HEADER SIGNALING PROTEIN 30-JAN-17 5UNH TITLE SYNCHROTRON STRUCTURE OF HUMAN ANGIOTENSIN II TYPE 2 RECEPTOR IN TITLE 2 COMPLEX WITH COMPOUND 2 (N-[(FURAN-2-YL)METHYL]-N-(4-OXO-2-PROPYL-3- TITLE 3 {[2'-(2H-TETRAZOL-5-YL)[1,1'- BIPHENYL]-4-YL]METHYL}-3,4- TITLE 4 DIHYDROQUINAZOLIN-6-YL)BENZAMIDE) COMPND MOL_ID: 1; COMPND 2 MOLECULE: SOLUBLE CYTOCHROME B562,TYPE-2 ANGIOTENSIN II RECEPTOR; COMPND 3 CHAIN: A, B; COMPND 4 FRAGMENT: UNP P0ABE7 RESIDUES 23-128 AND UNP P50052 35-335 LINKED VIA COMPND 5 LINKER RESDIUES GSGS,UNP P0ABE7 RESIDUES 23-128 AND UNP P50052 35-335 COMPND 6 LINKED VIA LINKER RESDIUES GSGS; COMPND 7 SYNONYM: CYTOCHROME B-562,ANGIOTENSIN II TYPE-2 RECEPTOR,AT2; COMPND 8 ENGINEERED: YES; COMPND 9 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI, HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 562, 9606; SOURCE 5 GENE: CYBC, AGTR2; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SF9; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PFASTBAC KEYWDS HUMAN ANGIOTENSIN II RECEPTOR COMPLEX, GPCR SIGNALING, GPCR, BRIL, KEYWDS 2 MEMBRANE PROTEIN, LCP, SYNCHROTRON, BLOOD PRESSURE REGULATION, KEYWDS 3 COMPOUND 2 (CPD 2), SIGNALING PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR H.ZHANG,G.W.HAN,A.BATYUK,A.ISHCHENKO,K.L.WHITE,N.PATEL,A.SADYBEKOV, AUTHOR 2 B.ZAMLYNNY,M.T.RUDD,K.HOLLENSTEIN,A.TOLSTIKOVA,T.A.WHITE,M.S.HUNTER, AUTHOR 3 U.WEIERSTALL,W.LIU,K.BABAOGLU,E.L.MOORE,R.D.KATZ,J.M.SHIPMAN, AUTHOR 4 M.GARCIA-CALVO,S.SHARMA,P.SHETH,S.M.SOISSON,R.C.STEVENS,V.KATRITCH, AUTHOR 5 V.CHEREZOV REVDAT 2 10-MAY-17 5UNH 1 JRNL REVDAT 1 05-APR-17 5UNH 0 JRNL AUTH H.ZHANG,G.W.HAN,A.BATYUK,A.ISHCHENKO,K.L.WHITE,N.PATEL, JRNL AUTH 2 A.SADYBEKOV,B.ZAMLYNNY,M.T.RUDD,K.HOLLENSTEIN,A.TOLSTIKOVA, JRNL AUTH 3 T.A.WHITE,M.S.HUNTER,U.WEIERSTALL,W.LIU,K.BABAOGLU, JRNL AUTH 4 E.L.MOORE,R.D.KATZ,J.M.SHIPMAN,M.GARCIA-CALVO,S.SHARMA, JRNL AUTH 5 P.SHETH,S.M.SOISSON,R.C.STEVENS,V.KATRITCH,V.CHEREZOV JRNL TITL STRUCTURAL BASIS FOR SELECTIVITY AND DIVERSITY IN JRNL TITL 2 ANGIOTENSIN II RECEPTORS. JRNL REF NATURE V. 544 327 2017 JRNL REFN ESSN 1476-4687 JRNL PMID 28379944 JRNL DOI 10.1038/NATURE22035 REMARK 2 REMARK 2 RESOLUTION. 2.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.10.2 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) : 2.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 90.3 REMARK 3 NUMBER OF REFLECTIONS : 18462 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) : 0.218 REMARK 3 R VALUE (WORKING SET) : 0.216 REMARK 3 FREE R VALUE : 0.259 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.910 REMARK 3 FREE R VALUE TEST SET COUNT : 906 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 : 9 REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.08 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 82.73 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2714 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2170 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2584 REMARK 3 BIN R VALUE (WORKING SET) : 0.2160 REMARK 3 BIN FREE R VALUE : 0.2460 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.79 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 130 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.000 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 5783 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 94 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 79.10 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 100.3 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.32990 REMARK 3 B22 (A**2) : -4.87500 REMARK 3 B33 (A**2) : 4.54510 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -2.02410 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.470 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.421 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 : 0.922 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.861 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 6020 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 8214 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 2659 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : 106 ; 2.000 ; HARMONIC REMARK 3 GENERAL PLANES : 971 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 6020 ; 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 : 822 ; 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 : 6972 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.009 REMARK 3 BOND ANGLES (DEGREES) : 0.97 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.13 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 3.18 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 4 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: { A| 39 - 333 } REMARK 3 ORIGIN FOR THE GROUP (A): 114.6504 -74.2066 5.9264 REMARK 3 T TENSOR REMARK 3 T11: -0.2559 T22: -0.2318 REMARK 3 T33: 0.1474 T12: -0.0214 REMARK 3 T13: -0.0392 T23: -0.0205 REMARK 3 L TENSOR REMARK 3 L11: 3.4674 L22: 1.8742 REMARK 3 L33: 1.0939 L12: -0.8538 REMARK 3 L13: -0.5701 L23: -0.5120 REMARK 3 S TENSOR REMARK 3 S11: -0.0473 S12: -0.2428 S13: 0.2591 REMARK 3 S21: -0.0088 S22: 0.0117 S23: -0.0896 REMARK 3 S31: 0.0007 S32: 0.0623 S33: 0.0357 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: { B| 44 - 332 } REMARK 3 ORIGIN FOR THE GROUP (A): 109.7739 -88.1784 34.4947 REMARK 3 T TENSOR REMARK 3 T11: -0.3933 T22: 0.2711 REMARK 3 T33: -0.3425 T12: 0.2710 REMARK 3 T13: 0.0512 T23: 0.1672 REMARK 3 L TENSOR REMARK 3 L11: 4.1142 L22: 2.8509 REMARK 3 L33: 1.8774 L12: -1.5660 REMARK 3 L13: -0.6046 L23: 0.0902 REMARK 3 S TENSOR REMARK 3 S11: -0.4839 S12: -1.2601 S13: -0.2359 REMARK 3 S21: 0.6175 S22: 0.5784 S23: 0.3113 REMARK 3 S31: 0.1546 S32: 0.5355 S33: -0.0944 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: { A| 1001 - 1106 } REMARK 3 ORIGIN FOR THE GROUP (A): 78.2380 -55.0168 4.2674 REMARK 3 T TENSOR REMARK 3 T11: -0.4129 T22: -0.3365 REMARK 3 T33: 0.1578 T12: 0.0408 REMARK 3 T13: -0.0340 T23: 0.0506 REMARK 3 L TENSOR REMARK 3 L11: 12.4995 L22: 6.6114 REMARK 3 L33: 8.6577 L12: -2.3005 REMARK 3 L13: -3.5578 L23: 0.1853 REMARK 3 S TENSOR REMARK 3 S11: -0.0993 S12: -0.0642 S13: 0.1867 REMARK 3 S21: -0.3535 S22: 0.1118 S23: -0.3115 REMARK 3 S31: 0.0857 S32: 0.0440 S33: -0.0125 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: { B| 1002 - 1101 } REMARK 3 ORIGIN FOR THE GROUP (A): 142.7703 -66.7816 41.3025 REMARK 3 T TENSOR REMARK 3 T11: -0.3997 T22: 0.0844 REMARK 3 T33: -0.2247 T12: -0.1613 REMARK 3 T13: 0.0305 T23: -0.1066 REMARK 3 L TENSOR REMARK 3 L11: 4.1985 L22: 7.5969 REMARK 3 L33: 7.6322 L12: -0.9950 REMARK 3 L13: -3.4413 L23: -0.3795 REMARK 3 S TENSOR REMARK 3 S11: 0.0253 S12: -0.0181 S13: -0.4040 REMARK 3 S21: 0.6468 S22: -0.0717 S23: 0.3650 REMARK 3 S31: 0.0636 S32: -0.4027 S33: 0.0463 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 5UNH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-FEB-17. REMARK 100 THE DEPOSITION ID IS D_1000226118. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 04-DEC-16 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 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) : 1.033 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTFEL REMARK 200 DATA SCALING SOFTWARE : CRYSTFEL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18479 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 91.0 REMARK 200 DATA REDUNDANCY : 3.500 REMARK 200 R MERGE (I) : 0.13000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 5.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.06 REMARK 200 COMPLETENESS FOR SHELL (%) : 83.2 REMARK 200 DATA REDUNDANCY IN SHELL : 2.50 REMARK 200 R MERGE FOR SHELL (I) : 0.44000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.800 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: 4YAY, 4ZUD REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 50.42 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS-HCL, PH 8.0, 25 MM REMARK 280 POTASSIUM FORMATE, 25% (V/V) PEG400, AND 0.3% (V/V) (+/-)-2- REMARK 280 METHYL-2,4-PENTANEDIOL, LIPIDIC CUBIC PHASE, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 34.10000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 300 REMARK: AUTHORS STATE THAT THE BIOLOGICAL UNIT IS UNKNOWN REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1790 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 37860 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY A 1107 REMARK 465 SER A 1108 REMARK 465 GLY A 1109 REMARK 465 SER A 1110 REMARK 465 CYS A 35 REMARK 465 SER A 36 REMARK 465 GLN A 37 REMARK 465 LYS A 38 REMARK 465 GLY A 74 REMARK 465 PRO A 75 REMARK 465 LYS A 76 REMARK 465 PRO A 149 REMARK 465 PHE A 150 REMARK 465 LEU A 151 REMARK 465 SER A 152 REMARK 465 GLN A 153 REMARK 465 ARG A 154 REMARK 465 ARG A 155 REMARK 465 ASN A 156 REMARK 465 PRO A 157 REMARK 465 TRP A 158 REMARK 465 GLN A 159 REMARK 465 ASN A 242 REMARK 465 SER A 243 REMARK 465 ARG A 334 REMARK 465 VAL A 335 REMARK 465 ALA B 1001 REMARK 465 ILE B 1102 REMARK 465 GLN B 1103 REMARK 465 LYS B 1104 REMARK 465 TYR B 1105 REMARK 465 LEU B 1106 REMARK 465 GLY B 1107 REMARK 465 SER B 1108 REMARK 465 GLY B 1109 REMARK 465 SER B 1110 REMARK 465 CYS B 35 REMARK 465 SER B 36 REMARK 465 GLN B 37 REMARK 465 LYS B 38 REMARK 465 PRO B 39 REMARK 465 SER B 40 REMARK 465 ASP B 41 REMARK 465 LYS B 42 REMARK 465 HIS B 43 REMARK 465 CYS B 71 REMARK 465 GLN B 72 REMARK 465 LYS B 73 REMARK 465 GLY B 74 REMARK 465 PRO B 75 REMARK 465 LYS B 76 REMARK 465 LEU B 151 REMARK 465 SER B 152 REMARK 465 GLN B 153 REMARK 465 ARG B 154 REMARK 465 ARG B 155 REMARK 465 ASN B 156 REMARK 465 PRO B 157 REMARK 465 TRP B 158 REMARK 465 GLN B 159 REMARK 465 GLU B 202 REMARK 465 LYS B 203 REMARK 465 PHE B 333 REMARK 465 ARG B 334 REMARK 465 VAL B 335 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 41 CG OD1 OD2 REMARK 470 LYS A 77 CG CD CE NZ REMARK 470 TYR A 148 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 TYR A 162 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU A 188 CG CD OE1 OE2 REMARK 470 TYR A 189 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU A 202 CG CD OE1 OE2 REMARK 470 LYS A 203 CG CD CE NZ REMARK 470 HIS A 237 CG ND1 CD2 CE1 NE2 REMARK 470 LYS A 240 CG CD CE NZ REMARK 470 THR A 241 OG1 CG2 REMARK 470 LYS A 246 CG CD CE NZ REMARK 470 ASN A 247 CG OD1 ND2 REMARK 470 ARG A 251 CG CD NE CZ NH1 NH2 REMARK 470 GLN A 326 CG CD OE1 NE2 REMARK 470 LYS A 328 CG CD CE NZ REMARK 470 LEU A 329 CG CD1 CD2 REMARK 470 ARG A 330 CG CD NE CZ NH1 NH2 REMARK 470 PHE A 333 CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR B 52 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 PHE B 69 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS B 77 CG CD CE NZ REMARK 470 ARG B 107 CG CD NE CZ NH1 NH2 REMARK 470 TRP B 110 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP B 110 CZ3 CH2 REMARK 470 PHE B 112 CG CD1 CD2 CE1 CE2 CZ REMARK 470 MET B 116 CG SD CE REMARK 470 PHE B 120 CG CD1 CD2 CE1 CE2 CZ REMARK 470 PHE B 150 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ILE B 187 CG1 CG2 CD1 REMARK 470 GLU B 188 CG CD OE1 OE2 REMARK 470 TYR B 189 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LEU B 190 CG CD1 CD2 REMARK 470 PHE B 199 CG CD1 CD2 CE1 CE2 CZ REMARK 470 MET B 214 CG SD CE REMARK 470 LYS B 215 CG CD CE NZ REMARK 470 LYS B 236 CG CD CE NZ REMARK 470 LYS B 240 CG CD CE NZ REMARK 470 ARG B 248 CG CD NE CZ NH1 NH2 REMARK 470 ILE B 249 CG1 CG2 CD1 REMARK 470 THR B 250 OG1 CG2 REMARK 470 ASP B 252 CG OD1 OD2 REMARK 470 GLN B 253 CG CD OE1 NE2 REMARK 470 LYS B 256 CG CD CE NZ REMARK 470 ASN B 288 CG OD1 ND2 REMARK 470 PHE B 302 CG CD1 CD2 CE1 CE2 CZ REMARK 470 PHE B 308 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG B 324 CG CD NE CZ NH1 NH2 REMARK 470 PHE B 325 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLN B 326 CG CD OE1 NE2 REMARK 470 GLN B 327 CG CD OE1 NE2 REMARK 470 LYS B 328 CG CD CE NZ REMARK 470 ARG B 330 CG CD NE CZ NH1 NH2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 LEU A1003 -62.81 69.78 REMARK 500 PRO A1046 21.68 -71.91 REMARK 500 LYS A1047 -24.13 -142.16 REMARK 500 ASP A 41 7.79 -68.13 REMARK 500 PHE A 220 -53.98 -139.97 REMARK 500 MET B1058 32.67 -98.39 REMARK 500 TYR B 108 71.61 61.78 REMARK 500 PRO B 149 53.81 -94.14 REMARK 500 PHE B 220 -53.89 -140.47 REMARK 500 ASN B 242 76.33 58.55 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue 8EM A 1501 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue 8EM B 1501 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 5UNF RELATED DB: PDB REMARK 900 RELATED ID: 5UNG RELATED DB: PDB DBREF 5UNH A 1001 1106 UNP P0ABE7 C562_ECOLX 23 128 DBREF 5UNH A 35 335 UNP P50052 AGTR2_HUMAN 35 335 DBREF 5UNH B 1001 1106 UNP P0ABE7 C562_ECOLX 23 128 DBREF 5UNH B 35 335 UNP P50052 AGTR2_HUMAN 35 335 SEQADV 5UNH TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION SEQADV 5UNH ILE A 1102 UNP P0ABE7 HIS 124 ENGINEERED MUTATION SEQADV 5UNH LEU A 1106 UNP P0ABE7 ARG 128 ENGINEERED MUTATION SEQADV 5UNH GLY A 1107 UNP P0ABE7 LINKER SEQADV 5UNH SER A 1108 UNP P0ABE7 LINKER SEQADV 5UNH GLY A 1109 UNP P0ABE7 LINKER SEQADV 5UNH SER A 1110 UNP P0ABE7 LINKER SEQADV 5UNH TRP B 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION SEQADV 5UNH ILE B 1102 UNP P0ABE7 HIS 124 ENGINEERED MUTATION SEQADV 5UNH LEU B 1106 UNP P0ABE7 ARG 128 ENGINEERED MUTATION SEQADV 5UNH GLY B 1107 UNP P0ABE7 LINKER SEQADV 5UNH SER B 1108 UNP P0ABE7 LINKER SEQADV 5UNH GLY B 1109 UNP P0ABE7 LINKER SEQADV 5UNH SER B 1110 UNP P0ABE7 LINKER SEQRES 1 A 411 ALA ASP LEU GLU ASP ASN TRP GLU THR LEU ASN ASP ASN SEQRES 2 A 411 LEU LYS VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL SEQRES 3 A 411 LYS ASP ALA LEU THR LYS MET ARG ALA ALA ALA LEU ASP SEQRES 4 A 411 ALA GLN LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SER SEQRES 5 A 411 PRO ASP SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE SEQRES 6 A 411 ASP ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU SEQRES 7 A 411 ALA ASN GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA SEQRES 8 A 411 GLU GLN LEU LYS THR THR ARG ASN ALA TYR ILE GLN LYS SEQRES 9 A 411 TYR LEU GLY SER GLY SER CYS SER GLN LYS PRO SER ASP SEQRES 10 A 411 LYS HIS LEU ASP ALA ILE PRO ILE LEU TYR TYR ILE ILE SEQRES 11 A 411 PHE VAL ILE GLY PHE LEU VAL ASN ILE VAL VAL VAL THR SEQRES 12 A 411 LEU PHE CYS CYS GLN LYS GLY PRO LYS LYS VAL SER SER SEQRES 13 A 411 ILE TYR ILE PHE ASN LEU ALA VAL ALA ASP LEU LEU LEU SEQRES 14 A 411 LEU ALA THR LEU PRO LEU TRP ALA THR TYR TYR SER TYR SEQRES 15 A 411 ARG TYR ASP TRP LEU PHE GLY PRO VAL MET CYS LYS VAL SEQRES 16 A 411 PHE GLY SER PHE LEU THR LEU ASN MET PHE ALA SER ILE SEQRES 17 A 411 PHE PHE ILE THR CYS MET SER VAL ASP ARG TYR GLN SER SEQRES 18 A 411 VAL ILE TYR PRO PHE LEU SER GLN ARG ARG ASN PRO TRP SEQRES 19 A 411 GLN ALA SER TYR ILE VAL PRO LEU VAL TRP CYS MET ALA SEQRES 20 A 411 CYS LEU SER SER LEU PRO THR PHE TYR PHE ARG ASP VAL SEQRES 21 A 411 ARG THR ILE GLU TYR LEU GLY VAL ASN ALA CYS ILE MET SEQRES 22 A 411 ALA PHE PRO PRO GLU LYS TYR ALA GLN TRP SER ALA GLY SEQRES 23 A 411 ILE ALA LEU MET LYS ASN ILE LEU GLY PHE ILE ILE PRO SEQRES 24 A 411 LEU ILE PHE ILE ALA THR CYS TYR PHE GLY ILE ARG LYS SEQRES 25 A 411 HIS LEU LEU LYS THR ASN SER TYR GLY LYS ASN ARG ILE SEQRES 26 A 411 THR ARG ASP GLN VAL LEU LYS MET ALA ALA ALA VAL VAL SEQRES 27 A 411 LEU ALA PHE ILE ILE CYS TRP LEU PRO PHE HIS VAL LEU SEQRES 28 A 411 THR PHE LEU ASP ALA LEU ALA TRP MET GLY VAL ILE ASN SEQRES 29 A 411 SER CYS GLU VAL ILE ALA VAL ILE ASP LEU ALA LEU PRO SEQRES 30 A 411 PHE ALA ILE LEU LEU GLY PHE THR ASN SER CYS VAL ASN SEQRES 31 A 411 PRO PHE LEU TYR CYS PHE VAL GLY ASN ARG PHE GLN GLN SEQRES 32 A 411 LYS LEU ARG SER VAL PHE ARG VAL SEQRES 1 B 411 ALA ASP LEU GLU ASP ASN TRP GLU THR LEU ASN ASP ASN SEQRES 2 B 411 LEU LYS VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL SEQRES 3 B 411 LYS ASP ALA LEU THR LYS MET ARG ALA ALA ALA LEU ASP SEQRES 4 B 411 ALA GLN LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SER SEQRES 5 B 411 PRO ASP SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE SEQRES 6 B 411 ASP ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU SEQRES 7 B 411 ALA ASN GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA SEQRES 8 B 411 GLU GLN LEU LYS THR THR ARG ASN ALA TYR ILE GLN LYS SEQRES 9 B 411 TYR LEU GLY SER GLY SER CYS SER GLN LYS PRO SER ASP SEQRES 10 B 411 LYS HIS LEU ASP ALA ILE PRO ILE LEU TYR TYR ILE ILE SEQRES 11 B 411 PHE VAL ILE GLY PHE LEU VAL ASN ILE VAL VAL VAL THR SEQRES 12 B 411 LEU PHE CYS CYS GLN LYS GLY PRO LYS LYS VAL SER SER SEQRES 13 B 411 ILE TYR ILE PHE ASN LEU ALA VAL ALA ASP LEU LEU LEU SEQRES 14 B 411 LEU ALA THR LEU PRO LEU TRP ALA THR TYR TYR SER TYR SEQRES 15 B 411 ARG TYR ASP TRP LEU PHE GLY PRO VAL MET CYS LYS VAL SEQRES 16 B 411 PHE GLY SER PHE LEU THR LEU ASN MET PHE ALA SER ILE SEQRES 17 B 411 PHE PHE ILE THR CYS MET SER VAL ASP ARG TYR GLN SER SEQRES 18 B 411 VAL ILE TYR PRO PHE LEU SER GLN ARG ARG ASN PRO TRP SEQRES 19 B 411 GLN ALA SER TYR ILE VAL PRO LEU VAL TRP CYS MET ALA SEQRES 20 B 411 CYS LEU SER SER LEU PRO THR PHE TYR PHE ARG ASP VAL SEQRES 21 B 411 ARG THR ILE GLU TYR LEU GLY VAL ASN ALA CYS ILE MET SEQRES 22 B 411 ALA PHE PRO PRO GLU LYS TYR ALA GLN TRP SER ALA GLY SEQRES 23 B 411 ILE ALA LEU MET LYS ASN ILE LEU GLY PHE ILE ILE PRO SEQRES 24 B 411 LEU ILE PHE ILE ALA THR CYS TYR PHE GLY ILE ARG LYS SEQRES 25 B 411 HIS LEU LEU LYS THR ASN SER TYR GLY LYS ASN ARG ILE SEQRES 26 B 411 THR ARG ASP GLN VAL LEU LYS MET ALA ALA ALA VAL VAL SEQRES 27 B 411 LEU ALA PHE ILE ILE CYS TRP LEU PRO PHE HIS VAL LEU SEQRES 28 B 411 THR PHE LEU ASP ALA LEU ALA TRP MET GLY VAL ILE ASN SEQRES 29 B 411 SER CYS GLU VAL ILE ALA VAL ILE ASP LEU ALA LEU PRO SEQRES 30 B 411 PHE ALA ILE LEU LEU GLY PHE THR ASN SER CYS VAL ASN SEQRES 31 B 411 PRO PHE LEU TYR CYS PHE VAL GLY ASN ARG PHE GLN GLN SEQRES 32 B 411 LYS LEU ARG SER VAL PHE ARG VAL HET 8EM A1501 47 HET 8EM B1501 47 HETNAM 8EM N-[(FURAN-2-YL)METHYL]-N-(4-OXO-2-PROPYL-3-{[2'-(2H- HETNAM 2 8EM TETRAZOL-5-YL)[1,1'-BIPHENYL]-4-YL]METHYL}-3,4- HETNAM 3 8EM DIHYDROQUINAZOLIN-6-YL)BENZAMIDE FORMUL 3 8EM 2(C37 H31 N7 O3) HELIX 1 AA1 LEU A 1003 ALA A 1020 1 18 HELIX 2 AA2 ASN A 1022 LYS A 1042 1 21 HELIX 3 AA3 SER A 1055 GLU A 1081 1 27 HELIX 4 AA4 LYS A 1083 LEU A 1106 1 24 HELIX 5 AA5 PRO A 39 HIS A 43 5 5 HELIX 6 AA6 ASP A 45 LYS A 73 1 29 HELIX 7 AA7 VAL A 78 ALA A 95 1 18 HELIX 8 AA8 THR A 96 TYR A 104 1 9 HELIX 9 AA9 SER A 105 ARG A 107 5 3 HELIX 10 AB1 GLY A 113 TYR A 148 1 36 HELIX 11 AB2 TYR A 162 SER A 175 1 14 HELIX 12 AB3 SER A 175 PHE A 181 1 7 HELIX 13 AB4 PRO A 200 GLU A 202 5 3 HELIX 14 AB5 LYS A 203 PHE A 220 1 18 HELIX 15 AB6 PHE A 220 LEU A 239 1 20 HELIX 16 AB7 LYS A 246 GLY A 285 1 40 HELIX 17 AB8 SER A 289 TYR A 318 1 30 HELIX 18 AB9 VAL A 321 PHE A 333 1 13 HELIX 19 AC1 LEU B 1003 ALA B 1020 1 18 HELIX 20 AC2 ASN B 1022 GLN B 1041 1 20 HELIX 21 AC3 PRO B 1056 GLU B 1081 1 26 HELIX 22 AC4 LYS B 1083 TYR B 1101 1 19 HELIX 23 AC5 ASP B 45 CYS B 70 1 26 HELIX 24 AC6 VAL B 78 ALA B 95 1 18 HELIX 25 AC7 THR B 96 TYR B 106 1 11 HELIX 26 AC8 GLY B 113 TYR B 148 1 36 HELIX 27 AC9 TYR B 162 SER B 175 1 14 HELIX 28 AD1 SER B 175 PHE B 181 1 7 HELIX 29 AD2 ALA B 205 PHE B 220 1 16 HELIX 30 AD3 PHE B 220 LYS B 240 1 21 HELIX 31 AD4 GLY B 245 GLY B 285 1 41 HELIX 32 AD5 SER B 289 TYR B 318 1 30 HELIX 33 AD6 VAL B 321 ARG B 330 1 10 SHEET 1 AA1 2 ARG A 182 ILE A 187 0 SHEET 2 AA1 2 VAL A 192 MET A 197 -1 O ALA A 194 N ARG A 185 SHEET 1 AA2 2 ARG B 182 ILE B 187 0 SHEET 2 AA2 2 VAL B 192 MET B 197 -1 O ALA B 194 N ARG B 185 SSBOND 1 CYS A 117 CYS A 195 1555 1555 2.04 SSBOND 2 CYS B 117 CYS B 195 1555 1555 2.04 SITE 1 AC1 14 TRP A 100 TYR A 103 LEU A 124 THR A 125 SITE 2 AC1 14 MET A 128 PHE A 129 THR A 178 ARG A 182 SITE 3 AC1 14 CYS A 195 LYS A 215 TRP A 269 PHE A 272 SITE 4 AC1 14 GLY A 307 PHE A 308 SITE 1 AC2 14 TRP B 100 TYR B 103 LEU B 124 THR B 125 SITE 2 AC2 14 MET B 128 PHE B 129 THR B 178 ARG B 182 SITE 3 AC2 14 CYS B 195 MET B 197 TRP B 269 PHE B 272 SITE 4 AC2 14 ILE B 304 GLY B 307 CRYST1 78.420 68.200 89.060 90.00 104.32 90.00 P 1 21 1 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.012752 0.000000 0.003255 0.00000 SCALE2 0.000000 0.014663 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011588 0.00000 ATOM 1 N ALA A1001 85.384 -44.863 -2.363 1.00118.12 N ANISOU 1 N ALA A1001 12478 11002 21400 -710 2891 2534 N ATOM 2 CA ALA A1001 84.440 -45.677 -3.128 1.00114.75 C ANISOU 2 CA ALA A1001 12377 11060 20162 -266 2688 2810 C ATOM 3 C ALA A1001 85.192 -46.646 -4.075 1.00117.94 C ANISOU 3 C ALA A1001 12736 11981 20096 -184 2865 2941 C ATOM 4 O ALA A1001 84.825 -46.801 -5.246 1.00120.03 O ANISOU 4 O ALA A1001 13266 12531 19808 111 3030 3386 O ATOM 5 CB ALA A1001 83.489 -44.773 -3.911 1.00119.16 C ANISOU 5 CB ALA A1001 13281 11374 20620 40 2892 3436 C ATOM 6 N ASP A1002 86.226 -47.318 -3.545 1.00111.82 N ANISOU 6 N ASP A1002 11608 11380 19496 -398 2816 2526 N ATOM 7 CA ASP A1002 87.087 -48.196 -4.331 1.00112.68 C ANISOU 7 CA ASP A1002 11614 11914 19284 -310 3051 2586 C ATOM 8 C ASP A1002 86.996 -49.685 -3.901 1.00109.37 C ANISOU 8 C ASP A1002 11174 11911 18472 -136 2643 2133 C ATOM 9 O ASP A1002 87.959 -50.439 -4.101 1.00111.16 O ANISOU 9 O ASP A1002 11177 12396 18663 -104 2804 2010 O ATOM 10 CB ASP A1002 88.534 -47.676 -4.213 1.00119.96 C ANISOU 10 CB ASP A1002 12063 12670 20847 -671 3466 2580 C ATOM 11 CG ASP A1002 89.546 -48.292 -5.156 1.00139.66 C ANISOU 11 CG ASP A1002 14395 15551 23119 -579 3891 2756 C ATOM 12 OD1 ASP A1002 89.416 -48.087 -6.385 1.00145.47 O ANISOU 12 OD1 ASP A1002 15406 16396 23469 -386 4303 3268 O ATOM 13 OD2 ASP A1002 90.489 -48.954 -4.663 1.00146.89 O ANISOU 13 OD2 ASP A1002 14884 16702 24224 -660 3832 2402 O ATOM 14 N LEU A1003 85.828 -50.122 -3.371 1.00 97.44 N ANISOU 14 N LEU A1003 9891 10440 16691 4 2179 1930 N ATOM 15 CA LEU A1003 85.571 -51.493 -2.900 1.00 91.64 C ANISOU 15 CA LEU A1003 9185 9966 15667 149 1833 1561 C ATOM 16 C LEU A1003 86.376 -51.781 -1.615 1.00 92.08 C ANISOU 16 C LEU A1003 8848 10009 16130 15 1658 1223 C ATOM 17 O LEU A1003 85.760 -52.053 -0.587 1.00 89.45 O ANISOU 17 O LEU A1003 8526 9662 15799 31 1287 998 O ATOM 18 CB LEU A1003 85.832 -52.566 -3.984 1.00 92.76 C ANISOU 18 CB LEU A1003 9482 10436 15328 368 2019 1558 C ATOM 19 CG LEU A1003 85.646 -54.017 -3.553 1.00 94.59 C ANISOU 19 CG LEU A1003 9766 10787 15389 508 1763 1182 C ATOM 20 CD1 LEU A1003 84.698 -54.722 -4.455 1.00 94.65 C ANISOU 20 CD1 LEU A1003 10142 10982 14837 659 1683 1096 C ATOM 21 CD2 LEU A1003 86.976 -54.751 -3.511 1.00100.26 C ANISOU 21 CD2 LEU A1003 10209 11603 16282 596 2003 1054 C ATOM 22 N GLU A1004 87.731 -51.751 -1.682 1.00 89.19 N ANISOU 22 N GLU A1004 8103 9727 16058 -86 1926 1206 N ATOM 23 CA GLU A1004 88.650 -51.956 -0.551 1.00 88.37 C ANISOU 23 CA GLU A1004 7515 9753 16307 -184 1751 910 C ATOM 24 C GLU A1004 88.399 -50.882 0.523 1.00 89.80 C ANISOU 24 C GLU A1004 7543 9723 16855 -474 1511 704 C ATOM 25 O GLU A1004 88.361 -51.193 1.717 1.00 86.48 O ANISOU 25 O GLU A1004 6947 9472 16439 -449 1133 402 O ATOM 26 CB GLU A1004 90.116 -51.912 -1.046 1.00 94.57 C ANISOU 26 CB GLU A1004 7853 10704 17375 -266 2146 978 C ATOM 27 CG GLU A1004 91.165 -52.157 0.035 1.00107.93 C ANISOU 27 CG GLU A1004 8932 12677 19400 -326 1940 681 C ATOM 28 CD GLU A1004 92.583 -51.679 -0.237 1.00139.00 C ANISOU 28 CD GLU A1004 12252 16760 23801 -564 2293 695 C ATOM 29 OE1 GLU A1004 93.528 -52.349 0.241 1.00144.77 O ANISOU 29 OE1 GLU A1004 12480 17894 24632 -413 2196 542 O ATOM 30 OE2 GLU A1004 92.755 -50.621 -0.886 1.00135.33 O ANISOU 30 OE2 GLU A1004 11767 16012 23639 -893 2679 886 O ATOM 31 N ASP A1005 88.211 -49.623 0.065 1.00 88.87 N ANISOU 31 N ASP A1005 7520 9225 17023 -712 1770 884 N ATOM 32 CA ASP A1005 87.934 -48.427 0.860 1.00 90.02 C ANISOU 32 CA ASP A1005 7595 9009 17601 -1003 1672 674 C ATOM 33 C ASP A1005 86.523 -48.475 1.410 1.00 88.93 C ANISOU 33 C ASP A1005 7830 8795 17165 -807 1329 598 C ATOM 34 O ASP A1005 86.260 -47.913 2.475 1.00 87.46 O ANISOU 34 O ASP A1005 7551 8488 17191 -944 1102 243 O ATOM 35 CB ASP A1005 88.133 -47.165 0.006 1.00 97.10 C ANISOU 35 CB ASP A1005 8551 9410 18933 -1245 2178 1015 C ATOM 36 CG ASP A1005 89.547 -46.967 -0.523 1.00113.56 C ANISOU 36 CG ASP A1005 10198 11536 21414 -1514 2611 1116 C ATOM 37 OD1 ASP A1005 90.508 -47.400 0.157 1.00115.11 O ANISOU 37 OD1 ASP A1005 9879 12075 21783 -1654 2441 736 O ATOM 38 OD2 ASP A1005 89.696 -46.339 -1.587 1.00124.06 O ANISOU 38 OD2 ASP A1005 11661 12587 22888 -1573 3132 1604 O ATOM 39 N ASN A1006 85.616 -49.147 0.675 1.00 84.00 N ANISOU 39 N ASN A1006 7593 8283 16041 -498 1300 886 N ATOM 40 CA ASN A1006 84.225 -49.374 1.072 1.00 80.76 C ANISOU 40 CA ASN A1006 7476 7889 15319 -299 993 852 C ATOM 41 C ASN A1006 84.142 -50.486 2.118 1.00 83.28 C ANISOU 41 C ASN A1006 7688 8539 15416 -193 633 548 C ATOM 42 O ASN A1006 83.295 -50.416 3.007 1.00 80.51 O ANISOU 42 O ASN A1006 7402 8198 14992 -142 382 385 O ATOM 43 CB ASN A1006 83.357 -49.717 -0.132 1.00 78.85 C ANISOU 43 CB ASN A1006 7590 7733 14636 -59 1071 1216 C ATOM 44 CG ASN A1006 82.883 -48.520 -0.907 1.00 97.67 C ANISOU 44 CG ASN A1006 10163 9816 17130 -21 1323 1611 C ATOM 45 OD1 ASN A1006 83.212 -48.363 -2.085 1.00 96.58 O ANISOU 45 OD1 ASN A1006 10130 9720 16847 47 1642 1989 O ATOM 46 ND2 ASN A1006 82.059 -47.685 -0.282 1.00 87.64 N ANISOU 46 ND2 ASN A1006 8959 8262 16079 -1 1214 1570 N ATOM 47 N TRP A1007 85.025 -51.499 2.021 1.00 82.58 N ANISOU 47 N TRP A1007 7430 8716 15230 -118 657 516 N ATOM 48 CA TRP A1007 85.088 -52.592 2.984 1.00 82.28 C ANISOU 48 CA TRP A1007 7285 8958 15020 46 387 346 C ATOM 49 C TRP A1007 85.690 -52.103 4.295 1.00 89.34 C ANISOU 49 C TRP A1007 7804 10019 16124 -76 173 40 C ATOM 50 O TRP A1007 85.256 -52.552 5.357 1.00 88.52 O ANISOU 50 O TRP A1007 7692 10125 15816 61 -101 -80 O ATOM 51 CB TRP A1007 85.854 -53.801 2.440 1.00 82.44 C ANISOU 51 CB TRP A1007 7252 9150 14923 240 527 436 C ATOM 52 CG TRP A1007 84.966 -54.808 1.773 1.00 82.14 C ANISOU 52 CG TRP A1007 7600 9050 14558 417 550 536 C ATOM 53 CD1 TRP A1007 84.925 -55.108 0.443 1.00 86.13 C ANISOU 53 CD1 TRP A1007 8327 9521 14879 468 794 634 C ATOM 54 CD2 TRP A1007 83.953 -55.613 2.399 1.00 80.05 C ANISOU 54 CD2 TRP A1007 7528 8774 14115 525 332 501 C ATOM 55 NE1 TRP A1007 83.956 -56.054 0.201 1.00 84.60 N ANISOU 55 NE1 TRP A1007 8432 9292 14421 565 696 575 N ATOM 56 CE2 TRP A1007 83.352 -56.391 1.385 1.00 84.20 C ANISOU 56 CE2 TRP A1007 8357 9213 14422 581 438 519 C ATOM 57 CE3 TRP A1007 83.487 -55.747 3.722 1.00 80.31 C ANISOU 57 CE3 TRP A1007 7491 8891 14134 569 83 449 C ATOM 58 CZ2 TRP A1007 82.312 -57.291 1.650 1.00 82.46 C ANISOU 58 CZ2 TRP A1007 8337 8914 14082 611 311 468 C ATOM 59 CZ3 TRP A1007 82.449 -56.627 3.981 1.00 80.43 C ANISOU 59 CZ3 TRP A1007 7725 8839 13994 646 5 497 C ATOM 60 CH2 TRP A1007 81.882 -57.395 2.955 1.00 81.16 C ANISOU 60 CH2 TRP A1007 8083 8773 13980 636 123 498 C ATOM 61 N GLU A1008 86.652 -51.149 4.227 1.00 89.59 N ANISOU 61 N GLU A1008 7510 9978 16552 -355 311 -103 N ATOM 62 CA GLU A1008 87.256 -50.522 5.407 1.00 92.47 C ANISOU 62 CA GLU A1008 7463 10530 17141 -560 85 -529 C ATOM 63 C GLU A1008 86.176 -49.812 6.214 1.00 93.49 C ANISOU 63 C GLU A1008 7810 10497 17216 -606 -101 -765 C ATOM 64 O GLU A1008 86.179 -49.917 7.433 1.00 93.44 O ANISOU 64 O GLU A1008 7626 10846 17031 -555 -415 -1092 O ATOM 65 CB GLU A1008 88.372 -49.535 5.020 1.00 99.37 C ANISOU 65 CB GLU A1008 7950 11240 18566 -957 335 -670 C ATOM 66 CG GLU A1008 89.770 -50.016 5.369 1.00121.33 C ANISOU 66 CG GLU A1008 10121 14523 21454 -983 244 -835 C ATOM 67 CD GLU A1008 90.134 -49.991 6.843 1.00163.50 C ANISOU 67 CD GLU A1008 15041 20378 26703 -1011 -223 -1327 C ATOM 68 OE1 GLU A1008 90.702 -48.972 7.298 1.00170.75 O ANISOU 68 OE1 GLU A1008 15567 21283 28026 -1441 -279 -1797 O ATOM 69 OE2 GLU A1008 89.876 -51.001 7.539 1.00164.48 O ANISOU 69 OE2 GLU A1008 15215 20934 26344 -607 -519 -1248 O ATOM 70 N THR A1009 85.222 -49.146 5.519 1.00 87.91 N ANISOU 70 N THR A1009 7484 9317 16601 -632 103 -565 N ATOM 71 CA THR A1009 84.079 -48.435 6.106 1.00 86.46 C ANISOU 71 CA THR A1009 7531 8914 16405 -603 10 -726 C ATOM 72 C THR A1009 83.131 -49.440 6.787 1.00 84.26 C ANISOU 72 C THR A1009 7412 8993 15609 -290 -254 -675 C ATOM 73 O THR A1009 82.722 -49.205 7.926 1.00 84.54 O ANISOU 73 O THR A1009 7402 9201 15520 -250 -449 -994 O ATOM 74 CB THR A1009 83.351 -47.600 5.031 1.00 93.15 C ANISOU 74 CB THR A1009 8706 9222 17465 -600 320 -381 C ATOM 75 OG1 THR A1009 84.311 -46.869 4.264 1.00 99.41 O ANISOU 75 OG1 THR A1009 9364 9686 18720 -869 659 -272 O ATOM 76 CG2 THR A1009 82.332 -46.640 5.625 1.00 90.94 C ANISOU 76 CG2 THR A1009 8596 8629 17328 -557 300 -574 C ATOM 77 N LEU A1010 82.809 -50.560 6.098 1.00 75.78 N ANISOU 77 N LEU A1010 6515 8028 14250 -88 -224 -304 N ATOM 78 CA LEU A1010 81.923 -51.612 6.609 1.00 71.95 C ANISOU 78 CA LEU A1010 6174 7784 13378 149 -389 -196 C ATOM 79 C LEU A1010 82.531 -52.323 7.815 1.00 76.15 C ANISOU 79 C LEU A1010 6467 8757 13711 270 -598 -339 C ATOM 80 O LEU A1010 81.803 -52.634 8.756 1.00 75.49 O ANISOU 80 O LEU A1010 6437 8887 13360 418 -732 -362 O ATOM 81 CB LEU A1010 81.585 -52.630 5.511 1.00 69.47 C ANISOU 81 CB LEU A1010 6078 7413 12906 255 -276 131 C ATOM 82 CG LEU A1010 80.548 -52.170 4.481 1.00 72.89 C ANISOU 82 CG LEU A1010 6764 7619 13314 249 -175 317 C ATOM 83 CD1 LEU A1010 80.841 -52.743 3.121 1.00 72.95 C ANISOU 83 CD1 LEU A1010 6900 7603 13216 266 -14 514 C ATOM 84 CD2 LEU A1010 79.143 -52.533 4.911 1.00 73.72 C ANISOU 84 CD2 LEU A1010 6983 7810 13218 352 -312 348 C ATOM 85 N ASN A1011 83.860 -52.546 7.802 1.00 74.19 N ANISOU 85 N ASN A1011 5921 8698 13572 241 -611 -399 N ATOM 86 CA ASN A1011 84.576 -53.209 8.893 1.00 76.01 C ANISOU 86 CA ASN A1011 5854 9446 13580 433 -835 -473 C ATOM 87 C ASN A1011 84.855 -52.246 10.053 1.00 83.71 C ANISOU 87 C ASN A1011 6546 10738 14523 297 -1079 -959 C ATOM 88 O ASN A1011 84.890 -52.691 11.202 1.00 85.08 O ANISOU 88 O ASN A1011 6582 11434 14311 525 -1317 -1020 O ATOM 89 CB ASN A1011 85.875 -53.849 8.394 1.00 76.93 C ANISOU 89 CB ASN A1011 5694 9708 13830 515 -760 -341 C ATOM 90 CG ASN A1011 85.655 -55.054 7.508 1.00 85.58 C ANISOU 90 CG ASN A1011 7068 10578 14871 734 -542 48 C ATOM 91 OD1 ASN A1011 84.907 -55.978 7.846 1.00 79.88 O ANISOU 91 OD1 ASN A1011 6588 9839 13925 956 -559 264 O ATOM 92 ND2 ASN A1011 86.317 -55.085 6.358 1.00 71.83 N ANISOU 92 ND2 ASN A1011 5293 8650 13349 662 -294 120 N ATOM 93 N ASP A1012 85.039 -50.939 9.759 1.00 82.56 N ANISOU 93 N ASP A1012 6326 10274 14771 -61 -995 -1307 N ATOM 94 CA ASP A1012 85.277 -49.903 10.771 1.00 87.32 C ANISOU 94 CA ASP A1012 6681 11060 15437 -274 -1189 -1921 C ATOM 95 C ASP A1012 84.042 -49.743 11.651 1.00 90.03 C ANISOU 95 C ASP A1012 7294 11487 15424 -97 -1281 -2053 C ATOM 96 O ASP A1012 84.156 -49.787 12.878 1.00 93.08 O ANISOU 96 O ASP A1012 7495 12449 15422 17 -1551 -2388 O ATOM 97 CB ASP A1012 85.648 -48.549 10.123 1.00 92.53 C ANISOU 97 CB ASP A1012 7273 11142 16743 -725 -959 -2214 C ATOM 98 CG ASP A1012 87.134 -48.208 10.080 1.00115.28 C ANISOU 98 CG ASP A1012 9608 14196 19997 -1058 -993 -2523 C ATOM 99 OD1 ASP A1012 87.940 -49.085 9.682 1.00116.76 O ANISOU 99 OD1 ASP A1012 9558 14693 20113 -924 -995 -2215 O ATOM 100 OD2 ASP A1012 87.485 -47.044 10.385 1.00127.87 O ANISOU 100 OD2 ASP A1012 10998 15565 22024 -1469 -974 -3084 O ATOM 101 N ASN A1013 82.858 -49.605 11.014 1.00 81.95 N ANISOU 101 N ASN A1013 6676 9980 14480 -35 -1056 -1766 N ATOM 102 CA ASN A1013 81.574 -49.428 11.685 1.00 80.43 C ANISOU 102 CA ASN A1013 6717 9821 14023 147 -1062 -1830 C ATOM 103 C ASN A1013 81.132 -50.697 12.414 1.00 81.94 C ANISOU 103 C ASN A1013 6944 10540 13648 485 -1182 -1516 C ATOM 104 O ASN A1013 80.388 -50.593 13.390 1.00 83.06 O ANISOU 104 O ASN A1013 7139 10968 13452 648 -1231 -1667 O ATOM 105 CB ASN A1013 80.514 -48.959 10.703 1.00 76.45 C ANISOU 105 CB ASN A1013 6532 8723 13793 145 -804 -1560 C ATOM 106 CG ASN A1013 80.673 -47.500 10.369 1.00 98.88 C ANISOU 106 CG ASN A1013 9389 11012 17168 -99 -634 -1882 C ATOM 107 OD1 ASN A1013 80.284 -46.620 11.139 1.00 97.09 O ANISOU 107 OD1 ASN A1013 9177 10694 17018 -113 -629 -2340 O ATOM 108 ND2 ASN A1013 81.300 -47.205 9.242 1.00 88.72 N ANISOU 108 ND2 ASN A1013 8101 9327 16282 -293 -445 -1661 N ATOM 109 N LEU A1014 81.611 -51.881 11.979 1.00 75.85 N ANISOU 109 N LEU A1014 6147 9879 12793 609 -1180 -1077 N ATOM 110 CA LEU A1014 81.310 -53.149 12.651 1.00 75.16 C ANISOU 110 CA LEU A1014 6102 10185 12269 934 -1222 -699 C ATOM 111 C LEU A1014 81.886 -53.138 14.073 1.00 82.95 C ANISOU 111 C LEU A1014 6816 11901 12799 1123 -1484 -947 C ATOM 112 O LEU A1014 81.213 -53.571 15.008 1.00 83.70 O ANISOU 112 O LEU A1014 6992 12368 12443 1382 -1490 -791 O ATOM 113 CB LEU A1014 81.856 -54.345 11.860 1.00 73.52 C ANISOU 113 CB LEU A1014 5924 9839 12173 1036 -1123 -247 C ATOM 114 CG LEU A1014 80.866 -55.046 10.935 1.00 75.06 C ANISOU 114 CG LEU A1014 6444 9578 12499 1018 -892 114 C ATOM 115 CD1 LEU A1014 81.597 -55.858 9.889 1.00 74.57 C ANISOU 115 CD1 LEU A1014 6411 9271 12651 1029 -767 332 C ATOM 116 CD2 LEU A1014 79.902 -55.937 11.713 1.00 78.17 C ANISOU 116 CD2 LEU A1014 6969 10123 12609 1224 -822 427 C ATOM 117 N LYS A1015 83.115 -52.590 14.228 1.00 82.04 N ANISOU 117 N LYS A1015 6345 12041 12786 978 -1695 -1354 N ATOM 118 CA LYS A1015 83.822 -52.436 15.504 1.00 86.91 C ANISOU 118 CA LYS A1015 6603 13472 12947 1111 -2033 -1727 C ATOM 119 C LYS A1015 83.080 -51.432 16.384 1.00 91.78 C ANISOU 119 C LYS A1015 7300 14245 13328 1032 -2092 -2300 C ATOM 120 O LYS A1015 82.967 -51.642 17.594 1.00 94.76 O ANISOU 120 O LYS A1015 7589 15361 13057 1315 -2276 -2408 O ATOM 121 CB LYS A1015 85.277 -51.975 15.277 1.00 92.57 C ANISOU 121 CB LYS A1015 6842 14365 13965 861 -2234 -2117 C ATOM 122 CG LYS A1015 86.109 -52.889 14.375 1.00102.96 C ANISOU 122 CG LYS A1015 8029 15547 15544 968 -2131 -1610 C ATOM 123 CD LYS A1015 87.564 -52.436 14.311 1.00114.98 C ANISOU 123 CD LYS A1015 8961 17396 17331 741 -2333 -2005 C ATOM 124 CE LYS A1015 88.323 -53.048 13.161 1.00116.24 C ANISOU 124 CE LYS A1015 9014 17251 17901 763 -2107 -1592 C ATOM 125 NZ LYS A1015 89.730 -52.567 13.145 1.00126.46 N ANISOU 125 NZ LYS A1015 9640 18922 19487 520 -2277 -1982 N ATOM 126 N VAL A1016 82.558 -50.354 15.756 1.00 86.50 N ANISOU 126 N VAL A1016 6816 12883 13168 701 -1897 -2630 N ATOM 127 CA VAL A1016 81.797 -49.271 16.388 1.00 89.09 C ANISOU 127 CA VAL A1016 7265 13135 13450 623 -1854 -3213 C ATOM 128 C VAL A1016 80.520 -49.848 17.031 1.00 92.49 C ANISOU 128 C VAL A1016 7956 13831 13354 1004 -1725 -2864 C ATOM 129 O VAL A1016 80.230 -49.508 18.178 1.00 97.15 O ANISOU 129 O VAL A1016 8506 14956 13449 1160 -1817 -3285 O ATOM 130 CB VAL A1016 81.480 -48.121 15.383 1.00 91.12 C ANISOU 130 CB VAL A1016 7703 12450 14469 279 -1584 -3423 C ATOM 131 CG1 VAL A1016 80.569 -47.060 15.996 1.00 93.94 C ANISOU 131 CG1 VAL A1016 8232 12618 14842 293 -1463 -3964 C ATOM 132 CG2 VAL A1016 82.758 -47.478 14.853 1.00 93.56 C ANISOU 132 CG2 VAL A1016 7720 12499 15329 -144 -1639 -3776 C ATOM 133 N ILE A1017 79.797 -50.746 16.316 1.00 83.48 N ANISOU 133 N ILE A1017 7044 12369 12304 1137 -1501 -2132 N ATOM 134 CA ILE A1017 78.559 -51.380 16.795 1.00 82.36 C ANISOU 134 CA ILE A1017 7095 12407 11793 1424 -1313 -1725 C ATOM 135 C ILE A1017 78.845 -52.196 18.078 1.00 93.39 C ANISOU 135 C ILE A1017 8365 14683 12438 1778 -1451 -1549 C ATOM 136 O ILE A1017 78.057 -52.125 19.024 1.00 96.07 O ANISOU 136 O ILE A1017 8763 15439 12301 2002 -1353 -1603 O ATOM 137 CB ILE A1017 77.865 -52.229 15.678 1.00 79.02 C ANISOU 137 CB ILE A1017 6870 11453 11702 1394 -1080 -1059 C ATOM 138 CG1 ILE A1017 77.339 -51.314 14.546 1.00 75.92 C ANISOU 138 CG1 ILE A1017 6605 10362 11880 1155 -945 -1199 C ATOM 139 CG2 ILE A1017 76.710 -53.082 16.238 1.00 79.33 C ANISOU 139 CG2 ILE A1017 7015 11721 11407 1632 -870 -595 C ATOM 140 CD1 ILE A1017 77.218 -51.959 13.166 1.00 73.60 C ANISOU 140 CD1 ILE A1017 6428 9600 11936 1034 -842 -735 C ATOM 141 N GLU A1018 79.982 -52.911 18.126 1.00 93.49 N ANISOU 141 N GLU A1018 8182 15021 12319 1875 -1659 -1329 N ATOM 142 CA GLU A1018 80.377 -53.717 19.284 1.00 99.87 C ANISOU 142 CA GLU A1018 8844 16708 12392 2297 -1808 -1045 C ATOM 143 C GLU A1018 80.725 -52.861 20.512 1.00113.12 C ANISOU 143 C GLU A1018 10297 19221 13463 2378 -2108 -1779 C ATOM 144 O GLU A1018 80.421 -53.269 21.635 1.00117.45 O ANISOU 144 O GLU A1018 10845 20538 13243 2773 -2117 -1592 O ATOM 145 CB GLU A1018 81.564 -54.622 18.934 1.00101.79 C ANISOU 145 CB GLU A1018 8890 17065 12723 2432 -1959 -631 C ATOM 146 CG GLU A1018 81.148 -55.995 18.436 1.00112.30 C ANISOU 146 CG GLU A1018 10462 17984 14224 2636 -1641 257 C ATOM 147 CD GLU A1018 80.808 -56.063 16.961 1.00137.60 C ANISOU 147 CD GLU A1018 13877 20227 18179 2284 -1410 351 C ATOM 148 OE1 GLU A1018 81.730 -56.324 16.154 1.00140.02 O ANISOU 148 OE1 GLU A1018 14077 20281 18845 2210 -1463 401 O ATOM 149 OE2 GLU A1018 79.622 -55.857 16.609 1.00131.57 O ANISOU 149 OE2 GLU A1018 13352 19034 17604 2110 -1178 370 O ATOM 150 N LYS A1019 81.352 -51.686 20.301 1.00112.82 N ANISOU 150 N LYS A1019 10069 19035 13763 1997 -2324 -2622 N ATOM 151 CA LYS A1019 81.756 -50.775 21.378 1.00120.78 C ANISOU 151 CA LYS A1019 10835 20764 14294 1964 -2635 -3529 C ATOM 152 C LYS A1019 80.662 -49.731 21.711 1.00127.34 C ANISOU 152 C LYS A1019 11919 21318 15146 1865 -2407 -4123 C ATOM 153 O LYS A1019 80.836 -48.948 22.650 1.00134.21 O ANISOU 153 O LYS A1019 12653 22747 15596 1848 -2607 -4974 O ATOM 154 CB LYS A1019 83.083 -50.074 21.023 1.00126.01 C ANISOU 154 CB LYS A1019 11093 21385 15398 1544 -2964 -4195 C ATOM 155 CG LYS A1019 84.325 -50.955 21.181 1.00143.96 C ANISOU 155 CG LYS A1019 12943 24370 17387 1757 -3308 -3848 C ATOM 156 CD LYS A1019 84.858 -50.973 22.619 1.00162.29 C ANISOU 156 CD LYS A1019 14897 28042 18724 2070 -3765 -4272 C ATOM 157 CE LYS A1019 86.007 -51.937 22.791 1.00172.17 C ANISOU 157 CE LYS A1019 15705 30061 19652 2419 -4097 -3774 C ATOM 158 NZ LYS A1019 86.425 -52.049 24.213 1.00188.52 N ANISOU 158 NZ LYS A1019 17425 33589 20614 2840 -4559 -4054 N ATOM 159 N ALA A1020 79.535 -49.739 20.967 1.00118.86 N ANISOU 159 N ALA A1020 11185 19443 14535 1833 -1996 -3708 N ATOM 160 CA ALA A1020 78.414 -48.817 21.182 1.00120.22 C ANISOU 160 CA ALA A1020 11577 19297 14803 1827 -1721 -4144 C ATOM 161 C ALA A1020 77.592 -49.211 22.408 1.00128.92 C ANISOU 161 C ALA A1020 12751 21213 15021 2279 -1593 -4023 C ATOM 162 O ALA A1020 77.446 -50.402 22.700 1.00127.74 O ANISOU 162 O ALA A1020 12611 21516 14409 2587 -1535 -3226 O ATOM 163 CB ALA A1020 77.521 -48.779 19.954 1.00114.02 C ANISOU 163 CB ALA A1020 11037 17531 14753 1703 -1372 -3658 C ATOM 164 N ASP A1021 77.048 -48.205 23.113 1.00131.09 N ANISOU 164 N ASP A1021 13089 21629 15090 2331 -1491 -4802 N ATOM 165 CA ASP A1021 76.234 -48.404 24.313 1.00136.53 C ANISOU 165 CA ASP A1021 13842 23134 14897 2772 -1308 -4802 C ATOM 166 C ASP A1021 74.764 -48.016 24.079 1.00137.62 C ANISOU 166 C ASP A1021 14194 22733 15362 2882 -806 -4684 C ATOM 167 O ASP A1021 73.884 -48.559 24.753 1.00139.18 O ANISOU 167 O ASP A1021 14437 23458 14986 3246 -515 -4257 O ATOM 168 CB ASP A1021 76.815 -47.608 25.495 1.00148.66 C ANISOU 168 CB ASP A1021 15233 25502 15747 2826 -1599 -5901 C ATOM 169 CG ASP A1021 78.121 -48.166 26.034 1.00167.29 C ANISOU 169 CG ASP A1021 17284 28798 17481 2879 -2120 -5928 C ATOM 170 OD1 ASP A1021 79.159 -48.021 25.347 1.00166.64 O ANISOU 170 OD1 ASP A1021 16999 28348 17970 2501 -2426 -6100 O ATOM 171 OD2 ASP A1021 78.109 -48.724 27.153 1.00180.45 O ANISOU 171 OD2 ASP A1021 18882 31618 18064 3330 -2209 -5761 O ATOM 172 N ASN A1022 74.503 -47.083 23.137 1.00130.39 N ANISOU 172 N ASN A1022 13376 20807 15361 2601 -681 -5009 N ATOM 173 CA ASN A1022 73.154 -46.616 22.796 1.00128.37 C ANISOU 173 CA ASN A1022 13258 20009 15507 2742 -242 -4899 C ATOM 174 C ASN A1022 72.750 -47.042 21.374 1.00122.06 C ANISOU 174 C ASN A1022 12501 18398 15478 2568 -131 -4100 C ATOM 175 O ASN A1022 73.618 -47.278 20.531 1.00117.22 O ANISOU 175 O ASN A1022 11869 17406 15261 2269 -367 -3900 O ATOM 176 CB ASN A1022 73.024 -45.093 22.961 1.00135.86 C ANISOU 176 CB ASN A1022 14298 20488 16835 2690 -128 -5936 C ATOM 177 CG ASN A1022 74.145 -44.272 22.365 1.00166.80 C ANISOU 177 CG ASN A1022 18206 23752 21418 2237 -384 -6533 C ATOM 178 OD1 ASN A1022 75.287 -44.294 22.835 1.00166.56 O ANISOU 178 OD1 ASN A1022 18022 24186 21078 2027 -758 -7013 O ATOM 179 ND2 ASN A1022 73.825 -43.473 21.360 1.00157.79 N ANISOU 179 ND2 ASN A1022 17194 21555 21205 2093 -165 -6527 N ATOM 180 N ALA A1023 71.425 -47.150 21.124 1.00115.61 N ANISOU 180 N ALA A1023 11699 17400 14829 2769 228 -3673 N ATOM 181 CA ALA A1023 70.847 -47.549 19.834 1.00108.09 C ANISOU 181 CA ALA A1023 10736 15833 14501 2642 320 -2977 C ATOM 182 C ALA A1023 71.047 -46.472 18.761 1.00107.93 C ANISOU 182 C ALA A1023 10810 14919 15280 2460 286 -3254 C ATOM 183 O ALA A1023 71.063 -46.802 17.574 1.00101.97 O ANISOU 183 O ALA A1023 10063 13710 14971 2284 224 -2747 O ATOM 184 CB ALA A1023 69.368 -47.861 19.993 1.00109.50 C ANISOU 184 CB ALA A1023 10801 16199 14605 2908 689 -2557 C ATOM 185 N ALA A1024 71.206 -45.195 19.178 1.00108.60 N ANISOU 185 N ALA A1024 10979 14743 15540 2510 358 -4058 N ATOM 186 CA ALA A1024 71.465 -44.058 18.288 1.00108.36 C ANISOU 186 CA ALA A1024 11070 13786 16316 2355 409 -4332 C ATOM 187 C ALA A1024 72.865 -44.175 17.680 1.00109.42 C ANISOU 187 C ALA A1024 11211 13663 16702 1919 108 -4352 C ATOM 188 O ALA A1024 73.066 -43.784 16.530 1.00107.30 O ANISOU 188 O ALA A1024 11017 12681 17071 1753 150 -4092 O ATOM 189 CB ALA A1024 71.329 -42.750 19.047 1.00116.72 C ANISOU 189 CB ALA A1024 12227 14607 17513 2498 613 -5259 C ATOM 190 N GLN A1025 73.821 -44.738 18.455 1.00105.80 N ANISOU 190 N GLN A1025 10641 13858 15700 1778 -180 -4608 N ATOM 191 CA GLN A1025 75.199 -45.003 18.045 1.00103.46 C ANISOU 191 CA GLN A1025 10246 13523 15541 1407 -483 -4624 C ATOM 192 C GLN A1025 75.238 -46.136 17.020 1.00 99.34 C ANISOU 192 C GLN A1025 9716 12932 15098 1358 -537 -3704 C ATOM 193 O GLN A1025 75.996 -46.067 16.051 1.00 96.68 O ANISOU 193 O GLN A1025 9371 12143 15220 1084 -605 -3545 O ATOM 194 CB GLN A1025 76.051 -45.382 19.267 1.00109.17 C ANISOU 194 CB GLN A1025 10785 15156 15541 1401 -795 -5090 C ATOM 195 CG GLN A1025 77.050 -44.324 19.701 1.00134.22 C ANISOU 195 CG GLN A1025 13841 18239 18917 1082 -970 -6109 C ATOM 196 CD GLN A1025 78.116 -44.923 20.582 1.00156.93 C ANISOU 196 CD GLN A1025 16429 22101 21096 1042 -1398 -6378 C ATOM 197 OE1 GLN A1025 77.898 -45.208 21.764 1.00156.49 O ANISOU 197 OE1 GLN A1025 16321 22946 20193 1342 -1503 -6623 O ATOM 198 NE2 GLN A1025 79.295 -45.140 20.017 1.00148.14 N ANISOU 198 NE2 GLN A1025 15092 20906 20287 715 -1643 -6294 N ATOM 199 N VAL A1026 74.415 -47.180 17.250 1.00 92.64 N ANISOU 199 N VAL A1026 8862 12522 13814 1609 -466 -3131 N ATOM 200 CA VAL A1026 74.294 -48.383 16.419 1.00 86.32 C ANISOU 200 CA VAL A1026 8062 11686 13049 1570 -482 -2337 C ATOM 201 C VAL A1026 73.626 -48.034 15.074 1.00 86.99 C ANISOU 201 C VAL A1026 8238 11090 13722 1505 -333 -2011 C ATOM 202 O VAL A1026 74.139 -48.438 14.030 1.00 83.68 O ANISOU 202 O VAL A1026 7849 10386 13560 1316 -414 -1679 O ATOM 203 CB VAL A1026 73.536 -49.516 17.167 1.00 89.80 C ANISOU 203 CB VAL A1026 8457 12730 12934 1815 -378 -1882 C ATOM 204 CG1 VAL A1026 73.338 -50.741 16.282 1.00 84.71 C ANISOU 204 CG1 VAL A1026 7825 11916 12444 1718 -349 -1157 C ATOM 205 CG2 VAL A1026 74.258 -49.909 18.453 1.00 93.73 C ANISOU 205 CG2 VAL A1026 8872 13993 12751 1961 -534 -2078 C ATOM 206 N LYS A1027 72.505 -47.283 15.098 1.00 84.83 N ANISOU 206 N LYS A1027 7991 10620 13620 1710 -113 -2101 N ATOM 207 CA LYS A1027 71.777 -46.876 13.891 1.00 82.63 C ANISOU 207 CA LYS A1027 7754 9821 13823 1755 6 -1759 C ATOM 208 C LYS A1027 72.656 -46.003 12.978 1.00 86.18 C ANISOU 208 C LYS A1027 8329 9622 14795 1556 -14 -1878 C ATOM 209 O LYS A1027 72.564 -46.120 11.757 1.00 82.35 O ANISOU 209 O LYS A1027 7887 8844 14560 1509 -14 -1425 O ATOM 210 CB LYS A1027 70.482 -46.130 14.257 1.00 88.67 C ANISOU 210 CB LYS A1027 8469 10550 14670 2103 259 -1874 C ATOM 211 CG LYS A1027 69.467 -46.111 13.121 1.00103.30 C ANISOU 211 CG LYS A1027 10242 12178 16828 2245 329 -1346 C ATOM 212 CD LYS A1027 68.412 -45.036 13.286 1.00117.70 C ANISOU 212 CD LYS A1027 12012 13797 18912 2647 590 -1484 C ATOM 213 CE LYS A1027 67.789 -44.712 11.951 1.00126.38 C ANISOU 213 CE LYS A1027 13056 14575 20388 2805 593 -979 C ATOM 214 NZ LYS A1027 66.592 -43.844 12.080 1.00139.85 N ANISOU 214 NZ LYS A1027 14623 16187 22328 3298 847 -973 N ATOM 215 N ASP A1028 73.514 -45.150 13.580 1.00 87.42 N ANISOU 215 N ASP A1028 8523 9594 15097 1421 -17 -2503 N ATOM 216 CA ASP A1028 74.434 -44.244 12.889 1.00 89.40 C ANISOU 216 CA ASP A1028 8856 9190 15921 1162 37 -2683 C ATOM 217 C ASP A1028 75.498 -45.016 12.093 1.00 89.37 C ANISOU 217 C ASP A1028 8798 9242 15917 870 -135 -2338 C ATOM 218 O ASP A1028 75.802 -44.641 10.956 1.00 88.73 O ANISOU 218 O ASP A1028 8800 8657 16257 757 -17 -2033 O ATOM 219 CB ASP A1028 75.106 -43.305 13.898 1.00 97.84 C ANISOU 219 CB ASP A1028 9903 10152 17120 1004 48 -3562 C ATOM 220 CG ASP A1028 75.318 -41.907 13.363 1.00119.82 C ANISOU 220 CG ASP A1028 12827 12000 20701 881 327 -3817 C ATOM 221 OD1 ASP A1028 74.408 -41.061 13.535 1.00125.82 O ANISOU 221 OD1 ASP A1028 13720 12362 21723 1175 597 -3974 O ATOM 222 OD2 ASP A1028 76.388 -41.657 12.768 1.00127.55 O ANISOU 222 OD2 ASP A1028 13771 12613 22081 509 322 -3828 O ATOM 223 N ALA A1029 76.051 -46.095 12.688 1.00 82.83 N ANISOU 223 N ALA A1029 7832 9041 14600 804 -372 -2343 N ATOM 224 CA ALA A1029 77.054 -46.949 12.059 1.00 78.86 C ANISOU 224 CA ALA A1029 7250 8653 14062 606 -514 -2038 C ATOM 225 C ALA A1029 76.439 -47.795 10.944 1.00 76.60 C ANISOU 225 C ALA A1029 7067 8297 13739 697 -462 -1366 C ATOM 226 O ALA A1029 77.076 -47.973 9.907 1.00 74.41 O ANISOU 226 O ALA A1029 6817 7796 13661 549 -439 -1110 O ATOM 227 CB ALA A1029 77.709 -47.844 13.100 1.00 80.14 C ANISOU 227 CB ALA A1029 7232 9510 13708 628 -756 -2189 C ATOM 228 N LEU A1030 75.195 -48.288 11.148 1.00 71.13 N ANISOU 228 N LEU A1030 6405 7824 12798 922 -428 -1127 N ATOM 229 CA LEU A1030 74.459 -49.116 10.186 1.00 67.20 C ANISOU 229 CA LEU A1030 5947 7334 12251 966 -414 -610 C ATOM 230 C LEU A1030 74.049 -48.312 8.952 1.00 72.83 C ANISOU 230 C LEU A1030 6754 7618 13301 1009 -309 -394 C ATOM 231 O LEU A1030 74.007 -48.869 7.852 1.00 70.94 O ANISOU 231 O LEU A1030 6556 7363 13034 958 -344 -48 O ATOM 232 CB LEU A1030 73.223 -49.763 10.835 1.00 66.65 C ANISOU 232 CB LEU A1030 5795 7631 11898 1139 -381 -469 C ATOM 233 CG LEU A1030 73.489 -50.999 11.701 1.00 70.38 C ANISOU 233 CG LEU A1030 6211 8534 11997 1127 -433 -373 C ATOM 234 CD1 LEU A1030 72.369 -51.221 12.681 1.00 72.51 C ANISOU 234 CD1 LEU A1030 6381 9160 12010 1310 -303 -331 C ATOM 235 CD2 LEU A1030 73.692 -52.252 10.846 1.00 69.92 C ANISOU 235 CD2 LEU A1030 6191 8419 11957 982 -470 1 C ATOM 236 N THR A1031 73.773 -47.007 9.129 1.00 73.23 N ANISOU 236 N THR A1031 6849 7324 13651 1133 -162 -599 N ATOM 237 CA THR A1031 73.396 -46.099 8.040 1.00 75.13 C ANISOU 237 CA THR A1031 7192 7117 14235 1269 -10 -310 C ATOM 238 C THR A1031 74.621 -45.876 7.129 1.00 79.79 C ANISOU 238 C THR A1031 7882 7375 15061 1029 54 -183 C ATOM 239 O THR A1031 74.478 -45.886 5.898 1.00 78.83 O ANISOU 239 O THR A1031 7840 7163 14950 1101 104 273 O ATOM 240 CB THR A1031 72.819 -44.793 8.617 1.00 87.13 C ANISOU 240 CB THR A1031 8751 8268 16085 1507 198 -576 C ATOM 241 OG1 THR A1031 71.667 -45.117 9.396 1.00 87.82 O ANISOU 241 OG1 THR A1031 8703 8763 15902 1753 174 -645 O ATOM 242 CG2 THR A1031 72.432 -43.778 7.536 1.00 88.03 C ANISOU 242 CG2 THR A1031 8987 7854 16604 1742 410 -178 C ATOM 243 N LYS A1032 75.823 -45.711 7.744 1.00 77.89 N ANISOU 243 N LYS A1032 7591 7045 14959 750 49 -591 N ATOM 244 CA LYS A1032 77.100 -45.525 7.038 1.00 78.26 C ANISOU 244 CA LYS A1032 7637 6828 15269 472 144 -528 C ATOM 245 C LYS A1032 77.476 -46.810 6.285 1.00 78.36 C ANISOU 245 C LYS A1032 7627 7216 14929 421 20 -187 C ATOM 246 O LYS A1032 78.111 -46.743 5.232 1.00 78.98 O ANISOU 246 O LYS A1032 7755 7123 15131 325 162 93 O ATOM 247 CB LYS A1032 78.228 -45.114 8.009 1.00 82.43 C ANISOU 247 CB LYS A1032 7998 7310 16014 169 109 -1136 C ATOM 248 CG LYS A1032 78.052 -43.739 8.646 1.00 90.22 C ANISOU 248 CG LYS A1032 9028 7793 17457 134 287 -1610 C ATOM 249 CD LYS A1032 79.331 -43.266 9.324 1.00 99.93 C ANISOU 249 CD LYS A1032 10041 8946 18981 -280 250 -2255 C ATOM 250 CE LYS A1032 79.085 -42.201 10.363 1.00107.13 C ANISOU 250 CE LYS A1032 10968 9571 20167 -323 321 -2983 C ATOM 251 NZ LYS A1032 78.711 -42.786 11.679 1.00109.00 N ANISOU 251 NZ LYS A1032 11101 10543 19770 -154 19 -3421 N ATOM 252 N MET A1033 77.060 -47.969 6.824 1.00 71.05 N ANISOU 252 N MET A1033 6641 6769 13587 498 -191 -206 N ATOM 253 CA MET A1033 77.311 -49.276 6.233 1.00 68.23 C ANISOU 253 CA MET A1033 6288 6692 12946 466 -280 38 C ATOM 254 C MET A1033 76.433 -49.498 5.020 1.00 71.60 C ANISOU 254 C MET A1033 6841 7120 13245 587 -254 417 C ATOM 255 O MET A1033 76.951 -49.933 3.989 1.00 70.87 O ANISOU 255 O MET A1033 6815 7040 13072 528 -203 608 O ATOM 256 CB MET A1033 77.070 -50.395 7.254 1.00 69.04 C ANISOU 256 CB MET A1033 6304 7197 12730 518 -443 -61 C ATOM 257 CG MET A1033 78.205 -50.596 8.212 1.00 73.60 C ANISOU 257 CG MET A1033 6723 7975 13267 442 -532 -332 C ATOM 258 SD MET A1033 77.788 -51.825 9.464 1.00 76.80 S ANISOU 258 SD MET A1033 7067 8866 13248 614 -659 -289 S ATOM 259 CE MET A1033 78.201 -53.341 8.564 1.00 71.15 C ANISOU 259 CE MET A1033 6423 8125 12484 605 -619 76 C ATOM 260 N ARG A1034 75.100 -49.217 5.145 1.00 68.51 N ANISOU 260 N ARG A1034 6442 6792 12795 777 -296 498 N ATOM 261 CA ARG A1034 74.112 -49.405 4.074 1.00 68.27 C ANISOU 261 CA ARG A1034 6437 6913 12591 919 -350 816 C ATOM 262 C ARG A1034 74.509 -48.628 2.828 1.00 76.37 C ANISOU 262 C ARG A1034 7597 7719 13701 995 -204 1126 C ATOM 263 O ARG A1034 74.426 -49.180 1.731 1.00 76.86 O ANISOU 263 O ARG A1034 7710 8013 13478 1010 -261 1335 O ATOM 264 CB ARG A1034 72.697 -49.015 4.511 1.00 66.69 C ANISOU 264 CB ARG A1034 6110 6838 12390 1149 -398 848 C ATOM 265 CG ARG A1034 71.634 -49.685 3.649 1.00 73.07 C ANISOU 265 CG ARG A1034 6804 8029 12930 1214 -566 1064 C ATOM 266 CD ARG A1034 70.287 -48.988 3.664 1.00 77.25 C ANISOU 266 CD ARG A1034 7148 8698 13505 1529 -594 1220 C ATOM 267 NE ARG A1034 69.211 -49.906 3.269 1.00 76.19 N ANISOU 267 NE ARG A1034 6761 9062 13124 1481 -809 1263 N ATOM 268 CZ ARG A1034 68.715 -50.013 2.038 1.00 84.38 C ANISOU 268 CZ ARG A1034 7712 10423 13924 1569 -987 1471 C ATOM 269 NH1 ARG A1034 69.177 -49.248 1.058 1.00 70.89 N ANISOU 269 NH1 ARG A1034 6189 8601 12146 1777 -937 1764 N ATOM 270 NH2 ARG A1034 67.751 -50.885 1.780 1.00 69.26 N ANISOU 270 NH2 ARG A1034 5504 8983 11829 1440 -1208 1385 N ATOM 271 N ALA A1035 74.972 -47.371 3.001 1.00 75.55 N ANISOU 271 N ALA A1035 7557 7162 13985 1031 15 1137 N ATOM 272 CA ALA A1035 75.423 -46.521 1.905 1.00 78.86 C ANISOU 272 CA ALA A1035 8118 7275 14569 1104 261 1522 C ATOM 273 C ALA A1035 76.659 -47.124 1.225 1.00 81.85 C ANISOU 273 C ALA A1035 8532 7731 14834 868 348 1566 C ATOM 274 O ALA A1035 76.676 -47.236 -0.001 1.00 83.07 O ANISOU 274 O ALA A1035 8793 8045 14726 979 425 1940 O ATOM 275 CB ALA A1035 75.728 -45.126 2.421 1.00 83.58 C ANISOU 275 CB ALA A1035 8765 7244 15747 1105 536 1439 C ATOM 276 N ALA A1036 77.658 -47.564 2.031 1.00 76.38 N ANISOU 276 N ALA A1036 7724 7019 14278 590 323 1181 N ATOM 277 CA ALA A1036 78.913 -48.174 1.575 1.00 75.26 C ANISOU 277 CA ALA A1036 7536 6969 14090 394 420 1167 C ATOM 278 C ALA A1036 78.678 -49.504 0.847 1.00 77.62 C ANISOU 278 C ALA A1036 7900 7697 13894 467 282 1249 C ATOM 279 O ALA A1036 79.358 -49.771 -0.144 1.00 78.53 O ANISOU 279 O ALA A1036 8074 7893 13870 451 452 1418 O ATOM 280 CB ALA A1036 79.845 -48.386 2.754 1.00 74.87 C ANISOU 280 CB ALA A1036 7270 6922 14254 167 342 729 C ATOM 281 N ALA A1037 77.701 -50.309 1.314 1.00 72.10 N ANISOU 281 N ALA A1037 7187 7251 12957 534 20 1107 N ATOM 282 CA ALA A1037 77.341 -51.597 0.720 1.00 70.51 C ANISOU 282 CA ALA A1037 7041 7370 12381 540 -109 1076 C ATOM 283 C ALA A1037 76.681 -51.405 -0.653 1.00 77.59 C ANISOU 283 C ALA A1037 8053 8484 12943 690 -115 1343 C ATOM 284 O ALA A1037 76.946 -52.182 -1.569 1.00 78.18 O ANISOU 284 O ALA A1037 8217 8783 12705 670 -97 1309 O ATOM 285 CB ALA A1037 76.419 -52.357 1.651 1.00 69.02 C ANISOU 285 CB ALA A1037 6766 7319 12141 517 -324 884 C ATOM 286 N LEU A1038 75.847 -50.357 -0.799 1.00 77.06 N ANISOU 286 N LEU A1038 7980 8383 12915 886 -133 1603 N ATOM 287 CA LEU A1038 75.176 -50.015 -2.059 1.00 80.79 C ANISOU 287 CA LEU A1038 8523 9157 13018 1129 -167 1953 C ATOM 288 C LEU A1038 76.179 -49.452 -3.066 1.00 90.34 C ANISOU 288 C LEU A1038 9895 10266 14161 1194 158 2297 C ATOM 289 O LEU A1038 76.054 -49.698 -4.273 1.00 93.92 O ANISOU 289 O LEU A1038 10444 11130 14111 1340 151 2495 O ATOM 290 CB LEU A1038 74.047 -48.997 -1.821 1.00 82.37 C ANISOU 290 CB LEU A1038 8637 9314 13347 1411 -238 2208 C ATOM 291 CG LEU A1038 72.761 -49.529 -1.211 1.00 84.98 C ANISOU 291 CG LEU A1038 8746 9943 13601 1427 -548 1986 C ATOM 292 CD1 LEU A1038 72.030 -48.443 -0.486 1.00 86.23 C ANISOU 292 CD1 LEU A1038 8804 9863 14095 1679 -495 2126 C ATOM 293 CD2 LEU A1038 71.860 -50.147 -2.266 1.00 90.50 C ANISOU 293 CD2 LEU A1038 9336 11276 13773 1521 -829 2036 C ATOM 294 N ASP A1039 77.170 -48.694 -2.558 1.00 87.27 N ANISOU 294 N ASP A1039 9512 9374 14272 1068 454 2346 N ATOM 295 CA ASP A1039 78.228 -48.067 -3.340 1.00 90.64 C ANISOU 295 CA ASP A1039 10034 9604 14802 1054 860 2690 C ATOM 296 C ASP A1039 79.254 -49.113 -3.813 1.00 92.55 C ANISOU 296 C ASP A1039 10270 10096 14797 891 953 2490 C ATOM 297 O ASP A1039 79.901 -48.906 -4.844 1.00 96.59 O ANISOU 297 O ASP A1039 10875 10705 15120 958 1271 2813 O ATOM 298 CB ASP A1039 78.904 -46.949 -2.514 1.00 94.19 C ANISOU 298 CB ASP A1039 10410 9398 15979 877 1130 2679 C ATOM 299 CG ASP A1039 78.120 -45.633 -2.419 1.00113.36 C ANISOU 299 CG ASP A1039 12923 11418 18729 1110 1251 3017 C ATOM 300 OD1 ASP A1039 77.173 -45.434 -3.224 1.00117.01 O ANISOU 300 OD1 ASP A1039 13496 12145 18818 1487 1188 3454 O ATOM 301 OD2 ASP A1039 78.438 -44.815 -1.527 1.00122.68 O ANISOU 301 OD2 ASP A1039 14044 12038 20533 940 1399 2813 O ATOM 302 N ALA A1040 79.373 -50.249 -3.090 1.00 83.43 N ANISOU 302 N ALA A1040 9017 9053 13631 729 721 2003 N ATOM 303 CA ALA A1040 80.291 -51.343 -3.432 1.00 82.09 C ANISOU 303 CA ALA A1040 8837 9064 13290 640 816 1775 C ATOM 304 C ALA A1040 79.669 -52.337 -4.427 1.00 86.93 C ANISOU 304 C ALA A1040 9611 10134 