HEADER SIGNALING PROTEIN, HYDROLASE 12-AUG-10 3OE6 TITLE CRYSTAL STRUCTURE OF THE CXCR4 CHEMOKINE RECEPTOR IN COMPLEX WITH A TITLE 2 SMALL MOLECULE ANTAGONIST IT1T IN I222 SPACEGROUP COMPND MOL_ID: 1; COMPND 2 MOLECULE: C-X-C CHEMOKINE RECEPTOR TYPE 4, LYSOZYME CHIMERA; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: CXCR4 RESIDUES 2-228, LYSOZYME RESIDUES 1002-1161, CXCR4 COMPND 5 RESIDUES 231-325; COMPND 6 SYNONYM: CXC-R4, CXCR-4, STROMAL CELL-DERIVED FACTOR 1 RECEPTOR, SDF- COMPND 7 1 RECEPTOR, FUSIN, LEUKOCYTE-DERIVED SEVEN TRANSMEMBRANE DOMAIN COMPND 8 RECEPTOR, LESTR, LCR1, FB22, NPYRL, HM89, LYSIS PROTEIN, MURAMIDASE, COMPND 9 ENDOLYSIN; COMPND 10 EC: 3.2.1.17; COMPND 11 ENGINEERED: YES; COMPND 12 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ENTEROBACTERIA PHAGE T4; SOURCE 3 ORGANISM_TAXID: 9606, 10665; SOURCE 4 GENE: CXCR4, CXCR4_HUMAN,E; SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: SF9; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PFASTBAC KEYWDS STRUCTURAL GENOMICS, PSI-2, PROTEIN STRUCTURE INITIATIVE, ACCELERATED KEYWDS 2 TECHNOLOGIES CENTER FOR GENE TO 3D STRUCTURE, ATCG3D, 7TM, G KEYWDS 3 PROTEIN-COUPLED RECEPTOR, GPCR, SIGNAL TRANSDUCTION, HYDROLASE, KEYWDS 4 CANCER, HIV-1 CO-RECEPTOR, CHEMOKINE, CXCL12, SDF1, ISOTHIOUREA, KEYWDS 5 IT1T, CHIMERA, T4L FUSION, MEMBRANE PROTEIN, TRANSMEMBRANE, KEYWDS 6 SINGNALING PROTEIN, PSI-BIOLOGY, GPCR NETWORK, SIGNALING PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR B.WU,C.D.MOL,G.W.HAN,V.KATRITCH,E.Y.T.CHIEN,W.LIU,V.CHEREZOV, AUTHOR 2 R.C.STEVENS,ACCELERATED TECHNOLOGIES CENTER FOR GENE TO 3D STRUCTURE AUTHOR 3 (ATCG3D),GPCR NETWORK (GPCR) REVDAT 6 06-OCT-21 3OE6 1 REMARK SEQADV REVDAT 5 26-JUL-17 3OE6 1 SOURCE REMARK REVDAT 4 02-MAY-12 3OE6 1 REMARK VERSN REVDAT 3 16-FEB-11 3OE6 1 HEADER REVDAT 2 05-JAN-11 3OE6 1 JRNL REVDAT 1 27-OCT-10 3OE6 0 JRNL AUTH B.WU,E.Y.CHIEN,C.D.MOL,G.FENALTI,W.LIU,V.KATRITCH,R.ABAGYAN, JRNL AUTH 2 A.BROOUN,P.WELLS,F.C.BI,D.J.HAMEL,P.KUHN,T.M.HANDEL, JRNL AUTH 3 V.CHEREZOV,R.C.STEVENS JRNL TITL STRUCTURES OF THE CXCR4 CHEMOKINE GPCR WITH SMALL-MOLECULE JRNL TITL 2 AND CYCLIC PEPTIDE ANTAGONISTS. JRNL REF SCIENCE V. 330 1066 2010 JRNL REFN ISSN 0036-8075 JRNL PMID 20929726 JRNL DOI 10.1126/SCIENCE.1194396 REMARK 2 REMARK 2 RESOLUTION. 3.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.8.0 REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER, REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN, REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 8310 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.236 REMARK 3 R VALUE (WORKING SET) : 0.232 REMARK 3 FREE R VALUE : 0.306 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.890 REMARK 3 FREE R VALUE TEST SET COUNT : 406 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 5 REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.58 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2289 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2434 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2172 REMARK 3 BIN R VALUE (WORKING SET) : 0.2415 REMARK 3 BIN FREE R VALUE : 0.2797 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.11 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 117 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3356 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 79 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 89.11 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 69.12 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -1.48050 REMARK 3 B22 (A**2) : 5.02820 REMARK 3 B33 (A**2) : -3.54760 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.578 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL REMARK 3 REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797 REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.847 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.747 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 3521 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 4767 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 1170 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : 61 ; 2.000 ; HARMONIC REMARK 3 GENERAL PLANES : 501 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 3448 ; 20.000 ; HARMONIC REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : 463 ; 5.000 ; SEMIHARMONIC REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL REMARK 3 IDEAL-DIST CONTACT TERM : 3940 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.010 REMARK 3 BOND ANGLES (DEGREES) : 1.31 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.92 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 22.48 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 3 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: { A|35 - A|226 } REMARK 3 ORIGIN FOR THE GROUP (A): 16.6490 31.6020 57.3607 REMARK 3 T TENSOR REMARK 3 T11: -0.1656 T22: -0.1593 REMARK 3 T33: -0.0392 T12: 0.0343 REMARK 3 T13: -0.0383 T23: 0.0039 REMARK 3 L TENSOR REMARK 3 L11: 1.7894 L22: 2.3820 REMARK 3 L33: 2.7213 L12: -0.2014 REMARK 3 L13: -0.0230 L23: 0.7673 REMARK 3 S TENSOR REMARK 3 S11: 0.0141 S12: 0.0783 S13: 0.2435 REMARK 3 S21: 0.0109 S22: -0.0029 S23: -0.2000 REMARK 3 S31: 0.2532 S32: 0.1668 S33: -0.0112 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: { A|1010 - A|1159 } REMARK 3 ORIGIN FOR THE GROUP (A): 1.4948 23.5205 11.2511 REMARK 3 T TENSOR REMARK 3 T11: -0.0243 T22: 0.2227 REMARK 3 T33: -0.3040 T12: 0.1520 REMARK 3 T13: 0.0225 T23: 0.0184 REMARK 3 L TENSOR REMARK 3 L11: 0.0000 L22: 0.8159 REMARK 3 L33: 2.9429 L12: 0.2535 REMARK 3 L13: -0.7642 L23: 0.0777 REMARK 3 S TENSOR REMARK 3 S11: -0.0079 S12: -0.0205 S13: 0.0195 REMARK 3 S21: 0.0870 S22: 0.2047 S23: 0.0639 REMARK 3 S31: 0.4021 S32: 0.0755 S33: -0.1969 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: { A|235 - A|312 } REMARK 3 ORIGIN FOR THE GROUP (A): 10.1585 19.8890 60.4589 REMARK 3 T TENSOR REMARK 3 T11: -0.0082 T22: -0.0729 REMARK 3 T33: 0.0056 T12: -0.0193 REMARK 3 T13: -0.0115 T23: 0.0074 REMARK 3 L TENSOR REMARK 3 L11: 1.5458 L22: 0.9685 REMARK 3 L33: 0.0000 L12: -0.4452 REMARK 3 L13: 0.3227 L23: 0.5188 REMARK 3 S TENSOR REMARK 3 S11: 0.0855 S12: -0.1813 S13: -0.2110 REMARK 3 S21: -0.0025 S22: -0.0681 S23: -0.0897 REMARK 3 S31: 0.1624 S32: -0.0264 S33: -0.0174 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 3OE6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-OCT-10. REMARK 100 THE DEPOSITION ID IS D_1000061002. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 25-FEB-10 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.5 REMARK 200 NUMBER OF CRYSTALS USED : 4 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-D REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0330 REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL REMARK 200 OPTICS : MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10233 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 94.4 REMARK 200 DATA REDUNDANCY : 3.600 REMARK 200 R MERGE (I) : 0.13600 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 10.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.42 REMARK 200 COMPLETENESS FOR SHELL (%) : 78.2 REMARK 200 DATA REDUNDANCY IN SHELL : 2.20 REMARK 200 R MERGE FOR SHELL (I) : 0.67000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.500 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 57.96 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.93 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: LIPIDIC CUBIC PHASE MADE OF MONOOLEIN REMARK 280 AND CHOLESTEROL, 20-26% PEG400, 0.3M SODIUM MALONATE, 5MM NICKEL REMARK 280 CHLORIDE, 0.1M SODIUM CITRATE PH 5.0-5.5, LIPIDIC CUBIC PHASE, REMARK 280 TEMPERATURE 293K, PH 5.5 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -X,Y,-Z REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z+1/2 REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 35.56050 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 39.35550 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 120.29600 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 35.56050 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 39.35550 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 120.29600 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 35.56050 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 39.35550 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 120.29600 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 35.56050 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 39.35550 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 120.29600 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2640 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 47890 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 78.71100 REMARK 350 BIOMT3 2 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 ASP A -9 REMARK 465 TYR A -8 REMARK 465 LYS A -7 REMARK 465 ASP A -6 REMARK 465 ASP A -5 REMARK 465 ASP A -4 REMARK 465 ASP A -3 REMARK 465 ALA A -2 REMARK 465 GLY A -1 REMARK 465 ALA A 0 REMARK 465 PRO A 1 REMARK 465 GLU A 2 REMARK 465 GLY A 3 REMARK 465 ILE A 4 REMARK 465 SER A 5 REMARK 465 ILE A 6 REMARK 465 TYR A 7 REMARK 465 THR A 8 REMARK 465 SER A 9 REMARK 465 ASP A 10 REMARK 465 ASN A 11 REMARK 465 TYR A 12 REMARK 465 THR A 13 REMARK 465 GLU A 14 REMARK 465 GLU A 15 REMARK 465 MET A 16 REMARK 465 GLY A 17 REMARK 465 SER A 18 REMARK 465 GLY A 19 REMARK 465 ASP A 20 REMARK 465 TYR A 21 REMARK 465 ASP A 22 REMARK 465 SER A 23 REMARK 465 MET A 24 REMARK 465 LYS A 25 REMARK 465 GLU A 26 REMARK 465 PRO A 27 REMARK 465 CYS A 28 REMARK 465 PHE A 29 REMARK 465 ARG A 30 REMARK 465 GLU A 31 REMARK 465 GLU A 32 REMARK 465 ASN A 33 REMARK 465 ALA A 34 REMARK 465 SER A 227 REMARK 465 HIS A 228 REMARK 465 SER A 229 REMARK 465 GLY A 900 REMARK 465 SER A 901 REMARK 465 ASN A 1002 REMARK 465 ILE A 1003 REMARK 465 PHE A 1004 REMARK 465 GLU A 1005 REMARK 465 MET A 1006 REMARK 465 LEU A 1007 REMARK 465 ARG A 1008 REMARK 465 ILE A 1009 REMARK 465 THR A 1115 REMARK 465 ASN A 1116 REMARK 465 ALA A 1160 REMARK 465 TYR A 1161 REMARK 465 GLY A 1200 REMARK 465 SER A 1201 REMARK 465 LYS A 230 REMARK 465 GLY A 231 REMARK 465 HIS A 232 REMARK 465 GLN A 233 REMARK 465 LYS A 234 REMARK 465 ALA A 313 REMARK 465 GLN A 314 REMARK 465 HIS A 315 REMARK 465 ALA A 316 REMARK 465 LEU A 317 REMARK 465 THR A 318 REMARK 465 SER A 319 REMARK 465 VAL A 320 REMARK 465 SER A 321 REMARK 465 ARG A 322 REMARK 465 GLY A 323 REMARK 465 SER A 324 REMARK 465 SER A 325 REMARK 465 GLY A 326 REMARK 465 ARG A 327 REMARK 465 PRO A 328 REMARK 465 LEU A 329 REMARK 465 GLU A 330 REMARK 465 VAL A 331 REMARK 465 LEU A 332 REMARK 465 PHE A 333 REMARK 465 GLN A 334 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 ASP A 181 CG OD1 OD2 REMARK 470 THR A1059 OG1 CG2 REMARK 470 ASP A1092 CG OD1 OD2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O LYS A 38 CG PRO A 42 2.15 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ALA A 98 CB - CA - C ANGL. DEV. = 9.9 DEGREES REMARK 500 ALA A 100 N - CA - CB ANGL. DEV. = -9.9 DEGREES REMARK 500 ASN A 101 N - CA - CB ANGL. DEV. = 12.3 DEGREES REMARK 500 PRO A 147 C - N - CD ANGL. DEV. = -14.4 DEGREES REMARK 500 LYS A1083 CB - CA - C ANGL. DEV. = 14.5 DEGREES REMARK 500 ASP A1092 CB - CA - C ANGL. DEV. = -17.1 DEGREES REMARK 500 ALA A1093 CB - CA - C ANGL. DEV. = -11.0 DEGREES REMARK 500 ALA A1093 N - CA - C ANGL. DEV. = 17.9 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 OLC A 1600 REMARK 610 OLC A 1601 REMARK 610 OLC A 1602 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ITD A 1500 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC A 1600 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC A 1601 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC A 1602 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1603 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: ATCG3D_11 RELATED DB: TARGETDB REMARK 900 RELATED ID: 3ODU RELATED DB: PDB REMARK 900 SAME PROTEIN AT 2.5 A IN P21 SPACEGROUP REMARK 900 RELATED ID: 3OE0 RELATED DB: PDB REMARK 900 SAME PROTEIN IN COMPLEX WITH A CYCLIC PEPTIDE CVX15 REMARK 900 RELATED ID: 3OE8 RELATED DB: PDB REMARK 900 SAME PROTEIN IN P1 SPACEGROUP WITH 3 MOLECULES PER ASYMMETRIC UNIT REMARK 900 RELATED ID: 3OE9 RELATED DB: PDB REMARK 900 SAME PROTEIN IN P1 SPACEGROUP WITH 2 MOLECULES PER ASYMMETRIC UNIT REMARK 900 RELATED ID: GPCR-34 RELATED DB: TARGETTRACK REMARK 999 REMARK 999 SEQUENCE REMARK 999 THE PROTEIN IS A FUSION PROTEIN WITH RESIDUES ASN1002-TYR1161 OF T4 REMARK 999 LYSOZYME INSERTED BETWEEN SER229 AND LYS230 OF CXCR4, AS INDICATED REMARK 999 AS CXCR4-1 IN THE PUBLICATION. DBREF 3OE6 A 2 229 UNP P61073 CXCR4_HUMAN 2 229 DBREF 3OE6 A 1002 1161 UNP P00720 LYS_BPT4 1002 1161 DBREF 3OE6 A 230 325 UNP P61073 CXCR4_HUMAN 230 325 SEQADV 3OE6 ASP A -9 UNP P61073 EXPRESSION TAG SEQADV 3OE6 TYR A -8 UNP P61073 EXPRESSION TAG SEQADV 3OE6 LYS A -7 UNP P61073 EXPRESSION TAG SEQADV 3OE6 ASP A -6 UNP P61073 EXPRESSION TAG SEQADV 3OE6 ASP A -5 UNP P61073 EXPRESSION TAG SEQADV 3OE6 ASP A -4 UNP P61073 EXPRESSION TAG SEQADV 3OE6 ASP A -3 UNP P61073 EXPRESSION TAG SEQADV 3OE6 ALA A -2 UNP P61073 EXPRESSION TAG SEQADV 3OE6 GLY A -1 UNP P61073 EXPRESSION TAG SEQADV 3OE6 ALA A 0 UNP P61073 EXPRESSION TAG SEQADV 3OE6 PRO A 1 UNP P61073 EXPRESSION TAG SEQADV 3OE6 TRP A 125 UNP P61073 LEU 125 ENGINEERED MUTATION SEQADV 3OE6 GLY A 900 UNP P61073 LINKER SEQADV 3OE6 SER A 901 UNP P61073 LINKER SEQADV 3OE6 GLY A 1200 UNP P61073 LINKER SEQADV 3OE6 SER A 1201 UNP P61073 LINKER SEQADV 3OE6 THR A 1054 UNP P00720 CYS 1054 ENGINEERED MUTATION SEQADV 3OE6 ALA A 1097 UNP P00720 CYS 1097 ENGINEERED MUTATION SEQADV 3OE6 GLY A 326 UNP P61073 EXPRESSION TAG SEQADV 3OE6 ARG A 327 UNP P61073 EXPRESSION TAG SEQADV 3OE6 PRO A 328 UNP P61073 EXPRESSION TAG SEQADV 3OE6 LEU A 329 UNP P61073 EXPRESSION TAG SEQADV 3OE6 GLU A 330 UNP P61073 EXPRESSION TAG SEQADV 3OE6 VAL A 331 UNP P61073 EXPRESSION TAG SEQADV 3OE6 LEU A 332 UNP P61073 EXPRESSION TAG SEQADV 3OE6 PHE A 333 UNP P61073 EXPRESSION TAG SEQADV 3OE6 GLN A 334 UNP P61073 EXPRESSION TAG SEQRES 1 A 508 ASP TYR LYS ASP ASP ASP ASP ALA GLY ALA PRO GLU GLY SEQRES 2 A 508 ILE SER ILE TYR THR SER ASP ASN TYR THR GLU GLU MET SEQRES 3 A 508 GLY SER GLY ASP TYR ASP SER MET LYS GLU PRO CYS PHE SEQRES 4 A 508 ARG GLU GLU ASN ALA ASN PHE ASN LYS ILE PHE LEU PRO SEQRES 5 A 508 THR ILE TYR SER ILE ILE PHE LEU THR GLY ILE VAL GLY SEQRES 6 A 508 ASN GLY LEU VAL ILE LEU VAL MET GLY TYR GLN LYS LYS SEQRES 7 A 508 LEU ARG SER MET THR ASP LYS TYR ARG LEU HIS LEU SER SEQRES 8 A 508 VAL ALA ASP LEU LEU PHE VAL ILE THR LEU PRO PHE TRP SEQRES 9 A 508 ALA VAL ASP ALA VAL ALA ASN TRP TYR PHE GLY ASN PHE SEQRES 10 A 508 LEU CYS LYS ALA VAL HIS VAL ILE TYR THR VAL ASN LEU SEQRES 11 A 508 TYR SER SER VAL TRP ILE LEU ALA PHE ILE SER LEU ASP SEQRES 12 A 508 ARG TYR LEU ALA ILE VAL HIS ALA THR ASN SER GLN ARG SEQRES 13 A 508 PRO ARG LYS LEU LEU ALA GLU LYS VAL VAL TYR VAL GLY SEQRES 14 A 508 VAL TRP ILE PRO ALA LEU LEU LEU THR ILE PRO ASP PHE SEQRES 15 A 508 ILE PHE ALA ASN VAL SER GLU ALA ASP ASP ARG TYR ILE SEQRES 16 A 508 CYS ASP ARG PHE TYR PRO ASN ASP LEU TRP VAL VAL VAL SEQRES 17 A 508 PHE GLN PHE GLN HIS ILE MET VAL GLY LEU ILE LEU PRO SEQRES 18 A 508 GLY ILE VAL ILE LEU SER CYS TYR CYS ILE ILE ILE SER SEQRES 19 A 508 LYS LEU SER HIS SER GLY SER ASN ILE PHE GLU MET LEU SEQRES 20 A 508 ARG ILE ASP GLU GLY LEU ARG LEU LYS ILE TYR LYS ASP SEQRES 21 A 508 THR GLU GLY TYR TYR THR ILE GLY ILE GLY HIS LEU LEU SEQRES 22 A 508 THR LYS SER PRO SER LEU ASN ALA ALA LYS SER GLU LEU SEQRES 23 A 508 ASP LYS ALA ILE GLY ARG ASN THR ASN GLY VAL ILE THR SEQRES 24 A 508 LYS ASP GLU ALA GLU LYS LEU PHE ASN GLN ASP VAL ASP SEQRES 25 A 508 ALA ALA VAL ARG GLY ILE LEU ARG ASN ALA LYS LEU LYS SEQRES 26 A 508 PRO VAL TYR ASP SER LEU ASP ALA VAL ARG ARG ALA ALA SEQRES 27 A 508 LEU ILE ASN MET VAL PHE GLN MET GLY GLU THR GLY VAL SEQRES 28 A 508 ALA GLY PHE THR ASN SER LEU ARG MET LEU GLN GLN LYS SEQRES 29 A 508 ARG TRP ASP GLU ALA ALA VAL ASN LEU ALA LYS SER ARG SEQRES 30 A 508 TRP TYR ASN GLN THR PRO ASN ARG ALA LYS ARG VAL ILE SEQRES 31 A 508 THR THR PHE ARG THR GLY THR TRP ASP ALA TYR GLY SER SEQRES 32 A 508 LYS GLY HIS GLN LYS ARG LYS ALA LEU LYS THR THR VAL SEQRES 33 A 508 ILE LEU ILE LEU ALA PHE PHE ALA CYS TRP LEU PRO TYR SEQRES 34 A 508 TYR ILE GLY ILE SER ILE ASP SER PHE ILE LEU LEU GLU SEQRES 35 A 508 ILE ILE LYS GLN GLY CYS GLU PHE GLU ASN THR VAL HIS SEQRES 36 A 508 LYS TRP ILE SER ILE THR GLU ALA LEU ALA PHE PHE HIS SEQRES 37 A 508 CYS CYS LEU ASN PRO ILE LEU TYR ALA PHE LEU GLY ALA SEQRES 38 A 508 LYS PHE LYS THR SER ALA GLN HIS ALA LEU THR SER VAL SEQRES 39 A 508 SER ARG GLY SER SER GLY ARG PRO LEU GLU VAL LEU PHE SEQRES 40 A 508 GLN HET ITD A1500 27 HET OLC A1600 15 HET OLC A1601 15 HET OLC A1602 16 HET GOL A1603 6 HETNAM ITD (6,6-DIMETHYL-5,6-DIHYDROIMIDAZO[2,1-B][1,3]THIAZOL-3- HETNAM 2 ITD YL)METHYL N,N'-DICYCLOHEXYLIMIDOTHIOCARBAMATE HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETNAM GOL GLYCEROL HETSYN OLC 1-OLEOYL-R-GLYCEROL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 2 ITD C21 H34 N4 S2 FORMUL 3 OLC 3(C21 H40 O4) FORMUL 6 GOL C3 H8 O3 HELIX 1 1 PHE A 36 GLN A 66 1 31 HELIX 2 2 SER A 71 ILE A 89 1 19 HELIX 3 3 THR A 90 ALA A 100 1 11 HELIX 4 4 GLY A 105 HIS A 140 1 36 HELIX 5 5 SER A 144 LYS A 154 1 11 HELIX 6 6 LYS A 154 GLY A 159 1 6 HELIX 7 7 VAL A 160 LEU A 167 1 8 HELIX 8 8 THR A 168 PHE A 174 1 7 HELIX 9 9 ASP A 193 LEU A 208 1 16 HELIX 10 10 LEU A 208 LYS A 225 1 18 HELIX 11 11 SER A 1038 LEU A 1046 1 9 HELIX 12 12 THR A 1059 VAL A 1075 1 17 HELIX 13 13 LEU A 1084 LEU A 1091 1 8 HELIX 14 14 ASP A 1092 GLY A 1107 1 16 HELIX 15 15 GLY A 1110 PHE A 1114 5 5 HELIX 16 16 LEU A 1118 GLN A 1123 1 6 HELIX 17 17 ARG A 1125 ALA A 1134 1 10 HELIX 18 18 ARG A 1137 THR A 1142 1 6 HELIX 19 19 THR A 1142 THR A 1155 1 14 HELIX 20 20 ARG A 235 LEU A 267 1 33 HELIX 21 21 CYS A 274 TRP A 283 1 10 HELIX 22 22 ILE A 284 PHE A 292 1 9 HELIX 23 23 PHE A 293 CYS A 295 5 3 HELIX 24 24 CYS A 296 LEU A 301 1 6 SHEET 1 A 2 ALA A 175 ALA A 180 0 SHEET 2 A 2 ARG A 183 ARG A 188 -1 O ILE A 185 N SER A 178 SHEET 1 B 3 TYR A1018 LYS A1019 0 SHEET 2 B 3 TYR A1025 ILE A1027 -1 O THR A1026 N TYR A1018 SHEET 3 B 3 HIS A1031 THR A1034 -1 O HIS A1031 N ILE A1027 SSBOND 1 CYS A 109 CYS A 186 1555 1555 2.04 SITE 1 AC1 7 TRP A 94 ASP A 97 TYR A 116 ARG A 183 SITE 2 AC1 7 CYS A 186 ASP A 187 GLU A 288 SITE 1 AC2 8 LEU A 58 VAL A 59 VAL A 62 ILE A 269 SITE 2 AC2 8 ILE A 270 PRO A 299 TYR A 302 LEU A 305 SITE 1 AC3 4 VAL A 99 ALA A 100 TYR A 103 ILE A 223 SITE 1 AC4 5 LYS A 38 ILE A 39 PRO A 42 THR A 43 SITE 2 AC4 5 SER A 46 SITE 1 AC5 8 LEU A 120 SER A 123 VAL A 124 HIS A 203 SITE 2 AC5 8 GLY A 207 PHE A 248 TRP A 252 TYR A 256 CRYST1 71.121 78.711 240.592 90.00 90.00 90.00 I 2 2 2 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.014061 0.000000 0.000000 0.00000 SCALE2 0.000000 0.012705 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004156 0.00000 ATOM 1 N ASN A 35 17.386 15.338 82.755 1.00 89.78 N ANISOU 1 N ASN A 35 16829 9426 7856 1341 -1235 976 N ATOM 2 CA ASN A 35 18.516 16.168 82.337 1.00 88.06 C ANISOU 2 CA ASN A 35 16229 9392 7837 1558 -1480 830 C ATOM 3 C ASN A 35 19.167 15.691 81.018 1.00 90.49 C ANISOU 3 C ASN A 35 16358 9617 8406 1688 -1562 816 C ATOM 4 O ASN A 35 20.158 16.286 80.578 1.00 88.88 O ANISOU 4 O ASN A 35 15832 9556 8381 1866 -1751 701 O ATOM 5 CB ASN A 35 19.558 16.261 83.467 1.00 91.35 C ANISOU 5 CB ASN A 35 16796 9887 8025 1834 -1761 835 C ATOM 6 CG ASN A 35 19.146 17.117 84.645 1.00114.30 C ANISOU 6 CG ASN A 35 19746 12956 10725 1737 -1726 778 C ATOM 7 OD1 ASN A 35 18.607 18.222 84.492 1.00107.55 O ANISOU 7 OD1 ASN A 35 18587 12266 10013 1556 -1605 639 O ATOM 8 ND2 ASN A 35 19.448 16.653 85.851 1.00107.96 N ANISOU 8 ND2 ASN A 35 19328 12113 9577 1878 -1849 877 N ATOM 9 N PHE A 36 18.581 14.650 80.373 1.00 87.05 N ANISOU 9 N PHE A 36 16120 8957 7997 1581 -1405 919 N ATOM 10 CA PHE A 36 19.054 14.025 79.127 1.00 85.66 C ANISOU 10 CA PHE A 36 15845 8668 8033 1686 -1448 913 C ATOM 11 C PHE A 36 19.121 14.894 77.859 1.00 85.20 C ANISOU 11 C PHE A 36 15294 8771 8307 1620 -1412 760 C ATOM 12 O PHE A 36 19.671 14.439 76.850 1.00 83.48 O ANISOU 12 O PHE A 36 14980 8488 8251 1742 -1468 741 O ATOM 13 CB PHE A 36 18.364 12.670 78.874 1.00 88.94 C ANISOU 13 CB PHE A 36 16644 8783 8365 1573 -1290 1056 C ATOM 14 CG PHE A 36 18.828 11.565 79.796 1.00 94.15 C ANISOU 14 CG PHE A 36 17800 9229 8744 1772 -1412 1221 C ATOM 15 CD1 PHE A 36 20.092 11.002 79.653 1.00 98.70 C ANISOU 15 CD1 PHE A 36 18438 9734 9327 2133 -1671 1238 C ATOM 16 CD2 PHE A 36 17.996 11.075 80.795 1.00 98.65 C ANISOU 16 CD2 PHE A 36 18779 9663 9038 1604 -1264 1361 C ATOM 17 CE1 PHE A 36 20.524 9.985 80.508 1.00103.23 C ANISOU 17 CE1 PHE A 36 19485 10100 9636 2342 -1801 1397 C ATOM 18 CE2 PHE A 36 18.425 10.052 81.647 1.00105.13 C ANISOU 18 CE2 PHE A 36 20092 10269 9583 1793 -1379 1531 C ATOM 19 CZ PHE A 36 19.688 9.519 81.500 1.00104.54 C ANISOU 19 CZ PHE A 36 20083 10120 9519 2171 -1658 1551 C ATOM 20 N ASN A 37 18.622 16.157 77.927 1.00 79.97 N ANISOU 20 N ASN A 37 14332 8317 7737 1448 -1328 651 N ATOM 21 CA ASN A 37 18.666 17.147 76.836 1.00 76.64 C ANISOU 21 CA ASN A 37 13454 8057 7610 1381 -1297 514 C ATOM 22 C ASN A 37 20.124 17.539 76.500 1.00 79.61 C ANISOU 22 C ASN A 37 13575 8552 8120 1653 -1538 430 C ATOM 23 O ASN A 37 20.383 18.103 75.435 1.00 76.81 O ANISOU 23 O ASN A 37 12883 8292 8009 1640 -1526 340 O ATOM 24 CB ASN A 37 17.819 18.389 77.178 1.00 75.43 C ANISOU 24 CB ASN A 37 13093 8074 7494 1162 -1167 425 C ATOM 25 CG ASN A 37 18.489 19.410 78.079 1.00 93.97 C ANISOU 25 CG ASN A 37 15310 10603 9789 1273 -1328 336 C ATOM 26 OD1 ASN A 37 18.903 20.487 77.633 1.00 84.96 O ANISOU 26 OD1 ASN A 37 13812 9622 8849 1288 -1388 212 O ATOM 27 ND2 ASN A 37 18.615 19.098 79.365 1.00 86.72 N ANISOU 27 ND2 ASN A 37 14692 9661 8596 1349 -1402 396 N ATOM 28 N LYS A 38 21.050 17.211 77.395 1.00 78.21 N ANISOU 28 N LYS A 38 13565 8372 7779 1894 -1751 461 N ATOM 29 CA LYS A 38 22.468 17.426 77.141 1.00 78.08 C ANISOU 29 CA LYS A 38 13320 8467 7881 2166 -1990 381 C ATOM 30 C LYS A 38 22.968 16.390 76.139 1.00 81.45 C ANISOU 30 C LYS A 38 13790 8749 8407 2319 -2013 422 C ATOM 31 O LYS A 38 23.855 16.667 75.331 1.00 80.57 O ANISOU 31 O LYS A 38 13375 8740 8497 2454 -2101 330 O ATOM 32 CB LYS A 38 23.268 17.335 78.440 1.00 83.27 C ANISOU 32 CB LYS A 38 14151 9170 8317 2390 -2229 396 C ATOM 33 CG LYS A 38 22.847 18.340 79.500 1.00 95.90 C ANISOU 33 CG LYS A 38 15730 10915 9793 2260 -2222 340 C ATOM 34 CD LYS A 38 23.920 18.503 80.564 1.00107.33 C ANISOU 34 CD LYS A 38 17222 12475 11086 2512 -2514 300 C ATOM 35 CE LYS A 38 23.442 17.992 81.913 1.00120.82 C ANISOU 35 CE LYS A 38 19383 14095 12428 2515 -2522 417 C ATOM 36 NZ LYS A 38 24.517 18.052 82.942 1.00132.66 N ANISOU 36 NZ LYS A 38 20955 15699 13749 2789 -2835 384 N ATOM 37 N ILE A 39 22.385 15.197 76.199 1.00 78.10 N ANISOU 37 N ILE A 39 13752 8084 7840 2290 -1920 554 N ATOM 38 CA ILE A 39 22.719 14.115 75.267 1.00 77.93 C ANISOU 38 CA ILE A 39 13830 7886 7896 2419 -1921 592 C ATOM 39 C ILE A 39 21.985 14.109 73.910 1.00 78.16 C ANISOU 39 C ILE A 39 13699 7875 8122 2207 -1709 553 C ATOM 40 O ILE A 39 22.630 13.893 72.882 1.00 77.28 O ANISOU 40 O ILE A 39 13417 7770 8175 2338 -1746 494 O ATOM 41 CB ILE A 39 22.602 12.781 76.079 1.00 84.13 C ANISOU 41 CB ILE A 39 15146 8403 8415 2527 -1961 755 C ATOM 42 CG1 ILE A 39 23.567 12.770 77.300 1.00 87.07 C ANISOU 42 CG1 ILE A 39 15651 8835 8597 2810 -2226 784 C ATOM 43 CG2 ILE A 39 22.843 11.534 75.208 1.00 85.69 C ANISOU 43 CG2 ILE A 39 15524 8364 8670 2657 -1952 801 C ATOM 44 CD1 ILE A 39 22.945 13.206 78.627 1.00 94.02 C ANISOU 44 CD1 ILE A 39 16726 9765 9234 2671 -2198 840 C ATOM 45 N PHE A 40 20.660 14.395 73.902 1.00 72.34 N ANISOU 45 N PHE A 40 12997 7121 7370 1887 -1492 573 N ATOM 46 CA PHE A 40 19.848 14.461 72.681 1.00 69.55 C ANISOU 46 CA PHE A 40 12489 6751 7188 1669 -1302 530 C ATOM 47 C PHE A 40 20.268 15.644 71.795 1.00 68.83 C ANISOU 47 C PHE A 40 11926 6892 7333 1669 -1320 399 C ATOM 48 O PHE A 40 20.824 15.424 70.719 1.00 67.87 O ANISOU 48 O PHE A 40 11660 6771 7355 1773 -1341 352 O ATOM 49 CB PHE A 40 18.343 14.560 73.007 1.00 71.10 C ANISOU 49 CB PHE A 40 12803 6903 7309 1337 -1084 571 C ATOM 50 CG PHE A 40 17.682 13.315 73.552 1.00 75.33 C ANISOU 50 CG PHE A 40 13795 7180 7648 1250 -992 702 C ATOM 51 CD1 PHE A 40 17.399 13.195 74.906 1.00 80.74 C ANISOU 51 CD1 PHE A 40 14757 7823 8097 1216 -985 793 C ATOM 52 CD2 PHE A 40 17.292 12.285 72.702 1.00 78.37 C ANISOU 52 CD2 PHE A 40 14342 7358 8078 1179 -898 731 C ATOM 53 CE1 PHE A 40 16.766 12.053 75.408 1.00 84.23 C ANISOU 53 CE1 PHE A 40 15638 8014 8352 1112 -878 927 C ATOM 54 CE2 PHE A 40 16.663 11.140 73.204 1.00 83.73 C ANISOU 54 CE2 PHE A 40 15453 7776 8584 1071 -801 853 C ATOM 55 CZ PHE A 40 16.404 11.032 74.553 1.00 83.83 C ANISOU 55 CZ PHE A 40 15743 7744 8365 1034 -785 957 C ATOM 56 N LEU A 41 20.021 16.887 72.265 1.00 62.57 N ANISOU 56 N LEU A 41 10913 6288 6574 1556 -1306 341 N ATOM 57 CA LEU A 41 20.302 18.142 71.561 1.00 59.65 C ANISOU 57 CA LEU A 41 10122 6125 6419 1520 -1307 229 C ATOM 58 C LEU A 41 21.738 18.346 71.030 1.00 63.00 C ANISOU 58 C LEU A 41 10307 6653 6979 1762 -1468 159 C ATOM 59 O LEU A 41 21.850 18.626 69.837 1.00 61.28 O ANISOU 59 O LEU A 41 9859 6489 6937 1731 -1404 108 O ATOM 60 CB LEU A 41 19.803 19.385 72.332 1.00 58.72 C ANISOU 60 CB LEU A 41 9863 6156 6292 1373 -1276 179 C ATOM 61 CG LEU A 41 18.330 19.426 72.758 1.00 62.71 C ANISOU 61 CG LEU A 41 10513 6612 6702 1114 -1088 217 C ATOM 62 CD1 LEU A 41 18.043 20.654 73.593 1.00 62.15 C ANISOU 62 CD1 LEU A 41 10304 6694 6617 1028 -1084 149 C ATOM 63 CD2 LEU A 41 17.401 19.380 71.570 1.00 63.39 C ANISOU 63 CD2 LEU A 41 10492 6668 6927 927 -917 206 C ATOM 64 N PRO A 42 22.841 18.216 71.825 1.00 60.67 N ANISOU 64 N PRO A 42 10045 6397 6609 2001 -1672 149 N ATOM 65 CA PRO A 42 24.185 18.422 71.246 1.00 60.55 C ANISOU 65 CA PRO A 42 9755 6501 6749 2217 -1808 65 C ATOM 66 C PRO A 42 24.567 17.429 70.147 1.00 64.16 C ANISOU 66 C PRO A 42 10252 6851 7276 2347 -1779 77 C ATOM 67 O PRO A 42 25.394 17.766 69.304 1.00 63.16 O ANISOU 67 O PRO A 42 9835 6844 7320 2443 -1804 -4 O ATOM 68 CB PRO A 42 25.113 18.316 72.456 1.00 64.58 C ANISOU 68 CB PRO A 42 10348 7059 7131 2443 -2040 59 C ATOM 69 CG PRO A 42 24.373 17.475 73.402 1.00 70.45 C ANISOU 69 CG PRO A 42 11524 7622 7622 2415 -2022 180 C ATOM 70 CD PRO A 42 22.945 17.887 73.261 1.00 64.14 C ANISOU 70 CD PRO A 42 10761 6791 6819 2093 -1792 207 C ATOM 71 N THR A 43 23.960 16.221 70.146 1.00 61.36 N ANISOU 71 N THR A 43 10256 6268 6788 2340 -1716 172 N ATOM 72 CA THR A 43 24.187 15.203 69.117 1.00 61.53 C ANISOU 72 CA THR A 43 10364 6154 6859 2448 -1676 177 C ATOM 73 C THR A 43 23.520 15.670 67.815 1.00 63.27 C ANISOU 73 C THR A 43 10378 6428 7235 2233 -1489 128 C ATOM 74 O THR A 43 24.181 15.703 66.774 1.00 63.01 O ANISOU 74 O THR A 43 10137 6466 7339 2334 -1482 59 O ATOM 75 CB THR A 43 23.704 13.822 69.592 1.00 68.81 C ANISOU 75 CB THR A 43 11757 6796 7591 2484 -1666 291 C ATOM 76 OG1 THR A 43 24.383 13.481 70.801 1.00 70.62 O ANISOU 76 OG1 THR A 43 12174 6991 7666 2705 -1857 343 O ATOM 77 CG2 THR A 43 23.930 12.729 68.550 1.00 66.82 C ANISOU 77 CG2 THR A 43 11622 6378 7389 2602 -1629 282 C ATOM 78 N ILE A 44 22.225 16.065 67.894 1.00 57.79 N ANISOU 78 N ILE A 44 9730 5716 6513 1945 -1342 160 N ATOM 79 CA ILE A 44 21.434 16.557 66.759 1.00 55.27 C ANISOU 79 CA ILE A 44 9232 5451 6319 1730 -1179 122 C ATOM 80 C ILE A 44 22.054 17.847 66.186 1.00 57.51 C ANISOU 80 C ILE A 44 9106 5966 6780 1740 -1195 38 C ATOM 81 O ILE A 44 22.172 17.958 64.966 1.00 56.30 O ANISOU 81 O ILE A 44 8791 5859 6741 1727 -1124 -5 O ATOM 82 CB ILE A 44 19.902 16.651 67.076 1.00 57.41 C ANISOU 82 CB ILE A 44 9638 5657 6519 1438 -1033 168 C ATOM 83 CG1 ILE A 44 19.377 15.304 67.653 1.00 59.58 C ANISOU 83 CG1 ILE A 44 10336 5685 6618 1418 -1006 258 C ATOM 84 CG2 ILE A 44 19.097 17.034 65.821 1.00 56.33 C ANISOU 84 CG2 ILE A 44 9328 5570 6506 1246 -891 124 C ATOM 85 CD1 ILE A 44 18.143 15.383 68.572 1.00 66.98 C ANISOU 85 CD1 ILE A 44 11443 6574 7434 1177 -898 316 C ATOM 86 N TYR A 45 22.536 18.765 67.063 1.00 53.74 N ANISOU 86 N TYR A 45 8478 5624 6316 1774 -1293 11 N ATOM 87 CA TYR A 45 23.206 20.010 66.653 1.00 52.27 C ANISOU 87 CA TYR A 45 7919 5641 6302 1775 -1316 -69 C ATOM 88 C TYR A 45 24.544 19.752 65.945 1.00 56.70 C ANISOU 88 C TYR A 45 8308 6270 6965 1997 -1389 -125 C ATOM 89 O TYR A 45 24.858 20.451 64.975 1.00 55.15 O ANISOU 89 O TYR A 45 7841 6194 6921 1954 -1321 -175 O ATOM 90 CB TYR A 45 23.376 20.986 67.839 1.00 53.40 C ANISOU 90 CB TYR A 45 7969 5892 6426 1750 -1411 -99 C ATOM 91 CG TYR A 45 22.074 21.555 68.370 1.00 53.76 C ANISOU 91 CG TYR A 45 8092 5920 6414 1516 -1308 -73 C ATOM 92 CD1 TYR A 45 21.044 21.921 67.510 1.00 54.17 C ANISOU 92 CD1 TYR A 45 8074 5965 6542 1316 -1145 -65 C ATOM 93 CD2 TYR A 45 21.893 21.772 69.736 1.00 55.12 C ANISOU 93 CD2 TYR A 45 8392 6097 6453 1505 -1379 -66 C ATOM 94 CE1 TYR A 45 19.842 22.434 67.994 1.00 54.33 C ANISOU 94 CE1 TYR A 45 8141 5982 6521 1117 -1050 -54 C ATOM 95 CE2 TYR A 45 20.694 22.288 70.232 1.00 55.11 C ANISOU 95 CE2 TYR A 45 8451 6090 6397 1298 -1268 -55 C ATOM 96 CZ TYR A 45 19.673 22.622 69.356 1.00 60.32 C ANISOU 96 CZ TYR A 45 9023 6744 7151 1108 -1103 -52 C ATOM 97 OH TYR A 45 18.491 23.144 69.824 1.00 58.99 O ANISOU 97 OH TYR A 45 8884 6583 6945 919 -993 -55 O ATOM 98 N SER A 46 25.305 18.727 66.410 1.00 55.03 N ANISOU 98 N SER A 46 8266 5979 6665 2238 -1519 -114 N ATOM 99 CA SER A 46 26.594 18.308 65.843 1.00 55.97 C ANISOU 99 CA SER A 46 8243 6155 6868 2489 -1597 -177 C ATOM 100 C SER A 46 26.434 17.738 64.440 1.00 59.10 C ANISOU 100 C SER A 46 8644 6492 7320 2482 -1457 -187 C ATOM 101 O SER A 46 27.267 18.024 63.580 1.00 59.07 O ANISOU 101 O SER A 46 8378 6617 7448 2568 -1432 -260 O ATOM 102 CB SER A 46 27.272 17.273 66.737 1.00 61.63 C ANISOU 102 CB SER A 46 9188 6771 7456 2759 -1776 -153 C ATOM 103 OG SER A 46 27.738 17.851 67.944 1.00 70.96 O ANISOU 103 OG SER A 46 10308 8057 8596 2819 -1940 -170 O ATOM 104 N ILE A 47 25.375 16.928 64.212 1.00 54.97 N ANISOU 104 N ILE A 47 8416 5777 6692 2372 -1360 -123 N ATOM 105 CA ILE A 47 25.075 16.314 62.913 1.00 54.72 C ANISOU 105 CA ILE A 47 8434 5669 6687 2346 -1233 -141 C ATOM 106 C ILE A 47 24.815 17.392 61.831 1.00 56.81 C ANISOU 106 C ILE A 47 8404 6098 7083 2168 -1101 -181 C ATOM 107 O ILE A 47 25.465 17.363 60.783 1.00 56.59 O ANISOU 107 O ILE A 47 8218 6148 7137 2258 -1051 -240 O ATOM 108 CB ILE A 47 23.946 15.235 63.020 1.00 58.25 C ANISOU 108 CB ILE A 47 9268 5869 6996 2237 -1171 -72 C ATOM 109 CG1 ILE A 47 24.425 14.020 63.848 1.00 61.31 C ANISOU 109 CG1 ILE A 47 9970 6066 7258 2464 -1296 -29 C ATOM 110 CG2 ILE A 47 23.452 14.778 61.633 1.00 58.47 C ANISOU 110 CG2 ILE A 47 9325 5836 7053 2153 -1034 -109 C ATOM 111 CD1 ILE A 47 23.311 13.226 64.582 1.00 70.42 C ANISOU 111 CD1 ILE A 47 11521 6984 8251 2319 -1260 70 C ATOM 112 N ILE A 48 23.897 18.349 62.111 1.00 51.66 N ANISOU 112 N ILE A 48 7684 5499 6445 1930 -1045 -148 N ATOM 113 CA ILE A 48 23.512 19.445 61.205 1.00 49.56 C ANISOU 113 CA ILE A 48 7175 5367 6289 1754 -932 -166 C ATOM 114 C ILE A 48 24.690 20.380 60.884 1.00 53.43 C ANISOU 114 C ILE A 48 7330 6049 6922 1839 -955 -222 C ATOM 115 O ILE A 48 24.833 20.778 59.728 1.00 52.66 O ANISOU 115 O ILE A 48 7070 6036 6904 1797 -853 -244 O ATOM 116 CB ILE A 48 22.226 20.193 61.671 1.00 50.99 C ANISOU 116 CB ILE A 48 7380 5544 6452 1507 -879 -123 C ATOM 117 CG1 ILE A 48 21.083 19.197 61.945 1.00 51.46 C ANISOU 117 CG1 ILE A 48 7753 5421 6378 1406 -837 -76 C ATOM 118 CG2 ILE A 48 21.776 21.252 60.644 1.00 50.10 C ANISOU 118 CG2 ILE A 48 7046 5545 6445 1349 -771 -132 C ATOM 119 CD1 ILE A 48 20.214 19.569 63.072 1.00 57.20 C ANISOU 119 CD1 ILE A 48 8568 6125 7043 1262 -839 -38 C ATOM 120 N PHE A 49 25.545 20.703 61.881 1.00 50.46 N ANISOU 120 N PHE A 49 6856 5743 6574 1953 -1086 -249 N ATOM 121 CA PHE A 49 26.729 21.542 61.654 1.00 50.35 C ANISOU 121 CA PHE A 49 6511 5912 6707 2024 -1114 -317 C ATOM 122 C PHE A 49 27.737 20.824 60.745 1.00 55.90 C ANISOU 122 C PHE A 49 7133 6654 7452 2224 -1091 -371 C ATOM 123 O PHE A 49 28.299 21.460 59.854 1.00 55.53 O ANISOU 123 O PHE A 49 6831 6745 7524 2198 -1002 -411 O ATOM 124 CB PHE A 49 27.388 21.988 62.982 1.00 52.64 C ANISOU 124 CB PHE A 49 6719 6271 7010 2101 -1282 -352 C ATOM 125 CG PHE A 49 28.821 22.475 62.873 1.00 55.02 C ANISOU 125 CG PHE A 49 6700 6750 7456 2230 -1349 -443 C ATOM 126 CD1 PHE A 49 29.871 21.709 63.359 1.00 60.06 C ANISOU 126 CD1 PHE A 49 7334 7412 8074 2493 -1500 -495 C ATOM 127 CD2 PHE A 49 29.119 23.688 62.264 1.00 56.06 C ANISOU 127 CD2 PHE A 49 6531 7022 7748 2088 -1259 -478 C ATOM 128 CE1 PHE A 49 31.192 22.151 63.246 1.00 62.36 C ANISOU 128 CE1 PHE A 49 7293 7887 8512 2608 -1560 -595 C ATOM 129 CE2 PHE A 49 30.439 24.129 62.153 1.00 60.23 C ANISOU 129 CE2 PHE A 49 6748 7718 8421 2181 -1304 -569 C ATOM 130 CZ PHE A 49 31.466 23.357 62.642 1.00 60.53 C ANISOU 130 CZ PHE A 49 6754 7800 8447 2438 -1454 -635 C ATOM 131 N LEU A 50 27.960 19.510 60.968 1.00 53.66 N ANISOU 131 N LEU A 50 7077 6244 7067 2424 -1163 -373 N ATOM 132 CA LEU A 50 28.911 18.720 60.185 1.00 54.97 C ANISOU 132 CA LEU A 50 7191 6432 7264 2649 -1149 -438 C ATOM 133 C LEU A 50 28.420 18.409 58.771 1.00 58.64 C ANISOU 133 C LEU A 50 7704 6860 7716 2571 -973 -440 C ATOM 134 O LEU A 50 29.178 18.587 57.815 1.00 59.05 O ANISOU 134 O LEU A 50 7543 7041 7852 2639 -888 -503 O ATOM 135 CB LEU A 50 29.339 17.452 60.938 1.00 56.89 C ANISOU 135 CB LEU A 50 7674 6535 7407 2911 -1299 -441 C ATOM 136 CG LEU A 50 30.736 16.910 60.623 1.00 63.98 C ANISOU 136 CG LEU A 50 8416 7518 8375 3216 -1362 -537 C ATOM 137 CD1 LEU A 50 31.828 17.926 60.957 1.00 64.80 C ANISOU 137 CD1 LEU A 50 8127 7867 8628 3261 -1436 -612 C ATOM 138 CD2 LEU A 50 30.998 15.629 61.382 1.00 68.79 C ANISOU 138 CD2 LEU A 50 9317 7949 8869 3479 -1519 -521 C ATOM 139 N THR A 51 27.149 17.986 58.630 1.00 53.92 N ANISOU 139 N THR A 51 7375 6102 7012 2418 -915 -378 N ATOM 140 CA THR A 51 26.550 17.684 57.324 1.00 52.92 C ANISOU 140 CA THR A 51 7317 5937 6854 2327 -769 -386 C ATOM 141 C THR A 51 26.140 18.966 56.564 1.00 55.28 C ANISOU 141 C THR A 51 7392 6384 7226 2109 -650 -366 C ATOM 142 O THR A 51 25.908 18.913 55.356 1.00 54.97 O ANISOU 142 O THR A 51 7343 6371 7171 2058 -531 -382 O ATOM 143 CB THR A 51 25.419 16.658 57.453 1.00 58.81 C ANISOU 143 CB THR A 51 8424 6454 7465 2253 -765 -345 C ATOM 144 OG1 THR A 51 24.367 17.217 58.236 1.00 57.81 O ANISOU 144 OG1 THR A 51 8361 6294 7310 2037 -779 -273 O ATOM 145 CG2 THR A 51 25.883 15.334 58.059 1.00 58.30 C ANISOU 145 CG2 THR A 51 8613 6214 7324 2484 -870 -357 C ATOM 146 N GLY A 52 26.076 20.091 57.278 1.00 50.73 N ANISOU 146 N GLY A 52 6656 5896 6723 1992 -689 -333 N ATOM 147 CA GLY A 52 25.739 21.398 56.725 1.00 49.12 C ANISOU 147 CA GLY A 52 6251 5811 6600 1799 -595 -305 C ATOM 148 C GLY A 52 26.953 22.154 56.224 1.00 53.68 C ANISOU 148 C GLY A 52 6520 6570 7308 1856 -548 -349 C ATOM 149 O GLY A 52 26.884 22.784 55.167 1.00 53.00 O ANISOU 149 O GLY A 52 6316 6566 7258 1755 -420 -333 O ATOM 150 N ILE A 53 28.077 22.102 56.982 1.00 51.37 N ANISOU 150 N ILE A 53 6092 6343 7082 2015 -652 -406 N ATOM 151 CA ILE A 53 29.346 22.747 56.615 1.00 52.08 C ANISOU 151 CA ILE A 53 5858 6616 7312 2074 -613 -468 C ATOM 152 C ILE A 53 29.898 22.103 55.341 1.00 57.18 C ANISOU 152 C ILE A 53 6470 7313 7942 2193 -486 -514 C ATOM 153 O ILE A 53 30.386 22.812 54.460 1.00 56.87 O ANISOU 153 O ILE A 53 6214 7412 7983 2125 -351 -525 O ATOM 154 CB ILE A 53 30.352 22.775 57.811 1.00 56.32 C ANISOU 154 CB ILE A 53 6260 7219 7921 2221 -784 -533 C ATOM 155 CG1 ILE A 53 30.466 24.181 58.440 1.00 55.95 C ANISOU 155 CG1 ILE A 53 6000 7266 7994 2052 -819 -533 C ATOM 156 CG2 ILE A 53 31.729 22.142 57.508 1.00 59.63 C ANISOU 156 CG2 ILE A 53 6510 7747 8400 2472 -802 -634 C ATOM 157 CD1 ILE A 53 31.203 25.260 57.610 1.00 63.76 C ANISOU 157 CD1 ILE A 53 6663 8420 9144 1943 -686 -562 C ATOM 158 N VAL A 54 29.783 20.759 55.240 1.00 54.67 N ANISOU 158 N VAL A 54 6386 6873 7513 2362 -519 -540 N ATOM 159 CA VAL A 54 30.216 19.992 54.075 1.00 55.60 C ANISOU 159 CA VAL A 54 6522 7012 7592 2495 -405 -599 C ATOM 160 C VAL A 54 29.176 20.206 52.961 1.00 57.76 C ANISOU 160 C VAL A 54 6914 7252 7781 2304 -260 -544 C ATOM 161 O VAL A 54 29.539 20.706 51.897 1.00 58.00 O ANISOU 161 O VAL A 54 6786 7414 7839 2260 -111 -556 O ATOM 162 CB VAL A 54 30.491 18.498 54.407 1.00 60.80 C ANISOU 162 CB VAL A 54 7402 7529 8169 2755 -504 -656 C ATOM 163 CG1 VAL A 54 30.816 17.695 53.150 1.00 61.83 C ANISOU 163 CG1 VAL A 54 7581 7664 8249 2887 -375 -731 C ATOM 164 CG2 VAL A 54 31.622 18.366 55.424 1.00 62.34 C ANISOU 164 CG2 VAL A 54 7449 7789 8449 2971 -659 -713 C ATOM 165 N GLY A 55 27.907 19.903 53.252 1.00 52.17 N ANISOU 165 N GLY A 55 6465 6382 6974 2184 -305 -483 N ATOM 166 CA GLY A 55 26.789 20.064 52.328 1.00 50.52 C ANISOU 166 CA GLY A 55 6378 6136 6681 2004 -208 -437 C ATOM 167 C GLY A 55 26.708 21.423 51.657 1.00 52.96 C ANISOU 167 C GLY A 55 6480 6591 7053 1831 -100 -383 C ATOM 168 O GLY A 55 27.036 21.541 50.473 1.00 53.12 O ANISOU 168 O GLY A 55 6429 6706 7047 1838 32 -399 O ATOM 169 N ASN A 56 26.261 22.462 52.405 1.00 47.90 N ANISOU 169 N ASN A 56 5757 5960 6485 1677 -151 -317 N ATOM 170 CA ASN A 56 26.115 23.846 51.914 1.00 46.48 C ANISOU 170 CA ASN A 56 5404 5883 6376 1506 -65 -252 C ATOM 171 C ASN A 56 27.448 24.462 51.475 1.00 50.61 C ANISOU 171 C ASN A 56 5654 6567 7008 1554 29 -281 C ATOM 172 O ASN A 56 27.454 25.359 50.629 1.00 50.30 O ANISOU 172 O ASN A 56 5510 6609 6993 1436 150 -228 O ATOM 173 CB ASN A 56 25.426 24.749 52.946 1.00 45.15 C ANISOU 173 CB ASN A 56 5215 5670 6271 1361 -151 -197 C ATOM 174 CG ASN A 56 24.074 24.259 53.401 1.00 67.05 C ANISOU 174 CG ASN A 56 8222 8305 8949 1287 -220 -169 C ATOM 175 OD1 ASN A 56 23.060 24.405 52.706 1.00 61.90 O ANISOU 175 OD1 ASN A 56 7658 7628 8233 1173 -173 -128 O ATOM 176 ND2 ASN A 56 24.030 23.684 54.595 1.00 57.77 N ANISOU 176 ND2 ASN A 56 7148 7045 7757 1348 -333 -192 N ATOM 177 N GLY A 57 28.551 23.968 52.045 1.00 47.37 N ANISOU 177 N GLY A 57 5135 6203 6662 1727 -28 -364 N ATOM 178 CA GLY A 57 29.901 24.411 51.723 1.00 48.21 C ANISOU 178 CA GLY A 57 4953 6477 6886 1786 54 -418 C ATOM 179 C GLY A 57 30.252 24.120 50.281 1.00 51.30 C ANISOU 179 C GLY A 57 5326 6953 7212 1828 237 -437 C ATOM 180 O GLY A 57 30.713 25.015 49.565 1.00 51.37 O ANISOU 180 O GLY A 57 5150 7088 7281 1725 383 -409 O ATOM 181 N LEU A 58 29.989 22.868 49.843 1.00 46.65 N ANISOU 181 N LEU A 58 4950 6286 6488 1970 235 -484 N ATOM 182 CA LEU A 58 30.233 22.403 48.477 1.00 46.91 C ANISOU 182 CA LEU A 58 5016 6384 6422 2034 399 -523 C ATOM 183 C LEU A 58 29.425 23.203 47.460 1.00 48.73 C ANISOU 183 C LEU A 58 5304 6639 6571 1829 522 -423 C ATOM 184 O LEU A 58 29.972 23.546 46.412 1.00 49.45 O ANISOU 184 O LEU A 58 5286 6863 6639 1815 696 -424 O ATOM 185 CB LEU A 58 29.910 20.907 48.316 1.00 47.28 C ANISOU 185 CB LEU A 58 5330 6299 6336 2206 347 -597 C ATOM 186 CG LEU A 58 30.833 19.895 48.984 1.00 53.06 C ANISOU 186 CG LEU A 58 6043 7004 7115 2470 254 -706 C ATOM 187 CD1 LEU A 58 30.096 18.609 49.243 1.00 52.77 C ANISOU 187 CD1 LEU A 58 6343 6751 6957 2566 148 -731 C ATOM 188 CD2 LEU A 58 32.090 19.647 48.160 1.00 57.56 C ANISOU 188 CD2 LEU A 58 6415 7740 7717 2643 397 -812 C ATOM 189 N VAL A 59 28.138 23.516 47.774 1.00 42.50 N ANISOU 189 N VAL A 59 4682 5731 5736 1678 433 -338 N ATOM 190 CA VAL A 59 27.235 24.267 46.885 1.00 41.16 C ANISOU 190 CA VAL A 59 4585 5570 5484 1502 509 -239 C ATOM 191 C VAL A 59 27.825 25.630 46.512 1.00 45.26 C ANISOU 191 C VAL A 59 4880 6217 6102 1380 634 -164 C ATOM 192 O VAL A 59 28.116 25.842 45.338 1.00 45.67 O ANISOU 192 O VAL A 59 4911 6365 6076 1362 795 -141 O ATOM 193 CB VAL A 59 25.756 24.334 47.362 1.00 42.82 C ANISOU 193 CB VAL A 59 4983 5641 5645 1379 381 -178 C ATOM 194 CG1 VAL A 59 24.883 25.062 46.346 1.00 42.14 C ANISOU 194 CG1 VAL A 59 4961 5581 5468 1234 448 -86 C ATOM 195 CG2 VAL A 59 25.195 22.940 47.612 1.00 42.45 C ANISOU 195 CG2 VAL A 59 5170 5463 5497 1473 287 -252 C ATOM 196 N ILE A 60 28.066 26.508 47.508 1.00 41.68 N ANISOU 196 N ILE A 60 4266 5759 5812 1300 568 -134 N ATOM 197 CA ILE A 60 28.664 27.846 47.348 1.00 42.40 C ANISOU 197 CA ILE A 60 4139 5939 6029 1165 672 -70 C ATOM 198 C ILE A 60 29.973 27.792 46.521 1.00 49.86 C ANISOU 198 C ILE A 60 4898 7050 6998 1227 858 -120 C ATOM 199 O ILE A 60 30.174 28.612 45.615 1.00 49.99 O ANISOU 199 O ILE A 60 4853 7140 7002 1108 1025 -41 O ATOM 200 CB ILE A 60 28.841 28.515 48.752 1.00 44.48 C ANISOU 200 CB ILE A 60 4266 6163 6470 1107 538 -80 C ATOM 201 CG1 ILE A 60 27.477 28.963 49.320 1.00 42.31 C ANISOU 201 CG1 ILE A 60 4154 5748 6172 993 417 -5 C ATOM 202 CG2 ILE A 60 29.837 29.687 48.730 1.00 46.70 C ANISOU 202 CG2 ILE A 60 4278 6546 6920 995 641 -64 C ATOM 203 CD1 ILE A 60 27.304 28.761 50.801 1.00 44.44 C ANISOU 203 CD1 ILE A 60 4432 5942 6510 1028 238 -58 C ATOM 204 N LEU A 61 30.827 26.794 46.822 1.00 48.81 N ANISOU 204 N LEU A 61 4688 6970 6888 1421 832 -249 N ATOM 205 CA LEU A 61 32.109 26.543 46.164 1.00 51.53 C ANISOU 205 CA LEU A 61 4834 7482 7263 1523 996 -332 C ATOM 206 C LEU A 61 31.922 26.183 44.679 1.00 57.47 C ANISOU 206 C LEU A 61 5724 8286 7824 1540 1178 -313 C ATOM 207 O LEU A 61 32.518 26.839 43.821 1.00 58.32 O ANISOU 207 O LEU A 61 5698 8525 7936 1455 1382 -277 O ATOM 208 CB LEU A 61 32.869 25.430 46.923 1.00 52.41 C ANISOU 208 CB LEU A 61 4875 7608 7429 1767 880 -480 C ATOM 209 CG LEU A 61 34.358 25.270 46.638 1.00 59.59 C ANISOU 209 CG LEU A 61 5491 8710 8441 1893 1006 -596 C ATOM 210 CD1 LEU A 61 35.173 26.371 47.309 1.00 60.53 C ANISOU 210 CD1 LEU A 61 5286 8933 8780 1770 1003 -600 C ATOM 211 CD2 LEU A 61 34.842 23.912 47.097 1.00 62.45 C ANISOU 211 CD2 LEU A 61 5885 9053 8791 2183 890 -736 C ATOM 212 N VAL A 62 31.074 25.168 44.387 1.00 54.33 N ANISOU 212 N VAL A 62 5603 7783 7255 1635 1106 -338 N ATOM 213 CA VAL A 62 30.773 24.682 43.035 1.00 55.53 C ANISOU 213 CA VAL A 62 5930 7971 7200 1667 1241 -343 C ATOM 214 C VAL A 62 30.030 25.730 42.187 1.00 61.13 C ANISOU 214 C VAL A 62 6724 8690 7812 1462 1332 -190 C ATOM 215 O VAL A 62 30.385 25.904 41.021 1.00 62.73 O ANISOU 215 O VAL A 62 6924 9009 7900 1446 1526 -170 O ATOM 216 CB VAL A 62 30.094 23.284 43.050 1.00 58.65 C ANISOU 216 CB VAL A 62 6593 8234 7456 1816 1120 -431 C ATOM 217 CG1 VAL A 62 29.518 22.915 41.689 1.00 59.10 C ANISOU 217 CG1 VAL A 62 6864 8309 7284 1807 1225 -430 C ATOM 218 CG2 VAL A 62 31.066 22.207 43.521 1.00 59.83 C ANISOU 218 CG2 VAL A 62 6667 8396 7671 2059 1088 -585 C ATOM 219 N MET A 63 29.041 26.448 42.774 1.00 57.08 N ANISOU 219 N MET A 63 6283 8061 7342 1316 1197 -83 N ATOM 220 CA MET A 63 28.273 27.506 42.088 1.00 57.23 C ANISOU 220 CA MET A 63 6390 8070 7287 1140 1249 71 C ATOM 221 C MET A 63 29.184 28.614 41.530 1.00 65.66 C ANISOU 221 C MET A 63 7268 9259 8420 1028 1456 152 C ATOM 222 O MET A 63 28.928 29.119 40.437 1.00 66.47 O ANISOU 222 O MET A 63 7469 9404 8381 948 1584 255 O ATOM 223 CB MET A 63 27.214 28.135 43.013 1.00 57.00 C ANISOU 223 CB MET A 63 6416 7900 7340 1025 1067 150 C ATOM 224 CG MET A 63 26.059 27.224 43.351 1.00 58.76 C ANISOU 224 CG MET A 63 6854 8003 7468 1077 892 103 C ATOM 225 SD MET A 63 24.876 27.010 42.012 1.00 62.76 S ANISOU 225 SD MET A 63 7618 8505 7723 1043 903 154 S ATOM 226 CE MET A 63 23.616 26.154 42.868 1.00 57.43 C ANISOU 226 CE MET A 63 7108 7678 7035 1054 683 91 C ATOM 227 N GLY A 64 30.227 28.968 42.282 1.00 64.44 N ANISOU 227 N GLY A 64 6852 9159 8474 1019 1484 105 N ATOM 228 CA GLY A 64 31.193 29.986 41.890 1.00 66.87 C ANISOU 228 CA GLY A 64 6945 9579 8882 892 1684 162 C ATOM 229 C GLY A 64 32.148 29.532 40.802 1.00 74.88 C ANISOU 229 C GLY A 64 7885 10768 9797 969 1923 103 C ATOM 230 O GLY A 64 32.541 30.341 39.956 1.00 76.28 O ANISOU 230 O GLY A 64 8012 11029 9941 837 2135 200 O ATOM 231 N TYR A 65 32.522 28.230 40.814 1.00 73.02 N ANISOU 231 N TYR A 65 7654 10582 9508 1185 1896 -55 N ATOM 232 CA TYR A 65 33.452 27.602 39.866 1.00 76.18 C ANISOU 232 CA TYR A 65 7978 11152 9815 1307 2112 -153 C ATOM 233 C TYR A 65 33.013 27.671 38.400 1.00 83.19 C ANISOU 233 C TYR A 65 9082 12089 10439 1260 2286 -70 C ATOM 234 O TYR A 65 33.869 27.636 37.512 1.00 85.63 O ANISOU 234 O TYR A 65 9294 12564 10680 1282 2532 -104 O ATOM 235 CB TYR A 65 33.771 26.156 40.278 1.00 77.61 C ANISOU 235 CB TYR A 65 8167 11329 9993 1571 2006 -341 C ATOM 236 CG TYR A 65 35.217 25.773 40.060 1.00 82.28 C ANISOU 236 CG TYR A 65 8482 12112 10670 1707 2178 -483 C ATOM 237 CD1 TYR A 65 36.150 25.876 41.090 1.00 84.76 C ANISOU 237 CD1 TYR A 65 8491 12484 11229 1759 2109 -570 C ATOM 238 CD2 TYR A 65 35.655 25.288 38.831 1.00 85.39 C ANISOU 238 CD2 TYR A 65 8911 12641 10893 1796 2405 -545 C ATOM 239 CE1 TYR A 65 37.484 25.520 40.897 1.00 88.06 C ANISOU 239 CE1 TYR A 65 8622 13096 11739 1897 2259 -716 C ATOM 240 CE2 TYR A 65 36.986 24.936 38.624 1.00 89.11 C ANISOU 240 CE2 TYR A 65 9105 13303 11449 1931 2577 -690 C ATOM 241 CZ TYR A 65 37.897 25.051 39.661 1.00 96.41 C ANISOU 241 CZ TYR A 65 9706 14289 12637 1984 2500 -776 C ATOM 242 OH TYR A 65 39.208 24.702 39.454 1.00 99.18 O ANISOU 242 OH TYR A 65 9755 14846 13083 2128 2663 -931 O ATOM 243 N GLN A 66 31.695 27.777 38.142 1.00 79.28 N ANISOU 243 N GLN A 66 8871 11462 9789 1199 2162 33 N ATOM 244 CA GLN A 66 31.163 27.889 36.781 1.00 80.69 C ANISOU 244 CA GLN A 66 9279 11683 9698 1156 2286 120 C ATOM 245 C GLN A 66 29.978 28.858 36.662 1.00 83.63 C ANISOU 245 C GLN A 66 9831 11936 10008 990 2184 309 C ATOM 246 O GLN A 66 29.171 28.966 37.588 1.00 80.69 O ANISOU 246 O GLN A 66 9499 11419 9740 963 1959 329 O ATOM 247 CB GLN A 66 30.883 26.508 36.138 1.00 82.68 C ANISOU 247 CB GLN A 66 9732 11949 9732 1347 2266 -22 C ATOM 248 CG GLN A 66 29.654 25.749 36.660 1.00 98.30 C ANISOU 248 CG GLN A 66 11934 13754 11663 1406 1992 -65 C ATOM 249 CD GLN A 66 29.869 25.064 37.987 1.00118.60 C ANISOU 249 CD GLN A 66 14398 16230 14435 1514 1820 -182 C ATOM 250 OE1 GLN A 66 30.914 24.453 38.247 1.00116.52 O ANISOU 250 OE1 GLN A 66 13975 16036 14262 1661 1885 -313 O ATOM 251 NE2 GLN A 66 28.862 25.126 38.846 1.00108.24 N ANISOU 251 NE2 GLN A 66 13182 14759 13185 1455 1596 -138 N ATOM 252 N LYS A 67 29.900 29.573 35.528 1.00 82.29 N ANISOU 252 N LYS A 67 9768 11831 9666 888 2354 447 N ATOM 253 CA LYS A 67 28.839 30.535 35.230 1.00 81.52 C ANISOU 253 CA LYS A 67 9856 11634 9485 754 2274 638 C ATOM 254 C LYS A 67 27.952 30.013 34.096 1.00 86.30 C ANISOU 254 C LYS A 67 10760 12262 9769 821 2244 652 C ATOM 255 O LYS A 67 26.784 30.398 34.014 1.00 84.82 O ANISOU 255 O LYS A 67 10748 11976 9502 776 2078 753 O ATOM 256 CB LYS A 67 29.443 31.904 34.866 1.00 85.90 C ANISOU 256 CB LYS A 67 10317 12222 10100 572 2480 811 C ATOM 257 CG LYS A 67 28.508 33.090 35.117 1.00 99.06 C ANISOU 257 CG LYS A 67 12091 13731 11816 433 2353 1000 C ATOM 258 CD LYS A 67 28.380 33.999 33.896 1.00110.79 C ANISOU 258 CD LYS A 67 13754 15240 13100 326 2522 1204 C ATOM 259 CE LYS A 67 27.212 33.638 33.008 1.00120.17 C ANISOU 259 CE LYS A 67 15251 16419 13987 410 2403 1252 C ATOM 260 NZ LYS A 67 27.213 34.433 31.754 1.00130.94 N ANISOU 260 NZ LYS A 67 16804 17827 15120 330 2581 1449 N ATOM 261 N LYS A 68 28.508 29.131 33.233 1.00 85.12 N ANISOU 261 N LYS A 68 10659 12248 9436 938 2397 537 N ATOM 262 CA LYS A 68 27.837 28.523 32.078 1.00 86.26 C ANISOU 262 CA LYS A 68 11081 12440 9253 1013 2389 514 C ATOM 263 C LYS A 68 26.540 27.805 32.470 1.00 88.45 C ANISOU 263 C LYS A 68 11530 12588 9489 1074 2092 441 C ATOM 264 O LYS A 68 25.481 28.116 31.917 1.00 87.72 O ANISOU 264 O LYS A 68 11641 12463 9225 1031 1978 534 O ATOM 265 CB LYS A 68 28.797 27.570 31.332 1.00 91.28 C ANISOU 265 CB LYS A 68 11698 13234 9749 1150 2601 353 C ATOM 266 CG LYS A 68 28.258 27.063 29.991 1.00105.61 C ANISOU 266 CG LYS A 68 13805 15126 11197 1214 2637 330 C ATOM 267 CD LYS A 68 29.214 26.094 29.301 1.00114.99 C ANISOU 267 CD LYS A 68 14974 16465 12251 1364 2852 148 C ATOM 268 CE LYS A 68 28.568 25.366 28.142 1.00122.73 C ANISOU 268 CE LYS A 68 16262 17495 12874 1451 2830 72 C ATOM 269 NZ LYS A 68 28.334 26.256 26.973 1.00131.22 N ANISOU 269 NZ LYS A 68 17514 18669 13674 1348 2964 258 N ATOM 270 N LEU A 69 26.629 26.856 33.420 1.00 84.06 N ANISOU 270 N LEU A 69 10888 11960 9090 1171 1967 275 N ATOM 271 CA LEU A 69 25.479 26.089 33.893 1.00 82.02 C ANISOU 271 CA LEU A 69 10775 11571 8817 1211 1707 191 C ATOM 272 C LEU A 69 24.819 26.765 35.094 1.00 82.86 C ANISOU 272 C LEU A 69 10793 11540 9149 1110 1520 279 C ATOM 273 O LEU A 69 25.196 26.514 36.245 1.00 80.90 O ANISOU 273 O LEU A 69 10393 11225 9122 1136 1459 212 O ATOM 274 CB LEU A 69 25.863 24.617 34.194 1.00 82.28 C ANISOU 274 CB LEU A 69 10819 11580 8864 1375 1679 -30 C ATOM 275 CG LEU A 69 25.694 23.565 33.073 1.00 88.90 C ANISOU 275 CG LEU A 69 11878 12473 9425 1486 1721 -167 C ATOM 276 CD1 LEU A 69 24.240 23.417 32.633 1.00 88.49 C ANISOU 276 CD1 LEU A 69 12067 12357 9197 1427 1526 -151 C ATOM 277 CD2 LEU A 69 26.626 23.818 31.894 1.00 94.32 C ANISOU 277 CD2 LEU A 69 12554 13346 9937 1520 1997 -151 C ATOM 278 N ARG A 70 23.852 27.657 34.812 1.00 78.72 N ANISOU 278 N ARG A 70 10368 10980 8560 1005 1431 429 N ATOM 279 CA ARG A 70 23.115 28.393 35.836 1.00 76.23 C ANISOU 279 CA ARG A 70 9987 10541 8437 912 1261 513 C ATOM 280 C ARG A 70 21.682 28.705 35.415 1.00 78.42 C ANISOU 280 C ARG A 70 10440 10776 8581 868 1089 588 C ATOM 281 O ARG A 70 21.447 29.574 34.567 1.00 79.01 O ANISOU 281 O ARG A 70 10602 10894 8525 822 1137 735 O ATOM 282 CB ARG A 70 23.860 29.667 36.268 1.00 77.17 C ANISOU 282 CB ARG A 70 9921 10656 8745 811 1377 649 C ATOM 283 CG ARG A 70 23.909 29.854 37.776 1.00 85.40 C ANISOU 283 CG ARG A 70 10790 11590 10067 778 1260 615 C ATOM 284 CD ARG A 70 24.879 30.954 38.142 1.00 96.94 C ANISOU 284 CD ARG A 70 12053 13064 11714 683 1397 706 C ATOM 285 NE ARG A 70 25.430 30.783 39.486 1.00104.48 N ANISOU 285 NE ARG A 70 12812 13974 12913 695 1333 612 N ATOM 286 CZ ARG A 70 26.542 31.370 39.919 1.00119.70 C ANISOU 286 CZ ARG A 70 14522 15940 15021 641 1450 618 C ATOM 287 NH1 ARG A 70 27.238 32.167 39.117 1.00109.93 N ANISOU 287 NH1 ARG A 70 13231 14779 13758 552 1658 719 N