HEADER MEMBRANE PROTEIN 30-MAR-21 7M8W TITLE XFEL CRYSTAL STRUCTURE OF THE PROSTAGLANDIN D2 RECEPTOR CRTH2 IN TITLE 2 COMPLEX WITH 15R-METHYL-PGD2 COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROSTAGLANDIN D2 RECEPTOR 2, ENDOLYSIN CHIMERA; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ENTEROBACTERIA PHAGE T4; SOURCE 3 ORGANISM_COMMON: HUMAN, BACTERIOPHAGE T4; SOURCE 4 ORGANISM_TAXID: 9606, 10665; SOURCE 5 GENE: PTGDR2, CRTH2, DL1R, GPR44, E, T4TP126; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS KEYWDS PROSTAGLANDIN D2 RECEPTOR, CRTH2, 15R-METHYL-PGD2, G PROTEIN-COUPLED KEYWDS 2 RECEPTOR, GPCR, ENDOLYSIN FUSION, MEMBRANE PROTEIN, LCP EXPDTA X-RAY DIFFRACTION AUTHOR A.SHIRIAEVA,G.W.HAN,V.CHEREZOV REVDAT 1 25-AUG-21 7M8W 0 JRNL AUTH H.LIU,R.N.V.K.DEEPAK,A.SHIRIAEVA,C.GATI,A.BATYUK,H.HU, JRNL AUTH 2 U.WEIERSTALL,W.LIU,L.WANG,V.CHEREZOV,H.FAN,C.ZHANG JRNL TITL MOLECULAR BASIS FOR LIPID RECOGNITION BY THE PROSTAGLANDIN D JRNL TITL 2 2 RECEPTOR CRTH2. JRNL REF PROC.NATL.ACAD.SCI.USA V. 118 2021 JRNL REFN ESSN 1091-6490 JRNL PMID 34341104 JRNL DOI 10.1073/PNAS.2102813118 REMARK 2 REMARK 2 RESOLUTION. 2.61 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.18.2_3874 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.61 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.43 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 53.4 REMARK 3 NUMBER OF REFLECTIONS : 15642 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.231 REMARK 3 R VALUE (WORKING SET) : 0.229 REMARK 3 FREE R VALUE : 0.267 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990 REMARK 3 FREE R VALUE TEST SET COUNT : 781 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 32.4300 - 4.7300 1.00 4866 257 0.2239 0.2489 REMARK 3 2 4.7300 - 3.7600 1.00 4659 245 0.2074 0.2650 REMARK 3 3 3.7600 - 3.2800 0.65 3021 154 0.2611 0.2918 REMARK 3 4 3.2800 - 2.9800 0.28 1274 60 0.2850 0.2846 REMARK 3 5 2.9800 - 2.7700 0.15 656 38 0.3205 0.3855 REMARK 3 6 2.7700 - 2.6100 0.09 385 27 0.3290 0.4058 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.330 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.260 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.37 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 : NULL NULL REMARK 3 ANGLE : NULL NULL REMARK 3 CHIRALITY : NULL NULL REMARK 3 PLANARITY : NULL NULL REMARK 3 DIHEDRAL : NULL NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 4 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 3 THROUGH 32 ) REMARK 3 ORIGIN FOR THE GROUP (A): -7.2200 -57.0611 531.3694 REMARK 3 T TENSOR REMARK 3 T11: 0.7713 T22: 0.7296 REMARK 3 T33: 0.5198 T12: 0.0390 REMARK 3 T13: -0.1143 T23: 0.1412 REMARK 3 L TENSOR REMARK 3 L11: 0.9951 L22: 1.1180 REMARK 3 L33: 0.2731 L12: 0.3968 REMARK 3 L13: -0.2781 L23: 0.3145 REMARK 3 S TENSOR REMARK 3 S11: -0.2988 S12: 0.7457 S13: -0.1656 REMARK 3 S21: -1.3323 S22: 0.5046 S23: 0.5914 REMARK 3 S31: 0.3432 S32: -0.0173 S33: 0.0146 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 33 THROUGH 903 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.8174 -55.2577 560.4710 REMARK 3 T TENSOR REMARK 3 T11: 0.0737 T22: -0.0271 REMARK 3 T33: 0.1838 T12: 0.1420 REMARK 3 T13: 0.0586 T23: 0.0779 REMARK 3 L TENSOR REMARK 3 L11: 2.3665 L22: 1.3469 REMARK 3 L33: 2.8493 L12: -0.0024 REMARK 3 L13: 0.9019 L23: -0.4400 REMARK 3 S TENSOR REMARK 3 S11: -0.1856 S12: 0.0344 S13: 0.1083 REMARK 3 S21: -0.0392 S22: 0.0860 S23: 0.0027 REMARK 3 S31: -0.0401 S32: -0.1793 S33: -0.0752 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 904 THROUGH 244 ) REMARK 3 ORIGIN FOR THE GROUP (A): 9.1162 -48.0840 597.9843 REMARK 3 T TENSOR REMARK 3 T11: 0.4279 T22: 0.4541 REMARK 3 T33: 0.4269 T12: 0.1452 REMARK 3 T13: -0.1231 T23: -0.1301 REMARK 3 L TENSOR REMARK 3 L11: 2.6415 L22: 1.9935 REMARK 3 L33: 2.3411 L12: -0.3103 REMARK 3 L13: -0.6475 L23: 1.0924 REMARK 3 S TENSOR REMARK 3 S11: -0.2472 S12: -0.2398 S13: -0.0241 REMARK 3 S21: 0.3697 S22: 0.5209 S23: -0.5516 REMARK 3 S31: 0.5073 S32: 0.7806 S33: 0.0085 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 245 THROUGH 330 ) REMARK 3 ORIGIN FOR THE GROUP (A): -10.9660 -61.6620 561.9317 REMARK 3 T TENSOR REMARK 3 T11: 0.2414 T22: 0.0610 REMARK 3 T33: 0.2866 T12: -0.0969 REMARK 3 T13: -0.0776 T23: 0.1386 REMARK 3 L TENSOR REMARK 3 L11: 1.9999 L22: 1.8119 REMARK 3 L33: 2.2363 L12: 0.1853 REMARK 3 L13: 1.5916 L23: -0.8199 REMARK 3 S TENSOR REMARK 3 S11: -0.1445 S12: -0.0281 S13: -0.1024 REMARK 3 S21: -0.1082 S22: 0.0961 S23: 0.2693 REMARK 3 S31: 0.6089 S32: -0.4409 S33: -0.0555 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 7M8W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-MAR-21. REMARK 100 THE DEPOSITION ID IS D_1000255887. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 04-NOV-18 REMARK 200 TEMPERATURE (KELVIN) : 293 REMARK 200 PH : 6.0 REMARK 200 NUMBER OF CRYSTALS USED : 20358 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : FREE ELECTRON LASER REMARK 200 BEAMLINE : CXI REMARK 200 X-RAY GENERATOR MODEL : SLAC LCLS BEAMLINE CXI REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.33 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : CS-PAD CXI-1 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTFEL REMARK 200 DATA SCALING SOFTWARE : CRYSTFEL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29269 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600 REMARK 200 RESOLUTION RANGE LOW (A) : 32.430 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9 REMARK 200 DATA REDUNDANCY : 61.80 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 2.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69 REMARK 200 COMPLETENESS FOR SHELL (%) : 90.6 REMARK 200 DATA REDUNDANCY IN SHELL : 4.90 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.200 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: 6D27 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 72.22 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.43 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CHLORIDE, LITHIUM SULPHATE, REMARK 280 SODIUM CITRATE TRIBASIC DIHYDRATE, PEG 300, PROPYLENE GLYCOL REMARK 280 P400, PGD2, PH 6.0, LIPIDIC CUBIC PHASE, TEMPERATURE 283K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 25.70000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 132.70000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.90000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 132.70000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.70000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 33.90000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 300 REMARK: AUTHORS STATE THAT THE BIOLOGICAL UNIT IS UNKNOWN. 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA 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 0 REMARK 465 MET A 1 REMARK 465 SER A 2 REMARK 465 MET A 1049 REMARK 465 LEU A 1050 REMARK 465 ARG A 1051 REMARK 465 ILE A 1052 REMARK 465 ASP A 1053 REMARK 465 GLU A 1054 REMARK 465 GLY A 1055 REMARK 465 GLY A 1056 REMARK 465 GLY A 1057 REMARK 465 SER A 1058 REMARK 465 GLY A 1059 REMARK 465 GLY A 1060 REMARK 465 ASP A 1061 REMARK 465 GLU A 1062 REMARK 465 ALA A 1063 REMARK 465 SER A 331 REMARK 465 GLU A 332 REMARK 465 LEU A 333 REMARK 465 GLY A 334 REMARK 465 GLY A 335 REMARK 465 ALA A 336 REMARK 465 GLY A 337 REMARK 465 SER A 338 REMARK 465 SER A 339 REMARK 465 LEU A 340 REMARK 465 GLU A 341 REMARK 465 VAL A 342 REMARK 465 LEU A 343 REMARK 465 PHE A 344 REMARK 465 GLN A 345 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 SER A 22 OG REMARK 470 TYR A 30 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ASN A1002 CG OD1 ND2 REMARK 470 PHE A1004 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLU A1064 CG CD OE1 OE2 REMARK 470 LYS A1065 CG CD CE NZ REMARK 470 ARG A 317 CG CD NE CZ NH1 NH2 REMARK 470 ASP A 329 CG OD1 OD2 REMARK 470 ASP A 330 CG OD1 OD2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 HIS A 23 -127.22 57.93 REMARK 500 SER A 27 -6.18 66.05 REMARK 500 HIS A 95 64.76 65.40 REMARK 500 LEU A 99 54.55 -116.79 REMARK 500 ASN A 190 66.69 29.47 REMARK 500 PHE A 215 -62.83 -153.27 REMARK 500 PHE A1004 11.12 84.41 REMARK 500 GLN A1069 37.96 -163.41 REMARK 500 ARG A 239 60.12 71.13 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA A2402 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 SER A 76 OG REMARK 620 2 ASP A 77 OD1 86.4 REMARK 620 3 ASN A 114 OD1 57.8 82.8 REMARK 620 4 SER A 118 OG 76.7 133.9 51.8 REMARK 620 N 1 2 3 DBREF 7M8W A 1 236 UNP Q9Y5Y4 PD2R2_HUMAN 1 236 DBREF 7M8W A 1002 1055 UNP D9IEF7 D9IEF7_BPT4 2 12 DBREF 7M8W A 1061 1161 UNP D9IEF7 D9IEF7_BPT4 61 161 DBREF 7M8W A 238 339 UNP Q9Y5Y4 PD2R2_HUMAN 238 339 SEQADV 7M8W GLY A 0 UNP Q9Y5Y4 EXPRESSION TAG SEQADV 7M8W ALA A 25 UNP Q9Y5Y4 ASN 25 ENGINEERED MUTATION SEQADV 7M8W ALA A 204 UNP Q9Y5Y4 VAL 204 VARIANT SEQADV 7M8W ALA A 900 UNP Q9Y5Y4 LINKER SEQADV 7M8W ASP A 901 UNP Q9Y5Y4 LINKER SEQADV 7M8W LEU A 902 UNP Q9Y5Y4 LINKER SEQADV 7M8W GLY A 903 UNP Q9Y5Y4 LINKER SEQADV 7M8W LEU A 904 UNP Q9Y5Y4 LINKER SEQADV 7M8W GLN A 905 UNP Q9Y5Y4 LINKER SEQADV 7M8W HIS A 906 UNP Q9Y5Y4 LINKER SEQADV 7M8W ARG A 907 UNP Q9Y5Y4 LINKER SEQADV 7M8W GLY A 1056 UNP D9IEF7 LINKER SEQADV 7M8W GLY A 1057 UNP D9IEF7 LINKER SEQADV 7M8W SER A 1058 UNP D9IEF7 LINKER SEQADV 7M8W GLY A 1059 UNP D9IEF7 LINKER SEQADV 7M8W GLY A 1060 UNP D9IEF7 LINKER SEQADV 7M8W ALA A 1097 UNP D9IEF7 CYS 97 ENGINEERED MUTATION SEQADV 7M8W LEU A 340 UNP Q9Y5Y4 EXPRESSION TAG SEQADV 7M8W GLU A 341 UNP Q9Y5Y4 EXPRESSION TAG SEQADV 7M8W VAL A 342 UNP Q9Y5Y4 EXPRESSION TAG SEQADV 7M8W LEU A 343 UNP Q9Y5Y4 EXPRESSION TAG SEQADV 7M8W PHE A 344 UNP Q9Y5Y4 EXPRESSION TAG SEQADV 7M8W GLN A 345 UNP Q9Y5Y4 EXPRESSION TAG SEQRES 1 A 470 GLY MET SER ALA ASN ALA THR LEU LYS PRO LEU CYS PRO SEQRES 2 A 470 ILE LEU GLU GLN MET SER ARG LEU GLN SER HIS SER ALA SEQRES 3 A 470 THR SER ILE ARG TYR ILE ASP HIS ALA ALA VAL LEU LEU SEQRES 4 A 470 HIS GLY LEU ALA SER LEU LEU GLY LEU VAL GLU ASN GLY SEQRES 5 A 470 VAL ILE LEU PHE VAL VAL GLY CYS ARG MET ARG GLN THR SEQRES 6 A 470 VAL VAL THR THR TRP VAL LEU HIS LEU ALA LEU SER ASP SEQRES 7 A 470 LEU LEU ALA SER ALA SER LEU PRO PHE PHE THR TYR PHE SEQRES 8 A 470 LEU ALA VAL GLY HIS SER TRP GLU LEU GLY THR THR PHE SEQRES 9 A 470 CYS LYS LEU HIS SER SER ILE PHE PHE LEU ASN MET PHE SEQRES 10 A 470 ALA SER GLY PHE LEU LEU SER ALA ILE SER LEU ASP ARG SEQRES 11 A 470 CYS LEU GLN VAL VAL ARG PRO VAL TRP ALA GLN ASN HIS SEQRES 12 A 470 ARG THR VAL ALA ALA ALA HIS LYS VAL CYS LEU VAL LEU SEQRES 13 A 470 TRP ALA LEU ALA VAL LEU ASN THR VAL PRO TYR PHE VAL SEQRES 14 A 470 PHE ARG ASP THR ILE SER ARG LEU ASP GLY ARG ILE MET SEQRES 15 A 470 CYS TYR TYR ASN VAL LEU LEU LEU ASN PRO GLY PRO ASP SEQRES 16 A 470 ARG ASP ALA THR CYS ASN SER ARG GLN ALA ALA LEU ALA SEQRES 17 A 470 VAL SER LYS PHE LEU LEU ALA PHE LEU VAL PRO LEU ALA SEQRES 18 A 470 ILE ILE ALA SER SER HIS ALA ALA VAL SER LEU ARG LEU SEQRES 19 A 470 GLN HIS ARG ALA ASP LEU GLY LEU GLN HIS ARG ASN ILE SEQRES 20 A 470 PHE GLU MET LEU ARG ILE ASP GLU GLY GLY GLY SER GLY SEQRES 21 A 470 GLY ASP GLU ALA GLU LYS LEU PHE ASN GLN ASP VAL ASP SEQRES 22 A 470 ALA ALA VAL ARG GLY ILE LEU ARG ASN ALA LYS LEU LYS SEQRES 23 A 470 PRO VAL TYR ASP SER LEU ASP ALA VAL ARG ARG ALA ALA SEQRES 24 A 470 LEU ILE ASN MET VAL PHE GLN MET GLY GLU THR GLY VAL SEQRES 25 A 470 ALA GLY PHE THR ASN SER LEU ARG MET LEU GLN GLN LYS SEQRES 26 A 470 ARG TRP ASP GLU ALA ALA VAL ASN LEU ALA LYS SER ARG SEQRES 27 A 470 TRP TYR ASN GLN THR PRO ASN ARG ALA LYS ARG VAL ILE SEQRES 28 A 470 THR THR PHE ARG THR GLY THR TRP ASP ALA TYR ARG ARG SEQRES 29 A 470 ARG PRO GLY ARG PHE VAL ARG LEU VAL ALA ALA VAL VAL SEQRES 30 A 470 ALA ALA PHE ALA LEU CYS TRP GLY PRO TYR HIS VAL PHE SEQRES 31 A 470 SER LEU LEU GLU ALA ARG ALA HIS ALA ASN PRO GLY LEU SEQRES 32 A 470 ARG PRO LEU VAL TRP ARG GLY LEU PRO PHE VAL THR SER SEQRES 33 A 470 LEU ALA PHE PHE ASN SER VAL ALA ASN PRO VAL LEU TYR SEQRES 34 A 470 VAL LEU THR YCM PRO ASP MET LEU ARG LYS LEU ARG ARG SEQRES 35 A 470 SER LEU ARG THR VAL LEU GLU SER VAL LEU VAL ASP ASP SEQRES 36 A 470 SER GLU LEU GLY GLY ALA GLY SER SER LEU GLU VAL LEU SEQRES 37 A 470 PHE GLN MODRES 7M8W YCM A 308 CYS MODIFIED RESIDUE HET YCM A 308 10 HET YSS A2401 26 HET NA A2402 1 HET FLC A2403 13 HET SO4 A2404 5 HET SO4 A2405 5 HET SO4 A2406 5 HET SO4 A2407 5 HET SO4 A2408 5 HETNAM YCM S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE HETNAM YSS 15R-METHYL-PROSTAGLANDIN D2 HETNAM NA SODIUM ION HETNAM FLC CITRATE ANION HETNAM SO4 SULFATE ION HETSYN YCM CYSTEINE-S-ACETAMIDE HETSYN YSS (5Z,13E,15R,16E)-9ALPHA,15-DIHYDROXY-15-METHYL-11-OXO- HETSYN 2 YSS 12ALPHA-PROSTA-5,13,16-TRIEN-1-OIC ACID FORMUL 1 YCM C5 H10 N2 O3 S FORMUL 2 YSS C21 H34 O5 FORMUL 3 NA NA 1+ FORMUL 4 FLC C6 H5 O7 3- FORMUL 5 SO4 5(O4 S 2-) FORMUL 10 HOH *12(H2 O) HELIX 1 AA1 CYS A 11 LEU A 20 1 10 HELIX 2 AA2 ASP A 32 ARG A 60 1 29 HELIX 3 AA3 THR A 64 VAL A 93 1 30 HELIX 4 AA4 THR A 101 ARG A 135 1 35 HELIX 5 AA5 ARG A 135 ARG A 143 1 9 HELIX 6 AA6 THR A 144 THR A 163 1 20 HELIX 7 AA7 THR A 163 PHE A 169 1 7 HELIX 8 AA8 VAL A 186 LEU A 189 5 4 HELIX 9 AA9 ASP A 194 ALA A 214 1 21 HELIX 10 AB1 PHE A 215 LEU A 904 1 27 HELIX 11 AB2 ASP A 1070 ASN A 1081 1 12 HELIX 12 AB3 LEU A 1084 SER A 1090 1 7 HELIX 13 AB4 ASP A 1092 ALA A 1112 1 21 HELIX 14 AB5 PHE A 1114 GLN A 1123 1 10 HELIX 15 AB6 ARG A 1125 LYS A 1135 1 11 HELIX 16 AB7 SER A 1136 THR A 1142 1 7 HELIX 17 AB8 THR A 1142 GLY A 1156 1 15 HELIX 18 AB9 TRP A 1158 ARG A 238 5 5 HELIX 19 AC1 PHE A 244 HIS A 273 1 30 HELIX 20 AC2 ALA A 274 PRO A 276 5 3 HELIX 21 AC3 GLY A 277 THR A 307 1 31 HELIX 22 AC4 YCM A 308 SER A 325 1 18 SHEET 1 AA1 2 ARG A 170 SER A 174 0 SHEET 2 AA1 2 ILE A 180 TYR A 184 -1 O MET A 181 N ILE A 173 SSBOND 1 CYS A 11 CYS A 199 1555 1555 2.03 SSBOND 2 CYS A 104 CYS A 182 1555 1555 2.03 LINK C THR A 307 N YCM A 308 1555 1555 1.33 LINK C YCM A 308 N PRO A 309 1555 1555 1.34 LINK OG SER A 76 NA NA A2402 1555 1555 3.19 LINK OD1 ASP A 77 NA NA A2402 1555 1555 2.35 LINK OD1 ASN A 114 NA NA A2402 1555 1555 3.16 LINK OG SER A 118 NA NA A2402 1555 1555 2.43 CRYST1 51.400 67.800 265.400 90.00 90.00 90.00 P 21 21 21 4 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 0.019455 0.000000 0.000000 0.00000 SCALE2 0.000000 0.014749 0.000000 0.00000 SCALE3 0.000000 0.000000 0.003768 0.00000 ATOM 1 N ALA A 3 -2.664 -44.733 529.589 1.00 61.70 N ANISOU 1 N ALA A 3 8748 9249 5445 411 -284 2389 N ATOM 2 CA ALA A 3 -4.001 -44.173 529.439 1.00 89.84 C ANISOU 2 CA ALA A 3 12217 12740 9179 327 -631 2657 C ATOM 3 C ALA A 3 -4.118 -43.364 528.148 1.00 99.48 C ANISOU 3 C ALA A 3 13695 13987 10114 145 -796 2793 C ATOM 4 O ALA A 3 -4.522 -43.893 527.113 1.00109.96 O ANISOU 4 O ALA A 3 15288 15289 11205 -20 -1016 2787 O ATOM 5 CB ALA A 3 -4.349 -43.309 530.642 1.00 78.03 C ANISOU 5 CB ALA A 3 10341 11232 8075 474 -580 2811 C ATOM 6 N ASN A 4 -3.759 -42.080 528.210 1.00 99.97 N ANISOU 6 N ASN A 4 13683 14103 10197 174 -687 2916 N ATOM 7 CA ASN A 4 -3.877 -41.183 527.059 1.00119.00 C ANISOU 7 CA ASN A 4 16316 16536 12361 11 -837 3073 C ATOM 8 C ASN A 4 -2.649 -41.360 526.168 1.00127.12 C ANISOU 8 C ASN A 4 17679 17655 12966 -64 -612 2876 C ATOM 9 O ASN A 4 -1.678 -40.600 526.217 1.00132.29 O ANISOU 9 O ASN A 4 18342 18384 13538 -14 -341 2830 O ATOM 10 CB ASN A 4 -4.042 -39.739 527.521 1.00118.84 C ANISOU 10 CB ASN A 4 16068 16457 12631 82 -789 3179 C ATOM 11 CG ASN A 4 -2.907 -39.274 528.417 1.00118.97 C ANISOU 11 CG ASN A 4 15910 16558 12736 240 -403 3071 C ATOM 12 OD1 ASN A 4 -2.815 -39.671 529.580 1.00101.74 O ANISOU 12 OD1 ASN A 4 13465 14392 10799 398 -264 3018 O ATOM 13 ND2 ASN A 4 -2.043 -38.418 527.881 1.00119.52 N ANISOU 13 ND2 ASN A 4 16121 16669 12623 200 -226 3020 N ATOM 14 N ALA A 5 -2.711 -42.389 525.321 1.00110.38 N ANISOU 14 N ALA A 5 15840 15522 10579 -194 -725 2748 N ATOM 15 CA ALA A 5 -1.610 -42.725 524.420 1.00 79.86 C ANISOU 15 CA ALA A 5 12309 11732 6302 -283 -525 2538 C ATOM 16 C ALA A 5 -0.302 -42.906 525.189 1.00 91.42 C ANISOU 16 C ALA A 5 13672 13262 7802 -114 -98 2302 C ATOM 17 O ALA A 5 0.755 -42.410 524.789 1.00 92.73 O ANISOU 17 O ALA A 5 13981 13508 7743 -129 150 2208 O ATOM 18 CB ALA A 5 -1.458 -41.663 523.326 1.00 63.45 C ANISOU 18 CB ALA A 5 10435 9672 4002 -402 -569 2635 C ATOM 19 N THR A 6 -0.379 -43.617 526.314 1.00 84.80 N ANISOU 19 N THR A 6 12580 12387 7253 49 -15 2209 N ATOM 20 CA THR A 6 0.783 -43.977 527.116 1.00 72.93 C ANISOU 20 CA THR A 6 10966 10937 5806 218 361 1977 C ATOM 21 C THR A 6 0.885 -45.494 527.195 1.00 65.93 C ANISOU 21 C THR A 6 10157 10009 4885 234 383 1755 C ATOM 22 O THR A 6 -0.134 -46.188 527.256 1.00 80.03 O ANISOU 22 O THR A 6 11907 11710 6792 196 123 1816 O ATOM 23 CB THR A 6 0.704 -43.400 528.538 1.00 80.55 C ANISOU 23 CB THR A 6 11530 11904 7171 420 477 2064 C ATOM 24 OG1 THR A 6 -0.494 -43.863 529.178 1.00 92.01 O ANISOU 24 OG1 THR A 6 12776 13261 8923 456 229 2183 O ATOM 25 CG2 THR A 6 0.711 -41.880 528.512 1.00 81.66 C ANISOU 25 CG2 THR A 6 11581 12085 7360 415 495 2263 C ATOM 26 N LEU A 7 2.115 -46.003 527.173 1.00 62.48 N ANISOU 26 N LEU A 7 9826 9627 4286 289 695 1495 N ATOM 27 CA LEU A 7 2.393 -47.422 527.332 1.00 59.20 C ANISOU 27 CA LEU A 7 9467 9173 3853 328 772 1262 C ATOM 28 C LEU A 7 3.225 -47.629 528.590 1.00 63.88 C ANISOU 28 C LEU A 7 9801 9796 4675 557 1083 1120 C ATOM 29 O LEU A 7 4.046 -46.781 528.955 1.00 74.32 O ANISOU 29 O LEU A 7 11025 11199 6016 649 1324 1106 O ATOM 30 CB LEU A 7 3.136 -47.987 526.111 1.00 55.09 C ANISOU 30 CB LEU A 7 9325 8683 2923 177 863 1053 C ATOM 31 CG LEU A 7 3.486 -49.477 526.132 1.00 55.41 C ANISOU 31 CG LEU A 7 9457 8678 2918 199 952 794 C ATOM 32 CD1 LEU A 7 2.235 -50.338 526.088 1.00 89.58 C ANISOU 32 CD1 LEU A 7 13778 12901 7359 132 628 870 C ATOM 33 CD2 LEU A 7 4.409 -49.828 524.976 1.00 57.60 C ANISOU 33 CD2 LEU A 7 10091 9000 2795 60 1106 576 C ATOM 34 N LYS A 8 2.994 -48.759 529.264 1.00 50.04 N ANISOU 34 N LYS A 8 7935 7977 3100 650 1072 1020 N ATOM 35 CA LYS A 8 3.735 -49.103 530.469 1.00 46.49 C ANISOU 35 CA LYS A 8 7247 7549 2867 867 1344 884 C ATOM 36 C LYS A 8 4.103 -50.582 530.392 1.00 51.05 C ANISOU 36 C LYS A 8 7945 8076 3376 883 1420 644 C ATOM 37 O LYS A 8 3.238 -51.415 530.064 1.00 52.63 O ANISOU 37 O LYS A 8 8231 8187 3581 792 1184 663 O ATOM 38 CB LYS A 8 2.925 -48.818 531.738 1.00 44.26 C ANISOU 38 CB LYS A 8 6605 7231 2982 1006 1249 1063 C ATOM 39 CG LYS A 8 1.568 -49.497 531.771 1.00 49.62 C ANISOU 39 CG LYS A 8 7248 7795 3809 941 923 1183 C ATOM 40 CD LYS A 8 0.943 -49.456 533.159 1.00 59.55 C ANISOU 40 CD LYS A 8 8145 9013 5468 1100 892 1301 C ATOM 41 CE LYS A 8 0.548 -48.047 533.566 1.00 60.92 C ANISOU 41 CE LYS A 8 8112 9225 5810 1126 846 1529 C ATOM 42 NZ LYS A 8 -0.537 -48.062 534.587 1.00 55.74 N ANISOU 42 NZ LYS A 8 7159 8496 5524 1202 685 1692 N ATOM 43 N PRO A 9 5.358 -50.946 530.666 1.00 52.55 N ANISOU 43 N PRO A 9 8118 8292 3557 967 1712 403 N ATOM 44 CA PRO A 9 5.721 -52.370 530.666 1.00 52.62 C ANISOU 44 CA PRO A 9 8205 8236 3551 986 1782 175 C ATOM 45 C PRO A 9 5.189 -53.065 531.911 1.00 46.35 C ANISOU 45 C PRO A 9 7173 7401 3039 1184 1774 221 C ATOM 46 O PRO A 9 5.361 -52.580 533.032 1.00 42.59 O ANISOU 46 O PRO A 9 6381 6914 2887 1301 1831 273 O ATOM 47 CB PRO A 9 7.253 -52.347 530.637 1.00 51.76 C ANISOU 47 CB PRO A 9 7980 8093 3595 889 1942 -86 C ATOM 48 CG PRO A 9 7.613 -51.057 531.288 1.00 51.99 C ANISOU 48 CG PRO A 9 7762 8126 3864 908 1966 1 C ATOM 49 CD PRO A 9 6.524 -50.082 530.929 1.00 51.34 C ANISOU 49 CD PRO A 9 7776 8117 3615 913 1845 283 C ATOM 50 N LEU A 10 4.538 -54.206 531.705 1.00 51.77 N ANISOU 50 N LEU A 10 7944 7984 3744 1125 1606 176 N ATOM 51 CA LEU A 10 3.958 -54.995 532.778 1.00 44.66 C ANISOU 51 CA LEU A 10 6815 6998 3154 1254 1544 206 C ATOM 52 C LEU A 10 4.664 -56.339 532.890 1.00 44.94 C ANISOU 52 C LEU A 10 6925 6983 3165 1324 1714 -48 C ATOM 53 O LEU A 10 5.288 -56.824 531.942 1.00 46.75 O ANISOU 53 O LEU A 10 7419 7214 3128 1224 1800 -236 O ATOM 54 CB LEU A 10 2.460 -55.228 532.550 1.00 49.81 C ANISOU 54 CB LEU A 10 7470 7554 3902 1133 1184 387 C ATOM 55 CG LEU A 10 1.540 -54.008 532.508 1.00 45.51 C ANISOU 55 CG LEU A 10 6823 7031 3438 1066 966 661 C ATOM 56 CD1 LEU A 10 0.091 -54.465 532.494 1.00 54.02 C ANISOU 56 CD1 LEU A 10 7858 7996 4671 981 630 809 C ATOM 57 CD2 LEU A 10 1.795 -53.073 533.679 1.00 51.89 C ANISOU 57 CD2 LEU A 10 7320 7905 4490 1242 1115 769 C ATOM 58 N CYS A 11 4.549 -56.939 534.071 1.00 47.27 N ANISOU 58 N CYS A 11 6983 7230 3746 1494 1764 -50 N ATOM 59 CA CYS A 11 5.102 -58.257 534.323 1.00 43.34 C ANISOU 59 CA CYS A 11 6520 6667 3280 1578 1906 -265 C ATOM 60 C CYS A 11 4.218 -59.334 533.707 1.00 45.30 C ANISOU 60 C CYS A 11 6931 6789 3492 1441 1677 -290 C ATOM 61 O CYS A 11 3.019 -59.125 533.502 1.00 51.12 O ANISOU 61 O CYS A 11 7657 7479 4286 1333 1395 -108 O ATOM 62 CB CYS A 11 5.238 -58.487 535.822 1.00 49.17 C ANISOU 62 CB CYS A 11 6915 7351 4418 1725 1942 -232 C ATOM 63 SG CYS A 11 6.411 -57.374 536.613 1.00 44.81 S ANISOU 63 SG CYS A 11 6091 6771 4162 1601 1925 -237 S ATOM 64 N PRO A 12 4.784 -60.510 533.416 1.00 46.38 N ANISOU 64 N PRO A 12 7212 6865 3546 1444 1794 -518 N ATOM 65 CA PRO A 12 3.975 -61.554 532.765 1.00 48.41 C ANISOU 65 CA PRO A 12 7637 7001 3756 1302 1586 -560 C ATOM 66 C PRO A 12 2.719 -61.913 533.537 1.00 58.66 C ANISOU 66 C PRO A 12 8739 8202 5348 1339 1359 -385 C ATOM 67 O PRO A 12 1.686 -62.202 532.922 1.00 56.97 O ANISOU 67 O PRO A 12 8633 7915 5098 1181 1094 -313 O ATOM 68 CB PRO A 12 4.948 -62.741 532.670 1.00 49.10 C ANISOU 68 CB PRO A 12 7835 7039 3783 1361 1811 -840 C ATOM 69 CG PRO A 12 6.030 -62.447 533.661 1.00 62.58 C ANISOU 69 CG PRO A 12 9329 8813 5636 1565 2084 -895 C ATOM 70 CD PRO A 12 6.161 -60.962 533.675 1.00 45.88 C ANISOU 70 CD PRO A 12 7112 6812 3508 1523 2062 -740 C ATOM 71 N ILE A 13 2.773 -61.895 534.870 1.00 55.31 N ANISOU 71 N ILE A 13 8029 7775 5213 1538 1455 -316 N ATOM 72 CA ILE A 13 1.612 -62.293 535.659 1.00 53.18 C ANISOU 72 CA ILE A 13 7568 7406 5233 1576 1261 -162 C ATOM 73 C ILE A 13 0.463 -61.314 535.444 1.00 50.91 C ANISOU 73 C ILE A 13 7224 7134 4985 1460 990 85 C ATOM 74 O ILE A 13 -0.687 -61.719 535.242 1.00 45.66 O ANISOU 74 O ILE A 13 6573 6372 4403 1357 733 178 O ATOM 75 CB ILE A 13 1.984 -62.410 537.149 1.00 55.16 C ANISOU 75 CB ILE A 13 7528 7663 5766 1813 1439 -140 C ATOM 76 CG1 ILE A 13 3.177 -63.355 537.330 1.00 65.13 C ANISOU 76 CG1 ILE A 13 8848 8911 6989 1932 1707 -384 C ATOM 77 CG2 ILE A 13 0.792 -62.917 537.951 1.00 47.87 C ANISOU 77 CG2 ILE A 13 6422 6627 5138 1845 1253 5 C ATOM 78 CD1 ILE A 13 3.693 -63.435 538.759 1.00 83.09 C ANISOU 78 CD1 ILE A 13 10843 11195 9531 2127 1861 -367 C ATOM 79 N LEU A 14 0.753 -60.010 535.491 1.00 54.05 N ANISOU 79 N LEU A 14 7552 7649 5336 1477 1043 194 N ATOM 80 CA LEU A 14 -0.294 -59.018 535.268 1.00 50.17 C ANISOU 80 CA LEU A 14 7003 7170 4888 1371 791 432 C ATOM 81 C LEU A 14 -0.664 -58.915 533.795 1.00 46.54 C ANISOU 81 C LEU A 14 6838 6705 4138 1139 594 430 C ATOM 82 O LEU A 14 -1.846 -58.795 533.456 1.00 47.56 O ANISOU 82 O LEU A 14 6974 6776 4319 1015 301 585 O ATOM 83 CB LEU A 14 0.142 -57.652 535.790 1.00 43.85 C ANISOU 83 CB LEU A 14 6030 6491 4139 1462 917 549 C ATOM 84 CG LEU A 14 -0.262 -57.347 537.232 1.00 52.84 C ANISOU 84 CG LEU A 14 6823 7623 5630 1628 942 691 C ATOM 85 CD1 LEU A 14 0.769 -57.901 538.205 1.00 61.09 C ANISOU 85 CD1 LEU A 14 7744 8694 6772 1831 1235 537 C ATOM 86 CD2 LEU A 14 -0.465 -55.852 537.428 1.00 42.41 C ANISOU 86 CD2 LEU A 14 5357 6391 4368 1629 912 883 C ATOM 87 N GLU A 15 0.332 -58.947 532.909 1.00 59.29 N ANISOU 87 N GLU A 15 8699 8383 5447 1075 749 255 N ATOM 88 CA GLU A 15 0.039 -58.920 531.483 1.00 50.49 C ANISOU 88 CA GLU A 15 7886 7268 4030 847 574 236 C ATOM 89 C GLU A 15 -0.886 -60.065 531.097 1.00 52.21 C ANISOU 89 C GLU A 15 8205 7359 4274 735 347 201 C ATOM 90 O GLU A 15 -1.693 -59.928 530.171 1.00 55.70 O ANISOU 90 O GLU A 15 8806 7780 4577 546 84 284 O ATOM 91 CB GLU A 15 1.341 -58.982 530.685 1.00 51.53 C ANISOU 91 CB GLU A 15 8263 7474 3842 807 817 13 C ATOM 92 CG GLU A 15 1.193 -58.632 529.214 1.00 67.13 C ANISOU 92 CG GLU A 15 10551 9485 5469 572 672 13 C ATOM 93 CD GLU A 15 2.525 -58.327 528.553 1.00 66.52 C ANISOU 93 CD GLU A 15 10674 9505 5096 546 940 -167 C ATOM 94 OE1 GLU A 15 3.575 -58.593 529.175 1.00 78.05 O ANISOU 94 OE1 GLU A 15 12046 10991 6620 707 1237 -326 O ATOM 95 OE2 GLU A 15 2.522 -57.815 527.414 1.00116.05 O ANISOU 95 OE2 GLU A 15 17191 15828 11074 364 855 -149 O ATOM 96 N GLN A 16 -0.791 -61.194 531.801 1.00 51.52 N ANISOU 96 N GLN A 16 8026 7184 4366 849 441 81 N ATOM 97 CA GLN A 16 -1.702 -62.306 531.559 1.00 53.00 C ANISOU 97 CA GLN A 16 8278 7240 4619 757 236 50 C ATOM 98 C GLN A 16 -3.047 -62.079 532.240 1.00 52.17 C ANISOU 98 C GLN A 16 7941 7067 4813 770 -18 285 C ATOM 99 O GLN A 16 -4.098 -62.348 531.647 1.00 64.09 O ANISOU 99 O GLN A 16 9536 8507 6309 616 -299 355 O ATOM 100 CB GLN A 16 -1.066 -63.609 532.042 1.00 55.99 C ANISOU 100 CB GLN A 16 8649 7543 5081 874 442 -168 C ATOM 101 CG GLN A 16 -1.672 -64.860 531.431 1.00 73.75 C ANISOU 101 CG GLN A 16 11064 9667 7292 744 289 -280 C ATOM 102 CD GLN A 16 -0.928 -66.122 531.831 1.00 73.90 C ANISOU 102 CD GLN A 16 11093 9609 7377 858 515 -508 C ATOM 103 OE1 GLN A 16 0.232 -66.070 532.239 1.00 70.93 O ANISOU 103 OE1 GLN A 16 10678 9289 6983 999 799 -624 O ATOM 104 NE2 GLN A 16 -1.596 -67.265 531.716 1.00 90.56 N ANISOU 104 NE2 GLN A 16 13251 11585 9572 797 389 -572 N ATOM 105 N MET A 17 -3.036 -61.584 533.481 1.00 55.84 N ANISOU 105 N MET A 17 8112 7552 5552 950 79 404 N ATOM 106 CA MET A 17 -4.285 -61.225 534.146 1.00 50.11 C ANISOU 106 CA MET A 17 7154 6770 5115 961 -145 633 C ATOM 107 C MET A 17 -5.052 -60.177 533.353 1.00 55.62 C ANISOU 107 C MET A 17 7915 7508 5711 799 -404 820 C ATOM 108 O MET A 17 -6.289 -60.152 533.388 1.00 56.04 O ANISOU 108 O MET A 17 7881 7484 5926 724 -676 975 O ATOM 109 CB MET A 17 -4.002 -60.705 535.555 1.00 46.39 C ANISOU 109 CB MET A 17 6370 6339 4916 1173 32 722 C ATOM 110 CG MET A 17 -3.744 -61.786 536.588 1.00 51.13 C ANISOU 110 CG MET A 17 6835 6864 5727 1335 192 616 C ATOM 111 SD MET A 17 -2.873 -61.164 538.044 1.00 50.31 S ANISOU 111 SD MET A 17 6441 6855 5819 1586 489 647 S ATOM 112 CE MET A 17 -3.746 -59.629 538.352 1.00 40.39 C ANISOU 112 CE MET A 17 4979 5656 4712 1556 320 928 C ATOM 113 N SER A 18 -4.338 -59.296 532.648 1.00 56.29 N ANISOU 113 N SER A 18 8145 7708 5535 744 -322 811 N ATOM 114 CA SER A 18 -4.998 -58.291 531.824 1.00 59.04 C ANISOU 114 CA SER A 18 8576 8095 5763 587 -565 990 C ATOM 115 C SER A 18 -5.688 -58.927 530.624 1.00 59.38 C ANISOU 115 C SER A 18 8879 8076 5609 371 -828 952 C ATOM 116 O SER A 18 -6.825 -58.570 530.293 1.00 61.39 O ANISOU 116 O SER A 18 9110 8290 5926 255 -1133 1130 O ATOM 117 CB SER A 18 -3.982 -57.246 531.365 1.00 58.00 C ANISOU 117 CB SER A 18 8549 8098 5390 583 -388 976 C ATOM 118 OG SER A 18 -4.602 -56.247 530.576 1.00 69.56 O ANISOU 118 OG SER A 18 10095 9598 6738 434 -620 1161 O ATOM 119 N ARG A 19 -5.022 -59.875 529.966 1.00 70.13 N ANISOU 119 N ARG A 19 10483 9427 6737 313 -715 717 N ATOM 120 CA ARG A 19 -5.577 -60.545 528.796 1.00 77.97 C ANISOU 120 CA ARG A 19 11739 10368 7517 102 -940 650 C ATOM 121 C ARG A 19 -6.542 -61.667 529.163 1.00 76.13 C ANISOU 121 C ARG A 19 11420 9993 7512 94 -1106 634 C ATOM 122 O ARG A 19 -7.058 -62.336 528.260 1.00 85.29 O ANISOU 122 O ARG A 19 12782 11100 8523 -77 -1296 565 O ATOM 123 CB ARG A 19 -4.442 -61.088 527.919 1.00 75.90 C ANISOU 123 CB ARG A 19 11777 10153 6909 34 -735 392 C ATOM 124 CG ARG A 19 -3.540 -59.994 527.345 1.00 82.82 C ANISOU 124 CG ARG A 19 12785 11166 7516 2 -593 400 C ATOM 125 CD ARG A 19 -2.383 -60.562 526.534 1.00 95.33 C ANISOU 125 CD ARG A 19 14654 12791 8775 -60 -366 129 C ATOM 126 NE ARG A 19 -1.395 -59.538 526.193 1.00104.28 N ANISOU 126 NE ARG A 19 15875 14053 9694 -55 -173 122 N ATOM 127 CZ ARG A 19 -1.525 -58.664 525.197 1.00115.97 C ANISOU 127 CZ ARG A 19 17544 15607 10911 -220 -304 223 C ATOM 128 NH1 ARG A 19 -2.608 -58.671 524.429 1.00106.07 N ANISOU 128 NH1 ARG A 19 16412 14318 9572 -404 -643 343 N ATOM 129 NH2 ARG A 19 -0.567 -57.774 524.970 1.00120.01 N ANISOU 129 NH2 ARG A 19 18124 16228 11248 -201 -98 206 N ATOM 130 N LEU A 20 -6.797 -61.886 530.452 1.00 80.37 N ANISOU 130 N LEU A 20 11666 10469 8401 269 -1036 692 N ATOM 131 CA LEU A 20 -7.788 -62.866 530.879 1.00 93.48 C ANISOU 131 CA LEU A 20 13221 11990 10307 264 -1197 701 C ATOM 132 C LEU A 20 -9.173 -62.401 530.444 1.00107.90 C ANISOU 132 C LEU A 20 15018 13776 12203 115 -1572 907 C ATOM 133 O LEU A 20 -9.636 -61.335 530.866 1.00101.36 O ANISOU 133 O LEU A 20 14003 12982 11527 152 -1663 1121 O ATOM 134 CB LEU A 20 -7.727 -63.045 532.395 1.00 65.54 C ANISOU 134 CB LEU A 20 9371 8407 7124 486 -1030 741 C ATOM 135 CG LEU A 20 -8.233 -64.368 532.977 1.00 72.18 C ANISOU 135 CG LEU A 20 10131 9104 8191 532 -1050 659 C ATOM 136 CD1 LEU A 20 -7.942 -64.436 534.473 1.00 63.81 C ANISOU 136 CD1 LEU A 20 8783 8027 7436 761 -839 693 C ATOM 137 CD2 LEU A 20 -9.719 -64.563 532.713 1.00104.98 C ANISOU 137 CD2 LEU A 20 14248 13156 12484 394 -1399 789 C ATOM 138 N GLN A 21 -9.834 -63.194 529.602 1.00126.65 N ANISOU 138 N GLN A 21 17572 16076 14472 -55 -1789 839 N ATOM 139 CA GLN A 21 -11.123 -62.813 529.028 1.00138.52 C ANISOU 139 CA GLN A 21 19082 17545 16005 -217 -2164 1016 C ATOM 140 C GLN A 21 -12.241 -63.390 529.892 1.00147.88 C ANISOU 140 C GLN A 21 20022 18592 17572 -167 -2310 1097 C ATOM 141 O GLN A 21 -12.570 -64.575 529.801 1.00155.54 O ANISOU 141 O GLN A 21 21053 19459 18586 -211 -2355 965 O ATOM 142 CB GLN A 21 -11.228 -63.279 527.577 1.00125.82 C ANISOU 142 CB GLN A 21 17812 15944 14051 -444 -2332 900 C ATOM 143 CG GLN A 21 -11.175 -64.792 527.367 1.00115.01 C ANISOU 143 CG GLN A 21 16573 14478 12650 -487 -2287 665 C ATOM 144 CD GLN A 21 -11.271 -65.183 525.907 1.00130.85 C ANISOU 144 CD GLN A 21 18916 16502 14299 -723 -2451 548 C ATOM 145 OE1 GLN A 21 -10.997 -64.378 525.016 1.00137.49 O ANISOU 145 OE1 GLN A 21 19940 17451 14848 -837 -2512 595 O ATOM 146 NE2 GLN A 21 -11.672 -66.425 525.654 1.00145.37 N ANISOU 146 NE2 GLN A 21 20840 18235 16157 -801 -2524 394 N ATOM 147 N SER A 22 -12.819 -62.550 530.749 1.00139.68 N ANISOU 147 N SER A 22 18703 17548 16819 -74 -2372 1311 N ATOM 148 CA SER A 22 -14.033 -62.930 531.460 1.00130.84 C ANISOU 148 CA SER A 22 17354 16301 16060 -56 -2553 1418 C ATOM 149 C SER A 22 -15.208 -62.924 530.489 1.00141.38 C ANISOU 149 C SER A 22 18791 17586 17340 -267 -2940 1505 C ATOM 150 O SER A 22 -15.383 -61.976 529.718 1.00143.36 O ANISOU 150 O SER A 22 19135 17913 17422 -376 -3109 1630 O ATOM 151 CB SER A 22 -14.294 -61.976 532.625 1.00100.88 C ANISOU 151 CB SER A 22 13231 12519 12578 93 -2502 1616 C ATOM 152 N HIS A 23 -16.013 -63.984 530.524 1.00139.33 N ANISOU 152 N HIS A 23 18516 17198 17225 -325 -3081 1442 N ATOM 153 CA HIS A 23 -17.078 -64.206 529.534 1.00145.11 C ANISOU 153 CA HIS A 23 19374 17878 17885 -536 -3443 1480 C ATOM 154 C HIS A 23 -16.401 -64.240 528.162 1.00143.30 C ANISOU 154 C HIS A 23 19505 17744 17199 -690 -3458 1352 C ATOM 155 O HIS A 23 -15.436 -65.002 527.987 1.00129.52 O ANISOU 155 O HIS A 23 17929 16016 15268 -665 -3220 1131 O ATOM 156 CB HIS A 23 -18.183 -63.166 529.713 1.00143.68 C ANISOU 156 CB HIS A 23 18985 17682 17924 -567 -3718 1748 C ATOM 157 CG HIS A 23 -19.240 -63.564 530.700 1.00142.29 C ANISOU 157 CG HIS A 23 18521 17367 18176 -505 -3813 1828 C ATOM 158 ND1 HIS A 23 -20.086 -62.651 531.293 1.00137.69 N ANISOU 158 ND1 HIS A 23 17669 16759 17888 -467 -3959 2057 N ATOM 159 CD2 HIS A 23 -19.597 -64.777 531.187 1.00138.93 C ANISOU 159 CD2 HIS A 23 18035 16816 17937 -479 -3778 1707 C ATOM 160 CE1 HIS A 23 -20.912 -63.283 532.108 1.00125.94 C ANISOU 160 CE1 HIS A 23 15968 15138 16745 -423 -4006 2071 C ATOM 161 NE2 HIS A 23 -20.637 -64.574 532.062 1.00128.05 N ANISOU 161 NE2 HIS A 23 16360 15342 16953 -428 -3899 1864 N ATOM 162 N SER A 24 -16.848 -63.441 527.169 1.00133.65 N ANISOU 162 N SER A 24 18411 16585 15784 -851 -3723 1480 N ATOM 163 CA SER A 24 -16.379 -63.578 525.787 1.00141.66 C ANISOU 163 CA SER A 24 19785 17679 16359 -1030 -3780 1358 C ATOM 164 C SER A 24 -16.199 -62.202 525.134 1.00145.75 C ANISOU 164 C SER A 24 20392 18323 16663 -1097 -3876 1530 C ATOM 165 O SER A 24 -16.964 -61.805 524.255 1.00142.96 O ANISOU 165 O SER A 24 20143 17984 16191 -1267 -4198 1648 O ATOM 166 CB SER A 24 -17.345 -64.438 524.966 1.00138.71 C ANISOU 166 CB SER A 24 19550 17224 15929 -1226 -4084 1295 C ATOM 167 OG SER A 24 -17.551 -65.702 525.571 1.00136.52 O ANISOU 167 OG SER A 24 19186 16820 15865 -1168 -3998 1143 O ATOM 168 N ALA A 25 -15.167 -61.477 525.561 1.00133.74 N ANISOU 168 N ALA A 25 18831 16895 15089 -961 -3595 1542 N ATOM 169 CA ALA A 25 -14.719 -60.254 524.893 1.00115.17 C ANISOU 169 CA ALA A 25 16606 14670 12482 -1018 -3612 1661 C ATOM 170 C ALA A 25 -15.903 -59.365 524.516 1.00 99.68 C ANISOU 170 C ALA A 25 14569 12697 10607 -1128 -3992 1925 C ATOM 171 O ALA A 25 -16.123 -59.032 523.351 1.00 95.79 O ANISOU 171 O ALA A 25 14309 12258 9828 -1311 -4213 1975 O ATOM 172 CB ALA A 25 -13.887 -60.594 523.654 1.00 90.29 C ANISOU 172 CB ALA A 25 13838 11602 8864 -1167 -3541 1472 C ATOM 173 N THR A 26 -16.676 -58.980 525.534 1.00 95.62 N ANISOU 173 N THR A 26 13721 12110 10500 -1013 -4067 2097 N ATOM 174 CA THR A 26 -17.929 -58.282 525.277 1.00 78.79 C ANISOU 174 CA THR A 26 11480 9939 8517 -1109 -4441 2340 C ATOM 175 C THR A 26 -18.203 -57.152 526.266 1.00 82.72 C ANISOU 175 C THR A 26 11652 10432 9346 -963 -4411 2564 C ATOM 176 O THR A 26 -19.298 -56.577 526.232 1.00 84.18 O ANISOU 176 O THR A 26 11692 10565 9728 -1018 -4709 2771 O ATOM 177 CB THR A 26 -19.090 -59.293 525.276 1.00 94.29 C ANISOU 177 CB THR A 26 13383 11771 10673 -1191 -4696 2305 C ATOM 178 OG1 THR A 26 -20.230 -58.722 524.623 1.00110.53 O ANISOU 178 OG1 THR A 26 15432 13804 12759 -1339 -5100 2505 O ATOM 179 CG2 THR A 26 -19.463 -59.716 526.696 1.00 98.99 C ANISOU 179 CG2 THR A 26 13642 12255 11713 -1016 -4572 2309 C ATOM 180 N SER A 27 -17.259 -56.824 527.151 1.00 73.77 N ANISOU 180 N SER A 27 10392 9347 8289 -780 -4064 2525 N ATOM 181 CA SER A 27 -17.362 -55.657 528.024 1.00 66.20 C ANISOU 181 CA SER A 27 9149 8405 7601 -647 -4002 2724 C ATOM 182 C SER A 27 -18.492 -55.759 529.045 1.00 73.13 C ANISOU 182 C SER A 27 9684 9156 8944 -574 -4130 2843 C ATOM 183 O SER A 27 -18.615 -54.893 529.918 1.00 70.67 O ANISOU 183 O SER A 27 9101 8842 8908 -450 -3961 2920 O ATOM 184 CB SER A 27 -17.540 -54.387 527.187 1.00 67.67 C ANISOU 184 CB SER A 27 9425 8661 7625 -754 -4199 2926 C ATOM 185 OG SER A 27 -17.678 -53.247 528.016 1.00 65.68 O ANISOU 185 OG SER A 27 8872 8408 7675 -619 -4017 3022 O ATOM 186 N ILE A 28 -19.317 -56.798 528.956 1.00 69.31 N ANISOU 186 N ILE A 28 9205 8566 8566 -648 -4312 2776 N ATOM 187 CA ILE A 28 -20.396 -57.005 529.916 1.00 65.36 C ANISOU 187 CA ILE A 28 8388 7936 8510 -585 -4353 2822 C ATOM 188 C ILE A 28 -19.813 -57.639 531.171 1.00 62.61 C ANISOU 188 C ILE A 28 7874 7560 8355 -398 -4083 2736 C ATOM 189 O ILE A 28 -19.056 -58.613 531.095 1.00 68.39 O ANISOU 189 O ILE A 28 8770 8303 8913 -375 -3889 2522 O ATOM 190 CB ILE A 28 -21.503 -57.880 529.307 1.00 72.33 C ANISOU 190 CB ILE A 28 9343 8712 9429 -743 -4665 2791 C ATOM 191 CG1 ILE A 28 -22.192 -57.137 528.159 1.00 92.17 C ANISOU 191 CG1 ILE A 28 11973 11243 11805 -913 -4881 2870 C ATOM 192 CG2 ILE A 28 -22.521 -58.268 530.367 1.00 78.88 C ANISOU 192 CG2 ILE A 28 9866 9400 10706 -674 -4618 2780 C ATOM 193 CD1 ILE A 28 -22.468 -58.003 526.947 1.00104.26 C ANISOU 193 CD1 ILE A 28 13798 12765 13050 -1109 -5185 2804 C ATOM 194 N ARG A 29 -20.161 -57.085 532.329 1.00 60.42 N ANISOU 194 N ARG A 29 7285 7248 8425 -270 -3876 2770 N ATOM 195 CA ARG A 29 -19.596 -57.498 533.607 1.00 59.87 C ANISOU 195 CA ARG A 29 7035 7166 8547 -83 -3589 2701 C ATOM 196 C ARG A 29 -20.616 -58.313 534.387 1.00 60.85 C ANISOU 196 C ARG A 29 6971 7147 9002 -74 -3600 2646 C ATOM 197 O ARG A 29 -21.761 -57.881 534.559 1.00 61.44 O ANISOU 197 O ARG A 29 6907 7153 9284 -146 -3648 2676 O ATOM 198 CB ARG A 29 -19.165 -56.282 534.432 1.00 55.29 C ANISOU 198 CB ARG A 29 6271 6666 8071 40 -3271 2716 C ATOM 199 CG ARG A 29 -18.027 -55.483 533.825 1.00 55.20 C ANISOU 199 CG ARG A 29 6420 6796 7757 58 -3207 2766 C ATOM 200 CD ARG A 29 -17.774 -54.211 534.616 1.00 53.05 C ANISOU 200 CD ARG A 29 5955 6586 7616 159 -2922 2772 C ATOM 201 NE ARG A 29 -16.747 -53.374 534.003 1.00 55.34 N ANISOU 201 NE ARG A 29 6390 7004 7632 169 -2864 2828 N ATOM 202 CZ ARG A 29 -16.456 -52.138 534.396 1.00 56.23 C ANISOU 202 CZ ARG A 29 6389 7178 7797 227 -2667 2845 C ATOM 203 NH1 ARG A 29 -17.115 -51.582 535.404 1.00 50.18 N ANISOU 203 NH1 ARG A 29 5384 6358 7324 266 -2514 2799 N ATOM 204 NH2 ARG A 29 -15.504 -51.453 533.777 1.00 65.35 N ANISOU 204 NH2 ARG A 29 7692 8446 8692 229 -2621 2899 N ATOM 205 N TYR A 30 -20.198 -59.484 534.859 1.00 77.55 N ANISOU 205 N TYR A 30 9091 9211 11166 14 -3551 2567 N ATOM 206 CA TYR A 30 -21.020 -60.308 535.732 1.00 63.23 C ANISOU 206 CA TYR A 30 7096 7264 9666 43 -3508 2504 C ATOM 207 C TYR A 30 -20.805 -59.885 537.179 1.00 70.94 C ANISOU 207 C TYR A 30 7837 8265 10852 194 -3117 2451 C ATOM 208 O TYR A 30 -19.669 -59.667 537.612 1.00 63.97 O ANISOU 208 O TYR A 30 6952 7476 9877 331 -2880 2420 O ATOM 209 CB TYR A 30 -20.680 -61.789 535.559 1.00 56.91 C ANISOU 209 CB TYR A 30 6447 6395 8781 46 -3515 2350 C ATOM 210 N ILE A 31 -21.902 -59.765 537.921 1.00 75.20 N ANISOU 210 N ILE A 31 8200 8723 11648 153 -3052 2433 N ATOM 211 CA ILE A 31 -21.877 -59.285 539.299 1.00 74.16 C ANISOU 211 CA ILE A 31 7891 8618 11667 242 -2705 2367 C ATOM 212 C ILE A 31 -22.299 -60.425 540.214 1.00 61.33 C ANISOU 212 C ILE A 31 6176 6887 10240 276 -2615 2282 C ATOM 213 O ILE A 31 -23.422 -60.933 540.112 1.00 50.88 O ANISOU 213 O ILE A 31 4814 5437 9079 173 -2788 2297 O ATOM 214 CB ILE A 31 -22.783 -58.058 539.484 1.00 55.06 C ANISOU 214 CB ILE A 31 5378 6196 9348 148 -2683 2415 C ATOM 215 CG1 ILE A 31 -22.226 -56.883 538.678 1.00 50.48 C ANISOU 215 CG1 ILE A 31 4880 5727 8572 134 -2726 2492 C ATOM 216 CG2 ILE A 31 -22.899 -57.701 540.963 1.00 55.64 C ANISOU 216 CG2 ILE A 31 5310 6275 9556 202 -2358 2331 C ATOM 217 CD1 ILE A 31 -23.136 -55.677 538.624 1.00 70.91 C ANISOU 217 CD1 ILE A 31 7395 8293 11254 34 -2758 2557 C ATOM 218 N ASP A 32 -21.397 -60.820 541.114 1.00 51.67 N ANISOU 218 N ASP A 32 4922 5712 8998 418 -2340 2190 N ATOM 219 CA ASP A 32 -21.687 -61.829 542.131 1.00 52.59 C ANISOU 219 CA ASP A 32 4959 5745 9278 458 -2202 2102 C ATOM 220 C ASP A 32 -22.382 -61.129 543.295 1.00 56.01 C ANISOU 220 C ASP A 32 5276 6183 9823 410 -1995 2068 C ATOM 221 O ASP A 32 -21.769 -60.745 544.295 1.00 51.50 O ANISOU 221 O ASP A 32 4682 5698 9186 481 -1713 1992 O ATOM 222 CB ASP A 32 -20.410 -62.530 542.574 1.00 63.84 C ANISOU 222 CB ASP A 32 6424 7220 10612 623 -1997 2016 C ATOM 223 CG ASP A 32 -20.656 -63.577 543.645 1.00 56.40 C ANISOU 223 CG ASP A 32 5415 6199 9815 663 -1841 1923 C ATOM 224 OD1 ASP A 32 -21.830 -63.941 543.870 1.00 64.89 O ANISOU 224 OD1 ASP A 32 6424 7161 11070 559 -1940 1936 O ATOM 225 OD2 ASP A 32 -19.672 -64.034 544.265 1.00 57.77 O ANISOU 225 OD2 ASP A 32 5609 6423 9918 793 -1616 1836 O ATOM 226 N HIS A 33 -23.699 -60.962 543.153 1.00 79.02 N ANISOU 226 N HIS A 33 8661 11531 9833 -744 -1100 1290 N ATOM 227 CA HIS A 33 -24.465 -60.236 544.162 1.00 74.46 C ANISOU 227 CA HIS A 33 7827 11094 9368 -599 -1064 1413 C ATOM 228 C HIS A 33 -24.297 -60.847 545.548 1.00 77.22 C ANISOU 228 C HIS A 33 8157 11348 9834 -615 -928 1393 C ATOM 229 O HIS A 33 -24.406 -60.138 546.555 1.00 73.13 O ANISOU 229 O HIS A 33 7507 10872 9407 -425 -836 1454 O ATOM 230 CB HIS A 33 -25.945 -60.204 543.773 1.00 74.82 C ANISOU 230 CB HIS A 33 7616 11430 9383 -705 -1222 1517 C ATOM 231 CG HIS A 33 -26.343 -58.975 543.016 1.00 82.49 C ANISOU 231 CG HIS A 33 8569 12469 10306 -522 -1258 1559 C ATOM 232 ND1 HIS A 33 -26.849 -57.853 543.636 1.00 93.10 N ANISOU 232 ND1 HIS A 33 9819 13825 11730 -279 -1166 1594 N ATOM 233 CD2 HIS A 33 -26.309 -58.691 541.693 1.00 74.83 C ANISOU 233 CD2 HIS A 33 7679 11543 9212 -556 -1379 1563 C ATOM 234 CE1 HIS A 33 -27.110 -56.930 542.727 1.00 79.87 C ANISOU 234 CE1 HIS A 33 8160 12183 10003 -178 -1237 1623 C ATOM 235 NE2 HIS A 33 -26.791 -57.413 541.540 1.00108.83 N ANISOU 235 NE2 HIS A 33 11926 15879 13546 -339 -1360 1616 N ATOM 236 N ALA A 34 -24.034 -62.153 545.623 1.00 74.69 N ANISOU 236 N ALA A 34 7975 10898 9508 -833 -920 1307 N ATOM 237 CA ALA A 34 -23.832 -62.791 546.919 1.00 49.73 C ANISOU 237 CA ALA A 34 4812 7636 6449 -862 -799 1305 C ATOM 238 C ALA A 34 -22.652 -62.171 547.658 1.00 54.70 C ANISOU 238 C ALA A 34 5557 8087 7140 -622 -639 1267 C ATOM 239 O ALA A 34 -22.767 -61.785 548.827 1.00 42.78 O ANISOU 239 O ALA A 34 3926 6617 5712 -494 -540 1324 O ATOM 240 CB ALA A 34 -23.618 -64.293 546.730 1.00 55.16 C ANISOU 240 CB ALA A 34 5676 8160 7120 -1130 -838 1214 C ATOM 241 N ALA A 35 -21.506 -62.056 546.983 1.00 54.23 N ANISOU 241 N ALA A 35 5727 7847 7032 -559 -613 1171 N ATOM 242 CA ALA A 35 -20.319 -61.518 547.636 1.00 45.87 C ANISOU 242 CA ALA A 35 4780 6618 6031 -357 -473 1136 C ATOM 243 C ALA A 35 -20.545 -60.084 548.095 1.00 36.03 C ANISOU 243 C ALA A 35 3380 5475 4832 -117 -444 1226 C ATOM 244 O ALA A 35 -20.152 -59.711 549.207 1.00 51.71 O ANISOU 244 O ALA A 35 5347 7400 6901 28 -335 1233 O ATOM 245 CB ALA A 35 -19.121 -61.592 546.690 1.00 37.53 C ANISOU 245 CB ALA A 35 3963 5399 4898 -340 -460 1032 C ATOM 246 N VAL A 36 -21.192 -59.271 547.258 1.00 42.75 N ANISOU 246 N VAL A 36 4130 6480 5632 -68 -552 1291 N ATOM 247 CA VAL A 36 -21.363 -57.855 547.575 1.00 44.76 C ANISOU 247 CA VAL A 36 4270 6799 5937 179 -546 1369 C ATOM 248 C VAL A 36 -22.066 -57.695 548.917 1.00 42.28 C ANISOU 248 C VAL A 36 3807 6557 5699 262 -460 1381 C ATOM 249 O VAL A 36 -21.608 -56.955 549.795 1.00 50.20 O ANISOU 249 O VAL A 36 4901 7431 6744 426 -345 1313 O ATOM 250 CB VAL A 36 -22.136 -57.145 546.448 1.00 50.53 C ANISOU 250 CB VAL A 36 4918 7685 6596 194 -688 1439 C ATOM 251 CG1 VAL A 36 -22.446 -55.706 546.837 1.00 47.45 C ANISOU 251 CG1 VAL A 36 4545 7236 6247 409 -624 1401 C ATOM 252 CG2 VAL A 36 -21.349 -57.196 545.142 1.00 51.14 C ANISOU 252 CG2 VAL A 36 5184 7683 6564 123 -748 1410 C ATOM 253 N LEU A 37 -23.187 -58.394 549.099 1.00 46.22 N ANISOU 253 N LEU A 37 4139 7237 6187 115 -501 1425 N ATOM 254 CA LEU A 37 -23.930 -58.267 550.347 1.00 48.40 C ANISOU 254 CA LEU A 37 4321 7579 6490 180 -401 1414 C ATOM 255 C LEU A 37 -23.109 -58.774 551.525 1.00 47.55 C ANISOU 255 C LEU A 37 4283 7345 6438 194 -273 1383 C ATOM 256 O LEU A 37 -23.091 -58.152 552.594 1.00 37.91 O ANISOU 256 O LEU A 37 3099 6080 5226 347 -170 1327 O ATOM 257 CB LEU A 37 -25.253 -59.024 550.245 1.00 44.39 C ANISOU 257 CB LEU A 37 3629 7289 5948 -10 -470 1480 C ATOM 258 CG LEU A 37 -26.147 -58.967 551.484 1.00 55.71 C ANISOU 258 CG LEU A 37 4944 8836 7386 43 -376 1489 C ATOM 259 CD1 LEU A 37 -26.510 -57.528 551.834 1.00 61.58 C ANISOU 259 CD1 LEU A 37 5688 9581 8127 305 -332 1433 C ATOM 260 CD2 LEU A 37 -27.399 -59.797 551.267 1.00 75.17 C ANISOU 260 CD2 LEU A 37 7237 11510 9812 -172 -452 1567 C ATOM 261 N LEU A 38 -22.419 -59.901 551.344 1.00 48.09 N ANISOU 261 N LEU A 38 4398 7337 6538 21 -287 1399 N ATOM 262 CA LEU A 38 -21.574 -60.443 552.402 1.00 43.06 C ANISOU 262 CA LEU A 38 3878 6534 5948 26 -161 1355 C ATOM 263 C LEU A 38 -20.579 -59.397 552.890 1.00 43.42 C ANISOU 263 C LEU A 38 4031 6439 6028 281 -73 1303 C ATOM 264 O LEU A 38 -20.578 -59.016 554.067 1.00 34.54 O ANISOU 264 O LEU A 38 2945 5284 4894 384 24 1252 O ATOM 265 CB LEU A 38 -20.846 -61.686 551.889 1.00 37.47 C ANISOU 265 CB LEU A 38 3396 5622 5221 -184 -176 1280 C ATOM 266 CG LEU A 38 -19.780 -62.292 552.803 1.00 44.91 C ANISOU 266 CG LEU A 38 4499 6352 6211 -171 -61 1229 C ATOM 267 CD1 LEU A 38 -20.417 -62.904 554.039 1.00 51.83 C ANISOU 267 CD1 LEU A 38 5241 7328 7124 -253 -6 1309 C ATOM 268 CD2 LEU A 38 -18.961 -63.323 552.042 1.00 59.13 C ANISOU 268 CD2 LEU A 38 6541 7935 7989 -319 -91 1132 C ATOM 269 N HIS A 39 -19.722 -58.917 551.987 1.00 30.03 N ANISOU 269 N HIS A 39 2485 4606 4318 342 -107 1260 N ATOM 270 CA HIS A 39 -18.727 -57.925 552.377 1.00 36.24 C ANISOU 270 CA HIS A 39 3444 5217 5109 514 -29 1170 C ATOM 271 C HIS A 39 -19.392 -56.651 552.882 1.00 30.95 C ANISOU 271 C HIS A 39 2772 4586 4401 632 -21 1097 C ATOM 272 O HIS A 39 -18.933 -56.050 553.860 1.00 34.55 O ANISOU 272 O HIS A 39 3330 4943 4854 711 44 998 O ATOM 273 CB HIS A 39 -17.799 -57.621 551.202 1.00 30.96 C ANISOU 273 CB HIS A 39 2907 4435 4422 532 -76 1161 C ATOM 274 CG HIS A 39 -16.907 -58.762 550.824 1.00 29.11 C ANISOU 274 CG HIS A 39 2826 4063 4170 398 -50 1110 C ATOM 275 ND1 HIS A 39 -17.326 -59.804 550.024 1.00 26.04 N ANISOU 275 ND1 HIS A 39 2470 3708 3717 193 -115 1085 N ATOM 276 CD2 HIS A 39 -15.618 -59.027 551.142 1.00 32.89 C ANISOU 276 CD2 HIS A 39 3466 4357 4673 429 37 1044 C ATOM 277 CE1 HIS A 39 -16.332 -60.659 549.863 1.00 35.68 C ANISOU 277 CE1 HIS A 39 3875 4759 4924 121 -67 996 C ATOM 278 NE2 HIS A 39 -15.284 -60.211 550.531 1.00 22.73 N ANISOU 278 NE2 HIS A 39 2306 2993 3337 265 29 976 N ATOM 279 N GLY A 40 -20.471 -56.219 552.228 1.00 31.48 N ANISOU 279 N GLY A 40 2722 4798 4441 638 -105 1140 N ATOM 280 CA GLY A 40 -21.167 -55.031 552.694 1.00 32.57 C ANISOU 280 CA GLY A 40 2842 4964 4569 765 -110 1075 C ATOM 281 C GLY A 40 -21.660 -55.182 554.119 1.00 38.19 C ANISOU 281 C GLY A 40 3491 5740 5279 797 -31 1042 C ATOM 282 O GLY A 40 -21.460 -54.301 554.959 1.00 32.61 O ANISOU 282 O GLY A 40 2860 4951 4578 905 0 940 O ATOM 283 N LEU A 41 -22.303 -56.314 554.414 1.00 41.84 N ANISOU 283 N LEU A 41 3810 6357 5732 683 -11 1132 N ATOM 284 CA LEU A 41 -22.700 -56.598 555.789 1.00 32.80 C ANISOU 284 CA LEU A 41 2607 5286 4571 696 71 1122 C ATOM 285 C LEU A 41 -21.482 -56.663 556.697 1.00 33.53 C ANISOU 285 C LEU A 41 2866 5200 4674 730 151 1049 C ATOM 286 O LEU A 41 -21.502 -56.137 557.816 1.00 43.64 O ANISOU 286 O LEU A 41 4179 6471 5933 817 200 976 O ATOM 287 CB LEU A 41 -23.487 -57.908 555.845 1.00 39.58 C ANISOU 287 CB LEU A 41 3294 6327 5418 518 66 1244 C ATOM 288 CG LEU A 41 -23.894 -58.421 557.230 1.00 55.94 C ANISOU 288 CG LEU A 41 5298 8495 7461 495 150 1265 C ATOM 289 CD1 LEU A 41 -24.698 -57.378 557.994 1.00 40.59 C ANISOU 289 CD1 LEU A 41 3295 6652 5474 658 180 1204 C ATOM 290 CD2 LEU A 41 -24.684 -59.715 557.096 1.00 52.45 C ANISOU 290 CD2 LEU A 41 4699 8217 7011 266 119 1390 C ATOM 291 N ALA A 42 -20.406 -57.297 556.227 1.00 32.00 N ANISOU 291 N ALA A 42 2775 4869 4514 659 159 1066 N ATOM 292 CA ALA A 42 -19.168 -57.334 556.998 1.00 35.38 C ANISOU 292 CA ALA A 42 3371 5122 4950 686 226 993 C ATOM 293 C ALA A 42 -18.692 -55.925 557.323 1.00 35.29 C ANISOU 293 C ALA A 42 3492 5001 4917 797 209 851 C ATOM 294 O ALA A 42 -18.332 -55.625 558.468 1.00 37.33 O ANISOU 294 O ALA A 42 3813 5216 5155 836 246 776 O ATOM 295 CB ALA A 42 -18.093 -58.099 556.226 1.00 27.76 C ANISOU 295 CB ALA A 42 2494 4020 4035 613 228 1024 C ATOM 296 N SER A 43 -18.696 -55.039 556.323 1.00 31.02 N ANISOU 296 N SER A 43 2982 4419 4384 836 137 819 N ATOM 297 CA SER A 43 -18.291 -53.658 556.560 1.00 21.64 C ANISOU 297 CA SER A 43 1898 3123 3202 918 92 695 C ATOM 298 C SER A 43 -19.118 -53.036 557.675 1.00 31.36 C ANISOU 298 C SER A 43 3048 4444 4425 1019 114 673 C ATOM 299 O SER A 43 -18.583 -52.338 558.544 1.00 26.04 O ANISOU 299 O SER A 43 2444 3705 3745 1083 140 621 O ATOM 300 CB SER A 43 -18.432 -52.841 555.276 1.00 21.93 C ANISOU 300 CB SER A 43 1945 3132 3255 948 3 705 C ATOM 301 OG SER A 43 -17.810 -53.487 554.176 1.00 38.99 O ANISOU 301 OG SER A 43 4148 5259 5408 870 1 771 O ATOM 302 N LEU A 44 -20.428 -53.285 557.670 1.00 35.33 N ANISOU 302 N LEU A 44 3390 5110 4924 1035 105 718 N ATOM 303 CA LEU A 44 -21.288 -52.742 558.715 1.00 38.68 C ANISOU 303 CA LEU A 44 3720 5645 5334 1140 135 698 C ATOM 304 C LEU A 44 -20.926 -53.323 560.077 1.00 39.98 C ANISOU 304 C LEU A 44 3906 5829 5456 1123 223 687 C ATOM 305 O LEU A 44 -20.673 -52.584 561.036 1.00 35.56 O ANISOU 305 O LEU A 44 3391 5243 4877 1219 250 633 O ATOM 306 CB LEU A 44 -22.750 -53.031 558.376 1.00 42.16 C ANISOU 306 CB LEU A 44 3962 6293 5763 1144 119 774 C ATOM 307 CG LEU A 44 -23.779 -52.604 559.422 1.00 48.71 C ANISOU 307 CG LEU A 44 4666 7271 6571 1247 155 752 C ATOM 308 CD1 LEU A 44 -23.720 -51.102 559.636 1.00 47.17 C ANISOU 308 CD1 LEU A 44 4522 7000 6402 1420 125 682 C ATOM 309 CD2 LEU A 44 -25.170 -53.043 558.999 1.00 44.24 C ANISOU 309 CD2 LEU A 44 3885 6949 5975 1226 146 860 C ATOM 310 N LEU A 45 -20.878 -54.652 560.174 1.00 39.07 N ANISOU 310 N LEU A 45 3754 5769 5321 1008 268 763 N ATOM 311 CA LEU A 45 -20.568 -55.290 561.450 1.00 44.16 C ANISOU 311 CA LEU A 45 4414 6440 5927 986 344 773 C ATOM 312 C LEU A 45 -19.212 -54.836 561.975 1.00 32.97 C ANISOU 312 C LEU A 45 3176 4841 4509 1010 352 689 C ATOM 313 O LEU A 45 -19.089 -54.413 563.130 1.00 37.65 O ANISOU 313 O LEU A 45 3787 5456 5060 1085 389 655 O ATOM 314 CB LEU A 45 -20.597 -56.810 561.292 1.00 46.25 C ANISOU 314 CB LEU A 45 4612 6773 6188 854 384 912 C ATOM 315 CG LEU A 45 -21.983 -57.453 561.239 1.00 43.32 C ANISOU 315 CG LEU A 45 4026 6642 5792 792 390 1031 C ATOM 316 CD1 LEU A 45 -21.890 -58.886 560.746 1.00 33.56 C ANISOU 316 CD1 LEU A 45 2735 5425 4590 613 388 1161 C ATOM 317 CD2 LEU A 45 -22.636 -57.405 562.609 1.00 58.82 C ANISOU 317 CD2 LEU A 45 5902 8759 7687 843 451 1034 C ATOM 318 N GLY A 46 -18.183 -54.899 561.128 1.00 34.75 N ANISOU 318 N GLY A 46 3524 4913 4766 952 322 674 N ATOM 319 CA GLY A 46 -16.843 -54.566 561.585 1.00 37.45 C ANISOU 319 CA GLY A 46 4016 5116 5098 953 339 626 C ATOM 320 C GLY A 46 -16.747 -53.159 562.144 1.00 32.93 C ANISOU 320 C GLY A 46 3475 4519 4517 1069 317 553 C ATOM 321 O GLY A 46 -16.053 -52.920 563.134 1.00 33.20 O ANISOU 321 O GLY A 46 3577 4514 4525 1093 340 515 O ATOM 322 N LEU A 47 -17.440 -52.209 561.516 1.00 25.81 N ANISOU 322 N LEU A 47 2523 3636 3646 1145 262 534 N ATOM 323 CA LEU A 47 -17.402 -50.832 561.994 1.00 26.94 C ANISOU 323 CA LEU A 47 2693 3737 3807 1266 227 462 C ATOM 324 C LEU A 47 -18.112 -50.697 563.334 1.00 32.44 C ANISOU 324 C LEU A 47 3314 4555 4455 1365 276 440 C ATOM 325 O LEU A 47 -17.585 -50.085 564.270 1.00 36.80 O ANISOU 325 O LEU A 47 3927 5062 4992 1428 282 378 O ATOM 326 CB LEU A 47 -18.032 -49.907 560.953 1.00 37.31 C ANISOU 326 CB LEU A 47 3964 5033 5177 1331 150 460 C ATOM 327 CG LEU A 47 -17.288 -49.858 559.618 1.00 38.31 C ANISOU 327 CG LEU A 47 4172 5047 5339 1249 95 480 C ATOM 328 CD1 LEU A 47 -18.190 -49.315 558.521 1.00 38.87 C ANISOU 328 CD1 LEU A 47 4171 5147 5451 1300 19 511 C ATOM 329 CD2 LEU A 47 -16.031 -49.017 559.753 1.00 41.97 C ANISOU 329 CD2 LEU A 47 4761 5356 5830 1248 61 427 C ATOM 330 N VAL A 48 -19.312 -51.269 563.447 1.00 28.16 N ANISOU 330 N VAL A 48 2630 4183 3884 1379 309 491 N ATOM 331 CA VAL A 48 -20.074 -51.146 564.684 1.00 29.58 C ANISOU 331 CA VAL A 48 2720 4517 4002 1479 363 478 C ATOM 332 C VAL A 48 -19.408 -51.935 565.804 1.00 34.73 C ANISOU 332 C VAL A 48 3422 5182 4592 1427 426 489 C ATOM 333 O VAL A 48 -19.307 -51.458 566.941 1.00 45.24 O ANISOU 333 O VAL A 48 4769 6549 5871 1520 452 438 O ATOM 334 CB VAL A 48 -21.528 -51.598 564.461 1.00 35.38 C ANISOU 334 CB VAL A 48 3268 5455 4718 1488 383 544 C ATOM 335 CG1 VAL A 48 -22.329 -51.453 565.743 1.00 27.96 C ANISOU 335 CG1 VAL A 48 2222 4704 3696 1597 447 534 C ATOM 336 CG2 VAL A 48 -22.168 -50.797 563.335 1.00 37.89 C ANISOU 336 CG2 VAL A 48 3535 5761 5100 1547 310 539 C ATOM 337 N GLU A 49 -18.947 -53.150 565.508 1.00 32.07 N ANISOU 337 N GLU A 49 3111 4815 4261 1286 446 556 N ATOM 338 CA GLU A 49 -18.335 -53.982 566.539 1.00 22.54 C ANISOU 338 CA GLU A 49 1945 3615 3005 1236 499 582 C ATOM 339 C GLU A 49 -17.122 -53.292 567.151 1.00 29.26 C ANISOU 339 C GLU A 49 2939 4334 3845 1276 484 506 C ATOM 340 O GLU A 49 -17.095 -52.998 568.351 1.00 32.31 O ANISOU 340 O GLU A 49 3325 4783 4170 1356 512 472 O ATOM 341 CB GLU A 49 -17.941 -55.337 565.953 1.00 30.29 C ANISOU 341 CB GLU A 49 2944 4545 4019 1085 508 662 C ATOM 342 CG GLU A 49 -19.108 -56.252 565.650 1.00 23.29 C ANISOU 342 CG GLU A 49 1899 3811 3138 1017 526 746 C ATOM 343 CD GLU A 49 -18.657 -57.587 565.101 1.00 32.60 C ANISOU 343 CD GLU A 49 3094 4942 4352 890 543 859 C ATOM 344 OE1 GLU A 49 -19.500 -58.497 564.967 1.00 60.82 O ANISOU 344 OE1 GLU A 49 6525 8662 7922 818 567 986 O ATOM 345 OE2 GLU A 49 -17.454 -57.724 564.800 1.00 33.91 O ANISOU 345 OE2 GLU A 49 3405 4926 4553 852 528 824 O ATOM 346 N ASN A 50 -16.100 -53.025 566.337 1.00 37.28 N ANISOU 346 N ASN A 50 4069 5182 4915 1218 439 480 N ATOM 347 CA ASN A 50 -14.901 -52.390 566.867 1.00 34.18 C ANISOU 347 CA ASN A 50 3794 4674 4519 1234 418 413 C ATOM 348 C ASN A 50 -15.190 -51.004 567.424 1.00 32.12 C ANISOU 348 C ASN A 50 3527 4420 4256 1375 386 325 C ATOM 349 O ASN A 50 -14.411 -50.502 568.242 1.00 28.70 O ANISOU 349 O ASN A 50 3165 3934 3806 1411 374 268 O ATOM 350 CB ASN A 50 -13.822 -52.320 565.787 1.00 20.03 C ANISOU 350 CB ASN A 50 2098 2730 2783 1139 377 408 C ATOM 351 CG ASN A 50 -13.157 -53.662 565.548 1.00 29.24 C ANISOU 351 CG ASN A 50 3301 3864 3944 1014 418 477 C ATOM 352 OD1 ASN A 50 -12.370 -54.130 566.372 1.00 32.20 O ANISOU 352 OD1 ASN A 50 3728 4218 4290 986 446 484 O ATOM 353 ND2 ASN A 50 -13.475 -54.292 564.423 1.00 27.96 N ANISOU 353 ND2 ASN A 50 3114 3696 3816 945 417 526 N ATOM 354 N GLY A 51 -16.291 -50.377 567.007 1.00 30.31 N ANISOU 354 N GLY A 51 3213 4255 4049 1462 367 313 N ATOM 355 CA GLY A 51 -16.668 -49.106 567.603 1.00 32.17 C ANISOU 355 CA GLY A 51 3438 4501 4282 1617 343 230 C ATOM 356 C GLY A 51 -17.076 -49.249 569.057 1.00 31.99 C ANISOU 356 C GLY A 51 3371 4627 4158 1709 403 209 C ATOM 357 O GLY A 51 -16.596 -48.515 569.925 1.00 43.26 O ANISOU 357 O GLY A 51 4862 6017 5559 1794 389 131 O ATOM 358 N VAL A 52 -17.966 -50.202 569.346 1.00 33.32 N ANISOU 358 N VAL A 52 3423 4972 4263 1692 468 280 N ATOM 359 CA VAL A 52 -18.406 -50.399 570.724 1.00 36.18 C ANISOU 359 CA VAL A 52 3725 5506 4516 1776 530 273 C ATOM 360 C VAL A 52 -17.264 -50.927 571.581 1.00 38.36 C ANISOU 360 C VAL A 52 4099 5726 4749 1716 546 275 C ATOM 361 O VAL A 52 -17.168 -50.600 572.770 1.00 40.95 O ANISOU 361 O VAL A 52 4439 6127 4995 1812 566 223 O ATOM 362 CB VAL A 52 -19.638 -51.326 570.775 1.00 39.79 C ANISOU 362 CB VAL A 52 4015 6182 4923 1750 593 368 C ATOM 363 CG1 VAL A 52 -20.795 -50.709 570.003 1.00 30.01 C ANISOU 363 CG1 VAL A 52 2664 5018 3719 1828 573 361 C ATOM 364 CG2 VAL A 52 -19.317 -52.710 570.225 1.00 47.19 C ANISOU 364 CG2 VAL A 52 4951 7085 5894 1567 608 476 C ATOM 365 N ILE A 53 -16.386 -51.751 571.005 1.00 42.63 N ANISOU 365 N ILE A 53 4711 6146 5340 1566 536 333 N ATOM 366 CA ILE A 53 -15.241 -52.256 571.758 1.00 36.55 C ANISOU 366 CA ILE A 53 4033 5316 4540 1513 545 340 C ATOM 367 C ILE A 53 -14.340 -51.105 572.187 1.00 30.85 C ANISOU 367 C ILE A 53 3417 4480 3826 1583 492 231 C ATOM 368 O ILE A 53 -13.883 -51.049 573.335 1.00 27.85 O ANISOU 368 O ILE A 53 3070 4135 3375 1633 503 198 O ATOM 369 CB ILE A 53 -14.473 -53.296 570.922 1.00 40.22 C ANISOU 369 CB ILE A 53 4552 5664 5064 1352 542 418 C ATOM 370 CG1 ILE A 53 -15.288 -54.587 570.788 1.00 43.49 C ANISOU 370 CG1 ILE A 53 4864 6193 5469 1282 595 531 C ATOM 371 CG2 ILE A 53 -13.109 -53.575 571.537 1.00 35.76 C ANISOU 371 CG2 ILE A 53 4095 5005 4486 1307 537 411 C ATOM 372 CD1 ILE A 53 -15.538 -55.314 572.100 1.00 23.01 C ANISOU 372 CD1 ILE A 53 2210 3744 2789 1301 654 585 C ATOM 373 N LEU A 54 -14.072 -50.169 571.275 1.00 32.27 N ANISOU 373 N LEU A 54 3644 4525 4092 1585 428 178 N ATOM 374 CA LEU A 54 -13.248 -49.019 571.625 1.00 31.02 C ANISOU 374 CA LEU A 54 3577 4251 3960 1645 368 81 C ATOM 375 C LEU A 54 -13.882 -48.196 572.739 1.00 36.07 C ANISOU 375 C LEU A 54 4192 4990 4522 1821 374 -3 C ATOM 376 O LEU A 54 -13.167 -47.625 573.570 1.00 39.48 O ANISOU 376 O LEU A 54 4699 5377 4925 1876 344 -76 O ATOM 377 CB LEU A 54 -13.008 -48.148 570.391 1.00 40.68 C ANISOU 377 CB LEU A 54 4834 5322 5298 1619 298 58 C ATOM 378 CG LEU A 54 -11.650 -48.292 569.698 1.00 37.86 C ANISOU 378 CG LEU A 54 4558 4814 5012 1481 257 76 C ATOM 379 CD1 LEU A 54 -11.304 -49.751 569.431 1.00 47.44 C ANISOU 379 CD1 LEU A 54 5767 6063 6195 1350 307 163 C ATOM 380 CD2 LEU A 54 -11.641 -47.506 568.397 1.00 43.75 C ANISOU 380 CD2 LEU A 54 5310 5446 5865 1460 195 73 C ATOM 381 N PHE A 55 -15.214 -48.116 572.774 1.00 38.15 N ANISOU 381 N PHE A 55 4349 5401 4745 1918 411 3 N ATOM 382 CA PHE A 55 -15.875 -47.352 573.827 1.00 43.19 C ANISOU 382 CA PHE A 55 4955 6161 5295 2103 423 -85 C ATOM 383 C PHE A 55 -15.827 -48.086 575.161 1.00 46.20 C ANISOU 383 C PHE A 55 5309 6701 5543 2124 485 -70 C ATOM 384 O PHE A 55 -15.473 -47.500 576.191 1.00 53.27 O ANISOU 384 O PHE A 55 6258 7614 6368 2230 469 -161 O ATOM 385 CB PHE A 55 -17.322 -47.056 573.438 1.00 50.50 C ANISOU 385 CB PHE A 55 5756 7218 6215 2205 446 -80 C ATOM 386 CG PHE A 55 -18.157 -46.545 574.577 1.00 50.96 C ANISOU 386 CG PHE A 55 5749 7462 6154 2398 482 -156 C ATOM 387 CD1 PHE A 55 -18.003 -45.248 575.039 1.00 58.20 C ANISOU 387 CD1 PHE A 55 6741 8309 7064 2560 427 -290 C ATOM 388 CD2 PHE A 55 -19.090 -47.363 575.190 1.00 36.52 C ANISOU 388 CD2 PHE A 55 3779 5883 4214 2419 569 -95 C ATOM 389 CE1 PHE A 55 -18.766 -44.776 576.089 1.00 54.92 C ANISOU 389 CE1 PHE A 55 6267 8072 6526 2753 459 -374 C ATOM 390 CE2 PHE A 55 -19.857 -46.897 576.240 1.00 53.79 C ANISOU 390 CE2 PHE A 55 5893 8266 6277 2602 608 -167 C ATOM 391 CZ PHE A 55 -19.694 -45.602 576.690 1.00 70.34 C ANISOU 391 CZ PHE A 55 8072 10294 8361 2776 554 -314 C ATOM 392 N VAL A 56 -16.177 -49.374 575.164 1.00 41.01 N ANISOU 392 N VAL A 56 4569 6162 4852 2025 552 46 N ATOM 393 CA VAL A 56 -16.216 -50.133 576.413 1.00 42.13 C ANISOU 393 CA VAL A 56 4667 6470 4869 2040 615 82 C ATOM 394 C VAL A 56 -14.836 -50.156 577.059 1.00 50.84 C ANISOU 394 C VAL A 56 5897 7457 5961 2006 581 48 C ATOM 395 O VAL A 56 -14.659 -49.750 578.213 1.00 59.72 O ANISOU 395 O VAL A 56 7044 8658 6988 2115 583 -25 O ATOM 396 CB VAL A 56 -16.733 -51.560 576.160 1.00 44.00 C ANISOU 396 CB VAL A 56 4800 6818 5100 1912 680 230 C ATOM 397 CG1 VAL A 56 -16.572 -52.416 577.413 1.00 54.00 C ANISOU 397 CG1 VAL A 56 6033 8229 6255 1902 738 287 C ATOM 398 CG2 VAL A 56 -18.185 -51.527 575.714 1.00 49.80 C ANISOU 398 CG2 VAL A 56 5384 7713 5826 1956 715 263 C ATOM 399 N VAL A 57 -13.836 -50.630 576.314 1.00 51.63 N ANISOU 399 N VAL A 57 6079 7383 6157 1859 549 98 N ATOM 400 CA VAL A 57 -12.482 -50.710 576.852 1.00 49.27 C ANISOU 400 CA VAL A 57 5887 6979 5854 1817 516 76 C ATOM 401 C VAL A 57 -11.948 -49.317 577.156 1.00 48.03 C ANISOU 401 C VAL A 57 5818 6725 5709 1918 442 -62 C ATOM 402 O VAL A 57 -11.243 -49.108 578.150 1.00 58.64 O ANISOU 402 O VAL A 57 7218 8072 6990 1967 422 -117 O ATOM 403 CB VAL A 57 -11.564 -51.465 575.872 1.00 36.25 C ANISOU 403 CB VAL A 57 4293 5174 4305 1646 499 154 C ATOM 404 CG1 VAL A 57 -10.139 -51.502 576.400 1.00 52.85 C ANISOU 404 CG1 VAL A 57 6494 7179 6409 1608 463 131 C ATOM 405 CG2 VAL A 57 -12.084 -52.875 575.633 1.00 32.50 C ANISOU 405 CG2 VAL A 57 3743 4783 3821 1555 565 288 C ATOM 406 N GLY A 58 -12.275 -48.345 576.309 1.00 37.38 N ANISOU 406 N GLY A 58 4479 5283 4440 1954 396 -117 N ATOM 407 CA GLY A 58 -11.720 -47.012 576.431 1.00 44.17 C ANISOU 407 CA GLY A 58 5431 6015 5339 2034 313 -236 C ATOM 408 C GLY A 58 -12.310 -46.173 577.546 1.00 61.29 C ANISOU 408 C GLY A 58 7596 8291 7400 2231 308 -353 C ATOM 409 O GLY A 58 -11.568 -45.611 578.359 1.00 72.24 O ANISOU 409 O GLY A 58 9068 9631 8750 2290 258 -442 O ATOM 410 N CYS A 59 -13.640 -46.076 577.603 1.00 55.23 N ANISOU 410 N CYS A 59 6728 7677 6578 2341 356 -359 N ATOM 411 CA CYS A 59 -14.304 -45.170 578.531 1.00 64.17 C ANISOU 411 CA CYS A 59 7850 8918 7612 2550 350 -483 C ATOM 412 C CYS A 59 -14.946 -45.855 579.728 1.00 58.44 C ANISOU 412 C CYS A 59 7029 8455 6720 2627 437 -469 C ATOM 413 O CYS A 59 -15.150 -45.195 580.752 1.00 78.78 O ANISOU 413 O CYS A 59 9618 11125 9189 2795 429 -586 O ATOM 414 CB CYS A 59 -15.386 -44.362 577.798 1.00 63.70 C ANISOU 414 CB CYS A 59 7737 8860 7604 2658 337 -519 C ATOM 415 SG CYS A 59 -14.753 -43.228 576.538 1.00 50.15 S ANISOU 415 SG CYS A 59 6135 6848 6072 2618 224 -555 S ATOM 416 N ARG A 60 -15.271 -47.144 579.633 1.00 42.20 N ANISOU 416 N ARG A 60 4875 6522 4637 2512 517 -329 N ATOM 417 CA ARG A 60 -16.011 -47.840 580.679 1.00 56.70 C ANISOU 417 CA ARG A 60 6593 8630 6320 2570 607 -289 C ATOM 418 C ARG A 60 -15.204 -48.984 581.287 1.00 52.05 C ANISOU 418 C ARG A 60 6021 8069 5687 2448 639 -195 C ATOM 419 O ARG A 60 -15.773 -49.990 581.713 1.00 53.84 O ANISOU 419 O ARG A 60 6133 8488 5836 2406 721 -87 O ATOM 420 CB ARG A 60 -17.338 -48.367 580.131 1.00 50.12 C ANISOU 420 CB ARG A 60 5599 7961 5484 2555 678 -194 C ATOM 421 CG ARG A 60 -18.305 -47.289 579.663 1.00 70.44 C ANISOU 421 CG ARG A 60 8127 10557 8081 2705 658 -281 C ATOM 422 CD ARG A 60 -18.958 -46.571 580.832 1.00 73.88 C ANISOU 422 CD ARG A 60 8514 11191 8367 2927 684 -400 C ATOM 423 NE ARG A 60 -20.080 -45.736 580.406 1.00 99.12 N ANISOU 423 NE ARG A 60 11632 14456 11575 3080 683 -461 N ATOM 424 CZ ARG A 60 -19.989 -44.451 580.073 1.00102.12 C ANISOU 424 CZ ARG A 60 12104 14674 12023 3210 602 -592 C ATOM 425 NH1 ARG A 60 -18.820 -43.822 580.112 1.00 90.44 N ANISOU 425 NH1 ARG A 60 10800 12957 10606 3194 512 -676 N ATOM 426 NH2 ARG A 60 -21.076 -43.788 579.700 1.00 96.96 N ANISOU 426 NH2 ARG A 60 11363 14099 11379 3357 607 -635 N ATOM 427 N MET A 61 -13.881 -48.848 581.345 1.00 44.09 N ANISOU 427 N MET A 61 5146 6876 4729 2388 574 -227 N ATOM 428 CA MET A 61 -13.037 -49.930 581.831 1.00 45.40 C ANISOU 428 CA MET A 61 5332 7048 4869 2276 598 -134 C ATOM 429 C MET A 61 -11.798 -49.345 582.492 1.00 52.50 C ANISOU 429 C MET A 61 6361 7834 5753 2313 526 -235 C ATOM 430 O MET A 61 -11.275 -48.319 582.049 1.00 51.08 O ANISOU 430 O MET A 61 6276 7477 5654 2337 441 -335 O ATOM 431 CB MET A 61 -12.643 -50.873 580.686 1.00 54.38 C ANISOU 431 CB MET A 61 6478 8048 6135 2087 601 -3 C ATOM 432 CG MET A 61 -12.561 -52.341 581.078 1.00 43.38 C ANISOU 432 CG MET A 61 5027 6755 4702 1985 668 143 C ATOM 433 SD MET A 61 -12.909 -53.437 579.687 1.00 63.01 S ANISOU 433 SD MET A 61 7463 9166 7313 1812 695 292 S ATOM 434 CE MET A 61 -12.840 -55.037 580.491 1.00 53.67 C ANISOU 434 CE MET A 61 6213 8128 6050 1744 769 461 C ATOM 435 N ARG A 62 -11.336 -50.006 583.552 1.00 47.90 N ANISOU 435 N ARG A 62 5774 7357 5069 2312 556 -202 N ATOM 436 CA ARG A 62 -10.156 -49.553 584.281 1.00 55.61 C ANISOU 436 CA ARG A 62 6862 8251 6016 2348 489 -293 C ATOM 437 C ARG A 62 -8.931 -49.696 583.385 1.00 51.80 C ANISOU 437 C ARG A 62 6473 7526 5684 2202 424 -254 C ATOM 438 O ARG A 62 -8.547 -50.812 583.021 1.00 54.82 O ANISOU 438 O ARG A 62 6836 7882 6111 2071 458 -122 O ATOM 439 CB ARG A 62 -9.992 -50.358 585.569 1.00 54.60 C ANISOU 439 CB ARG A 62 6701 8356 5687 2428 535 -234 C ATOM 440 CG ARG A 62 -8.961 -49.786 586.533 1.00 83.50 C ANISOU 440 CG ARG A 62 10468 12003 9253 2533 459 -351 C ATOM 441 CD ARG A 62 -8.915 -50.561 587.849 1.00 77.07 C ANISOU 441 CD ARG A 62 9602 11455 8225 2622 513 -291 C ATOM 442 NE ARG A 62 -8.184 -51.823 587.731 1.00 83.70 N ANISOU 442 NE ARG A 62 10438 12282 9084 2509 541 -115 N ATOM 443 CZ ARG A 62 -6.872 -51.957 587.917 1.00 80.36 C ANISOU 443 CZ ARG A 62 10113 11753 8667 2496 476 -116 C ATOM 444 NH1 ARG A 62 -6.124 -50.906 588.230 1.00 83.39 N ANISOU 444 NH1 ARG A 62 10608 12032 9043 2574 372 -287 N ATOM 445 NH2 ARG A 62 -6.304 -53.148 587.787 1.00 68.47 N ANISOU 445 NH2 ARG A 62 8594 10244 7178 2410 513 57 N ATOM 446 N GLN A 63 -8.314 -48.569 583.032 1.00 45.78 N ANISOU 446 N GLN A 63 5807 6589 4999 2224 329 -368 N ATOM 447 CA GLN A 63 -7.213 -48.571 582.073 1.00 51.86 C ANISOU 447 CA GLN A 63 6646 7143 5917 2083 269 -334 C ATOM 448 C GLN A 63 -5.996 -49.256 582.679 1.00 37.61 C ANISOU 448 C GLN A 63 4881 5318 4090 2022 256 -294 C ATOM 449 O GLN A 63 -5.414 -48.767 583.652 1.00 64.85 O ANISOU 449 O GLN A 63 8387 8782 7471 2104 207 -388 O ATOM 450 CB GLN A 63 -6.880 -47.144 581.648 1.00 44.00 C ANISOU 450 CB GLN A 63 5732 5981 5004 2126 170 -459 C ATOM 451 CG GLN A 63 -7.892 -46.545 580.691 1.00 62.15 C ANISOU 451 CG GLN A 63 7996 8249 7368 2152 175 -470 C ATOM 452 CD GLN A 63 -8.061 -47.380 579.438 1.00 70.48 C ANISOU 452 CD GLN A 63 8995 9262 8522 2000 222 -336 C ATOM 453 OE1 GLN A 63 -7.104 -47.982 578.947 1.00 71.94 O ANISOU 453 OE1 GLN A 63 9201 9353 8779 1861 214 -265 O ATOM 454 NE2 GLN A 63 -9.284 -47.436 578.923 1.00 69.63 N ANISOU 454 NE2 GLN A 63 8809 9233 8414 2033 271 -307 N ATOM 455 N THR A 64 -5.615 -50.388 582.101 1.00 44.53 N ANISOU 455 N THR A 64 5731 6162 5026 1886 297 -160 N ATOM 456 CA THR A 64 -4.413 -51.124 582.464 1.00 44.85 C ANISOU 456 CA THR A 64 5804 6165 5072 1819 285 -105 C ATOM 457 C THR A 64 -3.490 -51.190 581.245 1.00 45.58 C ANISOU 457 C THR A 64 5927 6071 5321 1674 245 -68 C ATOM 458 O THR A 64 -3.750 -50.573 580.207 1.00 46.38 O ANISOU 458 O THR A 64 6029 6077 5515 1633 222 -92 O ATOM 459 CB THR A 64 -4.775 -52.520 582.977 1.00 46.75 C ANISOU 459 CB THR A 64 5991 6572 5199 1833 376 38 C ATOM 460 OG1 THR A 64 -5.445 -53.254 581.944 1.00 49.16 O ANISOU 460 OG1 THR A 64 6233 6842 5604 1708 431 137 O ATOM 461 CG2 THR A 64 -5.683 -52.426 584.192 1.00 65.74 C ANISOU 461 CG2 THR A 64 8354 9226 7397 2017 419 18 C ATOM 462 N VAL A 65 -2.394 -51.937 581.380 1.00 50.74 N ANISOU 462 N VAL A 65 6597 6683 5999 1603 238 -8 N ATOM 463 CA VAL A 65 -1.485 -52.118 580.252 1.00 44.42 C ANISOU 463 CA VAL A 65 5805 5736 5337 1468 211 31 C ATOM 464 C VAL A 65 -2.094 -53.062 579.223 1.00 30.67 C ANISOU 464 C VAL A 65 4019 3997 3635 1373 283 135 C ATOM 465 O VAL A 65 -2.002 -52.824 578.013 1.00 29.02 O ANISOU 465 O VAL A 65 3805 3695 3526 1290 268 135 O ATOM 466 CB VAL A 65 -0.115 -52.619 580.744 1.00 42.10 C ANISOU 466 CB VAL A 65 5530 5406 5059 1435 178 57 C ATOM 467 CG1 VAL A 65 0.676 -53.232 579.602 1.00 24.89 C ANISOU 467 CG1 VAL A 65 3330 3125 3001 1296 182 125 C ATOM 468 CG2 VAL A 65 0.667 -51.475 581.373 1.00 53.85 C ANISOU 468 CG2 VAL A 65 7067 6839 6553 1499 81 -57 C ATOM 469 N VAL A 66 -2.726 -54.143 579.682 1.00 30.39 N ANISOU 469 N VAL A 66 3951 4072 3524 1387 359 227 N ATOM 470 CA VAL A 66 -3.311 -55.104 578.753 1.00 25.85 C ANISOU 470 CA VAL A 66 3341 3492 2989 1298 423 329 C ATOM 471 C VAL A 66 -4.425 -54.451 577.945 1.00 28.69 C ANISOU 471 C VAL A 66 3672 3854 3375 1307 426 296 C ATOM 472 O VAL A 66 -4.535 -54.660 576.731 1.00 28.01 O ANISOU 472 O VAL A 66 3578 3698 3366 1217 435 326 O ATOM 473 CB VAL A 66 -3.809 -56.348 579.510 1.00 34.07 C ANISOU 473 CB VAL A 66 4344 4648 3952 1318 499 447 C ATOM 474 CG1 VAL A 66 -4.522 -57.292 578.557 1.00 49.68 C ANISOU 474 CG1 VAL A 66 6284 6611 5982 1231 560 548 C ATOM 475 CG2 VAL A 66 -2.645 -57.063 580.181 1.00 45.96 C ANISOU 475 CG2 VAL A 66 5877 6138 5449 1305 495 489 C ATOM 476 N THR A 67 -5.267 -53.646 578.601 1.00 38.08 N ANISOU 476 N THR A 67 4840 5134 4495 1424 420 229 N ATOM 477 CA THR A 67 -6.316 -52.937 577.875 1.00 27.12 C ANISOU 477 CA THR A 67 3419 3750 3136 1450 418 189 C ATOM 478 C THR A 67 -5.730 -52.067 576.774 1.00 35.44 C ANISOU 478 C THR A 67 4512 4649 4305 1390 352 129 C ATOM 479 O THR A 67 -6.360 -51.882 575.727 1.00 43.68 O ANISOU 479 O THR A 67 5528 5662 5406 1356 356 139 O ATOM 480 CB THR A 67 -7.147 -52.073 578.828 1.00 39.49 C ANISOU 480 CB THR A 67 4960 5435 4608 1604 415 102 C ATOM 481 OG1 THR A 67 -6.309 -51.081 579.435 1.00 52.48 O ANISOU 481 OG1 THR A 67 6675 7019 6245 1667 343 -10 O ATOM 482 CG2 THR A 67 -7.800 -52.923 579.910 1.00 41.04 C ANISOU 482 CG2 THR A 67 5091 5821 4682 1663 487 169 C ATOM 483 N THR A 68 -4.528 -51.529 576.988 1.00 30.83 N ANISOU 483 N THR A 68 3982 3973 3759 1378 290 73 N ATOM 484 CA THR A 68 -3.913 -50.679 575.976 1.00 29.63 C ANISOU 484 CA THR A 68 3851 3682 3724 1318 226 30 C ATOM 485 C THR A 68 -3.541 -51.475 574.730 1.00 24.99 C ANISOU 485 C THR A 68 3244 3042 3208 1183 249 108 C ATOM 486 O THR A 68 -3.615 -50.944 573.616 1.00 26.11 O ANISOU 486 O THR A 68 3377 3115 3430 1139 221 96 O ATOM 487 CB THR A 68 -2.685 -49.976 576.556 1.00 36.65 C ANISOU 487 CB THR A 68 4791 4494 4641 1334 154 -35 C ATOM 488 OG1 THR A 68 -3.036 -49.352 577.799 1.00 36.67 O ANISOU 488 OG1 THR A 68 4824 4561 4549 1471 134 -117 O ATOM 489 CG2 THR A 68 -2.172 -48.912 575.593 1.00 26.80 C ANISOU 489 CG2 THR A 68 3557 3108 3519 1289 88 -72 C ATOM 490 N TRP A 69 -3.146 -52.742 574.886 1.00 29.43 N ANISOU 490 N TRP A 69 3804 3640 3739 1124 298 186 N ATOM 491 CA TRP A 69 -2.907 -53.577 573.712 1.00 18.99 C ANISOU 491 CA TRP A 69 2469 2282 2464 1012 332 254 C ATOM 492 C TRP A 69 -4.211 -53.861 572.976 1.00 26.27 C ANISOU 492 C TRP A 69 3358 3244 3378 1003 378 296 C ATOM 493 O TRP A 69 -4.290 -53.717 571.751 1.00 29.55 O ANISOU 493 O TRP A 69 3765 3614 3850 944 370 300 O ATOM 494 CB TRP A 69 -2.236 -54.892 574.110 1.00 25.66 C ANISOU 494 CB TRP A 69 3320 3146 3282 965 380 328 C ATOM 495 CG TRP A 69 -0.977 -54.753 574.922 1.00 24.24 C ANISOU 495 CG TRP A 69 3164 2942 3106 983 335 297 C ATOM 496 CD1 TRP A 69 -0.736 -55.295 576.149 1.00 23.67 C ANISOU 496 CD1 TRP A 69 3101 2923 2969 1034 350 322 C ATOM 497 CD2 TRP A 69 0.211 -54.035 574.562 1.00 24.38 C ANISOU 497 CD2 TRP A 69 3187 2876 3200 952 262 244 C ATOM 498 NE1 TRP A 69 0.525 -54.961 576.577 1.00 25.85 N ANISOU 498 NE1 TRP A 69 3392 3153 3277 1038 289 283 N ATOM 499 CE2 TRP A 69 1.127 -54.187 575.621 1.00 21.58 C ANISOU 499 CE2 TRP A 69 2845 2525 2829 986 234 236 C ATOM 500 CE3 TRP A 69 0.588 -53.280 573.449 1.00 43.15 C ANISOU 500 CE3 TRP A 69 5554 5179 5662 902 216 210 C ATOM 501 CZ2 TRP A 69 2.394 -53.610 575.601 1.00 23.91 C ANISOU 501 CZ2 TRP A 69 3136 2747 3200 968 158 197 C ATOM 502 CZ3 TRP A 69 1.850 -52.709 573.431 1.00 40.55 C ANISOU 502 CZ3 TRP A 69 5221 4780 5408 885 144 176 C ATOM 503 CH2 TRP A 69 2.736 -52.877 574.500 1.00 21.08 C ANISOU 503 CH2 TRP A 69 2761 2314 2935 915 115 171 C ATOM 504 N VAL A 70 -5.249 -54.268 573.712 1.00 31.44 N ANISOU 504 N VAL A 70 3986 3996 3965 1067 424 331 N ATOM 505 CA VAL A 70 -6.530 -54.581 573.086 1.00 31.26 C ANISOU 505 CA VAL A 70 3914 4023 3943 1064 463 377 C ATOM 506 C VAL A 70 -7.094 -53.358 572.382 1.00 18.42 C ANISOU 506 C VAL A 70 2273 2369 2358 1104 416 304 C ATOM 507 O VAL A 70 -7.745 -53.477 571.337 1.00 33.04 O ANISOU 507 O VAL A 70 4094 4214 4246 1066 426 332 O ATOM 508 CB VAL A 70 -7.520 -55.130 574.135 1.00 31.59 C ANISOU 508 CB VAL A 70 3904 4197 3902 1139 515 428 C ATOM 509 CG1 VAL A 70 -8.914 -55.273 573.537 1.00 27.69 C ANISOU 509 CG1 VAL A 70 3334 3770 3415 1149 544 465 C ATOM 510 CG2 VAL A 70 -7.041 -56.466 574.675 1.00 33.28 C ANISOU 510 CG2 VAL A 70 4126 4424 4094 1091 564 525 C ATOM 511 N LEU A 71 -6.870 -52.167 572.942 1.00 30.00 N ANISOU 511 N LEU A 71 3760 3814 3826 1186 361 211 N ATOM 512 CA LEU A 71 -7.413 -50.952 572.344 1.00 22.93 C ANISOU 512 CA LEU A 71 2852 2877 2982 1239 313 145 C ATOM 513 C LEU A 71 -6.816 -50.706 570.964 1.00 31.86 C ANISOU 513 C LEU A 71 3999 3899 4209 1142 274 152 C ATOM 514 O LEU A 71 -7.544 -50.538 569.978 1.00 28.61 O ANISOU 514 O LEU A 71 3556 3482 3831 1133 272 167 O ATOM 515 CB LEU A 71 -7.150 -49.761 573.267 1.00 31.77 C ANISOU 515 CB LEU A 71 4006 3973 4092 1346 262 47 C ATOM 516 CG LEU A 71 -8.119 -48.587 573.138 1.00 45.22 C ANISOU 516 CG LEU A 71 5692 5678 5812 1460 234 -20 C ATOM 517 CD1 LEU A 71 -9.469 -48.934 573.751 1.00 45.86 C ANISOU 517 CD1 LEU A 71 5706 5922 5797 1558 296 -9 C ATOM 518 CD2 LEU A 71 -7.536 -47.342 573.788 1.00 48.13 C ANISOU 518 CD2 LEU A 71 6124 5968 6194 1544 166 -119 C ATOM 519 N HIS A 72 -5.484 -50.699 570.870 1.00 21.35 N ANISOU 519 N HIS A 72 2706 2492 2915 1075 241 145 N ATOM 520 CA HIS A 72 -4.842 -50.497 569.576 1.00 28.04 C ANISOU 520 CA HIS A 72 3558 3258 3837 990 207 155 C ATOM 521 C HIS A 72 -5.173 -51.636 568.621 1.00 33.35 C ANISOU 521 C HIS A 72 4213 3972 4485 909 271 234 C ATOM 522 O HIS A 72 -5.339 -51.420 567.414 1.00 30.19 O ANISOU 522 O HIS A 72 3803 3543 4123 872 259 246 O ATOM 523 CB HIS A 72 -3.330 -50.364 569.758 1.00 29.81 C ANISOU 523 CB HIS A 72 3809 3416 4100 942 166 139 C ATOM 524 CG HIS A 72 -2.908 -49.073 570.390 1.00 33.36 C ANISOU 524 CG HIS A 72 4274 3787 4613 1004 94 70 C ATOM 525 ND1 HIS A 72 -2.393 -48.022 569.662 1.00 32.64 N ANISOU 525 ND1 HIS A 72 4182 3587 4635 984 27 55 N ATOM 526 CD2 HIS A 72 -2.926 -48.663 571.680 1.00 35.52 C ANISOU 526 CD2 HIS A 72 4572 4074 4849 1090 88 24 C ATOM 527 CE1 HIS A 72 -2.110 -47.021 570.476 1.00 33.74 C ANISOU 527 CE1 HIS A 72 4350 3664 4805 1050 -1 15 C ATOM 528 NE2 HIS A 72 -2.425 -47.384 571.707 1.00 37.87 N ANISOU 528 NE2 HIS A 72 4896 4266 5226 1120 26 -18 N ATOM 529 N LEU A 73 -5.278 -52.858 569.147 1.00 30.63 N ANISOU 529 N LEU A 73 3866 3688 4084 884 341 292 N ATOM 530 CA LEU A 73 -5.597 -54.004 568.304 1.00 26.04 C ANISOU 530 CA LEU A 73 3267 3127 3501 807 403 367 C ATOM 531 C LEU A 73 -6.978 -53.866 567.677 1.00 35.85 C ANISOU 531 C LEU A 73 4468 4405 4749 835 409 383 C ATOM 532 O LEU A 73 -7.194 -54.318 566.546 1.00 37.51 O ANISOU 532 O LEU A 73 4663 4603 4985 774 428 418 O ATOM 533 CB LEU A 73 -5.506 -55.289 569.126 1.00 21.91 C ANISOU 533 CB LEU A 73 2745 2644 2937 788 465 429 C ATOM 534 CG LEU A 73 -5.400 -56.605 568.358 1.00 27.64 C ANISOU 534 CG LEU A 73 3461 3356 3686 699 523 495 C ATOM 535 CD1 LEU A 73 -4.111 -56.670 567.554 1.00 35.06 C ANISOU 535 CD1 LEU A 73 4419 4242 4661 633 515 475 C ATOM 536 CD2 LEU A 73 -5.488 -57.767 569.335 1.00 27.88 C ANISOU 536 CD2 LEU A 73 3487 3418 3690 701 575 556 C ATOM 537 N ALA A 74 -7.925 -53.257 568.394 1.00 27.94 N ANISOU 537 N ALA A 74 3437 3456 3723 934 395 353 N ATOM 538 CA ALA A 74 -9.244 -52.999 567.833 1.00 22.25 C ANISOU 538 CA ALA A 74 2658 2782 3013 978 394 360 C ATOM 539 C ALA A 74 -9.272 -51.757 566.955 1.00 26.24 C ANISOU 539 C ALA A 74 3169 3224 3578 1005 326 303 C ATOM 540 O ALA A 74 -10.181 -51.620 566.129 1.00 34.41 O ANISOU 540 O ALA A 74 4160 4280 4635 1019 318 319 O ATOM 541 CB ALA A 74 -10.275 -52.856 568.953 1.00 31.17 C ANISOU 541 CB ALA A 74 3734 4018 4089 1086 415 350 C ATOM 542 N LEU A 75 -8.312 -50.845 567.121 1.00 26.35 N ANISOU 542 N LEU A 75 3227 3156 3627 1015 269 244 N ATOM 543 CA LEU A 75 -8.222 -49.703 566.218 1.00 32.84 C ANISOU 543 CA LEU A 75 4056 3896 4525 1031 195 207 C ATOM 544 C LEU A 75 -7.828 -50.152 564.816 1.00 26.75 C ANISOU 544 C LEU A 75 3294 3099 3769 933 201 256 C ATOM 545 O LEU A 75 -8.420 -49.715 563.823 1.00 26.33 O ANISOU 545 O LEU A 75 3222 3033 3750 947 170 265 O ATOM 546 CB LEU A 75 -7.221 -48.684 566.755 1.00 22.46 C ANISOU 546 CB LEU A 75 2781 2488 3265 1055 130 146 C ATOM 547 CG LEU A 75 -6.914 -47.536 565.792 1.00 29.60 C ANISOU 547 CG LEU A 75 3694 3280 4272 1053 45 130 C ATOM 548 CD1 LEU A 75 -8.178 -46.744 565.502 1.00 36.05 C ANISOU 548 CD1 LEU A 75 4474 4092 5131 1147 24 119 C ATOM 549 CD2 LEU A 75 -5.821 -46.642 566.353 1.00 43.00 C ANISOU 549 CD2 LEU A 75 5421 4872 6046 1057 -10 94 C ATOM 550 N SER A 76 -6.821 -51.022 564.717 1.00 20.04 N ANISOU 550 N SER A 76 2471 2249 2895 843 244 290 N ATOM 551 CA SER A 76 -6.441 -51.561 563.416 1.00 32.83 C ANISOU 551 CA SER A 76 4091 3860 4523 758 271 336 C ATOM 552 C SER A 76 -7.628 -52.245 562.750 1.00 35.03 C ANISOU 552 C SER A 76 4329 4189 4791 750 308 382 C ATOM 553 O SER A 76 -7.926 -51.997 561.576 1.00 35.83 O ANISOU 553 O SER A 76 4418 4279 4916 738 287 397 O ATOM 554 CB SER A 76 -5.276 -52.541 563.574 1.00 31.43 C ANISOU 554 CB SER A 76 3931 3685 4326 679 326 362 C ATOM 555 OG SER A 76 -5.676 -53.709 564.275 1.00 37.04 O ANISOU 555 OG SER A 76 4632 4443 4999 666 387 397 O ATOM 556 N ASP A 77 -8.330 -53.100 563.497 1.00 24.59 N ANISOU 556 N ASP A 77 2982 2926 3436 761 356 410 N ATOM 557 CA ASP A 77 -9.490 -53.783 562.939 1.00 33.03 C ANISOU 557 CA ASP A 77 3999 4043 4506 755 380 457 C ATOM 558 C ASP A 77 -10.554 -52.790 562.490 1.00 32.14 C ANISOU 558 C ASP A 77 3843 3953 4416 835 326 436 C ATOM 559 O ASP A 77 -11.293 -53.061 561.536 1.00 25.23 O ANISOU 559 O ASP A 77 2926 3103 3557 823 320 470 O ATOM 560 CB ASP A 77 -10.057 -54.767 563.964 1.00 23.16 C ANISOU 560 CB ASP A 77 2721 2855 3226 763 430 497 C ATOM 561 CG ASP A 77 -9.114 -55.931 564.236 1.00 32.15 C ANISOU 561 CG ASP A 77 3895 3961 4359 684 480 530 C ATOM 562 OD1 ASP A 77 -8.348 -56.298 563.318 1.00 31.38 O ANISOU 562 OD1 ASP A 77 3822 3816 4286 615 488 528 O ATOM 563 OD2 ASP A 77 -9.137 -56.476 565.361 1.00 32.83 O ANISOU 563 OD2 ASP A 77 3980 4076 4417 699 512 555 O ATOM 564 N LEU A 78 -10.641 -51.635 563.153 1.00 26.97 N ANISOU 564 N LEU A 78 3192 3285 3770 924 280 378 N ATOM 565 CA LEU A 78 -11.574 -50.605 562.708 1.00 29.93 C ANISOU 565 CA LEU A 78 3524 3663 4183 1012 222 353 C ATOM 566 C LEU A 78 -11.148 -50.015 561.368 1.00 30.74 C ANISOU 566 C LEU A 78 3657 3691 4331 979 165 359 C ATOM 567 O LEU A 78 -11.983 -49.822 560.477 1.00 33.07 O ANISOU 567 O LEU A 78 3910 4007 4648 1005 135 383 O ATOM 568 CB LEU A 78 -11.683 -49.506 563.764 1.00 39.58 C ANISOU 568 CB LEU A 78 4747 4867 5423 1121 185 283 C ATOM 569 CG LEU A 78 -12.747 -48.439 563.501 1.00 21.18 C ANISOU 569 CG LEU A 78 2362 2540 3145 1236 132 257 C ATOM 570 CD1 LEU A 78 -14.136 -48.978 563.819 1.00 31.90 C ANISOU 570 CD1 LEU A 78 3621 4042 4459 1295 183 286 C ATOM 571 CD2 LEU A 78 -12.455 -47.183 564.303 1.00 19.71 C ANISOU 571 CD2 LEU A 78 2205 2277 3008 1330 87 187 C ATOM 572 N LEU A 79 -9.854 -49.718 561.207 1.00 32.94 N ANISOU 572 N LEU A 79 4002 3892 4623 928 146 343 N ATOM 573 CA LEU A 79 -9.372 -49.184 559.936 1.00 23.51 C ANISOU 573 CA LEU A 79 2835 2638 3461 896 97 361 C ATOM 574 C LEU A 79 -9.605 -50.175 558.805 1.00 15.78 C ANISOU 574 C LEU A 79 1832 1705 2457 825 145 422 C ATOM 575 O LEU A 79 -10.005 -49.787 557.702 1.00 18.78 O ANISOU 575 O LEU A 79 2202 2075 2857 836 102 449 O ATOM 576 CB LEU A 79 -7.887 -48.836 560.038 1.00 25.47 C ANISOU 576 CB LEU A 79 3141 2817 3719 849 80 343 C ATOM 577 CG LEU A 79 -7.503 -47.800 561.094 1.00 33.19 C ANISOU 577 CG LEU A 79 4146 3724 4742 914 7 278 C ATOM 578 CD1 LEU A 79 -5.989 -47.670 561.170 1.00 37.44 C ANISOU 578 CD1 LEU A 79 4733 4210 5282 856 -7 273 C ATOM 579 CD2 LEU A 79 -8.145 -46.456 560.793 1.00 25.60 C ANISOU 579 CD2 LEU A 79 3180 2681 3865 1003 -101 255 C ATOM 580 N ALA A 80 -9.356 -51.461 559.058 1.00 25.06 N ANISOU 580 N ALA A 80 3003 2922 3598 756 224 445 N ATOM 581 CA ALA A 80 -9.671 -52.482 558.066 1.00 21.64 C ANISOU 581 CA ALA A 80 2545 2520 3157 699 257 490 C ATOM 582 C ALA A 80 -11.158 -52.469 557.739 1.00 30.66 C ANISOU 582 C ALA A 80 3622 3718 4308 752 226 514 C ATOM 583 O ALA A 80 -11.550 -52.495 556.566 1.00 29.03 O ANISOU 583 O ALA A 80 3396 3520 4113 744 193 544 O ATOM 584 CB ALA A 80 -9.244 -53.858 558.578 1.00 19.95 C ANISOU 584 CB ALA A 80 2338 2321 2922 634 330 502 C ATOM 585 N SER A 81 -12.003 -52.412 558.772 1.00 25.28 N ANISOU 585 N SER A 81 2898 3088 3621 813 233 504 N ATOM 586 CA SER A 81 -13.442 -52.334 558.548 1.00 33.86 C ANISOU 586 CA SER A 81 3894 4253 4717 873 204 527 C ATOM 587 C SER A 81 -13.819 -51.084 557.767 1.00 29.62 C ANISOU 587 C SER A 81 3348 3691 4214 943 121 516 C ATOM 588 O SER A 81 -14.864 -51.056 557.108 1.00 33.10 O ANISOU 588 O SER A 81 3715 4194 4668 976 84 548 O ATOM 589 CB SER A 81 -14.184 -52.356 559.886 1.00 27.78 C ANISOU 589 CB SER A 81 3068 3559 3929 941 232 513 C ATOM 590 OG SER A 81 -13.803 -53.474 560.668 1.00 41.20 O ANISOU 590 OG SER A 81 4782 5273 5598 881 299 535 O ATOM 591 N ALA A 82 -12.995 -50.036 557.838 1.00 28.62 N ANISOU 591 N ALA A 82 3290 3473 4110 968 80 477 N ATOM 592 CA ALA A 82 -13.300 -48.798 557.132 1.00 26.33 C ANISOU 592 CA ALA A 82 3004 3133 3868 1039 -15 474 C ATOM 593 C ALA A 82 -12.879 -48.849 555.668 1.00 37.63 C ANISOU 593 C ALA A 82 4469 4535 5294 978 -45 526 C ATOM 594 O ALA A 82 -13.476 -48.159 554.834 1.00 36.40 O ANISOU 594 O ALA A 82 4296 4370 5163 1029 -124 555 O ATOM 595 CB ALA A 82 -12.626 -47.617 557.831 1.00 27.71 C ANISOU 595 CB ALA A 82 3235 3205 4088 1093 -69 414 C ATOM 596 N SER A 83 -11.855 -49.638 555.335 1.00 33.71 N ANISOU 596 N SER A 83 4016 4026 4767 876 15 541 N ATOM 597 CA SER A 83 -11.498 -49.839 553.937 1.00 30.77 C ANISOU 597 CA SER A 83 3664 3646 4383 822 -1 592 C ATOM 598 C SER A 83 -12.392 -50.868 553.261 1.00 37.64 C ANISOU 598 C SER A 83 4473 4595 5232 798 7 632 C ATOM 599 O SER A 83 -12.534 -50.837 552.034 1.00 43.39 O ANISOU 599 O SER A 83 5204 5334 5949 785 -42 679 O ATOM 600 CB SER A 83 -10.035 -50.276 553.813 1.00 32.22 C ANISOU 600 CB SER A 83 3901 3792 4550 739 57 585 C ATOM 601 OG SER A 83 -9.874 -51.643 554.152 1.00 36.30 O ANISOU 601 OG SER A 83 4402 4347 5041 682 137 575 O ATOM 602 N LEU A 84 -13.001 -51.766 554.033 1.00 24.39 N ANISOU 602 N LEU A 84 2742 2976 3548 792 54 621 N ATOM 603 CA LEU A 84 -13.812 -52.822 553.436 1.00 37.53 C ANISOU 603 CA LEU A 84 4344 4713 5202 762 45 659 C ATOM 604 C LEU A 84 -14.957 -52.285 552.582 1.00 37.60 C ANISOU 604 C LEU A 84 4283 4787 5216 814 -45 702 C ATOM 605 O LEU A 84 -15.235 -52.889 551.531 1.00 35.84 O ANISOU 605 O LEU A 84 4022 4616 4980 781 -68 780 O ATOM 606 CB LEU A 84 -14.334 -53.752 554.538 1.00 26.90 C ANISOU 606 CB LEU A 84 2942 3421 3857 751 101 652 C ATOM 607 CG LEU A 84 -14.993 -55.049 554.060 1.00 32.30 C ANISOU 607 CG LEU A 84 3540 4180 4552 710 116 736 C ATOM 608 CD1 LEU A 84 -14.048 -55.859 553.176 1.00 29.73 C ANISOU 608 CD1 LEU A 84 3277 3788 4233 649 139 767 C ATOM 609 CD2 LEU A 84 -15.447 -55.882 555.249 1.00 50.27 C ANISOU 609 CD2 LEU A 84 5750 6510 6839 699 180 759 C ATOM 610 N PRO A 85 -15.658 -51.209 552.957 1.00 36.44 N ANISOU 610 N PRO A 85 4096 4656 5093 906 -88 694 N ATOM 611 CA PRO A 85 -16.712 -50.686 552.070 1.00 33.68 C ANISOU 611 CA PRO A 85 3677 4370 4750 958 -183 740 C ATOM 612 C PRO A 85 -16.253 -50.477 550.638 1.00 39.21 C ANISOU 612 C PRO A 85 4440 5036 5423 921 -247 791 C ATOM 613 O PRO A 85 -16.969 -50.848 549.700 1.00 41.11 O ANISOU 613 O PRO A 85 4600 5379 5641 909 -288 886 O ATOM 614 CB PRO A 85 -17.092 -49.356 552.735 1.00 26.28 C ANISOU 614 CB PRO A 85 2730 3398 3857 1077 -222 706 C ATOM 615 CG PRO A 85 -16.807 -49.563 554.173 1.00 26.53 C ANISOU 615 CG PRO A 85 2768 3419 3894 1087 -139 646 C ATOM 616 CD PRO A 85 -15.618 -50.491 554.242 1.00 38.80 C ANISOU 616 CD PRO A 85 4403 4926 5415 976 -63 639 C ATOM 617 N PHE A 86 -15.067 -49.899 550.440 1.00 49.76 N ANISOU 617 N PHE A 86 5884 6263 6758 903 -237 782 N ATOM 618 CA PHE A 86 -14.577 -49.675 549.085 1.00 31.27 C ANISOU 618 CA PHE A 86 3604 3899 4377 866 -290 842 C ATOM 619 C PHE A 86 -14.292 -50.987 548.370 1.00 32.99 C ANISOU 619 C PHE A 86 3802 4180 4552 783 -241 906 C ATOM 620 O PHE A 86 -14.386 -51.053 547.139 1.00 45.41 O ANISOU 620 O PHE A 86 5367 5809 6079 759 -288 1009 O ATOM 621 CB PHE A 86 -13.328 -48.799 549.125 1.00 26.48 C ANISOU 621 CB PHE A 86 3097 3181 3784 859 -278 834 C ATOM 622 CG PHE A 86 -13.565 -47.454 549.741 1.00 45.15 C ANISOU 622 CG PHE A 86 5477 5477 6200 955 -337 812 C ATOM 623 CD1 PHE A 86 -14.054 -46.407 548.979 1.00 48.65 C ANISOU 623 CD1 PHE A 86 5941 5895 6648 1021 -446 869 C ATOM 624 CD2 PHE A 86 -13.320 -47.241 551.086 1.00 53.86 C ANISOU 624 CD2 PHE A 86 6584 6537 7344 987 -296 735 C ATOM 625 CE1 PHE A 86 -14.283 -45.167 549.545 1.00 65.26 C ANISOU 625 CE1 PHE A 86 8076 7914 8805 1130 -521 840 C ATOM 626 CE2 PHE A 86 -13.547 -46.004 551.658 1.00 70.23 C ANISOU 626 CE2 PHE A 86 8682 8534 9469 1089 -372 702 C ATOM 627 CZ PHE A 86 -14.029 -44.966 550.886 1.00 62.84 C ANISOU 627 CZ PHE A 86 7773 7556 8547 1166 -489 750 C ATOM 628 N PHE A 87 -13.950 -52.037 549.119 1.00 40.55 N ANISOU 628 N PHE A 87 4751 5136 5522 744 -152 865 N ATOM 629 CA PHE A 87 -13.740 -53.341 548.503 1.00 40.27 C ANISOU 629 CA PHE A 87 4693 5147 5460 686 -114 939 C ATOM 630 C PHE A 87 -15.055 -53.966 548.058 1.00 45.96 C ANISOU 630 C PHE A 87 5278 6016 6169 677 -176 1044 C ATOM 631 O PHE A 87 -15.068 -54.783 547.130 1.00 44.75 O ANISOU 631 O PHE A 87 5107 5934 5963 619 -218 1138 O ATOM 632 CB PHE A 87 -13.006 -54.263 549.477 1.00 46.24 C ANISOU 632 CB PHE A 87 5487 5840 6243 655 -15 865 C ATOM 633 CG PHE A 87 -12.793 -55.654 548.954 1.00 39.89 C ANISOU 633 CG PHE A 87 4681 5046 5429 614 15 933 C ATOM 634 CD1 PHE A 87 -12.153 -55.862 547.746 1.00 39.61 C ANISOU 634 CD1 PHE A 87 4713 5005 5331 594 -1 992 C ATOM 635 CD2 PHE A 87 -13.222 -56.753 549.677 1.00 50.43 C ANISOU 635 CD2 PHE A 87 5961 6389 6811 596 52 948 C ATOM 636 CE1 PHE A 87 -11.953 -57.140 547.264 1.00 34.69 C ANISOU 636 CE1 PHE A 87 4144 4375 4663 530 19 1003 C ATOM 637 CE2 PHE A 87 -13.022 -58.035 549.201 1.00 41.76 C ANISOU 637 CE2 PHE A 87 4908 5260 5698 525 61 976 C ATOM 638 CZ PHE A 87 -12.386 -58.228 547.994 1.00 22.16 C ANISOU 638 CZ PHE A 87 2538 2765 3115 463 48 940 C ATOM 639 N THR A 88 -16.167 -53.600 548.703 1.00 39.60 N ANISOU 639 N THR A 88 4373 5280 5394 722 -199 1031 N ATOM 640 CA THR A 88 -17.466 -54.108 548.272 1.00 44.68 C ANISOU 640 CA THR A 88 4856 6101 6018 693 -274 1128 C ATOM 641 C THR A 88 -17.914 -53.428 546.985 1.00 32.04 C ANISOU 641 C THR A 88 3241 4573 4358 695 -390 1199 C ATOM 642 O THR A 88 -18.446 -54.084 546.081 1.00 41.12 O ANISOU 642 O THR A 88 4312 5869 5442 607 -479 1292 O ATOM 643 CB THR A 88 -18.509 -53.904 549.370 1.00 34.07 C ANISOU 643 CB THR A 88 3403 4828 4715 746 -252 1090 C ATOM 644 OG1 THR A 88 -18.904 -52.529 549.410 1.00 70.18 O ANISOU 644 OG1 THR A 88 8000 9368 9299 849 -298 1040 O ATOM 645 CG2 THR A 88 -17.942 -54.292 550.723 1.00 37.41 C ANISOU 645 CG2 THR A 88 3877 5163 5175 753 -139 1007 C ATOM 646 N TYR A 89 -17.695 -52.115 546.879 1.00 29.81 N ANISOU 646 N TYR A 89 3041 4195 4089 775 -411 1157 N ATOM 647 CA TYR A 89 -18.014 -51.407 545.644 1.00 45.33 C ANISOU 647 CA TYR A 89 5013 6209 6001 781 -520 1234 C ATOM 648 C TYR A 89 -17.254 -52.004 544.468 1.00 36.73 C ANISOU 648 C TYR A 89 3989 5152 4817 680 -543 1312 C ATOM 649 O TYR A 89 -17.808 -52.157 543.373 1.00 38.22 O ANISOU 649 O TYR A 89 4132 5477 4913 621 -646 1401 O ATOM 650 CB TYR A 89 -17.685 -49.923 545.804 1.00 44.58 C ANISOU 650 CB TYR A 89 5020 5971 5947 876 -545 1178 C ATOM 651 CG TYR A 89 -17.989 -49.070 544.592 1.00 37.18 C ANISOU 651 CG TYR A 89 4103 5060 4962 895 -659 1266 C ATOM 652 CD1 TYR A 89 -19.288 -48.673 544.305 1.00 33.43 C ANISOU 652 CD1 TYR A 89 3521 4690 4490 954 -756 1309 C ATOM 653 CD2 TYR A 89 -16.973 -48.644 543.745 1.00 57.05 C ANISOU 653 CD2 TYR A 89 6742 7506 7429 854 -671 1312 C ATOM 654 CE1 TYR A 89 -19.569 -47.886 543.202 1.00 37.25 C ANISOU 654 CE1 TYR A 89 4030 5196 4928 975 -867 1394 C ATOM 655 CE2 TYR A 89 -17.246 -47.856 542.640 1.00 45.66 C ANISOU 655 CE2 TYR A 89 5324 6091 5933 865 -775 1406 C ATOM 656 CZ TYR A 89 -18.545 -47.480 542.375 1.00 31.14 C ANISOU 656 CZ TYR A 89 3389 4346 4099 929 -876 1446 C ATOM 657 OH TYR A 89 -18.822 -46.697 541.278 1.00 48.31 O ANISOU 657 OH TYR A 89 5591 6546 6218 944 -985 1544 O ATOM 658 N PHE A 90 -15.982 -52.352 544.681 1.00 43.59 N ANISOU 658 N PHE A 90 4966 5909 5687 655 -454 1272 N ATOM 659 CA PHE A 90 -15.198 -53.010 543.642 1.00 36.65 C ANISOU 659 CA PHE A 90 4160 5068 4695 570 -463 1336 C ATOM 660 C PHE A 90 -15.876 -54.281 543.147 1.00 29.97 C ANISOU 660 C PHE A 90 3238 4394 3754 467 -540 1401 C ATOM 661 O PHE A 90 -15.742 -54.639 541.972 1.00 52.76 O ANISOU 661 O PHE A 90 6189 7370 6486 360 -595 1416 O ATOM 662 CB PHE A 90 -13.800 -53.321 544.183 1.00 45.10 C ANISOU 662 CB PHE A 90 5340 5997 5799 574 -337 1266 C ATOM 663 CG PHE A 90 -12.963 -54.164 543.266 1.00 32.10 C ANISOU 663 CG PHE A 90 3780 4395 4021 503 -318 1319 C ATOM 664 CD1 PHE A 90 -12.189 -53.578 542.278 1.00 42.37 C ANISOU 664 CD1 PHE A 90 5165 5708 5224 477 -321 1361 C ATOM 665 CD2 PHE A 90 -12.942 -55.543 543.399 1.00 31.57 C ANISOU 665 CD2 PHE A 90 3746 4332 3916 413 -268 1212 C ATOM 666 CE1 PHE A 90 -11.414 -54.352 541.433 1.00 42.69 C ANISOU 666 CE1 PHE A 90 5301 5810 5108 399 -274 1344 C ATOM 667 CE2 PHE A 90 -12.170 -56.326 542.558 1.00 43.96 C ANISOU 667 CE2 PHE A 90 5440 5911 5351 320 -219 1121 C ATOM 668 CZ PHE A 90 -11.403 -55.730 541.574 1.00 45.82 C ANISOU 668 CZ PHE A 90 5743 6196 5471 321 -215 1180 C ATOM 669 N LEU A 91 -16.601 -54.976 544.025 1.00 38.69 N ANISOU 669 N LEU A 91 4236 5534 4932 452 -529 1370 N ATOM 670 CA LEU A 91 -17.301 -56.192 543.625 1.00 46.31 C ANISOU 670 CA LEU A 91 5178 6603 5817 270 -574 1301 C ATOM 671 C LEU A 91 -18.639 -55.880 542.962 1.00 44.53 C ANISOU 671 C LEU A 91 4801 6582 5537 235 -730 1393 C ATOM 672 O LEU A 91 -19.033 -56.557 542.005 1.00 36.04 O ANISOU 672 O LEU A 91 3749 5611 4333 72 -815 1363 O ATOM 673 CB LEU A 91 -17.505 -57.091 544.844 1.00 36.33 C ANISOU 673 CB LEU A 91 3869 5283 4653 234 -491 1227 C ATOM 674 CG LEU A 91 -16.215 -57.568 545.513 1.00 37.99 C ANISOU 674 CG LEU A 91 4225 5297 4912 258 -348 1132 C ATOM 675 CD1 LEU A 91 -16.507 -58.113 546.898 1.00 44.93 C ANISOU 675 CD1 LEU A 91 5031 6134 5906 266 -276 1107 C ATOM 676 CD2 LEU A 91 -15.526 -58.620 544.650 1.00 45.84 C ANISOU 676 CD2 LEU A 91 5389 6235 5792 118 -331 1019 C ATOM 677 N ALA A 92 -19.350 -54.864 543.459 1.00 46.14 N ANISOU 677 N ALA A 92 4874 6821 5834 379 -752 1460 N ATOM 678 CA ALA A 92 -20.640 -54.507 542.877 1.00 40.59 C ANISOU 678 CA ALA A 92 4049 6280 5095 356 -864 1503 C ATOM 679 C ALA A 92 -20.482 -54.020 541.444 1.00 44.71 C ANISOU 679 C ALA A 92 4653 6847 5486 320 -963 1556 C ATOM 680 O ALA A 92 -21.305 -54.336 540.577 1.00 39.85 O ANISOU 680 O ALA A 92 3970 6404 4768 210 -1088 1594 O ATOM 681 CB ALA A 92 -21.320 -53.439 543.732 1.00 40.04 C ANISOU 681 CB ALA A 92 3911 6159 5144 521 -812 1468 C ATOM 682 N VAL A 93 -19.432 -53.242 541.177 1.00 51.68 N ANISOU 682 N VAL A 93 5686 7585 6367 397 -907 1556 N ATOM 683 CA VAL A 93 -19.174 -52.773 539.820 1.00 35.83 C ANISOU 683 CA VAL A 93 3765 5623 4224 355 -985 1617 C ATOM 684 C VAL A 93 -18.925 -53.945 538.882 1.00 43.90 C ANISOU 684 C VAL A 93 4840 6790 5049 174 -1052 1621 C ATOM 685 O VAL A 93 -19.170 -53.846 537.674 1.00 68.11 O ANISOU 685 O VAL A 93 7938 9978 7964 96 -1149 1658 O ATOM 686 CB VAL A 93 -17.985 -51.791 539.825 1.00 46.62 C ANISOU 686 CB VAL A 93 5277 6805 5631 443 -900 1614 C ATOM 687 CG1 VAL A 93 -17.511 -51.513 538.406 1.00 63.32 C ANISOU 687 CG1 VAL A 93 7490 8986 7583 372 -958 1685 C ATOM 688 CG2 VAL A 93 -18.370 -50.497 540.530 1.00 36.03 C ANISOU 688 CG2 VAL A 93 3916 5336 4439 595 -888 1589 C ATOM 689 N GLY A 94 -18.438 -55.063 539.411 1.00 53.45 N ANISOU 689 N GLY A 94 6098 7955 6256 95 -979 1527 N ATOM 690 CA GLY A 94 -18.091 -56.204 538.590 1.00 43.59 C ANISOU 690 CA GLY A 94 4984 6736 4844 -84 -973 1393 C ATOM 691 C GLY A 94 -16.595 -56.430 538.571 1.00 45.37 C ANISOU 691 C GLY A 94 5391 6813 5036 -62 -822 1304 C ATOM 692 O GLY A 94 -16.023 -56.788 537.538 1.00 49.86 O ANISOU 692 O GLY A 94 6088 7432 5425 -141 -819 1244 O ATOM 693 N HIS A 95 -15.951 -56.208 539.717 1.00 36.72 N ANISOU 693 N HIS A 95 4297 5551 4103 53 -698 1292 N ATOM 694 CA HIS A 95 -14.514 -56.410 539.857 1.00 43.02 C ANISOU 694 CA HIS A 95 5239 6213 4895 86 -551 1215 C ATOM 695 C HIS A 95 -13.739 -55.428 538.989 1.00 49.71 C ANISOU 695 C HIS A 95 6147 7101 5641 132 -551 1323 C ATOM 696 O HIS A 95 -13.045 -55.827 538.047 1.00 41.08 O ANISOU 696 O HIS A 95 5166 6067 4377 63 -516 1265 O ATOM 697 CB HIS A 95 -14.141 -57.851 539.507 1.00 44.16 C ANISOU 697 CB HIS A 95 5508 6332 4937 -40 -501 1028 C ATOM 698 CG HIS A 95 -14.846 -58.871 540.343 1.00 46.24 C ANISOU 698 CG HIS A 95 5730 6536 5302 -114 -508 937 C ATOM 699 ND1 HIS A 95 -14.204 -59.611 541.312 1.00 39.04 N ANISOU 699 ND1 HIS A 95 4880 5455 4499 -92 -390 836 N ATOM 700 CD2 HIS A 95 -16.142 -59.266 540.364 1.00 54.48 C ANISOU 700 CD2 HIS A 95 6667 7676 6355 -219 -626 951 C ATOM 701 CE1 HIS A 95 -15.072 -60.423 541.889 1.00 64.86 C ANISOU 701 CE1 HIS A 95 8094 8712 7839 -188 -433 798 C ATOM 702 NE2 HIS A 95 -16.255 -60.233 541.333 1.00 56.29 N ANISOU 702 NE2 HIS A 95 6900 7791 6696 -272 -573 865 N ATOM 703 N SER A 96 -13.855 -54.141 539.303 1.00 51.04 N ANISOU 703 N SER A 96 6244 7240 5911 249 -593 1483 N ATOM 704 CA SER A 96 -13.125 -53.099 538.598 1.00 38.82 C ANISOU 704 CA SER A 96 4756 5683 4310 277 -588 1578 C ATOM 705 C SER A 96 -12.944 -51.918 539.537 1.00 35.71 C ANISOU 705 C SER A 96 4339 5094 4135 390 -545 1557 C ATOM 706 O SER A 96 -13.869 -51.549 540.266 1.00 39.80 O ANISOU 706 O SER A 96 4772 5569 4781 457 -585 1531 O ATOM 707 CB SER A 96 -13.862 -52.659 537.331 1.00 39.29 C ANISOU 707 CB SER A 96 4799 5896 4232 215 -718 1650 C ATOM 708 OG SER A 96 -13.237 -51.527 536.757 1.00 46.94 O ANISOU 708 OG SER A 96 5824 6811 5199 238 -703 1713 O ATOM 709 N TRP A 97 -11.750 -51.335 539.520 1.00 28.27 N ANISOU 709 N TRP A 97 3477 4052 3213 399 -467 1552 N ATOM 710 CA TRP A 97 -11.443 -50.180 540.354 1.00 23.70 C ANISOU 710 CA TRP A 97 2908 3298 2800 472 -447 1510 C ATOM 711 C TRP A 97 -11.732 -48.912 539.558 1.00 37.77 C ANISOU 711 C TRP A 97 4711 5082 4559 477 -542 1599 C ATOM 712 O TRP A 97 -10.983 -48.560 538.640 1.00 35.63 O ANISOU 712 O TRP A 97 4499 4848 4192 417 -538 1676 O ATOM 713 CB TRP A 97 -9.993 -50.219 540.821 1.00 25.47 C ANISOU 713 CB TRP A 97 3194 3423 3060 461 -331 1457 C ATOM 714 CG TRP A 97 -9.707 -49.149 541.804 1.00 20.57 C ANISOU 714 CG TRP A 97 2591 2642 2583 513 -330 1386 C ATOM 715 CD1 TRP A 97 -9.108 -47.951 541.561 1.00 27.13 C ANISOU 715 CD1 TRP A 97 3478 3402 3429 504 -361 1425 C ATOM 716 CD2 TRP A 97 -10.036 -49.161 543.196 1.00 29.29 C ANISOU 716 CD2 TRP A 97 3669 3652 3809 573 -308 1259 C ATOM 717 NE1 TRP A 97 -9.034 -47.216 542.718 1.00 35.76 N ANISOU 717 NE1 TRP A 97 4594 4359 4634 560 -368 1325 N ATOM 718 CE2 TRP A 97 -9.598 -47.938 543.737 1.00 36.65 C ANISOU 718 CE2 TRP A 97 4656 4464 4803 600 -335 1215 C ATOM 719 CE3 TRP A 97 -10.656 -50.089 544.039 1.00 24.24 C ANISOU 719 CE3 TRP A 97 2969 3028 3212 600 -271 1184 C ATOM 720 CZ2 TRP A 97 -9.757 -47.619 545.083 1.00 43.86 C ANISOU 720 CZ2 TRP A 97 5570 5292 5802 654 -330 1093 C ATOM 721 CZ3 TRP A 97 -10.814 -49.772 545.372 1.00 20.95 C ANISOU 721 CZ3 TRP A 97 2546 2527 2888 646 -255 1064 C ATOM 722 CH2 TRP A 97 -10.366 -48.548 545.882 1.00 41.06 C ANISOU 722 CH2 TRP A 97 5155 4970 5475 672 -290 1012 C ATOM 723 N GLU A 98 -12.814 -48.219 539.917 1.00 30.59 N ANISOU 723 N GLU A 98 3754 4135 3732 554 -625 1590 N ATOM 724 CA GLU A 98 -13.285 -47.055 539.177 1.00 31.43 C ANISOU 724 CA GLU A 98 3883 4240 3821 581 -730 1680 C ATOM 725 C GLU A 98 -13.057 -45.750 539.933 1.00 44.82 C ANISOU 725 C GLU A 98 5640 5753 5635 670 -744 1635 C ATOM 726 O GLU A 98 -13.666 -44.729 539.597 1.00 39.17 O ANISOU 726 O GLU A 98 4943 5008 4931 735 -841 1691 O ATOM 727 CB GLU A 98 -14.770 -47.214 538.847 1.00 47.16 C ANISOU 727 CB GLU A 98 5778 6353 5789 613 -835 1715 C ATOM 728 CG GLU A 98 -15.127 -48.522 538.156 1.00 50.19 C ANISOU 728 CG GLU A 98 6103 6932 6035 514 -849 1744 C ATOM 729 CD GLU A 98 -14.610 -48.601 536.730 1.00 53.84 C ANISOU 729 CD GLU A 98 6630 7516 6311 408 -877 1840 C ATOM 730 OE1 GLU A 98 -14.051 -47.598 536.236 1.00 50.86 O ANISOU 730 OE1 GLU A 98 6322 7075 5925 412 -887 1909 O ATOM 731 OE2 GLU A 98 -14.770 -49.668 536.099 1.00 54.59 O ANISOU 731 OE2 GLU A 98 6711 7779 6251 313 -894 1840 O ATOM 732 N LEU A 99 -12.188 -45.759 540.945 1.00 29.81 N ANISOU 732 N LEU A 99 3782 3736 3810 678 -658 1532 N ATOM 733 CA LEU A 99 -12.002 -44.586 541.789 1.00 27.22 C ANISOU 733 CA LEU A 99 3525 3249 3569 761 -682 1465 C ATOM 734 C LEU A 99 -10.586 -44.036 541.680 1.00 38.77 C ANISOU 734 C LEU A 99 5076 4629 5025 699 -637 1493 C ATOM 735 O LEU A 99 -9.897 -43.868 542.692 1.00 47.15 O ANISOU 735 O LEU A 99 6147 5603 6165 706 -584 1423 O ATOM 736 CB LEU A 99 -12.325 -44.930 543.244 1.00 44.77 C ANISOU 736 CB LEU A 99 5708 5422 5879 825 -641 1316 C ATOM 737 CG LEU A 99 -13.732 -45.479 543.481 1.00 38.50 C ANISOU 737 CG LEU A 99 4812 4718 5099 883 -678 1283 C ATOM 738 CD1 LEU A 99 -13.913 -45.844 544.939 1.00 34.62 C ANISOU 738 CD1 LEU A 99 4271 4193 4690 925 -618 1156 C ATOM 739 CD2 LEU A 99 -14.791 -44.477 543.041 1.00 43.29 C ANISOU 739 CD2 LEU A 99 5411 5328 5709 984 -803 1340 C ATOM 740 N GLY A 100 -10.145 -43.747 540.460 1.00 49.98 N ANISOU 740 N GLY A 100 6519 6103 6367 624 -658 1637 N ATOM 741 CA GLY A 100 -8.845 -43.140 540.257 1.00 53.34 C ANISOU 741 CA GLY A 100 7008 6469 6788 555 -623 1692 C ATOM 742 C GLY A 100 -7.700 -43.997 540.752 1.00 39.80 C ANISOU 742 C GLY A 100 5276 4767 5079 487 -507 1621 C ATOM 743 O GLY A 100 -7.914 -45.062 541.338 1.00 35.46 O ANISOU 743 O GLY A 100 4675 4254 4543 500 -452 1522 O ATOM 744 N THR A 101 -6.472 -43.532 540.525 1.00 57.44 N ANISOU 744 N THR A 101 7543 6976 7306 413 -472 1682 N ATOM 745 CA THR A 101 -5.283 -44.292 540.886 1.00 47.68 C ANISOU 745 CA THR A 101 6280 5769 6069 352 -365 1634 C ATOM 746 C THR A 101 -4.826 -44.014 542.312 1.00 37.69 C ANISOU 746 C THR A 101 5017 4380 4923 392 -344 1519 C ATOM 747 O THR A 101 -4.415 -44.939 543.021 1.00 41.63 O ANISOU 747 O THR A 101 5478 4896 5442 392 -267 1417 O ATOM 748 CB THR A 101 -4.141 -43.972 539.917 1.00 50.88 C ANISOU 748 CB THR A 101 6686 6245 6401 245 -335 1775 C ATOM 749 OG1 THR A 101 -4.583 -44.172 538.568 1.00 59.38 O ANISOU 749 OG1 THR A 101 7752 7465 7345 200 -360 1895 O ATOM 750 CG2 THR A 101 -2.935 -44.862 540.195 1.00 31.53 C ANISOU 750 CG2 THR A 101 4189 3855 3934 197 -217 1733 C ATOM 751 N THR A 102 -4.891 -42.754 542.749 1.00 43.87 N ANISOU 751 N THR A 102 5832 5046 5790 426 -412 1554 N ATOM 752 CA THR A 102 -4.342 -42.398 544.053 1.00 33.66 C ANISOU 752 CA THR A 102 4539 3651 4600 451 -396 1472 C ATOM 753 C THR A 102 -5.087 -43.090 545.186 1.00 37.31 C ANISOU 753 C THR A 102 4966 4108 5103 533 -372 1320 C ATOM 754 O THR A 102 -4.490 -43.392 546.226 1.00 42.43 O ANISOU 754 O THR A 102 5593 4731 5798 531 -321 1231 O ATOM 755 CB THR A 102 -4.375 -40.880 544.237 1.00 54.76 C ANISOU 755 CB THR A 102 7272 6190 7343 480 -485 1543 C ATOM 756 OG1 THR A 102 -3.637 -40.254 543.179 1.00 80.43 O ANISOU 756 OG1 THR A 102 10544 9452 10562 380 -509 1702 O ATOM 757 CG2 THR A 102 -3.763 -40.486 545.572 1.00 59.56 C ANISOU 757 CG2 THR A 102 7892 6695 8041 501 -474 1460 C ATOM 758 N PHE A 103 -6.386 -43.348 545.013 1.00 44.97 N ANISOU 758 N PHE A 103 5922 5113 6050 599 -409 1298 N ATOM 759 CA PHE A 103 -7.142 -44.046 546.048 1.00 41.22 C ANISOU 759 CA PHE A 103 5399 4654 5610 662 -383 1170 C ATOM 760 C PHE A 103 -6.833 -45.537 546.065 1.00 49.87 C ANISOU 760 C PHE A 103 6436 5843 6670 605 -288 1113 C ATOM 761 O PHE A 103 -6.921 -46.172 547.123 1.00 52.21 O ANISOU 761 O PHE A 103 6690 6143 7003 624 -235 1012 O ATOM 762 CB PHE A 103 -8.643 -43.822 545.850 1.00 36.31 C ANISOU 762 CB PHE A 103 4764 4050 4980 752 -459 1176 C ATOM 763 CG PHE A 103 -9.439 -43.895 547.124 1.00 52.15 C ANISOU 763 CG PHE A 103 6736 6036 7041 842 -462 1063 C ATOM 764 CD1 PHE A 103 -9.473 -42.818 547.995 1.00 66.20 C ANISOU 764 CD1 PHE A 103 8571 7712 8870 933 -509 1026 C ATOM 765 CD2 PHE A 103 -10.155 -45.037 547.449 1.00 62.63 C ANISOU 765 CD2 PHE A 103 7981 7453 8363 840 -418 1000 C ATOM 766 CE1 PHE A 103 -10.203 -42.878 549.169 1.00 77.97 C ANISOU 766 CE1 PHE A 103 10032 9198 10395 1024 -518 920 C ATOM 767 CE2 PHE A 103 -10.888 -45.105 548.623 1.00 66.67 C ANISOU 767 CE2 PHE A 103 8450 7962 8921 913 -416 909 C ATOM 768 CZ PHE A 103 -10.912 -44.024 549.484 1.00 69.73 C ANISOU 768 CZ PHE A 103 8886 8254 9353 1004 -471 865 C ATOM 769 N CYS A 104 -6.468 -46.109 544.914 1.00 53.94 N ANISOU 769 N CYS A 104 6957 6434 7102 541 -264 1181 N ATOM 770 CA CYS A 104 -6.050 -47.506 544.876 1.00 37.65 C ANISOU 770 CA CYS A 104 4865 4444 4998 502 -176 1128 C ATOM 771 C CYS A 104 -4.838 -47.756 545.759 1.00 37.14 C ANISOU 771 C CYS A 104 4779 4349 4984 481 -94 1068 C ATOM 772 O CYS A 104 -4.628 -48.891 546.203 1.00 52.65 O ANISOU 772 O CYS A 104 6711 6347 6946 481 -18 993 O ATOM 773 CB CYS A 104 -5.748 -47.921 543.433 1.00 33.60 C ANISOU 773 CB CYS A 104 4355 4032 4378 447 -157 1252 C ATOM 774 SG CYS A 104 -4.674 -49.367 543.269 1.00 27.88 S ANISOU 774 SG CYS A 104 3598 3394 3600 417 -17 1244 S ATOM 775 N LYS A 105 -4.043 -46.722 546.034 1.00 31.81 N ANISOU 775 N LYS A 105 4122 3609 4354 466 -115 1103 N ATOM 776 CA LYS A 105 -2.894 -46.878 546.917 1.00 39.35 C ANISOU 776 CA LYS A 105 5051 4543 5358 447 -52 1052 C ATOM 777 C LYS A 105 -3.308 -46.796 548.382 1.00 35.27 C ANISOU 777 C LYS A 105 4517 3974 4910 497 -53 947 C ATOM 778 O LYS A 105 -2.981 -47.685 549.177 1.00 40.01 O ANISOU 778 O LYS A 105 5077 4605 5521 496 24 868 O ATOM 779 CB LYS A 105 -1.848 -45.813 546.592 1.00 37.10 C ANISOU 779 CB LYS A 105 4795 4213 5087 397 -84 1146 C ATOM 780 CG LYS A 105 -1.351 -45.856 545.156 1.00 29.99 C ANISOU 780 CG LYS A 105 3911 3387 4097 332 -73 1266 C ATOM 781 CD LYS A 105 -0.413 -44.694 544.863 1.00 35.58 C ANISOU 781 CD LYS A 105 4640 4053 4825 268 -110 1379 C ATOM 782 CE LYS A 105 0.225 -44.820 543.490 1.00 47.18 C ANISOU 782 CE LYS A 105 6113 5631 6184 187 -77 1502 C ATOM 783 NZ LYS A 105 1.129 -46.000 543.410 1.00 53.17 N ANISOU 783 NZ LYS A 105 6793 6506 6905 173 42 1492 N ATOM 784 N LEU A 106 -4.032 -45.739 548.756 1.00 29.93 N ANISOU 784 N LEU A 106 3882 3223 4268 546 -138 948 N ATOM 785 CA LEU A 106 -4.443 -45.572 550.148 1.00 38.00 C ANISOU 785 CA LEU A 106 4903 4202 5331 602 -147 852 C ATOM 786 C LEU A 106 -5.294 -46.745 550.615 1.00 28.24 C ANISOU 786 C LEU A 106 3610 3041 4079 620 -88 780 C ATOM 787 O LEU A 106 -5.028 -47.346 551.662 1.00 37.96 O ANISOU 787 O LEU A 106 4814 4290 5319 614 -28 709 O ATOM 788 CB LEU A 106 -5.215 -44.264 550.307 1.00 42.36 C ANISOU 788 CB LEU A 106 5524 4664 5906 684 -252 868 C ATOM 789 CG LEU A 106 -4.442 -42.983 550.005 1.00 50.28 C ANISOU 789 CG LEU A 106 6603 5569 6933 673 -309 948 C ATOM 790 CD1 LEU A 106 -5.393 -41.897 549.534 1.00 71.24 C ANISOU 790 CD1 LEU A 106 9320 8158 9588 757 -398 1007 C ATOM 791 CD2 LEU A 106 -3.680 -42.528 551.238 1.00 60.76 C ANISOU 791 CD2 LEU A 106 7963 6824 8299 686 -308 889 C ATOM 792 N HIS A 107 -6.329 -47.084 549.844 1.00 29.52 N ANISOU 792 N HIS A 107 3756 3249 4211 638 -108 810 N ATOM 793 CA HIS A 107 -7.218 -48.175 550.223 1.00 22.64 C ANISOU 793 CA HIS A 107 2832 2444 3324 650 -61 759 C ATOM 794 C HIS A 107 -6.433 -49.455 550.478 1.00 25.46 C ANISOU 794 C HIS A 107 3167 2847 3661 595 44 720 C ATOM 795 O HIS A 107 -6.648 -50.144 551.482 1.00 38.10 O ANISOU 795 O HIS A 107 4744 4468 5266 596 96 660 O ATOM 796 CB HIS A 107 -8.262 -48.388 549.125 1.00 37.48 C ANISOU 796 CB HIS A 107 4699 4372 5168 664 -110 815 C ATOM 797 CG HIS A 107 -8.996 -49.687 549.231 1.00 37.58 C ANISOU 797 CG HIS A 107 4664 4456 5158 656 -66 783 C ATOM 798 ND1 HIS A 107 -9.796 -50.005 550.307 1.00 46.08 N ANISOU 798 ND1 HIS A 107 5696 5553 6261 690 -46 730 