13286 762 674 1660 C ATOM 305 O ALA A1040 80.415 -53.030 -5.121 1.00 87.69 O ANISOU 305 O ALA A1040 9770 10396 13151 773 862 1547 O ATOM 306 CB ALA A1040 80.735 -52.070 -2.177 1.00 79.01 C ANISOU 306 CB ALA A1040 8274 8535 13211 479 675 1382 C ATOM 307 N GLN A1041 78.316 -52.387 -4.516 1.00 84.08 N ANISOU 307 N GLN A1041 9279 10003 12665 850 353 1643 N ATOM 308 CA GLN A1041 77.584 -53.263 -5.438 1.00 86.38 C ANISOU 308 CA GLN A1041 9657 10787 12375 905 144 1433 C ATOM 309 C GLN A1041 77.818 -52.860 -6.904 1.00 96.75 C ANISOU 309 C GLN A1041 11127 12515 13120 1135 332 1750 C ATOM 310 O GLN A1041 77.844 -53.731 -7.774 1.00 98.96 O ANISOU 310 O GLN A1041 11511 13199 12891 1148 301 1455 O ATOM 311 CB GLN A1041 76.078 -53.260 -5.127 1.00 87.49 C ANISOU 311 CB GLN A1041 9674 11133 12435 924 -251 1364 C ATOM 312 CG GLN A1041 75.385 -54.585 -5.476 1.00105.51 C ANISOU 312 CG GLN A1041 11932 13755 14401 762 -522 855 C ATOM 313 CD GLN A1041 73.883 -54.475 -5.656 1.00125.40 C ANISOU 313 CD GLN A1041 14255 16711 16679 808 -909 835 C ATOM 314 OE1 GLN A1041 73.135 -54.161 -4.725 1.00116.39 O ANISOU 314 OE1 GLN A1041 12919 15424 15878 784 -1044 905 O ATOM 315 NE2 GLN A1041 73.399 -54.782 -6.854 1.00124.56 N ANISOU 315 NE2 GLN A1041 14152 17226 15947 879 -1104 693 N ATOM 316 N LYS A1042 77.988 -51.553 -7.174 1.00 97.06 N ANISOU 316 N LYS A1042 11195 12441 13242 1327 563 2344 N ATOM 317 CA LYS A1042 78.226 -51.037 -8.525 1.00103.44 C ANISOU 317 CA LYS A1042 12161 13642 13498 1605 819 2817 C ATOM 318 C LYS A1042 79.686 -51.231 -8.984 1.00110.15 C ANISOU 318 C LYS A1042 13082 14404 14366 1531 1308 2848 C ATOM 319 O LYS A1042 79.959 -51.161 -10.189 1.00115.20 O ANISOU 319 O LYS A1042 13869 15499 14401 1751 1550 3120 O ATOM 320 CB LYS A1042 77.853 -49.554 -8.596 1.00108.81 C ANISOU 320 CB LYS A1042 12858 14117 14367 1865 967 3536 C ATOM 321 CG LYS A1042 76.363 -49.295 -8.493 1.00121.59 C ANISOU 321 CG LYS A1042 14384 16016 15799 2094 529 3625 C ATOM 322 CD LYS A1042 76.103 -47.831 -8.260 1.00134.54 C ANISOU 322 CD LYS A1042 16038 17210 17870 2354 743 4284 C ATOM 323 CE LYS A1042 74.616 -47.574 -8.342 1.00147.61 C ANISOU 323 CE LYS A1042 17560 19273 19252 2700 332 4451 C ATOM 324 NZ LYS A1042 74.291 -46.174 -8.739 1.00160.34 N ANISOU 324 NZ LYS A1042 19255 20693 20973 3183 589 5306 N ATOM 325 N ALA A1043 80.611 -51.458 -8.024 1.00103.52 N ANISOU 325 N ALA A1043 12100 13058 14175 1256 1456 2591 N ATOM 326 CA ALA A1043 82.045 -51.646 -8.272 1.00104.92 C ANISOU 326 CA ALA A1043 12222 13137 14507 1171 1913 2591 C ATOM 327 C ALA A1043 82.364 -53.037 -8.845 1.00110.27 C ANISOU 327 C ALA A1043 12986 14188 14724 1211 1915 2091 C ATOM 328 O ALA A1043 81.610 -53.985 -8.630 1.00107.79 O ANISOU 328 O ALA A1043 12728 13993 14235 1168 1536 1609 O ATOM 329 CB ALA A1043 82.828 -51.421 -6.983 1.00101.83 C ANISOU 329 CB ALA A1043 11565 12187 14938 895 1973 2445 C ATOM 330 N THR A1044 83.499 -53.149 -9.560 1.00111.60 N ANISOU 330 N THR A1044 13150 14496 14757 1282 2397 2193 N ATOM 331 CA THR A1044 83.984 -54.398 -10.163 1.00114.06 C ANISOU 331 CA THR A1044 13553 15108 14679 1372 2528 1709 C ATOM 332 C THR A1044 85.198 -54.921 -9.362 1.00116.98 C ANISOU 332 C THR A1044 13658 15097 15693 1253 2748 1478 C ATOM 333 O THR A1044 86.130 -54.142 -9.132 1.00117.46 O ANISOU 333 O THR A1044 13469 14965 16196 1169 3086 1839 O ATOM 334 CB THR A1044 84.336 -54.193 -11.654 1.00129.78 C ANISOU 334 CB THR A1044 15722 17674 15914 1637 2946 1988 C ATOM 335 OG1 THR A1044 85.363 -53.205 -11.768 1.00132.54 O ANISOU 335 OG1 THR A1044 15903 17848 16609 1621 3491 2592 O ATOM 336 CG2 THR A1044 83.127 -53.798 -12.509 1.00131.83 C ANISOU 336 CG2 THR A1044 16214 18483 15391 1844 2669 2208 C ATOM 337 N PRO A1045 85.233 -56.223 -8.954 1.00112.65 N ANISOU 337 N PRO A1045 13130 14439 15234 1257 2590 904 N ATOM 338 CA PRO A1045 86.382 -56.728 -8.172 1.00111.59 C ANISOU 338 CA PRO A1045 12707 14007 15685 1248 2779 767 C ATOM 339 C PRO A1045 87.756 -56.426 -8.797 1.00121.96 C ANISOU 339 C PRO A1045 13804 15491 17044 1359 3367 1006 C ATOM 340 O PRO A1045 87.859 -56.389 -10.027 1.00126.13 O ANISOU 340 O PRO A1045 14524 16408 16992 1525 3696 1086 O ATOM 341 CB PRO A1045 86.128 -58.236 -8.111 1.00113.10 C ANISOU 341 CB PRO A1045 13078 14107 15788 1351 2654 182 C ATOM 342 CG PRO A1045 84.663 -58.359 -8.169 1.00115.81 C ANISOU 342 CG PRO A1045 13674 14507 15821 1226 2209 -4 C ATOM 343 CD PRO A1045 84.212 -57.279 -9.124 1.00114.01 C ANISOU 343 CD PRO A1045 13553 14712 15055 1260 2237 372 C ATOM 344 N PRO A1046 88.826 -56.224 -7.976 1.00119.70 N ANISOU 344 N PRO A1046 13078 14997 17405 1278 3512 1110 N ATOM 345 CA PRO A1046 90.149 -55.888 -8.550 1.00125.17 C ANISOU 345 CA PRO A1046 13457 15881 18220 1338 4103 1352 C ATOM 346 C PRO A1046 90.854 -57.057 -9.271 1.00135.00 C ANISOU 346 C PRO A1046 14739 17367 19188 1680 4482 1031 C ATOM 347 O PRO A1046 92.074 -57.022 -9.473 1.00138.82 O ANISOU 347 O PRO A1046 14841 17994 19909 1772 4954 1152 O ATOM 348 CB PRO A1046 90.948 -55.404 -7.335 1.00125.14 C ANISOU 348 CB PRO A1046 12904 15640 19005 1114 4017 1437 C ATOM 349 CG PRO A1046 90.317 -56.067 -6.170 1.00124.21 C ANISOU 349 CG PRO A1046 12840 15289 19065 1120 3455 1117 C ATOM 350 CD PRO A1046 88.862 -56.215 -6.496 1.00116.98 C ANISOU 350 CD PRO A1046 12453 14328 17667 1122 3139 1025 C ATOM 351 N LYS A1047 90.076 -58.066 -9.699 1.00132.67 N ANISOU 351 N LYS A1047 14884 17116 18410 1857 4307 588 N ATOM 352 CA LYS A1047 90.527 -59.239 -10.449 1.00137.72 C ANISOU 352 CA LYS A1047 15680 17909 18738 2192 4652 145 C ATOM 353 C LYS A1047 89.480 -59.634 -11.512 1.00146.15 C ANISOU 353 C LYS A1047 17293 19265 18972 2254 4545 -211 C ATOM 354 O LYS A1047 89.849 -60.246 -12.516 1.00151.85 O ANISOU 354 O LYS A1047 18194 20295 19206 2517 4939 -534 O ATOM 355 CB LYS A1047 90.838 -60.417 -9.511 1.00138.01 C ANISOU 355 CB LYS A1047 15599 17530 19309 2350 4520 -226 C ATOM 356 CG LYS A1047 92.214 -60.337 -8.860 1.00145.45 C ANISOU 356 CG LYS A1047 15942 18446 20875 2482 4786 13 C ATOM 357 CD LYS A1047 92.469 -61.527 -7.960 1.00151.74 C ANISOU 357 CD LYS A1047 16648 18876 22130 2750 4654 -253 C ATOM 358 CE LYS A1047 93.763 -61.404 -7.199 1.00161.53 C ANISOU 358 CE LYS A1047 17208 20210 23958 2908 4795 12 C ATOM 359 NZ LYS A1047 93.834 -62.383 -6.081 1.00168.29 N ANISOU 359 NZ LYS A1047 17965 20733 25244 3179 4535 -76 N ATOM 360 N LEU A1048 88.188 -59.258 -11.308 1.00140.37 N ANISOU 360 N LEU A1048 16782 18505 18049 2024 4014 -182 N ATOM 361 CA LEU A1048 87.097 -59.532 -12.257 1.00143.79 C ANISOU 361 CA LEU A1048 17631 19328 17677 2043 3796 -523 C ATOM 362 C LEU A1048 86.905 -58.349 -13.235 1.00152.35 C ANISOU 362 C LEU A1048 18790 20997 18098 2108 3946 39 C ATOM 363 O LEU A1048 85.805 -58.137 -13.755 1.00152.98 O ANISOU 363 O LEU A1048 19104 21450 17573 2093 3598 2 O ATOM 364 CB LEU A1048 85.771 -59.862 -11.528 1.00139.24 C ANISOU 364 CB LEU A1048 17176 18468 17261 1790 3150 -805 C ATOM 365 CG LEU A1048 85.637 -61.232 -10.831 1.00142.92 C ANISOU 365 CG LEU A1048 17710 18399 18193 1740 3016 -1415 C ATOM 366 CD1 LEU A1048 84.235 -61.421 -10.283 1.00139.83 C ANISOU 366 CD1 LEU A1048 17415 17836 17878 1448 2445 -1619 C ATOM 367 CD2 LEU A1048 85.938 -62.393 -11.778 1.00152.63 C ANISOU 367 CD2 LEU A1048 19207 19732 19054 1938 3335 -2114 C ATOM 368 N GLU A1049 87.999 -57.602 -13.495 1.00152.61 N ANISOU 368 N GLU A1049 18592 21128 18265 2200 4495 589 N ATOM 369 CA GLU A1049 88.055 -56.449 -14.403 1.00157.63 C ANISOU 369 CA GLU A1049 19278 22225 18391 2298 4820 1282 C ATOM 370 C GLU A1049 87.834 -56.893 -15.846 1.00170.20 C ANISOU 370 C GLU A1049 21222 24596 18851 2616 5024 1033 C ATOM 371 O GLU A1049 87.156 -56.207 -16.610 1.00173.58 O ANISOU 371 O GLU A1049 21851 25543 18558 2741 4948 1435 O ATOM 372 CB GLU A1049 89.418 -55.729 -14.294 1.00161.09 C ANISOU 372 CB GLU A1049 19322 22510 19375 2260 5457 1843 C ATOM 373 CG GLU A1049 89.836 -55.322 -12.888 1.00166.69 C ANISOU 373 CG GLU A1049 19608 22557 21170 1938 5282 1975 C ATOM 374 CD GLU A1049 91.321 -55.061 -12.708 1.00192.10 C ANISOU 374 CD GLU A1049 22321 25679 24989 1879 5857 2214 C ATOM 375 OE1 GLU A1049 91.669 -53.990 -12.161 1.00188.26 O ANISOU 375 OE1 GLU A1049 21510 24885 25133 1581 5947 2676 O ATOM 376 OE2 GLU A1049 92.137 -55.931 -13.092 1.00188.42 O ANISOU 376 OE2 GLU A1049 21748 25433 24409 2121 6224 1896 O ATOM 377 N ASP A1050 88.418 -58.049 -16.204 1.00170.63 N ANISOU 377 N ASP A1050 21344 24750 18737 2789 5291 359 N ATOM 378 CA ASP A1050 88.371 -58.656 -17.533 1.00179.17 C ANISOU 378 CA ASP A1050 22753 26570 18751 3102 5541 -93 C ATOM 379 C ASP A1050 86.980 -59.215 -17.868 1.00183.56 C ANISOU 379 C ASP A1050 23651 27446 18647 3040 4882 -743 C ATOM 380 O ASP A1050 86.574 -59.169 -19.032 1.00190.40 O ANISOU 380 O ASP A1050 24774 29159 18411 3264 4904 -855 O ATOM 381 CB ASP A1050 89.415 -59.790 -17.638 1.00184.56 C ANISOU 381 CB ASP A1050 23386 27097 19641 3302 6027 -727 C ATOM 382 CG ASP A1050 90.788 -59.474 -17.064 1.00195.18 C ANISOU 382 CG ASP A1050 24256 28066 21837 3326 6570 -248 C ATOM 383 OD1 ASP A1050 91.442 -58.531 -17.567 1.00199.82 O ANISOU 383 OD1 ASP A1050 24659 28998 22265 3398 7090 474 O ATOM 384 OD2 ASP A1050 91.224 -60.193 -16.137 1.00197.60 O ANISOU 384 OD2 ASP A1050 24350 27768 22962 3286 6497 -584 O ATOM 385 N LYS A1051 86.267 -59.754 -16.854 1.00173.21 N ANISOU 385 N LYS A1051 22306 25520 17987 2735 4311 -1172 N ATOM 386 CA LYS A1051 84.951 -60.391 -16.999 1.00173.55 C ANISOU 386 CA LYS A1051 22566 25746 17630 2567 3678 -1872 C ATOM 387 C LYS A1051 83.808 -59.380 -17.174 1.00176.67 C ANISOU 387 C LYS A1051 22950 26622 17556 2515 3177 -1346 C ATOM 388 O LYS A1051 83.791 -58.331 -16.524 1.00170.96 O ANISOU 388 O LYS A1051 22030 25602 17325 2453 3134 -532 O ATOM 389 CB LYS A1051 84.645 -61.315 -15.801 1.00169.53 C ANISOU 389 CB LYS A1051 21988 24352 18074 2256 3352 -2406 C ATOM 390 CG LYS A1051 85.723 -62.361 -15.494 1.00179.98 C ANISOU 390 CG LYS A1051 23305 25101 19979 2378 3822 -2855 C ATOM 391 CD LYS A1051 85.692 -63.570 -16.427 1.00196.59 C ANISOU 391 CD LYS A1051 25736 27415 21544 2499 3997 -3884 C ATOM 392 CE LYS A1051 86.895 -64.467 -16.246 1.00207.86 C ANISOU 392 CE LYS A1051 27148 28311 23520 2759 4592 -4200 C ATOM 393 NZ LYS A1051 88.134 -63.875 -16.821 1.00217.93 N ANISOU 393 NZ LYS A1051 28264 30018 24520 3132 5245 -3677 N ATOM 394 N SER A1052 82.846 -59.737 -18.051 1.00179.32 N ANISOU 394 N SER A1052 23473 27710 16951 2555 2791 -1880 N ATOM 395 CA SER A1052 81.631 -58.996 -18.407 1.00180.86 C ANISOU 395 CA SER A1052 23636 28569 16512 2591 2243 -1540 C ATOM 396 C SER A1052 80.702 -58.797 -17.185 1.00176.07 C ANISOU 396 C SER A1052 22800 27345 16752 2245 1681 -1426 C ATOM 397 O SER A1052 80.741 -59.627 -16.275 1.00170.45 O ANISOU 397 O SER A1052 22033 25869 16861 1929 1596 -1951 O ATOM 398 CB SER A1052 80.880 -59.740 -19.511 1.00193.78 C ANISOU 398 CB SER A1052 25449 31149 17028 2646 1900 -2428 C ATOM 399 OG SER A1052 80.537 -61.061 -19.120 1.00202.39 O ANISOU 399 OG SER A1052 26577 31767 18557 2264 1645 -3572 O ATOM 400 N PRO A1053 79.849 -57.738 -17.143 1.00171.92 N ANISOU 400 N PRO A1053 22142 27142 16036 2341 1328 -731 N ATOM 401 CA PRO A1053 78.989 -57.531 -15.958 1.00164.41 C ANISOU 401 CA PRO A1053 20956 25622 15889 2049 860 -632 C ATOM 402 C PRO A1053 77.820 -58.518 -15.821 1.00169.07 C ANISOU 402 C PRO A1053 21454 26359 16425 1720 251 -1544 C ATOM 403 O PRO A1053 77.283 -58.654 -14.720 1.00162.41 O ANISOU 403 O PRO A1053 20423 24908 16378 1418 -16 -1608 O ATOM 404 CB PRO A1053 78.453 -56.103 -16.146 1.00167.17 C ANISOU 404 CB PRO A1053 21211 26344 15964 2350 745 368 C ATOM 405 CG PRO A1053 79.269 -55.499 -17.251 1.00178.30 C ANISOU 405 CG PRO A1053 22812 28299 16635 2767 1277 956 C ATOM 406 CD PRO A1053 79.674 -56.642 -18.115 1.00179.69 C ANISOU 406 CD PRO A1053 23182 28972 16122 2777 1409 87 C ATOM 407 N ASP A1054 77.420 -59.192 -16.916 1.00173.83 N ANISOU 407 N ASP A1054 22163 27784 16099 1753 46 -2265 N ATOM 408 CA ASP A1054 76.300 -60.137 -16.903 1.00176.37 C ANISOU 408 CA ASP A1054 22348 28301 16364 1365 -528 -3229 C ATOM 409 C ASP A1054 76.747 -61.597 -16.656 1.00180.36 C ANISOU 409 C ASP A1054 23022 28117 17388 999 -314 -4274 C ATOM 410 O ASP A1054 75.898 -62.491 -16.613 1.00183.31 O ANISOU 410 O ASP A1054 23298 28485 17869 591 -699 -5156 O ATOM 411 CB ASP A1054 75.504 -60.034 -18.217 1.00188.67 C ANISOU 411 CB ASP A1054 23863 31218 16605 1570 -959 -3524 C ATOM 412 CG ASP A1054 74.761 -58.721 -18.412 1.00199.32 C ANISOU 412 CG ASP A1054 24984 33265 17484 1947 -1287 -2535 C ATOM 413 OD1 ASP A1054 74.516 -58.016 -17.404 1.00192.06 O ANISOU 413 OD1 ASP A1054 23881 31713 17381 1914 -1323 -1842 O ATOM 414 OD2 ASP A1054 74.387 -58.419 -19.564 1.00215.01 O ANISOU 414 OD2 ASP A1054 26972 36454 18268 2305 -1515 -2476 O ATOM 415 N SER A1055 78.063 -61.827 -16.460 1.00173.76 N ANISOU 415 N SER A1055 22404 26662 16955 1145 320 -4151 N ATOM 416 CA SER A1055 78.656 -63.147 -16.200 1.00174.02 C ANISOU 416 CA SER A1055 22621 25942 17557 939 642 -4984 C ATOM 417 C SER A1055 78.202 -63.722 -14.835 1.00170.08 C ANISOU 417 C SER A1055 21968 24436 18218 517 470 -5113 C ATOM 418 O SER A1055 77.900 -62.930 -13.939 1.00162.35 O ANISOU 418 O SER A1055 20765 23226 17697 487 295 -4362 O ATOM 419 CB SER A1055 80.180 -63.059 -16.248 1.00176.62 C ANISOU 419 CB SER A1055 23111 25939 18058 1293 1355 -4613 C ATOM 420 OG SER A1055 80.689 -62.170 -15.267 1.00177.52 O ANISOU 420 OG SER A1055 23035 25549 18866 1374 1511 -3628 O ATOM 421 N PRO A1056 78.171 -65.074 -14.636 1.00168.73 N ANISOU 421 N PRO A1056 21932 23623 18556 214 574 -6018 N ATOM 422 CA PRO A1056 77.735 -65.620 -13.333 1.00162.85 C ANISOU 422 CA PRO A1056 21053 21927 18894 -155 481 -6016 C ATOM 423 C PRO A1056 78.647 -65.241 -12.160 1.00156.81 C ANISOU 423 C PRO A1056 20234 20436 18910 64 822 -5155 C ATOM 424 O PRO A1056 78.193 -65.291 -11.016 1.00151.13 O ANISOU 424 O PRO A1056 19347 19173 18902 -154 673 -4868 O ATOM 425 CB PRO A1056 77.735 -67.135 -13.557 1.00171.60 C ANISOU 425 CB PRO A1056 22392 22458 20349 -434 682 -7119 C ATOM 426 CG PRO A1056 78.663 -67.355 -14.695 1.00182.67 C ANISOU 426 CG PRO A1056 24089 24255 21064 -72 1073 -7542 C ATOM 427 CD PRO A1056 78.485 -66.163 -15.584 1.00179.45 C ANISOU 427 CD PRO A1056 23583 25061 19539 199 816 -7088 C ATOM 428 N GLU A1057 79.914 -64.850 -12.437 1.00151.73 N ANISOU 428 N GLU A1057 19688 19856 18105 487 1271 -4757 N ATOM 429 CA GLU A1057 80.889 -64.409 -11.426 1.00144.16 C ANISOU 429 CA GLU A1057 18600 18377 17798 703 1565 -3989 C ATOM 430 C GLU A1057 80.514 -63.029 -10.880 1.00139.75 C ANISOU 430 C GLU A1057 17786 18086 17227 699 1274 -3144 C ATOM 431 O GLU A1057 80.677 -62.775 -9.682 1.00132.87 O ANISOU 431 O GLU A1057 16743 16723 17019 660 1254 -2686 O ATOM 432 CB GLU A1057 82.319 -64.366 -12.001 1.00148.18 C ANISOU 432 CB GLU A1057 19197 18986 18117 1116 2134 -3869 C ATOM 433 CG GLU A1057 82.877 -65.711 -12.432 1.00165.56 C ANISOU 433 CG GLU A1057 21650 20807 20447 1227 2536 -4662 C ATOM 434 CD GLU A1057 82.705 -66.032 -13.903 1.00195.79 C ANISOU 434 CD GLU A1057 25736 25305 23349 1286 2609 -5405 C ATOM 435 OE1 GLU A1057 83.263 -65.292 -14.746 1.00192.05 O ANISOU 435 OE1 GLU A1057 25267 25544 22158 1585 2829 -5092 O ATOM 436 OE2 GLU A1057 82.040 -67.047 -14.214 1.00196.81 O ANISOU 436 OE2 GLU A1057 26059 25246 23472 1026 2481 -6325 O ATOM 437 N MET A1058 80.045 -62.133 -11.763 1.00137.48 N ANISOU 437 N MET A1058 17484 18587 16165 786 1076 -2934 N ATOM 438 CA MET A1058 79.628 -60.776 -11.413 1.00132.42 C ANISOU 438 CA MET A1058 16643 18186 15484 838 846 -2148 C ATOM 439 C MET A1058 78.228 -60.770 -10.795 1.00132.20 C ANISOU 439 C MET A1058 16439 18133 15657 546 313 -2239 C ATOM 440 O MET A1058 77.880 -59.827 -10.084 1.00126.88 O ANISOU 440 O MET A1058 15581 17380 15249 563 155 -1648 O ATOM 441 CB MET A1058 79.663 -59.872 -12.652 1.00139.80 C ANISOU 441 CB MET A1058 17648 19959 15509 1127 902 -1804 C ATOM 442 CG MET A1058 81.051 -59.369 -12.998 1.00144.41 C ANISOU 442 CG MET A1058 18287 20535 16047 1417 1488 -1336 C ATOM 443 SD MET A1058 81.628 -58.005 -11.955 1.00142.01 S ANISOU 443 SD MET A1058 17735 19747 16474 1438 1655 -362 S ATOM 444 CE MET A1058 80.596 -56.663 -12.561 1.00141.15 C ANISOU 444 CE MET A1058 17619 20243 15767 1600 1377 284 C ATOM 445 N LYS A1059 77.431 -61.820 -11.067 1.00131.72 N ANISOU 445 N LYS A1059 16413 18126 15508 262 71 -3019 N ATOM 446 CA LYS A1059 76.069 -61.957 -10.554 1.00130.16 C ANISOU 446 CA LYS A1059 15980 17950 15525 -72 -401 -3194 C ATOM 447 C LYS A1059 76.056 -62.283 -9.051 1.00126.67 C ANISOU 447 C LYS A1059 15431 16656 16040 -268 -323 -2994 C ATOM 448 O LYS A1059 75.281 -61.660 -8.324 1.00122.57 O ANISOU 448 O LYS A1059 14669 16165 15739 -342 -584 -2608 O ATOM 449 CB LYS A1059 75.278 -63.012 -11.350 1.00139.89 C ANISOU 449 CB LYS A1059 17235 19500 16419 -393 -653 -4171 C ATOM 450 CG LYS A1059 74.790 -62.524 -12.717 1.00155.31 C ANISOU 450 CG LYS A1059 19156 22581 17275 -222 -964 -4334 C ATOM 451 CD LYS A1059 73.601 -61.559 -12.622 1.00161.57 C ANISOU 451 CD LYS A1059 19581 23993 17817 -188 -1480 -3866 C ATOM 452 CE LYS A1059 73.208 -61.003 -13.966 1.00175.16 C ANISOU 452 CE LYS A1059 21262 26909 18383 111 -1775 -3863 C ATOM 453 NZ LYS A1059 72.124 -59.996 -13.844 1.00180.98 N ANISOU 453 NZ LYS A1059 21622 28221 18922 268 -2234 -3276 N ATOM 454 N ASP A1060 76.914 -63.229 -8.584 1.00121.67 N ANISOU 454 N ASP A1060 14973 15316 15940 -286 56 -3211 N ATOM 455 CA ASP A1060 76.995 -63.617 -7.178 1.00116.24 C ANISOU 455 CA ASP A1060 14208 13886 16070 -390 167 -2962 C ATOM 456 C ASP A1060 77.603 -62.485 -6.359 1.00110.33 C ANISOU 456 C ASP A1060 13326 13108 15486 -126 226 -2170 C ATOM 457 O ASP A1060 77.223 -62.329 -5.197 1.00105.81 O ANISOU 457 O ASP A1060 12594 12254 15353 -213 127 -1865 O ATOM 458 CB ASP A1060 77.778 -64.925 -6.980 1.00121.21 C ANISOU 458 CB ASP A1060 15063 13807 17186 -376 574 -3335 C ATOM 459 CG ASP A1060 77.430 -65.637 -5.691 1.00134.16 C ANISOU 459 CG ASP A1060 16640 14738 19597 -563 636 -3209 C ATOM 460 OD1 ASP A1060 77.961 -65.239 -4.630 1.00130.07 O ANISOU 460 OD1 ASP A1060 16021 14000 19401 -350 728 -2594 O ATOM 461 OD2 ASP A1060 76.598 -66.562 -5.735 1.00146.80 O ANISOU 461 OD2 ASP A1060 18271 16042 21463 -937 593 -3721 O ATOM 462 N PHE A1061 78.501 -61.670 -6.970 1.00104.55 N ANISOU 462 N PHE A1061 12640 12690 14393 168 402 -1866 N ATOM 463 CA PHE A1061 79.146 -60.513 -6.334 1.00 99.06 C ANISOU 463 CA PHE A1061 11798 11964 13876 355 485 -1204 C ATOM 464 C PHE A1061 78.117 -59.449 -5.936 1.00 99.35 C ANISOU 464 C PHE A1061 11657 12227 13863 290 145 -845 C ATOM 465 O PHE A1061 78.178 -58.934 -4.820 1.00 94.04 O ANISOU 465 O PHE A1061 10837 11287 13605 289 115 -514 O ATOM 466 CB PHE A1061 80.220 -59.885 -7.253 1.00102.73 C ANISOU 466 CB PHE A1061 12328 12725 13979 614 800 -980 C ATOM 467 CG PHE A1061 80.763 -58.568 -6.737 1.00100.41 C ANISOU 467 CG PHE A1061 11856 12398 13899 713 885 -350 C ATOM 468 CD1 PHE A1061 81.790 -58.539 -5.802 1.00100.32 C ANISOU 468 CD1 PHE A1061 11681 12015 14419 753 1079 -174 C ATOM 469 CD2 PHE A1061 80.216 -57.360 -7.153 1.00102.32 C ANISOU 469 CD2 PHE A1061 12068 12966 13841 768 762 49 C ATOM 470 CE1 PHE A1061 82.265 -57.327 -5.303 1.00 98.69 C ANISOU 470 CE1 PHE A1061 11277 11758 14461 759 1137 277 C ATOM 471 CE2 PHE A1061 80.681 -56.153 -6.640 1.00102.59 C ANISOU 471 CE2 PHE A1061 11959 12830 14193 808 883 563 C ATOM 472 CZ PHE A1061 81.710 -56.143 -5.730 1.00 97.99 C ANISOU 472 CZ PHE A1061 11207 11871 14154 762 1066 620 C ATOM 473 N ARG A1062 77.227 -59.077 -6.877 1.00 99.31 N ANISOU 473 N ARG A1062 11652 12770 13310 291 -98 -910 N ATOM 474 CA ARG A1062 76.168 -58.090 -6.660 1.00 97.88 C ANISOU 474 CA ARG A1062 11283 12864 13044 315 -412 -567 C ATOM 475 C ARG A1062 75.091 -58.667 -5.748 1.00 99.72 C ANISOU 475 C ARG A1062 11329 12909 13649 41 -675 -801 C ATOM 476 O ARG A1062 74.446 -57.911 -5.022 1.00 96.54 O ANISOU 476 O ARG A1062 10736 12501 13444 75 -826 -474 O ATOM 477 CB ARG A1062 75.549 -57.629 -7.988 1.00103.54 C ANISOU 477 CB ARG A1062 12012 14326 13003 475 -611 -537 C ATOM 478 CG ARG A1062 76.482 -56.789 -8.852 1.00116.89 C ANISOU 478 CG ARG A1062 13866 16249 14298 797 -300 -90 C ATOM 479 CD ARG A1062 75.761 -56.141 -10.022 1.00135.70 C ANISOU 479 CD ARG A1062 16241 19427 15893 1056 -510 145 C ATOM 480 NE ARG A1062 75.200 -57.123 -10.956 1.00152.46 N ANISOU 480 NE ARG A1062 18392 22149 17387 951 -773 -528 N ATOM 481 CZ ARG A1062 75.823 -57.586 -12.036 1.00170.97 C ANISOU 481 CZ ARG A1062 20958 24879 19123 1058 -576 -823 C ATOM 482 NH1 ARG A1062 77.047 -57.162 -12.337 1.00158.05 N ANISOU 482 NH1 ARG A1062 19510 23101 17441 1284 -75 -426 N ATOM 483 NH2 ARG A1062 75.233 -58.473 -12.822 1.00162.63 N ANISOU 483 NH2 ARG A1062 19910 24375 17506 921 -857 -1559 N ATOM 484 N HIS A1063 74.913 -60.010 -5.780 1.00 98.36 N ANISOU 484 N HIS A1063 11215 12540 13618 -229 -669 -1369 N ATOM 485 CA HIS A1063 73.942 -60.732 -4.955 1.00 97.98 C ANISOU 485 CA HIS A1063 10991 12243 13995 -553 -817 -1597 C ATOM 486 C HIS A1063 74.396 -60.797 -3.482 1.00 94.68 C ANISOU 486 C HIS A1063 10555 11239 14180 -525 -608 -1256 C ATOM 487 O HIS A1063 73.560 -60.693 -2.581 1.00 93.20 O ANISOU 487 O HIS A1063 10160 10991 14263 -646 -724 -1110 O ATOM 488 CB HIS A1063 73.713 -62.146 -5.512 1.00104.75 C ANISOU 488 CB HIS A1063 11950 12959 14893 -877 -791 -2323 C ATOM 489 CG HIS A1063 72.800 -62.985 -4.680 1.00109.63 C ANISOU 489 CG HIS A1063 12391 13205 16060 -1269 -836 -2537 C ATOM 490 ND1 HIS A1063 71.426 -62.791 -4.694 1.00114.02 N ANISOU 490 ND1 HIS A1063 12587 14180 16555 -1519 -1188 -2647 N ATOM 491 CD2 HIS A1063 73.092 -63.987 -3.823 1.00111.58 C ANISOU 491 CD2 HIS A1063 12747 12720 16930 -1420 -531 -2588 C ATOM 492 CE1 HIS A1063 70.929 -63.673 -3.844 1.00114.67 C ANISOU 492 CE1 HIS A1063 12566 13754 17249 -1869 -1057 -2778 C ATOM 493 NE2 HIS A1063 71.890 -64.413 -3.290 1.00113.64 N ANISOU 493 NE2 HIS A1063 12738 12901 17540 -1809 -652 -2713 N ATOM 494 N GLY A1064 75.703 -60.982 -3.271 1.00 87.27 N ANISOU 494 N GLY A1064 9799 9963 13398 -340 -302 -1140 N ATOM 495 CA GLY A1064 76.321 -61.046 -1.950 1.00 82.54 C ANISOU 495 CA GLY A1064 9166 8946 13250 -237 -132 -820 C ATOM 496 C GLY A1064 76.120 -59.782 -1.138 1.00 81.29 C ANISOU 496 C GLY A1064 8823 8944 13118 -121 -264 -391 C ATOM 497 O GLY A1064 76.045 -59.845 0.093 1.00 78.87 O ANISOU 497 O GLY A1064 8420 8443 13105 -112 -243 -205 O ATOM 498 N PHE A1065 76.020 -58.625 -1.838 1.00 76.69 N ANISOU 498 N PHE A1065 8209 8715 12217 -4 -372 -229 N ATOM 499 CA PHE A1065 75.782 -57.312 -1.253 1.00 73.84 C ANISOU 499 CA PHE A1065 7708 8436 11912 120 -459 123 C ATOM 500 C PHE A1065 74.285 -57.090 -0.986 1.00 77.85 C ANISOU 500 C PHE A1065 8026 9158 12395 42 -711 129 C ATOM 501 O PHE A1065 73.968 -56.358 -0.053 1.00 75.67 O ANISOU 501 O PHE A1065 7622 8825 12304 122 -738 333 O ATOM 502 CB PHE A1065 76.368 -56.187 -2.123 1.00 76.76 C ANISOU 502 CB PHE A1065 8145 8970 12052 307 -368 374 C ATOM 503 CG PHE A1065 77.835 -55.938 -1.845 1.00 77.64 C ANISOU 503 CG PHE A1065 8285 8836 12379 376 -99 489 C ATOM 504 CD1 PHE A1065 78.239 -55.255 -0.700 1.00 78.50 C ANISOU 504 CD1 PHE A1065 8259 8734 12836 386 -74 626 C ATOM 505 CD2 PHE A1065 78.814 -56.403 -2.718 1.00 82.45 C ANISOU 505 CD2 PHE A1065 9011 9481 12834 425 129 405 C ATOM 506 CE1 PHE A1065 79.598 -55.053 -0.427 1.00 79.49 C ANISOU 506 CE1 PHE A1065 8311 8716 13177 405 127 668 C ATOM 507 CE2 PHE A1065 80.174 -56.194 -2.449 1.00 84.88 C ANISOU 507 CE2 PHE A1065 9245 9623 13383 481 382 509 C ATOM 508 CZ PHE A1065 80.556 -55.525 -1.304 1.00 80.73 C ANISOU 508 CZ PHE A1065 8530 8918 13227 451 355 636 C ATOM 509 N ASP A1066 73.371 -57.732 -1.769 1.00 77.11 N ANISOU 509 N ASP A1066 7874 9342 12083 -121 -891 -147 N ATOM 510 CA ASP A1066 71.912 -57.662 -1.556 1.00 78.14 C ANISOU 510 CA ASP A1066 7716 9751 12223 -231 -1139 -186 C ATOM 511 C ASP A1066 71.545 -58.363 -0.241 1.00 79.71 C ANISOU 511 C ASP A1066 7800 9626 12860 -428 -1037 -218 C ATOM 512 O ASP A1066 70.621 -57.933 0.453 1.00 79.77 O ANISOU 512 O ASP A1066 7555 9768 12985 -413 -1117 -72 O ATOM 513 CB ASP A1066 71.140 -58.298 -2.726 1.00 85.38 C ANISOU 513 CB ASP A1066 8537 11099 12806 -423 -1379 -577 C ATOM 514 CG ASP A1066 71.162 -57.513 -4.022 1.00100.05 C ANISOU 514 CG ASP A1066 10437 13493 14084 -160 -1537 -461 C ATOM 515 OD1 ASP A1066 70.823 -56.308 -3.996 1.00101.31 O ANISOU 515 OD1 ASP A1066 10486 13864 14143 147 -1614 -19 O ATOM 516 OD2 ASP A1066 71.451 -58.119 -5.073 1.00109.10 O ANISOU 516 OD2 ASP A1066 11727 14865 14861 -236 -1568 -809 O ATOM 517 N ILE A1067 72.296 -59.436 0.094 1.00 74.37 N ANISOU 517 N ILE A1067 7311 8530 12415 -558 -815 -360 N ATOM 518 CA ILE A1067 72.186 -60.211 1.332 1.00 72.83 C ANISOU 518 CA ILE A1067 7080 7979 12611 -675 -630 -275 C ATOM 519 C ILE A1067 72.651 -59.311 2.488 1.00 71.96 C ANISOU 519 C ILE A1067 6945 7853 12543 -396 -564 96 C ATOM 520 O ILE A1067 71.951 -59.177 3.496 1.00 71.55 O ANISOU 520 O ILE A1067 6720 7856 12610 -401 -541 253 O ATOM 521 CB ILE A1067 73.030 -61.525 1.224 1.00 77.29 C ANISOU 521 CB ILE A1067 7897 8073 13397 -767 -378 -456 C ATOM 522 CG1 ILE A1067 72.501 -62.457 0.119 1.00 82.75 C ANISOU 522 CG1 ILE A1067 8621 8738 14083 -1100 -428 -974 C ATOM 523 CG2 ILE A1067 73.120 -62.256 2.570 1.00 77.43 C ANISOU 523 CG2 ILE A1067 7922 7706 13792 -761 -126 -191 C ATOM 524 CD1 ILE A1067 73.524 -63.472 -0.384 1.00 91.89 C ANISOU 524 CD1 ILE A1067 10092 9461 15360 -1083 -170 -1241 C ATOM 525 N LEU A1068 73.830 -58.682 2.301 1.00 65.60 N ANISOU 525 N LEU A1068 6286 7010 11629 -175 -520 186 N ATOM 526 CA LEU A1068 74.498 -57.777 3.228 1.00 63.20 C ANISOU 526 CA LEU A1068 5952 6700 11359 41 -483 396 C ATOM 527 C LEU A1068 73.627 -56.552 3.556 1.00 68.35 C ANISOU 527 C LEU A1068 6443 7566 11961 131 -607 494 C ATOM 528 O LEU A1068 73.544 -56.185 4.722 1.00 68.48 O ANISOU 528 O LEU A1068 6374 7599 12048 225 -572 570 O ATOM 529 CB LEU A1068 75.829 -57.338 2.617 1.00 62.69 C ANISOU 529 CB LEU A1068 6008 6576 11237 161 -410 401 C ATOM 530 CG LEU A1068 76.996 -57.219 3.571 1.00 66.82 C ANISOU 530 CG LEU A1068 6491 7011 11887 295 -320 486 C ATOM 531 CD1 LEU A1068 78.221 -57.890 2.996 1.00 68.05 C ANISOU 531 CD1 LEU A1068 6734 7043 12079 353 -165 441 C ATOM 532 CD2 LEU A1068 77.289 -55.764 3.889 1.00 68.81 C ANISOU 532 CD2 LEU A1068 6644 7336 12163 365 -370 526 C ATOM 533 N VAL A1069 72.961 -55.946 2.542 1.00 65.53 N ANISOU 533 N VAL A1069 6039 7407 11453 152 -741 494 N ATOM 534 CA VAL A1069 72.064 -54.794 2.707 1.00 65.43 C ANISOU 534 CA VAL A1069 5864 7569 11429 319 -832 628 C ATOM 535 C VAL A1069 70.803 -55.261 3.447 1.00 71.31 C ANISOU 535 C VAL A1069 6357 8481 12258 226 -873 596 C ATOM 536 O VAL A1069 70.328 -54.552 4.335 1.00 71.33 O ANISOU 536 O VAL A1069 6230 8530 12342 385 -828 678 O ATOM 537 CB VAL A1069 71.731 -54.085 1.361 1.00 71.20 C ANISOU 537 CB VAL A1069 6599 8520 11934 455 -954 744 C ATOM 538 CG1 VAL A1069 70.648 -53.026 1.526 1.00 72.85 C ANISOU 538 CG1 VAL A1069 6603 8905 12173 700 -1036 931 C ATOM 539 CG2 VAL A1069 72.968 -53.460 0.745 1.00 70.40 C ANISOU 539 CG2 VAL A1069 6726 8230 11791 560 -811 870 C ATOM 540 N GLY A1070 70.309 -56.453 3.097 1.00 70.11 N ANISOU 540 N GLY A1070 6130 8390 12119 -47 -914 445 N ATOM 541 CA GLY A1070 69.146 -57.082 3.724 1.00 71.96 C ANISOU 541 CA GLY A1070 6083 8748 12511 -235 -891 417 C ATOM 542 C GLY A1070 69.331 -57.316 5.213 1.00 74.36 C ANISOU 542 C GLY A1070 6403 8884 12967 -188 -653 570 C ATOM 543 O GLY A1070 68.420 -57.056 6.006 1.00 74.05 O ANISOU 543 O GLY A1070 6116 9035 12983 -138 -585 669 O ATOM 544 N GLN A1071 70.540 -57.777 5.599 1.00 70.30 N ANISOU 544 N GLN A1071 6157 8082 12470 -151 -519 609 N ATOM 545 CA GLN A1071 70.946 -58.016 6.986 1.00 69.97 C ANISOU 545 CA GLN A1071 6159 7977 12449 -26 -326 792 C ATOM 546 C GLN A1071 71.125 -56.695 7.754 1.00 72.20 C ANISOU 546 C GLN A1071 6404 8451 12577 262 -366 805 C ATOM 547 O GLN A1071 70.856 -56.660 8.959 1.00 73.06 O ANISOU 547 O GLN A1071 6432 8719 12607 381 -238 906 O ATOM 548 CB GLN A1071 72.237 -58.838 7.033 1.00 70.91 C ANISOU 548 CB GLN A1071 6523 7814 12607 3 -224 839 C ATOM 549 CG GLN A1071 71.985 -60.348 6.941 1.00 96.37 C ANISOU 549 CG GLN A1071 9802 10732 16080 -230 -27 891 C ATOM 550 CD GLN A1071 73.239 -61.171 6.738 1.00117.35 C ANISOU 550 CD GLN A1071 12706 13054 18827 -140 93 921 C ATOM 551 OE1 GLN A1071 73.283 -62.067 5.892 1.00114.33 O ANISOU 551 OE1 GLN A1071 12444 12355 18642 -336 173 740 O ATOM 552 NE2 GLN A1071 74.277 -60.918 7.527 1.00108.61 N ANISOU 552 NE2 GLN A1071 11649 12036 17583 173 113 1113 N ATOM 553 N ILE A1072 71.571 -55.616 7.057 1.00 66.19 N ANISOU 553 N ILE A1072 5712 7660 11778 372 -502 693 N ATOM 554 CA ILE A1072 71.749 -54.275 7.634 1.00 65.38 C ANISOU 554 CA ILE A1072 5596 7602 11645 596 -509 616 C ATOM 555 C ILE A1072 70.356 -53.714 7.986 1.00 72.41 C ANISOU 555 C ILE A1072 6263 8700 12551 715 -480 639 C ATOM 556 O ILE A1072 70.183 -53.180 9.081 1.00 73.41 O ANISOU 556 O ILE A1072 6335 8940 12618 885 -380 563 O ATOM 557 CB ILE A1072 72.583 -53.327 6.702 1.00 67.07 C ANISOU 557 CB ILE A1072 5946 7610 11929 641 -573 556 C ATOM 558 CG1 ILE A1072 74.080 -53.681 6.747 1.00 65.32 C ANISOU 558 CG1 ILE A1072 5853 7254 11712 574 -551 497 C ATOM 559 CG2 ILE A1072 72.400 -51.850 7.067 1.00 69.99 C ANISOU 559 CG2 ILE A1072 6289 7897 12405 836 -536 465 C ATOM 560 CD1 ILE A1072 74.938 -53.142 5.569 1.00 68.41 C ANISOU 560 CD1 ILE A1072 6356 7450 12186 538 -539 513 C ATOM 561 N ASP A1073 69.368 -53.888 7.084 1.00 71.24 N ANISOU 561 N ASP A1073 5949 8668 12450 641 -569 713 N ATOM 562 CA ASP A1073 67.981 -53.448 7.257 1.00 74.51 C ANISOU 562 CA ASP A1073 6051 9352 12909 771 -557 765 C ATOM 563 C ASP A1073 67.284 -54.155 8.437 1.00 80.79 C ANISOU 563 C ASP A1073 6646 10347 13706 697 -359 816 C ATOM 564 O ASP A1073 66.465 -53.533 9.118 1.00 82.47 O ANISOU 564 O ASP A1073 6646 10771 13919 914 -239 824 O ATOM 565 CB ASP A1073 67.183 -53.686 5.964 1.00 78.99 C ANISOU 565 CB ASP A1073 6415 10120 13476 668 -762 812 C ATOM 566 CG ASP A1073 67.446 -52.699 4.839 1.00 96.41 C ANISOU 566 CG ASP A1073 8733 12288 15611 894 -913 894 C ATOM 567 OD1 ASP A1073 67.944 -51.580 5.128 1.00 97.41 O ANISOU 567 OD1 ASP A1073 9028 12170 15814 1160 -809 936 O ATOM 568 OD2 ASP A1073 67.102 -53.022 3.674 1.00105.70 O ANISOU 568 OD2 ASP A1073 9814 13694 16652 809 -1120 915 O ATOM 569 N ASP A1074 67.600 -55.453 8.663 1.00 77.94 N ANISOU 569 N ASP A1074 6356 9895 13363 421 -269 885 N ATOM 570 CA ASP A1074 67.064 -56.251 9.773 1.00 80.43 C ANISOU 570 CA ASP A1074 6528 10342 13690 341 1 1053 C ATOM 571 C ASP A1074 67.561 -55.675 11.100 1.00 85.35 C ANISOU 571 C ASP A1074 7274 11097 14056 654 149 1065 C ATOM 572 O ASP A1074 66.773 -55.495 12.031 1.00 87.73 O ANISOU 572 O ASP A1074 7379 11693 14262 794 362 1139 O ATOM 573 CB ASP A1074 67.478 -57.728 9.635 1.00 83.04 C ANISOU 573 CB ASP A1074 6990 10399 14163 23 106 1173 C ATOM 574 CG ASP A1074 66.728 -58.545 8.592 1.00 99.56 C ANISOU 574 CG ASP A1074 8889 12406 16532 -381 35 1070 C ATOM 575 OD1 ASP A1074 65.716 -58.037 8.043 1.00102.61 O ANISOU 575 OD1 ASP A1074 8941 13086 16960 -418 -120 956 O ATOM 576 OD2 ASP A1074 67.132 -59.710 8.346 1.00106.94 O ANISOU 576 OD2 ASP A1074 9981 12996 17654 -648 138 1079 O ATOM 577 N ALA A1075 68.873 -55.357 11.153 1.00 80.28 N ANISOU 577 N ALA A1075 6923 10297 13284 761 31 946 N ATOM 578 CA ALA A1075 69.565 -54.745 12.287 1.00 80.66 C ANISOU 578 CA ALA A1075 7080 10519 13050 1021 69 818 C ATOM 579 C ALA A1075 69.071 -53.316 12.514 1.00 85.85 C ANISOU 579 C ALA A1075 7654 11268 13698 1255 67 535 C ATOM 580 O ALA A1075 68.964 -52.886 13.663 1.00 88.09 O ANISOU 580 O ALA A1075 7912 11833 13726 1472 197 392 O ATOM 581 CB ALA A1075 71.062 -54.746 12.036 1.00 79.18 C ANISOU 581 CB ALA A1075 7116 10144 12826 1004 -102 709 C ATOM 582 N LEU A1076 68.755 -52.593 11.417 1.00 81.54 N ANISOU 582 N LEU A1076 7075 10492 13412 1249 -56 466 N ATOM 583 CA LEU A1076 68.226 -51.229 11.445 1.00 83.40 C ANISOU 583 CA LEU A1076 7248 10680 13761 1519 -15 270 C ATOM 584 C LEU A1076 66.830 -51.210 12.057 1.00 90.78 C ANISOU 584 C LEU A1076 7875 11959 14658 1694 189 348 C ATOM 585 O LEU A1076 66.516 -50.291 12.813 1.00 93.31 O ANISOU 585 O LEU A1076 8167 12357 14930 1990 345 117 O ATOM 586 CB LEU A1076 68.183 -50.625 10.033 1.00 82.62 C ANISOU 586 CB LEU A1076 7180 10288 13925 1526 -167 351 C ATOM 587 CG LEU A1076 69.428 -49.891 9.548 1.00 86.19 C ANISOU 587 CG LEU A1076 7909 10337 14504 1498 -242 209 C ATOM 588 CD1 LEU A1076 69.461 -49.856 8.033 1.00 85.90 C ANISOU 588 CD1 LEU A1076 7914 10136 14588 1440 -372 455 C ATOM 589 CD2 LEU A1076 69.490 -48.468 10.105 1.00 90.97 C ANISOU 589 CD2 LEU A1076 8586 10697 15282 1748 -104 -87 C ATOM 590 N LYS A1077 66.003 -52.234 11.740 1.00 87.87 N ANISOU 590 N LYS A1077 7253 11789 14344 1491 217 631 N ATOM 591 CA LYS A1077 64.642 -52.395 12.253 1.00 91.57 C ANISOU 591 CA LYS A1077 7327 12633 14833 1577 441 758 C ATOM 592 C LYS A1077 64.654 -52.591 13.777 1.00 97.88 C ANISOU 592 C LYS A1077 8151 13725 15314 1716 753 744 C ATOM 593 O LYS A1077 63.754 -52.107 14.460 1.00101.75 O ANISOU 593 O LYS A1077 8400 14521 15741 1979 1001 700 O ATOM 594 CB LYS A1077 63.939 -53.576 11.565 1.00 95.12 C ANISOU 594 CB LYS A1077 7488 13182 15471 1195 398 1002 C ATOM 595 CG LYS A1077 62.458 -53.324 11.269 1.00120.01 C ANISOU 595 CG LYS A1077 10100 16683 18817 1274 438 1074 C ATOM 596 CD LYS A1077 61.538 -53.811 12.388 1.00139.60 C ANISOU 596 CD LYS A1077 12233 19532 21276 1258 837 1229 C ATOM 597 CE LYS A1077 60.096 -53.435 12.147 1.00161.20 C ANISOU 597 CE LYS A1077 14348 22674 24225 1391 891 1278 C ATOM 598 NZ LYS A1077 59.199 -53.992 13.196 1.00177.65 N ANISOU 598 NZ LYS A1077 16042 25134 26322 1322 1344 1467 N ATOM 599 N LEU A1078 65.689 -53.272 14.304 1.00 92.27 N ANISOU 599 N LEU A1078 7721 12977 14359 1599 748 796 N ATOM 600 CA LEU A1078 65.868 -53.509 15.739 1.00 94.20 C ANISOU 600 CA LEU A1078 8028 13600 14166 1780 1001 836 C ATOM 601 C LEU A1078 66.336 -52.230 16.445 1.00 98.17 C ANISOU 601 C LEU A1078 8687 14215 14399 2121 968 340 C ATOM 602 O LEU A1078 65.794 -51.886 17.496 1.00101.92 O ANISOU 602 O LEU A1078 9064 15102 14558 2397 1235 222 O ATOM 603 CB LEU A1078 66.871 -54.647 15.979 1.00 92.81 C ANISOU 603 CB LEU A1078 8078 13370 13817 1616 966 1108 C ATOM 604 CG LEU A1078 66.477 -56.020 15.453 1.00 96.99 C ANISOU 604 CG LEU A1078 8508 13694 14652 1265 1087 1552 C ATOM 605 CD1 LEU A1078 67.700 -56.881 15.234 1.00 95.17 C ANISOU 605 CD1 LEU A1078 8568 13180 14413 1150 961 1711 C ATOM 606 CD2 LEU A1078 65.486 -56.703 16.380 1.00103.75 C ANISOU 606 CD2 LEU A1078 9125 14883 15412 1272 1537 1943 C ATOM 607 N ALA A1079 67.332 -51.523 15.852 1.00 90.51 N ANISOU 607 N ALA A1079 7947 12866 13577 2080 676 17 N ATOM 608 CA ALA A1079 67.910 -50.272 16.361 1.00 91.33 C ANISOU 608 CA ALA A1079 8206 12917 13578 2287 623 -555 C ATOM 609 C ALA A1079 66.870 -49.157 16.435 1.00 97.83 C ANISOU 609 C ALA A1079 8898 13677 14597 2585 829 -805 C ATOM 610 O ALA A1079 66.894 -48.387 17.395 1.00101.99 O ANISOU 610 O ALA A1079 9483 14381 14886 2835 969 -1277 O ATOM 611 CB ALA A1079 69.074 -49.836 15.485 1.00 88.66 C ANISOU 611 CB ALA A1079 8071 12086 13530 2090 333 -744 C ATOM 612 N ASN A1080 65.947 -49.086 15.439 1.00 92.40 N ANISOU 612 N ASN A1080 8009 12784 14316 2592 845 -513 N ATOM 613 CA ASN A1080 64.864 -48.090 15.363 1.00 95.21 C ANISOU 613 CA ASN A1080 8169 13083 14923 2953 1044 -626 C ATOM 614 C ASN A1080 63.789 -48.343 16.428 1.00101.81 C ANISOU 614 C ASN A1080 8714 14496 15474 3189 1404 -583 C ATOM 615 O ASN A1080 63.093 -47.406 16.826 1.00105.40 O ANISOU 615 O ASN A1080 9058 14984 16005 3588 1651 -846 O ATOM 616 CB ASN A1080 64.235 -48.065 13.971 1.00 93.60 C ANISOU 616 CB ASN A1080 7768 12656 15141 2922 895 -256 C ATOM 617 CG ASN A1080 64.903 -47.091 13.037 1.00110.69 C ANISOU 617 CG ASN A1080 10189 14220 17647 2978 729 -361 C ATOM 618 OD1 ASN A1080 65.895 -47.403 12.373 1.00 93.14 O ANISOU 618 OD1 ASN A1080 8190 11743 15455 2677 500 -291 O ATOM 619 ND2 ASN A1080 64.368 -45.884 12.967 1.00110.26 N ANISOU 619 ND2 ASN A1080 10105 13903 17887 3393 898 -494 N ATOM 620 N GLU A1081 63.669 -49.606 16.887 1.00 97.26 N ANISOU 620 N GLU A1081 8021 14337 14598 2965 1490 -226 N ATOM 621 CA GLU A1081 62.746 -50.036 17.941 1.00101.56 C ANISOU 621 CA GLU A1081 8289 15472 14827 3129 1899 -67 C ATOM 622 C GLU A1081 63.378 -49.830 19.335 1.00108.05 C ANISOU 622 C GLU A1081 9367 16676 15009 3351 2055 -416 C ATOM 623 O GLU A1081 62.691 -49.965 20.353 1.00112.61 O ANISOU 623 O GLU A1081 9774 17810 15203 3592 2449 -364 O ATOM 624 CB GLU A1081 62.361 -51.513 17.747 1.00101.99 C ANISOU 624 CB GLU A1081 8117 15705 14929 2748 1975 535 C ATOM 625 CG GLU A1081 61.320 -51.760 16.670 1.00112.40 C ANISOU 625 CG GLU A1081 9000 16935 16771 2562 1919 801 C ATOM 626 CD GLU A1081 60.956 -53.219 16.466 1.00138.48 C ANISOU 626 CD GLU A1081 12073 20320 20223 2091 2013 1274 C ATOM 627 OE1 GLU A1081 61.867 -54.035 16.193 1.00123.05 O ANISOU 627 OE1 GLU A1081 10424 18080 18249 1778 1838 1407 O ATOM 628 OE2 GLU A1081 59.750 -53.545 16.561 1.00145.94 O ANISOU 628 OE2 GLU A1081 12504 21583 21363 2025 2287 1496 O ATOM 629 N GLY A1082 64.674 -49.503 19.349 1.00101.84 N ANISOU 629 N GLY A1082 8947 15656 14091 3268 1744 -778 N ATOM 630 CA GLY A1082 65.467 -49.279 20.552 1.00104.89 C ANISOU 630 CA GLY A1082 9558 16459 13839 3434 1749 -1209 C ATOM 631 C GLY A1082 65.929 -50.582 21.164 1.00108.61 C ANISOU 631 C GLY A1082 10065 17410 13792 3323 1760 -716 C ATOM 632 O GLY A1082 65.725 -50.812 22.359 1.00114.68 O ANISOU 632 O GLY A1082 10810 18858 13906 3584 2028 -687 O ATOM 633 N LYS A1083 66.538 -51.455 20.335 1.00 98.12 N ANISOU 633 N LYS A1083 8802 15732 12745 2979 1509 -290 N ATOM 634 CA LYS A1083 67.001 -52.781 20.740 1.00 97.29 C ANISOU 634 CA LYS A1083 8752 15907 12309 2890 1547 284 C ATOM 635 C LYS A1083 68.494 -52.928 20.433 1.00 97.66 C ANISOU 635 C LYS A1083 9026 15760 12320 2755 1119 153 C ATOM 636 O LYS A1083 68.861 -53.453 19.379 1.00 93.14 O ANISOU 636 O LYS A1083 8497 14673 12220 2463 942 403 O ATOM 637 CB LYS A1083 66.158 -53.868 20.034 1.00 97.48 C ANISOU 637 CB LYS A1083 8580 15656 12802 2603 1755 955 C ATOM 638 CG LYS A1083 64.671 -53.830 20.401 1.00108.40 C ANISOU 638 CG LYS A1083 9622 17329 14235 2708 2208 1137 C ATOM 639 CD LYS A1083 63.808 -54.704 19.510 1.00111.82 C ANISOU 639 CD LYS A1083 9770 17439 15277 2323 2331 1611 C ATOM 640 CE LYS A1083 62.365 -54.626 19.942 1.00123.04 C ANISOU 640 CE LYS A1083 10757 19236 16758 2424 2788 1771 C ATOM 641 NZ LYS A1083 61.467 -55.342 19.003 1.00130.41 N ANISOU 641 NZ LYS A1083 11308 19901 18343 1993 2844 2090 N ATOM 642 N VAL A1084 69.354 -52.445 21.361 1.00 96.55 N ANISOU 642 N VAL A1084 8992 16095 11599 2973 952 -293 N ATOM 643 CA VAL A1084 70.823 -52.432 21.245 1.00 94.09 C ANISOU 643 CA VAL A1084 8793 15761 11196 2881 529 -527 C ATOM 644 C VAL A1084 71.377 -53.859 21.136 1.00 95.78 C ANISOU 644 C VAL A1084 9040 16016 11337 2844 506 220 C ATOM 645 O VAL A1084 71.981 -54.188 20.113 1.00 90.81 O ANISOU 645 O VAL A1084 8458 14845 11201 2590 309 346 O ATOM 646 CB VAL A1084 71.512 -51.652 22.397 1.00103.68 C ANISOU 646 CB VAL A1084 10021 17641 11730 3120 346 -1224 C ATOM 647 CG1 VAL A1084 73.011 -51.506 22.146 1.00102.54 C ANISOU 647 CG1 VAL A1084 9881 17450 11630 2952 -123 -1554 C ATOM 648 CG2 VAL A1084 70.880 -50.279 22.600 1.00106.22 C ANISOU 648 CG2 VAL A1084 10347 17850 12160 3194 469 -1999 C ATOM 649 N LYS A1085 71.162 -54.695 22.179 1.00 96.38 N ANISOU 649 N LYS A1085 9104 16712 10805 3134 756 738 N ATOM 650 CA LYS A1085 71.631 -56.086 22.272 1.00 96.38 C ANISOU 650 CA LYS A1085 9160 16751 10710 3207 836 1541 C ATOM 651 C LYS A1085 71.193 -56.947 21.074 1.00 94.51 C ANISOU 651 C LYS A1085 8949 15672 11289 2842 1000 2023 C ATOM 652 O LYS A1085 71.935 -57.834 20.654 1.00 92.07 O ANISOU 652 O LYS A1085 8730 15066 11188 2794 922 2408 O ATOM 653 CB LYS A1085 71.136 -56.723 23.580 1.00105.86 C ANISOU 653 CB LYS A1085 10347 18700 11174 3600 1229 2106 C ATOM 654 CG LYS A1085 72.142 -56.680 24.730 1.00121.88 C ANISOU 654 CG LYS A1085 12388 21668 12251 4049 983 2030 C ATOM 655 CD LYS A1085 72.072 -55.388 25.536 1.00134.91 C ANISOU 655 CD LYS A1085 13977 23997 13283 4223 828 1125 C ATOM 656 CE LYS A1085 73.176 -55.305 26.558 1.00152.76 C ANISOU 656 CE LYS A1085 16193 27253 14597 4605 459 898 C ATOM 657 NZ LYS A1085 73.188 -53.984 27.238 1.00167.12 N ANISOU 657 NZ LYS A1085 17955 29643 15899 4683 262 -192 N ATOM 658 N GLU A1086 70.003 -56.667 20.522 1.00 89.73 N ANISOU 658 N GLU A1086 8238 14720 11136 2605 1214 1948 N ATOM 659 CA GLU A1086 69.424 -57.376 19.381 1.00 86.04 C ANISOU 659 CA GLU A1086 7729 13562 11399 2215 1335 2254 C ATOM 660 C GLU A1086 70.059 -56.903 18.071 1.00 84.85 C ANISOU 660 C GLU A1086 7650 12856 11731 1955 937 1833 C ATOM 661 O GLU A1086 70.353 -57.743 17.218 1.00 83.15 O ANISOU 661 O GLU A1086 7511 12159 11923 1721 907 2078 O ATOM 662 CB GLU A1086 67.896 -57.211 19.340 1.00 88.62 C ANISOU 662 CB GLU A1086 7810 13900 11960 2089 1672 2310 C ATOM 663 CG GLU A1086 67.179 -57.831 20.528 1.00101.65 C ANISOU 663 CG GLU A1086 9358 16048 13217 2290 2182 2844 C ATOM 664 CD GLU A1086 66.949 -56.902 21.706 1.00115.98 C ANISOU 664 CD GLU A1086 11125 18619 14322 2711 2289 2533 C ATOM 665 OE1 GLU A1086 65.769 -56.584 21.977 1.00122.92 O ANISOU 665 OE1 GLU A1086 11759 19710 15233 2745 2631 2522 O ATOM 666 OE2 GLU A1086 67.935 -56.487 22.357 1.00 96.42 O ANISOU 666 OE2 GLU A1086 8820 16562 11255 3008 2035 2252 O ATOM 667 N ALA A1087 70.289 -55.572 17.917 1.00 79.17 N ANISOU 667 N ALA A1087 6924 12180 10976 2006 680 1206 N ATOM 668 CA ALA A1087 70.930 -54.987 16.733 1.00 74.07 C ANISOU 668 CA ALA A1087 6352 11043 10749 1797 363 855 C ATOM 669 C ALA A1087 72.416 -55.355 16.676 1.00 77.21 C ANISOU 669 C ALA A1087 6867 11423 11046 1812 118 858 C ATOM 670 O ALA A1087 72.944 -55.546 15.580 1.00 74.04 O ANISOU 670 O ALA A1087 6531 10570 11031 1603 -21 860 O ATOM 671 CB ALA A1087 70.763 -53.478 16.724 1.00 74.81 C ANISOU 671 CB ALA A1087 6416 11126 10883 1874 258 261 C ATOM 672 N GLN A1088 73.078 -55.475 17.852 1.00 77.05 N ANISOU 672 N GLN A1088 6838 11970 10466 2093 69 869 N ATOM 673 CA GLN A1088 74.485 -55.871 17.970 1.00 77.41 C ANISOU 673 CA GLN A1088 6897 12168 10349 2192 -177 914 C ATOM 674 C GLN A1088 74.651 -57.366 17.615 1.00 82.10 C ANISOU 674 C GLN A1088 7578 12479 11137 2203 -3 1607 C ATOM 675 O GLN A1088 75.695 -57.757 17.083 1.00 80.85 O ANISOU 675 O GLN A1088 7438 12122 11158 2192 -165 1661 O ATOM 676 CB GLN A1088 75.021 -55.584 19.382 1.00 84.27 C ANISOU 676 CB GLN A1088 7675 13875 10471 2539 -308 732 C ATOM 677 CG GLN A1088 75.326 -54.108 19.649 1.00 96.75 C ANISOU 677 CG GLN A1088 9170 15650 11940 2475 -558 -136 C ATOM 678 CD GLN A1088 75.761 -53.825 21.073 1.00118.72 C ANISOU 678 CD GLN A1088 11842 19364 13901 2797 -713 -443 C ATOM 679 OE1 GLN A1088 75.418 -54.538 22.022 1.00118.44 O ANISOU 679 OE1 GLN A1088 11817 19923 13259 3140 -536 21 O ATOM 680 NE2 GLN A1088 76.495 -52.742 21.263 1.00112.76 N ANISOU 680 NE2 GLN A1088 10970 18779 13094 2684 -1027 -1258 N ATOM 681 N ALA A1089 73.610 -58.185 17.902 1.00 80.71 N ANISOU 681 N ALA A1089 7438 12242 10985 2214 371 2114 N ATOM 682 CA ALA A1089 73.558 -59.617 17.597 1.00 81.81 C ANISOU 682 CA ALA A1089 7684 11967 11433 2171 643 2751 C ATOM 683 C ALA A1089 73.398 -59.844 16.088 1.00 83.84 C ANISOU 683 C ALA A1089 8003 11476 12377 1757 609 2588 C ATOM 684 O ALA A1089 73.982 -60.784 15.544 1.00 83.28 O ANISOU 684 O ALA A1089 8051 10989 12603 1725 668 2832 O ATOM 685 CB ALA A1089 72.412 -60.268 18.351 1.00 86.65 C ANISOU 685 CB ALA A1089 8273 12708 11943 2218 1101 3273 C ATOM 686 N ALA A1090 72.609 -58.975 15.416 1.00 79.44 N ANISOU 686 N ALA A1090 7360 10787 12036 1491 522 2170 N ATOM 687 CA ALA A1090 72.366 -59.016 13.973 1.00 76.87 C ANISOU 687 CA ALA A1090 7061 9929 12217 1137 437 1966 C ATOM 688 C ALA A1090 73.617 -58.587 13.191 1.00 81.56 C ANISOU 688 C ALA A1090 7747 10360 12884 1140 145 1667 C ATOM 689 O ALA A1090 73.792 -58.991 12.037 1.00 80.11 O ANISOU 689 O ALA A1090 7647 9761 13032 930 116 1609 O ATOM 690 CB ALA A1090 71.191 -58.123 13.619 1.00 76.54 C ANISOU 690 CB ALA A1090 6855 9945 12281 984 411 1692 C ATOM 691 N ALA A1091 74.490 -57.778 13.832 1.00 80.05 N ANISOU 691 N ALA A1091 7511 10533 12373 1359 -54 1444 N ATOM 692 CA ALA A1091 75.759 -57.305 13.283 1.00 78.66 C ANISOU 692 CA ALA A1091 7335 10281 12272 1351 -294 1169 C ATOM 693 C ALA A1091 76.786 -58.442 13.227 1.00 85.10 C ANISOU 693 C ALA A1091 8197 11012 13125 1499 -258 1489 C ATOM 694 O ALA A1091 77.650 -58.432 12.351 1.00 83.64 O ANISOU 694 O ALA A1091 8023 10594 13163 1424 -348 1357 O ATOM 695 CB ALA A1091 76.295 -56.154 14.117 1.00 81.04 C ANISOU 695 CB ALA A1091 7505 11020 12265 1482 -499 775 C ATOM 696 N GLU A1092 76.684 -59.426 14.148 1.00 85.79 N ANISOU 696 N GLU A1092 8310 11279 13006 1749 -78 1958 N ATOM 697 CA GLU A1092 77.549 -60.614 14.194 1.00 88.41 C ANISOU 697 CA GLU A1092 8702 11478 13411 1993 31 2382 C ATOM 698 C GLU A1092 77.289 -61.523 12.977 1.00 90.31 C ANISOU 698 C GLU A1092 9131 10981 14200 1743 252 2464 C ATOM 699 O GLU A1092 78.183 -62.258 12.566 1.00 90.76 O ANISOU 699 O GLU A1092 9251 10782 14453 1891 314 2605 O ATOM 700 CB GLU A1092 77.334 -61.408 15.498 1.00 95.45 C ANISOU 700 CB GLU A1092 9608 12710 13950 2361 244 2973 C ATOM 701 CG GLU A1092 77.885 -60.746 16.754 1.00114.83 C ANISOU 701 CG GLU A1092 11869 16035 15728 2719 -7 2904 C ATOM 702 CD GLU A1092 77.630 -61.446 18.082 1.00156.25 C ANISOU 702 CD GLU A1092 17131 21768 20468 3149 210 3540 C ATOM 703 OE1 GLU A1092 76.953 -62.500 18.099 1.00161.03 O ANISOU 703 OE1 GLU A1092 17911 21944 21328 3154 637 4128 O ATOM 704 OE2 GLU A1092 78.106 -60.923 19.116 1.00159.27 O ANISOU 704 OE2 GLU A1092 17343 22986 20186 3472 -34 3436 O ATOM 705 N GLN A1093 76.063 -61.472 12.410 1.00 85.19 N ANISOU 705 N GLN A1093 8542 10038 13789 1379 365 2331 N ATOM 706 CA GLN A1093 75.663 -62.237 11.228 1.00 84.42 C ANISOU 706 CA GLN A1093 8586 9334 14158 1065 520 2250 C ATOM 707 C GLN A1093 76.331 -61.677 9.960 1.00 84.75 C ANISOU 707 C GLN A1093 8654 9249 14299 937 306 1817 C ATOM 708 O GLN A1093 76.591 -62.444 9.028 1.00 86.18 O ANISOU 708 O GLN A1093 8978 9002 14763 830 422 1737 O ATOM 709 CB GLN A1093 74.140 -62.254 11.081 1.00 86.28 C ANISOU 709 CB GLN A1093 8760 9472 14551 715 638 2197 C ATOM 710 CG GLN A1093 73.476 -63.363 11.905 1.00113.69 C ANISOU 710 CG GLN A1093 12258 12759 18178 713 1034 2693 C ATOM 711 CD GLN A1093 71.985 -63.172 12.116 1.00141.21 C ANISOU 711 CD GLN A1093 15551 16365 21739 419 1157 2684 C ATOM 712 OE1 GLN A1093 71.467 -63.363 13.226 1.00137.73 O ANISOU 712 OE1 GLN A1093 15030 16159 21143 549 1414 3089 O ATOM 713 NE2 GLN A1093 71.252 -62.828 11.053 1.00136.42 N ANISOU 713 NE2 GLN A1093 14829 15658 21346 44 996 2256 N ATOM 714 N LEU A1094 76.624 -60.350 9.934 1.00 76.45 N ANISOU 714 N LEU A1094 7477 8545 13027 954 42 1537 N ATOM 715 CA LEU A1094 77.314 -59.666 8.831 1.00 72.54 C ANISOU 715 CA LEU A1094 6987 7974 12602 858 -105 1220 C ATOM 716 C LEU A1094 78.746 -60.182 8.698 1.00 75.03 C ANISOU 716 C LEU A1094 7296 8238 12974 1074 -69 1293 C ATOM 717 O LEU A1094 79.260 -60.259 7.587 1.00 73.39 O ANISOU 717 O LEU A1094 7156 7817 12912 994 -30 1131 O ATOM 718 CB LEU A1094 77.325 -58.144 9.045 1.00 70.89 C ANISOU 718 CB LEU A1094 6642 8057 12237 838 -309 974 C ATOM 719 CG LEU A1094 76.038 -57.402 8.724 1.00 74.90 C ANISOU 719 CG LEU A1094 7141 8559 12758 668 -346 850 C ATOM 720 CD1 LEU A1094 75.851 -56.222 9.641 1.00 75.38 C ANISOU 720 CD1 LEU A1094 7081 8900 12661 769 -441 699 C ATOM 721 CD2 LEU A1094 76.021 -56.932 7.285 1.00 76.69 C ANISOU 721 CD2 LEU A1094 7438 8595 13106 511 -395 696 C ATOM 722 N LYS A1095 79.371 -60.549 9.841 1.00 73.22 N ANISOU 722 N LYS A1095 6959 8273 12587 1393 -73 1559 N ATOM 723 CA LYS A1095 80.717 -61.118 9.927 1.00 75.32 C ANISOU 723 CA LYS A1095 7132 8596 12890 1706 -48 1713 C ATOM 724 C LYS A1095 80.796 -62.412 9.120 1.00 81.89 C ANISOU 724 C LYS A1095 8190 8861 14063 1741 249 1856 C ATOM 725 O LYS A1095 81.801 -62.641 8.455 1.00 82.69 O ANISOU 725 O LYS A1095 8253 8858 14306 1867 305 1776 O ATOM 726 CB LYS A1095 81.126 -61.383 11.389 1.00 80.81 C ANISOU 726 CB LYS A1095 7662 9774 13269 2105 -121 2060 C ATOM 727 CG LYS A1095 81.504 -60.139 12.174 1.00 89.96 C ANISOU 727 CG LYS A1095 8537 11575 14070 2120 -453 1772 C ATOM 728 CD LYS A1095 81.928 -60.483 13.591 1.00100.31 C ANISOU 728 CD LYS A1095 9669 13504 14942 2561 -560 2094 C ATOM 729 CE LYS A1095 82.281 -59.242 14.374 1.00111.57 C ANISOU 729 CE LYS A1095 10801 15604 15986 2525 -916 1652 C ATOM 730 NZ LYS A1095 82.777 -59.571 15.735 1.00127.60 N ANISOU 730 NZ LYS A1095 12616 18409 17459 2995 -1084 1921 N ATOM 731 N THR A1096 79.723 -63.236 9.156 1.00 80.14 N ANISOU 731 N THR A1096 8183 8254 14011 1602 471 2017 N ATOM 732 CA THR A1096 79.615 -64.503 8.422 1.00 82.89 C ANISOU 732 CA THR A1096 8779 7953 14764 1550 791 2048 C ATOM 733 C THR A1096 79.508 -64.216 6.904 1.00 84.95 C ANISOU 733 C THR A1096 9138 8012 15126 1216 747 1522 C ATOM 734 O THR A1096 80.032 -64.988 6.099 1.00 86.62 O ANISOU 734 O THR A1096 9502 7836 15572 1274 951 1384 O ATOM 735 CB THR A1096 78.417 -65.327 8.959 1.00 92.54 C ANISOU 735 CB THR A1096 10138 8837 16185 1390 1045 2321 C ATOM 736 OG1 THR A1096 78.421 -65.323 10.391 1.00 92.80 O ANISOU 736 OG1 THR A1096 10064 9240 15958 1712 1064 2834 O ATOM 737 CG2 THR A1096 78.418 -66.769 8.458 1.00 95.71 C ANISOU 737 CG2 THR A1096 10801 8461 17105 1368 1446 2390 C ATOM 738 N THR A1097 78.849 -63.098 6.529 1.00 78.38 N ANISOU 738 N THR A1097 8223 7473 14086 927 502 1250 N ATOM 739 CA THR A1097 78.678 -62.681 5.134 1.00 76.95 C ANISOU 739 CA THR A1097 8114 7252 13869 671 429 841 C ATOM 740 C THR A1097 80.007 -62.130 4.596 1.00 80.15 C ANISOU 740 C THR A1097 8443 7830 14182 859 405 757 C ATOM 741 O THR A1097 80.389 -62.460 3.474 1.00 81.16 O ANISOU 741 O THR A1097 8697 7798 14344 829 533 527 O ATOM 742 CB THR A1097 77.528 -61.652 5.000 1.00 82.20 C ANISOU 742 CB THR A1097 8686 8193 14352 407 201 710 C ATOM 743 OG1 THR A1097 76.421 -62.054 5.810 1.00 87.64 O ANISOU 743 OG1 THR A1097 9334 8835 15130 287 247 867 O ATOM 744 CG2 THR A1097 77.062 -61.475 3.561 1.00 78.21 C ANISOU 744 CG2 THR A1097 8267 7686 13763 168 131 365 C ATOM 745 N ARG A1098 80.702 -61.297 5.401 1.00 74.89 N ANISOU 745 N ARG A1098 7542 7517 13394 1030 257 902 N ATOM 746 CA ARG A1098 81.985 -60.669 5.069 1.00 74.41 C ANISOU 746 CA ARG A1098 7295 7664 13313 1150 238 835 C ATOM 747 C ARG A1098 83.091 -61.739 4.907 1.00 83.01 C ANISOU 747 C ARG A1098 8367 8597 14575 1467 465 938 C ATOM 748 O ARG A1098 83.979 -61.566 4.068 1.00 84.31 O ANISOU 748 O ARG A1098 8456 8799 14780 1513 581 809 O ATOM 749 CB ARG A1098 82.344 -59.619 6.145 1.00 71.07 C ANISOU 749 CB ARG A1098 6582 7652 12772 1195 5 878 C ATOM 750 CG ARG A1098 83.808 -59.185 6.225 1.00 66.78 C ANISOU 750 CG ARG A1098 5711 7378 12286 1329 -27 837 C ATOM 751 CD ARG A1098 84.394 -59.719 7.502 1.00 62.27 C ANISOU 751 CD ARG A1098 4911 7119 11628 1668 -136 1052 C ATOM 752 NE ARG A1098 84.592 -58.677 8.501 1.00 60.11 N ANISOU 752 NE ARG A1098 4344 7312 11182 1609 -424 902 N ATOM 753 CZ ARG A1098 84.918 -58.909 9.768 1.00 77.61 C ANISOU 753 CZ ARG A1098 6341 9986 13162 1891 -609 1040 C ATOM 754 NH1 ARG A1098 85.116 -57.899 10.604 1.00 69.44 N ANISOU 754 NH1 ARG A1098 5033 9413 11939 1793 -888 761 N ATOM 755 NH2 ARG A1098 85.038 -60.156 10.212 1.00 61.68 N ANISOU 755 NH2 ARG A1098 4387 7967 11083 2291 -500 1455 N ATOM 756 N ASN A1099 83.029 -62.829 5.705 1.00 81.64 N ANISOU 756 N ASN A1099 8259 8242 14520 1719 576 1215 N ATOM 757 CA ASN A1099 83.975 -63.934 5.629 1.00 85.66 C ANISOU 757 CA ASN A1099 8775 8519 15252 2110 835 1381 C ATOM 758 C ASN A1099 83.708 -64.784 4.386 1.00 92.61 C ANISOU 758 C ASN A1099 9990 8850 16347 1991 1137 1095 C ATOM 759 O ASN A1099 84.655 -65.312 3.804 1.00 96.18 O ANISOU 759 O ASN A1099 10436 9159 16950 2256 1374 1030 O ATOM 760 CB ASN A1099 83.936 -64.798 6.885 1.00 90.08 C ANISOU 760 CB ASN A1099 9329 9021 15875 2468 901 1863 C ATOM 761 CG ASN A1099 84.277 -64.080 8.174 1.00114.74 C ANISOU 761 CG ASN A1099 12112 12808 18678 2659 589 2105 C ATOM 762 OD1 ASN A1099 84.915 -63.019 8.200 1.00106.25 O ANISOU 762 OD1 ASN A1099 10720 12219 17430 2587 334 1891 O ATOM 763 ND2 ASN A1099 83.797 -64.620 9.283 1.00111.27 N ANISOU 763 ND2 ASN A1099 11730 12408 18140 2871 621 2530 N ATOM 764 N ALA A1100 82.432 -64.906 3.971 1.00 88.20 N ANISOU 764 N ALA A1100 9685 8037 15791 1597 1125 873 N ATOM 765 CA ALA A1100 82.035 -65.639 2.765 1.00 90.38 C ANISOU 765 CA ALA A1100 10257 7882 16200 1394 1340 453 C ATOM 766 C ALA A1100 82.503 -64.874 1.496 1.00 93.01 C ANISOU 766 C ALA A1100 10566 8527 16249 1305 1299 103 C ATOM 767 O ALA A1100 82.726 -65.481 0.449 1.00 95.38 O ANISOU 767 O ALA A1100 11063 8605 16573 1312 1528 -253 O ATOM 768 CB ALA A1100 80.527 -65.841 2.751 1.00 90.92 C ANISOU 768 CB ALA A1100 10472 7760 16314 959 1258 292 C ATOM 769 N TYR A1101 82.707 -63.546 1.634 1.00 86.23 N ANISOU 769 N TYR A1101 9468 8165 15131 1247 1054 220 N ATOM 770 CA TYR A1101 83.207 -62.660 0.588 1.00 85.77 C ANISOU 770 CA TYR A1101 9350 8414 14825 1186 1065 59 C ATOM 771 C TYR A1101 84.723 -62.796 0.453 1.00 91.11 C ANISOU 771 C TYR A1101 9827 9174 15618 1521 1302 144 C ATOM 772 O TYR A1101 85.205 -62.983 -0.662 1.00 93.62 O ANISOU 772 O TYR A1101 10239 9495 15836 1580 1551 -75 O ATOM 773 CB TYR A1101 82.830 -61.178 0.872 1.00 84.30 C ANISOU 773 CB TYR A1101 8987 8590 14453 990 784 194 C ATOM 774 CG TYR A1101 83.525 -60.178 -0.037 1.00 87.72 C ANISOU 774 CG TYR A1101 9320 9283 14725 963 874 183 C ATOM 775 CD1 TYR A1101 84.770 -59.644 0.298 1.00 90.67 C ANISOU 775 CD1 TYR A1101 9374 9823 15252 1088 957 332 C ATOM 776 CD2 TYR A1101 82.947 -59.778 -1.240 1.00 89.27 C ANISOU 776 CD2 TYR A1101 9709 9599 14613 817 893 51 C ATOM 777 CE1 TYR A1101 85.445 -58.779 -0.565 1.00 92.51 C ANISOU 777 CE1 TYR A1101 9497 10236 15416 1028 1136 366 C ATOM 778 CE2 TYR A1101 83.601 -58.892 -2.099 1.00 91.29 C ANISOU 778 CE2 TYR A1101 9899 10078 14711 828 1061 150 C ATOM 779 CZ TYR A1101 84.851 -58.398 -1.757 1.00 97.91 C ANISOU 779 CZ TYR A1101 10432 10981 15787 911 1217 318 C ATOM 780 OH TYR A1101 85.498 -57.521 -2.589 1.00 98.86 O ANISOU 780 OH TYR A1101 10462 11272 15828 877 1458 463 O ATOM 781 N ILE A1102 85.474 -62.629 1.571 1.00 86.29 N ANISOU 781 N ILE A1102 8891 8728 15166 1745 1214 445 N ATOM 782 CA ILE A1102 86.945 -62.644 1.590 1.00 88.57 C ANISOU 782 CA ILE A1102 8836 9227 15591 2065 1377 553 C ATOM 783 C ILE A1102 87.511 -64.021 1.131 1.00 95.38 C ANISOU 783 C ILE A1102 9846 9733 16663 2448 1758 493 C ATOM 