ATOM 288 NH2 ARG A 70 26.972 31.158 41.156 1.00104.55 N ANISOU 288 NH2 ARG A 70 12438 13985 13302 668 1359 521 N ATOM 289 N SER A 71 20.729 27.972 36.012 1.00 72.44 N ANISOU 289 N SER A 71 9735 9935 7855 886 889 484 N ATOM 290 CA SER A 71 19.297 28.158 35.793 1.00 71.11 C ANISOU 290 CA SER A 71 9688 9732 7600 846 698 519 C ATOM 291 C SER A 71 18.801 29.151 36.842 1.00 71.15 C ANISOU 291 C SER A 71 9570 9638 7827 765 596 617 C ATOM 292 O SER A 71 19.562 29.500 37.749 1.00 69.88 O ANISOU 292 O SER A 71 9250 9432 7871 741 662 631 O ATOM 293 CB SER A 71 18.559 26.825 35.909 1.00 74.56 C ANISOU 293 CB SER A 71 10228 10131 7969 885 555 341 C ATOM 294 OG SER A 71 18.441 26.376 37.249 1.00 81.28 O ANISOU 294 OG SER A 71 10982 10870 9032 868 469 262 O ATOM 295 N MET A 72 17.543 29.604 36.736 1.00 65.80 N ANISOU 295 N MET A 72 8956 8932 7113 732 431 672 N ATOM 296 CA MET A 72 17.000 30.555 37.702 1.00 63.39 C ANISOU 296 CA MET A 72 8541 8533 7011 670 334 752 C ATOM 297 C MET A 72 16.917 29.977 39.113 1.00 62.98 C ANISOU 297 C MET A 72 8375 8394 7160 651 262 633 C ATOM 298 O MET A 72 17.362 30.632 40.052 1.00 61.72 O ANISOU 298 O MET A 72 8081 8171 7197 613 293 675 O ATOM 299 CB MET A 72 15.666 31.141 37.239 1.00 66.21 C ANISOU 299 CB MET A 72 8980 8892 7284 663 171 824 C ATOM 300 CG MET A 72 15.616 32.647 37.359 1.00 70.10 C ANISOU 300 CG MET A 72 9428 9329 7879 630 182 1004 C ATOM 301 SD MET A 72 16.264 33.509 35.912 1.00 76.93 S ANISOU 301 SD MET A 72 10431 10259 8541 644 338 1195 S ATOM 302 CE MET A 72 17.885 33.924 36.474 1.00 73.51 C ANISOU 302 CE MET A 72 9850 9791 8289 579 578 1233 C ATOM 303 N THR A 73 16.437 28.724 39.243 1.00 57.25 N ANISOU 303 N THR A 73 7717 7661 6376 673 179 483 N ATOM 304 CA THR A 73 16.320 27.977 40.505 1.00 54.47 C ANISOU 304 CA THR A 73 7306 7219 6171 657 116 370 C ATOM 305 C THR A 73 17.695 27.831 41.186 1.00 55.35 C ANISOU 305 C THR A 73 7313 7309 6407 696 240 349 C ATOM 306 O THR A 73 17.777 27.962 42.406 1.00 53.24 O ANISOU 306 O THR A 73 6946 6968 6313 671 201 334 O ATOM 307 CB THR A 73 15.600 26.632 40.255 1.00 63.03 C ANISOU 307 CB THR A 73 8521 8292 7133 664 25 222 C ATOM 308 OG1 THR A 73 14.368 26.876 39.571 1.00 62.14 O ANISOU 308 OG1 THR A 73 8474 8226 6911 626 -98 238 O ATOM 309 CG2 THR A 73 15.315 25.851 41.541 1.00 61.10 C ANISOU 309 CG2 THR A 73 8252 7938 7023 631 -43 121 C ATOM 310 N ASP A 74 18.768 27.606 40.390 1.00 52.01 N ANISOU 310 N ASP A 74 6905 6963 5892 761 388 345 N ATOM 311 CA ASP A 74 20.150 27.479 40.868 1.00 51.44 C ANISOU 311 CA ASP A 74 6709 6904 5932 813 512 316 C ATOM 312 C ASP A 74 20.706 28.801 41.428 1.00 53.96 C ANISOU 312 C ASP A 74 6857 7218 6429 747 568 431 C ATOM 313 O ASP A 74 21.595 28.774 42.281 1.00 53.76 O ANISOU 313 O ASP A 74 6693 7179 6556 767 604 391 O ATOM 314 CB ASP A 74 21.070 26.897 39.779 1.00 55.06 C ANISOU 314 CB ASP A 74 7217 7465 6237 902 667 268 C ATOM 315 CG ASP A 74 20.667 25.524 39.267 1.00 64.38 C ANISOU 315 CG ASP A 74 8572 8636 7252 977 619 128 C ATOM 316 OD1 ASP A 74 20.764 25.298 38.041 1.00 66.45 O ANISOU 316 OD1 ASP A 74 8945 8988 7316 1015 700 115 O ATOM 317 OD2 ASP A 74 20.245 24.680 40.091 1.00 67.28 O ANISOU 317 OD2 ASP A 74 8981 8900 7683 990 504 31 O ATOM 318 N LYS A 75 20.184 29.953 40.962 1.00 49.21 N ANISOU 318 N LYS A 75 6270 6618 5808 672 566 568 N ATOM 319 CA LYS A 75 20.587 31.257 41.491 1.00 48.12 C ANISOU 319 CA LYS A 75 5997 6442 5844 593 609 675 C ATOM 320 C LYS A 75 19.952 31.445 42.871 1.00 49.11 C ANISOU 320 C LYS A 75 6055 6463 6143 557 460 639 C ATOM 321 O LYS A 75 20.615 31.933 43.787 1.00 48.47 O ANISOU 321 O LYS A 75 5831 6345 6238 525 481 635 O ATOM 322 CB LYS A 75 20.219 32.400 40.532 1.00 51.28 C ANISOU 322 CB LYS A 75 6470 6853 6162 538 652 840 C ATOM 323 CG LYS A 75 21.220 32.536 39.395 1.00 64.64 C ANISOU 323 CG LYS A 75 8183 8648 7730 543 855 901 C ATOM 324 CD LYS A 75 21.001 33.778 38.544 1.00 73.20 C ANISOU 324 CD LYS A 75 9351 9721 8742 478 917 1091 C ATOM 325 CE LYS A 75 22.097 33.963 37.518 1.00 82.76 C ANISOU 325 CE LYS A 75 10572 11034 9840 459 1153 1158 C ATOM 326 NZ LYS A 75 22.122 32.863 36.513 1.00 91.73 N ANISOU 326 NZ LYS A 75 11837 12291 10725 554 1200 1077 N ATOM 327 N TYR A 76 18.687 30.995 43.029 1.00 43.51 N ANISOU 327 N TYR A 76 5442 5713 5375 560 314 598 N ATOM 328 CA TYR A 76 17.950 31.050 44.287 1.00 41.27 C ANISOU 328 CA TYR A 76 5112 5343 5225 526 185 552 C ATOM 329 C TYR A 76 18.527 30.057 45.304 1.00 43.28 C ANISOU 329 C TYR A 76 5327 5569 5547 566 173 432 C ATOM 330 O TYR A 76 18.706 30.422 46.464 1.00 42.12 O ANISOU 330 O TYR A 76 5084 5368 5550 540 137 417 O ATOM 331 CB TYR A 76 16.458 30.761 44.067 1.00 42.23 C ANISOU 331 CB TYR A 76 5334 5454 5258 511 52 530 C ATOM 332 CG TYR A 76 15.705 31.784 43.247 1.00 45.03 C ANISOU 332 CG TYR A 76 5726 5827 5557 493 16 647 C ATOM 333 CD1 TYR A 76 15.345 33.018 43.782 1.00 46.70 C ANISOU 333 CD1 TYR A 76 5862 5974 5908 455 -21 728 C ATOM 334 CD2 TYR A 76 15.233 31.472 41.974 1.00 47.13 C ANISOU 334 CD2 TYR A 76 6117 6166 5624 524 -3 664 C ATOM 335 CE1 TYR A 76 14.620 33.950 43.039 1.00 48.44 C ANISOU 335 CE1 TYR A 76 6132 6195 6078 463 -70 839 C ATOM 336 CE2 TYR A 76 14.518 32.397 41.215 1.00 49.03 C ANISOU 336 CE2 TYR A 76 6406 6424 5798 529 -58 778 C ATOM 337 CZ TYR A 76 14.197 33.628 41.757 1.00 56.60 C ANISOU 337 CZ TYR A 76 7290 7309 6905 504 -95 869 C ATOM 338 OH TYR A 76 13.474 34.529 41.012 1.00 58.48 O ANISOU 338 OH TYR A 76 7591 7550 7077 532 -162 985 O ATOM 339 N ARG A 77 18.833 28.809 44.868 1.00 39.49 N ANISOU 339 N ARG A 77 4935 5119 4950 638 199 345 N ATOM 340 CA ARG A 77 19.405 27.747 45.712 1.00 38.47 C ANISOU 340 CA ARG A 77 4805 4951 4863 705 183 235 C ATOM 341 C ARG A 77 20.787 28.096 46.262 1.00 43.60 C ANISOU 341 C ARG A 77 5295 5628 5642 746 257 234 C ATOM 342 O ARG A 77 21.178 27.558 47.298 1.00 42.92 O ANISOU 342 O ARG A 77 5179 5497 5632 795 205 164 O ATOM 343 CB ARG A 77 19.381 26.386 45.006 1.00 37.30 C ANISOU 343 CB ARG A 77 4806 4809 4556 780 194 142 C ATOM 344 CG ARG A 77 18.004 25.742 45.059 1.00 44.06 C ANISOU 344 CG ARG A 77 5803 5601 5337 724 78 93 C ATOM 345 CD ARG A 77 17.851 24.570 44.113 1.00 54.26 C ANISOU 345 CD ARG A 77 7258 6900 6458 774 88 3 C ATOM 346 NE ARG A 77 18.448 23.343 44.645 1.00 64.22 N ANISOU 346 NE ARG A 77 8591 8082 7726 862 92 -101 N ATOM 347 CZ ARG A 77 18.350 22.150 44.067 1.00 78.75 C ANISOU 347 CZ ARG A 77 10595 9884 9442 913 91 -204 C ATOM 348 NH1 ARG A 77 17.672 22.005 42.936 1.00 66.02 N ANISOU 348 NH1 ARG A 77 9084 8322 7681 875 81 -228 N ATOM 349 NH2 ARG A 77 18.931 21.092 44.616 1.00 65.60 N ANISOU 349 NH2 ARG A 77 9005 8125 7797 1009 91 -289 N ATOM 350 N LEU A 78 21.503 29.035 45.601 1.00 41.42 N ANISOU 350 N LEU A 78 4918 5427 5394 720 374 313 N ATOM 351 CA LEU A 78 22.790 29.539 46.074 1.00 41.92 C ANISOU 351 CA LEU A 78 4795 5531 5603 727 449 310 C ATOM 352 C LEU A 78 22.521 30.474 47.274 1.00 45.61 C ANISOU 352 C LEU A 78 5168 5924 6238 643 360 338 C ATOM 353 O LEU A 78 23.226 30.372 48.281 1.00 45.22 O ANISOU 353 O LEU A 78 5007 5868 6305 673 323 274 O ATOM 354 CB LEU A 78 23.567 30.260 44.947 1.00 43.43 C ANISOU 354 CB LEU A 78 4916 5819 5767 694 622 389 C ATOM 355 CG LEU A 78 24.848 31.027 45.347 1.00 48.97 C ANISOU 355 CG LEU A 78 5394 6570 6642 654 717 396 C ATOM 356 CD1 LEU A 78 25.928 30.100 45.884 1.00 49.60 C ANISOU 356 CD1 LEU A 78 5358 6709 6779 777 723 264 C ATOM 357 CD2 LEU A 78 25.391 31.827 44.188 1.00 53.47 C ANISOU 357 CD2 LEU A 78 5925 7217 7172 583 903 497 C ATOM 358 N HIS A 79 21.481 31.351 47.174 1.00 41.76 N ANISOU 358 N HIS A 79 4732 5382 5755 552 315 423 N ATOM 359 CA HIS A 79 21.069 32.273 48.239 1.00 40.88 C ANISOU 359 CA HIS A 79 4553 5190 5788 478 233 442 C ATOM 360 C HIS A 79 20.691 31.479 49.483 1.00 43.97 C ANISOU 360 C HIS A 79 4975 5531 6202 516 113 342 C ATOM 361 O HIS A 79 21.089 31.851 50.592 1.00 43.38 O ANISOU 361 O HIS A 79 4805 5427 6251 501 67 305 O ATOM 362 CB HIS A 79 19.871 33.136 47.803 1.00 41.30 C ANISOU 362 CB HIS A 79 4682 5194 5816 413 195 536 C ATOM 363 CG HIS A 79 20.209 34.255 46.876 1.00 46.02 C ANISOU 363 CG HIS A 79 5258 5802 6425 358 298 660 C ATOM 364 ND1 HIS A 79 20.897 35.370 47.314 1.00 48.22 N ANISOU 364 ND1 HIS A 79 5415 6038 6868 283 347 701 N ATOM 365 CD2 HIS A 79 19.890 34.421 45.572 1.00 48.74 C ANISOU 365 CD2 HIS A 79 5705 6183 6630 361 354 753 C ATOM 366 CE1 HIS A 79 21.005 36.165 46.262 1.00 49.04 C ANISOU 366 CE1 HIS A 79 5559 6143 6933 237 446 827 C ATOM 367 NE2 HIS A 79 20.417 35.632 45.186 1.00 49.72 N ANISOU 367 NE2 HIS A 79 5784 6282 6827 289 452 867 N ATOM 368 N LEU A 80 19.938 30.372 49.280 1.00 40.13 N ANISOU 368 N LEU A 80 4632 5032 5585 559 64 298 N ATOM 369 CA LEU A 80 19.479 29.424 50.300 1.00 39.06 C ANISOU 369 CA LEU A 80 4574 4835 5431 586 -30 215 C ATOM 370 C LEU A 80 20.687 28.775 50.999 1.00 44.54 C ANISOU 370 C LEU A 80 5217 5539 6168 681 -32 145 C ATOM 371 O LEU A 80 20.667 28.607 52.220 1.00 43.37 O ANISOU 371 O LEU A 80 5068 5341 6069 689 -112 103 O ATOM 372 CB LEU A 80 18.601 28.349 49.633 1.00 38.74 C ANISOU 372 CB LEU A 80 4699 4780 5239 599 -52 184 C ATOM 373 CG LEU A 80 17.515 27.690 50.481 1.00 42.03 C ANISOU 373 CG LEU A 80 5219 5119 5631 557 -142 132 C ATOM 374 CD1 LEU A 80 16.310 28.583 50.615 1.00 41.34 C ANISOU 374 CD1 LEU A 80 5100 5025 5583 459 -187 172 C ATOM 375 CD2 LEU A 80 17.060 26.392 49.854 1.00 44.03 C ANISOU 375 CD2 LEU A 80 5633 5350 5746 577 -150 75 C ATOM 376 N SER A 81 21.750 28.458 50.227 1.00 43.34 N ANISOU 376 N SER A 81 5015 5461 5993 758 56 132 N ATOM 377 CA SER A 81 22.981 27.865 50.745 1.00 44.54 C ANISOU 377 CA SER A 81 5088 5643 6191 874 53 59 C ATOM 378 C SER A 81 23.738 28.831 51.652 1.00 50.16 C ANISOU 378 C SER A 81 5611 6382 7067 841 29 56 C ATOM 379 O SER A 81 24.201 28.416 52.714 1.00 50.05 O ANISOU 379 O SER A 81 5571 6351 7096 913 -60 -9 O ATOM 380 CB SER A 81 23.870 27.376 49.609 1.00 49.16 C ANISOU 380 CB SER A 81 5645 6318 6717 965 171 36 C ATOM 381 OG SER A 81 23.335 26.187 49.056 1.00 58.22 O ANISOU 381 OG SER A 81 6985 7422 7714 1030 163 -5 O ATOM 382 N VAL A 82 23.838 30.118 51.256 1.00 47.67 N ANISOU 382 N VAL A 82 5178 6097 6837 730 98 125 N ATOM 383 CA VAL A 82 24.514 31.156 52.047 1.00 48.13 C ANISOU 383 CA VAL A 82 5057 6169 7062 668 79 116 C ATOM 384 C VAL A 82 23.725 31.389 53.348 1.00 51.33 C ANISOU 384 C VAL A 82 5517 6484 7501 629 -56 92 C ATOM 385 O VAL A 82 24.332 31.450 54.422 1.00 51.78 O ANISOU 385 O VAL A 82 5487 6548 7638 658 -135 24 O ATOM 386 CB VAL A 82 24.752 32.471 51.246 1.00 52.83 C ANISOU 386 CB VAL A 82 5548 6788 7738 543 198 204 C ATOM 387 CG1 VAL A 82 25.424 33.543 52.106 1.00 53.00 C ANISOU 387 CG1 VAL A 82 5390 6802 7944 458 173 179 C ATOM 388 CG2 VAL A 82 25.574 32.207 49.986 1.00 54.20 C ANISOU 388 CG2 VAL A 82 5671 7066 7859 576 353 226 C ATOM 389 N ALA A 83 22.375 31.455 53.249 1.00 46.07 N ANISOU 389 N ALA A 83 4994 5746 6764 575 -83 138 N ATOM 390 CA ALA A 83 21.467 31.649 54.384 1.00 44.46 C ANISOU 390 CA ALA A 83 4851 5465 6575 533 -184 115 C ATOM 391 C ALA A 83 21.594 30.517 55.413 1.00 47.67 C ANISOU 391 C ALA A 83 5342 5852 6920 623 -273 37 C ATOM 392 O ALA A 83 21.568 30.788 56.613 1.00 46.98 O ANISOU 392 O ALA A 83 5239 5736 6876 611 -353 -5 O ATOM 393 CB ALA A 83 20.030 31.764 53.896 1.00 44.27 C ANISOU 393 CB ALA A 83 4945 5395 6479 473 -182 167 C ATOM 394 N ASP A 84 21.769 29.263 54.934 1.00 44.15 N ANISOU 394 N ASP A 84 4997 5413 6366 718 -260 19 N ATOM 395 CA ASP A 84 21.919 28.061 55.756 1.00 43.64 C ANISOU 395 CA ASP A 84 5051 5305 6226 820 -338 -38 C ATOM 396 C ASP A 84 23.345 27.852 56.278 1.00 47.01 C ANISOU 396 C ASP A 84 5362 5788 6712 943 -383 -97 C ATOM 397 O ASP A 84 23.500 27.384 57.409 1.00 46.59 O ANISOU 397 O ASP A 84 5369 5697 6633 1008 -485 -137 O ATOM 398 CB ASP A 84 21.386 26.816 55.024 1.00 45.68 C ANISOU 398 CB ASP A 84 5491 5516 6347 863 -310 -39 C ATOM 399 CG ASP A 84 19.883 26.820 54.788 1.00 57.01 C ANISOU 399 CG ASP A 84 7046 6896 7718 744 -303 -7 C ATOM 400 OD1 ASP A 84 19.146 27.354 55.644 1.00 56.89 O ANISOU 400 OD1 ASP A 84 7033 6849 7734 661 -344 -1 O ATOM 401 OD2 ASP A 84 19.444 26.254 53.767 1.00 64.74 O ANISOU 401 OD2 ASP A 84 8114 7872 8613 740 -259 -1 O ATOM 402 N LEU A 85 24.381 28.204 55.478 1.00 43.56 N ANISOU 402 N LEU A 85 4755 5448 6349 974 -306 -102 N ATOM 403 CA LEU A 85 25.782 28.078 55.903 1.00 44.37 C ANISOU 403 CA LEU A 85 4696 5632 6531 1090 -346 -173 C ATOM 404 C LEU A 85 26.039 28.995 57.103 1.00 48.32 C ANISOU 404 C LEU A 85 5078 6142 7139 1032 -443 -206 C ATOM 405 O LEU A 85 26.621 28.554 58.099 1.00 48.82 O ANISOU 405 O LEU A 85 5129 6217 7201 1140 -564 -271 O ATOM 406 CB LEU A 85 26.775 28.385 54.757 1.00 45.35 C ANISOU 406 CB LEU A 85 4635 5872 6723 1104 -215 -176 C ATOM 407 CG LEU A 85 28.271 28.270 55.102 1.00 51.38 C ANISOU 407 CG LEU A 85 5183 6749 7588 1222 -245 -265 C ATOM 408 CD1 LEU A 85 28.730 26.823 55.125 1.00 52.45 C ANISOU 408 CD1 LEU A 85 5411 6882 7635 1440 -293 -328 C ATOM 409 CD2 LEU A 85 29.110 29.062 54.137 1.00 54.77 C ANISOU 409 CD2 LEU A 85 5386 7298 8124 1151 -93 -257 C ATOM 410 N LEU A 86 25.561 30.259 57.008 1.00 43.52 N ANISOU 410 N LEU A 86 4402 5521 6614 869 -399 -163 N ATOM 411 CA LEU A 86 25.665 31.304 58.027 1.00 42.81 C ANISOU 411 CA LEU A 86 4211 5424 6632 784 -475 -199 C ATOM 412 C LEU A 86 25.060 30.823 59.356 1.00 44.50 C ANISOU 412 C LEU A 86 4580 5571 6756 827 -609 -235 C ATOM 413 O LEU A 86 25.600 31.128 60.418 1.00 44.37 O ANISOU 413 O LEU A 86 4492 5581 6787 848 -717 -306 O ATOM 414 CB LEU A 86 24.928 32.564 57.532 1.00 42.23 C ANISOU 414 CB LEU A 86 4116 5302 6629 617 -393 -130 C ATOM 415 CG LEU A 86 25.451 33.912 58.024 1.00 47.50 C ANISOU 415 CG LEU A 86 4611 5975 7463 508 -408 -165 C ATOM 416 CD1 LEU A 86 26.438 34.506 57.032 1.00 48.99 C ANISOU 416 CD1 LEU A 86 4614 6233 7767 449 -287 -140 C ATOM 417 CD2 LEU A 86 24.305 34.882 58.261 1.00 48.08 C ANISOU 417 CD2 LEU A 86 4764 5944 7560 391 -407 -125 C ATOM 418 N PHE A 87 23.955 30.052 59.288 1.00 39.22 N ANISOU 418 N PHE A 87 4128 4823 5951 834 -598 -191 N ATOM 419 CA PHE A 87 23.286 29.507 60.462 1.00 38.13 C ANISOU 419 CA PHE A 87 4165 4616 5706 857 -691 -210 C ATOM 420 C PHE A 87 23.968 28.260 61.003 1.00 43.86 C ANISOU 420 C PHE A 87 4985 5340 6340 1027 -782 -246 C ATOM 421 O PHE A 87 24.156 28.179 62.219 1.00 44.19 O ANISOU 421 O PHE A 87 5073 5374 6344 1074 -896 -287 O ATOM 422 CB PHE A 87 21.788 29.273 60.217 1.00 38.19 C ANISOU 422 CB PHE A 87 4345 4543 5624 768 -633 -155 C ATOM 423 CG PHE A 87 21.096 28.408 61.246 1.00 39.29 C ANISOU 423 CG PHE A 87 4692 4607 5627 789 -692 -164 C ATOM 424 CD1 PHE A 87 20.647 27.138 60.918 1.00 41.91 C ANISOU 424 CD1 PHE A 87 5211 4874 5838 829 -669 -137 C ATOM 425 CD2 PHE A 87 20.928 28.849 62.556 1.00 41.84 C ANISOU 425 CD2 PHE A 87 5039 4922 5938 764 -765 -203 C ATOM 426 CE1 PHE A 87 20.025 26.331 61.871 1.00 43.11 C ANISOU 426 CE1 PHE A 87 5573 4944 5864 829 -706 -135 C ATOM 427 CE2 PHE A 87 20.315 28.037 63.512 1.00 44.74 C ANISOU 427 CE2 PHE A 87 5615 5223 6161 776 -801 -201 C ATOM 428 CZ PHE A 87 19.862 26.784 63.161 1.00 42.69 C ANISOU 428 CZ PHE A 87 5543 4891 5788 802 -766 -160 C ATOM 429 N VAL A 88 24.320 27.280 60.129 1.00 41.13 N ANISOU 429 N VAL A 88 4686 4993 5947 1129 -737 -232 N ATOM 430 CA VAL A 88 24.973 26.044 60.584 1.00 42.42 C ANISOU 430 CA VAL A 88 4957 5133 6025 1317 -826 -264 C ATOM 431 C VAL A 88 26.256 26.273 61.389 1.00 47.91 C ANISOU 431 C VAL A 88 5489 5921 6793 1437 -951 -338 C ATOM 432 O VAL A 88 26.492 25.549 62.353 1.00 48.35 O ANISOU 432 O VAL A 88 5672 5938 6759 1565 -1078 -358 O ATOM 433 CB VAL A 88 25.077 24.887 59.555 1.00 47.10 C ANISOU 433 CB VAL A 88 5657 5689 6550 1420 -760 -251 C ATOM 434 CG1 VAL A 88 23.698 24.417 59.102 1.00 45.77 C ANISOU 434 CG1 VAL A 88 5704 5409 6278 1309 -686 -195 C ATOM 435 CG2 VAL A 88 25.951 25.256 58.364 1.00 47.70 C ANISOU 435 CG2 VAL A 88 5515 5881 6728 1448 -663 -273 C ATOM 436 N ILE A 89 27.028 27.326 61.048 1.00 45.00 N ANISOU 436 N ILE A 89 4846 5669 6582 1382 -921 -377 N ATOM 437 CA ILE A 89 28.262 27.704 61.755 1.00 46.29 C ANISOU 437 CA ILE A 89 4802 5944 6843 1464 -1041 -468 C ATOM 438 C ILE A 89 28.002 28.201 63.188 1.00 50.04 C ANISOU 438 C ILE A 89 5328 6398 7288 1423 -1181 -503 C ATOM 439 O ILE A 89 28.907 28.150 64.024 1.00 51.34 O ANISOU 439 O ILE A 89 5401 6635 7471 1536 -1331 -582 O ATOM 440 CB ILE A 89 29.185 28.655 60.937 1.00 50.09 C ANISOU 440 CB ILE A 89 4968 6553 7510 1391 -950 -506 C ATOM 441 CG1 ILE A 89 28.515 30.013 60.648 1.00 49.36 C ANISOU 441 CG1 ILE A 89 4814 6433 7506 1158 -851 -463 C ATOM 442 CG2 ILE A 89 29.673 27.980 59.657 1.00 51.34 C ANISOU 442 CG2 ILE A 89 5076 6759 7671 1482 -826 -493 C ATOM 443 CD1 ILE A 89 29.452 31.207 60.577 1.00 58.27 C ANISOU 443 CD1 ILE A 89 5650 7662 8829 1055 -832 -523 C ATOM 444 N THR A 90 26.775 28.678 63.471 1.00 44.87 N ANISOU 444 N THR A 90 4813 5654 6582 1271 -1135 -453 N ATOM 445 CA THR A 90 26.411 29.148 64.812 1.00 44.78 C ANISOU 445 CA THR A 90 4873 5620 6521 1227 -1245 -491 C ATOM 446 C THR A 90 25.960 27.993 65.707 1.00 48.68 C ANISOU 446 C THR A 90 5652 6033 6812 1339 -1331 -462 C ATOM 447 O THR A 90 25.875 28.173 66.921 1.00 48.54 O ANISOU 447 O THR A 90 5711 6013 6717 1349 -1443 -500 O ATOM 448 CB THR A 90 25.391 30.302 64.765 1.00 52.34 C ANISOU 448 CB THR A 90 5821 6532 7534 1025 -1154 -471 C ATOM 449 OG1 THR A 90 24.198 29.875 64.101 1.00 50.46 O ANISOU 449 OG1 THR A 90 5748 6207 7219 962 -1033 -382 O ATOM 450 CG2 THR A 90 25.957 31.571 64.134 1.00 51.21 C ANISOU 450 CG2 THR A 90 5416 6450 7593 913 -1096 -503 C ATOM 451 N LEU A 91 25.685 26.807 65.109 1.00 45.04 N ANISOU 451 N LEU A 91 5358 5496 6257 1421 -1277 -397 N ATOM 452 CA LEU A 91 25.244 25.613 65.838 1.00 45.34 C ANISOU 452 CA LEU A 91 5698 5426 6104 1516 -1338 -353 C ATOM 453 C LEU A 91 26.213 25.121 66.929 1.00 52.05 C ANISOU 453 C LEU A 91 6592 6309 6877 1714 -1532 -398 C ATOM 454 O LEU A 91 25.702 24.783 67.991 1.00 52.85 O ANISOU 454 O LEU A 91 6920 6341 6821 1721 -1597 -370 O ATOM 455 CB LEU A 91 24.791 24.462 64.926 1.00 44.96 C ANISOU 455 CB LEU A 91 5823 5273 5986 1553 -1241 -286 C ATOM 456 CG LEU A 91 23.523 24.659 64.103 1.00 47.64 C ANISOU 456 CG LEU A 91 6217 5554 6329 1364 -1078 -233 C ATOM 457 CD1 LEU A 91 23.430 23.600 63.035 1.00 47.80 C ANISOU 457 CD1 LEU A 91 6344 5504 6312 1421 -1003 -201 C ATOM 458 CD2 LEU A 91 22.271 24.639 64.971 1.00 49.37 C ANISOU 458 CD2 LEU A 91 6636 5688 6432 1235 -1057 -196 C ATOM 459 N PRO A 92 27.572 25.107 66.772 1.00 49.54 N ANISOU 459 N PRO A 92 6063 6103 6657 1873 -1633 -469 N ATOM 460 CA PRO A 92 28.433 24.709 67.909 1.00 51.02 C ANISOU 460 CA PRO A 92 6287 6333 6764 2070 -1848 -519 C ATOM 461 C PRO A 92 28.177 25.554 69.165 1.00 53.60 C ANISOU 461 C PRO A 92 6632 6696 7037 1980 -1948 -562 C ATOM 462 O PRO A 92 28.234 25.015 70.269 1.00 54.05 O ANISOU 462 O PRO A 92 6892 6721 6924 2098 -2093 -553 O ATOM 463 CB PRO A 92 29.853 24.910 67.369 1.00 54.26 C ANISOU 463 CB PRO A 92 6370 6898 7347 2199 -1909 -614 C ATOM 464 CG PRO A 92 29.708 24.789 65.896 1.00 57.78 C ANISOU 464 CG PRO A 92 6733 7330 7891 2140 -1714 -580 C ATOM 465 CD PRO A 92 28.396 25.445 65.593 1.00 51.11 C ANISOU 465 CD PRO A 92 5975 6406 7037 1887 -1557 -513 C ATOM 466 N PHE A 93 27.825 26.851 68.992 1.00 48.62 N ANISOU 466 N PHE A 93 5822 6117 6535 1771 -1864 -603 N ATOM 467 CA PHE A 93 27.470 27.754 70.093 1.00 48.55 C ANISOU 467 CA PHE A 93 5830 6132 6485 1665 -1931 -659 C ATOM 468 C PHE A 93 26.169 27.286 70.758 1.00 52.19 C ANISOU 468 C PHE A 93 6626 6465 6737 1602 -1873 -575 C ATOM 469 O PHE A 93 26.032 27.418 71.973 1.00 52.88 O ANISOU 469 O PHE A 93 6844 6561 6687 1617 -1978 -607 O ATOM 470 CB PHE A 93 27.317 29.205 69.612 1.00 49.18 C ANISOU 470 CB PHE A 93 5664 6261 6762 1459 -1832 -714 C ATOM 471 CG PHE A 93 28.545 29.867 69.025 1.00 51.73 C ANISOU 471 CG PHE A 93 5643 6709 7303 1464 -1863 -802 C ATOM 472 CD1 PHE A 93 29.584 30.292 69.845 1.00 56.58 C ANISOU 472 CD1 PHE A 93 6092 7441 7965 1530 -2051 -928 C ATOM 473 CD2 PHE A 93 28.614 30.162 67.668 1.00 53.11 C ANISOU 473 CD2 PHE A 93 5653 6890 7635 1380 -1698 -764 C ATOM 474 CE1 PHE A 93 30.700 30.944 69.309 1.00 58.57 C ANISOU 474 CE1 PHE A 93 6003 7816 8436 1504 -2065 -1019 C ATOM 475 CE2 PHE A 93 29.730 30.817 67.132 1.00 56.95 C ANISOU 475 CE2 PHE A 93 5821 7495 8324 1357 -1699 -842 C ATOM 476 CZ PHE A 93 30.765 31.204 67.956 1.00 56.94 C ANISOU 476 CZ PHE A 93 5640 7609 8384 1412 -1878 -971 C ATOM 477 N TRP A 94 25.228 26.725 69.958 1.00 47.57 N ANISOU 477 N TRP A 94 6179 5772 6124 1527 -1704 -476 N ATOM 478 CA TRP A 94 23.943 26.170 70.415 1.00 46.70 C ANISOU 478 CA TRP A 94 6368 5540 5836 1445 -1615 -394 C ATOM 479 C TRP A 94 24.196 24.880 71.194 1.00 52.51 C ANISOU 479 C TRP A 94 7389 6199 6361 1619 -1726 -338 C ATOM 480 O TRP A 94 23.484 24.601 72.159 1.00 52.72 O ANISOU 480 O TRP A 94 7665 6162 6204 1579 -1723 -299 O ATOM 481 CB TRP A 94 23.022 25.858 69.216 1.00 43.58 C ANISOU 481 CB TRP A 94 6005 5064 5491 1327 -1424 -320 C ATOM 482 CG TRP A 94 22.292 27.033 68.634 1.00 42.77 C ANISOU 482 CG TRP A 94 5728 4994 5528 1136 -1297 -342 C ATOM 483 CD1 TRP A 94 22.839 28.134 68.045 1.00 45.21 C ANISOU 483 CD1 TRP A 94 5758 5390 6028 1091 -1290 -398 C ATOM 484 CD2 TRP A 94 20.873 27.166 68.497 1.00 41.36 C ANISOU 484 CD2 TRP A 94 5647 4754 5314 970 -1153 -301 C ATOM 485 NE1 TRP A 94 21.846 28.974 67.598 1.00 43.26 N ANISOU 485 NE1 TRP A 94 5453 5126 5858 922 -1163 -388 N ATOM 486 CE2 TRP A 94 20.629 28.402 67.856 1.00 44.16 C ANISOU 486 CE2 TRP A 94 5779 5161 5840 854 -1083 -335 C ATOM 487 CE3 TRP A 94 19.778 26.377 68.885 1.00 42.58 C ANISOU 487 CE3 TRP A 94 6051 4814 5312 904 -1076 -242 C ATOM 488 CZ2 TRP A 94 19.334 28.867 67.598 1.00 42.35 C ANISOU 488 CZ2 TRP A 94 5561 4901 5630 702 -957 -318 C ATOM 489 CZ3 TRP A 94 18.498 26.839 68.632 1.00 42.86 C ANISOU 489 CZ3 TRP A 94 6074 4835 5374 733 -939 -235 C ATOM 490 CH2 TRP A 94 18.283 28.067 67.992 1.00 42.49 C ANISOU 490 CH2 TRP A 94 5795 4850 5500 647 -889 -275 C ATOM 491 N ALA A 95 25.205 24.091 70.765 1.00 50.15 N ANISOU 491 N ALA A 95 7064 5904 6089 1818 -1817 -334 N ATOM 492 CA ALA A 95 25.590 22.831 71.397 1.00 51.80 C ANISOU 492 CA ALA A 95 7541 6024 6116 2024 -1942 -278 C ATOM 493 C ALA A 95 26.171 23.075 72.788 1.00 57.56 C ANISOU 493 C ALA A 95 8321 6829 6722 2137 -2148 -326 C ATOM 494 O ALA A 95 25.711 22.456 73.746 1.00 58.30 O ANISOU 494 O ALA A 95 8733 6828 6589 2170 -2186 -256 O ATOM 495 CB ALA A 95 26.587 22.080 70.522 1.00 53.30 C ANISOU 495 CB ALA A 95 7639 6216 6396 2225 -1991 -286 C ATOM 496 N VAL A 96 27.142 24.012 72.902 1.00 54.57 N ANISOU 496 N VAL A 96 7630 6619 6484 2179 -2272 -449 N ATOM 497 CA VAL A 96 27.813 24.383 74.155 1.00 56.28 C ANISOU 497 CA VAL A 96 7836 6940 6608 2284 -2494 -529 C ATOM 498 C VAL A 96 26.807 24.934 75.171 1.00 59.35 C ANISOU 498 C VAL A 96 8408 7303 6839 2120 -2449 -524 C ATOM 499 O VAL A 96 26.839 24.546 76.339 1.00 60.65 O ANISOU 499 O VAL A 96 8813 7454 6777 2220 -2582 -505 O ATOM 500 CB VAL A 96 29.016 25.341 73.922 1.00 60.94 C ANISOU 500 CB VAL A 96 8014 7719 7421 2318 -2613 -681 C ATOM 501 CG1 VAL A 96 29.645 25.783 75.244 1.00 62.93 C ANISOU 501 CG1 VAL A 96 8250 8087 7574 2407 -2855 -784 C ATOM 502 CG2 VAL A 96 30.071 24.697 73.026 1.00 61.65 C ANISOU 502 CG2 VAL A 96 7928 7853 7644 2508 -2659 -695 C ATOM 503 N ASP A 97 25.899 25.807 74.711 1.00 53.89 N ANISOU 503 N ASP A 97 7614 6603 6258 1880 -2258 -538 N ATOM 504 CA ASP A 97 24.845 26.428 75.515 1.00 53.44 C ANISOU 504 CA ASP A 97 7689 6528 6087 1710 -2175 -548 C ATOM 505 C ASP A 97 23.823 25.428 76.088 1.00 59.26 C ANISOU 505 C ASP A 97 8820 7128 6568 1688 -2083 -421 C ATOM 506 O ASP A 97 23.263 25.672 77.159 1.00 60.17 O ANISOU 506 O ASP A 97 9107 7248 6506 1629 -2081 -433 O ATOM 507 CB ASP A 97 24.058 27.424 74.647 1.00 52.55 C ANISOU 507 CB ASP A 97 7377 6415 6173 1485 -1976 -575 C ATOM 508 CG ASP A 97 22.761 27.898 75.247 1.00 60.27 C ANISOU 508 CG ASP A 97 8496 7355 7050 1311 -1840 -572 C ATOM 509 OD1 ASP A 97 21.702 27.371 74.852 1.00 59.90 O ANISOU 509 OD1 ASP A 97 8595 7211 6954 1214 -1667 -479 O ATOM 510 OD2 ASP A 97 22.803 28.777 76.133 1.00 66.18 O ANISOU 510 OD2 ASP A 97 9207 8174 7765 1275 -1909 -675 O ATOM 511 N ALA A 98 23.618 24.295 75.392 1.00 55.67 N ANISOU 511 N ALA A 98 8513 6549 6091 1734 -2005 -306 N ATOM 512 CA ALA A 98 22.686 23.242 75.790 1.00 55.90 C ANISOU 512 CA ALA A 98 8916 6423 5901 1696 -1901 -177 C ATOM 513 C ALA A 98 23.396 22.497 76.932 1.00 62.01 C ANISOU 513 C ALA A 98 9949 7175 6438 1913 -2106 -139 C ATOM 514 O ALA A 98 22.781 22.292 77.978 1.00 63.03 O ANISOU 514 O ALA A 98 10358 7259 6332 1866 -2083 -89 O ATOM 515 CB ALA A 98 22.179 22.473 74.579 1.00 55.43 C ANISOU 515 CB ALA A 98 8891 6239 5930 1636 -1742 -95 C ATOM 516 N VAL A 99 24.669 22.090 76.746 1.00 59.44 N ANISOU 516 N VAL A 99 9535 6886 6164 2156 -2304 -162 N ATOM 517 CA VAL A 99 25.425 21.348 77.771 1.00 62.13 C ANISOU 517 CA VAL A 99 10114 7208 6284 2403 -2532 -124 C ATOM 518 C VAL A 99 25.895 22.191 78.954 1.00 67.61 C ANISOU 518 C VAL A 99 10753 8061 6877 2449 -2718 -229 C ATOM 519 O VAL A 99 25.398 22.003 80.068 1.00 68.83 O ANISOU 519 O VAL A 99 11210 8176 6764 2433 -2733 -177 O ATOM 520 CB VAL A 99 26.384 20.350 77.060 1.00 67.05 C ANISOU 520 CB VAL A 99 10723 7771 6982 2652 -2642 -89 C ATOM 521 CG1 VAL A 99 25.615 19.336 76.233 1.00 66.01 C ANISOU 521 CG1 VAL A 99 10801 7432 6847 2582 -2446 34 C ATOM 522 CG2 VAL A 99 27.445 21.059 76.218 1.00 66.21 C ANISOU 522 CG2 VAL A 99 10161 7835 7159 2722 -2722 -228 C ATOM 523 N ALA A 100 26.796 23.139 78.706 1.00 63.69 N ANISOU 523 N ALA A 100 9874 7739 6586 2484 -2842 -381 N ATOM 524 CA ALA A 100 27.356 23.913 79.809 1.00 64.86 C ANISOU 524 CA ALA A 100 9956 8041 6648 2538 -3048 -504 C ATOM 525 C ALA A 100 26.991 25.370 80.151 1.00 66.80 C ANISOU 525 C ALA A 100 10002 8403 6975 2327 -2997 -646 C ATOM 526 O ALA A 100 26.571 25.637 81.277 1.00 67.65 O ANISOU 526 O ALA A 100 10309 8533 6864 2290 -3034 -667 O ATOM 527 CB ALA A 100 28.851 23.883 79.431 1.00 66.96 C ANISOU 527 CB ALA A 100 9926 8433 7084 2762 -3277 -600 C ATOM 528 N ASN A 101 27.097 26.304 79.252 1.00 60.91 N ANISOU 528 N ASN A 101 8902 7721 6518 2189 -2907 -738 N ATOM 529 CA ASN A 101 27.039 27.799 79.695 1.00 60.37 C ANISOU 529 CA ASN A 101 8623 7769 6545 2028 -2923 -906 C ATOM 530 C ASN A 101 27.172 28.722 78.461 1.00 62.15 C ANISOU 530 C ASN A 101 8470 8027 7117 1876 -2797 -974 C ATOM 531 O ASN A 101 27.415 28.250 77.348 1.00 60.66 O ANISOU 531 O ASN A 101 8168 7802 7079 1908 -2720 -907 O ATOM 532 CB ASN A 101 27.923 28.374 80.828 1.00 63.13 C ANISOU 532 CB ASN A 101 8909 8269 6809 2128 -3196 -1063 C ATOM 533 CG ASN A 101 27.279 28.371 82.185 1.00 79.38 C ANISOU 533 CG ASN A 101 11295 10318 8548 2118 -3230 -1062 C ATOM 534 OD1 ASN A 101 26.803 29.399 82.670 1.00 70.81 O ANISOU 534 OD1 ASN A 101 10169 9274 7462 1963 -3178 -1175 O ATOM 535 ND2 ASN A 101 27.291 27.223 82.845 1.00 72.33 N ANISOU 535 ND2 ASN A 101 10744 9370 7370 2291 -3320 -939 N ATOM 536 N TRP A 102 26.900 29.966 78.586 1.00 58.37 N ANISOU 536 N TRP A 102 7834 7592 6752 1707 -2747 -1089 N ATOM 537 CA TRP A 102 27.158 30.977 77.566 1.00 57.03 C ANISOU 537 CA TRP A 102 7317 7453 6900 1567 -2660 -1163 C ATOM 538 C TRP A 102 28.415 31.784 77.886 1.00 63.03 C ANISOU 538 C TRP A 102 7793 8356 7799 1601 -2871 -1340 C ATOM 539 O TRP A 102 28.343 32.893 78.416 1.00 63.53 O ANISOU 539 O TRP A 102 7772 8455 7912 1480 -2903 -1475 O ATOM 540 CB TRP A 102 25.958 31.915 77.436 1.00 54.02 C ANISOU 540 CB TRP A 102 6948 7001 6576 1345 -2453 -1175 C ATOM 541 CG TRP A 102 25.915 32.655 76.134 1.00 53.16 C ANISOU 541 CG TRP A 102 6572 6866 6760 1206 -2303 -1174 C ATOM 542 CD1 TRP A 102 26.205 33.973 75.931 1.00 56.11 C ANISOU 542 CD1 TRP A 102 6700 7270 7350 1076 -2301 -1296 C ATOM 543 CD2 TRP A 102 25.561 32.120 74.853 1.00 51.22 C ANISOU 543 CD2 TRP A 102 6299 6550 6611 1183 -2135 -1041 C ATOM 544 NE1 TRP A 102 26.053 34.291 74.603 1.00 53.94 N ANISOU 544 NE1 TRP A 102 6259 6946 7291 977 -2137 -1231 N ATOM 545 CE2 TRP A 102 25.659 33.171 73.920 1.00 54.13 C ANISOU 545 CE2 TRP A 102 6408 6918 7241 1044 -2037 -1080 C ATOM 546 CE3 TRP A 102 25.171 30.854 74.404 1.00 51.77 C ANISOU 546 CE3 TRP A 102 6553 6549 6568 1262 -2059 -897 C ATOM 547 CZ2 TRP A 102 25.381 32.996 72.566 1.00 51.74 C ANISOU 547 CZ2 TRP A 102 6026 6564 7067 992 -1872 -977 C ATOM 548 CZ3 TRP A 102 24.896 30.682 73.060 1.00 51.47 C ANISOU 548 CZ3 TRP A 102 6425 6461 6671 1205 -1899 -812 C ATOM 549 CH2 TRP A 102 25.002 31.747 72.157 1.00 51.19 C ANISOU 549 CH2 TRP A 102 6131 6443 6876 1077 -1810 -851 C ATOM 550 N TYR A 103 29.564 31.203 77.562 1.00 60.20 N ANISOU 550 N TYR A 103 7285 8079 7509 1768 -3015 -1349 N ATOM 551 CA TYR A 103 30.880 31.770 77.878 1.00 62.01 C ANISOU 551 CA TYR A 103 7225 8469 7868 1826 -3241 -1523 C ATOM 552 C TYR A 103 31.177 32.914 76.897 1.00 64.66 C ANISOU 552 C TYR A 103 7205 8828 8537 1626 -3118 -1603 C ATOM 553 O TYR A 103 31.844 33.885 77.265 1.00 65.97 O ANISOU 553 O TYR A 103 7147 9087 8832 1548 -3238 -1773 O ATOM 554 CB TYR A 103 31.992 30.702 77.772 1.00 64.99 C ANISOU 554 CB TYR A 103 7540 8932 8221 2089 -3422 -1504 C ATOM 555 CG TYR A 103 31.752 29.445 78.584 1.00 67.69 C ANISOU 555 CG TYR A 103 8259 9220 8242 2309 -3536 -1392 C ATOM 556 CD1 TYR A 103 31.235 28.297 77.991 1.00 68.47 C ANISOU 556 CD1 TYR A 103 8577 9183 8254 2391 -3399 -1211 C ATOM 557 CD2 TYR A 103 32.080 29.393 79.935 1.00 70.85 C ANISOU 557 CD2 TYR A 103 8805 9697 8418 2435 -3787 -1469 C ATOM 558 CE1 TYR A 103 31.020 27.135 78.732 1.00 70.28 C ANISOU 558 CE1 TYR A 103 9177 9336 8192 2581 -3495 -1097 C ATOM 559 CE2 TYR A 103 31.875 28.235 80.683 1.00 73.02 C ANISOU 559 CE2 TYR A 103 9454 9909 8382 2638 -3889 -1348 C ATOM 560 CZ TYR A 103 31.345 27.108 80.077 1.00 79.16 C ANISOU 560 CZ TYR A 103 10457 10532 9088 2707 -3737 -1158 C ATOM 561 OH TYR A 103 31.147 25.967 80.813 1.00 81.59 O ANISOU 561 OH TYR A 103 11156 10751 9092 2896 -3829 -1030 O ATOM 562 N PHE A 104 30.653 32.783 75.658 1.00 58.19 N ANISOU 562 N PHE A 104 6354 7914 7842 1538 -2877 -1477 N ATOM 563 CA PHE A 104 30.794 33.651 74.478 1.00 56.51 C ANISOU 563 CA PHE A 104 5864 7691 7918 1360 -2709 -1490 C ATOM 564 C PHE A 104 30.538 35.148 74.652 1.00 59.66 C ANISOU 564 C PHE A 104 6141 8063 8465 1134 -2662 -1603 C ATOM 565 O PHE A 104 31.094 35.942 73.893 1.00 59.57 O ANISOU 565 O PHE A 104 5853 8075 8705 1007 -2598 -1655 O ATOM 566 CB PHE A 104 30.022 33.069 73.278 1.00 55.93 C ANISOU 566 CB PHE A 104 5883 7505 7861 1332 -2471 -1314 C ATOM 567 CG PHE A 104 30.033 31.555 73.227 1.00 57.61 C ANISOU 567 CG PHE A 104 6297 7698 7895 1544 -2505 -1200 C ATOM 568 CD1 PHE A 104 28.881 30.827 73.500 1.00 59.37 C ANISOU 568 CD1 PHE A 104 6858 7797 7904 1558 -2420 -1077 C ATOM 569 CD2 PHE A 104 31.209 30.860 72.971 1.00 61.30 C ANISOU 569 CD2 PHE A 104 6617 8266 8410 1732 -2627 -1227 C ATOM 570 CE1 PHE A 104 28.898 29.432 73.487 1.00 60.61 C ANISOU 570 CE1 PHE A 104 7224 7906 7898 1743 -2453 -973 C ATOM 571 CE2 PHE A 104 31.227 29.467 72.964 1.00 64.61 C ANISOU 571 CE2 PHE A 104 7244 8642 8664 1944 -2668 -1127 C ATOM 572 CZ PHE A 104 30.069 28.763 73.213 1.00 61.48 C ANISOU 572 CZ PHE A 104 7205 8097 8057 1942 -2579 -996 C ATOM 573 N GLY A 105 29.715 35.520 75.628 1.00 55.65 N ANISOU 573 N GLY A 105 5844 7499 7801 1085 -2684 -1642 N ATOM 574 CA GLY A 105 29.440 36.921 75.929 1.00 55.41 C ANISOU 574 CA GLY A 105 5734 7428 7893 894 -2655 -1767 C ATOM 575 C GLY A 105 28.140 37.495 75.410 1.00 56.60 C ANISOU 575 C GLY A 105 5992 7428 8087 741 -2419 -1685 C ATOM 576 O GLY A 105 27.355 36.803 74.758 1.00 53.97 O ANISOU 576 O GLY A 105 5792 7025 7689 766 -2263 -1524 O ATOM 577 N ASN A 106 27.915 38.791 75.711 1.00 53.96 N ANISOU 577 N ASN A 106 5595 7039 7869 586 -2402 -1807 N ATOM 578 CA ASN A 106 26.713 39.546 75.347 1.00 52.26 C ANISOU 578 CA ASN A 106 5463 6680 7713 451 -2205 -1764 C ATOM 579 C ASN A 106 26.586 39.893 73.865 1.00 54.25 C ANISOU 579 C ASN A 106 5572 6852 8190 349 -2018 -1647 C ATOM 580 O ASN A 106 25.462 39.912 73.356 1.00 52.14 O ANISOU 580 O ASN A 106 5422 6485 7904 313 -1850 -1538 O ATOM 581 CB ASN A 106 26.554 40.788 76.215 1.00 55.30 C ANISOU 581 CB ASN A 106 5849 7022 8140 345 -2262 -1945 C ATOM 582 CG ASN A 106 25.175 40.906 76.819 1.00 78.69 C ANISOU 582 CG ASN A 106 9059 9906 10935 340 -2161 -1937 C ATOM 583 OD1 ASN A 106 24.947 40.546 77.980 1.00 74.43 O ANISOU 583 OD1 ASN A 106 8701 9422 10158 420 -2255 -2004 O ATOM 584 ND2 ASN A 106 24.219 41.399 76.037 1.00 67.97 N ANISOU 584 ND2 ASN A 106 7711 8425 9690 253 -1964 -1855 N ATOM 585 N PHE A 107 27.718 40.173 73.176 1.00 51.32 N ANISOU 585 N PHE A 107 4945 6531 8023 302 -2045 -1671 N ATOM 586 CA PHE A 107 27.711 40.485 71.742 1.00 49.89 C ANISOU 586 CA PHE A 107 4634 6285 8037 205 -1865 -1554 C ATOM 587 C PHE A 107 27.331 39.258 70.902 1.00 51.91 C ANISOU 587 C PHE A 107 4983 6556 8184 317 -1760 -1374 C ATOM 588 O PHE A 107 26.501 39.370 69.997 1.00 49.61 O ANISOU 588 O PHE A 107 4751 6173 7928 262 -1589 -1250 O ATOM 589 CB PHE A 107 29.056 41.076 71.269 1.00 53.45 C ANISOU 589 CB PHE A 107 4786 6799 8724 112 -1902 -1633 C ATOM 590 CG PHE A 107 29.199 41.123 69.762 1.00 54.20 C ANISOU 590 CG PHE A 107 4761 6860 8972 43 -1714 -1492 C ATOM 591 CD1 PHE A 107 30.025 40.224 69.098 1.00 57.61 C ANISOU 591 CD1 PHE A 107 5062 7414 9412 136 -1707 -1436 C ATOM 592 CD2 PHE A 107 28.462 42.027 69.004 1.00 55.55 C ANISOU 592 CD2 PHE A 107 4970 6877 9260 -98 -1543 -1411 C ATOM 593 CE1 PHE A 107 30.130 40.242 67.704 1.00 57.92 C ANISOU 593 CE1 PHE A 107 5010 7431 9565 76 -1521 -1308 C ATOM 594 CE2 PHE A 107 28.565 42.045 67.611 1.00 57.81 C ANISOU 594 CE2 PHE A 107 5175 7136 9653 -154 -1371 -1270 C ATOM 595 CZ PHE A 107 29.401 41.154 66.970 1.00 56.21 C ANISOU 595 CZ PHE A 107 4844 7066 9447 -74 -1355 -1221 C ATOM 596 N LEU A 108 27.967 38.099 71.185 1.00 49.02 N ANISOU 596 N LEU A 108 4630 6304 7690 480 -1874 -1366 N ATOM 597 CA LEU A 108 27.734 36.840 70.475 1.00 47.36 C ANISOU 597 CA LEU A 108 4519 6104 7373 600 -1798 -1218 C ATOM 598 C LEU A 108 26.355 36.235 70.761 1.00 49.83 C ANISOU 598 C LEU A 108 5122 6330 7481 634 -1724 -1123 C ATOM 599 O LEU A 108 25.882 35.413 69.975 1.00 48.20 O ANISOU 599 O LEU A 108 5006 6091 7218 677 -1616 -994 O ATOM 600 CB LEU A 108 28.875 35.834 70.711 1.00 48.79 C ANISOU 600 CB LEU A 108 4627 6416 7495 778 -1951 -1249 C ATOM 601 CG LEU A 108 30.188 36.125 69.961 1.00 54.66 C ANISOU 601 CG LEU A 108 5050 7262 8457 756 -1957 -1302 C ATOM 602 CD1 LEU A 108 31.363 35.396 70.591 1.00 56.74 C ANISOU 602 CD1 LEU A 108 5211 7675 8673 939 -2168 -1396 C ATOM 603 CD2 LEU A 108 30.085 35.766 68.482 1.00 55.68 C ANISOU 603 CD2 LEU A 108 5131 7364 8660 740 -1759 -1166 C ATOM 604 N CYS A 109 25.691 36.673 71.855 1.00 46.90 N ANISOU 604 N CYS A 109 4891 5925 7006 601 -1771 -1196 N ATOM 605 CA CYS A 109 24.329 36.260 72.200 1.00 45.72 C ANISOU 605 CA CYS A 109 4992 5703 6679 602 -1680 -1126 C ATOM 606 C CYS A 109 23.384 36.979 71.251 1.00 47.42 C ANISOU 606 C CYS A 109 5172 5820 7026 474 -1495 -1061 C ATOM 607 O CYS A 109 22.400 36.389 70.810 1.00 45.64 O ANISOU 607 O CYS A 109 5076 5547 6717 476 -1377 -953 O ATOM 608 CB CYS A 109 24.012 36.577 73.659 1.00 47.53 C ANISOU 608 CB CYS A 109 5359 5944 6757 609 -1777 -1241 C ATOM 609 SG CYS A 109 22.292 36.259 74.139 1.00 50.60 S ANISOU 609 SG CYS A 109 6021 6257 6947 577 -1631 -1179 S ATOM 610 N LYS A 110 23.714 38.246 70.908 1.00 44.04 N ANISOU 610 N LYS A 110 4568 5358 6808 362 -1477 -1125 N ATOM 611 CA LYS A 110 22.972 39.072 69.952 1.00 42.49 C ANISOU 611 CA LYS A 110 4326 5059 6758 252 -1323 -1061 C ATOM 612 C LYS A 110 23.205 38.570 68.514 1.00 45.50 C ANISOU 612 C LYS A 110 4631 5448 7209 259 -1222 -921 C ATOM 613 O LYS A 110 22.266 38.567 67.719 1.00 43.38 O ANISOU 613 O LYS A 110 4422 5116 6944 230 -1096 -820 O ATOM 614 CB LYS A 110 23.377 40.551 70.083 1.00 45.25 C ANISOU 614 CB LYS A 110 4537 5350 7307 134 -1345 -1172 C ATOM 615 CG LYS A 110 22.338 41.391 70.810 1.00 50.16 C ANISOU 615 CG LYS A 110 5268 5882 7909 88 -1319 -1251 C ATOM 616 CD LYS A 110 22.884 42.743 71.217 1.00 54.73 C ANISOU 616 CD LYS A 110 5738 6398 8660 -14 -1380 -1397 C ATOM 617 CE LYS A 110 22.865 42.925 72.714 1.00 58.89 C ANISOU 617 CE LYS A 110 6354 6960 9062 14 -1507 -1569 C ATOM 618 NZ LYS A 110 21.488 43.133 73.238 1.00 62.85 N ANISOU 618 NZ LYS A 110 7026 7399 9454 32 -1426 -1589 N ATOM 619 N ALA A 111 24.446 38.121 68.202 1.00 43.21 N ANISOU 619 N ALA A 111 4207 5245 6965 309 -1283 -927 N ATOM 620 CA ALA A 111 24.867 37.619 66.890 1.00 42.68 C ANISOU 620 CA ALA A 111 4055 5206 6956 327 -1190 -818 C ATOM 621 C ALA A 111 24.151 36.340 66.466 1.00 46.02 C ANISOU 621 C ALA A 111 4649 5626 7211 422 -1132 -705 C ATOM 622 O ALA A 111 23.687 36.260 65.325 1.00 44.73 O ANISOU 622 O ALA A 111 4492 5426 7076 390 -1005 -601 O ATOM 623 CB ALA A 111 26.376 37.416 66.859 1.00 44.93 C ANISOU 623 CB ALA A 111 4145 5605 7323 374 -1277 -882 C ATOM 624 N VAL A 112 24.057 35.345 67.375 1.00 43.23 N ANISOU 624 N VAL A 112 4446 5303 6678 534 -1226 -726 N ATOM 625 CA VAL A 112 23.415 34.047 67.103 1.00 42.40 C ANISOU 625 CA VAL A 112 4527 5175 6408 615 -1179 -630 C ATOM 626 C VAL A 112 21.899 34.156 66.889 1.00 45.40 C ANISOU 626 C VAL A 112 5044 5473 6733 532 -1061 -567 C ATOM 627 O VAL A 112 21.348 33.444 66.048 1.00 44.13 O ANISOU 627 O VAL A 112 4958 5286 6525 540 -973 -476 O ATOM 628 CB VAL A 112 23.793 32.926 68.107 1.00 47.23 C ANISOU 628 CB VAL A 112 5284 5823 6841 759 -1310 -655 C ATOM 629 CG1 VAL A 112 25.298 32.658 68.104 1.00 48.46 C ANISOU 629 CG1 VAL A 112 5281 6075 7057 874 -1430 -710 C ATOM 630 CG2 VAL A 112 23.294 33.236 69.516 1.00 47.63 C ANISOU 630 CG2 VAL A 112 5463 5861 6775 741 -1386 -727 C ATOM 631 N HIS A 113 21.237 35.046 67.649 1.00 42.34 N ANISOU 631 N HIS A 113 4679 5051 6357 456 -1062 -630 N ATOM 632 CA HIS A 113 19.804 35.296 67.553 1.00 41.66 C ANISOU 632 CA HIS A 113 4685 4903 6241 384 -957 -597 C ATOM 633 C HIS A 113 19.487 35.998 66.225 1.00 46.21 C ANISOU 633 C HIS A 113 5149 5440 6970 315 -855 -529 C ATOM 634 O HIS A 113 18.521 35.611 65.565 1.00 45.15 O ANISOU 634 O HIS A 113 5081 5282 6793 297 -769 -455 O ATOM 635 CB HIS A 113 19.318 36.131 68.745 1.00 43.08 C ANISOU 635 CB HIS A 113 4901 5066 6402 342 -988 -704 C ATOM 636 CG HIS A 113 19.038 35.338 69.982 1.00 47.05 C ANISOU 636 CG HIS A 113 5587 5595 6695 393 -1038 -739 C ATOM 637 ND1 HIS A 113 17.745 35.084 70.394 1.00 48.49 N ANISOU 637 ND1 HIS A 113 5909 5754 6762 354 -947 -728 N ATOM 638 CD2 HIS A 113 19.895 34.781 70.866 1.00 49.86 C ANISOU 638 CD2 HIS A 113 6008 6001 6936 479 -1167 -782 C ATOM 639 CE1 HIS A 113 17.852 34.378 71.508 1.00 48.78 C ANISOU 639 CE1 HIS A 113 6108 5818 6607 405 -1006 -754 C ATOM 640 NE2 HIS A 113 19.130 34.177 71.835 1.00 50.03 N ANISOU 640 NE2 HIS A 113 6237 6019 6754 491 -1150 -785 N ATOM 641 N VAL A 114 20.322 37.006 65.828 1.00 43.96 N ANISOU 641 N VAL A 114 4699 5148 6857 271 -867 -554 N ATOM 642 CA VAL A 114 20.221 37.783 64.577 1.00 43.51 C ANISOU 642 CA VAL A 114 4545 5045 6944 205 -775 -479 C ATOM 643 C VAL A 114 20.328 36.839 63.374 1.00 47.88 C ANISOU 643 C VAL A 114 5112 5634 7446 247 -710 -369 C ATOM 644 O VAL A 114 19.476 36.887 62.483 1.00 46.62 O ANISOU 644 O VAL A 114 4991 5442 7282 223 -629 -287 O ATOM 645 CB VAL A 114 21.244 38.960 64.523 1.00 48.20 C ANISOU 645 CB VAL A 114 4974 5616 7722 135 -798 -531 C ATOM 646 CG1 VAL A 114 21.528 39.421 63.093 1.00 47.88 C ANISOU 646 CG1 VAL A 114 4844 5548 7799 80 -695 -425 C ATOM 647 CG2 VAL A 114 20.767 40.134 65.368 1.00 48.56 C ANISOU 647 CG2 VAL A 114 5028 5580 7841 73 -827 -625 C ATOM 648 N ILE A 115 21.353 35.959 63.385 1.00 45.90 N ANISOU 648 N ILE A 115 4834 5455 7150 323 -756 -378 N ATOM 649 CA ILE A 115 21.610 34.939 62.363 1.00 45.81 C ANISOU 649 CA ILE A 115 4844 5483 7078 385 -703 -300 C ATOM 650 C ILE A 115 20.431 33.931 62.284 1.00 49.59 C ANISOU 650 C ILE A 115 5510 5931 7399 412 -673 -252 C ATOM 651 O ILE A 115 20.077 33.495 61.185 1.00 48.77 O ANISOU 651 O ILE A 115 5438 5826 7265 413 -599 -178 O ATOM 652 CB ILE A 115 23.019 34.295 62.586 1.00 50.01 C ANISOU 652 CB ILE A 115 5293 6099 7611 482 -775 -349 C ATOM 653 CG1 ILE A 115 24.127 35.236 62.055 1.00 51.48 C ANISOU 653 CG1 ILE A 115 5256 6329 7976 422 -746 -369 C ATOM 654 CG2 ILE A 115 23.139 32.907 61.949 1.00 50.77 C ANISOU 654 CG2 ILE A 115 5479 6221 7591 590 -750 -297 C ATOM 655 CD1 ILE A 115 25.509 35.062 62.663 1.00 59.78 C ANISOU 655 CD1 ILE A 115 6161 7474 9078 489 -850 -466 C ATOM 656 N TYR A 116 19.800 33.615 63.440 1.00 46.54 N ANISOU 656 N TYR A 116 5247 5524 6914 419 -724 -298 N ATOM 657 CA TYR A 116 18.641 32.721 63.512 1.00 45.94 C ANISOU 657 CA TYR A 116 5341 5415 6700 413 -685 -264 C ATOM 658 C TYR A 116 17.419 33.352 62.839 1.00 49.26 C ANISOU 658 C TYR A 116 5743 5806 7168 326 -601 -227 C ATOM 659 O TYR A 116 16.653 32.642 62.186 1.00 48.11 O ANISOU 659 O TYR A 116 5675 5652 6952 312 -550 -179 O ATOM 660 CB TYR A 116 18.322 32.340 64.969 1.00 47.68 C ANISOU 660 CB TYR A 116 5693 5624 6799 427 -742 -322 C ATOM 661 CG TYR A 116 17.214 31.316 65.116 1.00 49.37 C ANISOU 661 CG TYR A 116 6089 5801 6868 402 -687 -287 C ATOM 662 CD1 TYR A 116 17.426 29.980 64.786 1.00 51.49 C ANISOU 662 CD1 TYR A 116 6486 6047 7033 461 -688 -239 C ATOM 663 CD2 TYR A 116 15.970 31.676 65.623 1.00 50.07 C ANISOU 663 CD2 TYR A 116 6220 5875 6928 315 -630 -311 C ATOM 664 CE1 TYR A 116 16.416 29.031 64.931 1.00 52.30 C ANISOU 664 CE1 TYR A 116 6762 6099 7010 412 -632 -210 C ATOM 665 CE2 TYR A 116 14.952 30.733 65.777 1.00 51.08 C ANISOU 665 CE2 TYR A 116 6498 5977 6933 266 -566 -286 C ATOM 666 CZ TYR A 116 15.182 29.409 65.433 1.00 58.90 C ANISOU 666 CZ TYR A 116 7623 6932 7824 305 -567 -233 C ATOM 667 OH TYR A 116 14.184 28.473 65.576 1.00 59.94 O ANISOU 667 OH TYR A 116 7909 7021 7843 232 -498 -211 O ATOM 668 N THR A 117 17.251 34.685 62.997 1.00 46.08 N ANISOU 668 N THR A 117 5240 5383 6887 274 -598 -257 N ATOM 669 CA THR A 117 16.156 35.468 62.415 1.00 45.45 C ANISOU 669 CA THR A 117 5128 5269 6871 218 -539 -228 C ATOM 670 C THR A 117 16.337 35.601 60.893 1.00 49.18 C ANISOU 670 C THR A 117 5545 5744 7396 216 -491 -132 C ATOM 671 O THR A 117 15.351 35.488 60.155 1.00 48.15 O ANISOU 671 O THR A 117 5444 5613 7238 201 -452 -85 O ATOM 672 CB THR A 117 16.002 36.806 63.155 1.00 52.90 C ANISOU 672 CB THR A 117 6006 6169 7924 183 -559 -298 C ATOM 673 OG1 THR A 117 15.883 36.554 64.554 1.00 52.10 O ANISOU 673 OG1 THR A 117 5975 6081 7738 191 -600 -390 O ATOM 674 CG2 THR A 117 14.793 37.606 62.689 1.00 51.61 C ANISOU 674 CG2 THR A 117 5819 5965 7826 154 -511 -278 C ATOM 675 N VAL A 118 17.597 35.820 60.427 1.00 46.32 N ANISOU 675 N VAL A 118 5099 5398 7101 231 -492 -110 N ATOM 676 CA VAL A 118 17.926 35.919 58.998 1.00 46.26 C ANISOU 676 CA VAL A 118 5049 5405 7124 229 -429 -17 C ATOM 677 C VAL A 118 17.593 34.571 58.333 1.00 50.20 C ANISOU 677 C VAL A 118 5648 5945 7480 274 -407 18 C ATOM 678 O VAL A 118 16.750 34.538 57.443 1.00 49.41 O ANISOU 678 O VAL A 118 5587 5843 7344 259 -372 74 O ATOM 679 CB VAL A 118 19.387 36.385 58.704 1.00 50.75 C ANISOU 679 CB VAL A 118 5493 5996 7795 221 -413 -12 C ATOM 680 CG1 VAL A 118 19.659 36.456 57.200 1.00 50.74 C ANISOU 680 CG1 VAL A 118 5467 6015 7796 213 -322 90 C ATOM 681 CG2 VAL A 118 19.682 37.730 59.346 1.00 51.20 C ANISOU 681 CG2 VAL A 118 5459 5994 8001 154 -436 -59 C ATOM 682 N ASN A 119 18.198 33.466 58.817 1.00 47.44 N ANISOU 682 N ASN A 119 5351 5624 7049 335 -440 -22 N ATOM 683 CA ASN A 119 17.984 32.105 58.313 1.00 47.36 C ANISOU 683 CA ASN A 119 5460 5628 6909 382 -425 -4 C ATOM 684 C ASN A 119 16.514 31.678 58.315 1.00 51.69 C ANISOU 684 C ASN A 119 6117 6147 7374 332 -415 -1 C ATOM 685 O ASN A 119 16.093 30.984 57.390 1.00 51.18 O ANISOU 685 O ASN A 119 6118 6092 7237 333 -385 30 O ATOM 686 CB ASN A 119 18.820 31.103 59.103 1.00 48.00 C ANISOU 686 CB ASN A 119 5597 5715 6925 468 -480 -53 C ATOM 687 CG ASN A 119 18.620 29.668 58.684 1.00 67.92 C ANISOU 687 CG ASN A 119 8269 8221 9318 521 -468 -43 C ATOM 688 OD1 ASN A 119 17.851 28.915 59.293 1.00 63.12 O ANISOU 688 OD1 ASN A 119 7806 7563 8615 503 -486 -58 O ATOM 689 ND2 ASN A 119 19.300 29.266 57.624 1.00 58.45 N ANISOU 689 ND2 ASN A 119 7043 7055 8110 580 -427 -21 N ATOM 690 N LEU A 120 15.745 32.070 59.349 1.00 48.86 N ANISOU 690 N LEU A 120 5773 5764 7027 285 -437 -44 N ATOM 691 CA LEU A 120 14.332 31.708 59.462 1.00 48.67 C ANISOU 691 CA LEU A 120 5821 5729 6941 224 -417 -56 C ATOM 692 C LEU A 120 13.471 32.315 58.358 1.00 52.43 C ANISOU 692 C LEU A 120 6235 6225 7462 190 -392 -14 C ATOM 693 O LEU A 120 12.857 31.568 57.594 1.00 52.11 O ANISOU 693 O LEU A 120 6251 6201 7347 172 -378 1 O ATOM 694 CB LEU A 120 13.777 32.040 60.860 1.00 48.87 C ANISOU 694 CB LEU A 120 5863 5739 6965 187 -429 -121 C ATOM 695 CG LEU A 120 13.091 30.897 61.616 1.00 54.05 C ANISOU 695 CG LEU A 120 6666 6379 7491 148 -411 -150 C ATOM 696 CD1 LEU A 120 14.068 29.766 61.945 1.00 54.93 C ANISOU 696 CD1 LEU A 120 6905 6461 7505 215 -444 -140 C ATOM 697 CD2 LEU A 120 12.482 31.399 62.901 1.00 57.00 C ANISOU 697 CD2 LEU A 120 7044 6754 7860 106 -400 -213 C ATOM 698 N TYR A 121 13.452 33.652 58.243 1.00 48.86 N ANISOU 698 N TYR A 121 5676 5763 7126 187 -395 3 N ATOM 699 CA TYR A 121 12.624 34.321 57.244 1.00 48.81 C ANISOU 699 CA TYR A 121 5622 5766 7158 178 -388 51 C ATOM 700 C TYR A 121 13.153 34.285 55.821 1.00 52.02 C ANISOU 700 C TYR A 121 6031 6194 7542 207 -369 138 C ATOM 701 O TYR A 121 12.351 34.135 54.901 1.00 51.95 O ANISOU 701 O TYR A 121 6042 6216 7483 205 -376 170 O ATOM 702 CB TYR A 121 12.191 35.729 57.691 1.00 50.77 C ANISOU 702 CB TYR A 121 5786 5974 7532 174 -400 36 C ATOM 703 CG TYR A 121 11.570 35.767 59.076 1.00 53.13 C ANISOU 703 CG TYR A 121 6087 6265 7835 148 -405 -62 C ATOM 704 CD1 TYR A 121 10.535 34.901 59.423 1.00 55.19 C ANISOU 704 CD1 TYR A 121 6391 6568 8009 110 -388 -110 C ATOM 705 CD2 TYR A 121 12.012 36.676 60.032 1.00 54.28 C ANISOU 705 CD2 TYR A 121 6192 6364 8067 152 -417 -113 C ATOM 706 CE1 TYR A 121 9.981 34.915 60.703 1.00 56.47 C ANISOU 706 CE1 TYR A 121 6563 6733 8158 79 -369 -197 C ATOM 707 CE2 TYR A 121 11.447 36.715 61.306 1.00 55.41 C ANISOU 707 CE2 TYR A 121 6350 6510 8193 133 -412 -210 C ATOM 708 CZ TYR A 121 10.435 35.829 61.638 1.00 63.49 C ANISOU 708 CZ TYR A 121 7422 7584 9118 98 -381 -247 C ATOM 709 OH TYR A 121 9.885 35.858 62.895 1.00 65.88 O ANISOU 709 OH TYR A 121 7746 7898 9387 72 -354 -338 O ATOM 710 N SER A 122 14.483 34.383 55.631 1.00 47.86 N ANISOU 710 N SER A 122 5480 5664 7042 232 -344 167 N ATOM 711 CA SER A 122 15.088 34.338 54.296 1.00 47.42 C ANISOU 711 CA SER A 122 5428 5639 6952 256 -300 246 C ATOM 712 C SER A 122 14.837 32.992 53.608 1.00 49.17 C ANISOU 712 C SER A 122 5747 5906 7028 279 -295 237 C ATOM 713 O SER A 122 14.182 32.988 52.564 1.00 49.07 O ANISOU 713 O SER A 122 5767 5922 6954 278 -295 280 O ATOM 714 CB SER A 122 16.580 34.664 54.339 1.00 51.38 C ANISOU 714 CB SER A 122 5857 6143 7522 268 -260 260 C ATOM 715 OG SER A 122 17.330 33.623 54.945 1.00 59.73 O ANISOU 715 OG SER A 122 6934 7227 8533 310 -273 195 O ATOM 716 N SER A 123 15.286 31.859 54.220 1.00 43.68 N ANISOU 716 N SER A 123 5112 5210 6274 303 -301 176 N ATOM 717 CA SER A 123 15.115 30.507 53.669 1.00 42.86 C ANISOU 717 CA SER A 123 5124 5120 6040 325 -296 152 C ATOM 718 C SER A 123 13.702 30.235 53.163 1.00 45.26 C ANISOU 718 C SER A 123 5482 5436 6280 271 -321 144 C ATOM 719 O SER A 123 13.549 29.821 52.014 1.00 45.66 O ANISOU 719 O SER A 123 5582 5522 6245 283 -312 162 O ATOM 720 CB SER A 123 15.559 29.428 54.659 1.00 45.65 C ANISOU 720 CB SER A 123 5558 5435 6352 357 -316 89 C ATOM 721 OG SER A 123 14.679 29.314 55.761 1.00 52.11 O ANISOU 721 OG SER A 123 6417 6214 7170 298 -348 47 O ATOM 722 N VAL A 124 12.677 30.534 53.985 1.00 39.85 N ANISOU 722 N VAL A 124 4772 4734 5637 211 -352 109 N ATOM 723 CA VAL A 124 11.283 30.340 53.590 1.00 39.15 C ANISOU 723 CA VAL A 124 4693 4674 5510 153 -381 84 C ATOM 724 C VAL A 124 10.860 31.268 52.436 1.00 41.34 C ANISOU 724 C VAL A 124 4905 4999 5802 177 -405 147 C ATOM 725 O VAL A 124 10.255 30.786 51.478 1.00 41.47 O ANISOU 725 O VAL A 124 4962 5062 5733 167 -433 142 O ATOM 726 CB VAL A 124 10.286 30.266 54.785 1.00 43.07 C ANISOU 726 CB VAL A 124 5172 5154 6037 80 -388 15 C ATOM 727 CG1 VAL A 124 10.113 31.610 55.493 1.00 42.74 C ANISOU 727 CG1 VAL A 124 5017 5107 6117 90 -394 21 C ATOM 728 CG2 VAL A 124 8.942 29.680 54.360 1.00 43.37 C ANISOU 728 CG2 VAL A 124 5220 5234 6024 3 -409 -34 C ATOM 729 N TRP A 125 11.251 32.563 52.493 1.00 36.08 N ANISOU 729 N TRP A 125 4157 4315 5238 210 -399 209 N ATOM 730 CA TRP A 125 10.936 33.543 51.451 1.00 35.60 C ANISOU 730 CA TRP A 125 4061 4274 5190 244 -421 291 C ATOM 731 C TRP A 125 11.681 33.337 50.128 1.00 39.73 C ANISOU 731 C TRP A 125 4649 4832 5615 283 -387 367 C ATOM 732 O TRP A 125 11.150 33.732 49.088 1.00 39.97 O ANISOU 732 O TRP A 125 4697 4898 5590 309 -421 426 O ATOM 733 CB TRP A 125 10.999 34.988 51.962 1.00 33.94 C ANISOU 733 CB TRP A 125 3768 4005 5124 260 -423 331 C ATOM 734 CG TRP A 125 9.755 35.397 52.696 1.00 34.59 C ANISOU 734 CG TRP A 125 3785 4084 5274 248 -473 267 C ATOM 735 CD1 TRP A 125 9.558 35.394 54.045 1.00 36.88 C ANISOU 735 CD1 TRP A 125 4037 4348 5628 214 -462 181 C ATOM 736 CD2 TRP A 125 8.512 35.802 52.108 1.00 34.99 C ANISOU 736 CD2 TRP A 125 3795 4175 5324 278 -541 273 C ATOM 737 NE1 TRP A 125 8.276 35.795 54.337 1.00 36.47 N ANISOU 737 NE1 TRP A 125 3915 4319 5623 216 -500 129 N ATOM 738 CE2 TRP A 125 7.608 36.045 53.168 1.00 38.66 C ANISOU 738 CE2 TRP A 125 4180 4640 5872 260 -556 181 C ATOM 739 CE3 TRP A 125 8.073 35.991 50.786 1.00 37.09 C ANISOU 739 CE3 TRP A 125 4085 4486 5520 328 -596 344 C ATOM 740 CZ2 TRP A 125 6.295 36.472 52.948 1.00 38.75 C ANISOU 740 CZ2 TRP A 125 4108 4699 5917 295 -623 150 C ATOM 741 CZ3 TRP A 125 6.770 36.408 50.569 1.00 39.30 C ANISOU 741 CZ3 TRP A 125 4296 4810 5826 367 -682 320 C ATOM 742 CH2 TRP A 125 5.897 36.644 51.640 1.00 39.92 C ANISOU 742 CH2 TRP A 125 4270 4893 6007 353 -694 220 C ATOM 743 N ILE A 126 12.879 32.684 50.153 1.00 36.04 N ANISOU 743 N ILE A 126 4217 4362 5114 296 -322 359 N ATOM 744 CA ILE A 126 13.628 32.336 48.930 1.00 36.49 C ANISOU 744 CA ILE A 126 4334 4466 5064 335 -266 409 C ATOM 745 C ILE A 126 12.806 31.246 48.225 1.00 39.97 C ANISOU 745 C ILE A 126 4873 4956 5360 332 -312 354 C ATOM 746 O ILE A 126 12.613 31.311 47.012 1.00 40.52 O ANISOU 746 O ILE A 126 4995 5080 5322 357 -318 401 O ATOM 747 CB ILE A 126 15.103 31.884 49.174 1.00 39.52 C ANISOU 747 CB ILE A 126 4707 4848 5462 365 -185 392 C ATOM 748 CG1 ILE A 126 15.930 32.972 49.872 1.00 39.79 C ANISOU 748 CG1 ILE A 126 4627 4843 5649 349 -149 429 C ATOM 749 CG2 ILE A 126 15.788 31.471 47.856 1.00 41.06 C ANISOU 749 CG2 ILE A 126 4961 5108 5533 410 -110 429 C ATOM 750 CD1 ILE A 126 17.086 32.435 50.713 1.00 47.02 C ANISOU 750 CD1 ILE A 126 5497 5756 6614 375 -123 364 C ATOM 751 N LEU A 127 12.271 30.286 49.009 1.00 35.06 N ANISOU 751 N LEU A 127 4282 4309 4730 292 -348 255 N ATOM 752 CA LEU A 127 11.415 29.217 48.503 1.00 34.97 C ANISOU 752 CA LEU A 127 4359 4325 4605 259 -395 182 C ATOM 753 C LEU A 127 10.091 29.768 47.949 1.00 39.95 C ANISOU 753 C LEU A 127 4943 5013 5222 232 -481 190 C ATOM 754 O LEU A 127 9.511 29.152 47.054 1.00 40.56 O ANISOU 754 O LEU A 127 5083 5143 5184 220 -529 151 O ATOM 755 CB LEU A 127 11.174 28.128 49.564 1.00 34.33 C ANISOU 755 CB LEU A 127 4331 4182 4532 203 -397 86 C ATOM 756 CG LEU A 127 12.400 27.332 50.036 1.00 38.24 C ANISOU 756 CG LEU A 127 4899 4617 5012 254 -340 65 C ATOM 757 CD1 LEU A 127 12.055 26.475 51.204 1.00 37.54 C ANISOU 757 CD1 LEU A 127 4878 4452 4935 199 -350 -3 C ATOM 758 CD2 LEU A 127 12.978 26.471 48.930 1.00 41.58 C ANISOU 758 CD2 LEU A 127 5429 5059 5311 312 -310 45 C ATOM 759 N ALA A 128 9.637 30.943 48.453 1.00 36.37 N ANISOU 759 N ALA A 128 4381 4552 4888 234 -508 233 N ATOM 760 CA ALA A 128 8.433 31.624 47.967 1.00 36.98 C ANISOU 760 CA ALA A 128 4394 4683 4972 243 -600 247 C ATOM 761 C ALA A 128 8.727 32.239 46.593 1.00 42.24 C ANISOU 761 C ALA A 128 5111 5391 5547 319 -616 356 C ATOM 762 O ALA A 128 7.848 32.269 45.731 1.00 42.75 O ANISOU 762 O ALA A 128 5184 5528 5529 340 -709 354 O ATOM 763 CB ALA A 128 7.990 32.695 48.952 1.00 37.26 C ANISOU 763 CB ALA A 128 4312 4680 5165 246 -613 255 C ATOM 764 N PHE A 129 9.980 32.693 46.386 1.00 38.83 N ANISOU 764 N PHE A 129 4712 4920 5121 355 -523 447 N ATOM 765 CA PHE A 129 10.447 33.247 45.119 1.00 39.78 C ANISOU 765 CA PHE A 129 4902 5072 5141 413 -499 565 C ATOM 766 C PHE A 129 10.658 32.135 44.083 1.00 44.41 C ANISOU 766 C PHE A 129 5604 5733 5535 423 -486 526 C ATOM 767 O PHE A 129 10.481 32.392 42.891 1.00 45.02 O ANISOU 767 O PHE A 129 5757 5872 5477 468 -515 593 O ATOM 768 CB PHE A 129 11.725 34.073 45.314 1.00 41.49 C ANISOU 768 CB PHE A 129 5097 5224 5442 420 -383 662 C ATOM 769 CG PHE A 129 11.488 35.552 45.513 1.00 43.43 C ANISOU 769 CG PHE A 129 5291 5399 5811 436 -404 761 C ATOM 770 CD1 PHE A 129 11.157 36.058 46.764 1.00 45.73 C ANISOU 770 CD1 PHE A 129 5482 5619 6273 413 -432 711 C ATOM 771 CD2 PHE A 129 11.609 36.441 44.450 1.00 46.90 C ANISOU 771 CD2 PHE A 129 5800 5832 6187 478 -391 904 C ATOM 772 CE1 PHE A 129 10.941 37.428 46.948 1.00 47.25 C ANISOU 772 CE1 PHE A 129 5641 5728 6585 437 -453 790 C ATOM 773 CE2 PHE A 129 11.391 37.810 44.633 1.00 50.36 C ANISOU 773 CE2 PHE A 129 6217 6175 6744 499 -412 1000 C ATOM 774 CZ PHE A 129 11.058 38.295 45.880 1.00 47.75 C ANISOU 774 CZ PHE A 129 5781 5767 6596 481 -445 936 C ATOM 775 N ILE A 130 11.023 30.902 44.534 1.00 40.50 N ANISOU 775 N ILE A 130 5141 5227 5020 389 -448 415 N ATOM 776 CA ILE A 130 11.209 29.737 43.652 1.00 41.06 C ANISOU 776 CA ILE A 130 5333 5348 4919 401 -436 349 C ATOM 777 C ILE A 130 9.834 29.295 43.119 1.00 47.32 C ANISOU 777 C ILE A 130 6156 6203 5621 370 -571 274 C ATOM 778 O ILE A 130 9.728 28.835 41.980 1.00 48.45 O ANISOU 778 O ILE A 130 6402 6416 5592 395 -599 254 O ATOM 779 CB ILE A 130 12.032 28.577 44.295 1.00 42.94 C ANISOU 779 CB ILE A 130 5612 5532 5171 393 -361 257 C ATOM 780 CG1 ILE A 130 13.409 29.071 44.761 1.00 42.43 C ANISOU 780 CG1 ILE A 130 5489 5433 5200 433 -245 321 C ATOM 781 CG2 ILE A 130 12.219 27.425 43.309 1.00 44.78 C ANISOU 781 CG2 ILE A 130 5985 5803 5226 419 -346 180 C ATOM 782 CD1 ILE A 130 14.205 28.106 45.626 1.00 47.50 C ANISOU 782 CD1 ILE A 130 6145 6017 5888 449 -197 238 C ATOM 783 N SER A 131 8.781 29.492 43.931 1.00 43.97 N ANISOU 783 N SER A 131 5631 5765 5311 314 -654 227 N ATOM 784 CA SER A 131 7.401 29.211 43.547 1.00 44.91 C ANISOU 784 CA SER A 131 5724 5957 5382 275 -789 147 C ATOM 785 C SER A 131 6.954 30.289 42.543 1.00 50.04 C ANISOU 785 C SER A 131 6362 6685 5968 360 -878 250 C ATOM 786 O SER A 131 6.306 29.962 41.544 1.00 50.86 O ANISOU 786 O SER A 131 6516 6881 5928 374 -982 211 O ATOM 787 CB SER A 131 6.496 29.216 44.775 1.00 47.84 C ANISOU 787 CB SER A 131 5968 6300 5909 194 -824 71 C ATOM 788 OG SER A 131 6.944 28.273 45.733 1.00 55.99 O ANISOU 788 OG SER A 131 7040 7248 6985 122 -740 -1 O ATOM 789 N LEU A 132 7.334 31.569 42.799 1.00 46.12 N ANISOU 789 N LEU A 132 5812 6141 5569 420 -841 382 N ATOM 790 CA LEU A 132 7.032 32.721 41.939 1.00 46.82 C ANISOU 790 CA LEU A 132 5916 6265 5609 514 -912 511 C ATOM 791 C LEU A 132 7.749 32.594 40.592 1.00 51.64 C ANISOU 791 C LEU A 132 6687 6925 6008 566 -870 593 C ATOM 792 O LEU A 132 7.171 32.947 39.561 1.00 52.87 O ANISOU 792 O LEU A 132 6903 7157 6026 634 -977 646 O ATOM 793 CB LEU A 132 7.416 34.044 42.628 1.00 46.07 C ANISOU 793 CB LEU A 132 5752 6068 5682 548 -858 627 C ATOM 794 CG LEU A 132 6.272 34.894 43.177 1.00 50.38 C ANISOU 794 CG LEU A 132 6172 6605 6366 584 -972 617 C ATOM 795 CD1 LEU A 132 6.726 35.705 44.377 1.00 49.23 C ANISOU 795 CD1 LEU A 132 5945 6338 6421 569 -889 645 C ATOM 796 CD2 LEU A 132 5.711 35.815 42.111 1.00 54.35 C ANISOU 796 CD2 LEU A 132 6723 7144 6785 701 -1089 732 C ATOM 797 N ASP A 133 8.995 32.070 40.603 1.00 47.19 N ANISOU 797 N ASP A 133 6190 6329 5410 543 -716 596 N ATOM 798 CA ASP A 133 9.799 31.867 39.399 1.00 48.07 C ANISOU 798 CA ASP A 133 6448 6495 5322 587 -636 657 C ATOM 799 C ASP A 133 9.243 30.731 38.566 1.00 52.43 C ANISOU 799 C ASP A 133 7097 7144 5681 584 -722 533 C ATOM 800 O ASP A 133 9.297 30.798 37.340 1.00 53.60 O ANISOU 800 O ASP A 133 7370 7372 5622 641 -738 585 O ATOM 801 CB ASP A 133 11.266 31.599 39.741 1.00 49.35 C ANISOU 801 CB ASP A 133 6616 6607 5528 569 -446 670 C ATOM 802 CG ASP A 133 12.172 31.693 38.534 1.00 61.98 C ANISOU 802 CG ASP A 133 8340 8266 6943 616 -329 758 C ATOM 803 OD1 ASP A 133 12.412 30.648 37.890 1.00 63.50 O ANISOU 803 OD1 ASP A 133 8629 8522 6974 632 -300 666 O ATOM 804 OD2 ASP A 133 12.593 32.822 38.196 1.00 68.24 O ANISOU 804 OD2 ASP A 133 9145 9039 7745 635 -262 918 O ATOM 805 N ARG A 134 8.712 29.692 39.230 1.00 48.30 N ANISOU 805 N ARG A 134 6529 6606 5218 511 -774 370 N ATOM 806 CA ARG A 134 8.111 28.535 38.572 1.00 49.04 C ANISOU 806 CA ARG A 134 6708 6769 5158 481 -862 223 C ATOM 807 C ARG A 134 6.769 28.907 37.952 1.00 54.70 C ANISOU 807 C ARG A 134 7393 7587 5804 497 -1060 209 C ATOM 808 O ARG A 134 6.388 28.341 36.926 1.00 55.54 O ANISOU 808 O ARG A 134 7601 7786 5716 509 -1148 138 O ATOM 809 CB ARG A 134 7.965 27.362 39.550 1.00 46.92 C ANISOU 809 CB ARG A 134 6410 6426 4993 381 -845 65 C ATOM 810 CG ARG A 134 8.089 26.004 38.877 1.00 55.03 C ANISOU 810 CG ARG A 134 7585 7467 5857 357 -844 -75 C ATOM 811 CD ARG A 134 9.507 25.462 38.847 1.00 59.19 C ANISOU 811 CD ARG A 134 8212 7935 6344 409 -675 -71 C ATOM 812 NE ARG A 134 10.381 26.175 37.914 1.00 62.97 N ANISOU 812 NE ARG A 134 8747 8480 6698 509 -584 56 N ATOM 813 CZ ARG A 134 10.599 25.807 36.657 1.00 78.45 C ANISOU 813 CZ ARG A 134 10852 10525 8431 562 -573 30 C ATOM 814 NH1 ARG A 134 11.413 26.513 35.884 1.00 66.98 N ANISOU 814 NH1 ARG A 134 9449 9132 6868 641 -465 159 N ATOM 815 NH2 ARG A 134 10.003 24.729 36.160 1.00 67.43 N ANISOU 815 NH2 ARG A 134 9559 9152 6910 528 -663 -131 N ATOM 816 N TYR A 135 6.069 29.876 38.573 1.00 51.68 N ANISOU 816 N TYR A 135 6865 7190 5579 509 -1134 268 N ATOM 817 CA TYR A 135 4.797 30.410 38.097 1.00 53.41 C ANISOU 817 CA TYR A 135 7018 7508 5768 554 -1331 264 C ATOM 818 C TYR A 135 5.027 31.189 36.795 1.00 60.12 C ANISOU 818 C TYR A 135 8003 8421 6418 680 -1373 415 C ATOM 819 O TYR A 135 4.234 31.057 35.865 1.00 61.86 O ANISOU 819 O TYR A 135 8266 8761 6478 724 -1540 375 O ATOM 820 CB TYR A 135 4.127 31.269 39.196 1.00 53.81 C ANISOU 820 CB TYR A 135 6878 7511 6055 552 -1371 285 C ATOM 821 CG TYR A 135 3.265 32.413 38.710 1.00 57.39 C ANISOU 821 CG TYR A 135 7275 8026 6505 671 -1531 374 C ATOM 822 CD1 TYR A 135 1.985 32.191 38.203 1.00 61.03 C ANISOU 822 CD1 TYR A 135 7659 8621 6907 689 -1736 270 C ATOM 823 CD2 TYR A 135 3.699 33.734 38.809 1.00 58.34 C ANISOU 823 CD2 TYR A 135 7408 8063 6695 768 -1485 554 C ATOM 824 CE1 TYR A 135 1.183 33.242 37.765 1.00 63.57 C ANISOU 824 CE1 TYR A 135 7925 9002 7228 826 -1901 349 C ATOM 825 CE2 TYR A 135 2.905 34.797 38.384 1.00 60.97 C ANISOU 825 CE2 TYR A 135 7709 8429 7030 898 -1638 641 C ATOM 826 CZ TYR A 135 1.647 34.546 37.861 1.00 70.35 C ANISOU 826 CZ TYR A 135 8822 9759 8150 939 -1851 540 C ATOM 827 OH TYR A 135 0.862 35.593 37.437 1.00 72.90 O ANISOU 827 OH TYR A 135 9110 10117 8473 1095 -2020 626 O ATOM 828 N LEU A 136 6.127 31.959 36.716 1.00 56.75 N ANISOU 828 N LEU A 136 7651 7919 5992 730 -1222 585 N ATOM 829 CA LEU A 136 6.465 32.742 35.525 1.00 58.55 C ANISOU 829 CA LEU A 136 8034 8188 6026 835 -1222 755 C ATOM 830 C LEU A 136 7.007 31.869 34.387 1.00 64.66 C ANISOU 830 C LEU A 136 8991 9051 6528 841 -1171 714 C ATOM 831 O LEU A 136 6.655 32.104 33.228 1.00 66.38 O ANISOU 831 O LEU A 136 9337 9366 6517 922 -1274 771 O ATOM 832 CB LEU A 136 7.464 33.867 35.856 1.00 57.94 C ANISOU 832 CB LEU A 136 7969 7989 6055 856 -1057 946 C ATOM 833 CG LEU A 136 7.019 34.964 36.831 1.00 61.61 C ANISOU 833 CG LEU A 136 8293 8351 6766 874 -1101 1012 C ATOM 834 CD1 LEU A 136 8.205 35.744 37.322 1.00 60.90 C ANISOU 834 CD1 LEU A 136 8208 8129 6801 846 -907 1144 C ATOM 835 CD2 LEU A 136 6.010 35.912 36.198 1.00 65.69 C ANISOU 835 CD2 LEU A 136 8837 8901 7222 998 -1289 1111 C ATOM 836 N ALA A 137 7.852 30.868 34.714 1.00 60.93 N ANISOU 836 N ALA A 137 8536 8544 6069 768 -1020 610 N ATOM 837 CA ALA A 137 8.464 29.966 33.733 1.00 62.33 C ANISOU 837 CA ALA A 137 8883 8794 6006 780 -946 546 C ATOM 838 C ALA A 137 7.471 29.015 33.044 1.00 68.39 C ANISOU 838 C ALA A 137 9712 9670 6604 768 -1131 372 C ATOM 839 O ALA A 137 7.719 28.607 31.906 1.00 69.72 O ANISOU 839 O ALA A 137 10052 9928 6510 813 -1124 350 O ATOM 840 CB ALA A 137 9.596 29.179 34.376 1.00 61.57 C ANISOU 840 CB ALA A 137 8772 8619 6003 727 -748 473 C ATOM 841 N ILE A 138 6.332 28.736 33.674 1.00 65.02 N ANISOU 841 N ILE A 138 9146 9245 6314 706 -1295 251 N ATOM 842 CA ILE A 138 5.342 27.830 33.082 1.00 66.65 C ANISOU 842 CA ILE A 138 9383 9554 6386 668 -1478 66 C ATOM 843 C ILE A 138 4.042 28.485 32.581 1.00 72.87 C ANISOU 843 C ILE A 138 10104 10462 7121 726 -1730 81 C ATOM 844 O ILE A 138 3.492 28.078 31.558 1.00 74.86 O ANISOU 844 O ILE A 138 10449 10841 7153 752 -1883 -5 O ATOM 845 CB ILE A 138 4.974 26.692 34.058 1.00 68.43 C ANISOU 845 CB ILE A 138 9511 9708 6782 525 -1478 -134 C ATOM 846 CG1 ILE A 138 6.188 25.799 34.318 1.00 67.76 C ANISOU 846 CG1 ILE A 138 9533 9520 6693 495 -1272 -182 C ATOM 847 CG2 ILE A 138 3.813 25.877 33.511 1.00 70.78 C ANISOU 847 CG2 ILE A 138 9808 10109 6977 459 -1683 -329 C ATOM 848 CD1 ILE A 138 6.149 25.090 35.654 1.00 72.53 C ANISOU 848 CD1 ILE A 138 10038 9994 7527 378 -1212 -285 C ATOM 849 N VAL A 139 3.554 29.485 33.309 1.00 68.63 N ANISOU 849 N VAL A 139 9405 9889 6784 755 -1780 178 N ATOM 850 CA VAL A 139 2.236 30.105 33.050 1.00 70.15 C ANISOU 850 CA VAL A 139 9484 10188 6983 822 -2028 172 C ATOM 851 C VAL A 139 2.508 31.132 31.957 1.00 76.85 C ANISOU 851 C VAL A 139 10497 11083 7620 987 -2070 380 C ATOM 852 O VAL A 139 1.684 31.281 31.051 1.00 78.51 O ANISOU 852 O VAL A 139 10746 11429 7656 1074 -2289 363 O ATOM 853 CB VAL A 139 1.470 30.685 34.277 1.00 72.54 C ANISOU 853 CB VAL A 139 9535 10441 7587 796 -2076 160 C ATOM 854 CG1 VAL A 139 0.143 31.318 33.863 1.00 74.48 C ANISOU 854 CG1 VAL A 139 9662 10816 7820 897 -2340 146 C ATOM 855 CG2 VAL A 139 1.235 29.619 35.343 1.00 70.65 C ANISOU 855 CG2 VAL A 139 9164 10153 7528 619 -2012 -34 C ATOM 856 N HIS A 140 3.654 31.784 32.002 1.00 73.80 N ANISOU 856 N HIS A 140 10216 10591 7235 1023 -1866 567 N ATOM 857 CA HIS A 140 4.043 32.709 30.967 1.00 76.05 C ANISOU 857 CA HIS A 140 10691 10899 7308 1155 -1862 779 C ATOM 858 C HIS A 140 5.106 31.865 30.337 1.00 80.64 C ANISOU 858 C HIS A 140 11450 11501 7687 1108 -1683 744 C ATOM 859 O HIS A 140 6.186 31.746 30.864 1.00 79.02 O ANISOU 859 O HIS A 140 11244 11196 7583 1046 -1451 777 O ATOM 860 CB HIS A 140 4.615 33.935 31.617 1.00 75.89 C ANISOU 860 CB HIS A 140 10636 10727 7473 1187 -1728 983 C ATOM 861 CG HIS A 140 3.602 34.719 32.367 1.00 79.15 C ANISOU 861 CG HIS A 140 10861 11102 8110 1238 -1885 992 C ATOM 862 ND1 HIS A 140 3.856 35.967 32.876 1.00 80.44 N ANISOU 862 ND1 HIS A 140 11000 11127 8436 1293 -1821 1170 N ATOM 863 CD2 HIS A 140 2.322 34.433 32.680 1.00 81.17 C ANISOU 863 CD2 HIS A 140 10939 11445 8457 1242 -2099 835 C ATOM 864 CE1 HIS A 140 2.770 36.419 33.468 1.00 79.93 C ANISOU 864 CE1 HIS A 140 10757 11064 8547 1348 -1992 1119 C ATOM 865 NE2 HIS A 140 1.825 35.507 33.363 1.00 80.73 N ANISOU 865 NE2 HIS A 140 10751 11311 8612 1317 -2158 917 N ATOM 866 N ALA A 141 4.782 31.256 29.218 1.00 79.33 N ANISOU 866 N ALA A 141 11430 11476 7237 1144 -1800 660 N ATOM 867 CA ALA A 141 5.706 30.355 28.612 1.00 79.64 C ANISOU 867 CA ALA A 141 11635 11545 7079 1108 -1637 591 C ATOM 868 C ALA A 141 6.608 31.206 27.778 1.00 85.50 C ANISOU 868 C ALA A 141 12574 12290 7621 1196 -1487 824 C ATOM 869 O ALA A 141 7.802 31.276 28.008 1.00 83.75 O ANISOU 869 O ALA A 141 12384 11990 7449 1160 -1227 900 O ATOM 870 CB ALA A 141 4.973 29.367 27.779 1.00 82.28 C ANISOU 870 CB ALA A 141 12050 12023 7190 1103 -1824 390 C ATOM 871 N THR A 142 6.011 31.879 26.814 1.00 85.48 N ANISOU 871 N THR A 142 12702 12381 7395 1312 -1655 939 N ATOM 872 CA THR A 142 6.727 32.721 25.867 1.00 87.59 C ANISOU 872 CA THR A 142 13201 12660 7421 1399 -1532 1178 C ATOM 873 C THR A 142 7.553 33.868 26.462 1.00 91.72 C ANISOU 873 C THR A 142 13692 13020 8137 1385 -1322 1414 C ATOM 874 O THR A 142 8.774 33.931 26.273 1.00 91.48 O ANISOU 874 O THR A 142 13755 12953 8052 1342 -1047 1504 O ATOM 875 CB THR A 142 5.739 33.293 24.878 1.00 95.41 C ANISOU 875 CB THR A 142 14324 13764 8163 1540 -1802 1264 C ATOM 876 OG1 THR A 142 5.282 32.228 24.049 1.00 95.85 O ANISOU 876 OG1 THR A 142 14473 13987 7957 1548 -1947 1060 O ATOM 877 CG2 THR A 142 6.376 34.350 24.031 1.00 94.95 C ANISOU 877 CG2 THR A 142 14511 13683 7882 1630 -1682 1553 C ATOM 878 N ASN A 143 6.881 34.771 27.174 1.00 88.07 N ANISOU 878 N ASN A 143 13093 12464 7906 1420 -1449 1499 N ATOM 879 CA ASN A 143 7.455 36.042 27.618 1.00 87.55 C ANISOU 879 CA ASN A 143 13027 12235 8003 1425 -1305 1735 C ATOM 880 C ASN A 143 8.138 36.073 28.982 1.00 88.65 C ANISOU 880 C ASN A 143 12960 12227 8498 1304 -1119 1696 C ATOM 881 O ASN A 143 8.160 37.124 29.612 1.00 87.75 O ANISOU 881 O ASN A 143 12780 11972 8589 1312 -1097 1832 O ATOM 882 CB ASN A 143 6.328 37.079 27.641 1.00 89.17 C ANISOU 882 CB ASN A 143 13211 12404 8265 1554 -1558 1846 C ATOM 883 CG ASN A 143 4.942 36.441 27.614 1.00111.00 C ANISOU 883 CG ASN A 143 15852 15308 11016 1610 -1871 1641 C ATOM 884 OD1 ASN A 143 4.741 35.368 28.135 1.00103.23 O ANISOU 884 OD1 ASN A 143 14714 14376 10132 1511 -1885 1408 O ATOM 885 ND2 ASN A 143 3.993 37.110 26.999 1.00105.04 N ANISOU 885 ND2 ASN A 143 15165 14608 10136 1767 -2121 1730 N ATOM 886 N SER A 144 8.587 34.927 29.477 1.00 83.41 N ANISOU 886 N SER A 144 12193 11590 7908 1204 -1016 1499 N ATOM 887 CA SER A 144 8.879 34.775 30.902 1.00 80.20 C ANISOU 887 CA SER A 144 11563 11067 7842 1106 -928 1410 C ATOM 888 C SER A 144 10.210 35.332 31.404 1.00 82.99 C ANISOU 888 C SER A 144 11891 11300 8341 1037 -657 1533 C ATOM 889 O SER A 144 10.252 36.087 32.375 1.00 81.14 O ANISOU 889 O SER A 144 11526 10935 8367 1006 -636 1591 O ATOM 890 CB SER A 144 8.756 33.302 31.307 1.00 82.17 C ANISOU 890 CB SER A 144 11722 11376 8123 1033 -947 1152 C ATOM 891 OG SER A 144 9.742 32.512 30.664 1.00 90.75 O ANISOU 891 OG SER A 144 12935 12521 9026 1012 -772 1104 O ATOM 892 N GLN A 145 11.291 34.936 30.748 1.00 80.41 N ANISOU 892 N GLN A 145 11678 11025 7848 1010 -451 1554 N ATOM 893 CA GLN A 145 12.728 35.101 31.239 1.00 79.11 C ANISOU 893 CA GLN A 145 11448 10786 7825 923 -167 1603 C ATOM 894 C GLN A 145 12.863 36.587 31.462 1.00 82.64 C ANISOU 894 C GLN A 145 11899 11100 8401 914 -125 1825 C ATOM 895 O GLN A 145 13.793 37.044 32.126 1.00 81.50 O ANISOU 895 O GLN A 145 11656 10860 8453 831 54 1877 O ATOM 896 CB GLN A 145 13.652 34.426 30.365 1.00 81.84 C ANISOU 896 CB GLN A 145 11911 11238 7946 920 18 1575 C ATOM 897 CG GLN A 145 15.065 34.969 30.502 1.00 96.77 C ANISOU 897 CG GLN A 145 13765 13077 9926 847 307 1690 C ATOM 898 CD GLN A 145 15.864 34.253 31.573 1.00110.19 C ANISOU 898 CD GLN A 145 15260 14744 11864 785 421 1531 C ATOM 899 OE1 GLN A 145 16.824 34.798 32.117 1.00104.22 O ANISOU 899 OE1 GLN A 145 14390 13919 11287 714 595 1598 O ATOM 900 NE2 GLN A 145 15.469 33.023 31.882 1.00 99.77 N ANISOU 900 NE2 GLN A 145 13897 13468 10544 810 315 1319 N ATOM 901 N ARG A 146 11.932 37.351 30.894 1.00 79.94 N ANISOU 901 N ARG A 146 11676 10749 7948 1003 -299 1952 N ATOM 902 CA ARG A 146 12.053 38.792 30.995 1.00 80.26 C ANISOU 902 CA ARG A 146 11765 10639 8090 1006 -259 2177 C ATOM 903 C ARG A 146 12.123 39.354 32.419 1.00 80.53 C ANISOU 903 C ARG A 146 11591 10513 8495 941 -248 2151 C ATOM 904 O ARG A 146 12.980 40.197 32.651 1.00 80.59 O ANISOU 904 O ARG A 146 11602 10398 8620 867 -72 2285 O ATOM 905 CB ARG A 146 10.752 39.478 30.336 1.00 82.40 C ANISOU 905 CB ARG A 146 12175 10915 8220 1154 -524 2288 C ATOM 906 CG ARG A 146 10.822 39.545 28.807 1.00 95.14 C ANISOU 906 CG ARG A 146 14069 12634 9446 1228 -512 2428 C ATOM 907 CD ARG A 146 11.934 40.459 28.329 1.00104.72 C ANISOU 907 CD ARG A 146 15444 13749 10595 1164 -249 2669 C ATOM 908 NE ARG A 146 11.724 40.876 26.954 1.00115.33 N ANISOU 908 NE ARG A 146 17088 15152 11580 1261 -286 2857 N ATOM 909 CZ ARG A 146 12.176 40.215 25.898 1.00130.73 C ANISOU 909 CZ ARG A 146 19203 17264 13206 1262 -178 2847 C ATOM 910 NH1 ARG A 146 12.875 39.106 26.060 1.00115.20 N ANISOU 910 NH1 ARG A 146 17122 15404 11244 1179 -26 2654 N ATOM 911 NH2 ARG A 146 11.934 40.671 24.679 1.00121.78 N ANISOU 911 NH2 ARG A 146 18361 16179 11732 1358 -224 3031 N ATOM 912 N PRO A 147 11.318 38.861 33.353 1.00 73.60 N ANISOU 912 N PRO A 147 10537 9640 7790 953 -411 1974 N ATOM 913 CA PRO A 147 11.310 39.455 34.697 1.00 71.14 C ANISOU 913 CA PRO A 147 10045 9180 7805 904 -410 1950 C ATOM 914 C PRO A 147 11.793 38.429 35.699 1.00 71.53 C ANISOU 914 C PRO A 147 9914 9258 8007 813 -334 1749 C ATOM 915 O PRO A 147 12.048 38.716 36.868 1.00 69.70 O ANISOU 915 O PRO A 147 9532 8923 8027 753 -295 1704 O ATOM 916 CB PRO A 147 9.832 39.766 34.929 1.00 72.96 C ANISOU 916 CB PRO A 147 10228 9404 8089 1011 -674 1914 C ATOM 917 CG PRO A 147 9.107 38.771 34.093 1.00 78.25 C ANISOU 917 CG PRO A 147 10958 10253 8519 1072 -819 1809 C ATOM 918 CD PRO A 147 9.958 38.561 32.873 1.00 75.72 C ANISOU 918 CD PRO A 147 10842 10006 7921 1066 -675 1912 C ATOM 919 N ARG A 148 11.910 37.213 35.193 1.00 66.85 N ANISOU 919 N ARG A 148 9358 8802 7241 812 -322 1628 N ATOM 920 CA ARG A 148 12.384 36.053 35.949 1.00 64.27 C ANISOU 920 CA ARG A 148 8906 8507 7005 747 -255 1438 C ATOM 921 C ARG A 148 13.811 36.359 36.410 1.00 66.66 C ANISOU 921 C ARG A 148 9143 8743 7440 668 -26 1488 C ATOM 922 O ARG A 148 14.233 35.871 37.460 1.00 64.90 O ANISOU 922 O ARG A 148 8776 8487 7394 618 15 1367 O ATOM 923 CB ARG A 148 12.392 34.810 35.056 1.00 64.90 C ANISOU 923 CB ARG A 148 9091 8730 6840 773 -259 1327 C ATOM 924 CG ARG A 148 11.194 33.904 35.254 1.00 73.73 C ANISOU 924 CG ARG A 148 10170 9906 7937 790 -464 1153 C ATOM 925 CD ARG A 148 11.283 32.677 34.368 1.00 83.89 C ANISOU 925 CD ARG A 148 11575 11313 8985 805 -459 1031 C ATOM 926 NE ARG A 148 12.365 31.777 34.774 1.00 92.27 N ANISOU 926 NE ARG A 148 12602 12360 10095 761 -287 927 N ATOM 927 CZ ARG A 148 12.874 30.819 34.006 1.00110.64 C ANISOU 927 CZ ARG A 148 15042 14769 12228 783 -208 839 C ATOM 928 NH1 ARG A 148 12.414 30.629 32.776 1.00101.41 N ANISOU 928 NH1 ARG A 148 14036 13708 10787 835 -282 840 N ATOM 929 NH2 ARG A 148 13.852 30.047 34.459 1.00 98.61 N ANISOU 929 NH2 ARG A 148 13472 13221 10774 765 -62 743 N ATOM 930 N LYS A 149 14.543 37.172 35.613 1.00 63.56 N ANISOU 930 N LYS A 149 8860 8335 6957 655 121 1665 N ATOM 931 CA LYS A 149 15.888 37.641 35.916 1.00 62.92 C ANISOU 931 CA LYS A 149 8709 8198 7001 564 346 1729 C ATOM 932 C LYS A 149 15.769 38.833 36.872 1.00 65.86 C ANISOU 932 C LYS A 149 8988 8402 7633 517 314 1805 C ATOM 933 O LYS A 149 16.552 38.920 37.822 1.00 64.77 O ANISOU 933 O LYS A 149 8696 8207 7705 438 407 1748 O ATOM 934 CB LYS A 149 16.653 38.002 34.630 1.00 67.64 C ANISOU 934 CB LYS A 149 9467 8851 7381 551 531 1886 C ATOM 935 CG LYS A 149 18.109 38.399 34.862 1.00 83.23 C ANISOU 935 CG LYS A 149 11345 10795 9483 438 788 1934 C ATOM 936 CD LYS A 149 19.003 38.131 33.659 1.00 96.88 C ANISOU 936 CD LYS A 149 13186 12648 10975 425 1007 1996 C ATOM 937 CE LYS A 149 20.004 37.039 33.960 1.00108.07 C ANISOU 937 CE LYS A 149 14453 14174 12434 412 1144 1817 C ATOM 938 NZ LYS A 149 21.268 37.215 33.197 1.00118.92 N ANISOU 938 NZ LYS A 149 15838 15630 13716 347 1432 1892 N ATOM 939 N LEU A 150 14.757 39.716 36.650 1.00 62.40 N ANISOU 939 N LEU A 150 8641 7886 7181 578 167 1918 N ATOM 940 CA LEU A 150 14.465 40.889 37.489 1.00 61.40 C ANISOU 940 CA LEU A 150 8455 7585 7289 560 113 1983 C ATOM 941 C LEU A 150 14.238 40.451 38.938 1.00 62.48 C ANISOU 941 C LEU A 150 8387 7696 7656 534 37 1796 C ATOM 942 O LEU A 150 14.765 41.087 39.851 1.00 62.01 O ANISOU 942 O LEU A 150 8225 7520 7815 460 101 1794 O ATOM 943 CB LEU A 150 13.216 41.639 36.977 1.00 62.54 C ANISOU 943 CB LEU A 150 8727 7678 7355 678 -77 2095 C ATOM 944 CG LEU A 150 13.234 43.172 36.933 1.00 68.43 C ANISOU 944 CG LEU A 150 9568 8230 8201 679 -57 2291 C ATOM 945 CD1 LEU A 150 12.071 43.688 36.118 1.00 70.42 C ANISOU 945 CD1 LEU A 150 9984 8472 8299 833 -247 2408 C ATOM 946 CD2 LEU A 150 13.179 43.792 38.323 1.00 68.68 C ANISOU 946 CD2 LEU A 150 9440 8109 8547 635 -84 2219 C ATOM 947 N LEU A 151 13.486 39.350 39.145 1.00 56.81 N ANISOU 947 N LEU A 151 7621 7086 6881 583 -92 1636 N ATOM 948 CA LEU A 151 13.223 38.815 40.477 1.00 54.16 C ANISOU 948 CA LEU A 151 7117 6734 6726 555 -155 1463 C ATOM 949 C LEU A 151 14.472 38.172 41.081 1.00 56.02 C ANISOU 949 C LEU A 151 7257 6989 7041 475 -4 1375 C ATOM 950 O LEU A 151 14.824 38.494 42.214 1.00 54.75 O ANISOU 950 O LEU A 151 6973 6746 7083 423 17 1325 O ATOM 951 CB LEU A 151 12.076 37.786 40.457 1.00 53.70 C ANISOU 951 CB LEU A 151 7048 6780 6575 609 -317 1324 C ATOM 952 CG LEU A 151 10.631 38.281 40.307 1.00 59.40 C ANISOU 952 CG LEU A 151 7779 7500 7289 693 -513 1340 C ATOM 953 CD1 LEU A 151 9.675 37.112 40.343 1.00 58.88 C ANISOU 953 CD1 LEU A 151 7672 7552 7148 705 -643 1175 C ATOM 954 CD2 LEU A 151 10.232 39.244 41.429 1.00 62.02 C ANISOU 954 CD2 LEU A 151 7999 7703 7862 694 -559 1338 C ATOM 955 N ALA A 152 15.135 37.272 40.319 1.00 52.26 N ANISOU 955 N ALA A 152 6836 6622 6397 478 94 1349 N ATOM 956 CA ALA A 152 16.310 36.503 40.731 1.00 51.03 C ANISOU 956 CA ALA A 152 6592 6508 6288 437 226 1254 C ATOM 957 C ALA A 152 17.569 37.294 41.048 1.00 54.43 C ANISOU 957 C ALA A 152 6933 6883 6866 357 390 1322 C ATOM 958 O ALA A 152 18.306 36.890 41.948 1.00 52.91 O ANISOU 958 O ALA A 152 6606 6690 6808 327 433 1217 O ATOM 959 CB ALA A 152 16.620 35.422 39.711 1.00 52.58 C ANISOU 959 CB ALA A 152 6885 6835 6259 481 288 1209 C ATOM 960 N GLU A 153 17.791 38.402 40.379 1.00 52.30 N ANISOU 960 N GLU A 153 6735 6558 6577 321 470 1490 N ATOM 961 CA GLU A 153 19.008 39.125 40.632 1.00 52.91 C ANISOU 961 CA GLU A 153 6720 6584 6799 219 638 1545 C ATOM 962 C GLU A 153 18.841 40.479 41.262 1.00 56.91 C ANISOU 962 C GLU A 153 7199 6921 7503 154 609 1629 C ATOM 963 O GLU A 153 19.661 40.880 42.057 1.00 57.13 O ANISOU 963 O GLU A 153 7090 6893 7723 65 679 1591 O ATOM 964 CB GLU A 153 19.980 38.896 39.505 1.00 56.18 C ANISOU 964 CB GLU A 153 7188 7104 7054 195 838 1612 C ATOM 965 CG GLU A 153 19.525 39.368 38.196 1.00 67.65 C ANISOU 965 CG GLU A 153 8850 8566 8289 222 862 1780 C ATOM 966 CD GLU A 153 20.592 39.197 37.188 1.00 90.10 C ANISOU 966 CD GLU A 153 11735 11516 10984 182 1092 1840 C ATOM 967 OE1 GLU A 153 20.951 40.187 36.536 1.00 87.50 O ANISOU 967 OE1 GLU A 153 11499 11130 10618 108 1225 2019 O ATOM 968 OE2 GLU A 153 21.088 38.072 37.072 1.00 83.54 O ANISOU 968 OE2 GLU A 153 10846 10818 10077 224 1149 1706 O ATOM 969 N LYS A 154 17.749 41.165 40.936 1.00 52.84 N ANISOU 969 N LYS A 154 6811 6323 6943 209 489 1730 N ATOM 970 CA LYS A 154 17.462 42.457 41.546 1.00 52.51 C ANISOU 970 CA LYS A 154 6764 6099 7090 172 443 1800 C ATOM 971 C LYS A 154 16.528 42.586 42.769 1.00 53.97 C ANISOU 971 C LYS A 154 6860 6208 7437 218 266 1682 C ATOM 972 O LYS A 154 16.842 43.284 43.734 1.00 53.16 O ANISOU 972 O LYS A 154 6667 5987 7546 152 275 1647 O ATOM 973 CB LYS A 154 16.877 43.215 40.359 1.00 57.05 C ANISOU 973 CB LYS A 154 7549 6618 7507 225 426 1998 C ATOM 974 CG LYS A 154 17.859 44.176 39.708 1.00 74.07 C ANISOU 974 CG LYS A 154 9791 8684 9668 113 624 2178 C ATOM 975 CD LYS A 154 17.201 44.960 38.584 1.00 88.45 C ANISOU 975 CD LYS A 154 11856 10430 11320 183 589 2391 C ATOM 976 CE LYS A 154 17.704 44.504 37.224 1.00102.62 C ANISOU 976 CE LYS A 154 13791 12363 12837 178 732 2495 C ATOM 977 NZ LYS A 154 19.023 43.820 37.320 1.00111.14 N ANISOU 977 NZ LYS A 154 14724 13562 13942 63 940 2403 N ATOM 978 N VAL A 155 15.381 41.916 42.714 1.00 49.43 N ANISOU 978 N VAL A 155 6311 5709 6761 324 111 1614 N ATOM 979 CA VAL A 155 14.380 42.021 43.775 1.00 47.97 C ANISOU 979 CA VAL A 155 6046 5473 6708 371 -43 1504 C ATOM 980 C VAL A 155 14.664 41.033 44.907 1.00 50.13 C ANISOU 980 C VAL A 155 6174 5812 7060 334 -48 1317 C ATOM 981 O VAL A 155 14.256 41.249 46.048 1.00 49.05 O ANISOU 981 O VAL A 155 5949 5616 7071 331 -118 1222 O ATOM 982 CB VAL A 155 12.949 41.945 43.208 1.00 52.15 C ANISOU 982 CB VAL A 155 6653 6043 7117 493 -209 1524 C ATOM 983 CG1 VAL A 155 11.929 42.202 44.306 1.00 50.94 C ANISOU 983 CG1 VAL A 155 6399 5838 7118 537 -343 1414 C ATOM 984 CG2 VAL A 155 12.777 42.937 42.068 1.00 54.23 C ANISOU 984 CG2 VAL A 155 7085 6235 7285 545 -209 1726 C ATOM 985 N VAL A 156 15.361 39.951 44.580 1.00 45.82 N ANISOU 985 N VAL A 156 5619 5387 6406 316 28 1267 N ATOM 986 CA VAL A 156 15.697 38.907 45.558 1.00 43.70 C ANISOU 986 CA VAL A 156 5244 5176 6185 298 22 1103 C ATOM 987 C VAL A 156 16.342 39.525 46.831 1.00 47.13 C ANISOU 987 C VAL A 156 5554 5518 6835 231 46 1048 C ATOM 988 O VAL A 156 16.377 38.867 47.873 1.00 45.63 O ANISOU 988 O VAL A 156 5287 5350 6700 230 3 916 O ATOM 989 CB VAL A 156 16.556 37.774 44.922 1.00 47.45 C ANISOU 989 CB VAL A 156 5736 5773 6521 304 118 1070 C ATOM 990 CG1 VAL A 156 18.039 38.132 44.887 1.00 48.01 C ANISOU 990 CG1 VAL A 156 5734 5841 6668 237 278 1106 C ATOM 991 CG2 VAL A 156 16.332 36.441 45.626 1.00 45.82 C ANISOU 991 CG2 VAL A 156 5496 5626 6288 333 54 912 C ATOM 992 N TYR A 157 16.853 40.776 46.736 1.00 44.31 N ANISOU 992 N TYR A 157 5193 5052 6591 172 114 1148 N ATOM 993 CA TYR A 157 17.491 41.480 47.852 1.00 43.46 C ANISOU 993 CA TYR A 157 4974 4849 6689 95 133 1092 C ATOM 994 C TYR A 157 16.500 42.378 48.567 1.00 47.49 C ANISOU 994 C TYR A 157 5496 5231 7315 119 25 1076 C ATOM 995 O TYR A 157 16.465 42.400 49.799 1.00 46.09 O ANISOU 995 O TYR A 157 5233 5024 7255 103 -28 953 O ATOM 996 CB TYR A 157 18.692 42.299 47.366 1.00 45.67 C ANISOU 996 CB TYR A 157 5235 5077 7042 -9 282 1191 C ATOM 997 CG TYR A 157 19.804 41.455 46.794 1.00 46.98 C ANISOU 997 CG TYR A 157 5349 5380 7119 -33 408 1181 C ATOM 998 CD1 TYR A 157 19.919 41.260 45.420 1.00 49.79 C ANISOU 998 CD1 TYR A 157 5812 5805 7302 -16 504 1299 C ATOM 999 CD2 TYR A 157 20.755 40.865 47.619 1.00 47.06 C ANISOU 999 CD2 TYR A 157 5207 5460 7215 -61 430 1048 C ATOM 1000 CE1 TYR A 157 20.946 40.487 44.884 1.00 50.80 C ANISOU 1000 CE1 TYR A 157 5888 6067 7348 -28 635 1276 C ATOM 1001 CE2 TYR A 157 21.791 40.096 47.095 1.00 48.50 C ANISOU 1001 CE2 TYR A 157 5325 5774 7328 -62 547 1027 C ATOM 1002 CZ TYR A 157 21.882 39.910 45.725 1.00 56.34 C ANISOU 1002 CZ TYR A 157 6419 6833 8155 -46 657 1137 C ATOM 1003 OH TYR A 157 22.901 39.153 45.202 1.00 58.32 O ANISOU 1003 OH TYR A 157 6602 7220 8336 -37 785 1102 O ATOM 1004 N VAL A 158 15.694 43.114 47.781 1.00 45.50 N ANISOU 1004 N VAL A 158 5357 4909 7022 170 -11 1199 N ATOM 1005 CA VAL A 158 14.649 44.034 48.236 1.00 45.70 C ANISOU 1005 CA VAL A 158 5407 4810 7146 227 -116 1199 C ATOM 1006 C VAL A 158 13.492 43.243 48.874 1.00 48.68 C ANISOU 1006 C VAL A 158 5733 5277 7485 308 -240 1065 C ATOM 1007 O VAL A 158 12.891 43.710 49.841 1.00 48.35 O ANISOU 1007 O VAL A 158 5640 5167 7564 331 -305 979 O ATOM 1008 CB VAL A 158 14.197 44.944 47.058 1.00 51.43 C ANISOU 1008 CB VAL A 158 6282 5445 7812 282 -123 1385 C ATOM 1009 CG1 VAL A 158 12.861 45.637 47.332 1.00 51.64 C ANISOU 1009 CG1 VAL A 158 6338 5385 7900 398 -264 1377 C ATOM 1010 CG2 VAL A 158 15.276 45.968 46.720 1.00 52.96 C ANISOU 1010 CG2 VAL A 158 6528 5500 8095 173 10 1511 C ATOM 1011 N GLY A 159 13.228 42.051 48.346 1.00 44.48 N ANISOU 1011 N GLY A 159 5218 4895 6790 339 -258 1040 N ATOM 1012 CA GLY A 159 12.155 41.181 48.808 1.00 43.16 C ANISOU 1012 CA GLY A 159 5008 4820 6571 388 -357 919 C ATOM 1013 C GLY A 159 12.533 40.161 49.859 1.00 45.70 C ANISOU 1013 C GLY A 159 5255 5204 6907 337 -338 775 C ATOM 1014 O GLY A 159 11.665 39.736 50.624 1.00 44.89 O ANISOU 1014 O GLY A 159 5107 5133 6816 352 -403 667 O ATOM 1015 N VAL A 160 13.811 39.732 49.896 1.00 42.01 N ANISOU 1015 N VAL A 160 4772 4758 6430 282 -247 772 N ATOM 1016 CA VAL A 160 14.275 38.722 50.858 1.00 40.64 C ANISOU 1016 CA VAL A 160 4546 4639 6257 255 -240 647 C ATOM 1017 C VAL A 160 15.394 39.042 51.869 1.00 44.52 C ANISOU 1017 C VAL A 160 4956 5084 6875 202 -199 591 C ATOM 1018 O VAL A 160 15.262 38.667 53.032 1.00 43.65 O ANISOU 1018 O VAL A 160 4809 4976 6798 197 -243 481 O ATOM 1019 CB VAL A 160 14.663 37.373 50.185 1.00 44.20 C ANISOU 1019 CB VAL A 160 5046 5199 6551 271 -206 634 C ATOM 1020 CG1 VAL A 160 15.394 36.441 51.149 1.00 43.11 C ANISOU 1020 CG1 VAL A 160 4868 5088 6423 259 -193 527 C ATOM 1021 CG2 VAL A 160 13.437 36.682 49.596 1.00 43.94 C ANISOU 1021 CG2 VAL A 160 5079 5227 6388 309 -277 620 C ATOM 1022 N TRP A 161 16.473 39.725 51.438 1.00 41.86 N ANISOU 1022 N TRP A 161 4590 4710 6604 155 -117 664 N ATOM 1023 CA TRP A 161 17.629 40.031 52.286 1.00 41.84 C ANISOU 1023 CA TRP A 161 4487 4682 6729 94 -84 602 C ATOM 1024 C TRP A 161 17.382 41.286 53.116 1.00 45.57 C ANISOU 1024 C TRP A 161 4928 5024 7362 54 -123 575 C ATOM 1025 O TRP A 161 17.547 41.227 54.337 1.00 44.52 O ANISOU 1025 O TRP A 161 4738 4884 7296 41 -173 456 O ATOM 1026 CB TRP A 161 18.968 40.081 51.538 1.00 41.82 C ANISOU 1026 CB TRP A 161 4435 4719 6736 45 32 663 C ATOM 1027 CG TRP A 161 19.408 38.739 51.027 1.00 42.49 C ANISOU 1027 CG TRP A 161 4529 4935 6679 99 68 640 C ATOM 1028 CD1 TRP A 161 19.409 38.318 49.730 1.00 45.98 C ANISOU 1028 CD1 TRP A 161 5046 5442 6984 128 138 724 C ATOM 1029 CD2 TRP A 161 19.845 37.622 51.815 1.00 41.47 C ANISOU 1029 CD2 TRP A 161 4355 4879 6523 145 27 520 C ATOM 1030 NE1 TRP A 161 19.841 37.013 49.657 1.00 44.94 N ANISOU 1030 NE1 TRP A 161 4911 5414 6751 188 150 653 N ATOM 1031 CE2 TRP A 161 20.119 36.562 50.920 1.00 45.41 C ANISOU 1031 CE2 TRP A 161 4901 5473 6880 204 81 534 C ATOM 1032 CE3 TRP A 161 20.050 37.417 53.189 1.00 42.06 C ANISOU 1032 CE3 TRP A 161 4370 4943 6667 151 -52 403 C ATOM 1033 CZ2 TRP A 161 20.590 35.320 51.355 1.00 44.24 C ANISOU 1033 CZ2 TRP A 161 4743 5392 6674 273 56 438 C ATOM 1034 CZ3 TRP A 161 20.517 36.187 53.617 1.00 43.08 C ANISOU 1034 CZ3 TRP A 161 4495 5147 6727 220 -81 321 C ATOM 1035 CH2 TRP A 161 20.785 35.156 52.706 1.00 43.95 C ANISOU 1035 CH2 TRP A 161 4653 5333 6711 283 -28 340 C ATOM 1036 N ILE A 162 16.987 42.408 52.472 1.00 42.91 N ANISOU 1036 N ILE A 162 4646 4579 7079 42 -104 682 N ATOM 1037 CA ILE A 162 16.711 43.686 53.150 1.00 43.29 C ANISOU 1037 CA ILE A 162 4688 4473 7287 14 -138 661 C ATOM 1038 C ILE A 162 15.584 43.587 54.216 1.00 46.71 C ANISOU 1038 C ILE A 162 5116 4899 7732 78 -239 540 C ATOM 1039 O ILE A 162 15.840 44.001 55.349 1.00 46.54 O ANISOU 1039 O ILE A 162 5043 4824 7817 43 -266 429 O ATOM 1040 CB ILE A 162 16.621 44.911 52.181 1.00 47.85 C ANISOU 1040 CB ILE A 162 5351 4911 7920 -6 -91 817 C ATOM 1041 CG1 ILE A 162 17.965 45.127 51.442 1.00 49.46 C ANISOU 1041 CG1 ILE A 162 5534 5113 8144 -114 41 909 C ATOM 1042 CG2 ILE A 162 16.205 46.203 52.908 1.00 49.15 C ANISOU 1042 CG2 ILE A 162 5531 4892 8253 -14 -137 782 C ATOM 1043 CD1 ILE A 162 17.845 45.607 49.984 1.00 57.81 C ANISOU 1043 CD1 ILE A 162 6721 6125 9121 -109 114 1106 C ATOM 1044 N PRO A 163 14.387 42.993 53.940 1.00 42.59 N ANISOU 1044 N PRO A 163 4636 4445 7100 163 -293 541 N ATOM 1045 CA PRO A 163 13.367 42.897 55.002 1.00 41.69 C ANISOU 1045 CA PRO A 163 4497 4338 7004 206 -362 416 C ATOM 1046 C PRO A 163 13.729 41.935 56.138 1.00 44.21 C ANISOU 1046 C PRO A 163 4774 4743 7282 177 -371 285 C ATOM 1047 O PRO A 163 13.382 42.225 57.286 1.00 43.92 O ANISOU 1047 O PRO A 163 4711 4675 7300 178 -402 174 O ATOM 1048 CB PRO A 163 12.105 42.471 54.250 1.00 43.34 C ANISOU 1048 CB PRO A 163 4741 4615 7110 285 -407 457 C ATOM 1049 CG PRO A 163 12.597 41.778 53.054 1.00 47.82 C ANISOU 1049 CG PRO A 163 5356 5259 7553 277 -369 560 C ATOM 1050 CD PRO A 163 13.884 42.429 52.669 1.00 44.19 C ANISOU 1050 CD PRO A 163 4905 4727 7160 215 -291 644 C ATOM 1051 N ALA A 164 14.440 40.817 55.832 1.00 39.55 N ANISOU 1051 N ALA A 164 4188 4251 6588 160 -342 298 N ATOM 1052 CA ALA A 164 14.872 39.825 56.832 1.00 38.19 C ANISOU 1052 CA ALA A 164 4002 4150 6360 150 -359 193 C ATOM 1053 C ALA A 164 15.882 40.417 57.815 1.00 41.97 C ANISOU 1053 C ALA A 164 4418 4580 6948 106 -369 119 C ATOM 1054 O ALA A 164 15.788 40.154 59.013 1.00 41.23 O ANISOU 1054 O ALA A 164 4324 4502 6839 109 -412 10 O ATOM 1055 CB ALA A 164 15.451 38.591 56.158 1.00 38.41 C ANISOU 1055 CB ALA A 164 4058 4271 6266 164 -330 230 C ATOM 1056 N LEU A 165 16.830 41.234 57.313 1.00 39.17 N ANISOU 1056 N LEU A 165 4015 4170 6699 56 -328 175 N ATOM 1057 CA LEU A 165 17.833 41.901 58.146 1.00 39.58 C ANISOU 1057 CA LEU A 165 3989 4176 6875 -6 -343 96 C ATOM 1058 C LEU A 165 17.182 42.985 59.004 1.00 44.19 C ANISOU 1058 C LEU A 165 4584 4643 7561 -18 -386 20 C ATOM 1059 O LEU A 165 17.651 43.230 60.113 1.00 44.70 O ANISOU 1059 O LEU A 165 4609 4696 7680 -48 -433 -100 O ATOM 1060 CB LEU A 165 18.986 42.472 57.300 1.00 40.51 C ANISOU 1060 CB LEU A 165 4041 4266 7085 -81 -268 176 C ATOM 1061 CG LEU A 165 20.036 41.458 56.839 1.00 44.62 C ANISOU 1061 CG LEU A 165 4503 4915 7536 -73 -227 191 C ATOM 1062 CD1 LEU A 165 20.644 41.862 55.514 1.00 45.72 C ANISOU 1062 CD1 LEU A 165 4622 5046 7705 -128 -113 320 C ATOM 1063 CD2 LEU A 165 21.122 41.261 57.887 1.00 47.18 C ANISOU 1063 CD2 LEU A 165 4716 5292 7920 -95 -280 63 C ATOM 1064 N LEU A 166 16.083 43.601 58.515 1.00 40.42 N ANISOU 1064 N LEU A 166 4164 4090 7105 19 -379 79 N ATOM 1065 CA LEU A 166 15.325 44.609 59.258 1.00 40.81 C ANISOU 1065 CA LEU A 166 4229 4026 7249 37 -415 2 C ATOM 1066 C LEU A 166 14.513 43.941 60.382 1.00 44.03 C ANISOU 1066 C LEU A 166 4648 4516 7567 86 -457 -126 C ATOM 1067 O LEU A 166 14.330 44.540 61.445 1.00 44.24 O ANISOU 1067 O LEU A 166 4670 4487 7653 84 -486 -247 O ATOM 1068 CB LEU A 166 14.403 45.408 58.312 1.00 41.51 C ANISOU 1068 CB LEU A 166 4373 4017 7382 90 -403 111 C ATOM 1069 CG LEU A 166 14.699 46.919 58.180 1.00 47.87 C ANISOU 1069 CG LEU A 166 5203 4624 8362 51 -390 142 C ATOM 1070 CD1 LEU A 166 15.888 47.182 57.256 1.00 48.77 C ANISOU 1070 CD1 LEU A 166 5313 4697 8518 -46 -320 266 C ATOM 1071 CD2 LEU A 166 13.495 47.666 57.648 1.00 51.07 C ANISOU 1071 CD2 LEU A 166 5675 4930 8801 152 -413 207 C ATOM 1072 N LEU A 167 14.061 42.685 60.155 1.00 39.10 N ANISOU 1072 N LEU A 167 4046 4018 6793 121 -452 -102 N ATOM 1073 CA LEU A 167 13.293 41.878 61.112 1.00 37.77 C ANISOU 1073 CA LEU A 167 3902 3932 6517 146 -468 -201 C ATOM 1074 C LEU A 167 14.103 41.446 62.348 1.00 40.49 C ANISOU 1074 C LEU A 167 4253 4316 6817 119 -499 -308 C ATOM 1075 O LEU A 167 13.501 41.020 63.336 1.00 39.60 O ANISOU 1075 O LEU A 167 4178 4247 6620 131 -505 -398 O ATOM 1076 CB LEU A 167 12.689 40.642 60.414 1.00 36.94 C ANISOU 1076 CB LEU A 167 3832 3931 6274 168 -450 -139 C ATOM 1077 CG LEU A 167 11.367 40.847 59.680 1.00 41.72 C ANISOU 1077 CG LEU A 167 4430 4542 6880 211 -446 -97 C ATOM 1078 CD1 LEU A 167 11.257 39.913 58.497 1.00 41.24 C ANISOU 1078 CD1 LEU A 167 4398 4555 6716 216 -437 0 C ATOM 1079 CD2 LEU A 167 10.181 40.640 60.605 1.00 44.71 C ANISOU 1079 CD2 LEU A 167 4798 4966 7225 224 -441 -207 C ATOM 1080 N THR A 168 15.458 41.534 62.283 1.00 36.85 N ANISOU 1080 N THR A 168 3751 3847 6404 82 -517 -298 N ATOM 1081 CA THR A 168 16.390 41.161 63.365 1.00 36.46 C ANISOU 1081 CA THR A 168 3692 3844 6317 70 -573 -397 C ATOM 1082 C THR A 168 16.480 42.206 64.485 1.00 40.90 C ANISOU 1082 C THR A 168 4238 4336 6965 43 -619 -530 C ATOM 1083 O THR A 168 16.990 41.880 65.556 1.00 40.66 O ANISOU 1083 O THR A 168 4222 4356 6872 47 -681 -631 O ATOM 1084 CB THR A 168 17.796 40.831 62.832 1.00 43.02 C ANISOU 1084 CB THR A 168 4453 4716 7176 50 -581 -352 C ATOM 1085 OG1 THR A 168 18.446 42.028 62.398 1.00 42.90 O ANISOU 1085 OG1 THR A 168 4355 4614 7332 -19 -563 -336 O ATOM 1086 CG2 THR A 168 17.789 39.797 61.728 1.00 41.34 C ANISOU 1086 CG2 THR A 168 4265 4570 6871 85 -533 -238 C ATOM 1087 N ILE A 169 15.989 43.452 64.237 1.00 37.77 N ANISOU 1087 N ILE A 169 3826 3818 6705 26 -595 -532 N ATOM 1088 CA ILE A 169 15.958 44.579 65.190 1.00 38.56 C ANISOU 1088 CA ILE A 169 3924 3821 6904 3 -630 -666 C ATOM 1089 C ILE A 169 15.587 44.177 66.656 1.00 42.47 C ANISOU 1089 C ILE A 169 4476 4387 7273 34 -670 -815 C ATOM 1090 O ILE A 169 16.351 44.553 67.553 1.00 43.34 O ANISOU 1090 O ILE A 169 4575 4487 7407 1 -737 -934 O ATOM 1091 CB ILE A 169 15.206 45.827 64.616 1.00 42.29 C ANISOU 1091 CB ILE A 169 4405 4141 7523 14 -592 -632 C ATOM 1092 CG1 ILE A 169 16.094 46.573 63.589 1.00 43.46 C ANISOU 1092 CG1 ILE A 169 4512 4182 7819 -58 -569 -527 C ATOM 1093 CG2 ILE A 169 14.713 46.783 65.711 1.00 43.80 C ANISOU 1093 CG2 ILE A 169 4624 4241 7776 30 -617 -793 C ATOM 1094 CD1 ILE A 169 15.364 47.586 62.666 1.00 50.40 C ANISOU 1094 CD1 ILE A 169 5431 4908 8810 -30 -528 -427 C ATOM 1095 N PRO A 170 14.527 43.351 66.925 1.00 37.60 N ANISOU 1095 N PRO A 170 3923 3853 6511 86 -631 -813 N ATOM 1096 CA PRO A 170 14.249 42.939 68.315 1.00 37.48 C ANISOU 1096 CA PRO A 170 3980 3907 6354 103 -651 -940 C ATOM 1097 C PRO A 170 15.357 42.108 68.967 1.00 41.39 C ANISOU 1097 C PRO A 170 4507 4485 6733 97 -730 -967 C ATOM 1098 O PRO A 170 15.508 42.196 70.185 1.00 42.16 O ANISOU 1098 O PRO A 170 4659 4610 6749 103 -780 -1093 O ATOM 1099 CB PRO A 170 12.957 42.132 68.201 1.00 38.38 C ANISOU 1099 CB PRO A 170 4141 4092 6349 133 -571 -899 C ATOM 1100 CG PRO A 170 12.380 42.503 66.909 1.00 42.52 C ANISOU 1100 CG PRO A 170 4604 4567 6986 147 -529 -793 C ATOM 1101 CD PRO A 170 13.516 42.785 66.011 1.00 38.14 C ANISOU 1101 CD PRO A 170 4001 3958 6534 119 -566 -702 C ATOM 1102 N ASP A 171 16.136 41.314 68.180 1.00 36.47 N ANISOU 1102 N ASP A 171 3854 3908 6094 98 -746 -857 N ATOM 1103 CA ASP A 171 17.249 40.520 68.735 1.00 35.92 C ANISOU 1103 CA ASP A 171 3802 3919 5929 120 -836 -882 C ATOM 1104 C ASP A 171 18.323 41.448 69.307 1.00 38.55 C ANISOU 1104 C ASP A 171 4051 4224 6373 84 -932 -998 C ATOM 1105 O ASP A 171 18.910 41.120 70.332 1.00 39.13 O ANISOU 1105 O ASP A 171 4160 4361 6345 112 -1030 -1090 O ATOM 1106 CB ASP A 171 17.879 39.559 67.706 1.00 37.06 C ANISOU 1106 CB ASP A 171 3914 4111 6055 143 -827 -754 C ATOM 1107 CG ASP A 171 16.923 38.603 67.023 1.00 46.62 C ANISOU 1107 CG ASP A 171 5203 5343 7166 165 -743 -647 C ATOM 1108 OD1 ASP A 171 16.672 38.784 65.817 1.00 47.19 O ANISOU 1108 OD1 ASP A 171 5223 5386 7320 148 -681 -553 O ATOM 1109 OD2 ASP A 171 16.471 37.643 67.680 1.00 52.21 O ANISOU 1109 OD2 ASP A 171 6034 6095 7707 194 -741 -655 O ATOM 1110 N PHE A 172 18.567 42.607 68.662 1.00 33.25 N ANISOU 1110 N PHE A 172 3277 3452 5903 19 -909 -995 N ATOM 1111 CA PHE A 172 19.550 43.579 69.143 1.00 33.66 C ANISOU 1111 CA PHE A 172 3241 3459 6088 -46 -990 -1115 C ATOM 1112 C PHE A 172 19.090 44.214 70.454 1.00 37.84 C ANISOU 1112 C PHE A 172 3846 3956 6574 -43 -1039 -1284 C ATOM 1113 O PHE A 172 19.904 44.397 71.358 1.00 38.86 O ANISOU 1113 O PHE A 172 3953 4122 6688 -59 -1153 -1418 O ATOM 1114 CB PHE A 172 19.843 44.664 68.089 1.00 35.48 C ANISOU 1114 CB PHE A 172 3373 3565 6545 -133 -931 -1055 C ATOM 1115 CG PHE A 172 20.686 44.222 66.915 1.00 36.18 C ANISOU 1115 CG PHE A 172 3362 3697 6689 -159 -892 -923 C ATOM 1116 CD1 PHE A 172 20.163 44.210 65.630 1.00 38.17 C ANISOU 1116 CD1 PHE A 172 3626 3903 6974 -158 -783 -763 C ATOM 1117 CD2 PHE A 172 22.010 43.838 67.092 1.00 38.70 C ANISOU 1117 CD2 PHE A 172 3568 4112 7024 -178 -967 -968 C ATOM 1118 CE1 PHE A 172 20.945 43.806 64.542 1.00 38.76 C ANISOU 1118 CE1 PHE A 172 3619 4026 7082 -181 -733 -649 C ATOM 1119 CE2 PHE A 172 22.790 43.429 66.004 1.00 41.15 C ANISOU 1119 CE2 PHE A 172 3774 4474 7386 -195 -913 -859 C ATOM 1120 CZ PHE A 172 22.255 43.420 64.735 1.00 38.16 C ANISOU 1120 CZ PHE A 172 3426 4048 7027 -201 -788 -700 C ATOM 1121 N ILE A 173 17.782 44.502 70.570 1.00 33.18 N ANISOU 1121 N ILE A 173 3340 3313 5955 -13 -957 -1290 N ATOM 1122 CA ILE A 173 17.177 45.124 71.750 1.00 33.71 C ANISOU 1122 CA ILE A 173 3485 3349 5974 1 -972 -1455 C ATOM 1123 C ILE A 173 16.970 44.128 72.896 1.00 39.22 C ANISOU 1123 C ILE A 173 4301 4181 6419 59 -1006 -1515 C ATOM 1124 O ILE A 173 17.423 44.389 74.012 1.00 40.60 O ANISOU 1124 O ILE A 173 4517 4383 6525 58 -1099 -1666 O ATOM 1125 CB ILE A 173 15.853 45.885 71.402 1.00 36.01 C ANISOU 1125 CB ILE A 173 3799 3535 6349 25 -863 -1448 C ATOM 1126 CG1 ILE A 173 16.010 46.773 70.149 1.00 35.99 C ANISOU 1126 CG1 ILE A 173 3714 3388 6573 -17 -828 -1349 C ATOM 1127 CG2 ILE A 173 15.331 46.696 72.602 1.00 37.63 C ANISOU 1127 CG2 ILE A 173 4070 3695 6532 44 -872 -1645 C ATOM 1128 CD1 ILE A 173 14.735 47.035 69.395 1.00 40.76 C ANISOU 1128 CD1 ILE A 173 4332 3932 7224 40 -731 -1263 C ATOM 1129 N PHE A 174 16.281 43.001 72.623 1.00 35.28 N ANISOU 1129 N PHE A 174 3869 3759 5776 101 -932 -1398 N ATOM 1130 CA PHE A 174 15.876 42.016 73.628 1.00 35.60 C ANISOU 1130 CA PHE A 174 4055 3905 5567 145 -928 -1425 C ATOM 1131 C PHE A 174 16.819 40.890 74.040 1.00 40.02 C ANISOU 1131 C PHE A 174 4680 4562 5965 183 -1031 -1390 C ATOM 1132 O PHE A 174 16.826 40.553 75.225 1.00 40.55 O ANISOU 1132 O PHE A 174 4875 4691 5842 216 -1079 -1472 O ATOM 1133 CB PHE A 174 14.451 41.506 73.365 1.00 36.58 C ANISOU 1133 CB PHE A 174 4235 4048 5614 154 -780 -1355 C ATOM 1134 CG PHE A 174 13.457 42.613 73.090 1.00 38.34 C ANISOU 1134 CG PHE A 174 4393 4189 5985 148 -693 -1409 C ATOM 1135 CD1 PHE A 174 12.869 42.745 71.840 1.00 40.42 C ANISOU 1135 CD1 PHE A 174 4572 4406 6381 147 -624 -1295 C ATOM 1136 CD2 PHE A 174 13.123 43.533 74.077 1.00 41.82 C ANISOU 1136 CD2 PHE A 174 4864 4599 6426 158 -690 -1580 C ATOM 1137 CE1 PHE A 174 11.968 43.777 71.579 1.00 41.76 C ANISOU 1137 CE1 PHE A 174 4683 4495 6688 168 -563 -1342 C ATOM 1138 CE2 PHE A 174 12.219 44.565 73.816 1.00 45.06 C ANISOU 1138 CE2 PHE A 174 5216 4923 6983 177 -616 -1637 C ATOM 1139 CZ PHE A 174 11.642 44.676 72.570 1.00 42.18 C ANISOU 1139 CZ PHE A 174 4764 4509 6754 188 -557 -1513 C ATOM 1140 N ALA A 175 17.583 40.290 73.099 1.00 36.37 N ANISOU 1140 N ALA A 175 4143 4114 5563 194 -1062 -1269 N ATOM 1141 CA ALA A 175 18.506 39.189 73.422 1.00 36.89 C ANISOU 1141 CA ALA A 175 4264 4265 5488 259 -1168 -1234 C ATOM 1142 C ALA A 175 19.626 39.664 74.328 1.00 43.44 C ANISOU 1142 C ALA A 175 5053 5135 6318 275 -1335 -1375 C ATOM 1143 O ALA A 175 20.329 40.619 73.988 1.00 43.55 O ANISOU 1143 O ALA A 175 4906 5111 6530 220 -1384 -1439 O ATOM 1144 CB ALA A 175 19.068 38.555 72.158 1.00 36.64 C ANISOU 1144 CB ALA A 175 4142 4238 5541 274 -1154 -1096 C ATOM 1145 N ASN A 176 19.748 39.035 75.511 1.00 42.06 N ANISOU 1145 N ASN A 176 5033 5034 5915 342 -1423 -1429 N ATOM 1146 CA ASN A 176 20.743 39.389 76.523 1.00 44.31 C ANISOU 1146 CA ASN A 176 5304 5379 6153 374 -1608 -1578 C ATOM 1147 C ASN A 176 21.126 38.206 77.397 1.00 50.69 C ANISOU 1147 C ASN A 176 6285 6280 6694 490 -1722 -1554 C ATOM 1148 O ASN A 176 20.300 37.322 77.638 1.00 50.02 O ANISOU 1148 O ASN A 176 6395 6194 6416 521 -1630 -1460 O ATOM 1149 CB ASN A 176 20.233 40.532 77.404 1.00 45.42 C ANISOU 1149 CB ASN A 176 5480 5484 6294 318 -1601 -1748 C ATOM 1150 CG ASN A 176 20.535 41.898 76.859 1.00 67.74 C ANISOU 1150 CG ASN A 176 8118 8220 9402 221 -1598 -1833 C ATOM 1151 OD1 ASN A 176 21.657 42.397 76.968 1.00 64.97 O ANISOU 1151 OD1 ASN A 176 7636 7886 9164 194 -1737 -1930 O ATOM 1152 ND2 ASN A 176 19.535 42.537 76.266 1.00 57.96 N ANISOU 1152 ND2 ASN A 176 6861 6877 8284 166 -1441 -1801 N ATOM 1153 N VAL A 177 22.376 38.214 77.893 1.00 49.61 N ANISOU 1153 N VAL A 177 6080 6222 6548 552 -1927 -1643 N ATOM 1154 CA VAL A 177 22.908 37.196 78.801 1.00 51.37 C ANISOU 1154 CA VAL A 177 6466 6535 6518 690 -2082 -1635 C ATOM 1155 C VAL A 177 22.502 37.617 80.222 1.00 59.17 C ANISOU 1155 C VAL A 177 7629 7555 7297 690 -2136 -1773 C ATOM 1156 O VAL A 177 22.622 38.794 80.570 1.00 60.16 O ANISOU 1156 O VAL A 177 7654 7672 7530 615 -2177 -1939 O ATOM 1157 CB VAL A 177 24.448 37.019 78.658 1.00 56.31 C ANISOU 1157 CB VAL A 177 6911 7248 7235 774 -2293 -1679 C ATOM 1158 CG1 VAL A 177 24.964 35.858 79.509 1.00 57.61 C ANISOU 1158 CG1 VAL A 177 7259 7497 7132 952 -2464 -1647 C ATOM 1159 CG2 VAL A 177 24.852 36.818 77.203 1.00 54.66 C ANISOU 1159 CG2 VAL A 177 6500 7012 7256 754 -2211 -1569 C ATOM 1160 N SER A 178 21.994 36.671 81.024 1.00 57.64 N ANISOU 1160 N SER A 178 7710 7388 6802 767 -2123 -1705 N ATOM 1161 CA SER A 178 21.565 36.927 82.396 1.00 59.99 C ANISOU 1161 CA SER A 178 8214 7729 6851 776 -2155 -1820 C ATOM 1162 C SER A 178 21.857 35.684 83.228 1.00 67.94 C ANISOU 1162 C SER A 178 9483 8797 7534 919 -2270 -1735 C ATOM 1163 O SER A 178 21.912 34.576 82.683 1.00 66.58 O ANISOU 1163 O SER A 178 9380 8593 7325 983 -2240 -1562 O ATOM 1164 CB SER A 178 20.119 37.405 82.420 1.00 62.51 C ANISOU 1164 CB SER A 178 8606 7983 7163 664 -1910 -1827 C ATOM 1165 OG SER A 178 19.258 36.379 81.962 1.00 70.09 O ANISOU 1165 OG SER A 178 9696 8900 8034 655 -1733 -1642 O ATOM 1166 N GLU A 179 22.034 35.861 84.532 1.00 69.02 N ANISOU 1166 N GLU A 179 9784 9010 7430 972 -2401 -1855 N ATOM 1167 CA GLU A 179 22.427 34.765 85.410 1.00 71.68 C ANISOU 1167 CA GLU A 179 10390 9406 7441 1126 -2546 -1781 C ATOM 1168 C GLU A 179 21.194 33.991 85.877 1.00 77.53 C ANISOU 1168 C GLU A 179 11454 10098 7906 1096 -2333 -1647 C ATOM 1169 O GLU A 179 20.653 34.263 86.949 1.00 78.74 O ANISOU 1169 O GLU A 179 11804 10293 7821 1074 -2295 -1728 O ATOM 1170 CB GLU A 179 23.226 35.250 86.624 1.00 75.94 C ANISOU 1170 CB GLU A 179 10978 10063 7813 1209 -2806 -1967 C ATOM 1171 CG GLU A 179 24.565 34.554 86.804 1.00 88.29 C ANISOU 1171 CG GLU A 179 12522 11712 9313 1396 -3102 -1948 C ATOM 1172 CD GLU A 179 25.512 35.333 87.695 1.00109.95 C ANISOU 1172 CD GLU A 179 15177 14583 12015 1446 -3385 -2180 C ATOM 1173 OE1 GLU A 179 25.147 36.450 88.119 1.00100.27 O ANISOU 1173 OE1 GLU A 179 13907 13365 10828 1325 -3342 -2359 O ATOM 1174 OE2 GLU A 179 26.621 34.830 87.971 1.00105.23 O ANISOU 1174 OE2 GLU A 179 14552 14080 11350 1613 -3656 -2193 O ATOM 1175 N ALA A 180 20.788 33.009 85.076 1.00 73.75 N ANISOU 1175 N ALA A 180 11031 9534 7457 1090 -2195 -1449 N ATOM 1176 CA ALA A 180 19.816 32.019 85.505 1.00 74.52 C ANISOU 1176 CA ALA A 180 11452 9579 7284 1069 -2021 -1298 C ATOM 1177 C ALA A 180 20.578 31.330 86.625 1.00 82.57 C ANISOU 1177 C ALA A 180 12739 10656 7978 1241 -2246 -1277 C ATOM 1178 O ALA A 180 21.809 31.345 86.643 1.00 83.24 O ANISOU 1178 O ALA A 180 12713 10800 8115 1382 -2511 -1330 O ATOM 1179 CB ALA A 180 19.375 31.163 84.335 1.00 73.20 C ANISOU 1179 CB ALA A 180 11259 9304 7251 1025 -1861 -1115 C ATOM 1180 N ASP A 181 19.855 30.795 87.602 1.00 81.55 N ANISOU 1180 N ASP A 181 12956 10522 7509 1229 -2143 -1212 N ATOM 1181 CA ASP A 181 20.486 30.237 88.794 1.00 84.58 C ANISOU 1181 CA ASP A 181 13636 10963 7537 1393 -2355 -1195 C ATOM 1182 C ASP A 181 21.627 29.297 88.428 1.00 88.24 C ANISOU 1182 C ASP A 181 14111 11399 8017 1591 -2592 -1082 C ATOM 1183 O ASP A 181 21.406 28.276 87.777 1.00 87.33 O ANISOU 1183 O ASP A 181 14092 11165 7923 1603 -2493 -895 O ATOM 1184 CB ASP A 181 19.455 29.501 89.652 1.00 88.11 C ANISOU 1184 CB ASP A 181 14491 11369 7618 1337 -2155 -1070 C ATOM 1185 N ASP A 182 22.848 29.632 88.841 1.00 84.91 N ANISOU 1185 N ASP A 182 13584 11089 7591 1750 -2909 -1205 N ATOM 1186 CA ASP A 182 23.973 28.765 88.527 1.00 84.84 C ANISOU 1186 CA ASP A 182 13560 11072 7604 1964 -3148 -1117 C ATOM 1187 C ASP A 182 24.535 28.649 87.126 1.00 84.14 C ANISOU 1187 C ASP A 182 13141 10941 7888 1980 -3154 -1086 C ATOM 1188 O ASP A 182 25.451 27.866 86.875 1.00 84.59 O ANISOU 1188 O ASP A 182 13192 10993 7956 2174 -3340 -1016 O ATOM 1189 CB ASP A 182 23.772 27.442 89.270 1.00 89.09 C ANISOU 1189 CB ASP A 182 14563 11530 7756 2094 -3165 -917 C ATOM 1190 CG ASP A 182 24.677 27.309 90.479 1.00106.67 C ANISOU 1190 CG ASP A 182 16978 13872 9681 2314 -3495 -975 C ATOM 1191 OD1 ASP A 182 24.345 26.520 91.388 1.00110.30 O ANISOU 1191 OD1 ASP A 182 17867 14285 9756 2388 -3492 -842 O ATOM 1192 OD2 ASP A 182 25.720 27.995 90.520 1.00114.03 O ANISOU 1192 OD2 ASP A 182 17628 14941 10756 2407 -3759 -1155 O ATOM 1193 N ARG A 183 23.984 29.431 86.204 1.00 76.06 N ANISOU 1193 N ARG A 183 11846 9889 7164 1785 -2947 -1140 N ATOM 1194 CA ARG A 183 24.439 29.415 84.818 1.00 72.93 C ANISOU 1194 CA ARG A 183 11137 9457 7116 1777 -2921 -1114 C ATOM 1195 C ARG A 183 24.027 30.693 84.099 1.00 73.44 C ANISOU 1195 C ARG A 183 10884 9532 7487 1573 -2767 -1236 C ATOM 1196 O ARG A 183 23.073 31.359 84.501 1.00 72.59 O ANISOU 1196 O ARG A 