N ATOM 799 CD2 HIS A 107 -9.051 -50.749 548.393 1.00 47.29 C ANISOU 799 CD2 HIS A 107 5895 5737 6338 618 -50 803 C ATOM 800 CE1 HIS A 107 -10.312 -51.208 550.128 1.00 48.55 C ANISOU 800 CE1 HIS A 107 5976 5921 6548 666 -18 726 C ATOM 801 NE2 HIS A 107 -9.876 -51.680 548.974 1.00 59.34 N ANISOU 801 NE2 HIS A 107 7377 7300 7871 627 -28 764 N ATOM 802 N SER A 108 -5.504 -49.781 549.579 1.00 28.97 N ANISOU 802 N SER A 108 3625 3308 4076 553 73 758 N ATOM 803 CA SER A 108 -4.723 -51.004 549.728 1.00 20.69 C ANISOU 803 CA SER A 108 2564 2293 3005 524 167 718 C ATOM 804 C SER A 108 -3.784 -50.916 550.925 1.00 22.85 C ANISOU 804 C SER A 108 2825 2546 3311 512 217 671 C ATOM 805 O SER A 108 -3.680 -51.863 551.714 1.00 30.71 O ANISOU 805 O SER A 108 3809 3561 4298 504 280 618 O ATOM 806 CB SER A 108 -3.935 -51.275 548.448 1.00 27.16 C ANISOU 806 CB SER A 108 3407 3137 3776 502 180 774 C ATOM 807 OG SER A 108 -4.793 -51.322 547.321 1.00 41.80 O ANISOU 807 OG SER A 108 5288 5017 5577 502 118 831 O ATOM 808 N SER A 109 -3.087 -49.786 551.073 1.00 30.84 N ANISOU 808 N SER A 109 3848 3512 4358 508 176 698 N ATOM 809 CA SER A 109 -2.161 -49.626 552.191 1.00 33.37 C ANISOU 809 CA SER A 109 4161 3809 4708 497 203 661 C ATOM 810 C SER A 109 -2.858 -49.870 553.522 1.00 24.15 C ANISOU 810 C SER A 109 2992 2640 3544 518 208 594 C ATOM 811 O SER A 109 -2.262 -50.426 554.454 1.00 21.26 O ANISOU 811 O SER A 109 2616 2288 3173 502 258 557 O ATOM 812 CB SER A 109 -1.546 -48.226 552.167 1.00 17.28 C ANISOU 812 CB SER A 109 2152 1700 2714 494 124 704 C ATOM 813 OG SER A 109 -0.866 -47.990 550.948 1.00 31.44 O ANISOU 813 OG SER A 109 3946 3502 4497 463 120 789 O ATOM 814 N ILE A 110 -4.124 -49.464 553.628 1.00 20.77 N ANISOU 814 N ILE A 110 2574 2198 3118 560 153 587 N ATOM 815 CA ILE A 110 -4.871 -49.675 554.864 1.00 25.67 C ANISOU 815 CA ILE A 110 3190 2828 3737 591 157 535 C ATOM 816 C ILE A 110 -4.939 -51.159 555.194 1.00 16.56 C ANISOU 816 C ILE A 110 2011 1734 2546 555 246 518 C ATOM 817 O ILE A 110 -4.751 -51.562 556.348 1.00 15.41 O ANISOU 817 O ILE A 110 1867 1597 2391 550 278 487 O ATOM 818 CB ILE A 110 -6.271 -49.048 554.741 1.00 27.33 C ANISOU 818 CB ILE A 110 3400 3027 3958 657 86 538 C ATOM 819 CG1 ILE A 110 -6.155 -47.522 554.760 1.00 22.59 C ANISOU 819 CG1 ILE A 110 2849 2338 3395 712 -19 541 C ATOM 820 CG2 ILE A 110 -7.177 -49.540 555.855 1.00 13.35 C ANISOU 820 CG2 ILE A 110 1604 1293 2175 691 110 497 C ATOM 821 CD1 ILE A 110 -7.385 -46.809 554.245 1.00 47.74 C ANISOU 821 CD1 ILE A 110 6040 5505 6595 787 -102 561 C ATOM 822 N PHE A 111 -5.196 -51.996 554.186 1.00 28.80 N ANISOU 822 N PHE A 111 3551 3317 4075 534 274 541 N ATOM 823 CA PHE A 111 -5.209 -53.440 554.405 1.00 15.70 C ANISOU 823 CA PHE A 111 1887 1689 2390 505 340 524 C ATOM 824 C PHE A 111 -3.856 -53.933 554.899 1.00 25.45 C ANISOU 824 C PHE A 111 3132 2921 3616 475 398 508 C ATOM 825 O PHE A 111 -3.785 -54.772 555.805 1.00 36.78 O ANISOU 825 O PHE A 111 4571 4363 5040 460 435 489 O ATOM 826 CB PHE A 111 -5.602 -54.161 553.113 1.00 35.53 C ANISOU 826 CB PHE A 111 4402 4214 4883 502 335 543 C ATOM 827 CG PHE A 111 -5.317 -55.638 553.127 1.00 20.62 C ANISOU 827 CG PHE A 111 2531 2327 2977 479 387 517 C ATOM 828 CD1 PHE A 111 -4.096 -56.129 552.691 1.00 23.84 C ANISOU 828 CD1 PHE A 111 2967 2726 3366 470 432 506 C ATOM 829 CD2 PHE A 111 -6.273 -56.535 553.566 1.00 22.24 C ANISOU 829 CD2 PHE A 111 2728 2533 3190 476 384 507 C ATOM 830 CE1 PHE A 111 -3.831 -57.488 552.700 1.00 19.77 C ANISOU 830 CE1 PHE A 111 2483 2190 2837 463 466 475 C ATOM 831 CE2 PHE A 111 -6.017 -57.897 553.576 1.00 28.17 C ANISOU 831 CE2 PHE A 111 3508 3259 3938 460 413 480 C ATOM 832 CZ PHE A 111 -4.794 -58.373 553.142 1.00 17.27 C ANISOU 832 CZ PHE A 111 2169 1857 2537 456 451 458 C ATOM 833 N PHE A 112 -2.767 -53.430 554.309 1.00 27.46 N ANISOU 833 N PHE A 112 3389 3166 3878 468 401 524 N ATOM 834 CA PHE A 112 -1.433 -53.846 554.727 1.00 20.89 C ANISOU 834 CA PHE A 112 2557 2337 3044 448 453 517 C ATOM 835 C PHE A 112 -1.023 -53.215 556.050 1.00 15.85 C ANISOU 835 C PHE A 112 1915 1679 2429 447 432 500 C ATOM 836 O PHE A 112 -0.218 -53.797 556.784 1.00 30.17 O ANISOU 836 O PHE A 112 3729 3499 4236 433 468 490 O ATOM 837 CB PHE A 112 -0.408 -53.502 553.645 1.00 17.41 C ANISOU 837 CB PHE A 112 2107 1898 2608 450 466 552 C ATOM 838 CG PHE A 112 -0.531 -54.349 552.413 1.00 22.83 C ANISOU 838 CG PHE A 112 2813 2605 3257 463 495 561 C ATOM 839 CD1 PHE A 112 -0.045 -55.644 552.401 1.00 23.40 C ANISOU 839 CD1 PHE A 112 2911 2681 3297 465 553 537 C ATOM 840 CD2 PHE A 112 -1.140 -53.856 551.271 1.00 17.79 C ANISOU 840 CD2 PHE A 112 2179 1968 2611 478 450 595 C ATOM 841 CE1 PHE A 112 -0.160 -56.431 551.277 1.00 22.10 C ANISOU 841 CE1 PHE A 112 2784 2516 3096 491 567 532 C ATOM 842 CE2 PHE A 112 -1.259 -54.640 550.144 1.00 10.52 C ANISOU 842 CE2 PHE A 112 1290 1060 1647 497 463 602 C ATOM 843 CZ PHE A 112 -0.767 -55.929 550.146 1.00 17.32 C ANISOU 843 CZ PHE A 112 2183 1919 2478 509 524 562 C ATOM 844 N LEU A 113 -1.553 -52.034 556.371 1.00 21.56 N ANISOU 844 N LEU A 113 2644 2369 3177 472 361 495 N ATOM 845 CA LEU A 113 -1.229 -51.405 557.646 1.00 22.08 C ANISOU 845 CA LEU A 113 2723 2404 3261 488 323 466 C ATOM 846 C LEU A 113 -1.743 -52.241 558.813 1.00 26.33 C ANISOU 846 C LEU A 113 3267 2968 3767 493 354 440 C ATOM 847 O LEU A 113 -1.019 -52.480 559.787 1.00 31.78 O ANISOU 847 O LEU A 113 3963 3658 4454 488 365 425 O ATOM 848 CB LEU A 113 -1.809 -49.992 557.693 1.00 18.08 C ANISOU 848 CB LEU A 113 2244 1839 2787 535 225 457 C ATOM 849 CG LEU A 113 -1.491 -49.178 558.949 1.00 25.77 C ANISOU 849 CG LEU A 113 3251 2759 3781 574 157 413 C ATOM 850 CD1 LEU A 113 0.015 -49.067 559.157 1.00 33.50 C ANISOU 850 CD1 LEU A 113 4228 3719 4784 541 160 423 C ATOM 851 CD2 LEU A 113 -2.118 -47.803 558.859 1.00 13.09 C ANISOU 851 CD2 LEU A 113 1693 1075 2205 640 46 398 C ATOM 852 N ASN A 114 -2.996 -52.699 558.731 1.00 21.02 N ANISOU 852 N ASN A 114 2591 2320 3075 506 364 443 N ATOM 853 CA ASN A 114 -3.541 -53.539 559.793 1.00 26.31 C ANISOU 853 CA ASN A 114 3262 3016 3718 509 395 436 C ATOM 854 C ASN A 114 -2.828 -54.882 559.865 1.00 28.92 C ANISOU 854 C ASN A 114 3594 3363 4032 466 460 449 C ATOM 855 O ASN A 114 -2.784 -55.503 560.933 1.00 38.79 O ANISOU 855 O ASN A 114 4850 4621 5266 466 482 448 O ATOM 856 CB ASN A 114 -5.040 -53.744 559.582 1.00 17.39 C ANISOU 856 CB ASN A 114 2117 1908 2582 534 389 448 C ATOM 857 CG ASN A 114 -5.581 -54.931 560.350 1.00 27.45 C ANISOU 857 CG ASN A 114 3383 3211 3835 523 436 463 C ATOM 858 OD1 ASN A 114 -5.341 -55.079 561.552 1.00 30.31 O ANISOU 858 OD1 ASN A 114 3757 3579 4182 535 448 456 O ATOM 859 ND2 ASN A 114 -6.315 -55.788 559.657 1.00 34.47 N ANISOU 859 ND2 ASN A 114 4252 4113 4730 504 454 486 N ATOM 860 N MET A 115 -2.265 -55.341 558.749 1.00 22.28 N ANISOU 860 N MET A 115 2749 2522 3194 440 487 460 N ATOM 861 CA MET A 115 -1.529 -56.599 558.752 1.00 23.27 C ANISOU 861 CA MET A 115 2884 2649 3308 419 536 462 C ATOM 862 C MET A 115 -0.268 -56.491 559.604 1.00 18.92 C ANISOU 862 C MET A 115 2335 2093 2761 417 544 460 C ATOM 863 O MET A 115 -0.070 -57.266 560.547 1.00 16.56 O ANISOU 863 O MET A 115 2045 1794 2453 418 562 459 O ATOM 864 CB MET A 115 -1.187 -56.991 557.315 1.00 22.23 C ANISOU 864 CB MET A 115 2759 2514 3172 415 554 467 C ATOM 865 CG MET A 115 -0.426 -58.299 557.176 1.00 28.68 C ANISOU 865 CG MET A 115 3601 3317 3978 413 594 459 C ATOM 866 SD MET A 115 0.179 -58.566 555.499 1.00 28.18 S ANISOU 866 SD MET A 115 3563 3245 3900 431 611 460 S ATOM 867 CE MET A 115 1.296 -57.174 555.317 1.00 28.60 C ANISOU 867 CE MET A 115 3580 3319 3967 430 615 493 C ATOM 868 N PHE A 116 0.597 -55.521 559.291 1.00 20.11 N ANISOU 868 N PHE A 116 2473 2234 2932 419 524 462 N ATOM 869 CA PHE A 116 1.817 -55.347 560.075 1.00 29.05 C ANISOU 869 CA PHE A 116 3599 3357 4080 420 518 461 C ATOM 870 C PHE A 116 1.493 -54.988 561.520 1.00 24.21 C ANISOU 870 C PHE A 116 2999 2736 3462 440 479 438 C ATOM 871 O PHE A 116 2.110 -55.514 562.454 1.00 16.73 O ANISOU 871 O PHE A 116 2058 1791 2509 446 487 436 O ATOM 872 CB PHE A 116 2.705 -54.269 559.445 1.00 18.79 C ANISOU 872 CB PHE A 116 2276 2043 2820 419 493 474 C ATOM 873 CG PHE A 116 3.396 -54.705 558.178 1.00 17.96 C ANISOU 873 CG PHE A 116 2157 1953 2715 411 543 506 C ATOM 874 CD1 PHE A 116 4.343 -55.715 558.199 1.00 16.86 C ANISOU 874 CD1 PHE A 116 2020 1821 2564 415 591 519 C ATOM 875 CD2 PHE A 116 3.114 -54.086 556.971 1.00 16.45 C ANISOU 875 CD2 PHE A 116 1954 1763 2532 414 536 526 C ATOM 876 CE1 PHE A 116 4.982 -56.111 557.039 1.00 13.61 C ANISOU 876 CE1 PHE A 116 1608 1421 2144 427 635 547 C ATOM 877 CE2 PHE A 116 3.749 -54.477 555.808 1.00 13.34 C ANISOU 877 CE2 PHE A 116 1553 1389 2128 420 584 558 C ATOM 878 CZ PHE A 116 4.685 -55.491 555.842 1.00 18.01 C ANISOU 878 CZ PHE A 116 2154 1988 2701 429 636 568 C ATOM 879 N ALA A 117 0.521 -54.095 561.724 1.00 23.45 N ANISOU 879 N ALA A 117 2914 2629 3369 464 432 419 N ATOM 880 CA ALA A 117 0.197 -53.647 563.073 1.00 21.07 C ANISOU 880 CA ALA A 117 2633 2317 3057 504 387 389 C ATOM 881 C ALA A 117 -0.316 -54.800 563.927 1.00 27.11 C ANISOU 881 C ALA A 117 3404 3113 3782 506 434 402 C ATOM 882 O ALA A 117 0.119 -54.984 565.069 1.00 26.19 O ANISOU 882 O ALA A 117 3300 2998 3653 527 425 393 O ATOM 883 CB ALA A 117 -0.835 -52.523 563.013 1.00 25.29 C ANISOU 883 CB ALA A 117 3179 2827 3601 549 325 362 C ATOM 884 N SER A 118 -1.241 -55.596 563.383 1.00 23.34 N ANISOU 884 N SER A 118 2920 2658 3292 489 476 427 N ATOM 885 CA SER A 118 -1.783 -56.715 564.146 1.00 19.11 C ANISOU 885 CA SER A 118 2387 2142 2733 490 517 450 C ATOM 886 C SER A 118 -0.680 -57.691 564.530 1.00 19.11 C ANISOU 886 C SER A 118 2392 2136 2734 474 547 461 C ATOM 887 O SER A 118 -0.648 -58.190 565.662 1.00 16.34 O ANISOU 887 O SER A 118 2049 1793 2366 494 557 471 O ATOM 888 CB SER A 118 -2.871 -57.425 563.340 1.00 24.81 C ANISOU 888 CB SER A 118 3094 2873 3460 471 545 473 C ATOM 889 OG SER A 118 -3.961 -56.558 563.071 1.00 35.64 O ANISOU 889 OG SER A 118 4456 4255 4832 499 513 468 O ATOM 890 N GLY A 119 0.238 -57.966 563.604 1.00 13.35 N ANISOU 890 N GLY A 119 1656 1393 2023 450 561 460 N ATOM 891 CA GLY A 119 1.335 -58.867 563.912 1.00 17.14 C ANISOU 891 CA GLY A 119 2141 1863 2510 451 582 468 C ATOM 892 C GLY A 119 2.273 -58.310 564.965 1.00 16.52 C ANISOU 892 C GLY A 119 2062 1782 2432 474 549 460 C ATOM 893 O GLY A 119 2.706 -59.033 565.867 1.00 26.13 O ANISOU 893 O GLY A 119 3287 2998 3644 493 556 469 O ATOM 894 N PHE A 120 2.606 -57.021 564.867 1.00 17.52 N ANISOU 894 N PHE A 120 2182 1902 2574 478 504 439 N ATOM 895 CA PHE A 120 3.524 -56.426 565.834 1.00 16.77 C ANISOU 895 CA PHE A 120 2087 1792 2491 504 454 421 C ATOM 896 C PHE A 120 2.905 -56.377 567.226 1.00 17.13 C ANISOU 896 C PHE A 120 2157 1846 2504 545 429 405 C ATOM 897 O PHE A 120 3.569 -56.698 568.218 1.00 19.61 O ANISOU 897 O PHE A 120 2477 2160 2813 570 414 405 O ATOM 898 CB PHE A 120 3.934 -55.023 565.382 1.00 21.48 C ANISOU 898 CB PHE A 120 2673 2362 3126 505 396 397 C ATOM 899 CG PHE A 120 4.645 -54.988 564.051 1.00 20.87 C ANISOU 899 CG PHE A 120 2566 2284 3081 472 425 424 C ATOM 900 CD1 PHE A 120 5.234 -56.127 563.523 1.00 17.86 C ANISOU 900 CD1 PHE A 120 2173 1919 2695 460 488 455 C ATOM 901 CD2 PHE A 120 4.721 -53.808 563.329 1.00 20.39 C ANISOU 901 CD2 PHE A 120 2493 2198 3056 466 386 420 C ATOM 902 CE1 PHE A 120 5.884 -56.090 562.305 1.00 17.86 C ANISOU 902 CE1 PHE A 120 2148 1921 2716 445 518 481 C ATOM 903 CE2 PHE A 120 5.370 -53.764 562.109 1.00 24.52 C ANISOU 903 CE2 PHE A 120 2983 2727 3607 442 419 456 C ATOM 904 CZ PHE A 120 5.952 -54.907 561.596 1.00 26.29 C ANISOU 904 CZ PHE A 120 3195 2978 3817 434 490 486 C ATOM 905 N LEU A 121 1.634 -55.981 567.320 1.00 16.37 N ANISOU 905 N LEU A 121 2073 1760 2385 560 424 395 N ATOM 906 CA LEU A 121 0.994 -55.883 568.627 1.00 20.39 C ANISOU 906 CA LEU A 121 2604 2287 2857 613 407 383 C ATOM 907 C LEU A 121 0.903 -57.245 569.299 1.00 18.30 C ANISOU 907 C LEU A 121 2341 2050 2563 612 465 430 C ATOM 908 O LEU A 121 1.176 -57.372 570.498 1.00 20.59 O ANISOU 908 O LEU A 121 2644 2352 2828 655 451 429 O ATOM 909 CB LEU A 121 -0.395 -55.264 568.484 1.00 26.26 C ANISOU 909 CB LEU A 121 3351 3043 3585 640 399 370 C ATOM 910 CG LEU A 121 -0.416 -53.783 568.095 1.00 24.56 C ANISOU 910 CG LEU A 121 3139 2787 3406 667 322 314 C ATOM 911 CD1 LEU A 121 -1.828 -53.339 567.727 1.00 20.54 C ANISOU 911 CD1 LEU A 121 2624 2291 2890 698 320 308 C ATOM 912 CD2 LEU A 121 0.137 -52.926 569.224 1.00 27.56 C ANISOU 912 CD2 LEU A 121 3537 3135 3801 727 244 256 C ATOM 913 N LEU A 122 0.525 -58.279 568.544 1.00 19.31 N ANISOU 913 N LEU A 122 2456 2182 2700 572 524 468 N ATOM 914 CA LEU A 122 0.425 -59.609 569.134 1.00 23.58 C ANISOU 914 CA LEU A 122 2995 2730 3233 576 569 509 C ATOM 915 C LEU A 122 1.769 -60.079 569.668 1.00 26.26 C ANISOU 915 C LEU A 122 3338 3053 3585 591 556 510 C ATOM 916 O LEU A 122 1.822 -60.777 570.688 1.00 25.27 O ANISOU 916 O LEU A 122 3220 2937 3445 622 567 537 O ATOM 917 CB LEU A 122 -0.124 -60.602 568.109 1.00 25.31 C ANISOU 917 CB LEU A 122 3199 2935 3482 536 614 530 C ATOM 918 CG LEU A 122 -1.608 -60.436 567.763 1.00 23.57 C ANISOU 918 CG LEU A 122 2965 2734 3256 529 629 545 C ATOM 919 CD1 LEU A 122 -2.024 -61.441 566.702 1.00 40.44 C ANISOU 919 CD1 LEU A 122 5086 4846 5435 494 655 552 C ATOM 920 CD2 LEU A 122 -2.480 -60.586 568.999 1.00 24.16 C ANISOU 920 CD2 LEU A 122 3037 2846 3298 570 645 584 C ATOM 921 N SER A 123 2.864 -59.714 568.998 1.00 19.15 N ANISOU 921 N SER A 123 2429 2132 2714 574 532 488 N ATOM 922 CA SER A 123 4.184 -59.989 569.554 1.00 19.72 C ANISOU 922 CA SER A 123 2499 2192 2804 599 508 490 C ATOM 923 C SER A 123 4.399 -59.208 570.845 1.00 31.63 C ANISOU 923 C SER A 123 4019 3710 4290 644 452 470 C ATOM 924 O SER A 123 4.935 -59.744 571.822 1.00 28.12 O ANISOU 924 O SER A 123 3578 3269 3838 681 439 487 O ATOM 925 CB SER A 123 5.271 -59.645 568.535 1.00 27.04 C ANISOU 925 CB SER A 123 3404 3100 3770 579 496 478 C ATOM 926 OG SER A 123 4.985 -60.202 567.261 1.00 23.95 O ANISOU 926 OG SER A 123 3009 2701 3390 548 542 488 O ATOM 927 N ALA A 124 3.979 -57.940 570.868 1.00 23.92 N ANISOU 927 N ALA A 124 3049 2732 3305 651 408 429 N ATOM 928 CA ALA A 124 4.128 -57.132 572.074 1.00 20.45 C ANISOU 928 CA ALA A 124 2626 2293 2851 708 341 392 C ATOM 929 C ALA A 124 3.329 -57.718 573.232 1.00 20.96 C ANISOU 929 C ALA A 124 2711 2400 2854 754 371 420 C ATOM 930 O ALA A 124 3.819 -57.780 574.366 1.00 16.16 O ANISOU 930 O ALA A 124 2110 1802 2226 804 339 419 O ATOM 931 CB ALA A 124 3.691 -55.694 571.797 1.00 26.53 C ANISOU 931 CB ALA A 124 3403 3038 3639 719 281 333 C ATOM 932 N ILE A 125 2.097 -58.155 572.965 1.00 19.78 N ANISOU 932 N ILE A 125 2563 2279 2675 742 432 452 N ATOM 933 CA ILE A 125 1.280 -58.757 574.014 1.00 21.40 C ANISOU 933 CA ILE A 125 2776 2534 2821 789 471 496 C ATOM 934 C ILE A 125 1.967 -59.997 574.570 1.00 22.22 C ANISOU 934 C ILE A 125 2875 2636 2934 793 496 548 C ATOM 935 O ILE A 125 1.952 -60.244 575.782 1.00 25.64 O ANISOU 935 O ILE A 125 3315 3106 3322 851 493 575 O ATOM 936 CB ILE A 125 -0.126 -59.082 573.475 1.00 25.28 C ANISOU 936 CB ILE A 125 3255 3051 3300 769 530 533 C ATOM 937 CG1 ILE A 125 -0.855 -57.799 573.077 1.00 21.03 C ANISOU 937 CG1 ILE A 125 2720 2517 2753 788 493 480 C ATOM 938 CG2 ILE A 125 -0.941 -59.834 574.519 1.00 15.84 C ANISOU 938 CG2 ILE A 125 2050 1914 2053 815 579 599 C ATOM 939 CD1 ILE A 125 -2.055 -58.031 572.188 1.00 26.28 C ANISOU 939 CD1 ILE A 125 3364 3192 3428 756 535 511 C ATOM 940 N SER A 126 2.574 -60.799 573.694 1.00 23.60 N ANISOU 940 N SER A 126 3034 2768 3164 743 515 562 N ATOM 941 CA SER A 126 3.249 -62.011 574.147 1.00 29.85 C ANISOU 941 CA SER A 126 3821 3541 3978 759 523 606 C ATOM 942 C SER A 126 4.446 -61.679 575.027 1.00 24.52 C ANISOU 942 C SER A 126 3152 2865 3301 804 459 593 C ATOM 943 O SER A 126 4.579 -62.206 576.137 1.00 39.85 O ANISOU 943 O SER A 126 5099 4823 5218 852 449 634 O ATOM 944 CB SER A 126 3.688 -62.845 572.945 1.00 31.05 C ANISOU 944 CB SER A 126 3963 3643 4193 716 543 607 C ATOM 945 OG SER A 126 2.577 -63.469 572.332 1.00 65.82 O ANISOU 945 OG SER A 126 8360 8038 8609 685 591 625 O ATOM 946 N LEU A 127 5.334 -60.809 574.544 1.00 24.99 N ANISOU 946 N LEU A 127 3203 2903 3389 790 409 543 N ATOM 947 CA LEU A 127 6.522 -60.468 575.318 1.00 21.64 C ANISOU 947 CA LEU A 127 2772 2471 2978 832 336 530 C ATOM 948 C LEU A 127 6.144 -59.778 576.622 1.00 30.16 C ANISOU 948 C LEU A 127 3871 3586 4002 891 293 514 C ATOM 949 O LEU A 127 6.799 -59.978 577.652 1.00 21.80 O ANISOU 949 O LEU A 127 2812 2538 2932 941 247 534 O ATOM 950 CB LEU A 127 7.450 -59.590 574.479 1.00 24.40 C ANISOU 950 CB LEU A 127 3099 2789 3383 804 288 485 C ATOM 951 CG LEU A 127 8.128 -60.328 573.321 1.00 13.21 C ANISOU 951 CG LEU A 127 1656 1350 2012 771 327 507 C ATOM 952 CD1 LEU A 127 8.594 -59.361 572.250 1.00 15.44 C ANISOU 952 CD1 LEU A 127 1915 1617 2333 733 309 474 C ATOM 953 CD2 LEU A 127 9.298 -61.148 573.836 1.00 25.32 C ANISOU 953 CD2 LEU A 127 3172 2873 3575 815 300 542 C ATOM 954 N ASP A 128 5.087 -58.966 576.600 1.00 31.87 N ANISOU 954 N ASP A 128 4105 3825 4179 896 305 479 N ATOM 955 CA ASP A 128 4.592 -58.368 577.835 1.00 19.78 C ANISOU 955 CA ASP A 128 2595 2342 2578 972 277 459 C ATOM 956 C ASP A 128 4.233 -59.445 578.851 1.00 27.29 C ANISOU 956 C ASP A 128 3550 3353 3466 1018 323 538 C ATOM 957 O ASP A 128 4.696 -59.416 579.998 1.00 28.86 O ANISOU 957 O ASP A 128 3755 3586 3626 1081 277 549 O ATOM 958 CB ASP A 128 3.381 -57.485 577.534 1.00 28.09 C ANISOU 958 CB ASP A 128 3661 3414 3597 982 294 414 C ATOM 959 CG ASP A 128 2.676 -57.015 578.788 1.00 30.66 C ANISOU 959 CG ASP A 128 4007 3814 3829 1081 288 395 C ATOM 960 OD1 ASP A 128 3.307 -56.301 579.594 1.00 30.73 O ANISOU 960 OD1 ASP A 128 4028 3820 3828 1138 215 341 O ATOM 961 OD2 ASP A 128 1.489 -57.362 578.966 1.00 29.29 O ANISOU 961 OD2 ASP A 128 3831 3710 3589 1107 354 434 O ATOM 962 N ARG A 129 3.414 -60.416 578.439 1.00 29.56 N ANISOU 962 N ARG A 129 3828 3652 3750 985 405 601 N ATOM 963 CA ARG A 129 3.050 -61.509 579.335 1.00 31.81 C ANISOU 963 CA ARG A 129 4105 3983 3997 1020 443 692 C ATOM 964 C ARG A 129 4.276 -62.293 579.779 1.00 27.45 C ANISOU 964 C ARG A 129 3552 3392 3485 1028 394 733 C ATOM 965 O ARG A 129 4.267 -62.902 580.854 1.00 26.95 O ANISOU 965 O ARG A 129 3491 3369 3380 1075 382 807 O ATOM 966 CB ARG A 129 2.043 -62.431 578.644 1.00 45.51 C ANISOU 966 CB ARG A 129 5819 5709 5762 971 523 749 C ATOM 967 CG ARG A 129 1.730 -63.726 579.385 1.00 29.23 C ANISOU 967 CG ARG A 129 3742 3663 3703 988 544 857 C ATOM 968 CD ARG A 129 1.139 -63.473 580.759 1.00 39.12 C ANISOU 968 CD ARG A 129 4985 5034 4846 1072 553 914 C ATOM 969 NE ARG A 129 0.706 -64.716 581.394 1.00 48.05 N ANISOU 969 NE ARG A 129 6092 6196 5969 1091 593 1070 N ATOM 970 CZ ARG A 129 0.296 -64.815 582.655 1.00 43.28 C ANISOU 970 CZ ARG A 129 5462 5737 5245 1189 634 1195 C ATOM 971 NH1 ARG A 129 0.263 -63.743 583.435 1.00 45.96 N ANISOU 971 NH1 ARG A 129 5800 6220 5445 1316 657 1165 N ATOM 972 NH2 ARG A 129 -0.079 -65.992 583.139 1.00 41.67 N ANISOU 972 NH2 ARG A 129 5247 5543 5043 1146 628 1346 N ATOM 973 N CYS A 130 5.337 -62.293 578.970 1.00 24.78 N ANISOU 973 N CYS A 130 3207 2985 3223 988 359 697 N ATOM 974 CA CYS A 130 6.540 -63.036 579.327 1.00 26.09 C ANISOU 974 CA CYS A 130 3367 3115 3431 1007 307 737 C ATOM 975 C CYS A 130 7.348 -62.303 580.391 1.00 32.81 C ANISOU 975 C CYS A 130 4219 3998 4251 1064 218 722 C ATOM 976 O CYS A 130 7.772 -62.906 581.382 1.00 33.25 O ANISOU 976 O CYS A 130 4278 4072 4283 1108 175 790 O ATOM 977 CB CYS A 130 7.393 -63.284 578.084 1.00 35.38 C ANISOU 977 CB CYS A 130 4525 4225 4691 962 306 708 C ATOM 978 SG CYS A 130 8.803 -64.370 578.386 1.00 38.34 S ANISOU 978 SG CYS A 130 4890 4553 5123 1002 249 763 S ATOM 979 N LEU A 131 7.571 -60.999 580.205 1.00 28.23 N ANISOU 979 N LEU A 131 3634 3416 3675 1063 174 638 N ATOM 980 CA LEU A 131 8.277 -60.229 581.223 1.00 31.69 C ANISOU 980 CA LEU A 131 4071 3877 4095 1117 75 616 C ATOM 981 C LEU A 131 7.483 -60.174 582.519 1.00 36.54 C ANISOU 981 C LEU A 131 4711 4581 4590 1190 79 645 C ATOM 982 O LEU A 131 8.068 -60.070 583.603 1.00 35.22 O ANISOU 982 O LEU A 131 4546 4456 4381 1244 -1 671 O ATOM 983 CB LEU A 131 8.560 -58.815 580.716 1.00 36.60 C ANISOU 983 CB LEU A 131 4683 4457 4766 1099 20 520 C ATOM 984 CG LEU A 131 9.567 -58.702 579.571 1.00 45.18 C ANISOU 984 CG LEU A 131 5731 5473 5962 1039 -8 500 C ATOM 985 CD1 LEU A 131 9.633 -57.269 579.067 1.00 60.46 C ANISOU 985 CD1 LEU A 131 7657 7360 7956 1015 -63 420 C ATOM 986 CD2 LEU A 131 10.948 -59.182 580.008 1.00 60.89 C ANISOU 986 CD2 LEU A 131 7685 7454 7998 1062 -85 546 C ATOM 987 N GLN A 132 6.154 -60.249 582.428 1.00 43.36 N ANISOU 987 N GLN A 132 5591 5491 5392 1196 166 650 N ATOM 988 CA GLN A 132 5.323 -60.249 583.626 1.00 23.24 C ANISOU 988 CA GLN A 132 3062 3072 2696 1301 201 699 C ATOM 989 C GLN A 132 5.633 -61.444 584.519 1.00 30.92 C ANISOU 989 C GLN A 132 4032 4098 3618 1337 204 840 C ATOM 990 O GLN A 132 5.571 -61.333 585.748 1.00 34.94 O ANISOU 990 O GLN A 132 4558 4748 3970 1459 199 900 O ATOM 991 CB GLN A 132 3.848 -60.252 583.222 1.00 33.04 C ANISOU 991 CB GLN A 132 4302 4367 3885 1311 314 708 C ATOM 992 CG GLN A 132 2.866 -60.163 584.375 1.00 25.73 C ANISOU 992 CG GLN A 132 3385 3643 2750 1483 399 780 C ATOM 993 CD GLN A 132 1.429 -60.366 583.925 1.00 45.97 C ANISOU 993 CD GLN A 132 5919 6271 5276 1489 517 826 C ATOM 994 OE1 GLN A 132 1.167 -60.624 582.751 1.00 51.47 O ANISOU 994 OE1 GLN A 132 6601 6848 6106 1355 527 802 O ATOM 995 NE2 GLN A 132 0.490 -60.251 584.859 1.00 83.62 N ANISOU 995 NE2 GLN A 132 10663 11259 9849 1652 601 894 N ATOM 996 N VAL A 133 5.972 -62.584 583.923 1.00 31.67 N ANISOU 996 N VAL A 133 4112 4089 3831 1235 194 886 N ATOM 997 CA VAL A 133 6.219 -63.810 584.673 1.00 29.50 C ANISOU 997 CA VAL A 133 3846 3831 3533 1247 177 1024 C ATOM 998 C VAL A 133 7.700 -63.996 584.975 1.00 41.49 C ANISOU 998 C VAL A 133 5364 5293 5107 1241 56 1028 C ATOM 999 O VAL A 133 8.060 -64.454 586.061 1.00 64.30 O ANISOU 999 O VAL A 133 8267 8246 7917 1291 9 1134 O ATOM 1000 CB VAL A 133 5.655 -65.022 583.900 1.00 24.53 C ANISOU 1000 CB VAL A 133 3216 3117 2987 1168 228 1077 C ATOM 1001 CG1 VAL A 133 5.834 -66.301 584.708 1.00 40.76 C ANISOU 1001 CG1 VAL A 133 5300 5162 5024 1162 183 1223 C ATOM 1002 CG2 VAL A 133 4.189 -64.808 583.561 1.00 26.11 C ANISOU 1002 CG2 VAL A 133 3398 3376 3145 1166 338 1081 C ATOM 1003 N VAL A 134 8.573 -63.643 584.035 1.00 46.27 N ANISOU 1003 N VAL A 134 5947 5818 5816 1216 36 949 N ATOM 1004 CA VAL A 134 9.987 -63.973 584.169 1.00 39.36 C ANISOU 1004 CA VAL A 134 5053 4900 5001 1229 -55 974 C ATOM 1005 C VAL A 134 10.773 -62.894 584.910 1.00 43.98 C ANISOU 1005 C VAL A 134 5622 5533 5557 1265 -165 935 C ATOM 1006 O VAL A 134 11.781 -63.206 585.553 1.00 50.39 O ANISOU 1006 O VAL A 134 6420 6353 6373 1292 -263 992 O ATOM 1007 CB VAL A 134 10.597 -64.236 582.783 1.00 37.55 C ANISOU 1007 CB VAL A 134 4797 4579 4891 1190 -24 925 C ATOM 1008 CG1 VAL A 134 12.069 -64.599 582.910 1.00 72.63 C ANISOU 1008 CG1 VAL A 134 9209 8991 9395 1222 -114 954 C ATOM 1009 CG2 VAL A 134 9.831 -65.340 582.073 1.00 47.17 C ANISOU 1009 CG2 VAL A 134 6037 5747 6139 1156 65 962 C ATOM 1010 N ARG A 135 10.338 -61.635 584.850 1.00 39.66 N ANISOU 1010 N ARG A 135 5076 5012 4981 1269 -164 842 N ATOM 1011 CA ARG A 135 11.008 -60.527 585.534 1.00 42.48 C ANISOU 1011 CA ARG A 135 5425 5417 5301 1321 -267 807 C ATOM 1012 C ARG A 135 9.989 -59.795 586.399 1.00 35.86 C ANISOU 1012 C ARG A 135 4642 4717 4266 1440 -224 784 C ATOM 1013 O ARG A 135 9.657 -58.631 586.141 1.00 39.87 O ANISOU 1013 O ARG A 135 5171 5220 4759 1472 -226 674 O ATOM 1014 CB ARG A 135 11.656 -59.560 584.539 1.00 40.26 C ANISOU 1014 CB ARG A 135 5100 5038 5160 1258 -313 709 C ATOM 1015 CG ARG A 135 12.340 -60.207 583.341 1.00 66.22 C ANISOU 1015 CG ARG A 135 8351 8245 8565 1208 -280 715 C ATOM 1016 CD ARG A 135 13.453 -61.163 583.739 1.00 68.07 C ANISOU 1016 CD ARG A 135 8556 8481 8825 1233 -345 798 C ATOM 1017 NE ARG A 135 14.459 -60.543 584.593 1.00 85.76 N ANISOU 1017 NE ARG A 135 10760 10754 11072 1257 -493 816 N ATOM 1018 CZ ARG A 135 15.467 -61.205 585.153 1.00100.56 C ANISOU 1018 CZ ARG A 135 12605 12648 12953 1289 -580 891 C ATOM 1019 NH1 ARG A 135 15.600 -62.511 584.950 1.00 77.08 N ANISOU 1019 NH1 ARG A 135 9642 9654 9990 1312 -527 953 N ATOM 1020 NH2 ARG A 135 16.341 -60.565 585.920 1.00116.88 N ANISOU 1020 NH2 ARG A 135 14633 14763 15013 1306 -723 915 N ATOM 1021 N PRO A 136 9.480 -60.446 587.449 1.00 38.11 N ANISOU 1021 N PRO A 136 4958 5135 4387 1518 -193 883 N ATOM 1022 CA PRO A 136 8.440 -59.789 588.263 1.00 44.93 C ANISOU 1022 CA PRO A 136 5871 6170 5029 1657 -146 848 C ATOM 1023 C PRO A 136 8.880 -58.462 588.855 1.00 44.25 C ANISOU 1023 C PRO A 136 5827 6156 4831 1767 -261 725 C ATOM 1024 O PRO A 136 8.132 -57.478 588.794 1.00 39.52 O ANISOU 1024 O PRO A 136 5274 5596 4145 1863 -238 595 O ATOM 1025 CB PRO A 136 8.144 -60.829 589.356 1.00 30.35 C ANISOU 1025 CB PRO A 136 4030 4470 3034 1690 -124 1005 C ATOM 1026 CG PRO A 136 8.633 -62.120 588.817 1.00 52.88 C ANISOU 1026 CG PRO A 136 6851 7176 6063 1562 -123 1110 C ATOM 1027 CD PRO A 136 9.808 -61.789 587.956 1.00 47.24 C ANISOU 1027 CD PRO A 136 6105 6301 5541 1489 -208 1028 C ATOM 1028 N VAL A 137 10.086 -58.405 589.423 1.00 53.24 N ANISOU 1028 N VAL A 137 6955 7309 5966 1760 -402 751 N ATOM 1029 CA VAL A 137 10.522 -57.195 590.116 1.00 52.52 C ANISOU 1029 CA VAL A 137 6916 7299 5739 1864 -546 624 C ATOM 1030 C VAL A 137 10.597 -56.026 589.144 1.00 47.18 C ANISOU 1030 C VAL A 137 6255 6472 5200 1850 -577 472 C ATOM 1031 O VAL A 137 10.060 -54.943 589.404 1.00 47.08 O ANISOU 1031 O VAL A 137 6326 6497 5064 1973 -624 309 O ATOM 1032 CB VAL A 137 11.874 -57.432 590.811 1.00 67.08 C ANISOU 1032 CB VAL A 137 8726 9184 7576 1826 -703 699 C ATOM 1033 CG1 VAL A 137 12.276 -56.203 591.619 1.00 51.88 C ANISOU 1033 CG1 VAL A 137 6870 7361 5481 1919 -880 550 C ATOM 1034 CG2 VAL A 137 11.808 -58.671 591.692 1.00 67.86 C ANISOU 1034 CG2 VAL A 137 8813 9401 7569 1813 -672 867 C ATOM 1035 N TRP A 138 11.268 -56.227 588.008 1.00 50.85 N ANISOU 1035 N TRP A 138 6640 6763 5917 1700 -562 516 N ATOM 1036 CA TRP A 138 11.378 -55.153 587.029 1.00 46.69 C ANISOU 1036 CA TRP A 138 6114 6096 5532 1653 -585 403 C ATOM 1037 C TRP A 138 10.015 -54.775 586.470 1.00 38.25 C ANISOU 1037 C TRP A 138 5092 4994 4447 1672 -462 314 C ATOM 1038 O TRP A 138 9.785 -53.607 586.134 1.00 45.28 O ANISOU 1038 O TRP A 138 6036 5814 5355 1701 -507 179 O ATOM 1039 CB TRP A 138 12.318 -55.561 585.895 1.00 46.53 C ANISOU 1039 CB TRP A 138 5977 5937 5765 1484 -572 491 C ATOM 1040 CG TRP A 138 12.398 -54.536 584.811 1.00 47.20 C ANISOU 1040 CG TRP A 138 6046 5895 5994 1415 -574 415 C ATOM 1041 CD1 TRP A 138 13.312 -53.529 584.698 1.00 55.09 C ANISOU 1041 CD1 TRP A 138 7038 6850 7044 1418 -704 377 C ATOM 1042 CD2 TRP A 138 11.520 -54.409 583.687 1.00 50.63 C ANISOU 1042 CD2 TRP A 138 6469 6238 6530 1326 -452 378 C ATOM 1043 NE1 TRP A 138 13.060 -52.785 583.570 1.00 50.59 N ANISOU 1043 NE1 TRP A 138 6460 6163 6599 1344 -653 332 N ATOM 1044 CE2 TRP A 138 11.964 -53.304 582.932 1.00 41.93 C ANISOU 1044 CE2 TRP A 138 5352 5041 5539 1281 -496 336 C ATOM 1045 CE3 TRP A 138 10.402 -55.123 583.244 1.00 46.66 C ANISOU 1045 CE3 TRP A 138 5968 5737 6023 1276 -326 381 C ATOM 1046 CZ2 TRP A 138 11.330 -52.897 581.761 1.00 54.69 C ANISOU 1046 CZ2 TRP A 138 6944 6569 7265 1185 -405 310 C ATOM 1047 CZ3 TRP A 138 9.773 -54.717 582.080 1.00 48.05 C ANISOU 1047 CZ3 TRP A 138 6132 5835 6290 1193 -262 332 C ATOM 1048 CH2 TRP A 138 10.239 -53.615 581.352 1.00 61.94 C ANISOU 1048 CH2 TRP A 138 7870 7505 8161 1150 -302 298 C ATOM 1049 N ALA A 139 9.104 -55.742 586.356 1.00 42.78 N ANISOU 1049 N ALA A 139 5649 5614 4990 1650 -321 391 N ATOM 1050 CA ALA A 139 7.796 -55.459 585.777 1.00 46.31 C ANISOU 1050 CA ALA A 139 6119 6050 5425 1649 -209 328 C ATOM 1051 C ALA A 139 6.972 -54.566 586.695 1.00 44.52 C ANISOU 1051 C ALA A 139 5988 5957 4972 1855 -230 200 C ATOM 1052 O ALA A 139 6.388 -53.571 586.250 1.00 48.47 O ANISOU 1052 O ALA A 139 6527 6398 5491 1870 -234 72 O ATOM 1053 CB ALA A 139 7.056 -56.765 585.489 1.00 34.94 C ANISOU 1053 CB ALA A 139 4639 4641 3995 1583 -75 447 C ATOM 1054 N GLN A 140 6.927 -54.893 587.986 1.00 49.69 N ANISOU 1054 N GLN A 140 6674 6802 5403 2013 -256 229 N ATOM 1055 CA GLN A 140 6.138 -54.116 588.935 1.00 44.78 C ANISOU 1055 CA GLN A 140 6132 6354 4527 2244 -282 90 C ATOM 1056 C GLN A 140 6.675 -52.705 589.136 1.00 39.02 C ANISOU 1056 C GLN A 140 5497 5546 3784 2335 -464 -125 C ATOM 1057 O GLN A 140 6.058 -51.936 589.881 1.00 49.20 O ANISOU 1057 O GLN A 140 6865 6956 4872 2546 -511 -295 O ATOM 1058 CB GLN A 140 6.076 -54.838 590.283 1.00 35.39 C ANISOU 1058 CB GLN A 140 4938 5424 3085 2355 -282 191 C ATOM 1059 CG GLN A 140 7.425 -54.998 590.962 1.00 50.47 C ANISOU 1059 CG GLN A 140 6856 7342 4978 2297 -440 235 C ATOM 1060 CD GLN A 140 7.310 -55.581 592.354 1.00 70.79 C ANISOU 1060 CD GLN A 140 9434 10179 7286 2344 -441 317 C ATOM 1061 OE1 GLN A 140 6.395 -56.353 592.641 1.00 77.43 O ANISOU 1061 OE1 GLN A 140 10231 11159 8029 2350 -293 432 O ATOM 1062 NE2 GLN A 140 8.236 -55.208 593.231 1.00 70.03 N ANISOU 1062 NE2 GLN A 140 9381 10149 7076 2347 -610 259 N ATOM 1063 N ASN A 141 7.800 -52.351 588.510 1.00 39.79 N ANISOU 1063 N ASN A 141 5583 5450 4085 2194 -574 -128 N ATOM 1064 CA ASN A 141 8.354 -51.010 588.606 1.00 44.68 C ANISOU 1064 CA ASN A 141 6298 5956 4724 2255 -771 -321 C ATOM 1065 C ASN A 141 8.400 -50.271 587.276 1.00 46.47 C ANISOU 1065 C ASN A 141 6512 5947 5197 2094 -757 -361 C ATOM 1066 O ASN A 141 8.682 -49.067 587.273 1.00 49.53 O ANISOU 1066 O ASN A 141 6993 6208 5616 2134 -916 -528 O ATOM 1067 CB ASN A 141 9.771 -51.059 589.201 1.00 28.62 C ANISOU 1067 CB ASN A 141 4258 3938 2679 2222 -968 -280 C ATOM 1068 CG ASN A 141 9.779 -51.498 590.655 1.00 38.56 C ANISOU 1068 CG ASN A 141 5551 5459 3643 2338 -1029 -265 C ATOM 1069 OD1 ASN A 141 8.866 -51.180 591.415 1.00 44.29 O ANISOU 1069 OD1 ASN A 141 6353 6336 4141 2472 -991 -395 O ATOM 1070 ND2 ASN A 141 10.811 -52.235 591.047 1.00 45.95 N ANISOU 1070 ND2 ASN A 141 6413 6453 4591 2224 -1081 -114 N ATOM 1071 N HIS A 142 8.126 -50.940 586.153 1.00 32.96 N ANISOU 1071 N HIS A 142 4691 4177 3656 1907 -589 -213 N ATOM 1072 CA HIS A 142 8.166 -50.269 584.858 1.00 47.06 C ANISOU 1072 CA HIS A 142 6443 5786 5654 1746 -571 -220 C ATOM 1073 C HIS A 142 7.018 -50.622 583.923 1.00 36.61 C ANISOU 1073 C HIS A 142 5050 4458 4402 1636 -396 -156 C ATOM 1074 O HIS A 142 6.895 -49.971 582.881 1.00 37.18 O ANISOU 1074 O HIS A 142 5093 4412 4624 1521 -380 -163 O ATOM 1075 CB HIS A 142 9.495 -50.569 584.151 1.00 42.89 C ANISOU 1075 CB HIS A 142 5818 5163 5314 1595 -606 -97 C ATOM 1076 CG HIS A 142 10.695 -50.109 584.917 1.00 32.63 C ANISOU 1076 CG HIS A 142 4568 3852 3979 1667 -818 -148 C ATOM 1077 ND1 HIS A 142 11.369 -50.923 585.802 1.00 32.82 N ANISOU 1077 ND1 HIS A 142 4558 4000 3912 1714 -869 -65 N ATOM 1078 CD2 HIS A 142 11.332 -48.915 584.944 1.00 37.48 C ANISOU 1078 CD2 HIS A 142 5262 4340 4640 1684 -1021 -270 C ATOM 1079 CE1 HIS A 142 12.375 -50.252 586.335 1.00 50.97 C ANISOU 1079 CE1 HIS A 142 6898 6275 6195 1748 -1096 -129 C ATOM 1080 NE2 HIS A 142 12.376 -49.031 585.830 1.00 49.67 N ANISOU 1080 NE2 HIS A 142 6810 5943 6121 1732 -1205 -262 N ATOM 1081 N ARG A 143 6.176 -51.607 584.241 1.00 32.75 N ANISOU 1081 N ARG A 143 4534 4100 3811 1668 -279 -88 N ATOM 1082 CA ARG A 143 4.979 -51.888 583.447 1.00 29.56 C ANISOU 1082 CA ARG A 143 4076 3699 3457 1580 -154 -48 C ATOM 1083 C ARG A 143 3.919 -50.846 583.792 1.00 40.69 C ANISOU 1083 C ARG A 143 5553 5151 4755 1700 -168 -180 C ATOM 1084 O ARG A 143 3.029 -51.060 584.619 1.00 41.68 O ANISOU 1084 O ARG A 143 5705 5438 4693 1843 -123 -203 O ATOM 1085 CB ARG A 143 4.464 -53.297 583.705 1.00 29.54 C ANISOU 1085 CB ARG A 143 4034 3815 3375 1581 -45 74 C ATOM 1086 CG ARG A 143 5.104 -54.372 582.854 1.00 34.81 C ANISOU 1086 CG ARG A 143 4618 4398 4211 1403 -14 191 C ATOM 1087 CD ARG A 143 4.258 -55.636 582.870 1.00 42.60 C ANISOU 1087 CD ARG A 143 5584 5471 5131 1394 95 292 C ATOM 1088 NE ARG A 143 2.959 -55.431 582.232 1.00 35.88 N ANISOU 1088 NE ARG A 143 4722 4631 4281 1363 160 269 N ATOM 1089 CZ ARG A 143 1.955 -56.302 582.271 1.00 46.52 C ANISOU 1089 CZ ARG A 143 6058 6070 5548 1382 259 355 C ATOM 1090 NH1 ARG A 143 2.086 -57.448 582.927 1.00 51.47 N ANISOU 1090 NH1 ARG A 143 6682 6782 6092 1432 318 477 N ATOM 1091 NH2 ARG A 143 0.812 -56.027 581.657 1.00 51.27 N ANISOU 1091 NH2 ARG A 143 6643 6681 6155 1359 301 336 N ATOM 1092 N THR A 144 4.021 -49.694 583.138 1.00 40.64 N ANISOU 1092 N THR A 144 5564 5007 4869 1646 -230 -259 N ATOM 1093 CA THR A 144 3.089 -48.595 583.335 1.00 44.37 C ANISOU 1093 CA THR A 144 6096 5485 5279 1742 -259 -386 C ATOM 1094 C THR A 144 2.346 -48.322 582.034 1.00 38.56 C ANISOU 1094 C THR A 144 5284 4662 4706 1600 -184 -336 C ATOM 1095 O THR A 144 2.924 -48.414 580.946 1.00 41.15 O ANISOU 1095 O THR A 144 5578 4892 5167 1480 -185 -267 O ATOM 1096 CB THR A 144 3.819 -47.331 583.819 1.00 55.71 C ANISOU 1096 CB THR A 144 7649 6825 6695 1833 -429 -541 C ATOM 1097 OG1 THR A 144 2.910 -46.222 583.839 1.00 76.81 O ANISOU 1097 OG1 THR A 144 10370 9471 9346 1904 -458 -658 O ATOM 1098 CG2 THR A 144 5.013 -47.008 582.924 1.00 34.34 C ANISOU 1098 CG2 THR A 144 4923 3944 4181 1684 -494 -491 C ATOM 1099 N VAL A 145 1.055 -47.996 582.152 1.00 40.07 N ANISOU 1099 N VAL A 145 5479 4926 4819 1683 -145 -384 N ATOM 1100 CA VAL A 145 0.238 -47.762 580.964 1.00 33.79 C ANISOU 1100 CA VAL A 145 4652 4089 4098 1632 -107 -352 C ATOM 1101 C VAL A 145 0.860 -46.687 580.088 1.00 30.54 C ANISOU 1101 C VAL A 145 4276 3506 3821 1574 -189 -386 C ATOM 1102 O VAL A 145 0.656 -46.675 578.868 1.00 43.20 O ANISOU 1102 O VAL A 145 5840 5051 5523 1488 -160 -325 O ATOM 1103 CB VAL A 145 -1.203 -47.387 581.364 1.00 28.47 C ANISOU 1103 CB VAL A 145 3975 3521 3320 1758 -70 -414 C ATOM 1104 CG1 VAL A 145 -2.043 -47.117 580.127 1.00 50.11 C ANISOU 1104 CG1 VAL A 145 6680 6215 6143 1714 -40 -380 C ATOM 1105 CG2 VAL A 145 -1.828 -48.487 582.206 1.00 47.47 C ANISOU 1105 CG2 VAL A 145 6332 6113 5591 1809 20 -358 C ATOM 1106 N ALA A 146 1.618 -45.766 580.686 1.00 42.78 N ANISOU 1106 N ALA A 146 5903 4975 5376 1620 -296 -481 N ATOM 1107 CA ALA A 146 2.310 -44.755 579.895 1.00 41.63 C ANISOU 1107 CA ALA A 146 5798 4661 5359 1556 -383 -497 C ATOM 1108 C ALA A 146 3.243 -45.407 578.882 1.00 42.73 C ANISOU 1108 C ALA A 146 5867 4752 5618 1404 -348 -366 C ATOM 1109 O ALA A 146 3.240 -45.053 577.698 1.00 51.54 O ANISOU 1109 O ALA A 146 6960 5791 6833 1329 -339 -316 O ATOM 1110 CB ALA A 146 3.085 -43.813 580.818 1.00 52.40 C ANISOU 1110 CB ALA A 146 7264 5942 6704 1618 -519 -618 C ATOM 1111 N ALA A 147 4.041 -46.377 579.331 1.00 32.82 N ANISOU 1111 N ALA A 147 4572 3550 4349 1369 -325 -308 N ATOM 1112 CA ALA A 147 4.961 -47.056 578.424 1.00 35.58 C ANISOU 1112 CA ALA A 147 4845 3866 4808 1243 -288 -187 C ATOM 1113 C ALA A 147 4.204 -47.864 577.380 1.00 30.57 C ANISOU 1113 C ALA A 147 4135 3278 4203 1176 -183 -106 C ATOM 1114 O ALA A 147 4.538 -47.825 576.190 1.00 34.42 O ANISOU 1114 O ALA A 147 4576 3707 4795 1087 -161 -41 O ATOM 1115 CB ALA A 147 5.906 -47.959 579.215 1.00 45.32 C ANISOU 1115 CB ALA A 147 6049 5151 6018 1240 -294 -143 C ATOM 1116 N ALA A 148 3.178 -48.604 577.807 1.00 47.12 N ANISOU 1116 N ALA A 148 6221 5484 6198 1222 -121 -108 N ATOM 1117 CA ALA A 148 2.401 -49.400 576.864 1.00 26.48 C ANISOU 1117 CA ALA A 148 3552 2912 3596 1161 -42 -44 C ATOM 1118 C ALA A 148 1.900 -48.539 575.715 1.00 34.62 C ANISOU 1118 C ALA A 148 4576 3870 4709 1131 -50 -53 C ATOM 1119 O ALA A 148 1.949 -48.952 574.551 1.00 43.51 O ANISOU 1119 O ALA A 148 5651 4975 5906 1041 -24 4 O ATOM 1120 CB ALA A 148 1.232 -50.074 577.584 1.00 27.16 C ANISOU 1120 CB ALA A 148 3645 3128 3548 1234 21 -44 C ATOM 1121 N HIS A 149 1.419 -47.332 576.022 1.00 30.84 N ANISOU 1121 N HIS A 149 4154 3351 4211 1216 -98 -132 N ATOM 1122 CA AHIS A 149 0.982 -46.422 574.969 0.50 40.21 C ANISOU 1122 CA AHIS A 149 5344 4458 5475 1201 -114 -135 C ATOM 1123 CA BHIS A 149 0.982 -46.424 574.966 0.50 40.45 C ANISOU 1123 CA BHIS A 149 5375 4488 5506 1201 -114 -134 C ATOM 1124 C HIS A 149 2.142 -46.032 574.059 1.00 32.77 C ANISOU 1124 C HIS A 149 4391 3409 4652 1107 -141 -77 C ATOM 1125 O HIS A 149 1.995 -45.997 572.831 1.00 44.84 O ANISOU 1125 O HIS A 149 5876 4906 6255 1043 -109 -15 O ATOM 1126 CB AHIS A 149 0.345 -45.181 575.594 0.50 38.98 C ANISOU 1126 CB AHIS A 149 5269 4270 5271 1327 -180 -244 C ATOM 1127 CB BHIS A 149 0.338 -45.178 575.575 0.50 38.00 C ANISOU 1127 CB BHIS A 149 5145 4145 5148 1326 -180 -243 C ATOM 1128 CG AHIS A 149 0.088 -44.076 574.619 0.50 40.27 C ANISOU 1128 CG AHIS A 149 5458 4324 5519 1324 -222 -250 C ATOM 1129 CG BHIS A 149 -1.157 -45.234 575.625 0.50 42.16 C ANISOU 1129 CG BHIS A 149 5653 4758 5607 1409 -133 -269 C ATOM 1130 ND1AHIS A 149 0.709 -42.849 574.705 0.50 37.13 N ANISOU 1130 ND1AHIS A 149 5146 3797 5163 1346 -331 -307 N ATOM 1131 ND1BHIS A 149 -1.949 -44.893 574.550 0.50 43.25 N ANISOU 1131 ND1BHIS A 149 5762 4865 5804 1396 -115 -241 N ATOM 1132 CD2AHIS A 149 -0.723 -44.012 573.536 0.50 42.06 C ANISOU 1132 CD2AHIS A 149 5642 4545 5793 1302 -182 -203 C ATOM 1133 CD2BHIS A 149 -2.005 -45.589 576.620 0.50 31.90 C ANISOU 1133 CD2BHIS A 149 4354 3584 4183 1513 -99 -313 C ATOM 1134 CE1AHIS A 149 0.291 -42.076 573.719 0.50 45.84 C ANISOU 1134 CE1AHIS A 149 6262 4820 6335 1341 -351 -289 C ATOM 1135 CE1BHIS A 149 -3.220 -45.037 574.879 0.50 45.23 C ANISOU 1135 CE1BHIS A 149 5993 5216 5976 1488 -75 -270 C ATOM 1136 NE2AHIS A 149 -0.577 -42.758 572.994 0.50 42.00 N ANISOU 1136 NE2AHIS A 149 5695 4412 5853 1318 -257 -224 N ATOM 1137 NE2BHIS A 149 -3.282 -45.457 576.130 0.50 38.51 N ANISOU 1137 NE2BHIS A 149 5157 4466 5010 1560 -60 -311 N ATOM 1138 N LYS A 150 3.305 -45.735 574.644 1.00 35.53 N ANISOU 1138 N LYS A 150 4779 3710 5010 1105 -200 -91 N ATOM 1139 CA LYS A 150 4.460 -45.347 573.840 1.00 28.84 C ANISOU 1139 CA LYS A 150 3929 2779 4250 1027 -223 -27 C ATOM 1140 C LYS A 150 4.921 -46.490 572.943 1.00 38.63 C ANISOU 1140 C LYS A 150 5069 4069 5539 937 -121 91 C ATOM 1141 O LYS A 150 5.302 -46.266 571.788 1.00 41.21 O ANISOU 1141 O LYS A 150 5393 4368 5897 891 -86 161 O ATOM 1142 CB LYS A 150 5.596 -44.878 574.750 1.00 47.97 C ANISOU 1142 CB LYS A 150 6412 5148 6667 1043 -327 -73 C ATOM 1143 CG LYS A 150 5.489 -43.403 575.145 1.00 72.37 C ANISOU 1143 CG LYS A 150 9614 8122 9762 1096 -466 -183 C ATOM 1144 CD LYS A 150 5.573 -43.179 576.655 1.00 61.47 C ANISOU 1144 CD LYS A 150 8304 6748 8305 1187 -550 -299 C ATOM 1145 CE LYS A 150 4.607 -42.086 577.110 1.00 80.34 C ANISOU 1145 CE LYS A 150 10789 9087 10651 1296 -625 -429 C ATOM 1146 NZ LYS A 150 3.182 -42.406 576.781 1.00 64.10 N ANISOU 1146 NZ LYS A 150 8690 7121 8546 1352 -521 -422 N ATOM 1147 N VAL A 151 4.892 -47.723 573.453 1.00 34.41 N ANISOU 1147 N VAL A 151 4471 3614 4990 921 -89 100 N ATOM 1148 CA VAL A 151 5.291 -48.866 572.635 1.00 23.80 C ANISOU 1148 CA VAL A 151 3039 2318 3685 810 -77 145 C ATOM 1149 C VAL A 151 4.380 -48.993 571.422 1.00 24.72 C ANISOU 1149 C VAL A 151 3150 2452 3790 770 -104 114 C ATOM 1150 O VAL A 151 4.845 -49.216 570.298 1.00 41.63 O ANISOU 1150 O VAL A 151 5337 4613 5869 738 -170 98 O ATOM 1151 CB VAL A 151 5.288 -50.155 573.476 1.00 20.00 C ANISOU 1151 CB VAL A 151 2559 1908 3132 842 -85 123 C ATOM 1152 CG1 VAL A 151 5.417 -51.376 572.576 1.00 19.17 C ANISOU 1152 CG1 VAL A 151 2461 1871 2953 796 -67 141 C ATOM 1153 CG2 VAL A 151 6.409 -50.123 574.492 1.00 23.72 C ANISOU 1153 CG2 VAL A 151 3027 2365 3622 868 -102 149 C ATOM 1154 N CYS A 152 3.069 -48.852 571.627 1.00 25.20 N ANISOU 1154 N CYS A 152 3232 2530 3811 838 -65 92 N ATOM 1155 CA CYS A 152 2.135 -48.971 570.513 1.00 27.08 C ANISOU 1155 CA CYS A 152 3473 2794 4024 822 -61 88 C ATOM 1156 C CYS A 152 2.466 -47.975 569.409 1.00 34.50 C ANISOU 1156 C CYS A 152 4405 3665 5038 764 -120 96 C ATOM 1157 O CYS A 152 2.434 -48.319 568.221 1.00 28.54 O ANISOU 1157 O CYS A 152 3701 2946 4196 752 -139 101 O ATOM 1158 CB CYS A 152 0.703 -48.767 571.008 1.00 33.80 C ANISOU 1158 CB CYS A 152 4342 3688 4813 898 -12 66 C ATOM 1159 SG CYS A 152 0.091 -50.096 572.070 1.00 28.34 S ANISOU 1159 SG CYS A 152 3668 3130 3969 936 68 81 S ATOM 1160 N LEU A 153 2.798 -46.737 569.780 1.00 33.80 N ANISOU 1160 N LEU A 153 4332 3501 5010 801 -34 163 N ATOM 1161 CA LEU A 153 3.113 -45.730 568.772 1.00 32.95 C ANISOU 1161 CA LEU A 153 4322 3352 4847 830 14 230 C ATOM 1162 C LEU A 153 4.324 -46.139 567.943 1.00 28.83 C ANISOU 1162 C LEU A 153 3933 2882 4140 832 -31 231 C ATOM 1163 O LEU A 153 4.335 -45.968 566.719 1.00 33.11 O ANISOU 1163 O LEU A 153 4491 3399 4692 797 -105 228 O ATOM 1164 CB LEU A 153 3.353 -44.378 569.443 1.00 41.78 C ANISOU 1164 CB LEU A 153 5533 4332 6008 914 -97 172 C ATOM 1165 CG LEU A 153 2.169 -43.818 570.235 1.00 54.36 C ANISOU 1165 CG LEU A 153 7148 5909 7599 995 -151 73 C ATOM 1166 CD1 LEU A 153 2.535 -42.491 570.885 1.00 57.28 C ANISOU 1166 CD1 LEU A 153 7625 6164 7973 1046 -290 -15 C ATOM 1167 CD2 LEU A 153 0.945 -43.661 569.343 1.00 62.56 C ANISOU 1167 CD2 LEU A 153 8156 6955 8660 1013 -116 94 C ATOM 1168 N VAL A 154 5.356 -46.680 568.591 1.00 18.40 N ANISOU 1168 N VAL A 154 2603 1578 2808 820 -55 224 N ATOM 1169 CA VAL A 154 6.523 -47.146 567.850 1.00 19.10 C ANISOU 1169 CA VAL A 154 2656 1656 2945 755 -130 237 C ATOM 1170 C VAL A 154 6.128 -48.256 566.888 1.00 31.04 C ANISOU 1170 C VAL A 154 4079 3233 4483 687 -107 241 C ATOM 1171 O VAL A 154 6.554 -48.273 565.726 1.00 26.43 O ANISOU 1171 O VAL A 154 3434 2657 3951 615 -65 303 O ATOM 1172 CB VAL A 154 7.625 -47.608 568.821 1.00 19.32 C ANISOU 1172 CB VAL A 154 2664 1699 2978 763 -134 245 C ATOM 1173 CG1 VAL A 154 8.730 -48.328 568.061 1.00 23.98 C ANISOU 1173 CG1 VAL A 154 3151 2317 3641 677 -134 295 C ATOM 1174 CG2 VAL A 154 8.183 -46.422 569.586 1.00 24.12 C ANISOU 1174 CG2 VAL A 154 3286 2201 3676 779 -158 274 C ATOM 1175 N LEU A 155 5.309 -49.201 567.352 1.00 23.47 N ANISOU 1175 N LEU A 155 3081 2332 3503 688 -78 207 N ATOM 1176 CA LEU A 155 4.884 -50.290 566.480 1.00 22.38 C ANISOU 1176 CA LEU A 155 2872 2271 3359 622 44 259 C ATOM 1177 C LEU A 155 4.083 -49.765 565.293 1.00 18.40 C ANISOU 1177 C LEU A 155 2371 1757 2865 606 54 276 C ATOM 1178 O LEU A 155 4.274 -50.221 564.160 1.00 22.86 O ANISOU 1178 O LEU A 155 2888 2357 3440 551 129 329 O ATOM 1179 CB LEU A 155 4.073 -51.310 567.279 1.00 19.32 C ANISOU 1179 CB LEU A 155 2475 1942 2923 633 101 250 C ATOM 1180 CG LEU A 155 4.825 -51.978 568.434 1.00 22.16 C ANISOU 1180 CG LEU A 155 2831 2317 3270 650 99 247 C ATOM 1181 CD1 LEU A 155 3.936 -52.985 569.143 1.00 20.65 C ANISOU 1181 CD1 LEU A 155 2642 2184 3020 662 168 261 C ATOM 1182 CD2 LEU A 155 6.106 -52.646 567.945 1.00 35.46 C ANISOU 1182 CD2 LEU A 155 4477 4021 4974 608 146 298 C ATOM 1183 N TRP A 156 3.189 -48.800 565.529 1.00 21.99 N ANISOU 1183 N TRP A 156 2879 2158 3318 666 -29 227 N ATOM 1184 CA TRP A 156 2.447 -48.200 564.422 1.00 20.03 C ANISOU 1184 CA TRP A 156 2642 1889 3081 664 -36 245 C ATOM 1185 C TRP A 156 3.396 -47.555 563.421 1.00 28.08 C ANISOU 1185 C TRP A 156 3665 2865 4137 624 -44 303 C ATOM 1186 O TRP A 156 3.242 -47.723 562.205 1.00 25.17 O ANISOU 1186 O TRP A 156 3253 2523 3787 576 5 354 O ATOM 1187 CB TRP A 156 1.453 -47.163 564.945 1.00 13.87 C ANISOU 1187 CB TRP A 156 1922 1050 2298 747 -136 178 C ATOM 1188 CG TRP A 156 0.137 -47.731 565.380 1.00 18.63 C ANISOU 1188 CG TRP A 156 2463 1697 2919 767 -100 154 C ATOM 1189 CD1 TRP A 156 -0.314 -47.865 566.659 1.00 18.51 C ANISOU 1189 CD1 TRP A 156 2412 1692 2929 800 -90 116 C ATOM 1190 CD2 TRP A 156 -0.904 -48.237 564.533 1.00 19.07 C ANISOU 1190 CD2 TRP A 156 2489 1812 2944 750 -23 193 C ATOM 1191 NE1 TRP A 156 -1.571 -48.423 566.663 1.00 22.30 N ANISOU 1191 NE1 TRP A 156 2871 2243 3359 825 -14 130 N ATOM 1192 CE2 TRP A 156 -1.955 -48.661 565.370 1.00 30.62 C ANISOU 1192 CE2 TRP A 156 3925 3324 4386 789 18 174 C ATOM 1193 CE3 TRP A 156 -1.049 -48.373 563.150 1.00 25.18 C ANISOU 1193 CE3 TRP A 156 3253 2606 3709 706 19 248 C ATOM 1194 CZ2 TRP A 156 -3.132 -49.213 564.870 1.00 18.37 C ANISOU 1194 CZ2 TRP A 156 2350 1836 2794 790 83 206 C ATOM 1195 CZ3 TRP A 156 -2.220 -48.920 562.656 1.00 29.55 C ANISOU 1195 CZ3 TRP A 156 3776 3215 4237 703 78 271 C ATOM 1196 CH2 TRP A 156 -3.245 -49.334 563.515 1.00 14.33 C ANISOU 1196 CH2 TRP A 156 1832 1332 2282 745 105 251 C ATOM 1197 N ALA A 157 4.388 -46.812 563.917 1.00 23.81 N ANISOU 1197 N ALA A 157 3172 2260 3613 640 -96 309 N ATOM 1198 CA ALA A 157 5.365 -46.201 563.024 1.00 16.21 C ANISOU 1198 CA ALA A 157 2184 1256 2721 577 -103 385 C ATOM 1199 C ALA A 157 6.100 -47.263 562.219 1.00 19.91 C ANISOU 1199 C ALA A 157 2537 1810 3217 501 -17 439 C ATOM 1200 O ALA A 157 6.317 -47.101 561.012 1.00 37.28 O ANISOU 1200 O ALA A 157 4694 4018 5452 455 7 504 O ATOM 1201 CB ALA A 157 6.354 -45.357 563.826 1.00 21.81 C ANISOU 1201 CB ALA A 157 2934 1882 3470 583 -160 396 C ATOM 1202 N LEU A 158 6.487 -48.362 562.869 1.00 22.23 N ANISOU 1202 N LEU A 158 2788 2169 3489 498 39 421 N ATOM 1203 CA LEU A 158 7.092 -49.470 562.142 1.00 24.28 C ANISOU 1203 CA LEU A 158 2960 2508 3756 453 145 470 C ATOM 1204 C LEU A 158 6.106 -50.086 561.158 1.00 23.84 C ANISOU 1204 C LEU A 158 2892 2505 3661 442 222 478 C ATOM 1205 O LEU A 158 6.503 -50.524 560.072 1.00 31.13 O ANISOU 1205 O LEU A 158 3767 3468 4593 416 290 529 O ATOM 1206 CB LEU A 158 7.600 -50.522 563.129 1.00 26.46 C ANISOU 1206 CB LEU A 158 3221 2827 4006 465 183 451 C ATOM 1207 CG LEU A 158 8.703 -50.040 564.076 1.00 28.95 C ANISOU 1207 CG LEU A 158 3540 3099 4359 480 109 449 C ATOM 1208 CD1 LEU A 158 8.893 -51.012 565.226 1.00 37.14 C ANISOU 1208 CD1 LEU A 158 4584 4172 5358 511 126 418 C ATOM 1209 CD2 LEU A 158 10.011 -49.845 563.323 1.00 40.15 C ANISOU 1209 CD2 LEU A 158 4881 4522 5851 439 122 530 C ATOM 1210 N ALA A 159 4.821 -50.123 561.516 1.00 18.57 N ANISOU 1210 N ALA A 159 2270 1837 2950 470 209 432 N ATOM 1211 CA ALA A 159 3.816 -50.664 560.608 1.00 15.81 C ANISOU 1211 CA ALA A 159 1912 1530 2566 459 269 444 C ATOM 1212 C ALA A 159 3.628 -49.754 559.401 1.00 18.67 C ANISOU 1212 C ALA A 159 2273 1862 2960 453 236 480 C ATOM 1213 O ALA A 159 3.620 -50.218 558.254 1.00 25.08 O ANISOU 1213 O ALA A 159 3053 2714 3763 432 296 519 O ATOM 1214 CB ALA A 159 2.494 -50.857 561.349 1.00 17.44 C ANISOU 1214 CB ALA A 159 2155 1744 2729 491 257 400 C ATOM 1215 N VAL A 160 3.492 -48.448 559.640 1.00 19.60 N ANISOU 1215 N VAL A 160 2440 1899 3109 479 131 470 N ATOM 1216 CA VAL A 160 3.361 -47.495 558.547 1.00 24.73 C ANISOU 1216 CA VAL A 160 3106 2501 3788 471 84 520 C ATOM 1217 C VAL A 160 4.598 -47.507 557.665 1.00 30.99 C ANISOU 1217 C VAL A 160 3842 3311 4622 419 115 599 C ATOM 1218 O VAL A 160 4.533 -47.092 556.504 1.00 33.52 O ANISOU 1218 O VAL A 160 4156 3625 4953 400 105 663 O ATOM 1219 CB VAL A 160 3.093 -46.081 559.104 1.00 22.13 C ANISOU 1219 CB VAL A 160 2873 2060 3477 518 -35 500 C ATOM 1220 CG1 VAL A 160 3.234 -45.037 558.008 1.00 20.67 C ANISOU 1220 CG1 VAL A 160 2716 1809 3330 495 -86 580 C ATOM 1221 CG2 VAL A 160 1.708 -46.016 559.741 1.00 23.24 C ANISOU 1221 CG2 VAL A 160 3066 2193 3572 595 -65 429 C ATOM 1222 N LEU A 161 5.727 -47.992 558.184 1.00 41.69 N ANISOU 1222 N LEU A 161 5151 4693 5996 401 149 605 N ATOM 1223 CA LEU A 161 6.970 -47.963 557.424 1.00 25.15 C ANISOU 1223 CA LEU A 161 2989 2621 3945 362 175 691 C ATOM 1224 C LEU A 161 7.090 -49.162 556.493 1.00 17.88 C ANISOU 1224 C LEU A 161 2010 1798 2986 367 297 714 C ATOM 1225 O LEU A 161 7.534 -49.016 555.350 1.00 24.05 O ANISOU 1225 O LEU A 161 2753 2607 3777 353 318 792 O ATOM 1226 CB LEU A 161 8.156 -47.913 558.383 1.00 27.88 C ANISOU 1226 CB LEU A 161 3309 2951 4334 350 151 696 C ATOM 1227 CG LEU A 161 9.511 -47.561 557.773 1.00 40.81 C ANISOU 1227 CG LEU A 161 4874 4598 6033 304 145 805 C ATOM 1228 CD1 LEU A 161 9.486 -46.153 557.199 1.00 45.80 C ANISOU 1228 CD1 LEU A 161 5550 5147 6704 253 41 880 C ATOM 1229 CD2 LEU A 161 10.613 -47.706 558.815 1.00 42.22 C ANISOU 1229 CD2 LEU A 161 5018 4773 6253 298 125 806 C ATOM 1230 N ASN A 162 6.697 -50.350 556.955 1.00 17.04 N ANISOU 1230 N ASN A 162 1911 1738 2826 387 372 655 N ATOM 1231 CA ASN A 162 6.747 -51.532 556.104 1.00 30.52 C ANISOU 1231 CA ASN A 162 3601 3513 4483 398 478 669 C ATOM 1232 C ASN A 162 5.646 -51.550 555.053 1.00 31.74 C ANISOU 1232 C ASN A 162 3781 3680 4599 408 485 670 C ATOM 1233 O ASN A 162 5.715 -52.365 554.127 1.00 23.61 O ANISOU 1233 O ASN A 162 2749 2695 3525 425 556 688 O ATOM 1234 CB ASN A 162 6.659 -52.795 556.956 1.00 32.26 C ANISOU 1234 CB ASN A 162 3851 3753 4655 406 529 621 C ATOM 1235 CG ASN A 162 7.789 -52.899 557.944 1.00 28.05 C ANISOU 1235 CG ASN A 162 3293 3210 4153 406 520 627 C ATOM 1236 OD1 ASN A 162 8.481 -51.920 558.214 1.00 31.87 O ANISOU 1236 OD1 ASN A 162 3742 3666 4700 395 461 652 O ATOM 1237 ND2 ASN A 162 7.985 -54.089 558.493 1.00 50.85 N ANISOU 1237 ND2 ASN A 162 6206 6113 7002 419 563 608 N ATOM 1238 N THR A 163 4.635 -50.692 555.178 1.00 22.59 N ANISOU 1238 N THR A 163 2657 2475 3449 406 406 651 N ATOM 1239 CA THR A 163 3.601 -50.563 554.163 1.00 21.93 C ANISOU 1239 CA THR A 163 2596 2397 3338 416 393 664 C ATOM 1240 C THR A 163 3.941 -49.531 553.097 1.00 24.32 C ANISOU 1240 C THR A 163 2894 2678 3670 402 337 749 C ATOM 1241 O THR A 163 3.244 -49.465 552.079 1.00 35.46 O ANISOU 1241 O THR A 163 4324 4100 5050 408 325 779 O ATOM 1242 CB THR A 163 2.269 -50.182 554.812 1.00 28.06 C ANISOU 1242 CB THR A 163 3417 3138 4107 429 333 614 C ATOM 1243 OG1 THR A 163 2.443 -48.997 555.597 1.00 37.26 O ANISOU 1243 OG1 THR A 163 4609 4229 5317 433 241 608 O ATOM 1244 CG2 THR A 163 1.769 -51.305 555.702 1.00 39.76 C ANISOU 1244 CG2 THR A 163 4908 4653 5547 433 386 557 C ATOM 1245 N VAL A 164 4.989 -48.730 553.304 1.00 32.13 N ANISOU 1245 N VAL A 164 3863 3632 4711 375 293 801 N ATOM 1246 CA VAL A 164 5.378 -47.747 552.292 1.00 29.63 C ANISOU 1246 CA VAL A 164 3554 3294 4411 336 233 910 C ATOM 1247 C VAL A 164 5.638 -48.408 550.944 1.00 26.08 C ANISOU 1247 C VAL A 164 3074 2932 3905 340 303 975 C ATOM 1248 O VAL A 164 5.139 -47.901 549.926 1.00 36.99 O ANISOU 1248 O VAL A 164 4493 4312 5250 315 260 1042 O ATOM 1249 CB VAL A 164 6.586 -46.931 552.786 1.00 30.11 C ANISOU 1249 CB VAL A 164 3595 3310 4535 289 179 969 C ATOM 1250 CG1 VAL A 164 7.161 -46.097 551.654 1.00 24.96 C ANISOU 1250 CG1 VAL A 164 2943 2660 3881 219 136 1111 C ATOM 1251 CG2 VAL A 164 6.191 -46.044 553.954 1.00 29.62 C ANISOU 1251 CG2 VAL A 164 3601 3139 4513 293 83 911 C ATOM 1252 N PRO A 165 6.392 -49.507 550.853 1.00 23.71 N ANISOU 1252 N PRO A 165 2719 2708 3582 375 406 963 N ATOM 1253 CA PRO A 165 6.613 -50.120 549.533 1.00 29.89 C ANISOU 1253 CA PRO A 165 3461 3580 4315 412 497 1057 C ATOM 1254 C PRO A 165 5.324 -50.477 548.818 1.00 31.07 C ANISOU 1254 C PRO A 165 3678 3733 4397 430 489 1021 C ATOM 1255 O PRO A 165 5.219 -50.294 547.599 1.00 29.85 O ANISOU 1255 O PRO A 165 3524 3633 4184 418 497 1130 O ATOM 1256 CB PRO A 165 7.442 -51.370 549.864 1.00 19.02 C ANISOU 1256 CB PRO A 165 2015 2264 2949 499 643 1041 C ATOM 1257 CG PRO A 165 