784 O ILE A1102 88.588 -64.054 0.529 1.00 97.49 O ANISOU 784 O ILE A1102 9914 10143 16985 2671 2013 443 O ATOM 785 CB ILE A1102 87.565 -62.168 2.947 1.00 91.81 C ANISOU 785 CB ILE A1102 8798 10019 16068 2215 1113 828 C ATOM 786 CG1 ILE A1102 87.198 -63.080 4.139 1.00 93.62 C ANISOU 786 CG1 ILE A1102 9095 10116 16360 2492 1021 1113 C ATOM 787 CG2 ILE A1102 87.207 -60.703 3.236 1.00 89.08 C ANISOU 787 CG2 ILE A1102 8295 9971 15579 1831 822 758 C ATOM 788 CD1 ILE A1102 88.344 -63.341 5.137 1.00105.17 C ANISOU 788 CD1 ILE A1102 10104 11963 17892 2962 939 1420 C ATOM 789 N GLN A1103 86.774 -65.130 1.371 1.00 92.15 N ANISOU 789 N GLN A1103 9778 8821 16414 2510 1849 481 N ATOM 790 CA GLN A1103 87.174 -66.465 0.918 1.00 96.77 C ANISOU 790 CA GLN A1103 10583 8899 17286 2850 2263 363 C ATOM 791 C GLN A1103 87.128 -66.539 -0.612 1.00102.85 C ANISOU 791 C GLN A1103 11609 9587 17880 2684 2508 -170 C ATOM 792 O GLN A1103 87.961 -67.214 -1.217 1.00107.31 O ANISOU 792 O GLN A1103 12205 9983 18586 3028 2893 -331 O ATOM 793 CB GLN A1103 86.264 -67.553 1.515 1.00 99.65 C ANISOU 793 CB GLN A1103 11279 8641 17941 2843 2344 457 C ATOM 794 CG GLN A1103 86.593 -67.959 2.947 1.00111.66 C ANISOU 794 CG GLN A1103 12607 10154 19664 3256 2300 1072 C ATOM 795 CD GLN A1103 85.823 -69.185 3.407 1.00136.33 C ANISOU 795 CD GLN A1103 16093 12533 23172 3302 2550 1242 C ATOM 796 OE1 GLN A1103 84.618 -69.347 3.161 1.00130.97 O ANISOU 796 OE1 GLN A1103 15703 11520 22540 2816 2535 978 O ATOM 797 NE2 GLN A1103 86.497 -70.066 4.127 1.00134.89 N ANISOU 797 NE2 GLN A1103 15862 12086 23303 3896 2798 1737 N ATOM 798 N LYS A1104 86.172 -65.814 -1.228 1.00 96.62 N ANISOU 798 N LYS A1104 10982 8993 16738 2210 2289 -427 N ATOM 799 CA LYS A1104 85.940 -65.802 -2.669 1.00 98.85 C ANISOU 799 CA LYS A1104 11517 9352 16689 2037 2441 -921 C ATOM 800 C LYS A1104 86.708 -64.708 -3.428 1.00103.87 C ANISOU 800 C LYS A1104 11931 10562 16974 2060 2509 -852 C ATOM 801 O LYS A1104 87.306 -65.022 -4.460 1.00107.77 O ANISOU 801 O LYS A1104 12518 11127 17304 2234 2861 -1127 O ATOM 802 CB LYS A1104 84.437 -65.659 -2.972 1.00 99.28 C ANISOU 802 CB LYS A1104 11824 9391 16507 1562 2151 -1199 C ATOM 803 CG LYS A1104 83.602 -66.884 -2.593 1.00113.61 C ANISOU 803 CG LYS A1104 13899 10573 18694 1432 2204 -1422 C ATOM 804 CD LYS A1104 82.111 -66.640 -2.802 1.00120.24 C ANISOU 804 CD LYS A1104 14840 11514 19330 926 1873 -1674 C ATOM 805 CE LYS A1104 81.254 -67.757 -2.251 1.00128.45 C ANISOU 805 CE LYS A1104 16044 11913 20847 710 1944 -1817 C ATOM 806 NZ LYS A1104 79.802 -67.436 -2.336 1.00131.74 N ANISOU 806 NZ LYS A1104 16425 12527 21104 206 1597 -2014 N ATOM 807 N TYR A1105 86.687 -63.442 -2.943 1.00 97.77 N ANISOU 807 N TYR A1105 10879 10161 16107 1882 2231 -503 N ATOM 808 CA TYR A1105 87.271 -62.294 -3.658 1.00 98.39 C ANISOU 808 CA TYR A1105 10765 10691 15927 1815 2332 -378 C ATOM 809 C TYR A1105 88.640 -61.786 -3.111 1.00104.12 C ANISOU 809 C TYR A1105 10976 11636 16949 1997 2457 -65 C ATOM 810 O TYR A1105 89.015 -60.648 -3.415 1.00103.65 O ANISOU 810 O TYR A1105 10695 11876 16811 1827 2501 111 O ATOM 811 CB TYR A1105 86.252 -61.133 -3.718 1.00 95.94 C ANISOU 811 CB TYR A1105 10522 10581 15349 1454 2005 -255 C ATOM 812 CG TYR A1105 85.008 -61.518 -4.489 1.00 99.26 C ANISOU 812 CG TYR A1105 11334 10979 15400 1284 1880 -583 C ATOM 813 CD1 TYR A1105 84.971 -61.434 -5.878 1.00105.20 C ANISOU 813 CD1 TYR A1105 12286 12031 15654 1300 2065 -795 C ATOM 814 CD2 TYR A1105 83.902 -62.063 -3.840 1.00 98.48 C ANISOU 814 CD2 TYR A1105 11371 10614 15433 1116 1596 -712 C ATOM 815 CE1 TYR A1105 83.853 -61.857 -6.600 1.00109.10 C ANISOU 815 CE1 TYR A1105 13080 12618 15756 1144 1894 -1189 C ATOM 816 CE2 TYR A1105 82.778 -62.486 -4.549 1.00101.32 C ANISOU 816 CE2 TYR A1105 11997 10996 15502 911 1462 -1092 C ATOM 817 CZ TYR A1105 82.756 -62.378 -5.930 1.00113.79 C ANISOU 817 CZ TYR A1105 13746 12933 16556 922 1574 -1363 C ATOM 818 OH TYR A1105 81.648 -62.796 -6.629 1.00117.68 O ANISOU 818 OH TYR A1105 14439 13565 16708 709 1375 -1812 O ATOM 819 N LEU A1106 89.419 -62.647 -2.404 1.00102.83 N ANISOU 819 N LEU A1106 10599 11335 17138 2356 2556 5 N ATOM 820 CA LEU A1106 90.761 -62.307 -1.908 1.00126.11 C ANISOU 820 CA LEU A1106 12962 14593 20360 2567 2645 246 C ATOM 821 C LEU A1106 91.719 -63.484 -2.105 1.00150.78 C ANISOU 821 C LEU A1106 15983 17601 23707 3101 3030 198 C ATOM 822 O LEU A1106 92.617 -63.424 -2.946 1.00114.95 O ANISOU 822 O LEU A1106 11251 13276 19151 3258 3428 135 O ATOM 823 CB LEU A1106 90.743 -61.880 -0.421 1.00123.54 C ANISOU 823 CB LEU A1106 12302 14411 20229 2510 2207 492 C ATOM 824 CG LEU A1106 90.712 -60.371 -0.044 1.00125.45 C ANISOU 824 CG LEU A1106 12250 14958 20458 2087 1939 570 C ATOM 825 CD1 LEU A1106 91.840 -59.571 -0.699 1.00128.86 C ANISOU 825 CD1 LEU A1106 12247 15696 21017 1986 2229 603 C ATOM 826 CD2 LEU A1106 89.338 -59.742 -0.244 1.00122.89 C ANISOU 826 CD2 LEU A1106 12354 14454 19884 1710 1733 504 C ATOM 827 N PRO A 39 92.065 -73.783 -7.192 1.00103.88 N ANISOU 827 N PRO A 39 10689 12868 15912 -330 -1890 376 N ATOM 828 CA PRO A 39 91.281 -74.748 -6.405 1.00103.94 C ANISOU 828 CA PRO A 39 10598 12785 16110 -446 -1909 287 C ATOM 829 C PRO A 39 92.109 -75.937 -5.901 1.00106.48 C ANISOU 829 C PRO A 39 11041 12977 16439 -538 -1848 124 C ATOM 830 O PRO A 39 93.243 -76.138 -6.332 1.00106.10 O ANISOU 830 O PRO A 39 11152 12932 16229 -520 -1823 52 O ATOM 831 CB PRO A 39 90.197 -75.225 -7.389 1.00108.03 C ANISOU 831 CB PRO A 39 10979 13457 16611 -497 -2138 237 C ATOM 832 CG PRO A 39 90.393 -74.419 -8.674 1.00113.42 C ANISOU 832 CG PRO A 39 11693 14340 17063 -386 -2236 318 C ATOM 833 CD PRO A 39 91.316 -73.285 -8.359 1.00107.30 C ANISOU 833 CD PRO A 39 11022 13503 16244 -269 -2052 463 C ATOM 834 N SER A 40 91.520 -76.744 -5.007 1.00101.87 N ANISOU 834 N SER A 40 10370 12281 16054 -629 -1816 82 N ATOM 835 CA SER A 40 92.151 -77.946 -4.467 1.00100.68 C ANISOU 835 CA SER A 40 10304 11998 15953 -715 -1753 -46 C ATOM 836 C SER A 40 92.440 -78.967 -5.575 1.00103.57 C ANISOU 836 C SER A 40 10735 12408 16210 -785 -1904 -233 C ATOM 837 O SER A 40 93.384 -79.750 -5.463 1.00101.68 O ANISOU 837 O SER A 40 10623 12079 15933 -817 -1844 -340 O ATOM 838 CB SER A 40 91.249 -78.567 -3.412 1.00105.88 C ANISOU 838 CB SER A 40 10818 12546 16865 -791 -1698 -18 C ATOM 839 OG SER A 40 91.163 -77.713 -2.285 1.00115.00 O ANISOU 839 OG SER A 40 11945 13658 18093 -713 -1532 128 O ATOM 840 N ASP A 41 91.644 -78.906 -6.666 1.00101.03 N ANISOU 840 N ASP A 41 10323 12238 15826 -798 -2101 -274 N ATOM 841 CA ASP A 41 91.742 -79.746 -7.853 1.00101.53 C ANISOU 841 CA ASP A 41 10430 12388 15758 -853 -2277 -472 C ATOM 842 C ASP A 41 93.037 -79.441 -8.657 1.00102.24 C ANISOU 842 C ASP A 41 10722 12565 15561 -758 -2248 -508 C ATOM 843 O ASP A 41 93.221 -80.006 -9.737 1.00104.17 O ANISOU 843 O ASP A 41 11025 12914 15641 -772 -2384 -673 O ATOM 844 CB ASP A 41 90.487 -79.601 -8.719 1.00105.57 C ANISOU 844 CB ASP A 41 10772 13073 16266 -875 -2501 -486 C ATOM 845 N LYS A 42 93.957 -78.604 -8.114 1.00 93.25 N ANISOU 845 N LYS A 42 9684 11377 14368 -665 -2068 -368 N ATOM 846 CA LYS A 42 95.288 -78.378 -8.691 1.00 90.42 C ANISOU 846 CA LYS A 42 9507 11063 13787 -583 -2003 -384 C ATOM 847 C LYS A 42 96.251 -79.508 -8.261 1.00 88.62 C ANISOU 847 C LYS A 42 9400 10677 13593 -644 -1911 -531 C ATOM 848 O LYS A 42 97.449 -79.457 -8.556 1.00 87.00 O ANISOU 848 O LYS A 42 9341 10476 13240 -585 -1829 -546 O ATOM 849 CB LYS A 42 95.856 -77.018 -8.260 1.00 91.07 C ANISOU 849 CB LYS A 42 9622 11137 13844 -470 -1853 -179 C ATOM 850 CG LYS A 42 95.194 -75.836 -8.945 1.00109.91 C ANISOU 850 CG LYS A 42 11918 13685 16156 -376 -1926 -18 C ATOM 851 CD LYS A 42 95.949 -74.521 -8.724 1.00121.30 C ANISOU 851 CD LYS A 42 13412 15103 17575 -261 -1772 166 C ATOM 852 CE LYS A 42 95.443 -73.646 -7.594 1.00133.02 C ANISOU 852 CE LYS A 42 14797 16475 19271 -243 -1664 301 C ATOM 853 NZ LYS A 42 95.908 -74.132 -6.269 1.00139.15 N ANISOU 853 NZ LYS A 42 15617 17069 20186 -306 -1532 230 N ATOM 854 N HIS A 43 95.701 -80.537 -7.579 1.00 82.28 N ANISOU 854 N HIS A 43 8523 9735 13004 -760 -1919 -622 N ATOM 855 CA HIS A 43 96.361 -81.726 -7.036 1.00 79.82 C ANISOU 855 CA HIS A 43 8284 9248 12794 -829 -1832 -740 C ATOM 856 C HIS A 43 97.152 -82.513 -8.077 1.00 82.94 C ANISOU 856 C HIS A 43 8815 9674 13025 -829 -1888 -934 C ATOM 857 O HIS A 43 96.732 -82.641 -9.229 1.00 84.58 O ANISOU 857 O HIS A 43 9013 10024 13098 -833 -2055 -1056 O ATOM 858 CB HIS A 43 95.326 -82.666 -6.392 1.00 80.59 C ANISOU 858 CB HIS A 43 8236 9218 13168 -954 -1867 -792 C ATOM 859 CG HIS A 43 95.896 -83.907 -5.770 1.00 83.00 C ANISOU 859 CG HIS A 43 8590 9324 13621 -1021 -1765 -880 C ATOM 860 ND1 HIS A 43 96.172 -85.034 -6.524 1.00 85.69 N ANISOU 860 ND1 HIS A 43 8990 9612 13958 -1084 -1841 -1098 N ATOM 861 CD2 HIS A 43 96.224 -84.155 -4.481 1.00 83.00 C ANISOU 861 CD2 HIS A 43 8584 9179 13773 -1024 -1592 -771 C ATOM 862 CE1 HIS A 43 96.666 -85.920 -5.676 1.00 84.33 C ANISOU 862 CE1 HIS A 43 8842 9245 13956 -1122 -1704 -1099 C ATOM 863 NE2 HIS A 43 96.714 -85.440 -4.437 1.00 83.07 N ANISOU 863 NE2 HIS A 43 8642 9036 13885 -1085 -1554 -897 N ATOM 864 N LEU A 44 98.289 -83.061 -7.609 1.00 76.16 N ANISOU 864 N LEU A 44 8073 8683 12179 -819 -1743 -962 N ATOM 865 CA LEU A 44 99.250 -83.917 -8.284 1.00 75.50 C ANISOU 865 CA LEU A 44 8129 8571 11987 -811 -1731 -1132 C ATOM 866 C LEU A 44 99.663 -85.021 -7.324 1.00 76.31 C ANISOU 866 C LEU A 44 8242 8444 12306 -877 -1607 -1172 C ATOM 867 O LEU A 44 99.940 -84.743 -6.160 1.00 73.01 O ANISOU 867 O LEU A 44 7803 7941 11997 -861 -1468 -1013 O ATOM 868 CB LEU A 44 100.488 -83.098 -8.721 1.00 74.55 C ANISOU 868 CB LEU A 44 8147 8552 11626 -682 -1638 -1046 C ATOM 869 CG LEU A 44 100.359 -82.171 -9.939 1.00 79.94 C ANISOU 869 CG LEU A 44 8851 9471 12052 -591 -1741 -1014 C ATOM 870 CD1 LEU A 44 101.437 -81.116 -9.910 1.00 78.03 C ANISOU 870 CD1 LEU A 44 8691 9278 11679 -472 -1603 -838 C ATOM 871 CD2 LEU A 44 100.481 -82.945 -11.244 1.00 84.22 C ANISOU 871 CD2 LEU A 44 9473 10118 12408 -584 -1858 -1237 C ATOM 872 N ASP A 45 99.715 -86.270 -7.804 1.00 74.40 N ANISOU 872 N ASP A 45 8031 8108 12131 -944 -1655 -1383 N ATOM 873 CA ASP A 45 100.146 -87.436 -7.018 1.00 73.88 C ANISOU 873 CA ASP A 45 7974 7809 12288 -999 -1533 -1422 C ATOM 874 C ASP A 45 101.659 -87.404 -6.771 1.00 73.54 C ANISOU 874 C ASP A 45 8075 7730 12138 -903 -1365 -1360 C ATOM 875 O ASP A 45 102.153 -87.959 -5.780 1.00 73.76 O ANISOU 875 O ASP A 45 8099 7599 12327 -911 -1222 -1281 O ATOM 876 CB ASP A 45 99.786 -88.734 -7.761 1.00 79.11 C ANISOU 876 CB ASP A 45 8629 8370 13058 -1094 -1639 -1693 C ATOM 877 CG ASP A 45 98.327 -89.142 -7.807 1.00 98.22 C ANISOU 877 CG ASP A 45 10878 10753 15690 -1223 -1792 -1777 C ATOM 878 OD1 ASP A 45 97.479 -88.403 -7.259 1.00 98.53 O ANISOU 878 OD1 ASP A 45 10791 10855 15792 -1236 -1816 -1609 O ATOM 879 OD2 ASP A 45 98.030 -90.187 -8.405 1.00109.36 O ANISOU 879 OD2 ASP A 45 12273 12070 17211 -1310 -1888 -2018 O ATOM 880 N ALA A 46 102.404 -86.782 -7.703 1.00 65.27 N ANISOU 880 N ALA A 46 7144 6838 10817 -807 -1380 -1385 N ATOM 881 CA ALA A 46 103.856 -86.664 -7.645 1.00 61.44 C ANISOU 881 CA ALA A 46 6785 6343 10217 -711 -1232 -1327 C ATOM 882 C ALA A 46 104.339 -85.960 -6.377 1.00 58.62 C ANISOU 882 C ALA A 46 6398 5950 9926 -674 -1095 -1096 C ATOM 883 O ALA A 46 105.361 -86.364 -5.831 1.00 57.03 O ANISOU 883 O ALA A 46 6250 5653 9767 -640 -961 -1053 O ATOM 884 CB ALA A 46 104.358 -85.929 -8.870 1.00 62.57 C ANISOU 884 CB ALA A 46 7025 6685 10062 -612 -1277 -1355 C ATOM 885 N ILE A 47 103.612 -84.922 -5.907 1.00 52.54 N ANISOU 885 N ILE A 47 5539 5259 9164 -675 -1129 -957 N ATOM 886 CA ILE A 47 103.990 -84.136 -4.731 1.00 49.65 C ANISOU 886 CA ILE A 47 5142 4879 8842 -636 -1016 -767 C ATOM 887 C ILE A 47 104.043 -85.023 -3.450 1.00 53.10 C ANISOU 887 C ILE A 47 5530 5155 9489 -680 -912 -721 C ATOM 888 O ILE A 47 105.131 -85.077 -2.877 1.00 52.11 O ANISOU 888 O ILE A 47 5458 4993 9350 -628 -795 -653 O ATOM 889 CB ILE A 47 103.123 -82.875 -4.569 1.00 52.00 C ANISOU 889 CB ILE A 47 5355 5285 9118 -623 -1073 -653 C ATOM 890 CG1 ILE A 47 103.636 -81.773 -5.496 1.00 52.13 C ANISOU 890 CG1 ILE A 47 5435 5446 8928 -536 -1094 -610 C ATOM 891 CG2 ILE A 47 103.102 -82.372 -3.122 1.00 52.11 C ANISOU 891 CG2 ILE A 47 5304 5250 9244 -613 -970 -506 C ATOM 892 CD1 ILE A 47 102.582 -81.067 -6.226 1.00 62.85 C ANISOU 892 CD1 ILE A 47 6726 6931 10222 -532 -1223 -594 C ATOM 893 N PRO A 48 103.008 -85.802 -3.030 1.00 49.70 N ANISOU 893 N PRO A 48 4999 4629 9255 -766 -944 -749 N ATOM 894 CA PRO A 48 103.169 -86.620 -1.816 1.00 48.64 C ANISOU 894 CA PRO A 48 4819 4353 9309 -785 -821 -665 C ATOM 895 C PRO A 48 104.334 -87.637 -1.863 1.00 52.04 C ANISOU 895 C PRO A 48 5338 4669 9767 -761 -725 -716 C ATOM 896 O PRO A 48 105.050 -87.783 -0.863 1.00 50.86 O ANISOU 896 O PRO A 48 5189 4478 9656 -714 -599 -589 O ATOM 897 CB PRO A 48 101.826 -87.336 -1.719 1.00 51.58 C ANISOU 897 CB PRO A 48 5064 4636 9896 -888 -886 -708 C ATOM 898 CG PRO A 48 100.868 -86.429 -2.353 1.00 56.26 C ANISOU 898 CG PRO A 48 5605 5365 10407 -905 -1025 -732 C ATOM 899 CD PRO A 48 101.615 -85.881 -3.520 1.00 52.14 C ANISOU 899 CD PRO A 48 5208 4962 9639 -845 -1086 -822 C ATOM 900 N ILE A 49 104.548 -88.297 -3.035 1.00 48.13 N ANISOU 900 N ILE A 49 4916 4136 9234 -781 -786 -902 N ATOM 901 CA ILE A 49 105.628 -89.279 -3.247 1.00 47.52 C ANISOU 901 CA ILE A 49 4928 3942 9187 -750 -694 -974 C ATOM 902 C ILE A 49 106.991 -88.613 -3.023 1.00 51.74 C ANISOU 902 C ILE A 49 5545 4558 9554 -641 -593 -862 C ATOM 903 O ILE A 49 107.857 -89.195 -2.368 1.00 51.52 O ANISOU 903 O ILE A 49 5531 4439 9604 -602 -469 -788 O ATOM 904 CB ILE A 49 105.536 -89.906 -4.672 1.00 51.46 C ANISOU 904 CB ILE A 49 5498 4424 9631 -778 -792 -1226 C ATOM 905 CG1 ILE A 49 104.206 -90.704 -4.895 1.00 53.31 C ANISOU 905 CG1 ILE A 49 5632 4552 10071 -904 -905 -1369 C ATOM 906 CG2 ILE A 49 106.768 -90.729 -5.061 1.00 51.57 C ANISOU 906 CG2 ILE A 49 5623 4342 9628 -719 -689 -1313 C ATOM 907 CD1 ILE A 49 103.813 -91.832 -3.842 1.00 58.49 C ANISOU 907 CD1 ILE A 49 6179 4972 11073 -977 -811 -1304 C ATOM 908 N LEU A 50 107.154 -87.380 -3.541 1.00 47.79 N ANISOU 908 N LEU A 50 5083 4228 8846 -593 -647 -836 N ATOM 909 CA LEU A 50 108.376 -86.587 -3.453 1.00 46.31 C ANISOU 909 CA LEU A 50 4956 4124 8514 -501 -569 -736 C ATOM 910 C LEU A 50 108.653 -86.125 -2.027 1.00 48.41 C ANISOU 910 C LEU A 50 5158 4390 8845 -480 -488 -559 C ATOM 911 O LEU A 50 109.813 -85.971 -1.649 1.00 46.92 O ANISOU 911 O LEU A 50 5000 4212 8616 -417 -400 -483 O ATOM 912 CB LEU A 50 108.255 -85.386 -4.386 1.00 46.44 C ANISOU 912 CB LEU A 50 5006 4305 8336 -465 -649 -741 C ATOM 913 CG LEU A 50 109.013 -85.442 -5.703 1.00 52.52 C ANISOU 913 CG LEU A 50 5885 5141 8931 -401 -650 -838 C ATOM 914 CD1 LEU A 50 108.714 -86.704 -6.494 1.00 54.62 C ANISOU 914 CD1 LEU A 50 6197 5333 9224 -438 -695 -1044 C ATOM 915 CD2 LEU A 50 108.681 -84.219 -6.554 1.00 55.93 C ANISOU 915 CD2 LEU A 50 6322 5745 9182 -362 -730 -803 C ATOM 916 N TYR A 51 107.595 -85.940 -1.235 1.00 45.74 N ANISOU 916 N TYR A 51 4724 4049 8605 -529 -518 -499 N ATOM 917 CA TYR A 51 107.697 -85.525 0.159 1.00 45.05 C ANISOU 917 CA TYR A 51 4572 3984 8561 -503 -447 -349 C ATOM 918 C TYR A 51 108.215 -86.684 1.015 1.00 52.27 C ANISOU 918 C TYR A 51 5468 4789 9604 -491 -339 -286 C ATOM 919 O TYR A 51 109.079 -86.496 1.871 1.00 50.69 O ANISOU 919 O TYR A 51 5263 4626 9371 -430 -262 -180 O ATOM 920 CB TYR A 51 106.338 -85.013 0.643 1.00 45.35 C ANISOU 920 CB TYR A 51 4514 4059 8660 -547 -502 -309 C ATOM 921 CG TYR A 51 106.124 -83.540 0.350 1.00 45.85 C ANISOU 921 CG TYR A 51 4576 4246 8598 -520 -562 -291 C ATOM 922 CD1 TYR A 51 106.288 -83.029 -0.937 1.00 48.03 C ANISOU 922 CD1 TYR A 51 4914 4581 8752 -508 -635 -364 C ATOM 923 CD2 TYR A 51 105.716 -82.664 1.347 1.00 45.83 C ANISOU 923 CD2 TYR A 51 4507 4300 8605 -499 -539 -199 C ATOM 924 CE1 TYR A 51 106.116 -81.674 -1.207 1.00 48.21 C ANISOU 924 CE1 TYR A 51 4927 4704 8688 -475 -674 -320 C ATOM 925 CE2 TYR A 51 105.514 -81.310 1.084 1.00 46.16 C ANISOU 925 CE2 TYR A 51 4543 4428 8569 -472 -583 -184 C ATOM 926 CZ TYR A 51 105.718 -80.820 -0.196 1.00 55.78 C ANISOU 926 CZ TYR A 51 5816 5689 9690 -462 -648 -233 C ATOM 927 OH TYR A 51 105.513 -79.492 -0.479 1.00 61.67 O ANISOU 927 OH TYR A 51 6544 6504 10382 -428 -678 -193 O ATOM 928 N TYR A 52 107.748 -87.899 0.713 1.00 52.14 N ANISOU 928 N TYR A 52 5438 4636 9738 -544 -336 -355 N ATOM 929 CA TYR A 52 108.201 -89.087 1.407 1.00 52.87 C ANISOU 929 CA TYR A 52 5506 4598 9986 -529 -222 -285 C ATOM 930 C TYR A 52 109.611 -89.526 0.956 1.00 56.41 C ANISOU 930 C TYR A 52 6044 5008 10380 -464 -154 -316 C ATOM 931 O TYR A 52 110.407 -89.876 1.827 1.00 56.91 O ANISOU 931 O TYR A 52 6087 5055 10481 -403 -51 -185 O ATOM 932 CB TYR A 52 107.204 -90.234 1.218 1.00 56.40 C ANISOU 932 CB TYR A 52 5894 4878 10659 -615 -234 -353 C ATOM 933 CG TYR A 52 106.076 -90.267 2.229 1.00 59.94 C ANISOU 933 CG TYR A 52 6213 5316 11248 -655 -217 -227 C ATOM 934 CD1 TYR A 52 106.221 -90.933 3.444 1.00 62.59 C ANISOU 934 CD1 TYR A 52 6475 5589 11717 -618 -85 -46 C ATOM 935 CD2 TYR A 52 104.827 -89.728 1.928 1.00 61.19 C ANISOU 935 CD2 TYR A 52 6310 5522 11417 -723 -325 -280 C ATOM 936 CE1 TYR A 52 105.173 -90.998 4.364 1.00 63.32 C ANISOU 936 CE1 TYR A 52 6443 5678 11936 -642 -50 86 C ATOM 937 CE2 TYR A 52 103.767 -89.803 2.833 1.00 62.29 C ANISOU 937 CE2 TYR A 52 6320 5646 11702 -755 -294 -157 C ATOM 938 CZ TYR A 52 103.949 -90.427 4.055 1.00 68.66 C ANISOU 938 CZ TYR A 52 7062 6399 12628 -712 -151 27 C ATOM 939 OH TYR A 52 102.913 -90.479 4.952 1.00 71.15 O ANISOU 939 OH TYR A 52 7247 6715 13074 -728 -104 165 O ATOM 940 N ILE A 53 109.933 -89.502 -0.378 1.00 51.45 N ANISOU 940 N ILE A 53 5510 4381 9655 -464 -206 -478 N ATOM 941 CA ILE A 53 111.240 -90.000 -0.860 1.00 50.75 C ANISOU 941 CA ILE A 53 5504 4248 9530 -395 -124 -511 C ATOM 942 C ILE A 53 112.386 -89.166 -0.293 1.00 53.89 C ANISOU 942 C ILE A 53 5905 4765 9804 -312 -68 -370 C ATOM 943 O ILE A 53 113.504 -89.672 -0.210 1.00 53.01 O ANISOU 943 O ILE A 53 5819 4611 9713 -246 27 -327 O ATOM 944 CB ILE A 53 111.430 -90.223 -2.397 1.00 53.80 C ANISOU 944 CB ILE A 53 5996 4625 9821 -391 -169 -715 C ATOM 945 CG1 ILE A 53 111.918 -88.972 -3.133 1.00 53.23 C ANISOU 945 CG1 ILE A 53 5984 4732 9508 -339 -214 -717 C ATOM 946 CG2 ILE A 53 110.242 -90.830 -3.108 1.00 54.61 C ANISOU 946 CG2 ILE A 53 6092 4649 10007 -482 -269 -897 C ATOM 947 CD1 ILE A 53 113.359 -89.072 -3.555 1.00 58.85 C ANISOU 947 CD1 ILE A 53 6769 5454 10138 -245 -113 -703 C ATOM 948 N ILE A 54 112.129 -87.905 0.069 1.00 50.85 N ANISOU 948 N ILE A 54 5489 4521 9310 -314 -127 -306 N ATOM 949 CA ILE A 54 113.187 -87.066 0.637 1.00 50.28 C ANISOU 949 CA ILE A 54 5406 4554 9145 -249 -88 -195 C ATOM 950 C ILE A 54 113.136 -87.105 2.176 1.00 56.10 C ANISOU 950 C ILE A 54 6052 5318 9943 -234 -49 -51 C ATOM 951 O ILE A 54 114.073 -86.646 2.839 1.00 56.43 O ANISOU 951 O ILE A 54 6068 5441 9930 -180 -17 37 O ATOM 952 CB ILE A 54 113.216 -85.610 0.106 1.00 52.05 C ANISOU 952 CB ILE A 54 5649 4905 9222 -245 -158 -213 C ATOM 953 CG1 ILE A 54 112.137 -84.745 0.738 1.00 51.32 C ANISOU 953 CG1 ILE A 54 5493 4877 9128 -287 -227 -182 C ATOM 954 CG2 ILE A 54 113.197 -85.514 -1.418 1.00 53.69 C ANISOU 954 CG2 ILE A 54 5941 5123 9335 -243 -196 -330 C ATOM 955 CD1 ILE A 54 112.710 -83.726 1.647 1.00 61.53 C ANISOU 955 CD1 ILE A 54 6740 6262 10377 -253 -215 -94 C ATOM 956 N PHE A 55 112.045 -87.635 2.734 1.00 52.95 N ANISOU 956 N PHE A 55 5599 4866 9655 -279 -52 -27 N ATOM 957 CA PHE A 55 111.912 -87.750 4.172 1.00 52.84 C ANISOU 957 CA PHE A 55 5499 4895 9683 -250 -1 120 C ATOM 958 C PHE A 55 112.858 -88.826 4.656 1.00 61.30 C ANISOU 958 C PHE A 55 6556 5900 10836 -188 106 222 C ATOM 959 O PHE A 55 113.722 -88.523 5.461 1.00 62.23 O ANISOU 959 O PHE A 55 6643 6121 10881 -120 137 325 O ATOM 960 CB PHE A 55 110.440 -88.041 4.562 1.00 54.48 C ANISOU 960 CB PHE A 55 5640 5058 10001 -309 -17 137 C ATOM 961 CG PHE A 55 110.200 -88.810 5.848 1.00 55.48 C ANISOU 961 CG PHE A 55 5678 5165 10237 -276 78 304 C ATOM 962 CD1 PHE A 55 110.371 -88.202 7.084 1.00 57.18 C ANISOU 962 CD1 PHE A 55 5841 5536 10350 -211 103 426 C ATOM 963 CD2 PHE A 55 109.781 -90.132 5.818 1.00 57.98 C ANISOU 963 CD2 PHE A 55 5958 5310 10761 -305 145 337 C ATOM 964 CE1 PHE A 55 110.146 -88.906 8.266 1.00 58.34 C ANISOU 964 CE1 PHE A 55 5904 5694 10569 -161 199 600 C ATOM 965 CE2 PHE A 55 109.548 -90.836 7.004 1.00 61.13 C ANISOU 965 CE2 PHE A 55 6264 5692 11271 -263 250 526 C ATOM 966 CZ PHE A 55 109.734 -90.218 8.219 1.00 58.39 C ANISOU 966 CZ PHE A 55 5869 5528 10789 -185 279 667 C ATOM 967 N VAL A 56 112.723 -90.056 4.135 1.00 60.13 N ANISOU 967 N VAL A 56 6425 5578 10845 -209 158 183 N ATOM 968 CA VAL A 56 113.506 -91.219 4.545 1.00 61.86 C ANISOU 968 CA VAL A 56 6622 5694 11189 -147 276 289 C ATOM 969 C VAL A 56 114.997 -90.994 4.330 1.00 66.87 C ANISOU 969 C VAL A 56 7296 6389 11723 -68 309 309 C ATOM 970 O VAL A 56 115.798 -91.349 5.192 1.00 66.99 O ANISOU 970 O VAL A 56 7257 6440 11756 11 383 465 O ATOM 971 CB VAL A 56 113.017 -92.521 3.856 1.00 67.64 C ANISOU 971 CB VAL A 56 7369 6194 12137 -196 321 201 C ATOM 972 CG1 VAL A 56 111.744 -93.038 4.518 1.00 68.32 C ANISOU 972 CG1 VAL A 56 7363 6200 12396 -254 337 272 C ATOM 973 CG2 VAL A 56 112.798 -92.336 2.357 1.00 67.69 C ANISOU 973 CG2 VAL A 56 7474 6156 12090 -256 236 -37 C ATOM 974 N ILE A 57 115.352 -90.370 3.203 1.00 63.75 N ANISOU 974 N ILE A 57 6984 6020 11217 -83 254 166 N ATOM 975 CA ILE A 57 116.728 -90.073 2.825 1.00 63.57 C ANISOU 975 CA ILE A 57 6994 6050 11109 -14 287 177 C ATOM 976 C ILE A 57 117.344 -89.129 3.849 1.00 65.30 C ANISOU 976 C ILE A 57 7143 6444 11222 27 262 301 C ATOM 977 O ILE A 57 118.402 -89.439 4.399 1.00 65.05 O ANISOU 977 O ILE A 57 7067 6444 11206 101 323 415 O ATOM 978 CB ILE A 57 116.769 -89.499 1.366 1.00 67.01 C ANISOU 978 CB ILE A 57 7527 6496 11437 -39 235 10 C ATOM 979 CG1 ILE A 57 116.523 -90.595 0.289 1.00 69.61 C ANISOU 979 CG1 ILE A 57 7933 6662 11854 -53 271 -138 C ATOM 980 CG2 ILE A 57 118.037 -88.686 1.045 1.00 66.98 C ANISOU 980 CG2 ILE A 57 7536 6596 11317 22 250 43 C ATOM 981 CD1 ILE A 57 117.500 -91.844 0.257 1.00 83.91 C ANISOU 981 CD1 ILE A 57 9753 8332 13797 22 407 -104 C ATOM 982 N GLY A 58 116.657 -88.017 4.098 1.00 59.88 N ANISOU 982 N GLY A 58 6443 5867 10441 -20 170 268 N ATOM 983 CA GLY A 58 117.080 -86.992 5.033 1.00 58.86 C ANISOU 983 CA GLY A 58 6251 5899 10212 5 126 335 C ATOM 984 C GLY A 58 117.241 -87.534 6.430 1.00 63.60 C ANISOU 984 C GLY A 58 6766 6562 10836 61 170 486 C ATOM 985 O GLY A 58 118.192 -87.186 7.130 1.00 64.04 O ANISOU 985 O GLY A 58 6767 6738 10828 117 163 559 O ATOM 986 N PHE A 59 116.313 -88.387 6.839 1.00 60.04 N ANISOU 986 N PHE A 59 6295 6038 10480 50 213 539 N ATOM 987 CA PHE A 59 116.329 -88.977 8.161 1.00 61.04 C ANISOU 987 CA PHE A 59 6336 6229 10628 117 272 713 C ATOM 988 C PHE A 59 117.506 -89.907 8.288 1.00 65.87 C ANISOU 988 C PHE A 59 6921 6799 11306 199 359 830 C ATOM 989 O PHE A 59 118.167 -89.912 9.327 1.00 65.89 O ANISOU 989 O PHE A 59 6847 6943 11244 280 373 970 O ATOM 990 CB PHE A 59 115.009 -89.718 8.426 1.00 64.07 C ANISOU 990 CB PHE A 59 6694 6512 11136 81 316 758 C ATOM 991 CG PHE A 59 114.401 -89.416 9.768 1.00 66.68 C ANISOU 991 CG PHE A 59 6946 6995 11394 119 321 878 C ATOM 992 CD1 PHE A 59 113.612 -88.288 9.954 1.00 69.49 C ANISOU 992 CD1 PHE A 59 7304 7457 11641 79 240 791 C ATOM 993 CD2 PHE A 59 114.601 -90.270 10.849 1.00 70.55 C ANISOU 993 CD2 PHE A 59 7356 7528 11924 209 418 1087 C ATOM 994 CE1 PHE A 59 113.049 -88.008 11.206 1.00 71.12 C ANISOU 994 CE1 PHE A 59 7442 7815 11764 129 257 892 C ATOM 995 CE2 PHE A 59 114.039 -89.989 12.098 1.00 73.83 C ANISOU 995 CE2 PHE A 59 7699 8111 12240 263 432 1204 C ATOM 996 CZ PHE A 59 113.266 -88.859 12.268 1.00 71.02 C ANISOU 996 CZ PHE A 59 7354 7864 11764 222 352 1095 C ATOM 997 N LEU A 60 117.780 -90.674 7.213 1.00 62.98 N ANISOU 997 N LEU A 60 6616 6251 11063 185 415 766 N ATOM 998 CA LEU A 60 118.887 -91.614 7.161 1.00 63.40 C ANISOU 998 CA LEU A 60 6650 6230 11209 267 515 864 C ATOM 999 C LEU A 60 120.197 -90.861 7.192 1.00 65.50 C ANISOU 999 C LEU A 60 6894 6639 11352 318 479 879 C ATOM 1000 O LEU A 60 121.080 -91.176 7.995 1.00 66.36 O ANISOU 1000 O LEU A 60 6922 6835 11459 407 517 1037 O ATOM 1001 CB LEU A 60 118.805 -92.496 5.906 1.00 64.28 C ANISOU 1001 CB LEU A 60 6844 6110 11469 237 579 743 C ATOM 1002 CG LEU A 60 117.951 -93.776 5.993 1.00 71.12 C ANISOU 1002 CG LEU A 60 7694 6772 12555 217 664 777 C ATOM 1003 CD1 LEU A 60 117.913 -94.490 4.649 1.00 71.96 C ANISOU 1003 CD1 LEU A 60 7892 6664 12785 180 701 594 C ATOM 1004 CD2 LEU A 60 118.444 -94.735 7.077 1.00 76.45 C ANISOU 1004 CD2 LEU A 60 8269 7427 13352 318 783 1024 C ATOM 1005 N VAL A 61 120.294 -89.821 6.355 1.00 58.97 N ANISOU 1005 N VAL A 61 6128 5849 10428 263 401 728 N ATOM 1006 CA VAL A 61 121.533 -89.088 6.314 1.00 57.88 C ANISOU 1006 CA VAL A 61 5956 5825 10212 300 372 742 C ATOM 1007 C VAL A 61 121.793 -88.407 7.652 1.00 60.34 C ANISOU 1007 C VAL A 61 6165 6341 10420 328 300 831 C ATOM 1008 O VAL A 61 122.931 -88.465 8.118 1.00 60.32 O ANISOU 1008 O VAL A 61 6083 6428 10406 396 308 929 O ATOM 1009 CB VAL A 61 121.762 -88.132 5.129 1.00 61.14 C ANISOU 1009 CB VAL A 61 6437 6230 10564 251 328 599 C ATOM 1010 CG1 VAL A 61 122.041 -88.911 3.853 1.00 61.14 C ANISOU 1010 CG1 VAL A 61 6522 6072 10636 269 418 534 C ATOM 1011 CG2 VAL A 61 120.654 -87.098 4.940 1.00 60.11 C ANISOU 1011 CG2 VAL A 61 6347 6139 10355 164 230 483 C ATOM 1012 N ASN A 62 120.764 -87.843 8.302 1.00 55.03 N ANISOU 1012 N ASN A 62 5486 5749 9674 285 232 798 N ATOM 1013 CA ASN A 62 120.957 -87.185 9.589 1.00 53.64 C ANISOU 1013 CA ASN A 62 5221 5782 9376 319 160 852 C ATOM 1014 C ASN A 62 121.212 -88.177 10.732 1.00 54.99 C ANISOU 1014 C ASN A 62 5307 6034 9551 421 222 1050 C ATOM 1015 O ASN A 62 121.976 -87.855 11.644 1.00 53.89 O ANISOU 1015 O ASN A 62 5079 6084 9311 482 171 1118 O ATOM 1016 CB ASN A 62 119.802 -86.277 9.894 1.00 54.02 C ANISOU 1016 CB ASN A 62 5291 5889 9343 258 87 751 C ATOM 1017 CG ASN A 62 119.861 -85.013 9.061 1.00 73.11 C ANISOU 1017 CG ASN A 62 7753 8291 11734 183 9 588 C ATOM 1018 OD1 ASN A 62 120.810 -84.227 9.148 1.00 62.18 O ANISOU 1018 OD1 ASN A 62 6323 6990 10313 186 -46 555 O ATOM 1019 ND2 ASN A 62 118.857 -84.767 8.244 1.00 67.06 N ANISOU 1019 ND2 ASN A 62 7062 7419 10998 114 2 493 N ATOM 1020 N ILE A 63 120.643 -89.386 10.663 1.00 52.13 N ANISOU 1020 N ILE A 63 4962 5529 9315 442 330 1149 N ATOM 1021 CA ILE A 63 120.900 -90.355 11.727 1.00 54.10 C ANISOU 1021 CA ILE A 63 5122 5847 9587 552 408 1374 C ATOM 1022 C ILE A 63 122.349 -90.819 11.664 1.00 58.65 C ANISOU 1022 C ILE A 63 5642 6438 10205 635 445 1478 C ATOM 1023 O ILE A 63 122.946 -91.116 12.708 1.00 59.39 O ANISOU 1023 O ILE A 63 5631 6697 10237 739 452 1655 O ATOM 1024 CB ILE A 63 119.922 -91.564 11.821 1.00 58.38 C ANISOU 1024 CB ILE A 63 5669 6222 10292 560 530 1488 C ATOM 1025 CG1 ILE A 63 119.927 -92.475 10.578 1.00 60.11 C ANISOU 1025 CG1 ILE A 63 5958 6154 10726 520 619 1425 C ATOM 1026 CG2 ILE A 63 118.496 -91.158 12.190 1.00 57.70 C ANISOU 1026 CG2 ILE A 63 5596 6164 10162 501 501 1441 C ATOM 1027 CD1 ILE A 63 120.912 -93.746 10.665 1.00 75.06 C ANISOU 1027 CD1 ILE A 63 7797 7945 12777 628 752 1609 C ATOM 1028 N VAL A 64 122.901 -90.876 10.440 1.00 53.88 N ANISOU 1028 N VAL A 64 5101 5677 9695 598 472 1374 N ATOM 1029 CA VAL A 64 124.277 -91.288 10.198 1.00 54.34 C ANISOU 1029 CA VAL A 64 5108 5725 9813 675 522 1460 C ATOM 1030 C VAL A 64 125.195 -90.337 10.959 1.00 57.48 C ANISOU 1030 C VAL A 64 5404 6376 10059 705 405 1483 C ATOM 1031 O VAL A 64 126.138 -90.807 11.575 1.00 59.10 O ANISOU 1031 O VAL A 64 5503 6680 10272 806 427 1650 O ATOM 1032 CB VAL A 64 124.594 -91.396 8.673 1.00 57.50 C ANISOU 1032 CB VAL A 64 5606 5924 10316 631 576 1319 C ATOM 1033 CG1 VAL A 64 126.080 -91.184 8.368 1.00 57.35 C ANISOU 1033 CG1 VAL A 64 5528 5958 10302 687 585 1358 C ATOM 1034 CG2 VAL A 64 124.113 -92.735 8.111 1.00 57.99 C ANISOU 1034 CG2 VAL A 64 5730 5739 10565 645 714 1339 C ATOM 1035 N VAL A 65 124.891 -89.034 10.968 1.00 51.63 N ANISOU 1035 N VAL A 65 4683 5739 9194 621 278 1321 N ATOM 1036 CA VAL A 65 125.678 -88.000 11.661 1.00 51.57 C ANISOU 1036 CA VAL A 65 4578 5957 9061 627 148 1291 C ATOM 1037 C VAL A 65 125.667 -88.241 13.166 1.00 58.83 C ANISOU 1037 C VAL A 65 5396 7105 9853 718 107 1432 C ATOM 1038 O VAL A 65 126.700 -88.178 13.846 1.00 59.45 O ANISOU 1038 O VAL A 65 5354 7363 9873 788 50 1519 O ATOM 1039 CB VAL A 65 125.124 -86.579 11.317 1.00 53.41 C ANISOU 1039 CB VAL A 65 4866 6206 9222 512 38 1073 C ATOM 1040 CG1 VAL A 65 125.710 -85.489 12.201 1.00 53.95 C ANISOU 1040 CG1 VAL A 65 4831 6497 9172 507 -106 1010 C ATOM 1041 CG2 VAL A 65 125.288 -86.235 9.844 1.00 52.01 C ANISOU 1041 CG2 VAL A 65 4772 5846 9144 441 73 960 C ATOM 1042 N VAL A 66 124.478 -88.477 13.674 1.00 57.73 N ANISOU 1042 N VAL A 66 5297 6973 9664 719 134 1454 N ATOM 1043 CA VAL A 66 124.244 -88.690 15.085 1.00 59.69 C ANISOU 1043 CA VAL A 66 5465 7448 9766 813 114 1592 C ATOM 1044 C VAL A 66 125.019 -89.934 15.541 1.00 68.39 C ANISOU 1044 C VAL A 66 6473 8581 10932 948 210 1859 C ATOM 1045 O VAL A 66 125.734 -89.881 16.550 1.00 68.65 O ANISOU 1045 O VAL A 66 6389 8866 10829 1045 145 1971 O ATOM 1046 CB VAL A 66 122.708 -88.760 15.272 1.00 62.36 C ANISOU 1046 CB VAL A 66 5876 7730 10088 778 160 1568 C ATOM 1047 CG1 VAL A 66 122.265 -89.804 16.283 1.00 63.91 C ANISOU 1047 CG1 VAL A 66 6012 8005 10264 895 261 1817 C ATOM 1048 CG2 VAL A 66 122.140 -87.378 15.580 1.00 60.77 C ANISOU 1048 CG2 VAL A 66 5701 7658 9729 708 33 1362 C ATOM 1049 N THR A 67 124.925 -91.011 14.752 1.00 68.32 N ANISOU 1049 N THR A 67 6512 8313 11133 955 357 1946 N ATOM 1050 CA THR A 67 125.618 -92.258 15.042 1.00 71.20 C ANISOU 1050 CA THR A 67 6793 8647 11612 1083 476 2203 C ATOM 1051 C THR A 67 127.121 -92.111 14.866 1.00 77.28 C ANISOU 1051 C THR A 67 7477 9494 12391 1130 432 2232 C ATOM 1052 O THR A 67 127.877 -92.713 15.630 1.00 78.18 O ANISOU 1052 O THR A 67 7467 9747 12489 1261 456 2457 O ATOM 1053 CB THR A 67 125.092 -93.409 14.203 1.00 80.01 C ANISOU 1053 CB THR A 67 7985 9438 12978 1068 646 2250 C ATOM 1054 OG1 THR A 67 124.986 -93.005 12.849 1.00 82.11 O ANISOU 1054 OG1 THR A 67 8368 9502 13327 949 635 2014 O ATOM 1055 CG2 THR A 67 123.752 -93.937 14.708 1.00 77.11 C ANISOU 1055 CG2 THR A 67 7638 9014 12647 1067 721 2335 C ATOM 1056 N LEU A 68 127.571 -91.322 13.881 1.00 74.69 N ANISOU 1056 N LEU A 68 7200 9085 12093 1033 372 2030 N ATOM 1057 CA LEU A 68 129.002 -91.206 13.709 1.00 76.49 C ANISOU 1057 CA LEU A 68 7329 9379 12356 1078 343 2075 C ATOM 1058 C LEU A 68 129.601 -90.393 14.865 1.00 86.58 C ANISOU 1058 C LEU A 68 8469 10991 13436 1113 172 2089 C ATOM 1059 O LEU A 68 130.670 -90.772 15.340 1.00 87.86 O ANISOU 1059 O LEU A 68 8494 11287 13604 1215 161 2254 O ATOM 1060 CB LEU A 68 129.459 -90.742 12.329 1.00 74.81 C ANISOU 1060 CB LEU A 68 7186 8985 12254 992 361 1907 C ATOM 1061 CG LEU A 68 129.279 -89.333 11.886 1.00 77.99 C ANISOU 1061 CG LEU A 68 7636 9422 12577 864 236 1671 C ATOM 1062 CD1 LEU A 68 130.561 -88.529 12.101 1.00 78.65 C ANISOU 1062 CD1 LEU A 68 7581 9669 12633 866 124 1658 C ATOM 1063 CD2 LEU A 68 128.950 -89.312 10.416 1.00 79.32 C ANISOU 1063 CD2 LEU A 68 7942 9338 12856 788 322 1535 C ATOM 1064 N PHE A 69 128.881 -89.403 15.415 1.00 86.83 N ANISOU 1064 N PHE A 69 8528 11169 13294 1045 44 1933 N ATOM 1065 CA PHE A 69 129.356 -88.694 16.604 1.00 90.07 C ANISOU 1065 CA PHE A 69 8813 11910 13501 1085 -124 1920 C ATOM 1066 C PHE A 69 129.510 -89.686 17.759 1.00100.28 C ANISOU 1066 C PHE A 69 10001 13400 14700 1252 -82 2199 C ATOM 1067 O PHE A 69 130.494 -89.616 18.509 1.00100.01 O ANISOU 1067 O PHE A 69 9817 13614 14567 1336 -182 2290 O ATOM 1068 CB PHE A 69 128.386 -87.557 16.967 1.00 91.52 C ANISOU 1068 CB PHE A 69 9064 12183 13526 994 -237 1694 C ATOM 1069 CG PHE A 69 128.629 -86.261 16.225 1.00 92.82 C ANISOU 1069 CG PHE A 69 9257 12272 13737 853 -341 1433 C ATOM 1070 CD1 PHE A 69 129.388 -86.236 15.057 1.00 95.88 C ANISOU 1070 CD1 PHE A 69 9651 12467 14312 801 -293 1410 C ATOM 1071 CD2 PHE A 69 128.101 -85.069 16.691 1.00 95.51 C ANISOU 1071 CD2 PHE A 69 9614 12730 13945 782 -472 1219 C ATOM 1072 CE1 PHE A 69 129.631 -85.042 14.384 1.00 96.07 C ANISOU 1072 CE1 PHE A 69 9686 12423 14395 681 -372 1205 C ATOM 1073 CE2 PHE A 69 128.333 -83.870 16.008 1.00 97.88 C ANISOU 1073 CE2 PHE A 69 9928 12938 14323 655 -554 998 C ATOM 1074 CZ PHE A 69 129.109 -83.865 14.864 1.00 95.46 C ANISOU 1074 CZ PHE A 69 9617 12446 14209 606 -503 1005 C ATOM 1075 N CYS A 70 128.548 -90.652 17.863 1.00101.74 N ANISOU 1075 N CYS A 70 10255 13465 14936 1303 71 2350 N ATOM 1076 CA CYS A 70 128.560 -91.717 18.879 1.00105.32 C ANISOU 1076 CA CYS A 70 10615 14062 15339 1472 154 2661 C ATOM 1077 C CYS A 70 129.812 -92.563 18.736 1.00115.26 C ANISOU 1077 C CYS A 70 11759 15297 16738 1579 219 2877 C ATOM 1078 O CYS A 70 130.468 -92.861 19.724 1.00117.13 O ANISOU 1078 O CYS A 70 11850 15801 16854 1718 175 3081 O ATOM 1079 CB CYS A 70 127.302 -92.582 18.787 1.00105.30 C ANISOU 1079 CB CYS A 70 10705 13859 15446 1481 327 2771 C ATOM 1080 SG CYS A 70 126.187 -92.457 20.208 1.00110.37 S ANISOU 1080 SG CYS A 70 11328 14778 15832 1560 311 2868 S ATOM 1081 N CYS A 71 130.140 -92.966 17.488 1.00114.66 N ANISOU 1081 N CYS A 71 11745 14907 16913 1524 329 2836 N ATOM 1082 CA CYS A 71 131.317 -93.793 17.183 1.00117.51 C ANISOU 1082 CA CYS A 71 12007 15195 17445 1624 419 3026 C ATOM 1083 C CYS A 71 132.589 -93.026 17.493 1.00124.94 C ANISOU 1083 C CYS A 71 12803 16386 18282 1639 251 2992 C ATOM 1084 O CYS A 71 133.549 -93.612 17.998 1.00126.89 O ANISOU 1084 O CYS A 71 12896 16768 18550 1775 262 3225 O ATOM 1085 CB CYS A 71 131.300 -94.259 15.729 1.00116.92 C ANISOU 1085 CB CYS A 71 12051 14740 17634 1556 569 2935 C ATOM 1086 SG CYS A 71 129.971 -95.425 15.324 1.00120.73 S ANISOU 1086 SG CYS A 71 12669 14896 18308 1550 778 2995 S ATOM 1087 N GLN A 72 132.600 -91.718 17.180 1.00121.61 N ANISOU 1087 N GLN A 72 12418 16016 17772 1498 95 2708 N ATOM 1088 CA GLN A 72 133.747 -90.867 17.435 1.00122.69 C ANISOU 1088 CA GLN A 72 12409 16366 17840 1483 -79 2635 C ATOM 1089 C GLN A 72 134.012 -90.814 18.938 1.00129.30 C ANISOU 1089 C GLN A 72 13096 17597 18437 1597 -221 2761 C ATOM 1090 O GLN A 72 135.168 -90.969 19.346 1.00130.35 O ANISOU 1090 O GLN A 72 13051 17910 18566 1684 -290 2898 O ATOM 1091 CB GLN A 72 133.553 -89.461 16.838 1.00122.52 C ANISOU 1091 CB GLN A 72 12461 16296 17797 1304 -203 2307 C ATOM 1092 CG GLN A 72 134.795 -88.543 16.927 1.00137.88 C ANISOU 1092 CG GLN A 72 14244 18402 19743 1263 -373 2213 C ATOM 1093 CD GLN A 72 136.127 -89.251 16.753 1.00153.99 C ANISOU 1093 CD GLN A 72 16129 20451 21930 1365 -317 2429 C ATOM 1094 OE1 GLN A 72 136.419 -89.849 15.710 1.00148.86 O ANISOU 1094 OE1 GLN A 72 15529 19543 21488 1376 -147 2499 O ATOM 1095 NE2 GLN A 72 136.958 -89.208 17.786 1.00143.89 N ANISOU 1095 NE2 GLN A 72 14653 19481 20539 1451 -461 2536 N ATOM 1096 N LYS A 73 132.948 -90.644 19.760 1.00126.57 N ANISOU 1096 N LYS A 73 12811 17393 17886 1609 -257 2730 N ATOM 1097 CA LYS A 73 133.106 -90.648 21.219 1.00156.70 C ANISOU 1097 CA LYS A 73 16496 21611 21432 1740 -379 2857 C ATOM 1098 C LYS A 73 131.947 -91.386 21.912 1.00189.32 C ANISOU 1098 C LYS A 73 20696 25783 25455 1840 -255 3037 C ATOM 1099 O LYS A 73 130.911 -90.811 22.257 1.00150.84 O ANISOU 1099 O LYS A 73 15919 20968 20426 1786 -293 2883 O ATOM 1100 CB LYS A 73 133.309 -89.231 21.815 1.00159.22 C ANISOU 1100 CB LYS A 73 16761 22206 21528 1658 -636 2571 C ATOM 1101 CG LYS A 73 134.781 -88.802 21.951 1.00168.91 C ANISOU 1101 CG LYS A 73 17794 23613 22771 1662 -805 2547 C ATOM 1102 CD LYS A 73 135.520 -89.474 23.122 1.00177.01 C ANISOU 1102 CD LYS A 73 18628 25003 23627 1858 -872 2824 C ATOM 1103 CE LYS A 73 136.784 -90.186 22.692 1.00181.45 C ANISOU 1103 CE LYS A 73 19040 25500 24402 1931 -815 3049 C ATOM 1104 NZ LYS A 73 137.905 -89.242 22.441 1.00186.29 N ANISOU 1104 NZ LYS A 73 19513 26186 25081 1829 -1005 2857 N ATOM 1105 N LYS A 77 134.475 -80.589 20.437 1.00114.95 N ANISOU 1105 N LYS A 77 11054 16483 16140 688 -1629 555 N ATOM 1106 CA LYS A 77 134.700 -79.272 19.848 1.00113.77 C ANISOU 1106 CA LYS A 77 10878 16160 16187 516 -1713 286 C ATOM 1107 C LYS A 77 133.410 -78.447 19.797 1.00114.84 C ANISOU 1107 C LYS A 77 11182 16182 16270 439 -1696 57 C ATOM 1108 O LYS A 77 132.308 -78.998 19.733 1.00113.44 O ANISOU 1108 O LYS A 77 11169 15946 15986 495 -1559 145 O ATOM 1109 CB LYS A 77 135.309 -79.396 18.442 1.00114.58 C ANISOU 1109 CB LYS A 77 10975 15956 16603 448 -1574 401 C ATOM 1110 N VAL A 78 133.572 -77.115 19.818 1.00110.31 N ANISOU 1110 N VAL A 78 10551 15563 15798 308 -1833 -234 N ATOM 1111 CA VAL A 78 132.487 -76.132 19.760 1.00108.26 C ANISOU 1111 CA VAL A 78 10420 15179 15533 225 -1832 -479 C ATOM 1112 C VAL A 78 131.708 -76.265 18.446 1.00105.69 C ANISOU 1112 C VAL A 78 10265 14514 15378 176 -1622 -381 C ATOM 1113 O VAL A 78 130.477 -76.280 18.465 1.00103.79 O ANISOU 1113 O VAL A 78 10181 14220 15033 193 -1540 -412 O ATOM 1114 CB VAL A 78 132.988 -74.686 19.979 1.00114.31 C ANISOU 1114 CB VAL A 78 11063 15930 16438 91 -2016 -803 C ATOM 1115 CG1 VAL A 78 133.097 -74.369 21.467 1.00116.90 C ANISOU 1115 CG1 VAL A 78 11300 16616 16499 145 -2230 -1007 C ATOM 1116 CG2 VAL A 78 134.319 -74.420 19.268 1.00114.89 C ANISOU 1116 CG2 VAL A 78 10964 15877 16813 1 -2051 -759 C ATOM 1117 N SER A 79 132.428 -76.404 17.317 1.00 98.64 N ANISOU 1117 N SER A 79 9336 13411 14733 124 -1533 -254 N ATOM 1118 CA SER A 79 131.836 -76.578 15.991 1.00 94.47 C ANISOU 1118 CA SER A 79 8956 12586 14353 88 -1341 -154 C ATOM 1119 C SER A 79 130.989 -77.836 15.954 1.00 92.88 C ANISOU 1119 C SER A 79 8901 12393 13997 197 -1196 41 C ATOM 1120 O SER A 79 129.900 -77.820 15.391 1.00 90.87 O ANISOU 1120 O SER A 79 8802 11979 13744 175 -1091 28 O ATOM 1121 CB SER A 79 132.923 -76.658 14.919 1.00 97.84 C ANISOU 1121 CB SER A 79 9296 12848 15029 49 -1269 -27 C ATOM 1122 OG SER A 79 134.009 -75.773 15.145 1.00108.90 O ANISOU 1122 OG SER A 79 10501 14290 16585 -31 -1413 -149 O ATOM 1123 N SER A 80 131.488 -78.921 16.562 1.00 87.02 N ANISOU 1123 N SER A 80 8095 11833 13137 315 -1194 228 N ATOM 1124 CA SER A 80 130.802 -80.208 16.623 1.00 84.48 C ANISOU 1124 CA SER A 80 7881 11516 12700 426 -1053 437 C ATOM 1125 C SER A 80 129.516 -80.122 17.441 1.00 83.77 C ANISOU 1125 C SER A 80 7892 11536 12402 460 -1066 359 C ATOM 1126 O SER A 80 128.590 -80.908 17.214 1.00 82.44 O ANISOU 1126 O SER A 80 7846 11278 12198 505 -928 482 O ATOM 1127 CB SER A 80 131.716 -81.280 17.203 1.00 90.06 C ANISOU 1127 CB SER A 80 8467 12406 13346 552 -1056 662 C ATOM 1128 OG SER A 80 132.843 -81.500 16.371 1.00102.38 O ANISOU 1128 OG SER A 80 9941 13846 15112 537 -1009 765 O ATOM 1129 N ILE A 81 129.451 -79.161 18.380 1.00 77.79 N ANISOU 1129 N ILE A 81 7077 10966 11516 437 -1227 145 N ATOM 1130 CA ILE A 81 128.263 -78.966 19.211 1.00 76.07 C ANISOU 1130 CA ILE A 81 6945 10871 11087 479 -1237 52 C ATOM 1131 C ILE A 81 127.176 -78.282 18.361 1.00 75.07 C ANISOU 1131 C ILE A 81 6961 10483 11080 377 -1157 -79 C ATOM 1132 O ILE A 81 125.994 -78.583 18.559 1.00 73.55 O ANISOU 1132 O ILE A 81 6878 10284 10784 418 -1072 -45 O ATOM 1133 CB ILE A 81 128.585 -78.221 20.544 1.00 81.06 C ANISOU 1133 CB ILE A 81 7468 11815 11515 508 -1436 -148 C ATOM 1134 CG1 ILE A 81 129.585 -79.011 21.446 1.00 82.95 C ANISOU 1134 CG1 ILE A 81 7561 12361 11597 633 -1519 16 C ATOM 1135 CG2 ILE A 81 127.325 -77.808 21.337 1.00 81.19 C ANISOU 1135 CG2 ILE A 81 7581 11946 11321 547 -1438 -288 C ATOM 1136 CD1 ILE A 81 129.390 -80.578 21.546 1.00 86.45 C ANISOU 1136 CD1 ILE A 81 8035 12849 11962 779 -1360 375 C ATOM 1137 N TYR A 82 127.570 -77.443 17.369 1.00 69.00 N ANISOU 1137 N TYR A 82 6183 9494 10541 254 -1168 -192 N ATOM 1138 CA TYR A 82 126.582 -76.820 16.479 1.00 65.99 C ANISOU 1138 CA TYR A 82 5927 8868 10278 169 -1087 -282 C ATOM 1139 C TYR A 82 126.071 -77.848 15.441 1.00 64.92 C ANISOU 1139 C TYR A 82 5907 8546 10212 189 -913 -74 C ATOM 1140 O TYR A 82 124.903 -77.766 15.050 1.00 61.90 O ANISOU 1140 O TYR A 82 5643 8046 9830 168 -838 -97 O ATOM 1141 CB TYR A 82 127.104 -75.560 15.778 1.00 67.80 C ANISOU 1141 CB TYR A 82 6103 8929 10731 44 -1143 -448 C ATOM 1142 CG TYR A 82 127.533 -74.435 16.698 1.00 72.81 C ANISOU 1142 CG TYR A 82 6623 9695 11349 0 -1318 -700 C ATOM 1143 CD1 TYR A 82 126.614 -73.776 17.507 1.00 75.52 C ANISOU 1143 CD1 TYR A 82 7012 10123 11558 9 -1372 -896 C ATOM 1144 CD2 TYR A 82 128.838 -73.962 16.685 1.00 75.81 C ANISOU 1144 CD2 TYR A 82 6842 10091 11873 -57 -1425 -759 C ATOM 1145 CE1 TYR A 82 127.002 -72.722 18.339 1.00 78.49 C ANISOU 1145 CE1 TYR A 82 7287 10611 11924 -33 -1537 -1165 C ATOM 1146 CE2 TYR A 82 129.238 -72.909 17.511 1.00 79.09 C ANISOU 1146 CE2 TYR A 82 7142 10613 12297 -111 -1600 -1022 C ATOM 1147 CZ TYR A 82 128.316 -72.292 18.338 1.00 85.99 C ANISOU 1147 CZ TYR A 82 8075 11576 13022 -98 -1657 -1237 C ATOM 1148 OH TYR A 82 128.711 -71.259 19.153 1.00 88.55 O ANISOU 1148 OH TYR A 82 8289 12001 13356 -149 -1832 -1528 O ATOM 1149 N ILE A 83 126.931 -78.837 15.035 1.00 61.00 N ANISOU 1149 N ILE A 83 5371 8031 9774 235 -851 119 N ATOM 1150 CA ILE A 83 126.560 -79.922 14.088 1.00 58.76 C ANISOU 1150 CA ILE A 83 5190 7576 9559 263 -689 297 C ATOM 1151 C ILE A 83 125.432 -80.757 14.697 1.00 59.17 C ANISOU 1151 C ILE A 83 5322 7691 9471 336 -623 386 C ATOM 1152 O ILE A 83 124.442 -80.999 14.017 1.00 57.45 O ANISOU 1152 O ILE A 83 5219 7311 9300 308 -530 397 O ATOM 1153 CB ILE A 83 127.714 -80.869 13.630 1.00 62.08 C ANISOU 1153 CB ILE A 83 5548 7967 10073 316 -624 481 C ATOM 1154 CG1 ILE A 83 129.056 -80.137 13.377 1.00 63.55 C ANISOU 1154 CG1 ILE A 83 5600 8162 10384 267 -704 429 C ATOM 1155 CG2 ILE A 83 127.301 -81.732 12.414 1.00 60.55 C ANISOU 1155 CG2 ILE A 83 5476 7546 9982 319 -460 591 C ATOM 1156 CD1 ILE A 83 129.238 -79.373 12.106 1.00 71.33 C ANISOU 1156 CD1 ILE A 83 6616 8934 11553 173 -659 361 C ATOM 1157 N PHE A 84 125.573 -81.156 15.983 1.00 54.57 N ANISOU 1157 N PHE A 84 4665 7352 8716 432 -675 451 N ATOM 1158 CA PHE A 84 124.563 -81.928 16.703 1.00 53.78 C ANISOU 1158 CA PHE A 84 4615 7339 8481 517 -604 564 C ATOM 1159 C PHE A 84 123.218 -81.203 16.701 1.00 58.61 C ANISOU 1159 C PHE A 84 5321 7893 9054 462 -598 415 C ATOM 1160 O PHE A 84 122.209 -81.788 16.293 1.00 58.28 O ANISOU 1160 O PHE A 84 5368 7719 9057 461 -486 494 O ATOM 1161 CB PHE A 84 125.009 -82.202 18.144 1.00 56.73 C ANISOU 1161 CB PHE A 84 4880 8030 8646 636 -679 638 C ATOM 1162 CG PHE A 84 123.993 -82.955 18.965 1.00 57.90 C ANISOU 1162 CG PHE A 84 5063 8289 8646 739 -593 781 C ATOM 1163 CD1 PHE A 84 123.793 -84.312 18.776 1.00 60.96 C ANISOU 1163 CD1 PHE A 84 5468 8586 9107 809 -444 1037 C ATOM 1164 CD2 PHE A 84 123.224 -82.302 19.917 1.00 60.11 C ANISOU 1164 CD2 PHE A 84 5354 8754 8732 769 -648 661 C ATOM 1165 CE1 PHE A 84 122.838 -85.005 19.524 1.00 62.47 C ANISOU 1165 CE1 PHE A 84 5677 8864 9196 901 -349 1191 C ATOM 1166 CE2 PHE A 84 122.277 -82.998 20.670 1.00 63.72 C ANISOU 1166 CE2 PHE A 84 5833 9319 9058 873 -549 816 C ATOM 1167 CZ PHE A 84 122.098 -84.349 20.477 1.00 61.84 C ANISOU 1167 CZ PHE A 84 5601 8985 8911 936 -399 1093 C ATOM 1168 N ASN A 85 123.205 -79.935 17.151 1.00 54.39 N ANISOU 1168 N ASN A 85 4759 7451 8456 418 -719 195 N ATOM 1169 CA ASN A 85 121.986 -79.143 17.219 1.00 52.71 C ANISOU 1169 CA ASN A 85 4623 7192 8213 377 -715 44 C ATOM 1170 C ASN A 85 121.332 -78.984 15.854 1.00 53.69 C ANISOU 1170 C ASN A 85 4845 7031 8523 282 -634 30 C ATOM 1171 O ASN A 85 120.115 -79.141 15.763 1.00 52.86 O ANISOU 1171 O ASN A 85 4814 6863 8406 283 -562 48 O ATOM 1172 CB ASN A 85 122.263 -77.799 17.838 1.00 51.29 C ANISOU 1172 CB ASN A 85 4387 7126 7974 341 -856 -206 C ATOM 1173 CG ASN A 85 122.314 -77.875 19.329 1.00 63.23 C ANISOU 1173 CG ASN A 85 5837 8953 9232 451 -928 -231 C ATOM 1174 OD1 ASN A 85 123.376 -78.054 19.931 1.00 57.01 O ANISOU 1174 OD1 ASN A 85 4946 8354 8361 498 -1021 -210 O ATOM 1175 ND2 ASN A 85 121.151 -77.799 19.954 1.00 47.15 N ANISOU 1175 ND2 ASN A 85 3858 6998 7059 505 -880 -258 N ATOM 1176 N LEU A 86 122.124 -78.718 14.798 1.00 47.95 N ANISOU 1176 N LEU A 86 4110 6147 7961 210 -640 12 N ATOM 1177 CA LEU A 86 121.604 -78.566 13.439 1.00 45.47 C ANISOU 1177 CA LEU A 86 3885 5591 7799 135 -568 7 C ATOM 1178 C LEU A 86 121.010 -79.890 12.948 1.00 49.28 C ANISOU 1178 C LEU A 86 4442 5983 8300 169 -448 176 C ATOM 1179 O LEU A 86 119.949 -79.880 12.322 1.00 48.15 O ANISOU 1179 O LEU A 86 4381 5714 8202 131 -398 159 O ATOM 1180 CB LEU A 86 122.708 -78.058 12.484 1.00 44.61 C ANISOU 1180 CB LEU A 86 3738 5367 7844 73 -588 -20 C ATOM 1181 CG LEU A 86 122.456 -78.057 10.952 1.00 46.73 C ANISOU 1181 CG LEU A 86 4091 5415 8250 19 -504 13 C ATOM 1182 CD1 LEU A 86 121.294 -77.184 10.567 1.00 46.37 C ANISOU 1182 CD1 LEU A 86 4112 5276 8230 -35 -505 -92 C ATOM 1183 CD2 LEU A 86 123.671 -77.604 10.204 1.00 47.09 C ANISOU 1183 CD2 LEU A 86 4077 5390 8426 -17 -510 16 C ATOM 1184 N ALA A 87 121.674 -81.013 13.248 1.00 46.07 N ANISOU 1184 N ALA A 87 3996 5635 7871 241 -406 334 N ATOM 1185 CA ALA A 87 121.193 -82.330 12.847 1.00 46.16 C ANISOU 1185 CA ALA A 87 4065 5541 7934 275 -287 489 C ATOM 1186 C ALA A 87 119.901 -82.646 13.559 1.00 52.44 C ANISOU 1186 C ALA A 87 4886 6387 8652 305 -249 525 C ATOM 1187 O ALA A 87 118.988 -83.163 12.927 1.00 52.69 O ANISOU 1187 O ALA A 87 4986 6268 8765 274 -175 556 O ATOM 1188 CB ALA A 87 122.231 -83.397 13.145 1.00 47.61 C ANISOU 1188 CB ALA A 87 4183 5780 8127 358 -245 659 C ATOM 1189 N VAL A 88 119.803 -82.308 14.859 1.00 50.08 N ANISOU 1189 N VAL A 88 4528 6306 8194 367 -302 514 N ATOM 1190 CA VAL A 88 118.600 -82.539 15.660 1.00 50.42 C ANISOU 1190 CA VAL A 88 4583 6429 8145 414 -254 563 C ATOM 1191 C VAL A 88 117.454 -81.723 15.071 1.00 54.31 C ANISOU 1191 C VAL A 88 5146 6796 8694 329 -258 420 C ATOM 1192 O VAL A 88 116.371 -82.268 14.882 1.00 52.85 O ANISOU 1192 O VAL A 88 4997 6521 8562 322 -178 490 O ATOM 1193 CB VAL A 88 118.837 -82.226 17.163 1.00 55.91 C ANISOU 1193 CB VAL A 88 5202 7420 8623 513 -315 559 C ATOM 1194 CG1 VAL A 88 117.534 -82.017 17.933 1.00 55.68 C ANISOU 1194 CG1 VAL A 88 5190 7483 8483 554 -275 548 C ATOM 1195 CG2 VAL A 88 119.669 -83.321 17.823 1.00 57.51 C ANISOU 1195 CG2 VAL A 88 5327 7759 8764 624 -281 773 C ATOM 1196 N ALA A 89 117.706 -80.440 14.744 1.00 52.04 N ANISOU 1196 N ALA A 89 4866 6490 8419 264 -348 231 N ATOM 1197 CA ALA A 89 116.699 -79.551 14.167 1.00 51.42 C ANISOU 1197 CA ALA A 89 4841 6294 8402 192 -355 104 C ATOM 1198 C ALA A 89 116.231 -80.079 12.835 1.00 55.59 C ANISOU 1198 C ALA A 89 5437 6607 9078 129 -295 158 C ATOM 1199 O ALA A 89 115.031 -80.090 12.572 1.00 55.68 O ANISOU 1199 O ALA A 89 5484 6546 9125 104 -259 156 O ATOM 1200 CB ALA A 89 117.266 -78.157 14.001 1.00 52.15 C ANISOU 1200 CB ALA A 89 4914 6381 8521 139 -451 -81 C ATOM 1201 N ASP A 90 117.173 -80.549 12.009 1.00 52.08 N ANISOU 1201 N ASP A 90 5003 6072 8712 110 -284 204 N ATOM 1202 CA ASP A 90 116.876 -81.098 10.695 1.00 51.61 C ANISOU 1202 CA ASP A 90 5013 5828 8770 61 -232 234 C ATOM 1203 C ASP A 90 116.018 -82.341 10.815 1.00 55.64 C ANISOU 1203 C ASP A 90 5541 6288 9313 83 -151 349 C ATOM 1204 O ASP A 90 115.034 -82.456 10.092 1.00 55.96 O ANISOU 1204 O ASP A 90 5629 6212 9423 31 -134 322 O ATOM 1205 CB ASP A 90 118.163 -81.406 9.924 1.00 54.23 C ANISOU 1205 CB ASP A 90 5347 6098 9161 59 -221 265 C ATOM 1206 CG ASP A 90 118.847 -80.188 9.302 1.00 66.86 C ANISOU 1206 CG ASP A 90 6937 7672 10796 12 -279 161 C ATOM 1207 OD1 ASP A 90 118.131 -79.310 8.750 1.00 65.00 O ANISOU 1207 OD1 ASP A 90 6737 7372 10589 -40 -302 74 O ATOM 1208 OD2 ASP A 90 120.100 -80.145 9.307 1.00 75.39 O ANISOU 1208 OD2 ASP A 90 7965 8784 11894 29 -292 183 O ATOM 1209 N LEU A 91 116.336 -83.221 11.776 1.00 52.49 N ANISOU 1209 N LEU A 91 5091 5984 8871 160 -105 482 N ATOM 1210 CA LEU A 91 115.615 -84.465 12.015 1.00 52.42 C ANISOU 1210 CA LEU A 91 5075 5916 8924 189 -10 621 C ATOM 1211 C LEU A 91 114.146 -84.194 12.396 1.00 53.75 C ANISOU 1211 C LEU A 91 5241 6098 9084 170 3 606 C ATOM 1212 O LEU A 91 113.252 -84.860 11.871 1.00 52.62 O ANISOU 1212 O LEU A 91 5115 5814 9062 128 53 639 O ATOM 1213 CB LEU A 91 116.347 -85.265 13.116 1.00 53.78 C ANISOU 1213 CB LEU A 91 5175 6225 9036 296 37 791 C ATOM 1214 CG LEU A 91 116.591 -86.776 12.948 1.00 59.58 C ANISOU 1214 CG LEU A 91 5896 6840 9902 336 148 963 C ATOM 1215 CD1 LEU A 91 116.813 -87.183 11.503 1.00 59.63 C ANISOU 1215 CD1 LEU A 91 5974 6621 10061 266 168 891 C ATOM 1216 CD2 LEU A 91 117.772 -87.224 13.779 1.00 60.67 C ANISOU 1216 CD2 LEU A 91 5958 7124 9969 444 162 1106 C ATOM 1217 N LEU A 92 113.904 -83.185 13.253 1.00 49.50 N ANISOU 1217 N LEU A 92 4675 5721 8412 199 -46 539 N ATOM 1218 CA LEU A 92 112.554 -82.846 13.705 1.00 49.56 C ANISOU 1218 CA LEU A 92 4670 5759 8401 199 -22 528 C ATOM 1219 C LEU A 92 111.708 -82.219 12.599 1.00 53.07 C ANISOU 1219 C LEU A 92 5164 6054 8947 102 -59 409 C ATOM 1220 O LEU A 92 110.477 -82.373 12.589 1.00 51.88 O ANISOU 1220 O LEU A 92 4998 5856 8856 82 -21 437 O ATOM 1221 CB LEU A 92 112.580 -81.912 14.924 1.00 50.17 C ANISOU 1221 CB LEU A 92 4709 6054 8297 269 -59 466 C ATOM 1222 CG LEU A 92 113.238 -82.445 16.206 1.00 56.59 C ANISOU 1222 CG LEU A 92 5463 7081 8960 387 -33 588 C ATOM 1223 CD1 LEU A 92 113.161 -81.430 17.315 1.00 57.85 C ANISOU 1223 CD1 LEU A 92 5595 7462 8923 452 -83 478 C ATOM 1224 CD2 LEU A 92 112.624 -83.760 16.675 1.00 59.56 C ANISOU 1224 CD2 LEU A 92 5799 7452 9380 448 95 819 C ATOM 1225 N LEU A 93 112.374 -81.499 11.679 1.00 48.90 N ANISOU 1225 N LEU A 93 4679 5460 8440 48 -129 291 N ATOM 1226 CA LEU A 93 111.731 -80.814 10.566 1.00 47.65 C ANISOU 1226 CA LEU A 93 4564 5183 8358 -29 -170 192 C ATOM 1227 C LEU A 93 111.293 -81.827 9.506 1.00 50.90 C ANISOU 1227 C LEU A 93 5011 5441 8888 -81 -142 234 C ATOM 1228 O LEU A 93 110.173 -81.732 8.980 1.00 51.22 O ANISOU 1228 O LEU A 93 5056 5413 8993 -128 -154 208 O ATOM 1229 CB LEU A 93 112.706 -79.781 9.995 1.00 47.15 C ANISOU 1229 CB LEU A 93 4523 5110 8281 -53 -237 86 C ATOM 1230 CG LEU A 93 112.234 -78.911 8.829 1.00 52.10 C ANISOU 1230 CG LEU A 93 5187 5634 8973 -115 -277 5 C ATOM 1231 CD1 LEU A 93 111.142 -77.924 9.262 1.00 52.09 C ANISOU 1231 CD1 LEU A 93 5160 5664 8970 -115 -293 -55 C ATOM 1232 CD2 LEU A 93 113.401 -78.161 8.213 1.00 54.97 C ANISOU 1232 CD2 LEU A 93 5563 5974 9351 -131 -313 -49 C ATOM 1233 N LEU A 94 112.156 -82.834 9.248 1.00 45.47 N ANISOU 1233 N LEU A 94 4339 4702 8234 -67 -105 296 N ATOM 1234 CA LEU A 94 111.883 -83.896 8.272 1.00 44.39 C ANISOU 1234 CA LEU A 94 4239 4411 8216 -111 -75 310 C ATOM 1235 C LEU A 94 110.769 -84.799 8.763 1.00 50.60 C ANISOU 1235 C LEU A 94 4977 5151 9096 -117 -17 397 C ATOM 1236 O LEU A 94 109.938 -85.211 7.963 1.00 51.03 O ANISOU 1236 O LEU A 94 5045 5087 9258 -182 -29 356 O ATOM 1237 CB LEU A 94 113.146 -84.695 7.983 1.00 43.46 C ANISOU 1237 CB LEU A 94 4145 4250 8120 -79 -34 352 C ATOM 1238 CG LEU A 94 114.244 -83.912 7.262 1.00 46.22 C ANISOU 1238 CG LEU A 94 4535 4616 8412 -80 -79 276 C ATOM 1239 CD1 LEU A 94 115.575 -84.565 7.424 1.00 46.85 C ANISOU 1239 CD1 LEU A 94 4603 4703 8497 -24 -30 348 C ATOM 1240 CD2 LEU A 94 113.915 -83.671 5.809 1.00 46.91 C ANISOU 1240 CD2 LEU A 94 4692 4605 8527 -138 -113 175 C ATOM 1241 N ALA A 95 110.711 -85.038 10.083 1.00 48.29 N ANISOU 1241 N ALA A 95 4621 4966 8762 -48 42 518 N ATOM 1242 CA ALA A 95 109.692 -85.852 10.736 1.00 49.56 C ANISOU 1242 CA ALA A 95 4714 5101 9015 -37 121 642 C ATOM 1243 C ALA A 95 108.264 -85.297 10.488 1.00 54.43 C ANISOU 1243 C ALA A 95 5309 5693 9680 -96 89 583 C ATOM 1244 O ALA A 95 107.307 -86.044 10.609 1.00 56.20 O ANISOU 1244 O ALA A 95 5475 5838 10041 -121 143 662 O ATOM 1245 CB ALA A 95 109.973 -85.929 12.227 1.00 51.07 C ANISOU 1245 CB ALA A 95 4843 5468 9093 72 186 783 C ATOM 1246 N THR A 96 108.127 -84.014 10.137 1.00 48.32 N ANISOU 1246 N THR A 96 4567 4975 8819 -118 6 456 N ATOM 1247 CA THR A 96 106.816 -83.449 9.865 1.00 47.51 C ANISOU 1247 CA THR A 96 4435 4851 8767 -164 -25 410 C ATOM 1248 C THR A 96 106.348 -83.680 8.417 1.00 52.47 C ANISOU 1248 C THR A 96 5095 5335 9507 -259 -94 323 C ATOM 1249 O THR A 96 105.204 -83.355 8.123 1.00 52.83 O ANISOU 1249 O THR A 96 5100 5358 9614 -302 -127 299 O ATOM 1250 CB THR A 96 106.784 -81.945 10.152 1.00 46.05 C ANISOU 1250 CB THR A 96 4259 4778 8461 -135 -74 321 C ATOM 1251 OG1 THR A 96 107.512 -81.251 9.151 1.00 42.89 O ANISOU 1251 OG1 THR A 96 3927 4340 8031 -171 -153 210 O ATOM 1252 CG2 THR A 96 107.225 -81.579 11.564 1.00 42.82 C ANISOU 1252 CG2 THR A 96 3822 4536 7913 -39 -29 360 C ATOM 1253 N LEU A 97 107.206 -84.183 7.512 1.00 49.06 N ANISOU 1253 N LEU A 97 4731 4821 9089 -285 -118 270 N ATOM 1254 CA LEU A 97 106.875 -84.391 6.098 1.00 48.69 C ANISOU 1254 CA LEU A 97 4727 4668 9106 -361 -190 165 C ATOM 1255 C LEU A 97 105.684 -85.325 5.876 1.00 53.92 C ANISOU 1255 C LEU A 97 5326 5220 9940 -429 -189 176 C ATOM 1256 O LEU A 97 104.862 -84.981 5.019 1.00 54.88 O ANISOU 1256 O LEU A 97 5441 5324 10088 -488 -276 91 O ATOM 1257 CB LEU A 97 108.061 -84.868 5.282 1.00 48.67 C ANISOU 1257 CB LEU A 97 4808 4608 9077 -357 -192 110 C ATOM 1258 CG LEU A 97 108.983 -83.734 4.818 1.00 52.99 C ANISOU 1258 CG LEU A 97 5416 5233 9485 -328 -235 53 C ATOM 1259 CD1 LEU A 97 110.412 -84.201 4.711 1.00 53.61 C ANISOU 1259 CD1 LEU A 97 5543 5297 9532 -285 -188 68 C ATOM 1260 CD2 LEU A 97 108.526 -83.145 3.495 1.00 54.20 C ANISOU 1260 CD2 LEU A 97 5610 5373 9608 -371 -322 -47 C ATOM 1261 N PRO A 98 105.508 -86.458 6.626 1.00 49.83 N ANISOU 1261 N PRO A 98 4747 4633 9554 -422 -95 287 N ATOM 1262 CA PRO A 98 104.292 -87.274 6.436 1.00 49.96 C ANISOU 1262 CA PRO A 98 4679 4529 9776 -499 -94 299 C ATOM 1263 C PRO A 98 102.979 -86.497 6.698 1.00 51.95 C ANISOU 1263 C PRO A 98 4846 4850 10044 -520 -129 319 C ATOM 1264 O PRO A 98 101.997 -86.784 6.014 1.00 51.61 O ANISOU 1264 O PRO A 98 4749 4725 10135 -605 -195 259 O ATOM 1265 CB PRO A 98 104.470 -88.413 7.446 1.00 52.25 C ANISOU 1265 CB PRO A 98 4906 4753 10195 -460 44 464 C ATOM 1266 CG PRO A 98 105.948 -88.513 7.653 1.00 55.62 C ANISOU 1266 CG PRO A 98 5411 5221 10500 -383 86 489 C ATOM 1267 CD PRO A 98 106.387 -87.083 7.643 1.00 50.50 C ANISOU 1267 CD PRO A 98 4821 4739 9627 -344 16 420 C ATOM 1268 N LEU A 99 102.956 -85.513 7.641 1.00 46.90 N ANISOU 1268 N LEU A 99 4189 4359 9273 -443 -92 388 N ATOM 1269 CA LEU A 99 101.757 -84.705 7.904 1.00 47.14 C ANISOU 1269 CA LEU A 99 4140 4454 9317 -446 -111 406 C ATOM 1270 C LEU A 99 101.338 -83.877 6.694 1.00 52.70 C ANISOU 1270 C LEU A 99 4873 5159 9993 -501 -245 272 C ATOM 1271 O LEU A 99 100.151 -83.807 6.382 1.00 52.89 O ANISOU 1271 O LEU A 99 4811 5160 10125 -552 -290 270 O ATOM 1272 CB LEU A 99 101.981 -83.744 9.068 1.00 46.55 C ANISOU 1272 CB LEU A 99 4063 4537 9085 -343 -48 465 C ATOM 1273 CG LEU A 99 102.164 -84.321 10.430 1.00 52.34 C ANISOU 1273 CG LEU A 99 4749 5335 9801 -261 85 619 C ATOM 1274 CD1 LEU A 99 102.715 -83.265 11.372 1.00 51.40 C ANISOU 1274 CD1 LEU A 99 4663 5394 9471 -157 109 607 C ATOM 1275 CD2 LEU A 99 100.858 -84.848 10.977 1.00 56.56 C ANISOU 1275 CD2 LEU A 99 5153 5841 10495 -269 167 750 C ATOM 1276 N TRP A 100 102.304 -83.238 6.020 1.00 50.09 N ANISOU 1276 N TRP A 100 4649 4862 9520 -485 -305 178 N ATOM 1277 CA TRP A 100 102.025 -82.380 4.860 1.00 50.23 C ANISOU 1277 CA TRP A 100 4697 4902 9487 -515 -421 79 C ATOM 1278 C TRP A 100 101.766 -83.181 3.572 1.00 55.42 C ANISOU 1278 C TRP A 100 5371 5474 10214 -597 -514 -16 C ATOM 1279 O TRP A 100 101.026 -82.702 2.713 1.00 56.79 O ANISOU 1279 O TRP A 100 5519 5675 10385 -631 -616 -71 O ATOM 1280 CB TRP A 100 103.147 -81.370 4.623 1.00 48.03 C ANISOU 1280 CB TRP A 100 4512 4688 9048 -461 -435 35 C ATOM 1281 CG TRP A 100 103.753 -80.802 5.872 1.00 48.71 C ANISOU 1281 CG TRP A 100 4599 4848 9058 -386 -353 86 C ATOM 1282 CD1 TRP A 100 105.079 -80.773 6.190 1.00 51.10 C ANISOU 1282 CD1 TRP A 100 4966 5179 9272 -344 -320 80 C ATOM 1283 CD2 TRP A 100 103.057 -80.241 6.997 1.00 49.00 C ANISOU 1283 CD2 TRP A 100 4564 4955 9099 -339 -297 142 C ATOM 1284 NE1 TRP A 100 105.258 -80.214 7.432 1.00 50.87 N ANISOU 1284 NE1 TRP A 100 4908 5239 9181 -279 -264 114 N ATOM 1285 CE2 TRP A 100 104.035 -79.875 7.952 1.00 52.67 C ANISOU 1285 CE2 TRP A 100 5061 5497 9455 -269 -243 148 C ATOM 1286 CE3 TRP A 100 101.701 -80.009 7.294 1.00 50.88 C ANISOU 1286 CE3 TRP A 100 4708 5205 9420 -343 -286 186 C ATOM 1287 CZ2 TRP A 100 103.705 -79.276 9.173 1.00 51.97 C ANISOU 1287 CZ2 TRP A 100 4925 5505 9316 -201 -182 174 C ATOM 1288 CZ3 TRP A 100 101.374 -79.425 8.511 1.00 52.65 C ANISOU 1288 CZ3 TRP A 100 4885 5515 9605 -269 -207 230 C ATOM 1289 CH2 TRP A 100 102.369 -79.062 9.433 1.00 52.86 C ANISOU 1289 CH2 TRP A 100 4958 5626 9502 -197 -157 214 C ATOM 1290 N ALA A 101 102.401 -84.356 3.405 1.00 49.65 N ANISOU 1290 N ALA A 101 4682 4648 9536 -622 -482 -45 N ATOM 1291 CA ALA A 101 102.158 -85.218 2.251 1.00 49.28 C ANISOU 1291 CA ALA A 101 4651 4509 9563 -699 -566 -167 C ATOM 1292 C ALA A 101 100.761 -85.880 2.377 1.00 54.82 C ANISOU 1292 C ALA A 101 5218 5134 10476 -782 -594 -155 C ATOM 1293 O ALA A 101 100.180 -86.261 1.361 1.00 57.69 O ANISOU 1293 O ALA A 101 5563 5458 10899 -858 -708 -278 O ATOM 1294 CB ALA A 101 103.245 -86.264 2.154 1.00 50.06 C ANISOU 1294 CB ALA A 101 4827 4511 9684 -691 -502 -200 C ATOM 1295 N THR A 102 100.198 -85.946 3.622 1.00 48.71 N ANISOU 1295 N THR A 102 4342 4358 9808 -763 -494 -5 N ATOM 1296 CA THR A 102 98.846 -86.470 3.906 1.00 48.98 C ANISOU 1296 CA THR A 102 4222 4324 10064 -832 -495 48 C ATOM 1297 C THR A 102 97.782 -85.353 3.766 1.00 54.04 C ANISOU 1297 C THR A 102 4785 5075 10672 -830 -571 62 C ATOM 1298 O THR A 102 96.756 -85.570 3.129 1.00 54.19 O ANISOU 1298 O THR A 102 4708 5061 10818 -912 -672 8 O ATOM 1299 CB THR A 102 98.772 -87.094 5.285 1.00 49.40 C ANISOU 1299 CB THR A 102 4198 4333 10240 -794 -330 228 C ATOM 1300 OG1 THR A 102 99.716 -88.161 5.378 1.00 52.76 O ANISOU 1300 OG1 THR A 102 4681 4646 10720 -790 -258 232 O ATOM 1301 CG2 THR A 102 97.393 -87.590 5.616 1.00 42.02 C ANISOU 1301 CG2 THR A 102 3089 3326 9551 -859 -310 309 C ATOM 1302 N TYR A 103 98.030 -84.163 4.354 1.00 51.25 N ANISOU 1302 N TYR A 103 4464 4847 10161 -737 -525 128 N ATOM 1303 CA TYR A 103 97.159 -82.983 4.251 1.00 50.92 C ANISOU 1303 CA TYR A 103 4360 4904 10085 -714 -577 148 C ATOM 1304 C TYR A 103 96.922 -82.616 2.772 1.00 56.55 C ANISOU 1304 C TYR A 103 5096 5644 10744 -762 -746 25 C ATOM 1305 O TYR A 103 95.768 -82.462 2.373 1.00 58.92 O ANISOU 1305 O TYR A 103 5283 5963 11141 -806 -830 27 O ATOM 1306 CB TYR A 103 97.794 -81.822 5.027 1.00 50.19 C ANISOU 1306 CB TYR A 103 4330 4913 9826 -604 -497 196 C ATOM 1307 CG TYR A 103 97.077 -80.492 4.980 1.00 51.81 C ANISOU 1307 CG TYR A 103 4487 5202 9997 -560 -527 214 C ATOM 1308 CD1 TYR A 103 95.752 -80.372 5.399 1.00 54.56 C ANISOU 1308 CD1 TYR A 103 4690 5561 10479 -564 -504 295 C ATOM 1309 CD2 TYR A 103 97.763 -79.324 4.658 1.00 51.62 C ANISOU 1309 CD2 TYR A 103 4550 5237 9825 -502 -552 169 C ATOM 1310 CE1 TYR A 103 95.114 -79.132 5.436 1.00 54.02 C ANISOU 1310 CE1 TYR A 103 4572 5562 10392 -507 -512 322 C ATOM 1311 CE2 TYR A 103 97.132 -78.082 4.685 1.00 52.18 C ANISOU 1311 CE2 TYR A 103 4571 5362 9891 -452 -560 195 C ATOM 1312 CZ TYR A 103 95.805 -77.993 5.056 1.00 56.96 C ANISOU 1312 CZ TYR A 103 5039 5979 10625 -451 -541 268 C ATOM 1313 OH TYR A 103 95.211 -76.759 5.068 1.00 57.06 O ANISOU 1313 OH TYR A 103 5001 6035 10643 -391 -538 297 O ATOM 1314 N TYR A 104 98.000 -82.559 1.953 1.00 52.07 N ANISOU 1314 N TYR A 104 4668 5090 10028 -750 -794 -73 N ATOM 1315 CA TYR A 104 97.948 -82.273 0.514 1.00 52.66 C ANISOU 1315 CA TYR A 104 4783 5217 10007 -774 -943 -184 C ATOM 1316 C TYR A 104 97.123 -83.312 -0.255 1.00 61.90 C ANISOU 1316 C TYR A 104 5881 6329 11311 -880 -1060 -287 C ATOM 1317 O TYR A 104 96.527 -82.968 -1.283 1.00 63.65 O ANISOU 1317 O TYR A 104 6071 6631 11483 -903 -1205 -354 O ATOM 1318 CB TYR A 104 99.367 -82.236 -0.071 1.00 52.39 C ANISOU 1318 CB TYR A 104 4910 5196 9801 -733 -933 -253 C ATOM 1319 CG TYR A 104 99.411 -81.963 -1.560 1.00 53.35 C ANISOU 1319 CG TYR A 104 5086 5396 9790 -736 -1068 -355 C ATOM 1320 CD1 TYR A 104 99.463 -80.660 -2.047 1.00 53.86 C ANISOU 1320 CD1 TYR A 104 5168 5576 9721 -668 -1103 -304 C ATOM 1321 CD2 TYR A 104 99.400 -83.005 -2.484 1.00 55.26 C ANISOU 1321 CD2 TYR A 104 5356 5600 10040 -799 -1156 -501 C ATOM 1322 CE1 TYR A 104 99.488 -80.399 -3.415 1.00 53.49 C ANISOU 1322 CE1 TYR A 104 5164 5627 9532 -652 -1218 -368 C ATOM 1323 CE2 TYR A 104 99.396 -82.754 -3.855 1.00 57.11 C ANISOU 1323 CE2 TYR A 104 5639 5942 10118 -788 -1284 -599 C ATOM 1324 CZ TYR A 104 99.453 -81.448 -4.316 1.00 62.85 C ANISOU 1324 CZ TYR A 104 6382 6805 10692 -708 -1312 -518 C ATOM 1325 OH TYR A 104 99.458 -81.180 -5.662 1.00 65.74 O ANISOU 1325 OH TYR A 104 6792 7302 10883 -678 -1429 -585 O ATOM 1326 N SER A 105 97.121 -84.582 0.230 1.00 59.88 N ANISOU 1326 N SER A 105 5592 5934 11227 -942 -1000 -302 N ATOM 1327 CA SER A 105 96.444 -85.749 -0.361 1.00 61.68 C ANISOU 1327 CA SER A 105 5743 6057 11637 -1058 -1093 -420 C ATOM 1328 C SER A 105 94.947 -85.818 -0.079 1.00 69.24 C ANISOU 1328 C SER A 105 6503 6998 12806 -1127 -1140 -360 C ATOM 1329 O SER A 105 94.238 -86.596 -0.729 1.00 71.34 O ANISOU 1329 O SER A 105 6682 7198 13227 -1233 -1258 -478 O ATOM 1330 CB SER A 105 97.079 -87.038 0.141 1.00 63.54 C ANISOU 1330 CB SER A 105 6009 6121 12014 -1088 -982 -432 C ATOM 1331 OG SER A 105 98.361 -87.226 -0.423 1.00 69.24 O ANISOU 1331 OG SER A 105 6895 6838 12574 -1047 -971 -531 O ATOM 1332 N TYR A 106 94.478 -85.050 0.907 1.00 65.91 N ANISOU 1332 N TYR A 106 6004 6632 12405 -1066 -1044 -186 N ATOM 1333 CA TYR A 106 93.061 -84.970 1.238 1.00 67.61 C ANISOU 1333 CA TYR A 106 6024 6849 12816 -1111 -1066 -100 C ATOM 1334 C TYR A 106 92.544 -83.607 0.763 1.00 71.16 C ANISOU 1334 C TYR A 106 6449 7462 13129 -1053 -1158 -74 C ATOM 1335 O TYR A 106 91.568 -83.072 1.280 1.00 71.74 O ANISOU 1335 O TYR A 106 6384 7575 13300 -1033 -1128 46 O ATOM 1336 CB TYR A 106 92.848 -85.242 2.725 1.00 68.96 C ANISOU 1336 CB TYR A 106 6114 6957 13132 -1075 -870 85 C ATOM 1337 CG TYR A 106 93.013 -86.717 3.045 1.00 72.81 C ANISOU 1337 CG TYR A 106 6567 7265 13833 -1151 -799 82 C ATOM 1338 CD1 TYR A 106 92.051 -87.651 2.658 1.00 77.24 C ANISOU 1338 CD1 TYR A 106 6971 7702 14674 -1281 -877 30 C ATOM 1339 CD2 TYR A 106 94.107 -87.174 3.769 1.00 73.20 C ANISOU 1339 CD2 TYR A 106 6723 7260 13828 -1091 -651 141 C ATOM 1340 CE1 TYR A 106 92.201 -89.008 2.944 1.00 80.11 C ANISOU 1340 CE1 TYR A 106 7294 7869 15275 -1352 -800 32 C ATOM 1341 CE2 TYR A 106 94.269 -88.529 4.058 1.00 75.79 C ANISOU 1341 CE2 TYR A 106 7013 7410 14374 -1150 -573 160 C ATOM 1342 CZ TYR A 106 93.312 -89.443 3.647 1.00 88.14 C ANISOU 1342 CZ TYR A 106 8426 8829 16234 -1281 -640 107 C ATOM 1343 OH TYR A 106 93.485 -90.782 3.919 1.00 92.92 O ANISOU 1343 OH TYR A 106 8987 9228 17091 -1340 -552 127 O ATOM 1344 N ARG A 107 93.217 -83.088 -0.293 1.00 66.45 N ANISOU 1344 N ARG A 107 5982 6955 12311 -1022 -1264 -181 N ATOM 1345 CA ARG A 107 92.959 -81.842 -1.013 1.00 65.70 C ANISOU 1345 CA ARG A 107 5890 7013 12060 -959 -1360 -163 C ATOM 1346 C ARG A 107 92.775 -80.684 -0.006 1.00 68.20 C ANISOU 1346 C ARG A 107 6173 7373 12368 -857 -1228 3 C ATOM 1347 O ARG A 107 91.818 -79.913 -0.076 1.00 69.97 O ANISOU 1347 O ARG A 107 6279 7668 12639 -831 -1269 81 O ATOM 1348 CB ARG A 107 91.757 -82.028 -1.975 1.00 66.14 C ANISOU 1348 CB ARG A 107 5800 7129 12201 -1037 -1557 -229 C ATOM 1349 CG ARG A 107 92.111 -82.693 -3.325 1.00 67.92 C ANISOU 1349 CG ARG A 107 6103 7388 12316 -1096 -1727 -433 C ATOM 1350 CD ARG A 107 92.451 -84.174 -3.230 1.00 67.45 C ANISOU 1350 CD ARG A 107 6071 7162 12397 -1198 -1709 -570 C ATOM 1351 NE ARG A 107 92.497 -84.837 -4.536 1.00 71.48 N ANISOU 1351 NE ARG A 107 6619 7705 12835 -1264 -1892 -795 N ATOM 1352 CZ ARG A 107 92.928 -86.082 -4.730 1.00 85.56 C ANISOU 1352 CZ ARG A 107 8453 9346 14710 -1343 -1895 -962 C ATOM 1353 NH1 ARG A 107 93.382 -86.802 -3.711 1.00 76.32 N ANISOU 1353 NH1 ARG A 107 7299 7991 13709 -1361 -1720 -900 N ATOM 1354 NH2 ARG A 107 92.929 -86.610 -5.947 1.00 69.60 N ANISOU 1354 NH2 ARG A 107 6468 7371 12604 -1394 -2069 -1192 N ATOM 1355 N TYR A 108 93.695 -80.652 0.980 1.00 60.85 N ANISOU 1355 N TYR A 108 5339 6393 11388 -801 -1067 48 N ATOM 1356 CA TYR A 108 93.826 -79.713 2.093 1.00 58.05 C ANISOU 1356 CA TYR A 108 4989 6066 11001 -701 -921 161 C ATOM 1357 C TYR A 108 92.671 -79.833 3.116 1.00 61.12 C ANISOU 1357 C TYR A 108 5213 6436 11576 -700 -832 279 C ATOM 1358 O TYR A 108 92.154 -78.821 3.575 1.00 59.29 O ANISOU 1358 O TYR A 108 4923 6259 11345 -624 -778 360 O ATOM 1359 CB TYR A 108 94.012 -78.264 1.604 1.00 57.40 C ANISOU 1359 CB TYR A 108 4951 6073 10783 -617 -954 178 C ATOM 1360 CG TYR A 108 95.249 -78.075 0.751 1.00 56.13 C ANISOU 1360 CG TYR A 108 4951 5935 10442 -600 -1001 96 C ATOM 1361 CD1 TYR A 108 96.510 -77.973 1.329 1.00 56.67 C ANISOU 1361 CD1 TYR A 108 5144 5973 10416 -556 -896 81 C ATOM 1362 CD2 TYR A 108 95.158 -77.983 -0.633 1.00 56.48 C ANISOU 1362 CD2 TYR A 108 5011 6046 10404 -619 -1149 41 C ATOM 1363 CE1 TYR A 108 97.653 -77.803 0.547 1.00 55.20 C ANISOU 1363 CE1 TYR A 108 5088 5803 10082 -537 -927 22 C ATOM 1364 CE2 TYR A 108 96.292 -77.806 -1.422 1.00 55.77 C ANISOU 1364 CE2 TYR A 108 5062 5986 10143 -589 -1173 -16 C ATOM 1365 CZ TYR A 108 97.536 -77.715 -0.827 1.00 56.99 C ANISOU 1365 CZ TYR A 108 5332 6091 10230 -551 -1056 -21 C ATOM 1366 OH TYR A 108 98.649 -77.524 -1.599 1.00 54.32 O ANISOU 1366 OH TYR A 108 5117 5780 9742 -518 -1067 -61 O ATOM 1367 N ASP A 109 92.349 -81.066 3.544 1.00 59.46 N ANISOU 1367 N ASP A 109 4929 6136 11527 -773 -792 299 N ATOM 1368 CA ASP A 109 91.361 -81.307 4.600 1.00 61.09 C ANISOU 1368 CA ASP A 109 4977 6319 11915 -765 -675 437 C ATOM 1369 C ASP A 109 92.079 -81.883 5.828 1.00 67.56 C ANISOU 1369 C ASP A 109 5853 7100 12717 -717 -496 510 C ATOM 1370 O ASP A 109 92.497 -83.046 5.822 1.00 68.20 O ANISOU 1370 O ASP A 109 5954 7082 12875 -780 -482 491 O ATOM 1371 CB ASP A 109 90.205 -82.218 4.143 1.00 64.86 C ANISOU 1371 CB ASP A 109 5275 6726 12643 -886 -766 440 C ATOM 1372 CG ASP A 109 89.076 -82.381 5.151 1.00 77.89 C ANISOU 1372 CG ASP A 109 6733 8357 14504 -874 -640 608 C ATOM 1373 OD1 ASP A 109 88.804 -81.418 5.906 1.00 79.37 O ANISOU 1373 OD1 ASP A 109 6900 8629 14630 -761 -531 709 O ATOM 1374 OD2 ASP A 109 88.424 -83.449 5.145 1.00 84.26 O ANISOU 1374 OD2 ASP A 109 7401 9060 15553 -976 -652 634 O ATOM 1375 N TRP A 110 92.261 -81.039 6.858 1.00 64.57 N ANISOU 1375 N TRP A 110 5502 6803 12229 -597 -364 586 N ATOM 1376 CA TRP A 110 92.929 -81.370 8.111 1.00 64.14 C ANISOU 1376 CA TRP A 110 5499 6767 12106 -521 -198 663 C ATOM 1377 C TRP A 110 92.071 -82.346 8.923 1.00 73.14 C ANISOU 1377 C TRP A 110 6483 7857 13451 -539 -77 819 C ATOM 1378 O TRP A 110 90.941 -82.014 9.292 1.00 74.13 O ANISOU 1378 O TRP A 110 6464 8014 13689 -515 -27 915 O ATOM 1379 CB TRP A 110 93.226 -80.085 8.905 1.00 61.22 C ANISOU 1379 CB TRP A 110 5189 6514 11557 -389 -113 668 C ATOM 1380 CG TRP A 110 94.188 -80.315 10.024 1.00 61.13 C ANISOU 1380 CG TRP A 110 5263 6557 11408 -307 15 701 C ATOM 1381 CD1 TRP A 110 93.882 -80.515 11.334 1.00 64.81 C ANISOU 1381 CD1 TRP A 110 5667 7092 11866 -219 178 828 C ATOM 1382 CD2 TRP A 110 95.606 -80.479 9.911 1.00 59.46 C ANISOU 1382 CD2 TRP A 110 5201 6345 11045 -302 -12 620 C ATOM 1383 NE1 TRP A 110 95.027 -80.742 12.057 1.00 63.75 N ANISOU 1383 NE1 TRP A 110 5636 7018 11567 -155 242 827 N ATOM 1384 CE2 TRP A 110 96.102 -80.730 11.207 1.00 63.70 C ANISOU 1384 CE2 TRP A 110 5756 6963 11483 -209 126 700 C ATOM 1385 CE3 TRP A 110 96.512 -80.417 8.839 1.00 59.45 C ANISOU 1385 CE3 TRP A 110 5314 6297 10977 -358 -135 496 C ATOM 1386 CZ2 TRP A 110 97.467 -80.913 11.466 1.00 61.97 C ANISOU 1386 CZ2 TRP A 110 5656 6777 11112 -178 131 657 C ATOM 1387 CZ3 TRP A 110 97.860 -80.615 9.091 1.00 60.01 C ANISOU 1387 CZ3 TRP A 110 5503 6385 10912 -328 -115 458 C ATOM 1388 CH2 TRP A 110 98.328 -80.847 10.394 1.00 60.86 C ANISOU 1388 CH2 TRP A 110 5618 6572 10935 -242 10 536 C ATOM 1389 N LEU A 111 92.606 -83.555 9.179 1.00 73.12 N ANISOU 1389 N LEU A 111 6498 7768 13516 -576 -22 859 N ATOM 1390 CA LEU A 111 91.918 -84.621 9.928 1.00 75.79 C ANISOU 1390 CA LEU A 111 6685 8033 14080 -596 108 1032 C ATOM 1391 C LEU A 111 92.670 -85.018 11.220 1.00 82.22 C ANISOU 1391 C LEU A 111 7548 8904 14788 -483 294 1170 C ATOM 1392 O LEU A 111 92.399 -86.081 11.788 1.00 82.93 O ANISOU 1392 O LEU A 111 7537 8917 15057 -494 413 1328 O ATOM 1393 CB LEU A 111 91.724 -85.861 9.034 1.00 76.74 C ANISOU 1393 CB LEU A 111 6745 7969 14444 -750 13 976 C ATOM 1394 CG LEU A 111 90.602 -85.805 8.001 1.00 82.54 C ANISOU 1394 CG LEU A 111 7350 8649 15362 -868 -147 893 C ATOM 1395 CD1 LEU A 111 90.758 -86.915 7.008 1.00 83.70 C ANISOU 1395 CD1 LEU A 111 7496 8632 15675 -1012 -271 760 C ATOM 1396 CD2 LEU A 111 89.220 -85.950 8.652 1.00 87.57 C ANISOU 1396 CD2 LEU A 111 7759 9274 16240 -874 -51 1071 C ATOM 1397 N PHE A 112 93.576 -84.146 11.696 1.00 79.58 N ANISOU 1397 N PHE A 112 7353 8709 14172 -372 318 1118 N ATOM 1398 CA PHE A 112 94.377 -84.383 12.898 1.00 80.24 C ANISOU 1398 CA PHE A 112 7492 8893 14102 -252 465 1226 C ATOM 1399 C PHE A 112 93.860 -83.608 14.129 1.00 85.25 C ANISOU 1399 C PHE A 112 8077 9704 14612 -107 607 1328 C ATOM 1400 O PHE A 112 94.175 -83.992 15.255 1.00 86.24 O ANISOU 1400 O PHE A 112 8194 9928 14644 1 754 1469 O ATOM 1401 CB PHE A 112 95.846 -84.023 12.641 1.00 80.60 C ANISOU 1401 CB PHE A 112 7720 8983 13920 -227 388 1084 C ATOM 1402 CG PHE A 112 96.499 -84.744 11.488 1.00 81.72 C ANISOU 1402 CG PHE A 112 7932 8974 14144 -342 269 977 C ATOM 1403 CD1 PHE A 112 97.094 -85.988 11.671 1.00 85.76 C ANISOU 1403 CD1 PHE A 112 8448 9395 14743 -358 332 1060 C ATOM 1404 CD2 PHE A 112 96.547 -84.166 10.223 1.00 82.92 C ANISOU 1404 CD2 PHE A 112 8146 9083 14278 -421 104 799 C ATOM 1405 CE1 PHE A 112 97.708 -86.651 10.602 1.00 86.38 C ANISOU 1405 CE1 PHE A 112 8596 9329 14897 -454 233 942 C ATOM 1406 CE2 PHE A 112 97.168 -84.823 9.157 1.00 85.65 C ANISOU 1406 CE2 PHE A 112 8563 9309 14669 -511 2 689 C ATOM 1407 CZ PHE A 112 97.745 -86.061 9.353 1.00 84.63 C ANISOU 1407 CZ PHE A 112 8442 9081 14632 -529 68 749 C ATOM 1408 N GLY A 113 93.087 -82.548 13.912 1.00 81.24 N ANISOU 1408 N GLY A 113 7531 9239 14095 -93 568 1261 N ATOM 1409 CA GLY A 113 92.538 -81.735 14.992 1.00 82.05 C ANISOU 1409 CA GLY A 113 7590 9500 14087 48 702 1327 C ATOM 1410 C GLY A 113 93.042 -80.302 14.992 1.00 85.10 C ANISOU 1410 C GLY A 113 8097 9986 14252 119 643 1146 C ATOM 1411 O GLY A 113 94.178 -80.059 14.584 1.00 82.53 O ANISOU 1411 O GLY A 113 7910 9654 13793 96 542 1008 O ATOM 1412 N PRO A 114 92.231 -79.321 15.468 1.00 83.02 N ANISOU 1412 N PRO A 114 7777 9806 13962 210 713 1143 N ATOM 1413 CA PRO A 114 92.684 -77.905 15.455 1.00 82.27 C ANISOU 1413 CA PRO A 114 7788 9773 13696 274 663 957 C ATOM 1414 C PRO A 114 93.836 -77.597 16.415 1.00 85.45 C ANISOU 1414 C PRO A 114 8317 10318 13831 381 710 874 C ATOM 1415 O PRO A 114 94.515 -76.579 16.237 1.00 84.51 O ANISOU 1415 O PRO A 114 8302 10213 13595 399 634 693 O ATOM 1416 CB PRO A 114 91.434 -77.114 15.844 1.00 85.46 C ANISOU 1416 CB PRO A 114 8079 10221 14171 357 758 999 C ATOM 1417 CG PRO A 114 90.580 -78.092 16.538 1.00 91.25 C ANISOU 1417 CG PRO A 114 8668 10985 15018 386 907 1220 C ATOM 1418 CD PRO A 114 90.854 -79.444 15.985 1.00 86.08 C ANISOU 1418 CD PRO A 114 7990 10215 14501 256 847 1308 C ATOM 1419 N VAL A 115 94.055 -78.468 17.423 1.00 81.86 N ANISOU 1419 N VAL A 115 7844 9971 13290 454 832 1012 N ATOM 1420 CA VAL A 115 95.140 -78.319 18.395 1.00 81.04 C ANISOU 1420 CA VAL A 115 7842 10035 12916 562 869 952 C ATOM 1421 C VAL A 115 96.442 -78.705 17.687 1.00 82.73 C ANISOU 1421 C VAL A 115 8165 10172 13098 466 729 868 C ATOM 1422 O VAL A 115 97.420 -77.967 17.777 1.00 82.48 O ANISOU 1422 O VAL A 115 8240 10199 12901 492 656 699 O ATOM 1423 CB VAL A 115 94.887 -79.109 19.712 1.00 86.49 C ANISOU 1423 CB VAL A 115 8462 10891 13509 692 1055 1160 C ATOM 1424 CG1 VAL A 115 96.024 -78.905 20.715 1.00 86.55 C ANISOU 1424 CG1 VAL A 115 8572 11109 13205 814 1072 1087 C ATOM 1425 CG2 VAL A 115 93.550 -78.702 20.343 1.00 87.89 C ANISOU 1425 CG2 VAL A 115 8523 11141 13730 792 1208 1251 C ATOM 1426 N MET A 116 96.422 -79.802 16.911 1.00 78.35 N ANISOU 1426 N MET A 116 7577 9469 12723 350 688 970 N ATOM 1427 CA MET A 116 97.571 -80.272 16.122 1.00 76.65 C ANISOU 1427 CA MET A 116 7456 9162 12506 259 568 901 C ATOM 1428 C MET A 116 97.963 -79.244 15.063 1.00 74.45 C ANISOU 1428 C MET A 116 7262 8803 12222 187 416 696 C ATOM 1429 O MET A 116 99.126 -79.181 14.696 1.00 72.69 O ANISOU 1429 O MET A 116 7137 8567 11914 159 332 601 O ATOM 1430 CB MET A 116 97.273 -81.615 15.432 1.00 80.20 C ANISOU 1430 CB MET A 116 7842 9446 13184 148 561 1027 C ATOM 1431 CG MET A 116 97.016 -82.780 16.378 1.00 86.69 C ANISOU 1431 CG MET A 116 8573 10307 14059 208 719 1260 C ATOM 1432 SD MET A 116 98.355 -84.008 16.490 1.00 92.01 S ANISOU 1432 SD MET A 116 9307 10951 14702 205 730 1343 S ATOM 1433 CE MET A 116 98.407 -84.666 14.823 1.00 87.57 C ANISOU 1433 CE MET A 116 8765 10118 14388 16 588 1243 C ATOM 1434 N CYS A 117 96.995 -78.439 14.577 1.00 68.98 N ANISOU 1434 N CYS A 117 6519 8061 11628 166 389 650 N ATOM 1435 CA CYS A 117 97.195 -77.379 13.581 1.00 66.87 C ANISOU 1435 CA CYS A 117 6311 7721 11375 115 265 493 C ATOM 1436 C CYS A 117 98.091 -76.272 14.171 1.00 67.70 C ANISOU 1436 C CYS A 117 6506 7919 11299 196 261 344 C ATOM 1437 O CYS A 117 98.978 -75.782 13.470 1.00 66.07 O ANISOU 1437 O CYS A 117 6382 7657 11066 149 161 228 O ATOM 1438 CB CYS A 117 95.851 -76.836 13.101 1.00 67.75 C ANISOU 1438 CB CYS A 117 6323 7779 11641 98 259 519 C ATOM 1439 SG CYS A 117 95.963 -75.551 11.826 1.00 70.97 S ANISOU 1439 SG CYS A 117 6779 8100 12088 51 121 379 S ATOM 1440 N LYS A 118 97.897 -75.926 15.464 1.00 63.24 N ANISOU 1440 N LYS A 118 5921 7498 10609 319 373 343 N ATOM 1441 CA LYS A 118 98.725 -74.947 16.172 1.00 62.21 C ANISOU 1441 CA LYS A 118 5866 7470 10303 399 368 176 C ATOM 1442 C LYS A 118 100.049 -75.568 16.625 1.00 66.09 C ANISOU 1442 C LYS A 118 6425 8050 10636 409 340 166 C ATOM 1443 O LYS A 118 101.096 -74.932 16.461 1.00 64.61 O ANISOU 1443 O LYS A 118 6311 7859 10381 392 254 14 O ATOM 1444 CB LYS A 118 97.998 -74.368 17.389 1.00 65.33 C ANISOU 1444 CB LYS A 118 6215 8005 10601 537 496 158 C ATOM 1445 CG LYS A 118 97.157 -73.170 17.055 1.00 69.77 C ANISOU 1445 CG LYS A 118 6745 8488 11276 553 504 68 C ATOM 1446 CD LYS A 118 96.737 -72.354 18.265 1.00 72.24 C ANISOU 1446 CD LYS A 118 7044 8937 11466 702 621 -25 C ATOM 1447 CE LYS A 118 95.987 -71.095 17.877 1.00 81.67 C ANISOU 1447 CE LYS A 118 8208 10024 12801 721 632 -124 C ATOM 1448 NZ LYS A 118 94.678 -71.370 17.236 1.00 97.97 N ANISOU 1448 NZ LYS A 118 10158 11998 15069 687 668 49 N ATOM 1449 N VAL A 119 99.998 -76.809 17.202 1.00 62.79 N ANISOU 1449 N VAL A 119 5968 7708 10181 441 419 342 N ATOM 1450 CA VAL A 119 101.146 -77.550 17.746 1.00 62.17 C ANISOU 1450 CA VAL A 119 5931 7732 9957 473 414 384 C ATOM 1451 C VAL A 119 102.139 -77.910 16.636 1.00 66.21 C ANISOU 1451 C VAL A 119 6505 8105 10547 357 295 346 C ATOM 1452 O VAL A 119 103.283 -77.486 16.723 1.00 66.02 O ANISOU 1452 O VAL A 119 6544 8130 10412 363 223 228 O ATOM 1453 CB VAL A 119 100.713 -78.796 18.564 1.00 66.16 C ANISOU 1453 CB VAL A 119 6362 8330 10445 542 549 622 C ATOM 1454 CG1 VAL A 119 101.907 -79.683 18.917 1.00 65.70 C ANISOU 1454 CG1 VAL A 119 6337 8347 10280 566 538 700 C ATOM 1455 CG2 VAL A 119 99.963 -78.385 19.827 1.00 67.44 C ANISOU 1455 CG2 VAL A 119 6473 8685 10465 690 680 656 C ATOM 1456 N PHE A 120 101.714 -78.666 15.608 1.00 63.54 N ANISOU 1456 N PHE A 120 6144 7599 10397 254 273 435 N ATOM 1457 CA PHE A 120 102.586 -79.073 14.506 1.00 63.12 C ANISOU 1457 CA PHE A 120 6153 7418 10412 155 175 398 C ATOM 1458 C PHE A 120 102.898 -77.917 13.546 1.00 64.45 C ANISOU 1458 C PHE A 120 6378 7505 10603 98 65 230 C ATOM 1459 O PHE A 120 103.940 -77.949 12.895 1.00 63.28 O ANISOU 1459 O PHE A 120 6294 7306 10443 51 -7 173 O ATOM 1460 CB PHE A 120 102.038 -80.289 13.759 1.00 66.06 C ANISOU 1460 CB PHE A 120 6484 7647 10968 72 187 521 C ATOM 1461 CG PHE A 120 102.337 -81.543 14.544 1.00 70.20 C ANISOU 1461 CG PHE A 120 6975 8218 11482 120 284 688 C ATOM 1462 CD1 PHE A 120 103.644 -82.012 14.664 1.00 74.44 C ANISOU 1462 CD1 PHE A 120 7567 8784 11931 140 266 695 C ATOM 1463 CD2 PHE A 120 101.326 -82.223 15.212 1.00 74.70 C ANISOU 1463 CD2 PHE A 120 7443 8806 12134 157 404 858 C ATOM 1464 CE1 PHE A 120 103.931 -83.151 15.424 1.00 77.01 C ANISOU 1464 CE1 PHE A 120 7851 9157 12251 201 364 874 C ATOM 1465 CE2 PHE A 120 101.616 -83.369 15.968 1.00 79.60 C ANISOU 1465 CE2 PHE A 120 8021 9466 12756 215 510 1044 C ATOM 1466 CZ PHE A 120 102.914 -83.826 16.066 1.00 77.75 C ANISOU 1466 CZ PHE A 120 7847 9262 12432 239 489 1053 C ATOM 1467 N GLY A 121 102.033 -76.904 13.507 1.00 59.65 N ANISOU 1467 N GLY A 121 5741 6890 10033 112 68 168 N ATOM 1468 CA GLY A 121 102.247 -75.705 12.704 1.00 58.31 C ANISOU 1468 CA GLY A 121 5610 6644 9901 77 -14 34 C ATOM 1469 C GLY A 121 103.421 -74.893 13.226 1.00 60.08 C ANISOU 1469 C GLY A 121 5889 6935 10006 116 -44 -104 C ATOM 1470 O GLY A 121 104.283 -74.480 12.449 1.00 58.53 O ANISOU 1470 O GLY A 121 5740 6663 9835 64 -119 -174 O ATOM 1471 N SER A 122 103.472 -74.684 14.558 1.00 56.36 N ANISOU 1471 N SER A 122 5402 6612 9399 212 17 -142 N ATOM 1472 CA SER A 122 104.542 -73.960 15.246 1.00 55.93 C ANISOU 1472 CA SER A 122 5383 6650 9219 255 -21 -295 C ATOM 1473 C SER A 122 105.825 -74.783 15.323 1.00 57.71 C ANISOU 1473 C SER A 122 5639 6929 9359 239 -64 -257 C ATOM 1474 O SER A 122 106.907 -74.227 15.149 1.00 57.38 O ANISOU 1474 O SER A 122 5626 6874 9302 212 -140 -373 O ATOM 1475 CB SER A 122 104.106 -73.581 16.655 1.00 61.31 C ANISOU 1475 CB SER A 122 6036 7504 9754 374 54 -353 C ATOM 1476 OG SER A 122 102.858 -72.916 16.622 1.00 71.64 O ANISOU 1476 OG SER A 122 7306 8762 11151 401 115 -367 O ATOM 1477 N PHE A 123 105.707 -76.098 15.590 1.00 53.12 N ANISOU 1477 N PHE A 123 5040 6399 8746 258 -9 -86 N ATOM 1478 CA PHE A 123 106.839 -77.023 15.678 1.00 53.13 C ANISOU 1478 CA PHE A 123 5059 6445 8685 256 -30 -14 C ATOM 1479 C PHE A 123 107.626 -77.015 14.372 1.00 55.36 C ANISOU 1479 C PHE A 123 5386 6568 9079 156 -111 -50 C ATOM 1480 O PHE A 123 108.852 -77.034 14.404 1.00 54.64 O ANISOU 1480 O PHE A 123 5315 6512 8936 154 -161 -88 O ATOM 1481 CB PHE A 123 106.362 -78.444 16.030 1.00 55.80 C ANISOU 1481 CB PHE A 123 5357 6812 9033 288 65 199 C ATOM 1482 CG PHE A 123 107.440 -79.450 16.360 1.00 58.10 C ANISOU 1482 CG PHE A 123 5650 7169 9256 319 70 304 C ATOM 1483 CD1 PHE A 123 108.102 -79.408 17.582 1.00 62.45 C ANISOU 1483 CD1 PHE A 123 6183 7940 9606 426 78 308 C ATOM 1484 CD2 PHE A 123 107.749 -80.476 15.475 1.00 59.76 C ANISOU 1484 CD2 PHE A 123 5874 7230 9600 251 72 403 C ATOM 1485 CE1 PHE A 123 109.085 -80.347 17.894 1.00 63.69 C ANISOU 1485 CE1 PHE A 123 6327 8167 9705 465 85 429 C ATOM 1486 CE2 PHE A 123 108.723 -81.422 15.792 1.00 63.04 C ANISOU 1486 CE2 PHE A 123 6283 7695 9973 291 92 514 C ATOM 1487 CZ PHE A 123 109.386 -81.351 16.999 1.00 62.25 C ANISOU 1487 CZ PHE A 123 6157 7816 9681 399 99 540 C ATOM 1488 N LEU A 124 106.919 -76.914 13.236 1.00 51.85 N ANISOU 1488 N LEU A 124 4953 5967 8781 81 -125 -40 N ATOM 1489 CA LEU A 124 107.500 -76.841 11.901 1.00 51.23 C ANISOU 1489 CA LEU A 124 4921 5751 8795 -1 -191 -69 C ATOM 1490 C LEU A 124 108.359 -75.583 11.760 1.00 58.05 C ANISOU 1490 C LEU A 124 5802 6607 9647 -9 -253 -210 C ATOM 1491 O LEU A 124 109.500 -75.679 11.307 1.00 59.17 O ANISOU 1491 O LEU A 124 5969 6721 9790 -36 -292 -224 O ATOM 1492 CB LEU A 124 106.381 -76.851 10.839 1.00 50.70 C ANISOU 1492 CB LEU A 124 4848 5561 8855 -60 -199 -38 C ATOM 1493 CG LEU A 124 106.797 -76.595 9.387 1.00 54.45 C ANISOU 1493 CG LEU A 124 5370 5919 9399 -128 -266 -72 C ATOM 1494 CD1 LEU A 124 107.372 -77.841 8.750 1.00 54.58 C ANISOU 1494 CD1 LEU A 124 5423 5885 9430 -164 -269 -11 C ATOM 1495 CD2 LEU A 124 105.639 -76.081 8.583 1.00 56.00 C ANISOU 1495 CD2 LEU A 124 5544 6047 9685 -160 -291 -71 C ATOM 1496 N THR A 125 107.812 -74.415 12.156 1.00 55.01 N ANISOU 1496 N THR A 125 5395 6234 9271 16 -252 -312 N ATOM 1497 CA THR A 125 108.457 -73.103 12.071 1.00 54.97 C ANISOU 1497 CA THR A 125 5391 6191 9305 5 -301 -456 C ATOM 1498 C THR A 125 109.647 -73.005 13.062 1.00 59.41 C ANISOU 1498 C THR A 125 5942 6876 9754 39 -335 -548 C ATOM 1499 O THR A 125 110.692 -72.470 12.688 1.00 59.15 O ANISOU 1499 O THR A 125 5909 6792 9774 -1 -391 -619 O ATOM 1500 CB THR A 125 107.401 -72.003 12.291 1.00 61.89 C ANISOU 1500 CB THR A 125 6239 7034 10242 33 -274 -535 C ATOM 1501 OG1 THR A 125 106.313 -72.237 11.398 1.00 61.95 O ANISOU 1501 OG1 THR A 125 6241 6954 10343 5 -254 -429 O ATOM 1502 CG2 THR A 125 107.939 -70.615 12.028 1.00 59.70 C ANISOU 1502 CG2 THR A 125 5954 6663 10065 12 -313 -674 C ATOM 1503 N LEU A 126 109.492 -73.543 14.293 1.00 55.63 N ANISOU 1503 N LEU A 126 5445 6569 9123 115 -302 -532 N ATOM 1504 CA LEU A 126 110.514 -73.547 15.349 1.00 55.72 C ANISOU 1504 CA LEU A 126 5436 6747 8989 165 -344 -609 C ATOM 1505 C LEU A 126 111.799 -74.242 14.899 1.00 58.99 C ANISOU 1505 C LEU A 126 5853 7150 9409 128 -389 -539 C ATOM 1506 O LEU A 126 112.878 -73.737 15.178 1.00 60.09 O ANISOU 1506 O LEU A 126 5967 7337 9529 119 -462 -648 O ATOM 1507 CB LEU A 126 109.970 -74.247 16.609 1.00 56.67 C ANISOU 1507 CB LEU A 126 5536 7068 8927 271 -279 -537 C ATOM 1508 CG LEU A 126 110.737 -74.031 17.909 1.00 62.47 C ANISOU 1508 CG LEU A 126 6242 8029 9463 352 -324 -646 C ATOM 1509 CD1 LEU A 126 109.790 -73.847 19.059 1.00 64.48 C ANISOU 1509 CD1 LEU A 126 6483 8451 9564 462 -255 -678 C ATOM 1510 CD2 LEU A 126 111.651 -75.190 18.201 1.00 63.55 C ANISOU 1510 CD2 LEU A 126 6361 8283 9500 383 -336 -499 C ATOM 1511 N ASN A 127 111.682 -75.410 14.244 1.00 53.95 N ANISOU 1511 N ASN A 127 5238 6451 8810 108 -345 -365 N ATOM 1512 CA ASN A 127 112.811 -76.211 13.773 1.00 52.26 C ANISOU 1512 CA ASN A 127 5029 6214 8612 86 -364 -280 C ATOM 1513 C ASN A 127 113.345 -75.737 12.429 1.00 55.44 C ANISOU 1513 C ASN A 127 5459 6447 9159 3 -398 -313 C ATOM 1514 O ASN A 127 114.519 -75.967 12.151 1.00 55.18 O ANISOU 1514 O ASN A 127 5415 6409 9140 -11 -426 -295 O ATOM 1515 CB ASN A 127 112.436 -77.680 13.698 1.00 46.33 C ANISOU 1515 CB ASN A 127 4289 5457 7856 108 -289 -94 C ATOM 1516 CG ASN A 127 112.255 -78.291 15.056 1.00 50.83 C ANISOU 1516 CG ASN A 127 4818 6216 8278 207 -244 -12 C ATOM 1517 OD1 ASN A 127 111.159 -78.691 15.418 1.00 49.18 O ANISOU 1517 OD1 ASN A 127 4600 6026 8061 240 -170 69 O ATOM 1518 ND2 ASN A 127 113.315 -78.349 15.854 1.00 36.24 N ANISOU 1518 ND2 ASN A 127 2935 4527 6310 263 -285 -22 N ATOM 1519 N MET A 128 112.507 -75.089 11.596 1.00 52.44 N ANISOU 1519 N MET A 128 5105 5939 8882 -42 -390 -345 N ATOM 1520 CA MET A 128 112.951 -74.554 10.308 1.00 52.41 C ANISOU 1520 CA MET A 128 5122 5792 8999 -103 -412 -357 C ATOM 1521 C MET A 128 113.913 -73.390 10.574 1.00 57.33 C ANISOU 1521 C MET A 128 5700 6414 9668 -118 -466 -482 C ATOM 1522 O MET A 128 114.996 -73.364 9.990 1.00 57.09 O ANISOU 1522 O MET A 128 5660 6338 9695 -148 -483 -463 O ATOM 1523 CB MET A 128 111.766 -74.127 9.427 1.00 54.78 C ANISOU 1523 CB MET A 128 5447 5983 9383 -132 -395 -342 C ATOM 1524 CG MET A 128 112.187 -73.566 8.075 1.00 59.08 C ANISOU 1524 CG MET A 128 6011 6406 10031 -176 -409 -328 C ATOM 1525 SD MET A 128 111.088 -72.258 7.465 1.00 65.05 S ANISOU 1525 SD MET A 128 6754 7066 10898 -187 -409 -358 S ATOM 1526 CE MET A 128 111.468 -70.922 8.602 1.00 62.66 C ANISOU 1526 CE MET A 128 6391 6774 10644 -171 -425 -515 C ATOM 1527 N PHE A 129 113.547 -72.480 11.506 1.00 54.45 N ANISOU 1527 N PHE A 129 5302 6103 9285 -96 -488 -616 N ATOM 1528 CA PHE A 129 114.380 -71.349 11.904 1.00 55.37 C ANISOU 1528 CA PHE A 129 5363 6211 9463 -115 -547 -772 C ATOM 1529 C PHE A 129 115.624 -71.816 12.664 1.00 60.78 C ANISOU 1529 C PHE A 129 6004 7036 10055 -99 -603 -797 C ATOM 1530 O PHE A 129 116.703 -71.297 12.392 1.00 61.57 O ANISOU 1530 O PHE A 129 6054 7084 10254 -144 -651 -849 O ATOM 1531 CB PHE A 129 113.596 -70.336 12.748 1.00 58.30 C ANISOU 1531 CB PHE A 129 5714 6605 9831 -86 -551 -933 C ATOM 1532 CG PHE A 129 112.758 -69.368 11.952 1.00 59.71 C ANISOU 1532 CG PHE A 129 5900 6610 10175 -113 -515 -947 C ATOM 1533 CD1 PHE A 129 113.344 -68.517 11.019 1.00 62.90 C ANISOU 1533 CD1 PHE A 129 6279 6851 10770 -172 -526 -955 C ATOM 1534 CD2 PHE A 129 111.389 -69.273 12.165 1.00 62.16 C ANISOU 1534 CD2 PHE A 129 6230 6926 10463 -71 -462 -937 C ATOM 1535 CE1 PHE A 129 112.570 -67.614 10.285 1.00 63.74 C ANISOU 1535 CE1 PHE A 129 6383 6804 11032 -182 -485 -940 C ATOM 1536 CE2 PHE A 129 110.618 -68.356 11.443 1.00 65.09 C ANISOU 1536 CE2 PHE A 129 6595 7144 10992 -85 -430 -936 C ATOM 1537 CZ PHE A 129 111.213 -67.537 10.506 1.00 62.89 C ANISOU 1537 CZ PHE A 129 6294 6707 10893 -138 -442 -933 C ATOM 1538 N ALA A 130 115.491 -72.806 13.585 1.00 56.77 N ANISOU 1538 N ALA A 130 5501 6702 9366 -31 -594 -738 N ATOM 1539 CA ALA A 130 116.615 -73.360 14.354 1.00 56.61 C ANISOU 1539 CA ALA A 130 5430 6845 9236 5 -647 -729 C ATOM 1540 C ALA A 130 117.655 -73.999 13.425 1.00 58.89 C ANISOU 1540 C ALA A 130 5712 7053 9610 -33 -641 -602 C ATOM 1541 O ALA A 130 118.840 -73.929 13.720 1.00 59.81 O ANISOU 1541 O ALA A 130 5761 7237 9727 -37 -705 -634 O ATOM 1542 CB ALA A 130 116.125 -74.372 15.369 1.00 57.63 C ANISOU 1542 CB ALA A 130 5566 7162 9167 99 -610 -635 C ATOM 1543 N SER A 131 117.218 -74.577 12.290 1.00 53.41 N ANISOU 1543 N SER A 131 5083 6220 8992 -57 -568 -472 N ATOM 1544 CA SER A 131 118.100 -75.152 11.271 1.00 52.67 C ANISOU 1544 CA SER A 131 4997 6037 8978 -83 -542 -363 C ATOM 1545 C SER A 131 118.852 -74.035 10.534 1.00 56.31 C ANISOU 1545 C SER A 131 5418 6382 9594 -147 -574 -435 C ATOM 1546 O SER A 131 120.055 -74.165 10.329 1.00 57.55 O ANISOU 1546 O SER A 131 5524 6543 9800 -156 -590 -402 O ATOM 1547 CB SER A 131 117.307 -75.999 10.280 1.00 55.84 C ANISOU 1547 CB SER A 131 5482 6332 9404 -89 -463 -243 C ATOM 1548 OG SER A 131 118.094 -76.367 9.159 1.00 65.56 O ANISOU 1548 OG SER A 131 6732 7466 10711 -110 -432 -169 O ATOM 1549 N ILE A 132 118.145 -72.933 10.165 1.00 50.98 N ANISOU 1549 N ILE A 132 4756 5602 9011 -185 -574 -520 N ATOM 1550 CA ILE A 132 118.689 -71.753 9.459 1.00 49.57 C ANISOU 1550 CA ILE A 132 4532 5289 9014 -242 -585 -572 C ATOM 1551 C ILE A 132 119.674 -70.995 10.358 1.00 51.85 C ANISOU 1551 C ILE A 132 4714 5632 9355 -265 -671 -717 C ATOM 1552 O ILE A 132 120.763 -70.631 9.907 1.00 51.33 O ANISOU 1552 O ILE A 132 4579 5502 9424 -306 -684 -704 O ATOM 1553 CB ILE A 132 117.557 -70.803 8.947 1.00 51.84 C ANISOU 1553 CB ILE A 132 4851 5453 9392 -261 -556 -609 C ATOM 1554 CG1 ILE A 132 116.613 -71.518 7.944 1.00 51.27 C ANISOU 1554 CG1 ILE A 132 4870 5337 9276 -245 -492 -473 C ATOM 1555 CG2 ILE A 132 118.157 -69.569 8.301 1.00 51.69 C ANISOU 1555 CG2 ILE A 132 4770 5288 9584 -311 -555 -641 C ATOM 1556 CD1 ILE A 132 115.242 -70.867 7.755 1.00 61.68 C ANISOU 1556 CD1 ILE A 132 6213 6594 10628 -242 -474 -497 C ATOM 1557 N PHE A 133 119.285 -70.765 11.621 1.00 48.53 N ANISOU 1557 N PHE A 133 4275 5338 8828 -236 -730 -859 N ATOM 1558 CA PHE A 133 120.074 -70.019 12.596 1.00 50.04 C ANISOU 1558 CA PHE A 133 4367 5606 9041 -255 -833 -1044 C ATOM 1559 C PHE A 133 121.331 -70.786 13.023 1.00 54.62 C ANISOU 1559 C PHE A 133 4877 6330 9545 -239 -891 -993 C ATOM 1560 O PHE A 133 122.302 -70.141 13.421 1.00 55.59 O ANISOU 1560 O PHE A 133 4891 6474 9755 -280 -983 -1118 O ATOM 1561 CB PHE A 133 119.227 -69.627 13.826 1.00 52.82 C ANISOU 1561 CB PHE A 133 4730 6081 9257 -209 -871 -1217 C ATOM 1562 CG PHE A 133 118.012 -68.730 13.633 1.00 54.62 C ANISOU 1562 CG PHE A 133 5004 6181 9569 -215 -821 -1299 C ATOM 1563 CD1 PHE A 133 117.799 -68.057 12.431 1.00 57.27 C ANISOU 1563 CD1 PHE A 133 5348 6289 10122 -270 -763 -1240 C ATOM 1564 CD2 PHE A 133 117.097 -68.540 14.666 1.00 57.74 C ANISOU 1564 CD2 PHE A 133 5425 6692 9823 -152 -824 -1424 C ATOM 1565 CE1 PHE A 133 116.675 -67.243 12.256 1.00 58.68 C ANISOU 1565 CE1 PHE A 133 5557 6354 10386 -264 -714 -1295 C ATOM 1566 CE2 PHE A 133 115.982 -67.714 14.496 1.00 60.97 C ANISOU 1566 CE2 PHE A 133 5866 6978 10323 -149 -768 -1492 C ATOM 1567 CZ PHE A 133 115.776 -67.074 13.291 1.00 58.74 C ANISOU 1567 CZ PHE A 133 5587 6463 10268 -206 -717 -1424 C ATOM 1568 N PHE A 134 121.336 -72.141 12.924 1.00 50.01 N ANISOU 1568 N PHE A 134 4342 5833 8826 -181 -840 -810 N ATOM 1569 CA PHE A 134 122.528 -72.916 13.275 1.00 50.34 C ANISOU 1569 CA PHE A 134 4311 6004 8811 -152 -882 -731 C ATOM 1570 C PHE A 134 123.477 -73.003 12.071 1.00 56.34 C ANISOU 1570 C PHE A 134 5041 6617 9750 -198 -835 -613 C ATOM 1571 O PHE A 134 124.684 -73.160 12.280 1.00 57.94 O ANISOU 1571 O PHE A 134 5141 6887 9988 -200 -887 -592 O ATOM 1572 CB PHE A 134 122.210 -74.306 13.856 1.00 51.12 C ANISOU 1572 CB PHE A 134 4456 6263 8706 -57 -842 -585 C ATOM 1573 CG PHE A 134 121.943 -74.321 15.350 1.00 53.05 C ANISOU 1573 CG PHE A 134 4668 6745 8743 13 -915 -679 C ATOM 1574 CD1 PHE A 134 122.917 -73.911 16.254 1.00 57.21 C ANISOU 1574 CD1 PHE A 134 5081 7441 9216 21 -1044 -802 C ATOM 1575 CD2 PHE A 134 120.737 -74.794 15.853 1.00 53.72 C ANISOU 1575 CD2 PHE A 134 4829 6903 8681 79 -853 -635 C ATOM 1576 CE1 PHE A 134 122.663 -73.913 17.631 1.00 59.35 C ANISOU 1576 CE1 PHE A 134 5326 7963 9259 100 -1115 -897 C ATOM 1577 CE2 PHE A 134 120.485 -74.794 17.226 1.00 57.77 C ANISOU 1577 CE2 PHE A 134 5314 7656 8982 161 -904 -709 C ATOM 1578 CZ PHE A 134 121.450 -74.355 18.108 1.00 57.61 C ANISOU 1578 CZ PHE A 134 5192 7818 8879 177 -1036 -844 C ATOM 1579 N ILE A 135 122.955 -72.839 10.824 1.00 51.66 N ANISOU 1579 N ILE A 135 4525 5837 9265 -228 -740 -538 N ATOM 1580 CA ILE A 135 123.774 -72.788 9.593 1.00 51.01 C ANISOU 1580 CA ILE A 135 4421 5619 9343 -260 -677 -427 C ATOM 1581 C ILE A 135 124.638 -71.518 9.661 1.00 57.15 C ANISOU 1581 C ILE A 135 5067 6328 10318 -333 -742 -540 C ATOM 1582 O ILE A 135 125.818 -71.540 9.295 1.00 56.95 O ANISOU 1582 O ILE A 135 4949 6279 10409 -351 -738 -474 O ATOM 1583 CB ILE A 135 122.897 -72.846 8.302 1.00 52.09 C ANISOU 1583 CB ILE A 135 4672 5607 9511 -262 -571 -334 C ATOM 1584 CG1 ILE A 135 122.440 -74.288 8.010 1.00 50.97 C ANISOU 1584 CG1 ILE A 135 4632 5506 9227 -203 -503 -208 C ATOM 1585 CG2 ILE A 135 123.615 -72.248 7.075 1.00 51.99 C ANISOU 1585 CG2 ILE A 135 4623 5451 9681 -298 -510 -258 C ATOM 1586 CD1 ILE A 135 121.166 -74.389 7.142 1.00 54.26 C ANISOU 1586 CD1 ILE A 135 5166 5832 9619 -203 -441 -175 C ATOM 1587 N THR A 136 124.032 -70.433 10.175 1.00 56.40 N ANISOU 1587 N THR A 136 4957 6198 10275 -371 -798 -715 N ATOM 1588 CA THR A 136 124.632 -69.117 10.383 1.00 58.97 C ANISOU 1588 CA THR A 136 5158 6434 10814 -449 -867 -869 C ATOM 1589 C THR A 136 125.761 -69.221 11.427 1.00 68.17 C ANISOU 1589 C THR A 136 6189 7758 11953 -459 -997 -971 C ATOM 1590 O THR A 136 126.862 -68.732 11.167 1.00 69.27 O ANISOU 1590 O THR A 136 6197 7828 12294 -519 -1027 -976 O ATOM 1591 CB THR A 136 123.543 -68.122 10.778 1.00 63.10 C ANISOU 1591 CB THR A 136 5716 6890 11368 -467 -885 -1040 C ATOM 1592 OG1 THR A 136 122.483 -68.210 9.826 1.00 59.44 O ANISOU 1592 OG1 THR A 136 5369 6316 10898 -444 -774 -915 O ATOM 1593 CG2 THR A 136 124.046 -66.707 10.827 1.00 62.48 C ANISOU 1593 CG2 THR A 136 5516 6662 11563 -552 -933 -1198 C ATOM 1594 N CYS A 137 125.500 -69.904 12.570 1.00 66.71 N ANISOU 1594 N CYS A 137 6030 7798 11521 -394 -1068 -1029 N ATOM 1595 CA CYS A 137 126.476 -70.147 13.638 1.00 69.02 C ANISOU 1595 CA CYS A 137 6201 8296 11726 -379 -1201 -1109 C ATOM 1596 C CYS A 137 127.705 -70.851 13.074 1.00 74.25 C ANISOU 1596 C CYS A 137 6783 8964 12466 -376 -1176 -922 C ATOM 1597 O CYS A 137 128.833 -70.458 13.369 1.00 75.13 O ANISOU 1597 O CYS A 137 6736 9112 12699 -423 -1274 -989 O ATOM 1598 CB CYS A 137 125.847 -70.963 14.761 1.00 69.75 C ANISOU 1598 CB CYS A 137 6358 8635 11508 -279 -1237 -1123 C ATOM 1599 SG CYS A 137 124.660 -70.044 15.770 1.00 74.87 S ANISOU 1599 SG CYS A 137 7058 9343 12045 -269 -1295 -1390 S ATOM 1600 N MET A 138 127.470 -71.881 12.240 1.00 70.27 N ANISOU 1600 N MET A 138 6381 8414 11904 -320 -1042 -696 N ATOM 1601 CA MET A 138 128.488 -72.690 11.586 1.00 69.84 C ANISOU 1601 CA MET A 138 6278 8348 11908 -294 -979 -499 C ATOM 1602 C MET A 138 129.369 -71.861 10.658 1.00 72.60 C ANISOU 1602 C MET A 138 6525 8521 12539 -374 -948 -477 C ATOM 1603 O MET A 138 130.576 -72.106 10.605 1.00 73.50 O ANISOU 1603 O MET A 138 6510 8673 12744 -375 -966 -399 O ATOM 1604 CB MET A 138 127.840 -73.842 10.801 1.00 70.73 C ANISOU 1604 CB MET A 138 6545 8414 11917 -224 -832 -309 C ATOM 1605 CG MET A 138 127.632 -75.106 11.615 1.00 74.85 C ANISOU 1605 CG MET A 138 7105 9115 12218 -128 -837 -225 C ATOM 1606 SD MET A 138 129.049 -75.642 12.617 1.00 82.00 S ANISOU 1606 SD MET A 138 7837 10244 13076 -76 -943 -176 S ATOM 1607 CE MET A 138 130.318 -75.924 11.360 1.00 78.81 C ANISOU 1607 CE MET A 138 7360 9695 12887 -88 -843 -6 C ATOM 1608 N SER A 139 128.774 -70.889 9.933 1.00 66.81 N ANISOU 1608 N SER A 139 5835 7597 11952 -433 -893 -526 N ATOM 1609 CA SER A 139 129.509 -70.016 9.018 1.00 66.61 C ANISOU 1609 CA SER A 139 5709 7388 12213 -503 -841 -480 C ATOM 1610 C SER A 139 130.363 -68.999 9.794 1.00 70.36 C ANISOU 1610 C SER A 139 5988 7865 12879 -593 -984 -663 C ATOM 1611 O SER A 139 131.486 -68.713 9.376 1.00 71.21 O ANISOU 1611 O SER A 139 5948 7903 13206 -637 -972 -593 O ATOM 1612 CB SER A 139 128.557 -69.307 8.060 1.00 69.45 C ANISOU 1612 CB SER A 139 6169 7558 12661 -523 -736 -455 C ATOM 1613 OG SER A 139 128.323 -70.099 6.907 1.00 76.29 O ANISOU 1613 OG SER A 139 7152 8383 13451 -460 -591 -250 O ATOM 1614 N VAL A 140 129.844 -68.484 10.932 1.00 65.65 N ANISOU 1614 N VAL A 140 5387 7355 12204 -616 -1117 -902 N ATOM 1615 CA VAL A 140 130.538 -67.525 11.803 1.00 66.78 C ANISOU 1615 CA VAL A 140 5352 7518 12502 -702 -1279 -1136 C ATOM 1616 C VAL A 140 131.731 -68.220 12.478 1.00 71.54 C ANISOU 1616 C VAL A 140 5815 8332 13035 -681 -1393 -1111 C ATOM 1617 O VAL A 140 132.797 -67.615 12.591 1.00 72.34 O ANISOU 1617 O VAL A 140 5722 8396 13367 -763 -1480 -1182 O ATOM 1618 CB VAL A 140 129.577 -66.878 12.842 1.00 70.42 C ANISOU 1618 CB VAL A 140 5868 8038 12851 -710 -1382 -1412 C ATOM 1619 CG1 VAL A 140 130.325 -65.971 13.817 1.00 72.45 C ANISOU 1619 CG1 VAL A 140 5943 8341 13244 -795 -1569 -1694 C ATOM 1620 CG2 VAL A 140 128.457 -66.107 12.151 1.00 69.20 C ANISOU 1620 CG2 VAL A 140 5825 7660 12809 -730 -1268 -1425 C ATOM 1621 N ASP A 141 131.555 -69.490 12.897 1.00 67.95 N ANISOU 1621 N ASP A 141 5446 8088 12284 -572 -1387 -996 N ATOM 1622 CA ASP A 141 132.591 -70.293 13.553 1.00 68.85 C ANISOU 1622 CA ASP A 141 5438 8425 12298 -524 -1482 -932 C ATOM 1623 C ASP A 141 133.736 -70.610 12.589 1.00 72.57 C ANISOU 1623 C ASP A 141 5799 8794 12978 -536 -1392 -714 C ATOM 1624 O ASP A 141 134.893 -70.391 12.950 1.00 74.46 O ANISOU 1624 O ASP A 141 5837 9102 13352 -578 -1502 -748 O ATOM 1625 CB ASP A 141 132.001 -71.582 14.133 1.00 69.84 C ANISOU 1625 CB ASP A 141 5690 8764 12082 -392 -1460 -822 C ATOM 1626 CG ASP A 141 132.764 -72.091 15.331 1.00 86.13 C ANISOU 1626 CG ASP A 141 7624 11122 13982 -336 -1618 -852 C ATOM 1627 OD1 ASP A 141 132.658 -71.465 16.414 1.00 88.89 O ANISOU 1627 OD1 ASP A 141 7914 11623 14235 -357 -1785 -1095 O ATOM 1628 OD2 ASP A 141 133.478 -73.106 15.190 1.00 95.30 O ANISOU 1628 OD2 ASP A 141 8737 12369 15105 -264 -1576 -636 O ATOM 1629 N ARG A 142 133.413 -71.080 11.357 1.00 67.43 N ANISOU 1629 N ARG A 142 5275 7986 12359 -497 -1194 -502 N ATOM 1630 CA ARG A 142 134.381 -71.384 10.293 1.00 67.55 C ANISOU 1630 CA ARG A 142 5216 7894 12557 -489 -1068 -283 C ATOM 1631 C ARG A 142 135.184 -70.137 9.913 1.00 76.69 C ANISOU 1631 C ARG A 142 6188 8887 14065 -608 -1093 -344 C ATOM 1632 O ARG A 142 136.369 -70.253 9.606 1.00 79.19 O ANISOU 1632 O ARG A 142 6341 9196 14553 -617 -1074 -223 O ATOM 1633 CB ARG A 142 133.691 -71.960 9.052 1.00 63.63 C ANISOU 1633 CB ARG A 142 4910 7263 12002 -426 -860 -100 C ATOM 1634 CG ARG A 142 133.374 -73.441 9.172 1.00 71.97 C ANISOU 1634 CG ARG A 142 6094 8447 12804 -306 -800 32 C ATOM 1635 CD ARG A 142 132.714 -73.988 7.922 1.00 77.14 C ANISOU 1635 CD ARG A 142 6929 8969 13413 -254 -612 175 C ATOM 1636 NE ARG A 142 132.759 -75.451 7.889 1.00 75.32 N ANISOU 1636 NE ARG A 142 6776 8820 13020 -144 -535 319 N ATOM 1637 CZ ARG A 142 132.481 -76.189 6.818 1.00 79.98 C ANISOU 1637 CZ ARG A 142 7500 9317 13574 -83 -374 448 C ATOM 1638 NH1 ARG A 142 132.127 -75.610 5.677 1.00 47.98 N ANISOU 1638 NH1 ARG A 142 3519 5113 9599 -111 -275 465 N ATOM 1639 NH2 ARG A 142 132.550 -77.512 6.883 1.00 76.74 N ANISOU 1639 NH2 ARG A 142 7146 8965 13047 12 -310 558 N ATOM 1640 N TYR A 143 134.551 -68.949 9.962 1.00 74.22 N ANISOU 1640 N TYR A 143 5887 8435 13877 -696 -1129 -524 N ATOM 1641 CA TYR A 143 135.215 -67.682 9.678 1.00 76.21 C ANISOU 1641 CA TYR A 143 5956 8502 14498 -817 -1153 -598 C ATOM 1642 C TYR A 143 136.142 -67.302 10.834 1.00 82.94 C ANISOU 1642 C TYR A 143 6587 9485 15443 -891 -1375 -799 C ATOM 1643 O TYR A 143 137.262 -66.867 10.584 1.00 84.08 O ANISOU 1643 O TYR A 143 6518 9550 15879 -963 -1392 -758 O ATOM 1644 CB TYR A 143 134.182 -66.568 9.405 1.00 77.45 C ANISOU 1644 CB TYR A 143 6198 8460 14769 -877 -1115 -726 C ATOM 1645 CG TYR A 143 134.784 -65.180 9.388 1.00 81.50 C ANISOU 1645 CG TYR A 143 6508 8775 15683 -1012 -1167 -855 C ATOM 1646 CD1 TYR A 143 135.539 -64.739 8.305 1.00 83.96 C ANISOU 1646 CD1 TYR A 143 6698 8889 16315 -1051 -1029 -656 C ATOM 1647 CD2 TYR A 143 134.621 -64.316 10.466 1.00 84.04 C ANISOU 1647 CD2 TYR A 143 6752 9106 16074 -1097 -1348 -1177 C ATOM 1648 CE1 TYR A 143 136.122 -63.476 8.299 1.00 87.39 C ANISOU 1648 CE1 TYR A 143 6924 9120 17161 -1181 -1068 -760 C ATOM 1649 CE2 TYR A 143 135.192 -63.046 10.468 1.00 87.59 C ANISOU 1649 CE2 TYR A 143 7002 9348 16929 -1230 -1399 -1315 C ATOM 1650 CZ TYR A 143 135.940 -62.628 9.379 1.00 97.75 C ANISOU 1650 CZ TYR A 143 8157 10419 18563 -1276 -1256 -1097 C ATOM 1651 OH TYR A 143 136.508 -61.373 9.369 1.00103.41 O ANISOU 1651 OH TYR A 143 8661 10907 19724 -1414 -1294 -1217 O ATOM 1652 N GLN A 144 135.665 -67.463 12.089 1.00 80.58 N ANISOU 1652 N GLN A 144 6330 9395 14891 -869 -1543 -1015 N ATOM 1653 CA GLN A 144 136.390 -67.161 13.329 1.00 83.34 C ANISOU 1653 CA GLN A 144 6492 9929 15245 -921 -1783 -1246 C ATOM 1654 C GLN A 144 137.667 -68.009 13.453 1.00 89.10 C ANISOU 1654 C GLN A 144 7057 10829 15970 -880 -1830 -1076 C ATOM 1655 O GLN A 144 138.688 -67.516 13.943 1.00 90.32 O ANISOU 1655 O GLN A 144 6973 11032 16314 -964 -1990 -1196 O ATOM 1656 CB GLN A 144 135.478 -67.398 14.543 1.00 84.70 C ANISOU 1656 CB GLN A 144 6790 10334 15060 -858 -1911 -1452 C ATOM 1657 CG GLN A 144 135.607 -66.336 15.635 1.00108.95 C ANISOU 1657 CG GLN A 144 9732 13466 18200 -952 -2135 -1828 C ATOM 1658 CD GLN A 144 134.563 -66.443 16.729 1.00128.60 C ANISOU 1658 CD GLN A 144 12366 16163 20335 -878 -2225 -2035 C ATOM 1659 OE1 GLN A 144 133.533 -67.107 16.595 1.00120.95 O ANISOU 1659 OE1 GLN A 144 11607 15233 19118 -776 -2101 -1910 O ATOM 1660 NE2 GLN A 144 134.805 -65.772 17.847 1.00127.25 N ANISOU 1660 NE2 GLN A 144 12079 16134 20136 -927 -2444 -2366 N ATOM 1661 N SER A 145 137.603 -69.276 12.997 1.00 85.10 N ANISOU 1661 N SER A 145 6668 10402 15266 -753 -1690 -803 N ATOM 1662 CA SER A 145 138.720 -70.217 13.024 1.00 86.24 C ANISOU 1662 CA SER A 145 6679 10694 15394 -686 -1695 -601 C ATOM 1663 C SER A 145 139.733 -69.919 11.909 1.00 92.28 C ANISOU 1663 C SER A 145 7292 11254 16516 -740 -1568 -419 C ATOM 1664 O SER A 145 140.936 -70.094 12.131 1.00 94.58 O ANISOU 1664 O SER A 145 7361 11639 16938 -751 -1645 -354 O ATOM 1665 CB SER A 145 138.217 -71.654 12.911 1.00 87.03 C ANISOU 1665 CB SER A 145 6966 10915 15186 -528 -1570 -385 C ATOM 1666 OG SER A 145 137.665 -71.923 11.635 1.00 91.99 O ANISOU 1666 OG SER A 145 7767 11331 15852 -495 -1336 -208 O ATOM 1667 N VAL A 146 139.247 -69.471 10.723 1.00 87.27 N ANISOU 1667 N VAL A 146 6767 10357 16033 -765 -1373 -325 N ATOM 1668 CA VAL A 146 140.064 -69.134 9.549 1.00 87.94 C ANISOU 1668 CA VAL A 146 6732 10237 16442 -800 -1213 -128 C ATOM 1669 C VAL A 146 140.984 -67.927 9.856 1.00 96.94 C ANISOU 1669 C VAL A 146 7586 11283 17963 -954 -1348 -274 C ATOM 1670 O VAL A 146 142.119 -67.903 9.376 1.00 98.84 O ANISOU 1670 O VAL A 146 7626 11469 18460 -975 -1294 -113 O ATOM 1671 CB VAL A 146 139.171 -68.921 8.296 1.00 89.59 C ANISOU 1671 CB VAL A 146 7144 10227 16668 -774 -986 -4 C ATOM 1672 CG1 VAL A 146 139.643 -67.770 7.404 1.00 90.46 C ANISOU 1672 CG1 VAL A 146 7113 10081 17176 -870 -884 58 C ATOM 1673 CG2 VAL A 146 139.055 -70.215 7.502 1.00 87.57 C ANISOU 1673 CG2 VAL A 146 7051 10020 16203 -627 -797 250 C ATOM 1674 N ILE A 147 140.526 -66.970 10.685 1.00 95.17 N ANISOU 1674 N ILE A 147 7334 11043 17785 -1058 -1525 -584 N ATOM 1675 CA ILE A 147 141.322 -65.794 11.046 1.00 98.32 C ANISOU 1675 CA ILE A 147 7460 11334 18562 -1217 -1671 -772 C ATOM 1676 C ILE A 147 142.275 -66.129 12.236 1.00106.18 C ANISOU 1676 C ILE A 147 8243 12606 19495 -1234 -1927 -906 C ATOM 1677 O ILE A 147 143.456 -65.773 12.168 1.00108.99 O ANISOU 1677 O ILE A 147 8323 12918 20169 -1318 -1986 -875 O ATOM 1678 CB ILE A 147 140.427 -64.542 11.319 1.00101.68 C ANISOU 1678 CB ILE A 147 7942 11583 19110 -1322 -1732 -1059 C ATOM 1679 CG1 ILE A 147 139.339 -64.321 10.223 1.00 99.45 C ANISOU 1679 CG1 ILE A 147 7889 11077 18821 -1279 -1491 -913 C ATOM 1680 CG2 ILE A 147 141.255 -63.277 11.548 1.00106.33 C ANISOU 1680 CG2 ILE A 147 8241 11998 20159 -1499 -1857 -1250 C ATOM 1681 CD1 ILE A 147 139.790 -64.126 8.728 1.00105.99 C ANISOU 1681 CD1 ILE A 147 8667 11665 19937 -1275 -1237 -590 C ATOM 1682 N TYR A 148 141.789 -66.875 13.262 1.00102.26 N ANISOU 1682 N TYR A 148 7865 12402 18587 -1142 -2064 -1017 N ATOM 1683 CA TYR A 148 142.537 -67.284 14.469 1.00134.02 C ANISOU 1683 CA TYR A 148 11715 16743 22464 -1126 -2315 -1135 C ATOM 1684 C TYR A 148 143.948 -67.868 14.169 1.00142.92 C ANISOU 1684 C TYR A 148 12604 17939 23760 -1104 -2302 -888 C ATOM 1685 O TYR A 148 144.102 -68.969 13.637 1.00 94.45 O ANISOU 1685 O TYR A 148 6546 11856 17486 -972 -2138 -585 O ATOM 1686 CB TYR A 148 141.722 -68.295 15.293 1.00133.84 C ANISOU 1686 CB TYR A 148 11900 17013 21940 -975 -2363 -1145 C ATOM 1687 N ALA A 160 129.843 -70.153 24.179 1.00106.85 N ANISOU 1687 N ALA A 160 10268 15507 14824 32 -2556 -2388 N ATOM 1688 CA ALA A 160 129.264 -71.168 23.298 1.00103.71 C ANISOU 1688 CA ALA A 160 10004 14951 14452 83 -2325 -2020 C ATOM 1689 C ALA A 160 128.072 -71.877 23.944 1.00106.63 C ANISOU 1689 C ALA A 160 10523 15505 14488 238 -2216 -1908 C ATOM 1690 O ALA A 160 127.146 -72.262 23.230 1.00103.38 O ANISOU 1690 O ALA A 160 10252 14892 14136 247 -2025 -1734 O ATOM 1691 CB ALA A 160 130.317 -72.186 22.900 1.00104.19 C ANISOU 1691 CB ALA A 160 9965 15057 14567 110 -2312 -1719 C ATOM 1692 N SER A 161 128.096 -72.043 25.291 1.00105.62 N ANISOU 1692 N SER A 161 10354 15768 14009 363 -2338 -2004 N ATOM 1693 CA SER A 161 127.030 -72.657 26.107 1.00105.20 C ANISOU 1693 CA SER A 161 10416 15948 13608 530 -2244 -1906 C ATOM 1694 C SER A 161 125.879 -71.658 26.321 1.00107.72 C ANISOU 1694 C SER A 161 10848 16175 13905 509 -2206 -2186 C ATOM 1695 O SER A 161 124.873 -71.972 26.967 1.00107.23 O ANISOU 1695 O SER A 161 10884 16276 13582 638 -2115 -2141 O ATOM 1696 CB SER A 161 127.591 -73.123 27.450 1.00111.68 C ANISOU 1696 CB SER A 161 11134 17244 14056 681 -2395 -1904 C ATOM 1697 OG SER A 161 128.011 -72.032 28.252 1.00123.45 O ANISOU 1697 OG SER A 161 12535 18910 15459 644 -2618 -2311 O ATOM 1698 N TYR A 162 126.057 -70.449 25.760 1.00103.22 N ANISOU 1698 N TYR A 162 10252 15333 13633 349 -2267 -2460 N ATOM 1699 CA TYR A 162 125.135 -69.323 25.771 1.00102.56 C ANISOU 1699 CA TYR A 162 10252 15083 13633 299 -2235 -2748 C ATOM 1700 C TYR A 162 124.448 -69.174 24.405 1.00101.13 C ANISOU 1700 C TYR A 162 10172 14481 13772 203 -2047 -2602 C ATOM 1701 O TYR A 162 123.275 -68.820 24.365 1.00100.21 O ANISOU 1701 O TYR A 162 10170 14263 13643 227 -1933 -2658 O ATOM 1702 CB TYR A 162 125.892 -68.032 26.134 1.00106.48 C ANISOU 1702 CB TYR A 162 10626 15563 14270 188 -2444 -3166 C ATOM 1703 N ILE A 163 125.175 -69.445 23.297 1.00 94.38 N ANISOU 1703 N ILE A 163 9269 13400 13192 103 -2014 -2412 N ATOM 1704 CA ILE A 163 124.693 -69.320 21.919 1.00 90.63 C ANISOU 1704 CA ILE A 163 8873 12549 13012 14 -1853 -2264 C ATOM 1705 C ILE A 163 123.613 -70.368 21.626 1.00 90.05 C ANISOU 1705 C ILE A 163 8942 12472 12800 109 -1667 -1977 C ATOM 1706 O ILE A 163 122.525 -69.980 21.207 1.00 88.70 O ANISOU 1706 O ILE A 163 8873 12125 12704 95 -1556 -1998 O ATOM 1707 CB ILE A 163 125.869 -69.379 20.894 1.00 93.19 C ANISOU 1707 CB ILE A 163 9097 12684 13629 -96 -1869 -2137 C ATOM 1708 CG1 ILE A 163 126.745 -68.120 20.996 1.00 96.12 C ANISOU 1708 CG1 ILE A 163 9322 12963 14234 -222 -2027 -2436 C ATOM 1709 CG2 ILE A 163 125.370 -69.547 19.455 1.00 91.03 C ANISOU 1709 CG2 ILE A 163 8918 12087 13581 -150 -1687 -1920 C ATOM 1710 CD1 ILE A 163 128.218 -68.381 20.932 1.00107.19 C ANISOU 1710 CD1 ILE A 163 10554 14437 15735 -268 -2144 -2377 C ATOM 1711 N VAL A 164 123.896 -71.673 21.847 1.00 84.39 N ANISOU 1711 N VAL A 164 8220 11939 11904 205 -1634 -1710 N ATOM 1712 CA VAL A 164 122.930 -72.751 21.579 1.00 81.63 C ANISOU 1712 CA VAL A 164 7986 11572 11458 288 -1459 -1432 C ATOM 1713 C VAL A 164 121.552 -72.437 22.264 1.00 83.74 C ANISOU 1713 C VAL A 164 8347 11918 11551 363 -1395 -1535 C ATOM 1714 O VAL A 164 120.578 -72.367 21.507 1.00 81.50 O ANISOU 1714 O VAL A 164 8158 11411 11397 328 -1266 -1470 O ATOM 1715 CB VAL A 164 123.454 -74.194 21.874 1.00 85.82 C ANISOU 1715 CB VAL A 164 8482 12294 11831 393 -1430 -1136 C ATOM 1716 CG1 VAL A 164 124.366 -74.264 23.097 1.00 88.48 C ANISOU 1716 CG1 VAL A 164 8697 12985 11937 475 -1594 -1214 C ATOM 1717 CG2 VAL A 164 122.328 -75.212 21.961 1.00 84.66 C ANISOU 1717 CG2 VAL A 164 8439 12173 11556 493 -1263 -900 C ATOM 1718 N PRO A 165 121.416 -72.135 23.597 1.00 81.07 N ANISOU 1718 N PRO A 165 7984 11879 10939 461 -1480 -1714 N ATOM 1719 CA PRO A 165 120.069 -71.825 24.125 1.00 80.38 C ANISOU 1719 CA PRO A 165 7988 11839 10712 537 -1389 -1797 C ATOM 1720 C PRO A 165 119.440 -70.564 23.520 1.00 82.25 C ANISOU 1720 C PRO A 165 8272 11790 11189 432 -1364 -2025 C ATOM 1721 O PRO A 165 118.218 -70.516 23.376 1.00 80.79 O ANISOU 1721 O PRO A 165 8174 11516 11007 465 -1232 -1981 O ATOM 1722 CB PRO A 165 120.291 -71.671 25.632 1.00 85.13 C ANISOU 1722 CB PRO A 165 8541 12835 10970 664 -1504 -1972 C ATOM 1723 CG PRO A 165 121.732 -71.426 25.795 1.00 91.43 C ANISOU 1723 CG PRO A 165 9212 13726 11799 607 -1696 -2097 C ATOM 1724 CD PRO A 165 122.420 -72.130 24.686 1.00 85.04 C ANISOU 1724 CD PRO A 165 8374 12711 11225 524 -1654 -1833 C ATOM 1725 N LEU A 166 120.262 -69.565 23.131 1.00 78.75 N ANISOU 1725 N LEU A 166 7759 11189 10973 307 -1482 -2247 N ATOM 1726 CA LEU A 166 119.776 -68.338 22.488 1.00 78.03 C ANISOU 1726 CA LEU A 166 7694 10797 11156 205 -1453 -2440 C ATOM 1727 C LEU A 166 119.199 -68.605 21.092 1.00 79.45 C ANISOU 1727 C LEU A 166 7944 10672 11573 140 -1303 -2198 C ATOM 1728 O LEU A 166 118.205 -67.982 20.725 1.00 78.16 O ANISOU 1728 O LEU A 166 7841 10332 11525 125 -1215 -2252 O ATOM 1729 CB LEU A 166 120.874 -67.275 22.372 1.00 79.48 C ANISOU 1729 CB LEU A 166 7765 10868 11565 83 -1605 -2701 C ATOM 1730 CG LEU A 166 120.573 -65.946 23.125 1.00 86.93 C ANISOU 1730 CG LEU A 166 8692 11810 12528 75 -1680 -3104 C ATOM 1731 CD1 LEU A 166 121.826 -65.246 23.535 1.00 93.24 C ANISOU 1731 CD1 LEU A 166 9351 12652 13422 -8 -1879 -3377 C ATOM 1732 CD2 LEU A 166 119.581 -64.972 22.405 1.00 86.20 C ANISOU 1732 CD2 LEU A 166 8663 11383 12705 19 -1558 -3181 C ATOM 1733 N VAL A 167 119.817 -69.530 20.321 1.00 75.22 N ANISOU 1733 N VAL A 167 7395 10083 11101 109 -1276 -1937 N ATOM 1734 CA VAL A 167 119.400 -69.899 18.960 1.00 72.60 C ANISOU 1734 CA VAL A 167 7127 9495 10964 53 -1150 -1711 C ATOM 1735 C VAL A 167 118.020 -70.571 19.012 1.00 76.20 C ANISOU 1735 C VAL A 167 7684 9978 11290 135 -1016 -1557 C ATOM 1736 O VAL A 167 117.203 -70.365 18.112 1.00 74.79 O ANISOU 1736 O VAL A 167 7564 9587 11264 94 -923 -1490 O ATOM 1737 CB VAL A 167 120.459 -70.777 18.245 1.00 75.53 C ANISOU 1737 CB VAL A 167 7459 9835 11405 19 -1154 -1497 C ATOM 1738 CG1 VAL A 167 119.970 -71.249 16.883 1.00 73.06 C ANISOU 1738 CG1 VAL A 167 7223 9292 11245 -20 -1024 -1281 C ATOM 1739 CG2 VAL A 167 121.772 -70.021 18.092 1.00 76.53 C ANISOU 1739 CG2 VAL A 167 7467 9903 11707 -71 -1275 -1639 C ATOM 1740 N TRP A 168 117.750 -71.330 20.084 1.00 73.88 N ANISOU 1740 N TRP A 168 7397 9952 10721 253 -1006 -1499 N ATOM 1741 CA TRP A 168 116.460 -71.981 20.285 1.00 72.67 C ANISOU 1741 CA TRP A 168 7317 9845 10451 