HEADER MEMBRANE PROTEIN/INHIBITOR 23-MAR-18 5ZKC TITLE CRYSTAL STRUCTURE OF RATIONALLY THERMOSTABILIZED M2 MUSCARINIC TITLE 2 ACETYLCHOLINE RECEPTOR BOUND WITH NMS COMPND MOL_ID: 1; COMPND 2 MOLECULE: MUSCARINIC ACETYLCHOLINE RECEPTOR M2,APO-CYTOCHROME B562, COMPND 3 MUSCARINIC ACETYLCHOLINE RECEPTOR M2; COMPND 4 CHAIN: A; COMPND 5 FRAGMENT: UNP RESIDUES 10-217,UNP RESIDUES 377-466; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: CHRM2; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS GPCR CRYSTALLOGRAPHY, RATIONALLY THERMOSTABILIZED MUTANT, MEMBRANE KEYWDS 2 PROTEIN-INHIBITOR COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR R.SUNO,S.MAEDA,S.YASUDA,K.YAMASHITA,K.HIRATA,S.HORITA,M.S.TAWARAMOTO, AUTHOR 2 H.TSUJIMOTO,T.MURATA,M.KINOSHITA,M.YAMAMOTO,B.K.KOBILKA,S.IWATA, AUTHOR 3 T.KOBAYASHI REVDAT 3 23-MAR-22 5ZKC 1 REMARK REVDAT 2 28-NOV-18 5ZKC 1 JRNL REVDAT 1 21-NOV-18 5ZKC 0 JRNL AUTH R.SUNO,S.LEE,S.MAEDA,S.YASUDA,K.YAMASHITA,K.HIRATA,S.HORITA, JRNL AUTH 2 M.S.TAWARAMOTO,H.TSUJIMOTO,T.MURATA,M.KINOSHITA,M.YAMAMOTO, JRNL AUTH 3 B.K.KOBILKA,N.VAIDEHI,S.IWATA,T.KOBAYASHI JRNL TITL STRUCTURAL INSIGHTS INTO THE SUBTYPE-SELECTIVE ANTAGONIST JRNL TITL 2 BINDING TO THE M2MUSCARINIC RECEPTOR JRNL REF NAT. CHEM. BIOL. V. 14 1150 2018 JRNL REFN ESSN 1552-4469 JRNL PMID 30420692 JRNL DOI 10.1038/S41589-018-0152-Y REMARK 2 REMARK 2 RESOLUTION. 2.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.11.1_2575: ???) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.97 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 21307 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.233 REMARK 3 R VALUE (WORKING SET) : 0.231 REMARK 3 FREE R VALUE : 0.259 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.360 REMARK 3 FREE R VALUE TEST SET COUNT : 1142 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 48.9793 - 4.5990 1.00 2590 144 0.2261 0.2573 REMARK 3 2 4.5990 - 3.6507 1.00 2523 143 0.2112 0.2306 REMARK 3 3 3.6507 - 3.1893 1.00 2540 145 0.2251 0.2626 REMARK 3 4 3.1893 - 2.8978 1.00 2469 142 0.2290 0.2622 REMARK 3 5 2.8978 - 2.6901 1.00 2508 142 0.2251 0.2355 REMARK 3 6 2.6901 - 2.5315 1.00 2528 142 0.2451 0.2848 REMARK 3 7 2.5315 - 2.4047 1.00 2493 141 0.2814 0.2849 REMARK 3 8 2.4047 - 2.3000 1.00 2514 143 0.3032 0.3421 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.260 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.780 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.002 3151 REMARK 3 ANGLE : 0.489 4302 REMARK 3 CHIRALITY : 0.035 512 REMARK 3 PLANARITY : 0.004 520 REMARK 3 DIHEDRAL : 12.260 1892 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 9 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 16 THROUGH 92 ) REMARK 3 ORIGIN FOR THE GROUP (A): 171.8130 35.8617 531.8383 REMARK 3 T TENSOR REMARK 3 T11: 0.2072 T22: 0.1617 REMARK 3 T33: 0.2805 T12: 0.0301 REMARK 3 T13: 0.0408 T23: -0.0208 REMARK 3 L TENSOR REMARK 3 L11: 4.4863 L22: 2.5421 REMARK 3 L33: 8.5729 L12: -0.9463 REMARK 3 L13: 1.3030 L23: -0.8786 REMARK 3 S TENSOR REMARK 3 S11: 0.0049 S12: 0.0355 S13: -0.0721 REMARK 3 S21: 0.1706 S22: 0.1376 S23: 0.1044 REMARK 3 S31: 0.1034 S32: -0.0978 S33: -0.1599 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 93 THROUGH 195 ) REMARK 3 ORIGIN FOR THE GROUP (A): 189.7611 31.8193 530.4989 REMARK 3 T TENSOR REMARK 3 T11: 0.1821 T22: 0.4482 REMARK 3 T33: 0.3035 T12: -0.0357 REMARK 3 T13: -0.0356 T23: -0.0244 REMARK 3 L TENSOR REMARK 3 L11: 1.7905 L22: 2.6826 REMARK 3 L33: 2.3481 L12: -0.2684 REMARK 3 L13: -0.0712 L23: -0.5793 REMARK 3 S TENSOR REMARK 3 S11: -0.0551 S12: -0.1295 S13: 0.0349 REMARK 3 S21: 0.2217 S22: -0.0124 S23: -0.2434 REMARK 3 S31: -0.1046 S32: 0.4129 S33: 0.0971 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 196 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): 187.7565 14.8786 541.4810 REMARK 3 T TENSOR REMARK 3 T11: 0.2964 T22: 0.5534 REMARK 3 T33: 0.3708 T12: 0.0948 REMARK 3 T13: -0.0585 T23: -0.0588 REMARK 3 L TENSOR REMARK 3 L11: 7.2269 L22: 6.7781 REMARK 3 L33: 3.4702 L12: -1.2042 REMARK 3 L13: -3.1763 L23: 3.6394 REMARK 3 S TENSOR REMARK 3 S11: -0.9035 S12: -1.3540 S13: -0.1478 REMARK 3 S21: 0.6647 S22: -0.3840 S23: -0.4647 REMARK 3 S31: 0.6909 S32: -0.3472 S33: 1.0775 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND ((RESID 214 THROUGH 214) OR (RESID REMARK 3 1001 THROUGH 1018 )) REMARK 3 ORIGIN FOR THE GROUP (A): 171.9055 15.8716 563.4619 REMARK 3 T TENSOR REMARK 3 T11: 1.0218 T22: 1.9318 REMARK 3 T33: 0.6803 T12: 0.1257 REMARK 3 T13: -0.0541 T23: 0.3266 REMARK 3 L TENSOR REMARK 3 L11: 1.0509 L22: 2.9063 REMARK 3 L33: 5.1268 L12: 1.0511 REMARK 3 L13: -1.5428 L23: 0.7472 REMARK 3 S TENSOR REMARK 3 S11: -0.5003 S12: -0.4415 S13: 0.0597 REMARK 3 S21: -0.2656 S22: 0.5590 S23: -0.7316 REMARK 3 S31: 1.1439 S32: 2.2922 S33: -0.0639 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1019 THROUGH 1055 ) REMARK 3 ORIGIN FOR THE GROUP (A): 171.4250 12.3077 570.4895 REMARK 3 T TENSOR REMARK 3 T11: 1.3507 T22: 1.6316 REMARK 3 T33: 0.8169 T12: 0.0703 REMARK 3 T13: -0.0140 T23: 0.1404 REMARK 3 L TENSOR REMARK 3 L11: 5.2595 L22: 2.4955 REMARK 3 L33: 5.4633 L12: -0.1124 REMARK 3 L13: 4.4032 L23: 0.0103 REMARK 3 S TENSOR REMARK 3 S11: 0.1211 S12: -0.6433 S13: -1.1444 REMARK 3 S21: -0.6876 S22: 0.4032 S23: -0.4829 REMARK 3 S31: 0.7470 S32: 0.2598 S33: -0.4195 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1056 THROUGH 1080 ) REMARK 3 ORIGIN FOR THE GROUP (A): 166.7022 13.3331 577.8029 REMARK 3 T TENSOR REMARK 3 T11: 1.5098 T22: 2.9963 REMARK 3 T33: 1.0466 T12: -0.4062 REMARK 3 T13: -0.3360 T23: 0.8121 REMARK 3 L TENSOR REMARK 3 L11: 8.4646 L22: 1.7776 REMARK 3 L33: 0.5842 L12: -2.2148 REMARK 3 L13: 1.4012 L23: 0.0260 REMARK 3 S TENSOR REMARK 3 S11: -0.7173 S12: 0.0577 S13: 0.2876 REMARK 3 S21: -0.8363 S22: 0.9756 S23: 0.1856 REMARK 3 S31: 1.7112 S32: -1.2770 S33: -0.1062 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'A' AND ((RESID 1081 THROUGH 1106) OR (RESID REMARK 3 380 THROUGH 380) ) REMARK 3 ORIGIN FOR THE GROUP (A): 164.4302 21.0155 572.3787 REMARK 3 T TENSOR REMARK 3 T11: 1.1196 T22: 1.6203 REMARK 3 T33: 0.8327 T12: -0.1266 REMARK 3 T13: 0.0215 T23: 0.1347 REMARK 3 L TENSOR REMARK 3 L11: 3.7031 L22: 3.0195 REMARK 3 L33: 7.6547 L12: 0.5177 REMARK 3 L13: 4.7513 L23: 2.4197 REMARK 3 S TENSOR REMARK 3 S11: 0.4825 S12: -3.0725 S13: -0.4976 REMARK 3 S21: 0.6546 S22: -0.1317 S23: 0.1508 REMARK 3 S31: -0.1908 S32: -1.4054 S33: -0.6921 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 381 THROUGH 411 ) REMARK 3 ORIGIN FOR THE GROUP (A): 179.6785 19.9640 535.4091 REMARK 3 T TENSOR REMARK 3 T11: 0.1404 T22: 0.2323 REMARK 3 T33: 0.2533 T12: 0.0069 REMARK 3 T13: -0.0544 T23: 0.0084 REMARK 3 L TENSOR REMARK 3 L11: 4.5410 L22: 5.9171 REMARK 3 L33: 4.4787 L12: 0.2930 REMARK 3 L13: 0.1259 L23: 1.0342 REMARK 3 S TENSOR REMARK 3 S11: 0.0705 S12: -0.5650 S13: -0.0184 REMARK 3 S21: 0.4134 S22: 0.1444 S23: 0.0213 REMARK 3 S31: -0.4007 S32: 0.4879 S33: -0.1634 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 412 THROUGH 458 ) REMARK 3 ORIGIN FOR THE GROUP (A): 171.6825 29.0350 534.9498 REMARK 3 T TENSOR REMARK 3 T11: 0.2220 T22: 0.4168 REMARK 3 T33: 0.3469 T12: -0.0487 REMARK 3 T13: -0.0372 T23: 0.0654 REMARK 3 L TENSOR REMARK 3 L11: 2.3862 L22: 6.3501 REMARK 3 L33: 8.0387 L12: -1.3941 REMARK 3 L13: -1.9143 L23: 5.0541 REMARK 3 S TENSOR REMARK 3 S11: -0.1472 S12: -0.2645 S13: 0.0177 REMARK 3 S21: 0.5157 S22: -0.1373 S23: 0.3064 REMARK 3 S31: 0.2769 S32: -0.2467 S33: 0.3203 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 5ZKC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-MAR-18. REMARK 100 THE DEPOSITION ID IS D_1300007232. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 28-SEP-15 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SPRING-8 REMARK 200 BEAMLINE : BL32XU REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225-HS REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21307 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 48.90 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 14.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 51.66 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM MES-NAOH PH 6.2-7.0, 26-32 % REMARK 280 PEG300, 300~500MM AMMONIUM FLUORIDE, 1% 1,2,3-HEPTANETRIOL, REMARK 280 0.5MM NMS AND 5% DMSO, LIPIDIC CUBIC PHASE, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 29.48000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 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: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY A -1 REMARK 465 PRO A 0 REMARK 465 MET A 1 REMARK 465 ASP A 2 REMARK 465 ASP A 3 REMARK 465 SER A 4 REMARK 465 THR A 5 REMARK 465 ASP A 6 REMARK 465 SER A 7 REMARK 465 SER A 8 REMARK 465 ASP A 9 REMARK 465 ASN A 10 REMARK 465 SER A 11 REMARK 465 LEU A 12 REMARK 465 ALA A 13 REMARK 465 LEU A 14 REMARK 465 THR A 15 REMARK 465 SER A 215 REMARK 465 ARG A 216 REMARK 465 ILE A 217 REMARK 465 PRO A 377 REMARK 465 PRO A 378 REMARK 465 PRO A 379 REMARK 465 TYR A 459 REMARK 465 LYS A 460 REMARK 465 ASN A 461 REMARK 465 ILE A 462 REMARK 465 GLY A 463 REMARK 465 ALA A 464 REMARK 465 THR A 465 REMARK 465 ARG A 466 REMARK 465 LEU A 467 REMARK 465 GLU A 468 REMARK 465 VAL A 469 REMARK 465 LEU A 470 REMARK 465 PHE A 471 REMARK 465 GLN A 472 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 GLU A1057 CG CD OE1 OE2 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 PRO A1046 70.59 -68.35 REMARK 500 LYS A1083 43.39 -103.41 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue 3C0 A 501 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 5ZK8 RELATED DB: PDB REMARK 900 RELATED ID: 5ZKB RELATED DB: PDB REMARK 900 RELATED ID: 5ZK3 RELATED DB: PDB DBREF 5ZKC A 10 217 UNP P08172 ACM2_HUMAN 10 217 DBREF 5ZKC A 1001 1106 PDB 5ZKC 5ZKC 1001 1106 DBREF 5ZKC A 377 466 UNP P08172 ACM2_HUMAN 377 466 SEQADV 5ZKC GLY A -1 UNP P08172 EXPRESSION TAG SEQADV 5ZKC PRO A 0 UNP P08172 EXPRESSION TAG SEQADV 5ZKC MET A 1 UNP P08172 EXPRESSION TAG SEQADV 5ZKC ASP A 2 UNP P08172 EXPRESSION TAG SEQADV 5ZKC ASP A 3 UNP P08172 EXPRESSION TAG SEQADV 5ZKC SER A 4 UNP P08172 EXPRESSION TAG SEQADV 5ZKC THR A 5 UNP P08172 EXPRESSION TAG SEQADV 5ZKC ASP A 6 UNP P08172 EXPRESSION TAG SEQADV 5ZKC SER A 7 UNP P08172 EXPRESSION TAG SEQADV 5ZKC SER A 8 UNP P08172 EXPRESSION TAG SEQADV 5ZKC ASP A 9 UNP P08172 EXPRESSION TAG SEQADV 5ZKC ARG A 110 UNP P08172 SER 110 ENGINEERED MUTATION SEQADV 5ZKC LEU A 467 UNP P08172 EXPRESSION TAG SEQADV 5ZKC GLU A 468 UNP P08172 EXPRESSION TAG SEQADV 5ZKC VAL A 469 UNP P08172 EXPRESSION TAG SEQADV 5ZKC LEU A 470 UNP P08172 EXPRESSION TAG SEQADV 5ZKC PHE A 471 UNP P08172 EXPRESSION TAG SEQADV 5ZKC GLN A 472 UNP P08172 EXPRESSION TAG SEQRES 1 A 421 GLY PRO MET ASP ASP SER THR ASP SER SER ASP ASN SER SEQRES 2 A 421 LEU ALA LEU THR SER PRO TYR LYS THR PHE GLU VAL VAL SEQRES 3 A 421 PHE ILE VAL LEU VAL ALA GLY SER LEU SER LEU VAL THR SEQRES 4 A 421 ILE ILE GLY ASN ILE LEU VAL MET VAL SER ILE LYS VAL SEQRES 5 A 421 ASN ARG HIS LEU GLN THR VAL ASN ASN TYR PHE LEU PHE SEQRES 6 A 421 SER LEU ALA CYS ALA ASP LEU ILE ILE GLY VAL PHE SER SEQRES 7 A 421 MET ASN LEU TYR THR LEU TYR THR VAL ILE GLY TYR TRP SEQRES 8 A 421 PRO LEU GLY PRO VAL VAL CYS ASP LEU TRP LEU ALA LEU SEQRES 9 A 421 ASP TYR VAL VAL SER ASN ALA ARG VAL MET ASN LEU LEU SEQRES 10 A 421 ILE ILE SER PHE ASP ARG TYR PHE CYS VAL THR LYS PRO SEQRES 11 A 421 LEU THR TYR PRO VAL LYS ARG THR THR LYS MET ALA GLY SEQRES 12 A 421 MET MET ILE ALA ALA ALA TRP VAL LEU SER PHE ILE LEU SEQRES 13 A 421 TRP ALA PRO ALA ILE LEU PHE TRP GLN PHE ILE VAL GLY SEQRES 14 A 421 VAL ARG THR VAL GLU ASP GLY GLU CYS TYR ILE GLN PHE SEQRES 15 A 421 PHE SER ASN ALA ALA VAL THR PHE GLY THR ALA ILE ALA SEQRES 16 A 421 ALA PHE TYR LEU PRO VAL ILE ILE MET THR VAL LEU TYR SEQRES 17 A 421 TRP HIS ILE SER ARG ALA SER LYS SER ARG ILE ALA ASP SEQRES 18 A 421 LEU GLU ASP ASN TRP GLU THR LEU ASN ASP ASN LEU LYS SEQRES 19 A 421 VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS ASP SEQRES 20 A 421 ALA LEU THR LYS MET ARG ALA ALA ALA LEU ASP ALA GLN SEQRES 21 A 421 LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SER PRO ASP SEQRES 22 A 421 SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE ASP ILE SEQRES 23 A 421 LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA ASN SEQRES 24 A 421 GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU GLN SEQRES 25 A 421 LEU LYS THR THR ARG ASN ALA TYR ILE GLN LYS TYR LEU SEQRES 26 A 421 PRO PRO PRO SER ARG GLU LYS LYS VAL THR ARG THR ILE SEQRES 27 A 421 LEU ALA ILE LEU LEU ALA PHE ILE ILE THR TRP ALA PRO SEQRES 28 A 421 TYR ASN VAL MET VAL LEU ILE ASN THR PHE CYS ALA PRO SEQRES 29 A 421 CYS ILE PRO ASN THR VAL TRP THR ILE GLY TYR TRP LEU SEQRES 30 A 421 CYS TYR ILE ASN SER THR ILE ASN PRO ALA CYS TYR ALA SEQRES 31 A 421 LEU CYS ASN ALA THR PHE LYS LYS THR PHE LYS HIS LEU SEQRES 32 A 421 LEU MET CYS HIS TYR LYS ASN ILE GLY ALA THR ARG LEU SEQRES 33 A 421 GLU VAL LEU PHE GLN HET 3C0 A 501 23 HETNAM 3C0 N-METHYL SCOPOLAMINE HETSYN 3C0 (1R,2R,4S,5S,7S)-7-{[(2S)-3-HYDROXY-2- HETSYN 2 3C0 PHENYLPROPANOYL]OXY}-9,9-DIMETHYL-3-OXA-9- HETSYN 3 3C0 AZONIATRICYCLO[3.3.1.0~2,4~]NONANE FORMUL 2 3C0 C18 H24 N O4 1+ FORMUL 3 HOH *34(H2 O) HELIX 1 AA1 SER A 16 ASN A 51 1 36 HELIX 2 AA2 ARG A 52 GLN A 55 5 4 HELIX 3 AA3 THR A 56 PHE A 75 1 20 HELIX 4 AA4 PHE A 75 GLY A 87 1 13 HELIX 5 AA5 GLY A 92 LYS A 127 1 36 HELIX 6 AA6 TYR A 131 ARG A 135 5 5 HELIX 7 AA7 THR A 136 GLY A 167 1 32 HELIX 8 AA8 ILE A 178 SER A 182 5 5 HELIX 9 AA9 ASN A 183 PHE A 195 1 13 HELIX 10 AB1 PHE A 195 LYS A 214 1 20 HELIX 11 AB2 ASP A 1002 LYS A 1019 1 18 HELIX 12 AB3 ASN A 1022 ALA A 1043 1 22 HELIX 13 AB4 LYS A 1047 LYS A 1051 5 5 HELIX 14 AB5 SER A 1055 GLU A 1081 1 27 HELIX 15 AB6 LYS A 1083 TYR A 1101 1 19 HELIX 16 AB7 ARG A 381 THR A 411 1 31 HELIX 17 AB8 PRO A 418 ALA A 441 1 24 HELIX 18 AB9 ASN A 444 MET A 456 1 13 SSBOND 1 CYS A 96 CYS A 176 1555 1555 2.03 SSBOND 2 CYS A 413 CYS A 416 1555 1555 2.03 SITE 1 AC1 12 ASP A 103 TYR A 104 SER A 107 ASN A 108 SITE 2 AC1 12 ALA A 191 TRP A 400 TYR A 403 ASN A 404 SITE 3 AC1 12 TYR A 426 CYS A 429 TYR A 430 HOH A 629 CRYST1 46.430 58.960 88.970 90.00 98.82 90.00 P 1 21 1 2 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.021538 0.000000 0.003340 0.00000 SCALE2 0.000000 0.016961 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011374 0.00000 ATOM 1 N SER A 16 152.838 30.669 506.180 1.00105.15 N ANISOU 1 N SER A 16 10641 18573 10739 -1760 -3501 -1238 N ATOM 2 CA SER A 16 153.850 30.098 507.062 1.00101.89 C ANISOU 2 CA SER A 16 10554 17624 10535 -1865 -3394 -1377 C ATOM 3 C SER A 16 153.658 30.561 508.504 1.00100.05 C ANISOU 3 C SER A 16 10069 17339 10605 -1878 -3136 -1103 C ATOM 4 O SER A 16 154.409 31.405 508.993 1.00 93.04 O ANISOU 4 O SER A 16 9195 16394 9760 -1547 -2872 -947 O ATOM 5 CB SER A 16 155.250 30.472 506.573 1.00101.15 C ANISOU 5 CB SER A 16 10794 17384 10256 -1485 -3248 -1476 C ATOM 6 OG SER A 16 156.242 30.030 507.482 1.00 98.30 O ANISOU 6 OG SER A 16 10709 16554 10088 -1535 -3117 -1590 O ATOM 7 N PRO A 17 152.648 30.009 509.187 1.00104.38 N ANISOU 7 N PRO A 17 10391 17920 11349 -2259 -3209 -1037 N ATOM 8 CA PRO A 17 152.386 30.425 510.571 1.00106.31 C ANISOU 8 CA PRO A 17 10391 18158 11843 -2260 -2950 -766 C ATOM 9 C PRO A 17 153.296 29.743 511.581 1.00112.24 C ANISOU 9 C PRO A 17 11459 18354 12833 -2440 -2856 -875 C ATOM 10 O PRO A 17 153.611 30.318 512.627 1.00109.10 O ANISOU 10 O PRO A 17 10976 17887 12590 -2279 -2594 -681 O ATOM 11 CB PRO A 17 150.921 30.025 510.778 1.00103.46 C ANISOU 11 CB PRO A 17 9660 18116 11533 -2610 -3065 -653 C ATOM 12 CG PRO A 17 150.749 28.831 509.900 1.00107.08 C ANISOU 12 CG PRO A 17 10347 18423 11917 -3002 -3423 -967 C ATOM 13 CD PRO A 17 151.644 29.045 508.700 1.00107.55 C ANISOU 13 CD PRO A 17 10723 18418 11723 -2694 -3524 -1184 C ATOM 14 N TYR A 18 153.727 28.516 511.279 1.00126.03 N ANISOU 14 N TYR A 18 13603 19680 14602 -2745 -3075 -1194 N ATOM 15 CA TYR A 18 154.519 27.759 512.244 1.00126.13 C ANISOU 15 CA TYR A 18 13951 19130 14843 -2921 -3001 -1299 C ATOM 16 C TYR A 18 155.939 28.304 512.350 1.00117.69 C ANISOU 16 C TYR A 18 13136 17858 13722 -2538 -2813 -1359 C ATOM 17 O TYR A 18 156.506 28.358 513.447 1.00114.03 O ANISOU 17 O TYR A 18 12741 17133 13453 -2529 -2616 -1270 O ATOM 18 CB TYR A 18 154.537 26.278 511.863 1.00138.38 C ANISOU 18 CB TYR A 18 15900 20246 16430 -3297 -3292 -1637 C ATOM 19 CG TYR A 18 154.861 25.356 513.017 1.00144.70 C ANISOU 19 CG TYR A 18 16962 20505 17514 -3579 -3220 -1658 C ATOM 20 CD1 TYR A 18 156.176 25.040 513.333 1.00143.52 C ANISOU 20 CD1 TYR A 18 17263 19855 17414 -3399 -3131 -1839 C ATOM 21 CD2 TYR A 18 153.851 24.801 513.792 1.00150.72 C ANISOU 21 CD2 TYR A 18 17522 21281 18465 -4009 -3225 -1474 C ATOM 22 CE1 TYR A 18 156.476 24.198 514.388 1.00144.65 C ANISOU 22 CE1 TYR A 18 17666 19492 17803 -3617 -3049 -1828 C ATOM 23 CE2 TYR A 18 154.141 23.957 514.849 1.00151.89 C ANISOU 23 CE2 TYR A 18 17931 20936 18844 -4257 -3142 -1445 C ATOM 24 CZ TYR A 18 155.455 23.660 515.142 1.00148.45 C ANISOU 24 CZ TYR A 18 17961 19976 18468 -4049 -3056 -1618 C ATOM 25 OH TYR A 18 155.747 22.821 516.193 1.00148.51 O ANISOU 25 OH TYR A 18 18249 19488 18689 -4255 -2966 -1560 O ATOM 26 N LYS A 19 156.529 28.715 511.223 1.00115.06 N ANISOU 26 N LYS A 19 12935 17673 13110 -2220 -2859 -1498 N ATOM 27 CA LYS A 19 157.879 29.270 511.256 1.00106.62 C ANISOU 27 CA LYS A 19 12064 16492 11953 -1844 -2656 -1546 C ATOM 28 C LYS A 19 157.919 30.577 512.038 1.00 95.49 C ANISOU 28 C LYS A 19 10314 15323 10643 -1568 -2371 -1197 C ATOM 29 O LYS A 19 158.852 30.814 512.815 1.00 91.10 O ANISOU 29 O LYS A 19 9907 14474 10234 -1404 -2145 -1158 O ATOM 30 CB LYS A 19 158.398 29.486 509.835 1.00112.86 C ANISOU 30 CB LYS A 19 13022 17470 12390 -1541 -2728 -1715 C ATOM 31 CG LYS A 19 158.445 28.229 508.984 1.00121.04 C ANISOU 31 CG LYS A 19 14457 18248 13285 -1733 -3020 -2088 C ATOM 32 CD LYS A 19 159.444 27.222 509.527 1.00122.28 C ANISOU 32 CD LYS A 19 15098 17809 13554 -1793 -3015 -2365 C ATOM 33 CE LYS A 19 159.523 26.002 508.624 1.00128.00 C ANISOU 33 CE LYS A 19 16301 18228 14106 -1911 -3319 -2733 C ATOM 34 NZ LYS A 19 160.525 25.011 509.102 1.00127.44 N ANISOU 34 NZ LYS A 19 16777 17546 14099 -1918 -3291 -2972 N ATOM 35 N THR A 20 156.920 31.440 511.840 1.00 84.27 N ANISOU 35 N THR A 20 8506 14333 9180 -1444 -2341 -925 N ATOM 36 CA THR A 20 156.856 32.682 512.601 1.00 80.00 C ANISOU 36 CA THR A 20 7699 13956 8741 -1131 -2083 -595 C ATOM 37 C THR A 20 156.642 32.408 514.084 1.00 71.78 C ANISOU 37 C THR A 20 6564 12707 8000 -1343 -1954 -488 C ATOM 38 O THR A 20 157.221 33.089 514.938 1.00 59.37 O ANISOU 38 O THR A 20 4998 10998 6562 -1109 -1720 -345 O ATOM 39 CB THR A 20 155.744 33.580 512.058 1.00 83.45 C ANISOU 39 CB THR A 20 7801 14854 9052 -918 -2084 -354 C ATOM 40 OG1 THR A 20 154.491 32.886 512.122 1.00 88.11 O ANISOU 40 OG1 THR A 20 8175 15611 9692 -1273 -2240 -364 O ATOM 41 CG2 THR A 20 156.032 33.970 510.615 1.00 83.85 C ANISOU 41 CG2 THR A 20 7958 15107 8792 -670 -2177 -409 C ATOM 42 N PHE A 21 155.811 31.414 514.410 1.00 74.72 N ANISOU 42 N PHE A 21 6888 13016 8487 -1775 -2083 -538 N ATOM 43 CA PHE A 21 155.618 31.049 515.810 1.00 76.58 C ANISOU 43 CA PHE A 21 7069 13049 8980 -1998 -1948 -417 C ATOM 44 C PHE A 21 156.901 30.512 516.428 1.00 72.52 C ANISOU 44 C PHE A 21 6932 12027 8594 -2073 -1888 -577 C ATOM 45 O PHE A 21 157.153 30.731 517.618 1.00 70.56 O ANISOU 45 O PHE A 21 6659 11618 8530 -2031 -1677 -426 O ATOM 46 CB PHE A 21 154.491 30.022 515.939 1.00 85.39 C ANISOU 46 CB PHE A 21 8084 14195 10164 -2469 -2107 -421 C ATOM 47 CG PHE A 21 154.231 29.580 517.353 1.00 91.49 C ANISOU 47 CG PHE A 21 8811 14789 11161 -2711 -1957 -265 C ATOM 48 CD1 PHE A 21 153.440 30.342 518.198 1.00 95.11 C ANISOU 48 CD1 PHE A 21 8891 15599 11648 -2552 -1743 28 C ATOM 49 CD2 PHE A 21 154.773 28.399 517.835 1.00 93.84 C ANISOU 49 CD2 PHE A 21 9482 14559 11612 -3055 -2025 -408 C ATOM 50 CE1 PHE A 21 153.199 29.937 519.498 1.00 96.95 C ANISOU 50 CE1 PHE A 21 9086 15713 12036 -2752 -1594 179 C ATOM 51 CE2 PHE A 21 154.536 27.990 519.134 1.00 94.83 C ANISOU 51 CE2 PHE A 21 9584 14531 11917 -3264 -1877 -229 C ATOM 52 CZ PHE A 21 153.748 28.759 519.966 1.00 96.21 C ANISOU 52 CZ PHE A 21 9348 15113 12096 -3124 -1660 67 C ATOM 53 N GLU A 22 157.725 29.812 515.642 1.00 69.42 N ANISOU 53 N GLU A 22 6932 11349 8093 -2123 -2046 -887 N ATOM 54 CA GLU A 22 159.001 29.333 516.161 1.00 69.41 C ANISOU 54 CA GLU A 22 7393 10753 8226 -2012 -1908 -1025 C ATOM 55 C GLU A 22 159.925 30.493 516.509 1.00 64.17 C ANISOU 55 C GLU A 22 6739 10040 7602 -1511 -1589 -871 C ATOM 56 O GLU A 22 160.632 30.446 517.522 1.00 58.66 O ANISOU 56 O GLU A 22 6207 8994 7089 -1436 -1401 -821 O ATOM 57 CB GLU A 22 159.672 28.401 515.150 1.00 75.78 C ANISOU 57 CB GLU A 22 8632 11292 8867 -2043 -2118 -1402 C ATOM 58 CG GLU A 22 158.959 27.073 514.942 1.00 84.28 C ANISOU 58 CG GLU A 22 9875 12188 9960 -2552 -2440 -1597 C ATOM 59 CD GLU A 22 159.714 26.145 514.008 1.00 89.39 C ANISOU 59 CD GLU A 22 11035 12483 10444 -2472 -2632 -2004 C ATOM 60 OE1 GLU A 22 160.856 25.764 514.340 1.00 89.83 O ANISOU 60 OE1 GLU A 22 11486 12116 10530 -2293 -2539 -2162 O ATOM 61 OE2 GLU A 22 159.171 25.804 512.937 1.00 95.05 O ANISOU 61 OE2 GLU A 22 11767 13350 10997 -2530 -2866 -2166 O ATOM 62 N VAL A 23 159.928 31.544 515.687 1.00 63.29 N ANISOU 62 N VAL A 23 6466 10272 7310 -1187 -1542 -781 N ATOM 63 CA VAL A 23 160.765 32.706 515.973 1.00 58.97 C ANISOU 63 CA VAL A 23 5950 9657 6800 -776 -1268 -611 C ATOM 64 C VAL A 23 160.268 33.428 517.219 1.00 55.41 C ANISOU 64 C VAL A 23 5273 9237 6545 -716 -1085 -347 C ATOM 65 O VAL A 23 161.061 33.812 518.087 1.00 46.76 O ANISOU 65 O VAL A 23 4321 7852 5596 -561 -877 -282 O ATOM 66 CB VAL A 23 160.811 33.645 514.754 1.00 60.11 C ANISOU 66 CB VAL A 23 6008 10143 6688 -480 -1282 -537 C ATOM 67 CG1 VAL A 23 161.609 34.898 515.081 1.00 54.32 C ANISOU 67 CG1 VAL A 23 5327 9304 6009 -129 -1019 -321 C ATOM 68 CG2 VAL A 23 161.404 32.927 513.552 1.00 66.20 C ANISOU 68 CG2 VAL A 23 7020 10915 7219 -491 -1435 -818 C ATOM 69 N VAL A 24 158.953 33.625 517.327 1.00 57.13 N ANISOU 69 N VAL A 24 5121 9847 6741 -821 -1166 -200 N ATOM 70 CA VAL A 24 158.395 34.284 518.504 1.00 51.58 C ANISOU 70 CA VAL A 24 4182 9242 6175 -713 -989 33 C ATOM 71 C VAL A 24 158.616 33.432 519.748 1.00 47.49 C ANISOU 71 C VAL A 24 3785 8397 5862 -986 -911 2 C ATOM 72 O VAL A 24 158.911 33.954 520.830 1.00 44.82 O ANISOU 72 O VAL A 24 3474 7911 5645 -810 -698 120 O ATOM 73 CB VAL A 24 156.904 34.596 518.284 1.00 53.38 C ANISOU 73 CB VAL A 24 3927 10064 6291 -740 -1099 196 C ATOM 74 CG1 VAL A 24 156.305 35.247 519.522 1.00 51.76 C ANISOU 74 CG1 VAL A 24 3482 9998 6188 -565 -893 417 C ATOM 75 CG2 VAL A 24 156.727 35.494 517.071 1.00 52.21 C ANISOU 75 CG2 VAL A 24 3688 10229 5920 -411 -1177 257 C ATOM 76 N PHE A 25 158.487 32.109 519.615 1.00 49.35 N ANISOU 76 N PHE A 25 4134 8492 6124 -1416 -1098 -156 N ATOM 77 CA PHE A 25 158.717 31.224 520.754 1.00 55.24 C ANISOU 77 CA PHE A 25 5049 8888 7052 -1688 -1043 -156 C ATOM 78 C PHE A 25 160.171 31.274 521.208 1.00 54.36 C ANISOU 78 C PHE A 25 5333 8289 7032 -1441 -882 -249 C ATOM 79 O PHE A 25 160.452 31.279 522.413 1.00 54.96 O ANISOU 79 O PHE A 25 5465 8177 7242 -1420 -720 -146 O ATOM 80 CB PHE A 25 158.309 29.794 520.394 1.00 62.76 C ANISOU 80 CB PHE A 25 6127 9714 8007 -2212 -1317 -310 C ATOM 81 CG PHE A 25 158.466 28.813 521.522 1.00 66.92 C ANISOU 81 CG PHE A 25 6864 9854 8710 -2529 -1289 -269 C ATOM 82 CD1 PHE A 25 157.472 28.671 522.478 1.00 69.83 C ANISOU 82 CD1 PHE A 25 6928 10453 9150 -2801 -1224 -18 C ATOM 83 CD2 PHE A 25 159.602 28.026 521.621 1.00 67.73 C ANISOU 83 CD2 PHE A 25 7475 9378 8880 -2504 -1313 -463 C ATOM 84 CE1 PHE A 25 157.613 27.767 523.515 1.00 71.41 C ANISOU 84 CE1 PHE A 25 7364 10281 9489 -3047 -1173 58 C ATOM 85 CE2 PHE A 25 159.748 27.121 522.656 1.00 70.81 C ANISOU 85 CE2 PHE A 25 8095 9392 9419 -2768 -1300 -395 C ATOM 86 CZ PHE A 25 158.752 26.991 523.604 1.00 72.48 C ANISOU 86 CZ PHE A 25 8013 9824 9704 -3090 -1241 -120 C ATOM 87 N ILE A 26 161.110 31.317 520.259 1.00 52.65 N ANISOU 87 N ILE A 26 5364 7923 6716 -1245 -925 -435 N ATOM 88 CA ILE A 26 162.527 31.355 520.613 1.00 53.91 C ANISOU 88 CA ILE A 26 5836 7711 6935 -1012 -781 -518 C ATOM 89 C ILE A 26 162.876 32.670 521.302 1.00 48.48 C ANISOU 89 C ILE A 26 5037 7079 6304 -703 -543 -327 C ATOM 90 O ILE A 26 163.621 32.689 522.289 1.00 42.84 O ANISOU 90 O ILE A 26 4465 6108 5706 -628 -406 -304 O ATOM 91 CB ILE A 26 163.395 31.118 519.363 1.00 58.15 C ANISOU 91 CB ILE A 26 6598 8190 7305 -862 -871 -746 C ATOM 92 CG1 ILE A 26 163.332 29.648 518.941 1.00 63.63 C ANISOU 92 CG1 ILE A 26 7559 8655 7964 -1129 -1106 -1002 C ATOM 93 CG2 ILE A 26 164.835 31.543 519.615 1.00 55.19 C ANISOU 93 CG2 ILE A 26 6403 7618 6949 -557 -685 -764 C ATOM 94 CD1 ILE A 26 163.779 28.685 520.018 1.00 65.85 C ANISOU 94 CD1 ILE A 26 8114 8484 8420 -1261 -1091 -1039 C ATOM 95 N VAL A 27 162.345 33.786 520.798 1.00 46.38 N ANISOU 95 N VAL A 27 4547 7131 5946 -512 -510 -193 N ATOM 96 CA VAL A 27 162.617 35.083 521.414 1.00 40.73 C ANISOU 96 CA VAL A 27 3794 6405 5277 -218 -315 -26 C ATOM 97 C VAL A 27 162.066 35.127 522.834 1.00 42.23 C ANISOU 97 C VAL A 27 3869 6582 5592 -258 -205 90 C ATOM 98 O VAL A 27 162.714 35.645 523.753 1.00 39.16 O ANISOU 98 O VAL A 27 3606 5989 5285 -108 -54 128 O ATOM 99 CB VAL A 27 162.041 36.216 520.544 1.00 42.55 C ANISOU 99 CB VAL A 27 3852 6946 5368 15 -332 109 C ATOM 100 CG1 VAL A 27 162.106 37.544 521.281 1.00 37.52 C ANISOU 100 CG1 VAL A 27 3223 6247 4788 313 -162 279 C ATOM 101 CG2 VAL A 27 162.794 36.300 519.223 1.00 43.63 C ANISOU 101 CG2 VAL A 27 4131 7094 5350 89 -397 27 C ATOM 102 N LEU A 28 160.867 34.575 523.040 1.00 39.12 N ANISOU 102 N LEU A 28 3224 6447 5193 -480 -282 153 N ATOM 103 CA LEU A 28 160.273 34.569 524.373 1.00 38.96 C ANISOU 103 CA LEU A 28 3049 6506 5246 -524 -159 290 C ATOM 104 C LEU A 28 161.054 33.675 525.329 1.00 36.01 C ANISOU 104 C LEU A 28 2936 5753 4992 -705 -112 230 C ATOM 105 O LEU A 28 161.285 34.050 526.485 1.00 34.49 O ANISOU 105 O LEU A 28 2778 5480 4846 -572 49 306 O ATOM 106 CB LEU A 28 158.811 34.129 524.298 1.00 43.64 C ANISOU 106 CB LEU A 28 3253 7546 5781 -773 -256 403 C ATOM 107 CG LEU A 28 157.838 35.116 523.644 1.00 45.36 C ANISOU 107 CG LEU A 28 3125 8250 5859 -515 -279 518 C ATOM 108 CD1 LEU A 28 156.427 34.548 523.627 1.00 53.30 C ANISOU 108 CD1 LEU A 28 3705 9748 6797 -812 -385 631 C ATOM 109 CD2 LEU A 28 157.876 36.456 524.360 1.00 44.53 C ANISOU 109 CD2 LEU A 28 3005 8175 5739 -33 -71 631 C ATOM 110 N VAL A 29 161.459 32.488 524.874 1.00 31.53 N ANISOU 110 N VAL A 29 2578 4946 4454 -977 -262 87 N ATOM 111 CA VAL A 29 162.208 31.584 525.742 1.00 41.54 C ANISOU 111 CA VAL A 29 4128 5832 5823 -1106 -238 44 C ATOM 112 C VAL A 29 163.592 32.148 526.042 1.00 40.75 C ANISOU 112 C VAL A 29 4259 5477 5748 -788 -116 -31 C ATOM 113 O VAL A 29 164.055 32.111 527.189 1.00 46.32 O ANISOU 113 O VAL A 29 5063 6024 6512 -736 -5 24 O ATOM 114 CB VAL A 29 162.287 30.181 525.113 1.00 45.30 C ANISOU 114 CB VAL A 29 4836 6066 6312 -1427 -456 -111 C ATOM 115 CG1 VAL A 29 163.252 29.302 525.895 1.00 47.16 C ANISOU 115 CG1 VAL A 29 5435 5849 6635 -1450 -442 -165 C ATOM 116 CG2 VAL A 29 160.909 29.542 525.075 1.00 50.89 C ANISOU 116 CG2 VAL A 29 5314 7007 7015 -1856 -590 -4 C ATOM 117 N ALA A 30 164.274 32.683 525.025 1.00 38.40 N ANISOU 117 N ALA A 30 4029 5177 5384 -591 -138 -141 N ATOM 118 CA ALA A 30 165.608 33.238 525.241 1.00 36.73 C ANISOU 118 CA ALA A 30 3985 4787 5184 -350 -33 -190 C ATOM 119 C ALA A 30 165.559 34.459 526.152 1.00 36.54 C ANISOU 119 C ALA A 30 3871 4824 5190 -167 125 -54 C ATOM 120 O ALA A 30 166.410 34.615 527.035 1.00 31.92 O ANISOU 120 O ALA A 30 3414 4063 4650 -85 207 -63 O ATOM 121 CB ALA A 30 166.259 33.590 523.904 1.00 29.58 C ANISOU 121 CB ALA A 30 3125 3944 4170 -217 -77 -291 C ATOM 122 N GLY A 31 164.574 35.338 525.948 1.00 32.46 N ANISOU 122 N GLY A 31 3148 4556 4628 -76 153 59 N ATOM 123 CA GLY A 31 164.423 36.485 526.827 1.00 30.68 C ANISOU 123 CA GLY A 31 2890 4357 4410 143 286 158 C ATOM 124 C GLY A 31 164.067 36.098 528.249 1.00 35.31 C ANISOU 124 C GLY A 31 3442 4943 5031 89 371 212 C ATOM 125 O GLY A 31 164.488 36.762 529.200 1.00 31.42 O ANISOU 125 O GLY A 31 3050 4347 4542 254 473 217 O ATOM 126 N SER A 32 163.287 35.025 528.414 1.00 32.99 N ANISOU 126 N SER A 32 3018 4772 4745 -166 322 261 N ATOM 127 CA SER A 32 162.961 34.543 529.753 1.00 36.16 C ANISOU 127 CA SER A 32 3386 5200 5154 -261 411 356 C ATOM 128 C SER A 32 164.182 33.939 530.434 1.00 35.35 C ANISOU 128 C SER A 32 3575 4748 5108 -298 416 282 C ATOM 129 O SER A 32 164.404 34.161 531.630 1.00 32.06 O ANISOU 129 O SER A 32 3210 4305 4665 -199 523 329 O ATOM 130 CB SER A 32 161.826 33.521 529.685 1.00 36.97 C ANISOU 130 CB SER A 32 3275 5522 5250 -604 341 468 C ATOM 131 OG SER A 32 160.655 34.097 529.126 1.00 46.06 O ANISOU 131 OG SER A 32 4087 7091 6324 -549 332 552 O ATOM 132 N LEU A 33 164.976 33.161 529.692 1.00 35.06 N ANISOU 132 N LEU A 33 3728 4473 5119 -404 294 160 N ATOM 133 CA LEU A 33 166.188 32.577 530.258 1.00 35.68 C ANISOU 133 CA LEU A 33 4067 4259 5232 -372 286 89 C ATOM 134 C LEU A 33 167.163 33.661 530.697 1.00 32.34 C ANISOU 134 C LEU A 33 3701 3797 4789 -115 374 41 C ATOM 135 O LEU A 33 167.734 33.594 531.792 1.00 35.07 O ANISOU 135 O LEU A 33 4148 4051 5124 -54 423 56 O ATOM 136 CB LEU A 33 166.842 31.643 529.239 1.00 37.00 C ANISOU 136 CB LEU A 33 4417 4224 5418 -441 142 -61 C ATOM 137 CG LEU A 33 166.118 30.324 528.965 1.00 44.22 C ANISOU 137 CG LEU A 33 5408 5034 6361 -744 4 -52 C ATOM 138 CD1 LEU A 33 166.666 29.668 527.711 1.00 45.56 C ANISOU 138 CD1 LEU A 33 5763 5042 6504 -732 -149 -259 C ATOM 139 CD2 LEU A 33 166.241 29.389 530.158 1.00 45.09 C ANISOU 139 CD2 LEU A 33 5699 4922 6511 -865 10 54 C ATOM 140 N SER A 34 167.370 34.667 529.844 1.00 31.79 N ANISOU 140 N SER A 34 3581 3796 4703 12 378 -7 N ATOM 141 CA SER A 34 168.262 35.768 530.192 1.00 32.42 C ANISOU 141 CA SER A 34 3735 3813 4771 181 435 -39 C ATOM 142 C SER A 34 167.785 36.491 531.445 1.00 36.08 C ANISOU 142 C SER A 34 4186 4321 5201 291 531 20 C ATOM 143 O SER A 34 168.589 36.820 532.325 1.00 35.10 O ANISOU 143 O SER A 34 4182 4095 5061 357 553 -24 O ATOM 144 CB SER A 34 168.371 36.741 529.018 1.00 27.33 C ANISOU 144 CB SER A 34 3055 3224 4106 254 419 -44 C ATOM 145 OG SER A 34 169.083 37.910 529.385 1.00 33.02 O ANISOU 145 OG SER A 34 3870 3852 4824 355 458 -45 O ATOM 146 N LEU A 35 166.479 36.746 531.543 1.00 39.12 N ANISOU 146 N LEU A 35 4411 4903 5549 331 582 111 N ATOM 147 CA LEU A 35 165.952 37.489 532.683 1.00 39.52 C ANISOU 147 CA LEU A 35 4443 5050 5522 512 689 149 C ATOM 148 C LEU A 35 166.096 36.700 533.978 1.00 37.21 C ANISOU 148 C LEU A 35 4193 4758 5187 440 739 183 C ATOM 149 O LEU A 35 166.449 37.266 535.019 1.00 38.10 O ANISOU 149 O LEU A 35 4416 4837 5222 591 794 139 O ATOM 150 CB LEU A 35 164.490 37.856 532.433 1.00 42.60 C ANISOU 150 CB LEU A 35 4593 5743 5851 615 742 252 C ATOM 151 CG LEU A 35 163.838 38.745 533.491 1.00 46.89 C ANISOU 151 CG LEU A 35 5103 6444 6269 907 867 273 C ATOM 152 CD1 LEU A 35 164.627 40.033 533.656 1.00 43.32 C ANISOU 152 CD1 LEU A 35 4932 5718 5808 1141 853 146 C ATOM 153 CD2 LEU A 35 162.396 39.038 533.115 1.00 54.13 C ANISOU 153 CD2 LEU A 35 5718 7742 7106 1049 915 386 C ATOM 154 N VAL A 36 165.823 35.394 533.937 1.00 35.28 N ANISOU 154 N VAL A 36 3892 4536 4975 202 705 266 N ATOM 155 CA VAL A 36 165.990 34.561 535.125 1.00 38.50 C ANISOU 155 CA VAL A 36 4376 4916 5335 117 742 345 C ATOM 156 C VAL A 36 167.453 34.520 535.546 1.00 33.03 C ANISOU 156 C VAL A 36 3918 3981 4652 195 688 233 C ATOM 157 O VAL A 36 167.773 34.581 536.740 1.00 32.20 O ANISOU 157 O VAL A 36 3892 3892 4449 282 736 251 O ATOM 158 CB VAL A 36 165.431 33.149 534.870 1.00 40.65 C ANISOU 158 CB VAL A 36 4608 5177 5659 -197 682 472 C ATOM 159 CG1 VAL A 36 165.799 32.210 536.010 1.00 37.94 C ANISOU 159 CG1 VAL A 36 4423 4721 5274 -290 696 581 C ATOM 160 CG2 VAL A 36 163.921 33.203 534.692 1.00 38.34 C ANISOU 160 CG2 VAL A 36 4011 5233 5325 -315 739 616 C ATOM 161 N THR A 37 168.364 34.420 534.574 1.00 30.29 N ANISOU 161 N THR A 37 3654 3464 4391 178 586 119 N ATOM 162 CA THR A 37 169.790 34.400 534.890 1.00 29.88 C ANISOU 162 CA THR A 37 3750 3270 4332 258 531 22 C ATOM 163 C THR A 37 170.225 35.696 535.563 1.00 32.26 C ANISOU 163 C THR A 37 4084 3606 4567 402 566 -51 C ATOM 164 O THR A 37 171.009 35.678 536.520 1.00 32.57 O ANISOU 164 O THR A 37 4215 3624 4536 457 544 -86 O ATOM 165 CB THR A 37 170.611 34.163 533.622 1.00 32.36 C ANISOU 165 CB THR A 37 4085 3495 4715 241 441 -77 C ATOM 166 OG1 THR A 37 170.174 32.959 532.977 1.00 30.80 O ANISOU 166 OG1 THR A 37 3918 3222 4562 119 381 -55 O ATOM 167 CG2 THR A 37 172.092 34.035 533.965 1.00 30.30 C ANISOU 167 CG2 THR A 37 3907 3180 4424 333 386 -156 C ATOM 168 N ILE A 38 169.726 36.832 535.073 1.00 28.33 N ANISOU 168 N ILE A 38 3540 3145 4079 468 599 -79 N ATOM 169 CA ILE A 38 170.110 38.124 535.635 1.00 33.42 C ANISOU 169 CA ILE A 38 4295 3739 4667 590 602 -169 C ATOM 170 C ILE A 38 169.585 38.267 537.058 1.00 37.68 C ANISOU 170 C ILE A 38 4878 4375 5064 722 677 -164 C ATOM 171 O ILE A 38 170.330 38.621 537.979 1.00 38.99 O ANISOU 171 O ILE A 38 5177 4493 5144 770 638 -256 O ATOM 172 CB ILE A 38 169.611 39.266 534.732 1.00 30.60 C ANISOU 172 CB ILE A 38 3936 3342 4346 662 609 -176 C ATOM 173 CG1 ILE A 38 170.323 39.223 533.379 1.00 29.13 C ANISOU 173 CG1 ILE A 38 3721 3094 4254 531 538 -173 C ATOM 174 CG2 ILE A 38 169.824 40.612 535.405 1.00 29.27 C ANISOU 174 CG2 ILE A 38 3963 3045 4113 798 596 -274 C ATOM 175 CD1 ILE A 38 169.811 40.240 532.386 1.00 30.01 C ANISOU 175 CD1 ILE A 38 3840 3173 4387 594 539 -129 C ATOM 176 N ILE A 39 168.296 37.985 537.261 1.00 38.38 N ANISOU 176 N ILE A 39 4831 4651 5099 776 783 -53 N ATOM 177 CA ILE A 39 167.678 38.199 538.569 1.00 39.40 C ANISOU 177 CA ILE A 39 4965 4959 5046 942 888 -34 C ATOM 178 C ILE A 39 168.296 37.275 539.612 1.00 37.62 C ANISOU 178 C ILE A 39 4807 4750 4736 862 876 13 C ATOM 179 O ILE A 39 168.637 37.703 540.720 1.00 36.53 O ANISOU 179 O ILE A 39 4792 4651 4435 1001 885 -68 O ATOM 180 CB ILE A 39 166.154 38.006 538.480 1.00 36.00 C ANISOU 180 CB ILE A 39 4290 4827 4560 990 1017 117 C ATOM 181 CG1 ILE A 39 165.536 39.041 537.537 1.00 37.68 C ANISOU 181 CG1 ILE A 39 4445 5053 4817 1156 1019 72 C ATOM 182 CG2 ILE A 39 165.525 38.098 539.861 1.00 31.72 C ANISOU 182 CG2 ILE A 39 3708 4559 3785 1170 1156 165 C ATOM 183 CD1 ILE A 39 164.049 38.859 537.328 1.00 41.94 C ANISOU 183 CD1 ILE A 39 4674 5965 5295 1213 1126 227 C ATOM 184 N GLY A 40 168.447 35.993 539.273 1.00 35.08 N ANISOU 184 N GLY A 40 4439 4384 4505 656 839 139 N ATOM 185 CA GLY A 40 168.971 35.042 540.239 1.00 33.55 C ANISOU 185 CA GLY A 40 4339 4184 4224 609 821 226 C ATOM 186 C GLY A 40 170.378 35.376 540.696 1.00 37.54 C ANISOU 186 C GLY A 40 5002 4576 4686 696 708 75 C ATOM 187 O GLY A 40 170.699 35.264 541.881 1.00 36.40 O ANISOU 187 O GLY A 40 4940 4520 4369 782 710 90 O ATOM 188 N ASN A 41 171.236 35.790 539.764 1.00 29.70 N ANISOU 188 N ASN A 41 4024 3435 3824 663 605 -58 N ATOM 189 CA ASN A 41 172.617 36.085 540.125 1.00 32.16 C ANISOU 189 CA ASN A 41 4419 3707 4095 694 483 -183 C ATOM 190 C ASN A 41 172.758 37.435 540.815 1.00 38.91 C ANISOU 190 C ASN A 41 5367 4583 4833 779 464 -340 C ATOM 191 O ASN A 41 173.624 37.591 541.683 1.00 38.44 O ANISOU 191 O ASN A 41 5386 4572 4649 808 371 -424 O ATOM 192 CB ASN A 41 173.508 36.018 538.885 1.00 25.99 C ANISOU 192 CB ASN A 41 3579 2832 3464 606 394 -242 C ATOM 193 CG ASN A 41 173.738 34.598 538.423 1.00 29.54 C ANISOU 193 CG ASN A 41 4016 3232 3976 588 364 -149 C ATOM 194 OD1 ASN A 41 174.508 33.856 539.034 1.00 35.53 O ANISOU 194 OD1 ASN A 41 4830 4007 4665 663 297 -122 O ATOM 195 ND2 ASN A 41 173.064 34.206 537.347 1.00 26.29 N ANISOU 195 ND2 ASN A 41 3560 2749 3681 509 396 -109 N ATOM 196 N ILE A 42 171.928 38.416 540.454 1.00 38.39 N ANISOU 196 N ILE A 42 5319 4476 4790 837 530 -391 N ATOM 197 CA ILE A 42 171.939 39.683 541.179 1.00 38.53 C ANISOU 197 CA ILE A 42 5511 4452 4678 962 502 -562 C ATOM 198 C ILE A 42 171.476 39.471 542.616 1.00 44.75 C ANISOU 198 C ILE A 42 6351 5433 5217 1136 575 -559 C ATOM 199 O ILE A 42 172.031 40.054 543.555 1.00 47.94 O ANISOU 199 O ILE A 42 6921 5839 5455 1207 490 -720 O ATOM 200 CB ILE A 42 171.079 40.731 540.448 1.00 37.68 C ANISOU 200 CB ILE A 42 5447 4233 4637 1060 556 -601 C ATOM 201 CG1 ILE A 42 171.762 41.171 539.155 1.00 43.01 C ANISOU 201 CG1 ILE A 42 6124 4712 5506 876 459 -611 C ATOM 202 CG2 ILE A 42 170.823 41.932 541.342 1.00 36.62 C ANISOU 202 CG2 ILE A 42 5554 4031 4329 1278 543 -785 C ATOM 203 CD1 ILE A 42 171.035 42.284 538.433 1.00 48.27 C ANISOU 203 CD1 ILE A 42 6889 5227 6226 987 484 -629 C ATOM 204 N LEU A 43 170.467 38.616 542.811 1.00 41.00 N ANISOU 204 N LEU A 43 5733 5151 4695 1181 726 -367 N ATOM 205 CA LEU A 43 170.014 38.304 544.164 1.00 38.81 C ANISOU 205 CA LEU A 43 5473 5123 4151 1327 822 -306 C ATOM 206 C LEU A 43 171.124 37.664 544.986 1.00 39.12 C ANISOU 206 C LEU A 43 5598 5181 4083 1272 707 -299 C ATOM 207 O LEU A 43 171.282 37.973 546.172 1.00 37.40 O ANISOU 207 O LEU A 43 5496 5110 3605 1421 696 -384 O ATOM 208 CB LEU A 43 168.791 37.388 544.113 1.00 37.25 C ANISOU 208 CB LEU A 43 5064 5148 3940 1285 997 -39 C ATOM 209 CG LEU A 43 167.465 38.030 543.700 1.00 43.78 C ANISOU 209 CG LEU A 43 5742 6136 4757 1426 1141 -22 C ATOM 210 CD1 LEU A 43 166.387 36.969 543.556 1.00 45.41 C ANISOU 210 CD1 LEU A 43 5684 6596 4974 1267 1278 273 C ATOM 211 CD2 LEU A 43 167.050 39.085 544.710 1.00 48.06 C ANISOU 211 CD2 LEU A 43 6389 6853 5017 1775 1222 -183 C ATOM 212 N VAL A 44 171.903 36.769 544.375 1.00 37.45 N ANISOU 212 N VAL A 44 5337 4849 4042 1101 612 -207 N ATOM 213 CA VAL A 44 173.007 36.132 545.091 1.00 40.00 C ANISOU 213 CA VAL A 44 5723 5214 4259 1103 487 -187 C ATOM 214 C VAL A 44 174.078 37.158 545.439 1.00 41.01 C ANISOU 214 C VAL A 44 5946 5328 4309 1123 318 -444 C ATOM 215 O VAL A 44 174.551 37.226 546.580 1.00 43.31 O ANISOU 215 O VAL A 44 6325 5771 4360 1215 243 -504 O ATOM 216 CB VAL A 44 173.588 34.973 544.262 1.00 41.90 C ANISOU 216 CB VAL A 44 5905 5323 4693 988 421 -54 C ATOM 217 CG1 VAL A 44 174.857 34.445 544.913 1.00 44.57 C ANISOU 217 CG1 VAL A 44 6292 5726 4917 1059 268 -55 C ATOM 218 CG2 VAL A 44 172.561 33.862 544.114 1.00 41.85 C ANISOU 218 CG2 VAL A 44 5872 5297 4735 916 546 202 C ATOM 219 N MET A 45 174.475 37.972 544.459 1.00 37.71 N ANISOU 219 N MET A 45 5514 4738 4076 1005 244 -586 N ATOM 220 CA MET A 45 175.532 38.954 544.688 1.00 41.26 C ANISOU 220 CA MET A 45 6048 5151 4477 924 58 -807 C ATOM 221 C MET A 45 175.121 39.974 545.742 1.00 44.38 C ANISOU 221 C MET A 45 6662 5559 4640 1058 44 -1000 C ATOM 222 O MET A 45 175.889 40.275 546.663 1.00 51.23 O ANISOU 222 O MET A 45 7628 6523 5315 1055 -111 -1146 O ATOM 223 CB MET A 45 175.890 39.649 543.374 1.00 41.07 C ANISOU 223 CB MET A 45 5980 4933 4693 734 6 -865 C ATOM 224 CG MET A 45 176.544 38.735 542.353 1.00 38.37 C ANISOU 224 CG MET A 45 5428 4626 4525 629 -9 -731 C ATOM 225 SD MET A 45 176.538 39.446 540.697 0.71 35.89 S ANISOU 225 SD MET A 45 5049 4134 4453 450 9 -733 S ATOM 226 CE MET A 45 177.371 40.999 541.002 1.00 38.87 C ANISOU 226 CE MET A 45 5571 4411 4785 248 -169 -926 C ATOM 227 N VAL A 46 173.907 40.517 545.626 1.00 43.52 N ANISOU 227 N VAL A 46 6631 5382 4522 1208 196 -1018 N ATOM 228 CA VAL A 46 173.461 41.538 546.570 1.00 44.25 C ANISOU 228 CA VAL A 46 6967 5475 4370 1417 192 -1236 C ATOM 229 C VAL A 46 173.302 40.949 547.968 1.00 47.49 C ANISOU 229 C VAL A 46 7392 6202 4450 1601 243 -1201 C ATOM 230 O VAL A 46 173.609 41.606 548.970 1.00 55.52 O ANISOU 230 O VAL A 46 8621 7269 5205 1713 134 -1428 O ATOM 231 CB VAL A 46 172.160 42.193 546.068 1.00 42.48 C ANISOU 231 CB VAL A 46 6788 5160 4194 1615 357 -1243 C ATOM 232 CG1 VAL A 46 171.579 43.121 547.123 1.00 42.83 C ANISOU 232 CG1 VAL A 46 7078 5250 3944 1927 381 -1460 C ATOM 233 CG2 VAL A 46 172.421 42.960 544.780 1.00 42.51 C ANISOU 233 CG2 VAL A 46 6848 4828 4477 1446 271 -1291 C ATOM 234 N SER A 47 172.841 39.698 548.060 1.00 41.95 N ANISOU 234 N SER A 47 6491 5708 3739 1618 394 -910 N ATOM 235 CA SER A 47 172.666 39.069 549.367 1.00 46.00 C ANISOU 235 CA SER A 47 7017 6538 3923 1774 459 -808 C ATOM 236 C SER A 47 173.993 38.936 550.104 1.00 47.04 C ANISOU 236 C SER A 47 7232 6736 3905 1718 230 -908 C ATOM 237 O SER A 47 174.059 39.145 551.321 1.00 46.35 O ANISOU 237 O SER A 47 7275 6868 3467 1887 195 -1010 O ATOM 238 CB SER A 47 172.008 37.700 549.210 1.00 44.49 C ANISOU 238 CB SER A 47 6627 6484 3791 1716 634 -432 C ATOM 239 OG SER A 47 170.685 37.834 548.723 1.00 51.94 O ANISOU 239 OG SER A 47 7450 7483 4802 1768 842 -334 O ATOM 240 N ILE A 48 175.060 38.583 549.384 1.00 42.96 N ANISOU 240 N ILE A 48 6618 6085 3618 1506 69 -882 N ATOM 241 CA ILE A 48 176.369 38.459 550.016 1.00 45.47 C ANISOU 241 CA ILE A 48 6948 6536 3794 1457 -165 -967 C ATOM 242 C ILE A 48 176.906 39.827 550.422 1.00 48.86 C ANISOU 242 C ILE A 48 7562 6905 4098 1398 -365 -1329 C ATOM 243 O ILE A 48 177.576 39.956 551.455 1.00 55.85 O ANISOU 243 O ILE A 48 8526 7992 4700 1438 -537 -1458 O ATOM 244 CB ILE A 48 177.343 37.722 549.077 1.00 43.47 C ANISOU 244 CB ILE A 48 6496 6218 3801 1291 -266 -840 C ATOM 245 CG1 ILE A 48 176.800 36.336 548.722 1.00 44.66 C ANISOU 245 CG1 ILE A 48 6556 6353 4059 1356 -103 -512 C ATOM 246 CG2 ILE A 48 178.718 37.599 549.713 1.00 38.36 C ANISOU 246 CG2 ILE A 48 5793 5791 2989 1270 -516 -915 C ATOM 247 CD1 ILE A 48 177.685 35.562 547.767 1.00 41.04 C ANISOU 247 CD1 ILE A 48 5947 5818 3830 1278 -190 -415 C ATOM 248 N LYS A 49 176.612 40.869 549.639 1.00 43.68 N ANISOU 248 N LYS A 49 7007 5956 3634 1296 -364 -1495 N ATOM 249 CA LYS A 49 177.154 42.191 549.936 1.00 46.16 C ANISOU 249 CA LYS A 49 7565 6111 3861 1181 -586 -1836 C ATOM 250 C LYS A 49 176.453 42.849 551.120 1.00 56.15 C ANISOU 250 C LYS A 49 9130 7439 4767 1470 -560 -2061 C ATOM 251 O LYS A 49 177.068 43.653 551.830 1.00 60.06 O ANISOU 251 O LYS A 49 9813 7897 5110 1378 -778 -2314 O ATOM 252 CB LYS A 49 177.055 43.093 548.704 1.00 48.44 C ANISOU 252 CB LYS A 49 7922 6018 4463 987 -600 -1904 C ATOM 253 CG LYS A 49 177.854 42.616 547.498 1.00 51.83 C ANISOU 253 CG LYS A 49 8068 6420 5206 695 -640 -1723 C ATOM 254 CD LYS A 49 179.114 43.446 547.277 1.00 57.79 C ANISOU 254 CD LYS A 49 8849 7087 6022 323 -920 -1886 C ATOM 255 CE LYS A 49 180.195 43.118 548.294 1.00 62.85 C ANISOU 255 CE LYS A 49 9395 8060 6424 254 -1139 -1966 C ATOM 256 NZ LYS A 49 181.453 43.874 548.035 1.00 65.96 N ANISOU 256 NZ LYS A 49 9736 8446 6880 -177 -1422 -2094 N ATOM 257 N VAL A 50 175.176 42.531 551.351 1.00 54.25 N ANISOU 257 N VAL A 50 8876 7316 4421 1777 -284 -1931 N ATOM 258 CA VAL A 50 174.408 43.186 552.409 1.00 57.67 C ANISOU 258 CA VAL A 50 9443 7832 4638 2007 -206 -2026 C ATOM 259 C VAL A 50 174.327 42.363 553.688 1.00 62.35 C ANISOU 259 C VAL A 50 9959 8849 4881 2186 -142 -1899 C ATOM 260 O VAL A 50 173.846 42.879 554.710 1.00 63.89 O ANISOU 260 O VAL A 50 10264 9164 4847 2379 -107 -2003 O ATOM 261 CB VAL A 50 172.979 43.531 551.939 1.00 57.65 C ANISOU 261 CB VAL A 50 9398 7755 4751 2215 45 -1928 C ATOM 262 CG1 VAL A 50 173.019 44.315 550.635 1.00 60.91 C ANISOU 262 CG1 VAL A 50 9883 7753 5508 2053 -13 -2000 C ATOM 263 CG2 VAL A 50 172.143 42.266 551.797 1.00 53.71 C ANISOU 263 CG2 VAL A 50 8620 7566 4221 2331 313 -1588 C ATOM 264 N ASN A 51 174.772 41.110 553.671 1.00 61.70 N ANISOU 264 N ASN A 51 9707 8996 4741 2143 -127 -1664 N ATOM 265 CA ASN A 51 174.686 40.230 554.832 1.00 59.97 C ANISOU 265 CA ASN A 51 9417 9165 4205 2294 -58 -1462 C ATOM 266 C ASN A 51 176.095 39.794 555.211 1.00 58.62 C ANISOU 266 C ASN A 51 9232 9119 3921 2168 -332 -1489 C ATOM 267 O ASN A 51 176.740 39.051 554.464 1.00 54.68 O ANISOU 267 O ASN A 51 8580 8573 3622 2021 -398 -1324 O ATOM 268 CB ASN A 51 173.798 39.021 554.538 1.00 58.41 C ANISOU 268 CB ASN A 51 9030 9139 4026 2368 226 -1055 C ATOM 269 CG ASN A 51 173.386 38.278 555.795 1.00 58.75 C ANISOU 269 CG ASN A 51 9016 9554 3752 2514 347 -806 C ATOM 270 OD1 ASN A 51 174.002 38.425 556.850 1.00 56.74 O ANISOU 270 OD1 ASN A 51 8849 9458 3252 2573 194 -914 O ATOM 271 ND2 ASN A 51 172.338 37.470 555.686 1.00 59.86 N ANISOU 271 ND2 ASN A 51 9000 9843 3901 2538 617 -456 N ATOM 272 N ARG A 52 176.569 40.255 556.372 1.00 61.14 N ANISOU 272 N ARG A 52 9658 9588 3986 2203 -491 -1664 N ATOM 273 CA ARG A 52 177.887 39.842 556.842 1.00 64.73 C ANISOU 273 CA ARG A 52 10048 10234 4312 2095 -761 -1669 C ATOM 274 C ARG A 52 177.932 38.349 557.137 1.00 63.84 C ANISOU 274 C ARG A 52 9778 10399 4080 2229 -665 -1261 C ATOM 275 O ARG A 52 178.988 37.722 556.994 1.00 66.29 O ANISOU 275 O ARG A 52 9962 10814 4409 2163 -856 -1164 O ATOM 276 CB ARG A 52 178.286 40.635 558.087 1.00 77.57 C ANISOU 276 CB ARG A 52 11830 11981 5663 2106 -935 -1932 C ATOM 277 CG ARG A 52 178.585 42.105 557.842 1.00 85.97 C ANISOU 277 CG ARG A 52 13099 12724 6843 1896 -1117 -2332 C ATOM 278 CD ARG A 52 177.343 42.964 558.006 1.00 92.67 C ANISOU 278 CD ARG A 52 14148 13382 7679 2093 -915 -2464 C ATOM 279 NE ARG A 52 177.655 44.243 558.636 1.00 99.86 N ANISOU 279 NE ARG A 52 15334 14134 8472 2012 -1109 -2836 N ATOM 280 CZ ARG A 52 177.681 44.437 559.950 1.00105.70 C ANISOU 280 CZ ARG A 52 16195 15107 8859 2161 -1164 -2959 C ATOM 281 NH1 ARG A 52 177.413 43.435 560.776 1.00105.82 N ANISOU 281 NH1 ARG A 52 16062 15532 8611 2394 -1032 -2713 N ATOM 282 NH2 ARG A 52 177.976 45.633 560.440 1.00112.35 N ANISOU 282 NH2 ARG A 52 17321 15764 9605 2067 -1352 -3319 N ATOM 283 N HIS A 53 176.806 37.765 557.556 1.00 61.62 N ANISOU 283 N HIS A 53 9489 10238 3684 2409 -379 -995 N ATOM 284 CA HIS A 53 176.755 36.327 557.792 1.00 59.94 C ANISOU 284 CA HIS A 53 9179 10203 3393 2486 -277 -554 C ATOM 285 C HIS A 53 177.018 35.527 556.523 1.00 63.40 C ANISOU 285 C HIS A 53 9526 10442 4119 2386 -273 -346 C ATOM 286 O HIS A 53 177.414 34.359 556.609 1.00 