8.073 -51.083 551.174 1.00 35.73 C ANISOU 1257 CG PRO A 165 4116 4336 5126 458 601 990 C ATOM 1258 CD PRO A 165 7.098 -50.230 551.924 1.00 34.41 C ANISOU 1258 CD PRO A 165 4033 4076 4966 399 468 904 C ATOM 1259 N TYR A 166 4.329 -50.975 549.553 1.00 33.69 N ANISOU 1259 N TYR A 166 4063 4023 4716 441 467 885 N ATOM 1260 CA TYR A 166 3.080 -51.385 548.925 1.00 27.65 C ANISOU 1260 CA TYR A 166 3348 3261 3896 456 453 859 C ATOM 1261 C TYR A 166 2.300 -50.189 548.400 1.00 25.17 C ANISOU 1261 C TYR A 166 3069 2911 3583 417 346 924 C ATOM 1262 O TYR A 166 1.636 -50.292 547.363 1.00 19.43 O ANISOU 1262 O TYR A 166 2374 2214 2796 416 331 973 O ATOM 1263 CB TYR A 166 2.246 -52.188 549.922 1.00 33.43 C ANISOU 1263 CB TYR A 166 4096 3975 4633 473 479 752 C ATOM 1264 CG TYR A 166 2.957 -53.432 550.402 1.00 24.84 C ANISOU 1264 CG TYR A 166 3005 2910 3522 493 575 703 C ATOM 1265 CD1 TYR A 166 3.853 -53.377 551.460 1.00 17.99 C ANISOU 1265 CD1 TYR A 166 2109 2035 2693 476 598 693 C ATOM 1266 CD2 TYR A 166 2.747 -54.657 549.784 1.00 26.93 C ANISOU 1266 CD2 TYR A 166 3316 3192 3725 527 627 676 C ATOM 1267 CE1 TYR A 166 4.512 -54.508 551.894 1.00 31.46 C ANISOU 1267 CE1 TYR A 166 3834 3750 4370 485 666 668 C ATOM 1268 CE2 TYR A 166 3.401 -55.794 550.212 1.00 26.80 C ANISOU 1268 CE2 TYR A 166 3330 3170 3682 538 687 641 C ATOM 1269 CZ TYR A 166 4.282 -55.714 551.267 1.00 26.58 C ANISOU 1269 CZ TYR A 166 3276 3135 3689 515 704 645 C ATOM 1270 OH TYR A 166 4.934 -56.845 551.692 1.00 29.03 O ANISOU 1270 OH TYR A 166 3626 3426 3979 532 736 622 O ATOM 1271 N PHE A 167 2.371 -49.051 549.093 1.00 24.07 N ANISOU 1271 N PHE A 167 2932 2705 3510 391 274 937 N ATOM 1272 CA PHE A 167 1.735 -47.841 548.586 1.00 32.48 C ANISOU 1272 CA PHE A 167 4047 3716 4577 363 171 1007 C ATOM 1273 C PHE A 167 2.370 -47.391 547.278 1.00 35.58 C ANISOU 1273 C PHE A 167 4454 4150 4913 303 158 1140 C ATOM 1274 O PHE A 167 1.683 -46.843 546.408 1.00 48.73 O ANISOU 1274 O PHE A 167 6169 5813 6535 282 100 1209 O ATOM 1275 CB PHE A 167 1.826 -46.728 549.633 1.00 31.55 C ANISOU 1275 CB PHE A 167 3952 3499 4535 357 95 990 C ATOM 1276 CG PHE A 167 1.083 -45.474 549.260 1.00 31.41 C ANISOU 1276 CG PHE A 167 4006 3402 4527 354 -12 1048 C ATOM 1277 CD1 PHE A 167 1.690 -44.497 548.488 1.00 18.04 C ANISOU 1277 CD1 PHE A 167 2342 1678 2834 292 -63 1173 C ATOM 1278 CD2 PHE A 167 -0.218 -45.266 549.693 1.00 39.83 C ANISOU 1278 CD2 PHE A 167 5109 4426 5598 414 -58 986 C ATOM 1279 CE1 PHE A 167 1.009 -43.341 548.146 1.00 31.84 C ANISOU 1279 CE1 PHE A 167 4162 3342 4595 298 -157 1234 C ATOM 1280 CE2 PHE A 167 -0.904 -44.112 549.355 1.00 34.68 C ANISOU 1280 CE2 PHE A 167 4527 3695 4955 436 -153 1040 C ATOM 1281 CZ PHE A 167 -0.290 -43.149 548.582 1.00 28.27 C ANISOU 1281 CZ PHE A 167 3751 2840 4151 381 -202 1163 C ATOM 1282 N VAL A 168 3.674 -47.616 547.119 1.00 25.03 N ANISOU 1282 N VAL A 168 3074 2869 3568 272 215 1188 N ATOM 1283 CA VAL A 168 4.384 -47.102 545.951 1.00 29.78 C ANISOU 1283 CA VAL A 168 3646 3546 4121 200 225 1360 C ATOM 1284 C VAL A 168 4.035 -47.906 544.706 1.00 36.47 C ANISOU 1284 C VAL A 168 4481 4523 4852 214 297 1420 C ATOM 1285 O VAL A 168 3.756 -47.343 543.641 1.00 45.10 O ANISOU 1285 O VAL A 168 5604 5664 5868 151 259 1526 O ATOM 1286 CB VAL A 168 5.900 -47.105 546.211 1.00 30.75 C ANISOU 1286 CB VAL A 168 3679 3723 4280 168 281 1427 C ATOM 1287 CG1 VAL A 168 6.665 -46.929 544.909 1.00 41.43 C ANISOU 1287 CG1 VAL A 168 4979 5223 5539 89 326 1596 C ATOM 1288 CG2 VAL A 168 6.261 -46.013 547.197 1.00 38.31 C ANISOU 1288 CG2 VAL A 168 4669 4556 5331 123 184 1408 C ATOM 1289 N PHE A 169 4.049 -49.231 544.818 1.00 34.40 N ANISOU 1289 N PHE A 169 4186 4320 4563 298 405 1352 N ATOM 1290 CA PHE A 169 3.894 -50.103 543.664 1.00 29.25 C ANISOU 1290 CA PHE A 169 3538 3807 3767 319 491 1396 C ATOM 1291 C PHE A 169 2.442 -50.472 543.386 1.00 32.16 C ANISOU 1291 C PHE A 169 3975 4148 4097 347 448 1347 C ATOM 1292 O PHE A 169 2.189 -51.353 542.559 1.00 39.59 O ANISOU 1292 O PHE A 169 4939 5198 4905 372 519 1355 O ATOM 1293 CB PHE A 169 4.736 -51.368 543.850 1.00 31.23 C ANISOU 1293 CB PHE A 169 3744 4134 3987 412 639 1346 C ATOM 1294 CG PHE A 169 6.217 -51.121 543.766 1.00 35.37 C ANISOU 1294 CG PHE A 169 4183 4753 4502 379 694 1419 C ATOM 1295 CD1 PHE A 169 6.812 -50.803 542.557 1.00 44.48 C ANISOU 1295 CD1 PHE A 169 5305 6083 5513 292 724 1519 C ATOM 1296 CD2 PHE A 169 7.013 -51.208 544.893 1.00 30.59 C ANISOU 1296 CD2 PHE A 169 3521 4080 4022 427 712 1384 C ATOM 1297 CE1 PHE A 169 8.172 -50.575 542.476 1.00 38.62 C ANISOU 1297 CE1 PHE A 169 4468 5450 4757 251 773 1584 C ATOM 1298 CE2 PHE A 169 8.374 -50.981 544.818 1.00 19.39 C ANISOU 1298 CE2 PHE A 169 2012 2762 2594 391 753 1461 C ATOM 1299 CZ PHE A 169 8.954 -50.666 543.610 1.00 24.17 C ANISOU 1299 CZ PHE A 169 2578 3547 3059 299 784 1558 C ATOM 1300 N ARG A 170 1.487 -49.816 544.041 1.00 30.56 N ANISOU 1300 N ARG A 170 3809 3818 3985 341 335 1290 N ATOM 1301 CA ARG A 170 0.083 -50.002 543.703 1.00 30.90 C ANISOU 1301 CA ARG A 170 3900 3850 3992 358 279 1269 C ATOM 1302 C ARG A 170 -0.237 -49.149 542.486 1.00 30.01 C ANISOU 1302 C ARG A 170 3819 3795 3789 288 208 1402 C ATOM 1303 O ARG A 170 -0.064 -47.926 542.517 1.00 46.09 O ANISOU 1303 O ARG A 170 5875 5767 5872 241 128 1454 O ATOM 1304 CB ARG A 170 -0.825 -49.623 544.869 1.00 21.51 C ANISOU 1304 CB ARG A 170 2730 2533 2908 384 194 1149 C ATOM 1305 CG ARG A 170 -1.243 -50.791 545.761 1.00 40.61 C ANISOU 1305 CG ARG A 170 5133 4935 5361 442 250 1019 C ATOM 1306 CD ARG A 170 -1.987 -51.903 545.026 1.00 20.94 C ANISOU 1306 CD ARG A 170 2657 2507 2792 478 295 1042 C ATOM 1307 NE ARG A 170 -1.642 -53.207 545.588 1.00 28.64 N ANISOU 1307 NE ARG A 170 3630 3473 3777 533 402 957 N ATOM 1308 CZ ARG A 170 -2.489 -54.220 545.746 1.00 28.97 C ANISOU 1308 CZ ARG A 170 3701 3500 3808 567 419 905 C ATOM 1309 NH1 ARG A 170 -3.765 -54.101 545.399 1.00 34.17 N ANISOU 1309 NH1 ARG A 170 4367 4170 4445 554 338 939 N ATOM 1310 NH2 ARG A 170 -2.059 -55.360 546.267 1.00 21.87 N ANISOU 1310 NH2 ARG A 170 2823 2567 2920 612 512 826 N ATOM 1311 N ASP A 171 -0.694 -49.789 541.418 1.00 30.06 N ANISOU 1311 N ASP A 171 3842 3927 3651 281 235 1453 N ATOM 1312 CA ASP A 171 -1.026 -49.092 540.188 1.00 30.94 C ANISOU 1312 CA ASP A 171 3982 4124 3651 211 171 1577 C ATOM 1313 C ASP A 171 -2.367 -49.595 539.676 1.00 26.39 C ANISOU 1313 C ASP A 171 3435 3597 2994 233 121 1572 C ATOM 1314 O ASP A 171 -2.868 -50.642 540.097 1.00 24.89 O ANISOU 1314 O ASP A 171 3247 3407 2804 291 159 1487 O ATOM 1315 CB ASP A 171 0.059 -49.292 539.123 1.00 36.80 C ANISOU 1315 CB ASP A 171 4704 5048 4231 145 262 1660 C ATOM 1316 CG ASP A 171 -0.048 -48.296 537.986 1.00 44.20 C ANISOU 1316 CG ASP A 171 5660 6057 5076 57 190 1799 C ATOM 1317 OD1 ASP A 171 -0.883 -47.372 538.077 1.00 47.81 O ANISOU 1317 OD1 ASP A 171 6151 6401 5614 57 68 1837 O ATOM 1318 OD2 ASP A 171 0.701 -48.441 536.997 1.00 43.16 O ANISOU 1318 OD2 ASP A 171 5508 6103 4786 -5 261 1864 O ATOM 1319 N THR A 172 -2.949 -48.819 538.770 1.00 28.06 N ANISOU 1319 N THR A 172 3670 3851 3138 187 29 1672 N ATOM 1320 CA THR A 172 -4.190 -49.182 538.102 1.00 25.62 C ANISOU 1320 CA THR A 172 3380 3625 2731 193 -38 1692 C ATOM 1321 C THR A 172 -3.857 -49.726 536.718 1.00 35.84 C ANISOU 1321 C THR A 172 4695 5142 3782 125 12 1750 C ATOM 1322 O THR A 172 -3.301 -49.006 535.882 1.00 53.87 O ANISOU 1322 O THR A 172 6981 7497 5988 57 6 1850 O ATOM 1323 CB THR A 172 -5.126 -47.978 538.001 1.00 24.52 C ANISOU 1323 CB THR A 172 3250 3399 2666 203 -176 1754 C ATOM 1324 OG1 THR A 172 -4.363 -46.800 537.713 1.00 31.37 O ANISOU 1324 OG1 THR A 172 4137 4224 3560 154 -198 1845 O ATOM 1325 CG2 THR A 172 -5.884 -47.778 539.299 1.00 30.15 C ANISOU 1325 CG2 THR A 172 3950 3949 3559 291 -222 1648 C ATOM 1326 N ILE A 173 -4.189 -50.993 536.483 1.00 31.78 N ANISOU 1326 N ILE A 173 4201 4744 3132 140 63 1676 N ATOM 1327 CA ILE A 173 -3.921 -51.666 535.217 1.00 37.02 C ANISOU 1327 CA ILE A 173 4902 5640 3526 84 120 1669 C ATOM 1328 C ILE A 173 -5.249 -51.929 534.522 1.00 30.30 C ANISOU 1328 C ILE A 173 4076 4887 2551 57 3 1678 C ATOM 1329 O ILE A 173 -6.181 -52.467 535.133 1.00 49.61 O ANISOU 1329 O ILE A 173 6516 7278 5057 96 -50 1626 O ATOM 1330 CB ILE A 173 -3.142 -52.977 535.423 1.00 40.85 C ANISOU 1330 CB ILE A 173 5410 6201 3909 126 280 1530 C ATOM 1331 CG1 ILE A 173 -1.678 -52.686 535.767 1.00 41.31 C ANISOU 1331 CG1 ILE A 173 5423 6230 4042 136 396 1535 C ATOM 1332 CG2 ILE A 173 -3.228 -53.848 534.173 1.00 55.49 C ANISOU 1332 CG2 ILE A 173 7326 8295 5462 88 319 1451 C ATOM 1333 CD1 ILE A 173 -1.475 -52.053 537.120 1.00 36.41 C ANISOU 1333 CD1 ILE A 173 4755 5380 3697 179 367 1554 C ATOM 1334 N SER A 174 -5.333 -51.560 533.247 1.00 33.57 N ANISOU 1334 N SER A 174 4509 5456 2790 -14 -41 1749 N ATOM 1335 CA SER A 174 -6.553 -51.728 532.471 1.00 45.05 C ANISOU 1335 CA SER A 174 5979 7023 4115 -51 -168 1763 C ATOM 1336 C SER A 174 -6.604 -53.130 531.878 1.00 39.61 C ANISOU 1336 C SER A 174 5354 6524 3171 -81 -116 1612 C ATOM 1337 O SER A 174 -5.648 -53.576 531.237 1.00 53.43 O ANISOU 1337 O SER A 174 7147 8407 4747 -98 5 1542 O ATOM 1338 CB SER A 174 -6.633 -50.685 531.354 1.00 42.32 C ANISOU 1338 CB SER A 174 5630 6756 3692 -110 -244 1903 C ATOM 1339 OG SER A 174 -6.719 -49.375 531.883 1.00 71.34 O ANISOU 1339 OG SER A 174 9269 10247 7591 -80 -311 2019 O ATOM 1340 N ARG A 175 -7.715 -53.822 532.105 1.00 42.84 N ANISOU 1340 N ARG A 175 5769 6948 3559 -88 -210 1545 N ATOM 1341 CA ARG A 175 -7.974 -55.104 531.472 1.00 45.96 C ANISOU 1341 CA ARG A 175 6244 7518 3699 -141 -206 1375 C ATOM 1342 C ARG A 175 -8.604 -54.894 530.097 1.00 52.74 C ANISOU 1342 C ARG A 175 7125 8551 4363 -224 -321 1405 C ATOM 1343 O ARG A 175 -9.061 -53.802 529.752 1.00 53.16 O ANISOU 1343 O ARG A 175 7121 8583 4494 -233 -419 1571 O ATOM 1344 CB ARG A 175 -8.885 -55.960 532.354 1.00 48.15 C ANISOU 1344 CB ARG A 175 6515 7652 4129 -135 -264 1226 C ATOM 1345 CG ARG A 175 -8.149 -56.784 533.399 1.00 48.89 C ANISOU 1345 CG ARG A 175 6639 7555 4383 -62 -117 1048 C ATOM 1346 CD ARG A 175 -9.079 -57.246 534.515 1.00 55.70 C ANISOU 1346 CD ARG A 175 7459 8231 5472 -53 -181 977 C ATOM 1347 NE ARG A 175 -8.543 -58.403 535.230 1.00 94.89 N ANISOU 1347 NE ARG A 175 12489 13043 10520 -17 -68 766 N ATOM 1348 CZ ARG A 175 -9.023 -58.869 536.381 1.00 98.95 C ANISOU 1348 CZ ARG A 175 12973 13379 11245 0 -79 708 C ATOM 1349 NH1 ARG A 175 -10.054 -58.275 536.970 1.00 78.24 N ANISOU 1349 NH1 ARG A 175 10240 10722 8765 -7 -184 832 N ATOM 1350 NH2 ARG A 175 -8.466 -59.932 536.951 1.00 71.93 N ANISOU 1350 NH2 ARG A 175 9626 9819 7886 32 18 531 N ATOM 1351 N LEU A 176 -8.615 -55.963 529.297 1.00 54.47 N ANISOU 1351 N LEU A 176 7438 8934 4323 -277 -308 1223 N ATOM 1352 CA LEU A 176 -9.313 -55.914 528.018 1.00 52.60 C ANISOU 1352 CA LEU A 176 7229 8864 3891 -357 -429 1228 C ATOM 1353 C LEU A 176 -10.825 -55.877 528.196 1.00 53.68 C ANISOU 1353 C LEU A 176 7307 8982 4106 -410 -630 1272 C ATOM 1354 O LEU A 176 -11.530 -55.381 527.311 1.00 65.69 O ANISOU 1354 O LEU A 176 8803 10602 5555 -456 -753 1360 O ATOM 1355 CB LEU A 176 -8.920 -57.113 527.153 1.00 71.12 C ANISOU 1355 CB LEU A 176 9705 11366 5952 -389 -366 983 C ATOM 1356 CG LEU A 176 -7.476 -57.148 526.645 1.00 77.26 C ANISOU 1356 CG LEU A 176 10527 12218 6611 -329 -172 932 C ATOM 1357 CD1 LEU A 176 -7.230 -58.416 525.841 1.00 68.73 C ANISOU 1357 CD1 LEU A 176 9585 11264 5265 -332 -122 650 C ATOM 1358 CD2 LEU A 176 -7.155 -55.916 525.810 1.00 71.51 C ANISOU 1358 CD2 LEU A 176 9739 11572 5859 -349 -176 1154 C ATOM 1359 N ASP A 177 -11.334 -56.369 529.328 1.00 59.41 N ANISOU 1359 N ASP A 177 7999 9591 4983 -405 -665 1222 N ATOM 1360 CA ASP A 177 -12.766 -56.363 529.594 1.00 52.04 C ANISOU 1360 CA ASP A 177 6979 8646 4148 -455 -849 1265 C ATOM 1361 C ASP A 177 -13.337 -54.957 529.713 1.00 56.67 C ANISOU 1361 C ASP A 177 7438 9160 4933 -386 -928 1491 C ATOM 1362 O ASP A 177 -14.560 -54.809 529.805 1.00 63.76 O ANISOU 1362 O ASP A 177 8243 10071 5913 -406 -1074 1537 O ATOM 1363 CB ASP A 177 -13.061 -57.124 530.896 1.00 52.64 C ANISOU 1363 CB ASP A 177 7026 8507 4466 -432 -815 1127 C ATOM 1364 CG ASP A 177 -12.391 -58.485 530.950 1.00 70.62 C ANISOU 1364 CG ASP A 177 9441 10706 6684 -453 -696 847 C ATOM 1365 OD1 ASP A 177 -11.144 -58.534 531.007 1.00 66.90 O ANISOU 1365 OD1 ASP A 177 9036 10198 6186 -376 -527 797 O ATOM 1366 OD2 ASP A 177 -13.113 -59.505 530.947 1.00 98.80 O ANISOU 1366 OD2 ASP A 177 13050 14249 10242 -546 -777 681 O ATOM 1367 N GLY A 178 -12.491 -53.929 529.714 1.00 48.44 N ANISOU 1367 N GLY A 178 6391 8037 3975 -309 -836 1615 N ATOM 1368 CA GLY A 178 -12.875 -52.632 530.214 1.00 56.14 C ANISOU 1368 CA GLY A 178 7272 8866 5193 -225 -886 1780 C ATOM 1369 C GLY A 178 -12.742 -52.499 531.712 1.00 48.03 C ANISOU 1369 C GLY A 178 6191 7630 4427 -130 -828 1775 C ATOM 1370 O GLY A 178 -12.924 -51.395 532.241 1.00 59.83 O ANISOU 1370 O GLY A 178 7627 8975 6131 -45 -850 1871 O ATOM 1371 N ARG A 179 -12.434 -53.588 532.413 1.00 32.67 N ANISOU 1371 N ARG A 179 4275 5670 2469 -141 -755 1652 N ATOM 1372 CA ARG A 179 -12.205 -53.533 533.847 1.00 51.25 C ANISOU 1372 CA ARG A 179 6583 7830 5060 -49 -684 1645 C ATOM 1373 C ARG A 179 -10.859 -52.890 534.152 1.00 39.75 C ANISOU 1373 C ARG A 179 5168 6247 3690 13 -542 1677 C ATOM 1374 O ARG A 179 -9.880 -53.061 533.420 1.00 50.26 O ANISOU 1374 O ARG A 179 6573 7669 4856 -29 -452 1657 O ATOM 1375 CB ARG A 179 -12.240 -54.936 534.449 1.00 47.94 C ANISOU 1375 CB ARG A 179 6197 7370 4649 -83 -622 1443 C ATOM 1376 CG ARG A 179 -13.595 -55.619 534.424 1.00 33.00 C ANISOU 1376 CG ARG A 179 4247 5537 2755 -161 -754 1369 C ATOM 1377 CD ARG A 179 -13.491 -56.992 535.077 1.00 49.15 C ANISOU 1377 CD ARG A 179 6348 7465 4862 -204 -672 1139 C ATOM 1378 NE ARG A 179 -14.791 -57.529 535.471 1.00 70.58 N ANISOU 1378 NE ARG A 179 8973 10189 7657 -276 -787 1102 N ATOM 1379 CZ ARG A 179 -15.461 -58.473 534.814 1.00 84.22 C ANISOU 1379 CZ ARG A 179 10737 12011 9251 -420 -884 985 C ATOM 1380 NH1 ARG A 179 -16.636 -58.880 535.275 1.00 78.55 N ANISOU 1380 NH1 ARG A 179 9911 11307 8629 -495 -988 979 N ATOM 1381 NH2 ARG A 179 -14.969 -59.017 533.706 1.00 87.03 N ANISOU 1381 NH2 ARG A 179 11236 12458 9374 -494 -880 871 N ATOM 1382 N ILE A 180 -10.813 -52.155 535.257 1.00 46.79 N ANISOU 1382 N ILE A 180 6006 6935 4838 108 -522 1706 N ATOM 1383 CA ILE A 180 -9.590 -51.530 535.745 1.00 31.72 C ANISOU 1383 CA ILE A 180 4125 4885 3044 151 -409 1715 C ATOM 1384 C ILE A 180 -9.151 -52.296 536.982 1.00 26.61 C ANISOU 1384 C ILE A 180 3474 4123 2513 207 -305 1619 C ATOM 1385 O ILE A 180 -9.916 -52.428 537.945 1.00 44.18 O ANISOU 1385 O ILE A 180 5642 6254 4892 264 -341 1582 O ATOM 1386 CB ILE A 180 -9.795 -50.039 536.052 1.00 27.08 C ANISOU 1386 CB ILE A 180 3505 4144 2639 205 -473 1787 C ATOM 1387 CG1 ILE A 180 -10.184 -49.291 534.771 1.00 33.25 C ANISOU 1387 CG1 ILE A 180 4299 5035 3298 154 -571 1902 C ATOM 1388 CG2 ILE A 180 -8.533 -49.447 536.663 1.00 26.10 C ANISOU 1388 CG2 ILE A 180 3411 3877 2631 224 -377 1774 C ATOM 1389 CD1 ILE A 180 -10.498 -47.825 534.978 1.00 33.36 C ANISOU 1389 CD1 ILE A 180 4304 4904 3466 213 -649 1975 C ATOM 1390 N MET A 181 -7.930 -52.816 536.950 1.00 27.74 N ANISOU 1390 N MET A 181 3672 4287 2581 198 -169 1574 N ATOM 1391 CA MET A 181 -7.366 -53.518 538.089 1.00 27.27 C ANISOU 1391 CA MET A 181 3618 4111 2634 265 -54 1487 C ATOM 1392 C MET A 181 -6.660 -52.535 539.011 1.00 32.03 C ANISOU 1392 C MET A 181 4186 4522 3462 313 -22 1484 C ATOM 1393 O MET A 181 -6.210 -51.468 538.588 1.00 31.70 O ANISOU 1393 O MET A 181 4142 4468 3433 280 -51 1551 O ATOM 1394 CB MET A 181 -6.377 -54.594 537.637 1.00 26.78 C ANISOU 1394 CB MET A 181 3629 4124 2424 239 87 1332 C ATOM 1395 CG MET A 181 -6.999 -55.726 536.842 1.00 43.16 C ANISOU 1395 CG MET A 181 5764 6310 4325 171 56 1172 C ATOM 1396 SD MET A 181 -5.894 -57.146 536.697 1.00 45.33 S ANISOU 1396 SD MET A 181 6139 6588 4497 193 223 927 S ATOM 1397 CE MET A 181 -4.524 -56.432 535.791 1.00 33.00 C ANISOU 1397 CE MET A 181 4571 5207 2761 199 332 1041 C ATOM 1398 N CYS A 182 -6.584 -52.903 540.287 1.00 27.76 N ANISOU 1398 N CYS A 182 3624 3837 3085 380 28 1397 N ATOM 1399 CA CYS A 182 -5.783 -52.196 541.286 1.00 27.53 C ANISOU 1399 CA CYS A 182 3571 3655 3235 411 64 1343 C ATOM 1400 C CYS A 182 -4.912 -53.263 541.937 1.00 25.21 C ANISOU 1400 C CYS A 182 3295 3326 2960 454 200 1256 C ATOM 1401 O CYS A 182 -5.384 -54.024 542.787 1.00 27.71 O ANISOU 1401 O CYS A 182 3607 3568 3353 502 220 1176 O ATOM 1402 CB CYS A 182 -6.664 -51.473 542.303 1.00 38.94 C ANISOU 1402 CB CYS A 182 4974 4977 4847 451 -20 1283 C ATOM 1403 SG CYS A 182 -5.836 -50.934 543.828 1.00 27.22 S ANISOU 1403 SG CYS A 182 3479 3340 3525 475 20 1153 S ATOM 1404 N TYR A 183 -3.650 -53.334 541.526 1.00 18.49 N ANISOU 1404 N TYR A 183 2460 2531 2036 440 295 1273 N ATOM 1405 CA TYR A 183 -2.804 -54.460 541.897 1.00 24.12 C ANISOU 1405 CA TYR A 183 3205 3235 2723 500 441 1195 C ATOM 1406 C TYR A 183 -1.346 -54.041 541.780 1.00 27.28 C ANISOU 1406 C TYR A 183 3569 3675 3121 488 518 1215 C ATOM 1407 O TYR A 183 -1.028 -52.935 541.333 1.00 25.36 O ANISOU 1407 O TYR A 183 3289 3466 2879 418 455 1301 O ATOM 1408 CB TYR A 183 -3.109 -55.672 541.013 1.00 37.61 C ANISOU 1408 CB TYR A 183 4986 5061 4243 480 484 1087 C ATOM 1409 CG TYR A 183 -2.718 -57.005 541.607 1.00 29.84 C ANISOU 1409 CG TYR A 183 4047 3992 3299 534 577 891 C ATOM 1410 CD1 TYR A 183 -3.370 -57.507 542.724 1.00 29.85 C ANISOU 1410 CD1 TYR A 183 4048 3836 3457 564 547 822 C ATOM 1411 CD2 TYR A 183 -1.714 -57.774 541.034 1.00 35.86 C ANISOU 1411 CD2 TYR A 183 4852 4838 3936 561 693 778 C ATOM 1412 CE1 TYR A 183 -3.022 -58.730 543.264 1.00 39.53 C ANISOU 1412 CE1 TYR A 183 5327 4968 4725 606 618 663 C ATOM 1413 CE2 TYR A 183 -1.360 -58.998 541.566 1.00 34.55 C ANISOU 1413 CE2 TYR A 183 4739 4572 3816 627 765 601 C ATOM 1414 CZ TYR A 183 -2.019 -59.473 542.679 1.00 30.96 C ANISOU 1414 CZ TYR A 183 4297 3939 3529 642 721 551 C ATOM 1415 OH TYR A 183 -1.668 -60.693 543.210 1.00 18.98 O ANISOU 1415 OH TYR A 183 2844 2305 2062 701 779 395 O ATOM 1416 N TYR A 184 -0.459 -54.949 542.187 1.00 33.68 N ANISOU 1416 N TYR A 184 4394 4476 3928 559 654 1137 N ATOM 1417 CA TYR A 184 0.971 -54.678 542.155 1.00 23.78 C ANISOU 1417 CA TYR A 184 3081 3278 2676 558 731 1152 C ATOM 1418 C TYR A 184 1.404 -54.234 540.764 1.00 28.22 C ANISOU 1418 C TYR A 184 3627 4041 3053 473 739 1231 C ATOM 1419 O TYR A 184 0.881 -54.697 539.747 1.00 37.96 O ANISOU 1419 O TYR A 184 4917 5410 4096 451 753 1214 O ATOM 1420 CB TYR A 184 1.769 -55.924 542.550 1.00 30.60 C ANISOU 1420 CB TYR A 184 3967 4139 3520 661 886 1030 C ATOM 1421 CG TYR A 184 1.533 -56.418 543.956 1.00 25.59 C ANISOU 1421 CG TYR A 184 3350 3306 3067 740 887 959 C ATOM 1422 CD1 TYR A 184 2.277 -55.927 545.018 1.00 33.88 C ANISOU 1422 CD1 TYR A 184 4322 4266 4286 763 869 964 C ATOM 1423 CD2 TYR A 184 0.579 -57.391 544.220 1.00 38.97 C ANISOU 1423 CD2 TYR A 184 5116 4912 4781 759 855 823 C ATOM 1424 CE1 TYR A 184 2.069 -56.382 546.307 1.00 33.43 C ANISOU 1424 CE1 TYR A 184 4261 4090 4351 779 860 850 C ATOM 1425 CE2 TYR A 184 0.363 -57.852 545.504 1.00 28.17 C ANISOU 1425 CE2 TYR A 184 3754 3375 3573 815 845 763 C ATOM 1426 CZ TYR A 184 1.112 -57.344 546.543 1.00 32.00 C ANISOU 1426 CZ TYR A 184 4160 3840 4160 777 836 753 C ATOM 1427 OH TYR A 184 0.903 -57.800 547.823 1.00 34.09 O ANISOU 1427 OH TYR A 184 4421 4050 4483 685 761 634 O ATOM 1428 N ASN A 185 2.378 -53.320 540.728 1.00 35.09 N ANISOU 1428 N ASN A 185 4423 4937 3971 417 726 1312 N ATOM 1429 CA ASN A 185 3.057 -52.919 539.495 1.00 26.39 C ANISOU 1429 CA ASN A 185 3292 4030 2704 332 754 1388 C ATOM 1430 C ASN A 185 4.543 -52.849 539.845 1.00 36.72 C ANISOU 1430 C ASN A 185 4513 5380 4061 343 835 1391 C ATOM 1431 O ASN A 185 5.095 -51.780 540.119 1.00 31.28 O ANISOU 1431 O ASN A 185 3769 4646 3471 272 772 1494 O ATOM 1432 CB ASN A 185 2.532 -51.594 538.951 1.00 40.46 C ANISOU 1432 CB ASN A 185 5082 5795 4495 220 615 1528 C ATOM 1433 CG ASN A 185 3.111 -51.253 537.591 1.00 46.70 C ANISOU 1433 CG ASN A 185 5854 6792 5096 130 647 1613 C ATOM 1434 OD1 ASN A 185 4.138 -51.797 537.183 1.00 38.38 O ANISOU 1434 OD1 ASN A 185 4755 5894 3933 142 771 1573 O ATOM 1435 ND2 ASN A 185 2.453 -50.344 536.881 1.00 47.65 N ANISOU 1435 ND2 ASN A 185 6007 6918 5180 49 537 1725 N ATOM 1436 N VAL A 186 5.189 -54.015 539.837 1.00 45.69 N ANISOU 1436 N VAL A 186 5639 6597 5125 435 968 1262 N ATOM 1437 CA VAL A 186 6.589 -54.102 540.240 1.00 42.12 C ANISOU 1437 CA VAL A 186 5093 6186 4724 466 1040 1248 C ATOM 1438 C VAL A 186 7.450 -53.168 539.398 1.00 50.64 C ANISOU 1438 C VAL A 186 6092 7428 5722 347 1035 1380 C ATOM 1439 O VAL A 186 8.337 -52.479 539.918 1.00 48.01 O ANISOU 1439 O VAL A 186 5675 7071 5494 305 1013 1464 O ATOM 1440 CB VAL A 186 7.068 -55.563 540.141 1.00 47.30 C ANISOU 1440 CB VAL A 186 5765 6909 5297 591 1166 1056 C ATOM 1441 CG1 VAL A 186 8.579 -55.630 540.073 1.00 48.95 C ANISOU 1441 CG1 VAL A 186 5865 7242 5493 605 1239 1047 C ATOM 1442 CG2 VAL A 186 6.544 -56.373 541.320 1.00 25.25 C ANISOU 1442 CG2 VAL A 186 3039 3907 2649 703 1160 943 C ATOM 1443 N LEU A 187 7.202 -53.124 538.092 1.00 50.42 N ANISOU 1443 N LEU A 187 6090 7567 5500 285 1052 1405 N ATOM 1444 CA LEU A 187 8.000 -52.317 537.177 1.00 47.91 C ANISOU 1444 CA LEU A 187 5701 7418 5083 174 1061 1533 C ATOM 1445 C LEU A 187 7.561 -50.858 537.129 1.00 44.30 C ANISOU 1445 C LEU A 187 5256 6864 4711 44 916 1717 C ATOM 1446 O LEU A 187 7.980 -50.133 536.221 1.00 43.31 O ANISOU 1446 O LEU A 187 5096 6870 4491 -60 906 1842 O ATOM 1447 CB LEU A 187 7.937 -52.912 535.767 1.00 43.77 C ANISOU 1447 CB LEU A 187 5207 7120 4305 173 1143 1473 C ATOM 1448 CG LEU A 187 8.270 -54.399 535.634 1.00 35.19 C ANISOU 1448 CG LEU A 187 4137 6120 3114 311 1277 1251 C ATOM 1449 CD1 LEU A 187 7.969 -54.876 534.224 1.00 58.16 C ANISOU 1449 CD1 LEU A 187 7104 9227 5765 303 1329 1182 C ATOM 1450 CD2 LEU A 187 9.721 -54.672 535.995 1.00 48.18 C ANISOU 1450 CD2 LEU A 187 5665 7836 4806 366 1371 1212 C ATOM 1451 N LEU A 188 6.735 -50.410 538.078 1.00 46.08 N ANISOU 1451 N LEU A 188 5534 6859 5114 56 802 1727 N ATOM 1452 CA LEU A 188 6.245 -49.037 538.034 1.00 45.44 C ANISOU 1452 CA LEU A 188 5485 6662 5120 -45 656 1862 C ATOM 1453 C LEU A 188 7.385 -48.031 538.104 1.00 45.89 C ANISOU 1453 C LEU A 188 5461 6738 5237 -144 634 1989 C ATOM 1454 O LEU A 188 7.282 -46.940 537.533 1.00 57.42 O ANISOU 1454 O LEU A 188 6937 8192 6689 -249 548 2124 O ATOM 1455 CB LEU A 188 5.258 -48.791 539.177 1.00 34.44 C ANISOU 1455 CB LEU A 188 4154 5019 3914 9 548 1804 C ATOM 1456 CG LEU A 188 4.616 -47.401 539.215 1.00 26.03 C ANISOU 1456 CG LEU A 188 3141 3805 2943 -62 393 1895 C ATOM 1457 CD1 LEU A 188 3.569 -47.267 538.124 1.00 49.90 C ANISOU 1457 CD1 LEU A 188 6229 6890 5842 -88 341 1946 C ATOM 1458 CD2 LEU A 188 4.010 -47.118 540.581 1.00 53.86 C ANISOU 1458 CD2 LEU A 188 6705 7101 6660 3 309 1798 C ATOM 1459 N LEU A 189 8.472 -48.368 538.797 1.00 38.38 N ANISOU 1459 N LEU A 189 4423 5811 4348 -112 705 1954 N ATOM 1460 CA LEU A 189 9.577 -47.440 538.981 1.00 60.74 C ANISOU 1460 CA LEU A 189 7170 8662 7247 -212 676 2077 C ATOM 1461 C LEU A 189 10.905 -48.178 538.907 1.00 71.11 C ANISOU 1461 C LEU A 189 8360 10171 8489 -180 814 2049 C ATOM 1462 O LEU A 189 11.017 -49.336 539.319 1.00 71.46 O ANISOU 1462 O LEU A 189 8394 10237 8521 -51 909 1906 O ATOM 1463 CB LEU A 189 9.464 -46.694 540.319 1.00 52.50 C ANISOU 1463 CB LEU A 189 6152 7372 6425 -216 559 2073 C ATOM 1464 CG LEU A 189 8.396 -45.598 540.342 1.00 70.33 C ANISOU 1464 CG LEU A 189 8519 9444 8758 -265 407 2115 C ATOM 1465 CD1 LEU A 189 7.187 -46.034 541.154 1.00 79.23 C ANISOU 1465 CD1 LEU A 189 9736 10398 9971 -150 366 1967 C ATOM 1466 CD2 LEU A 189 8.968 -44.290 540.875 1.00 65.82 C ANISOU 1466 CD2 LEU A 189 7938 8752 8317 -366 299 2212 C ATOM 1467 N ASN A 190 11.918 -47.471 538.387 1.00 77.15 N ANISOU 1467 N ASN A 190 9030 11075 9210 -296 820 2189 N ATOM 1468 CA ASN A 190 13.278 -47.959 538.168 1.00 81.03 C ANISOU 1468 CA ASN A 190 9381 11786 9621 -286 943 2190 C ATOM 1469 C ASN A 190 13.307 -49.460 537.901 1.00 74.30 C ANISOU 1469 C ASN A 190 8527 11059 8643 -129 1091 2005 C ATOM 1470 O ASN A 190 13.835 -50.229 538.715 1.00 78.65 O ANISOU 1470 O ASN A 190 9034 11587 9262 -20 1149 1895 O ATOM 1471 CB ASN A 190 14.173 -47.610 539.363 1.00 91.95 C ANISOU 1471 CB ASN A 190 10682 13081 11175 -302 903 2222 C ATOM 1472 CG ASN A 190 13.515 -47.902 540.697 1.00102.55 C ANISOU 1472 CG ASN A 190 12101 14173 12688 -202 844 2109 C ATOM 1473 OD1 ASN A 190 13.730 -48.959 541.292 1.00113.75 O ANISOU 1473 OD1 ASN A 190 13500 15596 14125 -67 925 1977 O ATOM 1474 ND2 ASN A 190 12.712 -46.958 541.181 1.00 94.98 N ANISOU 1474 ND2 ASN A 190 11235 12996 11856 -260 701 2152 N ATOM 1475 N PRO A 191 12.755 -49.913 536.779 1.00 65.11 N ANISOU 1475 N PRO A 191 7418 10022 7298 -111 1147 1960 N ATOM 1476 CA PRO A 191 12.861 -51.331 536.423 1.00 41.40 C ANISOU 1476 CA PRO A 191 4424 7144 4164 34 1286 1767 C ATOM 1477 C PRO A 191 14.279 -51.685 536.006 1.00 73.25 C ANISOU 1477 C PRO A 191 8314 11414 8102 59 1409 1755 C ATOM 1478 O PRO A 191 15.086 -50.826 535.643 1.00 91.45 O ANISOU 1478 O PRO A 191 10512 13847 10386 -59 1399 1920 O ATOM 1479 CB PRO A 191 11.882 -51.478 535.256 1.00 53.33 C ANISOU 1479 CB PRO A 191 6035 8733 5496 14 1288 1749 C ATOM 1480 CG PRO A 191 11.857 -50.123 534.627 1.00 59.44 C ANISOU 1480 CG PRO A 191 6788 9546 6250 -154 1197 1969 C ATOM 1481 CD PRO A 191 12.034 -49.137 535.754 1.00 67.57 C ANISOU 1481 CD PRO A 191 7792 10369 7511 -223 1078 2081 C ATOM 1482 N GLY A 192 14.579 -52.979 536.064 1.00 57.42 N ANISOU 1482 N GLY A 192 6308 9463 6044 217 1521 1555 N ATOM 1483 CA GLY A 192 15.907 -53.454 535.760 1.00 66.95 C ANISOU 1483 CA GLY A 192 7381 10882 7174 276 1640 1514 C ATOM 1484 C GLY A 192 16.113 -53.705 534.281 1.00 69.57 C ANISOU 1484 C GLY A 192 7692 11479 7261 274 1742 1496 C ATOM 1485 O GLY A 192 15.157 -53.897 533.523 1.00 77.08 O ANISOU 1485 O GLY A 192 8760 12439 8089 270 1736 1449 O ATOM 1486 N PRO A 193 17.373 -53.707 533.834 1.00 52.20 N ANISOU 1486 N PRO A 193 5339 9516 4978 279 1835 1537 N ATOM 1487 CA PRO A 193 17.654 -54.091 532.443 1.00 79.75 C ANISOU 1487 CA PRO A 193 8801 13282 8220 308 1950 1495 C ATOM 1488 C PRO A 193 17.093 -55.453 532.068 1.00 85.46 C ANISOU 1488 C PRO A 193 9650 13983 8836 479 2027 1230 C ATOM 1489 O PRO A 193 16.875 -55.714 530.881 1.00 82.10 O ANISOU 1489 O PRO A 193 9265 13735 8195 490 2090 1183 O ATOM 1490 CB PRO A 193 19.187 -54.086 532.382 1.00 78.47 C ANISOU 1490 CB PRO A 193 8438 13347 8031 329 2043 1545 C ATOM 1491 CG PRO A 193 19.601 -53.113 533.432 1.00 74.57 C ANISOU 1491 CG PRO A 193 7861 12729 7741 211 1937 1722 C ATOM 1492 CD PRO A 193 18.584 -53.233 534.533 1.00 74.55 C ANISOU 1492 CD PRO A 193 8007 12394 7926 240 1830 1648 C ATOM 1493 N ASP A 194 16.867 -56.326 533.046 1.00 69.15 N ANISOU 1493 N ASP A 194 7655 11707 6914 609 2018 1056 N ATOM 1494 CA ASP A 194 16.269 -57.641 532.838 1.00 66.96 C ANISOU 1494 CA ASP A 194 7516 11356 6570 763 2066 798 C ATOM 1495 C ASP A 194 14.930 -57.632 533.573 1.00 70.87 C ANISOU 1495 C ASP A 194 8163 11573 7192 736 1948 772 C ATOM 1496 O ASP A 194 14.863 -57.963 534.759 1.00 65.89 O ANISOU 1496 O ASP A 194 7550 10732 6752 796 1901 715 O ATOM 1497 CB ASP A 194 17.204 -58.738 533.347 1.00 71.76 C ANISOU 1497 CB ASP A 194 8070 11952 7243 943 2149 618 C ATOM 1498 CG ASP A 194 16.699 -60.132 533.039 1.00 83.65 C ANISOU 1498 CG ASP A 194 9723 13380 8680 1102 2196 344 C ATOM 1499 OD1 ASP A 194 15.612 -60.259 532.436 1.00 78.55 O ANISOU 1499 OD1 ASP A 194 9219 12701 7924 1069 2167 289 O ATOM 1500 OD2 ASP A 194 17.394 -61.105 533.403 1.00 87.79 O ANISOU 1500 OD2 ASP A 194 10223 13871 9262 1258 2254 185 O ATOM 1501 N ARG A 195 13.863 -57.248 532.865 1.00 63.92 N ANISOU 1501 N ARG A 195 7387 10703 6199 646 1897 822 N ATOM 1502 CA ARG A 195 12.559 -57.118 533.511 1.00 49.19 C ANISOU 1502 CA ARG A 195 5648 8601 4443 611 1781 826 C ATOM 1503 C ARG A 195 12.103 -58.443 534.109 1.00 57.38 C ANISOU 1503 C ARG A 195 6794 9464 5545 762 1793 583 C ATOM 1504 O ARG A 195 11.531 -58.471 535.206 1.00 56.85 O ANISOU 1504 O ARG A 195 6772 9172 5657 775 1713 580 O ATOM 1505 CB ARG A 195 11.523 -56.601 532.514 1.00 58.63 C ANISOU 1505 CB ARG A 195 6934 9864 5479 502 1726 907 C ATOM 1506 CG ARG A 195 11.833 -55.224 531.956 1.00 67.67 C ANISOU 1506 CG ARG A 195 7989 11140 6584 339 1682 1165 C ATOM 1507 CD ARG A 195 10.656 -54.668 531.169 1.00 62.04 C ANISOU 1507 CD ARG A 195 7378 10436 5756 233 1591 1258 C ATOM 1508 NE ARG A 195 11.090 -53.733 530.134 1.00 79.41 N ANISOU 1508 NE ARG A 195 9505 12844 7824 109 1590 1447 N ATOM 1509 CZ ARG A 195 11.435 -54.086 528.898 1.00 70.82 C ANISOU 1509 CZ ARG A 195 8406 12010 6494 124 1682 1402 C ATOM 1510 NH1 ARG A 195 11.400 -55.360 528.528 1.00 66.07 N ANISOU 1510 NH1 ARG A 195 7872 11474 5758 263 1779 1158 N ATOM 1511 NH2 ARG A 195 11.817 -53.162 528.028 1.00 73.79 N ANISOU 1511 NH2 ARG A 195 8705 12571 6761 0 1673 1597 N ATOM 1512 N ASP A 196 12.338 -59.551 533.402 1.00 47.05 N ANISOU 1512 N ASP A 196 5535 8246 4094 878 1886 376 N ATOM 1513 CA ASP A 196 11.999 -60.857 533.957 1.00 65.34 C ANISOU 1513 CA ASP A 196 7960 10377 6488 1018 1886 139 C ATOM 1514 C ASP A 196 12.632 -61.046 535.329 1.00 63.77 C ANISOU 1514 C ASP A 196 7691 10010 6531 1084 1862 138 C ATOM 1515 O ASP A 196 12.030 -61.660 536.216 1.00 40.21 O ANISOU 1515 O ASP A 196 4794 6796 3688 1138 1798 42 O ATOM 1516 CB ASP A 196 12.442 -61.967 532.998 1.00 70.48 C ANISOU 1516 CB ASP A 196 8659 11154 6967 1141 1993 -78 C ATOM 1517 CG ASP A 196 12.078 -63.356 533.496 1.00 66.03 C ANISOU 1517 CG ASP A 196 8225 10374 6488 1277 1977 -329 C ATOM 1518 OD1 ASP A 196 12.547 -63.749 534.586 1.00 43.76 O ANISOU 1518 OD1 ASP A 196 5363 7392 3872 1349 1957 -360 O ATOM 1519 OD2 ASP A 196 11.316 -64.056 532.795 1.00 68.51 O ANISOU 1519 OD2 ASP A 196 8690 10676 6667 1303 1972 -490 O ATOM 1520 N ALA A 197 13.844 -60.517 535.524 1.00 63.43 N ANISOU 1520 N ALA A 197 7487 10081 6531 1071 1905 252 N ATOM 1521 CA ALA A 197 14.492 -60.608 536.828 1.00 43.02 C ANISOU 1521 CA ALA A 197 4831 7353 4161 1119 1869 268 C ATOM 1522 C ALA A 197 13.820 -59.690 537.842 1.00 55.14 C ANISOU 1522 C ALA A 197 6379 8715 5859 1017 1748 428 C ATOM 1523 O ALA A 197 13.515 -60.106 538.965 1.00 60.13 O ANISOU 1523 O ALA A 197 7063 9128 6658 1069 1681 374 O ATOM 1524 CB ALA A 197 15.977 -60.271 536.699 1.00 67.72 C ANISOU 1524 CB ALA A 197 7781 10678 7273 1128 1945 350 C ATOM 1525 N THR A 198 13.576 -58.434 537.461 1.00 40.20 N ANISOU 1525 N THR A 198 4446 6909 3921 871 1712 630 N ATOM 1526 CA THR A 198 12.982 -57.485 538.397 1.00 37.56 C ANISOU 1526 CA THR A 198 4121 6404 3745 780 1597 786 C ATOM 1527 C THR A 198 11.590 -57.937 538.818 1.00 41.96 C ANISOU 1527 C THR A 198 4829 6758 4356 815 1531 702 C ATOM 1528 O THR A 198 11.246 -57.904 540.006 1.00 50.94 O ANISOU 1528 O THR A 198 5996 7690 5670 838 1458 716 O ATOM 1529 CB THR A 198 12.924 -56.091 537.773 1.00 41.74 C ANISOU 1529 CB THR A 198 4597 7048 4215 612 1556 1009 C ATOM 1530 OG1 THR A 198 14.219 -55.726 537.283 1.00 70.17 O ANISOU 1530 OG1 THR A 198 8054 10859 7748 574 1624 1089 O ATOM 1531 CG2 THR A 198 12.475 -55.067 538.805 1.00 52.22 C ANISOU 1531 CG2 THR A 198 5928 8185 5729 528 1431 1163 C ATOM 1532 N CYS A 199 10.774 -58.368 537.855 1.00 50.16 N ANISOU 1532 N CYS A 199 5966 7857 5235 817 1554 617 N ATOM 1533 CA CYS A 199 9.442 -58.864 538.183 1.00 44.66 C ANISOU 1533 CA CYS A 199 5409 6987 4572 848 1495 535 C ATOM 1534 C CYS A 199 9.524 -60.022 539.168 1.00 53.22 C ANISOU 1534 C CYS A 199 6544 7880 5795 977 1490 363 C ATOM 1535 O CYS A 199 8.837 -60.031 540.196 1.00 49.27 O ANISOU 1535 O CYS A 199 6098 7172 5449 986 1415 382 O ATOM 1536 CB CYS A 199 8.715 -59.296 536.909 1.00 43.39 C ANISOU 1536 CB CYS A 199 5347 6951 4189 835 1524 443 C ATOM 1537 SG CYS A 199 8.201 -57.937 535.843 1.00 41.36 S ANISOU 1537 SG CYS A 199 5073 6862 3781 661 1476 664 S ATOM 1538 N ASN A 200 10.367 -61.011 538.869 1.00 39.85 N ANISOU 1538 N ASN A 200 4837 6247 4056 1073 1562 201 N ATOM 1539 CA ASN A 200 10.535 -62.132 539.786 1.00 55.70 C ANISOU 1539 CA ASN A 200 6893 8064 6207 1180 1536 50 C ATOM 1540 C ASN A 200 11.174 -61.680 541.092 1.00 49.04 C ANISOU 1540 C ASN A 200 5965 7115 5555 1170 1480 160 C ATOM 1541 O ASN A 200 10.736 -62.081 542.177 1.00 41.89 O ANISOU 1541 O ASN A 200 5122 5997 4798 1188 1399 132 O ATOM 1542 CB ASN A 200 11.379 -63.221 539.129 1.00 51.52 C ANISOU 1542 CB ASN A 200 6358 7626 5590 1287 1623 -136 C ATOM 1543 CG ASN A 200 11.323 -64.534 539.880 1.00 59.69 C ANISOU 1543 CG ASN A 200 7476 8448 6757 1386 1578 -309 C ATOM 1544 OD1 ASN A 200 10.356 -64.817 540.590 1.00 65.73 O ANISOU 1544 OD1 ASN A 200 8339 9010 7624 1366 1487 -324 O ATOM 1545 ND2 ASN A 200 12.363 -65.346 539.728 1.00 62.28 N ANISOU 1545 ND2 ASN A 200 7760 8820 7083 1489 1641 -429 N ATOM 1546 N SER A 201 12.203 -60.836 541.006 1.00 52.21 N ANISOU 1546 N SER A 201 6226 7666 5944 1128 1517 289 N ATOM 1547 CA SER A 201 12.927 -60.413 542.199 1.00 33.49 C ANISOU 1547 CA SER A 201 3777 5216 3734 1118 1466 384 C ATOM 1548 C SER A 201 12.010 -59.671 543.164 1.00 42.79 C ANISOU 1548 C SER A 201 5010 6207 5041 1051 1361 503 C ATOM 1549 O SER A 201 11.794 -60.108 544.301 1.00 37.92 O ANISOU 1549 O SER A 201 4451 5401 4558 1078 1290 463 O ATOM 1550 CB SER A 201 14.114 -59.535 541.796 1.00 50.56 C ANISOU 1550 CB SER A 201 5777 7590 5843 1064 1522 517 C ATOM 1551 OG SER A 201 14.720 -58.936 542.928 1.00 62.58 O ANISOU 1551 OG SER A 201 7226 9041 7510 1033 1462 629 O ATOM 1552 N ARG A 202 11.455 -58.541 542.723 1.00 39.48 N ANISOU 1552 N ARG A 202 4576 5842 4583 955 1347 654 N ATOM 1553 CA ARG A 202 10.687 -57.697 543.633 1.00 41.80 C ANISOU 1553 CA ARG A 202 4904 5965 5012 901 1255 778 C ATOM 1554 C ARG A 202 9.427 -58.398 544.125 1.00 33.32 C ANISOU 1554 C ARG A 202 3971 4697 3993 943 1208 683 C ATOM 1555 O ARG A 202 9.116 -58.353 545.321 1.00 34.14 O ANISOU 1555 O ARG A 202 4117 4619 4238 943 1136 701 O ATOM 1556 CB ARG A 202 10.333 -56.383 542.945 1.00 37.23 C ANISOU 1556 CB ARG A 202 4283 5481 4380 782 1233 952 C ATOM 1557 CG ARG A 202 11.481 -55.396 542.883 1.00 48.06 C ANISOU 1557 CG ARG A 202 5519 6976 5765 696 1231 1097 C ATOM 1558 CD ARG A 202 11.125 -54.201 542.021 1.00 46.54 C ANISOU 1558 CD ARG A 202 5308 6872 5503 552 1189 1255 C ATOM 1559 NE ARG A 202 12.153 -53.169 542.054 1.00 51.56 N ANISOU 1559 NE ARG A 202 5826 7592 6173 445 1161 1406 N ATOM 1560 CZ ARG A 202 12.113 -52.054 541.332 1.00 51.23 C ANISOU 1560 CZ ARG A 202 5761 7621 6083 299 1109 1557 C ATOM 1561 NH1 ARG A 202 11.095 -51.824 540.512 1.00 51.10 N ANISOU 1561 NH1 ARG A 202 5829 7610 5976 250 1077 1578 N ATOM 1562 NH2 ARG A 202 13.095 -51.170 541.429 1.00 77.15 N ANISOU 1562 NH2 ARG A 202 8940 10967 9407 196 1079 1689 N ATOM 1563 N GLN A 203 8.688 -59.053 543.226 1.00 35.44 N ANISOU 1563 N GLN A 203 4316 5010 4140 965 1245 580 N ATOM 1564 CA GLN A 203 7.450 -59.704 543.637 1.00 25.78 C ANISOU 1564 CA GLN A 203 3218 3612 2963 989 1199 497 C ATOM 1565 C GLN A 203 7.700 -60.809 544.654 1.00 47.10 C ANISOU 1565 C GLN A 203 5967 6156 5774 1033 1151 373 C ATOM 1566 O GLN A 203 6.794 -61.146 545.423 1.00 46.25 O ANISOU 1566 O GLN A 203 5938 5884 5750 1008 1080 350 O ATOM 1567 CB GLN A 203 6.716 -60.273 542.423 1.00 48.56 C ANISOU 1567 CB GLN A 203 6182 6592 5676 1001 1247 395 C ATOM 1568 CG GLN A 203 5.277 -60.672 542.716 1.00 37.40 C ANISOU 1568 CG GLN A 203 4890 5025 4295 1001 1201 348 C ATOM 1569 CD GLN A 203 4.423 -59.490 543.152 1.00 40.02 C ANISOU 1569 CD GLN A 203 5202 5304 4700 937 1154 527 C ATOM 1570 OE1 GLN A 203 4.659 -58.356 542.738 1.00 45.14 O ANISOU 1570 OE1 GLN A 203 5774 6068 5311 870 1148 682 O ATOM 1571 NE2 GLN A 203 3.431 -59.751 544.000 1.00 45.42 N ANISOU 1571 NE2 GLN A 203 5949 5811 5499 943 1101 507 N ATOM 1572 N ALA A 204 8.905 -61.377 544.674 1.00 43.22 N ANISOU 1572 N ALA A 204 5417 5729 5276 1081 1181 299 N ATOM 1573 CA ALA A 204 9.257 -62.373 545.678 1.00 33.67 C ANISOU 1573 CA ALA A 204 4233 4391 4168 1106 1121 203 C ATOM 1574 C ALA A 204 9.742 -61.741 546.976 1.00 34.05 C ANISOU 1574 C ALA A 204 4234 4374 4332 1050 1053 310 C ATOM 1575 O ALA A 204 9.480 -62.283 548.055 1.00 30.51 O ANISOU 1575 O ALA A 204 3829 3800 3963 1015 969 271 O ATOM 1576 CB ALA A 204 10.333 -63.312 545.132 1.00 44.88 C ANISOU 1576 CB ALA A 204 5609 5909 5535 1199 1185 68 C ATOM 1577 N ALA A 205 10.449 -60.612 546.895 1.00 38.83 N ANISOU 1577 N ALA A 205 4744 5075 4934 1030 1085 444 N ATOM 1578 CA ALA A 205 10.922 -59.949 548.107 1.00 24.80 C ANISOU 1578 CA ALA A 205 2932 3235 3257 977 1025 539 C ATOM 1579 C ALA A 205 9.756 -59.458 548.954 1.00 30.54 C ANISOU 1579 C ALA A 205 3740 3816 4046 889 946 592 C ATOM 1580 O ALA A 205 9.743 -59.638 550.178 1.00 35.92 O ANISOU 1580 O ALA A 205 4443 4419 4785 830 873 563 O ATOM 1581 CB ALA A 205 11.841 -58.786 547.738 1.00 26.10 C ANISOU 1581 CB ALA A 205 2971 3535 3412 967 1074 682 C ATOM 1582 N LEU A 206 8.763 -58.836 548.318 1.00 38.36 N ANISOU 1582 N LEU A 206 4762 4800 5014 874 962 658 N ATOM 1583 CA LEU A 206 7.617 -58.324 549.060 1.00 30.45 C ANISOU 1583 CA LEU A 206 3815 3695 4059 784 900 694 C ATOM 1584 C LEU A 206 6.863 -59.449 549.755 1.00 30.53 C ANISOU 1584 C LEU A 206 3890 3635 4074 742 830 550 C ATOM 1585 O LEU A 206 6.470 -59.318 550.920 1.00 34.35 O ANISOU 1585 O LEU A 206 4379 4078 4595 668 786 549 O ATOM 1586 CB LEU A 206 6.691 -57.560 548.116 1.00 24.61 C ANISOU 1586 CB LEU A 206 3084 2975 3293 801 936 791 C ATOM 1587 CG LEU A 206 7.264 -56.256 547.560 1.00 27.39 C ANISOU 1587 CG LEU A 206 3337 3398 3673 831 964 967 C ATOM 1588 CD1 LEU A 206 6.479 -55.791 546.341 1.00 33.76 C ANISOU 1588 CD1 LEU A 206 4114 4298 4415 844 981 1005 C ATOM 1589 CD2 LEU A 206 7.260 -55.182 548.640 1.00 47.13 C ANISOU 1589 CD2 LEU A 206 5773 5868 6266 701 886 953 C ATOM 1590 N ALA A 207 6.659 -60.567 549.058 1.00 24.65 N ANISOU 1590 N ALA A 207 3189 2889 3288 808 852 451 N ATOM 1591 CA ALA A 207 5.871 -61.657 549.623 1.00 26.19 C ANISOU 1591 CA ALA A 207 3441 3007 3502 781 794 351 C ATOM 1592 C ALA A 207 6.559 -62.274 550.835 1.00 24.39 C ANISOU 1592 C ALA A 207 3210 2740 3315 783 789 350 C ATOM 1593 O ALA A 207 5.894 -62.643 551.810 1.00 39.66 O ANISOU 1593 O ALA A 207 5169 4622 5277 734 758 347 O ATOM 1594 CB ALA A 207 5.608 -62.716 548.553 1.00 30.33 C ANISOU 1594 CB ALA A 207 4020 3526 3979 861 833 240 C ATOM 1595 N VAL A 208 7.885 -62.396 550.795 1.00 35.20 N ANISOU 1595 N VAL A 208 4536 4152 4688 847 821 349 N ATOM 1596 CA VAL A 208 8.607 -63.061 551.876 1.00 22.67 C ANISOU 1596 CA VAL A 208 2942 2533 3140 869 814 341 C ATOM 1597 C VAL A 208 8.732 -62.146 553.089 1.00 33.83 C ANISOU 1597 C VAL A 208 4321 3947 4588 789 796 434 C ATOM 1598 O VAL A 208 8.422 -62.545 554.218 1.00 29.50 O ANISOU 1598 O VAL A 208 3788 3357 4064 755 772 430 O ATOM 1599 CB VAL A 208 9.988 -63.530 551.382 1.00 22.31 C ANISOU 1599 CB VAL A 208 2843 2548 3086 979 856 295 C ATOM 1600 CG1 VAL A 208 10.765 -64.161 552.518 1.00 28.67 C ANISOU 1600 CG1 VAL A 208 3634 3321 3938 1012 842 293 C ATOM 1601 CG2 VAL A 208 9.837 -64.511 550.227 1.00 29.47 C ANISOU 1601 CG2 VAL A 208 3781 3464 3953 1062 883 164 C ATOM 1602 N SER A 209 9.191 -60.910 552.879 1.00 23.56 N ANISOU 1602 N SER A 209 2966 2697 3291 761 808 512 N ATOM 1603 CA SER A 209 9.314 -59.974 553.993 1.00 29.64 C ANISOU 1603 CA SER A 209 3699 3464 4100 687 789 576 C ATOM 1604 C SER A 209 7.979 -59.800 554.703 1.00 22.90 C ANISOU 1604 C SER A 209 2874 2579 3247 610 762 559 C ATOM 1605 O SER A 209 7.919 -59.769 555.938 1.00 33.67 O ANISOU 1605 O SER A 209 4225 3932 4635 578 742 555 O ATOM 1606 CB SER A 209 9.823 -58.624 553.491 1.00 40.11 C ANISOU 1606 CB SER A 209 4963 4836 5442 666 798 658 C ATOM 1607 OG SER A 209 8.815 -57.943 552.761 1.00 40.12 O ANISOU 1607 OG SER A 209 4980 4840 5424 626 795 675 O ATOM 1608 N LYS A 210 6.899 -59.686 553.931 1.00 28.09 N ANISOU 1608 N LYS A 210 3561 3234 3878 593 758 543 N ATOM 1609 CA LYS A 210 5.562 -59.634 554.508 1.00 22.62 C ANISOU 1609 CA LYS A 210 2881 2527 3185 540 730 517 C ATOM 1610 C LYS A 210 5.277 -60.874 555.343 1.00 27.73 C ANISOU 1610 C LYS A 210 3561 3137 3838 550 719 472 C ATOM 1611 O LYS A 210 4.723 -60.779 556.444 1.00 33.08 O ANISOU 1611 O LYS A 210 4224 3815 4529 513 700 470 O ATOM 1612 CB LYS A 210 4.542 -59.492 553.381 1.00 40.58 C ANISOU 1612 CB LYS A 210 5179 4806 5432 540 723 504 C ATOM 1613 CG LYS A 210 3.099 -59.733 553.766 1.00 57.00 C ANISOU 1613 CG LYS A 210 7272 6870 7513 508 691 470 C ATOM 1614 CD LYS A 210 2.169 -59.396 552.600 1.00 40.31 C ANISOU 1614 CD LYS A 210 5171 4765 5380 514 674 465 C ATOM 1615 CE LYS A 210 2.385 -60.335 551.415 1.00 28.67 C ANISOU 1615 CE LYS A 210 3754 3265 3874 571 685 426 C ATOM 1616 NZ LYS A 210 1.419 -60.085 550.309 1.00 32.40 N ANISOU 1616 NZ LYS A 210 4242 3742 4326 583 660 416 N ATOM 1617 N PHE A 211 5.655 -62.049 554.834 1.00 31.67 N ANISOU 1617 N PHE A 211 4102 3602 4330 610 726 430 N ATOM 1618 CA PHE A 211 5.395 -63.293 555.550 1.00 25.66 C ANISOU 1618 CA PHE A 211 3374 2790 3586 629 710 386 C ATOM 1619 C PHE A 211 6.243 -63.417 556.808 1.00 27.96 C ANISOU 1619 C PHE A 211 3637 3084 3903 636 709 409 C ATOM 1620 O PHE A 211 5.804 -64.024 557.792 1.00 47.14 O ANISOU 1620 O PHE A 211 6076 5486 6348 626 692 399 O ATOM 1621 CB PHE A 211 5.648 -64.480 554.622 1.00 38.87 C ANISOU 1621 CB PHE A 211 5100 4413 5256 707 710 315 C ATOM 1622 CG PHE A 211 5.569 -65.812 555.305 1.00 29.52 C ANISOU 1622 CG PHE A 211 3956 3156 4106 740 686 268 C ATOM 1623 CD1 PHE A 211 4.347 -66.332 555.697 1.00 29.51 C ANISOU 1623 CD1 PHE A 211 3985 3106 4121 699 653 251 C ATOM 1624 CD2 PHE A 211 6.715 -66.548 555.546 1.00 30.26 C ANISOU 1624 CD2 PHE A 211 4051 3224 4222 820 690 242 C ATOM 1625 CE1 PHE A 211 4.270 -67.561 556.325 1.00 41.49 C ANISOU 1625 CE1 PHE A 211 5546 4540 5680 729 622 218 C ATOM 1626 CE2 PHE A 211 6.646 -67.779 556.172 1.00 44.45 C ANISOU 1626 CE2 PHE A 211 5891 4937 6060 859 658 202 C ATOM 1627 CZ PHE A 211 5.420 -68.287 556.563 1.00 46.64 C ANISOU 1627 CZ PHE A 211 6209 5154 6356 809 622 194 C ATOM 1628 N LEU A 212 7.455 -62.861 556.801 1.00 27.53 N ANISOU 1628 N LEU A 212 3545 3062 3855 660 725 442 N ATOM 1629 CA LEU A 212 8.325 -62.957 557.968 1.00 27.02 C ANISOU 1629 CA LEU A 212 3449 2999 3817 675 716 461 C ATOM 1630 C LEU A 212 7.926 -61.955 559.044 1.00 28.64 C ANISOU 1630 C LEU A 212 3620 3231 4030 605 699 493 C ATOM 1631 O LEU A 212 7.660 -62.330 560.192 1.00 40.95 O ANISOU 1631 O LEU A 212 5183 4780 5598 598 680 487 O ATOM 1632 CB LEU A 212 9.780 -62.739 557.550 1.00 16.18 C ANISOU 1632 CB LEU A 212 2036 1656 2458 736 734 481 C ATOM 1633 CG LEU A 212 10.320 -63.788 556.580 1.00 34.80 C ANISOU 1633 CG LEU A 212 4415 4000 4809 837 752 426 C ATOM 1634 CD1 LEU A 212 11.685 -63.380 556.050 1.00 38.61 C ANISOU 1634 CD1 LEU A 212 4829 4545 5297 903 778 448 C ATOM 1635 CD2 LEU A 212 10.388 -65.146 557.257 1.00 36.76 C ANISOU 1635 CD2 LEU A 212 4699 4188 5083 895 731 376 C ATOM 1636 N LEU A 213 7.878 -60.670 558.689 1.00 17.57 N ANISOU 1636 N LEU A 213 2185 1861 2628 563 699 522 N ATOM 1637 CA LEU A 213 7.650 -59.638 559.693 1.00 31.56 C ANISOU 1637 CA LEU A 213 3924 3651 4417 517 670 532 C ATOM 1638 C LEU A 213 6.227 -59.667 560.236 1.00 28.28 C ANISOU 1638 C LEU A 213 3529 3234 3983 485 654 506 C ATOM 1639 O LEU A 213 6.003 -59.289 561.391 1.00 27.35 O ANISOU 1639 O LEU A 213 3400 3121 3869 475 626 500 O ATOM 1640 CB LEU A 213 7.953 -58.261 559.104 1.00 26.08 C ANISOU 1640 CB LEU A 213 3188 2977 3745 491 665 561 C ATOM 1641 CG LEU A 213 9.358 -58.073 558.533 1.00 19.24 C ANISOU 1641 CG LEU A 213 2285 2123 2904 523 684 604 C ATOM 1642 CD1 LEU A 213 9.527 -56.660 558.006 1.00 28.97 C ANISOU 1642 CD1 LEU A 213 3467 3371 4171 490 674 643 C ATOM 1643 CD2 LEU A 213 10.414 -58.382 559.583 1.00 49.44 C ANISOU 1643 CD2 LEU A 213 6082 5944 6756 553 665 610 C ATOM 1644 N ALA A 214 5.256 -60.102 559.432 1.00 23.59 N ANISOU 1644 N ALA A 214 2963 2633 3367 478 667 491 N ATOM 1645 CA ALA A 214 3.849 -59.965 559.784 1.00 29.89 C ANISOU 1645 CA ALA A 214 3765 3437 4153 452 652 477 C ATOM 1646 C ALA A 214 3.178 -61.292 560.117 1.00 34.72 C ANISOU 1646 C ALA A 214 4408 4023 4763 463 657 459 C ATOM 1647 O ALA A 214 1.959 -61.320 560.320 1.00 28.46 O ANISOU 1647 O ALA A 214 3613 3234 3965 446 649 453 O ATOM 1648 CB ALA A 214 3.093 -59.276 558.646 1.00 34.60 C ANISOU 1648 CB ALA A 214 4358 4046 4741 436 648 476 C ATOM 1649 N PHE A 215 3.932 -62.389 560.187 1.00 36.34 N ANISOU 1649 N PHE A 215 4637 4193 4977 500 666 451 N ATOM 1650 CA PHE A 215 3.319 -63.681 560.466 1.00 33.71 C ANISOU 1650 CA PHE A 215 4337 3815 4657 517 660 430 C ATOM 1651 C PHE A 215 4.296 -64.639 561.134 1.00 28.73 C ANISOU 1651 C PHE A 215 3724 3145 4047 566 656 429 C ATOM 1652 O PHE A 215 4.076 -65.061 562.274 1.00 39.43 O ANISOU 1652 O PHE A 215 5077 4490 5414 570 646 441 O ATOM 1653 CB PHE A 215 2.779 -64.299 559.174 1.00 27.57 C ANISOU 1653 CB PHE A 215 3599 2996 3879 527 656 395 C ATOM 1654 CG PHE A 215 1.830 -65.444 559.400 1.00 33.50 C ANISOU 1654 CG PHE A 215 4385 3686 4657 531 633 372 C ATOM 1655 CD1 PHE A 215 0.484 -65.210 559.638 1.00 38.95 C ANISOU 1655 CD1 PHE A 215 5054 4392 5352 492 623 382 C ATOM 1656 CD2 PHE A 215 2.281 -66.753 559.369 1.00 30.44 C ANISOU 1656 CD2 PHE A 215 4054 3214 4298 579 612 341 C ATOM 1657 CE1 PHE A 215 -0.393 -66.260 559.844 1.00 26.35 C ANISOU 1657 CE1 PHE A 215 3491 2729 3791 491 594 371 C ATOM 1658 CE2 PHE A 215 1.409 -67.808 559.574 1.00 17.14 C ANISOU 1658 CE2 PHE A 215 2415 1446 2650 577 574 324 C ATOM 1659 CZ PHE A 215 0.071 -67.561 559.812 1.00 21.51 C ANISOU 1659 CZ PHE A 215 2946 2016 3209 527 564 344 C ATOM 1660 N LEU A 216 5.377 -64.991 560.437 1.00 27.15 N ANISOU 1660 N LEU A 216 3540 2923 3854 614 661 415 N ATOM 1661 CA LEU A 216 6.299 -65.989 560.967 1.00 31.85 C ANISOU 1661 CA LEU A 216 4153 3471 4478 681 648 407 C ATOM 1662 C LEU A 216 6.942 -65.515 562.265 1.00 30.81 C ANISOU 1662 C LEU A 216 3981 3375 4350 678 642 445 C ATOM 1663 O LEU A 216 6.873 -66.197 563.295 1.00 34.82 O ANISOU 1663 O LEU A 216 4501 3854 4876 699 623 453 O ATOM 1664 CB LEU A 216 7.370 -66.306 559.924 1.00 43.19 C ANISOU 1664 CB LEU A 216 5601 4889 5919 750 658 379 C ATOM 1665 CG LEU A 216 8.172 -67.584 560.180 1.00 45.59 C ANISOU 1665 CG LEU A 216 5936 5124 6264 846 636 347 C ATOM 1666 CD1 LEU A 216 7.271 -68.810 560.080 1.00 29.58 C ANISOU 1666 CD1 LEU A 216 3980 2996 4263 861 602 303 C ATOM 1667 CD2 LEU A 216 9.338 -67.687 559.210 1.00 43.80 C ANISOU 1667 CD2 LEU A 216 5696 4907 6040 932 654 316 C ATOM 1668 N VAL A 217 7.567 -64.337 562.239 1.00 21.23 N ANISOU 1668 N VAL A 217 2723 2217 3127 656 649 468 N ATOM 1669 CA VAL A 217 8.221 -63.824 563.443 1.00 24.54 C ANISOU 1669 CA VAL A 217 3107 2662 3554 659 629 494 C ATOM 1670 C VAL A 217 7.220 -63.608 564.571 1.00 26.63 C ANISOU 1670 C VAL A 217 3374 2940 3803 623 615 500 C ATOM 1671 O VAL A 217 7.497 -64.038 565.703 1.00 23.78 O ANISOU 1671 O VAL A 217 3015 2571 3451 653 595 512 O ATOM 1672 CB VAL A 217 9.019 -62.552 563.108 1.00 26.24 C ANISOU 1672 CB VAL A 217 3277 2919 3775 641 627 512 C ATOM 1673 CG1 VAL A 217 9.532 -61.897 564.382 1.00 38.26 C ANISOU 1673 CG1 VAL A 217 4767 4461 5310 639 590 526 C ATOM 1674 CG2 VAL A 217 10.171 -62.884 562.174 1.00 32.39 C ANISOU 1674 CG2 VAL A 217 4043 3694 4571 698 645 516 C ATOM 1675 N PRO A 218 6.072 -62.960 564.355 1.00 25.52 N ANISOU 1675 N PRO A 218 3233 2823 3640 572 623 494 N ATOM 1676 CA PRO A 218 5.079 -62.871 565.440 1.00 32.79 C ANISOU 1676 CA PRO A 218 4156 3758 4544 557 615 501 C ATOM 1677 C PRO A 218 4.758 -64.214 566.073 1.00 34.10 C ANISOU 1677 C PRO A 218 4346 3886 4724 587 618 510 C ATOM 1678 O PRO A 218 4.837 -64.355 567.300 1.00 29.93 O ANISOU 1678 O PRO A 218 3817 3364 4191 609 604 530 O ATOM 1679 CB PRO A 218 3.863 -62.258 564.737 1.00 21.28 C ANISOU 1679 CB PRO A 218 2695 2321 3070 514 626 491 C ATOM 1680 CG PRO A 218 4.444 -61.430 563.651 1.00 36.30 C ANISOU 1680 CG PRO A 218 4584 4232 4976 499 626 484 C ATOM 1681 CD PRO A 218 5.693 -62.139 563.191 1.00 33.62 C ANISOU 1681 CD PRO A 218 4250 3867 4656 535 635 487 C ATOM 1682 N LEU A 219 4.406 -65.215 565.264 1.00 26.74 N ANISOU 1682 N LEU A 219 3443 2904 3813 594 626 496 N ATOM 1683 CA LEU A 219 4.076 -66.521 565.822 1.00 32.13 C ANISOU 1683 CA LEU A 219 4159 3523 4525 624 611 505 C ATOM 1684 C LEU A 219 5.274 -67.126 566.544 1.00 20.92 C ANISOU 1684 C LEU A 219 2751 2070 3127 684 586 520 C ATOM 1685 O LEU A 219 5.117 -67.771 567.587 1.00 24.50 O ANISOU 1685 O LEU A 219 3220 2494 3596 706 566 551 O ATOM 1686 CB LEU A 219 3.579 -67.452 564.716 1.00 19.37 C ANISOU 1686 CB LEU A 219 2588 1834 2936 628 601 474 C ATOM 1687 CG LEU A 219 2.281 -67.018 564.024 1.00 22.94 C ANISOU 1687 CG LEU A 219 3030 2311 3377 575 613 463 C ATOM 1688 CD1 LEU A 219 1.920 -67.991 562.910 1.00 25.72 C ANISOU 1688 CD1 LEU A 219 3441 2572 3758 585 586 424 C ATOM 1689 CD2 LEU A 219 1.125 -66.891 565.012 1.00 16.74 C ANISOU 1689 CD2 LEU A 219 2217 1552 2590 550 619 498 C ATOM 1690 N ALA A 220 6.480 -66.927 566.010 1.00 16.40 N ANISOU 1690 N ALA A 220 2169 1501 2560 716 584 506 N ATOM 1691 CA ALA A 220 7.672 -67.424 566.689 1.00 16.57 C ANISOU 1691 CA ALA A 220 2191 1498 2608 783 556 521 C ATOM 1692 C ALA A 220 7.826 -66.777 568.059 1.00 21.70 C ANISOU 1692 C ALA A 220 2810 2199 3238 776 541 555 C ATOM 1693 O ALA A 220 8.036 -67.464 569.065 1.00 27.85 O ANISOU 1693 O ALA A 220 3603 2946 4034 818 511 584 O ATOM 1694 CB ALA A 220 8.908 -67.163 565.830 1.00 22.42 C ANISOU 1694 CB ALA A 220 2910 2250 3359 822 562 503 C ATOM 1695 N ILE A 221 7.712 -65.449 568.117 1.00 18.29 N ANISOU 1695 N ILE A 221 2342 1834 2772 729 551 551 N ATOM 1696 CA ILE A 221 7.773 -64.754 569.399 1.00 24.30 C ANISOU 1696 CA ILE A 221 3086 2635 3511 731 525 568 C ATOM 1697 C ILE A 221 6.663 -65.244 570.318 1.00 24.26 C ANISOU 1697 C ILE A 221 3102 2626 3487 729 531 592 C ATOM 1698 O ILE A 221 6.881 -65.478 571.513 1.00 24.23 O ANISOU 1698 O ILE A 221 3103 2625 3477 766 504 621 O ATOM 1699 CB ILE A 221 7.695 -63.231 569.178 1.00 24.25 C ANISOU 1699 CB ILE A 221 3055 2678 3482 687 519 546 C ATOM 1700 CG1 ILE A 221 8.957 -62.731 568.475 1.00 21.14 C ANISOU 1700 CG1 ILE A 221 2629 2286 3117 695 505 539 C ATOM 1701 CG2 ILE A 221 7.498 -62.507 570.502 1.00 23.30 C ANISOU 1701 CG2 ILE A 221 2934 2586 3333 698 481 547 C ATOM 1702 CD1 ILE A 221 8.794 -61.367 567.831 1.00 27.18 C ANISOU 1702 CD1 ILE A 221 3375 3075 3878 646 501 521 C ATOM 1703 N ILE A 222 5.455 -65.410 569.774 1.00 27.90 N ANISOU 1703 N ILE A 222 3574 3084 3942 690 564 586 N ATOM 1704 CA ILE A 222 4.324 -65.850 570.586 1.00 22.95 C ANISOU 1704 CA ILE A 222 2957 2459 3305 689 574 618 C ATOM 1705 C ILE A 222 4.601 -67.226 571.179 1.00 24.80 C ANISOU 1705 C ILE A 222 3222 2621 3578 732 546 658 C ATOM 1706 O ILE A 222 4.453 -67.444 572.387 1.00 21.55 O ANISOU 1706 O ILE A 222 2815 2219 3154 758 530 705 O ATOM 1707 CB ILE A 222 3.034 -65.853 569.747 1.00 16.88 C ANISOU 1707 CB ILE A 222 2185 1692 2538 643 607 606 C ATOM 1708 CG1 ILE A 222 2.625 -64.423 569.388 1.00 29.65 C ANISOU 1708 CG1 ILE A 222 3779 3374 4115 608 621 581 C ATOM 1709 CG2 ILE A 222 1.920 -66.551 570.501 1.00 14.76 C ANISOU 1709 CG2 ILE A 222 1919 1411 2278 647 613 652 C ATOM 1710 