 O ATOM 2079 CB ASN A 359 60.151-101.983 207.221 1.00138.65 C ANISOU 2079 CB ASN A 359 19745 22703 10232 -1332 -2363 -725 C ATOM 2080 CG ASN A 359 59.598-103.219 207.897 1.00145.44 C ANISOU 2080 CG ASN A 359 20627 23635 11000 -1076 -2210 -580 C ATOM 2081 OD1 ASN A 359 58.387-103.353 208.077 1.00146.92 O ANISOU 2081 OD1 ASN A 359 20997 23652 11172 -952 -2031 -659 O ATOM 2082 ND2 ASN A 359 60.483-104.132 208.276 1.00148.48 N ANISOU 2082 ND2 ASN A 359 20820 24272 11324 -994 -2277 -358 N ATOM 2083 N LYS A 360 57.490-102.816 205.341 1.00106.11 N ANISOU 2083 N LYS A 360 15751 18117 6451 -1007 -1882 -768 N ATOM 2084 CA LYS A 360 56.995-103.732 204.323 1.00102.70 C ANISOU 2084 CA LYS A 360 15198 17634 6191 -851 -1725 -633 C ATOM 2085 C LYS A 360 56.465-103.023 203.084 1.00106.21 C ANISOU 2085 C LYS A 360 15674 17855 6828 -939 -1675 -772 C ATOM 2086 O LYS A 360 56.268-103.676 202.054 1.00105.67 O ANISOU 2086 O LYS A 360 15471 17759 6918 -845 -1583 -660 O ATOM 2087 CB LYS A 360 55.888-104.612 204.903 1.00107.05 C ANISOU 2087 CB LYS A 360 15862 18139 6674 -636 -1514 -578 C ATOM 2088 CG LYS A 360 54.577-103.875 205.139 1.00109.43 C ANISOU 2088 CG LYS A 360 16411 18221 6946 -633 -1372 -808 C ATOM 2089 CD LYS A 360 53.476-104.820 205.588 1.00112.66 C ANISOU 2089 CD LYS A 360 16886 18608 7311 -430 -1148 -722 C ATOM 2090 CE LYS A 360 52.156-104.088 205.755 1.00114.64 C ANISOU 2090 CE LYS A 360 17350 18666 7544 -405 -992 -943 C ATOM 2091 NZ LYS A 360 51.074-105.003 206.204 1.00114.71 N ANISOU 2091 NZ LYS A 360 17397 18677 7512 -226 -769 -843 N ATOM 2092 N TRP A 361 56.217-101.716 203.154 1.00109.02 N ANISOU 2092 N TRP A 361 16215 18035 7172 -1105 -1735 -1011 N ATOM 2093 CA TRP A 361 55.633-101.019 202.017 1.00104.31 C ANISOU 2093 CA TRP A 361 15680 17192 6760 -1179 -1680 -1147 C ATOM 2094 C TRP A 361 56.658-100.645 200.957 1.00100.58 C ANISOU 2094 C TRP A 361 15020 16758 6437 -1362 -1837 -1090 C ATOM 2095 O TRP A 361 56.277-100.438 199.802 1.00102.11 O ANISOU 2095 O TRP A 361 15195 16792 6812 -1390 -1778 -1125 O ATOM 2096 CB TRP A 361 54.887 -99.766 202.482 1.00108.80 C ANISOU 2096 CB TRP A 361 16547 17519 7272 -1246 -1669 -1426 C ATOM 2097 CG TRP A 361 53.514-100.070 202.997 1.00113.72 C ANISOU 2097 CG TRP A 361 17338 18040 7830 -1039 -1445 -1502 C ATOM 2098 CD1 TRP A 361 53.103-100.063 204.298 1.00119.31 C ANISOU 2098 CD1 TRP A 361 18198 18801 8331 -940 -1400 -1567 C ATOM 2099 CD2 TRP A 361 52.372-100.448 202.218 1.00113.68 C ANISOU 2099 CD2 TRP A 361 17340 17874 7980 -899 -1227 -1507 C ATOM 2100 NE1 TRP A 361 51.774-100.404 204.376 1.00120.80 N ANISOU 2100 NE1 TRP A 361 18483 18893 8523 -753 -1166 -1608 N ATOM 2101 CE2 TRP A 361 51.302-100.646 203.113 1.00115.14 C ANISOU 2101 CE2 TRP A 361 17677 18048 8023 -732 -1056 -1573 C ATOM 2102 CE3 TRP A 361 52.151-100.635 200.850 1.00113.92 C ANISOU 2102 CE3 TRP A 361 17232 17721 8330 -860 -1150 -1442 C ATOM 2103 CZ2 TRP A 361 50.030-101.021 202.684 1.00114.46 C ANISOU 2103 CZ2 TRP A 361 17593 17792 8105 -543 -817 -1569 C ATOM 2104 CZ3 TRP A 361 50.888-101.006 200.426 1.00112.34 C ANISOU 2104 CZ3 TRP A 361 17051 17335 8299 -672 -918 -1446 C ATOM 2105 CH2 TRP A 361 49.844-101.196 201.340 1.00114.69 C ANISOU 2105 CH2 TRP A 361 17486 17641 8450 -521 -756 -1505 C ATOM 2106 N ILE A 362 57.944-100.555 201.310 1.00 97.54 N ANISOU 2106 N ILE A 362 14487 16593 5982 -1488 -2030 -996 N ATOM 2107 CA ILE A 362 58.956-100.254 200.299 1.00 99.04 C ANISOU 2107 CA ILE A 362 14461 16859 6310 -1659 -2168 -915 C ATOM 2108 C ILE A 362 59.319-101.471 199.464 1.00103.39 C ANISOU 2108 C ILE A 362 14728 17586 6970 -1494 -2106 -674 C ATOM 2109 O ILE A 362 60.064-101.339 198.484 1.00102.58 O ANISOU 2109 O ILE A 362 14422 17556 6997 -1595 -2187 -592 O ATOM 2110 CB ILE A 362 60.222 -99.656 200.942 1.00 99.40 C ANISOU 2110 CB ILE A 362 14431 17090 6245 -1870 -2393 -900 C ATOM 2111 CG1 ILE A 362 61.096-100.752 201.552 1.00100.37 C ANISOU 2111 CG1 ILE A 362 14325 17554 6258 -1741 -2436 -670 C ATOM 2112 CG2 ILE A 362 59.848 -98.611 201.987 1.00101.42 C ANISOU 2112 CG2 ILE A 362 14990 17191 6355 -1981 -2450 -1129 C ATOM 2113 CD1 ILE A 362 62.415-100.927 200.833 1.00 97.90 C ANISOU 2113 CD1 ILE A 362 13682 17487 6030 -1835 -2564 -490 C ATOM 2114 N ILE A 363 58.827-102.654 199.830 1.00102.76 N ANISOU 2114 N ILE A 363 14632 17573 6840 -1235 -1963 -552 N ATOM 2115 CA ILE A 363 58.953-103.835 198.994 1.00 98.95 C ANISOU 2115 CA ILE A 363 13937 17189 6471 -1032 -1875 -342 C ATOM 2116 C ILE A 363 57.629-104.216 198.335 1.00 95.77 C ANISOU 2116 C ILE A 363 13642 16457 6290 -856 -1638 -382 C ATOM 2117 O ILE A 363 57.632-104.667 197.183 1.00 96.26 O ANISOU 2117 O ILE A 363 13565 16426 6585 -761 -1568 -290 O ATOM 2118 CB ILE A 363 59.531-105.023 199.797 1.00101.12 C ANISOU 2118 CB ILE A 363 14092 17702 6627 -829 -1882 -126 C ATOM 2119 CG1 ILE A 363 59.345-106.346 199.048 1.00 98.97 C ANISOU 2119 CG1 ILE A 363 13691 17448 6465 -555 -1750 73 C ATOM 2120 CG2 ILE A 363 58.912-105.095 201.181 1.00105.09 C ANISOU 2120 CG2 ILE A 363 14812 18173 6942 -778 -1828 -194 C ATOM 2121 CD1 ILE A 363 59.816-107.555 199.818 1.00103.44 C ANISOU 2121 CD1 ILE A 363 14186 18189 6927 -332 -1744 285 C ATOM 2122 N GLN A 364 56.495-104.012 199.012 1.00 94.64 N ANISOU 2122 N GLN A 364 13737 16126 6095 -809 -1511 -521 N ATOM 2123 CA GLN A 364 55.206-104.314 198.397 1.00 92.65 C ANISOU 2123 CA GLN A 364 13571 15566 6067 -657 -1285 -558 C ATOM 2124 C GLN A 364 54.863-103.335 197.281 1.00 95.03 C ANISOU 2124 C GLN A 364 13905 15612 6592 -780 -1276 -708 C ATOM 2125 O GLN A 364 54.230-103.727 196.294 1.00 96.04 O ANISOU 2125 O GLN A 364 13985 15543 6963 -666 -1134 -671 O ATOM 2126 CB GLN A 364 54.096-104.310 199.449 1.00 91.82 C ANISOU 2126 CB GLN A 364 13688 15378 5822 -577 -1151 -660 C ATOM 2127 CG GLN A 364 54.153-105.467 200.431 1.00 96.73 C ANISOU 2127 CG GLN A 364 14293 16198 6263 -417 -1107 -486 C ATOM 2128 CD GLN A 364 52.977-105.474 201.390 1.00104.03 C ANISOU 2128 CD GLN A 364 15421 17049 7056 -341 -954 -577 C ATOM 2129 OE1 GLN A 364 53.010-106.140 202.425 1.00110.49 O ANISOU 2129 OE1 GLN A 364 16274 18042 7665 -259 -940 -476 O ATOM 2130 NE2 GLN A 364 51.930-104.733 201.049 1.00103.62 N ANISOU 2130 NE2 GLN A 364 15501 16753 7118 -357 -838 -762 N ATOM 2131 N VAL A 365 55.258-102.066 197.416 1.00 91.60 N ANISOU 2131 N VAL A 365 13564 15167 6071 -1016 -1430 -876 N ATOM 2132 CA VAL A 365 54.948-101.078 196.379 1.00 87.53 C ANISOU 2132 CA VAL A 365 13108 14394 5756 -1141 -1433 -1016 C ATOM 2133 C VAL A 365 55.623-101.408 195.050 1.00 81.08 C ANISOU 2133 C VAL A 365 12043 13609 5155 -1157 -1467 -871 C ATOM 2134 O VAL A 365 54.943-101.362 194.011 1.00 77.82 O ANISOU 2134 O VAL A 365 11628 12956 4985 -1094 -1347 -897 O ATOM 2135 CB VAL A 365 55.274 -99.662 196.881 1.00 88.46 C ANISOU 2135 CB VAL A 365 13420 14481 5709 -1405 -1609 -1220 C ATOM 2136 CG1 VAL A 365 55.452 -98.708 195.716 1.00 90.60 C ANISOU 2136 CG1 VAL A 365 13695 14564 6167 -1586 -1683 -1299 C ATOM 2137 CG2 VAL A 365 54.171 -99.165 197.803 1.00 87.15 C ANISOU 2137 CG2 VAL A 365 13550 14148 5414 -1335 -1509 -1420 C ATOM 2138 N PRO A 366 56.923-101.734 194.996 1.00 80.22 N ANISOU 2138 N PRO A 366 11713 13802 4963 -1230 -1621 -715 N ATOM 2139 CA PRO A 366 57.492-102.158 193.704 1.00 76.59 C ANISOU 2139 CA PRO A 366 11007 13389 4705 -1197 -1624 -568 C ATOM 2140 C PRO A 366 56.824-103.400 193.140 1.00 78.56 C ANISOU 2140 C PRO A 366 11190 13527 5134 -903 -1422 -442 C ATOM 2141 O PRO A 366 56.644-103.502 191.919 1.00 80.58 O ANISOU 2141 O PRO A 366 11358 13640 5619 -860 -1353 -413 O ATOM 2142 CB PRO A 366 58.970-102.404 194.036 1.00 76.39 C ANISOU 2142 CB PRO A 366 10756 13774 4496 -1283 -1817 -414 C ATOM 2143 CG PRO A 366 59.233-101.563 195.228 1.00 77.92 C ANISOU 2143 CG PRO A 366 11107 14069 4429 -1496 -1968 -541 C ATOM 2144 CD PRO A 366 57.970-101.613 196.028 1.00 77.49 C ANISOU 2144 CD PRO A 366 11324 13784 4335 -1364 -1813 -675 C ATOM 2145 N ILE A 367 56.448-104.349 193.999 1.00 76.76 N ANISOU 2145 N ILE A 367 11013 13354 4797 -710 -1330 -363 N ATOM 2146 CA ILE A 367 55.719-105.524 193.531 1.00 74.14 C ANISOU 2146 CA ILE A 367 10665 12882 4622 -457 -1141 -249 C ATOM 2147 C ILE A 367 54.344-105.124 193.010 1.00 76.12 C ANISOU 2147 C ILE A 367 11072 12787 5063 -445 -977 -394 C ATOM 2148 O ILE A 367 53.873-105.650 191.995 1.00 66.49 O ANISOU 2148 O ILE A 367 9799 11404 4060 -333 -860 -338 O ATOM 2149 CB ILE A 367 55.625-106.573 194.655 1.00 74.07 C ANISOU 2149 CB ILE A 367 10704 13009 4432 -285 -1093 -127 C ATOM 2150 CG1 ILE A 367 57.016-107.110 194.997 1.00 75.02 C ANISOU 2150 CG1 ILE A 367 10637 13482 4384 -248 -1250 49 C ATOM 2151 CG2 ILE A 367 54.692-107.708 194.259 1.00 68.63 C ANISOU 2151 CG2 ILE A 367 10059 12126 3893 -64 -895 -27 C ATOM 2152 CD1 ILE A 367 57.017-108.146 196.100 1.00 78.06 C ANISOU 2152 CD1 ILE A 367 11072 14009 4577 -74 -1219 187 C ATOM 2153 N LEU A 368 53.682-104.184 193.689 1.00 78.83 N ANISOU 2153 N LEU A 368 11613 13023 5317 -551 -967 -585 N ATOM 2154 CA LEU A 368 52.406-103.679 193.195 1.00 77.28 C ANISOU 2154 CA LEU A 368 11553 12525 5285 -531 -822 -730 C ATOM 2155 C LEU A 368 52.569-102.952 191.868 1.00 80.53 C ANISOU 2155 C LEU A 368 11900 12786 5911 -642 -864 -788 C ATOM 2156 O LEU A 368 51.678-103.015 191.013 1.00 72.55 O ANISOU 2156 O LEU A 368 10904 11553 5108 -565 -729 -815 O ATOM 2157 CB LEU A 368 51.766-102.752 194.227 1.00 78.27 C ANISOU 2157 CB LEU A 368 11909 12590 5240 -599 -817 -930 C ATOM 2158 CG LEU A 368 51.016-103.409 195.385 1.00 83.72 C ANISOU 2158 CG LEU A 368 12703 13341 5767 -455 -691 -908 C ATOM 2159 CD1 LEU A 368 50.472-102.348 196.327 1.00 86.15 C ANISOU 2159 CD1 LEU A 368 13239 13599 5893 -520 -699 -1128 C ATOM 2160 CD2 LEU A 368 49.895-104.290 194.857 1.00 82.48 C ANISOU 2160 CD2 LEU A 368 12520 13032 5787 -280 -477 -828 C ATOM 2161 N ALA A 369 53.694-102.259 191.678 1.00 84.78 N ANISOU 2161 N ALA A 369 12361 13455 6395 -834 -1054 -797 N ATOM 2162 CA ALA A 369 53.918-101.536 190.431 1.00 82.19 C ANISOU 2162 CA ALA A 369 11972 13003 6255 -963 -1106 -837 C ATOM 2163 C ALA A 369 53.968-102.487 189.242 1.00 76.75 C ANISOU 2163 C ALA A 369 11086 12296 5778 -816 -1015 -678 C ATOM 2164 O ALA A 369 53.502-102.148 188.148 1.00 77.94 O ANISOU 2164 O ALA A 369 11233 12245 6136 -828 -956 -723 O ATOM 2165 CB ALA A 369 55.206-100.719 190.522 1.00 86.90 C ANISOU 2165 CB ALA A 369 12502 13793 6723 -1221 -1337 -844 C ATOM 2166 N SER A 370 54.527-103.684 189.437 1.00 72.88 N ANISOU 2166 N SER A 370 10449 12012 5231 -665 -1006 -494 N ATOM 2167 CA SER A 370 54.555-104.665 188.358 1.00 70.31 C ANISOU 2167 CA SER A 370 9973 11656 5087 -497 -917 -349 C ATOM 2168 C SER A 370 53.154-105.169 188.038 1.00 66.21 C ANISOU 2168 C SER A 370 9572 10860 4726 -347 -715 -381 C ATOM 2169 O SER A 370 52.834-105.435 186.874 1.00 61.68 O ANISOU 2169 O SER A 370 8937 10142 4356 -286 -638 -350 O ATOM 2170 CB SER A 370 55.472-105.831 188.727 1.00 71.64 C ANISOU 2170 CB SER A 370 9992 12096 5132 -343 -959 -149 C ATOM 2171 OG SER A 370 54.904-106.615 189.761 1.00 73.66 O ANISOU 2171 OG SER A 370 10371 12346 5272 -200 -872 -110 O ATOM 2172 N ILE A 371 52.306-105.308 189.059 1.00 67.00 N ANISOU 2172 N ILE A 371 9834 10902 4722 -294 -628 -437 N ATOM 2173 CA ILE A 371 50.930-105.736 188.831 1.00 61.98 C ANISOU 2173 CA ILE A 371 9297 10038 4214 -178 -438 -462 C ATOM 2174 C ILE A 371 50.158-104.666 188.068 1.00 64.57 C ANISOU 2174 C ILE A 371 9692 10138 4703 -269 -396 -628 C ATOM 2175 O ILE A 371 49.351-104.975 187.183 1.00 62.07 O ANISOU 2175 O ILE A 371 9363 9644 4576 -196 -275 -617 O ATOM 2176 CB ILE A 371 50.254-106.085 190.169 1.00 62.17 C ANISOU 2176 CB ILE A 371 9461 10102 4060 -113 -359 -474 C ATOM 2177 CG1 ILE A 371 51.016-107.213 190.868 1.00 69.67 C ANISOU 2177 CG1 ILE A 371 10353 11266 4855 -8 -402 -289 C ATOM 2178 CG2 ILE A 371 48.800-106.474 189.953 1.00 58.51 C ANISOU 2178 CG2 ILE A 371 9080 9439 3713 -19 -164 -493 C ATOM 2179 CD1 ILE A 371 50.443-107.594 192.216 1.00 70.54 C ANISOU 2179 CD1 ILE A 371 10595 11440 4768 46 -334 -280 C ATOM 2180 N VAL A 372 50.391-103.393 188.397 1.00 66.39 N ANISOU 2180 N VAL A 372 10009 10363 4853 -430 -503 -781 N ATOM 2181 CA VAL A 372 49.755-102.309 187.655 1.00 67.63 C ANISOU 2181 CA VAL A 372 10249 10294 5152 -510 -483 -935 C ATOM 2182 C VAL A 372 50.276-102.268 186.225 1.00 67.92 C ANISOU 2182 C VAL A 372 10135 10286 5387 -560 -527 -869 C ATOM 2183 O VAL A 372 49.515-102.035 185.277 1.00 70.91 O ANISOU 2183 O VAL A 372 10526 10463 5954 -532 -441 -915 O ATOM 2184 CB VAL A 372 49.972-100.967 188.377 1.00 69.86 C ANISOU 2184 CB VAL A 372 10699 10564 5280 -675 -607 -1112 C ATOM 2185 CG1 VAL A 372 49.352 -99.827 187.582 1.00 63.94 C ANISOU 2185 CG1 VAL A 372 10061 9559 4673 -743 -597 -1265 C ATOM 2186 CG2 VAL A 372 49.392-101.019 189.784 1.00 67.67 C ANISOU 2186 CG2 VAL A 372 10579 10338 4796 -604 -549 -1186 C ATOM 2187 N LEU A 373 51.579-102.498 186.044 1.00 66.53 N ANISOU 2187 N LEU A 373 9801 10316 5159 -628 -661 -755 N ATOM 2188 CA LEU A 373 52.138-102.570 184.698 1.00 62.37 C ANISOU 2188 CA LEU A 373 9106 9791 4798 -656 -695 -673 C ATOM 2189 C LEU A 373 51.529-103.723 183.912 1.00 61.12 C ANISOU 2189 C LEU A 373 8879 9538 4807 -454 -540 -568 C ATOM 2190 O LEU A 373 51.223-103.580 182.722 1.00 60.16 O ANISOU 2190 O LEU A 373 8710 9274 4872 -454 -496 -575 O ATOM 2191 CB LEU A 373 53.659-102.711 184.772 1.00 61.24 C ANISOU 2191 CB LEU A 373 8783 9949 4535 -739 -858 -552 C ATOM 2192 CG LEU A 373 54.403-102.970 183.461 1.00 58.71 C ANISOU 2192 CG LEU A 373 8249 9712 4346 -736 -890 -435 C ATOM 2193 CD1 LEU A 373 54.175-101.839 182.465 1.00 57.93 C ANISOU 2193 CD1 LEU A 373 8185 9432 4396 -908 -920 -536 C ATOM 2194 CD2 LEU A 373 55.889-103.168 183.726 1.00 58.81 C ANISOU 2194 CD2 LEU A 373 8065 10083 4198 -795 -1045 -305 C ATOM 2195 N ASN A 374 51.333-104.872 184.564 1.00 61.15 N ANISOU 2195 N ASN A 374 8890 9609 4735 -291 -462 -469 N ATOM 2196 CA ASN A 374 50.734-106.016 183.885 1.00 57.75 C ANISOU 2196 CA ASN A 374 8430 9068 4442 -117 -326 -368 C ATOM 2197 C ASN A 374 49.289-105.737 183.494 1.00 58.37 C ANISOU 2197 C ASN A 374 8620 8890 4666 -108 -185 -472 C ATOM 2198 O ASN A 374 48.844-106.148 182.416 1.00 63.28 O ANISOU 2198 O ASN A 374 9199 9380 5465 -48 -108 -436 O ATOM 2199 CB ASN A 374 50.823-107.258 184.769 1.00 59.33 C ANISOU 2199 CB ASN A 374 8654 9379 4509 35 -285 -237 C ATOM 2200 CG ASN A 374 52.210-107.861 184.780 1.00 66.20 C ANISOU 2200 CG ASN A 374 9379 10494 5282 101 -398 -90 C ATOM 2201 OD1 ASN A 374 52.980-107.679 183.839 1.00 66.46 O ANISOU 2201 OD1 ASN A 374 9266 10597 5390 77 -468 -54 O ATOM 2202 ND2 ASN A 374 52.536-108.587 185.843 1.00 73.66 N ANISOU 2202 ND2 ASN A 374 10354 11588 6048 193 -416 4 N ATOM 2203 N PHE A 375 48.540-105.042 184.353 1.00 57.78 N ANISOU 2203 N PHE A 375 8686 8758 4509 -156 -151 -602 N ATOM 2204 CA PHE A 375 47.173-104.677 183.999 1.00 60.45 C ANISOU 2204 CA PHE A 375 9110 8889 4969 -134 -21 -703 C ATOM 2205 C PHE A 375 47.143-103.726 182.811 1.00 65.69 C ANISOU 2205 C PHE A 375 9745 9412 5802 -221 -59 -788 C ATOM 2206 O PHE A 375 46.197-103.753 182.017 1.00 58.50 O ANISOU 2206 O PHE A 375 8836 8341 5051 -174 45 -811 O ATOM 2207 CB PHE A 375 46.461-104.056 185.202 1.00 61.43 C ANISOU 2207 CB PHE A 375 9387 9011 4941 -144 18 -832 C ATOM 2208 CG PHE A 375 46.086-105.053 186.265 1.00 72.62 C ANISOU 2208 CG PHE A 375 10843 10532 6217 -46 104 -745 C ATOM 2209 CD1 PHE A 375 45.974-106.401 185.962 1.00 70.81 C ANISOU 2209 CD1 PHE A 375 10549 10309 6046 51 178 -578 C ATOM 2210 CD2 PHE A 375 45.842-104.642 187.567 1.00 77.02 C ANISOU 2210 CD2 PHE A 375 11520 11172 6572 -53 108 -830 C ATOM 2211 CE1 PHE A 375 45.629-107.320 186.936 1.00 71.73 C ANISOU 2211 CE1 PHE A 375 10719 10508 6027 124 251 -485 C ATOM 2212 CE2 PHE A 375 45.495-105.557 188.546 1.00 76.20 C ANISOU 2212 CE2 PHE A 375 11449 11174 6328 28 189 -739 C ATOM 2213 CZ PHE A 375 45.388-106.897 188.229 1.00 75.17 C ANISOU 2213 CZ PHE A 375 11253 11044 6262 110 259 -560 C ATOM 2214 N ILE A 376 48.171-102.889 182.665 1.00 70.27 N ANISOU 2214 N ILE A 376 10295 10059 6343 -359 -213 -824 N ATOM 2215 CA ILE A 376 48.252-102.009 181.504 1.00 70.37 C ANISOU 2215 CA ILE A 376 10282 9947 6509 -458 -261 -881 C ATOM 2216 C ILE A 376 48.572-102.814 180.250 1.00 67.40 C ANISOU 2216 C ILE A 376 9739 9580 6290 -398 -235 -749 C ATOM 2217 O ILE A 376 47.949-102.632 179.197 1.00 68.38 O ANISOU 2217 O ILE A 376 9851 9545 6587 -384 -173 -773 O ATOM 2218 CB ILE A 376 49.290-100.900 181.746 1.00 71.29 C ANISOU 2218 CB ILE A 376 10424 10143 6520 -657 -444 -943 C ATOM 2219 CG1 ILE A 376 48.811 -99.953 182.849 1.00 69.66 C ANISOU 2219 CG1 ILE A 376 10433 9865 6170 -713 -467 -1110 C ATOM 2220 CG2 ILE A 376 49.567-100.141 180.463 1.00 68.93 C ANISOU 2220 CG2 ILE A 376 10074 9744 6373 -776 -507 -958 C ATOM 2221 CD1 ILE A 376 49.784 -98.838 183.159 1.00 72.95 C ANISOU 2221 CD1 ILE A 376 10918 10335 6466 -936 -659 -1181 C ATOM 2222 N LEU A 377 49.548-103.721 180.345 1.00 65.18 N ANISOU 2222 N LEU A 377 9333 9493 5940 -347 -282 -608 N ATOM 2223 CA LEU A 377 49.898-104.556 179.201 1.00 59.33 C ANISOU 2223 CA LEU A 377 8450 8771 5323 -256 -254 -485 C ATOM 2224 C LEU A 377 48.760-105.501 178.838 1.00 57.45 C ANISOU 2224 C LEU A 377 8261 8368 5199 -108 -95 -453 C ATOM 2225 O LEU A 377 48.541-105.794 177.657 1.00 61.29 O ANISOU 2225 O LEU A 377 8689 8758 5839 -67 -50 -420 O ATOM 2226 CB LEU A 377 51.171-105.346 179.500 1.00 59.44 C ANISOU 2226 CB LEU A 377 8334 9041 5209 -193 -336 -342 C ATOM 2227 CG LEU A 377 52.415-104.544 179.882 1.00 57.49 C ANISOU 2227 CG LEU A 377 8001 9018 4826 -354 -507 -342 C ATOM 2228 CD1 LEU A 377 53.505-105.474 180.390 1.00 51.73 C ANISOU 2228 CD1 LEU A 377 7145 8566 3944 -246 -567 -193 C ATOM 2229 CD2 LEU A 377 52.912-103.723 178.703 1.00 59.05 C ANISOU 2229 CD2 LEU A 377 8092 9216 5130 -495 -580 -356 C ATOM 2230 N PHE A 378 48.027-105.990 179.841 1.00 54.88 N ANISOU 2230 N PHE A 378 8044 8019 4789 -42 -13 -458 N ATOM 2231 CA PHE A 378 46.920-106.904 179.579 1.00 54.11 C ANISOU 2231 CA PHE A 378 7996 7782 4781 63 131 -416 C ATOM 2232 C PHE A 378 45.832-106.232 178.750 1.00 58.85 C ANISOU 2232 C PHE A 378 8621 8195 5546 20 205 -517 C ATOM 2233 O PHE A 378 45.294-106.834 177.813 1.00 58.67 O ANISOU 2233 O PHE A 378 8570 8063 5659 71 279 -470 O ATOM 2234 CB PHE A 378 46.350-107.420 180.901 1.00 51.61 C ANISOU 2234 CB PHE A 378 7786 7505 4320 111 199 -399 C ATOM 2235 CG PHE A 378 45.191-108.363 180.742 1.00 50.85 C ANISOU 2235 CG PHE A 378 7744 7286 4292 182 341 -342 C ATOM 2236 CD1 PHE A 378 45.404-109.726 180.618 1.00 50.87 C ANISOU 2236 CD1 PHE A 378 7756 7287 4286 280 366 -192 C ATOM 2237 CD2 PHE A 378 43.887-107.889 180.736 1.00 48.63 C ANISOU 2237 CD2 PHE A 378 7510 6896 4070 150 445 -433 C ATOM 2238 CE1 PHE A 378 44.340-110.597 180.479 1.00 51.09 C ANISOU 2238 CE1 PHE A 378 7851 7193 4366 308 483 -132 C ATOM 2239 CE2 PHE A 378 42.821-108.755 180.594 1.00 48.35 C ANISOU 2239 CE2 PHE A 378 7506 6778 4085 185 568 -368 C ATOM 2240 CZ PHE A 378 43.048-110.111 180.467 1.00 50.98 C ANISOU 2240 CZ PHE A 378 7860 7097 4411 246 583 -217 C ATOM 2241 N ILE A 379 45.498-104.983 179.079 1.00 58.41 N ANISOU 2241 N ILE A 379 8627 8096 5468 -67 181 -657 N ATOM 2242 CA ILE A 379 44.415-104.293 178.385 1.00 59.39 C ANISOU 2242 CA ILE A 379 8785 8051 5731 -81 252 -755 C ATOM 2243 C ILE A 379 44.808-103.981 176.945 1.00 58.97 C ANISOU 2243 C ILE A 379 8641 7927 5839 -126 202 -741 C ATOM 2244 O ILE A 379 43.980-104.064 176.030 1.00 53.16 O ANISOU 2244 O ILE A 379 7884 7064 5248 -96 279 -746 O ATOM 2245 CB ILE A 379 44.016-103.024 179.160 1.00 61.47 C ANISOU 2245 CB ILE A 379 9169 8278 5907 -133 232 -912 C ATOM 2246 CG1 ILE A 379 43.438-103.397 180.526 1.00 64.72 C ANISOU 2246 CG1 ILE A 379 9665 8767 6158 -68 309 -926 C ATOM 2247 CG2 ILE A 379 43.006-102.206 178.377 1.00 66.44 C ANISOU 2247 CG2 ILE A 379 9832 8737 6674 -126 289 -1012 C ATOM 2248 CD1 ILE A 379 43.078-102.203 181.382 1.00 70.11 C ANISOU 2248 CD1 ILE A 379 10489 9427 6725 -90 292 -1089 C ATOM 2249 N ASN A 380 46.076-103.629 176.717 1.00 59.11 N ANISOU 2249 N ASN A 380 8592 8045 5823 -206 71 -714 N ATOM 2250 CA ASN A 380 46.523-103.336 175.359 1.00 62.30 C ANISOU 2250 CA ASN A 380 8898 8413 6362 -256 23 -687 C ATOM 2251 C ASN A 380 46.476-104.577 174.476 1.00 61.84 C ANISOU 2251 C ASN A 380 8750 8349 6399 -141 92 -570 C ATOM 2252 O ASN A 380 46.130-104.491 173.292 1.00 59.03 O ANISOU 2252 O ASN A 380 8351 7890 6188 -141 121 -571 O ATOM 2253 CB ASN A 380 47.938-102.755 175.382 1.00 67.54 C ANISOU 2253 CB ASN A 380 9488 9232 6941 -380 -132 -664 C ATOM 2254 CG ASN A 380 47.983-101.349 175.947 1.00 76.54 C ANISOU 2254 CG ASN A 380 10744 10324 8012 -533 -222 -792 C ATOM 2255 OD1 ASN A 380 47.089-100.934 176.682 1.00 80.54 O ANISOU 2255 OD1 ASN A 380 11398 10723 8481 -509 -169 -900 O ATOM 2256 ND2 ASN A 380 49.030-100.607 175.603 1.00 81.64 N ANISOU 2256 ND2 ASN A 380 11334 11055 8629 -694 -361 -780 N ATOM 2257 N ILE A 381 46.809-105.741 175.035 1.00 58.59 N ANISOU 2257 N ILE A 381 8328 8036 5898 -38 115 -471 N ATOM 2258 CA ILE A 381 46.921-106.950 174.225 1.00 53.09 C ANISOU 2258 CA ILE A 381 7580 7325 5267 80 161 -360 C ATOM 2259 C ILE A 381 45.541-107.471 173.839 1.00 54.89 C ANISOU 2259 C ILE A 381 7882 7371 5605 122 288 -372 C ATOM 2260 O ILE A 381 45.300-107.834 172.682 1.00 58.05 O ANISOU 2260 O ILE A 381 8247 7681 6127 152 320 -345 O ATOM 2261 CB ILE A 381 47.746-108.015 174.969 1.00 48.35 C ANISOU 2261 CB ILE A 381 6972 6875 4524 191 135 -245 C ATOM 2262 CG1 ILE A 381 49.203-107.563 175.092 1.00 49.43 C ANISOU 2262 CG1 ILE A 381 6986 7234 4559 152 1 -211 C ATOM 2263 CG2 ILE A 381 47.655-109.359 174.263 1.00 41.63 C ANISOU 2263 CG2 ILE A 381 6134 5957 3725 339 195 -141 C ATOM 2264 CD1 ILE A 381 50.060-108.475 175.939 1.00 51.97 C ANISOU 2264 CD1 ILE A 381 7291 7738 4719 270 -37 -100 C ATOM 2265 N VAL A 382 44.611-107.514 174.798 1.00 56.75 N ANISOU 2265 N VAL A 382 8211 7565 5785 118 360 -409 N ATOM 2266 CA VAL A 382 43.295-108.080 174.522 1.00 55.66 C ANISOU 2266 CA VAL A 382 8124 7297 5729 140 479 -401 C ATOM 2267 C VAL A 382 42.483-107.209 173.572 1.00 57.43 C ANISOU 2267 C VAL A 382 8316 7406 6100 84 509 -490 C ATOM 2268 O VAL A 382 41.577-107.715 172.900 1.00 62.11 O ANISOU 2268 O VAL A 382 8908 7901 6790 95 586 -467 O ATOM 2269 CB VAL A 382 42.517-108.319 175.830 1.00 56.10 C ANISOU 2269 CB VAL A 382 8267 7381 5669 144 553 -406 C ATOM 2270 CG1 VAL A 382 43.255-109.313 176.713 1.00 58.29 C ANISOU 2270 CG1 VAL A 382 8588 7758 5800 208 527 -297 C ATOM 2271 CG2 VAL A 382 42.287-107.007 176.565 1.00 57.68 C ANISOU 2271 CG2 VAL A 382 8491 7618 5808 90 537 -537 C ATOM 2272 N ARG A 383 42.779-105.909 173.493 1.00 59.30 N ANISOU 2272 N ARG A 383 8534 7647 6349 19 443 -588 N ATOM 2273 CA ARG A 383 42.080-105.051 172.543 1.00 63.34 C ANISOU 2273 CA ARG A 383 9026 8043 6997 -19 460 -664 C ATOM 2274 C ARG A 383 42.533-105.288 171.109 1.00 64.58 C ANISOU 2274 C ARG A 383 9098 8162 7277 -24 426 -610 C ATOM 2275 O ARG A 383 41.827-104.892 170.176 1.00 64.84 O ANISOU 2275 O ARG A 383 9110 8094 7434 -40 456 -645 O ATOM 2276 CB ARG A 383 42.283-103.577 172.898 1.00 72.56 C ANISOU 2276 CB ARG A 383 10241 9198 8129 -88 389 -782 C ATOM 2277 CG ARG A 383 41.455-103.081 174.071 1.00 87.37 C ANISOU 2277 CG ARG A 383 12218 11071 9907 -63 444 -874 C ATOM 2278 CD ARG A 383 41.293-101.568 174.009 1.00 97.34 C ANISOU 2278 CD ARG A 383 13561 12244 11182 -107 391 -1007 C ATOM 2279 NE ARG A 383 42.561-100.865 174.186 1.00102.88 N ANISOU 2279 NE ARG A 383 14290 12983 11815 -215 247 -1029 N ATOM 2280 CZ ARG A 383 42.860-100.120 175.245 1.00105.19 C ANISOU 2280 CZ ARG A 383 14700 13300 11968 -259 185 -1117 C ATOM 2281 NH1 ARG A 383 41.975 -99.969 176.220 1.00104.76 N ANISOU 2281 NH1 ARG A 383 14745 13236 11823 -177 265 -1198 N ATOM 2282 NH2 ARG A 383 44.038 -99.517 175.325 1.00106.24 N ANISOU 2282 NH2 ARG A 383 14849 13480 12039 -390 41 -1124 N ATOM 2283 N VAL A 384 43.687-105.928 170.915 1.00 61.17 N ANISOU 2283 N VAL A 384 8613 7824 6804 3 366 -524 N ATOM 2284 CA VAL A 384 44.296-106.075 169.603 1.00 52.22 C ANISOU 2284 CA VAL A 384 7391 6692 5758 10 326 -476 C ATOM 2285 C VAL A 384 44.394-107.535 169.180 1.00 58.37 C ANISOU 2285 C VAL A 384 8172 7465 6541 122 370 -376 C ATOM 2286 O VAL A 384 44.166-107.864 168.010 1.00 68.09 O ANISOU 2286 O VAL A 384 9376 8623 7873 145 393 -356 O ATOM 2287 CB VAL A 384 45.687-105.401 169.570 1.00 48.82 C ANISOU 2287 CB VAL A 384 6878 6405 5264 -52 205 -464 C ATOM 2288 CG1 VAL A 384 46.421-105.739 168.296 1.00 56.68 C ANISOU 2288 CG1 VAL A 384 7764 7454 6318 -20 175 -393 C ATOM 2289 CG2 VAL A 384 45.544-103.892 169.711 1.00 39.04 C ANISOU 2289 CG2 VAL A 384 5672 5120 4041 -185 149 -567 C ATOM 2290 N LEU A 385 44.716-108.428 170.110 1.00 58.29 N ANISOU 2290 N LEU A 385 8214 7518 6414 196 379 -312 N ATOM 2291 CA LEU A 385 44.855-109.847 169.806 1.00 60.09 C ANISOU 2291 CA LEU A 385 8489 7716 6627 316 411 -214 C ATOM 2292 C LEU A 385 43.493-110.523 169.916 1.00 65.57 C ANISOU 2292 C LEU A 385 9293 8258 7364 301 509 -210 C ATOM 2293 O LEU A 385 42.888-110.540 170.994 1.00 67.62 O ANISOU 2293 O LEU A 385 9613 8522 7557 267 552 -219 O ATOM 2294 CB LEU A 385 45.863-110.504 170.748 1.00 60.76 C ANISOU 2294 CB LEU A 385 8591 7939 6557 412 366 -134 C ATOM 2295 CG LEU A 385 46.222-111.956 170.432 1.00 62.04 C ANISOU 2295 CG LEU A 385 8824 8067 6680 572 381 -28 C ATOM 2296 CD1 LEU A 385 46.790-112.065 169.028 1.00 59.72 C ANISOU 2296 CD1 LEU A 385 8452 7781 6458 640 355 -15 C ATOM 2297 CD2 LEU A 385 47.206-112.501 171.452 1.00 59.47 C ANISOU 2297 CD2 LEU A 385 8512 7893 6190 682 331 53 C ATOM 2298 N ALA A 386 43.016-111.077 168.805 1.00 64.10 N ANISOU 2298 N ALA A 386 9126 7954 7276 314 543 -192 N ATOM 2299 CA ALA A 386 41.735-111.767 168.800 1.00 63.12 C ANISOU 2299 CA ALA A 386 9096 7698 7189 270 626 -174 C ATOM 2300 C ALA A 386 41.832-113.087 169.556 1.00 60.59 C ANISOU 2300 C ALA A 386 8914 7348 6758 335 644 -75 C ATOM 2301 O ALA A 386 42.897-113.702 169.645 1.00 57.65 O ANISOU 2301 O ALA A 386 8576 7019 6308 457 594 -13 O ATOM 2302 CB ALA A 386 41.267-112.018 167.366 1.00 61.06 C ANISOU 2302 CB ALA A 386 8828 7323 7051 254 640 -181 C ATOM 2303 N THR A 387 40.697-113.520 170.110 1.00 65.53 N ANISOU 2303 N THR A 387 9621 7910 7369 255 716 -52 N ATOM 2304 CA THR A 387 40.667-114.778 170.846 1.00 72.13 C ANISOU 2304 CA THR A 387 10612 8696 8097 288 734 54 C ATOM 2305 C THR A 387 40.852-115.987 169.938 1.00 72.89 C ANISOU 2305 C THR A 387 10840 8640 8214 353 716 123 C ATOM 2306 O THR A 387 41.278-117.043 170.417 1.00 73.09 O ANISOU 2306 O THR A 387 11017 8616 8138 439 699 215 O ATOM 2307 CB THR A 387 39.355-114.913 171.621 1.00 76.64 C ANISOU 2307 CB THR A 387 11224 9257 8639 159 817 72 C ATOM 2308 OG1 THR A 387 38.248-114.818 170.716 1.00 84.33 O ANISOU 2308 OG1 THR A 387 12161 10150 9729 50 863 43 O ATOM 2309 CG2 THR A 387 39.241-113.816 172.670 1.00 77.95 C ANISOU 2309 CG2 THR A 387 11295 9575 8749 133 837 3 C ATOM 2310 N LYS A 388 40.544-115.857 168.648 1.00 72.50 N ANISOU 2310 N LYS A 388 10755 8510 8283 324 714 78 N ATOM 2311 CA LYS A 388 40.687-116.954 167.702 1.00 72.65 C ANISOU 2311 CA LYS A 388 10916 8373 8316 387 694 125 C ATOM 2312 C LYS A 388 40.920-116.382 166.311 1.00 69.09 C ANISOU 2312 C LYS A 388 10353 7921 7975 409 668 53 C ATOM 2313 O LYS A 388 40.298-115.389 165.925 1.00 67.96 O ANISOU 2313 O LYS A 388 10072 7819 7930 301 689 -19 O ATOM 2314 CB LYS A 388 39.454-117.867 167.711 1.00 78.10 C ANISOU 2314 CB LYS A 388 11763 8903 9008 246 740 179 C ATOM 2315 CG LYS A 388 39.637-119.160 166.932 1.00 89.44 C ANISOU 2315 CG LYS A 388 13418 10142 10423 312 707 234 C ATOM 2316 CD LYS A 388 38.440-120.077 167.105 1.00 98.88 C ANISOU 2316 CD LYS A 388 14788 11183 11599 132 739 302 C ATOM 2317 CE LYS A 388 38.656-121.416 166.420 1.00105.21 C ANISOU 2317 CE LYS A 388 15864 11752 12358 194 693 355 C ATOM 2318 NZ LYS A 388 37.507-122.344 166.618 1.00109.22 N ANISOU 2318 NZ LYS A 388 16566 12098 12833 -19 710 434 N ATOM 2319 N GLY A1218 41.826-117.008 165.569 1.00 65.84 N ANISOU 2319 N GLY A1218 10007 7471 7538 565 624 76 N ATOM 2320 CA GLY A1218 42.152-116.566 164.230 1.00 66.33 C ANISOU 2320 CA GLY A1218 9971 7547 7683 602 601 20 C ATOM 2321 C GLY A1218 41.198-117.117 163.188 1.00 64.92 C ANISOU 2321 C GLY A1218 9896 7192 7578 516 620 5 C ATOM 2322 O GLY A1218 40.099-117.589 163.490 1.00 67.38 O ANISOU 2322 O GLY A1218 10313 7391 7899 375 654 28 O ATOM 2323 N ILE A1219 41.635-117.049 161.935 1.00 57.97 N ANISOU 2323 N ILE A1219 8980 6306 6740 591 593 -31 N ATOM 2324 CA ILE A1219 40.844-117.540 160.814 1.00 54.11 C ANISOU 2324 CA ILE A1219 8589 5660 6310 518 598 -54 C ATOM 2325 C ILE A1219 41.162-119.010 160.592 1.00 53.28 C ANISOU 2325 C ILE A1219 8752 5383 6110 645 576 -6 C ATOM 2326 O ILE A1219 42.248-119.494 160.930 1.00 57.11 O ANISOU 2326 O ILE A1219 9301 5905 6495 851 553 34 O ATOM 2327 CB ILE A1219 41.100-116.710 159.538 1.00 54.78 C ANISOU 2327 CB ILE A1219 8512 5823 6479 531 581 -118 C ATOM 2328 CG1 ILE A1219 42.522-116.938 159.023 1.00 51.52 C ANISOU 2328 CG1 ILE A1219 8085 5497 5993 759 545 -108 C ATOM 2329 CG2 ILE A1219 40.859-115.233 159.808 1.00 55.84 C ANISOU 2329 CG2 ILE A1219 8417 6102 6696 420 592 -162 C ATOM 2330 CD1 ILE A1219 42.803-116.289 157.688 1.00 46.07 C ANISOU 2330 CD1 ILE A1219 7259 4882 5364 775 530 -156 C ATOM 2331 N ASP A1220 40.201-119.732 160.027 1.00 49.20 N ANISOU 2331 N ASP A1220 8403 4677 5615 524 578 -6 N ATOM 2332 CA ASP A1220 40.388-121.142 159.711 1.00 47.95 C ANISOU 2332 CA ASP A1220 8549 4305 5363 625 547 29 C ATOM 2333 C ASP A1220 41.301-121.280 158.497 1.00 55.23 C ANISOU 2333 C ASP A1220 9485 5236 6264 835 517 -19 C ATOM 2334 O ASP A1220 40.846-121.218 157.354 1.00 59.07 O ANISOU 2334 O ASP A1220 9975 5663 6806 767 508 -74 O ATOM 2335 CB ASP A1220 39.040-121.818 159.455 1.00 49.26 C ANISOU 2335 CB ASP A1220 8892 4271 5553 388 547 43 C ATOM 2336 CG ASP A1220 39.154-123.326 159.335 1.00 57.38 C ANISOU 2336 CG ASP A1220 10293 5038 6470 459 505 88 C ATOM 2337 OD1 ASP A1220 40.276-123.858 159.470 1.00 60.38 O ANISOU 2337 OD1 ASP A1220 10796 5393 6753 726 483 107 O ATOM 2338 OD2 ASP A1220 38.115-123.980 159.108 1.00 62.91 O ANISOU 2338 OD2 ASP A1220 11172 5560 7172 247 490 107 O HETATM 2339 N YCM A1221 42.590-121.471 158.756 1.00 57.99 N ANISOU 2339 N YCM A1221 9832 5681 6519 1098 503 6 N HETATM 2340 CA YCM A1221 43.586-121.520 157.702 1.00 61.35 C ANISOU 2340 CA YCM A1221 10225 6181 6903 1328 484 -30 C HETATM 2341 CB YCM A1221 44.984-121.508 158.307 1.00 67.74 C ANISOU 2341 CB YCM A1221 10949 7183 7606 1591 474 19 C HETATM 2342 SG YCM A1221 45.463-119.835 158.569 1.00 76.99 S ANISOU 2342 SG YCM A1221 11711 8686 8856 1503 483 4 S HETATM 2343 CD YCM A1221 45.381-119.377 156.871 1.00 79.18 C ANISOU 2343 CD YCM A1221 11890 8990 9205 1487 484 -71 C HETATM 2344 CE YCM A1221 46.756-119.025 156.367 1.00 78.69 C ANISOU 2344 CE YCM A1221 11644 9183 9070 1704 471 -59 C HETATM 2345 OZ1 YCM A1221 46.954-118.898 155.171 1.00 84.51 O ANISOU 2345 OZ1 YCM A1221 12332 9963 9813 1758 472 -96 O HETATM 2346 NZ2 YCM A1221 47.709-118.881 157.286 1.00 74.38 N ANISOU 2346 NZ2 YCM A1221 10991 8827 8442 1823 458 1 N HETATM 2347 C YCM A1221 43.429-122.728 156.826 1.00 63.79 C ANISOU 2347 C YCM A1221 10847 6246 7147 1422 459 -50 C HETATM 2348 O YCM A1221 43.854-122.697 155.651 1.00 61.64 O ANISOU 2348 O YCM A1221 10551 6007 6861 1547 451 -105 O ATOM 2349 N SER A1222 42.832-123.787 157.359 1.00 68.40 N ANISOU 2349 N SER A1222 11733 6580 7677 1358 444 -7 N ATOM 2350 CA SER A1222 42.646-125.017 156.600 1.00 66.93 C ANISOU 2350 CA SER A1222 11905 6113 7411 1431 407 -27 C ATOM 2351 C SER A1222 41.560-124.860 155.541 1.00 61.38 C ANISOU 2351 C SER A1222 11215 5307 6799 1186 397 -94 C ATOM 2352 O SER A1222 41.462-125.669 154.619 1.00 64.55 O ANISOU 2352 O SER A1222 11873 5511 7142 1241 361 -138 O ATOM 2353 CB SER A1222 42.299-126.176 157.537 1.00 72.23 C ANISOU 2353 CB SER A1222 12917 6534 7994 1399 383 53 C ATOM 2354 OG SER A1222 41.064-125.946 158.191 1.00 73.55 O ANISOU 2354 OG SER A1222 13047 6658 8241 1050 399 91 O ATOM 2355 N PHE A1223 40.745-123.815 155.675 1.00 54.93 N ANISOU 2355 N PHE A1223 10128 4627 6114 925 426 -105 N ATOM 2356 CA PHE A1223 39.613-123.588 154.786 1.00 50.96 C ANISOU 2356 CA PHE A1223 9601 4061 5700 674 416 -154 C ATOM 2357 C PHE A1223 39.837-122.445 153.807 1.00 49.32 C ANISOU 2357 C PHE A1223 9099 4060 5580 696 431 -222 C ATOM 2358 O PHE A1223 39.553-122.591 152.614 1.00 39.97 O ANISOU 2358 O PHE A1223 7974 2809 4403 667 406 -280 O ATOM 2359 CB PHE A1223 38.343-123.322 155.610 1.00 45.76 C ANISOU 2359 CB PHE A1223 8873 3399 5114 355 438 -106 C ATOM 2360 CG PHE A1223 37.115-123.106 154.773 1.00 44.15 C ANISOU 2360 CG PHE A1223 8624 3161 4991 89 425 -141 C ATOM 2361 CD1 PHE A1223 36.398-124.185 154.284 1.00 44.64 C ANISOU 2361 CD1 PHE A1223 8982 2980 4998 -57 373 -136 C ATOM 2362 CD2 PHE A1223 36.680-121.826 154.471 1.00 42.09 C ANISOU 2362 CD2 PHE A1223 8033 3108 4850 -15 456 -176 C ATOM 2363 CE1 PHE A1223 35.270-123.993 153.511 1.00 44.31 C ANISOU 2363 CE1 PHE A1223 8882 2934 5019 -313 353 -162 C ATOM 2364 CE2 PHE A1223 35.553-121.627 153.697 1.00 40.36 C ANISOU 2364 CE2 PHE A1223 7759 2879 4696 -242 440 -201 C ATOM 2365 CZ PHE A1223 34.849-122.712 153.216 1.00 43.24 C ANISOU 2365 CZ PHE A1223 8394 3030 5004 -396 389 -192 C ATOM 2366 N TRP A1224 40.334-121.301 154.277 1.00 41.98 N ANISOU 2366 N TRP A1224 7864 3376 4709 734 465 -214 N ATOM 2367 CA TRP A1224 40.480-120.113 153.434 1.00 38.50 C ANISOU 2367 CA TRP A1224 7145 3127 4357 718 475 -264 C ATOM 2368 C TRP A1224 41.784-120.213 152.648 1.00 44.08 C ANISOU 2368 C TRP A1224 7835 3930 4982 996 465 -287 C ATOM 2369 O TRP A1224 42.814-119.630 152.998 1.00 53.48 O ANISOU 2369 O TRP A1224 8844 5326 6150 1140 477 -264 O ATOM 2370 CB TRP A1224 40.422-118.848 154.279 1.00 35.40 C ANISOU 2370 CB TRP A1224 6470 2930 4050 622 505 -246 C ATOM 2371 CG TRP A1224 39.167-118.747 155.082 1.00 45.23 C ANISOU 2371 CG TRP A1224 7716 4114 5354 383 527 -223 C ATOM 2372 CD1 TRP A1224 39.039-118.930 156.426 1.00 47.34 C ANISOU 2372 CD1 TRP A1224 8020 4377 5589 347 548 -170 C ATOM 2373 CD2 TRP A1224 37.854-118.458 154.589 1.00 45.74 C ANISOU 2373 CD2 TRP A1224 7734 4141 5506 154 530 -244 C ATOM 2374 NE1 TRP A1224 37.729-118.763 156.805 1.00 48.50 N ANISOU 2374 NE1 TRP A1224 8138 4496 5794 111 572 -157 N ATOM 2375 CE2 TRP A1224 36.981-118.475 155.695 1.00 43.00 C ANISOU 2375 CE2 TRP A1224 7382 3784 5171 -8 560 -200 C ATOM 2376 CE3 TRP A1224 37.333-118.182 153.321 1.00 40.05 C ANISOU 2376 CE3 TRP A1224 6961 3413 4843 75 511 -291 C ATOM 2377 CZ2 TRP A1224 35.616-118.227 155.572 1.00 36.92 C ANISOU 2377 CZ2 TRP A1224 6544 3017 4467 -238 574 -198 C ATOM 2378 CZ3 TRP A1224 35.978-117.936 153.200 1.00 42.43 C ANISOU 2378 CZ3 TRP A1224 7202 3705 5215 -157 517 -290 C ATOM 2379 CH2 TRP A1224 35.134-117.960 154.320 1.00 47.64 C ANISOU 2379 CH2 TRP A1224 7845 4375 5883 -308 550 -242 C ATOM 2380 N ASN A1225 41.724-120.963 151.549 1.00 42.09 N ANISOU 2380 N ASN A1225 7775 3544 4676 1065 441 -332 N ATOM 2381 CA ASN A1225 42.871-121.182 150.679 1.00 41.33 C ANISOU 2381 CA ASN A1225 7686 3537 4480 1345 437 -360 C ATOM 2382 C ASN A1225 42.380-121.253 149.241 1.00 48.02 C ANISOU 2382 C ASN A1225 8591 4315 5339 1287 418 -430 C ATOM 2383 O ASN A1225 41.408-121.958 148.955 1.00 56.12 O ANISOU 2383 O ASN A1225 9847 5108 6366 1138 388 -458 O ATOM 2384 CB ASN A1225 43.611-122.470 151.064 1.00 41.81 C ANISOU 2384 CB ASN A1225 8036 3464 4385 1613 425 -337 C ATOM 2385 CG ASN A1225 44.963-122.601 150.384 1.00 54.37 C ANISOU 2385 CG ASN A1225 9581 5222 5855 1955 434 -351 C ATOM 2386 OD1 ASN A1225 45.112-122.315 149.196 1.00 57.56 O ANISOU 2386 OD1 ASN A1225 9909 5708 6252 1998 437 -403 O ATOM 2387 ND2 ASN A1225 45.960-123.040 151.143 1.00 55.75 N ANISOU 2387 ND2 ASN A1225 9791 5470 5921 2209 440 -297 N ATOM 2388 N GLU A1226 43.051-120.530 148.339 1.00 47.25 N ANISOU 2388 N GLU A1226 8284 4429 5240 1391 430 -453 N ATOM 2389 CA GLU A1226 42.625-120.526 146.944 1.00 52.98 C ANISOU 2389 CA GLU A1226 9046 5116 5968 1341 412 -518 C ATOM 2390 C GLU A1226 42.910-121.850 146.247 1.00 49.03 C ANISOU 2390 C GLU A1226 8886 4429 5315 1546 389 -571 C ATOM 2391 O GLU A1226 42.300-122.134 145.211 1.00 52.78 O ANISOU 2391 O GLU A1226 9488 4787 5777 1464 360 -634 O ATOM 2392 CB GLU A1226 43.295-119.382 146.177 1.00 51.30 C ANISOU 2392 CB GLU A1226 8520 5188 5782 1392 433 -516 C ATOM 2393 CG GLU A1226 42.546-118.979 144.911 1.00 55.29 C ANISOU 2393 CG GLU A1226 8984 5683 6341 1240 414 -566 C ATOM 2394 CD GLU A1226 43.374-118.118 143.975 1.00 70.56 C ANISOU 2394 CD GLU A1226 10675 7881 8253 1341 431 -559 C ATOM 2395 OE1 GLU A1226 44.618-118.173 144.056 1.00 78.03 O ANISOU 2395 OE1 GLU A1226 11546 9004 9099 1579 456 -530 O ATOM 2396 OE2 GLU A1226 42.778-117.387 143.155 1.00 72.83 O ANISOU 2396 OE2 GLU A1226 10841 8215 8617 1179 418 -574 O ATOM 2397 N SER A1227 43.810-122.670 146.794 1.00 46.63 N ANISOU 2397 N SER A1227 8745 4088 4885 1818 397 -549 N ATOM 2398 CA SER A1227 44.114-123.965 146.196 1.00 57.51 C ANISOU 2398 CA SER A1227 10488 5262 6100 2051 373 -604 C ATOM 2399 C SER A1227 42.945-124.941 146.263 1.00 58.97 C ANISOU 2399 C SER A1227 11044 5078 6285 1847 317 -634 C ATOM 2400 O SER A1227 43.043-126.033 145.694 1.00 57.07 O ANISOU 2400 O SER A1227 11129 4640 5913 1982 279 -682 O ATOM 2401 CB SER A1227 45.343-124.580 146.869 1.00 67.45 C ANISOU 2401 CB SER A1227 11830 6577 7221 2409 392 -561 C ATOM 2402 OG SER A1227 46.487-123.764 146.683 1.00 70.93 O ANISOU 2402 OG SER A1227 11931 7385 7634 2602 436 -530 O ATOM 2403 N TYR A1228 41.856-124.587 146.949 1.00 55.68 N ANISOU 2403 N TYR A1228 10559 4596 6001 1508 306 -594 N ATOM 2404 CA TYR A1228 40.632-125.377 146.908 1.00 48.94 C ANISOU 2404 CA TYR A1228 10001 3441 5152 1247 250 -611 C ATOM 2405 C TYR A1228 39.806-125.123 145.655 1.00 51.36 C ANISOU 2405 C TYR A1228 10286 3731 5500 1050 216 -680 C ATOM 2406 O TYR A1228 38.911-125.918 145.351 1.00 57.55 O ANISOU 2406 O TYR A1228 11346 4271 6250 858 154 -705 O ATOM 2407 CB TYR A1228 39.769-125.095 148.142 1.00 45.58 C ANISOU 2407 CB TYR A1228 9482 2998 4837 964 258 -530 C ATOM 2408 CG TYR A1228 40.267-125.739 149.417 1.00 49.31 C ANISOU 2408 CG TYR A1228 10112 3381 5244 1093 268 -458 C ATOM 2409 CD1 TYR A1228 39.959-127.061 149.717 1.00 47.55 C ANISOU 2409 CD1 TYR A1228 10294 2856 4918 1068 215 -438 C ATOM 2410 CD2 TYR A1228 41.031-125.021 150.327 1.00 52.28 C ANISOU 2410 CD2 TYR A1228 10222 3989 5653 1220 319 -402 C ATOM 2411 CE1 TYR A1228 40.408-127.653 150.882 1.00 52.71 C ANISOU 2411 CE1 TYR A1228 11074 3449 5505 1182 219 -359 C ATOM 2412 CE2 TYR A1228 41.485-125.605 151.496 1.00 53.71 C ANISOU 2412 CE2 TYR A1228 10541 4102 5765 1340 323 -332 C ATOM 2413 CZ TYR A1228 41.170-126.920 151.768 1.00 53.84 C ANISOU 2413 CZ TYR A1228 10977 3800 5681 1336 277 -311 C ATOM 2414 OH TYR A1228 41.621-127.500 152.931 1.00 54.77 O ANISOU 2414 OH TYR A1228 11240 3847 5724 1461 278 -232 O ATOM 2415 N LEU A1229 40.080-124.047 144.927 1.00 50.88 N ANISOU 2415 N LEU A1229 9903 3930 5502 1078 248 -701 N ATOM 2416 CA LEU A1229 39.295-123.683 143.759 1.00 47.22 C ANISOU 2416 CA LEU A1229 9380 3482 5080 890 216 -756 C ATOM 2417 C LEU A1229 39.930-124.231 142.485 1.00 52.13 C ANISOU 2417 C LEU A1229 10184 4066 5557 1125 197 -844 C ATOM 2418 O LEU A1229 41.132-124.501 142.423 1.00 55.59 O ANISOU 2418 O LEU A1229 10662 4576 5884 1463 231 -855 O ATOM 2419 CB LEU A1229 39.150-122.163 143.663 1.00 42.84 C ANISOU 2419 CB LEU A1229 8388 3216 4672 774 255 -723 C ATOM 2420 CG LEU A1229 38.623-121.472 144.923 1.00 42.61 C ANISOU 2420 CG LEU A1229 8154 3258 4777 586 283 -646 C ATOM 2421 CD1 LEU A1229 38.458-119.977 144.697 1.00 37.04 C ANISOU 2421 CD1 LEU A1229 7067 2803 4202 487 311 -626 C ATOM 2422 CD2 LEU A1229 37.313-122.098 145.368 1.00 39.75 C ANISOU 2422 CD2 LEU A1229 7970 2693 4442 301 243 -628 C ATOM 2423 N THR A1230 39.099-124.392 141.461 1.00 55.79 N ANISOU 2423 N THR A1230 10750 4437 6011 947 144 -905 N ATOM 2424 CA THR A1230 39.521-124.932 140.178 1.00 67.58 C ANISOU 2424 CA THR A1230 12442 5877 7356 1134 118 -1001 C ATOM 2425 C THR A1230 39.407-123.866 139.095 1.00 68.24 C ANISOU 2425 C THR A1230 12221 6209 7497 1069 131 -1020 C ATOM 2426 O THR A1230 38.613-122.927 139.203 1.00 62.52 O ANISOU 2426 O THR A1230 11226 5605 6925 805 131 -973 O ATOM 2427 CB THR A1230 38.684-126.156 139.793 1.00 71.85 C ANISOU 2427 CB THR A1230 13314 6164 7821 956 24 -1022 C ATOM 2428 OG1 THR A1230 37.307-125.780 139.670 1.00 75.74 O ANISOU 2428 OG1 THR A1230 13751 6606 8423 564 -23 -1019 O ATOM 2429 CG2 THR A1230 38.811-127.237 140.851 1.00 71.32 C ANISOU 2429 CG2 THR A1230 13466 5931 7703 989 2 -953 C ATOM 2430 N GLY A1231 40.211-124.023 138.048 1.00 73.93 N ANISOU 2430 N GLY A1231 12994 7012 8084 1327 145 -1086 N ATOM 2431 CA GLY A1231 40.221-123.072 136.953 1.00 72.15 C ANISOU 2431 CA GLY A1231 12500 7027 7886 1293 158 -1098 C ATOM 2432 C GLY A1231 40.900-121.768 137.335 1.00 72.39 C ANISOU 2432 C GLY A1231 12098 7385 8023 1346 229 -1009 C ATOM 2433 O GLY A1231 41.323-121.548 138.469 1.00 77.22 O ANISOU 2433 O GLY A1231 12598 8047 8693 1393 267 -941 O ATOM 2434 N SER A1232 41.001-120.885 136.346 1.00 64.88 N ANISOU 2434 N SER A1232 10910 6654 7086 1325 241 -1006 N ATOM 2435 CA SER A1232 41.609-119.583 136.560 1.00 59.95 C ANISOU 2435 CA SER A1232 9893 6332 6555 1338 295 -918 C ATOM 2436 C SER A1232 40.603-118.618 137.180 1.00 58.41 C ANISOU 2436 C SER A1232 9487 6144 6562 1023 278 -856 C ATOM 2437 O SER A1232 39.390-118.841 137.160 1.00 58.48 O ANISOU 2437 O SER A1232 9601 5985 6635 787 227 -878 O ATOM 2438 CB SER A1232 42.138-119.010 135.246 1.00 53.95 C ANISOU 2438 CB SER A1232 8974 5806 5719 1436 313 -927 C ATOM 2439 OG SER A1232 41.072-118.699 134.367 1.00 55.75 O ANISOU 2439 OG SER A1232 9198 5987 5998 1204 260 -955 O ATOM 2440 N ARG A1233 41.129-117.523 137.734 1.00 56.48 N ANISOU 2440 N ARG A1233 8942 6108 6408 1021 319 -775 N ATOM 2441 CA ARG A1233 40.265-116.532 138.365 1.00 49.40 C ANISOU 2441 CA ARG A1233 7850 5227 5691 765 308 -720 C ATOM 2442 C ARG A1233 39.360-115.845 137.350 1.00 52.75 C ANISOU 2442 C ARG A1233 8169 5692 6179 577 271 -725 C ATOM 2443 O ARG A1233 38.220-115.497 137.677 1.00 53.13 O ANISOU 2443 O ARG A1233 8172 5668 6345 355 244 -709 O ATOM 2444 CB ARG A1233 41.107-115.499 139.112 1.00 45.77 C ANISOU 2444 CB ARG A1233 7125 4970 5294 812 350 -641 C ATOM 2445 CG ARG A1233 40.310-114.638 140.073 1.00 32.76 C ANISOU 2445 CG ARG A1233 5337 3299 3812 597 345 -596 C ATOM 2446 CD ARG A1233 41.166-113.537 140.671 1.00 39.14 C ANISOU 2446 CD ARG A1233 5902 4301 4667 627 371 -527 C ATOM 2447 NE ARG A1233 40.478-112.864 141.769 1.00 45.02 N ANISOU 2447 NE ARG A1233 6563 4997 5545 463 370 -498 N ATOM 2448 CZ ARG A1233 40.533-113.262 143.036 1.00 44.09 C ANISOU 2448 CZ ARG A1233 6512 4805 5436 480 388 -491 C ATOM 2449 NH1 ARG A1233 41.247-114.329 143.368 1.00 31.88 N ANISOU 2449 NH1 ARG A1233 5120 3215 3777 654 403 -504 N ATOM 2450 NH2 ARG A1233 39.874-112.594 143.971 1.00 39.49 N ANISOU 2450 NH2 ARG A1233 5847 4194 4962 338 391 -471 N ATOM 2451 N ASP A1234 39.844-115.642 136.122 1.00 61.46 N ANISOU 2451 N ASP A1234 9225 6930 7197 672 270 -739 N ATOM 2452 CA ASP A1234 39.007-115.038 135.090 1.00 61.08 C ANISOU 2452 CA ASP A1234 9090 6925 7193 506 229 -740 C ATOM 2453 C ASP A1234 37.824-115.933 134.746 1.00 49.72 C ANISOU 2453 C ASP A1234 7882 5278 5733 359 168 -808 C ATOM 2454 O ASP A1234 36.704-115.446 134.555 1.00 42.40 O ANISOU 2454 O ASP A1234 6869 4340 4901 141 127 -789 O ATOM 2455 CB ASP A1234 39.836-114.747 133.840 1.00 78.08 C ANISOU 2455 CB ASP A1234 11164 9271 9231 649 243 -739 C ATOM 2456 CG ASP A1234 40.903-113.701 134.078 1.00 96.07 C ANISOU 2456 CG ASP A1234 13179 11789 11534 729 290 -650 C ATOM 2457 OD1 ASP A1234 40.706-112.840 134.961 1.00103.50 O ANISOU 2457 OD1 ASP A1234 13963 12748 12615 607 293 -587 O ATOM 2458 OD2 ASP A1234 41.939-113.738 133.380 1.00105.45 O ANISOU 2458 OD2 ASP A1234 14319 13156 12590 909 322 -642 O ATOM 2459 N GLU A1235 38.055-117.246 134.662 1.00 49.86 N ANISOU 2459 N GLU A1235 8198 5129 5616 475 157 -884 N ATOM 2460 CA GLU A1235 36.962-118.174 134.391 1.00 50.69 C ANISOU 2460 CA GLU A1235 8558 5016 5687 307 86 -946 C ATOM 2461 C GLU A1235 35.954-118.188 135.532 1.00 52.69 C ANISOU 2461 C GLU A1235 8799 5153 6069 79 70 -904 C ATOM 2462 O GLU A1235 34.741-118.239 135.297 1.00 55.93 O ANISOU 2462 O GLU A1235 9224 5506 6521 -165 11 -905 O ATOM 2463 CB GLU A1235 37.514-119.579 134.152 1.00 59.66 C ANISOU 2463 CB GLU A1235 10058 5968 6641 496 74 -1037 C ATOM 2464 CG GLU A1235 38.381-119.713 132.914 1.00 