183 10839 9415 7327 1426 -2609 -1294 O ATOM 1197 CB ARG A 183 23.881 28.194 84.085 1.00 71.33 C ANISOU 1197 CB ARG A 183 11106 9107 6891 1783 -2748 -896 C ATOM 1198 CG ARG A 183 22.432 28.341 83.647 1.00 78.26 C ANISOU 1198 CG ARG A 183 12034 9890 7811 1556 -2420 -834 C ATOM 1199 CD ARG A 183 22.153 27.542 82.385 1.00 81.39 C ANISOU 1199 CD ARG A 183 12392 10166 8367 1528 -2274 -688 C ATOM 1200 NE ARG A 183 22.420 28.316 81.176 1.00 84.35 N ANISOU 1200 NE ARG A 183 12384 10568 9097 1454 -2233 -761 N ATOM 1201 CZ ARG A 183 22.721 27.780 79.998 1.00 95.73 C ANISOU 1201 CZ ARG A 183 13704 11952 10718 1489 -2200 -681 C ATOM 1202 NH1 ARG A 183 22.949 28.562 78.951 1.00 81.43 N ANISOU 1202 NH1 ARG A 183 11562 10174 9205 1413 -2153 -746 N ATOM 1203 NH2 ARG A 183 22.794 26.463 79.865 1.00 82.10 N ANISOU 1203 NH2 ARG A 183 12203 10128 8864 1601 -2208 -537 N ATOM 1204 N TYR A 184 24.748 31.034 83.036 1.00 67.87 N ANISOU 1204 N TYR A 184 9846 8843 7097 1570 -2808 -1273 N ATOM 1205 CA TYR A 184 24.447 32.243 82.283 1.00 65.23 C ANISOU 1205 CA TYR A 184 9222 8501 7060 1387 -2674 -1372 C ATOM 1206 C TYR A 184 23.496 31.947 81.159 1.00 64.61 C ANISOU 1206 C TYR A 184 9130 8307 7112 1273 -2407 -1232 C ATOM 1207 O TYR A 184 23.881 31.383 80.159 1.00 62.99 O ANISOU 1207 O TYR A 184 8819 8068 7045 1318 -2391 -1139 O ATOM 1208 CB TYR A 184 25.699 32.819 81.659 1.00 66.72 C ANISOU 1208 CB TYR A 184 9056 8767 7528 1418 -2831 -1478 C ATOM 1209 CG TYR A 184 26.557 33.614 82.592 1.00 70.91 C ANISOU 1209 CG TYR A 184 9486 9421 8037 1453 -3072 -1681 C ATOM 1210 CD1 TYR A 184 26.954 33.097 83.799 1.00 75.50 C ANISOU 1210 CD1 TYR A 184 10285 10080 8323 1611 -3284 -1711 C ATOM 1211 CD2 TYR A 184 26.988 34.867 82.254 1.00 71.49 C ANISOU 1211 CD2 TYR A 184 9254 9528 8381 1327 -3095 -1843 C ATOM 1212 CE1 TYR A 184 27.745 33.806 84.641 1.00 78.30 C ANISOU 1212 CE1 TYR A 184 10543 10558 8650 1645 -3523 -1909 C ATOM 1213 CE2 TYR A 184 27.774 35.586 83.097 1.00 74.67 C ANISOU 1213 CE2 TYR A 184 9559 10039 8773 1343 -3321 -2043 C ATOM 1214 CZ TYR A 184 28.153 35.049 84.288 1.00 84.27 C ANISOU 1214 CZ TYR A 184 10981 11347 9691 1504 -3541 -2083 C ATOM 1215 OH TYR A 184 28.943 35.758 85.147 1.00 87.33 O ANISOU 1215 OH TYR A 184 11271 11856 10056 1523 -3787 -2299 O ATOM 1216 N ILE A 185 22.251 32.352 81.323 1.00 59.14 N ANISOU 1216 N ILE A 185 8533 7564 6375 1127 -2202 -1231 N ATOM 1217 CA ILE A 185 21.218 32.170 80.297 1.00 56.27 C ANISOU 1217 CA ILE A 185 8142 7104 6134 1005 -1953 -1119 C ATOM 1218 C ILE A 185 21.197 33.324 79.281 1.00 57.17 C ANISOU 1218 C ILE A 185 7939 7207 6577 888 -1878 -1191 C ATOM 1219 O ILE A 185 21.245 34.488 79.674 1.00 57.22 O ANISOU 1219 O ILE A 185 7831 7245 6665 826 -1910 -1341 O ATOM 1220 CB ILE A 185 19.828 31.792 80.922 1.00 59.42 C ANISOU 1220 CB ILE A 185 8812 7457 6308 918 -1756 -1058 C ATOM 1221 CG1 ILE A 185 19.614 30.261 80.881 1.00 60.36 C ANISOU 1221 CG1 ILE A 185 9195 7502 6236 980 -1712 -874 C ATOM 1222 CG2 ILE A 185 18.639 32.532 80.282 1.00 57.95 C ANISOU 1222 CG2 ILE A 185 8498 7228 6290 747 -1523 -1079 C ATOM 1223 CD1 ILE A 185 18.505 29.690 81.816 1.00 70.33 C ANISOU 1223 CD1 ILE A 185 10784 8731 7205 913 -1558 -810 C ATOM 1224 N CYS A 186 21.158 32.984 77.980 1.00 50.96 N ANISOU 1224 N CYS A 186 7029 6366 5966 865 -1783 -1085 N ATOM 1225 CA CYS A 186 21.104 33.937 76.869 1.00 48.85 C ANISOU 1225 CA CYS A 186 6495 6074 5993 761 -1696 -1113 C ATOM 1226 C CYS A 186 19.997 33.816 75.833 1.00 50.04 C ANISOU 1226 C CYS A 186 6631 6146 6234 661 -1481 -1008 C ATOM 1227 O CYS A 186 20.076 32.957 74.955 1.00 49.05 O ANISOU 1227 O CYS A 186 6512 5990 6134 693 -1439 -890 O ATOM 1228 CB CYS A 186 22.362 33.837 76.002 1.00 48.99 C ANISOU 1228 CB CYS A 186 6300 6124 6191 828 -1803 -1101 C ATOM 1229 SG CYS A 186 22.107 34.235 74.243 1.00 50.52 S ANISOU 1229 SG CYS A 186 6274 6257 6665 725 -1633 -1020 S ATOM 1230 N ASP A 187 18.971 34.678 75.943 1.00 45.08 N ANISOU 1230 N ASP A 187 5983 5490 5654 550 -1354 -1063 N ATOM 1231 CA ASP A 187 17.812 34.808 75.047 1.00 42.82 C ANISOU 1231 CA ASP A 187 5655 5147 5469 453 -1163 -996 C ATOM 1232 C ASP A 187 17.059 36.109 75.246 1.00 44.47 C ANISOU 1232 C ASP A 187 5775 5337 5783 369 -1085 -1105 C ATOM 1233 O ASP A 187 17.325 36.842 76.202 1.00 45.34 O ANISOU 1233 O ASP A 187 5896 5473 5859 375 -1162 -1238 O ATOM 1234 CB ASP A 187 16.809 33.689 75.400 1.00 44.95 C ANISOU 1234 CB ASP A 187 6153 5401 5524 436 -1047 -906 C ATOM 1235 CG ASP A 187 16.226 33.744 76.792 1.00 58.05 C ANISOU 1235 CG ASP A 187 7995 7093 6968 421 -1019 -979 C ATOM 1236 OD1 ASP A 187 16.996 33.953 77.746 1.00 60.33 O ANISOU 1236 OD1 ASP A 187 8341 7427 7154 490 -1164 -1062 O ATOM 1237 OD2 ASP A 187 15.006 33.513 76.932 1.00 63.74 O ANISOU 1237 OD2 ASP A 187 8805 7802 7611 339 -852 -954 O ATOM 1238 N ARG A 188 16.101 36.377 74.346 1.00 37.62 N ANISOU 1238 N ARG A 188 4830 4425 5039 300 -941 -1054 N ATOM 1239 CA ARG A 188 15.270 37.570 74.364 1.00 36.31 C ANISOU 1239 CA ARG A 188 4576 4227 4993 241 -857 -1143 C ATOM 1240 C ARG A 188 14.495 37.770 75.654 1.00 39.42 C ANISOU 1240 C ARG A 188 5100 4654 5222 229 -802 -1252 C ATOM 1241 O ARG A 188 13.716 36.899 76.053 1.00 39.17 O ANISOU 1241 O ARG A 188 5215 4657 5013 211 -704 -1204 O ATOM 1242 CB ARG A 188 14.333 37.590 73.151 1.00 34.26 C ANISOU 1242 CB ARG A 188 4228 3928 4861 195 -726 -1051 C ATOM 1243 CG ARG A 188 15.053 37.598 71.813 1.00 39.33 C ANISOU 1243 CG ARG A 188 4738 4536 5669 202 -764 -954 C ATOM 1244 CD ARG A 188 14.290 36.767 70.818 1.00 44.73 C ANISOU 1244 CD ARG A 188 5436 5218 6340 181 -665 -830 C ATOM 1245 NE ARG A 188 14.201 37.426 69.518 1.00 54.66 N ANISOU 1245 NE ARG A 188 6546 6431 7791 163 -636 -775 N ATOM 1246 CZ ARG A 188 13.188 38.195 69.134 1.00 69.36 C ANISOU 1246 CZ ARG A 188 8339 8262 9752 136 -561 -791 C ATOM 1247 NH1 ARG A 188 13.185 38.741 67.925 1.00 60.22 N ANISOU 1247 NH1 ARG A 188 7074 7060 8748 133 -549 -722 N ATOM 1248 NH2 ARG A 188 12.169 38.423 69.954 1.00 51.88 N ANISOU 1248 NH2 ARG A 188 6166 6067 7478 121 -496 -875 N ATOM 1249 N PHE A 189 14.739 38.915 76.314 1.00 35.49 N ANISOU 1249 N PHE A 189 4556 4145 4781 231 -860 -1405 N ATOM 1250 CA PHE A 189 14.064 39.327 77.538 1.00 36.17 C ANISOU 1250 CA PHE A 189 4752 4266 4727 226 -808 -1541 C ATOM 1251 C PHE A 189 13.313 40.619 77.260 1.00 39.84 C ANISOU 1251 C PHE A 189 5088 4667 5385 198 -725 -1640 C ATOM 1252 O PHE A 189 13.922 41.606 76.845 1.00 39.31 O ANISOU 1252 O PHE A 189 4892 4524 5519 194 -805 -1694 O ATOM 1253 CB PHE A 189 15.058 39.493 78.696 1.00 39.50 C ANISOU 1253 CB PHE A 189 5263 4732 5013 271 -972 -1659 C ATOM 1254 CG PHE A 189 15.528 38.191 79.302 1.00 41.26 C ANISOU 1254 CG PHE A 189 5674 5025 4978 325 -1042 -1577 C ATOM 1255 CD1 PHE A 189 14.724 37.488 80.190 1.00 44.88 C ANISOU 1255 CD1 PHE A 189 6347 5532 5172 320 -938 -1561 C ATOM 1256 CD2 PHE A 189 16.784 37.685 79.008 1.00 42.83 C ANISOU 1256 CD2 PHE A 189 5840 5238 5197 385 -1210 -1518 C ATOM 1257 CE1 PHE A 189 15.158 36.288 80.751 1.00 46.20 C ANISOU 1257 CE1 PHE A 189 6722 5740 5093 375 -1005 -1470 C ATOM 1258 CE2 PHE A 189 17.218 36.486 79.569 1.00 46.07 C ANISOU 1258 CE2 PHE A 189 6437 5697 5369 461 -1288 -1439 C ATOM 1259 CZ PHE A 189 16.401 35.794 80.436 1.00 44.89 C ANISOU 1259 CZ PHE A 189 6529 5574 4952 456 -1189 -1408 C ATOM 1260 N TYR A 190 11.986 40.594 77.440 1.00 36.57 N ANISOU 1260 N TYR A 190 4702 4276 4918 178 -559 -1659 N ATOM 1261 CA TYR A 190 11.094 41.718 77.157 1.00 36.58 C ANISOU 1261 CA TYR A 190 4583 4221 5094 179 -468 -1748 C ATOM 1262 C TYR A 190 10.540 42.374 78.437 1.00 42.63 C ANISOU 1262 C TYR A 190 5428 5020 5751 197 -411 -1942 C ATOM 1263 O TYR A 190 10.589 41.737 79.491 1.00 43.58 O ANISOU 1263 O TYR A 190 5711 5227 5620 194 -400 -1976 O ATOM 1264 CB TYR A 190 9.915 41.230 76.299 1.00 36.75 C ANISOU 1264 CB TYR A 190 4537 4263 5164 155 -321 -1642 C ATOM 1265 CG TYR A 190 10.251 40.213 75.233 1.00 36.95 C ANISOU 1265 CG TYR A 190 4543 4290 5206 131 -345 -1454 C ATOM 1266 CD1 TYR A 190 9.797 38.900 75.332 1.00 38.47 C ANISOU 1266 CD1 TYR A 190 4842 4552 5222 90 -266 -1361 C ATOM 1267 CD2 TYR A 190 10.947 40.575 74.086 1.00 36.70 C ANISOU 1267 CD2 TYR A 190 4394 4183 5368 142 -431 -1373 C ATOM 1268 CE1 TYR A 190 10.063 37.966 74.333 1.00 37.68 C ANISOU 1268 CE1 TYR A 190 4735 4441 5141 71 -285 -1204 C ATOM 1269 CE2 TYR A 190 11.225 39.650 73.082 1.00 36.33 C ANISOU 1269 CE2 TYR A 190 4333 4142 5327 127 -443 -1214 C ATOM 1270 CZ TYR A 190 10.779 38.345 73.210 1.00 42.90 C ANISOU 1270 CZ TYR A 190 5274 5040 5986 97 -375 -1137 C ATOM 1271 OH TYR A 190 11.051 37.423 72.228 1.00 43.15 O ANISOU 1271 OH TYR A 190 5305 5067 6023 87 -389 -997 O ATOM 1272 N PRO A 191 9.955 43.604 78.372 1.00 39.80 N ANISOU 1272 N PRO A 191 4970 4590 5561 225 -363 -2068 N ATOM 1273 CA PRO A 191 9.378 44.212 79.586 1.00 41.52 C ANISOU 1273 CA PRO A 191 5265 4843 5668 254 -292 -2268 C ATOM 1274 C PRO A 191 8.214 43.418 80.181 1.00 46.24 C ANISOU 1274 C PRO A 191 5940 5572 6056 235 -104 -2268 C ATOM 1275 O PRO A 191 8.091 43.349 81.407 1.00 47.99 O ANISOU 1275 O PRO A 191 6306 5871 6059 238 -60 -2388 O ATOM 1276 CB PRO A 191 8.913 45.594 79.108 1.00 43.61 C ANISOU 1276 CB PRO A 191 5393 4983 6196 302 -271 -2371 C ATOM 1277 CG PRO A 191 9.668 45.848 77.866 1.00 46.58 C ANISOU 1277 CG PRO A 191 5658 5243 6796 286 -382 -2239 C ATOM 1278 CD PRO A 191 9.808 44.517 77.222 1.00 40.59 C ANISOU 1278 CD PRO A 191 4906 4567 5951 244 -373 -2037 C ATOM 1279 N ASN A 192 7.382 42.800 79.320 1.00 41.28 N ANISOU 1279 N ASN A 192 5223 4975 5488 205 9 -2137 N ATOM 1280 CA ASN A 192 6.219 42.005 79.731 1.00 41.83 C ANISOU 1280 CA ASN A 192 5333 5168 5393 157 206 -2126 C ATOM 1281 C ASN A 192 5.961 40.788 78.825 1.00 45.17 C ANISOU 1281 C ASN A 192 5732 5622 5809 85 248 -1926 C ATOM 1282 O ASN A 192 6.526 40.702 77.730 1.00 43.47 O ANISOU 1282 O ASN A 192 5438 5333 5746 93 138 -1805 O ATOM 1283 CB ASN A 192 4.967 42.887 79.861 1.00 42.40 C ANISOU 1283 CB ASN A 192 5273 5265 5573 202 356 -2279 C ATOM 1284 CG ASN A 192 4.754 43.850 78.722 1.00 58.01 C ANISOU 1284 CG ASN A 192 7050 7131 7860 272 301 -2275 C ATOM 1285 OD1 ASN A 192 4.336 43.474 77.624 1.00 51.00 O ANISOU 1285 OD1 ASN A 192 6042 6243 7093 256 316 -2144 O ATOM 1286 ND2 ASN A 192 5.043 45.119 78.961 1.00 49.18 N ANISOU 1286 ND2 ASN A 192 5908 5907 6869 352 231 -2419 N ATOM 1287 N ASP A 193 5.104 39.845 79.283 1.00 42.67 N ANISOU 1287 N ASP A 193 5491 5411 5310 7 418 -1898 N ATOM 1288 CA ASP A 193 4.751 38.634 78.532 1.00 41.40 C ANISOU 1288 CA ASP A 193 5328 5276 5128 -82 476 -1729 C ATOM 1289 C ASP A 193 3.863 38.872 77.304 1.00 44.49 C ANISOU 1289 C ASP A 193 5484 5665 5754 -85 525 -1700 C ATOM 1290 O ASP A 193 3.677 37.944 76.517 1.00 43.51 O ANISOU 1290 O ASP A 193 5345 5548 5640 -155 540 -1567 O ATOM 1291 CB ASP A 193 4.191 37.524 79.444 1.00 44.71 C ANISOU 1291 CB ASP A 193 5927 5789 5273 -188 642 -1702 C ATOM 1292 CG ASP A 193 3.016 37.928 80.306 1.00 58.65 C ANISOU 1292 CG ASP A 193 7656 7663 6965 -216 851 -1858 C ATOM 1293 OD1 ASP A 193 1.920 37.350 80.122 1.00 59.92 O ANISOU 1293 OD1 ASP A 193 7745 7904 7120 -316 1032 -1837 O ATOM 1294 OD2 ASP A 193 3.199 38.794 81.195 1.00 65.99 O ANISOU 1294 OD2 ASP A 193 8630 8605 7838 -143 840 -2010 O ATOM 1295 N LEU A 194 3.347 40.108 77.114 1.00 41.52 N ANISOU 1295 N LEU A 194 4936 5273 5565 0 534 -1825 N ATOM 1296 CA LEU A 194 2.535 40.478 75.947 1.00 40.89 C ANISOU 1296 CA LEU A 194 4634 5190 5713 31 549 -1804 C ATOM 1297 C LEU A 194 3.398 40.473 74.676 1.00 43.11 C ANISOU 1297 C LEU A 194 4878 5363 6138 59 378 -1655 C ATOM 1298 O LEU A 194 2.915 40.070 73.622 1.00 41.65 O ANISOU 1298 O LEU A 194 4586 5196 6045 35 382 -1563 O ATOM 1299 CB LEU A 194 1.866 41.853 76.125 1.00 42.19 C ANISOU 1299 CB LEU A 194 4652 5341 6036 145 583 -1975 C ATOM 1300 CG LEU A 194 0.874 42.004 77.275 1.00 49.15 C ANISOU 1300 CG LEU A 194 5526 6344 6804 138 774 -2149 C ATOM 1301 CD1 LEU A 194 0.606 43.462 77.566 1.00 50.62 C ANISOU 1301 CD1 LEU A 194 5622 6475 7138 281 764 -2330 C ATOM 1302 CD2 LEU A 194 -0.434 41.288 76.985 1.00 52.62 C ANISOU 1302 CD2 LEU A 194 5825 6926 7243 58 943 -2139 C ATOM 1303 N TRP A 195 4.682 40.885 74.798 1.00 39.34 N ANISOU 1303 N TRP A 195 4491 4786 5671 100 233 -1639 N ATOM 1304 CA TRP A 195 5.686 40.920 73.729 1.00 37.51 C ANISOU 1304 CA TRP A 195 4237 4456 5558 119 83 -1508 C ATOM 1305 C TRP A 195 5.939 39.544 73.101 1.00 40.38 C ANISOU 1305 C TRP A 195 4660 4853 5829 46 75 -1346 C ATOM 1306 O TRP A 195 6.281 39.478 71.916 1.00 38.80 O ANISOU 1306 O TRP A 195 4392 4604 5745 58 1 -1235 O ATOM 1307 CB TRP A 195 7.008 41.468 74.267 1.00 36.31 C ANISOU 1307 CB TRP A 195 4174 4225 5398 150 -47 -1550 C ATOM 1308 CG TRP A 195 7.088 42.960 74.366 1.00 37.97 C ANISOU 1308 CG TRP A 195 4310 4337 5779 223 -92 -1674 C ATOM 1309 CD1 TRP A 195 6.829 43.722 75.465 1.00 42.47 C ANISOU 1309 CD1 TRP A 195 4918 4907 6313 259 -56 -1855 C ATOM 1310 CD2 TRP A 195 7.544 43.865 73.351 1.00 37.24 C ANISOU 1310 CD2 TRP A 195 4120 4115 5913 264 -184 -1625 C ATOM 1311 NE1 TRP A 195 7.064 45.049 75.189 1.00 42.34 N ANISOU 1311 NE1 TRP A 195 4832 4756 6500 322 -124 -1929 N ATOM 1312 CE2 TRP A 195 7.503 45.164 73.895 1.00 42.53 C ANISOU 1312 CE2 TRP A 195 4778 4694 6689 321 -200 -1781 C ATOM 1313 CE3 TRP A 195 7.947 43.705 72.014 1.00 37.12 C ANISOU 1313 CE3 TRP A 195 4041 4048 6015 256 -244 -1464 C ATOM 1314 CZ2 TRP A 195 7.858 46.298 73.156 1.00 42.05 C ANISOU 1314 CZ2 TRP A 195 4650 4474 6852 362 -275 -1770 C ATOM 1315 CZ3 TRP A 195 8.304 44.826 71.284 1.00 38.67 C ANISOU 1315 CZ3 TRP A 195 4169 4104 6418 297 -311 -1447 C ATOM 1316 CH2 TRP A 195 8.266 46.103 71.855 1.00 40.82 C ANISOU 1316 CH2 TRP A 195 4440 4271 6799 345 -326 -1594 C ATOM 1317 N VAL A 196 5.797 38.454 73.900 1.00 37.68 N ANISOU 1317 N VAL A 196 4464 4584 5270 -29 153 -1332 N ATOM 1318 CA VAL A 196 5.959 37.052 73.472 1.00 36.87 C ANISOU 1318 CA VAL A 196 4456 4495 5057 -103 160 -1192 C ATOM 1319 C VAL A 196 4.941 36.764 72.355 1.00 41.70 C ANISOU 1319 C VAL A 196 4923 5140 5782 -146 225 -1141 C ATOM 1320 O VAL A 196 5.294 36.150 71.347 1.00 40.27 O ANISOU 1320 O VAL A 196 4738 4925 5636 -161 164 -1024 O ATOM 1321 CB VAL A 196 5.825 36.044 74.649 1.00 41.29 C ANISOU 1321 CB VAL A 196 5221 5109 5359 -177 253 -1194 C ATOM 1322 CG1 VAL A 196 6.209 34.634 74.215 1.00 40.19 C ANISOU 1322 CG1 VAL A 196 5215 4942 5115 -235 234 -1044 C ATOM 1323 CG2 VAL A 196 6.667 36.471 75.848 1.00 42.06 C ANISOU 1323 CG2 VAL A 196 5453 5197 5331 -120 184 -1273 C ATOM 1324 N VAL A 197 3.699 37.261 72.531 1.00 39.95 N ANISOU 1324 N VAL A 197 4569 4989 5620 -156 340 -1244 N ATOM 1325 CA VAL A 197 2.588 37.154 71.582 1.00 39.91 C ANISOU 1325 CA VAL A 197 4389 5041 5733 -184 394 -1233 C ATOM 1326 C VAL A 197 2.830 38.044 70.340 1.00 43.29 C ANISOU 1326 C VAL A 197 4677 5401 6371 -78 263 -1190 C ATOM 1327 O VAL A 197 2.599 37.575 69.225 1.00 42.40 O ANISOU 1327 O VAL A 197 4501 5299 6312 -100 228 -1103 O ATOM 1328 CB VAL A 197 1.237 37.439 72.279 1.00 45.64 C ANISOU 1328 CB VAL A 197 5005 5881 6456 -214 558 -1375 C ATOM 1329 CG1 VAL A 197 0.091 37.477 71.280 1.00 45.76 C ANISOU 1329 CG1 VAL A 197 4798 5970 6620 -221 585 -1387 C ATOM 1330 CG2 VAL A 197 0.960 36.409 73.368 1.00 46.59 C ANISOU 1330 CG2 VAL A 197 5282 6069 6351 -348 709 -1388 C ATOM 1331 N VAL A 198 3.322 39.304 70.529 1.00 40.12 N ANISOU 1331 N VAL A 198 4247 4921 6075 30 192 -1249 N ATOM 1332 CA VAL A 198 3.649 40.257 69.444 1.00 39.10 C ANISOU 1332 CA VAL A 198 4021 4699 6137 128 76 -1198 C ATOM 1333 C VAL A 198 4.736 39.658 68.539 1.00 42.10 C ANISOU 1333 C VAL A 198 4473 5021 6501 103 -24 -1043 C ATOM 1334 O VAL A 198 4.752 39.929 67.341 1.00 40.91 O ANISOU 1334 O VAL A 198 4249 4834 6462 144 -88 -958 O ATOM 1335 CB VAL A 198 4.067 41.669 69.948 1.00 43.41 C ANISOU 1335 CB VAL A 198 4560 5144 6791 224 28 -1295 C ATOM 1336 CG1 VAL A 198 4.029 42.697 68.821 1.00 43.18 C ANISOU 1336 CG1 VAL A 198 4427 5016 6965 322 -58 -1245 C ATOM 1337 CG2 VAL A 198 3.196 42.139 71.096 1.00 44.83 C ANISOU 1337 CG2 VAL A 198 4710 5383 6941 249 138 -1470 C ATOM 1338 N PHE A 199 5.631 38.838 69.111 1.00 38.91 N ANISOU 1338 N PHE A 199 4217 4614 5951 47 -36 -1008 N ATOM 1339 CA PHE A 199 6.681 38.201 68.333 1.00 37.98 C ANISOU 1339 CA PHE A 199 4163 4455 5814 36 -120 -878 C ATOM 1340 C PHE A 199 6.393 36.771 67.902 1.00 42.78 C ANISOU 1340 C PHE A 199 4832 5115 6306 -41 -80 -796 C ATOM 1341 O PHE A 199 7.063 36.269 66.993 1.00 42.13 O ANISOU 1341 O PHE A 199 4776 5004 6230 -37 -141 -693 O ATOM 1342 CB PHE A 199 8.052 38.369 68.983 1.00 39.72 C ANISOU 1342 CB PHE A 199 4479 4620 5994 57 -199 -886 C ATOM 1343 CG PHE A 199 8.539 39.795 68.945 1.00 41.55 C ANISOU 1343 CG PHE A 199 4636 4767 6385 118 -263 -938 C ATOM 1344 CD1 PHE A 199 8.472 40.541 67.771 1.00 44.24 C ANISOU 1344 CD1 PHE A 199 4873 5045 6893 157 -296 -876 C ATOM 1345 CD2 PHE A 199 9.080 40.389 70.074 1.00 44.51 C ANISOU 1345 CD2 PHE A 199 5061 5115 6735 132 -294 -1049 C ATOM 1346 CE1 PHE A 199 8.909 41.862 67.739 1.00 45.69 C ANISOU 1346 CE1 PHE A 199 5010 5122 7228 200 -346 -916 C ATOM 1347 CE2 PHE A 199 9.538 41.701 70.035 1.00 47.83 C ANISOU 1347 CE2 PHE A 199 5422 5438 7314 171 -353 -1107 C ATOM 1348 CZ PHE A 199 9.426 42.438 68.875 1.00 45.63 C ANISOU 1348 CZ PHE A 199 5047 5080 7212 201 -371 -1037 C ATOM 1349 N GLN A 200 5.388 36.115 68.515 1.00 40.15 N ANISOU 1349 N GLN A 200 4524 4858 5874 -119 32 -847 N ATOM 1350 CA GLN A 200 5.017 34.774 68.081 1.00 39.74 C ANISOU 1350 CA GLN A 200 4534 4838 5728 -213 77 -779 C ATOM 1351 C GLN A 200 4.096 34.893 66.882 1.00 43.75 C ANISOU 1351 C GLN A 200 4881 5390 6353 -220 75 -765 C ATOM 1352 O GLN A 200 4.300 34.173 65.908 1.00 42.75 O ANISOU 1352 O GLN A 200 4779 5249 6215 -244 32 -680 O ATOM 1353 CB GLN A 200 4.401 33.932 69.201 1.00 42.24 C ANISOU 1353 CB GLN A 200 4964 5205 5881 -320 206 -825 C ATOM 1354 CG GLN A 200 4.318 32.436 68.866 1.00 62.33 C ANISOU 1354 CG GLN A 200 7635 7736 8311 -427 242 -741 C ATOM 1355 CD GLN A 200 5.619 31.852 68.348 1.00 82.04 C ANISOU 1355 CD GLN A 200 10258 10144 10769 -371 126 -633 C ATOM 1356 OE1 GLN A 200 6.632 31.779 69.057 1.00 78.15 O ANISOU 1356 OE1 GLN A 200 9897 9606 10191 -315 73 -615 O ATOM 1357 NE2 GLN A 200 5.613 31.426 67.094 1.00 72.85 N ANISOU 1357 NE2 GLN A 200 9049 8966 9665 -378 82 -571 N ATOM 1358 N PHE A 201 3.124 35.841 66.930 1.00 41.22 N ANISOU 1358 N PHE A 201 4396 5121 6145 -181 109 -855 N ATOM 1359 CA PHE A 201 2.181 36.120 65.843 1.00 41.42 C ANISOU 1359 CA PHE A 201 4247 5200 6289 -157 84 -857 C ATOM 1360 C PHE A 201 2.946 36.607 64.616 1.00 46.15 C ANISOU 1360 C PHE A 201 4834 5725 6976 -64 -48 -752 C ATOM 1361 O PHE A 201 2.679 36.131 63.512 1.00 46.07 O ANISOU 1361 O PHE A 201 4787 5743 6973 -80 -92 -691 O ATOM 1362 CB PHE A 201 1.118 37.156 66.263 1.00 44.20 C ANISOU 1362 CB PHE A 201 4429 5613 6750 -95 133 -983 C ATOM 1363 CG PHE A 201 -0.230 37.074 65.570 1.00 46.42 C ANISOU 1363 CG PHE A 201 4519 6009 7111 -107 150 -1030 C ATOM 1364 CD1 PHE A 201 -1.393 37.439 66.235 1.00 50.93 C ANISOU 1364 CD1 PHE A 201 4939 6684 7728 -108 253 -1170 C ATOM 1365 CD2 PHE A 201 -0.334 36.649 64.250 1.00 47.98 C ANISOU 1365 CD2 PHE A 201 4675 6221 7336 -112 60 -946 C ATOM 1366 CE1 PHE A 201 -2.634 37.375 65.593 1.00 52.89 C ANISOU 1366 CE1 PHE A 201 4978 7055 8062 -112 256 -1227 C ATOM 1367 CE2 PHE A 201 -1.574 36.575 63.614 1.00 51.94 C ANISOU 1367 CE2 PHE A 201 4987 6840 7906 -119 53 -1002 C ATOM 1368 CZ PHE A 201 -2.717 36.944 64.288 1.00 51.54 C ANISOU 1368 CZ PHE A 201 4767 6898 7916 -118 146 -1143 C ATOM 1369 N GLN A 202 3.917 37.524 64.814 1.00 43.00 N ANISOU 1369 N GLN A 202 4473 5232 6634 20 -105 -734 N ATOM 1370 CA GLN A 202 4.765 38.053 63.744 1.00 42.51 C ANISOU 1370 CA GLN A 202 4412 5089 6650 91 -206 -629 C ATOM 1371 C GLN A 202 5.556 36.920 63.074 1.00 47.17 C ANISOU 1371 C GLN A 202 5107 5676 7142 39 -233 -525 C ATOM 1372 O GLN A 202 5.662 36.911 61.850 1.00 46.66 O ANISOU 1372 O GLN A 202 5018 5605 7107 68 -287 -441 O ATOM 1373 CB GLN A 202 5.704 39.136 64.286 1.00 43.75 C ANISOU 1373 CB GLN A 202 4599 5144 6881 151 -242 -649 C ATOM 1374 CG GLN A 202 6.452 39.911 63.210 1.00 53.49 C ANISOU 1374 CG GLN A 202 5817 6285 8221 213 -322 -547 C ATOM 1375 CD GLN A 202 7.905 40.036 63.568 1.00 69.10 C ANISOU 1375 CD GLN A 202 7873 8190 10192 197 -352 -522 C ATOM 1376 OE1 GLN A 202 8.349 41.064 64.084 1.00 63.94 O ANISOU 1376 OE1 GLN A 202 7212 7455 9629 224 -372 -573 O ATOM 1377 NE2 GLN A 202 8.668 38.976 63.338 1.00 60.84 N ANISOU 1377 NE2 GLN A 202 6899 7175 9044 153 -359 -458 N ATOM 1378 N HIS A 203 6.073 35.956 63.872 1.00 44.76 N ANISOU 1378 N HIS A 203 4926 5372 6708 -26 -195 -533 N ATOM 1379 CA HIS A 203 6.824 34.800 63.378 1.00 44.46 C ANISOU 1379 CA HIS A 203 5002 5319 6571 -59 -216 -451 C ATOM 1380 C HIS A 203 5.970 33.921 62.469 1.00 46.57 C ANISOU 1380 C HIS A 203 5253 5641 6802 -119 -200 -427 C ATOM 1381 O HIS A 203 6.432 33.549 61.394 1.00 45.51 O ANISOU 1381 O HIS A 203 5142 5492 6656 -100 -248 -351 O ATOM 1382 CB HIS A 203 7.440 33.978 64.532 1.00 46.21 C ANISOU 1382 CB HIS A 203 5375 5522 6659 -97 -188 -469 C ATOM 1383 CG HIS A 203 7.959 32.631 64.116 1.00 50.04 C ANISOU 1383 CG HIS A 203 5990 5987 7035 -127 -197 -399 C ATOM 1384 ND1 HIS A 203 7.332 31.459 64.515 1.00 52.69 N ANISOU 1384 ND1 HIS A 203 6435 6333 7252 -222 -129 -410 N ATOM 1385 CD2 HIS A 203 8.997 32.313 63.310 1.00 51.74 C ANISOU 1385 CD2 HIS A 203 6241 6167 7251 -74 -258 -325 C ATOM 1386 CE1 HIS A 203 8.014 30.470 63.958 1.00 51.93 C ANISOU 1386 CE1 HIS A 203 6451 6192 7089 -213 -161 -344 C ATOM 1387 NE2 HIS A 203 9.025 30.933 63.222 1.00 51.68 N ANISOU 1387 NE2 HIS A 203 6372 6141 7124 -118 -238 -296 N ATOM 1388 N ILE A 204 4.735 33.600 62.898 1.00 42.70 N ANISOU 1388 N ILE A 204 4714 5218 6290 -197 -129 -502 N ATOM 1389 CA ILE A 204 3.788 32.764 62.151 1.00 42.39 C ANISOU 1389 CA ILE A 204 4639 5242 6225 -280 -112 -508 C ATOM 1390 C ILE A 204 3.404 33.453 60.829 1.00 46.37 C ANISOU 1390 C ILE A 204 5007 5782 6830 -204 -199 -479 C ATOM 1391 O ILE A 204 3.334 32.795 59.787 1.00 45.82 O ANISOU 1391 O ILE A 204 4957 5730 6722 -228 -242 -438 O ATOM 1392 CB ILE A 204 2.560 32.380 63.038 1.00 46.22 C ANISOU 1392 CB ILE A 204 5076 5802 6681 -396 1 -609 C ATOM 1393 CG1 ILE A 204 3.011 31.615 64.304 1.00 46.61 C ANISOU 1393 CG1 ILE A 204 5309 5804 6596 -471 87 -613 C ATOM 1394 CG2 ILE A 204 1.527 31.558 62.261 1.00 47.30 C ANISOU 1394 CG2 ILE A 204 5146 6013 6813 -503 13 -636 C ATOM 1395 CD1 ILE A 204 2.086 31.748 65.531 1.00 54.34 C ANISOU 1395 CD1 ILE A 204 6249 6849 7548 -549 217 -714 C ATOM 1396 N MET A 205 3.225 34.785 60.878 1.00 43.26 N ANISOU 1396 N MET A 205 4498 5385 6552 -103 -230 -498 N ATOM 1397 CA MET A 205 2.858 35.629 59.744 1.00 43.48 C ANISOU 1397 CA MET A 205 4416 5430 6675 -5 -319 -460 C ATOM 1398 C MET A 205 3.943 35.674 58.648 1.00 45.44 C ANISOU 1398 C MET A 205 4750 5613 6901 50 -390 -334 C ATOM 1399 O MET A 205 3.695 35.210 57.535 1.00 45.16 O ANISOU 1399 O MET A 205 4713 5621 6824 47 -441 -291 O ATOM 1400 CB MET A 205 2.482 37.042 60.233 1.00 46.74 C ANISOU 1400 CB MET A 205 4720 5821 7218 97 -325 -512 C ATOM 1401 CG MET A 205 1.367 37.676 59.448 1.00 51.97 C ANISOU 1401 CG MET A 205 5226 6548 7971 181 -391 -533 C ATOM 1402 SD MET A 205 -0.206 36.821 59.685 1.00 57.95 S ANISOU 1402 SD MET A 205 5833 7474 8710 79 -336 -664 S ATOM 1403 CE MET A 205 -1.031 37.285 58.191 1.00 55.84 C ANISOU 1403 CE MET A 205 5427 7279 8509 192 -483 -633 C ATOM 1404 N VAL A 206 5.141 36.196 58.972 1.00 40.04 N ANISOU 1404 N VAL A 206 4137 4836 6239 92 -389 -285 N ATOM 1405 CA VAL A 206 6.263 36.341 58.039 1.00 38.59 C ANISOU 1405 CA VAL A 206 4019 4596 6047 135 -431 -172 C ATOM 1406 C VAL A 206 6.951 34.990 57.715 1.00 40.84 C ANISOU 1406 C VAL A 206 4419 4895 6205 79 -414 -138 C ATOM 1407 O VAL A 206 7.456 34.813 56.607 1.00 40.64 O ANISOU 1407 O VAL A 206 4430 4868 6144 107 -442 -58 O ATOM 1408 CB VAL A 206 7.271 37.437 58.509 1.00 42.18 C ANISOU 1408 CB VAL A 206 4480 4951 6593 184 -431 -148 C ATOM 1409 CG1 VAL A 206 8.174 37.894 57.366 1.00 41.94 C ANISOU 1409 CG1 VAL A 206 4479 4871 6585 227 -461 -27 C ATOM 1410 CG2 VAL A 206 6.551 38.643 59.119 1.00 42.70 C ANISOU 1410 CG2 VAL A 206 4459 4985 6779 235 -436 -215 C ATOM 1411 N GLY A 207 6.915 34.061 58.665 1.00 36.07 N ANISOU 1411 N GLY A 207 3879 4297 5528 7 -365 -198 N ATOM 1412 CA GLY A 207 7.553 32.769 58.502 1.00 34.90 C ANISOU 1412 CA GLY A 207 3858 4136 5265 -32 -351 -174 C ATOM 1413 C GLY A 207 6.738 31.700 57.795 1.00 37.38 C ANISOU 1413 C GLY A 207 4204 4498 5501 -101 -350 -191 C ATOM 1414 O GLY A 207 7.273 30.973 56.958 1.00 37.08 O ANISOU 1414 O GLY A 207 4247 4448 5392 -92 -368 -148 O ATOM 1415 N LEU A 208 5.454 31.585 58.126 1.00 32.79 N ANISOU 1415 N LEU A 208 3551 3974 4933 -175 -326 -265 N ATOM 1416 CA LEU A 208 4.645 30.493 57.580 1.00 32.49 C ANISOU 1416 CA LEU A 208 3538 3980 4828 -273 -323 -303 C ATOM 1417 C LEU A 208 3.313 30.740 56.845 1.00 36.88 C ANISOU 1417 C LEU A 208 3943 4640 5431 -299 -367 -355 C ATOM 1418 O LEU A 208 3.016 29.995 55.910 1.00 37.44 O ANISOU 1418 O LEU A 208 4041 4742 5443 -343 -407 -362 O ATOM 1419 CB LEU A 208 4.311 29.430 58.657 1.00 32.63 C ANISOU 1419 CB LEU A 208 3654 3970 4773 -401 -234 -360 C ATOM 1420 CG LEU A 208 3.254 28.365 58.302 1.00 37.62 C ANISOU 1420 CG LEU A 208 4292 4642 5360 -546 -210 -424 C ATOM 1421 CD1 LEU A 208 3.819 27.297 57.379 1.00 37.18 C ANISOU 1421 CD1 LEU A 208 4383 4529 5214 -557 -247 -390 C ATOM 1422 CD2 LEU A 208 2.686 27.734 59.542 1.00 40.73 C ANISOU 1422 CD2 LEU A 208 4741 5021 5715 -684 -97 -481 C ATOM 1423 N ILE A 209 2.513 31.747 57.277 1.00 32.60 N ANISOU 1423 N ILE A 209 3242 4153 4991 -266 -366 -402 N ATOM 1424 CA ILE A 209 1.192 32.048 56.708 1.00 33.20 C ANISOU 1424 CA ILE A 209 3143 4343 5127 -270 -418 -467 C ATOM 1425 C ILE A 209 1.382 32.803 55.395 1.00 37.60 C ANISOU 1425 C ILE A 209 3667 4914 5706 -136 -539 -388 C ATOM 1426 O ILE A 209 0.903 32.322 54.370 1.00 38.07 O ANISOU 1426 O ILE A 209 3707 5041 5716 -156 -613 -397 O ATOM 1427 CB ILE A 209 0.127 32.645 57.681 1.00 37.01 C ANISOU 1427 CB ILE A 209 3459 4896 5706 -288 -361 -572 C ATOM 1428 CG1 ILE A 209 -0.402 31.556 58.654 1.00 37.93 C ANISOU 1428 CG1 ILE A 209 3608 5038 5767 -470 -234 -658 C ATOM 1429 CG2 ILE A 209 -1.032 33.320 56.930 1.00 38.53 C ANISOU 1429 CG2 ILE A 209 3444 5206 5990 -218 -453 -623 C ATOM 1430 CD1 ILE A 209 -1.259 32.058 59.857 1.00 45.55 C ANISOU 1430 CD1 ILE A 209 4440 6067 6799 -502 -130 -763 C ATOM 1431 N LEU A 210 2.100 33.942 55.409 1.00 33.98 N ANISOU 1431 N LEU A 210 3217 4385 5308 -11 -560 -310 N ATOM 1432 CA LEU A 210 2.349 34.729 54.193 1.00 34.22 C ANISOU 1432 CA LEU A 210 3247 4408 5348 113 -658 -211 C ATOM 1433 C LEU A 210 3.164 33.973 53.104 1.00 39.06 C ANISOU 1433 C LEU A 210 3999 5007 5834 101 -683 -131 C ATOM 1434 O LEU A 210 2.662 33.909 51.980 1.00 39.96 O ANISOU 1434 O LEU A 210 4094 5191 5898 135 -772 -114 O ATOM 1435 CB LEU A 210 2.898 36.136 54.483 1.00 33.93 C ANISOU 1435 CB LEU A 210 3199 4278 5416 227 -660 -147 C ATOM 1436 CG LEU A 210 1.962 37.106 55.207 1.00 38.99 C ANISOU 1436 CG LEU A 210 3694 4933 6186 288 -665 -226 C ATOM 1437 CD1 LEU A 210 2.750 38.209 55.894 1.00 38.72 C ANISOU 1437 CD1 LEU A 210 3696 4772 6244 351 -630 -193 C ATOM 1438 CD2 LEU A 210 0.934 37.690 54.259 1.00 42.09 C ANISOU 1438 CD2 LEU A 210 3974 5398 6619 394 -781 -221 C ATOM 1439 N PRO A 211 4.341 33.327 53.393 1.00 34.70 N ANISOU 1439 N PRO A 211 3583 4383 5220 61 -613 -96 N ATOM 1440 CA PRO A 211 5.028 32.553 52.336 1.00 34.21 C ANISOU 1440 CA PRO A 211 3641 4320 5036 60 -628 -42 C ATOM 1441 C PRO A 211 4.215 31.335 51.871 1.00 37.66 C ANISOU 1441 C PRO A 211 4099 4828 5383 -32 -658 -125 C ATOM 1442 O PRO A 211 4.270 30.982 50.691 1.00 37.31 O ANISOU 1442 O PRO A 211 4110 4823 5244 -10 -713 -100 O ATOM 1443 CB PRO A 211 6.355 32.146 52.988 1.00 35.03 C ANISOU 1443 CB PRO A 211 3852 4337 5120 48 -547 -15 C ATOM 1444 CG PRO A 211 6.094 32.177 54.431 1.00 39.35 C ANISOU 1444 CG PRO A 211 4364 4856 5731 -4 -496 -83 C ATOM 1445 CD PRO A 211 5.089 33.258 54.666 1.00 35.51 C ANISOU 1445 CD PRO A 211 3733 4409 5352 28 -528 -113 C ATOM 1446 N GLY A 212 3.451 30.740 52.793 1.00 33.98 N ANISOU 1446 N GLY A 212 3590 4377 4943 -143 -616 -226 N ATOM 1447 CA GLY A 212 2.563 29.611 52.529 1.00 34.56 C ANISOU 1447 CA GLY A 212 3666 4508 4958 -267 -631 -322 C ATOM 1448 C GLY A 212 1.467 29.936 51.529 1.00 39.30 C ANISOU 1448 C GLY A 212 4135 5232 5566 -245 -747 -362 C ATOM 1449 O GLY A 212 1.158 29.099 50.675 1.00 39.64 O ANISOU 1449 O GLY A 212 4222 5319 5521 -302 -802 -407 O ATOM 1450 N ILE A 213 0.880 31.165 51.610 1.00 35.56 N ANISOU 1450 N ILE A 213 3503 4812 5195 -149 -798 -351 N ATOM 1451 CA ILE A 213 -0.158 31.638 50.681 1.00 36.39 C ANISOU 1451 CA ILE A 213 3470 5041 5316 -86 -934 -380 C ATOM 1452 C ILE A 213 0.462 31.777 49.282 1.00 40.71 C ANISOU 1452 C ILE A 213 4135 5588 5747 16 -1024 -276 C ATOM 1453 O ILE A 213 -0.075 31.200 48.337 1.00 41.78 O ANISOU 1453 O ILE A 213 4269 5812 5793 -11 -1120 -325 O ATOM 1454 CB ILE A 213 -0.894 32.922 51.177 1.00 39.79 C ANISOU 1454 CB ILE A 213 3716 5511 5891 17 -964 -394 C ATOM 1455 CG1 ILE A 213 -1.738 32.613 52.438 1.00 40.58 C ANISOU 1455 CG1 ILE A 213 3680 5655 6082 -104 -869 -528 C ATOM 1456 CG2 ILE A 213 -1.783 33.528 50.073 1.00 41.85 C ANISOU 1456 CG2 ILE A 213 3858 5887 6156 136 -1134 -396 C ATOM 1457 CD1 ILE A 213 -2.104 33.819 53.334 1.00 47.21 C ANISOU 1457 CD1 ILE A 213 4383 6489 7064 -7 -837 -549 C ATOM 1458 N VAL A 214 1.628 32.468 49.173 1.00 35.46 N ANISOU 1458 N VAL A 214 3577 4824 5072 115 -984 -143 N ATOM 1459 CA VAL A 214 2.374 32.674 47.919 1.00 34.87 C ANISOU 1459 CA VAL A 214 3628 4739 4880 206 -1029 -27 C ATOM 1460 C VAL A 214 2.724 31.326 47.246 1.00 39.11 C ANISOU 1460 C VAL A 214 4299 5297 5263 125 -1020 -70 C ATOM 1461 O VAL A 214 2.383 31.146 46.076 1.00 40.19 O ANISOU 1461 O VAL A 214 4470 5515 5285 159 -1120 -70 O ATOM 1462 CB VAL A 214 3.627 33.577 48.099 1.00 37.07 C ANISOU 1462 CB VAL A 214 3985 4902 5197 286 -950 110 C ATOM 1463 CG1 VAL A 214 4.278 33.903 46.756 1.00 37.20 C ANISOU 1463 CG1 VAL A 214 4120 4922 5090 374 -983 236 C ATOM 1464 CG2 VAL A 214 3.288 34.860 48.851 1.00 36.90 C ANISOU 1464 CG2 VAL A 214 3850 4835 5335 356 -955 132 C ATOM 1465 N ILE A 215 3.377 30.389 47.990 1.00 34.02 N ANISOU 1465 N ILE A 215 3740 4575 4612 30 -908 -111 N ATOM 1466 CA ILE A 215 3.778 29.059 47.504 1.00 33.49 C ANISOU 1466 CA ILE A 215 3817 4492 4415 -40 -885 -162 C ATOM 1467 C ILE A 215 2.551 28.268 47.051 1.00 38.59 C ANISOU 1467 C ILE A 215 4418 5231 5016 -140 -977 -292 C ATOM 1468 O ILE A 215 2.528 27.789 45.912 1.00 38.94 O ANISOU 1468 O ILE A 215 4543 5325 4927 -127 -1047 -313 O ATOM 1469 CB ILE A 215 4.643 28.268 48.538 1.00 35.27 C ANISOU 1469 CB ILE A 215 4142 4600 4659 -103 -760 -179 C ATOM 1470 CG1 ILE A 215 6.012 28.945 48.780 1.00 34.44 C ANISOU 1470 CG1 ILE A 215 4081 4423 4582 -2 -685 -64 C ATOM 1471 CG2 ILE A 215 4.831 26.810 48.100 1.00 36.47 C ANISOU 1471 CG2 ILE A 215 4445 4720 4691 -177 -746 -255 C ATOM 1472 CD1 ILE A 215 6.734 28.568 50.097 1.00 38.81 C ANISOU 1472 CD1 ILE A 215 4676 4876 5194 -36 -590 -75 C ATOM 1473 N LEU A 216 1.530 28.148 47.931 1.00 35.59 N ANISOU 1473 N LEU A 216 3901 4879 4742 -244 -972 -388 N ATOM 1474 CA LEU A 216 0.303 27.418 47.609 1.00 37.04 C ANISOU 1474 CA LEU A 216 4004 5160 4911 -368 -1051 -529 C ATOM 1475 C LEU A 216 -0.488 28.037 46.463 1.00 43.11 C ANISOU 1475 C LEU A 216 4662 6074 5642 -278 -1221 -539 C ATOM 1476 O LEU A 216 -1.175 27.295 45.763 1.00 44.33 O ANISOU 1476 O LEU A 216 4806 6311 5727 -359 -1314 -648 O ATOM 1477 CB LEU A 216 -0.580 27.129 48.834 1.00 37.22 C ANISOU 1477 CB LEU A 216 3897 5189 5057 -517 -981 -632 C ATOM 1478 CG LEU A 216 -0.330 25.790 49.523 1.00 41.51 C ANISOU 1478 CG LEU A 216 4584 5619 5568 -688 -864 -693 C ATOM 1479 CD1 LEU A 216 -0.683 25.862 50.990 1.00 41.31 C ANISOU 1479 CD1 LEU A 216 4485 5560 5652 -781 -742 -720 C ATOM 1480 CD2 LEU A 216 -1.117 24.668 48.859 1.00 45.61 C ANISOU 1480 CD2 LEU A 216 5119 6183 6028 -843 -924 -829 C ATOM 1481 N SER A 217 -0.360 29.369 46.235 1.00 39.63 N ANISOU 1481 N SER A 217 4160 5657 5241 -109 -1272 -424 N ATOM 1482 CA SER A 217 -1.015 30.056 45.117 1.00 41.00 C ANISOU 1482 CA SER A 217 4261 5955 5361 13 -1446 -403 C ATOM 1483 C SER A 217 -0.336 29.638 43.813 1.00 45.40 C ANISOU 1483 C SER A 217 5013 6520 5718 62 -1495 -350 C ATOM 1484 O SER A 217 -1.012 29.117 42.929 1.00 46.28 O ANISOU 1484 O SER A 217 5117 6742 5727 35 -1625 -440 O ATOM 1485 CB SER A 217 -0.950 31.572 45.285 1.00 43.88 C ANISOU 1485 CB SER A 217 4553 6300 5820 184 -1470 -279 C ATOM 1486 OG SER A 217 -1.641 31.993 46.448 1.00 51.34 O ANISOU 1486 OG SER A 217 5313 7250 6943 155 -1428 -346 O ATOM 1487 N CYS A 218 1.005 29.806 43.730 1.00 41.09 N ANISOU 1487 N CYS A 218 4634 5863 5113 122 -1382 -222 N ATOM 1488 CA CYS A 218 1.841 29.469 42.576 1.00 41.55 C ANISOU 1488 CA CYS A 218 4885 5921 4980 176 -1382 -161 C ATOM 1489 C CYS A 218 1.628 28.046 42.075 1.00 47.70 C ANISOU 1489 C CYS A 218 5754 6734 5636 61 -1411 -306 C ATOM 1490 O CYS A 218 1.251 27.878 40.913 1.00 49.17 O ANISOU 1490 O CYS A 218 5990 7023 5670 98 -1537 -338 O ATOM 1491 CB CYS A 218 3.312 29.748 42.865 1.00 40.16 C ANISOU 1491 CB CYS A 218 4830 5623 4808 224 -1221 -33 C ATOM 1492 SG CYS A 218 3.710 31.505 43.035 1.00 43.66 S ANISOU 1492 SG CYS A 218 5221 6017 5352 365 -1202 153 S ATOM 1493 N TYR A 219 1.817 27.029 42.948 1.00 43.96 N ANISOU 1493 N TYR A 219 5312 6169 5223 -76 -1304 -399 N ATOM 1494 CA TYR A 219 1.630 25.628 42.567 1.00 44.86 C ANISOU 1494 CA TYR A 219 5532 6276 5238 -199 -1319 -544 C ATOM 1495 C TYR A 219 0.187 25.230 42.267 1.00 51.09 C ANISOU 1495 C TYR A 219 6192 7186 6035 -310 -1467 -700 C ATOM 1496 O TYR A 219 -0.031 24.317 41.466 1.00 51.93 O ANISOU 1496 O TYR A 219 6392 7323 6014 -376 -1536 -813 O ATOM 1497 CB TYR A 219 2.348 24.665 43.521 1.00 44.87 C ANISOU 1497 CB TYR A 219 5644 6119 5287 -295 -1164 -576 C ATOM 1498 CG TYR A 219 3.851 24.748 43.373 1.00 45.79 C ANISOU 1498 CG TYR A 219 5912 6148 5338 -177 -1051 -463 C ATOM 1499 CD1 TYR A 219 4.623 25.434 44.308 1.00 46.17 C ANISOU 1499 CD1 TYR A 219 5923 6121 5499 -119 -945 -351 C ATOM 1500 CD2 TYR A 219 4.496 24.208 42.265 1.00 47.47 C ANISOU 1500 CD2 TYR A 219 6291 6370 5376 -118 -1052 -475 C ATOM 1501 CE1 TYR A 219 6.003 25.553 44.156 1.00 46.15 C ANISOU 1501 CE1 TYR A 219 6024 6058 5451 -16 -845 -258 C ATOM 1502 CE2 TYR A 219 5.873 24.337 42.094 1.00 47.71 C ANISOU 1502 CE2 TYR A 219 6429 6344 5355 -6 -937 -378 C ATOM 1503 CZ TYR A 219 6.625 24.994 43.053 1.00 54.47 C ANISOU 1503 CZ TYR A 219 7226 7130 6341 40 -835 -271 C ATOM 1504 OH TYR A 219 7.985 25.108 42.902 1.00 56.44 O ANISOU 1504 OH TYR A 219 7551 7338 6555 140 -723 -191 O ATOM 1505 N CYS A 220 -0.791 25.958 42.848 1.00 48.18 N ANISOU 1505 N CYS A 220 5598 6894 5813 -321 -1523 -715 N ATOM 1506 CA CYS A 220 -2.222 25.766 42.609 1.00 49.98 C ANISOU 1506 CA CYS A 220 5643 7269 6079 -412 -1671 -866 C ATOM 1507 C CYS A 220 -2.537 26.185 41.161 1.00 54.29 C ANISOU 1507 C CYS A 220 6200 7959 6467 -279 -1869 -855 C ATOM 1508 O CYS A 220 -3.337 25.529 40.498 1.00 56.17 O ANISOU 1508 O CYS A 220 6400 8306 6638 -365 -2006 -1005 O ATOM 1509 CB CYS A 220 -3.040 26.566 43.618 1.00 50.58 C ANISOU 1509 CB CYS A 220 5470 7393 6354 -418 -1661 -873 C ATOM 1510 SG CYS A 220 -4.831 26.337 43.492 1.00 57.49 S ANISOU 1510 SG CYS A 220 6060 8469 7317 -540 -1822 -1079 S ATOM 1511 N ILE A 221 -1.884 27.264 40.675 1.00 48.78 N ANISOU 1511 N ILE A 221 5569 7259 5706 -78 -1884 -677 N ATOM 1512 CA ILE A 221 -2.010 27.771 39.306 1.00 49.43 C ANISOU 1512 CA ILE A 221 5713 7460 5609 73 -2053 -621 C ATOM 1513 C ILE A 221 -1.284 26.797 38.360 1.00 53.27 C ANISOU 1513 C ILE A 221 6442 7925 5874 44 -2033 -657 C ATOM 1514 O ILE A 221 -1.824 26.470 37.303 1.00 54.75 O ANISOU 1514 O ILE A 221 6662 8238 5902 55 -2199 -744 O ATOM 1515 CB ILE A 221 -1.467 29.229 39.175 1.00 51.57 C ANISOU 1515 CB ILE A 221 6009 7698 5886 279 -2041 -402 C ATOM 1516 CG1 ILE A 221 -2.215 30.199 40.112 1.00 51.49 C ANISOU 1516 CG1 ILE A 221 5767 7699 6099 323 -2065 -385 C ATOM 1517 CG2 ILE A 221 -1.547 29.725 37.730 1.00 54.08 C ANISOU 1517 CG2 ILE A 221 6435 8125 5987 437 -2206 -322 C ATOM 1518 CD1 ILE A 221 -1.452 31.481 40.477 1.00 56.20 C ANISOU 1518 CD1 ILE A 221 6404 8181 6768 467 -1974 -183 C ATOM 1519 N ILE A 222 -0.069 26.330 38.757 1.00 47.51 N ANISOU 1519 N ILE A 222 5875 7042 5133 15 -1834 -603 N ATOM 1520 CA ILE A 222 0.778 25.395 37.996 1.00 47.05 C ANISOU 1520 CA ILE A 222 6052 6942 4885 3 -1775 -639 C ATOM 1521 C ILE A 222 0.076 24.049 37.746 1.00 52.06 C ANISOU 1521 C ILE A 222 6711 7600 5468 -164 -1854 -864 C ATOM 1522 O ILE A 222 -0.038 23.652 36.591 1.00 53.21 O ANISOU 1522 O ILE A 222 6970 7832 5415 -138 -1963 -935 O ATOM 1523 CB ILE A 222 2.217 25.250 38.598 1.00 47.80 C ANISOU 1523 CB ILE A 222 6275 6872 5013 26 -1550 -538 C ATOM 1524 CG1 ILE A 222 2.987 26.590 38.526 1.00 46.91 C ANISOU 1524 CG1 ILE A 222 6163 6750 4910 186 -1485 -323 C ATOM 1525 CG2 ILE A 222 3.024 24.132 37.910 1.00 49.07 C ANISOU 1525 CG2 ILE A 222 6660 6984 4999 14 -1482 -612 C ATOM 1526 CD1 ILE A 222 4.146 26.747 39.533 1.00 50.10 C ANISOU 1526 CD1 ILE A 222 6585 7008 5442 191 -1286 -230 C ATOM 1527 N ILE A 223 -0.419 23.374 38.803 1.00 48.18 N ANISOU 1527 N ILE A 223 6123 7033 5148 -340 -1798 -977 N ATOM 1528 CA ILE A 223 -1.096 22.076 38.660 1.00 49.64 C ANISOU 1528 CA ILE A 223 6337 7213 5311 -532 -1855 -1193 C ATOM 1529 C ILE A 223 -2.364 22.089 37.789 1.00 55.43 C ANISOU 1529 C ILE A 223 6940 8142 5980 -570 -2091 -1332 C ATOM 1530 O ILE A 223 -2.516 21.210 36.941 1.00 56.91 O ANISOU 1530 O ILE A 223 7248 8356 6019 -636 -2177 -1476 O ATOM 1531 CB ILE A 223 -1.238 21.263 39.984 1.00 52.14 C ANISOU 1531 CB ILE A 223 6626 7379 5808 -729 -1714 -1268 C ATOM 1532 CG1 ILE A 223 -2.220 21.900 40.992 1.00 52.49 C ANISOU 1532 CG1 ILE A 223 6396 7485 6061 -802 -1723 -1271 C ATOM 1533 CG2 ILE A 223 0.121 20.968 40.621 1.00 51.03 C ANISOU 1533 CG2 ILE A 223 6670 7044 5675 -679 -1513 -1162 C ATOM 1534 CD1 ILE A 223 -3.623 21.309 40.973 1.00 61.78 C ANISOU 1534 CD1 ILE A 223 7403 8765 7306 -1005 -1837 -1474 C ATOM 1535 N SER A 224 -3.245 23.091 37.980 1.00 52.01 N ANISOU 1535 N SER A 224 6262 7845 5654 -514 -2205 -1297 N ATOM 1536 CA SER A 224 -4.496 23.226 37.232 1.00 54.56 C ANISOU 1536 CA SER A 224 6417 8376 5939 -524 -2450 -1427 C ATOM 1537 C SER A 224 -4.288 23.630 35.768 1.00 60.37 C ANISOU 1537 C SER A 224 7288 9233 6417 -339 -2616 -1374 C ATOM 1538 O SER A 224 -4.983 23.108 34.894 1.00 62.30 O ANISOU 1538 O SER A 224 7525 9607 6537 -390 -2805 -1536 O ATOM 1539 CB SER A 224 -5.451 24.189 37.930 1.00 58.31 C ANISOU 1539 CB SER A 224 6584 8955 6616 -493 -2513 -1406 C ATOM 1540 OG SER A 224 -5.034 25.537 37.791 1.00 67.55 O ANISOU 1540 OG SER A 224 7753 10142 7770 -252 -2528 -1196 O ATOM 1541 N LYS A 225 -3.332 24.543 35.498 1.00 55.93 N ANISOU 1541 N LYS A 225 6856 8629 5766 -135 -2545 -1151 N ATOM 1542 CA LYS A 225 -3.017 24.997 34.136 1.00 57.10 C ANISOU 1542 CA LYS A 225 7170 8879 5648 46 -2666 -1065 C ATOM 1543 C LYS A 225 -2.054 24.054 33.389 1.00 60.25 C ANISOU 1543 C LYS A 225 7858 9210 5825 25 -2575 -1107 C ATOM 1544 O LYS A 225 -1.661 24.357 32.262 1.00 61.17 O ANISOU 1544 O LYS A 225 8144 9403 5694 167 -2637 -1033 O ATOM 1545 CB LYS A 225 -2.492 26.443 34.143 1.00 58.72 C ANISOU 1545 CB LYS A 225 7386 9067 5860 259 -2625 -806 C ATOM 1546 CG LYS A 225 -3.549 27.468 33.749 1.00 74.04 C ANISOU 1546 CG LYS A 225 9156 11169 7807 399 -2863 -769 C ATOM 1547 CD LYS A 225 -3.087 28.892 34.024 1.00 80.46 C ANISOU 1547 CD LYS A 225 9968 11914 8688 582 -2798 -519 C ATOM 1548 CE LYS A 225 -3.985 29.911 33.363 1.00 88.19 C ANISOU 1548 CE LYS A 225 10856 13040 9612 770 -3050 -457 C ATOM 1549 NZ LYS A 225 -3.548 31.299 33.659 1.00 93.99 N ANISOU 1549 NZ LYS A 225 11611 13676 10426 942 -2982 -215 N ATOM 1550 N LEU A 226 -1.692 22.940 34.017 1.00 54.99 N ANISOU 1550 N LEU A 226 7255 8400 5239 -142 -2426 -1223 N ATOM 1551 CA LEU A 226 -0.785 21.976 33.407 1.00 54.71 C ANISOU 1551 CA LEU A 226 7487 8282 5019 -155 -2330 -1284 C ATOM 1552 C LEU A 226 -1.394 20.578 33.390 1.00 59.70 C ANISOU 1552 C LEU A 226 8146 8880 5657 -366 -2388 -1547 C ATOM 1553 O LEU A 226 -2.615 20.423 33.393 1.00 60.65 O ANISOU 1553 O LEU A 226 8089 9109 5847 -484 -2562 -1693 O ATOM 1554 CB LEU A 226 0.554 21.957 34.147 1.00 52.13 C ANISOU 1554 CB LEU A 226 7271 7769 4769 -117 -2064 -1149 C ATOM 1555 CG LEU A 226 1.672 21.132 33.506 1.00 57.16 C ANISOU 1555 CG LEU A 226 8176 8326 5217 -76 -1940 -1184 C ATOM 1556 CD1 LEU A 226 2.290 21.881 32.336 1.00 58.44 C ANISOU 1556 CD1 LEU A 226 8471 8600 5134 116 -1949 -1047 C ATOM 1557 CD2 LEU A 226 2.731 20.770 34.536 1.00 57.01 C ANISOU 1557 CD2 LEU A 226 8210 8108 5343 -94 -1704 -1125 C ATOM 1558 N ASP A1010 1.451 30.266 18.499 1.00 71.24 N ANISOU 1558 N ASP A1010 8958 11688 6420 1545 673 139 N ATOM 1559 CA ASP A1010 1.921 30.384 17.122 1.00 70.81 C ANISOU 1559 CA ASP A1010 8847 11679 6379 1531 646 105 C ATOM 1560 C ASP A1010 0.766 30.460 16.119 1.00 73.78 C ANISOU 1560 C ASP A1010 9193 12018 6820 1505 665 203 C ATOM 1561 O ASP A1010 0.676 31.438 15.373 1.00 73.28 O ANISOU 1561 O ASP A1010 9098 11963 6782 1479 723 211 O ATOM 1562 CB ASP A1010 2.881 29.235 16.761 1.00 73.04 C ANISOU 1562 CB ASP A1010 9129 12009 6614 1580 537 35 C ATOM 1563 CG ASP A1010 4.256 29.340 17.391 1.00 86.30 C ANISOU 1563 CG ASP A1010 10794 13777 8219 1612 512 -77 C ATOM 1564 OD1 ASP A1010 4.983 30.305 17.070 1.00 87.20 O ANISOU 1564 OD1 ASP A1010 10856 13960 8318 1566 554 -147 O ATOM 1565 OD2 ASP A1010 4.623 28.433 18.169 1.00 93.98 O ANISOU 1565 OD2 ASP A1010 11810 14760 9138 1683 449 -98 O ATOM 1566 N GLU A1011 -0.109 29.437 16.098 1.00 69.92 N ANISOU 1566 N GLU A1011 8723 11496 6347 1508 619 274 N ATOM 1567 CA GLU A1011 -1.246 29.378 15.175 1.00 69.74 C ANISOU 1567 CA GLU A1011 8657 11467 6373 1472 624 369 C ATOM 1568 C GLU A1011 -2.568 29.808 15.835 1.00 73.18 C ANISOU 1568 C GLU A1011 9077 11884 6844 1463 700 472 C ATOM 1569 O GLU A1011 -3.488 30.236 15.135 1.00 72.78 O ANISOU 1569 O GLU A1011 8964 11858 6833 1449 731 553 O ATOM 1570 CB GLU A1011 -1.372 27.990 14.513 1.00 71.43 C ANISOU 1570 CB GLU A1011 8899 11675 6566 1451 530 379 C ATOM 1571 CG GLU A1011 -0.091 27.429 13.887 1.00 84.14 C ANISOU 1571 CG GLU A1011 10533 13302 8133 1480 460 283 C ATOM 1572 CD GLU A1011 0.506 28.142 12.682 1.00105.23 C ANISOU 1572 CD GLU A1011 13145 16013 10823 1466 466 241 C ATOM 1573 OE1 GLU A1011 1.754 28.234 12.613 1.00 95.16 O ANISOU 1573 OE1 GLU A1011 11868 14775 9515 1499 448 142 O ATOM 1574 OE2 GLU A1011 -0.263 28.563 11.786 1.00 99.56 O ANISOU 1574 OE2 GLU A1011 12384 15299 10146 1423 486 307 O ATOM 1575 N GLY A1012 -2.644 29.683 17.163 1.00 69.61 N ANISOU 1575 N GLY A1012 8679 11397 6374 1479 728 468 N ATOM 1576 CA GLY A1012 -3.800 30.079 17.965 1.00 69.63 C ANISOU 1576 CA GLY A1012 8674 11378 6403 1477 811 556 C ATOM 1577 C GLY A1012 -4.955 29.096 17.999 1.00 73.56 C ANISOU 1577 C GLY A1012 9160 11881 6907 1433 783 634 C ATOM 1578 O GLY A1012 -5.238 28.430 17.000 1.00 73.43 O ANISOU 1578 O GLY A1012 9110 11899 6890 1392 720 655 O ATOM 1579 N LEU A1013 -5.647 29.025 19.157 1.00 69.91 N ANISOU 1579 N LEU A1013 8731 11389 6444 1429 838 674 N ATOM 1580 CA LEU A1013 -6.800 28.152 19.396 1.00 70.01 C ANISOU 1580 CA LEU A1013 8738 11413 6451 1368 832 742 C ATOM 1581 C LEU A1013 -8.077 28.972 19.631 1.00 74.39 C ANISOU 1581 C LEU A1013 9199 12015 7052 1375 935 845 C ATOM 1582 O LEU A1013 -8.092 29.865 20.481 1.00 74.10 O ANISOU 1582 O LEU A1013 9182 11943 7030 1428 1027 853 O ATOM 1583 CB LEU A1013 -6.521 27.202 20.582 1.00 70.13 C ANISOU 1583 CB LEU A1013 8886 11350 6410 1355 809 697 C ATOM 1584 CG LEU A1013 -7.694 26.359 21.109 1.00 75.45 C ANISOU 1584 CG LEU A1013 9586 12018 7062 1276 827 755 C ATOM 1585 CD1 LEU A1013 -7.776 25.017 20.406 1.00 75.75 C ANISOU 1585 CD1 LEU A1013 9680 12056 7045 1197 741 744 C ATOM 1586 CD2 LEU A1013 -7.578 26.151 22.601 1.00 78.47 C ANISOU 1586 CD2 LEU A1013 10089 12315 7410 1290 866 728 C ATOM 1587 N ARG A1014 -9.145 28.646 18.883 1.00 71.32 N ANISOU 1587 N ARG A1014 8709 11715 6675 1322 921 923 N ATOM 1588 CA ARG A1014 -10.451 29.304 18.954 1.00 71.81 C ANISOU 1588 CA ARG A1014 8650 11863 6772 1339 1008 1030 C ATOM 1589 C ARG A1014 -11.550 28.231 18.952 1.00 76.33 C ANISOU 1589 C ARG A1014 9175 12511 7317 1225 979 1081 C ATOM 1590 O ARG A1014 -11.693 27.501 17.965 1.00 75.99 O ANISOU 1590 O ARG A1014 9097 12527 7248 1144 897 1084 O ATOM 1591 CB ARG A1014 -10.615 30.255 17.758 1.00 72.03 C ANISOU 1591 CB ARG A1014 8567 11968 6833 1400 1020 1081 C ATOM 1592 CG ARG A1014 -11.308 31.572 18.069 1.00 82.05 C ANISOU 1592 CG ARG A1014 9772 13269 8135 1508 1147 1163 C ATOM 1593 CD ARG A1014 -10.415 32.741 17.693 1.00 90.31 C ANISOU 1593 CD ARG A1014 10874 14252 9189 1598 1190 1127 C ATOM 1594 NE ARG A1014 -11.180 33.927 17.302 1.00100.40 N ANISOU 1594 NE ARG A1014 12079 15586 10483 1707 1288 1224 N ATOM 1595 CZ ARG A1014 -11.594 34.871 18.141 1.00116.37 C ANISOU 1595 CZ ARG A1014 14134 17572 12510 1799 1424 1273 C ATOM 1596 NH1 ARG A1014 -12.280 35.914 17.693 1.00106.74 N ANISOU 1596 NH1 ARG A1014 12860 16402 11292 1920 1514 1367 N ATOM 1597 NH2 ARG A1014 -11.329 34.779 19.441 1.00100.83 N ANISOU 1597 NH2 ARG A1014 12265 15513 10535 1778 1475 1231 N ATOM 1598 N LEU A1015 -12.305 28.118 20.063 1.00 73.37 N ANISOU 1598 N LEU A1015 8809 12133 6937 1203 1052 1114 N ATOM 1599 CA LEU A1015 -13.359 27.109 20.218 1.00 74.02 C ANISOU 1599 CA LEU A1015 8858 12289 6979 1072 1042 1151 C ATOM 1600 C LEU A1015 -14.719 27.463 19.595 1.00 78.88 C ANISOU 1600 C LEU A1015 9265 13096 7611 1050 1077 1260 C ATOM 1601 O LEU A1015 -15.596 26.598 19.514 1.00 79.42 O ANISOU 1601 O LEU A1015 9283 13260 7633 913 1058 1287 O ATOM 1602 CB LEU A1015 -13.503 26.646 21.679 1.00 74.29 C ANISOU 1602 CB LEU A1015 9014 12231 6984 1036 1098 1124 C ATOM 1603 CG LEU A1015 -12.319 25.884 22.302 1.00 78.36 C ANISOU 1603 CG LEU A1015 9742 12581 7449 1031 1041 1019 C ATOM 1604 CD1 LEU A1015 -12.624 25.512 23.736 1.00 79.08 C ANISOU 1604 CD1 LEU A1015 9948 12591 7508 998 1104 1006 C ATOM 1605 CD2 LEU A1015 -11.971 24.620 21.518 1.00 80.60 C ANISOU 1605 CD2 LEU A1015 10106 12851 7665 934 932 974 C ATOM 1606 N LYS A1016 -14.880 28.716 19.132 1.00 75.51 N ANISOU 1606 N LYS A1016 8722 12733 7237 1183 1128 1321 N ATOM 1607 CA LYS A1016 -16.091 29.222 18.481 1.00 76.54 C ANISOU 1607 CA LYS A1016 8643 13060 7379 1211 1160 1434 C ATOM 1608 C LYS A1016 -15.735 29.731 17.064 1.00 80.06 C ANISOU 1608 C LYS A1016 9023 13558 7839 1270 1098 1451 C ATOM 1609 O LYS A1016 -14.701 30.386 16.904 1.00 78.56 O ANISOU 1609 O LYS A1016 8930 13246 7673 1363 1101 1402 O ATOM 1610 CB LYS A1016 -16.744 30.317 19.357 1.00 79.69 C ANISOU 1610 CB LYS A1016 8984 13481 7815 1348 1305 1506 C ATOM 1611 CG LYS A1016 -17.747 31.226 18.644 1.00 96.17 C ANISOU 1611 CG LYS A1016 10868 15756 9918 1463 1354 1628 C ATOM 1612 CD LYS A1016 -18.980 31.522 19.482 1.00108.23 C ANISOU 1612 CD LYS A1016 12276 17401 11447 1506 1472 1715 C ATOM 1613 CE LYS A1016 -20.197 30.734 19.042 1.00122.56 C ANISOU 1613 CE LYS A1016 13889 19459 13221 1377 1427 1775 C ATOM 1614 NZ LYS A1016 -20.642 31.068 17.657 1.00133.23 N ANISOU 1614 NZ LYS A1016 15060 21000 14559 1424 1364 1850 N ATOM 1615 N ILE A1017 -16.586 29.421 16.048 1.00 77.51 N ANISOU 1615 N ILE A1017 8539 13420 7490 1203 1041 1518 N ATOM 1616 CA ILE A1017 -16.402 29.812 14.637 1.00 77.25 C ANISOU 1616 CA ILE A1017 8437 13455 7459 1243 975 1544 C ATOM 1617 C ILE A1017 -15.987 31.270 14.442 1.00 80.38 C ANISOU 1617 C ILE A1017 8846 13796 7899 1445 1047 1571 C ATOM 1618 O ILE A1017 -16.554 32.164 15.076 1.00 80.85 O ANISOU 1618 O ILE A1017 8857 13884 7979 1575 1161 1638 O ATOM 1619 CB ILE A1017 -17.540 29.374 13.668 1.00 81.66 C ANISOU 1619 CB ILE A1017 8800 14253 7973 1147 913 1627 C ATOM 1620 CG1 ILE A1017 -18.952 29.601 14.271 1.00 83.63 C ANISOU 1620 CG1 ILE A1017 8867 14696 8214 1167 994 1728 C ATOM 1621 CG2 ILE A1017 -17.326 27.930 13.195 1.00 82.15 C ANISOU 1621 CG2 ILE A1017 8933 14306 7974 925 801 1562 C ATOM 1622 CD1 ILE A1017 -20.078 29.773 13.257 1.00 91.78 C ANISOU 1622 CD1 ILE A1017 9657 16005 9211 1164 957 1837 C ATOM 1623 N TYR A1018 -14.964 31.491 13.597 1.00 74.96 N ANISOU 1623 N TYR A1018 8245 13019 7218 1466 991 1513 N ATOM 1624 CA TYR A1018 -14.377 32.803 13.320 1.00 73.79 C ANISOU 1624 CA TYR A1018 8153 12791 7093 1625 1057 1514 C ATOM 1625 C TYR A1018 -13.934 32.931 11.863 1.00 76.42 C ANISOU 1625 C TYR A1018 8477 13145 7414 1621 976 1504 C ATOM 1626 O TYR A1018 -13.705 31.923 11.191 1.00 75.76 O ANISOU 1626 O TYR A1018 8391 13083 7310 1486 864 1463 O ATOM 1627 CB TYR A1018 -13.175 33.056 14.263 1.00 73.63 C ANISOU 1627 CB TYR A1018 8319 12570 7088 1646 1106 1409 C ATOM 1628 CG TYR A1018 -11.968 32.177 13.991 1.00 73.91 C ANISOU 1628 CG TYR A1018 8466 12506 7111 1538 1002 1287 C ATOM 1629 CD1 TYR A1018 -10.863 32.670 13.300 1.00 75.10 C ANISOU 1629 CD1 TYR A1018 8696 12576 7262 1569 983 1218 C ATOM 1630 CD2 TYR A1018 -11.924 30.860 14.437 1.00 74.34 C ANISOU 1630 CD2 TYR A1018 8556 12546 7144 1410 933 1241 C ATOM 1631 CE1 TYR A1018 -9.750 31.865 13.048 1.00 74.87 C ANISOU 1631 CE1 TYR A1018 8756 12473 7217 1486 893 1109 C ATOM 1632 CE2 TYR A1018 -10.828 30.041 14.171 1.00 74.30 C ANISOU 1632 CE2 TYR A1018 8660 12452 7117 1338 844 1138 C ATOM 1633 CZ TYR A1018 -9.741 30.548 13.480 1.00 80.44 C ANISOU 1633 CZ TYR A1018 9494 13169 7902 1383 823 1074 C ATOM 1634 OH TYR A1018 -8.657 29.743 13.233 1.00 79.84 O ANISOU 1634 OH TYR A1018 9513 13022 7801 1329 741 974 O ATOM 1635 N LYS A1019 -13.777 34.175 11.396 1.00 72.33 N ANISOU 1635 N LYS A1019 7980 12602 6901 1768 1042 1538 N ATOM 1636 CA LYS A1019 -13.297 34.471 10.054 1.00 71.58 C ANISOU 1636 CA LYS A1019 7901 12504 6791 1779 984 1525 C ATOM 1637 C LYS A1019 -11.784 34.686 10.122 1.00 73.49 C ANISOU 1637 C LYS A1019 8323 12560 7040 1760 990 1394 C ATOM 1638 O LYS A1019 -11.310 35.462 10.959 1.00 72.62 O ANISOU 1638 O LYS A1019 8317 12340 6936 1833 1094 1360 O ATOM 1639 CB LYS A1019 -13.999 35.713 9.483 1.00 75.24 C ANISOU 1639 CB LYS A1019 8304 13046 7238 1954 1059 1637 C ATOM 1640 CG LYS A1019 -15.388 35.438 8.923 1.00 90.13 C ANISOU 1640 CG LYS A1019 9978 15167 9101 1965 1012 1764 C ATOM 1641 CD LYS A1019 -15.962 36.684 8.257 