CD1 ILE A 222 1.679 -64.338 568.205 1.00 33.83 C ANISOU 1710 CD1 ILE A 222 4301 3899 4653 566 641 563 C ATOM 1711 N ALA A 223 5.012 -68.175 570.336 1.00 27.37 N ANISOU 1711 N ALA A 223 3581 2867 3951 748 529 643 N ATOM 1712 CA ALA A 223 5.266 -69.528 570.818 1.00 20.37 C ANISOU 1712 CA ALA A 223 2747 1881 3113 793 480 683 C ATOM 1713 C ALA A 223 6.403 -69.541 571.829 1.00 26.79 C ANISOU 1713 C ALA A 223 3552 2703 3925 851 445 715 C ATOM 1714 O ALA A 223 6.296 -70.160 572.894 1.00 39.07 O ANISOU 1714 O ALA A 223 5133 4224 5488 876 407 778 O ATOM 1715 CB ALA A 223 5.583 -70.451 569.643 1.00 26.30 C ANISOU 1715 CB ALA A 223 3550 2531 3914 816 456 645 C ATOM 1716 N SER A 224 7.501 -68.851 571.517 1.00 27.50 N ANISOU 1716 N SER A 224 3606 2837 4007 872 448 681 N ATOM 1717 CA SER A 224 8.630 -68.805 572.440 1.00 33.28 C ANISOU 1717 CA SER A 224 4321 3580 4743 931 405 710 C ATOM 1718 C SER A 224 8.202 -68.256 573.795 1.00 32.36 C ANISOU 1718 C SER A 224 4192 3524 4579 922 395 750 C ATOM 1719 O SER A 224 8.478 -68.859 574.839 1.00 42.81 O ANISOU 1719 O SER A 224 5535 4822 5909 967 348 809 O ATOM 1720 CB SER A 224 9.751 -67.955 571.846 1.00 29.71 C ANISOU 1720 CB SER A 224 3821 3176 4290 941 409 671 C ATOM 1721 OG SER A 224 10.150 -68.454 570.582 1.00 66.18 O ANISOU 1721 OG SER A 224 8451 7750 8945 962 424 637 O ATOM 1722 N SER A 225 7.510 -67.116 573.795 1.00 27.90 N ANISOU 1722 N SER A 225 3602 3035 3963 872 431 722 N ATOM 1723 CA SER A 225 7.043 -66.528 575.045 1.00 24.54 C ANISOU 1723 CA SER A 225 3171 2668 3483 880 421 749 C ATOM 1724 C SER A 225 6.205 -67.526 575.832 1.00 29.09 C ANISOU 1724 C SER A 225 3777 3217 4059 892 419 823 C ATOM 1725 O SER A 225 6.399 -67.705 577.040 1.00 26.92 O ANISOU 1725 O SER A 225 3510 2958 3758 931 381 882 O ATOM 1726 CB SER A 225 6.233 -65.264 574.753 1.00 30.56 C ANISOU 1726 CB SER A 225 3918 3496 4199 835 457 703 C ATOM 1727 OG SER A 225 6.964 -64.369 573.932 1.00 38.34 O ANISOU 1727 OG SER A 225 4883 4488 5195 813 446 649 O ATOM 1728 N HIS A 226 5.275 -68.201 575.153 1.00 31.21 N ANISOU 1728 N HIS A 226 4064 3440 4357 855 449 830 N ATOM 1729 CA HIS A 226 4.393 -69.138 575.840 1.00 38.97 C ANISOU 1729 CA HIS A 226 5078 4384 5346 850 433 915 C ATOM 1730 C HIS A 226 5.183 -70.278 576.468 1.00 34.33 C ANISOU 1730 C HIS A 226 4542 3706 4794 892 358 987 C ATOM 1731 O HIS A 226 4.838 -70.759 577.554 1.00 41.29 O ANISOU 1731 O HIS A 226 5451 4585 5651 896 323 1085 O ATOM 1732 CB HIS A 226 3.351 -69.685 574.867 1.00 35.08 C ANISOU 1732 CB HIS A 226 4601 3835 4891 797 455 908 C ATOM 1733 CG HIS A 226 2.453 -70.721 575.467 1.00 40.36 C ANISOU 1733 CG HIS A 226 5318 4442 5575 769 419 1012 C ATOM 1734 ND1 HIS A 226 1.397 -70.403 576.293 1.00 34.28 N ANISOU 1734 ND1 HIS A 226 4519 3753 4753 748 445 1080 N ATOM 1735 CD2 HIS A 226 2.459 -72.072 575.365 1.00 43.22 C ANISOU 1735 CD2 HIS A 226 5768 4663 5989 750 348 1073 C ATOM 1736 CE1 HIS A 226 0.787 -71.513 576.671 1.00 57.16 C ANISOU 1736 CE1 HIS A 226 7481 6574 7664 698 394 1191 C ATOM 1737 NE2 HIS A 226 1.412 -72.539 576.122 1.00 50.36 N ANISOU 1737 NE2 HIS A 226 6702 5564 6867 694 330 1187 N ATOM 1738 N ALA A 227 6.241 -70.733 575.795 1.00 33.61 N ANISOU 1738 N ALA A 227 4470 3544 4756 925 326 950 N ATOM 1739 CA ALA A 227 7.049 -71.812 576.351 1.00 39.93 C ANISOU 1739 CA ALA A 227 5326 4249 5599 981 245 1016 C ATOM 1740 C ALA A 227 7.836 -71.353 577.571 1.00 40.51 C ANISOU 1740 C ALA A 227 5370 4392 5629 1029 210 1059 C ATOM 1741 O ALA A 227 8.056 -72.143 578.496 1.00 42.59 O ANISOU 1741 O ALA A 227 5681 4605 5896 1060 140 1155 O ATOM 1742 CB ALA A 227 7.993 -72.363 575.284 1.00 39.20 C ANISOU 1742 CB ALA A 227 5253 4069 5574 1027 222 958 C ATOM 1743 N ALA A 228 8.265 -70.088 577.594 1.00 34.44 N ANISOU 1743 N ALA A 228 4536 3731 4820 1033 242 996 N ATOM 1744 CA ALA A 228 9.071 -69.600 578.710 1.00 31.00 C ANISOU 1744 CA ALA A 228 4077 3356 4346 1080 191 1027 C ATOM 1745 C ALA A 228 8.235 -69.449 579.975 1.00 34.72 C ANISOU 1745 C ALA A 228 4563 3890 4740 1072 184 1103 C ATOM 1746 O ALA A 228 8.649 -69.874 581.060 1.00 33.39 O ANISOU 1746 O ALA A 228 4417 3724 4547 1111 115 1190 O ATOM 1747 CB ALA A 228 9.726 -68.270 578.339 1.00 36.99 C ANISOU 1747 CB ALA A 228 4777 4189 5087 1077 206 939 C ATOM 1748 N VAL A 229 7.054 -68.841 579.858 1.00 46.90 N ANISOU 1748 N VAL A 229 6091 5493 6237 1027 251 1079 N ATOM 1749 CA VAL A 229 6.200 -68.674 581.029 1.00 46.87 C ANISOU 1749 CA VAL A 229 6094 5569 6147 1029 253 1155 C ATOM 1750 C VAL A 229 5.730 -70.029 581.539 1.00 38.25 C ANISOU 1750 C VAL A 229 5060 4411 5062 1007 215 1289 C ATOM 1751 O VAL A 229 5.623 -70.250 582.751 1.00 44.14 O ANISOU 1751 O VAL A 229 5830 5208 5733 1018 173 1396 O ATOM 1752 CB VAL A 229 5.010 -67.753 580.701 1.00 19.46 C ANISOU 1752 CB VAL A 229 2589 2176 2630 1001 335 1100 C ATOM 1753 CG1 VAL A 229 5.503 -66.422 580.155 1.00 37.34 C ANISOU 1753 CG1 VAL A 229 4823 4477 4886 1009 350 978 C ATOM 1754 CG2 VAL A 229 4.075 -68.427 579.716 1.00 49.10 C ANISOU 1754 CG2 VAL A 229 6349 5866 6441 941 382 1105 C ATOM 1755 N SER A 230 5.448 -70.958 580.624 1.00 29.20 N ANISOU 1755 N SER A 230 3951 3148 3996 967 217 1292 N ATOM 1756 CA SER A 230 4.959 -72.271 581.025 1.00 42.34 C ANISOU 1756 CA SER A 230 5699 4718 5670 927 163 1424 C ATOM 1757 C SER A 230 5.944 -72.967 581.955 1.00 46.13 C ANISOU 1757 C SER A 230 6235 5151 6142 974 66 1519 C ATOM 1758 O SER A 230 5.545 -73.556 582.967 1.00 43.24 O ANISOU 1758 O SER A 230 5927 4791 5711 944 23 1659 O ATOM 1759 CB SER A 230 4.698 -73.123 579.783 1.00 35.11 C ANISOU 1759 CB SER A 230 4834 3658 4848 888 157 1390 C ATOM 1760 OG SER A 230 4.213 -74.407 580.132 1.00 87.95 O ANISOU 1760 OG SER A 230 11638 10231 11549 835 88 1520 O ATOM 1761 N LEU A 231 7.236 -72.910 581.630 1.00 43.00 N ANISOU 1761 N LEU A 231 5820 4715 5802 1046 31 1453 N ATOM 1762 CA LEU A 231 8.232 -73.576 582.462 1.00 39.78 C ANISOU 1762 CA LEU A 231 5459 4259 5396 1105 -70 1541 C ATOM 1763 C LEU A 231 8.446 -72.831 583.773 1.00 37.04 C ANISOU 1763 C LEU A 231 5077 4057 4941 1128 -91 1593 C ATOM 1764 O LEU A 231 8.615 -73.455 584.827 1.00 43.89 O ANISOU 1764 O LEU A 231 6003 4918 5756 1138 -168 1725 O ATOM 1765 CB LEU A 231 9.549 -73.708 581.698 1.00 50.24 C ANISOU 1765 CB LEU A 231 6761 5516 6814 1183 -101 1457 C ATOM 1766 CG LEU A 231 9.685 -74.924 580.777 1.00 60.79 C ANISOU 1766 CG LEU A 231 8174 6672 8250 1200 -141 1452 C ATOM 1767 CD1 LEU A 231 8.709 -74.876 579.608 1.00 62.59 C ANISOU 1767 CD1 LEU A 231 8407 6868 8506 1131 -66 1374 C ATOM 1768 CD2 LEU A 231 11.114 -75.026 580.273 1.00 80.65 C ANISOU 1768 CD2 LEU A 231 10654 9149 10839 1302 -178 1388 C ATOM 1769 N ARG A 232 8.441 -71.496 583.732 1.00 38.48 N ANISOU 1769 N ARG A 232 5177 4364 5080 1136 -34 1494 N ATOM 1770 CA ARG A 232 8.621 -70.728 584.959 1.00 39.89 C ANISOU 1770 CA ARG A 232 5333 4678 5146 1164 -67 1530 C ATOM 1771 C ARG A 232 7.509 -71.026 585.956 1.00 38.84 C ANISOU 1771 C ARG A 232 5243 4620 4895 1118 -59 1657 C ATOM 1772 O ARG A 232 7.767 -71.187 587.155 1.00 49.33 O ANISOU 1772 O ARG A 232 6602 6015 6124 1134 -126 1762 O ATOM 1773 CB ARG A 232 8.675 -69.232 584.641 1.00 38.76 C ANISOU 1773 CB ARG A 232 5119 4629 4980 1177 -16 1393 C ATOM 1774 CG ARG A 232 8.674 -68.323 585.870 1.00 49.54 C ANISOU 1774 CG ARG A 232 6473 6134 6215 1208 -54 1411 C ATOM 1775 CD ARG A 232 9.877 -68.567 586.776 1.00 51.89 C ANISOU 1775 CD ARG A 232 6782 6444 6491 1257 -173 1477 C ATOM 1776 NE ARG A 232 11.113 -68.041 586.200 1.00 67.14 N ANISOU 1776 NE ARG A 232 8663 8338 8510 1290 -215 1382 N ATOM 1777 CZ ARG A 232 11.575 -66.809 586.402 1.00 84.46 C ANISOU 1777 CZ ARG A 232 10817 10601 10674 1308 -251 1300 C ATOM 1778 NH1 ARG A 232 12.710 -66.428 585.829 1.00 85.28 N ANISOU 1778 NH1 ARG A 232 10871 10664 10866 1325 -295 1232 N ATOM 1779 NH2 ARG A 232 10.912 -65.955 587.173 1.00 82.64 N ANISOU 1779 NH2 ARG A 232 10596 10480 10323 1312 -251 1287 N ATOM 1780 N LEU A 233 6.265 -71.105 585.481 1.00 44.29 N ANISOU 1780 N LEU A 233 5934 5313 5583 1055 21 1658 N ATOM 1781 CA LEU A 233 5.158 -71.434 586.372 1.00 39.17 C ANISOU 1781 CA LEU A 233 5318 4751 4813 995 37 1791 C ATOM 1782 C LEU A 233 5.283 -72.858 586.899 1.00 39.84 C ANISOU 1782 C LEU A 233 5506 4736 4895 953 -41 1956 C ATOM 1783 O LEU A 233 4.952 -73.127 588.060 1.00 35.65 O ANISOU 1783 O LEU A 233 5008 4306 4233 928 -56 2102 O ATOM 1784 CB LEU A 233 3.829 -71.237 585.648 1.00 34.75 C ANISOU 1784 CB LEU A 233 4723 4215 4264 937 138 1762 C ATOM 1785 CG LEU A 233 3.521 -69.790 585.257 1.00 31.86 C ANISOU 1785 CG LEU A 233 4263 3966 3878 998 231 1631 C ATOM 1786 CD1 LEU A 233 2.201 -69.707 584.514 1.00 29.80 C ANISOU 1786 CD1 LEU A 233 3962 3725 3637 951 325 1622 C ATOM 1787 CD2 LEU A 233 3.499 -68.891 586.483 1.00 35.49 C ANISOU 1787 CD2 LEU A 233 4680 4632 4173 1088 261 1677 C ATOM 1788 N GLN A 234 5.757 -73.782 586.062 1.00 47.23 N ANISOU 1788 N GLN A 234 6498 5484 5966 954 -84 1945 N ATOM 1789 CA GLN A 234 6.068 -75.120 586.553 1.00 50.35 C ANISOU 1789 CA GLN A 234 7014 5751 6366 939 -179 2092 C ATOM 1790 C GLN A 234 7.116 -75.057 587.654 1.00 47.40 C ANISOU 1790 C GLN A 234 6649 5437 5926 1012 -264 2156 C ATOM 1791 O GLN A 234 7.018 -75.771 588.659 1.00 69.15 O ANISOU 1791 O GLN A 234 9489 8196 8588 985 -322 2318 O ATOM 1792 CB GLN A 234 6.556 -75.999 585.401 1.00 49.12 C ANISOU 1792 CB GLN A 234 6919 5380 6366 962 -221 2038 C ATOM 1793 CG GLN A 234 6.886 -77.435 585.792 1.00 37.99 C ANISOU 1793 CG GLN A 234 5664 3798 4973 965 -329 2180 C ATOM 1794 CD GLN A 234 7.917 -78.059 584.873 1.00 55.98 C ANISOU 1794 CD GLN A 234 7982 5894 7394 1057 -397 2099 C ATOM 1795 OE1 GLN A 234 7.652 -78.299 583.695 1.00 46.49 O ANISOU 1795 OE1 GLN A 234 6795 4586 6283 1041 -371 2006 O ATOM 1796 NE2 GLN A 234 9.107 -78.315 585.407 1.00 55.10 N ANISOU 1796 NE2 GLN A 234 7883 5756 7296 1159 -486 2133 N ATOM 1797 N HIS A 235 8.127 -74.203 587.483 1.00 41.44 N ANISOU 1797 N HIS A 235 5808 4729 5208 1098 -276 2036 N ATOM 1798 CA HIS A 235 9.195 -74.110 588.470 1.00 50.12 C ANISOU 1798 CA HIS A 235 6909 5884 6251 1169 -371 2090 C ATOM 1799 C HIS A 235 8.742 -73.383 589.729 1.00 54.95 C ANISOU 1799 C HIS A 235 7502 6699 6675 1146 -363 2151 C ATOM 1800 O HIS A 235 9.171 -73.735 590.833 1.00 61.36 O ANISOU 1800 O HIS A 235 8363 7560 7388 1164 -448 2271 O ATOM 1801 CB HIS A 235 10.405 -73.408 587.857 1.00 49.75 C ANISOU 1801 CB HIS A 235 6774 5829 6299 1253 -388 1946 C ATOM 1802 CG HIS A 235 11.557 -73.258 588.799 1.00 54.00 C ANISOU 1802 CG HIS A 235 7301 6428 6790 1324 -497 1993 C ATOM 1803 ND1 HIS A 235 12.018 -74.294 589.581 1.00 74.67 N ANISOU 1803 ND1 HIS A 235 10002 8988 9382 1355 -603 2141 N ATOM 1804 CD2 HIS A 235 12.340 -72.192 589.087 1.00 67.86 C ANISOU 1804 CD2 HIS A 235 8976 8290 8516 1369 -527 1915 C ATOM 1805 CE1 HIS A 235 13.036 -73.874 590.311 1.00 78.43 C ANISOU 1805 CE1 HIS A 235 10438 9546 9814 1419 -692 2152 C ATOM 1806 NE2 HIS A 235 13.252 -72.601 590.030 1.00 78.03 N ANISOU 1806 NE2 HIS A 235 10290 9596 9762 1424 -651 2015 N ATOM 1807 N ARG A 236 7.880 -72.373 589.591 1.00 41.51 N ANISOU 1807 N ARG A 236 5731 5128 4913 1122 -260 2076 N ATOM 1808 CA ARG A 236 7.426 -71.640 590.767 1.00 42.37 C ANISOU 1808 CA ARG A 236 5797 5477 4825 1146 -217 2152 C ATOM 1809 C ARG A 236 6.508 -72.498 591.626 1.00 43.46 C ANISOU 1809 C ARG A 236 5991 5687 4834 1072 -197 2348 C ATOM 1810 O ARG A 236 6.545 -72.415 592.859 1.00 55.21 O ANISOU 1810 O ARG A 236 7484 7347 6147 1086 -221 2460 O ATOM 1811 CB ARG A 236 6.721 -70.354 590.344 1.00 48.96 C ANISOU 1811 CB ARG A 236 6543 6436 5624 1175 -101 2025 C ATOM 1812 CG ARG A 236 6.590 -69.326 591.457 1.00 59.40 C ANISOU 1812 CG ARG A 236 7821 8011 6736 1247 -80 2035 C ATOM 1813 CD ARG A 236 5.907 -68.064 590.957 1.00 66.21 C ANISOU 1813 CD ARG A 236 8617 8972 7568 1304 26 1894 C ATOM 1814 NE ARG A 236 6.668 -67.425 589.886 1.00 73.86 N ANISOU 1814 NE ARG A 236 9568 9795 8700 1328 3 1723 N ATOM 1815 CZ ARG A 236 6.255 -66.363 589.201 1.00 74.50 C ANISOU 1815 CZ ARG A 236 9611 9896 8799 1368 75 1583 C ATOM 1816 NH1 ARG A 236 5.079 -65.810 589.468 1.00 67.76 N ANISOU 1816 NH1 ARG A 236 8728 9206 7810 1417 178 1586 N ATOM 1817 NH2 ARG A 236 7.020 -65.852 588.244 1.00 64.68 N ANISOU 1817 NH2 ARG A 236 8357 8517 7702 1357 40 1441 N ATOM 1818 N ALA A 900 5.677 -73.329 590.994 1.00 44.25 N ANISOU 1818 N ALA A 900 6138 5666 5008 982 -158 2393 N ATOM 1819 CA ALA A 900 4.782 -74.197 591.752 1.00 56.51 C ANISOU 1819 CA ALA A 900 7749 7276 6447 887 -139 2589 C ATOM 1820 C ALA A 900 5.568 -75.190 592.599 1.00 68.80 C ANISOU 1820 C ALA A 900 9418 8756 7966 891 -261 2736 C ATOM 1821 O ALA A 900 5.209 -75.455 593.752 1.00 73.80 O ANISOU 1821 O ALA A 900 10071 9542 8429 852 -258 2900 O ATOM 1822 CB ALA A 900 3.836 -74.930 590.803 1.00 48.89 C ANISOU 1822 CB ALA A 900 6826 6164 5585 783 -91 2599 C ATOM 1823 N ASP A 901 6.646 -75.748 592.046 1.00 70.35 N ANISOU 1823 N ASP A 901 9688 8732 8311 944 -368 2678 N ATOM 1824 CA ASP A 901 7.466 -76.684 592.807 1.00 67.08 C ANISOU 1824 CA ASP A 901 9384 8233 7869 976 -493 2812 C ATOM 1825 C ASP A 901 8.006 -76.026 594.072 1.00 70.90 C ANISOU 1825 C ASP A 901 9813 8939 8189 1033 -530 2872 C ATOM 1826 O ASP A 901 7.959 -76.610 595.162 1.00 69.11 O ANISOU 1826 O ASP A 901 9650 8783 7825 1010 -573 3053 O ATOM 1827 CB ASP A 901 8.617 -77.197 591.938 1.00 49.98 C ANISOU 1827 CB ASP A 901 7258 5839 5894 1066 -586 2725 C ATOM 1828 CG ASP A 901 8.137 -77.860 590.659 1.00 57.99 C ANISOU 1828 CG ASP A 901 8319 6653 7061 1030 -546 2673 C ATOM 1829 OD1 ASP A 901 6.910 -77.894 590.426 1.00 66.57 O ANISOU 1829 OD1 ASP A 901 9414 7767 8114 922 -457 2695 O ATOM 1830 OD2 ASP A 901 8.988 -78.346 589.884 1.00 45.53 O ANISOU 1830 OD2 ASP A 901 6767 4901 5631 1110 -607 2608 O ATOM 1831 N LEU A 902 8.516 -74.800 593.946 1.00 70.08 N ANISOU 1831 N LEU A 902 9595 8949 8084 1106 -516 2723 N ATOM 1832 CA LEU A 902 9.099 -74.117 595.096 1.00 70.77 C ANISOU 1832 CA LEU A 902 9640 9243 8008 1165 -568 2757 C ATOM 1833 C LEU A 902 8.045 -73.802 596.150 1.00 79.80 C ANISOU 1833 C LEU A 902 10758 10651 8910 1112 -484 2867 C ATOM 1834 O LEU A 902 8.293 -73.967 597.350 1.00 95.42 O ANISOU 1834 O LEU A 902 12766 12773 10716 1118 -544 2994 O ATOM 1835 CB LEU A 902 9.801 -72.842 594.634 1.00 46.78 C ANISOU 1835 CB LEU A 902 6498 6253 5023 1246 -569 2564 C ATOM 1836 CG LEU A 902 10.991 -73.091 593.706 1.00 73.56 C ANISOU 1836 CG LEU A 902 9890 9428 8631 1299 -655 2457 C ATOM 1837 CD1 LEU A 902 11.397 -71.814 592.985 1.00 72.54 C ANISOU 1837 CD1 LEU A 902 9656 9331 8573 1341 -621 2260 C ATOM 1838 CD2 LEU A 902 12.162 -73.665 594.493 1.00 75.31 C ANISOU 1838 CD2 LEU A 902 10158 9626 8832 1360 -808 2555 C ATOM 1839 N GLY A 903 6.863 -73.354 595.724 1.00 82.18 N ANISOU 1839 N GLY A 903 10999 11037 9187 1062 -347 2818 N ATOM 1840 CA GLY A 903 5.825 -73.017 596.684 1.00 81.00 C ANISOU 1840 CA GLY A 903 10807 11169 8802 1020 -257 2904 C ATOM 1841 C GLY A 903 5.432 -74.196 597.552 1.00 64.69 C ANISOU 1841 C GLY A 903 8823 9125 6632 924 -281 3135 C ATOM 1842 O GLY A 903 5.125 -74.034 598.736 1.00 56.93 O ANISOU 1842 O GLY A 903 7822 8392 5418 909 -265 3233 O ATOM 1843 N LEU A 904 5.438 -75.398 596.978 1.00 73.09 N ANISOU 1843 N LEU A 904 13095 4624 10050 3175 568 -113 N ATOM 1844 CA LEU A 904 5.111 -76.609 597.719 1.00 79.17 C ANISOU 1844 CA LEU A 904 14134 5086 10862 3243 671 69 C ATOM 1845 C LEU A 904 6.242 -77.065 598.630 1.00106.63 C ANISOU 1845 C LEU A 904 17690 8553 14272 3633 535 205 C ATOM 1846 O LEU A 904 6.115 -78.113 599.274 1.00 94.79 O ANISOU 1846 O LEU A 904 16425 6790 12803 3734 609 366 O ATOM 1847 CB LEU A 904 4.736 -77.726 596.743 1.00 78.75 C ANISOU 1847 CB LEU A 904 14118 4745 11057 3098 835 -91 C ATOM 1848 CG LEU A 904 3.435 -77.467 595.981 1.00 76.40 C ANISOU 1848 CG LEU A 904 13786 4429 10812 2697 984 -203 C ATOM 1849 CD1 LEU A 904 3.230 -78.491 594.878 1.00 78.27 C ANISOU 1849 CD1 LEU A 904 14014 4439 11287 2570 1110 -424 C ATOM 1850 CD2 LEU A 904 2.253 -77.468 596.935 1.00 76.52 C ANISOU 1850 CD2 LEU A 904 14003 4355 10715 2528 1097 30 C ATOM 1851 N GLN A 905 7.339 -76.318 598.687 1.00 98.52 N ANISOU 1851 N GLN A 905 16470 7808 13155 3850 339 137 N ATOM 1852 CA GLN A 905 8.382 -76.495 599.684 1.00 97.24 C ANISOU 1852 CA GLN A 905 16353 7720 12872 4216 173 268 C ATOM 1853 C GLN A 905 8.288 -75.367 600.705 1.00103.37 C ANISOU 1853 C GLN A 905 17125 8776 13377 4245 43 409 C ATOM 1854 O GLN A 905 7.608 -74.359 600.494 1.00 95.23 O ANISOU 1854 O GLN A 905 16006 7902 12277 4007 61 371 O ATOM 1855 CB GLN A 905 9.764 -76.529 599.023 1.00 98.25 C ANISOU 1855 CB GLN A 905 16243 7984 13104 4452 40 60 C ATOM 1856 CG GLN A 905 9.942 -77.685 598.047 1.00100.10 C ANISOU 1856 CG GLN A 905 16478 7943 13612 4452 167 -98 C ATOM 1857 CD GLN A 905 11.157 -77.521 597.155 1.00102.11 C ANISOU 1857 CD GLN A 905 16446 8374 13978 4606 73 -359 C ATOM 1858 OE1 GLN A 905 12.286 -77.416 597.634 1.00113.16 O ANISOU 1858 OE1 GLN A 905 17749 9940 15306 4909 -99 -349 O ATOM 1859 NE2 GLN A 905 10.930 -77.492 595.847 1.00 97.23 N ANISOU 1859 NE2 GLN A 905 15681 7738 13524 4394 189 -608 N ATOM 1860 N HIS A 906 8.983 -75.545 601.828 1.00107.53 N ANISOU 1860 N HIS A 906 17745 9363 13747 4545 -93 564 N ATOM 1861 CA HIS A 906 8.881 -74.619 602.955 1.00116.83 C ANISOU 1861 CA HIS A 906 18955 10782 14654 4594 -212 703 C ATOM 1862 C HIS A 906 9.762 -73.388 602.729 1.00121.28 C ANISOU 1862 C HIS A 906 19211 11731 15140 4675 -423 529 C ATOM 1863 O HIS A 906 10.688 -73.093 603.483 1.00126.22 O ANISOU 1863 O HIS A 906 19773 12567 15617 4941 -619 547 O ATOM 1864 CB HIS A 906 9.253 -75.334 604.246 1.00109.25 C ANISOU 1864 CB HIS A 906 18226 9738 13544 4882 -269 926 C ATOM 1865 CG HIS A 906 8.577 -76.658 604.412 1.00108.49 C ANISOU 1865 CG HIS A 906 18423 9245 13553 4839 -66 1085 C ATOM 1866 ND1 HIS A 906 9.234 -77.777 604.878 1.00104.35 N ANISOU 1866 ND1 HIS A 906 18058 8530 13058 5131 -92 1194 N ATOM 1867 CD2 HIS A 906 7.303 -77.044 604.167 1.00108.89 C ANISOU 1867 CD2 HIS A 906 18629 9052 13693 4536 168 1145 C ATOM 1868 CE1 HIS A 906 8.393 -78.795 604.914 1.00105.96 C ANISOU 1868 CE1 HIS A 906 18514 8376 13370 5006 123 1321 C ATOM 1869 NE2 HIS A 906 7.214 -78.377 604.489 1.00111.70 N ANISOU 1869 NE2 HIS A 906 19236 9072 14134 4640 284 1286 N ATOM 1870 N ARG A 907 9.441 -72.654 601.666 1.00112.27 N ANISOU 1870 N ARG A 907 17874 10683 14100 4433 -379 348 N ATOM 1871 CA ARG A 907 10.182 -71.464 601.268 1.00112.61 C ANISOU 1871 CA ARG A 907 17612 11069 14104 4459 -548 160 C ATOM 1872 C ARG A 907 9.264 -70.247 601.216 1.00120.36 C ANISOU 1872 C ARG A 907 18540 12193 14998 4184 -520 160 C ATOM 1873 O ARG A 907 9.383 -69.386 600.342 1.00129.54 O ANISOU 1873 O ARG A 907 19473 13524 16221 4055 -551 -23 O ATOM 1874 CB ARG A 907 10.879 -71.686 599.925 1.00 95.37 C ANISOU 1874 CB ARG A 907 15207 8893 12135 4463 -535 -91 C ATOM 1875 CG ARG A 907 12.376 -71.420 599.966 1.00106.17 C ANISOU 1875 CG ARG A 907 16332 10522 13484 4747 -744 -235 C ATOM 1876 CD ARG A 907 13.067 -71.815 598.668 1.00110.59 C ANISOU 1876 CD ARG A 907 16691 11065 14261 4762 -700 -480 C ATOM 1877 NE ARG A 907 13.845 -73.046 598.809 1.00120.40 N ANISOU 1877 NE ARG A 907 18003 12141 15602 5033 -711 -467 N ATOM 1878 CZ ARG A 907 13.417 -74.262 598.475 1.00105.48 C ANISOU 1878 CZ ARG A 907 16304 9901 13872 5007 -541 -421 C ATOM 1879 NH1 ARG A 907 12.205 -74.439 597.966 1.00 94.51 N ANISOU 1879 NH1 ARG A 907 15048 8300 12562 4708 -344 -397 N ATOM 1880 NH2 ARG A 907 14.212 -75.310 598.649 1.00 95.75 N ANISOU 1880 NH2 ARG A 907 15120 8530 12731 5281 -570 -411 N ATOM 1881 N ASN A1002 8.331 -70.161 602.160 1.00109.83 N ANISOU 1881 N ASN A1002 17418 10791 13520 4094 -455 363 N ATOM 1882 CA ASN A1002 7.396 -69.043 602.252 1.00105.12 C ANISOU 1882 CA ASN A1002 16792 10315 12835 3846 -423 383 C ATOM 1883 C ASN A1002 7.723 -68.247 603.512 1.00133.14 C ANISOU 1883 C ASN A1002 20338 14105 16146 4000 -590 470 C ATOM 1884 O ASN A1002 7.081 -68.404 604.551 1.00131.66 O ANISOU 1884 O ASN A1002 20363 13851 15810 3995 -534 659 O ATOM 1885 CB ASN A1002 5.944 -69.549 602.271 1.00101.56 C ANISOU 1885 CB ASN A1002 16565 9601 12422 3579 -187 518 C ATOM 1886 N ILE A1003 8.743 -67.396 603.418 1.00150.42 N ANISOU 1886 N ILE A1003 22273 16582 18299 4135 -792 314 N ATOM 1887 CA ILE A1003 9.096 -66.461 604.483 1.00151.41 C ANISOU 1887 CA ILE A1003 22337 16976 18215 4253 -966 335 C ATOM 1888 C ILE A1003 8.705 -65.034 604.097 1.00144.47 C ANISOU 1888 C ILE A1003 21265 16292 17334 4041 -1001 223 C ATOM 1889 O ILE A1003 9.164 -64.078 604.719 1.00141.77 O ANISOU 1889 O ILE A1003 20789 16211 16866 4122 -1164 165 O ATOM 1890 CB ILE A1003 10.591 -66.557 604.857 1.00151.19 C ANISOU 1890 CB ILE A1003 22159 17150 18136 4577 -1184 234 C ATOM 1891 CG1 ILE A1003 11.459 -65.644 603.998 1.00146.50 C ANISOU 1891 CG1 ILE A1003 21207 16813 17644 4566 -1318 -27 C ATOM 1892 CG2 ILE A1003 11.090 -67.993 604.700 1.00141.31 C ANISOU 1892 CG2 ILE A1003 21032 15678 16981 4766 -1138 283 C ATOM 1893 CD1 ILE A1003 12.949 -65.601 604.367 1.00136.70 C ANISOU 1893 CD1 ILE A1003 19768 15815 16357 4859 -1539 -164 C ATOM 1894 N PHE A1004 7.856 -64.888 603.072 1.00150.05 N ANISOU 1894 N PHE A1004 21956 16872 18184 3771 -848 184 N ATOM 1895 CA PHE A1004 7.370 -63.620 602.515 1.00137.13 C ANISOU 1895 CA PHE A1004 20155 15371 16579 3551 -853 85 C ATOM 1896 C PHE A1004 8.308 -62.995 601.489 1.00140.70 C ANISOU 1896 C PHE A1004 20295 16009 17154 3574 -962 -157 C ATOM 1897 O PHE A1004 8.092 -61.834 601.100 1.00130.85 O ANISOU 1897 O PHE A1004 18883 14907 15926 3429 -997 -251 O ATOM 1898 CB PHE A1004 7.106 -62.581 603.609 1.00 79.37 C ANISOU 1898 CB PHE A1004 12839 8239 9077 3552 -949 150 C ATOM 1899 N GLU A1005 9.325 -63.715 601.025 1.00145.84 N ANISOU 1899 N GLU A1005 20854 16661 17898 3746 -1006 -266 N ATOM 1900 CA GLU A1005 10.278 -63.180 600.050 1.00128.27 C ANISOU 1900 CA GLU A1005 18313 14630 15793 3767 -1092 -513 C ATOM 1901 C GLU A1005 9.947 -63.720 598.657 1.00103.70 C ANISOU 1901 C GLU A1005 15193 11347 12863 3608 -922 -614 C ATOM 1902 O GLU A1005 9.460 -62.980 597.797 1.00106.26 O ANISOU 1902 O GLU A1005 15412 11713 13250 3392 -860 -714 O ATOM 1903 CB GLU A1005 11.726 -63.534 600.435 1.00129.96 C ANISOU 1903 CB GLU A1005 18383 15005 15989 4063 -1259 -608 C ATOM 1904 CG GLU A1005 12.003 -63.662 601.940 1.00141.77 C ANISOU 1904 CG GLU A1005 20008 16570 17288 4274 -1389 -466 C ATOM 1905 CD GLU A1005 12.542 -62.400 602.597 1.00138.58 C ANISOU 1905 CD GLU A1005 19393 16490 16770 4317 -1578 -566 C ATOM 1906 OE1 GLU A1005 13.292 -61.642 601.937 1.00148.78 O ANISOU 1906 OE1 GLU A1005 20372 18000 18159 4288 -1661 -789 O ATOM 1907 OE2 GLU A1005 12.234 -62.168 603.780 1.00130.09 O ANISOU 1907 OE2 GLU A1005 18458 15459 15513 4374 -1634 -437 O ATOM 1908 N GLU A1064 22.705 -52.036 584.510 1.00 91.17 N ANISOU 1908 N GLU A1064 8535 13607 12500 1227 85 -3841 N ATOM 1909 CA GLU A1064 22.590 -53.413 584.980 1.00 99.77 C ANISOU 1909 CA GLU A1064 9781 14556 13572 1579 -57 -3855 C ATOM 1910 C GLU A1064 21.798 -54.231 583.972 1.00102.80 C ANISOU 1910 C GLU A1064 10403 14805 13852 1514 84 -3768 C ATOM 1911 O GLU A1064 21.002 -53.667 583.213 1.00114.00 O ANISOU 1911 O GLU A1064 11944 16198 15172 1217 227 -3614 O ATOM 1912 CB GLU A1064 21.930 -53.472 586.355 1.00108.45 C ANISOU 1912 CB GLU A1064 11093 15480 14632 1762 -290 -3675 C ATOM 1913 N LYS A1065 22.020 -55.551 583.991 1.00110.37 N ANISOU 1913 N LYS A1065 11426 15676 14834 1801 36 -3871 N ATOM 1914 CA LYS A1065 21.539 -56.435 582.937 1.00 99.52 C ANISOU 1914 CA LYS A1065 10210 14210 13392 1756 187 -3881 C ATOM 1915 C LYS A1065 20.107 -56.091 582.558 1.00105.45 C ANISOU 1915 C LYS A1065 11250 14816 14000 1492 255 -3617 C ATOM 1916 O LYS A1065 19.329 -55.620 583.395 1.00106.48 O ANISOU 1916 O LYS A1065 11545 14820 14093 1464 137 -3402 O ATOM 1917 CB LYS A1065 21.628 -57.895 583.380 1.00 81.29 C ANISOU 1917 CB LYS A1065 8038 11717 11132 2125 78 -3946 C ATOM 1918 N LEU A1066 19.749 -56.324 581.296 1.00 99.20 N ANISOU 1918 N LEU A1066 10514 14057 13122 1305 442 -3643 N ATOM 1919 CA LEU A1066 18.432 -55.910 580.827 1.00 94.06 C ANISOU 1919 CA LEU A1066 10096 13315 12326 1044 506 -3412 C ATOM 1920 C LEU A1066 17.354 -56.543 581.694 1.00 86.28 C ANISOU 1920 C LEU A1066 9416 12048 11319 1179 361 -3228 C ATOM 1921 O LEU A1066 17.388 -57.746 581.967 1.00 97.99 O ANISOU 1921 O LEU A1066 11007 13375 12850 1419 309 -3301 O ATOM 1922 CB LEU A1066 18.225 -56.294 579.357 1.00 80.08 C ANISOU 1922 CB LEU A1066 8350 11629 10448 874 707 -3497 C ATOM 1923 CG LEU A1066 18.722 -55.322 578.275 1.00 78.19 C ANISOU 1923 CG LEU A1066 7911 11656 10141 598 900 -3552 C ATOM 1924 CD1 LEU A1066 17.897 -55.471 576.999 1.00 61.93 C ANISOU 1924 CD1 LEU A1066 6000 9633 7897 382 1053 -3499 C ATOM 1925 CD2 LEU A1066 18.701 -53.869 578.736 1.00 90.97 C ANISOU 1925 CD2 LEU A1066 9454 13337 11773 420 874 -3387 C ATOM 1926 N PHE A1067 16.394 -55.724 582.124 1.00 86.69 N ANISOU 1926 N PHE A1067 9606 12026 11305 1022 308 -2989 N ATOM 1927 CA PHE A1067 15.342 -56.151 583.040 1.00 75.92 C ANISOU 1927 CA PHE A1067 8516 10412 9919 1120 181 -2801 C ATOM 1928 C PHE A1067 15.969 -56.732 584.312 1.00 76.64 C ANISOU 1928 C PHE A1067 8601 10407 10110 1458 11 -2849 C ATOM 1929 O PHE A1067 15.846 -57.914 584.629 1.00 67.54 O ANISOU 1929 O PHE A1067 7605 9071 8986 1679 -32 -2870 O ATOM 1930 CB PHE A1067 14.405 -57.134 582.329 1.00 67.60 C ANISOU 1930 CB PHE A1067 7683 9208 8794 1072 265 -2782 C ATOM 1931 CG PHE A1067 14.178 -56.794 580.879 1.00 57.12 C ANISOU 1931 CG PHE A1067 6300 8043 7360 802 437 -2825 C ATOM 1932 CD1 PHE A1067 13.541 -55.618 580.519 1.00 60.99 C ANISOU 1932 CD1 PHE A1067 6795 8628 7751 538 476 -2658 C ATOM 1933 CD2 PHE A1067 14.614 -57.644 579.878 1.00 64.05 C ANISOU 1933 CD2 PHE A1067 7126 8984 8228 826 560 -3035 C ATOM 1934 CE1 PHE A1067 13.338 -55.301 579.187 1.00 57.29 C ANISOU 1934 CE1 PHE A1067 6291 8320 7158 308 628 -2679 C ATOM 1935 CE2 PHE A1067 14.412 -57.332 578.546 1.00 63.05 C ANISOU 1935 CE2 PHE A1067 6955 9030 7971 584 717 -3076 C ATOM 1936 CZ PHE A1067 13.775 -56.160 578.203 1.00 48.95 C ANISOU 1936 CZ PHE A1067 5185 7345 6070 329 748 -2888 C ATOM 1937 N ASN A1068 16.652 -55.842 585.034 1.00 75.16 N ANISOU 1937 N ASN A1068 8231 10351 9975 1492 -84 -2865 N ATOM 1938 CA ASN A1068 17.525 -56.232 586.132 1.00 84.30 C ANISOU 1938 CA ASN A1068 9303 11509 11218 1816 -253 -2959 C ATOM 1939 C ASN A1068 16.732 -56.452 587.419 1.00 83.53 C ANISOU 1939 C ASN A1068 9461 11201 11076 1968 -413 -2754 C ATOM 1940 O ASN A1068 15.499 -56.384 587.454 1.00 73.82 O ANISOU 1940 O ASN A1068 8470 9814 9767 1822 -382 -2554 O ATOM 1941 CB ASN A1068 18.601 -55.170 586.353 1.00 96.28 C ANISOU 1941 CB ASN A1068 10495 13278 12810 1775 -288 -3094 C ATOM 1942 CG ASN A1068 18.067 -53.943 587.069 1.00112.99 C ANISOU 1942 CG ASN A1068 12639 15399 14894 1614 -358 -2928 C ATOM 1943 OD1 ASN A1068 18.175 -53.827 588.291 1.00 86.01 O ANISOU 1943 OD1 ASN A1068 9240 11952 11487 1794 -536 -2893 O ATOM 1944 ND2 ASN A1068 17.479 -53.024 586.310 1.00126.54 N ANISOU 1944 ND2 ASN A1068 14364 17152 16563 1285 -220 -2826 N ATOM 1945 N GLN A1069 17.469 -56.715 588.499 1.00100.81 N ANISOU 1945 N GLN A1069 11588 13404 13309 2269 -586 -2812 N ATOM 1946 CA GLN A1069 16.890 -56.945 589.816 1.00110.57 C ANISOU 1946 CA GLN A1069 13055 14471 14487 2452 -744 -2630 C ATOM 1947 C GLN A1069 17.973 -56.807 590.883 1.00109.79 C ANISOU 1947 C GLN A1069 12779 14512 14426 2739 -942 -2741 C ATOM 1948 O GLN A1069 17.985 -57.555 591.867 1.00119.60 O ANISOU 1948 O GLN A1069 14183 15629 15632 3047 -1086 -2671 O ATOM 1949 CB GLN A1069 16.242 -58.333 589.875 1.00119.48 C ANISOU 1949 CB GLN A1069 14490 15315 15591 2619 -721 -2533 C ATOM 1950 CG GLN A1069 15.447 -58.615 591.146 1.00122.56 C ANISOU 1950 CG GLN A1069 15169 15498 15899 2764 -838 -2307 C ATOM 1951 CD GLN A1069 15.932 -59.850 591.892 1.00119.31 C ANISOU 1951 CD GLN A1069 14893 14935 15506 3169 -948 -2313 C ATOM 1952 OE1 GLN A1069 17.097 -60.239 591.791 1.00110.75 O ANISOU 1952 OE1 GLN A1069 13616 13963 14499 3399 -1008 -2504 O ATOM 1953 NE2 GLN A1069 15.032 -60.474 592.646 1.00107.47 N ANISOU 1953 NE2 GLN A1069 13724 13173 13935 3262 -968 -2099 N ATOM 1954 N ASP A1070 18.886 -55.852 590.700 1.00 97.04 N ANISOU 1954 N ASP A1070 10831 13161 12878 2641 -951 -2917 N ATOM 1955 CA ASP A1070 20.065 -55.717 591.556 1.00 96.89 C ANISOU 1955 CA ASP A1070 10573 13328 12913 2903 -1136 -3089 C ATOM 1956 C ASP A1070 19.709 -54.850 592.758 1.00 89.05 C ANISOU 1956 C ASP A1070 9627 12359 11848 2894 -1288 -2973 C ATOM 1957 O ASP A1070 19.761 -53.620 592.692 1.00 86.77 O ANISOU 1957 O ASP A1070 9170 12210 11589 2640 -1255 -3011 O ATOM 1958 CB ASP A1070 21.232 -55.127 590.772 1.00 98.59 C ANISOU 1958 CB ASP A1070 10388 13821 13252 2784 -1054 -3363 C ATOM 1959 CG ASP A1070 22.539 -55.179 591.542 1.00 96.73 C ANISOU 1959 CG ASP A1070 9933 13768 13052 2996 -1239 -3524 C ATOM 1960 OD1 ASP A1070 22.520 -55.573 592.728 1.00 88.75 O ANISOU 1960 OD1 ASP A1070 9083 12686 11950 3233 -1437 -3415 O ATOM 1961 OD2 ASP A1070 23.587 -54.832 590.958 1.00105.89 O ANISOU 1961 OD2 ASP A1070 10791 15137 14304 2890 -1176 -3738 O ATOM 1962 N VAL A1071 19.356 -55.499 593.869 1.00 88.35 N ANISOU 1962 N VAL A1071 9777 12129 11663 3174 -1447 -2832 N ATOM 1963 CA VAL A1071 18.986 -54.765 595.075 1.00 82.14 C ANISOU 1963 CA VAL A1071 9059 11368 10784 3190 -1594 -2725 C ATOM 1964 C VAL A1071 20.222 -54.184 595.753 1.00 82.57 C ANISOU 1964 C VAL A1071 8812 11696 10865 3295 -1762 -2931 C ATOM 1965 O VAL A1071 20.212 -53.035 596.209 1.00 74.72 O ANISOU 1965 O VAL A1071 7680 10834 9878 3157 -1814 -2980 O ATOM 1966 CB VAL A1071 18.193 -55.679 596.026 1.00 74.75 C ANISOU 1966 CB VAL A1071 8500 10192 9708 3434 -1685 -2491 C ATOM 1967 CG1 VAL A1071 17.641 -54.883 597.200 1.00 96.78 C ANISOU 1967 CG1 VAL A1071 11388 13003 12380 3409 -1803 -2366 C ATOM 1968 CG2 VAL A1071 17.067 -56.378 595.275 1.00 85.09 C ANISOU 1968 CG2 VAL A1071 10103 11226 11003 3283 -1495 -2308 C ATOM 1969 N ASP A1072 21.305 -54.964 595.829 1.00 97.54 N ANISOU 1969 N ASP A1072 10627 13669 12766 3486 -1835 -3042 N ATOM 1970 CA ASP A1072 22.502 -54.504 596.528 1.00101.91 C ANISOU 1970 CA ASP A1072 10942 14466 13312 3555 -1988 -3228 C ATOM 1971 C ASP A1072 23.054 -53.219 595.922 1.00 97.25 C ANISOU 1971 C ASP A1072 9993 14094 12862 3263 -1900 -3450 C ATOM 1972 O ASP A1072 23.621 -52.389 596.642 1.00102.07 O ANISOU 1972 O ASP A1072 10445 14874 13465 3222 -2005 -3574 O ATOM 1973 CB ASP A1072 23.578 -55.592 596.506 1.00101.38 C ANISOU 1973 CB ASP A1072 10827 14440 13251 3803 -2056 -3328 C ATOM 1974 CG ASP A1072 23.133 -56.871 597.191 1.00 98.96 C ANISOU 1974 CG ASP A1072 10878 13911 12813 4092 -2137 -3102 C ATOM 1975 OD1 ASP A1072 22.250 -57.565 596.644 1.00103.04 O ANISOU 1975 OD1 ASP A1072 11627 14185 13338 4079 -2010 -2938 O ATOM 1976 OD2 ASP A1072 23.672 -57.184 598.274 1.00101.04 O ANISOU 1976 OD2 ASP A1072 11192 14237 12961 4325 -2316 -3094 O ATOM 1977 N ALA A1073 22.906 -53.039 594.608 1.00 87.60 N ANISOU 1977 N ALA A1073 8650 12867 11766 3046 -1691 -3506 N ATOM 1978 CA ALA A1073 23.465 -51.859 593.956 1.00 88.37 C ANISOU 1978 CA ALA A1073 8419 13158 11998 2743 -1569 -3700 C ATOM 1979 C ALA A1073 22.815 -50.582 594.473 1.00 90.95 C ANISOU 1979 C ALA A1073 8734 13497 12325 2540 -1582 -3639 C ATOM 1980 O ALA A1073 23.502 -49.598 594.774 1.00 79.33 O ANISOU 1980 O ALA A1073 7044 12184 10913 2393 -1604 -3798 O ATOM 1981 CB ALA A1073 23.296 -51.975 592.441 1.00101.96 C ANISOU 1981 CB ALA A1073 10062 14860 13817 2547 -1317 -3735 C ATOM 1982 N ALA A1074 21.484 -50.578 594.587 1.00 89.92 N ANISOU 1982 N ALA A1074 8870 13175 12122 2505 -1556 -3402 N ATOM 1983 CA ALA A1074 20.786 -49.371 595.015 1.00 77.65 C ANISOU 1983 CA ALA A1074 7371 11586 10547 2255 -1544 -3299 C ATOM 1984 C ALA A1074 21.045 -49.071 596.486 1.00 82.55 C ANISOU 1984 C ALA A1074 7957 12306 11102 2461 -1788 -3362 C ATOM 1985 O ALA A1074 21.240 -47.909 596.861 1.00 87.77 O ANISOU 1985 O ALA A1074 8474 13063 11812 2270 -1799 -3456 O ATOM 1986 CB ALA A1074 19.287 -49.510 594.756 1.00 75.69 C ANISOU 1986 CB ALA A1074 7497 11070 10192 2108 -1432 -2987 C ATOM 1987 N VAL A1075 21.055 -50.105 597.333 1.00 87.09 N ANISOU 1987 N VAL A1075 8756 12810 11524 2781 -1943 -3270 N ATOM 1988 CA VAL A1075 21.260 -49.887 598.762 1.00 73.16 C ANISOU 1988 CA VAL A1075 7068 11107 9622 2927 -2133 -3275 C ATOM 1989 C VAL A1075 22.576 -49.168 599.006 1.00 86.58 C ANISOU 1989 C VAL A1075 8458 13041 11396 2860 -2177 -3559 C ATOM 1990 O VAL A1075 22.692 -48.364 599.939 1.00 90.90 O ANISOU 1990 O VAL A1075 8969 13669 11899 2826 -2263 -3627 O ATOM 1991 CB VAL A1075 21.203 -51.226 599.524 1.00 69.36 C ANISOU 1991 CB VAL A1075 6871 10522 8963 3280 -2264 -3128 C ATOM 1992 CG1 VAL A1075 21.524 -51.015 600.997 1.00 77.45 C ANISOU 1992 CG1 VAL A1075 7955 11645 9827 3440 -2448 -3154 C ATOM 1993 CG2 VAL A1075 19.838 -51.873 599.367 1.00 76.59 C ANISOU 1993 CG2 VAL A1075 8122 11172 9805 3320 -2197 -2843 C ATOM 1994 N ARG A1076 23.587 -49.441 598.180 1.00 89.52 N ANISOU 1994 N ARG A1076 8607 13521 11885 2838 -2106 -3739 N ATOM 1995 CA ARG A1076 24.861 -48.747 598.319 1.00 96.30 C ANISOU 1995 CA ARG A1076 9163 14594 12831 2754 -2123 -4023 C ATOM 1996 C ARG A1076 24.779 -47.314 597.809 1.00 80.57 C ANISOU 1996 C ARG A1076 6977 12640 10995 2372 -1959 -4114 C ATOM 1997 O ARG A1076 25.507 -46.444 598.302 1.00 68.11 O ANISOU 1997 O ARG A1076 5218 11190 9468 2279 -1982 -4307 O ATOM 1998 CB ARG A1076 25.955 -49.530 597.592 1.00 99.85 C ANISOU 1998 CB ARG A1076 9443 15142 13352 2852 -2092 -4183 C ATOM 1999 CG ARG A1076 26.223 -50.892 598.225 1.00 99.07 C ANISOU 1999 CG ARG A1076 9520 15011 13109 3240 -2267 -4114 C ATOM 2000 CD ARG A1076 27.416 -51.608 597.602 1.00108.44 C ANISOU 2000 CD ARG A1076 10513 16312 14375 3348 -2255 -4301 C ATOM 2001 NE ARG A1076 27.037 -52.450 596.468 1.00 96.97 N ANISOU 2001 NE ARG A1076 9140 14723 12980 3342 -2111 -4197 N ATOM 2002 CZ ARG A1076 27.040 -52.060 595.196 1.00101.10 C ANISOU 2002 CZ ARG A1076 9502 15264 13648 3073 -1893 -4270 C ATOM 2003 NH1 ARG A1076 27.403 -50.826 594.867 1.00101.44 N ANISOU 2003 NH1 ARG A1076 9301 15439 13802 2773 -1784 -4427 N ATOM 2004 NH2 ARG A1076 26.678 -52.911 594.246 1.00 80.95 N ANISOU 2004 NH2 ARG A1076 7046 12589 11125 3099 -1768 -4183 N ATOM 2005 N GLY A1077 23.906 -47.046 596.835 1.00 86.88 N ANISOU 2005 N GLY A1077 7818 13320 11872 2147 -1784 -3976 N ATOM 2006 CA GLY A1077 23.652 -45.674 596.436 1.00 92.05 C ANISOU 2006 CA GLY A1077 8349 13969 12657 1782 -1627 -4003 C ATOM 2007 C GLY A1077 22.698 -44.950 597.360 1.00 85.48 C ANISOU 2007 C GLY A1077 7679 13041 11758 1734 -1707 -3872 C ATOM 2008 O GLY A1077 22.789 -43.728 597.513 1.00 83.43 O ANISOU 2008 O GLY A1077 7313 12796 11592 1492 -1636 -3950 O ATOM 2009 N ILE A1078 21.772 -45.681 597.985 1.00 80.70 N ANISOU 2009 N ILE A1078 7346 12323 10993 1958 -1839 -3669 N ATOM 2010 CA ILE A1078 20.866 -45.071 598.954 1.00 81.82 C ANISOU 2010 CA ILE A1078 7660 12383 11046 1936 -1924 -3548 C ATOM 2011 C ILE A1078 21.640 -44.604 600.181 1.00 87.99 C ANISOU 2011 C ILE A1078 8366 13293 11772 2037 -2055 -3722 C ATOM 2012 O ILE A1078 21.451 -43.483 600.668 1.00 85.54 O ANISOU 2012 O ILE A1078 8015 12982 11506 1864 -2034 -3771 O ATOM 2013 CB ILE A1078 19.747 -46.058 599.335 1.00 77.21 C ANISOU 2013 CB ILE A1078 7401 11645 10289 2165 -2019 -3288 C ATOM 2014 CG1 ILE A1078 18.743 -46.192 598.187 1.00 73.49 C ANISOU 2014 CG1 ILE A1078 7109 10966 9849 1949 -1807 -3063 C ATOM 2015 CG2 ILE A1078 19.053 -45.612 600.624 1.00 78.68 C ANISOU 2015 CG2 ILE A1078 7776 11786 10334 2221 -2139 -3195 C ATOM 2016 CD1 ILE A1078 17.765 -47.341 598.352 1.00 69.50 C ANISOU 2016 CD1 ILE A1078 6976 10254 9178 2130 -1818 -2796 C ATOM 2017 N LEU A1079 22.521 -45.461 600.702 1.00 88.00 N ANISOU 2017 N LEU A1079 8351 13407 11678 2323 -2189 -3822 N ATOM 2018 CA LEU A1079 23.323 -45.082 601.860 1.00 79.97 C ANISOU 2018 CA LEU A1079 7244 12542 10598 2439 -2323 -4008 C ATOM 2019 C LEU A1079 24.351 -44.017 601.502 1.00 80.27 C ANISOU 2019 C LEU A1079 6955 12713 10830 2200 -2219 -4285 C ATOM 2020 O LEU A1079 24.752 -43.230 602.367 1.00 89.61 O ANISOU 2020 O LEU A1079 8044 13990 12013 2178 -2275 -4439 O ATOM 2021 CB LEU A1079 24.010 -46.317 602.444 1.00 83.18 C ANISOU 2021 CB LEU A1079 7721 13034 10851 2808 -2493 -4034 C ATOM 2022 CG LEU A1079 23.066 -47.387 603.000 1.00 78.41 C ANISOU 2022 CG LEU A1079 7475 12283 10036 3067 -2592 -3753 C ATOM 2023 CD1 LEU A1079 23.809 -48.691 603.247 1.00 65.04 C ANISOU 2023 CD1 LEU A1079 5841 10639 8231 3398 -2714 -3762 C ATOM 2024 CD2 LEU A1079 22.401 -46.904 604.278 1.00 82.01 C ANISOU 2024 CD2 LEU A1079 8102 12721 10336 3118 -2684 -3669 C ATOM 2025 N ARG A1080 24.785 -43.972 600.240 1.00 82.93 N ANISOU 2025 N ARG A1080 7121 13059 11330 2015 -2053 -4352 N ATOM 2026 CA ARG A1080 25.744 -42.964 599.806 1.00 80.67 C ANISOU 2026 CA ARG A1080 6543 12876 11232 1761 -1918 -4595 C ATOM 2027 C ARG A1080 25.124 -41.577 599.683 1.00 91.33 C ANISOU 2027 C ARG A1080 7882 14116 12703 1426 -1769 -4552 C ATOM 2028 O ARG A1080 25.866 -40.595 599.577 1.00 87.03 O ANISOU 2028 O ARG A1080 7127 13634 12305 1221 -1665 -4748 O ATOM 2029 CB ARG A1080 26.363 -43.377 598.468 1.00 83.83 C ANISOU 2029 CB ARG A1080 6787 13313 11751 1662 -1765 -4661 C ATOM 2030 CG ARG A1080 27.528 -42.503 598.020 1.00 97.70 C ANISOU 2030 CG ARG A1080 8243 15192 13687 1432 -1624 -4928 C ATOM 2031 CD ARG A1080 28.302 -43.144 596.872 1.00107.95 C ANISOU 2031 CD ARG A1080 9389 16566 15061 1411 -1510 -5020 C ATOM 2032 NE ARG A1080 29.533 -42.418 596.555 1.00139.81 N ANISOU 2032 NE ARG A1080 13135 20736 19248 1228 -1393 -5296 N ATOM 2033 CZ ARG A1080 29.631 -41.443 595.653 1.00131.73 C ANISOU 2033 CZ ARG A1080 12002 19665 18386 870 -1139 -5318 C ATOM 2034 NH1 ARG A1080 28.570 -41.052 594.958 1.00132.24 N ANISOU 2034 NH1 ARG A1080 12215 19556 18475 652 -979 -5078 N ATOM 2035 NH2 ARG A1080 30.802 -40.853 595.445 1.00101.56 N ANISOU 2035 NH2 ARG A1080 7925 15967 14695 728 -1042 -5578 N ATOM 2036 N ASN A1081 23.798 -41.471 599.701 1.00 94.37 N ANISOU 2036 N ASN A1081 8491 14332 13034 1368 -1756 -4304 N ATOM 2037 CA ASN A1081 23.107 -40.190 599.634 1.00 90.53 C ANISOU 2037 CA ASN A1081 8026 13717 12652 1068 -1628 -4239 C ATOM 2038 C ASN A1081 22.736 -39.744 601.043 1.00 83.98 C ANISOU 2038 C ASN A1081 7300 12888 11719 1179 -1778 -4252 C ATOM 2039 O ASN A1081 22.168 -40.522 601.817 1.00 68.78 O ANISOU 2039 O ASN A1081 5577 10955 9602 1440 -1945 -4128 O ATOM 2040 CB ASN A1081 21.854 -40.291 598.763 1.00 86.72 C ANISOU 2040 CB ASN A1081 7719 13053 12178 921 -1519 -3971 C ATOM 2041 CG ASN A1081 21.228 -38.939 598.486 1.00 95.47 C ANISOU 2041 CG ASN A1081 8843 14014 13419 583 -1358 -3902 C ATOM 2042 OD1 ASN A1081 20.652 -38.313 599.376 1.00 97.48 O ANISOU 2042 OD1 ASN A1081 9199 14202 13639 576 -1425 -3869 O ATOM 2043 ND2 ASN A1081 21.333 -38.482 597.243 1.00 87.69 N ANISOU 2043 ND2 ASN A1081 7770 12970 12579 306 -1135 -3871 N ATOM 2044 N ALA A1082 23.058 -38.491 601.371 1.00 85.57 N ANISOU 2044 N ALA A1082 7371 13095 12046 981 -1705 -4401 N ATOM 2045 CA ALA A1082 22.816 -37.995 602.722 1.00 87.62 C ANISOU 2045 CA ALA A1082 7693 13382 12218 1079 -1836 -4455 C ATOM 2046 C ALA A1082 21.326 -37.917 603.030 1.00 96.75 C ANISOU 2046 C ALA A1082 9119 14365 13278 1065 -1860 -4199 C ATOM 2047 O ALA A1082 20.902 -38.216 604.153 1.00 99.21 O ANISOU 2047 O ALA A1082 9578 14707 13409 1280 -2020 -4157 O ATOM 2048 CB ALA A1082 23.475 -36.628 602.901 1.00 87.78 C ANISOU 2048 CB ALA A1082 7504 13428 12419 848 -1730 -4681 C ATOM 2049 N LYS A1083 20.515 -37.510 602.051 1.00 98.89 N ANISOU 2049 N LYS A1083 9461 14455 13657 814 -1698 -4028 N ATOM 2050 CA LYS A1083 19.083 -37.357 602.283 1.00 89.47 C ANISOU 2050 CA LYS A1083 8513 13093 12388 776 -1711 -3801 C ATOM 2051 C LYS A1083 18.370 -38.693 602.446 1.00 80.57 C ANISOU 2051 C LYS A1083 7612 11953 11049 1038 -1848 -3606 C ATOM 2052 O LYS A1083 17.309 -38.741 603.077 1.00 76.60 O ANISOU 2052 O LYS A1083 7327 11360 10418 1103 -1918 -3456 O ATOM 2053 CB LYS A1083 18.450 -36.573 601.133 1.00 75.92 C ANISOU 2053 CB LYS A1083 6812 11187 10846 439 -1499 -3672 C ATOM 2054 CG LYS A1083 18.859 -35.107 601.086 1.00 72.05 C ANISOU 2054 CG LYS A1083 6177 10639 10560 169 -1348 -3806 C ATOM 2055 CD LYS A1083 18.528 -34.470 599.742 1.00 84.45 C ANISOU 2055 CD LYS A1083 7747 12036 12303 -148 -1113 -3674 C ATOM 2056 CE LYS A1083 17.586 -33.285 599.894 1.00 86.94 C ANISOU 2056 CE LYS A1083 8184 12139 12711 -350 -1021 -3570 C ATOM 2057 NZ LYS A1083 16.220 -33.693 600.333 1.00 54.90 N ANISOU 2057 NZ LYS A1083 4371 7981 8508 -241 -1132 -3378 N ATOM 2058 N LEU A1084 18.929 -39.773 601.905 1.00 77.41 N ANISOU 2058 N LEU A1084 7170 11633 10608 1191 -1879 -3608 N ATOM 2059 CA LEU A1084 18.271 -41.073 601.916 1.00 72.71 C ANISOU 2059 CA LEU A1084 6798 10996 9834 1431 -1982 -3412 C ATOM 2060 C LEU A1084 18.806 -42.012 602.988 1.00 67.13 C ANISOU 2060 C LEU A1084 6163 10410 8931 1796 -2170 -3456 C ATOM 2061 O LEU A1084 18.076 -42.907 603.428 1.00 66.93 O ANISOU 2061 O LEU A1084 6393 10317 8721 2009 -2265 -3266 O ATOM 2062 CB LEU A1084 18.419 -41.744 600.545 1.00 82.02 C ANISOU 2062 CB LEU A1084 7913 12154 11096 1375 -1879 -3359 C ATOM 2063 CG LEU A1084 18.032 -40.875 599.344 1.00 90.44 C ANISOU 2063 CG LEU A1084 8897 13116 12350 1005 -1670 -3314 C ATOM 2064 CD1 LEU A1084 18.327 -41.592 598.030 1.00 72.32 C ANISOU 2064 CD1 LEU A1084 6577 10804 10099 963 -1520 -3253 C ATOM 2065 CD2 LEU A1084 16.564 -40.467 599.415 1.00 71.34 C ANISOU 2065 CD2 LEU A1084 6783 10459 9865 876 -1586 -3041 C ATOM 2066 N LYS A1085 20.056 -41.838 603.418 1.00 64.89 N ANISOU 2066 N LYS A1085 5676 10300 8680 1871 -2220 -3697 N ATOM 2067 CA LYS A1085 20.611 -42.735 604.430 1.00 74.19 C ANISOU 2067 CA LYS A1085 6925 11599 9664 2221 -2402 -3741 C ATOM 2068 C LYS A1085 19.778 -42.768 605.705 1.00 73.23 C ANISOU 2068 C LYS A1085 7049 11441 9335 2373 -2515 -3611 C ATOM 2069 O LYS A1085 19.374 -43.868 606.127 1.00 68.09 O ANISOU 2069 O LYS A1085 6641 10745 8487 2630 -2608 -3433 O ATOM 2070 CB LYS A1085 22.059 -42.328 604.726 1.00 77.66 C ANISOU 2070 CB LYS A1085 7081 12243 10184 2241 -2436 -4050 C ATOM 2071 CG LYS A1085 22.703 -43.121 605.856 1.00 82.17 C ANISOU 2071 CG LYS A1085 7705 12963 10552 2596 -2635 -4121 C ATOM 2072 CD LYS A1085 24.196 -42.845 605.964 1.00 86.82 C ANISOU 2072 CD LYS A1085 7991 13766 11232 2622 -2672 -4441 C ATOM 2073 CE LYS A1085 24.485 -41.451 606.506 1.00 90.92 C ANISOU 2073 CE LYS A1085 8324 14362 11858 2429 -2636 -4651 C ATOM 2074 NZ LYS A1085 24.071 -41.295 607.928 1.00 69.16 N ANISOU 2074 NZ LYS A1085 5711 11655 8912 2597 -2776 -4628 N ATOM 2075 N PRO A1086 19.477 -41.638 606.355 1.00 71.07 N ANISOU 2075 N PRO A1086 6739 11172 9091 2228 -2500 -3682 N ATOM 2076 CA PRO A1086 18.696 -41.710 607.600 1.00 73.15 C ANISOU 2076 CA PRO A1086 7236 11418 9141 2383 -2600 -3565 C ATOM 2077 C PRO A1086 17.297 -42.256 607.399 1.00 69.08 C ANISOU 2077 C PRO A1086 7025 10709 8515 2392 -2569 -3262 C ATOM 2078 O PRO A1086 16.778 -42.950 608.282 1.00 76.58 O ANISOU 2078 O PRO A1086 8224 11638 9235 2616 -2656 -3110 O ATOM 2079 CB PRO A1086 18.676 -40.255 608.083 1.00 78.98 C ANISOU 2079 CB PRO A1086 7830 12187 9992 2168 -2554 -3730 C ATOM 2080 CG PRO A1086 18.818 -39.451 606.837 1.00 69.64 C ANISOU 2080 CG PRO A1086 6458 10920 9081 1840 -2381 -3794 C ATOM 2081 CD PRO A1086 19.708 -40.245 605.928 1.00 71.88 C ANISOU 2081 CD PRO A1086 6616 11267 9427 1901 -2365 -3844 C ATOM 2082 N VAL A1087 16.672 -41.968 606.257 1.00 61.64 N ANISOU 2082 N VAL A1087 6075 9623 7724 2151 -2439 -3166 N ATOM 2083 CA VAL A1087 15.330 -42.477 606.003 1.00 65.00 C ANISOU 2083 CA VAL A1087 6779 9867 8050 2150 -2410 -2893 C ATOM 2084 C VAL A1087 15.374 -43.978 605.754 1.00 69.19 C ANISOU 2084 C VAL A1087 7475 10360 8453 2405 -2459 -2738 C ATOM 2085 O VAL A1087 14.465 -44.713 606.157 1.00 65.15 O ANISOU 2085 O VAL A1087 7260 9732 7764 2545 -2482 -2512 O ATOM 2086 CB VAL A1087 14.685 -41.720 604.829 1.00 58.84 C ANISOU 2086 CB VAL A1087 5934 8955 7468 1818 -2263 -2850 C ATOM 2087 CG1 VAL A1087 13.193 -42.016 604.763 1.00 43.72 C ANISOU 2087 CG1 VAL A1087 4347 6817 5448 1772 -2170 -2553 C ATOM 2088 CG2 VAL A1087 14.930 -40.223 604.965 1.00 60.21 C ANISOU 2088 CG2 VAL A1087 5911 9150 7814 1562 -2186 -3030 C ATOM 2089 N TYR A1088 16.428 -44.460 605.091 1.00 58.89 N ANISOU 2089 N TYR A1088 5991 9139 7244 2464 -2458 -2856 N ATOM 2090 CA TYR A1088 16.564 -45.898 604.891 1.00 68.96 C ANISOU 2090 CA TYR A1088 7421 10367 8415 2720 -2498 -2728 C ATOM 2091 C TYR A1088 16.917 -46.612 606.190 1.00 69.86 C ANISOU 2091 C TYR A1088 7696 10547 8302 3032 -2632 -2704 C ATOM 2092 O TYR A1088 16.607 -47.799 606.345 1.00 75.32 O ANISOU 2092 O TYR A1088 8638 11129 8851 3246 -2653 -2514 O ATOM 2093 CB TYR A1088 17.620 -46.189 603.826 1.00 70.21 C ANISOU 2093 CB TYR A1088 7331 10604 8740 2694 -2452 -2883 C ATOM 2094 CG TYR A1088 17.827 -47.667 603.579 1.00 66.29 C ANISOU 2094 CG TYR A1088 6983 10044 8159 2956 -2481 -2771 C ATOM 2095 CD1 TYR A1088 16.957 -48.383 602.767 1.00 70.19 C ANISOU 2095 CD1 TYR A1088 7655 10346 8667 2953 -2393 -2563 C ATOM 2096 CD2 TYR A1088 18.888 -48.347 604.161 1.00 66.33 C ANISOU 2096 CD2 TYR A1088 6955 10169 8078 3207 -2592 -2878 C ATOM 2097 CE1 TYR A1088 17.138 -49.733 602.540 1.00 70.82 C ANISOU 2097 CE1 TYR A1088 7887 10333 8689 3179 -2393 -2466 C ATOM 2098 CE2 TYR A1088 19.077 -49.699 603.939 1.00 77.79 C ANISOU 2098 CE2 TYR A1088 8555 11539 9462 3438 -2610 -2772 C ATOM 2099 CZ TYR A1088 18.199 -50.386 603.128 1.00 71.55 C ANISOU 2099 CZ TYR A1088 7951 10536 8699 3416 -2502 -2565 C ATOM 2100 OH TYR A1088 18.382 -51.732 602.903 1.00 81.42 O ANISOU 2100 OH TYR A1088 9359 11676 9901 3630 -2498 -2464 O ATOM 2101 N ASP A1089 17.571 -45.919 607.124 1.00 63.56 N ANISOU 2101 N ASP A1089 6761 9918 7472 3060 -2712 -2894 N ATOM 2102 CA ASP A1089 17.917 -46.538 608.399 1.00 57.85 C ANISOU 2102 CA ASP A1089 6179 9282 6522 3357 -2845 -2879 C ATOM 2103 C ASP A1089 16.749 -46.535 609.377 1.00 68.13 C ANISOU 2103 C ASP A1089 7777 10487 7624 3406 -2850 -2673 C ATOM 2104 O ASP A1089 16.627 -47.457 610.191 1.00 78.53 O ANISOU 2104 O ASP A1089 9333 11779 8724 3659 -2912 -2529 O ATOM 2105 CB ASP A1089 19.116 -45.823 609.022 1.00 60.79 C ANISOU 2105 CB ASP A1089 6273 9892 6933 3382 -2935 -3181 C ATOM 2106 CG ASP A1089 20.377 -45.972 608.196 1.00 92.04 C ANISOU 2106 CG ASP A1089 9951 13963 11056 3373 -2935 -3392 C ATOM 2107 OD1 ASP A1089 20.469 -46.946 607.418 1.00 89.88 O ANISOU 2107 OD1 ASP A1089 9740 13609 10801 3456 -2909 -3293 O ATOM 2108 OD2 ASP A1089 21.279 -45.118 608.328 1.00 91.29 O ANISOU 2108 OD2 ASP A1089 9573 14036 11075 3279 -2951 -3663 O ATOM 2109 N SER A1090 15.889 -45.519 609.315 1.00 70.29 N ANISOU 2109 N SER A1090 8043 10700 7966 3165 -2775 -2656 N ATOM 2110 CA SER A1090 14.758 -45.387 610.222 1.00 54.07 C ANISOU 2110 CA SER A1090 6244 8565 5734 3182 -2765 -2487 C ATOM 2111 C SER A1090 13.542 -46.182 609.771 1.00 57.56 C ANISOU 2111 C SER A1090 6993 8776 6102 3178 -2674 -2184 C ATOM 2112 O SER A1090 12.430 -45.905 610.238 1.00 68.06 O ANISOU 2112 O SER A1090 8514 10014 7333 3110 -2623 -2045 O ATOM 2113 CB SER A1090 14.374 -43.912 610.367 1.00 72.53 C ANISOU 2113 CB SER A1090 8435 10935 8187 2921 -2722 -2619 C ATOM 2114 OG SER A1090 13.838 -43.414 609.154 1.00 58.17 O ANISOU 2114 OG SER A1090 6546 8988 6569 2649 -2607 -2586 O ATOM 2115 N LEU A1091 13.720 -47.150 608.879 1.00 60.18 N ANISOU 2115 N LEU A1091 7372 9010 6485 3245 -2641 -2090 N ATOM 2116 CA LEU A1091 12.618 -47.895 608.293 1.00 70.04 C ANISOU 2116 CA LEU A1091 8885 10024 7704 3220 -2536 -1822 C ATOM 2117 C LEU A1091 12.734 -49.373 608.636 1.00 60.16 C ANISOU 2117 C LEU A1091 7888 8673 6297 3488 -2540 -1648 C ATOM 2118 O LEU A1091 13.835 -49.908 608.794 1.00 70.77 O ANISOU 2118 O LEU A1091 9139 10124 7625 3673 -2625 -1755 O ATOM 2119 CB LEU A1091 12.591 -47.722 606.770 1.00 60.17 C ANISOU 2119 CB LEU A1091 7471 8708 6684 3029 -2461 -1854 C ATOM 2120 CG LEU A1091 11.569 -46.734 606.205 1.00 60.93 C ANISOU 2120 CG LEU A1091 7566 8680 6904 2672 -2292 -1798 C ATOM 2121 CD1 LEU A1091 11.582 -45.416 606.966 1.00 66.71 C ANISOU 2121 CD1 LEU A1091 8156 9554 7638 2566 -2363 -1964 C ATOM 2122 CD2 LEU A1091 11.836 -46.503 604.725 1.00 52.65 C ANISOU 2122 CD2 LEU A1091 6332 7578 6093 2433 -2150 -1852 C ATOM 2123 N ASP A1092 11.580 -50.026 608.753 1.00 49.73 N ANISOU 2123 N ASP A1092 6892 7137 4867 3496 -2436 -1381 N ATOM 2124 CA ASP A1092 11.555 -51.467 608.932 1.00 62.98 C ANISOU 2124 CA ASP A1092 8835 8663 6433 3700 -2394 -1193 C ATOM 2125 C ASP A1092 11.908 -52.164 607.619 1.00 60.79 C ANISOU 2125 C ASP A1092 8491 8278 6330 3691 -2341 -1196 C ATOM 2126 O ASP A1092 12.030 -51.541 606.561 1.00 55.06 O ANISOU 2126 O ASP A1092 7536 7585 5799 3521 -2322 -1317 O ATOM 2127 CB ASP A1092 10.184 -51.926 609.423 1.00 67.47 C ANISOU 2127 CB ASP A1092 9762 9017 6858 3668 -2260 -918 C ATOM 2128 CG ASP A1092 9.075 -51.582 608.453 1.00 59.89 C ANISOU 2128 CG ASP A1092 8844 7886 6025 3423 -2128 -820 C ATOM 2129 OD1 ASP A1092 9.042 -50.428 607.978 1.00 61.46 O ANISOU 2129 OD1 ASP A1092 8814 8187 6349 3241 -2161 -961 O ATOM 2130 OD2 ASP A1092 8.242 -52.465 608.160 1.00 51.93 O ANISOU 2130 OD2 ASP A1092 8094 6634 5002 3399 -1981 -608 O ATOM 2131 N ALA A1093 12.068 -53.485 607.698 1.00 68.30 N ANISOU 2131 N ALA A1093 9643 9094 7212 3873 -2307 -1063 N ATOM 2132 CA ALA A1093 12.476 -54.245 606.523 1.00 52.09 C ANISOU 2132 CA ALA A1093 7533 6938 5320 3889 -2254 -1082 C ATOM 2133 C ALA A1093 11.495 -54.058 605.374 1.00 48.95 C ANISOU 2133 C ALA A1093 7167 6358 5075 3659 -2102 -1004 C ATOM 2134 O ALA A1093 11.902 -53.945 604.212 1.00 48.03 O ANISOU 2134 O ALA A1093 6844 6258 5147 3581 -2076 -1131 O ATOM 2135 CB ALA A1093 12.607 -55.726 606.881 1.00 87.41 C ANISOU 2135 CB ALA A1093 12266 11254 9692 4105 -2220 -922 C ATOM 2136 N VAL A1094 10.196 -54.021 605.677 1.00 53.16 N ANISOU 2136 N VAL A1094 7950 6720 5530 3546 -1992 -806 N ATOM 2137 CA VAL A1094 9.189 -53.959 604.623 1.00 44.83 C ANISOU 2137 CA VAL A1094 6949 5473 4610 3272 -1801 -723 C ATOM 2138 C VAL A1094 9.244 -52.616 603.904 1.00 47.94 C ANISOU 2138 C VAL A1094 7043 6017 5157 2967 -1770 -888 C ATOM 2139 O VAL A1094 9.246 -52.554 602.670 1.00 47.75 O ANISOU 2139 O VAL A1094 6895 5952 5296 2768 -1657 -943 O ATOM 2140 CB VAL A1094 7.789 -54.222 605.205 1.00 55.13 C ANISOU 2140 CB VAL A1094 8577 6577 5794 3185 -1667 -486 C ATOM 2141 CG1 VAL A1094 6.737 -54.119 604.114 1.00 56.61 C ANISOU 2141 CG1 VAL A1094 8782 6600 6126 2842 -1452 -428 C ATOM 2142 CG2 VAL A1094 7.740 -55.585 605.876 1.00 72.65 C ANISOU 2142 CG2 VAL A1094 11093 8635 7878 3404 -1633 -315 C ATOM 2143 N ARG A1095 9.281 -51.521 604.663 1.00 53.94 N ANISOU 2143 N ARG A1095 7692 6943 5859 2925 -1864 -967 N ATOM 2144 CA ARG A1095 9.266 -50.203 604.041 1.00 44.15 C ANISOU 2144 CA ARG A1095 6196 5808 4772 2631 -1819 -1104 C ATOM 2145 C ARG A1095 10.582 -49.879 603.351 1.00 41.92 C ANISOU 2145 C ARG A1095 5587 5704 4637 2636 -1891 -1338 C ATOM 2146 O ARG A1095 10.607 -49.015 602.468 1.00 63.54 O ANISOU 2146 O ARG A1095 8131 8479 7534 2371 -1802 -1427 O ATOM 2147 CB ARG A1095 8.940 -49.134 605.083 1.00 51.97 C ANISOU 2147 CB ARG A1095 7164 6908 5674 2588 -1890 -1142 C ATOM 2148 CG ARG A1095 7.520 -49.225 605.625 1.00 49.75 C ANISOU 2148 CG ARG A1095 7164 6461 5276 2509 -1778 -930 C ATOM 2149 CD ARG A1095 7.231 -48.125 606.634 1.00 47.44 C ANISOU 2149 