68.38 C ANISOU 2464 CG GLU A1235 11210 7186 7586 729 88 -1094 C ATOM 2465 CD GLU A1235 39.023-121.083 132.800 1.00 76.45 C ANISOU 2465 CD GLU A1235 12605 8024 8417 973 85 -1187 C ATOM 2466 OE1 GLU A1235 38.913-121.876 133.759 1.00 76.11 O ANISOU 2466 OE1 GLU A1235 12775 7767 8375 972 74 -1192 O ATOM 2467 OE2 GLU A1235 39.637-121.367 131.750 1.00 81.06 O ANISOU 2467 OE2 GLU A1235 13281 8676 8841 1177 93 -1252 O ATOM 2468 N ARG A1236 36.436-118.141 136.776 1.00 51.60 N ANISOU 2468 N ARG A1236 8620 5002 5981 153 120 -860 N ATOM 2469 CA ARG A1236 35.529-118.193 137.918 1.00 49.22 C ANISOU 2469 CA ARG A1236 8310 4606 5783 -46 114 -817 C ATOM 2470 C ARG A1236 34.699-116.921 138.026 1.00 44.44 C ANISOU 2470 C ARG A1236 7398 4156 5330 -229 117 -756 C ATOM 2471 O ARG A1236 33.526-116.973 138.416 1.00 50.69 O ANISOU 2471 O ARG A1236 8175 4900 6185 -450 90 -732 O ATOM 2472 CB ARG A1236 36.316-118.438 139.205 1.00 51.68 C ANISOU 2472 CB ARG A1236 8657 4881 6098 96 168 -787 C ATOM 2473 CG ARG A1236 37.083-119.752 139.217 1.00 52.33 C ANISOU 2473 CG ARG A1236 9065 4792 6024 299 163 -840 C ATOM 2474 CD ARG A1236 37.495-120.148 140.626 1.00 54.11 C ANISOU 2474 CD ARG A1236 9361 4941 6257 374 198 -798 C ATOM 2475 NE ARG A1236 38.324-119.137 141.275 1.00 53.50 N ANISOU 2475 NE ARG A1236 9001 5078 6249 491 260 -740 N ATOM 2476 CZ ARG A1236 39.649-119.087 141.185 1.00 53.10 C ANISOU 2476 CZ ARG A1236 8905 5153 6118 762 297 -737 C ATOM 2477 NH1 ARG A1236 40.301-119.992 140.467 1.00 50.41 N ANISOU 2477 NH1 ARG A1236 8784 4749 5623 979 289 -795 N ATOM 2478 NH2 ARG A1236 40.323-118.133 141.813 1.00 50.93 N ANISOU 2478 NH2 ARG A1236 8368 5077 5906 816 340 -677 N ATOM 2479 N LYS A1237 35.281-115.769 137.683 1.00 39.99 N ANISOU 2479 N LYS A1237 6592 3785 4817 -138 148 -723 N ATOM 2480 CA LYS A1237 34.524-114.523 137.759 1.00 39.87 C ANISOU 2480 CA LYS A1237 6315 3896 4938 -281 147 -666 C ATOM 2481 C LYS A1237 33.471-114.449 136.661 1.00 46.90 C ANISOU 2481 C LYS A1237 7187 4807 5825 -440 84 -679 C ATOM 2482 O LYS A1237 32.359-113.959 136.893 1.00 52.55 O ANISOU 2482 O LYS A1237 7775 5560 6631 -611 65 -641 O ATOM 2483 CB LYS A1237 35.462-113.320 137.677 1.00 37.92 C ANISOU 2483 CB LYS A1237 5849 3824 4735 -157 185 -622 C ATOM 2484 CG LYS A1237 34.767-111.999 137.978 1.00 40.50 C ANISOU 2484 CG LYS A1237 5942 4244 5200 -275 185 -563 C ATOM 2485 CD LYS A1237 35.716-110.818 137.900 1.00 37.47 C ANISOU 2485 CD LYS A1237 5381 4006 4851 -181 208 -515 C ATOM 2486 CE LYS A1237 35.998-110.425 136.464 1.00 36.83 C ANISOU 2486 CE LYS A1237 5244 4033 4718 -152 181 -506 C ATOM 2487 NZ LYS A1237 36.849-109.205 136.393 1.00 39.57 N ANISOU 2487 NZ LYS A1237 5415 4522 5097 -103 195 -440 N ATOM 2488 N LYS A1238 33.803-114.926 135.459 1.00 50.22 N ANISOU 2488 N LYS A1238 7729 5222 6132 -376 51 -730 N ATOM 2489 CA LYS A1238 32.835-114.911 134.367 1.00 51.96 C ANISOU 2489 CA LYS A1238 7943 5468 6331 -530 -18 -745 C ATOM 2490 C LYS A1238 31.661-115.835 134.663 1.00 47.04 C ANISOU 2490 C LYS A1238 7477 4703 5693 -747 -74 -765 C ATOM 2491 O LYS A1238 30.505-115.487 134.394 1.00 49.91 O ANISOU 2491 O LYS A1238 7723 5135 6107 -941 -121 -732 O ATOM 2492 CB LYS A1238 33.515-115.305 133.057 1.00 60.13 C ANISOU 2492 CB LYS A1238 9101 6523 7223 -401 -40 -805 C ATOM 2493 CG LYS A1238 32.609-115.231 131.839 1.00 66.97 C ANISOU 2493 CG LYS A1238 9956 7437 8052 -550 -117 -820 C ATOM 2494 CD LYS A1238 33.361-115.584 130.567 1.00 71.44 C ANISOU 2494 CD LYS A1238 10644 8038 8462 -402 -129 -883 C ATOM 2495 CE LYS A1238 32.450-115.517 129.353 1.00 76.68 C ANISOU 2495 CE LYS A1238 11303 8756 9078 -558 -213 -899 C ATOM 2496 NZ LYS A1238 33.181-115.837 128.097 1.00 83.39 N ANISOU 2496 NZ LYS A1238 12271 9653 9759 -405 -222 -964 N ATOM 2497 N SER A1239 31.937-117.014 135.222 1.00 46.49 N ANISOU 2497 N SER A1239 7673 4444 5546 -721 -74 -808 N ATOM 2498 CA SER A1239 30.858-117.920 135.598 1.00 53.80 C ANISOU 2498 CA SER A1239 8764 5227 6450 -956 -131 -812 C ATOM 2499 C SER A1239 30.030-117.343 136.741 1.00 56.13 C ANISOU 2499 C SER A1239 8851 5598 6878 -1106 -100 -729 C ATOM 2500 O SER A1239 28.804-117.499 136.766 1.00 59.68 O ANISOU 2500 O SER A1239 9263 6067 7344 -1351 -149 -698 O ATOM 2501 CB SER A1239 31.429-119.285 135.981 1.00 55.24 C ANISOU 2501 CB SER A1239 9306 5167 6514 -877 -138 -869 C ATOM 2502 OG SER A1239 30.393-120.201 136.292 1.00 62.90 O ANISOU 2502 OG SER A1239 10465 5984 7449 -1137 -205 -865 O ATOM 2503 N LEU A1240 30.682-116.667 137.690 1.00 52.89 N ANISOU 2503 N LEU A1240 8298 5247 6551 -962 -20 -691 N ATOM 2504 CA LEU A1240 29.961-116.084 138.818 1.00 51.49 C ANISOU 2504 CA LEU A1240 7933 5146 6486 -1071 17 -621 C ATOM 2505 C LEU A1240 29.008-114.987 138.357 1.00 52.66 C ANISOU 2505 C LEU A1240 7805 5484 6720 -1176 0 -576 C ATOM 2506 O LEU A1240 27.827-114.980 138.722 1.00 50.99 O ANISOU 2506 O LEU A1240 7502 5331 6542 -1365 -17 -532 O ATOM 2507 CB LEU A1240 30.952-115.535 139.844 1.00 46.61 C ANISOU 2507 CB LEU A1240 7234 4553 5924 -882 98 -602 C ATOM 2508 CG LEU A1240 30.329-114.757 141.002 1.00 47.23 C ANISOU 2508 CG LEU A1240 7109 4726 6111 -952 145 -540 C ATOM 2509 CD1 LEU A1240 29.649-115.707 141.975 1.00 51.39 C ANISOU 2509 CD1 LEU A1240 7767 5152 6609 -1106 146 -517 C ATOM 2510 CD2 LEU A1240 31.376-113.905 141.703 1.00 52.57 C ANISOU 2510 CD2 LEU A1240 7673 5460 6841 -763 208 -529 C ATOM 2511 N LEU A1241 29.510-114.041 137.558 1.00 48.09 N ANISOU 2511 N LEU A1241 7086 5015 6169 -1049 4 -578 N ATOM 2512 CA LEU A1241 28.662-112.955 137.078 1.00 49.61 C ANISOU 2512 CA LEU A1241 7035 5376 6438 -1117 -16 -530 C ATOM 2513 C LEU A1241 27.542-113.471 136.187 1.00 53.84 C ANISOU 2513 C LEU A1241 7597 5941 6916 -1317 -100 -532 C ATOM 2514 O LEU A1241 26.466-112.865 136.129 1.00 53.06 O ANISOU 2514 O LEU A1241 7303 5985 6873 -1427 -120 -478 O ATOM 2515 CB LEU A1241 29.504-111.920 136.331 1.00 46.76 C ANISOU 2515 CB LEU A1241 6559 5105 6101 -953 -5 -523 C ATOM 2516 CG LEU A1241 30.541-111.165 137.166 1.00 46.35 C ANISOU 2516 CG LEU A1241 6434 5065 6111 -789 65 -505 C ATOM 2517 CD1 LEU A1241 31.358-110.225 136.293 1.00 43.11 C ANISOU 2517 CD1 LEU A1241 5926 4749 5704 -669 62 -487 C ATOM 2518 CD2 LEU A1241 29.866-110.404 138.299 1.00 42.06 C ANISOU 2518 CD2 LEU A1241 5736 4570 5675 -828 101 -459 C ATOM 2519 N SER A1242 27.773-114.584 135.486 1.00 58.74 N ANISOU 2519 N SER A1242 8465 6436 7418 -1359 -153 -595 N ATOM 2520 CA SER A1242 26.722-115.167 134.660 1.00 63.15 C ANISOU 2520 CA SER A1242 9080 7011 7905 -1579 -247 -603 C ATOM 2521 C SER A1242 25.616-115.770 135.518 1.00 63.17 C ANISOU 2521 C SER A1242 9091 6997 7912 -1817 -266 -560 C ATOM 2522 O SER A1242 24.438-115.714 135.147 1.00 63.16 O ANISOU 2522 O SER A1242 8971 7124 7903 -2022 -327 -518 O ATOM 2523 CB SER A1242 27.316-116.219 133.724 1.00 67.85 C ANISOU 2523 CB SER A1242 9977 7450 8353 -1551 -301 -694 C ATOM 2524 OG SER A1242 26.325-116.768 132.874 1.00 76.28 O ANISOU 2524 OG SER A1242 11116 8528 9338 -1780 -405 -708 O ATOM 2525 N LYS A1243 25.976-116.348 136.669 1.00 63.82 N ANISOU 2525 N LYS A1243 9304 6946 7998 -1799 -216 -560 N ATOM 2526 CA LYS A1243 24.968-116.864 137.589 1.00 65.61 C ANISOU 2526 CA LYS A1243 9523 7178 8227 -2027 -223 -503 C ATOM 2527 C LYS A1243 24.066-115.746 138.092 1.00 65.11 C ANISOU 2527 C LYS A1243 9107 7362 8271 -2065 -182 -419 C ATOM 2528 O LYS A1243 22.863-115.949 138.286 1.00 68.11 O ANISOU 2528 O LYS A1243 9383 7860 8636 -2294 -215 -358 O ATOM 2529 CB LYS A1243 25.643-117.577 138.760 1.00 72.27 C ANISOU 2529 CB LYS A1243 10564 7838 9055 -1964 -168 -511 C ATOM 2530 CG LYS A1243 26.474-118.791 138.376 1.00 77.84 C ANISOU 2530 CG LYS A1243 11651 8284 9640 -1910 -209 -591 C ATOM 2531 CD LYS A1243 25.613-119.920 137.834 1.00 82.89 C ANISOU 2531 CD LYS A1243 12517 8811 10165 -2195 -319 -603 C ATOM 2532 CE LYS A1243 26.450-121.161 137.557 1.00 82.03 C ANISOU 2532 CE LYS A1243 12836 8408 9925 -2114 -359 -689 C ATOM 2533 NZ LYS A1243 25.623-122.310 137.096 1.00 81.28 N ANISOU 2533 NZ LYS A1243 13015 8162 9707 -2415 -479 -705 N ATOM 2534 N PHE A1244 24.629-114.559 138.313 1.00 66.22 N ANISOU 2534 N PHE A1244 9064 7588 8508 -1840 -112 -411 N ATOM 2535 CA PHE A1244 23.858-113.399 138.737 1.00 67.69 C ANISOU 2535 CA PHE A1244 8941 7989 8788 -1822 -72 -343 C ATOM 2536 C PHE A1244 23.202-112.666 137.574 1.00 73.20 C ANISOU 2536 C PHE A1244 9458 8858 9496 -1843 -131 -319 C ATOM 2537 O PHE A1244 22.474-111.696 137.808 1.00 80.34 O ANISOU 2537 O PHE A1244 10110 9949 10466 -1812 -108 -260 O ATOM 2538 CB PHE A1244 24.756-112.435 139.518 1.00 65.01 C ANISOU 2538 CB PHE A1244 8524 7640 8539 -1581 17 -349 C ATOM 2539 CG PHE A1244 25.269-113.002 140.813 1.00 66.27 C ANISOU 2539 CG PHE A1244 8810 7676 8691 -1555 79 -356 C ATOM 2540 CD1 PHE A1244 24.443-113.754 141.631 1.00 66.72 C ANISOU 2540 CD1 PHE A1244 8895 7742 8713 -1739 85 -316 C ATOM 2541 CD2 PHE A1244 26.580-112.790 141.207 1.00 61.41 C ANISOU 2541 CD2 PHE A1244 8280 6955 8096 -1356 127 -394 C ATOM 2542 CE1 PHE A1244 24.912-114.277 142.822 1.00 63.60 C ANISOU 2542 CE1 PHE A1244 8624 7237 8306 -1715 140 -314 C ATOM 2543 CE2 PHE A1244 27.054-113.312 142.396 1.00 56.65 C ANISOU 2543 CE2 PHE A1244 7791 6252 7480 -1326 178 -396 C ATOM 2544 CZ PHE A1244 26.219-114.057 143.204 1.00 56.71 C ANISOU 2544 CZ PHE A1244 7840 6254 7455 -1500 185 -357 C ATOM 2545 N GLY A1245 23.438-113.099 136.340 1.00 68.94 N ANISOU 2545 N GLY A1245 9047 8265 8884 -1880 -207 -363 N ATOM 2546 CA GLY A1245 22.825-112.462 135.190 1.00 67.36 C ANISOU 2546 CA GLY A1245 8685 8228 8678 -1908 -271 -336 C ATOM 2547 C GLY A1245 23.490-111.176 134.756 1.00 69.59 C ANISOU 2547 C GLY A1245 8840 8566 9034 -1675 -238 -329 C ATOM 2548 O GLY A1245 22.797-110.204 134.427 1.00 72.80 O ANISOU 2548 O GLY A1245 9024 9148 9488 -1648 -254 -269 O ATOM 2549 N MET A1246 24.820-111.138 134.744 1.00 66.61 N ANISOU 2549 N MET A1246 8600 8051 8659 -1506 -198 -380 N ATOM 2550 CA MET A1246 25.568-109.949 134.366 1.00 59.84 C ANISOU 2550 CA MET A1246 7640 7237 7860 -1311 -171 -364 C ATOM 2551 C MET A1246 26.686-110.328 133.406 1.00 55.85 C ANISOU 2551 C MET A1246 7300 6648 7273 -1227 -189 -420 C ATOM 2552 O MET A1246 27.088-111.490 133.311 1.00 50.54 O ANISOU 2552 O MET A1246 6845 5849 6509 -1262 -202 -484 O ATOM 2553 CB MET A1246 26.164-109.239 135.591 1.00 60.31 C ANISOU 2553 CB MET A1246 7643 7260 8014 -1169 -84 -349 C ATOM 2554 CG MET A1246 25.151-108.820 136.643 1.00 57.81 C ANISOU 2554 CG MET A1246 7169 7031 7766 -1212 -49 -302 C ATOM 2555 SD MET A1246 25.934-108.062 138.081 1.00 57.95 S ANISOU 2555 SD MET A1246 7164 6985 7869 -1046 46 -303 S ATOM 2556 CE MET A1246 24.506-107.745 139.116 1.00 63.12 C ANISOU 2556 CE MET A1246 7638 7778 8567 -1107 80 -253 C ATOM 2557 N ASP A1247 27.183-109.323 132.690 1.00 59.16 N ANISOU 2557 N ASP A1247 7621 7142 7716 -1107 -191 -390 N ATOM 2558 CA ASP A1247 28.350-109.502 131.845 1.00 66.13 C ANISOU 2558 CA ASP A1247 8619 7989 8518 -1000 -192 -429 C ATOM 2559 C ASP A1247 29.623-109.329 132.669 1.00 57.21 C ANISOU 2559 C ASP A1247 7531 6789 7417 -847 -114 -439 C ATOM 2560 O ASP A1247 29.588-108.984 133.851 1.00 58.97 O ANISOU 2560 O ASP A1247 7696 6983 7727 -828 -66 -419 O ATOM 2561 CB ASP A1247 28.331-108.514 130.681 1.00 82.26 C ANISOU 2561 CB ASP A1247 10534 10161 10558 -960 -231 -377 C ATOM 2562 CG ASP A1247 27.125-108.693 129.783 1.00 96.90 C ANISOU 2562 CG ASP A1247 12342 12109 12368 -1104 -317 -363 C ATOM 2563 OD1 ASP A1247 26.637-109.838 129.658 1.00103.12 O ANISOU 2563 OD1 ASP A1247 13261 12843 13075 -1237 -358 -418 O ATOM 2564 OD2 ASP A1247 26.666-107.688 129.200 1.00101.24 O ANISOU 2564 OD2 ASP A1247 12729 12783 12954 -1090 -350 -292 O ATOM 2565 N GLU A1248 30.762-109.570 132.026 1.00 56.82 N ANISOU 2565 N GLU A1248 7574 6732 7282 -735 -102 -470 N ATOM 2566 CA GLU A1248 32.043-109.442 132.705 1.00 60.97 C ANISOU 2566 CA GLU A1248 8123 7231 7813 -590 -35 -471 C ATOM 2567 C GLU A1248 32.340-107.984 133.033 1.00 61.45 C ANISOU 2567 C GLU A1248 7997 7373 7978 -545 -13 -393 C ATOM 2568 O GLU A1248 32.034-107.076 132.255 1.00 57.33 O ANISOU 2568 O GLU A1248 7361 6941 7480 -566 -48 -338 O ATOM 2569 CB GLU A1248 33.164-110.027 131.846 1.00 69.12 C ANISOU 2569 CB GLU A1248 9274 8282 8708 -467 -27 -514 C ATOM 2570 CG GLU A1248 33.334-111.530 131.986 1.00 79.63 C ANISOU 2570 CG GLU A1248 10849 9476 9931 -440 -27 -603 C ATOM 2571 CD GLU A1248 34.464-112.069 131.131 1.00 92.97 C ANISOU 2571 CD GLU A1248 12656 11200 11470 -274 -11 -650 C ATOM 2572 OE1 GLU A1248 34.600-111.623 129.972 1.00 97.81 O ANISOU 2572 OE1 GLU A1248 13203 11935 12026 -255 -33 -633 O ATOM 2573 OE2 GLU A1248 35.224-112.932 131.620 1.00 98.30 O ANISOU 2573 OE2 GLU A1248 13487 11791 12072 -147 26 -699 O ATOM 2574 N GLY A1249 32.940-107.767 134.196 1.00 58.34 N ANISOU 2574 N GLY A1249 7592 6939 7637 -487 39 -386 N ATOM 2575 CA GLY A1249 33.291-106.427 134.628 1.00 50.19 C ANISOU 2575 CA GLY A1249 6424 5955 6693 -455 54 -321 C ATOM 2576 C GLY A1249 34.039-106.492 135.940 1.00 44.71 C ANISOU 2576 C GLY A1249 5755 5209 6024 -398 106 -333 C ATOM 2577 O GLY A1249 34.102-107.536 136.598 1.00 47.95 O ANISOU 2577 O GLY A1249 6276 5543 6399 -384 133 -383 O ATOM 2578 N VAL A1250 34.618-105.351 136.309 1.00 40.59 N ANISOU 2578 N VAL A1250 5143 4725 5556 -372 113 -280 N ATOM 2579 CA VAL A1250 35.354-105.254 137.565 1.00 39.69 C ANISOU 2579 CA VAL A1250 5038 4580 5463 -330 153 -285 C ATOM 2580 C VAL A1250 34.367-105.386 138.717 1.00 36.22 C ANISOU 2580 C VAL A1250 4615 4052 5097 -371 173 -315 C ATOM 2581 O VAL A1250 33.478-104.545 138.892 1.00 43.99 O ANISOU 2581 O VAL A1250 5528 5028 6160 -410 158 -293 O ATOM 2582 CB VAL A1250 36.135-103.938 137.642 1.00 39.79 C ANISOU 2582 CB VAL A1250 4963 4649 5508 -328 139 -220 C ATOM 2583 CG1 VAL A1250 37.123-103.977 138.798 1.00 33.55 C ANISOU 2583 CG1 VAL A1250 4185 3857 4704 -289 171 -225 C ATOM 2584 CG2 VAL A1250 36.850-103.687 136.327 1.00 43.37 C ANISOU 2584 CG2 VAL A1250 5374 5217 5888 -317 114 -171 C ATOM 2585 N THR A1251 34.517-106.447 139.503 1.00 32.84 N ANISOU 2585 N THR A1251 4281 3564 4631 -352 208 -359 N ATOM 2586 CA THR A1251 33.529-106.826 140.504 1.00 40.16 C ANISOU 2586 CA THR A1251 5234 4424 5602 -407 230 -382 C ATOM 2587 C THR A1251 33.987-106.408 141.896 1.00 42.69 C ANISOU 2587 C THR A1251 5543 4722 5956 -368 268 -381 C ATOM 2588 O THR A1251 35.107-106.726 142.311 1.00 26.91 O ANISOU 2588 O THR A1251 3592 2725 3908 -301 286 -387 O ATOM 2589 CB THR A1251 33.274-108.332 140.466 1.00 40.81 C ANISOU 2589 CB THR A1251 5458 4437 5610 -437 235 -424 C ATOM 2590 OG1 THR A1251 32.852-108.709 139.149 1.00 42.38 O ANISOU 2590 OG1 THR A1251 5683 4654 5764 -482 190 -434 O ATOM 2591 CG2 THR A1251 32.195-108.714 141.468 1.00 35.91 C ANISOU 2591 CG2 THR A1251 4850 3770 5026 -525 256 -430 C ATOM 2592 N PHE A1252 33.113-105.701 142.606 1.00 31.88 N ANISOU 2592 N PHE A1252 4108 3345 4660 -400 279 -375 N ATOM 2593 CA PHE A1252 33.325-105.315 143.993 1.00 26.73 C ANISOU 2593 CA PHE A1252 3456 2668 4032 -371 314 -385 C ATOM 2594 C PHE A1252 32.304-106.030 144.868 1.00 34.92 C ANISOU 2594 C PHE A1252 4517 3680 5070 -419 353 -403 C ATOM 2595 O PHE A1252 31.138-106.170 144.484 1.00 38.37 O ANISOU 2595 O PHE A1252 4907 4146 5525 -483 346 -395 O ATOM 2596 CB PHE A1252 33.197-103.799 144.167 1.00 33.02 C ANISOU 2596 CB PHE A1252 4176 3475 4896 -351 297 -366 C ATOM 2597 CG PHE A1252 34.134-103.004 143.299 1.00 26.51 C ANISOU 2597 CG PHE A1252 3329 2677 4067 -339 251 -330 C ATOM 2598 CD1 PHE A1252 33.793-102.688 141.992 1.00 38.16 C ANISOU 2598 CD1 PHE A1252 4760 4187 5552 -358 211 -297 C ATOM 2599 CD2 PHE A1252 35.351-102.564 143.792 1.00 26.37 C ANISOU 2599 CD2 PHE A1252 3327 2667 4027 -322 243 -319 C ATOM 2600 CE1 PHE A1252 34.651-101.955 141.193 1.00 30.69 C ANISOU 2600 CE1 PHE A1252 3791 3277 4593 -361 170 -251 C ATOM 2601 CE2 PHE A1252 36.214-101.831 142.998 1.00 35.22 C ANISOU 2601 CE2 PHE A1252 4415 3834 5133 -339 199 -270 C ATOM 2602 CZ PHE A1252 35.863-101.526 141.697 1.00 30.50 C ANISOU 2602 CZ PHE A1252 3779 3266 4545 -359 165 -234 C ATOM 2603 N MET A1253 32.740-106.485 146.043 1.00 30.05 N ANISOU 2603 N MET A1253 3964 3029 4425 -397 391 -419 N ATOM 2604 CA MET A1253 31.879-107.234 146.947 1.00 31.40 C ANISOU 2604 CA MET A1253 4167 3184 4581 -453 431 -424 C ATOM 2605 C MET A1253 31.896-106.620 148.339 1.00 34.35 C ANISOU 2605 C MET A1253 4514 3567 4969 -412 473 -433 C ATOM 2606 O MET A1253 32.942-106.179 148.825 1.00 34.21 O ANISOU 2606 O MET A1253 4520 3536 4941 -347 470 -443 O ATOM 2607 CB MET A1253 32.297-108.714 147.038 1.00 32.10 C ANISOU 2607 CB MET A1253 4403 3202 4592 -474 436 -429 C ATOM 2608 CG MET A1253 31.598-109.479 148.161 1.00 45.25 C ANISOU 2608 CG MET A1253 6122 4842 6229 -544 478 -420 C ATOM 2609 SD MET A1253 32.000-111.234 148.249 1.00 54.98 S ANISOU 2609 SD MET A1253 7576 5950 7363 -574 471 -418 S ATOM 2610 CE MET A1253 33.752-111.175 147.931 1.00 47.63 C ANISOU 2610 CE MET A1253 6702 5001 6393 -399 455 -438 C ATOM 2611 N PHE A1254 30.723-106.592 148.969 1.00 32.34 N ANISOU 2611 N PHE A1254 4205 3356 4726 -455 510 -428 N ATOM 2612 CA PHE A1254 30.572-106.285 150.383 1.00 30.69 C ANISOU 2612 CA PHE A1254 3990 3166 4506 -421 562 -441 C ATOM 2613 C PHE A1254 29.870-107.450 151.064 1.00 38.63 C ANISOU 2613 C PHE A1254 5033 4186 5458 -510 604 -418 C ATOM 2614 O PHE A1254 28.906-108.004 150.524 1.00 38.97 O ANISOU 2614 O PHE A1254 5041 4270 5497 -611 599 -390 O ATOM 2615 CB PHE A1254 29.767-104.996 150.591 1.00 33.38 C ANISOU 2615 CB PHE A1254 4220 3570 4893 -363 576 -453 C ATOM 2616 CG PHE A1254 29.417-104.715 152.029 1.00 32.41 C ANISOU 2616 CG PHE A1254 4089 3483 4740 -320 636 -473 C ATOM 2617 CD1 PHE A1254 30.268-103.973 152.832 1.00 34.15 C ANISOU 2617 CD1 PHE A1254 4367 3656 4952 -242 635 -512 C ATOM 2618 CD2 PHE A1254 28.228-105.181 152.574 1.00 36.32 C ANISOU 2618 CD2 PHE A1254 4516 4078 5205 -366 692 -450 C ATOM 2619 CE1 PHE A1254 29.946-103.711 154.153 1.00 36.30 C ANISOU 2619 CE1 PHE A1254 4645 3966 5183 -195 689 -539 C ATOM 2620 CE2 PHE A1254 27.903-104.924 153.893 1.00 35.47 C ANISOU 2620 CE2 PHE A1254 4396 4025 5054 -316 755 -468 C ATOM 2621 CZ PHE A1254 28.763-104.187 154.683 1.00 35.91 C ANISOU 2621 CZ PHE A1254 4525 4019 5100 -222 755 -518 C ATOM 2622 N ILE A1255 30.353-107.823 152.246 1.00 38.96 N ANISOU 2622 N ILE A1255 5149 4203 5452 -489 640 -422 N ATOM 2623 CA ILE A1255 29.718-108.859 153.054 1.00 34.29 C ANISOU 2623 CA ILE A1255 4604 3625 4801 -580 683 -389 C ATOM 2624 C ILE A1255 29.806-108.447 154.516 1.00 34.83 C ANISOU 2624 C ILE A1255 4664 3735 4836 -522 738 -401 C ATOM 2625 O ILE A1255 30.894-108.152 155.021 1.00 38.01 O ANISOU 2625 O ILE A1255 5125 4092 5223 -436 729 -428 O ATOM 2626 CB ILE A1255 30.348-110.250 152.824 1.00 29.99 C ANISOU 2626 CB ILE A1255 4229 2966 4199 -630 657 -368 C ATOM 2627 CG1 ILE A1255 29.648-111.304 153.682 1.00 33.66 C ANISOU 2627 CG1 ILE A1255 4764 3428 4596 -749 694 -320 C ATOM 2628 CG2 ILE A1255 31.856-110.239 153.078 1.00 29.33 C ANISOU 2628 CG2 ILE A1255 4236 2816 4091 -507 639 -391 C ATOM 2629 CD1 ILE A1255 30.119-112.718 153.411 1.00 36.93 C ANISOU 2629 CD1 ILE A1255 5385 3700 4947 -802 659 -297 C ATOM 2630 N GLY A1256 28.666-108.397 155.186 1.00 33.53 N ANISOU 2630 N GLY A1256 4414 3678 4649 -567 794 -379 N ATOM 2631 CA GLY A1256 28.643-108.011 156.581 1.00 37.73 C ANISOU 2631 CA GLY A1256 4937 4267 5133 -507 853 -394 C ATOM 2632 C GLY A1256 27.266-107.556 157.014 1.00 41.85 C ANISOU 2632 C GLY A1256 5311 4953 5639 -513 916 -380 C ATOM 2633 O GLY A1256 26.322-107.492 156.227 1.00 37.87 O ANISOU 2633 O GLY A1256 4694 4530 5165 -565 911 -354 O ATOM 2634 N ARG A1257 27.184-107.235 158.302 1.00 41.96 N ANISOU 2634 N ARG A1257 5319 5031 5592 -450 977 -398 N ATOM 2635 CA ARG A1257 25.936-106.800 158.913 1.00 41.76 C ANISOU 2635 CA ARG A1257 5151 5193 5525 -422 1054 -386 C ATOM 2636 C ARG A1257 25.486-105.462 158.334 1.00 40.66 C ANISOU 2636 C ARG A1257 4904 5099 5444 -282 1044 -437 C ATOM 2637 O ARG A1257 26.302-104.570 158.083 1.00 38.42 O ANISOU 2637 O ARG A1257 4690 4697 5210 -174 996 -502 O ATOM 2638 CB ARG A1257 26.130-106.687 160.426 1.00 40.57 C ANISOU 2638 CB ARG A1257 5045 5088 5283 -359 1118 -407 C ATOM 2639 CG ARG A1257 24.884-106.456 161.262 1.00 46.06 C ANISOU 2639 CG ARG A1257 5599 6004 5897 -330 1214 -385 C ATOM 2640 CD ARG A1257 25.266-106.591 162.733 1.00 47.36 C ANISOU 2640 CD ARG A1257 5844 6193 5958 -293 1270 -399 C ATOM 2641 NE ARG A1257 24.141-106.493 163.659 1.00 49.60 N ANISOU 2641 NE ARG A1257 5999 6710 6139 -267 1374 -371 N ATOM 2642 CZ ARG A1257 23.880-105.424 164.404 1.00 53.75 C ANISOU 2642 CZ ARG A1257 6486 7328 6610 -79 1429 -447 C ATOM 2643 NH1 ARG A1257 24.655-104.351 164.323 1.00 52.50 N ANISOU 2643 NH1 ARG A1257 6427 7023 6497 76 1379 -555 N ATOM 2644 NH2 ARG A1257 22.841-105.426 165.229 1.00 61.83 N ANISOU 2644 NH2 ARG A1257 7379 8593 7522 -48 1532 -414 N ATOM 2645 N PHE A1258 24.178-105.325 158.118 1.00 39.00 N ANISOU 2645 N PHE A1258 4526 5071 5221 -288 1085 -399 N ATOM 2646 CA PHE A1258 23.597-104.073 157.632 1.00 41.63 C ANISOU 2646 CA PHE A1258 4752 5469 5594 -127 1083 -437 C ATOM 2647 C PHE A1258 23.207-103.232 158.841 1.00 41.14 C ANISOU 2647 C PHE A1258 4663 5511 5458 49 1162 -488 C ATOM 2648 O PHE A1258 22.130-103.412 159.416 1.00 43.47 O ANISOU 2648 O PHE A1258 4815 6029 5675 57 1244 -447 O ATOM 2649 CB PHE A1258 22.395-104.336 156.729 1.00 46.86 C ANISOU 2649 CB PHE A1258 5234 6301 6270 -203 1081 -365 C ATOM 2650 CG PHE A1258 22.751-104.873 155.366 1.00 43.67 C ANISOU 2650 CG PHE A1258 4868 5785 5941 -336 991 -336 C ATOM 2651 CD1 PHE A1258 24.073-105.040 154.984 1.00 43.58 C ANISOU 2651 CD1 PHE A1258 5032 5550 5978 -356 926 -373 C ATOM 2652 CD2 PHE A1258 21.754-105.200 154.460 1.00 51.74 C ANISOU 2652 CD2 PHE A1258 5742 6947 6969 -437 970 -270 C ATOM 2653 CE1 PHE A1258 24.391-105.533 153.729 1.00 44.06 C ANISOU 2653 CE1 PHE A1258 5130 5523 6090 -457 851 -352 C ATOM 2654 CE2 PHE A1258 22.066-105.690 153.206 1.00 48.44 C ANISOU 2654 CE2 PHE A1258 5372 6427 6604 -555 885 -252 C ATOM 2655 CZ PHE A1258 23.385-105.858 152.840 1.00 46.39 C ANISOU 2655 CZ PHE A1258 5298 5939 6390 -557 830 -296 C ATOM 2656 N ASP A1259 24.085-102.309 159.231 1.00 40.48 N ANISOU 2656 N ASP A1259 4718 5276 5386 186 1136 -578 N ATOM 2657 CA ASP A1259 23.850-101.432 160.370 1.00 48.13 C ANISOU 2657 CA ASP A1259 5710 6303 6275 368 1199 -649 C ATOM 2658 C ASP A1259 24.237-100.007 159.997 1.00 53.55 C ANISOU 2658 C ASP A1259 6495 6841 7012 544 1140 -736 C ATOM 2659 O ASP A1259 24.835 -99.756 158.947 1.00 58.23 O ANISOU 2659 O ASP A1259 7141 7286 7699 502 1051 -733 O ATOM 2660 CB ASP A1259 24.622-101.901 161.610 1.00 47.60 C ANISOU 2660 CB ASP A1259 5766 6190 6129 324 1225 -673 C ATOM 2661 CG ASP A1259 26.031-102.345 161.284 1.00 52.94 C ANISOU 2661 CG ASP A1259 6593 6662 6862 208 1139 -675 C ATOM 2662 OD1 ASP A1259 26.815-101.516 160.779 1.00 54.39 O ANISOU 2662 OD1 ASP A1259 6869 6689 7107 264 1062 -730 O ATOM 2663 OD2 ASP A1259 26.355-103.525 161.534 1.00 56.86 O ANISOU 2663 OD2 ASP A1259 7115 7159 7331 64 1146 -616 O ATOM 2664 N ARG A1260 23.901 -99.066 160.880 1.00 55.23 N ANISOU 2664 N ARG A1260 6748 7089 7149 741 1188 -813 N ATOM 2665 CA ARG A1260 23.970 -97.651 160.533 1.00 72.69 C ANISOU 2665 CA ARG A1260 9059 9170 9390 930 1137 -890 C ATOM 2666 C ARG A1260 25.321 -97.013 160.838 1.00 78.77 C ANISOU 2666 C ARG A1260 10068 9690 10172 919 1054 -971 C ATOM 2667 O ARG A1260 25.787 -96.169 160.065 1.00 84.19 O ANISOU 2667 O ARG A1260 10856 10204 10928 949 965 -995 O ATOM 2668 CB ARG A1260 22.859 -96.881 161.251 1.00 78.28 C ANISOU 2668 CB ARG A1260 9710 10034 9997 1181 1226 -939 C ATOM 2669 CG ARG A1260 21.468 -97.206 160.734 1.00 87.18 C ANISOU 2669 CG ARG A1260 10579 11430 11116 1223 1291 -853 C ATOM 2670 CD ARG A1260 20.449 -96.166 161.164 1.00 94.70 C ANISOU 2670 CD ARG A1260 11484 12519 11979 1533 1360 -906 C ATOM 2671 NE ARG A1260 19.173 -96.349 160.478 1.00 96.61 N ANISOU 2671 NE ARG A1260 11462 13028 12220 1583 1403 -814 N ATOM 2672 CZ ARG A1260 18.908 -95.885 159.261 1.00 94.06 C ANISOU 2672 CZ ARG A1260 11093 12663 11983 1632 1334 -781 C ATOM 2673 NH1 ARG A1260 17.720 -96.099 158.712 1.00101.41 N ANISOU 2673 NH1 ARG A1260 11764 13872 12896 1670 1373 -691 N ATOM 2674 NH2 ARG A1260 19.831 -95.208 158.593 1.00 86.03 N ANISOU 2674 NH2 ARG A1260 10283 11343 11063 1633 1224 -828 N ATOM 2675 N GLY A1261 25.966 -97.385 161.940 1.00 68.90 N ANISOU 2675 N GLY A1261 8907 8425 8846 863 1074 -1005 N ATOM 2676 CA GLY A1261 27.220 -96.745 162.291 1.00 64.40 C ANISOU 2676 CA GLY A1261 8549 7649 8270 841 989 -1079 C ATOM 2677 C GLY A1261 28.336 -97.692 162.677 1.00 65.17 C ANISOU 2677 C GLY A1261 8688 7718 8357 656 961 -1047 C ATOM 2678 O GLY A1261 29.170 -97.359 163.525 1.00 64.22 O ANISOU 2678 O GLY A1261 8711 7518 8171 649 927 -1109 O ATOM 2679 N GLN A1262 28.377 -98.872 162.058 1.00 60.21 N ANISOU 2679 N GLN A1262 7944 7151 7782 511 968 -951 N ATOM 2680 CA GLN A1262 29.349 -99.887 162.445 1.00 49.97 C ANISOU 2680 CA GLN A1262 6684 5840 6461 367 951 -912 C ATOM 2681 C GLN A1262 30.034-100.508 161.232 1.00 46.49 C ANISOU 2681 C GLN A1262 6218 5329 6115 238 881 -844 C ATOM 2682 O GLN A1262 31.181-100.168 160.922 1.00 49.81 O ANISOU 2682 O GLN A1262 6724 5639 6564 194 797 -857 O ATOM 2683 CB GLN A1262 28.667-100.967 163.289 1.00 52.64 C ANISOU 2683 CB GLN A1262 6941 6342 6718 333 1051 -862 C ATOM 2684 CG GLN A1262 28.044-100.435 164.573 1.00 59.27 C ANISOU 2684 CG GLN A1262 7799 7283 7439 466 1130 -927 C ATOM 2685 CD GLN A1262 26.939-101.324 165.105 1.00 67.10 C ANISOU 2685 CD GLN A1262 8651 8486 8358 443 1243 -858 C ATOM 2686 OE1 GLN A1262 27.173-102.475 165.474 1.00 72.37 O ANISOU 2686 OE1 GLN A1262 9312 9193 8990 310 1263 -786 O ATOM 2687 NE2 GLN A1262 25.721-100.793 165.143 1.00 65.35 N ANISOU 2687 NE2 GLN A1262 8316 8409 8105 573 1315 -872 N ATOM 2688 N LYS A1263 29.346-101.418 160.540 1.00 46.10 N ANISOU 2688 N LYS A1263 6054 5358 6106 171 915 -769 N ATOM 2689 CA LYS A1263 29.946-102.112 159.405 1.00 54.32 C ANISOU 2689 CA LYS A1263 7085 6337 7218 61 856 -711 C ATOM 2690 C LYS A1263 30.032-101.246 158.153 1.00 50.33 C ANISOU 2690 C LYS A1263 6565 5756 6803 87 788 -719 C ATOM 2691 O LYS A1263 30.853-101.534 157.275 1.00 44.45 O ANISOU 2691 O LYS A1263 5839 4946 6104 15 726 -688 O ATOM 2692 CB LYS A1263 29.168-103.394 159.101 1.00 65.30 C ANISOU 2692 CB LYS A1263 8389 7817 8605 -36 903 -633 C ATOM 2693 CG LYS A1263 29.884-104.659 159.549 1.00 70.46 C ANISOU 2693 CG LYS A1263 9118 8445 9209 -131 905 -589 C ATOM 2694 CD LYS A1263 30.468-104.493 160.943 1.00 76.80 C ANISOU 2694 CD LYS A1263 10002 9254 9925 -83 927 -625 C ATOM 2695 CE LYS A1263 31.409-105.632 161.290 1.00 82.34 C ANISOU 2695 CE LYS A1263 10793 9913 10579 -149 909 -579 C ATOM 2696 NZ LYS A1263 32.127-105.382 162.571 1.00 85.54 N ANISOU 2696 NZ LYS A1263 11275 10328 10898 -101 912 -613 N ATOM 2697 N GLY A1264 29.207-100.209 158.046 1.00 43.27 N ANISOU 2697 N GLY A1264 5640 4877 5926 199 800 -755 N ATOM 2698 CA GLY A1264 29.371 -99.220 157.001 1.00 46.94 C ANISOU 2698 CA GLY A1264 6125 5247 6463 236 727 -763 C ATOM 2699 C GLY A1264 28.724 -99.533 155.671 1.00 49.79 C ANISOU 2699 C GLY A1264 6370 5654 6893 201 714 -701 C ATOM 2700 O GLY A1264 29.183 -99.018 154.645 1.00 44.31 O ANISOU 2700 O GLY A1264 5701 4876 6260 184 641 -687 O ATOM 2701 N VAL A1265 27.668-100.351 155.647 1.00 46.27 N ANISOU 2701 N VAL A1265 5798 5350 6432 173 777 -658 N ATOM 2702 CA VAL A1265 26.979-100.587 154.381 1.00 44.09 C ANISOU 2702 CA VAL A1265 5410 5132 6211 132 756 -601 C ATOM 2703 C VAL A1265 26.313 -99.306 153.893 1.00 48.98 C ANISOU 2703 C VAL A1265 5994 5754 6864 280 736 -618 C ATOM 2704 O VAL A1265 26.112 -99.124 152.687 1.00 52.43 O ANISOU 2704 O VAL A1265 6380 6186 7356 265 685 -579 O ATOM 2705 CB VAL A1265 25.966-101.741 154.513 1.00 41.94 C ANISOU 2705 CB VAL A1265 5013 5022 5900 40 818 -545 C ATOM 2706 CG1 VAL A1265 24.751-101.309 155.322 1.00 34.17 C ANISOU 2706 CG1 VAL A1265 3919 4205 4860 154 899 -552 C ATOM 2707 CG2 VAL A1265 25.550-102.242 153.136 1.00 37.60 C ANISOU 2707 CG2 VAL A1265 4379 4508 5398 -59 773 -486 C ATOM 2708 N ASP A1266 25.975 -98.396 154.811 1.00 46.50 N ANISOU 2708 N ASP A1266 5721 5443 6506 438 773 -676 N ATOM 2709 CA ASP A1266 25.393 -97.120 154.410 1.00 42.28 C ANISOU 2709 CA ASP A1266 5191 4881 5991 613 749 -697 C ATOM 2710 C ASP A1266 26.400 -96.273 153.641 1.00 42.11 C ANISOU 2710 C ASP A1266 5314 4654 6031 597 645 -708 C ATOM 2711 O ASP A1266 26.029 -95.550 152.709 1.00 50.92 O ANISOU 2711 O ASP A1266 6417 5738 7190 670 598 -682 O ATOM 2712 CB ASP A1266 24.885 -96.368 155.639 1.00 50.67 C ANISOU 2712 CB ASP A1266 6301 5976 6974 804 813 -771 C ATOM 2713 CG ASP A1266 25.930 -96.265 156.733 1.00 58.25 C ANISOU 2713 CG ASP A1266 7434 6811 7887 773 807 -841 C ATOM 2714 OD1 ASP A1266 26.699 -97.234 156.917 1.00 57.14 O ANISOU 2714 OD1 ASP A1266 7302 6663 7747 604 803 -817 O ATOM 2715 OD2 ASP A1266 25.986 -95.216 157.407 1.00 61.52 O ANISOU 2715 OD2 ASP A1266 7987 7134 8255 923 802 -922 O ATOM 2716 N VAL A1267 27.678 -96.349 154.018 1.00 40.89 N ANISOU 2716 N VAL A1267 5292 4373 5870 497 605 -735 N ATOM 2717 CA VAL A1267 28.714 -95.621 153.293 1.00 38.71 C ANISOU 2717 CA VAL A1267 5137 3932 5640 442 504 -728 C ATOM 2718 C VAL A1267 28.855 -96.165 151.877 1.00 36.75 C ANISOU 2718 C VAL A1267 4795 3716 5454 333 463 -648 C ATOM 2719 O VAL A1267 29.028 -95.403 150.918 1.00 35.09 O ANISOU 2719 O VAL A1267 4622 3425 5287 341 392 -618 O ATOM 2720 CB VAL A1267 30.046 -95.686 154.062 1.00 32.60 C ANISOU 2720 CB VAL A1267 4490 3068 4829 344 472 -763 C ATOM 2721 CG1 VAL A1267 31.166 -95.059 153.249 1.00 32.50 C ANISOU 2721 CG1 VAL A1267 4569 2928 4852 246 367 -734 C ATOM 2722 CG2 VAL A1267 29.912 -94.996 155.411 1.00 34.25 C ANISOU 2722 CG2 VAL A1267 4818 3229 4965 454 499 -852 C ATOM 2723 N LEU A1268 28.777 -97.487 151.722 1.00 34.13 N ANISOU 2723 N LEU A1268 4357 3493 5116 230 502 -613 N ATOM 2724 CA LEU A1268 28.895 -98.089 150.399 1.00 33.29 C ANISOU 2724 CA LEU A1268 4180 3418 5051 132 465 -549 C ATOM 2725 C LEU A1268 27.711 -97.720 149.514 1.00 39.17 C ANISOU 2725 C LEU A1268 4819 4237 5829 201 458 -512 C ATOM 2726 O LEU A1268 27.888 -97.359 148.345 1.00 37.47 O ANISOU 2726 O LEU A1268 4598 3987 5652 180 395 -470 O ATOM 2727 CB LEU A1268 29.017 -99.606 150.523 1.00 29.83 C ANISOU 2727 CB LEU A1268 3693 3056 4585 17 505 -530 C ATOM 2728 CG LEU A1268 29.003-100.340 149.184 1.00 34.50 C ANISOU 2728 CG LEU A1268 4226 3682 5200 -76 470 -477 C ATOM 2729 CD1 LEU A1268 30.193 -99.921 148.337 1.00 40.21 C ANISOU 2729 CD1 LEU A1268 5013 4319 5944 -109 398 -460 C ATOM 2730 CD2 LEU A1268 28.990-101.837 149.392 1.00 32.05 C ANISOU 2730 CD2 LEU A1268 3908 3421 4850 -179 507 -465 C ATOM 2731 N LEU A1269 26.493 -97.805 150.057 1.00 36.79 N ANISOU 2731 N LEU A1269 4418 4061 5500 286 524 -519 N ATOM 2732 CA LEU A1269 25.306 -97.485 149.271 1.00 38.24 C ANISOU 2732 CA LEU A1269 4472 4358 5701 362 519 -475 C ATOM 2733 C LEU A1269 25.333 -96.040 148.790 1.00 45.05 C ANISOU 2733 C LEU A1269 5414 5107 6594 506 459 -478 C ATOM 2734 O LEU A1269 24.939 -95.751 147.654 1.00 50.64 O ANISOU 2734 O LEU A1269 6062 5843 7335 522 410 -424 O ATOM 2735 CB LEU A1269 24.047 -97.762 150.092 1.00 34.40 C ANISOU 2735 CB LEU A1269 3850 4059 5161 439 607 -477 C ATOM 2736 CG LEU A1269 23.820 -99.230 150.459 1.00 41.05 C ANISOU 2736 CG LEU A1269 4608 5023 5965 272 659 -451 C ATOM 2737 CD1 LEU A1269 22.537 -99.402 151.253 1.00 42.30 C ANISOU 2737 CD1 LEU A1269 4614 5400 6059 337 745 -436 C ATOM 2738 CD2 LEU A1269 23.806-100.099 149.212 1.00 33.40 C ANISOU 2738 CD2 LEU A1269 3581 4086 5024 106 607 -392 C ATOM 2739 N LYS A1270 25.796 -95.118 149.638 1.00 41.47 N ANISOU 2739 N LYS A1270 5115 4517 6125 607 455 -540 N ATOM 2740 CA LYS A1270 25.932 -93.730 149.209 1.00 40.84 C ANISOU 2740 CA LYS A1270 5166 4283 6067 726 384 -543 C ATOM 2741 C LYS A1270 27.018 -93.587 148.149 1.00 44.84 C ANISOU 2741 C LYS A1270 5748 4669 6621 579 291 -494 C ATOM 2742 O LYS A1270 26.877 -92.794 147.210 1.00 52.68 O ANISOU 2742 O LYS A1270 6774 5599 7643 629 226 -447 O ATOM 2743 CB LYS A1270 26.232 -92.834 150.411 1.00 43.82 C ANISOU 2743 CB LYS A1270 5726 4523 6402 843 391 -630 C ATOM 2744 CG LYS A1270 25.328 -91.616 150.527 1.00 52.68 C ANISOU 2744 CG LYS A1270 6914 5601 7501 1098 388 -655 C ATOM 2745 CD LYS A1270 25.466 -90.699 149.324 1.00 61.79 C ANISOU 2745 CD LYS A1270 8154 6620 8704 1124 288 -597 C ATOM 2746 CE LYS A1270 24.482 -89.542 149.393 1.00 70.36 C ANISOU 2746 CE LYS A1270 9310 7664 9760 1412 284 -616 C ATOM 2747 NZ LYS A1270 24.680 -88.713 150.614 1.00 75.05 N ANISOU 2747 NZ LYS A1270 10129 8097 10291 1550 293 -722 N ATOM 2748 N ALA A1271 28.107 -94.349 148.281 1.00 37.45 N ANISOU 2748 N ALA A1271 4836 3713 5682 408 286 -497 N ATOM 2749 CA ALA A1271 29.165 -94.306 147.278 1.00 38.23 C ANISOU 2749 CA ALA A1271 4976 3743 5806 271 210 -444 C ATOM 2750 C ALA A1271 28.695 -94.860 145.940 1.00 42.20 C ANISOU 2750 C ALA A1271 5344 4355 6335 227 195 -374 C ATOM 2751 O ALA A1271 29.141 -94.391 144.887 1.00 40.38 O ANISOU 2751 O ALA A1271 5143 4075 6124 181 126 -317 O ATOM 2752 CB ALA A1271 30.390 -95.076 147.771 1.00 35.99 C ANISOU 2752 CB ALA A1271 4724 3456 5496 130 218 -461 C ATOM 2753 N ILE A1272 27.801 -95.851 145.958 1.00 41.27 N ANISOU 2753 N ILE A1272 5084 4390 6207 224 255 -372 N ATOM 2754 CA ILE A1272 27.271 -96.392 144.711 1.00 39.92 C ANISOU 2754 CA ILE A1272 4792 4327 6048 171 233 -312 C ATOM 2755 C ILE A1272 26.376 -95.369 144.024 1.00 42.59 C ANISOU 2755 C ILE A1272 5095 4679 6407 302 193 -270 C ATOM 2756 O ILE A1272 26.359 -95.268 142.791 1.00 49.86 O ANISOU 2756 O ILE A1272 5981 5622 7342 265 136 -209 O ATOM 2757 CB ILE A1272 26.533 -97.718 144.978 1.00 39.55 C ANISOU 2757 CB ILE A1272 4621 4432 5973 105 295 -319 C ATOM 2758 CG1 ILE A1272 27.524 -98.792 145.431 1.00 41.54 C ANISOU 2758 CG1 ILE A1272 4935 4648 6199 -20 319 -348 C ATOM 2759 CG2 ILE A1272 25.780 -98.180 143.738 1.00 35.46 C ANISOU 2759 CG2 ILE A1272 3981 4035 5455 52 263 -262 C ATOM 2760 CD1 ILE A1272 26.875-100.113 145.777 1.00 44.85 C ANISOU 2760 CD1 ILE A1272 5279 5179 6583 -104 373 -350 C ATOM 2761 N GLU A1273 25.626 -94.587 144.805 1.00 40.71 N ANISOU 2761 N GLU A1273 4870 4434 6162 473 222 -300 N ATOM 2762 CA GLU A1273 24.809 -93.529 144.216 1.00 43.96 C ANISOU 2762 CA GLU A1273 5271 4848 6585 639 182 -259 C ATOM 2763 C GLU A1273 25.677 -92.447 143.589 1.00 47.54 C ANISOU 2763 C GLU A1273 5899 5100 7064 637 91 -228 C ATOM 2764 O GLU A1273 25.360 -91.938 142.508 1.00 52.25 O ANISOU 2764 O GLU A1273 6478 5700 7676 677 31 -158 O ATOM 2765 CB GLU A1273 23.882 -92.924 145.270 1.00 40.93 C ANISOU 2765 CB GLU A1273 4883 4500 6171 856 240 -307 C ATOM 2766 CG GLU A1273 22.842 -93.884 145.820 1.00 43.30 C ANISOU 2766 CG GLU A1273 4979 5042 6432 863 330 -313 C ATOM 2767 CD GLU A1273 21.748 -93.170 146.591 1.00 49.51 C ANISOU 2767 CD GLU A1273 5718 5920 7172 1118 386 -339 C ATOM 2768 OE1 GLU A1273 20.604 -93.672 146.605 1.00 50.99 O ANISOU 2768 OE1 GLU A1273 5690 6361 7323 1158 438 -303 O ATOM 2769 OE2 GLU A1273 22.028 -92.102 147.176 1.00 51.17 O ANISOU 2769 OE2 GLU A1273 6111 5958 7372 1279 375 -393 O ATOM 2770 N ILE A1274 26.775 -92.079 144.254 1.00 50.43 N ANISOU 2770 N ILE A1274 6435 5298 7427 578 75 -272 N ATOM 2771 CA ILE A1274 27.691 -91.088 143.696 1.00 50.44 C ANISOU 2771 CA ILE A1274 6607 5115 7443 527 -18 -231 C ATOM 2772 C ILE A1274 28.257 -91.575 142.369 1.00 55.69 C ANISOU 2772 C ILE A1274 7198 5841 8119 366 -64 -149 C ATOM 2773 O ILE A1274 28.342 -90.816 141.395 1.00 62.12 O ANISOU 2773 O ILE A1274 8068 6592 8945 368 -139 -74 O ATOM 2774 CB ILE A1274 28.809 -90.769 144.707 1.00 47.99 C ANISOU 2774 CB ILE A1274 6468 4653 7113 449 -30 -290 C ATOM 2775 CG1 ILE A1274 28.232 -90.070 145.939 1.00 47.02 C ANISOU 2775 CG1 ILE A1274 6460 4442 6964 631 2 -375 C ATOM 2776 CG2 ILE A1274 29.895 -89.922 144.061 1.00 48.51 C ANISOU 2776 CG2 ILE A1274 6687 4562 7183 325 -132 -229 C ATOM 2777 CD1 ILE A1274 29.249 -89.837 147.035 1.00 46.09 C ANISOU 2777 CD1 ILE A1274 6505 4193 6813 549 -9 -444 C ATOM 2778 N LEU A1275 28.638 -92.851 142.304 1.00 49.93 N ANISOU 2778 N LEU A1275 6357 5234 7379 234 -20 -160 N ATOM 2779 CA LEU A1275 29.215 -93.408 141.089 1.00 43.77 C ANISOU 2779 CA LEU A1275 5515 4524 6592 98 -55 -97 C ATOM 2780 C LEU A1275 28.180 -93.681 140.007 1.00 44.25 C ANISOU 2780 C LEU A1275 5444 4714 6656 138 -67 -46 C ATOM 2781 O LEU A1275 28.553 -93.800 138.835 1.00 43.16 O ANISOU 2781 O LEU A1275 5280 4613 6504 55 -113 17 O ATOM 2782 CB LEU A1275 29.961 -94.705 141.409 1.00 41.63 C ANISOU 2782 CB LEU A1275 5197 4328 6294 -25 -5 -135 C ATOM 2783 CG LEU A1275 31.170 -94.596 142.337 1.00 44.23 C ANISOU 2783 CG LEU A1275 5630 4571 6605 -89 -1 -171 C ATOM 2784 CD1 LEU A1275 31.678 -95.981 142.702 1.00 43.84 C ANISOU 2784 CD1 LEU A1275 5524 4612 6522 -164 55 -208 C ATOM 2785 CD2 LEU A1275 32.269 -93.768 141.689 1.00 39.09 C ANISOU 2785 CD2 LEU A1275 5063 3846 5942 -180 -79 -105 C ATOM 2786 N SER A1276 26.896 -93.773 140.366 1.00 37.32 N ANISOU 2786 N SER A1276 4471 3925 5783 258 -28 -66 N ATOM 2787 CA SER A1276 25.879 -94.190 139.405 1.00 38.95 C ANISOU 2787 CA SER A1276 4524 4295 5980 271 -41 -17 C ATOM 2788 C SER A1276 25.719 -93.205 138.253 1.00 43.95 C ANISOU 2788 C SER A1276 5184 4896 6621 330 -124 70 C ATOM 2789 O SER A1276 25.229 -93.594 137.187 1.00 44.63 O ANISOU 2789 O SER A1276 5158 5111 6687 292 -155 123 O ATOM 2790 CB SER A1276 24.537 -94.388 140.112 1.00 38.39 C ANISOU 2790 CB SER A1276 4327 4358 5900 389 17 -43 C ATOM 2791 OG SER A1276 24.073 -93.176 140.679 1.00 44.73 O ANISOU 2791 OG SER A1276 5198 5084 6714 592 15 -50 O ATOM 2792 N SER A1277 26.115 -91.947 138.437 1.00 45.53 N ANISOU 2792 N SER A1277 5543 4919 6838 414 -167 88 N ATOM 2793 CA SER A1277 26.031 -90.955 137.374 1.00 46.21 C ANISOU 2793 CA SER A1277 5687 4945 6926 466 -253 182 C ATOM 2794 C SER A1277 27.287 -90.893 136.516 1.00 50.81 C ANISOU 2794 C SER A1277 6347 5464 7496 289 -309 240 C ATOM 2795 O SER A1277 27.248 -90.299 135.433 1.00 58.70 O ANISOU 2795 O SER A1277 7367 6452 8483 292 -379 334 O ATOM 2796 CB SER A1277 25.745 -89.570 137.965 1.00 45.85 C ANISOU 2796 CB SER A1277 5807 4721 6894 654 -282 180 C ATOM 2797 OG SER A1277 26.728 -89.210 138.919 1.00 53.03 O ANISOU 2797 OG SER A1277 6891 5449 7808 595 -278 122 O ATOM 2798 N LYS A1278 28.390 -91.486 136.966 1.00 49.69 N ANISOU 2798 N LYS A1278 6237 5299 7344 144 -278 197 N ATOM 2799 CA LYS A1278 29.611 -91.514 136.177 1.00 46.67 C ANISOU 2799 CA LYS A1278 5894 4908 6932 -18 -319 256 C ATOM 2800 C LYS A1278 29.463 -92.467 134.993 1.00 48.61 C ANISOU 2800 C LYS A1278 5999 5332 7139 -87 -318 290 C ATOM 2801 O LYS A1278 28.660 -93.404 135.009 1.00 50.70 O ANISOU 2801 O LYS A1278 6143 5720 7399 -62 -275 244 O ATOM 2802 CB LYS A1278 30.797 -91.951 137.038 1.00 50.39 C ANISOU 2802 CB LYS A1278 6413 5343 7389 -131 -283 201 C ATOM 2803 CG LYS A1278 30.942 -91.213 138.360 1.00 54.71 C ANISOU 2803 CG LYS A1278 7097 5728 7960 -78 -278 144 C ATOM 2804 CD LYS A1278 31.693 -89.906 138.194 1.00 62.47 C ANISOU 2804 CD LYS A1278 8257 6542 8937 -139 -366 213 C ATOM 2805 CE LYS A1278 32.159 -89.364 139.538 1.00 69.44 C ANISOU 2805 CE LYS A1278 9292 7270 9822 -142 -367 144 C ATOM 2806 NZ LYS A1278 31.022 -89.073 140.455 1.00 73.12 N ANISOU 2806 NZ LYS A1278 9802 7667 10315 60 -330 61 N ATOM 2807 N LYS A1279 30.260 -92.216 133.952 1.00 53.42 N ANISOU 2807 N LYS A1279 6631 5957 7708 -187 -368 373 N ATOM 2808 CA LYS A1279 30.309 -93.145 132.828 1.00 55.37 C ANISOU 2808 CA LYS A1279 6769 6369 7898 -257 -366 394 C ATOM 2809 C LYS A1279 31.042 -94.427 133.196 1.00 51.93 C ANISOU 2809 C LYS A1279 6294 6009 7426 -337 -300 316 C ATOM 2810 O LYS A1279 30.763 -95.487 132.623 1.00 47.32 O ANISOU 2810 O LYS A1279 5633 5546 6799 -362 -280 286 O ATOM 2811 CB LYS A1279 30.975 -92.484 131.622 1.00 59.93 C ANISOU 2811 CB LYS A1279 7382 6961 8428 -331 -432 511 C ATOM 2812 CG LYS A1279 32.299 -91.809 131.940 1.00 65.48 C ANISOU 2812 CG LYS A1279 8190 7571 9118 -433 -452 555 C ATOM 2813 CD LYS A1279 33.016 -91.374 130.674 1.00 75.64 C ANISOU 2813 CD LYS A1279 9481 8924 10335 -536 -507 680 C ATOM 2814 CE LYS A1279 34.143 -90.403 130.985 1.00 81.07 C ANISOU 2814 CE LYS A1279 10285 9506 11011 -655 -550 753 C ATOM 2815 NZ LYS A1279 35.071 -90.928 132.024 1.00 82.63 N ANISOU 2815 NZ LYS A1279 10476 9716 11202 -719 -497 679 N ATOM 2816 N GLU A1280 31.975 -94.353 134.148 1.00 57.28 N ANISOU 2816 N GLU A1280 7037 6613 8112 -375 -272 282 N ATOM 2817 CA GLU A1280 32.711 -95.530 134.590 1.00 54.96 C ANISOU 2817 CA GLU A1280 6718 6385 7780 -424 -211 214 C ATOM 2818 C GLU A1280 31.843 -96.512 135.366 1.00 50.93 C ANISOU 2818 C GLU A1280 6169 5890 7294 -372 -152 118 C ATOM 2819 O GLU A1280 32.292 -97.633 135.627 1.00 52.34 O ANISOU 2819 O GLU A1280 6338 6115 7432 -402 -105 62 O ATOM 2820 CB GLU A1280 33.905 -95.107 135.448 1.00 51.45 C ANISOU 2820 CB GLU A1280 6343 5875 7332 -477 -205 214 C ATOM 2821 CG GLU A1280 34.947 -94.287 134.706 1.00 57.23 C ANISOU 2821 CG GLU A1280 7101 6624 8019 -574 -262 320 C ATOM 2822 CD GLU A1280 34.807 -92.799 134.955 1.00 64.41 C ANISOU 2822 CD GLU A1280 8125 7373 8976 -584 -330 378 C ATOM 2823 OE1 GLU A1280 35.840 -92.136 135.190 1.00 71.91 O ANISOU 2823 OE1 GLU A1280 9138 8283 9900 -691 -366 430 O ATOM 2824 OE2 GLU A1280 33.666 -92.293 134.924 1.00 70.76 O ANISOU 2824 OE2 GLU A1280 8960 8094 9833 -484 -351 375 O ATOM 2825 N PHE A1281 30.621 -96.122 135.735 1.00 45.93 N ANISOU 2825 N PHE A1281 5513 5225 6714 -292 -154 106 N ATOM 2826 CA PHE A1281 29.744 -97.015 136.483 1.00 42.37 C ANISOU 2826 CA PHE A1281 5009 4814 6276 -264 -99 32 C ATOM 2827 C PHE A1281 29.360 -98.241 135.669 1.00 48.53 C ANISOU 2827 C PHE A1281 5723 5712 7003 -328 -96 17 C ATOM 2828 O PHE A1281 29.164 -99.323 136.233 1.00 48.13 O ANISOU 2828 O PHE A1281 5668 5684 6936 -362 -50 -45 O ATOM 2829 CB PHE A1281 28.492 -96.258 136.923 1.00 42.47 C ANISOU 2829 CB PHE A1281 4985 4813 6338 -152 -103 38 C ATOM 2830 CG PHE A1281 27.640 -97.006 137.904 1.00 38.54 C ANISOU 2830 CG PHE A1281 4425 4369 5848 -127 -39 -26 C ATOM 2831 CD1 PHE A1281 28.044 -97.150 139.222 1.00 34.47 C ANISOU 2831 CD1 PHE A1281 3968 3784 5344 -115 16 -88 C ATOM 2832 CD2 PHE A1281 26.429 -97.552 137.516 1.00 38.28 C ANISOU 2832 CD2 PHE A1281 4269 4473 5800 -130 -39 -16 C ATOM 2833 CE1 PHE A1281 27.262 -97.833 140.130 1.00 34.87 C ANISOU 2833 CE1 PHE A1281 3960 3897 5391 -102 77 -135 C ATOM 2834 CE2 PHE A1281 25.639 -98.236 138.420 1.00 41.33 C ANISOU 2834 CE2 PHE A1281 4589 4931 6183 -133 19 -60 C ATOM 2835 CZ PHE A1281 26.057 -98.377 139.730 1.00 42.90 C ANISOU 2835 CZ PHE A1281 4851 5055 6393 -116 80 -118 C ATOM 2836 N GLN A1282 29.248 -98.095 134.345 1.00 53.17 N ANISOU 2836 N GLN A1282 6279 6368 7557 -351 -150 75 N ATOM 2837 CA GLN A1282 28.873 -99.219 133.496 1.00 52.16 C ANISOU 2837 CA GLN A1282 6110 6343 7364 -419 -159 55 C ATOM 2838 C GLN A1282 29.937-100.309 133.470 1.00 39.73 C ANISOU 2838 C GLN A1282 4608 4764 5723 -473 -126 1 C ATOM 2839 O GLN A1282 29.616-101.462 133.171 1.00 37.50 O ANISOU 2839 O GLN A1282 4339 4523 5386 -526 -121 -46 O ATOM 2840 CB GLN A1282 28.590 -98.730 132.076 1.00 67.53 C ANISOU 2840 CB GLN A1282 8014 8368 9275 -424 -229 131 C ATOM 2841 CG GLN A1282 27.467 -97.705 131.990 1.00 81.73 C ANISOU 2841 CG GLN A1282 9741 10186 11126 -344 -269 191 C ATOM 2842 CD GLN A1282 26.137 -98.253 132.475 1.00 90.84 C ANISOU 2842 CD GLN A1282 10796 11424 12293 -337 -253 157 C ATOM 2843 OE1 GLN A1282 25.834 -99.433 132.292 1.00 96.80 O ANISOU 2843 OE1 GLN A1282 11528 12252 12999 -434 -246 112 O ATOM 2844 NE2 GLN A1282 25.338 -97.398 133.102 1.00 89.59 N ANISOU 2844 NE2 GLN A1282 10587 11260 12191 -222 -248 181 N ATOM 2845 N GLU A1283 31.189 -99.973 133.779 1.00 38.27 N ANISOU 2845 N GLU A1283 4476 4532 5532 -459 -106 11 N ATOM 2846 CA GLU A1283 32.260-100.959 133.823 1.00 41.09 C ANISOU 2846 CA GLU A1283 4891 4904 5816 -474 -69 -34 C ATOM 2847 C GLU A1283 32.344-101.691 135.156 1.00 42.26 C ANISOU 2847 C GLU A1283 5086 4986 5984 -462 -12 -106 C ATOM 2848 O GLU A1283 33.116-102.650 135.267 1.00 41.20 O ANISOU 2848 O GLU A1283 5013 4857 5785 -453 19 -149 O ATOM 2849 CB GLU A1283 33.605-100.286 133.535 1.00 50.15 C ANISOU 2849 CB GLU A1283 6046 6079 6931 -471 -76 24 C ATOM 2850 CG GLU A1283 33.748 -99.728 132.131 1.00 50.79 C ANISOU 2850 CG GLU A1283 6090 6244 6962 -494 -127 104 C ATOM 2851 CD GLU A1283 35.031 -98.940 131.957 1.00 61.51 C ANISOU 2851 CD GLU A1283 7442 7642 8288 -521 -136 181 C ATOM 2852 OE1 GLU A1283 35.054 -97.748 132.332 1.00 66.05 O ANISOU 2852 OE1 GLU A1283 8026 8143 8927 -545 -169 240 O ATOM 2853 OE2 GLU A1283 36.023 -99.516 131.461 1.00 66.40 O ANISOU 