66.40 O ANISOU 286 O HIS A 53 9856 10866 4507 2419 -299 -20 O ATOM 287 CB HIS A 53 175.400 35.934 558.385 1.00 58.61 C ANISOU 287 CB HIS A 53 8997 10187 3084 2607 39 -292 C ATOM 288 CG HIS A 53 175.144 36.508 559.745 1.00 70.18 C ANISOU 288 CG HIS A 53 10536 11905 4224 2757 45 -438 C ATOM 289 ND1 HIS A 53 175.582 35.903 560.903 1.00 73.14 N ANISOU 289 ND1 HIS A 53 10925 12556 4309 2847 -25 -280 N ATOM 290 CD2 HIS A 53 174.492 37.631 560.130 1.00 70.74 C ANISOU 290 CD2 HIS A 53 10687 11988 4204 2862 108 -727 C ATOM 291 CE1 HIS A 53 175.213 36.629 561.943 1.00 70.46 C ANISOU 291 CE1 HIS A 53 10663 12412 3696 2988 1 -475 C ATOM 292 NE2 HIS A 53 174.551 37.683 561.502 1.00 76.48 N ANISOU 292 NE2 HIS A 53 11474 13011 4574 3012 78 -751 N ATOM 293 N LEU A 54 176.806 36.127 555.352 1.00 58.20 N ANISOU 293 N LEU A 54 8808 9459 3846 2210 -236 -506 N ATOM 294 CA LEU A 54 177.090 35.493 554.074 1.00 57.34 C ANISOU 294 CA LEU A 54 8548 9063 4177 2034 -234 -347 C ATOM 295 C LEU A 54 178.462 35.863 553.527 1.00 57.49 C ANISOU 295 C LEU A 54 8465 9017 4363 1893 -511 -558 C ATOM 296 O LEU A 54 178.793 35.474 552.405 1.00 53.95 O ANISOU 296 O LEU A 54 7878 8367 4254 1770 -517 -478 O ATOM 297 CB LEU A 54 176.014 35.857 553.049 1.00 55.52 C ANISOU 297 CB LEU A 54 8277 8571 4246 1926 -20 -355 C ATOM 298 CG LEU A 54 174.653 35.175 553.179 1.00 60.91 C ANISOU 298 CG LEU A 54 8938 9318 4886 1978 271 -43 C ATOM 299 CD1 LEU A 54 173.670 35.741 552.164 1.00 59.60 C ANISOU 299 CD1 LEU A 54 8696 8960 4988 1889 435 -111 C ATOM 300 CD2 LEU A 54 174.796 33.672 553.005 1.00 63.00 C ANISOU 300 CD2 LEU A 54 9167 9515 5256 1916 292 349 C ATOM 301 N GLN A 55 179.263 36.610 554.284 1.00 62.02 N ANISOU 301 N GLN A 55 9089 9792 4685 1893 -746 -826 N ATOM 302 CA GLN A 55 180.571 37.061 553.810 1.00 58.67 C ANISOU 302 CA GLN A 55 8517 9381 4392 1695 -1021 -1020 C ATOM 303 C GLN A 55 181.655 36.099 554.293 1.00 60.11 C ANISOU 303 C GLN A 55 8545 9878 4414 1824 -1203 -846 C ATOM 304 O GLN A 55 182.460 36.395 555.177 1.00 67.00 O ANISOU 304 O GLN A 55 9405 11066 4988 1848 -1446 -992 O ATOM 305 CB GLN A 55 180.834 38.492 554.267 1.00 58.56 C ANISOU 305 CB GLN A 55 8655 9375 4221 1551 -1212 -1428 C ATOM 306 CG GLN A 55 179.891 39.505 553.643 1.00 54.16 C ANISOU 306 CG GLN A 55 8271 8453 3853 1459 -1066 -1608 C ATOM 307 CD GLN A 55 180.153 40.918 554.114 1.00 63.15 C ANISOU 307 CD GLN A 55 9656 9506 4831 1332 -1282 -2025 C ATOM 308 OE1 GLN A 55 180.925 41.142 555.046 1.00 71.07 O ANISOU 308 OE1 GLN A 55 10678 10725 5599 1275 -1502 -2155 O ATOM 309 NE2 GLN A 55 179.509 41.884 553.470 1.00 64.28 N ANISOU 309 NE2 GLN A 55 9982 9277 5166 1253 -1204 -2192 N ATOM 310 N THR A 56 181.659 34.922 553.677 1.00 58.83 N ANISOU 310 N THR A 56 8283 9623 4449 1927 -1096 -537 N ATOM 311 CA THR A 56 182.628 33.875 553.960 1.00 57.21 C ANISOU 311 CA THR A 56 7953 9651 4131 2131 -1246 -332 C ATOM 312 C THR A 56 183.476 33.614 552.723 1.00 53.46 C ANISOU 312 C THR A 56 7225 9109 3977 2060 -1317 -330 C ATOM 313 O THR A 56 183.189 34.104 551.628 1.00 48.73 O ANISOU 313 O THR A 56 6569 8255 3691 1845 -1217 -432 O ATOM 314 CB THR A 56 181.933 32.583 554.407 1.00 59.97 C ANISOU 314 CB THR A 56 8477 9928 4381 2380 -1075 56 C ATOM 315 OG1 THR A 56 181.024 32.150 553.386 1.00 57.49 O ANISOU 315 OG1 THR A 56 8215 9219 4409 2285 -838 202 O ATOM 316 CG2 THR A 56 181.164 32.810 555.696 1.00 53.53 C ANISOU 316 CG2 THR A 56 7864 9293 3181 2470 -992 89 C ATOM 317 N VAL A 57 184.536 32.825 552.913 1.00 53.01 N ANISOU 317 N VAL A 57 7008 9324 3808 2284 -1490 -202 N ATOM 318 CA VAL A 57 185.436 32.505 551.807 1.00 54.74 C ANISOU 318 CA VAL A 57 6950 9585 4265 2301 -1555 -196 C ATOM 319 C VAL A 57 184.695 31.742 550.715 1.00 52.63 C ANISOU 319 C VAL A 57 6798 8883 4317 2353 -1322 -30 C ATOM 320 O VAL A 57 184.892 31.995 549.520 1.00 55.16 O ANISOU 320 O VAL A 57 6954 9099 4906 2212 -1276 -124 O ATOM 321 CB VAL A 57 186.657 31.720 552.320 1.00 58.64 C ANISOU 321 CB VAL A 57 7255 10494 4532 2631 -1775 -73 C ATOM 322 CG1 VAL A 57 187.584 31.369 551.168 1.00 58.50 C ANISOU 322 CG1 VAL A 57 6922 10560 4745 2694 -1798 -74 C ATOM 323 CG2 VAL A 57 187.400 32.528 553.371 1.00 57.81 C ANISOU 323 CG2 VAL A 57 7011 10758 4196 2461 -1970 -260 C ATOM 324 N ASN A 58 183.837 30.796 551.105 1.00 53.50 N ANISOU 324 N ASN A 58 7195 8747 4383 2531 -1180 227 N ATOM 325 CA ASN A 58 183.047 30.061 550.121 1.00 54.42 C ANISOU 325 CA ASN A 58 7458 8428 4791 2522 -986 374 C ATOM 326 C ASN A 58 182.198 31.008 549.283 1.00 49.82 C ANISOU 326 C ASN A 58 6846 7625 4457 2182 -825 198 C ATOM 327 O ASN A 58 182.167 30.908 548.051 1.00 49.87 O ANISOU 327 O ASN A 58 6777 7436 4736 2107 -761 156 O ATOM 328 CB ASN A 58 182.167 29.023 550.817 1.00 55.83 C ANISOU 328 CB ASN A 58 7964 8390 4860 2657 -874 696 C ATOM 329 CG ASN A 58 182.969 27.899 551.437 1.00 61.83 C ANISOU 329 CG ASN A 58 8821 9257 5416 3042 -1029 927 C ATOM 330 OD1 ASN A 58 184.091 27.619 551.020 1.00 70.22 O ANISOU 330 OD1 ASN A 58 9709 10475 6497 3271 -1187 866 O ATOM 331 ND2 ASN A 58 182.391 27.243 552.436 1.00 60.86 N ANISOU 331 ND2 ASN A 58 8971 9077 5078 3137 -979 1217 N ATOM 332 N ASN A 59 181.510 31.945 549.936 1.00 49.89 N ANISOU 332 N ASN A 59 6928 7679 4348 2013 -765 85 N ATOM 333 CA ASN A 59 180.643 32.860 549.206 1.00 45.35 C ANISOU 333 CA ASN A 59 6357 6891 3982 1755 -618 -66 C ATOM 334 C ASN A 59 181.427 33.907 548.425 1.00 50.66 C ANISOU 334 C ASN A 59 6824 7627 4799 1553 -732 -325 C ATOM 335 O ASN A 59 180.870 34.510 547.503 1.00 50.60 O ANISOU 335 O ASN A 59 6807 7402 5017 1367 -623 -410 O ATOM 336 CB ASN A 59 179.666 33.530 550.169 1.00 43.04 C ANISOU 336 CB ASN A 59 6225 6643 3485 1719 -516 -114 C ATOM 337 CG ASN A 59 178.755 32.529 550.861 1.00 46.91 C ANISOU 337 CG ASN A 59 6884 7106 3834 1852 -360 194 C ATOM 338 OD1 ASN A 59 178.362 31.522 550.272 1.00 46.61 O ANISOU 338 OD1 ASN A 59 6893 6842 3972 1853 -265 424 O ATOM 339 ND2 ASN A 59 178.420 32.801 552.117 1.00 50.98 N ANISOU 339 ND2 ASN A 59 7505 7855 4009 1946 -339 204 N ATOM 340 N TYR A 60 182.699 34.133 548.764 1.00 50.64 N ANISOU 340 N TYR A 60 6641 7941 4660 1568 -956 -426 N ATOM 341 CA TYR A 60 183.554 34.944 547.903 1.00 51.28 C ANISOU 341 CA TYR A 60 6475 8119 4889 1331 -1065 -601 C ATOM 342 C TYR A 60 183.766 34.259 546.560 1.00 48.94 C ANISOU 342 C TYR A 60 6028 7725 4843 1390 -974 -495 C ATOM 343 O TYR A 60 183.674 34.895 545.503 1.00 42.23 O ANISOU 343 O TYR A 60 5090 6751 4203 1166 -911 -577 O ATOM 344 CB TYR A 60 184.896 35.214 548.588 1.00 57.17 C ANISOU 344 CB TYR A 60 7002 9310 5410 1314 -1337 -699 C ATOM 345 CG TYR A 60 184.970 36.549 549.290 1.00 67.61 C ANISOU 345 CG TYR A 60 8404 10694 6590 1029 -1487 -954 C ATOM 346 CD1 TYR A 60 184.262 36.779 550.461 1.00 74.38 C ANISOU 346 CD1 TYR A 60 9547 11508 7206 1121 -1478 -1018 C ATOM 347 CD2 TYR A 60 185.754 37.579 548.785 1.00 72.80 C ANISOU 347 CD2 TYR A 60 8873 11453 7334 660 -1643 -1129 C ATOM 348 CE1 TYR A 60 184.326 37.995 551.107 1.00 81.06 C ANISOU 348 CE1 TYR A 60 10530 12374 7897 900 -1633 -1296 C ATOM 349 CE2 TYR A 60 185.826 38.801 549.426 1.00 79.76 C ANISOU 349 CE2 TYR A 60 9904 12312 8089 373 -1815 -1381 C ATOM 350 CZ TYR A 60 185.109 39.002 550.587 1.00 85.83 C ANISOU 350 CZ TYR A 60 10998 13000 8613 518 -1816 -1487 C ATOM 351 OH TYR A 60 185.174 40.215 551.233 1.00 93.89 O ANISOU 351 OH TYR A 60 12227 13963 9482 272 -2005 -1782 O ATOM 352 N PHE A 61 184.049 32.955 546.585 1.00 38.68 N ANISOU 352 N PHE A 61 4730 6466 3502 1716 -974 -313 N ATOM 353 CA PHE A 61 184.147 32.193 545.345 1.00 40.43 C ANISOU 353 CA PHE A 61 4886 6549 3926 1838 -887 -239 C ATOM 354 C PHE A 61 182.810 32.164 544.613 1.00 40.11 C ANISOU 354 C PHE A 61 5055 6077 4107 1701 -679 -205 C ATOM 355 O PHE A 61 182.760 32.310 543.386 1.00 42.23 O ANISOU 355 O PHE A 61 5229 6247 4570 1604 -605 -257 O ATOM 356 CB PHE A 61 184.625 30.773 545.641 1.00 42.83 C ANISOU 356 CB PHE A 61 5257 6899 4119 2264 -948 -61 C ATOM 357 CG PHE A 61 185.946 30.709 546.356 1.00 50.34 C ANISOU 357 CG PHE A 61 5963 8338 4825 2467 -1164 -72 C ATOM 358 CD1 PHE A 61 186.925 31.660 546.124 1.00 52.10 C ANISOU 358 CD1 PHE A 61 5806 8975 5015 2263 -1288 -236 C ATOM 359 CD2 PHE A 61 186.205 29.696 547.263 1.00 52.02 C ANISOU 359 CD2 PHE A 61 6321 8614 4829 2844 -1256 106 C ATOM 360 CE1 PHE A 61 188.140 31.600 546.783 1.00 57.55 C ANISOU 360 CE1 PHE A 61 6215 10187 5464 2424 -1507 -240 C ATOM 361 CE2 PHE A 61 187.416 29.630 547.926 1.00 57.80 C ANISOU 361 CE2 PHE A 61 6799 9850 5311 3064 -1472 105 C ATOM 362 CZ PHE A 61 188.386 30.582 547.686 1.00 60.58 C ANISOU 362 CZ PHE A 61 6730 10645 5641 2832 -1585 -80 C ATOM 363 N LEU A 62 181.712 31.973 545.351 1.00 42.70 N ANISOU 363 N LEU A 62 5641 6200 4382 1691 -582 -104 N ATOM 364 CA LEU A 62 180.395 31.967 544.721 1.00 42.97 C ANISOU 364 CA LEU A 62 5820 5905 4602 1544 -395 -58 C ATOM 365 C LEU A 62 180.013 33.348 544.205 1.00 38.86 C ANISOU 365 C LEU A 62 5216 5358 4191 1276 -341 -238 C ATOM 366 O LEU A 62 179.248 33.458 543.240 1.00 38.62 O ANISOU 366 O LEU A 62 5201 5121 4351 1164 -220 -235 O ATOM 367 CB LEU A 62 179.342 31.455 545.704 1.00 41.64 C ANISOU 367 CB LEU A 62 5884 5625 4312 1581 -297 125 C ATOM 368 CG LEU A 62 179.537 30.029 546.225 1.00 44.96 C ANISOU 368 CG LEU A 62 6476 5974 4632 1816 -343 367 C ATOM 369 CD1 LEU A 62 178.380 29.628 547.127 1.00 44.39 C ANISOU 369 CD1 LEU A 62 6611 5815 4440 1763 -217 591 C ATOM 370 CD2 LEU A 62 179.696 29.040 545.079 1.00 43.42 C ANISOU 370 CD2 LEU A 62 6340 5518 4640 1905 -349 418 C ATOM 371 N PHE A 63 180.527 34.407 544.834 1.00 40.79 N ANISOU 371 N PHE A 63 5401 5791 4308 1174 -449 -394 N ATOM 372 CA PHE A 63 180.270 35.759 544.349 1.00 39.72 C ANISOU 372 CA PHE A 63 5252 5565 4273 927 -432 -564 C ATOM 373 C PHE A 63 180.887 35.964 542.972 1.00 38.39 C ANISOU 373 C PHE A 63 4885 5399 4302 791 -445 -593 C ATOM 374 O PHE A 63 180.239 36.487 542.058 1.00 30.67 O ANISOU 374 O PHE A 63 3936 4225 3492 658 -341 -612 O ATOM 375 CB PHE A 63 180.819 36.784 545.343 1.00 37.22 C ANISOU 375 CB PHE A 63 4968 5411 3765 824 -593 -743 C ATOM 376 CG PHE A 63 180.459 38.203 545.012 1.00 38.19 C ANISOU 376 CG PHE A 63 5193 5347 3970 591 -596 -920 C ATOM 377 CD1 PHE A 63 181.266 38.964 544.182 1.00 41.14 C ANISOU 377 CD1 PHE A 63 5430 5729 4473 323 -699 -1000 C ATOM 378 CD2 PHE A 63 179.314 38.777 545.536 1.00 40.72 C ANISOU 378 CD2 PHE A 63 5757 5495 4222 656 -494 -989 C ATOM 379 CE1 PHE A 63 180.935 40.270 543.877 1.00 43.13 C ANISOU 379 CE1 PHE A 63 5845 5739 4804 104 -719 -1134 C ATOM 380 CE2 PHE A 63 178.978 40.083 545.235 1.00 42.81 C ANISOU 380 CE2 PHE A 63 6176 5538 4553 507 -510 -1155 C ATOM 381 CZ PHE A 63 179.789 40.830 544.405 1.00 43.29 C ANISOU 381 CZ PHE A 63 6158 5527 4762 220 -633 -1223 C ATOM 382 N SER A 64 182.150 35.561 542.812 1.00 40.33 N ANISOU 382 N SER A 64 4907 5916 4499 848 -568 -585 N ATOM 383 CA SER A 64 182.805 35.658 541.512 1.00 39.95 C ANISOU 383 CA SER A 64 4626 5967 4588 755 -560 -590 C ATOM 384 C SER A 64 182.102 34.791 540.476 1.00 35.52 C ANISOU 384 C SER A 64 4132 5186 4177 896 -405 -499 C ATOM 385 O SER A 64 181.974 35.182 539.309 1.00 33.64 O ANISOU 385 O SER A 64 3816 4891 4074 763 -332 -515 O ATOM 386 CB SER A 64 184.274 35.261 541.644 1.00 41.62 C ANISOU 386 CB SER A 64 4539 6607 4668 864 -710 -583 C ATOM 387 OG SER A 64 184.912 35.238 540.381 1.00 45.50 O ANISOU 387 OG SER A 64 4769 7272 5248 827 -673 -567 O ATOM 388 N LEU A 65 181.642 33.606 540.885 1.00 31.27 N ANISOU 388 N LEU A 65 3761 4516 3604 1145 -368 -395 N ATOM 389 CA LEU A 65 180.905 32.741 539.970 1.00 35.96 C ANISOU 389 CA LEU A 65 4473 4855 4335 1233 -257 -327 C ATOM 390 C LEU A 65 179.579 33.375 539.566 1.00 37.39 C ANISOU 390 C LEU A 65 4766 4793 4647 1017 -128 -331 C ATOM 391 O LEU A 65 179.158 33.269 538.408 1.00 31.72 O ANISOU 391 O LEU A 65 4033 3958 4060 966 -58 -338 O ATOM 392 CB LEU A 65 180.679 31.374 540.616 1.00 37.46 C ANISOU 392 CB LEU A 65 4876 4901 4456 1484 -274 -192 C ATOM 393 CG LEU A 65 180.291 30.232 539.679 1.00 42.70 C ANISOU 393 CG LEU A 65 5691 5301 5233 1610 -232 -144 C ATOM 394 CD1 LEU A 65 181.383 29.995 538.647 1.00 44.93 C ANISOU 394 CD1 LEU A 65 5789 5769 5515 1798 -279 -246 C ATOM 395 CD2 LEU A 65 180.017 28.968 540.474 1.00 44.62 C ANISOU 395 CD2 LEU A 65 6218 5327 5407 1797 -270 22 C ATOM 396 N ALA A 66 178.907 34.040 540.510 1.00 37.08 N ANISOU 396 N ALA A 66 4832 4714 4545 925 -101 -335 N ATOM 397 CA ALA A 66 177.674 34.747 540.184 1.00 32.83 C ANISOU 397 CA ALA A 66 4366 4009 4099 784 18 -344 C ATOM 398 C ALA A 66 177.942 35.965 539.308 1.00 37.55 C ANISOU 398 C ALA A 66 4866 4611 4789 611 6 -452 C ATOM 399 O ALA A 66 177.066 36.376 538.539 1.00 35.60 O ANISOU 399 O ALA A 66 4645 4229 4653 538 96 -441 O ATOM 400 CB ALA A 66 176.947 35.156 541.465 1.00 28.62 C ANISOU 400 CB ALA A 66 3965 3484 3425 807 57 -335 C ATOM 401 N ACYS A 67 179.138 36.551 539.412 0.50 40.38 N ANISOU 401 N ACYS A 67 5106 5141 5095 526 -114 -534 N ATOM 402 N BCYS A 67 179.134 36.558 539.411 0.50 40.37 N ANISOU 402 N BCYS A 67 5106 5139 5094 525 -114 -534 N ATOM 403 CA ACYS A 67 179.486 37.680 538.556 0.50 39.35 C ANISOU 403 CA ACYS A 67 4897 5006 5050 302 -136 -590 C ATOM 404 CA BCYS A 67 179.480 37.682 538.546 0.50 39.33 C ANISOU 404 CA BCYS A 67 4895 5002 5049 301 -135 -589 C ATOM 405 C ACYS A 67 179.643 37.242 537.104 0.50 38.32 C ANISOU 405 C ACYS A 67 4619 4916 5027 304 -70 -527 C ATOM 406 C BCYS A 67 179.626 37.232 537.098 0.50 38.30 C ANISOU 406 C BCYS A 67 4618 4911 5025 305 -68 -526 C ATOM 407 O ACYS A 67 179.152 37.915 536.190 0.50 37.45 O ANISOU 407 O ACYS A 67 4527 4690 5013 180 -8 -509 O ATOM 408 O BCYS A 67 179.120 37.888 536.180 0.50 37.33 O ANISOU 408 O BCYS A 67 4514 4670 4999 185 -5 -508 O ATOM 409 CB ACYS A 67 180.767 38.345 539.061 0.50 40.49 C ANISOU 409 CB ACYS A 67 4923 5364 5098 140 -299 -668 C ATOM 410 CB BCYS A 67 180.767 38.348 539.032 0.50 40.49 C ANISOU 410 CB BCYS A 67 4920 5363 5101 138 -298 -667 C ATOM 411 SG ACYS A 67 181.330 39.738 538.057 0.50 40.47 S ANISOU 411 SG ACYS A 67 4836 5351 5192 -232 -348 -682 S ATOM 412 SG BCYS A 67 180.599 39.279 540.568 0.50 40.21 S ANISOU 412 SG BCYS A 67 5112 5246 4918 68 -413 -809 S ATOM 413 N ALA A 68 180.328 36.118 536.874 1.00 35.99 N ANISOU 413 N ALA A 68 4195 4790 4689 482 -89 -498 N ATOM 414 CA ALA A 68 180.463 35.593 535.520 1.00 35.41 C ANISOU 414 CA ALA A 68 4012 4771 4672 548 -27 -473 C ATOM 415 C ALA A 68 179.114 35.153 534.963 1.00 33.19 C ANISOU 415 C ALA A 68 3905 4217 4490 586 71 -443 C ATOM 416 O ALA A 68 178.825 35.358 533.779 1.00 26.80 O ANISOU 416 O ALA A 68 3050 3394 3739 526 128 -438 O ATOM 417 CB ALA A 68 181.460 34.433 535.506 1.00 31.10 C ANISOU 417 CB ALA A 68 3342 4446 4028 818 -79 -478 C ATOM 418 N ASP A 69 178.275 34.544 535.806 1.00 31.47 N ANISOU 418 N ASP A 69 3866 3819 4271 665 87 -406 N ATOM 419 CA ASP A 69 176.943 34.142 535.367 1.00 31.80 C ANISOU 419 CA ASP A 69 4029 3655 4398 639 165 -359 C ATOM 420 C ASP A 69 176.093 35.352 535.004 1.00 33.29 C ANISOU 420 C ASP A 69 4208 3792 4647 486 230 -357 C ATOM 421 O ASP A 69 175.297 35.300 534.059 1.00 34.51 O ANISOU 421 O ASP A 69 4357 3885 4871 445 278 -334 O ATOM 422 CB ASP A 69 176.260 33.316 536.456 1.00 27.72 C ANISOU 422 CB ASP A 69 3672 3014 3845 700 174 -273 C ATOM 423 CG ASP A 69 176.934 31.981 536.684 1.00 33.88 C ANISOU 423 CG ASP A 69 4541 3757 4576 885 100 -244 C ATOM 424 OD1 ASP A 69 177.505 31.439 535.718 1.00 35.39 O ANISOU 424 OD1 ASP A 69 4704 3956 4787 991 64 -307 O ATOM 425 OD2 ASP A 69 176.894 31.473 537.825 1.00 39.41 O ANISOU 425 OD2 ASP A 69 5358 4422 5195 956 77 -156 O ATOM 426 N LEU A 70 176.241 36.450 535.749 1.00 28.95 N ANISOU 426 N LEU A 70 3683 3260 4059 420 214 -390 N ATOM 427 CA LEU A 70 175.494 37.663 535.433 1.00 26.51 C ANISOU 427 CA LEU A 70 3424 2855 3795 335 259 -395 C ATOM 428 C LEU A 70 175.914 38.237 534.085 1.00 32.96 C ANISOU 428 C LEU A 70 4150 3698 4673 224 253 -381 C ATOM 429 O LEU A 70 175.064 38.665 533.296 1.00 31.84 O ANISOU 429 O LEU A 70 4030 3484 4586 212 306 -336 O ATOM 430 CB LEU A 70 175.682 38.698 536.542 1.00 27.16 C ANISOU 430 CB LEU A 70 3623 2895 3802 309 211 -471 C ATOM 431 CG LEU A 70 174.990 40.047 536.338 1.00 34.89 C ANISOU 431 CG LEU A 70 4736 3711 4810 281 233 -499 C ATOM 432 CD1 LEU A 70 173.487 39.862 536.190 1.00 34.94 C ANISOU 432 CD1 LEU A 70 4755 3690 4832 429 353 -435 C ATOM 433 CD2 LEU A 70 175.312 40.991 537.490 1.00 37.76 C ANISOU 433 CD2 LEU A 70 5280 3994 5073 268 150 -625 C ATOM 434 N ILE A 71 177.220 38.256 533.807 1.00 36.47 N ANISOU 434 N ILE A 71 4469 4300 5087 148 191 -398 N ATOM 435 CA ILE A 71 177.706 38.759 532.524 1.00 32.28 C ANISOU 435 CA ILE A 71 3821 3867 4578 25 204 -347 C ATOM 436 C ILE A 71 177.148 37.922 531.379 1.00 30.34 C ANISOU 436 C ILE A 71 3526 3654 4348 138 269 -322 C ATOM 437 O ILE A 71 176.761 38.455 530.331 1.00 29.91 O ANISOU 437 O ILE A 71 3458 3593 4311 75 308 -261 O ATOM 438 CB ILE A 71 179.246 38.787 532.510 1.00 33.37 C ANISOU 438 CB ILE A 71 3758 4278 4644 -72 138 -352 C ATOM 439 CG1 ILE A 71 179.774 39.742 533.583 1.00 33.05 C ANISOU 439 CG1 ILE A 71 3778 4199 4581 -257 33 -391 C ATOM 440 CG2 ILE A 71 179.764 39.181 531.133 1.00 25.98 C ANISOU 440 CG2 ILE A 71 2658 3524 3691 -198 180 -263 C ATOM 441 CD1 ILE A 71 181.274 39.686 533.768 1.00 34.28 C ANISOU 441 CD1 ILE A 71 3681 4695 4647 -373 -57 -393 C ATOM 442 N ILE A 72 177.088 36.601 531.564 1.00 25.19 N ANISOU 442 N ILE A 72 2880 3016 3676 303 264 -368 N ATOM 443 CA ILE A 72 176.521 35.725 530.541 1.00 29.58 C ANISOU 443 CA ILE A 72 3447 3555 4237 392 289 -383 C ATOM 444 C ILE A 72 175.050 36.051 530.313 1.00 33.21 C ANISOU 444 C ILE A 72 3989 3866 4764 330 326 -335 C ATOM 445 O ILE A 72 174.576 36.092 529.170 1.00 33.70 O ANISOU 445 O ILE A 72 4017 3969 4820 314 340 -322 O ATOM 446 CB ILE A 72 176.719 34.249 530.934 1.00 33.25 C ANISOU 446 CB ILE A 72 3991 3968 4675 567 245 -443 C ATOM 447 CG1 ILE A 72 178.207 33.892 530.935 1.00 32.35 C ANISOU 447 CG1 ILE A 72 3751 4078 4462 715 209 -492 C ATOM 448 CG2 ILE A 72 175.944 33.332 529.998 1.00 39.54 C ANISOU 448 CG2 ILE A 72 4880 4658 5485 611 235 -486 C ATOM 449 CD1 ILE A 72 178.878 34.073 529.597 1.00 27.23 C ANISOU 449 CD1 ILE A 72 2931 3684 3733 748 243 -518 C ATOM 450 N GLY A 73 174.306 36.293 531.394 1.00 29.61 N ANISOU 450 N GLY A 73 3617 3293 4341 317 343 -306 N ATOM 451 CA GLY A 73 172.894 36.604 531.257 1.00 35.70 C ANISOU 451 CA GLY A 73 4407 4008 5149 299 386 -249 C ATOM 452 C GLY A 73 172.627 37.961 530.638 1.00 37.98 C ANISOU 452 C GLY A 73 4687 4297 5446 275 409 -204 C ATOM 453 O GLY A 73 171.607 38.151 529.971 1.00 38.42 O ANISOU 453 O GLY A 73 4706 4379 5511 297 429 -151 O ATOM 454 N VAL A 74 173.527 38.920 530.849 1.00 38.81 N ANISOU 454 N VAL A 74 4834 4369 5541 219 389 -210 N ATOM 455 CA VAL A 74 173.316 40.272 530.336 1.00 34.96 C ANISOU 455 CA VAL A 74 4420 3798 5067 181 391 -143 C ATOM 456 C VAL A 74 173.812 40.391 528.900 1.00 40.76 C ANISOU 456 C VAL A 74 5061 4649 5776 97 390 -69 C ATOM 457 O VAL A 74 173.069 40.794 527.997 1.00 38.93 O ANISOU 457 O VAL A 74 4835 4423 5536 137 407 15 O ATOM 458 CB VAL A 74 173.997 41.307 531.250 1.00 34.07 C ANISOU 458 CB VAL A 74 4453 3541 4951 100 342 -181 C ATOM 459 CG1 VAL A 74 173.932 42.692 530.624 1.00 28.88 C ANISOU 459 CG1 VAL A 74 3940 2719 4313 27 319 -94 C ATOM 460 CG2 VAL A 74 173.347 41.312 532.625 1.00 33.67 C ANISOU 460 CG2 VAL A 74 4515 3404 4873 237 355 -262 C ATOM 461 N PHE A 75 175.078 40.046 528.668 1.00 42.28 N ANISOU 461 N PHE A 75 5145 4991 5929 5 373 -87 N ATOM 462 CA PHE A 75 175.707 40.274 527.373 1.00 41.42 C ANISOU 462 CA PHE A 75 4923 5064 5752 -80 393 1 C ATOM 463 C PHE A 75 175.603 39.067 526.445 1.00 39.98 C ANISOU 463 C PHE A 75 4623 5075 5494 51 414 -59 C ATOM 464 O PHE A 75 175.134 39.194 525.310 1.00 40.96 O ANISOU 464 O PHE A 75 4723 5282 5556 72 433 2 O ATOM 465 CB PHE A 75 177.180 40.655 527.566 1.00 41.03 C ANISOU 465 CB PHE A 75 4766 5159 5663 -259 370 31 C ATOM 466 CG PHE A 75 177.381 41.982 528.244 1.00 42.94 C ANISOU 466 CG PHE A 75 5166 5185 5964 -464 313 89 C ATOM 467 CD1 PHE A 75 177.479 43.146 527.501 1.00 43.95 C ANISOU 467 CD1 PHE A 75 5378 5232 6091 -657 308 258 C ATOM 468 CD2 PHE A 75 177.481 42.063 529.623 1.00 43.16 C ANISOU 468 CD2 PHE A 75 5298 5068 6031 -467 249 -25 C ATOM 469 CE1 PHE A 75 177.667 44.369 528.120 1.00 43.55 C ANISOU 469 CE1 PHE A 75 5551 4899 6098 -863 224 296 C ATOM 470 CE2 PHE A 75 177.669 43.283 530.249 1.00 42.69 C ANISOU 470 CE2 PHE A 75 5438 4774 6007 -654 167 -16 C ATOM 471 CZ PHE A 75 177.763 44.437 529.495 1.00 42.92 C ANISOU 471 CZ PHE A 75 5590 4663 6056 -859 146 137 C ATOM 472 N SER A 76 176.030 37.894 526.914 1.00 35.77 N ANISOU 472 N SER A 76 4050 4597 4946 159 396 -185 N ATOM 473 CA SER A 76 176.221 36.756 526.020 1.00 32.07 C ANISOU 473 CA SER A 76 3522 4286 4379 303 394 -278 C ATOM 474 C SER A 76 174.898 36.240 525.467 1.00 35.45 C ANISOU 474 C SER A 76 4041 4606 4821 345 365 -317 C ATOM 475 O SER A 76 174.756 36.050 524.253 1.00 35.26 O ANISOU 475 O SER A 76 3980 4727 4690 387 363 -337 O ATOM 476 CB SER A 76 176.971 35.645 526.751 1.00 31.33 C ANISOU 476 CB SER A 76 3430 4206 4268 450 359 -398 C ATOM 477 OG SER A 76 178.271 36.077 527.119 1.00 40.61 O ANISOU 477 OG SER A 76 4450 5588 5393 417 370 -363 O ATOM 478 N MET A 77 173.922 35.991 526.344 1.00 32.80 N ANISOU 478 N MET A 77 3804 4066 4594 322 340 -323 N ATOM 479 CA MET A 77 172.661 35.407 525.897 1.00 32.57 C ANISOU 479 CA MET A 77 3813 3987 4576 306 294 -349 C ATOM 480 C MET A 77 171.944 36.315 524.905 1.00 28.27 C ANISOU 480 C MET A 77 3198 3557 3986 277 305 -253 C ATOM 481 O MET A 77 171.442 35.847 523.877 1.00 31.73 O ANISOU 481 O MET A 77 3614 4098 4343 284 251 -299 O ATOM 482 CB MET A 77 171.760 35.109 527.095 1.00 33.20 C ANISOU 482 CB MET A 77 3949 3907 4757 254 289 -319 C ATOM 483 CG MET A 77 172.178 33.900 527.912 1.00 36.60 C ANISOU 483 CG MET A 77 4493 4200 5212 280 251 -391 C ATOM 484 SD MET A 77 171.054 33.618 529.292 0.78 28.74 S ANISOU 484 SD MET A 77 3538 3086 4296 181 271 -292 S ATOM 485 CE MET A 77 171.644 32.042 529.898 1.00 27.24 C ANISOU 485 CE MET A 77 3544 2696 4110 210 196 -347 C ATOM 486 N ASN A 78 171.890 37.617 525.193 1.00 28.06 N ANISOU 486 N ASN A 78 3168 3499 3995 257 355 -123 N ATOM 487 CA ASN A 78 171.125 38.526 524.344 1.00 34.41 C ANISOU 487 CA ASN A 78 3945 4374 4754 277 355 0 C ATOM 488 C ASN A 78 171.795 38.729 522.990 1.00 39.16 C ANISOU 488 C ASN A 78 4497 5165 5215 270 361 46 C ATOM 489 O ASN A 78 171.117 38.746 521.956 1.00 39.91 O ANISOU 489 O ASN A 78 4549 5404 5211 311 324 83 O ATOM 490 CB ASN A 78 170.922 39.859 525.062 1.00 36.62 C ANISOU 490 CB ASN A 78 4316 4495 5104 297 392 116 C ATOM 491 CG ASN A 78 169.965 39.747 526.231 1.00 40.43 C ANISOU 491 CG ASN A 78 4816 4882 5662 368 403 85 C ATOM 492 OD1 ASN A 78 168.942 39.067 526.145 1.00 40.64 O ANISOU 492 OD1 ASN A 78 4743 5017 5683 389 382 69 O ATOM 493 ND2 ASN A 78 170.296 40.407 527.333 1.00 41.70 N ANISOU 493 ND2 ASN A 78 5095 4876 5874 385 431 77 N ATOM 494 N LEU A 79 173.122 38.882 522.970 1.00 37.39 N ANISOU 494 N LEU A 79 4250 5005 4953 218 406 55 N ATOM 495 CA LEU A 79 173.820 39.039 521.697 1.00 38.61 C ANISOU 495 CA LEU A 79 4317 5421 4933 213 439 121 C ATOM 496 C LEU A 79 173.712 37.778 520.849 1.00 35.08 C ANISOU 496 C LEU A 79 3826 5157 4345 338 399 -55 C ATOM 497 O LEU A 79 173.582 37.856 519.622 1.00 36.45 O ANISOU 497 O LEU A 79 3954 5552 4341 383 397 -18 O ATOM 498 CB LEU A 79 175.286 39.405 521.935 1.00 39.05 C ANISOU 498 CB LEU A 79 4290 5585 4961 108 500 180 C ATOM 499 CG LEU A 79 175.550 40.841 522.396 1.00 42.63 C ANISOU 499 CG LEU A 79 4822 5874 5502 -87 514 377 C ATOM 500 CD1 LEU A 79 177.041 41.104 522.523 1.00 44.72 C ANISOU 500 CD1 LEU A 79 4946 6329 5717 -260 553 442 C ATOM 501 CD2 LEU A 79 174.909 41.839 521.447 1.00 44.56 C ANISOU 501 CD2 LEU A 79 5150 6096 5686 -115 517 588 C ATOM 502 N TYR A 80 173.765 36.605 521.483 1.00 29.70 N ANISOU 502 N TYR A 80 3195 4366 3722 403 353 -249 N ATOM 503 CA TYR A 80 173.646 35.360 520.731 1.00 32.24 C ANISOU 503 CA TYR A 80 3564 4770 3917 524 281 -452 C ATOM 504 C TYR A 80 172.230 35.171 520.197 1.00 34.30 C ANISOU 504 C TYR A 80 3865 4998 4169 470 179 -475 C ATOM 505 O TYR A 80 172.041 34.628 519.103 1.00 32.86 O ANISOU 505 O TYR A 80 3703 4972 3811 534 109 -594 O ATOM 506 CB TYR A 80 174.060 34.176 521.603 1.00 28.52 C ANISOU 506 CB TYR A 80 3202 4113 3521 606 239 -628 C ATOM 507 CG TYR A 80 174.251 32.893 520.830 1.00 25.57 C ANISOU 507 CG TYR A 80 2947 3774 2995 779 157 -866 C ATOM 508 CD1 TYR A 80 175.255 32.780 519.878 1.00 30.18 C ANISOU 508 CD1 TYR A 80 3454 4668 3346 979 212 -941 C ATOM 509 CD2 TYR A 80 173.433 31.794 521.054 1.00 28.07 C ANISOU 509 CD2 TYR A 80 3469 3816 3381 739 20 -1016 C ATOM 510 CE1 TYR A 80 175.436 31.612 519.166 1.00 29.12 C ANISOU 510 CE1 TYR A 80 3475 4552 3039 1201 130 -1200 C ATOM 511 CE2 TYR A 80 173.608 30.619 520.347 1.00 30.84 C ANISOU 511 CE2 TYR A 80 4010 4120 3587 898 -87 -1265 C ATOM 512 CZ TYR A 80 174.612 30.535 519.405 1.00 29.70 C ANISOU 512 CZ TYR A 80 3817 4269 3199 1163 -33 -1377 C ATOM 513 OH TYR A 80 174.793 29.369 518.697 1.00 32.62 O ANISOU 513 OH TYR A 80 4419 4580 3393 1386 -145 -1665 O ATOM 514 N THR A 81 171.224 35.611 520.957 1.00 34.58 N ANISOU 514 N THR A 81 3896 4877 4366 365 163 -372 N ATOM 515 CA THR A 81 169.848 35.546 520.474 1.00 41.54 C ANISOU 515 CA THR A 81 4736 5820 5226 307 66 -357 C ATOM 516 C THR A 81 169.645 36.460 519.273 1.00 43.30 C ANISOU 516 C THR A 81 4876 6292 5284 367 72 -224 C ATOM 517 O THR A 81 168.984 36.079 518.299 1.00 35.04 O ANISOU 517 O THR A 81 3796 5423 4094 370 -35 -289 O ATOM 518 CB THR A 81 168.878 35.917 521.596 1.00 36.86 C ANISOU 518 CB THR A 81 4101 5095 4807 235 80 -249 C ATOM 519 OG1 THR A 81 169.088 35.047 522.715 1.00 39.82 O ANISOU 519 OG1 THR A 81 4563 5259 5307 171 80 -339 O ATOM 520 CG2 THR A 81 167.439 35.786 521.123 1.00 38.36 C ANISOU 520 CG2 THR A 81 4174 5439 4960 172 -25 -223 C ATOM 521 N LEU A 82 170.208 37.670 519.326 1.00 43.53 N ANISOU 521 N LEU A 82 4892 6327 5319 396 179 -29 N ATOM 522 CA LEU A 82 170.160 38.566 518.176 1.00 44.43 C ANISOU 522 CA LEU A 82 4968 6653 5260 448 193 147 C ATOM 523 C LEU A 82 170.858 37.949 516.971 1.00 44.96 C ANISOU 523 C LEU A 82 5006 7000 5077 503 187 43 C ATOM 524 O LEU A 82 170.390 38.079 515.834 1.00 44.00 O ANISOU 524 O LEU A 82 4847 7121 4751 561 131 86 O ATOM 525 CB LEU A 82 170.800 39.906 518.536 1.00 42.63 C ANISOU 525 CB LEU A 82 4795 6305 5098 411 297 382 C ATOM 526 CG LEU A 82 170.754 40.988 517.457 1.00 49.35 C ANISOU 526 CG LEU A 82 5662 7303 5788 440 314 640 C ATOM 527 CD1 LEU A 82 169.321 41.438 517.232 1.00 50.99 C ANISOU 527 CD1 LEU A 82 5871 7513 5990 570 226 735 C ATOM 528 CD2 LEU A 82 171.640 42.161 517.841 1.00 47.18 C ANISOU 528 CD2 LEU A 82 5490 6851 5585 317 401 857 C ATOM 529 N TYR A 83 171.985 37.274 517.207 1.00 39.05 N ANISOU 529 N TYR A 83 4269 6258 4312 524 243 -101 N ATOM 530 CA TYR A 83 172.729 36.634 516.127 1.00 38.57 C ANISOU 530 CA TYR A 83 4179 6497 3979 650 257 -233 C ATOM 531 C TYR A 83 171.896 35.551 515.451 1.00 41.33 C ANISOU 531 C TYR A 83 4610 6890 4203 716 95 -486 C ATOM 532 O TYR A 83 171.767 35.526 514.221 1.00 41.21 O ANISOU 532 O TYR A 83 4572 7170 3915 801 56 -512 O ATOM 533 CB TYR A 83 174.031 36.054 516.685 1.00 34.35 C ANISOU 533 CB TYR A 83 3628 5963 3461 722 338 -354 C ATOM 534 CG TYR A 83 174.973 35.459 515.660 1.00 37.76 C ANISOU 534 CG TYR A 83 4000 6763 3582 926 389 -488 C ATOM 535 CD1 TYR A 83 174.956 35.877 514.336 1.00 33.81 C ANISOU 535 CD1 TYR A 83 3425 6632 2791 980 423 -393 C ATOM 536 CD2 TYR A 83 175.882 34.475 516.024 1.00 45.13 C ANISOU 536 CD2 TYR A 83 4957 7706 4485 1111 406 -707 C ATOM 537 CE1 TYR A 83 175.821 35.329 513.403 1.00 36.41 C ANISOU 537 CE1 TYR A 83 3686 7359 2788 1209 488 -526 C ATOM 538 CE2 TYR A 83 176.748 33.922 515.101 1.00 48.81 C ANISOU 538 CE2 TYR A 83 5362 8551 4634 1376 463 -850 C ATOM 539 CZ TYR A 83 176.714 34.352 513.793 1.00 55.03 C ANISOU 539 CZ TYR A 83 6059 9732 5118 1422 512 -766 C ATOM 540 OH TYR A 83 177.580 33.798 512.877 1.00 60.00 O ANISOU 540 OH TYR A 83 6616 10790 5392 1721 583 -916 O ATOM 541 N THR A 84 171.313 34.648 516.242 1.00 38.82 N ANISOU 541 N THR A 84 4399 6284 4067 649 -15 -665 N ATOM 542 CA THR A 84 170.621 33.501 515.663 1.00 43.98 C ANISOU 542 CA THR A 84 5175 6922 4615 645 -201 -930 C ATOM 543 C THR A 84 169.268 33.883 515.072 1.00 43.42 C ANISOU 543 C THR A 84 5013 6994 4491 529 -328 -846 C ATOM 544 O THR A 84 168.853 33.304 514.062 1.00 44.29 O ANISOU 544 O THR A 84 5172 7272 4382 544 -478 -1022 O ATOM 545 CB THR A 84 170.454 32.406 516.718 1.00 47.96 C ANISOU 545 CB THR A 84 5845 7046 5332 555 -285 -1103 C ATOM 546 OG1 THR A 84 169.714 32.922 517.831 1.00 45.91 O ANISOU 546 OG1 THR A 84 5499 6614 5332 377 -257 -911 O ATOM 547 CG2 THR A 84 171.817 31.929 517.205 1.00 51.01 C ANISOU 547 CG2 THR A 84 6322 7334 5724 741 -187 -1203 C ATOM 548 N VAL A 85 168.572 34.850 515.674 1.00 41.79 N ANISOU 548 N VAL A 85 4676 6748 4454 443 -282 -592 N ATOM 549 CA VAL A 85 167.247 35.225 515.184 1.00 42.71 C ANISOU 549 CA VAL A 85 4662 7053 4513 384 -405 -495 C ATOM 550 C VAL A 85 167.355 35.996 513.873 1.00 42.59 C ANISOU 550 C VAL A 85 4584 7384 4213 528 -395 -362 C ATOM 551 O VAL A 85 166.608 35.736 512.921 1.00 46.05 O ANISOU 551 O VAL A 85 4970 8080 4446 527 -556 -433 O ATOM 552 CB VAL A 85 166.487 36.026 516.257 1.00 40.61 C ANISOU 552 CB VAL A 85 4280 6665 4484 337 -346 -274 C ATOM 553 CG1 VAL A 85 165.287 36.733 515.652 1.00 47.45 C ANISOU 553 CG1 VAL A 85 4969 7812 5246 388 -435 -107 C ATOM 554 CG2 VAL A 85 166.044 35.107 517.384 1.00 44.07 C ANISOU 554 CG2 VAL A 85 4742 6867 5136 157 -394 -395 C ATOM 555 N ILE A 86 168.283 36.953 513.798 1.00 44.72 N ANISOU 555 N ILE A 86 4859 7682 4450 628 -218 -152 N ATOM 556 CA ILE A 86 168.449 37.725 512.571 1.00 47.61 C ANISOU 556 CA ILE A 86 5182 8375 4530 743 -190 35 C ATOM 557 C ILE A 86 169.050 36.863 511.464 1.00 48.83 C ANISOU 557 C ILE A 86 5379 8813 4361 833 -229 -197 C ATOM 558 O ILE A 86 168.753 37.063 510.279 1.00 48.69 O ANISOU 558 O ILE A 86 5323 9140 4036 923 -295 -148 O ATOM 559 CB ILE A 86 169.294 38.984 512.855 1.00 51.69 C ANISOU 559 CB ILE A 86 5717 8808 5115 749 0 354 C ATOM 560 CG1 ILE A 86 168.475 40.001 513.656 1.00 56.49 C ANISOU 560 CG1 ILE A 86 6336 9173 5953 742 -1 581 C ATOM 561 CG2 ILE A 86 169.807 39.615 511.573 1.00 49.49 C ANISOU 561 CG2 ILE A 86 5417 8877 4510 829 64 562 C ATOM 562 CD1 ILE A 86 169.047 41.405 513.634 1.00 60.43 C ANISOU 562 CD1 ILE A 86 6924 9573 6464 744 121 927 C ATOM 563 N GLY A 87 169.873 35.879 511.821 1.00 48.58 N ANISOU 563 N GLY A 87 5440 8656 4363 853 -198 -462 N ATOM 564 CA GLY A 87 170.473 34.982 510.855 1.00 51.61 C ANISOU 564 CA GLY A 87 5901 9281 4425 1012 -234 -735 C ATOM 565 C GLY A 87 171.886 35.339 510.444 1.00 54.28 C ANISOU 565 C GLY A 87 6172 9890 4562 1166 -18 -632 C ATOM 566 O GLY A 87 172.512 34.568 509.705 1.00 62.10 O ANISOU 566 O GLY A 87 7216 11122 5257 1369 -16 -877 O ATOM 567 N TYR A 88 172.401 36.478 510.895 1.00 49.19 N ANISOU 567 N TYR A 88 5412 9229 4050 1073 155 -282 N ATOM 568 CA TYR A 88 173.775 36.886 510.633 1.00 50.70 C ANISOU 568 CA TYR A 88 5482 9704 4078 1131 365 -129 C ATOM 569 C TYR A 88 174.174 37.868 511.726 1.00 47.68 C ANISOU 569 C TYR A 88 5045 9057 4015 921 478 158 C ATOM 570 O TYR A 88 173.368 38.213 512.594 1.00 44.43 O ANISOU 570 O TYR A 88 4713 8265 3905 795 402 214 O ATOM 571 CB TYR A 88 173.923 37.494 509.233 1.00 54.71 C ANISOU 571 CB TYR A 88 5900 10706 4181 1207 431 82 C ATOM 572 CG TYR A 88 173.073 38.724 508.994 1.00 54.07 C ANISOU 572 CG TYR A 88 5827 10571 4145 1070 397 456 C ATOM 573 CD1 TYR A 88 171.765 38.610 508.543 1.00 55.75 C ANISOU 573 CD1 TYR A 88 6106 10777 4302 1117 202 390 C ATOM 574 CD2 TYR A 88 173.582 39.998 509.214 1.00 51.83 C ANISOU 574 CD2 TYR A 88 5499 10245 3950 899 542 879 C ATOM 575 CE1 TYR A 88 170.985 39.730 508.321 1.00 55.32 C ANISOU 575 CE1 TYR A 88 6058 10696 4267 1071 164 737 C ATOM 576 CE2 TYR A 88 172.808 41.124 508.997 1.00 53.13 C ANISOU 576 CE2 TYR A 88 5739 10299 4149 830 496 1221 C ATOM 577 CZ TYR A 88 171.510 40.983 508.551 1.00 57.13 C ANISOU 577 CZ TYR A 88 6297 10822 4587 954 314 1150 C ATOM 578 OH TYR A 88 170.736 42.100 508.333 1.00 60.10 O ANISOU 578 OH TYR A 88 6746 11112 4977 961 263 1495 O ATOM 579 N TRP A 89 175.431 38.314 511.685 1.00 48.02 N ANISOU 579 N TRP A 89 4944 9336 3968 879 656 333 N ATOM 580 CA TRP A 89 175.927 39.261 512.674 1.00 47.79 C ANISOU 580 CA TRP A 89 4877 9072 4210 635 739 590 C ATOM 581 C TRP A 89 175.607 40.677 512.211 1.00 39.09 C ANISOU 581 C TRP A 89 3813 7962 3079 454 770 1007 C ATOM 582 O TRP A 89 176.181 41.134 511.210 1.00 42.16 O ANISOU 582 O TRP A 89 4093 8752 3173 426 877 1240 O ATOM 583 CB TRP A 89 177.424 39.093 512.887 1.00 45.14 C ANISOU 583 CB TRP A 89 4338 9019 3795 621 889 599 C ATOM 584 CG TRP A 89 177.926 39.939 514.003 1.00 41.19 C ANISOU 584 CG TRP A 89 3813 8258 3581 336 927 801 C ATOM 585 CD1 TRP A 89 178.658 41.083 513.900 1.00 39.70 C ANISOU 585 CD1 TRP A 89 3518 8201 3365 49 1029 1166 C ATOM 586 CD2 TRP A 89 177.698 39.732 515.401 1.00 34.68 C ANISOU 586 CD2 TRP A 89 3097 6984 3097 282 845 653 C ATOM 587 NE1 TRP A 89 178.917 41.593 515.149 1.00 43.28 N ANISOU 587 NE1 TRP A 89 4024 8296 4125 -183 995 1216 N ATOM 588 CE2 TRP A 89 178.336 40.782 516.088 1.00 37.94 C ANISOU 588 CE2 TRP A 89 3471 7281 3663 -18 891 902 C ATOM 589 CE3 TRP A 89 177.023 38.754 516.138 1.00 43.52 C ANISOU 589 CE3 TRP A 89 4353 7795 4388 436 732 347 C ATOM 590 CZ2 TRP A 89 178.319 40.883 517.477 1.00 36.71 C ANISOU 590 CZ2 TRP A 89 3406 6738 3802 -124 826 822 C ATOM 591 CZ3 TRP A 89 177.007 38.856 517.517 1.00 40.81 C ANISOU 591 CZ3 TRP A 89 4080 7090 4336 327 692 311 C ATOM 592 CH2 TRP A 89 177.652 39.913 518.172 1.00 34.89 C ANISOU 592 CH2 TRP A 89 3288 6259 3711 73 739 532 C ATOM 593 N PRO A 90 174.704 41.398 512.884 1.00 37.65 N ANISOU 593 N PRO A 90 3794 7345 3165 356 681 1125 N ATOM 594 CA PRO A 90 174.255 42.696 512.367 1.00 45.39 C ANISOU 594 CA PRO A 90 4885 8264 4099 266 678 1508 C ATOM 595 C PRO A 90 174.983 43.892 512.962 1.00 47.40 C ANISOU 595 C PRO A 90 5216 8275 4519 -22 753 1822 C ATOM 596 O PRO A 90 174.825 45.018 512.478 1.00 52.70 O ANISOU 596 O PRO A 90 6025 8868 5132 -125 757 2183 O ATOM 597 CB PRO A 90 172.775 42.709 512.758 1.00 40.53 C ANISOU 597 CB PRO A 90 4406 7337 3655 401 523 1415 C ATOM 598 CG PRO A 90 172.772 41.990 514.081 1.00 34.41 C ANISOU 598 CG PRO A 90 3634 6272 3170 380 495 1122 C ATOM 599 CD PRO A 90 173.880 40.953 514.023 1.00 34.31 C ANISOU 599 CD PRO A 90 3477 6508 3049 391 569 898 C ATOM 600 N LEU A 91 175.785 43.671 514.002 1.00 51.57 N ANISOU 600 N LEU A 91 5684 8668 5242 -164 791 1695 N ATOM 601 CA LEU A 91 176.351 44.788 514.753 1.00 53.09 C ANISOU 601 CA LEU A 91 5991 8549 5630 -475 807 1934 C ATOM 602 C LEU A 91 177.641 45.306 514.123 1.00 64.73 C ANISOU 602 C LEU A 91 7297 10388 6910 -764 935 2236 C ATOM 603 O LEU A 91 177.747 46.494 513.801 1.00 81.97 O ANISOU 603 O LEU A 91 9637 12430 9079 -1013 941 2615 O ATOM 604 CB LEU A 91 176.577 44.376 516.211 1.00 46.31 C ANISOU 604 CB LEU A 91 5141 7403 5051 -514 764 1670 C ATOM 605 CG LEU A 91 175.298 43.971 516.948 1.00 41.49 C ANISOU 605 CG LEU A 91 4686 6446 4634 -283 655 1429 C ATOM 606 CD1 LEU A 91 175.566 43.737 518.425 1.00 37.76 C ANISOU 606 CD1 LEU A 91 4248 5692 4408 -346 624 1232 C ATOM 607 CD2 LEU A 91 174.213 45.022 516.752 1.00 34.56 C ANISOU 607 CD2 LEU A 91 4057 5270 3805 -219 584 1637 C ATOM 608 N GLY A 92 178.631 44.436 513.955 1.00 57.16 N ANISOU 608 N GLY A 92 6022 9906 5790 -732 1038 2091 N ATOM 609 CA GLY A 92 179.872 44.830 513.335 1.00 60.33 C ANISOU 609 CA GLY A 92 6221 10664 6036 -943 1117 2280 C ATOM 610 C GLY A 92 181.023 43.922 513.712 1.00 60.23 C ANISOU 610 C GLY A 92 5907 10984 5994 -871 1154 2026 C ATOM 611 O GLY A 92 180.914 43.078 514.606 1.00 55.41 O ANISOU 611 O GLY A 92 5264 10285 5503 -711 1135 1742 O ATOM 612 N PRO A 93 182.163 44.086 513.033 1.00 43.36 N ANISOU 612 N PRO A 93 5175 6176 5124 -504 -294 662 N ATOM 613 CA PRO A 93 183.326 43.246 513.363 1.00 36.65 C ANISOU 613 CA PRO A 93 4251 5421 4254 -577 -206 579 C ATOM 614 C PRO A 93 183.919 43.554 514.726 1.00 35.64 C ANISOU 614 C PRO A 93 4054 5228 4259 -642 -161 515 C ATOM 615 O PRO A 93 184.372 42.634 515.419 1.00 30.44 O ANISOU 615 O PRO A 93 3303 4641 3623 -656 -140 415 O ATOM 616 CB PRO A 93 184.310 43.554 512.226 1.00 37.66 C ANISOU 616 CB PRO A 93 4447 5602 4259 -638 -115 681 C ATOM 617 CG PRO A 93 183.940 44.931 511.780 1.00 39.19 C ANISOU 617 CG PRO A 93 4754 5673 4465 -642 -133 819 C ATOM 618 CD PRO A 93 182.448 45.033 511.941 1.00 42.64 C ANISOU 618 CD PRO A 93 5206 6050 4946 -528 -267 811 C ATOM 619 N VAL A 94 183.936 44.826 515.132 1.00 31.14 N ANISOU 619 N VAL A 94 3541 4517 3774 -682 -153 568 N ATOM 620 CA VAL A 94 184.486 45.184 516.438 1.00 35.17 C ANISOU 620 CA VAL A 94 4011 4956 4396 -753 -129 495 C ATOM 621 C VAL A 94 183.628 44.600 517.552 1.00 35.85 C ANISOU 621 C VAL A 94 4044 5034 4543 -669 -182 382 C ATOM 622 O VAL A 94 184.136 43.971 518.488 1.00 35.31 O ANISOU 622 O VAL A 94 3899 5014 4501 -701 -168 288 O ATOM 623 CB VAL A 94 184.616 46.712 516.568 1.00 36.03 C ANISOU 623 CB VAL A 94 4224 4887 4577 -815 -116 569 C ATOM 624 CG1 VAL A 94 185.133 47.083 517.950 1.00 37.24 C ANISOU 624 CG1 VAL A 94 4359 4960 4832 -893 -113 473 C ATOM 625 CG2 VAL A 94 185.532 47.258 515.488 1.00 38.04 C ANISOU 625 CG2 VAL A 94 4525 5152 4776 -915 -47 698 C ATOM 626 N VAL A 95 182.310 44.801 517.469 1.00 37.90 N ANISOU 626 N VAL A 95 4335 5237 4827 -558 -239 401 N ATOM 627 CA VAL A 95 181.412 44.257 518.483 1.00 33.84 C ANISOU 627 CA VAL A 95 3760 4720 4376 -474 -269 311 C ATOM 628 C VAL A 95 181.445 42.735 518.469 1.00 33.55 C ANISOU 628 C VAL A 95 3624 4830 4291 -462 -280 243 C ATOM 629 O VAL A 95 181.295 42.092 519.515 1.00 32.99 O ANISOU 629 O VAL A 95 3492 4779 4263 -444 -273 158 O ATOM 630 CB VAL A 95 179.983 44.800 518.277 1.00 33.30 C ANISOU 630 CB VAL A 95 3720 4575 4359 -352 -322 365 C ATOM 631 CG1 VAL A 95 179.063 44.317 519.388 1.00 32.45 C ANISOU 631 CG1 VAL A 95 3536 4464 4329 -268 -325 284 C ATOM 632 CG2 VAL A 95 180.002 46.318 518.223 1.00 34.38 C ANISOU 632 CG2 VAL A 95 3975 4543 4543 -353 -305 439 C ATOM 633 N CYS A 96 181.650 42.133 517.295 1.00 33.81 N ANISOU 633 N CYS A 96 3657 4960 4228 -469 -295 280 N ATOM 634 CA CYS A 96 181.811 40.684 517.225 1.00 34.45 C ANISOU 634 CA CYS A 96 3668 5159 4261 -462 -299 208 C ATOM 635 C CYS A 96 183.037 40.229 518.009 1.00 34.14 C ANISOU 635 C CYS A 96 3576 5164 4233 -527 -230 145 C ATOM 636 O CYS A 96 182.971 39.269 518.785 1.00 26.45 O ANISOU 636 O CYS A 96 2537 4226 3285 -505 -232 68 O ATOM 637 CB CYS A 96 181.911 40.232 515.769 1.00 36.77 C ANISOU 637 CB CYS A 96 4007 5536 4429 -457 -318 251 C ATOM 638 SG CYS A 96 182.530 38.547 515.594 0.94 40.61 S ANISOU 638 SG CYS A 96 4444 6144 4842 -460 -290 156 S ATOM 639 N ASP A 97 184.170 40.908 517.811 1.00 26.84 N ANISOU 639 N ASP A 97 2671 4235 3293 -610 -173 187 N ATOM 640 CA ASP A 97 185.392 40.529 518.514 1.00 37.04 C ANISOU 640 CA ASP A 97 3888 5581 4605 -675 -123 140 C ATOM 641 C ASP A 97 185.259 40.752 520.015 1.00 32.97 C ANISOU 641 C ASP A 97 3351 5001 4173 -682 -148 72 C ATOM 642 O ASP A 97 185.762 39.953 520.813 1.00 34.62 O ANISOU 642 O ASP A 97 3490 5270 4392 -684 -144 9 O ATOM 643 CB ASP A 97 186.583 41.310 517.956 1.00 39.39 C ANISOU 643 CB ASP A 97 4191 5888 4889 -777 -59 215 C ATOM 644 CG ASP A 97 186.838 41.015 516.489 1.00 49.88 C ANISOU 644 CG ASP A 97 5548 7298 6107 -763 -8 283 C ATOM 645 OD1 ASP A 97 186.391 39.952 516.010 1.00 52.29 O ANISOU 645 OD1 ASP A 97 5854 7674 6341 -683 -24 242 O ATOM 646 OD2 ASP A 97 187.489 41.843 515.817 1.00 50.57 O ANISOU 646 OD2 ASP A 97 5667 7373 6172 -835 51 377 O ATOM 647 N LEU A 98 184.582 41.829 520.419 1.00 30.65 N ANISOU 647 N LEU A 98 3132 4583 3932 -676 -172 85 N ATOM 648 CA LEU A 98 184.381 42.081 521.842 1.00 29.60 C ANISOU 648 CA LEU A 98 3009 4382 3854 -670 -187 12 C ATOM 649 C LEU A 98 183.446 41.048 522.460 1.00 31.56 C ANISOU 649 C LEU A 98 3214 4670 4108 -571 -200 -45 C ATOM 650 O LEU A 98 183.633 40.647 523.614 1.00 38.19 O ANISOU 650 O LEU A 98 4031 5523 4955 -568 -198 -112 O ATOM 651 CB LEU A 98 183.839 43.494 522.054 1.00 33.08 C ANISOU 651 CB LEU A 98 3559 4663 4346 -667 -194 35 C ATOM 652 CG LEU A 98 184.756 44.647 521.639 1.00 37.56 C ANISOU 652 CG LEU A 98 4188 5153 4930 -787 -180 92 C ATOM 653 CD1 LEU A 98 184.048 45.983 521.809 1.00 36.65 C ANISOU 653 CD1 LEU A 98 4203 4852 4870 -759 -187 115 C ATOM 654 CD2 LEU A 98 186.053 44.617 522.435 1.00 41.92 C ANISOU 654 CD2 LEU A 98 4693 5739 5494 -910 -184 37 C ATOM 655 N TRP A 99 182.434 40.607 521.709 1.00 27.77 N ANISOU 655 N TRP A 99 2721 4210 3622 -495 -220 -14 N ATOM 656 CA TRP A 99 181.508 39.607 522.232 1.00 28.94 C ANISOU 656 CA TRP A 99 2813 4390 3793 -420 -230 -55 C ATOM 657 C TRP A 99 182.186 38.250 522.385 1.00 29.44 C ANISOU 657 C TRP A 99 2813 4555 3820 -438 -220 -99 C ATOM 658 O TRP A 99 181.996 37.567 523.398 1.00 33.32 O ANISOU 658 O TRP A 99 3272 5058 4331 -411 -208 -145 O ATOM 659 CB TRP A 99 180.281 39.504 521.323 1.00 32.02 C ANISOU 659 CB TRP A 99 3190 4777 4197 -355 -275 -6 C ATOM 660 CG TRP A 99 179.400 38.329 521.626 1.00 30.53 C ANISOU 660 CG TRP A 99 2924 4634 4041 -306 -293 -37 C ATOM 661 CD1 TRP A 99 178.710 38.096 522.780 1.00 36.85 C ANISOU 661 CD1 TRP A 99 3685 5410 4906 -260 -261 -68 C ATOM 662 CD2 TRP A 99 179.108 37.229 520.755 1.00 31.64 C ANISOU 662 CD2 TRP A 99 3026 4843 4151 -307 -342 -40 C ATOM 663 NE1 TRP A 99 178.011 36.917 522.684 1.00 38.08 N ANISOU 663 NE1 TRP A 99 3765 5614 5089 -243 -285 -76 N ATOM 664 CE2 TRP A 99 178.237 36.365 521.451 1.00 33.48 C ANISOU 664 CE2 TRP A 99 3188 5083 4452 -275 -344 -67 C ATOM 665 CE3 TRP A 99 179.499 36.889 519.457 1.00 32.81 C ANISOU 665 CE3 TRP A 99 3208 5045 4214 -333 -381 -24 C ATOM 666 CZ2 TRP A 99 177.753 35.185 520.892 1.00 32.93 C ANISOU 666 CZ2 TRP A 99 3074 5054 4382 -284 -397 -83 C ATOM 667 CZ3 TRP A 99 179.016 35.717 518.903 1.00 39.64 C ANISOU 667 CZ3 TRP A 99 4047 5955 5060 -329 -435 -54 C ATOM 668 CH2 TRP A 99 178.152 34.879 519.620 1.00 37.66 C ANISOU 668 CH2 TRP A 99 3721 5695 4893 -312 -450 -85 C ATOM 669 N LEU A 100 182.981 37.846 521.393 1.00 33.95 N ANISOU 669 N LEU A 100 3374 5195 4333 -473 -215 -80 N ATOM 670 CA LEU A 100 183.695 36.576 521.485 1.00 35.43 C ANISOU 670 CA LEU A 100 3507 5466 4490 -471 -196 -121 C ATOM 671 C LEU A 100 184.732 36.603 522.601 1.00 33.28 C ANISOU 671 C LEU A 100 3199 5213 4232 -508 -174 -150 C ATOM 672 O LEU A 100 184.867 35.634 523.358 1.00 27.85 O ANISOU 672 O LEU A 100 2473 4559 3550 -477 -172 -188 O ATOM 673 CB LEU A 100 184.360 36.253 520.149 1.00 32.36 C ANISOU 673 CB LEU A 100 3126 5143 4026 -485 -175 -95 C ATOM 674 CG LEU A 100 183.434 35.992 518.961 1.00 32.59 C ANISOU 674 CG LEU A 100 3203 5172 4006 -449 -217 -77 C ATOM 675 CD1 LEU A 100 184.227 36.042 517.668 1.00 30.60 C ANISOU 675 CD1 LEU A 100 2993 4981 3654 -468 -178 -42 C ATOM 676 CD2 LEU A 100 182.740 34.649 519.114 1.00 28.93 C ANISOU 676 CD2 LEU A 100 2717 4720 3557 -404 -251 -135 C ATOM 677 N ALA A 101 185.484 37.701 522.709 1.00 31.21 N ANISOU 677 N ALA A 101 2953 4928 3979 -580 -168 -128 N ATOM 678 CA ALA A 101 186.507 37.797 523.745 1.00 33.74 C ANISOU 678 CA ALA A 101 3234 5273 4312 -633 -175 -158 C ATOM 679 C ALA A 101 185.883 37.800 525.134 1.00 32.52 C ANISOU 679 C ALA A 101 3116 5068 4172 -598 -201 -211 C ATOM 680 O ALA A 101 186.368 37.115 526.041 1.00 29.17 O ANISOU 680 O ALA A 101 2655 4694 3734 -587 -215 -243 O ATOM 681 CB ALA A 101 187.359 39.049 523.533 1.00 27.97 C ANISOU 681 CB ALA A 101 2516 4512 3600 -741 -175 -123 C ATOM 682 N LEU A 102 184.804 38.564 525.317 1.00 34.57 N ANISOU 682 N LEU A 102 3451 5230 4453 -568 -201 -214 N ATOM 683 CA LEU A 102 184.113 38.580 526.602 1.00 34.45 C ANISOU 683 CA LEU A 102 3480 5168 4441 -518 -197 -261 C ATOM 684 C LEU A 102 183.577 37.198 526.957 1.00 38.89 C ANISOU 684 C LEU A 102 3992 5788 4997 -445 -180 -269 C ATOM 685 O LEU A 102 183.665 36.766 528.111 1.00 41.75 O ANISOU 685 O LEU A 102 4365 6166 5333 -423 -175 -301 O ATOM 686 CB LEU A 102 182.978 39.606 526.573 1.00 30.97 C ANISOU 686 CB LEU A 102 3117 4615 4037 -474 -179 -253 C ATOM 687 CG LEU A 102 182.139 39.719 527.848 1.00 37.97 C ANISOU 687 CG LEU A 102 4057 5449 4923 -402 -145 -299 C ATOM 688 CD1 LEU A 102 183.001 40.169 529.015 1.00 42.83 C ANISOU 688 CD1 LEU A 102 4745 6044 5484 -456 -167 -365 C ATOM 689 CD2 LEU A 102 180.976 40.672 527.638 1.00 38.84 C ANISOU 689 CD2 LEU A 102 4219 5452 5085 -332 -114 -278 C ATOM 690 N ASP A 103 183.016 36.493 525.973 1.00 34.50 N ANISOU 690 N ASP A 103 3393 5258 4460 -412 -174 -238 N ATOM 691 CA ASP A 103 182.462 35.166 526.222 1.00 29.46 C ANISOU 691 CA ASP A 103 2711 4651 3832 -359 -161 -243 C ATOM 692 C ASP A 103 183.540 34.194 526.689 1.00 30.00 C ANISOU 692 C ASP A 103 2747 4786 3865 -365 -163 -259 C ATOM 693 O ASP A 103 183.349 33.460 527.665 1.00 31.90 O ANISOU 693 O ASP A 103 2988 5033 4101 -329 -148 -268 O ATOM 694 CB ASP A 103 181.776 34.648 524.957 1.00 30.67 C ANISOU 694 CB ASP A 103 2837 4812 4007 -345 -179 -218 C ATOM 695 CG ASP A 103 180.315 34.331 525.179 1.00 36.73 C ANISOU 695 CG ASP A 103 3578 5542 4836 -298 -174 -205 C ATOM 696 OD1 ASP A 103 179.848 34.470 526.327 1.00 41.65 O ANISOU 696 OD1 ASP A 103 4206 6138 5481 -267 -133 -211 O ATOM 697 OD2 ASP A 103 179.635 33.936 524.209 1.00 38.70 O ANISOU 697 OD2 ASP A 103 3801 5795 5108 -296 -213 -188 O ATOM 698 N TYR A 104 184.684 34.176 526.002 1.00 29.86 N ANISOU 698 N TYR A 104 2698 4823 3825 -404 -174 -253 N ATOM 699 CA TYR A 104 185.727 33.208 526.323 1.00 29.66 C ANISOU 699 CA TYR A 104 2622 4868 3781 -389 -175 -258 C ATOM 700 C TYR A 104 186.479 33.577 527.596 1.00 29.41 C ANISOU 700 C TYR A 104 2587 4859 3727 -413 -206 -271 C ATOM 701 O TYR A 104 186.875 32.690 528.359 1.00 34.35 O ANISOU 701 O TYR A 104 3192 5525 4336 -372 -216 -270 O ATOM 702 CB TYR A 104 186.690 33.069 525.143 1.00 30.65 C ANISOU 