CD ARG A1095 6834 6289 4903 2466 -1842 -995 C ATOM 2150 NE ARG A1095 5.848 -48.160 607.103 1.00 49.69 N ANISOU 2150 NE ARG A1095 7363 6426 5090 2374 -1716 -808 N ATOM 2151 CZ ARG A1095 5.403 -48.945 608.080 1.00 51.42 C ANISOU 2151 CZ ARG A1095 7855 6584 5096 2559 -1719 -654 C ATOM 2152 NH1 ARG A1095 4.126 -48.901 608.434 1.00 50.29 N ANISOU 2152 NH1 ARG A1095 7905 6314 4888 2439 -1579 -503 N ATOM 2153 NH2 ARG A1095 6.227 -49.778 608.703 1.00 54.74 N ANISOU 2153 NH2 ARG A1095 8359 7071 5368 2870 -1857 -646 N ATOM 2154 N ARG A1096 11.672 -50.550 603.725 1.00 44.06 N ANISOU 2154 N ARG A1096 5794 6088 4859 2936 -2044 -1437 N ATOM 2155 CA ARG A1096 12.933 -50.337 603.025 1.00 52.05 C ANISOU 2155 CA ARG A1096 6481 7274 6023 2944 -2097 -1673 C ATOM 2156 C ARG A1096 12.858 -50.824 601.583 1.00 56.78 C ANISOU 2156 C ARG A1096 7056 7749 6769 2788 -1923 -1650 C ATOM 2157 O ARG A1096 13.485 -50.231 600.699 1.00 69.26 O ANISOU 2157 O ARG A1096 8368 9443 8506 2620 -1873 -1815 O ATOM 2158 CB ARG A1096 14.071 -51.033 603.772 1.00 62.02 C ANISOU 2158 CB ARG A1096 7681 8688 7194 3333 -2311 -1783 C ATOM 2159 CG ARG A1096 14.503 -50.305 605.036 1.00 60.30 C ANISOU 2159 CG ARG A1096 7391 8664 6855 3386 -2446 -1896 C ATOM 2160 CD ARG A1096 15.597 -51.053 605.776 1.00 62.35 C ANISOU 2160 CD ARG A1096 7649 9036 7003 3654 -2558 -1973 C ATOM 2161 NE ARG A1096 15.880 -50.453 607.077 1.00 57.28 N ANISOU 2161 NE ARG A1096 6985 8557 6220 3724 -2670 -2061 N ATOM 2162 CZ ARG A1096 16.905 -50.792 607.854 1.00 72.33 C ANISOU 2162 CZ ARG A1096 8835 10619 8029 3945 -2794 -2177 C ATOM 2163 NH1 ARG A1096 17.759 -51.729 607.462 1.00101.56 N ANISOU 2163 NH1 ARG A1096 12496 14333 11759 4114 -2828 -2217 N ATOM 2164 NH2 ARG A1096 17.080 -50.191 609.023 1.00 75.65 N ANISOU 2164 NH2 ARG A1096 9234 11187 8323 4001 -2886 -2261 N ATOM 2165 N ALA A1097 12.103 -51.895 601.325 1.00 48.93 N ANISOU 2165 N ALA A1097 6340 6527 5725 2833 -1821 -1456 N ATOM 2166 CA ALA A1097 11.954 -52.379 599.956 1.00 51.74 C ANISOU 2166 CA ALA A1097 6684 6769 6205 2678 -1654 -1446 C ATOM 2167 C ALA A1097 11.154 -51.399 599.109 1.00 54.27 C ANISOU 2167 C ALA A1097 6945 7062 6614 2299 -1497 -1412 C ATOM 2168 O ALA A1097 11.519 -51.119 597.961 1.00 61.13 O ANISOU 2168 O ALA A1097 7632 7989 7607 2126 -1403 -1512 O ATOM 2169 CB ALA A1097 11.288 -53.753 599.952 1.00 56.56 C ANISOU 2169 CB ALA A1097 7613 7129 6749 2808 -1579 -1262 C ATOM 2170 N ALA A1098 10.053 -50.875 599.653 1.00 56.52 N ANISOU 2170 N ALA A1098 7384 7263 6828 2174 -1463 -1269 N ATOM 2171 CA ALA A1098 9.276 -49.880 598.924 1.00 55.96 C ANISOU 2171 CA ALA A1098 7255 7168 6838 1843 -1334 -1230 C ATOM 2172 C ALA A1098 10.115 -48.653 598.600 1.00 45.33 C ANISOU 2172 C ALA A1098 5602 6013 5610 1707 -1362 -1413 C ATOM 2173 O ALA A1098 9.903 -48.008 597.568 1.00 43.36 O ANISOU 2173 O ALA A1098 5250 5763 5462 1454 -1239 -1416 O ATOM 2174 CB ALA A1098 8.043 -49.484 599.736 1.00 35.06 C ANISOU 2174 CB ALA A1098 4802 4421 4100 1773 -1314 -1071 C ATOM 2175 N LEU A1099 11.067 -48.313 599.472 1.00 50.51 N ANISOU 2175 N LEU A1099 6108 6834 6250 1871 -1520 -1567 N ATOM 2176 CA LEU A1099 11.975 -47.209 599.186 1.00 49.79 C ANISOU 2176 CA LEU A1099 5704 6922 6291 1739 -1539 -1773 C ATOM 2177 C LEU A1099 12.911 -47.552 598.033 1.00 40.45 C ANISOU 2177 C LEU A1099 4328 5818 5224 1708 -1472 -1901 C ATOM 2178 O LEU A1099 13.212 -46.694 597.195 1.00 47.25 O ANISOU 2178 O LEU A1099 4996 6743 6215 1470 -1369 -1985 O ATOM 2179 CB LEU A1099 12.769 -46.855 600.444 1.00 52.51 C ANISOU 2179 CB LEU A1099 5925 7441 6583 1935 -1737 -1935 C ATOM 2180 CG LEU A1099 13.840 -45.771 600.308 1.00 49.04 C ANISOU 2180 CG LEU A1099 5138 7203 6293 1819 -1773 -2192 C ATOM 2181 CD1 LEU A1099 13.223 -44.454 599.869 1.00 48.52 C ANISOU 2181 CD1 LEU A1099 5024 7072 6341 1483 -1638 -2162 C ATOM 2182 CD2 LEU A1099 14.593 -45.604 601.618 1.00 59.24 C ANISOU 2182 CD2 LEU A1099 6319 8682 7506 2050 -1995 -2367 C ATOM 2183 N ILE A1100 13.385 -48.800 597.976 1.00 53.07 N ANISOU 2183 N ILE A1100 5981 7406 6779 1948 -1518 -1917 N ATOM 2184 CA ILE A1100 14.251 -49.216 596.877 1.00 54.46 C ANISOU 2184 CA ILE A1100 5977 7655 7059 1933 -1444 -2051 C ATOM 2185 C ILE A1100 13.475 -49.230 595.566 1.00 49.28 C ANISOU 2185 C ILE A1100 5405 6876 6443 1670 -1237 -1933 C ATOM 2186 O ILE A1100 14.021 -48.914 594.502 1.00 48.59 O ANISOU 2186 O ILE A1100 5127 6879 6456 1510 -1127 -2040 O ATOM 2187 CB ILE A1100 14.876 -50.590 597.177 1.00 51.44 C ANISOU 2187 CB ILE A1100 5654 7266 6624 2279 -1546 -2092 C ATOM 2188 CG1 ILE A1100 15.751 -50.515 598.430 1.00 45.75 C ANISOU 2188 CG1 ILE A1100 4818 6714 5852 2557 -1772 -2226 C ATOM 2189 CG2 ILE A1100 15.701 -51.065 595.992 1.00 51.19 C ANISOU 2189 CG2 ILE A1100 5442 7303 6705 2262 -1451 -2239 C ATOM 2190 CD1 ILE A1100 16.172 -51.868 598.966 1.00 62.63 C ANISOU 2190 CD1 ILE A1100 7084 8811 7902 2945 -1897 -2206 C ATOM 2191 N ASN A1101 12.195 -49.605 595.618 1.00 52.03 N ANISOU 2191 N ASN A1101 6034 7030 6706 1622 -1179 -1718 N ATOM 2192 CA ASN A1101 11.376 -49.585 594.412 1.00 46.38 C ANISOU 2192 CA ASN A1101 5394 6218 6012 1376 -1002 -1612 C ATOM 2193 C ASN A1101 11.307 -48.182 593.824 1.00 47.02 C ANISOU 2193 C ASN A1101 5313 6379 6173 1088 -918 -1628 C ATOM 2194 O ASN A1101 11.365 -48.011 592.601 1.00 49.08 O ANISOU 2194 O ASN A1101 5497 6672 6480 906 -783 -1641 O ATOM 2195 CB ASN A1101 9.975 -50.114 594.719 1.00 44.15 C ANISOU 2195 CB ASN A1101 5414 5729 5633 1367 -968 -1398 C ATOM 2196 CG ASN A1101 9.902 -51.630 594.673 1.00 51.01 C ANISOU 2196 CG ASN A1101 6463 6465 6455 1559 -959 -1364 C ATOM 2197 OD1 ASN A1101 10.907 -52.306 594.456 1.00 56.92 O ANISOU 2197 OD1 ASN A1101 7115 7272 7239 1728 -992 -1497 O ATOM 2198 ND2 ASN A1101 8.708 -52.170 594.879 1.00 60.32 N ANISOU 2198 ND2 ASN A1101 7898 7456 7566 1532 -905 -1193 N ATOM 2199 N MET A1102 11.196 -47.161 594.677 1.00 35.39 N ANISOU 2199 N MET A1102 3796 4938 4714 1046 -990 -1629 N ATOM 2200 CA MET A1102 11.208 -45.792 594.174 1.00 35.97 C ANISOU 2200 CA MET A1102 3719 5062 4884 784 -905 -1649 C ATOM 2201 C MET A1102 12.510 -45.492 593.445 1.00 46.23 C ANISOU 2201 C MET A1102 4741 6528 6297 719 -854 -1845 C ATOM 2202 O MET A1102 12.505 -44.859 592.383 1.00 57.22 O ANISOU 2202 O MET A1102 6053 7938 7752 485 -706 -1826 O ATOM 2203 CB MET A1102 11.010 -44.801 595.318 1.00 35.32 C ANISOU 2203 CB MET A1102 3619 4985 4814 777 -1000 -1661 C ATOM 2204 CG MET A1102 9.672 -44.906 596.013 1.00 36.82 C ANISOU 2204 CG MET A1102 4065 5023 4902 803 -1024 -1472 C ATOM 2205 SD MET A1102 9.340 -43.490 597.078 1.00 35.67 S ANISOU 2205 SD MET A1102 3880 4881 4794 725 -1086 -1496 S ATOM 2206 CE MET A1102 9.232 -42.169 595.871 1.00 38.07 C ANISOU 2206 CE MET A1102 4049 5161 5256 396 -923 -1474 C ATOM 2207 N VAL A1103 13.637 -45.939 594.001 1.00 51.40 N ANISOU 2207 N VAL A1103 5243 7314 6974 928 -970 -2036 N ATOM 2208 CA VAL A1103 14.925 -45.695 593.359 1.00 52.09 C ANISOU 2208 CA VAL A1103 5037 7577 7179 874 -918 -2251 C ATOM 2209 C VAL A1103 14.976 -46.378 591.999 1.00 49.04 C ANISOU 2209 C VAL A1103 4663 7184 6786 802 -763 -2229 C ATOM 2210 O VAL A1103 15.492 -45.816 591.025 1.00 65.56 O ANISOU 2210 O VAL A1103 6582 9368 8961 600 -619 -2304 O ATOM 2211 CB VAL A1103 16.074 -46.158 594.273 1.00 46.73 C ANISOU 2211 CB VAL A1103 4189 7053 6515 1153 -1098 -2467 C ATOM 2212 CG1 VAL A1103 17.416 -45.881 593.618 1.00 65.85 C ANISOU 2212 CG1 VAL A1103 6273 9672 9074 1087 -1036 -2716 C ATOM 2213 CG2 VAL A1103 15.985 -45.463 595.622 1.00 44.20 C ANISOU 2213 CG2 VAL A1103 3862 6760 6174 1221 -1257 -2500 C ATOM 2214 N PHE A1104 14.446 -47.600 591.907 1.00 44.73 N ANISOU 2214 N PHE A1104 4326 6528 6142 957 -779 -2131 N ATOM 2215 CA PHE A1104 14.385 -48.275 590.614 1.00 51.43 C ANISOU 2215 CA PHE A1104 5203 7363 6973 883 -631 -2119 C ATOM 2216 C PHE A1104 13.563 -47.470 589.615 1.00 49.02 C ANISOU 2216 C PHE A1104 4957 7015 6654 573 -468 -1973 C ATOM 2217 O PHE A1104 13.889 -47.427 588.423 1.00 61.48 O ANISOU 2217 O PHE A1104 6443 8673 8244 427 -321 -2019 O ATOM 2218 CB PHE A1104 13.790 -49.676 590.772 1.00 52.27 C ANISOU 2218 CB PHE A1104 5554 7318 6988 1083 -671 -2031 C ATOM 2219 CG PHE A1104 14.680 -50.651 591.500 1.00 53.15 C ANISOU 2219 CG PHE A1104 5621 7464 7109 1413 -808 -2167 C ATOM 2220 CD1 PHE A1104 16.061 -50.562 591.421 1.00 60.95 C ANISOU 2220 CD1 PHE A1104 6321 8648 8190 1504 -842 -2402 C ATOM 2221 CD2 PHE A1104 14.126 -51.670 592.257 1.00 56.79 C ANISOU 2221 CD2 PHE A1104 6331 7758 7488 1639 -899 -2056 C ATOM 2222 CE1 PHE A1104 16.869 -51.465 592.088 1.00 53.99 C ANISOU 2222 CE1 PHE A1104 5394 7805 7315 1836 -985 -2525 C ATOM 2223 CE2 PHE A1104 14.929 -52.576 592.924 1.00 59.61 C ANISOU 2223 CE2 PHE A1104 6670 8133 7845 1967 -1029 -2156 C ATOM 2224 CZ PHE A1104 16.301 -52.472 592.840 1.00 52.46 C ANISOU 2224 CZ PHE A1104 5470 7434 7028 2078 -1083 -2391 C ATOM 2225 N GLN A1105 12.495 -46.822 590.084 1.00 53.94 N ANISOU 2225 N GLN A1105 5734 7521 7241 479 -493 -1796 N ATOM 2226 CA GLN A1105 11.555 -46.173 589.176 1.00 48.20 C ANISOU 2226 CA GLN A1105 5097 6735 6482 228 -362 -1629 C ATOM 2227 C GLN A1105 12.050 -44.799 588.734 1.00 48.13 C ANISOU 2227 C GLN A1105 4906 6813 6568 5 -267 -1661 C ATOM 2228 O GLN A1105 12.031 -44.485 587.539 1.00 70.45 O ANISOU 2228 O GLN A1105 7703 9683 9380 -180 -116 -1617 O ATOM 2229 CB GLN A1105 10.181 -46.061 589.844 1.00 43.21 C ANISOU 2229 CB GLN A1105 4694 5939 5784 230 -423 -1435 C ATOM 2230 CG GLN A1105 9.525 -47.407 590.136 1.00 32.60 C ANISOU 2230 CG GLN A1105 3559 4480 4348 399 -472 -1374 C ATOM 2231 CD GLN A1105 8.232 -47.273 590.918 1.00 32.49 C ANISOU 2231 CD GLN A1105 3748 4319 4279 400 -523 -1203 C ATOM 2232 OE1 GLN A1105 7.562 -46.244 590.857 1.00 40.91 O ANISOU 2232 OE1 GLN A1105 4823 5361 5361 239 -493 -1100 O ATOM 2233 NE2 GLN A1105 7.878 -48.315 591.660 1.00 38.90 N ANISOU 2233 NE2 GLN A1105 4724 5025 5030 585 -591 -1171 N ATOM 2234 N MET A1106 12.497 -43.966 589.676 1.00 52.69 N ANISOU 2234 N MET A1106 5366 7414 7239 16 -347 -1741 N ATOM 2235 CA MET A1106 12.873 -42.589 589.369 1.00 62.19 C ANISOU 2235 CA MET A1106 6417 8656 8556 -211 -249 -1764 C ATOM 2236 C MET A1106 14.301 -42.250 589.775 1.00 64.72 C ANISOU 2236 C MET A1106 6453 9129 9009 -184 -276 -2022 C ATOM 2237 O MET A1106 14.701 -41.083 589.680 1.00 59.23 O ANISOU 2237 O MET A1106 5615 8454 8436 -374 -196 -2072 O ATOM 2238 CB MET A1106 11.899 -41.610 590.034 1.00 57.30 C ANISOU 2238 CB MET A1106 5918 7897 7955 -291 -289 -1617 C ATOM 2239 CG MET A1106 11.874 -41.659 591.551 1.00 41.98 C ANISOU 2239 CG MET A1106 3995 5935 6022 -107 -472 -1690 C ATOM 2240 SD MET A1106 10.431 -40.809 592.231 1.00 49.93 S ANISOU 2240 SD MET A1106 5199 6761 7010 -174 -506 -1493 S ATOM 2241 CE MET A1106 10.437 -39.282 591.289 1.00 62.30 C ANISOU 2241 CE MET A1106 6677 8283 8710 -482 -330 -1427 C ATOM 2242 N GLY A1107 15.086 -43.226 590.205 1.00 70.81 N ANISOU 2242 N GLY A1107 7132 10004 9769 46 -384 -2192 N ATOM 2243 CA GLY A1107 16.460 -42.980 590.584 1.00 60.84 C ANISOU 2243 CA GLY A1107 5571 8915 8630 92 -427 -2462 C ATOM 2244 C GLY A1107 16.575 -42.297 591.936 1.00 56.43 C ANISOU 2244 C GLY A1107 4950 8363 8128 158 -586 -2549 C ATOM 2245 O GLY A1107 15.619 -41.745 592.479 1.00 79.40 O ANISOU 2245 O GLY A1107 8027 11135 11005 110 -624 -2399 O ATOM 2246 N GLU A1108 17.791 -42.334 592.485 1.00 62.86 N ANISOU 2246 N GLU A1108 5501 9356 9029 276 -684 -2817 N ATOM 2247 CA GLU A1108 18.013 -41.701 593.779 1.00 63.91 C ANISOU 2247 CA GLU A1108 5543 9533 9205 346 -849 -2944 C ATOM 2248 C GLU A1108 17.958 -40.185 593.672 1.00 57.67 C ANISOU 2248 C GLU A1108 4656 8694 8562 40 -730 -2964 C ATOM 2249 O GLU A1108 17.560 -39.516 594.629 1.00 68.02 O ANISOU 2249 O GLU A1108 6012 9948 9884 39 -828 -2966 O ATOM 2250 CB GLU A1108 19.352 -42.148 594.374 1.00 72.62 C ANISOU 2250 CB GLU A1108 6368 10867 10358 563 -1000 -3245 C ATOM 2251 CG GLU A1108 20.573 -41.836 593.525 1.00 98.50 C ANISOU 2251 CG GLU A1108 9312 14314 13800 410 -860 -3475 C ATOM 2252 CD GLU A1108 21.865 -42.269 594.200 1.00105.57 C ANISOU 2252 CD GLU A1108 9968 15422 14723 645 -1015 -3761 C ATOM 2253 OE1 GLU A1108 21.824 -42.606 595.404 1.00 81.07 O ANISOU 2253 OE1 GLU A1108 6954 12335 11513 902 -1234 -3779 O ATOM 2254 OE2 GLU A1108 22.916 -42.275 593.527 1.00128.39 O ANISOU 2254 OE2 GLU A1108 12662 18423 17696 571 -892 -3923 O ATOM 2255 N THR A1109 18.352 -39.627 592.526 1.00 58.16 N ANISOU 2255 N THR A1109 4593 8768 8736 -220 -511 -2977 N ATOM 2256 CA THR A1109 18.252 -38.184 592.342 1.00 65.26 C ANISOU 2256 CA THR A1109 5434 9578 9784 -521 -371 -2964 C ATOM 2257 C THR A1109 16.807 -37.709 592.434 1.00 60.75 C ANISOU 2257 C THR A1109 5165 8775 9141 -593 -353 -2675 C ATOM 2258 O THR A1109 16.549 -36.590 592.891 1.00 68.78 O ANISOU 2258 O THR A1109 6176 9694 10264 -734 -337 -2680 O ATOM 2259 CB THR A1109 18.851 -37.782 590.994 1.00 86.03 C ANISOU 2259 CB THR A1109 7924 12248 12515 -781 -114 -2981 C ATOM 2260 OG1 THR A1109 18.209 -38.517 589.943 1.00102.41 O ANISOU 2260 OG1 THR A1109 10203 14266 14441 -776 -12 -2755 O ATOM 2261 CG2 THR A1109 20.348 -38.061 590.968 1.00 88.94 C ANISOU 2261 CG2 THR A1109 7941 12858 12994 -740 -116 -3309 C ATOM 2262 N GLY A1110 15.856 -38.537 592.007 1.00 52.16 N ANISOU 2262 N GLY A1110 4333 7599 7887 -500 -354 -2441 N ATOM 2263 CA GLY A1110 14.458 -38.156 592.028 1.00 65.71 C ANISOU 2263 CA GLY A1110 6318 9115 9535 -561 -336 -2176 C ATOM 2264 C GLY A1110 13.818 -38.322 593.389 1.00 57.59 C ANISOU 2264 C GLY A1110 5416 8033 8433 -369 -532 -2163 C ATOM 2265 O GLY A1110 13.157 -37.405 593.887 1.00 60.45 O ANISOU 2265 O GLY A1110 5853 8273 8844 -456 -537 -2097 O ATOM 2266 N VAL A1111 14.007 -39.492 594.005 1.00 49.79 N ANISOU 2266 N VAL A1111 4463 7130 7326 -102 -687 -2224 N ATOM 2267 CA VAL A1111 13.434 -39.729 595.326 1.00 54.33 C ANISOU 2267 CA VAL A1111 5173 7668 7801 94 -866 -2204 C ATOM 2268 C VAL A1111 14.009 -38.747 596.335 1.00 51.95 C ANISOU 2268 C VAL A1111 4694 7438 7607 72 -957 -2415 C ATOM 2269 O VAL A1111 13.334 -38.368 597.300 1.00 64.90 O ANISOU 2269 O VAL A1111 6448 9010 9202 121 -1046 -2379 O ATOM 2270 CB VAL A1111 13.668 -41.190 595.762 1.00 52.75 C ANISOU 2270 CB VAL A1111 5042 7543 7456 395 -1005 -2228 C ATOM 2271 CG1 VAL A1111 13.149 -42.157 594.705 1.00 57.89 C ANISOU 2271 CG1 VAL A1111 5853 8117 8024 395 -900 -2054 C ATOM 2272 CG2 VAL A1111 15.138 -41.431 596.041 1.00 62.13 C ANISOU 2272 CG2 VAL A1111 5957 8944 8707 522 -1098 -2507 C ATOM 2273 N ALA A1112 15.259 -38.322 596.138 1.00 60.71 N ANISOU 2273 N ALA A1112 5513 8693 8860 -9 -931 -2657 N ATOM 2274 CA ALA A1112 15.848 -37.311 597.007 1.00 62.24 C ANISOU 2274 CA ALA A1112 5508 8958 9181 -69 -1001 -2892 C ATOM 2275 C ALA A1112 15.171 -35.955 596.849 1.00 60.59 C ANISOU 2275 C ALA A1112 5357 8564 9102 -335 -867 -2803 C ATOM 2276 O ALA A1112 15.235 -35.135 597.771 1.00 56.47 O ANISOU 2276 O ALA A1112 4762 8042 8654 -364 -940 -2950 O ATOM 2277 CB ALA A1112 17.345 -37.182 596.723 1.00 50.58 C ANISOU 2277 CB ALA A1112 3685 7683 7850 -120 -981 -3185 C ATOM 2278 N GLY A1113 14.527 -35.703 595.707 1.00 55.77 N ANISOU 2278 N GLY A1113 4876 7798 8516 -520 -677 -2570 N ATOM 2279 CA GLY A1113 13.824 -34.446 595.526 1.00 44.61 C ANISOU 2279 CA GLY A1113 3541 6187 7221 -744 -552 -2454 C ATOM 2280 C GLY A1113 12.649 -34.281 596.468 1.00 56.56 C ANISOU 2280 C GLY A1113 5265 7577 8649 -642 -659 -2339 C ATOM 2281 O GLY A1113 12.285 -33.155 596.821 1.00 68.02 O ANISOU 2281 O GLY A1113 6723 8899 10222 -772 -618 -2353 O ATOM 2282 N PHE A1114 12.039 -35.390 596.889 1.00 45.28 N ANISOU 2282 N PHE A1114 4011 6176 7016 -413 -781 -2229 N ATOM 2283 CA PHE A1114 10.898 -35.358 597.802 1.00 48.15 C ANISOU 2283 CA PHE A1114 4579 6439 7277 -307 -870 -2118 C ATOM 2284 C PHE A1114 11.399 -34.982 599.193 1.00 53.23 C ANISOU 2284 C PHE A1114 5106 7187 7932 -203 -1027 -2367 C ATOM 2285 O PHE A1114 11.551 -35.817 600.087 1.00 57.46 O ANISOU 2285 O PHE A1114 5676 7848 8308 35 -1193 -2434 O ATOM 2286 CB PHE A1114 10.184 -36.704 597.816 1.00 65.54 C ANISOU 2286 CB PHE A1114 6994 8641 9267 -110 -932 -1938 C ATOM 2287 CG PHE A1114 9.588 -37.093 596.491 1.00 47.22 C ANISOU 2287 CG PHE A1114 4792 6229 6919 -209 -791 -1711 C ATOM 2288 CD1 PHE A1114 10.362 -37.700 595.519 1.00 37.31 C ANISOU 2288 CD1 PHE A1114 3442 5066 5667 -230 -727 -1740 C ATOM 2289 CD2 PHE A1114 8.249 -36.861 596.224 1.00 48.15 C ANISOU 2289 CD2 PHE A1114 5107 6188 7002 -274 -728 -1484 C ATOM 2290 CE1 PHE A1114 9.815 -38.061 594.305 1.00 48.99 C ANISOU 2290 CE1 PHE A1114 5030 6482 7101 -318 -603 -1549 C ATOM 2291 CE2 PHE A1114 7.696 -37.220 595.011 1.00 33.19 C ANISOU 2291 CE2 PHE A1114 3310 4235 5065 -357 -616 -1291 C ATOM 2292 CZ PHE A1114 8.478 -37.821 594.051 1.00 41.65 C ANISOU 2292 CZ PHE A1114 4296 5403 6126 -381 -554 -1324 C ATOM 2293 N THR A1115 11.655 -33.686 599.377 1.00 53.95 N ANISOU 2293 N THR A1115 5063 7223 8211 -385 -972 -2508 N ATOM 2294 CA THR A1115 12.223 -33.215 600.635 1.00 57.91 C ANISOU 2294 CA THR A1115 5419 7842 8742 -317 -1115 -2791 C ATOM 2295 C THR A1115 11.235 -33.388 601.784 1.00 62.46 C ANISOU 2295 C THR A1115 6195 8388 9149 -145 -1237 -2727 C ATOM 2296 O THR A1115 11.541 -34.035 602.792 1.00 61.70 O ANISOU 2296 O THR A1115 6093 8461 8890 81 -1417 -2846 O ATOM 2297 CB THR A1115 12.641 -31.748 600.503 1.00 59.47 C ANISOU 2297 CB THR A1115 5463 7944 9189 -568 -984 -2928 C ATOM 2298 OG1 THR A1115 11.495 -30.950 600.177 1.00 75.27 O ANISOU 2298 OG1 THR A1115 7623 9695 11280 -721 -869 -2745 O ATOM 2299 CG2 THR A1115 13.692 -31.584 599.413 1.00 49.09 C ANISOU 2299 CG2 THR A1115 3973 6667 8012 -728 -829 -2970 C ATOM 2300 N ASN A1116 10.030 -32.829 601.642 1.00 63.47 N ANISOU 2300 N ASN A1116 6503 8307 9305 -241 -1139 -2533 N ATOM 2301 CA ASN A1116 9.081 -32.837 602.751 1.00 52.01 C ANISOU 2301 CA ASN A1116 5219 6826 7717 -109 -1228 -2498 C ATOM 2302 C ASN A1116 8.557 -34.235 603.046 1.00 39.45 C ANISOU 2302 C ASN A1116 3825 5299 5865 126 -1315 -2329 C ATOM 2303 O ASN A1116 8.264 -34.551 604.204 1.00 53.89 O ANISOU 2303 O ASN A1116 5745 7204 7527 301 -1436 -2375 O ATOM 2304 CB ASN A1116 7.917 -31.892 602.451 1.00 58.43 C ANISOU 2304 CB ASN A1116 6158 7399 8645 -265 -1092 -2337 C ATOM 2305 CG ASN A1116 8.159 -30.488 602.967 1.00 69.39 C ANISOU 2305 CG ASN A1116 7414 8718 10235 -408 -1067 -2554 C ATOM 2306 OD1 ASN A1116 7.412 -29.987 603.808 1.00 68.56 O ANISOU 2306 OD1 ASN A1116 7393 8546 10111 -373 -1094 -2585 O ATOM 2307 ND2 ASN A1116 9.215 -29.848 602.474 1.00 74.57 N ANISOU 2307 ND2 ASN A1116 7856 9386 11092 -576 -1003 -2722 N ATOM 2308 N SER A1117 8.426 -35.081 602.025 1.00 54.80 N ANISOU 2308 N SER A1117 5846 7208 7767 127 -1244 -2136 N ATOM 2309 CA SER A1117 7.821 -36.392 602.229 1.00 48.68 C ANISOU 2309 CA SER A1117 5279 6447 6772 322 -1296 -1963 C ATOM 2310 C SER A1117 8.772 -37.353 602.933 1.00 41.73 C ANISOU 2310 C SER A1117 4346 5765 5745 562 -1460 -2100 C ATOM 2311 O SER A1117 8.340 -38.145 603.779 1.00 46.40 O ANISOU 2311 O SER A1117 5108 6387 6136 764 -1550 -2031 O ATOM 2312 CB SER A1117 7.377 -36.975 600.891 1.00 43.90 C ANISOU 2312 CB SER A1117 4764 5740 6176 239 -1168 -1739 C ATOM 2313 OG SER A1117 6.610 -36.035 600.161 1.00 64.96 O ANISOU 2313 OG SER A1117 7459 8245 8978 30 -1029 -1616 O ATOM 2314 N LEU A1118 10.061 -37.313 602.590 1.00 40.19 N ANISOU 2314 N LEU A1118 3919 5705 5646 549 -1496 -2290 N ATOM 2315 CA LEU A1118 11.030 -38.146 603.294 1.00 47.09 C ANISOU 2315 CA LEU A1118 4714 6786 6393 800 -1673 -2444 C ATOM 2316 C LEU A1118 11.030 -37.831 604.783 1.00 51.96 C ANISOU 2316 C LEU A1118 5339 7513 6889 945 -1834 -2591 C ATOM 2317 O LEU A1118 11.170 -38.731 605.619 1.00 48.83 O ANISOU 2317 O LEU A1118 5041 7231 6282 1212 -1981 -2586 O ATOM 2318 CB LEU A1118 12.426 -37.942 602.705 1.00 58.39 C ANISOU 2318 CB LEU A1118 5844 8359 7981 735 -1677 -2667 C ATOM 2319 CG LEU A1118 12.717 -38.595 601.352 1.00 45.43 C ANISOU 2319 CG LEU A1118 4179 6684 6398 673 -1556 -2562 C ATOM 2320 CD1 LEU A1118 13.996 -38.034 600.754 1.00 42.11 C ANISOU 2320 CD1 LEU A1118 3438 6388 6175 533 -1512 -2799 C ATOM 2321 CD2 LEU A1118 12.821 -40.104 601.496 1.00 47.10 C ANISOU 2321 CD2 LEU A1118 4520 6952 6426 952 -1652 -2476 C ATOM 2322 N ARG A1119 10.871 -36.553 605.128 1.00 43.69 N ANISOU 2322 N ARG A1119 4200 6431 5969 777 -1803 -2722 N ATOM 2323 CA ARG A1119 10.784 -36.160 606.529 1.00 42.41 C ANISOU 2323 CA ARG A1119 4049 6375 5689 894 -1942 -2877 C ATOM 2324 C ARG A1119 9.685 -36.931 607.246 1.00 50.42 C ANISOU 2324 C ARG A1119 5371 7336 6451 1074 -1971 -2657 C ATOM 2325 O ARG A1119 9.853 -37.350 608.397 1.00 43.08 O ANISOU 2325 O ARG A1119 4499 6561 5308 1301 -2130 -2732 O ATOM 2326 CB ARG A1119 10.530 -34.656 606.619 1.00 53.46 C ANISOU 2326 CB ARG A1119 5354 7667 7291 653 -1838 -2990 C ATOM 2327 CG ARG A1119 10.529 -34.093 608.024 1.00 65.65 C ANISOU 2327 CG ARG A1119 6899 9302 8744 747 -1906 -3127 C ATOM 2328 CD ARG A1119 10.130 -32.628 608.018 1.00 70.06 C ANISOU 2328 CD ARG A1119 7394 9708 9518 507 -1780 -3209 C ATOM 2329 NE ARG A1119 8.744 -32.444 607.598 1.00 58.26 N ANISOU 2329 NE ARG A1119 6091 7997 8050 400 -1697 -3030 N ATOM 2330 CZ ARG A1119 8.146 -31.263 607.479 1.00 77.74 C ANISOU 2330 CZ ARG A1119 8554 10280 10705 208 -1574 -3045 C ATOM 2331 NH1 ARG A1119 8.810 -30.146 607.747 1.00 89.59 N ANISOU 2331 NH1 ARG A1119 9879 11781 12379 91 -1516 -3227 N ATOM 2332 NH2 ARG A1119 6.880 -31.199 607.091 1.00 77.64 N ANISOU 2332 NH2 ARG A1119 8730 10069 10702 150 -1470 -2819 N ATOM 2333 N MET A1120 8.548 -37.127 606.576 1.00 50.22 N ANISOU 2333 N MET A1120 5541 7098 6440 972 -1814 -2386 N ATOM 2334 CA MET A1120 7.428 -37.822 607.200 1.00 48.27 C ANISOU 2334 CA MET A1120 5577 6784 5979 1105 -1806 -2179 C ATOM 2335 C MET A1120 7.756 -39.290 607.444 1.00 51.09 C ANISOU 2335 C MET A1120 6063 7224 6124 1364 -1901 -2080 C ATOM 2336 O MET A1120 7.426 -39.837 608.502 1.00 54.70 O ANISOU 2336 O MET A1120 6693 7739 6351 1562 -1982 -2030 O ATOM 2337 CB MET A1120 6.184 -37.691 606.321 1.00 49.89 C ANISOU 2337 CB MET A1120 5923 6757 6274 924 -1618 -1937 C ATOM 2338 CG MET A1120 5.944 -36.288 605.781 1.00 54.32 C ANISOU 2338 CG MET A1120 6357 7204 7080 669 -1509 -1998 C ATOM 2339 SD MET A1120 5.932 -35.029 607.069 1.00 56.73 S ANISOU 2339 SD MET A1120 6577 7566 7411 653 -1578 -2246 S ATOM 2340 CE MET A1120 4.251 -35.183 607.650 1.00 61.01 C ANISOU 2340 CE MET A1120 7389 7982 7811 692 -1501 -2039 C ATOM 2341 N LEU A1121 8.404 -39.942 606.476 1.00 42.49 N ANISOU 2341 N LEU A1121 4901 6135 5107 1371 -1882 -2048 N ATOM 2342 CA LEU A1121 8.722 -41.360 606.619 1.00 48.01 C ANISOU 2342 CA LEU A1121 5728 6881 5633 1622 -1959 -1950 C ATOM 2343 C LEU A1121 9.682 -41.592 607.777 1.00 44.08 C ANISOU 2343 C LEU A1121 5157 6615 4976 1887 -2178 -2135 C ATOM 2344 O LEU A1121 9.488 -42.504 608.590 1.00 50.19 O ANISOU 2344 O LEU A1121 6137 7418 5516 2134 -2262 -2026 O ATOM 2345 CB LEU A1121 9.320 -41.896 605.320 1.00 44.16 C ANISOU 2345 CB LEU A1121 5138 6361 5278 1567 -1894 -1927 C ATOM 2346 CG LEU A1121 8.458 -41.755 604.067 1.00 36.22 C ANISOU 2346 CG LEU A1121 4197 5156 4407 1322 -1692 -1748 C ATOM 2347 CD1 LEU A1121 9.168 -42.382 602.883 1.00 36.18 C ANISOU 2347 CD1 LEU A1121 4093 5159 4494 1302 -1642 -1752 C ATOM 2348 CD2 LEU A1121 7.091 -42.388 604.275 1.00 49.79 C ANISOU 2348 CD2 LEU A1121 6213 6711 5993 1346 -1610 -1499 C ATOM 2349 N GLN A1122 10.731 -40.774 607.866 1.00 43.21 N ANISOU 2349 N GLN A1122 4753 6676 4987 1842 -2273 -2417 N ATOM 2350 CA GLN A1122 11.691 -40.934 608.950 1.00 52.72 C ANISOU 2350 CA GLN A1122 5875 8084 6074 2067 -2415 -2572 C ATOM 2351 C GLN A1122 11.031 -40.732 610.306 1.00 52.00 C ANISOU 2351 C GLN A1122 5959 8018 5780 2168 -2453 -2533 C ATOM 2352 O GLN A1122 11.466 -41.321 611.302 1.00 48.92 O ANISOU 2352 O GLN A1122 5640 7747 5199 2416 -2548 -2535 O ATOM 2353 CB GLN A1122 12.849 -39.955 608.770 1.00 53.66 C ANISOU 2353 CB GLN A1122 5655 8324 6410 1930 -2406 -2851 C ATOM 2354 CG GLN A1122 13.938 -40.083 609.822 1.00 62.99 C ANISOU 2354 CG GLN A1122 6728 9714 7493 2146 -2527 -3025 C ATOM 2355 CD GLN A1122 15.178 -39.287 609.469 1.00 80.17 C ANISOU 2355 CD GLN A1122 8565 12005 9891 2015 -2505 -3300 C ATOM 2356 OE1 GLN A1122 15.258 -38.681 608.400 1.00 72.11 O ANISOU 2356 OE1 GLN A1122 7399 10900 9099 1761 -2384 -3343 O ATOM 2357 NE2 GLN A1122 16.156 -39.287 610.368 1.00 91.52 N ANISOU 2357 NE2 GLN A1122 9881 13636 11255 2185 -2613 -3487 N ATOM 2358 N GLN A1123 9.979 -39.919 610.360 1.00 46.06 N ANISOU 2358 N GLN A1123 5281 7157 5062 1982 -2374 -2500 N ATOM 2359 CA GLN A1123 9.271 -39.620 611.595 1.00 49.77 C ANISOU 2359 CA GLN A1123 5903 7652 5353 2048 -2387 -2479 C ATOM 2360 C GLN A1123 8.055 -40.512 611.809 1.00 47.02 C ANISOU 2360 C GLN A1123 5899 7182 4784 2147 -2345 -2205 C ATOM 2361 O GLN A1123 7.218 -40.202 612.662 1.00 75.69 O ANISOU 2361 O GLN A1123 9677 10801 8282 2150 -2314 -2167 O ATOM 2362 CB GLN A1123 8.838 -38.153 611.608 1.00 52.00 C ANISOU 2362 CB GLN A1123 6062 7882 5814 1791 -2311 -2627 C ATOM 2363 CG GLN A1123 9.991 -37.170 611.556 1.00 49.13 C ANISOU 2363 CG GLN A1123 5378 7623 5668 1679 -2324 -2897 C ATOM 2364 CD GLN A1123 9.527 -35.728 611.572 1.00 57.81 C ANISOU 2364 CD GLN A1123 6380 8628 6958 1428 -2227 -3023 C ATOM 2365 OE1 GLN A1123 8.347 -35.443 611.783 1.00 45.33 O ANISOU 2365 OE1 GLN A1123 4968 6927 5329 1364 -2166 -2929 O ATOM 2366 NE2 GLN A1123 10.456 -34.807 611.345 1.00 68.18 N ANISOU 2366 NE2 GLN A1123 7426 9984 8497 1285 -2199 -3238 N ATOM 2367 N LYS A1124 7.927 -41.597 611.049 1.00 51.66 N ANISOU 2367 N LYS A1124 6618 7663 5348 2211 -2310 -2009 N ATOM 2368 CA LYS A1124 6.821 -42.538 611.195 1.00 55.31 C ANISOU 2368 CA LYS A1124 7407 7958 5651 2274 -2196 -1712 C ATOM 2369 C LYS A1124 5.471 -41.895 610.883 1.00 53.98 C ANISOU 2369 C LYS A1124 7324 7600 5586 2019 -1998 -1598 C ATOM 2370 O LYS A1124 4.424 -42.445 611.237 1.00 67.77 O ANISOU 2370 O LYS A1124 9323 9233 7194 2045 -1896 -1394 O ATOM 2371 CB LYS A1124 6.798 -43.144 612.605 1.00 59.47 C ANISOU 2371 CB LYS A1124 8133 8601 5861 2550 -2298 -1661 C ATOM 2372 CG LYS A1124 8.134 -43.718 613.072 1.00 68.53 C ANISOU 2372 CG LYS A1124 9179 9902 6957 2782 -2420 -1748 C ATOM 2373 CD LYS A1124 8.207 -45.225 612.877 1.00 80.51 C ANISOU 2373 CD LYS A1124 10913 11316 8362 2981 -2403 -1526 C ATOM 2374 CE LYS A1124 9.601 -45.758 613.175 1.00 79.40 C ANISOU 2374 CE LYS A1124 10646 11323 8201 3203 -2526 -1643 C ATOM 2375 NZ LYS A1124 10.603 -45.288 612.177 1.00 78.03 N ANISOU 2375 NZ LYS A1124 10148 11227 8272 3101 -2577 -1856 N ATOM 2376 N ARG A1125 5.469 -40.731 610.228 1.00 44.09 N ANISOU 2376 N ARG A1125 5864 6308 4581 1775 -1937 -1725 N ATOM 2377 CA ARG A1125 4.227 -40.062 609.834 1.00 45.09 C ANISOU 2377 CA ARG A1125 6048 6254 4830 1546 -1761 -1621 C ATOM 2378 C ARG A1125 3.791 -40.616 608.479 1.00 48.05 C ANISOU 2378 C ARG A1125 6469 6449 5340 1417 -1620 -1424 C ATOM 2379 O ARG A1125 3.974 -40.002 607.426 1.00 43.72 O ANISOU 2379 O ARG A1125 5760 5839 5013 1229 -1557 -1460 O ATOM 2380 CB ARG A1125 4.414 -38.551 609.790 1.00 51.77 C ANISOU 2380 CB ARG A1125 6672 7121 5878 1364 -1759 -1836 C ATOM 2381 CG ARG A1125 4.485 -37.887 611.159 1.00 47.34 C ANISOU 2381 CG ARG A1125 6093 6709 5187 1451 -1862 -2031 C ATOM 2382 CD ARG A1125 4.097 -36.412 611.094 1.00 44.83 C ANISOU 2382 CD ARG A1125 5639 6312 5082 1234 -1786 -2176 C ATOM 2383 NE ARG A1125 5.251 -35.527 610.955 1.00 43.64 N ANISOU 2383 NE ARG A1125 5213 6258 5109 1154 -1872 -2453 N ATOM 2384 CZ ARG A1125 5.171 -34.230 610.669 1.00 53.13 C ANISOU 2384 CZ ARG A1125 6266 7364 6556 944 -1799 -2591 C ATOM 2385 NH1 ARG A1125 3.989 -33.658 610.477 1.00 48.44 N ANISOU 2385 NH1 ARG A1125 5769 6580 6055 813 -1653 -2472 N ATOM 2386 NH2 ARG A1125 6.275 -33.503 610.569 1.00 62.39 N ANISOU 2386 NH2 ARG A1125 7189 8623 7893 865 -1866 -2852 N ATOM 2387 N TRP A1126 3.186 -41.803 608.520 1.00 58.56 N ANISOU 2387 N TRP A1126 8031 7695 6525 1515 -1563 -1214 N ATOM 2388 CA TRP A1126 2.846 -42.527 607.300 1.00 40.78 C ANISOU 2388 CA TRP A1126 5833 5294 4370 1422 -1447 -1048 C ATOM 2389 C TRP A1126 1.681 -41.873 606.566 1.00 40.47 C ANISOU 2389 C TRP A1126 5790 5105 4481 1179 -1289 -955 C ATOM 2390 O TRP A1126 1.854 -41.368 605.452 1.00 42.11 O ANISOU 2390 O TRP A1126 5852 5270 4878 1016 -1241 -975 O ATOM 2391 CB TRP A1126 2.509 -43.985 607.618 1.00 38.51 C ANISOU 2391 CB TRP A1126 5800 4937 3895 1591 -1421 -865 C ATOM 2392 CG TRP A1126 3.513 -44.655 608.504 1.00 43.17 C ANISOU 2392 CG TRP A1126 6435 5667 4301 1873 -1583 -924 C ATOM 2393 CD1 TRP A1126 3.271 -45.256 609.702 1.00 37.71 C ANISOU 2393 CD1 TRP A1126 5961 5008 3361 2074 -1623 -842 C ATOM 2394 CD2 TRP A1126 4.921 -44.784 608.267 1.00 46.54 C ANISOU 2394 CD2 TRP A1126 6683 6232 4770 1997 -1729 -1077 C ATOM 2395 NE1 TRP A1126 4.437 -45.757 610.224 1.00 58.43 N ANISOU 2395 NE1 TRP A1126 8560 7782 5860 2334 -1801 -924 N ATOM 2396 CE2 TRP A1126 5.466 -45.480 609.363 1.00 39.63 C ANISOU 2396 CE2 TRP A1126 5924 5472 3662 2292 -1873 -1080 C ATOM 2397 CE3 TRP A1126 5.772 -44.381 607.234 1.00 50.92 C ANISOU 2397 CE3 TRP A1126 6986 6831 5530 1890 -1747 -1212 C ATOM 2398 CZ2 TRP A1126 6.822 -45.782 609.456 1.00 51.94 C ANISOU 2398 CZ2 TRP A1126 7340 7196 5200 2495 -2049 -1225 C ATOM 2399 CZ3 TRP A1126 7.121 -44.682 607.329 1.00 48.15 C ANISOU 2399 CZ3 TRP A1126 6488 6642 5166 2070 -1902 -1365 C ATOM 2400 CH2 TRP A1126 7.631 -45.375 608.431 1.00 60.49 C ANISOU 2400 CH2 TRP A1126 8155 8324 6506 2376 -2060 -1377 C ATOM 2401 N ASP A1127 0.495 -41.868 607.184 1.00 47.45 N ANISOU 2401 N ASP A1127 6833 5919 5277 1160 -1206 -853 N ATOM 2402 CA ASP A1127 -0.682 -41.309 606.525 1.00 40.44 C ANISOU 2402 CA ASP A1127 5939 4900 4525 956 -1066 -765 C ATOM 2403 C ASP A1127 -0.409 -39.910 605.993 1.00 41.06 C ANISOU 2403 C ASP A1127 5802 4985 4815 801 -1075 -891 C ATOM 2404 O ASP A1127 -0.931 -39.532 604.938 1.00 30.04 O ANISOU 2404 O ASP A1127 4352 3489 3573 638 -986 -815 O ATOM 2405 CB ASP A1127 -1.865 -41.272 607.496 1.00 29.83 C ANISOU 2405 CB ASP A1127 4749 3521 3062 970 -991 -699 C ATOM 2406 CG ASP A1127 -2.390 -42.652 607.828 1.00 45.85 C ANISOU 2406 CG ASP A1127 7014 5490 4915 1067 -923 -532 C ATOM 2407 OD1 ASP A1127 -1.834 -43.639 607.305 1.00 63.44 O ANISOU 2407 OD1 ASP A1127 9291 7693 7122 1134 -943 -469 O ATOM 2408 OD2 ASP A1127 -3.360 -42.750 608.608 1.00 55.97 O ANISOU 2408 OD2 ASP A1127 8435 6744 6089 1073 -838 -467 O ATOM 2409 N GLU A1128 0.406 -39.132 606.704 1.00 42.05 N ANISOU 2409 N GLU A1128 5806 5224 4948 851 -1181 -1086 N ATOM 2410 CA GLU A1128 0.712 -37.779 606.258 1.00 42.17 C ANISOU 2410 CA GLU A1128 5623 5219 5179 695 -1174 -1216 C ATOM 2411 C GLU A1128 1.642 -37.788 605.052 1.00 43.78 C ANISOU 2411 C GLU A1128 5680 5425 5528 611 -1176 -1235 C ATOM 2412 O GLU A1128 1.522 -36.932 604.168 1.00 29.45 O ANISOU 2412 O GLU A1128 3762 3523 3904 437 -1101 -1224 O ATOM 2413 CB GLU A1128 1.325 -36.991 607.413 1.00 46.26 C ANISOU 2413 CB GLU A1128 6048 5861 5667 764 -1282 -1449 C ATOM 2414 CG GLU A1128 0.921 -35.526 607.462 1.00 45.64 C ANISOU 2414 CG GLU A1128 5862 5703 5774 611 -1229 -1555 C ATOM 2415 CD GLU A1128 1.270 -34.879 608.791 1.00 44.06 C ANISOU 2415 CD GLU A1128 5612 5626 5503 692 -1325 -1789 C ATOM 2416 OE1 GLU A1128 1.570 -33.665 608.815 1.00 41.99 O ANISOU 2416 OE1 GLU A1128 5196 5336 5425 578 -1323 -1967 O ATOM 2417 OE2 GLU A1128 1.248 -35.592 609.815 1.00 34.89 O ANISOU 2417 OE2 GLU A1128 4573 4588 4095 871 -1398 -1796 O ATOM 2418 N ALA A1129 2.573 -38.744 604.995 1.00 41.59 N ANISOU 2418 N ALA A1129 5396 5247 5159 740 -1255 -1260 N ATOM 2419 CA ALA A1129 3.459 -38.841 603.841 1.00 35.69 C ANISOU 2419 CA ALA A1129 4508 4516 4538 665 -1242 -1286 C ATOM 2420 C ALA A1129 2.690 -39.253 602.594 1.00 29.57 C ANISOU 2420 C ALA A1129 3810 3610 3815 543 -1113 -1085 C ATOM 2421 O ALA A1129 2.982 -38.776 601.491 1.00 39.76 O ANISOU 2421 O ALA A1129 4984 4871 5253 393 -1049 -1080 O ATOM 2422 CB ALA A1129 4.584 -39.835 604.125 1.00 35.60 C ANISOU 2422 CB ALA A1129 4471 4644 4413 859 -1360 -1368 C ATOM 2423 N ALA A1130 1.703 -40.139 602.749 1.00 34.47 N ANISOU 2423 N ALA A1130 4628 4160 4310 601 -1067 -923 N ATOM 2424 CA ALA A1130 0.956 -40.630 601.595 1.00 36.95 C ANISOU 2424 CA ALA A1130 5009 4371 4660 493 -957 -756 C ATOM 2425 C ALA A1130 0.245 -39.495 600.872 1.00 38.86 C ANISOU 2425 C ALA A1130 5180 4530 5054 300 -873 -705 C ATOM 2426 O ALA A1130 0.256 -39.429 599.636 1.00 39.69 O ANISOU 2426 O ALA A1130 5232 4606 5242 182 -810 -638 O ATOM 2427 CB ALA A1130 -0.051 -41.690 602.038 1.00 37.61 C ANISOU 2427 CB ALA A1130 5306 4385 4597 571 -913 -618 C ATOM 2428 N VAL A1131 -0.381 -38.590 601.627 1.00 34.65 N ANISOU 2428 N VAL A1131 4651 3962 4554 278 -870 -734 N ATOM 2429 CA VAL A1131 -1.063 -37.453 601.015 1.00 28.51 C ANISOU 2429 CA VAL A1131 3811 3089 3931 122 -797 -683 C ATOM 2430 C VAL A1131 -0.100 -36.685 600.123 1.00 42.96 C ANISOU 2430 C VAL A1131 5482 4927 5915 9 -786 -744 C ATOM 2431 O VAL A1131 -0.446 -36.281 599.005 1.00 55.90 O ANISOU 2431 O VAL A1131 7096 6498 7647 -117 -710 -634 O ATOM 2432 CB VAL A1131 -1.667 -36.549 602.106 1.00 38.40 C ANISOU 2432 CB VAL A1131 5074 4309 5208 139 -805 -753 C ATOM 2433 CG1 VAL A1131 -2.167 -35.245 601.507 1.00 47.90 C ANISOU 2433 CG1 VAL A1131 6197 5400 6602 -1 -741 -723 C ATOM 2434 CG2 VAL A1131 -2.790 -37.276 602.839 1.00 36.40 C ANISOU 2434 CG2 VAL A1131 4983 4040 4808 220 -776 -667 C ATOM 2435 N ASN A1132 1.126 -36.477 600.599 1.00 39.37 N ANISOU 2435 N ASN A1132 4914 4563 5482 52 -858 -922 N ATOM 2436 CA ASN A1132 2.093 -35.707 599.830 1.00 39.47 C ANISOU 2436 CA ASN A1132 4760 4584 5655 -74 -828 -1001 C ATOM 2437 C ASN A1132 2.460 -36.412 598.529 1.00 36.03 C ANISOU 2437 C ASN A1132 4311 4174 5205 -125 -774 -906 C ATOM 2438 O ASN A1132 2.552 -35.772 597.475 1.00 46.73 O ANISOU 2438 O ASN A1132 5603 5478 6676 -275 -686 -845 O ATOM 2439 CB ASN A1132 3.338 -35.452 600.675 1.00 52.48 C ANISOU 2439 CB ASN A1132 6268 6350 7322 -12 -924 -1243 C ATOM 2440 CG ASN A1132 4.219 -34.374 600.094 1.00 64.62 C ANISOU 2440 CG ASN A1132 7619 7870 9063 -176 -872 -1357 C ATOM 2441 OD1 ASN A1132 5.013 -34.630 599.191 1.00 83.12 O ANISOU 2441 OD1 ASN A1132 9871 10263 11447 -236 -832 -1363 O ATOM 2442 ND2 ASN A1132 4.079 -33.156 600.603 1.00 35.59 N ANISOU 2442 ND2 ASN A1132 3886 4114 5521 -256 -856 -1454 N ATOM 2443 N LEU A1133 2.673 -37.730 598.580 1.00 38.18 N ANISOU 2443 N LEU A1133 4651 4522 5334 1 -818 -891 N ATOM 2444 CA LEU A1133 3.082 -38.455 597.379 1.00 48.36 C ANISOU 2444 CA LEU A1133 5921 5846 6607 -37 -766 -833 C ATOM 2445 C LEU A1133 1.960 -38.509 596.351 1.00 35.15 C ANISOU 2445 C LEU A1133 4344 4084 4927 -145 -671 -636 C ATOM 2446 O LEU A1133 2.218 -38.451 595.143 1.00 52.42 O ANISOU 2446 O LEU A1133 6481 6286 7151 -252 -599 -585 O ATOM 2447 CB LEU A1133 3.537 -39.868 597.741 1.00 49.09 C ANISOU 2447 CB LEU A1133 6076 6017 6560 141 -835 -870 C ATOM 2448 CG LEU A1133 5.002 -40.015 598.156 1.00 36.47 C ANISOU 2448 CG LEU A1133 4328 4554 4974 243 -924 -1069 C ATOM 2449 CD1 LEU A1133 5.313 -39.164 599.366 1.00 31.53 C ANISOU 2449 CD1 LEU A1133 3629 3972 4380 287 -1013 -1216 C ATOM 2450 CD2 LEU A1133 5.331 -41.472 598.438 1.00 40.47 C ANISOU 2450 CD2 LEU A1133 4925 5110 5342 443 -989 -1072 C ATOM 2451 N ALA A1134 0.711 -38.634 596.805 1.00 37.50 N ANISOU 2451 N ALA A1134 4773 4306 5169 -116 -669 -534 N ATOM 2452 CA ALA A1134 -0.412 -38.654 595.876 1.00 39.52 C ANISOU 2452 CA ALA A1134 5098 4499 5420 -208 -596 -367 C ATOM 2453 C ALA A1134 -0.584 -37.324 595.154 1.00 38.50 C ANISOU 2453 C ALA A1134 4893 4312 5424 -349 -540 -306 C ATOM 2454 O ALA A1134 -1.269 -37.273 594.128 1.00 48.72 O ANISOU 2454 O ALA A1134 6217 5584 6711 -428 -486 -169 O ATOM 2455 CB ALA A1134 -1.701 -39.019 596.614 1.00 44.86 C ANISOU 2455 CB ALA A1134 5905 5115 6025 -150 -601 -296 C ATOM 2456 N LYS A1135 0.015 -36.251 595.669 1.00 39.56 N ANISOU 2456 N LYS A1135 4934 4420 5679 -380 -550 -406 N ATOM 2457 CA LYS A1135 -0.001 -34.954 595.008 1.00 47.19 C ANISOU 2457 CA LYS A1135 5837 5302 6793 -514 -481 -350 C ATOM 2458 C LYS A1135 1.122 -34.790 593.991 1.00 43.92 C ANISOU 2458 C LYS A1135 5320 4939 6428 -619 -418 -371 C ATOM 2459 O LYS A1135 1.103 -33.823 593.223 1.00 43.84 O ANISOU 2459 O LYS A1135 5283 4853 6521 -742 -336 -284 O ATOM 2460 CB LYS A1135 0.101 -33.836 596.052 1.00 45.22 C ANISOU 2460 CB LYS A1135 5534 4975 6672 -515 -504 -467 C ATOM 2461 CG LYS A1135 -1.150 -33.643 596.902 1.00 54.85 C ANISOU 2461 CG LYS A1135 6845 6122 7874 -444 -532 -429 C ATOM 2462 CD LYS A1135 -0.795 -33.155 598.304 1.00 62.19 C ANISOU 2462 CD LYS A1135 7732 7053 8843 -382 -591 -620 C ATOM 2463 CE LYS A1135 -2.022 -32.715 599.089 1.00 53.69 C ANISOU 2463 CE LYS A1135 6730 5895 7777 -333 -592 -595 C ATOM 2464 NZ LYS A1135 -2.394 -31.295 598.819 1.00 85.34 N ANISOU 2464 NZ LYS A1135 10696 9749 11981 -424 -533 -567 N ATOM 2465 N SER A1136 2.086 -35.706 593.962 1.00 49.41 N ANISOU 2465 N SER A1136 5963 5756 7053 -568 -445 -480 N ATOM 2466 CA SER A1136 3.261 -35.549 593.123 1.00 47.67 C ANISOU 2466 CA SER A1136 5619 5603 6888 -666 -377 -540 C ATOM 2467 C SER A1136 2.967 -35.970 591.686 1.00 52.76 C ANISOU 2467 C SER A1136 6315 6278 7452 -740 -293 -383 C ATOM 2468 O SER A1136 2.034 -36.727 591.406 1.00 53.97 O ANISOU 2468 O SER A1136 6584 6436 7486 -688 -313 -273 O ATOM 2469 CB SER A1136 4.426 -36.376 593.668 1.00 52.98 C ANISOU 2469 CB SER A1136 6198 6410 7523 -561 -446 -736 C ATOM 2470 OG SER A1136 4.215 -37.760 593.441 1.00 36.48 O ANISOU 2470 OG SER A1136 4196 4384 5280 -451 -478 -696 O ATOM 2471 N ARG A1137 3.791 -35.460 590.768 1.00 59.53 N ANISOU 2471 N ARG A1137 7079 7166 8373 -871 -191 -386 N ATOM 2472 CA ARG A1137 3.703 -35.892 589.378 1.00 49.41 C ANISOU 2472 CA ARG A1137 5833 5950 6989 -940 -107 -264 C ATOM 2473 C ARG A1137 3.933 -37.393 589.265 1.00 50.08 C ANISOU 2473 C ARG A1137 5935 6157 6937 -832 -153 -339 C ATOM 2474 O ARG A1137 3.295 -38.070 588.450 1.00 52.40 O ANISOU 2474 O ARG A1137 6317 6488 7106 -832 -134 -235 O ATOM 2475 CB ARG A1137 4.726 -35.134 588.532 1.00 50.55 C ANISOU 2475 CB ARG A1137 5866 6120 7221 -1099 28 -280 C ATOM 2476 CG ARG A1137 4.245 -34.775 587.136 1.00 65.10 C ANISOU 2476 CG ARG A1137 7786 7956 8992 -1213 139 -67 C ATOM 2477 CD ARG A1137 5.319 -35.031 586.086 1.00 97.70 C ANISOU 2477 CD ARG A1137 11827 12217 13080 -1314 264 -114 C ATOM 2478 NE ARG A1137 6.616 -34.461 586.442 1.00109.39 N ANISOU 2478 NE ARG A1137 13137 13705 14722 -1398 331 -288 N ATOM 2479 CZ ARG A1137 7.718 -34.599 585.710 1.00110.71 C ANISOU 2479 CZ ARG A1137 13184 13991 14890 -1495 452 -377 C ATOM 2480 NH1 ARG A1137 7.687 -35.287 584.574 1.00 99.25 N ANISOU 2480 NH1 ARG A1137 11777 12659 13275 -1514 520 -303 N ATOM 2481 NH2 ARG A1137 8.855 -34.047 586.113 1.00104.67 N ANISOU 2481 NH2 ARG A1137 12243 13234 14292 -1577 509 -557 N ATOM 2482 N TRP A1138 4.842 -37.928 590.083 1.00 59.52 N ANISOU 2482 N TRP A1138 7044 7415 8154 -731 -218 -528 N ATOM 2483 CA TRP A1138 5.141 -39.355 590.049 1.00 47.53 C ANISOU 2483 CA TRP A1138 5547 5988 6525 -605 -261 -605 C ATOM 2484 C TRP A1138 3.878 -40.188 590.210 1.00 44.25 C ANISOU 2484 C TRP A1138 5306 5514 5993 -522 -312 -492 C ATOM 2485 O TRP A1138 3.726 -41.232 589.566 1.00 42.82 O ANISOU 2485 O TRP A1138 5181 5377 5711 -493 -292 -478 O ATOM 2486 CB TRP A1138 6.154 -39.690 591.146 1.00 61.42 C ANISOU 2486 CB TRP A1138 7204 7806 8328 -469 -355 -808 C ATOM 2487 CG TRP A1138 6.341 -41.153 591.390 1.00 42.12 C ANISOU 2487 CG TRP A1138 4815 5413 5777 -293 -422 -871 C ATOM 2488 CD1 TRP A1138 6.790 -42.080 590.500 1.00 35.82 C ANISOU 2488 CD1 TRP A1138 3999 4692 4921 -277 -371 -906 C ATOM 2489 CD2 TRP A1138 6.100 -41.855 592.615 1.00 37.67 C ANISOU 2489 CD2 TRP A1138 4343 4816 5154 -103 -543 -905 C ATOM 2490 NE1 TRP A1138 6.838 -43.319 591.091 1.00 31.94 N ANISOU 2490 NE1 TRP A1138 3585 4195 4355 -84 -454 -960 N ATOM 2491 CE2 TRP A1138 6.419 -43.207 592.390 1.00 28.57 C ANISOU 2491 CE2 TRP A1138 3235 3701 3920 26 -558 -947 C ATOM 2492 CE3 TRP A1138 5.644 -41.471 593.880 1.00 38.59 C ANISOU 2492 CE3 TRP A1138 4517 4873 5271 -26 -632 -903 C ATOM 2493 CZ2 TRP A1138 6.298 -44.177 593.381 1.00 34.28 C ANISOU 2493 CZ2 TRP A1138 4072 4388 4566 230 -656 -965 C ATOM 2494 CZ3 TRP A1138 5.522 -42.436 594.862 1.00 29.09 C ANISOU 2494 CZ3 TRP A1138 3424 3659 3971 171 -728 -923 C ATOM 2495 CH2 TRP A1138 5.848 -43.772 594.607 1.00 36.18 C ANISOU 2495 CH2 TRP A1138 4377 4578 4791 299 -738 -943 C ATOM 2496 N TYR A1139 2.955 -39.739 591.063 1.00 50.02 N ANISOU 2496 N TYR A1139 6117 6144 6743 -491 -366 -425 N ATOM 2497 CA TYR A1139 1.707 -40.467 591.253 1.00 48.72 C ANISOU 2497 CA TYR A1139 6104 5924 6485 -432 -397 -326 C ATOM 2498 C TYR A1139 0.682 -40.144 590.173 1.00 48.98 C ANISOU 2498 C TYR A1139 6189 5939 6483 -547 -338 -164 C ATOM 2499 O TYR A1139 -0.159 -40.990 589.854 1.00 52.00 O ANISOU 2499 O TYR A1139 6664 6322 6773 -530 -340 -109 O ATOM 2500 CB TYR A1139 1.120 -40.156 592.630 1.00 40.33 C ANISOU 2500 CB TYR A1139 5099 4779 5447 -349 -470 -333 C ATOM 2501 CG TYR A1139 -0.221 -40.807 592.871 1.00 34.24 C ANISOU 2501 CG TYR A1139 4471 3946 4594 -311 -479 -234 C ATOM 2502 CD1 TYR A1139 -0.304 -42.103 593.359 1.00 35.16 C ANISOU 2502 CD1 TYR A1139 4685 4056 4618 -196 -505 -267 C ATOM 2503 CD2 TYR A1139 -1.404 -40.128 592.609 1.00 36.84 C ANISOU 2503 CD2 TYR A1139 4834 4216 4947 -388 -454 -110 C ATOM 2504 CE1 TYR A1139 -1.527 -42.706 593.579 1.00 45.90 C ANISOU 2504 CE1 TYR A1139 6170 5351 5917 -185 -491 -186 C ATOM 2505 CE2 TYR A1139 -2.631 -40.720 592.827 1.00 44.20 C ANISOU 2505 CE2 TYR A1139 5872 5107 5818 -365 -455 -42 C ATOM 2506 CZ TYR A1139 -2.687 -42.010 593.311 1.00 51.43 C ANISOU 2506 CZ TYR A1139 6879 6015 6647 -276 -465 -84 C ATOM 2507 OH TYR A1139 -3.906 -42.609 593.532 1.00 69.97 O ANISOU 2507 OH TYR A1139 9326 8312 8947 -276 -444 -25 O ATOM 2508 N ASN A1140 0.731 -38.941 589.605 1.00 45.24 N ANISOU 2508 N ASN A1140 5660 5447 6082 -662 -285 -89 N ATOM 2509 CA ASN A1140 -0.271 -38.502 588.643 1.00 43.88 C ANISOU 2509 CA ASN A1140 5541 5261 5869 -745 -248 82 C ATOM 2510 C ASN A1140 0.041 -38.928 587.214 1.00 40.88 C ANISOU 2510 C ASN A1140 5150 4997 5386 -821 -177 120 C ATOM 2511 O ASN A1140 -0.779 -38.691 586.321 1.00 44.42 O ANISOU 2511 O ASN A1140 5645 5467 5764 -876 -159 259 O ATOM 2512 CB ASN A1140 -0.423 -36.980 588.710 1.00 59.13 C ANISOU 2512 CB ASN A1140 7445 7097 7926 -815 -220 170 C ATOM 2513 CG ASN A1140 -0.918 -36.506 590.065 1.00 70.15 C ANISOU 2513 CG ASN A1140 8857 8384 9414 -743 -285 130 C ATOM 2514 OD1 ASN A1140 -1.728 -37.173 590.711 1.00 70.03 O ANISOU 2514 OD1 ASN A1140 8911 8357 9342 -657 -343 122 O ATOM 2515 ND2 ASN A1140 -0.430 -35.351 590.504 1.00 71.70 N ANISOU 2515 ND2 ASN A1140 8990 8497 9754 -786 -264 94 N ATOM 2516 N GLN A1141 1.196 -39.546 586.974 1.00 44.75 N ANISOU 2516 N GLN A1141 5573 5573 5858 -817 -142 -7 N ATOM 2517 CA GLN A1141 1.545 -40.102 585.671 1.00 45.54 C ANISOU 2517 CA GLN A1141 5660 5798 5845 -879 -69 -5 C ATOM 2518 C GLN A1141 1.558 -41.621 585.657 1.00 41.31 C ANISOU 2518 C GLN A1141 5163 5315 5218 -792 -97 -116 C ATOM 2519 O GLN A1141 1.143 -42.230 584.668 1.00 44.87 O ANISOU 2519 O GLN A1141 5655 5843 5549 -830 -66 -89 O ATOM 2520 CB GLN A1141 2.919 -39.587 585.226 1.00 49.23 C ANISOU 2520 CB GLN A1141 6004 6331 6371 -959 26 -77 C ATOM 2521 CG GLN A1141 2.918 -38.147 584.745 1.00 63.99 C ANISOU 2521 CG GLN A1141 7856 8153 8305 -1088 106 62 C ATOM 2522 CD GLN A1141 4.293 -37.685 584.301 1.00 91.28 C ANISOU 2522 CD GLN A1141 11185 11672 11828 -1192 226 -21 C ATOM 2523 OE1 GLN A1141 5.296 -38.358 584.546 1.00 89.03 O ANISOU 2523 OE1 GLN A1141 10796 11467 11564 -1149 229 -207 O ATOM 2524 NE2 GLN A1141 4.347 -36.530 583.645 1.00 98.62 N ANISOU 2524 NE2 GLN A1141 12118 12560 12795 -1326 332 118 N ATOM 2525 N THR A1142 2.027 -42.247 586.733 1.00 54.27 N ANISOU 2525 N THR A1142 6797 6914 6911 -670 -156 -242 N ATOM 2526 CA THR A1142 2.084 -43.702 586.858 1.00 44.04 C ANISOU 2526 CA THR A1142 5556 5626 5550 -566 -179 -341 C ATOM 2527 C THR A1142 1.457 -44.078 588.194 1.00 41.75 C ANISOU 2527 C THR A1142 5360 5216 5285 -449 -264 -337 C ATOM 2528 O THR A1142 2.146 -44.514 589.125 1.00 54.65 O ANISOU 2528 O THR A1142 6986 6826 6952 -320 -314 -437 O ATOM 2529 CB THR A1142 3.524 -44.206 586.756 1.00 45.76 C ANISOU 2529 CB THR A1142 5669 5925 5793 -508 -154 -505 C ATOM 2530 OG1 THR A1142 4.259 -43.805 587.919 1.00 52.97 O ANISOU 2530 OG1 THR A1142 6511 6808 6806 -419 -218 -586 O ATOM 2531 CG2 THR A1142 4.202 -43.634 585.519 1.00 65.71 C ANISOU 2531 CG2 THR A1142 8088 8575 8303 -645 -46 -507 C ATOM 2532 N PRO A1143 0.138 -43.912 588.323 1.00 29.58 N ANISOU 2532 N PRO A1143 3909 3610 3721 -483 -281 -223 N ATOM 2533 CA PRO A1143 -0.490 -44.100 589.640 1.00 43.12 C ANISOU 2533 CA PRO A1143 5710 5215 5458 -389 -341 -210 C ATOM 2534 C PRO A1143 -0.404 -45.521 590.166 1.00 42.12 C ANISOU 2534 C PRO A1143 5681 5038 5285 -270 -353 -283 C ATOM 2535 O PRO A1143 -0.151 -45.716 591.361 1.00 49.83 O ANISOU 2535 O PRO A1143 6701 5955 6276 -146 -404 -317 O ATOM 2536 CB PRO A1143 -1.943 -43.671 589.391 1.00 37.09 C ANISOU 2536 CB PRO A1143 4997 4418 4678 -472 -335 -83 C ATOM 2537 CG PRO A1143 -2.157 -43.905 587.941 1.00 39.45 C ANISOU 2537 CG PRO A1143 5276 4810 4904 -571 -287 -54 C ATOM 2538 CD PRO A1143 -0.848 -43.581 587.282 1.00 45.86 C ANISOU 2538 CD PRO A1143 5991 5710 5724 -601 -248 -107 C ATOM 2539 N ASN A1144 -0.611 -46.525 589.312 1.00 27.47 N ANISOU 2539 N ASN A1144 3869 3199 3370 -298 -306 -309 N ATOM 2540 CA ASN A1144 -0.659 -47.900 589.798 1.00 41.04 C ANISOU 2540 CA ASN A1144 5705 4827 5061 -191 -301 -365 C ATOM 2541 C ASN A1144 0.628 -48.275 590.521 1.00 38.72 C ANISOU 2541 C ASN A1144 5392 4529 4791 -25 -346 -461 C ATOM 2542 O ASN A1144 0.594 -48.792 591.644 1.00 34.07 O ANISOU 2542 O ASN A1144 4906 3845 4193 109 -385 -457 O ATOM 2543 CB ASN A1144 -0.923 -48.858 588.637 1.00 53.16 C ANISOU 2543 CB ASN A1144 7267 6386 6545 -260 -236 -413 C ATOM 2544 CG ASN A1144 -2.352 -48.785 588.137 1.00 67.16 C ANISOU 2544 CG ASN A1144 9078 8154 8284 -392 -211 -338 C ATOM 2545 OD1 ASN A1144 -3.289 -48.627 588.922 1.00 50.43 O ANISOU 2545 OD1 ASN A1144 7023 5954 6185 -394 -225 -267 O ATOM 2546 ND2 ASN A1144 -2.528 -48.899 586.825 1.00 79.67 N ANISOU 2546 ND2 ASN A1144 10614 9846 9811 -500 -174 -365 N ATOM 2547 N ARG A1145 1.780 -48.018 589.896 1.00 48.77 N ANISOU 2547 N ARG A1145 6529 5914 6087 -28 -340 -550 N ATOM 2548 CA ARG A1145 3.043 -48.380 590.528 1.00 37.29 C ANISOU 2548 CA ARG A1145 5024 4482 4662 141 -393 -664 C ATOM 2549 C ARG A1145 3.341 -47.494 591.730 1.00 35.49 C ANISOU 2549 C ARG A1145 4753 4260 4472 210 -480 -660 C ATOM 2550 O ARG A1145 3.973 -47.948 592.690 1.00 41.71 O ANISOU 2550 O ARG A1145 5561 5033 5252 391 -556 -722 O ATOM 2551 CB ARG A1145 4.184 -48.310 589.512 1.00 31.46 C ANISOU 2551 CB ARG A1145 4125 3879 3948 105 -350 -781 C ATOM 2552 CG ARG A1145 4.468 -46.927 588.959 1.00 33.81 C ANISOU 2552 CG ARG A1145 4274 4285 4288 -52 -317 -759 C ATOM 2553 CD ARG A1145 5.738 -46.925 588.112 1.00 38.61 C ANISOU 2553 CD ARG A1145 4717 5031 4922 -75 -259 -892 C ATOM 2554 NE ARG A1145 6.135 -45.576 587.717 1.00 47.32 N ANISOU 2554 NE ARG A1145 5682 6217 6080 -225 -212 -872 N ATOM 2555 CZ ARG A1145 7.245 -45.284 587.047 1.00 41.29 C ANISOU 2555 CZ ARG A1145 4753 5579 5355 -283 -141 -979 C ATOM 2556 NH1 ARG A1145 7.517 -44.023 586.736 1.00 46.20 N ANISOU 2556 NH1 ARG A1145 5272 6245 6037 -435 -81 -941 N ATOM 2557 NH2 ARG A1145 8.086 -46.247 586.689 1.00 36.52 N ANISOU 2557 NH2 ARG A1145 4087 5049 4740 -190 -119 -1126 N ATOM 2558 N ALA A1146 2.901 -46.235 591.700 1.00 28.60 N ANISOU 2558 N ALA A1146 3821 3408 3637 79 -474 -592 N ATOM 2559 CA ALA A1146 3.099 -45.361 592.850 1.00 26.93 C ANISOU 2559 CA ALA A1146 3571 3194 3467 132 -550 -607 C ATOM 2560 C ALA A1146 2.149 -45.713 593.989 1.00 35.56 C ANISOU 2560 C ALA A1146 4830 4179 4503 220 -590 -530 C ATOM 2561 O ALA A1146 2.548 -45.702 595.158 1.00 37.48 O ANISOU 2561 O ALA A1146 5090 4424 4726 361 -671 -578 O ATOM 2562 CB ALA A1146 2.926 -43.900 592.437 1.00 29.14 C ANISOU 2562 CB ALA A1146 3746 3504 3824 -36 -516 -563 C ATOM 2563 N LYS A1147 0.889 -46.023 593.671 1.00 38.76 N ANISOU 2563 N LYS A1147 5351 4502 4872 138 -530 -418 N ATOM 2564 CA LYS A1147 -0.038 -46.473 594.704 1.00 31.67 C ANISOU 2564 CA LYS A1147 4614 3499 3920 208 -538 -348 C ATOM 2565 C LYS A1147 0.512 -47.695 595.427 1.00 32.96 C ANISOU 2565 C LYS A1147 4891 3614 4018 399 -571 -387 C ATOM 2566 O LYS A1147 0.354 -47.830 596.645 1.00 35.87 O ANISOU 2566 O LYS A1147 5362 3937 4330 519 -613 -361 O ATOM 2567 CB LYS A1147 -1.402 -46.785 594.088 1.00 38.19 C ANISOU 2567 CB LYS A1147 5521 4258 4730 79 -457 -252 C ATOM 2568 CG LYS A1147 -2.504 -47.030 595.110 1.00 49.00 C ANISOU 2568 CG LYS A1147 7031 5527 6060 106 -438 -178 C ATOM 2569 CD LYS A1147 -3.805 -47.454 594.443 1.00 69.83 C ANISOU 2569 CD LYS A1147 9723 8114 8696 -27 -355 -115 C ATOM 2570 CE LYS A1147 -4.965 -47.469 595.433 1.00 84.84 C ANISOU 2570 CE LYS A1147 11727 9932 10577 -30 -318 -48 C ATOM 2571 NZ LYS A1147 -4.743 -48.412 596.568 1.00 86.44 N ANISOU 2571 NZ LYS A1147 12095 10040 10710 113 -306 -41 N ATOM 2572 N ARG A1148 1.166 -48.593 594.689 1.00 33.22 N ANISOU 2572 N ARG A1148 4916 3656 4052 441 -550 -447 N ATOM 2573 CA ARG A1148 1.791 -49.757 595.307 1.00 35.56 C ANISOU 2573 CA ARG A1148 5319 3894 4300 648 -585 -483 C ATOM 2574 C ARG A1148 2.830 -49.337 596.336 1.00 32.68 C ANISOU 2574 C ARG A1148 4883 3615 3918 822 -708 -557 C ATOM 2575 O ARG A1148 2.880 -49.879 597.445 1.00 35.04 O ANISOU 2575 O ARG A1148 5316 3860 4138 1001 -762 -526 O ATOM 2576 CB ARG A1148 2.441 -50.624 594.231 1.00 50.58 C ANISOU 2576 CB ARG A1148 7182 5807 6230 660 -542 -567 C ATOM 2577 CG ARG A1148 1.754 -51.944 593.969 1.00 41.52 C ANISOU 2577 CG ARG A1148 6216 4502 5057 668 -457 -524 C ATOM 2578 CD ARG A1148 2.326 -52.571 592.711 1.00 46.24 C ANISOU 2578 CD ARG A1148 6741 5136 5692 636 -404 -631 C ATOM 2579 NE ARG A1148 1.513 -52.264 591.537 1.00 45.10 N ANISOU 2579 NE ARG A1148 6547 5032 5555 406 -322 -617 N ATOM 2580 CZ ARG A1148 1.982 -52.153 590.297 1.00 46.59 C ANISOU 2580 CZ ARG A1148 6606 5338 5757 313 -282 -704 C ATOM 2581 NH1 ARG A1148 3.276 -52.304 590.049 1.00 61.52 N ANISOU 2581 NH1 ARG A1148 8386 7315 7675 418 -305 -823 N ATOM 2582 NH2 ARG A1148 1.151 -51.876 589.301 1.00 45.56 N ANISOU 2582 NH2 ARG A1148 6451 5255 5605 120 -221 -675 N ATOM 2583 N VAL A1149 3.679 -48.373 595.978 1.00 32.83 N ANISOU 2583 N VAL A1149 4691 3776 4006 768 -749 -660 N ATOM 2584 CA VAL A1149 4.741 -47.946 596.880 1.00 33.54 C ANISOU 2584 CA VAL A1149 4674 3976 4095 919 -873 -770 C ATOM 2585 C VAL A1149 4.171 -47.132 598.033 1.00 36.85 C ANISOU 2585 C VAL A1149 5140 4389 4474 923 -924 -727 C ATOM 2586 O VAL A1149 4.596 -47.283 599.184 1.00 36.89 O ANISOU 2586 O VAL A1149 5185 4431 4400 1110 -1030 -766 O ATOM 2587 CB VAL A1149 5.809 -47.158 596.103 1.00 35.02 C ANISOU 2587 CB VAL A1149 4608 4310 4389 830 -877 -911 C ATOM 2588 CG1 VAL A1149 6.859 -46.619 597.056 1.00 40.83 C ANISOU 2588 CG1 VAL A1149 5203 5173 5138 962 -1007 -1054 C ATOM 2589 CG2 VAL A1149 6.447 -48.040 595.040 1.00 46.63 C ANISOU 2589 CG2 VAL A1149 6029 5804 5883 850 -823 -975 C ATOM 2590 N ILE A1150 3.207 -46.256 597.748 1.00 48.69 N ANISOU 2590 N ILE A1150 6634 5848 6017 730 -856 -651 N ATOM 2591 CA ILE A1150 2.639 -45.411 598.796 1.00 39.81 C ANISOU 2591 CA ILE A1150 5540 4717 4868 725 -892 -629 C ATOM 2592 C ILE A1150 1.981 -46.268 599.869 1.00 39.00 C ANISOU 2592 C ILE A1150 