336 -875 -1348 C ATOM 1742 C TRP A 168 115.428 -70.961 20.772 1.00 78.49 C ANISOU 1742 C TRP A 168 8084 10572 11165 367 -847 -1553 C ATOM 1743 O TRP A 168 114.271 -71.044 20.376 1.00 76.84 O ANISOU 1743 O TRP A 168 7930 10251 11014 376 -733 -1460 O ATOM 1744 CB TRP A 168 116.585 -73.168 21.244 1.00 71.74 C ANISOU 1744 CB TRP A 168 7181 10010 10066 462 -855 -1176 C ATOM 1745 CG TRP A 168 117.278 -74.341 20.621 1.00 71.13 C ANISOU 1745 CG TRP A 168 7089 9889 10048 445 -830 -921 C ATOM 1746 CD1 TRP A 168 118.577 -74.713 20.795 1.00 74.62 C ANISOU 1746 CD1 TRP A 168 7459 10440 10455 449 -921 -884 C ATOM 1747 CD2 TRP A 168 116.724 -75.250 19.669 1.00 68.91 C ANISOU 1747 CD2 TRP A 168 6862 9426 9895 418 -709 -686 C ATOM 1748 NE1 TRP A 168 118.861 -75.811 20.025 1.00 72.43 N ANISOU 1748 NE1 TRP A 168 7191 10053 10274 435 -848 -633 N ATOM 1749 CE2 TRP A 168 117.741 -76.167 19.325 1.00 72.11 C ANISOU 1749 CE2 TRP A 168 7232 9833 10333 414 -720 -520 C ATOM 1750 CE3 TRP A 168 115.457 -75.391 19.078 1.00 68.97 C ANISOU 1750 CE3 TRP A 168 6936 9272 9998 398 -595 -607 C ATOM 1751 CZ2 TRP A 168 117.533 -77.211 18.418 1.00 69.92 C ANISOU 1751 CZ2 TRP A 168 6996 9393 10179 391 -618 -300 C ATOM 1752 CZ3 TRP A 168 115.249 -76.434 18.191 1.00 69.12 C ANISOU 1752 CZ3 TRP A 168 6987 9143 10132 368 -511 -390 C ATOM 1753 CH2 TRP A 168 116.284 -77.320 17.855 1.00 69.44 C ANISOU 1753 CH2 TRP A 168 7004 9178 10204 364 -521 -251 C ATOM 1754 N CYS A 169 115.856 -69.975 21.582 1.00 78.58 N ANISOU 1754 N CYS A 169 8053 10690 11114 377 -953 -1843 N ATOM 1755 CA CYS A 169 114.982 -68.914 22.072 1.00 80.68 C ANISOU 1755 CA CYS A 169 8344 10936 11374 410 -927 -2077 C ATOM 1756 C CYS A 169 114.523 -68.014 20.910 1.00 82.54 C ANISOU 1756 C CYS A 169 8600 10821 11939 301 -879 -2119 C ATOM 1757 O CYS A 169 113.346 -67.664 20.854 1.00 81.66 O ANISOU 1757 O CYS A 169 8533 10630 11862 337 -777 -2126 O ATOM 1758 CB CYS A 169 115.670 -68.107 23.167 1.00 84.70 C ANISOU 1758 CB CYS A 169 8799 11633 11752 440 -1067 -2404 C ATOM 1759 SG CYS A 169 114.750 -66.637 23.688 1.00 91.18 S ANISOU 1759 SG CYS A 169 9646 12377 12620 468 -1041 -2754 S ATOM 1760 N MET A 170 115.443 -67.668 19.980 1.00 78.32 N ANISOU 1760 N MET A 170 8025 10090 11645 179 -942 -2122 N ATOM 1761 CA MET A 170 115.168 -66.853 18.785 1.00 76.91 C ANISOU 1761 CA MET A 170 7853 9587 11782 81 -895 -2118 C ATOM 1762 C MET A 170 114.221 -67.585 17.829 1.00 75.80 C ANISOU 1762 C MET A 170 7780 9337 11685 85 -770 -1840 C ATOM 1763 O MET A 170 113.412 -66.941 17.161 1.00 73.02 O ANISOU 1763 O MET A 170 7449 8790 11505 61 -702 -1834 O ATOM 1764 CB MET A 170 116.465 -66.487 18.052 1.00 79.59 C ANISOU 1764 CB MET A 170 8121 9779 12339 -34 -978 -2138 C ATOM 1765 CG MET A 170 117.203 -65.317 18.671 1.00 86.15 C ANISOU 1765 CG MET A 170 8868 10592 13272 -80 -1095 -2458 C ATOM 1766 SD MET A 170 118.704 -64.895 17.740 1.00 90.88 S ANISOU 1766 SD MET A 170 9359 10994 14177 -222 -1173 -2443 S ATOM 1767 CE MET A 170 119.838 -66.142 18.329 1.00 87.78 C ANISOU 1767 CE MET A 170 8920 10896 13536 -187 -1274 -2340 C ATOM 1768 N ALA A 171 114.321 -68.932 17.776 1.00 71.33 N ANISOU 1768 N ALA A 171 7238 8894 10971 119 -743 -1613 N ATOM 1769 CA ALA A 171 113.460 -69.788 16.958 1.00 69.40 C ANISOU 1769 CA ALA A 171 7048 8566 10753 121 -640 -1365 C ATOM 1770 C ALA A 171 112.042 -69.857 17.565 1.00 75.34 C ANISOU 1770 C ALA A 171 7832 9393 11399 208 -549 -1352 C ATOM 1771 O ALA A 171 111.062 -69.923 16.820 1.00 73.76 O ANISOU 1771 O ALA A 171 7661 9058 11307 191 -472 -1239 O ATOM 1772 CB ALA A 171 114.066 -71.175 16.841 1.00 69.03 C ANISOU 1772 CB ALA A 171 7006 8617 10605 133 -638 -1159 C ATOM 1773 N CYS A 172 111.938 -69.804 18.914 1.00 74.64 N ANISOU 1773 N CYS A 172 7731 9532 11096 305 -558 -1470 N ATOM 1774 CA CYS A 172 110.673 -69.809 19.665 1.00 75.66 C ANISOU 1774 CA CYS A 172 7879 9767 11101 408 -461 -1470 C ATOM 1775 C CYS A 172 109.921 -68.527 19.408 1.00 77.94 C ANISOU 1775 C CYS A 172 8172 9885 11558 391 -429 -1636 C ATOM 1776 O CYS A 172 108.711 -68.561 19.213 1.00 77.63 O ANISOU 1776 O CYS A 172 8147 9787 11563 424 -327 -1544 O ATOM 1777 CB CYS A 172 110.921 -70.000 21.159 1.00 79.08 C ANISOU 1777 CB CYS A 172 8295 10510 11241 530 -484 -1568 C ATOM 1778 SG CYS A 172 111.494 -71.659 21.613 1.00 83.51 S ANISOU 1778 SG CYS A 172 8842 11301 11587 594 -476 -1299 S ATOM 1779 N LEU A 173 110.638 -67.388 19.442 1.00 73.92 N ANISOU 1779 N LEU A 173 7637 9289 11160 341 -515 -1882 N ATOM 1780 CA LEU A 173 110.117 -66.034 19.227 1.00 73.75 C ANISOU 1780 CA LEU A 173 7607 9076 11339 322 -490 -2067 C ATOM 1781 C LEU A 173 109.642 -65.827 17.784 1.00 73.69 C ANISOU 1781 C LEU A 173 7605 8796 11598 242 -438 -1900 C ATOM 1782 O LEU A 173 108.588 -65.227 17.578 1.00 73.92 O ANISOU 1782 O LEU A 173 7636 8711 11737 270 -357 -1907 O ATOM 1783 CB LEU A 173 111.201 -64.995 19.581 1.00 75.42 C ANISOU 1783 CB LEU A 173 7774 9248 11636 272 -605 -2359 C ATOM 1784 CG LEU A 173 111.120 -64.320 20.949 1.00 82.86 C ANISOU 1784 CG LEU A 173 8708 10358 12418 361 -635 -2669 C ATOM 1785 CD1 LEU A 173 111.379 -65.302 22.090 1.00 84.31 C ANISOU 1785 CD1 LEU A 173 8902 10900 12232 464 -668 -2642 C ATOM 1786 CD2 LEU A 173 112.130 -63.224 21.045 1.00 86.77 C ANISOU 1786 CD2 LEU A 173 9146 10741 13084 280 -753 -2961 C ATOM 1787 N SER A 174 110.403 -66.345 16.798 1.00 66.47 N ANISOU 1787 N SER A 174 6689 7795 10771 154 -482 -1744 N ATOM 1788 CA SER A 174 110.102 -66.227 15.367 1.00 63.78 C ANISOU 1788 CA SER A 174 6356 7234 10645 85 -446 -1578 C ATOM 1789 C SER A 174 108.910 -67.097 14.952 1.00 65.28 C ANISOU 1789 C SER A 174 6578 7445 10780 118 -364 -1359 C ATOM 1790 O SER A 174 108.357 -66.875 13.879 1.00 63.41 O ANISOU 1790 O SER A 174 6343 7051 10700 82 -333 -1245 O ATOM 1791 CB SER A 174 111.324 -66.592 14.527 1.00 65.86 C ANISOU 1791 CB SER A 174 6610 7435 10980 -1 -509 -1487 C ATOM 1792 OG SER A 174 112.464 -65.805 14.831 1.00 73.80 O ANISOU 1792 OG SER A 174 7563 8405 12073 -46 -588 -1673 O ATOM 1793 N SER A 175 108.518 -68.083 15.789 1.00 62.79 N ANISOU 1793 N SER A 175 6279 7328 10252 188 -332 -1293 N ATOM 1794 CA SER A 175 107.388 -68.985 15.512 1.00 61.62 C ANISOU 1794 CA SER A 175 6142 7201 10071 214 -255 -1090 C ATOM 1795 C SER A 175 106.133 -68.628 16.341 1.00 66.74 C ANISOU 1795 C SER A 175 6772 7919 10668 309 -165 -1135 C ATOM 1796 O SER A 175 105.174 -69.398 16.353 1.00 66.41 O ANISOU 1796 O SER A 175 6720 7922 10590 341 -94 -973 O ATOM 1797 CB SER A 175 107.786 -70.442 15.745 1.00 63.66 C ANISOU 1797 CB SER A 175 6415 7598 10176 223 -257 -934 C ATOM 1798 OG SER A 175 108.172 -70.669 17.088 1.00 74.90 O ANISOU 1798 OG SER A 175 7829 9239 11391 306 -260 -1010 O ATOM 1799 N LEU A 176 106.130 -67.452 17.002 1.00 65.48 N ANISOU 1799 N LEU A 176 6600 7754 10524 353 -163 -1359 N ATOM 1800 CA LEU A 176 104.993 -66.950 17.781 1.00 67.04 C ANISOU 1800 CA LEU A 176 6781 8006 10684 456 -67 -1433 C ATOM 1801 C LEU A 176 103.814 -66.503 16.872 1.00 71.23 C ANISOU 1801 C LEU A 176 7283 8352 11428 442 0 -1326 C ATOM 1802 O LEU A 176 102.675 -66.841 17.223 1.00 71.55 O ANISOU 1802 O LEU A 176 7300 8461 11425 513 94 -1228 O ATOM 1803 CB LEU A 176 105.400 -65.818 18.728 1.00 68.89 C ANISOU 1803 CB LEU A 176 7014 8280 10881 508 -88 -1736 C ATOM 1804 CG LEU A 176 106.016 -66.285 20.034 1.00 75.14 C ANISOU 1804 CG LEU A 176 7819 9347 11383 585 -120 -1843 C ATOM 1805 CD1 LEU A 176 106.735 -65.170 20.720 1.00 77.33 C ANISOU 1805 CD1 LEU A 176 8093 9638 11653 597 -192 -2175 C ATOM 1806 CD2 LEU A 176 104.974 -66.903 20.955 1.00 79.22 C ANISOU 1806 CD2 LEU A 176 8335 10070 11694 719 0 -1747 C ATOM 1807 N PRO A 177 104.023 -65.833 15.692 1.00 66.10 N ANISOU 1807 N PRO A 177 6626 7485 11005 358 -42 -1309 N ATOM 1808 CA PRO A 177 102.872 -65.511 14.825 1.00 64.69 C ANISOU 1808 CA PRO A 177 6409 7167 11002 358 13 -1176 C ATOM 1809 C PRO A 177 102.202 -66.756 14.233 1.00 64.73 C ANISOU 1809 C PRO A 177 6405 7221 10967 331 22 -930 C ATOM 1810 O PRO A 177 101.019 -66.685 13.919 1.00 64.62 O ANISOU 1810 O PRO A 177 6343 7167 11041 358 77 -826 O ATOM 1811 CB PRO A 177 103.491 -64.646 13.732 1.00 66.22 C ANISOU 1811 CB PRO A 177 6598 7155 11409 281 -41 -1192 C ATOM 1812 CG PRO A 177 104.811 -64.176 14.300 1.00 71.48 C ANISOU 1812 CG PRO A 177 7283 7827 12048 256 -103 -1400 C ATOM 1813 CD PRO A 177 105.277 -65.331 15.088 1.00 66.81 C ANISOU 1813 CD PRO A 177 6725 7455 11203 271 -133 -1389 C ATOM 1814 N THR A 178 102.923 -67.892 14.108 1.00 59.14 N ANISOU 1814 N THR A 178 5733 6595 10142 281 -31 -845 N ATOM 1815 CA THR A 178 102.353 -69.165 13.636 1.00 57.63 C ANISOU 1815 CA THR A 178 5532 6441 9925 250 -23 -639 C ATOM 1816 C THR A 178 101.442 -69.713 14.739 1.00 61.67 C ANISOU 1816 C THR A 178 6006 7098 10327 339 74 -590 C ATOM 1817 O THR A 178 100.305 -70.101 14.468 1.00 61.00 O ANISOU 1817 O THR A 178 5867 6996 10314 344 123 -454 O ATOM 1818 CB THR A 178 103.456 -70.172 13.248 1.00 63.19 C ANISOU 1818 CB THR A 178 6283 7171 10554 182 -92 -579 C ATOM 1819 OG1 THR A 178 104.257 -69.632 12.205 1.00 66.02 O ANISOU 1819 OG1 THR A 178 6668 7401 11017 112 -164 -609 O ATOM 1820 CG2 THR A 178 102.903 -71.482 12.788 1.00 59.13 C ANISOU 1820 CG2 THR A 178 5758 6672 10039 148 -82 -397 C ATOM 1821 N PHE A 179 101.946 -69.715 15.985 1.00 59.11 N ANISOU 1821 N PHE A 179 5703 6929 9829 413 102 -697 N ATOM 1822 CA PHE A 179 101.225 -70.202 17.155 1.00 60.39 C ANISOU 1822 CA PHE A 179 5832 7264 9849 520 209 -647 C ATOM 1823 C PHE A 179 99.979 -69.394 17.433 1.00 65.42 C ANISOU 1823 C PHE A 179 6417 7875 10564 597 306 -678 C ATOM 1824 O PHE A 179 98.977 -69.975 17.828 1.00 65.80 O ANISOU 1824 O PHE A 179 6409 7997 10593 653 405 -537 O ATOM 1825 CB PHE A 179 102.125 -70.204 18.403 1.00 63.49 C ANISOU 1825 CB PHE A 179 6261 7852 10010 598 204 -780 C ATOM 1826 CG PHE A 179 101.450 -70.791 19.622 1.00 66.28 C ANISOU 1826 CG PHE A 179 6582 8418 10182 727 325 -698 C ATOM 1827 CD1 PHE A 179 101.378 -72.169 19.803 1.00 68.74 C ANISOU 1827 CD1 PHE A 179 6872 8823 10425 734 369 -472 C ATOM 1828 CD2 PHE A 179 100.865 -69.967 20.576 1.00 69.68 C ANISOU 1828 CD2 PHE A 179 7001 8950 10524 849 410 -838 C ATOM 1829 CE1 PHE A 179 100.746 -72.709 20.924 1.00 71.06 C ANISOU 1829 CE1 PHE A 179 7124 9314 10561 863 499 -362 C ATOM 1830 CE2 PHE A 179 100.216 -70.509 21.686 1.00 74.16 C ANISOU 1830 CE2 PHE A 179 7536 9730 10912 984 540 -741 C ATOM 1831 CZ PHE A 179 100.169 -71.876 21.857 1.00 71.95 C ANISOU 1831 CZ PHE A 179 7226 9547 10563 991 586 -491 C ATOM 1832 N TYR A 180 100.043 -68.069 17.271 1.00 62.83 N ANISOU 1832 N TYR A 180 6098 7437 10338 605 290 -855 N ATOM 1833 CA TYR A 180 98.909 -67.206 17.546 1.00 64.29 C ANISOU 1833 CA TYR A 180 6232 7581 10614 690 391 -899 C ATOM 1834 C TYR A 180 97.816 -67.319 16.474 1.00 66.18 C ANISOU 1834 C TYR A 180 6400 7686 11060 644 406 -706 C ATOM 1835 O TYR A 180 96.642 -67.304 16.838 1.00 66.83 O ANISOU 1835 O TYR A 180 6412 7804 11176 720 512 -629 O ATOM 1836 CB TYR A 180 99.371 -65.744 17.699 1.00 67.76 C ANISOU 1836 CB TYR A 180 6696 7917 11131 712 372 -1156 C ATOM 1837 CG TYR A 180 98.270 -64.802 18.136 1.00 72.99 C ANISOU 1837 CG TYR A 180 7310 8540 11882 821 493 -1231 C ATOM 1838 CD1 TYR A 180 97.851 -64.753 19.462 1.00 77.47 C ANISOU 1838 CD1 TYR A 180 7878 9288 12271 959 602 -1332 C ATOM 1839 CD2 TYR A 180 97.630 -63.974 17.219 1.00 74.11 C ANISOU 1839 CD2 TYR A 180 7402 8474 12282 800 507 -1187 C ATOM 1840 CE1 TYR A 180 96.810 -63.912 19.864 1.00 81.32 C ANISOU 1840 CE1 TYR A 180 8319 9738 12842 1071 731 -1400 C ATOM 1841 CE2 TYR A 180 96.594 -63.123 17.609 1.00 77.04 C ANISOU 1841 CE2 TYR A 180 7718 8798 12753 909 630 -1241 C ATOM 1842 CZ TYR A 180 96.186 -63.094 18.934 1.00 87.59 C ANISOU 1842 CZ TYR A 180 9059 10304 13917 1044 745 -1355 C ATOM 1843 OH TYR A 180 95.162 -62.259 19.325 1.00 89.67 O ANISOU 1843 OH TYR A 180 9269 10521 14282 1164 881 -1414 O ATOM 1844 N PHE A 181 98.181 -67.465 15.177 1.00 61.08 N ANISOU 1844 N PHE A 181 5764 6905 10538 528 300 -624 N ATOM 1845 CA PHE A 181 97.195 -67.461 14.090 1.00 60.30 C ANISOU 1845 CA PHE A 181 5594 6695 10622 487 289 -464 C ATOM 1846 C PHE A 181 96.815 -68.836 13.456 1.00 63.72 C ANISOU 1846 C PHE A 181 5995 7158 11057 409 246 -263 C ATOM 1847 O PHE A 181 95.684 -68.913 12.966 1.00 63.58 O ANISOU 1847 O PHE A 181 5889 7103 11166 405 263 -138 O ATOM 1848 CB PHE A 181 97.643 -66.510 12.965 1.00 61.05 C ANISOU 1848 CB PHE A 181 5706 6619 10873 430 210 -503 C ATOM 1849 CG PHE A 181 97.674 -65.049 13.365 1.00 63.13 C ANISOU 1849 CG PHE A 181 5963 6789 11233 501 265 -672 C ATOM 1850 CD1 PHE A 181 96.497 -64.329 13.526 1.00 66.80 C ANISOU 1850 CD1 PHE A 181 6350 7206 11824 587 360 -652 C ATOM 1851 CD2 PHE A 181 98.881 -64.392 13.569 1.00 64.79 C ANISOU 1851 CD2 PHE A 181 6237 6947 11434 481 224 -855 C ATOM 1852 CE1 PHE A 181 96.529 -62.984 13.908 1.00 69.09 C ANISOU 1852 CE1 PHE A 181 6636 7388 12229 657 422 -822 C ATOM 1853 CE2 PHE A 181 98.913 -63.048 13.954 1.00 68.71 C ANISOU 1853 CE2 PHE A 181 6722 7334 12053 539 275 -1033 C ATOM 1854 CZ PHE A 181 97.737 -62.350 14.114 1.00 68.03 C ANISOU 1854 CZ PHE A 181 6567 7189 12092 629 377 -1019 C ATOM 1855 N ARG A 182 97.693 -69.881 13.431 1.00 59.86 N ANISOU 1855 N ARG A 182 5565 6723 10455 347 191 -235 N ATOM 1856 CA ARG A 182 97.331 -71.182 12.797 1.00 59.88 C ANISOU 1856 CA ARG A 182 5534 6723 10493 268 153 -68 C ATOM 1857 C ARG A 182 96.092 -71.825 13.433 1.00 66.74 C ANISOU 1857 C ARG A 182 6303 7663 11394 315 255 64 C ATOM 1858 O ARG A 182 96.078 -72.026 14.646 1.00 68.25 O ANISOU 1858 O ARG A 182 6490 7975 11467 402 358 59 O ATOM 1859 CB ARG A 182 98.478 -72.219 12.839 1.00 58.34 C ANISOU 1859 CB ARG A 182 5414 6570 10182 215 106 -60 C ATOM 1860 CG ARG A 182 99.508 -72.104 11.731 1.00 62.05 C ANISOU 1860 CG ARG A 182 5957 6948 10670 130 -9 -107 C ATOM 1861 CD ARG A 182 99.089 -72.767 10.441 1.00 62.38 C ANISOU 1861 CD ARG A 182 5977 6912 10813 41 -85 -5 C ATOM 1862 NE ARG A 182 99.689 -72.083 9.296 1.00 62.11 N ANISOU 1862 NE ARG A 182 5990 6791 10817 -3 -172 -50 N ATOM 1863 CZ ARG A 182 99.345 -72.289 8.030 1.00 78.85 C ANISOU 1863 CZ ARG A 182 8098 8857 13006 -63 -251 12 C ATOM 1864 NH1 ARG A 182 98.417 -73.185 7.723 1.00 72.24 N ANISOU 1864 NH1 ARG A 182 7197 8027 12222 -103 -270 99 N ATOM 1865 NH2 ARG A 182 99.933 -71.604 7.058 1.00 65.55 N ANISOU 1865 NH2 ARG A 182 6455 7115 11337 -81 -311 -11 N ATOM 1866 N ASP A 183 95.051 -72.129 12.627 1.00 62.82 N ANISOU 1866 N ASP A 183 5713 7101 11055 263 228 186 N ATOM 1867 CA ASP A 183 93.834 -72.773 13.137 1.00 63.61 C ANISOU 1867 CA ASP A 183 5691 7249 11230 293 323 330 C ATOM 1868 C ASP A 183 93.039 -73.426 12.019 1.00 65.89 C ANISOU 1868 C ASP A 183 5888 7457 11691 187 235 446 C ATOM 1869 O ASP A 183 93.202 -73.064 10.856 1.00 63.76 O ANISOU 1869 O ASP A 183 5641 7111 11474 121 111 409 O ATOM 1870 CB ASP A 183 92.933 -71.797 13.921 1.00 67.34 C ANISOU 1870 CB ASP A 183 6093 7764 11728 417 448 315 C ATOM 1871 CG ASP A 183 92.120 -72.476 15.019 1.00 82.73 C ANISOU 1871 CG ASP A 183 7951 9824 13661 495 601 442 C ATOM 1872 OD1 ASP A 183 92.549 -73.546 15.511 1.00 82.85 O ANISOU 1872 OD1 ASP A 183 7986 9905 13589 482 631 512 O ATOM 1873 OD2 ASP A 183 91.059 -71.945 15.379 1.00 92.19 O ANISOU 1873 OD2 ASP A 183 9049 11038 14939 576 701 488 O ATOM 1874 N VAL A 184 92.186 -74.404 12.366 1.00 63.26 N ANISOU 1874 N VAL A 184 5443 7146 11447 172 298 587 N ATOM 1875 CA VAL A 184 91.359 -75.094 11.385 1.00 62.90 C ANISOU 1875 CA VAL A 184 5289 7026 11585 64 207 680 C ATOM 1876 C VAL A 184 90.129 -74.226 11.094 1.00 66.56 C ANISOU 1876 C VAL A 184 5623 7478 12187 102 213 727 C ATOM 1877 O VAL A 184 89.415 -73.837 12.015 1.00 66.54 O ANISOU 1877 O VAL A 184 5543 7531 12209 205 355 784 O ATOM 1878 CB VAL A 184 90.992 -76.530 11.822 1.00 67.32 C ANISOU 1878 CB VAL A 184 5765 7583 12231 17 269 813 C ATOM 1879 CG1 VAL A 184 89.894 -77.114 10.944 1.00 67.96 C ANISOU 1879 CG1 VAL A 184 5694 7587 12541 -89 183 896 C ATOM 1880 CG2 VAL A 184 92.222 -77.429 11.793 1.00 66.24 C ANISOU 1880 CG2 VAL A 184 5749 7428 11992 -35 234 773 C ATOM 1881 N ARG A 185 89.927 -73.885 9.809 1.00 62.52 N ANISOU 1881 N ARG A 185 5093 6910 11753 32 62 706 N ATOM 1882 CA ARG A 185 88.789 -73.093 9.351 1.00 63.25 C ANISOU 1882 CA ARG A 185 5052 6994 11987 64 41 768 C ATOM 1883 C ARG A 185 88.077 -73.829 8.231 1.00 69.63 C ANISOU 1883 C ARG A 185 5745 7774 12936 -57 -111 832 C ATOM 1884 O ARG A 185 88.725 -74.483 7.415 1.00 69.05 O ANISOU 1884 O ARG A 185 5748 7674 12814 -156 -241 771 O ATOM 1885 CB ARG A 185 89.208 -71.687 8.895 1.00 61.13 C ANISOU 1885 CB ARG A 185 4859 6701 11668 127 9 686 C ATOM 1886 CG ARG A 185 89.656 -70.777 10.031 1.00 70.50 C ANISOU 1886 CG ARG A 185 6122 7905 12762 253 159 601 C ATOM 1887 CD ARG A 185 88.528 -70.290 10.934 1.00 75.43 C ANISOU 1887 CD ARG A 185 6620 8562 13477 368 315 668 C ATOM 1888 NE ARG A 185 89.049 -69.579 12.106 1.00 77.48 N ANISOU 1888 NE ARG A 185 6969 8857 13614 487 456 550 N ATOM 1889 CZ ARG A 185 89.303 -70.153 13.278 1.00 85.01 C ANISOU 1889 CZ ARG A 185 7958 9903 14440 536 571 535 C ATOM 1890 NH1 ARG A 185 89.069 -71.446 13.455 1.00 76.11 N ANISOU 1890 NH1 ARG A 185 6777 8821 13320 477 580 655 N ATOM 1891 NH2 ARG A 185 89.785 -69.436 14.285 1.00 59.14 N ANISOU 1891 NH2 ARG A 185 4763 6676 11031 649 678 401 N ATOM 1892 N THR A 186 86.745 -73.744 8.214 1.00 68.96 N ANISOU 1892 N THR A 186 5471 7701 13028 -45 -95 947 N ATOM 1893 CA THR A 186 85.914 -74.412 7.222 1.00 70.76 C ANISOU 1893 CA THR A 186 5555 7917 13412 -159 -249 1002 C ATOM 1894 C THR A 186 85.863 -73.599 5.926 1.00 76.10 C ANISOU 1894 C THR A 186 6236 8611 14067 -166 -417 972 C ATOM 1895 O THR A 186 85.584 -72.397 5.962 1.00 76.68 O ANISOU 1895 O THR A 186 6287 8700 14148 -60 -370 1006 O ATOM 1896 CB THR A 186 84.495 -74.625 7.774 1.00 84.35 C ANISOU 1896 CB THR A 186 7049 9652 15348 -139 -160 1152 C ATOM 1897 OG1 THR A 186 83.962 -73.348 8.128 1.00 90.74 O ANISOU 1897 OG1 THR A 186 7808 10494 16177 -2 -63 1201 O ATOM 1898 CG2 THR A 186 84.456 -75.538 8.994 1.00 82.40 C ANISOU 1898 CG2 THR A 186 6774 9396 15138 -130 13 1222 C ATOM 1899 N ILE A 187 86.124 -74.251 4.791 1.00 72.90 N ANISOU 1899 N ILE A 187 5857 8208 13635 -280 -604 911 N ATOM 1900 CA ILE A 187 86.048 -73.623 3.480 1.00 73.16 C ANISOU 1900 CA ILE A 187 5883 8289 13624 -285 -775 899 C ATOM 1901 C ILE A 187 84.798 -74.230 2.828 1.00 80.14 C ANISOU 1901 C ILE A 187 6556 9213 14681 -371 -918 958 C ATOM 1902 O ILE A 187 84.850 -75.341 2.291 1.00 79.47 O ANISOU 1902 O ILE A 187 6461 9117 14615 -497 -1044 884 O ATOM 1903 CB ILE A 187 87.389 -73.803 2.704 1.00 74.80 C ANISOU 1903 CB ILE A 187 6293 8494 13632 -326 -870 773 C ATOM 1904 CG1 ILE A 187 88.456 -72.818 3.231 1.00 73.50 C ANISOU 1904 CG1 ILE A 187 6292 8299 13336 -224 -743 738 C ATOM 1905 CG2 ILE A 187 87.232 -73.616 1.195 1.00 76.81 C ANISOU 1905 CG2 ILE A 187 6526 8827 13832 -358 -1076 762 C ATOM 1906 CD1 ILE A 187 89.304 -73.313 4.318 1.00 78.84 C ANISOU 1906 CD1 ILE A 187 7083 8929 13945 -223 -611 674 C ATOM 1907 N GLU A 188 83.648 -73.523 2.978 1.00 79.88 N ANISOU 1907 N GLU A 188 6341 9216 14795 -302 -886 1089 N ATOM 1908 CA GLU A 188 82.306 -73.926 2.514 1.00 82.51 C ANISOU 1908 CA GLU A 188 6428 9595 15327 -366 -1006 1172 C ATOM 1909 C GLU A 188 82.246 -74.196 1.012 1.00 88.11 C ANISOU 1909 C GLU A 188 7114 10388 15975 -453 -1274 1106 C ATOM 1910 O GLU A 188 81.470 -75.050 0.595 1.00 89.13 O ANISOU 1910 O GLU A 188 7082 10538 16245 -567 -1411 1094 O ATOM 1911 CB GLU A 188 81.263 -72.853 2.889 1.00 85.07 C ANISOU 1911 CB GLU A 188 6584 9951 15789 -241 -910 1332 C ATOM 1912 N TYR A 189 83.086 -73.498 0.211 1.00 84.51 N ANISOU 1912 N TYR A 189 6816 9985 15310 -400 -1345 1058 N ATOM 1913 CA TYR A 189 83.203 -73.653 -1.243 1.00 85.23 C ANISOU 1913 CA TYR A 189 6921 10188 15275 -451 -1585 992 C ATOM 1914 C TYR A 189 83.619 -75.070 -1.637 1.00 90.69 C ANISOU 1914 C TYR A 189 7673 10854 15930 -604 -1706 820 C ATOM 1915 O TYR A 189 83.076 -75.621 -2.612 1.00 91.73 O ANISOU 1915 O TYR A 189 7701 11074 16077 -691 -1923 757 O ATOM 1916 CB TYR A 189 84.229 -72.640 -1.807 1.00 84.79 C ANISOU 1916 CB TYR A 189 7048 10170 14998 -346 -1574 993 C ATOM 1917 N LEU A 190 84.553 -75.680 -0.872 1.00 86.47 N ANISOU 1917 N LEU A 190 7296 10201 15356 -636 -1570 737 N ATOM 1918 CA LEU A 190 85.094 -77.025 -1.105 1.00 86.15 C ANISOU 1918 CA LEU A 190 7334 10099 15300 -767 -1641 577 C ATOM 1919 C LEU A 190 84.605 -78.096 -0.092 1.00 89.32 C ANISOU 1919 C LEU A 190 7626 10373 15940 -856 -1537 594 C ATOM 1920 O LEU A 190 84.872 -79.277 -0.311 1.00 88.26 O ANISOU 1920 O LEU A 190 7517 10166 15853 -974 -1600 471 O ATOM 1921 CB LEU A 190 86.628 -76.963 -1.107 1.00 84.21 C ANISOU 1921 CB LEU A 190 7348 9817 14831 -730 -1568 486 C ATOM 1922 CG LEU A 190 87.305 -76.233 -2.267 1.00 88.73 C ANISOU 1922 CG LEU A 190 8045 10502 15166 -668 -1678 449 C ATOM 1923 CD1 LEU A 190 88.624 -75.662 -1.848 1.00 86.58 C ANISOU 1923 CD1 LEU A 190 7977 10180 14740 -586 -1529 444 C ATOM 1924 CD2 LEU A 190 87.509 -77.143 -3.469 1.00 93.45 C ANISOU 1924 CD2 LEU A 190 8682 11161 15664 -764 -1881 287 C ATOM 1925 N GLY A 191 83.909 -77.663 0.973 1.00 85.86 N ANISOU 1925 N GLY A 191 7067 9907 15651 -789 -1371 749 N ATOM 1926 CA GLY A 191 83.408 -78.528 2.048 1.00 85.56 C ANISOU 1926 CA GLY A 191 6911 9763 15836 -840 -1230 818 C ATOM 1927 C GLY A 191 84.556 -79.215 2.753 1.00 85.45 C ANISOU 1927 C GLY A 191 7079 9652 15736 -849 -1094 759 C ATOM 1928 O GLY A 191 84.511 -80.417 3.022 1.00 85.88 O ANISOU 1928 O GLY A 191 7087 9603 15940 -950 -1074 737 O ATOM 1929 N VAL A 192 85.614 -78.426 2.998 1.00 78.74 N ANISOU 1929 N VAL A 192 6431 8831 14656 -742 -1007 735 N ATOM 1930 CA VAL A 192 86.892 -78.875 3.524 1.00 76.27 C ANISOU 1930 CA VAL A 192 6313 8458 14210 -732 -904 670 C ATOM 1931 C VAL A 192 87.370 -77.941 4.632 1.00 78.50 C ANISOU 1931 C VAL A 192 6684 8767 14377 -589 -708 738 C ATOM 1932 O VAL A 192 87.416 -76.715 4.480 1.00 77.95 O ANISOU 1932 O VAL A 192 6649 8757 14211 -495 -705 750 O ATOM 1933 CB VAL A 192 87.897 -79.002 2.338 1.00 78.24 C ANISOU 1933 CB VAL A 192 6730 8724 14274 -776 -1060 511 C ATOM 1934 CG1 VAL A 192 89.284 -78.485 2.667 1.00 75.82 C ANISOU 1934 CG1 VAL A 192 6640 8420 13748 -692 -964 470 C ATOM 1935 CG2 VAL A 192 87.942 -80.426 1.814 1.00 78.69 C ANISOU 1935 CG2 VAL A 192 6769 8699 14430 -918 -1164 401 C ATOM 1936 N ASN A 193 87.699 -78.564 5.762 1.00 73.99 N ANISOU 1936 N ASN A 193 6138 8148 13825 -571 -545 784 N ATOM 1937 CA ASN A 193 88.249 -77.953 6.965 1.00 72.37 C ANISOU 1937 CA ASN A 193 6024 7979 13496 -443 -358 824 C ATOM 1938 C ASN A 193 89.729 -77.878 6.760 1.00 72.73 C ANISOU 1938 C ASN A 193 6282 8019 13331 -434 -383 705 C ATOM 1939 O ASN A 193 90.376 -78.919 6.696 1.00 71.59 O ANISOU 1939 O ASN A 193 6202 7821 13179 -502 -397 666 O ATOM 1940 CB ASN A 193 87.906 -78.813 8.194 1.00 75.79 C ANISOU 1940 CB ASN A 193 6370 8387 14037 -429 -184 945 C ATOM 1941 CG ASN A 193 86.501 -78.713 8.713 1.00105.99 C ANISOU 1941 CG ASN A 193 9981 12231 18059 -398 -96 1094 C ATOM 1942 OD1 ASN A 193 85.604 -78.138 8.089 1.00105.17 O ANISOU 1942 OD1 ASN A 193 9758 12148 18055 -408 -184 1113 O ATOM 1943 ND2 ASN A 193 86.272 -79.330 9.859 1.00 96.80 N ANISOU 1943 ND2 ASN A 193 8751 11066 16963 -357 86 1222 N ATOM 1944 N ALA A 194 90.280 -76.672 6.599 1.00 67.43 N ANISOU 1944 N ALA A 194 5714 7393 12513 -354 -389 649 N ATOM 1945 CA ALA A 194 91.709 -76.535 6.337 1.00 65.48 C ANISOU 1945 CA ALA A 194 5654 7139 12084 -349 -417 542 C ATOM 1946 C ALA A 194 92.457 -75.847 7.462 1.00 69.47 C ANISOU 1946 C ALA A 194 6252 7679 12463 -241 -277 522 C ATOM 1947 O ALA A 194 91.908 -74.961 8.120 1.00 69.65 O ANISOU 1947 O ALA A 194 6222 7738 12506 -150 -187 557 O ATOM 1948 CB ALA A 194 91.929 -75.781 5.040 1.00 65.64 C ANISOU 1948 CB ALA A 194 5724 7174 12043 -360 -560 483 C ATOM 1949 N CYS A 195 93.721 -76.278 7.674 1.00 65.05 N ANISOU 1949 N CYS A 195 5828 7112 11776 -249 -263 457 N ATOM 1950 CA CYS A 195 94.676 -75.745 8.638 1.00 64.06 C ANISOU 1950 CA CYS A 195 5803 7030 11506 -164 -166 408 C ATOM 1951 C CYS A 195 95.318 -74.536 7.969 1.00 63.89 C ANISOU 1951 C CYS A 195 5865 6995 11416 -140 -231 317 C ATOM 1952 O CYS A 195 96.143 -74.702 7.065 1.00 62.88 O ANISOU 1952 O CYS A 195 5822 6836 11234 -193 -323 266 O ATOM 1953 CB CYS A 195 95.697 -76.823 9.015 1.00 65.04 C ANISOU 1953 CB CYS A 195 6010 7152 11551 -191 -142 399 C ATOM 1954 SG CYS A 195 96.965 -76.298 10.210 1.00 69.30 S ANISOU 1954 SG CYS A 195 6660 7774 11897 -91 -50 331 S ATOM 1955 N ILE A 196 94.857 -73.322 8.330 1.00 58.73 N ANISOU 1955 N ILE A 196 5174 6355 10787 -58 -178 309 N ATOM 1956 CA ILE A 196 95.304 -72.063 7.713 1.00 57.47 C ANISOU 1956 CA ILE A 196 5063 6157 10616 -28 -221 248 C ATOM 1957 C ILE A 196 95.634 -70.982 8.752 1.00 60.37 C ANISOU 1957 C ILE A 196 5461 6532 10947 71 -115 165 C ATOM 1958 O ILE A 196 95.228 -71.092 9.910 1.00 61.79 O ANISOU 1958 O ILE A 196 5604 6768 11104 133 -9 165 O ATOM 1959 CB ILE A 196 94.242 -71.533 6.699 1.00 61.36 C ANISOU 1959 CB ILE A 196 5455 6627 11231 -33 -292 325 C ATOM 1960 CG1 ILE A 196 92.828 -71.403 7.312 1.00 62.58 C ANISOU 1960 CG1 ILE A 196 5464 6806 11508 16 -216 409 C ATOM 1961 CG2 ILE A 196 94.212 -72.360 5.419 1.00 62.94 C ANISOU 1961 CG2 ILE A 196 5656 6829 11430 -130 -434 354 C ATOM 1962 CD1 ILE A 196 92.431 -69.985 7.616 1.00 68.14 C ANISOU 1962 CD1 ILE A 196 6129 7484 12276 121 -141 402 C ATOM 1963 N MET A 197 96.356 -69.929 8.329 1.00 54.66 N ANISOU 1963 N MET A 197 4796 5749 10224 88 -142 92 N ATOM 1964 CA MET A 197 96.661 -68.784 9.184 1.00 53.89 C ANISOU 1964 CA MET A 197 4719 5630 10128 172 -57 -17 C ATOM 1965 C MET A 197 95.386 -67.957 9.258 1.00 57.55 C ANISOU 1965 C MET A 197 5075 6063 10729 244 4 34 C ATOM 1966 O MET A 197 94.969 -67.358 8.264 1.00 55.86 O ANISOU 1966 O MET A 197 4813 5785 10627 240 -45 106 O ATOM 1967 CB MET A 197 97.869 -67.974 8.653 1.00 55.53 C ANISOU 1967 CB MET A 197 5006 5757 10337 154 -103 -102 C ATOM 1968 CG MET A 197 99.227 -68.644 8.881 1.00 57.94 C ANISOU 1968 CG MET A 197 5409 6098 10508 105 -137 -174 C ATOM 1969 SD MET A 197 99.839 -68.540 10.590 1.00 62.62 S ANISOU 1969 SD MET A 197 6039 6776 10978 168 -57 -330 S ATOM 1970 CE MET A 197 100.794 -67.023 10.533 1.00 59.43 C ANISOU 1970 CE MET A 197 5665 6257 10657 182 -66 -487 C ATOM 1971 N ALA A 198 94.708 -68.034 10.408 1.00 56.61 N ANISOU 1971 N ALA A 198 4907 6008 10594 316 114 22 N ATOM 1972 CA ALA A 198 93.433 -67.365 10.663 1.00 58.67 C ANISOU 1972 CA ALA A 198 5054 6254 10983 400 199 75 C ATOM 1973 C ALA A 198 93.630 -65.892 11.105 1.00 66.26 C ANISOU 1973 C ALA A 198 6034 7135 12006 493 277 -58 C ATOM 1974 O ALA A 198 93.373 -65.538 12.265 1.00 66.93 O ANISOU 1974 O ALA A 198 6112 7263 12053 588 396 -151 O ATOM 1975 CB ALA A 198 92.644 -68.148 11.708 1.00 60.16 C ANISOU 1975 CB ALA A 198 5179 6553 11128 446 303 133 C ATOM 1976 N PHE A 199 94.078 -65.029 10.161 1.00 64.64 N ANISOU 1976 N PHE A 199 5848 6809 11902 471 214 -67 N ATOM 1977 CA PHE A 199 94.295 -63.590 10.401 1.00 66.31 C ANISOU 1977 CA PHE A 199 6065 6897 12232 546 282 -186 C ATOM 1978 C PHE A 199 92.965 -62.861 10.606 1.00 74.72 C ANISOU 1978 C PHE A 199 7012 7922 13455 651 386 -124 C ATOM 1979 O PHE A 199 91.961 -63.304 10.030 1.00 74.87 O ANISOU 1979 O PHE A 199 6933 7982 13534 642 359 55 O ATOM 1980 CB PHE A 199 95.056 -62.937 9.234 1.00 67.43 C ANISOU 1980 CB PHE A 199 6237 6913 12472 496 201 -157 C ATOM 1981 CG PHE A 199 96.433 -63.470 8.955 1.00 67.27 C ANISOU 1981 CG PHE A 199 6323 6910 12326 403 113 -216 C ATOM 1982 CD1 PHE A 199 97.428 -63.407 9.922 1.00 70.02 C ANISOU 1982 CD1 PHE A 199 6750 7274 12579 401 136 -407 C ATOM 1983 CD2 PHE A 199 96.758 -63.968 7.703 1.00 68.26 C ANISOU 1983 CD2 PHE A 199 6465 7041 12431 327 6 -86 C ATOM 1984 CE1 PHE A 199 98.705 -63.885 9.658 1.00 70.03 C ANISOU 1984 CE1 PHE A 199 6835 7292 12483 321 57 -447 C ATOM 1985 CE2 PHE A 199 98.037 -64.446 7.436 1.00 69.99 C ANISOU 1985 CE2 PHE A 199 6777 7272 12542 253 -59 -135 C ATOM 1986 CZ PHE A 199 99.002 -64.403 8.416 1.00 68.35 C ANISOU 1986 CZ PHE A 199 6637 7073 12261 249 -32 -307 C ATOM 1987 N PRO A 200 92.910 -61.738 11.379 1.00 74.81 N ANISOU 1987 N PRO A 200 7022 7849 13553 751 502 -273 N ATOM 1988 CA PRO A 200 91.621 -61.029 11.539 1.00 76.59 C ANISOU 1988 CA PRO A 200 7128 8026 13947 864 614 -204 C ATOM 1989 C PRO A 200 91.115 -60.525 10.182 1.00 81.83 C ANISOU 1989 C PRO A 200 7700 8587 14807 853 555 -7 C ATOM 1990 O PRO A 200 91.902 -59.927 9.433 1.00 81.57 O ANISOU 1990 O PRO A 200 7707 8437 14847 816 497 -14 O ATOM 1991 CB PRO A 200 91.937 -59.897 12.523 1.00 79.66 C ANISOU 1991 CB PRO A 200 7557 8320 14390 961 735 -443 C ATOM 1992 CG PRO A 200 93.400 -59.711 12.457 1.00 83.09 C ANISOU 1992 CG PRO A 200 8107 8697 14766 882 655 -603 C ATOM 1993 CD PRO A 200 93.991 -61.061 12.128 1.00 76.96 C ANISOU 1993 CD PRO A 200 7390 8063 13787 767 532 -519 C ATOM 1994 N PRO A 201 89.912 -60.987 9.748 1.00 78.88 N ANISOU 1994 N PRO A 201 7201 8284 14486 866 541 193 N ATOM 1995 CA PRO A 201 89.415 -60.629 8.406 1.00 79.00 C ANISOU 1995 CA PRO A 201 7119 8248 14648 857 458 397 C ATOM 1996 C PRO A 201 89.228 -59.126 8.219 1.00 85.50 C ANISOU 1996 C PRO A 201 7889 8894 15704 964 550 406 C ATOM 1997 O PRO A 201 89.043 -58.677 7.083 1.00 86.27 O ANISOU 1997 O PRO A 201 7920 8939 15920 969 487 578 O ATOM 1998 CB PRO A 201 88.085 -61.379 8.316 1.00 81.24 C ANISOU 1998 CB PRO A 201 7262 8654 14953 864 444 566 C ATOM 1999 CG PRO A 201 88.202 -62.485 9.327 1.00 85.14 C ANISOU 1999 CG PRO A 201 7808 9269 15272 824 476 476 C ATOM 2000 CD PRO A 201 88.930 -61.826 10.458 1.00 80.91 C ANISOU 2000 CD PRO A 201 7382 8678 14684 894 601 253 C ATOM 2001 N GLU A 202 89.318 -58.354 9.330 1.00 82.79 N ANISOU 2001 N GLU A 202 7576 8459 15422 1054 701 216 N ATOM 2002 CA GLU A 202 89.258 -56.894 9.367 1.00 84.01 C ANISOU 2002 CA GLU A 202 7693 8406 15821 1158 814 167 C ATOM 2003 C GLU A 202 90.362 -56.293 8.459 1.00 87.70 C ANISOU 2003 C GLU A 202 8220 8732 16372 1098 741 176 C ATOM 2004 O GLU A 202 90.060 -55.390 7.676 1.00 89.92 O ANISOU 2004 O GLU A 202 8414 8877 16875 1156 767 327 O ATOM 2005 CB GLU A 202 89.394 -56.397 10.816 1.00 86.36 C ANISOU 2005 CB GLU A 202 8047 8657 16107 1242 966 -109 C ATOM 2006 N LYS A 203 91.616 -56.831 8.534 1.00 80.72 N ANISOU 2006 N LYS A 203 7469 7887 15315 987 654 45 N ATOM 2007 CA LYS A 203 92.783 -56.447 7.715 1.00 78.86 C ANISOU 2007 CA LYS A 203 7292 7542 15130 917 583 57 C ATOM 2008 C LYS A 203 93.594 -57.730 7.364 1.00 79.74 C ANISOU 2008 C LYS A 203 7501 7818 14978 786 438 66 C ATOM 2009 O LYS A 203 94.763 -57.866 7.742 1.00 78.54 O ANISOU 2009 O LYS A 203 7453 7651 14738 721 412 -101 O ATOM 2010 CB LYS A 203 93.644 -55.383 8.430 1.00 81.29 C ANISOU 2010 CB LYS A 203 7651 7651 15584 938 674 -190 C ATOM 2011 N TYR A 204 92.935 -58.675 6.647 1.00 74.58 N ANISOU 2011 N TYR A 204 6803 7320 14212 752 344 257 N ATOM 2012 CA TYR A 204 93.457 -59.989 6.256 1.00 72.27 C ANISOU 2012 CA TYR A 204 6587 7184 13690 639 213 281 C ATOM 2013 C TYR A 204 94.542 -59.879 5.180 1.00 76.00 C ANISOU 2013 C TYR A 204 7119 7612 14144 576 129 342 C ATOM 2014 O TYR A 204 95.544 -60.602 5.251 1.00 74.70 O ANISOU 2014 O TYR A 204 7058 7503 13821 492 69 253 O ATOM 2015 CB TYR A 204 92.311 -60.897 5.762 1.00 73.20 C ANISOU 2015 CB TYR A 204 6615 7451 13746 626 140 453 C ATOM 2016 CG TYR A 204 92.681 -62.361 5.652 1.00 73.22 C ANISOU 2016 CG TYR A 204 6686 7601 13532 515 31 437 C ATOM 2017 CD1 TYR A 204 92.466 -63.237 6.712 1.00 74.87 C ANISOU 2017 CD1 TYR A 204 6914 7899 13634 497 68 346 C ATOM 2018 CD2 TYR A 204 93.225 -62.877 4.479 1.00 73.23 C ANISOU 2018 CD2 TYR A 204 6730 7652 13442 439 -99 521 C ATOM 2019 CE1 TYR A 204 92.836 -64.580 6.630 1.00 74.44 C ANISOU 2019 CE1 TYR A 204 6917 7952 13413 399 -17 339 C ATOM 2020 CE2 TYR A 204 93.592 -64.220 4.380 1.00 73.05 C ANISOU 2020 CE2 TYR A 204 6773 7741 13242 342 -189 489 C ATOM 2021 CZ TYR A 204 93.392 -65.069 5.460 1.00 79.05 C ANISOU 2021 CZ TYR A 204 7546 8563 13927 319 -147 401 C ATOM 2022 OH TYR A 204 93.743 -66.392 5.370 1.00 75.87 O ANISOU 2022 OH TYR A 204 7198 8246 13383 227 -223 383 O ATOM 2023 N ALA A 205 94.330 -59.004 4.174 1.00 72.91 N ANISOU 2023 N ALA A 205 6656 7133 13914 628 133 514 N ATOM 2024 CA ALA A 205 95.270 -58.784 3.070 1.00 71.95 C ANISOU 2024 CA ALA A 205 6574 6975 13791 594 77 616 C ATOM 2025 C ALA A 205 96.576 -58.171 3.572 1.00 73.76 C ANISOU 2025 C ALA A 205 6880 7049 14097 564 139 447 C ATOM 2026 O ALA A 205 97.652 -58.584 3.135 1.00 72.75 O ANISOU 2026 O ALA A 205 6829 6948 13863 492 80 437 O ATOM 2027 CB ALA A 205 94.642 -57.885 2.011 1.00 74.28 C ANISOU 2027 CB ALA A 205 6755 7213 14255 682 93 860 C ATOM 2028 N GLN A 206 96.470 -57.201 4.506 1.00 69.75 N ANISOU 2028 N GLN A 206 6342 6380 13778 621 256 303 N ATOM 2029 CA GLN A 206 97.577 -56.484 5.149 1.00 69.19 C ANISOU 2029 CA GLN A 206 6320 6143 13825 596 315 99 C ATOM 2030 C GLN A 206 98.468 -57.481 5.914 1.00 67.26 C ANISOU 2030 C GLN A 206 6189 6023 13343 504 248 -101 C ATOM 2031 O GLN A 206 99.694 -57.420 5.797 1.00 65.83 O ANISOU 2031 O GLN A 206 6061 5789 13163 438 219 -170 O ATOM 2032 CB GLN A 206 97.013 -55.375 6.083 1.00 73.01 C ANISOU 2032 CB GLN A 206 6746 6458 14538 687 448 -46 C ATOM 2033 CG GLN A 206 98.044 -54.696 6.998 1.00104.64 C ANISOU 2033 CG GLN A 206 10798 10306 18654 657 497 -331 C ATOM 2034 CD GLN A 206 97.422 -53.787 8.037 1.00135.23 C ANISOU 2034 CD GLN A 206 14631 14049 22703 749 621 -524 C ATOM 2035 OE1 GLN A 206 97.280 -54.148 9.215 1.00130.92 O ANISOU 2035 OE1 GLN A 206 14135 13605 22005 763 636 -749 O ATOM 2036 NE2 GLN A 206 97.082 -52.574 7.631 1.00133.09 N ANISOU 2036 NE2 GLN A 206 14267 13545 22755 823 722 -442 N ATOM 2037 N TRP A 207 97.837 -58.394 6.681 1.00 60.27 N ANISOU 2037 N TRP A 207 5328 5304 12270 506 232 -170 N ATOM 2038 CA TRP A 207 98.507 -59.400 7.495 1.00 57.46 C ANISOU 2038 CA TRP A 207 5064 5085 11683 441 182 -329 C ATOM 2039 C TRP A 207 99.249 -60.429 6.650 1.00 57.96 C ANISOU 2039 C TRP A 207 5189 5253 11581 350 72 -224 C ATOM 2040 O TRP A 207 100.361 -60.782 7.007 1.00 56.94 O ANISOU 2040 O TRP A 207 5131 5146 11357 290 37 -344 O ATOM 2041 CB TRP A 207 97.504 -60.100 8.413 1.00 55.74 C ANISOU 2041 CB TRP A 207 4834 5013 11332 484 214 -368 C ATOM 2042 CG TRP A 207 97.456 -59.512 9.789 1.00 57.52 C ANISOU 2042 CG TRP A 207 5067 5207 11579 549 309 -601 C ATOM 2043 CD1 TRP A 207 96.460 -58.748 10.324 1.00 61.79 C ANISOU 2043 CD1 TRP A 207 5541 5687 12252 655 421 -641 C ATOM 2044 CD2 TRP A 207 98.470 -59.616 10.798 1.00 57.07 C ANISOU 2044 CD2 TRP A 207 5089 5192 11402 523 299 -839 C ATOM 2045 NE1 TRP A 207 96.783 -58.382 11.612 1.00 61.88 N ANISOU 2045 NE1 TRP A 207 5594 5702 12217 699 484 -905 N ATOM 2046 CE2 TRP A 207 98.010 -58.905 11.931 1.00 62.15 C ANISOU 2046 CE2 TRP A 207 5715 5809 12090 618 402 -1031 C ATOM 2047 CE3 TRP A 207 99.722 -60.260 10.862 1.00 56.89 C ANISOU 2047 CE3 TRP A 207 5144 5240 11232 436 210 -908 C ATOM 2048 CZ2 TRP A 207 98.749 -58.829 13.119 1.00 61.94 C ANISOU 2048 CZ2 TRP A 207 5749 5843 11942 626 406 -1300 C ATOM 2049 CZ3 TRP A 207 100.452 -60.188 12.040 1.00 58.97 C ANISOU 2049 CZ3 TRP A 207 5456 5559 11391 442 212 -1154 C ATOM 2050 CH2 TRP A 207 99.967 -59.478 13.152 1.00 61.29 C ANISOU 2050 CH2 TRP A 207 5735 5843 11711 535 302 -1354 C ATOM 2051 N SER A 208 98.653 -60.898 5.541 1.00 53.05 N ANISOU 2051 N SER A 208 4536 4699 10923 344 15 -11 N ATOM 2052 CA SER A 208 99.266 -61.880 4.643 1.00 50.92 C ANISOU 2052 CA SER A 208 4325 4530 10494 270 -86 81 C ATOM 2053 C SER A 208 100.511 -61.298 3.955 1.00 55.10 C ANISOU 2053 C SER A 208 4886 4955 11095 242 -89 103 C ATOM 2054 O SER A 208 101.503 -62.008 3.799 1.00 53.75 O ANISOU 2054 O SER A 208 4789 4841 10794 177 -139 69 O ATOM 2055 CB SER A 208 98.254 -62.363 3.609 1.00 53.64 C ANISOU 2055 CB SER A 208 4615 4971 10796 281 -152 277 C ATOM 2056 OG SER A 208 97.145 -62.995 4.232 1.00 59.70 O ANISOU 2056 OG SER A 208 5338 5830 11515 292 -150 266 O ATOM 2057 N ALA A 209 100.475 -59.997 3.590 1.00 53.62 N ANISOU 2057 N ALA A 209 4633 4606 11136 297 -21 167 N ATOM 2058 CA ALA A 209 101.599 -59.283 2.966 1.00 53.90 C ANISOU 2058 CA ALA A 209 4670 4511 11297 280 3 212 C ATOM 2059 C ALA A 209 102.710 -59.009 3.995 1.00 58.84 C ANISOU 2059 C ALA A 209 5335 5045 11977 229 29 -24 C ATOM 2060 O ALA A 209 103.884 -59.215 3.679 1.00 58.97 O ANISOU 2060 O ALA A 209 5390 5054 11962 170 1 -30 O ATOM 2061 CB ALA A 209 101.124 -57.981 2.341 1.00 56.15 C ANISOU 2061 CB ALA A 209 4857 4637 11841 361 82 368 C ATOM 2062 N GLY A 210 102.326 -58.588 5.211 1.00 55.16 N ANISOU 2062 N GLY A 210 4853 4528 11576 255 77 -220 N ATOM 2063 CA GLY A 210 103.237 -58.313 6.321 1.00 54.91 C ANISOU 2063 CA GLY A 210 4850 4440 11575 217 85 -480 C ATOM 2064 C GLY A 210 103.988 -59.537 6.808 1.00 57.59 C ANISOU 2064 C GLY A 210 5274 4957 11653 149 3 -574 C ATOM 2065 O GLY A 210 105.196 -59.463 7.055 1.00 56.50 O ANISOU 2065 O GLY A 210 5155 4784 11530 91 -25 -687 O ATOM 2066 N ILE A 211 103.280 -60.688 6.915 1.00 53.91 N ANISOU 2066 N ILE A 211 4845 4675 10964 157 -34 -513 N ATOM 2067 CA ILE A 211 103.837 -61.976 7.348 1.00 52.35 C ANISOU 2067 CA ILE A 211 4720 4648 10524 106 -99 -564 C ATOM 2068 C ILE A 211 104.712 -62.564 6.225 1.00 53.48 C ANISOU 2068 C ILE A 211 4900 4810 10609 45 -157 -427 C ATOM 2069 O ILE A 211 105.767 -63.116 6.539 1.00 52.50 O ANISOU 2069 O ILE A 211 4821 4740 10388 -4 -195 -503 O ATOM 2070 CB ILE A 211 102.720 -62.947 7.843 1.00 55.24 C ANISOU 2070 CB ILE A 211 5095 5170 10724 137 -99 -532 C ATOM 2071 CG1 ILE A 211 102.099 -62.491 9.197 1.00 57.16 C ANISOU 2071 CG1 ILE A 211 5314 5430 10973 206 -30 -699 C ATOM 2072 CG2 ILE A 211 103.132 -64.405 7.890 1.00 54.82 C ANISOU 2072 CG2 ILE A 211 5103 5271 10453 86 -160 -499 C ATOM 2073 CD1 ILE A 211 103.052 -62.270 10.435 1.00 68.27 C ANISOU 2073 CD1 ILE A 211 6756 6867 12317 203 -31 -945 C ATOM 2074 N ALA A 212 104.321 -62.406 4.934 1.00 48.48 N ANISOU 2074 N ALA A 212 4243 4143 10033 59 -159 -228 N ATOM 2075 CA ALA A 212 105.142 -62.880 3.805 1.00 47.13 C ANISOU 2075 CA ALA A 212 4109 4000 9798 20 -199 -99 C ATOM 2076 C ALA A 212 106.525 -62.180 3.793 1.00 53.21 C ANISOU 2076 C ALA A 212 4868 4649 10700 -13 -174 -154 C ATOM 2077 O ALA A 212 107.542 -62.835 3.555 1.00 51.72 O ANISOU 2077 O ALA A 212 4725 4513 10414 -59 -206 -149 O ATOM 2078 CB ALA A 212 104.423 -62.652 2.486 1.00 47.65 C ANISOU 2078 CB ALA A 212 4141 4067 9895 62 -203 115 C ATOM 2079 N LEU A 213 106.560 -60.873 4.112 1.00 52.13 N ANISOU 2079 N LEU A 213 4664 4341 10802 8 -113 -215 N ATOM 2080 CA LEU A 213 107.794 -60.094 4.180 1.00 54.00 C ANISOU 2080 CA LEU A 213 4864 4432 11221 -32 -87 -282 C ATOM 2081 C LEU A 213 108.703 -60.552 5.360 1.00 59.65 C ANISOU 2081 C LEU A 213 5610 5209 11843 -90 -139 -514 C ATOM 2082 O LEU A 213 109.924 -60.640 5.175 1.00 58.84 O ANISOU 2082 O LEU A 213 5502 5086 11768 -143 -158 -521 O ATOM 2083 CB LEU A 213 107.459 -58.604 4.293 1.00 56.28 C ANISOU 2083 CB LEU A 213 5063 4503 11817 5 -6 -308 C ATOM 2084 CG LEU A 213 107.548 -57.749 3.003 1.00 62.49 C ANISOU 2084 CG LEU A 213 5782 5145 12816 39 64 -64 C ATOM 2085 CD1 LEU A 213 106.462 -58.103 1.992 1.00 61.41 C ANISOU 2085 CD1 LEU A 213 5654 5120 12560 109 61 175 C ATOM 2086 CD2 LEU A 213 107.420 -56.278 3.338 1.00 68.75 C ANISOU 2086 CD2 LEU A 213 6479 5686 13959 64 152 -130 C ATOM 2087 N MET A 214 108.110 -60.880 6.542 1.00 57.66 N ANISOU 2087 N MET A 214 5384 5053 11470 -70 -159 -683 N ATOM 2088 CA MET A 214 108.819 -61.379 7.739 1.00 57.97 C ANISOU 2088 CA MET A 214 5451 5200 11374 -102 -213 -890 C ATOM 2089 C MET A 214 109.486 -62.725 7.436 1.00 61.34 C ANISOU 2089 C MET A 214 5938 5782 11585 -139 -269 -800 C ATOM 2090 O MET A 214 110.564 -63.022 7.961 1.00 62.36 O ANISOU 2090 O MET A 214 6069 5961 11662 -179 -315 -901 O ATOM 2091 CB MET A 214 107.847 -61.516 8.935 1.00 61.03 C ANISOU 2091 CB MET A 214 5856 5687 11645 -45 -201 -1035 C ATOM 2092 CG MET A 214 108.380 -62.369 10.100 1.00 64.80 C ANISOU 2092 CG MET A 214 6374 6352 11895 -53 -258 -1185 C ATOM 2093 SD MET A 214 107.177 -62.603 11.419 1.00 70.07 S ANISOU 2093 SD MET A 214 7059 7165 12398 36 -220 -1305 S ATOM 2094 CE MET A 214 107.963 -63.889 12.356 1.00 65.58 C ANISOU 2094 CE MET A 214 6538 6839 11540 28 -287 -1360 C ATOM 2095 N LYS A 215 108.837 -63.536 6.586 1.00 55.33 N ANISOU 2095 N LYS A 215 5219 5095 10709 -123 -268 -615 N ATOM 2096 CA LYS A 215 109.361 -64.832 6.169 1.00 52.70 C ANISOU 2096 CA LYS A 215 4945 4884 10193 -151 -308 -526 C ATOM 2097 C LYS A 215 110.688 -64.667 5.404 1.00 56.16 C ANISOU 2097 C LYS A 215 5372 5257 10710 -192 -310 -465 C ATOM 2098 O LYS A 215 111.587 -65.478 5.610 1.00 55.88 O ANISOU 2098 O LYS A 215 5364 5302 10565 -220 -342 -486 O ATOM 2099 CB LYS A 215 108.346 -65.580 5.293 1.00 52.60 C ANISOU 2099 CB LYS A 215 4968 4936 10081 -130 -311 -365 C ATOM 2100 CG LYS A 215 107.125 -66.073 6.018 1.00 58.29 C ANISOU 2100 CG LYS A 215 5693 5744 10709 -99 -310 -397 C ATOM 2101 CD LYS A 215 106.231 -66.812 5.046 1.00 61.51 C ANISOU 2101 CD LYS A 215 6118 6204 11047 -96 -332 -246 C ATOM 2102 CE LYS A 215 104.928 -67.182 5.677 1.00 59.55 C ANISOU 2102 CE LYS A 215 5847 6022 10759 -67 -322 -254 C ATOM 2103 NZ LYS A 215 104.295 -68.292 4.936 1.00 69.04 N ANISOU 2103 NZ LYS A 215 7067 7296 11868 -89 -365 -145 N ATOM 2104 N ASN A 216 110.800 -63.626 4.534 1.00 51.94 N ANISOU 2104 N ASN A 216 4788 4576 10372 -186 -264 -371 N ATOM 2105 CA ASN A 216 111.973 -63.339 3.706 1.00 51.98 C ANISOU 2105 CA ASN A 216 4764 4505 10483 -213 -239 -275 C ATOM 2106 C ASN A 216 113.134 -62.708 4.497 1.00 58.13 C ANISOU 2106 C ASN A 216 5474 5195 11416 -266 -251 -432 C ATOM 2107 O ASN A 216 114.283 -63.098 4.300 1.00 56.34 O ANISOU 2107 O ASN A 216 5239 4993 11176 -301 -264 -407 O ATOM 2108 CB ASN A 216 111.602 -62.410 2.540 1.00 52.02 C ANISOU 2108 CB ASN A 216 4725 4389 10653 -175 -172 -92 C ATOM 2109 CG ASN A 216 110.597 -62.943 1.541 1.00 69.93 C ANISOU 2109 CG ASN A 216 7042 6754 12774 -122 -174 79 C ATOM 2110 OD1 ASN A 216 109.725 -62.211 1.058 1.00 61.84 O ANISOU 2110 OD1 ASN A 216 5979 5670 11849 -73 -140 181 O ATOM 2111 ND2 ASN A 216 110.723 -64.206 1.161 1.00 63.62 N ANISOU 2111 ND2 ASN A 216 6321 6103 11749 -129 -216 117 N ATOM 2112 N ILE A 217 112.841 -61.714 5.351 1.00 57.67 N ANISOU 2112 N ILE A 217 5360 5033 11518 -269 -248 -598 N ATOM 2113 CA ILE A 217 113.849 -61.001 6.137 1.00 59.25 C ANISOU 2113 CA ILE A 217 5483 5140 11889 -325 -275 -787 C ATOM 2114 C ILE A 217 114.517 -61.953 7.156 1.00 64.31 C ANISOU 2114 C ILE A 217 6154 5962 12319 -351 -364 -936 C ATOM 2115 O ILE A 217 115.737 -62.103 7.131 1.00 64.29 O ANISOU 2115 O ILE A 217 6108 5963 12357 -401 -396 -946 O ATOM 2116 CB ILE A 217 113.227 -59.743 6.821 1.00 64.16 C ANISOU 2116 CB ILE A 217 6047 5608 12722 -312 -249 -959 C ATOM 2117 CG1 ILE A 217 112.567 -58.761 5.808 1.00 65.82 C ANISOU 2117 CG1 ILE A 217 6213 5628 13169 -274 -149 -781 C ATOM 2118 CG2 ILE A 217 114.223 -59.015 7.725 1.00 66.72 C ANISOU 2118 CG2 ILE A 217 6288 5841 13223 -377 -297 -1207 C ATOM 2119 CD1 ILE A 217 113.431 -58.297 4.536 1.00 77.87 C ANISOU 2119 CD1 ILE A 217 7673 7015 14901 -296 -85 -556 C ATOM 2120 N LEU A 218 113.720 -62.593 8.026 1.00 61.67 N ANISOU 2120 N LEU A 218 5882 5782 11768 -311 -396 -1028 N ATOM 2121 CA LEU A 218 114.203 -63.480 9.086 1.00 61.88 C ANISOU 2121 CA LEU A 218 5933 6000 11580 -313 -470 -1150 C ATOM 2122 C LEU A 218 114.713 -64.828 8.593 1.00 63.98 C ANISOU 2122 C LEU A 218 6251 6394 11665 -316 -484 -988 C ATOM 2123 O LEU A 218 115.587 -65.418 9.232 1.00 63.78 O ANISOU 2123 O LEU A 218 6213 6485 11536 -330 -541 -1051 O ATOM 2124 CB LEU A 218 113.085 -63.733 10.115 1.00 62.51 C ANISOU 2124 CB LEU A 218 6058 6204 11489 -251 -472 -1259 C ATOM 2125 CG LEU A 218 113.002 -62.766 11.288 1.00 69.74 C ANISOU 2125 CG LEU A 218 6928 7097 12472 -239 -496 -1527 C ATOM 2126 CD1 LEU A 218 111.670 -62.900 11.993 1.00 69.61 C ANISOU 2126 CD1 LEU A 218 6958 7175 12317 -158 -456 -1576 C ATOM 2127 CD2 LEU A 218 114.159 -62.988 12.278 1.00 74.47 C ANISOU 2127 CD2 LEU A 218 7492 7827 12976 -266 -595 -1704 C ATOM 2128 N GLY A 219 114.128 -65.333 7.513 1.00 58.45 N ANISOU 2128 N GLY A 219 5606 5681 10920 -296 -434 -793 N ATOM 2129 CA GLY A 219 114.463 -66.647 6.977 1.00 55.38 C ANISOU 2129 CA GLY A 219 5277 5398 10368 -292 -436 -654 C ATOM 2130 C GLY A 219 115.407 -66.691 5.796 1.00 54.57 C ANISOU 2130 C GLY A 219 5163 5228 10345 -314 -405 -513 C ATOM 2131 O GLY A 219 115.871 -67.783 5.458 1.00 54.60 O ANISOU 2131 O GLY A 219 5211 5315 10219 -308 -405 -429 O ATOM 2132 N PHE A 220 115.692 -65.543 5.142 1.00 47.59 N ANISOU 2132 N PHE A 220 4216 4187 9678 -332 -365 -472 N ATOM 2133 CA PHE A 220 116.584 -65.560 3.986 1.00 46.54 C ANISOU 2133 CA PHE A 220 4065 4001 9616 -339 -315 -312 C ATOM 2134 C PHE A 220 117.554 -64.367 3.932 1.00 54.07 C ANISOU 2134 C PHE A 220 4900 4798 10845 -383 -291 -334 C ATOM 2135 O PHE A 220 118.756 -64.602 3.815 1.00 54.86 O ANISOU 2135 O PHE A 220 4953 4904 10985 -411 -291 -305 O ATOM 2136 CB PHE A 220 115.792 -65.648 2.669 1.00 46.93 C ANISOU 2136 CB PHE A 220 4172 4039 9621 -291 -257 -126 C ATOM 2137 CG PHE A 220 116.622 -66.001 1.451 1.00 48.05 C ANISOU 2137 CG PHE A 220 4325 4188 9743 -274 -200 47 C ATOM 2138 CD1 PHE A 220 117.006 -67.317 1.206 1.00 50.55 C ANISOU 2138 CD1 PHE A 220 4715 4626 9865 -260 -209 79 C ATOM 2139 CD2 PHE A 220 116.990 -65.026 0.533 1.00 50.70 C ANISOU 2139 CD2 PHE A 220 4598 4407 10260 -260 -123 187 C ATOM 2140 CE1 PHE A 220 117.761 -67.645 0.076 1.00 51.45 C ANISOU 2140 CE1 PHE A 220 4845 4753 9949 -229 -144 227 C ATOM 2141 CE2 PHE A 220 117.742 -65.356 -0.598 1.00 53.96 C ANISOU 2141 CE2 PHE A 220 5022 4847 10635 -226 -55 358 C ATOM 2142 CZ PHE A 220 118.124 -66.664 -0.817 1.00 51.49 C ANISOU 2142 CZ PHE A 220 4790 4665 10110 -209 -66 366 C ATOM 2143 N ILE A 221 117.054 -63.115 3.997 1.00 51.07 N ANISOU 2143 N ILE A 221 4462 4266 10676 -389 -265 -377 N ATOM 2144 CA ILE A 221 117.865 -61.904 3.878 1.00 52.19 C ANISOU 2144 CA ILE A 221 4478 4218 11134 -436 -229 -389 C ATOM 2145 C ILE A 221 118.950 -61.874 4.960 1.00 57.77 C ANISOU 2145 C ILE A 221 5106 4941 11902 -505 -313 -592 C ATOM 2146 O ILE A 221 120.131 -61.953 4.610 1.00 58.17 O ANISOU 2146 O ILE A 221 5087 4968 12046 -540 -301 -522 O ATOM 2147 CB ILE A 221 116.988 -60.603 3.877 1.00 56.89 C ANISOU 2147 CB ILE A 221 5026 4634 11957 -422 -182 -419 C ATOM 2148 CG1 ILE A 221 115.928 -60.591 2.732 1.00 57.67 C ANISOU 2148 CG1 ILE A 221 5182 4733 11998 -345 -106 -190 C ATOM 2149 CG2 ILE A 221 117.828 -59.311 3.879 1.00 58.61 C ANISOU 2149 CG2 ILE A 221 5097 4618 12553 -481 -143 -458 C ATOM 2150 CD1 ILE A 221 116.445 -60.924 1.272 1.00 71.89 C ANISOU 2150 CD1 ILE A 221 6994 6560 13760 -309 -31 88 C ATOM 2151 N ILE A 222 118.562 -61.760 6.252 1.00 55.29 N ANISOU 2151 N ILE A 222 4797 4682 11529 -517 -396 -838 N ATOM 2152 CA ILE A 222 119.505 -61.676 7.376 1.00 56.37 C ANISOU 2152 CA ILE A 222 4855 4866 11698 -575 -498 -1060 C ATOM 2153 C ILE A 222 120.418 -62.912 7.383 1.00 60.56 C ANISOU 2153 C ILE A 222 5403 5574 12033 -575 -540 -982 C ATOM 2154 O ILE A 222 121.637 -62.719 7.382 1.00 62.41 O ANISOU 2154 O ILE A 222 5530 5769 12413 -630 -568 -995 O ATOM 2155 CB ILE A 222 118.815 -61.424 8.748 1.00 59.78 C ANISOU 2155 CB ILE A 222 5307 5369 12037 -561 -575 -1334 C ATOM 2156 CG1 ILE A 222 118.258 -59.982 8.817 1.00 60.88 C ANISOU 2156 CG1 ILE A 222 5388 5283 12461 -576 -533 -1454 C ATOM 2157 CG2 ILE A 222 119.789 -61.695 9.911 1.00 61.50 C ANISOU 2157 CG2 ILE A 222 5464 5729 12175 -600 -703 -1544 C ATOM 2158 CD1 ILE A 222 117.230 -59.747 9.900 1.00 62.81 C ANISOU 2158 CD1 ILE A 222 5682 5590 12593 -529 -563 -1675 C ATOM 2159 N PRO A 223 119.907 -64.164 7.306 1.00 54.96 N ANISOU 2159 N PRO A 223 4813 5039 11032 -515 -535 -885 N ATOM 2160 CA PRO A 223 120.828 -65.307 7.272 1.00 54.05 C ANISOU 2160 CA PRO A 223 4703 5063 10769 -509 -559 -801 C ATOM 2161 C PRO A 223 121.832 -65.224 6.107 1.00 57.67 C ANISOU 2161 C PRO A 223 5105 5423 11386 -529 -486 -616 C ATOM 2162 O PRO A 223 123.033 -65.301 6.368 1.00 58.05 O ANISOU 2162 O PRO A 223 5055 5491 11509 -566 -525 -638 O ATOM 2163 CB PRO A 223 119.887 -66.509 7.138 1.00 54.25 C ANISOU 2163 CB PRO A 223 4866 5223 10522 -441 -535 -706 C ATOM 2164 CG PRO A 223 118.601 -66.043 7.715 1.00 58.60 C ANISOU 2164 CG PRO A 223 5459 5769 11036 -420 -545 -820 C ATOM 2165 CD PRO A 223 118.500 -64.623 7.295 1.00 55.51 C ANISOU 2165 CD PRO A 223 4999 5176 10915 -453 -508 -850 C ATOM 2166 N LEU A 224 121.363 -64.961 4.858 1.00 52.96 N ANISOU 2166 N LEU A 224 4550 4722 10850 -500 -381 -435 N ATOM 2167 CA LEU A 224 122.215 -64.857 3.661 1.00 52.06 C ANISOU 2167 CA LEU A 224 4389 4529 10863 -497 -286 -232 C ATOM 2168 C LEU A 224 123.286 -63.787 3.787 1.00 57.55 C ANISOU 2168 C LEU A 224 4916 5073 11879 -569 -284 -270 C ATOM 2169 O LEU A 224 124.362 -63.982 3.230 1.00 57.76 O ANISOU 2169 O LEU A 224 4874 5088 11985 -575 -235 -142 O ATOM 2170 CB LEU A 224 121.404 -64.615 2.374 1.00 51.10 C ANISOU 2170 CB LEU A 224 4336 4343 10735 -441 -181 -42 C ATOM 2171 CG LEU A 224 121.983 -65.176 1.062 1.00 54.99 C ANISOU 2171 CG LEU A 224 4858 4869 11168 -389 -79 189 C ATOM 2172 CD1 LEU A 224 122.659 -64.090 0.245 1.00 56.22 C ANISOU 2172 CD1 LEU A 224 4895 4864 11601 -397 23 341 C ATOM 2173 CD2 LEU A 224 122.892 -66.420 1.280 1.00 55.66 C ANISOU 2173 CD2 LEU A 224 4964 5087 11096 -381 -101 186 C ATOM 2174 N ILE A 225 123.006 -62.671 4.495 1.00 55.78 N ANISOU 2174 N ILE A 225 4616 4725 11853 -622 -332 -447 N ATOM 2175 CA ILE A 225 123.983 -61.598 4.726 1.00 57.91 C ANISOU 2175 CA ILE A 225 4707 4825 12469 -707 -346 -525 C ATOM 2176 C ILE A 225 125.206 -62.219 5.417 1.00 62.75 C ANISOU 2176 C ILE A 225 5240 5563 13039 -751 -443 -613 C ATOM 2177 O ILE A 225 126.322 -62.095 4.903 1.00 63.33 O ANISOU 2177 O ILE A 225 5196 5572 13296 -783 -399 -494 O ATOM 2178 CB ILE A 225 123.358 -60.415 5.539 1.00 62.59 C ANISOU 2178 CB ILE A 225 5252 5276 13255 -752 -396 -761 C ATOM 2179 CG1 ILE A 225 122.487 -59.519 4.628 1.00 63.75 C ANISOU 2179 CG1 ILE A 225 5413 5232 13578 -716 -270 -612 C ATOM 2180 CG2 ILE A 225 124.421 -59.581 6.278 1.00 65.04 C ANISOU 2180 CG2 ILE A 225 5380 5470 13864 -859 -479 -962 C ATOM 2181 CD1 ILE A 225 121.499 -58.552 5.360 1.00 67.89 C ANISOU 2181 CD1 ILE A 225 5936 5635 14224 -724 -296 -823 C ATOM 2182 N PHE A 226 124.963 -62.961 6.529 1.00 58.63 N ANISOU 2182 N PHE A 226 4781 5237 12260 -736 -563 -789 N ATOM 2183 CA PHE A 226 125.975 -63.648 7.333 1.00 58.84 C ANISOU 2183 CA PHE A 226 4739 5426 12190 -757 -672 -875 C ATOM 2184 C PHE A 226 126.734 -64.708 6.551 1.00 60.81 C ANISOU 2184 C PHE A 226 5005 5761 12341 -713 -602 -639 C ATOM 2185 O PHE A 226 127.959 -64.698 6.591 1.00 61.99 O ANISOU 2185 O PHE A 226 5015 5908 12630 -754 -627 -616 O ATOM 2186 CB PHE A 226 125.334 -64.312 8.551 1.00 60.45 C ANISOU 2186 CB PHE A 226 5032 5842 12094 -717 -782 -1051 C ATOM 2187 CG PHE A 226 124.954 -63.378 9.664 1.00 63.80 C ANISOU 2187 CG PHE A 226 5411 6245 12587 -758 -887 -1346 C ATOM 2188 CD1 PHE A 226 125.866 -63.047 10.655 1.00 69.33 C ANISOU 2188 CD1 PHE A 226 5974 7009 13361 -819 -1029 -1561 C ATOM 2189 CD2 PHE A 226 123.670 -62.865 9.751 1.00 65.56 C ANISOU 2189 CD2 PHE A 226 5724 6398 12787 -729 -848 -1419 C ATOM 2190 CE1 PHE A 226 125.514 -62.174 11.687 1.00 72.17 C ANISOU 2190 CE1 PHE A 226 6295 7354 13771 -852 -1130 -1868 C ATOM 2191 CE2 PHE A 226 123.311 -62.014 10.795 1.00 70.25 C ANISOU 2191 CE2 PHE A 226 6282 6972 13438 -755 -933 -1709 C ATOM 2192 CZ PHE A 226 124.237 -61.670 11.754 1.00 70.54 C ANISOU 2192 CZ PHE A 226 6191 7068 13542 -815 -1073 -1942 C ATOM 2193 N ILE A 227 126.024 -65.629 5.860 1.00 54.20 N ANISOU 2193 N ILE A 227 4327 4996 11272 -630 -516 -478 N ATOM 2194 CA ILE A 227 126.641 -66.706 5.069 1.00 52.85 C ANISOU 2194 CA ILE A 227 4192 4899 10988 -574 -436 -271 C ATOM 2195 C ILE A 227 127.590 -66.109 4.012 1.00 55.69 C ANISOU 2195 C ILE A 227 4438 5114 11606 -594 -327 -100 C ATOM 2196 O ILE A 227 128.705 -66.596 3.861 1.00 56.48 O ANISOU 2196 O ILE A 227 4459 5260 11742 -589 -308 -11 O ATOM 2197 CB ILE A 227 125.615 -67.685 4.393 1.00 54.76 C ANISOU 2197 CB ILE A 227 4624 5213 10970 -488 -361 -153 C ATOM 2198 CG1 ILE A 227 124.302 -67.918 5.213 1.00 55.16 C ANISOU 2198 CG1 ILE A 227 4783 5344 10831 -471 -432 -294 C ATOM 2199 CG2 ILE A 227 126.271 -69.010 4.033 1.00 54.84 C ANISOU 2199 CG2 ILE A 227 4675 5335 10827 -429 -316 -24 C ATOM 2200 CD1 ILE A 227 124.396 -68.590 6.634 1.00 66.84 C ANISOU 2200 CD1 ILE A 227 6256 6997 12145 -466 -550 -441 C ATOM 2201 N ALA A 228 127.153 -65.047 3.310 1.00 50.76 N ANISOU 2201 N ALA A 228 3796 4317 11173 -610 -248 -39 N ATOM 2202 CA ALA A 228 127.926 -64.387 2.269 1.00 51.25 C ANISOU 2202 CA ALA A 228 3748 4233 11492 -619 -122 154 C ATOM 2203 C ALA A 228 129.105 -63.583 2.838 1.00 57.60 C ANISOU 2203 C ALA A 228 4330 4930 12624 -720 -179 67 C ATOM 2204 O ALA A 228 130.188 -63.638 2.247 1.00 58.64 O ANISOU 2204 O ALA A 228 4350 5029 12900 -720 -98 229 O ATOM 2205 CB ALA A 228 127.025 -63.494 1.441 1.00 52.17 C ANISOU 2205 CB ALA A 228 3904 4206 11710 -595 -24 256 C ATOM 2206 N THR A 229 128.916 -62.851 3.973 1.00 55.07 N ANISOU 2206 N THR A 229 3938 4560 12425 -804 -316 -195 N ATOM 2207 CA THR A 229 129.999 -62.070 4.601 1.00 57.55 C ANISOU 2207 CA THR A 229 4031 4774 13059 -914 -400 -328 C ATOM 2208 C THR A 229 131.122 -62.995 5.077 1.00 62.78 C ANISOU 2208 C THR A 229 4617 5614 13623 -918 -481 -333 C ATOM 2209 O THR A 229 132.293 -62.675 4.880 1.00 63.02 O ANISOU 2209 O THR A 229 4460 5569 13916 -974 -465 -265 O ATOM 2210 CB THR A 229 129.466 -61.205 5.748 1.00 67.68 C ANISOU 2210 CB THR A 229 5280 5997 14439 -989 -540 -647 C ATOM 2211 OG1 THR A 229 128.458 -60.356 5.224 1.00 64.95 O ANISOU 2211 OG1 THR A 229 4994 5472 14211 -974 -445 -609 O ATOM 2212 CG2 THR A 229 130.536 -60.378 6.416 1.00 70.00 C ANISOU 2212 CG2 THR A 229 5342 6185 15071 -1113 -648 -826 C ATOM 2213 N CYS A 230 130.756 -64.158 5.659 1.00 60.22 N ANISOU 2213 N CYS A 230 4428 5519 12935 -852 -554 -388 N ATOM 2214 CA CYS A 230 131.694 -65.174 6.147 1.00 60.54 C ANISOU 2214 CA CYS A 230 4412 5748 12840 -830 -625 -372 C ATOM 2215 C CYS A 230 132.449 -65.833 5.004 1.00 63.40 C ANISOU 2215 C CYS A 230 4763 6106 13219 -768 -468 -84 C ATOM 2216 O CYS A 230 133.649 -66.029 5.151 1.00 65.55 O ANISOU 2216 O CYS A 230 4877 6417 13612 -791 -495 -39 O ATOM 2217 CB CYS A 230 130.984 -66.211 7.004 1.00 59.79 C ANISOU 2217 CB CYS A 230 4469 5877 12372 -763 -715 -472 C ATOM 2218 SG CYS A 230 130.424 -65.576 8.602 1.00 65.15 S ANISOU 2218 SG CYS A 230 5124 6635 12996 -820 -918 -828 S ATOM 2219 N TYR A 231 131.782 -66.158 3.871 