702 CB TYR A 104 2700 5054 3894 -408 -158 -242 C ATOM 703 CG TYR A 104 186.191 32.112 524.086 1.00 32.91 C ANISOU 703 CG TYR A 104 2998 5335 4170 -360 -135 -247 C ATOM 704 CD1 TYR A 104 185.129 32.452 523.258 1.00 33.00 C ANISOU 704 CD1 TYR A 104 3058 5300 4181 -367 -148 -242 C ATOM 705 CD2 TYR A 104 186.772 30.861 523.925 1.00 32.79 C ANISOU 705 CD2 TYR A 104 2954 5357 4147 -304 -111 -259 C ATOM 706 CE1 TYR A 104 184.663 31.576 522.295 1.00 37.05 C ANISOU 706 CE1 TYR A 104 3595 5807 4673 -336 -150 -259 C ATOM 707 CE2 TYR A 104 186.316 29.979 522.967 1.00 32.83 C ANISOU 707 CE2 TYR A 104 2998 5341 4136 -266 -97 -282 C ATOM 708 CZ TYR A 104 185.261 30.340 522.153 1.00 37.87 C ANISOU 708 CZ TYR A 104 3689 5936 4762 -290 -124 -286 C ATOM 709 OH TYR A 104 184.802 29.463 521.197 1.00 34.58 O ANISOU 709 OH TYR A 104 3323 5498 4319 -265 -133 -319 O ATOM 710 N VAL A 105 186.690 34.872 527.842 1.00 27.30 N ANISOU 710 N VAL A 105 2355 4561 3456 -481 -231 -283 N ATOM 711 CA VAL A 105 187.354 35.291 529.075 1.00 31.13 C ANISOU 711 CA VAL A 105 2860 5061 3909 -518 -283 -311 C ATOM 712 C VAL A 105 186.485 34.963 530.282 1.00 34.14 C ANISOU 712 C VAL A 105 3317 5407 4249 -453 -272 -335 C ATOM 713 O VAL A 105 186.964 34.431 531.290 1.00 35.60 O ANISOU 713 O VAL A 105 3504 5638 4383 -432 -306 -341 O ATOM 714 CB VAL A 105 187.704 36.789 529.017 1.00 32.51 C ANISOU 714 CB VAL A 105 3076 5182 4093 -618 -315 -328 C ATOM 715 CG1 VAL A 105 188.054 37.304 530.404 1.00 35.54 C ANISOU 715 CG1 VAL A 105 3526 5551 4427 -655 -381 -381 C ATOM 716 CG2 VAL A 105 188.860 37.025 528.057 1.00 33.75 C ANISOU 716 CG2 VAL A 105 3138 5399 4287 -697 -322 -289 C ATOM 717 N VAL A 106 185.188 35.272 530.193 1.00 34.39 N ANISOU 717 N VAL A 106 3407 5361 4299 -414 -220 -339 N ATOM 718 CA VAL A 106 184.273 34.990 531.297 1.00 36.25 C ANISOU 718 CA VAL A 106 3706 5566 4501 -347 -179 -350 C ATOM 719 C VAL A 106 184.160 33.489 531.528 1.00 36.77 C ANISOU 719 C VAL A 106 3726 5679 4565 -290 -156 -313 C ATOM 720 O VAL A 106 184.155 33.020 532.674 1.00 38.19 O ANISOU 720 O VAL A 106 3950 5876 4685 -252 -147 -310 O ATOM 721 CB VAL A 106 182.899 35.631 531.025 1.00 39.51 C ANISOU 721 CB VAL A 106 4156 5895 4961 -309 -117 -348 C ATOM 722 CG1 VAL A 106 181.833 35.018 531.915 1.00 36.97 C ANISOU 722 CG1 VAL A 106 3855 5561 4630 -231 -43 -334 C ATOM 723 CG2 VAL A 106 182.967 37.139 531.236 1.00 37.91 C ANISOU 723 CG2 VAL A 106 4043 5617 4745 -344 -130 -391 C ATOM 724 N SER A 107 184.081 32.710 530.447 1.00 35.32 N ANISOU 724 N SER A 107 3473 5509 4440 -282 -146 -285 N ATOM 725 CA SER A 107 183.961 31.262 530.587 1.00 36.94 C ANISOU 725 CA SER A 107 3650 5730 4657 -233 -125 -253 C ATOM 726 C SER A 107 185.225 30.654 531.180 1.00 40.12 C ANISOU 726 C SER A 107 4033 6199 5011 -217 -167 -243 C ATOM 727 O SER A 107 185.150 29.722 531.990 1.00 43.45 O ANISOU 727 O SER A 107 4477 6624 5409 -165 -153 -212 O ATOM 728 CB SER A 107 183.649 30.632 529.232 1.00 43.09 C ANISOU 728 CB SER A 107 4380 6495 5498 -234 -117 -245 C ATOM 729 OG SER A 107 182.457 31.167 528.683 1.00 46.78 O ANISOU 729 OG SER A 107 4851 6912 6012 -245 -100 -244 O ATOM 730 N ASN A 108 186.394 31.158 530.783 1.00 36.86 N ANISOU 730 N ASN A 108 3574 5842 4591 -260 -219 -256 N ATOM 731 CA ASN A 108 187.641 30.648 531.343 1.00 35.94 C ANISOU 731 CA ASN A 108 3409 5803 4442 -242 -273 -238 C ATOM 732 C ASN A 108 187.773 31.017 532.815 1.00 34.96 C ANISOU 732 C ASN A 108 3353 5696 4235 -244 -324 -247 C ATOM 733 O ASN A 108 188.298 30.232 533.612 1.00 31.79 O ANISOU 733 O ASN A 108 2947 5341 3789 -192 -360 -213 O ATOM 734 CB ASN A 108 188.831 31.179 530.545 1.00 34.73 C ANISOU 734 CB ASN A 108 3163 5715 4318 -298 -309 -241 C ATOM 735 CG ASN A 108 190.077 30.343 530.738 1.00 41.65 C ANISOU 735 CG ASN A 108 3944 6682 5199 -251 -346 -205 C ATOM 736 OD1 ASN A 108 190.361 29.446 529.943 1.00 38.08 O ANISOU 736 OD1 ASN A 108 3437 6245 4786 -191 -299 -184 O ATOM 737 ND2 ASN A 108 190.824 30.625 531.800 1.00 42.60 N ANISOU 737 ND2 ASN A 108 4048 6863 5277 -272 -434 -200 N ATOM 738 N ALA A 109 187.307 32.211 533.193 1.00 30.65 N ANISOU 738 N ALA A 109 2884 5106 3656 -296 -329 -293 N ATOM 739 CA ALA A 109 187.315 32.596 534.600 1.00 34.28 C ANISOU 739 CA ALA A 109 3444 5569 4010 -294 -369 -319 C ATOM 740 C ALA A 109 186.382 31.711 535.416 1.00 39.40 C ANISOU 740 C ALA A 109 4165 6195 4612 -204 -296 -282 C ATOM 741 O ALA A 109 186.659 31.412 536.583 1.00 37.75 O ANISOU 741 O ALA A 109 4023 6023 4299 -171 -332 -269 O ATOM 742 CB ALA A 109 186.927 34.069 534.745 1.00 31.28 C ANISOU 742 CB ALA A 109 3154 5121 3609 -356 -372 -387 C ATOM 743 N ARG A 110 185.268 31.285 534.816 1.00 37.55 N ANISOU 743 N ARG A 110 3915 5900 4450 -172 -198 -257 N ATOM 744 CA ARG A 110 184.361 30.361 535.490 1.00 38.48 C ANISOU 744 CA ARG A 110 4077 5992 4551 -103 -115 -205 C ATOM 745 C ARG A 110 185.041 29.027 535.768 1.00 36.88 C ANISOU 745 C ARG A 110 3847 5829 4335 -55 -144 -142 C ATOM 746 O ARG A 110 184.959 28.493 536.880 1.00 37.36 O ANISOU 746 O ARG A 110 3981 5903 4312 -5 -128 -96 O ATOM 747 CB ARG A 110 183.108 30.145 534.642 1.00 39.57 C ANISOU 747 CB ARG A 110 4171 6063 4799 -100 -27 -188 C ATOM 748 CG ARG A 110 182.348 28.879 534.998 1.00 46.28 C ANISOU 748 CG ARG A 110 5020 6884 5679 -54 50 -116 C ATOM 749 CD ARG A 110 181.384 28.493 533.896 1.00 52.37 C ANISOU 749 CD ARG A 110 5716 7601 6582 -76 90 -103 C ATOM 750 NE ARG A 110 180.595 29.637 533.456 1.00 55.46 N ANISOU 750 NE ARG A 110 6091 7969 7013 -97 112 -139 N ATOM 751 CZ ARG A 110 179.526 30.094 534.098 1.00 56.63 C ANISOU 751 CZ ARG A 110 6260 8092 7164 -69 200 -124 C ATOM 752 NH1 ARG A 110 179.116 29.503 535.212 1.00 49.82 N ANISOU 752 NH1 ARG A 110 5442 7230 6257 -28 282 -73 N ATOM 753 NH2 ARG A 110 178.866 31.144 533.629 1.00 63.80 N ANISOU 753 NH2 ARG A 110 7149 8975 8119 -70 215 -152 N ATOM 754 N VAL A 111 185.710 28.470 534.757 1.00 37.69 N ANISOU 754 N VAL A 111 3855 5948 4516 -59 -177 -133 N ATOM 755 CA VAL A 111 186.352 27.166 534.904 1.00 36.21 C ANISOU 755 CA VAL A 111 3642 5781 4336 7 -195 -72 C ATOM 756 C VAL A 111 187.408 27.212 536.000 1.00 35.70 C ANISOU 756 C VAL A 111 3597 5799 4166 34 -288 -50 C ATOM 757 O VAL A 111 187.451 26.348 536.884 1.00 33.19 O ANISOU 757 O VAL A 111 3332 5484 3792 103 -287 18 O ATOM 758 CB VAL A 111 186.951 26.712 533.561 1.00 34.50 C ANISOU 758 CB VAL A 111 3328 5568 4213 9 -205 -83 C ATOM 759 CG1 VAL A 111 187.821 25.487 533.757 1.00 31.39 C ANISOU 759 CG1 VAL A 111 2906 5195 3825 95 -228 -26 C ATOM 760 CG2 VAL A 111 185.842 26.429 532.560 1.00 35.40 C ANISOU 760 CG2 VAL A 111 3443 5596 4411 -13 -132 -99 C ATOM 761 N MET A 112 188.275 28.225 535.964 1.00 34.85 N ANISOU 761 N MET A 112 3450 5760 4032 -26 -378 -100 N ATOM 762 CA MET A 112 189.287 28.354 537.002 1.00 41.08 C ANISOU 762 CA MET A 112 4249 6638 4721 -17 -496 -86 C ATOM 763 C MET A 112 188.686 28.735 538.348 1.00 42.25 C ANISOU 763 C MET A 112 4554 6775 4725 -10 -497 -97 C ATOM 764 O MET A 112 189.306 28.476 539.383 1.00 42.05 O ANISOU 764 O MET A 112 4574 6816 4588 26 -587 -63 O ATOM 765 CB MET A 112 190.348 29.369 536.576 1.00 38.14 C ANISOU 765 CB MET A 112 3782 6334 4376 -109 -598 -138 C ATOM 766 CG MET A 112 191.189 28.887 535.405 1.00 37.92 C ANISOU 766 CG MET A 112 3592 6349 4468 -95 -593 -110 C ATOM 767 SD MET A 112 192.763 29.743 535.257 0.54 47.18 S ANISOU 767 SD MET A 112 4613 7643 5670 -187 -727 -125 S ATOM 768 CE MET A 112 192.198 31.420 535.023 1.00 28.43 C ANISOU 768 CE MET A 112 2319 5197 3285 -335 -721 -217 C ATOM 769 N ASN A 113 187.492 29.330 538.358 1.00 43.13 N ANISOU 769 N ASN A 113 4751 6808 4829 -32 -396 -138 N ATOM 770 CA ASN A 113 186.790 29.547 539.619 1.00 38.56 C ANISOU 770 CA ASN A 113 4330 6214 4109 1 -352 -140 C ATOM 771 C ASN A 113 186.345 28.223 540.226 1.00 36.83 C ANISOU 771 C ASN A 113 4154 5984 3856 93 -279 -33 C ATOM 772 O ASN A 113 186.469 28.015 541.439 1.00 34.87 O ANISOU 772 O ASN A 113 4021 5774 3454 139 -303 3 O ATOM 773 CB ASN A 113 185.591 30.469 539.398 1.00 41.15 C ANISOU 773 CB ASN A 113 4714 6459 4461 -25 -240 -200 C ATOM 774 CG ASN A 113 185.049 31.047 540.690 1.00 50.34 C ANISOU 774 CG ASN A 113 6052 7613 5461 6 -197 -233 C ATOM 775 OD1 ASN A 113 185.233 30.484 541.770 1.00 58.94 O ANISOU 775 OD1 ASN A 113 7234 8748 6413 60 -212 -187 O ATOM 776 ND2 ASN A 113 184.369 32.182 540.584 1.00 49.82 N ANISOU 776 ND2 ASN A 113 6045 7485 5401 -17 -139 -312 N ATOM 777 N LEU A 114 185.825 27.314 539.398 1.00 37.45 N ANISOU 777 N LEU A 114 4155 6003 4071 114 -193 20 N ATOM 778 CA LEU A 114 185.464 25.990 539.891 1.00 39.43 C ANISOU 778 CA LEU A 114 4445 6222 4315 187 -126 130 C ATOM 779 C LEU A 114 186.693 25.217 540.351 1.00 36.86 C ANISOU 779 C LEU A 114 4110 5961 3934 250 -241 194 C ATOM 780 O LEU A 114 186.616 24.442 541.312 1.00 38.69 O ANISOU 780 O LEU A 114 4433 6192 4074 319 -222 289 O ATOM 781 CB LEU A 114 184.717 25.216 538.806 1.00 34.86 C ANISOU 781 CB LEU A 114 3786 5552 3907 177 -34 156 C ATOM 782 CG LEU A 114 183.467 25.888 538.236 1.00 37.69 C ANISOU 782 CG LEU A 114 4122 5853 4344 121 63 107 C ATOM 783 CD1 LEU A 114 182.918 25.085 537.067 1.00 40.22 C ANISOU 783 CD1 LEU A 114 4357 6096 4829 97 106 124 C ATOM 784 CD2 LEU A 114 182.414 26.068 539.316 1.00 37.56 C ANISOU 784 CD2 LEU A 114 4203 5820 4248 144 180 146 C ATOM 785 N LEU A 115 187.829 25.409 539.677 1.00 32.98 N ANISOU 785 N LEU A 115 3503 5528 3499 233 -354 158 N ATOM 786 CA LEU A 115 189.071 24.791 540.127 1.00 40.20 C ANISOU 786 CA LEU A 115 4380 6522 4370 301 -476 221 C ATOM 787 C LEU A 115 189.514 25.361 541.468 1.00 44.77 C ANISOU 787 C LEU A 115 5060 7192 4760 302 -588 220 C ATOM 788 O LEU A 115 190.072 24.639 542.302 1.00 47.91 O ANISOU 788 O LEU A 115 5497 7639 5069 384 -661 311 O ATOM 789 CB LEU A 115 190.163 24.982 539.073 1.00 42.60 C ANISOU 789 CB LEU A 115 4515 6883 4789 279 -555 182 C ATOM 790 CG LEU A 115 189.963 24.282 537.726 1.00 45.16 C ANISOU 790 CG LEU A 115 4753 7130 5274 299 -462 182 C ATOM 791 CD1 LEU A 115 190.952 24.809 536.697 1.00 44.59 C ANISOU 791 CD1 LEU A 115 4527 7127 5287 260 -515 129 C ATOM 792 CD2 LEU A 115 190.106 22.779 537.882 1.00 42.93 C ANISOU 792 CD2 LEU A 115 4488 6796 5027 420 -433 283 C ATOM 793 N ILE A 116 189.285 26.656 541.689 1.00 41.43 N ANISOU 793 N ILE A 116 4692 6784 4266 214 -610 117 N ATOM 794 CA ILE A 116 189.617 27.258 542.977 1.00 42.41 C ANISOU 794 CA ILE A 116 4946 6980 4188 205 -718 93 C ATOM 795 C ILE A 116 188.760 26.656 544.082 1.00 43.97 C ANISOU 795 C ILE A 116 5323 7148 4237 288 -619 171 C ATOM 796 O ILE A 116 189.264 26.303 545.154 1.00 42.94 O ANISOU 796 O ILE A 116 5286 7088 3943 345 -714 231 O ATOM 797 CB ILE A 116 189.468 28.789 542.907 1.00 40.22 C ANISOU 797 CB ILE A 116 4714 6692 3877 93 -746 -47 C ATOM 798 CG1 ILE A 116 190.603 29.403 542.084 1.00 39.64 C ANISOU 798 CG1 ILE A 116 4474 6673 3916 1 -881 -102 C ATOM 799 CG2 ILE A 116 189.442 29.393 544.304 1.00 41.39 C ANISOU 799 CG2 ILE A 116 5060 6876 3790 92 -815 -91 C ATOM 800 CD1 ILE A 116 190.469 30.898 541.871 1.00 39.74 C ANISOU 800 CD1 ILE A 116 4529 6646 3927 -121 -903 -231 C ATOM 801 N ILE A 117 187.456 26.511 543.834 1.00 37.29 N ANISOU 801 N ILE A 117 4520 6203 3447 294 -426 181 N ATOM 802 CA ILE A 117 186.562 25.927 544.830 1.00 34.69 C ANISOU 802 CA ILE A 117 4344 5842 2995 365 -297 270 C ATOM 803 C ILE A 117 186.951 24.483 545.113 1.00 36.38 C ANISOU 803 C ILE A 117 4552 6057 3215 455 -313 422 C ATOM 804 O ILE A 117 186.935 24.034 546.266 1.00 37.11 O ANISOU 804 O ILE A 117 4789 6181 3132 524 -311 512 O ATOM 805 CB ILE A 117 185.100 26.034 544.360 1.00 34.43 C ANISOU 805 CB ILE A 117 4305 5707 3068 344 -87 260 C ATOM 806 CG1 ILE A 117 184.725 27.493 544.097 1.00 35.70 C ANISOU 806 CG1 ILE A 117 4480 5858 3226 277 -73 118 C ATOM 807 CG2 ILE A 117 184.161 25.414 545.385 1.00 34.93 C ANISOU 807 CG2 ILE A 117 4507 5745 3020 410 70 368 C ATOM 808 CD1 ILE A 117 183.324 27.674 543.552 1.00 36.77 C ANISOU 808 CD1 ILE A 117 4578 5907 3487 265 115 112 C ATOM 809 N SER A 118 187.311 23.733 544.068 1.00 34.48 N ANISOU 809 N SER A 118 4161 5775 3166 463 -324 454 N ATOM 810 CA SER A 118 187.651 22.325 544.247 1.00 36.15 C ANISOU 810 CA SER A 118 4374 5956 3407 559 -327 597 C ATOM 811 C SER A 118 188.965 22.160 545.000 1.00 36.92 C ANISOU 811 C SER A 118 4482 6169 3376 629 -519 648 C ATOM 812 O SER A 118 189.065 21.322 545.903 1.00 38.48 O ANISOU 812 O SER A 118 4787 6371 3465 723 -528 780 O ATOM 813 CB SER A 118 187.716 21.628 542.889 1.00 37.80 C ANISOU 813 CB SER A 118 4436 6080 3848 556 -289 595 C ATOM 814 OG SER A 118 186.484 21.750 542.197 1.00 37.82 O ANISOU 814 OG SER A 118 4423 5981 3965 485 -137 552 O ATOM 815 N PHE A 119 189.985 22.945 544.642 1.00 36.76 N ANISOU 815 N PHE A 119 4347 6246 3373 583 -678 556 N ATOM 816 CA PHE A 119 191.263 22.851 545.341 1.00 47.24 C ANISOU 816 CA PHE A 119 5654 7702 4594 638 -885 604 C ATOM 817 C PHE A 119 191.158 23.380 546.767 1.00 46.67 C ANISOU 817 C PHE A 119 5777 7703 4253 637 -958 603 C ATOM 818 O PHE A 119 191.730 22.795 547.694 1.00 47.06 O ANISOU 818 O PHE A 119 5897 7822 4163 728 -1070 712 O ATOM 819 CB PHE A 119 192.348 23.600 544.567 1.00 45.73 C ANISOU 819 CB PHE A 119 5268 7600 4509 568 -1029 510 C ATOM 820 CG PHE A 119 193.027 22.771 543.513 1.00 43.67 C ANISOU 820 CG PHE A 119 4816 7323 4451 633 -1023 560 C ATOM 821 CD1 PHE A 119 193.981 21.828 543.863 1.00 43.86 C ANISOU 821 CD1 PHE A 119 4779 7406 4478 762 -1129 682 C ATOM 822 CD2 PHE A 119 192.720 22.940 542.173 1.00 42.28 C ANISOU 822 CD2 PHE A 119 4532 7077 4457 577 -911 485 C ATOM 823 CE1 PHE A 119 194.612 21.064 542.895 1.00 47.97 C ANISOU 823 CE1 PHE A 119 5133 7907 5186 843 -1106 722 C ATOM 824 CE2 PHE A 119 193.348 22.182 541.201 1.00 42.91 C ANISOU 824 CE2 PHE A 119 4459 7141 4702 647 -891 520 C ATOM 825 CZ PHE A 119 194.295 21.243 541.562 1.00 43.75 C ANISOU 825 CZ PHE A 119 4506 7299 4818 785 -981 635 C ATOM 826 N ASP A 120 190.435 24.488 546.962 1.00 44.30 N ANISOU 826 N ASP A 120 5578 7386 3868 545 -896 482 N ATOM 827 CA ASP A 120 190.260 25.031 548.307 1.00 47.57 C ANISOU 827 CA ASP A 120 6210 7858 4006 550 -944 461 C ATOM 828 C ASP A 120 189.591 24.019 549.225 1.00 49.27 C ANISOU 828 C ASP A 120 6596 8041 4085 662 -822 615 C ATOM 829 O ASP A 120 189.992 23.859 550.385 1.00 44.93 O ANISOU 829 O ASP A 120 6196 7573 3301 723 -931 678 O ATOM 830 CB ASP A 120 189.442 26.321 548.249 1.00 49.65 C ANISOU 830 CB ASP A 120 6561 8075 4230 453 -850 305 C ATOM 831 CG ASP A 120 189.132 26.878 549.622 1.00 57.77 C ANISOU 831 CG ASP A 120 7846 9144 4959 471 -863 268 C ATOM 832 OD1 ASP A 120 190.029 27.500 550.228 1.00 58.61 O ANISOU 832 OD1 ASP A 120 8011 9345 4912 432 -1080 198 O ATOM 833 OD2 ASP A 120 187.992 26.694 550.095 1.00 59.66 O ANISOU 833 OD2 ASP A 120 8230 9323 5114 523 -655 308 O ATOM 834 N ARG A 121 188.565 23.329 548.725 1.00 42.34 N ANISOU 834 N ARG A 121 5700 7040 3345 683 -600 683 N ATOM 835 CA ARG A 121 187.923 22.283 549.509 1.00 44.92 C ANISOU 835 CA ARG A 121 6170 7319 3577 776 -466 850 C ATOM 836 C ARG A 121 188.856 21.099 549.724 1.00 49.94 C ANISOU 836 C ARG A 121 6776 7978 4220 883 -590 1007 C ATOM 837 O ARG A 121 188.798 20.446 550.773 1.00 49.34 O ANISOU 837 O ARG A 121 6864 7919 3964 973 -580 1149 O ATOM 838 CB ARG A 121 186.633 21.835 548.820 1.00 42.79 C ANISOU 838 CB ARG A 121 5857 6908 3494 748 -215 882 C ATOM 839 CG ARG A 121 185.848 20.780 549.578 1.00 45.21 C ANISOU 839 CG ARG A 121 6301 7146 3732 818 -47 1063 C ATOM 840 CD ARG A 121 185.350 21.306 550.910 1.00 53.11 C ANISOU 840 CD ARG A 121 7526 8212 4441 848 26 1076 C ATOM 841 NE ARG A 121 184.520 20.324 551.601 1.00 59.37 N ANISOU 841 NE ARG A 121 8444 8939 5175 905 221 1263 N ATOM 842 CZ ARG A 121 183.958 20.523 552.788 1.00 60.84 C ANISOU 842 CZ ARG A 121 8840 9170 5105 949 338 1319 C ATOM 843 NH1 ARG A 121 183.218 19.572 553.340 1.00 60.59 N ANISOU 843 NH1 ARG A 121 8905 9073 5043 993 530 1509 N ATOM 844 NH2 ARG A 121 184.136 21.672 553.426 1.00 62.33 N ANISOU 844 NH2 ARG A 121 9154 9463 5064 947 270 1185 N ATOM 845 N TYR A 122 189.715 20.804 548.745 1.00 47.22 N ANISOU 845 N TYR A 122 6229 7634 4078 887 -697 990 N ATOM 846 CA TYR A 122 190.647 19.691 548.886 1.00 50.90 C ANISOU 846 CA TYR A 122 6650 8118 4574 1011 -812 1137 C ATOM 847 C TYR A 122 191.642 19.948 550.011 1.00 46.75 C ANISOU 847 C TYR A 122 6199 7753 3811 1066 -1044 1176 C ATOM 848 O TYR A 122 191.894 19.072 550.845 1.00 48.74 O ANISOU 848 O TYR A 122 6560 8019 3940 1187 -1090 1343 O ATOM 849 CB TYR A 122 191.370 19.442 547.563 1.00 47.79 C ANISOU 849 CB TYR A 122 6017 7701 4442 1011 -862 1093 C ATOM 850 CG TYR A 122 192.429 18.366 547.647 1.00 51.51 C ANISOU 850 CG TYR A 122 6418 8194 4961 1158 -983 1234 C ATOM 851 CD1 TYR A 122 192.080 17.023 547.699 1.00 54.01 C ANISOU 851 CD1 TYR A 122 6807 8373 5343 1267 -870 1391 C ATOM 852 CD2 TYR A 122 193.778 18.694 547.672 1.00 52.94 C ANISOU 852 CD2 TYR A 122 6453 8526 5136 1189 -1209 1217 C ATOM 853 CE1 TYR A 122 193.046 16.036 547.775 1.00 56.81 C ANISOU 853 CE1 TYR A 122 7105 8730 5748 1423 -975 1525 C ATOM 854 CE2 TYR A 122 194.751 17.716 547.748 1.00 52.37 C ANISOU 854 CE2 TYR A 122 6297 8480 5121 1344 -1317 1355 C ATOM 855 CZ TYR A 122 194.380 16.388 547.800 1.00 57.00 C ANISOU 855 CZ TYR A 122 6974 8920 5766 1471 -1197 1508 C ATOM 856 OH TYR A 122 195.347 15.410 547.875 1.00 61.80 O ANISOU 856 OH TYR A 122 7507 9538 6436 1646 -1299 1650 O ATOM 857 N PHE A 123 192.216 21.152 550.052 1.00 46.73 N ANISOU 857 N PHE A 123 6147 7869 3741 973 -1204 1027 N ATOM 858 CA PHE A 123 193.172 21.484 551.102 1.00 50.97 C ANISOU 858 CA PHE A 123 6751 8566 4050 1000 -1457 1044 C ATOM 859 C PHE A 123 192.503 21.647 552.461 1.00 58.10 C ANISOU 859 C PHE A 123 7952 9490 4633 1026 -1415 1079 C ATOM 860 O PHE A 123 193.180 21.525 553.488 1.00 66.24 O ANISOU 860 O PHE A 123 9090 10638 5440 1090 -1609 1151 O ATOM 861 CB PHE A 123 193.935 22.756 550.725 1.00 49.57 C ANISOU 861 CB PHE A 123 6438 8489 3907 866 -1638 866 C ATOM 862 CG PHE A 123 194.796 22.602 549.502 1.00 51.24 C ANISOU 862 CG PHE A 123 6353 8716 4402 853 -1699 851 C ATOM 863 CD1 PHE A 123 195.641 21.513 549.370 1.00 48.64 C ANISOU 863 CD1 PHE A 123 5889 8421 4172 990 -1783 1000 C ATOM 864 CD2 PHE A 123 194.746 23.534 548.479 1.00 49.46 C ANISOU 864 CD2 PHE A 123 5988 8464 4339 717 -1658 695 C ATOM 865 CE1 PHE A 123 196.433 21.362 548.247 1.00 54.34 C ANISOU 865 CE1 PHE A 123 6340 9160 5147 995 -1814 987 C ATOM 866 CE2 PHE A 123 195.534 23.389 547.350 1.00 49.92 C ANISOU 866 CE2 PHE A 123 5783 8544 4641 710 -1692 689 C ATOM 867 CZ PHE A 123 196.379 22.301 547.234 1.00 51.48 C ANISOU 867 CZ PHE A 123 5845 8783 4932 851 -1763 831 C ATOM 868 N CYS A 124 191.196 21.923 552.493 1.00 59.67 N ANISOU 868 N CYS A 124 8284 9586 4800 982 -1168 1034 N ATOM 869 CA CYS A 124 190.485 21.974 553.767 1.00 62.24 C ANISOU 869 CA CYS A 124 8897 9928 4824 1026 -1079 1085 C ATOM 870 C CYS A 124 190.366 20.588 554.389 1.00 67.73 C ANISOU 870 C CYS A 124 9698 10590 5448 1167 -1013 1327 C ATOM 871 O CYS A 124 190.468 20.439 555.613 1.00 71.86 O ANISOU 871 O CYS A 124 10441 11190 5673 1241 -1076 1417 O ATOM 872 CB CYS A 124 189.099 22.592 553.579 1.00 65.67 C ANISOU 872 CB CYS A 124 9412 10263 5275 957 -807 988 C ATOM 873 SG CYS A 124 189.065 24.397 553.573 1.00 70.97 S ANISOU 873 SG CYS A 124 10132 10980 5853 826 -876 721 S ATOM 874 N VAL A 125 190.147 19.561 553.563 1.00 73.23 N ANISOU 874 N VAL A 125 10258 11162 6406 1206 -889 1434 N ATOM 875 CA VAL A 125 189.957 18.206 554.075 1.00 76.41 C ANISOU 875 CA VAL A 125 10766 11492 6775 1331 -804 1670 C ATOM 876 C VAL A 125 191.253 17.412 554.166 1.00 79.05 C ANISOU 876 C VAL A 125 11018 11886 7134 1454 -1038 1798 C ATOM 877 O VAL A 125 191.280 16.369 554.838 1.00 82.75 O ANISOU 877 O VAL A 125 11613 12316 7510 1579 -1020 2008 O ATOM 878 CB VAL A 125 188.953 17.420 553.207 1.00 78.35 C ANISOU 878 CB VAL A 125 10938 11543 7288 1306 -540 1729 C ATOM 879 CG1 VAL A 125 187.697 18.247 552.962 1.00 77.71 C ANISOU 879 CG1 VAL A 125 10881 11414 7231 1186 -321 1600 C ATOM 880 CG2 VAL A 125 189.598 16.998 551.897 1.00 81.08 C ANISOU 880 CG2 VAL A 125 11034 11826 7947 1305 -611 1691 C ATOM 881 N THR A 126 192.330 17.865 553.518 1.00 71.84 N ANISOU 881 N THR A 126 9888 11061 6346 1428 -1250 1690 N ATOM 882 CA THR A 126 193.596 17.147 553.549 1.00 71.94 C ANISOU 882 CA THR A 126 9783 11143 6410 1556 -1470 1811 C ATOM 883 C THR A 126 194.677 17.837 554.366 1.00 71.39 C ANISOU 883 C THR A 126 9719 11285 6119 1561 -1783 1777 C ATOM 884 O THR A 126 195.633 17.171 554.774 1.00 69.99 O ANISOU 884 O THR A 126 9500 11188 5906 1695 -1977 1924 O ATOM 885 CB THR A 126 194.125 16.922 552.124 1.00 54.01 C ANISOU 885 CB THR A 126 7223 8816 4484 1549 -1470 1750 C ATOM 886 OG1 THR A 126 194.265 18.182 551.456 1.00 52.24 O ANISOU 886 OG1 THR A 126 6856 8660 4331 1394 -1518 1530 O ATOM 887 CG2 THR A 126 193.174 16.035 551.338 1.00 61.62 C ANISOU 887 CG2 THR A 126 8190 9561 5661 1560 -1199 1802 C ATOM 888 N LYS A 127 194.556 19.139 554.613 1.00 69.46 N ANISOU 888 N LYS A 127 9528 11131 5734 1421 -1848 1590 N ATOM 889 CA LYS A 127 195.505 19.883 555.442 1.00 68.39 C ANISOU 889 CA LYS A 127 9427 11188 5371 1395 -2158 1534 C ATOM 890 C LYS A 127 194.738 20.706 556.471 1.00 64.58 C ANISOU 890 C LYS A 127 9250 10733 4555 1328 -2110 1443 C ATOM 891 O LYS A 127 194.745 21.942 556.426 1.00 60.59 O ANISOU 891 O LYS A 127 8755 10273 3993 1186 -2178 1237 O ATOM 892 CB LYS A 127 196.399 20.776 554.581 1.00 68.44 C ANISOU 892 CB LYS A 127 9156 11276 5571 1271 -2333 1365 C ATOM 893 CG LYS A 127 197.208 20.026 553.534 1.00 66.82 C ANISOU 893 CG LYS A 127 8642 11058 5689 1347 -2365 1444 C ATOM 894 CD LYS A 127 197.962 20.985 552.628 1.00 69.54 C ANISOU 894 CD LYS A 127 8717 11479 6228 1206 -2487 1278 C ATOM 895 CE LYS A 127 198.726 20.238 551.546 1.00 74.98 C ANISOU 895 CE LYS A 127 9103 12155 7231 1295 -2480 1354 C ATOM 896 NZ LYS A 127 199.366 21.166 550.571 1.00 76.08 N ANISOU 896 NZ LYS A 127 8978 12358 7570 1152 -2548 1202 N ATOM 897 N PRO A 128 194.067 20.049 557.423 1.00 66.67 N ANISOU 897 N PRO A 128 9779 10964 4589 1433 -1983 1596 N ATOM 898 CA PRO A 128 193.277 20.804 558.409 1.00 71.57 C ANISOU 898 CA PRO A 128 10703 11600 4892 1379 -1894 1507 C ATOM 899 C PRO A 128 194.126 21.572 559.407 1.00 77.39 C ANISOU 899 C PRO A 128 11542 12438 5424 1281 -2175 1402 C ATOM 900 O PRO A 128 193.632 22.543 559.995 1.00 81.17 O ANISOU 900 O PRO A 128 12219 12925 5696 1187 -2131 1248 O ATOM 901 CB PRO A 128 192.446 19.716 559.110 1.00 75.46 C ANISOU 901 CB PRO A 128 11406 11999 5265 1498 -1663 1727 C ATOM 902 CG PRO A 128 192.605 18.474 558.265 1.00 74.18 C ANISOU 902 CG PRO A 128 11050 11745 5390 1602 -1597 1907 C ATOM 903 CD PRO A 128 193.955 18.598 557.641 1.00 72.33 C ANISOU 903 CD PRO A 128 10541 11605 5335 1597 -1890 1855 C ATOM 904 N LEU A 129 195.379 21.172 559.619 1.00 74.83 N ANISOU 904 N LEU A 129 11088 12187 5159 1297 -2458 1482 N ATOM 905 CA LEU A 129 196.239 21.834 560.590 1.00 75.68 C ANISOU 905 CA LEU A 129 11280 12400 5077 1189 -2747 1408 C ATOM 906 C LEU A 129 196.958 23.051 560.026 1.00 74.18 C ANISOU 906 C LEU A 129 10912 12265 5007 1014 -2951 1189 C ATOM 907 O LEU A 129 197.480 23.858 560.803 1.00 75.35 O ANISOU 907 O LEU A 129 11155 12493 4982 880 -3159 1088 O ATOM 908 CB LEU A 129 197.277 20.846 561.134 1.00 74.65 C ANISOU 908 CB LEU A 129 11087 12322 4956 1282 -2970 1612 C ATOM 909 CG LEU A 129 196.742 19.583 561.813 1.00 81.16 C ANISOU 909 CG LEU A 129 12093 13085 5660 1447 -2810 1853 C ATOM 910 CD1 LEU A 129 197.890 18.692 562.266 1.00 87.55 C ANISOU 910 CD1 LEU A 129 12816 13944 6506 1538 -3063 2041 C ATOM 911 CD2 LEU A 129 195.845 19.946 562.985 1.00 85.01 C ANISOU 911 CD2 LEU A 129 12926 13580 5795 1411 -2669 1829 C ATOM 912 N THR A 130 197.002 23.203 558.704 1.00 71.85 N ANISOU 912 N THR A 130 10357 11937 5004 1000 -2891 1121 N ATOM 913 CA THR A 130 197.751 24.283 558.073 1.00 75.12 C ANISOU 913 CA THR A 130 10574 12389 5578 831 -3076 934 C ATOM 914 C THR A 130 196.881 25.200 557.229 1.00 74.96 C ANISOU 914 C THR A 130 10544 12310 5629 744 -2879 747 C ATOM 915 O THR A 130 196.982 26.426 557.351 1.00 75.46 O ANISOU 915 O THR A 130 10669 12372 5631 577 -2973 552 O ATOM 916 CB THR A 130 198.882 23.701 557.207 1.00 78.75 C ANISOU 916 CB THR A 130 10675 12883 6364 875 -3220 1022 C ATOM 917 OG1 THR A 130 199.824 23.017 558.043 1.00 86.00 O ANISOU 917 OG1 THR A 130 11599 13856 7221 943 -3449 1174 O ATOM 918 CG2 THR A 130 199.595 24.805 556.439 1.00 80.08 C ANISOU 918 CG2 THR A 130 10620 13069 6736 697 -3365 838 C ATOM 919 N TYR A 131 196.019 24.640 556.376 1.00 71.02 N ANISOU 919 N TYR A 131 9971 11756 5257 848 -2612 805 N ATOM 920 CA TYR A 131 195.332 25.467 555.383 1.00 64.82 C ANISOU 920 CA TYR A 131 9108 10872 4649 733 -2425 637 C ATOM 921 C TYR A 131 194.266 26.380 555.980 1.00 60.59 C ANISOU 921 C TYR A 131 8870 10266 3885 676 -2271 490 C ATOM 922 O TYR A 131 194.223 27.563 555.600 1.00 63.44 O ANISOU 922 O TYR A 131 9215 10593 4298 532 -2294 292 O ATOM 923 CB TYR A 131 194.752 24.578 554.279 1.00 65.10 C ANISOU 923 CB TYR A 131 8972 10777 4987 800 -2159 739 C ATOM 924 CG TYR A 131 194.127 25.362 553.151 1.00 62.89 C ANISOU 924 CG TYR A 131 8582 10381 4932 676 -1979 582 C ATOM 925 CD1 TYR A 131 194.914 26.091 552.269 1.00 63.58 C ANISOU 925 CD1 TYR A 131 8435 10503 5221 552 -2113 467 C ATOM 926 CD2 TYR A 131 192.751 25.376 552.966 1.00 58.66 C ANISOU 926 CD2 TYR A 131 8169 9708 4412 683 -1676 561 C ATOM 927 CE1 TYR A 131 194.350 26.812 551.236 1.00 61.39 C ANISOU 927 CE1 TYR A 131 8071 10119 5136 445 -1954 338 C ATOM 928 CE2 TYR A 131 192.178 26.093 551.934 1.00 51.38 C ANISOU 928 CE2 TYR A 131 7144 8686 3691 581 -1529 429 C ATOM 929 CZ TYR A 131 192.982 26.810 551.073 1.00 52.75 C ANISOU 929 CZ TYR A 131 7108 8891 4045 465 -1671 319 C ATOM 930 OH TYR A 131 192.417 27.526 550.044 1.00 57.61 O ANISOU 930 OH TYR A 131 7635 9406 4849 370 -1529 201 O ATOM 931 N PRO A 132 193.374 25.923 556.873 1.00 63.15 N ANISOU 931 N PRO A 132 9466 10559 3967 785 -2096 577 N ATOM 932 CA PRO A 132 192.284 26.811 557.322 1.00 69.40 C ANISOU 932 CA PRO A 132 10518 11276 4576 746 -1901 432 C ATOM 933 C PRO A 132 192.744 28.136 557.910 1.00 75.88 C ANISOU 933 C PRO A 132 11491 12149 5190 622 -2115 217 C ATOM 934 O PRO A 132 192.008 29.126 557.811 1.00 80.32 O ANISOU 934 O PRO A 132 12177 12624 5716 560 -1975 43 O ATOM 935 CB PRO A 132 191.553 25.958 558.367 1.00 71.65 C ANISOU 935 CB PRO A 132 11064 11565 4596 898 -1732 602 C ATOM 936 CG PRO A 132 191.796 24.566 557.931 1.00 70.38 C ANISOU 936 CG PRO A 132 10720 11390 4633 998 -1701 832 C ATOM 937 CD PRO A 132 193.203 24.560 557.410 1.00 67.43 C ANISOU 937 CD PRO A 132 10085 11110 4423 954 -2019 820 C ATOM 938 N VAL A 133 193.931 28.197 558.516 1.00 73.30 N ANISOU 938 N VAL A 133 11130 11914 4809 541 -2417 229 N ATOM 939 CA VAL A 133 194.389 29.474 559.054 1.00 77.33 C ANISOU 939 CA VAL A 133 11738 12446 5200 363 -2591 27 C ATOM 940 C VAL A 133 194.853 30.399 557.931 1.00 78.26 C ANISOU 940 C VAL A 133 11633 12529 5575 212 -2695 -133 C ATOM 941 O VAL A 133 194.784 31.626 558.064 1.00 83.56 O ANISOU 941 O VAL A 133 12396 13160 6193 78 -2720 -338 O ATOM 942 CB VAL A 133 195.489 29.258 560.110 1.00 82.97 C ANISOU 942 CB VAL A 133 12463 13305 5756 316 -2874 99 C ATOM 943 CG1 VAL A 133 196.780 28.780 559.468 1.00 82.53 C ANISOU 943 CG1 VAL A 133 12080 13323 5953 272 -3134 207 C ATOM 944 CG2 VAL A 133 195.720 30.535 560.908 1.00 88.74 C ANISOU 944 CG2 VAL A 133 13337 14088 6292 173 -2987 -118 C ATOM 945 N LYS A 134 195.320 29.839 556.815 1.00 74.01 N ANISOU 945 N LYS A 134 10791 12004 5326 239 -2736 -45 N ATOM 946 CA LYS A 134 195.710 30.629 555.654 1.00 76.65 C ANISOU 946 CA LYS A 134 10886 12307 5929 103 -2797 -174 C ATOM 947 C LYS A 134 194.528 30.984 554.765 1.00 76.89 C ANISOU 947 C LYS A 134 10914 12190 6112 107 -2475 -249 C ATOM 948 O LYS A 134 194.727 31.580 553.701 1.00 78.06 O ANISOU 948 O LYS A 134 10857 12278 6523 -11 -2464 -331 O ATOM 949 CB LYS A 134 196.754 29.870 554.832 1.00 79.87 C ANISOU 949 CB LYS A 134 10928 12790 6630 117 -2925 -36 C ATOM 950 CG LYS A 134 197.704 29.033 555.669 1.00 88.95 C ANISOU 950 CG LYS A 134 12070 14017 7709 184 -3142 125 C ATOM 951 CD LYS A 134 198.567 28.132 554.802 1.00 95.29 C ANISOU 951 CD LYS A 134 12517 14874 8817 258 -3197 272 C ATOM 952 CE LYS A 134 199.570 28.936 553.994 1.00100.63 C ANISOU 952 CE LYS A 134 12924 15543 9766 103 -3353 163 C ATOM 953 NZ LYS A 134 200.475 28.053 553.210 1.00102.18 N ANISOU 953 NZ LYS A 134 12776 15795 10252 183 -3386 308 N ATOM 954 N ARG A 135 193.310 30.634 555.177 1.00 74.65 N ANISOU 954 N ARG A 135 10840 11828 5695 227 -2200 -207 N ATOM 955 CA ARG A 135 192.118 30.771 554.346 1.00 68.55 C ANISOU 955 CA ARG A 135 10034 10904 5109 242 -1872 -232 C ATOM 956 C ARG A 135 191.355 32.012 554.801 1.00 65.27 C ANISOU 956 C ARG A 135 9881 10395 4523 192 -1775 -427 C ATOM 957 O ARG A 135 190.413 31.950 555.591 1.00 68.62 O ANISOU 957 O ARG A 135 10557 10786 4728 293 -1586 -421 O ATOM 958 CB ARG A 135 191.275 29.502 554.441 1.00 66.43 C ANISOU 958 CB ARG A 135 9785 10610 4846 402 -1626 -38 C ATOM 959 CG ARG A 135 190.123 29.407 553.468 1.00 60.69 C ANISOU 959 CG ARG A 135 8958 9744 4357 416 -1314 -28 C ATOM 960 CD ARG A 135 189.537 28.005 553.501 1.00 57.10 C ANISOU 960 CD ARG A 135 8477 9270 3947 548 -1127 182 C ATOM 961 NE ARG A 135 188.364 27.876 552.643 1.00 57.27 N ANISOU 961 NE ARG A 135 8410 9165 4186 553 -840 195 N ATOM 962 CZ ARG A 135 187.114 28.016 553.068 1.00 53.33 C ANISOU 962 CZ ARG A 135 8070 8601 3594 602 -587 195 C ATOM 963 NH1 ARG A 135 186.872 28.288 554.343 1.00 50.40 N ANISOU 963 NH1 ARG A 135 7976 8274 2899 659 -565 179 N ATOM 964 NH2 ARG A 135 186.105 27.882 552.219 1.00 48.88 N ANISOU 964 NH2 ARG A 135 7385 7933 3256 597 -356 214 N ATOM 965 N THR A 136 191.780 33.161 554.284 1.00 58.38 N ANISOU 965 N THR A 136 8949 9473 3759 38 -1896 -598 N ATOM 966 CA THR A 136 191.221 34.457 554.645 1.00 60.59 C ANISOU 966 CA THR A 136 9475 9645 3903 -21 -1840 -803 C ATOM 967 C THR A 136 190.501 35.069 553.447 1.00 65.30 C ANISOU 967 C THR A 136 9937 10089 4783 -67 -1631 -867 C ATOM 968 O THR A 136 190.490 34.514 552.344 1.00 59.58 O ANISOU 968 O THR A 136 8938 9356 4345 -67 -1550 -761 O ATOM 969 CB THR A 136 192.319 35.396 555.152 1.00 62.76 C ANISOU 969 CB THR A 136 9839 9964 4044 -177 -2179 -962 C ATOM 970 OG1 THR A 136 193.202 35.723 554.072 1.00 58.90 O ANISOU 970 OG1 THR A 136 9045 9477 3859 -331 -2333 -978 O ATOM 971 CG2 THR A 136 193.115 34.736 556.271 1.00 60.68 C ANISOU 971 CG2 THR A 136 9633 9868 3556 -145 -2389 -871 C ATOM 972 N THR A 137 189.896 36.237 553.677 1.00 68.52 N ANISOU 972 N THR A 137 10560 10373 5100 -98 -1546 -1044 N ATOM 973 CA THR A 137 189.203 36.935 552.598 1.00 66.70 C ANISOU 973 CA THR A 137 10228 9993 5123 -134 -1363 -1107 C ATOM 974 C THR A 137 190.190 37.555 551.617 1.00 65.42 C ANISOU 974 C THR A 137 9847 9811 5200 -316 -1563 -1164 C ATOM 975 O THR A 137 189.922 37.612 550.411 1.00 63.65 O ANISOU 975 O THR A 137 9411 9519 5253 -342 -1447 -1126 O ATOM 976 CB THR A 137 188.275 38.006 553.170 1.00 67.95 C ANISOU 976 CB THR A 137 10688 10015 5113 -92 -1209 -1274 C ATOM 977 OG1 THR A 137 189.042 38.955 553.920 1.00 76.27 O ANISOU 977 OG1 THR A 137 11961 11055 5963 -205 -1455 -1454 O ATOM 978 CG2 THR A 137 187.228 37.376 554.075 1.00 67.18 C ANISOU 978 CG2 THR A 137 10785 9945 4795 96 -966 -1200 C ATOM 979 N LYS A 138 191.333 38.033 552.116 1.00 63.00 N ANISOU 979 N LYS A 138 9586 9563 4787 -449 -1864 -1252 N ATOM 980 CA LYS A 138 192.346 38.598 551.230 1.00 63.54 C ANISOU 980 CA LYS A 138 9429 9625 5090 -637 -2055 -1290 C ATOM 981 C LYS A 138 192.929 37.534 550.309 1.00 63.55 C ANISOU 981 C LYS A 138 9072 9742 5332 -623 -2073 -1104 C ATOM 982 O LYS A 138 193.184 37.799 549.127 1.00 65.78 O ANISOU 982 O LYS A 138 9127 9983 5884 -711 -2048 -1088 O ATOM 983 CB LYS A 138 193.447 39.267 552.055 1.00 68.98 C ANISOU 983 CB LYS A 138 10234 10365 5609 -792 -2390 -1415 C ATOM 984 CG LYS A 138 194.632 39.758 551.242 1.00 72.45 C ANISOU 984 CG LYS A 138 10404 10825 6297 -998 -2605 -1428 C ATOM 985 CD LYS A 138 195.601 40.541 552.111 1.00 82.41 C ANISOU 985 CD LYS A 138 11709 12103 7499 -1094 -2827 -1553 C ATOM 986 CE LYS A 138 196.908 40.807 551.385 1.00 89.24 C ANISOU 986 CE LYS A 138 12244 13012 8652 -1249 -3010 -1523 C ATOM 987 NZ LYS A 138 197.650 39.545 551.107 1.00 92.56 N ANISOU 987 NZ LYS A 138 12377 13615 9177 -1174 -3093 -1331 N ATOM 988 N MET A 139 193.143 36.322 550.828 1.00 61.29 N ANISOU 988 N MET A 139 8746 9596 4948 -504 -2106 -961 N ATOM 989 CA MET A 139 193.639 35.237 549.986 1.00 60.36 C ANISOU 989 CA MET A 139 8312 9570 5050 -461 -2100 -787 C ATOM 990 C MET A 139 192.623 34.865 548.916 1.00 55.89 C ANISOU 990 C MET A 139 7639 8903 4692 -382 -1804 -721 C ATOM 991 O MET A 139 192.987 34.627 547.758 1.00 56.58 O ANISOU 991 O MET A 139 7468 8997 5032 -420 -1783 -661 O ATOM 992 CB MET A 139 193.981 34.018 550.842 1.00 65.57 C ANISOU 992 CB MET A 139 8991 10373 5548 -330 -2184 -643 C ATOM 993 CG MET A 139 194.641 32.889 550.062 1.00 66.51 C ANISOU 993 CG MET A 139 8799 10584 5887 -275 -2205 -470 C ATOM 994 SD MET A 139 194.087 31.251 550.571 0.42 65.74 S ANISOU 994 SD MET A 139 8755 10529 5693 -49 -2060 -268 S ATOM 995 CE MET A 139 192.400 31.261 549.967 1.00 64.65 C ANISOU 995 CE MET A 139 8704 10217 5644 12 -1682 -283 C ATOM 996 N ALA A 140 191.341 34.805 549.286 1.00 52.58 N ANISOU 996 N ALA A 140 7413 8398 4165 -271 -1574 -731 N ATOM 997 CA ALA A 140 190.301 34.474 548.317 1.00 50.42 C ANISOU 997 CA ALA A 140 7039 8033 4086 -204 -1309 -671 C ATOM 998 C ALA A 140 190.183 35.549 547.244 1.00 47.25 C ANISOU 998 C ALA A 140 6551 7520 3883 -317 -1272 -771 C ATOM 999 O ALA A 140 189.973 35.236 546.066 1.00 42.46 O ANISOU 999 O ALA A 140 5746 6883 3503 -316 -1168 -706 O ATOM 1000 CB ALA A 140 188.964 34.274 549.031 1.00 48.44 C ANISOU 1000 CB ALA A 140 7003 7724 3679 -70 -1077 -658 C ATOM 1001 N GLY A 141 190.317 36.819 547.631 1.00 48.60 N ANISOU 1001 N GLY A 141 6885 7620 3962 -415 -1359 -928 N ATOM 1002 CA GLY A 141 190.252 37.891 546.652 1.00 43.58 C ANISOU 1002 CA GLY A 141 6186 6862 3509 -527 -1333 -1014 C ATOM 1003 C GLY A 141 191.404 37.856 545.667 1.00 50.98 C ANISOU 1003 C GLY A 141 6852 7862 4658 -656 -1481 -967 C ATOM 1004 O GLY A 141 191.217 38.095 544.471 1.00 58.29 O ANISOU 1004 O GLY A 141 7630 8724 5794 -693 -1386 -944 O ATOM 1005 N MET A 142 192.614 37.561 546.154 1.00 54.11 N ANISOU 1005 N MET A 142 7173 8390 4995 -721 -1714 -945 N ATOM 1006 CA MET A 142 193.770 37.485 545.266 1.00 53.49 C ANISOU 1006 CA MET A 142 6811 8391 5121 -836 -1845 -887 C ATOM 1007 C MET A 142 193.658 36.305 544.308 1.00 48.38 C ANISOU 1007 C MET A 142 5936 7801 4645 -726 -1706 -734 C ATOM 1008 O MET A 142 194.020 36.419 543.131 1.00 45.22 O ANISOU 1008 O MET A 142 5333 7396 4454 -790 -1673 -699 O ATOM 1009 CB MET A 142 195.062 37.396 546.083 1.00 57.62 C ANISOU 1009 CB MET A 142 7289 9056 5545 -917 -2134 -889 C ATOM 1010 CG MET A 142 195.394 38.660 546.863 1.00 62.64 C ANISOU 1010 CG MET A 142 8126 9631 6044 -1075 -2318 -1058 C ATOM 1011 SD MET A 142 197.050 38.640 547.582 0.33 66.74 S ANISOU 1011 SD MET A 142 8521 10324 6513 -1210 -2694 -1054 S ATOM 1012 CE MET A 142 196.939 37.225 548.675 1.00 66.94 C ANISOU 1012 CE MET A 142 8625 10510 6299 -1001 -2730 -937 C ATOM 1013 N MET A 143 193.163 35.162 544.792 1.00 40.38 N ANISOU 1013 N MET A 143 4968 6837 3539 -564 -1620 -641 N ATOM 1014 CA MET A 143 192.959 34.014 543.914 1.00 50.70 C ANISOU 1014 CA MET A 143 6094 8168 5000 -459 -1483 -510 C ATOM 1015 C MET A 143 191.920 34.315 542.841 1.00 48.86 C ANISOU 1015 C MET A 143 5847 7808 4911 -452 -1268 -528 C ATOM 1016 O MET A 143 192.101 33.955 541.672 1.00 46.03 O ANISOU 1016 O MET A 143 5300 7454 4736 -456 -1208 -471 O ATOM 1017 CB MET A 143 192.543 32.791 544.732 1.00 51.78 C ANISOU 1017 CB MET A 143 6317 8352 5004 -299 -1428 -408 C ATOM 1018 CG MET A 143 193.703 31.959 545.257 1.00 64.19 C ANISOU 1018 CG MET A 143 7787 10073 6531 -258 -1616 -313 C ATOM 1019 SD MET A 143 193.143 30.547 546.232 0.85 71.20 S ANISOU 1019 SD MET A 143 8809 10988 7255 -66 -1538 -177 S ATOM 1020 CE MET A 143 194.631 29.552 546.268 1.00 78.10 C ANISOU 1020 CE MET A 143 9465 12020 8189 -11 -1743 -44 C ATOM 1021 N ILE A 144 190.821 34.970 543.222 1.00 44.02 N ANISOU 1021 N ILE A 144 5433 7083 4209 -433 -1152 -606 N ATOM 1022 CA ILE A 144 189.789 35.328 542.253 1.00 47.99 C ANISOU 1022 CA ILE A 144 5920 7469 4845 -420 -965 -620 C ATOM 1023 C ILE A 144 190.327 36.344 541.253 1.00 43.88 C ANISOU 1023 C ILE A 144 5298 6902 4473 -559 -1021 -674 C ATOM 1024 O ILE A 144 190.107 36.224 540.042 1.00 44.31 O ANISOU 1024 O ILE A 144 5217 6928 4693 -561 -929 -629 O ATOM 1025 CB ILE A 144 188.535 35.854 542.973 1.00 49.37 C ANISOU 1025 CB ILE A 144 6322 7544 4895 -354 -829 -686 C ATOM 1026 CG1 ILE A 144 187.815 34.711 543.689 1.00 56.71 C ANISOU 1026 CG1 ILE A 144 7313 8512 5722 -212 -712 -596 C ATOM 1027 CG2 ILE A 144 187.605 36.547 541.990 1.00 39.60 C ANISOU 1027 CG2 ILE A 144 5063 6182 3801 -360 -681 -716 C ATOM 1028 CD1 ILE A 144 186.665 35.170 544.543 1.00 62.63 C ANISOU 1028 CD1 ILE A 144 8281 9188 6327 -135 -567 -650 C ATOM 1029 N ALA A 145 191.036 37.363 541.746 1.00 43.08 N ANISOU 1029 N ALA A 145 5273 6788 4309 -682 -1176 -770 N ATOM 1030 CA ALA A 145 191.601 38.366 540.851 1.00 43.72 C ANISOU 1030 CA ALA A 145 5265 6814 4534 -832 -1230 -811 C ATOM 1031 C ALA A 145 192.600 37.741 539.887 1.00 45.64 C ANISOU 1031 C ALA A 145 5235 7170 4937 -873 -1277 -710 C ATOM 1032 O ALA A 145 192.614 38.071 538.695 1.00 46.74 O ANISOU 1032 O ALA A 145 5261 7266 5230 -924 -1204 -683 O ATOM 1033 CB ALA A 145 192.253 39.485 541.663 1.00 41.47 C ANISOU 1033 CB ALA A 145 5115 6491 4152 -974 -1409 -933 C ATOM 1034 N ALA A 146 193.442 36.830 540.384 1.00 46.39 N ANISOU 1034 N ALA A 146 5226 7409 4990 -839 -1390 -646 N ATOM 1035 CA ALA A 146 194.387 36.144 539.510 1.00 46.89 C ANISOU 1035 CA ALA A 146 5027 7585 5205 -845 -1414 -545 C ATOM 1036 C ALA A 146 193.669 35.307 538.460 1.00 48.98 C ANISOU 1036 C ALA A 146 5216 7822 5571 -727 -1218 -470 C ATOM 1037 O ALA A 146 194.163 35.165 537.336 1.00 49.34 O ANISOU 1037 O ALA A 146 5084 7901 5762 -753 -1176 -418 O ATOM 1038 CB ALA A 146 195.334 35.269 540.337 1.00 40.17 C ANISOU 1038 CB ALA A 146 4089 6889 4286 -797 -1570 -483 C ATOM 1039 N ALA A 147 192.508 34.744 538.804 1.00 47.64 N ANISOU 1039 N ALA A 147 5182 7594 5326 -603 -1096 -462 N ATOM 1040 CA ALA A 147 191.760 33.943 537.840 1.00 45.51 C ANISOU 1040 CA ALA A 147 4852 7288 5152 -508 -930 -400 C ATOM 1041 C ALA A 147 191.220 34.802 536.702 1.00 42.15 C ANISOU 1041 C ALA A 147 4418 6766 4833 -572 -834 -434 C ATOM 1042 O ALA A 147 191.283 34.406 535.532 1.00 37.26 O ANISOU 1042 O ALA A 147 3675 6156 4327 -558 -763 -386 O ATOM 1043 CB ALA A 147 190.624 33.202 538.546 1.00 42.30 C ANISOU 1043 CB ALA A 147 4583 6838 4650 -383 -828 -377 C ATOM 1044 N TRP A 148 190.685 35.981 537.023 1.00 41.02 N ANISOU 1044 N TRP A 148 4418 6523 4644 -635 -832 -517 N ATOM 1045 CA TRP A 148 190.139 36.848 535.985 1.00 39.26 C ANISOU 1045 CA TRP A 148 4201 6198 4518 -684 -749 -538 C ATOM 1046 C TRP A 148 191.244 37.449 535.124 1.00 44.10 C ANISOU 1046 C TRP A 148 4680 6842 5236 -816 -815 -524 C ATOM 1047 O TRP A 148 191.086 37.572 533.904 1.00 40.41 O ANISOU 1047 O TRP A 148 4139 6348 4868 -828 -734 -485 O ATOM 1048 CB TRP A 148 189.286 37.947 536.616 1.00 40.49 C ANISOU 1048 CB TRP A 148 4557 6226 4602 -696 -722 -627 C ATOM 1049 CG TRP A 148 187.939 37.471 537.074 1.00 41.71 C ANISOU 1049 CG TRP A 148 4814 6335 4698 -560 -593 -622 C ATOM 1050 CD1 TRP A 148 187.601 37.037 538.323 1.00 45.87 C ANISOU 1050 CD1 TRP A 148 5458 6886 5084 -484 -586 -638 C ATOM 1051 CD2 TRP A 148 186.749 37.379 536.282 1.00 38.18 C ANISOU 1051 CD2 TRP A 148 4352 5821 4334 -489 -452 -588 C ATOM 1052 NE1 TRP A 148 186.274 36.682 538.358 1.00 44.49 N ANISOU 1052 NE1 TRP A 148 5330 6661 4913 -374 -431 -611 N ATOM 1053 CE2 TRP A 148 185.728 36.883 537.117 1.00 41.52 C ANISOU 1053 CE2 TRP A 148 4865 6231 4681 -377 -357 -583 C ATOM 1054 CE3 TRP A 148 186.447 37.669 534.947 1.00 42.02 C ANISOU 1054 CE3 TRP A 148 4755 6263 4947 -510 -401 -556 C ATOM 1055 CZ2 TRP A 148 184.428 36.670 536.662 1.00 41.97 C ANISOU 1055 CZ2 TRP A 148 4906 6235 4806 -296 -220 -546 C ATOM 1056 CZ3 TRP A 148 185.155 37.457 534.497 1.00 43.80 C ANISOU 1056 CZ3 TRP A 148 4982 6437 5224 -423 -283 -525 C ATOM 1057 CH2 TRP A 148 184.162 36.963 535.353 1.00 40.76 C ANISOU 1057 CH2 TRP A 148 4661 6042 4782 -322 -197 -520 C ATOM 1058 N VAL A 149 192.369 37.825 535.736 1.00 45.85 N ANISOU 1058 N VAL A 149 4864 7124 5432 -919 -965 -549 N ATOM 1059 CA VAL A 149 193.468 38.411 534.972 1.00 45.67 C ANISOU 1059 CA VAL A 149 4691 7137 5524 -1061 -1024 -524 C ATOM 1060 C VAL A 149 194.095 37.369 534.052 1.00 41.98 C ANISOU 1060 C VAL A 149 4009 6794 5149 -1003 -971 -423 C ATOM 1061 O VAL A 149 194.371 37.641 532.878 1.00 44.89 O ANISOU 1061 O VAL A 149 4275 7161 5619 -1053 -901 -378 O ATOM 1062 CB VAL A 149 194.511 39.032 535.917 1.00 46.32 C ANISOU 1062 CB VAL A 149 4771 7261 5567 -1198 -1216 -576 C ATOM 1063 CG1 VAL A 149 195.728 39.494 535.133 1.00 43.82 C ANISOU 1063 CG1 VAL A 149 4252 7005 5392 -1351 -1271 -526 C ATOM 1064 CG2 VAL A 149 193.900 40.195 536.684 1.00 45.38 C ANISOU 1064 CG2 VAL A 149 4894 6991 5359 -1263 -1255 -694 C ATOM 1065 N LEU A 150 194.332 36.161 534.571 1.00 37.97 N ANISOU 1065 N LEU A 150 3442 6387 4596 -888 -996 -382 N ATOM 1066 CA LEU A 150 194.872 35.093 533.735 1.00 40.67 C ANISOU 1066 CA LEU A 150 3604 6829 5021 -805 -932 -295 C ATOM 1067 C LEU A 150 193.925 34.754 532.592 1.00 41.27 C ANISOU 1067 C LEU A 150 3712 6831 5136 -730 -765 -278 C ATOM 1068 O LEU A 150 194.367 34.499 531.466 1.00 40.55 O ANISOU 1068 O LEU A 150 3497 6783 5126 -723 -691 -229 O ATOM 1069 CB LEU A 150 195.155 33.852 534.579 1.00 43.72 C ANISOU 1069 CB LEU A 150 3958 7304 5348 -677 -986 -254 C ATOM 1070 CG LEU A 150 196.573 33.721 535.133 1.00 55.61 C ANISOU 1070 CG LEU A 150 5300 8955 6875 -717 -1144 -215 C ATOM 1071 CD1 LEU A 150 196.674 32.514 536.047 1.00 56.41 C ANISOU 1071 CD1 LEU A 150 5412 9123 6899 -570 -1199 -166 C ATOM 1072 CD2 LEU A 150 197.576 33.618 533.995 1.00 59.42 C ANISOU 1072 CD2 LEU A 150 5547 9526 7505 -744 -1098 -149 C ATOM 1073 N SER A 151 192.619 34.741 532.864 1.00 36.38 N ANISOU 1073 N SER A 151 3258 6109 4456 -671 -703 -315 N ATOM 1074 CA SER A 151 191.652 34.465 531.807 1.00 35.21 C ANISOU 1074 CA SER A 151 3139 5893 4347 -612 -572 -301 C ATOM 1075 C SER A 151 191.685 35.548 530.737 1.00 31.80 C ANISOU 1075 C SER A 151 2694 5412 3976 -712 -534 -303 C ATOM 1076 O SER A 151 191.643 35.249 529.538 1.00 33.00 O ANISOU 1076 O SER A 151 2788 5575 4176 -687 -453 -265 O ATOM 1077 CB SER A 151 190.250 34.334 532.400 1.00 35.71 C ANISOU 1077 CB SER A 151 3356 5864 4349 -542 -522 -332 C ATOM 1078 OG SER A 151 190.189 33.257 533.319 1.00 38.72 O ANISOU 1078 OG SER A 151 3756 6286 4672 -449 -537 -310 O ATOM 1079 N PHE A 152 191.765 36.814 531.154 1.00 31.88 N ANISOU 1079 N PHE A 152 2775 5360 3979 -823 -594 -347 N ATOM 1080 CA PHE A 152 191.832 37.910 530.193 1.00 36.66 C ANISOU 1080 CA PHE A 152 3383 5901 4646 -925 -561 -335 C ATOM 1081 C PHE A 152 193.090 37.820 529.337 1.00 41.69 C ANISOU 1081 C PHE A 152 3842 6642 5358 -993 -554 -270 C ATOM 1082 O PHE A 152 193.039 38.029 528.121 1.00 43.27 O ANISOU 1082 O PHE A 152 4012 6829 5598 -1006 -466 -223 O ATOM 1083 CB PHE A 152 191.774 39.250 530.927 1.00 38.77 C ANISOU 1083 CB PHE A 152 3774 6062 4896 -1035 -635 -400 C ATOM 1084 CG PHE A 152 191.910 40.445 530.024 1.00 45.44 C ANISOU 1084 CG PHE A 152 4634 6819 5811 -1151 -608 -379 C ATOM 1085 CD1 PHE A 152 190.808 40.957 529.359 1.00 42.75 C ANISOU 1085 CD1 PHE A 152 4402 6360 5480 -1106 -524 -371 C ATOM 1086 CD2 PHE A 152 193.138 41.062 529.848 1.00 45.16 C ANISOU 1086 CD2 PHE A 152 4498 6819 5841 -1308 -670 -354 C ATOM 1087 CE1 PHE A 152 190.929 42.058 528.531 1.00 42.89 C ANISOU 1087 CE1 PHE A 152 4450 6288 5558 -1205 -499 -335 C ATOM 1088 CE2 PHE A 152 193.266 42.162 529.020 1.00 46.27 C ANISOU 1088 CE2 PHE A 152 4662 6867 6051 -1423 -636 -318 C ATOM 1089 CZ PHE A 152 192.159 42.660 528.362 1.00 47.63 C ANISOU 1089 CZ PHE A 152 4966 6913 6220 -1366 -549 -307 C ATOM 1090 N ILE A 153 194.231 37.509 529.956 1.00 44.36 N ANISOU 1090 N ILE A 153 4055 7091 5711 -1030 -643 -258 N ATOM 1091 CA ILE A 153 195.482 37.425 529.209 1.00 41.27 C ANISOU 1091 CA ILE A 153 3463 6813 5405 -1089 -626 -187 C ATOM 1092 C ILE A 153 195.480 36.222 528.273 1.00 38.12 C ANISOU 1092 C ILE A 153 2981 6488 5015 -947 -505 -134 C ATOM 1093 O ILE A 153 196.052 36.277 527.176 1.00 38.73 O ANISOU 1093 O ILE A 153 2952 6618 5146 -970 -416 -75 O ATOM 1094 CB ILE A 153 196.673 37.391 530.188 1.00 42.99 C ANISOU 1094 CB ILE A 153 3551 7139 5646 -1159 -771 -184 C ATOM 1095 CG1 ILE A 153 196.736 38.695 530.985 1.00 47.14 C ANISOU 1095 CG1 ILE A 153 4176 7575 6160 -1326 -898 -251 C ATOM 1096 CG2 ILE A 153 197.982 37.159 529.450 1.00 40.08 C ANISOU 1096 CG2 ILE A 153 2934 6911 5384 -1197 -740 -96 C ATOM 1097 CD1 ILE A 153 197.867 38.746 531.989 1.00 49.18 C ANISOU 1097 CD1 ILE A 153 4319 7936 6430 -1417 -1077 -259 C ATOM 1098 N LEU A 154 194.829 35.127 528.671 1.00 38.07 N ANISOU 1098 N LEU A 154 3034 6477 4952 -801 -492 -155 N ATOM 1099 CA LEU A 154 194.836 33.923 527.845 1.00 40.10 C ANISOU 1099 CA LEU A 154 3235 6784 5217 -667 -388 -120 C ATOM 1100 C LEU A 154 194.017 34.104 526.572 1.00 45.51 C ANISOU 1100 C LEU A 154 4005 7397 5890 -654 -275 -120 C ATOM 1101 O LEU A 154 194.423 33.643 525.499 1.00 48.24 O ANISOU 1101 O LEU A 154 4284 7797 6250 -608 -179 -84 O ATOM 1102 CB LEU A 154 194.310 32.728 528.643 1.00 42.36 C ANISOU 1102 CB LEU A 154 3581 7059 5455 -531 -409 -138 C ATOM 1103 CG LEU A 154 195.265 32.058 529.635 1.00 50.01 C ANISOU 1103 CG LEU A 154 4443 8129 6430 -482 -501 -109 C ATOM 1104 CD1 LEU A 154 194.588 30.872 530.304 1.00 51.23 C ANISOU 1104 CD1 LEU A 154 4689 8246 6532 -344 -498 -112 C ATOM 1105 CD2 LEU A 154 196.546 31.627 528.941 1.00 52.52 C ANISOU 1105 CD2 LEU A 154 4558 8571 