1.00 99.83 C ANISOU 1641 CD LYS A1019 11161 16469 10300 2167 1079 1874 C ATOM 1642 CE LYS A1019 -17.296 36.433 7.593 1.00111.68 C ANISOU 1642 CE LYS A1019 12431 18237 11766 2186 1019 2002 C ATOM 1643 NZ LYS A1019 -18.390 36.232 8.583 1.00121.47 N ANISOU 1643 NZ LYS A1019 13521 19622 13010 2210 1075 2077 N ATOM 1644 N ASP A1020 -11.035 34.052 9.223 1.00 69.22 N ANISOU 1644 N ASP A1020 7817 11993 6491 1662 887 1321 N ATOM 1645 CA ASP A1020 -9.577 34.199 9.190 1.00 67.98 C ANISOU 1645 CA ASP A1020 7805 11692 6333 1639 886 1193 C ATOM 1646 C ASP A1020 -9.110 35.495 8.514 1.00 71.78 C ANISOU 1646 C ASP A1020 8358 12116 6799 1732 957 1185 C ATOM 1647 O ASP A1020 -9.923 36.349 8.162 1.00 72.51 O ANISOU 1647 O ASP A1020 8407 12263 6879 1841 1017 1286 O ATOM 1648 CB ASP A1020 -8.935 32.991 8.502 1.00 69.29 C ANISOU 1648 CB ASP A1020 7989 11850 6489 1508 759 1117 C ATOM 1649 CG ASP A1020 -9.496 32.743 7.116 1.00 80.88 C ANISOU 1649 CG ASP A1020 9375 13417 7940 1469 682 1178 C ATOM 1650 OD1 ASP A1020 -10.137 33.660 6.560 1.00 82.30 O ANISOU 1650 OD1 ASP A1020 9497 13661 8114 1560 723 1264 O ATOM 1651 OD2 ASP A1020 -9.296 31.632 6.582 1.00 86.76 O ANISOU 1651 OD2 ASP A1020 10125 14173 8667 1350 582 1142 O ATOM 1652 N THR A1021 -7.795 35.631 8.340 1.00 67.05 N ANISOU 1652 N THR A1021 7873 11412 6189 1691 953 1064 N ATOM 1653 CA THR A1021 -7.200 36.829 7.719 1.00 66.75 C ANISOU 1653 CA THR A1021 7934 11304 6122 1748 1029 1033 C ATOM 1654 C THR A1021 -7.963 37.254 6.438 1.00 71.68 C ANISOU 1654 C THR A1021 8505 11999 6730 1808 1012 1131 C ATOM 1655 O THR A1021 -8.111 38.450 6.182 1.00 71.83 O ANISOU 1655 O THR A1021 8594 11980 6716 1914 1112 1171 O ATOM 1656 CB THR A1021 -5.660 36.712 7.693 1.00 72.78 C ANISOU 1656 CB THR A1021 8801 11980 6872 1663 1012 878 C ATOM 1657 OG1 THR A1021 -5.221 35.994 8.846 1.00 72.25 O ANISOU 1657 OG1 THR A1021 8739 11894 6818 1615 991 815 O ATOM 1658 CG2 THR A1021 -4.962 38.068 7.650 1.00 71.02 C ANISOU 1658 CG2 THR A1021 8713 11666 6605 1701 1135 824 C ATOM 1659 N GLU A1022 -8.474 36.276 5.666 1.00 68.68 N ANISOU 1659 N GLU A1022 8014 11721 6360 1740 890 1172 N ATOM 1660 CA GLU A1022 -9.233 36.519 4.436 1.00 69.40 C ANISOU 1660 CA GLU A1022 8036 11906 6428 1781 851 1267 C ATOM 1661 C GLU A1022 -10.775 36.506 4.490 1.00 74.74 C ANISOU 1661 C GLU A1022 8552 12746 7098 1854 845 1420 C ATOM 1662 O GLU A1022 -11.428 36.882 3.516 1.00 75.06 O ANISOU 1662 O GLU A1022 8532 12880 7108 1916 822 1508 O ATOM 1663 CB GLU A1022 -8.634 35.670 3.291 1.00 70.22 C ANISOU 1663 CB GLU A1022 8148 12009 6525 1652 730 1202 C ATOM 1664 CG GLU A1022 -8.200 34.262 3.668 1.00 80.09 C ANISOU 1664 CG GLU A1022 9385 13251 7794 1513 640 1128 C ATOM 1665 CD GLU A1022 -7.278 33.573 2.678 1.00 99.38 C ANISOU 1665 CD GLU A1022 11888 15647 10225 1406 555 1037 C ATOM 1666 OE1 GLU A1022 -7.472 33.740 1.451 1.00 93.94 O ANISOU 1666 OE1 GLU A1022 11189 14992 9513 1393 515 1072 O ATOM 1667 OE2 GLU A1022 -6.379 32.831 3.137 1.00 90.88 O ANISOU 1667 OE2 GLU A1022 10870 14504 9156 1341 529 936 O ATOM 1668 N GLY A1023 -11.332 36.143 5.644 1.00 71.88 N ANISOU 1668 N GLY A1023 8124 12427 6760 1854 873 1451 N ATOM 1669 CA GLY A1023 -12.773 36.146 5.872 1.00 73.21 C ANISOU 1669 CA GLY A1023 8128 12767 6921 1921 883 1588 C ATOM 1670 C GLY A1023 -13.500 34.839 5.645 1.00 77.76 C ANISOU 1670 C GLY A1023 8555 13498 7493 1775 764 1621 C ATOM 1671 O GLY A1023 -14.717 34.847 5.433 1.00 78.55 O ANISOU 1671 O GLY A1023 8490 13787 7569 1813 750 1738 O ATOM 1672 N TYR A1024 -12.774 33.709 5.702 1.00 73.64 N ANISOU 1672 N TYR A1024 8094 12907 6980 1608 683 1518 N ATOM 1673 CA TYR A1024 -13.365 32.379 5.534 1.00 74.05 C ANISOU 1673 CA TYR A1024 8053 13073 7008 1441 580 1533 C ATOM 1674 C TYR A1024 -13.659 31.761 6.897 1.00 78.13 C ANISOU 1674 C TYR A1024 8562 13583 7539 1390 615 1519 C ATOM 1675 O TYR A1024 -12.886 31.966 7.836 1.00 77.02 O ANISOU 1675 O TYR A1024 8540 13295 7429 1431 677 1445 O ATOM 1676 CB TYR A1024 -12.445 31.453 4.717 1.00 74.55 C ANISOU 1676 CB TYR A1024 8216 13054 7055 1295 479 1437 C ATOM 1677 CG TYR A1024 -12.066 31.951 3.337 1.00 76.58 C ANISOU 1677 CG TYR A1024 8500 13303 7296 1321 441 1437 C ATOM 1678 CD1 TYR A1024 -10.767 31.811 2.857 1.00 77.50 C ANISOU 1678 CD1 TYR A1024 8761 13268 7418 1282 417 1323 C ATOM 1679 CD2 TYR A1024 -13.014 32.520 2.488 1.00 78.59 C ANISOU 1679 CD2 TYR A1024 8632 13711 7520 1383 425 1551 C ATOM 1680 CE1 TYR A1024 -10.413 32.249 1.583 1.00 78.42 C ANISOU 1680 CE1 TYR A1024 8912 13369 7516 1294 387 1318 C ATOM 1681 CE2 TYR A1024 -12.674 32.961 1.211 1.00 79.59 C ANISOU 1681 CE2 TYR A1024 8798 13819 7622 1404 389 1551 C ATOM 1682 CZ TYR A1024 -11.372 32.814 0.758 1.00 86.51 C ANISOU 1682 CZ TYR A1024 9831 14528 8509 1351 372 1432 C ATOM 1683 OH TYR A1024 -11.028 33.251 -0.501 1.00 88.24 O ANISOU 1683 OH TYR A1024 10101 14724 8704 1363 343 1427 O ATOM 1684 N TYR A1025 -14.770 31.009 7.011 1.00 75.84 N ANISOU 1684 N TYR A1025 8139 13459 7219 1291 577 1586 N ATOM 1685 CA TYR A1025 -15.170 30.367 8.266 1.00 75.84 C ANISOU 1685 CA TYR A1025 8133 13463 7220 1225 613 1576 C ATOM 1686 C TYR A1025 -14.168 29.302 8.713 1.00 79.29 C ANISOU 1686 C TYR A1025 8743 13732 7650 1101 571 1453 C ATOM 1687 O TYR A1025 -13.838 28.400 7.946 1.00 78.38 O ANISOU 1687 O TYR A1025 8681 13604 7496 969 481 1410 O ATOM 1688 CB TYR A1025 -16.608 29.820 8.193 1.00 78.30 C ANISOU 1688 CB TYR A1025 8256 14011 7485 1126 586 1672 C ATOM 1689 CG TYR A1025 -17.668 30.899 8.110 1.00 80.91 C ANISOU 1689 CG TYR A1025 8400 14522 7820 1289 650 1800 C ATOM 1690 CD1 TYR A1025 -17.973 31.691 9.214 1.00 83.00 C ANISOU 1690 CD1 TYR A1025 8650 14766 8122 1441 774 1838 C ATOM 1691 CD2 TYR A1025 -18.388 31.107 6.938 1.00 82.81 C ANISOU 1691 CD2 TYR A1025 8485 14961 8016 1299 589 1889 C ATOM 1692 CE1 TYR A1025 -18.952 32.683 9.146 1.00 84.91 C ANISOU 1692 CE1 TYR A1025 8731 15172 8358 1617 843 1962 C ATOM 1693 CE2 TYR A1025 -19.375 32.090 6.861 1.00 85.15 C ANISOU 1693 CE2 TYR A1025 8608 15440 8306 1477 647 2015 C ATOM 1694 CZ TYR A1025 -19.654 32.876 7.968 1.00 92.72 C ANISOU 1694 CZ TYR A1025 9560 16368 9302 1644 779 2053 C ATOM 1695 OH TYR A1025 -20.620 33.849 7.894 1.00 95.02 O ANISOU 1695 OH TYR A1025 9691 16835 9577 1844 847 2182 O ATOM 1696 N THR A1026 -13.637 29.465 9.932 1.00 76.26 N ANISOU 1696 N THR A1026 8461 13217 7299 1159 641 1399 N ATOM 1697 CA THR A1026 -12.627 28.593 10.540 1.00 75.66 C ANISOU 1697 CA THR A1026 8554 12980 7212 1088 614 1286 C ATOM 1698 C THR A1026 -12.955 28.285 12.020 1.00 80.62 C ANISOU 1698 C THR A1026 9217 13574 7842 1077 677 1280 C ATOM 1699 O THR A1026 -13.720 29.030 12.638 1.00 80.67 O ANISOU 1699 O THR A1026 9131 13645 7874 1158 762 1350 O ATOM 1700 CB THR A1026 -11.222 29.212 10.364 1.00 83.64 C ANISOU 1700 CB THR A1026 9682 13844 8252 1182 622 1197 C ATOM 1701 OG1 THR A1026 -11.295 30.621 10.581 1.00 84.69 O ANISOU 1701 OG1 THR A1026 9780 13975 8425 1331 717 1237 O ATOM 1702 CG2 THR A1026 -10.626 28.953 8.986 1.00 81.62 C ANISOU 1702 CG2 THR A1026 9453 13580 7978 1135 538 1162 C ATOM 1703 N ILE A1027 -12.399 27.170 12.567 1.00 77.53 N ANISOU 1703 N ILE A1027 8968 13077 7414 983 639 1199 N ATOM 1704 CA ILE A1027 -12.549 26.721 13.966 1.00 77.72 C ANISOU 1704 CA ILE A1027 9068 13038 7426 961 689 1176 C ATOM 1705 C ILE A1027 -11.364 25.841 14.409 1.00 80.78 C ANISOU 1705 C ILE A1027 9654 13261 7777 937 644 1065 C ATOM 1706 O ILE A1027 -10.826 25.080 13.602 1.00 80.07 O ANISOU 1706 O ILE A1027 9638 13139 7647 874 566 1021 O ATOM 1707 CB ILE A1027 -13.953 26.116 14.309 1.00 82.17 C ANISOU 1707 CB ILE A1027 9538 13733 7949 837 709 1248 C ATOM 1708 CG1 ILE A1027 -14.287 26.275 15.817 1.00 82.71 C ANISOU 1708 CG1 ILE A1027 9638 13756 8032 873 803 1251 C ATOM 1709 CG2 ILE A1027 -14.101 24.664 13.825 1.00 83.38 C ANISOU 1709 CG2 ILE A1027 9769 13895 8015 644 629 1217 C ATOM 1710 CD1 ILE A1027 -15.752 26.098 16.196 1.00 91.05 C ANISOU 1710 CD1 ILE A1027 10556 14973 9066 789 854 1334 C ATOM 1711 N GLY A1028 -10.973 25.971 15.678 1.00 77.00 N ANISOU 1711 N GLY A1028 9263 12685 7307 997 697 1026 N ATOM 1712 CA GLY A1028 -9.857 25.233 16.259 1.00 76.31 C ANISOU 1712 CA GLY A1028 9357 12458 7179 1008 660 927 C ATOM 1713 C GLY A1028 -8.518 25.797 15.835 1.00 79.59 C ANISOU 1713 C GLY A1028 9806 12815 7618 1110 632 856 C ATOM 1714 O GLY A1028 -8.409 26.998 15.559 1.00 78.93 O ANISOU 1714 O GLY A1028 9635 12765 7589 1188 676 875 O ATOM 1715 N ILE A1029 -7.490 24.936 15.770 1.00 76.07 N ANISOU 1715 N ILE A1029 9493 12288 7122 1112 566 773 N ATOM 1716 CA ILE A1029 -6.149 25.361 15.366 1.00 75.31 C ANISOU 1716 CA ILE A1029 9419 12159 7037 1200 536 694 C ATOM 1717 C ILE A1029 -6.033 25.414 13.828 1.00 79.94 C ANISOU 1717 C ILE A1029 9945 12794 7633 1169 487 701 C ATOM 1718 O ILE A1029 -5.575 24.458 13.189 1.00 79.56 O ANISOU 1718 O ILE A1029 9978 12716 7536 1132 421 663 O ATOM 1719 CB ILE A1029 -4.999 24.589 16.096 1.00 78.06 C ANISOU 1719 CB ILE A1029 9917 12418 7324 1254 496 601 C ATOM 1720 CG1 ILE A1029 -5.241 24.530 17.623 1.00 78.55 C ANISOU 1720 CG1 ILE A1029 10046 12431 7370 1275 544 603 C ATOM 1721 CG2 ILE A1029 -3.622 25.208 15.793 1.00 77.99 C ANISOU 1721 CG2 ILE A1029 9894 12413 7327 1345 477 517 C ATOM 1722 CD1 ILE A1029 -4.838 23.217 18.285 1.00 85.05 C ANISOU 1722 CD1 ILE A1029 11045 13169 8103 1279 499 557 C ATOM 1723 N GLY A1030 -6.504 26.534 13.273 1.00 77.04 N ANISOU 1723 N GLY A1030 9452 12496 7323 1189 529 756 N ATOM 1724 CA GLY A1030 -6.482 26.871 11.850 1.00 77.04 C ANISOU 1724 CA GLY A1030 9385 12548 7339 1172 497 773 C ATOM 1725 C GLY A1030 -7.096 25.894 10.867 1.00 81.87 C ANISOU 1725 C GLY A1030 9992 13203 7911 1057 429 812 C ATOM 1726 O GLY A1030 -6.567 25.742 9.761 1.00 81.22 O ANISOU 1726 O GLY A1030 9925 13116 7818 1039 379 782 O ATOM 1727 N HIS A1031 -8.219 25.239 11.242 1.00 79.47 N ANISOU 1727 N HIS A1031 9671 12946 7577 965 432 875 N ATOM 1728 CA HIS A1031 -8.932 24.290 10.373 1.00 80.13 C ANISOU 1728 CA HIS A1031 9754 13087 7605 820 375 915 C ATOM 1729 C HIS A1031 -9.967 25.045 9.542 1.00 84.04 C ANISOU 1729 C HIS A1031 10070 13731 8129 797 381 1013 C ATOM 1730 O HIS A1031 -10.805 25.753 10.106 1.00 83.83 O ANISOU 1730 O HIS A1031 9928 13786 8138 839 441 1081 O ATOM 1731 CB HIS A1031 -9.595 23.170 11.200 1.00 81.76 C ANISOU 1731 CB HIS A1031 10044 13277 7743 709 381 925 C ATOM 1732 CG HIS A1031 -10.272 22.106 10.386 1.00 86.24 C ANISOU 1732 CG HIS A1031 10645 13895 8227 530 332 953 C ATOM 1733 ND1 HIS A1031 -9.706 20.854 10.221 1.00 88.14 N ANISOU 1733 ND1 HIS A1031 11087 14024 8379 458 293 892 N ATOM 1734 CD2 HIS A1031 -11.468 22.129 9.754 1.00 88.93 C ANISOU 1734 CD2 HIS A1031 10849 14391 8550 409 321 1036 C ATOM 1735 CE1 HIS A1031 -10.560 20.163 9.481 1.00 88.48 C ANISOU 1735 CE1 HIS A1031 11125 14143 8349 278 265 935 C ATOM 1736 NE2 HIS A1031 -11.635 20.890 9.174 1.00 89.38 N ANISOU 1736 NE2 HIS A1031 11027 14431 8503 237 275 1021 N ATOM 1737 N LEU A1032 -9.910 24.886 8.205 1.00 80.47 N ANISOU 1737 N LEU A1032 9601 13318 7657 739 320 1021 N ATOM 1738 CA LEU A1032 -10.818 25.551 7.273 1.00 80.86 C ANISOU 1738 CA LEU A1032 9488 13517 7720 724 310 1114 C ATOM 1739 C LEU A1032 -12.118 24.911 6.786 1.00 86.63 C ANISOU 1739 C LEU A1032 10121 14405 8388 564 272 1196 C ATOM 1740 O LEU A1032 -12.095 24.078 5.878 1.00 86.74 O ANISOU 1740 O LEU A1032 10193 14426 8338 429 205 1183 O ATOM 1741 CB LEU A1032 -10.120 25.817 5.924 1.00 80.36 C ANISOU 1741 CB LEU A1032 9445 13428 7659 737 260 1086 C ATOM 1742 CG LEU A1032 -10.858 26.720 4.925 1.00 85.25 C ANISOU 1742 CG LEU A1032 9913 14184 8294 765 252 1176 C ATOM 1743 CD1 LEU A1032 -10.484 28.181 5.118 1.00 84.84 C ANISOU 1743 CD1 LEU A1032 9825 14102 8308 945 325 1181 C ATOM 1744 CD2 LEU A1032 -10.561 26.299 3.497 1.00 87.22 C ANISOU 1744 CD2 LEU A1032 10203 14434 8503 676 174 1161 C ATOM 1745 N LEU A1033 -13.245 25.334 7.350 1.00 84.20 N ANISOU 1745 N LEU A1033 9664 14235 8092 575 318 1279 N ATOM 1746 CA LEU A1033 -14.546 24.829 6.922 1.00 85.42 C ANISOU 1746 CA LEU A1033 9689 14586 8181 419 285 1360 C ATOM 1747 C LEU A1033 -15.027 24.938 5.473 1.00 89.72 C ANISOU 1747 C LEU A1033 10123 15277 8688 353 214 1420 C ATOM 1748 O LEU A1033 -15.232 23.930 4.798 1.00 89.77 O ANISOU 1748 O LEU A1033 10178 15319 8610 162 149 1410 O ATOM 1749 CB LEU A1033 -15.606 25.432 7.847 1.00 86.34 C ANISOU 1749 CB LEU A1033 9643 14838 8325 481 361 1439 C ATOM 1750 CG LEU A1033 -15.609 24.931 9.293 1.00 91.10 C ANISOU 1750 CG LEU A1033 10338 15350 8925 456 423 1397 C ATOM 1751 CD1 LEU A1033 -14.360 25.398 10.026 1.00 89.98 C ANISOU 1751 CD1 LEU A1033 10345 14996 8849 613 465 1318 C ATOM 1752 CD2 LEU A1033 -16.864 25.390 10.018 1.00 94.79 C ANISOU 1752 CD2 LEU A1033 10623 15990 9402 478 494 1486 C ATOM 1753 N THR A1034 -15.206 26.172 5.009 1.00 86.34 N ANISOU 1753 N THR A1034 9564 14928 8313 511 230 1484 N ATOM 1754 CA THR A1034 -15.706 26.445 3.661 1.00 87.04 C ANISOU 1754 CA THR A1034 9536 15169 8366 481 164 1553 C ATOM 1755 C THR A1034 -15.538 27.938 3.343 1.00 90.57 C ANISOU 1755 C THR A1034 9915 15620 8878 712 207 1600 C ATOM 1756 O THR A1034 -15.638 28.782 4.242 1.00 89.92 O ANISOU 1756 O THR A1034 9796 15518 8850 872 297 1623 O ATOM 1757 CB THR A1034 -17.092 25.870 3.272 1.00 97.97 C ANISOU 1757 CB THR A1034 10748 16813 9663 309 115 1640 C ATOM 1758 OG1 THR A1034 -17.237 25.915 1.850 1.00 98.74 O ANISOU 1758 OG1 THR A1034 10795 17009 9713 253 31 1678 O ATOM 1759 CG2 THR A1034 -18.258 26.593 3.944 1.00 97.88 C ANISOU 1759 CG2 THR A1034 10516 17007 9669 411 176 1743 C ATOM 1760 N LYS A1035 -15.294 28.253 2.059 1.00 87.02 N ANISOU 1760 N LYS A1035 9467 15186 8412 723 150 1613 N ATOM 1761 CA LYS A1035 -15.125 29.618 1.557 1.00 86.66 C ANISOU 1761 CA LYS A1035 9389 15133 8403 925 187 1655 C ATOM 1762 C LYS A1035 -16.480 30.267 1.222 1.00 92.80 C ANISOU 1762 C LYS A1035 9946 16167 9147 1007 186 1799 C ATOM 1763 O LYS A1035 -16.523 31.417 0.777 1.00 92.82 O ANISOU 1763 O LYS A1035 9921 16185 9162 1191 221 1855 O ATOM 1764 CB LYS A1035 -14.147 29.653 0.368 1.00 87.97 C ANISOU 1764 CB LYS A1035 9684 15178 8562 902 134 1592 C ATOM 1765 CG LYS A1035 -12.726 29.266 0.761 1.00 97.84 C ANISOU 1765 CG LYS A1035 11135 16190 9850 880 154 1454 C ATOM 1766 CD LYS A1035 -11.742 29.373 -0.382 1.00107.57 C ANISOU 1766 CD LYS A1035 12485 17309 11077 867 115 1388 C ATOM 1767 CE LYS A1035 -10.357 29.015 0.095 1.00117.63 C ANISOU 1767 CE LYS A1035 13929 18382 12384 863 141 1254 C ATOM 1768 NZ LYS A1035 -9.325 29.275 -0.938 1.00126.40 N ANISOU 1768 NZ LYS A1035 15146 19385 13495 870 124 1183 N ATOM 1769 N SER A1036 -17.587 29.531 1.475 1.00 90.81 N ANISOU 1769 N SER A1036 9540 16121 8843 874 152 1858 N ATOM 1770 CA SER A1036 -18.963 29.980 1.274 1.00 92.56 C ANISOU 1770 CA SER A1036 9514 16633 9019 935 146 1995 C ATOM 1771 C SER A1036 -19.330 30.983 2.383 1.00 96.67 C ANISOU 1771 C SER A1036 9969 17165 9596 1161 271 2049 C ATOM 1772 O SER A1036 -19.191 30.645 3.563 1.00 95.78 O ANISOU 1772 O SER A1036 9910 16962 9520 1130 334 1999 O ATOM 1773 CB SER A1036 -19.920 28.789 1.295 1.00 97.42 C ANISOU 1773 CB SER A1036 10002 17461 9554 685 80 2019 C ATOM 1774 OG SER A1036 -21.277 29.196 1.240 1.00108.35 O ANISOU 1774 OG SER A1036 11117 19161 10891 743 80 2148 O ATOM 1775 N PRO A1037 -19.809 32.205 2.042 1.00 94.09 N ANISOU 1775 N PRO A1037 9543 16941 9267 1394 315 2152 N ATOM 1776 CA PRO A1037 -20.148 33.190 3.091 1.00 94.35 C ANISOU 1776 CA PRO A1037 9539 16966 9342 1621 450 2207 C ATOM 1777 C PRO A1037 -21.372 32.847 3.952 1.00 99.91 C ANISOU 1777 C PRO A1037 10035 17900 10026 1590 483 2280 C ATOM 1778 O PRO A1037 -21.625 33.536 4.944 1.00 99.62 O ANISOU 1778 O PRO A1037 9984 17839 10026 1758 604 2315 O ATOM 1779 CB PRO A1037 -20.339 34.498 2.306 1.00 96.84 C ANISOU 1779 CB PRO A1037 9830 17330 9636 1873 481 2302 C ATOM 1780 CG PRO A1037 -19.752 34.233 0.940 1.00100.66 C ANISOU 1780 CG PRO A1037 10393 17767 10087 1772 369 2262 C ATOM 1781 CD PRO A1037 -20.008 32.785 0.702 1.00 96.34 C ANISOU 1781 CD PRO A1037 9772 17329 9503 1478 253 2224 C ATOM 1782 N SER A1038 -22.109 31.772 3.598 1.00 97.75 N ANISOU 1782 N SER A1038 9611 17844 9687 1361 385 2296 N ATOM 1783 CA SER A1038 -23.295 31.309 4.323 1.00 99.30 C ANISOU 1783 CA SER A1038 9597 18287 9846 1280 408 2354 C ATOM 1784 C SER A1038 -22.920 30.729 5.700 1.00102.41 C ANISOU 1784 C SER A1038 10120 18501 10289 1185 483 2262 C ATOM 1785 O SER A1038 -22.040 29.868 5.790 1.00100.37 O ANISOU 1785 O SER A1038 10058 18037 10042 1009 443 2145 O ATOM 1786 CB SER A1038 -24.068 30.293 3.488 1.00104.33 C ANISOU 1786 CB SER A1038 10068 19191 10379 1023 282 2380 C ATOM 1787 OG SER A1038 -25.286 29.919 4.112 1.00115.75 O ANISOU 1787 OG SER A1038 11286 20918 11776 939 307 2439 O ATOM 1788 N LEU A1039 -23.580 31.231 6.765 1.00100.14 N ANISOU 1788 N LEU A1039 9733 18289 10028 1317 596 2317 N ATOM 1789 CA LEU A1039 -23.363 30.853 8.166 1.00 99.35 C ANISOU 1789 CA LEU A1039 9741 18037 9972 1262 684 2248 C ATOM 1790 C LEU A1039 -23.691 29.391 8.468 1.00103.43 C ANISOU 1790 C LEU A1039 10248 18619 10430 946 628 2186 C ATOM 1791 O LEU A1039 -22.825 28.665 8.959 1.00101.25 O ANISOU 1791 O LEU A1039 10194 18103 10173 818 623 2072 O ATOM 1792 CB LEU A1039 -24.166 31.777 9.105 1.00100.62 C ANISOU 1792 CB LEU A1039 9770 18301 10159 1480 821 2340 C ATOM 1793 CG LEU A1039 -23.550 33.133 9.442 1.00104.55 C ANISOU 1793 CG LEU A1039 10406 18596 10723 1775 934 2358 C ATOM 1794 CD1 LEU A1039 -24.036 34.215 8.487 1.00106.01 C ANISOU 1794 CD1 LEU A1039 10463 18939 10877 2012 938 2481 C ATOM 1795 CD2 LEU A1039 -23.874 33.530 10.863 1.00107.02 C ANISOU 1795 CD2 LEU A1039 10729 18859 11074 1881 1082 2374 C ATOM 1796 N ASN A1040 -24.944 28.971 8.196 1.00102.39 N ANISOU 1796 N ASN A1040 9867 18821 10217 822 594 2261 N ATOM 1797 CA ASN A1040 -25.455 27.620 8.457 1.00103.15 C ANISOU 1797 CA ASN A1040 9938 19023 10230 500 555 2211 C ATOM 1798 C ASN A1040 -24.805 26.539 7.592 1.00106.87 C ANISOU 1798 C ASN A1040 10575 19388 10641 248 438 2125 C ATOM 1799 O ASN A1040 -24.597 25.422 8.074 1.00106.00 O ANISOU 1799 O ASN A1040 10618 19169 10488 16 434 2035 O ATOM 1800 CB ASN A1040 -26.984 27.578 8.334 1.00106.02 C ANISOU 1800 CB ASN A1040 9966 19806 10510 436 554 2317 C ATOM 1801 CG ASN A1040 -27.708 28.630 9.147 1.00127.34 C ANISOU 1801 CG ASN A1040 12488 22635 13258 699 678 2413 C ATOM 1802 OD1 ASN A1040 -28.427 29.477 8.603 1.00123.19 O ANISOU 1802 OD1 ASN A1040 11731 22361 12715 891 677 2533 O ATOM 1803 ND2 ASN A1040 -27.524 28.619 10.465 1.00118.04 N ANISOU 1803 ND2 ASN A1040 11428 21285 12137 727 791 2365 N ATOM 1804 N ALA A1041 -24.477 26.873 6.325 1.00103.85 N ANISOU 1804 N ALA A1041 10182 19026 10249 301 350 2151 N ATOM 1805 CA ALA A1041 -23.836 25.958 5.371 1.00103.27 C ANISOU 1805 CA ALA A1041 10270 18850 10119 87 242 2078 C ATOM 1806 C ALA A1041 -22.423 25.576 5.821 1.00105.49 C ANISOU 1806 C ALA A1041 10875 18745 10460 87 262 1951 C ATOM 1807 O ALA A1041 -21.984 24.452 5.572 1.00104.57 O ANISOU 1807 O ALA A1041 10932 18517 10281 -136 210 1869 O ATOM 1808 CB ALA A1041 -23.803 26.579 3.984 1.00104.28 C ANISOU 1808 CB ALA A1041 10310 19079 10233 182 158 2142 C ATOM 1809 N ALA A1042 -21.725 26.510 6.500 1.00101.34 N ANISOU 1809 N ALA A1042 10435 18026 10044 339 342 1936 N ATOM 1810 CA ALA A1042 -20.380 26.307 7.039 1.00 99.43 C ANISOU 1810 CA ALA A1042 10468 17449 9861 373 368 1821 C ATOM 1811 C ALA A1042 -20.438 25.430 8.288 1.00103.76 C ANISOU 1811 C ALA A1042 11124 17911 10390 243 421 1758 C ATOM 1812 O ALA A1042 -19.643 24.494 8.405 1.00102.30 O ANISOU 1812 O ALA A1042 11161 17532 10178 117 392 1660 O ATOM 1813 CB ALA A1042 -19.732 27.647 7.360 1.00 99.10 C ANISOU 1813 CB ALA A1042 10463 17269 9922 662 441 1831 C ATOM 1814 N LYS A1043 -21.397 25.714 9.204 1.00102.06 N ANISOU 1814 N LYS A1043 10757 17839 10180 277 501 1817 N ATOM 1815 CA LYS A1043 -21.617 24.958 10.442 1.00102.36 C ANISOU 1815 CA LYS A1043 10881 17817 10194 153 564 1767 C ATOM 1816 C LYS A1043 -21.883 23.485 10.125 1.00107.77 C ANISOU 1816 C LYS A1043 11649 18542 10756 -165 501 1716 C ATOM 1817 O LYS A1043 -21.167 22.623 10.636 1.00106.25 O ANISOU 1817 O LYS A1043 11706 18127 10538 -262 505 1620 O ATOM 1818 CB LYS A1043 -22.776 25.554 11.265 1.00106.18 C ANISOU 1818 CB LYS A1043 11147 18504 10693 232 660 1853 C ATOM 1819 CG LYS A1043 -22.483 26.912 11.896 1.00117.42 C ANISOU 1819 CG LYS A1043 12557 19834 12225 536 756 1892 C ATOM 1820 CD LYS A1043 -23.441 27.225 13.046 1.00127.46 C ANISOU 1820 CD LYS A1043 13697 21226 13507 587 872 1946 C ATOM 1821 CE LYS A1043 -24.746 27.858 12.617 1.00139.45 C ANISOU 1821 CE LYS A1043 14897 23088 14999 668 892 2077 C ATOM 1822 NZ LYS A1043 -25.649 28.085 13.775 1.00149.25 N ANISOU 1822 NZ LYS A1043 16018 24443 16247 711 1014 2123 N ATOM 1823 N SER A1044 -22.859 23.211 9.224 1.00106.88 N ANISOU 1823 N SER A1044 11343 18711 10557 -321 442 1779 N ATOM 1824 CA SER A1044 -23.248 21.870 8.762 1.00108.09 C ANISOU 1824 CA SER A1044 11561 18941 10569 -653 385 1740 C ATOM 1825 C SER A1044 -22.116 21.131 8.023 1.00111.17 C ANISOU 1825 C SER A1044 12224 19090 10925 -739 312 1654 C ATOM 1826 O SER A1044 -22.142 19.898 7.947 1.00111.18 O ANISOU 1826 O SER A1044 12393 19041 10808 -999 293 1594 O ATOM 1827 CB SER A1044 -24.512 21.935 7.906 1.00113.91 C ANISOU 1827 CB SER A1044 12000 20059 11220 -779 334 1835 C ATOM 1828 OG SER A1044 -24.397 22.889 6.861 1.00123.31 O ANISOU 1828 OG SER A1044 13051 21340 12462 -593 273 1907 O ATOM 1829 N GLU A1045 -21.125 21.883 7.493 1.00106.64 N ANISOU 1829 N GLU A1045 11707 18364 10446 -523 281 1647 N ATOM 1830 CA GLU A1045 -19.946 21.327 6.828 1.00105.41 C ANISOU 1830 CA GLU A1045 11801 17975 10276 -557 223 1565 C ATOM 1831 C GLU A1045 -18.924 20.854 7.880 1.00109.18 C ANISOU 1831 C GLU A1045 12548 18154 10780 -505 275 1464 C ATOM 1832 O GLU A1045 -18.085 20.001 7.575 1.00107.99 O ANISOU 1832 O GLU A1045 12638 17816 10579 -586 241 1386 O ATOM 1833 CB GLU A1045 -19.339 22.339 5.832 1.00105.65 C ANISOU 1833 CB GLU A1045 11771 17985 10387 -359 175 1594 C ATOM 1834 CG GLU A1045 -18.372 21.748 4.813 1.00113.12 C ANISOU 1834 CG GLU A1045 12915 18770 11296 -434 103 1528 C ATOM 1835 CD GLU A1045 -18.881 20.586 3.978 1.00129.67 C ANISOU 1835 CD GLU A1045 15060 20963 13247 -733 39 1525 C ATOM 1836 OE1 GLU A1045 -18.294 19.486 4.084 1.00117.96 O ANISOU 1836 OE1 GLU A1045 13834 19293 11692 -871 39 1441 O ATOM 1837 OE2 GLU A1045 -19.860 20.770 3.220 1.00123.56 O ANISOU 1837 OE2 GLU A1045 14076 20452 12419 -828 -9 1606 O ATOM 1838 N LEU A1046 -19.024 21.377 9.125 1.00106.50 N ANISOU 1838 N LEU A1046 12175 17779 10512 -369 358 1469 N ATOM 1839 CA LEU A1046 -18.160 20.970 10.233 1.00105.69 C ANISOU 1839 CA LEU A1046 12308 17422 10428 -315 407 1382 C ATOM 1840 C LEU A1046 -18.906 20.449 11.472 1.00110.79 C ANISOU 1840 C LEU A1046 12974 18095 11026 -425 483 1376 C ATOM 1841 O LEU A1046 -18.310 20.275 12.540 1.00109.62 O ANISOU 1841 O LEU A1046 12997 17756 10900 -353 533 1317 O ATOM 1842 CB LEU A1046 -17.060 21.989 10.555 1.00104.24 C ANISOU 1842 CB LEU A1046 12166 17073 10369 -43 429 1355 C ATOM 1843 CG LEU A1046 -15.648 21.426 10.373 1.00107.91 C ANISOU 1843 CG LEU A1046 12885 17293 10823 -12 389 1255 C ATOM 1844 CD1 LEU A1046 -15.098 21.709 8.979 1.00107.60 C ANISOU 1844 CD1 LEU A1046 12826 17260 10799 21 316 1255 C ATOM 1845 CD2 LEU A1046 -14.710 21.942 11.430 1.00109.44 C ANISOU 1845 CD2 LEU A1046 13177 17311 11094 181 440 1201 C ATOM 1846 N ASP A1047 -20.215 20.159 11.301 1.00109.36 N ANISOU 1846 N ASP A1047 12620 18163 10768 -612 490 1435 N ATOM 1847 CA ASP A1047 -21.077 19.531 12.303 1.00110.47 C ANISOU 1847 CA ASP A1047 12769 18369 10836 -777 562 1428 C ATOM 1848 C ASP A1047 -20.939 18.025 12.066 1.00114.83 C ANISOU 1848 C ASP A1047 13578 18818 11233 -1052 535 1353 C ATOM 1849 O ASP A1047 -21.093 17.231 12.996 1.00114.88 O ANISOU 1849 O ASP A1047 13756 18730 11165 -1178 595 1302 O ATOM 1850 CB ASP A1047 -22.551 19.949 12.111 1.00114.24 C ANISOU 1850 CB ASP A1047 12916 19200 11290 -857 581 1527 C ATOM 1851 CG ASP A1047 -23.001 21.179 12.884 1.00124.70 C ANISOU 1851 CG ASP A1047 14029 20622 12730 -625 661 1597 C ATOM 1852 OD1 ASP A1047 -22.657 21.290 14.083 1.00124.46 O ANISOU 1852 OD1 ASP A1047 14122 20420 12748 -531 739 1559 O ATOM 1853 OD2 ASP A1047 -23.768 21.988 12.315 1.00131.95 O ANISOU 1853 OD2 ASP A1047 14664 21799 13674 -544 650 1695 O ATOM 1854 N LYS A1048 -20.632 17.649 10.803 1.00111.29 N ANISOU 1854 N LYS A1048 13177 18376 10730 -1141 451 1347 N ATOM 1855 CA LYS A1048 -20.437 16.283 10.324 1.00111.61 C ANISOU 1855 CA LYS A1048 13478 18313 10614 -1393 423 1283 C ATOM 1856 C LYS A1048 -18.977 15.815 10.490 1.00113.50 C ANISOU 1856 C LYS A1048 14049 18213 10864 -1268 415 1195 C ATOM 1857 O LYS A1048 -18.700 14.617 10.372 1.00113.47 O ANISOU 1857 O LYS A1048 14326 18064 10723 -1439 417 1133 O ATOM 1858 CB LYS A1048 -20.917 16.166 8.863 1.00115.16 C ANISOU 1858 CB LYS A1048 13799 18962 10995 -1555 342 1328 C ATOM 1859 CG LYS A1048 -21.341 14.759 8.430 1.00131.09 C ANISOU 1859 CG LYS A1048 16009 20991 12808 -1914 336 1286 C ATOM 1860 CD LYS A1048 -22.640 14.284 9.101 1.00141.29 C ANISOU 1860 CD LYS A1048 17206 22489 13989 -2168 401 1299 C ATOM 1861 CE LYS A1048 -22.565 12.841 9.547 1.00149.79 C ANISOU 1861 CE LYS A1048 18645 23381 14886 -2430 457 1211 C ATOM 1862 NZ LYS A1048 -21.610 12.646 10.676 1.00155.30 N ANISOU 1862 NZ LYS A1048 19618 23755 15634 -2244 517 1143 N ATOM 1863 N ALA A1049 -18.056 16.753 10.792 1.00108.29 N ANISOU 1863 N ALA A1049 13360 17434 10353 -972 412 1189 N ATOM 1864 CA ALA A1049 -16.633 16.468 11.018 1.00106.75 C ANISOU 1864 CA ALA A1049 13427 16954 10177 -817 402 1109 C ATOM 1865 C ALA A1049 -16.383 15.933 12.438 1.00110.08 C ANISOU 1865 C ALA A1049 14056 17204 10566 -792 471 1052 C ATOM 1866 O ALA A1049 -15.369 15.275 12.681 1.00108.84 O ANISOU 1866 O ALA A1049 14170 16821 10363 -728 467 981 O ATOM 1867 CB ALA A1049 -15.805 17.720 10.779 1.00105.97 C ANISOU 1867 CB ALA A1049 13199 16829 10236 -540 375 1121 C ATOM 1868 N ILE A1050 -17.313 16.221 13.367 1.00107.18 N ANISOU 1868 N ILE A1050 13559 16949 10214 -833 537 1087 N ATOM 1869 CA ILE A1050 -17.267 15.797 14.771 1.00107.05 C ANISOU 1869 CA ILE A1050 13715 16794 10165 -826 611 1043 C ATOM 1870 C ILE A1050 -18.357 14.763 15.092 1.00113.00 C ANISOU 1870 C ILE A1050 14553 17619 10764 -1125 664 1037 C ATOM 1871 O ILE A1050 -18.117 13.844 15.878 1.00112.95 O ANISOU 1871 O ILE A1050 14831 17430 10655 -1193 709 975 O ATOM 1872 CB ILE A1050 -17.281 17.003 15.752 1.00109.29 C ANISOU 1872 CB ILE A1050 13827 17104 10595 -609 661 1074 C ATOM 1873 CG1 ILE A1050 -18.306 18.086 15.323 1.00110.26 C ANISOU 1873 CG1 ILE A1050 13589 17502 10802 -592 669 1172 C ATOM 1874 CG2 ILE A1050 -15.872 17.587 15.912 1.00108.13 C ANISOU 1874 CG2 ILE A1050 13762 16777 10545 -343 631 1033 C ATOM 1875 CD1 ILE A1050 -18.912 18.897 16.453 1.00118.00 C ANISOU 1875 CD1 ILE A1050 14422 18553 11861 -494 758 1213 C ATOM 1876 N GLY A1051 -19.526 14.926 14.470 1.00110.90 N ANISOU 1876 N GLY A1051 14044 17623 10471 -1302 658 1100 N ATOM 1877 CA GLY A1051 -20.673 14.036 14.616 1.00112.66 C ANISOU 1877 CA GLY A1051 14292 17977 10538 -1623 706 1097 C ATOM 1878 C GLY A1051 -21.673 14.437 15.680 1.00117.21 C ANISOU 1878 C GLY A1051 14692 18700 11142 -1655 792 1129 C ATOM 1879 O GLY A1051 -22.099 13.585 16.465 1.00117.76 O ANISOU 1879 O GLY A1051 14939 18712 11092 -1843 865 1083 O ATOM 1880 N ARG A1052 -22.073 15.732 15.697 1.00113.37 N ANISOU 1880 N ARG A1052 13869 18403 10803 -1472 794 1209 N ATOM 1881 CA ARG A1052 -23.033 16.320 16.648 1.00113.99 C ANISOU 1881 CA ARG A1052 13736 18644 10929 -1453 882 1255 C ATOM 1882 C ARG A1052 -23.572 17.665 16.156 1.00117.66 C ANISOU 1882 C ARG A1052 13815 19368 11521 -1277 865 1360 C ATOM 1883 O ARG A1052 -22.874 18.377 15.431 1.00115.87 O ANISOU 1883 O ARG A1052 13534 19101 11388 -1079 800 1385 O ATOM 1884 CB ARG A1052 -22.362 16.553 18.014 1.00113.55 C ANISOU 1884 CB ARG A1052 13856 18342 10947 -1266 950 1212 C ATOM 1885 CG ARG A1052 -22.602 15.462 19.052 1.00126.41 C ANISOU 1885 CG ARG A1052 15747 19837 12445 -1462 1028 1141 C ATOM 1886 CD ARG A1052 -21.698 15.625 20.265 1.00136.95 C ANISOU 1886 CD ARG A1052 17299 20894 13843 -1258 1070 1092 C ATOM 1887 NE ARG A1052 -20.327 15.163 20.018 1.00145.30 N ANISOU 1887 NE ARG A1052 18640 21685 14884 -1145 1003 1029 N ATOM 1888 CZ ARG A1052 -19.305 15.957 19.709 1.00158.05 C ANISOU 1888 CZ ARG A1052 20214 23215 16622 -885 944 1036 C ATOM 1889 NH1 ARG A1052 -18.098 15.446 19.504 1.00144.26 N ANISOU 1889 NH1 ARG A1052 18719 21250 14844 -797 888 974 N ATOM 1890 NH2 ARG A1052 -19.482 17.269 19.601 1.00144.60 N ANISOU 1890 NH2 ARG A1052 18226 21652 15065 -710 947 1104 N ATOM 1891 N ASN A1053 -24.792 18.033 16.602 1.00115.77 N ANISOU 1891 N ASN A1053 13320 19387 11279 -1334 934 1420 N ATOM 1892 CA ASN A1053 -25.419 19.324 16.305 1.00115.93 C ANISOU 1892 CA ASN A1053 12980 19662 11406 -1141 941 1529 C ATOM 1893 C ASN A1053 -24.907 20.282 17.385 1.00118.76 C ANISOU 1893 C ASN A1053 13373 19847 11905 -851 1019 1536 C ATOM 1894 O ASN A1053 -25.304 20.173 18.551 1.00118.87 O ANISOU 1894 O ASN A1053 13423 19830 11911 -881 1118 1520 O ATOM 1895 CB ASN A1053 -26.953 19.221 16.328 1.00118.33 C ANISOU 1895 CB ASN A1053 12996 20337 11628 -1332 986 1588 C ATOM 1896 CG ASN A1053 -27.547 18.202 15.379 1.00139.26 C ANISOU 1896 CG ASN A1053 15620 23178 14114 -1670 920 1573 C ATOM 1897 OD1 ASN A1053 -28.269 17.287 15.793 1.00135.03 O ANISOU 1897 OD1 ASN A1053 15130 22734 13443 -1964 970 1531 O ATOM 1898 ND2 ASN A1053 -27.299 18.352 14.084 1.00129.63 N ANISOU 1898 ND2 ASN A1053 14329 22035 12892 -1653 812 1605 N ATOM 1899 N THR A1054 -23.965 21.169 17.014 1.00113.75 N ANISOU 1899 N THR A1054 12756 19080 11385 -588 979 1551 N ATOM 1900 CA THR A1054 -23.297 22.080 17.950 1.00112.13 C ANISOU 1900 CA THR A1054 12622 18682 11300 -324 1047 1547 C ATOM 1901 C THR A1054 -23.621 23.572 17.841 1.00115.54 C ANISOU 1901 C THR A1054 12809 19248 11842 -61 1093 1648 C ATOM 1902 O THR A1054 -23.402 24.295 18.819 1.00114.40 O ANISOU 1902 O THR A1054 12706 18987 11774 113 1183 1653 O ATOM 1903 CB THR A1054 -21.780 21.817 17.956 1.00118.64 C ANISOU 1903 CB THR A1054 13740 19188 12149 -243 992 1458 C ATOM 1904 OG1 THR A1054 -21.305 21.675 16.613 1.00117.77 O ANISOU 1904 OG1 THR A1054 13627 19096 12024 -262 884 1455 O ATOM 1905 CG2 THR A1054 -21.394 20.597 18.787 1.00117.31 C ANISOU 1905 CG2 THR A1054 13867 18814 11892 -402 1008 1360 C ATOM 1906 N ASN A1055 -24.114 24.039 16.671 1.00112.64 N ANISOU 1906 N ASN A1055 12212 19112 11474 -26 1036 1727 N ATOM 1907 CA ASN A1055 -24.431 25.452 16.389 1.00112.59 C ANISOU 1907 CA ASN A1055 11989 19239 11552 239 1075 1831 C ATOM 1908 C ASN A1055 -23.178 26.359 16.502 1.00113.88 C ANISOU 1908 C ASN A1055 12318 19135 11817 487 1087 1804 C ATOM 1909 O ASN A1055 -23.290 27.549 16.816 1.00113.48 O ANISOU 1909 O ASN A1055 12188 19093 11836 720 1170 1868 O ATOM 1910 CB ASN A1055 -25.615 25.974 17.248 1.00115.52 C ANISOU 1910 CB ASN A1055 12152 19808 11932 303 1198 1910 C ATOM 1911 CG ASN A1055 -26.990 25.823 16.626 1.00142.08 C ANISOU 1911 CG ASN A1055 15201 23565 15219 190 1180 1996 C ATOM 1912 OD1 ASN A1055 -27.718 26.805 16.432 1.00137.13 O ANISOU 1912 OD1 ASN A1055 14326 23157 14620 382 1226 2107 O ATOM 1913 ND2 ASN A1055 -27.404 24.591 16.353 1.00135.46 N ANISOU 1913 ND2 ASN A1055 14366 22834 14267 -124 1122 1949 N ATOM 1914 N GLY A1056 -22.015 25.749 16.260 1.00108.30 N ANISOU 1914 N GLY A1056 11848 18199 11104 423 1012 1707 N ATOM 1915 CA GLY A1056 -20.722 26.414 16.311 1.00105.94 C ANISOU 1915 CA GLY A1056 11715 17658 10880 606 1009 1660 C ATOM 1916 C GLY A1056 -19.780 25.849 17.367 1.00107.65 C ANISOU 1916 C GLY A1056 12197 17608 11098 574 1028 1554 C ATOM 1917 O GLY A1056 -18.898 25.039 17.083 1.00106.36 O ANISOU 1917 O GLY A1056 12215 17298 10899 488 950 1470 O ATOM 1918 N VAL A1057 -19.992 26.304 18.595 1.00103.44 N ANISOU 1918 N VAL A1057 11684 17018 10599 657 1137 1563 N ATOM 1919 CA VAL A1057 -19.203 25.969 19.793 1.00101.86 C ANISOU 1919 CA VAL A1057 11719 16580 10402 659 1173 1477 C ATOM 1920 C VAL A1057 -18.782 24.503 19.923 1.00104.32 C ANISOU 1920 C VAL A1057 12230 16777 10628 465 1103 1386 C ATOM 1921 O VAL A1057 -19.633 23.619 19.869 1.00105.01 O ANISOU 1921 O VAL A1057 12282 16979 10638 272 1098 1394 O ATOM 1922 CB VAL A1057 -19.872 26.425 21.126 1.00106.54 C ANISOU 1922 CB VAL A1057 12285 17176 11018 713 1307 1511 C ATOM 1923 CG1 VAL A1057 -18.822 26.781 22.176 1.00105.12 C ANISOU 1923 CG1 VAL A1057 12318 16748 10875 823 1351 1444 C ATOM 1924 CG2 VAL A1057 -20.845 27.585 20.924 1.00107.40 C ANISOU 1924 CG2 VAL A1057 12150 17482 11174 856 1390 1629 C ATOM 1925 N ILE A1058 -17.470 24.261 20.129 1.00 98.78 N ANISOU 1925 N ILE A1058 11746 15856 9929 518 1058 1298 N ATOM 1926 CA ILE A1058 -16.880 22.919 20.251 1.00 98.07 C ANISOU 1926 CA ILE A1058 11885 15626 9750 384 995 1210 C ATOM 1927 C ILE A1058 -15.978 22.831 21.501 1.00100.91 C ANISOU 1927 C ILE A1058 12460 15769 10112 468 1025 1138 C ATOM 1928 O ILE A1058 -15.473 23.857 21.967 1.00 99.73 O ANISOU 1928 O ILE A1058 12293 15563 10038 633 1067 1140 O ATOM 1929 CB ILE A1058 -16.217 22.329 18.967 1.00100.56 C ANISOU 1929 CB ILE A1058 12257 15924 10027 333 882 1175 C ATOM 1930 CG1 ILE A1058 -14.988 23.142 18.496 1.00 99.38 C ANISOU 1930 CG1 ILE A1058 12125 15685 9952 518 840 1145 C ATOM 1931 CG2 ILE A1058 -17.235 22.090 17.842 1.00102.38 C ANISOU 1931 CG2 ILE A1058 12310 16371 10219 188 846 1239 C ATOM 1932 CD1 ILE A1058 -13.814 22.274 18.054 1.00103.90 C ANISOU 1932 CD1 ILE A1058 12896 16112 10470 503 753 1058 C ATOM 1933 N THR A1059 -15.792 21.610 22.040 1.00 97.45 N ANISOU 1933 N THR A1059 12237 15211 9577 350 1009 1074 N ATOM 1934 CA THR A1059 -14.971 21.349 23.229 1.00 96.53 C ANISOU 1934 CA THR A1059 12343 14896 9437 420 1026 1005 C ATOM 1935 C THR A1059 -13.460 21.390 22.930 1.00 98.61 C ANISOU 1935 C THR A1059 12726 15031 9709 557 945 938 C ATOM 1936 O THR A1059 -13.070 21.366 21.762 1.00 97.84 O ANISOU 1936 O THR A1059 12577 14978 9620 566 874 935 O ATOM 1937 CB THR A1059 -15.354 20.006 23.840 1.00105.28 C ANISOU 1937 CB THR A1059 13654 15925 10421 250 1041 966 C ATOM 1938 N LYS A1060 -12.617 21.452 23.986 1.00 94.19 N ANISOU 1938 N LYS A1060 12320 14326 9142 661 956 883 N ATOM 1939 CA LYS A1060 -11.154 21.490 23.868 1.00 92.87 C ANISOU 1939 CA LYS A1060 12255 14059 8971 796 883 814 C ATOM 1940 C LYS A1060 -10.582 20.171 23.325 1.00 96.41 C ANISOU 1940 C LYS A1060 12885 14432 9316 749 799 760 C ATOM 1941 O LYS A1060 -9.683 20.208 22.483 1.00 95.36 O ANISOU 1941 O LYS A1060 12744 14299 9191 823 728 728 O ATOM 1942 CB LYS A1060 -10.503 21.866 25.208 1.00 95.10 C ANISOU 1942 CB LYS A1060 12645 14234 9256 903 918 774 C ATOM 1943 CG LYS A1060 -9.046 22.306 25.085 1.00107.23 C ANISOU 1943 CG LYS A1060 14208 15728 10807 1051 855 711 C ATOM 1944 CD LYS A1060 -8.394 22.461 26.450 1.00116.30 C ANISOU 1944 CD LYS A1060 15485 16777 11926 1133 876 666 C ATOM 1945 CE LYS A1060 -6.884 22.447 26.385 1.00124.32 C ANISOU 1945 CE LYS A1060 16565 17763 12910 1258 793 588 C ATOM 1946 NZ LYS A1060 -6.333 23.709 25.824 1.00130.80 N ANISOU 1946 NZ LYS A1060 17222 18664 13812 1325 798 583 N ATOM 1947 N ASP A1061 -11.099 19.017 23.805 1.00 93.60 N ANISOU 1947 N ASP A1061 12706 14006 8852 625 818 748 N ATOM 1948 CA ASP A1061 -10.678 17.684 23.363 1.00 93.67 C ANISOU 1948 CA ASP A1061 12933 13920 8736 571 760 703 C ATOM 1949 C ASP A1061 -11.119 17.406 21.922 1.00 96.98 C ANISOU 1949 C ASP A1061 13259 14441 9147 452 723 733 C ATOM 1950 O ASP A1061 -10.436 16.666 21.211 1.00 96.59 O ANISOU 1950 O ASP A1061 13344 14328 9029 463 662 695 O ATOM 1951 CB ASP A1061 -11.183 16.596 24.323 1.00 96.67 C ANISOU 1951 CB ASP A1061 13554 14186 8990 459 809 682 C ATOM 1952 CG ASP A1061 -10.466 16.584 25.661 1.00107.57 C ANISOU 1952 CG ASP A1061 15099 15430 10343 594 821 638 C ATOM 1953 OD1 ASP A1061 -9.684 15.641 25.906 1.00108.32 O ANISOU 1953 OD1 ASP A1061 15447 15388 10324 657 782 585 O ATOM 1954 OD2 ASP A1061 -10.688 17.519 26.463 1.00113.95 O ANISOU 1954 OD2 ASP A1061 15791 16271 11235 643 873 659 O ATOM 1955 N GLU A1062 -12.240 18.027 21.489 1.00 93.16 N ANISOU 1955 N GLU A1062 12545 14123 8730 348 761 803 N ATOM 1956 CA GLU A1062 -12.778 17.926 20.128 1.00 93.01 C ANISOU 1956 CA GLU A1062 12397 14235 8708 230 724 842 C ATOM 1957 C GLU A1062 -11.820 18.606 19.144 1.00 94.91 C ANISOU 1957 C GLU A1062 12540 14496 9027 374 656 833 C ATOM 1958 O GLU A1062 -11.516 18.039 18.093 1.00 94.17 O ANISOU 1958 O GLU A1062 12500 14397 8885 323 597 817 O ATOM 1959 CB GLU A1062 -14.177 18.563 20.041 1.00 95.10 C ANISOU 1959 CB GLU A1062 12412 14696 9025 124 782 925 C ATOM 1960 CG GLU A1062 -15.279 17.710 20.647 1.00107.08 C ANISOU 1960 CG GLU A1062 14005 16240 10443 -84 844 933 C ATOM 1961 CD GLU A1062 -16.665 18.327 20.668 1.00128.41 C ANISOU 1961 CD GLU A1062 16442 19160 13188 -177 907 1014 C ATOM 1962 OE1 GLU A1062 -17.123 18.814 19.609 1.00119.81 O ANISOU 1962 OE1 GLU A1062 15133 18249 12140 -199 874 1071 O ATOM 1963 OE2 GLU A1062 -17.329 18.243 21.726 1.00125.64 O ANISOU 1963 OE2 GLU A1062 16110 18809 12817 -236 989 1019 O ATOM 1964 N ALA A1063 -11.325 19.810 19.513 1.00 90.24 N ANISOU 1964 N ALA A1063 11825 13917 8544 543 672 836 N ATOM 1965 CA ALA A1063 -10.374 20.614 18.744 1.00 88.74 C ANISOU 1965 CA ALA A1063 11545 13743 8429 680 625 819 C ATOM 1966 C ALA A1063 -9.018 19.918 18.647 1.00 91.20 C ANISOU 1966 C ALA A1063 12047 13926 8681 766 560 734 C ATOM 1967 O ALA A1063 -8.353 20.035 17.617 1.00 90.25 O ANISOU 1967 O ALA A1063 11892 13822 8576 809 506 714 O ATOM 1968 CB ALA A1063 -10.213 21.987 19.378 1.00 88.85 C ANISOU 1968 CB ALA A1063 11432 13783 8545 814 679 835 C ATOM 1969 N GLU A1064 -8.617 19.190 19.717 1.00 87.30 N ANISOU 1969 N GLU A1064 11754 13307 8111 798 569 687 N ATOM 1970 CA GLU A1064 -7.369 18.425 19.779 1.00 86.68 C ANISOU 1970 CA GLU A1064 11870 13111 7953 903 512 612 C ATOM 1971 C GLU A1064 -7.428 17.257 18.787 1.00 90.58 C ANISOU 1971 C GLU A1064 12501 13567 8349 805 473 605 C ATOM 1972 O GLU A1064 -6.426 16.972 18.131 1.00 89.86 O ANISOU 1972 O GLU A1064 12472 13439 8231 896 419 562 O ATOM 1973 CB GLU A1064 -7.102 17.923 21.207 1.00 88.38 C ANISOU 1973 CB GLU A1064 12273 13209 8097 961 536 577 C ATOM 1974 CG GLU A1064 -5.628 17.678 21.491 1.00 97.54 C ANISOU 1974 CG GLU A1064 13553 14297 9210 1145 479 504 C ATOM 1975 CD GLU A1064 -5.298 17.251 22.908 1.00113.65 C ANISOU 1975 CD GLU A1064 15773 16233 11175 1223 493 472 C ATOM 1976 OE1 GLU A1064 -4.840 16.099 23.087 1.00105.57 O ANISOU 1976 OE1 GLU A1064 14988 15101 10024 1269 466 437 O ATOM 1977 OE2 GLU A1064 -5.471 18.072 23.838 1.00104.69 O ANISOU 1977 OE2 GLU A1064 14557 15120 10100 1246 534 481 O ATOM 1978 N LYS A1065 -8.612 16.611 18.660 1.00 87.50 N ANISOU 1978 N LYS A1065 12154 13194 7898 609 507 647 N ATOM 1979 CA LYS A1065 -8.867 15.514 17.720 1.00 87.77 C ANISOU 1979 CA LYS A1065 12328 13197 7823 467 486 647 C ATOM 1980 C LYS A1065 -8.835 16.039 16.282 1.00 89.98 C ANISOU 1980 C LYS A1065 12427 13590 8170 443 440 672 C ATOM 1981 O LYS A1065 -8.291 15.371 15.402 1.00 89.71 O ANISOU 1981 O LYS A1065 12514 13500 8070 435 399 645 O ATOM 1982 CB LYS A1065 -10.228 14.860 18.005 1.00 91.70 C ANISOU 1982 CB LYS A1065 12883 13721 8238 234 543 684 C ATOM 1983 CG LYS A1065 -10.126 13.497 18.671 1.00109.46 C ANISOU 1983 CG LYS A1065 15475 15795 10319 178 572 639 C ATOM 1984 CD LYS A1065 -11.427 12.713 18.534 1.00121.21 C ANISOU 1984 CD LYS A1065 17036 17321 11698 -106 624 666 C ATOM 1985 CE LYS A1065 -11.391 11.390 19.263 1.00132.49 C ANISOU 1985 CE LYS A1065 18836 18560 12944 -177 671 620 C ATOM 1986 NZ LYS A1065 -11.575 11.558 20.730 1.00140.44 N ANISOU 1986 NZ LYS A1065 19891 19511 13960 -125 725 611 N ATOM 1987 N LEU A1066 -9.418 17.244 16.056 1.00 85.04 N ANISOU 1987 N LEU A1066 11527 13115 7669 441 452 727 N ATOM 1988 CA LEU A1066 -9.486 17.929 14.762 1.00 83.77 C ANISOU 1988 CA LEU A1066 11177 13071 7579 430 414 761 C ATOM 1989 C LEU A1066 -8.092 18.362 14.315 1.00 85.86 C ANISOU 1989 C LEU A1066 11445 13284 7892 608 369 704 C ATOM 1990 O LEU A1066 -7.765 18.212 13.138 1.00 85.32 O ANISOU 1990 O LEU A1066 11373 13230 7814 586 324 697 O ATOM 1991 CB LEU A1066 -10.443 19.132 14.839 1.00 83.57 C ANISOU 1991 CB LEU A1066 10886 13207 7661 420 453 836 C ATOM 1992 CG LEU A1066 -11.093 19.592 13.534 1.00 88.14 C ANISOU 1992 CG LEU A1066 11275 13939 8273 340 424 898 C ATOM 1993 CD1 LEU A1066 -12.312 18.751 13.195 1.00 89.63 C ANISOU 1993 CD1 LEU A1066 11465 14222 8369 108 427 943 C ATOM 1994 CD2 LEU A1066 -11.519 21.037 13.634 1.00 89.87 C ANISOU 1994 CD2 LEU A1066 11256 14280 8610 440 462 958 C ATOM 1995 N PHE A1067 -7.262 18.860 15.264 1.00 81.36 N ANISOU 1995 N PHE A1067 10889 12660 7363 772 382 661 N ATOM 1996 CA PHE A1067 -5.868 19.245 15.021 1.00 80.14 C ANISOU 1996 CA PHE A1067 10736 12474 7239 937 344 595 C ATOM 1997 C PHE A1067 -5.068 17.983 14.711 1.00 85.45 C ANISOU 1997 C PHE A1067 11632 13037 7798 965 302 540 C ATOM 1998 O PHE A1067 -4.208 18.013 13.831 1.00 84.68 O ANISOU 1998 O PHE A1067 11527 12941 7705 1031 262 503 O ATOM 1999 CB PHE A1067 -5.269 19.996 16.232 1.00 80.97 C ANISOU 1999 CB PHE A1067 10810 12563 7390 1076 372 561 C ATOM 2000 CG PHE A1067 -3.774 20.237 16.176 1.00 81.36 C ANISOU 2000 CG PHE A1067 10877 12596 7442 1234 333 481 C ATOM 2001 CD1 PHE A1067 -3.252 21.322 15.482 1.00 83.30 C ANISOU 2001 CD1 PHE A1067 10964 12917 7768 1282 328 465 C ATOM 2002 CD2 PHE A1067 -2.892 19.388 16.832 1.00 83.40 C ANISOU 2002 CD2 PHE A1067 11309 12770 7610 1335 305 422 C ATOM 2003 CE1 PHE A1067 -1.872 21.544 15.431 1.00 83.59 C ANISOU 2003 CE1 PHE A1067 11002 12962 7798 1407 297 384 C ATOM 2004 CE2 PHE A1067 -1.513 19.604 16.773 1.00 85.76 C ANISOU 2004 CE2 PHE A1067 11596 13088 7902 1482 266 348 C ATOM 2005 CZ PHE A1067 -1.012 20.682 16.075 1.00 83.05 C ANISOU 2005 CZ PHE A1067 11079 12835 7641 1508 263 326 C ATOM 2006 N ASN A1068 -5.358 16.875 15.434 1.00 83.62 N ANISOU 2006 N ASN A1068 11611 12705 7455 918 320 535 N ATOM 2007 CA ASN A1068 -4.711 15.582 15.216 1.00 84.43 C ANISOU 2007 CA ASN A1068 11972 12683 7425 950 297 491 C ATOM 2008 C ASN A1068 -5.084 15.030 13.847 1.00 88.91 C ANISOU 2008 C ASN A1068 12578 13257 7947 808 280 513 C ATOM 2009 O ASN A1068 -4.232 14.447 13.190 1.00 88.86 O ANISOU 2009 O ASN A1068 12698 13184 7879 879 252 474 O ATOM 2010 CB ASN A1068 -5.029 14.582 16.332 1.00 87.01 C ANISOU 2010 CB ASN A1068 12540 12890 7632 923 333 485 C ATOM 2011 CG ASN A1068 -4.165 14.722 17.569 1.00110.73 C ANISOU 2011 CG ASN A1068 15603 15843 10628 1117 329 440 C ATOM 2012 OD1 ASN A1068 -4.657 14.674 18.702 1.00104.36 O ANISOU 2012 OD1 ASN A1068 14851 14999 9802 1093 368 450 O ATOM 2013 ND2 ASN A1068 -2.854 14.870 17.392 1.00103.18 N ANISOU 2013 ND2 ASN A1068 14637 14891 9677 1307 283 386 N ATOM 2014 N GLN A1069 -6.333 15.266 13.394 1.00 85.59 N ANISOU 2014 N GLN A1069 12036 12931 7555 613 297 577 N ATOM 2015 CA GLN A1069 -6.793 14.859 12.066 1.00 85.85 C ANISOU 2015 CA GLN A1069 12076 12999 7546 453 277 605 C ATOM 2016 C GLN A1069 -6.161 15.761 10.995 1.00 89.31 C ANISOU 2016 C GLN A1069 12334 13514 8088 538 233 599 C ATOM 2017 O GLN A1069 -5.905 15.295 9.884 1.00 89.30 O ANISOU 2017 O GLN A1069 12404 13488 8039 487 206 590 O ATOM 2018 CB GLN A1069 -8.327 14.848 11.977 1.00 87.83 C ANISOU 2018 CB GLN A1069 12230 13359 7783 221 304 674 C ATOM 2019 CG GLN A1069 -8.938 13.560 12.518 1.00102.87 C ANISOU 2019 CG GLN A1069 14387 15169 9529 59 348 669 C ATOM 2020 CD GLN A1069 -10.436 13.632 12.683 1.00121.78 C ANISOU 2020 CD GLN A1069 16659 17701 11912 -164 383 729 C ATOM 2021 OE1 GLN A1069 -10.964 14.377 13.517 1.00116.64 O ANISOU 2021 OE1 GLN A1069 15840 17133 11344 -134 414 759 O ATOM 2022 NE2 GLN A1069 -11.151 12.810 11.930 1.00114.81 N ANISOU 2022 NE2 GLN A1069 15868 16845 10911 -401 386 747 N ATOM 2023 N ASP A1070 -5.874 17.038 11.348 1.00 85.03 N ANISOU 2023 N ASP A1070 11582 13051 7676 665 235 599 N ATOM 2024 CA ASP A1070 -5.204 17.996 10.465 1.00 84.11 C ANISOU 2024 CA ASP A1070 11308 12998 7653 752 206 583 C ATOM 2025 C ASP A1070 -3.738 17.603 10.319 1.00 88.17 C ANISOU 2025 C ASP A1070 11947 13424 8131 906 180 500 C ATOM 2026 O ASP A1070 -3.182 17.756 9.233 1.00 87.56 O ANISOU 2026 O ASP A1070 11840 13361 8070 923 153 479 O ATOM 2027 CB ASP A1070 -5.314 19.435 10.994 1.00 85.22 C ANISOU 2027 CB ASP A1070 11233 13230 7918 835 233 602 C ATOM 2028 CG ASP A1070 -6.606 20.145 10.643 1.00 95.74 C ANISOU 2028 CG ASP A1070 12382 14688 9306 724 252 691 C ATOM 2029 OD1 ASP A1070 -7.217 20.746 11.554 1.00 96.64 O ANISOU 2029 OD1 ASP A1070 12406 14848 9467 741 299 727 O ATOM 2030 OD2 ASP A1070 -6.991 20.132 9.450 1.00101.20 O ANISOU 2030 OD2 ASP A1070 13019 15439 9993 631 222 725 O ATOM 2031 N VAL A1071 -3.117 17.085 11.407 1.00 85.22 N ANISOU 2031 N VAL A1071 11712 12968 7700 1023 189 455 N ATOM 2032 CA VAL A1071 -1.725 16.623 11.404 1.00 85.16 C ANISOU 2032 CA VAL A1071 11820 12897 7640 1194 165 379 C ATOM 2033 C VAL A1071 -1.642 15.246 10.732 1.00 90.61 C ANISOU 2033 C VAL A1071 12755 13476 8198 1147 159 374 C ATOM 2034 O VAL A1071 -0.943 15.136 9.733 1.00 90.27 O ANISOU 2034 O VAL A1071 12723 13427 8146 1189 138 344 O ATOM 2035 CB VAL A1071 -1.022 16.678 12.793 1.00 88.79 C ANISOU 2035 CB VAL A1071 12320 13334 8083 1358 169 335 C ATOM 2036 CG1 VAL A1071 0.373 16.054 12.738 1.00 88.82 C ANISOU 2036 CG1 VAL A1071 12445 13295 8008 1543 140 263 C ATOM 2037 CG2 VAL A1071 -0.935 18.110 13.308 1.00 87.72 C ANISOU 2037 CG2 VAL A1071 11955 13304 8069 1400 181 331 C ATOM 2038 N ASP A1072 -2.391 14.227 11.231 1.00 88.41 N ANISOU 2038 N ASP A1072 12679 13104 7809 1045 187 402 N ATOM 2039 CA ASP A1072 -2.428 12.853 10.694 1.00 89.49 C ANISOU 2039 CA ASP A1072 13099 13111 7792 976 200 400 C ATOM 2040 C ASP A1072 -2.610 12.770 9.169 1.00 93.76 C ANISOU 2040 C ASP A1072 13619 13674 8332 847 185 417 C ATOM 2041 O ASP A1072 -2.171 11.793 8.564 1.00 94.24 O ANISOU 2041 O ASP A1072 13906 13625 8277 855 194 396 O ATOM 2042 CB ASP A1072 -3.484 11.988 11.415 1.00 92.38 C ANISOU 2042 CB ASP A1072 13656 13397 8048 818 246 434 C ATOM 2043 CG ASP A1072 -3.072 11.419 12.769 1.00102.97 C ANISOU 2043 CG ASP A1072 15188 14630 9304 959 269 403 C ATOM 2044 OD1 ASP A1072 -2.422 12.149 13.554 1.00102.52 O ANISOU 2044 OD1 ASP A1072 14999 14626 9330 1136 249 377 O ATOM 2045 OD2 ASP A1072 -3.453 10.265 13.066 1.00110.73 O ANISOU 2045 OD2 ASP A1072 16461 15480 10133 878 311 407 O ATOM 2046 N ALA A1073 -3.242 13.791 8.554 1.00 89.65 N ANISOU 2046 N ALA A1073 12842 13290 7931 739 166 457 N ATOM 2047 CA ALA A1073 -3.447 13.864 7.105 1.00 89.47 C ANISOU 2047 CA ALA A1073 12772 13306 7916 617 144 478 C ATOM 2048 C ALA A1073 -2.288 14.599 6.418 1.00 92.37 C ANISOU 2048 C ALA A1073 13017 13709 8370 776 115 430 C ATOM 2049 O ALA A1073 -1.909 14.230 5.303 1.00 92.19 O ANISOU 2049 O ALA A1073 13072 13648 8308 748 105 415 O ATOM 2050 CB ALA A1073 -4.768 14.547 6.790 1.00 90.14 C ANISOU 2050 CB ALA A1073 12652 13529 8067 427 137 552 C ATOM 2051 N ALA A1074 -1.728 15.632 7.085 1.00 87.89 N ANISOU 2051 N ALA A1074 12270 13214 7911 928 110 401 N ATOM 2052 CA ALA A1074 -0.603 16.427 6.579 1.00 86.96 C ANISOU 2052 CA ALA A1074 12024 13146 7870 1068 93 344 C ATOM 2053 C ALA A1074 0.755 15.792 6.920 1.00 90.85 C ANISOU 2053 C ALA A1074 12654 13573 8294 1266 91 267 C ATOM 2054 O ALA A1074 1.776 16.186 6.347 1.00 90.01 O ANISOU 2054 O ALA A1074 12475 13505 8219 1370 80 211 O ATOM 2055 CB ALA A1074 -0.676 17.847 7.119 1.00 86.81 C ANISOU 2055 CB ALA A1074 11764 13240 7979 1113 98 348 C ATOM 2056 N VAL A1075 0.761 14.804 7.840 1.00 87.99 N ANISOU 2056 N VAL A1075 12491 13117 7826 1322 106 265 N ATOM 2057 CA VAL A1075 1.957 14.065 8.253 1.00 88.30 C ANISOU 2057 CA VAL A1075 12685 13094 7773 1531 105 205 C ATOM 2058 C VAL A1075 2.254 12.914 7.276 1.00 92.66 C ANISOU 2058 C VAL A1075 13473 13529 8205 1526 119 199 C ATOM 2059 O VAL A1075 3.396 12.454 7.193 1.00 92.74 O ANISOU 2059 O VAL A1075 13573 13512 8152 1718 120 146 O ATOM 2060 CB VAL A1075 1.916 13.644 9.752 1.00 92.72 C ANISOU 2060 CB VAL A1075 13351 13606 8271 1625 115 204 C ATOM 2061 CG1 VAL A1075 1.281 12.271 9.961 1.00 93.69 C ANISOU 2061 CG1 VAL A1075 13785 13570 8241 1549 149 238 C ATOM 2062 CG2 VAL A1075 3.297 13.712 10.384 1.00 92.67 C ANISOU 2062 CG2 VAL A1075 13323 13645 8244 1881 95 135 C ATOM 2063 N ARG A1076 1.221 12.475 6.526 1.00 89.10 N ANISOU 2063 N ARG A1076 13118 13021 7716 1305 134 253 N ATOM 2064 CA ARG A1076 1.325 11.426 5.514 1.00 89.56 C ANISOU 2064 CA ARG A1076 13415 12960 7652 1249 157 255 C ATOM 2065 C ARG A1076 2.017 11.978 4.268 1.00 92.08 C ANISOU 2065 C ARG A1076 13605 13338 8042 1277 139 224 C ATOM 2066 O ARG A1076 2.782 11.260 3.625 1.00 91.95 O ANISOU 2066 O ARG A1076 13759 13239 7940 1365 159 192 O ATOM 2067 CB ARG A1076 -0.061 10.857 5.168 1.00 90.59 C ANISOU 2067 CB ARG A1076 13671 13036 7712 969 177 320 C ATOM 2068 CG ARG A1076 -0.617 9.921 6.239 1.00102.64 C ANISOU 2068 CG ARG A1076 15432 14454 9111 932 216 338 C ATOM 2069 CD ARG A1076 -1.887 9.207 5.810 1.00113.82 C ANISOU 2069 CD ARG A1076 17005 15818 10422 635 246 390 C ATOM 2070 NE ARG A1076 -3.069 10.071 5.873 1.00121.35 N ANISOU 2070 NE ARG A1076 17698 16926 11484 442 221 441 N ATOM 2071 CZ ARG A1076 -3.644 10.633 4.814 1.00135.42 C ANISOU 2071 CZ ARG A1076 19305 18818 13332 279 190 477 C ATOM 2072 NH1 ARG A1076 -3.156 10.432 3.597 1.00123.41 N ANISOU 2072 NH1 ARG A1076 17846 17259 11785 266 181 464 N ATOM 2073 NH2 ARG A1076 -4.717 11.400 4.965 1.00122.41 N ANISOU 2073 NH2 ARG A1076 17420 17319 11769 137 171 530 N ATOM 2074 N GLY A1077 1.768 13.256 3.978 1.00 87.57 N ANISOU 2074 N GLY A1077 12749 12905 7620 1214 108 231 N ATOM 2075 CA GLY A1077 2.343 13.980 2.849 1.00 86.98 C ANISOU 2075 CA GLY A1077 12528 12896 7624 1223 93 201 C ATOM 2076 C GLY A1077 3.844 14.181 2.928 1.00 91.02 C ANISOU 2076 C GLY A1077 12990 13445 8149 1456 95 116 C ATOM 2077 O GLY A1077 4.512 14.250 1.891 1.00 90.80 O ANISOU 2077 O GLY A1077 12953 13421 8127 1481 100 79 O ATOM 2078 N ILE A1078 4.382 14.283 4.162 1.00 87.47 N ANISOU 2078 N ILE A1078 12501 13035 7698 1624 91 83 N ATOM 2079 CA ILE A1078 5.817 14.447 4.444 1.00 87.27 C ANISOU 2079 CA ILE A1078 12409 13083 7669 1855 87 1 C ATOM 2080 C ILE A1078 6.554 13.149 4.068 1.00 91.87 C ANISOU 2080 C ILE A1078 13240 13556 8109 1993 112 -21 C ATOM 2081 O ILE A1078 7.649 13.197 3.503 1.00 91.48 O ANISOU 2081 O ILE A1078 13146 13559 8053 2126 118 -82 O ATOM 2082 CB ILE A1078 6.070 14.857 5.931 1.00 90.22 C ANISOU 2082 