2853 OE2 GLU A1283 8052 8371 8808 -517 -112 184 O ATOM 2854 N MET A1284 31.579-101.274 136.159 1.00 38.28 N ANISOU 2854 N MET A1284 4562 4427 5558 -447 4 -118 N ATOM 2855 CA MET A1284 31.668-101.835 137.498 1.00 33.51 C ANISOU 2855 CA MET A1284 3999 3765 4969 -436 58 -176 C ATOM 2856 C MET A1284 30.540-102.828 137.751 1.00 34.94 C ANISOU 2856 C MET A1284 4173 3960 5144 -480 76 -216 C ATOM 2857 O MET A1284 29.464-102.747 137.153 1.00 37.40 O ANISOU 2857 O MET A1284 4416 4330 5464 -511 45 -195 O ATOM 2858 CB MET A1284 31.620-100.727 138.553 1.00 37.67 C ANISOU 2858 CB MET A1284 4518 4227 5566 -391 69 -166 C ATOM 2859 CG MET A1284 32.726 -99.694 138.423 1.00 36.81 C ANISOU 2859 CG MET A1284 4435 4090 5460 -385 40 -120 C ATOM 2860 SD MET A1284 32.393 -98.218 139.403 1.00 39.71 S ANISOU 2860 SD MET A1284 4833 4352 5903 -335 25 -111 S ATOM 2861 CE MET A1284 33.866 -97.256 139.077 1.00 40.54 C ANISOU 2861 CE MET A1284 4990 4430 5984 -393 -26 -46 C ATOM 2862 N ARG A1285 30.807-103.774 138.648 1.00 29.91 N ANISOU 2862 N ARG A1285 3605 3277 4482 -492 122 -266 N ATOM 2863 CA ARG A1285 29.820-104.734 139.119 1.00 32.04 C ANISOU 2863 CA ARG A1285 3885 3548 4741 -560 141 -295 C ATOM 2864 C ARG A1285 29.871-104.765 140.639 1.00 32.64 C ANISOU 2864 C ARG A1285 3981 3577 4845 -534 198 -318 C ATOM 2865 O ARG A1285 30.953-104.695 141.228 1.00 36.56 O ANISOU 2865 O ARG A1285 4536 4022 5333 -481 222 -332 O ATOM 2866 CB ARG A1285 30.080-106.136 138.551 1.00 35.00 C ANISOU 2866 CB ARG A1285 4374 3896 5028 -619 129 -331 C ATOM 2867 CG ARG A1285 30.260-106.183 137.038 1.00 40.96 C ANISOU 2867 CG ARG A1285 5135 4697 5729 -629 76 -321 C ATOM 2868 CD ARG A1285 28.962-105.890 136.304 1.00 49.50 C ANISOU 2868 CD ARG A1285 6117 5864 6828 -705 27 -289 C ATOM 2869 NE ARG A1285 29.117-105.996 134.855 1.00 54.46 N ANISOU 2869 NE ARG A1285 6761 6541 7391 -721 -28 -282 N ATOM 2870 CZ ARG A1285 29.396-104.972 134.053 1.00 53.43 C ANISOU 2870 CZ ARG A1285 6557 6470 7276 -668 -57 -231 C ATOM 2871 NH1 ARG A1285 29.550-103.754 134.556 1.00 51.30 N ANISOU 2871 NH1 ARG A1285 6210 6195 7086 -600 -42 -185 N ATOM 2872 NH2 ARG A1285 29.520-105.165 132.747 1.00 43.81 N ANISOU 2872 NH2 ARG A1285 5358 5307 5982 -687 -104 -224 N ATOM 2873 N PHE A1286 28.705-104.860 141.274 1.00 33.17 N ANISOU 2873 N PHE A1286 3986 3684 4935 -574 221 -315 N ATOM 2874 CA PHE A1286 28.612-104.802 142.727 1.00 33.84 C ANISOU 2874 CA PHE A1286 4075 3746 5038 -545 279 -332 C ATOM 2875 C PHE A1286 27.779-105.959 143.256 1.00 38.91 C ANISOU 2875 C PHE A1286 4731 4413 5639 -652 306 -337 C ATOM 2876 O PHE A1286 26.706-106.261 142.720 1.00 38.53 O ANISOU 2876 O PHE A1286 4610 4450 5579 -742 282 -312 O ATOM 2877 CB PHE A1286 28.011-103.471 143.190 1.00 31.29 C ANISOU 2877 CB PHE A1286 3651 3465 4774 -457 291 -316 C ATOM 2878 CG PHE A1286 28.901-102.290 142.943 1.00 32.12 C ANISOU 2878 CG PHE A1286 3782 3510 4914 -370 263 -309 C ATOM 2879 CD1 PHE A1286 29.854-101.920 143.877 1.00 28.41 C ANISOU 2879 CD1 PHE A1286 3383 2964 4446 -325 284 -335 C ATOM 2880 CD2 PHE A1286 28.789-101.552 141.777 1.00 35.95 C ANISOU 2880 CD2 PHE A1286 4224 4017 5419 -351 207 -269 C ATOM 2881 CE1 PHE A1286 30.677-100.832 143.653 1.00 32.84 C ANISOU 2881 CE1 PHE A1286 3976 3472 5030 -282 246 -320 C ATOM 2882 CE2 PHE A1286 29.609-100.463 141.547 1.00 38.63 C ANISOU 2882 CE2 PHE A1286 4600 4294 5782 -299 173 -249 C ATOM 2883 CZ PHE A1286 30.555-100.103 142.487 1.00 32.39 C ANISOU 2883 CZ PHE A1286 3886 3427 4994 -275 191 -274 C ATOM 2884 N ILE A1287 28.277-106.595 144.314 1.00 35.39 N ANISOU 2884 N ILE A1287 4379 3902 5167 -655 350 -359 N ATOM 2885 CA ILE A1287 27.596-107.691 144.992 1.00 38.41 C ANISOU 2885 CA ILE A1287 4799 4290 5503 -767 378 -353 C ATOM 2886 C ILE A1287 27.555-107.354 146.476 1.00 37.26 C ANISOU 2886 C ILE A1287 4631 4159 5369 -713 445 -357 C ATOM 2887 O ILE A1287 28.606-107.248 147.120 1.00 36.03 O ANISOU 2887 O ILE A1287 4556 3926 5209 -633 465 -382 O ATOM 2888 CB ILE A1287 28.297-109.041 144.757 1.00 36.47 C ANISOU 2888 CB ILE A1287 4741 3929 5188 -825 359 -373 C ATOM 2889 CG1 ILE A1287 28.382-109.340 143.259 1.00 30.33 C ANISOU 2889 CG1 ILE A1287 4002 3139 4384 -861 294 -381 C ATOM 2890 CG2 ILE A1287 27.567-110.158 145.487 1.00 30.86 C ANISOU 2890 CG2 ILE A1287 4097 3203 4425 -965 379 -354 C ATOM 2891 CD1 ILE A1287 29.192-110.572 142.927 1.00 32.75 C ANISOU 2891 CD1 ILE A1287 4517 3318 4608 -869 273 -415 C ATOM 2892 N ILE A1288 26.351-107.179 147.014 1.00 33.61 N ANISOU 2892 N ILE A1288 4047 3815 4908 -754 479 -329 N ATOM 2893 CA ILE A1288 26.150-106.735 148.390 1.00 33.95 C ANISOU 2893 CA ILE A1288 4049 3902 4950 -687 548 -335 C ATOM 2894 C ILE A1288 25.454-107.853 149.152 1.00 40.17 C ANISOU 2894 C ILE A1288 4851 4740 5673 -827 586 -300 C ATOM 2895 O ILE A1288 24.348-108.270 148.786 1.00 42.72 O ANISOU 2895 O ILE A1288 5080 5179 5972 -954 576 -255 O ATOM 2896 CB ILE A1288 25.340-105.431 148.451 1.00 39.02 C ANISOU 2896 CB ILE A1288 4531 4663 5632 -575 565 -330 C ATOM 2897 CG1 ILE A1288 25.981-104.368 147.557 1.00 33.62 C ANISOU 2897 CG1 ILE A1288 3856 3910 5006 -467 512 -349 C ATOM 2898 CG2 ILE A1288 25.240-104.926 149.887 1.00 31.58 C ANISOU 2898 CG2 ILE A1288 3572 3754 4673 -479 638 -352 C ATOM 2899 CD1 ILE A1288 25.217-103.067 147.519 1.00 33.86 C ANISOU 2899 CD1 ILE A1288 3768 4025 5072 -336 517 -342 C ATOM 2900 N ILE A1289 26.099-108.334 150.212 1.00 38.54 N ANISOU 2900 N ILE A1289 4756 4456 5430 -816 625 -313 N ATOM 2901 CA ILE A1289 25.629-109.487 150.972 1.00 40.42 C ANISOU 2901 CA ILE A1289 5052 4709 5598 -959 657 -271 C ATOM 2902 C ILE A1289 25.552-109.099 152.440 1.00 40.11 C ANISOU 2902 C ILE A1289 4974 4733 5532 -886 735 -272 C ATOM 2903 O ILE A1289 26.535-108.611 153.007 1.00 41.71 O ANISOU 2903 O ILE A1289 5245 4857 5746 -756 748 -317 O ATOM 2904 CB ILE A1289 26.555-110.703 150.785 1.00 36.47 C ANISOU 2904 CB ILE A1289 4774 4028 5053 -1019 619 -276 C ATOM 2905 CG1 ILE A1289 26.743-110.998 149.296 1.00 36.70 C ANISOU 2905 CG1 ILE A1289 4857 3991 5096 -1058 543 -291 C ATOM 2906 CG2 ILE A1289 25.997-111.918 151.507 1.00 36.94 C ANISOU 2906 CG2 ILE A1289 4921 4080 5033 -1189 640 -221 C ATOM 2907 CD1 ILE A1289 27.786-112.043 149.013 1.00 38.23 C ANISOU 2907 CD1 ILE A1289 5280 4006 5241 -1053 508 -313 C ATOM 2908 N GLY A1290 24.398-109.310 153.054 1.00 35.56 N ANISOU 2908 N GLY A1290 4285 4317 4910 -976 785 -221 N ATOM 2909 CA GLY A1290 24.259-109.000 154.460 1.00 40.10 C ANISOU 2909 CA GLY A1290 4823 4972 5440 -906 866 -221 C ATOM 2910 C GLY A1290 22.806-108.937 154.887 1.00 48.58 C ANISOU 2910 C GLY A1290 5702 6292 6464 -974 925 -161 C ATOM 2911 O GLY A1290 21.892-109.234 154.119 1.00 51.98 O ANISOU 2911 O GLY A1290 6023 6836 6891 -1102 898 -108 O ATOM 2912 N LYS A1291 22.628-108.525 156.140 1.00 53.09 N ANISOU 2912 N LYS A1291 6226 6962 6985 -882 1007 -168 N ATOM 2913 CA LYS A1291 21.335-108.531 156.809 1.00 52.03 C ANISOU 2913 CA LYS A1291 5903 7092 6773 -929 1084 -104 C ATOM 2914 C LYS A1291 21.378-107.501 157.929 1.00 48.80 C ANISOU 2914 C LYS A1291 5448 6762 6333 -709 1165 -162 C ATOM 2915 O LYS A1291 22.453-107.131 158.403 1.00 49.58 O ANISOU 2915 O LYS A1291 5696 6694 6450 -592 1158 -234 O ATOM 2916 CB LYS A1291 21.020-109.923 157.364 1.00 64.00 C ANISOU 2916 CB LYS A1291 7479 8637 8200 -1174 1101 -11 C ATOM 2917 CG LYS A1291 19.575-110.360 157.263 1.00 79.20 C ANISOU 2917 CG LYS A1291 9203 10831 10057 -1360 1126 94 C ATOM 2918 CD LYS A1291 19.444-111.850 157.573 1.00 89.27 C ANISOU 2918 CD LYS A1291 10605 12061 11254 -1651 1109 191 C ATOM 2919 CE LYS A1291 18.062-112.389 157.218 1.00 98.65 C ANISOU 2919 CE LYS A1291 11605 13502 12375 -1901 1102 307 C ATOM 2920 NZ LYS A1291 18.050-113.881 157.213 1.00100.99 N ANISOU 2920 NZ LYS A1291 12089 13677 12607 -2218 1048 395 N ATOM 2921 N GLY A1292 20.199-107.040 158.351 1.00 47.86 N ANISOU 2921 N GLY A1292 5120 6912 6153 -651 1239 -129 N ATOM 2922 CA GLY A1292 20.125-106.140 159.490 1.00 47.26 C ANISOU 2922 CA GLY A1292 5011 6928 6018 -436 1324 -186 C ATOM 2923 C GLY A1292 19.021-105.098 159.455 1.00 50.65 C ANISOU 2923 C GLY A1292 5223 7602 6419 -247 1380 -194 C ATOM 2924 O GLY A1292 17.835-105.443 159.482 1.00 51.62 O ANISOU 2924 O GLY A1292 5134 8008 6473 -329 1429 -104 O ATOM 2925 N ASP A1293 19.410-103.821 159.415 1.00 47.11 N ANISOU 2925 N ASP A1293 4832 7052 6014 9 1369 -297 N ATOM 2926 CA ASP A1293 18.450-102.721 159.412 1.00 47.69 C ANISOU 2926 CA ASP A1293 4740 7324 6055 247 1419 -318 C ATOM 2927 C ASP A1293 17.530-102.852 158.201 1.00 48.50 C ANISOU 2927 C ASP A1293 4646 7586 6196 176 1380 -237 C ATOM 2928 O ASP A1293 18.020-102.987 157.071 1.00 47.30 O ANISOU 2928 O ASP A1293 4566 7260 6146 83 1281 -235 O ATOM 2929 CB ASP A1293 19.193-101.379 159.390 1.00 54.21 C ANISOU 2929 CB ASP A1293 5731 7932 6935 502 1382 -443 C ATOM 2930 CG ASP A1293 18.270-100.169 159.552 1.00 64.20 C ANISOU 2930 CG ASP A1293 6881 9365 8147 801 1437 -481 C ATOM 2931 OD1 ASP A1293 17.032-100.315 159.514 1.00 71.75 O ANISOU 2931 OD1 ASP A1293 7592 10634 9035 828 1500 -406 O ATOM 2932 OD2 ASP A1293 18.805 -99.053 159.721 1.00 68.31 O ANISOU 2932 OD2 ASP A1293 7566 9703 8687 1014 1412 -587 O ATOM 2933 N PRO A1294 16.206-102.860 158.393 1.00 53.75 N ANISOU 2933 N PRO A1294 5051 8601 6769 206 1452 -162 N ATOM 2934 CA PRO A1294 15.309-102.979 157.232 1.00 56.20 C ANISOU 2934 CA PRO A1294 5157 9092 7105 128 1406 -77 C ATOM 2935 C PRO A1294 15.435-101.833 156.243 1.00 58.20 C ANISOU 2935 C PRO A1294 5435 9229 7449 349 1338 -134 C ATOM 2936 O PRO A1294 15.314-102.058 155.033 1.00 61.40 O ANISOU 2936 O PRO A1294 5793 9614 7922 232 1252 -88 O ATOM 2937 CB PRO A1294 13.915-103.024 157.874 1.00 58.49 C ANISOU 2937 CB PRO A1294 5150 9819 7255 172 1513 9 C ATOM 2938 CG PRO A1294 14.140-103.512 159.255 1.00 59.68 C ANISOU 2938 CG PRO A1294 5367 9998 7309 120 1603 5 C ATOM 2939 CD PRO A1294 15.477-102.971 159.669 1.00 59.84 C ANISOU 2939 CD PRO A1294 5690 9650 7395 261 1578 -131 C ATOM 2940 N GLU A1295 15.668-100.607 156.720 1.00 58.00 N ANISOU 2940 N GLU A1295 5500 9118 7420 663 1369 -233 N ATOM 2941 CA GLU A1295 15.759 -99.472 155.805 1.00 64.67 C ANISOU 2941 CA GLU A1295 6391 9838 8341 876 1300 -278 C ATOM 2942 C GLU A1295 16.991 -99.563 154.915 1.00 64.07 C ANISOU 2942 C GLU A1295 6537 9412 8395 743 1184 -314 C ATOM 2943 O GLU A1295 16.946 -99.144 153.753 1.00 71.01 O ANISOU 2943 O GLU A1295 7400 10236 9345 773 1104 -295 O ATOM 2944 CB GLU A1295 15.764 -98.158 156.587 1.00 74.54 C ANISOU 2944 CB GLU A1295 7737 11041 9543 1233 1352 -380 C ATOM 2945 CG GLU A1295 14.502 -97.907 157.402 1.00 88.43 C ANISOU 2945 CG GLU A1295 9267 13174 11158 1434 1475 -352 C ATOM 2946 CD GLU A1295 13.231 -98.096 156.593 1.00104.62 C ANISOU 2946 CD GLU A1295 10999 15573 13180 1422 1478 -232 C ATOM 2947 OE1 GLU A1295 12.662 -99.208 156.626 1.00109.52 O ANISOU 2947 OE1 GLU A1295 11420 16442 13752 1159 1506 -124 O ATOM 2948 OE2 GLU A1295 12.804 -97.135 155.919 1.00109.63 O ANISOU 2948 OE2 GLU A1295 11588 16233 13832 1668 1445 -239 O ATOM 2949 N LEU A1296 18.092-100.101 155.437 1.00 56.23 N ANISOU 2949 N LEU A1296 5741 8202 7423 605 1173 -358 N ATOM 2950 CA LEU A1296 19.273-100.324 154.613 1.00 49.99 C ANISOU 2950 CA LEU A1296 5133 7125 6736 469 1072 -380 C ATOM 2951 C LEU A1296 19.103-101.529 153.699 1.00 47.41 C ANISOU 2951 C LEU A1296 4728 6849 6435 197 1023 -294 C ATOM 2952 O LEU A1296 19.713-101.580 152.625 1.00 38.70 O ANISOU 2952 O LEU A1296 3708 5585 5411 123 934 -294 O ATOM 2953 CB LEU A1296 20.505-100.497 155.501 1.00 49.19 C ANISOU 2953 CB LEU A1296 5252 6807 6633 432 1077 -450 C ATOM 2954 CG LEU A1296 20.838 -99.278 156.364 1.00 51.17 C ANISOU 2954 CG LEU A1296 5629 6959 6854 677 1103 -549 C ATOM 2955 CD1 LEU A1296 21.968 -99.581 157.338 1.00 49.71 C ANISOU 2955 CD1 LEU A1296 5630 6612 6645 610 1109 -606 C ATOM 2956 CD2 LEU A1296 21.187 -98.083 155.485 1.00 41.03 C ANISOU 2956 CD2 LEU A1296 4442 5501 5646 822 1020 -590 C ATOM 2957 N GLU A1297 18.283-102.501 154.100 1.00 46.80 N ANISOU 2957 N GLU A1297 4504 6995 6282 37 1076 -218 N ATOM 2958 CA GLU A1297 17.974-103.613 153.207 1.00 50.29 C ANISOU 2958 CA GLU A1297 4883 7491 6733 -232 1019 -136 C ATOM 2959 C GLU A1297 17.136-103.147 152.024 1.00 53.39 C ANISOU 2959 C GLU A1297 5100 8033 7151 -190 967 -89 C ATOM 2960 O GLU A1297 17.387-103.548 150.881 1.00 54.62 O ANISOU 2960 O GLU A1297 5297 8096 7359 -329 878 -69 O ATOM 2961 CB GLU A1297 17.255-104.722 153.974 1.00 55.13 C ANISOU 2961 CB GLU A1297 5390 8309 7246 -436 1081 -55 C ATOM 2962 CG GLU A1297 18.135-105.912 154.316 1.00 65.69 C ANISOU 2962 CG GLU A1297 6934 9445 8579 -655 1062 -53 C ATOM 2963 CD GLU A1297 17.470-106.865 155.291 1.00 76.96 C ANISOU 2963 CD GLU A1297 8286 11058 9896 -835 1132 29 C ATOM 2964 OE1 GLU A1297 17.333-106.501 156.479 1.00 79.04 O ANISOU 2964 OE1 GLU A1297 8514 11423 10094 -708 1225 13 O ATOM 2965 OE2 GLU A1297 17.076-107.973 154.869 1.00 81.50 O ANISOU 2965 OE2 GLU A1297 8849 11678 10440 -1111 1090 111 O ATOM 2966 N GLY A1298 16.139-102.297 152.276 1.00 49.39 N ANISOU 2966 N GLY A1298 4401 7767 6597 17 1021 -71 N ATOM 2967 CA GLY A1298 15.346-101.763 151.183 1.00 50.31 C ANISOU 2967 CA GLY A1298 4347 8039 6731 94 970 -21 C ATOM 2968 C GLY A1298 16.148-100.850 150.277 1.00 49.08 C ANISOU 2968 C GLY A1298 4350 7623 6677 238 887 -81 C ATOM 2969 O GLY A1298 15.962-100.850 149.057 1.00 47.56 O ANISOU 2969 O GLY A1298 4104 7445 6522 178 805 -39 O ATOM 2970 N TRP A1299 17.052-100.058 150.861 1.00 46.69 N ANISOU 2970 N TRP A1299 4247 7084 6408 415 903 -175 N ATOM 2971 CA TRP A1299 17.917 -99.203 150.056 1.00 42.34 C ANISOU 2971 CA TRP A1299 3868 6272 5946 517 820 -222 C ATOM 2972 C TRP A1299 18.806-100.037 149.141 1.00 43.13 C ANISOU 2972 C TRP A1299 4081 6199 6108 273 737 -211 C ATOM 2973 O TRP A1299 19.009 -99.688 147.972 1.00 48.68 O ANISOU 2973 O TRP A1299 4805 6826 6864 276 656 -194 O ATOM 2974 CB TRP A1299 18.759 -98.310 150.969 1.00 43.90 C ANISOU 2974 CB TRP A1299 4273 6254 6154 699 846 -321 C ATOM 2975 CG TRP A1299 19.537 -97.240 150.252 1.00 45.49 C ANISOU 2975 CG TRP A1299 4648 6208 6430 816 762 -359 C ATOM 2976 CD1 TRP A1299 19.442 -96.893 148.935 1.00 41.46 C ANISOU 2976 CD1 TRP A1299 4108 5673 5972 818 679 -312 C ATOM 2977 CD2 TRP A1299 20.530 -96.378 150.821 1.00 48.75 C ANISOU 2977 CD2 TRP A1299 5294 6367 6861 928 747 -445 C ATOM 2978 NE1 TRP A1299 20.315 -95.873 148.649 1.00 40.30 N ANISOU 2978 NE1 TRP A1299 4163 5272 5877 920 616 -355 N ATOM 2979 CE2 TRP A1299 20.994 -95.537 149.790 1.00 44.68 C ANISOU 2979 CE2 TRP A1299 4883 5681 6412 979 653 -437 C ATOM 2980 CE3 TRP A1299 21.073 -96.236 152.103 1.00 53.89 C ANISOU 2980 CE3 TRP A1299 6079 6925 7471 975 797 -523 C ATOM 2981 CZ2 TRP A1299 21.974 -94.569 150.000 1.00 49.96 C ANISOU 2981 CZ2 TRP A1299 5789 6089 7107 1056 604 -499 C ATOM 2982 CZ3 TRP A1299 22.047 -95.274 152.310 1.00 56.16 C ANISOU 2982 CZ3 TRP A1299 6600 6955 7783 1057 746 -594 C ATOM 2983 CH2 TRP A1299 22.487 -94.454 151.263 1.00 56.96 C ANISOU 2983 CH2 TRP A1299 6804 6888 7951 1087 649 -579 C ATOM 2984 N ALA A1300 19.334-101.152 149.651 1.00 42.47 N ANISOU 2984 N ALA A1300 4076 6055 6006 74 758 -218 N ATOM 2985 CA ALA A1300 20.138-102.035 148.813 1.00 41.55 C ANISOU 2985 CA ALA A1300 4074 5786 5928 -134 686 -212 C ATOM 2986 C ALA A1300 19.290-102.697 147.734 1.00 41.26 C ANISOU 2986 C ALA A1300 3893 5910 5874 -295 634 -136 C ATOM 2987 O ALA A1300 19.714-102.791 146.577 1.00 36.88 O ANISOU 2987 O ALA A1300 3397 5257 5359 -360 553 -132 O ATOM 2988 CB ALA A1300 20.833-103.088 149.675 1.00 36.13 C ANISOU 2988 CB ALA A1300 3516 5000 5211 -281 721 -233 C ATOM 2989 N ARG A1301 18.088-103.158 148.093 1.00 39.30 N ANISOU 2989 N ARG A1301 3452 5925 5556 -372 677 -72 N ATOM 2990 CA ARG A1301 17.196-103.746 147.100 1.00 40.35 C ANISOU 2990 CA ARG A1301 3431 6240 5659 -545 618 6 C ATOM 2991 C ARG A1301 16.786-102.730 146.043 1.00 47.55 C ANISOU 2991 C ARG A1301 4236 7224 6606 -386 561 27 C ATOM 2992 O ARG A1301 16.567-103.095 144.883 1.00 44.43 O ANISOU 2992 O ARG A1301 3803 6868 6213 -518 478 66 O ATOM 2993 CB ARG A1301 15.955-104.326 147.781 1.00 47.09 C ANISOU 2993 CB ARG A1301 4072 7403 6418 -659 677 84 C ATOM 2994 CG ARG A1301 16.216-105.574 148.604 1.00 56.90 C ANISOU 2994 CG ARG A1301 5420 8589 7611 -890 711 93 C ATOM 2995 CD ARG A1301 16.717-106.712 147.731 1.00 68.40 C ANISOU 2995 CD ARG A1301 7038 9875 9075 -1154 619 97 C ATOM 2996 NE ARG A1301 16.881-107.950 148.487 1.00 75.50 N ANISOU 2996 NE ARG A1301 8059 10713 9916 -1378 643 118 N ATOM 2997 CZ ARG A1301 17.351-109.083 147.973 1.00 74.74 C ANISOU 2997 CZ ARG A1301 8153 10439 9806 -1602 573 115 C ATOM 2998 NH1 ARG A1301 17.465-110.161 148.735 1.00 74.52 N ANISOU 2998 NH1 ARG A1301 8251 10344 9718 -1787 594 141 N ATOM 2999 NH2 ARG A1301 17.707-109.136 146.697 1.00 67.88 N ANISOU 2999 NH2 ARG A1301 7364 9455 8973 -1632 480 87 N ATOM 3000 N SER A1302 16.676-101.455 146.424 1.00 46.24 N ANISOU 3000 N SER A1302 4040 7070 6460 -99 600 1 N ATOM 3001 CA SER A1302 16.319-100.422 145.458 1.00 46.10 C ANISOU 3001 CA SER A1302 3949 7096 6472 78 543 26 C ATOM 3002 C SER A1302 17.399-100.264 144.395 1.00 45.82 C ANISOU 3002 C SER A1302 4101 6798 6510 36 452 -3 C ATOM 3003 O SER A1302 17.092-100.157 143.203 1.00 46.59 O ANISOU 3003 O SER A1302 4130 6956 6615 5 375 45 O ATOM 3004 CB SER A1302 16.074 -99.097 146.176 1.00 45.59 C ANISOU 3004 CB SER A1302 3872 7046 6404 409 601 -6 C ATOM 3005 OG SER A1302 15.053 -99.228 147.149 1.00 47.37 O ANISOU 3005 OG SER A1302 3906 7548 6544 472 694 22 O ATOM 3006 N LEU A1303 18.669-100.251 144.807 1.00 42.89 N ANISOU 3006 N LEU A1303 3955 6159 6184 31 461 -76 N ATOM 3007 CA LEU A1303 19.759-100.117 143.845 1.00 43.00 C ANISOU 3007 CA LEU A1303 4132 5953 6252 -12 383 -96 C ATOM 3008 C LEU A1303 19.856-101.343 142.946 1.00 47.46 C ANISOU 3008 C LEU A1303 4701 6535 6796 -261 328 -71 C ATOM 3009 O LEU A1303 20.190-101.225 141.761 1.00 49.43 O ANISOU 3009 O LEU A1303 4988 6729 7064 -292 253 -55 O ATOM 3010 CB LEU A1303 21.080 -99.884 144.577 1.00 35.51 C ANISOU 3010 CB LEU A1303 3395 4758 5338 27 407 -169 C ATOM 3011 CG LEU A1303 21.189 -98.609 145.415 1.00 41.55 C ANISOU 3011 CG LEU A1303 4222 5446 6119 260 443 -210 C ATOM 3012 CD1 LEU A1303 22.549 -98.523 146.087 1.00 34.61 C ANISOU 3012 CD1 LEU A1303 3547 4341 5262 244 451 -277 C ATOM 3013 CD2 LEU A1303 20.935 -97.379 144.557 1.00 43.20 C ANISOU 3013 CD2 LEU A1303 4423 5631 6358 428 382 -179 C ATOM 3014 N GLU A1304 19.577-102.529 143.493 1.00 48.15 N ANISOU 3014 N GLU A1304 4769 6690 6834 -442 362 -67 N ATOM 3015 CA GLU A1304 19.598-103.741 142.680 1.00 47.12 C ANISOU 3015 CA GLU A1304 4676 6559 6668 -682 303 -50 C ATOM 3016 C GLU A1304 18.535-103.688 141.592 1.00 43.86 C ANISOU 3016 C GLU A1304 4086 6352 6225 -741 236 18 C ATOM 3017 O GLU A1304 18.768-104.129 140.461 1.00 43.09 O ANISOU 3017 O GLU A1304 4047 6211 6115 -858 157 21 O ATOM 3018 CB GLU A1304 19.393-104.971 143.566 1.00 51.25 C ANISOU 3018 CB GLU A1304 5229 7109 7135 -868 348 -49 C ATOM 3019 CG GLU A1304 19.387-106.287 142.806 1.00 51.48 C ANISOU 3019 CG GLU A1304 5341 7105 7113 -1126 280 -37 C ATOM 3020 CD GLU A1304 18.980-107.461 143.671 1.00 54.28 C ANISOU 3020 CD GLU A1304 5722 7501 7402 -1328 314 -14 C ATOM 3021 OE1 GLU A1304 18.145-107.270 144.580 1.00 58.65 O ANISOU 3021 OE1 GLU A1304 6115 8242 7929 -1312 379 30 O ATOM 3022 OE2 GLU A1304 19.495-108.575 143.442 1.00 55.41 O ANISOU 3022 OE2 GLU A1304 6055 7490 7510 -1496 276 -37 O ATOM 3023 N GLU A1305 17.361-103.149 141.918 1.00 42.66 N ANISOU 3023 N GLU A1305 3714 6447 6050 -650 266 74 N ATOM 3024 CA GLU A1305 16.290-103.017 140.941 1.00 49.88 C ANISOU 3024 CA GLU A1305 4427 7600 6926 -685 201 150 C ATOM 3025 C GLU A1305 16.528-101.848 139.994 1.00 54.63 C ANISOU 3025 C GLU A1305 5037 8144 7576 -485 146 158 C ATOM 3026 O GLU A1305 16.085-101.887 138.841 1.00 59.56 O ANISOU 3026 O GLU A1305 5577 8877 8175 -549 63 208 O ATOM 3027 CB GLU A1305 14.954-102.861 141.672 1.00 59.16 C ANISOU 3027 CB GLU A1305 5340 9094 8042 -639 259 217 C ATOM 3028 CG GLU A1305 13.738-102.694 140.783 1.00 75.77 C ANISOU 3028 CG GLU A1305 7190 11506 10091 -662 196 311 C ATOM 3029 CD GLU A1305 12.444-102.803 141.565 1.00 90.83 C ANISOU 3029 CD GLU A1305 8820 13774 11917 -667 258 387 C ATOM 3030 OE1 GLU A1305 11.950-103.936 141.743 1.00 95.36 O ANISOU 3030 OE1 GLU A1305 9324 14487 12420 -958 249 431 O ATOM 3031 OE2 GLU A1305 11.932-101.757 142.017 1.00 95.47 O ANISOU 3031 OE2 GLU A1305 9268 14505 12501 -378 316 406 O ATOM 3032 N LYS A1306 17.240-100.817 140.452 1.00 54.84 N ANISOU 3032 N LYS A1306 5178 7995 7665 -258 183 114 N ATOM 3033 CA LYS A1306 17.470 -99.632 139.634 1.00 49.29 C ANISOU 3033 CA LYS A1306 4506 7217 7004 -70 129 132 C ATOM 3034 C LYS A1306 18.609 -99.827 138.640 1.00 47.91 C ANISOU 3034 C LYS A1306 4511 6833 6858 -171 61 108 C ATOM 3035 O LYS A1306 18.566 -99.264 137.540 1.00 46.58 O ANISOU 3035 O LYS A1306 4327 6676 6695 -120 -11 152 O ATOM 3036 CB LYS A1306 17.755 -98.431 140.538 1.00 57.49 C ANISOU 3036 CB LYS A1306 5621 8138 8084 195 186 95 C ATOM 3037 CG LYS A1306 17.925 -97.107 139.812 1.00 64.64 C ANISOU 3037 CG LYS A1306 6586 8948 9027 401 128 123 C ATOM 3038 CD LYS A1306 18.125 -95.969 140.802 1.00 69.97 C ANISOU 3038 CD LYS A1306 7365 9492 9726 653 179 78 C ATOM 3039 CE LYS A1306 18.195 -94.626 140.096 1.00 78.94 C ANISOU 3039 CE LYS A1306 8584 10520 10891 859 113 116 C ATOM 3040 NZ LYS A1306 18.323 -93.500 141.062 1.00 86.16 N ANISOU 3040 NZ LYS A1306 9634 11289 11815 1108 153 66 N ATOM 3041 N HIS A1307 19.623-100.614 138.996 1.00 44.66 N ANISOU 3041 N HIS A1307 4266 6247 6455 -302 84 45 N ATOM 3042 CA HIS A1307 20.795-100.813 138.155 1.00 44.13 C ANISOU 3042 CA HIS A1307 4365 6001 6401 -372 34 20 C ATOM 3043 C HIS A1307 21.009-102.297 137.895 1.00 49.70 C ANISOU 3043 C HIS A1307 5135 6696 7053 -602 19 -9 C ATOM 3044 O HIS A1307 20.886-103.121 138.806 1.00 54.31 O ANISOU 3044 O HIS A1307 5738 7283 7616 -695 70 -36 O ATOM 3045 CB HIS A1307 22.051-100.217 138.800 1.00 45.99 C ANISOU 3045 CB HIS A1307 4770 6015 6687 -270 70 -31 C ATOM 3046 CG HIS A1307 21.910 -98.775 139.176 1.00 51.12 C ANISOU 3046 CG HIS A1307 5414 6628 7381 -53 79 -15 C ATOM 3047 ND1 HIS A1307 21.586 -98.368 140.453 1.00 53.61 N ANISOU 3047 ND1 HIS A1307 5716 6948 7707 67 149 -46 N ATOM 3048 CD2 HIS A1307 22.046 -97.645 138.444 1.00 52.60 C ANISOU 3048 CD2 HIS A1307 5630 6760 7594 68 24 27 C ATOM 3049 CE1 HIS A1307 21.531 -97.048 140.491 1.00 55.28 C ANISOU 3049 CE1 HIS A1307 5962 7094 7946 263 134 -32 C ATOM 3050 NE2 HIS A1307 21.806 -96.585 139.285 1.00 56.39 N ANISOU 3050 NE2 HIS A1307 6133 7192 8100 262 56 17 N ATOM 3051 N GLY A1308 21.342-102.630 136.649 1.00 48.78 N ANISOU 3051 N GLY A1308 5072 6558 6905 -688 -53 -3 N ATOM 3052 CA GLY A1308 21.596-103.998 136.250 1.00 46.01 C ANISOU 3052 CA GLY A1308 4824 6169 6489 -886 -80 -40 C ATOM 3053 C GLY A1308 22.963-104.538 136.596 1.00 46.11 C ANISOU 3053 C GLY A1308 5042 5976 6502 -890 -46 -108 C ATOM 3054 O GLY A1308 23.263-105.690 136.271 1.00 51.50 O ANISOU 3054 O GLY A1308 5847 6600 7122 -1023 -67 -146 O ATOM 3055 N ASN A1309 23.809-103.740 137.247 1.00 39.56 N ANISOU 3055 N ASN A1309 4262 5038 5732 -744 2 -124 N ATOM 3056 CA ASN A1309 25.135-104.174 137.665 1.00 39.17 C ANISOU 3056 CA ASN A1309 4379 4827 5678 -733 36 -178 C ATOM 3057 C ASN A1309 25.265-104.249 139.184 1.00 39.24 C ANISOU 3057 C ASN A1309 4412 4782 5714 -697 112 -206 C ATOM 3058 O ASN A1309 26.379-104.179 139.712 1.00 40.59 O ANISOU 3058 O ASN A1309 4689 4838 5897 -639 143 -238 O ATOM 3059 CB ASN A1309 26.204-103.248 137.081 1.00 30.74 C ANISOU 3059 CB ASN A1309 3357 3688 4634 -627 17 -166 C ATOM 3060 CG ASN A1309 25.994-101.797 137.468 1.00 43.04 C ANISOU 3060 CG ASN A1309 4842 5248 6262 -493 24 -129 C ATOM 3061 OD1 ASN A1309 24.881-101.385 137.795 1.00 41.94 O ANISOU 3061 OD1 ASN A1309 4589 5201 6145 -453 30 -103 O ATOM 3062 ND2 ASN A1309 27.064-101.012 137.428 1.00 30.20 N ANISOU 3062 ND2 ASN A1309 3288 3527 4660 -423 19 -122 N ATOM 3063 N VAL A1310 24.147-104.390 139.895 1.00 39.73 N ANISOU 3063 N VAL A1310 4368 4950 5777 -733 141 -188 N ATOM 3064 CA VAL A1310 24.132-104.464 141.352 1.00 41.46 C ANISOU 3064 CA VAL A1310 4598 5147 6009 -702 217 -209 C ATOM 3065 C VAL A1310 23.337-105.695 141.766 1.00 46.26 C ANISOU 3065 C VAL A1310 5191 5827 6559 -872 232 -199 C ATOM 3066 O VAL A1310 22.175-105.849 141.376 1.00 51.02 O ANISOU 3066 O VAL A1310 5657 6592 7135 -961 205 -153 O ATOM 3067 CB VAL A1310 23.527-103.197 141.986 1.00 38.90 C ANISOU 3067 CB VAL A1310 4150 4899 5730 -545 252 -189 C ATOM 3068 CG1 VAL A1310 23.417-103.360 143.496 1.00 40.46 C ANISOU 3068 CG1 VAL A1310 4355 5098 5921 -520 333 -214 C ATOM 3069 CG2 VAL A1310 24.363-101.978 141.640 1.00 31.67 C ANISOU 3069 CG2 VAL A1310 3292 3876 4866 -401 227 -195 C ATOM 3070 N LYS A1311 23.962-106.565 142.556 1.00 41.22 N ANISOU 3070 N LYS A1311 4692 5076 5893 -926 268 -233 N ATOM 3071 CA LYS A1311 23.333-107.778 143.063 1.00 43.65 C ANISOU 3071 CA LYS A1311 5030 5417 6140 -1104 280 -217 C ATOM 3072 C LYS A1311 23.331-107.738 144.584 1.00 42.19 C ANISOU 3072 C LYS A1311 4839 5234 5958 -1060 364 -219 C ATOM 3073 O LYS A1311 24.347-107.397 145.200 1.00 40.75 O ANISOU 3073 O LYS A1311 4748 4933 5801 -937 399 -259 O ATOM 3074 CB LYS A1311 24.066-109.025 142.558 1.00 43.92 C ANISOU 3074 CB LYS A1311 5279 5292 6117 -1214 238 -251 C ATOM 3075 CG LYS A1311 23.639-110.323 143.223 1.00 48.36 C ANISOU 3075 CG LYS A1311 5940 5823 6610 -1398 247 -236 C ATOM 3076 CD LYS A1311 22.184-110.651 142.935 1.00 52.71 C ANISOU 3076 CD LYS A1311 6352 6554 7120 -1595 212 -174 C ATOM 3077 CE LYS A1311 21.786-111.972 143.577 1.00 49.06 C ANISOU 3077 CE LYS A1311 6011 6049 6580 -1815 211 -147 C ATOM 3078 NZ LYS A1311 20.353-112.310 143.349 1.00 46.00 N ANISOU 3078 NZ LYS A1311 5470 5869 6140 -2044 172 -73 N ATOM 3079 N VAL A1312 22.194-108.083 145.186 1.00 39.92 N ANISOU 3079 N VAL A1312 4434 5101 5632 -1168 395 -170 N ATOM 3080 CA VAL A1312 22.022-108.059 146.634 1.00 43.22 C ANISOU 3080 CA VAL A1312 4825 5563 6035 -1135 479 -163 C ATOM 3081 C VAL A1312 21.570-109.439 147.094 1.00 48.96 C ANISOU 3081 C VAL A1312 5620 6301 6684 -1365 483 -121 C ATOM 3082 O VAL A1312 20.640-110.016 146.519 1.00 54.30 O ANISOU 3082 O VAL A1312 6225 7093 7315 -1553 438 -69 O ATOM 3083 CB VAL A1312 21.014-106.980 147.072 1.00 46.03 C ANISOU 3083 CB VAL A1312 4950 6135 6405 -1013 529 -132 C ATOM 3084 CG1 VAL A1312 20.773-107.055 148.570 1.00 43.77 C ANISOU 3084 CG1 VAL A1312 4636 5916 6080 -988 621 -125 C ATOM 3085 CG2 VAL A1312 21.514-105.599 146.686 1.00 49.33 C ANISOU 3085 CG2 VAL A1312 5351 6498 6896 -784 518 -172 C ATOM 3086 N ILE A1313 22.226-109.961 148.128 1.00 44.80 N ANISOU 3086 N ILE A1313 5236 5653 6132 -1362 530 -138 N ATOM 3087 CA ILE A1313 21.891-111.252 148.718 1.00 48.45 C ANISOU 3087 CA ILE A1313 5799 6097 6515 -1573 536 -91 C ATOM 3088 C ILE A1313 21.671-111.041 150.210 1.00 48.72 C ANISOU 3088 C ILE A1313 5766 6222 6523 -1523 631 -67 C ATOM 3089 O ILE A1313 22.607-110.677 150.932 1.00 44.61 O ANISOU 3089 O ILE A1313 5334 5592 6025 -1362 672 -116 O ATOM 3090 CB ILE A1313 22.987-112.305 148.480 1.00 49.19 C ANISOU 3090 CB ILE A1313 6183 5927 6581 -1619 491 -129 C ATOM 3091 CG1 ILE A1313 23.198-112.532 146.983 1.00 46.36 C ANISOU 3091 CG1 ILE A1313 5898 5488 6229 -1657 400 -160 C ATOM 3092 CG2 ILE A1313 22.631-113.607 149.181 1.00 51.31 C ANISOU 3092 CG2 ILE A1313 6587 6148 6761 -1833 494 -73 C ATOM 3093 CD1 ILE A1313 24.305-113.515 146.668 1.00 46.97 C ANISOU 3093 CD1 ILE A1313 6265 5317 6266 -1654 359 -206 C ATOM 3094 N THR A1314 20.443-111.276 150.673 1.00 52.36 N ANISOU 3094 N THR A1314 6066 6904 6926 -1665 665 11 N ATOM 3095 CA THR A1314 20.113-111.146 152.086 1.00 53.89 C ANISOU 3095 CA THR A1314 6182 7222 7072 -1631 762 43 C ATOM 3096 C THR A1314 19.922-112.479 152.794 1.00 60.18 C ANISOU 3096 C THR A1314 7106 7985 7777 -1871 770 115 C ATOM 3097 O THR A1314 19.747-112.488 154.017 1.00 62.93 O ANISOU 3097 O THR A1314 7415 8423 8072 -1855 851 147 O ATOM 3098 CB THR A1314 18.841-110.302 152.269 1.00 53.60 C ANISOU 3098 CB THR A1314 5839 7510 7017 -1577 816 90 C ATOM 3099 OG1 THR A1314 17.771-110.867 151.499 1.00 55.37 O ANISOU 3099 OG1 THR A1314 5937 7904 7197 -1808 762 172 O ATOM 3100 CG2 THR A1314 19.084-108.868 151.831 1.00 50.11 C ANISOU 3100 CG2 THR A1314 5306 7075 6658 -1297 819 19 C ATOM 3101 N GLU A1315 19.946-113.596 152.073 1.00 65.77 N ANISOU 3101 N GLU A1315 7978 8558 8453 -2093 685 141 N ATOM 3102 CA GLU A1315 19.802-114.894 152.710 1.00 73.78 C ANISOU 3102 CA GLU A1315 9160 9500 9374 -2332 679 214 C ATOM 3103 C GLU A1315 21.146-115.372 153.256 1.00 76.70 C ANISOU 3103 C GLU A1315 9816 9582 9746 -2221 684 162 C ATOM 3104 O GLU A1315 22.203-114.795 152.985 1.00 71.08 O ANISOU 3104 O GLU A1315 9172 8733 9104 -1989 679 72 O ATOM 3105 CB GLU A1315 19.230-115.918 151.730 1.00 81.09 C ANISOU 3105 CB GLU A1315 10179 10383 10250 -2629 575 263 C ATOM 3106 CG GLU A1315 20.173-116.292 150.598 1.00 93.82 C ANISOU 3106 CG GLU A1315 12037 11712 11898 -2581 482 177 C ATOM 3107 CD GLU A1315 19.650-117.446 149.762 1.00104.19 C ANISOU 3107 CD GLU A1315 13507 12944 13137 -2891 374 217 C ATOM 3108 OE1 GLU A1315 18.559-117.965 150.078 1.00108.27 O ANISOU 3108 OE1 GLU A1315 13935 13626 13575 -3170 365 322 O ATOM 3109 OE2 GLU A1315 20.331-117.834 148.789 1.00106.21 O ANISOU 3109 OE2 GLU A1315 13976 12977 13400 -2861 295 145 O ATOM 3110 N MET A1316 21.093-116.447 154.039 1.00 82.88 N ANISOU 3110 N MET A1316 10763 10287 10440 -2394 690 232 N ATOM 3111 CA MET A1316 22.294-117.012 154.637 1.00 86.16 C ANISOU 3111 CA MET A1316 11453 10447 10838 -2293 693 202 C ATOM 3112 C MET A1316 23.065-117.818 153.600 1.00 75.23 C ANISOU 3112 C MET A1316 10348 8780 9455 -2310 593 152 C ATOM 3113 O MET A1316 22.487-118.636 152.877 1.00 72.78 O ANISOU 3113 O MET A1316 10139 8416 9099 -2544 517 188 O ATOM 3114 CB MET A1316 21.928-117.891 155.832 1.00101.90 C ANISOU 3114 CB MET A1316 13538 12454 12726 -2471 730 306 C ATOM 3115 CG MET A1316 23.122-118.495 156.550 1.00113.13 C ANISOU 3115 CG MET A1316 15239 13630 14115 -2356 733 289 C ATOM 3116 SD MET A1316 22.636-119.588 157.900 1.00124.03 S ANISOU 3116 SD MET A1316 16749 15017 15361 -2590 768 430 S ATOM 3117 CE MET A1316 21.676-120.814 157.014 1.00126.67 C ANISOU 3117 CE MET A1316 17227 15276 15626 -2984 663 517 C ATOM 3118 N LEU A1317 24.373-117.585 153.528 1.00 65.35 N ANISOU 3118 N LEU A1317 9224 7361 8245 -2062 592 70 N ATOM 3119 CA LEU A1317 25.249-118.264 152.585 1.00 59.50 C ANISOU 3119 CA LEU A1317 8740 6371 7494 -2012 512 12 C ATOM 3120 C LEU A1317 26.245-119.133 153.337 1.00 59.32 C ANISOU 3120 C LEU A1317 8999 6133 7408 -1928 514 20 C ATOM 3121 O LEU A1317 26.755-118.740 154.392 1.00 58.55 O ANISOU 3121 O LEU A1317 8853 6079 7314 -1787 579 25 O ATOM 3122 CB LEU A1317 26.008-117.262 151.704 1.00 52.45 C ANISOU 3122 CB LEU A1317 7745 5492 6691 -1776 504 -83 C ATOM 3123 CG LEU A1317 25.201-116.394 150.739 1.00 49.04 C ANISOU 3123 CG LEU A1317 7073 5236 6323 -1816 485 -98 C ATOM 3124 CD1 LEU A1317 26.124-115.439 149.999 1.00 42.53 C ANISOU 3124 CD1 LEU A1317 6186 4399 5576 -1578 478 -180 C ATOM 3125 CD2 LEU A1317 24.422-117.256 149.758 1.00 51.90 C ANISOU 3125 CD2 LEU A1317 7527 5558 6634 -2059 400 -73 C ATOM 3126 N SER A1318 26.522-120.313 152.790 1.00 57.67 N ANISOU 3126 N SER A1318 9095 5689 7130 -2007 437 18 N ATOM 3127 CA SER A1318 27.567-121.159 153.342 1.00 55.24 C ANISOU 3127 CA SER A1318 9079 5156 6754 -1880 429 20 C ATOM 3128 C SER A1318 28.933-120.539 153.078 1.00 54.34 C ANISOU 3128 C SER A1318 8943 5018 6687 -1550 445 -68 C ATOM 3129 O SER A1318 29.126-119.795 152.113 1.00 56.64 O ANISOU 3129 O SER A1318 9095 5381 7044 -1455 433 -136 O ATOM 3130 CB SER A1318 27.504-122.559 152.735 1.00 52.69 C ANISOU 3130 CB SER A1318 9117 4566 6334 -2027 335 31 C ATOM 3131 OG SER A1318 27.777-122.521 151.345 1.00 57.49 O ANISOU 3131 OG SER A1318 9778 5105 6961 -1961 274 -57 O ATOM 3132 N ARG A1319 29.892-120.852 153.952 1.00 52.62 N ANISOU 3132 N ARG A1319 8856 4713 6424 -1382 471 -56 N ATOM 3133 CA ARG A1319 31.231-120.305 153.782 1.00 51.92 C ANISOU 3133 CA ARG A1319 8732 4633 6362 -1083 483 -124 C ATOM 3134 C ARG A1319 31.946-120.897 152.573 1.00 50.93 C ANISOU 3134 C ARG A1319 8807 4346 6199 -962 419 -186 C ATOM 3135 O ARG A1319 32.957-120.339 152.134 1.00 56.20 O ANISOU 3135 O ARG A1319 9397 5067 6890 -735 426 -242 O ATOM 3136 CB ARG A1319 32.060-120.520 155.049 1.00 46.82 C ANISOU 3136 CB ARG A1319 8164 3963 5664 -937 520 -86 C ATOM 3137 CG ARG A1319 32.293-121.971 155.413 1.00 51.17 C ANISOU 3137 CG ARG A1319 9068 4276 6097 -957 482 -33 C ATOM 3138 CD ARG A1319 33.319-122.079 156.528 1.00 59.36 C ANISOU 3138 CD ARG A1319 10163 5309 7080 -753 512 -3 C ATOM 3139 NE ARG A1319 33.737-123.458 156.759 1.00 67.37 N ANISOU 3139 NE ARG A1319 11545 6076 7977 -707 467 43 N ATOM 3140 CZ ARG A1319 34.729-123.809 157.570 1.00 67.25 C ANISOU 3140 CZ ARG A1319 11644 6019 7890 -500 476 75 C ATOM 3141 NH1 ARG A1319 35.408-122.879 158.228 1.00 60.56 N ANISOU 3141 NH1 ARG A1319 10563 5371 7076 -344 524 64 N ATOM 3142 NH2 ARG A1319 35.043-125.089 157.720 1.00 69.87 N ANISOU 3142 NH2 ARG A1319 12336 6105 8108 -449 429 120 N ATOM 3143 N GLU A1320 31.448-122.009 152.026 1.00 44.71 N ANISOU 3143 N GLU A1320 8280 3368 5339 -1114 355 -176 N ATOM 3144 CA GLU A1320 31.972-122.491 150.752 1.00 49.16 C ANISOU 3144 CA GLU A1320 9026 3792 5860 -1008 294 -250 C ATOM 3145 C GLU A1320 31.632-121.526 149.623 1.00 51.27 C ANISOU 3145 C GLU A1320 9049 4219 6212 -1034 287 -307 C ATOM 3146 O GLU A1320 32.476-121.243 148.766 1.00 52.91 O ANISOU 3146 O GLU A1320 9243 4440 6419 -833 278 -374 O ATOM 3147 CB GLU A1320 31.429-123.886 150.441 1.00 49.49 C ANISOU 3147 CB GLU A1320 9433 3575 5797 -1192 215 -232 C ATOM 3148 CG GLU A1320 32.061-125.006 151.249 1.00 53.52 C ANISOU 3148 CG GLU A1320 10282 3857 6197 -1093 202 -191 C ATOM 3149 CD GLU A1320 31.443-125.157 152.624 1.00 63.77 C ANISOU 3149 CD GLU A1320 11551 5187 7490 -1274 238 -81 C ATOM 3150 OE1 GLU A1320 30.391-124.533 152.877 1.00 67.63 O ANISOU 3150 OE1 GLU A1320 11784 5865 8047 -1505 268 -39 O ATOM 3151 OE2 GLU A1320 32.008-125.904 153.450 1.00 68.26 O ANISOU 3151 OE2 GLU A1320 12351 5605 7977 -1173 238 -33 O ATOM 3152 N PHE A1321 30.400-121.009 149.609 1.00 48.47 N ANISOU 3152 N PHE A1321 8492 4005 5921 -1272 292 -273 N ATOM 3153 CA PHE A1321 30.024-120.038 148.587 1.00 46.46 C ANISOU 3153 CA PHE A1321 7997 3910 5745 -1289 284 -316 C ATOM 3154 C PHE A1321 30.696-118.692 148.823 1.00 44.68 C ANISOU 3154 C PHE A1321 7498 3867 5610 -1085 346 -337 C ATOM 3155 O PHE A1321 31.019-117.986 147.861 1.00 45.31 O ANISOU 3155 O PHE A1321 7457 4024 5733 -989 334 -385 O ATOM 3156 CB PHE A1321 28.504-119.880 148.543 1.00 55.00 C ANISOU 3156 CB PHE A1321 8929 5112 6856 -1583 270 -264 C ATOM 3157 CG PHE A1321 28.010-119.112 147.349 1.00 69.22 C ANISOU 3157 CG PHE A1321 10536 7050 8715 -1621 240 -300 C ATOM 3158 CD1 PHE A1321 28.187-119.609 146.068 1.00 74.13 C ANISOU 3158 CD1 PHE A1321 11318 7560 9286 -1626 165 -358 C ATOM 3159 CD2 PHE A1321 27.361-117.898 147.507 1.00 75.20 C ANISOU 3159 CD2 PHE A1321 10964 8045 9565 -1638 284 -276 C ATOM 3160 CE1 PHE A1321 27.733-118.907 144.966 1.00 78.44 C ANISOU 3160 CE1 PHE A1321 11686 8240 9877 -1661 134 -384 C ATOM 3161 CE2 PHE A1321 26.904-117.192 146.408 1.00 75.52 C ANISOU 3161 CE2 PHE A1321 10833 8208 9652 -1660 252 -300 C ATOM 3162 CZ PHE A1321 27.090-117.698 145.137 1.00 76.32 C ANISOU 3162 CZ PHE A1321 11085 8207 9706 -1679 176 -350 C ATOM 3163 N VAL A1322 30.914-118.321 150.087 1.00 44.37 N ANISOU 3163 N VAL A1322 7371 3894 5591 -1029 407 -300 N ATOM 3164 CA VAL A1322 31.645-117.093 150.384 1.00 43.15 C ANISOU 3164 CA VAL A1322 7001 3886 5507 -846 454 -323 C ATOM 3165 C VAL A1322 33.080-117.199 149.884 1.00 47.47 C ANISOU 3165 C VAL A1322 7640 4379 6017 -611 438 -368 C ATOM 3166 O VAL A1322 33.631-116.244 149.320 1.00 47.32 O ANISOU 3166 O VAL A1322 7460 4472 6050 -499 442 -400 O ATOM 3167 CB VAL A1322 31.589-116.790 151.893 1.00 33.97 C ANISOU 3167 CB VAL A1322 5764 2794 4351 -842 515 -279 C ATOM 3168 CG1 VAL A1322 32.416-115.556 152.224 1.00 32.52 C ANISOU 3168 CG1 VAL A1322 5396 2737 4224 -667 549 -309 C ATOM 3169 CG2 VAL A1322 30.150-116.607 152.340 1.00 34.55 C ANISOU 3169 CG2 VAL A1322 5709 2969 4448 -1056 541 -231 C ATOM 3170 N ARG A1323 33.705-118.364 150.075 1.00 50.39 N ANISOU 3170 N ARG A1323 8272 4585 6288 -530 419 -364 N ATOM 3171 CA ARG A1323 35.057-118.570 149.569 1.00 45.42 C ANISOU 3171 CA ARG A1323 7728 3927 5601 -283 408 -402 C ATOM 3172 C ARG A1323 35.090-118.512 148.048 1.00 46.46 C ANISOU 3172 C ARG A1323 7866 4058 5728 -261 368 -458 C ATOM 3173 O ARG A1323 36.061-118.023 147.459 1.00 47.42 O ANISOU 3173 O ARG A1323 7900 4275 5842 -80 373 -486 O ATOM 3174 CB ARG A1323 35.604-119.907 150.072 1.00 36.80 C ANISOU 3174 CB ARG A1323 6945 2648 4391 -184 393 -384 C ATOM 3175 CG ARG A1323 37.013-120.219 149.595 1.00 42.12 C ANISOU 3175 CG ARG A1323 7711 3312 4981 108 385 -417 C ATOM 3176 CD ARG A1323 37.500-121.545 150.151 1.00 45.49 C ANISOU 3176 CD ARG A1323 8459 3541 5283 230 369 -395 C ATOM 3177 NE ARG A1323 36.666-122.657 149.709 1.00 45.62 N ANISOU 3177 NE ARG A1323 8776 3314 5241 76 315 -406 N ATOM 3178 CZ ARG A1323 36.767-123.897 150.175 1.00 50.69 C ANISOU 3178 CZ ARG A1323 9757 3727 5777 111 286 -379 C ATOM 3179 NH1 ARG A1323 37.667-124.185 151.104 1.00 48.74 N ANISOU 3179 NH1 ARG A1323 9574 3475 5470 317 310 -337 N ATOM 3180 NH2 ARG A1323 35.966-124.848 149.716 1.00 57.75 N ANISOU 3180 NH2 ARG A1323 10935 4392 6616 -67 224 -389 N ATOM 3181 N GLU A1324 34.039-119.011 147.395 1.00 48.52 N ANISOU 3181 N GLU A1324 8225 4228 5981 -455 324 -468 N ATOM 3182 CA GLU A1324 33.952-118.909 145.943 1.00 49.64 C ANISOU 3182 CA GLU A1324 8364 4382 6114 -456 282 -522 C ATOM 3183 C GLU A1324 33.923-117.451 145.499 1.00 45.15 C ANISOU 3183 C GLU A1324 7476 4028 5651 -444 304 -524 C ATOM 3184 O GLU A1324 34.496-117.096 144.462 1.00 38.83 O ANISOU 3184 O GLU A1324 6626 3291 4837 -332 290 -560 O ATOM 3185 CB GLU A1324 32.711-119.649 145.444 1.00 60.60 C ANISOU 3185 CB GLU A1324 9897 5652 7474 -710 222 -524 C ATOM 3186 CG GLU A1324 32.824-120.196 144.031 1.00 77.62 C ANISOU 3186 CG GLU A1324 12224 7717 9551 -684 160 -592 C ATOM 3187 CD GLU A1324 33.776-121.374 143.938 1.00 92.66 C ANISOU 3187 CD GLU A1324 14468 9417 11320 -491 140 -634 C ATOM 3188 OE1 GLU A1324 34.744-121.299 143.152 1.00 95.75 O ANISOU 3188 OE1 GLU A1324 14879 9843 11657 -259 145 -688 O ATOM 3189 OE2 GLU A1324 33.556-122.374 144.656 1.00 96.13 O ANISOU 3189 OE2 GLU A1324 15159 9668 11699 -562 120 -608 O ATOM 3190 N LEU A1325 33.272-116.589 146.283 1.00 42.07 N ANISOU 3190 N LEU A1325 6878 3752 5356 -549 338 -482 N ATOM 3191 CA LEU A1325 33.204-115.173 145.940 1.00 33.41 C ANISOU 3191 CA LEU A1325 5510 2831 4355 -533 354 -481 C ATOM 3192 C LEU A1325 34.537-114.475 146.188 1.00 39.05 C ANISOU 3192 C LEU A1325 6132 3629 5075 -332 382 -485 C ATOM 3193 O LEU A1325 34.977-113.664 145.365 1.00 42.67 O ANISOU 3193 O LEU A1325 6465 4188 5561 -268 372 -495 O ATOM 3194 CB LEU A1325 32.084-114.501 146.733 1.00 40.16 C ANISOU 3194 CB LEU A1325 6196 3774 5291 -680 382 -442 C ATOM 3195 CG LEU A1325 30.657-114.834 146.291 1.00 44.57 C ANISOU 3195 CG LEU A1325 6743 4337 5854 -898 350 -425 C ATOM 3196 CD1 LEU A1325 29.697-114.725 147.458 1.00 40.04 C ANISOU 3196 CD1 LEU A1325 6079 3826 5307 -1026 391 -374 C ATOM 3197 CD2 LEU A1325 30.228-113.909 145.165 1.00 46.30 C ANISOU 3197 CD2 LEU A1325 6786 4673 6132 -916 321 -436 C ATOM 3198 N TYR A1326 35.189-114.770 147.317 1.00 37.24 N ANISOU 3198 N TYR A1326 5962 3374 4813 -245 414 -466 N ATOM 3199 CA TYR A1326 36.496-114.178 147.597 1.00 30.37 C ANISOU 3199 CA TYR A1326 5002 2605 3931 -72 432 -461 C ATOM 3200 C TYR A1326 37.499-114.500 146.495 1.00 32.22 C ANISOU 3200 C TYR A1326 5290 2861 4089 84 411 -485 C ATOM 3201 O TYR A1326 38.352-113.669 146.160 1.00 35.35 O ANISOU 3201 O TYR A1326 5537 3401 4494 174 414 -476 O ATOM 3202 CB TYR A1326 37.030-114.674 148.939 1.00 35.10 C ANISOU 3202 CB TYR A1326 5685 3169 4481 1 459 -435 C ATOM 3203 CG TYR A1326 36.349-114.119 150.168 1.00 39.46 C ANISOU 3203 CG TYR A1326 6144 3753 5094 -108 491 -410 C ATOM 3204 CD1 TYR A1326 35.658-112.916 150.129 1.00 29.48 C ANISOU 3204 CD1 TYR A1326 4690 2584 3927 -202 500 -415 C ATOM 3205 CD2 TYR A1326 36.415-114.798 151.379 1.00 31.04 C ANISOU 3205 CD2 TYR A1326 5191 2626 3976 -98 514 -381 C ATOM 3206 CE1 TYR A1326 35.039-112.411 151.259 1.00 32.65 C ANISOU 3206 CE1 TYR A1326 5016 3023 4366 -272 535 -401 C ATOM 3207 CE2 TYR A1326 35.803-114.303 152.513 1.00 30.68 C ANISOU 3207 CE2 TYR A1326 5061 2628 3969 -188 549 -360 C ATOM 3208 CZ TYR A1326 35.117-113.111 152.450 1.00 35.20 C ANISOU 3208 CZ TYR A1326 5444 3300 4631 -268 562 -375 C ATOM 3209 OH TYR A1326 34.510-112.620 153.584 1.00 42.00 O ANISOU 3209 OH TYR A1326 6229 4215 5513 -329 603 -362 O ATOM 3210 N GLY A1327 37.423-115.703 145.932 1.00 31.88 N ANISOU 3210 N GLY A1327 5470 2683 3960 116 388 -513 N ATOM 3211 CA GLY A1327 38.335-116.146 144.901 1.00 44.31 C ANISOU 3211 CA GLY A1327 7126 4274 5436 292 374 -545 C ATOM 3212 C GLY A1327 37.913-115.832 143.483 1.00 49.69 C ANISOU 3212 C GLY A1327 7760 4991 6128 230 344 -577 C ATOM 3213 O GLY A1327 38.572-116.284 142.542 1.00 56.25 O ANISOU 3213 O GLY A1327 8678 5832 6861 374 334 -611 O ATOM 3214 N SER A1328 36.837-115.075 143.298 1.00 42.58 N ANISOU 3214 N SER A1328 6724 4123 5333 37 331 -566 N ATOM 3215 CA SER A1328 36.344-114.715 141.974 1.00 39.48 C ANISOU 3215 CA SER A1328 6273 3776 4953 -34 296 -587 C ATOM 3216 C SER A1328 36.253-113.215 141.757 1.00 40.55 C ANISOU 3216 C SER A1328 6142 4075 5192 -81 301 -551 C ATOM 3217 O SER A1328 36.555-112.737 140.660 1.00 40.71 O ANISOU 3217 O SER A1328 6085 4189 5196 -45 284 -552 O ATOM 3218 CB SER A1328 34.964-115.342 141.733 1.00 41.54 C ANISOU 3218 CB SER A1328 6649 3914 5222 -237 255 -605 C ATOM 3219 OG SER A1328 35.028-116.754 141.801 1.00 53.71 O ANISOU 3219 OG SER A1328 8480 5271 6655 -214 234 -639 O ATOM 3220 N VAL A1329 35.845-112.455 142.772 1.00 33.69 N ANISOU 3220 N VAL A1329 5145 3237 4418 -157 323 -517 N ATOM 3221 CA VAL A1329 35.710-111.010 142.639 1.00 31.35 C ANISOU 3221 CA VAL A1329 4636 3061 4216 -196 322 -485 C ATOM 3222 C VAL A1329 37.090-110.378 142.520 1.00 28.36 C ANISOU 3222 C VAL A1329 4170 2797 3810 -67 331 -462 C ATOM 3223 O VAL A1329 38.112-111.039 142.735 1.00 43.71 O ANISOU 3223 O VAL A1329 6191 4751 5666 63 348 -467 O ATOM 3224 CB VAL A1329 34.934-110.409 143.825 1.00 38.26 C ANISOU 3224 CB VAL A1329 5427 3930 5181 -284 345 -465 C ATOM 3225 CG1 VAL A1329 33.598-111.114 144.003 1.00 30.92 C ANISOU 3225 CG1 VAL A1329 4564 2926 4260 -423 340 -472 C ATOM 3226 CG2 VAL A1329 35.771-110.488 145.090 1.00 29.07 C ANISOU 3226 CG2 VAL A1329 4288 2761 3997 -202 381 -457 C ATOM 3227 N ASP A1330 37.126-109.093 142.179 1.00 34.59 N ANISOU 3227 N ASP A1330 4799 3681 4664 -104 317 -428 N ATOM 3228 CA ASP A1330 38.373-108.350 142.070 1.00 33.40 C ANISOU 3228 CA ASP A1330 4547 3656 4487 -32 316 -390 C ATOM 3229 C ASP A1330 38.721-107.601 143.345 1.00 36.90 C ANISOU 3229 C ASP A1330 4924 4117 4979 -48 327 -368 C ATOM 3230 O ASP A1330 39.884-107.595 143.756 1.00 44.64 O ANISOU 3230 O ASP A1330 5878 5183 5901 27 334 -345 O ATOM 3231 CB ASP A1330 38.295-107.363 140.901 1.00 35.29 C ANISOU 3231 CB ASP A1330 4675 3980 4755 -81 282 -354 C ATOM 3232 CG ASP A1330 38.077-108.052 139.571 1.00 39.80 C ANISOU 3232 CG ASP A1330 5307 4558 5259 -59 266 -377 C ATOM 3233 OD1 ASP A1330 38.850-108.980 139.248 1.00 43.46 O ANISOU 3233 OD1 ASP A1330 5854 5047 5611 58 282 -400 O ATOM 3234 OD2 ASP A1330 37.131-107.672 138.850 1.00 41.91 O ANISOU 3234 OD2 ASP A1330 5541 4808 5573 -146 236 -374 O ATOM 3235 N PHE A1331 37.738-106.967 143.979 1.00 32.27 N ANISOU 3235 N PHE A1331 4310 3467 4486 -138 327 -374 N ATOM 3236 CA PHE A1331 37.971-106.187 145.183 1.00 28.06 C ANISOU 3236 CA PHE A1331 3735 2937 3990 -155 334 -366 C ATOM 3237 C PHE A1331 36.883-106.485 146.202 1.00 34.29 C ANISOU 3237 C PHE A1331 4572 3634 4821 -195 365 -397 C ATOM 3238 O PHE A1331 35.726-106.722 145.847 1.00 37.97 O ANISOU 3238 O PHE A1331 5047 4058 5323 -250 369 -410 O ATOM 3239 CB PHE A1331 38.008-104.679 144.887 1.00 29.25 C ANISOU 3239 CB PHE A1331 3789 3123 4203 -213 296 -334 C ATOM 3240 CG PHE A1331 39.095-104.274 143.930 1.00 30.81 C ANISOU 3240 CG PHE A1331 3922 3433 4352 -203 263 -285 C ATOM 3241 CD1 PHE A1331 38.875-104.290 142.562 1.00 36.21 C ANISOU 3241 CD1 PHE A1331 4581 4151 5026 -210 245 -266 C ATOM 3242 CD2 PHE A1331 40.334-103.869 144.399 1.00 31.92 C ANISOU 3242 CD2 PHE A1331 4017 3668 4444 -197 249 -249 C ATOM 3243 