6826 -449 -460 -47 C ATOM 1106 N TRP A 155 192.867 34.768 526.664 1.00 42.50 N ANISOU 1106 N TRP A 155 3774 6900 5476 -685 -284 -157 N ATOM 1107 CA TRP A 155 191.895 34.771 525.576 1.00 37.40 C ANISOU 1107 CA TRP A 155 3217 6187 4807 -649 -204 -156 C ATOM 1108 C TRP A 155 191.739 36.108 524.868 1.00 33.56 C ANISOU 1108 C TRP A 155 2778 5639 4332 -754 -185 -133 C ATOM 1109 O TRP A 155 191.598 36.129 523.644 1.00 33.19 O ANISOU 1109 O TRP A 155 2744 5596 4269 -742 -111 -98 O ATOM 1110 CB TRP A 155 190.527 34.320 526.098 1.00 35.39 C ANISOU 1110 CB TRP A 155 3081 5847 4518 -574 -218 -199 C ATOM 1111 CG TRP A 155 190.448 32.846 526.315 1.00 35.66 C ANISOU 1111 CG TRP A 155 3095 5914 4541 -460 -201 -205 C ATOM 1112 CD1 TRP A 155 190.429 32.188 527.510 1.00 36.21 C ANISOU 1112 CD1 TRP A 155 3170 5991 4598 -409 -246 -216 C ATOM 1113 CD2 TRP A 155 190.392 31.839 525.301 1.00 36.78 C ANISOU 1113 CD2 TRP A 155 3225 6072 4677 -381 -133 -200 C ATOM 1114 NE1 TRP A 155 190.355 30.831 527.302 1.00 35.35 N ANISOU 1114 NE1 TRP A 155 3050 5891 4491 -305 -208 -209 N ATOM 1115 CE2 TRP A 155 190.332 30.592 525.953 1.00 36.84 C ANISOU 1115 CE2 TRP A 155 3232 6081 4686 -288 -140 -208 C ATOM 1116 CE3 TRP A 155 190.384 31.872 523.903 1.00 36.80 C ANISOU 1116 CE3 TRP A 155 3237 6082 4662 -379 -67 -190 C ATOM 1117 CZ2 TRP A 155 190.264 29.390 525.255 1.00 38.11 C ANISOU 1117 CZ2 TRP A 155 3403 6232 4844 -197 -86 -217 C ATOM 1118 CZ3 TRP A 155 190.316 30.679 523.213 1.00 37.48 C ANISOU 1118 CZ3 TRP A 155 3339 6174 4728 -286 -16 -207 C ATOM 1119 CH2 TRP A 155 190.258 29.456 523.889 1.00 39.78 C ANISOU 1119 CH2 TRP A 155 3631 6449 5035 -199 -26 -225 C ATOM 1120 N ALA A 156 191.753 37.226 525.594 1.00 32.29 N ANISOU 1120 N ALA A 156 2663 5415 4192 -854 -251 -151 N ATOM 1121 CA ALA A 156 191.448 38.511 524.965 1.00 32.07 C ANISOU 1121 CA ALA A 156 2711 5293 4180 -943 -233 -126 C ATOM 1122 C ALA A 156 192.464 38.923 523.904 1.00 40.45 C ANISOU 1122 C ALA A 156 3680 6414 5276 -1028 -171 -48 C ATOM 1123 O ALA A 156 192.038 39.310 522.802 1.00 42.79 O ANISOU 1123 O ALA A 156 4037 6671 5552 -1026 -105 0 O ATOM 1124 CB ALA A 156 191.293 39.592 526.039 1.00 33.86 C ANISOU 1124 CB ALA A 156 3026 5417 4421 -1028 -316 -175 C ATOM 1125 N PRO A 157 193.784 38.881 524.143 1.00 44.61 N ANISOU 1125 N PRO A 157 4056 7040 5854 -1102 -186 -21 N ATOM 1126 CA PRO A 157 194.711 39.326 523.085 1.00 43.79 C ANISOU 1126 CA PRO A 157 3853 6995 5791 -1188 -101 69 C ATOM 1127 C PRO A 157 194.620 38.504 521.811 1.00 38.29 C ANISOU 1127 C PRO A 157 3143 6370 5037 -1076 27 112 C ATOM 1128 O PRO A 157 194.672 39.068 520.711 1.00 37.78 O ANISOU 1128 O PRO A 157 3108 6293 4954 -1118 114 182 O ATOM 1129 CB PRO A 157 196.091 39.191 523.749 1.00 43.83 C ANISOU 1129 CB PRO A 157 3664 7116 5873 -1265 -152 86 C ATOM 1130 CG PRO A 157 195.818 39.227 525.206 1.00 43.93 C ANISOU 1130 CG PRO A 157 3731 7083 5878 -1274 -297 0 C ATOM 1131 CD PRO A 157 194.514 38.518 525.370 1.00 45.08 C ANISOU 1131 CD PRO A 157 4021 7167 5939 -1121 -284 -58 C ATOM 1132 N ALA A 158 194.483 37.182 521.927 1.00 32.08 N ANISOU 1132 N ALA A 158 2328 5649 4213 -933 41 71 N ATOM 1133 CA ALA A 158 194.417 36.338 520.737 1.00 34.09 C ANISOU 1133 CA ALA A 158 2593 5960 4401 -824 157 90 C ATOM 1134 C ALA A 158 193.126 36.576 519.961 1.00 42.44 C ANISOU 1134 C ALA A 158 3828 6919 5378 -790 167 79 C ATOM 1135 O ALA A 158 193.145 36.707 518.733 1.00 52.85 O ANISOU 1135 O ALA A 158 5189 8258 6634 -781 257 127 O ATOM 1136 CB ALA A 158 194.551 34.866 521.127 1.00 29.71 C ANISOU 1136 CB ALA A 158 1986 5468 3836 -681 158 41 C ATOM 1137 N ILE A 159 191.992 36.638 520.661 1.00 38.22 N ANISOU 1137 N ILE A 159 3398 6285 4840 -767 77 21 N ATOM 1138 CA ILE A 159 190.711 36.807 519.978 1.00 33.85 C ANISOU 1138 CA ILE A 159 2986 5649 4227 -727 69 16 C ATOM 1139 C ILE A 159 190.642 38.164 519.286 1.00 31.99 C ANISOU 1139 C ILE A 159 2814 5354 3987 -818 89 90 C ATOM 1140 O ILE A 159 190.165 38.276 518.150 1.00 28.63 O ANISOU 1140 O ILE A 159 2472 4920 3488 -790 125 130 O ATOM 1141 CB ILE A 159 189.547 36.616 520.968 1.00 33.97 C ANISOU 1141 CB ILE A 159 3066 5579 4261 -682 -18 -49 C ATOM 1142 CG1 ILE A 159 189.476 35.157 521.422 1.00 31.84 C ANISOU 1142 CG1 ILE A 159 2760 5355 3984 -584 -23 -104 C ATOM 1143 CG2 ILE A 159 188.230 37.046 520.338 1.00 32.33 C ANISOU 1143 CG2 ILE A 159 2975 5286 4021 -656 -40 -39 C ATOM 1144 CD1 ILE A 159 188.409 34.888 522.455 1.00 32.05 C ANISOU 1144 CD1 ILE A 159 2836 5310 4033 -545 -87 -153 C ATOM 1145 N LEU A 160 191.133 39.211 519.949 1.00 34.59 N ANISOU 1145 N LEU A 160 3117 5635 4389 -933 57 111 N ATOM 1146 CA LEU A 160 190.984 40.561 519.419 1.00 35.07 C ANISOU 1146 CA LEU A 160 3261 5602 4462 -1023 68 183 C ATOM 1147 C LEU A 160 192.020 40.897 518.352 1.00 37.04 C ANISOU 1147 C LEU A 160 3454 5923 4698 -1097 175 285 C ATOM 1148 O LEU A 160 191.719 41.662 517.429 1.00 39.77 O ANISOU 1148 O LEU A 160 3894 6212 5003 -1125 215 366 O ATOM 1149 CB LEU A 160 191.071 41.582 520.555 1.00 35.80 C ANISOU 1149 CB LEU A 160 3375 5587 4640 -1125 -9 155 C ATOM 1150 CG LEU A 160 190.017 41.479 521.658 1.00 40.00 C ANISOU 1150 CG LEU A 160 3984 6035 5178 -1055 -93 62 C ATOM 1151 CD1 LEU A 160 190.302 42.490 522.758 1.00 40.72 C ANISOU 1151 CD1 LEU A 160 4113 6026 5333 -1161 -160 23 C ATOM 1152 CD2 LEU A 160 188.621 41.674 521.091 1.00 39.92 C ANISOU 1152 CD2 LEU A 160 4095 5940 5131 -963 -94 77 C ATOM 1153 N PHE A 161 193.233 40.352 518.454 1.00 32.83 N ANISOU 1153 N PHE A 161 2762 5515 4196 -1123 228 295 N ATOM 1154 CA PHE A 161 194.353 40.837 517.658 1.00 39.39 C ANISOU 1154 CA PHE A 161 3505 6416 5046 -1219 340 403 C ATOM 1155 C PHE A 161 194.990 39.791 516.754 1.00 37.73 C ANISOU 1155 C PHE A 161 3210 6359 4765 -1123 472 428 C ATOM 1156 O PHE A 161 195.990 40.100 516.096 1.00 38.95 O ANISOU 1156 O PHE A 161 3270 6595 4936 -1190 592 525 O ATOM 1157 CB PHE A 161 195.433 41.425 518.578 1.00 44.23 C ANISOU 1157 CB PHE A 161 3971 7041 5793 -1371 296 415 C ATOM 1158 CG PHE A 161 194.912 42.449 519.548 1.00 49.43 C ANISOU 1158 CG PHE A 161 4728 7538 6514 -1468 167 370 C ATOM 1159 CD1 PHE A 161 194.026 43.431 519.135 1.00 49.25 C ANISOU 1159 CD1 PHE A 161 4883 7360 6467 -1491 159 403 C ATOM 1160 CD2 PHE A 161 195.304 42.422 520.876 1.00 54.43 C ANISOU 1160 CD2 PHE A 161 5288 8172 7219 -1523 52 294 C ATOM 1161 CE1 PHE A 161 193.544 44.371 520.027 1.00 48.08 C ANISOU 1161 CE1 PHE A 161 4841 7050 6376 -1561 56 353 C ATOM 1162 CE2 PHE A 161 194.827 43.358 521.774 1.00 52.88 C ANISOU 1162 CE2 PHE A 161 5211 7822 7062 -1602 -59 237 C ATOM 1163 CZ PHE A 161 193.945 44.334 521.349 1.00 50.92 C ANISOU 1163 CZ PHE A 161 5142 7408 6797 -1618 -49 263 C ATOM 1164 N TRP A 162 194.456 38.567 516.699 1.00 35.13 N ANISOU 1164 N TRP A 162 2918 6069 4362 -968 464 346 N ATOM 1165 CA TRP A 162 195.034 37.557 515.815 1.00 40.93 C ANISOU 1165 CA TRP A 162 3604 6929 5019 -862 597 355 C ATOM 1166 C TRP A 162 194.950 37.987 514.356 1.00 44.12 C ANISOU 1166 C TRP A 162 4116 7347 5300 -863 715 439 C ATOM 1167 O TRP A 162 195.858 37.704 513.566 1.00 44.21 O ANISOU 1167 O TRP A 162 4057 7473 5268 -837 871 497 O ATOM 1168 CB TRP A 162 194.338 36.211 516.015 1.00 39.60 C ANISOU 1168 CB TRP A 162 3494 6758 4793 -707 551 243 C ATOM 1169 CG TRP A 162 194.865 35.120 515.135 1.00 42.07 C ANISOU 1169 CG TRP A 162 3791 7173 5019 -581 684 229 C ATOM 1170 CD1 TRP A 162 194.221 34.530 514.087 1.00 45.70 C ANISOU 1170 CD1 TRP A 162 4408 7624 5330 -484 726 192 C ATOM 1171 CD2 TRP A 162 196.150 34.491 515.223 1.00 47.23 C ANISOU 1171 CD2 TRP A 162 4267 7952 5728 -530 791 249 C ATOM 1172 NE1 TRP A 162 195.023 33.569 513.519 1.00 52.21 N ANISOU 1172 NE1 TRP A 162 5186 8547 6103 -372 863 175 N ATOM 1173 CE2 TRP A 162 196.213 33.526 514.198 1.00 52.73 C ANISOU 1173 CE2 TRP A 162 5037 8698 6299 -389 914 216 C ATOM 1174 CE3 TRP A 162 197.252 34.648 516.070 1.00 49.51 C ANISOU 1174 CE3 TRP A 162 4338 8315 6158 -587 788 290 C ATOM 1175 CZ2 TRP A 162 197.334 32.723 513.996 1.00 57.59 C ANISOU 1175 CZ2 TRP A 162 5516 9430 6934 -286 1054 225 C ATOM 1176 CZ3 TRP A 162 198.364 33.850 515.867 1.00 52.42 C ANISOU 1176 CZ3 TRP A 162 4547 8813 6556 -491 912 311 C ATOM 1177 CH2 TRP A 162 198.396 32.900 514.839 1.00 55.84 C ANISOU 1177 CH2 TRP A 162 5059 9289 6871 -333 1055 280 C ATOM 1178 N GLN A 163 193.866 38.673 513.984 1.00 41.25 N ANISOU 1178 N GLN A 163 3926 6873 4874 -883 647 455 N ATOM 1179 CA GLN A 163 193.724 39.172 512.619 1.00 39.96 C ANISOU 1179 CA GLN A 163 3888 6717 4578 -886 740 550 C ATOM 1180 C GLN A 163 194.883 40.086 512.239 1.00 39.17 C ANISOU 1180 C GLN A 163 3692 6662 4528 -1015 873 689 C ATOM 1181 O GLN A 163 195.362 40.054 511.099 1.00 38.95 O ANISOU 1181 O GLN A 163 3693 6718 4389 -993 1027 772 O ATOM 1182 CB GLN A 163 192.388 39.902 512.471 1.00 34.71 C ANISOU 1182 CB GLN A 163 3398 5916 3872 -893 618 561 C ATOM 1183 CG GLN A 163 192.132 40.928 513.567 1.00 46.29 C ANISOU 1183 CG GLN A 163 4844 7254 5490 -999 511 566 C ATOM 1184 CD GLN A 163 190.719 41.476 513.549 1.00 42.79 C ANISOU 1184 CD GLN A 163 4557 6678 5023 -964 391 560 C ATOM 1185 OE1 GLN A 163 190.201 41.858 512.500 1.00 48.46 O ANISOU 1185 OE1 GLN A 163 5404 7376 5632 -936 404 636 O ATOM 1186 NE2 GLN A 163 190.085 41.515 514.715 1.00 39.80 N ANISOU 1186 NE2 GLN A 163 4165 6216 4743 -956 277 476 N ATOM 1187 N PHE A 164 195.349 40.906 513.183 1.00 37.15 N ANISOU 1187 N PHE A 164 3327 6350 4437 -1156 817 716 N ATOM 1188 CA PHE A 164 196.477 41.790 512.916 1.00 44.02 C ANISOU 1188 CA PHE A 164 4084 7253 5388 -1309 930 849 C ATOM 1189 C PHE A 164 197.803 41.040 512.931 1.00 40.09 C ANISOU 1189 C PHE A 164 3357 6932 4944 -1293 1057 864 C ATOM 1190 O PHE A 164 198.760 41.471 512.278 1.00 42.18 O ANISOU 1190 O PHE A 164 3522 7274 5229 -1375 1214 992 O ATOM 1191 CB PHE A 164 196.504 42.932 513.934 1.00 44.16 C ANISOU 1191 CB PHE A 164 4077 7134 5567 -1479 807 859 C ATOM 1192 CG PHE A 164 195.224 43.714 514.002 1.00 44.16 C ANISOU 1192 CG PHE A 164 4291 6952 5535 -1478 692 846 C ATOM 1193 CD1 PHE A 164 194.887 44.606 512.997 1.00 45.91 C ANISOU 1193 CD1 PHE A 164 4662 7095 5685 -1514 752 971 C ATOM 1194 CD2 PHE A 164 194.359 43.561 515.074 1.00 45.23 C ANISOU 1194 CD2 PHE A 164 4478 6996 5712 -1430 533 720 C ATOM 1195 CE1 PHE A 164 193.709 45.329 513.057 1.00 45.61 C ANISOU 1195 CE1 PHE A 164 4810 6889 5631 -1493 644 969 C ATOM 1196 CE2 PHE A 164 193.180 44.282 515.140 1.00 45.48 C ANISOU 1196 CE2 PHE A 164 4688 6866 5727 -1410 442 714 C ATOM 1197 CZ PHE A 164 192.855 45.166 514.130 1.00 45.10 C ANISOU 1197 CZ PHE A 164 4777 6739 5621 -1437 493 838 C ATOM 1198 N ILE A 165 197.882 39.927 513.665 1.00 44.20 N ANISOU 1198 N ILE A 165 3784 7515 5494 -1184 999 747 N ATOM 1199 CA ILE A 165 199.106 39.129 513.680 1.00 41.38 C ANISOU 1199 CA ILE A 165 3204 7325 5192 -1133 1117 762 C ATOM 1200 C ILE A 165 199.313 38.454 512.330 1.00 43.75 C ANISOU 1200 C ILE A 165 3560 7731 5332 -996 1319 797 C ATOM 1201 O ILE A 165 200.406 38.503 511.753 1.00 47.61 O ANISOU 1201 O ILE A 165 3899 8346 5843 -1015 1503 899 O ATOM 1202 CB ILE A 165 199.066 38.100 514.823 1.00 47.02 C ANISOU 1202 CB ILE A 165 3831 8062 5972 -1035 994 636 C ATOM 1203 CG1 ILE A 165 198.899 38.803 516.170 1.00 49.40 C ANISOU 1203 CG1 ILE A 165 4097 8268 6405 -1170 800 599 C ATOM 1204 CG2 ILE A 165 200.331 37.256 514.819 1.00 48.43 C ANISOU 1204 CG2 ILE A 165 3774 8413 6215 -958 1114 661 C ATOM 1205 CD1 ILE A 165 200.028 39.743 516.507 1.00 57.02 C ANISOU 1205 CD1 ILE A 165 4869 9273 7525 -1364 807 696 C ATOM 1206 N VAL A 166 198.269 37.807 511.808 1.00 43.07 N ANISOU 1206 N VAL A 166 3688 7597 5080 -857 1290 710 N ATOM 1207 CA VAL A 166 198.358 37.221 510.476 1.00 46.17 C ANISOU 1207 CA VAL A 166 4187 8072 5285 -730 1466 727 C ATOM 1208 C VAL A 166 198.216 38.272 509.384 1.00 42.71 C ANISOU 1208 C VAL A 166 3883 7612 4732 -815 1559 860 C ATOM 1209 O VAL A 166 198.541 37.995 508.223 1.00 44.38 O ANISOU 1209 O VAL A 166 4165 7914 4783 -736 1742 909 O ATOM 1210 CB VAL A 166 197.303 36.118 510.285 1.00 52.79 C ANISOU 1210 CB VAL A 166 5214 8860 5982 -565 1383 579 C ATOM 1211 CG1 VAL A 166 197.572 34.961 511.234 1.00 50.83 C ANISOU 1211 CG1 VAL A 166 4840 8638 5835 -463 1331 467 C ATOM 1212 CG2 VAL A 166 195.902 36.677 510.494 1.00 50.37 C ANISOU 1212 CG2 VAL A 166 5090 8406 5645 -617 1188 544 C ATOM 1213 N GLY A 167 197.742 39.469 509.723 1.00 43.48 N ANISOU 1213 N GLY A 167 4032 7586 4900 -966 1444 923 N ATOM 1214 CA GLY A 167 197.630 40.542 508.758 1.00 45.77 C ANISOU 1214 CA GLY A 167 4452 7838 5100 -1053 1525 1070 C ATOM 1215 C GLY A 167 196.409 40.493 507.871 1.00 45.01 C ANISOU 1215 C GLY A 167 4634 7679 4789 -958 1467 1050 C ATOM 1216 O GLY A 167 196.352 41.238 506.886 1.00 47.48 O ANISOU 1216 O GLY A 167 5076 7981 4982 -998 1554 1182 O ATOM 1217 N VAL A 168 195.433 39.645 508.180 1.00 42.76 N ANISOU 1217 N VAL A 168 4442 7352 4451 -840 1318 898 N ATOM 1218 CA VAL A 168 194.219 39.545 507.378 1.00 46.07 C ANISOU 1218 CA VAL A 168 5106 7720 4679 -756 1229 871 C ATOM 1219 C VAL A 168 193.086 39.059 508.270 1.00 44.00 C ANISOU 1219 C VAL A 168 4873 7362 4484 -708 1009 727 C ATOM 1220 O VAL A 168 193.268 38.160 509.097 1.00 40.76 O ANISOU 1220 O VAL A 168 4347 6973 4165 -660 976 611 O ATOM 1221 CB VAL A 168 194.421 38.618 506.158 1.00 53.26 C ANISOU 1221 CB VAL A 168 6133 8750 5354 -620 1369 842 C ATOM 1222 CG1 VAL A 168 194.837 37.219 506.599 1.00 49.43 C ANISOU 1222 CG1 VAL A 168 5544 8335 4901 -504 1402 693 C ATOM 1223 CG2 VAL A 168 193.160 38.569 505.308 1.00 42.52 C ANISOU 1223 CG2 VAL A 168 5030 7340 3786 -551 1247 817 C ATOM 1224 N ARG A 169 191.917 39.675 508.115 1.00 47.44 N ANISOU 1224 N ARG A 169 5455 7691 4881 -718 865 748 N ATOM 1225 CA ARG A 169 190.702 39.244 508.796 1.00 40.37 C ANISOU 1225 CA ARG A 169 4595 6711 4033 -665 669 629 C ATOM 1226 C ARG A 169 189.918 38.350 507.842 1.00 37.50 C ANISOU 1226 C ARG A 169 4392 6387 3470 -549 618 559 C ATOM 1227 O ARG A 169 189.353 38.830 506.853 1.00 37.80 O ANISOU 1227 O ARG A 169 4589 6416 3357 -535 587 633 O ATOM 1228 CB ARG A 169 189.863 40.440 509.241 1.00 35.86 C ANISOU 1228 CB ARG A 169 4068 6000 3555 -732 541 693 C ATOM 1229 CG ARG A 169 188.551 40.048 509.899 1.00 36.57 C ANISOU 1229 CG ARG A 169 4182 6013 3698 -671 357 588 C ATOM 1230 CD ARG A 169 187.734 41.264 510.294 1.00 34.00 C ANISOU 1230 CD ARG A 169 3903 5550 3467 -712 254 656 C ATOM 1231 NE ARG A 169 186.496 40.882 510.967 1.00 36.57 N ANISOU 1231 NE ARG A 169 4222 5815 3856 -647 100 563 N ATOM 1232 CZ ARG A 169 186.391 40.674 512.275 1.00 37.89 C ANISOU 1232 CZ ARG A 169 4285 5938 4174 -658 59 477 C ATOM 1233 NH1 ARG A 169 187.452 40.813 513.059 1.00 36.50 N ANISOU 1233 NH1 ARG A 169 4005 5770 4093 -733 136 463 N ATOM 1234 NH2 ARG A 169 185.224 40.327 512.801 1.00 32.73 N ANISOU 1234 NH2 ARG A 169 3628 5238 3572 -596 -60 409 N ATOM 1235 N THR A 170 189.889 37.052 508.135 1.00 38.21 N ANISOU 1235 N THR A 170 4449 6514 3557 -469 601 416 N ATOM 1236 CA THR A 170 189.159 36.102 507.309 1.00 41.20 C ANISOU 1236 CA THR A 170 4983 6913 3759 -373 537 324 C ATOM 1237 C THR A 170 187.682 36.014 507.668 1.00 43.39 C ANISOU 1237 C THR A 170 5308 7098 4080 -366 315 265 C ATOM 1238 O THR A 170 186.917 35.387 506.928 1.00 44.70 O ANISOU 1238 O THR A 170 5610 7272 4104 -311 221 200 O ATOM 1239 CB THR A 170 189.795 34.711 507.412 1.00 40.64 C ANISOU 1239 CB THR A 170 4871 6902 3670 -287 625 197 C ATOM 1240 OG1 THR A 170 189.738 34.255 508.769 1.00 41.04 O ANISOU 1240 OG1 THR A 170 4771 6900 3923 -297 557 121 O ATOM 1241 CG2 THR A 170 191.247 34.759 506.963 1.00 45.30 C ANISOU 1241 CG2 THR A 170 5397 7600 4215 -273 860 263 C ATOM 1242 N VAL A 171 187.266 36.621 508.777 1.00 43.85 N ANISOU 1242 N VAL A 171 5259 7073 4330 -421 229 283 N ATOM 1243 CA VAL A 171 185.854 36.654 509.148 1.00 40.83 C ANISOU 1243 CA VAL A 171 4897 6609 4007 -410 40 248 C ATOM 1244 C VAL A 171 185.153 37.649 508.227 1.00 41.71 C ANISOU 1244 C VAL A 171 5134 6698 4015 -414 -34 363 C ATOM 1245 O VAL A 171 185.365 38.860 508.330 1.00 43.53 O ANISOU 1245 O VAL A 171 5358 6883 4300 -464 2 483 O ATOM 1246 CB VAL A 171 185.665 37.029 510.621 1.00 41.75 C ANISOU 1246 CB VAL A 171 4874 6647 4344 -452 -1 235 C ATOM 1247 CG1 VAL A 171 184.192 36.952 511.004 1.00 42.41 C ANISOU 1247 CG1 VAL A 171 4960 6659 4494 -425 -171 199 C ATOM 1248 CG2 VAL A 171 186.506 36.124 511.514 1.00 33.93 C ANISOU 1248 CG2 VAL A 171 3764 5688 3441 -446 75 146 C ATOM 1249 N GLU A 172 184.322 37.140 507.324 1.00 42.92 N ANISOU 1249 N GLU A 172 5410 6878 4018 -364 -147 329 N ATOM 1250 CA GLU A 172 183.664 37.992 506.349 1.00 47.87 C ANISOU 1250 CA GLU A 172 6168 7500 4520 -352 -233 445 C ATOM 1251 C GLU A 172 182.546 38.799 507.009 1.00 48.49 C ANISOU 1251 C GLU A 172 6182 7481 4761 -356 -379 499 C ATOM 1252 O GLU A 172 182.159 38.563 508.157 1.00 47.28 O ANISOU 1252 O GLU A 172 5898 7273 4795 -363 -421 430 O ATOM 1253 CB GLU A 172 183.115 37.153 505.196 1.00 51.68 C ANISOU 1253 CB GLU A 172 6805 8049 4782 -299 -333 381 C ATOM 1254 CG GLU A 172 184.144 36.214 504.586 1.00 64.70 C ANISOU 1254 CG GLU A 172 8532 9784 6266 -271 -180 300 C ATOM 1255 CD GLU A 172 183.575 35.369 503.465 1.00 78.24 C ANISOU 1255 CD GLU A 172 10431 11549 7747 -221 -290 213 C ATOM 1256 OE1 GLU A 172 182.940 35.939 502.553 1.00 84.13 O ANISOU 1256 OE1 GLU A 172 11311 12316 8338 -210 -403 299 O ATOM 1257 OE2 GLU A 172 183.758 34.134 503.502 1.00 82.70 O ANISOU 1257 OE2 GLU A 172 11016 12126 8280 -193 -274 60 O ATOM 1258 N ASP A 173 182.031 39.771 506.260 1.00 50.59 N ANISOU 1258 N ASP A 173 6549 7725 4948 -339 -448 633 N ATOM 1259 CA ASP A 173 180.970 40.630 506.768 1.00 50.76 C ANISOU 1259 CA ASP A 173 6519 7650 5117 -317 -576 702 C ATOM 1260 C ASP A 173 179.708 39.820 507.037 1.00 44.51 C ANISOU 1260 C ASP A 173 5657 6866 4387 -275 -759 605 C ATOM 1261 O ASP A 173 179.266 39.034 506.193 1.00 42.76 O ANISOU 1261 O ASP A 173 5511 6717 4017 -254 -868 554 O ATOM 1262 CB ASP A 173 180.681 41.755 505.772 1.00 59.78 C ANISOU 1262 CB ASP A 173 7800 8771 6143 -289 -620 877 C ATOM 1263 CG ASP A 173 179.557 42.663 506.227 1.00 67.63 C ANISOU 1263 CG ASP A 173 8746 9660 7292 -240 -750 958 C ATOM 1264 OD1 ASP A 173 179.579 43.094 507.399 1.00 70.09 O ANISOU 1264 OD1 ASP A 173 8946 9874 7810 -257 -700 936 O ATOM 1265 OD2 ASP A 173 178.658 42.954 505.410 1.00 71.36 O ANISOU 1265 OD2 ASP A 173 9295 10147 7673 -176 -901 1043 O ATOM 1266 N GLY A 174 179.130 40.015 508.220 1.00 43.42 N ANISOU 1266 N GLY A 174 5379 6651 4469 -269 -791 579 N ATOM 1267 CA GLY A 174 177.971 39.263 508.645 1.00 38.93 C ANISOU 1267 CA GLY A 174 4707 6086 3999 -242 -936 498 C ATOM 1268 C GLY A 174 178.279 37.975 509.375 1.00 37.66 C ANISOU 1268 C GLY A 174 4463 5948 3897 -278 -888 345 C ATOM 1269 O GLY A 174 177.347 37.314 509.851 1.00 37.86 O ANISOU 1269 O GLY A 174 4391 5966 4027 -272 -991 281 O ATOM 1270 N GLU A 175 179.547 37.593 509.474 1.00 39.44 N ANISOU 1270 N GLU A 175 4718 6201 4067 -313 -735 295 N ATOM 1271 CA GLU A 175 179.967 36.424 510.228 1.00 41.64 C ANISOU 1271 CA GLU A 175 4924 6490 4407 -333 -676 165 C ATOM 1272 C GLU A 175 180.572 36.851 511.558 1.00 38.18 C ANISOU 1272 C GLU A 175 4378 6000 4130 -356 -560 166 C ATOM 1273 O GLU A 175 181.011 37.990 511.732 1.00 39.38 O ANISOU 1273 O GLU A 175 4537 6113 4313 -372 -496 253 O ATOM 1274 CB GLU A 175 180.986 35.600 509.436 1.00 51.64 C ANISOU 1274 CB GLU A 175 6289 7829 5502 -335 -586 103 C ATOM 1275 CG GLU A 175 180.470 35.069 508.112 1.00 60.75 C ANISOU 1275 CG GLU A 175 7585 9036 6462 -314 -699 75 C ATOM 1276 CD GLU A 175 181.547 34.361 507.315 1.00 69.68 C ANISOU 1276 CD GLU A 175 8836 10232 7406 -298 -577 15 C ATOM 1277 OE1 GLU A 175 182.739 34.515 507.657 1.00 72.31 O ANISOU 1277 OE1 GLU A 175 9129 10584 7762 -301 -397 32 O ATOM 1278 OE2 GLU A 175 181.202 33.650 506.350 1.00 72.98 O ANISOU 1278 OE2 GLU A 175 9387 10686 7656 -279 -662 -53 O ATOM 1279 N CYS A 176 180.590 35.914 512.505 1.00 40.40 N ANISOU 1279 N CYS A 176 4569 6271 4508 -361 -542 69 N ATOM 1280 CA CYS A 176 181.193 36.175 513.811 1.00 39.85 C ANISOU 1280 CA CYS A 176 4409 6164 4567 -381 -447 57 C ATOM 1281 C CYS A 176 181.700 34.849 514.370 1.00 38.83 C ANISOU 1281 C CYS A 176 4233 6061 4458 -380 -401 -46 C ATOM 1282 O CYS A 176 180.906 34.014 514.813 1.00 40.22 O ANISOU 1282 O CYS A 176 4366 6215 4700 -368 -465 -104 O ATOM 1283 CB CYS A 176 180.205 36.836 514.759 1.00 38.36 C ANISOU 1283 CB CYS A 176 4149 5899 4526 -364 -499 85 C ATOM 1284 SG CYS A 176 181.001 37.393 516.271 0.79 33.86 S ANISOU 1284 SG CYS A 176 3516 5279 4071 -393 -392 71 S ATOM 1285 N TYR A 177 183.018 34.671 514.348 1.00 33.42 N ANISOU 1285 N TYR A 177 3549 5422 3728 -391 -286 -57 N ATOM 1286 CA TYR A 177 183.638 33.476 514.898 1.00 35.11 C ANISOU 1286 CA TYR A 177 3717 5657 3965 -372 -233 -140 C ATOM 1287 C TYR A 177 185.101 33.779 515.181 1.00 34.64 C ANISOU 1287 C TYR A 177 3608 5646 3908 -390 -109 -114 C ATOM 1288 O TYR A 177 185.670 34.734 514.647 1.00 32.58 O ANISOU 1288 O TYR A 177 3368 5410 3602 -424 -56 -39 O ATOM 1289 CB TYR A 177 183.497 32.278 513.951 1.00 35.87 C ANISOU 1289 CB TYR A 177 3898 5778 3953 -336 -256 -214 C ATOM 1290 CG TYR A 177 184.108 32.493 512.585 1.00 43.02 C ANISOU 1290 CG TYR A 177 4910 6747 4687 -322 -201 -188 C ATOM 1291 CD1 TYR A 177 183.401 33.143 511.582 1.00 44.33 C ANISOU 1291 CD1 TYR A 177 5171 6920 4754 -331 -282 -136 C ATOM 1292 CD2 TYR A 177 185.387 32.038 512.294 1.00 47.74 C ANISOU 1292 CD2 TYR A 177 5513 7406 5219 -291 -64 -208 C ATOM 1293 CE1 TYR A 177 183.953 33.340 510.331 1.00 45.75 C ANISOU 1293 CE1 TYR A 177 5467 7163 4753 -315 -223 -103 C ATOM 1294 CE2 TYR A 177 185.948 32.230 511.044 1.00 50.50 C ANISOU 1294 CE2 TYR A 177 5964 7822 5401 -271 13 -179 C ATOM 1295 CZ TYR A 177 185.227 32.881 510.067 1.00 48.77 C ANISOU 1295 CZ TYR A 177 5858 7606 5066 -286 -66 -127 C ATOM 1296 OH TYR A 177 185.782 33.075 508.822 1.00 53.70 O ANISOU 1296 OH TYR A 177 6603 8300 5500 -263 19 -89 O ATOM 1297 N ILE A 178 185.699 32.956 516.039 1.00 35.60 N ANISOU 1297 N ILE A 178 3657 5780 4091 -369 -67 -166 N ATOM 1298 CA ILE A 178 187.108 33.121 516.372 1.00 35.82 C ANISOU 1298 CA ILE A 178 3605 5868 4138 -382 34 -141 C ATOM 1299 C ILE A 178 187.957 32.739 515.168 1.00 35.12 C ANISOU 1299 C ILE A 178 3556 5857 3932 -347 134 -136 C ATOM 1300 O ILE A 178 187.846 31.626 514.636 1.00 39.69 O ANISOU 1300 O ILE A 178 4196 6443 4442 -278 145 -205 O ATOM 1301 CB ILE A 178 187.475 32.288 517.607 1.00 35.26 C ANISOU 1301 CB ILE A 178 3446 5794 4156 -352 36 -189 C ATOM 1302 CG1 ILE A 178 186.875 32.920 518.864 1.00 35.55 C ANISOU 1302 CG1 ILE A 178 3448 5770 4290 -394 -31 -180 C ATOM 1303 CG2 ILE A 178 188.980 32.162 517.732 1.00 35.28 C ANISOU 1303 CG2 ILE A 178 3354 5881 4169 -344 132 -168 C ATOM 1304 CD1 ILE A 178 187.329 32.265 520.145 1.00 40.00 C ANISOU 1304 CD1 ILE A 178 3936 6340 4920 -370 -31 -209 C ATOM 1305 N GLN A 179 188.820 33.662 514.740 1.00 35.16 N ANISOU 1305 N GLN A 179 3532 5913 3912 -395 217 -54 N ATOM 1306 CA GLN A 179 189.540 33.478 513.484 1.00 43.16 C ANISOU 1306 CA GLN A 179 4595 7007 4796 -361 334 -30 C ATOM 1307 C GLN A 179 190.530 32.322 513.562 1.00 47.42 C ANISOU 1307 C GLN A 179 5067 7613 5336 -277 436 -83 C ATOM 1308 O GLN A 179 190.629 31.524 512.623 1.00 47.90 O ANISOU 1308 O GLN A 179 5220 7704 5274 -196 499 -131 O ATOM 1309 CB GLN A 179 190.252 34.772 513.091 1.00 40.83 C ANISOU 1309 CB GLN A 179 4270 6748 4496 -445 413 90 C ATOM 1310 CG GLN A 179 190.988 34.687 511.762 1.00 41.61 C ANISOU 1310 CG GLN A 179 4424 6938 4447 -412 559 136 C ATOM 1311 CD GLN A 179 191.291 36.053 511.176 1.00 46.21 C ANISOU 1311 CD GLN A 179 5029 7527 5002 -505 616 273 C ATOM 1312 OE1 GLN A 179 190.580 37.024 511.436 1.00 48.85 O ANISOU 1312 OE1 GLN A 179 5404 7774 5383 -574 518 320 O ATOM 1313 NE2 GLN A 179 192.351 36.134 510.380 1.00 45.96 N ANISOU 1313 NE2 GLN A 179 4972 7595 4898 -504 788 343 N ATOM 1314 N PHE A 180 191.274 32.207 514.663 1.00 48.28 N ANISOU 1314 N PHE A 180 5025 7744 5575 -286 450 -78 N ATOM 1315 CA PHE A 180 192.240 31.115 514.711 1.00 55.49 C ANISOU 1315 CA PHE A 180 5863 8722 6497 -186 548 -115 C ATOM 1316 C PHE A 180 191.590 29.758 514.959 1.00 59.79 C ANISOU 1316 C PHE A 180 6486 9198 7035 -90 491 -222 C ATOM 1317 O PHE A 180 192.306 28.751 514.988 1.00 64.72 O ANISOU 1317 O PHE A 180 7072 9851 7667 14 570 -259 O ATOM 1318 CB PHE A 180 193.320 31.389 515.762 1.00 52.49 C ANISOU 1318 CB PHE A 180 5285 8403 6256 -221 568 -64 C ATOM 1319 CG PHE A 180 192.786 31.700 517.128 1.00 51.86 C ANISOU 1319 CG PHE A 180 5167 8255 6283 -284 428 -77 C ATOM 1320 CD1 PHE A 180 192.449 30.681 518.003 1.00 51.39 C ANISOU 1320 CD1 PHE A 180 5106 8151 6268 -212 364 -141 C ATOM 1321 CD2 PHE A 180 192.645 33.012 517.547 1.00 52.51 C ANISOU 1321 CD2 PHE A 180 5227 8309 6414 -411 369 -23 C ATOM 1322 CE1 PHE A 180 191.966 30.964 519.265 1.00 51.91 C ANISOU 1322 CE1 PHE A 180 5150 8163 6412 -261 252 -149 C ATOM 1323 CE2 PHE A 180 192.163 33.303 518.808 1.00 52.84 C ANISOU 1323 CE2 PHE A 180 5255 8287 6535 -456 254 -46 C ATOM 1324 CZ PHE A 180 191.824 32.276 519.670 1.00 51.41 C ANISOU 1324 CZ PHE A 180 5071 8079 6382 -379 200 -107 C ATOM 1325 N PHE A 181 190.271 29.700 515.131 1.00 55.43 N ANISOU 1325 N PHE A 181 6033 8549 6478 -121 363 -266 N ATOM 1326 CA PHE A 181 189.544 28.438 515.180 1.00 58.99 C ANISOU 1326 CA PHE A 181 6574 8920 6919 -54 307 -362 C ATOM 1327 C PHE A 181 189.158 27.932 513.795 1.00 65.11 C ANISOU 1327 C PHE A 181 7517 9682 7539 -11 324 -425 C ATOM 1328 O PHE A 181 188.332 27.020 513.690 1.00 64.12 O ANISOU 1328 O PHE A 181 7492 9471 7398 12 247 -510 O ATOM 1329 CB PHE A 181 188.291 28.574 516.050 1.00 54.33 C ANISOU 1329 CB PHE A 181 5991 8240 6413 -115 166 -373 C ATOM 1330 CG PHE A 181 188.564 28.489 517.524 1.00 50.64 C ANISOU 1330 CG PHE A 181 5406 7761 6074 -120 146 -353 C ATOM 1331 CD1 PHE A 181 189.811 28.109 517.990 1.00 50.10 C ANISOU 1331 CD1 PHE A 181 5236 7754 6046 -64 223 -336 C ATOM 1332 CD2 PHE A 181 187.571 28.780 518.444 1.00 50.17 C ANISOU 1332 CD2 PHE A 181 5337 7637 6089 -171 51 -347 C ATOM 1333 CE1 PHE A 181 190.066 28.027 519.346 1.00 50.52 C ANISOU 1333 CE1 PHE A 181 5194 7805 6197 -66 186 -313 C ATOM 1334 CE2 PHE A 181 187.820 28.699 519.803 1.00 51.95 C ANISOU 1334 CE2 PHE A 181 5479 7856 6403 -170 35 -329 C ATOM 1335 CZ PHE A 181 189.070 28.322 520.253 1.00 50.87 C ANISOU 1335 CZ PHE A 181 5256 7782 6292 -121 92 -313 C ATOM 1336 N SER A 182 189.733 28.506 512.734 1.00 68.78 N ANISOU 1336 N SER A 182 8022 10228 7884 -7 421 -383 N ATOM 1337 CA SER A 182 189.470 28.023 511.384 1.00 69.54 C ANISOU 1337 CA SER A 182 8300 10324 7797 45 445 -446 C ATOM 1338 C SER A 182 189.957 26.595 511.182 1.00 71.74 C ANISOU 1338 C SER A 182 8641 10576 8040 169 525 -552 C ATOM 1339 O SER A 182 189.477 25.909 510.272 1.00 75.98 O ANISOU 1339 O SER A 182 9362 11068 8440 210 501 -648 O ATOM 1340 CB SER A 182 190.128 28.948 510.359 1.00 69.27 C ANISOU 1340 CB SER A 182 8293 10392 7633 33 564 -360 C ATOM 1341 OG SER A 182 189.672 30.281 510.508 1.00 69.71 O ANISOU 1341 OG SER A 182 8312 10449 7725 -78 490 -258 O ATOM 1342 N ASN A 183 190.896 26.138 512.005 1.00 68.29 N ANISOU 1342 N ASN A 183 8063 10160 7723 234 611 -539 N ATOM 1343 CA ASN A 183 191.372 24.762 511.982 1.00 65.09 C ANISOU 1343 CA ASN A 183 7706 9709 7317 370 687 -630 C ATOM 1344 C ASN A 183 190.653 23.985 513.078 1.00 57.14 C ANISOU 1344 C ASN A 183 6688 8578 6446 357 558 -677 C ATOM 1345 O ASN A 183 190.700 24.373 514.251 1.00 52.60 O ANISOU 1345 O ASN A 183 5962 8012 6011 308 507 -608 O ATOM 1346 CB ASN A 183 192.888 24.711 512.177 1.00 69.52 C ANISOU 1346 CB ASN A 183 8106 10379 7931 468 865 -569 C ATOM 1347 CG ASN A 183 193.446 23.311 512.046 1.00 72.19 C ANISOU 1347 CG ASN A 183 8499 10667 8262 640 966 -658 C ATOM 1348 OD1 ASN A 183 193.717 22.644 513.042 1.00 72.89 O ANISOU 1348 OD1 ASN A 183 8496 10710 8490 698 945 -657 O ATOM 1349 ND2 ASN A 183 193.624 22.858 510.811 1.00 77.91 N ANISOU 1349 ND2 ASN A 183 9392 11394 8815 732 1078 -734 N ATOM 1350 N ALA A 184 189.981 22.897 512.691 1.00 49.36 N ANISOU 1350 N ALA A 184 5872 7471 5410 395 506 -794 N ATOM 1351 CA ALA A 184 189.182 22.136 513.645 1.00 42.86 C ANISOU 1351 CA ALA A 184 5054 6516 4715 365 387 -829 C ATOM 1352 C ALA A 184 190.042 21.531 514.747 1.00 44.13 C ANISOU 1352 C ALA A 184 5089 6668 5012 458 454 -791 C ATOM 1353 O ALA A 184 189.590 21.413 515.892 1.00 42.89 O ANISOU 1353 O ALA A 184 4859 6456 4981 411 369 -753 O ATOM 1354 CB ALA A 184 188.397 21.042 512.919 1.00 36.27 C ANISOU 1354 CB ALA A 184 4434 5543 3803 378 323 -965 C ATOM 1355 N ALA A 185 191.274 21.129 514.423 1.00 41.73 N ANISOU 1355 N ALA A 185 4754 6420 4680 598 609 -793 N ATOM 1356 CA ALA A 185 192.150 20.559 515.441 1.00 46.00 C ANISOU 1356 CA ALA A 185 5160 6965 5353 703 662 -744 C ATOM 1357 C ALA A 185 192.533 21.589 516.497 1.00 44.68 C ANISOU 1357 C ALA A 185 4776 6912 5289 626 623 -619 C ATOM 1358 O ALA A 185 192.764 21.229 517.657 1.00 43.90 O ANISOU 1358 O ALA A 185 4582 6793 5306 656 584 -572 O ATOM 1359 CB ALA A 185 193.402 19.967 514.791 1.00 46.57 C ANISOU 1359 CB ALA A 185 5226 7088 5379 884 846 -765 C ATOM 1360 N VAL A 186 192.615 22.866 516.116 1.00 44.95 N ANISOU 1360 N VAL A 186 4746 7058 5277 525 629 -563 N ATOM 1361 CA VAL A 186 192.896 23.915 517.092 1.00 43.44 C ANISOU 1361 CA VAL A 186 4376 6952 5177 431 575 -461 C ATOM 1362 C VAL A 186 191.744 24.041 518.080 1.00 41.57 C ANISOU 1362 C VAL A 186 4169 6624 5004 334 424 -461 C ATOM 1363 O VAL A 186 191.955 24.195 519.289 1.00 40.83 O ANISOU 1363 O VAL A 186 3964 6546 5003 316 372 -407 O ATOM 1364 CB VAL A 186 193.179 25.249 516.375 1.00 46.40 C ANISOU 1364 CB VAL A 186 4704 7437 5489 337 620 -403 C ATOM 1365 CG1 VAL A 186 193.319 26.379 517.387 1.00 39.28 C ANISOU 1365 CG1 VAL A 186 3654 6589 4683 218 543 -316 C ATOM 1366 CG2 VAL A 186 194.434 25.135 515.521 1.00 32.83 C ANISOU 1366 CG2 VAL A 186 2924 5828 3722 436 797 -380 C ATOM 1367 N THR A 187 190.508 23.968 517.581 1.00 42.76 N ANISOU 1367 N THR A 187 4463 6682 5100 272 352 -520 N ATOM 1368 CA THR A 187 189.345 24.043 518.459 1.00 41.17 C ANISOU 1368 CA THR A 187 4278 6397 4966 187 228 -516 C ATOM 1369 C THR A 187 189.309 22.866 519.427 1.00 38.75 C ANISOU 1369 C THR A 187 3976 6002 4746 255 212 -526 C ATOM 1370 O THR A 187 188.943 23.026 520.598 1.00 40.34 O ANISOU 1370 O THR A 187 4121 6185 5023 213 151 -478 O ATOM 1371 CB THR A 187 188.066 24.091 517.624 1.00 40.81 C ANISOU 1371 CB THR A 187 4367 6281 4858 117 152 -573 C ATOM 1372 OG1 THR A 187 188.217 25.057 516.577 1.00 47.20 O ANISOU 1372 OG1 THR A 187 5197 7171 5564 80 179 -557 O ATOM 1373 CG2 THR A 187 186.875 24.475 518.489 1.00 32.78 C ANISOU 1373 CG2 THR A 187 3324 5209 3922 21 42 -544 C ATOM 1374 N PHE A 188 189.690 21.676 518.956 1.00 35.43 N ANISOU 1374 N PHE A 188 3635 5517 4308 366 273 -585 N ATOM 1375 CA PHE A 188 189.698 20.506 519.827 1.00 36.44 C ANISOU 1375 CA PHE A 188 3783 5541 4520 440 264 -583 C ATOM 1376 C PHE A 188 190.795 20.605 520.879 1.00 37.62 C ANISOU 1376 C PHE A 188 3778 5778 4736 513 293 -493 C ATOM 1377 O PHE A 188 190.588 20.219 522.035 1.00 32.02 O ANISOU 1377 O PHE A 188 3047 5022 4098 519 243 -445 O ATOM 1378 CB PHE A 188 189.864 19.236 518.996 1.00 40.94 C ANISOU 1378 CB PHE A 188 4500 6002 5056 550 326 -676 C ATOM 1379 CG PHE A 188 189.791 17.973 519.801 1.00 47.49 C ANISOU 1379 CG PHE A 188 5379 6689 5976 625 317 -673 C ATOM 1380 CD1 PHE A 188 188.750 17.764 520.691 1.00 48.76 C ANISOU 1380 CD1 PHE A 188 5560 6754 6212 531 224 -642 C ATOM 1381 CD2 PHE A 188 190.756 16.989 519.661 1.00 44.57 C ANISOU 1381 CD2 PHE A 188 5039 6277 5620 798 414 -692 C ATOM 1382 CE1 PHE A 188 188.677 16.602 521.434 1.00 47.09 C ANISOU 1382 CE1 PHE A 188 5404 6403 6083 594 225 -622 C ATOM 1383 CE2 PHE A 188 190.688 15.823 520.399 1.00 48.19 C ANISOU 1383 CE2 PHE A 188 5559 6587 6167 874 405 -677 C ATOM 1384 CZ PHE A 188 189.648 15.630 521.288 1.00 48.55 C ANISOU 1384 CZ PHE A 188 5633 6534 6282 765 309 -638 C ATOM 1385 N GLY A 189 191.971 21.107 520.496 1.00 36.99 N ANISOU 1385 N GLY A 189 3587 5834 4634 567 372 -463 N ATOM 1386 CA GLY A 189 193.014 21.343 521.480 1.00 40.63 C ANISOU 1386 CA GLY A 189 3875 6401 5164 613 372 -372 C ATOM 1387 C GLY A 189 192.574 22.313 522.559 1.00 41.82 C ANISOU 1387 C GLY A 189 3958 6590 5342 483 263 -315 C ATOM 1388 O GLY A 189 192.894 22.137 523.737 1.00 41.56 O ANISOU 1388 O GLY A 189 3856 6575 5361 511 211 -256 O ATOM 1389 N THR A 190 191.835 23.354 522.168 1.00 38.92 N ANISOU 1389 N THR A 190 3622 6233 4932 351 229 -332 N ATOM 1390 CA THR A 190 191.239 24.254 523.148 1.00 41.08 C ANISOU 1390 CA THR A 190 3869 6514 5226 238 136 -296 C ATOM 1391 C THR A 190 190.262 23.511 524.052 1.00 43.92 C ANISOU 1391 C THR A 190 4310 6759 5617 242 81 -298 C ATOM 1392 O THR A 190 190.243 23.727 525.270 1.00 44.19 O ANISOU 1392 O THR A 190 4306 6809 5674 224 28 -250 O ATOM 1393 CB THR A 190 190.542 25.411 522.431 1.00 47.62 C ANISOU 1393 CB THR A 190 4735 7351 6008 119 121 -314 C ATOM 1394 OG1 THR A 190 191.525 26.330 521.937 1.00 51.83 O ANISOU 1394 OG1 THR A 190 5171 7997 6524 88 166 -279 O ATOM 1395 CG2 THR A 190 189.591 26.137 523.367 1.00 50.63 C ANISOU 1395 CG2 THR A 190 5133 7695 6410 26 37 -296 C ATOM 1396 N ALA A 191 189.451 22.620 523.474 1.00 45.31 N ANISOU 1396 N ALA A 191 4606 6819 5792 261 94 -352 N ATOM 1397 CA ALA A 191 188.508 21.848 524.276 1.00 40.90 C ANISOU 1397 CA ALA A 191 4118 6142 5278 253 55 -343 C ATOM 1398 C ALA A 191 189.221 20.927 525.256 1.00 39.01 C ANISOU 1398 C ALA A 191 3857 5885 5080 362 66 -288 C ATOM 1399 O ALA A 191 188.702 20.667 526.348 1.00 37.65 O ANISOU 1399 O ALA A 191 3705 5665 4935 347 32 -238 O ATOM 1400 CB ALA A 191 187.582 21.040 523.366 1.00 41.01 C ANISOU 1400 CB ALA A 191 4259 6029 5294 236 56 -416 C ATOM 1401 N ILE A 192 190.405 20.431 524.892 1.00 41.81 N ANISOU 1401 N ILE A 192 4168 6281 5437 481 119 -286 N ATOM 1402 CA ILE A 192 191.146 19.553 525.793 1.00 41.09 C ANISOU 1402 CA ILE A 192 4047 6178 5389 605 121 -221 C ATOM 1403 C ILE A 192 191.764 20.353 526.932 1.00 42.71 C ANISOU 1403 C ILE A 192 4125 6515 5588 584 57 -140 C ATOM 1404 O ILE A 192 191.688 19.956 528.102 1.00 42.77 O ANISOU 1404 O ILE A 192 4147 6498 5606 615 10 -74 O ATOM 1405 CB ILE A 192 192.211 18.762 525.012 1.00 41.71 C ANISOU 1405 CB ILE A 192 4108 6258 5480 760 206 -243 C ATOM 1406 CG1 ILE A 192 191.548 17.809 524.016 1.00 45.21 C ANISOU 1406 CG1 ILE A 192 4721 6539 5917 786 257 -338 C ATOM 1407 CG2 ILE A 192 193.116 17.998 525.966 1.00 38.84 C ANISOU 1407 CG2 ILE A 192 3681 5907 5170 906 199 -156 C ATOM 1408 CD1 ILE A 192 192.532 17.001 523.202 1.00 46.29 C ANISOU 1408 CD1 ILE A 192 4873 6659 6054 955 361 -377 C ATOM 1409 N ALA A 193 192.375 21.496 526.615 1.00 44.11 N ANISOU 1409 N ALA A 193 4190 6829 5743 525 50 -143 N ATOM 1410 CA ALA A 193 193.085 22.269 527.628 1.00 43.81 C ANISOU 1410 CA ALA A 193 4031 6916 5701 494 -27 -80 C ATOM 1411 C ALA A 193 192.135 23.046 528.531 1.00 45.51 C ANISOU 1411 C ALA A 193 4306 7109 5876 374 -99 -76 C ATOM 1412 O ALA A 193 192.397 23.189 529.729 1.00 44.34 O ANISOU 1412 O ALA A 193 4134 7006 5706 376 -173 -25 O ATOM 1413 CB ALA A 193 194.075 23.223 526.960 1.00 48.47 C ANISOU 1413 CB ALA A 193 4476 7643 6296 453 -7 -80 C ATOM 1414 N ALA A 194 191.031 23.554 527.984 1.00 42.92 N ANISOU 1414 N ALA A 194 4060 6717 5532 278 -79 -130 N ATOM 1415 CA ALA A 194 190.157 24.447 528.733 1.00 37.36 C ANISOU 1415 CA ALA A 194 3398 6000 4795 176 -127 -130 C ATOM 1416 C ALA A 194 188.955 23.755 529.361 1.00 37.28 C ANISOU 1416 C ALA A 194 3497 5877 4789 181 -116 -117 C ATOM 1417 O ALA A 194 188.409 24.277 530.339 1.00 42.51 O ANISOU 1417 O ALA A 194 4193 6541 5418 136 -144 -97 O ATOM 1418 CB ALA A 194 189.664 25.588 527.834 1.00 36.97 C ANISOU 1418 CB ALA A 194 3353 5958 4735 71 -114 -179 C ATOM 1419 N PHE A 195 188.518 22.613 528.833 1.00 29.56 N ANISOU 1419 N PHE A 195 2581 4797 3853 230 -71 -128 N ATOM 1420 CA PHE A 195 187.359 21.928 529.395 1.00 33.17 C ANISOU 1420 CA PHE A 195 3128 5140 4335 215 -56 -104 C ATOM 1421 C PHE A 195 187.689 20.541 529.932 1.00 35.33 C ANISOU 1421 C PHE A 195 3448 5338 4636 319 -39 -48 C ATOM 1422 O PHE A 195 187.407 20.264 531.101 1.00 42.69 O ANISOU 1422 O PHE A 195 4418 6250 5551 333 -45 24 O ATOM 1423 CB PHE A 195 186.231 21.838 528.359 1.00 33.68 C ANISOU 1423 CB PHE A 195 3240 5117 4440 144 -35 -163 C ATOM 1424 CG PHE A 195 185.039 21.063 528.840 1.00 28.58 C ANISOU 1424 CG PHE A 195 2661 4352 3847 113 -16 -132 C ATOM 1425 CD1 PHE A 195 184.160 21.617 529.755 1.00 24.71 C ANISOU 1425 CD1 PHE A 195 2167 3870 3352 58 -8 -89 C ATOM 1426 CD2 PHE A 195 184.807 19.775 528.390 1.00 25.83 C ANISOU 1426 CD2 PHE A 195 2382 3877 3557 139 3 -144 C ATOM 1427 CE1 PHE A 195 183.066 20.903 530.205 1.00 29.93 C ANISOU 1427 CE1 PHE A 195 2868 4430 4073 23 27 -44 C ATOM 1428 CE2 PHE A 195 183.715 19.057 528.835 1.00 26.28 C ANISOU 1428 CE2 PHE A 195 2489 3816 3679 89 21 -106 C ATOM 1429 CZ PHE A 195 182.842 19.622 529.744 1.00 27.71 C ANISOU 1429 CZ PHE A 195 2643 4023 3864 28 38 -48 C ATOM 1430 N TYR A 196 188.290 19.663 529.126 1.00 33.36 N ANISOU 1430 N TYR A 196 4343 3561 4771 1213 -872 -584 N ATOM 1431 CA TYR A 196 188.380 18.257 529.513 1.00 36.62 C ANISOU 1431 CA TYR A 196 4628 4097 5191 954 -543 -620 C ATOM 1432 C TYR A 196 189.363 18.049 530.659 1.00 39.69 C ANISOU 1432 C TYR A 196 4805 4325 5948 867 -468 -406 C ATOM 1433 O TYR A 196 189.058 17.338 531.624 1.00 38.39 O ANISOU 1433 O TYR A 196 4453 4388 5745 775 -429 -513 O ATOM 1434 CB TYR A 196 188.751 17.399 528.304 1.00 36.39 C ANISOU 1434 CB TYR A 196 4839 3917 5069 812 -114 -489 C ATOM 1435 CG TYR A 196 187.578 17.143 527.383 1.00 42.89 C ANISOU 1435 CG TYR A 196 5778 5082 5438 855 -177 -842 C ATOM 1436 CD1 TYR A 196 186.567 16.261 527.746 1.00 40.97 C ANISOU 1436 CD1 TYR A 196 5317 5208 5040 717 -130 -1258 C ATOM 1437 CD2 TYR A 196 187.476 17.785 526.158 1.00 45.36 C ANISOU 1437 CD2 TYR A 196 6409 5355 5470 1049 -274 -780 C ATOM 1438 CE1 TYR A 196 185.489 16.025 526.914 1.00 42.72 C ANISOU 1438 CE1 TYR A 196 5564 5780 4888 757 -216 -1681 C ATOM 1439 CE2 TYR A 196 186.403 17.556 525.318 1.00 46.67 C ANISOU 1439 CE2 TYR A 196 6651 5907 5173 1139 -405 -1145 C ATOM 1440 CZ TYR A 196 185.414 16.675 525.701 1.00 45.68 C ANISOU 1440 CZ TYR A 196 6233 6175 4948 985 -395 -1635 C ATOM 1441 OH TYR A 196 184.344 16.444 524.867 1.00 46.50 O ANISOU 1441 OH TYR A 196 6338 6696 4633 1074 -551 -2094 O ATOM 1442 N LEU A 197 190.547 18.654 530.577 1.00 42.03 N ANISOU 1442 N LEU A 197 5127 4239 6603 910 -435 -118 N ATOM 1443 CA LEU A 197 191.498 18.534 531.681 1.00 46.17 C ANISOU 1443 CA LEU A 197 5395 4669 7478 880 -453 23 C ATOM 1444 C LEU A 197 190.975 19.152 532.973 1.00 41.36 C ANISOU 1444 C LEU A 197 4533 4376 6807 992 -875 -225 C ATOM 1445 O LEU A 197 191.108 18.511 534.030 1.00 30.91 O ANISOU 1445 O LEU A 197 3031 3250 5462 956 -881 -216 O ATOM 1446 CB LEU A 197 192.851 19.130 531.273 1.00 48.99 C ANISOU 1446 CB LEU A 197 5804 4680 8131 820 -300 257 C ATOM 1447 CG LEU A 197 193.611 18.363 530.190 1.00 52.14 C ANISOU 1447 CG LEU A 197 6396 4859 8557 647 151 470 C ATOM 1448 CD1 LEU A 197 194.981 18.980 529.957 1.00 55.41 C ANISOU 1448 CD1 LEU A 197 6763 5132 9159 546 259 564 C ATOM 1449 CD2 LEU A 197 193.734 16.891 530.556 1.00 51.01 C ANISOU 1449 CD2 LEU A 197 6138 4774 8468 530 404 551 C ATOM 1450 N PRO A 198 190.387 20.358 532.980 1.00 44.55 N ANISOU 1450 N PRO A 198 4963 4877 7085 1068 -1152 -428 N ATOM 1451 CA PRO A 198 189.808 20.859 534.240 1.00 45.49 C ANISOU 1451 CA PRO A 198 4942 5324 7018 1024 -1374 -690 C ATOM 1452 C PRO A 198 188.713 19.968 534.804 1.00 44.69 C ANISOU 1452 C PRO A 198 4778 5598 6603 1001 -1373 -906 C ATOM 1453 O PRO A 198 188.638 19.791 536.027 1.00 43.84 O ANISOU 1453 O PRO A 198 4582 5698 6377 942 -1373 -960 O ATOM 1454 CB PRO A 198 189.270 22.242 533.847 1.00 42.93 C ANISOU 1454 CB PRO A 198 4717 4922 6672 1094 -1551 -852 C ATOM 1455 CG PRO A 198 190.113 22.655 532.701 1.00 41.77 C ANISOU 1455 CG PRO A 198 4709 4392 6771 1151 -1418 -570 C ATOM 1456 CD PRO A 198 190.369 21.396 531.931 1.00 44.00 C ANISOU 1456 CD PRO A 198 5108 4568 7042 1154 -1167 -369 C ATOM 1457 N VAL A 199 187.854 19.405 533.950 1.00 40.23 N ANISOU 1457 N VAL A 199 4249 5149 5888 1056 -1349 -1064 N ATOM 1458 CA VAL A 199 186.800 18.517 534.436 1.00 42.14 C ANISOU 1458 CA VAL A 199 4392 5761 5857 955 -1250 -1345 C ATOM 1459 C VAL A 199 187.405 17.280 535.090 1.00 38.91 C ANISOU 1459 C VAL A 199 3975 5329 5479 803 -888 -1086 C ATOM 1460 O VAL A 199 186.916 16.801 536.121 1.00 37.22 O ANISOU 1460 O VAL A 199 3664 5377 5103 749 -826 -1207 O ATOM 1461 CB VAL A 199 185.838 18.146 533.290 1.00 39.66 C ANISOU 1461 CB VAL A 199 4199 5547 5325 917 -1140 -1579 C ATOM 1462 CG1 VAL A 199 184.959 16.970 533.683 1.00 34.86 C ANISOU 1462 CG1 VAL A 199 3494 5211 4541 715 -841 -1850 C ATOM 1463 CG2 VAL A 199 184.975 19.342 532.918 1.00 37.68 C ANISOU 1463 CG2 VAL A 199 4012 5322 4984 1097 -1380 -1759 C ATOM 1464 N ILE A 200 188.488 16.754 534.511 1.00 37.81 N ANISOU 1464 N ILE A 200 3953 4856 5556 751 -619 -710 N ATOM 1465 CA ILE A 200 189.159 15.595 535.095 1.00 35.16 C ANISOU 1465 CA ILE A 200 3608 4441 5308 665 -286 -411 C ATOM 1466 C ILE A 200 189.751 15.948 536.454 1.00 29.41 C ANISOU 1466 C ILE A 200 2713 3842 4620 808 -556 -298 C ATOM 1467 O ILE A 200 189.694 15.152 537.400 1.00 30.60 O ANISOU 1467 O ILE A 200 2851 4154 4622 806 -410 -186 O ATOM 1468 CB ILE A 200 190.233 15.058 534.131 1.00 37.66 C ANISOU 1468 CB ILE A 200 4046 4347 5916 595 41 -74 C ATOM 1469 CG1 ILE A 200 189.580 14.469 532.880 1.00 37.86 C ANISOU 1469 CG1 ILE A 200 4241 4330 5814 434 362 -230 C ATOM 1470 CG2 ILE A 200 191.105 14.016 534.816 1.00 34.83 C ANISOU 1470 CG2 ILE A 200 3639 3859 5738 585 311 280 C ATOM 1471 CD1 ILE A 200 190.574 14.001 531.841 1.00 35.02 C ANISOU 1471 CD1 ILE A 200 4016 3578 5710 344 715 42 C ATOM 1472 N ILE A 201 190.325 17.146 536.575 1.00 29.68 N ANISOU 1472 N ILE A 201 2624 3807 4847 945 -937 -339 N ATOM 1473 CA ILE A 201 190.919 17.555 537.844 1.00 40.55 C ANISOU 1473 CA ILE A 201 3864 5351 6191 1025 -1168 -299 C ATOM 1474 C ILE A 201 189.845 17.697 538.917 1.00 41.40 C ANISOU 1474 C ILE A 201 3956 5864 5910 1011 -1292 -576 C ATOM 1475 O ILE A 201 190.009 17.219 540.046 1.00 37.32 O ANISOU 1475 O ILE A 201 3366 5595 5219 1099 -1340 -496 O ATOM 1476 CB ILE A 201 191.719 18.858 537.662 1.00 38.68 C ANISOU 1476 CB ILE A 201 3663 4914 6119 970 -1270 -325 C ATOM 1477 CG1 ILE A 201 192.877 18.634 536.690 1.00 39.30 C ANISOU 1477 CG1 ILE A 201 3764 4591 6575 954 -1088 -79 C ATOM 1478 CG2 ILE A 201 192.236 19.360 539.002 1.00 39.32 C ANISOU 1478 CG2 ILE A 201 3636 5201 6104 990 -1429 -375 C ATOM 1479 CD1 ILE A 201 193.659 19.888 536.365 1.00 43.71 C ANISOU 1479 CD1 ILE A 201 4314 4905 7390 899 -1161 -160 C ATOM 1480 N MET A 202 188.725 18.340 538.580 1.00 43.24 N ANISOU 1480 N MET A 202 4280 6153 5996 929 -1320 -895 N ATOM 1481 CA MET A 202 187.656 18.522 539.557 1.00 48.73 C ANISOU 1481 CA MET A 202 4977 7143 6395 902 -1338 -1179 C ATOM 1482 C MET A 202 187.005 17.198 539.937 1.00 48.41 C ANISOU 1482 C MET A 202 4808 7471 6114 912 -1199 -1285 C ATOM 1483 O MET A 202 186.547 17.040 541.075 1.00 50.11 O ANISOU 1483 O MET A 202 4979 8014 6046 925 -1199 -1416 O ATOM 1484 CB MET A 202 186.612 19.496 539.012 1.00 44.45 C ANISOU 1484 CB MET A 202 4534 6506 5847 878 -1327 -1448 C ATOM 1485 CG MET A 202 187.173 20.871 538.700 1.00 44.05 C ANISOU 1485 CG MET A 202 4549 6179 6009 915 -1445 -1403 C ATOM 1486 SD MET A 202 185.946 22.015 538.046 0.52 46.92 S ANISOU 1486 SD MET A 202 4986 6444 6396 1005 -1468 -1668 S ATOM 1487 CE MET A 202 185.320 21.088 536.652 1.00 26.75 C ANISOU 1487 CE MET A 202 2487 3918 3761 1017 -1392 -1692 C ATOM 1488 N THR A 203 186.956 16.242 539.007 1.00 39.32 N ANISOU 1488 N THR A 203 3769 6129 5041 798 -836 -1137 N ATOM 1489 CA THR A 203 186.410 14.925 539.319 1.00 42.11 C ANISOU 1489 CA THR A 203 4240 6544 5214 643 -332 -1075 C ATOM 1490 C THR A 203 187.293 14.189 540.319 1.00 38.96 C ANISOU 1490 C THR A 203 3929 6136 4739 744 -180 -615 C ATOM 1491 O THR A 203 186.800 13.625 541.303 1.00 38.65 O ANISOU 1491 O THR A 203 3967 6309 4409 727 44 -602 O ATOM 1492 CB THR A 203 186.252 14.107 538.035 1.00 43.59 C ANISOU 1492 CB THR A 203 4534 6465 5563 470 66 -1047 C ATOM 1493 OG1 THR A 203 185.237 14.696 537.213 1.00 40.76 O ANISOU 1493 OG1 THR A 203 4100 6221 5166 419 -97 -1521 O ATOM 1494 CG2 THR A 203 185.872 12.668 538.356 1.00 44.84 C ANISOU 1494 CG2 THR A 203 4801 6581 5657 293 679 -949 C ATOM 1495 N VAL A 204 188.607 14.186 540.081 1.00 34.70 N ANISOU 1495 N VAL A 204 3382 5348 4454 872 -286 -231 N ATOM 1496 CA VAL A 204 189.531 13.543 541.012 1.00 38.02 C ANISOU 1496 CA VAL A 204 3850 5782 4815 1049 -237 211 C ATOM 1497 C VAL A 204 189.521 14.265 542.351 1.00 40.96 C ANISOU 1497 C VAL A 204 4117 6583 4862 1239 -664 77 C ATOM 1498 O VAL A 204 189.540 13.632 543.415 1.00 37.95 O ANISOU 1498 O VAL A 204 3860 6414 4145 1361 -544 304 O ATOM 1499 CB VAL A 204 190.946 13.489 540.408 1.00 37.23 C ANISOU 1499 CB VAL A 204 3681 5327 5137 1150 -302 553 C ATOM 1500 CG1 VAL A 204 191.912 12.824 541.375 1.00 37.71 C ANISOU 1500 CG1 VAL A 204 3749 5429 5149 1398 -319 995 C ATOM 1501 CG2 VAL A 204 190.926 12.755 539.079 1.00 37.15 C ANISOU 1501 CG2 VAL A 204 3791 4919 5407 942 161 646 C ATOM 1502 N LEU A 205 189.485 15.600 542.323 1.00 37.85 N ANISOU 1502 N LEU A 205 3511 6317 4552 1276 -1143 -296 N ATOM 1503 CA LEU A 205 189.445 16.364 543.565 1.00 41.16 C ANISOU 1503 CA LEU A 205 3806 7141 4692 1412 -1534 -524 C ATOM 1504 C LEU A 205 188.194 16.034 544.367 1.00 40.56 C ANISOU 1504 C LEU A 205 3845 7433 4133 1339 -1332 -744 C ATOM 1505 O LEU A 205 188.273 15.749 545.567 1.00 40.96 O ANISOU 1505 O LEU A 205 3976 7814 3772 1479 -1354 -631 O ATOM 1506 CB LEU A 205 189.526 17.862 543.269 1.00 41.44 C ANISOU 1506 CB LEU A 205 3862 6841 5040 1188 -1654 -782 C ATOM 1507 CG LEU A 205 190.920 18.392 542.920 1.00 43.50 C ANISOU 1507 CG LEU A 205 4061 6789 5680 1167 -1743 -565 C ATOM 1508 CD1 LEU A 205 190.864 19.865 542.556 1.00 41.28 C ANISOU 1508 CD1 LEU A 205 3800 6296 