CB ILE A1078 12684 13534 8063 1978 72 -19 C ATOM 2083 CG1 ILE A1078 5.190 16.057 6.351 1.00 89.56 C ANISOU 2083 CG1 ILE A1078 12397 13527 8103 1835 65 15 C ATOM 2084 CG2 ILE A1078 7.554 15.163 6.172 1.00 91.20 C ANISOU 2084 CG2 ILE A1078 12690 13780 8182 2195 61 -108 C ATOM 2085 CD1 ILE A1078 5.032 16.258 7.842 1.00 96.45 C ANISOU 2085 CD1 ILE A1078 13240 14428 8979 1898 60 21 C ATOM 2086 N LEU A1079 5.925 11.995 4.365 1.00 89.21 N ANISOU 2086 N LEU A1079 13177 13068 7651 1956 135 29 N ATOM 2087 CA LEU A1079 6.451 10.655 4.099 1.00 90.34 C ANISOU 2087 CA LEU A1079 13623 13071 7631 2081 175 22 C ATOM 2088 C LEU A1079 6.411 10.285 2.603 1.00 94.70 C ANISOU 2088 C LEU A1079 14285 13543 8151 1967 204 29 C ATOM 2089 O LEU A1079 7.071 9.326 2.197 1.00 95.30 O ANISOU 2089 O LEU A1079 14589 13517 8103 2097 246 13 O ATOM 2090 CB LEU A1079 5.703 9.603 4.949 1.00 91.21 C ANISOU 2090 CB LEU A1079 14016 13030 7608 2049 202 72 C ATOM 2091 CG LEU A1079 5.610 9.852 6.466 1.00 95.46 C ANISOU 2091 CG LEU A1079 14489 13619 8162 2141 179 72 C ATOM 2092 CD1 LEU A1079 4.448 9.094 7.070 1.00 96.11 C ANISOU 2092 CD1 LEU A1079 14803 13562 8151 1987 209 130 C ATOM 2093 CD2 LEU A1079 6.912 9.504 7.176 1.00 98.30 C ANISOU 2093 CD2 LEU A1079 14890 14014 8447 2463 173 21 C ATOM 2094 N ARG A1080 5.639 11.043 1.791 1.00 90.56 N ANISOU 2094 N ARG A1080 13610 13066 7732 1734 184 56 N ATOM 2095 CA ARG A1080 5.504 10.838 0.345 1.00 90.50 C ANISOU 2095 CA ARG A1080 13682 12998 7706 1595 202 66 C ATOM 2096 C ARG A1080 6.410 11.759 -0.477 1.00 93.93 C ANISOU 2096 C ARG A1080 13895 13547 8246 1662 190 6 C ATOM 2097 O ARG A1080 6.872 11.352 -1.546 1.00 93.95 O ANISOU 2097 O ARG A1080 14009 13487 8202 1664 220 -13 O ATOM 2098 CB ARG A1080 4.035 10.945 -0.099 1.00 90.07 C ANISOU 2098 CB ARG A1080 13634 12921 7669 1290 188 140 C ATOM 2099 CG ARG A1080 3.335 9.592 -0.236 1.00101.38 C ANISOU 2099 CG ARG A1080 15411 14181 8928 1157 231 187 C ATOM 2100 CD ARG A1080 2.848 9.035 1.093 1.00111.66 C ANISOU 2100 CD ARG A1080 16839 15431 10155 1179 245 210 C ATOM 2101 NE ARG A1080 2.668 7.582 1.050 1.00120.85 N ANISOU 2101 NE ARG A1080 18403 16400 11116 1140 310 228 N ATOM 2102 CZ ARG A1080 3.604 6.697 1.384 1.00134.64 C ANISOU 2102 CZ ARG A1080 20393 18028 12738 1375 358 195 C ATOM 2103 NH1 ARG A1080 3.348 5.397 1.320 1.00123.10 N ANISOU 2103 NH1 ARG A1080 19325 16370 11076 1322 430 216 N ATOM 2104 NH2 ARG A1080 4.802 7.105 1.784 1.00120.30 N ANISOU 2104 NH2 ARG A1080 18434 16293 10980 1665 340 143 N ATOM 2105 N ASN A1081 6.667 12.990 0.016 1.00 89.72 N ANISOU 2105 N ASN A1081 13068 13174 7846 1706 155 -27 N ATOM 2106 CA ASN A1081 7.554 13.945 -0.650 1.00 89.22 C ANISOU 2106 CA ASN A1081 12795 13229 7875 1758 151 -95 C ATOM 2107 C ASN A1081 8.997 13.496 -0.389 1.00 95.44 C ANISOU 2107 C ASN A1081 13611 14056 8598 2024 174 -172 C ATOM 2108 O ASN A1081 9.437 13.474 0.763 1.00 95.54 O ANISOU 2108 O ASN A1081 13574 14135 8591 2186 161 -194 O ATOM 2109 CB ASN A1081 7.292 15.377 -0.151 1.00 87.19 C ANISOU 2109 CB ASN A1081 12254 13118 7758 1702 120 -103 C ATOM 2110 CG ASN A1081 8.149 16.457 -0.779 1.00105.03 C ANISOU 2110 CG ASN A1081 14307 15497 10103 1726 127 -179 C ATOM 2111 OD1 ASN A1081 9.369 16.535 -0.575 1.00 96.48 O ANISOU 2111 OD1 ASN A1081 13153 14500 9004 1896 139 -261 O ATOM 2112 ND2 ASN A1081 7.514 17.361 -1.507 1.00 97.07 N ANISOU 2112 ND2 ASN A1081 13191 14511 9181 1556 119 -154 N ATOM 2113 N ALA A1082 9.713 13.110 -1.462 1.00 93.27 N ANISOU 2113 N ALA A1082 13416 13744 8279 2071 209 -209 N ATOM 2114 CA ALA A1082 11.091 12.611 -1.415 1.00 94.36 C ANISOU 2114 CA ALA A1082 13583 13927 8341 2331 239 -278 C ATOM 2115 C ALA A1082 12.158 13.658 -1.051 1.00 98.08 C ANISOU 2115 C ALA A1082 13752 14621 8893 2454 222 -370 C ATOM 2116 O ALA A1082 13.250 13.277 -0.618 1.00 98.43 O ANISOU 2116 O ALA A1082 13779 14752 8869 2694 233 -423 O ATOM 2117 CB ALA A1082 11.446 11.933 -2.733 1.00 95.83 C ANISOU 2117 CB ALA A1082 13948 14005 8460 2325 292 -287 C ATOM 2118 N LYS A1083 11.855 14.963 -1.228 1.00 93.78 N ANISOU 2118 N LYS A1083 12977 14175 8479 2292 200 -388 N ATOM 2119 CA LYS A1083 12.801 16.055 -0.954 1.00 93.52 C ANISOU 2119 CA LYS A1083 12670 14349 8514 2356 194 -480 C ATOM 2120 C LYS A1083 13.105 16.189 0.550 1.00 98.14 C ANISOU 2120 C LYS A1083 13156 15051 9082 2497 162 -497 C ATOM 2121 O LYS A1083 14.277 16.296 0.929 1.00 98.84 O ANISOU 2121 O LYS A1083 13117 15301 9136 2670 163 -576 O ATOM 2122 CB LYS A1083 12.612 17.240 -1.926 1.00 95.15 C ANISOU 2122 CB LYS A1083 12729 14596 8829 2158 205 -508 C ATOM 2123 CG LYS A1083 12.763 16.891 -3.417 1.00111.23 C ANISOU 2123 CG LYS A1083 14876 16539 10846 2092 242 -516 C ATOM 2124 CD LYS A1083 14.197 16.520 -3.835 1.00121.72 C ANISOU 2124 CD LYS A1083 16182 17953 12113 2274 284 -609 C ATOM 2125 CE LYS A1083 14.255 15.887 -5.210 1.00131.09 C ANISOU 2125 CE LYS A1083 17544 19006 13258 2227 328 -601 C ATOM 2126 NZ LYS A1083 13.715 14.499 -5.221 1.00139.75 N ANISOU 2126 NZ LYS A1083 18938 19913 14249 2270 337 -518 N ATOM 2127 N LEU A1084 12.070 16.097 1.387 1.00 94.05 N ANISOU 2127 N LEU A1084 12704 14455 8576 2427 135 -421 N ATOM 2128 CA LEU A1084 12.236 16.110 2.845 1.00 93.93 C ANISOU 2128 CA LEU A1084 12636 14518 8535 2552 105 -425 C ATOM 2129 C LEU A1084 12.134 14.848 3.723 1.00 98.29 C ANISOU 2129 C LEU A1084 13408 14972 8965 2714 96 -379 C ATOM 2130 O LEU A1084 12.404 14.891 4.923 1.00 97.97 O ANISOU 2130 O LEU A1084 13315 15012 8897 2834 69 -391 O ATOM 2131 CB LEU A1084 11.137 17.090 3.260 1.00 92.75 C ANISOU 2131 CB LEU A1084 12387 14363 8493 2353 90 -379 C ATOM 2132 CG LEU A1084 9.832 16.471 3.766 1.00 97.20 C ANISOU 2132 CG LEU A1084 13125 14771 9036 2266 80 -277 C ATOM 2133 CD1 LEU A1084 9.033 17.484 4.571 1.00 96.39 C ANISOU 2133 CD1 LEU A1084 12884 14716 9026 2148 67 -246 C ATOM 2134 CD2 LEU A1084 9.009 15.931 2.607 1.00 99.52 C ANISOU 2134 CD2 LEU A1084 13580 14916 9318 2112 97 -217 C ATOM 2135 N LYS A1085 11.743 13.736 3.107 1.00 95.26 N ANISOU 2135 N LYS A1085 13287 14410 8499 2708 124 -327 N ATOM 2136 CA LYS A1085 11.553 12.441 3.773 1.00 96.08 C ANISOU 2136 CA LYS A1085 13666 14375 8464 2839 134 -278 C ATOM 2137 C LYS A1085 12.851 11.874 4.408 1.00101.21 C ANISOU 2137 C LYS A1085 14330 15122 9003 3162 131 -330 C ATOM 2138 O LYS A1085 12.716 11.165 5.407 1.00101.65 O ANISOU 2138 O LYS A1085 14544 15114 8963 3286 123 -296 O ATOM 2139 CB LYS A1085 11.042 11.362 2.795 1.00 99.01 C ANISOU 2139 CB LYS A1085 14338 14536 8747 2763 181 -227 C ATOM 2140 CG LYS A1085 10.430 10.143 3.475 1.00112.27 C ANISOU 2140 CG LYS A1085 16339 16033 10287 2801 203 -162 C ATOM 2141 CD LYS A1085 10.375 8.950 2.533 1.00123.07 C ANISOU 2141 CD LYS A1085 18033 17208 11522 2799 266 -134 C ATOM 2142 CE LYS A1085 10.033 7.651 3.230 1.00133.94 C ANISOU 2142 CE LYS A1085 19769 18399 12722 2883 305 -85 C ATOM 2143 NZ LYS A1085 8.600 7.572 3.617 1.00141.83 N ANISOU 2143 NZ LYS A1085 20867 19294 13729 2620 300 -21 N ATOM 2144 N PRO A1086 14.097 12.186 3.923 1.00 97.93 N ANISOU 2144 N PRO A1086 13745 14873 8591 3305 137 -410 N ATOM 2145 CA PRO A1086 15.298 11.649 4.601 1.00 99.09 C ANISOU 2145 CA PRO A1086 13881 15147 8622 3628 128 -453 C ATOM 2146 C PRO A1086 15.682 12.627 5.721 1.00101.80 C ANISOU 2146 C PRO A1086 13944 15714 9022 3657 70 -501 C ATOM 2147 O PRO A1086 16.527 12.302 6.554 1.00102.32 O ANISOU 2147 O PRO A1086 13972 15910 8995 3904 44 -529 O ATOM 2148 CB PRO A1086 16.374 11.582 3.514 1.00101.61 C ANISOU 2148 CB PRO A1086 14129 15560 8919 3738 166 -518 C ATOM 2149 CG PRO A1086 15.916 12.525 2.475 1.00104.60 C ANISOU 2149 CG PRO A1086 14376 15931 9438 3459 179 -535 C ATOM 2150 CD PRO A1086 14.422 12.418 2.463 1.00 99.13 C ANISOU 2150 CD PRO A1086 13852 15026 8786 3220 175 -446 C ATOM 2151 N VAL A1087 15.053 13.825 5.731 1.00 96.48 N ANISOU 2151 N VAL A1087 13083 15083 8491 3407 53 -508 N ATOM 2152 CA VAL A1087 15.252 14.882 6.727 1.00 95.52 C ANISOU 2152 CA VAL A1087 12717 15146 8431 3375 11 -550 C ATOM 2153 C VAL A1087 14.338 14.611 7.929 1.00 98.53 C ANISOU 2153 C VAL A1087 13227 15416 8795 3354 -14 -479 C ATOM 2154 O VAL A1087 14.821 14.582 9.060 1.00 98.71 O ANISOU 2154 O VAL A1087 13196 15549 8759 3503 -51 -498 O ATOM 2155 CB VAL A1087 15.044 16.310 6.146 1.00 98.05 C ANISOU 2155 CB VAL A1087 12807 15550 8895 3130 23 -592 C ATOM 2156 CG1 VAL A1087 15.431 17.379 7.166 1.00 97.60 C ANISOU 2156 CG1 VAL A1087 12516 15693 8875 3110 -6 -648 C ATOM 2157 CG2 VAL A1087 15.825 16.505 4.848 1.00 98.11 C ANISOU 2157 CG2 VAL A1087 12728 15631 8917 3124 58 -659 C ATOM 2158 N TYR A1088 13.027 14.408 7.672 1.00 93.90 N ANISOU 2158 N TYR A1088 12805 14621 8250 3163 6 -398 N ATOM 2159 CA TYR A1088 11.992 14.121 8.672 1.00 93.29 C ANISOU 2159 CA TYR A1088 12867 14418 8160 3101 -5 -327 C ATOM 2160 C TYR A1088 12.294 12.827 9.435 1.00 97.64 C ANISOU 2160 C TYR A1088 13662 14887 8550 3334 -9 -302 C ATOM 2161 O TYR A1088 12.105 12.785 10.651 1.00 97.43 O ANISOU 2161 O TYR A1088 13662 14866 8491 3388 -35 -286 O ATOM 2162 CB TYR A1088 10.615 14.052 7.983 1.00 93.78 C ANISOU 2162 CB TYR A1088 13052 14299 8281 2850 24 -252 C ATOM 2163 CG TYR A1088 9.453 13.691 8.885 1.00 95.72 C ANISOU 2163 CG TYR A1088 13448 14413 8508 2758 25 -178 C ATOM 2164 CD1 TYR A1088 8.754 14.674 9.580 1.00 96.67 C ANISOU 2164 CD1 TYR A1088 13413 14585 8731 2620 13 -160 C ATOM 2165 CD2 TYR A1088 8.999 12.379 8.975 1.00 97.59 C ANISOU 2165 CD2 TYR A1088 13997 14465 8617 2791 49 -126 C ATOM 2166 CE1 TYR A1088 7.649 14.353 10.370 1.00 97.27 C ANISOU 2166 CE1 TYR A1088 13619 14547 8792 2525 21 -93 C ATOM 2167 CE2 TYR A1088 7.913 12.043 9.782 1.00 98.50 C ANISOU 2167 CE2 TYR A1088 14255 14463 8708 2684 58 -65 C ATOM 2168 CZ TYR A1088 7.239 13.034 10.474 1.00104.38 C ANISOU 2168 CZ TYR A1088 14818 15277 9565 2552 42 -49 C ATOM 2169 OH TYR A1088 6.182 12.697 11.281 1.00104.31 O ANISOU 2169 OH TYR A1088 14942 15162 9529 2448 57 7 O ATOM 2170 N ASP A1089 12.759 11.780 8.720 1.00 94.59 N ANISOU 2170 N ASP A1089 13471 14415 8053 3476 22 -299 N ATOM 2171 CA ASP A1089 13.100 10.478 9.294 1.00 95.65 C ANISOU 2171 CA ASP A1089 13881 14450 8011 3723 33 -273 C ATOM 2172 C ASP A1089 14.353 10.527 10.173 1.00100.25 C ANISOU 2172 C ASP A1089 14326 15243 8522 4014 -12 -328 C ATOM 2173 O ASP A1089 14.403 9.828 11.190 1.00100.90 O ANISOU 2173 O ASP A1089 14577 15276 8486 4186 -26 -300 O ATOM 2174 CB ASP A1089 13.223 9.406 8.199 1.00 98.19 C ANISOU 2174 CB ASP A1089 14465 14611 8231 3784 94 -252 C ATOM 2175 CG ASP A1089 11.905 9.025 7.549 1.00106.40 C ANISOU 2175 CG ASP A1089 15725 15419 9284 3512 138 -185 C ATOM 2176 OD1 ASP A1089 10.912 8.822 8.286 1.00106.55 O ANISOU 2176 OD1 ASP A1089 15873 15323 9289 3390 137 -134 O ATOM 2177 OD2 ASP A1089 11.875 8.884 6.312 1.00112.39 O ANISOU 2177 OD2 ASP A1089 16532 16116 10055 3421 176 -186 O ATOM 2178 N SER A1090 15.348 11.362 9.800 1.00 96.14 N ANISOU 2178 N SER A1090 13500 14966 8064 4061 -35 -407 N ATOM 2179 CA SER A1090 16.589 11.537 10.564 1.00 96.70 C ANISOU 2179 CA SER A1090 13382 15292 8066 4311 -83 -470 C ATOM 2180 C SER A1090 16.351 12.309 11.874 1.00 98.76 C ANISOU 2180 C SER A1090 13495 15658 8372 4245 -139 -477 C ATOM 2181 O SER A1090 17.121 12.147 12.824 1.00 99.54 O ANISOU 2181 O SER A1090 13535 15912 8374 4463 -186 -501 O ATOM 2182 CB SER A1090 17.665 12.211 9.717 1.00100.42 C ANISOU 2182 CB SER A1090 13572 15999 8584 4338 -81 -559 C ATOM 2183 OG SER A1090 17.275 13.510 9.301 1.00107.37 O ANISOU 2183 OG SER A1090 14227 16942 9628 4047 -79 -595 O ATOM 2184 N LEU A1091 15.242 13.049 11.879 1.00 92.78 N ANISOU 2184 N LEU A1091 12706 14800 7747 3953 -127 -447 N ATOM 2185 CA LEU A1091 14.790 13.856 13.000 1.00 91.41 C ANISOU 2185 CA LEU A1091 12418 14680 7634 3839 -160 -444 C ATOM 2186 C LEU A1091 13.992 13.077 14.047 1.00 94.47 C ANISOU 2186 C LEU A1091 13065 14884 7946 3878 -164 -370 C ATOM 2187 O LEU A1091 12.973 12.446 13.766 1.00 93.35 O ANISOU 2187 O LEU A1091 13162 14508 7798 3771 -124 -303 O ATOM 2188 CB LEU A1091 13.966 15.045 12.499 1.00 89.66 C ANISOU 2188 CB LEU A1091 12046 14439 7583 3528 -135 -443 C ATOM 2189 CG LEU A1091 14.722 16.103 11.693 1.00 93.91 C ANISOU 2189 CG LEU A1091 12307 15174 8201 3451 -128 -527 C ATOM 2190 CD1 LEU A1091 13.779 17.202 11.228 1.00 92.46 C ANISOU 2190 CD1 LEU A1091 12032 14932 8168 3160 -95 -510 C ATOM 2191 CD2 LEU A1091 15.868 16.683 12.508 1.00 96.79 C ANISOU 2191 CD2 LEU A1091 12444 15812 8520 3569 -171 -609 C ATOM 2192 N ASP A1092 14.510 13.160 15.260 1.00 91.40 N ANISOU 2192 N ASP A1092 12616 14621 7490 4024 -213 -391 N ATOM 2193 CA ASP A1092 13.950 12.626 16.528 1.00 91.43 C ANISOU 2193 CA ASP A1092 12820 14502 7416 4078 -228 -338 C ATOM 2194 C ASP A1092 12.699 13.319 16.776 1.00 92.98 C ANISOU 2194 C ASP A1092 13003 14585 7740 3792 -202 -300 C ATOM 2195 O ASP A1092 12.250 14.211 15.956 1.00 91.67 O ANISOU 2195 O ASP A1092 12678 14435 7718 3566 -174 -308 O ATOM 2196 CB ASP A1092 14.602 13.231 17.642 1.00 93.73 C ANISOU 2196 CB ASP A1092 12929 14999 7684 4163 -287 -382 C ATOM 2197 N ALA A1093 11.986 12.916 17.816 1.00 88.56 N ANISOU 2197 N ALA A1093 12626 13890 7132 3782 -200 -250 N ATOM 2198 CA ALA A1093 10.662 13.476 18.035 1.00 86.50 C ANISOU 2198 CA ALA A1093 12372 13507 6986 3511 -164 -203 C ATOM 2199 C ALA A1093 10.239 14.933 18.080 1.00 88.18 C ANISOU 2199 C ALA A1093 12325 13819 7362 3288 -155 -219 C ATOM 2200 O ALA A1093 9.398 15.389 17.306 1.00 86.27 O ANISOU 2200 O ALA A1093 12038 13509 7231 3080 -114 -190 O ATOM 2201 CB ALA A1093 10.132 13.029 19.387 1.00 87.73 C ANISOU 2201 CB ALA A1093 12714 13553 7066 3543 -167 -164 C ATOM 2202 N VAL A1094 10.851 15.649 19.009 1.00 84.96 N ANISOU 2202 N VAL A1094 11755 13574 6952 3341 -191 -263 N ATOM 2203 CA VAL A1094 10.683 17.096 19.184 1.00 83.47 C ANISOU 2203 CA VAL A1094 11328 13499 6890 3160 -176 -290 C ATOM 2204 C VAL A1094 10.977 18.000 17.955 1.00 86.64 C ANISOU 2204 C VAL A1094 11518 14006 7395 3043 -154 -334 C ATOM 2205 O VAL A1094 10.397 19.122 17.929 1.00 85.24 O ANISOU 2205 O VAL A1094 11217 13838 7331 2849 -115 -329 O ATOM 2206 CB VAL A1094 11.778 17.544 20.171 1.00 87.91 C ANISOU 2206 CB VAL A1094 11745 14271 7383 3287 -229 -357 C ATOM 2207 CG1 VAL A1094 12.541 18.735 19.611 1.00 87.32 C ANISOU 2207 CG1 VAL A1094 11391 14412 7377 3203 -227 -436 C ATOM 2208 CG2 VAL A1094 11.169 17.881 21.523 1.00 87.40 C ANISOU 2208 CG2 VAL A1094 11733 14154 7320 3220 -224 -327 C ATOM 2209 N ARG A1095 12.049 17.679 17.229 1.00 83.72 N ANISOU 2209 N ARG A1095 11084 13754 6971 3181 -180 -389 N ATOM 2210 CA ARG A1095 12.582 18.442 16.053 1.00 82.85 C ANISOU 2210 CA ARG A1095 10780 13766 6934 3099 -162 -448 C ATOM 2211 C ARG A1095 11.747 18.059 14.852 1.00 86.11 C ANISOU 2211 C ARG A1095 11308 14002 7408 2991 -121 -393 C ATOM 2212 O ARG A1095 11.639 18.796 13.897 1.00 84.83 O ANISOU 2212 O ARG A1095 11029 13865 7336 2852 -91 -411 O ATOM 2213 CB ARG A1095 14.014 17.940 15.972 1.00 83.77 C ANISOU 2213 CB ARG A1095 10827 14066 6937 3332 -208 -518 C ATOM 2214 CG ARG A1095 15.054 18.945 16.349 1.00 91.31 C ANISOU 2214 CG ARG A1095 11520 15292 7882 3328 -231 -613 C ATOM 2215 CD ARG A1095 16.380 18.267 16.614 1.00 99.18 C ANISOU 2215 CD ARG A1095 12462 16487 8736 3596 -289 -668 C ATOM 2216 NE ARG A1095 17.481 18.920 15.918 1.00104.44 N ANISOU 2216 NE ARG A1095 12880 17401 9402 3586 -287 -768 N ATOM 2217 CZ ARG A1095 18.627 18.324 15.621 1.00117.71 C ANISOU 2217 CZ ARG A1095 14489 19258 10979 3807 -320 -818 C ATOM 2218 NH1 ARG A1095 18.816 17.066 15.968 1.00106.12 N ANISOU 2218 NH1 ARG A1095 13196 17732 9394 4071 -354 -771 N ATOM 2219 NH2 ARG A1095 19.582 18.981 14.984 1.00102.81 N ANISOU 2219 NH2 ARG A1095 12364 17606 9095 3768 -310 -914 N ATOM 2220 N ARG A1096 11.148 16.879 14.955 1.00 83.38 N ANISOU 2220 N ARG A1096 11210 13475 6997 3052 -120 -327 N ATOM 2221 CA ARG A1096 10.280 16.297 13.936 1.00 82.90 C ANISOU 2221 CA ARG A1096 11304 13235 6961 2945 -84 -267 C ATOM 2222 C ARG A1096 8.977 17.110 13.939 1.00 85.78 C ANISOU 2222 C ARG A1096 11619 13524 7449 2698 -49 -213 C ATOM 2223 O ARG A1096 8.472 17.457 12.871 1.00 84.37 O ANISOU 2223 O ARG A1096 11398 13310 7349 2552 -23 -193 O ATOM 2224 CB ARG A1096 9.999 14.823 14.276 1.00 84.09 C ANISOU 2224 CB ARG A1096 11758 13214 6979 3067 -83 -216 C ATOM 2225 CG ARG A1096 9.739 13.937 13.071 1.00 93.87 C ANISOU 2225 CG ARG A1096 13174 14313 8179 3042 -52 -186 C ATOM 2226 CD ARG A1096 9.001 12.665 13.446 1.00104.98 C ANISOU 2226 CD ARG A1096 14912 15506 9469 3057 -27 -122 C ATOM 2227 NE ARG A1096 9.906 11.625 13.933 1.00117.89 N ANISOU 2227 NE ARG A1096 16728 17124 10940 3337 -40 -139 N ATOM 2228 CZ ARG A1096 10.418 10.656 13.181 1.00135.44 C ANISOU 2228 CZ ARG A1096 19132 19275 13054 3475 -17 -140 C ATOM 2229 NH1 ARG A1096 11.236 9.757 13.712 1.00125.75 N ANISOU 2229 NH1 ARG A1096 18070 18040 11669 3758 -26 -150 N ATOM 2230 NH2 ARG A1096 10.115 10.575 11.890 1.00121.85 N ANISOU 2230 NH2 ARG A1096 17438 17487 11373 3340 18 -130 N ATOM 2231 N ALA A1097 8.460 17.436 15.145 1.00 82.63 N ANISOU 2231 N ALA A1097 11222 13111 7061 2663 -48 -188 N ATOM 2232 CA ALA A1097 7.239 18.221 15.351 1.00 81.48 C ANISOU 2232 CA ALA A1097 11027 12910 7022 2461 -8 -132 C ATOM 2233 C ALA A1097 7.417 19.674 14.916 1.00 84.16 C ANISOU 2233 C ALA A1097 11130 13373 7473 2354 13 -168 C ATOM 2234 O ALA A1097 6.454 20.282 14.447 1.00 83.03 O ANISOU 2234 O ALA A1097 10942 13183 7422 2193 52 -119 O ATOM 2235 CB ALA A1097 6.807 18.155 16.809 1.00 82.46 C ANISOU 2235 CB ALA A1097 11224 12993 7115 2478 -7 -106 C ATOM 2236 N ALA A1098 8.644 20.224 15.062 1.00 80.68 N ANISOU 2236 N ALA A1098 10546 13098 7012 2442 -7 -254 N ATOM 2237 CA ALA A1098 8.982 21.594 14.665 1.00 79.80 C ANISOU 2237 CA ALA A1098 10234 13107 6979 2339 23 -305 C ATOM 2238 C ALA A1098 8.862 21.778 13.144 1.00 82.88 C ANISOU 2238 C ALA A1098 10586 13475 7428 2253 44 -305 C ATOM 2239 O ALA A1098 8.420 22.837 12.692 1.00 81.52 O ANISOU 2239 O ALA A1098 10322 13311 7343 2114 88 -296 O ATOM 2240 CB ALA A1098 10.385 21.948 15.132 1.00 81.29 C ANISOU 2240 CB ALA A1098 10292 13491 7103 2445 -7 -406 C ATOM 2241 N LEU A1099 9.228 20.735 12.365 1.00 79.94 N ANISOU 2241 N LEU A1099 10306 13065 7001 2342 17 -309 N ATOM 2242 CA LEU A1099 9.138 20.727 10.904 1.00 79.42 C ANISOU 2242 CA LEU A1099 10236 12964 6976 2269 33 -307 C ATOM 2243 C LEU A1099 7.668 20.664 10.457 1.00 82.69 C ANISOU 2243 C LEU A1099 10736 13230 7453 2112 57 -207 C ATOM 2244 O LEU A1099 7.324 21.255 9.433 1.00 81.73 O ANISOU 2244 O LEU A1099 10552 13103 7400 1995 80 -196 O ATOM 2245 CB LEU A1099 9.947 19.558 10.313 1.00 80.34 C ANISOU 2245 CB LEU A1099 10452 13072 7000 2419 7 -336 C ATOM 2246 CG LEU A1099 10.246 19.616 8.810 1.00 84.76 C ANISOU 2246 CG LEU A1099 10985 13633 7588 2369 24 -362 C ATOM 2247 CD1 LEU A1099 11.519 20.401 8.529 1.00 85.18 C ANISOU 2247 CD1 LEU A1099 10845 13876 7645 2412 29 -470 C ATOM 2248 CD2 LEU A1099 10.366 18.223 8.232 1.00 87.65 C ANISOU 2248 CD2 LEU A1099 11547 13891 7866 2471 15 -338 C ATOM 2249 N ILE A1100 6.805 19.957 11.229 1.00 79.25 N ANISOU 2249 N ILE A1100 10439 12687 6986 2108 52 -138 N ATOM 2250 CA ILE A1100 5.363 19.845 10.964 1.00 78.45 C ANISOU 2250 CA ILE A1100 10405 12475 6928 1954 74 -44 C ATOM 2251 C ILE A1100 4.723 21.222 11.218 1.00 81.33 C ANISOU 2251 C ILE A1100 10613 12891 7397 1842 111 -19 C ATOM 2252 O ILE A1100 3.874 21.653 10.433 1.00 80.53 O ANISOU 2252 O ILE A1100 10471 12769 7359 1716 131 34 O ATOM 2253 CB ILE A1100 4.697 18.693 11.783 1.00 82.08 C ANISOU 2253 CB ILE A1100 11063 12816 7307 1973 68 10 C ATOM 2254 CG1 ILE A1100 5.386 17.338 11.498 1.00 83.36 C ANISOU 2254 CG1 ILE A1100 11416 12911 7346 2103 45 -14 C ATOM 2255 CG2 ILE A1100 3.182 18.597 11.513 1.00 82.49 C ANISOU 2255 CG2 ILE A1100 11161 12787 7395 1790 92 102 C ATOM 2256 CD1 ILE A1100 5.280 16.302 12.610 1.00 90.92 C ANISOU 2256 CD1 ILE A1100 12576 13776 8192 2199 39 4 C ATOM 2257 N ASN A1101 5.189 21.934 12.277 1.00 77.53 N ANISOU 2257 N ASN A1101 10051 12485 6923 1894 122 -59 N ATOM 2258 CA ASN A1101 4.745 23.287 12.635 1.00 76.63 C ANISOU 2258 CA ASN A1101 9813 12413 6889 1810 172 -45 C ATOM 2259 C ASN A1101 5.114 24.265 11.518 1.00 79.82 C ANISOU 2259 C ASN A1101 10100 12880 7347 1749 197 -82 C ATOM 2260 O ASN A1101 4.416 25.257 11.309 1.00 78.96 O ANISOU 2260 O ASN A1101 9929 12768 7307 1658 247 -41 O ATOM 2261 CB ASN A1101 5.363 23.732 13.970 1.00 77.73 C ANISOU 2261 CB ASN A1101 9916 12618 6999 1878 178 -94 C ATOM 2262 CG ASN A1101 4.835 25.043 14.523 1.00100.43 C ANISOU 2262 CG ASN A1101 12710 15511 9938 1793 244 -73 C ATOM 2263 OD1 ASN A1101 3.661 25.408 14.354 1.00 95.90 O ANISOU 2263 OD1 ASN A1101 12136 14875 9426 1706 286 9 O ATOM 2264 ND2 ASN A1101 5.687 25.767 15.233 1.00 91.21 N ANISOU 2264 ND2 ASN A1101 11477 14434 8745 1819 259 -145 N ATOM 2265 N MET A1102 6.201 23.958 10.792 1.00 76.61 N ANISOU 2265 N MET A1102 9677 12528 6902 1809 169 -157 N ATOM 2266 CA MET A1102 6.717 24.705 9.648 1.00 76.16 C ANISOU 2266 CA MET A1102 9531 12527 6879 1756 191 -208 C ATOM 2267 C MET A1102 5.876 24.393 8.389 1.00 79.78 C ANISOU 2267 C MET A1102 10040 12899 7374 1672 187 -139 C ATOM 2268 O MET A1102 5.661 25.286 7.564 1.00 78.91 O ANISOU 2268 O MET A1102 9868 12800 7317 1587 221 -135 O ATOM 2269 CB MET A1102 8.188 24.322 9.417 1.00 79.09 C ANISOU 2269 CB MET A1102 9868 12999 7184 1861 162 -314 C ATOM 2270 CG MET A1102 9.066 25.463 9.011 1.00 82.59 C ANISOU 2270 CG MET A1102 10181 13561 7640 1813 200 -407 C ATOM 2271 SD MET A1102 10.630 24.825 8.376 1.00 87.63 S ANISOU 2271 SD MET A1102 10773 14321 8203 1926 167 -519 S ATOM 2272 CE MET A1102 11.720 25.306 9.665 1.00 84.90 C ANISOU 2272 CE MET A1102 10309 14160 7790 1992 161 -613 C ATOM 2273 N VAL A1103 5.402 23.124 8.255 1.00 76.41 N ANISOU 2273 N VAL A1103 9740 12386 6906 1690 149 -87 N ATOM 2274 CA VAL A1103 4.590 22.622 7.134 1.00 75.89 C ANISOU 2274 CA VAL A1103 9742 12242 6850 1596 138 -21 C ATOM 2275 C VAL A1103 3.212 23.297 7.080 1.00 78.89 C ANISOU 2275 C VAL A1103 10074 12604 7297 1475 164 73 C ATOM 2276 O VAL A1103 2.838 23.797 6.022 1.00 78.26 O ANISOU 2276 O VAL A1103 9949 12528 7256 1394 172 100 O ATOM 2277 CB VAL A1103 4.524 21.058 7.078 1.00 80.40 C ANISOU 2277 CB VAL A1103 10493 12723 7334 1637 103 0 C ATOM 2278 CG1 VAL A1103 3.404 20.554 6.166 1.00 80.24 C ANISOU 2278 CG1 VAL A1103 10552 12625 7312 1498 96 83 C ATOM 2279 CG2 VAL A1103 5.858 20.462 6.641 1.00 80.69 C ANISOU 2279 CG2 VAL A1103 10573 12781 7306 1761 86 -84 C ATOM 2280 N PHE A1104 2.476 23.340 8.209 1.00 75.22 N ANISOU 2280 N PHE A1104 9614 12126 6840 1471 178 124 N ATOM 2281 CA PHE A1104 1.143 23.955 8.279 1.00 74.77 C ANISOU 2281 CA PHE A1104 9498 12070 6840 1377 208 218 C ATOM 2282 C PHE A1104 1.144 25.448 7.896 1.00 76.26 C ANISOU 2282 C PHE A1104 9564 12314 7097 1358 257 216 C ATOM 2283 O PHE A1104 0.135 25.956 7.401 1.00 76.06 O ANISOU 2283 O PHE A1104 9488 12300 7112 1291 276 295 O ATOM 2284 CB PHE A1104 0.511 23.744 9.667 1.00 77.18 C ANISOU 2284 CB PHE A1104 9835 12355 7136 1390 226 259 C ATOM 2285 CG PHE A1104 -0.998 23.631 9.657 1.00 79.51 C ANISOU 2285 CG PHE A1104 10118 12642 7451 1286 239 366 C ATOM 2286 CD1 PHE A1104 -1.618 22.389 9.599 1.00 83.62 C ANISOU 2286 CD1 PHE A1104 10752 13112 7909 1218 209 405 C ATOM 2287 CD2 PHE A1104 -1.798 24.767 9.728 1.00 81.80 C ANISOU 2287 CD2 PHE A1104 10289 12982 7808 1256 288 426 C ATOM 2288 CE1 PHE A1104 -3.014 22.284 9.595 1.00 85.00 C ANISOU 2288 CE1 PHE A1104 10897 13310 8091 1103 222 498 C ATOM 2289 CE2 PHE A1104 -3.193 24.662 9.721 1.00 85.15 C ANISOU 2289 CE2 PHE A1104 10678 13431 8244 1171 299 527 C ATOM 2290 CZ PHE A1104 -3.791 23.422 9.657 1.00 83.87 C ANISOU 2290 CZ PHE A1104 10604 13240 8021 1086 264 559 C ATOM 2291 N GLN A1105 2.289 26.126 8.087 1.00 70.68 N ANISOU 2291 N GLN A1105 8816 11649 6389 1416 280 123 N ATOM 2292 CA GLN A1105 2.487 27.542 7.792 1.00 69.38 C ANISOU 2292 CA GLN A1105 8572 11524 6265 1395 340 100 C ATOM 2293 C GLN A1105 2.805 27.805 6.313 1.00 72.64 C ANISOU 2293 C GLN A1105 8972 11942 6687 1351 335 75 C ATOM 2294 O GLN A1105 2.191 28.688 5.712 1.00 71.96 O ANISOU 2294 O GLN A1105 8853 11852 6636 1305 374 124 O ATOM 2295 CB GLN A1105 3.601 28.099 8.700 1.00 70.41 C ANISOU 2295 CB GLN A1105 8676 11707 6369 1447 371 1 C ATOM 2296 CG GLN A1105 3.903 29.591 8.528 1.00 77.73 C ANISOU 2296 CG GLN A1105 9554 12667 7315 1408 451 -38 C ATOM 2297 CD GLN A1105 5.153 30.061 9.245 1.00 91.10 C ANISOU 2297 CD GLN A1105 11218 14435 8960 1427 476 -153 C ATOM 2298 OE1 GLN A1105 5.388 31.264 9.391 1.00 85.24 O ANISOU 2298 OE1 GLN A1105 10461 13712 8212 1381 554 -189 O ATOM 2299 NE2 GLN A1105 5.995 29.135 9.697 1.00 81.75 N ANISOU 2299 NE2 GLN A1105 10033 13302 7728 1494 415 -215 N ATOM 2300 N MET A1106 3.773 27.062 5.742 1.00 69.13 N ANISOU 2300 N MET A1106 8560 11505 6204 1375 293 1 N ATOM 2301 CA MET A1106 4.255 27.256 4.368 1.00 68.71 C ANISOU 2301 CA MET A1106 8502 11453 6150 1335 292 -40 C ATOM 2302 C MET A1106 3.706 26.279 3.324 1.00 72.32 C ANISOU 2302 C MET A1106 9028 11855 6597 1288 240 17 C ATOM 2303 O MET A1106 3.470 26.682 2.185 1.00 71.56 O ANISOU 2303 O MET A1106 8925 11745 6517 1223 245 36 O ATOM 2304 CB MET A1106 5.797 27.259 4.319 1.00 71.23 C ANISOU 2304 CB MET A1106 8798 11836 6430 1387 296 -172 C ATOM 2305 CG MET A1106 6.450 28.114 5.387 1.00 74.87 C ANISOU 2305 CG MET A1106 9194 12372 6879 1415 342 -241 C ATOM 2306 SD MET A1106 8.238 28.235 5.172 1.00 79.53 S ANISOU 2306 SD MET A1106 9722 13084 7413 1449 349 -401 S ATOM 2307 CE MET A1106 8.331 29.695 4.182 1.00 76.10 C ANISOU 2307 CE MET A1106 9263 12650 7001 1329 431 -440 C ATOM 2308 N GLY A1107 3.556 25.012 3.705 1.00 69.36 N ANISOU 2308 N GLY A1107 8734 11441 6179 1316 195 40 N ATOM 2309 CA GLY A1107 3.096 23.946 2.821 1.00 69.61 C ANISOU 2309 CA GLY A1107 8864 11411 6175 1258 152 86 C ATOM 2310 C GLY A1107 4.261 23.128 2.303 1.00 74.36 C ANISOU 2310 C GLY A1107 9542 11992 6720 1321 135 4 C ATOM 2311 O GLY A1107 5.365 23.661 2.162 1.00 73.75 O ANISOU 2311 O GLY A1107 9403 11970 6647 1378 156 -89 O ATOM 2312 N GLU A1108 4.026 21.826 2.021 1.00 72.23 N ANISOU 2312 N GLU A1108 9415 11646 6385 1308 104 35 N ATOM 2313 CA GLU A1108 5.021 20.865 1.514 1.00 73.00 C ANISOU 2313 CA GLU A1108 9623 11704 6411 1383 95 -28 C ATOM 2314 C GLU A1108 6.020 21.255 0.422 1.00 77.91 C ANISOU 2314 C GLU A1108 10204 12355 7042 1398 111 -107 C ATOM 2315 O GLU A1108 7.118 20.705 0.385 1.00 78.28 O ANISOU 2315 O GLU A1108 10291 12415 7037 1513 116 -181 O ATOM 2316 CB GLU A1108 4.335 19.673 0.816 1.00 74.99 C ANISOU 2316 CB GLU A1108 10051 11848 6594 1296 75 35 C ATOM 2317 CG GLU A1108 3.988 18.512 1.730 1.00 86.97 C ANISOU 2317 CG GLU A1108 11723 13293 8029 1333 67 69 C ATOM 2318 CD GLU A1108 3.180 17.406 1.076 1.00109.81 C ANISOU 2318 CD GLU A1108 14805 16079 10839 1205 60 133 C ATOM 2319 OE1 GLU A1108 2.064 17.122 1.570 1.00105.84 O ANISOU 2319 OE1 GLU A1108 14340 15557 10318 1100 53 204 O ATOM 2320 OE2 GLU A1108 3.658 16.820 0.075 1.00104.56 O ANISOU 2320 OE2 GLU A1108 14256 15353 10120 1199 66 108 O ATOM 2321 N THR A1109 5.649 22.231 -0.429 1.00 74.55 N ANISOU 2321 N THR A1109 9698 11949 6677 1291 124 -92 N ATOM 2322 CA THR A1109 6.449 22.733 -1.551 1.00 74.53 C ANISOU 2322 CA THR A1109 9664 11967 6688 1273 147 -162 C ATOM 2323 C THR A1109 7.280 23.906 -1.006 1.00 78.92 C ANISOU 2323 C THR A1109 10075 12628 7281 1324 187 -249 C ATOM 2324 O THR A1109 8.443 24.049 -1.387 1.00 78.90 O ANISOU 2324 O THR A1109 10038 12680 7260 1370 211 -350 O ATOM 2325 CB THR A1109 5.601 23.078 -2.790 1.00 81.86 C ANISOU 2325 CB THR A1109 10613 12848 7641 1129 140 -99 C ATOM 2326 OG1 THR A1109 4.845 21.926 -3.172 1.00 81.04 O ANISOU 2326 OG1 THR A1109 10646 12661 7485 1063 103 -23 O ATOM 2327 CG2 THR A1109 6.443 23.543 -3.980 1.00 80.82 C ANISOU 2327 CG2 THR A1109 10472 12720 7514 1104 168 -175 C ATOM 2328 N GLY A1110 6.686 24.705 -0.120 1.00 75.70 N ANISOU 2328 N GLY A1110 9592 12255 6916 1309 200 -212 N ATOM 2329 CA GLY A1110 7.337 25.864 0.486 1.00 75.67 C ANISOU 2329 CA GLY A1110 9475 12341 6934 1331 246 -286 C ATOM 2330 C GLY A1110 8.547 25.525 1.337 1.00 80.26 C ANISOU 2330 C GLY A1110 10014 13012 7468 1448 245 -382 C ATOM 2331 O GLY A1110 9.640 26.048 1.100 1.00 80.02 O ANISOU 2331 O GLY A1110 9912 13071 7421 1458 277 -489 O ATOM 2332 N VAL A1111 8.359 24.626 2.321 1.00 77.20 N ANISOU 2332 N VAL A1111 9673 12609 7049 1535 207 -347 N ATOM 2333 CA VAL A1111 9.406 24.166 3.243 1.00 77.61 C ANISOU 2333 CA VAL A1111 9695 12750 7042 1671 193 -421 C ATOM 2334 C VAL A1111 10.515 23.347 2.560 1.00 82.20 C ANISOU 2334 C VAL A1111 10305 13366 7562 1766 181 -494 C ATOM 2335 O VAL A1111 11.657 23.382 3.019 1.00 82.25 O ANISOU 2335 O VAL A1111 10226 13503 7523 1867 183 -585 O ATOM 2336 CB VAL A1111 8.848 23.464 4.510 1.00 81.68 C ANISOU 2336 CB VAL A1111 10274 13227 7532 1743 160 -358 C ATOM 2337 CG1 VAL A1111 8.190 24.468 5.448 1.00 81.05 C ANISOU 2337 CG1 VAL A1111 10127 13167 7503 1683 186 -324 C ATOM 2338 CG2 VAL A1111 7.885 22.332 4.156 1.00 81.55 C ANISOU 2338 CG2 VAL A1111 10417 13073 7497 1720 130 -262 C ATOM 2339 N ALA A1112 10.182 22.641 1.454 1.00 78.81 N ANISOU 2339 N ALA A1112 9990 12831 7125 1732 173 -454 N ATOM 2340 CA ALA A1112 11.116 21.812 0.681 1.00 79.30 C ANISOU 2340 CA ALA A1112 10108 12897 7126 1820 174 -510 C ATOM 2341 C ALA A1112 12.063 22.616 -0.239 1.00 83.31 C ANISOU 2341 C ALA A1112 10506 13498 7650 1778 216 -612 C ATOM 2342 O ALA A1112 12.795 22.026 -1.040 1.00 83.40 O ANISOU 2342 O ALA A1112 10558 13512 7618 1836 228 -659 O ATOM 2343 CB ALA A1112 10.355 20.758 -0.111 1.00 80.12 C ANISOU 2343 CB ALA A1112 10400 12839 7202 1779 159 -428 C ATOM 2344 N GLY A1113 12.050 23.940 -0.093 1.00 79.51 N ANISOU 2344 N GLY A1113 9901 13088 7221 1678 248 -648 N ATOM 2345 CA GLY A1113 12.914 24.853 -0.832 1.00 79.48 C ANISOU 2345 CA GLY A1113 9798 13176 7224 1611 299 -753 C ATOM 2346 C GLY A1113 14.043 25.398 0.022 1.00 84.15 C ANISOU 2346 C GLY A1113 10237 13961 7777 1666 319 -865 C ATOM 2347 O GLY A1113 14.763 26.299 -0.412 1.00 83.66 O ANISOU 2347 O GLY A1113 10082 13997 7710 1585 372 -963 O ATOM 2348 N PHE A1114 14.196 24.857 1.226 1.00 81.64 N ANISOU 2348 N PHE A1114 9897 13702 7420 1793 279 -853 N ATOM 2349 CA PHE A1114 15.246 25.299 2.137 1.00 82.28 C ANISOU 2349 CA PHE A1114 9826 13988 7450 1848 285 -954 C ATOM 2350 C PHE A1114 16.505 24.453 1.979 1.00 87.45 C ANISOU 2350 C PHE A1114 10423 14780 8023 2012 269 -1033 C ATOM 2351 O PHE A1114 17.565 24.797 2.503 1.00 87.88 O ANISOU 2351 O PHE A1114 10322 15048 8020 2056 275 -1134 O ATOM 2352 CB PHE A1114 14.755 25.247 3.585 1.00 83.93 C ANISOU 2352 CB PHE A1114 10036 14199 7653 1899 250 -899 C ATOM 2353 CG PHE A1114 13.956 26.449 3.998 1.00 84.71 C ANISOU 2353 CG PHE A1114 10122 14252 7810 1747 288 -867 C ATOM 2354 CD1 PHE A1114 14.544 27.474 4.720 1.00 88.17 C ANISOU 2354 CD1 PHE A1114 10444 14835 8221 1686 325 -949 C ATOM 2355 CD2 PHE A1114 12.616 26.555 3.664 1.00 86.10 C ANISOU 2355 CD2 PHE A1114 10406 14250 8057 1665 293 -753 C ATOM 2356 CE1 PHE A1114 13.811 28.582 5.102 1.00 88.54 C ANISOU 2356 CE1 PHE A1114 10508 14824 8310 1556 375 -916 C ATOM 2357 CE2 PHE A1114 11.878 27.660 4.042 1.00 88.40 C ANISOU 2357 CE2 PHE A1114 10691 14503 8395 1553 337 -717 C ATOM 2358 CZ PHE A1114 12.476 28.675 4.762 1.00 86.77 C ANISOU 2358 CZ PHE A1114 10393 14417 8161 1503 383 -797 C ATOM 2359 N SER A1117 19.771 24.708 4.308 1.00102.11 N ANISOU 2359 N SER A1117 11803 17349 9644 2287 227 -1305 N ATOM 2360 CA SER A1117 19.063 24.780 5.580 1.00101.33 C ANISOU 2360 CA SER A1117 11750 17196 9554 2296 188 -1234 C ATOM 2361 C SER A1117 18.351 23.468 5.890 1.00104.36 C ANISOU 2361 C SER A1117 12316 17401 9934 2468 132 -1114 C ATOM 2362 O SER A1117 17.737 23.318 6.946 1.00103.81 O ANISOU 2362 O SER A1117 12309 17271 9865 2499 98 -1048 O ATOM 2363 CB SER A1117 18.058 25.934 5.569 1.00103.76 C ANISOU 2363 CB SER A1117 12108 17366 9950 2066 236 -1197 C ATOM 2364 OG SER A1117 18.611 27.098 6.158 1.00113.30 O ANISOU 2364 OG SER A1117 13176 18749 11124 1938 273 -1290 O ATOM 2365 N LEU A1118 18.437 22.520 4.962 1.00100.38 N ANISOU 2365 N LEU A1118 11914 16808 9418 2570 133 -1089 N ATOM 2366 CA LEU A1118 17.799 21.213 5.135 1.00 99.78 C ANISOU 2366 CA LEU A1118 12047 16548 9317 2719 95 -982 C ATOM 2367 C LEU A1118 18.832 20.088 5.081 1.00104.46 C ANISOU 2367 C LEU A1118 12650 17244 9797 2982 75 -1013 C ATOM 2368 O LEU A1118 18.663 19.082 5.772 1.00104.38 O ANISOU 2368 O LEU A1118 12775 17166 9719 3161 37 -950 O ATOM 2369 CB LEU A1118 16.680 20.973 4.110 1.00 98.67 C ANISOU 2369 CB LEU A1118 12088 16151 9251 2594 120 -895 C ATOM 2370 CG LEU A1118 15.310 21.580 4.406 1.00101.81 C ANISOU 2370 CG LEU A1118 12549 16396 9738 2412 123 -810 C ATOM 2371 CD1 LEU A1118 14.427 21.506 3.184 1.00101.21 C ANISOU 2371 CD1 LEU A1118 12596 16134 9725 2275 147 -747 C ATOM 2372 CD2 LEU A1118 14.616 20.872 5.560 1.00104.07 C ANISOU 2372 CD2 LEU A1118 12956 16591 9995 2498 80 -724 C ATOM 2373 N ARG A1119 19.905 20.263 4.271 1.00101.59 N ANISOU 2373 N ARG A1119 12151 17045 9405 3012 108 -1111 N ATOM 2374 CA ARG A1119 21.005 19.297 4.151 1.00103.02 C ANISOU 2374 CA ARG A1119 12309 17360 9473 3278 100 -1149 C ATOM 2375 C ARG A1119 21.861 19.297 5.432 1.00107.70 C ANISOU 2375 C ARG A1119 12735 18217 9970 3449 46 -1198 C ATOM 2376 O ARG A1119 22.546 18.311 5.713 1.00108.96 O ANISOU 2376 O ARG A1119 12918 18463 10018 3725 21 -1194 O ATOM 2377 CB ARG A1119 21.846 19.531 2.870 1.00103.83 C ANISOU 2377 CB ARG A1119 12308 17565 9578 3245 159 -1240 C ATOM 2378 CG ARG A1119 22.726 20.787 2.861 1.00114.82 C ANISOU 2378 CG ARG A1119 13416 19236 10976 3105 183 -1375 C ATOM 2379 CD ARG A1119 22.787 21.462 1.495 1.00124.57 C ANISOU 2379 CD ARG A1119 14626 20426 12277 2903 256 -1433 C ATOM 2380 NE ARG A1119 23.525 20.682 0.496 1.00132.53 N ANISOU 2380 NE ARG A1119 15659 21462 13236 3048 293 -1466 N ATOM 2381 CZ ARG A1119 23.742 21.072 -0.758 1.00144.61 C ANISOU 2381 CZ ARG A1119 17178 22963 14805 2913 360 -1522 C ATOM 2382 NH1 ARG A1119 23.283 22.243 -1.186 1.00129.83 N ANISOU 2382 NH1 ARG A1119 15279 21034 13017 2633 396 -1553 N ATOM 2383 NH2 ARG A1119 24.421 20.297 -1.593 1.00131.91 N ANISOU 2383 NH2 ARG A1119 15600 21376 13144 3064 398 -1547 N ATOM 2384 N MET A1120 21.795 20.407 6.206 1.00103.03 N ANISOU 2384 N MET A1120 11987 17746 9412 3285 32 -1240 N ATOM 2385 CA MET A1120 22.491 20.617 7.479 1.00103.60 C ANISOU 2385 CA MET A1120 11892 18072 9398 3383 -21 -1288 C ATOM 2386 C MET A1120 21.683 19.979 8.620 1.00106.27 C ANISOU 2386 C MET A1120 12407 18253 9716 3487 -76 -1180 C ATOM 2387 O MET A1120 22.260 19.328 9.494 1.00107.19 O ANISOU 2387 O MET A1120 12502 18504 9722 3719 -131 -1178 O ATOM 2388 CB MET A1120 22.678 22.121 7.759 1.00105.33 C ANISOU 2388 CB MET A1120 11910 18455 9656 3123 4 -1378 C ATOM 2389 CG MET A1120 23.538 22.851 6.754 1.00109.46 C ANISOU 2389 CG MET A1120 12253 19155 10180 2995 64 -1500 C ATOM 2390 SD MET A1120 23.480 24.636 7.040 1.00112.84 S ANISOU 2390 SD MET A1120 12538 19685 10649 2647 116 -1590 S ATOM 2391 CE MET A1120 24.629 25.192 5.803 1.00110.50 C ANISOU 2391 CE MET A1120 12057 19605 10323 2541 190 -1739 C ATOM 2392 N LEU A1121 20.347 20.172 8.604 1.00100.58 N ANISOU 2392 N LEU A1121 11861 17258 9098 3317 -59 -1092 N ATOM 2393 CA LEU A1121 19.404 19.649 9.597 1.00 99.74 C ANISOU 2393 CA LEU A1121 11937 16972 8987 3364 -96 -989 C ATOM 2394 C LEU A1121 19.326 18.114 9.580 1.00104.53 C ANISOU 2394 C LEU A1121 12772 17437 9506 3614 -116 -915 C ATOM 2395 O LEU A1121 19.133 17.508 10.637 1.00104.69 O ANISOU 2395 O LEU A1121 12901 17420 9458 3753 -159 -864 O ATOM 2396 CB LEU A1121 18.011 20.273 9.385 1.00 97.78 C ANISOU 2396 CB LEU A1121 11795 16488 8869 3109 -60 -919 C ATOM 2397 CG LEU A1121 17.107 20.389 10.617 1.00101.43 C ANISOU 2397 CG LEU A1121 12342 16849 9349 3064 -85 -848 C ATOM 2398 CD1 LEU A1121 17.278 21.733 11.300 1.00100.90 C ANISOU 2398 CD1 LEU A1121 12092 16933 9313 2906 -74 -909 C ATOM 2399 CD2 LEU A1121 15.654 20.217 10.235 1.00102.51 C ANISOU 2399 CD2 LEU A1121 12670 16704 9574 2927 -58 -743 C ATOM 2400 N GLN A1122 19.490 17.490 8.394 1.00101.33 N ANISOU 2400 N GLN A1122 12459 16947 9094 3670 -79 -910 N ATOM 2401 CA GLN A1122 19.456 16.031 8.242 1.00102.20 C ANISOU 2401 CA GLN A1122 12820 16907 9106 3901 -78 -843 C ATOM 2402 C GLN A1122 20.779 15.351 8.622 1.00108.47 C ANISOU 2402 C GLN A1122 13539 17923 9752 4228 -106 -890 C ATOM 2403 O GLN A1122 20.765 14.226 9.122 1.00109.01 O ANISOU 2403 O GLN A1122 13814 17897 9707 4462 -122 -829 O ATOM 2404 CB GLN A1122 18.957 15.607 6.841 1.00102.88 C ANISOU 2404 CB GLN A1122 13076 16778 9236 3810 -19 -807 C ATOM 2405 CG GLN A1122 19.865 15.962 5.659 1.00115.55 C ANISOU 2405 CG GLN A1122 14524 18523 10858 3799 23 -893 C ATOM 2406 CD GLN A1122 20.841 14.858 5.327 1.00135.56 C ANISOU 2406 CD GLN A1122 17131 21117 13260 4101 39 -908 C ATOM 2407 OE1 GLN A1122 20.459 13.716 5.046 1.00131.40 O ANISOU 2407 OE1 GLN A1122 16888 20372 12666 4217 64 -832 O ATOM 2408 NE2 GLN A1122 22.125 15.180 5.344 1.00129.01 N ANISOU 2408 NE2 GLN A1122 16049 20589 12380 4230 33 -1006 N ATOM 2409 N GLN A1123 21.916 16.045 8.392 1.00106.11 N ANISOU 2409 N GLN A1123 12947 17927 9442 4244 -108 -999 N ATOM 2410 CA GLN A1123 23.279 15.581 8.680 1.00108.27 C ANISOU 2410 CA GLN A1123 13076 18486 9577 4542 -135 -1059 C ATOM 2411 C GLN A1123 23.578 15.592 10.196 1.00113.17 C ANISOU 2411 C GLN A1123 13613 19277 10109 4679 -214 -1058 C ATOM 2412 O GLN A1123 24.663 15.178 10.616 1.00114.83 O ANISOU 2412 O GLN A1123 13700 19744 10187 4949 -252 -1096 O ATOM 2413 CB GLN A1123 24.289 16.469 7.926 1.00110.03 C ANISOU 2413 CB GLN A1123 12991 18991 9826 4449 -106 -1185 C ATOM 2414 CG GLN A1123 25.592 15.768 7.532 1.00128.20 C ANISOU 2414 CG GLN A1123 15190 21521 11999 4751 -97 -1236 C ATOM 2415 CD GLN A1123 25.495 14.955 6.259 1.00147.57 C ANISOU 2415 CD GLN A1123 17847 23769 14455 4828 -25 -1201 C ATOM 2416 OE1 GLN A1123 24.930 15.388 5.247 1.00141.52 O ANISOU 2416 OE1 GLN A1123 17138 22831 13803 4583 30 -1204 O ATOM 2417 NE2 GLN A1123 26.104 13.777 6.266 1.00141.56 N ANISOU 2417 NE2 GLN A1123 17198 23032 13555 5179 -19 -1169 N ATOM 2418 N LYS A1124 22.596 16.053 11.005 1.00108.45 N ANISOU 2418 N LYS A1124 13088 18538 9579 4497 -238 -1010 N ATOM 2419 CA LYS A1124 22.621 16.206 12.467 1.00108.83 C ANISOU 2419 CA LYS A1124 13090 18693 9568 4555 -306 -1001 C ATOM 2420 C LYS A1124 23.556 17.350 12.896 1.00113.85 C ANISOU 2420 C LYS A1124 13371 19696 10191 4461 -337 -1116 C ATOM 2421 O LYS A1124 24.067 17.355 14.021 1.00114.50 O ANISOU 2421 O LYS A1124 13352 19977 10174 4584 -403 -1134 O ATOM 2422 CB LYS A1124 22.924 14.889 13.217 1.00113.06 C ANISOU 2422 CB LYS A1124 13806 19210 9943 4915 -351 -939 C ATOM 2423 CG LYS A1124 21.749 13.918 13.201 1.00125.52 C ANISOU 2423 CG LYS A1124 15771 20397 11524 4934 -321 -822 C ATOM 2424 CD LYS A1124 22.105 12.570 13.805 1.00136.29 C ANISOU 2424 CD LYS A1124 17355 21719 12709 5301 -347 -765 C ATOM 2425 CE LYS A1124 20.941 11.611 13.722 1.00144.30 C ANISOU 2425 CE LYS A1124 18775 22340 13713 5284 -302 -658 C ATOM 2426 NZ LYS A1124 21.281 10.281 14.286 1.00153.28 N ANISOU 2426 NZ LYS A1124 20172 23410 14658 5644 -312 -602 N ATOM 2427 N ARG A1125 23.724 18.355 12.000 1.00110.13 N ANISOU 2427 N ARG A1125 12727 19304 9814 4218 -284 -1195 N ATOM 2428 CA ARG A1125 24.513 19.565 12.233 1.00110.55 C ANISOU 2428 CA ARG A1125 12469 19677 9859 4054 -288 -1315 C ATOM 2429 C ARG A1125 23.484 20.542 12.816 1.00112.66 C ANISOU 2429 C ARG A1125 12788 19789 10229 3765 -274 -1287 C ATOM 2430 O ARG A1125 22.707 21.151 12.075 1.00110.22 O ANISOU 2430 O ARG A1125 12547 19286 10047 3529 -210 -1273 O ATOM 2431 CB ARG A1125 25.142 20.110 10.933 1.00111.19 C ANISOU 2431 CB ARG A1125 12386 19881 9980 3931 -222 -1411 C ATOM 2432 CG ARG A1125 26.300 19.277 10.386 1.00123.64 C ANISOU 2432 CG ARG A1125 13865 21666 11446 4214 -228 -1454 C ATOM 2433 CD ARG A1125 26.830 19.857 9.088 1.00133.76 C ANISOU 2433 CD ARG A1125 15002 23045 12777 4063 -153 -1550 C ATOM 2434 NE ARG A1125 28.294 19.810 9.019 1.00145.75 N ANISOU 2434 NE ARG A1125 16237 24971 14171 4221 -165 -1658 N ATOM 2435 CZ ARG A1125 28.986 18.986 8.238 1.00162.60 C ANISOU 2435 CZ ARG A1125 18360 27176 16245 4456 -141 -1669 C ATOM 2436 NH1 ARG A1125 30.313 19.018 8.242 1.00152.52 N ANISOU 2436 NH1 ARG A1125 16795 26305 14851 4594 -152 -1771 N ATOM 2437 NH2 ARG A1125 28.360 18.129 7.441 1.00148.65 N ANISOU 2437 NH2 ARG A1125 16870 25085 14526 4550 -99 -1579 N ATOM 2438 N TRP A1126 23.428 20.704 14.128 1.00109.98 N ANISOU 2438 N TRP A1126 12428 19524 9836 3784 -328 -1274 N ATOM 2439 CA TRP A1126 22.357 21.511 14.713 1.00108.32 C ANISOU 2439 CA TRP A1126 12306 19131 9720 3539 -305 -1233 C ATOM 2440 C TRP A1126 22.467 23.040 14.540 1.00110.95 C ANISOU 2440 C TRP A1126 12467 19579 10111 3222 -247 -1323 C ATOM 2441 O TRP A1126 21.593 23.638 13.934 1.00109.05 O ANISOU 2441 O TRP A1126 12318 19125 9991 3014 -179 -1294 O ATOM 2442 CB TRP A1126 22.125 21.141 16.180 1.00107.82 C ANISOU 2442 CB TRP A1126 12323 19059 9583 3655 -372 -1178 C ATOM 2443 CG TRP A1126 22.871 19.924 16.650 1.00110.93 C ANISOU 2443 CG TRP A1126 12740 19578 9830 4007 -448 -1160 C ATOM 2444 CD1 TRP A1126 22.344 18.701 16.929 1.00114.14 C ANISOU 2444 CD1 TRP A1126 13407 19764 10198 4225 -472 -1057 C ATOM 2445 CD2 TRP A1126 24.283 19.821 16.922 1.00113.09 C ANISOU 2445 CD2 TRP A1126 12774 20237 9960 4189 -505 -1246 C ATOM 2446 NE1 TRP A1126 23.334 17.839 17.347 1.00115.86 N ANISOU 2446 NE1 TRP A1126 13581 20184 10255 4549 -538 -1068 N ATOM 2447 CE2 TRP A1126 24.531 18.505 17.348 1.00118.61 C ANISOU 2447 CE2 TRP A1126 13609 20918 10540 4540 -564 -1182 C ATOM 2448 CE3 TRP A1126 25.360 20.718 16.842 1.00115.46 C ANISOU 2448 CE3 TRP A1126 12757 20903 10209 4083 -509 -1374 C ATOM 2449 CZ2 TRP A1126 25.800 18.065 17.689 1.00120.31 C ANISOU 2449 CZ2 TRP A1126 13644 21476 10593 4812 -630 -1232 C ATOM 2450 CZ3 TRP A1126 26.612 20.279 17.178 1.00119.25 C ANISOU 2450 CZ3 TRP A1126 13042 21738 10531 4328 -577 -1430 C ATOM 2451 CH2 TRP A1126 26.825 18.967 17.595 1.00121.32 C ANISOU 2451 CH2 TRP A1126 13433 21983 10681 4701 -640 -1356 C ATOM 2452 N ASP A1127 23.514 23.670 15.068 1.00108.09 N ANISOU 2452 N ASP A1127 11868 19551 9650 3183 -269 -1430 N ATOM 2453 CA ASP A1127 23.608 25.131 15.133 1.00107.02 C ANISOU 2453 CA ASP A1127 11606 19519 9538 2870 -208 -1517 C ATOM 2454 C ASP A1127 23.870 25.704 13.734 1.00109.33 C ANISOU 2454 C ASP A1127 11826 19825 9889 2711 -126 -1590 C ATOM 2455 O ASP A1127 23.534 26.866 13.492 1.00107.63 O ANISOU 2455 O ASP A1127 11610 19552 9730 2435 -48 -1629 O ATOM 2456 CB ASP A1127 24.629 25.640 16.161 1.00110.54 C ANISOU 2456 CB ASP A1127 11832 20326 9842 2842 -254 -1615 C ATOM 2457 CG ASP A1127 24.243 25.307 17.588 1.00120.51 C ANISOU 2457 CG ASP A1127 13187 21546 11054 2940 -323 -1544 C ATOM 2458 OD1 ASP A1127 23.612 26.160 18.245 1.00120.39 O ANISOU 2458 OD1 ASP A1127 13238 21428 11075 2729 -286 -1532 O ATOM 2459 OD2 ASP A1127 24.528 24.172 18.029 1.00126.69 O ANISOU 2459 OD2 ASP A1127 14000 22377 11759 3236 -408 -1496 O ATOM 2460 N GLU A1128 24.444 24.898 12.818 1.00106.19 N ANISOU 2460 N GLU A1128 11389 19486 9473 2889 -136 -1605 N ATOM 2461 CA GLU A1128 24.746 25.320 11.442 1.00105.51 C ANISOU 2461 CA GLU A1128 11242 19410 9436 2760 -60 -1675 C ATOM 2462 C GLU A1128 23.483 25.566 10.599 1.00106.45 C ANISOU 2462 C GLU A1128 11580 19159 9707 2608 6 -1592 C ATOM 2463 O GLU A1128 23.469 26.485 9.775 1.00105.26 O ANISOU 2463 O GLU A1128 11399 18989 9606 2385 86 -1653 O ATOM 2464 CB GLU A1128 25.708 24.337 10.749 1.00108.38 C ANISOU 2464 CB GLU A1128 11512 19938 9730 3010 -85 -1709 C ATOM 2465 CG GLU A1128 27.134 24.410 11.283 1.00120.59 C ANISOU 2465 CG GLU A1128 12769 21928 11122 3104 -129 -1824 C ATOM 2466 CD GLU A1128 28.236 23.803 10.435 1.00140.68 C ANISOU 2466 CD GLU A1128 15159 24698 13595 3290 -125 -1892 C ATOM 2467 OE1 GLU A1128 29.419 24.099 10.718 1.00133.31 O ANISOU 2467 OE1 GLU A1128 13948 24164 12539 3304 -144 -2007 O ATOM 2468 OE2 GLU A1128 27.929 23.035 9.495 1.00134.49 O ANISOU 2468 OE2 GLU A1128 14527 23704 12870 3416 -98 -1832 O ATOM 2469 N ALA A1129 22.422 24.759 10.823 1.00101.35 N ANISOU 2469 N ALA A1129 11157 18231 9122 2723 -25 -1457 N ATOM 2470 CA ALA A1129 21.130 24.867 10.134 1.00 98.84 C ANISOU 2470 CA ALA A1129 11041 17576 8936 2599 23 -1363 C ATOM 2471 C ALA A1129 20.281 25.977 10.748 1.00 99.98 C ANISOU 2471 C ALA A1129 11231 17616 9142 2374 63 -1338 C ATOM 2472 O ALA A1129 19.573 26.675 10.022 1.00 98.25 O ANISOU 2472 O ALA A1129 11084 17232 9014 2193 130 -1317 O ATOM 2473 CB ALA A1129 20.381 23.546 10.214 1.00 99.29 C ANISOU 2473 CB ALA A1129 11310 17408 9010 2797 -24 -1237 C ATOM 2474 N ALA A1130 20.348 26.123 12.090 1.00 95.90 N ANISOU 2474 N ALA A1130 10680 17190 8566 2398 24 -1336 N ATOM 2475 CA ALA A1130 19.612 27.112 12.875 1.00 94.31 C ANISOU 2475 CA ALA A1130 10529 16902 8403 2212 63 -1311 C ATOM 2476 C ALA A1130 19.907 28.546 12.434 1.00 96.70 C ANISOU 2476 C ALA A1130 10742 17288 8711 1951 156 -1407 C ATOM 2477 O ALA A1130 18.967 29.307 12.200 1.00 95.13 O ANISOU 2477 O ALA A1130 10657 16891 8596 1789 226 -1359 O ATOM 2478 CB ALA A1130 19.916 26.934 14.353 1.00 95.97 C ANISOU 2478 CB ALA A1130 10699 17245 8522 2301 1 -1312 C ATOM 2479 N VAL A1131 21.203 28.905 12.289 1.00 93.43 N ANISOU 2479 N VAL A1131 10131 17169 8197 1910 161 -1543 N ATOM 2480 CA VAL A1131 21.632 30.238 11.838 1.00 92.77 C ANISOU 2480 CA VAL A1131 9971 17187 8091 1647 258 -1655 C ATOM 2481 C VAL A1131 21.298 30.466 10.357 1.00 94.62 C ANISOU 2481 C VAL A1131 10278 17260 8413 1562 328 -1652 C ATOM 2482 O VAL A1131 21.073 31.608 9.951 1.00 93.75 O ANISOU 2482 O VAL A1131 10213 17086 8322 1337 425 -1692 O ATOM 2483 CB VAL A1131 23.111 30.590 12.177 1.00 98.43 C ANISOU 2483 CB VAL A1131 10448 18292 8659 1597 248 -1810 C ATOM 2484 CG1 VAL A1131 23.317 30.737 13.683 1.00 99.02 C ANISOU 2484 CG1 VAL A1131 10470 18513 8641 1602 199 -1818 C ATOM 2485 CG2 VAL A1131 24.095 29.581 11.582 1.00 99.44 C ANISOU 2485 CG2 VAL A1131 10427 18620 8737 1808 186 -1857 C ATOM 2486 N ASN A1132 21.255 29.370 9.564 1.00 90.03 N ANISOU 2486 N ASN A1132 9727 16604 7875 1744 281 -1603 N ATOM 2487 CA ASN A1132 20.940 29.375 8.134 1.00 88.49 C ANISOU 2487 CA ASN A1132 9610 16253 7760 1692 332 -1590 C ATOM 2488 C ASN A1132 19.453 29.654 7.903 1.00 89.76 C ANISOU 2488 C ASN A1132 9974 16092 8038 1613 365 -1464 C ATOM 2489 O ASN A1132 19.115 30.394 6.973 1.00 88.55 O ANISOU 2489 O ASN A1132 9882 15829 7935 1458 440 -1475 O ATOM 2490 CB ASN A1132 21.368 28.054 7.481 1.00 88.78 C ANISOU 2490 CB ASN A1132 9631 16312 7788 1918 273 -1573 C ATOM 2491 CG ASN A1132 21.515 28.067 5.972 1.00105.65 C ANISOU 2491 CG ASN A1132 11792 18384 9967 1863 326 -1606 C ATOM 2492 OD1 ASN A1132 21.690 27.019 5.351 1.00 98.88 O ANISOU 2492 OD1 ASN A1132 10967 17492 9112 2032 294 -1577 O ATOM 2493 ND2 ASN A1132 21.479 29.237 5.338 1.00 95.88 N ANISOU 2493 ND2 ASN A1132 10554 17123 8752 1627 415 -1669 N ATOM 2494 N LEU A1133 18.570 29.082 8.761 1.00 85.17 N ANISOU 2494 N LEU A1133 9497 15371 7492 1719 311 -1347 N ATOM 2495 CA LEU A1133 17.113 29.288 8.721 1.00 83.24 C ANISOU 2495 CA LEU A1133 9423 14854 7350 1658 336 -1221 C ATOM 2496 C LEU A1133 16.779 30.744 9.072 1.00 85.99 C ANISOU 2496 C LEU A1133 9790 15179 7705 1452 425 -1244 C ATOM 2497 O LEU A1133 15.821 31.301 8.535 1.00 84.57 O ANISOU 2497 O LEU A1133 9722 14812 7600 1357 482 -1177 O ATOM 2498 CB LEU A1133 16.391 28.342 9.702 1.00 83.05 C ANISOU 2498 CB LEU A1133 9489 14727 7339 1811 263 -1109 C ATOM 2499 CG LEU A1133 16.247 26.865 9.314 1.00 87.81 C ANISOU 2499 CG LEU A1133 10170 15248 7947 2002 194 -1044 C ATOM 2500 CD1 LEU A1133 15.986 26.012 10.544 1.00 88.33 C ANISOU 2500 CD1 LEU A1133 10297 15292 7974 2155 126 -980 C ATOM 2501 CD2 LEU A1133 15.128 26.653 8.300 1.00 88.93 C ANISOU 2501 CD2 LEU A1133 10453 15154 8184 1948 214 -947 C ATOM 2502 N ALA A1134 17.589 31.359 9.963 1.00 82.84 N ANISOU 2502 N ALA A1134 9287 14976 7213 1385 442 -1339 N ATOM 2503 CA ALA A1134 17.465 32.749 10.407 1.00 82.23 C ANISOU 2503 CA ALA A1134 9239 14898 7107 1181 538 -1379 C ATOM 2504 C ALA A1134 17.934 33.755 9.334 1.00 85.34 C ANISOU 2504 C ALA A1134 9623 15325 7478 995 639 -1478 C ATOM 2505 O ALA A1134 17.920 34.965 9.574 1.00 84.89 O ANISOU 2505 O ALA A1134 9615 15263 7377 810 738 -1525 O ATOM 2506 CB ALA A1134 18.242 32.949 11.702 1.00 84.09 C ANISOU 2506 CB ALA A1134 9371 15348 7232 1164 516 -1453 C ATOM 2507 N LYS A1135 18.343 33.253 8.156 1.00 81.61 N ANISOU 2507 N LYS A1135 9107 14873 7026 1040 621 -1510 N ATOM 2508 CA LYS A1135 18.795 34.070 7.031 1.00 81.60 C ANISOU 2508 CA LYS A1135 9108 14892 7005 875 713 -1604 C ATOM 2509 C LYS A1135 17.768 34.027 5.882 1.00 84.65 C ANISOU 2509 C LYS A1135 9644 15020 7499 880 736 -1504 C ATOM 2510 O LYS A1135 18.075 34.405 4.744 1.00 84.50 O ANISOU 2510 O LYS A1135 9641 14988 7478 787 792 -1563 O ATOM 2511 CB LYS A1135 20.197 33.631 6.577 1.00 85.08 C ANISOU 2511 CB LYS A1135 9367 15593 7368 903 686 -1737 C ATOM 2512 CG LYS A1135 21.065 34.792 6.111 1.00 97.55 C ANISOU 2512 CG LYS A1135 10895 17314 8855 667 796 -1892 C ATOM 2513 CD LYS A1135 22.540 34.441 6.128 1.00108.93 C ANISOU 2513 CD LYS A1135 12108 19091 10190 687 765 -2036 C ATOM 2514 CE LYS A1135 23.396 35.607 5.697 1.00120.65 C ANISOU 2514 CE LYS A1135 13542 20730 11570 422 883 -2199 C ATOM 2515 NZ LYS A1135 24.843 35.281 5.775 1.00131.38 N ANISOU 2515 NZ LYS A1135 14648 22457 12813 435 852 -2343 N ATOM 2516 N SER A1136 16.533 33.592 6.201 1.00 80.11 N ANISOU 2516 N SER A1136 9177 14250 7011 978 694 -1353 N ATOM 2517 CA SER A1136 15.425 33.493 5.252 1.00 78.84 C ANISOU 2517 CA SER A1136 9147 13863 6947 990 702 -1241 C ATOM 2518 C SER A1136 14.412 34.628 5.450 1.00 82.09 C ANISOU 2518 C SER A1136 9687 14117 7386 885 788 -1173 C ATOM 2519 O SER A1136 14.589 35.466 6.340 1.00 81.89 O ANISOU 2519 O SER A1136 9668 14143 7303 800 849 -1214 O ATOM 2520 CB SER A1136 14.746 32.129 5.366 1.00 81.66 C ANISOU 2520 CB SER A1136 9530 14130 7369 1168 596 -1123 C ATOM 2521 OG SER A1136 14.109 31.959 6.620 1.00 89.27 O ANISOU 2521 OG SER A1136 10518 15056 8343 1228 566 -1045 O ATOM 2522 N ARG A1137 13.362 34.662 4.603 1.00 77.92 N ANISOU 2522 N ARG A1137 9266 13404 6935 894 797 -1067 N ATOM 2523 CA ARG A1137 12.307 35.670 4.671 1.00 77.23 C ANISOU 2523 CA ARG A1137 9304 13165 6873 833 878 -983 C ATOM 2524 C ARG A1137 11.249 35.297 5.697 1.00 79.79 C ANISOU 2524 C ARG A1137 9654 13412 7249 929 838 -854 C ATOM 2525 O ARG A1137 10.645 36.187 6.291 1.00 79.37 O ANISOU 2525 O ARG A1137 9677 13291 