1.00 56.85 N ANISOU 2219 N TYR A 231 4091 5238 12272 -686 -309 103 N ATOM 2220 CA TYR A 231 132.462 -66.767 2.729 1.00 56.59 C ANISOU 2220 CA TYR A 231 4061 5209 12232 -611 -146 363 C ATOM 2221 C TYR A 231 133.542 -65.832 2.163 1.00 63.37 C ANISOU 2221 C TYR A 231 4708 5907 13464 -666 -62 489 C ATOM 2222 O TYR A 231 134.674 -66.272 1.945 1.00 63.65 O ANISOU 2222 O TYR A 231 4629 5982 13574 -648 -15 613 O ATOM 2223 CB TYR A 231 131.490 -67.185 1.607 1.00 56.69 C ANISOU 2223 CB TYR A 231 4278 5221 12040 -512 -5 510 C ATOM 2224 CG TYR A 231 132.223 -67.514 0.317 1.00 60.48 C ANISOU 2224 CG TYR A 231 4745 5684 12553 -434 181 769 C ATOM 2225 CD1 TYR A 231 133.075 -68.618 0.236 1.00 61.78 C ANISOU 2225 CD1 TYR A 231 4900 5962 12612 -372 219 852 C ATOM 2226 CD2 TYR A 231 132.148 -66.670 -0.787 1.00 62.90 C ANISOU 2226 CD2 TYR A 231 5026 5859 13014 -414 326 941 C ATOM 2227 CE1 TYR A 231 133.816 -68.881 -0.914 1.00 61.81 C ANISOU 2227 CE1 TYR A 231 4879 5952 12653 -291 401 1080 C ATOM 2228 CE2 TYR A 231 132.884 -66.927 -1.946 1.00 64.95 C ANISOU 2228 CE2 TYR A 231 5260 6121 13296 -330 507 1185 C ATOM 2229 CZ TYR A 231 133.708 -68.041 -2.007 1.00 70.51 C ANISOU 2229 CZ TYR A 231 5965 6942 13882 -268 545 1244 C ATOM 2230 OH TYR A 231 134.422 -68.319 -3.147 1.00 71.65 O ANISOU 2230 OH TYR A 231 6093 7098 14034 -171 737 1477 O ATOM 2231 N PHE A 232 133.181 -64.558 1.907 1.00 61.16 N ANISOU 2231 N PHE A 232 4367 5435 13435 -729 -31 474 N ATOM 2232 CA PHE A 232 134.092 -63.560 1.356 1.00 62.80 C ANISOU 2232 CA PHE A 232 4363 5454 14042 -787 63 607 C ATOM 2233 C PHE A 232 135.108 -63.093 2.409 1.00 71.07 C ANISOU 2233 C PHE A 232 5174 6469 15360 -914 -94 427 C ATOM 2234 O PHE A 232 136.152 -62.552 2.041 1.00 72.76 O ANISOU 2234 O PHE A 232 5178 6560 15908 -965 -27 548 O ATOM 2235 CB PHE A 232 133.315 -62.383 0.752 1.00 64.27 C ANISOU 2235 CB PHE A 232 4562 5438 14420 -803 156 664 C ATOM 2236 CG PHE A 232 132.639 -62.736 -0.553 1.00 63.72 C ANISOU 2236 CG PHE A 232 4664 5401 14144 -671 336 912 C ATOM 2237 CD1 PHE A 232 133.376 -62.831 -1.736 1.00 66.15 C ANISOU 2237 CD1 PHE A 232 4917 5690 14525 -597 530 1209 C ATOM 2238 CD2 PHE A 232 131.267 -62.978 -0.602 1.00 63.57 C ANISOU 2238 CD2 PHE A 232 4856 5447 13851 -616 311 847 C ATOM 2239 CE1 PHE A 232 132.754 -63.169 -2.943 1.00 65.75 C ANISOU 2239 CE1 PHE A 232 5029 5703 14249 -464 686 1420 C ATOM 2240 CE2 PHE A 232 130.642 -63.313 -1.808 1.00 65.04 C ANISOU 2240 CE2 PHE A 232 5193 5685 13835 -496 455 1058 C ATOM 2241 CZ PHE A 232 131.392 -63.406 -2.971 1.00 63.91 C ANISOU 2241 CZ PHE A 232 5001 5540 13742 -419 637 1335 C ATOM 2242 N GLY A 233 134.813 -63.351 3.688 1.00 68.69 N ANISOU 2242 N GLY A 233 4902 6293 14902 -957 -299 149 N ATOM 2243 CA GLY A 233 135.709 -63.066 4.806 1.00 71.16 C ANISOU 2243 CA GLY A 233 5009 6639 15388 -1064 -487 -61 C ATOM 2244 C GLY A 233 136.818 -64.107 4.874 1.00 76.50 C ANISOU 2244 C GLY A 233 5601 7489 15974 -1020 -499 58 C ATOM 2245 O GLY A 233 137.982 -63.783 5.158 1.00 77.42 O ANISOU 2245 O GLY A 233 5476 7577 16362 -1100 -562 44 O ATOM 2246 N ILE A 234 136.446 -65.376 4.584 1.00 71.98 N ANISOU 2246 N ILE A 234 5222 7089 15037 -892 -432 181 N ATOM 2247 CA ILE A 234 137.335 -66.530 4.492 1.00 71.79 C ANISOU 2247 CA ILE A 234 5163 7223 14889 -815 -401 331 C ATOM 2248 C ILE A 234 138.149 -66.383 3.186 1.00 76.40 C ANISOU 2248 C ILE A 234 5652 7681 15696 -780 -183 622 C ATOM 2249 O ILE A 234 139.375 -66.470 3.236 1.00 78.08 O ANISOU 2249 O ILE A 234 5659 7910 16100 -802 -184 706 O ATOM 2250 CB ILE A 234 136.521 -67.864 4.582 1.00 72.73 C ANISOU 2250 CB ILE A 234 5531 7524 14578 -691 -386 350 C ATOM 2251 CG1 ILE A 234 136.064 -68.130 6.038 1.00 72.70 C ANISOU 2251 CG1 ILE A 234 5560 7689 14373 -715 -603 98 C ATOM 2252 CG2 ILE A 234 137.309 -69.071 4.025 1.00 73.90 C ANISOU 2252 CG2 ILE A 234 5684 7773 14622 -581 -266 572 C ATOM 2253 CD1 ILE A 234 134.964 -69.191 6.205 1.00 76.58 C ANISOU 2253 CD1 ILE A 234 6299 8314 14486 -614 -589 92 C ATOM 2254 N ARG A 235 137.474 -66.085 2.045 1.00 71.97 N ANISOU 2254 N ARG A 235 5223 7001 15121 -725 -1 776 N ATOM 2255 CA ARG A 235 138.103 -65.907 0.733 1.00 72.79 C ANISOU 2255 CA ARG A 235 5260 7002 15394 -669 229 1068 C ATOM 2256 C ARG A 235 139.167 -64.802 0.763 1.00 79.61 C ANISOU 2256 C ARG A 235 5823 7695 16729 -784 233 1112 C ATOM 2257 O ARG A 235 140.218 -64.984 0.162 1.00 80.50 O ANISOU 2257 O ARG A 235 5794 7797 16995 -748 364 1327 O ATOM 2258 CB ARG A 235 137.053 -65.619 -0.354 1.00 72.77 C ANISOU 2258 CB ARG A 235 5446 6922 15281 -595 388 1193 C ATOM 2259 CG ARG A 235 137.570 -65.811 -1.776 1.00 85.12 C ANISOU 2259 CG ARG A 235 7008 8465 16868 -481 641 1511 C ATOM 2260 CD ARG A 235 136.509 -65.504 -2.810 1.00 98.80 C ANISOU 2260 CD ARG A 235 8920 10155 18465 -402 775 1627 C ATOM 2261 NE ARG A 235 136.973 -64.503 -3.771 1.00116.93 N ANISOU 2261 NE ARG A 235 11072 12293 21062 -393 960 1874 N ATOM 2262 CZ ARG A 235 136.267 -64.072 -4.812 1.00141.44 C ANISOU 2262 CZ ARG A 235 14280 15358 24105 -311 1107 2043 C ATOM 2263 NH1 ARG A 235 135.054 -64.557 -5.049 1.00132.98 N ANISOU 2263 NH1 ARG A 235 13453 14391 22682 -239 1080 1976 N ATOM 2264 NH2 ARG A 235 136.773 -63.159 -5.629 1.00134.06 N ANISOU 2264 NH2 ARG A 235 13190 14282 23465 -297 1285 2294 N ATOM 2265 N LYS A 236 138.918 -63.697 1.502 1.00 77.88 N ANISOU 2265 N LYS A 236 5499 7343 16751 -922 90 897 N ATOM 2266 CA LYS A 236 139.860 -62.577 1.638 1.00 81.37 C ANISOU 2266 CA LYS A 236 5641 7592 17685 -1056 70 892 C ATOM 2267 C LYS A 236 141.105 -62.947 2.462 1.00 88.47 C ANISOU 2267 C LYS A 236 6315 8600 18700 -1120 -80 810 C ATOM 2268 O LYS A 236 142.160 -62.341 2.253 1.00 90.59 O ANISOU 2268 O LYS A 236 6314 8737 19368 -1197 -38 910 O ATOM 2269 CB LYS A 236 139.185 -61.348 2.276 1.00 84.58 C ANISOU 2269 CB LYS A 236 6009 7820 18307 -1184 -55 637 C ATOM 2270 CG LYS A 236 139.445 -60.062 1.509 1.00 95.83 C ANISOU 2270 CG LYS A 236 7261 8947 20202 -1249 99 794 C ATOM 2271 CD LYS A 236 139.692 -58.861 2.418 1.00107.88 C ANISOU 2271 CD LYS A 236 8569 10277 22145 -1432 -70 516 C ATOM 2272 CE LYS A 236 140.118 -57.645 1.612 1.00118.09 C ANISOU 2272 CE LYS A 236 9652 11250 23966 -1497 106 714 C ATOM 2273 NZ LYS A 236 140.799 -56.611 2.441 1.00121.93 N ANISOU 2273 NZ LYS A 236 9850 11538 24942 -1691 -52 469 N ATOM 2274 N HIS A 237 140.977 -63.915 3.403 1.00 84.29 N ANISOU 2274 N HIS A 237 5878 8310 17837 -1086 -253 641 N ATOM 2275 CA HIS A 237 142.061 -64.361 4.290 1.00 85.37 C ANISOU 2275 CA HIS A 237 5815 8598 18022 -1129 -421 556 C ATOM 2276 C HIS A 237 142.993 -65.362 3.626 1.00 88.92 C ANISOU 2276 C HIS A 237 6216 9152 18419 -1015 -270 845 C ATOM 2277 O HIS A 237 144.180 -65.385 3.951 1.00 90.11 O ANISOU 2277 O HIS A 237 6110 9338 18788 -1064 -336 877 O ATOM 2278 CB HIS A 237 141.495 -64.989 5.570 1.00 84.93 C ANISOU 2278 CB HIS A 237 5882 8773 17614 -1118 -654 287 C ATOM 2279 N LEU A 238 142.454 -66.222 2.747 1.00 83.50 N ANISOU 2279 N LEU A 238 5768 8521 17436 -862 -80 1035 N ATOM 2280 CA LEU A 238 143.227 -67.253 2.064 1.00 83.24 C ANISOU 2280 CA LEU A 238 5726 8584 17316 -731 86 1294 C ATOM 2281 C LEU A 238 143.967 -66.703 0.840 1.00 89.05 C ANISOU 2281 C LEU A 238 6318 9154 18362 -712 329 1579 C ATOM 2282 O LEU A 238 145.054 -67.198 0.521 1.00 90.34 O ANISOU 2282 O LEU A 238 6332 9367 18627 -654 428 1769 O ATOM 2283 CB LEU A 238 142.322 -68.418 1.666 1.00 80.71 C ANISOU 2283 CB LEU A 238 5724 8389 16554 -578 179 1341 C ATOM 2284 CG LEU A 238 142.215 -69.539 2.701 1.00 85.10 C ANISOU 2284 CG LEU A 238 6356 9162 16817 -532 17 1210 C ATOM 2285 CD1 LEU A 238 141.107 -69.272 3.717 1.00 84.43 C ANISOU 2285 CD1 LEU A 238 6398 9127 16556 -600 -187 929 C ATOM 2286 CD2 LEU A 238 141.979 -70.881 2.028 1.00 86.67 C ANISOU 2286 CD2 LEU A 238 6765 9455 16713 -362 182 1366 C ATOM 2287 N LEU A 239 143.403 -65.665 0.185 1.00 85.11 N ANISOU 2287 N LEU A 239 5848 8463 18026 -753 432 1623 N ATOM 2288 CA LEU A 239 143.969 -65.002 -0.999 1.00 86.56 C ANISOU 2288 CA LEU A 239 5898 8479 18510 -729 679 1914 C ATOM 2289 C LEU A 239 145.158 -64.093 -0.612 1.00 94.11 C ANISOU 2289 C LEU A 239 6480 9294 19984 -879 618 1923 C ATOM 2290 O LEU A 239 145.909 -63.638 -1.482 1.00 95.88 O ANISOU 2290 O LEU A 239 6528 9391 20509 -863 823 2192 O ATOM 2291 CB LEU A 239 142.873 -64.199 -1.724 1.00 86.03 C ANISOU 2291 CB LEU A 239 5988 8267 18433 -718 791 1957 C ATOM 2292 CG LEU A 239 142.140 -64.848 -2.928 1.00 89.04 C ANISOU 2292 CG LEU A 239 6646 8729 18456 -534 1009 2154 C ATOM 2293 CD1 LEU A 239 141.718 -66.310 -2.664 1.00 86.61 C ANISOU 2293 CD1 LEU A 239 6577 8650 17682 -425 949 2055 C ATOM 2294 CD2 LEU A 239 140.913 -64.025 -3.322 1.00 90.49 C ANISOU 2294 CD2 LEU A 239 6977 8797 18609 -543 1040 2129 C ATOM 2295 N LYS A 240 145.313 -63.837 0.700 1.00 91.13 N ANISOU 2295 N LYS A 240 5976 8947 19704 -1021 333 1624 N ATOM 2296 CA LYS A 240 146.405 -63.091 1.330 1.00 93.64 C ANISOU 2296 CA LYS A 240 5933 9167 20478 -1183 198 1544 C ATOM 2297 C LYS A 240 147.114 -64.060 2.294 1.00 97.52 C ANISOU 2297 C LYS A 240 6338 9906 20809 -1173 2 1433 C ATOM 2298 O LYS A 240 146.748 -65.240 2.318 1.00 95.53 O ANISOU 2298 O LYS A 240 6307 9858 20132 -1033 20 1462 O ATOM 2299 CB LYS A 240 145.866 -61.835 2.047 1.00 96.91 C ANISOU 2299 CB LYS A 240 6280 9401 21141 -1360 17 1248 C ATOM 2300 N THR A 241 148.107 -63.579 3.078 1.00 96.39 N ANISOU 2300 N THR A 241 5869 9746 21008 -1318 -185 1309 N ATOM 2301 CA THR A 241 148.908 -64.342 4.057 1.00128.80 C ANISOU 2301 CA THR A 241 9828 14091 25020 -1322 -397 1210 C ATOM 2302 C THR A 241 149.734 -65.453 3.364 1.00160.01 C ANISOU 2302 C THR A 241 13751 18167 28878 -1159 -199 1544 C ATOM 2303 O THR A 241 149.221 -66.505 2.976 1.00116.91 O ANISOU 2303 O THR A 241 8561 12839 23022 -990 -75 1653 O ATOM 2304 CB THR A 241 148.049 -64.888 5.213 1.00134.04 C ANISOU 2304 CB THR A 241 10701 14975 25254 -1306 -646 903 C ATOM 2305 N TYR A 244 150.916 -69.613 -4.625 1.00148.67 N ANISOU 2305 N TYR A 244 13038 16816 26632 47 1850 3498 N ATOM 2306 CA TYR A 244 151.937 -70.651 -4.466 1.00149.23 C ANISOU 2306 CA TYR A 244 12990 17014 26697 152 1900 3606 C ATOM 2307 C TYR A 244 151.778 -71.756 -5.532 1.00150.83 C ANISOU 2307 C TYR A 244 13447 17310 26552 396 2179 3759 C ATOM 2308 O TYR A 244 150.885 -71.675 -6.377 1.00149.43 O ANISOU 2308 O TYR A 244 13527 17113 26137 473 2314 3772 O ATOM 2309 CB TYR A 244 151.881 -71.246 -3.040 1.00149.67 C ANISOU 2309 CB TYR A 244 13030 17197 26642 74 1581 3350 C ATOM 2310 CG TYR A 244 153.233 -71.643 -2.483 1.00153.89 C ANISOU 2310 CG TYR A 244 13246 17810 27416 74 1527 3449 C ATOM 2311 CD1 TYR A 244 154.124 -70.683 -2.010 1.00158.73 C ANISOU 2311 CD1 TYR A 244 13484 18342 28483 -92 1408 3468 C ATOM 2312 CD2 TYR A 244 153.617 -72.979 -2.414 1.00154.22 C ANISOU 2312 CD2 TYR A 244 13348 17999 27248 237 1591 3521 C ATOM 2313 CE1 TYR A 244 155.373 -71.041 -1.501 1.00161.79 C ANISOU 2313 CE1 TYR A 244 13558 18816 29098 -94 1345 3564 C ATOM 2314 CE2 TYR A 244 154.855 -73.350 -1.892 1.00157.28 C ANISOU 2314 CE2 TYR A 244 13431 18469 27860 247 1539 3630 C ATOM 2315 CZ TYR A 244 155.733 -72.377 -1.441 1.00167.08 C ANISOU 2315 CZ TYR A 244 14295 19650 29539 81 1412 3654 C ATOM 2316 OH TYR A 244 156.957 -72.734 -0.931 1.00169.26 O ANISOU 2316 OH TYR A 244 14252 20020 30041 89 1348 3764 O ATOM 2317 N GLY A 245 152.675 -72.742 -5.501 1.00146.65 N ANISOU 2317 N GLY A 245 12828 16880 26014 518 2265 3874 N ATOM 2318 CA GLY A 245 152.676 -73.878 -6.413 1.00145.22 C ANISOU 2318 CA GLY A 245 12858 16782 25537 753 2525 3995 C ATOM 2319 C GLY A 245 152.076 -75.111 -5.773 1.00144.74 C ANISOU 2319 C GLY A 245 13032 16834 25129 813 2388 3789 C ATOM 2320 O GLY A 245 151.073 -75.640 -6.263 1.00142.54 O ANISOU 2320 O GLY A 245 13080 16580 24498 903 2450 3689 O ATOM 2321 N LYS A 246 152.683 -75.565 -4.658 1.00139.62 N ANISOU 2321 N LYS A 246 12204 16257 24589 762 2196 3731 N ATOM 2322 CA LYS A 246 152.243 -76.737 -3.895 1.00136.49 C ANISOU 2322 CA LYS A 246 11976 15967 23917 817 2059 3570 C ATOM 2323 C LYS A 246 151.135 -76.379 -2.884 1.00134.99 C ANISOU 2323 C LYS A 246 11913 15794 23582 657 1751 3286 C ATOM 2324 O LYS A 246 150.214 -77.174 -2.689 1.00132.08 O ANISOU 2324 O LYS A 246 11815 15473 22896 712 1703 3142 O ATOM 2325 CB LYS A 246 153.435 -77.382 -3.168 1.00140.49 C ANISOU 2325 CB LYS A 246 12215 16564 24603 857 2004 3675 C ATOM 2326 N ASN A 247 151.226 -75.186 -2.256 1.00129.94 N ANISOU 2326 N ASN A 247 11075 15107 23189 463 1552 3202 N ATOM 2327 CA ASN A 247 150.277 -74.702 -1.250 1.00126.84 C ANISOU 2327 CA ASN A 247 10766 14731 22698 307 1261 2927 C ATOM 2328 C ASN A 247 149.008 -74.067 -1.859 1.00125.28 C ANISOU 2328 C ASN A 247 10826 14432 22344 269 1303 2825 C ATOM 2329 O ASN A 247 148.118 -73.678 -1.103 1.00123.31 O ANISOU 2329 O ASN A 247 10670 14187 21994 155 1087 2598 O ATOM 2330 CB ASN A 247 150.952 -73.710 -0.303 1.00130.13 C ANISOU 2330 CB ASN A 247 10852 15138 23453 119 1026 2852 C ATOM 2331 N ARG A 248 148.906 -73.970 -3.200 1.00119.46 N ANISOU 2331 N ARG A 248 10200 13619 21571 374 1578 2993 N ATOM 2332 CA ARG A 248 147.699 -73.417 -3.820 1.00116.47 C ANISOU 2332 CA ARG A 248 10060 13168 21026 357 1619 2918 C ATOM 2333 C ARG A 248 146.618 -74.498 -3.946 1.00114.64 C ANISOU 2333 C ARG A 248 10174 13015 20371 463 1625 2788 C ATOM 2334 O ARG A 248 145.438 -74.168 -3.909 1.00112.86 O ANISOU 2334 O ARG A 248 10140 12764 19976 408 1537 2635 O ATOM 2335 CB ARG A 248 147.983 -72.750 -5.186 1.00118.38 C ANISOU 2335 CB ARG A 248 10267 13315 21397 425 1897 3158 C ATOM 2336 CG ARG A 248 148.273 -73.699 -6.350 1.00129.65 C ANISOU 2336 CG ARG A 248 11829 14806 22625 648 2191 3342 C ATOM 2337 CD ARG A 248 147.571 -73.262 -7.618 1.00139.24 C ANISOU 2337 CD ARG A 248 13231 15988 23685 731 2389 3436 C ATOM 2338 NE ARG A 248 147.492 -74.355 -8.589 1.00148.58 N ANISOU 2338 NE ARG A 248 14631 17265 24556 946 2611 3503 N ATOM 2339 CZ ARG A 248 146.419 -75.117 -8.781 1.00160.20 C ANISOU 2339 CZ ARG A 248 16415 18800 25655 1012 2579 3329 C ATOM 2340 NH1 ARG A 248 145.309 -74.902 -8.084 1.00148.21 N ANISOU 2340 NH1 ARG A 248 15027 17265 24021 887 2345 3103 N ATOM 2341 NH2 ARG A 248 146.442 -76.092 -9.680 1.00143.69 N ANISOU 2341 NH2 ARG A 248 14500 16785 23310 1205 2784 3373 N ATOM 2342 N ILE A 249 147.022 -75.778 -4.086 1.00108.81 N ANISOU 2342 N ILE A 249 9499 12359 19485 612 1730 2849 N ATOM 2343 CA ILE A 249 146.117 -76.923 -4.246 1.00105.81 C ANISOU 2343 CA ILE A 249 9423 12033 18747 719 1757 2735 C ATOM 2344 C ILE A 249 145.258 -77.061 -2.987 1.00105.84 C ANISOU 2344 C ILE A 249 9505 12081 18629 608 1478 2501 C ATOM 2345 O ILE A 249 144.042 -77.235 -3.092 1.00103.08 O ANISOU 2345 O ILE A 249 9402 11726 18038 603 1435 2357 O ATOM 2346 CB ILE A 249 146.927 -78.225 -4.567 1.00109.78 C ANISOU 2346 CB ILE A 249 9924 12588 19199 899 1934 2860 C ATOM 2347 CG1 ILE A 249 147.762 -78.067 -5.851 1.00112.69 C ANISOU 2347 CG1 ILE A 249 10219 12926 19670 1026 2232 3095 C ATOM 2348 CG2 ILE A 249 146.031 -79.457 -4.677 1.00108.53 C ANISOU 2348 CG2 ILE A 249 10061 12458 18716 1001 1958 2727 C ATOM 2349 CD1 ILE A 249 149.234 -78.494 -5.727 1.00123.34 C ANISOU 2349 CD1 ILE A 249 11307 14303 21255 1106 2340 3291 C ATOM 2350 N THR A 250 145.897 -76.937 -1.806 1.00102.05 N ANISOU 2350 N THR A 250 8802 11656 18318 519 1287 2467 N ATOM 2351 CA THR A 250 145.260 -77.057 -0.493 1.00 99.91 C ANISOU 2351 CA THR A 250 8563 11461 17937 427 1021 2265 C ATOM 2352 C THR A 250 144.317 -75.868 -0.210 1.00101.59 C ANISOU 2352 C THR A 250 8826 11615 18158 273 868 2091 C ATOM 2353 O THR A 250 143.201 -76.107 0.252 1.00 99.88 O ANISOU 2353 O THR A 250 8803 11430 17719 250 756 1924 O ATOM 2354 CB THR A 250 146.297 -77.280 0.635 1.00105.56 C ANISOU 2354 CB THR A 250 9013 12286 18810 398 866 2291 C ATOM 2355 OG1 THR A 250 145.657 -77.207 1.909 1.00 99.35 O ANISOU 2355 OG1 THR A 250 8249 11592 17908 306 603 2091 O ATOM 2356 CG2 THR A 250 147.474 -76.320 0.595 1.00107.78 C ANISOU 2356 CG2 THR A 250 8973 12529 19450 316 858 2400 C ATOM 2357 N ARG A 251 144.739 -74.616 -0.501 1.00 97.61 N ANISOU 2357 N ARG A 251 8147 11014 17925 173 878 2137 N ATOM 2358 CA ARG A 251 143.914 -73.421 -0.271 1.00 95.89 C ANISOU 2358 CA ARG A 251 7956 10713 17766 32 752 1983 C ATOM 2359 C ARG A 251 142.654 -73.445 -1.136 1.00 96.38 C ANISOU 2359 C ARG A 251 8308 10721 17589 85 861 1956 C ATOM 2360 O ARG A 251 141.585 -73.096 -0.637 1.00 95.19 O ANISOU 2360 O ARG A 251 8282 10564 17321 10 720 1774 O ATOM 2361 CB ARG A 251 144.708 -72.124 -0.519 1.00 98.19 C ANISOU 2361 CB ARG A 251 7984 10879 18445 -75 776 2070 C ATOM 2362 N ASP A 252 142.770 -73.897 -2.410 1.00 91.83 N ANISOU 2362 N ASP A 252 7840 10126 16926 222 1109 2131 N ATOM 2363 CA ASP A 252 141.656 -74.005 -3.365 1.00 89.87 C ANISOU 2363 CA ASP A 252 7860 9855 16432 292 1221 2120 C ATOM 2364 C ASP A 252 140.578 -74.963 -2.838 1.00 89.47 C ANISOU 2364 C ASP A 252 8043 9879 16072 315 1108 1935 C ATOM 2365 O ASP A 252 139.392 -74.647 -2.915 1.00 87.89 O ANISOU 2365 O ASP A 252 8008 9657 15729 276 1047 1818 O ATOM 2366 CB ASP A 252 142.158 -74.468 -4.750 1.00 92.94 C ANISOU 2366 CB ASP A 252 8302 10249 16762 456 1502 2331 C ATOM 2367 CG ASP A 252 142.810 -73.395 -5.622 1.00105.96 C ANISOU 2367 CG ASP A 252 9788 11814 18658 456 1667 2542 C ATOM 2368 OD1 ASP A 252 143.095 -72.285 -5.101 1.00107.76 O ANISOU 2368 OD1 ASP A 252 9813 11955 19178 315 1563 2538 O ATOM 2369 OD2 ASP A 252 143.050 -73.670 -6.821 1.00111.62 O ANISOU 2369 OD2 ASP A 252 10574 12552 19284 600 1905 2713 O ATOM 2370 N GLN A 253 141.006 -76.106 -2.269 1.00 84.09 N ANISOU 2370 N GLN A 253 7357 9280 15316 376 1081 1924 N ATOM 2371 CA GLN A 253 140.144 -77.137 -1.697 1.00 81.50 C ANISOU 2371 CA GLN A 253 7215 9014 14738 407 992 1783 C ATOM 2372 C GLN A 253 139.344 -76.597 -0.491 1.00 81.66 C ANISOU 2372 C GLN A 253 7233 9061 14734 273 748 1593 C ATOM 2373 O GLN A 253 138.161 -76.914 -0.370 1.00 80.41 O ANISOU 2373 O GLN A 253 7269 8910 14371 270 695 1470 O ATOM 2374 CB GLN A 253 140.987 -78.360 -1.289 1.00 83.68 C ANISOU 2374 CB GLN A 253 7426 9358 15009 504 1029 1857 C ATOM 2375 CG GLN A 253 140.245 -79.685 -1.400 1.00106.32 C ANISOU 2375 CG GLN A 253 10523 12242 17633 602 1078 1794 C ATOM 2376 CD GLN A 253 141.184 -80.863 -1.351 1.00135.34 C ANISOU 2376 CD GLN A 253 14136 15947 21340 730 1188 1912 C ATOM 2377 OE1 GLN A 253 141.712 -81.230 -0.293 1.00133.35 O ANISOU 2377 OE1 GLN A 253 13742 15766 21157 722 1078 1936 O ATOM 2378 NE2 GLN A 253 141.398 -81.497 -2.496 1.00131.09 N ANISOU 2378 NE2 GLN A 253 13703 15361 20743 860 1409 1988 N ATOM 2379 N VAL A 254 139.981 -75.778 0.376 1.00 76.17 N ANISOU 2379 N VAL A 254 6312 8380 14249 166 603 1562 N ATOM 2380 CA VAL A 254 139.363 -75.172 1.565 1.00 74.09 C ANISOU 2380 CA VAL A 254 6023 8154 13975 44 371 1366 C ATOM 2381 C VAL A 254 138.289 -74.164 1.107 1.00 75.63 C ANISOU 2381 C VAL A 254 6334 8245 14158 -26 369 1278 C ATOM 2382 O VAL A 254 137.193 -74.123 1.674 1.00 73.95 O ANISOU 2382 O VAL A 254 6250 8057 13791 -65 253 1120 O ATOM 2383 CB VAL A 254 140.430 -74.517 2.504 1.00 79.35 C ANISOU 2383 CB VAL A 254 6401 8864 14885 -50 219 1339 C ATOM 2384 CG1 VAL A 254 139.780 -73.828 3.699 1.00 78.75 C ANISOU 2384 CG1 VAL A 254 6306 8834 14782 -168 -17 1108 C ATOM 2385 CG2 VAL A 254 141.454 -75.540 3.003 1.00 80.03 C ANISOU 2385 CG2 VAL A 254 6362 9074 14971 30 210 1441 C ATOM 2386 N LEU A 255 138.592 -73.389 0.056 1.00 71.80 N ANISOU 2386 N LEU A 255 5799 7647 13834 -29 510 1402 N ATOM 2387 CA LEU A 255 137.675 -72.395 -0.499 1.00 70.65 C ANISOU 2387 CA LEU A 255 5741 7397 13707 -78 533 1367 C ATOM 2388 C LEU A 255 136.478 -73.044 -1.169 1.00 72.35 C ANISOU 2388 C LEU A 255 6228 7636 13627 5 604 1347 C ATOM 2389 O LEU A 255 135.389 -72.475 -1.114 1.00 70.68 O ANISOU 2389 O LEU A 255 6117 7386 13353 -45 539 1244 O ATOM 2390 CB LEU A 255 138.393 -71.476 -1.488 1.00 72.19 C ANISOU 2390 CB LEU A 255 5797 7475 14156 -81 690 1552 C ATOM 2391 CG LEU A 255 139.368 -70.490 -0.870 1.00 78.37 C ANISOU 2391 CG LEU A 255 6294 8186 15297 -202 604 1545 C ATOM 2392 CD1 LEU A 255 140.337 -69.958 -1.913 1.00 80.18 C ANISOU 2392 CD1 LEU A 255 6365 8318 15781 -170 806 1792 C ATOM 2393 CD2 LEU A 255 138.641 -69.377 -0.154 1.00 81.10 C ANISOU 2393 CD2 LEU A 255 6613 8447 15753 -338 439 1352 C ATOM 2394 N LYS A 256 136.670 -74.243 -1.775 1.00 69.29 N ANISOU 2394 N LYS A 256 5951 7308 13070 130 732 1433 N ATOM 2395 CA LYS A 256 135.598 -75.010 -2.418 1.00 68.13 C ANISOU 2395 CA LYS A 256 6053 7186 12646 209 790 1391 C ATOM 2396 C LYS A 256 134.549 -75.458 -1.379 1.00 71.08 C ANISOU 2396 C LYS A 256 6535 7607 12864 159 619 1204 C ATOM 2397 O LYS A 256 133.342 -75.411 -1.653 1.00 68.49 O ANISOU 2397 O LYS A 256 6369 7268 12386 153 596 1123 O ATOM 2398 CB LYS A 256 136.156 -76.213 -3.199 1.00 70.71 C ANISOU 2398 CB LYS A 256 6454 7553 12862 351 960 1496 C ATOM 2399 CG LYS A 256 136.692 -75.873 -4.612 1.00 89.36 C ANISOU 2399 CG LYS A 256 8806 9887 15258 441 1173 1674 C ATOM 2400 CD LYS A 256 135.834 -74.881 -5.466 1.00102.82 C ANISOU 2400 CD LYS A 256 10594 11556 16919 426 1209 1698 C ATOM 2401 CE LYS A 256 134.515 -75.412 -6.002 1.00110.83 C ANISOU 2401 CE LYS A 256 11854 12611 17643 473 1198 1590 C ATOM 2402 NZ LYS A 256 133.765 -74.369 -6.761 1.00112.57 N ANISOU 2402 NZ LYS A 256 12119 12811 17840 463 1222 1640 N ATOM 2403 N MET A 257 135.020 -75.830 -0.172 1.00 68.81 N ANISOU 2403 N MET A 257 6143 7383 12619 126 498 1148 N ATOM 2404 CA MET A 257 134.184 -76.229 0.963 1.00 68.19 C ANISOU 2404 CA MET A 257 6132 7371 12408 88 341 997 C ATOM 2405 C MET A 257 133.420 -75.020 1.521 1.00 73.61 C ANISOU 2405 C MET A 257 6797 8026 13144 -24 205 860 C ATOM 2406 O MET A 257 132.286 -75.165 1.987 1.00 73.11 O ANISOU 2406 O MET A 257 6855 7989 12935 -44 125 743 O ATOM 2407 CB MET A 257 135.043 -76.877 2.052 1.00 71.24 C ANISOU 2407 CB MET A 257 6385 7856 12826 103 260 1008 C ATOM 2408 CG MET A 257 135.591 -78.217 1.637 1.00 75.77 C ANISOU 2408 CG MET A 257 7001 8451 13336 226 392 1128 C ATOM 2409 SD MET A 257 137.036 -78.715 2.590 1.00 82.34 S ANISOU 2409 SD MET A 257 7605 9388 14291 259 340 1223 S ATOM 2410 CE MET A 257 136.271 -79.360 3.989 1.00 78.26 C ANISOU 2410 CE MET A 257 7140 8990 13604 253 179 1117 C ATOM 2411 N ALA A 258 134.043 -73.833 1.458 1.00 70.68 N ANISOU 2411 N ALA A 258 6265 7589 13002 -96 190 879 N ATOM 2412 CA ALA A 258 133.442 -72.582 1.898 1.00 69.80 C ANISOU 2412 CA ALA A 258 6114 7414 12991 -201 83 751 C ATOM 2413 C ALA A 258 132.381 -72.121 0.890 1.00 70.52 C ANISOU 2413 C ALA A 258 6355 7418 13022 -186 171 778 C ATOM 2414 O ALA A 258 131.353 -71.572 1.286 1.00 69.55 O ANISOU 2414 O ALA A 258 6294 7271 12861 -237 86 652 O ATOM 2415 CB ALA A 258 134.524 -71.521 2.059 1.00 72.27 C ANISOU 2415 CB ALA A 258 6193 7657 13610 -282 55 772 C ATOM 2416 N ALA A 259 132.631 -72.358 -0.412 1.00 64.99 N ANISOU 2416 N ALA A 259 5707 6684 12301 -106 343 945 N ATOM 2417 CA ALA A 259 131.733 -71.962 -1.494 1.00 63.61 C ANISOU 2417 CA ALA A 259 5662 6458 12049 -71 434 1001 C ATOM 2418 C ALA A 259 130.468 -72.804 -1.525 1.00 65.44 C ANISOU 2418 C ALA A 259 6103 6753 12008 -32 398 907 C ATOM 2419 O ALA A 259 129.412 -72.301 -1.890 1.00 64.13 O ANISOU 2419 O ALA A 259 6026 6558 11784 -43 385 878 O ATOM 2420 CB ALA A 259 132.454 -72.072 -2.829 1.00 65.29 C ANISOU 2420 CB ALA A 259 5866 6656 12284 23 629 1206 C ATOM 2421 N ALA A 260 130.583 -74.088 -1.154 1.00 62.69 N ANISOU 2421 N ALA A 260 5819 6485 11515 15 385 872 N ATOM 2422 CA ALA A 260 129.503 -75.073 -1.174 1.00 61.16 C ANISOU 2422 CA ALA A 260 5806 6338 11094 52 362 791 C ATOM 2423 C ALA A 260 128.355 -74.711 -0.237 1.00 66.31 C ANISOU 2423 C ALA A 260 6494 6998 11702 -22 218 644 C ATOM 2424 O ALA A 260 127.201 -74.748 -0.666 1.00 65.68 O ANISOU 2424 O ALA A 260 6540 6911 11503 -16 213 603 O ATOM 2425 CB ALA A 260 130.048 -76.445 -0.815 1.00 61.64 C ANISOU 2425 CB ALA A 260 5886 6455 11080 111 385 799 C ATOM 2426 N VAL A 261 128.665 -74.340 1.023 1.00 64.18 N ANISOU 2426 N VAL A 261 6108 6753 11524 -87 102 562 N ATOM 2427 CA VAL A 261 127.661 -74.008 2.050 1.00 63.57 C ANISOU 2427 CA VAL A 261 6055 6703 11398 -144 -28 415 C ATOM 2428 C VAL A 261 126.811 -72.763 1.679 1.00 66.04 C ANISOU 2428 C VAL A 261 6383 6929 11781 -193 -41 376 C ATOM 2429 O VAL A 261 125.629 -72.736 2.015 1.00 64.70 O ANISOU 2429 O VAL A 261 6298 6772 11514 -206 -96 288 O ATOM 2430 CB VAL A 261 128.260 -73.875 3.478 1.00 68.39 C ANISOU 2430 CB VAL A 261 6533 7388 12065 -188 -152 325 C ATOM 2431 CG1 VAL A 261 128.800 -75.208 3.969 1.00 67.93 C ANISOU 2431 CG1 VAL A 261 6476 7433 11903 -125 -148 373 C ATOM 2432 CG2 VAL A 261 129.345 -72.808 3.548 1.00 70.12 C ANISOU 2432 CG2 VAL A 261 6572 7554 12516 -246 -173 332 C ATOM 2433 N VAL A 262 127.389 -71.775 0.973 1.00 63.05 N ANISOU 2433 N VAL A 262 5916 6458 11581 -210 23 460 N ATOM 2434 CA VAL A 262 126.660 -70.563 0.586 1.00 63.02 C ANISOU 2434 CA VAL A 262 5911 6357 11678 -245 29 454 C ATOM 2435 C VAL A 262 125.831 -70.828 -0.692 1.00 66.10 C ANISOU 2435 C VAL A 262 6442 6750 11923 -176 121 556 C ATOM 2436 O VAL A 262 124.694 -70.358 -0.778 1.00 65.86 O ANISOU 2436 O VAL A 262 6472 6695 11855 -186 90 515 O ATOM 2437 CB VAL A 262 127.569 -69.293 0.483 1.00 68.37 C ANISOU 2437 CB VAL A 262 6412 6916 12650 -301 56 502 C ATOM 2438 CG1 VAL A 262 128.540 -69.343 -0.693 1.00 69.12 C ANISOU 2438 CG1 VAL A 262 6460 6981 12822 -245 207 709 C ATOM 2439 CG2 VAL A 262 126.747 -68.014 0.456 1.00 68.54 C ANISOU 2439 CG2 VAL A 262 6415 6821 12808 -346 38 459 C ATOM 2440 N LEU A 263 126.373 -71.606 -1.646 1.00 61.94 N ANISOU 2440 N LEU A 263 5966 6264 11304 -99 229 676 N ATOM 2441 CA LEU A 263 125.678 -71.920 -2.891 1.00 61.46 C ANISOU 2441 CA LEU A 263 6038 6236 11079 -24 307 755 C ATOM 2442 C LEU A 263 124.505 -72.883 -2.655 1.00 64.18 C ANISOU 2442 C LEU A 263 6527 6646 11212 -16 233 637 C ATOM 2443 O LEU A 263 123.466 -72.709 -3.287 1.00 64.16 O ANISOU 2443 O LEU A 263 6609 6657 11112 3 227 640 O ATOM 2444 CB LEU A 263 126.653 -72.491 -3.928 1.00 62.53 C ANISOU 2444 CB LEU A 263 6185 6406 11168 65 448 893 C ATOM 2445 CG LEU A 263 127.101 -71.529 -5.041 1.00 68.83 C ANISOU 2445 CG LEU A 263 6920 7163 12067 111 576 1079 C ATOM 2446 CD1 LEU A 263 128.125 -70.516 -4.537 1.00 70.31 C ANISOU 2446 CD1 LEU A 263 6911 7249 12557 45 590 1139 C ATOM 2447 CD2 LEU A 263 127.706 -72.294 -6.198 1.00 71.27 C ANISOU 2447 CD2 LEU A 263 7295 7548 12235 228 721 1196 C ATOM 2448 N ALA A 264 124.647 -73.858 -1.723 1.00 59.80 N ANISOU 2448 N ALA A 264 5985 6131 10603 -31 176 545 N ATOM 2449 CA ALA A 264 123.591 -74.824 -1.382 1.00 58.18 C ANISOU 2449 CA ALA A 264 5895 5972 10240 -30 116 446 C ATOM 2450 C ALA A 264 122.407 -74.143 -0.677 1.00 61.75 C ANISOU 2450 C ALA A 264 6345 6411 10705 -90 15 354 C ATOM 2451 O ALA A 264 121.269 -74.587 -0.836 1.00 60.37 O ANISOU 2451 O ALA A 264 6264 6259 10417 -86 -17 306 O ATOM 2452 CB ALA A 264 124.148 -75.933 -0.504 1.00 58.61 C ANISOU 2452 CB ALA A 264 5936 6063 10270 -22 99 409 C ATOM 2453 N PHE A 265 122.669 -73.067 0.093 1.00 59.17 N ANISOU 2453 N PHE A 265 5909 6046 10528 -143 -33 320 N ATOM 2454 CA PHE A 265 121.615 -72.332 0.783 1.00 58.77 C ANISOU 2454 CA PHE A 265 5850 5976 10505 -189 -113 225 C ATOM 2455 C PHE A 265 120.723 -71.590 -0.220 1.00 64.31 C ANISOU 2455 C PHE A 265 6593 6631 11212 -174 -82 284 C ATOM 2456 O PHE A 265 119.498 -71.647 -0.077 1.00 63.18 O ANISOU 2456 O PHE A 265 6507 6505 10994 -179 -130 231 O ATOM 2457 CB PHE A 265 122.201 -71.354 1.813 1.00 60.99 C ANISOU 2457 CB PHE A 265 6001 6219 10952 -246 -169 148 C ATOM 2458 CG PHE A 265 121.179 -70.628 2.668 1.00 62.23 C ANISOU 2458 CG PHE A 265 6149 6360 11134 -283 -245 22 C ATOM 2459 CD1 PHE A 265 120.680 -71.207 3.831 1.00 64.15 C ANISOU 2459 CD1 PHE A 265 6416 6694 11265 -286 -317 -88 C ATOM 2460 CD2 PHE A 265 120.749 -69.347 2.334 1.00 65.14 C ANISOU 2460 CD2 PHE A 265 6478 6623 11649 -304 -231 25 C ATOM 2461 CE1 PHE A 265 119.747 -70.532 4.625 1.00 64.93 C ANISOU 2461 CE1 PHE A 265 6507 6787 11377 -306 -372 -205 C ATOM 2462 CE2 PHE A 265 119.809 -68.677 3.126 1.00 68.06 C ANISOU 2462 CE2 PHE A 265 6839 6970 12051 -328 -289 -98 C ATOM 2463 CZ PHE A 265 119.317 -69.274 4.267 1.00 65.28 C ANISOU 2463 CZ PHE A 265 6517 6718 11567 -328 -358 -219 C ATOM 2464 N ILE A 266 121.321 -70.903 -1.224 1.00 63.30 N ANISOU 2464 N ILE A 266 6425 6452 11174 -148 1 411 N ATOM 2465 CA ILE A 266 120.526 -70.136 -2.196 1.00 64.42 C ANISOU 2465 CA ILE A 266 6592 6566 11321 -118 35 500 C ATOM 2466 C ILE A 266 119.824 -71.068 -3.209 1.00 69.50 C ANISOU 2466 C ILE A 266 7365 7304 11738 -55 50 536 C ATOM 2467 O ILE A 266 118.749 -70.709 -3.693 1.00 70.30 O ANISOU 2467 O ILE A 266 7503 7421 11787 -38 26 558 O ATOM 2468 CB ILE A 266 121.280 -68.974 -2.903 1.00 68.78 C ANISOU 2468 CB ILE A 266 7044 7029 12060 -103 128 649 C ATOM 2469 CG1 ILE A 266 122.480 -69.458 -3.736 1.00 70.69 C ANISOU 2469 CG1 ILE A 266 7279 7306 12274 -48 235 776 C ATOM 2470 CG2 ILE A 266 121.688 -67.898 -1.899 1.00 69.38 C ANISOU 2470 CG2 ILE A 266 6984 6985 12391 -180 93 576 C ATOM 2471 CD1 ILE A 266 122.846 -68.533 -4.936 1.00 82.80 C ANISOU 2471 CD1 ILE A 266 8758 8797 13905 11 360 987 C ATOM 2472 N ILE A 267 120.383 -72.255 -3.501 1.00 64.80 N ANISOU 2472 N ILE A 267 6834 6771 11018 -22 82 529 N ATOM 2473 CA ILE A 267 119.717 -73.176 -4.428 1.00 64.90 C ANISOU 2473 CA ILE A 267 6969 6864 10824 30 84 521 C ATOM 2474 C ILE A 267 118.438 -73.739 -3.758 1.00 68.79 C ANISOU 2474 C ILE A 267 7513 7376 11249 -16 -23 391 C ATOM 2475 O ILE A 267 117.395 -73.822 -4.409 1.00 69.30 O ANISOU 2475 O ILE A 267 7636 7486 11210 1 -61 383 O ATOM 2476 CB ILE A 267 120.684 -74.298 -4.931 1.00 68.32 C ANISOU 2476 CB ILE A 267 7456 7337 11165 84 161 533 C ATOM 2477 CG1 ILE A 267 121.803 -73.744 -5.848 1.00 70.30 C ANISOU 2477 CG1 ILE A 267 7661 7591 11460 151 287 688 C ATOM 2478 CG2 ILE A 267 119.954 -75.481 -5.594 1.00 68.60 C ANISOU 2478 CG2 ILE A 267 7622 7441 11004 119 139 451 C ATOM 2479 CD1 ILE A 267 121.367 -72.803 -7.037 1.00 83.15 C ANISOU 2479 CD1 ILE A 267 9294 9256 13042 211 334 822 C ATOM 2480 N CYS A 268 118.516 -74.055 -2.450 1.00 63.57 N ANISOU 2480 N CYS A 268 6816 6687 10650 -69 -70 303 N ATOM 2481 CA CYS A 268 117.432 -74.640 -1.669 1.00 62.16 C ANISOU 2481 CA CYS A 268 6668 6524 10425 -106 -148 203 C ATOM 2482 C CYS A 268 116.351 -73.640 -1.233 1.00 63.17 C ANISOU 2482 C CYS A 268 6755 6632 10614 -138 -206 179 C ATOM 2483 O CYS A 268 115.173 -74.003 -1.237 1.00 62.51 O ANISOU 2483 O CYS A 268 6709 6574 10469 -149 -257 138 O ATOM 2484 CB CYS A 268 118.004 -75.368 -0.460 1.00 62.71 C ANISOU 2484 CB CYS A 268 6710 6596 10520 -127 -159 149 C ATOM 2485 SG CYS A 268 118.940 -76.865 -0.872 1.00 67.30 S ANISOU 2485 SG CYS A 268 7350 7191 11032 -83 -91 166 S ATOM 2486 N TRP A 269 116.727 -72.416 -0.832 1.00 58.75 N ANISOU 2486 N TRP A 269 6110 6017 10194 -154 -198 198 N ATOM 2487 CA TRP A 269 115.750 -71.467 -0.297 1.00 58.32 C ANISOU 2487 CA TRP A 269 6013 5929 10219 -177 -241 159 C ATOM 2488 C TRP A 269 115.355 -70.276 -1.212 1.00 59.38 C ANISOU 2488 C TRP A 269 6117 6015 10432 -151 -212 260 C ATOM 2489 O TRP A 269 114.285 -69.716 -0.976 1.00 58.08 O ANISOU 2489 O TRP A 269 5933 5831 10303 -155 -246 239 O ATOM 2490 CB TRP A 269 116.245 -70.924 1.045 1.00 57.84 C ANISOU 2490 CB TRP A 269 5873 5832 10272 -216 -264 68 C ATOM 2491 CG TRP A 269 116.095 -71.911 2.165 1.00 58.66 C ANISOU 2491 CG TRP A 269 5996 6005 10285 -229 -307 -23 C ATOM 2492 CD1 TRP A 269 117.084 -72.649 2.750 1.00 61.44 C ANISOU 2492 CD1 TRP A 269 6337 6401 10606 -229 -306 -42 C ATOM 2493 CD2 TRP A 269 114.869 -72.298 2.806 1.00 58.52 C ANISOU 2493 CD2 TRP A 269 6006 6030 10201 -232 -345 -80 C ATOM 2494 NE1 TRP A 269 116.557 -73.444 3.745 1.00 60.62 N ANISOU 2494 NE1 TRP A 269 6250 6365 10416 -228 -339 -99 N ATOM 2495 CE2 TRP A 269 115.195 -73.262 3.789 1.00 62.21 C ANISOU 2495 CE2 TRP A 269 6476 6564 10596 -231 -359 -122 C ATOM 2496 CE3 TRP A 269 113.520 -71.918 2.650 1.00 59.84 C ANISOU 2496 CE3 TRP A 269 6181 6186 10370 -229 -364 -83 C ATOM 2497 CZ2 TRP A 269 114.220 -73.852 4.615 1.00 61.30 C ANISOU 2497 CZ2 TRP A 269 6374 6503 10414 -227 -379 -159 C ATOM 2498 CZ3 TRP A 269 112.557 -72.500 3.469 1.00 61.00 C ANISOU 2498 CZ3 TRP A 269 6337 6382 10457 -232 -389 -131 C ATOM 2499 CH2 TRP A 269 112.909 -73.450 4.440 1.00 61.46 C ANISOU 2499 CH2 TRP A 269 6400 6505 10448 -230 -391 -165 C ATOM 2500 N LEU A 270 116.170 -69.878 -2.219 1.00 54.80 N ANISOU 2500 N LEU A 270 5522 5416 9883 -114 -140 383 N ATOM 2501 CA LEU A 270 115.810 -68.741 -3.085 1.00 54.40 C ANISOU 2501 CA LEU A 270 5431 5324 9915 -74 -99 514 C ATOM 2502 C LEU A 270 114.515 -69.015 -3.894 1.00 56.55 C ANISOU 2502 C LEU A 270 5766 5685 10035 -32 -141 555 C ATOM 2503 O LEU A 270 113.649 -68.133 -3.873 1.00 57.63 O ANISOU 2503 O LEU A 270 5856 5783 10257 -23 -156 592 O ATOM 2504 CB LEU A 270 116.958 -68.302 -4.022 1.00 55.44 C ANISOU 2504 CB LEU A 270 5526 5431 10108 -31 5 669 C ATOM 2505 CG LEU A 270 116.703 -67.099 -4.951 1.00 61.46 C ANISOU 2505 CG LEU A 270 6232 6148 10971 25 72 850 C ATOM 2506 CD1 LEU A 270 116.876 -65.774 -4.222 1.00 62.04 C ANISOU 2506 CD1 LEU A 270 6183 6051 11338 -21 94 844 C ATOM 2507 CD2 LEU A 270 117.612 -67.143 -6.164 1.00 64.82 C ANISOU 2507 CD2 LEU A 270 6663 6623 11344 99 180 1027 C ATOM 2508 N PRO A 271 114.301 -70.188 -4.557 1.00 51.00 N ANISOU 2508 N PRO A 271 5158 5096 9126 -8 -168 535 N ATOM 2509 CA PRO A 271 113.042 -70.385 -5.307 1.00 50.77 C ANISOU 2509 CA PRO A 271 5168 5157 8964 23 -231 555 C ATOM 2510 C PRO A 271 111.767 -70.123 -4.482 1.00 55.10 C ANISOU 2510 C PRO A 271 5678 5679 9580 -18 -306 485 C ATOM 2511 O PRO A 271 110.874 -69.436 -4.984 1.00 56.69 O ANISOU 2511 O PRO A 271 5845 5902 9794 17 -328 566 O ATOM 2512 CB PRO A 271 113.130 -71.842 -5.760 1.00 52.04 C ANISOU 2512 CB PRO A 271 5428 5411 8934 27 -260 472 C ATOM 2513 CG PRO A 271 114.575 -72.093 -5.881 1.00 56.59 C ANISOU 2513 CG PRO A 271 6018 5964 9518 46 -170 501 C ATOM 2514 CD PRO A 271 115.188 -71.359 -4.722 1.00 51.94 C ANISOU 2514 CD PRO A 271 5342 5259 9133 -3 -143 491 C ATOM 2515 N PHE A 272 111.698 -70.611 -3.219 1.00 50.20 N ANISOU 2515 N PHE A 272 5053 5016 9004 -80 -335 353 N ATOM 2516 CA PHE A 272 110.552 -70.412 -2.324 1.00 49.53 C ANISOU 2516 CA PHE A 272 4929 4910 8980 -111 -387 286 C ATOM 2517 C PHE A 272 110.398 -68.940 -1.900 1.00 54.48 C ANISOU 2517 C PHE A 272 5469 5441 9789 -99 -352 324 C ATOM 2518 O PHE A 272 109.274 -68.440 -1.881 1.00 55.53 O ANISOU 2518 O PHE A 272 5564 5572 9965 -83 -378 346 O ATOM 2519 CB PHE A 272 110.653 -71.315 -1.079 1.00 50.49 C ANISOU 2519 CB PHE A 272 5065 5029 9088 -161 -405 159 C ATOM 2520 CG PHE A 272 109.728 -70.941 0.063 1.00 52.10 C ANISOU 2520 CG PHE A 272 5218 5210 9370 -180 -427 94 C ATOM 2521 CD1 PHE A 272 108.378 -71.261 0.019 1.00 55.19 C ANISOU 2521 CD1 PHE A 272 5599 5640 9731 -183 -474 92 C ATOM 2522 CD2 PHE A 272 110.207 -70.246 1.173 1.00 54.61 C ANISOU 2522 CD2 PHE A 272 5487 5470 9790 -190 -399 29 C ATOM 2523 CE1 PHE A 272 107.521 -70.892 1.062 1.00 56.14 C ANISOU 2523 CE1 PHE A 272 5665 5743 9922 -187 -475 45 C ATOM 2524 CE2 PHE A 272 109.348 -69.874 2.213 1.00 56.86 C ANISOU 2524 CE2 PHE A 272 5730 5747 10127 -191 -407 -40 C ATOM 2525 CZ PHE A 272 108.014 -70.208 2.154 1.00 54.84 C ANISOU 2525 CZ PHE A 272 5467 5530 9839 -185 -436 -23 C ATOM 2526 N HIS A 273 111.501 -68.268 -1.525 1.00 49.98 N ANISOU 2526 N HIS A 273 4860 4784 9345 -109 -295 321 N ATOM 2527 CA HIS A 273 111.471 -66.881 -1.062 1.00 50.24 C ANISOU 2527 CA HIS A 273 4806 4695 9588 -107 -258 326 C ATOM 2528 C HIS A 273 111.119 -65.901 -2.198 1.00 54.59 C ANISOU 2528 C HIS A 273 5316 5211 10217 -47 -213 504 C ATOM 2529 O HIS A 273 110.519 -64.852 -1.926 1.00 54.47 O ANISOU 2529 O HIS A 273 5230 5100 10364 -31 -193 522 O ATOM 2530 CB HIS A 273 112.789 -66.505 -0.369 1.00 51.04 C ANISOU 2530 CB HIS A 273 4865 4712 9817 -146 -223 257 C ATOM 2531 CG HIS A 273 112.874 -67.061 1.019 1.00 53.80 C ANISOU 2531 CG HIS A 273 5223 5093 10126 -190 -272 81 C ATOM 2532 ND1 HIS A 273 112.336 -66.386 2.096 1.00 55.79 N ANISOU 2532 ND1 HIS A 273 5428 5294 10474 -202 -287 -40 N ATOM 2533 CD2 HIS A 273 113.383 -68.238 1.452 1.00 55.07 C ANISOU 2533 CD2 HIS A 273 5433 5341 10150 -211 -300 22 C ATOM 2534 CE1 HIS A 273 112.551 -67.159 3.148 1.00 54.91 C ANISOU 2534 CE1 HIS A 273 5341 5262 10263 -225 -327 -163 C ATOM 2535 NE2 HIS A 273 113.179 -68.284 2.810 1.00 54.72 N ANISOU 2535 NE2 HIS A 273 5368 5316 10105 -232 -335 -120 N ATOM 2536 N VAL A 274 111.429 -66.267 -3.464 1.00 51.54 N ANISOU 2536 N VAL A 274 4970 4908 9704 -1 -194 639 N ATOM 2537 CA VAL A 274 111.081 -65.462 -4.649 1.00 52.66 C ANISOU 2537 CA VAL A 274 5076 5063 9871 78 -152 840 C ATOM 2538 C VAL A 274 109.553 -65.510 -4.819 1.00 54.52 C ANISOU 2538 C VAL A 274 5308 5374 10034 105 -227 853 C ATOM 2539 O VAL A 274 108.913 -64.468 -4.972 1.00 53.64 O ANISOU 2539 O VAL A 274 5121 5201 10060 149 -201 958 O ATOM 2540 CB VAL A 274 111.850 -65.937 -5.926 1.00 57.28 C ANISOU 2540 CB VAL A 274 5713 5756 10294 134 -110 970 C ATOM 2541 CG1 VAL A 274 111.155 -65.485 -7.218 1.00 58.09 C ANISOU 2541 CG1 VAL A 274 5804 5959 10310 233 -103 1169 C ATOM 2542 CG2 VAL A 274 113.311 -65.472 -5.899 1.00 57.32 C ANISOU 2542 CG2 VAL A 274 5675 5659 10447 126 -7 1027 C ATOM 2543 N LEU A 275 108.987 -66.730 -4.729 1.00 50.99 N ANISOU 2543 N LEU A 275 4930 5044 9399 75 -317 744 N ATOM 2544 CA LEU A 275 107.555 -67.038 -4.822 1.00 51.20 C ANISOU 2544 CA LEU A 275 4948 5155 9351 81 -405 730 C ATOM 2545 C LEU A 275 106.754 -66.357 -3.713 1.00 55.12 C ANISOU 2545 C LEU A 275 5371 5550 10024 61 -401 671 C ATOM 2546 O LEU A 275 105.631 -65.921 -3.967 1.00 55.42 O ANISOU 2546 O LEU A 275 5352 5613 10093 99 -432 744 O ATOM 2547 CB LEU A 275 107.359 -68.560 -4.749 1.00 50.38 C ANISOU 2547 CB LEU A 275 4924 5153 9065 30 -486 597 C ATOM 2548 CG LEU A 275 107.112 -69.308 -6.060 1.00 55.66 C ANISOU 2548 CG LEU A 275 5649 5979 9522 66 -551 636 C ATOM 2549 CD1 LEU A 275 108.167 -69.006 -7.109 1.00 56.20 C ANISOU 2549 CD1 LEU A 275 5752 6088 9515 134 -480 757 C ATOM 2550 CD2 LEU A 275 107.090 -70.792 -5.821 1.00 58.26 C ANISOU 2550 CD2 LEU A 275 6050 6351 9734 3 -612 476 C ATOM 2551 N THR A 276 107.339 -66.256 -2.501 1.00 51.80 N ANISOU 2551 N THR A 276 4947 5026 9709 10 -364 540 N ATOM 2552 CA THR A 276 106.762 -65.619 -1.312 1.00 52.28 C ANISOU 2552 CA THR A 276 4949 4993 9923 -2 -346 448 C ATOM 2553 C THR A 276 106.720 -64.090 -1.500 1.00 59.14 C ANISOU 2553 C THR A 276 5732 5726 11013 48 -273 547 C ATOM 2554 O THR A 276 105.736 -63.465 -1.091 1.00 60.39 O ANISOU 2554 O THR A 276 5830 5835 11281 76 -263 544 O ATOM 2555 CB THR A 276 107.542 -66.059 -0.063 1.00 55.83 C ANISOU 2555 CB THR A 276 5428 5412 10374 -61 -338 275 C ATOM 2556 OG1 THR A 276 107.272 -67.445 0.138 1.00 56.30 O ANISOU 2556 OG1 THR A 276 5549 5585 10259 -94 -396 213 O ATOM 2557 CG2 THR A 276 107.159 -65.294 1.200 1.00 49.45 C ANISOU 2557 CG2 THR A 276 4565 4516 9709 -62 -309 156 C ATOM 2558 N PHE A 277 107.757 -63.490 -2.124 1.00 56.30 N ANISOU 2558 N PHE A 277 5357 5296 10738 63 -210 645 N ATOM 2559 CA PHE A 277 107.759 -62.039 -2.370 1.00 57.30 C ANISOU 2559 CA PHE A 277 5391 5269 11113 112 -125 763 C ATOM 2560 C PHE A 277 106.743 -61.671 -3.457 1.00 63.39 C ANISOU 2560 C PHE A 277 6122 6107 11857 200 -129 974 C ATOM 2561 O PHE A 277 106.091 -60.631 -3.347 1.00 65.00 O ANISOU 2561 O PHE A 277 6240 6200 12256 247 -81 1043 O ATOM 2562 CB PHE A 277 109.157 -61.508 -2.737 1.00 58.90 C ANISOU 2562 CB PHE A 277 5568 5368 11444 102 -46 832 C ATOM 2563 CG PHE A 277 109.197 -59.997 -2.823 1.00 61.14 C ANISOU 2563 CG PHE A 277 5740 5449 12041 139 53 936 C ATOM 2564 CD1 PHE A 277 109.156 -59.215 -1.675 1.00 64.02 C ANISOU 2564 CD1 PHE A 277 6048 5638 12640 101 78 766 C ATOM 2565 CD2 PHE A 277 109.248 -59.355 -4.053 1.00 64.22 C ANISOU 2565 CD2 PHE A 277 6079 5825 12497 221 127 1204 C ATOM 2566 CE1 PHE A 277 109.165 -57.816 -1.758 1.00 66.32 C ANISOU 2566 CE1 PHE A 277 6230 5712 13257 134 176 849 C ATOM 2567 CE2 PHE A 277 109.268 -57.953 -4.133 1.00 68.01 C ANISOU 2567 CE2 PHE A 277 6443 6093 13303 259 233 1322 C ATOM 2568 CZ PHE A 277 109.227 -57.197 -2.985 1.00 66.13 C ANISOU 2568 CZ PHE A 277 6148 5652 13325 210 257 1136 C ATOM 2569 N LEU A 278 106.610 -62.529 -4.494 1.00 59.51 N ANISOU 2569 N LEU A 278 5688 5801 11123 226 -189 1069 N ATOM 2570 CA LEU A 278 105.651 -62.363 -5.588 1.00 60.26 C ANISOU 2570 CA LEU A 278 5748 6017 11129 312 -224 1258 C ATOM 2571 C LEU A 278 104.218 -62.466 -5.060 1.00 66.21 C ANISOU 2571 C LEU A 278 6461 6803 11893 311 -295 1197 C ATOM 2572 O LEU A 278 103.341 -61.732 -5.525 1.00 67.66 O ANISOU 2572 O LEU A 278 6561 6993 12155 388 -289 1353 O ATOM 2573 CB LEU A 278 105.888 -63.408 -6.693 1.00 59.72 C ANISOU 2573 CB LEU A 278 5764 6158 10768 331 -291 1307 C ATOM 2574 CG LEU A 278 107.112 -63.213 -7.580 1.00 64.00 C ANISOU 2574 CG LEU A 278 6331 6714 11272 376 -208 1444 C ATOM 2575 CD1 LEU A 278 107.377 -64.446 -8.408 1.00 62.99 C ANISOU 2575 CD1 LEU A 278 6306 6788 10838 382 -276 1412 C ATOM 2576 CD2 LEU A 278 106.953 -62.008 -8.485 1.00 68.90 C ANISOU 2576 CD2 LEU A 278 6861 7315 12003 489 -126 1721 C ATOM 2577 N ASP A 279 103.999 -63.364 -4.076 1.00 62.45 N ANISOU 2577 N ASP A 279 6033 6347 11349 231 -351 989 N ATOM 2578 CA ASP A 279 102.719 -63.585 -3.398 1.00 62.73 C ANISOU 2578 CA ASP A 279 6026 6407 11402 220 -402 915 C ATOM 2579 C ASP A 279 102.364 -62.379 -2.527 1.00 66.43 C ANISOU 2579 C ASP A 279 6411 6702 12127 250 -313 898 C ATOM 2580 O ASP A 279 101.188 -62.029 -2.448 1.00 68.50 O ANISOU 2580 O ASP A 279 6597 6972 12459 295 -323 953 O ATOM 2581 CB ASP A 279 102.757 -64.871 -2.546 1.00 63.89 C ANISOU 2581 CB ASP A 279 6243 6610 11422 132 -458 720 C ATOM 2582 CG ASP A 279 101.561 -65.055 -1.620 1.00 79.06 C ANISOU 2582 CG ASP A 279 8111 8534 13392 120 -479 641 C ATOM 2583 OD1 ASP A 279 100.442 -65.309 -2.135 1.00 81.23 O ANISOU 2583 OD1 ASP A 279 8334 8906 13625 140 -549 717 O ATOM 2584 OD2 ASP A 279 101.738 -64.925 -0.383 1.00 85.20 O ANISOU 2584 OD2 ASP A 279 8892 9228 14250 96 -424 508 O ATOM 2585 N ALA A 280 103.364 -61.752 -1.875 1.00 60.79 N ANISOU 2585 N ALA A 280 5704 5830 11563 227 -229 813 N ATOM 2586 CA ALA A 280 103.170 -60.576 -1.019 1.00 61.23 C ANISOU 2586 CA ALA A 280 5688 5699 11878 252 -141 753 C ATOM 2587 C ALA A 280 102.638 -59.396 -1.834 1.00 67.03 C ANISOU 2587 C ALA A 280 6322 6348 12797 347 -78 974 C ATOM 2588 O ALA A 280 101.759 -58.670 -1.363 1.00 68.35 O ANISOU 2588 O ALA A 280 6414 6425 13132 396 -33 971 O ATOM 2589 CB ALA A 280 104.480 -60.205 -0.353 1.00 61.99 C ANISOU 2589 CB ALA A 280 5807 5658 12089 198 -86 614 C ATOM 2590 N LEU A 281 103.149 -59.235 -3.077 1.00 62.63 N ANISOU 2590 N LEU A 281 5761 5833 12202 386 -69 1179 N ATOM 2591 CA LEU A 281 102.748 -58.178 -4.014 1.00 62.85 C ANISOU 2591 CA LEU A 281 5691 5807 12381 493 -4 1443 C ATOM 2592 C LEU A 281 101.319 -58.400 -4.511 1.00 64.95 C ANISOU 2592 C LEU A 281 5906 6231 12541 560 -81 1565 C ATOM 2593 O LEU A 281 100.636 -57.433 -4.820 1.00 64.93 O ANISOU 2593 O LEU A 281 5797 6157 12716 653 -24 1738 O ATOM 2594 CB LEU A 281 103.726 -58.096 -5.207 1.00 62.86 C ANISOU 2594 CB LEU A 281 5709 5855 12321 525 29 1640 C ATOM 2595 CG LEU A 281 105.195 -57.827 -4.876 1.00 65.63 C ANISOU 2595 CG LEU A 281 6082 6050 12802 463 110 1561 C ATOM 2596 CD1 LEU A 281 106.089 -58.273 -5.993 1.00 65.21 C ANISOU 2596 CD1 LEU A 281 6077 6124 12577 483 115 1715 C ATOM 2597 CD2 LEU A 281 105.437 -56.381 -4.541 1.00 68.31 C ANISOU 2597 CD2 LEU A 281 6314 6113 13527 489 242 1612 C ATOM 2598 N ALA A 282 100.874 -59.670 -4.584 1.00 61.33 N ANISOU 2598 N ALA A 282 5511 5977 11814 512 -209 1478 N ATOM 2599 CA ALA A 282 99.516 -60.049 -4.989 1.00 62.41 C ANISOU 2599 CA ALA A 282 5591 6277 11845 552 -309 1557 C ATOM 2600 C ALA A 282 98.519 -59.565 -3.946 1.00 68.34 C ANISOU 2600 C ALA A 282 6261 6918 12788 566 -267 1482 C ATOM 2601 O ALA A 282 97.513 -58.951 -4.309 1.00 69.72 O ANISOU 2601 O ALA A 282 6324 7105 13061 654 -263 1645 O ATOM 2602 CB ALA A 282 99.413 -61.556 -5.171 1.00 61.87 C ANISOU 2602 CB ALA A 282 5607 6409 11491 475 -447 1437 C ATOM 2603 N TRP A 283 98.839 -59.786 -2.652 1.00 64.72 N ANISOU 2603 N TRP A 283 5853 6355 12383 493 -227 1245 N ATOM 2604 CA TRP A 283 98.053 -59.325 -1.513 1.00 65.66 C ANISOU 2604 CA TRP A 283 5912 6366 12671 512 -164 1138 C ATOM 2605 C TRP A 283 98.006 -57.788 -1.439 1.00 73.35 C ANISOU 2605 C TRP A 283 6796 7124 13951 600 -31 1228 C ATOM 2606 O TRP A 283 96.979 -57.247 -1.018 1.00 74.28 O ANISOU 2606 O TRP A 283 6823 7184 14215 665 16 1249 O ATOM 2607 CB TRP A 283 98.605 -59.906 -0.208 1.00 63.16 C ANISOU 2607 CB TRP A 283 5681 6012 12303 426 -149 870 C ATOM 2608 CG TRP A 283 98.176 -61.324 0.036 1.00 63.21 C ANISOU 2608 CG TRP A 283 5735 6197 12087 361 -249 788 C ATOM 2609 CD1 TRP A 283 98.963 -62.439 0.012 1.00 64.67 C ANISOU 2609 CD1 TRP A 283 6022 6473 12077 277 -314 696 C ATOM 2610 CD2 TRP A 283 96.836 -61.781 0.287 1.00 63.48 C ANISOU 2610 CD2 TRP A 283 5698 6324 12097 376 -289 807 C ATOM 2611 NE1 TRP A 283 98.198 -63.562 0.236 1.00 63.56 N ANISOU 2611 NE1 TRP A 283 5882 6463 11805 236 -390 655 N ATOM 2612 CE2 TRP A 283 96.891 -63.186 0.416 1.00 65.91 C ANISOU 2612 CE2 TRP A 283 6070 6767 12207 291 -377 722 C ATOM 2613 CE3 TRP A 283 95.589 -61.136 0.404 1.00 66.06 C ANISOU 2613 CE3 TRP A 283 5901 6626 12571 455 -252 899 C ATOM 2614 CZ2 TRP A 283 95.755 -63.955 0.692 1.00 65.34 C ANISOU 2614 CZ2 TRP A 283 5937 6794 12094 274 -428 721 C ATOM 2615 CZ3 TRP A 283 94.460 -61.900 0.657 1.00 67.72 C ANISOU 2615 CZ3 TRP A 283 6051 6953 12726 442 -307 903 C ATOM 2616 CH2 TRP A 283 94.548 -63.293 0.795 1.00 67.14 C ANISOU 2616 CH2 TRP A 283 6038 7005 12468 348 -395 815 C ATOM 2617 N MET A 284 99.110 -57.093 -1.856 1.00 71.33 N ANISOU 2617 N MET A 284 6555 6737 13812 604 37 1287 N ATOM 2618 CA MET A 284 99.234 -55.621 -1.897 1.00 72.86 C ANISOU 2618 CA MET A 284 6656 6690 14336 680 174 1387 C ATOM 2619 C MET A 284 98.376 -55.006 -3.010 1.00 76.55 C ANISOU 2619 C MET A 284 7009 7199 14879 803 188 1707 C ATOM 2620 O MET A 284 97.907 -53.876 -2.876 1.00 78.31 O ANISOU 2620 O MET A 284 7127 7239 15387 889 298 1797 O ATOM 2621 CB MET A 284 100.692 -55.202 -2.121 1.00 75.72 C ANISOU 2621 CB MET A 284 7053 6916 14799 637 235 1383 C ATOM 2622 CG MET A 284 101.520 -55.152 -0.876 1.00 79.43 C ANISOU 2622 CG MET A 284 7579 7245 15356 547 266 1080 C ATOM 2623 SD MET A 284 103.238 -55.406 -1.324 1.00 83.92 S ANISOU 2623 SD MET A 284 8211 7796 15878 465 262 1079 S ATOM 2624 CE MET A 284 103.836 -56.294 0.169 1.00 79.23 C ANISOU 2624 CE MET A 284 7722 7246 15135 344 194 697 C ATOM 2625 N GLY A 285 98.205 -55.755 -4.094 1.00 71.08 N ANISOU 2625 N GLY A 285 6335 6746 13927 816 77 1871 N ATOM 2626 CA GLY A 285 97.452 -55.336 -5.266 1.00 71.83 C ANISOU 2626 CA GLY A 285 6326 6949 14017 937 58 2185 C ATOM 2627 C GLY A 285 98.337 -54.957 -6.438 1.00 75.20 C ANISOU 2627 C GLY A 285 6755 7397 14419 990 98 2420 C ATOM 2628 O GLY A 285 97.855 -54.364 -7.404 1.00 76.95 O ANISOU 2628 O GLY A 285 6877 7681 14678 1114 116 2717 O ATOM 2629 N VAL A 286 99.636 -55.305 -6.369 1.00 69.66 N ANISOU 2629 N VAL A 286 6158 6658 13653 906 117 2306 N ATOM 2630 CA VAL A 286 100.623 -55.014 -7.414 1.00 70.66 C ANISOU 2630 CA VAL A 286 6292 6802 13754 951 174 2518 C ATOM 2631 C VAL A 286 100.347 -55.927 -8.610 1.00 77.33 C ANISOU 2631 C VAL A 286 7178 7981 14223 994 41 2657 C ATOM 2632 O VAL A 286 99.970 -55.440 -9.677 1.00 78.90 O ANISOU 2632 O VAL A 286 7297 8289 14392 1122 53 2956 O ATOM 2633 CB VAL A 286 102.091 -55.139 -6.911 1.00 73.15 C ANISOU 2633 CB VAL A 286 6692 6975 14128 845 234 2343 C ATOM 2634 CG1 VAL A 286 103.071 -54.537 -7.914 1.00 74.52 C ANISOU 2634 CG1 VAL A 286 6832 7104 14378 908 342 2602 C ATOM 2635 CG2 VAL A 286 102.265 -54.507 -5.535 1.00 72.46 C ANISOU 2635 CG2 VAL A 286 6582 6605 14345 777 314 2105 C ATOM 2636 N ILE A 287 100.516 -57.245 -8.419 1.00 74.85 N ANISOU 2636 N ILE A 287 6984 7831 13626 892 -86 2436 N ATOM 2637 CA ILE A 287 100.268 -58.254 -9.443 1.00 76.11 C ANISOU 2637 CA ILE A 287 7197 8300 13423 912 -229 2490 C ATOM 2638 C ILE A 287 98.816 -58.718 -9.278 1.00 82.84 C ANISOU 2638 C ILE A 287 7993 9288 14194 911 -366 2438 C ATOM 2639 O ILE A 287 98.413 -59.102 -8.178 1.00 81.76 O ANISOU 2639 O ILE A 287 7870 9067 14129 822 -390 2217 O ATOM 2640 CB ILE A 287 101.334 -59.412 -9.438 1.00 77.90 C ANISOU 2640 CB ILE A 287 7574 8607 13416 811 -276 2295 C ATOM 2641 CG1 ILE A 287 100.947 -60.567 -10.378 1.00 78.89 C ANISOU 2641 CG1 ILE A 287 7760 9040 13172 820 -438 2282 C ATOM 2642 CG2 ILE A 287 101.700 -59.931 -8.047 1.00 76.30 C ANISOU 2642 CG2 ILE A 287 7440 8254 13296 673 -272 1987 C ATOM 2643 CD1 ILE A 287 101.337 -60.320 -11.848 1.00 91.68 C ANISOU 2643 CD1 ILE A 287 9378 10845 14610 947 -421 2544 C ATOM 2644 N ASN A 288 98.020 -58.605 -10.360 1.00 82.73 N ANISOU 2644 N ASN A 288 7901 9485 14046 1020 -447 2662 N ATOM 2645 CA ASN A 288 96.601 -58.968 -10.369 1.00 83.86 C ANISOU 2645 CA ASN A 288 7959 9777 14126 1030 -587 2654 C ATOM 2646 C ASN A 288 96.248 -60.022 -11.448 1.00 89.48 C ANISOU 2646 C ASN A 288 8703 10824 14469 1035 -782 2656 C ATOM 2647 O ASN A 288 95.109 -60.491 -11.487 1.00 89.91 O ANISOU 2647 O ASN A 288 8685 11020 14457 1021 -925 2618 O ATOM 2648 CB ASN A 288 95.738 -57.720 -10.541 1.00 88.08 C ANISOU 2648 CB ASN A 288 8327 10245 14896 1165 -516 2919 C ATOM 2649 CG ASN A 288 95.520 -56.962 -9.259 1.00116.37 C ANISOU 2649 CG ASN A 288 11857 13527 18833 1140 -380 2825 C ATOM 2650 OD1 ASN A 288 95.365 -57.538 -8.168 1.00107.50 O ANISOU 2650 OD1 ASN A 288 10783 12325 17739 1029 -400 2558 O ATOM 2651 ND2 ASN A 288 95.483 -55.644 -9.371 1.00112.50 N ANISOU 2651 ND2 ASN A 288 11262 12864 18620 1254 -233 3048 N ATOM 2652 N SER A 289 97.228 -60.421 -12.285 1.00 86.41 N ANISOU 2652 N SER A 289 8421 10561 13851 1050 -788 2678 N ATOM 2653 CA SER A 289 97.061 -61.426 -13.339 1.00 86.81 C ANISOU 2653 CA SER A 289 8524 10927 13534 1060 -963 2643 C ATOM 2654 C SER A 289 96.919 -62.804 -12.717 1.00 88.98 C ANISOU 2654 C SER A 289 8885 11219 13703 899 -1086 2308 C ATOM 2655 O SER A 289 97.893 -63.339 -12.188 1.00 87.06 O ANISOU 2655 O SER A 289 8766 10858 13456 808 -1024 2128 O ATOM 2656 CB SER A 289 98.247 -61.392 -14.305 1.00 90.72 C ANISOU 2656 CB SER A 289 9113 11521 13835 1134 -894 2758 C ATOM 2657 OG SER A 289 98.315 -62.538 -15.140 1.00 98.05 O ANISOU 2657 OG SER A 289 10134 12724 14398 1119 -1048 2633 O ATOM 2658 N CYS A 290 95.706 -63.383 -12.790 1.00 86.28 N ANISOU 2658 N CYS A 290 8466 11024 13292 866 -1259 2237 N ATOM 2659 CA CYS A 290 95.397 -64.711 -12.249 1.00 84.65 C ANISOU 2659 CA CYS A 290 8313 10833 13018 715 -1382 1942 C ATOM 2660 C CYS A 290 96.208 -65.809 -12.973 1.00 86.16 C ANISOU 2660 C CYS A 290 8652 11172 12914 675 -1460 1786 C ATOM 2661 O CYS A 290 96.457 -66.855 -12.376 1.00 83.83 O ANISOU 2661 O CYS A 290 8440 10805 12607 546 -1489 1539 O ATOM 2662 CB CYS A 290 93.897 -64.989 -12.296 1.00 86.64 C ANISOU 2662 CB CYS A 290 8419 11212 13289 698 -1549 1936 C ATOM 2663 SG CYS A 290 93.023 -64.633 -10.742 1.00 89.55 S ANISOU 2663 SG CYS A 290 8674 11335 14016 635 -1464 1890 S ATOM 2664 N GLU A 291 96.650 -65.546 -14.230 1.00 83.14 N ANISOU 2664 N GLU A 291 8300 10988 12300 795 -1474 1940 N ATOM 2665 CA GLU A 291 97.520 -66.424 -15.017 1.00 82.61 C ANISOU 2665 CA GLU A 291 8378 11068 11940 792 -1515 1818 C ATOM 2666 C GLU A 291 98.859 -66.577 -14.286 1.00 83.81 C ANISOU 2666 C GLU A 291 8658 10992 12193 727 -1343 1716 C ATOM 2667 O GLU A 291 99.304 -67.699 -14.065 1.00 82.85 O ANISOU 2667 O GLU A 291 8645 10853 11982 627 -1381 1476 O ATOM 2668 CB GLU A 291 97.744 -65.853 -16.430 1.00 86.49 C ANISOU 2668 CB GLU A 291 8861 11814 12185 968 -1520 2062 C ATOM 2669 CG GLU A 291 96.506 -65.834 -17.310 1.00102.38 C ANISOU 2669 CG GLU A 291 10755 14118 14028 1044 -1720 2151 C ATOM 2670 CD GLU A 291 96.626 -64.967 -18.551 1.00129.65 C ANISOU 2670 CD GLU A 291 14164 17810 17287 1249 -1693 2472 C ATOM 2671 OE1 GLU A 291 97.492 -65.261 -19.407 1.00126.11 O ANISOU 2671 OE1 GLU A 291 13830 17522 16564 1322 -1666 2478 O ATOM 2672 OE2 GLU A 291 95.846 -63.995 -18.670 1.00125.53 O ANISOU 2672 OE2 GLU A 291 13489 17320 16887 1347 -1691 2731 O ATOM 2673 N VAL A 292 99.460 -65.441 -13.848 1.00 78.67 N ANISOU 2673 N VAL A 292 7980 10151 11760 778 -1156 1895 N ATOM 2674 CA VAL A 292 100.736 -65.380 -13.118 1.00 75.73 C ANISOU 2674 CA VAL A 292 7697 9556 11520 723 -992 1825 C ATOM 2675 C VAL A 292 100.544 -65.922 -11.682 1.00 74.41 C ANISOU 2675 C VAL A 292 7543 9190 11541 574 -996 1589 C ATOM 2676 O VAL A 292 101.405 -66.661 -11.198 1.00 71.97 O ANISOU 2676 O VAL A 292 7337 8797 11210 492 -958 1416 O ATOM 2677 CB VAL A 292 101.335 -63.939 -13.126 1.00 80.41 C ANISOU 2677 CB VAL A 292 8230 10004 12320 820 -807 2086 C ATOM 2678 CG1 VAL A 292 102.627 -63.854 -12.306 1.00 78.58 C ANISOU 2678 CG1 VAL A 292 8068 9537 12251 749 -656 1996 C ATOM 2679 CG2 VAL A 292 101.578 -63.443 -14.553 1.00 82.53 C ANISOU 2679 CG2 VAL A 292 8483 10480 12394 981 -782 2353 C ATOM 2680 N ILE A 293 99.407 -65.580 -11.024 1.00 69.25 N ANISOU 2680 N ILE A 293 6777 8474 11059 552 -1036 1595 N ATOM 2681 CA ILE A 293 99.053 -66.017 -9.661 1.00 66.44 C ANISOU 2681 CA ILE A 293 6413 7957 10873 434 -1031 1405 C ATOM 2682 C ILE A 293 98.914 -67.556 -9.621 1.00 67.69 C ANISOU 2682 C ILE A 293 6644 8203 10872 327 -1157 1174 C ATOM 2683 O ILE A 293 99.338 -68.172 -8.643 1.00 65.66 O ANISOU 2683 O ILE A 293 6446 7816 10686 233 -1113 1009 O ATOM 2684 CB ILE A 293 97.770 -65.296 -9.131 1.00 69.92 C ANISOU 2684 CB ILE A 293 6705 8346 11515 459 -1041 1489 C ATOM 2685 CG1 ILE A 293 98.008 -63.788 -8.974 1.00 70.51 C ANISOU 2685 CG1 ILE A 293 6713 8271 11806 555 -889 1685 C ATOM 2686 CG2 ILE A 293 97.292 -65.880 -7.788 1.00 69.45 C ANISOU 2686 CG2 ILE A 293 6634 8165 11590 350 -1041 1298 C ATOM 2687 CD1 ILE A 293 96.736 -62.924 -9.059 1.00 77.85 C ANISOU 2687 CD1 ILE A 293 7483 9217 12880 639 -905 1859 C ATOM 2688 N ALA A 294 98.356 -68.165 -10.690 1.00 64.17 N ANISOU 2688 N ALA A 294 6190 7976 10215 345 -1312 1163 N ATOM 2689 CA ALA A 294 98.182 -69.614 -10.806 1.00 62.88 C ANISOU 2689 CA ALA A 294 6085 7889 9917 245 -1441 937 C ATOM 2690 C ALA A 294 99.527 -70.336 -10.820 1.00 64.81 C ANISOU 2690 C ALA A 294 6485 8083 10056 211 -1369 809 C ATOM 2691 O ALA A 294 99.661 -71.364 -10.161 1.00 62.98 O ANISOU 2691 O ALA A 294 6303 7764 9860 106 -1382 619 O ATOM 2692 CB ALA A 294 97.397 -69.951 -12.060 1.00 65.67 C ANISOU 2692 CB ALA A 294 6394 8499 10058 287 -1626 949 C ATOM 2693 N VAL A 295 100.528 -69.773 -11.532 1.00 61.97 N ANISOU 2693 N VAL A 295 6191 7769 9587 307 -1279 934 N ATOM 2694 CA VAL A 