5588 1040 -1769 -810 C ATOM 1509 CD2 LEU A 205 191.889 18.161 544.071 1.00 39.21 C ANISOU 1509 CD2 LEU A 205 3425 6433 5039 1310 -1919 -396 C ATOM 1510 N TYR A 206 187.025 16.051 543.718 1.00 42.75 N ANISOU 1510 N TYR A 206 4145 7649 4449 1117 -1102 -1070 N ATOM 1511 CA TYR A 206 185.802 15.679 544.421 1.00 45.08 C ANISOU 1511 CA TYR A 206 4529 8223 4374 989 -804 -1329 C ATOM 1512 C TYR A 206 185.856 14.239 544.912 1.00 45.28 C ANISOU 1512 C TYR A 206 4847 8194 4162 970 -238 -882 C ATOM 1513 O TYR A 206 185.301 13.924 545.971 1.00 43.49 O ANISOU 1513 O TYR A 206 4757 8248 3520 969 -21 -917 O ATOM 1514 CB TYR A 206 184.574 15.876 543.529 1.00 40.35 C ANISOU 1514 CB TYR A 206 3841 7552 3938 767 -662 -1802 C ATOM 1515 CG TYR A 206 183.303 15.444 544.225 1.00 38.04 C ANISOU 1515 CG TYR A 206 3589 7509 3354 597 -286 -2134 C ATOM 1516 CD1 TYR A 206 182.683 16.272 545.150 1.00 39.72 C ANISOU 1516 CD1 TYR A 206 3665 8010 3416 614 -497 -2479 C ATOM 1517 CD2 TYR A 206 182.746 14.194 543.987 1.00 39.09 C ANISOU 1517 CD2 TYR A 206 3883 7486 3484 393 363 -2051 C ATOM 1518 CE1 TYR A 206 181.533 15.875 545.807 1.00 49.58 C ANISOU 1518 CE1 TYR A 206 4946 9362 4532 419 -116 -2681 C ATOM 1519 CE2 TYR A 206 181.596 13.788 544.640 1.00 42.72 C ANISOU 1519 CE2 TYR A 206 4368 8122 3742 207 787 -2377 C ATOM 1520 CZ TYR A 206 180.994 14.634 545.548 1.00 48.38 C ANISOU 1520 CZ TYR A 206 4975 9057 4352 210 497 -2628 C ATOM 1521 OH TYR A 206 179.849 14.239 546.201 1.00 57.02 O ANISOU 1521 OH TYR A 206 6123 10123 5417 -6 869 -2782 O ATOM 1522 N TRP A 207 186.506 13.352 544.153 1.00 43.04 N ANISOU 1522 N TRP A 207 4681 7524 4147 955 55 -457 N ATOM 1523 CA TRP A 207 186.641 11.965 544.586 1.00 45.15 C ANISOU 1523 CA TRP A 207 5233 7651 4270 968 629 22 C ATOM 1524 C TRP A 207 187.371 11.878 545.920 1.00 52.95 C ANISOU 1524 C TRP A 207 6353 8919 4848 1292 431 410 C ATOM 1525 O TRP A 207 186.974 11.112 546.806 1.00 50.28 O ANISOU 1525 O TRP A 207 6288 8695 4122 1329 843 633 O ATOM 1526 CB TRP A 207 187.374 11.156 543.516 1.00 44.81 C ANISOU 1526 CB TRP A 207 5239 7125 4662 925 911 387 C ATOM 1527 CG TRP A 207 187.227 9.676 543.660 1.00 46.59 C ANISOU 1527 CG TRP A 207 5732 7085 4885 851 1647 768 C ATOM 1528 CD1 TRP A 207 186.445 9.008 544.557 1.00 50.95 C ANISOU 1528 CD1 TRP A 207 6508 7749 5103 796 2131 815 C ATOM 1529 CD2 TRP A 207 187.879 8.675 542.873 1.00 49.21 C ANISOU 1529 CD2 TRP A 207 6142 6944 5610 813 2052 1147 C ATOM 1530 NE1 TRP A 207 186.572 7.651 544.378 1.00 56.03 N ANISOU 1530 NE1 TRP A 207 7372 7984 5934 734 2829 1225 N ATOM 1531 CE2 TRP A 207 187.447 7.421 543.350 1.00 55.01 C ANISOU 1531 CE2 TRP A 207 7141 7498 6262 745 2778 1418 C ATOM 1532 CE3 TRP A 207 188.787 8.716 541.811 1.00 47.13 C ANISOU 1532 CE3 TRP A 207 5756 6366 5785 819 1922 1271 C ATOM 1533 CZ2 TRP A 207 187.893 6.221 542.801 1.00 58.04 C ANISOU 1533 CZ2 TRP A 207 7642 7385 7025 688 3333 1784 C ATOM 1534 CZ3 TRP A 207 189.228 7.525 541.268 1.00 48.97 C ANISOU 1534 CZ3 TRP A 207 6101 6149 6357 756 2477 1621 C ATOM 1535 CH2 TRP A 207 188.781 6.296 541.762 1.00 52.15 C ANISOU 1535 CH2 TRP A 207 6742 6370 6704 696 3173 1872 C ATOM 1536 N HIS A 208 188.437 12.663 546.085 1.00 46.01 N ANISOU 1536 N HIS A 208 5282 8160 4039 1540 -187 476 N ATOM 1537 CA HIS A 208 189.128 12.705 547.369 1.00 52.84 C ANISOU 1537 CA HIS A 208 6210 9396 4469 1887 -498 738 C ATOM 1538 C HIS A 208 188.291 13.405 548.433 1.00 52.62 C ANISOU 1538 C HIS A 208 6180 9894 3918 1879 -674 312 C ATOM 1539 O HIS A 208 188.406 13.080 549.620 1.00 57.52 O ANISOU 1539 O HIS A 208 7012 10867 3977 2110 -670 546 O ATOM 1540 CB HIS A 208 190.481 13.397 547.215 1.00 49.90 C ANISOU 1540 CB HIS A 208 5542 9019 4398 2125 -1115 792 C ATOM 1541 CG HIS A 208 191.400 12.713 546.252 1.00 60.39 C ANISOU 1541 CG HIS A 208 6858 9841 6246 2148 -930 1203 C ATOM 1542 ND1 HIS A 208 191.826 11.414 546.426 1.00 51.29 N ANISOU 1542 ND1 HIS A 208 5958 8481 5049 2304 -526 1802 N ATOM 1543 CD2 HIS A 208 191.974 13.146 545.104 1.00 44.83 C ANISOU 1543 CD2 HIS A 208 4664 7508 4861 2035 -1050 1101 C ATOM 1544 CE1 HIS A 208 192.620 11.076 545.426 1.00 49.32 C ANISOU 1544 CE1 HIS A 208 5603 7773 5364 2272 -422 2008 C ATOM 1545 NE2 HIS A 208 192.727 12.109 544.611 1.00 52.62 N ANISOU 1545 NE2 HIS A 208 5746 8101 6147 2101 -725 1591 N ATOM 1546 N ILE A 209 187.450 14.361 548.031 1.00 53.01 N ANISOU 1546 N ILE A 209 6006 10007 4127 1639 -825 -306 N ATOM 1547 CA ILE A 209 186.571 15.039 548.983 1.00 60.29 C ANISOU 1547 CA ILE A 209 6889 11393 4623 1593 -940 -786 C ATOM 1548 C ILE A 209 185.582 14.050 549.588 1.00 63.60 C ANISOU 1548 C ILE A 209 7658 11885 4624 1462 -258 -674 C ATOM 1549 O ILE A 209 185.496 13.896 550.812 1.00 59.72 O ANISOU 1549 O ILE A 209 7377 11780 3535 1612 -201 -573 O ATOM 1550 CB ILE A 209 185.839 16.212 548.307 1.00 61.92 C ANISOU 1550 CB ILE A 209 6770 11568 5189 1381 -1201 -1455 C ATOM 1551 CG1 ILE A 209 186.836 17.266 547.835 1.00 59.22 C ANISOU 1551 CG1 ILE A 209 6218 10804 5478 1415 -1585 -1440 C ATOM 1552 CG2 ILE A 209 184.841 16.837 549.268 1.00 67.04 C ANISOU 1552 CG2 ILE A 209 7372 12427 5672 1257 -1137 -1879 C ATOM 1553 CD1 ILE A 209 187.703 17.786 548.933 1.00 62.02 C ANISOU 1553 CD1 ILE A 209 6558 11258 5749 1559 -1839 -1367 C ATOM 1554 N SER A 210 184.813 13.370 548.733 1.00 64.57 N ANISOU 1554 N SER A 210 7845 11637 5052 1174 297 -723 N ATOM 1555 CA SER A 210 183.801 12.442 549.226 1.00 68.82 C ANISOU 1555 CA SER A 210 8667 12166 5315 986 1043 -705 C ATOM 1556 C SER A 210 184.424 11.242 549.929 1.00 69.36 C ANISOU 1556 C SER A 210 9168 12147 5037 1210 1463 57 C ATOM 1557 O SER A 210 183.788 10.645 550.803 1.00 65.58 O ANISOU 1557 O SER A 210 9007 11785 4126 1171 2007 163 O ATOM 1558 CB SER A 210 182.906 11.980 548.078 1.00 53.36 C ANISOU 1558 CB SER A 210 6605 9827 3844 627 1519 -1006 C ATOM 1559 OG SER A 210 183.656 11.315 547.079 1.00 52.87 O ANISOU 1559 OG SER A 210 6573 9327 4187 644 1631 -602 O ATOM 1560 N ARG A 211 185.654 10.873 549.565 1.00 70.53 N ANISOU 1560 N ARG A 211 9346 12069 5383 1460 1253 599 N ATOM 1561 CA ARG A 211 186.345 9.806 550.280 1.00 76.37 C ANISOU 1561 CA ARG A 211 10482 12741 5793 1770 1553 1363 C ATOM 1562 C ARG A 211 186.877 10.280 551.626 1.00 84.58 C ANISOU 1562 C ARG A 211 11635 14362 6139 2170 1057 1516 C ATOM 1563 O ARG A 211 187.015 9.473 552.552 1.00 89.87 O ANISOU 1563 O ARG A 211 12734 15132 6281 2430 1387 2062 O ATOM 1564 CB ARG A 211 187.484 9.237 549.427 1.00 79.73 C ANISOU 1564 CB ARG A 211 10853 12722 6719 1918 1493 1850 C ATOM 1565 CG ARG A 211 187.018 8.265 548.350 1.00 83.43 C ANISOU 1565 CG ARG A 211 11380 12599 7722 1585 2221 1902 C ATOM 1566 CD ARG A 211 188.164 7.431 547.795 1.00 90.59 C ANISOU 1566 CD ARG A 211 12339 13059 9022 1780 2326 2508 C ATOM 1567 NE ARG A 211 188.668 7.942 546.523 1.00 91.79 N ANISOU 1567 NE ARG A 211 12133 12981 9761 1644 1981 2253 N ATOM 1568 CZ ARG A 211 189.778 8.660 546.390 1.00 93.70 C ANISOU 1568 CZ ARG A 211 12133 13322 10147 1886 1302 2310 C ATOM 1569 NH1 ARG A 211 190.511 8.957 547.454 1.00 99.50 N ANISOU 1569 NH1 ARG A 211 12889 14427 10489 2290 824 2561 N ATOM 1570 NH2 ARG A 211 190.158 9.079 545.189 1.00 87.52 N ANISOU 1570 NH2 ARG A 211 11082 12274 9896 1727 1119 2091 N ATOM 1571 N ALA A 212 187.175 11.576 551.756 1.00 85.65 N ANISOU 1571 N ALA A 212 11404 14885 6256 2238 286 1035 N ATOM 1572 CA ALA A 212 187.582 12.111 553.052 1.00 92.34 C ANISOU 1572 CA ALA A 212 12300 16360 6423 2582 -207 1021 C ATOM 1573 C ALA A 212 186.395 12.214 554.001 1.00 98.92 C ANISOU 1573 C ALA A 212 13345 17446 6793 2374 156 692 C ATOM 1574 O ALA A 212 186.507 11.879 555.186 1.00104.17 O ANISOU 1574 O ALA A 212 14317 18297 6968 2554 215 962 O ATOM 1575 CB ALA A 212 188.248 13.474 552.873 1.00 88.70 C ANISOU 1575 CB ALA A 212 11310 16031 6361 2597 -1041 501 C ATOM 1576 N SER A 213 185.249 12.678 553.499 1.00100.99 N ANISOU 1576 N SER A 213 13426 17659 7285 1974 395 79 N ATOM 1577 CA SER A 213 184.043 12.733 554.316 1.00109.72 C ANISOU 1577 CA SER A 213 14696 18856 8137 1701 807 -270 C ATOM 1578 C SER A 213 183.519 11.346 554.662 1.00113.60 C ANISOU 1578 C SER A 213 15711 19040 8414 1600 1713 217 C ATOM 1579 O SER A 213 182.797 11.199 555.654 1.00121.99 O ANISOU 1579 O SER A 213 17052 20185 9111 1463 2067 126 O ATOM 1580 CB SER A 213 182.956 13.535 553.597 1.00110.95 C ANISOU 1580 CB SER A 213 14464 18884 8808 1293 812 -1048 C ATOM 1581 OG SER A 213 183.403 14.846 553.297 1.00111.53 O ANISOU 1581 OG SER A 213 14068 19071 9235 1350 34 -1456 O ATOM 1582 N LYS A 214 183.862 10.334 553.871 1.00167.03 N ANISOU 1582 N LYS A 214 17272 31759 14431 4315 2843 1952 N ATOM 1583 CA LYS A 214 183.440 8.964 554.133 1.00160.03 C ANISOU 1583 CA LYS A 214 17010 30402 13393 5016 2919 2173 C ATOM 1584 C LYS A 214 184.449 8.240 555.018 1.00167.94 C ANISOU 1584 C LYS A 214 17539 31988 14284 5976 2906 2136 C ATOM 1585 O LYS A 214 184.146 7.879 556.155 1.00165.10 O ANISOU 1585 O LYS A 214 17246 31610 13874 6426 2632 2284 O ATOM 1586 CB LYS A 214 183.252 8.205 552.818 1.00171.71 C ANISOU 1586 CB LYS A 214 19151 31331 14762 4959 3343 2212 C ATOM 1587 CG LYS A 214 183.154 6.698 552.972 1.00147.81 C ANISOU 1587 CG LYS A 214 16703 27921 11535 5771 3540 2380 C ATOM 1588 CD LYS A 214 183.087 6.018 551.615 1.00150.33 C ANISOU 1588 CD LYS A 214 17634 27752 11732 5662 4001 2379 C ATOM 1589 CE LYS A 214 183.176 4.507 551.749 1.00153.55 C ANISOU 1589 CE LYS A 214 18586 27832 11922 6523 4263 2513 C ATOM 1590 NZ LYS A 214 182.075 3.957 552.585 1.00150.03 N ANISOU 1590 NZ LYS A 214 18763 26838 11402 6695 4023 2766 N ATOM 1591 N ALA A1001 184.246 12.782 563.739 1.00155.93 N ANISOU 1591 N ALA A1001 13082 33149 13016 5614 159 2017 N ATOM 1592 CA ALA A1001 183.856 11.817 562.718 1.00155.86 C ANISOU 1592 CA ALA A1001 13739 32499 12982 5847 476 2162 C ATOM 1593 C ALA A1001 182.428 11.335 562.947 1.00152.27 C ANISOU 1593 C ALA A1001 14184 31132 12542 5798 406 2434 C ATOM 1594 O ALA A1001 181.479 11.902 562.408 1.00148.72 O ANISOU 1594 O ALA A1001 14119 30137 12252 5108 433 2475 O ATOM 1595 CB ALA A1001 184.818 10.640 562.704 1.00159.51 C ANISOU 1595 CB ALA A1001 14052 33307 13248 6799 632 2179 C ATOM 1596 N ASP A1002 182.287 10.283 563.756 1.00155.50 N ANISOU 1596 N ASP A1002 14925 31389 12770 6540 316 2617 N ATOM 1597 CA ASP A1002 180.963 9.741 564.044 1.00154.66 C ANISOU 1597 CA ASP A1002 15675 30443 12647 6520 269 2858 C ATOM 1598 C ASP A1002 180.137 10.705 564.887 1.00151.98 C ANISOU 1598 C ASP A1002 15309 29990 12446 5949 -42 2869 C ATOM 1599 O ASP A1002 178.916 10.801 564.710 1.00148.27 O ANISOU 1599 O ASP A1002 15423 28827 12085 5515 -43 2991 O ATOM 1600 CB ASP A1002 181.091 8.391 564.750 1.00162.13 C ANISOU 1600 CB ASP A1002 16993 31276 13334 7461 268 3038 C ATOM 1601 CG ASP A1002 179.774 7.906 565.322 1.00160.94 C ANISOU 1601 CG ASP A1002 17654 30355 13138 7429 179 3260 C ATOM 1602 OD1 ASP A1002 178.935 7.405 564.545 1.00159.24 O ANISOU 1602 OD1 ASP A1002 18139 29426 12939 7233 404 3370 O ATOM 1603 OD2 ASP A1002 179.576 8.032 566.548 1.00161.68 O ANISOU 1603 OD2 ASP A1002 17687 30573 13171 7571 -110 3313 O ATOM 1604 N LEU A1003 180.783 11.419 565.814 1.00153.14 N ANISOU 1604 N LEU A1003 14778 30823 12586 5941 -302 2734 N ATOM 1605 CA LEU A1003 180.058 12.334 566.692 1.00147.66 C ANISOU 1605 CA LEU A1003 14054 30041 12008 5427 -579 2731 C ATOM 1606 C LEU A1003 179.332 13.411 565.896 1.00141.78 C ANISOU 1606 C LEU A1003 13403 28940 11527 4509 -510 2667 C ATOM 1607 O LEU A1003 178.173 13.732 566.185 1.00136.59 O ANISOU 1607 O LEU A1003 13170 27736 10993 4119 -612 2774 O ATOM 1608 CB LEU A1003 181.021 12.967 567.697 1.00149.26 C ANISOU 1608 CB LEU A1003 13464 31114 12135 5523 -837 2561 C ATOM 1609 CG LEU A1003 181.676 12.011 568.696 1.00151.35 C ANISOU 1609 CG LEU A1003 13611 31771 12122 6432 -992 2644 C ATOM 1610 CD1 LEU A1003 182.717 12.735 569.536 1.00154.13 C ANISOU 1610 CD1 LEU A1003 13182 32916 12465 6354 -1164 2396 C ATOM 1611 CD2 LEU A1003 180.623 11.367 569.579 1.00147.91 C ANISOU 1611 CD2 LEU A1003 13921 30631 11645 6625 -1083 2848 C ATOM 1612 N GLU A1004 179.999 13.984 564.891 1.00143.29 N ANISOU 1612 N GLU A1004 13207 29434 11801 4163 -332 2492 N ATOM 1613 CA GLU A1004 179.357 14.996 564.059 1.00139.55 C ANISOU 1613 CA GLU A1004 12858 28611 11552 3318 -257 2444 C ATOM 1614 C GLU A1004 178.192 14.404 563.277 1.00133.88 C ANISOU 1614 C GLU A1004 12952 27024 10891 3204 -113 2652 C ATOM 1615 O GLU A1004 177.178 15.075 563.054 1.00126.53 O ANISOU 1615 O GLU A1004 12315 25620 10139 2611 -170 2712 O ATOM 1616 CB GLU A1004 180.383 15.618 563.110 1.00145.51 C ANISOU 1616 CB GLU A1004 13080 29869 12340 3012 -62 2212 C ATOM 1617 CG GLU A1004 181.779 15.749 563.705 1.00152.66 C ANISOU 1617 CG GLU A1004 13167 31723 13115 3346 -129 2000 C ATOM 1618 CD GLU A1004 181.829 16.691 564.892 1.00153.00 C ANISOU 1618 CD GLU A1004 12788 32163 13183 3067 -427 1897 C ATOM 1619 OE1 GLU A1004 181.232 17.786 564.811 1.00150.24 O ANISOU 1619 OE1 GLU A1004 12501 31582 13003 2334 -474 1849 O ATOM 1620 OE2 GLU A1004 182.463 16.336 565.907 1.00156.42 O ANISOU 1620 OE2 GLU A1004 12845 33133 13453 3588 -613 1869 O ATOM 1621 N ASP A1005 178.318 13.143 562.856 1.00137.19 N ANISOU 1621 N ASP A1005 13744 27231 11152 3772 79 2762 N ATOM 1622 CA ASP A1005 177.251 12.473 562.122 1.00134.32 C ANISOU 1622 CA ASP A1005 14169 26068 10798 3676 231 2948 C ATOM 1623 C ASP A1005 176.021 12.215 562.984 1.00130.75 C ANISOU 1623 C ASP A1005 14225 25085 10368 3674 44 3129 C ATOM 1624 O ASP A1005 174.920 12.071 562.442 1.00127.42 O ANISOU 1624 O ASP A1005 14375 24018 10022 3341 103 3255 O ATOM 1625 CB ASP A1005 177.773 11.156 561.542 1.00135.83 C ANISOU 1625 CB ASP A1005 14642 26186 10781 4312 510 3003 C ATOM 1626 CG ASP A1005 178.791 11.369 560.437 1.00137.62 C ANISOU 1626 CG ASP A1005 14490 26793 11008 4217 764 2830 C ATOM 1627 OD1 ASP A1005 178.826 10.552 559.493 1.00138.81 O ANISOU 1627 OD1 ASP A1005 15046 26635 11061 4395 1056 2880 O ATOM 1628 OD2 ASP A1005 179.543 12.365 560.501 1.00138.46 O ANISOU 1628 OD2 ASP A1005 13911 27495 11204 3927 692 2631 O ATOM 1629 N ASN A1006 176.182 12.149 564.306 1.00132.60 N ANISOU 1629 N ASN A1006 14264 25593 10527 4025 -177 3138 N ATOM 1630 CA ASN A1006 175.057 11.992 565.221 1.00130.04 C ANISOU 1630 CA ASN A1006 14378 24809 10222 3989 -349 3281 C ATOM 1631 C ASN A1006 174.430 13.334 565.586 1.00125.57 C ANISOU 1631 C ASN A1006 13589 24220 9903 3291 -549 3217 C ATOM 1632 O ASN A1006 173.203 13.476 565.563 1.00118.60 O ANISOU 1632 O ASN A1006 13147 22763 9154 2927 -585 3324 O ATOM 1633 CB ASN A1006 175.505 11.265 566.494 1.00132.99 C ANISOU 1633 CB ASN A1006 14707 25454 10369 4699 -486 3329 C ATOM 1634 CG ASN A1006 175.872 9.818 566.243 1.00137.65 C ANISOU 1634 CG ASN A1006 15699 25899 10704 5439 -280 3442 C ATOM 1635 OD1 ASN A1006 177.040 9.439 566.330 1.00142.79 O ANISOU 1635 OD1 ASN A1006 15967 27088 11201 5995 -244 3380 O ATOM 1636 ND2 ASN A1006 174.873 8.996 565.943 1.00136.01 N ANISOU 1636 ND2 ASN A1006 16269 24967 10443 5454 -135 3604 N ATOM 1637 N TRP A1007 175.260 14.323 565.931 1.00129.22 N ANISOU 1637 N TRP A1007 13369 25309 10421 3101 -668 3035 N ATOM 1638 CA TRP A1007 174.743 15.624 566.345 1.00127.51 C ANISOU 1638 CA TRP A1007 12947 25082 10418 2461 -835 2962 C ATOM 1639 C TRP A1007 174.063 16.346 565.188 1.00127.53 C ANISOU 1639 C TRP A1007 13139 24673 10644 1795 -725 2973 C ATOM 1640 O TRP A1007 173.048 17.024 565.386 1.00126.07 O ANISOU 1640 O TRP A1007 13146 24105 10650 1341 -826 3025 O ATOM 1641 CB TRP A1007 175.873 16.473 566.927 1.00128.11 C ANISOU 1641 CB TRP A1007 12267 25949 10462 2394 -954 2746 C ATOM 1642 CG TRP A1007 175.408 17.737 567.582 1.00125.56 C ANISOU 1642 CG TRP A1007 11759 25635 10312 1812 -1121 2665 C ATOM 1643 CD1 TRP A1007 175.655 19.013 567.170 1.00126.17 C ANISOU 1643 CD1 TRP A1007 11477 25919 10541 1183 -1095 2501 C ATOM 1644 CD2 TRP A1007 174.607 17.845 568.767 1.00123.14 C ANISOU 1644 CD2 TRP A1007 11658 25094 10035 1797 -1308 2738 C ATOM 1645 NE1 TRP A1007 175.063 19.910 568.026 1.00125.48 N ANISOU 1645 NE1 TRP A1007 11364 25733 10579 795 -1252 2471 N ATOM 1646 CE2 TRP A1007 174.413 19.219 569.014 1.00123.13 C ANISOU 1646 CE2 TRP A1007 11395 25173 10216 1159 -1384 2611 C ATOM 1647 CE3 TRP A1007 174.038 16.915 569.642 1.00121.46 C ANISOU 1647 CE3 TRP A1007 11855 24595 9700 2250 -1398 2892 C ATOM 1648 CZ2 TRP A1007 173.673 19.684 570.100 1.00120.55 C ANISOU 1648 CZ2 TRP A1007 11183 24657 9966 973 -1540 2630 C ATOM 1649 CZ3 TRP A1007 173.304 17.379 570.720 1.00120.14 C ANISOU 1649 CZ3 TRP A1007 11800 24227 9620 2039 -1549 2898 C ATOM 1650 CH2 TRP A1007 173.128 18.751 570.939 1.00119.72 C ANISOU 1650 CH2 TRP A1007 11454 24290 9745 1417 -1626 2775 C ATOM 1651 N GLU A1008 174.610 16.220 563.976 1.00129.14 N ANISOU 1651 N GLU A1008 13296 24951 10821 1739 -517 2925 N ATOM 1652 CA GLU A1008 173.967 16.817 562.808 1.00126.17 C ANISOU 1652 CA GLU A1008 13160 24161 10616 1137 -416 2956 C ATOM 1653 C GLU A1008 172.605 16.186 562.550 1.00121.22 C ANISOU 1653 C GLU A1008 13233 22787 10037 1095 -411 3172 C ATOM 1654 O GLU A1008 171.642 16.885 562.212 1.00119.12 O ANISOU 1654 O GLU A1008 13168 22126 9965 573 -475 3235 O ATOM 1655 CB GLU A1008 174.871 16.673 561.583 1.00133.29 C ANISOU 1655 CB GLU A1008 13915 25292 11437 1126 -173 2860 C ATOM 1656 CG GLU A1008 174.273 17.207 560.292 1.00133.50 C ANISOU 1656 CG GLU A1008 14236 24895 11592 530 -61 2903 C ATOM 1657 CD GLU A1008 175.174 16.967 559.097 1.00139.31 C ANISOU 1657 CD GLU A1008 14877 25837 12218 537 208 2803 C ATOM 1658 OE1 GLU A1008 176.202 16.276 559.259 1.00144.43 O ANISOU 1658 OE1 GLU A1008 15252 26923 12701 1059 323 2713 O ATOM 1659 OE2 GLU A1008 174.857 17.467 557.997 1.00139.75 O ANISOU 1659 OE2 GLU A1008 15133 25619 12347 32 308 2816 O ATOM 1660 N THR A1009 172.506 14.863 562.704 1.00119.62 N ANISOU 1660 N THR A1009 13412 22389 9649 1643 -329 3285 N ATOM 1661 CA THR A1009 171.224 14.184 562.539 1.00113.92 C ANISOU 1661 CA THR A1009 13360 20985 8938 1599 -309 3469 C ATOM 1662 C THR A1009 170.207 14.665 563.568 1.00109.48 C ANISOU 1662 C THR A1009 12882 20187 8530 1388 -528 3524 C ATOM 1663 O THR A1009 169.019 14.819 563.255 1.00110.20 O ANISOU 1663 O THR A1009 13335 19774 8763 1016 -560 3628 O ATOM 1664 CB THR A1009 171.419 12.670 562.644 1.00117.49 C ANISOU 1664 CB THR A1009 14215 21301 9126 2251 -156 3558 C ATOM 1665 OG1 THR A1009 172.336 12.231 561.633 1.00123.11 O ANISOU 1665 OG1 THR A1009 14865 22204 9708 2441 80 3502 O ATOM 1666 CG2 THR A1009 170.096 11.942 562.466 1.00114.51 C ANISOU 1666 CG2 THR A1009 14550 20227 8730 2155 -110 3726 C ATOM 1667 N LEU A1010 170.655 14.911 564.802 1.00108.30 N ANISOU 1667 N LEU A1010 12388 20413 8347 1617 -678 3450 N ATOM 1668 CA LEU A1010 169.746 15.354 565.855 1.00106.11 C ANISOU 1668 CA LEU A1010 12188 19926 8201 1433 -861 3485 C ATOM 1669 C LEU A1010 169.179 16.737 565.551 1.00101.76 C ANISOU 1669 C LEU A1010 11454 19269 7942 754 -947 3441 C ATOM 1670 O LEU A1010 167.972 16.971 565.691 1.00 99.47 O ANISOU 1670 O LEU A1010 11454 18520 7820 464 -1011 3531 O ATOM 1671 CB LEU A1010 170.469 15.343 567.203 1.00111.35 C ANISOU 1671 CB LEU A1010 12511 21064 8731 1813 -1000 3403 C ATOM 1672 CG LEU A1010 169.649 15.686 568.447 1.00 91.20 C ANISOU 1672 CG LEU A1010 10054 18334 6265 1694 -1170 3425 C ATOM 1673 CD1 LEU A1010 169.949 14.698 569.560 1.00101.21 C ANISOU 1673 CD1 LEU A1010 11476 19597 7384 2272 -1190 3398 C ATOM 1674 CD2 LEU A1010 169.926 17.109 568.906 1.00 90.75 C ANISOU 1674 CD2 LEU A1010 9475 18628 6379 1260 -1305 3274 C ATOM 1675 N ASN A1011 170.040 17.672 565.140 1.00103.67 N ANISOU 1675 N ASN A1011 11219 19932 8241 496 -936 3299 N ATOM 1676 CA ASN A1011 169.578 19.023 564.833 1.00103.75 C ANISOU 1676 CA ASN A1011 11086 19830 8503 -135 -995 3258 C ATOM 1677 C ASN A1011 168.699 19.045 563.588 1.00102.28 C ANISOU 1677 C ASN A1011 11294 19128 8438 -474 -921 3387 C ATOM 1678 O ASN A1011 167.717 19.794 563.531 1.00103.39 O ANISOU 1678 O ASN A1011 11559 18923 8800 -882 -1008 3450 O ATOM 1679 CB ASN A1011 170.771 19.963 564.656 1.00112.27 C ANISOU 1679 CB ASN A1011 11602 21483 9570 -344 -966 3059 C ATOM 1680 CG ASN A1011 171.519 20.206 565.951 1.00118.17 C ANISOU 1680 CG ASN A1011 11912 22762 10224 -141 -1083 2917 C ATOM 1681 OD1 ASN A1011 170.969 20.034 567.037 1.00113.80 O ANISOU 1681 OD1 ASN A1011 11479 22081 9677 8 -1212 2967 O ATOM 1682 ND2 ASN A1011 172.778 20.615 565.842 1.00125.08 N ANISOU 1682 ND2 ASN A1011 12274 24254 10998 -158 -1037 2731 N ATOM 1683 N ASP A1012 169.044 18.243 562.577 1.00100.22 N ANISOU 1683 N ASP A1012 11230 18819 8029 -308 -762 3429 N ATOM 1684 CA ASP A1012 168.249 18.209 561.353 1.00 96.02 C ANISOU 1684 CA ASP A1012 11089 17825 7570 -638 -699 3552 C ATOM 1685 C ASP A1012 166.832 17.723 561.633 1.00 94.26 C ANISOU 1685 C ASP A1012 11329 17059 7427 -662 -784 3715 C ATOM 1686 O ASP A1012 165.854 18.340 561.197 1.00 94.55 O ANISOU 1686 O ASP A1012 11517 16753 7657 -1084 -867 3800 O ATOM 1687 CB ASP A1012 168.928 17.322 560.308 1.00 97.11 C ANISOU 1687 CB ASP A1012 11383 18019 7496 -423 -486 3553 C ATOM 1688 CG ASP A1012 170.185 17.950 559.735 1.00 99.49 C ANISOU 1688 CG ASP A1012 11244 18803 7755 -545 -375 3385 C ATOM 1689 OD1 ASP A1012 170.262 19.196 559.690 1.00 99.41 O ANISOU 1689 OD1 ASP A1012 10950 18922 7901 -986 -447 3306 O ATOM 1690 OD2 ASP A1012 171.094 17.199 559.326 1.00101.68 O ANISOU 1690 OD2 ASP A1012 11471 19324 7838 -206 -194 3326 O ATOM 1691 N ASN A1013 166.703 16.613 562.363 1.00 94.67 N ANISOU 1691 N ASN A1013 11614 17034 7323 -208 -758 3758 N ATOM 1692 CA ASN A1013 165.384 16.092 562.703 1.00 96.12 C ANISOU 1692 CA ASN A1013 12237 16717 7566 -241 -809 3879 C ATOM 1693 C ASN A1013 164.627 17.009 563.654 1.00 95.68 C ANISOU 1693 C ASN A1013 12017 16568 7768 -489 -985 3855 C ATOM 1694 O ASN A1013 163.394 16.946 563.706 1.00 94.06 O ANISOU 1694 O ASN A1013 12095 15871 7773 -673 -1020 3871 O ATOM 1695 CB ASN A1013 165.509 14.693 563.310 1.00 99.87 C ANISOU 1695 CB ASN A1013 13036 17067 7843 303 -702 3864 C ATOM 1696 CG ASN A1013 165.907 13.649 562.288 1.00105.20 C ANISOU 1696 CG ASN A1013 14037 17636 8297 513 -492 3900 C ATOM 1697 OD1 ASN A1013 165.055 12.985 561.697 1.00105.41 O ANISOU 1697 OD1 ASN A1013 14553 17142 8357 386 -408 3922 O ATOM 1698 ND2 ASN A1013 167.209 13.499 562.072 1.00108.70 N ANISOU 1698 ND2 ASN A1013 14205 18579 8517 830 -394 3877 N ATOM 1699 N LEU A1014 165.333 17.851 564.413 1.00 96.11 N ANISOU 1699 N LEU A1014 11616 17040 7860 -495 -1070 3749 N ATOM 1700 CA LEU A1014 164.649 18.829 565.252 1.00 94.91 C ANISOU 1700 CA LEU A1014 11314 16801 7946 -774 -1210 3724 C ATOM 1701 C LEU A1014 164.008 19.922 564.406 1.00 98.89 C ANISOU 1701 C LEU A1014 11787 17079 8708 -1304 -1257 3767 C ATOM 1702 O LEU A1014 162.884 20.356 564.686 1.00 98.87 O ANISOU 1702 O LEU A1014 11901 16745 8921 -1536 -1343 3832 O ATOM 1703 CB LEU A1014 165.625 19.429 566.265 1.00 92.43 C ANISOU 1703 CB LEU A1014 10544 16985 7591 -666 -1268 3566 C ATOM 1704 CG LEU A1014 165.002 20.389 567.282 1.00 88.28 C ANISOU 1704 CG LEU A1014 9884 16381 7276 -924 -1383 3520 C ATOM 1705 CD1 LEU A1014 163.882 19.701 568.043 1.00 84.28 C ANISOU 1705 CD1 LEU A1014 9747 15479 6795 -784 -1413 3612 C ATOM 1706 CD2 LEU A1014 166.057 20.917 568.239 1.00 90.87 C ANISOU 1706 CD2 LEU A1014 9772 17242 7510 -835 -1434 3352 C ATOM 1707 N LYS A1015 164.714 20.383 563.370 1.00105.94 N ANISOU 1707 N LYS A1015 12529 18148 9575 -1491 -1196 3733 N ATOM 1708 CA LYS A1015 164.124 21.335 562.436 1.00107.05 C ANISOU 1708 CA LYS A1015 12715 18041 9916 -1967 -1237 3800 C ATOM 1709 C LYS A1015 162.947 20.716 561.695 1.00102.96 C ANISOU 1709 C LYS A1015 12638 17047 9437 -2053 -1260 3976 C ATOM 1710 O LYS A1015 161.929 21.379 561.467 1.00101.84 O ANISOU 1710 O LYS A1015 12569 16557 9568 -2344 -1352 4016 O ATOM 1711 CB LYS A1015 165.181 21.824 561.444 1.00114.53 C ANISOU 1711 CB LYS A1015 13469 19270 10777 -2141 -1137 3720 C ATOM 1712 CG LYS A1015 166.353 22.560 562.074 1.00120.27 C ANISOU 1712 CG LYS A1015 13721 20509 11466 -2149 -1109 3522 C ATOM 1713 CD LYS A1015 167.338 23.024 561.010 1.00123.65 C ANISOU 1713 CD LYS A1015 13981 21196 11803 -2371 -980 3431 C ATOM 1714 CE LYS A1015 168.499 23.795 561.619 1.00126.47 C ANISOU 1714 CE LYS A1015 13841 22098 12114 -2441 -943 3209 C ATOM 1715 NZ LYS A1015 169.461 24.269 560.584 1.00129.01 N ANISOU 1715 NZ LYS A1015 13994 22682 12341 -2699 -789 3095 N ATOM 1716 N VAL A1016 163.071 19.444 561.307 1.00 99.20 N ANISOU 1716 N VAL A1016 12439 16457 8795 -1757 -1140 3964 N ATOM 1717 CA VAL A1016 161.985 18.762 560.606 1.00 94.01 C ANISOU 1717 CA VAL A1016 12191 15268 8260 -1806 -1111 3972 C ATOM 1718 C VAL A1016 160.745 18.683 561.489 1.00 95.27 C ANISOU 1718 C VAL A1016 12460 15101 8637 -1800 -1193 3954 C ATOM 1719 O VAL A1016 159.612 18.807 561.006 1.00 95.54 O ANISOU 1719 O VAL A1016 12647 14769 8888 -2015 -1248 3958 O ATOM 1720 CB VAL A1016 162.446 17.368 560.139 1.00 88.45 C ANISOU 1720 CB VAL A1016 11800 14525 7282 -1479 -933 3958 C ATOM 1721 CG1 VAL A1016 161.288 16.588 559.539 1.00 87.49 C ANISOU 1721 CG1 VAL A1016 12115 13878 7250 -1534 -888 3939 C ATOM 1722 CG2 VAL A1016 163.575 17.499 559.129 1.00 86.39 C ANISOU 1722 CG2 VAL A1016 11431 14575 6817 -1535 -829 3978 C ATOM 1723 N ILE A1017 160.937 18.486 562.796 1.00 98.18 N ANISOU 1723 N ILE A1017 12733 15629 8940 -1555 -1205 3927 N ATOM 1724 CA ILE A1017 159.806 18.475 563.720 1.00 99.82 C ANISOU 1724 CA ILE A1017 13031 15562 9334 -1577 -1264 3908 C ATOM 1725 C ILE A1017 159.138 19.843 563.764 1.00101.16 C ANISOU 1725 C ILE A1017 12963 15668 9804 -1959 -1406 3951 C ATOM 1726 O ILE A1017 157.905 19.950 563.770 1.00100.17 O ANISOU 1726 O ILE A1017 12945 15211 9905 -2115 -1457 3960 O ATOM 1727 CB ILE A1017 160.259 18.026 565.122 1.00102.06 C ANISOU 1727 CB ILE A1017 13275 16049 9455 -1237 -1245 3865 C ATOM 1728 CG1 ILE A1017 160.521 16.522 565.149 1.00104.93 C ANISOU 1728 CG1 ILE A1017 14011 16306 9553 -836 -1099 3835 C ATOM 1729 CG2 ILE A1017 159.218 18.391 566.166 1.00 99.81 C ANISOU 1729 CG2 ILE A1017 12987 15566 9370 -1351 -1316 3854 C ATOM 1730 CD1 ILE A1017 160.793 15.979 566.530 1.00104.89 C ANISOU 1730 CD1 ILE A1017 14054 16408 9390 -482 -1088 3791 C ATOM 1731 N GLU A1018 159.940 20.911 563.792 1.00103.45 N ANISOU 1731 N GLU A1018 12929 16293 10084 -2117 -1463 3980 N ATOM 1732 CA GLU A1018 159.383 22.254 563.922 1.00104.91 C ANISOU 1732 CA GLU A1018 12929 16410 10523 -2463 -1578 4037 C ATOM 1733 C GLU A1018 158.559 22.643 562.699 1.00106.28 C ANISOU 1733 C GLU A1018 13226 16244 10911 -2728 -1631 4087 C ATOM 1734 O GLU A1018 157.503 23.273 562.833 1.00106.32 O ANISOU 1734 O GLU A1018 13217 15998 11183 -2904 -1725 4128 O ATOM 1735 CB GLU A1018 160.506 23.267 564.154 1.00110.72 C ANISOU 1735 CB GLU A1018 13323 17548 11198 -2577 -1576 3976 C ATOM 1736 CG GLU A1018 160.020 24.700 564.312 1.00114.68 C ANISOU 1736 CG GLU A1018 13667 17917 11988 -2913 -1640 3973 C ATOM 1737 CD GLU A1018 161.151 25.684 564.545 1.00120.43 C ANISOU 1737 CD GLU A1018 14080 18995 12684 -3048 -1585 3819 C ATOM 1738 OE1 GLU A1018 162.269 25.243 564.885 1.00123.78 O ANISOU 1738 OE1 GLU A1018 14334 19816 12880 -2843 -1520 3694 O ATOM 1739 OE2 GLU A1018 160.919 26.901 564.386 1.00121.82 O ANISOU 1739 OE2 GLU A1018 14180 19053 13052 -3360 -1600 3820 O ATOM 1740 N LYS A1019 159.016 22.275 561.503 1.00124.14 N ANISOU 1740 N LYS A1019 19676 18377 9112 -920 -1903 231 N ATOM 1741 CA LYS A1019 158.357 22.651 560.257 1.00118.76 C ANISOU 1741 CA LYS A1019 19434 17351 8339 -1103 -2101 145 C ATOM 1742 C LYS A1019 157.710 21.450 559.570 1.00115.01 C ANISOU 1742 C LYS A1019 19087 16684 7928 -1244 -2065 277 C ATOM 1743 O LYS A1019 157.702 21.344 558.342 1.00114.96 O ANISOU 1743 O LYS A1019 19505 16322 7852 -1446 -2074 216 O ATOM 1744 CB LYS A1019 159.337 23.346 559.313 1.00113.45 C ANISOU 1744 CB LYS A1019 19162 16385 7559 -1310 -2029 25 C ATOM 1745 CG LYS A1019 160.516 22.492 558.861 1.00109.70 C ANISOU 1745 CG LYS A1019 18759 15815 7107 -1442 -1641 63 C ATOM 1746 CD LYS A1019 161.238 23.145 557.692 1.00107.58 C ANISOU 1746 CD LYS A1019 18902 15314 6659 -1709 -1586 -27 C ATOM 1747 CE LYS A1019 162.240 22.199 557.049 1.00107.80 C ANISOU 1747 CE LYS A1019 19006 15294 6659 -1810 -1204 -38 C ATOM 1748 NZ LYS A1019 162.841 22.789 555.820 1.00110.98 N ANISOU 1748 NZ LYS A1019 19790 15561 6815 -2100 -1134 -103 N ATOM 1749 N ALA A1020 157.147 20.537 560.356 1.00112.32 N ANISOU 1749 N ALA A1020 18386 16582 7709 -1153 -2056 471 N ATOM 1750 CA ALA A1020 156.460 19.384 559.795 1.00112.42 C ANISOU 1750 CA ALA A1020 18503 16391 7819 -1303 -2103 626 C ATOM 1751 C ALA A1020 155.037 19.751 559.391 1.00114.22 C ANISOU 1751 C ALA A1020 18801 16610 7987 -1347 -2434 620 C ATOM 1752 O ALA A1020 154.393 20.605 560.006 1.00116.71 O ANISOU 1752 O ALA A1020 18875 17245 8224 -1181 -2621 563 O ATOM 1753 CB ALA A1020 156.436 18.231 560.796 1.00113.98 C ANISOU 1753 CB ALA A1020 18292 16828 8187 -1252 -2013 901 C ATOM 1754 N ASP A1021 154.548 19.090 558.342 1.00113.27 N ANISOU 1754 N ASP A1021 19009 16125 7901 -1546 -2528 653 N ATOM 1755 CA ASP A1021 153.215 19.338 557.804 1.00114.39 C ANISOU 1755 CA ASP A1021 19257 16203 8003 -1617 -2857 650 C ATOM 1756 C ASP A1021 152.172 18.352 558.310 1.00117.66 C ANISOU 1756 C ASP A1021 19324 16820 8562 -1673 -2994 935 C ATOM 1757 O ASP A1021 151.014 18.733 558.507 1.00119.01 O ANISOU 1757 O ASP A1021 19283 17240 8693 -1632 -3247 970 O ATOM 1758 CB ASP A1021 153.243 19.292 556.272 1.00111.62 C ANISOU 1758 CB ASP A1021 19504 15332 7573 -1825 -2926 511 C ATOM 1759 CG ASP A1021 154.253 20.252 555.676 1.00110.96 C ANISOU 1759 CG ASP A1021 19720 15076 7362 -1834 -2780 289 C ATOM 1760 OD1 ASP A1021 154.507 21.311 556.286 1.00112.45 O ANISOU 1760 OD1 ASP A1021 19682 15474 7571 -1671 -2775 203 O ATOM 1761 OD2 ASP A1021 154.793 19.946 554.592 1.00 95.52 O ANISOU 1761 OD2 ASP A1021 18148 12789 5355 -1986 -2655 202 O ATOM 1762 N ASN A1022 152.549 17.091 558.519 1.00123.41 N ANISOU 1762 N ASN A1022 19977 17451 9460 -1773 -2865 1149 N ATOM 1763 CA ASN A1022 151.597 16.077 558.955 1.00125.99 C ANISOU 1763 CA ASN A1022 20001 17925 9944 -1907 -3039 1490 C ATOM 1764 C ASN A1022 152.133 15.295 560.148 1.00124.16 C ANISOU 1764 C ASN A1022 19355 17982 9839 -1869 -2875 1767 C ATOM 1765 O ASN A1022 153.161 15.659 560.728 1.00121.65 O ANISOU 1765 O ASN A1022 18937 17812 9474 -1692 -2628 1666 O ATOM 1766 CB ASN A1022 151.261 15.125 557.804 1.00130.94 C ANISOU 1766 CB ASN A1022 21051 17999 10700 -2148 -3214 1528 C ATOM 1767 CG ASN A1022 152.471 14.358 557.309 1.00134.76 C ANISOU 1767 CG ASN A1022 21877 18048 11276 -2158 -3020 1424 C ATOM 1768 OD1 ASN A1022 153.603 14.831 557.407 1.00134.99 O ANISOU 1768 OD1 ASN A1022 21969 18107 11213 -2007 -2740 1228 O ATOM 1769 ND2 ASN A1022 152.237 13.167 556.771 1.00138.81 N ANISOU 1769 ND2 ASN A1022 22605 18162 11976 -2324 -3197 1539 N ATOM 1770 N ALA A1023 151.440 14.217 560.519 1.00123.57 N ANISOU 1770 N ALA A1023 19042 17981 9928 -2060 -3041 2145 N ATOM 1771 CA ALA A1023 151.807 13.425 561.685 1.00121.80 C ANISOU 1771 CA ALA A1023 18412 18046 9819 -2074 -2954 2488 C ATOM 1772 C ALA A1023 152.908 12.410 561.405 1.00120.31 C ANISOU 1772 C ALA A1023 18521 17346 9845 -2110 -2864 2496 C ATOM 1773 O ALA A1023 153.459 11.846 562.356 1.00121.51 O ANISOU 1773 O ALA A1023 18393 17679 10095 -2079 -2777 2730 O ATOM 1774 CB ALA A1023 150.576 12.700 562.236 1.00121.68 C ANISOU 1774 CB ALA A1023 17988 18364 9881 -2317 -3212 2955 C ATOM 1775 N ALA A1024 153.239 12.160 560.137 1.00120.81 N ANISOU 1775 N ALA A1024 19133 16802 9967 -2152 -2899 2233 N ATOM 1776 CA ALA A1024 154.284 11.191 559.826 1.00126.71 C ANISOU 1776 CA ALA A1024 20153 17087 10904 -2120 -2834 2168 C ATOM 1777 C ALA A1024 155.675 11.790 559.993 1.00131.26 C ANISOU 1777 C ALA A1024 20758 17745 11372 -1863 -2466 1872 C ATOM 1778 O ALA A1024 156.595 11.110 560.462 1.00132.99 O ANISOU 1778 O ALA A1024 20900 17889 11742 -1765 -2363 1924 O ATOM 1779 CB ALA A1024 154.100 10.656 558.406 1.00128.62 C ANISOU 1779 CB ALA A1024 20950 16708 11212 -2227 -3021 1963 C ATOM 1780 N GLN A1025 155.848 13.058 559.612 1.00131.71 N ANISOU 1780 N GLN A1025 20923 17941 11181 -1766 -2301 1576 N ATOM 1781 CA GLN A1025 157.167 13.681 559.679 1.00130.72 C ANISOU 1781 CA GLN A1025 20833 17886 10948 -1578 -1978 1314 C ATOM 1782 C GLN A1025 157.621 13.879 561.121 1.00128.45 C ANISOU 1782 C GLN A1025 20053 18067 10686 -1431 -1842 1485 C ATOM 1783 O GLN A1025 158.807 13.713 561.430 1.00129.00 O ANISOU 1783 O GLN A1025 20070 18134 10809 -1295 -1624 1401 O ATOM 1784 CB GLN A1025 157.151 15.011 558.927 1.00131.79 C ANISOU 1784 CB GLN A1025 21218 18031 10823 -1575 -1917 1021 C ATOM 1785 CG GLN A1025 157.002 14.856 557.423 1.00136.41 C ANISOU 1785 CG GLN A1025 22336 18165 11329 -1706 -1992 812 C ATOM 1786 CD GLN A1025 156.539 16.130 556.749 1.00138.64 C ANISOU 1786 CD GLN A1025 22845 18463 11368 -1774 -2073 641 C ATOM 1787 OE1 GLN A1025 157.254 16.714 555.936 1.00139.31 O ANISOU 1787 OE1 GLN A1025 23242 18420 11269 -1802 -1926 409 O ATOM 1788 NE2 GLN A1025 155.329 16.564 557.080 1.00139.32 N ANISOU 1788 NE2 GLN A1025 22765 18725 11446 -1805 -2328 766 N ATOM 1789 N VAL A1026 156.699 14.239 562.016 1.00129.93 N ANISOU 1789 N VAL A1026 19855 18700 10814 -1439 -1970 1709 N ATOM 1790 CA VAL A1026 157.063 14.408 563.420 1.00129.96 C ANISOU 1790 CA VAL A1026 19378 19204 10795 -1289 -1858 1873 C ATOM 1791 C VAL A1026 157.434 13.068 564.044 1.00128.05 C ANISOU 1791 C VAL A1026 18971 18894 10787 -1344 -1882 2194 C ATOM 1792 O VAL A1026 158.347 12.988 564.874 1.00125.90 O ANISOU 1792 O VAL A1026 18480 18806 10549 -1199 -1723 2234 O ATOM 1793 CB VAL A1026 155.925 15.099 564.194 1.00128.79 C ANISOU 1793 CB VAL A1026 18834 19625 10475 -1253 -1997 2002 C ATOM 1794 CG1 VAL A1026 155.946 16.596 563.943 1.00125.73 C ANISOU 1794 CG1 VAL A1026 18548 19353 9872 -1085 -1972 1637 C ATOM 1795 CG2 VAL A1026 154.581 14.517 563.796 1.00130.01 C ANISOU 1795 CG2 VAL A1026 18987 19728 10684 -1482 -2267 2235 C ATOM 1796 N LYS A1027 156.737 11.996 563.656 1.00129.16 N ANISOU 1796 N LYS A1027 19229 18739 11106 -1562 -2127 2437 N ATOM 1797 CA LYS A1027 157.054 10.673 564.185 1.00133.67 C ANISOU 1797 CA LYS A1027 19701 19149 11937 -1643 -2245 2767 C ATOM 1798 C LYS A1027 158.429 10.207 563.721 1.00134.67 C ANISOU 1798 C LYS A1027 20125 18828 12216 -1474 -2098 2494 C ATOM 1799 O LYS A1027 159.258 9.781 564.534 1.00135.82 O ANISOU 1799 O LYS A1027 20068 19062 12475 -1357 -2023 2609 O ATOM 1800 CB LYS A1027 155.983 9.664 563.769 1.00137.69 C ANISOU 1800 CB LYS A1027 20321 19368 12628 -1943 -2612 3077 C ATOM 1801 CG LYS A1027 154.685 9.757 564.548 1.00139.16 C ANISOU 1801 CG LYS A1027 20055 20107 12711 -2148 -2783 3500 C ATOM 1802 CD LYS A1027 153.742 8.634 564.150 1.00141.46 C ANISOU 1802 CD LYS A1027 20451 20066 13230 -2499 -3181 3862 C ATOM 1803 CE LYS A1027 152.479 8.639 564.993 1.00142.15 C ANISOU 1803 CE LYS A1027 20007 20800 13204 -2744 -3341 4347 C ATOM 1804 NZ LYS A1027 151.577 7.507 564.640 1.00144.94 N ANISOU 1804 NZ LYS A1027 20439 20827 13805 -3148 -3768 4763 N ATOM 1805 N ASP A1028 158.683 10.271 562.411 1.00136.93 N ANISOU 1805 N ASP A1028 20874 18666 12487 -1449 -2061 2125 N ATOM 1806 CA ASP A1028 159.956 9.798 561.876 1.00137.55 C ANISOU 1806 CA ASP A1028 21208 18382 12671 -1263 -1915 1823 C ATOM 1807 C ASP A1028 161.124 10.603 562.431 1.00132.56 C ANISOU 1807 C ASP A1028 20363 18088 11915 -1042 -1563 1636 C ATOM 1808 O ASP A1028 162.171 10.039 562.771 1.00134.40 O ANISOU 1808 O ASP A1028 20524 18243 12299 -872 -1473 1589 O ATOM 1809 CB ASP A1028 159.938 9.855 560.348 1.00140.29 C ANISOU 1809 CB ASP A1028 22060 18315 12930 -1279 -1914 1448 C ATOM 1810 CG ASP A1028 161.230 9.360 559.731 1.00144.73 C ANISOU 1810 CG ASP A1028 22853 18590 13550 -1053 -1749 1090 C ATOM 1811 OD1 ASP A1028 161.581 8.182 559.949 1.00148.86 O ANISOU 1811 OD1 ASP A1028 23392 18820 14349 -963 -1928 1164 O ATOM 1812 OD2 ASP A1028 161.894 10.148 559.025 1.00144.82 O ANISOU 1812 OD2 ASP A1028 23016 18684 13324 -968 -1462 738 O ATOM 1813 N ALA A1029 160.965 11.925 562.529 1.00125.58 N ANISOU 1813 N ALA A1029 19380 17561 10774 -1036 -1403 1523 N ATOM 1814 CA ALA A1029 162.035 12.749 563.077 1.00121.68 C ANISOU 1814 CA ALA A1029 18685 17374 10173 -860 -1123 1364 C ATOM 1815 C ALA A1029 162.219 12.515 564.572 1.00115.07 C ANISOU 1815 C ALA A1029 17387 16909 9425 -768 -1137 1661 C ATOM 1816 O ALA A1029 163.344 12.606 565.073 1.00 97.08 O ANISOU 1816 O ALA A1029 14953 14750 7184 -600 -953 1573 O ATOM 1817 CB ALA A1029 161.763 14.226 562.792 1.00 95.05 C ANISOU 1817 CB ALA A1029 15367 14219 6530 -889 -1045 1174 C ATOM 1818 N LEU A1030 161.138 12.217 565.299 1.00108.89 N ANISOU 1818 N LEU A1030 16361 16358 8656 -887 -1353 2025 N ATOM 1819 CA LEU A1030 161.265 11.898 566.719 1.00109.46 C ANISOU 1819 CA LEU A1030 15991 16828 8772 -831 -1382 2356 C ATOM 1820 C LEU A1030 162.070 10.620 566.924 1.00117.15 C ANISOU 1820 C LEU A1030 16994 17480 10036 -792 -1446 2496 C ATOM 1821 O LEU A1030 162.963 10.563 567.778 1.00117.04 O ANISOU 1821 O LEU A1030 16744 17659 10068 -633 -1340 2540 O ATOM 1822 CB LEU A1030 159.882 11.765 567.360 1.00107.67 C ANISOU 1822 CB LEU A1030 15478 16971 8461 -1008 -1602 2748 C ATOM 1823 CG LEU A1030 159.276 13.011 568.007 1.00103.89 C ANISOU 1823 CG LEU A1030 14685 17113 7674 -913 -1545 2694 C ATOM 1824 CD1 LEU A1030 157.852 12.733 568.457 1.00103.49 C ANISOU 1824 CD1 LEU A1030 14342 17444 7534 -1099 -1762 3068 C ATOM 1825 CD2 LEU A1030 160.126 13.478 569.178 1.00105.12 C ANISOU 1825 CD2 LEU A1030 14504 17703 7732 -687 -1385 2677 C ATOM 1826 N THR A1031 161.761 9.579 566.149 1.00124.97 N ANISOU 1826 N THR A1031 18288 17957 11238 -919 -1663 2554 N ATOM 1827 CA THR A1031 162.439 8.298 566.315 1.00131.02 C ANISOU 1827 CA THR A1031 19119 18346 12317 -860 -1824 2674 C ATOM 1828 C THR A1031 163.901 8.386 565.892 1.00132.49 C ANISOU 1828 C THR A1031 19439 18345 12555 -567 -1572 2237 C ATOM 1829 O THR A1031 164.792 7.909 566.604 1.00133.42 O ANISOU 1829 O THR A1031 19380 18483 12831 -403 -1564 2302 O ATOM 1830 CB THR A1031 161.714 7.215 565.515 1.00132.41 C ANISOU 1830 CB THR A1031 19628 17970 12714 -1050 -2182 2792 C ATOM 1831 OG1 THR A1031 161.672 7.589 564.132 1.00129.52 O ANISOU 1831 OG1 THR A1031 19666 17299 12249 -1015 -2085 2355 O ATOM 1832 CG2 THR A1031 160.293 7.040 566.030 1.00133.67 C ANISOU 1832 CG2 THR A1031 19579 18371 12840 -1381 -2449 3295 C ATOM 1833 N LYS A1032 164.166 8.994 564.734 1.00133.40 N ANISOU 1833 N LYS A1032 19847 18314 12524 -508 -1370 1802 N ATOM 1834 CA LYS A1032 165.535 9.053 564.229 1.00135.18 C ANISOU 1834 CA LYS A1032 20170 18431 12762 -256 -1115 1389 C ATOM 1835 C LYS A1032 166.402 9.977 565.077 1.00134.47 C ANISOU 1835 C LYS A1032 19733 18812 12547 -127 -833 1342 C ATOM 1836 O LYS A1032 167.601 9.725 565.250 1.00136.15 O ANISOU 1836 O LYS A1032 19842 19024 12866 91 -695 1175 O ATOM 1837 CB LYS A1032 165.532 9.492 562.764 1.00137.84 C ANISOU 1837 CB LYS A1032 20890 18571 12913 -280 -973 988 C ATOM 1838 CG LYS A1032 166.848 9.252 562.041 1.00141.03 C ANISOU 1838 CG LYS A1032 21415 18846 13323 -31 -749 560 C ATOM 1839 CD LYS A1032 166.626 9.052 560.549 1.00142.33 C ANISOU 1839 CD LYS A1032 22021 18689 13370 -55 -760 234 C ATOM 1840 CE LYS A1032 165.853 10.210 559.939 1.00139.12 C ANISOU 1840 CE LYS A1032 21773 18434 12651 -305 -669 215 C ATOM 1841 NZ LYS A1032 165.534 9.973 558.505 1.00140.01 N ANISOU 1841 NZ LYS A1032 22332 18235 12629 -351 -719 -64 N ATOM 1842 N MET A1033 165.819 11.053 565.611 1.00132.63 N ANISOU 1842 N MET A1033 19313 18985 12096 -237 -774 1464 N ATOM 1843 CA MET A1033 166.563 11.915 566.525 1.00132.10 C ANISOU 1843 CA MET A1033 18918 19348 11925 -113 -583 1436 C ATOM 1844 C MET A1033 166.871 11.196 567.832 1.00136.57 C ANISOU 1844 C MET A1033 19147 20078 12665 -12 -697 1750 C ATOM 1845 O MET A1033 167.960 11.361 568.395 1.00137.13 O ANISOU 1845 O MET A1033 19011 20314 12778 165 -554 1662 O ATOM 1846 CB MET A1033 165.781 13.200 566.797 1.00126.24 C ANISOU 1846 CB MET A1033 18082 18969 10917 -210 -574 1457 C ATOM 1847 CG MET A1033 166.460 14.152 567.765 1.00124.27 C ANISOU 1847 CG MET A1033 17517 19144 10555 -74 -446 1408 C ATOM 1848 SD MET A1033 165.287 15.255 568.574 1.00120.36 S ANISOU 1848 SD MET A1033 16801 19130 9801 -98 -588 1526 S ATOM 1849 CE MET A1033 164.340 15.811 567.165 1.00117.46 C ANISOU 1849 CE MET A1033 16849 18476 9305 -281 -656 1337 C ATOM 1850 N ARG A1034 165.927 10.390 568.326 1.00140.97 N ANISOU 1850 N ARG A1034 19637 20605 13319 -151 -974 2147 N ATOM 1851 CA ARG A1034 166.154 9.657 569.568 1.00147.24 C ANISOU 1851 CA ARG A1034 20127 21561 14257 -108 -1125 2516 C ATOM 1852 C ARG A1034 167.234 8.597 569.394 1.00151.01 C ANISOU 1852 C ARG A1034 20713 21616 15048 68 -1189 2421 C ATOM 1853 O ARG A1034 168.049 8.379 570.299 1.00153.74 O ANISOU 1853 O ARG A1034 20809 22116 15488 221 -1183 2519 O ATOM 1854 CB ARG A1034 164.848 9.025 570.052 1.00154.61 C ANISOU 1854 CB ARG A1034 20962 22581 15202 -367 -1429 3014 C ATOM 1855 CG ARG A1034 164.972 8.276 571.370 1.00160.93 C ANISOU 1855 CG ARG A1034 21439 23602 16103 -392 -1616 3483 C ATOM 1856 CD ARG A1034 163.621 7.792 571.879 1.00166.09 C ANISOU 1856 CD ARG A1034 21930 24480 16696 -711 -1890 4027 C ATOM 1857 NE ARG A1034 162.977 6.855 570.961 1.00170.86 N ANISOU 1857 NE ARG A1034 22871 24514 17533 -929 -2174 4136 N ATOM 1858 CZ ARG A1034 161.968 7.171 570.155 1.00170.54 C ANISOU 1858 CZ ARG A1034 22993 24415 17390 -1098 -2202 4064 C ATOM 1859 NH1 ARG A1034 161.444 6.253 569.352 1.00172.09 N ANISOU 1859 NH1 ARG A1034 23507 24059 17820 -1292 -2502 4165 N ATOM 1860 NH2 ARG A1034 161.481 8.404 570.152 1.00168.36 N ANISOU 1860 NH2 ARG A1034 22572 24608 16787 -1061 -1974 3879 N ATOM 1861 N ALA A1035 167.258 7.925 568.240 1.00151.75 N ANISOU 1861 N ALA A1035 21177 21182 15299 78 -1276 2204 N ATOM 1862 CA ALA A1035 168.318 6.960 567.967 1.00154.56 C ANISOU 1862 CA ALA A1035 21647 21137 15941 323 -1350 2007 C ATOM 1863 C ALA A1035 169.675 7.649 567.891 1.00151.02 C ANISOU 1863 C ALA A1035 21057 20911 15412 588 -985 1605 C ATOM 1864 O ALA A1035 170.661 7.173 568.465 1.00154.17 O ANISOU 1864 O ALA A1035 21278 21303 15998 813 -1008 1585 O ATOM 1865 CB ALA A1035 168.018 6.202 566.673 1.00158.35 C ANISOU 1865 CB ALA A1035 22565 21048 16554 320 -1521 1779 C ATOM 1866 N ALA A1036 169.742 8.779 567.180 1.00143.97 N ANISOU 1866 N ALA A1036 20237 20219 14246 543 -674 1302 N ATOM 1867 CA ALA A1036 170.985 9.540 567.115 1.00138.29 C ANISOU 1867 CA ALA A1036 19352 19765 13426 714 -337 978 C ATOM 1868 C ALA A1036 171.340 10.153 568.464 1.00132.10 C ANISOU 1868 C ALA A1036 18171 19423 12598 747 -287 1187 C ATOM 1869 O ALA A1036 172.521 10.389 568.743 1.00131.91 O ANISOU 1869 O ALA A1036 17937 19570 12614 928 -114 1012 O ATOM 1870 CB ALA A1036 170.883 10.629 566.046 1.00137.93 C ANISOU 1870 CB ALA A1036 19501 19819 13089 582 -78 684 C ATOM 1871 N ALA A1037 170.341 10.425 569.307 1.00128.48 N ANISOU 1871 N ALA A1037 17584 19193 12038 586 -441 1546 N ATOM 1872 CA ALA A1037 170.624 10.966 570.633 1.00124.06 C ANISOU 1872 CA ALA A1037 16649 19087 11401 646 -423 1730 C ATOM 1873 C ALA A1037 171.290 9.925 571.523 1.00125.40 C ANISOU 1873 C ALA A1037 16621 19196 11828 807 -586 1943 C ATOM 1874 O ALA A1037 172.235 10.241 572.257 1.00126.53 O ANISOU 1874 O ALA A1037 16498 19591 11985 970 -492 1893 O ATOM 1875 CB ALA A1037 169.339 11.482 571.280 1.00119.32 C ANISOU 1875 CB ALA A1037 15937 18820 10581 471 -546 2026 C ATOM 1876 N LEU A1038 170.813 8.679 571.474 1.00127.07 N ANISOU 1876 N LEU A1038 16973 19049 12260 752 -876 2194 N ATOM 1877 CA LEU A1038 171.399 7.631 572.303 1.00132.59 C ANISOU 1877 CA LEU A1038 17528 19622 13230 887 -1113 2433 C ATOM 1878 C LEU A1038 172.787 7.242 571.809 1.00136.85 C ANISOU 1878 C LEU A1038 18104 19899 13995 1202 -1014 2029 C ATOM 1879 O LEU A1038 173.686 6.982 572.617 1.00138.94 O ANISOU 1879 O LEU A1038 18129 20264 14399 1395 -1061 2079 O ATOM 1880 CB LEU A1038 170.476 6.413 572.342 1.00135.62 C ANISOU 1880 CB LEU A1038 18082 19641 13809 700 -1523 2840 C ATOM 1881 CG LEU A1038 169.093 6.644 572.959 1.00133.26 C ANISOU 1881 CG LEU A1038 17658 19687 13289 372 -1647 3313 C ATOM 1882 CD1 LEU A1038 168.318 5.338 573.048 1.00136.35 C ANISOU 1882 CD1 LEU A1038 18187 19705 13913 143 -2098 3779 C ATOM 1883 CD2 LEU A1038 169.215 7.297 574.328 1.00131.59 C ANISOU 1883 CD2 LEU A1038 17026 20126 12848 394 -1559 3550 C ATOM 1884 N ASP A1039 172.983 7.191 570.488 1.00136.84 N ANISOU 1884 N ASP A1039 18381 19602 14012 1271 -881 1618 N ATOM 1885 CA ASP A1039 174.317 6.926 569.958 1.00139.40 C ANISOU 1885 CA ASP A1039 18681 19803 14483 1596 -733 1179 C ATOM 1886 C ASP A1039 175.282 8.051 570.307 1.00134.02 C ANISOU 1886 C ASP A1039 17680 19610 13630 1674 -380 988 C ATOM 1887 O ASP A1039 176.470 7.805 570.547 1.00137.61 O ANISOU 1887 O ASP A1039 17924 20122 14241 1943 -322 803 O ATOM 1888 CB ASP A1039 174.266 6.721 568.444 1.00144.94 C ANISOU 1888 CB ASP A1039 19726 20192 15151 1645 -635 768 C ATOM 1889 CG ASP A1039 173.977 5.283 568.060 1.00151.41 C ANISOU 1889 CG ASP A1039 20833 20418 16279 1764 -1041 782 C ATOM 1890 OD1 ASP A1039 172.981 5.045 567.344 1.00151.96 O ANISOU 1890 OD1 ASP A1039 21228 20202 16309 1578 -1185 823 O ATOM 1891 OD2 ASP A1039 174.742 4.390 568.482 1.00155.22 O ANISOU 1891 OD2 ASP A1039 21225 20691 17060 2048 -1261 750 O ATOM 1892 N ALA A1040 174.794 9.294 570.336 1.00125.31 N ANISOU 1892 N ALA A1040 16540 18849 12225 1447 -181 1022 N ATOM 1893 CA ALA A1040 175.626 10.403 570.785 1.00119.54 C ANISOU 1893 CA ALA A1040 15518 18550 11350 1478 66 897 C ATOM 1894 C ALA A1040 175.799 10.413 572.297 1.00118.28 C ANISOU 1894 C ALA A1040 15036 18662 11245 1542 -88 1210 C ATOM 1895 O ALA A1040 176.728 11.055 572.797 1.00117.84 O ANISOU 1895 O ALA A1040 14709 18903 11161 1639 47 1099 O ATOM 1896 CB ALA A1040 175.037 11.734 570.320 1.00117.24 C ANISOU 1896 CB ALA A1040 15334 18471 10742 1228 243 820 C ATOM 1897 N GLN A1041 174.928 9.717 573.031 1.00117.97 N ANISOU 1897 N GLN A1041 15010 18550 11265 1468 -381 1615 N ATOM 1898 CA GLN A1041 175.056 9.643 574.482 1.00116.18 C ANISOU 1898 CA GLN A1041 14477 18621 11046 1519 -543 1948 C ATOM 1899 C GLN A1041 176.122 8.637 574.900 1.00117.86 