CE1 PHE A1331 39.870-103.919 141.680 1.00 36.53 C ANISOU 3243 CE1 PHE A1331 4551 4318 5009 -205 222 -211 C ATOM 3244 CE2 PHE A1331 41.336-103.496 143.521 1.00 34.04 C ANISOU 3244 CE2 PHE A1331 4203 4076 4654 -204 222 -188 C ATOM 3245 CZ PHE A1331 41.103-103.521 142.159 1.00 38.30 C ANISOU 3245 CZ PHE A1331 4718 4650 5183 -204 212 -168 C ATOM 3246 N VAL A1332 37.270-106.474 147.476 1.00 31.11 N ANISOU 3246 N VAL A1332 4192 3227 4403 -172 386 -404 N ATOM 3247 CA VAL A1332 36.344-106.605 148.595 1.00 27.58 C ANISOU 3247 CA VAL A1332 3775 2722 3983 -207 422 -426 C ATOM 3248 C VAL A1332 36.333-105.285 149.351 1.00 31.41 C ANISOU 3248 C VAL A1332 4201 3221 4512 -221 415 -434 C ATOM 3249 O VAL A1332 37.392-104.772 149.732 1.00 34.40 O ANISOU 3249 O VAL A1332 4568 3640 4864 -201 392 -424 O ATOM 3250 CB VAL A1332 36.729-107.769 149.523 1.00 35.87 C ANISOU 3250 CB VAL A1332 4928 3742 4961 -165 454 -429 C ATOM 3251 CG1 VAL A1332 35.874-107.748 150.783 1.00 27.05 C ANISOU 3251 CG1 VAL A1332 3824 2593 3859 -207 494 -441 C ATOM 3252 CG2 VAL A1332 36.568-109.089 148.801 1.00 35.44 C ANISOU 3252 CG2 VAL A1332 4978 3631 4857 -155 455 -429 C ATOM 3253 N ILE A1333 35.141-104.736 149.562 1.00 31.24 N ANISOU 3253 N ILE A1333 4148 3174 4549 -252 431 -450 N ATOM 3254 CA ILE A1333 34.974-103.443 150.213 1.00 34.29 C ANISOU 3254 CA ILE A1333 4509 3550 4972 -243 423 -469 C ATOM 3255 C ILE A1333 34.619-103.680 151.674 1.00 38.01 C ANISOU 3255 C ILE A1333 5016 4014 5412 -226 473 -499 C ATOM 3256 O ILE A1333 33.608-104.324 151.982 1.00 38.21 O ANISOU 3256 O ILE A1333 5036 4047 5434 -241 521 -501 O ATOM 3257 CB ILE A1333 33.903-102.595 149.510 1.00 26.86 C ANISOU 3257 CB ILE A1333 3509 2598 4098 -246 410 -468 C ATOM 3258 CG1 ILE A1333 34.303-102.345 148.056 1.00 26.63 C ANISOU 3258 CG1 ILE A1333 3448 2582 4089 -267 357 -431 C ATOM 3259 CG2 ILE A1333 33.701-101.280 150.245 1.00 27.29 C ANISOU 3259 CG2 ILE A1333 3577 2614 4176 -208 401 -497 C ATOM 3260 CD1 ILE A1333 33.300-101.527 147.275 1.00 26.92 C ANISOU 3260 CD1 ILE A1333 3430 2612 4184 -262 335 -418 C ATOM 3261 N ILE A1334 35.449-103.161 152.573 1.00 38.19 N ANISOU 3261 N ILE A1334 5074 4035 5402 -209 459 -516 N ATOM 3262 CA ILE A1334 35.242-103.308 154.011 1.00 35.37 C ANISOU 3262 CA ILE A1334 4758 3681 4999 -188 503 -546 C ATOM 3263 C ILE A1334 35.173-101.916 154.629 1.00 39.41 C ANISOU 3263 C ILE A1334 5290 4162 5522 -167 482 -591 C ATOM 3264 O ILE A1334 36.172-101.430 155.177 1.00 37.32 O ANISOU 3264 O ILE A1334 5068 3894 5217 -180 441 -603 O ATOM 3265 CB ILE A1334 36.356-104.154 154.649 1.00 31.62 C ANISOU 3265 CB ILE A1334 4333 3235 4448 -179 501 -528 C ATOM 3266 CG1 ILE A1334 36.629-105.396 153.796 1.00 35.82 C ANISOU 3266 CG1 ILE A1334 4877 3772 4962 -175 503 -488 C ATOM 3267 CG2 ILE A1334 35.972-104.559 156.061 1.00 27.88 C ANISOU 3267 CG2 ILE A1334 3905 2770 3920 -164 554 -547 C ATOM 3268 CD1 ILE A1334 37.802-106.222 154.263 1.00 35.90 C ANISOU 3268 CD1 ILE A1334 4937 3816 4888 -128 496 -464 C ATOM 3269 N PRO A1335 34.023-101.233 154.558 1.00 40.03 N ANISOU 3269 N PRO A1335 5345 4221 5643 -129 504 -617 N ATOM 3270 CA PRO A1335 33.918 -99.847 155.028 1.00 38.44 C ANISOU 3270 CA PRO A1335 5197 3961 5446 -84 477 -666 C ATOM 3271 C PRO A1335 33.466 -99.732 156.483 1.00 40.51 C ANISOU 3271 C PRO A1335 5506 4240 5647 -24 532 -723 C ATOM 3272 O PRO A1335 32.547 -98.974 156.813 1.00 40.42 O ANISOU 3272 O PRO A1335 5506 4215 5639 62 560 -766 O ATOM 3273 CB PRO A1335 32.884 -99.250 154.069 1.00 34.73 C ANISOU 3273 CB PRO A1335 4676 3475 5045 -40 474 -657 C ATOM 3274 CG PRO A1335 31.956-100.402 153.811 1.00 38.03 C ANISOU 3274 CG PRO A1335 5000 3981 5469 -51 538 -626 C ATOM 3275 CD PRO A1335 32.789-101.673 153.885 1.00 36.01 C ANISOU 3275 CD PRO A1335 4760 3748 5176 -125 543 -595 C ATOM 3276 N SER A1336 34.115-100.484 157.367 1.00 41.07 N ANISOU 3276 N SER A1336 5606 4348 5651 -54 550 -721 N ATOM 3277 CA SER A1336 33.733-100.492 158.772 1.00 41.02 C ANISOU 3277 CA SER A1336 5642 4374 5570 -5 606 -767 C ATOM 3278 C SER A1336 34.032 -99.150 159.431 1.00 41.83 C ANISOU 3278 C SER A1336 5849 4405 5639 36 561 -842 C ATOM 3279 O SER A1336 35.006 -98.470 159.098 1.00 43.51 O ANISOU 3279 O SER A1336 6120 4551 5861 -20 473 -844 O ATOM 3280 CB SER A1336 34.471-101.605 159.517 1.00 44.19 C ANISOU 3280 CB SER A1336 6063 4828 5901 -48 622 -737 C ATOM 3281 OG SER A1336 34.265-102.860 158.896 1.00 53.87 O ANISOU 3281 OG SER A1336 7236 6085 7147 -87 651 -672 O ATOM 3282 N TYR A1337 33.171 -98.763 160.373 1.00 43.83 N ANISOU 3282 N TYR A1337 6134 4677 5842 131 621 -902 N ATOM 3283 CA TYR A1337 33.482 -97.614 161.217 1.00 55.00 C ANISOU 3283 CA TYR A1337 7689 6014 7196 178 581 -988 C ATOM 3284 C TYR A1337 34.520 -97.976 162.271 1.00 56.94 C ANISOU 3284 C TYR A1337 7998 6289 7349 111 557 -1000 C ATOM 3285 O TYR A1337 35.378 -97.155 162.614 1.00 57.03 O ANISOU 3285 O TYR A1337 8124 6225 7319 66 473 -1044 O ATOM 3286 CB TYR A1337 32.212 -97.076 161.875 1.00 56.78 C ANISOU 3286 CB TYR A1337 7931 6265 7378 334 658 -1055 C ATOM 3287 CG TYR A1337 31.370 -96.215 160.963 1.00 60.77 C ANISOU 3287 CG TYR A1337 8424 6713 7955 432 649 -1064 C ATOM 3288 CD1 TYR A1337 30.434 -96.782 160.110 1.00 62.18 C ANISOU 3288 CD1 TYR A1337 8442 6985 8198 452 702 -999 C ATOM 3289 CD2 TYR A1337 31.513 -94.833 160.955 1.00 61.69 C ANISOU 3289 CD2 TYR A1337 8700 6676 8063 502 580 -1135 C ATOM 3290 CE1 TYR A1337 29.661 -95.998 159.274 1.00 64.26 C ANISOU 3290 CE1 TYR A1337 8683 7214 8517 553 690 -1000 C ATOM 3291 CE2 TYR A1337 30.745 -94.040 160.122 1.00 62.88 C ANISOU 3291 CE2 TYR A1337 8853 6766 8272 612 568 -1136 C ATOM 3292 CZ TYR A1337 29.821 -94.628 159.285 1.00 60.90 C ANISOU 3292 CZ TYR A1337 8420 6634 8086 644 625 -1066 C ATOM 3293 OH TYR A1337 29.053 -93.846 158.454 1.00 52.14 O ANISOU 3293 OH TYR A1337 7302 5482 7026 764 610 -1059 O ATOM 3294 N PHE A1338 34.455 -99.199 162.792 1.00 56.46 N ANISOU 3294 N PHE A1338 7871 6336 7246 95 623 -956 N ATOM 3295 CA PHE A1338 35.482 -99.717 163.681 1.00 60.11 C ANISOU 3295 CA PHE A1338 8376 6844 7621 38 598 -945 C ATOM 3296 C PHE A1338 35.605-101.215 163.450 1.00 58.16 C ANISOU 3296 C PHE A1338 8043 6673 7381 0 639 -854 C ATOM 3297 O PHE A1338 34.605-101.899 163.212 1.00 52.16 O ANISOU 3297 O PHE A1338 7217 5951 6649 20 716 -819 O ATOM 3298 CB PHE A1338 35.175 -99.415 165.154 1.00 65.52 C ANISOU 3298 CB PHE A1338 9143 7562 8188 102 640 -1019 C ATOM 3299 CG PHE A1338 33.781 -99.783 165.577 1.00 72.15 C ANISOU 3299 CG PHE A1338 9927 8483 9006 196 760 -1024 C ATOM 3300 CD1 PHE A1338 33.498-101.055 166.049 1.00 76.27 C ANISOU 3300 CD1 PHE A1338 10383 9113 9484 170 834 -956 C ATOM 3301 CD2 PHE A1338 32.758 -98.851 165.519 1.00 74.64 C ANISOU 3301 CD2 PHE A1338 10254 8774 9330 311 796 -1090 C ATOM 3302 CE1 PHE A1338 32.217-101.393 166.443 1.00 82.83 C ANISOU 3302 CE1 PHE A1338 11144 10045 10281 228 943 -946 C ATOM 3303 CE2 PHE A1338 31.476 -99.183 165.913 1.00 79.85 C ANISOU 3303 CE2 PHE A1338 10830 9555 9955 400 910 -1085 C ATOM 3304 CZ PHE A1338 31.205-100.455 166.376 1.00 84.33 C ANISOU 3304 CZ PHE A1338 11315 10249 10478 343 984 -1009 C ATOM 3305 N GLU A1339 36.834-101.711 163.509 1.00 58.74 N ANISOU 3305 N GLU A1339 8126 6773 7421 -56 583 -811 N ATOM 3306 CA GLU A1339 37.120-103.122 163.253 1.00 59.60 C ANISOU 3306 CA GLU A1339 8192 6930 7524 -71 608 -726 C ATOM 3307 C GLU A1339 38.394-103.472 164.006 1.00 60.02 C ANISOU 3307 C GLU A1339 8279 7044 7481 -85 559 -701 C ATOM 3308 O GLU A1339 39.507-103.228 163.514 1.00 63.26 O ANISOU 3308 O GLU A1339 8666 7476 7894 -119 480 -679 O ATOM 3309 CB GLU A1339 37.264-103.407 161.761 1.00 63.90 C ANISOU 3309 CB GLU A1339 8674 7441 8163 -95 581 -678 C ATOM 3310 CG GLU A1339 37.352-104.881 161.419 1.00 70.24 C ANISOU 3310 CG GLU A1339 9467 8262 8958 -92 612 -603 C ATOM 3311 CD GLU A1339 36.089-105.638 161.777 1.00 79.84 C ANISOU 3311 CD GLU A1339 10690 9478 10168 -95 698 -587 C ATOM 3312 OE1 GLU A1339 34.989-105.174 161.408 1.00 82.78 O ANISOU 3312 OE1 GLU A1339 11013 9841 10597 -101 733 -612 O ATOM 3313 OE2 GLU A1339 36.196-106.694 162.435 1.00 84.69 O ANISOU 3313 OE2 GLU A1339 11355 10111 10712 -94 729 -541 O ATOM 3314 N PRO A1340 38.276-104.042 165.207 1.00 59.91 N ANISOU 3314 N PRO A1340 8309 7082 7371 -59 603 -696 N ATOM 3315 CA PRO A1340 39.481-104.282 166.017 1.00 59.60 C ANISOU 3315 CA PRO A1340 8301 7119 7227 -64 549 -673 C ATOM 3316 C PRO A1340 40.404-105.344 165.446 1.00 58.88 C ANISOU 3316 C PRO A1340 8175 7068 7130 -44 521 -582 C ATOM 3317 O PRO A1340 41.625-105.236 165.615 1.00 62.94 O ANISOU 3317 O PRO A1340 8667 7664 7582 -50 447 -558 O ATOM 3318 CB PRO A1340 38.908-104.705 167.377 1.00 61.24 C ANISOU 3318 CB PRO A1340 8566 7369 7334 -32 617 -682 C ATOM 3319 CG PRO A1340 37.551-105.246 167.063 1.00 61.88 C ANISOU 3319 CG PRO A1340 8626 7415 7471 -20 714 -663 C ATOM 3320 CD PRO A1340 37.042-104.428 165.913 1.00 61.03 C ANISOU 3320 CD PRO A1340 8466 7239 7483 -31 702 -704 C ATOM 3321 N PHE A1341 39.871-106.361 164.776 1.00 47.95 N ANISOU 3321 N PHE A1341 6788 5638 5795 -18 572 -531 N ATOM 3322 CA PHE A1341 40.687-107.482 164.324 1.00 44.78 C ANISOU 3322 CA PHE A1341 6391 5258 5366 36 553 -451 C ATOM 3323 C PHE A1341 40.754-107.617 162.811 1.00 45.77 C ANISOU 3323 C PHE A1341 6469 5339 5582 40 537 -434 C ATOM 3324 O PHE A1341 41.823-107.919 162.276 1.00 45.20 O ANISOU 3324 O PHE A1341 6363 5326 5484 90 490 -393 O ATOM 3325 CB PHE A1341 40.162-108.786 164.940 1.00 49.03 C ANISOU 3325 CB PHE A1341 7019 5762 5847 69 616 -396 C ATOM 3326 CG PHE A1341 39.917-108.693 166.419 1.00 57.06 C ANISOU 3326 CG PHE A1341 8083 6829 6769 61 645 -408 C ATOM 3327 CD1 PHE A1341 40.961-108.430 167.291 1.00 60.91 C ANISOU 3327 CD1 PHE A1341 8572 7415 7155 90 592 -406 C ATOM 3328 CD2 PHE A1341 38.644-108.862 166.939 1.00 58.38 C ANISOU 3328 CD2 PHE A1341 8280 6967 6933 20 726 -416 C ATOM 3329 CE1 PHE A1341 40.742-108.338 168.653 1.00 62.19 C ANISOU 3329 CE1 PHE A1341 8783 7629 7217 84 617 -420 C ATOM 3330 CE2 PHE A1341 38.418-108.772 168.301 1.00 61.58 C ANISOU 3330 CE2 PHE A1341 8724 7437 7236 20 760 -426 C ATOM 3331 CZ PHE A1341 39.470-108.511 169.159 1.00 62.89 C ANISOU 3331 CZ PHE A1341 8910 7684 7303 55 705 -432 C ATOM 3332 N GLY A1342 39.647-107.405 162.107 1.00 43.95 N ANISOU 3332 N GLY A1342 6226 5028 5447 -3 575 -462 N ATOM 3333 CA GLY A1342 39.658-107.461 160.655 1.00 40.48 C ANISOU 3333 CA GLY A1342 5743 4552 5087 -6 556 -451 C ATOM 3334 C GLY A1342 39.875-108.841 160.073 1.00 43.73 C ANISOU 3334 C GLY A1342 6213 4928 5475 52 568 -394 C ATOM 3335 O GLY A1342 40.653-108.993 159.122 1.00 41.46 O ANISOU 3335 O GLY A1342 5895 4668 5192 99 530 -373 O ATOM 3336 N LEU A1343 39.204-109.857 160.620 1.00 45.75 N ANISOU 3336 N LEU A1343 6565 5122 5694 49 617 -366 N ATOM 3337 CA LEU A1343 39.361-111.212 160.106 1.00 52.57 C ANISOU 3337 CA LEU A1343 7535 5913 6525 102 620 -315 C ATOM 3338 C LEU A1343 38.745-111.382 158.722 1.00 53.60 C ANISOU 3338 C LEU A1343 7662 5969 6735 61 619 -328 C ATOM 3339 O LEU A1343 39.164-112.275 157.979 1.00 55.11 O ANISOU 3339 O LEU A1343 7935 6107 6898 127 602 -304 O ATOM 3340 CB LEU A1343 38.749-112.219 161.081 1.00 62.38 C ANISOU 3340 CB LEU A1343 8906 7094 7703 77 664 -273 C ATOM 3341 CG LEU A1343 39.323-112.219 162.502 1.00 70.09 C ANISOU 3341 CG LEU A1343 9906 8143 8581 123 666 -251 C ATOM 3342 CD1 LEU A1343 38.607-113.237 163.374 1.00 74.22 C ANISOU 3342 CD1 LEU A1343 10560 8600 9039 80 713 -196 C ATOM 3343 CD2 LEU A1343 40.821-112.484 162.488 1.00 71.61 C ANISOU 3343 CD2 LEU A1343 10103 8405 8701 262 612 -220 C ATOM 3344 N VAL A1344 37.763-110.552 158.363 1.00 48.94 N ANISOU 3344 N VAL A1344 6986 5378 6231 -33 636 -366 N ATOM 3345 CA VAL A1344 37.191-110.614 157.021 1.00 46.90 C ANISOU 3345 CA VAL A1344 6706 5070 6043 -76 627 -376 C ATOM 3346 C VAL A1344 38.237-110.229 155.983 1.00 47.20 C ANISOU 3346 C VAL A1344 6689 5150 6094 -5 577 -383 C ATOM 3347 O VAL A1344 38.297-110.811 154.893 1.00 53.31 O ANISOU 3347 O VAL A1344 7502 5880 6871 16 561 -377 O ATOM 3348 CB VAL A1344 35.942-109.719 156.928 1.00 54.25 C ANISOU 3348 CB VAL A1344 7539 6019 7054 -169 653 -408 C ATOM 3349 CG1 VAL A1344 35.456-109.621 155.489 1.00 65.91 C ANISOU 3349 CG1 VAL A1344 8973 7469 8601 -208 631 -416 C ATOM 3350 CG2 VAL A1344 34.844-110.253 157.827 1.00 58.67 C ANISOU 3350 CG2 VAL A1344 8136 6571 7585 -244 710 -386 C ATOM 3351 N ALA A1345 39.081-109.248 156.307 1.00 40.04 N ANISOU 3351 N ALA A1345 5695 4336 5183 22 547 -394 N ATOM 3352 CA ALA A1345 40.142-108.852 155.389 1.00 32.55 C ANISOU 3352 CA ALA A1345 4674 3463 4230 71 500 -384 C ATOM 3353 C ALA A1345 41.114-109.998 155.147 1.00 35.69 C ANISOU 3353 C ALA A1345 5138 3886 4536 198 492 -345 C ATOM 3354 O ALA A1345 41.494-110.272 154.004 1.00 41.14 O ANISOU 3354 O ALA A1345 5818 4593 5219 251 477 -337 O ATOM 3355 CB ALA A1345 40.877-107.627 155.932 1.00 28.37 C ANISOU 3355 CB ALA A1345 4052 3032 3694 44 461 -391 C ATOM 3356 N LEU A1346 41.518-110.690 156.216 1.00 39.63 N ANISOU 3356 N LEU A1346 5713 4390 4953 264 503 -320 N ATOM 3357 CA LEU A1346 42.479-111.779 156.076 1.00 36.57 C ANISOU 3357 CA LEU A1346 5402 4028 4464 421 494 -279 C ATOM 3358 C LEU A1346 41.906-112.922 155.249 1.00 43.60 C ANISOU 3358 C LEU A1346 6445 4771 5351 456 512 -284 C ATOM 3359 O LEU A1346 42.634-113.573 154.491 1.00 51.85 O ANISOU 3359 O LEU A1346 7537 5832 6332 595 499 -272 O ATOM 3360 CB LEU A1346 42.910-112.273 157.456 1.00 38.83 C ANISOU 3360 CB LEU A1346 5753 4339 4662 484 500 -245 C ATOM 3361 CG LEU A1346 43.705-111.269 158.291 1.00 44.97 C ANISOU 3361 CG LEU A1346 6396 5280 5410 462 467 -239 C ATOM 3362 CD1 LEU A1346 43.964-111.809 159.689 1.00 31.93 C ANISOU 3362 CD1 LEU A1346 4821 3645 3667 514 474 -206 C ATOM 3363 CD2 LEU A1346 45.011-110.925 157.594 1.00 41.76 C ANISOU 3363 CD2 LEU A1346 5859 5052 4957 543 422 -209 C ATOM 3364 N GLU A1347 40.603-113.183 155.378 1.00 37.77 N ANISOU 3364 N GLU A1347 5788 3897 4668 330 539 -301 N ATOM 3365 CA GLU A1347 39.987-114.250 154.597 1.00 42.65 C ANISOU 3365 CA GLU A1347 6565 4364 5275 321 542 -305 C ATOM 3366 C GLU A1347 39.951-113.901 153.113 1.00 44.28 C ANISOU 3366 C GLU A1347 6707 4589 5527 315 521 -337 C ATOM 3367 O GLU A1347 40.264-114.744 152.263 1.00 42.48 O ANISOU 3367 O GLU A1347 6598 4300 5243 408 507 -344 O ATOM 3368 CB GLU A1347 38.579-114.534 155.119 1.00 43.52 C ANISOU 3368 CB GLU A1347 6745 4366 5425 152 570 -301 C ATOM 3369 CG GLU A1347 38.545-115.058 156.544 1.00 50.52 C ANISOU 3369 CG GLU A1347 7722 5224 6247 151 594 -259 C ATOM 3370 CD GLU A1347 37.150-115.055 157.136 1.00 56.32 C ANISOU 3370 CD GLU A1347 8461 5920 7019 -32 631 -248 C ATOM 3371 OE1 GLU A1347 36.192-114.711 156.412 1.00 59.56 O ANISOU 3371 OE1 GLU A1347 8804 6324 7503 -151 635 -271 O ATOM 3372 OE2 GLU A1347 37.011-115.394 158.328 1.00 62.36 O ANISOU 3372 OE2 GLU A1347 9285 6680 7730 -52 657 -209 O ATOM 3373 N ALA A1348 39.577-112.664 152.782 1.00 40.01 N ANISOU 3373 N ALA A1348 5994 4127 5079 216 517 -358 N ATOM 3374 CA ALA A1348 39.526-112.262 151.380 1.00 41.33 C ANISOU 3374 CA ALA A1348 6094 4322 5287 203 495 -379 C ATOM 3375 C ALA A1348 40.923-112.153 150.782 1.00 38.85 C ANISOU 3375 C ALA A1348 5719 4135 4907 351 474 -364 C ATOM 3376 O ALA A1348 41.135-112.514 149.619 1.00 45.68 O ANISOU 3376 O ALA A1348 6613 5001 5742 411 463 -375 O ATOM 3377 CB ALA A1348 38.776-110.937 151.238 1.00 39.67 C ANISOU 3377 CB ALA A1348 5731 4157 5185 74 493 -395 C ATOM 3378 N MET A1349 41.891-111.661 151.560 1.00 31.64 N ANISOU 3378 N MET A1349 4714 3350 3959 407 467 -336 N ATOM 3379 CA MET A1349 43.246-111.510 151.041 1.00 30.31 C ANISOU 3379 CA MET A1349 4451 3352 3715 534 447 -306 C ATOM 3380 C MET A1349 43.897-112.863 150.783 1.00 40.66 C ANISOU 3380 C MET A1349 5900 4645 4905 736 458 -296 C ATOM 3381 O MET A1349 44.660-113.015 149.822 1.00 45.82 O ANISOU 3381 O MET A1349 6512 5407 5492 858 453 -287 O ATOM 3382 CB MET A1349 44.091-110.681 152.007 1.00 31.40 C ANISOU 3382 CB MET A1349 4456 3643 3831 520 427 -272 C ATOM 3383 CG MET A1349 43.673-109.225 152.097 1.00 42.72 C ANISOU 3383 CG MET A1349 5769 5099 5364 345 404 -284 C ATOM 3384 SD MET A1349 44.522-108.346 153.417 1.00 42.62 S ANISOU 3384 SD MET A1349 5660 5220 5313 298 369 -259 S ATOM 3385 CE MET A1349 46.196-108.311 152.779 1.00 38.09 C ANISOU 3385 CE MET A1349 4940 4906 4627 397 333 -188 C ATOM 3386 N CYS A1350 43.610-113.858 151.628 1.00 40.15 N ANISOU 3386 N CYS A1350 6011 4446 4799 783 473 -294 N ATOM 3387 CA CYS A1350 44.136-115.200 151.400 1.00 35.02 C ANISOU 3387 CA CYS A1350 5544 3731 4029 987 478 -289 C ATOM 3388 C CYS A1350 43.612-115.814 150.110 1.00 33.29 C ANISOU 3388 C CYS A1350 5459 3384 3804 1000 475 -335 C ATOM 3389 O CYS A1350 44.244-116.728 149.569 1.00 37.40 O ANISOU 3389 O CYS A1350 6112 3887 4212 1203 474 -342 O ATOM 3390 CB CYS A1350 43.793-116.116 152.577 1.00 41.65 C ANISOU 3390 CB CYS A1350 6576 4418 4831 1003 487 -270 C ATOM 3391 SG CYS A1350 44.770-115.834 154.072 1.00 53.05 S ANISOU 3391 SG CYS A1350 7920 6026 6213 1084 484 -210 S ATOM 3392 N LEU A1351 42.480-115.334 149.603 1.00 36.04 N ANISOU 3392 N LEU A1351 5782 3651 4260 800 471 -368 N ATOM 3393 CA LEU A1351 41.884-115.860 148.386 1.00 43.20 C ANISOU 3393 CA LEU A1351 6810 4441 5161 777 458 -413 C ATOM 3394 C LEU A1351 42.098-114.953 147.180 1.00 43.50 C ANISOU 3394 C LEU A1351 6669 4626 5232 758 449 -424 C ATOM 3395 O LEU A1351 41.429-115.131 146.157 1.00 40.96 O ANISOU 3395 O LEU A1351 6410 4228 4926 693 434 -462 O ATOM 3396 CB LEU A1351 40.395-116.116 148.611 1.00 46.64 C ANISOU 3396 CB LEU A1351 7353 4694 5674 561 453 -431 C ATOM 3397 CG LEU A1351 40.175-117.359 149.471 1.00 54.50 C ANISOU 3397 CG LEU A1351 8599 5506 6601 584 454 -416 C ATOM 3398 CD1 LEU A1351 38.939-117.237 150.337 1.00 63.48 C ANISOU 3398 CD1 LEU A1351 9737 6565 7817 357 465 -396 C ATOM 3399 CD2 LEU A1351 40.083-118.583 148.580 1.00 50.83 C ANISOU 3399 CD2 LEU A1351 8403 4865 6043 656 427 -454 C ATOM 3400 N GLY A1352 43.017-113.991 147.274 1.00 42.21 N ANISOU 3400 N GLY A1352 6290 4676 5070 799 451 -386 N ATOM 3401 CA GLY A1352 43.398-113.175 146.143 1.00 45.92 C ANISOU 3401 CA GLY A1352 6596 5302 5548 791 441 -378 C ATOM 3402 C GLY A1352 42.596-111.907 145.947 1.00 49.36 C ANISOU 3402 C GLY A1352 6887 5749 6118 578 424 -375 C ATOM 3403 O GLY A1352 42.942-111.107 145.068 1.00 56.49 O ANISOU 3403 O GLY A1352 7650 6785 7029 554 410 -354 O ATOM 3404 N ALA A1353 41.539-111.693 146.724 1.00 39.82 N ANISOU 3404 N ALA A1353 5711 4415 5005 432 426 -389 N ATOM 3405 CA ALA A1353 40.733-110.488 146.585 1.00 38.51 C ANISOU 3405 CA ALA A1353 5419 4254 4957 264 412 -388 C ATOM 3406 C ALA A1353 41.449-109.302 147.218 1.00 40.98 C ANISOU 3406 C ALA A1353 5577 4697 5295 235 399 -351 C ATOM 3407 O ALA A1353 41.902-109.377 148.364 1.00 45.37 O ANISOU 3407 O ALA A1353 6140 5275 5825 266 408 -339 O ATOM 3408 CB ALA A1353 39.360-110.686 147.225 1.00 29.13 C ANISOU 3408 CB ALA A1353 4306 2919 3842 141 424 -413 C ATOM 3409 N ILE A1354 41.554-108.211 146.468 1.00 36.43 N ANISOU 3409 N ILE A1354 4875 4204 4763 165 372 -329 N ATOM 3410 CA ILE A1354 42.242-107.010 146.934 1.00 31.53 C ANISOU 3410 CA ILE A1354 4128 3692 4159 105 344 -289 C ATOM 3411 C ILE A1354 41.285-106.208 147.805 1.00 30.64 C ANISOU 3411 C ILE A1354 4025 3471 4146 -9 339 -316 C ATOM 3412 O ILE A1354 40.184-105.864 147.358 1.00 33.59 O ANISOU 3412 O ILE A1354 4409 3756 4598 -76 339 -337 O ATOM 3413 CB ILE A1354 42.760-106.174 145.755 1.00 31.82 C ANISOU 3413 CB ILE A1354 4048 3852 4190 64 310 -243 C ATOM 3414 CG1 ILE A1354 43.633-107.036 144.842 1.00 35.66 C ANISOU 3414 CG1 ILE A1354 4523 4466 4561 203 326 -223 C ATOM 3415 CG2 ILE A1354 43.528-104.961 146.257 1.00 31.15 C ANISOU 3415 CG2 ILE A1354 3856 3871 4110 -29 268 -194 C ATOM 3416 CD1 ILE A1354 43.951-106.393 143.512 1.00 28.82 C ANISOU 3416 CD1 ILE A1354 3552 3720 3677 165 304 -178 C ATOM 3417 N PRO A1355 41.649-105.892 149.044 1.00 36.60 N ANISOU 3417 N PRO A1355 4776 4240 4888 -23 336 -316 N ATOM 3418 CA PRO A1355 40.711-105.202 149.934 1.00 27.00 C ANISOU 3418 CA PRO A1355 3588 2923 3748 -102 341 -352 C ATOM 3419 C PRO A1355 40.729-103.687 149.769 1.00 42.16 C ANISOU 3419 C PRO A1355 5449 4848 5723 -197 293 -343 C ATOM 3420 O PRO A1355 41.774-103.069 149.549 1.00 27.36 O ANISOU 3420 O PRO A1355 3511 3075 3811 -235 246 -299 O ATOM 3421 CB PRO A1355 41.198-105.608 151.329 1.00 27.89 C ANISOU 3421 CB PRO A1355 3741 3055 3800 -63 356 -358 C ATOM 3422 CG PRO A1355 42.668-105.790 151.154 1.00 32.44 C ANISOU 3422 CG PRO A1355 4254 3787 4284 -5 328 -309 C ATOM 3423 CD PRO A1355 42.872-106.315 149.749 1.00 31.81 C ANISOU 3423 CD PRO A1355 4152 3750 4184 55 333 -287 C ATOM 3424 N ILE A1356 39.540-103.099 149.869 1.00 36.28 N ANISOU 3424 N ILE A1356 4730 3996 5058 -237 301 -378 N ATOM 3425 CA ILE A1356 39.352-101.654 149.972 1.00 32.96 C ANISOU 3425 CA ILE A1356 4306 3529 4687 -305 257 -383 C ATOM 3426 C ILE A1356 38.650-101.432 151.305 1.00 34.30 C ANISOU 3426 C ILE A1356 4538 3624 4869 -290 286 -440 C ATOM 3427 O ILE A1356 37.452-101.709 151.437 1.00 43.51 O ANISOU 3427 O ILE A1356 5719 4737 6075 -258 334 -471 O ATOM 3428 CB ILE A1356 38.531-101.084 148.808 1.00 34.57 C ANISOU 3428 CB ILE A1356 4487 3685 4963 -326 240 -371 C ATOM 3429 CG1 ILE A1356 39.194-101.400 147.467 1.00 31.24 C ANISOU 3429 CG1 ILE A1356 4005 3352 4514 -334 218 -315 C ATOM 3430 CG2 ILE A1356 38.340 -99.582 148.968 1.00 27.33 C ANISOU 3430 CG2 ILE A1356 3604 2692 4090 -376 189 -375 C ATOM 3431 CD1 ILE A1356 38.371-100.971 146.266 1.00 26.71 C ANISOU 3431 CD1 ILE A1356 3407 2742 3997 -351 202 -298 C ATOM 3432 N ALA A1357 39.383-100.946 152.304 1.00 32.88 N ANISOU 3432 N ALA A1357 4389 3460 4643 -317 258 -452 N ATOM 3433 CA ALA A1357 38.883-100.937 153.671 1.00 35.99 C ANISOU 3433 CA ALA A1357 4846 3809 5017 -289 293 -508 C ATOM 3434 C ALA A1357 39.143 -99.599 154.350 1.00 35.04 C ANISOU 3434 C ALA A1357 4790 3635 4886 -340 237 -542 C ATOM 3435 O ALA A1357 40.008 -98.821 153.940 1.00 37.48 O ANISOU 3435 O ALA A1357 5097 3960 5184 -423 161 -509 O ATOM 3436 CB ALA A1357 39.514-102.065 154.499 1.00 40.67 C ANISOU 3436 CB ALA A1357 5446 4476 5531 -251 324 -498 C ATOM 3437 N SER A1358 38.375 -99.347 155.409 1.00 31.76 N ANISOU 3437 N SER A1358 4444 3161 4464 -295 273 -607 N ATOM 3438 CA SER A1358 38.577 -98.160 156.226 1.00 35.39 C ANISOU 3438 CA SER A1358 5004 3550 4892 -327 222 -658 C ATOM 3439 C SER A1358 39.866 -98.280 157.028 1.00 38.00 C ANISOU 3439 C SER A1358 5347 3960 5131 -396 174 -647 C ATOM 3440 O SER A1358 40.237 -99.367 157.476 1.00 41.76 O ANISOU 3440 O SER A1358 5776 4534 5557 -365 213 -624 O ATOM 3441 CB SER A1358 37.396 -97.957 157.176 1.00 35.75 C ANISOU 3441 CB SER A1358 5114 3537 4933 -231 286 -736 C ATOM 3442 OG SER A1358 36.158 -97.989 156.491 1.00 38.62 O ANISOU 3442 OG SER A1358 5433 3874 5368 -158 337 -736 O ATOM 3443 N ALA A1359 40.545 -97.148 157.219 1.00 36.60 N ANISOU 3443 N ALA A1359 5243 3741 4923 -496 82 -657 N ATOM 3444 CA ALA A1359 41.797 -97.117 157.974 1.00 40.85 C ANISOU 3444 CA ALA A1359 5784 4375 5363 -590 18 -641 C ATOM 3445 C ALA A1359 41.487 -97.049 159.470 1.00 41.86 C ANISOU 3445 C ALA A1359 6014 4469 5421 -546 41 -724 C ATOM 3446 O ALA A1359 41.712 -96.047 160.151 1.00 47.75 O ANISOU 3446 O ALA A1359 6885 5141 6116 -615 -28 -779 O ATOM 3447 CB ALA A1359 42.666 -95.949 157.530 1.00 44.82 C ANISOU 3447 CB ALA A1359 6326 4856 5849 -754 -101 -607 C ATOM 3448 N VAL A1360 40.948 -98.151 159.981 1.00 37.42 N ANISOU 3448 N VAL A1360 5411 3959 4848 -435 136 -732 N ATOM 3449 CA VAL A1360 40.593 -98.250 161.389 1.00 42.57 C ANISOU 3449 CA VAL A1360 6143 4607 5424 -382 175 -800 C ATOM 3450 C VAL A1360 41.034 -99.604 161.924 1.00 46.35 C ANISOU 3450 C VAL A1360 6550 5219 5841 -342 221 -750 C ATOM 3451 O VAL A1360 40.988-100.619 161.221 1.00 45.53 O ANISOU 3451 O VAL A1360 6361 5163 5776 -298 266 -688 O ATOM 3452 CB VAL A1360 39.081 -98.056 161.633 1.00 42.56 C ANISOU 3452 CB VAL A1360 6195 4512 5465 -268 261 -869 C ATOM 3453 CG1 VAL A1360 38.640 -96.663 161.217 1.00 41.40 C ANISOU 3453 CG1 VAL A1360 6148 4221 5363 -272 211 -923 C ATOM 3454 CG2 VAL A1360 38.268 -99.122 160.906 1.00 40.40 C ANISOU 3454 CG2 VAL A1360 5813 4274 5263 -200 350 -819 C ATOM 3455 N GLY A1361 41.475 -99.605 163.177 1.00 50.37 N ANISOU 3455 N GLY A1361 7115 5781 6244 -353 203 -779 N ATOM 3456 CA GLY A1361 41.652-100.844 163.918 1.00 46.75 C ANISOU 3456 CA GLY A1361 6623 5424 5715 -290 257 -740 C ATOM 3457 C GLY A1361 42.600-101.815 163.264 1.00 51.75 C ANISOU 3457 C GLY A1361 7152 6171 6341 -280 240 -642 C ATOM 3458 O GLY A1361 43.719-101.458 162.898 1.00 53.21 O ANISOU 3458 O GLY A1361 7278 6442 6496 -353 156 -601 O ATOM 3459 N GLY A1362 42.140-103.058 163.087 1.00 53.13 N ANISOU 3459 N GLY A1362 7306 6349 6533 -190 319 -600 N ATOM 3460 CA GLY A1362 43.009-104.087 162.547 1.00 53.70 C ANISOU 3460 CA GLY A1362 7311 6516 6579 -140 310 -515 C ATOM 3461 C GLY A1362 43.247-103.968 161.055 1.00 55.28 C ANISOU 3461 C GLY A1362 7434 6714 6857 -155 287 -481 C ATOM 3462 O GLY A1362 44.325-104.324 160.566 1.00 60.27 O ANISOU 3462 O GLY A1362 7988 7466 7444 -133 248 -417 O ATOM 3463 N LEU A1363 42.253-103.475 160.311 1.00 46.85 N ANISOU 3463 N LEU A1363 6377 5530 5892 -181 313 -518 N ATOM 3464 CA LEU A1363 42.437-103.245 158.882 1.00 45.74 C ANISOU 3464 CA LEU A1363 6169 5389 5820 -204 288 -487 C ATOM 3465 C LEU A1363 43.605-102.307 158.623 1.00 43.19 C ANISOU 3465 C LEU A1363 5786 5161 5464 -299 193 -459 C ATOM 3466 O LEU A1363 44.321-102.463 157.628 1.00 42.68 O ANISOU 3466 O LEU A1363 5632 5187 5398 -302 166 -399 O ATOM 3467 CB LEU A1363 41.154-102.673 158.281 1.00 35.48 C ANISOU 3467 CB LEU A1363 4895 3959 4628 -223 319 -532 C ATOM 3468 CG LEU A1363 39.847-103.416 158.576 1.00 37.74 C ANISOU 3468 CG LEU A1363 5222 4173 4943 -166 408 -556 C ATOM 3469 CD1 LEU A1363 38.660-102.603 158.094 1.00 28.81 C ANISOU 3469 CD1 LEU A1363 4092 2954 3900 -180 427 -599 C ATOM 3470 CD2 LEU A1363 39.847-104.792 157.936 1.00 28.57 C ANISOU 3470 CD2 LEU A1363 4051 3025 3780 -115 444 -504 C ATOM 3471 N ARG A1364 43.819-101.340 159.516 1.00 47.03 N ANISOU 3471 N ARG A1364 6324 5636 5910 -383 139 -500 N ATOM 3472 CA ARG A1364 44.918-100.394 159.357 1.00 47.98 C ANISOU 3472 CA ARG A1364 6402 5843 5986 -516 35 -469 C ATOM 3473 C ARG A1364 46.269-101.084 159.509 1.00 49.53 C ANISOU 3473 C ARG A1364 6483 6261 6075 -502 1 -387 C ATOM 3474 O ARG A1364 47.224-100.754 158.796 1.00 55.05 O ANISOU 3474 O ARG A1364 7075 7096 6745 -580 -61 -318 O ATOM 3475 CB ARG A1364 44.764 -99.270 160.379 1.00 55.05 C ANISOU 3475 CB ARG A1364 7418 6651 6848 -611 -20 -544 C ATOM 3476 CG ARG A1364 45.545 -98.015 160.078 1.00 67.53 C ANISOU 3476 CG ARG A1364 9010 8242 8407 -791 -139 -526 C ATOM 3477 CD ARG A1364 45.075 -96.888 160.979 1.00 81.92 C ANISOU 3477 CD ARG A1364 11013 9905 10210 -858 -184 -625 C ATOM 3478 NE ARG A1364 46.006 -95.767 160.970 1.00 95.88 N ANISOU 3478 NE ARG A1364 12822 11687 11919 -1064 -319 -605 N ATOM 3479 CZ ARG A1364 47.080 -95.694 161.748 1.00107.02 C ANISOU 3479 CZ ARG A1364 14208 13246 13210 -1179 -400 -580 C ATOM 3480 NH1 ARG A1364 47.352 -96.679 162.593 1.00110.78 N ANISOU 3480 NH1 ARG A1364 14618 13863 13612 -1082 -356 -573 N ATOM 3481 NH2 ARG A1364 47.880 -94.640 161.680 1.00112.23 N ANISOU 3481 NH2 ARG A1364 14912 13916 13814 -1400 -532 -555 N ATOM 3482 N ASP A1365 46.365-102.048 160.427 1.00 47.92 N ANISOU 3482 N ASP A1365 6294 6113 5802 -397 42 -384 N ATOM 3483 CA ASP A1365 47.623-102.751 160.650 1.00 52.72 C ANISOU 3483 CA ASP A1365 6794 6941 6294 -346 12 -304 C ATOM 3484 C ASP A1365 47.855-103.852 159.626 1.00 54.80 C ANISOU 3484 C ASP A1365 6982 7273 6567 -201 64 -240 C ATOM 3485 O ASP A1365 49.008-104.154 159.297 1.00 59.64 O ANISOU 3485 O ASP A1365 7468 8098 7096 -162 29 -161 O ATOM 3486 CB ASP A1365 47.649-103.344 162.058 1.00 61.55 C ANISOU 3486 CB ASP A1365 7976 8087 7324 -278 30 -320 C ATOM 3487 CG ASP A1365 47.241-102.344 163.119 1.00 69.71 C ANISOU 3487 CG ASP A1365 9116 9030 8341 -394 -7 -402 C ATOM 3488 OD1 ASP A1365 47.593-101.153 162.983 1.00 74.30 O ANISOU 3488 OD1 ASP A1365 9697 9613 8922 -552 -91 -421 O ATOM 3489 OD2 ASP A1365 46.565-102.749 164.087 1.00 71.62 O ANISOU 3489 OD2 ASP A1365 9454 9199 8561 -329 48 -448 O ATOM 3490 N ILE A1366 46.785-104.468 159.123 1.00 50.23 N ANISOU 3490 N ILE A1366 6480 6529 6075 -116 144 -273 N ATOM 3491 CA ILE A1366 46.936-105.534 158.138 1.00 48.13 C ANISOU 3491 CA ILE A1366 6183 6296 5808 22 189 -228 C ATOM 3492 C ILE A1366 47.305-104.956 156.779 1.00 46.73 C ANISOU 3492 C ILE A1366 5901 6186 5669 -34 159 -196 C ATOM 3493 O ILE A1366 48.265-105.397 156.137 1.00 43.87 O ANISOU 3493 O ILE A1366 5434 6000 5236 45 148 -129 O ATOM 3494 CB ILE A1366 45.647-106.368 158.054 1.00 41.47 C ANISOU 3494 CB ILE A1366 5468 5253 5035 93 271 -272 C ATOM 3495 CG1 ILE A1366 45.381-107.088 159.375 1.00 39.19 C ANISOU 3495 CG1 ILE A1366 5278 4923 4688 152 304 -281 C ATOM 3496 CG2 ILE A1366 45.729-107.356 156.900 1.00 32.83 C ANISOU 3496 CG2 ILE A1366 4375 4158 3942 214 305 -240 C ATOM 3497 CD1 ILE A1366 44.023-107.751 159.438 1.00 30.52 C ANISOU 3497 CD1 ILE A1366 4303 3642 3653 168 378 -316 C ATOM 3498 N ILE A1367 46.560-103.950 156.329 1.00 45.08 N ANISOU 3498 N ILE A1367 5718 5850 5560 -161 145 -238 N ATOM 3499 CA ILE A1367 46.615-103.484 154.949 1.00 40.01 C ANISOU 3499 CA ILE A1367 5006 5226 4968 -210 129 -209 C ATOM 3500 C ILE A1367 47.660-102.385 154.817 1.00 46.49 C ANISOU 3500 C ILE A1367 5722 6202 5741 -362 38 -154 C ATOM 3501 O ILE A1367 47.705-101.451 155.628 1.00 53.60 O ANISOU 3501 O ILE A1367 6666 7064 6636 -495 -19 -180 O ATOM 3502 CB ILE A1367 45.235-102.985 154.493 1.00 33.45 C ANISOU 3502 CB ILE A1367 4262 4181 4264 -258 156 -271 C ATOM 3503 CG1 ILE A1367 44.203-104.107 154.618 1.00 29.08 C ANISOU 3503 CG1 ILE A1367 3800 3504 3747 -142 239 -312 C ATOM 3504 CG2 ILE A1367 45.295-102.461 153.067 1.00 35.11 C ANISOU 3504 CG2 ILE A1367 4406 4414 4521 -312 133 -234 C ATOM 3505 CD1 ILE A1367 42.784-103.659 154.370 1.00 28.43 C ANISOU 3505 CD1 ILE A1367 3781 3248 3773 -184 268 -368 C ATOM 3506 N THR A1368 48.496-102.495 153.792 1.00 41.29 N ANISOU 3506 N THR A1368 4930 5722 5035 -350 24 -76 N ATOM 3507 CA THR A1368 49.424-101.453 153.384 1.00 49.71 C ANISOU 3507 CA THR A1368 5880 6950 6057 -523 -61 -3 C ATOM 3508 C THR A1368 49.132-101.071 151.935 1.00 50.29 C ANISOU 3508 C THR A1368 5921 6995 6193 -564 -55 26 C ATOM 3509 O THR A1368 48.244-101.632 151.290 1.00 50.49 O ANISOU 3509 O THR A1368 6008 6885 6290 -453 11 -16 O ATOM 3510 CB THR A1368 50.876-101.909 153.556 1.00 60.48 C ANISOU 3510 CB THR A1368 7072 8634 7271 -479 -87 90 C ATOM 3511 OG1 THR A1368 51.124-103.050 152.725 1.00 64.25 O ANISOU 3511 OG1 THR A1368 7482 9224 7707 -267 -17 121 O ATOM 3512 CG2 THR A1368 51.142-102.276 155.007 1.00 62.30 C ANISOU 3512 CG2 THR A1368 7341 8896 7436 -438 -100 66 C ATOM 3513 N ASN A1369 49.895-100.102 151.420 1.00 49.38 N ANISOU 3513 N ASN A1369 5707 7014 6039 -740 -130 106 N ATOM 3514 CA ASN A1369 49.657 -99.624 150.061 1.00 43.46 C ANISOU 3514 CA ASN A1369 4928 6245 5339 -800 -133 146 C ATOM 3515 C ASN A1369 49.892-100.718 149.030 1.00 37.23 C ANISOU 3515 C ASN A1369 4040 5601 4505 -612 -59 179 C ATOM 3516 O ASN A1369 49.253-100.718 147.972 1.00 39.92 O ANISOU 3516 O ASN A1369 4409 5853 4908 -586 -29 171 O ATOM 3517 CB ASN A1369 50.543 -98.413 149.759 1.00 41.72 C ANISOU 3517 CB ASN A1369 4623 6165 5066 -1046 -235 245 C ATOM 3518 CG ASN A1369 50.302 -97.847 148.369 1.00 47.79 C ANISOU 3518 CG ASN A1369 5370 6909 5877 -1123 -244 300 C ATOM 3519 OD1 ASN A1369 49.264 -97.238 148.108 1.00 46.27 O ANISOU 3519 OD1 ASN A1369 5323 6461 5798 -1164 -251 249 O ATOM 3520 ND2 ASN A1369 51.262 -98.043 147.471 1.00 41.98 N ANISOU 3520 ND2 ASN A1369 4448 6459 5042 -1131 -242 409 N ATOM 3521 N GLU A1370 50.788-101.657 149.318 1.00 38.74 N ANISOU 3521 N GLU A1370 4127 6013 4580 -467 -31 214 N ATOM 3522 CA GLU A1370 51.091-102.743 148.397 1.00 38.03 C ANISOU 3522 CA GLU A1370 3966 6062 4422 -255 39 236 C ATOM 3523 C GLU A1370 50.151-103.933 148.542 1.00 39.43 C ANISOU 3523 C GLU A1370 4303 6028 4650 -49 117 139 C ATOM 3524 O GLU A1370 50.257-104.880 147.757 1.00 48.68 O ANISOU 3524 O GLU A1370 5469 7258 5768 134 173 138 O ATOM 3525 CB GLU A1370 52.538-103.211 148.585 1.00 42.53 C ANISOU 3525 CB GLU A1370 4348 6987 4823 -163 33 326 C ATOM 3526 CG GLU A1370 53.586-102.258 148.022 1.00 65.69 C ANISOU 3526 CG GLU A1370 7076 10210 7672 -350 -31 452 C ATOM 3527 CD GLU A1370 53.703-100.973 148.820 1.00 83.86 C ANISOU 3527 CD GLU A1370 9393 12463 10006 -645 -134 474 C ATOM 3528 OE1 GLU A1370 53.514-101.018 150.055 1.00 86.52 O ANISOU 3528 OE1 GLU A1370 9823 12688 10363 -654 -155 416 O ATOM 3529 OE2 GLU A1370 53.977 -99.916 148.212 1.00 87.61 O ANISOU 3529 OE2 GLU A1370 9804 13004 10481 -872 -197 550 O ATOM 3530 N THR A1371 49.237-103.916 149.519 1.00 36.30 N ANISOU 3530 N THR A1371 4055 5394 4342 -79 122 59 N ATOM 3531 CA THR A1371 48.335-105.042 149.739 1.00 37.47 C ANISOU 3531 CA THR A1371 4355 5352 4529 78 189 -19 C ATOM 3532 C THR A1371 46.876-104.607 149.848 1.00 41.25 C ANISOU 3532 C THR A1371 4967 5556 5150 -18 198 -95 C ATOM 3533 O THR A1371 46.043-105.379 150.331 1.00 45.11 O ANISOU 3533 O THR A1371 5581 5886 5674 57 244 -154 O ATOM 3534 CB THR A1371 48.738-105.835 150.989 1.00 35.39 C ANISOU 3534 CB THR A1371 4131 5121 4193 193 203 -26 C ATOM 3535 OG1 THR A1371 48.698-104.984 152.142 1.00 37.70 O ANISOU 3535 OG1 THR A1371 4434 5380 4512 44 155 -38 O ATOM 3536 CG2 THR A1371 50.140-106.410 150.834 1.00 33.07 C ANISOU 3536 CG2 THR A1371 3701 5119 3746 339 201 52 C ATOM 3537 N GLY A1372 46.546-103.400 149.411 1.00 40.16 N ANISOU 3537 N GLY A1372 4807 5369 5085 -179 155 -86 N ATOM 3538 CA GLY A1372 45.168-102.955 149.435 1.00 29.60 C ANISOU 3538 CA GLY A1372 3577 3800 3870 -240 165 -151 C ATOM 3539 C GLY A1372 45.082-101.443 149.360 1.00 31.60 C ANISOU 3539 C GLY A1372 3822 4008 4177 -413 98 -135 C ATOM 3540 O GLY A1372 46.078-100.751 149.146 1.00 37.46 O ANISOU 3540 O GLY A1372 4477 4892 4865 -516 39 -66 O ATOM 3541 N ILE A1373 43.857-100.951 149.536 1.00 32.28 N ANISOU 3541 N ILE A1373 4007 3896 4363 -443 106 -195 N ATOM 3542 CA ILE A1373 43.552 -99.525 149.525 1.00 36.42 C ANISOU 3542 CA ILE A1373 4576 4319 4944 -574 44 -195 C ATOM 3543 C ILE A1373 42.853 -99.178 150.832 1.00 39.09 C ANISOU 3543 C ILE A1373 5025 4513 5313 -571 52 -274 C ATOM 3544 O ILE A1373 41.902 -99.859 151.230 1.00 36.91 O ANISOU 3544 O ILE A1373 4795 4158 5072 -474 118 -331 O ATOM 3545 CB ILE A1373 42.667 -99.138 148.327 1.00 42.83 C ANISOU 3545 CB ILE A1373 5398 5039 5835 -579 46 -187 C ATOM 3546 CG1 ILE A1373 43.253 -99.671 147.019 1.00 42.19 C ANISOU 3546 CG1 ILE A1373 5214 5108 5711 -556 54 -120 C ATOM 3547 CG2 ILE A1373 42.497 -97.628 148.257 1.00 46.30 C ANISOU 3547 CG2 ILE A1373 5903 5369 6318 -703 -29 -173 C ATOM 3548 CD1 ILE A1373 42.390 -99.380 145.809 1.00 38.26 C ANISOU 3548 CD1 ILE A1373 4723 4537 5279 -558 54 -109 C ATOM 3549 N LEU A1374 43.315 -98.117 151.489 1.00 39.80 N ANISOU 3549 N LEU A1374 5167 4576 5380 -685 -19 -276 N ATOM 3550 CA LEU A1374 42.712 -97.634 152.723 1.00 42.82 C ANISOU 3550 CA LEU A1374 5672 4824 5774 -680 -20 -358 C ATOM 3551 C LEU A1374 42.035 -96.291 152.486 1.00 45.36 C ANISOU 3551 C LEU A1374 6106 4970 6157 -737 -70 -384 C ATOM 3552 O LEU A1374 42.531 -95.460 151.719 1.00 50.96 O ANISOU 3552 O LEU A1374 6817 5676 6869 -854 -144 -323 O ATOM 3553 CB LEU A1374 43.753 -97.507 153.839 1.00 46.20 C ANISOU 3553 CB LEU A1374 6108 5341 6106 -753 -68 -357 C ATOM 3554 CG LEU A1374 44.226 -98.817 154.471 1.00 48.18 C ANISOU 3554 CG LEU A1374 6288 5732 6287 -655 -14 -350 C ATOM 3555 CD1 LEU A1374 44.967 -98.550 155.770 1.00 54.28 C ANISOU 3555 CD1 LEU A1374 7093 6564 6968 -719 -64 -366 C ATOM 3556 CD2 LEU A1374 43.054 -99.756 154.708 1.00 48.90 C ANISOU 3556 CD2 LEU A1374 6419 5733 6427 -509 86 -406 C ATOM 3557 N VAL A1375 40.899 -96.085 153.150 1.00 41.35 N ANISOU 3557 N VAL A1375 5698 4323 5691 -647 -28 -468 N ATOM 3558 CA VAL A1375 40.115 -94.866 153.004 1.00 41.84 C ANISOU 3558 CA VAL A1375 5886 4208 5804 -645 -65 -504 C ATOM 3559 C VAL A1375 39.658 -94.401 154.379 1.00 41.78 C ANISOU 3559 C VAL A1375 6015 4096 5763 -593 -57 -603 C ATOM 3560 O VAL A1375 39.533 -95.195 155.315 1.00 44.86 O ANISOU 3560 O VAL A1375 6380 4550 6114 -527 6 -645 O ATOM 3561 CB VAL A1375 38.898 -95.070 152.073 1.00 43.57 C ANISOU 3561 CB VAL A1375 6062 4384 6109 -534 -8 -501 C ATOM 3562 CG1 VAL A1375 39.350 -95.230 150.636 1.00 45.49 C ANISOU 3562 CG1 VAL A1375 6205 4703 6375 -597 -35 -408 C ATOM 3563 CG2 VAL A1375 38.097 -96.281 152.516 1.00 41.12 C ANISOU 3563 CG2 VAL A1375 5682 4134 5807 -413 98 -540 C ATOM 3564 N LYS A1376 39.411 -93.098 154.494 1.00 42.69 N ANISOU 3564 N LYS A1376 6294 4044 5884 -618 -124 -639 N ATOM 3565 CA LYS A1376 38.857 -92.548 155.723 1.00 43.74 C ANISOU 3565 CA LYS A1376 6583 4060 5976 -538 -115 -747 C ATOM 3566 C LYS A1376 37.480 -93.143 155.990 1.00 45.55 C ANISOU 3566 C LYS A1376 6761 4305 6242 -339 5 -800 C ATOM 3567 O LYS A1376 36.669 -93.306 155.076 1.00 50.59 O ANISOU 3567 O LYS A1376 7321 4946 6953 -262 45 -768 O ATOM 3568 CB LYS A1376 38.760 -91.025 155.624 1.00 55.24 C ANISOU 3568 CB LYS A1376 8254 5304 7430 -576 -213 -776 C ATOM 3569 CG LYS A1376 38.289 -90.341 156.895 1.00 67.68 C ANISOU 3569 CG LYS A1376 10030 6743 8942 -485 -215 -899 C ATOM 3570 CD LYS A1376 37.709 -88.966 156.601 1.00 80.60 C ANISOU 3570 CD LYS A1376 11890 8141 10595 -427 -281 -937 C ATOM 3571 CE LYS A1376 38.686 -88.102 155.817 1.00 89.27 C ANISOU 3571 CE LYS A1376 13086 9141 11693 -649 -421 -855 C ATOM 3572 NZ LYS A1376 38.086 -86.787 155.452 1.00 96.12 N ANISOU 3572 NZ LYS A1376 14195 9749 12577 -582 -490 -881 N ATOM 3573 N ALA A1377 37.220 -93.474 157.252 1.00 52.84 N ANISOU 3573 N ALA A1377 7717 5256 7103 -268 61 -874 N ATOM 3574 CA ALA A1377 35.951 -94.088 157.614 1.00 49.48 C ANISOU 3574 CA ALA A1377 7226 4883 6692 -102 178 -912 C ATOM 3575 C ALA A1377 34.819 -93.068 157.565 1.00 52.34 C ANISOU 3575 C ALA A1377 7690 5121 7075 47 189 -971 C ATOM 3576 O ALA A1377 35.004 -91.892 157.891 1.00 58.68 O ANISOU 3576 O ALA A1377 8684 5770 7843 52 116 -1027 O ATOM 3577 CB ALA A1377 36.042 -94.707 159.008 1.00 43.61 C ANISOU 3577 CB ALA A1377 6492 4218 5861 -75 234 -964 C ATOM 3578 N GLY A1378 33.640 -93.529 157.150 1.00 51.90 N ANISOU 3578 N GLY A1378 7514 5139 7068 171 275 -956 N ATOM 3579 CA GLY A1378 32.454 -92.698 157.124 1.00 55.87 C ANISOU 3579 CA GLY A1378 8073 5575 7579 352 302 -1003 C ATOM 3580 C GLY A1378 32.392 -91.673 156.014 1.00 60.91 C ANISOU 3580 C GLY A1378 8790 6075 8278 363 219 -971 C ATOM 3581 O GLY A1378 31.545 -90.774 156.072 1.00 65.62 O ANISOU 3581 O GLY A1378 9485 6581 8867 534 222 -1017 O ATOM 3582 N ASP A1379 33.252 -91.775 155.002 1.00 55.94 N ANISOU 3582 N ASP A1379 8124 5433 7700 200 147 -887 N ATOM 3583 CA ASP A1379 33.291 -90.803 153.913 1.00 55.52 C ANISOU 3583 CA ASP A1379 8151 5247 7696 183 60 -839 C ATOM 3584 C ASP A1379 32.877 -91.478 152.612 1.00 52.33 C ANISOU 3584 C ASP A1379 7556 4960 7369 174 87 -748 C ATOM 3585 O ASP A1379 33.677 -92.216 152.015 1.00 48.62 O ANISOU 3585 O ASP A1379 6980 4578 6915 26 73 -682 O ATOM 3586 CB ASP A1379 34.694 -90.200 153.786 1.00 61.50 C ANISOU 3586 CB ASP A1379 9037 5900 8429 -22 -60 -808 C ATOM 3587 CG ASP A1379 34.710 -88.916 152.976 1.00 77.52 C ANISOU 3587 CG ASP A1379 11231 7740 10484 -39 -163 -773 C ATOM 3588 OD1 ASP A1379 33.971 -88.822 151.974 1.00 82.83 O ANISOU 3588 OD1 ASP A1379 11837 8417 11218 49 -150 -721 O ATOM 3589 OD2 ASP A1379 35.467 -87.994 153.347 1.00 84.45 O ANISOU 3589 OD2 ASP A1379 12315 8460 11312 -150 -264 -792 O ATOM 3590 N PRO A1380 31.650 -91.262 152.128 1.00 50.84 N ANISOU 3590 N PRO A1380 7315 4786 7215 335 125 -742 N ATOM 3591 CA PRO A1380 31.244 -91.904 150.867 1.00 44.43 C ANISOU 3591 CA PRO A1380 6326 4091 6465 311 140 -657 C ATOM 3592 C PRO A1380 32.036 -91.417 149.668 1.00 45.25 C ANISOU 3592 C PRO A1380 6470 4120 6604 182 42 -574 C ATOM 3593 O PRO A1380 32.221 -92.181 148.713 1.00 41.41 O ANISOU 3593 O PRO A1380 5842 3743 6146 96 47 -506 O ATOM 3594 CB PRO A1380 29.756 -91.540 150.744 1.00 39.43 C ANISOU 3594 CB PRO A1380 5646 3492 5844 523 187 -671 C ATOM 3595 CG PRO A1380 29.342 -91.083 152.115 1.00 45.10 C ANISOU 3595 CG PRO A1380 6473 4167 6498 670 233 -771 C ATOM 3596 CD PRO A1380 30.562 -90.469 152.722 1.00 49.75 C ANISOU 3596 CD PRO A1380 7269 4585 7049 559 157 -813 C ATOM 3597 N GLY A1381 32.510 -90.169 149.690 1.00 42.75 N ANISOU 3597 N GLY A1381 6353 3616 6274 159 -49 -577 N ATOM 3598 CA GLY A1381 33.270 -89.657 148.563 1.00 38.55 C ANISOU 3598 CA GLY A1381 5861 3022 5764 17 -145 -483 C ATOM 3599 C GLY A1381 34.634 -90.307 148.428 1.00 45.53 C ANISOU 3599 C GLY A1381 6674 4002 6624 -199 -168 -436 C ATOM 3600 O GLY A1381 35.067 -90.635 147.319 1.00 50.27 O ANISOU 3600 O GLY A1381 7171 4688 7242 -297 -190 -347 O ATOM 3601 N GLU A1382 35.334 -90.497 149.550 1.00 48.35 N ANISOU 3601 N GLU A1382 7079 4362 6928 -264 -164 -492 N ATOM 3602 CA GLU A1382 36.638 -91.152 149.500 1.00 49.86 C ANISOU 3602 CA GLU A1382 7183 4678 7083 -442 -182 -444 C ATOM 3603 C GLU A1382 36.511 -92.598 149.040 1.00 45.10 C ANISOU 3603 C GLU A1382 6370 4268 6497 -416 -96 -419 C ATOM 3604 O GLU A1382 37.391 -93.111 148.339 1.00 54.03 O ANISOU 3604 O GLU A1382 7403 5515 7611 -524 -113 -348 O ATOM 3605 CB GLU A1382 37.323 -91.086 150.864 1.00 57.69 C ANISOU 3605 CB GLU A1382 8264 5648 8005 -499 -196 -511 C ATOM 3606 CG GLU A1382 38.090 -89.802 151.116 1.00 73.21 C ANISOU 3606 CG GLU A1382 10433 7456 9927 -639 -318 -504 C ATOM 3607 CD GLU A1382 39.278 -90.014 152.033 1.00 87.26 C ANISOU 3607 CD GLU A1382 12219 9311 11625 -790 -354 -517 C ATOM 3608 OE1 GLU A1382 39.733 -91.171 152.158 1.00 86.36 O ANISOU 3608 OE1 GLU A1382 11928 9393 11493 -801 -294 -497 O ATOM 3609 OE2 GLU A1382 39.757 -89.026 152.630 1.00 95.63 O ANISOU 3609 OE2 GLU A1382 13471 10232 12630 -896 -448 -545 O ATOM 3610 N LEU A1383 35.428 -93.273 149.428 1.00 39.99 N ANISOU 3610 N LEU A1383 5660 3664 5872 -274 -7 -474 N ATOM 3611 CA LEU A1383 35.215 -94.639 148.966 1.00 43.87 C ANISOU 3611 CA LEU A1383 5988 4307 6374 -263 64 -451 C ATOM 3612 C LEU A1383 34.886 -94.667 147.479 1.00 49.57 C ANISOU 3612 C LEU A1383 6633 5065 7139 -270 44 -380 C ATOM 3613 O LEU A1383 35.341 -95.558 146.752 1.00 54.63 O ANISOU 3613 O LEU A1383 7175 5815 7767 -325 56 -337 O ATOM 3614 CB LEU A1383 34.105 -95.302 149.780 1.00 32.78 C ANISOU 3614 CB LEU A1383 4541 2941 4971 -144 156 -515 C ATOM 3615 CG LEU A1383 33.795 -96.759 149.434 1.00 37.26 C ANISOU 3615 CG LEU A1383 4977 3639 5540 -150 222 -496 C ATOM 3616 CD1 LEU A1383 35.038 -97.619 149.590 1.00 36.29 C ANISOU 3616 CD1 LEU A1383 4838 3582 5369 -237 220 -478 C ATOM 3617 CD2 LEU A1383 32.660 -97.284 150.298 1.00 33.87 C ANISOU 3617 CD2 LEU A1383 4512 3254 5104 -62 305 -545 C ATOM 3618 N ALA A1384 34.104 -93.692 147.007 1.00 44.99 N ANISOU 3618 N ALA A1384 6106 4392 6597 -202 10 -368 N ATOM 3619 CA ALA A1384 33.777 -93.629 145.587 1.00 45.75 C ANISOU 3619 CA ALA A1384 6134 4524 6726 -209 -18 -294 C ATOM 3620 C ALA A1384 35.023 -93.387 144.745 1.00 46.27 C ANISOU 3620 C ALA A1384 6205 4608 6767 -357 -86 -213 C ATOM 3621 O ALA A1384 35.176 -93.974 143.666 1.00 43.44 O ANISOU 3621 O ALA A1384 5744 4356 6404 -395 -83 -157 O ATOM 3622 CB ALA A1384 32.737 -92.538 145.335 1.00 40.42 C ANISOU 3622 CB ALA A1384 5528 3741 6087 -88 -48 -290 C ATOM 3623 N ASN A1385 35.929 -92.530 145.223 1.00 44.76 N ANISOU 3623 N ASN A1385 6132 4328 6548 -450 -151 -203 N ATOM 3624 CA ASN A1385 37.160 -92.277 144.482 1.00 46.07 C ANISOU 3624 CA ASN A1385 6284 4546 6675 -613 -216 -111 C ATOM 3625 C ASN A1385 38.081 -93.491 144.506 1.00 45.22 C ANISOU 3625 C ASN A1385 6041 4626 6515 -668 -170 -102 C ATOM 3626 O ASN A1385 38.759 -93.781 143.513 1.00 46.95 O ANISOU 3626 O ASN A1385 6169 4968 6700 -740 -184 -25 O ATOM 3627 CB ASN A1385 37.872 -91.047 145.045 1.00 48.15 C ANISOU 3627 CB ASN A1385 6715 4671 6910 -728 -307 -98 C ATOM 3628 CG ASN A1385 37.207 -89.749 144.628 1.00 55.63 C ANISOU 3628 CG ASN A1385 7823 5422 7892 -692 -377 -73 C ATOM 3629 OD1 ASN A1385 36.609 -89.661 143.555 1.00 58.77 O ANISOU 3629 OD1 ASN A1385 8175 5831 8323 -639 -380 -17 O ATOM 3630 ND2 ASN A1385 37.312 -88.731 145.473 1.00 64.93 N ANISOU 3630 ND2 ASN A1385 9204 6413 9052 -715 -439 -114 N ATOM 3631 N ALA A1386 38.120 -94.213 145.629 1.00 39.72 N ANISOU 3631 N ALA A1386 5334 3957 5801 -620 -114 -178 N ATOM 3632 CA ALA A1386 38.930 -95.425 145.695 1.00 34.95 C ANISOU 3632 CA ALA A1386 4620 3519 5142 -636 -69 -171 C ATOM 3633 C ALA A1386 38.419 -96.479 144.721 1.00 34.65 C ANISOU 3633 C ALA A1386 4482 3570 5115 -565 -15 -161 C ATOM 3634 O