5659 4530 4628 869 -902 -538 C ATOM 2593 O ILE A1150 2.308 -46.169 601.058 1.00 39.76 O ANISOU 2593 O ILE A1150 5791 4677 4639 1021 -993 -580 O ATOM 2594 CB ILE A1150 1.638 -44.409 598.192 1.00 42.64 C ANISOU 2594 CB ILE A1150 5862 5030 5311 506 -807 -553 C ATOM 2595 CG1 ILE A1150 2.372 -43.399 597.303 1.00 37.66 C ANISOU 2595 CG1 ILE A1150 5025 4475 4807 372 -795 -632 C ATOM 2596 CG2 ILE A1150 0.855 -43.712 599.306 1.00 38.28 C ANISOU 2596 CG2 ILE A1150 5371 4445 4729 513 -826 -525 C ATOM 2597 CD1 ILE A1150 1.457 -42.551 596.445 1.00 44.89 C ANISOU 2597 CD1 ILE A1150 5919 5338 5799 174 -707 -531 C ATOM 2598 N THR A1151 1.056 -47.140 599.462 1.00 35.96 N ANISOU 2598 N THR A1151 5429 4019 4213 821 -801 -417 N ATOM 2599 CA THR A1151 0.350 -47.966 600.436 1.00 35.23 C ANISOU 2599 CA THR A1151 5563 3823 3999 929 -774 -315 C ATOM 2600 C THR A1151 1.308 -48.846 601.228 1.00 45.32 C ANISOU 2600 C THR A1151 6930 5117 5171 1187 -866 -343 C ATOM 2601 O THR A1151 1.058 -49.127 602.406 1.00 51.70 O ANISOU 2601 O THR A1151 7895 5899 5850 1322 -890 -283 O ATOM 2602 CB THR A1151 -0.701 -48.829 599.737 1.00 27.15 C ANISOU 2602 CB THR A1151 4668 2657 2989 815 -638 -209 C ATOM 2603 OG1 THR A1151 -0.132 -49.428 598.566 1.00 66.87 O ANISOU 2603 OG1 THR A1151 9638 7687 8083 789 -618 -257 O ATOM 2604 CG2 THR A1151 -1.912 -47.989 599.345 1.00 40.80 C ANISOU 2604 CG2 THR A1151 6348 4373 4781 604 -562 -159 C ATOM 2605 N THR A1152 2.406 -49.287 600.610 1.00 47.20 N ANISOU 2605 N THR A1152 7072 5408 5456 1270 -916 -433 N ATOM 2606 CA THR A1152 3.372 -50.104 601.337 1.00 36.78 C ANISOU 2606 CA THR A1152 5819 4113 4043 1545 -1022 -466 C ATOM 2607 C THR A1152 3.978 -49.325 602.498 1.00 45.14 C ANISOU 2607 C THR A1152 6801 5327 5023 1678 -1169 -551 C ATOM 2608 O THR A1152 4.227 -49.888 603.571 1.00 53.54 O ANISOU 2608 O THR A1152 8006 6397 5938 1909 -1250 -514 O ATOM 2609 CB THR A1152 4.466 -50.600 600.392 1.00 41.47 C ANISOU 2609 CB THR A1152 6279 4756 4723 1602 -1049 -576 C ATOM 2610 OG1 THR A1152 3.872 -51.308 599.297 1.00 46.57 O ANISOU 2610 OG1 THR A1152 6994 5267 5432 1469 -911 -517 O ATOM 2611 CG2 THR A1152 5.425 -51.527 601.128 1.00 36.29 C ANISOU 2611 CG2 THR A1152 5697 4115 3976 1917 -1165 -604 C ATOM 2612 N PHE A1153 4.232 -48.028 602.301 1.00 36.28 N ANISOU 2612 N PHE A1153 5459 4330 3995 1539 -1204 -668 N ATOM 2613 CA PHE A1153 4.680 -47.190 603.409 1.00 38.14 C ANISOU 2613 CA PHE A1153 5614 4710 4168 1631 -1333 -774 C ATOM 2614 C PHE A1153 3.594 -47.059 604.470 1.00 43.16 C ANISOU 2614 C PHE A1153 6443 5284 4670 1640 -1300 -661 C ATOM 2615 O PHE A1153 3.886 -47.080 605.671 1.00 54.85 O ANISOU 2615 O PHE A1153 7989 6853 6000 1827 -1407 -690 O ATOM 2616 CB PHE A1153 5.093 -45.809 602.897 1.00 36.02 C ANISOU 2616 CB PHE A1153 5080 4548 4059 1444 -1344 -924 C ATOM 2617 CG PHE A1153 6.322 -45.820 602.030 1.00 38.56 C ANISOU 2617 CG PHE A1153 5184 4970 4498 1443 -1380 -1068 C ATOM 2618 CD1 PHE A1153 7.408 -46.619 602.347 1.00 42.71 C ANISOU 2618 CD1 PHE A1153 5675 5590 4963 1684 -1499 -1156 C ATOM 2619 CD2 PHE A1153 6.390 -45.030 600.894 1.00 37.67 C ANISOU 2619 CD2 PHE A1153 4901 4860 4552 1208 -1290 -1111 C ATOM 2620 CE1 PHE A1153 8.536 -46.629 601.551 1.00 49.21 C ANISOU 2620 CE1 PHE A1153 6278 6517 5902 1681 -1521 -1306 C ATOM 2621 CE2 PHE A1153 7.517 -45.037 600.092 1.00 46.90 C ANISOU 2621 CE2 PHE A1153 5868 6129 5823 1192 -1300 -1245 C ATOM 2622 CZ PHE A1153 8.591 -45.838 600.422 1.00 51.58 C ANISOU 2622 CZ PHE A1153 6408 6824 6366 1425 -1412 -1353 C ATOM 2623 N ARG A1154 2.337 -46.920 604.047 1.00 44.33 N ANISOU 2623 N ARG A1154 6678 5300 4866 1446 -1152 -539 N ATOM 2624 CA ARG A1154 1.244 -46.767 605.001 1.00 36.48 C ANISOU 2624 CA ARG A1154 5849 4252 3761 1434 -1097 -443 C ATOM 2625 C ARG A1154 1.112 -48.005 605.880 1.00 50.54 C ANISOU 2625 C ARG A1154 7891 5963 5348 1643 -1093 -318 C ATOM 2626 O ARG A1154 1.301 -47.941 607.100 1.00 54.83 O ANISOU 2626 O ARG A1154 8518 6590 5724 1809 -1176 -329 O ATOM 2627 CB ARG A1154 -0.066 -46.489 604.261 1.00 52.45 C ANISOU 2627 CB ARG A1154 7891 6149 5887 1193 -938 -346 C ATOM 2628 CG ARG A1154 -0.159 -45.091 603.661 1.00 50.16 C ANISOU 2628 CG ARG A1154 7386 5912 5759 1003 -936 -434 C ATOM 2629 CD ARG A1154 -1.435 -44.385 604.095 1.00 56.68 C ANISOU 2629 CD ARG A1154 8257 6688 6590 887 -854 -381 C ATOM 2630 NE ARG A1154 -2.625 -44.949 603.464 1.00 61.89 N ANISOU 2630 NE ARG A1154 9017 7220 7277 762 -715 -244 N ATOM 2631 CZ ARG A1154 -3.871 -44.732 603.878 1.00 69.17 C ANISOU 2631 CZ ARG A1154 10015 8085 8182 685 -621 -177 C ATOM 2632 NH1 ARG A1154 -4.105 -43.968 604.939 1.00 58.03 N ANISOU 2632 NH1 ARG A1154 8604 6726 6717 724 -645 -228 N ATOM 2633 NH2 ARG A1154 -4.888 -45.288 603.233 1.00 74.95 N ANISOU 2633 NH2 ARG A1154 10809 8717 8952 566 -502 -78 N ATOM 2634 N THR A1155 0.795 -49.150 605.270 1.00 42.08 N ANISOU 2634 N THR A1155 6961 4736 4293 1637 -993 -200 N ATOM 2635 CA THR A1155 0.520 -50.350 606.053 1.00 62.52 C ANISOU 2635 CA THR A1155 9831 7207 6716 1809 -950 -51 C ATOM 2636 C THR A1155 1.789 -50.962 606.629 1.00 44.75 C ANISOU 2636 C THR A1155 7617 5037 4350 2112 -1109 -88 C ATOM 2637 O THR A1155 1.754 -51.541 607.720 1.00 61.97 O ANISOU 2637 O THR A1155 10013 7197 6335 2312 -1134 14 O ATOM 2638 CB THR A1155 -0.204 -51.388 605.196 1.00 62.11 C ANISOU 2638 CB THR A1155 9913 6944 6742 1696 -784 66 C ATOM 2639 OG1 THR A1155 0.683 -51.876 604.182 1.00 71.81 O ANISOU 2639 OG1 THR A1155 11037 8167 8081 1733 -826 -8 O ATOM 2640 CG2 THR A1155 -1.440 -50.777 604.545 1.00 65.28 C ANISOU 2640 CG2 THR A1155 10247 7295 7262 1406 -647 84 C ATOM 2641 N GLY A1156 2.908 -50.855 605.920 1.00 56.26 N ANISOU 2641 N GLY A1156 8868 6591 5916 2160 -1215 -229 N ATOM 2642 CA GLY A1156 4.119 -51.523 606.345 1.00 63.13 C ANISOU 2642 CA GLY A1156 9750 7538 6698 2460 -1368 -275 C ATOM 2643 C GLY A1156 4.141 -53.009 606.079 1.00 68.81 C ANISOU 2643 C GLY A1156 10685 8061 7398 2599 -1300 -142 C ATOM 2644 O GLY A1156 5.033 -53.700 606.586 1.00 51.73 O ANISOU 2644 O GLY A1156 8586 5931 5136 2893 -1424 -142 O ATOM 2645 N THR A1157 3.183 -53.525 605.312 1.00 58.73 N ANISOU 2645 N THR A1157 9520 6579 6215 2404 -1111 -38 N ATOM 2646 CA THR A1157 3.140 -54.919 604.906 1.00 63.84 C ANISOU 2646 CA THR A1157 10362 7009 6886 2491 -1019 64 C ATOM 2647 C THR A1157 3.517 -55.024 603.431 1.00 63.71 C ANISOU 2647 C THR A1157 10155 6983 7070 2356 -981 -59 C ATOM 2648 O THR A1157 3.895 -54.035 602.792 1.00 73.35 O ANISOU 2648 O THR A1157 11106 8372 8393 2218 -1032 -205 O ATOM 2649 CB THR A1157 1.753 -55.510 605.170 1.00 70.58 C ANISOU 2649 CB THR A1157 11488 7635 7696 2363 -819 253 C ATOM 2650 OG1 THR A1157 0.781 -54.832 604.365 1.00 69.66 O ANISOU 2650 OG1 THR A1157 11249 7510 7709 2034 -698 219 O ATOM 2651 CG2 THR A1157 1.383 -55.369 606.635 1.00 78.04 C ANISOU 2651 CG2 THR A1157 12622 8608 8423 2490 -840 373 C ATOM 2652 N TRP A1158 3.409 -56.237 602.884 1.00 73.56 N ANISOU 2652 N TRP A1158 11553 8024 8372 2390 -878 0 N ATOM 2653 CA TRP A1158 3.736 -56.493 601.486 1.00 60.90 C ANISOU 2653 CA TRP A1158 9799 6403 6939 2275 -827 -119 C ATOM 2654 C TRP A1158 2.529 -56.989 600.700 1.00 63.07 C ANISOU 2654 C TRP A1158 10186 6481 7297 2022 -625 -52 C ATOM 2655 O TRP A1158 2.692 -57.615 599.647 1.00 76.91 O ANISOU 2655 O TRP A1158 11904 8157 9163 1966 -558 -124 O ATOM 2656 CB TRP A1158 4.883 -57.500 601.382 1.00 50.93 C ANISOU 2656 CB TRP A1158 8561 5097 5692 2557 -903 -173 C ATOM 2657 CG TRP A1158 5.651 -57.371 600.110 1.00 68.40 C ANISOU 2657 CG TRP A1158 10519 7415 8055 2484 -914 -360 C ATOM 2658 CD1 TRP A1158 5.667 -58.248 599.064 1.00 76.70 C ANISOU 2658 CD1 TRP A1158 11593 8329 9219 2436 -806 -409 C ATOM 2659 CD2 TRP A1158 6.510 -56.289 599.740 1.00 73.71 C ANISOU 2659 CD2 TRP A1158 10873 8354 8780 2438 -1024 -533 C ATOM 2660 NE1 TRP A1158 6.489 -57.779 598.067 1.00 81.68 N ANISOU 2660 NE1 TRP A1158 11942 9140 9951 2370 -842 -597 N ATOM 2661 CE2 TRP A1158 7.019 -56.577 598.458 1.00 90.39 C ANISOU 2661 CE2 TRP A1158 12834 10486 11025 2364 -969 -669 C ATOM 2662 CE3 TRP A1158 6.901 -55.103 600.370 1.00 60.97 C ANISOU 2662 CE3 TRP A1158 9089 6959 7119 2441 -1153 -597 C ATOM 2663 CZ2 TRP A1158 7.898 -55.723 597.794 1.00 88.58 C ANISOU 2663 CZ2 TRP A1158 12295 10486 10876 2291 -1026 -848 C ATOM 2664 CZ3 TRP A1158 7.773 -54.257 599.711 1.00 56.66 C ANISOU 2664 CZ3 TRP A1158 8232 6624 6672 2362 -1212 -783 C ATOM 2665 CH2 TRP A1158 8.263 -54.571 598.437 1.00 67.87 C ANISOU 2665 CH2 TRP A1158 9512 8057 8219 2286 -1143 -898 C ATOM 2666 N ASP A1159 1.316 -56.719 601.188 1.00 64.09 N ANISOU 2666 N ASP A1159 10437 6540 7375 1868 -527 67 N ATOM 2667 CA ASP A1159 0.120 -57.176 600.487 1.00 74.55 C ANISOU 2667 CA ASP A1159 11848 7695 8782 1622 -340 112 C ATOM 2668 C ASP A1159 -0.063 -56.454 599.159 1.00 71.06 C ANISOU 2668 C ASP A1159 11157 7378 8464 1374 -322 -15 C ATOM 2669 O ASP A1159 -0.571 -57.047 598.199 1.00 76.66 O ANISOU 2669 O ASP A1159 11882 7983 9262 1222 -206 -47 O ATOM 2670 CB ASP A1159 -1.113 -56.976 601.368 1.00 62.48 C ANISOU 2670 CB ASP A1159 10477 6092 7171 1517 -240 251 C ATOM 2671 CG ASP A1159 -0.927 -57.532 602.766 1.00 78.98 C ANISOU 2671 CG ASP A1159 12819 8092 9099 1765 -261 394 C ATOM 2672 OD1 ASP A1159 -0.175 -58.518 602.921 1.00 89.36 O ANISOU 2672 OD1 ASP A1159 14269 9292 10390 1993 -290 425 O ATOM 2673 OD2 ASP A1159 -1.530 -56.979 603.710 1.00 76.51 O ANISOU 2673 OD2 ASP A1159 12571 7827 8674 1742 -247 475 O ATOM 2674 N ALA A1160 0.343 -55.183 599.081 1.00 64.13 N ANISOU 2674 N ALA A1160 10055 6722 7590 1329 -431 -90 N ATOM 2675 CA ALA A1160 0.145 -54.413 597.858 1.00 61.90 C ANISOU 2675 CA ALA A1160 9556 6556 7406 1100 -409 -180 C ATOM 2676 C ALA A1160 0.728 -55.136 596.653 1.00 69.03 C ANISOU 2676 C ALA A1160 10397 7442 8391 1090 -376 -285 C ATOM 2677 O ALA A1160 0.171 -55.076 595.550 1.00 79.56 O ANISOU 2677 O ALA A1160 11656 8786 9785 884 -295 -325 O ATOM 2678 CB ALA A1160 0.774 -53.027 598.001 1.00 58.61 C ANISOU 2678 CB ALA A1160 8921 6355 6992 1094 -531 -249 C ATOM 2679 N TYR A1161 1.850 -55.825 596.842 1.00 63.11 N ANISOU 2679 N TYR A1161 9669 6675 7635 1320 -441 -340 N ATOM 2680 CA TYR A1161 2.444 -56.637 595.782 1.00 60.07 C ANISOU 2680 CA TYR A1161 9239 6257 7327 1340 -401 -453 C ATOM 2681 C TYR A1161 1.864 -58.052 595.828 1.00 74.99 C ANISOU 2681 C TYR A1161 11381 7880 9234 1377 -280 -392 C ATOM 2682 O TYR A1161 2.573 -59.053 595.943 1.00 69.87 O ANISOU 2682 O TYR A1161 10829 7115 8602 1585 -289 -420 O ATOM 2683 CB TYR A1161 3.963 -56.640 595.909 1.00 66.02 C ANISOU 2683 CB TYR A1161 9862 7135 8088 1573 -529 -565 C ATOM 2684 CG TYR A1161 4.571 -55.253 595.851 1.00 73.51 C ANISOU 2684 CG TYR A1161 10554 8334 9043 1514 -629 -645 C ATOM 2685 CD1 TYR A1161 4.938 -54.683 594.637 1.00 80.86 C ANISOU 2685 CD1 TYR A1161 11266 9411 10048 1349 -598 -763 C ATOM 2686 CD2 TYR A1161 4.771 -54.511 597.008 1.00 81.92 C ANISOU 2686 CD2 TYR A1161 11602 9486 10039 1615 -743 -606 C ATOM 2687 CE1 TYR A1161 5.491 -53.415 594.579 1.00 72.85 C ANISOU 2687 CE1 TYR A1161 10029 8597 9054 1279 -665 -829 C ATOM 2688 CE2 TYR A1161 5.323 -53.242 596.960 1.00 68.54 C ANISOU 2688 CE2 TYR A1161 9672 7998 8371 1545 -822 -696 C ATOM 2689 CZ TYR A1161 5.680 -52.700 595.743 1.00 61.58 C ANISOU 2689 CZ TYR A1161 8583 7234 7582 1373 -776 -802 C ATOM 2690 OH TYR A1161 6.229 -51.439 595.689 1.00 59.35 O ANISOU 2690 OH TYR A1161 8078 7130 7341 1288 -832 -885 O ATOM 2691 N ARG A 238 0.532 -58.107 595.747 1.00 88.89 N ANISOU 2691 N ARG A 238 13241 9535 10998 1168 -161 -314 N ATOM 2692 CA ARG A 238 -0.203 -59.365 595.705 1.00 91.11 C ANISOU 2692 CA ARG A 238 13748 9553 11318 1133 -15 -269 C ATOM 2693 C ARG A 238 0.451 -60.349 594.747 1.00 82.81 C ANISOU 2693 C ARG A 238 12688 8422 10354 1189 26 -405 C ATOM 2694 O ARG A 238 1.027 -61.358 595.168 1.00 86.62 O ANISOU 2694 O ARG A 238 13331 8730 10850 1410 32 -387 O ATOM 2695 CB ARG A 238 -1.651 -59.136 595.263 1.00 83.05 C ANISOU 2695 CB ARG A 238 12724 8505 10325 836 105 -247 C ATOM 2696 CG ARG A 238 -2.587 -58.599 596.330 1.00 90.94 C ANISOU 2696 CG ARG A 238 13813 9485 11254 781 129 -101 C ATOM 2697 CD ARG A 238 -4.030 -58.941 595.979 1.00 97.66 C ANISOU 2697 CD ARG A 238 14725 10221 12159 529 287 -88 C ATOM 2698 NE ARG A 238 -4.292 -60.372 596.142 1.00 86.94 N ANISOU 2698 NE ARG A 238 13604 8581 10850 557 430 -63 N ATOM 2699 CZ ARG A 238 -5.115 -60.904 597.044 1.00 79.53 C ANISOU 2699 CZ ARG A 238 12882 7446 9891 533 557 62 C ATOM 2700 NH1 ARG A 238 -5.799 -60.141 597.888 1.00 87.27 N ANISOU 2700 NH1 ARG A 238 13867 8497 10795 481 561 166 N ATOM 2701 NH2 ARG A 238 -5.261 -62.219 597.097 1.00 88.52 N ANISOU 2701 NH2 ARG A 238 14220 8324 11091 551 694 79 N ATOM 2702 N ARG A 239 0.365 -60.048 593.453 1.00 79.07 N ANISOU 2702 N ARG A 239 12031 8079 9934 997 54 -540 N ATOM 2703 CA ARG A 239 0.833 -60.949 592.409 1.00105.59 C ANISOU 2703 CA ARG A 239 15369 11379 13373 1005 114 -696 C ATOM 2704 C ARG A 239 -0.106 -62.147 592.319 1.00 92.70 C ANISOU 2704 C ARG A 239 13953 9465 11805 914 274 -686 C ATOM 2705 O ARG A 239 0.307 -63.294 592.525 1.00 79.19 O ANISOU 2705 O ARG A 239 12409 7530 10150 1081 325 -701 O ATOM 2706 CB ARG A 239 2.278 -61.380 592.674 1.00 92.88 C ANISOU 2706 CB ARG A 239 13744 9770 11776 1306 24 -756 C ATOM 2707 CG ARG A 239 3.097 -61.595 591.406 1.00 47.44 C ANISOU 2707 CG ARG A 239 7812 4130 6083 1295 35 -962 C ATOM 2708 CD ARG A 239 4.556 -61.893 591.715 1.00 53.40 C ANISOU 2708 CD ARG A 239 8509 4923 6859 1601 -67 -1034 C ATOM 2709 NE ARG A 239 4.739 -63.237 592.258 1.00100.40 N ANISOU 2709 NE ARG A 239 14700 10586 12861 1831 -28 -1000 N ATOM 2710 CZ ARG A 239 5.918 -63.765 592.576 1.00 93.96 C ANISOU 2710 CZ ARG A 239 13878 9747 12074 2140 -109 -1055 C ATOM 2711 NH1 ARG A 239 7.034 -63.065 592.409 1.00 59.65 N ANISOU 2711 NH1 ARG A 239 9278 5666 7718 2242 -232 -1167 N ATOM 2712 NH2 ARG A 239 5.981 -64.997 593.062 1.00 86.88 N ANISOU 2712 NH2 ARG A 239 13227 8556 11225 2350 -64 -1000 N ATOM 2713 N ARG A 240 -1.376 -61.878 592.029 1.00 75.16 N ANISOU 2713 N ARG A 240 11725 7247 9585 651 356 -665 N ATOM 2714 CA ARG A 240 -2.364 -62.913 591.752 1.00 78.42 C ANISOU 2714 CA ARG A 240 12291 7427 10077 498 520 -700 C ATOM 2715 C ARG A 240 -2.287 -63.312 590.284 1.00 71.19 C ANISOU 2715 C ARG A 240 11252 6577 9222 363 567 -916 C ATOM 2716 O ARG A 240 -1.662 -62.628 589.476 1.00 55.21 O ANISOU 2716 O ARG A 240 9018 4802 7157 350 482 -1011 O ATOM 2717 CB ARG A 240 -3.762 -62.416 592.126 1.00 63.72 C ANISOU 2717 CB ARG A 240 10448 5571 8192 280 580 -602 C ATOM 2718 CG ARG A 240 -4.184 -62.773 593.550 1.00 82.39 C ANISOU 2718 CG ARG A 240 13054 7719 10533 374 642 -414 C ATOM 2719 CD ARG A 240 -5.579 -63.411 593.648 1.00 82.67 C ANISOU 2719 CD ARG A 240 13220 7556 10636 150 827 -397 C ATOM 2720 NE ARG A 240 -5.779 -64.014 594.968 1.00 97.20 N ANISOU 2720 NE ARG A 240 15261 9223 12447 263 897 -211 N ATOM 2721 CZ ARG A 240 -6.956 -64.216 595.559 1.00 79.67 C ANISOU 2721 CZ ARG A 240 13089 6950 10233 105 1020 -123 C ATOM 2722 NH1 ARG A 240 -8.088 -63.870 594.961 1.00 72.90 N ANISOU 2722 NH1 ARG A 240 12108 6167 9425 -168 1087 -211 N ATOM 2723 NH2 ARG A 240 -6.999 -64.774 596.762 1.00 69.68 N ANISOU 2723 NH2 ARG A 240 11990 5571 8914 225 1076 47 N ATOM 2724 N PRO A 241 -2.914 -64.428 589.906 1.00 63.57 N ANISOU 2724 N PRO A 241 10414 5388 8351 253 714 -1006 N ATOM 2725 CA PRO A 241 -2.767 -64.929 588.532 1.00 59.13 C ANISOU 2725 CA PRO A 241 9747 4880 7841 144 761 -1240 C ATOM 2726 C PRO A 241 -3.156 -63.891 587.490 1.00 55.72 C ANISOU 2726 C PRO A 241 9064 4781 7325 -66 698 -1322 C ATOM 2727 O PRO A 241 -3.843 -62.907 587.772 1.00 64.73 O ANISOU 2727 O PRO A 241 10129 6064 8400 -175 646 -1207 O ATOM 2728 CB PRO A 241 -3.712 -66.140 588.488 1.00 71.29 C ANISOU 2728 CB PRO A 241 11470 6118 9499 3 940 -1305 C ATOM 2729 CG PRO A 241 -3.855 -66.559 589.912 1.00 72.21 C ANISOU 2729 CG PRO A 241 11807 5992 9637 144 979 -1084 C ATOM 2730 CD PRO A 241 -3.780 -65.300 590.719 1.00 73.26 C ANISOU 2730 CD PRO A 241 11891 6299 9645 213 857 -909 C ATOM 2731 N GLY A 242 -2.691 -64.126 586.260 1.00 63.03 N ANISOU 2731 N GLY A 242 9868 5831 8249 -111 705 -1523 N ATOM 2732 CA GLY A 242 -2.937 -63.191 585.186 1.00 70.66 C ANISOU 2732 CA GLY A 242 10612 7122 9112 -285 646 -1595 C ATOM 2733 C GLY A 242 -4.288 -63.390 584.526 1.00 67.11 C ANISOU 2733 C GLY A 242 10136 6696 8665 -552 714 -1688 C ATOM 2734 O GLY A 242 -4.881 -64.469 584.558 1.00 42.44 O ANISOU 2734 O GLY A 242 7141 3340 5643 -629 833 -1782 O ATOM 2735 N ARG A 243 -4.771 -62.314 583.912 1.00 78.83 N ANISOU 2735 N ARG A 243 11446 8468 10038 -692 635 -1666 N ATOM 2736 CA ARG A 243 -6.047 -62.283 583.214 1.00 71.30 C ANISOU 2736 CA ARG A 243 10418 7615 9059 -934 660 -1755 C ATOM 2737 C ARG A 243 -5.819 -62.187 581.707 1.00 53.38 C ANISOU 2737 C ARG A 243 7993 5608 6683 -1027 635 -1942 C ATOM 2738 O ARG A 243 -4.685 -62.103 581.224 1.00 53.93 O ANISOU 2738 O ARG A 243 8011 5777 6702 -915 613 -1995 O ATOM 2739 CB ARG A 243 -6.900 -61.110 583.701 1.00 73.04 C ANISOU 2739 CB ARG A 243 10564 7966 9223 -1007 581 -1573 C ATOM 2740 CG ARG A 243 -7.774 -61.407 584.908 1.00 64.11 C ANISOU 2740 CG ARG A 243 9569 6599 8189 -1034 650 -1459 C ATOM 2741 CD ARG A 243 -8.769 -60.279 585.118 1.00 57.73 C ANISOU 2741 CD ARG A 243 8648 5960 7328 -1138 579 -1339 C ATOM 2742 NE ARG A 243 -8.115 -58.977 585.014 1.00 82.52 N ANISOU 2742 NE ARG A 243 11669 9320 10363 -1043 447 -1216 N ATOM 2743 CZ ARG A 243 -8.741 -57.835 584.744 1.00 81.92 C ANISOU 2743 CZ ARG A 243 11453 9456 10216 -1120 360 -1139 C ATOM 2744 NH1 ARG A 243 -8.049 -56.706 584.668 1.00 74.04 N ANISOU 2744 NH1 ARG A 243 10370 8618 9144 -1032 261 -1028 N ATOM 2745 NH2 ARG A 243 -10.053 -57.816 584.542 1.00 74.21 N ANISOU 2745 NH2 ARG A 243 10416 8529 9253 -1282 374 -1178 N ATOM 2746 N PHE A 244 -6.923 -62.199 580.962 1.00 56.55 N ANISOU 2746 N PHE A 244 8310 6136 7040 -1233 639 -2051 N ATOM 2747 CA PHE A 244 -6.924 -62.056 579.508 1.00 45.04 C ANISOU 2747 CA PHE A 244 6705 4963 5444 -1340 606 -2225 C ATOM 2748 C PHE A 244 -6.171 -63.181 578.813 1.00 42.38 C ANISOU 2748 C PHE A 244 6409 4551 5142 -1309 696 -2468 C ATOM 2749 O PHE A 244 -5.848 -63.073 577.625 1.00 43.15 O ANISOU 2749 O PHE A 244 6394 4893 5106 -1356 677 -2615 O ATOM 2750 CB PHE A 244 -6.344 -60.701 579.089 1.00 38.87 C ANISOU 2750 CB PHE A 244 5792 4476 4500 -1283 491 -2083 C ATOM 2751 CG PHE A 244 -7.031 -59.531 579.727 1.00 45.03 C ANISOU 2751 CG PHE A 244 6527 5327 5253 -1300 402 -1852 C ATOM 2752 CD1 PHE A 244 -8.253 -59.086 579.254 1.00 48.21 C ANISOU 2752 CD1 PHE A 244 6833 5899 5586 -1453 347 -1857 C ATOM 2753 CD2 PHE A 244 -6.456 -58.877 580.802 1.00 41.34 C ANISOU 2753 CD2 PHE A 244 6107 4765 4835 -1155 367 -1645 C ATOM 2754 CE1 PHE A 244 -8.888 -58.011 579.841 1.00 48.86 C ANISOU 2754 CE1 PHE A 244 6871 6037 5657 -1454 267 -1654 C ATOM 2755 CE2 PHE A 244 -7.085 -57.800 581.391 1.00 59.40 C ANISOU 2755 CE2 PHE A 244 8354 7108 7106 -1169 292 -1452 C ATOM 2756 CZ PHE A 244 -8.303 -57.367 580.910 1.00 65.65 C ANISOU 2756 CZ PHE A 244 9053 8052 7839 -1315 246 -1453 C ATOM 2757 N VAL A 245 -5.881 -64.266 579.528 1.00 39.54 N ANISOU 2757 N VAL A 245 5866 4111 5047 -122 33 1227 N ATOM 2758 CA VAL A 245 -5.212 -65.400 578.904 1.00 37.70 C ANISOU 2758 CA VAL A 245 5637 3798 4889 -174 -4 1213 C ATOM 2759 C VAL A 245 -6.113 -66.029 577.850 1.00 27.36 C ANISOU 2759 C VAL A 245 4307 2481 3608 -274 10 1210 C ATOM 2760 O VAL A 245 -5.673 -66.331 576.735 1.00 30.77 O ANISOU 2760 O VAL A 245 4722 2864 4105 -265 -27 1150 O ATOM 2761 CB VAL A 245 -4.786 -66.422 579.973 1.00 41.39 C ANISOU 2761 CB VAL A 245 6168 4226 5332 -223 -10 1295 C ATOM 2762 CG1 VAL A 245 -3.992 -67.554 579.339 1.00 52.06 C ANISOU 2762 CG1 VAL A 245 7546 5478 6756 -253 -64 1274 C ATOM 2763 CG2 VAL A 245 -3.975 -65.740 581.065 1.00 49.33 C ANISOU 2763 CG2 VAL A 245 7189 5248 6304 -134 -32 1306 C ATOM 2764 N ARG A 246 -7.391 -66.228 578.182 1.00 37.51 N ANISOU 2764 N ARG A 246 5589 3827 4838 -376 66 1281 N ATOM 2765 CA ARG A 246 -8.331 -66.757 577.200 1.00 39.13 C ANISOU 2765 CA ARG A 246 5755 4037 5074 -487 68 1284 C ATOM 2766 C ARG A 246 -8.462 -65.817 576.009 1.00 33.54 C ANISOU 2766 C ARG A 246 4983 3348 4414 -432 42 1194 C ATOM 2767 O ARG A 246 -8.509 -66.263 574.856 1.00 33.79 O ANISOU 2767 O ARG A 246 4998 3338 4501 -467 6 1156 O ATOM 2768 CB ARG A 246 -9.692 -66.987 577.855 1.00 30.37 C ANISOU 2768 CB ARG A 246 4616 3034 3890 -638 115 1398 C ATOM 2769 CG ARG A 246 -9.681 -68.063 578.920 1.00 57.22 C ANISOU 2769 CG ARG A 246 8076 6428 7236 -724 133 1496 C ATOM 2770 CD ARG A 246 -11.017 -68.148 579.641 1.00 58.11 C ANISOU 2770 CD ARG A 246 8124 6713 7242 -909 161 1640 C ATOM 2771 NE ARG A 246 -11.272 -66.969 580.466 1.00 63.82 N ANISOU 2771 NE ARG A 246 8800 7592 7857 -877 200 1695 N ATOM 2772 CZ ARG A 246 -12.314 -66.836 581.282 1.00 75.49 C ANISOU 2772 CZ ARG A 246 10183 9299 9199 -1005 266 1825 C ATOM 2773 NH1 ARG A 246 -13.209 -67.811 581.390 1.00 94.05 N ANISOU 2773 NH1 ARG A 246 12479 11733 11522 -1184 289 1911 N ATOM 2774 NH2 ARG A 246 -12.463 -65.727 581.996 1.00 73.68 N ANISOU 2774 NH2 ARG A 246 9900 9248 8848 -943 314 1870 N ATOM 2775 N LEU A 247 -8.519 -64.510 576.269 1.00 30.52 N ANISOU 2775 N LEU A 247 4571 3023 4002 -345 45 1164 N ATOM 2776 CA LEU A 247 -8.611 -63.538 575.187 1.00 32.29 C ANISOU 2776 CA LEU A 247 4721 3269 4278 -294 -8 1088 C ATOM 2777 C LEU A 247 -7.391 -63.615 574.279 1.00 30.39 C ANISOU 2777 C LEU A 247 4476 2969 4101 -226 -69 1008 C ATOM 2778 O LEU A 247 -7.512 -63.836 573.069 1.00 24.24 O ANISOU 2778 O LEU A 247 3665 2179 3367 -259 -95 974 O ATOM 2779 CB LEU A 247 -8.763 -62.133 575.773 1.00 29.74 C ANISOU 2779 CB LEU A 247 4340 3009 3950 -221 -68 1116 C ATOM 2780 CG LEU A 247 -8.336 -60.953 574.896 1.00 23.98 C ANISOU 2780 CG LEU A 247 3543 2286 3282 -108 -136 1009 C ATOM 2781 CD1 LEU A 247 -9.128 -60.923 573.616 1.00 44.56 C ANISOU 2781 CD1 LEU A 247 6047 4919 5965 -185 -166 1009 C ATOM 2782 CD2 LEU A 247 -8.509 -59.652 575.653 1.00 48.03 C ANISOU 2782 CD2 LEU A 247 6534 5376 6341 -9 -206 1045 C ATOM 2783 N VAL A 248 -6.198 -63.459 574.855 1.00 28.09 N ANISOU 2783 N VAL A 248 4216 2652 3805 -140 -88 987 N ATOM 2784 CA VAL A 248 -4.983 -63.436 574.046 1.00 22.28 C ANISOU 2784 CA VAL A 248 3460 1888 3116 -84 -133 924 C ATOM 2785 C VAL A 248 -4.839 -64.738 573.270 1.00 21.25 C ANISOU 2785 C VAL A 248 3375 1689 3011 -138 -117 933 C ATOM 2786 O VAL A 248 -4.376 -64.747 572.123 1.00 21.50 O ANISOU 2786 O VAL A 248 3387 1710 3073 -117 -138 888 O ATOM 2787 CB VAL A 248 -3.756 -63.163 574.935 1.00 25.00 C ANISOU 2787 CB VAL A 248 3823 2221 3454 -7 -152 919 C ATOM 2788 CG1 VAL A 248 -2.475 -63.311 574.135 1.00 27.76 C ANISOU 2788 CG1 VAL A 248 4155 2548 3845 32 -184 876 C ATOM 2789 CG2 VAL A 248 -3.842 -61.770 575.543 1.00 20.22 C ANISOU 2789 CG2 VAL A 248 3175 1674 2832 57 -185 898 C ATOM 2790 N ALA A 249 -5.229 -65.858 573.881 1.00 26.17 N ANISOU 2790 N ALA A 249 4060 2264 3620 -211 -86 998 N ATOM 2791 CA ALA A 249 -5.157 -67.135 573.181 1.00 27.48 C ANISOU 2791 CA ALA A 249 4276 2348 3818 -266 -92 1008 C ATOM 2792 C ALA A 249 -6.090 -67.156 571.977 1.00 24.01 C ANISOU 2792 C ALA A 249 3810 1921 3393 -331 -101 987 C ATOM 2793 O ALA A 249 -5.710 -67.621 570.897 1.00 36.36 O ANISOU 2793 O ALA A 249 5396 3432 4985 -321 -119 952 O ATOM 2794 CB ALA A 249 -5.493 -68.276 574.140 1.00 21.78 C ANISOU 2794 CB ALA A 249 3620 1577 3078 -354 -88 1091 C ATOM 2795 N ALA A 250 -7.315 -66.651 572.141 1.00 28.61 N ANISOU 2795 N ALA A 250 4343 2573 3955 -398 -88 1012 N ATOM 2796 CA ALA A 250 -8.277 -66.681 571.044 1.00 33.77 C ANISOU 2796 CA ALA A 250 4960 3245 4626 -477 -107 1001 C ATOM 2797 C ALA A 250 -7.819 -65.802 569.888 1.00 26.34 C ANISOU 2797 C ALA A 250 3970 2328 3710 -400 -140 926 C ATOM 2798 O ALA A 250 -7.848 -66.221 568.725 1.00 30.32 O ANISOU 2798 O ALA A 250 4493 2795 4232 -426 -164 900 O ATOM 2799 CB ALA A 250 -9.654 -66.240 571.543 1.00 44.82 C ANISOU 2799 CB ALA A 250 6294 4732 6004 -565 -79 1055 C ATOM 2800 N VAL A 251 -7.382 -64.578 570.188 1.00 18.82 N ANISOU 2800 N VAL A 251 2957 1437 2755 -310 -154 895 N ATOM 2801 CA VAL A 251 -6.988 -63.658 569.127 1.00 31.93 C ANISOU 2801 CA VAL A 251 4550 3139 4445 -255 -203 838 C ATOM 2802 C VAL A 251 -5.812 -64.223 568.342 1.00 28.84 C ANISOU 2802 C VAL A 251 4212 2689 4057 -207 -199 807 C ATOM 2803 O VAL A 251 -5.744 -64.091 567.114 1.00 31.93 O ANISOU 2803 O VAL A 251 4588 3085 4461 -209 -221 779 O ATOM 2804 CB VAL A 251 -6.664 -62.272 569.713 1.00 28.96 C ANISOU 2804 CB VAL A 251 4091 2834 4080 -177 -238 818 C ATOM 2805 CG1 VAL A 251 -6.251 -61.315 568.605 1.00 37.04 C ANISOU 2805 CG1 VAL A 251 5022 3906 5146 -142 -302 771 C ATOM 2806 CG2 VAL A 251 -7.863 -61.728 570.475 1.00 26.19 C ANISOU 2806 CG2 VAL A 251 3698 2529 3723 -206 -228 857 C ATOM 2807 N VAL A 252 -4.867 -64.859 569.036 1.00 23.23 N ANISOU 2807 N VAL A 252 3565 1923 3337 -162 -168 819 N ATOM 2808 CA VAL A 252 -3.718 -65.444 568.352 1.00 21.58 C ANISOU 2808 CA VAL A 252 3405 1654 3140 -106 -150 802 C ATOM 2809 C VAL A 252 -4.168 -66.564 567.425 1.00 20.33 C ANISOU 2809 C VAL A 252 3313 1413 2997 -164 -139 809 C ATOM 2810 O VAL A 252 -3.671 -66.696 566.300 1.00 38.32 O ANISOU 2810 O VAL A 252 5609 3664 5287 -130 -132 786 O ATOM 2811 CB VAL A 252 -2.677 -65.933 569.376 1.00 17.96 C ANISOU 2811 CB VAL A 252 2991 1150 2682 -51 -128 826 C ATOM 2812 CG1 VAL A 252 -1.616 -66.773 568.692 1.00 18.61 C ANISOU 2812 CG1 VAL A 252 3126 1150 2793 5 -98 827 C ATOM 2813 CG2 VAL A 252 -2.033 -64.749 570.076 1.00 17.14 C ANISOU 2813 CG2 VAL A 252 2823 1122 2567 7 -159 810 C ATOM 2814 N ALA A 253 -5.111 -67.391 567.878 1.00 24.03 N ANISOU 2814 N ALA A 253 3823 1841 3464 -260 -146 845 N ATOM 2815 CA ALA A 253 -5.641 -68.442 567.014 1.00 21.07 C ANISOU 2815 CA ALA A 253 3519 1386 3101 -339 -171 846 C ATOM 2816 C ALA A 253 -6.351 -67.844 565.808 1.00 24.12 C ANISOU 2816 C ALA A 253 3865 1819 3480 -378 -197 815 C ATOM 2817 O ALA A 253 -6.158 -68.293 564.672 1.00 44.99 O ANISOU 2817 O ALA A 253 6562 4405 6128 -379 -213 788 O ATOM 2818 CB ALA A 253 -6.590 -69.343 567.803 1.00 44.62 C ANISOU 2818 CB ALA A 253 6547 4332 6073 -459 -193 902 C ATOM 2819 N ALA A 254 -7.180 -66.823 566.037 1.00 35.69 N ANISOU 2819 N ALA A 254 5238 3386 4937 -409 -208 821 N ATOM 2820 CA ALA A 254 -7.858 -66.156 564.931 1.00 28.70 C ANISOU 2820 CA ALA A 254 4299 2555 4053 -447 -249 799 C ATOM 2821 C ALA A 254 -6.851 -65.550 563.963 1.00 26.99 C ANISOU 2821 C ALA A 254 4069 2350 3836 -355 -251 757 C ATOM 2822 O ALA A 254 -6.960 -65.719 562.744 1.00 26.60 O ANISOU 2822 O ALA A 254 4049 2276 3780 -381 -272 739 O ATOM 2823 CB ALA A 254 -8.795 -65.077 565.473 1.00 25.52 C ANISOU 2823 CB ALA A 254 3780 2258 3659 -476 -269 819 C ATOM 2824 N PHE A 255 -5.854 -64.845 564.498 1.00 29.66 N ANISOU 2824 N PHE A 255 4364 2728 4175 -256 -234 748 N ATOM 2825 CA PHE A 255 -4.817 -64.260 563.656 1.00 23.25 C ANISOU 2825 CA PHE A 255 3532 1940 3363 -178 -234 725 C ATOM 2826 C PHE A 255 -4.150 -65.317 562.787 1.00 25.82 C ANISOU 2826 C PHE A 255 3961 2164 3687 -149 -184 723 C ATOM 2827 O PHE A 255 -3.877 -65.080 561.605 1.00 33.98 O ANISOU 2827 O PHE A 255 4998 3200 4712 -131 -186 715 O ATOM 2828 CB PHE A 255 -3.782 -63.560 564.536 1.00 26.44 C ANISOU 2828 CB PHE A 255 3884 2391 3771 -95 -233 723 C ATOM 2829 CG PHE A 255 -2.559 -63.115 563.797 1.00 16.74 C ANISOU 2829 CG PHE A 255 2639 1180 2541 -21 -227 716 C ATOM 2830 CD1 PHE A 255 -2.515 -61.871 563.194 1.00 24.52 C ANISOU 2830 CD1 PHE A 255 3508 2258 3549 -29 -293 709 C ATOM 2831 CD2 PHE A 255 -1.449 -63.937 563.713 1.00 20.84 C ANISOU 2831 CD2 PHE A 255 3248 1624 3047 53 -158 728 C ATOM 2832 CE1 PHE A 255 -1.386 -61.455 562.515 1.00 26.84 C ANISOU 2832 CE1 PHE A 255 3778 2574 3844 24 -290 718 C ATOM 2833 CE2 PHE A 255 -0.318 -63.530 563.036 1.00 25.52 C ANISOU 2833 CE2 PHE A 255 3833 2236 3627 125 -147 735 C ATOM 2834 CZ PHE A 255 -0.284 -62.286 562.436 1.00 24.26 C ANISOU 2834 CZ PHE A 255 3558 2176 3484 104 -216 732 C ATOM 2835 N ALA A 256 -3.880 -66.494 563.357 1.00 25.36 N ANISOU 2835 N ALA A 256 3979 2010 3645 -144 -152 738 N ATOM 2836 CA ALA A 256 -3.160 -67.524 562.616 1.00 27.52 C ANISOU 2836 CA ALA A 256 4335 2175 3946 -105 -130 736 C ATOM 2837 C ALA A 256 -4.016 -68.118 561.504 1.00 24.63 C ANISOU 2837 C ALA A 256 4047 1750 3562 -193 -178 710 C ATOM 2838 O ALA A 256 -3.523 -68.352 560.395 1.00 39.21 O ANISOU 2838 O ALA A 256 5943 3547 5407 -156 -177 691 O ATOM 2839 CB ALA A 256 -2.690 -68.621 563.570 1.00 35.78 C ANISOU 2839 CB ALA A 256 5442 3129 5023 -89 -123 755 C ATOM 2840 N LEU A 257 -5.298 -68.372 561.778 1.00 35.73 N ANISOU 2840 N LEU A 257 5469 3159 4948 -314 -227 713 N ATOM 2841 CA LEU A 257 -6.143 -69.020 560.779 1.00 31.52 C ANISOU 2841 CA LEU A 257 5024 2564 4387 -416 -287 689 C ATOM 2842 C LEU A 257 -6.518 -68.073 559.647 1.00 36.60 C ANISOU 2842 C LEU A 257 5617 3283 5007 -437 -308 674 C ATOM 2843 O LEU A 257 -6.654 -68.511 558.500 1.00 47.41 O ANISOU 2843 O LEU A 257 7078 4590 6345 -473 -343 644 O ATOM 2844 CB LEU A 257 -7.411 -69.573 561.431 1.00 35.87 C ANISOU 2844 CB LEU A 257 5591 3107 4930 -552 -338 718 C ATOM 2845 CG LEU A 257 -7.220 -70.688 562.459 1.00 43.16 C ANISOU 2845 CG LEU A 257 6592 3942 5867 -567 -341 744 C ATOM 2846 CD1 LEU A 257 -8.565 -71.121 563.017 1.00 52.46 C ANISOU 2846 CD1 LEU A 257 7768 5132 7033 -721 -393 793 C ATOM 2847 CD2 LEU A 257 -6.485 -71.872 561.850 1.00 39.11 C ANISOU 2847 CD2 LEU A 257 6235 3274 5350 -531 -369 704 C ATOM 2848 N CYS A 258 -6.698 -66.786 559.939 1.00 34.33 N ANISOU 2848 N CYS A 258 5197 3122 4726 -419 -303 691 N ATOM 2849 CA CYS A 258 -7.183 -65.869 558.914 1.00 20.48 C ANISOU 2849 CA CYS A 258 3386 1442 2954 -458 -350 685 C ATOM 2850 C CYS A 258 -6.064 -65.414 557.985 1.00 21.94 C ANISOU 2850 C CYS A 258 3578 1631 3125 -364 -317 680 C ATOM 2851 O CYS A 258 -6.244 -65.387 556.763 1.00 36.25 O ANISOU 2851 O CYS A 258 5435 3432 4905 -403 -347 672 O ATOM 2852 CB CYS A 258 -7.854 -64.662 559.569 1.00 42.88 C ANISOU 2852 CB CYS A 258 6074 4405 5812 -476 -390 706 C ATOM 2853 SG CYS A 258 -9.297 -65.075 560.573 1.00 22.78 S ANISOU 2853 SG CYS A 258 3499 1872 3285 -589 -415 737 S ATOM 2854 N TRP A 259 -4.908 -65.055 558.541 1.00 25.36 N ANISOU 2854 N TRP A 259 3971 2086 3577 -247 -256 694 N ATOM 2855 CA TRP A 259 -3.795 -64.562 557.741 1.00 33.66 C ANISOU 2855 CA TRP A 259 5013 3159 4619 -154 -216 714 C ATOM 2856 C TRP A 259 -2.895 -65.670 557.211 1.00 38.98 C ANISOU 2856 C TRP A 259 5785 3716 5310 -82 -158 722 C ATOM 2857 O TRP A 259 -2.106 -65.417 556.293 1.00 42.42 O ANISOU 2857 O TRP A 259 6217 4163 5739 -14 -129 757 O ATOM 2858 CB TRP A 259 -2.962 -63.573 558.560 1.00 16.32 C ANISOU 2858 CB TRP A 259 2720 1051 2430 -74 -204 729 C ATOM 2859 CG TRP A 259 -3.687 -62.294 558.802 1.00 23.66 C ANISOU 2859 CG TRP A 259 3513 2100 3376 -139 -309 721 C ATOM 2860 CD1 TRP A 259 -4.433 -61.967 559.896 1.00 29.14 C ANISOU 2860 CD1 TRP A 259 4133 2836 4104 -180 -355 710 C ATOM 2861 CD2 TRP A 259 -3.754 -61.170 557.918 1.00 28.29 C ANISOU 2861 CD2 TRP A 259 4003 2776 3971 -168 -384 737 C ATOM 2862 NE1 TRP A 259 -4.955 -60.705 559.751 1.00 31.58 N ANISOU 2862 NE1 TRP A 259 4298 3247 4455 -220 -452 714 N ATOM 2863 CE2 TRP A 259 -4.553 -60.194 558.545 1.00 28.41 C ANISOU 2863 CE2 TRP A 259 3873 2877 4044 -222 -481 729 C ATOM 2864 CE3 TRP A 259 -3.213 -60.894 556.659 1.00 28.06 C ANISOU 2864 CE3 TRP A 259 3991 2761 3907 -152 -378 767 C ATOM 2865 CZ2 TRP A 259 -4.823 -58.960 557.956 1.00 33.95 C ANISOU 2865 CZ2 TRP A 259 4437 3670 4791 -269 -583 744 C ATOM 2866 CZ3 TRP A 259 -3.483 -59.669 556.075 1.00 26.17 C ANISOU 2866 CZ3 TRP A 259 3619 2626 3699 -210 -482 787 C ATOM 2867 CH2 TRP A 259 -4.281 -58.717 556.723 1.00 39.90 C ANISOU 2867 CH2 TRP A 259 5204 4441 5517 -272 -589 773 C ATOM 2868 N GLY A 260 -2.996 -66.883 557.748 1.00 33.47 N ANISOU 2868 N GLY A 260 5173 2910 4635 -98 -165 694 N ATOM 2869 CA GLY A 260 -2.220 -67.994 557.254 1.00 30.36 C ANISOU 2869 CA GLY A 260 4895 2389 4251 -36 -161 669 C ATOM 2870 C GLY A 260 -2.492 -68.274 555.788 1.00 34.30 C ANISOU 2870 C GLY A 260 5599 2802 4634 -79 -235 621 C ATOM 2871 O GLY A 260 -1.582 -68.271 554.954 1.00 25.20 O ANISOU 2871 O GLY A 260 4560 1600 3415 17 -229 616 O ATOM 2872 N PRO A 261 -3.762 -68.515 555.443 1.00 33.29 N ANISOU 2872 N PRO A 261 5551 2648 4449 -225 -311 585 N ATOM 2873 CA PRO A 261 -4.089 -68.790 554.033 1.00 34.71 C ANISOU 2873 CA PRO A 261 5965 2734 4489 -292 -398 533 C ATOM 2874 C PRO A 261 -3.656 -67.687 553.091 1.00 32.32 C ANISOU 2874 C PRO A 261 5641 2511 4129 -265 -396 583 C ATOM 2875 O PRO A 261 -3.174 -67.970 551.986 1.00 33.94 O ANISOU 2875 O PRO A 261 6088 2614 4192 -223 -411 547 O ATOM 2876 CB PRO A 261 -5.617 -68.944 554.053 1.00 27.88 C ANISOU 2876 CB PRO A 261 5086 1890 3616 -475 -486 523 C ATOM 2877 CG PRO A 261 -5.941 -69.345 555.443 1.00 35.65 C ANISOU 2877 CG PRO A 261 5942 2900 4703 -475 -442 544 C ATOM 2878 CD PRO A 261 -4.944 -68.633 556.313 1.00 42.44 C ANISOU 2878 CD PRO A 261 6618 3854 5655 -334 -327 592 C ATOM 2879 N TYR A 262 -3.811 -66.427 553.500 1.00 31.26 N ANISOU 2879 N TYR A 262 5245 2552 4080 -276 -372 662 N ATOM 2880 CA TYR A 262 -3.416 -65.322 552.636 1.00 30.39 C ANISOU 2880 CA TYR A 262 5081 2541 3925 -264 -386 734 C ATOM 2881 C TYR A 262 -1.944 -65.423 552.260 1.00 30.35 C ANISOU 2881 C TYR A 262 5159 2502 3871 -99 -318 778 C ATOM 2882 O TYR A 262 -1.584 -65.340 551.080 1.00 31.81 O ANISOU 2882 O TYR A 262 5522 2664 3900 -81 -336 805 O ATOM 2883 CB TYR A 262 -3.697 -63.989 553.326 1.00 29.60 C ANISOU 2883 CB TYR A 262 4701 2623 3924 -264 -364 780 C ATOM 2884 CG TYR A 262 -3.006 -62.836 552.647 1.00 19.26 C ANISOU 2884 CG TYR A 262 3299 1431 2587 -222 -369 861 C ATOM 2885 CD1 TYR A 262 -3.457 -62.361 551.427 1.00 25.97 C ANISOU 2885 CD1 TYR A 262 4187 2326 3355 -337 -475 899 C ATOM 2886 CD2 TYR A 262 -1.893 -62.234 553.216 1.00 23.60 C ANISOU 2886 CD2 TYR A 262 3732 2060 3175 -80 -274 900 C ATOM 2887 CE1 TYR A 262 -2.827 -61.312 550.794 1.00 33.00 C ANISOU 2887 CE1 TYR A 262 4970 3351 4219 -312 -490 987 C ATOM 2888 CE2 TYR A 262 -1.256 -61.183 552.592 1.00 26.52 C ANISOU 2888 CE2 TYR A 262 4020 2549 3506 -54 -297 967 C ATOM 2889 CZ TYR A 262 -1.728 -60.726 551.380 1.00 28.73 C ANISOU 2889 CZ TYR A 262 4304 2887 3726 -170 -403 1020 C ATOM 2890 OH TYR A 262 -1.096 -59.679 550.750 1.00 25.12 O ANISOU 2890 OH TYR A 262 3731 2572 3241 -162 -432 1096 O ATOM 2891 N HIS A 263 -1.076 -65.618 553.255 1.00 30.44 N ANISOU 2891 N HIS A 263 5051 2522 3993 29 -235 793 N ATOM 2892 CA HIS A 263 0.355 -65.659 552.983 1.00 39.10 C ANISOU 2892 CA HIS A 263 6184 3615 5058 200 -177 844 C ATOM 2893 C HIS A 263 0.739 -66.880 552.158 1.00 34.19 C ANISOU 2893 C HIS A 263 5936 2798 4257 320 -141 737 C ATOM 2894 O HIS A 263 1.735 -66.842 551.429 1.00 42.22 O ANISOU 2894 O HIS A 263 7071 3822 5151 507 -54 772 O ATOM 2895 CB HIS A 263 1.138 -65.630 554.296 1.00 20.73 C ANISOU 2895 CB HIS A 263 3625 1341 2910 269 -137 878 C ATOM 2896 CG HIS A 263 1.077 -64.310 555.002 1.00 19.75 C ANISOU 2896 CG HIS A 263 3192 1428 2885 243 -78 946 C ATOM 2897 ND1 HIS A 263 0.363 -64.117 556.165 1.00 32.21 N ANISOU 2897 ND1 HIS A 263 4757 3033 4447 216 -15 866 N ATOM 2898 CD2 HIS A 263 1.635 -63.113 554.702 1.00 26.94 C ANISOU 2898 CD2 HIS A 263 4092 2491 3653 330 12 949 C ATOM 2899 CE1 HIS A 263 0.490 -62.861 556.555 1.00 26.23 C ANISOU 2899 CE1 HIS A 263 4016 2365 3586 220 -57 837 C ATOM 2900 NE2 HIS A 263 1.256 -62.230 555.684 1.00 20.62 N ANISOU 2900 NE2 HIS A 263 3321 1716 2797 267 -81 864 N ATOM 2901 N VAL A 264 -0.032 -67.965 552.250 1.00 33.44 N ANISOU 2901 N VAL A 264 6025 2543 4137 245 -187 608 N ATOM 2902 CA VAL A 264 0.276 -69.152 551.457 1.00 32.01 C ANISOU 2902 CA VAL A 264 6212 2156 3794 371 -161 469 C ATOM 2903 C VAL A 264 0.146 -68.841 549.971 1.00 32.67 C ANISOU 2903 C VAL A 264 6462 2286 3665 369 -156 438 C ATOM 2904 O VAL A 264 1.060 -69.103 549.180 1.00 39.58 O ANISOU 2904 O VAL A 264 7385 3257 4398 562 -43 357 O ATOM 2905 CB VAL A 264 -0.632 -70.325 551.868 1.00 32.11 C ANISOU 2905 CB VAL A 264 6328 2033 3837 243 -249 352 C ATOM 2906 CG1 VAL A 264 -0.574 -71.434 550.830 1.00 41.88 C ANISOU 2906 CG1 VAL A 264 7953 3065 4896 328 -267 181 C ATOM 2907 CG2 VAL A 264 -0.225 -70.857 553.233 1.00 38.36 C ANISOU 2907 CG2 VAL A 264 6938 2838 4798 284 -223 368 C ATOM 2908 N PHE A 265 -0.986 -68.259 549.571 1.00 31.42 N ANISOU 2908 N PHE A 265 6263 2191 3485 131 -267 477 N ATOM 2909 CA PHE A 265 -1.208 -68.001 548.153 1.00 39.44 C ANISOU 2909 CA PHE A 265 7323 3365 4298 75 -275 419 C ATOM 2910 C PHE A 265 -0.298 -66.899 547.629 1.00 30.93 C ANISOU 2910 C PHE A 265 6010 2582 3161 171 -180 538 C ATOM 2911 O PHE A 265 0.139 -66.958 546.475 1.00 37.13 O ANISOU 2911 O PHE A 265 6851 3518 3738 246 -110 470 O ATOM 2912 CB PHE A 265 -2.674 -67.649 547.908 1.00 37.04 C ANISOU 2912 CB PHE A 265 7019 3045 4008 -212 -438 450 C ATOM 2913 CG PHE A 265 -3.559 -68.848 547.738 1.00 37.72 C ANISOU 2913 CG PHE A 265 7393 2894 4046 -325 -541 304 C ATOM 2914 CD1 PHE A 265 -4.060 -69.519 548.840 1.00 31.39 C ANISOU 2914 CD1 PHE A 265 6612 1915 3400 -384 -595 302 C ATOM 2915 CD2 PHE A 265 -3.885 -69.309 546.473 1.00 35.55 C ANISOU 2915 CD2 PHE A 265 7324 2621 3561 -373 -589 169 C ATOM 2916 CE1 PHE A 265 -4.873 -70.626 548.682 1.00 42.81 C ANISOU 2916 CE1 PHE A 265 8223 3239 4805 -489 -695 186 C ATOM 2917 CE2 PHE A 265 -4.696 -70.413 546.309 1.00 51.75 C ANISOU 2917 CE2 PHE A 265 9654 4435 5573 -488 -714 42 C ATOM 2918 CZ PHE A 265 -5.192 -71.072 547.415 1.00 48.41 C ANISOU 2918 CZ PHE A 265 9244 3827 5321 -556 -778 65 C ATOM 2919 N SER A 266 0.005 -65.896 548.455 1.00 33.39 N ANISOU 2919 N SER A 266 6063 2981 3643 165 -183 719 N ATOM 2920 CA SER A 266 0.866 -64.810 547.998 1.00 39.61 C ANISOU 2920 CA SER A 266 6619 4039 4392 230 -122 863 C ATOM 2921 C SER A 266 2.253 -65.327 547.639 1.00 42.14 C ANISOU 2921 C SER A 266 6960 4449 4601 495 53 814 C ATOM 2922 O SER A 266 2.868 -64.860 546.673 1.00 37.95 O ANISOU 2922 O SER A 266 6335 4167 3915 548 129 861 O ATOM 2923 CB SER A 266 0.953 -63.725 549.070 1.00 36.46 C ANISOU 2923 CB SER A 266 5969 3669 4214 185 -185 1054 C ATOM 2924 OG SER A 266 1.633 -62.580 548.583 1.00 49.74 O ANISOU 2924 OG SER A 266 7426 5601 5871 197 -175 1218 O ATOM 2925 N LEU A 267 2.768 -66.285 548.413 1.00 29.99 N ANISOU 2925 N LEU A 267 5532 2721 3141 664 118 730 N ATOM 2926 CA LEU A 267 4.061 -66.878 548.087 1.00 31.08 C ANISOU 2926 CA LEU A 267 5694 2930 3185 941 285 666 C ATOM 2927 C LEU A 267 3.977 -67.712 546.815 1.00 40.00 C ANISOU 2927 C LEU A 267 7058 4085 4054 1013 345 456 C ATOM 2928 O LEU A 267 4.886 -67.670 545.977 1.00 40.65 O ANISOU 2928 O LEU A 267 7086 4392 3968 1185 488 437 O ATOM 2929 CB LEU A 267 4.556 -67.721 549.261 1.00 30.55 C ANISOU 2929 CB LEU A 267 5700 2624 3283 1096 311 627 C ATOM 2930 CG LEU A 267 4.793 -66.938 550.556 1.00 33.45 C ANISOU 2930 CG LEU A 267 5849 2972 3888 1054 260 828 C ATOM 2931 CD1 LEU A 267 4.945 -67.883 551.735 1.00 29.15 C ANISOU 2931 CD1 LEU A 267 5410 2169 3495 1129 242 766 C ATOM 2932 CD2 LEU A 267 6.014 -66.034 550.435 1.00 32.26 C ANISOU 2932 CD2 LEU A 267 5423 3082 3753 1179 350 1004 C ATOM 2933 N LEU A 268 2.892 -68.474 546.649 1.00 34.99 N ANISOU 2933 N LEU A 268 6685 3233 3376 883 235 299 N ATOM 2934 CA LEU A 268 2.683 -69.182 545.391 1.00 41.33 C ANISOU 2934 CA LEU A 268 7733 4052 3920 920 255 96 C ATOM 2935 C LEU A 268 2.720 -68.212 544.220 1.00 41.55 C ANISOU 2935 C LEU A 268 7622 4412 3754 839 289 177 C ATOM 2936 O LEU A 268 3.319 -68.501 543.178 1.00 61.00 O ANISOU 2936 O LEU A 268 10161 7043 5974 993 410 69 O ATOM 2937 CB LEU A 268 1.349 -69.928 545.422 1.00 44.47 C ANISOU 2937 CB LEU A 268 8399 4171 4325 720 80 -32 C ATOM 2938 CG LEU A 268 1.275 -71.154 546.336 1.00 37.72 C ANISOU 2938 CG LEU A 268 7758 2969 3604 796 32 -147 C ATOM 2939 CD1 LEU A 268 -0.160 -71.644 546.454 1.00 42.97 C ANISOU 2939 CD1 LEU A 268 8620 3399 4307 528 -167 -199 C ATOM 2940 CD2 LEU A 268 2.174 -72.268 545.822 1.00 51.88 C ANISOU 2940 CD2 LEU A 268 9774 4686 5251 1095 139 -364 C ATOM 2941 N GLU A 269 2.091 -67.047 544.383 1.00 37.71 N ANISOU 2941 N GLU A 269 6931 4028 3368 603 180 370 N ATOM 2942 CA GLU A 269 2.147 -66.015 543.355 1.00 35.38 C ANISOU 2942 CA GLU A 269 6478 4046 2918 504 185 489 C ATOM 2943 C GLU A 269 3.588 -65.669 543.005 1.00 46.47 C ANISOU 2943 C GLU A 269 7697 5733 4225 726 375 575 C ATOM 2944 O GLU A 269 3.937 -65.537 541.825 1.00 57.62 O ANISOU 2944 O GLU A 269 9115 7396 5381 764 460 552 O ATOM 2945 CB GLU A 269 1.404 -64.772 543.843 1.00 37.09 C ANISOU 2945 CB GLU A 269 6473 4297 3323 256 28 701 C ATOM 2946 CG GLU A 269 1.130 -63.738 542.774 1.00 33.00 C ANISOU 2946 CG GLU A 269 5832 4040 2665 88 -35 824 C ATOM 2947 CD GLU A 269 0.714 -62.401 543.358 1.00 30.46 C ANISOU 2947 CD GLU A 269 5249 3765 2560 -92 -180 1053 C ATOM 2948 OE1 GLU A 269 0.734 -62.254 544.599 1.00 45.24 O ANISOU 2948 OE1 GLU A 269 7027 5489 4673 -65 -210 1113 O ATOM 2949 OE2 GLU A 269 0.367 -61.492 542.576 1.00 60.52 O ANISOU 2949 OE2 GLU A 269 8951 7751 6292 -257 -274 1171 O ATOM 2950 N ALA A 270 4.441 -65.514 544.020 1.00 44.37 N ANISOU 2950 N ALA A 270 7259 5444 4156 867 441 685 N ATOM 2951 CA ALA A 270 5.847 -65.225 543.763 1.00 48.16 C ANISOU 2951 CA ALA A 270 7539 6193 4567 1080 618 787 C ATOM 2952 C ALA A 270 6.508 -66.372 543.012 1.00 58.01 C ANISOU 2952 C ALA A 270 8979 7479 5582 1348 796 559 C ATOM 2953 O ALA A 270 7.304 -66.148 542.091 1.00 61.28 O ANISOU 2953 O ALA A 270 9290 8209 5785 1467 945 590 O ATOM 2954 CB ALA A 270 6.574 -64.950 545.080 1.00 44.62 C ANISOU 2954 CB ALA A 270 6896 5667 4392 1174 628 939 C ATOM 2955 N ARG A 271 6.185 -67.612 543.389 1.00 65.56 N ANISOU 2955 N ARG A 271 10218 8121 6570 1448 777 329 N ATOM 2956 CA ARG A 271 6.725 -68.771 542.691 1.00 69.43 C ANISOU 2956 CA ARG A 271 10935 8600 6847 1717 917 76 C ATOM 2957 C ARG A 271 6.067 -68.985 541.335 1.00 73.04 C ANISOU 2957 C ARG A 271 11608 9149 6995 1631 897 -85 C ATOM 2958 O ARG A 271 6.666 -69.628 540.467 1.00 73.86 O ANISOU 2958 O ARG A 271 11841 9375 6848 1862 1044 -265 O ATOM 2959 CB ARG A 271 6.556 -70.021 543.555 1.00 65.82 C ANISOU 2959 CB ARG A 271 10728 7741 6539 1835 863 -108 C ATOM 2960 CG ARG A 271 7.109 -71.293 542.931 1.00 79.55 C ANISOU 2960 CG ARG A 271 12728 9409 8087 2140 980 -394 C ATOM 2961 CD ARG A 271 7.084 -72.454 543.919 1.00100.76 C ANISOU 2961 CD ARG A 271 15628 11690 10968 2261 907 -532 C ATOM 2962 NE ARG A 271 6.103 -73.476 543.556 1.00108.51 N ANISOU 2962 NE ARG A 271 17003 12371 11855 2183 760 -776 N ATOM 2963 CZ ARG A 271 6.329 -74.471 542.702 1.00119.02 C ANISOU 2963 CZ ARG A 271 18617 13641 12964 2401 810 -1054 C ATOM 2964 NH1 ARG A 271 7.508 -74.592 542.103 1.00114.27 N ANISOU 2964 NH1 ARG A 271 17937 13281 12200 2730 1028 -1133 N ATOM 2965 NH2 ARG A 271 5.370 -75.350 542.441 1.00101.09 N ANISOU 2965 NH2 ARG A 271 16709 11069 10631 2293 635 -1254 N ATOM 2966 N ALA A 272 4.859 -68.454 541.129 1.00 67.84 N ANISOU 2966 N ALA A 272 10990 8444 6344 1312 715 -27 N ATOM 2967 CA ALA A 272 4.149 -68.655 539.872 1.00 51.97 C ANISOU 2967 CA ALA A 272 9199 6498 4049 1199 662 -170 C ATOM 2968 C ALA A 272 4.757 -67.874 538.716 1.00 64.66 C ANISOU 2968 C ALA A 272 10639 8540 5389 1221 791 -70 C ATOM 2969 O ALA A 272 4.414 -68.149 537.561 1.00 63.80 O ANISOU 2969 O ALA A 272 10727 8528 4985 1190 790 -214 O ATOM 2970 CB ALA A 272 2.679 -68.266 540.028 1.00 58.11 C ANISOU 2970 CB ALA A 272 10035 7108 4937 844 419 -109 C ATOM 2971 N HIS A 273 5.632 -66.905 538.990 1.00 64.63 N ANISOU 2971 N HIS A 273 10282 8801 5473 1258 889 182 N ATOM 2972 CA HIS A 273 6.326 -66.223 537.904 1.00 50.66 C ANISOU 2972 CA HIS A 273 8339 7469 3442 1289 1025 297 C ATOM 2973 C HIS A 273 7.103 -67.221 537.055 1.00 66.20 C ANISOU 2973 C HIS A 273 10483 9570 5101 1607 1243 50 C ATOM 2974 O HIS A 273 6.977 -67.242 535.825 1.00 67.81 O ANISOU 2974 O HIS A 273 10800 9993 4971 1586 1290 -36 O ATOM 2975 CB HIS A 273 7.264 -65.154 538.465 1.00 55.29 C ANISOU 2975 CB HIS A 273 8520 8287 4203 1303 1090 612 C ATOM 2976 CG HIS A 273 8.077 -64.458 537.418 1.00 63.71 C ANISOU 2976 CG HIS A 273 9373 9824 5012 1332 1235 769 C ATOM 2977 ND1 HIS A 273 9.260 -64.972 536.931 1.00 56.93 N ANISOU 2977 ND1 HIS A 273 8466 9217 3950 1644 1494 694 N ATOM 2978 CD2 HIS A 273 7.876 -63.291 536.761 1.00 60.19 C ANISOU 2978 CD2 HIS A 273 8742 9653 4475 1086 1156 1008 C ATOM 2979 CE1 HIS A 273 9.752 -64.152 536.019 1.00 56.83 C ANISOU 2979 CE1 HIS A 273 8239 9634 3719 1579 1579 888 C ATOM 2980 NE2 HIS A 273 8.933 -63.123 535.899 1.00 52.83 N ANISOU 2980 NE2 HIS A 273 7653 9142 3279 1234 1368 1086 N ATOM 2981 N ALA A 274 7.913 -68.061 537.700 1.00 71.29 N ANISOU 2981 N ALA A 274 11158 10083 5848 1914 1372 -72 N ATOM 2982 CA ALA A 274 8.667 -69.077 536.975 1.00 58.15 C ANISOU 2982 CA ALA A 274 9669 8515 3912 2260 1577 -334 C ATOM 2983 C ALA A 274 7.773 -70.235 536.545 1.00 69.08 C ANISOU 2983 C ALA A 274 11513 9582 5151 2271 1466 -678 C ATOM 2984 O ALA A 274 7.850 -70.695 535.400 1.00 74.56 O ANISOU 2984 O ALA A 274 12407 10429 5496 2391 1555 -882 O ATOM 2985 CB ALA A 274 9.821 -69.583 537.840 1.00 64.97 C ANISOU 2985 CB ALA A 274 10404 9323 4960 2589 1729 -343 C ATOM 2986 N ASN A 275 6.918 -70.722 537.449 1.00 57.61 N ANISOU 2986 N ASN A 275 10239 7694 3957 2141 1264 -741 N ATOM 2987 CA ASN A 275 6.022 -71.830 537.147 1.00 59.11 C ANISOU 2987 CA ASN A 275 10864 7544 4050 2117 1118 -1038 C ATOM 2988 C ASN A 275 4.658 -71.282 536.748 1.00 64.11 C ANISOU 2988 C ASN A 275 11579 8129 4650 1717 894 -964 C ATOM 2989 O ASN A 275 3.844 -70.960 537.628 1.00 74.36 O ANISOU 2989 O ASN A 275 12817 9207 6230 1468 713 -826 O ATOM 2990 CB ASN A 275 5.892 -72.761 538.354 1.00 61.78 C ANISOU 2990 CB ASN A 275 11353 7436 4683 2201 1019 -1137 C ATOM 2991 CG ASN A 275 7.210 -73.401 538.744 1.00 92.11 C ANISOU 2991 CG ASN A 275 15139 11287 8570 2608 1217 -1228 C ATOM 2992 OD1 ASN A 275 7.670 -73.263 539.880 1.00 94.13 O ANISOU 2992 OD1 ASN A 275 15200 11448 9118 2658 1229 -1078 O ATOM 2993 ND2 ASN A 275 7.827 -74.105 537.802 1.00102.04 N ANISOU 2993 ND2 ASN A 275 16571 12665 9534 2910 1369 -1478 N ATOM 2994 N PRO A 276 4.357 -71.146 535.453 1.00 59.84 N ANISOU 2994 N PRO A 276 11166 7797 3772 1643 896 -1046 N ATOM 2995 CA PRO A 276 3.045 -70.603 535.065 1.00 68.23 C ANISOU 2995 CA PRO A 276 12295 8813 4818 1255 665 -960 C ATOM 2996 C PRO A 276 1.877 -71.487 535.460 1.00 68.15 C ANISOU 2996 C PRO A 276 12611 8349 4935 1103 423 -1122 C ATOM 2997 O PRO A 276 0.743 -70.995 535.515 1.00 64.11 O ANISOU 2997 O PRO A 276 12086 7748 4524 766 214 -1002 O ATOM 2998 CB PRO A 276 3.156 -70.472 533.541 1.00 61.76 C ANISOU 2998 CB PRO A 276 11585 8315 3567 1268 741 -1051 C ATOM 2999 CG PRO A 276 4.159 -71.499 533.153 1.00 91.35 C ANISOU 2999 CG PRO A 276 15513 12102 7093 1679 952 -1326 C ATOM 3000 CD PRO A 276 5.157 -71.535 534.277 1.00 72.95 C ANISOU 3000 CD PRO A 276 12936 9741 5041 1914 1100 -1232 C ATOM 3001 N GLY A 277 2.111 -72.772 535.735 1.00 72.50 N ANISOU 3001 N GLY A 277 13445 8607 5492 1335 433 -1380 N ATOM 3002 CA GLY A 277 1.013 -73.651 536.095 1.00 69.10 C ANISOU 3002 CA GLY A 277 13331 7742 5181 1173 184 -1517 C ATOM 3003 C GLY A 277 0.262 -73.188 537.326 1.00 70.10 C ANISOU 3003 C GLY A 277 13268 7680 5686 909 31 -1287 C ATOM 3004 O GLY A 277 -0.940 -73.436 537.454 1.00 82.58 O ANISOU 3004 O GLY A 277 15007 9018 7353 639 -201 -1293 O ATOM 3005 N LEU A 278 0.953 -72.513 538.246 1.00 82.05 N ANISOU 3005 N LEU A 278 14440 9310 7424 984 156 -1081 N ATOM 3006 CA LEU A 278 0.309 -72.043 539.467 1.00 72.50 C ANISOU 3006 CA LEU A 278 13045 7943 6559 763 30 -872 C ATOM 3007 C LEU A 278 -0.578 -70.832 539.216 1.00 68.22 C ANISOU 3007 C LEU A 278 12298 7572 6049 433 -89 -656 C ATOM 3008 O LEU A 278 -1.547 -70.616 539.952 1.00 59.95 O ANISOU 3008 O LEU A 278 11197 6354 5228 193 -255 -545 O ATOM 3009 CB LEU A 278 1.367 -71.696 540.513 1.00 52.94 C ANISOU 3009 CB LEU A 278 10286 5534 4297 956 188 -729 C ATOM 3010 CG LEU A 278 2.319 -72.829 540.893 1.00 65.85 C ANISOU 3010 CG LEU A 278 12076 6997 5946 1298 303 -913 C ATOM 3011 CD1 LEU A 278 3.450 -72.304 541.763 1.00 67.35 C ANISOU 3011 CD1 LEU A 278 11945 7326 6320 1480 466 -739 C ATOM 3012 CD2 LEU A 278 1.561 -73.941 541.599 1.00 71.34 C ANISOU 3012 CD2 LEU A 278 13058 7251 6796 1225 118 -1040 C ATOM 3013 N ARG A 279 -0.270 -70.041 538.188 1.00 60.53 N ANISOU 3013 N ARG A 279 11207 6939 4852 417 -11 -591 N ATOM 3014 CA ARG A 279 -0.961 -68.771 537.974 1.00 61.82 C ANISOU 3014 CA ARG A 279 11138 7284 5066 126 -123 -358 C ATOM 3015 C ARG A 279 -2.479 -68.892 537.999 1.00 57.14 C ANISOU 3015 C ARG A 279 10683 6466 4559 -187 -379 -363 C ATOM 3016 O ARG A 279 -3.120 -68.127 538.736 1.00 59.92 O ANISOU 3016 O ARG A 279 10818 6788 5161 -383 -488 -171 O ATOM 3017 CB ARG A 279 -0.488 -68.166 536.644 1.00 65.47 C ANISOU 3017 CB ARG A 279 11547 8119 5211 145 -28 -329 C ATOM 3018 CG ARG A 279 0.992 -67.813 536.631 1.00 73.08 C ANISOU 3018 CG ARG A 279 12287 9372 6107 416 225 -254 C ATOM 3019 CD ARG A 279 1.427 -67.227 535.299 1.00 64.42 C ANISOU 3019 CD ARG A 279 11130 8671 4676 414 321 -206 C ATOM 3020 NE ARG A 279 2.870 -67.009 535.260 1.00 68.88 N ANISOU 3020 NE ARG A 279 11482 9526 5161 686 575 -138 N ATOM 3021 CZ ARG A 279 3.522 -66.471 534.234 1.00 62.55 C ANISOU 3021 CZ ARG A 279 10562 9126 4077 727 709 -58 C ATOM 3022 NH1 ARG A 279 2.863 -66.086 533.149 1.00 79.59 N ANISOU 3022 NH1 ARG A 279 12809 11436 5994 512 608 -41 N ATOM 3023 NH2 ARG A 279 4.837 -66.316 534.294 1.00 80.50 N ANISOU 3023 NH2 ARG A 279 12618 11662 6305 976 941 20 N ATOM 3024 N PRO A 280 -3.112 -69.803 537.255 1.00 59.94 N ANISOU 3024 N PRO A 280 11385 6662 4728 -247 -492 -570 N ATOM 3025 CA PRO A 280 -4.581 -69.885 537.331 1.00 62.43 C ANISOU 3025 CA PRO A 280 11798 6770 5151 -567 -751 -540 C ATOM 3026 C PRO A 280 -5.085 -70.173 538.733 1.00 47.95 C ANISOU 3026 C PRO A 280 9899 4665 3656 -638 -831 -472 C ATOM 3027 O PRO A 280 -6.108 -69.614 539.149 1.00 45.97 O ANISOU 3027 O PRO A 280 9503 4373 3590 -896 -985 -317 O ATOM 3028 CB PRO A 280 -4.918 -71.017 536.350 1.00 83.89 C ANISOU 3028 CB PRO A 280 14941 9334 7599 -557 -844 -804 C ATOM 3029 CG PRO A 280 -3.665 -71.818 536.239 1.00 86.60 C ANISOU 3029 CG PRO A 280 15434 9680 7791 -187 -637 -1006 C ATOM 3030 CD PRO A 280 -2.547 -70.832 536.366 1.00 81.38 C ANISOU 3030 CD PRO A 280 14424 9360 7137 -22 -405 -843 C ATOM 3031 N LEU A 281 -4.384 -71.027 539.483 1.00 60.70 N ANISOU 3031 N LEU A 281 11608 6103 5352 -409 -729 -579 N ATOM 3032 CA LEU A 281 -4.781 -71.299 540.861 1.00 57.58 C ANISOU 3032 CA LEU A 281 11145 5470 5262 -472 -793 -499 C ATOM 3033 C LEU A 281 -4.703 -70.038 541.711 1.00 55.90 C ANISOU 3033 C LEU A 281 10534 5430 5275 -533 -741 -246 C ATOM 3034 O LEU A 281 -5.614 -69.749 542.496 1.00 52.92 O ANISOU 3034 O LEU A 281 10038 4957 5113 -735 -863 -121 O ATOM 3035 CB LEU A 281 -3.897 -72.399 541.449 1.00 44.58 C ANISOU 3035 CB LEU A 281 9669 3622 3649 -196 -690 -651 C ATOM 3036 CG LEU A 281 -3.918 -72.565 542.970 1.00 58.80 C ANISOU 3036 CG LEU A 281 11349 5239 5752 -198 -698 -542 C ATOM 3037 CD1 LEU A 281 -5.335 -72.751 543.486 1.00 62.45 C ANISOU 3037 CD1 LEU A 281 11850 5504 6373 -514 -915 -464 C ATOM 3038 CD2 LEU A 281 -3.045 -73.743 543.372 1.00 83.20 C ANISOU 3038 CD2 LEU A 281 14650 8113 8849 76 -623 -709 C ATOM 3039 N VAL A 282 -3.622 -69.273 541.565 1.00 59.17 N ANISOU 3039 N VAL A 282 10738 6104 5640 -357 -567 -167 