C ANISOU 1899 C GLN A1041 14561 18638 11581 1776 -695 1957 C ATOM 1900 O GLN A1041 176.915 8.910 575.808 1.00118.40 O ANISOU 1900 O GLN A1041 14334 18989 11662 1914 -683 1987 O ATOM 1901 CB GLN A1041 173.711 9.273 575.108 1.00108.33 C ANISOU 1901 CB GLN A1041 13506 17706 9949 1302 -796 2424 C ATOM 1902 CG GLN A1041 173.743 9.156 576.621 1.00109.32 C ANISOU 1902 CG GLN A1041 13309 18213 10014 1326 -969 2814 C ATOM 1903 CD GLN A1041 172.552 8.399 577.170 1.00110.91 C ANISOU 1903 CD GLN A1041 13518 18452 10172 1095 -1262 3351 C ATOM 1904 OE1 GLN A1041 172.044 8.712 578.247 1.00110.88 O ANISOU 1904 OE1 GLN A1041 13257 18955 9918 1013 -1325 3672 O ATOM 1905 NE2 GLN A1041 172.102 7.390 576.432 1.00112.77 N ANISOU 1905 NE2 GLN A1041 14035 18177 10636 983 -1459 3455 N ATOM 1906 N LYS A1042 176.151 7.470 574.251 1.00119.49 N ANISOU 1906 N LYS A1042 14996 18344 12060 1866 -879 1911 N ATOM 1907 CA LYS A1042 177.097 6.424 574.623 1.00120.53 C ANISOU 1907 CA LYS A1042 15040 18222 12535 2149 -1106 1905 C ATOM 1908 C LYS A1042 178.541 6.801 574.316 1.00119.02 C ANISOU 1908 C LYS A1042 14641 18167 12412 2445 -837 1436 C ATOM 1909 O LYS A1042 179.458 6.175 574.858 1.00123.51 O ANISOU 1909 O LYS A1042 15030 18664 13233 2712 -999 1419 O ATOM 1910 CB LYS A1042 176.741 5.119 573.908 1.00122.27 C ANISOU 1910 CB LYS A1042 15597 17822 13040 2202 -1424 1907 C ATOM 1911 CG LYS A1042 175.319 4.634 574.152 1.00121.64 C ANISOU 1911 CG LYS A1042 15712 17576 12929 1865 -1736 2411 C ATOM 1912 CD LYS A1042 174.994 3.429 573.280 1.00125.06 C ANISOU 1912 CD LYS A1042 16525 17336 13655 1907 -2073 2348 C ATOM 1913 CE LYS A1042 173.547 2.987 573.435 1.00125.33 C ANISOU 1913 CE LYS A1042 16743 17216 13662 1512 -2387 2867 C ATOM 1914 NZ LYS A1042 173.226 1.846 572.532 1.00128.90 N ANISOU 1914 NZ LYS A1042 17599 16960 14416 1542 -2764 2783 N ATOM 1915 N ALA A1043 178.765 7.802 573.472 1.00116.84 N ANISOU 1915 N ALA A1043 14372 18103 11918 2385 -453 1080 N ATOM 1916 CA ALA A1043 180.103 8.197 573.063 1.00117.98 C ANISOU 1916 CA ALA A1043 14293 18441 12093 2603 -173 656 C ATOM 1917 C ALA A1043 180.575 9.415 573.852 1.00137.83 C ANISOU 1917 C ALA A1043 16486 21456 14426 2508 5 707 C ATOM 1918 O ALA A1043 179.802 10.093 574.533 1.00112.88 O ANISOU 1918 O ALA A1043 13320 18504 11065 2290 -46 985 O ATOM 1919 CB ALA A1043 180.142 8.484 571.561 1.00118.39 C ANISOU 1919 CB ALA A1043 14549 18430 12005 2567 118 249 C ATOM 1920 N THR A1044 181.876 9.685 573.748 1.00130.64 N ANISOU 1920 N THR A1044 15292 20757 13588 2692 195 411 N ATOM 1921 CA THR A1044 182.522 10.737 574.513 1.00128.62 C ANISOU 1921 CA THR A1044 14711 20932 13226 2632 305 436 C ATOM 1922 C THR A1044 182.864 11.912 573.615 1.00126.60 C ANISOU 1922 C THR A1044 14432 20925 12744 2430 651 164 C ATOM 1923 O THR A1044 183.454 11.718 572.543 1.00131.11 O ANISOU 1923 O THR A1044 15004 21479 13331 2504 872 -156 O ATOM 1924 CB THR A1044 183.796 10.212 575.185 1.00135.99 C ANISOU 1924 CB THR A1044 15288 21955 14428 2951 215 360 C ATOM 1925 OG1 THR A1044 184.724 9.774 574.184 1.00140.97 O ANISOU 1925 OG1 THR A1044 15835 22538 15190 3176 402 -51 O ATOM 1926 CG2 THR A1044 183.463 9.049 576.101 1.00141.14 C ANISOU 1926 CG2 THR A1044 15988 22333 15306 3118 -186 681 C ATOM 1927 N PRO A1045 182.512 13.131 574.009 1.00120.35 N ANISOU 1927 N PRO A1045 13621 20378 11729 2177 680 278 N ATOM 1928 CA PRO A1045 182.837 14.300 573.195 1.00120.62 C ANISOU 1928 CA PRO A1045 13656 20611 11563 1932 937 77 C ATOM 1929 C PRO A1045 184.258 14.763 573.460 1.00122.64 C ANISOU 1929 C PRO A1045 13503 21189 11905 1989 1054 -68 C ATOM 1930 O PRO A1045 184.923 14.248 574.373 1.00124.72 O ANISOU 1930 O PRO A1045 13489 21523 12376 2239 920 -17 O ATOM 1931 CB PRO A1045 181.808 15.337 573.666 1.00115.54 C ANISOU 1931 CB PRO A1045 13176 20034 10690 1686 803 270 C ATOM 1932 CG PRO A1045 181.605 14.993 575.101 1.00107.37 C ANISOU 1932 CG PRO A1045 11980 19080 9734 1856 538 524 C ATOM 1933 CD PRO A1045 181.705 13.487 575.189 1.00116.35 C ANISOU 1933 CD PRO A1045 13116 19974 11119 2103 443 600 C ATOM 1934 N PRO A1046 184.775 15.728 572.675 1.00122.78 N ANISOU 1934 N PRO A1046 13463 21419 11769 1739 1283 -228 N ATOM 1935 CA PRO A1046 186.113 16.271 572.961 1.00125.91 C ANISOU 1935 CA PRO A1046 13435 22165 12241 1726 1372 -320 C ATOM 1936 C PRO A1046 186.139 17.077 574.252 1.00129.22 C ANISOU 1936 C PRO A1046 13715 22710 12673 1670 1116 -134 C ATOM 1937 O PRO A1046 186.265 18.305 574.225 1.00127.51 O ANISOU 1937 O PRO A1046 13487 22639 12323 1376 1093 -117 O ATOM 1938 CB PRO A1046 186.406 17.157 571.740 1.00125.78 C ANISOU 1938 CB PRO A1046 13459 22327 12004 1372 1641 -452 C ATOM 1939 CG PRO A1046 185.460 16.683 570.667 1.00124.26 C ANISOU 1939 CG PRO A1046 13675 21873 11666 1332 1748 -520 C ATOM 1940 CD PRO A1046 184.237 16.224 571.394 1.00121.17 C ANISOU 1940 CD PRO A1046 13563 21149 11326 1454 1469 -322 C ATOM 1941 N LYS A1047 186.019 16.398 575.390 1.00134.91 N ANISOU 1941 N LYS A1047 14344 23371 13544 1948 886 9 N ATOM 1942 CA LYS A1047 185.975 17.093 576.668 1.00137.13 C ANISOU 1942 CA LYS A1047 14504 23805 13793 1941 626 168 C ATOM 1943 C LYS A1047 187.356 17.602 577.061 1.00142.77 C ANISOU 1943 C LYS A1047 14803 24805 14637 1945 633 73 C ATOM 1944 O LYS A1047 188.386 17.063 576.648 1.00145.59 O ANISOU 1944 O LYS A1047 14886 25264 15167 2069 807 -78 O ATOM 1945 CB LYS A1047 185.432 16.179 577.765 1.00135.80 C ANISOU 1945 CB LYS A1047 14350 23548 13701 2209 380 390 C ATOM 1946 CG LYS A1047 183.956 15.883 577.639 1.00131.71 C ANISOU 1946 CG LYS A1047 14198 22826 13022 2145 304 558 C ATOM 1947 CD LYS A1047 183.407 15.244 578.896 1.00131.25 C ANISOU 1947 CD LYS A1047 14099 22806 12966 2319 31 851 C ATOM 1948 CE LYS A1047 181.899 15.130 578.811 1.00131.21 C ANISOU 1948 CE LYS A1047 14399 22699 12757 2200 -43 1040 C ATOM 1949 NZ LYS A1047 181.259 16.450 578.548 1.00130.42 N ANISOU 1949 NZ LYS A1047 14448 22719 12388 1989 -15 938 N ATOM 1950 N LEU A1048 187.366 18.653 577.873 1.00146.57 N ANISOU 1950 N LEU A1048 15227 25430 15033 1825 417 144 N ATOM 1951 CA LEU A1048 188.611 19.229 578.354 1.00156.19 C ANISOU 1951 CA LEU A1048 16061 26904 16379 1794 354 83 C ATOM 1952 C LEU A1048 189.180 18.392 579.494 1.00165.27 C ANISOU 1952 C LEU A1048 16924 28140 17731 2156 190 152 C ATOM 1953 O LEU A1048 188.443 17.792 580.281 1.00165.81 O ANISOU 1953 O LEU A1048 17123 28114 17765 2361 9 314 O ATOM 1954 CB LEU A1048 188.399 20.670 578.822 1.00153.74 C ANISOU 1954 CB LEU A1048 15835 26661 15919 1548 104 112 C ATOM 1955 CG LEU A1048 188.311 21.773 577.761 1.00151.50 C ANISOU 1955 CG LEU A1048 15735 26331 15499 1119 186 50 C ATOM 1956 CD1 LEU A1048 187.094 21.600 576.861 1.00148.46 C ANISOU 1956 CD1 LEU A1048 15776 25705 14927 1027 317 59 C ATOM 1957 CD2 LEU A1048 188.287 23.141 578.424 1.00149.96 C ANISOU 1957 CD2 LEU A1048 15586 26160 15233 940 -180 61 C ATOM 1958 N GLU A1049 190.512 18.351 579.562 1.00174.21 N ANISOU 1958 N GLU A1049 17645 29481 19067 2214 245 46 N ATOM 1959 CA GLU A1049 191.303 17.639 580.566 1.00180.27 C ANISOU 1959 CA GLU A1049 18081 30351 20063 2547 78 80 C ATOM 1960 C GLU A1049 191.225 16.122 580.436 1.00182.02 C ANISOU 1960 C GLU A1049 18325 30379 20456 2894 124 83 C ATOM 1961 O GLU A1049 191.804 15.413 581.270 1.00185.12 O ANISOU 1961 O GLU A1049 18485 30798 21053 3193 -62 134 O ATOM 1962 CB GLU A1049 190.918 18.047 581.995 1.00183.64 C ANISOU 1962 CB GLU A1049 18540 30836 20397 2627 -290 256 C ATOM 1963 CG GLU A1049 191.063 19.536 582.278 1.00187.15 C ANISOU 1963 CG GLU A1049 18967 31431 20712 2352 -448 215 C ATOM 1964 CD GLU A1049 192.338 20.121 581.698 1.00193.19 C ANISOU 1964 CD GLU A1049 19391 32379 21634 2133 -321 75 C ATOM 1965 OE1 GLU A1049 192.270 20.744 580.617 1.00194.10 O ANISOU 1965 OE1 GLU A1049 19617 32473 21659 1799 -125 9 O ATOM 1966 OE2 GLU A1049 193.409 19.953 582.318 1.00196.96 O ANISOU 1966 OE2 GLU A1049 19475 33044 22316 2278 -424 51 O ATOM 1967 N ASP A1050 190.547 15.604 579.410 1.00176.84 N ANISOU 1967 N ASP A1050 17954 29501 19736 2864 323 24 N ATOM 1968 CA ASP A1050 190.449 14.166 579.150 1.00171.88 C ANISOU 1968 CA ASP A1050 17398 28618 19292 3184 319 -6 C ATOM 1969 C ASP A1050 190.022 13.408 580.407 1.00162.68 C ANISOU 1969 C ASP A1050 16295 27301 18215 3412 -42 276 C ATOM 1970 O ASP A1050 190.727 12.539 580.922 1.00163.90 O ANISOU 1970 O ASP A1050 16232 27413 18628 3725 -209 278 O ATOM 1971 CB ASP A1050 191.770 13.620 578.600 1.00177.13 C ANISOU 1971 CB ASP A1050 17676 29428 20197 3422 485 -299 C ATOM 1972 CG ASP A1050 192.142 14.230 577.262 1.00178.93 C ANISOU 1972 CG ASP A1050 17831 29871 20285 3183 872 -549 C ATOM 1973 OD1 ASP A1050 191.228 14.667 576.532 1.00176.53 O ANISOU 1973 OD1 ASP A1050 17886 29445 19743 2906 1005 -515 O ATOM 1974 OD2 ASP A1050 193.348 14.268 576.939 1.00182.88 O ANISOU 1974 OD2 ASP A1050 17896 30694 20896 3263 1039 -766 O ATOM 1975 N LYS A1051 188.838 13.761 580.896 1.00152.83 N ANISOU 1975 N LYS A1051 15337 26001 16730 3245 -174 526 N ATOM 1976 CA LYS A1051 188.372 13.278 582.186 1.00145.32 C ANISOU 1976 CA LYS A1051 14412 25044 15759 3376 -506 850 C ATOM 1977 C LYS A1051 187.738 11.895 582.066 1.00139.98 C ANISOU 1977 C LYS A1051 13964 24010 15211 3519 -641 1035 C ATOM 1978 O LYS A1051 187.220 11.511 581.013 1.00135.24 O ANISOU 1978 O LYS A1051 13614 23151 14621 3457 -491 939 O ATOM 1979 CB LYS A1051 187.376 14.273 582.783 1.00142.42 C ANISOU 1979 CB LYS A1051 14205 24867 15040 3160 -591 1015 C ATOM 1980 CG LYS A1051 187.885 15.709 582.789 1.00142.11 C ANISOU 1980 CG LYS A1051 14023 25087 14884 2989 -525 817 C ATOM 1981 CD LYS A1051 186.798 16.699 583.180 1.00140.15 C ANISOU 1981 CD LYS A1051 13989 24971 14290 2819 -629 895 C ATOM 1982 CE LYS A1051 186.462 16.609 584.659 1.00140.49 C ANISOU 1982 CE LYS A1051 13946 25256 14176 2983 -932 1128 C ATOM 1983 NZ LYS A1051 185.370 17.548 585.037 1.00137.36 N ANISOU 1983 NZ LYS A1051 13728 25051 13413 2886 -1037 1147 N ATOM 1984 N SER A1052 187.787 11.146 583.168 1.00140.54 N ANISOU 1984 N SER A1052 13959 24059 15382 3694 -967 1319 N ATOM 1985 CA SER A1052 187.275 9.786 583.217 1.00138.91 C ANISOU 1985 CA SER A1052 13956 23483 15340 3807 -1204 1564 C ATOM 1986 C SER A1052 185.749 9.791 583.130 1.00131.96 C ANISOU 1986 C SER A1052 13415 22534 14189 3541 -1222 1850 C ATOM 1987 O SER A1052 185.113 10.839 583.260 1.00121.27 O ANISOU 1987 O SER A1052 12101 21466 12508 3328 -1091 1869 O ATOM 1988 CB SER A1052 187.747 9.102 584.500 1.00129.98 C ANISOU 1988 CB SER A1052 12646 22386 14355 4010 -1586 1851 C ATOM 1989 OG SER A1052 187.240 9.758 585.649 1.00128.40 O ANISOU 1989 OG SER A1052 12391 22566 13831 3866 -1705 2146 O ATOM 1990 N PRO A1053 185.127 8.630 582.893 1.00131.28 N ANISOU 1990 N PRO A1053 13574 22061 14245 3552 -1415 2067 N ATOM 1991 CA PRO A1053 183.655 8.583 582.900 1.00131.56 C ANISOU 1991 CA PRO A1053 13884 22077 14027 3273 -1464 2394 C ATOM 1992 C PRO A1053 183.036 8.939 584.242 1.00136.53 C ANISOU 1992 C PRO A1053 14401 23134 14339 3146 -1637 2808 C ATOM 1993 O PRO A1053 181.876 9.368 584.275 1.00136.45 O ANISOU 1993 O PRO A1053 14515 23316 14012 2915 -1577 2980 O ATOM 1994 CB PRO A1053 183.344 7.131 582.504 1.00130.32 C ANISOU 1994 CB PRO A1053 13971 21380 14164 3330 -1734 2571 C ATOM 1995 CG PRO A1053 184.618 6.376 582.733 1.00132.17 C ANISOU 1995 CG PRO A1053 14028 21410 14779 3680 -1935 2433 C ATOM 1996 CD PRO A1053 185.709 7.354 582.443 1.00131.91 C ANISOU 1996 CD PRO A1053 13708 21679 14731 3816 -1601 1970 C ATOM 1997 N ASP A1054 183.765 8.778 585.348 1.00143.59 N ANISOU 1997 N ASP A1054 15048 24222 15285 3307 -1854 2959 N ATOM 1998 CA ASP A1054 183.257 9.164 586.661 1.00145.99 C ANISOU 1998 CA ASP A1054 15216 25022 15231 3217 -2008 3317 C ATOM 1999 C ASP A1054 183.267 10.669 586.886 1.00144.55 C ANISOU 1999 C ASP A1054 14894 25308 14721 3190 -1789 3045 C ATOM 2000 O ASP A1054 182.779 11.123 587.927 1.00147.05 O ANISOU 2000 O ASP A1054 15096 26097 14679 3153 -1898 3260 O ATOM 2001 CB ASP A1054 184.071 8.486 587.765 1.00153.07 C ANISOU 2001 CB ASP A1054 15913 25964 16284 3404 -2345 3566 C ATOM 2002 CG ASP A1054 183.824 6.992 587.841 1.00159.79 C ANISOU 2002 CG ASP A1054 16931 26385 17397 3385 -2698 3974 C ATOM 2003 OD1 ASP A1054 183.253 6.430 586.883 1.00160.95 O ANISOU 2003 OD1 ASP A1054 17343 26116 17695 3282 -2671 3964 O ATOM 2004 OD2 ASP A1054 184.195 6.380 588.866 1.00163.86 O ANISOU 2004 OD2 ASP A1054 17330 26959 17970 3463 -3044 4317 O ATOM 2005 N SER A1055 183.799 11.445 585.946 1.00140.98 N ANISOU 2005 N SER A1055 14449 24752 14366 3204 -1515 2585 N ATOM 2006 CA SER A1055 183.978 12.870 586.150 1.00134.66 C ANISOU 2006 CA SER A1055 13529 24308 13327 3176 -1392 2318 C ATOM 2007 C SER A1055 182.635 13.597 586.183 1.00129.40 C ANISOU 2007 C SER A1055 13021 23893 12254 3000 -1339 2384 C ATOM 2008 O SER A1055 181.644 13.128 585.615 1.00128.30 O ANISOU 2008 O SER A1055 13100 23584 12063 2853 -1284 2536 O ATOM 2009 CB SER A1055 184.849 13.452 585.044 1.00129.66 C ANISOU 2009 CB SER A1055 12876 23483 12906 3165 -1135 1876 C ATOM 2010 OG SER A1055 184.224 13.316 583.780 1.00125.54 O ANISOU 2010 OG SER A1055 12625 22666 12407 3012 -922 1768 O ATOM 2011 N PRO A1056 182.578 14.751 586.853 1.00134.66 N ANISOU 2011 N PRO A1056 13312 25295 12557 4248 -1734 3038 N ATOM 2012 CA PRO A1056 181.354 15.567 586.806 1.00132.79 C ANISOU 2012 CA PRO A1056 12515 25531 12408 4056 -1977 3251 C ATOM 2013 C PRO A1056 181.025 16.080 585.416 1.00131.01 C ANISOU 2013 C PRO A1056 12297 25092 12388 3496 -2003 3559 C ATOM 2014 O PRO A1056 179.866 16.428 585.160 1.00131.95 O ANISOU 2014 O PRO A1056 12156 25573 12407 3130 -2164 3868 O ATOM 2015 CB PRO A1056 181.664 16.721 587.770 1.00133.76 C ANISOU 2015 CB PRO A1056 11816 25879 13127 4842 -2205 2755 C ATOM 2016 CG PRO A1056 182.762 16.207 588.652 1.00132.50 C ANISOU 2016 CG PRO A1056 11843 25575 12928 5439 -2080 2345 C ATOM 2017 CD PRO A1056 183.578 15.301 587.784 1.00131.80 C ANISOU 2017 CD PRO A1056 12548 24873 12656 5075 -1790 2482 C ATOM 2018 N GLU A1057 182.005 16.145 584.513 1.00129.03 N ANISOU 2018 N GLU A1057 12313 24306 12408 3433 -1848 3503 N ATOM 2019 CA GLU A1057 181.738 16.596 583.152 1.00128.89 C ANISOU 2019 CA GLU A1057 12302 24149 12523 2922 -1848 3847 C ATOM 2020 C GLU A1057 181.086 15.498 582.317 1.00125.85 C ANISOU 2020 C GLU A1057 12604 23800 11413 2179 -1723 4245 C ATOM 2021 O GLU A1057 180.184 15.776 581.519 1.00126.83 O ANISOU 2021 O GLU A1057 12638 24131 11421 1684 -1823 4610 O ATOM 2022 CB GLU A1057 183.034 17.073 582.494 1.00123.77 C ANISOU 2022 CB GLU A1057 11636 22977 12413 3155 -1712 3677 C ATOM 2023 N MET A1058 181.529 14.249 582.488 1.00127.84 N ANISOU 2023 N MET A1058 13521 23842 11211 2102 -1525 4164 N ATOM 2024 CA MET A1058 180.926 13.139 581.754 1.00128.87 C ANISOU 2024 CA MET A1058 14281 23962 10720 1421 -1440 4471 C ATOM 2025 C MET A1058 179.540 12.805 582.292 1.00130.67 C ANISOU 2025 C MET A1058 14404 24662 10581 1123 -1596 4756 C ATOM 2026 O MET A1058 178.636 12.463 581.521 1.00134.30 O ANISOU 2026 O MET A1058 15064 25255 10711 507 -1650 5085 O ATOM 2027 CB MET A1058 181.833 11.910 581.820 1.00128.85 C ANISOU 2027 CB MET A1058 14968 23543 10445 1454 -1208 4274 C ATOM 2028 CG MET A1058 183.018 11.946 580.869 1.00129.07 C ANISOU 2028 CG MET A1058 15280 23111 10649 1497 -1020 4094 C ATOM 2029 SD MET A1058 182.557 11.647 579.151 1.00130.93 S ANISOU 2029 SD MET A1058 15893 23346 10509 747 -982 4403 S ATOM 2030 CE MET A1058 181.826 10.018 579.281 1.00133.44 C ANISOU 2030 CE MET A1058 16866 23651 10185 237 -978 4500 C ATOM 2031 N LYS A1059 179.359 12.888 583.612 1.00131.18 N ANISOU 2031 N LYS A1059 14138 25019 10685 1567 -1671 4634 N ATOM 2032 CA LYS A1059 178.068 12.564 584.212 1.00131.97 C ANISOU 2032 CA LYS A1059 14093 25617 10432 1331 -1796 4933 C ATOM 2033 C LYS A1059 176.995 13.556 583.782 1.00134.35 C ANISOU 2033 C LYS A1059 13868 26295 10882 1075 -2024 5159 C ATOM 2034 O LYS A1059 175.896 13.163 583.371 1.00132.38 O ANISOU 2034 O LYS A1059 13743 26266 10291 503 -2095 5526 O ATOM 2035 CB LYS A1059 178.195 12.534 585.734 1.00131.87 C ANISOU 2035 CB LYS A1059 13768 25924 10414 1956 -1816 4739 C ATOM 2036 CG LYS A1059 178.689 11.212 586.290 1.00133.95 C ANISOU 2036 CG LYS A1059 14583 25988 10322 2015 -1616 4751 C ATOM 2037 CD LYS A1059 178.959 11.317 587.781 1.00136.26 C ANISOU 2037 CD LYS A1059 14502 26652 10618 2736 -1632 4537 C ATOM 2038 CE LYS A1059 179.021 9.945 588.428 1.00140.59 C ANISOU 2038 CE LYS A1059 15509 27174 10734 2694 -1464 4756 C ATOM 2039 NZ LYS A1059 177.684 9.291 588.449 1.00144.30 N ANISOU 2039 NZ LYS A1059 16039 27978 10809 2131 -1504 5303 N ATOM 2040 N ASP A1060 177.296 14.853 583.872 1.00129.38 N ANISOU 2040 N ASP A1060 12621 25719 10817 1498 -2158 4939 N ATOM 2041 CA ASP A1060 176.329 15.867 583.471 1.00129.73 C ANISOU 2041 CA ASP A1060 12113 26086 11094 1291 -2392 5148 C ATOM 2042 C ASP A1060 176.139 15.893 581.959 1.00134.41 C ANISOU 2042 C ASP A1060 12986 26469 11615 676 -2363 5464 C ATOM 2043 O ASP A1060 175.087 16.328 581.476 1.00131.23 O ANISOU 2043 O ASP A1060 12325 26362 11175 290 -2534 5772 O ATOM 2044 CB ASP A1060 176.769 17.238 583.987 1.00128.58 C ANISOU 2044 CB ASP A1060 11191 25987 11679 1938 -2565 4800 C ATOM 2045 CG ASP A1060 177.374 18.103 582.904 1.00127.90 C ANISOU 2045 CG ASP A1060 10938 25513 12144 1888 -2571 4829 C ATOM 2046 OD1 ASP A1060 176.690 19.041 582.447 1.00130.86 O ANISOU 2046 OD1 ASP A1060 10811 26063 12849 1725 -2773 5034 O ATOM 2047 OD2 ASP A1060 178.523 17.837 582.498 1.00131.16 O ANISOU 2047 OD2 ASP A1060 11708 25461 12668 2008 -2369 4682 O ATOM 2048 N PHE A1061 177.142 15.442 581.200 1.00129.88 N ANISOU 2048 N PHE A1061 12916 25430 11004 601 -2153 5385 N ATOM 2049 CA PHE A1061 176.986 15.306 579.754 1.00131.01 C ANISOU 2049 CA PHE A1061 13377 25455 10945 33 -2103 5672 C ATOM 2050 C PHE A1061 175.936 14.255 579.418 1.00133.06 C ANISOU 2050 C PHE A1061 14092 25906 10559 -612 -2127 5952 C ATOM 2051 O PHE A1061 175.056 14.483 578.579 1.00135.06 O ANISOU 2051 O PHE A1061 14270 26387 10661 -1091 -2253 6264 O ATOM 2052 CB PHE A1061 178.333 14.954 579.116 1.00130.54 C ANISOU 2052 CB PHE A1061 13760 24907 10930 149 -1856 5479 C ATOM 2053 CG PHE A1061 178.252 14.624 577.651 1.00132.28 C ANISOU 2053 CG PHE A1061 14375 25071 10814 -397 -1778 5725 C ATOM 2054 CD1 PHE A1061 178.278 13.307 577.222 1.00133.81 C ANISOU 2054 CD1 PHE A1061 15286 25120 10435 -780 -1651 5690 C ATOM 2055 CD2 PHE A1061 178.157 15.630 576.703 1.00135.28 C ANISOU 2055 CD2 PHE A1061 14374 25562 11466 -505 -1843 5985 C ATOM 2056 CE1 PHE A1061 178.206 12.998 575.875 1.00136.27 C ANISOU 2056 CE1 PHE A1061 15929 25443 10403 -1238 -1601 5843 C ATOM 2057 CE2 PHE A1061 178.085 15.327 575.354 1.00134.92 C ANISOU 2057 CE2 PHE A1061 14662 25562 11039 -965 -1769 6214 C ATOM 2058 CZ PHE A1061 178.110 14.009 574.941 1.00136.46 C ANISOU 2058 CZ PHE A1061 15575 25657 10616 -1319 -1653 6108 C ATOM 2059 N ARG A1062 176.021 13.089 580.063 1.00133.60 N ANISOU 2059 N ARG A1062 14612 25871 10279 -628 -2018 5854 N ATOM 2060 CA ARG A1062 174.999 12.064 579.882 1.00135.96 C ANISOU 2060 CA ARG A1062 15276 26310 10074 -1215 -2063 6119 C ATOM 2061 C ARG A1062 173.649 12.521 580.419 1.00136.64 C ANISOU 2061 C ARG A1062 14858 26921 10137 -1347 -2283 6390 C ATOM 2062 O ARG A1062 172.607 12.163 579.858 1.00138.64 O ANISOU 2062 O ARG A1062 15224 27312 10142 -1915 -2378 6649 O ATOM 2063 CB ARG A1062 175.425 10.765 580.570 1.00136.72 C ANISOU 2063 CB ARG A1062 15879 26146 9923 -1149 -1904 5997 C ATOM 2064 CG ARG A1062 176.711 10.154 580.044 1.00137.77 C ANISOU 2064 CG ARG A1062 16559 25743 10042 -1058 -1691 5710 C ATOM 2065 CD ARG A1062 177.057 8.897 580.827 1.00139.29 C ANISOU 2065 CD ARG A1062 17188 25682 10054 -976 -1562 5625 C ATOM 2066 NE ARG A1062 178.285 8.264 580.356 1.00139.54 N ANISOU 2066 NE ARG A1062 17746 25186 10086 -883 -1368 5321 N ATOM 2067 CZ ARG A1062 178.823 7.182 580.908 1.00141.60 C ANISOU 2067 CZ ARG A1062 18421 25119 10261 -777 -1240 5202 C ATOM 2068 NH1 ARG A1062 178.243 6.610 581.955 1.00143.58 N ANISOU 2068 NH1 ARG A1062 18607 25535 10410 -748 -1273 5415 N ATOM 2069 NH2 ARG A1062 179.943 6.672 580.415 1.00142.08 N ANISOU 2069 NH2 ARG A1062 18935 24703 10345 -689 -1075 4897 N ATOM 2070 N HIS A1063 173.647 13.305 581.501 1.00135.26 N ANISOU 2070 N HIS A1063 14110 27012 10272 -807 -2362 6265 N ATOM 2071 CA HIS A1063 172.391 13.742 582.103 1.00136.11 C ANISOU 2071 CA HIS A1063 13704 27624 10387 -872 -2551 6453 C ATOM 2072 C HIS A1063 171.619 14.667 581.170 1.00140.24 C ANISOU 2072 C HIS A1063 13887 28251 11146 -1214 -2708 6614 C ATOM 2073 O HIS A1063 170.385 14.614 581.116 1.00137.97 O ANISOU 2073 O HIS A1063 13473 28122 10827 -1599 -2765 6769 O ATOM 2074 CB HIS A1063 172.662 14.429 583.440 1.00134.92 C ANISOU 2074 CB HIS A1063 12977 27759 10526 -143 -2610 6186 C ATOM 2075 CG HIS A1063 171.422 14.725 584.224 1.00136.20 C ANISOU 2075 CG HIS A1063 12685 28282 10785 -159 -2668 6209 C ATOM 2076 ND1 HIS A1063 170.456 13.774 584.473 1.00138.47 N ANISOU 2076 ND1 HIS A1063 13209 28654 10751 -576 -2583 6450 N ATOM 2077 CD2 HIS A1063 170.989 15.865 584.813 1.00135.87 C ANISOU 2077 CD2 HIS A1063 11965 28497 11162 194 -2781 5997 C ATOM 2078 CE1 HIS A1063 169.482 14.314 585.184 1.00139.39 C ANISOU 2078 CE1 HIS A1063 12802 29144 11015 -473 -2637 6435 C ATOM 2079 NE2 HIS A1063 169.781 15.581 585.405 1.00137.83 N ANISOU 2079 NE2 HIS A1063 12077 29043 11249 -10 -2744 6132 N ATOM 2080 N GLY A1064 172.329 15.523 580.432 1.00135.18 N ANISOU 2080 N GLY A1064 13068 27511 10783 -1066 -2767 6602 N ATOM 2081 CA GLY A1064 171.663 16.376 579.462 1.00135.94 C ANISOU 2081 CA GLY A1064 12853 27704 11095 -1398 -2906 6828 C ATOM 2082 C GLY A1064 170.948 15.585 578.383 1.00138.04 C ANISOU 2082 C GLY A1064 13617 27864 10967 -2112 -2844 7030 C ATOM 2083 O GLY A1064 169.842 15.941 577.970 1.00139.34 O ANISOU 2083 O GLY A1064 13547 28186 11208 -2469 -2949 7193 O ATOM 2084 N PHE A1065 171.570 14.502 577.912 1.00138.72 N ANISOU 2084 N PHE A1065 14379 27665 10665 -2305 -2682 6970 N ATOM 2085 CA PHE A1065 170.917 13.638 576.936 1.00142.17 C ANISOU 2085 CA PHE A1065 15280 27972 10767 -2931 -2656 7045 C ATOM 2086 C PHE A1065 169.751 12.876 577.554 1.00143.01 C ANISOU 2086 C PHE A1065 15437 28154 10749 -3224 -2705 7091 C ATOM 2087 O PHE A1065 168.751 12.620 576.873 1.00145.27 O ANISOU 2087 O PHE A1065 15776 28490 10928 -3721 -2797 7211 O ATOM 2088 CB PHE A1065 171.931 12.664 576.332 1.00143.12 C ANISOU 2088 CB PHE A1065 16077 27760 10543 -3012 -2486 6900 C ATOM 2089 CG PHE A1065 172.822 13.281 575.296 1.00141.61 C ANISOU 2089 CG PHE A1065 15891 27528 10385 -2919 -2424 6931 C ATOM 2090 CD1 PHE A1065 173.929 14.025 575.665 1.00139.21 C ANISOU 2090 CD1 PHE A1065 15335 27128 10430 -2367 -2338 6839 C ATOM 2091 CD2 PHE A1065 172.549 13.120 573.949 1.00144.06 C ANISOU 2091 CD2 PHE A1065 16417 27840 10480 -3339 -2427 6990 C ATOM 2092 CE1 PHE A1065 174.749 14.596 574.707 1.00139.27 C ANISOU 2092 CE1 PHE A1065 15303 27014 10601 -2264 -2232 6864 C ATOM 2093 CE2 PHE A1065 173.363 13.686 572.988 1.00144.24 C ANISOU 2093 CE2 PHE A1065 16410 27881 10516 -3234 -2340 7067 C ATOM 2094 CZ PHE A1065 174.465 14.425 573.367 1.00146.51 C ANISOU 2094 CZ PHE A1065 16441 28091 11134 -2717 -2243 7072 C ATOM 2095 N ASP A1066 169.858 12.506 578.833 1.00147.58 N ANISOU 2095 N ASP A1066 15966 28771 11335 -2909 -2648 7022 N ATOM 2096 CA ASP A1066 168.768 11.792 579.494 1.00144.29 C ANISOU 2096 CA ASP A1066 15537 28467 10820 -3156 -2676 7143 C ATOM 2097 C ASP A1066 167.531 12.676 579.608 1.00144.67 C ANISOU 2097 C ASP A1066 14991 28876 11100 -3273 -2825 7284 C ATOM 2098 O ASP A1066 166.412 12.239 579.314 1.00147.02 O ANISOU 2098 O ASP A1066 15315 29243 11304 -3750 -2901 7450 O ATOM 2099 CB ASP A1066 169.222 11.303 580.872 1.00149.29 C ANISOU 2099 CB ASP A1066 16179 29130 11415 -2717 -2558 7075 C ATOM 2100 CG ASP A1066 168.265 10.291 581.482 1.00152.92 C ANISOU 2100 CG ASP A1066 16730 29650 11724 -3006 -2544 7280 C ATOM 2101 OD1 ASP A1066 167.230 9.977 580.855 1.00156.58 O ANISOU 2101 OD1 ASP A1066 17236 30128 12128 -3552 -2649 7457 O ATOM 2102 OD2 ASP A1066 168.553 9.802 582.594 1.00152.89 O ANISOU 2102 OD2 ASP A1066 16728 29698 11665 -2676 -2434 7290 O ATOM 2103 N ILE A1067 167.715 13.927 580.037 1.00142.60 N ANISOU 2103 N ILE A1067 14168 28846 11166 -2834 -2882 7210 N ATOM 2104 CA ILE A1067 166.602 14.870 580.091 1.00142.99 C ANISOU 2104 CA ILE A1067 13643 29211 11476 -2922 -3014 7317 C ATOM 2105 C ILE A1067 166.070 15.154 578.693 1.00144.65 C ANISOU 2105 C ILE A1067 13905 29364 11689 -3430 -3111 7488 C ATOM 2106 O ILE A1067 164.862 15.352 578.506 1.00145.70 O ANISOU 2106 O ILE A1067 13802 29687 11870 -3767 -3203 7642 O ATOM 2107 CB ILE A1067 167.040 16.164 580.809 1.00140.85 C ANISOU 2107 CB ILE A1067 12773 29117 11627 -2300 -3064 7131 C ATOM 2108 CG1 ILE A1067 167.463 15.860 582.248 1.00147.96 C ANISOU 2108 CG1 ILE A1067 13584 30144 12490 -1763 -2970 6912 C ATOM 2109 CG2 ILE A1067 165.925 17.202 580.790 1.00145.62 C ANISOU 2109 CG2 ILE A1067 12825 29955 12548 -2386 -3174 7201 C ATOM 2110 CD1 ILE A1067 167.860 17.087 583.039 1.00144.75 C ANISOU 2110 CD1 ILE A1067 12590 29861 12550 -1099 -3025 6588 C ATOM 2111 N LEU A1068 166.953 15.171 577.691 1.00144.37 N ANISOU 2111 N LEU A1068 14169 29100 11585 -3479 -3082 7469 N ATOM 2112 CA LEU A1068 166.511 15.390 576.318 1.00146.18 C ANISOU 2112 CA LEU A1068 14456 29321 11763 -3925 -3157 7625 C ATOM 2113 C LEU A1068 165.583 14.273 575.855 1.00148.33 C ANISOU 2113 C LEU A1068 15113 29548 11699 -4495 -3193 7675 C ATOM 2114 O LEU A1068 164.565 14.533 575.202 1.00150.11 O ANISOU 2114 O LEU A1068 15160 29933 11944 -4870 -3313 7825 O ATOM 2115 CB LEU A1068 167.721 15.506 575.390 1.00145.28 C ANISOU 2115 CB LEU A1068 14610 29010 11581 -3823 -3077 7593 C ATOM 2116 CG LEU A1068 167.455 16.034 573.979 1.00146.62 C ANISOU 2116 CG LEU A1068 14701 29258 11751 -4135 -3139 7782 C ATOM 2117 CD1 LEU A1068 167.045 17.499 574.022 1.00145.86 C ANISOU 2117 CD1 LEU A1068 13889 29395 12137 -3976 -3260 8001 C ATOM 2118 CD2 LEU A1068 168.674 15.840 573.091 1.00146.83 C ANISOU 2118 CD2 LEU A1068 15096 29103 11589 -4050 -3008 7735 C ATOM 2119 N VAL A1069 165.916 13.023 576.185 1.00149.48 N ANISOU 2119 N VAL A1069 15765 29473 11557 -4564 -3106 7565 N ATOM 2120 CA VAL A1069 165.041 11.906 575.844 1.00152.38 C ANISOU 2120 CA VAL A1069 16458 29788 11650 -5098 -3180 7634 C ATOM 2121 C VAL A1069 163.736 11.986 576.627 1.00155.08 C ANISOU 2121 C VAL A1069 16395 30402 12128 -5240 -3271 7816 C ATOM 2122 O VAL A1069 162.675 11.597 576.123 1.00156.98 O ANISOU 2122 O VAL A1069 16650 30730 12265 -5730 -3405 7951 O ATOM 2123 CB VAL A1069 165.767 10.568 576.084 1.00153.30 C ANISOU 2123 CB VAL A1069 17178 29589 11479 -5123 -3073 7519 C ATOM 2124 CG1 VAL A1069 164.848 9.393 575.789 1.00157.14 C ANISOU 2124 CG1 VAL A1069 17954 30031 11721 -5697 -3194 7636 C ATOM 2125 CG2 VAL A1069 167.022 10.485 575.229 1.00152.67 C ANISOU 2125 CG2 VAL A1069 17501 29273 11234 -5006 -2972 7325 C ATOM 2126 N GLY A1070 163.785 12.497 577.860 1.00151.41 N ANISOU 2126 N GLY A1070 15541 30112 11877 -4805 -3206 7814 N ATOM 2127 CA GLY A1070 162.565 12.643 578.639 1.00152.51 C ANISOU 2127 CA GLY A1070 15250 30570 12128 -4891 -3264 7982 C ATOM 2128 C GLY A1070 161.575 13.591 577.992 1.00155.44 C ANISOU 2128 C GLY A1070 15206 31171 12681 -5139 -3399 8101 C ATOM 2129 O GLY A1070 160.385 13.286 577.880 1.00155.41 O ANISOU 2129 O GLY A1070 15098 31322 12629 -5553 -3497 8278 O ATOM 2130 N GLN A1071 162.055 14.760 577.558 1.00153.25 N ANISOU 2130 N GLN A1071 14671 30918 12638 -4892 -3410 8037 N ATOM 2131 CA GLN A1071 161.196 15.689 576.832 1.00151.73 C ANISOU 2131 CA GLN A1071 14115 30902 12635 -5127 -3522 8186 C ATOM 2132 C GLN A1071 160.797 15.135 575.470 1.00154.29 C ANISOU 2132 C GLN A1071 14776 31134 12715 -5682 -3624 8275 C ATOM 2133 O GLN A1071 159.718 15.463 574.962 1.00156.02 O ANISOU 2133 O GLN A1071 14768 31531 12982 -6024 -3734 8436 O ATOM 2134 CB GLN A1071 161.898 17.037 576.667 1.00149.47 C ANISOU 2134 CB GLN A1071 13480 30618 12695 -4722 -3511 8149 C ATOM 2135 CG GLN A1071 162.305 17.703 577.968 1.00147.29 C ANISOU 2135 CG GLN A1071 12838 30426 12699 -4116 -3445 7978 C ATOM 2136 CD GLN A1071 163.157 18.935 577.739 1.00145.44 C ANISOU 2136 CD GLN A1071 12311 30082 12867 -3705 -3465 7910 C ATOM 2137 OE1 GLN A1071 163.372 19.738 578.648 1.00144.10 O ANISOU 2137 OE1 GLN A1071 11781 29921 13048 -3194 -3454 7702 O ATOM 2138 NE2 GLN A1071 163.653 19.089 576.517 1.00145.78 N ANISOU 2138 NE2 GLN A1071 12506 29996 12887 -3903 -3496 8059 N ATOM 2139 N ILE A1072 161.654 14.310 574.863 1.00154.82 N ANISOU 2139 N ILE A1072 15385 30936 12503 -5757 -3584 8149 N ATOM 2140 CA ILE A1072 161.318 13.691 573.583 1.00161.11 C ANISOU 2140 CA ILE A1072 16532 31677 13006 -6245 -3684 8166 C ATOM 2141 C ILE A1072 160.115 12.772 573.738 1.00165.09 C ANISOU 2141 C ILE A1072 17120 32260 13347 -6718 -3810 8271 C ATOM 2142 O ILE A1072 159.181 12.801 572.928 1.00167.76 O ANISOU 2142 O ILE A1072 17383 32750 13610 -7131 -3960 8379 O ATOM 2143 CB ILE A1072 162.540 12.940 573.018 1.00158.01 C ANISOU 2143 CB ILE A1072 16720 30997 12320 -6180 -3590 7967 C ATOM 2144 CG1 ILE A1072 163.463 13.903 572.269 1.00156.57 C ANISOU 2144 CG1 ILE A1072 16428 30815 12245 -5901 -3518 7955 C ATOM 2145 CG2 ILE A1072 162.106 11.796 572.109 1.00161.90 C ANISOU 2145 CG2 ILE A1072 17673 31430 12411 -6699 -3705 7920 C ATOM 2146 CD1 ILE A1072 164.691 13.240 571.683 1.00156.88 C ANISOU 2146 CD1 ILE A1072 17009 30612 11985 -5809 -3397 7759 C ATOM 2147 N ASP A1073 160.112 11.950 574.787 1.00160.87 N ANISOU 2147 N ASP A1073 16715 31647 12762 -6663 -3758 8277 N ATOM 2148 CA ASP A1073 159.010 11.027 575.022 1.00164.07 C ANISOU 2148 CA ASP A1073 17167 32130 13042 -7117 -3883 8452 C ATOM 2149 C ASP A1073 157.758 11.729 575.528 1.00165.65 C ANISOU 2149 C ASP A1073 16784 32674 13481 -7193 -3947 8659 C ATOM 2150 O ASP A1073 156.652 11.213 575.330 1.00168.81 O ANISOU 2150 O ASP A1073 17146 33198 13797 -7668 -4099 8841 O ATOM 2151 CB ASP A1073 159.446 9.940 576.007 1.00164.48 C ANISOU 2151 CB ASP A1073 17506 32003 12987 -7016 -3787 8474 C ATOM 2152 CG ASP A1073 160.334 8.895 575.360 1.00165.85 C ANISOU 2152 CG ASP A1073 18332 31830 12853 -7168 -3779 8325 C ATOM 2153 OD1 ASP A1073 159.829 8.132 574.513 1.00169.39 O ANISOU 2153 OD1 ASP A1073 19059 32238 13062 -7697 -3959 8365 O ATOM 2154 OD2 ASP A1073 161.538 8.853 575.680 1.00163.75 O ANISOU 2154 OD2 ASP A1073 18292 31352 12572 -6764 -3607 8155 O ATOM 2155 N ASP A1074 157.902 12.886 576.180 1.00161.40 N ANISOU 2155 N ASP A1074 15788 32304 13234 -6746 -3841 8638 N ATOM 2156 CA ASP A1074 156.729 13.700 576.477 1.00161.76 C ANISOU 2156 CA ASP A1074 15289 32678 13496 -6819 -3886 8807 C ATOM 2157 C ASP A1074 156.121 14.259 575.197 1.00165.36 C ANISOU 2157 C ASP A1074 15666 33191 13971 -7172 -4018 8883 C ATOM 2158 O ASP A1074 154.894 14.311 575.056 1.00165.18 O ANISOU 2158 O ASP A1074 15420 33371 13969 -7525 -4118 9066 O ATOM 2159 CB ASP A1074 157.093 14.830 577.440 1.00158.73 C ANISOU 2159 CB ASP A1074 14465 32444 13401 -6231 -3742 8726 C ATOM 2160 CG ASP A1074 157.388 14.333 578.843 1.00161.35 C ANISOU 2160 CG ASP A1074 14753 32858 13693 -5876 -3614 8684 C ATOM 2161 OD1 ASP A1074 157.528 13.107 579.031 1.00159.81 O ANISOU 2161 OD1 ASP A1074 14920 32530 13270 -6055 -3614 8739 O ATOM 2162 OD2 ASP A1074 157.472 15.173 579.764 1.00156.51 O ANISOU 2162 OD2 ASP A1074 13746 32446 13274 -5401 -3510 8597 O ATOM 2163 N ALA A1075 156.967 14.677 574.250 1.00162.11 N ANISOU 2163 N ALA A1075 15423 32630 13541 -7071 -4010 8770 N ATOM 2164 CA ALA A1075 156.469 15.147 572.962 1.00165.69 C ANISOU 2164 CA ALA A1075 15818 33171 13966 -7382 -4125 8864 C ATOM 2165 C ALA A1075 155.841 14.012 572.165 1.00172.08 C ANISOU 2165 C ALA A1075 16994 33966 14422 -7940 -4292 8878 C ATOM 2166 O ALA A1075 154.801 14.200 571.524 1.00175.27 O ANISOU 2166 O ALA A1075 17237 34555 14802 -8302 -4423 9020 O ATOM 2167 CB ALA A1075 157.601 15.796 572.166 1.00162.46 C ANISOU 2167 CB ALA A1075 15484 32649 13593 -7117 -4063 8785 C ATOM 2168 N LEU A1076 156.461 12.829 572.188 1.00172.05 N ANISOU 2168 N LEU A1076 17493 33741 14136 -8016 -4295 8733 N ATOM 2169 CA LEU A1076 155.900 11.684 571.477 1.00175.68 C ANISOU 2169 CA LEU A1076 18318 34181 14251 -8557 -4483 8735 C ATOM 2170 C LEU A1076 154.561 11.270 572.075 1.00179.19 C ANISOU 2170 C LEU A1076 18531 34794 14757 -8927 -4614 8971 C ATOM 2171 O LEU A1076 153.629 10.922 571.341 1.00181.97 O ANISOU 2171 O LEU A1076 18912 35274 14955 -9412 -4816 9062 O ATOM 2172 CB LEU A1076 156.891 10.518 571.502 1.00177.81 C ANISOU 2172 CB LEU A1076 19169 34156 14233 -8545 -4448 8550 C ATOM 2173 CG LEU A1076 156.902 9.520 570.337 1.00183.22 C ANISOU 2173 CG LEU A1076 20346 34785 14483 -8984 -4627 8417 C ATOM 2174 CD1 LEU A1076 158.153 8.659 570.399 1.00183.67 C ANISOU 2174 CD1 LEU A1076 20943 34537 14307 -8833 -4530 8200 C ATOM 2175 CD2 LEU A1076 155.661 8.640 570.324 1.00187.57 C ANISOU 2175 CD2 LEU A1076 20918 35441 14908 -9580 -4889 8593 C ATOM 2176 N LYS A1077 154.450 11.296 573.405 1.00179.98 N ANISOU 2176 N LYS A1077 18386 34932 15066 -8694 -4503 9082 N ATOM 2177 CA LYS A1077 153.184 10.978 574.057 1.00181.63 C ANISOU 2177 CA LYS A1077 18304 35358 15350 -9001 -4598 9356 C ATOM 2178 C LYS A1077 152.084 11.926 573.599 1.00176.07 C ANISOU 2178 C LYS A1077 17175 34925 14799 -9178 -4665 9489 C ATOM 2179 O LYS A1077 151.046 11.494 573.086 1.00179.54 O ANISOU 2179 O LYS A1077 17609 35480 15126 -9688 -4858 9646 O ATOM 2180 CB LYS A1077 153.350 11.034 575.578 1.00175.63 C ANISOU 2180 CB LYS A1077 17283 34675 14772 -8599 -4420 9439 C ATOM 2181 CG LYS A1077 152.038 10.982 576.353 1.00175.51 C ANISOU 2181 CG LYS A1077 16831 34982 14871 -8809 -4464 9748 C ATOM 2182 CD LYS A1077 152.272 11.127 577.851 1.00174.99 C ANISOU 2182 CD LYS A1077 16472 35077 14941 -8322 -4257 9803 C ATOM 2183 CE LYS A1077 150.959 11.195 578.618 1.00177.46 C ANISOU 2183 CE LYS A1077 16288 35787 15350 -8482 -4268 10116 C ATOM 2184 NZ LYS A1077 150.127 12.358 578.200 1.00176.70 N ANISOU 2184 NZ LYS A1077 15828 35904 15407 -8538 -4266 10128 N ATOM 2185 N LEU A1078 152.308 13.234 573.761 1.00173.21 N ANISOU 2185 N LEU A1078 16465 34652 14695 -8765 -4512 9443 N ATOM 2186 CA LEU A1078 151.310 14.222 573.365 1.00175.52 C ANISOU 2186 CA LEU A1078 16374 35166 15151 -8885 -4536 9596 C ATOM 2187 C LEU A1078 151.007 14.154 571.874 1.00179.74 C ANISOU 2187 C LEU A1078 17104 35697 15491 -9274 -4706 9592 C ATOM 2188 O LEU A1078 149.889 14.473 571.454 1.00181.51 O ANISOU 2188 O LEU A1078 17123 36103 15738 -9571 -4793 9767 O ATOM 2189 CB LEU A1078 151.786 15.622 573.753 1.00173.80 C ANISOU 2189 CB LEU A1078 15821 34978 15237 -8348 -4348 9548 C ATOM 2190 CG LEU A1078 152.049 15.820 575.249 1.00174.15 C ANISOU 2190 CG LEU A1078 15635 35090 15442 -7892 -4174 9508 C ATOM 2191 CD1 LEU A1078 152.928 17.033 575.495 1.00171.58 C ANISOU 2191 CD1 LEU A1078 15130 34693 15371 -7319 -4029 9366 C ATOM 2192 CD2 LEU A1078 150.742 15.948 576.012 1.00176.57 C ANISOU 2192 CD2 LEU A1078 15595 35680 15812 -8011 -4148 9715 C ATOM 2193 N ALA A1079 151.983 13.744 571.060 1.00182.20 N ANISOU 2193 N ALA A1079 17818 35829 15581 -9250 -4741 9392 N ATOM 2194 CA ALA A1079 151.719 13.560 569.638 1.00189.04 C ANISOU 2194 CA ALA A1079 18889 36758 16179 -9594 -4903 9359 C ATOM 2195 C ALA A1079 150.772 12.392 569.394 1.00197.16 C ANISOU 2195 C ALA A1079 20129 37839 16944 -10165 -5136 9420 C ATOM 2196 O ALA A1079 149.971 12.430 568.453 1.00201.22 O ANISOU 2196 O ALA A1079 20623 38519 17312 -10503 -5294 9477 O ATOM 2197 CB ALA A1079 153.030 13.352 568.879 1.00186.98 C ANISOU 2197 CB ALA A1079 19018 36334 15692 -9393 -4859 9118 C ATOM 2198 N ASN A1080 150.845 11.351 570.226 1.00201.12 N ANISOU 2198 N ASN A1080 20821 38212 17384 -10283 -5175 9437 N ATOM 2199 CA ASN A1080 149.941 10.214 570.104 1.00213.04 C ANISOU 2199 CA ASN A1080 22493 39761 18691 -10863 -5432 9566 C ATOM 2200 C ASN A1080 148.591 10.457 570.767 1.00219.90 C ANISOU 2200 C ASN A1080 22914 40855 19784 -11083 -5469 9891 C ATOM 2201 O ASN A1080 147.623 9.766 570.434 1.00225.17 O ANISOU 2201 O ASN A1080 23630 41610 20316 -11608 -5711 10044 O ATOM 2202 CB ASN A1080 150.586 8.959 570.698 1.00216.60 C ANISOU 2202 CB ASN A1080 23331 39975 18991 -10938 -5476 9532 C ATOM 2203 CG ASN A1080 151.410 8.191 569.683 1.00219.91 C ANISOU 2203 CG ASN A1080 24319 40216 19022 -11068 -5598 9239 C ATOM 2204 OD1 ASN A1080 152.526 8.585 569.343 1.00217.57 O ANISOU 2204 OD1 ASN A1080 24201 39804 18664 -10669 -5424 8994 O ATOM 2205 ND2 ASN A1080 150.865 7.082 569.197 1.00225.17 N ANISOU 2205 ND2 ASN A1080 25259 40877 19420 -11634 -5920 9258 N ATOM 2206 N GLU A1081 148.502 11.411 571.698 1.00178.56 N ANISOU 2206 N GLU A1081 16773 33053 18018 -6331 275 7252 N ATOM 2207 CA GLU A1081 147.225 11.723 572.329 1.00189.19 C ANISOU 2207 CA GLU A1081 17364 35774 18747 -6464 605 6902 C ATOM 2208 C GLU A1081 146.280 12.475 571.402 1.00188.74 C ANISOU 2208 C GLU A1081 16807 35980 18927 -5987 937 6259 C ATOM 2209 O GLU A1081 145.092 12.591 571.720 1.00198.18 O ANISOU 2209 O GLU A1081 17383 38191 19725 -6078 1126 5966 O ATOM 2210 CB GLU A1081 147.437 12.557 573.597 1.00193.73 C ANISOU 2210 CB GLU A1081 17649 37432 18526 -6294 949 6418 C ATOM 2211 CG GLU A1081 148.417 11.984 574.610 1.00195.62 C ANISOU 2211 CG GLU A1081 18304 37519 18502 -6689 655 6930 C ATOM 2212 CD GLU A1081 147.993 10.635 575.152 1.00203.48 C ANISOU 2212 CD GLU A1081 19338 38610 19366 -7513 215 7704 C ATOM 2213 OE1 GLU A1081 148.239 9.614 574.476 1.00201.49 O ANISOU 2213 OE1 GLU A1081 19552 37305 19699 -7779 -272 8292 O ATOM 2214 OE2 GLU A1081 147.412 10.595 576.257 1.00212.46 O ANISOU 2214 OE2 GLU A1081 20046 40873 19806 -7878 328 7689 O ATOM 2215 N GLY A1082 146.773 12.983 570.278 1.00178.28 N ANISOU 2215 N GLY A1082 16012 33393 18334 -5219 806 5770 N ATOM 2216 CA GLY A1082 146.012 13.879 569.437 1.00172.34 C ANISOU 2216 CA GLY A1082 15052 32568 17862 -4463 970 4874 C ATOM 2217 C GLY A1082 146.396 15.335 569.560 1.00165.88 C ANISOU 2217 C GLY A1082 14343 31809 16876 -3551 1221 3823 C ATOM 2218 O GLY A1082 145.721 16.188 568.973 1.00166.33 O ANISOU 2218 O GLY A1082 14227 31901 17071 -2878 1329 2997 O ATOM 2219 N LYS A1083 147.458 15.644 570.301 1.00159.20 N ANISOU 2219 N LYS A1083 13809 30943 15739 -3506 1265 3822 N ATOM 2220 CA LYS A1083 147.964 17.003 570.491 1.00150.42 C ANISOU 2220 CA LYS A1083 12888 29813 14452 -2707 1443 2886 C ATOM 2221 C LYS A1083 149.209 17.259 569.654 1.00139.00 C ANISOU 2221 C LYS A1083 12343 26807 13664 -2279 1188 2776 C ATOM 2222 O LYS A1083 150.190 17.817 570.150 1.00136.04 O ANISOU 2222 O LYS A1083 12287 26298 13103 -2070 1225 2548 O ATOM 2223 CB LYS A1083 148.252 17.261 571.967 1.00153.04 C ANISOU 2223 CB LYS A1083 12883 31334 13930 -2948 1691 2886 C ATOM 2224 CG LYS A1083 147.024 17.544 572.810 1.00159.79 C ANISOU 2224 CG LYS A1083 12794 33914 14005 -3070 2047 2558 C ATOM 2225 CD LYS A1083 146.595 18.993 572.672 1.00158.23 C ANISOU 2225 CD LYS A1083 12425 34028 13667 -2088 2220 1315 C ATOM 2226 CE LYS A1083 145.520 19.348 573.683 1.00167.43 C ANISOU 2226 CE LYS A1083 12608 37062 13946 -2136 2583 884 C ATOM 2227 NZ LYS A1083 145.195 20.800 573.647 1.00168.33 N ANISOU 2227 NZ LYS A1083 12607 37467 13884 -1097 2668 -394 N ATOM 2228 N VAL A1084 149.201 16.817 568.392 1.00132.71 N ANISOU 2228 N VAL A1084 11947 24859 13619 -2187 923 2957 N ATOM 2229 CA VAL A1084 150.371 16.924 567.520 1.00121.45 C ANISOU 2229 CA VAL A1084 11337 21996 12813 -1867 683 2916 C ATOM 2230 C VAL A1084 150.955 18.331 567.528 1.00117.42 C ANISOU 2230 C VAL A1084 11153 21271 12192 -1166 818 2022 C ATOM 2231 O VAL A1084 152.175 18.507 567.423 1.00113.47 O ANISOU 2231 O VAL A1084 11200 20036 11878 -1070 716 2024 O ATOM 2232 CB VAL A1084 150.004 16.471 566.090 1.00113.03 C ANISOU 2232 CB VAL A1084 10560 19888 12496 -1734 431 3025 C ATOM 2233 CG1 VAL A1084 151.247 16.379 565.220 1.00100.27 C ANISOU 2233 CG1 VAL A1084 9735 16890 11475 -1526 182 3094 C ATOM 2234 CG2 VAL A1084 149.284 15.134 566.132 1.00111.46 C ANISOU 2234 CG2 VAL A1084 10001 19985 12366 -2444 269 3871 C ATOM 2235 N LYS A1085 150.104 19.352 567.665 1.00120.36 N ANISOU 2235 N LYS A1085 11194 22290 12247 -671 1012 1228 N ATOM 2236 CA LYS A1085 150.601 20.720 567.772 1.00121.53 C ANISOU 2236 CA LYS A1085 11674 22274 12227 -23 1076 369 C ATOM 2237 C LYS A1085 151.399 20.931 569.054 1.00127.29 C ANISOU 2237 C LYS A1085 12324 23656 12383 -216 1214 431 C ATOM 2238 O LYS A1085 152.346 21.724 569.068 1.00125.85 O ANISOU 2238 O LYS A1085 12639 22955 12221 109 1169 31 O ATOM 2239 CB LYS A1085 149.438 21.713 567.705 1.00124.14 C ANISOU 2239 CB LYS A1085 11645 23214 12311 585 1172 -521 C ATOM 2240 CG LYS A1085 148.213 21.215 566.948 1.00122.43 C ANISOU 2240 CG LYS A1085 11068 23062 12388 568 1118 -446 C ATOM 2241 CD LYS A1085 147.183 20.617 567.900 1.00128.88 C ANISOU 2241 CD LYS A1085 10926 25405 12639 94 1350 -160 C ATOM 2242 CE LYS A1085 145.974 20.081 567.152 1.00128.88 C ANISOU 2242 CE LYS A1085 10528 25499 12939 16 1285 -64 C ATOM 2243 NZ LYS A1085 144.972 19.479 568.076 1.00135.97 N ANISOU 2243 NZ LYS A1085 10453 27962 13248 -547 1528 241 N ATOM 2244 N GLU A1086 151.037 20.233 570.134 1.00135.08 N ANISOU 2244 N GLU A1086 12710 25780 12836 -776 1367 941 N ATOM 2245 CA GLU A1086 151.776 20.364 571.386 1.00137.72 C ANISOU 2245 CA GLU A1086 12971 26763 12594 -989 1480 1045 C ATOM 2246 C GLU A1086 153.143 19.697 571.301 1.00132.17 C ANISOU 2246 C GLU A1086 12831 25155 12234 -1336 1259 1672 C ATOM 2247 O GLU A1086 154.082 20.120 571.986 1.00133.40 O ANISOU 2247 O GLU A1086 13192 25370 12123 -1280 1276 1536 O ATOM 2248 CB GLU A1086 150.960 19.775 572.538 1.00150.16 C ANISOU 2248 CB GLU A1086 13757 29844 13453 -1547 1698 1444 C ATOM 2249 CG GLU A1086 151.515 20.059 573.924 1.00158.93 C ANISOU 2249 CG GLU A1086 14706 31846 13835 -1696 1851 1423 C ATOM 2250 CD GLU A1086 150.616 19.533 575.026 1.00172.03 C ANISOU 2250 CD GLU A1086 15561 35092 14712 -2268 2097 1777 C ATOM 2251 OE1 GLU A1086 149.545 18.975 574.707 1.00176.62 O ANISOU 2251 OE1 GLU A1086 15680 36104 15326 -2561 2155 2018 O ATOM 2252 OE2 GLU A1086 150.980 19.675 576.212 1.00177.78 O ANISOU 2252 OE2 GLU A1086 16112 36665 14772 -2455 2230 1817 O ATOM 2253 N ALA A1087 153.275 18.655 570.474 1.00131.59 N ANISOU 2253 N ALA A1087 12997 24256 12745 -1667 1021 2321 N ATOM 2254 CA ALA A1087 154.585 18.052 570.256 1.00124.07 C ANISOU 2254 CA ALA A1087 12585 22380 12176 -1879 758 2798 C ATOM 2255 C ALA A1087 155.531 19.021 569.560 1.00118.50 C ANISOU 2255 C ALA A1087 12471 20725 11829 -1316 719 2161 C ATOM 2256 O ALA A1087 156.743 18.991 569.802 1.00116.51 O ANISOU 2256 O ALA A1087 12552 20090 11625 -1382 612 2265 O ATOM 2257 CB ALA A1087 154.445 16.763 569.447 1.00116.63 C ANISOU 2257 CB ALA A1087 11775 20746 11793 -2269 462 3539 C ATOM 2258 N GLN A1088 154.995 19.886 568.694 1.00122.26 N ANISOU 2258 N GLN A1088 13092 20821 12539 -787 778 1499 N ATOM 2259 CA GLN A1088 155.812 20.932 568.085 1.00121.98 C ANISOU 2259 CA GLN A1088 13642 19963 12744 -307 740 866 C ATOM 2260 C GLN A1088 156.238 21.969 569.117 1.00127.59 C ANISOU 2260 C GLN A1088 14319 21275 12885 -92 882 335 C ATOM 2261 O GLN A1088 157.362 22.481 569.061 1.00126.76 O ANISOU 2261 O GLN A1088 14666 20630 12868 12 818 116 O ATOM 2262 CB GLN A1088 155.047 21.600 566.943 1.00124.97 C ANISOU 2262 CB GLN A1088 14229 19795 13460 184 709 308 C ATOM 2263 CG GLN A1088 154.801 20.700 565.745 1.00124.00 C ANISOU 2263 CG GLN A1088 14276 18862 13974 50 531 746 C ATOM 2264 CD GLN A1088 154.081 21.417 564.619 1.00124.19 C ANISOU 2264 CD GLN A1088 14560 18317 14309 558 475 165 C ATOM 2265 OE1 GLN A1088 153.155 22.195 564.854 1.00129.51 O ANISOU 2265 OE1 GLN A1088 14978 19550 14681 924 564 -404 O ATOM 2266 NE2 GLN A1088 154.509 21.164 563.388 1.00118.92 N ANISOU 2266 NE2 GLN A1088 14410 16547 14229 610 300 275 N ATOM 2267 N ALA A1089 155.349 22.302 570.057 1.00131.99 N ANISOU 2267 N ALA A1089 14327 22984 12839 -22 1070 92 N ATOM 2268 CA ALA A1089 155.724 23.212 571.135 1.00130.53 C ANISOU 2268 CA ALA A1089 14073 23459 12064 180 1182 -394 C ATOM 2269 C ALA A1089 156.800 22.597 572.022 1.00126.44 C ANISOU 2269 C ALA A1089 13573 23129 11341 -292 1156 167 C ATOM 2270 O ALA A1089 157.686 23.302 572.520 1.00124.98 O ANISOU 2270 O ALA A1089 13640 22893 10953 -138 1142 -173 O ATOM 2271 CB ALA A1089 154.492 23.588 571.959 1.00138.81 C ANISOU 2271 CB ALA A1089 14449 25818 12473 353 1389 -769 C ATOM 2272 N ALA A1090 156.734 21.280 572.236 1.00124.04 N ANISOU 2272 N ALA A1090 13028 23020 11083 -874 1103 1023 N ATOM 2273 CA ALA A1090 157.761 20.602 573.020 1.00121.98 C ANISOU 2273 CA ALA A1090 12840 22841 10666 -1314 990 1588 C ATOM 2274 C ALA A1090 159.108 20.607 572.308 1.00116.26 C ANISOU 2274 C ALA A1090 12722 20953 10500 -1228 772 1586 C ATOM 2275 O ALA A1090 160.152 20.517 572.963 1.00117.02 O ANISOU 2275 O ALA A1090 12949 21070 10443 -1381 681 1724 O ATOM 2276 CB ALA A1090 157.325 19.169 573.333 1.00121.64 C ANISOU 2276 CB ALA A1090 12483 23173 10562 -1967 890 2518 C ATOM 2277 N ALA A1091 159.107 20.695 570.975 1.00114.03 N ANISOU 2277 N ALA A1091 12790 19697 10841 -998 683 1423 N ATOM 2278 CA ALA A1091 160.366 20.809 570.244 1.00115.30 C ANISOU 2278 CA ALA A1091 13483 18845 11480 -908 519 1327 C ATOM 2279 C ALA A1091 161.094 22.099 570.601 1.00123.13 C ANISOU 2279 C ALA A1091 14727 19836 12222 -603 606 636 C ATOM 2280 O ALA A1091 162.330 22.126 570.667 1.00122.14 O ANISOU 2280 O ALA A1091 14865 19332 12209 -691 500 644 O ATOM 2281 CB ALA A1091 160.110 20.732 568.739 1.00108.99 C ANISOU 2281 CB ALA A1091 13000 17094 11319 -719 436 1241 C ATOM 2282 N GLU A1092 160.346 23.183 570.817 1.00134.51 N ANISOU 2282 N GLU A1092 16092 21689 13326 -230 758 2 N ATOM 2283 CA GLU A1092 160.951 24.410 571.325 1.00137.08 C ANISOU 2283 CA GLU A1092 16648 22103 13334 45 785 -646 C ATOM 2284 C GLU A1092 161.587 24.179 572.690 1.00137.75 C ANISOU 2284 C GLU A1092 16481 22930 12926 -211 807 -416 C ATOM 2285 O GLU A1092 162.685 24.678 572.965 1.00137.89 O ANISOU 2285 O GLU A1092 16777 22712 12902 -200 734 -641 O ATOM 2286 CB GLU A1092 159.905 25.522 571.404 1.00147.65 C ANISOU 2286 CB GLU A1092 17913 23830 14357 538 870 -1371 C ATOM 2287 CG GLU A1092 159.296 