ALA A1386 39.210 -97.213 144.116 1.00 43.67 O ANISOU 3634 O ALA A1386 5543 4849 6202 -585 -3 -121 O ATOM 3635 CB ALA A1386 38.946 -95.972 147.122 1.00 29.10 C ANISOU 3635 CB ALA A1386 3907 2771 4378 -588 -23 -250 C ATOM 3636 N ILE A1387 37.098 -96.569 144.558 1.00 33.46 N ANISOU 3636 N ILE A1387 4337 3353 5022 -479 16 -197 N ATOM 3637 CA ILE A1387 36.527 -97.506 143.596 1.00 34.99 C ANISOU 3637 CA ILE A1387 4452 3622 5220 -437 52 -189 C ATOM 3638 C ILE A1387 36.889 -97.098 142.172 1.00 37.18 C ANISOU 3638 C ILE A1387 4690 3952 5484 -490 2 -107 C ATOM 3639 O ILE A1387 37.151 -97.951 141.315 1.00 39.10 O ANISOU 3639 O ILE A1387 4869 4301 5684 -488 20 -87 O ATOM 3640 CB ILE A1387 35.004 -97.606 143.799 1.00 33.87 C ANISOU 3640 CB ILE A1387 4308 3426 5134 -354 88 -235 C ATOM 3641 CG1 ILE A1387 34.694 -98.233 145.162 1.00 29.51 C ANISOU 3641 CG1 ILE A1387 3777 2860 4575 -311 150 -306 C ATOM 3642 CG2 ILE A1387 34.357 -98.407 142.676 1.00 29.25 C ANISOU 3642 CG2 ILE A1387 3649 2915 4548 -344 101 -217 C ATOM 3643 CD1 ILE A1387 33.228 -98.215 145.530 1.00 27.88 C ANISOU 3643 CD1 ILE A1387 3551 2635 4408 -235 189 -342 C ATOM 3644 N LEU A1388 36.921 -95.791 141.898 1.00 37.14 N ANISOU 3644 N LEU A1388 4739 3868 5504 -537 -64 -57 N ATOM 3645 CA LEU A1388 37.346 -95.324 140.581 1.00 38.55 C ANISOU 3645 CA LEU A1388 4887 4101 5660 -606 -116 37 C ATOM 3646 C LEU A1388 38.813 -95.648 140.328 1.00 43.96 C ANISOU 3646 C LEU A1388 5510 4932 6259 -696 -123 91 C ATOM 3647 O LEU A1388 39.186 -96.036 139.214 1.00 41.28 O ANISOU 3647 O LEU A1388 5095 4721 5870 -711 -121 145 O ATOM 3648 CB LEU A1388 37.101 -93.822 140.450 1.00 39.34 C ANISOU 3648 CB LEU A1388 5090 4060 5797 -644 -193 87 C ATOM 3649 CG LEU A1388 35.651 -93.370 140.292 1.00 41.88 C ANISOU 3649 CG LEU A1388 5450 4274 6186 -528 -195 64 C ATOM 3650 CD1 LEU A1388 35.540 -91.866 140.484 1.00 40.19 C ANISOU 3650 CD1 LEU A1388 5388 3882 5998 -539 -272 96 C ATOM 3651 CD2 LEU A1388 35.113 -93.778 138.929 1.00 41.32 C ANISOU 3651 CD2 LEU A1388 5287 4301 6113 -504 -195 112 C ATOM 3652 N LYS A1389 39.662 -95.491 141.347 1.00 42.59 N ANISOU 3652 N LYS A1389 5363 4763 6057 -750 -131 79 N ATOM 3653 CA LYS A1389 41.068 -95.849 141.195 1.00 45.19 C ANISOU 3653 CA LYS A1389 5606 5273 6292 -822 -134 135 C ATOM 3654 C LYS A1389 41.248 -97.352 141.042 1.00 42.66 C ANISOU 3654 C LYS A1389 5202 5086 5920 -710 -57 94 C ATOM 3655 O LYS A1389 42.195 -97.799 140.384 1.00 41.25 O ANISOU 3655 O LYS A1389 4931 5090 5652 -717 -48 149 O ATOM 3656 CB LYS A1389 41.875 -95.336 142.388 1.00 47.26 C ANISOU 3656 CB LYS A1389 5911 5519 6528 -911 -170 131 C ATOM 3657 CG LYS A1389 41.910 -93.823 142.510 1.00 51.83 C ANISOU 3657 CG LYS A1389 6606 5955 7133 -1046 -263 177 C ATOM 3658 CD LYS A1389 42.567 -93.394 143.812 1.00 64.32 C ANISOU 3658 CD LYS A1389 8257 7498 8684 -1133 -302 149 C ATOM 3659 CE LYS A1389 43.979 -93.944 143.930 1.00 66.55 C ANISOU 3659 CE LYS A1389 8400 8024 8860 -1212 -301 207 C ATOM 3660 NZ LYS A1389 44.603 -93.584 145.234 1.00 66.89 N ANISOU 3660 NZ LYS A1389 8501 8049 8864 -1302 -345 179 N ATOM 3661 N ALA A1390 40.357 -98.146 141.641 1.00 39.32 N ANISOU 3661 N ALA A1390 4820 4580 5541 -605 -3 2 N ATOM 3662 CA ALA A1390 40.433 -99.592 141.474 1.00 39.63 C ANISOU 3662 CA ALA A1390 4826 4704 5529 -504 61 -38 C ATOM 3663 C ALA A1390 40.046-100.011 140.063 1.00 39.10 C ANISOU 3663 C ALA A1390 4727 4689 5442 -474 66 -19 C ATOM 3664 O ALA A1390 40.576-101.000 139.544 1.00 40.95 O ANISOU 3664 O ALA A1390 4931 5034 5593 -407 99 -23 O ATOM 3665 CB ALA A1390 39.542-100.290 142.501 1.00 31.39 C ANISOU 3665 CB ALA A1390 3848 3549 4531 -434 109 -128 C ATOM 3666 N LEU A1391 39.130 -99.276 139.429 1.00 42.94 N ANISOU 3666 N LEU A1391 5227 5096 5992 -508 32 1 N ATOM 3667 CA LEU A1391 38.752 -99.586 138.054 1.00 43.12 C ANISOU 3667 CA LEU A1391 5218 5178 5989 -492 27 25 C ATOM 3668 C LEU A1391 39.901 -99.305 137.093 1.00 37.04 C ANISOU 3668 C LEU A1391 4378 4569 5128 -536 5 113 C ATOM 3669 O LEU A1391 40.204-100.122 136.216 1.00 42.19 O ANISOU 3669 O LEU A1391 4996 5339 5696 -481 31 112 O ATOM 3670 CB LEU A1391 37.509 -98.790 137.657 1.00 40.16 C ANISOU 3670 CB LEU A1391 4864 4698 5698 -510 -10 37 C ATOM 3671 CG LEU A1391 37.165 -98.774 136.164 1.00 35.95 C ANISOU 3671 CG LEU A1391 4293 4233 5134 -517 -37 85 C ATOM 3672 CD1 LEU A1391 36.913-100.173 135.636 1.00 40.86 C ANISOU 3672 CD1 LEU A1391 4911 4917 5695 -460 2 26 C ATOM 3673 CD2 LEU A1391 35.961 -97.899 135.915 1.00 30.19 C ANISOU 3673 CD2 LEU A1391 3579 3407 4486 -519 -79 106 C ATOM 3674 N GLU A1392 40.552 -98.149 137.241 1.00 42.24 N ANISOU 3674 N GLU A1392 5021 5239 5791 -640 -44 192 N ATOM 3675 CA GLU A1392 41.697 -97.840 136.392 1.00 54.88 C ANISOU 3675 CA GLU A1392 6535 7025 7293 -709 -65 295 C ATOM 3676 C GLU A1392 42.847 -98.806 136.636 1.00 57.24 C ANISOU 3676 C GLU A1392 6757 7509 7481 -643 -14 285 C ATOM 3677 O GLU A1392 43.623 -99.091 135.717 1.00 55.03 O ANISOU 3677 O GLU A1392 6388 7430 7091 -625 1 344 O ATOM 3678 CB GLU A1392 42.151 -96.399 136.624 1.00 63.88 C ANISOU 3678 CB GLU A1392 7693 8123 8454 -868 -140 387 C ATOM 3679 CG GLU A1392 41.137 -95.364 136.171 1.00 73.79 C ANISOU 3679 CG GLU A1392 9034 9208 9796 -911 -197 417 C ATOM 3680 CD GLU A1392 40.813 -95.477 134.692 1.00 81.33 C ANISOU 3680 CD GLU A1392 9941 10247 10712 -893 -201 471 C ATOM 3681 OE1 GLU A1392 41.744 -95.711 133.892 1.00 82.29 O ANISOU 3681 OE1 GLU A1392 9968 10572 10726 -929 -192 543 O ATOM 3682 OE2 GLU A1392 39.625 -95.339 134.330 1.00 83.01 O ANISOU 3682 OE2 GLU A1392 10204 10344 10993 -838 -214 445 O ATOM 3683 N LEU A1393 42.968 -99.320 137.860 1.00 60.66 N ANISOU 3683 N LEU A1393 7224 7893 7932 -591 15 216 N ATOM 3684 CA LEU A1393 43.999-100.310 138.145 1.00 57.89 C ANISOU 3684 CA LEU A1393 6811 7713 7473 -493 63 205 C ATOM 3685 C LEU A1393 43.701-101.630 137.445 1.00 58.51 C ANISOU 3685 C LEU A1393 6917 7820 7493 -334 120 141 C ATOM 3686 O LEU A1393 44.621-102.318 136.987 1.00 59.19 O ANISOU 3686 O LEU A1393 6940 8097 7452 -234 155 160 O ATOM 3687 CB LEU A1393 44.110-100.519 139.656 1.00 49.52 C ANISOU 3687 CB LEU A1393 5795 6574 6445 -475 74 150 C ATOM 3688 CG LEU A1393 45.389-101.165 140.187 1.00 47.47 C ANISOU 3688 CG LEU A1393 5455 6510 6072 -405 101 169 C ATOM 3689 CD1 LEU A1393 46.577-100.236 139.993 1.00 49.04 C ANISOU 3689 CD1 LEU A1393 5522 6914 6197 -542 52 289 C ATOM 3690 CD2 LEU A1393 45.221-101.526 141.648 1.00 50.98 C ANISOU 3690 CD2 LEU A1393 5972 6843 6556 -367 115 100 C ATOM 3691 N SER A1394 42.418-101.991 137.344 1.00 56.34 N ANISOU 3691 N SER A1394 6743 7366 7298 -307 127 66 N ATOM 3692 CA SER A1394 42.030-103.269 136.760 1.00 56.83 C ANISOU 3692 CA SER A1394 6871 7417 7304 -184 166 -5 C ATOM 3693 C SER A1394 42.356-103.360 135.276 1.00 62.89 C ANISOU 3693 C SER A1394 7590 8333 7973 -155 165 36 C ATOM 3694 O SER A1394 42.407-104.470 134.736 1.00 71.50 O ANISOU 3694 O SER A1394 8739 9455 8972 -32 198 -20 O ATOM 3695 CB SER A1394 40.536-103.503 136.976 1.00 59.26 C ANISOU 3695 CB SER A1394 7277 7523 7715 -208 160 -77 C ATOM 3696 OG SER A1394 39.778-102.479 136.360 1.00 60.01 O ANISOU 3696 OG SER A1394 7342 7576 7884 -305 114 -34 O ATOM 3697 N ARG A1395 42.572-102.226 134.605 1.00 62.74 N ANISOU 3697 N ARG A1395 7482 8396 7959 -266 124 132 N ATOM 3698 CA ARG A1395 42.916-102.254 133.188 1.00 58.65 C ANISOU 3698 CA ARG A1395 6908 8043 7335 -246 124 183 C ATOM 3699 C ARG A1395 44.279-102.885 132.942 1.00 63.50 C ANISOU 3699 C ARG A1395 7441 8901 7786 -129 173 209 C ATOM 3700 O ARG A1395 44.560-103.306 131.815 1.00 65.41 O ANISOU 3700 O ARG A1395 7658 9286 7907 -50 194 218 O ATOM 3701 CB ARG A1395 42.871-100.840 132.611 1.00 51.75 C ANISOU 3701 CB ARG A1395 5965 7197 6500 -405 65 298 C ATOM 3702 CG ARG A1395 41.580-100.104 132.930 1.00 52.16 C ANISOU 3702 CG ARG A1395 6094 7020 6706 -489 16 281 C ATOM 3703 CD ARG A1395 41.448 -98.808 132.149 1.00 53.18 C ANISOU 3703 CD ARG A1395 6191 7158 6857 -616 -48 395 C ATOM 3704 NE ARG A1395 40.253 -98.067 132.544 1.00 54.58 N ANISOU 3704 NE ARG A1395 6446 7120 7172 -660 -93 379 N ATOM 3705 CZ ARG A1395 39.027 -98.338 132.108 1.00 56.49 C ANISOU 3705 CZ ARG A1395 6728 7273 7462 -614 -101 330 C ATOM 3706 NH1 ARG A1395 38.830 -99.337 131.259 1.00 63.43 N ANISOU 3706 NH1 ARG A1395 7600 8237 8264 -545 -75 286 N ATOM 3707 NH2 ARG A1395 37.997 -97.612 132.523 1.00 46.11 N ANISOU 3707 NH2 ARG A1395 5465 5795 6261 -632 -138 325 N ATOM 3708 N SER A1396 45.125-102.959 133.963 1.00 63.31 N ANISOU 3708 N SER A1396 7369 8943 7744 -105 191 222 N ATOM 3709 CA SER A1396 46.383-103.683 133.896 1.00 60.83 C ANISOU 3709 CA SER A1396 6972 8872 7269 45 242 240 C ATOM 3710 C SER A1396 46.258-105.004 134.650 1.00 63.88 C ANISOU 3710 C SER A1396 7485 9147 7638 229 287 124 C ATOM 3711 O SER A1396 45.265-105.270 135.331 1.00 70.01 O ANISOU 3711 O SER A1396 8396 9675 8531 203 276 45 O ATOM 3712 CB SER A1396 47.522-102.836 134.470 1.00 60.51 C ANISOU 3712 CB SER A1396 6769 9026 7196 -61 222 354 C ATOM 3713 OG SER A1396 48.775-103.464 134.273 1.00 67.23 O ANISOU 3713 OG SER A1396 7499 10173 7872 91 272 392 O ATOM 3714 N ASP A1397 47.283-105.841 134.515 1.00 65.43 N ANISOU 3714 N ASP A1397 7641 9542 7676 422 338 123 N ATOM 3715 CA ASP A1397 47.289-107.125 135.202 1.00 69.47 C ANISOU 3715 CA ASP A1397 8294 9951 8151 617 377 25 C ATOM 3716 C ASP A1397 47.407-106.910 136.706 1.00 68.43 C ANISOU 3716 C ASP A1397 8154 9740 8106 558 363 32 C ATOM 3717 O ASP A1397 48.246-106.131 137.170 1.00 67.75 O ANISOU 3717 O ASP A1397 7907 9830 8007 474 346 123 O ATOM 3718 CB ASP A1397 48.439-107.994 134.692 1.00 79.34 C ANISOU 3718 CB ASP A1397 9499 11452 9193 870 434 31 C ATOM 3719 CG ASP A1397 48.259-109.465 135.033 1.00 87.73 C ANISOU 3719 CG ASP A1397 10780 12356 10197 1101 469 -86 C ATOM 3720 OD1 ASP A1397 47.689-109.774 136.100 1.00 89.91 O ANISOU 3720 OD1 ASP A1397 11180 12405 10578 1065 455 -137 O ATOM 3721 OD2 ASP A1397 48.690-110.317 134.227 1.00 89.35 O ANISOU 3721 OD2 ASP A1397 11048 12662 10241 1323 510 -125 O ATOM 3722 N LEU A1398 46.558-107.600 137.468 1.00 61.97 N ANISOU 3722 N LEU A1398 7514 8665 7368 587 366 -61 N ATOM 3723 CA LEU A1398 46.528-107.485 138.921 1.00 47.72 C ANISOU 3723 CA LEU A1398 5726 6764 5642 538 356 -67 C ATOM 3724 C LEU A1398 47.057-108.729 139.624 1.00 48.43 C ANISOU 3724 C LEU A1398 5911 6852 5638 753 395 -110 C ATOM 3725 O LEU A1398 46.951-108.823 140.851 1.00 52.07 O ANISOU 3725 O LEU A1398 6415 7215 6153 731 391 -124 O ATOM 3726 CB LEU A1398 45.104-107.192 139.398 1.00 38.06 C ANISOU 3726 CB LEU A1398 4616 5262 4584 387 329 -122 C ATOM 3727 CG LEU A1398 44.537-105.808 139.086 1.00 40.98 C ANISOU 3727 CG LEU A1398 4904 5601 5066 181 282 -75 C ATOM 3728 CD1 LEU A1398 43.107-105.695 139.584 1.00 34.52 C ANISOU 3728 CD1 LEU A1398 4194 4533 4387 86 268 -136 C ATOM 3729 CD2 LEU A1398 45.411-104.738 139.710 1.00 43.76 C ANISOU 3729 CD2 LEU A1398 5117 6087 5424 76 252 10 C ATOM 3730 N SER A1399 47.623-109.683 138.879 1.00 48.86 N ANISOU 3730 N SER A1399 6012 7011 5543 972 433 -133 N ATOM 3731 CA SER A1399 48.079-110.928 139.490 1.00 50.53 C ANISOU 3731 CA SER A1399 6353 7190 5654 1207 467 -177 C ATOM 3732 C SER A1399 49.154-110.676 140.539 1.00 55.19 C ANISOU 3732 C SER A1399 6793 7975 6200 1253 469 -103 C ATOM 3733 O SER A1399 49.143-111.295 141.610 1.00 58.83 O ANISOU 3733 O SER A1399 7361 8325 6667 1330 474 -129 O ATOM 3734 CB SER A1399 48.596-111.883 138.413 1.00 54.60 C ANISOU 3734 CB SER A1399 6944 7806 5995 1461 506 -212 C ATOM 3735 OG SER A1399 47.558-112.263 137.528 1.00 61.67 O ANISOU 3735 OG SER A1399 8015 8497 6919 1417 495 -293 O ATOM 3736 N LYS A1400 50.091-109.769 140.253 1.00 57.02 N ANISOU 3736 N LYS A1400 6777 8507 6379 1194 461 -2 N ATOM 3737 CA LYS A1400 51.145-109.472 141.218 1.00 57.90 C ANISOU 3737 CA LYS A1400 6724 8838 6437 1208 451 78 C ATOM 3738 C LYS A1400 50.579-108.789 142.457 1.00 52.12 C ANISOU 3738 C LYS A1400 6017 7929 5857 991 405 73 C ATOM 3739 O LYS A1400 51.061-109.017 143.574 1.00 50.89 O ANISOU 3739 O LYS A1400 5846 7816 5673 1043 399 89 O ATOM 3740 CB LYS A1400 52.224-108.608 140.565 1.00 67.09 C ANISOU 3740 CB LYS A1400 7611 10376 7503 1146 443 198 C ATOM 3741 CG LYS A1400 53.421-108.340 141.460 1.00 82.64 C ANISOU 3741 CG LYS A1400 9384 12630 9386 1157 426 293 C ATOM 3742 CD LYS A1400 53.989-109.639 142.012 1.00 92.75 C ANISOU 3742 CD LYS A1400 10735 13966 10540 1481 470 262 C ATOM 3743 CE LYS A1400 55.092-109.378 143.023 1.00 98.17 C ANISOU 3743 CE LYS A1400 11224 14931 11145 1483 444 358 C ATOM 3744 NZ LYS A1400 55.576-110.640 143.649 1.00101.79 N ANISOU 3744 NZ LYS A1400 11772 15419 11486 1813 481 331 N ATOM 3745 N PHE A1401 49.557-107.949 142.280 1.00 45.04 N ANISOU 3745 N PHE A1401 5160 6842 5111 762 372 51 N ATOM 3746 CA PHE A1401 48.884-107.342 143.423 1.00 39.47 C ANISOU 3746 CA PHE A1401 4507 5947 4542 584 336 29 C ATOM 3747 C PHE A1401 48.220-108.407 144.289 1.00 45.92 C ANISOU 3747 C PHE A1401 5524 6535 5388 694 363 -54 C ATOM 3748 O PHE A1401 48.289-108.348 145.523 1.00 48.36 O ANISOU 3748 O PHE A1401 5849 6805 5722 664 351 -54 O ATOM 3749 CB PHE A1401 47.858-106.318 142.929 1.00 37.30 C ANISOU 3749 CB PHE A1401 4251 5515 4407 368 302 18 C ATOM 3750 CG PHE A1401 47.469-105.275 143.950 1.00 36.75 C ANISOU 3750 CG PHE A1401 4179 5336 4450 173 255 23 C ATOM 3751 CD1 PHE A1401 47.750-105.439 145.295 1.00 41.16 C ANISOU 3751 CD1 PHE A1401 4758 5880 5000 187 251 11 C ATOM 3752 CD2 PHE A1401 46.810-104.123 143.550 1.00 40.40 C ANISOU 3752 CD2 PHE A1401 4633 5702 5015 -13 214 36 C ATOM 3753 CE1 PHE A1401 47.383-104.478 146.220 1.00 44.44 C ANISOU 3753 CE1 PHE A1401 5190 6191 5503 19 208 4 C ATOM 3754 CE2 PHE A1401 46.443-103.159 144.471 1.00 43.47 C ANISOU 3754 CE2 PHE A1401 5048 5974 5493 -166 170 29 C ATOM 3755 CZ PHE A1401 46.729-103.338 145.808 1.00 42.61 C ANISOU 3755 CZ PHE A1401 4965 5855 5371 -152 168 8 C ATOM 3756 N ARG A1402 47.584-109.397 143.660 1.00 40.92 N ANISOU 3756 N ARG A1402 5055 5751 4742 811 395 -122 N ATOM 3757 CA ARG A1402 46.898-110.433 144.425 1.00 37.36 C ANISOU 3757 CA ARG A1402 4815 5069 4313 884 414 -190 C ATOM 3758 C ARG A1402 47.886-111.291 145.207 1.00 41.65 C ANISOU 3758 C ARG A1402 5383 5710 4731 1094 433 -169 C ATOM 3759 O ARG A1402 47.589-111.721 146.327 1.00 45.13 O ANISOU 3759 O ARG A1402 5932 6017 5198 1100 435 -188 O ATOM 3760 CB ARG A1402 46.047-111.299 143.496 1.00 34.75 C ANISOU 3760 CB ARG A1402 4668 4557 3977 938 429 -262 C ATOM 3761 CG ARG A1402 45.021-110.514 142.694 1.00 33.45 C ANISOU 3761 CG ARG A1402 4474 4309 3926 744 407 -278 C ATOM 3762 CD ARG A1402 44.030-111.428 141.993 1.00 31.35 C ANISOU 3762 CD ARG A1402 4406 3846 3660 760 410 -352 C ATOM 3763 NE ARG A1402 43.177-110.692 141.062 1.00 32.88 N ANISOU 3763 NE ARG A1402 4546 4011 3936 602 384 -357 N ATOM 3764 CZ ARG A1402 42.119-109.972 141.422 1.00 35.19 C ANISOU 3764 CZ ARG A1402 4811 4194 4364 417 363 -359 C ATOM 3765 NH1 ARG A1402 41.777-109.883 142.701 1.00 32.35 N ANISOU 3765 NH1 ARG A1402 4473 3746 4073 359 369 -362 N ATOM 3766 NH2 ARG A1402 41.403-109.337 140.504 1.00 34.67 N ANISOU 3766 NH2 ARG A1402 4695 4122 4358 304 337 -356 N ATOM 3767 N GLU A1403 49.068-111.543 144.640 1.00 44.35 N ANISOU 3767 N GLU A1403 5617 6304 4928 1278 450 -123 N ATOM 3768 CA GLU A1403 50.061-112.353 145.340 1.00 47.09 C ANISOU 3768 CA GLU A1403 5972 6777 5141 1511 467 -94 C ATOM 3769 C GLU A1403 50.572-111.647 146.590 1.00 48.02 C ANISOU 3769 C GLU A1403 5944 7020 5283 1404 435 -31 C ATOM 3770 O GLU A1403 50.768-112.285 147.632 1.00 50.64 O ANISOU 3770 O GLU A1403 6360 7306 5575 1510 438 -31 O ATOM 3771 CB GLU A1403 51.219-112.695 144.404 1.00 56.67 C ANISOU 3771 CB GLU A1403 7070 8281 6180 1746 496 -52 C ATOM 3772 CG GLU A1403 50.869-113.708 143.323 1.00 73.53 C ANISOU 3772 CG GLU A1403 9407 10286 8245 1932 530 -128 C ATOM 3773 CD GLU A1403 50.276-114.987 143.888 1.00 85.32 C ANISOU 3773 CD GLU A1403 11218 11471 9730 2066 537 -204 C ATOM 3774 OE1 GLU A1403 49.033-115.083 143.971 1.00 88.57 O ANISOU 3774 OE1 GLU A1403 11803 11584 10266 1891 520 -267 O ATOM 3775 OE2 GLU A1403 51.054-115.893 144.255 1.00 90.00 O ANISOU 3775 OE2 GLU A1403 11885 12128 10183 2345 557 -193 O ATOM 3776 N ASN A1404 50.797-110.333 146.508 1.00 45.37 N ANISOU 3776 N ASN A1404 5406 6832 5001 1186 399 23 N ATOM 3777 CA ASN A1404 51.224-109.585 147.686 1.00 46.13 C ANISOU 3777 CA ASN A1404 5386 7025 5116 1050 355 72 C ATOM 3778 C ASN A1404 50.165-109.614 148.779 1.00 43.27 C ANISOU 3778 C ASN A1404 5194 6373 4875 941 348 7 C ATOM 3779 O ASN A1404 50.499-109.658 149.969 1.00 44.03 O ANISOU 3779 O ASN A1404 5284 6502 4944 945 331 25 O ATOM 3780 CB ASN A1404 51.551-108.140 147.308 1.00 48.54 C ANISOU 3780 CB ASN A1404 5490 7493 5458 808 306 136 C ATOM 3781 CG ASN A1404 52.739-108.035 146.371 1.00 56.72 C ANISOU 3781 CG ASN A1404 6315 8882 6352 891 312 226 C ATOM 3782 OD1 ASN A1404 53.624-108.891 146.373 1.00 62.43 O ANISOU 3782 OD1 ASN A1404 6984 9808 6928 1137 343 259 O ATOM 3783 ND2 ASN A1404 52.768-106.978 145.568 1.00 55.36 N ANISOU 3783 ND2 ASN A1404 6021 8796 6215 694 282 275 N ATOM 3784 N CYS A1405 48.886-109.596 148.397 1.00 39.76 N ANISOU 3784 N CYS A1405 4891 5666 4552 845 361 -63 N ATOM 3785 CA CYS A1405 47.818-109.666 149.388 1.00 37.16 C ANISOU 3785 CA CYS A1405 4708 5088 4323 749 364 -118 C ATOM 3786 C CYS A1405 47.783-111.029 150.069 1.00 39.67 C ANISOU 3786 C CYS A1405 5199 5300 4573 930 396 -139 C ATOM 3787 O CYS A1405 47.489-111.122 151.267 1.00 43.14 O ANISOU 3787 O CYS A1405 5704 5652 5034 890 394 -147 O ATOM 3788 CB CYS A1405 46.473-109.358 148.731 1.00 40.53 C ANISOU 3788 CB CYS A1405 5217 5304 4878 613 371 -176 C ATOM 3789 SG CYS A1405 46.326-107.674 148.082 1.00 46.43 S ANISOU 3789 SG CYS A1405 5804 6118 5718 392 327 -149 S ATOM 3790 N LYS A1406 48.077-112.097 149.324 1.00 42.23 N ANISOU 3790 N LYS A1406 5617 5623 4806 1135 423 -148 N ATOM 3791 CA LYS A1406 48.123-113.427 149.924 1.00 45.24 C ANISOU 3791 CA LYS A1406 6197 5886 5106 1324 444 -160 C ATOM 3792 C LYS A1406 49.257-113.535 150.936 1.00 42.09 C ANISOU 3792 C LYS A1406 5706 5683 4601 1451 432 -95 C ATOM 3793 O LYS A1406 49.046-113.971 152.074 1.00 44.45 O ANISOU 3793 O LYS A1406 6115 5877 4896 1462 431 -92 O ATOM 3794 CB LYS A1406 48.278-114.493 148.841 1.00 53.93 C ANISOU 3794 CB LYS A1406 7439 6939 6113 1535 468 -189 C ATOM 3795 CG LYS A1406 47.016-114.793 148.060 1.00 58.54 C ANISOU 3795 CG LYS A1406 8195 7270 6780 1425 473 -261 C ATOM 3796 CD LYS A1406 47.242-115.987 147.150 1.00 69.16 C ANISOU 3796 CD LYS A1406 9731 8544 8003 1654 489 -299 C ATOM 3797 CE LYS A1406 46.006-116.320 146.339 1.00 77.20 C ANISOU 3797 CE LYS A1406 10927 9319 9088 1526 481 -371 C ATOM 3798 NZ LYS A1406 46.242-117.509 145.476 1.00 77.43 N ANISOU 3798 NZ LYS A1406 11182 9257 8983 1749 487 -419 N ATOM 3799 N LYS A1407 50.471-113.143 150.535 1.00 39.58 N ANISOU 3799 N LYS A1407 5178 5674 4188 1542 421 -33 N ATOM 3800 CA LYS A1407 51.618-113.232 151.434 1.00 41.03 C ANISOU 3800 CA LYS A1407 5242 6094 4253 1665 402 40 C ATOM 3801 C LYS A1407 51.402-112.400 152.692 1.00 39.61 C ANISOU 3801 C LYS A1407 5002 5902 4147 1447 363 52 C ATOM 3802 O LYS A1407 51.806-112.804 153.789 1.00 42.72 O ANISOU 3802 O LYS A1407 5422 6337 4471 1531 351 84 O ATOM 3803 CB LYS A1407 52.888-112.782 150.714 1.00 46.71 C ANISOU 3803 CB LYS A1407 5699 7188 4859 1747 393 115 C ATOM 3804 CG LYS A1407 53.184-113.536 149.430 1.00 67.81 C ANISOU 3804 CG LYS A1407 8415 9914 7437 1983 437 101 C ATOM 3805 CD LYS A1407 54.378-112.930 148.707 1.00 80.44 C ANISOU 3805 CD LYS A1407 9716 11922 8924 2023 433 187 C ATOM 3806 CE LYS A1407 54.608-113.596 147.361 1.00 87.07 C ANISOU 3806 CE LYS A1407 10596 12825 9664 2256 483 165 C ATOM 3807 NZ LYS A1407 54.846-115.059 147.502 1.00 92.31 N ANISOU 3807 NZ LYS A1407 11473 13402 10199 2619 520 133 N ATOM 3808 N ARG A1408 50.766-111.236 152.554 1.00 38.66 N ANISOU 3808 N ARG A1408 4814 5720 4155 1179 341 26 N ATOM 3809 CA ARG A1408 50.529-110.380 153.711 1.00 43.43 C ANISOU 3809 CA ARG A1408 5383 6299 4818 980 303 23 C ATOM 3810 C ARG A1408 49.573-111.040 154.696 1.00 38.79 C ANISOU 3810 C ARG A1408 5008 5455 4276 986 329 -27 C ATOM 3811 O ARG A1408 49.851-111.098 155.899 1.00 43.89 O ANISOU 3811 O ARG A1408 5661 6141 4874 991 311 -6 O ATOM 3812 CB ARG A1408 49.988-109.025 153.257 1.00 46.95 C ANISOU 3812 CB ARG A1408 5751 6702 5386 723 274 -1 C ATOM 3813 CG ARG A1408 49.668-108.070 154.396 1.00 47.22 C ANISOU 3813 CG ARG A1408 5784 6682 5478 525 233 -22 C ATOM 3814 CD ARG A1408 50.863-107.881 155.314 1.00 48.02 C ANISOU 3814 CD ARG A1408 5760 7027 5458 534 181 43 C ATOM 3815 NE ARG A1408 50.591-106.910 156.368 1.00 54.48 N ANISOU 3815 NE ARG A1408 6594 7791 6317 336 133 14 N ATOM 3816 CZ ARG A1408 51.374-106.713 157.423 1.00 55.79 C ANISOU 3816 CZ ARG A1408 6694 8117 6387 308 82 50 C ATOM 3817 NH1 ARG A1408 52.482-107.428 157.569 1.00 58.75 N ANISOU 3817 NH1 ARG A1408 6964 8734 6624 472 73 128 N ATOM 3818 NH2 ARG A1408 51.048-105.807 158.334 1.00 53.42 N ANISOU 3818 NH2 ARG A1408 6438 7741 6120 126 37 8 N ATOM 3819 N ALA A1409 48.441-111.547 154.204 1.00 35.87 N ANISOU 3819 N ALA A1409 4806 4836 3988 975 369 -85 N ATOM 3820 CA ALA A1409 47.481-112.201 155.087 1.00 41.34 C ANISOU 3820 CA ALA A1409 5692 5300 4715 956 396 -119 C ATOM 3821 C ALA A1409 48.058-113.477 155.686 1.00 43.70 C ANISOU 3821 C ALA A1409 6117 5599 4887 1178 407 -79 C ATOM 3822 O ALA A1409 47.803-113.792 156.854 1.00 44.73 O ANISOU 3822 O ALA A1409 6340 5657 5000 1165 410 -69 O ATOM 3823 CB ALA A1409 46.189-112.504 154.331 1.00 32.38 C ANISOU 3823 CB ALA A1409 4692 3931 3678 880 428 -177 C ATOM 3824 N MET A1410 48.840-114.223 154.904 1.00 43.68 N ANISOU 3824 N MET A1410 6129 5682 4786 1397 413 -54 N ATOM 3825 CA MET A1410 49.401-115.472 155.404 1.00 42.27 C ANISOU 3825 CA MET A1410 6096 5488 4476 1647 421 -16 C ATOM 3826 C MET A1410 50.465-115.217 156.467 1.00 46.56 C ANISOU 3826 C MET A1410 6495 6275 4922 1715 389 55 C ATOM 3827 O MET A1410 50.479-115.886 157.507 1.00 48.30 O ANISOU 3827 O MET A1410 6842 6428 5083 1796 387 83 O ATOM 3828 CB MET A1410 49.967-116.292 154.245 1.00 38.19 C ANISOU 3828 CB MET A1410 5640 5005 3864 1894 437 -17 C ATOM 3829 CG MET A1410 48.903-117.060 153.471 1.00 45.26 C ANISOU 3829 CG MET A1410 6789 5598 4811 1879 461 -84 C ATOM 3830 SD MET A1410 49.468-117.765 151.907 1.00 55.92 S ANISOU 3830 SD MET A1410 8203 6989 6055 2134 478 -111 S ATOM 3831 CE MET A1410 51.246-117.661 152.094 1.00 53.12 C ANISOU 3831 CE MET A1410 7610 7040 5532 2409 473 -24 C ATOM 3832 N SER A1411 51.356-114.250 156.233 1.00 46.39 N ANISOU 3832 N SER A1411 6208 6544 4874 1668 357 91 N ATOM 3833 CA SER A1411 52.393-113.962 157.220 1.00 46.40 C ANISOU 3833 CA SER A1411 6053 6806 4771 1705 313 163 C ATOM 3834 C SER A1411 51.822-113.261 158.446 1.00 53.64 C ANISOU 3834 C SER A1411 6982 7642 5758 1477 288 142 C ATOM 3835 O SER A1411 52.368-113.399 159.546 1.00 60.18 O ANISOU 3835 O SER A1411 7786 8585 6495 1526 258 189 O ATOM 3836 CB SER A1411 53.502-113.112 156.600 1.00 42.78 C ANISOU 3836 CB SER A1411 5303 6697 4254 1682 278 218 C ATOM 3837 OG SER A1411 53.122-111.749 156.533 1.00 52.35 O ANISOU 3837 OG SER A1411 6399 7913 5580 1375 245 191 O ATOM 3838 N PHE A1412 50.734-112.507 158.278 1.00 51.49 N ANISOU 3838 N PHE A1412 6747 7185 5632 1242 299 72 N ATOM 3839 CA PHE A1412 50.112-111.851 159.423 1.00 47.30 C ANISOU 3839 CA PHE A1412 6245 6569 5156 1050 284 40 C ATOM 3840 C PHE A1412 49.397-112.858 160.314 1.00 50.48 C ANISOU 3840 C PHE A1412 6868 6770 5544 1118 322 33 C ATOM 3841 O PHE A1412 49.471-112.766 161.544 1.00 56.20 O ANISOU 3841 O PHE A1412 7607 7527 6219 1083 305 49 O ATOM 3842 CB PHE A1412 49.141-110.772 158.946 1.00 35.81 C ANISOU 3842 CB PHE A1412 4772 4985 3850 817 288 -31 C ATOM 3843 CG PHE A1412 48.468-110.022 160.060 1.00 36.16 C ANISOU 3843 CG PHE A1412 4852 4946 3942 643 278 -76 C ATOM 3844 CD1 PHE A1412 49.070-108.911 160.629 1.00 38.02 C ANISOU 3844 CD1 PHE A1412 4962 5335 4148 510 214 -72 C ATOM 3845 CD2 PHE A1412 47.226-110.418 160.529 1.00 37.78 C ANISOU 3845 CD2 PHE A1412 5220 4927 4209 605 332 -122 C ATOM 3846 CE1 PHE A1412 48.450-108.215 161.651 1.00 41.05 C ANISOU 3846 CE1 PHE A1412 5403 5633 4560 370 205 -126 C ATOM 3847 CE2 PHE A1412 46.603-109.727 161.550 1.00 43.68 C ANISOU 3847 CE2 PHE A1412 5994 5619 4983 470 332 -166 C ATOM 3848 CZ PHE A1412 47.215-108.624 162.112 1.00 42.33 C ANISOU 3848 CZ PHE A1412 5718 5586 4780 365 270 -175 C ATOM 3849 N SER A1413 48.693-113.822 159.717 1.00 44.87 N ANISOU 3849 N SER A1413 6338 5848 4865 1200 369 14 N ATOM 3850 CA SER A1413 47.989-114.816 160.520 1.00 49.73 C ANISOU 3850 CA SER A1413 7176 6260 5458 1236 400 22 C ATOM 3851 C SER A1413 48.946-115.842 161.116 1.00 52.70 C ANISOU 3851 C SER A1413 7627 6716 5680 1480 384 99 C ATOM 3852 O SER A1413 48.696-116.354 162.212 1.00 51.82 O ANISOU 3852 O SER A1413 7643 6526 5520 1490 390 130 O ATOM 3853 CB SER A1413 46.916-115.506 159.682 1.00 57.39 C ANISOU 3853 CB SER A1413 8328 6975 6503 1211 442 -18 C ATOM 3854 OG SER A1413 47.461-115.997 158.472 1.00 71.67 O ANISOU 3854 OG SER A1413 10149 8807 8277 1373 439 -17 O ATOM 3855 N ASP A 398 50.035-116.161 160.413 1.00 53.40 N ANISOU 3855 N ASP A 398 7638 6971 5680 1691 367 136 N ATOM 3856 CA ASP A 398 51.058-117.033 160.981 1.00 57.04 C ANISOU 3856 CA ASP A 398 8138 7555 5979 1956 347 216 C ATOM 3857 C ASP A 398 51.674-116.407 162.224 1.00 54.82 C ANISOU 3857 C ASP A 398 7702 7493 5634 1895 303 264 C ATOM 3858 O ASP A 398 51.833-117.068 163.258 1.00 58.31 O ANISOU 3858 O ASP A 398 8255 7915 5984 1997 293 317 O ATOM 3859 CB ASP A 398 52.135-117.318 159.935 1.00 64.13 C ANISOU 3859 CB ASP A 398 8932 8649 6787 2199 342 246 C ATOM 3860 CG ASP A 398 51.746-118.432 158.989 1.00 76.20 C ANISOU 3860 CG ASP A 398 10705 9943 8304 2372 378 215 C ATOM 3861 OD1 ASP A 398 50.653-119.010 159.165 1.00 78.38 O ANISOU 3861 OD1 ASP A 398 11234 9904 8644 2283 400 179 O ATOM 3862 OD2 ASP A 398 52.540-118.734 158.076 1.00 79.99 O ANISOU 3862 OD2 ASP A 398 11128 10565 8701 2594 383 227 O ATOM 3863 N THR A 399 52.026-115.124 162.137 1.00 54.69 N ANISOU 3863 N THR A 399 7442 7681 5658 1719 268 247 N ATOM 3864 CA THR A 399 52.591-114.421 163.282 1.00 53.67 C ANISOU 3864 CA THR A 399 7172 7756 5463 1623 212 281 C ATOM 3865 C THR A 399 51.578-114.315 164.415 1.00 58.06 C ANISOU 3865 C THR A 399 7875 8116 6068 1463 229 242 C ATOM 3866 O THR A 399 51.926-114.491 165.589 1.00 60.50 O ANISOU 3866 O THR A 399 8199 8510 6277 1496 201 287 O ATOM 3867 CB THR A 399 53.074-113.037 162.843 1.00 53.51 C ANISOU 3867 CB THR A 399 6899 7950 5481 1430 164 265 C ATOM 3868 OG1 THR A 399 54.233-113.179 162.012 1.00 53.27 O ANISOU 3868 OG1 THR A 399 6693 8189 5359 1593 144 331 O ATOM 3869 CG2 THR A 399 53.419-112.177 164.037 1.00 53.93 C ANISOU 3869 CG2 THR A 399 6852 8155 5485 1263 98 274 C ATOM 3870 N ARG A 400 50.312-114.060 164.079 1.00 58.56 N ANISOU 3870 N ARG A 400 8044 7934 6273 1299 276 164 N ATOM 3871 CA ARG A 400 49.282-113.923 165.105 1.00 57.48 C ANISOU 3871 CA ARG A 400 8027 7637 6174 1150 303 128 C ATOM 3872 C ARG A 400 49.000-115.249 165.801 1.00 56.62 C ANISOU 3872 C ARG A 400 8136 7388 5988 1286 334 184 C ATOM 3873 O ARG A 400 48.772-115.280 167.016 1.00 53.29 O ANISOU 3873 O ARG A 400 7771 6964 5511 1236 334 202 O ATOM 3874 CB ARG A 400 48.004-113.361 164.490 1.00 55.07 C ANISOU 3874 CB ARG A 400 7757 7139 6027 964 349 42 C ATOM 3875 CG ARG A 400 47.979-111.853 164.421 1.00 53.59 C ANISOU 3875 CG ARG A 400 7410 7043 5908 774 316 -20 C ATOM 3876 CD ARG A 400 48.214-111.269 165.796 1.00 52.50 C ANISOU 3876 CD ARG A 400 7243 7009 5694 694 280 -24 C ATOM 3877 NE ARG A 400 47.506-110.008 165.972 1.00 49.75 N ANISOU 3877 NE ARG A 400 6865 6608 5430 495 277 -111 N ATOM 3878 CZ ARG A 400 48.057-108.814 165.796 1.00 48.76 C ANISOU 3878 CZ ARG A 400 6613 6600 5314 378 211 -140 C ATOM 3879 NH1 ARG A 400 49.330-108.712 165.442 1.00 50.31 N ANISOU 3879 NH1 ARG A 400 6669 7007 5439 418 144 -80 N ATOM 3880 NH2 ARG A 400 47.331-107.724 165.978 1.00 48.63 N ANISOU 3880 NH2 ARG A 400 6615 6495 5367 221 210 -225 N ATOM 3881 N GLN A 401 48.997-116.352 165.050 1.00 60.21 N ANISOU 3881 N GLN A 401 8735 7714 6429 1454 357 213 N ATOM 3882 CA GLN A 401 48.745-117.652 165.661 1.00 65.25 C ANISOU 3882 CA GLN A 401 9619 8186 6986 1579 376 275 C ATOM 3883 C GLN A 401 49.872-118.050 166.603 1.00 70.68 C ANISOU 3883 C GLN A 401 10282 9062 7511 1769 330 364 C ATOM 3884 O GLN A 401 49.625-118.695 167.630 1.00 64.69 O ANISOU 3884 O GLN A 401 9681 8219 6678 1794 336 418 O ATOM 3885 CB GLN A 401 48.554-118.715 164.578 1.00 75.78 C ANISOU 3885 CB GLN A 401 11141 9324 8329 1722 398 277 C ATOM 3886 CG GLN A 401 47.696-119.892 165.012 1.00 90.68 C ANISOU 3886 CG GLN A 401 13336 10927 10191 1719 425 314 C ATOM 3887 CD GLN A 401 46.231-119.522 165.151 1.00 99.07 C ANISOU 3887 CD GLN A 401 14440 11827 11374 1429 469 264 C ATOM 3888 OE1 GLN A 401 45.639-119.668 166.221 1.00 95.95 O ANISOU 3888 OE1 GLN A 401 14124 11379 10953 1319 488 298 O ATOM 3889 NE2 GLN A 401 45.637-119.045 164.062 1.00104.37 N ANISOU 3889 NE2 GLN A 401 15048 12441 12168 1311 488 189 N ATOM 3890 N GLN A 402 51.109-117.672 166.275 1.00 75.98 N ANISOU 3890 N GLN A 402 10748 10007 8115 1899 284 390 N ATOM 3891 CA GLN A 402 52.234-117.948 167.162 1.00 75.83 C ANISOU 3891 CA GLN A 402 10660 10221 7931 2075 232 481 C ATOM 3892 C GLN A 402 52.114-117.163 168.463 1.00 70.08 C ANISOU 3892 C GLN A 402 9851 9598 7180 1883 203 477 C ATOM 3893 O GLN A 402 52.385-117.698 169.545 1.00 77.72 O ANISOU 3893 O GLN A 402 10897 10606 8026 1975 182 548 O ATOM 3894 CB GLN A 402 53.545-117.622 166.449 1.00 82.93 C ANISOU 3894 CB GLN A 402 11314 11434 8760 2226 189 514 C ATOM 3895 CG GLN A 402 54.789-117.742 167.311 1.00 93.45 C ANISOU 3895 CG GLN A 402 12511 13081 9915 2392 124 614 C ATOM 3896 CD GLN A 402 56.054-117.410 166.543 1.00102.29 C ANISOU 3896 CD GLN A 402 13358 14549 10957 2528 86 657 C ATOM 3897 OE1 GLN A 402 56.090-117.504 165.316 1.00103.22 O ANISOU 3897 OE1 GLN A 402 13453 14643 11123 2603 119 628 O ATOM 3898 NE2 GLN A 402 57.098-117.014 167.261 1.00108.42 N ANISOU 3898 NE2 GLN A 402 13918 15674 11603 2551 15 731 N ATOM 3899 N TYR A 403 51.706-115.895 168.379 1.00 64.02 N ANISOU 3899 N TYR A 403 8942 8867 6515 1626 198 393 N ATOM 3900 CA TYR A 403 51.548-115.091 169.586 1.00 63.35 C ANISOU 3900 CA TYR A 403 8805 8864 6401 1445 170 369 C ATOM 3901 C TYR A 403 50.373-115.569 170.427 1.00 62.07 C ANISOU 3901 C TYR A 403 8860 8468 6255 1370 229 358 C ATOM 3902 O TYR A 403 50.408-115.457 171.658 1.00 66.74 O ANISOU 3902 O TYR A 403 9471 9132 6755 1328 210 380 O ATOM 3903 CB TYR A 403 51.361-113.616 169.225 1.00 64.29 C ANISOU 3903 CB TYR A 403 8761 9044 6621 1202 148 276 C ATOM 3904 CG TYR A 403 52.530-112.981 168.505 1.00 66.71 C ANISOU 3904 CG TYR A 403 8834 9614 6900 1215 80 298 C ATOM 3905 CD1 TYR A 403 53.760-113.623 168.420 1.00 73.17 C ANISOU 3905 CD1 TYR A 403 9553 10665 7582 1439 39 399 C ATOM 3906 CD2 TYR A 403 52.404-111.731 167.915 1.00 66.18 C ANISOU 3906 CD2 TYR A 403 8642 9573 6930 1005 56 226 C ATOM 3907 CE1 TYR A 403 54.826-113.041 167.762 1.00 75.43 C ANISOU 3907 CE1 TYR A 403 9599 11233 7827 1438 -19 433 C ATOM 3908 CE2 TYR A 403 53.464-111.141 167.260 1.00 70.88 C ANISOU 3908 CE2 TYR A 403 9022 10420 7491 986 -8 261 C ATOM 3909 CZ TYR A 403 54.673-111.800 167.185 1.00 75.16 C ANISOU 3909 CZ TYR A 403 9444 11220 7893 1195 -43 367 C ATOM 3910 OH TYR A 403 55.732-111.214 166.528 1.00 81.32 O ANISOU 3910 OH TYR A 403 9982 12291 8624 1166 -103 414 O ATOM 3911 N ARG A 404 49.327-116.097 169.786 1.00 54.65 N ANISOU 3911 N ARG A 404 8077 7267 5421 1342 298 330 N ATOM 3912 CA ARG A 404 48.155-116.551 170.527 1.00 51.52 C ANISOU 3912 CA ARG A 404 7869 6672 5036 1244 356 332 C ATOM 3913 C ARG A 404 48.482-117.738 171.422 1.00 55.03 C ANISOU 3913 C ARG A 404 8484 7090 5334 1406 347 445 C ATOM 3914 O ARG A 404 47.902-117.875 172.505 1.00 56.07 O ANISOU 3914 O ARG A 404 8710 7180 5414 1320 372 468 O ATOM 3915 CB ARG A 404 47.032-116.913 169.557 1.00 48.87 C ANISOU 3915 CB ARG A 404 7651 6086 4832 1167 420 292 C ATOM 3916 CG ARG A 404 45.634-116.679 170.102 1.00 54.40 C ANISOU 3916 CG ARG A 404 8422 6657 5592 960 484 254 C ATOM 3917 CD ARG A 404 44.580-117.169 169.123 1.00 65.76 C ANISOU 3917 CD ARG A 404 9971 7873 7142 886 534 233 C ATOM 3918 NE ARG A 404 44.980-116.941 167.736 1.00 77.92 N ANISOU 3918 NE ARG A 404 11429 9412 8765 943 513 188 N ATOM 3919 CZ ARG A 404 44.819-115.791 167.090 1.00 82.01 C ANISOU 3919 CZ ARG A 404 11773 9997 9389 836 511 104 C ATOM 3920 NH1 ARG A 404 45.214-115.677 165.829 1.00 85.32 N ANISOU 3920 NH1 ARG A 404 12127 10421 9868 894 492 78 N ATOM 3921 NH2 ARG A 404 44.267-114.754 167.705 1.00 80.57 N ANISOU 3921 NH2 ARG A 404 11496 9874 9244 682 528 46 N ATOM 3922 N LYS A 405 49.402-118.605 170.989 1.00 55.44 N ANISOU 3922 N LYS A 405 8585 7173 5308 1654 314 518 N ATOM 3923 CA LYS A 405 49.792-119.744 171.813 1.00 61.07 C ANISOU 3923 CA LYS A 405 9476 7856 5871 1841 296 634 C ATOM 3924 C LYS A 405 50.503-119.289 173.081 1.00 64.30 C ANISOU 3924 C LYS A 405 9762 8519 6150 1847 244 676 C ATOM 3925 O LYS A 405 50.274-119.845 174.161 1.00 71.03 O ANISOU 3925 O LYS A 405 10759 9326 6904 1859 249 747 O ATOM 3926 CB LYS A 405 50.680-120.691 171.008 1.00 61.91 C ANISOU 3926 CB LYS A 405 9656 7954 5913 2143 270 694 C ATOM 3927 CG LYS A 405 49.996-121.302 169.799 1.00 64.63 C ANISOU 3927 CG LYS A 405 10174 8024 6358 2153 313 654 C ATOM 3928 CD LYS A 405 50.967-122.135 168.980 1.00 69.74 C ANISOU 3928 CD LYS A 405 10885 8690 6923 2481 286 697 C ATOM 3929 CE LYS A 405 50.294-122.710 167.747 1.00 79.72 C ANISOU 3929 CE LYS A 405 12337 9676 8276 2484 321 643 C ATOM 3930 NZ LYS A 405 51.252-123.474 166.901 1.00 89.61 N ANISOU 3930 NZ LYS A 405 13658 10955 9437 2827 300 670 N ATOM 3931 N LEU A 406 51.371-118.281 172.969 1.00 61.25 N ANISOU 3931 N LEU A 406 9113 8407 5752 1825 189 640 N ATOM 3932 CA LEU A 406 52.037-117.747 174.152 1.00 67.17 C ANISOU 3932 CA LEU A 406 9739 9410 6374 1795 126 670 C ATOM 3933 C LEU A 406 51.057-116.991 175.040 1.00 60.62 C ANISOU 3933 C LEU A 406 8936 8519 5580 1536 158 597 C ATOM 3934 O LEU A 406 51.134-117.073 176.271 1.00 61.70 O ANISOU 3934 O LEU A 406 9114 8736 5592 1524 138 640 O ATOM 3935 CB LEU A 406 53.198-116.845 173.735 1.00 48.54 C ANISOU 3935 CB LEU A 406 7094 7361 3988 1800 50 655 C ATOM 3936 CG LEU A 406 53.919-116.084 174.850 1.00 60.56 C ANISOU 3936 CG LEU A 406 8459 9168 5381 1713 -34 669 C ATOM 3937 CD1 LEU A 406 54.479-117.044 175.896 1.00 52.09 C ANISOU 3937 CD1 LEU A 406 7475 8193 4125 1917 -67 795 C ATOM 3938 CD2 LEU A 406 55.021-115.206 174.273 1.00 49.73 C ANISOU 3938 CD2 LEU A 406 6807 8098 3991 1680 -114 662 C ATOM 3939 N ALA A 407 50.123-116.255 174.433 1.00 53.13 N ANISOU 3939 N ALA A 407 7965 7435 4787 1342 209 486 N ATOM 3940 CA ALA A 407 49.141-115.507 175.206 1.00 54.78 C ANISOU 3940 CA ALA A 407 8197 7591 5025 1126 249 408 C ATOM 3941 C ALA A 407 48.109-116.411 175.866 1.00 62.05 C ANISOU 3941 C ALA A 407 9335 8323 5918 1111 325 459 C ATOM 3942 O ALA A 407 47.443-115.979 176.813 1.00 65.24 O ANISOU 3942 O ALA A 407 9764 8740 6286 979 357 424 O ATOM 3943 CB ALA A 407 48.438-114.483 174.315 1.00 48.81 C ANISOU 3943 CB ALA A 407 7357 6751 4437 955 281 284 C ATOM 3944 N LYS A 408 47.960-117.652 175.390 1.00 61.07 N ANISOU 3944 N LYS A 408 9378 8027 5800 1239 351 542 N ATOM 3945 CA LYS A 408 47.003-118.570 176.000 1.00 64.79 C ANISOU 3945 CA LYS A 408 10070 8314 6233 1198 414 610 C ATOM 3946 C LYS A 408 47.334-118.841 177.461 1.00 67.74 C ANISOU 3946 C LYS A 408 10498 8809 6430 1238 390 693 C ATOM 3947 O LYS A 408 46.435-119.141 178.255 1.00 72.42 O ANISOU 3947 O LYS A 408 11214 9322 6980 1129 447 726 O ATOM 3948 CB LYS A 408 46.956-119.881 175.214 1.00 73.64 C ANISOU 3948 CB LYS A 408 11392 9216 7370 1335 423 689 C ATOM 3949 CG LYS A 408 45.925-119.904 174.095 1.00 80.06 C ANISOU 3949 CG LYS A 408 12252 9821 8345 1207 480 625 C ATOM 3950 CD LYS A 408 44.510-119.940 174.652 1.00 87.18 C ANISOU 3950 CD LYS A 408 13242 10609 9272 983 557 624 C ATOM 3951 CE LYS A 408 43.473-119.988 173.541 1.00 86.43 C ANISOU 3951 CE LYS A 408 13180 10333 9328 848 605 571 C ATOM 3952 NZ LYS A 408 43.475-118.745 172.720 1.00 82.98 N ANISOU 3952 NZ LYS A 408 12516 9991 9022 787 605 441 N ATOM 3953 N SER A 409 48.609-118.741 177.836 1.00 63.96 N ANISOU 3953 N SER A 409 9920 8545 5837 1388 306 734 N ATOM 3954 CA SER A 409 49.029-118.924 179.218 1.00 58.15 C ANISOU 3954 CA SER A 409 9216 7958 4921 1432 269 811 C ATOM 3955 C SER A 409 49.526-117.648 179.877 1.00 61.61 C ANISOU 3955 C SER A 409 9449 8656 5303 1328 215 729 C ATOM 3956 O SER A 409 49.329-117.477 181.081 1.00 67.55 O ANISOU 3956 O SER A 409 10235 9493 5937 1259 216 741 O ATOM 3957 CB SER A 409 50.129-119.990 179.304 1.00 55.88 C ANISOU 3957 CB SER A 409 9004 7725 4502 1711 204 951 C ATOM 3958 OG SER A 409 51.283-119.590 178.588 1.00 62.20 O ANISOU 3958 OG SER A 409 9606 8717 5308 1841 133 931 O ATOM 3959 N THR A 410 50.159-116.748 179.120 1.00 58.85 N ANISOU 3959 N THR A 410 8902 8432 5025 1303 163 648 N ATOM 3960 CA THR A 410 50.646-115.503 179.706 1.00 56.79 C ANISOU 3960 CA THR A 410 8473 8398 4707 1175 95 567 C ATOM 3961 C THR A 410 49.493-114.613 180.153 1.00 51.09 C ANISOU 3961 C THR A 410 7786 7586 4040 956 158 444 C ATOM 3962 O THR A 410 49.540-114.029 181.242 1.00 51.05 O ANISOU 3962 O THR A 410 7770 7709 3918 872 130 407 O ATOM 3963 CB THR A 410 51.539-114.762 178.710 1.00 58.80 C ANISOU 3963 CB THR A 410 8521 8793 5028 1171 24 521 C ATOM 3964 OG1 THR A 410 52.642-115.599 178.339 1.00 64.39 O ANISOU 3964 OG1 THR A 410 9178 9626 5660 1405 -28 641 O ATOM 3965 CG2 THR A 410 52.075-113.478 179.325 1.00 54.60 C ANISOU 3965 CG2 THR A 410 7841 8481 4424 1008 -63 444 C ATOM 3966 N LEU A 411 48.445-114.501 179.335 1.00 57.46 N ANISOU 3966 N LEU A 411 8635 8184 5011 874 244 377 N ATOM 3967 CA LEU A 411 47.293-113.688 179.708 1.00 57.09 C ANISOU 3967 CA LEU A 411 8614 8065 5012 700 314 265 C ATOM 3968 C LEU A 411 46.485-114.298 180.845 1.00 56.52 C ANISOU 3968 C LEU A 411 8687 7955 4831 683 386 320 C ATOM 3969 O LEU A 411 45.547-113.655 181.328 1.00 62.17 O ANISOU 3969 O LEU A 411 9418 8655 5550 563 450 234 O ATOM 3970 CB LEU A 411 46.389-113.461 178.496 1.00 53.20 C ANISOU 3970 CB LEU A 411 8112 7385 4716 631 383 195 C ATOM 3971 CG LEU A 411 46.976-112.609 177.369 1.00 56.58 C ANISOU 3971 CG LEU A 411 8394 7846 5260 605 324 121 C ATOM 3972 CD1 LEU A 411 45.974-112.449 176.236 1.00 56.16 C ANISOU 3972 CD1 LEU A 411 8346 7605 5389 540 397 60 C ATOM 3973 CD2 LEU A 411 47.416-111.252 177.896 1.00 52.20 C ANISOU 3973 CD2 LEU A 411 7744 7438 4653 492 251 19 C ATOM 3974 N VAL A 412 46.815-115.511 181.275 1.00 52.63 N ANISOU 3974 N VAL A 412 8306 7454 4236 808 379 464 N ATOM 3975 CA VAL A 412 46.175-116.131 182.426 1.00 58.03 C ANISOU 3975 CA VAL A 412 9131 8126 4792 786 437 541 C ATOM 3976 C VAL A 412 46.991-115.926 183.696 1.00 58.04 C ANISOU 3976 C VAL A 412 9112 8349 4593 827 364 571 C ATOM 3977 O VAL A 412 46.433-115.630 184.752 1.00 60.70 O ANISOU 3977 O VAL A 412 9490 8751 4823 742 404 546 O ATOM 3978 CB VAL A 412 45.933-117.633 182.156 1.00 58.91 C ANISOU 3978 CB VAL A 412 9422 8058 4903 879 472 692 C ATOM 3979 CG1 VAL A 412 45.321-118.305 183.375 1.00 57.14 C ANISOU 3979 CG1 VAL A 412 9350 7830 4531 840 524 794 C ATOM 3980 CG2 VAL A 412 45.040-117.816 180.940 1.00 54.53 C ANISOU 3980 CG2 VAL A 412 8897 7288 4534 808 539 656 C ATOM 3981 N LEU A 413 48.317-116.064 183.605 1.00 58.80 N ANISOU 3981 N LEU A 413 9132 8585 4623 958 254 625 N ATOM 3982 CA LEU A 413 49.157-115.962 184.793 1.00 60.08 C ANISOU 3982 CA LEU A 413 9268 8979 4582 1003 171 671 C ATOM 3983 C LEU A 413 49.285-114.526 185.283 1.00 61.75 C ANISOU 3983 C LEU A 413 9361 9348 4752 849 124 521 C ATOM 3984 O LEU A 413 49.436-114.299 186.489 1.00 67.31 O ANISOU 3984 O LEU A 413 10090 10200 5282 817 93 521 O ATOM 3985 CB LEU A 413 50.541-116.547 184.508 1.00 60.63 C ANISOU 3985 CB LEU A 413 9269 9182 4584 1200 66 783 C ATOM 3986 CG LEU A 413 50.584-118.017 184.089 1.00 62.84 C ANISOU 3986 CG LEU A 413 9702 9302 4871 1398 94 935 C ATOM 3987 CD1 LEU A 413 52.022-118.494 183.961 1.00 65.95 C ANISOU 3987 CD1 LEU A 413 10012 9883 5162 1630 -13 1041 C ATOM 3988 CD2 LEU A 413 49.814-118.883 185.073 1.00 66.35 C ANISOU 3988 CD2 LEU A 413 10364 9636 5210 1392 158 1036 C ATOM 3989 N MET A 414 49.239-113.549 184.377 1.00 62.24 N ANISOU 3989 N MET A 414 9313 9372 4961 751 112 392 N ATOM 3990 CA MET A 414 49.361-112.154 184.795 1.00 69.93 C ANISOU 3990 CA MET A 414 10215 10459 5895 598 56 244 C ATOM 3991 C MET A 414 48.227-111.716 185.715 1.00 74.99 C ANISOU 3991 C MET A 414 10967 11049 6477 500 143 155 C ATOM 3992 O MET A 414 48.518-111.195 186.806 1.00 76.95 O ANISOU 3992 O MET A 414 11232 11450 6555 450 89 111 O ATOM 3993 CB MET A 414 49.469-111.248 183.563 1.00 70.87 C ANISOU 3993 CB MET A 414 10222 10515 6191 514 29 138 C ATOM 3994 CG MET A 414 50.723-111.460 182.732 1.00 75.72 C ANISOU 3994 CG MET A 414 10691 11250 6830 595 -68 215 C ATOM 3995 SD MET A 414 50.611-110.668 181.115 1.00 75.29 S ANISOU 3995 SD MET A 414 10530 11075 7002 510 -65 121 S ATOM 3996 CE MET A 414 50.468-108.945 181.576 1.00 74.14 C ANISOU 3996 CE MET A 414 10374 10964 6831 278 -127 -57 C ATOM 3997 N PRO A 415 46.936-111.889 185.367 1.00 75.08 N ANISOU 3997 N PRO A 415 11050 10874 6603 471 276 125 N ATOM 3998 CA PRO A 415 45.881-111.453 186.292 1.00 74.43 C ANISOU 3998 CA PRO A 415 11050 10791 6439 398 364 46 C ATOM 3999 C PRO A 415 45.708-112.394 187.474 1.00 73.69 C ANISOU 3999 C PRO A 415 11060 10776 6162 450 405 171 C ATOM 4000 O PRO A 415 45.308-111.960 188.557 1.00 76.83 O ANISOU 4000 O PRO A 415 11510 11272 6412 406 434 114 O ATOM 4001 CB PRO A 415 44.631-111.425 185.406 1.00 73.32 C ANISOU 4001 CB PRO A 415 10916 10460 6481 358 487 0 C ATOM 4002 CG PRO A 415 44.885-112.472 184.395 1.00 74.84 C ANISOU 4002 CG PRO A 415 11102 10539 6795 431 486 124 C ATOM 4003 CD PRO A 415 46.364-112.430 184.119 1.00 74.10 C ANISOU 4003 CD PRO A 415 10926 10554 6676 498 348 158 C ATOM 4004 N LEU A 416 46.005-113.682 187.282 1.00 68.89 N ANISOU 4004 N LEU A 416 10501 10122 5554 550 405 343 N ATOM 4005 CA LEU A 416 45.845-114.646 188.367 1.00 67.98 C ANISOU 4005 CA LEU A 416 10505 10060 5264 597 438 484 C ATOM 4006 C LEU A 416 46.770-114.316 189.532 1.00 68.49 C ANISOU 4006 C LEU A 416 10555 10357 5111 622 336 487 C ATOM 4007 O LEU A 416 46.339-114.268 190.690 1.00 72.42 O ANISOU 4007 O LEU A 416 11124 10950 5441 587 377 489 O ATOM 4008 CB LEU A 416 46.110-116.062 187.856 1.00 68.75 C ANISOU 4008 CB LEU A 416 10687 10035 5401 714 435 666 C ATOM 4009 CG LEU A 416 45.807-117.204 188.828 1.00 64.70 C ANISOU 4009 CG LEU A 416 10338 9519 4728 753 477 837 C ATOM 4010 CD1 LEU A 416 44.304-117.360 189.015 1.00 63.15 C ANISOU 4010 CD1 LEU A 416 10217 9220 4556 619 622 837 C ATOM 4011 CD2 LEU A 416 46.434-118.505 188.349 1.00 61.60 C ANISOU 4011 CD2 LEU A 416 10047 9011 4346 910 431 1008 C ATOM 4012 N PHE A 417 48.052-114.085 189.241 1.00 68.49 N ANISOU 4012 N PHE A 417 10453 10470 5099 680 201 490 N ATOM 4013 CA PHE A 417 48.995-113.720 190.293 1.00 67.95 C ANISOU 4013 CA PHE A 417 10351 10646 4820 685 86 492 C ATOM 4014 C PHE A 417 48.710-112.322 190.827 1.00 68.34 C ANISOU 4014 C PHE A 417 10383 10770 4812 534 71 297 C ATOM 4015 O PHE A 417 48.873-112.064 192.025 1.00 73.16 O ANISOU 4015 O PHE A 417 11040 11542 5217 506 34 279 O ATOM 4016 CB PHE A 417 50.428-113.811 189.768 1.00 64.99 C ANISOU 4016 CB PHE A 417 9842 10405 4446 774 -56 554 C ATOM 4017 CG PHE A 417 50.953-115.216 189.661 1.00 71.30 C ANISOU 4017 CG PHE A 417 10687 11198 5207 974 -69 758 C ATOM 4018 CD1 PHE A 417 50.369-116.129 188.799 1.00 72.73 C ANISOU 4018 CD1 PHE A 417 10956 11141 5536 1054 21 833 C ATOM 4019 CD2 PHE A 417 52.043-115.618 190.413 1.00 82.87 C ANISOU 4019 CD2 PHE A 417 12117 12894 6477 1088 -181 875 C ATOM 4020 CE1 PHE A 417 50.854-117.419 188.697 1.00 75.93 C ANISOU 4020 CE1 PHE A 417 11443 11510 5895 1253 3 1013 C ATOM 4021 CE2 PHE A 417 52.534-116.907 190.316 1.00 88.36 C ANISOU 4021 CE2 PHE A 417 12873 13573 7126 1305 -195 1064 C ATOM 4022 CZ PHE A 417 51.939-117.808 189.456 1.00 83.79 C ANISOU 4022 CZ PHE A 417 12412 12728 6697 1392 -104 1129 C ATOM 4023 N GLY A 418 48.277-111.410 189.956 1.00 65.70 N ANISOU 4023 N GLY A 418 10001 10312 4649 444 97 149 N ATOM 4024 CA GLY A 418 48.047-110.040 190.388 1.00 64.84 C ANISOU 4024 CA GLY A 418 9907 10242 4487 317 71 -45 C ATOM 4025 C GLY A 418 46.815-109.899 191.262 1.00 69.54 C ANISOU 4025 C GLY A 418 10622 10808 4990 298 201 -109 C ATOM 4026 O GLY A 418 46.853-109.241 192.305 1.00 72.09 O ANISOU 4026 O GLY A 418 11007 