N ATOM 3040 CA VAL A 282 -3.476 -68.043 542.333 1.00 40.22 C ANISOU 3040 CA VAL A 282 7979 3857 3448 -405 -539 68 C ATOM 3041 C VAL A 282 -4.524 -67.020 541.909 1.00 45.97 C ANISOU 3041 C VAL A 282 8560 4705 4201 -686 -696 211 C ATOM 3042 O VAL A 282 -5.094 -66.315 542.751 1.00 52.45 O ANISOU 3042 O VAL A 282 9170 5506 5252 -816 -775 363 O ATOM 3043 CB VAL A 282 -2.048 -67.492 542.180 1.00 36.77 C ANISOU 3043 CB VAL A 282 7359 3671 2941 -167 -338 133 C ATOM 3044 CG1 VAL A 282 -1.903 -66.173 542.917 1.00 45.95 C ANISOU 3044 CG1 VAL A 282 8168 4977 4314 -230 -344 380 C ATOM 3045 CG2 VAL A 282 -1.037 -68.504 542.695 1.00 48.43 C ANISOU 3045 CG2 VAL A 282 8957 5016 4427 121 -192 0 C ATOM 3046 N TRP A 283 -4.797 -66.922 540.604 1.00 54.00 N ANISOU 3046 N TRP A 283 9688 5849 4981 -777 -749 159 N ATOM 3047 CA TRP A 283 -5.769 -65.947 540.118 1.00 48.97 C ANISOU 3047 CA TRP A 283 8915 5328 4365 -1043 -914 300 C ATOM 3048 C TRP A 283 -7.095 -66.080 540.853 1.00 40.30 C ANISOU 3048 C TRP A 283 7807 4016 3488 -1261 -1094 340 C ATOM 3049 O TRP A 283 -7.641 -65.098 541.369 1.00 46.06 O ANISOU 3049 O TRP A 283 8281 4805 4415 -1391 -1176 511 O ATOM 3050 CB TRP A 283 -6.002 -66.129 538.617 1.00 55.40 C ANISOU 3050 CB TRP A 283 9929 6248 4871 -1126 -972 204 C ATOM 3051 CG TRP A 283 -4.839 -65.802 537.746 1.00 62.11 C ANISOU 3051 CG TRP A 283 10746 7380 5471 -953 -803 200 C ATOM 3052 CD1 TRP A 283 -3.684 -65.172 538.108 1.00 69.07 C ANISOU 3052 CD1 TRP A 283 11390 8453 6399 -773 -632 318 C ATOM 3053 CD2 TRP A 283 -4.717 -66.094 536.351 1.00 48.31 C ANISOU 3053 CD2 TRP A 283 9206 5772 3375 -952 -791 81 C ATOM 3054 NE1 TRP A 283 -2.850 -65.053 537.020 1.00 68.48 N ANISOU 3054 NE1 TRP A 283 11342 8648 6030 -662 -503 292 N ATOM 3055 CE2 TRP A 283 -3.463 -65.613 535.930 1.00 56.69 C ANISOU 3055 CE2 TRP A 283 10125 7133 4279 -762 -591 139 C ATOM 3056 CE3 TRP A 283 -5.550 -66.718 535.417 1.00 57.64 C ANISOU 3056 CE3 TRP A 283 10684 6862 4356 -1097 -937 -65 C ATOM 3057 CZ2 TRP A 283 -3.021 -65.734 534.613 1.00 70.80 C ANISOU 3057 CZ2 TRP A 283 12049 9151 5700 -704 -512 52 C ATOM 3058 CZ3 TRP A 283 -5.110 -66.838 534.112 1.00 70.74 C ANISOU 3058 CZ3 TRP A 283 12501 8727 5650 -1038 -873 -165 C ATOM 3059 CH2 TRP A 283 -3.858 -66.349 533.722 1.00 62.52 C ANISOU 3059 CH2 TRP A 283 11306 8004 4443 -839 -652 -108 C ATOM 3060 N ARG A 284 -7.633 -67.297 540.898 1.00 46.75 N ANISOU 3060 N ARG A 284 8901 4587 4275 -1303 -1166 185 N ATOM 3061 CA ARG A 284 -8.933 -67.522 541.515 1.00 52.93 C ANISOU 3061 CA ARG A 284 9680 5185 5247 -1531 -1340 233 C ATOM 3062 C ARG A 284 -8.826 -67.669 543.027 1.00 48.62 C ANISOU 3062 C ARG A 284 9006 4512 4955 -1460 -1278 294 C ATOM 3063 O ARG A 284 -9.731 -67.238 543.750 1.00 56.01 O ANISOU 3063 O ARG A 284 9761 5427 6092 -1618 -1370 418 O ATOM 3064 CB ARG A 284 -9.580 -68.765 540.893 1.00 59.27 C ANISOU 3064 CB ARG A 284 10840 5772 5907 -1637 -1475 64 C ATOM 3065 CG ARG A 284 -10.858 -69.262 541.575 1.00 86.12 C ANISOU 3065 CG ARG A 284 14185 9030 9507 -1804 -1609 141 C ATOM 3066 CD ARG A 284 -10.956 -70.785 541.532 1.00107.24 C ANISOU 3066 CD ARG A 284 17126 11500 12119 -1731 -1631 3 C ATOM 3067 NE ARG A 284 -9.764 -71.429 542.084 1.00106.13 N ANISOU 3067 NE ARG A 284 17144 11218 11962 -1499 -1496 -130 N ATOM 3068 CZ ARG A 284 -9.619 -72.742 542.239 1.00109.48 C ANISOU 3068 CZ ARG A 284 17768 11463 12367 -1385 -1500 -245 C ATOM 3069 NH1 ARG A 284 -10.595 -73.573 541.892 1.00121.60 N ANISOU 3069 NH1 ARG A 284 19390 12921 13892 -1505 -1643 -244 N ATOM 3070 NH2 ARG A 284 -8.494 -73.226 542.746 1.00 92.11 N ANISOU 3070 NH2 ARG A 284 15670 9159 10168 -1147 -1368 -350 N ATOM 3071 N GLY A 285 -7.736 -68.260 543.523 1.00 45.93 N ANISOU 3071 N GLY A 285 8744 4104 4604 -1215 -1120 212 N ATOM 3072 CA GLY A 285 -7.645 -68.580 544.936 1.00 46.98 C ANISOU 3072 CA GLY A 285 8808 4089 4954 -1157 -1076 257 C ATOM 3073 C GLY A 285 -7.197 -67.443 545.826 1.00 36.62 C ANISOU 3073 C GLY A 285 7168 2931 3817 -1084 -988 424 C ATOM 3074 O GLY A 285 -7.438 -67.491 547.036 1.00 40.34 O ANISOU 3074 O GLY A 285 7462 3390 4475 -1061 -966 467 O ATOM 3075 N LEU A 286 -6.558 -66.420 545.265 1.00 40.06 N ANISOU 3075 N LEU A 286 7433 3601 4185 -1012 -924 497 N ATOM 3076 CA LEU A 286 -5.972 -65.367 546.087 1.00 36.38 C ANISOU 3076 CA LEU A 286 6682 3262 3880 -922 -853 650 C ATOM 3077 C LEU A 286 -7.030 -64.396 546.607 1.00 32.06 C ANISOU 3077 C LEU A 286 5869 2793 3519 -1087 -970 764 C ATOM 3078 O LEU A 286 -6.960 -63.985 547.772 1.00 37.83 O ANISOU 3078 O LEU A 286 6337 3600 4435 -982 -907 777 O ATOM 3079 CB LEU A 286 -4.898 -64.609 545.302 1.00 27.91 C ANISOU 3079 CB LEU A 286 5499 2427 2677 -794 -757 702 C ATOM 3080 CG LEU A 286 -4.062 -63.618 546.117 1.00 33.80 C ANISOU 3080 CG LEU A 286 5976 3288 3577 -676 -688 859 C ATOM 3081 CD1 LEU A 286 -3.195 -64.339 547.143 1.00 39.01 C ANISOU 3081 CD1 LEU A 286 6684 3817 4321 -473 -561 814 C ATOM 3082 CD2 LEU A 286 -3.201 -62.761 545.202 1.00 32.17 C ANISOU 3082 CD2 LEU A 286 5639 3342 3240 -617 -636 952 C ATOM 3083 N PRO A 287 -8.011 -63.990 545.794 1.00 35.00 N ANISOU 3083 N PRO A 287 6215 3238 3846 -1277 -1109 783 N ATOM 3084 CA PRO A 287 -9.032 -63.063 546.313 1.00 34.57 C ANISOU 3084 CA PRO A 287 5822 3348 3965 -1323 -1184 821 C ATOM 3085 C PRO A 287 -9.844 -63.637 547.461 1.00 46.54 C ANISOU 3085 C PRO A 287 7246 4830 5605 -1285 -1157 763 C ATOM 3086 O PRO A 287 -10.363 -62.871 548.284 1.00 44.02 O ANISOU 3086 O PRO A 287 6668 4632 5426 -1235 -1152 796 O ATOM 3087 CB PRO A 287 -9.914 -62.778 545.087 1.00 39.41 C ANISOU 3087 CB PRO A 287 6487 4018 4469 -1521 -1345 849 C ATOM 3088 CG PRO A 287 -9.111 -63.200 543.903 1.00 32.12 C ANISOU 3088 CG PRO A 287 5888 3009 3309 -1586 -1338 857 C ATOM 3089 CD PRO A 287 -8.235 -64.315 544.375 1.00 42.17 C ANISOU 3089 CD PRO A 287 7354 4142 4527 -1399 -1186 735 C ATOM 3090 N PHE A 288 -9.976 -64.963 547.540 1.00 39.65 N ANISOU 3090 N PHE A 288 6597 3797 4670 -1306 -1143 680 N ATOM 3091 CA PHE A 288 -10.768 -65.565 548.608 1.00 30.28 C ANISOU 3091 CA PHE A 288 5318 2599 3589 -1291 -1119 657 C ATOM 3092 C PHE A 288 -10.039 -65.494 549.945 1.00 31.61 C ANISOU 3092 C PHE A 288 5355 2776 3878 -1125 -978 656 C ATOM 3093 O PHE A 288 -10.658 -65.223 550.981 1.00 37.56 O ANISOU 3093 O PHE A 288 5917 3610 4745 -1101 -947 679 O ATOM 3094 CB PHE A 288 -11.109 -67.011 548.245 1.00 47.67 C ANISOU 3094 CB PHE A 288 7790 4632 5690 -1369 -1170 582 C ATOM 3095 CG PHE A 288 -11.697 -67.808 549.379 1.00 78.55 C ANISOU 3095 CG PHE A 288 11636 8513 9699 -1355 -1137 575 C ATOM 3096 CD1 PHE A 288 -12.878 -67.412 549.988 1.00 82.03 C ANISOU 3096 CD1 PHE A 288 11854 9075 10239 -1413 -1164 641 C ATOM 3097 CD2 PHE A 288 -11.075 -68.965 549.824 1.00 80.36 C ANISOU 3097 CD2 PHE A 288 12038 8585 9910 -1285 -1086 510 C ATOM 3098 CE1 PHE A 288 -13.420 -68.149 551.028 1.00 76.46 C ANISOU 3098 CE1 PHE A 288 11106 8342 9605 -1423 -1135 650 C ATOM 3099 CE2 PHE A 288 -11.613 -69.705 550.863 1.00 79.84 C ANISOU 3099 CE2 PHE A 288 11912 8496 9928 -1297 -1070 523 C ATOM 3100 CZ PHE A 288 -12.786 -69.297 551.464 1.00 80.94 C ANISOU 3100 CZ PHE A 288 11837 8763 10156 -1375 -1092 597 C ATOM 3101 N VAL A 289 -8.724 -65.729 549.944 1.00 26.66 N ANISOU 3101 N VAL A 289 4844 2067 3219 -1005 -889 635 N ATOM 3102 CA VAL A 289 -7.967 -65.657 551.191 1.00 34.36 C ANISOU 3102 CA VAL A 289 5689 3060 4307 -844 -758 643 C ATOM 3103 C VAL A 289 -7.856 -64.217 551.677 1.00 36.51 C ANISOU 3103 C VAL A 289 5688 3505 4679 -783 -729 706 C ATOM 3104 O VAL A 289 -7.701 -63.972 552.880 1.00 44.27 O ANISOU 3104 O VAL A 289 6527 4536 5756 -688 -646 706 O ATOM 3105 CB VAL A 289 -6.576 -66.299 551.021 1.00 34.01 C ANISOU 3105 CB VAL A 289 5835 2885 4201 -709 -676 614 C ATOM 3106 CG1 VAL A 289 -6.708 -67.794 550.788 1.00 26.48 C ANISOU 3106 CG1 VAL A 289 5165 1738 3160 -735 -708 517 C ATOM 3107 CG2 VAL A 289 -5.808 -65.644 549.880 1.00 36.24 C ANISOU 3107 CG2 VAL A 289 6207 3189 4374 -688 -686 664 C ATOM 3108 N THR A 290 -7.916 -63.244 550.763 1.00 39.17 N ANISOU 3108 N THR A 290 5966 3935 4983 -838 -808 756 N ATOM 3109 CA THR A 290 -7.863 -61.845 551.176 1.00 29.37 C ANISOU 3109 CA THR A 290 4477 2848 3834 -783 -815 800 C ATOM 3110 C THR A 290 -9.140 -61.439 551.901 1.00 30.23 C ANISOU 3110 C THR A 290 4437 3031 4020 -826 -872 791 C ATOM 3111 O THR A 290 -9.087 -60.737 552.919 1.00 44.60 O ANISOU 3111 O THR A 290 6103 4919 5922 -740 -838 789 O ATOM 3112 CB THR A 290 -7.632 -60.940 549.965 1.00 28.94 C ANISOU 3112 CB THR A 290 4389 2878 3727 -845 -907 866 C ATOM 3113 OG1 THR A 290 -6.517 -61.421 549.203 1.00 25.65 O ANISOU 3113 OG1 THR A 290 4150 2397 3199 -809 -849 898 O ATOM 3114 CG2 THR A 290 -7.347 -59.515 550.417 1.00 35.54 C ANISOU 3114 CG2 THR A 290 4982 3854 4667 -773 -924 899 C ATOM 3115 N SER A 291 -10.298 -61.863 551.388 1.00 31.02 N ANISOU 3115 N SER A 291 4591 3115 4080 -956 -964 793 N ATOM 3116 CA SER A 291 -11.549 -61.613 552.094 1.00 25.03 C ANISOU 3116 CA SER A 291 3704 2417 3388 -984 -1003 808 C ATOM 3117 C SER A 291 -11.543 -62.274 553.462 1.00 32.79 C ANISOU 3117 C SER A 291 4685 3354 4421 -924 -890 774 C ATOM 3118 O SER A 291 -12.163 -61.767 554.404 1.00 42.13 O ANISOU 3118 O SER A 291 5734 4601 5673 -898 -887 793 O ATOM 3119 CB SER A 291 -12.733 -62.119 551.268 1.00 34.59 C ANISOU 3119 CB SER A 291 4988 3613 4543 -1133 -1106 827 C ATOM 3120 OG SER A 291 -12.793 -61.474 550.007 1.00 31.63 O ANISOU 3120 OG SER A 291 4621 3289 4110 -1197 -1217 869 O ATOM 3121 N LEU A 292 -10.849 -63.405 553.589 1.00 33.47 N ANISOU 3121 N LEU A 292 4925 3322 4468 -902 -808 733 N ATOM 3122 CA LEU A 292 -10.709 -64.044 554.892 1.00 32.53 C ANISOU 3122 CA LEU A 292 4807 3160 4393 -841 -705 713 C ATOM 3123 C LEU A 292 -9.993 -63.127 555.873 1.00 23.66 C ANISOU 3123 C LEU A 292 3556 2108 3325 -712 -638 718 C ATOM 3124 O LEU A 292 -10.467 -62.903 556.993 1.00 40.17 O ANISOU 3124 O LEU A 292 5562 4239 5463 -706 -635 735 O ATOM 3125 CB LEU A 292 -9.953 -65.361 554.738 1.00 22.92 C ANISOU 3125 CB LEU A 292 3781 1797 3129 -823 -654 675 C ATOM 3126 CG LEU A 292 -9.735 -66.157 556.019 1.00 30.93 C ANISOU 3126 CG LEU A 292 4806 2758 4188 -768 -562 665 C ATOM 3127 CD1 LEU A 292 -11.059 -66.429 556.708 1.00 30.86 C ANISOU 3127 CD1 LEU A 292 4744 2779 4203 -877 -605 696 C ATOM 3128 CD2 LEU A 292 -9.014 -67.451 555.701 1.00 42.63 C ANISOU 3128 CD2 LEU A 292 6484 4084 5628 -750 -552 629 C ATOM 3129 N ALA A 293 -8.852 -62.573 555.461 1.00 23.43 N ANISOU 3129 N ALA A 293 3520 2096 3287 -624 -609 716 N ATOM 3130 CA ALA A 293 -8.098 -61.691 556.344 1.00 26.34 C ANISOU 3130 CA ALA A 293 3776 2529 3702 -523 -591 725 C ATOM 3131 C ALA A 293 -8.958 -60.529 556.826 1.00 30.83 C ANISOU 3131 C ALA A 293 4173 3206 4335 -546 -689 748 C ATOM 3132 O ALA A 293 -8.899 -60.151 558.002 1.00 28.89 O ANISOU 3132 O ALA A 293 3850 2989 4137 -496 -677 748 O ATOM 3133 CB ALA A 293 -6.851 -61.175 555.626 1.00 39.86 C ANISOU 3133 CB ALA A 293 5489 4261 5396 -449 -567 737 C ATOM 3134 N PHE A 294 -9.771 -59.954 555.936 1.00 31.67 N ANISOU 3134 N PHE A 294 4221 3366 4445 -617 -790 773 N ATOM 3135 CA PHE A 294 -10.648 -58.863 556.346 1.00 36.00 C ANISOU 3135 CA PHE A 294 4605 4005 5070 -620 -890 806 C ATOM 3136 C PHE A 294 -11.591 -59.310 557.456 1.00 28.27 C ANISOU 3136 C PHE A 294 3614 3010 4119 -640 -851 816 C ATOM 3137 O PHE A 294 -11.764 -58.612 558.460 1.00 46.29 O ANISOU 3137 O PHE A 294 5789 5332 6467 -586 -859 826 O ATOM 3138 CB PHE A 294 -11.444 -58.344 555.147 1.00 29.95 C ANISOU 3138 CB PHE A 294 3802 3285 4294 -689 -1009 849 C ATOM 3139 CG PHE A 294 -10.746 -57.260 554.375 1.00 33.98 C ANISOU 3139 CG PHE A 294 4229 3860 4820 -667 -1096 868 C ATOM 3140 CD1 PHE A 294 -10.640 -55.979 554.896 1.00 36.77 C ANISOU 3140 CD1 PHE A 294 4474 4256 5240 -581 -1044 831 C ATOM 3141 CD2 PHE A 294 -10.208 -57.516 553.125 1.00 26.92 C ANISOU 3141 CD2 PHE A 294 3424 2951 3852 -722 -1109 878 C ATOM 3142 CE1 PHE A 294 -10.001 -54.973 554.188 1.00 38.17 C ANISOU 3142 CE1 PHE A 294 4625 4465 5413 -561 -1011 804 C ATOM 3143 CE2 PHE A 294 -9.567 -56.517 552.410 1.00 27.99 C ANISOU 3143 CE2 PHE A 294 3487 3144 4002 -716 -1144 893 C ATOM 3144 CZ PHE A 294 -9.464 -55.242 552.943 1.00 24.12 C ANISOU 3144 CZ PHE A 294 2895 2693 3577 -622 -1054 839 C ATOM 3145 N PHE A 295 -12.196 -60.489 557.301 1.00 26.66 N ANISOU 3145 N PHE A 295 3518 2743 3867 -727 -809 812 N ATOM 3146 CA PHE A 295 -13.176 -60.946 558.279 1.00 22.63 C ANISOU 3146 CA PHE A 295 2985 2230 3383 -776 -774 835 C ATOM 3147 C PHE A 295 -12.550 -61.177 559.648 1.00 30.30 C ANISOU 3147 C PHE A 295 3970 3177 4366 -705 -683 822 C ATOM 3148 O PHE A 295 -13.279 -61.273 560.641 1.00 36.20 O ANISOU 3148 O PHE A 295 4671 3942 5142 -735 -653 854 O ATOM 3149 CB PHE A 295 -13.860 -62.223 557.777 1.00 43.96 C ANISOU 3149 CB PHE A 295 5798 4868 6036 -903 -771 838 C ATOM 3150 CG PHE A 295 -14.633 -62.040 556.485 1.00 58.16 C ANISOU 3150 CG PHE A 295 7590 6694 7816 -996 -883 865 C ATOM 3151 CD1 PHE A 295 -14.907 -60.772 555.983 1.00 45.57 C ANISOU 3151 CD1 PHE A 295 5875 5181 6259 -965 -976 904 C ATOM 3152 CD2 PHE A 295 -15.091 -63.143 555.778 1.00 50.94 C ANISOU 3152 CD2 PHE A 295 6796 5714 6845 -1113 -911 860 C ATOM 3153 CE1 PHE A 295 -15.615 -60.610 554.803 1.00 33.15 C ANISOU 3153 CE1 PHE A 295 4305 3628 4660 -1046 -1076 939 C ATOM 3154 CE2 PHE A 295 -15.802 -62.987 554.596 1.00 43.58 C ANISOU 3154 CE2 PHE A 295 5871 4805 5883 -1204 -1020 888 C ATOM 3155 CZ PHE A 295 -16.064 -61.719 554.110 1.00 45.30 C ANISOU 3155 CZ PHE A 295 5969 5110 6133 -1169 -1095 929 C ATOM 3156 N ASN A 296 -11.220 -61.255 559.728 1.00 35.72 N ANISOU 3156 N ASN A 296 4716 3826 5029 -618 -639 786 N ATOM 3157 CA ASN A 296 -10.567 -61.327 561.031 1.00 28.65 C ANISOU 3157 CA ASN A 296 3827 2916 4142 -543 -569 778 C ATOM 3158 C ASN A 296 -10.904 -60.106 561.876 1.00 37.32 C ANISOU 3158 C ASN A 296 4780 4093 5306 -495 -604 796 C ATOM 3159 O ASN A 296 -11.090 -60.215 563.094 1.00 25.15 O ANISOU 3159 O ASN A 296 3236 2549 3772 -479 -551 811 O ATOM 3160 CB ASN A 296 -9.054 -61.451 560.854 1.00 30.34 C ANISOU 3160 CB ASN A 296 4106 3093 4329 -454 -527 745 C ATOM 3161 CG ASN A 296 -8.307 -61.419 562.176 1.00 30.66 C ANISOU 3161 CG ASN A 296 4146 3127 4377 -376 -472 739 C ATOM 3162 OD1 ASN A 296 -7.993 -60.349 562.697 1.00 38.88 O ANISOU 3162 OD1 ASN A 296 5082 4232 5460 -322 -506 735 O ATOM 3163 ND2 ASN A 296 -8.017 -62.594 562.722 1.00 25.75 N ANISOU 3163 ND2 ASN A 296 3641 2423 3721 -376 -398 741 N ATOM 3164 N SER A 297 -10.981 -58.930 561.247 1.00 29.20 N ANISOU 3164 N SER A 297 3636 3130 4330 -474 -698 797 N ATOM 3165 CA SER A 297 -11.353 -57.712 561.955 1.00 28.55 C ANISOU 3165 CA SER A 297 3414 3103 4331 -431 -745 807 C ATOM 3166 C SER A 297 -12.807 -57.718 562.401 1.00 31.75 C ANISOU 3166 C SER A 297 3737 3520 4807 -498 -796 899 C ATOM 3167 O SER A 297 -13.186 -56.886 563.233 1.00 26.26 O ANISOU 3167 O SER A 297 2918 2844 4217 -468 -840 942 O ATOM 3168 CB SER A 297 -11.089 -56.494 561.069 1.00 20.23 C ANISOU 3168 CB SER A 297 2244 2102 3342 -426 -860 793 C ATOM 3169 OG SER A 297 -9.706 -56.370 560.785 1.00 40.64 O ANISOU 3169 OG SER A 297 4856 4679 5907 -403 -846 754 O ATOM 3170 N VAL A 298 -13.622 -58.628 561.874 1.00 29.31 N ANISOU 3170 N VAL A 298 3486 3198 4454 -601 -783 931 N ATOM 3171 CA VAL A 298 -15.000 -58.756 562.330 1.00 38.72 C ANISOU 3171 CA VAL A 298 4593 4422 5697 -695 -797 1020 C ATOM 3172 C VAL A 298 -15.128 -59.800 563.436 1.00 26.27 C ANISOU 3172 C VAL A 298 3082 2829 4072 -755 -682 1037 C ATOM 3173 O VAL A 298 -16.051 -59.723 564.252 1.00 31.91 O ANISOU 3173 O VAL A 298 3687 3604 4835 -819 -664 1121 O ATOM 3174 CB VAL A 298 -15.922 -59.099 561.147 1.00 30.88 C ANISOU 3174 CB VAL A 298 3607 3446 4679 -801 -849 1038 C ATOM 3175 CG1 VAL A 298 -17.378 -59.070 561.582 1.00 42.47 C ANISOU 3175 CG1 VAL A 298 4947 4984 6206 -900 -852 1120 C ATOM 3176 CG2 VAL A 298 -15.687 -58.139 559.991 1.00 44.50 C ANISOU 3176 CG2 VAL A 298 5303 5181 6426 -739 -958 1033 C ATOM 3177 N ALA A 299 -14.224 -60.776 563.482 1.00 26.29 N ANISOU 3177 N ALA A 299 3251 2758 3982 -737 -598 968 N ATOM 3178 CA ALA A 299 -14.289 -61.821 564.495 1.00 25.99 C ANISOU 3178 CA ALA A 299 3291 2687 3895 -789 -504 991 C ATOM 3179 C ALA A 299 -13.606 -61.416 565.795 1.00 29.31 C ANISOU 3179 C ALA A 299 3709 3107 4319 -692 -451 999 C ATOM 3180 O ALA A 299 -14.095 -61.755 566.877 1.00 37.82 O ANISOU 3180 O ALA A 299 4766 4214 5389 -751 -403 1073 O ATOM 3181 CB ALA A 299 -13.661 -63.109 563.961 1.00 18.58 C ANISOU 3181 CB ALA A 299 2528 1650 2881 -803 -449 928 C ATOM 3182 N ASN A 300 -12.488 -60.693 565.714 1.00 33.62 N ANISOU 3182 N ASN A 300 4272 3635 4866 -554 -459 929 N ATOM 3183 CA ASN A 300 -11.779 -60.279 566.924 1.00 30.65 C ANISOU 3183 CA ASN A 300 3909 3254 4483 -456 -419 923 C ATOM 3184 C ASN A 300 -12.694 -59.595 567.930 1.00 36.89 C ANISOU 3184 C ASN A 300 4562 4100 5353 -480 -448 1039 C ATOM 3185 O ASN A 300 -12.646 -59.956 569.117 1.00 39.65 O ANISOU 3185 O ASN A 300 4955 4449 5661 -483 -382 1090 O ATOM 3186 CB ASN A 300 -10.609 -59.358 566.547 1.00 26.93 C ANISOU 3186 CB ASN A 300 3431 2792 4010 -328 -443 831 C ATOM 3187 CG ASN A 300 -9.370 -60.125 566.109 1.00 35.23 C ANISOU 3187 CG ASN A 300 4578 3791 5017 -307 -425 794 C ATOM 3188 OD1 ASN A 300 -9.199 -61.299 566.440 1.00 36.74 O ANISOU 3188 OD1 ASN A 300 4880 3920 5159 -337 -362 807 O ATOM 3189 ND2 ASN A 300 -8.493 -59.455 565.368 1.00 42.58 N ANISOU 3189 ND2 ASN A 300 5461 4745 5972 -261 -479 756 N ATOM 3190 N PRO A 301 -13.542 -58.636 567.546 1.00 32.33 N ANISOU 3190 N PRO A 301 3813 3576 4896 -496 -538 1103 N ATOM 3191 CA PRO A 301 -14.444 -58.030 568.541 1.00 33.72 C ANISOU 3191 CA PRO A 301 3829 3816 5168 -511 -533 1251 C ATOM 3192 C PRO A 301 -15.323 -59.043 569.252 1.00 35.38 C ANISOU 3192 C PRO A 301 4013 4128 5304 -673 -417 1351 C ATOM 3193 O PRO A 301 -15.583 -58.895 570.453 1.00 34.55 O ANISOU 3193 O PRO A 301 3842 4140 5146 -630 -331 1389 O ATOM 3194 CB PRO A 301 -15.269 -57.046 567.701 1.00 30.18 C ANISOU 3194 CB PRO A 301 3187 3409 4870 -521 -644 1276 C ATOM 3195 CG PRO A 301 -14.382 -56.701 566.557 1.00 49.36 C ANISOU 3195 CG PRO A 301 5700 5770 7284 -451 -734 1146 C ATOM 3196 CD PRO A 301 -13.624 -57.958 566.241 1.00 43.21 C ANISOU 3196 CD PRO A 301 5121 4962 6336 -485 -643 1057 C ATOM 3197 N VAL A 302 -15.792 -60.072 568.544 1.00 37.66 N ANISOU 3197 N VAL A 302 4362 4424 5523 -801 -406 1313 N ATOM 3198 CA VAL A 302 -16.609 -61.097 569.185 1.00 23.76 C ANISOU 3198 CA VAL A 302 2589 2760 3679 -953 -315 1386 C ATOM 3199 C VAL A 302 -15.764 -61.933 570.138 1.00 32.03 C ANISOU 3199 C VAL A 302 3819 3731 4619 -928 -241 1372 C ATOM 3200 O VAL A 302 -16.192 -62.249 571.254 1.00 28.14 O ANISOU 3200 O VAL A 302 3280 3349 4063 -996 -156 1470 O ATOM 3201 CB VAL A 302 -17.296 -61.972 568.122 1.00 37.71 C ANISOU 3201 CB VAL A 302 4396 4510 5421 -1079 -354 1351 C ATOM 3202 CG1 VAL A 302 -17.993 -63.143 568.778 1.00 33.18 C ANISOU 3202 CG1 VAL A 302 3840 3999 4768 -1228 -285 1422 C ATOM 3203 CG2 VAL A 302 -18.287 -61.149 567.306 1.00 36.55 C ANISOU 3203 CG2 VAL A 302 4057 4462 5368 -1110 -426 1372 C ATOM 3204 N LEU A 303 -14.553 -62.305 569.717 1.00 38.98 N ANISOU 3204 N LEU A 303 4890 4452 5468 -827 -259 1249 N ATOM 3205 CA LEU A 303 -13.677 -63.088 570.583 1.00 33.06 C ANISOU 3205 CA LEU A 303 4302 3625 4635 -786 -191 1222 C ATOM 3206 C LEU A 303 -13.369 -62.340 571.873 1.00 28.05 C ANISOU 3206 C LEU A 303 3634 3040 3984 -707 -162 1287 C ATOM 3207 O LEU A 303 -13.285 -62.949 572.947 1.00 29.22 O ANISOU 3207 O LEU A 303 3847 3204 4051 -743 -96 1341 O ATOM 3208 CB LEU A 303 -12.385 -63.435 569.843 1.00 32.09 C ANISOU 3208 CB LEU A 303 4328 3370 4495 -668 -191 1081 C ATOM 3209 CG LEU A 303 -12.565 -64.267 568.571 1.00 39.82 C ANISOU 3209 CG LEU A 303 5358 4295 5478 -729 -208 1033 C ATOM 3210 CD1 LEU A 303 -11.262 -64.359 567.790 1.00 36.49 C ANISOU 3210 CD1 LEU A 303 5018 3794 5051 -616 -221 943 C ATOM 3211 CD2 LEU A 303 -13.083 -65.657 568.916 1.00 31.36 C ANISOU 3211 CD2 LEU A 303 4351 3189 4376 -857 -178 1089 C ATOM 3212 N TYR A 304 -13.196 -61.018 571.788 1.00 30.13 N ANISOU 3212 N TYR A 304 3800 3324 4326 -589 -219 1289 N ATOM 3213 CA TYR A 304 -12.944 -60.224 572.986 1.00 29.63 C ANISOU 3213 CA TYR A 304 3707 3301 4251 -481 -203 1365 C ATOM 3214 C TYR A 304 -14.029 -60.458 574.031 1.00 41.26 C ANISOU 3214 C TYR A 304 5057 4980 5640 -588 -91 1518 C ATOM 3215 O TYR A 304 -13.738 -60.695 575.209 1.00 42.91 O ANISOU 3215 O TYR A 304 5338 5237 5730 -558 -25 1549 O ATOM 3216 CB TYR A 304 -12.873 -58.735 572.629 1.00 27.69 C ANISOU 3216 CB TYR A 304 3348 3045 4130 -319 -304 1353 C ATOM 3217 CG TYR A 304 -11.808 -58.344 571.626 1.00 22.11 C ANISOU 3217 CG TYR A 304 2718 2237 3446 -224 -381 1148 C ATOM 3218 CD1 TYR A 304 -10.715 -59.161 571.374 1.00 23.77 C ANISOU 3218 CD1 TYR A 304 3092 2383 3556 -221 -330 1023 C ATOM 3219 CD2 TYR A 304 -11.899 -57.143 570.935 1.00 31.54 C ANISOU 3219 CD2 TYR A 304 3801 3440 4742 -137 -480 1089 C ATOM 3220 CE1 TYR A 304 -9.743 -58.791 570.455 1.00 44.33 C ANISOU 3220 CE1 TYR A 304 5726 4971 6145 -150 -349 885 C ATOM 3221 CE2 TYR A 304 -10.937 -56.766 570.017 1.00 31.09 C ANISOU 3221 CE2 TYR A 304 3795 3359 4657 -101 -504 927 C ATOM 3222 CZ TYR A 304 -9.860 -57.591 569.780 1.00 30.24 C ANISOU 3222 CZ TYR A 304 3828 3224 4438 -108 -431 845 C ATOM 3223 OH TYR A 304 -8.902 -57.214 568.865 1.00 31.46 O ANISOU 3223 OH TYR A 304 3967 3387 4600 -94 -466 764 O ATOM 3224 N VAL A 305 -15.291 -60.400 573.609 1.00 54.71 N ANISOU 3224 N VAL A 305 6562 6858 7366 -683 -59 1527 N ATOM 3225 CA VAL A 305 -16.408 -60.484 574.544 1.00 37.86 C ANISOU 3225 CA VAL A 305 4253 5012 5118 -729 70 1565 C ATOM 3226 C VAL A 305 -16.621 -61.912 575.030 1.00 34.80 C ANISOU 3226 C VAL A 305 3953 4639 4630 -976 144 1734 C ATOM 3227 O VAL A 305 -16.909 -62.140 576.210 1.00 37.74 O ANISOU 3227 O VAL A 305 4291 5192 4857 -993 255 1789 O ATOM 3228 CB VAL A 305 -17.673 -59.909 573.881 1.00 43.04 C ANISOU 3228 CB VAL A 305 4645 5854 5855 -743 68 1530 C ATOM 3229 CG1 VAL A 305 -18.924 -60.542 574.461 1.00 58.19 C ANISOU 3229 CG1 VAL A 305 6385 8049 7677 -913 199 1644 C ATOM 3230 CG2 VAL A 305 -17.709 -58.398 574.050 1.00 43.61 C ANISOU 3230 CG2 VAL A 305 4590 6010 5970 -462 33 1363 C ATOM 3231 N LEU A 306 -16.498 -62.894 574.135 1.00 40.35 N ANISOU 3231 N LEU A 306 4798 5153 5379 -1076 63 1671 N ATOM 3232 CA LEU A 306 -16.765 -64.278 574.516 1.00 34.43 C ANISOU 3232 CA LEU A 306 4152 4385 4545 -1215 92 1692 C ATOM 3233 C LEU A 306 -15.795 -64.759 575.588 1.00 40.92 C ANISOU 3233 C LEU A 306 5155 5117 5276 -1160 127 1692 C ATOM 3234 O LEU A 306 -16.181 -65.512 576.490 1.00 47.01 O ANISOU 3234 O LEU A 306 5933 5980 5949 -1264 188 1774 O ATOM 3235 CB LEU A 306 -16.686 -65.185 573.289 1.00 31.61 C ANISOU 3235 CB LEU A 306 3918 3838 4253 -1267 2 1601 C ATOM 3236 CG LEU A 306 -17.739 -64.950 572.205 1.00 47.89 C ANISOU 3236 CG LEU A 306 5832 5976 6389 -1350 -51 1606 C ATOM 3237 CD1 LEU A 306 -17.426 -65.784 570.971 1.00 37.54 C ANISOU 3237 CD1 LEU A 306 4678 4470 5116 -1364 -138 1508 C ATOM 3238 CD2 LEU A 306 -19.128 -65.269 572.731 1.00 47.93 C ANISOU 3238 CD2 LEU A 306 5652 6213 6347 -1513 6 1733 C ATOM 3239 N THR A 307 -14.535 -64.342 575.506 1.00 40.07 N ANISOU 3239 N THR A 307 5187 4835 5201 -995 82 1598 N ATOM 3240 CA THR A 307 -13.496 -64.875 576.381 1.00 38.92 C ANISOU 3240 CA THR A 307 5223 4573 4991 -928 99 1571 C ATOM 3241 C THR A 307 -13.148 -63.939 577.535 1.00 34.06 C ANISOU 3241 C THR A 307 4594 4055 4291 -827 134 1633 C ATOM 3242 O THR A 307 -12.123 -64.118 578.196 1.00 44.00 O ANISOU 3242 O THR A 307 6007 5200 5511 -736 125 1591 O ATOM 3243 CB THR A 307 -12.212 -65.163 575.592 1.00 37.05 C ANISOU 3243 CB THR A 307 5141 4109 4828 -792 46 1413 C ATOM 3244 OG1 THR A 307 -11.647 -63.928 575.138 1.00 51.68 O ANISOU 3244 OG1 THR A 307 6964 5938 6734 -643 -3 1338 O ATOM 3245 CG2 THR A 307 -12.511 -66.057 574.397 1.00 46.76 C ANISOU 3245 CG2 THR A 307 6385 5263 6117 -865 19 1362 C HETATM 3246 N YCM A 308 -13.993 -62.943 577.779 1.00 30.76 N ANISOU 3246 N YCM A 308 3975 3872 3840 -823 186 1738 N HETATM 3247 CA YCM A 308 -13.789 -62.055 578.899 1.00 44.21 C ANISOU 3247 CA YCM A 308 5651 5720 5426 -669 238 1754 C HETATM 3248 CB YCM A 308 -12.867 -60.894 578.523 1.00 28.55 C ANISOU 3248 CB YCM A 308 3719 3580 3550 -420 124 1601 C HETATM 3249 SG YCM A 308 -12.322 -59.889 579.872 1.00 40.87 S ANISOU 3249 SG YCM A 308 5332 5219 4977 -173 124 1495 S HETATM 3250 CD YCM A 308 -11.098 -60.855 580.706 1.00 57.54 C ANISOU 3250 CD YCM A 308 7714 7141 7008 -251 96 1625 C HETATM 3251 CE YCM A 308 -11.597 -61.522 581.967 1.00 51.80 C ANISOU 3251 CE YCM A 308 7000 6617 6065 -364 220 1725 C HETATM 3252 OZ1 YCM A 308 -12.739 -61.261 582.406 1.00 37.59 O ANISOU 3252 OZ1 YCM A 308 5020 5119 4145 -368 345 1699 O HETATM 3253 NZ2 YCM A 308 -10.778 -62.413 582.613 1.00 65.96 N ANISOU 3253 NZ2 YCM A 308 8995 8261 7806 -445 194 1791 N HETATM 3254 C YCM A 308 -15.083 -61.493 579.484 1.00 52.95 C ANISOU 3254 C YCM A 308 6510 7187 6420 -630 367 1714 C HETATM 3255 O YCM A 308 -15.655 -60.510 579.010 1.00 58.01 O ANISOU 3255 O YCM A 308 6973 7934 7132 -494 359 1589 O ATOM 3256 N PRO A 309 -15.570 -62.144 580.553 1.00 51.28 N ANISOU 3256 N PRO A 309 6277 7182 6024 -753 490 1830 N ATOM 3257 CA PRO A 309 -16.777 -61.720 581.274 1.00 51.08 C ANISOU 3257 CA PRO A 309 6009 7546 5854 -716 644 1810 C ATOM 3258 C PRO A 309 -16.791 -60.234 581.628 1.00 54.39 C ANISOU 3258 C PRO A 309 6337 8082 6246 -390 651 1588 C ATOM 3259 O PRO A 309 -17.811 -59.574 581.425 1.00 64.31 O ANISOU 3259 O PRO A 309 7349 9567 7520 -303 714 1506 O ATOM 3260 CB PRO A 309 -16.739 -62.579 582.538 1.00 63.90 C ANISOU 3260 CB PRO A 309 7720 9302 7258 -858 743 1964 C ATOM 3261 CG PRO A 309 -16.071 -63.833 582.101 1.00 40.90 C ANISOU 3261 CG PRO A 309 5028 6062 4450 -1059 626 2063 C ATOM 3262 CD PRO A 309 -15.046 -63.421 581.070 1.00 55.17 C ANISOU 3262 CD PRO A 309 6970 7544 6449 -944 479 1978 C ATOM 3263 N ASP A 310 -15.675 -59.716 582.147 1.00 44.01 N ANISOU 3263 N ASP A 310 5220 6602 4900 -210 571 1495 N ATOM 3264 CA ASP A 310 -15.605 -58.291 582.454 1.00 43.99 C ANISOU 3264 CA ASP A 310 5169 6659 4886 102 536 1278 C ATOM 3265 C ASP A 310 -15.919 -57.449 581.224 1.00 52.26 C ANISOU 3265 C ASP A 310 6076 7627 6152 204 434 1163 C ATOM 3266 O ASP A 310 -16.447 -56.338 581.349 1.00 52.13 O ANISOU 3266 O ASP A 310 5916 7753 6138 427 435 996 O ATOM 3267 CB ASP A 310 -14.220 -57.939 583.001 1.00 50.78 C ANISOU 3267 CB ASP A 310 6289 7284 5720 240 413 1223 C ATOM 3268 CG ASP A 310 -13.845 -58.761 584.223 1.00 71.99 C ANISOU 3268 CG ASP A 310 9131 10030 8191 135 490 1344 C ATOM 3269 OD1 ASP A 310 -14.721 -58.993 585.083 1.00 70.35 O ANISOU 3269 OD1 ASP A 310 8810 10141 7778 92 656 1379 O ATOM 3270 OD2 ASP A 310 -12.671 -59.180 584.323 1.00 94.20 O ANISOU 3270 OD2 ASP A 310 12171 12580 11039 92 383 1415 O ATOM 3271 N MET A 311 -15.603 -57.958 580.031 1.00 49.81 N ANISOU 3271 N MET A 311 5813 7090 6023 50 339 1245 N ATOM 3272 CA MET A 311 -15.892 -57.220 578.807 1.00 57.54 C ANISOU 3272 CA MET A 311 6667 7993 7202 118 234 1158 C ATOM 3273 C MET A 311 -17.387 -57.221 578.506 1.00 50.99 C ANISOU 3273 C MET A 311 5554 7438 6381 49 336 1170 C ATOM 3274 O MET A 311 -17.982 -56.165 578.259 1.00 55.80 O ANISOU 3274 O MET A 311 5988 8153 7061 228 306 1034 O ATOM 3275 CB MET A 311 -15.105 -57.828 577.645 1.00 58.92 C ANISOU 3275 CB MET A 311 6985 7867 7534 -30 116 1245 C ATOM 3276 CG MET A 311 -15.121 -57.006 576.364 1.00 63.80 C ANISOU 3276 CG MET A 311 7523 8370 8350 44 -21 1162 C ATOM 3277 SD MET A 311 -13.552 -56.185 576.012 1.00 46.29 S ANISOU 3277 SD MET A 311 5497 5848 6244 219 -213 1090 S ATOM 3278 CE MET A 311 -12.427 -57.578 575.996 1.00 58.00 C ANISOU 3278 CE MET A 311 7227 7111 7697 40 -201 1245 C ATOM 3279 N LEU A 312 -18.014 -58.400 578.532 1.00 49.19 N ANISOU 3279 N LEU A 312 5274 7325 6092 -214 443 1342 N ATOM 3280 CA LEU A 312 -19.445 -58.481 578.258 1.00 51.39 C ANISOU 3280 CA LEU A 312 5267 7876 6383 -308 535 1387 C ATOM 3281 C LEU A 312 -20.252 -57.774 579.336 1.00 48.16 C ANISOU 3281 C LEU A 312 4656 7822 5821 -119 683 1292 C ATOM 3282 O LEU A 312 -21.284 -57.159 579.045 1.00 49.50 O ANISOU 3282 O LEU A 312 4561 8198 6049 -34 717 1228 O ATOM 3283 CB LEU A 312 -19.877 -59.942 578.145 1.00 38.31 C ANISOU 3283 CB LEU A 312 3617 6254 4686 -650 597 1614 C ATOM 3284 CG LEU A 312 -21.342 -60.163 577.756 1.00 48.03 C ANISOU 3284 CG LEU A 312 4551 7750 5950 -802 669 1704 C ATOM 3285 CD1 LEU A 312 -21.471 -61.263 576.713 1.00 49.36 C ANISOU 3285 CD1 LEU A 312 4785 7737 6231 -1112 577 1868 C ATOM 3286 CD2 LEU A 312 -22.178 -60.493 578.981 1.00 60.62 C ANISOU 3286 CD2 LEU A 312 5975 9723 7335 -855 866 1800 C ATOM 3287 N ARG A 313 -19.799 -57.850 580.588 1.00 56.52 N ANISOU 3287 N ARG A 313 5836 8963 6678 -41 769 1280 N ATOM 3288 CA ARG A 313 -20.561 -57.265 581.686 1.00 62.59 C ANISOU 3288 CA ARG A 313 6428 10097 7258 141 930 1187 C ATOM 3289 C ARG A 313 -20.691 -55.757 581.516 1.00 55.23 C ANISOU 3289 C ARG A 313 5398 9172 6414 486 853 934 C ATOM 3290 O ARG A 313 -21.798 -55.209 581.560 1.00 68.76 O ANISOU 3290 O ARG A 313 6834 11168 8123 605 942 858 O ATOM 3291 CB ARG A 313 -19.893 -57.599 583.020 1.00 68.77 C ANISOU 3291 CB ARG A 313 7407 10925 7798 163 1007 1213 C ATOM 3292 CG ARG A 313 -20.810 -57.462 584.226 1.00 69.51 C ANISOU 3292 CG ARG A 313 7314 11463 7633 248 1226 1193 C ATOM 3293 CD ARG A 313 -20.022 -57.454 585.526 1.00 93.33 C ANISOU 3293 CD ARG A 313 10557 14496 10409 344 1265 1157 C ATOM 3294 NE ARG A 313 -18.770 -58.199 585.415 1.00 82.17 N ANISOU 3294 NE ARG A 313 9454 12723 9046 180 1130 1276 N ATOM 3295 CZ ARG A 313 -18.668 -59.523 585.498 1.00 83.42 C ANISOU 3295 CZ ARG A 313 9690 12846 9159 -136 1163 1520 C ATOM 3296 NH1 ARG A 313 -19.747 -60.270 585.691 1.00102.31 N ANISOU 3296 NH1 ARG A 313 11877 15543 11454 -351 1319 1691 N ATOM 3297 NH2 ARG A 313 -17.481 -60.102 585.385 1.00 82.41 N ANISOU 3297 NH2 ARG A 313 9843 12375 9094 -238 1028 1600 N ATOM 3298 N LYS A 314 -19.567 -55.067 581.315 1.00 57.83 N ANISOU 3298 N LYS A 314 5947 9191 6834 649 673 809 N ATOM 3299 CA LYS A 314 -19.599 -53.615 581.188 1.00 56.40 C ANISOU 3299 CA LYS A 314 5709 8976 6744 972 559 574 C ATOM 3300 C LYS A 314 -20.206 -53.162 579.868 1.00 60.15 C ANISOU 3300 C LYS A 314 5996 9393 7466 963 453 552 C ATOM 3301 O LYS A 314 -20.558 -51.984 579.739 1.00 70.69 O ANISOU 3301 O LYS A 314 7216 10757 8886 1220 372 370 O ATOM 3302 CB LYS A 314 -18.189 -53.047 581.348 1.00 45.99 C ANISOU 3302 CB LYS A 314 4683 7335 5458 1114 374 482 C ATOM 3303 CG LYS A 314 -17.547 -53.423 582.679 1.00 80.64 C ANISOU 3303 CG LYS A 314 9271 11767 9603 1133 454 498 C ATOM 3304 CD LYS A 314 -16.263 -52.651 582.946 1.00 82.27 C ANISOU 3304 CD LYS A 314 9735 11685 9838 1316 255 384 C ATOM 3305 CE LYS A 314 -15.526 -53.192 584.169 1.00100.78 C ANISOU 3305 CE LYS A 314 12301 14035 11955 1283 312 440 C ATOM 3306 NZ LYS A 314 -15.060 -54.599 583.984 1.00 71.02 N ANISOU 3306 NZ LYS A 314 8637 10164 8182 969 362 682 N ATOM 3307 N LEU A 315 -20.335 -54.061 578.891 1.00 64.94 N ANISOU 3307 N LEU A 315 6580 9906 8189 678 435 729 N ATOM 3308 CA LEU A 315 -21.094 -53.734 577.690 1.00 64.14 C ANISOU 3308 CA LEU A 315 6276 9802 8293 638 353 729 C ATOM 3309 C LEU A 315 -22.591 -53.733 577.975 1.00 65.02 C ANISOU 3309 C LEU A 315 6053 10299 8354 645 518 741 C ATOM 3310 O LEU A 315 -23.313 -52.837 577.524 1.00 78.06 O ANISOU 3310 O LEU A 315 7493 12033 10134 806 461 630 O ATOM 3311 CB LEU A 315 -20.756 -54.724 576.575 1.00 52.88 C ANISOU 3311 CB LEU A 315 4952 8156 6983 332 278 906 C ATOM 3312 CG LEU A 315 -21.461 -54.521 575.231 1.00 57.52 C ANISOU 3312 CG LEU A 315 5368 8712 7776 244 174 931 C ATOM 3313 CD1 LEU A 315 -20.947 -53.276 574.520 1.00 52.38 C ANISOU 3313 CD1 LEU A 315 4757 7851 7296 451 -34 782 C ATOM 3314 CD2 LEU A 315 -21.290 -55.751 574.355 1.00 40.96 C ANISOU 3314 CD2 LEU A 315 3376 6462 5726 -84 146 1116 C ATOM 3315 N ARG A 316 -23.074 -54.723 578.731 1.00 63.43 N ANISOU 3315 N ARG A 316 5788 10343 7968 470 716 887 N ATOM 3316 CA ARG A 316 -24.500 -54.787 579.038 1.00 68.07 C ANISOU 3316 CA ARG A 316 6031 11336 8496 458 888 930 C ATOM 3317 C ARG A 316 -24.930 -53.596 579.886 1.00 61.17 C ANISOU 3317 C ARG A 316 5009 10700 7531 836 964 701 C ATOM 3318 O ARG A 316 -25.934 -52.940 579.590 1.00 67.44 O ANISOU 3318 O ARG A 316 5515 11689 8422 973 980 623 O ATOM 3319 CB ARG A 316 -24.830 -56.101 579.752 1.00 68.19 C ANISOU 3319 CB ARG A 316 6027 11567 8315 178 1074 1156 C ATOM 3320 CG ARG A 316 -24.493 -57.354 578.953 1.00 67.91 C ANISOU 3320 CG ARG A 316 6142 11297 8366 -196 991 1380 C ATOM 3321 CD ARG A 316 -25.502 -58.472 579.195 1.00 78.69 C ANISOU 3321 CD ARG A 316 7314 12945 9639 -501 1136 1626 C ATOM 3322 NE ARG A 316 -25.610 -58.841 580.605 1.00 86.32 N ANISOU 3322 NE ARG A 316 8268 14194 10334 -500 1332 1686 N ATOM 3323 CZ ARG A 316 -26.456 -59.751 581.079 1.00 97.80 C ANISOU 3323 CZ ARG A 316 9682 15789 11689 -711 1398 1827 C ATOM 3324 NH1 ARG A 316 -27.278 -60.395 580.259 1.00 93.29 N ANISOU 3324 NH1 ARG A 316 9043 15148 11257 -936 1308 1940 N ATOM 3325 NH2 ARG A 316 -26.485 -60.019 582.378 1.00 91.44 N ANISOU 3325 NH2 ARG A 316 8909 15192 10643 -690 1542 1855 N ATOM 3326 N ARG A 317 -24.169 -53.290 580.939 1.00 69.38 N ANISOU 3326 N ARG A 317 6252 11718 8390 1018 997 583 N ATOM 3327 CA ARG A 317 -24.539 -52.189 581.825 1.00 73.12 C ANISOU 3327 CA ARG A 317 6622 12413 8747 1394 1066 345 C ATOM 3328 C ARG A 317 -24.712 -50.894 581.041 1.00 79.72 C ANISOU 3328 C ARG A 317 7368 13102 9820 1658 873 142 C ATOM 3329 O ARG A 317 -25.683 -50.154 581.246 1.00 86.20 O ANISOU 3329 O ARG A 317 7925 14182 10645 1895 941 3 O ATOM 3330 CB ARG A 317 -23.481 -52.019 582.917 1.00 64.00 C ANISOU 3330 CB ARG A 317 5770 11161 7387 1535 1063 243 C ATOM 3331 N SER A 318 -23.781 -50.605 580.130 1.00 81.35 N ANISOU 3331 N SER A 318 7783 12899 10227 1621 627 130 N ATOM 3332 CA SER A 318 -23.921 -49.425 579.284 1.00 72.87 C ANISOU 3332 CA SER A 318 6631 11661 9394 1826 413 -26 C ATOM 3333 C SER A 318 -25.053 -49.590 578.277 1.00 66.53 C ANISOU 3333 C SER A 318 5521 10988 8770 1689 420 76 C ATOM 3334 O SER A 318 -25.688 -48.601 577.894 1.00 81.61 O ANISOU 3334 O SER A 318 7366 12809 10832 1822 312 -62 O ATOM 3335 CB SER A 318 -22.603 -49.138 578.565 1.00 84.33 C ANISOU 3335 CB SER A 318 8378 12666 10997 1787 154 -28 C ATOM 3336 OG SER A 318 -22.101 -50.300 577.927 1.00 79.83 O ANISOU 3336 OG SER A 318 7930 11946 10455 1437 159 198 O ATOM 3337 N LEU A 319 -25.317 -50.824 577.836 1.00 70.00 N ANISOU 3337 N LEU A 319 5915 11479 9203 1331 512 318 N ATOM 3338 CA LEU A 319 -26.439 -51.062 576.934 1.00 81.89 C ANISOU 3338 CA LEU A 319 7165 13086 10862 1159 510 427 C ATOM 3339 C LEU A 319 -27.775 -50.861 577.637 1.00 85.21 C ANISOU 3339 C LEU A 319 7353 13831 11192 1250 690 372 C ATOM 3340 O LEU A 319 -28.782 -50.566 576.984 1.00 88.02 O ANISOU 3340 O LEU A 319 7541 14196 11705 1215 643 369 O ATOM 3341 CB LEU A 319 -26.383 -52.476 576.363 1.00 78.77 C ANISOU 3341 CB LEU A 319 6798 12664 10467 752 549 701 C ATOM 3342 CG LEU A 319 -27.281 -52.667 575.141 1.00 85.46 C ANISOU 3342 CG LEU A 319 7519 13444 11507 543 452 791 C ATOM 3343 CD1 LEU A 319 -26.484 -52.422 573.873 1.00 82.98 C ANISOU 3343 CD1 LEU A 319 7383 12758 11388 477 205 787 C ATOM 3344 CD2 LEU A 319 -27.922 -54.043 575.133 1.00 90.11 C ANISOU 3344 CD2 LEU A 319 8052 14174 12012 190 578 1029 C ATOM 3345 N ARG A 320 -27.812 -51.055 578.955 1.00 83.98 N ANISOU 3345 N ARG A 320 7186 13944 10777 1356 896 341 N ATOM 3346 CA ARG A 320 -29.043 -50.852 579.711 1.00 83.44 C ANISOU 3346 CA ARG A 320 6907 14199 10597 1456 1075 290 C ATOM 3347 C ARG A 320 -29.260 -49.378 580.023 1.00 85.45 C ANISOU 3347 C ARG A 320 7160 14405 10903 1844 999 2 C ATOM 3348 O ARG A 320 -30.381 -48.869 579.898 1.00 84.70 O ANISOU 3348 O ARG A 320 6863 14423 10896 1929 1023 -53 O ATOM 3349 CB ARG A 320 -29.001 -51.666 581.003 1.00 81.23 C ANISOU 3349 CB ARG A 320 6644 14218 10000 1389 1319 383 C ATOM 3350 CG ARG A 320 -29.363 -53.145 580.853 1.00104.69 C ANISOU 3350 CG ARG A 320 9561 17301 12916 970 1422 692 C ATOM 3351 CD ARG A 320 -28.997 -53.782 579.514 1.00 96.23 C ANISOU 3351 CD ARG A 320 8560 15941 12061 676 1250 860 C ATOM 3352 NE ARG A 320 -29.149 -55.228 579.633 1.00 94.62 N ANISOU 3352 NE ARG A 320 8397 15799 11756 295 1334 1131 N ATOM 3353 CZ ARG A 320 -28.720 -56.136 578.765 1.00 99.35 C ANISOU 3353 CZ ARG A 320 9134 16155 12461 -15 1217 1310 C ATOM 3354 NH1 ARG A 320 -28.942 -57.412 579.037 1.00 96.72 N ANISOU 3354 NH1 ARG A 320 8868 15860 12021 -329 1277 1527 N ATOM 3355 NH2 ARG A 320 -28.083 -55.795 577.653 1.00103.89 N ANISOU 3355 NH2 ARG A 320 9802 16428 13242 -11 1023 1266 N ATOM 3356 N THR A 321 -28.199 -48.680 580.432 1.00 89.98 N ANISOU 3356 N THR A 321 7972 14790 11427 2075 891 -175 N ATOM 3357 CA THR A 321 -28.296 -47.240 580.646 1.00 86.38 C ANISOU 3357 CA THR A 321 7579 14201 11040 2410 764 -441 C ATOM 3358 C THR A 321 -28.796 -46.526 579.397 1.00 90.07 C ANISOU 3358 C THR A 321 7966 14426 11829 2390 561 -454 C ATOM 3359 O THR A 321 -29.523 -45.530 579.499 1.00110.64 O ANISOU 3359 O THR A 321 10485 17043 14509 2598 527 -602 O ATOM 3360 CB THR A 321 -26.934 -46.681 581.066 1.00 95.17 C ANISOU 3360 CB THR A 321 9015 15055 12091 2586 613 -590 C ATOM 3361 OG1 THR A 321 -26.525 -47.289 582.297 1.00107.15 O ANISOU 3361 OG1 THR A 321 10608 16807 13296 2625 807 -584 O ATOM 3362 CG2 THR A 321 -27.004 -45.172 581.246 1.00100.60 C ANISOU 3362 CG2 THR A 321 9807 15560 12857 2885 446 -842 C ATOM 3363 N VAL A 322 -28.420 -47.014 578.212 1.00 80.07 N ANISOU 3363 N VAL A 322 6735 12938 10751 2138 423 -295 N ATOM 3364 CA VAL A 322 -28.939 -46.436 576.978 1.00 84.43 C ANISOU 3364 CA VAL A 322 7210 13272 11599 2078 238 -274 C ATOM 3365 C VAL A 322 -30.397 -46.830 576.756 1.00100.79 C ANISOU 3365 C VAL A 322 8966 15608 13723 1971 372 -178 C ATOM 3366 O VAL A 322 -31.123 -46.132 576.036 1.00100.91 O ANISOU 3366 O VAL A 322 8866 15517 13960 2011 257 -204 O ATOM 3367 CB VAL A 322 -28.056 -46.846 575.780 1.00 91.79 C ANISOU 3367 CB VAL A 322 8299 13885 12691 1837 45 -139 C ATOM 3368 CG1 VAL A 322 -28.055 -48.346 575.588 1.00 99.19 C ANISOU 3368 CG1 VAL A 322 9167 14987 13532 1531 175 73 C ATOM 3369 CG2 VAL A 322 -28.514 -46.157 574.500 1.00 88.25 C ANISOU 3369 CG2 VAL A 322 7806 13189 12535 1776 -159 -107 C ATOM 3370 N LEU A 323 -30.848 -47.935 577.354 1.00106.69 N ANISOU 3370 N LEU A 323 9577 16687 14274 1817 606 -44 N ATOM 3371 CA LEU A 323 -32.236 -48.371 577.261 1.00 97.05 C ANISOU 3371 CA LEU A 323 8066 15731 13077 1695 741 68 C ATOM 3372 C LEU A 323 -33.014 -48.135 578.551 1.00 93.68 C ANISOU 3372 C LEU A 323 7482 15669 12443 1905 971 -23 C ATOM 3373 O LEU A 323 -34.148 -48.611 578.672 1.00103.57 O ANISOU 3373 O LEU A 323 8490 17193 13670 1797 1117 91 O ATOM 3374 CB LEU A 323 -32.304 -49.855 576.883 1.00 86.98 C ANISOU 3374 CB LEU A 323 6763 14543 11744 1302 815 337 C ATOM 3375 CG LEU A 323 -31.609 -50.275 575.584 1.00 86.21 C ANISOU 3375 CG LEU A 323 6822 14116 11816 1058 606 444 C ATOM 3376 CD1 LEU A 323 -31.932 -51.725 575.234 1.00 81.85 C ANISOU 3376 CD1 LEU A 323 6243 13653 11206 667 677 709 C ATOM 3377 CD2 LEU A 323 -31.981 -49.349 574.441 1.00 89.16 C ANISOU 3377 CD2 LEU A 323 7155 14242 12478 1123 382 349 C ATOM 3378 N GLU A 324 -32.437 -47.414 579.518 1.00101.83 N ANISOU 3378 N GLU A 324 8661 16710 13318 2198 999 -225 N ATOM 3379 CA GLU A 324 -33.091 -47.180 580.800 1.00114.30 C ANISOU 3379 CA GLU A 324 10125 18637 14667 2410 1216 -331 C ATOM 3380 C GLU A 324 -33.477 -45.726 581.032 1.00122.38 C ANISOU 3380 C GLU A 324 11132 19597 15770 2778 1135 -591 C ATOM 3381 O GLU A 324 -34.328 -45.463 581.887 1.00120.07 O ANISOU 3381 O GLU A 324 10676 19608 15337 2955 1309 -675 O ATOM 3382 CB GLU A 324 -32.186 -47.645 581.952 1.00 91.16 C ANISOU 3382 CB GLU A 324 7390 15825 11422 2444 1344 -352 C ATOM 3383 CG GLU A 324 -32.869 -47.679 583.313 1.00 96.37 C ANISOU 3383 CG GLU A 324 7934 16887 11796 2590 1597 -409 C ATOM 3384 CD GLU A 324 -32.376 -48.821 584.183 1.00 95.66 C ANISOU 3384 CD GLU A 324 7935 16997 11414 2399 1776 -250 C ATOM 3385 OE1 GLU A 324 -32.290 -49.962 583.681 1.00 85.25 O ANISOU 3385 OE1 GLU A 324 6594 15671 10128 2047 1797 9 O ATOM 3386 OE2 GLU A 324 -32.070 -48.578 585.368 1.00 74.13 O ANISOU 3386 OE2 GLU A 324 5321 14418 8427 2592 1883 -381 O ATOM 3387 N SER A 325 -32.880 -44.783 580.299 1.00115.55 N ANISOU 3387 N SER A 325 10438 18346 15121 2886 872 -708 N ATOM 3388 CA SER A 325 -33.280 -43.386 580.430 1.00109.45 C ANISOU 3388 CA SER A 325 9662 17479 14444 3204 767 -930 C ATOM 3389 C SER A 325 -34.685 -43.153 579.891 1.00117.10 C ANISOU 3389 C SER A 325 10310 18575 15607 3206 802 -877 C ATOM 3390 O SER A 325 -35.395 -42.264 580.375 1.00111.59 O ANISOU 3390 O SER A 325 9508 17989 14904 3482 838 -1042 O ATOM 3391 CB SER A 325 -32.279 -42.487 579.706 1.00105.83 C ANISOU 3391 CB SER A 325 9482 16557 14173 3254 458 -1012 C ATOM 3392 OG SER A 325 -31.012 -42.524 580.337 1.00101.87 O ANISOU 3392 OG SER A 325 9279 15937 13491 3304 414 -1095 O ATOM 3393 N VAL A 326 -35.101 -43.937 578.895 1.00139.47 N ANISOU 3393 N VAL A 326 12990 21390 18613 2904 784 -653 N ATOM 3394 CA VAL A 326 -36.434 -43.781 578.322 1.00114.57 C ANISOU 3394 CA VAL A 326 9527 18343 15662 2879 800 -584 C ATOM 3395 C VAL A 326 -37.512 -44.093 579.351 1.00118.29 C ANISOU 3395 C VAL A 326 9734 19277 15935 2972 1085 -591 C ATOM 3396 O VAL A 326 -38.589 -43.484 579.338 1.00117.09 O ANISOU 3396 O VAL A 326 9345 19247 15897 3132 1119 -648 O ATOM 3397 CB VAL A 326 -36.580 -44.678 577.075 1.00 83.44 C ANISOU 3397 CB VAL A 326 5509 14280 11914 2504 707 -345 C ATOM 3398 CG1 VAL A 326 -35.558 -44.295 576.016 1.00 91.70 C ANISOU 3398 CG1 VAL A 326 6808 14874 13158 2422 423 -333 C ATOM 3399 CG2 VAL A 326 -36.432 -46.148 577.451 1.00 71.84 C ANISOU 3399 CG2 VAL A 326 4028 13047 10222 2220 891 -162 C ATOM 3400 N LEU A 327 -37.250 -45.044 580.249 1.00113.79 N ANISOU 3400 N LEU A 327 9196 18973 15067 2865 1294 -516 N ATOM 3401 CA LEU A 327 -38.309 -45.596 581.088 1.00118.02 C ANISOU 3401 CA LEU A 327 9467 19963 15414 2851 1569 -437 C ATOM 3402 C LEU A 327 -38.683 -44.679 582.249 1.00135.39 C ANISOU 3402 C LEU A 327 11623 22379 17438 3241 1698 -677 C ATOM 3403 O LEU A 327 -39.864 -44.578 582.601 1.00154.14 O ANISOU 3403 O LEU A 327 13712 25059 19796 3332 1855 -671 O ATOM 3404 CB LEU A 327 -37.890 -46.967 581.623 1.00104.55 C ANISOU 3404 CB LEU A 327 7826 18449 13448 2565 1732 -234 C ATOM 3405 CG LEU A 327 -38.559 -48.175 580.959 1.00 98.35 C ANISOU 3405 CG LEU A 327 6859 17770 12739 2167 1773 70 C ATOM 3406 CD1 LEU A 327 -38.004 -48.421 579.565 1.00109.64 C ANISOU 3406 CD1 LEU A 327 8416 18816 14425 1933 1528 166 C ATOM 3407 CD2 LEU A 327 -38.412 -49.422 581.817 1.00 98.31 C ANISOU 3407 CD2 LEU A 327 6884 18035 12435 1934 1973 265 C ATOM 3408 N VAL A 328 -37.709 -44.009 582.859 1.00124.10 N ANISOU 3408 N VAL A 328 10477 20802 15876 3474 1628 -891 N ATOM 3409 CA VAL A 328 -37.905 -43.338 584.141 1.00138.46 C ANISOU 3409 CA VAL A 328 12310 22849 17447 3816 1765 -1117 C ATOM 3410 C VAL A 328 -38.094 -41.845 583.906 1.00154.08 C ANISOU 3410 C VAL A 328 14324 24607 19612 4156 1582 -1370 C ATOM 3411 O VAL A 328 -37.206 -41.175 583.363 1.00153.78 O ANISOU 3411 O VAL A 328 14543 24168 19719 4209 1323 -1469 O ATOM 3412 CB VAL A 328 -36.727 -43.602 585.092 1.00 99.72 C ANISOU 3412 CB VAL A 328 7710 17938 12241 3850 1803 -1191 C ATOM 3413 CG1 VAL A 328 -36.919 -42.845 586.389 1.00100.59 C ANISOU 3413 CG1 VAL A 328 7860 18263 12097 4210 1918 -1441 C ATOM 3414 CG2 VAL A 328 -36.585 -45.096 585.358 1.00 95.13 C ANISOU 3414 CG2 VAL A 328 7090 17580 11474 3502 1986 -919 C ATOM 3415 N ASP A 329 -39.250 -41.326 584.328 1.00147.61 N ANISOU 3415 N ASP A 329 13249 24051 18784 4379 1711 -1464 N ATOM 3416 CA ASP A 329 -39.550 -39.894 584.295 1.00128.70 C ANISOU 3416 CA ASP A 329 10871 21501 16527 4737 1566 -1718 C ATOM 3417 C ASP A 329 -39.176 -39.280 582.947 1.00143.73 C ANISOU 3417 C ASP A 329 12882 22934 18794 4665 1246 -1694 C ATOM 3418 O ASP A 329 -38.457 -38.282 582.864 1.00143.61 O ANISOU 3418 O ASP A 329 13132 22598 18835 4844 1017 -1876 O ATOM 3419 CB ASP A 329 -38.844 -39.166 585.441 1.00113.82 C ANISOU 3419 CB ASP A 329 9264 19606 14376 5048 1551 -1998 C ATOM 3420 N ASP A 330 -39.681 -39.891 581.879 1.00138.67 N ANISOU 3420 N ASP A 330 12039 22255 18393 4383 1220 -1453 N ATOM 3421 CA ASP A 330 -39.371 -39.460 580.520 1.00119.67 C ANISOU 3421 CA ASP A 330 9718 19425 16326 4260 929 -1376 C ATOM 3422 C ASP A 330 -39.543 -37.954 580.351 1.00121.50 C ANISOU 3422 C ASP A 330 10009 19435 16719 4575 731 -1582 C ATOM 3423 O ASP A 330 -38.703 -37.291 579.742 1.00124.31 O ANISOU 3423 O ASP A 330 10630 19400 17202 4571 464 -1621 O ATOM 3424 CB ASP A 330 -40.256 -40.199 579.514 1.00106.67 C ANISOU 3424 CB ASP A 330 7774 17841 14915 3972 951 -1115 C TER 3425 ASP A 330 HETATM 3426 C10 YSS A2401 -6.791 -58.022 540.768 1.00 26.30 C HETATM 3427 C13 YSS A2401 -7.842 -56.243 543.887 1.00 42.92 C HETATM 3428 C15 YSS A2401 -8.502 -54.452 545.459 1.00 48.36 C HETATM 3429 C17 YSS A2401 -7.899 -54.451 548.059 1.00 47.09 C HETATM 3430 C20 YSS A2401 -5.131 -55.063 549.534 1.00 37.51 C HETATM 3431 C21 YSS A2401 -9.455 -53.278 545.227 1.00 42.42 C HETATM 3432 C01 YSS A2401 -2.084 -58.713 547.656 1.00 30.48 C HETATM 3433 C02 YSS A2401 -3.566 -59.190 547.592 1.00 25.94 C HETATM 3434 C03 YSS A2401 -4.509 -58.303 546.761 1.00 25.25 C HETATM 3435 C04 YSS A2401 -5.954 -58.873 546.573 1.00 37.84 C HETATM 3436 C05 YSS A2401 -6.120 -60.183 545.879 1.00 40.01 C HETATM 3437 C06 YSS A2401 -6.891 -60.594 544.814 1.00 41.21 C HETATM 3438 C07 YSS A2401 -7.779 -59.576 544.184 1.00 28.69 C HETATM 3439 C08 YSS A2401 -7.018 -58.636 543.186 1.00 42.02 C HETATM 3440 C09 YSS A2401 -6.789 -59.240 541.747 1.00 31.05 C HETATM 3441 C11 YSS A2401 -7.179 -56.895 541.602 1.00 35.41 C HETATM 3442 C12 YSS A2401 -7.737 -57.331 542.887 1.00 43.38 C HETATM 3443 C14 YSS A2401 -8.860 -55.437 544.321 1.00 55.38 C HETATM 3444 C16 YSS A2401 -8.627 -55.120 546.864 1.00 42.97 C HETATM 3445 C18 YSS A2401 -7.718 -55.334 549.331 1.00 30.42 C HETATM 3446 C19 YSS A2401 -6.342 -56.018 549.495 1.00 25.34 C HETATM 3447 O1 YSS A2401 -1.163 -59.571 547.817 1.00 27.40 O HETATM 3448 O2 YSS A2401 -1.843 -57.481 547.540 1.00 25.08 O HETATM 3449 O3 YSS A2401 -7.855 -60.106 541.448 1.00 46.62 O HETATM 3450 O4 YSS A2401 -7.054 -55.679 541.253 1.00 33.42 O HETATM 3451 O5 YSS A2401 -7.147 -54.047 545.239 1.00 29.29 O HETATM 3452 NA NA A2402 -6.177 -56.849 564.032 1.00 31.28 NA HETATM 3453 CAC FLC A2403 -3.381 -58.220 585.780 1.00114.65 C HETATM 3454 CA FLC A2403 -2.315 -57.692 584.815 1.00100.04 C HETATM 3455 CB FLC A2403 -2.299 -56.160 584.730 1.00101.55 C HETATM 3456 CBC FLC A2403 -2.911 -55.713 583.355 1.00 77.44 C HETATM 3457 CG FLC A2403 -0.848 -55.674 584.822 1.00110.85 C HETATM 3458 CGC FLC A2403 -0.723 -54.169 584.573 1.00 95.45 C HETATM 3459 OA1 FLC A2403 -4.600 -58.126 585.552 1.00111.07 O HETATM 3460 OA2 FLC A2403 -2.942 -58.770 586.850 1.00 90.79 O HETATM 3461 OB1 FLC A2403 -2.258 -55.189 582.458 1.00 82.19 O HETATM 3462 OB2 FLC A2403 -4.174 -55.960 583.284 1.00 69.08 O HETATM 3463 OG1 FLC A2403 0.223 -53.693 583.905 1.00 78.06 O HETATM 3464 OG2 FLC A2403 -1.627 -53.425 585.073 1.00 99.63 O HETATM 3465 OHB FLC A2403 -3.045 -55.595 585.770 1.00114.46 O HETATM 3466 S SO4 A2404 0.211 -47.089 585.708 1.00 48.82 S HETATM 3467 O1 SO4 A2404 0.334 -48.519 585.439 1.00 46.59 O HETATM 3468 O2 SO4 A2404 0.306 -46.334 584.460 1.00 58.34 O HETATM 3469 O3 SO4 A2404 1.284 -46.666 586.604 1.00 59.51 O HETATM 3470 O4 SO4 A2404 -1.083 -46.835 586.335 1.00 62.41 O HETATM 3471 S SO4 A2405 8.438 -31.299 612.218 1.00 52.32 S HETATM 3472 O1 SO4 A2405 8.985 -31.023 610.893 1.00 64.35 O HETATM 3473 O2 SO4 A2405 6.991 -31.108 612.206 1.00 61.38 O HETATM 3474 O3 SO4 A2405 8.727 -32.681 612.585 1.00 62.91 O HETATM 3475 O4 SO4 A2405 9.044 -30.393 613.189 1.00 67.15 O HETATM 3476 S SO4 A2406 7.065 -59.547 594.534 1.00137.43 S HETATM 3477 O1 SO4 A2406 7.943 -60.336 593.673 1.00113.70 O HETATM 3478 O2 SO4 A2406 5.840 -59.224 593.805 1.00103.38 O HETATM 3479 O3 SO4 A2406 6.734 -60.315 595.734 1.00114.27 O HETATM 3480 O4 SO4 A2406 7.747 -58.314 594.925 1.00100.02 O HETATM 3481 S SO4 A2407 7.756 -33.618 598.555 1.00 99.49 S HETATM 3482 O1 SO4 A2407 8.571 -32.666 597.803 1.00 76.33 O HETATM 3483 O2 SO4 A2407 7.066 -34.517 597.634 1.00 86.80 O HETATM 3484 O3 SO4 A2407 6.762 -32.905 599.350 1.00 86.98 O HETATM 3485 O4 SO4 A2407 8.610 -34.394 599.450 1.00 79.29 O HETATM 3486 S SO4 A2408 -2.364 -64.263 596.771 1.00139.84 S HETATM 3487 O1 SO4 A2408 -1.682 -63.566 595.683 1.00107.08 O HETATM 3488 O2 SO4 A2408 -3.531 -64.974 596.256 1.00116.52 O HETATM 3489 O3 SO4 A2408 -2.789 -63.290 597.776 1.00131.82 O HETATM 3490 O4 SO4 A2408 -1.455 -65.228 597.382 1.00126.43 O HETATM 3491 O HOH A2501 -7.243 -62.718 541.035 1.00 38.08 O HETATM 3492 O HOH A2502 -6.443 -58.993 561.331 1.00 37.65 O HETATM 3493 O HOH A2503 -5.713 -55.642 557.175 1.00 38.87 O HETATM 3494 O HOH A2504 1.831 -52.275 586.513 1.00 23.68 O HETATM 3495 O HOH A2505 -7.711 -57.899 559.045 1.00 30.58 O HETATM 3496 O HOH A2506 -16.211 -53.520 531.418 1.00 57.08 O HETATM 3497 O HOH A2507 -6.228 -60.784 565.005 1.00 22.72 O HETATM 3498 O HOH A2508 -20.044 -52.117 527.305 1.00 33.91 O HETATM 3499 O HOH A2509 1.061 -53.188 546.107 1.00 36.06 O HETATM 3500 O HOH A2510 2.501 -60.159 547.378 1.00 40.59 O HETATM 3501 O HOH A2511 9.846 -78.290 601.946 1.00 62.77 O HETATM 3502 O HOH A2512 -4.329 -37.311 594.306 1.00 36.61 O CONECT 63 1537 CONECT 555 3452 CONECT 562 3452 CONECT 774 1403 CONECT 858 3452 CONECT 889 3452 CONECT 1403 774 CONECT 1537 63 CONECT 3241 3246 CONECT 3246 3241 3247 CONECT 3247 3246 3248 3254 CONECT 3248 3247 3249 CONECT 3249 3248 3250 CONECT 3250 3249 3251 CONECT 3251 3250 3252 3253 CONECT 3252 3251 CONECT 3253 3251 CONECT 3254 3247 3255 3256 CONECT 3255 3254 CONECT 3256 3254 CONECT 3426 3440 3441 CONECT 3427 3442 3443 CONECT 3428 3431 3443 3444 3451 CONECT 3429 3444 3445 CONECT 3430 3446 CONECT 3431 3428 CONECT 3432 3433 3447 3448 CONECT 3433 3432 3434 CONECT 3434 3433 3435 CONECT 3435 3434 3436 CONECT 3436 3435 3437 CONECT 3437 3436 3438 CONECT 3438 3437 3439 CONECT 3439 3438 3440 3442 CONECT 3440 3426 3439 3449 CONECT 3441 3426 3442 3450 CONECT 3442 3427 3439 3441 CONECT 3443 3427 3428 CONECT 3444 3428 3429 CONECT 3445 3429 3446 CONECT 3446 3430 3445 CONECT 3447 3432 CONECT 3448 3432 CONECT 3449 3440 CONECT 3450 3441 CONECT 3451 3428 CONECT 3452 555 562 858 889 CONECT 3453 3454 3459 3460 CONECT 3454 3453 3455 CONECT 3455 3454 3456 3457 3465 CONECT 3456 3455 3461 3462 CONECT 3457 3455 3458 CONECT 3458 3457 3463 3464 CONECT 3459 3453 CONECT 3460 3453 CONECT 3461 3456 CONECT 3462 3456 CONECT 3463 3458 CONECT 3464 3458 CONECT 3465 3455 CONECT 3466 3467 3468 3469 3470 CONECT 3467 3466 CONECT 3468 3466 CONECT 3469 3466 CONECT 3470 3466 CONECT 3471 3472 3473 3474 3475 CONECT 3472 3471 CONECT 3473 3471 CONECT 3474 3471 CONECT 3475 3471 CONECT 3476 3477 3478 3479 3480 CONECT 3477 3476 CONECT 3478 3476 CONECT 3479 3476 CONECT 3480 3476 CONECT 3481 3482 3483 3484 3485 CONECT 3482 3481 CONECT 3483 3481 CONECT 3484 3481 CONECT 3485 3481 CONECT 3486 3487 3488 3489 3490 CONECT 3487 3486 CONECT 3488 3486 CONECT 3489 3486 CONECT 3490 3486 MASTER 349 0 9 22 2 0 0 6 3494 1 85 37 END