7191 889 914 -810 O ATOM 2526 CB ARG A1137 11.682 35.907 3.299 1.00 77.86 C ANISOU 2526 CB ARG A1137 9474 13109 6998 807 903 -928 C ATOM 2527 CG ARG A1137 11.147 37.328 3.125 1.00 90.12 C ANISOU 2527 CG ARG A1137 11161 14555 8527 711 1027 -907 C ATOM 2528 CD ARG A1137 11.747 38.037 1.919 1.00101.58 C ANISOU 2528 CD ARG A1137 12672 15993 9928 593 1103 -1000 C ATOM 2529 NE ARG A1137 11.888 37.150 0.761 1.00109.60 N ANISOU 2529 NE ARG A1137 13650 17004 10989 633 1026 -997 N ATOM 2530 CZ ARG A1137 10.922 36.872 -0.106 1.00122.89 C ANISOU 2530 CZ ARG A1137 15397 18560 12736 684 989 -882 C ATOM 2531 NH1 ARG A1137 9.719 37.421 0.027 1.00109.73 N ANISOU 2531 NH1 ARG A1137 13820 16775 11098 717 1019 -757 N ATOM 2532 NH2 ARG A1137 11.145 36.039 -1.112 1.00108.96 N ANISOU 2532 NH2 ARG A1137 13606 16795 10998 704 924 -890 N ATOM 2533 N TRP A1138 11.046 33.981 5.927 1.00 75.62 N ANISOU 2533 N TRP A1138 9077 12893 6763 1055 727 -798 N ATOM 2534 CA TRP A1138 10.108 33.444 6.919 1.00 74.93 C ANISOU 2534 CA TRP A1138 9011 12742 6716 1143 682 -686 C ATOM 2535 C TRP A1138 10.513 33.894 8.332 1.00 78.71 C ANISOU 2535 C TRP A1138 9464 13301 7139 1127 712 -732 C ATOM 2536 O TRP A1138 9.647 34.081 9.188 1.00 78.07 O ANISOU 2536 O TRP A1138 9434 13145 7084 1148 732 -647 O ATOM 2537 CB TRP A1138 9.997 31.912 6.782 1.00 73.49 C ANISOU 2537 CB TRP A1138 8807 12555 6562 1263 569 -639 C ATOM 2538 CG TRP A1138 9.789 31.156 8.057 1.00 74.60 C ANISOU 2538 CG TRP A1138 8942 12709 6694 1358 513 -598 C ATOM 2539 CD1 TRP A1138 8.628 31.035 8.764 1.00 77.07 C ANISOU 2539 CD1 TRP A1138 9311 12924 7049 1383 511 -485 C ATOM 2540 CD2 TRP A1138 10.766 30.380 8.762 1.00 75.06 C ANISOU 2540 CD2 TRP A1138 8938 12890 6690 1447 452 -668 C ATOM 2541 NE1 TRP A1138 8.829 30.255 9.878 1.00 76.91 N ANISOU 2541 NE1 TRP A1138 9283 12942 6997 1470 456 -485 N ATOM 2542 CE2 TRP A1138 10.132 29.823 9.890 1.00 78.95 C ANISOU 2542 CE2 TRP A1138 9473 13336 7189 1520 415 -593 C ATOM 2543 CE3 TRP A1138 12.129 30.100 8.542 1.00 76.97 C ANISOU 2543 CE3 TRP A1138 9090 13290 6864 1481 426 -787 C ATOM 2544 CZ2 TRP A1138 10.808 29.011 10.808 1.00 78.89 C ANISOU 2544 CZ2 TRP A1138 9437 13419 7119 1631 350 -630 C ATOM 2545 CZ3 TRP A1138 12.799 29.297 9.453 1.00 79.21 C ANISOU 2545 CZ3 TRP A1138 9326 13685 7087 1602 360 -821 C ATOM 2546 CH2 TRP A1138 12.145 28.775 10.577 1.00 79.61 C ANISOU 2546 CH2 TRP A1138 9436 13672 7140 1678 322 -742 C ATOM 2547 N TYR A1139 11.828 34.116 8.545 1.00 75.64 N ANISOU 2547 N TYR A1139 8996 13076 6668 1078 722 -871 N ATOM 2548 CA TYR A1139 12.396 34.620 9.793 1.00 75.91 C ANISOU 2548 CA TYR A1139 8997 13219 6625 1032 752 -937 C ATOM 2549 C TYR A1139 11.971 36.080 10.027 1.00 79.14 C ANISOU 2549 C TYR A1139 9512 13548 7011 896 885 -933 C ATOM 2550 O TYR A1139 11.774 36.465 11.180 1.00 79.02 O ANISOU 2550 O TYR A1139 9530 13530 6965 877 918 -918 O ATOM 2551 CB TYR A1139 13.930 34.470 9.790 1.00 78.17 C ANISOU 2551 CB TYR A1139 9150 13732 6818 1005 725 -1089 C ATOM 2552 CG TYR A1139 14.637 35.104 10.972 1.00 81.08 C ANISOU 2552 CG TYR A1139 9473 14247 7086 921 760 -1176 C ATOM 2553 CD1 TYR A1139 14.703 34.453 12.201 1.00 83.30 C ANISOU 2553 CD1 TYR A1139 9713 14596 7343 1022 685 -1152 C ATOM 2554 CD2 TYR A1139 15.260 36.344 10.854 1.00 82.66 C ANISOU 2554 CD2 TYR A1139 9684 14522 7201 730 869 -1285 C ATOM 2555 CE1 TYR A1139 15.362 35.028 13.287 1.00 85.04 C ANISOU 2555 CE1 TYR A1139 9890 14962 7461 935 711 -1231 C ATOM 2556 CE2 TYR A1139 15.922 36.927 11.932 1.00 84.54 C ANISOU 2556 CE2 TYR A1139 9886 14905 7330 628 903 -1369 C ATOM 2557 CZ TYR A1139 15.972 36.264 13.147 1.00 92.74 C ANISOU 2557 CZ TYR A1139 10869 16018 8350 732 819 -1340 C ATOM 2558 OH TYR A1139 16.625 36.833 14.213 1.00 95.60 O ANISOU 2558 OH TYR A1139 11195 16532 8596 623 847 -1423 O ATOM 2559 N ASN A1140 11.836 36.885 8.945 1.00 74.92 N ANISOU 2559 N ASN A1140 9048 12938 6481 807 967 -946 N ATOM 2560 CA ASN A1140 11.424 38.286 9.050 1.00 74.59 C ANISOU 2560 CA ASN A1140 9142 12797 6401 693 1108 -939 C ATOM 2561 C ASN A1140 9.911 38.491 8.945 1.00 76.94 C ANISOU 2561 C ASN A1140 9551 12902 6782 770 1138 -776 C ATOM 2562 O ASN A1140 9.391 39.420 9.563 1.00 76.90 O ANISOU 2562 O ASN A1140 9656 12815 6749 734 1241 -738 O ATOM 2563 CB ASN A1140 12.222 39.220 8.120 1.00 76.59 C ANISOU 2563 CB ASN A1140 9438 13085 6577 539 1204 -1058 C ATOM 2564 CG ASN A1140 12.030 39.016 6.630 1.00104.06 C ANISOU 2564 CG ASN A1140 12935 16493 10108 559 1188 -1038 C ATOM 2565 OD1 ASN A1140 10.937 39.189 6.074 1.00 97.96 O ANISOU 2565 OD1 ASN A1140 12258 15562 9401 614 1206 -919 O ATOM 2566 ND2 ASN A1140 13.126 38.760 5.932 1.00 97.85 N ANISOU 2566 ND2 ASN A1140 12062 15835 9282 501 1166 -1160 N ATOM 2567 N GLN A1141 9.210 37.618 8.180 1.00 72.16 N ANISOU 2567 N GLN A1141 8914 12235 6268 875 1053 -682 N ATOM 2568 CA GLN A1141 7.753 37.644 7.985 1.00 71.29 C ANISOU 2568 CA GLN A1141 8870 11982 6236 954 1060 -525 C ATOM 2569 C GLN A1141 7.036 37.371 9.306 1.00 75.25 C ANISOU 2569 C GLN A1141 9371 12458 6764 1023 1047 -441 C ATOM 2570 O GLN A1141 6.132 38.114 9.687 1.00 74.83 O ANISOU 2570 O GLN A1141 9401 12310 6719 1038 1131 -356 O ATOM 2571 CB GLN A1141 7.322 36.604 6.932 1.00 72.02 C ANISOU 2571 CB GLN A1141 8912 12051 6401 1024 955 -461 C ATOM 2572 CG GLN A1141 7.567 37.012 5.485 1.00 85.53 C ANISOU 2572 CG GLN A1141 10661 13734 8103 967 984 -496 C ATOM 2573 CD GLN A1141 6.854 36.107 4.507 1.00102.97 C ANISOU 2573 CD GLN A1141 12847 15896 10381 1029 893 -405 C ATOM 2574 OE1 GLN A1141 5.972 36.542 3.759 1.00 97.95 O ANISOU 2574 OE1 GLN A1141 12269 15176 9770 1038 920 -317 O ATOM 2575 NE2 GLN A1141 7.199 34.823 4.502 1.00 95.18 N ANISOU 2575 NE2 GLN A1141 11784 14965 9415 1076 785 -421 N ATOM 2576 N THR A1142 7.449 36.293 9.996 1.00 71.98 N ANISOU 2576 N THR A1142 8868 12126 6353 1075 946 -466 N ATOM 2577 CA THR A1142 6.922 35.867 11.292 1.00 71.80 C ANISOU 2577 CA THR A1142 8845 12089 6347 1138 921 -403 C ATOM 2578 C THR A1142 8.125 35.837 12.257 1.00 76.78 C ANISOU 2578 C THR A1142 9430 12848 6894 1100 907 -523 C ATOM 2579 O THR A1142 8.740 34.786 12.421 1.00 76.58 O ANISOU 2579 O THR A1142 9325 12914 6858 1162 804 -564 O ATOM 2580 CB THR A1142 6.185 34.516 11.157 1.00 77.44 C ANISOU 2580 CB THR A1142 9521 12771 7132 1241 809 -309 C ATOM 2581 OG1 THR A1142 7.061 33.542 10.591 1.00 76.27 O ANISOU 2581 OG1 THR A1142 9308 12702 6969 1268 715 -380 O ATOM 2582 CG2 THR A1142 4.906 34.613 10.336 1.00 75.23 C ANISOU 2582 CG2 THR A1142 9273 12391 6921 1262 824 -185 C ATOM 2583 N PRO A1143 8.534 36.985 12.849 1.00 74.07 N ANISOU 2583 N PRO A1143 9142 12525 6476 997 1013 -586 N ATOM 2584 CA PRO A1143 9.737 36.978 13.701 1.00 74.75 C ANISOU 2584 CA PRO A1143 9167 12766 6467 941 994 -709 C ATOM 2585 C PRO A1143 9.667 36.107 14.955 1.00 79.38 C ANISOU 2585 C PRO A1143 9717 13390 7053 1031 911 -678 C ATOM 2586 O PRO A1143 10.544 35.264 15.147 1.00 79.52 O ANISOU 2586 O PRO A1143 9635 13546 7033 1082 812 -745 O ATOM 2587 CB PRO A1143 9.972 38.462 14.009 1.00 77.03 C ANISOU 2587 CB PRO A1143 9559 13037 6671 789 1143 -767 C ATOM 2588 CG PRO A1143 9.156 39.213 13.005 1.00 81.03 C ANISOU 2588 CG PRO A1143 10173 13393 7220 775 1235 -698 C ATOM 2589 CD PRO A1143 7.973 38.346 12.745 1.00 75.72 C ANISOU 2589 CD PRO A1143 9481 12623 6667 923 1160 -554 C ATOM 2590 N ASN A1144 8.638 36.308 15.803 1.00 75.74 N ANISOU 2590 N ASN A1144 9343 12809 6626 1059 956 -577 N ATOM 2591 CA ASN A1144 8.444 35.560 17.050 1.00 75.53 C ANISOU 2591 CA ASN A1144 9311 12790 6596 1135 892 -541 C ATOM 2592 C ASN A1144 8.064 34.101 16.773 1.00 79.44 C ANISOU 2592 C ASN A1144 9762 13265 7156 1272 768 -477 C ATOM 2593 O ASN A1144 8.498 33.205 17.499 1.00 79.55 O ANISOU 2593 O ASN A1144 9744 13346 7135 1347 680 -498 O ATOM 2594 CB ASN A1144 7.371 36.237 17.916 1.00 74.78 C ANISOU 2594 CB ASN A1144 9332 12558 6524 1120 992 -448 C ATOM 2595 CG ASN A1144 7.542 37.729 18.127 1.00 92.01 C ANISOU 2595 CG ASN A1144 11610 14713 8637 988 1141 -491 C ATOM 2596 OD1 ASN A1144 8.587 38.330 17.827 1.00 83.42 O ANISOU 2596 OD1 ASN A1144 10504 13727 7464 876 1174 -609 O ATOM 2597 ND2 ASN A1144 6.504 38.366 18.644 1.00 84.10 N ANISOU 2597 ND2 ASN A1144 10721 13573 7661 995 1244 -396 N ATOM 2598 N ARG A1145 7.269 33.873 15.711 1.00 75.39 N ANISOU 2598 N ARG A1145 9260 12662 6725 1302 764 -400 N ATOM 2599 CA ARG A1145 6.783 32.553 15.299 1.00 74.75 C ANISOU 2599 CA ARG A1145 9164 12542 6696 1401 664 -334 C ATOM 2600 C ARG A1145 7.874 31.648 14.712 1.00 78.47 C ANISOU 2600 C ARG A1145 9565 13122 7129 1455 568 -417 C ATOM 2601 O ARG A1145 7.767 30.427 14.828 1.00 78.00 O ANISOU 2601 O ARG A1145 9517 13047 7071 1551 482 -385 O ATOM 2602 CB ARG A1145 5.572 32.679 14.353 1.00 74.74 C ANISOU 2602 CB ARG A1145 9192 12427 6779 1395 694 -226 C ATOM 2603 CG ARG A1145 4.409 33.488 14.944 1.00 85.62 C ANISOU 2603 CG ARG A1145 10631 13709 8193 1376 791 -130 C ATOM 2604 CD ARG A1145 4.008 34.652 14.051 1.00 94.15 C ANISOU 2604 CD ARG A1145 11737 14743 9294 1326 887 -103 C ATOM 2605 NE ARG A1145 3.457 35.773 14.815 1.00102.12 N ANISOU 2605 NE ARG A1145 12821 15689 10291 1303 1011 -61 N ATOM 2606 CZ ARG A1145 4.108 36.903 15.078 1.00114.33 C ANISOU 2606 CZ ARG A1145 14426 17244 11769 1227 1109 -135 C ATOM 2607 NH1 ARG A1145 3.525 37.862 15.785 1.00101.51 N ANISOU 2607 NH1 ARG A1145 12898 15544 10130 1216 1231 -87 N ATOM 2608 NH2 ARG A1145 5.346 37.085 14.634 1.00 98.54 N ANISOU 2608 NH2 ARG A1145 12399 15333 9710 1156 1095 -261 N ATOM 2609 N ALA A1146 8.922 32.243 14.097 1.00 75.20 N ANISOU 2609 N ALA A1146 9089 12814 6670 1392 591 -525 N ATOM 2610 CA ALA A1146 10.052 31.528 13.488 1.00 75.23 C ANISOU 2610 CA ALA A1146 9011 12944 6631 1443 516 -614 C ATOM 2611 C ALA A1146 11.156 31.192 14.490 1.00 79.60 C ANISOU 2611 C ALA A1146 9495 13661 7089 1494 463 -702 C ATOM 2612 O ALA A1146 11.727 30.103 14.410 1.00 79.51 O ANISOU 2612 O ALA A1146 9445 13720 7046 1616 375 -724 O ATOM 2613 CB ALA A1146 10.629 32.334 12.338 1.00 75.94 C ANISOU 2613 CB ALA A1146 9061 13082 6713 1343 572 -691 C ATOM 2614 N LYS A1147 11.467 32.134 15.417 1.00 76.40 N ANISOU 2614 N LYS A1147 9081 13319 6626 1404 522 -751 N ATOM 2615 CA LYS A1147 12.493 32.002 16.465 1.00 77.08 C ANISOU 2615 CA LYS A1147 9095 13583 6607 1427 477 -836 C ATOM 2616 C LYS A1147 12.253 30.771 17.358 1.00 80.75 C ANISOU 2616 C LYS A1147 9594 14023 7063 1590 381 -775 C ATOM 2617 O LYS A1147 13.217 30.112 17.753 1.00 81.12 O ANISOU 2617 O LYS A1147 9565 14230 7027 1690 300 -837 O ATOM 2618 CB LYS A1147 12.564 33.287 17.314 1.00 79.92 C ANISOU 2618 CB LYS A1147 9485 13968 6913 1274 573 -876 C ATOM 2619 CG LYS A1147 13.797 33.381 18.218 1.00 94.23 C ANISOU 2619 CG LYS A1147 11198 16010 8595 1247 536 -989 C ATOM 2620 CD LYS A1147 13.683 34.490 19.267 1.00103.30 C ANISOU 2620 CD LYS A1147 12416 17150 9684 1099 628 -1008 C ATOM 2621 CE LYS A1147 12.829 34.131 20.468 1.00112.00 C ANISOU 2621 CE LYS A1147 13619 18126 10810 1171 612 -909 C ATOM 2622 NZ LYS A1147 13.429 33.042 21.285 1.00121.02 N ANISOU 2622 NZ LYS A1147 14694 19398 11889 1314 484 -926 N ATOM 2623 N ARG A1148 10.971 30.468 17.662 1.00 76.29 N ANISOU 2623 N ARG A1148 9146 13266 6574 1620 393 -654 N ATOM 2624 CA ARG A1148 10.551 29.315 18.465 1.00 76.01 C ANISOU 2624 CA ARG A1148 9183 13166 6530 1754 320 -587 C ATOM 2625 C ARG A1148 10.933 28.010 17.756 1.00 80.82 C ANISOU 2625 C ARG A1148 9787 13796 7126 1899 229 -588 C ATOM 2626 O ARG A1148 11.521 27.129 18.382 1.00 81.26 O ANISOU 2626 O ARG A1148 9847 13925 7104 2034 152 -609 O ATOM 2627 CB ARG A1148 9.032 29.344 18.712 1.00 74.22 C ANISOU 2627 CB ARG A1148 9074 12736 6391 1725 369 -463 C ATOM 2628 CG ARG A1148 8.541 30.505 19.565 1.00 81.24 C ANISOU 2628 CG ARG A1148 10000 13579 7288 1615 466 -444 C ATOM 2629 CD ARG A1148 7.063 30.362 19.864 1.00 85.88 C ANISOU 2629 CD ARG A1148 10687 13989 7954 1616 506 -319 C ATOM 2630 NE ARG A1148 6.532 31.543 20.542 1.00 92.03 N ANISOU 2630 NE ARG A1148 11511 14713 8745 1521 617 -293 N ATOM 2631 CZ ARG A1148 5.919 32.550 19.930 1.00106.19 C ANISOU 2631 CZ ARG A1148 13316 16441 10592 1444 717 -256 C ATOM 2632 NH1 ARG A1148 5.469 33.585 20.629 1.00 95.28 N ANISOU 2632 NH1 ARG A1148 11998 15000 9204 1377 827 -230 N ATOM 2633 NH2 ARG A1148 5.746 32.534 18.614 1.00 92.61 N ANISOU 2633 NH2 ARG A1148 11557 14709 8923 1440 712 -240 N ATOM 2634 N VAL A1149 10.620 27.914 16.441 1.00 77.20 N ANISOU 2634 N VAL A1149 9328 13272 6733 1873 244 -565 N ATOM 2635 CA VAL A1149 10.884 26.766 15.560 1.00 77.22 C ANISOU 2635 CA VAL A1149 9349 13266 6727 1985 180 -561 C ATOM 2636 C VAL A1149 12.393 26.483 15.458 1.00 82.06 C ANISOU 2636 C VAL A1149 9849 14085 7246 2081 128 -673 C ATOM 2637 O VAL A1149 12.803 25.336 15.641 1.00 82.10 O ANISOU 2637 O VAL A1149 9891 14115 7189 2247 58 -670 O ATOM 2638 CB VAL A1149 10.203 26.943 14.172 1.00 80.42 C ANISOU 2638 CB VAL A1149 9775 13563 7220 1903 217 -516 C ATOM 2639 CG1 VAL A1149 10.433 25.732 13.272 1.00 80.59 C ANISOU 2639 CG1 VAL A1149 9840 13556 7224 2007 159 -508 C ATOM 2640 CG2 VAL A1149 8.707 27.206 14.322 1.00 79.42 C ANISOU 2640 CG2 VAL A1149 9734 13269 7174 1825 263 -402 C ATOM 2641 N ILE A1150 13.205 27.533 15.197 1.00 79.21 N ANISOU 2641 N ILE A1150 9357 13876 6863 1976 170 -771 N ATOM 2642 CA ILE A1150 14.671 27.478 15.093 1.00 80.33 C ANISOU 2642 CA ILE A1150 9354 14259 6910 2033 133 -890 C ATOM 2643 C ILE A1150 15.299 26.947 16.400 1.00 85.99 C ANISOU 2643 C ILE A1150 10040 15111 7521 2166 61 -914 C ATOM 2644 O ILE A1150 16.150 26.054 16.348 1.00 86.73 O ANISOU 2644 O ILE A1150 10083 15333 7538 2339 -9 -949 O ATOM 2645 CB ILE A1150 15.239 28.862 14.635 1.00 83.45 C ANISOU 2645 CB ILE A1150 9637 14773 7297 1842 212 -990 C ATOM 2646 CG1 ILE A1150 14.927 29.108 13.136 1.00 83.04 C ANISOU 2646 CG1 ILE A1150 9607 14622 7324 1765 262 -982 C ATOM 2647 CG2 ILE A1150 16.749 29.012 14.924 1.00 85.52 C ANISOU 2647 CG2 ILE A1150 9723 15332 7437 1859 182 -1124 C ATOM 2648 CD1 ILE A1150 14.795 30.579 12.711 1.00 88.94 C ANISOU 2648 CD1 ILE A1150 10347 15352 8095 1552 370 -1024 C ATOM 2649 N THR A1151 14.841 27.469 17.560 1.00 82.72 N ANISOU 2649 N THR A1151 9670 14660 7099 2097 82 -887 N ATOM 2650 CA THR A1151 15.303 27.078 18.898 1.00 83.75 C ANISOU 2650 CA THR A1151 9791 14901 7129 2202 18 -900 C ATOM 2651 C THR A1151 14.929 25.618 19.219 1.00 88.36 C ANISOU 2651 C THR A1151 10509 15369 7695 2416 -57 -818 C ATOM 2652 O THR A1151 15.679 24.943 19.930 1.00 89.30 O ANISOU 2652 O THR A1151 10603 15621 7705 2580 -134 -844 O ATOM 2653 CB THR A1151 14.832 28.099 19.953 1.00 92.00 C ANISOU 2653 CB THR A1151 10870 15909 8176 2047 76 -891 C ATOM 2654 OG1 THR A1151 15.100 29.420 19.480 1.00 92.11 O ANISOU 2654 OG1 THR A1151 10805 15993 8201 1844 164 -963 O ATOM 2655 CG2 THR A1151 15.508 27.910 21.311 1.00 91.97 C ANISOU 2655 CG2 THR A1151 10829 16064 8050 2120 12 -929 C ATOM 2656 N THR A1152 13.790 25.130 18.667 1.00 83.92 N ANISOU 2656 N THR A1152 10094 14566 7225 2411 -33 -720 N ATOM 2657 CA THR A1152 13.296 23.756 18.847 1.00 83.77 C ANISOU 2657 CA THR A1152 10242 14402 7185 2574 -82 -640 C ATOM 2658 C THR A1152 14.244 22.729 18.189 1.00 88.93 C ANISOU 2658 C THR A1152 10878 15152 7761 2770 -142 -677 C ATOM 2659 O THR A1152 14.428 21.639 18.740 1.00 89.44 O ANISOU 2659 O THR A1152 11051 15195 7736 2961 -199 -649 O ATOM 2660 CB THR A1152 11.804 23.642 18.463 1.00 88.19 C ANISOU 2660 CB THR A1152 10947 14707 7852 2474 -31 -534 C ATOM 2661 OG1 THR A1152 11.076 24.673 19.130 1.00 86.82 O ANISOU 2661 OG1 THR A1152 10768 14481 7737 2319 31 -508 O ATOM 2662 CG2 THR A1152 11.193 22.301 18.846 1.00 85.75 C ANISOU 2662 CG2 THR A1152 10838 14240 7505 2599 -67 -455 C ATOM 2663 N PHE A1153 14.877 23.092 17.044 1.00 85.68 N ANISOU 2663 N PHE A1153 10338 14845 7371 2729 -123 -741 N ATOM 2664 CA PHE A1153 15.850 22.230 16.362 1.00 86.71 C ANISOU 2664 CA PHE A1153 10432 15085 7427 2913 -166 -784 C ATOM 2665 C PHE A1153 17.157 22.181 17.151 1.00 92.60 C ANISOU 2665 C PHE A1153 11030 16109 8043 3057 -228 -867 C ATOM 2666 O PHE A1153 17.729 21.101 17.322 1.00 93.44 O ANISOU 2666 O PHE A1153 11184 16270 8049 3298 -285 -861 O ATOM 2667 CB PHE A1153 16.124 22.705 14.929 1.00 88.10 C ANISOU 2667 CB PHE A1153 10512 15295 7666 2810 -120 -832 C ATOM 2668 CG PHE A1153 14.949 22.661 13.982 1.00 88.51 C ANISOU 2668 CG PHE A1153 10696 15103 7831 2689 -71 -753 C ATOM 2669 CD1 PHE A1153 14.299 21.463 13.704 1.00 91.67 C ANISOU 2669 CD1 PHE A1153 11291 15313 8224 2787 -88 -668 C ATOM 2670 CD2 PHE A1153 14.539 23.804 13.309 1.00 89.76 C ANISOU 2670 CD2 PHE A1153 10788 15232 8085 2477 -6 -766 C ATOM 2671 CE1 PHE A1153 13.228 21.422 12.806 1.00 91.51 C ANISOU 2671 CE1 PHE A1153 11377 15097 8295 2659 -48 -597 C ATOM 2672 CE2 PHE A1153 13.471 23.761 12.412 1.00 91.52 C ANISOU 2672 CE2 PHE A1153 11116 15255 8401 2376 31 -690 C ATOM 2673 CZ PHE A1153 12.820 22.571 12.167 1.00 89.55 C ANISOU 2673 CZ PHE A1153 11039 14840 8147 2461 5 -607 C ATOM 2674 N ARG A1154 17.640 23.321 17.600 1.00 89.46 N ANISOU 2674 N ARG A1154 10462 15894 7634 2916 -212 -944 N ATOM 2675 CA ARG A1154 18.805 23.333 18.454 1.00 90.95 C ANISOU 2675 CA ARG A1154 10500 16368 7690 3026 -275 -1020 C ATOM 2676 C ARG A1154 18.571 22.497 19.715 1.00 96.30 C ANISOU 2676 C ARG A1154 11313 16987 8288 3202 -341 -955 C ATOM 2677 O ARG A1154 19.432 21.712 20.113 1.00 97.75 O ANISOU 2677 O ARG A1154 11460 17334 8345 3437 -416 -975 O ATOM 2678 CB ARG A1154 19.146 24.765 18.852 1.00 90.46 C ANISOU 2678 CB ARG A1154 10275 16472 7624 2793 -234 -1105 C ATOM 2679 CG ARG A1154 20.231 25.393 18.036 1.00 99.46 C ANISOU 2679 CG ARG A1154 11196 17863 8729 2712 -212 -1226 C ATOM 2680 CD ARG A1154 20.070 26.887 17.951 1.00106.01 C ANISOU 2680 CD ARG A1154 11965 18711 9604 2410 -122 -1284 C ATOM 2681 NE ARG A1154 20.597 27.573 19.121 1.00113.57 N ANISOU 2681 NE ARG A1154 12823 19867 10459 2319 -136 -1347 N ATOM 2682 CZ ARG A1154 20.523 28.885 19.305 1.00125.33 C ANISOU 2682 CZ ARG A1154 14285 21382 11953 2054 -53 -1401 C ATOM 2683 NH1 ARG A1154 21.018 29.451 20.394 1.00110.56 N ANISOU 2683 NH1 ARG A1154 12339 19693 9973 1965 -66 -1459 N ATOM 2684 NH2 ARG A1154 19.945 29.635 18.389 1.00111.52 N ANISOU 2684 NH2 ARG A1154 12598 19470 10304 1878 46 -1397 N ATOM 2685 N THR A1155 17.437 22.654 20.383 1.00 92.03 N ANISOU 2685 N THR A1155 10931 16225 7809 3101 -313 -877 N ATOM 2686 CA THR A1155 17.325 22.035 21.703 1.00 92.79 C ANISOU 2686 CA THR A1155 11143 16296 7818 3240 -371 -833 C ATOM 2687 C THR A1155 16.218 21.074 22.133 1.00 97.01 C ANISOU 2687 C THR A1155 11950 16540 8368 3321 -371 -720 C ATOM 2688 O THR A1155 16.470 19.923 22.490 1.00 97.60 O ANISOU 2688 O THR A1155 12150 16592 8340 3555 -428 -689 O ATOM 2689 CB THR A1155 17.221 23.111 22.807 1.00100.79 C ANISOU 2689 CB THR A1155 12094 17379 8824 3066 -355 -859 C ATOM 2690 OG1 THR A1155 15.882 23.616 22.863 1.00 99.18 O ANISOU 2690 OG1 THR A1155 12024 16914 8745 2880 -275 -787 O ATOM 2691 CG2 THR A1155 18.180 24.258 22.526 1.00 99.29 C ANISOU 2691 CG2 THR A1155 11656 17461 8609 2916 -335 -976 C ATOM 2692 N GLY A1156 14.994 21.384 21.855 1.00 92.94 N ANISOU 2692 N GLY A1156 11545 15792 7976 3147 -302 -656 N ATOM 2693 CA GLY A1156 13.860 20.632 22.359 1.00 92.66 C ANISOU 2693 CA GLY A1156 11752 15497 7955 3170 -289 -557 C ATOM 2694 C GLY A1156 12.599 21.360 22.779 1.00 95.84 C ANISOU 2694 C GLY A1156 12220 15728 8467 2956 -218 -500 C ATOM 2695 O GLY A1156 12.309 22.454 22.294 1.00 94.50 O ANISOU 2695 O GLY A1156 11938 15571 8397 2768 -157 -516 O ATOM 2696 N THR A1157 11.845 20.748 23.686 1.00 92.87 N ANISOU 2696 N THR A1157 12035 15189 8062 2993 -220 -433 N ATOM 2697 CA THR A1157 10.593 21.323 24.163 1.00 91.85 C ANISOU 2697 CA THR A1157 11976 14895 8026 2811 -149 -372 C ATOM 2698 C THR A1157 10.854 22.446 25.161 1.00 96.79 C ANISOU 2698 C THR A1157 12497 15632 8646 2713 -132 -412 C ATOM 2699 O THR A1157 10.639 22.285 26.363 1.00 97.41 O ANISOU 2699 O THR A1157 12676 15665 8670 2740 -143 -391 O ATOM 2700 CB THR A1157 9.692 20.263 24.823 1.00 99.75 C ANISOU 2700 CB THR A1157 13226 15685 8989 2868 -148 -293 C ATOM 2701 OG1 THR A1157 10.174 18.953 24.498 1.00100.85 O ANISOU 2701 OG1 THR A1157 13493 15801 9025 3069 -203 -290 O ATOM 2702 CG2 THR A1157 8.258 20.405 24.337 1.00 96.27 C ANISOU 2702 CG2 THR A1157 12857 15054 8668 2694 -68 -217 C ATOM 2703 N TRP A1158 11.315 23.585 24.655 1.00 92.86 N ANISOU 2703 N TRP A1158 11815 15272 8194 2590 -99 -473 N ATOM 2704 CA TRP A1158 11.579 24.748 25.494 1.00 92.68 C ANISOU 2704 CA TRP A1158 11705 15353 8156 2466 -66 -518 C ATOM 2705 C TRP A1158 10.888 25.981 24.925 1.00 95.75 C ANISOU 2705 C TRP A1158 12043 15674 8664 2255 42 -505 C ATOM 2706 O TRP A1158 11.540 26.890 24.411 1.00 95.64 O ANISOU 2706 O TRP A1158 11889 15799 8652 2160 71 -578 O ATOM 2707 CB TRP A1158 13.084 24.995 25.612 1.00 92.51 C ANISOU 2707 CB TRP A1158 11512 15617 8023 2524 -130 -626 C ATOM 2708 CG TRP A1158 13.849 23.808 26.114 1.00 94.74 C ANISOU 2708 CG TRP A1158 11829 15995 8174 2766 -239 -636 C ATOM 2709 CD1 TRP A1158 14.620 22.959 25.377 1.00 98.40 C ANISOU 2709 CD1 TRP A1158 12247 16560 8582 2947 -303 -663 C ATOM 2710 CD2 TRP A1158 13.915 23.339 27.466 1.00 95.50 C ANISOU 2710 CD2 TRP A1158 12030 16089 8168 2867 -292 -617 C ATOM 2711 NE1 TRP A1158 15.163 21.990 26.185 1.00 99.22 N ANISOU 2711 NE1 TRP A1158 12420 16727 8550 3170 -391 -657 N ATOM 2712 CE2 TRP A1158 14.746 22.201 27.473 1.00100.78 C ANISOU 2712 CE2 TRP A1158 12712 16864 8717 3123 -390 -630 C ATOM 2713 CE3 TRP A1158 13.353 23.771 28.672 1.00 96.65 C ANISOU 2713 CE3 TRP A1158 12267 16149 8306 2773 -262 -588 C ATOM 2714 CZ2 TRP A1158 15.028 21.490 28.637 1.00101.37 C ANISOU 2714 CZ2 TRP A1158 12893 16962 8660 3292 -462 -614 C ATOM 2715 CZ3 TRP A1158 13.635 23.063 29.826 1.00 99.33 C ANISOU 2715 CZ3 TRP A1158 12709 16510 8521 2924 -335 -576 C ATOM 2716 CH2 TRP A1158 14.464 21.935 29.801 1.00101.26 C ANISOU 2716 CH2 TRP A1158 12968 16862 8643 3183 -437 -589 C ATOM 2717 N ASP A1159 9.562 26.004 25.016 1.00 91.35 N ANISOU 2717 N ASP A1159 11606 14907 8197 2185 107 -413 N ATOM 2718 CA ASP A1159 8.771 27.110 24.466 1.00118.08 C ANISOU 2718 CA ASP A1159 14960 18213 11692 2017 214 -383 C ATOM 2719 C ASP A1159 7.605 27.484 25.384 1.00141.83 C ANISOU 2719 C ASP A1159 18079 21064 14745 1940 292 -305 C ATOM 2720 O ASP A1159 7.696 27.325 26.600 1.00101.15 O ANISOU 2720 O ASP A1159 12998 15908 9528 1968 275 -307 O ATOM 2721 CB ASP A1159 8.284 26.799 23.034 1.00119.22 C ANISOU 2721 CB ASP A1159 15089 18286 11923 2013 223 -345 C ATOM 2722 CG ASP A1159 7.210 25.727 22.901 1.00129.29 C ANISOU 2722 CG ASP A1159 16497 19390 13236 2062 210 -250 C ATOM 2723 OD1 ASP A1159 6.412 25.805 21.942 1.00128.74 O ANISOU 2723 OD1 ASP A1159 16425 19238 13253 1998 248 -196 O ATOM 2724 OD2 ASP A1159 7.182 24.798 23.743 1.00136.72 O ANISOU 2724 OD2 ASP A1159 17551 20285 14110 2160 161 -231 O ATOM 2725 N ARG A 235 9.631 19.531 33.726 1.00 61.07 N ANISOU 2725 N ARG A 235 8765 7646 6793 1508 242 -968 N ATOM 2726 CA ARG A 235 8.986 18.471 34.492 1.00 60.32 C ANISOU 2726 CA ARG A 235 8603 7463 6851 1462 126 -1063 C ATOM 2727 C ARG A 235 9.881 17.989 35.628 1.00 63.67 C ANISOU 2727 C ARG A 235 8943 7818 7432 1349 152 -1014 C ATOM 2728 O ARG A 235 9.488 18.014 36.794 1.00 62.00 O ANISOU 2728 O ARG A 235 8697 7526 7335 1242 113 -974 O ATOM 2729 CB ARG A 235 8.617 17.300 33.579 1.00 61.64 C ANISOU 2729 CB ARG A 235 8756 7661 7004 1586 42 -1231 C ATOM 2730 CG ARG A 235 7.432 16.482 34.068 1.00 74.17 C ANISOU 2730 CG ARG A 235 10301 9161 8720 1568 -95 -1338 C ATOM 2731 CD ARG A 235 7.818 15.028 34.285 1.00 88.19 C ANISOU 2731 CD ARG A 235 11980 10886 10643 1571 -152 -1437 C ATOM 2732 NE ARG A 235 8.883 14.886 35.274 1.00 98.35 N ANISOU 2732 NE ARG A 235 13208 12124 12036 1458 -91 -1340 N ATOM 2733 CZ ARG A 235 9.351 13.720 35.706 1.00113.07 C ANISOU 2733 CZ ARG A 235 14984 13928 14050 1432 -134 -1392 C ATOM 2734 NH1 ARG A 235 10.323 13.686 36.608 1.00100.09 N ANISOU 2734 NH1 ARG A 235 13296 12241 12491 1333 -82 -1299 N ATOM 2735 NH2 ARG A 235 8.847 12.586 35.238 1.00100.87 N ANISOU 2735 NH2 ARG A 235 13391 12359 12577 1508 -237 -1541 N ATOM 2736 N LYS A 236 11.086 17.550 35.280 1.00 60.95 N ANISOU 2736 N LYS A 236 8564 7507 7087 1378 218 -1020 N ATOM 2737 CA LYS A 236 12.048 17.057 36.279 1.00 59.96 C ANISOU 2737 CA LYS A 236 8358 7317 7108 1284 239 -982 C ATOM 2738 C LYS A 236 12.505 18.215 37.174 1.00 62.68 C ANISOU 2738 C LYS A 236 8709 7635 7471 1177 320 -832 C ATOM 2739 O LYS A 236 12.740 18.011 38.364 1.00 61.28 O ANISOU 2739 O LYS A 236 8477 7384 7422 1077 299 -791 O ATOM 2740 CB LYS A 236 13.259 16.410 35.582 1.00 63.19 C ANISOU 2740 CB LYS A 236 8730 7775 7506 1348 294 -1033 C ATOM 2741 CG LYS A 236 14.112 15.528 36.489 1.00 75.78 C ANISOU 2741 CG LYS A 236 10232 9290 9271 1274 275 -1041 C ATOM 2742 CD LYS A 236 15.412 15.123 35.803 1.00 85.52 C ANISOU 2742 CD LYS A 236 11429 10577 10489 1330 348 -1083 C ATOM 2743 CE LYS A 236 16.174 14.049 36.550 1.00 92.80 C ANISOU 2743 CE LYS A 236 12255 11417 11587 1277 303 -1123 C ATOM 2744 NZ LYS A 236 16.803 14.560 37.799 1.00 98.23 N ANISOU 2744 NZ LYS A 236 12919 12035 12370 1155 343 -1002 N ATOM 2745 N ALA A 237 12.632 19.426 36.585 1.00 59.58 N ANISOU 2745 N ALA A 237 8379 7305 6951 1205 409 -752 N ATOM 2746 CA ALA A 237 13.017 20.666 37.263 1.00 58.56 C ANISOU 2746 CA ALA A 237 8256 7158 6838 1121 486 -616 C ATOM 2747 C ALA A 237 11.905 21.096 38.219 1.00 60.50 C ANISOU 2747 C ALA A 237 8505 7345 7135 1041 408 -592 C ATOM 2748 O ALA A 237 12.200 21.552 39.324 1.00 59.54 O ANISOU 2748 O ALA A 237 8343 7175 7104 942 424 -518 O ATOM 2749 CB ALA A 237 13.292 21.764 36.240 1.00 60.09 C ANISOU 2749 CB ALA A 237 8515 7429 6886 1185 590 -543 C ATOM 2750 N LEU A 238 10.630 20.921 37.797 1.00 55.84 N ANISOU 2750 N LEU A 238 7960 6763 6493 1089 321 -664 N ATOM 2751 CA LEU A 238 9.429 21.229 38.577 1.00 54.12 C ANISOU 2751 CA LEU A 238 7746 6496 6321 1025 240 -666 C ATOM 2752 C LEU A 238 9.306 20.278 39.780 1.00 55.06 C ANISOU 2752 C LEU A 238 7790 6538 6591 939 173 -695 C ATOM 2753 O LEU A 238 8.938 20.724 40.863 1.00 53.63 O ANISOU 2753 O LEU A 238 7585 6316 6474 844 155 -644 O ATOM 2754 CB LEU A 238 8.179 21.160 37.670 1.00 54.77 C ANISOU 2754 CB LEU A 238 7891 6605 6314 1115 164 -757 C ATOM 2755 CG LEU A 238 6.786 21.257 38.317 1.00 59.13 C ANISOU 2755 CG LEU A 238 8443 7104 6921 1064 66 -796 C ATOM 2756 CD1 LEU A 238 6.492 22.660 38.818 1.00 58.81 C ANISOU 2756 CD1 LEU A 238 8426 7059 6860 998 95 -700 C ATOM 2757 CD2 LEU A 238 5.709 20.843 37.337 1.00 62.72 C ANISOU 2757 CD2 LEU A 238 8943 7576 7310 1171 -19 -918 C ATOM 2758 N LYS A 239 9.649 18.986 39.597 1.00 50.30 N ANISOU 2758 N LYS A 239 7147 5919 6047 973 138 -773 N ATOM 2759 CA LYS A 239 9.602 17.976 40.660 1.00 48.56 C ANISOU 2759 CA LYS A 239 6855 5621 5975 899 74 -792 C ATOM 2760 C LYS A 239 10.641 18.250 41.754 1.00 49.30 C ANISOU 2760 C LYS A 239 6902 5687 6143 805 130 -692 C ATOM 2761 O LYS A 239 10.320 18.100 42.929 1.00 47.90 O ANISOU 2761 O LYS A 239 6689 5459 6054 716 89 -658 O ATOM 2762 CB LYS A 239 9.769 16.553 40.085 1.00 51.60 C ANISOU 2762 CB LYS A 239 7202 5991 6413 969 19 -904 C ATOM 2763 CG LYS A 239 9.438 15.441 41.086 1.00 60.32 C ANISOU 2763 CG LYS A 239 8236 7005 7678 901 -64 -928 C ATOM 2764 CD LYS A 239 9.650 14.047 40.519 1.00 66.66 C ANISOU 2764 CD LYS A 239 8988 7783 8557 970 -125 -1040 C ATOM 2765 CE LYS A 239 9.474 12.998 41.591 1.00 71.35 C ANISOU 2765 CE LYS A 239 9509 8278 9324 893 -197 -1035 C ATOM 2766 NZ LYS A 239 9.306 11.643 41.013 1.00 78.36 N ANISOU 2766 NZ LYS A 239 10340 9125 10307 963 -281 -1161 N ATOM 2767 N THR A 240 11.872 18.640 41.369 1.00 44.93 N ANISOU 2767 N THR A 240 6347 5169 5554 828 221 -649 N ATOM 2768 CA THR A 240 12.972 18.926 42.295 1.00 44.00 C ANISOU 2768 CA THR A 240 6182 5025 5511 753 275 -568 C ATOM 2769 C THR A 240 12.615 20.035 43.295 1.00 46.04 C ANISOU 2769 C THR A 240 6441 5271 5780 668 286 -481 C ATOM 2770 O THR A 240 12.835 19.859 44.495 1.00 44.90 O ANISOU 2770 O THR A 240 6248 5084 5727 589 261 -445 O ATOM 2771 CB THR A 240 14.282 19.148 41.532 1.00 54.65 C ANISOU 2771 CB THR A 240 7527 6414 6823 804 375 -553 C ATOM 2772 OG1 THR A 240 14.529 18.007 40.710 1.00 56.84 O ANISOU 2772 OG1 THR A 240 7793 6705 7100 881 350 -651 O ATOM 2773 CG2 THR A 240 15.476 19.365 42.455 1.00 53.60 C ANISOU 2773 CG2 THR A 240 7336 6243 6785 736 425 -487 C ATOM 2774 N THR A 241 12.023 21.145 42.806 1.00 41.72 N ANISOU 2774 N THR A 241 5947 4764 5142 688 314 -454 N ATOM 2775 CA THR A 241 11.583 22.265 43.646 1.00 40.28 C ANISOU 2775 CA THR A 241 5760 4574 4969 615 316 -387 C ATOM 2776 C THR A 241 10.349 21.914 44.492 1.00 43.16 C ANISOU 2776 C THR A 241 6114 4908 5376 559 221 -420 C ATOM 2777 O THR A 241 10.292 22.320 45.653 1.00 42.29 O ANISOU 2777 O THR A 241 5965 4781 5322 478 210 -375 O ATOM 2778 CB THR A 241 11.486 23.581 42.863 1.00 46.42 C ANISOU 2778 CB THR A 241 6588 5394 5654 653 378 -340 C ATOM 2779 OG1 THR A 241 10.874 24.557 43.702 1.00 46.84 O ANISOU 2779 OG1 THR A 241 6630 5436 5734 583 357 -297 O ATOM 2780 CG2 THR A 241 10.678 23.458 41.598 1.00 44.57 C ANISOU 2780 CG2 THR A 241 6428 5200 5308 745 355 -397 C ATOM 2781 N VAL A 242 9.380 21.148 43.915 1.00 39.28 N ANISOU 2781 N VAL A 242 5651 4411 4862 605 153 -503 N ATOM 2782 CA VAL A 242 8.168 20.662 44.596 1.00 38.05 C ANISOU 2782 CA VAL A 242 5480 4219 4758 559 67 -545 C ATOM 2783 C VAL A 242 8.585 19.798 45.798 1.00 41.98 C ANISOU 2783 C VAL A 242 5912 4671 5368 484 42 -518 C ATOM 2784 O VAL A 242 8.135 20.067 46.915 1.00 41.33 O ANISOU 2784 O VAL A 242 5802 4576 5325 403 21 -481 O ATOM 2785 CB VAL A 242 7.199 19.930 43.623 1.00 41.63 C ANISOU 2785 CB VAL A 242 5967 4668 5184 637 2 -652 C ATOM 2786 CG1 VAL A 242 6.285 18.939 44.344 1.00 40.99 C ANISOU 2786 CG1 VAL A 242 5844 4527 5204 591 -82 -701 C ATOM 2787 CG2 VAL A 242 6.374 20.922 42.820 1.00 41.50 C ANISOU 2787 CG2 VAL A 242 6016 4689 5063 687 -2 -673 C ATOM 2788 N ILE A 243 9.494 18.815 45.582 1.00 38.74 N ANISOU 2788 N ILE A 243 5476 4240 5005 514 47 -534 N ATOM 2789 CA ILE A 243 9.979 17.959 46.664 1.00 38.39 C ANISOU 2789 CA ILE A 243 5372 4146 5066 451 19 -503 C ATOM 2790 C ILE A 243 10.889 18.705 47.657 1.00 42.10 C ANISOU 2790 C ILE A 243 5814 4626 5554 388 69 -414 C ATOM 2791 O ILE A 243 11.052 18.245 48.786 1.00 41.73 O ANISOU 2791 O ILE A 243 5726 4549 5579 325 38 -375 O ATOM 2792 CB ILE A 243 10.502 16.552 46.230 1.00 42.01 C ANISOU 2792 CB ILE A 243 5801 4564 5596 496 -15 -560 C ATOM 2793 CG1 ILE A 243 11.984 16.536 45.868 1.00 42.49 C ANISOU 2793 CG1 ILE A 243 5848 4639 5660 529 45 -547 C ATOM 2794 CG2 ILE A 243 9.620 15.848 45.192 1.00 43.56 C ANISOU 2794 CG2 ILE A 243 6016 4754 5783 572 -70 -665 C ATOM 2795 CD1 ILE A 243 12.759 15.780 46.879 1.00 47.98 C ANISOU 2795 CD1 ILE A 243 6485 5279 6465 475 20 -509 C ATOM 2796 N LEU A 244 11.470 19.851 47.240 1.00 38.33 N ANISOU 2796 N LEU A 244 5357 4191 5017 409 142 -382 N ATOM 2797 CA LEU A 244 12.305 20.678 48.113 1.00 37.74 C ANISOU 2797 CA LEU A 244 5248 4123 4970 358 187 -310 C ATOM 2798 C LEU A 244 11.386 21.438 49.068 1.00 41.80 C ANISOU 2798 C LEU A 244 5754 4653 5477 291 157 -282 C ATOM 2799 O LEU A 244 11.647 21.450 50.275 1.00 41.82 O ANISOU 2799 O LEU A 244 5712 4648 5529 231 140 -243 O ATOM 2800 CB LEU A 244 13.197 21.658 47.307 1.00 37.94 C ANISOU 2800 CB LEU A 244 5286 4177 4951 403 279 -285 C ATOM 2801 CG LEU A 244 14.009 22.724 48.085 1.00 41.85 C ANISOU 2801 CG LEU A 244 5739 4675 5487 359 329 -220 C ATOM 2802 CD1 LEU A 244 15.042 22.084 49.011 1.00 42.21 C ANISOU 2802 CD1 LEU A 244 5726 4685 5626 327 317 -207 C ATOM 2803 CD2 LEU A 244 14.701 23.682 47.135 1.00 43.08 C ANISOU 2803 CD2 LEU A 244 5909 4852 5605 406 424 -192 C ATOM 2804 N ILE A 245 10.308 22.062 48.527 1.00 37.78 N ANISOU 2804 N ILE A 245 5286 4167 4902 306 147 -308 N ATOM 2805 CA ILE A 245 9.334 22.832 49.310 1.00 36.84 C ANISOU 2805 CA ILE A 245 5157 4066 4775 247 117 -298 C ATOM 2806 C ILE A 245 8.526 21.907 50.234 1.00 40.88 C ANISOU 2806 C ILE A 245 5644 4556 5333 192 50 -314 C ATOM 2807 O ILE A 245 8.339 22.240 51.411 1.00 40.37 O ANISOU 2807 O ILE A 245 5541 4508 5289 125 36 -281 O ATOM 2808 CB ILE A 245 8.475 23.798 48.435 1.00 39.65 C ANISOU 2808 CB ILE A 245 5561 4445 5057 282 121 -325 C ATOM 2809 CG1 ILE A 245 9.389 24.790 47.676 1.00 40.02 C ANISOU 2809 CG1 ILE A 245 5625 4512 5069 326 199 -282 C ATOM 2810 CG2 ILE A 245 7.460 24.572 49.290 1.00 39.86 C ANISOU 2810 CG2 ILE A 245 5567 4488 5088 217 83 -328 C ATOM 2811 CD1 ILE A 245 8.861 25.297 46.373 1.00 46.00 C ANISOU 2811 CD1 ILE A 245 6448 5288 5739 396 211 -303 C ATOM 2812 N LEU A 246 8.116 20.725 49.725 1.00 37.58 N ANISOU 2812 N LEU A 246 5242 4103 4935 223 11 -362 N ATOM 2813 CA LEU A 246 7.385 19.737 50.515 1.00 37.29 C ANISOU 2813 CA LEU A 246 5177 4034 4959 174 -46 -368 C ATOM 2814 C LEU A 246 8.228 19.216 51.686 1.00 40.66 C ANISOU 2814 C LEU A 246 5556 4446 5446 121 -47 -300 C ATOM 2815 O LEU A 246 7.691 19.052 52.784 1.00 40.53 O ANISOU 2815 O LEU A 246 5512 4434 5454 55 -73 -268 O ATOM 2816 CB LEU A 246 6.867 18.584 49.644 1.00 37.82 C ANISOU 2816 CB LEU A 246 5258 4054 5057 226 -90 -440 C ATOM 2817 CG LEU A 246 5.405 18.704 49.215 1.00 42.65 C ANISOU 2817 CG LEU A 246 5894 4661 5651 237 -131 -510 C ATOM 2818 CD1 LEU A 246 5.176 18.079 47.860 1.00 43.25 C ANISOU 2818 CD1 LEU A 246 6000 4716 5719 332 -158 -600 C ATOM 2819 CD2 LEU A 246 4.469 18.076 50.244 1.00 45.83 C ANISOU 2819 CD2 LEU A 246 6255 5030 6126 163 -174 -502 C ATOM 2820 N ALA A 247 9.545 19.005 51.469 1.00 36.05 N ANISOU 2820 N ALA A 247 4963 3851 4882 153 -18 -280 N ATOM 2821 CA ALA A 247 10.446 18.532 52.521 1.00 35.40 C ANISOU 2821 CA ALA A 247 4840 3753 4859 114 -26 -221 C ATOM 2822 C ALA A 247 10.768 19.635 53.519 1.00 39.13 C ANISOU 2822 C ALA A 247 5288 4274 5307 70 -1 -171 C ATOM 2823 O ALA A 247 10.998 19.333 54.695 1.00 39.30 O ANISOU 2823 O ALA A 247 5275 4297 5359 23 -26 -123 O ATOM 2824 CB ALA A 247 11.721 17.963 51.927 1.00 36.32 C ANISOU 2824 CB ALA A 247 4949 3837 5015 165 -7 -232 C ATOM 2825 N PHE A 248 10.779 20.914 53.064 1.00 34.63 N ANISOU 2825 N PHE A 248 4730 3742 4686 87 43 -183 N ATOM 2826 CA PHE A 248 11.053 22.059 53.940 1.00 33.65 C ANISOU 2826 CA PHE A 248 4571 3661 4554 52 61 -152 C ATOM 2827 C PHE A 248 9.993 22.194 55.029 1.00 37.51 C ANISOU 2827 C PHE A 248 5039 4186 5026 -12 20 -143 C ATOM 2828 O PHE A 248 10.341 22.362 56.197 1.00 37.00 O ANISOU 2828 O PHE A 248 4932 4150 4974 -49 7 -108 O ATOM 2829 CB PHE A 248 11.212 23.370 53.152 1.00 34.94 C ANISOU 2829 CB PHE A 248 4746 3847 4684 84 113 -164 C ATOM 2830 CG PHE A 248 11.521 24.567 54.024 1.00 35.71 C ANISOU 2830 CG PHE A 248 4792 3980 4796 53 125 -142 C ATOM 2831 CD1 PHE A 248 12.818 24.821 54.451 1.00 38.34 C ANISOU 2831 CD1 PHE A 248 5080 4303 5183 61 153 -117 C ATOM 2832 CD2 PHE A 248 10.515 25.445 54.411 1.00 37.18 C ANISOU 2832 CD2 PHE A 248 4967 4206 4953 18 104 -158 C ATOM 2833 CE1 PHE A 248 13.100 25.921 55.260 1.00 38.97 C ANISOU 2833 CE1 PHE A 248 5102 4414 5291 39 156 -110 C ATOM 2834 CE2 PHE A 248 10.798 26.542 55.226 1.00 39.55 C ANISOU 2834 CE2 PHE A 248 5207 4540 5278 -6 107 -152 C ATOM 2835 CZ PHE A 248 12.090 26.776 55.641 1.00 37.72 C ANISOU 2835 CZ PHE A 248 4928 4299 5103 7 131 -128 C ATOM 2836 N PHE A 249 8.708 22.108 54.651 1.00 34.25 N ANISOU 2836 N PHE A 249 4654 3776 4584 -22 -2 -180 N ATOM 2837 CA PHE A 249 7.621 22.195 55.616 1.00 33.95 C ANISOU 2837 CA PHE A 249 4594 3772 4533 -84 -35 -180 C ATOM 2838 C PHE A 249 7.449 20.897 56.420 1.00 39.15 C ANISOU 2838 C PHE A 249 5239 4409 5229 -121 -67 -141 C ATOM 2839 O PHE A 249 6.865 20.926 57.507 1.00 38.69 O ANISOU 2839 O PHE A 249 5151 4390 5158 -178 -83 -116 O ATOM 2840 CB PHE A 249 6.328 22.694 54.959 1.00 35.27 C ANISOU 2840 CB PHE A 249 4789 3946 4668 -82 -46 -241 C ATOM 2841 CG PHE A 249 6.437 24.133 54.503 1.00 36.30 C ANISOU 2841 CG PHE A 249 4922 4106 4764 -61 -21 -261 C ATOM 2842 CD1 PHE A 249 6.443 25.176 55.427 1.00 38.90 C ANISOU 2842 CD1 PHE A 249 5201 4489 5089 -101 -21 -253 C ATOM 2843 CD2 PHE A 249 6.553 24.446 53.155 1.00 38.51 C ANISOU 2843 CD2 PHE A 249 5250 4363 5020 3 0 -287 C ATOM 2844 CE1 PHE A 249 6.564 26.504 55.009 1.00 39.46 C ANISOU 2844 CE1 PHE A 249 5266 4577 5152 -82 -2 -268 C ATOM 2845 CE2 PHE A 249 6.663 25.777 52.736 1.00 41.18 C ANISOU 2845 CE2 PHE A 249 5590 4721 5336 21 25 -290 C ATOM 2846 CZ PHE A 249 6.669 26.796 53.667 1.00 38.82 C ANISOU 2846 CZ PHE A 249 5235 4462 5051 -24 22 -280 C ATOM 2847 N ALA A 250 8.018 19.776 55.911 1.00 36.47 N ANISOU 2847 N ALA A 250 4913 4007 4937 -88 -76 -131 N ATOM 2848 CA ALA A 250 8.007 18.480 56.585 1.00 36.84 C ANISOU 2848 CA ALA A 250 4944 4015 5039 -118 -110 -84 C ATOM 2849 C ALA A 250 8.925 18.525 57.811 1.00 41.78 C ANISOU 2849 C ALA A 250 5537 4671 5666 -145 -113 -13 C ATOM 2850 O ALA A 250 8.520 18.050 58.872 1.00 41.68 O ANISOU 2850 O ALA A 250 5505 4675 5655 -195 -134 41 O ATOM 2851 CB ALA A 250 8.437 17.376 55.631 1.00 37.88 C ANISOU 2851 CB ALA A 250 5090 4070 5233 -67 -126 -108 C ATOM 2852 N CYS A 251 10.135 19.139 57.677 1.00 38.88 N ANISOU 2852 N CYS A 251 5162 4314 5296 -110 -89 -15 N ATOM 2853 CA CYS A 251 11.110 19.320 58.767 1.00 39.21 C ANISOU 2853 CA CYS A 251 5171 4385 5344 -121 -96 34 C ATOM 2854 C CYS A 251 10.505 20.204 59.846 1.00 44.24 C ANISOU 2854 C CYS A 251 5779 5108 5922 -165 -99 46 C ATOM 2855 O CYS A 251 10.664 19.922 61.033 1.00 44.53 O ANISOU 2855 O CYS A 251 5792 5179 5946 -193 -124 98 O ATOM 2856 CB CYS A 251 12.413 19.925 58.246 1.00 39.31 C ANISOU 2856 CB CYS A 251 5173 4384 5380 -71 -64 11 C ATOM 2857 SG CYS A 251 13.289 18.903 57.043 1.00 43.50 S ANISOU 2857 SG CYS A 251 5725 4826 5976 -15 -57 -13 S ATOM 2858 N TRP A 252 9.819 21.283 59.419 1.00 40.90 N ANISOU 2858 N TRP A 252 5358 4723 5461 -167 -76 -6 N ATOM 2859 CA TRP A 252 9.178 22.268 60.283 1.00 40.64 C ANISOU 2859 CA TRP A 252 5290 4773 5378 -205 -79 -18 C ATOM 2860 C TRP A 252 7.813 21.863 60.846 1.00 44.90 C ANISOU 2860 C TRP A 252 5830 5345 5885 -261 -96 -11 C ATOM 2861 O TRP A 252 7.346 22.518 61.785 1.00 44.68 O ANISOU 2861 O TRP A 252 5765 5399 5813 -296 -102 -16 O ATOM 2862 CB TRP A 252 9.118 23.632 59.594 1.00 38.95 C ANISOU 2862 CB TRP A 252 5067 4576 5155 -183 -53 -77 C ATOM 2863 CG TRP A 252 10.441 24.330 59.580 1.00 40.06 C ANISOU 2863 CG TRP A 252 5177 4712 5330 -144 -33 -77 C ATOM 2864 CD1 TRP A 252 11.260 24.513 58.507 1.00 42.91 C ANISOU 2864 CD1 TRP A 252 5557 5019 5728 -95 4 -86 C ATOM 2865 CD2 TRP A 252 11.123 24.893 60.710 1.00 39.98 C ANISOU 2865 CD2 TRP A 252 5108 4755 5329 -147 -48 -69 C ATOM 2866 NE1 TRP A 252 12.403 25.174 58.891 1.00 42.55 N ANISOU 2866 NE1 TRP A 252 5463 4979 5725 -73 18 -84 N ATOM 2867 CE2 TRP A 252 12.347 25.416 60.240 1.00 44.13 C ANISOU 2867 CE2 TRP A 252 5613 5242 5913 -101 -20 -79 C ATOM 2868 CE3 TRP A 252 10.816 25.013 62.078 1.00 41.38 C ANISOU 2868 CE3 TRP A 252 5243 5012 5468 -181 -83 -61 C ATOM 2869 CZ2 TRP A 252 13.262 26.054 61.088 1.00 43.65 C ANISOU 2869 CZ2 TRP A 252 5487 5210 5888 -86 -31 -88 C ATOM 2870 CZ3 TRP A 252 11.727 25.634 62.918 1.00 42.98 C ANISOU 2870 CZ3 TRP A 252 5385 5255 5691 -160 -99 -70 C ATOM 2871 CH2 TRP A 252 12.929 26.152 62.423 1.00 43.66 C ANISOU 2871 CH2 TRP A 252 5447 5291 5850 -112 -76 -88 C ATOM 2872 N LEU A 253 7.183 20.787 60.301 1.00 41.21 N ANISOU 2872 N LEU A 253 5395 4815 5447 -268 -104 -3 N ATOM 2873 CA LEU A 253 5.884 20.294 60.776 1.00 41.00 C ANISOU 2873 CA LEU A 253 5364 4803 5412 -322 -114 6 C ATOM 2874 C LEU A 253 5.886 19.843 62.254 1.00 46.70 C ANISOU 2874 C LEU A 253 6056 5581 6107 -370 -123 86 C ATOM 2875 O LEU A 253 5.013 20.320 62.976 1.00 46.73 O ANISOU 2875 O LEU A 253 6033 5659 6063 -415 -116 76 O ATOM 2876 CB LEU A 253 5.251 19.231 59.845 1.00 40.82 C ANISOU 2876 CB LEU A 253 5372 4690 5449 -313 -124 -12 C ATOM 2877 CG LEU A 253 3.894 18.636 60.271 1.00 44.84 C ANISOU 2877 CG LEU A 253 5868 5194 5976 -369 -130 -6 C ATOM 2878 CD1 LEU A 253 2.750 19.601 60.019 1.00 44.18 C ANISOU 2878 CD1 LEU A 253 5780 5150 5858 -387 -123 -88 C ATOM 2879 CD2 LEU A 253 3.626 17.360 59.543 1.00 47.67 C ANISOU 2879 CD2 LEU A 253 6241 5449 6422 -352 -150 -8 C ATOM 2880 N PRO A 254 6.826 18.998 62.762 1.00 44.29 N ANISOU 2880 N PRO A 254 5752 5251 5826 -360 -139 163 N ATOM 2881 CA PRO A 254 6.759 18.620 64.188 1.00 44.70 C ANISOU 2881 CA PRO A 254 5782 5367 5835 -401 -149 247 C ATOM 2882 C PRO A 254 6.969 19.801 65.136 1.00 48.47 C ANISOU 2882 C PRO A 254 6221 5965 6229 -403 -147 227 C ATOM 2883 O PRO A 254 6.413 19.804 66.237 1.00 48.52 O ANISOU 2883 O PRO A 254 6204 6057 6173 -444 -144 266 O ATOM 2884 CB PRO A 254 7.845 17.545 64.333 1.00 46.96 C ANISOU 2884 CB PRO A 254 6082 5587 6174 -376 -177 322 C ATOM 2885 CG PRO A 254 8.160 17.107 62.943 1.00 51.38 C ANISOU 2885 CG PRO A 254 6668 6039 6816 -335 -180 274 C ATOM 2886 CD PRO A 254 7.961 18.322 62.099 1.00 46.20 C ANISOU 2886 CD PRO A 254 6015 5408 6131 -311 -153 177 C ATOM 2887 N TYR A 255 7.730 20.820 64.695 1.00 44.39 N ANISOU 2887 N TYR A 255 5692 5456 5717 -359 -145 163 N ATOM 2888 CA TYR A 255 7.951 22.032 65.481 1.00 43.94 C ANISOU 2888 CA TYR A 255 5587 5504 5606 -353 -150 124 C ATOM 2889 C TYR A 255 6.687 22.896 65.528 1.00 47.48 C ANISOU 2889 C TYR A 255 6010 6018 6014 -391 -136 58 C ATOM 2890 O TYR A 255 6.372 23.412 66.602 1.00 47.99 O ANISOU 2890 O TYR A 255 6028 6190 6015 -413 -144 49 O ATOM 2891 CB TYR A 255 9.154 22.834 64.960 1.00 44.57 C ANISOU 2891 CB TYR A 255 5651 5555 5729 -295 -151 77 C ATOM 2892 CG TYR A 255 9.462 24.069 65.777 1.00 45.64 C ANISOU 2892 CG TYR A 255 5721 5785 5833 -281 -165 28 C ATOM 2893 CD1 TYR A 255 10.046 23.969 67.034 1.00 48.16 C ANISOU 2893 CD1 TYR A 255 6007 6177 6113 -270 -196 60 C ATOM 2894 CD2 TYR A 255 9.167 25.340 65.292 1.00 45.57 C ANISOU 2894 CD2 TYR A 255 5679 5794 5840 -275 -153 -54 C ATOM 2895 CE1 TYR A 255 10.333 25.103 67.791 1.00 49.17 C ANISOU 2895 CE1 TYR A 255 6065 6395 6220 -248 -217 0 C ATOM 2896 CE2 TYR A 255 9.467 26.483 66.032 1.00 46.48 C ANISOU 2896 CE2 TYR A 255 5722 5990 5949 -259 -173 -108 C ATOM 2897 CZ TYR A 255 10.057 26.359 67.280 1.00 54.41 C ANISOU 2897 CZ TYR A 255 6688 7069 6916 -243 -206 -88 C ATOM 2898 OH TYR A 255 10.339 27.473 68.034 1.00 54.53 O ANISOU 2898 OH TYR A 255 6621 7168 6930 -219 -234 -156 O ATOM 2899 N TYR A 256 5.968 23.055 64.380 1.00 42.58 N ANISOU 2899 N TYR A 256 5414 5335 5428 -395 -121 4 N ATOM 2900 CA TYR A 256 4.718 23.828 64.297 1.00 41.64 C ANISOU 2900 CA TYR A 256 5275 5262 5286 -430 -115 -68 C ATOM 2901 C TYR A 256 3.709 23.316 65.336 1.00 46.34 C ANISOU 2901 C TYR A 256 5850 5926 5833 -492 -109 -35 C ATOM 2902 O TYR A 256 3.121 24.120 66.063 1.00 45.85 O ANISOU 2902 O TYR A 256 5738 5963 5721 -519 -111 -81 O ATOM 2903 CB TYR A 256 4.082 23.728 62.898 1.00 41.94 C ANISOU 2903 CB TYR A 256 5358 5210 5369 -419 -108 -117 C ATOM 2904 CG TYR A 256 4.834 24.373 61.756 1.00 42.93 C ANISOU 2904 CG TYR A 256 5505 5279 5528 -361 -102 -153 C ATOM 2905 CD1 TYR A 256 5.692 25.450 61.970 1.00 44.69 C ANISOU 2905 CD1 TYR A 256 5690 5540 5752 -334 -102 -172 C ATOM 2906 CD2 TYR A 256 4.630 23.959 60.439 1.00 43.55 C ANISOU 2906 CD2 TYR A 256 5637 5270 5640 -330 -96 -175 C ATOM 2907 CE1 TYR A 256 6.363 26.066 60.914 1.00 45.47 C ANISOU 2907 CE1 TYR A 256 5804 5584 5886 -284 -87 -195 C ATOM 2908 CE2 TYR A 256 5.290 24.568 59.374 1.00 44.03 C ANISOU 2908 CE2 TYR A 256 5721 5290 5718 -275 -83 -200 C ATOM 2909 CZ TYR A 256 6.154 25.624 59.615 1.00 51.18 C ANISOU 2909 CZ TYR A 256 6590 6230 6627 -256 -73 -204 C ATOM 2910 OH TYR A 256 6.810 26.228 58.567 1.00 51.56 O ANISOU 2910 OH TYR A 256 6658 6235 6698 -205 -49 -217 O ATOM 2911 N ILE A 257 3.543 21.970 65.409 1.00 43.44 N ANISOU 2911 N ILE A 257 5515 5504 5487 -512 -102 45 N ATOM 2912 CA ILE A 257 2.648 21.250 66.321 1.00 43.97 C ANISOU 2912 CA ILE A 257 5568 5615 5524 -572 -85 103 C ATOM 2913 C ILE A 257 2.944 21.599 67.792 1.00 49.09 C ANISOU 2913 C ILE A 257 6174 6399 6079 -584 -86 145 C ATOM 2914 O ILE A 257 2.011 21.893 68.547 1.00 49.19 O ANISOU 2914 O ILE A 257 6150 6506 6034 -631 -67 129 O ATOM 2915 CB ILE A 257 2.661 19.712 66.025 1.00 47.39 C ANISOU 2915 CB ILE A 257 6040 5942 6026 -580 -82 192 C ATOM 2916 CG1 ILE A 257 2.108 19.416 64.606 1.00 47.10 C ANISOU 2916 CG1 ILE A 257 6032 5788 6075 -566 -85 126 C ATOM 2917 CG2 ILE A 257 1.888 18.905 67.089 1.00 49.05 C ANISOU 2917 CG2 ILE A 257 6231 6194 6211 -643 -58 281 C ATOM 2918 CD1 ILE A 257 2.643 18.148 63.940 1.00 52.58 C ANISOU 2918 CD1 ILE A 257 6761 6361 6858 -538 -101 178 C ATOM 2919 N GLY A 258 4.230 21.613 68.154 1.00 45.83 N ANISOU 2919 N GLY A 258 5764 5998 5651 -538 -110 184 N ATOM 2920 CA GLY A 258 4.708 21.940 69.496 1.00 45.98 C ANISOU 2920 CA GLY A 258 5746 6144 5581 -529 -124 215 C ATOM 2921 C GLY A 258 4.316 23.332 69.948 1.00 48.71 C ANISOU 2921 C GLY A 258 6028 6609 5872 -530 -129 111 C ATOM 2922 O GLY A 258 3.651 23.481 70.976 1.00 48.73 O ANISOU 2922 O GLY A 258 5993 6732 5790 -564 -117 115 O ATOM 2923 N ILE A 259 4.688 24.352 69.145 1.00 44.16 N ANISOU 2923 N ILE A 259 5435 5997 5349 -495 -144 15 N ATOM 2924 CA ILE A 259 4.384 25.776 69.362 1.00 43.48 C ANISOU 2924 CA ILE A 259 5279 5996 5245 -490 -159 -99 C ATOM 2925 C ILE A 259 2.864 25.988 69.478 1.00 46.67 C ANISOU 2925 C ILE A 259 5661 6451 5620 -553 -138 -149 C ATOM 2926 O ILE A 259 2.416 26.701 70.383 1.00 45.84 O ANISOU 2926 O ILE A 259 5490 6475 5454 -568 -146 -205 O ATOM 2927 CB ILE A 259 5.052 26.672 68.261 1.00 45.72 C ANISOU 2927 CB ILE A 259 5559 6196 5616 -444 -172 -169 C ATOM 2928 CG1 ILE A 259 6.589 26.494 68.212 1.00 46.02 C ANISOU 2928 CG1 ILE A 259 5607 6187 5692 -383 -188 -128 C ATOM 2929 CG2 ILE A 259 4.658 28.160 68.364 1.00 46.22 C ANISOU 2929 CG2 ILE A 259 5545 6327 5688 -442 -193 -287 C ATOM 2930 CD1 ILE A 259 7.374 26.732 69.552 1.00 54.63 C ANISOU 2930 CD1 ILE A 259 6642 7384 6729 -351 -222 -122 C ATOM 2931 N SER A 260 2.084 25.324 68.587 1.00 43.00 N ANISOU 2931 N SER A 260 5246 5888 5203 -585 -113 -135 N ATOM 2932 CA SER A 260 0.621 25.383 68.543 1.00 42.74 C ANISOU 2932 CA SER A 260 5198 5875 5167 -644 -93 -186 C ATOM 2933 C SER A 260 0.001 24.986 69.879 1.00 47.99 C ANISOU 2933 C SER A 260 5827 6663 5745 -693 -66 -140 C ATOM 2934 O SER A 260 -1.013 25.572 70.261 1.00 48.35 O ANISOU 2934 O SER A 260 5821 6789 5762 -734 -56 -217 O ATOM 2935 CB SER A 260 0.076 24.511 67.417 1.00 45.61 C ANISOU 2935 CB SER A 260 5623 6102 5606 -657 -77 -168 C ATOM 2936 OG SER A 260 0.559 24.937 66.154 1.00 52.18 O ANISOU 2936 OG SER A 260 6488 6836 6500 -608 -97 -215 O ATOM 2937 N ILE A 261 0.630 24.030 70.606 1.00 44.72 N ANISOU 2937 N ILE A 261 5438 6268 5286 -688 -55 -17 N ATOM 2938 CA ILE A 261 0.179 23.578 71.928 1.00 45.07 C ANISOU 2938 CA ILE A 261 5456 6436 5232 -727 -24 54 C ATOM 2939 C ILE A 261 0.449 24.654 73.011 1.00 48.19 C ANISOU 2939 C ILE A 261 5779 7003 5527 -703 -48 -11 C ATOM 2940 O ILE A 261 -0.447 24.919 73.818 1.00 48.18 O ANISOU 2940 O ILE A 261 5728 7125 5452 -744 -21 -41 O ATOM 2941 CB ILE A 261 0.673 22.134 72.272 1.00 48.87 C ANISOU 2941 CB ILE A 261 5992 6867 5709 -730 -8 218 C ATOM 2942 CG1 ILE A 261 0.090 21.111 71.263 1.00 49.19 C ANISOU 2942 CG1 ILE A 261 6080 6749 5862 -763 15 257 C ATOM 2943 CG2 ILE A 261 0.303 21.724 73.706 1.00 50.65 C ANISOU 2943 CG2 ILE A 261 6194 7234 5816 -763 26 308 C ATOM 2944 CD1 ILE A 261 0.892 19.822 71.081 1.00 55.88 C ANISOU 2944 CD1 ILE A 261 6983 7489 6761 -744 5 387 C ATOM 2945 N ASP A 262 1.638 25.320 72.983 1.00 43.82 N ANISOU 2945 N ASP A 262 5212 6455 4982 -634 -97 -48 N ATOM 2946 CA ASP A 262 1.985 26.404 73.930 1.00 43.55 C ANISOU 2946 CA ASP A 262 5098 6573 4876 -597 -133 -130 C ATOM 2947 C ASP A 262 1.092 27.617 73.719 1.00 45.62 C ANISOU 2947 C ASP A 262 5289 6883 5162 -620 -142 -281 C ATOM 2948 O ASP A 262 0.820 28.347 74.675 1.00 45.62 O ANISOU 2948 O ASP A 262 5210 7037 5088 -617 -157 -354 O ATOM 2949 CB ASP A 262 3.437 26.874 73.785 1.00 45.07 C ANISOU 2949 CB ASP A 262 5283 6731 5109 -517 -186 -150 C ATOM 2950 CG ASP A 262 4.452 25.779 73.655 1.00 56.22 C ANISOU 2950 CG ASP A 262 6768 8054 6539 -487 -189 -25 C ATOM 2951 OD1 ASP A 262 5.020 25.637 72.559 1.00 55.76 O ANISOU 2951 OD1 ASP A 262 6751 7853 6582 -468 -194 -22 O ATOM 2952 OD2 ASP A 262 4.700 25.080 74.660 1.00 64.70 O ANISOU 2952 OD2 ASP A 262 7856 9204 7523 -481 -189 68 O ATOM 2953 N SER A 263 0.673 27.855 72.455 1.00 40.07 N ANISOU 2953 N SER A 263 4611 6051 4564 -637 -140 -332 N ATOM 2954 CA SER A 263 -0.222 28.945 72.098 1.00 38.89 C ANISOU 2954 CA SER A 263 4403 5920 4454 -661 -155 -471 C ATOM 2955 C SER A 263 -1.520 28.731 72.855 1.00 42.40 C ANISOU 2955 C SER A 263 4811 6470 4828 -728 -117 -489 C ATOM 2956 O SER A 263 -2.000 29.668 73.491 1.00 42.11 O ANISOU 2956 O SER A 263 4688 6556 4756 -736 -136 -599 O ATOM 2957 CB SER A 263 -0.459 28.979 70.593 1.00 41.72 C ANISOU 2957 CB SER A 263 4815 6114 4923 -664 -157 -495 C ATOM 2958 OG SER A 263 0.742 29.284 69.903 1.00 50.62 O ANISOU 2958 OG SER A 263 5965 7155 6111 -602 -183 -483 O ATOM 2959 N PHE A 264 -2.017 27.473 72.886 1.00 38.66 N ANISOU 2959 N PHE A 264 4397 5956 4336 -773 -63 -380 N ATOM 2960 CA PHE A 264 -3.217 27.094 73.635 1.00 39.17 C ANISOU 2960 CA PHE A 264 4431 6113 4338 -842 -10 -372 C ATOM 2961 C PHE A 264 -2.968 27.147 75.156 1.00 43.39 C ANISOU 2961 C PHE A 264 4916 6840 4730 -832 1 -337 C ATOM 2962 O PHE A 264 -3.902 27.414 75.916 1.00 43.33 O ANISOU 2962 O PHE A 264 4847 6963 4656 -876 32 -389 O ATOM 2963 CB PHE A 264 -3.724 25.704 73.214 1.00 41.29 C ANISOU 2963 CB PHE A 264 4771 6268 4649 -888 44 -256 C ATOM 2964 CG PHE A 264 -4.122 25.519 71.764 1.00 41.88 C ANISOU 2964 CG PHE A 264 4893 6165 4855 -894 34 -296 C ATOM 2965 CD1 PHE A 264 -4.430 26.612 70.960 1.00 44.14 C ANISOU 2965 CD1 PHE A 264 5154 6414 5203 -880 -9 -438 C ATOM 2966 CD2 PHE A 264 -4.227 24.249 71.214 1.00 43.94 C ANISOU 2966 CD2 PHE A 264 5219 6298 5179 -910 63 -195 C ATOM 2967 CE1 PHE A 264 -4.803 26.436 69.625 1.00 44.40 C ANISOU 2967 CE1 PHE A 264 5236 6293 5341 -876 -22 -475 C ATOM 2968 CE2 PHE A 264 -4.602 24.074 69.881 1.00 45.98 C ANISOU 2968 CE2 PHE A 264 5517 6402 5550 -905 48 -244 C ATOM 2969 CZ PHE A 264 -4.893 25.167 69.095 1.00 43.31 C ANISOU 2969 CZ PHE A 264 5163 6039 5256 -886 6 -383 C ATOM 2970 N ILE A 265 -1.708 26.908 75.592 1.00 39.63 N ANISOU 2970 N ILE A 265 4464 6387 4206 -771 -26 -257 N ATOM 2971 CA ILE A 265 -1.306 26.951 76.999 1.00 40.14 C ANISOU 2971 CA ILE A 265 4490 6633 4128 -742 -29 -222 C ATOM 2972 C ILE A 265 -1.346 28.393 77.530 1.00 44.91 C ANISOU 