11254 5129 252 169 -202 O ATOM 4027 N VAL A 419 45.704-110.512 190.847 1.00 67.71 N ANISOU 4027 N VAL A 419 10423 10431 4873 329 349 -59 N ATOM 4028 CA VAL A 419 44.467-110.396 191.613 1.00 67.20 C ANISOU 4028 CA VAL A 419 10441 10373 4719 312 487 -108 C ATOM 4029 C VAL A 419 44.602-111.095 192.960 1.00 70.96 C ANISOU 4029 C VAL A 419 10996 11014 4952 348 493 7 C ATOM 4030 O VAL A 419 44.164-110.572 193.991 1.00 73.13 O ANISOU 4030 O VAL A 419 11335 11401 5052 327 533 -78 O ATOM 4031 CB VAL A 419 43.280-110.945 190.800 1.00 66.61 C ANISOU 4031 CB VAL A 419 10357 10133 4818 314 634 -58 C ATOM 4032 CG1 VAL A 419 42.042-111.064 191.675 1.00 71.93 C ANISOU 4032 CG1 VAL A 419 11092 10870 5370 302 782 -57 C ATOM 4033 CG2 VAL A 419 42.998-110.046 189.604 1.00 59.11 C ANISOU 4033 CG2 VAL A 419 9337 9041 4082 277 636 -199 C ATOM 4034 N HIS A 420 45.217-112.280 192.978 1.00 71.63 N ANISOU 4034 N HIS A 420 11090 11115 5010 416 453 202 N ATOM 4035 CA HIS A 420 45.406-112.994 194.237 1.00 70.95 C ANISOU 4035 CA HIS A 420 11088 11182 4689 457 449 332 C ATOM 4036 C HIS A 420 46.280-112.195 195.196 1.00 72.69 C ANISOU 4036 C HIS A 420 11303 11611 4705 438 323 241 C ATOM 4037 O HIS A 420 45.965-112.072 196.385 1.00 73.91 O ANISOU 4037 O HIS A 420 11534 11902 4647 424 356 224 O ATOM 4038 CB HIS A 420 46.011-114.373 193.979 1.00 70.60 C ANISOU 4038 CB HIS A 420 11072 11094 4660 558 409 556 C ATOM 4039 CG HIS A 420 44.999-115.425 193.648 1.00 72.43 C ANISOU 4039 CG HIS A 420 11389 11158 4974 557 542 688 C ATOM 4040 ND1 HIS A 420 44.518-115.622 192.372 1.00 71.14 N ANISOU 4040 ND1 HIS A 420 11197 10788 5046 539 594 680 N ATOM 4041 CD2 HIS A 420 44.374-116.337 194.431 1.00 72.10 C ANISOU 4041 CD2 HIS A 420 11465 11128 4800 549 625 839 C ATOM 4042 CE1 HIS A 420 43.642-116.611 192.382 1.00 72.54 C ANISOU 4042 CE1 HIS A 420 11475 10854 5232 512 698 816 C ATOM 4043 NE2 HIS A 420 43.536-117.062 193.619 1.00 73.68 N ANISOU 4043 NE2 HIS A 420 11710 11127 5158 512 720 919 N ATOM 4044 N TYR A 421 47.384-111.636 194.692 1.00 70.14 N ANISOU 4044 N TYR A 421 10888 11329 4433 424 176 184 N ATOM 4045 CA TYR A 421 48.276-110.862 195.551 1.00 72.57 C ANISOU 4045 CA TYR A 421 11188 11841 4543 373 35 101 C ATOM 4046 C TYR A 421 47.563-109.652 196.140 1.00 76.97 C ANISOU 4046 C TYR A 421 11826 12405 5015 280 76 -115 C ATOM 4047 O TYR A 421 47.726-109.343 197.326 1.00 83.69 O ANISOU 4047 O TYR A 421 12750 13421 5627 257 35 -159 O ATOM 4048 CB TYR A 421 49.515-110.425 194.768 1.00 70.02 C ANISOU 4048 CB TYR A 421 10733 11565 4306 343 -127 82 C ATOM 4049 CG TYR A 421 50.524-109.657 195.593 1.00 75.28 C ANISOU 4049 CG TYR A 421 11379 12460 4766 258 -295 13 C ATOM 4050 CD1 TYR A 421 50.455-108.273 195.702 1.00 77.53 C ANISOU 4050 CD1 TYR A 421 11703 12732 5025 110 -351 -203 C ATOM 4051 CD2 TYR A 421 51.547-110.315 196.263 1.00 81.37 C ANISOU 4051 CD2 TYR A 421 12103 13456 5357 324 -406 165 C ATOM 4052 CE1 TYR A 421 51.372-107.568 196.456 1.00 82.12 C ANISOU 4052 CE1 TYR A 421 12284 13512 5406 4 -517 -269 C ATOM 4053 CE2 TYR A 421 52.471-109.618 197.020 1.00 86.20 C ANISOU 4053 CE2 TYR A 421 12685 14298 5768 227 -570 107 C ATOM 4054 CZ TYR A 421 52.379-108.245 197.112 1.00 86.93 C ANISOU 4054 CZ TYR A 421 12825 14368 5838 53 -627 -112 C ATOM 4055 OH TYR A 421 53.296-107.547 197.864 1.00 86.92 O ANISOU 4055 OH TYR A 421 12813 14587 5628 -72 -803 -172 O ATOM 4056 N ILE A 422 46.767-108.955 195.327 1.00 75.61 N ANISOU 4056 N ILE A 422 11652 12054 5024 240 155 -254 N ATOM 4057 CA ILE A 422 46.066-107.771 195.812 1.00 80.88 C ANISOU 4057 CA ILE A 422 12412 12707 5611 187 196 -469 C ATOM 4058 C ILE A 422 44.998-108.157 196.828 1.00 83.92 C ANISOU 4058 C ILE A 422 12887 13165 5834 243 351 -446 C ATOM 4059 O ILE A 422 44.859-107.515 197.876 1.00 87.73 O ANISOU 4059 O ILE A 422 13468 13764 6100 232 344 -564 O ATOM 4060 CB ILE A 422 45.471-106.983 194.630 1.00 82.28 C ANISOU 4060 CB ILE A 422 12562 12674 6026 156 243 -605 C ATOM 4061 CG1 ILE A 422 46.589-106.393 193.767 1.00 81.18 C ANISOU 4061 CG1 ILE A 422 12346 12495 6004 72 76 -646 C ATOM 4062 CG2 ILE A 422 44.543-105.885 195.128 1.00 83.54 C ANISOU 4062 CG2 ILE A 422 12839 12800 6101 153 317 -815 C ATOM 4063 CD1 ILE A 422 46.090-105.609 192.575 1.00 82.55 C ANISOU 4063 CD1 ILE A 422 12500 12461 6407 36 108 -768 C ATOM 4064 N VAL A 423 44.231-109.212 196.541 1.00 81.00 N ANISOU 4064 N VAL A 423 12491 12735 5552 296 488 -291 N ATOM 4065 CA VAL A 423 43.180-109.638 197.462 1.00 79.77 C ANISOU 4065 CA VAL A 423 12400 12670 5240 329 642 -243 C ATOM 4066 C VAL A 423 43.780-110.111 198.781 1.00 81.90 C ANISOU 4066 C VAL A 423 12737 13149 5234 346 583 -146 C ATOM 4067 O VAL A 423 43.291-109.760 199.862 1.00 83.73 O ANISOU 4067 O VAL A 423 13046 13521 5244 354 643 -216 O ATOM 4068 CB VAL A 423 42.306-110.725 196.810 1.00 76.96 C ANISOU 4068 CB VAL A 423 12002 12201 5038 343 782 -76 C ATOM 4069 CG1 VAL A 423 41.390-111.362 197.841 1.00 67.84 C ANISOU 4069 CG1 VAL A 423 10904 11180 3693 350 923 29 C ATOM 4070 CG2 VAL A 423 41.491-110.133 195.671 1.00 70.91 C ANISOU 4070 CG2 VAL A 423 11171 11266 4504 327 860 -193 C ATOM 4071 N PHE A 424 44.852-110.906 198.717 1.00 82.57 N ANISOU 4071 N PHE A 424 12792 13270 5312 366 464 17 N ATOM 4072 CA PHE A 424 45.490-111.385 199.940 1.00 81.27 C ANISOU 4072 CA PHE A 424 12684 13313 4883 393 394 125 C ATOM 4073 C PHE A 424 46.122-110.247 200.731 1.00 86.94 C ANISOU 4073 C PHE A 424 13440 14185 5407 343 270 -55 C ATOM 4074 O PHE A 424 46.152-110.296 201.967 1.00 92.13 O ANISOU 4074 O PHE A 424 14177 15028 5799 351 264 -42 O ATOM 4075 CB PHE A 424 46.539-112.446 199.609 1.00 79.63 C ANISOU 4075 CB PHE A 424 12431 13110 4717 456 286 337 C ATOM 4076 CG PHE A 424 45.962-113.717 199.054 1.00 85.28 C ANISOU 4076 CG PHE A 424 13166 13671 5563 508 395 534 C ATOM 4077 CD1 PHE A 424 44.719-114.167 199.468 1.00 88.34 C ANISOU 4077 CD1 PHE A 424 13628 14035 5902 482 563 593 C ATOM 4078 CD2 PHE A 424 46.660-114.460 198.115 1.00 82.24 C ANISOU 4078 CD2 PHE A 424 12735 13175 5339 577 326 663 C ATOM 4079 CE1 PHE A 424 44.184-115.336 198.958 1.00 86.28 C ANISOU 4079 CE1 PHE A 424 13406 13623 5753 495 650 779 C ATOM 4080 CE2 PHE A 424 46.130-115.629 197.602 1.00 80.17 C ANISOU 4080 CE2 PHE A 424 12531 12744 5186 618 415 835 C ATOM 4081 CZ PHE A 424 44.890-116.068 198.025 1.00 82.46 C ANISOU 4081 CZ PHE A 424 12907 12994 5430 561 571 895 C ATOM 4082 N MET A 425 46.628-109.220 200.046 1.00 85.89 N ANISOU 4082 N MET A 425 13265 13978 5391 278 164 -222 N ATOM 4083 CA MET A 425 47.210-108.084 200.751 1.00 90.00 C ANISOU 4083 CA MET A 425 13850 14619 5728 199 32 -404 C ATOM 4084 C MET A 425 46.139-107.219 201.403 1.00 95.52 C ANISOU 4084 C MET A 425 14681 15308 6303 201 146 -602 C ATOM 4085 O MET A 425 46.363-106.669 202.487 1.00 94.82 O ANISOU 4085 O MET A 425 14700 15370 5957 174 84 -705 O ATOM 4086 CB MET A 425 48.058-107.248 199.792 1.00 85.80 C ANISOU 4086 CB MET A 425 13246 13999 5354 104 -119 -510 C ATOM 4087 CG MET A 425 48.819-106.115 200.458 1.00 90.45 C ANISOU 4087 CG MET A 425 13911 14706 5752 -17 -291 -679 C ATOM 4088 SD MET A 425 49.644-105.048 199.263 1.00 93.54 S ANISOU 4088 SD MET A 425 14231 14973 6336 -168 -455 -803 S ATOM 4089 CE MET A 425 48.245-104.502 198.289 1.00 91.57 C ANISOU 4089 CE MET A 425 14037 14419 6335 -123 -274 -945 C ATOM 4090 N LEU A 426 44.973-107.090 200.767 1.00 97.89 N ANISOU 4090 N LEU A 426 14976 15448 6768 243 311 -658 N ATOM 4091 CA LEU A 426 43.886-106.293 201.320 1.00 99.92 C ANISOU 4091 CA LEU A 426 15344 15711 6910 284 436 -840 C ATOM 4092 C LEU A 426 43.115-107.018 202.415 1.00100.27 C ANISOU 4092 C LEU A 426 15427 15933 6739 355 583 -735 C ATOM 4093 O LEU A 426 42.247-106.405 203.045 1.00104.72 O ANISOU 4093 O LEU A 426 16077 16559 7153 410 693 -878 O ATOM 4094 CB LEU A 426 42.922-105.873 200.207 1.00101.63 C ANISOU 4094 CB LEU A 426 15518 15721 7377 316 555 -929 C ATOM 4095 CG LEU A 426 43.479-104.929 199.139 1.00100.59 C ANISOU 4095 CG LEU A 426 15375 15400 7445 246 429 -1067 C ATOM 4096 CD1 LEU A 426 42.424-104.630 198.083 1.00100.27 C ANISOU 4096 CD1 LEU A 426 15288 15172 7638 296 562 -1130 C ATOM 4097 CD2 LEU A 426 43.998-103.644 199.767 1.00 98.14 C ANISOU 4097 CD2 LEU A 426 15222 15113 6956 188 293 -1292 C ATOM 4098 N THR A 427 43.403-108.299 202.650 1.00101.50 N ANISOU 4098 N THR A 427 15528 16173 6863 362 590 -487 N ATOM 4099 CA THR A 427 42.754-109.050 203.715 1.00103.39 C ANISOU 4099 CA THR A 427 15811 16589 6884 406 717 -357 C ATOM 4100 C THR A 427 43.671-109.090 204.924 1.00106.19 C ANISOU 4100 C THR A 427 16244 17156 6949 395 587 -332 C ATOM 4101 O THR A 427 44.749-109.699 204.851 1.00107.27 O ANISOU 4101 O THR A 427 16340 17322 7096 376 445 -187 O ATOM 4102 CB THR A 427 42.421-110.466 203.260 1.00 98.92 C ANISOU 4102 CB THR A 427 15173 15965 6448 411 805 -88 C ATOM 4103 OG1 THR A 427 41.569-110.408 202.108 1.00 93.06 O ANISOU 4103 OG1 THR A 427 14354 15034 5970 406 916 -116 O ATOM 4104 CG2 THR A 427 41.709-111.226 204.373 1.00 97.46 C ANISOU 4104 CG2 THR A 427 15040 15964 6026 429 937 58 C ATOM 4105 N PRO A 428 43.295-108.483 206.039 1.00112.90 N ANISOU 4105 N PRO A 428 17200 18151 7547 411 626 -463 N ATOM 4106 CA PRO A 428 44.197-108.385 207.189 1.00119.41 C ANISOU 4106 CA PRO A 428 18101 19106 8164 366 482 -461 C ATOM 4107 C PRO A 428 44.242-109.684 207.987 1.00126.04 C ANISOU 4107 C PRO A 428 18931 20064 8895 380 519 -195 C ATOM 4108 O PRO A 428 43.524-110.646 207.717 1.00122.36 O ANISOU 4108 O PRO A 428 18417 19571 8503 409 660 -15 O ATOM 4109 CB PRO A 428 43.581-107.251 208.008 1.00122.60 C ANISOU 4109 CB PRO A 428 18634 19521 8427 369 534 -703 C ATOM 4110 CG PRO A 428 42.123-107.352 207.716 1.00120.57 C ANISOU 4110 CG PRO A 428 18337 19217 8256 440 768 -711 C ATOM 4111 CD PRO A 428 42.015-107.793 206.279 1.00115.16 C ANISOU 4111 CD PRO A 428 17531 18409 7816 455 799 -625 C ATOM 4112 N TYR A 429 45.115-109.687 208.995 1.00138.92 N ANISOU 4112 N TYR A 429 20620 21818 10344 350 381 -171 N ATOM 4113 CA TYR A 429 45.281-110.799 209.920 1.00151.24 C ANISOU 4113 CA TYR A 429 22199 23496 11771 365 389 62 C ATOM 4114 C TYR A 429 44.432-110.624 211.178 1.00163.75 C ANISOU 4114 C TYR A 429 23882 25179 13157 366 514 12 C ATOM 4115 O TYR A 429 44.761-111.182 212.232 1.00165.99 O ANISOU 4115 O TYR A 429 24216 25586 13266 362 476 138 O ATOM 4116 CB TYR A 429 46.759-110.952 210.297 1.00153.76 C ANISOU 4116 CB TYR A 429 22508 23911 12003 344 162 133 C ATOM 4117 CG TYR A 429 47.728-110.905 209.121 1.00155.57 C ANISOU 4117 CG TYR A 429 22625 24079 12406 339 17 149 C ATOM 4118 CD1 TYR A 429 48.080-109.696 208.528 1.00155.77 C ANISOU 4118 CD1 TYR A 429 22638 24053 12495 275 -80 -81 C ATOM 4119 CD2 TYR A 429 48.307-112.066 208.620 1.00155.76 C ANISOU 4119 CD2 TYR A 429 22565 24095 12523 401 -28 396 C ATOM 4120 CE1 TYR A 429 48.962-109.644 207.461 1.00153.33 C ANISOU 4120 CE1 TYR A 429 22210 23710 12337 256 -211 -59 C ATOM 4121 CE2 TYR A 429 49.196-112.024 207.552 1.00153.45 C ANISOU 4121 CE2 TYR A 429 22157 23765 12381 413 -154 414 C ATOM 4122 CZ TYR A 429 49.519-110.808 206.978 1.00152.92 C ANISOU 4122 CZ TYR A 429 22054 23675 12374 331 -243 189 C ATOM 4123 OH TYR A 429 50.398-110.749 205.919 1.00152.74 O ANISOU 4123 OH TYR A 429 21902 23638 12496 327 -368 212 O ATOM 4124 N THR A 430 43.342-109.862 211.077 1.00172.58 N ANISOU 4124 N THR A 430 25023 26252 14297 383 662 -167 N ATOM 4125 CA THR A 430 42.555-109.482 212.244 1.00186.72 C ANISOU 4125 CA THR A 430 26904 28148 15894 399 776 -256 C ATOM 4126 C THR A 430 41.798-110.657 212.850 1.00196.32 C ANISOU 4126 C THR A 430 28094 29459 17039 405 929 -17 C ATOM 4127 O THR A 430 41.478-110.626 214.043 1.00201.83 O ANISOU 4127 O THR A 430 28866 30290 17531 410 981 -22 O ATOM 4128 CB THR A 430 41.590-108.357 211.852 1.00187.39 C ANISOU 4128 CB THR A 430 27005 28151 16042 440 895 -506 C ATOM 4129 OG1 THR A 430 42.349-107.253 211.342 1.00186.33 O ANISOU 4129 OG1 THR A 430 26928 27909 15959 414 736 -725 O ATOM 4130 CG2 THR A 430 40.765-107.877 213.039 1.00189.88 C ANISOU 4130 CG2 THR A 430 27410 28582 16153 479 1017 -616 C ATOM 4131 N GLU A 431 41.529-111.706 212.074 1.00199.48 N ANISOU 4131 N GLU A 431 28407 29792 17596 395 994 198 N ATOM 4132 CA GLU A 431 40.611-112.737 212.544 1.00200.23 C ANISOU 4132 CA GLU A 431 28490 29953 17638 374 1156 412 C ATOM 4133 C GLU A 431 41.212-113.610 213.643 1.00201.29 C ANISOU 4133 C GLU A 431 28701 30196 17586 352 1081 609 C ATOM 4134 O GLU A 431 40.458-114.146 214.461 1.00203.56 O ANISOU 4134 O GLU A 431 29016 30582 17744 329 1206 727 O ATOM 4135 CB GLU A 431 40.142-113.581 211.356 1.00201.50 C ANISOU 4135 CB GLU A 431 28562 29983 18017 348 1236 581 C ATOM 4136 CG GLU A 431 39.049-114.603 211.664 1.00202.84 C ANISOU 4136 CG GLU A 431 28719 30196 18156 292 1411 800 C ATOM 4137 CD GLU A 431 37.929-114.060 212.532 1.00205.00 C ANISOU 4137 CD GLU A 431 28982 30620 18288 301 1576 693 C ATOM 4138 OE1 GLU A 431 37.492-114.798 213.440 1.00207.12 O ANISOU 4138 OE1 GLU A 431 29286 31000 18409 256 1653 863 O ATOM 4139 OE2 GLU A 431 37.480-112.916 212.303 1.00204.72 O ANISOU 4139 OE2 GLU A 431 28908 30589 18286 359 1629 447 O ATOM 4140 N VAL A 432 42.540-113.755 213.687 1.00188.31 N ANISOU 4140 N VAL A 432 27084 28546 15919 361 879 652 N ATOM 4141 CA VAL A 432 43.244-114.465 214.754 1.00180.16 C ANISOU 4141 CA VAL A 432 26125 27624 14703 357 782 818 C ATOM 4142 C VAL A 432 42.679-115.875 214.902 1.00174.78 C ANISOU 4142 C VAL A 432 25465 26924 14021 330 888 1114 C ATOM 4143 O VAL A 432 42.047-116.208 215.913 1.00174.97 O ANISOU 4143 O VAL A 432 25546 27057 13876 303 989 1191 O ATOM 4144 CB VAL A 432 43.170-113.693 216.085 1.00178.37 C ANISOU 4144 CB VAL A 432 25985 27559 14229 357 780 663 C ATOM 4145 CG1 VAL A 432 44.132-114.283 217.114 1.00178.70 C ANISOU 4145 CG1 VAL A 432 26097 27717 14086 357 639 810 C ATOM 4146 CG2 VAL A 432 43.486-112.223 215.866 1.00175.08 C ANISOU 4146 CG2 VAL A 432 25583 27119 13819 365 700 352 C ATOM 4147 N SER A 433 42.876-116.700 213.870 1.00167.38 N ANISOU 4147 N SER A 433 24492 25836 13269 332 865 1279 N ATOM 4148 CA SER A 433 42.540-118.127 213.895 1.00162.87 C ANISOU 4148 CA SER A 433 23980 25197 12707 295 924 1579 C ATOM 4149 C SER A 433 41.036-118.373 214.055 1.00164.33 C ANISOU 4149 C SER A 433 24164 25398 12877 214 1147 1629 C ATOM 4150 O SER A 433 40.616-119.293 214.759 1.00164.82 O ANISOU 4150 O SER A 433 24308 25493 12825 158 1210 1835 O ATOM 4151 CB SER A 433 43.333-118.853 214.980 1.00159.50 C ANISOU 4151 CB SER A 433 23653 24858 12093 316 809 1750 C ATOM 4152 OG SER A 433 42.938-120.209 215.072 1.00155.50 O ANISOU 4152 OG SER A 433 23237 24266 11579 270 866 2036 O ATOM 4153 N GLY A 434 40.218-117.552 213.394 1.00166.91 N ANISOU 4153 N GLY A 434 24394 25706 13320 207 1264 1446 N ATOM 4154 CA GLY A 434 38.790-117.777 213.327 1.00167.15 C ANISOU 4154 CA GLY A 434 24382 25755 13374 135 1473 1497 C ATOM 4155 C GLY A 434 38.424-118.553 212.077 1.00167.27 C ANISOU 4155 C GLY A 434 24367 25585 13605 76 1516 1650 C ATOM 4156 O GLY A 434 39.282-119.062 211.353 1.00166.60 O ANISOU 4156 O GLY A 434 24316 25351 13634 101 1388 1744 O ATOM 4157 N THR A 435 37.115-118.640 211.821 1.00169.79 N ANISOU 4157 N THR A 435 24615 25921 13977 0 1700 1677 N ATOM 4158 CA THR A 435 36.642-119.308 210.611 1.00168.95 C ANISOU 4158 CA THR A 435 24477 25642 14074 -77 1751 1809 C ATOM 4159 C THR A 435 37.102-118.568 209.360 1.00166.64 C ANISOU 4159 C THR A 435 24102 25233 13983 -4 1683 1631 C ATOM 4160 O THR A 435 37.480-119.191 208.361 1.00164.18 O ANISOU 4160 O THR A 435 23815 24740 13826 -18 1620 1748 O ATOM 4161 CB THR A 435 35.116-119.432 210.637 1.00167.64 C ANISOU 4161 CB THR A 435 24221 25557 13918 -179 1959 1858 C ATOM 4162 OG1 THR A 435 34.526-118.157 210.928 1.00168.27 O ANISOU 4162 OG1 THR A 435 24176 25803 13956 -104 2051 1597 O ATOM 4163 CG2 THR A 435 34.678-120.448 211.692 1.00169.09 C ANISOU 4163 CG2 THR A 435 24500 25816 13929 -275 2020 2099 C ATOM 4164 N LEU A 436 37.084-117.235 209.401 1.00167.08 N ANISOU 4164 N LEU A 436 24073 25377 14032 80 1690 1349 N ATOM 4165 CA LEU A 436 37.604-116.452 208.286 1.00163.24 C ANISOU 4165 CA LEU A 436 23524 24781 13721 153 1611 1168 C ATOM 4166 C LEU A 436 39.109-116.636 208.145 1.00154.62 C ANISOU 4166 C LEU A 436 22501 23612 12635 217 1401 1198 C ATOM 4167 O LEU A 436 39.634-116.708 207.028 1.00155.26 O ANISOU 4167 O LEU A 436 22556 23549 12888 253 1326 1201 O ATOM 4168 CB LEU A 436 37.271-114.973 208.481 1.00171.09 C ANISOU 4168 CB LEU A 436 24455 25868 14683 228 1653 858 C ATOM 4169 CG LEU A 436 35.812-114.568 208.693 1.00175.84 C ANISOU 4169 CG LEU A 436 24968 26579 15266 214 1856 787 C ATOM 4170 CD1 LEU A 436 35.721-113.117 209.152 1.00177.26 C ANISOU 4170 CD1 LEU A 436 25145 26840 15365 321 1862 482 C ATOM 4171 CD2 LEU A 436 34.998-114.779 207.427 1.00175.07 C ANISOU 4171 CD2 LEU A 436 24756 26380 15383 167 1957 831 C ATOM 4172 N TRP A 437 39.819-116.706 209.272 1.00144.30 N ANISOU 4172 N TRP A 437 21273 22413 11140 240 1305 1222 N ATOM 4173 CA TRP A 437 41.274-116.807 209.236 1.00135.80 C ANISOU 4173 CA TRP A 437 20236 21306 10056 307 1098 1244 C ATOM 4174 C TRP A 437 41.719-118.147 208.665 1.00132.69 C ANISOU 4174 C TRP A 437 19897 20764 9754 313 1040 1517 C ATOM 4175 O TRP A 437 42.623-118.206 207.823 1.00128.09 O ANISOU 4175 O TRP A 437 19292 20078 9298 388 915 1522 O ATOM 4176 CB TRP A 437 41.838-116.611 210.642 1.00132.28 C ANISOU 4176 CB TRP A 437 19860 21026 9374 321 1017 1220 C ATOM 4177 CG TRP A 437 43.328-116.510 210.724 1.00124.41 C ANISOU 4177 CG TRP A 437 18875 20048 8348 385 799 1210 C ATOM 4178 CD1 TRP A 437 44.072-115.367 210.719 1.00120.69 C ANISOU 4178 CD1 TRP A 437 18367 19631 7857 411 676 982 C ATOM 4179 CD2 TRP A 437 44.256-117.593 210.853 1.00120.26 C ANISOU 4179 CD2 TRP A 437 18399 19494 7801 426 673 1443 C ATOM 4180 NE1 TRP A 437 45.407-115.671 210.829 1.00118.61 N ANISOU 4180 NE1 TRP A 437 18103 19401 7563 454 482 1065 N ATOM 4181 CE2 TRP A 437 45.546-117.031 210.914 1.00118.42 C ANISOU 4181 CE2 TRP A 437 18126 19329 7538 483 480 1345 C ATOM 4182 CE3 TRP A 437 44.121-118.983 210.917 1.00118.28 C ANISOU 4182 CE3 TRP A 437 18231 19159 7550 420 699 1728 C ATOM 4183 CZ2 TRP A 437 46.693-117.809 211.034 1.00116.90 C ANISOU 4183 CZ2 TRP A 437 17947 19147 7323 555 322 1521 C ATOM 4184 CZ3 TRP A 437 45.259-119.752 211.040 1.00117.63 C ANISOU 4184 CZ3 TRP A 437 18192 19058 7444 501 538 1895 C ATOM 4185 CH2 TRP A 437 46.529-119.164 211.096 1.00116.59 C ANISOU 4185 CH2 TRP A 437 17992 19018 7289 579 356 1791 C ATOM 4186 N GLN A 438 41.090-119.237 209.110 1.00131.66 N ANISOU 4186 N GLN A 438 19852 20613 9560 236 1127 1747 N ATOM 4187 CA GLN A 438 41.521-120.562 208.680 1.00133.60 C ANISOU 4187 CA GLN A 438 20198 20692 9874 244 1060 2013 C ATOM 4188 C GLN A 438 41.211-120.814 207.208 1.00128.06 C ANISOU 4188 C GLN A 438 19467 19784 9407 243 1100 2043 C ATOM 4189 O GLN A 438 41.939-121.561 206.546 1.00126.04 O ANISOU 4189 O GLN A 438 19278 19356 9254 320 998 2178 O ATOM 4190 CB GLN A 438 40.873-121.634 209.558 1.00138.44 C ANISOU 4190 CB GLN A 438 20937 21316 10347 136 1138 2249 C ATOM 4191 CG GLN A 438 39.357-121.700 209.464 1.00139.71 C ANISOU 4191 CG GLN A 438 21071 21485 10529 -8 1344 2271 C ATOM 4192 CD GLN A 438 38.774-122.816 210.309 1.00144.48 C ANISOU 4192 CD GLN A 438 21817 22086 10993 -124 1412 2521 C ATOM 4193 OE1 GLN A 438 39.497-123.512 211.022 1.00148.41 O ANISOU 4193 OE1 GLN A 438 22446 22577 11367 -96 1303 2672 O ATOM 4194 NE2 GLN A 438 37.460-122.992 210.233 1.00144.25 N ANISOU 4194 NE2 GLN A 438 21758 22068 10984 -250 1589 2572 N ATOM 4195 N VAL A 439 40.149-120.207 206.675 1.00124.17 N ANISOU 4195 N VAL A 439 18877 19299 9003 172 1247 1917 N ATOM 4196 CA VAL A 439 39.841-120.410 205.263 1.00121.04 C ANISOU 4196 CA VAL A 439 18455 18701 8835 167 1285 1938 C ATOM 4197 C VAL A 439 40.727-119.533 204.382 1.00117.83 C ANISOU 4197 C VAL A 439 17949 18190 8630 271 1161 1717 C ATOM 4198 O VAL A 439 41.089-119.932 203.270 1.00115.20 O ANISOU 4198 O VAL A 439 17620 17618 8533 297 1099 1750 O ATOM 4199 CB VAL A 439 38.343-120.173 204.991 1.00117.40 C ANISOU 4199 CB VAL A 439 17901 18273 8432 27 1478 1897 C ATOM 4200 CG1 VAL A 439 37.967-118.713 205.202 1.00118.62 C ANISOU 4200 CG1 VAL A 439 17911 18612 8546 70 1543 1608 C ATOM 4201 CG2 VAL A 439 37.976-120.634 203.586 1.00111.48 C ANISOU 4201 CG2 VAL A 439 17135 17236 7987 -41 1492 1937 C ATOM 4202 N ARG A 440 41.109-118.345 204.859 1.00113.09 N ANISOU 4202 N ARG A 440 17273 17766 7929 326 1118 1494 N ATOM 4203 CA ARG A 440 42.050-117.523 204.104 1.00111.42 C ANISOU 4203 CA ARG A 440 16980 17473 7883 400 981 1305 C ATOM 4204 C ARG A 440 43.449-118.123 204.148 1.00108.44 C ANISOU 4204 C ARG A 440 16652 17077 7474 503 799 1432 C ATOM 4205 O ARG A 440 44.152-118.151 203.132 1.00111.30 O ANISOU 4205 O ARG A 440 16964 17281 8042 559 702 1409 O ATOM 4206 CB ARG A 440 42.056-116.092 204.649 1.00114.01 C ANISOU 4206 CB ARG A 440 17247 17979 8091 409 974 1036 C ATOM 4207 CG ARG A 440 42.430-115.010 203.630 1.00116.38 C ANISOU 4207 CG ARG A 440 17449 18155 8613 422 901 801 C ATOM 4208 CD ARG A 440 43.924-114.976 203.331 1.00117.89 C ANISOU 4208 CD ARG A 440 17620 18325 8849 480 695 804 C ATOM 4209 NE ARG A 440 44.705-114.447 204.445 1.00120.14 N ANISOU 4209 NE ARG A 440 17938 18840 8871 499 581 737 N ATOM 4210 CZ ARG A 440 45.285-113.251 204.447 1.00120.94 C ANISOU 4210 CZ ARG A 440 18002 18998 8953 478 472 515 C ATOM 4211 NH1 ARG A 440 45.178-112.459 203.388 1.00119.07 N ANISOU 4211 NH1 ARG A 440 17694 18599 8947 445 467 347 N ATOM 4212 NH2 ARG A 440 45.978-112.848 205.503 1.00121.47 N ANISOU 4212 NH2 ARG A 440 18112 19280 8761 477 362 467 N ATOM 4213 N MET A 441 43.865-118.614 205.316 1.00104.79 N ANISOU 4213 N MET A 441 16280 16791 6744 540 753 1571 N ATOM 4214 CA MET A 441 45.202-119.181 205.447 1.00101.68 C ANISOU 4214 CA MET A 441 15920 16411 6305 656 577 1698 C ATOM 4215 C MET A 441 45.328-120.484 204.666 1.00 93.54 C ANISOU 4215 C MET A 441 14984 15143 5414 721 567 1928 C ATOM 4216 O MET A 441 46.387-120.772 204.098 1.00 90.64 O ANISOU 4216 O MET A 441 14597 14708 5135 848 432 1973 O ATOM 4217 CB MET A 441 45.531-119.397 206.925 1.00105.97 C ANISOU 4217 CB MET A 441 16518 17128 6619 636 522 1765 C ATOM 4218 CG MET A 441 46.990-119.168 207.285 1.00106.98 C ANISOU 4218 CG MET A 441 16595 17379 6674 728 319 1742 C ATOM 4219 SD MET A 441 47.583-117.519 206.855 1.00109.67 S ANISOU 4219 SD MET A 441 16785 17831 7055 710 223 1429 S ATOM 4220 CE MET A 441 46.353-116.485 207.645 1.00113.31 C ANISOU 4220 CE MET A 441 17273 18382 7398 581 375 1214 C ATOM 4221 N HIS A 442 44.258-121.281 204.616 1.00 91.93 N ANISOU 4221 N HIS A 442 14886 14811 5235 629 704 2074 N ATOM 4222 CA HIS A 442 44.308-122.529 203.860 1.00 91.91 C ANISOU 4222 CA HIS A 442 15013 14538 5371 669 690 2281 C ATOM 4223 C HIS A 442 44.399-122.269 202.362 1.00 95.50 C ANISOU 4223 C HIS A 442 15378 14766 6140 688 673 2159 C ATOM 4224 O HIS A 442 45.175-122.927 201.658 1.00 98.89 O ANISOU 4224 O HIS A 442 15862 15032 6678 818 575 2251 O ATOM 4225 CB HIS A 442 43.084-123.391 204.174 1.00 91.45 C ANISOU 4225 CB HIS A 442 15094 14399 5255 517 835 2464 C ATOM 4226 CG HIS A 442 43.192-124.152 205.458 1.00 96.43 C ANISOU 4226 CG HIS A 442 15824 15127 5690 477 801 2643 C ATOM 4227 ND1 HIS A 442 43.216-123.536 206.691 1.00100.95 N ANISOU 4227 ND1 HIS A 442 16331 15965 6060 437 803 2560 N ATOM 4228 CD2 HIS A 442 43.282-125.481 205.701 1.00100.19 C ANISOU 4228 CD2 HIS A 442 16476 15453 6139 469 758 2897 C ATOM 4229 CE1 HIS A 442 43.316-124.452 207.637 1.00102.81 C ANISOU 4229 CE1 HIS A 442 16694 16222 6148 405 769 2761 C ATOM 4230 NE2 HIS A 442 43.358-125.641 207.063 1.00102.90 N ANISOU 4230 NE2 HIS A 442 16848 15988 6262 423 738 2972 N ATOM 4231 N TYR A 443 43.618-121.312 201.854 1.00 96.36 N ANISOU 4231 N TYR A 443 15352 14871 6389 576 768 1953 N ATOM 4232 CA TYR A 443 43.590-121.079 200.414 1.00 97.10 C ANISOU 4232 CA TYR A 443 15366 14750 6779 578 763 1846 C ATOM 4233 C TYR A 443 44.856-120.379 199.936 1.00 93.07 C ANISOU 4233 C TYR A 443 14732 14285 6344 706 613 1708 C ATOM 4234 O TYR A 443 45.393-120.715 198.874 1.00 91.96 O ANISOU 4234 O TYR A 443 14580 13972 6387 790 549 1729 O ATOM 4235 CB TYR A 443 42.352-120.268 200.035 1.00100.28 C ANISOU 4235 CB TYR A 443 15661 15147 7295 431 908 1679 C ATOM 4236 CG TYR A 443 42.263-119.965 198.557 1.00100.83 C ANISOU 4236 CG TYR A 443 15643 15007 7663 425 906 1565 C ATOM 4237 CD1 TYR A 443 41.964-120.965 197.641 1.00101.21 C ANISOU 4237 CD1 TYR A 443 15783 14801 7871 401 925 1701 C ATOM 4238 CD2 TYR A 443 42.479-118.680 198.077 1.00100.91 C ANISOU 4238 CD2 TYR A 443 15496 15064 7783 437 877 1322 C ATOM 4239 CE1 TYR A 443 41.884-120.695 196.288 1.00100.84 C ANISOU 4239 CE1 TYR A 443 15658 14572 8084 397 922 1596 C ATOM 4240 CE2 TYR A 443 42.400-118.400 196.725 1.00101.83 C ANISOU 4240 CE2 TYR A 443 15533 14995 8163 430 874 1226 C ATOM 4241 CZ TYR A 443 42.102-119.411 195.836 1.00101.03 C ANISOU 4241 CZ TYR A 443 15510 14664 8215 414 899 1363 C ATOM 4242 OH TYR A 443 42.022-119.138 194.490 1.00101.51 O ANISOU 4242 OH TYR A 443 15494 14551 8527 408 894 1267 O ATOM 4243 N GLU A 444 45.347-119.402 200.702 1.00 89.63 N ANISOU 4243 N GLU A 444 14207 14090 5758 714 553 1569 N ATOM 4244 CA GLU A 444 46.552-118.691 200.288 1.00 88.16 C ANISOU 4244 CA GLU A 444 13895 13975 5627 796 402 1447 C ATOM 4245 C GLU A 444 47.782-119.588 200.351 1.00 87.37 C ANISOU 4245 C GLU A 444 13836 13905 5456 966 262 1632 C ATOM 4246 O GLU A 444 48.695-119.442 199.530 1.00 85.37 O ANISOU 4246 O GLU A 444 13481 13628 5326 1057 156 1598 O ATOM 4247 CB GLU A 444 46.753-117.443 201.147 1.00 89.54 C ANISOU 4247 CB GLU A 444 13994 14391 5636 736 360 1256 C ATOM 4248 CG GLU A 444 47.819-116.498 200.617 1.00 90.59 C ANISOU 4248 CG GLU A 444 13985 14589 5846 754 212 1099 C ATOM 4249 CD GLU A 444 47.936-115.225 201.435 1.00 92.45 C ANISOU 4249 CD GLU A 444 14186 15025 5917 668 166 896 C ATOM 4250 OE1 GLU A 444 47.074-114.994 202.308 1.00 95.28 O ANISOU 4250 OE1 GLU A 444 14621 15458 6124 611 271 849 O ATOM 4251 OE2 GLU A 444 48.893-114.456 201.204 1.00 95.35 O ANISOU 4251 OE2 GLU A 444 14454 15479 6294 652 23 785 O ATOM 4252 N MET A 445 47.825-120.521 201.306 1.00 86.76 N ANISOU 4252 N MET A 445 13901 13891 5172 1021 259 1835 N ATOM 4253 CA MET A 445 48.927-121.478 201.343 1.00 88.07 C ANISOU 4253 CA MET A 445 14129 14067 5267 1217 133 2031 C ATOM 4254 C MET A 445 48.857-122.440 200.165 1.00 83.93 C ANISOU 4254 C MET A 445 13695 13242 4953 1308 154 2143 C ATOM 4255 O MET A 445 49.891-122.810 199.597 1.00 82.50 O ANISOU 4255 O MET A 445 13483 13045 4820 1492 42 2203 O ATOM 4256 CB MET A 445 48.922-122.250 202.663 1.00 95.61 C ANISOU 4256 CB MET A 445 15240 15144 5945 1254 128 2229 C ATOM 4257 CG MET A 445 49.405-121.454 203.865 1.00106.96 C ANISOU 4257 CG MET A 445 16574 16879 7189 1198 51 2129 C ATOM 4258 SD MET A 445 51.043-120.741 203.634 1.00115.16 S ANISOU 4258 SD MET A 445 17403 18125 8228 1309 -158 2028 S ATOM 4259 CE MET A 445 51.979-122.183 203.155 1.00114.77 C ANISOU 4259 CE MET A 445 17412 17940 8255 1551 -252 2275 C ATOM 4260 N LEU A 446 47.648-122.859 199.786 1.00 83.06 N ANISOU 4260 N LEU A 446 13697 12905 4956 1182 293 2173 N ATOM 4261 CA LEU A 446 47.497-123.727 198.622 1.00 87.74 C ANISOU 4261 CA LEU A 446 14397 13192 5749 1241 311 2259 C ATOM 4262 C LEU A 446 47.906-123.010 197.343 1.00 86.69 C ANISOU 4262 C LEU A 446 14086 12999 5852 1275 274 2081 C ATOM 4263 O LEU A 446 48.572-123.595 196.481 1.00 83.42 O ANISOU 4263 O LEU A 446 13704 12450 5542 1439 207 2143 O ATOM 4264 CB LEU A 446 46.054-124.220 198.517 1.00 89.91 C ANISOU 4264 CB LEU A 446 14811 13268 6084 1050 462 2320 C ATOM 4265 CG LEU A 446 45.687-125.484 199.292 1.00 99.96 C ANISOU 4265 CG LEU A 446 16342 14453 7185 1038 489 2580 C ATOM 4266 CD1 LEU A 446 44.185-125.709 199.258 1.00103.04 C ANISOU 4266 CD1 LEU A 446 16807 14725 7619 789 644 2614 C ATOM 4267 CD2 LEU A 446 46.420-126.684 198.716 1.00102.33 C ANISOU 4267 CD2 LEU A 446 16838 14519 7523 1240 395 2756 C ATOM 4268 N PHE A 447 47.521-121.741 197.204 1.00 85.34 N ANISOU 4268 N PHE A 447 13739 12929 5758 1132 315 1860 N ATOM 4269 CA PHE A 447 47.811-121.007 195.977 1.00 83.01 C ANISOU 4269 CA PHE A 447 13283 12570 5689 1136 287 1693 C ATOM 4270 C PHE A 447 49.297-120.693 195.859 1.00 86.18 C ANISOU 4270 C PHE A 447 13548 13151 6048 1294 128 1674 C ATOM 4271 O PHE A 447 49.913-120.943 194.816 1.00 88.77 O ANISOU 4271 O PHE A 447 13827 13388 6516 1415 75 1686 O ATOM 4272 CB PHE A 447 46.980-119.724 195.929 1.00 81.10 C ANISOU 4272 CB PHE A 447 12914 12378 5520 949 370 1470 C ATOM 4273 CG PHE A 447 47.160-118.931 194.665 1.00 73.94 C ANISOU 4273 CG PHE A 447 11858 11390 4847 931 348 1303 C ATOM 4274 CD1 PHE A 447 46.440-119.250 193.526 1.00 75.15 C ANISOU 4274 CD1 PHE A 447 12037 11297 5218 891 428 1296 C ATOM 4275 CD2 PHE A 447 48.042-117.865 194.619 1.00 71.94 C ANISOU 4275 CD2 PHE A 447 11443 11308 4584 937 241 1159 C ATOM 4276 CE1 PHE A 447 46.601-118.522 192.361 1.00 75.68 C ANISOU 4276 CE1 PHE A 447 11970 11295 5491 876 408 1150 C ATOM 4277 CE2 PHE A 447 48.208-117.134 193.458 1.00 75.21 C ANISOU 4277 CE2 PHE A 447 11727 11647 5204 906 219 1019 C ATOM 4278 CZ PHE A 447 47.486-117.463 192.328 1.00 75.73 C ANISOU 4278 CZ PHE A 447 11817 11470 5487 884 306 1015 C ATOM 4279 N ASN A 448 49.894-120.151 196.924 1.00 83.64 N ANISOU 4279 N ASN A 448 13156 13104 5519 1291 49 1649 N ATOM 4280 CA ASN A 448 51.287-119.722 196.854 1.00 83.66 C ANISOU 4280 CA ASN A 448 12994 13327 5466 1400 -110 1624 C ATOM 4281 C ASN A 448 52.245-120.899 196.715 1.00 86.81 C ANISOU 4281 C ASN A 448 13449 13731 5803 1655 -197 1837 C ATOM 4282 O ASN A 448 53.295-120.767 196.076 1.00 87.36 O ANISOU 4282 O ASN A 448 13370 13905 5918 1781 -301 1832 O ATOM 4283 CB ASN A 448 51.644-118.895 198.089 1.00 85.38 C ANISOU 4283 CB ASN A 448 13144 13840 5456 1315 -181 1550 C ATOM 4284 CG ASN A 448 50.837-117.616 198.186 1.00 85.99 C ANISOU 4284 CG ASN A 448 13171 13919 5582 1099 -113 1317 C ATOM 4285 OD1 ASN A 448 49.823-117.456 197.507 1.00 82.84 O ANISOU 4285 OD1 ASN A 448 12802 13309 5365 1012 11 1235 O ATOM 4286 ND2 ASN A 448 51.283-116.698 199.035 1.00 86.01 N ANISOU 4286 ND2 ASN A 448 13107 14163 5412 1018 -198 1208 N ATOM 4287 N SER A 449 51.908-122.052 197.298 1.00 88.54 N ANISOU 4287 N SER A 449 13886 13845 5910 1740 -157 2030 N ATOM 4288 CA SER A 449 52.822-123.189 197.248 1.00 92.62 C ANISOU 4288 CA SER A 449 14490 14357 6343 2014 -244 2237 C ATOM 4289 C SER A 449 52.835-123.832 195.866 1.00 83.24 C ANISOU 4289 C SER A 449 13361 12897 5368 2142 -219 2265 C ATOM 4290 O SER A 449 53.883-124.297 195.403 1.00 80.48 O ANISOU 4290 O SER A 449 12968 12605 5005 2391 -313 2349 O ATOM 4291 CB SER A 449 52.450-124.215 198.318 1.00102.33 C ANISOU 4291 CB SER A 449 15968 15537 7377 2058 -216 2442 C ATOM 4292 OG SER A 449 51.123-124.680 198.146 1.00108.78 O ANISOU 4292 OG SER A 449 16977 16065 8289 1906 -73 2467 O ATOM 4293 N PHE A 450 51.687-123.867 195.191 1.00 83.56 N ANISOU 4293 N PHE A 450 13495 12658 5596 1986 -94 2197 N ATOM 4294 CA PHE A 450 51.583-124.464 193.866 1.00 87.54 C ANISOU 4294 CA PHE A 450 14077 12886 6300 2081 -66 2210 C ATOM 4295 C PHE A 450 51.799-123.456 192.741 1.00 82.78 C ANISOU 4295 C PHE A 450 13236 12319 5899 2024 -73 2013 C ATOM 4296 O PHE A 450 51.446-123.743 191.592 1.00 83.71 O ANISOU 4296 O PHE A 450 13404 12198 6204 2037 -24 1982 O ATOM 4297 CB PHE A 450 50.225-125.149 193.697 1.00 87.60 C ANISOU 4297 CB PHE A 450 14326 12568 6391 1930 61 2263 C ATOM 4298 CG PHE A 450 50.100-126.446 194.445 1.00 89.25 C ANISOU 4298 CG PHE A 450 14827 12650 6433 2023 57 2497 C ATOM 4299 CD1 PHE A 450 50.675-127.605 193.948 1.00 90.10 C ANISOU 4299 CD1 PHE A 450 15134 12567 6533 2277 -1 2648 C ATOM 4300 CD2 PHE A 450 49.400-126.509 195.638 1.00 89.65 C ANISOU 4300 CD2 PHE A 450 14970 12769 6325 1861 113 2567 C ATOM 4301 CE1 PHE A 450 50.559-128.801 194.634 1.00 95.23 C ANISOU 4301 CE1 PHE A 450 16058 13066 7060 2341 -15 2851 C ATOM 4302 CE2 PHE A 450 49.280-127.701 196.327 1.00 91.57 C ANISOU 4302 CE2 PHE A 450 15495 12890 6408 1929 105 2797 C ATOM 4303 CZ PHE A 450 49.860-128.849 195.824 1.00 94.01 C ANISOU 4303 CZ PHE A 450 15972 12975 6771 2145 35 2921 C ATOM 4304 N GLN A 451 52.369-122.286 193.043 1.00 78.82 N ANISOU 4304 N GLN A 451 12491 12104 5353 1949 -138 1884 N ATOM 4305 CA GLN A 451 52.611-121.297 191.997 1.00 74.33 C ANISOU 4305 CA GLN A 451 11706 11573 4964 1879 -154 1709 C ATOM 4306 C GLN A 451 53.628-121.801 190.981 1.00 69.02 C ANISOU 4306 C GLN A 451 10966 10905 4354 2123 -226 1774 C ATOM 4307 O GLN A 451 53.437-121.636 189.770 1.00 67.29 O ANISOU 4307 O GLN A 451 10699 10536 4332 2109 -188 1691 O ATOM 4308 CB GLN A 451 53.072-119.976 192.614 1.00 73.85 C ANISOU 4308 CB GLN A 451 11433 11812 4814 1736 -227 1572 C ATOM 4309 CG GLN A 451 51.941-119.136 193.182 1.00 73.09 C ANISOU 4309 CG GLN A 451 11368 11675 4726 1480 -136 1429 C ATOM 4310 CD GLN A 451 52.422-117.822 193.762 1.00 79.03 C ANISOU 4310 CD GLN A 451 11954 12691 5382 1344 -221 1281 C ATOM 4311 OE1 GLN A 451 53.610-117.649 194.035 1.00 79.04 O ANISOU 4311 OE1 GLN A 451 11826 12945 5260 1420 -357 1318 O ATOM 4312 NE2 GLN A 451 51.500-116.886 193.951 1.00 84.47 N ANISOU 4312 NE2 GLN A 451 12651 13328 6117 1142 -146 1112 N ATOM 4313 N GLY A 452 54.713-122.419 191.451 1.00 71.21 N ANISOU 4313 N GLY A 452 11232 11368 4454 2363 -328 1924 N ATOM 4314 CA GLY A 452 55.671-123.004 190.527 1.00 80.99 C ANISOU 4314 CA GLY A 452 12418 12629 5727 2642 -387 2000 C ATOM 4315 C GLY A 452 55.068-124.123 189.700 1.00 87.97 C ANISOU 4315 C GLY A 452 13561 13132 6730 2766 -306 2070 C ATOM 4316 O GLY A 452 55.401-124.289 188.523 1.00 89.21 O ANISOU 4316 O GLY A 452 13674 13210 7012 2899 -306 2042 O ATOM 4317 N PHE A 453 54.167-124.902 190.303 1.00 87.08 N ANISOU 4317 N PHE A 453 13732 12781 6572 2713 -238 2162 N ATOM 4318 CA PHE A 453 53.476-125.949 189.559 1.00 84.08 C ANISOU 4318 CA PHE A 453 13634 12013 6302 2774 -167 2225 C ATOM 4319 C PHE A 453 52.512-125.362 188.534 1.00 75.79 C ANISOU 4319 C PHE A 453 12537 10766 5492 2541 -72 2058 C ATOM 4320 O PHE A 453 52.305-125.957 187.470 1.00 70.90 O ANISOU 4320 O PHE A 453 12046 9893 5000 2624 -42 2060 O ATOM 4321 CB PHE A 453 52.737-126.874 190.526 1.00 88.81 C ANISOU 4321 CB PHE A 453 14541 12428 6776 2726 -127 2378 C ATOM 4322 CG PHE A 453 52.038-128.022 189.857 1.00 91.29 C ANISOU 4322 CG PHE A 453 15183 12328 7174 2763 -71 2462 C ATOM 4323 CD1 PHE A 453 52.763-129.075 189.326 1.00 92.45 C ANISOU 4323 CD1 PHE A 453 15513 12333 7281 3093 -131 2580 C ATOM 4324 CD2 PHE A 453 50.656-128.054 189.771 1.00 92.92 C ANISOU 4324 CD2 PHE A 453 15524 12297 7486 2470 36 2427 C ATOM 4325 CE1 PHE A 453 52.124-130.136 188.712 1.00 95.74 C ANISOU 4325 CE1 PHE A 453 16250 12342 7786 3100 -91 2636 C ATOM 4326 CE2 PHE A 453 50.011-129.113 189.160 1.00 95.54 C ANISOU 4326 CE2 PHE A 453 16167 12249 7884 2468 74 2508 C ATOM 4327 CZ PHE A 453 50.746-130.155 188.630 1.00 96.02 C ANISOU 4327 CZ PHE A 453 16440 12138 7906 2785 5 2616 C ATOM 4328 N PHE A 454 51.916-124.206 188.834 1.00 73.73 N ANISOU 4328 N PHE A 454 12107 10619 5287 2263 -27 1911 N ATOM 4329 CA PHE A 454 51.066-123.535 187.856 1.00 74.99 C ANISOU 4329 CA PHE A 454 12193 10630 5670 2061 54 1749 C ATOM 4330 C PHE A 454 51.881-123.043 186.667 1.00 77.55 C ANISOU 4330 C PHE A 454 12314 11034 6116 2169 4 1657 C ATOM 4331 O PHE A 454 51.465-123.199 185.513 1.00 78.49 O ANISOU 4331 O PHE A 454 12474 10941 6407 2157 52 1603 O ATOM 4332 CB PHE A 454 50.328-122.365 188.509 1.00 77.24 C ANISOU 4332 CB PHE A 454 12348 11039 5961 1781 106 1613 C ATOM 4333 CG PHE A 454 49.336-122.776 189.559 1.00 80.48 C ANISOU 4333 CG PHE A 454 12938 11375 6266 1645 182 1689 C ATOM 4334 CD1 PHE A 454 48.704-124.007 189.494 1.00 82.59 C ANISOU 4334 CD1 PHE A 454 13475 11376 6529 1665 234 1834 C ATOM 4335 CD2 PHE A 454 49.034-121.927 190.610 1.00 78.21 C ANISOU 4335 CD2 PHE A 454 12558 11286 5871 1488 200 1618 C ATOM 4336 CE1 PHE A 454 47.789-124.382 190.460 1.00 79.71 C ANISOU 4336 CE1 PHE A 454 13263 10968 6056 1516 304 1920 C ATOM 4337 CE2 PHE A 454 48.121-122.296 191.579 1.00 76.44 C ANISOU 4337 CE2 PHE A 454 12484 11027 5534 1367 279 1693 C ATOM 4338 CZ PHE A 454 47.497-123.526 191.503 1.00 77.32 C ANISOU 4338 CZ PHE A 454 12841 10894 5643 1374 332 1852 C ATOM 4339 N VAL A 455 53.045-122.447 186.932 1.00 79.83 N ANISOU 4339 N VAL A 455 12377 11645 6309 2263 -96 1644 N ATOM 4340 CA VAL A 455 53.878-121.918 185.857 1.00 76.14 C ANISOU 4340 CA VAL A 455 11687 11305 5936 2346 -148 1569 C ATOM 4341 C VAL A 455 54.464-123.053 185.024 1.00 79.38 C ANISOU 4341 C VAL A 455 12208 11602 6350 2658 -166 1680 C ATOM 4342 O VAL A 455 54.594-122.939 183.799 1.00 79.16 O ANISOU 4342 O VAL A 455 12108 11508 6463 2707 -151 1614 O ATOM 4343 CB VAL A 455 54.975-121.010 186.442 1.00 73.49 C ANISOU 4343 CB VAL A 455 11080 11372 5472 2336 -260 1545 C ATOM 4344 CG1 VAL A 455 55.915-120.532 185.353 1.00 77.82 C ANISOU 4344 CG1 VAL A 455 11385 12089 6094 2420 -318 1498 C ATOM 4345 CG2 VAL A 455 54.349-119.825 187.160 1.00 68.77 C ANISOU 4345 CG2 VAL A 455 10407 10848 4877 2027 -242 1408 C ATOM 4346 N ALA A 456 54.819-124.166 185.671 1.00 82.84 N ANISOU 4346 N ALA A 456 12839 12010 6626 2886 -198 1850 N ATOM 4347 CA ALA A 456 55.377-125.300 184.940 1.00 82.10 C ANISOU 4347 CA ALA A 456 12896 11787 6513 3221 -218 1956 C ATOM 4348 C ALA A 456 54.359-125.892 183.974 1.00 77.69 C ANISOU 4348 C ALA A 456 12583 10812 6122 3163 -128 1917 C ATOM 4349 O ALA A 456 54.713-126.308 182.865 1.00 82.02 O ANISOU 4349 O ALA A 456 13163 11262 6738 3356 -129 1907 O ATOM 4350 CB ALA A 456 55.869-126.367 185.918 1.00 88.37 C ANISOU 4350 CB ALA A 456 13886 12602 7087 3472 -274 2150 C ATOM 4351 N ILE A 457 53.089-125.939 184.379 1.00 73.92 N ANISOU 4351 N ILE A 457 12278 10106 5703 2896 -50 1898 N ATOM 4352 CA ILE A 457 52.050-126.465 183.500 1.00 79.14 C ANISOU 4352 CA ILE A 457 13161 10391 6518 2794 29 1865 C ATOM 4353 C ILE A 457 51.767-125.491 182.362 1.00 78.51 C ANISOU 4353 C ILE A 457 12864 10325 6642 2639 68 1687 C ATOM 4354 O ILE A 457 51.590-125.898 181.208 1.00 76.92 O ANISOU 4354 O ILE A 457 12758 9914 6555 2704 92 1653 O ATOM 4355 CB ILE A 457 50.779-126.780 184.311 1.00 83.78 C ANISOU 4355 CB ILE A 457 13962 10781 7088 2536 99 1914 C ATOM 4356 CG1 ILE A 457 50.909-128.137 185.003 1.00 90.70 C ANISOU 4356 CG1 ILE A 457 15175 11493 7795 2713 66 2114 C ATOM 4357 CG2 ILE A 457 49.541-126.744 183.426 1.00 86.44 C ANISOU 4357 CG2 ILE A 457 14387 10841 7616 2299 187 1824 C ATOM 4358 CD1 ILE A 457 49.629-128.611 185.653 1.00 96.53 C ANISOU 4358 CD1 ILE A 457 16154 12009 8515 2451 136 2187 C ATOM 4359 N ALA A 458 51.744-124.191 182.662 1.00 80.24 N ANISOU 4359 N ALA A 458 12804 10785 6900 2439 70 1570 N ATOM 4360 CA ALA A 458 51.331-123.206 181.668 1.00 79.81 C ANISOU 4360 CA ALA A 458 12566 10720 7038 2260 111 1405 C ATOM 4361 C ALA A 458 52.363-123.032 180.560 1.00 84.61 C ANISOU 4361 C ALA A 458 13005 11450 7693 2455 60 1370 C ATOM 4362 O ALA A 458 51.996-122.711 179.423 1.00 84.75 O ANISOU 4362 O ALA A 458 12974 11354 7874 2382 98 1271 O ATOM 4363 CB ALA A 458 51.054-121.865 182.348 1.00 75.16 C ANISOU 4363 CB ALA A 458 11763 10337 6458 2009 118 1293 C ATOM 4364 N TYR A 459 53.645-123.240 180.856 1.00 85.42 N ANISOU 4364 N TYR A 459 13007 11804 7647 2705 -26 1456 N ATOM 4365 CA TYR A 459 54.711-122.943 179.908 1.00 84.00 C ANISOU 4365 CA TYR A 459 12606 11827 7484 2880 -76 1431 C ATOM 4366 C TYR A 459 55.451-124.174 179.401 1.00 88.27 C ANISOU 4366 C TYR A 459 13294 12308 7936 3265 -102 1546 C ATOM 4367 O TYR A 459 56.357-124.030 178.574 1.00 96.07 O ANISOU 4367 O TYR A 459 14099 13482 8920 3448 -135 1537 O ATOM 4368 CB TYR A 459 55.718-121.972 180.536 1.00 81.20 C ANISOU 4368 CB TYR A 459 11937 11894 7022 2846 -164 1425 C ATOM 4369 CG TYR A 459 55.213-120.552 180.646 1.00 80.72 C ANISOU 4369 CG TYR A 459 11695 11910 7065 2496 -153 1277 C ATOM 4370 CD1 TYR A 459 54.533-119.952 179.594 1.00 79.57 C ANISOU 4370 CD1 TYR A 459 11510 11607 7118 2326 -93 1148 C ATOM 4371 CD2 TYR A 459 55.412-119.812 181.803 1.00 82.98 C ANISOU 4371 CD2 TYR A 459 11871 12419 7240 2345 -207 1264 C ATOM 4372 CE1 TYR A 459 54.070-118.653 179.691 1.00 76.97 C ANISOU 4372 CE1 TYR A 459 11041 11329 6876 2031 -86 1015 C ATOM 4373 CE2 TYR A 459 54.951-118.514 181.910 1.00 79.62 C ANISOU 4373 CE2 TYR A 459 11318 12037 6897 2044 -201 1120 C ATOM 4374 CZ TYR A 459 54.281-117.940 180.852 1.00 76.25 C ANISOU 4374 CZ TYR A 459 10861 11440 6669 1896 -141 998 C ATOM 4375 OH TYR A 459 53.822-116.647 180.956 1.00 73.34 O ANISOU 4375 OH TYR A 459 10392 11098 6375 1622 -139 857 O ATOM 4376 N CYS A 460 55.100-125.374 179.861 1.00 86.07 N ANISOU 4376 N CYS A 460 13346 11778 7577 3400 -88 1658 N ATOM 4377 CA CYS A 460 55.817-126.561 179.413 1.00 91.49 C ANISOU 4377 CA CYS A 460 14213 12385 8163 3799 -119 1766 C ATOM 4378 C CYS A 460 54.885-127.745 179.187 1.00 91.74 C ANISOU 4378 C CYS A 460 14681 11949 8228 3821 -70 1810 C ATOM 4379 O CYS A 460 54.792-128.262 178.069 1.00 97.47 O ANISOU 4379 O CYS A 460 15547 12461 9025 3949 -47 1774 O ATOM 4380 CB CYS A 460 56.905-126.941 180.419 1.00 98.97 C ANISOU 4380 CB CYS A 460 15111 13611 8884 4066 -203 1913 C ATOM 4381 SG CYS A 460 57.882-128.382 179.935 1.00104.59 S ANISOU 4381 SG CYS A 460 16027 14252 9461 4602 -240 2037 S ATOM 4382 N PHE A 461 54.193-128.182 180.241 1.00 86.00 N ANISOU 4382 N PHE A 461 14175 11064 7439 3687 -58 1892 N ATOM 4383 CA PHE A 461 53.381-129.390 180.142 1.00 87.69 C ANISOU 4383 CA PHE A 461 14826 10842 7652 3697 -29 1966 C ATOM 4384 C PHE A 461 52.201-129.208 179.195 1.00 96.95 C ANISOU 4384 C PHE A 461 16076 11734 9025 3416 46 1844 C ATOM 4385 O PHE A 461 51.743-130.182 178.587 1.00100.50 O ANISOU 4385 O PHE A 461 16860 11829 9498 3472 57 1872 O ATOM 4386 CB PHE A 461 52.897-129.810 181.530 1.00 85.36 C ANISOU 4386 CB PHE A 461 14718 10482 7235 3578 -33 2093 C ATOM 4387 CG PHE A 461 54.011-130.095 182.501 1.00 81.69 C ANISOU 4387 CG PHE A 461 14209 10275 6556 3861 -114 2229 C ATOM 4388 CD1 PHE A 461 55.223-130.601 182.059 1.00 81.08 C ANISOU 4388 CD1 PHE A 461 14058 10309 6441 4225 -165 2236 C ATOM 4389 CD2 PHE A 461 53.848-129.851 183.855 1.00 81.69 C ANISOU 4389 CD2 PHE A 461 14171 10424 6444 3715 -125 2300 C ATOM 4390 CE1 PHE A 461 56.249-130.861 182.949 1.00 83.78 C ANISOU 4390 CE1 PHE A 461 14278 10905 6652 4425 -228 2314 C ATOM 4391 CE2 PHE A 461 54.870-130.109 184.749 1.00 82.89 C ANISOU 4391 CE2 PHE A 461 14227 10821 6446 3925 -198 2391 C ATOM 4392 CZ PHE A 461 56.072-130.615 184.295 1.00 83.62 C ANISOU 4392 CZ PHE A 461 14229 11021 6523 4270 -250 2394 C ATOM 4393 N CYS A 462 51.699-127.983 179.052 1.00100.89 N ANISOU 4393 N CYS A 462 16288 12382 9663 3116 91 1711 N ATOM 4394 CA CYS A 462 50.606-127.693 178.135 1.00102.66 C ANISOU 4394 CA CYS A 462 16538 12390 10077 2855 160 1594 C ATOM 4395 C CYS A 462 51.076-127.073 176.827 1.00101.58 C ANISOU 4395 C CYS A 462 16181 12356 10060 2932 160 1468 C ATOM 4396 O CYS A 462 50.243-126.769 175.967 1.00 99.72 O ANISOU 4396 O CYS A 462 15941 11965 9983 2733 211 1365 O ATOM 4397 CB CYS A 462 49.581-126.768 178.801 1.00102.76 C ANISOU 4397 CB CYS A 462 16407 12471 10164 2475 219 1531 C ATOM 4398 SG CYS A 462 48.557-127.573 180.054 1.00111.63 S ANISOU 4398 SG CYS A 462 17832 13398 11185 2291 252 1669 S ATOM 4399 N ASN A 463 52.380-126.880 176.653 1.00 99.51 N ANISOU 4399 N ASN A 463 15724 12369 9717 3209 104 1481 N ATOM 4400 CA ASN A 463 52.891-126.308 175.416 1.00 98.05 C ANISOU 4400 CA ASN A 463 15317 12310 9625 3286 105 1378 C ATOM 4401 C ASN A 463 52.811-127.327 174.286 1.00 92.37 C ANISOU 4401 C ASN A 463 14870 11298 8928 3488 116 1376 C ATOM 4402 O ASN A 463 53.163-128.498 174.455 1.00 94.27 O ANISOU 4402 O ASN A 463 15398 11382 9039 3764 86 1481 O ATOM 4403 CB ASN A 463 54.332-125.836 175.605 1.00104.72 C ANISOU 4403 CB ASN A 463 15859 13575 10354 3515 39 1412 C ATOM 4404 CG ASN A 463 54.925-125.255 174.339 1.00105.25 C ANISOU 4404 CG ASN A 463 15683 13810 10498 3592 40 1324 C ATOM 4405 OD1 ASN A 463 55.812-125.848 173.726 1.00107.78 O ANISOU 4405 OD1 ASN A 463 16015 14204 10731 3932 16 1368 O ATOM 4406 ND2 ASN A 463 54.432-124.090 173.934 1.00102.28 N ANISOU 4406 ND2 ASN A 463 15089 13496 10275 3288 69 1202 N ATOM 4407 N GLY A 464 52.341-126.870 173.122 1.00 84.53 N ANISOU 4407 N GLY A 464 13802 10223 8092 3354 157 1253 N ATOM 4408 CA GLY A 464 52.183-127.768 171.990 1.00 80.79 C ANISOU 4408 CA GLY A 464 13592 9463 7641 3513 167 1231 C ATOM 4409 C GLY A 464 53.492-128.325 171.470 1.00 82.43 C ANISOU 4409 C GLY A 464 13797 9807 7715 3963 127 1274 C ATOM 4410 O GLY A 464 