25.915 570.068 1.00150.94 C ANISOU 2287 CG GLU A1092 18659 23464 15228 857 793 -1697 C ATOM 2288 CD GLU A1092 158.225 26.980 570.212 1.00159.35 C ANISOU 2288 CD GLU A1092 19632 24955 15961 1404 803 -2455 C ATOM 2289 OE1 GLU A1092 157.811 27.249 571.359 1.00165.81 O ANISOU 2289 OE1 GLU A1092 20006 26812 16183 1511 912 -2669 O ATOM 2290 OE2 GLU A1092 157.800 27.549 569.183 1.00158.80 O ANISOU 2290 OE2 GLU A1092 19938 24195 16204 1748 674 -2863 O ATOM 2291 N GLN A1093 160.905 23.431 573.562 1.00138.44 N ANISOU 2291 N GLN A1093 16047 23941 12613 -476 896 35 N ATOM 2292 CA GLN A1093 161.487 23.088 574.855 1.00135.99 C ANISOU 2292 CA GLN A1093 15525 24330 11814 -772 886 342 C ATOM 2293 C GLN A1093 162.702 22.187 574.682 1.00126.87 C ANISOU 2293 C GLN A1093 14619 22543 11042 -1119 649 897 C ATOM 2294 O GLN A1093 163.684 22.304 575.424 1.00127.02 O ANISOU 2294 O GLN A1093 14721 22695 10846 -1203 564 883 O ATOM 2295 CB GLN A1093 160.441 22.412 575.743 1.00146.37 C ANISOU 2295 CB GLN A1093 16251 26769 12594 -1070 1024 771 C ATOM 2296 CG GLN A1093 159.011 22.905 575.545 1.00152.54 C ANISOU 2296 CG GLN A1093 16681 28101 13176 -778 1232 356 C ATOM 2297 CD GLN A1093 158.746 24.272 576.155 1.00158.05 C ANISOU 2297 CD GLN A1093 17295 29399 13358 -254 1364 -533 C ATOM 2298 OE1 GLN A1093 159.665 24.969 576.586 1.00159.11 O ANISOU 2298 OE1 GLN A1093 17720 29380 13354 -84 1291 -885 O ATOM 2299 NE2 GLN A1093 157.476 24.658 576.196 1.00162.05 N ANISOU 2299 NE2 GLN A1093 17389 30608 13575 24 1527 -931 N ATOM 2300 N LEU A1094 162.640 21.263 573.719 1.00120.63 N ANISOU 2300 N LEU A1094 13935 21086 10813 -1294 509 1362 N ATOM 2301 CA LEU A1094 163.814 20.473 573.361 1.00111.95 C ANISOU 2301 CA LEU A1094 13098 19286 10150 -1505 235 1754 C ATOM 2302 C LEU A1094 164.959 21.375 572.925 1.00106.26 C ANISOU 2302 C LEU A1094 12766 17949 9659 -1253 218 1180 C ATOM 2303 O LEU A1094 166.113 21.176 573.322 1.00104.38 O ANISOU 2303 O LEU A1094 12620 17611 9428 -1377 58 1262 O ATOM 2304 CB LEU A1094 163.460 19.485 572.248 1.00101.65 C ANISOU 2304 CB LEU A1094 11874 17316 9433 -1625 76 2206 C ATOM 2305 CG LEU A1094 162.572 18.296 572.615 1.00102.18 C ANISOU 2305 CG LEU A1094 11622 17833 9368 -2027 -29 2951 C ATOM 2306 CD1 LEU A1094 162.036 17.625 571.363 1.00 97.67 C ANISOU 2306 CD1 LEU A1094 11159 16557 9393 -2032 -155 3209 C ATOM 2307 CD2 LEU A1094 163.357 17.306 573.450 1.00101.90 C ANISOU 2307 CD2 LEU A1094 11583 17951 9181 -2415 -339 3562 C ATOM 2308 N LYS A1095 164.651 22.371 572.092 1.00103.14 N ANISOU 2308 N LYS A1095 12613 17133 9443 -923 355 595 N ATOM 2309 CA LYS A1095 165.653 23.343 571.670 1.00102.33 C ANISOU 2309 CA LYS A1095 12912 16476 9492 -757 343 38 C ATOM 2310 C LYS A1095 166.216 24.103 572.865 1.00109.33 C ANISOU 2310 C LYS A1095 13752 17937 9853 -721 370 -294 C ATOM 2311 O LYS A1095 167.411 24.421 572.903 1.00109.68 O ANISOU 2311 O LYS A1095 14008 17687 9978 -786 279 -484 O ATOM 2312 CB LYS A1095 165.034 24.303 570.654 1.00100.96 C ANISOU 2312 CB LYS A1095 13052 15798 9512 -435 438 -501 C ATOM 2313 CG LYS A1095 165.959 24.739 569.529 1.00 97.15 C ANISOU 2313 CG LYS A1095 13059 14380 9472 -429 371 -778 C ATOM 2314 CD LYS A1095 165.167 25.432 568.425 1.00 93.90 C ANISOU 2314 CD LYS A1095 12984 13416 9277 -158 410 -1158 C ATOM 2315 CE LYS A1095 166.075 26.033 567.363 1.00 89.22 C ANISOU 2315 CE LYS A1095 12930 11958 9009 -209 357 -1472 C ATOM 2316 NZ LYS A1095 166.909 25.004 566.686 1.00 85.80 N ANISOU 2316 NZ LYS A1095 12474 11108 9019 -474 299 -1050 N ATOM 2317 N THR A1096 165.366 24.405 573.850 1.00117.48 N ANISOU 2317 N THR A1096 14479 19833 10324 -618 492 -394 N ATOM 2318 CA THR A1096 165.831 25.070 575.064 1.00122.40 C ANISOU 2318 CA THR A1096 15032 21077 10398 -564 502 -697 C ATOM 2319 C THR A1096 166.795 24.181 575.842 1.00123.23 C ANISOU 2319 C THR A1096 15001 21407 10414 -913 348 -184 C ATOM 2320 O THR A1096 167.868 24.628 576.266 1.00123.50 O ANISOU 2320 O THR A1096 15189 21373 10364 -922 252 -429 O ATOM 2321 CB THR A1096 164.635 25.461 575.937 1.00132.58 C ANISOU 2321 CB THR A1096 15956 23348 11072 -370 671 -900 C ATOM 2322 OG1 THR A1096 163.872 26.481 575.280 1.00134.69 O ANISOU 2322 OG1 THR A1096 16402 23377 11396 58 735 -1539 O ATOM 2323 CG2 THR A1096 165.102 25.977 577.291 1.00137.73 C ANISOU 2323 CG2 THR A1096 16490 24733 11106 -336 665 -1138 C ATOM 2324 N THR A1097 166.420 22.917 576.050 1.00123.35 N ANISOU 2324 N THR A1097 14749 21679 10440 -1214 280 528 N ATOM 2325 CA THR A1097 167.308 21.985 576.739 1.00120.02 C ANISOU 2325 CA THR A1097 14263 21383 9957 -1532 40 1047 C ATOM 2326 C THR A1097 168.576 21.741 575.933 1.00116.69 C ANISOU 2326 C THR A1097 14132 20083 10123 -1551 -177 1019 C ATOM 2327 O THR A1097 169.670 21.635 576.502 1.00117.29 O ANISOU 2327 O THR A1097 14242 20197 10126 -1636 -361 1022 O ATOM 2328 CB THR A1097 166.578 20.669 577.007 1.00116.11 C ANISOU 2328 CB THR A1097 13510 21231 9377 -1885 -60 1842 C ATOM 2329 OG1 THR A1097 165.455 20.912 577.862 1.00119.65 O ANISOU 2329 OG1 THR A1097 13611 22666 9186 -1925 173 1845 O ATOM 2330 CG2 THR A1097 167.504 19.657 577.673 1.00109.70 C ANISOU 2330 CG2 THR A1097 12722 20438 8522 -2200 -413 2394 C ATOM 2331 N ARG A1098 168.451 21.651 574.607 1.00117.35 N ANISOU 2331 N ARG A1098 14403 19415 10771 -1463 -161 962 N ATOM 2332 CA ARG A1098 169.632 21.497 573.767 1.00122.19 C ANISOU 2332 CA ARG A1098 15249 19273 11904 -1468 -323 851 C ATOM 2333 C ARG A1098 170.561 22.694 573.900 1.00129.65 C ANISOU 2333 C ARG A1098 16384 20138 12738 -1359 -248 202 C ATOM 2334 O ARG A1098 171.786 22.539 573.835 1.00130.54 O ANISOU 2334 O ARG A1098 16548 20009 13041 -1447 -412 130 O ATOM 2335 CB ARG A1098 169.218 21.300 572.308 1.00120.94 C ANISOU 2335 CB ARG A1098 15266 18387 12298 -1382 -281 855 C ATOM 2336 CG ARG A1098 170.383 21.058 571.360 1.00119.77 C ANISOU 2336 CG ARG A1098 15309 17535 12664 -1397 -428 741 C ATOM 2337 CD ARG A1098 169.917 20.947 569.916 1.00117.84 C ANISOU 2337 CD ARG A1098 15260 16609 12906 -1299 -365 709 C ATOM 2338 NE ARG A1098 169.279 22.174 569.447 1.00119.00 N ANISOU 2338 NE ARG A1098 15640 16612 12961 -1127 -100 209 N ATOM 2339 CZ ARG A1098 169.926 23.180 568.867 1.00119.54 C ANISOU 2339 CZ ARG A1098 16022 16292 13105 -1090 -5 -324 C ATOM 2340 NH1 ARG A1098 171.237 23.109 568.682 1.00120.55 N ANISOU 2340 NH1 ARG A1098 16190 16219 13393 -1234 -95 -445 N ATOM 2341 NH2 ARG A1098 169.263 24.258 568.473 1.00119.21 N ANISOU 2341 NH2 ARG A1098 16259 16073 12961 -924 149 -748 N ATOM 2342 N ASN A1099 170.002 23.888 574.101 1.00140.30 N ANISOU 2342 N ASN A1099 17835 21703 13771 -1167 -40 -295 N ATOM 2343 CA ASN A1099 170.803 25.086 574.312 1.00142.10 C ANISOU 2343 CA ASN A1099 18291 21860 13841 -1093 -20 -905 C ATOM 2344 C ASN A1099 171.276 25.224 575.752 1.00142.68 C ANISOU 2344 C ASN A1099 18177 22637 13398 -1137 -100 -931 C ATOM 2345 O ASN A1099 172.175 26.029 576.019 1.00145.58 O ANISOU 2345 O ASN A1099 18705 22944 13666 -1138 -153 -1363 O ATOM 2346 CB ASN A1099 170.005 26.330 573.907 1.00146.96 C ANISOU 2346 CB ASN A1099 19175 22327 14337 -826 135 -1462 C ATOM 2347 CG ASN A1099 170.875 27.400 573.271 1.00150.00 C ANISOU 2347 CG ASN A1099 19998 22108 14889 -846 100 -2012 C ATOM 2348 OD1 ASN A1099 171.948 27.111 572.740 1.00148.91 O ANISOU 2348 OD1 ASN A1099 19936 21559 15083 -1076 31 -1952 O ATOM 2349 ND2 ASN A1099 170.412 28.645 573.318 1.00153.06 N ANISOU 2349 ND2 ASN A1099 20675 22454 15026 -614 119 -2567 N ATOM 2350 N ALA A1100 170.698 24.463 576.683 1.00140.08 N ANISOU 2350 N ALA A1100 17528 22979 12716 -1210 -124 -469 N ATOM 2351 CA ALA A1100 171.142 24.521 578.071 1.00138.69 C ANISOU 2351 CA ALA A1100 17190 23494 12013 -1269 -217 -452 C ATOM 2352 C ALA A1100 172.394 23.687 578.304 1.00134.63 C ANISOU 2352 C ALA A1100 16641 22817 11697 -1485 -506 -140 C ATOM 2353 O ALA A1100 173.158 23.972 579.233 1.00108.47 O ANISOU 2353 O ALA A1100 13296 19847 8072 -1507 -626 -300 O ATOM 2354 CB ALA A1100 170.021 24.059 579.004 1.00135.11 C ANISOU 2354 CB ALA A1100 16415 23897 11023 -1317 -124 -77 C ATOM 2355 N TYR A1101 172.621 22.665 577.485 1.00119.64 N ANISOU 2355 N TYR A1101 14745 20402 10309 -1607 -658 264 N ATOM 2356 CA TYR A1101 173.788 21.794 577.593 1.00123.27 C ANISOU 2356 CA TYR A1101 15165 20662 11010 -1740 -1001 515 C ATOM 2357 C TYR A1101 174.438 21.601 576.229 1.00123.32 C ANISOU 2357 C TYR A1101 15298 19882 11677 -1711 -1055 366 C ATOM 2358 O TYR A1101 174.800 20.493 575.830 1.00124.63 O ANISOU 2358 O TYR A1101 15412 19742 12201 -1764 -1331 736 O ATOM 2359 CB TYR A1101 173.408 20.452 578.215 1.00128.76 C ANISOU 2359 CB TYR A1101 15709 21653 11561 -1926 -1268 1265 C ATOM 2360 CG TYR A1101 173.403 20.462 579.728 1.00137.11 C ANISOU 2360 CG TYR A1101 16643 23502 11951 -2030 -1351 1423 C ATOM 2361 CD1 TYR A1101 174.337 21.204 580.440 1.00139.00 C ANISOU 2361 CD1 TYR A1101 16899 23971 11943 -1949 -1396 979 C ATOM 2362 CD2 TYR A1101 172.462 19.733 580.445 1.00141.68 C ANISOU 2362 CD2 TYR A1101 17091 24624 12119 -2247 -1389 2022 C ATOM 2363 CE1 TYR A1101 174.338 21.218 581.823 1.00144.36 C ANISOU 2363 CE1 TYR A1101 17483 25380 11990 -2028 -1483 1111 C ATOM 2364 CE2 TYR A1101 172.454 19.741 581.829 1.00147.37 C ANISOU 2364 CE2 TYR A1101 17708 26116 12169 -2376 -1454 2177 C ATOM 2365 CZ TYR A1101 173.395 20.485 582.512 1.00148.16 C ANISOU 2365 CZ TYR A1101 17843 26412 12041 -2240 -1503 1711 C ATOM 2366 OH TYR A1101 173.392 20.498 583.888 1.00152.21 O ANISOU 2366 OH TYR A1101 18270 27697 11868 -2352 -1578 1852 O ATOM 2367 N ILE A1102 174.589 22.703 575.488 1.00121.43 N ANISOU 2367 N ILE A1102 15251 19308 11580 -1630 -816 -199 N ATOM 2368 CA ILE A1102 175.324 22.680 574.225 1.00115.95 C ANISOU 2368 CA ILE A1102 14674 17956 11425 -1653 -826 -417 C ATOM 2369 C ILE A1102 176.787 23.056 574.408 1.00115.76 C ANISOU 2369 C ILE A1102 14610 17939 11435 -1744 -945 -811 C ATOM 2370 O ILE A1102 177.590 22.860 573.482 1.00113.17 O ANISOU 2370 O ILE A1102 14277 17207 11514 -1801 -992 -975 O ATOM 2371 CB ILE A1102 174.671 23.616 573.186 1.00115.83 C ANISOU 2371 CB ILE A1102 14944 17515 11551 -1586 -530 -768 C ATOM 2372 CG1 ILE A1102 175.042 23.191 571.764 1.00113.30 C ANISOU 2372 CG1 ILE A1102 14717 16539 11791 -1626 -538 -770 C ATOM 2373 CG2 ILE A1102 175.076 25.062 573.439 1.00117.60 C ANISOU 2373 CG2 ILE A1102 15385 17794 11503 -1602 -401 -1381 C ATOM 2374 CD1 ILE A1102 174.405 24.040 570.686 1.00110.38 C ANISOU 2374 CD1 ILE A1102 14686 15695 11560 -1581 -292 -1069 C ATOM 2375 N GLN A1103 177.162 23.582 575.576 1.00114.22 N ANISOU 2375 N GLN A1103 14357 18235 10806 -1762 -998 -989 N ATOM 2376 CA GLN A1103 178.544 23.949 575.855 1.00111.68 C ANISOU 2376 CA GLN A1103 13962 17983 10488 -1864 -1134 -1371 C ATOM 2377 C GLN A1103 179.502 22.767 575.769 1.00109.60 C ANISOU 2377 C GLN A1103 13445 17660 10538 -1872 -1474 -1153 C ATOM 2378 O GLN A1103 180.718 22.980 575.718 1.00110.59 O ANISOU 2378 O GLN A1103 13450 17795 10775 -1952 -1582 -1520 O ATOM 2379 CB GLN A1103 178.632 24.595 577.241 1.00113.30 C ANISOU 2379 CB GLN A1103 14146 18763 10139 -1844 -1178 -1532 C ATOM 2380 CG GLN A1103 177.931 23.802 578.336 1.00112.96 C ANISOU 2380 CG GLN A1103 13954 19239 9727 -1770 -1314 -1006 C ATOM 2381 CD GLN A1103 177.795 24.582 579.629 1.00113.58 C ANISOU 2381 CD GLN A1103 14039 19925 9190 -1719 -1286 -1213 C ATOM 2382 OE1 GLN A1103 177.120 24.148 580.562 1.00114.30 O ANISOU 2382 OE1 GLN A1103 14023 20540 8863 -1693 -1328 -845 O ATOM 2383 NE2 GLN A1103 178.438 25.743 579.691 1.00113.23 N ANISOU 2383 NE2 GLN A1103 14130 19831 9061 -1730 -1228 -1805 N ATOM 2384 N LYS A1104 178.989 21.535 575.754 1.00107.44 N ANISOU 2384 N LYS A1104 13090 17332 10402 -1792 -1681 -591 N ATOM 2385 CA LYS A1104 179.839 20.358 575.635 1.00108.82 C ANISOU 2385 CA LYS A1104 13076 17379 10891 -1731 -2101 -401 C ATOM 2386 C LYS A1104 180.226 20.052 574.195 1.00110.26 C ANISOU 2386 C LYS A1104 13233 17034 11625 -1687 -2074 -577 C ATOM 2387 O LYS A1104 181.223 19.357 573.971 1.00112.35 O ANISOU 2387 O LYS A1104 13297 17224 12166 -1598 -2398 -678 O ATOM 2388 CB LYS A1104 179.142 19.134 576.239 1.00108.91 C ANISOU 2388 CB LYS A1104 13082 17499 10800 -1696 -2427 304 C ATOM 2389 CG LYS A1104 179.247 19.021 577.754 1.00112.79 C ANISOU 2389 CG LYS A1104 13527 18558 10771 -1749 -2652 517 C ATOM 2390 CD LYS A1104 178.370 20.034 578.468 1.00107.82 C ANISOU 2390 CD LYS A1104 12973 18387 9605 -1824 -2265 440 C ATOM 2391 CE LYS A1104 178.586 19.983 579.969 1.00119.33 C ANISOU 2391 CE LYS A1104 14376 20456 10507 -1876 -2477 587 C ATOM 2392 NZ LYS A1104 177.795 21.024 580.681 1.00119.81 N ANISOU 2392 NZ LYS A1104 14477 21031 10015 -1891 -2112 411 N ATOM 2393 N TYR A1105 179.472 20.549 573.220 1.00110.37 N ANISOU 2393 N TYR A1105 13440 16708 11787 -1721 -1721 -650 N ATOM 2394 CA TYR A1105 179.688 20.228 571.818 1.00112.37 C ANISOU 2394 CA TYR A1105 13702 16472 12523 -1684 -1676 -771 C ATOM 2395 C TYR A1105 180.133 21.463 571.043 1.00112.29 C ANISOU 2395 C TYR A1105 13817 16310 12537 -1866 -1308 -1352 C ATOM 2396 O TYR A1105 180.197 22.578 571.570 1.00113.77 O ANISOU 2396 O TYR A1105 14128 16705 12394 -2008 -1119 -1646 O ATOM 2397 CB TYR A1105 178.425 19.626 571.200 1.00114.42 C ANISOU 2397 CB TYR A1105 14120 16385 12968 -1593 -1634 -315 C ATOM 2398 CG TYR A1105 178.543 18.148 570.916 1.00119.46 C ANISOU 2398 CG TYR A1105 14639 16795 13954 -1433 -2074 84 C ATOM 2399 CD1 TYR A1105 179.422 17.678 569.949 1.00122.35 C ANISOU 2399 CD1 TYR A1105 14880 16871 14736 -1317 -2230 -178 C ATOM 2400 CD2 TYR A1105 177.776 17.223 571.610 1.00123.11 C ANISOU 2400 CD2 TYR A1105 15125 17347 14303 -1412 -2364 709 C ATOM 2401 CE1 TYR A1105 179.537 16.328 569.684 1.00125.67 C ANISOU 2401 CE1 TYR A1105 15224 17046 15480 -1107 -2710 135 C ATOM 2402 CE2 TYR A1105 177.883 15.870 571.352 1.00126.63 C ANISOU 2402 CE2 TYR A1105 15541 17506 15068 -1279 -2856 1085 C ATOM 2403 CZ TYR A1105 178.765 15.428 570.388 1.00127.49 C ANISOU 2403 CZ TYR A1105 15548 17275 15616 -1088 -3050 778 C ATOM 2404 OH TYR A1105 178.875 14.082 570.126 1.00129.37 O ANISOU 2404 OH TYR A1105 15785 17193 16177 -892 -3613 1102 O ATOM 2405 N LEU A1106 180.434 21.245 569.767 1.00110.12 N ANISOU 2405 N LEU A1106 13538 15660 12641 -1875 -1239 -1509 N ATOM 2406 CA LEU A1106 180.939 22.292 568.888 1.00108.12 C ANISOU 2406 CA LEU A1106 13421 15242 12417 -2128 -923 -2017 C ATOM 2407 C LEU A1106 179.794 23.009 568.179 1.00102.98 C ANISOU 2407 C LEU A1106 13200 14185 11744 -2177 -613 -1979 C ATOM 2408 O LEU A1106 178.919 22.373 567.593 1.00 98.64 O ANISOU 2408 O LEU A1106 12741 13320 11417 -2002 -623 -1650 O ATOM 2409 CB LEU A1106 181.912 21.707 567.857 1.00109.13 C ANISOU 2409 CB LEU A1106 13296 15263 12906 -2136 -996 -2253 C ATOM 2410 CG LEU A1106 183.170 20.979 568.344 1.00114.24 C ANISOU 2410 CG LEU A1106 13474 16298 13634 -2031 -1347 -2420 C ATOM 2411 CD1 LEU A1106 182.878 19.527 568.708 1.00113.93 C ANISOU 2411 CD1 LEU A1106 13291 16201 13795 -1653 -1809 -1954 C ATOM 2412 CD2 LEU A1106 184.252 21.042 567.279 1.00116.42 C ANISOU 2412 CD2 LEU A1106 13500 16617 14118 -2173 -1247 -2915 C ATOM 2413 N SER A 380 178.404 19.393 562.260 1.00126.30 N ANISOU 2413 N SER A 380 16331 15090 16565 -1482 -763 -1372 N ATOM 2414 CA SER A 380 179.245 19.738 561.120 1.00125.49 C ANISOU 2414 CA SER A 380 16213 14918 16549 -1645 -566 -1830 C ATOM 2415 C SER A 380 178.432 19.796 559.830 1.00121.72 C ANISOU 2415 C SER A 380 16091 13895 16262 -1609 -400 -1766 C ATOM 2416 O SER A 380 177.994 18.769 559.311 1.00122.19 O ANISOU 2416 O SER A 380 16111 13675 16643 -1308 -627 -1510 O ATOM 2417 CB SER A 380 180.391 18.734 560.975 1.00128.52 C ANISOU 2417 CB SER A 380 16120 15565 17148 -1455 -869 -2016 C ATOM 2418 OG SER A 380 181.249 18.773 562.102 1.00131.66 O ANISOU 2418 OG SER A 380 16196 16469 17358 -1502 -1028 -2150 O ATOM 2419 N ARG A 381 178.237 21.011 559.319 1.00134.90 N ANISOU 2419 N ARG A 381 20557 20791 9909 120 282 -203 N ATOM 2420 CA ARG A 381 177.499 21.238 558.081 1.00125.59 C ANISOU 2420 CA ARG A 381 19159 19315 9245 79 580 -254 C ATOM 2421 C ARG A 381 178.296 20.876 556.836 1.00113.79 C ANISOU 2421 C ARG A 381 17483 17552 8201 104 204 -137 C ATOM 2422 O ARG A 381 177.802 21.102 555.725 1.00109.43 O ANISOU 2422 O ARG A 381 16745 16770 8064 53 398 -194 O ATOM 2423 CB ARG A 381 177.070 22.704 558.000 1.00127.10 C ANISOU 2423 CB ARG A 381 19386 19400 9504 71 824 -790 C ATOM 2424 CG ARG A 381 178.244 23.669 557.942 1.00129.10 C ANISOU 2424 CG ARG A 381 19704 19586 9763 54 371 -1175 C ATOM 2425 CD ARG A 381 177.820 25.106 558.196 1.00133.18 C ANISOU 2425 CD ARG A 381 20306 20004 10291 29 605 -1691 C ATOM 2426 NE ARG A 381 177.048 25.667 557.093 1.00129.52 N ANISOU 2426 NE ARG A 381 19627 19218 10365 -1 921 -1831 N ATOM 2427 CZ ARG A 381 176.635 26.930 557.042 1.00131.08 C ANISOU 2427 CZ ARG A 381 19846 19223 10735 2 1120 -2256 C ATOM 2428 NH1 ARG A 381 175.937 27.361 556.000 1.00127.16 N ANISOU 2428 NH1 ARG A 381 19140 18419 10756 14 1376 -2341 N ATOM 2429 NH2 ARG A 381 176.922 27.762 558.033 1.00136.76 N ANISOU 2429 NH2 ARG A 381 20803 20040 11119 14 1044 -2596 N ATOM 2430 N GLU A 382 179.503 20.326 556.986 1.00107.03 N ANISOU 2430 N GLU A 382 16738 16646 7282 149 -326 8 N ATOM 2431 CA GLU A 382 180.381 20.110 555.842 1.00 97.79 C ANISOU 2431 CA GLU A 382 15337 15286 6534 26 -723 49 C ATOM 2432 C GLU A 382 179.845 19.061 554.875 1.00 91.79 C ANISOU 2432 C GLU A 382 14326 14413 6139 35 -583 440 C ATOM 2433 O GLU A 382 180.278 19.031 553.717 1.00 81.95 O ANISOU 2433 O GLU A 382 12690 13103 5343 66 -763 424 O ATOM 2434 CB GLU A 382 181.779 19.724 556.327 1.00100.02 C ANISOU 2434 CB GLU A 382 15661 15636 6707 47 -1316 109 C ATOM 2435 CG GLU A 382 182.420 20.765 557.237 1.00106.93 C ANISOU 2435 CG GLU A 382 16713 16653 7262 58 -1516 -292 C ATOM 2436 CD GLU A 382 182.532 22.132 556.583 1.00105.66 C ANISOU 2436 CD GLU A 382 16374 16425 7345 -71 -1469 -760 C ATOM 2437 OE1 GLU A 382 182.787 22.195 555.362 1.00103.36 O ANISOU 2437 OE1 GLU A 382 15742 16008 7524 -156 -1541 -775 O ATOM 2438 OE2 GLU A 382 182.359 23.147 557.290 1.00110.94 O ANISOU 2438 OE2 GLU A 382 17225 17172 7756 -77 -1352 -1118 O ATOM 2439 N LYS A 383 178.922 18.203 555.316 1.00 94.58 N ANISOU 2439 N LYS A 383 14834 14741 6360 16 -257 782 N ATOM 2440 CA LYS A 383 178.258 17.298 554.383 1.00 88.78 C ANISOU 2440 CA LYS A 383 13822 13861 6051 98 -61 1118 C ATOM 2441 C LYS A 383 177.432 18.076 553.366 1.00 78.20 C ANISOU 2441 C LYS A 383 12196 12432 5084 133 299 888 C ATOM 2442 O LYS A 383 177.366 17.701 552.190 1.00 72.39 O ANISOU 2442 O LYS A 383 11111 11453 4940 181 252 982 O ATOM 2443 CB LYS A 383 177.378 16.307 555.145 1.00 95.72 C ANISOU 2443 CB LYS A 383 14914 14715 6740 25 251 1498 C ATOM 2444 CG LYS A 383 178.047 14.978 555.465 1.00100.27 C ANISOU 2444 CG LYS A 383 15608 15209 7281 59 -120 1915 C ATOM 2445 CD LYS A 383 177.917 13.997 554.307 1.00 96.30 C ANISOU 2445 CD LYS A 383 14797 14434 7360 198 -153 2195 C ATOM 2446 CE LYS A 383 178.440 12.620 554.690 1.00101.29 C ANISOU 2446 CE LYS A 383 15589 14913 7985 242 -464 2591 C ATOM 2447 NZ LYS A 383 178.146 11.600 553.645 1.00 97.62 N ANISOU 2447 NZ LYS A 383 14858 14140 8095 343 -427 2839 N ATOM 2448 N LYS A 384 176.794 19.164 553.805 1.00 78.23 N ANISOU 2448 N LYS A 384 12337 12484 4903 70 642 534 N ATOM 2449 CA LYS A 384 176.063 20.023 552.881 1.00 70.93 C ANISOU 2449 CA LYS A 384 11137 11309 4502 74 923 249 C ATOM 2450 C LYS A 384 177.010 20.738 551.926 1.00 61.65 C ANISOU 2450 C LYS A 384 9730 10019 3676 54 547 -11 C ATOM 2451 O LYS A 384 176.689 20.924 550.747 1.00 61.82 O ANISOU 2451 O LYS A 384 9445 9783 4261 85 606 -47 O ATOM 2452 CB LYS A 384 175.217 21.028 553.668 1.00 78.35 C ANISOU 2452 CB LYS A 384 12299 12319 5151 44 1369 -88 C ATOM 2453 CG LYS A 384 174.785 22.264 552.886 1.00 81.28 C ANISOU 2453 CG LYS A 384 12465 12446 5972 68 1528 -492 C ATOM 2454 CD LYS A 384 175.664 23.468 553.211 1.00 90.43 C ANISOU 2454 CD LYS A 384 13808 13667 6884 -11 1281 -935 C ATOM 2455 CE LYS A 384 175.403 24.620 552.253 1.00 95.20 C ANISOU 2455 CE LYS A 384 14209 13954 8007 11 1355 -1267 C ATOM 2456 NZ LYS A 384 176.343 25.754 552.477 1.00100.98 N ANISOU 2456 NZ LYS A 384 15109 14692 8565 -108 1089 -1683 N ATOM 2457 N VAL A 385 178.181 21.147 552.419 1.00 59.82 N ANISOU 2457 N VAL A 385 9640 9983 3107 -14 157 -193 N ATOM 2458 CA VAL A 385 179.147 21.842 551.572 1.00 57.05 C ANISOU 2458 CA VAL A 385 9061 9540 3076 -80 -175 -445 C ATOM 2459 C VAL A 385 179.620 20.932 550.447 1.00 53.83 C ANISOU 2459 C VAL A 385 8307 9007 3140 -13 -408 -161 C ATOM 2460 O VAL A 385 179.720 21.354 549.288 1.00 49.62 O ANISOU 2460 O VAL A 385 7510 8263 3082 -36 -420 -277 O ATOM 2461 CB VAL A 385 180.326 22.359 552.418 1.00 61.68 C ANISOU 2461 CB VAL A 385 9838 10395 3205 -189 -568 -692 C ATOM 2462 CG1 VAL A 385 181.305 23.135 551.549 1.00 56.50 C ANISOU 2462 CG1 VAL A 385 8920 9636 2911 -307 -859 -970 C ATOM 2463 CG2 VAL A 385 179.822 23.222 553.565 1.00 61.42 C ANISOU 2463 CG2 VAL A 385 10174 10380 2783 -206 -321 -976 C ATOM 2464 N THR A 386 179.913 19.669 550.767 1.00 59.00 N ANISOU 2464 N THR A 386 8984 9775 3658 76 -588 214 N ATOM 2465 CA THR A 386 180.347 18.728 549.740 1.00 62.81 C ANISOU 2465 CA THR A 386 9154 10123 4587 164 -793 462 C ATOM 2466 C THR A 386 179.244 18.479 548.717 1.00 57.33 C ANISOU 2466 C THR A 386 8267 9134 4382 205 -450 569 C ATOM 2467 O THR A 386 179.513 18.403 547.512 1.00 54.63 O ANISOU 2467 O THR A 386 7640 8625 4493 222 -546 547 O ATOM 2468 CB THR A 386 180.797 17.418 550.389 1.00 49.52 C ANISOU 2468 CB THR A 386 7583 8576 2658 278 -1044 851 C ATOM 2469 OG1 THR A 386 181.905 17.673 551.263 1.00 53.30 O ANISOU 2469 OG1 THR A 386 8206 9268 2776 245 -1429 723 O ATOM 2470 CG2 THR A 386 181.224 16.416 549.330 1.00 46.56 C ANISOU 2470 CG2 THR A 386 6893 8028 2771 394 -1235 1075 C ATOM 2471 N ARG A 387 177.995 18.356 549.177 1.00 56.59 N ANISOU 2471 N ARG A 387 8317 8989 4197 214 -46 670 N ATOM 2472 CA ARG A 387 176.876 18.208 548.250 1.00 48.47 C ANISOU 2472 CA ARG A 387 7073 7698 3645 244 261 731 C ATOM 2473 C ARG A 387 176.742 19.427 547.347 1.00 39.39 C ANISOU 2473 C ARG A 387 5763 6391 2813 213 316 391 C ATOM 2474 O ARG A 387 176.497 19.293 546.142 1.00 41.00 O ANISOU 2474 O ARG A 387 5717 6385 3475 245 307 423 O ATOM 2475 CB ARG A 387 175.574 17.982 549.018 1.00 57.86 C ANISOU 2475 CB ARG A 387 8409 8898 4675 238 710 854 C ATOM 2476 CG ARG A 387 175.510 16.694 549.820 1.00 70.93 C ANISOU 2476 CG ARG A 387 10248 10646 6057 247 727 1263 C ATOM 2477 CD ARG A 387 174.196 16.615 550.582 1.00 80.05 C ANISOU 2477 CD ARG A 387 11537 11829 7049 196 1248 1348 C ATOM 2478 NE ARG A 387 174.134 15.463 551.477 1.00 89.86 N ANISOU 2478 NE ARG A 387 13034 13162 7948 168 1303 1761 N ATOM 2479 CZ ARG A 387 173.119 15.214 552.299 1.00 94.33 C ANISOU 2479 CZ ARG A 387 13770 13792 8281 91 1770 1906 C ATOM 2480 NH1 ARG A 387 172.080 16.037 552.341 1.00 97.04 N ANISOU 2480 NH1 ARG A 387 14009 14134 8728 60 2219 1637 N ATOM 2481 NH2 ARG A 387 173.142 14.143 553.081 1.00 96.14 N ANISOU 2481 NH2 ARG A 387 14227 14029 8274 2 1742 2255 N ATOM 2482 N THR A 388 176.891 20.625 547.916 1.00 42.66 N ANISOU 2482 N THR A 388 6350 6886 2973 148 366 63 N ATOM 2483 CA THR A 388 176.767 21.848 547.128 1.00 42.26 C ANISOU 2483 CA THR A 388 6204 6640 3214 117 419 -246 C ATOM 2484 C THR A 388 177.822 21.909 546.031 1.00 45.86 C ANISOU 2484 C THR A 388 6458 7018 3949 65 87 -273 C ATOM 2485 O THR A 388 177.518 22.263 544.885 1.00 42.59 O ANISOU 2485 O THR A 388 5877 6376 3930 78 132 -313 O ATOM 2486 CB THR A 388 176.866 23.069 548.044 1.00 48.98 C ANISOU 2486 CB THR A 388 7318 7573 3719 44 504 -608 C ATOM 2487 OG1 THR A 388 175.739 23.097 548.929 1.00 49.48 O ANISOU 2487 OG1 THR A 388 7544 7688 3568 106 901 -621 O ATOM 2488 CG2 THR A 388 176.894 24.352 547.232 1.00 40.47 C ANISOU 2488 CG2 THR A 388 6179 6245 2953 1 513 -912 C ATOM 2489 N ILE A 389 179.067 21.563 546.362 1.00 38.53 N ANISOU 2489 N ILE A 389 5538 6291 2813 9 -248 -250 N ATOM 2490 CA ILE A 389 180.131 21.558 545.362 1.00 37.18 C ANISOU 2490 CA ILE A 389 5135 6084 2908 -48 -526 -285 C ATOM 2491 C ILE A 389 179.815 20.567 544.250 1.00 31.97 C ANISOU 2491 C ILE A 389 4244 5269 2632 57 -508 -28 C ATOM 2492 O ILE A 389 179.962 20.880 543.062 1.00 32.35 O ANISOU 2492 O ILE A 389 4128 5158 3006 24 -523 -94 O ATOM 2493 CB ILE A 389 181.486 21.259 546.028 1.00 44.06 C ANISOU 2493 CB ILE A 389 6004 7232 3506 -97 -898 -305 C ATOM 2494 CG1 ILE A 389 181.936 22.463 546.858 1.00 54.24 C ANISOU 2494 CG1 ILE A 389 7487 8642 4481 -255 -965 -653 C ATOM 2495 CG2 ILE A 389 182.533 20.897 544.982 1.00 39.20 C ANISOU 2495 CG2 ILE A 389 5076 6607 3212 -115 -1145 -280 C ATOM 2496 CD1 ILE A 389 183.289 22.295 547.501 1.00 61.39 C ANISOU 2496 CD1 ILE A 389 8354 9836 5133 -323 -1381 -722 C ATOM 2497 N LEU A 390 179.361 19.364 544.613 1.00 33.50 N ANISOU 2497 N LEU A 390 4451 5495 2781 172 -469 267 N ATOM 2498 CA LEU A 390 179.009 18.369 543.604 1.00 35.45 C ANISOU 2498 CA LEU A 390 4499 5572 3397 261 -456 485 C ATOM 2499 C LEU A 390 177.914 18.883 542.679 1.00 36.98 C ANISOU 2499 C LEU A 390 4610 5529 3911 262 -214 413 C ATOM 2500 O LEU A 390 177.960 18.654 541.465 1.00 38.51 O ANISOU 2500 O LEU A 390 4628 5578 4426 280 -276 433 O ATOM 2501 CB LEU A 390 178.571 17.067 544.276 1.00 36.07 C ANISOU 2501 CB LEU A 390 4654 5676 3374 353 -415 812 C ATOM 2502 CG LEU A 390 178.112 15.960 543.322 1.00 37.99 C ANISOU 2502 CG LEU A 390 4717 5709 4009 429 -393 1025 C ATOM 2503 CD1 LEU A 390 179.252 15.525 542.412 1.00 35.90 C ANISOU 2503 CD1 LEU A 390 4258 5429 3952 477 -684 999 C ATOM 2504 CD2 LEU A 390 177.541 14.772 544.082 1.00 39.25 C ANISOU 2504 CD2 LEU A 390 4995 5844 4075 479 -298 1354 C ATOM 2505 N ALA A 391 176.922 19.586 543.232 1.00 38.85 N ANISOU 2505 N ALA A 391 4971 5730 4060 257 54 318 N ATOM 2506 CA ALA A 391 175.844 20.118 542.405 1.00 35.72 C ANISOU 2506 CA ALA A 391 4473 5109 3989 295 248 247 C ATOM 2507 C ALA A 391 176.366 21.152 541.416 1.00 31.82 C ANISOU 2507 C ALA A 391 3945 4490 3657 239 128 42 C ATOM 2508 O ALA A 391 175.970 21.158 540.245 1.00 29.65 O ANISOU 2508 O ALA A 391 3539 4035 3693 275 114 74 O ATOM 2509 CB ALA A 391 174.750 20.720 543.286 1.00 28.97 C ANISOU 2509 CB ALA A 391 3736 4256 3017 327 571 149 C ATOM 2510 N ILE A 392 177.258 22.035 541.869 1.00 39.45 N ANISOU 2510 N ILE A 392 5044 5545 4402 133 34 -167 N ATOM 2511 CA ILE A 392 177.831 23.040 540.980 1.00 36.19 C ANISOU 2511 CA ILE A 392 4624 4995 4134 32 -58 -344 C ATOM 2512 C ILE A 392 178.694 22.381 539.911 1.00 36.90 C ANISOU 2512 C ILE A 392 4530 5101 4389 -5 -256 -236 C ATOM 2513 O ILE A 392 178.672 22.782 538.741 1.00 34.03 O ANISOU 2513 O ILE A 392 4117 4567 4244 -35 -262 -257 O ATOM 2514 CB ILE A 392 178.626 24.076 541.796 1.00 35.81 C ANISOU 2514 CB ILE A 392 4749 5035 3823 -113 -116 -609 C ATOM 2515 CG1 ILE A 392 177.717 24.755 542.820 1.00 39.56 C ANISOU 2515 CG1 ILE A 392 5428 5478 4124 -59 118 -761 C ATOM 2516 CG2 ILE A 392 179.254 25.111 540.878 1.00 40.39 C ANISOU 2516 CG2 ILE A 392 5332 5442 4572 -262 -187 -772 C ATOM 2517 CD1 ILE A 392 178.433 25.760 543.700 1.00 41.48 C ANISOU 2517 CD1 ILE A 392 5879 5799 4084 -207 58 -1064 C ATOM 2518 N LEU A 393 179.466 21.360 540.293 1.00 34.38 N ANISOU 2518 N LEU A 393 4122 4985 3957 10 -418 -120 N ATOM 2519 CA LEU A 393 180.320 20.676 539.327 1.00 29.74 C ANISOU 2519 CA LEU A 393 3338 4423 3539 4 -582 -51 C ATOM 2520 C LEU A 393 179.496 19.899 538.307 1.00 29.04 C ANISOU 2520 C LEU A 393 3150 4164 3719 116 -514 113 C ATOM 2521 O LEU A 393 179.811 19.911 537.112 1.00 27.13 O ANISOU 2521 O LEU A 393 2815 3840 3652 85 -555 88 O ATOM 2522 CB LEU A 393 181.292 19.744 540.052 1.00 27.39 C ANISOU 2522 CB LEU A 393 2958 4359 3089 44 -792 32 C ATOM 2523 CG LEU A 393 182.321 20.422 540.960 1.00 34.88 C ANISOU 2523 CG LEU A 393 3954 5519 3779 -80 -950 -152 C ATOM 2524 CD1 LEU A 393 183.249 19.390 541.579 1.00 38.40 C ANISOU 2524 CD1 LEU A 393 4289 6193 4109 10 -1215 -35 C ATOM 2525 CD2 LEU A 393 183.109 21.469 540.191 1.00 36.93 C ANISOU 2525 CD2 LEU A 393 4130 5742 4160 -273 -973 -384 C ATOM 2526 N LEU A 394 178.441 19.215 538.758 1.00 27.87 N ANISOU 2526 N LEU A 394 3024 3967 3596 226 -405 273 N ATOM 2527 CA LEU A 394 177.613 18.444 537.834 1.00 31.12 C ANISOU 2527 CA LEU A 394 3326 4215 4284 309 -366 406 C ATOM 2528 C LEU A 394 176.853 19.353 536.877 1.00 30.93 C ANISOU 2528 C LEU A 394 3313 4005 4436 299 -286 311 C ATOM 2529 O LEU A 394 176.687 19.020 535.698 1.00 33.00 O ANISOU 2529 O LEU A 394 3491 4156 4891 321 -351 342 O ATOM 2530 CB LEU A 394 176.646 17.552 538.612 1.00 28.87 C ANISOU 2530 CB LEU A 394 3046 3916 4007 386 -245 595 C ATOM 2531 CG LEU A 394 177.288 16.378 539.353 1.00 35.06 C ANISOU 2531 CG LEU A 394 3840 4817 4662 427 -357 773 C ATOM 2532 CD1 LEU A 394 176.231 15.524 540.031 1.00 34.14 C ANISOU 2532 CD1 LEU A 394 3759 4642 4572 462 -190 991 C ATOM 2533 CD2 LEU A 394 178.132 15.547 538.403 1.00 39.65 C ANISOU 2533 CD2 LEU A 394 4280 5360 5423 471 -556 800 C ATOM 2534 N ALA A 395 176.375 20.500 537.366 1.00 28.59 N ANISOU 2534 N ALA A 395 3136 3661 4065 281 -160 189 N ATOM 2535 CA ALA A 395 175.708 21.453 536.485 1.00 29.08 C ANISOU 2535 CA ALA A 395 3233 3517 4302 301 -121 112 C ATOM 2536 C ALA A 395 176.652 21.942 535.394 1.00 30.34 C ANISOU 2536 C ALA A 395 3431 3627 4471 194 -249 48 C ATOM 2537 O ALA A 395 176.242 22.126 534.242 1.00 28.05 O ANISOU 2537 O ALA A 395 3142 3183 4334 222 -293 81 O ATOM 2538 CB ALA A 395 175.164 22.630 537.297 1.00 20.94 C ANISOU 2538 CB ALA A 395 2340 2421 3197 319 38 -35 C ATOM 2539 N PHE A 396 177.921 22.160 535.741 1.00 33.73 N ANISOU 2539 N PHE A 396 3889 4199 4727 61 -310 -43 N ATOM 2540 CA PHE A 396 178.905 22.596 534.756 1.00 33.37 C ANISOU 2540 CA PHE A 396 3851 4135 4691 -81 -380 -107 C ATOM 2541 C PHE A 396 179.198 21.496 533.743 1.00 30.60 C ANISOU 2541 C PHE A 396 3354 3831 4442 -40 -460 -7 C ATOM 2542 O PHE A 396 179.189 21.737 532.530 1.00 28.52 O ANISOU 2542 O PHE A 396 3132 3459 4245 -78 -465 2 O ATOM 2543 CB PHE A 396 180.185 23.035 535.469 1.00 30.87 C ANISOU 2543 CB PHE A 396 3535 3989 4206 -248 -427 -253 C ATOM 2544 CG PHE A 396 181.355 23.239 534.553 1.00 33.84 C ANISOU 2544 CG PHE A 396 3837 4410 4609 -419 -469 -316 C ATOM 2545 CD1 PHE A 396 181.431 24.358 533.743 1.00 32.95 C ANISOU 2545 CD1 PHE A 396 3874 4110 4536 -568 -395 -372 C ATOM 2546 CD2 PHE A 396 182.387 22.316 534.515 1.00 32.64 C ANISOU 2546 CD2 PHE A 396 3467 4480 4454 -428 -566 -314 C ATOM 2547 CE1 PHE A 396 182.511 24.550 532.903 1.00 35.68 C ANISOU 2547 CE1 PHE A 396 4154 4510 4892 -761 -379 -421 C ATOM 2548 CE2 PHE A 396 183.471 22.501 533.678 1.00 31.36 C ANISOU 2548 CE2 PHE A 396 3195 4385 4335 -590 -556 -396 C ATOM 2549 CZ PHE A 396 183.533 23.620 532.870 1.00 35.72 C ANISOU 2549 CZ PHE A 396 3899 4770 4901 -777 -443 -448 C ATOM 2550 N ILE A 397 179.460 20.279 534.225 1.00 30.63 N ANISOU 2550 N ILE A 397 3215 3980 4443 43 -523 68 N ATOM 2551 CA ILE A 397 179.833 19.185 533.331 1.00 33.86 C ANISOU 2551 CA ILE A 397 3488 4415 4962 96 -596 122 C ATOM 2552 C ILE A 397 178.688 18.845 532.384 1.00 34.50 C ANISOU 2552 C ILE A 397 3593 4316 5201 182 -588 200 C ATOM 2553 O ILE A 397 178.894 18.659 531.179 1.00 31.43 O ANISOU 2553 O ILE A 397 3219 3887 4838 159 -606 170 O ATOM 2554 CB ILE A 397 180.275 17.956 534.149 1.00 34.97 C ANISOU 2554 CB ILE A 397 3503 4693 5092 195 -679 203 C ATOM 2555 CG1 ILE A 397 181.521 18.285 534.972 1.00 35.58 C ANISOU 2555 CG1 ILE A 397 3524 4980 5015 118 -758 110 C ATOM 2556 CG2 ILE A 397 180.539 16.771 533.233 1.00 37.94 C ANISOU 2556 CG2 ILE A 397 3901 5043 5470 254 -625 193 C ATOM 2557 CD1 ILE A 397 181.950 17.175 535.907 1.00 37.39 C ANISOU 2557 CD1 ILE A 397 3688 5335 5182 243 -866 207 C ATOM 2558 N ILE A 398 177.461 18.781 532.907 1.00 33.58 N ANISOU 2558 N ILE A 398 3500 4104 5153 267 -537 279 N ATOM 2559 CA ILE A 398 176.337 18.290 532.115 1.00 32.33 C ANISOU 2559 CA ILE A 398 3417 3829 5038 289 -488 297 C ATOM 2560 C ILE A 398 175.917 19.314 531.064 1.00 33.27 C ANISOU 2560 C ILE A 398 3609 3816 5218 280 -538 266 C ATOM 2561 O ILE A 398 175.553 18.953 529.937 1.00 30.36 O ANISOU 2561 O ILE A 398 3289 3405 4843 263 -577 252 O ATOM 2562 CB ILE A 398 175.168 17.907 533.042 1.00 34.65 C ANISOU 2562 CB ILE A 398 3674 4098 5394 342 -402 367 C ATOM 2563 CG1 ILE A 398 175.534 16.672 533.869 1.00 36.28 C ANISOU 2563 CG1 ILE A 398 3838 4387 5562 355 -389 445 C ATOM 2564 CG2 ILE A 398 173.895 17.670 532.246 1.00 31.90 C ANISOU 2564 CG2 ILE A 398 3341 3653 5129 331 -391 354 C ATOM 2565 CD1 ILE A 398 174.538 16.350 534.957 1.00 41.88 C ANISOU 2565 CD1 ILE A 398 4470 5072 6370 403 -289 575 C ATOM 2566 N THR A 399 175.958 20.603 531.405 1.00 25.27 N ANISOU 2566 N THR A 399 2647 2718 4235 288 -538 246 N ATOM 2567 CA THR A 399 175.540 21.632 530.458 1.00 26.68 C ANISOU 2567 CA THR A 399 2978 2722 4436 287 -581 239 C ATOM 2568 C THR A 399 176.613 21.968 529.427 1.00 32.80 C ANISOU 2568 C THR A 399 3883 3516 5064 141 -608 210 C ATOM 2569 O THR A 399 176.280 22.499 528.361 1.00 36.61 O ANISOU 2569 O THR A 399 4517 3859 5533 142 -677 254 O ATOM 2570 CB THR A 399 175.135 22.908 531.201 1.00 26.76 C ANISOU 2570 CB THR A 399 3107 2613 4446 304 -487 184 C ATOM 2571 OG1 THR A 399 176.189 23.299 532.088 1.00 29.34 O ANISOU 2571 OG1 THR A 399 3486 3057 4605 168 -399 84 O ATOM 2572 CG2 THR A 399 173.859 22.684 532.000 1.00 25.79 C ANISOU 2572 CG2 THR A 399 2852 2457 4490 465 -420 203 C ATOM 2573 N TRP A 400 177.884 21.676 529.713 1.00 28.35 N ANISOU 2573 N TRP A 400 3256 3127 4387 17 -555 142 N ATOM 2574 CA TRP A 400 178.968 22.003 528.795 1.00 27.39 C ANISOU 2574 CA TRP A 400 3213 3053 4142 -150 -519 95 C ATOM 2575 C TRP A 400 179.484 20.808 528.004 1.00 28.45 C ANISOU 2575 C TRP A 400 3222 3317 4270 -129 -548 77 C ATOM 2576 O TRP A 400 180.156 21.008 526.986 1.00 30.13 O ANISOU 2576 O TRP A 400 3516 3562 4372 -248 -492 42 O ATOM 2577 CB TRP A 400 180.144 22.632 529.554 1.00 27.99 C ANISOU 2577 CB TRP A 400 3263 3243 4129 -328 -431 -13 C ATOM 2578 CG TRP A 400 179.921 24.053 529.971 1.00 26.09 C ANISOU 2578 CG TRP A 400 3221 2830 3863 -418 -378 -45 C ATOM 2579 CD1 TRP A 400 178.768 24.595 530.457 1.00 23.47 C ANISOU 2579 CD1 TRP A 400 2995 2316 3607 -284 -390 -14 C ATOM 2580 CD2 TRP A 400 180.877 25.118 529.923 1.00 24.16 C ANISOU 2580 CD2 TRP A 400 3085 2554 3541 -667 -292 -134 C ATOM 2581 NE1 TRP A 400 178.949 25.931 530.723 1.00 21.19 N ANISOU 2581 NE1 TRP A 400 2900 1862 3289 -408 -326 -87 N ATOM 2582 CE2 TRP A 400 180.235 26.277 530.403 1.00 21.98 C ANISOU 2582 CE2 TRP A 400 3017 2040 3296 -663 -271 -154 C ATOM 2583 CE3 TRP A 400 182.215 25.204 529.524 1.00 27.47 C ANISOU 2583 CE3 TRP A 400 3426 3116 3896 -901 -216 -212 C ATOM 2584 CZ2 TRP A 400 180.884 27.506 530.494 1.00 30.20 C ANISOU 2584 CZ2 TRP A 400 4226 2947 4303 -899 -194 -244 C ATOM 2585 CZ3 TRP A 400 182.857 26.426 529.617 1.00 33.73 C ANISOU 2585 CZ3 TRP A 400 4351 3806 4659 -1160 -126 -293 C ATOM 2586 CH2 TRP A 400 182.192 27.559 530.098 1.00 32.69 C ANISOU 2586 CH2 TRP A 400 4463 3403 4556 -1165 -125 -306 C ATOM 2587 N ALA A 401 179.196 19.582 528.441 1.00 27.40 N ANISOU 2587 N ALA A 401 2914 3246 4252 12 -612 95 N ATOM 2588 CA ALA A 401 179.676 18.410 527.712 1.00 32.04 C ANISOU 2588 CA ALA A 401 3393 3915 4867 54 -641 48 C ATOM 2589 C ALA A 401 179.123 18.294 526.293 1.00 33.54 C ANISOU 2589 C ALA A 401 3721 4005 5015 68 -697 48 C ATOM 2590 O ALA A 401 179.906 17.944 525.393 1.00 37.50 O ANISOU 2590 O ALA A 401 4233 4596 5422 14 -643 -45 O ATOM 2591 CB ALA A 401 179.371 17.137 528.512 1.00 28.31 C ANISOU 2591 CB ALA A 401 2845 3463 4449 177 -630 81 C ATOM 2592 N PRO A 402 177.833 18.545 526.016 1.00 36.39 N ANISOU 2592 N PRO A 402 4182 4207 5438 143 -810 131 N ATOM 2593 CA PRO A 402 177.355 18.381 524.629 1.00 34.79 C ANISOU 2593 CA PRO A 402 4123 3937 5160 159 -921 122 C ATOM 2594 C PRO A 402 178.104 19.228 523.615 1.00 32.76 C ANISOU 2594 C PRO A 402 4098 3710 4638 12 -835 107 C ATOM 2595 O PRO A 402 178.455 18.720 522.545 1.00 34.61 O ANISOU 2595 O PRO A 402 4412 4009 4730 -18 -831 31 O ATOM 2596 CB PRO A 402 175.876 18.781 524.721 1.00 33.59 C ANISOU 2596 CB PRO A 402 4011 3633 5118 249 -1041 210 C ATOM 2597 CG PRO A 402 175.503 18.484 526.122 1.00 36.09 C ANISOU 2597 CG PRO A 402 4190 4008 5513 244 -867 198 C ATOM 2598 CD PRO A 402 176.715 18.827 526.936 1.00 34.44 C ANISOU 2598 CD PRO A 402 3914 3869 5303 214 -811 203 C ATOM 2599 N TYR A 403 178.358 20.505 523.912 1.00 22.01 N ANISOU 2599 N TYR A 403 2871 2294 3200 -95 -747 171 N ATOM 2600 CA TYR A 403 179.093 21.340 522.966 1.00 28.31 C ANISOU 2600 CA TYR A 403 3912 3095 3748 -278 -630 187 C ATOM 2601 C TYR A 403 180.491 20.791 522.714 1.00 35.91 C ANISOU 2601 C TYR A 403 4746 4281 4619 -411 -431 45 C ATOM 2602 O TYR A 403 180.987 20.829 521.582 1.00 34.64 O ANISOU 2602 O TYR A 403 4743 4182 4238 -522 -328 17 O ATOM 2603 CB TYR A 403 179.171 22.781 523.476 1.00 24.68 C ANISOU 2603 CB TYR A 403 3606 2494 3278 -390 -559 269 C ATOM 2604 CG TYR A 403 180.077 23.671 522.650 1.00 31.07 C ANISOU 2604 CG TYR A 403 4661 3291 3855 -638 -387 303 C ATOM 2605 CD1 TYR A 403 179.594 24.350 521.537 1.00 32.42 C ANISOU 2605 CD1 TYR A 403 5191 3294 3833 -663 -455 455 C ATOM 2606 CD2 TYR A 403 181.418 23.833 522.983 1.00 33.43 C ANISOU 2606 CD2 TYR A 403 4827 3746 4128 -858 -161 193 C ATOM 2607 CE1 TYR A 403 180.422 25.163 520.779 1.00 34.55 C ANISOU 2607 CE1 TYR A 403 5723 3536 3867 -921 -264 520 C ATOM 2608 CE2 TYR A 403 182.253 24.638 522.227 1.00 32.67 C ANISOU 2608 CE2 TYR A 403 4933 3639 3842 -1129 40 225 C ATOM 2609 CZ TYR A 403 181.749 25.304 521.130 1.00 34.63 C ANISOU 2609 CZ TYR A 403 5578 3703 3878 -1169 8 401 C ATOM 2610 OH TYR A 403 182.576 26.111 520.381 1.00 35.19 O ANISOU 2610 OH TYR A 403 5886 3747 3736 -1468 241 467 O ATOM 2611 N ASN A 404 181.144 20.277 523.755 1.00 32.77 N ANISOU 2611 N ASN A 404 4059 4015 4379 -393 -372 -47 N ATOM 2612 CA ASN A 404 182.528 19.843 523.610 1.00 34.56 C ANISOU 2612 CA ASN A 404 4100 4457 4574 -497 -194 -196 C ATOM 2613 C ASN A 404 182.641 18.522 522.861 1.00 33.47 C ANISOU 2613 C ASN A 404 3871 4405 4441 -369 -205 -312 C ATOM 2614 O ASN A 404 183.656 18.281 522.196 1.00 31.51 O ANISOU 2614 O ASN A 404 3557 4314 4099 -457 -19 -448 O ATOM 2615 CB ASN A 404 183.191 19.748 524.985 1.00 29.84 C ANISOU 2615 CB ASN A 404 3223 3972 4140 -493 -188 -251 C ATOM 2616 CG ASN A 404 183.516 21.107 525.561 1.00 27.68 C ANISOU 2616 CG ASN A 404 3033 3658 3825 -693 -117 -223 C ATOM 2617 OD1 ASN A 404 184.562 21.682 525.262 1.00 25.30 O ANISOU 2617 OD1 ASN A 404 2702 3456 3456 -918 54 -299 O ATOM 2618 ND2 ASN A 404 182.612 21.639 526.377 1.00 28.06 N ANISOU 2618 ND2 ASN A 404 3183 3551 3929 -624 -228 -133 N ATOM 2619 N VAL A 405 181.627 17.657 522.948 1.00 32.09 N ANISOU 2619 N VAL A 405 3681 4122 4390 -174 -399 -283 N ATOM 2620 CA VAL A 405 181.652 16.458 522.118 1.00 37.93 C ANISOU 2620 CA VAL A 405 4391 4891 5130 -70 -423 -419 C ATOM 2621 C VAL A 405 181.312 16.809 520.675 1.00 32.33 C ANISOU 2621 C VAL A 405 3994 4153 4137 -148 -419 -429 C ATOM 2622 O VAL A 405 181.733 16.110 519.745 1.00 32.68 O ANISOU 2622 O VAL A 405 4073 4282 4061 -137 -340 -595 O ATOM 2623 CB VAL A 405 180.715 15.371 522.681 1.00 39.72 C ANISOU 2623 CB VAL A 405 4498 4987 5607 125 -628 -394 C ATOM 2624 CG1 VAL A 405 180.973 15.164 524.167 1.00 37.92 C ANISOU 2624 CG1 VAL A 405 4037 4782 5588 189 -637 -327 C ATOM 2625 CG2 VAL A 405 179.259 15.711 522.418 1.00 43.30 C ANISOU 2625 CG2 VAL A 405 5123 5269 6061 157 -825 -271 C ATOM 2626 N MET A 406 180.562 17.894 520.458 1.00 29.72 N ANISOU 2626 N MET A 406 3913 3700 3679 -213 -509 -258 N ATOM 2627 CA MET A 406 180.364 18.388 519.099 1.00 32.22 C ANISOU 2627 CA MET A 406 4579 3999 3664 -303 -513 -223 C ATOM 2628 C MET A 406 181.681 18.862 518.503 1.00 33.71 C ANISOU 2628 C MET A 406 4849 4351 3606 -519 -187 -288 C ATOM 2629 O MET A 406 181.933 18.677 517.307 1.00 35.64 O ANISOU 2629 O MET A 406 5305 4680 3555 -585 -92 -364 O ATOM 2630 CB MET A 406 179.337 19.521 519.084 1.00 29.36 C ANISOU 2630 CB MET A 406 4461 3441 3255 -299 -696 2 C ATOM 2631 CG MET A 406 177.942 19.116 519.532 1.00 27.30 C ANISOU 2631 CG MET A 406 4094 3033 3244 -95 -1001 55 C ATOM 2632 SD MET A 406 176.843 20.537 519.718 0.73 24.34 S ANISOU 2632 SD MET A 406 3919 2426 2903 -44 -1185 293 S ATOM 2633 CE MET A 406 175.611 19.867 520.834 1.00 27.65 C ANISOU 2633 CE MET A 406 3996 2762 3749 166 -1376 284 C ATOM 2634 N VAL A 407 182.536 19.475 519.327 1.00 32.83 N ANISOU 2634 N VAL A 407 4569 4299 3606 -650 -4 -274 N ATOM 2635 CA VAL A 407 183.863 19.874 518.870 1.00 36.43 C ANISOU 2635 CA VAL A 407 5009 4932 3901 -885 335 -360 C ATOM 2636 C VAL A 407 184.691 18.648 518.513 1.00 39.24 C ANISOU 2636 C VAL A 407 5114 5503 4294 -810 491 -619 C ATOM 2637 O VAL A 407 185.395 18.629 517.495 1.00 45.46 O ANISOU 2637 O VAL A 407 6001 6436 4836 -943 752 -728 O ATOM 2638 CB VAL A 407 184.560 20.735 519.942 1.00 34.35 C ANISOU 2638 CB VAL A 407 4562 4681 3808 -1044 446 -323 C ATOM 2639 CG1 VAL A 407 186.001 21.023 519.549 1.00 36.25 C ANISOU 2639 CG1 VAL A 407 4679 5133 3962 -1306 806 -448 C ATOM 2640 CG2 VAL A 407 183.796 22.031 520.162 1.00 27.50 C ANISOU 2640 CG2 VAL A 407 3994 3565 2891 -1125 333 -97 C ATOM 2641 N LEU A 408 184.617 17.604 519.342 1.00 36.61 N ANISOU 2641 N LEU A 408 4465 5178 4268 -589 347 -721 N ATOM 2642 CA LEU A 408 185.357 16.375 519.068 1.00 38.05 C ANISOU 2642 CA LEU A 408 4402 5509 4547 -463 462 -974 C ATOM 2643 C LEU A 408 184.909 15.741 517.755 1.00 38.58 C ANISOU 2643 C LEU A 408 4728 5557 4371 -404 457 -1092 C ATOM 2644 O LEU A 408 185.740 15.349 516.927 1.00 37.97 O ANISOU 2644 O LEU A 408 4629 5648 4150 -443 719 -1306 O ATOM 2645 CB LEU A 408 185.190 15.397 520.232 1.00 43.86 C ANISOU 2645 CB LEU A 408 4827 6184 5653 -222 256 -998 C ATOM 2646 CG LEU A 408 185.670 13.957 520.039 1.00 58.14 C ANISOU 2646 CG LEU A 408 6414 8039 7636 -11 282 -1234 C ATOM 2647 CD1 LEU A 408 187.120 13.902 519.582 1.00 63.75 C ANISOU 2647 CD1 LEU A 408 6903 8997 8322 -81 610 -1459 C ATOM 2648 CD2 LEU A 408 185.488 13.172 521.328 1.00 61.94 C ANISOU 2648 CD2 LEU A 408 6644 8421 8471 200 64 -1173 C ATOM 2649 N ILE A 409 183.594 15.630 517.549 1.00 34.08 N ANISOU 2649 N ILE A 409 4396 4799 3754 -310 160 -979 N ATOM 2650 CA ILE A 409 183.087 15.072 516.298 1.00 37.79 C ANISOU 2650 CA ILE A 409 5140 5251 3966 -267 91 -1103 C ATOM 2651 C ILE A 409 183.405 15.997 515.130 1.00 41.58 C ANISOU 2651 C ILE A 409 5989 5839 3970 -488 295 -1053 C ATOM 2652 O ILE A 409 183.622 15.535 514.002 1.00 39.81 O ANISOU 2652 O ILE A 409 5959 5720 3447 -506 414 -1237 O ATOM 2653 CB ILE A 409 181.575 14.797 516.414 1.00 37.80 C ANISOU 2653 CB ILE A 409 5258 5035 4071 -132 -314 -991 C ATOM 2654 CG1 ILE A 409 181.301 13.803 517.544 1.00 41.48 C ANISOU 2654 CG1 ILE A 409 5382 5388 4991 53 -460 -1028 C ATOM 2655 CG2 ILE A 409 181.019 14.256 515.104 1.00 36.15 C ANISOU 2655 CG2 ILE A 409 5343 4815 3577 -105 -444 -1138 C ATOM 2656 CD1 ILE A 409 179.831 13.503 517.753 1.00 46.12 C ANISOU 2656 CD1 ILE A 409 6012 5770 5742 152 -812 -926 C ATOM 2657 N ASN A 410 183.459 17.308 515.377 1.00 38.96 N ANISOU 2657 N ASN A 410 5788 5471 3546 -666 354 -808 N ATOM 2658 CA ASN A 410 183.756 18.265 514.317 1.00 42.96 C ANISOU 2658 CA ASN A 410 6689 6036 3598 -903 557 -699 C ATOM 2659 C ASN A 410 185.168 18.104 513.767 1.00 48.70 C ANISOU 2659 C ASN A 410 7312 7025 4168 -1073 1030 -908 C ATOM 2660 O ASN A 410 185.437 18.545 512.644 1.00 45.79 O ANISOU 2660 O ASN A 410 7299 6748 3352 -1258 1250 -881 O ATOM 2661 CB ASN A 410 183.546 19.692 514.836 1.00 41.09 C ANISOU 2661 CB ASN A 410 6592 5643 3378 -1055 522 -393 C ATOM 2662 CG ASN A 410 183.736 20.743 513.760 1.00 46.24 C ANISOU 2662 CG ASN A 410 7719 6285 3564 -1304 699 -212 C ATOM 2663 OD1 ASN A 410 182.894 20.903 512.876 1.00 50.34 O ANISOU 2663 OD1 ASN A 410 8649 6713 3763 -1257 483 -86 O ATOM 2664 ND2 ASN A 410 184.840 21.476 513.838 1.00 49.33 N ANISOU 2664 ND2 ASN A 410 8061 6766 3917 -1584 1080 -187 N ATOM 2665 N THR A 411 186.074 17.475 514.523 1.00 47.80 N ANISOU 2665 N THR A 411 6716 7041 4406 -1008 1194 -1112 N ATOM 2666 CA THR A 411 187.447 17.313 514.050 1.00 50.86 C ANISOU 2666 CA THR A 411 6915 7695 4715 -1151 1657 -1339 C ATOM 2667 C THR A 411 187.528 16.398 512.835 1.00 49.84 C ANISOU 2667 C THR A 411 6957 7690 4291 -1067 1800 -1605 C ATOM 2668 O THR A 411 188.411 16.573 511.989 1.00 50.39 O ANISOU 2668 O THR A 411 7094 7975 4076 -1254 2229 -1737 O ATOM 2669 CB THR A 411 188.337 16.763 515.165 1.00 53.39 C ANISOU 2669 CB THR A 411 6644 8120 5521 -1040 1722 -1507 C ATOM 2670 OG1 THR A 411 187.968 15.408 515.451 1.00 56.15 O ANISOU 2670 OG1 THR A 411 6808 8403 6124 -706 1493 -1687 O ATOM 2671 CG2 THR A 411 188.184 17.594 516.417 1.00 44.37 C ANISOU 2671 CG2 THR A 411 5361 6860 4636 -1107 1539 -1279 C ATOM 2672 N PHE A 412 186.630 15.418 512.732 1.00 45.64 N ANISOU 2672 N PHE A 412 4739 6445 6157 -186 1207 -591 N ATOM 2673 CA PHE A 412 186.669 14.458 511.640 1.00 48.43 C ANISOU 2673 CA PHE A 412 5286 6703 6413 -133 1321 -668 C ATOM 2674 C PHE A 412 185.399 14.422 510.801 1.00 49.20 C ANISOU 2674 C PHE A 412 5803 6615 6276 -267 1271 -474 C ATOM 2675 O PHE A 412 185.421 13.838 509.711 1.00 47.66 O ANISOU 2675 O PHE A 412 5803 6354 5953 -278 1398 -559 O ATOM 2676 CB PHE A 412 186.962 13.046 512.177 1.00 49.32 C ANISOU 2676 CB PHE A 412 5339 6771 6629 228 1154 -752 C ATOM 2677 CG PHE A 412 185.973 12.564 513.204 1.00 48.12 C ANISOU 2677 CG PHE A 412 5365 6450 6469 356 868 -522 C ATOM 2678 CD1 PHE A 412 186.185 12.796 514.555 1.00 48.00 C ANISOU 2678 CD1 PHE A 412 5173 6510 6553 528 683 -482 C ATOM 2679 CD2 PHE A 412 184.837 11.869 512.820 1.00 44.03 C ANISOU 2679 CD2 PHE A 412 5194 5702 5835 284 814 -390 C ATOM 2680 CE1 PHE A 412 185.277 12.349 515.502 1.00 47.68 C ANISOU 2680 CE1 PHE A 412 5362 6281 6472 616 489 -274 C ATOM 2681 CE2 PHE A 412 183.927 11.420 513.761 1.00 42.23 C ANISOU 2681 CE2 PHE A 412 5133 5301 5609 327 643 -228 C ATOM 2682 CZ PHE A 412 184.147 11.661 515.102 1.00 44.07 C ANISOU 2682 CZ PHE A 412 5250 5575 5919 490 501 -151 C ATOM 2683 N CYS A 413 184.301 15.024 511.263 1.00 50.39 N ANISOU 2683 N CYS A 413 6074 6709 6362 -346 1076 -261 N