2972 C ILE A 265 4986 7379 4698 -710 -78 -391 C ATOM 2973 O ILE A 265 -2.059 28.644 78.503 1.00 45.95 O ANISOU 2973 O ILE A 265 5054 7678 4726 -734 -54 -432 O ATOM 2974 CB ILE A 265 0.039 26.202 77.254 1.00 43.03 C ANISOU 2974 CB ILE A 265 4919 6966 4467 -682 -52 -90 C ATOM 2975 CG1 ILE A 265 -0.175 24.674 77.198 1.00 43.54 C ANISOU 2975 CG1 ILE A 265 5067 6946 4529 -727 5 88 C ATOM 2976 CG2 ILE A 265 0.692 26.610 78.593 1.00 44.70 C ANISOU 2976 CG2 ILE A 265 5079 7364 4542 -622 -87 -100 C ATOM 2977 CD1 ILE A 265 1.045 23.861 76.781 1.00 49.17 C ANISOU 2977 CD1 ILE A 265 5856 7531 5296 -680 -25 199 C ATOM 2978 N LEU A 266 -0.623 29.336 76.875 1.00 40.57 N ANISOU 2978 N LEU A 266 4409 6761 4245 -657 -144 -490 N ATOM 2979 CA LEU A 266 -0.570 30.756 77.262 1.00 40.15 C ANISOU 2979 CA LEU A 266 4242 6816 4198 -620 -204 -658 C ATOM 2980 C LEU A 266 -1.934 31.425 77.103 1.00 44.71 C ANISOU 2980 C LEU A 266 4755 7431 4802 -682 -192 -784 C ATOM 2981 O LEU A 266 -2.321 32.221 77.957 1.00 45.44 O ANISOU 2981 O LEU A 266 4745 7684 4835 -676 -215 -899 O ATOM 2982 CB LEU A 266 0.481 31.547 76.446 1.00 39.02 C ANISOU 2982 CB LEU A 266 4086 6557 4182 -556 -269 -718 C ATOM 2983 CG LEU A 266 1.930 31.038 76.377 1.00 43.29 C ANISOU 2983 CG LEU A 266 4683 7028 4737 -490 -290 -620 C ATOM 2984 CD1 LEU A 266 2.687 31.761 75.296 1.00 42.33 C ANISOU 2984 CD1 LEU A 266 4555 6763 4765 -451 -328 -676 C ATOM 2985 CD2 LEU A 266 2.655 31.197 77.702 1.00 46.71 C ANISOU 2985 CD2 LEU A 266 5061 7623 5064 -425 -328 -630 C ATOM 2986 N LEU A 267 -2.665 31.104 76.013 1.00 40.78 N ANISOU 2986 N LEU A 267 4312 6785 4396 -737 -162 -774 N ATOM 2987 CA LEU A 267 -3.986 31.680 75.736 1.00 40.64 C ANISOU 2987 CA LEU A 267 4241 6778 4423 -797 -156 -897 C ATOM 2988 C LEU A 267 -5.154 30.982 76.464 1.00 46.78 C ANISOU 2988 C LEU A 267 5010 7654 5110 -870 -81 -864 C ATOM 2989 O LEU A 267 -6.306 31.381 76.288 1.00 46.63 O ANISOU 2989 O LEU A 267 4944 7644 5129 -924 -71 -970 O ATOM 2990 CB LEU A 267 -4.250 31.829 74.217 1.00 39.40 C ANISOU 2990 CB LEU A 267 4136 6423 4410 -810 -173 -926 C ATOM 2991 CG LEU A 267 -3.379 32.841 73.462 1.00 42.66 C ANISOU 2991 CG LEU A 267 4531 6753 4925 -749 -243 -993 C ATOM 2992 CD1 LEU A 267 -3.564 32.711 71.968 1.00 41.34 C ANISOU 2992 CD1 LEU A 267 4442 6396 4870 -756 -245 -980 C ATOM 2993 CD2 LEU A 267 -3.660 34.274 73.916 1.00 45.29 C ANISOU 2993 CD2 LEU A 267 4734 7189 5283 -737 -305 -1164 C ATOM 2994 N GLU A 268 -4.846 29.970 77.303 1.00 44.73 N ANISOU 2994 N GLU A 268 4792 7468 4736 -871 -28 -719 N ATOM 2995 CA GLU A 268 -5.795 29.217 78.130 1.00 45.98 C ANISOU 2995 CA GLU A 268 4943 7730 4795 -936 56 -654 C ATOM 2996 C GLU A 268 -6.928 28.496 77.377 1.00 50.92 C ANISOU 2996 C GLU A 268 5612 8227 5510 -1016 117 -626 C ATOM 2997 O GLU A 268 -8.112 28.706 77.668 1.00 51.06 O ANISOU 2997 O GLU A 268 5568 8312 5519 -1077 156 -707 O ATOM 2998 CB GLU A 268 -6.304 30.062 79.319 1.00 48.16 C ANISOU 2998 CB GLU A 268 5103 8237 4959 -938 54 -774 C ATOM 2999 CG GLU A 268 -5.229 30.362 80.344 1.00 60.22 C ANISOU 2999 CG GLU A 268 6598 9918 6363 -856 12 -759 C ATOM 3000 CD GLU A 268 -5.588 31.401 81.383 1.00 86.46 C ANISOU 3000 CD GLU A 268 9792 13464 9593 -837 -15 -916 C ATOM 3001 OE1 GLU A 268 -6.666 31.280 82.008 1.00 86.26 O ANISOU 3001 OE1 GLU A 268 9722 13563 9490 -897 51 -942 O ATOM 3002 OE2 GLU A 268 -4.770 32.325 81.596 1.00 81.16 O ANISOU 3002 OE2 GLU A 268 9059 12847 8932 -759 -101 -1018 O ATOM 3003 N ILE A 269 -6.554 27.634 76.413 1.00 47.63 N ANISOU 3003 N ILE A 269 5291 7622 5183 -1013 122 -520 N ATOM 3004 CA ILE A 269 -7.481 26.796 75.639 1.00 47.59 C ANISOU 3004 CA ILE A 269 5331 7475 5276 -1075 172 -484 C ATOM 3005 C ILE A 269 -7.448 25.378 76.264 1.00 53.60 C ANISOU 3005 C ILE A 269 6142 8243 5981 -1106 249 -289 C ATOM 3006 O ILE A 269 -8.502 24.767 76.462 1.00 53.75 O ANISOU 3006 O ILE A 269 6147 8259 6015 -1176 321 -258 O ATOM 3007 CB ILE A 269 -7.215 26.874 74.106 1.00 49.20 C ANISOU 3007 CB ILE A 269 5595 7474 5625 -1047 119 -522 C ATOM 3008 CG1 ILE A 269 -7.577 28.283 73.574 1.00 48.71 C ANISOU 3008 CG1 ILE A 269 5473 7414 5621 -1034 55 -712 C ATOM 3009 CG2 ILE A 269 -7.999 25.813 73.330 1.00 49.62 C ANISOU 3009 CG2 ILE A 269 5700 7374 5779 -1095 163 -469 C ATOM 3010 CD1 ILE A 269 -6.514 28.967 72.776 1.00 53.55 C ANISOU 3010 CD1 ILE A 269 6112 7947 6287 -963 -19 -743 C ATOM 3011 N ILE A 270 -6.237 24.905 76.638 1.00 51.25 N ANISOU 3011 N ILE A 270 5894 7958 5620 -1052 232 -162 N ATOM 3012 CA ILE A 270 -5.995 23.649 77.360 1.00 52.60 C ANISOU 3012 CA ILE A 270 6111 8150 5724 -1068 290 34 C ATOM 3013 C ILE A 270 -5.400 24.024 78.728 1.00 57.27 C ANISOU 3013 C ILE A 270 6667 8954 6138 -1027 284 62 C ATOM 3014 O ILE A 270 -4.458 24.820 78.779 1.00 56.18 O ANISOU 3014 O ILE A 270 6514 8859 5971 -955 210 -7 O ATOM 3015 CB ILE A 270 -5.173 22.581 76.572 1.00 55.69 C ANISOU 3015 CB ILE A 270 6596 8355 6208 -1042 272 165 C ATOM 3016 CG1 ILE A 270 -3.793 23.100 76.103 1.00 55.36 C ANISOU 3016 CG1 ILE A 270 6583 8269 6181 -956 186 133 C ATOM 3017 CG2 ILE A 270 -5.981 22.019 75.402 1.00 56.15 C ANISOU 3017 CG2 ILE A 270 6679 8227 6427 -1088 291 146 C ATOM 3018 CD1 ILE A 270 -2.716 22.043 76.058 1.00 62.69 C ANISOU 3018 CD1 ILE A 270 7586 9110 7122 -920 172 291 C ATOM 3019 N LYS A 271 -5.998 23.537 79.830 1.00 55.53 N ANISOU 3019 N LYS A 271 6425 8875 5801 -1069 361 150 N ATOM 3020 CA LYS A 271 -5.565 23.915 81.183 1.00 56.49 C ANISOU 3020 CA LYS A 271 6507 9223 5733 -1026 358 167 C ATOM 3021 C LYS A 271 -4.894 22.816 82.028 1.00 61.91 C ANISOU 3021 C LYS A 271 7258 9955 6310 -1004 387 384 C ATOM 3022 O LYS A 271 -5.086 22.779 83.249 1.00 63.05 O ANISOU 3022 O LYS A 271 7373 10297 6286 -1002 431 438 O ATOM 3023 CB LYS A 271 -6.705 24.627 81.953 1.00 59.67 C ANISOU 3023 CB LYS A 271 6811 9814 6046 -1071 409 51 C ATOM 3024 CG LYS A 271 -6.991 26.061 81.498 1.00 69.95 C ANISOU 3024 CG LYS A 271 8030 11138 7408 -1057 342 -189 C ATOM 3025 CD LYS A 271 -5.977 27.082 82.030 1.00 77.67 C ANISOU 3025 CD LYS A 271 8961 12247 8304 -962 251 -286 C ATOM 3026 CE LYS A 271 -6.333 27.659 83.379 1.00 84.55 C ANISOU 3026 CE LYS A 271 9739 13384 9000 -949 270 -355 C ATOM 3027 NZ LYS A 271 -5.302 28.618 83.848 1.00 90.53 N ANISOU 3027 NZ LYS A 271 10445 14254 9700 -847 170 -459 N ATOM 3028 N GLN A 272 -4.077 21.954 81.392 1.00 58.03 N ANISOU 3028 N GLN A 272 6852 9289 5909 -982 358 505 N ATOM 3029 CA GLN A 272 -3.346 20.900 82.102 1.00 59.06 C ANISOU 3029 CA GLN A 272 7047 9437 5956 -956 368 711 C ATOM 3030 C GLN A 272 -2.150 21.533 82.802 1.00 63.87 C ANISOU 3030 C GLN A 272 7650 10177 6442 -854 286 677 C ATOM 3031 O GLN A 272 -1.397 22.271 82.167 1.00 62.64 O ANISOU 3031 O GLN A 272 7485 9957 6358 -798 203 555 O ATOM 3032 CB GLN A 272 -2.921 19.759 81.161 1.00 59.81 C ANISOU 3032 CB GLN A 272 7223 9295 6208 -968 358 836 C ATOM 3033 CG GLN A 272 -4.064 19.141 80.346 1.00 74.36 C ANISOU 3033 CG GLN A 272 9066 10987 8202 -1058 425 849 C ATOM 3034 CD GLN A 272 -5.262 18.733 81.175 1.00 96.83 C ANISOU 3034 CD GLN A 272 11872 13938 10979 -1137 535 925 C ATOM 3035 OE1 GLN A 272 -6.293 19.415 81.198 1.00 91.52 O ANISOU 3035 OE1 GLN A 272 11133 13337 10302 -1183 576 796 O ATOM 3036 NE2 GLN A 272 -5.157 17.603 81.855 1.00 93.09 N ANISOU 3036 NE2 GLN A 272 11439 13471 10461 -1156 585 1137 N ATOM 3037 N GLY A 273 -2.059 21.283 84.111 1.00 62.37 N ANISOU 3037 N GLY A 273 7458 10175 6067 -832 313 777 N ATOM 3038 CA GLY A 273 -1.095 21.813 85.078 1.00 63.13 C ANISOU 3038 CA GLY A 273 7538 10443 6006 -732 244 752 C ATOM 3039 C GLY A 273 0.301 22.234 84.654 1.00 66.79 C ANISOU 3039 C GLY A 273 8020 10826 6532 -637 128 684 C ATOM 3040 O GLY A 273 0.465 23.085 83.776 1.00 64.97 O ANISOU 3040 O GLY A 273 7753 10508 6426 -624 79 523 O ATOM 3041 N CYS A 274 1.319 21.709 85.359 1.00 64.96 N ANISOU 3041 N CYS A 274 7838 10639 6206 -565 83 801 N ATOM 3042 CA CYS A 274 2.715 22.049 85.090 1.00 64.25 C ANISOU 3042 CA CYS A 274 7761 10481 6171 -469 -27 742 C ATOM 3043 C CYS A 274 3.605 20.892 84.620 1.00 66.58 C ANISOU 3043 C CYS A 274 8153 10587 6557 -456 -56 901 C ATOM 3044 O CYS A 274 4.662 21.143 84.037 1.00 64.29 O ANISOU 3044 O CYS A 274 7873 10186 6369 -396 -135 836 O ATOM 3045 CB CYS A 274 3.335 22.837 86.241 1.00 65.86 C ANISOU 3045 CB CYS A 274 7911 10902 6210 -365 -94 657 C ATOM 3046 SG CYS A 274 3.116 24.632 86.102 1.00 68.94 S ANISOU 3046 SG CYS A 274 8167 11394 6632 -332 -142 367 S ATOM 3047 N GLU A 275 3.168 19.636 84.836 1.00 64.19 N ANISOU 3047 N GLU A 275 7913 10241 6234 -515 9 1103 N ATOM 3048 CA GLU A 275 3.904 18.449 84.394 1.00 63.94 C ANISOU 3048 CA GLU A 275 7966 10023 6304 -512 -18 1258 C ATOM 3049 C GLU A 275 3.771 18.255 82.880 1.00 65.76 C ANISOU 3049 C GLU A 275 8210 10017 6758 -563 -12 1208 C ATOM 3050 O GLU A 275 4.742 17.873 82.223 1.00 64.45 O ANISOU 3050 O GLU A 275 8086 9697 6707 -526 -74 1222 O ATOM 3051 CB GLU A 275 3.439 17.195 85.151 1.00 67.11 C ANISOU 3051 CB GLU A 275 8421 10455 6623 -558 48 1494 C ATOM 3052 CG GLU A 275 4.149 17.004 86.481 1.00 79.21 C ANISOU 3052 CG GLU A 275 9981 12156 7960 -476 5 1596 C ATOM 3053 CD GLU A 275 3.825 15.747 87.271 1.00100.65 C ANISOU 3053 CD GLU A 275 12756 14899 10587 -512 64 1852 C ATOM 3054 OE1 GLU A 275 3.932 15.800 88.518 1.00 92.73 O ANISOU 3054 OE1 GLU A 275 11758 14102 9372 -461 64 1923 O ATOM 3055 OE2 GLU A 275 3.496 14.707 86.655 1.00 94.77 O ANISOU 3055 OE2 GLU A 275 12050 13972 9988 -586 106 1984 O ATOM 3056 N PHE A 276 2.564 18.529 82.336 1.00 61.66 N ANISOU 3056 N PHE A 276 7654 9477 6296 -643 59 1140 N ATOM 3057 CA PHE A 276 2.236 18.414 80.913 1.00 59.91 C ANISOU 3057 CA PHE A 276 7439 9053 6269 -691 70 1078 C ATOM 3058 C PHE A 276 3.003 19.449 80.088 1.00 62.39 C ANISOU 3058 C PHE A 276 7730 9309 6665 -632 -3 901 C ATOM 3059 O PHE A 276 3.704 19.068 79.152 1.00 60.96 O ANISOU 3059 O PHE A 276 7590 8958 6617 -612 -41 907 O ATOM 3060 CB PHE A 276 0.715 18.513 80.693 1.00 61.62 C ANISOU 3060 CB PHE A 276 7617 9284 6511 -783 159 1041 C ATOM 3061 CG PHE A 276 0.257 18.328 79.266 1.00 61.90 C ANISOU 3061 CG PHE A 276 7662 9119 6739 -828 169 980 C ATOM 3062 CD1 PHE A 276 0.269 17.071 78.671 1.00 65.45 C ANISOU 3062 CD1 PHE A 276 8163 9391 7316 -859 182 1105 C ATOM 3063 CD2 PHE A 276 -0.222 19.403 78.528 1.00 62.76 C ANISOU 3063 CD2 PHE A 276 7724 9219 6902 -836 162 793 C ATOM 3064 CE1 PHE A 276 -0.150 16.902 77.347 1.00 65.39 C ANISOU 3064 CE1 PHE A 276 8160 9206 7478 -889 184 1035 C ATOM 3065 CE2 PHE A 276 -0.651 19.233 77.208 1.00 64.65 C ANISOU 3065 CE2 PHE A 276 7977 9281 7306 -868 166 736 C ATOM 3066 CZ PHE A 276 -0.611 17.984 76.625 1.00 63.05 C ANISOU 3066 CZ PHE A 276 7826 8912 7219 -891 177 852 C ATOM 3067 N GLU A 277 2.925 20.744 80.473 1.00 59.12 N ANISOU 3067 N GLU A 277 7247 9041 6174 -599 -23 747 N ATOM 3068 CA GLU A 277 3.648 21.835 79.804 1.00 57.74 C ANISOU 3068 CA GLU A 277 7036 8825 6077 -541 -89 582 C ATOM 3069 C GLU A 277 5.167 21.621 79.834 1.00 61.32 C ANISOU 3069 C GLU A 277 7524 9220 6556 -456 -167 614 C ATOM 3070 O GLU A 277 5.842 21.973 78.870 1.00 59.77 O ANISOU 3070 O GLU A 277 7329 8895 6485 -427 -204 537 O ATOM 3071 CB GLU A 277 3.239 23.231 80.330 1.00 59.17 C ANISOU 3071 CB GLU A 277 7123 9179 6181 -523 -101 414 C ATOM 3072 CG GLU A 277 3.494 23.468 81.810 1.00 73.46 C ANISOU 3072 CG GLU A 277 8898 11207 7808 -469 -122 428 C ATOM 3073 CD GLU A 277 3.292 24.890 82.295 1.00 97.56 C ANISOU 3073 CD GLU A 277 11844 14423 10803 -432 -155 240 C ATOM 3074 OE1 GLU A 277 4.235 25.703 82.164 1.00 96.68 O ANISOU 3074 OE1 GLU A 277 11691 14301 10742 -356 -233 128 O ATOM 3075 OE2 GLU A 277 2.207 25.182 82.848 1.00 91.34 O ANISOU 3075 OE2 GLU A 277 11006 13774 9924 -479 -104 203 O ATOM 3076 N ASN A 278 5.682 20.985 80.911 1.00 59.37 N ANISOU 3076 N ASN A 278 7306 9060 6191 -418 -187 735 N ATOM 3077 CA ASN A 278 7.096 20.644 81.101 1.00 59.43 C ANISOU 3077 CA ASN A 278 7349 9020 6213 -336 -265 779 C ATOM 3078 C ASN A 278 7.542 19.621 80.053 1.00 61.96 C ANISOU 3078 C ASN A 278 7738 9116 6689 -359 -269 865 C ATOM 3079 O ASN A 278 8.720 19.605 79.688 1.00 61.01 O ANISOU 3079 O ASN A 278 7632 8903 6646 -298 -333 839 O ATOM 3080 CB ASN A 278 7.335 20.100 82.520 1.00 63.52 C ANISOU 3080 CB ASN A 278 7890 9689 6556 -297 -282 904 C ATOM 3081 CG ASN A 278 8.783 19.984 82.936 1.00 92.56 C ANISOU 3081 CG ASN A 278 11589 13357 10223 -195 -378 916 C ATOM 3082 OD1 ASN A 278 9.275 18.896 83.262 1.00 88.23 O ANISOU 3082 OD1 ASN A 278 11108 12758 9658 -182 -400 1071 O ATOM 3083 ND2 ASN A 278 9.485 21.109 82.993 1.00 86.50 N ANISOU 3083 ND2 ASN A 278 10757 12640 9468 -118 -442 749 N ATOM 3084 N THR A 279 6.593 18.783 79.560 1.00 57.92 N ANISOU 3084 N THR A 279 7259 8516 6231 -444 -201 957 N ATOM 3085 CA THR A 279 6.843 17.773 78.525 1.00 56.88 C ANISOU 3085 CA THR A 279 7182 8175 6256 -470 -202 1028 C ATOM 3086 C THR A 279 6.572 18.306 77.117 1.00 57.94 C ANISOU 3086 C THR A 279 7300 8187 6530 -492 -188 896 C ATOM 3087 O THR A 279 7.179 17.821 76.165 1.00 56.83 O ANISOU 3087 O THR A 279 7191 7884 6517 -479 -212 900 O ATOM 3088 CB THR A 279 6.171 16.435 78.839 1.00 66.51 C ANISOU 3088 CB THR A 279 8444 9354 7474 -534 -155 1212 C ATOM 3089 OG1 THR A 279 4.758 16.616 78.903 1.00 66.79 O ANISOU 3089 OG1 THR A 279 8448 9451 7478 -611 -72 1200 O ATOM 3090 CG2 THR A 279 6.691 15.803 80.127 1.00 67.24 C ANISOU 3090 CG2 THR A 279 8567 9542 7440 -499 -182 1363 C ATOM 3091 N VAL A 280 5.692 19.325 76.987 1.00 53.33 N ANISOU 3091 N VAL A 280 6664 7682 5917 -520 -152 776 N ATOM 3092 CA VAL A 280 5.395 19.994 75.708 1.00 51.47 C ANISOU 3092 CA VAL A 280 6412 7349 5797 -534 -143 645 C ATOM 3093 C VAL A 280 6.683 20.734 75.291 1.00 54.56 C ANISOU 3093 C VAL A 280 6790 7702 6239 -456 -204 552 C ATOM 3094 O VAL A 280 7.131 20.583 74.151 1.00 53.00 O ANISOU 3094 O VAL A 280 6619 7358 6162 -444 -213 525 O ATOM 3095 CB VAL A 280 4.163 20.947 75.802 1.00 54.76 C ANISOU 3095 CB VAL A 280 6770 7868 6166 -579 -101 538 C ATOM 3096 CG1 VAL A 280 4.014 21.806 74.549 1.00 53.10 C ANISOU 3096 CG1 VAL A 280 6543 7569 6064 -577 -108 397 C ATOM 3097 CG2 VAL A 280 2.876 20.175 76.072 1.00 55.25 C ANISOU 3097 CG2 VAL A 280 6841 7945 6206 -661 -32 623 C ATOM 3098 N HIS A 281 7.310 21.459 76.254 1.00 51.91 N ANISOU 3098 N HIS A 281 6412 7499 5813 -398 -246 508 N ATOM 3099 CA HIS A 281 8.573 22.188 76.081 1.00 51.45 C ANISOU 3099 CA HIS A 281 6327 7418 5805 -319 -306 420 C ATOM 3100 C HIS A 281 9.724 21.207 75.840 1.00 55.85 C ANISOU 3100 C HIS A 281 6941 7852 6429 -281 -343 508 C ATOM 3101 O HIS A 281 10.614 21.497 75.038 1.00 54.19 O ANISOU 3101 O HIS A 281 6727 7537 6327 -241 -367 445 O ATOM 3102 CB AHIS A 281 8.838 23.106 77.294 0.65 52.87 C ANISOU 3102 CB AHIS A 281 6438 7778 5872 -264 -347 349 C ATOM 3103 CB BHIS A 281 8.862 23.106 77.285 0.35 52.76 C ANISOU 3103 CB BHIS A 281 6424 7763 5860 -263 -347 348 C ATOM 3104 CG AHIS A 281 10.267 23.527 77.471 0.65 56.20 C ANISOU 3104 CG AHIS A 281 6834 8185 6334 -173 -418 293 C ATOM 3105 CG BHIS A 281 7.808 24.143 77.534 0.35 55.88 C ANISOU 3105 CG BHIS A 281 6750 8282 6201 -294 -321 241 C ATOM 3106 ND1AHIS A 281 11.023 23.079 78.540 0.65 58.96 N ANISOU 3106 ND1AHIS A 281 7196 8608 6598 -113 -471 355 N ATOM 3107 ND1BHIS A 281 7.212 24.281 78.773 0.35 58.63 N ANISOU 3107 ND1BHIS A 281 7063 8817 6396 -298 -314 252 N ATOM 3108 CD2AHIS A 281 11.037 24.324 76.698 0.65 56.99 C ANISOU 3108 CD2AHIS A 281 6897 8198 6557 -132 -443 184 C ATOM 3109 CD2BHIS A 281 7.275 25.056 76.691 0.35 56.57 C ANISOU 3109 CD2BHIS A 281 6796 8330 6368 -320 -303 124 C ATOM 3110 CE1AHIS A 281 12.220 23.624 78.391 0.65 58.05 C ANISOU 3110 CE1AHIS A 281 7047 8447 6564 -37 -530 270 C ATOM 3111 CE1BHIS A 281 6.332 25.263 78.646 0.35 57.59 C ANISOU 3111 CE1BHIS A 281 6865 8752 6264 -329 -293 131 C ATOM 3112 NE2AHIS A 281 12.277 24.379 77.295 0.65 57.18 N ANISOU 3112 NE2AHIS A 281 6903 8238 6583 -48 -510 169 N ATOM 3113 NE2BHIS A 281 6.334 25.761 77.410 0.35 56.65 N ANISOU 3113 NE2BHIS A 281 6741 8496 6285 -343 -290 53 N ATOM 3114 N LYS A 282 9.663 20.023 76.489 1.00 54.58 N ANISOU 3114 N LYS A 282 6830 7697 6213 -298 -344 656 N ATOM 3115 CA LYS A 282 10.645 18.946 76.331 1.00 55.27 C ANISOU 3115 CA LYS A 282 6970 7664 6366 -269 -385 752 C ATOM 3116 C LYS A 282 10.594 18.379 74.901 1.00 60.00 C ANISOU 3116 C LYS A 282 7603 8078 7118 -303 -361 751 C ATOM 3117 O LYS A 282 11.591 17.832 74.432 1.00 60.06 O ANISOU 3117 O LYS A 282 7636 7968 7217 -268 -399 769 O ATOM 3118 CB LYS A 282 10.427 17.840 77.379 1.00 58.80 C ANISOU 3118 CB LYS A 282 7459 8164 6719 -287 -388 921 C ATOM 3119 CG LYS A 282 11.669 16.993 77.660 1.00 72.84 C ANISOU 3119 CG LYS A 282 9277 9867 8530 -231 -460 1004 C ATOM 3120 CD LYS A 282 11.654 16.347 79.051 1.00 85.48 C ANISOU 3120 CD LYS A 282 10906 11582 9990 -217 -483 1148 C ATOM 3121 CE LYS A 282 10.977 14.991 79.121 1.00 99.10 C ANISOU 3121 CE LYS A 282 12681 13239 11732 -286 -446 1328 C ATOM 3122 NZ LYS A 282 11.697 13.946 78.340 1.00108.25 N ANISOU 3122 NZ LYS A 282 13879 14200 13051 -283 -488 1385 N ATOM 3123 N TRP A 283 9.451 18.555 74.201 1.00 56.29 N ANISOU 3123 N TRP A 283 7127 7586 6675 -364 -301 716 N ATOM 3124 CA TRP A 283 9.257 18.099 72.826 1.00 55.37 C ANISOU 3124 CA TRP A 283 7038 7312 6689 -390 -279 698 C ATOM 3125 C TRP A 283 9.222 19.237 71.783 1.00 57.27 C ANISOU 3125 C TRP A 283 7250 7524 6984 -376 -263 552 C ATOM 3126 O TRP A 283 8.782 19.016 70.653 1.00 56.53 O ANISOU 3126 O TRP A 283 7177 7329 6973 -399 -237 524 O ATOM 3127 CB TRP A 283 8.053 17.146 72.723 1.00 54.73 C ANISOU 3127 CB TRP A 283 6980 7192 6623 -464 -234 786 C ATOM 3128 CG TRP A 283 8.442 15.696 72.751 1.00 56.70 C ANISOU 3128 CG TRP A 283 7271 7334 6939 -469 -258 918 C ATOM 3129 CD1 TRP A 283 8.615 14.872 71.676 1.00 59.39 C ANISOU 3129 CD1 TRP A 283 7635 7514 7416 -472 -267 925 C ATOM 3130 CD2 TRP A 283 8.761 14.914 73.909 1.00 57.81 C ANISOU 3130 CD2 TRP A 283 7430 7520 7016 -466 -283 1059 C ATOM 3131 NE1 TRP A 283 8.999 13.620 72.095 1.00 59.88 N ANISOU 3131 NE1 TRP A 283 7723 7511 7520 -476 -299 1058 N ATOM 3132 CE2 TRP A 283 9.096 13.617 73.462 1.00 62.39 C ANISOU 3132 CE2 TRP A 283 8042 7950 7714 -473 -309 1150 C ATOM 3133 CE3 TRP A 283 8.795 15.183 75.289 1.00 60.19 C ANISOU 3133 CE3 TRP A 283 7722 7978 7168 -453 -290 1117 C ATOM 3134 CZ2 TRP A 283 9.454 12.589 74.344 1.00 63.10 C ANISOU 3134 CZ2 TRP A 283 8158 8032 7787 -472 -342 1305 C ATOM 3135 CZ3 TRP A 283 9.134 14.161 76.163 1.00 62.98 C ANISOU 3135 CZ3 TRP A 283 8108 8334 7486 -448 -318 1274 C ATOM 3136 CH2 TRP A 283 9.472 12.887 75.690 1.00 64.16 C ANISOU 3136 CH2 TRP A 283 8291 8322 7764 -459 -345 1371 C ATOM 3137 N ILE A 284 9.710 20.446 72.160 1.00 52.31 N ANISOU 3137 N ILE A 284 6574 6985 6317 -333 -283 459 N ATOM 3138 CA ILE A 284 9.823 21.612 71.268 1.00 50.34 C ANISOU 3138 CA ILE A 284 6291 6709 6125 -313 -272 331 C ATOM 3139 C ILE A 284 11.271 21.701 70.803 1.00 53.07 C ANISOU 3139 C ILE A 284 6637 6970 6556 -248 -304 304 C ATOM 3140 O ILE A 284 11.518 21.806 69.602 1.00 52.00 O ANISOU 3140 O ILE A 284 6516 6729 6511 -240 -283 262 O ATOM 3141 CB ILE A 284 9.330 22.924 71.937 1.00 53.06 C ANISOU 3141 CB ILE A 284 6567 7196 6398 -312 -273 239 C ATOM 3142 CG1 ILE A 284 7.806 22.999 71.911 1.00 53.43 C ANISOU 3142 CG1 ILE A 284 6611 7292 6400 -382 -230 230 C ATOM 3143 CG2 ILE A 284 9.941 24.187 71.299 1.00 52.64 C ANISOU 3143 CG2 ILE A 284 6466 7118 6419 -268 -284 118 C ATOM 3144 CD1 ILE A 284 7.264 23.694 73.058 1.00 61.03 C ANISOU 3144 CD1 ILE A 284 7514 8420 7254 -390 -235 192 C ATOM 3145 N SER A 285 12.220 21.647 71.766 1.00 49.56 N ANISOU 3145 N SER A 285 6175 6576 6080 -199 -353 325 N ATOM 3146 CA SER A 285 13.662 21.713 71.543 1.00 48.73 C ANISOU 3146 CA SER A 285 6060 6398 6057 -134 -390 295 C ATOM 3147 C SER A 285 14.166 20.578 70.668 1.00 50.54 C ANISOU 3147 C SER A 285 6345 6480 6378 -137 -387 352 C ATOM 3148 O SER A 285 15.027 20.827 69.825 1.00 49.37 O ANISOU 3148 O SER A 285 6188 6242 6326 -102 -383 296 O ATOM 3149 CB SER A 285 14.409 21.754 72.871 1.00 53.27 C ANISOU 3149 CB SER A 285 6609 7065 6569 -81 -452 309 C ATOM 3150 OG SER A 285 14.053 22.931 73.576 1.00 62.94 O ANISOU 3150 OG SER A 285 7766 8425 7724 -67 -460 226 O ATOM 3151 N ILE A 286 13.612 19.351 70.835 1.00 46.46 N ANISOU 3151 N ILE A 286 5879 5936 5839 -178 -387 461 N ATOM 3152 CA ILE A 286 13.975 18.189 70.016 1.00 45.87 C ANISOU 3152 CA ILE A 286 5848 5720 5861 -183 -393 511 C ATOM 3153 C ILE A 286 13.464 18.402 68.587 1.00 47.96 C ANISOU 3153 C ILE A 286 6123 5907 6193 -204 -341 448 C ATOM 3154 O ILE A 286 14.229 18.220 67.643 1.00 47.24 O ANISOU 3154 O ILE A 286 6040 5717 6193 -173 -340 411 O ATOM 3155 CB ILE A 286 13.503 16.822 70.599 1.00 49.89 C ANISOU 3155 CB ILE A 286 6397 6211 6348 -221 -411 647 C ATOM 3156 CG1 ILE A 286 13.809 16.686 72.109 1.00 51.51 C ANISOU 3156 CG1 ILE A 286 6598 6520 6453 -202 -457 722 C ATOM 3157 CG2 ILE A 286 14.109 15.654 69.794 1.00 50.57 C ANISOU 3157 CG2 ILE A 286 6512 6143 6557 -213 -435 682 C ATOM 3158 CD1 ILE A 286 13.085 15.499 72.827 1.00 61.64 C ANISOU 3158 CD1 ILE A 286 7917 7813 7690 -250 -459 875 C ATOM 3159 N THR A 287 12.182 18.817 68.435 1.00 43.24 N ANISOU 3159 N THR A 287 5523 5361 5546 -251 -299 429 N ATOM 3160 CA THR A 287 11.553 19.083 67.137 1.00 41.73 C ANISOU 3160 CA THR A 287 5343 5109 5402 -266 -256 366 C ATOM 3161 C THR A 287 12.182 20.276 66.416 1.00 44.92 C ANISOU 3161 C THR A 287 5722 5506 5839 -224 -238 266 C ATOM 3162 O THR A 287 12.231 20.266 65.185 1.00 44.42 O ANISOU 3162 O THR A 287 5680 5364 5835 -211 -212 227 O ATOM 3163 CB THR A 287 10.025 19.160 67.237 1.00 44.77 C ANISOU 3163 CB THR A 287 5731 5545 5734 -326 -226 370 C ATOM 3164 OG1 THR A 287 9.655 20.195 68.141 1.00 42.75 O ANISOU 3164 OG1 THR A 287 5433 5420 5391 -335 -222 336 O ATOM 3165 CG2 THR A 287 9.395 17.846 67.654 1.00 42.69 C ANISOU 3165 CG2 THR A 287 5492 5253 5473 -370 -230 474 C ATOM 3166 N GLU A 288 12.690 21.277 67.177 1.00 40.80 N ANISOU 3166 N GLU A 288 5152 5066 5285 -197 -254 226 N ATOM 3167 CA GLU A 288 13.392 22.455 66.651 1.00 39.86 C ANISOU 3167 CA GLU A 288 4993 4937 5216 -156 -239 139 C ATOM 3168 C GLU A 288 14.752 22.008 66.117 1.00 43.40 C ANISOU 3168 C GLU A 288 5450 5286 5754 -108 -246 141 C ATOM 3169 O GLU A 288 15.173 22.469 65.060 1.00 42.34 O ANISOU 3169 O GLU A 288 5313 5090 5684 -85 -209 92 O ATOM 3170 CB GLU A 288 13.595 23.519 67.743 1.00 41.40 C ANISOU 3170 CB GLU A 288 5120 5242 5369 -136 -266 93 C ATOM 3171 CG GLU A 288 13.919 24.900 67.196 1.00 51.44 C ANISOU 3171 CG GLU A 288 6337 6508 6698 -109 -245 0 C ATOM 3172 CD GLU A 288 14.353 25.965 68.191 1.00 72.36 C ANISOU 3172 CD GLU A 288 8904 9248 9343 -75 -281 -64 C ATOM 3173 OE1 GLU A 288 14.859 27.017 67.734 1.00 61.44 O ANISOU 3173 OE1 GLU A 288 7467 7837 8041 -45 -268 -134 O ATOM 3174 OE2 GLU A 288 14.181 25.763 69.416 1.00 68.39 O ANISOU 3174 OE2 GLU A 288 8383 8843 8759 -74 -323 -45 O ATOM 3175 N ALA A 289 15.438 21.115 66.858 1.00 40.76 N ANISOU 3175 N ALA A 289 5125 4939 5423 -92 -293 197 N ATOM 3176 CA ALA A 289 16.731 20.560 66.480 1.00 40.83 C ANISOU 3176 CA ALA A 289 5138 4853 5523 -49 -310 196 C ATOM 3177 C ALA A 289 16.543 19.699 65.239 1.00 45.18 C ANISOU 3177 C ALA A 289 5736 5303 6128 -62 -282 210 C ATOM 3178 O ALA A 289 17.276 19.884 64.271 1.00 44.78 O ANISOU 3178 O ALA A 289 5680 5183 6150 -31 -252 161 O ATOM 3179 CB ALA A 289 17.310 19.740 67.624 1.00 42.35 C ANISOU 3179 CB ALA A 289 5334 5058 5698 -33 -379 260 C ATOM 3180 N LEU A 290 15.505 18.825 65.233 1.00 42.08 N ANISOU 3180 N LEU A 290 5382 4905 5700 -108 -285 269 N ATOM 3181 CA LEU A 290 15.140 17.964 64.102 1.00 41.70 C ANISOU 3181 CA LEU A 290 5372 4769 5705 -118 -268 273 C ATOM 3182 C LEU A 290 14.744 18.808 62.881 1.00 44.73 C ANISOU 3182 C LEU A 290 5760 5145 6091 -110 -209 197 C ATOM 3183 O LEU A 290 14.975 18.381 61.748 1.00 44.10 O ANISOU 3183 O LEU A 290 5701 4991 6065 -88 -190 169 O ATOM 3184 CB LEU A 290 13.978 17.023 64.475 1.00 42.13 C ANISOU 3184 CB LEU A 290 5452 4826 5729 -170 -283 346 C ATOM 3185 CG LEU A 290 14.291 15.847 65.393 1.00 47.73 C ANISOU 3185 CG LEU A 290 6169 5511 6456 -181 -339 443 C ATOM 3186 CD1 LEU A 290 13.056 15.411 66.130 1.00 48.44 C ANISOU 3186 CD1 LEU A 290 6269 5649 6487 -239 -337 522 C ATOM 3187 CD2 LEU A 290 14.856 14.670 64.623 1.00 50.75 C ANISOU 3187 CD2 LEU A 290 6565 5769 6950 -162 -366 451 C ATOM 3188 N ALA A 291 14.146 20.000 63.117 1.00 40.82 N ANISOU 3188 N ALA A 291 5244 4729 5535 -124 -184 163 N ATOM 3189 CA ALA A 291 13.730 20.927 62.067 1.00 39.98 C ANISOU 3189 CA ALA A 291 5142 4623 5426 -116 -135 100 C ATOM 3190 C ALA A 291 14.929 21.490 61.317 1.00 44.08 C ANISOU 3190 C ALA A 291 5644 5097 6007 -64 -102 57 C ATOM 3191 O ALA A 291 14.864 21.599 60.092 1.00 44.02 O ANISOU 3191 O ALA A 291 5663 5047 6017 -45 -61 26 O ATOM 3192 CB ALA A 291 12.899 22.061 62.647 1.00 40.33 C ANISOU 3192 CB ALA A 291 5157 4760 5408 -143 -129 74 C ATOM 3193 N PHE A 292 16.039 21.793 62.037 1.00 40.59 N ANISOU 3193 N PHE A 292 5159 4663 5602 -39 -121 54 N ATOM 3194 CA PHE A 292 17.273 22.351 61.467 1.00 40.28 C ANISOU 3194 CA PHE A 292 5090 4577 5640 8 -87 12 C ATOM 3195 C PHE A 292 17.888 21.532 60.335 1.00 45.35 C ANISOU 3195 C PHE A 292 5763 5131 6338 36 -60 6 C ATOM 3196 O PHE A 292 18.654 22.090 59.544 1.00 45.10 O ANISOU 3196 O PHE A 292 5713 5064 6357 70 -7 -30 O ATOM 3197 CB PHE A 292 18.315 22.706 62.543 1.00 42.07 C ANISOU 3197 CB PHE A 292 5257 4821 5906 34 -123 1 C ATOM 3198 CG PHE A 292 17.881 23.701 63.597 1.00 43.29 C ANISOU 3198 CG PHE A 292 5364 5071 6015 23 -148 -17 C ATOM 3199 CD1 PHE A 292 16.892 24.642 63.330 1.00 45.66 C ANISOU 3199 CD1 PHE A 292 5655 5419 6272 -2 -119 -42 C ATOM 3200 CD2 PHE A 292 18.491 23.725 64.844 1.00 45.66 C ANISOU 3200 CD2 PHE A 292 5621 5411 6316 44 -206 -19 C ATOM 3201 CE1 PHE A 292 16.481 25.543 64.311 1.00 46.34 C ANISOU 3201 CE1 PHE A 292 5688 5597 6322 -11 -148 -71 C ATOM 3202 CE2 PHE A 292 18.096 24.648 65.815 1.00 48.21 C ANISOU 3202 CE2 PHE A 292 5892 5833 6594 42 -233 -49 C ATOM 3203 CZ PHE A 292 17.095 25.549 65.542 1.00 45.73 C ANISOU 3203 CZ PHE A 292 5565 5568 6243 13 -203 -77 C ATOM 3204 N PHE A 293 17.506 20.231 60.214 1.00 42.67 N ANISOU 3204 N PHE A 293 5464 4756 5992 21 -93 39 N ATOM 3205 CA PHE A 293 17.945 19.330 59.142 1.00 43.00 C ANISOU 3205 CA PHE A 293 5531 4721 6087 48 -79 22 C ATOM 3206 C PHE A 293 17.613 19.941 57.776 1.00 46.93 C ANISOU 3206 C PHE A 293 6051 5217 6562 69 -9 -20 C ATOM 3207 O PHE A 293 18.283 19.618 56.795 1.00 46.69 O ANISOU 3207 O PHE A 293 6028 5140 6574 107 24 -51 O ATOM 3208 CB PHE A 293 17.332 17.916 59.294 1.00 45.29 C ANISOU 3208 CB PHE A 293 5851 4977 6381 24 -134 62 C ATOM 3209 CG PHE A 293 17.540 16.999 58.104 1.00 47.40 C ANISOU 3209 CG PHE A 293 6137 5172 6701 53 -127 29 C ATOM 3210 CD1 PHE A 293 16.539 16.828 57.152 1.00 50.60 C ANISOU 3210 CD1 PHE A 293 6576 5577 7074 54 -107 3 C ATOM 3211 CD2 PHE A 293 18.756 16.354 57.905 1.00 50.18 C ANISOU 3211 CD2 PHE A 293 6468 5460 7137 86 -143 8 C ATOM 3212 CE1 PHE A 293 16.749 16.025 56.024 1.00 51.82 C ANISOU 3212 CE1 PHE A 293 6741 5676 7273 92 -104 -43 C ATOM 3213 CE2 PHE A 293 18.963 15.545 56.781 1.00 53.33 C ANISOU 3213 CE2 PHE A 293 6875 5802 7584 118 -137 -37 C ATOM 3214 CZ PHE A 293 17.957 15.385 55.850 1.00 51.29 C ANISOU 3214 CZ PHE A 293 6649 5553 7286 124 -118 -64 C ATOM 3215 N HIS A 294 16.611 20.859 57.724 1.00 43.19 N ANISOU 3215 N HIS A 294 5587 4799 6022 48 12 -23 N ATOM 3216 CA HIS A 294 16.191 21.576 56.516 1.00 42.90 C ANISOU 3216 CA HIS A 294 5576 4769 5953 69 72 -55 C ATOM 3217 C HIS A 294 17.370 22.245 55.791 1.00 47.11 C ANISOU 3217 C HIS A 294 6088 5278 6534 113 139 -77 C ATOM 3218 O HIS A 294 17.353 22.361 54.564 1.00 47.03 O ANISOU 3218 O HIS A 294 6108 5255 6506 146 191 -96 O ATOM 3219 CB HIS A 294 15.048 22.571 56.813 1.00 43.26 C ANISOU 3219 CB HIS A 294 5624 4877 5936 36 72 -57 C ATOM 3220 CG HIS A 294 15.472 23.878 57.415 1.00 46.44 C ANISOU 3220 CG HIS A 294 5972 5316 6356 33 88 -62 C ATOM 3221 ND1 HIS A 294 15.903 24.928 56.626 1.00 48.16 N ANISOU 3221 ND1 HIS A 294 6177 5525 6597 62 150 -79 N ATOM 3222 CD2 HIS A 294 15.483 24.271 58.710 1.00 48.09 C ANISOU 3222 CD2 HIS A 294 6134 5573 6566 7 49 -55 C ATOM 3223 CE1 HIS A 294 16.175 25.918 57.460 1.00 47.50 C ANISOU 3223 CE1 HIS A 294 6031 5472 6545 52 142 -86 C ATOM 3224 NE2 HIS A 294 15.935 25.568 58.727 1.00 47.79 N ANISOU 3224 NE2 HIS A 294 6045 5549 6565 22 79 -79 N ATOM 3225 N CYS A 295 18.404 22.649 56.561 1.00 43.52 N ANISOU 3225 N CYS A 295 5577 4816 6142 117 137 -75 N ATOM 3226 CA CYS A 295 19.639 23.264 56.074 1.00 43.37 C ANISOU 3226 CA CYS A 295 5519 4763 6195 155 200 -95 C ATOM 3227 C CYS A 295 20.473 22.284 55.239 1.00 48.68 C ANISOU 3227 C CYS A 295 6206 5379 6910 190 223 -115 C ATOM 3228 O CYS A 295 21.374 22.708 54.511 1.00 48.21 O ANISOU 3228 O CYS A 295 6126 5294 6899 224 295 -133 O ATOM 3229 CB CYS A 295 20.442 23.837 57.240 1.00 43.14 C ANISOU 3229 CB CYS A 295 5419 4737 6234 152 174 -101 C ATOM 3230 SG CYS A 295 19.628 25.211 58.093 1.00 46.15 S ANISOU 3230 SG CYS A 295 5762 5192 6583 123 156 -100 S ATOM 3231 N CYS A 296 20.164 20.981 55.344 1.00 46.56 N ANISOU 3231 N CYS A 296 5968 5091 6632 182 163 -112 N ATOM 3232 CA CYS A 296 20.821 19.918 54.596 1.00 47.61 C ANISOU 3232 CA CYS A 296 6109 5172 6810 214 167 -142 C ATOM 3233 C CYS A 296 19.958 19.448 53.409 1.00 51.76 C ANISOU 3233 C CYS A 296 6689 5707 7271 233 184 -162 C ATOM 3234 O CYS A 296 20.436 18.640 52.616 1.00 52.03 O ANISOU 3234 O CYS A 296 6726 5708 7334 269 192 -201 O ATOM 3235 CB CYS A 296 21.204 18.760 55.516 1.00 48.72 C ANISOU 3235 CB CYS A 296 6233 5271 7009 200 79 -132 C ATOM 3236 SG CYS A 296 22.244 19.241 56.922 1.00 52.98 S ANISOU 3236 SG CYS A 296 6711 5802 7618 193 44 -120 S ATOM 3237 N LEU A 297 18.718 19.984 53.249 1.00 47.61 N ANISOU 3237 N LEU A 297 6200 5228 6661 216 187 -147 N ATOM 3238 CA LEU A 297 17.817 19.613 52.142 1.00 47.17 C ANISOU 3238 CA LEU A 297 6196 5183 6542 241 195 -175 C ATOM 3239 C LEU A 297 18.298 20.106 50.785 1.00 51.11 C ANISOU 3239 C LEU A 297 6713 5695 7012 299 282 -203 C ATOM 3240 O LEU A 297 18.217 19.360 49.810 1.00 51.35 O ANISOU 3240 O LEU A 297 6769 5720 7024 342 284 -247 O ATOM 3241 CB LEU A 297 16.378 20.101 52.369 1.00 46.56 C ANISOU 3241 CB LEU A 297 6151 5148 6392 209 171 -159 C ATOM 3242 CG LEU A 297 15.565 19.453 53.474 1.00 50.77 C ANISOU 3242 CG LEU A 297 6678 5678 6933 155 92 -133 C ATOM 3243 CD1 LEU A 297 14.284 20.200 53.662 1.00 50.27 C ANISOU 3243 CD1 LEU A 297 6636 5662 6803 124 86 -127 C ATOM 3244 CD2 LEU A 297 15.267 17.984 53.177 1.00 53.77 C ANISOU 3244 CD2 LEU A 297 7070 6011 7349 165 39 -154 C ATOM 3245 N ASN A 298 18.741 21.374 50.715 1.00 46.96 N ANISOU 3245 N ASN A 298 6172 5190 6481 301 352 -178 N ATOM 3246 CA ASN A 298 19.239 22.004 49.492 1.00 47.05 C ANISOU 3246 CA ASN A 298 6198 5217 6463 351 450 -184 C ATOM 3247 C ASN A 298 20.474 21.270 48.902 1.00 50.91 C ANISOU 3247 C ASN A 298 6662 5675 7006 393 489 -221 C ATOM 3248 O ASN A 298 20.430 20.961 47.707 1.00 51.37 O ANISOU 3248 O ASN A 298 6754 5755 7008 445 529 -253 O ATOM 3249 CB ASN A 298 19.505 23.498 49.725 1.00 48.51 C ANISOU 3249 CB ASN A 298 6355 5415 6663 336 511 -139 C ATOM 3250 CG ASN A 298 19.907 24.312 48.515 1.00 70.21 C ANISOU 3250 CG ASN A 298 9120 8180 9379 382 619 -121 C ATOM 3251 OD1 ASN A 298 19.746 23.913 47.349 1.00 62.79 O ANISOU 3251 OD1 ASN A 298 8229 7263 8366 431 654 -140 O ATOM 3252 ND2 ASN A 298 20.398 25.508 48.781 1.00 61.83 N ANISOU 3252 ND2 ASN A 298 8014 7109 8371 368 675 -81 N ATOM 3253 N PRO A 299 21.547 20.936 49.677 1.00 46.18 N ANISOU 3253 N PRO A 299 6003 5029 6512 376 473 -229 N ATOM 3254 CA PRO A 299 22.692 20.230 49.073 1.00 46.28 C ANISOU 3254 CA PRO A 299 5989 5012 6585 416 507 -277 C ATOM 3255 C PRO A 299 22.442 18.751 48.793 1.00 50.40 C ANISOU 3255 C PRO A 299 6525 5515 7110 434 434 -331 C ATOM 3256 O PRO A 299 23.032 18.218 47.853 1.00 50.86 O ANISOU 3256 O PRO A 299 6577 5572 7177 482 471 -386 O ATOM 3257 CB PRO A 299 23.806 20.402 50.108 1.00 47.84 C ANISOU 3257 CB PRO A 299 6118 5159 6902 391 497 -274 C ATOM 3258 CG PRO A 299 23.279 21.356 51.125 1.00 51.62 C ANISOU 3258 CG PRO A 299 6587 5654 7373 347 471 -223 C ATOM 3259 CD PRO A 299 21.815 21.221 51.098 1.00 46.88 C ANISOU 3259 CD PRO A 299 6046 5095 6672 329 422 -203 C ATOM 3260 N ILE A 300 21.595 18.083 49.615 1.00 46.25 N ANISOU 3260 N ILE A 300 6011 4973 6589 396 331 -318 N ATOM 3261 CA ILE A 300 21.246 16.663 49.468 1.00 46.07 C ANISOU 3261 CA ILE A 300 5992 4919 6593 407 248 -362 C ATOM 3262 C ILE A 300 20.575 16.401 48.114 1.00 49.99 C ANISOU 3262 C ILE A 300 6530 5454 7008 463 272 -414 C ATOM 3263 O ILE A 300 20.804 15.350 47.515 1.00 49.64 O ANISOU 3263 O ILE A 300 6472 5390 7001 502 241 -481 O ATOM 3264 CB ILE A 300 20.469 16.115 50.713 1.00 48.67 C ANISOU 3264 CB ILE A 300 6322 5221 6949 349 145 -317 C ATOM 3265 CG1 ILE A 300 21.353 15.192 51.570 1.00 49.44 C ANISOU 3265 CG1 ILE A 300 6372 5252 7162 332 77 -317 C ATOM 3266 CG2 ILE A 300 19.128 15.444 50.385 1.00 49.03 C ANISOU 3266 CG2 ILE A 300 6404 5273 6953 350 90 -332 C ATOM 3267 CD1 ILE A 300 22.161 15.886 52.685 1.00 56.66 C ANISOU 3267 CD1 ILE A 300 7253 6157 8118 302 81 -274 C ATOM 3268 N LEU A 301 19.796 17.386 47.615 1.00 46.85 N ANISOU 3268 N LEU A 301 6182 5115 6506 473 322 -389 N ATOM 3269 CA LEU A 301 19.116 17.301 46.321 1.00 47.30 C ANISOU 3269 CA LEU A 301 6286 5218 6467 535 344 -436 C ATOM 3270 C LEU A 301 20.044 17.523 45.124 1.00 52.59 C ANISOU 3270 C LEU A 301 6956 5926 7102 603 442 -471 C ATOM 3271 O LEU A 301 19.681 17.177 43.996 1.00 52.84 O ANISOU 3271 O LEU A 301 7019 6000 7060 670 452 -529 O ATOM 3272 CB LEU A 301 17.863 18.188 46.266 1.00 46.80 C ANISOU 3272 CB LEU A 301 6276 5197 6307 522 346 -399 C ATOM 3273 CG LEU A 301 16.664 17.672 47.069 1.00 50.95 C ANISOU 3273 CG LEU A 301 6810 5699 6852 475 247 -394 C ATOM 3274 CD1 LEU A 301 15.510 18.642 47.000 1.00 50.82 C ANISOU 3274 CD1 LEU A 301 6839 5722 6747 462 253 -368 C ATOM 3275 CD2 LEU A 301 16.224 16.304 46.589 1.00 53.40 C ANISOU 3275 CD2 LEU A 301 7116 5980 7192 511 174 -469 C ATOM 3276 N TYR A 302 21.254 18.058 45.382 1.00 49.53 N ANISOU 3276 N TYR A 302 6526 5521 6770 588 513 -443 N ATOM 3277 CA TYR A 302 22.295 18.258 44.380 1.00 50.32 C ANISOU 3277 CA TYR A 302 6612 5650 6857 643 619 -470 C ATOM 3278 C TYR A 302 23.190 17.015 44.290 1.00 54.81 C ANISOU 3278 C TYR A 302 7125 6179 7520 664 583 -554 C ATOM 3279 O TYR A 302 23.945 16.875 43.326 1.00 55.65 O ANISOU 3279 O TYR A 302 7217 6317 7611 719 657 -604 O ATOM 3280 CB TYR A 302 23.133 19.514 44.682 1.00 51.70 C ANISOU 3280 CB TYR A 302 6759 5818 7065 616 719 -401 C ATOM 3281 CG TYR A 302 22.542 20.793 44.132 1.00 53.66 C ANISOU 3281 CG TYR A 302 7059 6121 7209 627 795 -334 C ATOM 3282 CD1 TYR A 302 22.229 20.920 42.783 1.00 56.40 C ANISOU 3282 CD1 TYR A 302 7460 6537 7432 696 858 -346 C ATOM 3283 CD2 TYR A 302 22.335 21.897 44.956 1.00 53.84 C ANISOU 3283 CD2 TYR A 302 7071 6127 7258 574 803 -260 C ATOM 3284 CE1 TYR A 302 21.679 22.094 42.273 1.00 57.24 C ANISOU 3284 CE1 TYR A 302 7617 6689 7444 709 922 -275 C ATOM 3285 CE2 TYR A 302 21.797 23.081 44.455 1.00 54.80 C ANISOU 3285 CE2 TYR A 302 7234 6289 7300 584 865 -198 C ATOM 3286 CZ TYR A 302 21.472 23.176 43.112 1.00 62.62 C ANISOU 3286 CZ TYR A 302 8284 7341 8167 650 925 -200 C ATOM 3287 OH TYR A 302 20.928 24.332 42.610 1.00 64.02 O ANISOU 3287 OH TYR A 302 8505 7553 8264 662 979 -131 O ATOM 3288 N ALA A 303 23.097 16.110 45.288 1.00 50.54 N ANISOU 3288 N ALA A 303 6553 5571 7078 621 470 -567 N ATOM 3289 CA ALA A 303 23.863 14.864 45.303 1.00 50.58 C ANISOU 3289 CA ALA A 303 6502 5525 7191 637 414 -645 C ATOM 3290 C ALA A 303 23.335 13.920 44.227 1.00 53.79 C ANISOU 3290 C ALA A 303 6921 5963 7555 703 378 -736 C ATOM 3291 O ALA A 303 22.148 13.968 43.897 1.00 53.13 O ANISOU 3291 O ALA A 303 6888 5915 7385 718 349 -732 O ATOM 3292 CB ALA A 303 23.783 14.204 46.671 1.00 50.88 C ANISOU 3292 CB ALA A 303 6511 5483 7337 575 298 -617 C ATOM 3293 N PHE A 304 24.231 13.090 43.663 1.00 50.25 N ANISOU 3293 N PHE A 304 6419 5501 7170 746 378 -829 N ATOM 3294 CA PHE A 304 23.959 12.109 42.603 1.00 50.24 C ANISOU 3294 CA PHE A 304 6408 5531 7149 821 340 -942 C ATOM 3295 C PHE A 304 23.375 12.725 41.318 1.00 54.86 C ANISOU 3295 C PHE A 304 7054 6226 7564 894 422 -959 C ATOM 3296 O PHE A 304 22.554 12.097 40.641 1.00 55.00 O ANISOU 3296 O PHE A 304 7088 6275 7535 950 364 -1031 O ATOM 3297 CB PHE A 304 23.123 10.919 43.120 1.00 51.26 C ANISOU 3297 CB PHE A 304 6519 5594 7364 803 190 -974 C ATOM 3298 CG PHE A 304 23.670 10.251 44.358 1.00 51.84 C ANISOU 3298 CG PHE A 304 6538 5561 7597 738 104 -947 C ATOM 3299 CD1 PHE A 304 24.757 9.392 44.282 1.00 54.96 C ANISOU 3299 CD1 PHE A 304 6860 5906 8115 755 72 -1027 C ATOM 3300 CD2 PHE A 304 23.086 10.469 45.598 1.00 52.75 C ANISOU 3300 CD2 PHE A 304 6675 5630 7737 662 51 -843 C ATOM 3301 CE1 PHE A 304 25.259 8.772 45.426 1.00 55.44 C ANISOU 3301 CE1 PHE A 304 6876 5867 8323 699 -17 -999 C ATOM 3302 CE2 PHE A 304 23.586 9.845 46.741 1.00 55.21 C ANISOU 3302 CE2 PHE A 304 6943 5852 8182 609 -31 -811 C ATOM 3303 CZ PHE A 304 24.670 9.001 46.648 1.00 53.73 C ANISOU 3303 CZ PHE A 304 6688 5609 8117 628 -67 -886 C ATOM 3304 N LEU A 305 23.817 13.956 40.984 1.00 51.34 N ANISOU 3304 N LEU A 305 6639 5836 7032 897 555 -893 N ATOM 3305 CA LEU A 305 23.370 14.693 39.802 1.00 51.43 C ANISOU 3305 CA LEU A 305 6716 5953 6874 964 645 -884 C ATOM 3306 C LEU A 305 24.112 14.208 38.555 1.00 56.77 C ANISOU 3306 C LEU A 305 7365 6700 7506 1054 708 -987 C ATOM 3307 O LEU A 305 25.334 14.345 38.456 1.00 56.81 O ANISOU 3307 O LEU A 305 7321 6701 7562 1050 793 -995 O ATOM 3308 CB LEU A 305 23.527 16.211 40.015 1.00 50.90 C ANISOU 3308 CB LEU A 305 6686 5905 6749 926 758 -759 C ATOM 3309 CG LEU A 305 22.627 17.133 39.192 1.00 55.39 C ANISOU 3309 CG LEU A 305 7339 6559 7148 970 815 -708 C ATOM 3310 CD1 LEU A 305 21.155 16.899 39.495 1.00 54.80 C ANISOU 3310 CD1 LEU A 305 7312 6473 7038 960 698 -712 C ATOM 3311 CD2 LEU A 305 22.959 18.577 39.467 1.00 57.31 C ANISOU 3311 CD2 LEU A 305 7598 6802 7374 927 923 -585 C ATOM 3312 N GLY A 306 23.361 13.600 37.642 1.00 54.14 N ANISOU 3312 N GLY A 306 7055 6428 7087 1135 659 -1075 N ATOM 3313 CA GLY A 306 23.896 13.023 36.414 1.00 55.44 C ANISOU 3313 CA GLY A 306 7193 6675 7196 1234 699 -1193 C ATOM 3314 C GLY A 306 24.384 11.600 36.612 1.00 60.25 C ANISOU 3314 C GLY A 306 7709 7223 7960 1241 594 -1323 C ATOM 3315 O GLY A 306 24.770 10.938 35.643 1.00 60.74 O ANISOU 3315 O GLY A 306 7732 7349 7996 1326 602 -1448 O ATOM 3316 N ALA A 307 24.361 11.124 37.879 1.00 56.66 N ANISOU 3316 N ALA A 307 7216 6645 7668 1154 493 -1293 N ATOM 3317 CA ALA A 307 24.780 9.786 38.298 1.00 56.99 C ANISOU 3317 CA ALA A 307 7168 6600 7886 1143 375 -1391 C ATOM 3318 C ALA A 307 23.816 8.724 37.798 1.00 62.47 C ANISOU 3318 C ALA A 307 7847 7299 8591 1206 252 -1503 C ATOM 3319 O ALA A 307 22.599 8.880 37.912 1.00 61.41 O ANISOU 3319 O ALA A 307 7767 7164 8402 1204 201 -1466 O ATOM 3320 CB ALA A 307 24.896 9.719 39.812 1.00 56.67 C ANISOU 3320 CB ALA A 307 7108 6435 7989 1035 306 -1301 C ATOM 3321 N LYS A 308 24.378 7.647 37.232 1.00 61.22 N ANISOU 3321 N LYS A 308 7605 7140 8514 1266 201 -1650 N ATOM 3322 CA LYS A 308 23.650 6.519 36.658 1.00 62.04 C ANISOU 3322 CA LYS A 308 7668 7245 8659 1340 78 -1788 C ATOM 3323 C LYS A 308 23.502 5.403 37.705 1.00 66.14 C ANISOU 3323 C LYS A 308 8116 7614 9402 1275 -76 -1799 C ATOM 3324 O LYS A 308 24.460 4.665 37.945 1.00 66.81 O ANISOU 3324 O LYS A 308 8115 7637 9632 1261 -117 -1862 O ATOM 3325 CB LYS A 308 24.418 6.011 35.425 1.00 66.20 C ANISOU 3325 CB LYS A 308 8135 7866 9153 1446 114 -1950 C ATOM 3326 CG LYS A 308 23.615 5.965 34.131 1.00 84.20 C ANISOU 3326 CG LYS A 308 10447 10272 11273 1571 114 -2052 C ATOM 3327 CD LYS A 308 24.515 5.681 32.912 1.00 96.69 C ANISOU 3327 CD LYS A 308 11978 11975 12786 1676 182 -2197 C ATOM 3328 CE LYS A 308 24.866 4.219 32.724 1.00106.99 C ANISOU 3328 CE LYS A 308 13152 13231 14267 1721 53 -2383 C ATOM 3329 NZ LYS A 308 25.869 4.027 31.644 1.00117.09 N ANISOU 3329 NZ LYS A 308 14376 14631 15482 1812 133 -2520 N ATOM 3330 N PHE A 309 22.315 5.285 38.338 1.00 61.67 N ANISOU 3330 N PHE A 309 7581 6985 8865 1234 -161 -1736 N ATOM 3331 CA PHE A 309 22.027 4.256 39.351 1.00 61.26 C ANISOU 3331 CA PHE A 309 7468 6790 9016 1170 -302 -1723 C ATOM 3332 C PHE A 309 21.809 2.907 38.642 1.00 65.78 C ANISOU 3332 C PHE A 309 7948 7339 9709 1252 -422 -1898 C ATOM 3333 O PHE A 309 20.670 2.463 38.475 1.00 65.52 O ANISOU 3333 O PHE A 309 7912 7284 9700 1281 -505 -1937 O ATOM 3334 CB PHE A 309 20.791 4.658 40.187 1.00 62.26 C ANISOU 3334 CB PHE A 309 7660 6873 9122 1102 -333 -1596 C ATOM 3335 CG PHE A 309 21.022 5.547 41.393 1.00 62.97 C ANISOU 3335 CG PHE A 309 7802 6929 9193 995 -278 -1425 C ATOM 3336 CD1 PHE A 309 21.690 6.762 41.268 1.00 65.60 C ANISOU 3336 CD1 PHE A 309 8189 7339 9397 985 -143 -1361 C ATOM 3337 CD2 PHE A 309 20.484 5.217 42.632 1.00 64.52 C ANISOU 3337 CD2 PHE A 309 7994 7024 9495 907 -358 -1326 C ATOM 3338 CE1 PHE A 309 21.879 7.590 42.377 1.00 65.38 C ANISOU 3338 CE1 PHE A 309 8199 7281 9362 895 -101 -1218 C ATOM 3339 CE2 PHE A 309 20.664 6.054 43.737 1.00 66.21 C ANISOU 3339 CE2 PHE A 309 8254 7222 9681 818 -311 -1180 C ATOM 3340 CZ PHE A 309 21.364 7.231 43.603 1.00 63.80 C ANISOU 3340 CZ PHE A 309 7994 6989 9259 815 -187 -1134 C ATOM 3341 N LYS A 310 22.911 2.271 38.200 1.00 62.96 N ANISOU 3341 N LYS A 310 7505 6983 9432 1293 -432 -2015 N ATOM 3342 CA LYS A 310 22.869 1.032 37.419 1.00 64.00 C ANISOU 3342 CA LYS A 310 7533 7105 9678 1382 -541 -2205 C ATOM 3343 C LYS A 310 23.599 -0.163 38.040 1.00 67.67 C ANISOU 3343 C LYS A 310 7882 7433 10395 1344 -660 -2257 C ATOM 3344 O LYS A 310 23.112 -1.291 37.931 1.00 67.70 O ANISOU 3344 O LYS A 310 7801 7363 10559 1377 -798 -2357 O ATOM 3345 CB LYS A 310 23.411 1.286 35.993 1.00 68.00 C ANISOU 3345 CB LYS A 310 8034 7769 10034 1500 -451 -2345 C ATOM 3346 CG LYS A 310 22.630 2.318 35.178 1.00 83.19 C ANISOU 3346 CG LYS A 310 10067 9835 11708 1562 -351 -2316 C ATOM 3347 CD LYS A 310 21.603 1.666 34.263 1.00 95.26 C ANISOU 3347 CD LYS A 310 11568 11406 13219 1676 -446 -2466 C ATOM 3348 CE LYS A 310 20.367 2.513 34.093 1.00105.95 C ANISOU 3348 CE LYS A 310 13033 12815 14408 1691 -414 -2388 C ATOM 3349 NZ LYS A 310 19.472 2.428 35.279 1.00114.17 N ANISOU 3349 NZ LYS A 310 14093 13721 15567 1587 -491 -2268 N ATOM 3350 N THR A 311 24.784 0.071 38.631 1.00 63.61 N ANISOU 3350 N THR A 311 7357 6884 9926 1282 -612 -2201 N ATOM 3351 CA THR A 311 25.632 -0.978 39.211 1.00 63.53 C ANISOU 3351 CA THR A 311 7241 6747 10150 1248 -720 -2249 C ATOM 3352 C THR A 311 25.055 -1.605 40.481 1.00 65.86 C ANISOU 3352 C THR A 311 7523 6883 10617 1159 -846 -2134 C ATOM 3353 O THR A 311 24.448 -0.903 41.291 1.00 64.16 O ANISOU 3353 O THR A 311 7396 6653 10326 1087 -809 -1968 O ATOM 3354 CB THR A 311 27.075 -0.477 39.407 1.00 72.13 C ANISOU 3354 CB THR A 311 8325 7851 11231 1217 -627 -2234 C ATOM 3355 OG1 THR A 311 27.343 0.620 38.527 1.00 72.33 O ANISOU 3355 OG1 THR A 311 8415 8032 11037 1266 -460 -2243 O ATOM 3356 CG2 THR A 311 28.098 -1.571 39.180 1.00 72.08 C ANISOU 3356 CG2 THR A 311 8189 7785 11416 1247 -714 -2392 C ATOM 3357 N SER A 312 25.255 -2.929 40.652 1.00 62.74 N ANISOU 3357 N SER A 312 7014 6370 10456 1165 -995 -2221 N ATOM 3358 CA SER A 312 24.797 -3.691 41.818 1.00 82.17 C ANISOU 3358 CA SER A 312 9447 8669 13106 1085 -1123 -2115 C ATOM 3359 C SER A 312 25.709 -4.887 42.088 1.00102.06 C ANISOU 3359 C SER A 312 11842 11062 15874 1080 -1252 -2198 C ATOM 3360 O SER A 312 25.962 -5.227 43.242 1.00 62.34 O ANISOU 3360 O SER A 312 6806 5908 10974 998 -1321 -2078 O ATOM 3361 CB SER A 312 23.356 -4.153 41.634 1.00 85.67 C ANISOU 3361 CB SER A 312 9882 9085 13585 1108 -1197 -2123 C ATOM 3362 OG SER A 312 23.205 -4.920 40.451 1.00 95.80 O ANISOU 3362 OG SER A 312 11070 10398 14930 1217 -1261 -2333 O TER 3363 SER A 312 HETATM 3364 C1 ITD A1500 13.792 30.602 69.119 1.00 86.36 C HETATM 3365 N1 ITD A1500 15.438 28.886 69.702 1.00 82.01 N HETATM 3366 S1 ITD A1500 16.040 26.894 71.584 1.00 65.96 S HETATM 3367 C2 ITD A1500 15.135 30.316 69.780 1.00 26.42 C HETATM 3368 N2 ITD A1500 15.429 29.359 71.844 1.00 56.24 N HETATM 3369 S2 ITD A1500 17.050 30.502 74.625 1.00100.45 S HETATM 3370 C3 ITD A1500 16.256 31.102 69.107 1.00 71.13 C HETATM 3371 N3 ITD A1500 17.521 28.498 76.139 1.00189.72 N HETATM 3372 C4 ITD A1500 15.605 28.424 70.950 1.00 37.82 C HETATM 3373 N4 ITD A1500 19.348 29.278 74.885 1.00 38.39 N HETATM 3374 C5 ITD A1500 15.961 27.546 73.193 1.00 46.39 C HETATM 3375 C6 ITD A1500 15.079 30.654 71.281 1.00143.20 C HETATM 3376 C7 ITD A1500 15.601 28.911 73.113 1.00 58.04 C HETATM 3377 C8 ITD A1500 15.465 29.802 74.320 1.00127.39 C HETATM 3378 C9 ITD A1500 18.060 29.336 75.248 1.00145.61 C HETATM 3379 C10 ITD A1500 18.175 27.411 76.849 1.00176.70 C HETATM 3380 C11 ITD A1500 19.100 27.912 77.954 1.00 19.74 C HETATM 3381 C12 ITD A1500 19.532 26.728 78.817 1.00 60.79 C HETATM 3382 C13 ITD A1500 20.231 25.658 77.978 1.00117.60 C HETATM 3383 C14 ITD A1500 19.409 25.218 76.764 1.00 45.59 C HETATM 3384 C15 ITD A1500 18.883 26.400 75.948 1.00 92.48 C HETATM 3385 C16 ITD A1500 19.881 29.370 73.525 1.00 36.09 C HETATM 3386 C17 ITD A1500 18.918 28.964 72.409 1.00119.82 C HETATM 3387 C18 ITD A1500 19.573 29.085 71.035 1.00127.23 C HETATM 3388 C19 ITD A1500 20.158 30.474 70.790 1.00 21.04 C HETATM 3389 C20 ITD A1500 21.168 30.825 71.876 1.00 16.48 C HETATM 3390 C21 ITD A1500 20.526 30.728 73.257 1.00 73.02 C HETATM 3391 C8 OLC A1600 26.103 16.149 51.984 1.00 12.24 C HETATM 3392 C24 OLC A1600 25.035 21.215 40.758 1.00111.53 C HETATM 3393 C7 OLC A1600 26.735 16.544 50.652 1.00 63.37 C HETATM 3394 C6 OLC A1600 25.699 16.609 49.536 1.00 17.29 C HETATM 3395 C5 OLC A1600 26.345 16.614 48.155 1.00 15.10 C HETATM 3396 C4 OLC A1600 26.849 17.994 47.735 1.00 52.47 C HETATM 3397 C3 OLC A1600 26.414 18.358 46.312 1.00 3.00 C HETATM 3398 C2 OLC A1600 26.267 19.871 46.176 1.00 73.54 C HETATM 3399 C21 OLC A1600 26.670 20.832 42.617 1.00100.99 C HETATM 3400 C1 OLC A1600 27.025 20.400 44.979 1.00 58.71 C HETATM 3401 C22 OLC A1600 25.877 21.885 41.844 1.00 22.44 C HETATM 3402 O19 OLC A1600 28.224 20.625 44.987 1.00134.81 O HETATM 3403 O25 OLC A1600 24.569 22.162 39.786 1.00 31.63 O HETATM 3404 O23 OLC A1600 25.056 22.670 42.716 1.00 67.58 O HETATM 3405 O20 OLC A1600 26.169 20.609 43.932 1.00 47.79 O HETATM 3406 C8 OLC A1601 30.780 20.807 74.082 1.00 49.66 C HETATM 3407 C24 OLC A1601 28.816 20.514 82.924 1.00 62.74 C HETATM 3408 C7 OLC A1601 31.223 20.958 75.531 1.00 33.37 C HETATM 3409 C6 OLC A1601 32.541 21.720 75.633 1.00 29.68 C HETATM 3410 C5 OLC A1601 33.111 21.684 77.050 1.00 68.51 C HETATM 3411 C4 OLC A1601 32.148 22.291 78.069 1.00 41.34 C HETATM 3412 C3 OLC A1601 32.803 23.427 78.850 1.00 40.04 C HETATM 3413 C2 OLC A1601 33.611 22.900 80.031 1.00 41.76 C HETATM 3414 C21 OLC A1601 30.609 21.930 81.906 1.00 65.94 C HETATM 3415 C1 OLC A1601 32.758 22.902 81.277 1.00119.22 C HETATM 3416 C22 OLC A1601 29.999 20.535 81.967 1.00 84.04 C HETATM 3417 O19 OLC A1601 32.874 23.720 82.173 1.00 68.45 O HETATM 3418 O25 OLC A1601 27.737 21.293 82.400 1.00 63.07 O HETATM 3419 O23 OLC A1601 29.581 20.124 80.663 1.00 81.52 O HETATM 3420 O20 OLC A1601 31.864 21.863 81.233 1.00 70.04 O HETATM 3421 C9 OLC A1602 32.881 15.307 65.364 1.00 59.60 C HETATM 3422 C8 OLC A1602 31.814 14.622 66.189 1.00 97.56 C HETATM 3423 C24 OLC A1602 28.164 15.467 78.035 1.00116.65 C HETATM 3424 C7 OLC A1602 31.275 15.576 67.251 1.00153.18 C HETATM 3425 C6 OLC A1602 29.915 15.113 67.761 1.00 71.97 C HETATM 3426 C5 OLC A1602 29.668 15.604 69.182 1.00 89.15 C HETATM 3427 C4 OLC A1602 28.399 14.977 69.744 1.00 42.94 C HETATM 3428 C3 OLC A1602 28.551 14.679 71.229 1.00 51.92 C HETATM 3429 C2 OLC A1602 27.337 15.140 72.024 1.00 35.25 C HETATM 3430 C21 OLC A1602 27.971 15.866 75.606 1.00 66.02 C HETATM 3431 C1 OLC A1602 27.803 15.977 73.191 1.00 87.52 C HETATM 3432 C22 OLC A1602 27.471 15.002 76.755 1.00 78.36 C HETATM 3433 O19 OLC A1602 28.364 17.055 73.069 1.00 97.37 O HETATM 3434 O25 OLC A1602 27.255 15.503 79.143 1.00131.92 O HETATM 3435 O23 OLC A1602 26.044 15.116 76.848 1.00 55.45 O HETATM 3436 O20 OLC A1602 27.504 15.338 74.367 1.00 78.05 O HETATM 3437 C1 GOL A1603 10.972 29.048 58.068 1.00 60.53 C HETATM 3438 O1 GOL A1603 12.355 29.086 58.432 1.00 59.56 O HETATM 3439 C2 GOL A1603 10.184 28.243 59.103 1.00 60.31 C HETATM 3440 O2 GOL A1603 8.839 28.094 58.630 1.00 61.10 O HETATM 3441 C3 GOL A1603 10.234 28.976 60.456 1.00 60.40 C HETATM 3442 O3 GOL A1603 9.823 28.125 61.527 1.00 60.10 O CONECT 609 1229 CONECT 1229 609 CONECT 3364 3367 CONECT 3365 3367 3372 CONECT 3366 3372 3374 CONECT 3367 3364 3365 3370 3375 CONECT 3368 3372 3375 3376 CONECT 3369 3377 3378 CONECT 3370 3367 CONECT 3371 3378 3379 CONECT 3372 3365 3366 3368 CONECT 3373 3378 3385 CONECT 3374 3366 3376 CONECT 3375 3367 3368 CONECT 3376 3368 3374 3377 CONECT 3377 3369 3376 CONECT 3378 3369 3371 3373 CONECT 3379 3371 3380 3384 CONECT 3380 3379 3381 CONECT 3381 3380 3382 CONECT 3382 3381 3383 CONECT 3383 3382 3384 CONECT 3384 3379 3383 CONECT 3385 3373 3386 3390 CONECT 3386 3385 3387 CONECT 3387 3386 3388 CONECT 3388 3387 3389 CONECT 3389 3388 3390 CONECT 3390 3385 3389 CONECT 3391 3393 CONECT 3392 3401 3403 CONECT 3393 3391 3394 CONECT 3394 3393 3395 CONECT 3395 3394 3396 CONECT 3396 3395 3397 CONECT 3397 3396 3398 CONECT 3398 3397 3400 CONECT 3399 3401 3405 CONECT 3400 3398 3402 3405 CONECT 3401 3392 3399 3404 CONECT 3402 3400 CONECT 3403 3392 CONECT 3404 3401 CONECT 3405 3399 3400 CONECT 3406 3408 CONECT 3407 3416 3418 CONECT 3408 3406 3409 CONECT 3409 3408 3410 CONECT 3410 3409 3411 CONECT 3411 3410 3412 CONECT 3412 3411 3413 CONECT 3413 3412 3415 CONECT 3414 3416 3420 CONECT 3415 3413 3417 3420 CONECT 3416 3407 3414 3419 CONECT 3417 3415 CONECT 3418 3407 CONECT 3419 3416 CONECT 3420 3414 3415 CONECT 3421 3422 CONECT 3422 3421 3424 CONECT 3423 3432 3434 CONECT 3424 3422 3425 CONECT 3425 3424 3426 CONECT 3426 3425 3427 CONECT 3427 3426 3428 CONECT 3428 3427 3429 CONECT 3429 3428 3431 CONECT 3430 3432 3436 CONECT 3431 3429 3433 3436 CONECT 3432 3423 3430 3435 CONECT 3433 3431 CONECT 3434 3423 CONECT 3435 3432 CONECT 3436 3430 3431 CONECT 3437 3438 3439 CONECT 3438 3437 CONECT 3439 3437 3440 3441 CONECT 3440 3439 CONECT 3441 3439 3442 CONECT 3442 3441 MASTER 474 0 5 24 5 0 9 6 3435 1 81 40 END