53.546-129.477 171.029 1.00 83.41 O ANISOU 4410 O GLY A 464 14262 9662 7768 4207 115 1310 O ATOM 4411 N GLU A 465 54.561-127.527 171.512 1.00 79.16 N ANISOU 4411 N GLU A 465 13007 9816 7255 4081 101 1273 N ATOM 4412 CA GLU A 465 55.853-128.006 171.032 1.00 81.62 C ANISOU 4412 CA GLU A 465 13264 10326 7422 4523 67 1324 C ATOM 4413 C GLU A 465 56.442-129.047 171.974 1.00 85.97 C ANISOU 4413 C GLU A 465 14036 10854 7773 4842 18 1472 C ATOM 4414 O GLU A 465 57.022-130.041 171.523 1.00 92.77 O ANISOU 4414 O GLU A 465 15063 11633 8553 5159 22 1471 O ATOM 4415 CB GLU A 465 56.820-126.836 170.859 1.00 89.77 C ANISOU 4415 CB GLU A 465 13809 11851 8447 4521 48 1299 C ATOM 4416 CG GLU A 465 56.353-125.780 169.873 1.00 95.93 C ANISOU 4416 CG GLU A 465 14369 12668 9411 4235 89 1164 C ATOM 4417 CD GLU A 465 57.330-124.628 169.754 1.00100.61 C ANISOU 4417 CD GLU A 465 14502 13740 9984 4204 58 1157 C ATOM 4418 OE1 GLU A 465 58.344-124.629 170.484 1.00102.56 O ANISOU 4418 OE1 GLU A 465 14584 14310 10074 4383 3 1256 O ATOM 4419 OE2 GLU A 465 57.084-123.722 168.931 1.00100.77 O ANISOU 4419 OE2 GLU A 465 14329 13821 10139 3990 84 1059 O ATOM 4420 N VAL A 466 56.303-128.836 173.285 1.00 89.14 N ANISOU 4420 N VAL A 466 14403 11339 8129 4688 -7 1546 N ATOM 4421 CA VAL A 466 56.853-129.780 174.253 1.00 89.00 C ANISOU 4421 CA VAL A 466 14563 11315 7939 4942 -50 1675 C ATOM 4422 C VAL A 466 56.134-131.121 174.164 1.00 88.48 C ANISOU 4422 C VAL A 466 14967 10756 7893 4952 -23 1668 C ATOM 4423 O VAL A 466 56.768-132.182 174.188 1.00 83.94 O ANISOU 4423 O VAL A 466 14549 10115 7229 5221 -28 1677 O ATOM 4424 CB VAL A 466 56.779-129.189 175.672 1.00 83.81 C ANISOU 4424 CB VAL A 466 13771 10857 7213 4753 -86 1761 C ATOM 4425 CG1 VAL A 466 57.295-130.188 176.696 1.00 78.09 C ANISOU 4425 CG1 VAL A 466 13200 10113 6356 4946 -117 1861 C ATOM 4426 CG2 VAL A 466 57.565-127.889 175.745 1.00 85.02 C ANISOU 4426 CG2 VAL A 466 13426 11504 7373 4666 -113 1716 C ATOM 4427 N GLN A 467 54.802-131.095 174.056 1.00 91.54 N ANISOU 4427 N GLN A 467 15591 10804 8387 4645 5 1651 N ATOM 4428 CA GLN A 467 54.042-132.337 173.957 1.00 99.01 C ANISOU 4428 CA GLN A 467 16976 11290 9354 4585 20 1642 C ATOM 4429 C GLN A 467 54.417-133.117 172.704 1.00105.63 C ANISOU 4429 C GLN A 467 17957 11977 10200 4812 34 1535 C ATOM 4430 O GLN A 467 54.536-134.347 172.742 1.00110.22 O ANISOU 4430 O GLN A 467 18845 12327 10706 4953 22 1536 O ATOM 4431 CB GLN A 467 52.542-132.042 173.971 1.00 99.97 C ANISOU 4431 CB GLN A 467 17262 11129 9592 4175 52 1639 C ATOM 4432 CG GLN A 467 52.031-131.431 175.264 1.00 99.97 C ANISOU 4432 CG GLN A 467 17154 11254 9575 3901 59 1718 C ATOM 4433 CD GLN A 467 50.526-131.249 175.261 1.00102.10 C ANISOU 4433 CD GLN A 467 17525 11283 9987 3447 115 1670 C ATOM 4434 OE1 GLN A 467 49.836-131.703 174.348 1.00105.35 O ANISOU 4434 OE1 GLN A 467 18157 11390 10482 3355 133 1617 O ATOM 4435 NE2 GLN A 467 50.009-130.581 176.285 1.00100.69 N ANISOU 4435 NE2 GLN A 467 17180 11255 9823 3167 143 1689 N ATOM 4436 N ALA A 468 54.609-132.419 171.582 1.00107.00 N ANISOU 4436 N ALA A 468 17920 12288 10449 4848 58 1440 N ATOM 4437 CA ALA A 468 54.969-133.099 170.343 1.00101.31 C ANISOU 4437 CA ALA A 468 17320 11459 9714 5056 78 1330 C ATOM 4438 C ALA A 468 56.350-133.736 170.427 1.00107.93 C ANISOU 4438 C ALA A 468 18096 12528 10385 5468 69 1345 C ATOM 4439 O ALA A 468 56.623-134.715 169.723 1.00110.75 O ANISOU 4439 O ALA A 468 18686 12725 10668 5668 80 1278 O ATOM 4440 CB ALA A 468 54.904-132.121 169.170 1.00 90.85 C ANISOU 4440 CB ALA A 468 15746 10272 8500 4997 107 1236 C ATOM 4441 N GLU A 469 57.230-133.204 171.279 1.00120.43 N ANISOU 4441 N GLU A 469 19369 14497 11891 5592 48 1432 N ATOM 4442 CA GLU A 469 58.565-133.776 171.411 1.00124.58 C ANISOU 4442 CA GLU A 469 19806 15278 12251 5977 45 1456 C ATOM 4443 C GLU A 469 58.557-135.035 172.272 1.00126.25 C ANISOU 4443 C GLU A 469 20375 15240 12355 6091 20 1522 C ATOM 4444 O GLU A 469 59.306-135.978 171.997 1.00132.39 O ANISOU 4444 O GLU A 469 21295 16008 12998 6411 29 1502 O ATOM 4445 CB GLU A 469 59.529-132.739 171.990 1.00128.55 C ANISOU 4445 CB GLU A 469 19824 16312 12707 6039 23 1526 C ATOM 4446 CG GLU A 469 59.776-131.543 171.083 1.00128.62 C ANISOU 4446 CG GLU A 469 19451 16626 12792 5970 40 1466 C ATOM 4447 CD GLU A 469 60.427-131.925 169.766 1.00134.74 C ANISOU 4447 CD GLU A 469 20204 17474 13517 6226 91 1371 C ATOM 4448 OE1 GLU A 469 61.217-132.892 169.747 1.00140.21 O ANISOU 4448 OE1 GLU A 469 21015 18199 14059 6541 107 1375 O ATOM 4449 OE2 GLU A 469 60.145-131.259 168.748 1.00135.01 O ANISOU 4449 OE2 GLU A 469 20109 17538 13650 6115 115 1295 O ATOM 4450 N ILE A 470 57.722-135.073 173.312 1.00119.58 N ANISOU 4450 N ILE A 470 19685 14198 11552 5834 -10 1606 N ATOM 4451 CA ILE A 470 57.679-136.263 174.156 1.00122.58 C ANISOU 4451 CA ILE A 470 20407 14336 11831 5919 -39 1680 C ATOM 4452 C ILE A 470 56.878-137.376 173.487 1.00119.94 C ANISOU 4452 C ILE A 470 20545 13510 11515 5854 -34 1610 C ATOM 4453 O ILE A 470 57.126-138.560 173.744 1.00119.75 O ANISOU 4453 O ILE A 470 20833 13292 11375 6037 -56 1635 O ATOM 4454 CB ILE A 470 57.124-135.928 175.553 1.00124.09 C ANISOU 4454 CB ILE A 470 20584 14528 12038 5665 -72 1807 C ATOM 4455 CG1 ILE A 470 55.624-135.635 175.495 1.00124.35 C ANISOU 4455 CG1 ILE A 470 20789 14249 12212 5237 -57 1794 C ATOM 4456 CG2 ILE A 470 57.873-134.747 176.154 1.00121.04 C ANISOU 4456 CG2 ILE A 470 19727 14641 11624 5690 -88 1862 C ATOM 4457 CD1 ILE A 470 54.982-135.474 176.857 1.00122.43 C ANISOU 4457 CD1 ILE A 470 20590 13973 11955 4979 -78 1920 C ATOM 4458 N LYS A 471 55.916-137.030 172.626 1.00117.31 N ANISOU 4458 N LYS A 471 20277 12975 11319 5587 -12 1524 N ATOM 4459 CA LYS A 471 55.227-138.055 171.850 1.00122.22 C ANISOU 4459 CA LYS A 471 21319 13172 11948 5518 -16 1443 C ATOM 4460 C LYS A 471 56.138-138.641 170.780 1.00125.47 C ANISOU 4460 C LYS A 471 21784 13642 12246 5884 -1 1342 C ATOM 4461 O LYS A 471 56.023-139.827 170.449 1.00127.06 O ANISOU 4461 O LYS A 471 22378 13542 12359 5977 -23 1304 O ATOM 4462 CB LYS A 471 53.962-137.478 171.212 1.00121.12 C ANISOU 4462 CB LYS A 471 21202 12836 11982 5121 2 1380 C ATOM 4463 CG LYS A 471 52.911-137.019 172.209 1.00123.49 C ANISOU 4463 CG LYS A 471 21504 13041 12374 4735 -4 1477 C ATOM 4464 CD LYS A 471 51.722-136.386 171.502 1.00121.90 C ANISOU 4464 CD LYS A 471 21290 12690 12337 4365 24 1410 C ATOM 4465 CE LYS A 471 50.741-135.786 172.498 1.00119.54 C ANISOU 4465 CE LYS A 471 20941 12368 12109 3996 34 1510 C ATOM 4466 NZ LYS A 471 50.222-136.802 173.453 1.00120.61 N ANISOU 4466 NZ LYS A 471 21397 12252 12177 3860 2 1610 N ATOM 4467 N LYS A 472 57.042-137.827 170.232 1.00124.70 N ANISOU 4467 N LYS A 472 21302 13943 12137 6085 34 1303 N ATOM 4468 CA LYS A 472 58.027-138.333 169.282 1.00126.50 C ANISOU 4468 CA LYS A 472 21537 14301 12226 6456 58 1223 C ATOM 4469 C LYS A 472 58.993-139.301 169.953 1.00124.63 C ANISOU 4469 C LYS A 472 21434 14127 11792 6818 42 1287 C ATOM 4470 O LYS A 472 59.346-140.336 169.375 1.00127.06 O ANISOU 4470 O LYS A 472 22033 14286 11960 7068 41 1231 O ATOM 4471 CB LYS A 472 58.780-137.161 168.650 1.00133.52 C ANISOU 4471 CB LYS A 472 21939 15650 13144 6554 100 1189 C ATOM 4472 CG LYS A 472 60.185-137.487 168.170 1.00142.55 C ANISOU 4472 CG LYS A 472 22940 17123 14098 6992 131 1169 C ATOM 4473 CD LYS A 472 60.901-136.228 167.706 1.00144.16 C ANISOU 4473 CD LYS A 472 22617 17822 14336 7027 167 1161 C ATOM 4474 CE LYS A 472 62.372-136.491 167.433 1.00149.16 C ANISOU 4474 CE LYS A 472 23054 18857 14763 7446 201 1171 C ATOM 4475 NZ LYS A 472 63.079-135.265 166.971 1.00147.56 N ANISOU 4475 NZ LYS A 472 22325 19157 14584 7444 233 1174 N ATOM 4476 N SER A 473 59.425-138.986 171.176 1.00122.37 N ANISOU 4476 N SER A 473 20950 14063 11482 6853 24 1408 N ATOM 4477 CA SER A 473 60.343-139.870 171.887 1.00120.04 C ANISOU 4477 CA SER A 473 20765 13843 11003 7195 7 1480 C ATOM 4478 C SER A 473 59.647-141.152 172.327 1.00118.38 C ANISOU 4478 C SER A 473 21089 13141 10747 7135 -38 1507 C ATOM 4479 O SER A 473 60.250-142.231 172.301 1.00117.89 O ANISOU 4479 O SER A 473 21289 12989 10514 7453 -49 1505 O ATOM 4480 CB SER A 473 60.942-139.144 173.091 1.00118.39 C ANISOU 4480 CB SER A 473 20187 14013 10783 7212 -9 1606 C ATOM 4481 OG SER A 473 61.595-137.952 172.693 1.00118.10 O ANISOU 4481 OG SER A 473 19652 14442 10780 7240 22 1585 O ATOM 4482 N TRP A 474 58.379-141.055 172.734 1.00119.07 N ANISOU 4482 N TRP A 474 21349 12918 10976 6725 -66 1536 N ATOM 4483 CA TRP A 474 57.658-142.244 173.174 1.00126.07 C ANISOU 4483 CA TRP A 474 22732 13348 11823 6615 -115 1574 C ATOM 4484 C TRP A 474 57.311-143.154 172.003 1.00127.26 C ANISOU 4484 C TRP A 474 23268 13159 11927 6651 -122 1451 C ATOM 4485 O TRP A 474 57.229-144.376 172.174 1.00129.00 O ANISOU 4485 O TRP A 474 23914 13068 12031 6745 -166 1465 O ATOM 4486 CB TRP A 474 56.394-141.841 173.934 1.00130.98 C ANISOU 4486 CB TRP A 474 23394 13777 12594 6142 -136 1650 C ATOM 4487 CG TRP A 474 55.803-142.953 174.746 1.00138.68 C ANISOU 4487 CG TRP A 474 24797 14381 13513 6023 -190 1739 C ATOM 4488 CD1 TRP A 474 56.280-143.448 175.925 1.00142.31 C ANISOU 4488 CD1 TRP A 474 25325 14882 13864 6171 -224 1868 C ATOM 4489 CD2 TRP A 474 54.619-143.702 174.446 1.00142.46 C ANISOU 4489 CD2 TRP A 474 25687 14405 14038 5713 -223 1713 C ATOM 4490 NE1 TRP A 474 55.471-144.463 176.375 1.00146.07 N ANISOU 4490 NE1 TRP A 474 26237 14947 14317 5977 -273 1927 N ATOM 4491 CE2 TRP A 474 54.443-144.638 175.485 1.00147.53 C ANISOU 4491 CE2 TRP A 474 26635 14828 14593 5686 -275 1834 C ATOM 4492 CE3 TRP A 474 53.692-143.674 173.399 1.00140.22 C ANISOU 4492 CE3 TRP A 474 25533 13890 13854 5445 -217 1603 C ATOM 4493 CZ2 TRP A 474 53.379-145.537 175.508 1.00151.25 C ANISOU 4493 CZ2 TRP A 474 27532 14865 15073 5391 -322 1851 C ATOM 4494 CZ3 TRP A 474 52.637-144.567 173.424 1.00142.69 C ANISOU 4494 CZ3 TRP A 474 26260 13782 14173 5151 -267 1617 C ATOM 4495 CH2 TRP A 474 52.489-145.485 174.471 1.00149.15 C ANISOU 4495 CH2 TRP A 474 27373 14395 14902 5121 -319 1741 C ATOM 4496 N SER A 475 57.108-142.585 170.812 1.00128.14 N ANISOU 4496 N SER A 475 23244 13325 12117 6576 -87 1332 N ATOM 4497 CA SER A 475 56.829-143.408 169.640 1.00126.95 C ANISOU 4497 CA SER A 475 23441 12887 11906 6618 -100 1212 C ATOM 4498 C SER A 475 58.074-144.145 169.163 1.00131.31 C ANISOU 4498 C SER A 475 24081 13575 12236 7123 -88 1169 C ATOM 4499 O SER A 475 57.969-145.264 168.647 1.00134.08 O ANISOU 4499 O SER A 475 24861 13621 12462 7234 -123 1112 O ATOM 4500 CB SER A 475 56.259-142.546 168.514 1.00121.05 C ANISOU 4500 CB SER A 475 22507 12182 11305 6389 -68 1106 C ATOM 4501 OG SER A 475 55.030-141.955 168.898 1.00118.90 O ANISOU 4501 OG SER A 475 22198 11757 11223 5921 -78 1141 O ATOM 4502 N ARG A 476 59.254-143.540 169.321 1.00139.37 N ANISOU 4502 N ARG A 476 24703 15061 13191 7429 -41 1199 N ATOM 4503 CA ARG A 476 60.487-144.223 168.946 1.00149.05 C ANISOU 4503 CA ARG A 476 25983 16464 14186 7925 -21 1173 C ATOM 4504 C ARG A 476 60.831-145.336 169.926 1.00150.33 C ANISOU 4504 C ARG A 476 26465 16458 14195 8141 -64 1261 C ATOM 4505 O ARG A 476 61.464-146.326 169.541 1.00150.75 O ANISOU 4505 O ARG A 476 26794 16441 14043 8500 -70 1224 O ATOM 4506 CB ARG A 476 61.638-143.221 168.853 1.00156.37 C ANISOU 4506 CB ARG A 476 26357 17973 15082 8156 42 1192 C ATOM 4507 CG ARG A 476 61.485-142.203 167.735 1.00161.33 C ANISOU 4507 CG ARG A 476 26680 18794 15822 8013 86 1102 C ATOM 4508 CD ARG A 476 62.691-141.281 167.660 1.00168.63 C ANISOU 4508 CD ARG A 476 27065 20312 16693 8240 142 1132 C ATOM 4509 NE ARG A 476 62.615-140.375 166.518 1.00171.44 N ANISOU 4509 NE ARG A 476 27148 20856 17137 8127 182 1049 N ATOM 4510 CZ ARG A 476 63.561-139.500 166.195 1.00173.77 C ANISOU 4510 CZ ARG A 476 26969 21662 17394 8268 231 1062 C ATOM 4511 NH1 ARG A 476 64.662-139.409 166.930 1.00177.72 N ANISOU 4511 NH1 ARG A 476 27204 22551 17769 8522 246 1152 N ATOM 4512 NH2 ARG A 476 63.408-138.714 165.138 1.00170.62 N ANISOU 4512 NH2 ARG A 476 26354 21395 17079 8141 261 990 N ATOM 4513 N TRP A 477 60.428-145.195 171.188 1.00147.32 N ANISOU 4513 N TRP A 477 26061 16015 13900 7937 -97 1381 N ATOM 4514 CA TRP A 477 60.649-146.225 172.194 1.00146.12 C ANISOU 4514 CA TRP A 477 26219 15682 13619 8098 -145 1479 C ATOM 4515 C TRP A 477 59.564-147.293 172.202 1.00143.87 C ANISOU 4515 C TRP A 477 26501 14825 13339 7863 -212 1469 C ATOM 4516 O TRP A 477 59.721-148.305 172.893 1.00144.54 O ANISOU 4516 O TRP A 477 26920 14702 13298 8009 -260 1541 O ATOM 4517 CB TRP A 477 60.749-145.592 173.587 1.00149.96 C ANISOU 4517 CB TRP A 477 26413 16386 14177 7984 -156 1628 C ATOM 4518 CG TRP A 477 62.090-144.989 173.884 1.00150.32 C ANISOU 4518 CG TRP A 477 26003 16980 14133 8323 -115 1673 C ATOM 4519 CD1 TRP A 477 62.607-143.840 173.361 1.00145.81 C ANISOU 4519 CD1 TRP A 477 24941 16843 13616 8346 -61 1631 C ATOM 4520 CD2 TRP A 477 63.081-145.503 174.783 1.00153.07 C ANISOU 4520 CD2 TRP A 477 26332 17513 14313 8669 -129 1777 C ATOM 4521 NE1 TRP A 477 63.861-143.608 173.875 1.00147.68 N ANISOU 4521 NE1 TRP A 477 24848 17538 13728 8668 -41 1703 N ATOM 4522 CE2 TRP A 477 64.174-144.615 174.750 1.00151.96 C ANISOU 4522 CE2 TRP A 477 25667 17941 14132 8878 -81 1792 C ATOM 4523 CE3 TRP A 477 63.150-146.628 175.610 1.00156.39 C ANISOU 4523 CE3 TRP A 477 27129 17682 14610 8815 -181 1864 C ATOM 4524 CZ2 TRP A 477 65.323-144.817 175.512 1.00154.91 C ANISOU 4524 CZ2 TRP A 477 25868 18647 14345 9224 -82 1889 C ATOM 4525 CZ3 TRP A 477 64.291-146.827 176.366 1.00158.88 C ANISOU 4525 CZ3 TRP A 477 27284 18313 14769 9178 -181 1960 C ATOM 4526 CH2 TRP A 477 65.362-145.926 176.312 1.00158.36 C ANISOU 4526 CH2 TRP A 477 26681 18825 14666 9378 -131 1970 C ATOM 4527 N THR A 478 58.473-147.097 171.455 1.00141.79 N ANISOU 4527 N THR A 478 26351 14311 13212 7496 -222 1387 N ATOM 4528 CA THR A 478 57.363-148.047 171.402 1.00140.11 C ANISOU 4528 CA THR A 478 26649 13576 13010 7211 -290 1377 C ATOM 4529 C THR A 478 57.075-148.386 169.934 1.00139.79 C ANISOU 4529 C THR A 478 26823 13357 12935 7209 -294 1222 C ATOM 4530 O THR A 478 56.067-147.962 169.365 1.00139.93 O ANISOU 4530 O THR A 478 26828 13235 13105 6826 -299 1165 O ATOM 4531 CB THR A 478 56.121-147.492 172.105 1.00136.65 C ANISOU 4531 CB THR A 478 26145 13000 12776 6681 -309 1455 C ATOM 4532 OG1 THR A 478 55.764-146.231 171.526 1.00129.30 O ANISOU 4532 OG1 THR A 478 24821 12288 12019 6459 -256 1394 O ATOM 4533 CG2 THR A 478 56.384-147.307 173.593 1.00135.80 C ANISOU 4533 CG2 THR A 478 25888 13038 12670 6690 -317 1618 C ATOM 4534 N LEU A 479 57.969-149.163 169.327 1.00143.12 N ANISOU 4534 N LEU A 479 27444 13791 13143 7644 -294 1158 N ATOM 4535 CA LEU A 479 57.847-149.581 167.933 1.00135.68 C ANISOU 4535 CA LEU A 479 26730 12699 12122 7707 -303 1017 C ATOM 4536 C LEU A 479 57.647-151.090 167.883 1.00133.54 C ANISOU 4536 C LEU A 479 27089 11980 11670 7806 -387 1003 C ATOM 4537 O LEU A 479 58.553-151.853 168.234 1.00129.92 O ANISOU 4537 O LEU A 479 26809 11545 11009 8222 -395 1036 O ATOM 4538 CB LEU A 479 59.080-149.172 167.128 1.00121.10 C ANISOU 4538 CB LEU A 479 24584 11275 10156 8143 -231 949 C ATOM 4539 CG LEU A 479 59.184-147.702 166.720 1.00120.50 C ANISOU 4539 CG LEU A 479 23934 11604 10248 8017 -158 924 C ATOM 4540 CD1 LEU A 479 60.490-147.448 165.986 1.00119.37 C ANISOU 4540 CD1 LEU A 479 23521 11887 9946 8471 -92 876 C ATOM 4541 CD2 LEU A 479 57.997-147.304 165.857 1.00113.20 C ANISOU 4541 CD2 LEU A 479 23051 10464 9494 7588 -174 839 C ATOM 4542 N ALA A 480 56.468-151.514 167.436 1.00129.94 N ANISOU 4542 N ALA A 480 26967 11127 11279 7423 -451 957 N ATOM 4543 CA ALA A 480 56.143-152.933 167.335 1.00133.76 C ANISOU 4543 CA ALA A 480 28075 11153 11596 7451 -545 942 C ATOM 4544 C ALA A 480 57.035-153.639 166.319 1.00134.41 C ANISOU 4544 C ALA A 480 28393 11246 11431 7927 -546 835 C ATOM 4545 O ALA A 480 57.065-154.868 166.252 1.00139.19 O ANISOU 4545 O ALA A 480 29525 11515 11845 8080 -620 821 O ATOM 4546 CB ALA A 480 54.678-153.116 166.967 1.00129.58 C ANISOU 4546 CB ALA A 480 27794 10250 11192 6907 -613 912 C TER 4547 ALA A 480 HETATM 4548 N AC5 B 1 53.045-110.076 204.499 1.00118.66 N HETATM 4549 O AC5 B 1 51.509-111.410 202.468 1.00118.34 O HETATM 4550 CA AC5 B 1 53.583-110.475 203.198 1.00117.05 C HETATM 4551 C AC5 B 1 52.736-111.584 202.630 1.00110.02 C HETATM 4552 CB1 AC5 B 1 53.582-109.278 202.256 1.00120.87 C HETATM 4553 CB2 AC5 B 1 55.028-110.926 203.363 1.00119.91 C HETATM 4554 CG1 AC5 B 1 55.028-108.817 202.106 1.00120.21 C HETATM 4555 CG2 AC5 B 1 55.902-109.756 202.931 1.00119.64 C ATOM 4556 N VAL B 2 53.337-112.672 202.331 1.00181.12 N ANISOU 4556 N VAL B 2 23530 30180 15106 717 1097 1814 N ATOM 4557 CA VAL B 2 52.611-113.833 201.837 1.00148.84 C ANISOU 4557 CA VAL B 2 19754 26025 10774 740 957 1595 C ATOM 4558 C VAL B 2 52.360-114.797 202.989 1.00128.60 C ANISOU 4558 C VAL B 2 17363 23244 8255 726 822 1439 C ATOM 4559 O VAL B 2 53.047-114.744 204.010 1.00119.79 O ANISOU 4559 O VAL B 2 16132 22082 7301 768 881 1458 O ATOM 4560 CB VAL B 2 53.367-114.516 200.689 1.00132.10 C ANISOU 4560 CB VAL B 2 17739 24103 8351 960 1047 1440 C ATOM 4561 CG1 VAL B 2 53.267-113.681 199.424 1.00126.97 C ANISOU 4561 CG1 VAL B 2 16975 23644 7622 939 1128 1579 C ATOM 4562 CG2 VAL B 2 54.819-114.722 201.070 1.00124.08 C ANISOU 4562 CG2 VAL B 2 16595 23202 7348 1166 1207 1398 C HETATM 4563 N AIB B 3 51.377-115.676 202.810 1.00123.28 N ANISOU 4563 N AIB B 3 16967 22436 7437 661 633 1288 N HETATM 4564 CA AIB B 3 50.888-116.562 203.873 1.00104.47 C ANISOU 4564 CA AIB B 3 14765 19824 5105 600 458 1156 C HETATM 4565 C AIB B 3 51.975-117.403 204.501 1.00108.83 C ANISOU 4565 C AIB B 3 15373 20362 5616 788 511 978 C HETATM 4566 O AIB B 3 51.863-117.739 205.699 1.00102.57 O ANISOU 4566 O AIB B 3 14604 19398 4970 735 425 941 O HETATM 4567 CB1 AIB B 3 50.236-115.709 204.958 1.00101.13 C ANISOU 4567 CB1 AIB B 3 14164 19261 4999 405 409 1355 C HETATM 4568 CB2 AIB B 3 49.848-117.503 203.282 1.00105.96 C ANISOU 4568 CB2 AIB B 3 15274 19906 5081 533 245 1000 C ATOM 4569 N GLU B 4 53.007-117.755 203.742 1.00112.60 N ANISOU 4569 N GLU B 4 15867 21013 5902 1013 647 867 N ATOM 4570 CA GLU B 4 54.075-118.593 204.277 1.00110.14 C ANISOU 4570 CA GLU B 4 15613 20691 5546 1225 703 681 C ATOM 4571 C GLU B 4 54.939-117.826 205.275 1.00112.25 C ANISOU 4571 C GLU B 4 15581 20995 6073 1245 860 840 C ATOM 4572 O GLU B 4 55.593-118.427 206.126 1.00111.16 O ANISOU 4572 O GLU B 4 15474 20780 5982 1360 873 717 O ATOM 4573 CB GLU B 4 54.948-119.161 203.152 1.00111.45 C ANISOU 4573 CB GLU B 4 15867 21039 5440 1483 810 525 C ATOM 4574 CG GLU B 4 55.210-118.216 201.993 1.00116.44 C ANISOU 4574 CG GLU B 4 16304 21925 6013 1507 969 700 C ATOM 4575 CD GLU B 4 54.154-118.316 200.908 1.00118.60 C ANISOU 4575 CD GLU B 4 16763 22195 6103 1403 846 678 C ATOM 4576 OE1 GLU B 4 53.015-117.860 201.139 1.00117.03 O ANISOU 4576 OE1 GLU B 4 16572 21873 6022 1163 721 798 O ATOM 4577 OE2 GLU B 4 54.461-118.865 199.829 1.00122.10 O ANISOU 4577 OE2 GLU B 4 17349 22758 6287 1568 871 542 O ATOM 4578 N ILE B 5 54.939-116.497 205.172 1.00104.60 N ANISOU 4578 N ILE B 5 14335 20129 5280 1131 969 1111 N ATOM 4579 CA ILE B 5 55.697-115.686 206.120 1.00102.54 C ANISOU 4579 CA ILE B 5 13798 19880 5282 1121 1094 1285 C ATOM 4580 C ILE B 5 54.993-115.646 207.471 1.00109.54 C ANISOU 4580 C ILE B 5 14701 20522 6395 951 959 1325 C ATOM 4581 O ILE B 5 55.621-115.822 208.522 1.00102.62 O ANISOU 4581 O ILE B 5 13764 19573 5653 1007 995 1302 O ATOM 4582 CB ILE B 5 55.923-114.271 205.560 1.00106.16 C ANISOU 4582 CB ILE B 5 13975 20503 5860 1046 1225 1558 C ATOM 4583 CG1 ILE B 5 57.023-114.286 204.499 1.00111.11 C ANISOU 4583 CG1 ILE B 5 14514 21397 6305 1251 1398 1540 C ATOM 4584 CG2 ILE B 5 56.268-113.298 206.678 1.00 99.95 C ANISOU 4584 CG2 ILE B 5 12943 19641 5393 945 1277 1770 C ATOM 4585 CD1 ILE B 5 58.355-114.795 205.008 1.00109.34 C ANISOU 4585 CD1 ILE B 5 14222 21242 6079 1465 1522 1451 C ATOM 4586 N GLN B 6 53.679-115.407 207.464 1.00107.23 N ANISOU 4586 N GLN B 6 14484 20103 6153 748 802 1390 N ATOM 4587 CA GLN B 6 52.932-115.356 208.716 1.00101.57 C ANISOU 4587 CA GLN B 6 13776 19161 5654 587 665 1439 C ATOM 4588 C GLN B 6 52.927-116.706 209.418 1.00103.49 C ANISOU 4588 C GLN B 6 14253 19258 5811 651 538 1194 C ATOM 4589 O GLN B 6 52.893-116.763 210.652 1.00104.74 O ANISOU 4589 O GLN B 6 14375 19266 6156 598 486 1212 O ATOM 4590 CB GLN B 6 51.501-114.884 208.455 1.00105.75 C ANISOU 4590 CB GLN B 6 14340 19602 6239 377 521 1551 C ATOM 4591 CG GLN B 6 50.735-114.480 209.706 1.00116.54 C ANISOU 4591 CG GLN B 6 15639 20762 7880 210 409 1670 C ATOM 4592 CD GLN B 6 51.196-113.149 210.275 1.00124.39 C ANISOU 4592 CD GLN B 6 16350 21762 9149 175 532 1905 C ATOM 4593 OE1 GLN B 6 51.992-112.438 209.660 1.00129.87 O ANISOU 4593 OE1 GLN B 6 16889 22619 9836 245 689 2003 O ATOM 4594 NE2 GLN B 6 50.692-112.805 211.454 1.00122.52 N ANISOU 4594 NE2 GLN B 6 16052 21341 9159 65 448 1998 N ATOM 4595 N LEU B 7 52.962-117.801 208.653 1.00102.17 N ANISOU 4595 N LEU B 7 14337 19118 5365 768 475 959 N ATOM 4596 CA LEU B 7 53.042-119.125 209.261 1.00105.19 C ANISOU 4596 CA LEU B 7 14965 19344 5657 847 341 701 C ATOM 4597 C LEU B 7 54.331-119.284 210.056 1.00101.98 C ANISOU 4597 C LEU B 7 14451 18959 5337 1032 484 641 C ATOM 4598 O LEU B 7 54.318-119.817 211.171 1.00103.16 O ANISOU 4598 O LEU B 7 14667 18937 5591 1020 391 551 O ATOM 4599 CB LEU B 7 52.932-120.205 208.183 1.00113.97 C ANISOU 4599 CB LEU B 7 16378 20472 6452 957 249 459 C ATOM 4600 CG LEU B 7 52.978-121.671 208.624 1.00119.50 C ANISOU 4600 CG LEU B 7 17389 20981 7034 1045 75 159 C ATOM 4601 CD1 LEU B 7 52.055-122.502 207.756 1.00124.50 C ANISOU 4601 CD1 LEU B 7 18343 21527 7437 972 -140 13 C ATOM 4602 CD2 LEU B 7 54.394-122.229 208.560 1.00122.07 C ANISOU 4602 CD2 LEU B 7 17729 21385 7267 1348 228 -23 C ATOM 4603 N MET B 8 55.456-118.833 209.496 1.00103.49 N ANISOU 4603 N MET B 8 14469 19361 5491 1204 707 694 N ATOM 4604 CA MET B 8 56.721-118.904 210.218 1.00105.73 C ANISOU 4604 CA MET B 8 14622 19681 5870 1381 857 664 C ATOM 4605 C MET B 8 56.709-118.021 211.459 1.00102.65 C ANISOU 4605 C MET B 8 14006 19203 5795 1237 886 881 C ATOM 4606 O MET B 8 57.345-118.357 212.464 1.00100.21 O ANISOU 4606 O MET B 8 13672 18811 5592 1323 915 815 O ATOM 4607 CB MET B 8 57.877-118.501 209.302 1.00112.41 C ANISOU 4607 CB MET B 8 15297 20790 6623 1571 1084 720 C ATOM 4608 CG MET B 8 57.971-119.290 208.005 1.00123.66 C ANISOU 4608 CG MET B 8 16926 22321 7736 1736 1074 523 C ATOM 4609 SD MET B 8 58.302-121.044 208.244 1.00130.02 S ANISOU 4609 SD MET B 8 18085 22961 8354 1964 954 126 S ATOM 4610 CE MET B 8 58.500-121.577 206.545 1.00128.20 C ANISOU 4610 CE MET B 8 18021 22905 7784 2151 984 -18 C ATOM 4611 N HIS B 9 55.994-116.895 211.410 1.00 97.50 N ANISOU 4611 N HIS B 9 13196 18552 5298 1027 873 1134 N ATOM 4612 CA HIS B 9 55.954-115.994 212.557 1.00 94.59 C ANISOU 4612 CA HIS B 9 12625 18078 5238 894 888 1348 C ATOM 4613 C HIS B 9 55.095-116.564 213.678 1.00 91.69 C ANISOU 4613 C HIS B 9 12399 17468 4969 776 693 1271 C ATOM 4614 O HIS B 9 55.453-116.457 214.857 1.00 89.09 O ANISOU 4614 O HIS B 9 11984 17032 4832 773 707 1315 O ATOM 4615 CB HIS B 9 55.436-114.621 212.127 1.00100.94 C ANISOU 4615 CB HIS B 9 13240 18930 6182 726 916 1621 C ATOM 4616 CG HIS B 9 55.454-113.598 213.219 1.00102.62 C ANISOU 4616 CG HIS B 9 13251 19022 6716 606 930 1845 C ATOM 4617 ND1 HIS B 9 54.317-113.212 213.895 1.00100.76 N ANISOU 4617 ND1 HIS B 9 13032 18596 6656 421 779 1942 N ATOM 4618 CD2 HIS B 9 56.471-112.878 213.750 1.00102.60 C ANISOU 4618 CD2 HIS B 9 13035 19053 6895 649 1065 1993 C ATOM 4619 CE1 HIS B 9 54.632-112.299 214.797 1.00 99.48 C ANISOU 4619 CE1 HIS B 9 12687 18344 6765 368 821 2127 C ATOM 4620 NE2 HIS B 9 55.933-112.079 214.729 1.00100.24 N ANISOU 4620 NE2 HIS B 9 12647 18570 6872 493 989 2165 N ATOM 4621 N GLN B 10 53.962-117.168 213.335 1.00 97.76 N ANISOU 4621 N GLN B 10 13381 18148 5614 672 504 1167 N ATOM 4622 CA GLN B 10 53.087-117.773 214.331 1.00101.69 C ANISOU 4622 CA GLN B 10 14018 18425 6197 544 294 1097 C ATOM 4623 C GLN B 10 53.735-119.018 214.928 1.00100.73 C ANISOU 4623 C GLN B 10 14069 18218 5986 703 250 830 C ATOM 4624 O GLN B 10 53.547-119.321 216.105 1.00 98.40 O ANISOU 4624 O GLN B 10 13792 17650 5945 630 146 789 O ATOM 4625 CB GLN B 10 51.730-118.123 213.718 1.00111.73 C ANISOU 4625 CB GLN B 10 15471 19629 7355 385 95 1063 C ATOM 4626 CG GLN B 10 50.954-116.921 213.204 1.00123.16 C ANISOU 4626 CG GLN B 10 16760 21124 8910 233 118 1310 C ATOM 4627 CD GLN B 10 50.659-115.907 214.291 1.00129.77 C ANISOU 4627 CD GLN B 10 17386 21850 10072 110 126 1536 C ATOM 4628 OE1 GLN B 10 51.243-114.824 214.320 1.00135.19 O ANISOU 4628 OE1 GLN B 10 17853 22610 10904 135 282 1713 O ATOM 4629 NE2 GLN B 10 49.745-116.252 215.191 1.00127.77 N ANISOU 4629 NE2 GLN B 10 17201 21406 9938 -22 -55 1533 N HETATM 4630 N HRG B 11 54.497-119.734 214.106 1.00 98.99 N ANISOU 4630 N HRG B 11 13977 18104 5529 914 321 626 N HETATM 4631 CA HRG B 11 55.214-120.913 214.556 1.00 95.99 C ANISOU 4631 CA HRG B 11 13772 17560 5138 1092 287 341 C HETATM 4632 CB HRG B 11 55.825-121.656 213.374 1.00101.84 C ANISOU 4632 CB HRG B 11 14689 18479 5525 1332 346 130 C HETATM 4633 CG HRG B 11 55.683-123.591 211.815 1.00115.31 C ANISOU 4633 CG HRG B 11 16931 20108 6772 1537 152 -327 C HETATM 4634 CG' HRG B 11 55.090-122.955 213.067 1.00108.43 C ANISOU 4634 CG' HRG B 11 15897 19132 6170 1318 92 -138 C HETATM 4635 CD HRG B 11 55.156-125.001 211.584 1.00122.97 C ANISOU 4635 CD HRG B 11 18301 20853 7569 1550 -105 -621 C HETATM 4636 NE HRG B 11 55.710-125.575 210.373 1.00133.07 N ANISOU 4636 NE HRG B 11 19735 22229 8597 1762 -49 -790 N HETATM 4637 CZ HRG B 11 55.583-126.867 210.089 1.00136.63 C ANISOU 4637 CZ HRG B 11 20534 22487 8892 1838 -238 -1070 C HETATM 4638 NH1 HRG B 11 55.555-127.248 208.888 1.00137.21 N ANISOU 4638 NH1 HRG B 11 20764 22636 8734 1920 -254 -1164 N HETATM 4639 NH2 HRG B 11 55.492-127.758 211.075 1.00137.00 N ANISOU 4639 NH2 HRG B 11 20764 22249 9039 1820 -416 -1248 N HETATM 4640 C HRG B 11 56.293-120.522 215.523 1.00 93.45 C ANISOU 4640 C HRG B 11 13240 17168 5100 1180 448 401 C HETATM 4641 O HRG B 11 56.522-121.239 216.521 1.00 93.07 O ANISOU 4641 O HRG B 11 13279 16848 5235 1207 367 244 O ATOM 4642 N ALA B 12 56.964-119.407 215.252 1.00 90.34 N ANISOU 4642 N ALA B 12 12573 17009 4745 1217 664 631 N ATOM 4643 CA ALA B 12 58.035-118.925 216.116 1.00 87.06 C ANISOU 4643 CA ALA B 12 11936 16550 4593 1288 820 723 C ATOM 4644 C ALA B 12 57.496-118.540 217.489 1.00 87.19 C ANISOU 4644 C ALA B 12 11877 16273 4977 1095 712 835 C ATOM 4645 O ALA B 12 58.067-118.909 218.514 1.00 87.95 O ANISOU 4645 O ALA B 12 11962 16157 5298 1149 714 745 O ATOM 4646 CB ALA B 12 58.746-117.745 215.473 1.00 87.87 C ANISOU 4646 CB ALA B 12 11766 16975 4646 1329 1045 982 C ATOM 4647 N LYS B 13 56.389-117.793 217.502 1.00 82.39 N ANISOU 4647 N LYS B 13 11219 15663 4422 881 619 1033 N ATOM 4648 CA LYS B 13 55.769-117.423 218.770 1.00 85.78 C ANISOU 4648 CA LYS B 13 11587 15832 5173 710 506 1145 C ATOM 4649 C LYS B 13 55.194-118.635 219.490 1.00 83.78 C ANISOU 4649 C LYS B 13 11563 15287 4982 671 298 908 C ATOM 4650 O LYS B 13 55.172-118.668 220.726 1.00 78.95 O ANISOU 4650 O LYS B 13 10913 14428 4657 616 239 916 O ATOM 4651 CB LYS B 13 54.672-116.383 218.543 1.00 78.41 C ANISOU 4651 CB LYS B 13 10561 14989 4243 514 449 1406 C ATOM 4652 CG LYS B 13 55.160-115.066 217.969 1.00 93.69 C ANISOU 4652 CG LYS B 13 12265 17180 6154 520 630 1674 C ATOM 4653 CD LYS B 13 54.083-113.986 218.033 1.00 97.18 C ANISOU 4653 CD LYS B 13 12614 17579 6729 325 551 1914 C ATOM 4654 CE LYS B 13 52.841-114.357 217.228 1.00103.92 C ANISOU 4654 CE LYS B 13 13626 18432 7427 221 404 1843 C ATOM 4655 NZ LYS B 13 51.814-115.084 218.031 1.00104.24 N ANISOU 4655 NZ LYS B 13 13814 18282 7510 110 193 1760 N ATOM 4656 N TRP B 14 54.729-119.636 218.740 1.00 86.10 N ANISOU 4656 N TRP B 14 12102 15601 5010 694 176 703 N ATOM 4657 CA TRP B 14 54.127-120.808 219.365 1.00 94.41 C ANISOU 4657 CA TRP B 14 13390 16378 6104 633 -50 490 C ATOM 4658 C TRP B 14 55.183-121.694 220.014 1.00 99.71 C ANISOU 4658 C TRP B 14 14143 16869 6875 812 -16 255 C ATOM 4659 O TRP B 14 54.962-122.236 221.103 1.00104.63 O ANISOU 4659 O TRP B 14 14834 17211 7708 747 -147 169 O ATOM 4660 CB TRP B 14 53.322-121.596 218.333 1.00106.91 C ANISOU 4660 CB TRP B 14 15230 18030 7362 596 -211 350 C ATOM 4661 CG TRP B 14 52.556-122.734 218.918 1.00116.79 C ANISOU 4661 CG TRP B 14 16725 19006 8643 489 -476 170 C ATOM 4662 CD1 TRP B 14 51.286-122.699 219.412 1.00120.11 C ANISOU 4662 CD1 TRP B 14 17167 19311 9157 249 -676 279 C ATOM 4663 CD2 TRP B 14 53.011-124.082 219.072 1.00127.32 C ANISOU 4663 CD2 TRP B 14 18318 20152 9905 615 -580 -140 C ATOM 4664 NE1 TRP B 14 50.920-123.942 219.866 1.00126.54 N ANISOU 4664 NE1 TRP B 14 18231 19881 9969 201 -903 66 N ATOM 4665 CE2 TRP B 14 51.962-124.810 219.668 1.00131.03 C ANISOU 4665 CE2 TRP B 14 18960 20387 10437 422 -854 -199 C ATOM 4666 CE3 TRP B 14 54.202-124.746 218.764 1.00135.97 C ANISOU 4666 CE3 TRP B 14 19518 21264 10882 880 -473 -368 C ATOM 4667 CZ2 TRP B 14 52.069-126.166 219.964 1.00137.48 C ANISOU 4667 CZ2 TRP B 14 20062 20966 11208 471 -1034 -479 C ATOM 4668 CZ3 TRP B 14 54.306-126.093 219.058 1.00143.53 C ANISOU 4668 CZ3 TRP B 14 20765 21984 11787 950 -646 -657 C ATOM 4669 CH2 TRP B 14 53.246-126.788 219.651 1.00144.36 C ANISOU 4669 CH2 TRP B 14 21050 21838 11963 740 -929 -711 C ATOM 4670 N LEU B 15 56.337-121.855 219.361 1.00 99.12 N ANISOU 4670 N LEU B 15 14055 16962 6644 1043 160 155 N ATOM 4671 CA LEU B 15 57.403-122.664 219.943 1.00 97.26 C ANISOU 4671 CA LEU B 15 13885 16581 6489 1236 208 -62 C ATOM 4672 C LEU B 15 58.010-121.984 221.165 1.00 93.00 C ANISOU 4672 C LEU B 15 13106 15914 6316 1213 313 82 C ATOM 4673 O LEU B 15 58.382-122.656 222.134 1.00 93.73 O ANISOU 4673 O LEU B 15 13266 15758 6590 1260 259 -69 O ATOM 4674 CB LEU B 15 58.479-122.950 218.896 1.00 98.70 C ANISOU 4674 CB LEU B 15 14095 17017 6391 1508 380 -183 C ATOM 4675 CG LEU B 15 58.092-123.934 217.790 1.00106.02 C ANISOU 4675 CG LEU B 15 15327 18014 6942 1598 259 -410 C ATOM 4676 CD1 LEU B 15 59.206-124.052 216.761 1.00109.17 C ANISOU 4676 CD1 LEU B 15 15712 18706 7062 1890 459 -493 C ATOM 4677 CD2 LEU B 15 57.763-125.295 218.382 1.00106.46 C ANISOU 4677 CD2 LEU B 15 15693 17743 7013 1600 23 -695 C ATOM 4678 N ASN B 16 58.118-120.654 221.138 1.00 86.03 N ANISOU 4678 N ASN B 16 11954 15190 5543 1139 454 375 N ATOM 4679 CA ASN B 16 58.635-119.936 222.298 1.00 83.41 C ANISOU 4679 CA ASN B 16 11408 14726 5558 1102 533 530 C ATOM 4680 C ASN B 16 57.663-120.015 223.469 1.00 79.97 C ANISOU 4680 C ASN B 16 11019 13990 5376 914 342 556 C ATOM 4681 O ASN B 16 58.083-120.121 224.627 1.00 72.41 O ANISOU 4681 O ASN B 16 10013 12809 4691 925 337 529 O ATOM 4682 CB ASN B 16 58.920-118.480 221.933 1.00 89.64 C ANISOU 4682 CB ASN B 16 11927 15750 6383 1056 699 846 C ATOM 4683 CG ASN B 16 59.549-117.705 223.074 1.00 96.15 C ANISOU 4683 CG ASN B 16 12542 16440 7550 1028 777 1013 C ATOM 4684 OD1 ASN B 16 60.282-118.265 223.891 1.00101.33 O ANISOU 4684 OD1 ASN B 16 13212 16921 8369 1124 794 877 O ATOM 4685 ND2 ASN B 16 59.262-116.410 223.140 1.00 94.70 N ANISOU 4685 ND2 ASN B 16 12176 16332 7475 897 813 1309 N ATOM 4686 N SER B 17 56.365-119.969 223.186 1.00 83.87 N ANISOU 4686 N SER B 17 11601 14486 5779 744 183 615 N ATOM 4687 CA SER B 17 55.341-120.086 224.215 1.00 82.32 C ANISOU 4687 CA SER B 17 11447 14045 5786 566 -8 651 C ATOM 4688 C SER B 17 55.362-121.475 224.845 1.00 85.45 C ANISOU 4688 C SER B 17 12063 14179 6224 601 -159 369 C ATOM 4689 O SER B 17 55.193-121.620 226.056 1.00 87.27 O ANISOU 4689 O SER B 17 12277 14165 6716 534 -243 367 O ATOM 4690 CB SER B 17 53.959-119.793 223.626 1.00 80.12 C ANISOU 4690 CB SER B 17 11214 13874 5356 387 -142 777 C ATOM 4691 OG SER B 17 52.936-120.027 224.577 1.00 84.50 O ANISOU 4691 OG SER B 17 11815 14217 6074 224 -337 806 O HETATM 4692 N NLE B 18 55.571-122.490 224.014 1.00 85.62 N ANISOU 4692 N NLE B 18 12302 14250 5978 711 -199 131 N HETATM 4693 CA NLE B 18 55.630-123.865 224.476 1.00 82.59 C ANISOU 4693 CA NLE B 18 12164 13622 5594 757 -356 -154 C HETATM 4694 C NLE B 18 56.817-124.061 225.373 1.00 78.91 C ANISOU 4694 C NLE B 18 11627 13007 5347 910 -242 -249 C HETATM 4695 O NLE B 18 56.700-124.732 226.421 1.00 75.85 O ANISOU 4695 O NLE B 18 11329 12341 5150 868 -372 -364 O HETATM 4696 CB NLE B 18 55.703-124.822 223.290 1.00 85.99 C ANISOU 4696 CB NLE B 18 12853 14156 5663 875 -413 -383 C HETATM 4697 CG NLE B 18 54.383-125.558 223.096 1.00 93.46 C ANISOU 4697 CG NLE B 18 14038 14996 6477 689 -694 -453 C HETATM 4698 CD NLE B 18 54.083-126.441 224.302 1.00100.42 C ANISOU 4698 CD NLE B 18 15051 15540 7565 601 -893 -584 C HETATM 4699 CE NLE B 18 52.792-127.205 224.111 1.00102.72 C ANISOU 4699 CE NLE B 18 15577 15733 7719 400 -1189 -637 C ATOM 4700 N GLU B 19 57.955-123.494 224.986 1.00 78.10 N ANISOU 4700 N GLU B 19 11360 13094 5221 1082 -4 -193 N ATOM 4701 CA GLU B 19 59.181-123.612 225.767 1.00 81.98 C ANISOU 4701 CA GLU B 19 11759 13481 5909 1238 125 -263 C ATOM 4702 C GLU B 19 59.031-122.932 227.124 1.00 82.86 C ANISOU 4702 C GLU B 19 11694 13391 6397 1103 111 -90 C ATOM 4703 O GLU B 19 59.534-123.421 228.136 1.00 80.51 O ANISOU 4703 O GLU B 19 11417 12864 6309 1155 91 -205 O ATOM 4704 CB GLU B 19 60.359-123.006 225.002 1.00 86.72 C ANISOU 4704 CB GLU B 19 12183 14374 6393 1424 382 -184 C ATOM 4705 CG GLU B 19 61.713-123.245 225.648 1.00 92.36 C ANISOU 4705 CG GLU B 19 12813 15023 7258 1611 521 -272 C ATOM 4706 CD GLU B 19 62.807-122.396 225.031 1.00101.86 C ANISOU 4706 CD GLU B 19 13774 16535 8394 1745 775 -107 C ATOM 4707 OE1 GLU B 19 62.531-121.228 224.684 1.00103.13 O ANISOU 4707 OE1 GLU B 19 13746 16867 8571 1624 846 166 O ATOM 4708 OE2 GLU B 19 63.942-122.897 224.890 1.00107.71 O ANISOU 4708 OE2 GLU B 19 14512 17355 9060 1973 900 -244 O ATOM 4709 N ARG B 20 58.329-121.796 227.134 1.00 79.74 N ANISOU 4709 N ARG B 20 11136 13082 6079 940 118 185 N ATOM 4710 CA ARG B 20 58.158-121.046 228.373 1.00 70.93 C ANISOU 4710 CA ARG B 20 9858 11791 5300 830 105 367 C ATOM 4711 C ARG B 20 57.215-121.764 229.331 1.00 68.33 C ANISOU 4711 C ARG B 20 9671 11183 5110 699 -120 274 C ATOM 4712 O ARG B 20 57.455-121.788 230.544 1.00 68.90 O ANISOU 4712 O ARG B 20 9691 11027 5459 691 -142 272 O ATOM 4713 CB ARG B 20 57.647-119.638 228.065 1.00 65.04 C ANISOU 4713 CB ARG B 20 8922 11219 4570 711 162 683 C ATOM 4714 CG ARG B 20 57.585-118.725 229.276 1.00 62.26 C ANISOU 4714 CG ARG B 20 8402 10706 4548 630 164 888 C ATOM 4715 CD ARG B 20 57.023-117.355 228.926 1.00 61.92 C ANISOU 4715 CD ARG B 20 8204 10828 4494 523 199 1193 C ATOM 4716 NE ARG B 20 55.643-117.428 228.455 1.00 68.35 N ANISOU 4716 NE ARG B 20 9113 11709 5148 387 51 1232 N ATOM 4717 CZ ARG B 20 55.273-117.256 227.190 1.00 69.05 C ANISOU 4717 CZ ARG B 20 9229 12050 4959 367 74 1273 C ATOM 4718 NH1 ARG B 20 53.993-117.343 226.856 1.00 69.54 N ANISOU 4718 NH1 ARG B 20 9373 12158 4892 233 -73 1315 N ATOM 4719 NH2 ARG B 20 56.180-116.989 226.261 1.00 70.24 N ANISOU 4719 NH2 ARG B 20 9314 12417 4956 479 245 1282 N ATOM 4720 N VAL B 21 56.140-122.358 228.808 1.00 72.27 N ANISOU 4720 N VAL B 21 10346 11698 5414 591 -295 204 N ATOM 4721 CA VAL B 21 55.189-123.061 229.664 1.00 69.16 C ANISOU 4721 CA VAL B 21 10081 11066 5131 448 -524 137 C ATOM 4722 C VAL B 21 55.823-124.315 230.254 1.00 71.31 C ANISOU 4722 C VAL B 21 10526 11101 5468 549 -591 -148 C ATOM 4723 O VAL B 21 55.590-124.653 231.422 1.00 71.35 O ANISOU 4723 O VAL B 21 10546 10862 5703 480 -701 -175 O ATOM 4724 CB VAL B 21 53.904-123.383 228.880 1.00 72.37 C ANISOU 4724 CB VAL B 21 10631 11572 5296 295 -703 150 C ATOM 4725 CG1 VAL B 21 53.009-124.322 229.675 1.00 68.78 C ANISOU 4725 CG1 VAL B 21 10333 10881 4920 150 -957 55 C ATOM 4726 CG2 VAL B 21 53.159-122.102 228.542 1.00 72.60 C ANISOU 4726 CG2 VAL B 21 10475 11799 5310 180 -657 450 C ATOM 4727 N GLU B 22 56.635-125.024 229.465 1.00 74.17 N ANISOU 4727 N GLU B 22 11025 11536 5621 725 -526 -362 N ATOM 4728 CA GLU B 22 57.322-126.202 229.984 1.00 78.60 C ANISOU 4728 CA GLU B 22 11759 11877 6227 850 -581 -640 C ATOM 4729 C GLU B 22 58.256-125.835 231.129 1.00 75.23 C ANISOU 4729 C GLU B 22 11158 11309 6119 930 -451 -602 C ATOM 4730 O GLU B 22 58.380-126.584 232.105 1.00 70.22 O ANISOU 4730 O GLU B 22 10616 10410 5654 931 -553 -746 O ATOM 4731 CB GLU B 22 58.094-126.899 228.864 1.00 86.82 C ANISOU 4731 CB GLU B 22 12964 13059 6963 1063 -511 -859 C ATOM 4732 CG GLU B 22 57.364-128.082 228.258 1.00 98.74 C ANISOU 4732 CG GLU B 22 14803 14500 8214 1022 -745 -1072 C ATOM 4733 CD GLU B 22 57.193-129.224 229.243 1.00104.01 C ANISOU 4733 CD GLU B 22 15673 14832 9014 978 -955 -1274 C ATOM 4734 OE1 GLU B 22 58.056-129.378 230.133 1.00103.95 O ANISOU 4734 OE1 GLU B 22 15604 14671 9221 1088 -874 -1348 O ATOM 4735 OE2 GLU B 22 56.193-129.964 229.131 1.00107.55 O ANISOU 4735 OE2 GLU B 22 16343 15170 9353 825 -1208 -1348 O ATOM 4736 N TRP B 23 58.924-124.685 231.026 1.00 74.69 N ANISOU 4736 N TRP B 23 10838 11408 6133 989 -235 -402 N ATOM 4737 CA TRP B 23 59.762-124.219 232.123 1.00 65.63 C ANISOU 4737 CA TRP B 23 9515 10127 5296 1043 -122 -332 C ATOM 4738 C TRP B 23 58.927-123.879 233.350 1.00 62.53 C ANISOU 4738 C TRP B 23 9061 9514 5183 864 -253 -199 C ATOM 4739 O TRP B 23 59.361-124.108 234.485 1.00 57.73 O ANISOU 4739 O TRP B 23 8429 8678 4827 890 -264 -254 O ATOM 4740 CB TRP B 23 60.580-123.010 231.670 1.00 62.48 C ANISOU 4740 CB TRP B 23 8866 9967 4905 1118 113 -117 C ATOM 4741 CG TRP B 23 61.243-122.261 232.783 1.00 63.34 C ANISOU 4741 CG TRP B 23 8774 9950 5343 1121 207 29 C ATOM 4742 CD1 TRP B 23 62.487-122.484 233.299 1.00 64.19 C ANISOU 4742 CD1 TRP B 23 8820 9985 5585 1271 324 -56 C ATOM 4743 CD2 TRP B 23 60.696-121.158 233.517 1.00 62.20 C ANISOU 4743 CD2 TRP B 23 8471 9736 5426 973 183 291 C ATOM 4744 NE1 TRP B 23 62.747-121.590 234.310 1.00 62.58 N ANISOU 4744 NE1 TRP B 23 8432 9661 5685 1212 368 138 N ATOM 4745 CE2 TRP B 23 61.663-120.766 234.464 1.00 60.96 C ANISOU 4745 CE2 TRP B 23 8173 9450 5538 1037 281 348 C ATOM 4746 CE3 TRP B 23 59.481-120.468 233.467 1.00 58.30 C ANISOU 4746 CE3 TRP B 23 7948 9279 4925 804 83 483 C ATOM 4747 CZ2 TRP B 23 61.454-119.714 235.351 1.00 56.94 C ANISOU 4747 CZ2 TRP B 23 7515 8834 5287 940 273 583 C ATOM 4748 CZ3 TRP B 23 59.275-119.424 234.349 1.00 55.55 C ANISOU 4748 CZ3 TRP B 23 7446 8836 4826 723 84 714 C ATOM 4749 CH2 TRP B 23 60.256-119.057 235.279 1.00 53.34 C ANISOU 4749 CH2 TRP B 23 7046 8414 4809 792 173 759 C ATOM 4750 N LEU B 24 57.720-123.345 233.143 1.00 59.54 N ANISOU 4750 N LEU B 24 8658 9209 4755 691 -353 -24 N ATOM 4751 CA LEU B 24 56.867-122.987 234.270 1.00 59.49 C ANISOU 4751 CA LEU B 24 8587 9030 4988 538 -475 119 C ATOM 4752 C LEU B 24 56.301-124.225 234.954 1.00 61.94 C ANISOU 4752 C LEU B 24 9092 9098 5343 466 -691 -74 C ATOM 4753 O LEU B 24 56.189-124.262 236.184 1.00 65.21 O ANISOU 4753 O LEU B 24 9464 9297 6015 422 -755 -50 O ATOM 4754 CB LEU B 24 55.742-122.064 233.802 1.00 56.13 C ANISOU 4754 CB LEU B 24 8074 8780 4471 393 -517 367 C ATOM 4755 CG LEU B 24 54.770-121.603 234.888 1.00 53.74 C ANISOU 4755 CG LEU B 24 7693 8345 4380 253 -640 542 C ATOM 4756 CD1 LEU B 24 55.522-120.985 236.057 1.00 51.57 C ANISOU 4756 CD1 LEU B 24 7269 7904 4421 322 -544 625 C ATOM 4757 CD2 LEU B 24 53.772-120.616 234.316 1.00 53.78 C ANISOU 4757 CD2 LEU B 24 7605 8560 4271 144 -656 793 C ATOM 4758 N ARG B 25 55.932-125.247 234.177 1.00 59.83 N ANISOU 4758 N ARG B 25 9049 8860 4824 450 -817 -261 N ATOM 4759 CA ARG B 25 55.448-126.484 234.781 1.00 63.63 C ANISOU 4759 CA ARG B 25 9737 9104 5335 373 -1041 -449 C ATOM 4760 C ARG B 25 56.551-127.197 235.551 1.00 63.85 C ANISOU 4760 C ARG B 25 9825 8910 5524 522 -999 -661 C ATOM 4761 O ARG B 25 56.266-127.925 236.508 1.00 60.04 O ANISOU 4761 O ARG B 25 9436 8184 5191 453 -1157 -756 O ATOM 4762 CB ARG B 25 54.866-127.406 233.711 1.00 70.41 C ANISOU 4762 CB ARG B 25 10846 10036 5871 327 -1198 -602 C ATOM 4763 CG ARG B 25 53.650-126.838 233.000 1.00 82.20 C ANISOU 4763 CG ARG B 25 12300 11731 7201 156 -1275 -401 C ATOM 4764 CD ARG B 25 52.958-127.900 232.164 1.00 94.70 C ANISOU 4764 CD ARG B 25 14159 13324 8498 74 -1488 -559 C ATOM 4765 NE ARG B 25 51.852-127.352 231.383 1.00102.83 N ANISOU 4765 NE ARG B 25 15149 14570 9353 -80 -1551 -367 N ATOM 4766 CZ ARG B 25 50.618-127.189 231.848 1.00104.74 C ANISOU 4766 CZ ARG B 25 15341 14799 9656 -295 -1717 -192 C ATOM 4767 NH1 ARG B 25 50.326-127.528 233.097 1.00 99.60 N ANISOU 4767 NH1 ARG B 25 14671 13933 9238 -381 -1837 -182 N ATOM 4768 NH2 ARG B 25 49.675-126.684 231.063 1.00106.55 N ANISOU 4768 NH2 ARG B 25 15532 15244 9709 -419 -1762 -21 N ATOM 4769 N LYS B 26 57.810-126.999 235.154 1.00 66.46 N ANISOU 4769 N LYS B 26 10094 9332 5824 725 -790 -729 N ATOM 4770 CA LYS B 26 58.921-127.577 235.900 1.00 69.96 C ANISOU 4770 CA LYS B 26 10566 9587 6429 879 -729 -910 C ATOM 4771 C LYS B 26 59.105-126.872 237.239 1.00 67.18 C ANISOU 4771 C LYS B 26 10013 9078 6436 836 -678 -754 C ATOM 4772 O LYS B 26 59.392-127.518 238.254 1.00 61.42 O ANISOU 4772 O LYS B 26 9343 8097 5896 856 -746 -883 O ATOM 4773 CB LYS B 26 60.199-127.506 235.066 1.00 83.21 C ANISOU 4773 CB LYS B 26 12211 11448 7958 1111 -514 -996 C ATOM 4774 CG LYS B 26 61.272-128.507 235.459 1.00 96.43 C ANISOU 4774 CG LYS B 26 14007 12961 9669 1303 -490 -1264 C ATOM 4775 CD LYS B 26 62.409-128.498 234.447 1.00109.43 C ANISOU 4775 CD LYS B 26 15632 14846 11100 1543 -288 -1344 C ATOM 4776 CE LYS B 26 63.438-129.575 234.747 1.00114.68 C ANISOU 4776 CE LYS B 26 16443 15370 11759 1758 -273 -1626 C ATOM 4777 NZ LYS B 26 64.525-129.594 233.727 1.00117.88 N ANISOU 4777 NZ LYS B 26 16822 16040 11925 2013 -75 -1699 N ATOM 4778 N LYS B 27 58.938-125.547 237.262 1.00 65.41 N ANISOU 4778 N LYS B 27 9561 8989 6303 781 -566 -476 N ATOM 4779 CA LYS B 27 58.991-124.820 238.525 1.00 57.06 C ANISOU 4779 CA LYS B 27 8333 7776 5571 737 -542 -313 C ATOM 4780 C LYS B 27 57.806-125.176 239.412 1.00 55.45 C ANISOU 4780 C LYS B 27 8193 7390 5484 568 -759 -286 C ATOM 4781 O LYS B 27 57.949-125.275 240.636 1.00 52.34 O ANISOU 4781 O LYS B 27 7764 6773 5350 562 -798 -293 O ATOM 4782 CB LYS B 27 59.032-123.313 238.270 1.00 52.75 C ANISOU 4782 CB LYS B 27 7559 7416 5067 719 -397 -20 C ATOM 4783 CG LYS B 27 60.325-122.819 237.648 1.00 57.43 C ANISOU 4783 CG LYS B 27 8037 8175 5610 874 -173 1 C ATOM 4784 CD LYS B 27 61.512-123.071 238.562 1.00 56.74 C ANISOU 4784 CD LYS B 27 7901 7905 5752 998 -89 -97 C ATOM 4785 CE LYS B 27 62.802-122.567 237.935 1.00 64.19 C ANISOU 4785 CE LYS B 27 8708 9044 6637 1146 133 -49 C ATOM 4786 NZ LYS B 27 63.984-122.824 238.802 1.00 69.61 N ANISOU 4786 NZ LYS B 27 9339 9570 7539 1267 216 -137 N ATOM 4787 N LEU B 28 56.626-125.367 238.814 1.00 56.64 N ANISOU 4787 N LEU B 28 8434 7646 5442 428 -905 -244 N ATOM 4788 CA LEU B 28 55.461-125.768 239.594 1.00 55.79 C ANISOU 4788 CA LEU B 28 8381 7398 5417 259 -1122 -205 C ATOM 4789 C LEU B 28 55.677-127.116 240.266 1.00 61.00 C ANISOU 4789 C LEU B 28 9228 7802 6149 265 -1264 -458 C ATOM 4790 O LEU B 28 55.162-127.351 241.366 1.00 57.50 O ANISOU 4790 O LEU B 28 8775 7178 5895 171 -1392 -425 O ATOM 4791 CB LEU B 28 54.219-125.808 238.704 1.00 50.62 C ANISOU 4791 CB LEU B 28 7795 6926 4511 108 -1256 -120 C ATOM 4792 CG LEU B 28 53.623-124.450 238.329 1.00 59.89 C ANISOU 4792 CG LEU B 28 8779 8324 5654 54 -1175 174 C ATOM 4793 CD1 LEU B 28 52.468-124.616 237.354 1.00 55.59 C ANISOU 4793 CD1 LEU B 28 8318 7965 4836 -87 -1307 232 C ATOM 4794 CD2 LEU B 28 53.170-123.710 239.577 1.00 47.47 C ANISOU 4794 CD2 LEU B 28 7044 6648 4346 3 -1199 377 C ATOM 4795 N GLN B 29 56.434-128.011 239.627 1.00 64.07 N ANISOU 4795 N GLN B 29 9790 8171 6381 384 -1246 -710 N ATOM 4796 CA GLN B 29 56.775-129.272 240.273 1.00 65.80 C ANISOU 4796 CA GLN B 29 10199 8132 6672 415 -1372 -963 C ATOM 4797 C GLN B 29 57.746-129.058 241.427 1.00 60.25 C ANISOU 4797 C GLN B 29 9373 7246 6274 527 -1252 -981 C ATOM 4798 O GLN B 29 57.680-129.775 242.432 1.00 58.35 O ANISOU 4798 O GLN B 29 9211 6760 6199 488 -1379 -1086 O ATOM 4799 CB GLN B 29 57.362-130.245 239.250 1.00 75.04 C ANISOU 4799 CB GLN B 29 11602 9338 7574 544 -1382 -1229 C ATOM 4800 CG GLN B 29 57.510-131.668 239.763 1.00 85.05 C ANISOU 4800 CG GLN B 29 13122 10336 8856 557 -1566 -1502 C ATOM 4801 CD GLN B 29 56.175-132.319 240.074 1.00 92.23 C ANISOU 4801 CD GLN B 29 14173 11134 9737 315 -1859 -1480 C ATOM 4802 OE1 GLN B 29 55.145-131.953 239.508 1.00 93.09 O ANISOU 4802 OE1 GLN B 29 14257 11406 9708 161 -1940 -1319 