ATOM 2684 CA CYS A 413 183.065 15.045 510.483 1.00 47.59 C ANISOU 2684 CA CYS A 413 6045 6250 5787 -423 972 -159 C ATOM 2685 C CYS A 413 182.331 16.345 510.798 1.00 47.43 C ANISOU 2685 C CYS A 413 6097 6247 5677 -521 866 5 C ATOM 2686 O CYS A 413 181.559 16.409 511.760 1.00 47.85 O ANISOU 2686 O CYS A 413 6056 6303 5821 -489 647 105 O ATOM 2687 CB CYS A 413 182.194 13.834 510.785 1.00 43.87 C ANISOU 2687 CB CYS A 413 5634 5671 5362 -335 776 -157 C ATOM 2688 SG CYS A 413 180.655 13.802 509.838 0.80 42.72 S ANISOU 2688 SG CYS A 413 5758 5489 4983 -427 608 -171 S ATOM 2689 N ALA A 414 182.558 17.362 509.974 1.00 50.27 N ANISOU 2689 N ALA A 414 6678 6589 5834 -631 1049 24 N ATOM 2690 CA ALA A 414 181.863 18.637 510.111 1.00 49.31 C ANISOU 2690 CA ALA A 414 6741 6430 5566 -672 962 178 C ATOM 2691 C ALA A 414 180.380 18.522 509.752 1.00 48.91 C ANISOU 2691 C ALA A 414 6893 6366 5326 -546 641 231 C ATOM 2692 O ALA A 414 179.546 19.108 510.453 1.00 52.14 O ANISOU 2692 O ALA A 414 7247 6803 5761 -500 424 320 O ATOM 2693 CB ALA A 414 182.541 19.714 509.259 1.00 50.08 C ANISOU 2693 CB ALA A 414 7155 6431 5441 -818 1307 182 C ATOM 2694 N PRO A 415 179.996 17.807 508.684 1.00 47.78 N ANISOU 2694 N PRO A 415 6950 6210 4993 -480 591 129 N ATOM 2695 CA PRO A 415 178.556 17.649 508.409 1.00 50.58 C ANISOU 2695 CA PRO A 415 7387 6625 5205 -354 245 74 C ATOM 2696 C PRO A 415 177.800 16.888 509.486 1.00 47.60 C ANISOU 2696 C PRO A 415 6653 6315 5117 -387 47 14 C ATOM 2697 O PRO A 415 176.564 16.924 509.487 1.00 55.30 O ANISOU 2697 O PRO A 415 7586 7385 6039 -327 -221 -85 O ATOM 2698 CB PRO A 415 178.529 16.890 507.075 1.00 52.21 C ANISOU 2698 CB PRO A 415 7838 6819 5179 -303 270 -83 C ATOM 2699 CG PRO A 415 179.824 17.208 506.436 1.00 43.86 C ANISOU 2699 CG PRO A 415 6998 5660 4006 -382 653 -37 C ATOM 2700 CD PRO A 415 180.806 17.285 507.565 1.00 47.55 C ANISOU 2700 CD PRO A 415 7107 6132 4826 -512 849 18 C ATOM 2701 N CYS A 416 178.492 16.194 510.393 1.00 48.57 N ANISOU 2701 N CYS A 416 6541 6391 5522 -464 180 38 N ATOM 2702 CA CYS A 416 177.815 15.437 511.439 1.00 43.64 C ANISOU 2702 CA CYS A 416 5706 5755 5121 -511 69 1 C ATOM 2703 C CYS A 416 177.161 16.325 512.487 1.00 42.28 C ANISOU 2703 C CYS A 416 5388 5648 5027 -520 -71 104 C ATOM 2704 O CYS A 416 176.378 15.817 513.296 1.00 43.99 O ANISOU 2704 O CYS A 416 5468 5860 5388 -590 -142 50 O ATOM 2705 CB CYS A 416 178.796 14.487 512.124 1.00 45.33 C ANISOU 2705 CB CYS A 416 5830 5858 5534 -498 235 20 C ATOM 2706 SG CYS A 416 179.287 13.052 511.136 0.90 48.29 S ANISOU 2706 SG CYS A 416 6357 6115 5875 -472 379 -154 S ATOM 2707 N ILE A 417 177.462 17.617 512.501 1.00 34.80 N ANISOU 2707 N ILE A 417 4501 4736 3984 -474 -67 234 N ATOM 2708 CA ILE A 417 176.888 18.559 513.451 1.00 39.76 C ANISOU 2708 CA ILE A 417 5019 5417 4670 -461 -192 326 C ATOM 2709 C ILE A 417 176.217 19.677 512.665 1.00 43.10 C ANISOU 2709 C ILE A 417 5668 5881 4827 -333 -340 332 C ATOM 2710 O ILE A 417 176.887 20.550 512.112 1.00 46.65 O ANISOU 2710 O ILE A 417 6380 6246 5098 -304 -206 436 O ATOM 2711 CB ILE A 417 177.957 19.119 514.408 1.00 38.14 C ANISOU 2711 CB ILE A 417 4701 5182 4607 -503 -44 460 C ATOM 2712 CG1 ILE A 417 178.844 17.984 514.944 1.00 34.36 C ANISOU 2712 CG1 ILE A 417 4079 4667 4311 -508 73 426 C ATOM 2713 CG2 ILE A 417 177.293 19.848 515.560 1.00 29.47 C ANISOU 2713 CG2 ILE A 417 3471 4130 3597 -499 -175 534 C ATOM 2714 CD1 ILE A 417 178.120 17.018 515.848 1.00 35.83 C ANISOU 2714 CD1 ILE A 417 4189 4804 4621 -514 -12 408 C ATOM 2715 N PRO A 418 174.890 19.663 512.564 1.00 40.54 N ANISOU 2715 N PRO A 418 5277 5680 4448 -238 -604 188 N ATOM 2716 CA PRO A 418 174.191 20.771 511.901 1.00 39.96 C ANISOU 2716 CA PRO A 418 5444 5657 4083 2 -819 176 C ATOM 2717 C PRO A 418 174.281 22.056 512.714 1.00 38.40 C ANISOU 2717 C PRO A 418 5292 5399 3901 49 -805 355 C ATOM 2718 O PRO A 418 174.629 22.060 513.897 1.00 40.99 O ANISOU 2718 O PRO A 418 5377 5711 4488 -107 -694 440 O ATOM 2719 CB PRO A 418 172.743 20.275 511.805 1.00 39.95 C ANISOU 2719 CB PRO A 418 5200 5877 4104 90 -1127 -125 C ATOM 2720 CG PRO A 418 172.825 18.788 511.965 1.00 40.93 C ANISOU 2720 CG PRO A 418 5096 5999 4458 -160 -992 -271 C ATOM 2721 CD PRO A 418 173.983 18.542 512.877 1.00 38.43 C ANISOU 2721 CD PRO A 418 4745 5506 4351 -338 -700 -33 C ATOM 2722 N ASN A 419 173.951 23.169 512.051 1.00 39.41 N ANISOU 2722 N ASN A 419 5794 5471 3707 300 -928 405 N ATOM 2723 CA ASN A 419 174.018 24.471 512.711 1.00 44.38 C ANISOU 2723 CA ASN A 419 6562 5989 4310 361 -896 566 C ATOM 2724 C ASN A 419 173.037 24.560 513.874 1.00 46.47 C ANISOU 2724 C ASN A 419 6419 6428 4808 395 -1109 468 C ATOM 2725 O ASN A 419 173.332 25.191 514.896 1.00 46.68 O ANISOU 2725 O ASN A 419 6360 6390 4987 297 -1002 590 O ATOM 2726 CB ASN A 419 173.754 25.590 511.702 1.00 52.91 C ANISOU 2726 CB ASN A 419 8249 6917 4937 686 -991 635 C ATOM 2727 CG ASN A 419 173.707 26.961 512.351 1.00 66.69 C ANISOU 2727 CG ASN A 419 10208 8501 6630 777 -960 783 C ATOM 2728 OD1 ASN A 419 174.741 27.593 512.568 1.00 74.03 O ANISOU 2728 OD1 ASN A 419 11360 9193 7574 554 -604 952 O ATOM 2729 ND2 ASN A 419 172.503 27.427 512.665 1.00 70.05 N ANISOU 2729 ND2 ASN A 419 10544 9067 7006 1096 -1320 671 N ATOM 2730 N THR A 420 171.861 23.942 513.734 1.00 45.20 N ANISOU 2730 N THR A 420 5989 6504 4682 511 -1387 203 N ATOM 2731 CA THR A 420 170.888 23.953 514.823 1.00 44.98 C ANISOU 2731 CA THR A 420 5541 6659 4891 492 -1525 47 C ATOM 2732 C THR A 420 171.432 23.236 516.053 1.00 39.63 C ANISOU 2732 C THR A 420 4571 5933 4554 134 -1261 135 C ATOM 2733 O THR A 420 171.197 23.667 517.188 1.00 42.06 O ANISOU 2733 O THR A 420 4704 6261 5015 81 -1237 172 O ATOM 2734 CB THR A 420 169.576 23.315 514.362 1.00 46.22 C ANISOU 2734 CB THR A 420 5404 7108 5049 615 -1815 -353 C ATOM 2735 OG1 THR A 420 169.084 24.010 513.210 1.00 50.38 O ANISOU 2735 OG1 THR A 420 6244 7700 5197 1054 -2130 -453 O ATOM 2736 CG2 THR A 420 168.530 23.387 515.464 1.00 45.29 C ANISOU 2736 CG2 THR A 420 4830 7196 5182 565 -1900 -575 C ATOM 2737 N VAL A 421 172.171 22.143 515.846 1.00 35.12 N ANISOU 2737 N VAL A 421 3989 5286 4070 -72 -1072 165 N ATOM 2738 CA VAL A 421 172.761 21.416 516.966 1.00 36.16 C ANISOU 2738 CA VAL A 421 3948 5339 4452 -317 -851 257 C ATOM 2739 C VAL A 421 173.844 22.251 517.641 1.00 35.25 C ANISOU 2739 C VAL A 421 3929 5103 4360 -334 -713 498 C ATOM 2740 O VAL A 421 173.964 22.254 518.872 1.00 36.46 O ANISOU 2740 O VAL A 421 3933 5249 4670 -420 -649 558 O ATOM 2741 CB VAL A 421 173.301 20.056 516.487 1.00 37.03 C ANISOU 2741 CB VAL A 421 4084 5374 4611 -450 -708 211 C ATOM 2742 CG1 VAL A 421 174.035 19.343 517.609 1.00 28.79 C ANISOU 2742 CG1 VAL A 421 2977 4210 3754 -593 -509 327 C ATOM 2743 CG2 VAL A 421 172.159 19.197 515.966 1.00 33.70 C ANISOU 2743 CG2 VAL A 421 3524 5074 4206 -503 -815 -94 C ATOM 2744 N TRP A 422 174.651 22.967 516.851 1.00 35.44 N ANISOU 2744 N TRP A 422 4221 5028 4216 -271 -639 607 N ATOM 2745 CA TRP A 422 175.647 23.868 517.426 1.00 35.32 C ANISOU 2745 CA TRP A 422 4270 4915 4237 -340 -477 752 C ATOM 2746 C TRP A 422 174.989 24.919 518.312 1.00 35.45 C ANISOU 2746 C TRP A 422 4247 4949 4273 -270 -586 785 C ATOM 2747 O TRP A 422 175.458 25.195 519.423 1.00 29.69 O ANISOU 2747 O TRP A 422 3373 4216 3690 -368 -509 837 O ATOM 2748 CB TRP A 422 176.459 24.542 516.317 1.00 35.20 C ANISOU 2748 CB TRP A 422 4608 4757 4012 -340 -306 813 C ATOM 2749 CG TRP A 422 177.556 23.699 515.736 1.00 34.19 C ANISOU 2749 CG TRP A 422 4463 4606 3921 -466 -95 777 C ATOM 2750 CD1 TRP A 422 177.630 23.216 514.462 1.00 33.79 C ANISOU 2750 CD1 TRP A 422 4629 4518 3691 -426 -49 731 C ATOM 2751 CD2 TRP A 422 178.742 23.247 516.405 1.00 36.78 C ANISOU 2751 CD2 TRP A 422 4538 4971 4468 -607 80 744 C ATOM 2752 NE1 TRP A 422 178.785 22.492 514.295 1.00 37.63 N ANISOU 2752 NE1 TRP A 422 5003 5004 4291 -558 175 677 N ATOM 2753 CE2 TRP A 422 179.485 22.495 515.473 1.00 39.06 C ANISOU 2753 CE2 TRP A 422 4879 5244 4720 -647 240 670 C ATOM 2754 CE3 TRP A 422 179.245 23.405 517.701 1.00 31.74 C ANISOU 2754 CE3 TRP A 422 3631 4397 4032 -662 90 739 C ATOM 2755 CZ2 TRP A 422 180.704 21.900 515.795 1.00 38.35 C ANISOU 2755 CZ2 TRP A 422 4547 5217 4808 -714 397 569 C ATOM 2756 CZ3 TRP A 422 180.456 22.814 518.019 1.00 34.91 C ANISOU 2756 CZ3 TRP A 422 3808 4871 4584 -707 213 637 C ATOM 2757 CH2 TRP A 422 181.172 22.071 517.070 1.00 40.21 C ANISOU 2757 CH2 TRP A 422 4502 5541 5235 -721 361 543 C ATOM 2758 N THR A 423 173.899 25.522 517.828 1.00 31.99 N ANISOU 2758 N THR A 423 3938 4546 3669 -60 -791 726 N ATOM 2759 CA THR A 423 173.189 26.529 518.611 1.00 36.99 C ANISOU 2759 CA THR A 423 4540 5202 4313 58 -912 725 C ATOM 2760 C THR A 423 172.678 25.950 519.925 1.00 38.00 C ANISOU 2760 C THR A 423 4273 5473 4693 -64 -932 645 C ATOM 2761 O THR A 423 172.739 26.611 520.969 1.00 32.51 O ANISOU 2761 O THR A 423 3515 4758 4080 -96 -895 701 O ATOM 2762 CB THR A 423 172.032 27.107 517.795 1.00 43.56 C ANISOU 2762 CB THR A 423 5549 6092 4909 399 -1189 608 C ATOM 2763 OG1 THR A 423 172.537 27.673 516.578 1.00 44.32 O ANISOU 2763 OG1 THR A 423 6153 5992 4693 538 -1138 716 O ATOM 2764 CG2 THR A 423 171.306 28.188 518.584 1.00 45.37 C ANISOU 2764 CG2 THR A 423 5755 6340 5143 574 -1318 585 C ATOM 2765 N ILE A 424 172.173 24.714 519.893 1.00 41.45 N ANISOU 2765 N ILE A 424 4488 6025 5234 -153 -953 503 N ATOM 2766 CA ILE A 424 171.679 24.084 521.115 1.00 40.64 C ANISOU 2766 CA ILE A 424 4115 5997 5331 -310 -887 426 C ATOM 2767 C ILE A 424 172.820 23.864 522.101 1.00 37.10 C ANISOU 2767 C ILE A 424 3694 5430 4970 -444 -706 609 C ATOM 2768 O ILE A 424 172.688 24.147 523.298 1.00 37.77 O ANISOU 2768 O ILE A 424 3697 5526 5128 -484 -669 638 O ATOM 2769 CB ILE A 424 170.952 22.768 520.781 1.00 37.31 C ANISOU 2769 CB ILE A 424 3529 5659 4987 -434 -869 209 C ATOM 2770 CG1 ILE A 424 169.713 23.048 519.927 1.00 44.11 C ANISOU 2770 CG1 ILE A 424 4262 6725 5772 -265 -1110 -76 C ATOM 2771 CG2 ILE A 424 170.566 22.030 522.056 1.00 28.12 C ANISOU 2771 CG2 ILE A 424 2212 4481 3993 -655 -688 152 C ATOM 2772 CD1 ILE A 424 169.025 21.801 519.421 1.00 49.07 C ANISOU 2772 CD1 ILE A 424 4702 7462 6481 -420 -1092 -373 C ATOM 2773 N GLY A 425 173.960 23.366 521.616 1.00 36.24 N ANISOU 2773 N GLY A 425 3693 5234 4842 -481 -608 699 N ATOM 2774 CA GLY A 425 175.099 23.164 522.499 1.00 34.06 C ANISOU 2774 CA GLY A 425 3401 4904 4636 -528 -498 801 C ATOM 2775 C GLY A 425 175.632 24.464 523.069 1.00 38.25 C ANISOU 2775 C GLY A 425 3936 5435 5162 -511 -497 862 C ATOM 2776 O GLY A 425 176.051 24.521 524.230 1.00 41.55 O ANISOU 2776 O GLY A 425 4273 5874 5639 -521 -483 885 O ATOM 2777 N TYR A 426 175.636 25.522 522.255 1.00 36.16 N ANISOU 2777 N TYR A 426 3819 5123 4797 -477 -502 875 N ATOM 2778 CA TYR A 426 176.035 26.839 522.739 1.00 36.38 C ANISOU 2778 CA TYR A 426 3913 5097 4813 -499 -456 908 C ATOM 2779 C TYR A 426 175.091 27.333 523.827 1.00 44.05 C ANISOU 2779 C TYR A 426 4794 6120 5822 -441 -565 896 C ATOM 2780 O TYR A 426 175.528 27.926 524.822 1.00 39.63 O ANISOU 2780 O TYR A 426 4179 5562 5316 -491 -529 900 O ATOM 2781 CB TYR A 426 176.070 27.828 521.575 1.00 35.97 C ANISOU 2781 CB TYR A 426 4183 4898 4586 -458 -398 940 C ATOM 2782 CG TYR A 426 177.298 28.704 521.532 1.00 33.35 C ANISOU 2782 CG TYR A 426 3977 4440 4253 -629 -159 937 C ATOM 2783 CD1 TYR A 426 178.502 28.216 521.046 1.00 32.85 C ANISOU 2783 CD1 TYR A 426 3852 4386 4243 -785 36 873 C ATOM 2784 CD2 TYR A 426 177.250 30.024 521.960 1.00 30.02 C ANISOU 2784 CD2 TYR A 426 3726 3889 3790 -654 -98 949 C ATOM 2785 CE1 TYR A 426 179.627 29.012 520.994 1.00 29.40 C ANISOU 2785 CE1 TYR A 426 3467 3864 3838 -1005 309 781 C ATOM 2786 CE2 TYR A 426 178.372 30.830 521.912 1.00 34.10 C ANISOU 2786 CE2 TYR A 426 4357 4273 4326 -887 184 885 C ATOM 2787 CZ TYR A 426 179.558 30.319 521.428 1.00 30.40 C ANISOU 2787 CZ TYR A 426 3773 3847 3932 -1083 398 780 C ATOM 2788 OH TYR A 426 180.679 31.116 521.379 1.00 32.70 O ANISOU 2788 OH TYR A 426 4113 4037 4276 -1377 731 630 O ATOM 2789 N TRP A 427 173.788 27.094 523.655 1.00 43.77 N ANISOU 2789 N TRP A 427 4712 6155 5763 -340 -693 830 N ATOM 2790 CA TRP A 427 172.807 27.582 524.618 1.00 39.85 C ANISOU 2790 CA TRP A 427 4099 5733 5310 -286 -768 766 C ATOM 2791 C TRP A 427 172.871 26.803 525.924 1.00 38.00 C ANISOU 2791 C TRP A 427 3704 5550 5185 -413 -683 765 C ATOM 2792 O TRP A 427 172.723 27.385 527.004 1.00 40.82 O ANISOU 2792 O TRP A 427 4023 5924 5563 -415 -672 764 O ATOM 2793 CB TRP A 427 171.403 27.512 524.021 1.00 38.91 C ANISOU 2793 CB TRP A 427 3897 5732 5155 -138 -926 599 C ATOM 2794 CG TRP A 427 170.933 28.822 523.492 1.00 35.35 C ANISOU 2794 CG TRP A 427 3638 5238 4556 120 -1075 580 C ATOM 2795 CD1 TRP A 427 170.774 29.169 522.184 1.00 41.83 C ANISOU 2795 CD1 TRP A 427 4710 6004 5178 337 -1202 571 C ATOM 2796 CD2 TRP A 427 170.573 29.974 524.262 1.00 36.64 C ANISOU 2796 CD2 TRP A 427 3840 5371 4710 233 -1112 571 C ATOM 2797 NE1 TRP A 427 170.329 30.465 522.091 1.00 48.16 N ANISOU 2797 NE1 TRP A 427 5753 6719 5828 612 -1322 570 N ATOM 2798 CE2 TRP A 427 170.198 30.982 523.354 1.00 45.10 C ANISOU 2798 CE2 TRP A 427 5220 6344 5572 544 -1264 564 C ATOM 2799 CE3 TRP A 427 170.527 30.249 525.633 1.00 39.49 C ANISOU 2799 CE3 TRP A 427 4053 5761 5189 128 -1031 565 C ATOM 2800 CZ2 TRP A 427 169.784 32.245 523.770 1.00 45.66 C ANISOU 2800 CZ2 TRP A 427 5454 6326 5567 757 -1333 551 C ATOM 2801 CZ3 TRP A 427 170.115 31.505 526.044 1.00 42.03 C ANISOU 2801 CZ3 TRP A 427 4485 6027 5457 303 -1094 537 C ATOM 2802 CH2 TRP A 427 169.749 32.487 525.116 1.00 43.84 C ANISOU 2802 CH2 TRP A 427 5021 6140 5497 616 -1241 530 C ATOM 2803 N LEU A 428 173.079 25.486 525.846 1.00 34.03 N ANISOU 2803 N LEU A 428 3172 5041 4717 -499 -611 766 N ATOM 2804 CA LEU A 428 173.199 24.683 527.059 1.00 36.69 C ANISOU 2804 CA LEU A 428 3506 5354 5082 -573 -508 795 C ATOM 2805 C LEU A 428 174.334 25.184 527.943 1.00 36.26 C ANISOU 2805 C LEU A 428 3493 5286 4999 -521 -521 882 C ATOM 2806 O LEU A 428 174.216 25.190 529.174 1.00 35.93 O ANISOU 2806 O LEU A 428 3478 5249 4926 -514 -494 894 O ATOM 2807 CB LEU A 428 173.407 23.212 526.698 1.00 40.18 C ANISOU 2807 CB LEU A 428 4023 5717 5525 -633 -415 799 C ATOM 2808 CG LEU A 428 172.190 22.498 526.106 1.00 51.58 C ANISOU 2808 CG LEU A 428 5394 7186 7018 -752 -358 634 C ATOM 2809 CD1 LEU A 428 172.548 21.070 525.737 1.00 55.94 C ANISOU 2809 CD1 LEU A 428 6086 7604 7564 -825 -236 643 C ATOM 2810 CD2 LEU A 428 171.030 22.531 527.086 1.00 55.40 C ANISOU 2810 CD2 LEU A 428 5787 7715 7548 -872 -248 505 C ATOM 2811 N CYS A 429 175.447 25.601 527.332 1.00 27.64 N ANISOU 2811 N CYS A 429 2401 4190 3910 -497 -546 902 N ATOM 2812 CA CYS A 429 176.524 26.214 528.101 1.00 31.06 C ANISOU 2812 CA CYS A 429 2786 4667 4349 -475 -566 881 C ATOM 2813 C CYS A 429 176.050 27.490 528.785 1.00 33.88 C ANISOU 2813 C CYS A 429 3140 5032 4702 -496 -588 856 C ATOM 2814 O CYS A 429 176.403 27.754 529.941 1.00 36.16 O ANISOU 2814 O CYS A 429 3393 5374 4971 -469 -621 822 O ATOM 2815 CB CYS A 429 177.722 26.506 527.198 1.00 27.32 C ANISOU 2815 CB CYS A 429 2268 4200 3913 -523 -515 823 C ATOM 2816 SG CYS A 429 178.488 25.061 526.428 0.81 26.95 S ANISOU 2816 SG CYS A 429 2199 4161 3878 -463 -487 809 S ATOM 2817 N TYR A 430 175.256 28.301 528.082 1.00 28.76 N ANISOU 2817 N TYR A 430 2557 4328 4043 -500 -589 858 N ATOM 2818 CA TYR A 430 174.673 29.484 528.705 1.00 31.01 C ANISOU 2818 CA TYR A 430 2873 4594 4313 -472 -614 827 C ATOM 2819 C TYR A 430 173.742 29.100 529.849 1.00 30.30 C ANISOU 2819 C TYR A 430 2702 4584 4226 -446 -628 799 C ATOM 2820 O TYR A 430 173.714 29.770 530.888 1.00 28.21 O ANISOU 2820 O TYR A 430 2436 4337 3947 -440 -629 766 O ATOM 2821 CB TYR A 430 173.919 30.313 527.665 1.00 35.73 C ANISOU 2821 CB TYR A 430 3620 5104 4853 -377 -651 825 C ATOM 2822 CG TYR A 430 174.800 31.089 526.712 1.00 35.33 C ANISOU 2822 CG TYR A 430 3794 4890 4740 -427 -556 859 C ATOM 2823 CD1 TYR A 430 176.116 31.394 527.035 1.00 34.30 C ANISOU 2823 CD1 TYR A 430 3637 4730 4666 -606 -420 817 C ATOM 2824 CD2 TYR A 430 174.308 31.526 525.489 1.00 31.94 C ANISOU 2824 CD2 TYR A 430 3623 4337 4176 -294 -584 894 C ATOM 2825 CE1 TYR A 430 176.918 32.109 526.162 1.00 26.75 C ANISOU 2825 CE1 TYR A 430 2898 3602 3664 -733 -237 800 C ATOM 2826 CE2 TYR A 430 175.100 32.241 524.611 1.00 30.22 C ANISOU 2826 CE2 TYR A 430 3724 3905 3852 -366 -421 936 C ATOM 2827 CZ TYR A 430 176.405 32.530 524.952 1.00 34.37 C ANISOU 2827 CZ TYR A 430 4212 4382 4467 -628 -208 886 C ATOM 2828 OH TYR A 430 177.194 33.243 524.077 1.00 30.00 O ANISOU 2828 OH TYR A 430 3985 3594 3819 -780 47 883 O ATOM 2829 N ILE A 431 172.980 28.014 529.679 1.00 29.73 N ANISOU 2829 N ILE A 431 2581 4547 4167 -463 -598 784 N ATOM 2830 CA ILE A 431 172.015 27.591 530.693 1.00 32.21 C ANISOU 2830 CA ILE A 431 2849 4908 4481 -509 -515 720 C ATOM 2831 C ILE A 431 172.710 27.268 532.009 1.00 35.41 C ANISOU 2831 C ILE A 431 3369 5286 4800 -514 -462 789 C ATOM 2832 O ILE A 431 172.102 27.371 533.083 1.00 33.38 O ANISOU 2832 O ILE A 431 3147 5043 4494 -539 -377 749 O ATOM 2833 CB ILE A 431 171.186 26.397 530.169 1.00 36.92 C ANISOU 2833 CB ILE A 431 3387 5518 5121 -604 -423 640 C ATOM 2834 CG1 ILE A 431 170.377 26.811 528.938 1.00 45.47 C ANISOU 2834 CG1 ILE A 431 4330 6690 6258 -531 -543 505 C ATOM 2835 CG2 ILE A 431 170.247 25.860 531.238 1.00 37.14 C ANISOU 2835 CG2 ILE A 431 3404 5557 5150 -739 -226 539 C ATOM 2836 CD1 ILE A 431 169.576 28.072 529.136 1.00 49.27 C ANISOU 2836 CD1 ILE A 431 4717 7257 6745 -390 -645 388 C ATOM 2837 N ASN A 432 173.991 26.884 531.953 1.00 33.47 N ANISOU 2837 N ASN A 432 3186 5017 4513 -457 -521 862 N ATOM 2838 CA ASN A 432 174.765 26.670 533.173 1.00 34.95 C ANISOU 2838 CA ASN A 432 3485 5218 4575 -359 -558 884 C ATOM 2839 C ASN A 432 174.678 27.874 534.104 1.00 35.09 C ANISOU 2839 C ASN A 432 3467 5298 4566 -350 -600 816 C ATOM 2840 O ASN A 432 174.557 27.719 535.325 1.00 28.11 O ANISOU 2840 O ASN A 432 2721 4418 3540 -291 -578 819 O ATOM 2841 CB ASN A 432 176.225 26.371 532.821 1.00 34.19 C ANISOU 2841 CB ASN A 432 3344 5169 4478 -252 -676 870 C ATOM 2842 CG ASN A 432 177.065 26.034 534.040 1.00 35.31 C ANISOU 2842 CG ASN A 432 3591 5371 4456 -50 -792 840 C ATOM 2843 OD1 ASN A 432 176.539 25.660 535.088 1.00 38.19 O ANISOU 2843 OD1 ASN A 432 4188 5671 4652 18 -744 900 O ATOM 2844 ND2 ASN A 432 178.380 26.160 533.905 1.00 36.97 N ANISOU 2844 ND2 ASN A 432 3636 5715 4695 62 -939 712 N ATOM 2845 N SER A 433 174.728 29.083 533.542 1.00 29.60 N ANISOU 2845 N SER A 433 2653 4618 3975 -401 -639 755 N ATOM 2846 CA SER A 433 174.622 30.286 534.360 1.00 30.08 C ANISOU 2846 CA SER A 433 2708 4702 4019 -403 -660 672 C ATOM 2847 C SER A 433 173.220 30.455 534.932 1.00 40.13 C ANISOU 2847 C SER A 433 4007 5969 5270 -405 -572 653 C ATOM 2848 O SER A 433 173.058 31.041 536.010 1.00 42.86 O ANISOU 2848 O SER A 433 4395 6342 5547 -385 -561 592 O ATOM 2849 CB SER A 433 175.019 31.511 533.536 1.00 24.90 C ANISOU 2849 CB SER A 433 2022 3982 3457 -467 -665 615 C ATOM 2850 OG SER A 433 176.359 31.398 533.085 1.00 26.90 O ANISOU 2850 OG SER A 433 2206 4264 3752 -526 -680 563 O ATOM 2851 N THR A 434 172.202 29.949 534.233 1.00 37.54 N ANISOU 2851 N THR A 434 3624 5634 5005 -435 -504 651 N ATOM 2852 CA THR A 434 170.831 30.078 534.714 1.00 34.90 C ANISOU 2852 CA THR A 434 3221 5350 4690 -457 -396 538 C ATOM 2853 C THR A 434 170.581 29.190 535.927 1.00 36.09 C ANISOU 2853 C THR A 434 3504 5487 4719 -541 -214 548 C ATOM 2854 O THR A 434 169.985 29.634 536.916 1.00 34.40 O ANISOU 2854 O THR A 434 3312 5305 4453 -556 -113 462 O ATOM 2855 CB THR A 434 169.850 29.736 533.591 1.00 33.26 C ANISOU 2855 CB THR A 434 2851 5192 4593 -464 -393 443 C ATOM 2856 OG1 THR A 434 170.140 30.542 532.442 1.00 37.11 O ANISOU 2856 OG1 THR A 434 3343 5645 5113 -335 -562 466 O ATOM 2857 CG2 THR A 434 168.420 29.991 534.034 1.00 29.63 C ANISOU 2857 CG2 THR A 434 2212 4850 4194 -474 -296 220 C ATOM 2858 N ILE A 435 171.031 27.932 535.874 1.00 36.90 N ANISOU 2858 N ILE A 435 3762 5511 4747 -581 -146 653 N ATOM 2859 CA ILE A 435 170.783 26.989 536.962 1.00 40.74 C ANISOU 2859 CA ILE A 435 4527 5899 5054 -646 76 690 C ATOM 2860 C ILE A 435 171.827 27.066 538.067 1.00 45.03 C ANISOU 2860 C ILE A 435 5336 6413 5361 -468 -34 790 C ATOM 2861 O ILE A 435 171.669 26.395 539.099 1.00 46.54 O ANISOU 2861 O ILE A 435 5876 6490 5318 -458 139 841 O ATOM 2862 CB ILE A 435 170.716 25.542 536.434 1.00 40.46 C ANISOU 2862 CB ILE A 435 4643 5728 5004 -746 231 749 C ATOM 2863 CG1 ILE A 435 172.036 25.154 535.765 1.00 42.42 C ANISOU 2863 CG1 ILE A 435 4943 5947 5230 -576 7 884 C ATOM 2864 CG2 ILE A 435 169.558 25.385 535.461 1.00 41.73 C ANISOU 2864 CG2 ILE A 435 4514 5958 5384 -940 348 568 C ATOM 2865 CD1 ILE A 435 172.042 23.753 535.194 1.00 44.30 C ANISOU 2865 CD1 ILE A 435 5359 6025 5448 -641 144 941 C ATOM 2866 N ASN A 436 172.882 27.862 537.890 1.00 42.23 N ANISOU 2866 N ASN A 436 4850 6156 5040 -329 -301 783 N ATOM 2867 CA ASN A 436 173.921 27.956 538.914 1.00 42.85 C ANISOU 2867 CA ASN A 436 5098 6278 4904 -131 -464 786 C ATOM 2868 C ASN A 436 173.404 28.497 540.243 1.00 41.83 C ANISOU 2868 C ASN A 436 5130 6160 4602 -119 -380 731 C ATOM 2869 O ASN A 436 173.699 27.885 541.284 1.00 36.36 O ANISOU 2869 O ASN A 436 4797 5412 3608 39 -372 785 O ATOM 2870 CB ASN A 436 175.091 28.793 538.383 1.00 48.28 C ANISOU 2870 CB ASN A 436 5519 7101 5724 -71 -712 688 C ATOM 2871 CG ASN A 436 176.406 28.043 538.420 1.00 56.37 C ANISOU 2871 CG ASN A 436 6587 8190 6640 143 -905 676 C ATOM 2872 OD1 ASN A 436 176.591 27.130 539.224 1.00 61.33 O ANISOU 2872 OD1 ASN A 436 7527 8768 7006 353 -935 744 O ATOM 2873 ND2 ASN A 436 177.332 28.427 537.547 1.00 55.12 N ANISOU 2873 ND2 ASN A 436 6145 8134 6663 113 -1023 568 N ATOM 2874 N PRO A 437 172.654 29.606 540.301 1.00 43.54 N ANISOU 2874 N PRO A 437 5156 6431 4955 -236 -319 620 N ATOM 2875 CA PRO A 437 172.187 30.085 541.614 1.00 42.94 C ANISOU 2875 CA PRO A 437 5249 6368 4699 -219 -220 550 C ATOM 2876 C PRO A 437 171.299 29.093 542.346 1.00 45.26 C ANISOU 2876 C PRO A 437 5871 6533 4794 -303 107 607 C ATOM 2877 O PRO A 437 171.319 29.058 543.582 1.00 46.78 O ANISOU 2877 O PRO A 437 6390 6688 4694 -221 181 609 O ATOM 2878 CB PRO A 437 171.425 31.373 541.269 1.00 43.82 C ANISOU 2878 CB PRO A 437 5074 6538 5039 -314 -195 409 C ATOM 2879 CG PRO A 437 171.981 31.807 539.961 1.00 42.11 C ANISOU 2879 CG PRO A 437 4625 6332 5043 -316 -370 419 C ATOM 2880 CD PRO A 437 172.264 30.535 539.224 1.00 41.23 C ANISOU 2880 CD PRO A 437 4549 6177 4941 -329 -357 547 C ATOM 2881 N ALA A 438 170.525 28.278 541.626 1.00 42.67 N ANISOU 2881 N ALA A 438 5496 6120 4595 -485 334 627 N ATOM 2882 CA ALA A 438 169.648 27.322 542.290 1.00 37.78 C ANISOU 2882 CA ALA A 438 5208 5340 3807 -659 746 631 C ATOM 2883 C ALA A 438 170.416 26.180 542.942 1.00 54.61 C ANISOU 2883 C ALA A 438 7928 7257 5564 -497 781 831 C ATOM 2884 O ALA A 438 169.852 25.477 543.787 1.00 57.37 O ANISOU 2884 O ALA A 438 8742 7402 5654 -606 1154 864 O ATOM 2885 CB ALA A 438 168.630 26.760 541.297 1.00 38.93 C ANISOU 2885 CB ALA A 438 5095 5475 4221 -934 987 518 C ATOM 2886 N CYS A 439 171.682 25.978 542.573 1.00 46.74 N ANISOU 2886 N CYS A 439 6954 6290 4514 -222 420 941 N ATOM 2887 CA CYS A 439 172.451 24.874 543.130 1.00 48.95 C ANISOU 2887 CA CYS A 439 7807 6377 4417 43 385 1107 C ATOM 2888 C CYS A 439 172.975 25.161 544.531 1.00 55.53 C ANISOU 2888 C CYS A 439 9036 7225 4837 345 245 1119 C ATOM 2889 O CYS A 439 173.240 24.216 545.280 1.00 60.88 O ANISOU 2889 O CYS A 439 10373 7673 5087 574 324 1259 O ATOM 2890 CB CYS A 439 173.621 24.525 542.208 1.00 52.46 C ANISOU 2890 CB CYS A 439 8072 6895 4965 271 33 1153 C ATOM 2891 SG CYS A 439 173.122 23.913 540.583 1.00 54.63 S ANISOU 2891 SG CYS A 439 8038 7105 5616 -20 191 1165 S ATOM 2892 N TYR A 440 173.135 26.427 544.901 1.00 56.97 N ANISOU 2892 N TYR A 440 8892 7650 5104 376 38 967 N ATOM 2893 CA TYR A 440 173.638 26.745 546.234 1.00 61.63 C ANISOU 2893 CA TYR A 440 9833 8292 5293 670 -127 930 C ATOM 2894 C TYR A 440 172.766 27.737 546.988 1.00 64.71 C ANISOU 2894 C TYR A 440 10158 8740 5688 473 75 805 C ATOM 2895 O TYR A 440 172.637 27.623 548.210 1.00 75.20 O ANISOU 2895 O TYR A 440 11991 9980 6600 605 184 824 O ATOM 2896 CB TYR A 440 175.082 27.274 546.144 1.00 61.48 C ANISOU 2896 CB TYR A 440 9516 8551 5294 1001 -673 789 C ATOM 2897 CG TYR A 440 175.286 28.443 545.203 1.00 58.25 C ANISOU 2897 CG TYR A 440 8401 8366 5364 783 -823 614 C ATOM 2898 CD1 TYR A 440 175.674 28.239 543.885 1.00 59.30 C ANISOU 2898 CD1 TYR A 440 8180 8532 5820 695 -898 630 C ATOM 2899 CD2 TYR A 440 175.113 29.750 545.640 1.00 59.31 C ANISOU 2899 CD2 TYR A 440 8298 8642 5595 674 -864 434 C ATOM 2900 CE1 TYR A 440 175.871 29.305 543.025 1.00 59.54 C ANISOU 2900 CE1 TYR A 440 7695 8703 6224 499 -983 489 C ATOM 2901 CE2 TYR A 440 175.307 30.821 544.787 1.00 55.30 C ANISOU 2901 CE2 TYR A 440 7278 8256 5476 481 -953 289 C ATOM 2902 CZ TYR A 440 175.686 30.593 543.481 1.00 55.91 C ANISOU 2902 CZ TYR A 440 7069 8337 5837 393 -1000 325 C ATOM 2903 OH TYR A 440 175.882 31.656 542.627 1.00 50.69 O ANISOU 2903 OH TYR A 440 6020 7735 5504 202 -1036 199 O ATOM 2904 N ALA A 441 172.163 28.707 546.297 1.00 58.18 N ANISOU 2904 N ALA A 441 8770 8048 5288 199 125 671 N ATOM 2905 CA ALA A 441 171.383 29.725 546.991 1.00 57.23 C ANISOU 2905 CA ALA A 441 8559 7998 5187 66 281 517 C ATOM 2906 C ALA A 441 170.032 29.189 547.449 1.00 64.59 C ANISOU 2906 C ALA A 441 9751 8759 6031 -197 821 520 C ATOM 2907 O ALA A 441 169.598 29.474 548.570 1.00 67.04 O ANISOU 2907 O ALA A 441 10350 9040 6084 -207 1022 453 O ATOM 2908 CB ALA A 441 171.197 30.952 546.097 1.00 50.92 C ANISOU 2908 CB ALA A 441 7153 7361 4832 -66 145 364 C ATOM 2909 N LEU A 442 169.356 28.411 546.606 1.00 68.72 N ANISOU 2909 N LEU A 442 10169 9178 6763 -439 1088 552 N ATOM 2910 CA LEU A 442 168.045 27.875 546.948 1.00 81.26 C ANISOU 2910 CA LEU A 442 11915 10628 8330 -774 1661 461 C ATOM 2911 C LEU A 442 168.115 26.676 547.887 1.00 97.07 C ANISOU 2911 C LEU A 442 14735 12305 9840 -766 2003 633 C ATOM 2912 O LEU A 442 167.097 26.004 548.085 1.00 99.64 O ANISOU 2912 O LEU A 442 15272 12449 10138 -1119 2574 556 O ATOM 2913 CB LEU A 442 167.283 27.496 545.676 1.00 77.39 C ANISOU 2913 CB LEU A 442 10970 10176 8258 -1054 1815 351 C ATOM 2914 CG LEU A 442 166.994 28.643 544.707 1.00 74.96 C ANISOU 2914 CG LEU A 442 9951 10144 8384 -1036 1532 169 C ATOM 2915 CD1 LEU A 442 166.084 28.178 543.581 1.00 74.97 C ANISOU 2915 CD1 LEU A 442 9554 10204 8726 -1281 1703 3 C ATOM 2916 CD2 LEU A 442 166.388 29.832 545.438 1.00 77.22 C ANISOU 2916 CD2 LEU A 442 10064 10578 8699 -1023 1583 -37 C ATOM 2917 N CYS A 443 169.285 26.393 548.464 1.00113.41 N ANISOU 2917 N CYS A 443 17291 14293 11505 -363 1683 829 N ATOM 2918 CA CYS A 443 169.434 25.317 549.434 1.00120.19 C ANISOU 2918 CA CYS A 443 19075 14802 11790 -232 1954 1018 C ATOM 2919 C CYS A 443 170.122 25.787 550.709 1.00118.84 C ANISOU 2919 C CYS A 443 19351 14677 11125 176 1689 1050 C ATOM 2920 O CYS A 443 170.554 24.950 551.511 1.00123.17 O ANISOU 2920 O CYS A 443 20529 14965 11306 454 1665 1173 O ATOM 2921 CB CYS A 443 170.211 24.145 548.823 1.00126.76 C ANISOU 2921 CB CYS A 443 20224 15427 12511 -22 1804 1233 C ATOM 2922 SG CYS A 443 169.520 23.526 547.271 1.00129.11 S ANISOU 2922 SG CYS A 443 20020 15679 13359 -468 2061 1176 S ATOM 2923 N ASN A 444 170.232 27.096 550.918 1.00 98.67 N ANISOU 2923 N ASN A 444 16301 12444 8746 225 1404 862 N ATOM 2924 CA ASN A 444 170.909 27.665 552.074 1.00 85.14 C ANISOU 2924 CA ASN A 444 14905 10837 6607 599 1100 819 C ATOM 2925 C ASN A 444 169.937 28.562 552.827 1.00 80.09 C ANISOU 2925 C ASN A 444 14191 10262 5979 346 1431 634 C ATOM 2926 O ASN A 444 169.328 29.457 552.234 1.00 76.95 O ANISOU 2926 O ASN A 444 13104 10055 6079 72 1475 448 O ATOM 2927 CB ASN A 444 172.149 28.454 551.645 1.00 79.20 C ANISOU 2927 CB ASN A 444 13613 10425 6053 906 411 699 C ATOM 2928 CG ASN A 444 172.934 28.991 552.821 1.00 79.46 C ANISOU 2928 CG ASN A 444 13927 10615 5648 1310 45 580 C ATOM 2929 OD1 ASN A 444 172.709 30.114 553.271 1.00 77.39 O ANISOU 2929 OD1 ASN A 444 13399 10529 5477 1214 11 377 O ATOM 2930 ND2 ASN A 444 173.866 28.191 553.326 1.00 86.06 N ANISOU 2930 ND2 ASN A 444 15224 11383 6093 1765 -251 662 N ATOM 2931 N ALA A 445 169.798 28.318 554.133 1.00 77.74 N ANISOU 2931 N ALA A 445 14638 9791 5107 477 1656 679 N ATOM 2932 CA ALA A 445 168.811 29.046 554.925 1.00 75.05 C ANISOU 2932 CA ALA A 445 14300 9481 4737 220 2056 494 C ATOM 2933 C ALA A 445 169.135 30.534 554.998 1.00 72.05 C ANISOU 2933 C ALA A 445 13323 9459 4595 328 1631 256 C ATOM 2934 O ALA A 445 168.228 31.374 555.015 1.00 70.93 O ANISOU 2934 O ALA A 445 12778 9423 4749 49 1885 46 O ATOM 2935 CB ALA A 445 168.722 28.449 556.329 1.00 79.04 C ANISOU 2935 CB ALA A 445 15474 9699 4858 356 2226 568 C ATOM 2936 N THR A 446 170.423 30.880 555.049 1.00 72.69 N ANISOU 2936 N THR A 446 13329 9726 4564 733 994 241 N ATOM 2937 CA THR A 446 170.799 32.288 555.133 1.00 70.88 C ANISOU 2937 CA THR A 446 12570 9794 4566 789 626 -21 C ATOM 2938 C THR A 446 170.532 33.010 553.816 1.00 58.66 C ANISOU 2938 C THR A 446 10195 8376 3718 514 564 -119 C ATOM 2939 O THR A 446 170.109 34.172 553.815 1.00 57.51 O ANISOU 2939 O THR A 446 9666 8347 3840 379 584 -327 O ATOM 2940 CB THR A 446 172.268 32.421 555.533 1.00 65.03 C ANISOU 2940 CB THR A 446 11928 9247 3534 1253 -10 -98 C ATOM 2941 OG1 THR A 446 172.544 31.544 556.632 1.00 76.31 O ANISOU 2941 OG1 THR A 446 14196 10519 4280 1603 -1 36 O ATOM 2942 CG2 THR A 446 172.573 33.850 555.956 1.00 64.81 C ANISOU 2942 CG2 THR A 446 11525 9476 3624 1267 -281 -420 C ATOM 2943 N PHE A 447 170.776 32.340 552.686 1.00 56.06 N ANISOU 2943 N PHE A 447 9640 8003 3656 463 489 27 N ATOM 2944 CA PHE A 447 170.452 32.935 551.392 1.00 59.64 C ANISOU 2944 CA PHE A 447 9413 8541 4707 231 458 -43 C ATOM 2945 C PHE A 447 168.949 33.121 551.232 1.00 59.49 C ANISOU 2945 C PHE A 447 9212 8466 4926 -88 941 -131 C ATOM 2946 O PHE A 447 168.496 34.141 550.697 1.00 60.34 O ANISOU 2946 O PHE A 447 8838 8680 5407 -183 903 -298 O ATOM 2947 CB PHE A 447 171.004 32.073 550.256 1.00 51.62 C ANISOU 2947 CB PHE A 447 8259 7484 3870 252 305 127 C ATOM 2948 CG PHE A 447 172.379 32.472 549.800 1.00 51.38 C ANISOU 2948 CG PHE A 447 7955 7625 3942 460 -210 64 C ATOM 2949 CD1 PHE A 447 172.593 33.699 549.194 1.00 49.01 C ANISOU 2949 CD1 PHE A 447 7150 7456 4016 353 -384 -114 C ATOM 2950 CD2 PHE A 447 173.452 31.612 549.958 1.00 52.83 C ANISOU 2950 CD2 PHE A 447 8402 7826 3844 764 -492 150 C ATOM 2951 CE1 PHE A 447 173.855 34.067 548.767 1.00 47.61 C ANISOU 2951 CE1 PHE A 447 6710 7428 3953 459 -768 -231 C ATOM 2952 CE2 PHE A 447 174.717 31.973 549.532 1.00 50.61 C ANISOU 2952 CE2 PHE A 447 7780 7754 3693 928 -937 3 C ATOM 2953 CZ PHE A 447 174.918 33.202 548.935 1.00 48.33 C ANISOU 2953 CZ PHE A 447 6961 7599 3804 731 -1043 -199 C ATOM 2954 N LYS A 448 168.159 32.144 551.684 1.00 60.01 N ANISOU 2954 N LYS A 448 9672 8358 4772 -248 1413 -56 N ATOM 2955 CA LYS A 448 166.707 32.246 551.568 1.00 64.62 C ANISOU 2955 CA LYS A 448 10012 8940 5599 -580 1910 -237 C ATOM 2956 C LYS A 448 166.172 33.427 552.370 1.00 65.11 C ANISOU 2956 C LYS A 448 9962 9125 5651 -576 1997 -483 C ATOM 2957 O LYS A 448 165.367 34.220 551.868 1.00 66.92 O ANISOU 2957 O LYS A 448 9665 9492 6272 -678 2058 -710 O ATOM 2958 CB LYS A 448 166.050 30.945 552.029 1.00 73.88 C ANISOU 2958 CB LYS A 448 11703 9871 6498 -816 2483 -156 C ATOM 2959 CG LYS A 448 166.366 29.735 551.166 1.00 77.15 C ANISOU 2959 CG LYS A 448 12225 10125 6965 -871 2487 50 C ATOM 2960 CD LYS A 448 165.870 28.459 551.829 1.00 83.72 C ANISOU 2960 CD LYS A 448 13774 10623 7413 -1089 3090 148 C ATOM 2961 CE LYS A 448 166.219 27.231 551.007 1.00 85.74 C ANISOU 2961 CE LYS A 448 14211 10670 7694 -1128 3105 351 C ATOM 2962 NZ LYS A 448 165.566 27.259 549.671 1.00 85.82 N ANISOU 2962 NZ LYS A 448 13464 10844 8300 -1413 3138 173 N ATOM 2963 N LYS A 449 166.611 33.556 553.626 1.00 63.65 N ANISOU 2963 N LYS A 449 10296 8893 4994 -412 1983 -460 N ATOM 2964 CA LYS A 449 166.143 34.654 554.467 1.00 61.37 C ANISOU 2964 CA LYS A 449 9955 8707 4655 -403 2078 -703 C ATOM 2965 C LYS A 449 166.582 36.004 553.912 1.00 60.17 C ANISOU 2965 C LYS A 449 9280 8725 4857 -262 1622 -845 C ATOM 2966 O LYS A 449 165.836 36.987 553.987 1.00 61.58 O ANISOU 2966 O LYS A 449 9159 8986 5253 -313 1737 -1085 O ATOM 2967 CB LYS A 449 166.650 34.473 555.899 1.00 65.27 C ANISOU 2967 CB LYS A 449 11171 9116 4513 -213 2098 -643 C ATOM 2968 CG LYS A 449 166.267 35.605 556.842 1.00 75.32 C ANISOU 2968 CG LYS A 449 12441 10491 5684 -185 2178 -902 C ATOM 2969 CD LYS A 449 166.898 35.431 558.215 1.00 83.02 C ANISOU 2969 CD LYS A 449 14159 11405 5981 64 2110 -848 C ATOM 2970 CE LYS A 449 166.551 36.595 559.132 1.00 87.54 C ANISOU 2970 CE LYS A 449 14720 12087 6456 90 2174 -1129 C ATOM 2971 NZ LYS A 449 167.001 37.902 558.574 1.00 85.77 N ANISOU 2971 NZ LYS A 449 13880 12049 6661 172 1714 -1321 N ATOM 2972 N THR A 450 167.790 36.070 553.348 1.00 57.75 N ANISOU 2972 N THR A 450 8882 8455 4605 -89 1135 -725 N ATOM 2973 CA THR A 450 168.257 37.322 552.761 1.00 55.92 C ANISOU 2973 CA THR A 450 8227 8318 4700 -22 782 -865 C ATOM 2974 C THR A 450 167.493 37.646 551.483 1.00 53.42 C ANISOU 2974 C THR A 450 7419 8000 4878 -142 853 -904 C ATOM 2975 O THR A 450 167.210 38.817 551.204 1.00 50.25 O ANISOU 2975 O THR A 450 6758 7616 4719 -106 778 -1077 O ATOM 2976 CB THR A 450 169.758 37.251 552.486 1.00 54.71 C ANISOU 2976 CB THR A 450 8081 8219 4487 138 311 -790 C ATOM 2977 OG1 THR A 450 170.428 36.702 553.628 1.00 58.87 O ANISOU 2977 OG1 THR A 450 9092 8775 4499 336 202 -760 O ATOM 2978 CG2 THR A 450 170.308 38.641 552.216 1.00 51.07 C ANISOU 2978 CG2 THR A 450 7318 7817 4270 147 41 -1001 C ATOM 2979 N PHE A 451 167.158 36.623 550.693 1.00 52.27 N ANISOU 2979 N PHE A 451 7182 7819 4859 -251 983 -759 N ATOM 2980 CA PHE A 451 166.303 36.835 549.529 1.00 49.96 C ANISOU 2980 CA PHE A 451 6436 7563 4984 -326 1047 -842 C ATOM 2981 C PHE A 451 164.956 37.410 549.948 1.00 53.98 C ANISOU 2981 C PHE A 451 6762 8150 5598 -376 1365 -1127 C ATOM 2982 O PHE A 451 164.477 38.391 549.368 1.00 50.61 O ANISOU 2982 O PHE A 451 6006 7775 5450 -259 1252 -1299 O ATOM 2983 CB PHE A 451 166.108 35.523 548.765 1.00 48.58 C ANISOU 2983 CB PHE A 451 6221 7352 4884 -465 1178 -691 C ATOM 2984 CG PHE A 451 167.323 35.068 548.003 1.00 48.51 C ANISOU 2984 CG PHE A 451 6253 7293 4886 -383 838 -456 C ATOM 2985 CD1 PHE A 451 168.431 35.889 547.870 1.00 48.97 C ANISOU 2985 CD1 PHE A 451 6280 7368 4960 -235 463 -440 C ATOM 2986 CD2 PHE A 451 167.350 33.816 547.409 1.00 56.91 C ANISOU 2986 CD2 PHE A 451 7372 8293 5958 -480 930 -296 C ATOM 2987 CE1 PHE A 451 169.545 35.465 547.165 1.00 53.63 C ANISOU 2987 CE1 PHE A 451 6850 7945 5583 -182 190 -288 C ATOM 2988 CE2 PHE A 451 168.460 33.389 546.703 1.00 59.08 C ANISOU 2988 CE2 PHE A 451 7663 8535 6248 -386 629 -110 C ATOM 2989 CZ PHE A 451 169.559 34.214 546.581 1.00 56.74 C ANISOU 2989 CZ PHE A 451 7292 8291 5977 -234 260 -116 C ATOM 2990 N LYS A 452 164.333 36.806 550.964 1.00 61.83 N ANISOU 2990 N LYS A 452 8005 9140 6348 -529 1782 -1199 N ATOM 2991 CA LYS A 452 163.051 37.296 551.462 1.00 66.65 C ANISOU 2991 CA LYS A 452 8415 9856 7051 -605 2144 -1532 C ATOM 2992 C LYS A 452 163.146 38.752 551.903 1.00 67.15 C ANISOU 2992 C LYS A 452 8429 9952 7131 -388 1945 -1697 C ATOM 2993 O LYS A 452 162.237 39.549 551.642 1.00 68.30 O ANISOU 2993 O LYS A 452 8210 10203 7539 -297 1999 -1979 O ATOM 2994 CB LYS A 452 162.574 36.416 552.617 1.00 75.15 C ANISOU 2994 CB LYS A 452 9904 10869 7780 -844 2678 -1562 C ATOM 2995 CG LYS A 452 161.373 36.962 553.369 1.00 85.99 C ANISOU 2995 CG LYS A 452 11123 12359 9188 -945 3105 -1943 C ATOM 2996 CD LYS A 452 161.367 36.474 554.809 1.00 94.92 C ANISOU 2996 CD LYS A 452 12896 13358 9812 -1092 3535 -1905 C ATOM 2997 CE LYS A 452 162.612 36.944 555.548 1.00 95.03 C ANISOU 2997 CE LYS A 452 13395 13279 9433 -817 3133 -1682 C ATOM 2998 NZ LYS A 452 162.631 36.492 556.967 1.00 98.91 N ANISOU 2998 NZ LYS A 452 14596 13636 9349 -879 3502 -1640 N ATOM 2999 N HIS A 453 164.243 39.117 552.570 1.00 66.91 N ANISOU 2999 N HIS A 453 8763 9840 6821 -280 1700 -1563 N ATOM 3000 CA HIS A 453 164.419 40.499 553.005 1.00 66.18 C ANISOU 3000 CA HIS A 453 8664 9744 6736 -115 1526 -1740 C ATOM 3001 C HIS A 453 164.602 41.435 551.816 1.00 58.01 C ANISOU 3001 C HIS A 453 7310 8662 6069 34 1200 -1765 C ATOM 3002 O HIS A 453 164.094 42.562 551.823 1.00 57.51 O ANISOU 3002 O HIS A 453 7123 8580 6150 179 1189 -1985 O ATOM 3003 CB HIS A 453 165.609 40.595 553.960 1.00 68.43 C ANISOU 3003 CB HIS A 453 9378 9987 6635 -54 1319 -1651 C ATOM 3004 CG HIS A 453 165.828 41.965 554.522 1.00 71.63 C ANISOU 3004 CG HIS A 453 9816 10378 7021 62 1179 -1874 C ATOM 3005 ND1 HIS A 453 167.059 42.396 554.968 1.00 73.24 N ANISOU 3005 ND1 HIS A 453 10220 10572 7034 130 853 -1885 N ATOM 3006 CD2 HIS A 453 164.975 42.998 554.717 1.00 75.39 C ANISOU 3006 CD2 HIS A 453 10146 10850 7648 127 1325 -2135 C ATOM 3007 CE1 HIS A 453 166.955 43.637 555.409 1.00 76.11 C ANISOU 3007 CE1 HIS A 453 10584 10900 7434 186 830 -2134 C ATOM 3008 NE2 HIS A 453 165.701 44.026 555.267 1.00 75.85 N ANISOU 3008 NE2 HIS A 453 10371 10851 7598 207 1111 -2267 N ATOM 3009 N LEU A 454 165.324 40.988 550.786 1.00 57.08 N ANISOU 3009 N LEU A 454 7115 8495 6077 20 954 -1543 N ATOM 3010 CA LEU A 454 165.534 41.833 549.614 1.00 58.84 C ANISOU 3010 CA LEU A 454 7145 8620 6590 150 692 -1539 C ATOM 3011 C LEU A 454 164.250 42.030 548.819 1.00 58.94 C ANISOU 3011 C LEU A 454 6824 8695 6877 282 786 -1696 C ATOM 3012 O LEU A 454 164.088 43.058 548.152 1.00 58.67 O ANISOU 3012 O LEU A 454 6729 8553 7010 498 622 -1780 O ATOM 3013 CB LEU A 454 166.620 41.237 548.717 1.00 56.34 C ANISOU 3013 CB LEU A 454 6838 8248 6319 83 453 -1284 C ATOM 3014 CG LEU A 454 168.056 41.256 549.245 1.00 56.49 C ANISOU 3014 CG LEU A 454 7083 8244 6136 25 248 -1215 C ATOM 3015 CD1 LEU A 454 168.998 40.611 548.241 1.00 50.96 C ANISOU 3015 CD1 LEU A 454 6308 7524 5530 -30 48 -1016 C ATOM 3016 CD2 LEU A 454 168.497 42.675 549.563 1.00 58.88 C ANISOU 3016 CD2 LEU A 454 7470 8438 6462 64 139 -1410 C ATOM 3017 N LEU A 455 163.330 41.067 548.875 1.00 59.11 N ANISOU 3017 N LEU A 455 6647 8881 6931 169 1053 -1771 N ATOM 3018 CA LEU A 455 162.116 41.111 548.073 1.00 61.38 C ANISOU 3018 CA LEU A 455 6516 9311 7495 297 1108 -2003 C ATOM 3019 C LEU A 455 160.913 41.674 548.820 1.00 71.60 C ANISOU 3019 C LEU A 455 7615 10757 8832 389 1368 -2397 C ATOM 3020 O LEU A 455 159.910 42.003 548.178 1.00 74.66 O ANISOU 3020 O LEU A 455 7612 11296 9458 609 1332 -2682 O ATOM 3021 CB LEU A 455 161.778 39.710 547.549 1.00 56.14 C ANISOU 3021 CB LEU A 455 5659 8768 6905 74 1269 -1949 C ATOM 3022 CG LEU A 455 162.823 39.065 546.634 1.00 53.88 C ANISOU 3022 CG LEU A 455 5493 8361 6617 16 1018 -1600 C ATOM 3023 CD1 LEU A 455 162.384 37.672 546.207 1.00 55.64 C ANISOU 3023 CD1 LEU A 455 5552 8682 6906 -218 1227 -1589 C ATOM 3024 CD2 LEU A 455 163.087 39.944 545.422 1.00 54.39 C ANISOU 3024 CD2 LEU A 455 5473 8336 6858 296 646 -1554 C ATOM 3025 N MET A 456 160.983 41.799 550.143 1.00 78.13 N ANISOU 3025 N MET A 456 8696 11569 9422 263 1611 -2455 N ATOM 3026 CA MET A 456 159.863 42.338 550.900 1.00 87.79 C ANISOU 3026 CA MET A 456 9737 12940 10679 334 1900 -2855 C ATOM 3027 C MET A 456 159.851 43.861 550.827 1.00 92.69 C ANISOU 3027 C MET A 456 10389 13455 11374 709 1640 -2996 C ATOM 3028 O MET A 456 160.898 44.512 550.758 1.00 87.67 O ANISOU 3028 O MET A 456 10086 12583 10642 783 1364 -2775 O ATOM 3029 CB MET A 456 159.917 41.881 552.360 1.00 90.62 C ANISOU 3029 CB MET A 456 10433 13296 10703 58 2299 -2865 C ATOM 3030 CG MET A 456 161.147 42.338 553.133 1.00 92.38 C ANISOU 3030 CG MET A 456 11172 13325 10605 85 2099 -2628 C ATOM 3031 SD MET A 456 161.042 41.999 554.904 1.00 96.58 S ANISOU 3031 SD MET A 456 12158 13864 10674 -117 2541 -2707 S ATOM 3032 CE MET A 456 159.672 43.054 555.372 1.00 95.87 C ANISOU 3032 CE MET A 456 11740 13925 10763 20 2828 -3219 C ATOM 3033 N CYS A 457 158.646 44.425 550.833 1.00104.24 N ANISOU 3033 N CYS A 457 11499 15092 13017 945 1751 -3409 N ATOM 3034 CA CYS A 457 158.479 45.869 550.744 1.00109.88 C ANISOU 3034 CA CYS A 457 12278 15678 13793 1369 1528 -3579 C ATOM 3035 C CYS A 457 158.755 46.515 552.096 1.00108.34 C ANISOU 3035 C CYS A 457 12426 15377 13363 1293 1709 -3650 C ATOM 3036 O CYS A 457 158.202 46.098 553.119 1.00109.83 O ANISOU 3036 O CYS A 457 12552 15742 13436 1084 2105 -3852 O ATOM 3037 CB CYS A 457 157.067 46.214 550.270 1.00118.96 C ANISOU 3037 CB CYS A 457 12903 17090 15206 1736 1538 -4049 C ATOM 3038 SG CYS A 457 156.614 45.500 548.671 1.00120.22 S ANISOU 3038 SG CYS A 457 12611 17439 15627 1892 1279 -4071 S ATOM 3039 N HIS A 458 159.611 47.532 552.099 1.00100.24 N ANISOU 3039 N HIS A 458 11786 14050 12251 1436 1453 -3510 N ATOM 3040 CA HIS A 458 159.924 48.269 553.318 1.00 98.10 C ANISOU 3040 CA HIS A 458 11846 13668 11760 1391 1572 -3617 C ATOM 3041 C HIS A 458 159.029 49.496 553.459 1.00100.26 C ANISOU 3041 C HIS A 458 12047 13902 12146 1796 1593 -3993 C ATOM 3042 O HIS A 458 158.841 50.253 552.507 1.00 98.84 O ANISOU 3042 O HIS A 458 11860 13558 12136 2175 1334 -4026 O ATOM 3043 CB HIS A 458 161.396 48.688 553.334 1.00 92.86 C ANISOU 3043 CB HIS A 458 11620 12713 10948 1262 1320 -3341 C ATOM 3044 CG HIS A 458 162.330 47.605 553.776 1.00 85.63 C ANISOU 3044 CG HIS A 458 10850 11877 9808 902 1336 -3077 C ATOM 3045 ND1 HIS A 458 162.400 46.379 553.150 1.00 80.07 N ANISOU 3045 ND1 HIS A 458 9973 11295 9154 750 1333 -2851 N ATOM 3046 CD2 HIS A 458 163.234 47.564 554.784 1.00 84.40 C ANISOU 3046 CD2 HIS A 458 11018 11698 9352 718 1326 -3031 C ATOM 3047 CE1 HIS A 458 163.306 45.630 553.753 1.00 79.86 C ANISOU 3047 CE1 HIS A 458 10190 11291 8860 517 1325 -2656 C ATOM 3048 NE2 HIS A 458 163.826 46.326 554.748 1.00 82.11 N ANISOU 3048 NE2 HIS A 458 10767 11511 8921 513 1298 -2770 N TER 3049 HIS A 458 HETATM 3050 C10 3C0 A 501 186.162 24.462 525.611 1.00 34.81 C HETATM 3051 C13 3C0 A 501 181.993 26.873 524.822 1.00 32.90 C HETATM 3052 C15 3C0 A 501 181.445 29.302 524.157 1.00 26.84 C HETATM 3053 C17 3C0 A 501 182.944 29.399 526.035 1.00 30.50 C HETATM 3054 C20 3C0 A 501 180.373 30.961 525.640 1.00 25.67 C HETATM 3055 C21 3C0 A 501 179.294 28.953 525.264 1.00 30.78 C HETATM 3056 C22 3C0 A 501 181.520 28.881 526.359 1.00 29.05 C HETATM 3057 N19 3C0 A 501 180.643 29.535 525.367 1.00 29.82 N HETATM 3058 C14 3C0 A 501 181.408 27.811 523.747 1.00 27.34 C HETATM 3059 C16 3C0 A 501 182.891 29.701 524.561 1.00 31.61 C HETATM 3060 O18 3C0 A 501 183.150 30.759 525.543 1.00 32.58 O HETATM 3061 C23 3C0 A 501 181.517 27.346 526.215 1.00 31.45 C HETATM 3062 O12 3C0 A 501 183.435 26.779 524.685 1.00 34.63 O HETATM 3063 C02 3C0 A 501 184.031 25.774 525.378 1.00 30.65 C HETATM 3064 O01 3C0 A 501 183.435 24.859 525.945 1.00 25.23 O HETATM 3065 C03 3C0 A 501 185.563 25.850 525.373 1.00 32.89 C HETATM 3066 O11 3C0 A 501 185.766 23.592 524.544 1.00 30.62 O HETATM 3067 C04 3C0 A 501 185.997 26.749 526.346 1.00 31.01 C HETATM 3068 C05 3C0 A 501 186.502 27.984 525.959 1.00 26.21 C HETATM 3069 C06 3C0 A 501 186.935 28.891 526.918 1.00 32.40 C HETATM 3070 C07 3C0 A 501 186.862 28.564 528.267 1.00 31.71 C HETATM 3071 C08 3C0 A 501 186.356 27.328 528.656 1.00 34.96 C HETATM 3072 C09 3C0 A 501 185.922 26.421 527.695 1.00 31.48 C HETATM 3073 O HOH A 601 180.687 33.360 521.870 1.00 36.60 O HETATM 3074 O HOH A 602 177.671 42.983 511.035 1.00 34.50 O HETATM 3075 O HOH A 603 175.803 31.743 540.000 1.00 30.36 O HETATM 3076 O HOH A 604 179.389 27.343 536.417 1.00 32.79 O HETATM 3077 O HOH A 605 195.531 35.567 524.318 1.00 32.99 O HETATM 3078 O HOH A 606 185.271 26.863 521.227 1.00 32.21 O HETATM 3079 O HOH A 607 185.922 25.766 548.736 1.00 60.48 O HETATM 3080 O HOH A 608 180.191 21.417 512.231 1.00 47.62 O HETATM 3081 O HOH A 609 177.601 29.819 531.252 1.00 30.10 O HETATM 3082 O HOH A 610 186.705 20.705 516.318 1.00 38.59 O HETATM 3083 O HOH A 611 182.777 30.307 519.585 1.00 44.50 O HETATM 3084 O HOH A 612 183.919 40.750 509.657 1.00 51.36 O HETATM 3085 O HOH A 613 188.649 36.753 516.459 1.00 50.97 O HETATM 3086 O HOH A 614 177.051 34.558 510.287 1.00 55.10 O HETATM 3087 O HOH A 615 181.535 27.764 518.423 1.00 44.26 O HETATM 3088 O HOH A 616 176.574 22.158 525.570 1.00 20.08 O HETATM 3089 O HOH A 617 194.590 13.080 549.211 1.00 63.78 O HETATM 3090 O HOH A 618 182.253 40.519 511.754 1.00 47.64 O HETATM 3091 O HOH A 619 178.431 25.390 537.702 1.00 29.53 O HETATM 3092 O HOH A 620 186.947 37.367 515.024 1.00 38.06 O HETATM 3093 O HOH A 621 191.986 42.018 506.504 1.00 51.07 O HETATM 3094 O HOH A 622 191.361 38.448 515.570 1.00 28.62 O HETATM 3095 O HOH A 623 189.102 38.349 513.533 1.00 34.41 O HETATM 3096 O HOH A 624 189.359 27.020 531.185 1.00 42.91 O HETATM 3097 O HOH A 625 193.868 32.687 510.961 1.00 59.35 O HETATM 3098 O HOH A 626 183.973 30.689 517.006 1.00 41.24 O HETATM 3099 O HOH A 627 180.330 41.785 510.344 1.00 37.35 O HETATM 3100 O HOH A 628 172.798 21.749 546.961 1.00 56.57 O HETATM 3101 O HOH A 629 186.778 25.039 522.076 1.00 38.31 O HETATM 3102 O HOH A 630 184.083 29.445 554.671 1.00 71.05 O HETATM 3103 O HOH A 631 196.587 14.854 545.153 1.00 59.07 O HETATM 3104 O HOH A 632 191.255 17.715 512.292 1.00 61.37 O HETATM 3105 O HOH A 633 179.164 30.283 528.969 1.00 59.31 O HETATM 3106 O HOH A 634 182.262 29.185 515.580 1.00 46.01 O CONECT 638 1284 CONECT 1284 638 CONECT 2688 2706 CONECT 2706 2688 CONECT 3050 3065 3066 CONECT 3051 3058 3061 3062 CONECT 3052 3057 3058 3059 CONECT 3053 3056 3059 3060 CONECT 3054 3057 CONECT 3055 3057 CONECT 3056 3053 3057 3061 CONECT 3057 3052 3054 3055 3056 CONECT 3058 3051 3052 CONECT 3059 3052 3053 3060 CONECT 3060 3053 3059 CONECT 3061 3051 3056 CONECT 3062 3051 3063 CONECT 3063 3062 3064 3065 CONECT 3064 3063 CONECT 3065 3050 3063 3067 CONECT 3066 3050 CONECT 3067 3065 3068 3072 CONECT 3068 3067 3069 CONECT 3069 3068 3070 CONECT 3070 3069 3071 CONECT 3071 3070 3072 CONECT 3072 3067 3071 MASTER 404 0 1 18 0 0 3 6 3099 1 27 33 END