O ATOM 4803 NE2 GLN B 29 56.188-133.290 240.981 1.00 94.66 N ANISOU 4803 NE2 GLN B 29 14622 11169 10174 276 -2024 -1633 N ATOM 4804 N ASP B 30 58.646-128.079 241.305 1.00 55.22 N ANISOU 4804 N ASP B 30 8544 6724 5713 657 -1017 -873 N ATOM 4805 CA ASP B 30 59.534-127.751 242.415 1.00 51.57 C ANISOU 4805 CA ASP B 30 7948 6095 5550 748 -908 -856 C ATOM 4806 C ASP B 30 58.753-127.187 243.594 1.00 51.93 C ANISOU 4806 C ASP B 30 7874 6012 5846 613 -993 -663 C ATOM 4807 O ASP B 30 59.058-127.494 244.752 1.00 53.43 O ANISOU 4807 O ASP B 30 8059 5968 6276 630 -1029 -722 O ATOM 4808 CB ASP B 30 60.606-126.761 241.960 1.00 54.76 C ANISOU 4808 CB ASP B 30 8168 6673 5965 890 -655 -747 C ATOM 4809 CG ASP B 30 61.556-127.357 240.944 1.00 66.43 C ANISOU 4809 CG ASP B 30 9744 8278 7217 1065 -549 -945 C ATOM 4810 OD1 ASP B 30 61.462-128.575 240.681 1.00 71.77 O ANISOU 4810 OD1 ASP B 30 10654 8872 7745 1095 -674 -1191 O ATOM 4811 OD2 ASP B 30 62.398-126.606 240.408 1.00 68.80 O ANISOU 4811 OD2 ASP B 30 9894 8768 7480 1175 -347 -848 O ATOM 4812 N VAL B 31 57.745-126.354 243.319 1.00 49.07 N ANISOU 4812 N VAL B 31 7415 5804 5423 490 -1027 -430 N ATOM 4813 CA VAL B 31 56.890-125.847 244.388 1.00 50.14 C ANISOU 4813 CA VAL B 31 7448 5845 5760 378 -1121 -242 C ATOM 4814 C VAL B 31 56.135-126.992 245.045 1.00 52.94 C ANISOU 4814 C VAL B 31 7954 6020 6143 260 -1350 -366 C ATOM 4815 O VAL B 31 55.988-127.038 246.273 1.00 51.17 O ANISOU 4815 O VAL B 31 7681 5607 6152 233 -1414 -331 O ATOM 4816 CB VAL B 31 55.926-124.777 243.844 1.00 48.34 C ANISOU 4816 CB VAL B 31 7102 5845 5419 286 -1117 25 C ATOM 4817 CG1 VAL B 31 55.086-124.198 244.973 1.00 45.23 C ANISOU 4817 CG1 VAL B 31 6596 5369 5222 206 -1204 226 C ATOM 4818 CG2 VAL B 31 56.695-123.685 243.132 1.00 46.38 C ANISOU 4818 CG2 VAL B 31 6719 5774 5128 390 -904 146 C ATOM 4819 N HIS B 32 55.646-127.935 244.236 1.00 54.28 N ANISOU 4819 N HIS B 32 8312 6242 6070 185 -1487 -506 N ATOM 4820 CA HIS B 32 54.966-129.105 244.780 1.00 52.46 C ANISOU 4820 CA HIS B 32 8248 5838 5847 57 -1728 -627 C ATOM 4821 C HIS B 32 55.886-129.902 245.696 1.00 51.59 C ANISOU 4821 C HIS B 32 8219 5452 5930 153 -1733 -841 C ATOM 4822 O HIS B 32 55.474-130.334 246.779 1.00 52.75 O ANISOU 4822 O HIS B 32 8378 5413 6250 67 -1871 -840 O ATOM 4823 CB HIS B 32 54.452-129.983 243.639 1.00 59.51 C ANISOU 4823 CB HIS B 32 9358 6825 6428 -24 -1874 -758 C ATOM 4824 CG HIS B 32 53.683-131.182 244.097 1.00 66.90 C ANISOU 4824 CG HIS B 32 10479 7594 7345 -185 -2150 -861 C ATOM 4825 ND1 HIS B 32 52.355-131.119 244.463 1.00 69.15 N ANISOU 4825 ND1 HIS B 32 10715 7927 7632 -393 -2330 -672 N ATOM 4826 CD2 HIS B 32 54.054-132.475 244.250 1.00 70.97 C ANISOU 4826 CD2 HIS B 32 11232 7901 7835 -172 -2288 -1125 C ATOM 4827 CE1 HIS B 32 51.941-132.322 244.819 1.00 72.22 C ANISOU 4827 CE1 HIS B 32 11295 8145 8000 -518 -2570 -804 C ATOM 4828 NE2 HIS B 32 52.953-133.163 244.700 1.00 71.79 N ANISOU 4828 NE2 HIS B 32 11426 7920 7929 -387 -2555 -1085 N ATOM 4829 N ASN B 33 57.140-130.097 245.283 1.00 49.24 N ANISOU 4829 N ASN B 33 7969 5137 5603 336 -1580 -1018 N ATOM 4830 CA ASN B 33 58.082-130.851 246.103 1.00 50.78 C ANISOU 4830 CA ASN B 33 8242 5081 5971 445 -1573 -1227 C ATOM 4831 C ASN B 33 58.470-130.091 247.365 1.00 48.84 C ANISOU 4831 C ASN B 33 7794 4708 6054 484 -1473 -1093 C ATOM 4832 O ASN B 33 58.785-130.711 248.386 1.00 53.38 O ANISOU 4832 O ASN B 33 8419 5041 6822 500 -1537 -1210 O ATOM 4833 CB ASN B 33 59.328-131.198 245.289 1.00 52.60 C ANISOU 4833 CB ASN B 33 8557 5363 6064 651 -1424 -1432 C ATOM 4834 CG ASN B 33 59.036-132.176 244.171 1.00 61.70 C ANISOU 4834 CG ASN B 33 9966 6583 6895 642 -1552 -1620 C ATOM 4835 OD1 ASN B 33 58.059-132.923 244.223 1.00 63.89 O ANISOU 4835 OD1 ASN B 33 10406 6779 7091 479 -1790 -1662 O ATOM 4836 ND2 ASN B 33 59.889-132.183 243.152 1.00 67.91 N ANISOU 4836 ND2 ASN B 33 10792 7523 7489 819 -1402 -1728 N ATOM 4837 N TYR B 34 58.452-128.764 247.318 1.00 51.89 N ANISOU 4837 N TYR B 34 7966 5243 6507 500 -1327 -850 N ATOM 4838 CA TYR B 34 58.800-127.957 248.481 1.00 52.47 C ANISOU 4838 CA TYR B 34 7862 5195 6881 540 -1243 -708 C ATOM 4839 C TYR B 34 57.710-128.043 249.545 1.00 61.34 C ANISOU 4839 C TYR B 34 8966 6195 8147 400 -1420 -599 C ATOM 4840 O TYR B 34 57.973-127.846 250.730 1.00 59.28 O ANISOU 4840 O TYR B 34 8626 5752 8144 432 -1410 -563 O ATOM 4841 CB TYR B 34 59.029-126.500 248.075 1.00 50.28 C ANISOU 4841 CB TYR B 34 7387 5108 6610 590 -1063 -470 C ATOM 4842 CG TYR B 34 59.631-125.642 249.167 1.00 46.19 C ANISOU 4842 CG TYR B 34 6709 4454 6388 661 -964 -341 C ATOM 4843 CD1 TYR B 34 61.006-125.588 249.353 1.00 50.32 C ANISOU 4843 CD1 TYR B 34 7189 4899 7033 804 -812 -430 C ATOM 4844 CD2 TYR B 34 58.827-124.883 250.006 1.00 42.30 C ANISOU 4844 CD2 TYR B 34 6112 3919 6043 591 -1028 -126 C ATOM 4845 CE1 TYR B 34 61.562-124.805 250.347 1.00 50.65 C ANISOU 4845 CE1 TYR B 34 7094 4806 7344 858 -736 -307 C ATOM 4846 CE2 TYR B 34 59.375-124.097 251.003 1.00 42.26 C ANISOU 4846 CE2 TYR B 34 5984 3775 6299 664 -953 -12 C ATOM 4847 CZ TYR B 34 60.743-124.063 251.169 1.00 47.81 C ANISOU 4847 CZ TYR B 34 6654 4386 7127 788 -812 -103 C ATOM 4848 OH TYR B 34 61.295-123.283 252.158 1.00 54.59 O ANISOU 4848 OH TYR B 34 7401 5097 8245 849 -751 15 O HETATM 4849 N NH2 B 35 56.676-128.216 249.361 1.00 34.84 N TER 4850 NH2 B 35 HETATM 4851 C1 NAG C 1 61.150-131.243 258.388 1.00 37.21 C HETATM 4852 C2 NAG C 1 61.786-131.359 259.769 1.00 38.16 C HETATM 4853 C3 NAG C 1 62.385-130.028 260.188 1.00 42.82 C HETATM 4854 C4 NAG C 1 63.322-129.502 259.112 1.00 45.93 C HETATM 4855 C5 NAG C 1 62.644-129.486 257.749 1.00 43.21 C HETATM 4856 C6 NAG C 1 63.645-129.097 256.669 1.00 53.13 C HETATM 4857 C7 NAG C 1 60.530-133.053 260.990 1.00 51.40 C HETATM 4858 C8 NAG C 1 60.027-133.343 262.372 1.00 56.01 C HETATM 4859 N2 NAG C 1 60.794-131.773 260.741 1.00 39.17 N HETATM 4860 O3 NAG C 1 63.119-130.202 261.403 1.00 50.47 O HETATM 4861 O4 NAG C 1 63.694-128.162 259.439 1.00 52.91 O HETATM 4862 O5 NAG C 1 62.091-130.763 257.428 1.00 41.60 O HETATM 4863 O6 NAG C 1 63.224-127.881 256.042 1.00 59.46 O HETATM 4864 O7 NAG C 1 60.683-133.934 260.159 1.00 53.42 O HETATM 4865 C1 NAG C 2 64.992-127.974 259.951 1.00 53.48 C HETATM 4866 C2 NAG C 2 65.667-126.630 259.711 1.00 52.56 C HETATM 4867 C3 NAG C 2 66.963-126.535 260.497 1.00 63.37 C HETATM 4868 C4 NAG C 2 66.703-126.841 261.966 1.00 69.54 C HETATM 4869 C5 NAG C 2 65.997-128.186 262.102 1.00 64.73 C HETATM 4870 C6 NAG C 2 65.692-128.533 263.557 1.00 64.43 C HETATM 4871 C7 NAG C 2 65.085-125.744 257.535 1.00 48.72 C HETATM 4872 C8 NAG C 2 65.491-125.585 256.099 1.00 44.07 C HETATM 4873 N2 NAG C 2 65.923-126.442 258.296 1.00 49.51 N HETATM 4874 O3 NAG C 2 67.498-125.216 260.350 1.00 73.96 O HETATM 4875 O4 NAG C 2 67.951-126.888 262.663 1.00 85.63 O HETATM 4876 O5 NAG C 2 64.784-128.190 261.347 1.00 56.85 O HETATM 4877 O6 NAG C 2 64.626-127.707 264.037 1.00 68.46 O HETATM 4878 O7 NAG C 2 64.055-125.261 257.978 1.00 48.93 O HETATM 4879 C1 BMA C 3 67.939-125.710 263.440 0.85 96.59 C HETATM 4880 C2 BMA C 3 68.940-125.850 264.573 0.85101.82 C HETATM 4881 C3 BMA C 3 68.681-124.767 265.606 0.85104.55 C HETATM 4882 C4 BMA C 3 68.760-123.401 264.941 0.85106.35 C HETATM 4883 C5 BMA C 3 67.876-123.326 263.699 0.85105.33 C HETATM 4884 C6 BMA C 3 68.168-122.044 262.930 0.85104.34 C HETATM 4885 O2 BMA C 3 70.257-125.698 264.031 0.85101.33 O HETATM 4886 O3 BMA C 3 69.656-124.851 266.650 0.85104.83 O HETATM 4887 O4 BMA C 3 68.339-122.403 265.878 0.85108.04 O HETATM 4888 O5 BMA C 3 68.093-124.433 262.821 0.85101.26 O HETATM 4889 O6 BMA C 3 69.555-122.020 262.568 0.85102.74 O HETATM 4890 C1 MAN C 4 70.313-126.069 267.180 0.84104.10 C HETATM 4891 C2 MAN C 4 70.701-125.441 268.513 0.84105.59 C HETATM 4892 C3 MAN C 4 72.131-124.920 268.492 0.84105.42 C HETATM 4893 C4 MAN C 4 73.086-125.969 267.939 0.84101.29 C HETATM 4894 C5 MAN C 4 72.564-126.511 266.613 0.84100.98 C HETATM 4895 C6 MAN C 4 73.489-127.581 266.049 0.84 99.71 C HETATM 4896 O2 MAN C 4 70.557-126.419 269.544 0.84104.14 O HETATM 4897 O3 MAN C 4 72.521-124.580 269.827 0.84109.59 O HETATM 4898 O4 MAN C 4 74.381-125.385 267.753 0.84 99.01 O HETATM 4899 O5 MAN C 4 71.265-127.066 266.813 0.84101.22 O HETATM 4900 O6 MAN C 4 72.906-128.144 264.868 0.84 97.61 O HETATM 4901 C1 MAN C 5 70.229-120.752 262.465 0.62 98.32 C HETATM 4902 C2 MAN C 5 71.648-120.713 261.908 0.62 95.68 C HETATM 4903 C3 MAN C 5 72.663-121.120 262.970 0.62 95.25 C HETATM 4904 C4 MAN C 5 72.435-120.359 264.270 0.62 93.64 C HETATM 4905 C5 MAN C 5 70.973-120.442 264.691 0.62 96.04 C HETATM 4906 C6 MAN C 5 70.718-119.649 265.967 0.62 94.26 C HETATM 4907 O2 MAN C 5 71.940-119.390 261.446 0.62 94.34 O HETATM 4908 O3 MAN C 5 73.984-120.846 262.488 0.62 97.11 O HETATM 4909 O4 MAN C 5 73.257-120.917 265.301 0.62 89.84 O HETATM 4910 O5 MAN C 5 70.151-119.940 263.637 0.62 97.80 O HETATM 4911 O6 MAN C 5 71.419-120.262 267.055 0.62 92.50 O HETATM 4912 C1 FUC C 6 62.105-128.024 255.195 1.00 52.31 C HETATM 4913 C2 FUC C 6 62.220-127.739 253.702 1.00 55.01 C HETATM 4914 C3 FUC C 6 61.164-128.513 252.927 1.00 54.10 C HETATM 4915 C4 FUC C 6 59.789-128.196 253.494 1.00 56.29 C HETATM 4916 C5 FUC C 6 59.767-128.483 254.991 1.00 59.49 C HETATM 4917 C6 FUC C 6 58.418-128.117 255.594 1.00 64.23 C HETATM 4918 O2 FUC C 6 63.527-128.100 253.244 1.00 61.55 O HETATM 4919 O3 FUC C 6 61.218-128.145 251.546 1.00 51.15 O HETATM 4920 O4 FUC C 6 59.485-126.815 253.267 1.00 60.54 O HETATM 4921 O5 FUC C 6 60.787-127.743 255.665 1.00 55.58 O HETATM 4922 C1 NAG D 1 42.419-124.033 246.696 1.00 53.82 C HETATM 4923 C2 NAG D 1 41.184-124.839 247.083 1.00 64.86 C HETATM 4924 C3 NAG D 1 40.072-124.640 246.065 1.00 72.70 C HETATM 4925 C4 NAG D 1 39.793-123.155 245.881 1.00 77.05 C HETATM 4926 C5 NAG D 1 41.076-122.383 245.591 1.00 75.24 C HETATM 4927 C6 NAG D 1 40.808-120.882 245.557 1.00 85.78 C HETATM 4928 C7 NAG D 1 42.025-126.723 248.347 1.00 60.02 C HETATM 4929 C8 NAG D 1 42.346-128.188 248.348 1.00 61.69 C HETATM 4930 N2 NAG D 1 41.517-126.245 247.214 1.00 63.12 N HETATM 4931 O3 NAG D 1 38.886-125.295 246.529 1.00 72.61 O HETATM 4932 O4 NAG D 1 38.887-122.981 244.786 1.00 83.36 O HETATM 4933 O5 NAG D 1 42.078-122.651 246.573 1.00 67.01 O HETATM 4934 O6 NAG D 1 40.164-120.475 246.770 1.00 96.03 O HETATM 4935 O7 NAG D 1 42.218-126.015 249.323 1.00 54.59 O HETATM 4936 C1 NAG D 2 37.605-122.358 245.015 1.00 91.57 C HETATM 4937 C2 NAG D 2 36.880-121.979 243.725 1.00 97.21 C HETATM 4938 C3 NAG D 2 35.788-120.947 243.963 1.00103.22 C HETATM 4939 C4 NAG D 2 34.903-121.369 245.125 1.00107.28 C HETATM 4940 C5 NAG D 2 35.760-121.626 246.356 1.00101.49 C HETATM 4941 C6 NAG D 2 34.899-122.018 247.551 1.00102.42 C HETATM 4942 C7 NAG D 2 38.201-122.138 241.694 1.00 99.25 C HETATM 4943 C8 NAG D 2 39.216-121.474 240.812 1.00 98.31 C HETATM 4944 N2 NAG D 2 37.825-121.444 242.763 1.00 97.46 N HETATM 4945 O3 NAG D 2 34.998-120.827 242.775 1.00103.87 O HETATM 4946 O4 NAG D 2 33.958-120.333 245.409 1.00115.86 O HETATM 4947 O5 NAG D 2 36.703-122.663 246.081 1.00 94.27 O HETATM 4948 O6 NAG D 2 35.675-121.929 248.752 1.00102.78 O HETATM 4949 O7 NAG D 2 37.745-123.241 241.445 1.00101.98 O HETATM 4950 C1 BMA D 3 32.624-120.277 244.910 1.00124.90 C HETATM 4951 C2 BMA D 3 32.107-121.574 244.293 1.00131.92 C HETATM 4952 C3 BMA D 3 30.877-121.317 243.438 1.00132.71 C HETATM 4953 C4 BMA D 3 29.833-120.584 244.266 1.00133.07 C HETATM 4954 C5 BMA D 3 30.429-119.300 244.831 1.00130.33 C HETATM 4955 C6 BMA D 3 29.417-118.560 245.697 1.00129.14 C HETATM 4956 O2 BMA D 3 31.775-122.495 245.338 1.00135.08 O HETATM 4957 O3 BMA D 3 30.344-122.562 242.975 1.00132.29 O HETATM 4958 O4 BMA D 3 28.705-120.271 243.443 1.00134.11 O HETATM 4959 O5 BMA D 3 31.592-119.581 245.614 1.00126.73 O HETATM 4960 O6 BMA D 3 29.219-119.280 246.920 1.00127.86 O HETATM 4961 C1 FUC D 4 39.353-119.679 247.705 0.81105.38 C HETATM 4962 C2 FUC D 4 39.066-118.226 247.339 0.81111.60 C HETATM 4963 C3 FUC D 4 38.250-117.534 248.422 0.81115.56 C HETATM 4964 C4 FUC D 4 38.934-117.702 249.769 0.81115.63 C HETATM 4965 C5 FUC D 4 39.180-119.179 250.051 0.81113.46 C HETATM 4966 C6 FUC D 4 39.919-119.356 251.373 0.81113.74 C HETATM 4967 O2 FUC D 4 38.360-118.170 246.094 0.81114.72 O HETATM 4968 O3 FUC D 4 38.133-116.140 248.117 0.81117.62 O HETATM 4969 O4 FUC D 4 40.181-117.000 249.762 0.81116.11 O HETATM 4970 O5 FUC D 4 39.948-119.775 249.002 0.81109.49 O HETATM 4971 C1 NAG E 1 52.083-127.439 267.318 1.00114.28 C HETATM 4972 C2 NAG E 1 52.005-128.716 266.478 1.00129.11 C HETATM 4973 C3 NAG E 1 51.641-129.945 267.305 1.00137.94 C HETATM 4974 C4 NAG E 1 52.524-130.008 268.543 1.00142.30 C HETATM 4975 C5 NAG E 1 52.339-128.712 269.325 1.00136.08 C HETATM 4976 C6 NAG E 1 53.075-128.721 270.659 1.00139.49 C HETATM 4977 C7 NAG E 1 49.857-128.049 265.429 1.00135.94 C HETATM 4978 C8 NAG E 1 49.301-127.548 264.129 1.00135.45 C HETATM 4979 N2 NAG E 1 51.088-128.564 265.355 1.00133.48 N HETATM 4980 O3 NAG E 1 51.828-131.125 266.516 1.00140.30 O HETATM 4981 O4 NAG E 1 52.189-131.148 269.345 1.00149.95 O HETATM 4982 O5 NAG E 1 52.814-127.625 268.533 1.00125.51 O HETATM 4983 O6 NAG E 1 54.467-128.975 270.440 1.00141.15 O HETATM 4984 O7 NAG E 1 49.206-127.991 266.461 1.00137.97 O HETATM 4985 C1 NAG E 2 53.275-132.096 269.653 1.00155.69 C HETATM 4986 C2 NAG E 2 52.921-133.109 270.742 1.00159.15 C HETATM 4987 C3 NAG E 2 54.063-134.071 271.042 1.00158.62 C HETATM 4988 C4 NAG E 2 54.709-134.627 269.782 1.00160.45 C HETATM 4989 C5 NAG E 2 54.952-133.548 268.734 1.00161.18 C HETATM 4990 C6 NAG E 2 55.402-134.205 267.432 1.00162.20 C HETATM 4991 C7 NAG E 2 52.850-131.495 272.724 1.00158.62 C HETATM 4992 C8 NAG E 2 54.326-131.267 272.901 1.00157.31 C HETATM 4993 N2 NAG E 2 52.414-132.533 271.991 1.00160.11 N HETATM 4994 O3 NAG E 2 53.515-135.135 271.827 1.00158.42 O HETATM 4995 O4 NAG E 2 55.972-135.203 270.136 1.00157.26 O HETATM 4996 O5 NAG E 2 53.768-132.781 268.497 1.00157.93 O HETATM 4997 O6 NAG E 2 55.248-133.291 266.341 1.00162.83 O HETATM 4998 O7 NAG E 2 52.052-130.754 273.276 1.00158.14 O HETATM 4999 C1 BMA E 3 56.252-136.536 270.628 1.00155.95 C HETATM 5000 C2 BMA E 3 55.705-137.343 271.801 1.00156.24 C HETATM 5001 C3 BMA E 3 56.026-138.822 271.668 1.00151.10 C HETATM 5002 C4 BMA E 3 55.661-139.342 270.284 1.00149.49 C HETATM 5003 C5 BMA E 3 56.227-138.442 269.190 1.00149.99 C HETATM 5004 C6 BMA E 3 55.766-138.900 267.811 1.00147.18 C HETATM 5005 O2 BMA E 3 54.283-137.192 271.858 1.00159.74 O HETATM 5006 O3 BMA E 3 55.295-139.536 272.675 1.00149.90 O HETATM 5007 O4 BMA E 3 56.204-140.657 270.128 1.00148.54 O HETATM 5008 O5 BMA E 3 55.814-137.088 269.386 1.00154.56 O HETATM 5009 O6 BMA E 3 56.407-140.134 267.468 1.00145.78 O HETATM 5010 C1 MAN E 4 57.233-140.313 266.278 1.00145.50 C HETATM 5011 C2 MAN E 4 57.542-139.131 265.368 1.00146.38 C HETATM 5012 C3 MAN E 4 56.632-139.151 264.147 1.00145.52 C HETATM 5013 C4 MAN E 4 56.700-140.507 263.456 1.00145.07 C HETATM 5014 C5 MAN E 4 56.459-141.633 264.455 1.00143.71 C HETATM 5015 C6 MAN E 4 56.618-142.993 263.784 1.00141.04 C HETATM 5016 O2 MAN E 4 58.908-139.198 264.945 1.00145.78 O HETATM 5017 O3 MAN E 4 57.029-138.121 263.234 1.00143.77 O HETATM 5018 O4 MAN E 4 55.715-140.567 262.418 1.00142.68 O HETATM 5019 O5 MAN E 4 57.384-141.526 265.538 1.00143.46 O HETATM 5020 O6 MAN E 4 56.296-144.031 264.715 1.00140.09 O HETATM 5021 C1 MAN A1511 68.612-126.103 270.383 0.75105.33 C HETATM 5022 C2 MAN A1511 68.597-125.309 271.672 0.75106.43 C HETATM 5023 C3 MAN A1511 67.239-125.472 272.338 0.75106.95 C HETATM 5024 C4 MAN A1511 66.099-125.203 271.358 0.75106.54 C HETATM 5025 C5 MAN A1511 66.280-125.955 270.041 0.75106.35 C HETATM 5026 C6 MAN A1511 65.240-125.506 269.023 0.75106.45 C HETATM 5027 O2 MAN A1511 68.821-123.928 271.368 0.75106.77 O HETATM 5028 O3 MAN A1511 67.146-124.557 273.435 0.75107.15 O HETATM 5029 O4 MAN A1511 64.863-125.610 271.960 0.75105.32 O HETATM 5030 O5 MAN A1511 67.576-125.716 269.492 0.75105.20 O HETATM 5031 O6 MAN A1511 65.571-126.043 267.737 0.75105.49 O HETATM 5032 C1 MAN A1516 54.333-139.179 274.674 0.84133.17 C HETATM 5033 C2 MAN A1516 53.722-137.882 275.197 0.84133.36 C HETATM 5034 C3 MAN A1516 52.618-138.175 276.206 0.84131.94 C HETATM 5035 C4 MAN A1516 51.613-139.150 275.619 0.84134.06 C HETATM 5036 C5 MAN A1516 52.315-140.387 275.076 0.84135.87 C HETATM 5037 C6 MAN A1516 51.308-141.304 274.399 0.84137.84 C HETATM 5038 O2 MAN A1516 53.185-137.137 274.099 0.84136.38 O HETATM 5039 O3 MAN A1516 51.928-136.968 276.550 0.84130.03 O HETATM 5040 O4 MAN A1516 50.672-139.526 276.630 0.84134.33 O HETATM 5041 O5 MAN A1516 53.308-140.008 274.123 0.84135.47 O HETATM 5042 O6 MAN A1516 50.092-141.311 275.157 0.84138.74 O HETATM 5043 C1 MAN A1517 54.761-135.613 276.222 0.74116.29 C HETATM 5044 C2 MAN A1517 55.742-134.534 275.787 0.74116.72 C HETATM 5045 C3 MAN A1517 55.612-133.315 276.691 0.74118.42 C HETATM 5046 C4 MAN A1517 54.161-132.853 276.757 0.74118.78 C HETATM 5047 C5 MAN A1517 53.244-134.015 277.120 0.74116.71 C HETATM 5048 C6 MAN A1517 51.782-133.584 277.105 0.74113.48 C HETATM 5049 O2 MAN A1517 55.458-134.162 274.434 0.74115.38 O HETATM 5050 O3 MAN A1517 56.431-132.256 276.185 0.74118.54 O HETATM 5051 O4 MAN A1517 54.032-131.818 277.738 0.74119.24 O HETATM 5052 O5 MAN A1517 53.434-135.083 276.191 0.74116.93 O HETATM 5053 O6 MAN A1517 50.952-134.687 277.489 0.74110.92 O HETATM 5054 C1 OLA A1518 58.278-102.556 175.847 1.00105.40 C HETATM 5055 O1 OLA A1518 57.360-103.079 175.178 1.00104.77 O HETATM 5056 O2 OLA A1518 58.296-101.344 176.151 1.00106.96 O HETATM 5057 C2 OLA A1518 59.412-103.435 176.318 1.00101.68 C HETATM 5058 C3 OLA A1518 60.652-102.600 176.614 1.00 97.44 C HETATM 5059 C4 OLA A1518 61.738-103.499 177.192 1.00 95.35 C HETATM 5060 C5 OLA A1518 63.139-102.983 176.890 1.00 93.71 C HETATM 5061 C6 OLA A1518 64.149-104.112 177.066 1.00 93.27 C HETATM 5062 C7 OLA A1518 65.579-103.616 176.894 1.00 92.16 C HETATM 5063 C1 OLA A1519 70.584-114.315 179.788 1.00110.54 C HETATM 5064 O1 OLA A1519 70.884-113.653 178.771 1.00110.05 O HETATM 5065 O2 OLA A1519 70.403-113.792 180.909 1.00110.99 O HETATM 5066 C2 OLA A1519 70.437-115.813 179.660 1.00110.83 C HETATM 5067 C3 OLA A1519 70.440-116.205 178.187 1.00109.97 C HETATM 5068 C4 OLA A1519 70.344-117.717 178.027 1.00108.05 C HETATM 5069 C5 OLA A1519 70.288-118.111 176.556 1.00108.07 C HETATM 5070 C6 OLA A1519 71.487-117.558 175.797 1.00107.46 C HETATM 5071 C7 OLA A1519 71.359-117.839 174.305 1.00107.37 C HETATM 5072 C8 OLA A1519 72.461-117.134 173.524 1.00107.38 C HETATM 5073 C9 OLA A1519 73.809-117.578 174.041 1.00106.81 C HETATM 5074 C3 OLA A1520 37.866-110.688 174.316 1.00 94.63 C HETATM 5075 C4 OLA A1520 38.482-110.007 175.532 1.00 93.48 C HETATM 5076 C5 OLA A1520 38.629-110.986 176.690 1.00 92.45 C HETATM 5077 C6 OLA A1520 39.050-110.258 177.960 1.00 90.92 C HETATM 5078 C7 OLA A1520 38.712-111.083 179.196 1.00 90.20 C HETATM 5079 C8 OLA A1520 38.657-110.198 180.435 1.00 91.24 C HETATM 5080 C9 OLA A1520 38.113-110.995 181.597 1.00 92.04 C HETATM 5081 C1 OLA A1521 42.671-114.779 176.274 1.00101.54 C HETATM 5082 O1 OLA A1521 42.069-113.692 176.134 1.00102.25 O HETATM 5083 O2 OLA A1521 43.169-115.410 175.317 1.00101.76 O HETATM 5084 C2 OLA A1521 42.800-115.357 177.664 1.00 98.44 C HETATM 5085 C3 OLA A1521 42.215-114.389 178.685 1.00 94.51 C HETATM 5086 C4 OLA A1521 42.348-114.947 180.097 1.00 91.45 C HETATM 5087 C5 OLA A1521 41.791-113.981 181.136 1.00 88.55 C HETATM 5088 C6 OLA A1521 41.818-114.608 182.525 0.69 87.36 C HETATM 5089 C7 OLA A1521 41.174-113.694 183.561 0.72 86.80 C HETATM 5090 C8 OLA A1521 40.971-114.423 184.885 0.67 85.77 C HETATM 5091 C9 OLA A1521 42.312-114.788 185.475 0.57 85.18 C HETATM 5092 C10 OLA A1521 42.558-114.607 186.771 0.40 84.72 C HETATM 5093 C11 OLA A1521 41.505-114.039 187.694 1.00 84.79 C HETATM 5094 C12 OLA A1521 41.498-114.831 188.997 1.00 88.50 C HETATM 5095 C13 OLA A1521 40.557-114.206 190.023 1.00 88.26 C HETATM 5096 C14 OLA A1521 40.671-114.903 191.375 1.00 88.32 C HETATM 5097 C15 OLA A1521 39.677-114.317 192.371 1.00 89.27 C HETATM 5098 C16 OLA A1521 39.726-115.038 193.714 1.00 88.53 C HETATM 5099 C17 OLA A1521 40.946-114.624 194.529 1.00 89.39 C HETATM 5100 C18 OLA A1521 40.878-115.193 195.930 1.00 88.44 C HETATM 5101 C1 OLA A1522 46.560-128.502 175.735 1.00115.42 C HETATM 5102 O1 OLA A1522 47.578-128.157 175.096 1.00114.36 O HETATM 5103 O2 OLA A1522 45.679-129.249 175.259 1.00115.07 O HETATM 5104 C2 OLA A1522 46.392-127.991 177.146 1.00116.08 C HETATM 5105 C3 OLA A1522 45.082-127.221 177.270 0.88116.04 C HETATM 5106 C4 OLA A1522 45.101-126.323 178.501 1.00115.96 C HETATM 5107 C5 OLA A1522 46.110-125.194 178.325 0.79115.92 C HETATM 5108 C6 OLA A1522 46.313-124.413 179.619 0.81114.11 C HETATM 5109 C7 OLA A1522 47.237-123.222 179.389 1.00110.95 C HETATM 5110 C8 OLA A1522 47.606-122.537 180.700 1.00107.96 C HETATM 5111 C9 OLA A1522 46.349-122.182 181.458 1.00105.41 C HETATM 5112 C10 OLA A1522 46.258-122.417 182.765 1.00103.15 C HETATM 5113 C11 OLA A1522 47.414-123.028 183.521 1.00100.92 C HETATM 5114 C12 OLA A1522 47.429-122.478 184.942 0.76 98.36 C HETATM 5115 C13 OLA A1522 46.255-123.032 185.743 1.00 97.41 C HETATM 5116 C14 OLA A1522 46.032-122.240 187.025 1.00 97.78 C HETATM 5117 C15 OLA A1522 44.931-122.871 187.869 1.00 97.05 C HETATM 5118 C16 OLA A1522 44.580-121.986 189.060 0.91 97.11 C HETATM 5119 C17 OLA A1522 43.646-122.707 190.025 0.98 95.38 C HETATM 5120 C18 OLA A1522 43.320-121.834 191.218 1.00 91.17 C HETATM 5121 C7 OLA A1523 53.877 -96.016 187.480 1.00109.55 C HETATM 5122 C8 OLA A1523 54.193 -97.465 187.831 1.00108.55 C HETATM 5123 C9 OLA A1523 53.824 -98.357 186.669 1.00108.71 C HETATM 5124 C10 OLA A1523 54.747 -99.122 186.092 1.00108.72 C HETATM 5125 C11 OLA A1523 56.174 -99.108 186.588 1.00108.67 C HETATM 5126 C12 OLA A1523 56.619-100.532 186.900 1.00107.80 C HETATM 5127 C13 OLA A1523 58.118-100.593 187.166 1.00104.78 C HETATM 5128 C1 OLA A1524 49.613 -96.182 178.813 1.00149.06 C HETATM 5129 O1 OLA A1524 48.789 -95.508 178.158 1.00149.57 O HETATM 5130 O2 OLA A1524 50.016 -95.847 179.948 1.00149.27 O HETATM 5131 C2 OLA A1524 50.135 -97.464 178.210 1.00147.16 C HETATM 5132 C3 OLA A1524 51.645 -97.567 178.406 1.00144.67 C HETATM 5133 C4 OLA A1524 52.142 -98.946 177.985 1.00140.13 C HETATM 5134 C5 OLA A1524 53.655 -98.974 177.789 1.00133.90 C HETATM 5135 C6 OLA A1524 54.402 -99.215 179.096 1.00129.10 C HETATM 5136 C7 OLA A1524 55.893 -99.399 178.831 1.00124.74 C HETATM 5137 C8 OLA A1524 56.626 -99.909 180.068 1.00121.26 C HETATM 5138 C9 OLA A1524 58.050-100.257 179.699 1.00115.71 C HETATM 5139 C10 OLA A1524 59.047-100.065 180.561 1.00109.16 C HETATM 5140 C11 OLA A1524 58.777 -99.498 181.934 1.00103.75 C HETATM 5141 C1 OLA A1525 73.282-125.161 173.534 0.96104.30 C HETATM 5142 O1 OLA A1525 73.387-126.355 173.888 0.96104.70 O HETATM 5143 O2 OLA A1525 74.261-124.477 173.162 0.96104.91 O HETATM 5144 C2 OLA A1525 71.913-124.521 173.557 0.96102.27 C HETATM 5145 C3 OLA A1525 71.951-123.259 174.411 0.96 99.75 C HETATM 5146 C4 OLA A1525 72.307-122.035 173.574 0.96 97.88 C HETATM 5147 C5 OLA A1525 73.089-121.026 174.405 0.96 97.85 C HETATM 5148 C6 OLA A1525 74.467-121.565 174.770 0.96 97.60 C HETATM 5149 C7 OLA A1525 75.167-120.637 175.757 0.96 95.72 C HETATM 5150 C8 OLA A1525 74.416-120.608 177.082 0.96 93.77 C HETATM 5151 C9 OLA A1525 74.770-121.830 177.897 0.96 90.83 C HETATM 5152 C10 OLA A1525 74.692-121.787 179.225 0.96 88.56 C HETATM 5153 C11 OLA A1525 74.245-120.520 179.916 0.96 89.60 C HETATM 5154 C12 OLA A1525 72.968-120.788 180.706 0.96 92.54 C HETATM 5155 C13 OLA A1525 71.898-121.420 179.821 0.96 95.41 C HETATM 5156 C14 OLA A1525 70.575-121.561 180.566 0.96 96.35 C HETATM 5157 C15 OLA A1525 69.727-120.302 180.421 0.96 95.43 C HETATM 5158 C16 OLA A1525 69.134-119.879 181.759 0.96 93.54 C HETATM 5159 C17 OLA A1525 68.394-121.036 182.419 0.96 94.29 C HETATM 5160 C18 OLA A1525 68.002-120.693 183.839 0.96 93.71 C HETATM 5161 C1 OLA A1526 46.935-144.981 173.304 1.00112.70 C HETATM 5162 O1 OLA A1526 47.910-144.213 173.148 1.00112.61 O HETATM 5163 O2 OLA A1526 45.762-144.572 173.447 1.00113.73 O HETATM 5164 C2 OLA A1526 47.191-146.469 173.321 1.00110.18 C HETATM 5165 C3 OLA A1526 48.695-146.697 173.252 1.00107.62 C HETATM 5166 C4 OLA A1526 49.058-148.165 173.435 1.00104.23 C HETATM 5167 C5 OLA A1526 50.564-148.293 173.614 1.00101.15 C HETATM 5168 C6 OLA A1526 51.068-149.683 173.253 1.00 99.86 C HETATM 5169 C7 OLA A1526 52.579-149.638 173.073 1.00 99.59 C HETATM 5170 C8 OLA A1526 53.144-151.013 172.746 1.00 99.24 C HETATM 5171 C9 OLA A1526 52.714-151.460 171.369 1.00 99.72 C HETATM 5172 C10 OLA A1526 53.621-151.623 170.411 1.00 98.75 C HETATM 5173 C11 OLA A1526 55.072-151.327 170.707 1.00 99.40 C HETATM 5174 C12 OLA A1526 55.842-152.620 170.947 1.00 98.12 C HETATM 5175 C13 OLA A1526 57.333-152.343 171.097 1.00 95.89 C HETATM 5176 C14 OLA A1526 57.784-152.351 172.551 1.00 96.64 C HETATM 5177 C15 OLA A1526 57.598-151.010 173.242 1.00 97.37 C HETATM 5178 C16 OLA A1526 56.368-151.027 174.139 1.00 94.19 C HETATM 5179 C17 OLA A1526 56.747-151.107 175.613 1.00 91.01 C HETATM 5180 C18 OLA A1526 57.263-152.475 176.006 1.00 89.07 C HETATM 5181 C ACY A1527 45.780-106.668 239.165 1.00105.50 C HETATM 5182 O ACY A1527 45.747-107.349 238.117 1.00107.80 O HETATM 5183 OXT ACY A1527 46.846-106.195 239.615 1.00105.66 O HETATM 5184 CH3 ACY A1527 44.497-106.387 239.891 1.00101.75 C HETATM 5185 O1 PG4 A1528 53.543 -96.062 152.110 1.00167.14 O HETATM 5186 C1 PG4 A1528 54.317 -97.067 152.775 1.00168.79 C HETATM 5187 C2 PG4 A1528 53.554 -98.385 152.751 1.00169.19 C HETATM 5188 O2 PG4 A1528 52.620 -98.385 153.826 1.00169.59 O HETATM 5189 C3 PG4 A1528 51.324 -98.045 153.348 1.00169.34 C HETATM 5190 C4 PG4 A1528 50.294 -98.097 154.467 1.00169.41 C HETATM 5191 O3 PG4 A1528 49.394 -97.016 154.249 1.00169.27 O HETATM 5192 C5 PG4 A1528 48.026 -97.382 154.406 1.00168.25 C HETATM 5193 C6 PG4 A1528 47.201 -96.299 153.725 1.00166.58 C HETATM 5194 O4 PG4 A1528 47.701 -96.167 152.398 1.00164.76 O HETATM 5195 C7 PG4 A1528 48.177 -94.849 152.141 1.00162.26 C HETATM 5196 C8 PG4 A1528 49.405 -94.947 151.245 1.00160.04 C HETATM 5197 O5 PG4 A1528 49.028 -95.489 149.975 1.00158.89 O HETATM 5198 CL CL A1529 48.730 -98.493 157.524 1.00211.20 CL HETATM 5199 O HOH A1601 55.500-146.147 168.154 1.00 84.58 O HETATM 5200 O HOH A1602 52.013-127.711 260.151 1.00 79.14 O HETATM 5201 O HOH A1603 36.061 -88.476 141.612 1.00 55.52 O HETATM 5202 O HOH A1604 27.068 -98.853 159.217 1.00 41.77 O HETATM 5203 O HOH A1605 72.551-124.726 272.249 1.00114.56 O HETATM 5204 O HOH A1606 38.920-111.358 139.839 1.00 47.27 O HETATM 5205 O HOH A1607 26.293-102.089 158.151 1.00 34.31 O HETATM 5206 O HOH A1608 46.801 -97.400 148.454 1.00 65.46 O HETATM 5207 O HOH A1609 37.708-118.349 159.279 1.00 51.27 O HETATM 5208 O HOH A1610 44.764-113.520 164.606 1.00 45.38 O HETATM 5209 O HOH A1611 26.192 -95.131 133.879 1.00 54.80 O HETATM 5210 O HOH A1612 18.292-111.100 144.232 1.00 56.30 O HETATM 5211 O HOH A1613 54.634-122.866 249.014 1.00 35.21 O HETATM 5212 O HOH A1614 45.172-119.109 149.250 1.00 66.19 O HETATM 5213 O HOH A1615 32.593-103.442 157.009 1.00 43.65 O HETATM 5214 O HOH A1616 48.156-135.768 174.637 1.00 87.23 O HETATM 5215 O HOH A1617 57.138-108.259 166.487 1.00 71.33 O HETATM 5216 O HOH A1618 40.225-112.253 137.485 1.00 44.53 O HETATM 5217 O HOH A1619 59.918-120.922 257.236 1.00 63.34 O HETATM 5218 O HOH A1620 15.783-106.075 144.298 1.00 64.02 O HETATM 5219 O HOH A1621 55.008-114.148 177.785 1.00 55.07 O HETATM 5220 O HOH A1622 50.965-123.753 254.285 1.00 59.57 O HETATM 5221 O HOH A1623 45.494-123.993 153.943 1.00 54.78 O HETATM 5222 O HOH A1624 27.359-121.268 246.875 1.00 86.40 O HETATM 5223 O HOH A1625 42.881-119.243 140.973 1.00 61.77 O HETATM 5224 O HOH A1626 58.501-121.027 262.535 1.00 66.84 O HETATM 5225 O HOH A1627 52.602-114.931 196.408 1.00 56.22 O HETATM 5226 O HOH A1628 43.993-120.948 138.618 1.00 73.30 O HETATM 5227 O HOH A1629 53.550-109.451 188.609 1.00 63.98 O HETATM 5228 O HOH A1630 24.970 -89.425 141.419 1.00 53.53 O HETATM 5229 O HOH A1631 40.468-110.199 172.301 1.00 54.49 O HETATM 5230 O HOH A1632 56.365-125.311 257.581 1.00 49.65 O HETATM 5231 O HOH A1633 54.904 -97.754 149.684 1.00 69.17 O HETATM 5232 O HOH A1634 20.565-105.880 138.897 1.00 44.44 O HETATM 5233 O HOH A1635 44.920-120.415 244.303 1.00 49.90 O HETATM 5234 O HOH A1636 39.256 -93.930 159.119 1.00 70.16 O HETATM 5235 O HOH A1637 27.915-104.681 163.574 1.00 55.36 O HETATM 5236 O HOH A1638 62.047-119.178 256.839 1.00 58.38 O HETATM 5237 O HOH A1639 32.623-106.287 156.245 1.00 47.69 O HETATM 5238 O HOH A1640 45.984-128.960 264.198 1.00 69.91 O HETATM 5239 O HOH A1641 48.200-130.545 267.194 1.00 86.03 O HETATM 5240 O HOH A1642 60.492-125.347 257.171 1.00 77.67 O HETATM 5241 O HOH A1643 48.494-125.918 243.978 1.00 55.24 O HETATM 5242 O HOH A1644 32.912-106.855 153.129 1.00 42.78 O HETATM 5243 O HOH A1645 19.256 -94.351 144.170 1.00 64.19 O HETATM 5244 O HOH A1646 47.152-111.929 233.059 1.00 79.13 O HETATM 5245 O HOH A1647 60.140-111.709 245.756 1.00 48.99 O HETATM 5246 O HOH A1648 59.865-142.678 264.653 1.00 91.20 O HETATM 5247 O HOH A1649 63.072-131.876 254.959 1.00 54.44 O HETATM 5248 O HOH A1650 57.291-122.783 259.209 1.00 63.17 O HETATM 5249 O HOH A1651 58.427-120.349 259.636 1.00 49.21 O HETATM 5250 O HOH A1652 42.403-126.808 244.503 1.00 81.57 O HETATM 5251 O HOH A1653 58.082-104.893 253.966 1.00 77.59 O HETATM 5252 O HOH A1654 21.054-114.960 142.357 1.00 74.66 O HETATM 5253 O HOH A1655 37.169-109.680 162.703 1.00 62.99 O HETATM 5254 O HOH A1656 35.967-126.854 151.843 1.00 52.50 O HETATM 5255 O HOH A1657 55.238-126.011 268.963 1.00 76.52 O HETATM 5256 O HOH A1658 28.962-122.648 156.108 1.00 65.70 O HETATM 5257 O HOH A1659 44.666-110.917 165.998 1.00 50.13 O HETATM 5258 O HOH A1660 59.483-129.632 262.361 1.00 52.51 O HETATM 5259 O HOH A1661 53.229-108.790 150.851 1.00 57.70 O HETATM 5260 O HOH A1662 14.510-107.309 157.141 1.00 75.27 O HETATM 5261 O HOH A1663 18.283-104.559 137.520 1.00 76.00 O HETATM 5262 O HOH A1664 45.977-109.824 241.794 1.00 74.91 O HETATM 5263 O HOH A1665 29.377-108.355 160.071 1.00 38.45 O HETATM 5264 O HOH A1666 36.134-123.868 141.861 1.00 76.77 O HETATM 5265 O HOH A1667 52.904-113.981 267.445 1.00 57.38 O HETATM 5266 O HOH A1668 65.384-125.914 252.205 1.00 55.70 O HETATM 5267 O HOH A1669 24.547-120.908 150.529 1.00 79.42 O HETATM 5268 O HOH A1670 56.210-122.432 194.154 1.00 61.66 O HETATM 5269 O HOH A1671 18.667-112.417 146.483 1.00 71.75 O HETATM 5270 O HOH A1672 13.055-101.614 146.821 1.00 63.61 O HETATM 5271 O HOH A1673 54.038-127.109 264.441 1.00 71.10 O HETATM 5272 O HOH A1674 14.221 -98.893 143.026 1.00 65.39 O HETATM 5273 O HOH A1675 55.504-143.586 271.100 1.00 63.43 O HETATM 5274 O HOH A1676 39.271-102.945 133.270 1.00 70.30 O HETATM 5275 O HOH A1677 44.264-117.749 138.321 1.00 53.98 O HETATM 5276 O HOH A1678 47.469-114.754 231.641 1.00 54.84 O HETATM 5277 O HOH A1679 41.847-122.213 250.141 1.00 81.29 O HETATM 5278 O HOH A1680 64.460-121.364 242.854 1.00 72.66 O HETATM 5279 O HOH A1681 23.768 -99.982 135.025 1.00 52.79 O HETATM 5280 O HOH A1682 44.212 -93.931 149.308 1.00 64.77 O HETATM 5281 O HOH A1683 21.860 -99.742 163.417 1.00 69.13 O HETATM 5282 O HOH A1684 23.773-111.394 130.472 1.00 87.24 O HETATM 5283 O HOH A1685 43.035-106.238 131.168 1.00 89.01 O HETATM 5284 O HOH A1686 23.095 -94.243 158.848 1.00 66.83 O HETATM 5285 O HOH A1687 58.548-128.714 259.640 1.00 63.66 O HETATM 5286 O HOH A1688 44.227-112.324 138.148 1.00 69.94 O HETATM 5287 O HOH A1689 44.531-145.950 176.296 1.00 88.87 O HETATM 5288 O HOH A1690 68.704-129.212 266.181 1.00 70.00 O HETATM 5289 O HOH A1691 53.642-115.653 153.371 1.00 63.32 O HETATM 5290 O HOH A1692 32.930-119.435 240.431 1.00 94.67 O HETATM 5291 O HOH A1693 16.349-113.991 151.493 1.00 68.04 O HETATM 5292 O HOH A1694 25.805-106.173 133.950 1.00 53.16 O HETATM 5293 O HOH A1695 61.421-126.056 260.933 1.00 94.66 O HETATM 5294 O HOH A1696 48.057 -98.953 172.711 1.00 63.59 O HETATM 5295 O HOH A1697 49.570-114.024 196.800 1.00 73.91 O HETATM 5296 O HOH A1698 35.658-123.202 133.911 1.00 77.71 O HETATM 5297 O HOH A1699 45.095 -95.838 140.019 1.00 49.42 O HETATM 5298 O HOH A1700 65.467-122.360 260.778 1.00 82.66 O HETATM 5299 O HOH A1701 37.875-121.898 251.613 1.00 81.72 O HETATM 5300 O HOH A1702 54.881-141.187 248.291 1.00 72.60 O HETATM 5301 O HOH A1703 50.009-111.495 199.142 1.00100.72 O HETATM 5302 O HOH A1704 31.117 -94.528 164.775 1.00 54.36 O HETATM 5303 O HOH A1705 33.145-107.358 159.080 1.00 52.16 O HETATM 5304 O HOH A1706 20.557-116.258 135.398 1.00 82.30 O HETATM 5305 O HOH A1707 15.588-106.316 141.075 1.00 62.56 O HETATM 5306 O HOH A1708 14.299-105.554 151.518 1.00 59.13 O HETATM 5307 O HOH A1709 41.600-113.498 249.261 1.00 74.40 O HETATM 5308 O HOH A1710 50.151-109.182 228.253 1.00 70.79 O HETATM 5309 O HOH A1711 51.683-128.536 247.786 1.00 66.20 O HETATM 5310 O HOH A1712 41.370 -93.656 147.620 1.00 74.62 O HETATM 5311 O HOH A1713 56.645-117.638 145.240 1.00 92.37 O HETATM 5312 O HOH A1714 26.994-111.560 156.721 1.00 60.88 O HETATM 5313 O HOH A1715 50.744 -99.334 172.280 1.00 63.11 O HETATM 5314 O HOH A1716 22.070 -97.903 135.312 1.00 63.64 O HETATM 5315 O HOH A1717 38.072-127.377 155.808 1.00 89.95 O HETATM 5316 O HOH A1718 49.767-140.668 172.549 1.00 85.01 O HETATM 5317 O HOH A1719 57.547-107.795 145.654 1.00 80.47 O HETATM 5318 O HOH A1720 28.765-107.524 162.918 1.00 46.41 O HETATM 5319 O HOH A1721 51.789-126.846 245.095 1.00 56.31 O HETATM 5320 O HOH A1722 33.723-117.071 241.888 1.00 96.99 O HETATM 5321 O HOH A1723 48.370-126.530 270.388 1.00 84.66 O HETATM 5322 O HOH A1724 19.515-114.293 136.626 1.00 66.87 O HETATM 5323 O HOH A1725 12.203 -93.730 158.099 1.00 74.97 O HETATM 5324 O HOH A1726 58.946-141.584 165.124 1.00104.44 O HETATM 5325 O HOH A1727 26.329 -92.695 131.624 1.00 71.26 O HETATM 5326 O HOH A1728 64.179-105.537 246.718 1.00 68.74 O HETATM 5327 O HOH A1729 23.074 -91.752 134.049 1.00 75.64 O HETATM 5328 O HOH A1730 19.845-109.988 161.595 1.00 50.25 O HETATM 5329 O HOH A1731 25.717-122.266 141.527 1.00 77.13 O HETATM 5330 O HOH A1732 58.883-123.016 266.157 1.00 88.40 O HETATM 5331 O HOH A1733 51.246-144.098 178.540 1.00 73.76 O HETATM 5332 O HOH A1734 19.097-108.384 137.196 1.00 72.00 O HETATM 5333 O HOH A1735 38.937-122.334 231.557 1.00 74.44 O HETATM 5334 O HOH A1736 60.864-101.623 248.855 1.00 79.01 O HETATM 5335 O HOH A1737 67.025-125.379 241.873 1.00 72.94 O HETATM 5336 O HOH A1738 73.755-106.229 174.408 1.00 70.88 O HETATM 5337 O HOH A1739 60.493-123.765 268.194 1.00 75.61 O HETATM 5338 O HOH A1740 62.365-121.221 261.801 1.00 68.46 O HETATM 5339 O HOH A1741 79.166-127.424 174.715 1.00 88.62 O HETATM 5340 O HOH A1742 38.878-105.693 178.720 1.00 75.27 O HETATM 5341 O HOH A1743 40.062-118.956 179.169 1.00 79.35 O HETATM 5342 O HOH A1744 76.233-106.949 211.920 1.00 80.09 O HETATM 5343 O HOH A1745 32.767-110.403 245.706 1.00 84.81 O HETATM 5344 O HOH A1746 47.340-141.980 182.071 1.00 87.77 O HETATM 5345 O HOH A1747 47.658-136.438 183.971 1.00 70.04 O HETATM 5346 O HOH A1748 42.655-139.689 181.940 1.00 94.56 O HETATM 5347 O HOH B 101 54.633-125.722 248.003 1.00 42.16 O HETATM 5348 O HOH B 102 54.117-128.186 229.121 1.00 73.98 O HETATM 5349 O HOH B 103 62.932-126.840 237.711 1.00 67.32 O HETATM 5350 O HOH B 104 65.263-123.735 235.371 1.00 89.59 O HETATM 5351 O HOH B 105 48.431-130.625 233.805 1.00 72.35 O HETATM 5352 O HOH B 106 58.787-136.617 244.285 1.00 63.96 O HETATM 5353 O HOH B 107 51.612-126.642 242.522 1.00 65.52 O HETATM 5354 O HOH B 108 55.416-136.682 230.219 1.00 74.17 O CONECT 148 356 CONECT 278 605 CONECT 356 148 CONECT 453 787 CONECT 605 278 CONECT 632 4971 CONECT 709 4851 CONECT 754 4922 CONECT 787 453 CONECT 1434 2020 CONECT 2020 1434 CONECT 2333 2339 CONECT 2339 2333 2340 CONECT 2340 2339 2341 2347 CONECT 2341 2340 2342 CONECT 2342 2341 2343 CONECT 2343 2342 2344 CONECT 2344 2343 2345 2346 CONECT 2345 2344 CONECT 2346 2344 CONECT 2347 2340 2348 2349 CONECT 2348 2347 CONECT 2349 2347 CONECT 4548 4550 CONECT 4549 4551 CONECT 4550 4548 4551 4552 4553 CONECT 4551 4549 4550 4556 CONECT 4552 4550 4554 CONECT 4553 4550 4555 CONECT 4554 4552 4555 CONECT 4555 4553 4554 CONECT 4556 4551 CONECT 4558 4563 CONECT 4563 4558 4564 CONECT 4564 4563 4565 4567 4568 CONECT 4565 4564 4566 4569 CONECT 4566 4565 CONECT 4567 4564 CONECT 4568 4564 CONECT 4569 4565 CONECT 4623 4630 CONECT 4630 4623 4631 CONECT 4631 4630 4632 4640 CONECT 4632 4631 4634 CONECT 4633 4634 4635 CONECT 4634 4632 4633 CONECT 4635 4633 4636 CONECT 4636 4635 4637 CONECT 4637 4636 4638 4639 CONECT 4638 4637 CONECT 4639 4637 CONECT 4640 4631 4641 4642 CONECT 4641 4640 CONECT 4642 4640 CONECT 4688 4692 CONECT 4692 4688 4693 CONECT 4693 4692 4694 4696 CONECT 4694 4693 4695 4700 CONECT 4695 4694 CONECT 4696 4693 4697 CONECT 4697 4696 4698 CONECT 4698 4697 4699 CONECT 4699 4698 CONECT 4700 4694 CONECT 4851 709 4852 4862 CONECT 4852 4851 4853 4859 CONECT 4853 4852 4854 4860 CONECT 4854 4853 4855 4861 CONECT 4855 4854 4856 4862 CONECT 4856 4855 4863 CONECT 4857 4858 4859 4864 CONECT 4858 4857 CONECT 4859 4852 4857 CONECT 4860 4853 CONECT 4861 4854 4865 CONECT 4862 4851 4855 CONECT 4863 4856 4912 CONECT 4864 4857 CONECT 4865 4861 4866 4876 CONECT 4866 4865 4867 4873 CONECT 4867 4866 4868 4874 CONECT 4868 4867 4869 4875 CONECT 4869 4868 4870 4876 CONECT 4870 4869 4877 CONECT 4871 4872 4873 4878 CONECT 4872 4871 CONECT 4873 4866 4871 CONECT 4874 4867 CONECT 4875 4868 4879 CONECT 4876 4865 4869 CONECT 4877 4870 CONECT 4878 4871 CONECT 4879 4875 4880 4888 CONECT 4880 4879 4881 4885 CONECT 4881 4880 4882 4886 CONECT 4882 4881 4883 4887 CONECT 4883 4882 4884 4888 CONECT 4884 4883 4889 CONECT 4885 4880 CONECT 4886 4881 4890 CONECT 4887 4882 CONECT 4888 4879 4883 CONECT 4889 4884 4901 CONECT 4890 4886 4891 4899 CONECT 4891 4890 4892 4896 CONECT 4892 4891 4893 4897 CONECT 4893 4892 4894 4898 CONECT 4894 4893 4895 4899 CONECT 4895 4894 4900 CONECT 4896 4891 CONECT 4897 4892 CONECT 4898 4893 CONECT 4899 4890 4894 CONECT 4900 4895 CONECT 4901 4889 4902 4910 CONECT 4902 4901 4903 4907 CONECT 4903 4902 4904 4908 CONECT 4904 4903 4905 4909 CONECT 4905 4904 4906 4910 CONECT 4906 4905 4911 CONECT 4907 4902 CONECT 4908 4903 CONECT 4909 4904 CONECT 4910 4901 4905 CONECT 4911 4906 CONECT 4912 4863 4913 4921 CONECT 4913 4912 4914 4918 CONECT 4914 4913 4915 4919 CONECT 4915 4914 4916 4920 CONECT 4916 4915 4917 4921 CONECT 4917 4916 CONECT 4918 4913 CONECT 4919 4914 CONECT 4920 4915 CONECT 4921 4912 4916 CONECT 4922 754 4923 4933 CONECT 4923 4922 4924 4930 CONECT 4924 4923 4925 4931 CONECT 4925 4924 4926 4932 CONECT 4926 4925 4927 4933 CONECT 4927 4926 4934 CONECT 4928 4929 4930 4935 CONECT 4929 4928 CONECT 4930 4923 4928 CONECT 4931 4924 CONECT 4932 4925 4936 CONECT 4933 4922 4926 CONECT 4934 4927 4961 CONECT 4935 4928 CONECT 4936 4932 4937 4947 CONECT 4937 4936 4938 4944 CONECT 4938 4937 4939 4945 CONECT 4939 4938 4940 4946 CONECT 4940 4939 4941 4947 CONECT 4941 4940 4948 CONECT 4942 4943 4944 4949 CONECT 4943 4942 CONECT 4944 4937 4942 CONECT 4945 4938 CONECT 4946 4939 4950 CONECT 4947 4936 4940 CONECT 4948 4941 CONECT 4949 4942 CONECT 4950 4946 4951 4959 CONECT 4951 4950 4952 4956 CONECT 4952 4951 4953 4957 CONECT 4953 4952 4954 4958 CONECT 4954 4953 4955 4959 CONECT 4955 4954 4960 CONECT 4956 4951 CONECT 4957 4952 CONECT 4958 4953 CONECT 4959 4950 4954 CONECT 4960 4955 CONECT 4961 4934 4962 4970 CONECT 4962 4961 4963 4967 CONECT 4963 4962 4964 4968 CONECT 4964 4963 4965 4969 CONECT 4965 4964 4966 4970 CONECT 4966 4965 CONECT 4967 4962 CONECT 4968 4963 CONECT 4969 4964 CONECT 4970 4961 4965 CONECT 4971 632 4972 4982 CONECT 4972 4971 4973 4979 CONECT 4973 4972 4974 4980 CONECT 4974 4973 4975 4981 CONECT 4975 4974 4976 4982 CONECT 4976 4975 4983 CONECT 4977 4978 4979 4984 CONECT 4978 4977 CONECT 4979 4972 4977 CONECT 4980 4973 CONECT 4981 4974 4985 CONECT 4982 4971 4975 CONECT 4983 4976 CONECT 4984 4977 CONECT 4985 4981 4986 4996 CONECT 4986 4985 4987 4993 CONECT 4987 4986 4988 4994 CONECT 4988 4987 4989 4995 CONECT 4989 4988 4990 4996 CONECT 4990 4989 4997 CONECT 4991 4992 4993 4998 CONECT 4992 4991 CONECT 4993 4986 4991 CONECT 4994 4987 CONECT 4995 4988 4999 CONECT 4996 4985 4989 CONECT 4997 4990 CONECT 4998 4991 CONECT 4999 4995 5000 5008 CONECT 5000 4999 5001 5005 CONECT 5001 5000 5002 5006 CONECT 5002 5001 5003 5007 CONECT 5003 5002 5004 5008 CONECT 5004 5003 5009 CONECT 5005 5000 CONECT 5006 5001 CONECT 5007 5002 CONECT 5008 4999 5003 CONECT 5009 5004 5010 CONECT 5010 5009 5011 5019 CONECT 5011 5010 5012 5016 CONECT 5012 5011 5013 5017 CONECT 5013 5012 5014 5018 CONECT 5014 5013 5015 5019 CONECT 5015 5014 5020 CONECT 5016 5011 CONECT 5017 5012 CONECT 5018 5013 CONECT 5019 5010 5014 CONECT 5020 5015 CONECT 5021 5022 5030 CONECT 5022 5021 5023 5027 CONECT 5023 5022 5024 5028 CONECT 5024 5023 5025 5029 CONECT 5025 5024 5026 5030 CONECT 5026 5025 5031 CONECT 5027 5022 CONECT 5028 5023 CONECT 5029 5024 CONECT 5030 5021 5025 CONECT 5031 5026 CONECT 5032 5033 5041 CONECT 5033 5032 5034 5038 CONECT 5034 5033 5035 5039 CONECT 5035 5034 5036 5040 CONECT 5036 5035 5037 5041 CONECT 5037 5036 5042 CONECT 5038 5033 CONECT 5039 5034 CONECT 5040 5035 CONECT 5041 5032 5036 CONECT 5042 5037 CONECT 5043 5044 5052 CONECT 5044 5043 5045 5049 CONECT 5045 5044 5046 5050 CONECT 5046 5045 5047 5051 CONECT 5047 5046 5048 5052 CONECT 5048 5047 5053 CONECT 5049 5044 CONECT 5050 5045 CONECT 5051 5046 CONECT 5052 5043 5047 CONECT 5053 5048 CONECT 5054 5055 5056 5057 CONECT 5055 5054 CONECT 5056 5054 CONECT 5057 5054 5058 CONECT 5058 5057 5059 CONECT 5059 5058 5060 CONECT 5060 5059 5061 CONECT 5061 5060 5062 CONECT 5062 5061 CONECT 5063 5064 5065 5066 CONECT 5064 5063 CONECT 5065 5063 CONECT 5066 5063 5067 CONECT 5067 5066 5068 CONECT 5068 5067 5069 CONECT 5069 5068 5070 CONECT 5070 5069 5071 CONECT 5071 5070 5072 CONECT 5072 5071 5073 CONECT 5073 5072 CONECT 5074 5075 CONECT 5075 5074 5076 CONECT 5076 5075 5077 CONECT 5077 5076 5078 CONECT 5078 5077 5079 CONECT 5079 5078 5080 CONECT 5080 5079 CONECT 5081 5082 5083 5084 CONECT 5082 5081 CONECT 5083 5081 CONECT 5084 5081 5085 CONECT 5085 5084 5086 CONECT 5086 5085 5087 CONECT 5087 5086 5088 CONECT 5088 5087 5089 CONECT 5089 5088 5090 CONECT 5090 5089 5091 CONECT 5091 5090 5092 CONECT 5092 5091 5093 CONECT 5093 5092 5094 CONECT 5094 5093 5095 CONECT 5095 5094 5096 CONECT 5096 5095 5097 CONECT 5097 5096 5098 CONECT 5098 5097 5099 CONECT 5099 5098 5100 CONECT 5100 5099 CONECT 5101 5102 5103 5104 CONECT 5102 5101 CONECT 5103 5101 CONECT 5104 5101 5105 CONECT 5105 5104 5106 CONECT 5106 5105 5107 CONECT 5107 5106 5108 CONECT 5108 5107 5109 CONECT 5109 5108 5110 CONECT 5110 5109 5111 CONECT 5111 5110 5112 CONECT 5112 5111 5113 CONECT 5113 5112 5114 CONECT 5114 5113 5115 CONECT 5115 5114 5116 CONECT 5116 5115 5117 CONECT 5117 5116 5118 CONECT 5118 5117 5119 CONECT 5119 5118 5120 CONECT 5120 5119 CONECT 5121 5122 CONECT 5122 5121 5123 CONECT 5123 5122 5124 CONECT 5124 5123 5125 CONECT 5125 5124 5126 CONECT 5126 5125 5127 CONECT 5127 5126 CONECT 5128 5129 5130 5131 CONECT 5129 5128 CONECT 5130 5128 CONECT 5131 5128 5132 CONECT 5132 5131 5133 CONECT 5133 5132 5134 CONECT 5134 5133 5135 CONECT 5135 5134 5136 CONECT 5136 5135 5137 CONECT 5137 5136 5138 CONECT 5138 5137 5139 CONECT 5139 5138 5140 CONECT 5140 5139 CONECT 5141 5142 5143 5144 CONECT 5142 5141 CONECT 5143 5141 CONECT 5144 5141 5145 CONECT 5145 5144 5146 CONECT 5146 5145 5147 CONECT 5147 5146 5148 CONECT 5148 5147 5149 CONECT 5149 5148 5150 CONECT 5150 5149 5151 CONECT 5151 5150 5152 CONECT 5152 5151 5153 CONECT 5153 5152 5154 CONECT 5154 5153 5155 CONECT 5155 5154 5156 CONECT 5156 5155 5157 CONECT 5157 5156 5158 CONECT 5158 5157 5159 CONECT 5159 5158 5160 CONECT 5160 5159 CONECT 5161 5162 5163 5164 CONECT 5162 5161 CONECT 5163 5161 CONECT 5164 5161 5165 CONECT 5165 5164 5166 CONECT 5166 5165 5167 CONECT 5167 5166 5168 CONECT 5168 5167 5169 CONECT 5169 5168 5170 CONECT 5170 5169 5171 CONECT 5171 5170 5172 CONECT 5172 5171 5173 CONECT 5173 5172 5174 CONECT 5174 5173 5175 CONECT 5175 5174 5176 CONECT 5176 5175 5177 CONECT 5177 5176 5178 CONECT 5178 5177 5179 CONECT 5179 5178 5180 CONECT 5180 5179 CONECT 5181 5182 5183 5184 CONECT 5182 5181 CONECT 5183 5181 CONECT 5184 5181 CONECT 5185 5186 CONECT 5186 5185 5187 CONECT 5187 5186 5188 CONECT 5188 5187 5189 CONECT 5189 5188 5190 CONECT 5190 5189 5191 CONECT 5191 5190 5192 CONECT 5192 5191 5193 CONECT 5193 5192 5194 CONECT 5194 5193 5195 CONECT 5195 5194 5196 CONECT 5196 5195 5197 CONECT 5197 5196 MASTER 392 0 35 22 8 0 0 6 5344 2 411 50 END