295 101.893 -70.310 -11.657 1.00 61.37 C ANISOU 2694 CA VAL A 295 6250 7656 9412 300 -1192 852 C ATOM 2695 C VAL A 295 102.558 -70.389 -10.259 1.00 64.06 C ANISOU 2695 C VAL A 295 6617 7757 9965 213 -1072 766 C ATOM 2696 O VAL A 295 103.150 -71.422 -9.935 1.00 62.56 O ANISOU 2696 O VAL A 295 6514 7520 9737 144 -1065 600 O ATOM 2697 CB VAL A 295 102.746 -69.501 -12.676 1.00 66.22 C ANISOU 2697 CB VAL A 295 6895 8365 9900 435 -1098 1054 C ATOM 2698 CG1 VAL A 295 104.189 -70.005 -12.747 1.00 64.86 C ANISOU 2698 CG1 VAL A 295 6846 8143 9654 431 -989 985 C ATOM 2699 CG2 VAL A 295 102.105 -69.522 -14.063 1.00 68.46 C ANISOU 2699 CG2 VAL A 295 7159 8927 9925 534 -1225 1132 C ATOM 2700 N ILE A 296 102.427 -69.324 -9.432 1.00 60.83 N ANISOU 2700 N ILE A 296 6129 7206 9777 223 -984 872 N ATOM 2701 CA ILE A 296 102.981 -69.273 -8.070 1.00 59.85 C ANISOU 2701 CA ILE A 296 6017 6883 9840 153 -883 787 C ATOM 2702 C ILE A 296 102.436 -70.464 -7.261 1.00 65.05 C ANISOU 2702 C ILE A 296 6688 7514 10514 47 -954 596 C ATOM 2703 O ILE A 296 103.217 -71.219 -6.685 1.00 63.20 O ANISOU 2703 O ILE A 296 6527 7209 10277 -10 -912 477 O ATOM 2704 CB ILE A 296 102.701 -67.904 -7.366 1.00 62.89 C ANISOU 2704 CB ILE A 296 6304 7134 10457 187 -796 904 C ATOM 2705 CG1 ILE A 296 103.259 -66.711 -8.198 1.00 63.72 C ANISOU 2705 CG1 ILE A 296 6382 7239 10589 294 -710 1119 C ATOM 2706 CG2 ILE A 296 103.266 -67.895 -5.918 1.00 62.70 C ANISOU 2706 CG2 ILE A 296 6295 6932 10595 118 -710 781 C ATOM 2707 CD1 ILE A 296 102.735 -65.319 -7.820 1.00 67.29 C ANISOU 2707 CD1 ILE A 296 6718 7572 11275 347 -639 1260 C ATOM 2708 N ASP A 297 101.108 -70.653 -7.295 1.00 64.68 N ANISOU 2708 N ASP A 297 6559 7531 10486 27 -1061 586 N ATOM 2709 CA ASP A 297 100.367 -71.708 -6.606 1.00 65.38 C ANISOU 2709 CA ASP A 297 6624 7595 10623 -70 -1128 441 C ATOM 2710 C ASP A 297 100.811 -73.112 -7.024 1.00 69.28 C ANISOU 2710 C ASP A 297 7211 8130 10981 -130 -1187 285 C ATOM 2711 O ASP A 297 100.946 -73.975 -6.152 1.00 68.28 O ANISOU 2711 O ASP A 297 7107 7907 10928 -206 -1160 171 O ATOM 2712 CB ASP A 297 98.857 -71.545 -6.859 1.00 69.83 C ANISOU 2712 CB ASP A 297 7059 8243 11229 -67 -1241 490 C ATOM 2713 CG ASP A 297 98.256 -70.226 -6.384 1.00 93.95 C ANISOU 2713 CG ASP A 297 10006 11243 14447 -4 -1178 640 C ATOM 2714 OD1 ASP A 297 98.679 -69.723 -5.305 1.00 95.66 O ANISOU 2714 OD1 ASP A 297 10230 11314 14801 -6 -1052 634 O ATOM 2715 OD2 ASP A 297 97.330 -69.720 -7.059 1.00105.79 O ANISOU 2715 OD2 ASP A 297 11409 12848 15940 49 -1257 753 O ATOM 2716 N LEU A 298 101.034 -73.341 -8.345 1.00 66.82 N ANISOU 2716 N LEU A 298 6953 7962 10473 -85 -1260 281 N ATOM 2717 CA LEU A 298 101.458 -74.637 -8.894 1.00 66.98 C ANISOU 2717 CA LEU A 298 7068 8025 10355 -128 -1316 114 C ATOM 2718 C LEU A 298 102.898 -74.974 -8.485 1.00 67.23 C ANISOU 2718 C LEU A 298 7211 7950 10382 -129 -1182 72 C ATOM 2719 O LEU A 298 103.167 -76.113 -8.121 1.00 66.61 O ANISOU 2719 O LEU A 298 7184 7803 10324 -197 -1181 -72 O ATOM 2720 CB LEU A 298 101.353 -74.631 -10.439 1.00 69.53 C ANISOU 2720 CB LEU A 298 7421 8558 10439 -54 -1419 124 C ATOM 2721 CG LEU A 298 100.105 -75.120 -11.175 1.00 77.62 C ANISOU 2721 CG LEU A 298 8375 9735 11383 -81 -1614 41 C ATOM 2722 CD1 LEU A 298 98.896 -74.198 -10.971 1.00 78.31 C ANISOU 2722 CD1 LEU A 298 8309 9862 11585 -62 -1671 189 C ATOM 2723 CD2 LEU A 298 100.381 -75.155 -12.646 1.00 84.08 C ANISOU 2723 CD2 LEU A 298 9258 10773 11917 11 -1688 34 C ATOM 2724 N ALA A 299 103.810 -73.979 -8.525 1.00 60.77 N ANISOU 2724 N ALA A 299 6416 7112 9563 -54 -1068 208 N ATOM 2725 CA ALA A 299 105.233 -74.124 -8.219 1.00 58.36 C ANISOU 2725 CA ALA A 299 6193 6720 9259 -45 -943 197 C ATOM 2726 C ALA A 299 105.530 -74.210 -6.718 1.00 57.67 C ANISOU 2726 C ALA A 299 6085 6471 9355 -110 -867 158 C ATOM 2727 O ALA A 299 106.506 -74.860 -6.347 1.00 55.62 O ANISOU 2727 O ALA A 299 5890 6149 9096 -130 -802 93 O ATOM 2728 CB ALA A 299 106.007 -72.956 -8.817 1.00 59.42 C ANISOU 2728 CB ALA A 299 6330 6888 9359 54 -853 371 C ATOM 2729 N LEU A 300 104.715 -73.543 -5.867 1.00 52.04 N ANISOU 2729 N LEU A 300 5280 5703 8789 -130 -870 202 N ATOM 2730 CA LEU A 300 104.910 -73.435 -4.416 1.00 49.61 C ANISOU 2730 CA LEU A 300 4944 5273 8631 -170 -798 172 C ATOM 2731 C LEU A 300 105.163 -74.777 -3.674 1.00 50.19 C ANISOU 2731 C LEU A 300 5059 5296 8715 -238 -790 50 C ATOM 2732 O LEU A 300 106.115 -74.786 -2.891 1.00 48.52 O ANISOU 2732 O LEU A 300 4873 5018 8543 -240 -709 38 O ATOM 2733 CB LEU A 300 103.758 -72.685 -3.743 1.00 49.67 C ANISOU 2733 CB LEU A 300 4848 5256 8768 -172 -813 217 C ATOM 2734 CG LEU A 300 104.061 -72.054 -2.379 1.00 53.18 C ANISOU 2734 CG LEU A 300 5261 5597 9349 -175 -722 210 C ATOM 2735 CD1 LEU A 300 105.176 -71.001 -2.462 1.00 52.66 C ANISOU 2735 CD1 LEU A 300 5210 5475 9322 -130 -640 269 C ATOM 2736 CD2 LEU A 300 102.817 -71.453 -1.797 1.00 56.12 C ANISOU 2736 CD2 LEU A 300 5535 5956 9834 -167 -732 240 C ATOM 2737 N PRO A 301 104.418 -75.901 -3.856 1.00 45.90 N ANISOU 2737 N PRO A 301 4514 4773 8154 -292 -867 -36 N ATOM 2738 CA PRO A 301 104.776 -77.123 -3.101 1.00 45.11 C ANISOU 2738 CA PRO A 301 4445 4597 8097 -346 -831 -122 C ATOM 2739 C PRO A 301 106.176 -77.651 -3.467 1.00 50.30 C ANISOU 2739 C PRO A 301 5202 5237 8672 -323 -772 -157 C ATOM 2740 O PRO A 301 106.864 -78.204 -2.599 1.00 49.37 O ANISOU 2740 O PRO A 301 5102 5050 8605 -337 -701 -175 O ATOM 2741 CB PRO A 301 103.669 -78.123 -3.471 1.00 47.37 C ANISOU 2741 CB PRO A 301 4696 4895 8406 -408 -930 -204 C ATOM 2742 CG PRO A 301 102.564 -77.297 -4.048 1.00 52.11 C ANISOU 2742 CG PRO A 301 5220 5582 8997 -392 -1020 -150 C ATOM 2743 CD PRO A 301 103.236 -76.138 -4.714 1.00 47.86 C ANISOU 2743 CD PRO A 301 4718 5105 8361 -308 -990 -58 C ATOM 2744 N PHE A 302 106.616 -77.435 -4.734 1.00 48.49 N ANISOU 2744 N PHE A 302 5032 5083 8310 -274 -792 -150 N ATOM 2745 CA PHE A 302 107.941 -77.852 -5.221 1.00 48.86 C ANISOU 2745 CA PHE A 302 5169 5126 8271 -236 -723 -171 C ATOM 2746 C PHE A 302 109.050 -76.947 -4.651 1.00 51.66 C ANISOU 2746 C PHE A 302 5513 5441 8674 -197 -620 -72 C ATOM 2747 O PHE A 302 110.147 -77.430 -4.380 1.00 49.98 O ANISOU 2747 O PHE A 302 5340 5184 8465 -188 -547 -86 O ATOM 2748 CB PHE A 302 108.011 -77.896 -6.753 1.00 52.05 C ANISOU 2748 CB PHE A 302 5633 5644 8499 -182 -767 -190 C ATOM 2749 CG PHE A 302 107.079 -78.904 -7.381 1.00 54.90 C ANISOU 2749 CG PHE A 302 6009 6047 8804 -225 -882 -331 C ATOM 2750 CD1 PHE A 302 107.439 -80.244 -7.477 1.00 58.57 C ANISOU 2750 CD1 PHE A 302 6538 6451 9265 -257 -873 -474 C ATOM 2751 CD2 PHE A 302 105.848 -78.512 -7.897 1.00 57.64 C ANISOU 2751 CD2 PHE A 302 6294 6490 9116 -233 -1003 -324 C ATOM 2752 CE1 PHE A 302 106.579 -81.176 -8.072 1.00 60.45 C ANISOU 2752 CE1 PHE A 302 6780 6709 9478 -307 -987 -631 C ATOM 2753 CE2 PHE A 302 104.995 -79.441 -8.498 1.00 61.41 C ANISOU 2753 CE2 PHE A 302 6770 7011 9552 -283 -1128 -474 C ATOM 2754 CZ PHE A 302 105.368 -80.767 -8.583 1.00 59.91 C ANISOU 2754 CZ PHE A 302 6646 6746 9370 -324 -1121 -637 C ATOM 2755 N ALA A 303 108.757 -75.641 -4.451 1.00 48.20 N ANISOU 2755 N ALA A 303 5011 5010 8294 -176 -615 24 N ATOM 2756 CA ALA A 303 109.688 -74.681 -3.856 1.00 46.62 C ANISOU 2756 CA ALA A 303 4780 4754 8179 -153 -532 96 C ATOM 2757 C ALA A 303 109.777 -74.897 -2.336 1.00 50.13 C ANISOU 2757 C ALA A 303 5188 5129 8730 -199 -509 44 C ATOM 2758 O ALA A 303 110.826 -74.624 -1.741 1.00 49.36 O ANISOU 2758 O ALA A 303 5082 4992 8681 -193 -450 53 O ATOM 2759 CB ALA A 303 109.250 -73.276 -4.173 1.00 47.52 C ANISOU 2759 CB ALA A 303 4833 4878 8344 -116 -533 201 C ATOM 2760 N ILE A 304 108.686 -75.441 -1.724 1.00 46.79 N ANISOU 2760 N ILE A 304 4737 4703 8337 -240 -558 -7 N ATOM 2761 CA ILE A 304 108.585 -75.811 -0.297 1.00 45.44 C ANISOU 2761 CA ILE A 304 4532 4496 8238 -270 -533 -44 C ATOM 2762 C ILE A 304 109.485 -77.042 -0.035 1.00 47.95 C ANISOU 2762 C ILE A 304 4900 4793 8527 -279 -494 -79 C ATOM 2763 O ILE A 304 110.215 -77.069 0.958 1.00 46.17 O ANISOU 2763 O ILE A 304 4658 4555 8329 -272 -448 -77 O ATOM 2764 CB ILE A 304 107.092 -76.041 0.149 1.00 47.87 C ANISOU 2764 CB ILE A 304 4783 4811 8594 -301 -579 -58 C ATOM 2765 CG1 ILE A 304 106.403 -74.689 0.454 1.00 48.29 C ANISOU 2765 CG1 ILE A 304 4768 4868 8714 -277 -582 -18 C ATOM 2766 CG2 ILE A 304 106.978 -76.976 1.365 1.00 47.03 C ANISOU 2766 CG2 ILE A 304 4657 4684 8529 -325 -545 -83 C ATOM 2767 CD1 ILE A 304 104.853 -74.721 0.551 1.00 56.17 C ANISOU 2767 CD1 ILE A 304 5695 5885 9761 -294 -631 -6 C ATOM 2768 N LEU A 305 109.436 -78.035 -0.942 1.00 45.28 N ANISOU 2768 N LEU A 305 4617 4454 8132 -289 -516 -117 N ATOM 2769 CA LEU A 305 110.201 -79.286 -0.863 1.00 45.21 C ANISOU 2769 CA LEU A 305 4657 4405 8116 -292 -472 -153 C ATOM 2770 C LEU A 305 111.730 -79.036 -0.899 1.00 50.42 C ANISOU 2770 C LEU A 305 5344 5064 8749 -247 -401 -115 C ATOM 2771 O LEU A 305 112.460 -79.743 -0.203 1.00 49.71 O ANISOU 2771 O LEU A 305 5253 4944 8689 -240 -350 -109 O ATOM 2772 CB LEU A 305 109.782 -80.224 -1.996 1.00 45.67 C ANISOU 2772 CB LEU A 305 4771 4458 8125 -308 -515 -230 C ATOM 2773 CG LEU A 305 110.385 -81.607 -1.988 1.00 50.50 C ANISOU 2773 CG LEU A 305 5431 4999 8759 -313 -467 -284 C ATOM 2774 CD1 LEU A 305 109.849 -82.430 -0.851 1.00 50.47 C ANISOU 2774 CD1 LEU A 305 5372 4926 8879 -355 -449 -276 C ATOM 2775 CD2 LEU A 305 110.152 -82.295 -3.305 1.00 55.27 C ANISOU 2775 CD2 LEU A 305 6102 5607 9291 -316 -512 -392 C ATOM 2776 N LEU A 306 112.199 -78.021 -1.679 1.00 47.25 N ANISOU 2776 N LEU A 306 4951 4697 8306 -212 -393 -72 N ATOM 2777 CA LEU A 306 113.607 -77.619 -1.768 1.00 46.41 C ANISOU 2777 CA LEU A 306 4846 4586 8202 -173 -323 -20 C ATOM 2778 C LEU A 306 114.144 -77.156 -0.412 1.00 48.85 C ANISOU 2778 C LEU A 306 5084 4876 8599 -186 -305 -4 C ATOM 2779 O LEU A 306 115.311 -77.399 -0.112 1.00 48.48 O ANISOU 2779 O LEU A 306 5027 4822 8570 -167 -257 17 O ATOM 2780 CB LEU A 306 113.804 -76.514 -2.804 1.00 47.11 C ANISOU 2780 CB LEU A 306 4934 4706 8259 -134 -312 50 C ATOM 2781 CG LEU A 306 113.934 -76.955 -4.262 1.00 52.99 C ANISOU 2781 CG LEU A 306 5755 5504 8873 -86 -298 52 C ATOM 2782 CD1 LEU A 306 113.776 -75.768 -5.196 1.00 54.07 C ANISOU 2782 CD1 LEU A 306 5876 5695 8974 -40 -295 150 C ATOM 2783 CD2 LEU A 306 115.271 -77.634 -4.525 1.00 55.13 C ANISOU 2783 CD2 LEU A 306 6067 5761 9117 -46 -210 58 C ATOM 2784 N GLY A 307 113.285 -76.531 0.394 1.00 45.60 N ANISOU 2784 N GLY A 307 4621 4469 8235 -211 -346 -20 N ATOM 2785 CA GLY A 307 113.596 -76.095 1.750 1.00 45.77 C ANISOU 2785 CA GLY A 307 4579 4497 8313 -219 -343 -37 C ATOM 2786 C GLY A 307 113.927 -77.271 2.644 1.00 52.37 C ANISOU 2786 C GLY A 307 5417 5353 9129 -215 -324 -45 C ATOM 2787 O GLY A 307 114.893 -77.211 3.409 1.00 54.06 O ANISOU 2787 O GLY A 307 5593 5592 9355 -201 -308 -40 O ATOM 2788 N PHE A 308 113.153 -78.368 2.518 1.00 49.10 N ANISOU 2788 N PHE A 308 5036 4924 8694 -227 -326 -51 N ATOM 2789 CA PHE A 308 113.346 -79.626 3.257 1.00 49.07 C ANISOU 2789 CA PHE A 308 5030 4917 8696 -219 -291 -32 C ATOM 2790 C PHE A 308 114.575 -80.379 2.751 1.00 53.62 C ANISOU 2790 C PHE A 308 5644 5465 9265 -190 -240 -9 C ATOM 2791 O PHE A 308 115.215 -81.076 3.534 1.00 53.44 O ANISOU 2791 O PHE A 308 5596 5453 9255 -163 -201 34 O ATOM 2792 CB PHE A 308 112.106 -80.536 3.145 1.00 50.97 C ANISOU 2792 CB PHE A 308 5283 5118 8965 -250 -302 -44 C ATOM 2793 CG PHE A 308 110.949 -80.171 4.038 1.00 52.79 C ANISOU 2793 CG PHE A 308 5455 5382 9221 -264 -324 -37 C ATOM 2794 CD1 PHE A 308 110.962 -80.498 5.389 1.00 56.62 C ANISOU 2794 CD1 PHE A 308 5890 5914 9708 -237 -286 10 C ATOM 2795 CD2 PHE A 308 109.839 -79.510 3.529 1.00 54.75 C ANISOU 2795 CD2 PHE A 308 5692 5629 9482 -292 -375 -65 C ATOM 2796 CE1 PHE A 308 109.890 -80.149 6.218 1.00 57.69 C ANISOU 2796 CE1 PHE A 308 5973 6093 9855 -236 -288 22 C ATOM 2797 CE2 PHE A 308 108.766 -79.172 4.357 1.00 57.79 C ANISOU 2797 CE2 PHE A 308 6016 6043 9899 -296 -380 -51 C ATOM 2798 CZ PHE A 308 108.803 -79.483 5.699 1.00 56.16 C ANISOU 2798 CZ PHE A 308 5766 5881 9690 -267 -331 -12 C ATOM 2799 N THR A 309 114.897 -80.239 1.445 1.00 51.09 N ANISOU 2799 N THR A 309 5378 5118 8915 -183 -233 -26 N ATOM 2800 CA THR A 309 116.043 -80.867 0.768 1.00 51.75 C ANISOU 2800 CA THR A 309 5503 5176 8984 -143 -169 -9 C ATOM 2801 C THR A 309 117.365 -80.338 1.358 1.00 56.14 C ANISOU 2801 C THR A 309 5999 5766 9567 -114 -138 49 C ATOM 2802 O THR A 309 118.343 -81.086 1.403 1.00 55.77 O ANISOU 2802 O THR A 309 5950 5705 9535 -76 -80 87 O ATOM 2803 CB THR A 309 115.960 -80.640 -0.752 1.00 60.31 C ANISOU 2803 CB THR A 309 6656 6258 10003 -130 -169 -39 C ATOM 2804 OG1 THR A 309 114.652 -80.998 -1.196 1.00 62.16 O ANISOU 2804 OG1 THR A 309 6925 6480 10213 -166 -228 -106 O ATOM 2805 CG2 THR A 309 116.996 -81.442 -1.540 1.00 57.88 C ANISOU 2805 CG2 THR A 309 6403 5923 9665 -77 -90 -38 C ATOM 2806 N ASN A 310 117.379 -79.074 1.845 1.00 52.69 N ANISOU 2806 N ASN A 310 5500 5367 9152 -133 -180 51 N ATOM 2807 CA ASN A 310 118.536 -78.447 2.489 1.00 52.67 C ANISOU 2807 CA ASN A 310 5419 5397 9196 -122 -176 79 C ATOM 2808 C ASN A 310 118.999 -79.274 3.703 1.00 57.33 C ANISOU 2808 C ASN A 310 5964 6036 9782 -100 -172 102 C ATOM 2809 O ASN A 310 120.197 -79.333 3.966 1.00 58.09 O ANISOU 2809 O ASN A 310 6006 6159 9906 -74 -153 143 O ATOM 2810 CB ASN A 310 118.194 -77.017 2.903 1.00 52.64 C ANISOU 2810 CB ASN A 310 5359 5407 9236 -156 -230 41 C ATOM 2811 CG ASN A 310 119.329 -76.222 3.512 1.00 71.21 C ANISOU 2811 CG ASN A 310 7615 7779 11661 -161 -244 38 C ATOM 2812 OD1 ASN A 310 119.238 -75.751 4.655 1.00 63.76 O ANISOU 2812 OD1 ASN A 310 6612 6885 10730 -177 -299 -23 O ATOM 2813 ND2 ASN A 310 120.399 -76.011 2.752 1.00 61.94 N ANISOU 2813 ND2 ASN A 310 6419 6573 10542 -147 -196 96 N ATOM 2814 N SER A 311 118.054 -79.941 4.404 1.00 53.63 N ANISOU 2814 N SER A 311 5509 5584 9285 -103 -185 94 N ATOM 2815 CA SER A 311 118.301 -80.814 5.556 1.00 53.64 C ANISOU 2815 CA SER A 311 5468 5641 9272 -67 -170 147 C ATOM 2816 C SER A 311 119.030 -82.096 5.142 1.00 56.37 C ANISOU 2816 C SER A 311 5839 5933 9648 -25 -93 217 C ATOM 2817 O SER A 311 119.703 -82.705 5.972 1.00 55.54 O ANISOU 2817 O SER A 311 5679 5879 9546 23 -70 292 O ATOM 2818 CB SER A 311 116.986 -81.174 6.241 1.00 58.39 C ANISOU 2818 CB SER A 311 6074 6258 9853 -78 -181 144 C ATOM 2819 OG SER A 311 116.323 -80.018 6.723 1.00 70.18 O ANISOU 2819 OG SER A 311 7540 7805 11321 -103 -239 79 O ATOM 2820 N CYS A 312 118.870 -82.515 3.869 1.00 53.48 N ANISOU 2820 N CYS A 312 5553 5469 9299 -33 -53 188 N ATOM 2821 CA CYS A 312 119.526 -83.698 3.307 1.00 54.74 C ANISOU 2821 CA CYS A 312 5749 5554 9496 11 31 224 C ATOM 2822 C CYS A 312 120.945 -83.326 2.857 1.00 58.36 C ANISOU 2822 C CYS A 312 6180 6032 9961 51 69 263 C ATOM 2823 O CYS A 312 121.827 -84.181 2.863 1.00 60.19 O ANISOU 2823 O CYS A 312 6398 6238 10234 108 142 325 O ATOM 2824 CB CYS A 312 118.722 -84.300 2.153 1.00 56.03 C ANISOU 2824 CB CYS A 312 6010 5619 9661 -11 49 145 C ATOM 2825 SG CYS A 312 116.932 -84.428 2.443 1.00 60.03 S ANISOU 2825 SG CYS A 312 6529 6100 10179 -79 -15 88 S ATOM 2826 N VAL A 313 121.155 -82.062 2.453 1.00 52.83 N ANISOU 2826 N VAL A 313 5462 5368 9243 26 31 237 N ATOM 2827 CA VAL A 313 122.439 -81.544 1.984 1.00 52.52 C ANISOU 2827 CA VAL A 313 5378 5342 9236 54 71 285 C ATOM 2828 C VAL A 313 123.376 -81.318 3.180 1.00 59.99 C ANISOU 2828 C VAL A 313 6201 6366 10227 66 38 339 C ATOM 2829 O VAL A 313 124.533 -81.733 3.110 1.00 61.35 O ANISOU 2829 O VAL A 313 6324 6543 10443 115 94 413 O ATOM 2830 CB VAL A 313 122.279 -80.256 1.130 1.00 54.97 C ANISOU 2830 CB VAL A 313 5698 5648 9541 23 51 260 C ATOM 2831 CG1 VAL A 313 123.618 -79.789 0.566 1.00 55.12 C ANISOU 2831 CG1 VAL A 313 5659 5666 9616 57 115 333 C ATOM 2832 CG2 VAL A 313 121.280 -80.460 -0.002 1.00 54.43 C ANISOU 2832 CG2 VAL A 313 5742 5539 9398 20 62 207 C ATOM 2833 N ASN A 314 122.873 -80.683 4.271 1.00 57.57 N ANISOU 2833 N ASN A 314 5841 6131 9901 27 -54 299 N ATOM 2834 CA ASN A 314 123.598 -80.336 5.510 1.00 58.45 C ANISOU 2834 CA ASN A 314 5833 6352 10023 34 -117 314 C ATOM 2835 C ASN A 314 124.588 -81.427 6.013 1.00 63.35 C ANISOU 2835 C ASN A 314 6397 7020 10655 105 -74 422 C ATOM 2836 O ASN A 314 125.736 -81.050 6.252 1.00 63.29 O ANISOU 2836 O ASN A 314 6285 7067 10697 116 -96 454 O ATOM 2837 CB ASN A 314 122.635 -79.953 6.635 1.00 59.79 C ANISOU 2837 CB ASN A 314 5989 6602 10127 9 -200 247 C ATOM 2838 CG ASN A 314 121.979 -78.596 6.469 1.00 82.07 C ANISOU 2838 CG ASN A 314 8816 9400 12966 -54 -258 141 C ATOM 2839 OD1 ASN A 314 122.403 -77.743 5.671 1.00 76.69 O ANISOU 2839 OD1 ASN A 314 8120 8656 12362 -84 -251 126 O ATOM 2840 ND2 ASN A 314 120.912 -78.370 7.221 1.00 72.55 N ANISOU 2840 ND2 ASN A 314 7625 8241 11701 -67 -304 81 N ATOM 2841 N PRO A 315 124.245 -82.744 6.138 1.00 60.87 N ANISOU 2841 N PRO A 315 6131 6674 10322 155 -9 487 N ATOM 2842 CA PRO A 315 125.255 -83.733 6.587 1.00 61.76 C ANISOU 2842 CA PRO A 315 6176 6822 10469 235 44 612 C ATOM 2843 C PRO A 315 126.529 -83.783 5.728 1.00 64.79 C ANISOU 2843 C PRO A 315 6527 7157 10933 269 113 663 C ATOM 2844 O PRO A 315 127.613 -84.006 6.270 1.00 65.37 O ANISOU 2844 O PRO A 315 6489 7306 11042 320 113 755 O ATOM 2845 CB PRO A 315 124.509 -85.068 6.488 1.00 63.87 C ANISOU 2845 CB PRO A 315 6524 6996 10750 270 128 659 C ATOM 2846 CG PRO A 315 123.085 -84.713 6.643 1.00 67.52 C ANISOU 2846 CG PRO A 315 7048 7449 11158 209 77 572 C ATOM 2847 CD PRO A 315 122.938 -83.404 5.926 1.00 62.26 C ANISOU 2847 CD PRO A 315 6408 6774 10473 141 20 459 C ATOM 2848 N PHE A 316 126.397 -83.553 4.404 1.00 59.32 N ANISOU 2848 N PHE A 316 5923 6357 10261 248 173 611 N ATOM 2849 CA PHE A 316 127.498 -83.556 3.438 1.00 58.39 C ANISOU 2849 CA PHE A 316 5787 6192 10208 289 263 661 C ATOM 2850 C PHE A 316 128.328 -82.267 3.498 1.00 60.77 C ANISOU 2850 C PHE A 316 5972 6554 10563 250 207 666 C ATOM 2851 O PHE A 316 129.496 -82.282 3.114 1.00 60.43 O ANISOU 2851 O PHE A 316 5854 6508 10600 292 271 747 O ATOM 2852 CB PHE A 316 126.959 -83.765 2.013 1.00 59.32 C ANISOU 2852 CB PHE A 316 6046 6199 10294 293 347 599 C ATOM 2853 CG PHE A 316 126.342 -85.118 1.758 1.00 60.34 C ANISOU 2853 CG PHE A 316 6278 6236 10411 330 415 576 C ATOM 2854 CD1 PHE A 316 124.992 -85.342 2.001 1.00 62.71 C ANISOU 2854 CD1 PHE A 316 6650 6509 10668 279 360 498 C ATOM 2855 CD2 PHE A 316 127.105 -86.164 1.256 1.00 63.08 C ANISOU 2855 CD2 PHE A 316 6643 6512 10813 416 541 627 C ATOM 2856 CE1 PHE A 316 124.421 -86.599 1.765 1.00 64.00 C ANISOU 2856 CE1 PHE A 316 6892 6565 10860 301 421 469 C ATOM 2857 CE2 PHE A 316 126.535 -87.420 1.022 1.00 66.03 C ANISOU 2857 CE2 PHE A 316 7106 6773 11210 444 607 586 C ATOM 2858 CZ PHE A 316 125.197 -87.629 1.274 1.00 63.54 C ANISOU 2858 CZ PHE A 316 6853 6422 10867 381 543 505 C ATOM 2859 N LEU A 317 127.733 -81.164 3.968 1.00 56.99 N ANISOU 2859 N LEU A 317 5471 6119 10065 172 96 581 N ATOM 2860 CA LEU A 317 128.391 -79.854 4.032 1.00 57.47 C ANISOU 2860 CA LEU A 317 5417 6205 10213 119 38 561 C ATOM 2861 C LEU A 317 129.191 -79.617 5.300 1.00 61.08 C ANISOU 2861 C LEU A 317 5716 6783 10708 111 -65 568 C ATOM 2862 O LEU A 317 130.145 -78.845 5.260 1.00 60.72 O ANISOU 2862 O LEU A 317 5545 6748 10780 83 -90 580 O ATOM 2863 CB LEU A 317 127.352 -78.719 3.927 1.00 56.98 C ANISOU 2863 CB LEU A 317 5401 6114 10135 41 -29 452 C ATOM 2864 CG LEU A 317 126.640 -78.494 2.603 1.00 61.60 C ANISOU 2864 CG LEU A 317 6107 6604 10694 37 43 444 C ATOM 2865 CD1 LEU A 317 125.574 -77.442 2.753 1.00 61.26 C ANISOU 2865 CD1 LEU A 317 6088 6546 10643 -30 -34 350 C ATOM 2866 CD2 LEU A 317 127.614 -78.082 1.513 1.00 65.38 C ANISOU 2866 CD2 LEU A 317 6546 7033 11262 62 140 530 C ATOM 2867 N TYR A 318 128.777 -80.193 6.431 1.00 58.40 N ANISOU 2867 N TYR A 318 5372 6544 10272 134 -130 556 N ATOM 2868 CA TYR A 318 129.446 -79.882 7.682 1.00 60.53 C ANISOU 2868 CA TYR A 318 5493 6967 10539 132 -250 543 C ATOM 2869 C TYR A 318 130.037 -81.104 8.397 1.00 68.59 C ANISOU 2869 C TYR A 318 6455 8091 11514 228 -232 674 C ATOM 2870 O TYR A 318 131.200 -81.045 8.808 1.00 69.44 O ANISOU 2870 O TYR A 318 6414 8290 11680 250 -276 731 O ATOM 2871 CB TYR A 318 128.477 -79.136 8.617 1.00 62.03 C ANISOU 2871 CB TYR A 318 5697 7236 10636 80 -371 400 C ATOM 2872 CG TYR A 318 128.021 -77.788 8.089 1.00 64.39 C ANISOU 2872 CG TYR A 318 6017 7438 11011 -11 -401 273 C ATOM 2873 CD1 TYR A 318 128.880 -76.691 8.083 1.00 67.65 C ANISOU 2873 CD1 TYR A 318 6299 7838 11565 -72 -463 216 C ATOM 2874 CD2 TYR A 318 126.730 -77.605 7.605 1.00 63.96 C ANISOU 2874 CD2 TYR A 318 6097 7296 10909 -36 -367 220 C ATOM 2875 CE1 TYR A 318 128.473 -75.453 7.586 1.00 68.14 C ANISOU 2875 CE1 TYR A 318 6370 7788 11730 -150 -475 121 C ATOM 2876 CE2 TYR A 318 126.309 -76.367 7.113 1.00 64.73 C ANISOU 2876 CE2 TYR A 318 6204 7303 11088 -107 -386 128 C ATOM 2877 CZ TYR A 318 127.183 -75.291 7.113 1.00 75.27 C ANISOU 2877 CZ TYR A 318 7413 8612 12574 -161 -434 83 C ATOM 2878 OH TYR A 318 126.789 -74.062 6.630 1.00 80.98 O ANISOU 2878 OH TYR A 318 8135 9224 13410 -225 -438 11 O ATOM 2879 N CYS A 319 129.260 -82.193 8.562 1.00 66.34 N ANISOU 2879 N CYS A 319 6271 7791 11144 285 -167 733 N ATOM 2880 CA CYS A 319 129.732 -83.373 9.288 1.00 67.08 C ANISOU 2880 CA CYS A 319 6306 7972 11208 386 -136 883 C ATOM 2881 C CYS A 319 130.673 -84.232 8.455 1.00 69.22 C ANISOU 2881 C CYS A 319 6563 8143 11595 455 -2 1014 C ATOM 2882 O CYS A 319 131.712 -84.636 8.972 1.00 70.38 O ANISOU 2882 O CYS A 319 6578 8387 11777 524 -10 1134 O ATOM 2883 CB CYS A 319 128.564 -84.204 9.813 1.00 67.60 C ANISOU 2883 CB CYS A 319 6465 8042 11178 422 -104 914 C ATOM 2884 SG CYS A 319 129.061 -85.605 10.858 1.00 73.15 S ANISOU 2884 SG CYS A 319 7079 8863 11851 560 -59 1133 S ATOM 2885 N PHE A 320 130.305 -84.549 7.200 1.00 63.38 N ANISOU 2885 N PHE A 320 5954 7223 10905 449 121 992 N ATOM 2886 CA PHE A 320 131.102 -85.445 6.356 1.00 63.32 C ANISOU 2886 CA PHE A 320 5955 7110 10995 528 269 1096 C ATOM 2887 C PHE A 320 132.405 -84.793 5.855 1.00 72.22 C ANISOU 2887 C PHE A 320 6964 8253 12222 529 283 1134 C ATOM 2888 O PHE A 320 133.309 -85.515 5.433 1.00 73.99 O ANISOU 2888 O PHE A 320 7148 8434 12533 614 398 1249 O ATOM 2889 CB PHE A 320 130.272 -86.025 5.187 1.00 62.94 C ANISOU 2889 CB PHE A 320 6086 6882 10946 528 389 1033 C ATOM 2890 CG PHE A 320 129.016 -86.792 5.567 1.00 62.08 C ANISOU 2890 CG PHE A 320 6078 6725 10786 524 393 1006 C ATOM 2891 CD1 PHE A 320 128.906 -87.416 6.802 1.00 63.65 C ANISOU 2891 CD1 PHE A 320 6208 7011 10965 570 363 1108 C ATOM 2892 CD2 PHE A 320 127.952 -86.899 4.680 1.00 61.93 C ANISOU 2892 CD2 PHE A 320 6209 6580 10741 477 428 890 C ATOM 2893 CE1 PHE A 320 127.748 -88.097 7.151 1.00 63.74 C ANISOU 2893 CE1 PHE A 320 6295 6969 10954 566 382 1104 C ATOM 2894 CE2 PHE A 320 126.792 -87.589 5.033 1.00 63.42 C ANISOU 2894 CE2 PHE A 320 6468 6715 10914 463 430 867 C ATOM 2895 CZ PHE A 320 126.703 -88.190 6.262 1.00 61.74 C ANISOU 2895 CZ PHE A 320 6182 6572 10705 506 415 981 C ATOM 2896 N VAL A 321 132.534 -83.456 5.957 1.00 70.47 N ANISOU 2896 N VAL A 321 6675 8089 12013 440 173 1048 N ATOM 2897 CA VAL A 321 133.766 -82.746 5.580 1.00 72.32 C ANISOU 2897 CA VAL A 321 6767 8334 12377 427 178 1092 C ATOM 2898 C VAL A 321 134.284 -81.909 6.791 1.00 78.51 C ANISOU 2898 C VAL A 321 7369 9281 13179 372 -4 1054 C ATOM 2899 O VAL A 321 134.974 -80.903 6.618 1.00 78.47 O ANISOU 2899 O VAL A 321 7244 9278 13293 309 -53 1025 O ATOM 2900 CB VAL A 321 133.637 -81.901 4.280 1.00 76.02 C ANISOU 2900 CB VAL A 321 7304 8680 12899 375 251 1038 C ATOM 2901 CG1 VAL A 321 133.566 -82.789 3.036 1.00 76.07 C ANISOU 2901 CG1 VAL A 321 7448 8564 12891 456 435 1089 C ATOM 2902 CG2 VAL A 321 132.466 -80.928 4.340 1.00 74.41 C ANISOU 2902 CG2 VAL A 321 7184 8459 12628 276 156 890 C ATOM 2903 N GLY A 322 133.961 -82.375 7.998 1.00 76.55 N ANISOU 2903 N GLY A 322 7097 9170 12819 402 -99 1058 N ATOM 2904 CA GLY A 322 134.345 -81.754 9.261 1.00 77.54 C ANISOU 2904 CA GLY A 322 7065 9488 12907 370 -283 1004 C ATOM 2905 C GLY A 322 135.814 -81.902 9.587 1.00 82.76 C ANISOU 2905 C GLY A 322 7516 10254 13674 415 -317 1121 C ATOM 2906 O GLY A 322 136.484 -80.899 9.849 1.00 83.53 O ANISOU 2906 O GLY A 322 7462 10413 13862 340 -438 1044 O ATOM 2907 N ASN A 323 136.324 -83.152 9.567 1.00 78.87 N ANISOU 2907 N ASN A 323 7004 9772 13192 537 -210 1308 N ATOM 2908 CA ASN A 323 137.724 -83.471 9.854 1.00 80.29 C ANISOU 2908 CA ASN A 323 6977 10053 13477 604 -224 1457 C ATOM 2909 C ASN A 323 138.666 -82.840 8.818 1.00 84.79 C ANISOU 2909 C ASN A 323 7459 10507 14252 560 -154 1473 C ATOM 2910 O ASN A 323 139.698 -82.282 9.192 1.00 85.88 O ANISOU 2910 O ASN A 323 7384 10745 14500 530 -257 1490 O ATOM 2911 CB ASN A 323 137.927 -84.992 9.909 1.00 79.87 C ANISOU 2911 CB ASN A 323 6945 9990 13412 755 -86 1663 C ATOM 2912 CG ASN A 323 137.065 -85.719 10.914 1.00 97.48 C ANISOU 2912 CG ASN A 323 9243 12327 15469 815 -125 1698 C ATOM 2913 OD1 ASN A 323 136.541 -85.146 11.877 1.00 94.26 O ANISOU 2913 OD1 ASN A 323 8817 12079 14917 769 -286 1593 O ATOM 2914 ND2 ASN A 323 136.926 -87.019 10.725 1.00 88.22 N ANISOU 2914 ND2 ASN A 323 8139 11064 14317 928 33 1855 N ATOM 2915 N ARG A 324 138.277 -82.902 7.528 1.00 80.36 N ANISOU 2915 N ARG A 324 7055 9743 13736 556 17 1466 N ATOM 2916 CA ARG A 324 139.001 -82.386 6.360 1.00 80.19 C ANISOU 2916 CA ARG A 324 6987 9595 13884 536 133 1504 C ATOM 2917 C ARG A 324 139.250 -80.870 6.460 1.00 83.74 C ANISOU 2917 C ARG A 324 7312 10060 14445 399 1 1388 C ATOM 2918 O ARG A 324 140.351 -80.426 6.134 1.00 84.62 O ANISOU 2918 O ARG A 324 7248 10159 14744 385 24 1464 O ATOM 2919 CB ARG A 324 138.213 -82.724 5.077 1.00 78.92 C ANISOU 2919 CB ARG A 324 7057 9253 13675 562 315 1483 C ATOM 2920 CG ARG A 324 138.898 -82.387 3.758 1.00 88.09 C ANISOU 2920 CG ARG A 324 8201 10298 14970 580 477 1552 C ATOM 2921 CD ARG A 324 137.945 -82.588 2.599 1.00 96.61 C ANISOU 2921 CD ARG A 324 9517 11242 15948 597 614 1490 C ATOM 2922 NE ARG A 324 138.420 -83.628 1.688 1.00110.43 N ANISOU 2922 NE ARG A 324 11330 12913 17714 728 822 1596 N ATOM 2923 CZ ARG A 324 137.641 -84.296 0.845 1.00129.79 C ANISOU 2923 CZ ARG A 324 13993 15267 20054 779 941 1538 C ATOM 2924 NH1 ARG A 324 136.335 -84.055 0.802 1.00116.98 N ANISOU 2924 NH1 ARG A 324 12529 13617 18299 708 869 1395 N ATOM 2925 NH2 ARG A 324 138.158 -85.222 0.047 1.00119.58 N ANISOU 2925 NH2 ARG A 324 12747 13903 18784 904 1131 1613 N ATOM 2926 N PHE A 325 138.239 -80.090 6.904 1.00 78.96 N ANISOU 2926 N PHE A 325 6787 9467 13745 302 -126 1208 N ATOM 2927 CA PHE A 325 138.322 -78.635 7.041 1.00 79.08 C ANISOU 2927 CA PHE A 325 6700 9468 13879 168 -249 1071 C ATOM 2928 C PHE A 325 139.385 -78.225 8.062 1.00 87.00 C ANISOU 2928 C PHE A 325 7444 10627 14986 130 -425 1052 C ATOM 2929 O PHE A 325 140.189 -77.342 7.763 1.00 87.48 O ANISOU 2929 O PHE A 325 7339 10633 15268 54 -447 1047 O ATOM 2930 CB PHE A 325 136.959 -78.045 7.432 1.00 79.00 C ANISOU 2930 CB PHE A 325 6837 9449 13732 95 -343 881 C ATOM 2931 CG PHE A 325 136.884 -76.546 7.320 1.00 80.49 C ANISOU 2931 CG PHE A 325 6956 9559 14067 -36 -423 739 C ATOM 2932 CD1 PHE A 325 136.573 -75.937 6.109 1.00 82.84 C ANISOU 2932 CD1 PHE A 325 7335 9675 14466 -70 -294 760 C ATOM 2933 CD2 PHE A 325 137.116 -75.737 8.427 1.00 83.85 C ANISOU 2933 CD2 PHE A 325 7233 10093 14533 -119 -627 582 C ATOM 2934 CE1 PHE A 325 136.514 -74.542 6.003 1.00 84.22 C ANISOU 2934 CE1 PHE A 325 7433 9754 14811 -185 -352 651 C ATOM 2935 CE2 PHE A 325 137.060 -74.344 8.321 1.00 87.42 C ANISOU 2935 CE2 PHE A 325 7614 10441 15162 -243 -694 439 C ATOM 2936 CZ PHE A 325 136.756 -73.755 7.111 1.00 84.68 C ANISOU 2936 CZ PHE A 325 7342 9891 14944 -276 -549 486 C ATOM 2937 N GLN A 326 139.392 -78.874 9.252 1.00 85.38 N ANISOU 2937 N GLN A 326 7195 10620 14626 186 -550 1051 N ATOM 2938 CA GLN A 326 140.321 -78.606 10.354 1.00 87.36 C ANISOU 2938 CA GLN A 326 7203 11072 14917 166 -746 1023 C ATOM 2939 C GLN A 326 141.760 -79.008 10.011 1.00 91.70 C ANISOU 2939 C GLN A 326 7549 11636 15658 222 -683 1218 C ATOM 2940 O GLN A 326 142.674 -78.246 10.312 1.00 93.24 O ANISOU 2940 O GLN A 326 7513 11886 16028 145 -810 1174 O ATOM 2941 CB GLN A 326 139.869 -79.330 11.630 1.00 89.16 C ANISOU 2941 CB GLN A 326 7459 11528 14888 245 -866 1010 C ATOM 2942 N GLN A 327 141.959 -80.194 9.397 1.00 86.98 N ANISOU 2942 N GLN A 327 7025 10981 15042 354 -487 1426 N ATOM 2943 CA GLN A 327 143.271 -80.721 9.009 1.00 88.00 C ANISOU 2943 CA GLN A 327 6978 11113 15347 435 -389 1635 C ATOM 2944 C GLN A 327 143.933 -79.883 7.913 1.00 93.54 C ANISOU 2944 C GLN A 327 7589 11646 16305 364 -283 1662 C ATOM 2945 O GLN A 327 145.150 -79.709 7.945 1.00 96.02 O ANISOU 2945 O GLN A 327 7658 12005 16820 363 -305 1764 O ATOM 2946 CB GLN A 327 143.162 -82.181 8.556 1.00 88.50 C ANISOU 2946 CB GLN A 327 7176 11122 15329 598 -182 1822 C ATOM 2947 CG GLN A 327 143.506 -83.178 9.652 1.00110.26 C ANISOU 2947 CG GLN A 327 9834 14079 17982 714 -259 1949 C ATOM 2948 CD GLN A 327 142.373 -83.381 10.631 1.00134.69 C ANISOU 2948 CD GLN A 327 13060 17290 20824 714 -379 1844 C ATOM 2949 OE1 GLN A 327 141.494 -84.235 10.440 1.00128.11 O ANISOU 2949 OE1 GLN A 327 12430 16375 19872 784 -255 1882 O ATOM 2950 NE2 GLN A 327 142.381 -82.615 11.715 1.00129.88 N ANISOU 2950 NE2 GLN A 327 12332 16881 20136 638 -621 1706 N ATOM 2951 N LYS A 328 143.147 -79.360 6.958 1.00 88.99 N ANISOU 2951 N LYS A 328 7196 10887 15731 311 -168 1587 N ATOM 2952 CA LYS A 328 143.662 -78.533 5.863 1.00 89.70 C ANISOU 2952 CA LYS A 328 7216 10816 16050 256 -46 1635 C ATOM 2953 C LYS A 328 143.876 -77.067 6.307 1.00 96.86 C ANISOU 2953 C LYS A 328 7947 11717 17139 88 -228 1481 C ATOM 2954 O LYS A 328 144.658 -76.351 5.674 1.00 98.53 O ANISOU 2954 O LYS A 328 7999 11827 17612 36 -161 1553 O ATOM 2955 CB LYS A 328 142.729 -78.611 4.646 1.00 89.98 C ANISOU 2955 CB LYS A 328 7514 10680 15993 286 152 1635 C ATOM 2956 N LEU A 329 143.203 -76.628 7.397 1.00 93.51 N ANISOU 2956 N LEU A 329 7543 11397 16589 7 -448 1270 N ATOM 2957 CA LEU A 329 143.339 -75.274 7.950 1.00 94.46 C ANISOU 2957 CA LEU A 329 7504 11513 16875 -152 -640 1077 C ATOM 2958 C LEU A 329 144.571 -75.188 8.872 1.00100.34 C ANISOU 2958 C LEU A 329 7942 12429 17755 -182 -826 1077 C ATOM 2959 O LEU A 329 145.295 -74.193 8.833 1.00101.32 O ANISOU 2959 O LEU A 329 7846 12488 18163 -299 -900 1023 O ATOM 2960 CB LEU A 329 142.071 -74.838 8.695 1.00 93.39 C ANISOU 2960 CB LEU A 329 7528 11418 16537 -213 -785 835 C ATOM 2961 N ARG A 330 144.825 -76.243 9.672 1.00 97.49 N ANISOU 2961 N ARG A 330 7552 12282 17207 -72 -897 1151 N ATOM 2962 CA ARG A 330 145.985 -76.341 10.565 1.00100.08 C ANISOU 2962 CA ARG A 330 7590 12816 17622 -70 -1077 1181 C ATOM 2963 C ARG A 330 147.281 -76.555 9.750 1.00106.98 C ANISOU 2963 C ARG A 330 8261 13608 18778 -31 -927 1422 C ATOM 2964 O ARG A 330 148.381 -76.453 10.302 1.00109.14 O ANISOU 2964 O ARG A 330 8248 14016 19204 -51 -1066 1459 O ATOM 2965 CB ARG A 330 145.790 -77.469 11.588 1.00 99.19 C ANISOU 2965 CB ARG A 330 7521 12957 17209 62 -1167 1233 C ATOM 2966 N SER A 331 147.139 -76.824 8.431 1.00102.96 N ANISOU 2966 N SER A 331 7897 12891 18334 28 -646 1580 N ATOM 2967 CA SER A 331 148.229 -77.013 7.473 1.00104.31 C ANISOU 2967 CA SER A 331 7917 12960 18754 83 -448 1817 C ATOM 2968 C SER A 331 148.698 -75.667 6.892 1.00109.25 C ANISOU 2968 C SER A 331 8374 13418 19716 -65 -436 1779 C ATOM 2969 O SER A 331 149.894 -75.385 6.921 1.00110.90 O ANISOU 2969 O SER A 331 8287 13646 20202 -99 -466 1878 O ATOM 2970 CB SER A 331 147.788 -77.948 6.349 1.00107.18 C ANISOU 2970 CB SER A 331 8533 13198 18994 229 -152 1981 C ATOM 2971 OG SER A 331 148.760 -78.028 5.318 1.00120.19 O ANISOU 2971 OG SER A 331 10058 14737 20870 289 66 2197 O ATOM 2972 N VAL A 332 147.756 -74.852 6.367 1.00104.77 N ANISOU 2972 N VAL A 332 7982 12684 19141 -149 -387 1652 N ATOM 2973 CA VAL A 332 148.004 -73.535 5.757 1.00105.58 C ANISOU 2973 CA VAL A 332 7957 12595 19565 -285 -349 1626 C ATOM 2974 C VAL A 332 148.549 -72.513 6.791 1.00112.21 C ANISOU 2974 C VAL A 332 8514 13488 20634 -457 -634 1427 C ATOM 2975 O VAL A 332 149.446 -71.738 6.447 1.00113.93 O ANISOU 2975 O VAL A 332 8475 13593 21219 -547 -612 1491 O ATOM 2976 CB VAL A 332 146.763 -72.972 5.004 1.00106.96 C ANISOU 2976 CB VAL A 332 8398 12592 19648 -315 -233 1547 C ATOM 2977 CG1 VAL A 332 146.568 -73.670 3.665 1.00105.55 C ANISOU 2977 CG1 VAL A 332 8414 12322 19369 -169 74 1768 C ATOM 2978 CG2 VAL A 332 145.493 -73.054 5.837 1.00104.79 C ANISOU 2978 CG2 VAL A 332 8343 12403 19070 -338 -397 1309 C ATOM 2979 N PHE A 333 148.032 -72.529 8.041 1.00108.49 N ANISOU 2979 N PHE A 333 8079 13191 19951 -498 -893 1187 N ATOM 2980 CA PHE A 333 148.447 -71.622 9.118 1.00133.75 C ANISOU 2980 CA PHE A 333 11035 16474 23309 -652 -1189 945 C ATOM 2981 C PHE A 333 149.898 -71.882 9.583 1.00150.98 C ANISOU 2981 C PHE A 333 12872 18809 25685 -652 -1305 1049 C ATOM 2982 O PHE A 333 150.344 -73.025 9.694 1.00104.64 O ANISOU 2982 O PHE A 333 6990 13101 19667 -505 -1256 1241 O ATOM 2983 CB PHE A 333 147.485 -71.730 10.308 1.00134.71 C ANISOU 2983 CB PHE A 333 11312 16783 23089 -656 -1412 681 C TER 2984 PHE A 333 ATOM 2985 N ASP B1002 138.391 -60.647 55.346 1.00170.10 N ANISOU 2985 N ASP B1002 24182 22733 17715 -1078 3259 -796 N ATOM 2986 CA ASP B1002 139.713 -60.714 54.727 1.00167.08 C ANISOU 2986 CA ASP B1002 23609 22515 17357 -1277 2593 -913 C ATOM 2987 C ASP B1002 139.751 -61.740 53.583 1.00167.43 C ANISOU 2987 C ASP B1002 22938 22759 17921 -1295 2364 -787 C ATOM 2988 O ASP B1002 140.361 -61.459 52.550 1.00164.07 O ANISOU 2988 O ASP B1002 22157 22446 17737 -1371 2031 -881 O ATOM 2989 CB ASP B1002 140.797 -61.028 55.771 1.00171.37 C ANISOU 2989 CB ASP B1002 24663 23096 17353 -1417 2197 -959 C ATOM 2990 CG ASP B1002 141.181 -59.840 56.632 1.00183.31 C ANISOU 2990 CG ASP B1002 26858 24461 18329 -1521 2195 -1208 C ATOM 2991 OD1 ASP B1002 141.888 -58.943 56.123 1.00182.46 O ANISOU 2991 OD1 ASP B1002 26701 24360 18268 -1699 1923 -1436 O ATOM 2992 OD2 ASP B1002 140.805 -59.824 57.823 1.00192.93 O ANISOU 2992 OD2 ASP B1002 28701 25539 19063 -1448 2480 -1187 O ATOM 2993 N LEU B1003 139.108 -62.918 53.764 1.00164.76 N ANISOU 2993 N LEU B1003 22433 22428 17741 -1245 2581 -588 N ATOM 2994 CA LEU B1003 139.047 -63.976 52.745 1.00161.79 C ANISOU 2994 CA LEU B1003 21454 22185 17833 -1298 2427 -500 C ATOM 2995 C LEU B1003 138.012 -63.624 51.666 1.00164.90 C ANISOU 2995 C LEU B1003 21289 22667 18698 -1230 2655 -528 C ATOM 2996 O LEU B1003 138.261 -63.868 50.482 1.00161.64 O ANISOU 2996 O LEU B1003 20407 22405 18603 -1285 2369 -576 O ATOM 2997 CB LEU B1003 138.724 -65.341 53.376 1.00163.73 C ANISOU 2997 CB LEU B1003 21793 22344 18071 -1309 2632 -296 C ATOM 2998 CG LEU B1003 138.975 -66.556 52.484 1.00165.99 C ANISOU 2998 CG LEU B1003 21629 22698 18740 -1407 2421 -234 C ATOM 2999 CD1 LEU B1003 140.285 -67.235 52.840 1.00166.16 C ANISOU 2999 CD1 LEU B1003 21905 22725 18501 -1402 2003 -153 C ATOM 3000 CD2 LEU B1003 137.819 -67.531 52.557 1.00170.39 C ANISOU 3000 CD2 LEU B1003 21997 23144 19599 -1461 2900 -105 C ATOM 3001 N GLU B1004 136.856 -63.050 52.083 1.00164.30 N ANISOU 3001 N GLU B1004 21269 22514 18643 -1081 3171 -488 N ATOM 3002 CA GLU B1004 135.775 -62.606 51.196 1.00164.08 C ANISOU 3002 CA GLU B1004 20700 22618 19025 -942 3403 -481 C ATOM 3003 C GLU B1004 136.241 -61.395 50.375 1.00166.71 C ANISOU 3003 C GLU B1004 21000 22996 19346 -837 3168 -605 C ATOM 3004 O GLU B1004 135.770 -61.207 49.255 1.00165.23 O ANISOU 3004 O GLU B1004 20298 22994 19489 -735 3106 -599 O ATOM 3005 CB GLU B1004 134.510 -62.259 52.010 1.00169.66 C ANISOU 3005 CB GLU B1004 21511 23221 19733 -757 4061 -376 C ATOM 3006 CG GLU B1004 133.220 -62.239 51.202 1.00180.08 C ANISOU 3006 CG GLU B1004 22106 24758 21559 -624 4315 -307 C ATOM 3007 CD GLU B1004 131.989 -61.777 51.960 1.00200.26 C ANISOU 3007 CD GLU B1004 24693 27233 24165 -389 5005 -186 C ATOM 3008 OE1 GLU B1004 131.744 -60.550 52.007 1.00193.94 O ANISOU 3008 OE1 GLU B1004 24072 26360 23255 -97 5225 -192 O ATOM 3009 OE2 GLU B1004 131.254 -62.644 52.488 1.00193.35 O ANISOU 3009 OE2 GLU B1004 23662 26341 23461 -488 5378 -76 O ATOM 3010 N ASP B1005 137.181 -60.595 50.934 1.00163.79 N ANISOU 3010 N ASP B1005 21197 22457 18578 -880 3033 -721 N ATOM 3011 CA ASP B1005 137.758 -59.393 50.324 1.00162.59 C ANISOU 3011 CA ASP B1005 21151 22251 18374 -841 2878 -854 C ATOM 3012 C ASP B1005 138.784 -59.728 49.219 1.00162.86 C ANISOU 3012 C ASP B1005 20852 22446 18583 -1001 2349 -917 C ATOM 3013 O ASP B1005 138.984 -58.906 48.321 1.00161.24 O ANISOU 3013 O ASP B1005 20537 22241 18484 -926 2283 -971 O ATOM 3014 CB ASP B1005 138.404 -58.500 51.401 1.00166.96 C ANISOU 3014 CB ASP B1005 22449 22546 18443 -926 2939 -1004 C ATOM 3015 CG ASP B1005 137.430 -57.993 52.454 1.00181.35 C ANISOU 3015 CG ASP B1005 24710 24154 20042 -734 3531 -965 C ATOM 3016 OD1 ASP B1005 136.549 -57.175 52.106 1.00183.28 O ANISOU 3016 OD1 ASP B1005 24864 24319 20454 -457 3938 -915 O ATOM 3017 OD2 ASP B1005 137.559 -58.402 53.628 1.00189.39 O ANISOU 3017 OD2 ASP B1005 26184 25079 20695 -823 3608 -967 O ATOM 3018 N ASN B1006 139.421 -60.919 49.277 1.00158.29 N ANISOU 3018 N ASN B1006 20145 21972 18027 -1183 2029 -889 N ATOM 3019 CA ASN B1006 140.391 -61.357 48.267 1.00155.30 C ANISOU 3019 CA ASN B1006 19452 21730 17824 -1306 1590 -932 C ATOM 3020 C ASN B1006 139.698 -62.130 47.148 1.00158.11 C ANISOU 3020 C ASN B1006 19245 22261 18567 -1247 1584 -864 C ATOM 3021 O ASN B1006 140.110 -62.019 45.990 1.00155.70 O ANISOU 3021 O ASN B1006 18671 22060 18426 -1245 1360 -912 O ATOM 3022 CB ASN B1006 141.509 -62.191 48.883 1.00156.26 C ANISOU 3022 CB ASN B1006 19739 21867 17764 -1478 1257 -925 C ATOM 3023 CG ASN B1006 142.613 -61.362 49.497 1.00180.80 C ANISOU 3023 CG ASN B1006 23237 24915 20545 -1613 1029 -1063 C ATOM 3024 OD1 ASN B1006 142.840 -61.385 50.706 1.00178.46 O ANISOU 3024 OD1 ASN B1006 23368 24559 19879 -1665 1012 -1073 O ATOM 3025 ND2 ASN B1006 143.349 -60.625 48.678 1.00171.09 N ANISOU 3025 ND2 ASN B1006 21877 23703 19427 -1698 844 -1184 N ATOM 3026 N TRP B1007 138.644 -62.903 47.487 1.00156.56 N ANISOU 3026 N TRP B1007 18886 22095 18504 -1225 1845 -769 N ATOM 3027 CA TRP B1007 137.863 -63.649 46.502 1.00156.20 C ANISOU 3027 CA TRP B1007 18294 22233 18822 -1237 1840 -752 C ATOM 3028 C TRP B1007 136.993 -62.695 45.690 1.00158.30 C ANISOU 3028 C TRP B1007 18258 22654 19236 -1015 1956 -754 C ATOM 3029 O TRP B1007 136.808 -62.927 44.494 1.00157.01 O ANISOU 3029 O TRP B1007 17684 22696 19279 -1004 1753 -793 O ATOM 3030 CB TRP B1007 137.019 -64.752 47.146 1.00158.02 C ANISOU 3030 CB TRP B1007 18428 22427 19185 -1344 2118 -668 C ATOM 3031 CG TRP B1007 137.718 -66.081 47.184 1.00158.87 C ANISOU 3031 CG TRP B1007 18587 22454 19324 -1541 1932 -653 C ATOM 3032 CD1 TRP B1007 138.165 -66.737 48.293 1.00163.25 C ANISOU 3032 CD1 TRP B1007 19549 22816 19661 -1592 2014 -547 C ATOM 3033 CD2 TRP B1007 138.091 -66.896 46.058 1.00157.27 C ANISOU 3033 CD2 TRP B1007 18073 22334 19347 -1666 1653 -732 C ATOM 3034 NE1 TRP B1007 138.774 -67.919 47.932 1.00162.15 N ANISOU 3034 NE1 TRP B1007 19352 22622 19634 -1712 1827 -529 N ATOM 3035 CE2 TRP B1007 138.748 -68.040 46.566 1.00161.67 C ANISOU 3035 CE2 TRP B1007 18865 22712 19852 -1775 1620 -659 C ATOM 3036 CE3 TRP B1007 137.934 -66.772 44.664 1.00157.35 C ANISOU 3036 CE3 TRP B1007 17676 22545 19563 -1669 1441 -852 C ATOM 3037 CZ2 TRP B1007 139.242 -69.058 45.733 1.00160.08 C ANISOU 3037 CZ2 TRP B1007 18509 22484 19831 -1890 1431 -712 C ATOM 3038 CZ3 TRP B1007 138.446 -67.767 43.840 1.00157.91 C ANISOU 3038 CZ3 TRP B1007 17619 22610 19770 -1814 1225 -930 C ATOM 3039 CH2 TRP B1007 139.065 -68.908 44.373 1.00158.91 C ANISOU 3039 CH2 TRP B1007 17983 22516 19880 -1928 1248 -867 C ATOM 3040 N GLU B1008 136.504 -61.599 46.322 1.00154.89 N ANISOU 3040 N GLU B1008 18074 22117 18661 -808 2281 -709 N ATOM 3041 CA GLU B1008 135.728 -60.554 45.646 1.00155.01 C ANISOU 3041 CA GLU B1008 17875 22242 18779 -498 2437 -660 C ATOM 3042 C GLU B1008 136.580 -59.915 44.557 1.00153.73 C ANISOU 3042 C GLU B1008 17741 22101 18568 -445 2128 -720 C ATOM 3043 O GLU B1008 136.072 -59.675 43.470 1.00153.80 O ANISOU 3043 O GLU B1008 17381 22326 18729 -248 2047 -675 O ATOM 3044 CB GLU B1008 135.226 -59.483 46.630 1.00159.40 C ANISOU 3044 CB GLU B1008 18830 22583 19151 -269 2904 -601 C ATOM 3045 CG GLU B1008 133.726 -59.519 46.878 1.00173.16 C ANISOU 3045 CG GLU B1008 20210 24462 21121 -42 3328 -463 C ATOM 3046 CD GLU B1008 132.859 -58.996 45.748 1.00192.53 C ANISOU 3046 CD GLU B1008 22112 27210 23831 291 3318 -367 C ATOM 3047 OE1 GLU B1008 132.535 -57.787 45.756 1.00187.66 O ANISOU 3047 OE1 GLU B1008 21684 26487 23133 664 3599 -279 O ATOM 3048 OE2 GLU B1008 132.484 -59.803 44.866 1.00184.77 O ANISOU 3048 OE2 GLU B1008 20532 26561 23112 192 3034 -380 O ATOM 3049 N THR B1009 137.888 -59.702 44.837 1.00145.98 N ANISOU 3049 N THR B1009 17171 20919 17375 -630 1944 -817 N ATOM 3050 CA THR B1009 138.876 -59.142 43.910 1.00142.80 C ANISOU 3050 CA THR B1009 16833 20485 16940 -648 1704 -881 C ATOM 3051 C THR B1009 139.107 -60.115 42.735 1.00142.06 C ANISOU 3051 C THR B1009 16310 20625 17040 -729 1372 -896 C ATOM 3052 O THR B1009 139.100 -59.678 41.582 1.00141.34 O ANISOU 3052 O THR B1009 16069 20635 16999 -572 1288 -877 O ATOM 3053 CB THR B1009 140.189 -58.818 44.651 1.00149.45 C ANISOU 3053 CB THR B1009 18132 21099 17555 -896 1588 -999 C ATOM 3054 OG1 THR B1009 139.893 -58.119 45.862 1.00150.40 O ANISOU 3054 OG1 THR B1009 18700 21004 17442 -870 1888 -1025 O ATOM 3055 CG2 THR B1009 141.159 -57.994 43.806 1.00147.39 C ANISOU 3055 CG2 THR B1009 17969 20747 17286 -933 1467 -1068 C ATOM 3056 N LEU B1010 139.285 -61.423 43.031 1.00135.65 N ANISOU 3056 N LEU B1010 15363 19869 16308 -951 1223 -923 N ATOM 3057 CA LEU B1010 139.508 -62.468 42.027 1.00133.08 C ANISOU 3057 CA LEU B1010 14713 19702 16150 -1059 960 -968 C ATOM 3058 C LEU B1010 138.282 -62.657 41.131 1.00136.89 C ANISOU 3058 C LEU B1010 14758 20449 16806 -933 970 -959 C ATOM 3059 O LEU B1010 138.440 -62.854 39.926 1.00135.69 O ANISOU 3059 O LEU B1010 14412 20446 16697 -911 752 -1013 O ATOM 3060 CB LEU B1010 139.890 -63.800 42.692 1.00132.64 C ANISOU 3060 CB LEU B1010 14692 19572 16135 -1292 891 -978 C ATOM 3061 CG LEU B1010 141.328 -63.901 43.192 1.00136.12 C ANISOU 3061 CG LEU B1010 15424 19866 16431 -1405 716 -986 C ATOM 3062 CD1 LEU B1010 141.414 -64.742 44.439 1.00137.40 C ANISOU 3062 CD1 LEU B1010 15788 19916 16500 -1506 776 -917 C ATOM 3063 CD2 LEU B1010 142.249 -64.462 42.123 1.00137.23 C ANISOU 3063 CD2 LEU B1010 15405 20052 16684 -1459 470 -1036 C ATOM 3064 N ASN B1011 137.070 -62.566 41.710 1.00135.01 N ANISOU 3064 N ASN B1011 14356 20290 16652 -843 1222 -893 N ATOM 3065 CA ASN B1011 135.813 -62.717 40.975 1.00136.68 C ANISOU 3065 CA ASN B1011 14052 20824 17057 -730 1212 -882 C ATOM 3066 C ASN B1011 135.438 -61.430 40.224 1.00139.89 C ANISOU 3066 C ASN B1011 14396 21374 17382 -333 1224 -786 C ATOM 3067 O ASN B1011 134.811 -61.520 39.165 1.00141.01 O ANISOU 3067 O ASN B1011 14134 21844 17599 -210 1027 -792 O ATOM 3068 CB ASN B1011 134.683 -63.156 41.907 1.00140.32 C ANISOU 3068 CB ASN B1011 14296 21325 17695 -793 1521 -831 C ATOM 3069 CG ASN B1011 134.830 -64.579 42.405 1.00162.11 C ANISOU 3069 CG ASN B1011 17053 23968 20573 -1170 1530 -907 C ATOM 3070 OD1 ASN B1011 135.044 -65.524 41.632 1.00154.06 O ANISOU 3070 OD1 ASN B1011 15848 23026 19662 -1391 1279 -1032 O ATOM 3071 ND2 ASN B1011 134.696 -64.768 43.711 1.00155.33 N ANISOU 3071 ND2 ASN B1011 16456 22890 19674 -1235 1859 -826 N ATOM 3072 N ASP B1012 135.825 -60.247 40.758 1.00134.71 N ANISOU 3072 N ASP B1012 14170 20465 16548 -132 1454 -702 N ATOM 3073 CA ASP B1012 135.570 -58.944 40.130 1.00135.37 C ANISOU 3073 CA ASP B1012 14327 20573 16533 281 1556 -578 C ATOM 3074 C ASP B1012 136.349 -58.835 38.823 1.00135.10 C ANISOU 3074 C ASP B1012 14330 20600 16402 309 1255 -611 C ATOM 3075 O ASP B1012 135.762 -58.508 37.789 1.00136.94 O ANISOU 3075 O ASP B1012 14314 21100 16618 612 1145 -522 O ATOM 3076 CB ASP B1012 135.949 -57.776 41.069 1.00137.88 C ANISOU 3076 CB ASP B1012 15214 20498 16676 397 1918 -531 C ATOM 3077 CG ASP B1012 134.798 -57.124 41.823 1.00154.57 C ANISOU 3077 CG ASP B1012 17316 22585 18828 712 2350 -395 C ATOM 3078 OD1 ASP B1012 133.961 -57.865 42.399 1.00157.05 O ANISOU 3078 OD1 ASP B1012 17305 23059 19308 636 2455 -380 O ATOM 3079 OD2 ASP B1012 134.772 -55.873 41.898 1.00162.91 O ANISOU 3079 OD2 ASP B1012 18733 23412 19756 1022 2645 -303 O ATOM 3080 N ASN B1013 137.662 -59.155 38.870 1.00125.98 N ANISOU 3080 N ASN B1013 13466 19225 15176 11 1122 -728 N ATOM 3081 CA ASN B1013 138.564 -59.101 37.725 1.00122.96 C ANISOU 3081 CA ASN B1013 13167 18841 14713 1 915 -764 C ATOM 3082 C ASN B1013 138.245 -60.185 36.693 1.00125.07 C ANISOU 3082 C ASN B1013 13045 19432 15045 -68 598 -842 C ATOM 3083 O ASN B1013 138.546 -59.989 35.516 1.00124.92 O ANISOU 3083 O ASN B1013 13050 19504 14910 68 459 -832 O ATOM 3084 CB ASN B1013 140.010 -59.184 38.176 1.00118.45 C ANISOU 3084 CB ASN B1013 12924 17977 14104 -300 891 -861 C ATOM 3085 CG ASN B1013 140.490 -57.883 38.758 1.00131.44 C ANISOU 3085 CG ASN B1013 15003 19307 15633 -248 1156 -829 C ATOM 3086 OD1 ASN B1013 140.826 -56.941 38.038 1.00124.88 O ANISOU 3086 OD1 ASN B1013 14372 18354 14724 -81 1268 -770 O ATOM 3087 ND2 ASN B1013 140.483 -57.779 40.073 1.00121.93 N ANISOU 3087 ND2 ASN B1013 14000 17939 14389 -389 1294 -873 N ATOM 3088 N LEU B1014 137.607 -61.300 37.116 1.00120.67 N ANISOU 3088 N LEU B1014 12171 19024 14652 -287 518 -929 N ATOM 3089 CA LEU B1014 137.187 -62.365 36.200 1.00121.11 C ANISOU 3089 CA LEU B1014 11872 19366 14778 -423 236 -1058 C ATOM 3090 C LEU B1014 136.147 -61.824 35.212 1.00126.94 C ANISOU 3090 C LEU B1014 12294 20492 15445 -89 100 -988 C ATOM 3091 O LEU B1014 136.222 -62.123 34.020 1.00127.77 O ANISOU 3091 O LEU B1014 12319 20803 15426 -64 -175 -1070 O ATOM 3092 CB LEU B1014 136.625 -63.572 36.967 1.00121.99 C ANISOU 3092 CB LEU B1014 11738 19500 15113 -752 267 -1160 C ATOM 3093 CG LEU B1014 137.602 -64.713 37.233 1.00124.89 C ANISOU 3093 CG LEU B1014 12303 19620 15530 -1093 218 -1279 C ATOM 3094 CD1 LEU B1014 137.112 -65.593 38.361 1.00126.01 C ANISOU 3094 CD1 LEU B1014 12367 19654 15855 -1342 400 -1291 C ATOM 3095 CD2 LEU B1014 137.829 -65.553 35.987 1.00128.43 C ANISOU 3095 CD2 LEU B1014 12652 20187 15960 -1226 -46 -1450 C ATOM 3096 N LYS B1015 135.213 -60.985 35.711 1.00124.24 N ANISOU 3096 N LYS B1015 11806 20249 15150 209 304 -822 N ATOM 3097 CA LYS B1015 134.161 -60.321 34.933 1.00127.25 C ANISOU 3097 CA LYS B1015 11855 21024 15470 638 205 -684 C ATOM 3098 C LYS B1015 134.788 -59.308 33.974 1.00128.49 C ANISOU 3098 C LYS B1015 12386 21103 15333 1004 179 -548 C ATOM 3099 O LYS B1015 134.347 -59.190 32.827 1.00131.06 O ANISOU 3099 O LYS B1015 12520 21785 15493 1267 -91 -502 O ATOM 3100 CB LYS B1015 133.145 -59.623 35.863 1.00132.51 C ANISOU 3100 CB LYS B1015 12336 21726 16286 915 542 -501 C ATOM 3101 CG LYS B1015 132.482 -60.546 36.885 1.00146.20 C ANISOU 3101 CG LYS B1015 13733 23499 18317 573 676 -599 C ATOM 3102 CD LYS B1015 131.392 -59.839 37.685 1.00158.16 C ANISOU 3102 CD LYS B1015 15024 25087 19984 902 1054 -403 C ATOM 3103 CE LYS B1015 131.008 -60.623 38.917 1.00165.52 C ANISOU 3103 CE LYS B1015 15838 25891 21162 553 1335 -473 C ATOM 3104 NZ LYS B1015 129.553 -60.565 39.192 1.00178.77 N ANISOU 3104 NZ LYS B1015 16885 27916 23125 742 1534 -360 N ATOM 3105 N VAL B1016 135.840 -58.599 34.453 1.00119.88 N ANISOU 3105 N VAL B1016 11844 19543 14163 994 460 -494 N ATOM 3106 CA VAL B1016 136.608 -57.592 33.715 1.00118.49 C ANISOU 3106 CA VAL B1016 12114 19155 13752 1261 564 -369 C ATOM 3107 C VAL B1016 137.266 -58.246 32.485 1.00120.32 C ANISOU 3107 C VAL B1016 12375 19511 13832 1136 256 -485 C ATOM 3108 O VAL B1016 137.186 -57.675 31.397 1.00122.67 O ANISOU 3108 O VAL B1016 12786 19937 13886 1494 192 -353 O ATOM 3109 CB VAL B1016 137.649 -56.877 34.627 1.00119.41 C ANISOU 3109 CB VAL B1016 12753 18736 13882 1107 918 -369 C ATOM 3110 CG1 VAL B1016 138.546 -55.927 33.833 1.00119.33 C ANISOU 3110 CG1 VAL B1016 13198 18460 13682 1278 1070 -271 C ATOM 3111 CG2 VAL B1016 136.965 -56.131 35.766 1.00120.85 C ANISOU 3111 CG2 VAL B1016 13016 18763 14136 1276 1264 -265 C ATOM 3112 N ILE B1017 137.871 -59.450 32.652 1.00112.48 N ANISOU 3112 N ILE B1017 11310 18470 12957 672 97 -713 N ATOM 3113 CA ILE B1017 138.543 -60.198 31.577 1.00110.80 C ANISOU 3113 CA ILE B1017 11164 18318 12617 525 -132 -853 C ATOM 3114 C ILE B1017 137.533 -60.533 30.455 1.00116.63 C ANISOU 3114 C ILE B1017 11590 19546 13176 714 -480 -889 C ATOM 3115 O ILE B1017 137.873 -60.386 29.279 1.00117.32 O ANISOU 3115 O ILE B1017 11882 19714 12981 890 -596 -873 O ATOM 3116 CB ILE B1017 139.288 -61.461 32.118 1.00110.80 C ANISOU 3116 CB ILE B1017 11144 18142 12813 40 -180 -1065 C ATOM 3117 CG1 ILE B1017 140.479 -61.048 33.012 1.00108.29 C ANISOU 3117 CG1 ILE B1017 11143 17407 12594 -105 79 -1021 C ATOM 3118 CG2 ILE B1017 139.787 -62.363 30.976 1.00111.83 C ANISOU 3118 CG2 ILE B1017 11323 18348 12820 -88 -387 -1230 C ATOM 3119 CD1 ILE B1017 140.897 -62.060 34.072 1.00113.81 C ANISOU 3119 CD1 ILE B1017 11779 17959 13503 -473 72 -1137 C ATOM 3120 N GLU B1018 136.297 -60.923 30.818 1.00114.56 N ANISOU 3120 N GLU B1018 10839 19624 13064 685 -634 -931 N ATOM 3121 CA GLU B1018 135.242 -61.257 29.858 1.00118.66 C ANISOU 3121 CA GLU B1018 10951 20689 13444 813 -1029 -996 C ATOM 3122 C GLU B1018 134.754 -60.035 29.063 1.00124.43 C ANISOU 3122 C GLU B1018 11733 21669 13874 1443 -1075 -715 C ATOM 3123 O GLU B1018 134.447 -60.173 27.877 1.00127.21 O ANISOU 3123 O GLU B1018 12017 22398 13921 1612 -1431 -752 O ATOM 3124 CB GLU B1018 134.055 -61.920 30.567 1.00122.44 C ANISOU 3124 CB GLU B1018 10824 21459 14238 587 -1123 -1102 C ATOM 3125 CG GLU B1018 134.148 -63.433 30.610 1.00133.68 C ANISOU 3125 CG GLU B1018 12095 22869 15826 -6 -1289 -1441 C ATOM 3126 CD GLU B1018 134.987 -63.986 31.743 1.00148.62 C ANISOU 3126 CD GLU B1018 14256 24253 17960 -364 -969 -1494 C ATOM 3127 OE1 GLU B1018 134.419 -64.239 32.829 1.00146.27 O ANISOU 3127 OE1 GLU B1018 13718 23910 17949 -528 -781 -1479 O ATOM 3128 OE2 GLU B1018 136.211 -64.164 31.547 1.00134.48 O ANISOU 3128 OE2 GLU B1018 12908 22126 16063 -455 -897 -1534 O ATOM 3129 N LYS B1019 134.686 -58.854 29.708 1.00119.85 N ANISOU 3129 N LYS B1019 11324 20866 13348 1803 -708 -436 N ATOM 3130 CA LYS B1019 134.225 -57.613 29.078 1.00123.43 C ANISOU 3130 CA LYS B1019 11893 21466 13539 2472 -649 -110 C ATOM 3131 C LYS B1019 135.384 -56.797 28.450 1.00125.25 C ANISOU 3131 C LYS B1019 12829 21278 13483 2675 -394 34 C ATOM 3132 O LYS B1019 135.131 -55.766 27.819 1.00128.20 O ANISOU 3132 O LYS B1019 13423 21698 13590 3250 -296 328 O ATOM 3133 CB LYS B1019 133.440 -56.754 30.092 1.00127.55 C ANISOU 3133 CB LYS B1019 12255 21928 14281 2792 -310 122 C ATOM 3134 CG LYS B1019 132.015 -57.251 30.371 1.00144.70 C ANISOU 3134 CG LYS B1019 13644 24653 16681 2824 -547 96 C ATOM 3135 CD LYS B1019 131.005 -56.744 29.336 1.00163.31 C ANISOU 3135 CD LYS B1019 15642 27608 18798 3441 -867 324 C ATOM 3136 CE LYS B1019 129.637 -57.363 29.497 1.00182.50 C ANISOU 3136 CE LYS B1019 17175 30675 21491 3388 -1177 250 C ATOM 3137 NZ LYS B1019 128.719 -56.958 28.397 1.00199.53 N ANISOU 3137 NZ LYS B1019 18927 33510 23376 3973 -1608 451 N ATOM 3138 N ALA B1020 136.638 -57.272 28.595 1.00117.17 N ANISOU 3138 N ALA B1020 12140 19856 12525 2224 -269 -154 N ATOM 3139 CA ALA B1020 137.827 -56.615 28.038 1.00115.64 C ANISOU 3139 CA ALA B1020 12550 19252 12137 2311 14 -54 C ATOM 3140 C ALA B1020 137.930 -56.833 26.529 1.00122.02 C ANISOU 3140 C ALA B1020 13510 20317 12534 2522 -242 -44 C ATOM 3141 O ALA B1020 137.553 -57.897 26.031 1.00122.57 O ANISOU 3141 O ALA B1020 13278 20768 12525 2327 -663 -267 O ATOM 3142 CB ALA B1020 139.083 -57.131 28.719 1.00111.29 C ANISOU 3142 CB ALA B1020 12176 18276 11832 1764 196 -258 C ATOM 3143 N ASP B1021 138.457 -55.825 25.810 1.00119.99 N ANISOU 3143 N ASP B1021 13775 19816 11998 2900 46 204 N ATOM 3144 CA ASP B1021 138.627 -55.863 24.355 1.00122.81 C ANISOU 3144 CA ASP B1021 14420 20359 11885 3176 -109 267 C ATOM 3145 C ASP B1021 140.108 -55.910 23.950 1.00123.10 C ANISOU 3145 C ASP B1021 14956 19925 11892 2925 235 206 C ATOM 3146 O ASP B1021 140.423 -56.433 22.878 1.00124.50 O ANISOU 3146 O ASP B1021 15321 20236 11746 2943 86 123 O ATOM 3147 CB ASP B1021 137.930 -54.659 23.698 1.00130.33 C ANISOU 3147 CB ASP B1021 15598 21451 12470 3926 -31 668 C ATOM 3148 CG ASP B1021 136.410 -54.733 23.734 1.00144.74 C ANISOU 3148 CG ASP B1021 16846 23906 14242 4268 -474 745 C ATOM 3149 OD1 ASP B1021 135.830 -54.550 24.830 1.00144.00 O ANISOU 3149 OD1 ASP B1021 16398 23796 14520 4225 -374 767 O ATOM 3150 OD2 ASP B1021 135.800 -54.949 22.662 1.00155.42 O ANISOU 3150 OD2 ASP B1021 18098 25784 15169 4589 -914 787 O ATOM 3151 N ASN B1022 141.007 -55.370 24.800 1.00115.48 N ANISOU 3151 N ASN B1022 14192 18426 11258 2683 697 233 N ATOM 3152 CA ASN B1022 142.456 -55.350 24.557 1.00113.16 C ANISOU 3152 CA ASN B1022 14263 17691 11043 2405 1064 181 C ATOM 3153 C ASN B1022 143.212 -56.244 25.559 1.00110.94 C ANISOU 3153 C ASN B1022 13692 17254 11208 1789 1036 -106 C ATOM 3154 O ASN B1022 142.716 -56.495 26.658 1.00108.09 O ANISOU 3154 O ASN B1022 12992 16968 11109 1599 888 -202 O ATOM 3155 CB ASN B1022 143.015 -53.917 24.578 1.00116.77 C ANISOU 3155 CB ASN B1022 15218 17650 11498 2612 1643 451 C ATOM 3156 CG ASN B1022 142.558 -53.060 25.733 1.00149.22 C ANISOU 3156 CG ASN B1022 19289 21559 15850 2651 1835 542 C ATOM 3157 OD1 ASN B1022 141.386 -52.679 25.836 1.00148.32 O ANISOU 3157 OD1 ASN B1022 19053 21693 15610 3065 1697 702 O ATOM 3158 ND2 ASN B1022 143.491 -52.676 26.591 1.00141.45 N ANISOU 3158 ND2 ASN B1022 18431 20115 15199 2243 2183 447 N ATOM 3159 N ALA B1023 144.410 -56.730 25.161 1.00105.86 N ANISOU 3159 N ALA B1023 13189 16402 10632 1523 1199 -216 N ATOM 3160 CA ALA B1023 145.270 -57.600 25.974 1.00101.60 C ANISOU 3160 CA ALA B1023 12393 15726 10485 1018 1183 -441 C ATOM 3161 C ALA B1023 145.877 -56.852 27.166 1.00102.77 C ANISOU 3161 C ALA B1023 12536 15530 10982 769 1457 -414 C ATOM 3162 O ALA B1023 146.215 -57.484 28.168 1.00 99.12 O ANISOU 3162 O ALA B1023 11791 15051 10818 412 1332 -573 O ATOM 3163 CB ALA B1023 146.374 -58.198 25.118 1.00102.76 C ANISOU 3163 CB ALA B1023 12697 15749 10599 903 1343 -516 C ATOM 3164 N ALA B1024 146.010 -55.511 27.057 1.00101.36 N ANISOU 3164 N ALA B1024 12710 15065 10735 959 1834 -216 N ATOM 3165 CA ALA B1024 146.515 -54.643 28.123 1.00100.44 C ANISOU 3165 CA ALA B1024 12678 14592 10894 709 2117 -221 C ATOM 3166 C ALA B1024 145.507 -54.587 29.283 1.00101.72 C ANISOU 3166 C ALA B1024 12644 14879 11126 714 1911 -262 C ATOM 3167 O ALA B1024 145.911 -54.497 30.443 1.00 99.35 O ANISOU 3167 O ALA B1024 12265 14414 11071 367 1945 -389 O ATOM 3168 CB ALA B1024 146.784 -53.249 27.578 1.00104.89 C ANISOU 3168 CB ALA B1024 13745 14776 11332 934 2623 -2 C ATOM 3169 N GLN B1025 144.198 -54.663 28.954 1.00 98.78 N ANISOU 3169 N GLN B1025 12177 14827 10527 1113 1694 -157 N ATOM 3170 CA GLN B1025 143.081 -54.698 29.900 1.00 97.65 C ANISOU 3170 CA GLN B1025 11790 14864 10447 1188 1525 -168 C ATOM 3171 C GLN B1025 143.066 -56.032 30.647 1.00 97.88 C ANISOU 3171 C GLN B1025 11394 15109 10685 801 1181 -404 C ATOM 3172 O GLN B1025 142.812 -56.061 31.852 1.00 96.22 O ANISOU 3172 O GLN B1025 11070 14846 10643 624 1179 -473 O ATOM 3173 CB GLN B1025 141.749 -54.507 29.157 1.00101.94 C ANISOU 3173 CB GLN B1025 12247 15769 10715 1731 1360 20 C ATOM 3174 CG GLN B1025 141.078 -53.163 29.380 1.00118.14 C ANISOU 3174 CG GLN B1025 14566 17645 12678 2173 1683 276 C ATOM 3175 CD GLN B1025 139.620 -53.228 29.004 1.00140.63 C ANISOU 3175 CD GLN B1025 17101 20977 15354 2667 1411 433 C ATOM 3176 OE1 GLN B1025 139.254 -53.214 27.825 1.00136.67 O ANISOU 3176 OE1 GLN B1025 16624 20762 14544 3052 1236 578 O ATOM 3177 NE2 GLN B1025 138.753 -53.314 30.003 1.00137.23 N ANISOU 3177 NE2 GLN B1025 16352 20677 15111 2668 1364 407 N ATOM 3178 N VAL B1026 143.335 -57.134 29.917 1.00 93.38 N ANISOU 3178 N VAL B1026 10654 14749 10078 689 932 -520 N ATOM 3179 CA VAL B1026 143.357 -58.513 30.415 1.00 90.82 C ANISOU 3179 CA VAL B1026 9991 14588 9930 357 647 -727 C ATOM 3180 C VAL B1026 144.567 -58.725 31.344 1.00 92.23 C ANISOU 3180 C VAL B1026 10184 14487 10371 -32 759 -824 C ATOM 3181 O VAL B1026 144.393 -59.276 32.431 1.00 90.29 O ANISOU 3181 O VAL B1026 9753 14268 10286 -247 640 -911 O ATOM 3182 CB VAL B1026 143.340 -59.536 29.247 1.00 95.69 C ANISOU 3182 CB VAL B1026 10530 15438 10391 375 415 -832 C ATOM 3183 CG1 VAL B1026 143.448 -60.970 29.753 1.00 93.57 C ANISOU 3183 CG1 VAL B1026 9992 15237 10322 24 205 -1043 C ATOM 3184 CG2 VAL B1026 142.090 -59.371 28.388 1.00 98.89 C ANISOU 3184 CG2 VAL B1026 10862 16210 10502 735 200 -763 C ATOM 3185 N LYS B1027 145.776 -58.283 30.926 1.00 88.93 N ANISOU 3185 N LYS B1027 9972 13823 9994 -114 990 -797 N ATOM 3186 CA LYS B1027 147.009 -58.412 31.716 1.00 87.27 C ANISOU 3186 CA LYS B1027 9705 13411 10042 -474 1062 -883 C ATOM 3187 C LYS B1027 146.897 -57.648 33.045 1.00 91.21 C ANISOU 3187 C LYS B1027 10273 13759 10623 -625 1128 -899 C ATOM 3188 O LYS B1027 147.408 -58.122 34.057 1.00 89.67 O ANISOU 3188 O LYS B1027 9930 13555 10584 -908 996 -1000 O ATOM 3189 CB LYS B1027 148.228 -57.922 30.920 1.00 90.85 C ANISOU 3189 CB LYS B1027 10322 13648 10548 -522 1352 -838 C ATOM 3190 CG LYS B1027 149.548 -58.454 31.461 1.00101.67 C ANISOU 3190 CG LYS B1027 11469 14946 12216 -868 1336 -935 C ATOM 3191 CD LYS B1027 150.747 -57.650 30.995 1.00112.20 C ANISOU 3191 CD LYS B1027 12912 16031 13689 -998 1692 -894 C ATOM 3192 CE LYS B1027 151.913 -57.865 31.928 1.00121.70 C ANISOU 3192 CE LYS B1027 13817 17209 15216 -1380 1619 -996 C ATOM 3193 NZ LYS B1027 153.171 -57.288 31.389 1.00133.80 N ANISOU 3193 NZ LYS B1027 15326 18549 16964 -1554 1966 -974 N ATOM 3194 N ASP B1028 146.208 -56.487 33.033 1.00 89.57 N ANISOU 3194 N ASP B1028 10326 13430 10276 -401 1338 -793 N ATOM 3195 CA ASP B1028 145.984 -55.622 34.194 1.00 90.17 C ANISOU 3195 CA ASP B1028 10583 13306 10371 -495 1482 -816 C ATOM 3196 C ASP B1028 145.114 -56.311 35.259 1.00 91.63 C ANISOU 3196 C ASP B1028 10565 13685 10567 -529 1257 -875 C ATOM 3197 O ASP B1028 145.417 -56.208 36.450 1.00 90.96 O ANISOU 3197 O ASP B1028 10545 13483 10533 -785 1251 -977 O ATOM 3198 CB ASP B1028 145.335 -54.303 33.752 1.00 95.15 C ANISOU 3198 CB ASP B1028 11574 13742 10835 -141 1818 -649 C ATOM 3199 CG ASP B1028 145.836 -53.103 34.522 1.00109.99 C ANISOU 3199 CG ASP B1028 13830 15202 12760 -342 2152 -703 C ATOM 3200 OD1 ASP B1028 146.824 -52.483 34.073 1.00112.42 O ANISOU 3200 OD1 ASP B1028 14346 15234 13136 -512 2402 -715 O ATOM 3201 OD2 ASP B1028 145.248 -52.790 35.581 1.00117.23 O ANISOU 3201 OD2 ASP B1028 14849 16048 13645 -356 2192 -752 O ATOM 3202 N ALA B1029 144.045 -57.010 34.827 1.00 86.87 N ANISOU 3202 N ALA B1029 9724 13380 9903 -292 1082 -821 N ATOM 3203 CA ALA B1029 143.137 -57.742 35.709 1.00 85.26 C ANISOU 3203 CA ALA B1029 9291 13361 9745 -329 928 -863 C ATOM 3204 C ALA B1029 143.807 -58.997 36.278 1.00 86.34 C ANISOU 3204 C ALA B1029 9242 13548 10016 -664 704 -990 C ATOM 3205 O ALA B1029 143.599 -59.307 37.451 1.00 85.77 O ANISOU 3205 O ALA B1029 9157 13456 9976 -807 678 -1030 O ATOM 3206 CB ALA B1029 141.871 -58.121 34.960 1.00 86.99 C ANISOU 3206 CB ALA B1029 9248 13904 9899 -35 800 -791 C ATOM 3207 N LEU B1030 144.607 -59.712 35.450 1.00 81.18 N ANISOU 3207 N LEU B1030 8485 12941 9420 -748 582 -1033 N ATOM 3208 CA LEU B1030 145.331 -60.924 35.837 1.00 79.56 C ANISOU 3208 CA LEU B1030 8121 12757 9350 -987 409 -1115 C ATOM 3209 C LEU B1030 146.440 -60.618 36.852 1.00 84.73 C ANISOU 3209 C LEU B1030 8866 13250 10078 -1223 418 -1144 C ATOM 3210 O LEU B1030 146.743 -61.479 37.678 1.00 84.55 O ANISOU 3210 O LEU B1030 8747 13262 10118 -1367 268 -1169 O ATOM 3211 CB LEU B1030 145.934 -61.637 34.611 1.00 79.33 C ANISOU 3211 CB LEU B1030 8010 12778 9354 -960 356 -1143 C ATOM 3212 CG LEU B1030 144.975 -62.348 33.641 1.00 84.42 C ANISOU 3212 CG LEU B1030 8544 13628 9903 -821 240 -1186 C ATOM 3213 CD1 LEU B1030 145.680 -62.684 32.353 1.00 84.91 C ANISOU 3213 CD1 LEU B1030 8674 13677 9911 -761 267 -1217 C ATOM 3214 CD2 LEU B1030 144.410 -63.623 34.240 1.00 86.40 C ANISOU 3214 CD2 LEU B1030 8609 13963 10257 -975 93 -1271 C ATOM 3215 N THR B1031 147.055 -59.408 36.782 1.00 82.48 N ANISOU 3215 N THR B1031 8773 12790 9774 -1271 589 -1144 N ATOM 3216 CA THR B1031 148.107 -58.953 37.705 1.00 83.38 C ANISOU 3216 CA THR B1031 8957 12777 9947 -1557 568 -1221 C ATOM 3217 C THR B1031 147.481 -58.704 39.089 1.00 87.90 C ANISOU 3217 C THR B1031 9702 13316 10382 -1626 538 -1263 C ATOM 3218 O THR B1031 148.075 -59.083 40.105 1.00 88.47 O ANISOU 3218 O THR B1031 9746 13425 10443 -1834 351 -1323 O ATOM 3219 CB THR B1031 148.830 -57.711 37.141 1.00 94.05 C ANISOU 3219 CB THR B1031 10487 13911 11336 -1638 819 -1237 C ATOM 3220 OG1 THR B1031 149.418 -58.058 35.886 1.00 96.75 O ANISOU 3220 OG1 THR B1031 10689 14286 11787 -1557 885 -1182 O ATOM 3221 CG2 THR B1031 149.926 -57.182 38.067 1.00 93.21 C ANISOU 3221 CG2 THR B1031 10412 13696 11307 -2017 772 -1370 C ATOM 3222 N LYS B1032 146.269 -58.098 39.119 1.00 84.10 N ANISOU 3222 N LYS B1032 9397 12784 9775 -1411 729 -1214 N ATOM 3223 CA LYS B1032 145.507 -57.821 40.346 1.00 84.42 C ANISOU 3223 CA LYS B1032 9638 12766 9672 -1411 802 -1236 C ATOM 3224 C LYS B1032 145.041 -59.136 40.986 1.00 86.60 C ANISOU 3224 C LYS B1032 9717 13228 9958 -1422 617 -1208 C ATOM 3225 O LYS B1032 144.917 -59.214 42.209 1.00 87.22 O ANISOU 3225 O LYS B1032 9965 13265 9909 -1522 608 -1240 O ATOM 3226 CB LYS B1032 144.299 -56.900 40.070 1.00 87.55 C ANISOU 3226 CB LYS B1032 10205 13078 9982 -1097 1104 -1146 C ATOM 3227 CG LYS B1032 144.670 -55.481 39.646 1.00 94.98 C ANISOU 3227 CG LYS B1032 11480 13732 10877 -1060 1387 -1151 C ATOM 3228 CD LYS B1032 143.471 -54.548 39.698 1.00101.57 C ANISOU 3228 CD LYS B1032 12549 14442 11602 -703 1723 -1038 C ATOM 3229 CE LYS B1032 143.655 -53.324 38.835 1.00109.18 C ANISOU 3229 CE LYS B1032 13808 15140 12536 -523 2034 -956 C ATOM 3230 NZ LYS B1032 143.282 -53.584 37.419 1.00114.22 N ANISOU 3230 NZ LYS B1032 14206 15997 13194 -186 1971 -780 N ATOM 3231 N MET B1033 144.810 -60.167 40.153 1.00 81.03 N ANISOU 3231 N MET B1033 8709 12697 9381 -1333 498 -1158 N ATOM 3232 CA MET B1033 144.390 -61.492 40.594 1.00 80.10 C ANISOU 3232 CA MET B1033 8421 12697 9314 -1368 379 -1134 C ATOM 3233 C MET B1033 145.542 -62.240 41.236 1.00 83.75 C ANISOU 3233 C MET B1033 8883 13145 9795 -1551 178 -1146 C ATOM 3234 O MET B1033 145.354 -62.802 42.315 1.00 82.98 O ANISOU 3234 O MET B1033 8875 13041 9613 -1603 145 -1113 O ATOM 3235 CB MET B1033 143.833 -62.306 39.423 1.00 81.68 C ANISOU 3235 CB MET B1033 8346 13051 9637 -1264 325 -1125 C ATOM 3236 CG MET B1033 142.418 -61.957 39.077 1.00 86.74 C ANISOU 3236 CG MET B1033 8879 13816 10263 -1074 446 -1092 C ATOM 3237 SD MET B1033 141.868 -62.853 37.616 1.00 91.82 S ANISOU 3237 SD MET B1033 9206 14692 10992 -1013 290 -1143 S ATOM 3238 CE MET B1033 141.377 -64.413 38.362 1.00 88.80 C ANISOU 3238 CE MET B1033 8662 14324 10755 -1241 255 -1196 C ATOM 3239 N ARG B1034 146.730 -62.254 40.569 1.00 81.06 N ANISOU 3239 N ARG B1034 8433 12808 9559 -1615 66 -1169 N ATOM 3240 CA ARG B1034 147.937 -62.950 41.036 1.00 81.79 C ANISOU 3240 CA ARG B1034 8428 12939 9710 -1729 -143 -1149 C ATOM 3241 C ARG B1034 148.340 -62.469 42.420 1.00 89.09 C ANISOU 3241 C ARG B1034 9547 13851 10452 -1879 -260 -1182 C ATOM 3242 O ARG B1034 148.660 -63.297 43.270 1.00 89.97 O ANISOU 3242 O ARG B1034 9659 14029 10496 -1887 -433 -1114 O ATOM 3243 CB ARG B1034 149.116 -62.797 40.062 1.00 81.46 C ANISOU 3243 CB ARG B1034 8200 12907 9843 -1764 -171 -1166 C ATOM 3244 CG ARG B1034 150.140 -63.915 40.232 1.00 89.76 C ANISOU 3244 CG ARG B1034 9036 14041 11028 -1758 -352 -1094 C ATOM 3245 CD ARG B1034 151.515 -63.564 39.705 1.00 96.63 C ANISOU 3245 CD ARG B1034 9683 14947 12083 -1839 -381 -1107 C ATOM 3246 NE ARG B1034 152.298 -64.774 39.436 1.00105.71 N ANISOU 3246 NE ARG B1034 10590 16163 13412 -1709 -454 -1001 N ATOM 3247 CZ ARG B1034 153.174 -65.321 40.277 1.00119.76 C ANISOU 3247 CZ ARG B1034 12198 18070 15235 -1699 -684 -911 C ATOM 3248 NH1 ARG B1034 153.407 -64.769 41.460 1.00105.36 N ANISOU 3248 NH1 ARG B1034 10427 16353 13252 -1859 -915 -944 N ATOM 3249 NH2 ARG B1034 153.827 -66.425 39.935 1.00106.48 N ANISOU 3249 NH2 ARG B1034 10314 16412 13731 -1505 -683 -783 N ATOM 3250 N ALA B1035 148.289 -61.144 42.655 1.00 87.81 N ANISOU 3250 N ALA B1035 9603 13586 10176 -1985 -151 -1285 N ATOM 3251 CA ALA B1035 148.604 -60.540 43.946 1.00 90.95 C ANISOU 3251 CA ALA B1035 10270 13947 10340 -2170 -249 -1379 C ATOM 3252 C ALA B1035 147.605 -60.993 45.011 1.00 97.56 C ANISOU 3252 C ALA B1035 11348 14772 10950 -2070 -187 -1318 C ATOM 3253 O ALA B1035 148.030 -61.421 46.081 1.00 98.74 O ANISOU 3253 O ALA B1035 11618 14996 10905 -2143 -395 -1305 O ATOM 3254 CB ALA B1035 148.603 -59.025 43.830 1.00 92.99 C ANISOU 3254 CB ALA B1035 10783 14011 10537 -2301 -43 -1522 C ATOM 3255 N ALA B1036 146.289 -60.947 44.692 1.00 95.19 N ANISOU 3255 N ALA B1036 11090 14403 10677 -1885 99 -1262 N ATOM 3256 CA ALA B1036 145.186 -61.343 45.575 1.00 96.76 C ANISOU 3256 CA ALA B1036 11466 14572 10727 -1782 270 -1191 C ATOM 3257 C ALA B1036 145.232 -62.839 45.922 1.00101.63 C ANISOU 3257 C ALA B1036 11955 15279 11381 -1752 140 -1064 C ATOM 3258 O ALA B1036 144.927 -63.202 47.054 1.00103.37 O ANISOU 3258 O ALA B1036 12427 15462 11386 -1744 191 -1003 O ATOM 3259 CB ALA B1036 143.851 -61.000 44.933 1.00 96.91 C ANISOU 3259 CB ALA B1036 11396 14564 10864 -1586 582 -1150 C ATOM 3260 N ALA B1037 145.616 -63.698 44.950 1.00 96.84 N ANISOU 3260 N ALA B1037 11020 14750 11025 -1720 20 -1017 N ATOM 3261 CA ALA B1037 145.738 -65.149 45.125 1.00 97.03 C ANISOU 3261 CA ALA B1037 10954 14790 11123 -1677 -52 -895 C ATOM 3262 C ALA B1037 146.899 -65.493 46.068 1.00103.84 C ANISOU 3262 C ALA B1037 11941 15705 11806 -1699 -325 -823 C ATOM 3263 O ALA B1037 146.764 -66.398 46.893 1.00105.17 O ANISOU 3263 O ALA B1037 12269 15837 11852 -1625 -315 -683 O ATOM 3264 CB ALA B1037 145.930 -65.829 43.775 1.00 95.96 C ANISOU 3264 CB ALA B1037 10503 14684 11273 -1638 -80 -903 C ATOM 3265 N LEU B1038 148.022 -64.752 45.965 1.00101.60 N ANISOU 3265 N LEU B1038 11582 15518 11504 -1800 -563 -910 N ATOM 3266 CA LEU B1038 149.196 -64.930 46.825 1.00104.61 C ANISOU 3266 CA LEU B1038 11989 16041 11717 -1837 -905 -865 C ATOM 3267 C LEU B1038 148.905 -64.428 48.239 1.00113.96 C ANISOU 3267 C LEU B1038 13606 17217 12478 -1907 -947 -903 C ATOM 3268 O LEU B1038 149.393 -65.003 49.209 1.00116.39 O ANISOU 3268 O LEU B1038 14053 17631 12537 -1841 -1180 -789 O ATOM 3269 CB LEU B1038 150.415 -64.191 46.249 1.00104.78 C ANISOU 3269 CB LEU B1038 11735 16185 11893 -1994 -1119 -986 C ATOM 3270 CG LEU B1038 151.107 -64.826 45.048 1.00107.31 C ANISOU 3270 CG LEU B1038 11643 16553 12579 -1896 -1128 -915 C ATOM 3271 CD1 LEU B1038 151.823 -63.781 44.235 1.00106.86 C ANISOU 3271 CD1 LEU B1038 11381 16515 12707 -2080 -1119 -1065 C ATOM 3272 CD2 LEU B1038 152.081 -65.907 45.479 1.00112.21 C ANISOU 3272 CD2 LEU B1038 12075 17334 13228 -1738 -1396 -732 C ATOM 3273 N ASP B1039 148.103 -63.352 48.341 1.00112.55 N ANISOU 3273 N ASP B1039 13672 16901 12190 -2003 -701 -1052 N ATOM 3274 CA ASP B1039 147.699 -62.708 49.591 1.00116.43 C ANISOU 3274 CA ASP B1039 14655 17321 12265 -2072 -635 -1130 C ATOM 3275 C ASP B1039 146.646 -63.545 50.321 1.00122.82 C ANISOU 3275 C ASP B1039 15716 18034 12916 -1887 -372 -953 C ATOM 3276 O ASP B1039 146.580 -63.485 51.550 1.00125.73 O ANISOU 3276 O ASP B1039 16517 18385 12867 -1885 -391 -940 O ATOM 3277 CB ASP B1039 147.174 -61.290 49.298 1.00118.36 C ANISOU 3277 CB ASP B1039 15076 17390 12507 -2183 -363 -1328 C ATOM 3278 CG ASP B1039 146.864 -60.401 50.483 1.00136.00 C ANISOU 3278 CG ASP B1039 17875 19490 14308 -2284 -246 -1471 C ATOM 3279 OD1 ASP B1039 147.440 -60.631 51.571 1.00140.77 O ANISOU 3279 OD1 ASP B1039 18740 20203 14543 -2368 -528 -1494 O ATOM 3280 OD2 ASP B1039 146.101 -59.426 50.307 1.00142.58 O ANISOU 3280 OD2 ASP B1039 18916 20112 15145 -2264 120 -1567 O ATOM 3281 N ALA B1040 145.835 -64.321 49.574 1.00118.51 N ANISOU 3281 N ALA B1040 14919 17422 12688 -1757 -117 -832 N ATOM 3282 CA ALA B1040 144.790 -65.184 50.135 1.00120.10 C ANISOU 3282 CA ALA B1040 15284 17507 12842 -1635 201 -670 C ATOM 3283 C ALA B1040 145.370 -66.514 50.619 1.00127.94 C ANISOU 3283 C ALA B1040 16329 18525 13759 -1530 36 -461 C ATOM 3284 O ALA B1040 144.833 -67.122 51.553 1.00129.72 O ANISOU 3284 O ALA B1040 16883 18637 13767 -1440 250 -306 O ATOM 3285 CB ALA B1040 143.711 -65.438 49.098 1.00118.30 C ANISOU 3285 CB ALA B1040 14718 17224 13008 -1603 507 -669 C ATOM 3286 N GLN B1041 146.471 -66.951 49.972 1.00125.59 N ANISOU 3286 N GLN B1041 15723 18353 13642 -1510 -297 -433 N ATOM 3287 CA GLN B1041 147.223 -68.184 50.221 1.00128.21 C ANISOU 3287 CA GLN B1041 16037 18717 13962 -1342 -478 -213 C ATOM 3288 C GLN B1041 147.746 -68.280 51.672 1.00139.87 C ANISOU 3288 C GLN B1041 17926 20287 14932 -1236 -705 -78 C ATOM 3289 O GLN B1041 147.866 -69.386 52.203 1.00142.37 O ANISOU 3289 O GLN B1041 18420 20540 15135 -1022 -679 180 O ATOM 3290 CB GLN B1041 148.406 -68.250 49.236 1.00128.14 C ANISOU 3290 CB GLN B1041 15587 18863 14236 -1334 -788 -248 C ATOM 3291 CG GLN B1041 148.998 -69.639 49.014 1.00142.02 C ANISOU 3291 CG GLN B1041 17221 20585 16156 -1106 -835 -17 C ATOM 3292 CD GLN B1041 150.134 -69.635 48.014 1.00158.04 C ANISOU 3292 CD GLN B1041 18804 22759 18485 -1077 -1064 -54 C ATOM 3293 OE1 GLN B1041 151.067 -68.821 48.076 1.00152.90 O ANISOU 3293 OE1 GLN B1041 17964 22345 17787 -1166 -1388 -147 O ATOM 3294 NE2 GLN B1041 150.106 -70.583 47.092 1.00149.36 N ANISOU 3294 NE2 GLN B1041 17541 21506 17702 -965 -873 13 N ATOM 3295 N LYS B1042 148.038 -67.127 52.304 1.00139.99 N ANISOU 3295 N LYS B1042 18142 20433 14616 -1383 -914 -256 N ATOM 3296 CA LYS B1042 148.608 -67.023 53.652 1.00145.76 C ANISOU 3296 CA LYS B1042 19280 21316 14785 -1331 -1223 -200 C ATOM 3297 C LYS B1042 147.534 -66.886 54.746 1.00154.59 C ANISOU 3297 C LYS B1042 21017 22238 15481 -1295 -853 -164 C ATOM 3298 O LYS B1042 147.807 -67.209 55.904 1.00158.55 O ANISOU 3298 O LYS B1042 21958 22811 15474 -1158 -1010 -22 O ATOM 3299 CB LYS B1042 149.593 -65.839 53.713 1.00149.80 C ANISOU 3299 CB LYS B1042 19680 22075 15163 -1584 -1671 -473 C ATOM 3300 CG LYS B1042 150.884 -66.091 52.927 1.00164.46 C ANISOU 3300 CG LYS B1042 20942 24186 17359 -1585 -2081 -452 C ATOM 3301 CD LYS B1042 151.553 -64.798 52.439 1.00174.38 C ANISOU 3301 CD LYS B1042 21940 25564 18750 -1938 -2294 -778 C ATOM 3302 CE LYS B1042 152.619 -65.027 51.389 1.00182.82 C ANISOU 3302 CE LYS B1042 22360 26814 20292 -1945 -2511 -753 C ATOM 3303 NZ LYS B1042 152.675 -63.926 50.390 1.00188.15 N ANISOU 3303 NZ LYS B1042 22808 27389 21291 -2239 -2353 -1017 N ATOM 3304 N ALA B1043 146.320 -66.437 54.375 1.00150.87 N ANISOU 3304 N ALA B1043 20574 21538 15212 -1382 -352 -268 N ATOM 3305 CA ALA B1043 145.187 -66.237 55.285 1.00153.83 C ANISOU 3305 CA ALA B1043 21462 21703 15281 -1341 117 -238 C ATOM 3306 C ALA B1043 144.477 -67.549 55.650 1.00161.28 C ANISOU 3306 C ALA B1043 22561 22458 16261 -1149 504 67 C ATOM 3307 O ALA B1043 144.518 -68.511 54.880 1.00158.99 O ANISOU 3307 O ALA B1043 21903 22125 16381 -1097 536 197 O ATOM 3308 CB ALA B1043 144.186 -65.283 54.656 1.00151.82 C ANISOU 3308 CB ALA B1043 21067 21310 15307 -1458 513 -433 C ATOM 3309 N THR B1044 143.827 -67.574 56.836 1.00163.19 N ANISOU 3309 N THR B1044 23398 22549 16059 -1059 843 172 N ATOM 3310 CA THR B1044 143.050 -68.709 57.347 1.00165.91 C ANISOU 3310 CA THR B1044 23996 22649 16391 -905 1332 465 C ATOM 3311 C THR B1044 141.557 -68.353 57.258 1.00171.40 C ANISOU 3311 C THR B1044 24659 23128 17335 -994 2012 401 C ATOM 3312 O THR B1044 141.165 -67.304 57.774 1.00172.24 O ANISOU 3312 O THR B1044 25064 23214 17166 -1023 2177 249 O ATOM 3313 CB THR B1044 143.474 -69.095 58.772 1.00177.91 C ANISOU 3313 CB THR B1044 26231 24167 17199 -691 1243 685 C ATOM 3314 OG1 THR B1044 143.290 -67.979 59.646 1.00179.10 O ANISOU 3314 OG1 THR B1044 26886 24342 16823 -748 1281 501 O ATOM 3315 CG2 THR B1044 144.912 -69.601 58.840 1.00177.68 C ANISOU 3315 CG2 THR B1044 26135 24403 16972 -537 562 811 C ATOM 3316 N PRO B1045 140.725 -69.178 56.578 1.00168.45 N ANISOU 3316 N PRO B1045 23902 22602 17500 -1049 2406 493 N ATOM 3317 CA PRO B1045 139.294 -68.830 56.423 1.00169.01 C ANISOU 3317 CA PRO B1045 23794 22546 17877 -1139 3014 430 C ATOM 3318 C PRO B1045 138.478 -68.868 57.735 1.00179.49 C ANISOU 3318 C PRO B1045 25725 23648 18825 -1034 3616 591 C ATOM 3319 O PRO B1045 138.924 -69.501 58.696 1.00182.78 O ANISOU 3319 O PRO B1045 26708 23959 18782 -894 3614 806 O ATOM 3320 CB PRO B1045 138.782 -69.877 55.424 1.00168.95 C ANISOU 3320 CB PRO B1045 23230 22466 18497 -1273 3188 477 C ATOM 3321 CG PRO B1045 139.727 -71.012 55.535 1.00174.00 C ANISOU 3321 CG PRO B1045 24047 23032 19032 -1189 2928 666 C ATOM 3322 CD PRO B1045 141.057 -70.438 55.880 1.00169.06 C ANISOU 3322 CD PRO B1045 23665 22623 17948 -1050 2313 634 C ATOM 3323 N PRO B1046 137.278 -68.214 57.803 1.00177.92 N ANISOU 3323 N PRO B1046 25426 23375 18799 -1059 4163 519 N ATOM 3324 CA PRO B1046 136.487 -68.244 59.052 1.00183.46 C ANISOU 3324 CA PRO B1046 26716 23840 19150 -944 4822 681 C ATOM 3325 C PRO B1046 135.838 -69.608 59.341 1.00191.78 C ANISOU 3325 C PRO B1046 27795 24648 20427 -984 5357 954 C ATOM 3326 O PRO B1046 135.208 -69.777 60.388 1.00196.23 O ANISOU 3326 O PRO B1046 28874 24979 20705 -887 5967 1131 O ATOM 3327 CB PRO B1046 135.424 -67.167 58.821 1.00185.13 C ANISOU 3327 CB PRO B1046 26659 24070 19614 -934 5249 529 C ATOM 3328 CG PRO B1046 135.256 -67.117 57.352 1.00184.78 C ANISOU 3328 CG PRO B1046 25738 24233 20235 -1074 4982 386 C ATOM 3329 CD PRO B1046 136.605 -67.402 56.765 1.00176.49 C ANISOU 3329 CD PRO B1046 24609 23332 19116 -1140 4223 315 C ATOM 3330 N LYS B1047 135.985 -70.569 58.408 1.00187.08 N ANISOU 3330 N LYS B1047 26683 24064 20336 -1141 5178 977 N ATOM 3331 CA LYS B1047 135.478 -71.939 58.521 1.00190.31 C ANISOU 3331 CA LYS B1047 27095 24189 21025 -1247 5654 1198 C ATOM 3332 C LYS B1047 136.557 -72.844 59.123 1.00196.74 C ANISOU 3332 C LYS B1047 28507 24859 21384 -1062 5395 1449 C ATOM 3333 O LYS B1047 136.230 -73.800 59.827 1.00200.92 O ANISOU 3333 O LYS B1047 29466 25062 21814 -1016 5910 1726 O ATOM 3334 CB LYS B1047 135.030 -72.483 57.145 1.00190.09 C ANISOU 3334 CB LYS B1047 26223 24226 21776 -1544 5610 1044 C ATOM 3335 CG LYS B1047 133.939 -71.669 56.441 1.00204.06 C ANISOU 3335 CG LYS B1047 27302 26207 24025 -1689 5803 825 C ATOM 3336 CD LYS B1047 132.530 -72.074 56.857 1.00218.75 C ANISOU 3336 CD LYS B1047 29002 27884 26228 -1841 6638 926 C ATOM 3337 CE LYS B1047 131.498 -71.220 56.169 1.00228.19 C ANISOU 3337 CE LYS B1047 29452 29363 27885 -1909 6768 739 C ATOM 3338 NZ LYS B1047 130.126 -71.553 56.624 1.00241.85 N ANISOU 3338 NZ LYS B1047 30884 31059 29947 -2019 7450 871 N ATOM 3339 N LEU B1048 137.843 -72.536 58.840 1.00190.85 N ANISOU 3339 N LEU B1048 27774 24363 20380 -938 4620 1371 N ATOM 3340 CA LEU B1048 139.004 -73.295 59.319 1.00192.93 C ANISOU 3340 CA LEU B1048 28491 24594 20221 -695 4244 1614 C ATOM 3341 C LEU B1048 139.957 -72.400 60.152 1.00198.43 C ANISOU 3341 C LEU B1048 29674 25554 20166 -477 3705 1582 C ATOM 3342 O LEU B1048 141.163 -72.656 60.198 1.00198.04 O ANISOU 3342 O LEU B1048 29713 25684 19851 -302 3102 1668 O ATOM 3343 CB LEU B1048 139.769 -73.951 58.136 1.00189.35 C ANISOU 3343 CB LEU B1048 27509 24219 20216 -753 3791 1564 C ATOM 3344 CG LEU B1048 138.973 -74.490 56.926 1.00191.64 C ANISOU 3344 CG LEU B1048 27146 24382 21288 -1071 4084 1412 C ATOM 3345 CD1 LEU B1048 139.905 -74.854 55.785 1.00188.14 C ANISOU 3345 CD1 LEU B1048 26274 24065 21145 -1086 3552 1310 C ATOM 3346 CD2 LEU B1048 138.103 -75.687 57.294 1.00198.64 C ANISOU 3346 CD2 LEU B1048 28258 24828 22389 -1173 4825 1631 C ATOM 3347 N GLU B1049 139.404 -71.372 60.835 1.00197.13 N ANISOU 3347 N GLU B1049 29831 25409 19660 -490 3943 1454 N ATOM 3348 CA GLU B1049 140.161 -70.435 61.683 1.00199.38 C ANISOU 3348 CA GLU B1049 30648 25907 19199 -364 3497 1351 C ATOM 3349 C GLU B1049 140.718 -71.121 62.946 1.00210.58 C ANISOU 3349 C GLU B1049 32886 27265 19858 -58 3431 1679 C ATOM 3350 O GLU B1049 141.732 -70.672 63.486 1.00212.25 O ANISOU 3350 O GLU B1049 33426 27753 19465 56 2798 1622 O ATOM 3351 CB GLU B1049 139.323 -69.192 62.061 1.00201.40 C ANISOU 3351 CB GLU B1049 31104 26116 19302 -452 3884 1118 C ATOM 3352 CG GLU B1049 137.865 -69.451 62.424 1.00212.43 C ANISOU 3352 CG GLU B1049 32618 27187 20910 -454 4842 1257 C ATOM 3353 CD GLU B1049 137.522 -69.673 63.886 1.00231.79 C ANISOU 3353 CD GLU B1049 36008 29398 22663 -242 5358 1495 C ATOM 3354 OE1 GLU B1049 138.277 -69.200 64.766 1.00225.19 O ANISOU 3354 OE1 GLU B1049 35854 28678 21030 -97 4976 1459 O ATOM 3355 OE2 GLU B1049 136.460 -70.281 64.150 1.00223.94 O ANISOU 3355 OE2 GLU B1049 35070 28105 21914 -242 6167 1701 O ATOM 3356 N ASP B1050 140.068 -72.213 63.393 1.00211.40 N ANISOU 3356 N ASP B1050 33308 27018 19995 66 4075 2024 N ATOM 3357 CA ASP B1050 140.472 -73.007 64.555 1.00218.04 C ANISOU 3357 CA ASP B1050 34975 27736 20134 416 4134 2416 C ATOM 3358 C ASP B1050 141.552 -74.038 64.176 1.00222.15 C ANISOU 3358 C ASP B1050 35321 28346 20738 629 3616 2662 C ATOM 3359 O ASP B1050 142.395 -74.373 65.010 1.00226.52 O ANISOU 3359 O ASP B1050 36432 29029 20608 982 3238 2922 O ATOM 3360 CB ASP B1050 139.251 -73.729 65.166 1.00224.29 C ANISOU 3360 CB ASP B1050 36204 28041 20976 448 5172 2700 C ATOM 3361 CG ASP B1050 138.015 -72.865 65.359 1.00230.16 C ANISOU 3361 CG ASP B1050 36084 29165 22203 96 5348 2440 C ATOM 3362 OD1 ASP B1050 138.088 -71.886 66.133 1.00231.25 O ANISOU 3362 OD1 ASP B1050 36309 29659 21896 117 5075 2282 O ATOM 3363 OD2 ASP B1050 136.964 -73.195 64.768 1.00232.77 O ANISOU 3363 OD2 ASP B1050 35675 29448 23318 -160 5741 2406 O ATOM 3364 N LYS B1051 141.516 -74.527 62.915 1.00214.00 N ANISOU 3364 N LYS B1051 33529 27256 20525 439 3604 2580 N ATOM 3365 CA LYS B1051 142.407 -75.549 62.347 1.00213.39 C ANISOU 3365 CA LYS B1051 33206 27183 20690 622 3257 2788 C ATOM 3366 C LYS B1051 143.890 -75.145 62.368 1.00217.49 C ANISOU 3366 C LYS B1051 33609 28194 20833 837 2283 2751 C ATOM 3367 O LYS B1051 144.216 -73.956 62.332 1.00214.82 O ANISOU 3367 O LYS B1051 33088 28211 20321 671 1813 2418 O ATOM 3368 CB LYS B1051 141.987 -75.898 60.907 1.00210.21 C ANISOU 3368 CB LYS B1051 32005 26645 21220 296 3436 2588 C ATOM 3369 CG LYS B1051 140.592 -76.506 60.809 1.00224.15 C ANISOU 3369 CG LYS B1051 33778 27949 23440 48 4354 2634 C ATOM 3370 CD LYS B1051 140.471 -77.522 59.687 1.00230.61 C ANISOU 3370 CD LYS B1051 34116 28519 24986 -135 4533 2618 C ATOM 3371 CE LYS B1051 139.177 -78.290 59.799 1.00241.56 C ANISOU 3371 CE LYS B1051 35410 29561 26809 -428 5283 2688 C ATOM 3372 NZ LYS B1051 138.995 -79.242 58.674 1.00246.16 N ANISOU 3372 NZ LYS B1051 35245 30123 28160 -733 5151 2571 N ATOM 3373 N SER B1052 144.779 -76.157 62.424 1.00217.46 N ANISOU 3373 N SER B1052 33699 28193 20733 1210 2020 3101 N ATOM 3374 CA SER B1052 146.235 -75.982 62.459 1.00218.78 C ANISOU 3374 CA SER B1052 33679 28850 20596 1474 1113 3142 C ATOM 3375 C SER B1052 146.824 -75.833 61.038 1.00216.98 C ANISOU 3375 C SER B1052 32538 28812 21092 1276 729 2884 C ATOM 3376 O SER B1052 146.263 -76.400 60.096 1.00213.07 O ANISOU 3376 O SER B1052 31705 27987 21265 1102 1181 2841 O ATOM 3377 CB SER B1052 146.894 -77.148 63.189 1.00229.16 C ANISOU 3377 CB SER B1052 35508 30090 21473 2054 1047 3691 C ATOM 3378 OG SER B1052 146.621 -78.388 62.558 1.00237.37 O ANISOU 3378 OG SER B1052 36458 30657 23076 2154 1584 3942 O ATOM 3379 N PRO B1053 147.959 -75.102 60.857 1.00212.96 N ANISOU 3379 N PRO B1053 31631 28827 20459 1280 -84 2704 N ATOM 3380 CA PRO B1053 148.517 -74.929 59.500 1.00207.18 C ANISOU 3380 CA PRO B1053 30062 28252 20406 1096 -375 2470 C ATOM 3381 C PRO B1053 149.186 -76.178 58.908 1.00210.95 C ANISOU 3381 C PRO B1053 30297 28610 21245 1445 -380 2791 C ATOM 3382 O PRO B1053 149.356 -76.239 57.687 1.00205.74 O ANISOU 3382 O PRO B1053 29040 27919 21212 1280 -378 2613 O ATOM 3383 CB PRO B1053 149.555 -73.809 59.676 1.00209.73 C ANISOU 3383 CB PRO B1053 30111 29149 20429 999 -1185 2219 C ATOM 3384 CG PRO B1053 149.304 -73.225 61.036 1.00219.07 C ANISOU 3384 CG PRO B1053 31995 30437 20805 1016 -1266 2207 C ATOM 3385 CD PRO B1053 148.746 -74.341 61.848 1.00219.15 C ANISOU 3385 CD PRO B1053 32695 30084 20489 1390 -752 2659 C ATOM 3386 N ASP B1054 149.573 -77.155 59.749 1.00213.20 N ANISOU 3386 N ASP B1054 31080 28811 21117 1954 -364 3268 N ATOM 3387 CA ASP B1054 150.246 -78.377 59.299 1.00214.81 C ANISOU 3387 CA ASP B1054 31150 28857 21612 2379 -321 3629 C ATOM 3388 C ASP B1054 149.264 -79.539 59.028 1.00217.90 C ANISOU 3388 C ASP B1054 31899 28534 22360 2378 571 3819 C ATOM 3389 O ASP B1054 149.704 -80.621 58.628 1.00219.49 O ANISOU 3389 O ASP B1054 32092 28479 22827 2714 742 4107 O ATOM 3390 CB ASP B1054 151.316 -78.806 60.321 1.00224.49 C ANISOU 3390 CB ASP B1054 32687 30414 22197 3010 -838 4083 C ATOM 3391 CG ASP B1054 152.496 -77.856 60.448 1.00235.09 C ANISOU 3391 CG ASP B1054 33528 32502 23294 3015 -1789 3906 C ATOM 3392 OD1 ASP B1054 152.734 -77.068 59.504 1.00230.10 O ANISOU 3392 OD1 ASP B1054 32209 32080 23138 2607 -2024 3490 O ATOM 3393 OD2 ASP B1054 153.199 -77.920 61.479 1.00246.72 O ANISOU 3393 OD2 ASP B1054 35196 34265 24281 3145 -2336 4151 O ATOM 3394 N SER B1055 147.947 -79.306 59.211 1.00211.99 N ANISOU 3394 N SER B1055 31435 27458 21654 1985 1161 3642 N ATOM 3395 CA SER B1055 146.886 -80.296 58.986 1.00211.96 C ANISOU 3395 CA SER B1055 31721 26791 22021 1846 2035 3747 C ATOM 3396 C SER B1055 146.754 -80.666 57.482 1.00209.56 C ANISOU 3396 C SER B1055 30812 26282 22529 1541 2211 3477 C ATOM 3397 O SER B1055 147.075 -79.824 56.637 1.00204.15 O ANISOU 3397 O SER B1055 29493 25962 22113 1297 1770 3113 O ATOM 3398 CB SER B1055 145.556 -79.769 59.520 1.00215.36 C ANISOU 3398 CB SER B1055 32446 27044 22335 1465 2551 3578 C ATOM 3399 OG SER B1055 145.158 -78.579 58.860 1.00218.92 O ANISOU 3399 OG SER B1055 32331 27784 23066 999 2346 3083 O ATOM 3400 N PRO B1056 146.269 -81.889 57.114 1.00206.66 N ANISOU 3400 N PRO B1056 30667 25313 22540 1523 2870 3625 N ATOM 3401 CA PRO B1056 146.141 -82.232 55.678 1.00201.89 C ANISOU 3401 CA PRO B1056 29547 24521 22640 1205 3011 3319 C ATOM 3402 C PRO B1056 145.141 -81.353 54.908 1.00198.66 C ANISOU 3402 C PRO B1056 28629 24240 22612 564 3078 2795 C ATOM 3403 O PRO B1056 145.232 -81.277 53.682 1.00194.23 O ANISOU 3403 O PRO B1056 27553 23733 22512 326 2951 2488 O ATOM 3404 CB PRO B1056 145.682 -83.693 55.701 1.00208.34 C ANISOU 3404 CB PRO B1056 30870 24610 23680 1264 3778 3576 C ATOM 3405 CG PRO B1056 145.063 -83.883 57.038 1.00217.88 C ANISOU 3405 CG PRO B1056 32769 25592 24424 1386 4203 3895 C ATOM 3406 CD PRO B1056 145.851 -83.021 57.969 1.00214.50 C ANISOU 3406 CD PRO B1056 32438 25744 23319 1781 3533 4066 C ATOM 3407 N GLU B1057 144.198 -80.694 55.624 1.00194.09 N ANISOU 3407 N GLU B1057 28212 23714 21818 331 3290 2715 N ATOM 3408 CA GLU B1057 143.207 -79.774 55.045 1.00188.54 C ANISOU 3408 CA GLU B1057 27038 23177 21421 -185 3357 2279 C ATOM 3409 C GLU B1057 143.904 -78.488 54.594 1.00185.14 C ANISOU 3409 C GLU B1057 26121 23317 20905 -190 2641 2017 C ATOM 3410 O GLU B1057 143.503 -77.890 53.600 1.00179.90 O ANISOU 3410 O GLU B1057 24929 22804 20619 -524 2555 1658 O ATOM 3411 CB GLU B1057 142.082 -79.452 56.047 1.00192.50 C ANISOU 3411 CB GLU B1057 27891 23558 21691 -334 3842 2329 C ATOM 3412 CG GLU B1057 141.231 -80.644 56.457 1.00208.22 C ANISOU 3412 CG GLU B1057 30322 24952 23840 -432 4661 2552 C ATOM 3413 CD GLU B1057 141.657 -81.317 57.748 1.00232.40 C ANISOU 3413 CD GLU B1057 34211 27762 26329 45 4876 3062 C ATOM 3414 OE1 GLU B1057 141.621 -80.653 58.809 1.00226.86 O ANISOU 3414 OE1 GLU B1057 33881 27257 25057 230 4801 3190 O ATOM 3415 OE2 GLU B1057 141.994 -82.521 57.704 1.00229.12 O ANISOU 3415 OE2 GLU B1057 34123 26924 26008 247 5155 3338 O ATOM 3416 N MET B1058 144.973 -78.094 55.330 1.00181.88 N ANISOU 3416 N MET B1058 25902 23219 19986 183 2128 2207 N ATOM 3417 CA MET B1058 145.826 -76.927 55.073 1.00177.85 C ANISOU 3417 CA MET B1058 25000 23230 19344 186 1439 1996 C ATOM 3418 C MET B1058 147.113 -77.360 54.333 1.00178.97 C ANISOU 3418 C MET B1058 24797 23517 19687 434 1018 2071 C ATOM 3419 O MET B1058 148.188 -76.784 54.530 1.00178.74 O ANISOU 3419 O MET B1058 24594 23901 19417 615 427 2087 O ATOM 3420 CB MET B1058 146.153 -76.180 56.382 1.00183.42 C ANISOU 3420 CB MET B1058 26114 24217 19360 364 1130 2102 C ATOM 3421 CG MET B1058 144.959 -75.480 56.994 1.00187.23 C ANISOU 3421 CG MET B1058 26873 24608 19657 114 1524 1960 C ATOM 3422 SD MET B1058 145.388 -73.881 57.715 1.00191.70 S ANISOU 3422 SD MET B1058 27548 25631 19658 60 990 1731 S ATOM 3423 CE MET B1058 143.895 -73.514 58.574 1.00190.21 C ANISOU 3423 CE MET B1058 27861 25167 19244 -89 1690 1706 C ATOM 3424 N LYS B1059 146.980 -78.398 53.492 1.00173.78 N ANISOU 3424 N LYS B1059 24047 22503 19481 423 1362 2106 N ATOM 3425 CA LYS B1059 148.011 -78.967 52.621 1.00172.53 C ANISOU 3425 CA LYS B1059 23585 22357 19610 648 1155 2164 C ATOM 3426 C LYS B1059 147.485 -78.983 51.196 1.00169.94 C ANISOU 3426 C LYS B1059 22849 21884 19837 260 1361 1799 C ATOM 3427 O LYS B1059 148.245 -78.765 50.253 1.00166.90 O ANISOU 3427 O LYS B1059 22041 21687 19686 290 1073 1662 O ATOM 3428 CB LYS B1059 148.397 -80.393 53.054 1.00180.46 C ANISOU 3428 CB LYS B1059 25047 22971 20549 1094 1454 2607 C ATOM 3429 CG LYS B1059 149.343 -80.478 54.237 1.00198.00 C ANISOU 3429 CG LYS B1059 27568 25445 22218 1637 1077 3027 C ATOM 3430 CD LYS B1059 149.932 -81.880 54.339 1.00211.81 C ANISOU 3430 CD LYS B1059 29646 26830 24004 2169 1333 3476 C ATOM 3431 CE LYS B1059 150.529 -82.175 55.691 1.00226.98 C ANISOU 3431 CE LYS B1059 32046 28897 25300 2745 1112 3973 C ATOM 3432 NZ LYS B1059 149.501 -82.636 56.660 1.00237.45 N ANISOU 3432 NZ LYS B1059 34121 29791 26308 2716 1686 4178 N ATOM 3433 N ASP B1060 146.169 -79.246 51.051 1.00164.71 N ANISOU 3433 N ASP B1060 22307 20903 19372 -108 1867 1642 N ATOM 3434 CA ASP B1060 145.481 -79.314 49.760 1.00160.71 C ANISOU 3434 CA ASP B1060 21445 20275 19341 -515 2060 1277 C ATOM 3435 C ASP B1060 144.820 -77.985 49.371 1.00159.27 C ANISOU 3435 C ASP B1060 20858 20453 19205 -854 1862 933 C ATOM 3436 O ASP B1060 144.773 -77.661 48.186 1.00155.62 O ANISOU 3436 O ASP B1060 19991 20112 19025 -1052 1731 645 O ATOM 3437 CB ASP B1060 144.417 -80.415 49.767 1.00165.34 C ANISOU 3437 CB ASP B1060 22323 20332 20165 -763 2710 1280 C ATOM 3438 CG ASP B1060 144.209 -81.036 48.396 1.00171.89 C ANISOU 3438 CG ASP B1060 22922 20938 21449 -1041 2871 989 C ATOM 3439 OD1 ASP B1060 144.694 -82.161 48.178 1.00174.98 O ANISOU 3439 OD1 ASP B1060 23594 20934 21958 -864 3110 1134 O ATOM 3440 OD2 ASP B1060 143.573 -80.387 47.534 1.00173.43 O ANISOU 3440 OD2 ASP B1060 22687 21355 21855 -1411 2756 618 O ATOM 3441 N PHE B1061 144.268 -77.244 50.358 1.00155.59 N ANISOU 3441 N PHE B1061 20551 20124 18443 -894 1890 974 N ATOM 3442 CA PHE B1061 143.619 -75.947 50.125 1.00151.68 C ANISOU 3442 CA PHE B1061 19744 19928 17960 -1141 1766 697 C ATOM 3443 C PHE B1061 144.660 -74.879 49.766 1.00150.70 C ANISOU 3443 C PHE B1061 19348 20197 17715 -1031 1203 588 C ATOM 3444 O PHE B1061 144.325 -73.912 49.080 1.00146.85 O ANISOU 3444 O PHE B1061 18526 19913 17356 -1220 1085 329 O ATOM 3445 CB PHE B1061 142.790 -75.510 51.345 1.00155.80 C ANISOU 3445 CB PHE B1061 20591 20423 18180 -1168 2034 793 C ATOM 3446 CG PHE B1061 141.327 -75.893 51.293 1.00158.80 C ANISOU 3446 CG PHE B1061 20925 20567 18847 -1471 2602 710 C ATOM 3447 CD1 PHE B1061 140.905 -77.152 51.704 1.00166.01 C ANISOU 3447 CD1 PHE B1061 22164 21057 19855 -1507 3097 902 C ATOM 3448 CD2 PHE B1061 140.368 -74.984 50.860 1.00158.81 C ANISOU 3448 CD2 PHE B1061 20543 20766 19033 -1711 2667 457 C ATOM 3449 CE1 PHE B1061 139.551 -77.501 51.665 1.00168.90 C ANISOU 3449 CE1 PHE B1061 22421 21217 20535 -1851 3641 805 C ATOM 3450 CE2 PHE B1061 139.014 -75.333 50.824 1.00163.65 C ANISOU 3450 CE2 PHE B1061 21007 21224 19949 -1994 3171 385 C ATOM 3451 CZ PHE B1061 138.616 -76.589 51.226 1.00165.88 C ANISOU 3451 CZ PHE B1061 21567 21102 20358 -2097 3652 542 C ATOM 3452 N ARG B1062 145.921 -75.068 50.220 1.00147.51 N ANISOU 3452 N ARG B1062 19072 19900 17076 -721 872 799 N ATOM 3453 CA ARG B1062 147.053 -74.181 49.925 1.00144.74 C ANISOU 3453 CA ARG B1062 18427 19915 16651 -643 347 712 C ATOM 3454 C ARG B1062 147.595 -74.527 48.538 1.00144.35 C ANISOU 3454 C ARG B1062 17985 19853 17010 -652 284 598 C ATOM 3455 O ARG B1062 147.949 -73.629 47.772 1.00140.99 O ANISOU 3455 O ARG B1062 17211 19657 16704 -769 49 387 O ATOM 3456 CB ARG B1062 148.156 -74.279 51.005 1.00148.30 C ANISOU 3456 CB ARG B1062 19103 20548 16696 -318 -10 982 C ATOM 3457 CG ARG B1062 147.686 -74.224 52.477 1.00160.49 C ANISOU 3457 CG ARG B1062 21191 22049 17738 -233 93 1156 C ATOM 3458 CD ARG B1062 147.012 -72.925 52.908 1.00166.15 C ANISOU 3458 CD ARG B1062 21998 22903 18230 -489 91 916 C ATOM 3459 NE ARG B1062 145.576 -72.940 52.620 1.00170.49 N ANISOU 3459 NE ARG B1062 22567 23195 19015 -722 626 795 N ATOM 3460 CZ ARG B1062 144.738 -71.939 52.870 1.00180.67 C ANISOU 3460 CZ ARG B1062 23913 24526 20206 -909 783 612 C ATOM 3461 NH1 ARG B1062 145.181 -70.820 53.434 1.00168.05 N ANISOU 3461 NH1 ARG B1062 22448 23157 18245 -923 474 499 N ATOM 3462 NH2 ARG B1062 143.453 -72.046 52.565 1.00163.24 N ANISOU 3462 NH2 ARG B1062 21622 22130 18270 -1085 1261 533 N ATOM 3463 N HIS B1063 147.612 -75.841 48.211 1.00141.07 N ANISOU 3463 N HIS B1063 17687 19119 16796 -531 558 736 N ATOM 3464 CA HIS B1063 147.998 -76.422 46.922 1.00138.83 C ANISOU 3464 CA HIS B1063 17163 18711 16874 -526 625 633 C ATOM 3465 C HIS B1063 147.016 -75.946 45.845 1.00136.51 C ANISOU 3465 C HIS B1063 16625 18422 16820 -905 754 274 C ATOM 3466 O HIS B1063 147.429 -75.716 44.709 1.00133.97 O ANISOU 3466 O HIS B1063 16021 18193 16687 -943 639 101 O ATOM 3467 CB HIS B1063 148.039 -77.966 47.011 1.00143.33 C ANISOU 3467 CB HIS B1063 18064 18841 17554 -334 992 856 C ATOM 3468 CG HIS B1063 148.241 -78.652 45.693 1.00146.14 C ANISOU 3468 CG HIS B1063 18288 18977 18261 -374 1165 703 C ATOM 3469 ND1 HIS B1063 149.480 -78.713 45.096 1.00148.08 N ANISOU 3469 ND1 HIS B1063 18314 19340 18610 -91 966 771 N ATOM 3470 CD2 HIS B1063 147.340 -79.278 44.898 1.00147.64 C ANISOU 3470 CD2 HIS B1063 18549 18850 18699 -682 1523 469 C ATOM 3471 CE1 HIS B1063 149.297 -79.369 43.960 1.00147.24 C ANISOU 3471 CE1 HIS B1063 18217 18952 18776 -208 1240 582 C ATOM 3472 NE2 HIS B1063 148.023 -79.727 43.801 1.00147.41 N ANISOU 3472 NE2 HIS B1063 18418 18715 18877 -583 1548 378 N ATOM 3473 N GLY B1064 145.751 -75.756 46.229 1.00130.93 N ANISOU 3473 N GLY B1064 16015 17650 16082 -1152 985 183 N ATOM 3474 CA GLY B1064 144.689 -75.254 45.363 1.00127.44 C ANISOU 3474 CA GLY B1064 15304 17284 15834 -1476 1073 -122 C ATOM 3475 C GLY B1064 144.986 -73.870 44.820 1.00125.67 C ANISOU 3475 C GLY B1064 14776 17415 15557 -1491 745 -284 C ATOM 3476 O GLY B1064 144.652 -73.574 43.670 1.00123.48 O ANISOU 3476 O GLY B1064 14238 17227 15451 -1632 712 -508 O ATOM 3477 N PHE B1065 145.646 -73.023 45.638 1.00120.40 N ANISOU 3477 N PHE B1065 14177 16940 14627 -1349 502 -175 N ATOM 3478 CA PHE B1065 146.045 -71.671 45.249 1.00117.09 C ANISOU 3478 CA PHE B1065 13542 16795 14150 -1380 233 -316 C ATOM 3479 C PHE B1065 147.248 -71.696 44.320 1.00118.93 C ANISOU 3479 C PHE B1065 13545 17113 14530 -1281 21 -342 C ATOM 3480 O PHE B1065 147.339 -70.843 43.441 1.00116.61 O ANISOU 3480 O PHE B1065 13036 16955 14317 -1359 -65 -508 O ATOM 3481 CB PHE B1065 146.343 -70.797 46.470 1.00119.74 C ANISOU 3481 CB PHE B1065 14075 17271 14151 -1332 67 -240 C ATOM 3482 CG PHE B1065 145.091 -70.263 47.110 1.00121.43 C ANISOU 3482 CG PHE B1065 14460 17446 14232 -1444 312 -289 C ATOM 3483 CD1 PHE B1065 144.370 -69.235 46.515 1.00122.39 C ANISOU 3483 CD1 PHE B1065 14403 17663 14437 -1558 379 -475 C ATOM 3484 CD2 PHE B1065 144.621 -70.797 48.301 1.00126.57 C ANISOU 3484 CD2 PHE B1065 15464 17954 14673 -1392 520 -119 C ATOM 3485 CE1 PHE B1065 143.196 -68.755 47.097 1.00124.34 C ANISOU 3485 CE1 PHE B1065 14768 17877 14598 -1607 653 -494 C ATOM 3486 CE2 PHE B1065 143.448 -70.317 48.886 1.00130.29 C ANISOU 3486 CE2 PHE B1065 16080 18377 15048 -1477 821 -153 C ATOM 3487 CZ PHE B1065 142.746 -69.296 48.282 1.00126.44 C ANISOU 3487 CZ PHE B1065 15358 18000 14682 -1578 885 -342 C ATOM 3488 N ASP B1066 148.162 -72.671 44.501 1.00116.26 N ANISOU 3488 N ASP B1066 13262 16681 14228 -1074 -20 -155 N ATOM 3489 CA ASP B1066 149.348 -72.839 43.654 1.00115.40 C ANISOU 3489 CA ASP B1066 12915 16634 14298 -931 -150 -142 C ATOM 3490 C ASP B1066 148.919 -73.159 42.226 1.00114.54 C ANISOU 3490 C ASP B1066 12703 16393 14425 -1039 51 -341 C ATOM 3491 O ASP B1066 149.582 -72.741 41.277 1.00113.03 O ANISOU 3491 O ASP B1066 12295 16301 14348 -1013 -21 -430 O ATOM 3492 CB ASP B1066 150.271 -73.943 44.203 1.00121.27 C ANISOU 3492 CB ASP B1066 13756 17280 15040 -615 -172 144 C ATOM 3493 CG ASP B1066 150.991 -73.595 45.497 1.00137.77 C ANISOU 3493 CG ASP B1066 15890 19602 16854 -456 -491 347 C ATOM 3494 OD1 ASP B1066 151.666 -72.539 45.538 1.00138.37 O ANISOU 3494 OD1 ASP B1066 15717 19980 16878 -533 -800 261 O ATOM 3495 OD2 ASP B1066 150.944 -74.416 46.441 1.00147.71 O ANISOU 3495 OD2 ASP B1066 17446 20737 17940 -252 -432 595 O ATOM 3496 N ILE B1067 147.794 -73.897 42.089 1.00109.18 N ANISOU 3496 N ILE B1067 12189 15492 13804 -1183 312 -421 N ATOM 3497 CA ILE B1067 147.150 -74.265 40.827 1.00107.31 C ANISOU 3497 CA ILE B1067 11895 15148 13730 -1354 470 -659 C ATOM 3498 C ILE B1067 146.576 -72.982 40.209 1.00106.73 C ANISOU 3498 C ILE B1067 11606 15342 13603 -1502 334 -855 C ATOM 3499 O ILE B1067 146.811 -72.709 39.032 1.00105.20 O ANISOU 3499 O ILE B1067 11293 15218 13461 -1504 293 -998 O ATOM 3500 CB ILE B1067 146.060 -75.355 41.066 1.00112.46 C ANISOU 3500 CB ILE B1067 12754 15515 14462 -1539 765 -703 C ATOM 3501 CG1 ILE B1067 146.686 -76.677 41.562 1.00116.22 C ANISOU 3501 CG1 ILE B1067 13523 15643 14992 -1342 971 -482 C ATOM 3502 CG2 ILE B1067 145.204 -75.599 39.819 1.00113.10 C ANISOU 3502 CG2 ILE B1067 12735 15565 14671 -1808 852 -1017 C ATOM 3503 CD1 ILE B1067 145.713 -77.619 42.263 1.00127.59 C ANISOU 3503 CD1 ILE B1067 15243 16763 16471 -1508 1308 -434 C ATOM 3504 N LEU B1068 145.849 -72.195 41.028 1.00101.33 N ANISOU 3504 N LEU B1068 10922 14787 12792 -1581 301 -835 N ATOM 3505 CA LEU B1068 145.209 -70.930 40.673 1.00 98.57 C ANISOU 3505 CA LEU B1068 10418 14658 12375 -1656 225 -962 C ATOM 3506 C LEU B1068 146.227 -69.891 40.179 1.00 97.02 C ANISOU 3506 C LEU B1068 10124 14607 12130 -1552 48 -970 C ATOM 3507 O LEU B1068 145.961 -69.229 39.177 1.00 95.29 O ANISOU 3507 O LEU B1068 9794 14495 11918 -1565 31 -1094 O ATOM 3508 CB LEU B1068 144.449 -70.392 41.893 1.00 99.47 C ANISOU 3508 CB LEU B1068 10632 14811 12353 -1695 294 -887 C ATOM 3509 CG LEU B1068 143.105 -69.726 41.613 1.00104.54 C ANISOU 3509 CG LEU B1068 11120 15585 13014 -1789 390 -1006 C ATOM 3510 CD1 LEU B1068 142.043 -70.234 42.567 1.00106.81 C ANISOU 3510 CD1 LEU B1068 11481 15779 13325 -1892 637 -948 C ATOM 3511 CD2 LEU B1068 143.212 -68.203 41.698 1.00106.16 C ANISOU 3511 CD2 LEU B1068 11322 15943 13073 -1694 305 -1011 C ATOM 3512 N VAL B1069 147.394 -69.770 40.861 1.00 91.35 N ANISOU 3512 N VAL B1069 9439 13903 11366 -1454 -81 -833 N ATOM 3513 CA VAL B1069 148.477 -68.846 40.494 1.00 89.33 C ANISOU 3513 CA VAL B1069 9050 13771 11120 -1417 -223 -845 C ATOM 3514 C VAL B1069 149.121 -69.350 39.190 1.00 92.88 C ANISOU 3514 C VAL B1069 9372 14171 11745 -1336 -155 -887 C ATOM 3515 O VAL B1069 149.410 -68.543 38.305 1.00 92.54 O ANISOU 3515 O VAL B1069 9239 14196 11727 -1345 -138 -968 O ATOM 3516 CB VAL B1069 149.517 -68.642 41.640 1.00 93.94 C ANISOU 3516 CB VAL B1069 9638 14441 11614 -1378 -428 -712 C ATOM 3517 CG1 VAL B1069 150.731 -67.846 41.162 1.00 93.89 C ANISOU 3517 CG1 VAL B1069 9408 14560 11705 -1400 -552 -745 C ATOM 3518 CG2 VAL B1069 148.886 -67.950 42.848 1.00 93.95 C ANISOU 3518 CG2 VAL B1069 9849 14481 11367 -1472 -473 -714 C ATOM 3519 N GLY B1070 149.297 -70.669 39.081 1.00 89.68 N ANISOU 3519 N GLY B1070 9021 13610 11444 -1245 -62 -827 N ATOM 3520 CA GLY B1070 149.848 -71.330 37.901 1.00 89.92 C ANISOU 3520 CA GLY B1070 9016 13531 11617 -1147 70 -875 C ATOM 3521 C GLY B1070 149.022 -71.096 36.648 1.00 92.58 C ANISOU 3521 C GLY B1070 9393 13876 11909 -1252 157 -1092 C ATOM 3522 O GLY B1070 149.584 -70.844 35.579 1.00 92.70 O ANISOU 3522 O GLY B1070 9370 13904 11949 -1182 223 -1151 O ATOM 3523 N GLN B1071 147.676 -71.138 36.786 1.00 87.45 N ANISOU 3523 N GLN B1071 8804 13247 11178 -1410 156 -1202 N ATOM 3524 CA GLN B1071 146.710 -70.876 35.720 1.00 86.49 C ANISOU 3524 CA GLN B1071 8666 13222 10974 -1507 154 -1404 C ATOM 3525 C GLN B1071 146.696 -69.389 35.336 1.00 87.21 C ANISOU 3525 C GLN B1071 8673 13518 10944 -1442 69 -1400 C ATOM 3526 O GLN B1071 146.468 -69.077 34.167 1.00 86.97 O ANISOU 3526 O GLN B1071 8658 13571 10815 -1402 67 -1510 O ATOM 3527 CB GLN B1071 145.309 -71.329 36.140 1.00 89.01 C ANISOU 3527 CB GLN B1071 8972 13552 11297 -1699 168 -1495 C ATOM 3528 CG GLN B1071 145.051 -72.804 35.851 1.00112.44 C ANISOU 3528 CG GLN B1071 12068 16285 14369 -1839 307 -1616 C ATOM 3529 CD GLN B1071 143.785 -73.342 36.475 1.00133.36 C ANISOU 3529 CD GLN B1071 14680 18898 17092 -2082 383 -1684 C ATOM 3530 OE1 GLN B1071 143.784 -74.410 37.088 1.00130.74 O ANISOU 3530 OE1 GLN B1071 14511 18289 16874 -2165 570 -1634 O ATOM 3531 NE2 GLN B1071 142.669 -72.644 36.309 1.00126.46 N ANISOU 3531 NE2 GLN B1071 13585 18292 16172 -2187 279 -1783 N ATOM 3532 N ILE B1072 146.934 -68.479 36.316 1.00 82.14 N ANISOU 3532 N ILE B1072 7998 12934 10279 -1427 17 -1277 N ATOM 3533 CA ILE B1072 147.000 -67.027 36.095 1.00 81.28 C ANISOU 3533 CA ILE B1072 7879 12931 10072 -1377 4 -1263 C ATOM 3534 C ILE B1072 148.251 -66.726 35.235 1.00 87.10 C ANISOU 3534 C ILE B1072 8603 13627 10865 -1299 70 -1244 C ATOM 3535 O ILE B1072 148.151 -65.961 34.274 1.00 86.92 O ANISOU 3535 O ILE B1072 8633 13645 10748 -1225 141 -1277 O ATOM 3536 CB ILE B1072 146.964 -66.223 37.437 1.00 83.74 C ANISOU 3536 CB ILE B1072 8231 13256 10331 -1429 -35 -1181 C ATOM 3537 CG1 ILE B1072 145.534 -66.203 38.033 1.00 84.14 C ANISOU 3537 CG1 ILE B1072 8301 13358 10309 -1461 -1 -1197 C ATOM 3538 CG2 ILE B1072 147.464 -64.782 37.252 1.00 84.00 C ANISOU 3538 CG2 ILE B1072 8313 13297 10307 -1413 5 -1173 C ATOM 3539 CD1 ILE B1072 145.422 -65.835 39.551 1.00 87.12 C ANISOU 3539 CD1 ILE B1072 8805 13696 10602 -1514 10 -1120 C ATOM 3540 N ASP B1073 149.395 -67.375 35.550 1.00 85.05 N ANISOU 3540 N ASP B1073 8267 13289 10758 -1284 73 -1169 N ATOM 3541 CA ASP B1073 150.670 -67.244 34.833 1.00 86.28 C ANISOU 3541 CA ASP B1073 8335 13409 11039 -1209 183 -1131 C ATOM 3542 C ASP B1073 150.577 -67.738 33.374 1.00 90.76 C ANISOU 3542 C ASP B1073 9016 13908 11559 -1103 350 -1222 C ATOM 3543 O ASP B1073 151.232 -67.165 32.494 1.00 91.02 O ANISOU 3543 O ASP B1073 9060 13924 11599 -1035 510 -1212 O ATOM 3544 CB ASP B1073 151.783 -68.007 35.570 1.00 90.02 C ANISOU 3544 CB ASP B1073 8641 13860 11703 -1159 130 -1004 C ATOM 3545 CG ASP B1073 152.312 -67.338 36.831 1.00103.09 C ANISOU 3545 CG ASP B1073 10161 15632 13375 -1263 -66 -924 C ATOM 3546 OD1 ASP B1073 152.135 -66.107 36.973 1.00103.56 O ANISOU 3546 OD1 ASP B1073 10258 15739 13349 -1401 -86 -985 O ATOM 3547 OD2 ASP B1073 152.947 -68.038 37.654 1.00111.51 O ANISOU 3547 OD2 ASP B1073 11110 16737 14521 -1194 -195 -802 O ATOM 3548 N ASP B1074 149.777 -68.801 33.125 1.00 87.15 N ANISOU 3548 N ASP B1074 8675 13396 11041 -1114 335 -1324 N ATOM 3549 CA ASP B1074 149.544 -69.356 31.786 1.00 87.92 C ANISOU 3549 CA ASP B1074 8948 13435 11024 -1060 451 -1471 C ATOM 3550 C ASP B1074 148.792 -68.333 30.939 1.00 89.25 C ANISOU 3550 C ASP B1074 9201 13765 10943 -1033 402 -1544 C ATOM 3551 O ASP B1074 149.165 -68.091 29.791 1.00 90.08 O ANISOU 3551 O ASP B1074 9454 13854 10920 -916 540 -1576 O ATOM 3552 CB ASP B1074 148.747 -70.676 31.866 1.00 91.21 C ANISOU 3552 CB ASP B1074 9472 13746 11436 -1169 423 -1609 C ATOM 3553 CG ASP B1074 149.519 -71.909 32.312 1.00104.83 C ANISOU 3553 CG ASP B1074 11241 15225 13364 -1110 569 -1535 C ATOM 3554 OD1 ASP B1074 150.773 -71.834 32.409 1.00106.33 O ANISOU 3554 OD1 ASP B1074 11330 15366 13705 -938 679 -1373 O ATOM 3555 OD2 ASP B1074 148.875 -72.962 32.527 1.00111.25 O ANISOU 3555 OD2 ASP B1074 12183 15887 14199 -1227 599 -1632 O ATOM 3556 N ALA B1075 147.754 -67.711 31.539 1.00 82.88 N ANISOU 3556 N ALA B1075 8320 13111 10061 -1100 237 -1540 N ATOM 3557 CA ALA B1075 146.922 -66.667 30.951 1.00 82.21 C ANISOU 3557 CA ALA B1075 8280 13205 9750 -1008 174 -1550 C ATOM 3558 C ALA B1075 147.737 -65.390 30.739 1.00 84.03 C ANISOU 3558 C ALA B1075 8583 13382 9964 -889 337 -1409 C ATOM 3559 O ALA B1075 147.522 -64.692 29.745 1.00 85.64 O ANISOU 3559 O ALA B1075 8944 13644 9952 -727 403 -1392 O ATOM 3560 CB ALA B1075 145.730 -66.388 31.850 1.00 82.35 C ANISOU 3560 CB ALA B1075 8158 13364 9768 -1077 26 -1542 C ATOM 3561 N LEU B1076 148.683 -65.099 31.665 1.00 77.06 N ANISOU 3561 N LEU B1076 7596 12387 9297 -980 403 -1312 N ATOM 3562 CA LEU B1076 149.589 -63.947 31.600 1.00 75.74 C ANISOU 3562 CA LEU B1076 7460 12130 9189 -973 583 -1215 C ATOM 3563 C LEU B1076 150.555 -64.090 30.429 1.00 79.03 C ANISOU 3563 C LEU B1076 7948 12451 9628 -877 823 -1199 C ATOM 3564 O LEU B1076 150.837 -63.102 29.756 1.00 78.91 O ANISOU 3564 O LEU B1076 8082 12369 9532 -802 1037 -1136 O ATOM 3565 CB LEU B1076 150.378 -63.796 32.909 1.00 75.08 C ANISOU 3565 CB LEU B1076 7196 12004 9329 -1155 521 -1167 C ATOM 3566 CG LEU B1076 149.746 -62.959 34.016 1.00 78.89 C ANISOU 3566 CG LEU B1076 7722 12507 9745 -1252 422 -1161 C ATOM 3567 CD1 LEU B1076 150.313 -63.339 35.364 1.00 78.53 C ANISOU 3567 CD1 LEU B1076 7528 12479 9831 -1417 255 -1149 C ATOM 3568 CD2 LEU B1076 149.945 -61.467 33.771 1.00 82.97 C ANISOU 3568 CD2 LEU B1076 8399 12915 10211 -1265 620 -1130 C ATOM 3569 N LYS B1077 151.043 -65.327 30.178 1.00 75.87 N ANISOU 3569 N LYS B1077 7488 12008 9331 -859 844 -1245 N ATOM 3570 CA LYS B1077 151.952 -65.660 29.076 1.00 77.52 C ANISOU 3570 CA LYS B1077 7785 12104 9565 -738 1126 -1237 C ATOM 3571 C LYS B1077 151.278 -65.415 27.720 1.00 83.17 C ANISOU 3571 C LYS B1077 8841 12847 9912 -575 1211 -1303 C ATOM 3572 O LYS B1077 151.946 -64.990 26.781 1.00 84.10 O ANISOU 3572 O LYS B1077 9122 12866 9964 -456 1514 -1245 O ATOM 3573 CB LYS B1077 152.419 -67.120 29.184 1.00 80.22 C ANISOU 3573 CB LYS B1077 8047 12364 10070 -711 1143 -1277 C ATOM 3574 CG LYS B1077 153.880 -67.334 28.795 1.00 92.24 C ANISOU 3574 CG LYS B1077 9439 13764 11843 -612 1461 -1177 C ATOM 3575 CD LYS B1077 154.061 -67.711 27.329 1.00100.46 C ANISOU 3575 CD LYS B1077 10793 14677 12699 -434 1776 -1246 C ATOM 3576 CE LYS B1077 155.517 -67.780 26.943 1.00107.52 C ANISOU 3576 CE LYS B1077 11524 15451 13879 -316 2172 -1120 C ATOM 3577 NZ LYS B1077 155.692 -68.209 25.531 1.00118.19 N ANISOU 3577 NZ LYS B1077 13253 16642 15010 -121 2537 -1191 N ATOM 3578 N LEU B1078 149.955 -65.658 27.631 1.00 80.37 N ANISOU 3578 N LEU B1078 8579 12648 9308 -569 942 -1416 N ATOM 3579 CA LEU B1078 149.161 -65.439 26.420 1.00 82.63 C ANISOU 3579 CA LEU B1078 9152 13057 9188 -404 901 -1487 C ATOM 3580 C LEU B1078 148.913 -63.944 26.200 1.00 88.34 C ANISOU 3580 C LEU B1078 9991 13829 9747 -247 980 -1323 C ATOM 3581 O LEU B1078 149.087 -63.460 25.082 1.00 90.02 O ANISOU 3581 O LEU B1078 10503 14013 9687 -42 1172 -1264 O ATOM 3582 CB LEU B1078 147.825 -66.193 26.502 1.00 82.85 C ANISOU 3582 CB LEU B1078 9128 13289 9062 -492 547 -1671 C ATOM 3583 CG LEU B1078 147.908 -67.712 26.584 1.00 88.25 C ANISOU 3583 CG LEU B1078 9803 13865 9861 -661 514 -1860 C ATOM 3584 CD1 LEU B1078 146.654 -68.286 27.207 1.00 87.98 C ANISOU 3584 CD1 LEU B1078 9590 13989 9850 -858 207 -2001 C ATOM 3585 CD2 LEU B1078 148.174 -68.330 25.214 1.00 94.37 C ANISOU 3585 CD2 LEU B1078 10928 14569 10359 -571 647 -2018 C ATOM 3586 N ALA B1079 148.525 -63.217 27.273 1.00 84.43 N ANISOU 3586 N ALA B1079 9317 13366 9396 -324 878 -1240 N ATOM 3587 CA ALA B1079 148.249 -61.776 27.274 1.00 85.09 C ANISOU 3587 CA ALA B1079 9537 13426 9369 -179 997 -1080 C ATOM 3588 C ALA B1079 149.492 -60.955 26.896 1.00 91.30 C ANISOU 3588 C ALA B1079 10485 13948 10258 -175 1413 -953 C ATOM 3589 O ALA B1079 149.359 -59.966 26.175 1.00 92.32 O ANISOU 3589 O ALA B1079 10911 14006 10161 41 1627 -818 O ATOM 3590 CB ALA B1079 147.733 -61.344 28.640 1.00 83.86 C ANISOU 3590 CB ALA B1079 9183 13293 9388 -308 860 -1057 C ATOM 3591 N ASN B1080 150.693 -61.380 27.366 1.00 89.13 N ANISOU 3591 N ASN B1080 9999 13534 10331 -399 1543 -981 N ATOM 3592 CA ASN B1080 151.984 -60.732 27.084 1.00 91.66 C ANISOU 3592 CA ASN B1080 10345 13628 10853 -475 1948 -887 C ATOM 3593 C ASN B1080 152.412 -60.933 25.624 1.00 98.74 C ANISOU 3593 C ASN B1080 11524 14444 11549 -259 2266 -844 C ATOM 3594 O ASN B1080 153.184 -60.130 25.101 1.00 99.53 O ANISOU 3594 O ASN B1080 11773 14340 11705 -246 2688 -726 O ATOM 3595 CB ASN B1080 153.074 -61.242 28.023 1.00 94.24 C ANISOU 3595 CB ASN B1080 10266 13926 11614 -748 1921 -927 C ATOM 3596 CG ASN B1080 153.189 -60.436 29.292 1.00122.34 C ANISOU 3596 CG ASN B1080 13658 17458 15368 -1004 1813 -932 C ATOM 3597 OD1 ASN B1080 152.496 -60.685 30.282 1.00118.41 O ANISOU 3597 OD1 ASN B1080 13065 17079 14845 -1072 1488 -990 O ATOM 3598 ND2 ASN B1080 154.075 -59.450 29.290 1.00115.73 N ANISOU 3598 ND2 ASN B1080 12808 16443 14721 -1178 2114 -886 N ATOM 3599 N GLU B1081 151.909 -62.006 24.980 1.00 97.30 N ANISOU 3599 N GLU B1081 11447 14398 11125 -117 2093 -955 N ATOM 3600 CA GLU B1081 152.145 -62.337 23.571 1.00100.73 C ANISOU 3600 CA GLU B1081 12239 14778 11256 106 2345 -960 C ATOM 3601 C GLU B1081 151.130 -61.605 22.669 1.00108.65 C ANISOU 3601 C GLU B1081 13660 15895 11725 397 2283 -891 C ATOM 3602 O GLU B1081 151.280 -61.605 21.444 1.00111.78 O ANISOU 3602 O GLU B1081 14458 16248 11767 626 2512 -858 O ATOM 3603 CB GLU B1081 152.053 -63.858 23.349 1.00101.97 C ANISOU 3603 CB GLU B1081 12368 15004 11373 88 2177 -1158 C ATOM 3604 CG GLU B1081 153.283 -64.635 23.782 1.00112.57 C ANISOU 3604 CG GLU B1081 13421 16187 13162 -36 2393 -1161 C ATOM 3605 CD GLU B1081 153.186 -66.134 23.575 1.00136.37 C ANISOU 3605 CD GLU B1081 16489 19186 16139 -22 2302 -1342 C ATOM 3606 OE1 GLU B1081 152.237 -66.751 24.111 1.00129.75 O ANISOU 3606 OE1 GLU B1081 15581 18478 15241 -132 1908 -1482 O ATOM 3607 OE2 GLU B1081 154.074 -66.697 22.894 1.00136.03 O ANISOU 3607 OE2 GLU B1081 16570 18967 16150 92 2675 -1343 O ATOM 3608 N GLY B1082 150.119 -60.992 23.296 1.00104.80 N ANISOU 3608 N GLY B1082 13086 15560 11172 420 1987 -852 N ATOM 3609 CA GLY B1082 149.043 -60.266 22.631 1.00107.13 C ANISOU 3609 CA GLY B1082 13680 16026 11000 748 1860 -746 C ATOM 3610 C GLY B1082 147.974 -61.200 22.106 1.00112.81 C ANISOU 3610 C GLY B1082 14406 17096 11362 842 1404 -930 C ATOM 3611 O GLY B1082 147.611 -61.129 20.929 1.00115.99 O ANISOU 3611 O GLY B1082 15172 17632 11268 1126 1374 -908 O ATOM 3612 N LYS B1083 147.482 -62.100 22.979 1.00107.37 N ANISOU 3612 N LYS B1083 13332 16555 10910 582 1051 -1122 N ATOM 3613 CA LYS B1083 146.485 -63.118 22.643 1.00108.60 C ANISOU 3613 CA LYS B1083 13413 17018 10831 537 620 -1359 C ATOM 3614 C LYS B1083 145.271 -62.988 23.575 1.00112.33 C ANISOU 3614 C LYS B1083 13505 17753 11423 470 249 -1374 C ATOM 3615 O LYS B1083 145.190 -63.681 24.591 1.00109.47 O ANISOU 3615 O LYS B1083 12827 17357 11411 177 141 -1491 O ATOM 3616 CB LYS B1083 147.121 -64.525 22.721 1.00110.02 C ANISOU 3616 CB LYS B1083 13540 17047 11215 260 662 -1593 C ATOM 3617 CG LYS B1083 148.265 -64.735 21.730 1.00124.29 C ANISOU 3617 CG LYS B1083 15721 18607 12898 367 1071 -1584 C ATOM 3618 CD LYS B1083 149.061 -65.998 21.996 1.00133.30 C ANISOU 3618 CD LYS B1083 16779 19526 14342 153 1219 -1744 C ATOM 3619 CE LYS B1083 150.158 -66.150 20.971 1.00148.91 C ANISOU 3619 CE LYS B1083 19121 21260 16196 310 1687 -1715 C ATOM 3620 NZ LYS B1083 151.052 -67.295 21.280 1.00158.47 N ANISOU 3620 NZ LYS B1083 20226 22224 17761 180 1910 -1810 N ATOM 3621 N VAL B1084 144.336 -62.077 23.222 1.00111.75 N ANISOU 3621 N VAL B1084 13476 17931 11052 785 96 -1224 N ATOM 3622 CA VAL B1084 143.127 -61.752 23.994 1.00111.41 C ANISOU 3622 CA VAL B1084 13070 18156 11103 824 -187 -1181 C ATOM 3623 C VAL B1084 142.217 -62.981 24.128 1.00116.45 C ANISOU 3623 C VAL B1084 13363 19103 11778 555 -609 -1472 C ATOM 3624 O VAL B1084 141.985 -63.430 25.252 1.00113.90 O ANISOU 3624 O VAL B1084 12712 18735 11832 277 -649 -1546 O ATOM 3625 CB VAL B1084 142.346 -60.541 23.414 1.00118.73 C ANISOU 3625 CB VAL B1084 14137 19305 11672 1317 -236 -923 C ATOM 3626 CG1 VAL B1084 141.207 -60.120 24.341 1.00118.45 C ANISOU 3626 CG1 VAL B1084 13697 19491 11817 1393 -417 -838 C ATOM 3627 CG2 VAL B1084 143.265 -59.360 23.158 1.00118.59 C ANISOU 3627 CG2 VAL B1084 14552 18910 11598 1556 255 -647 C ATOM 3628 N LYS B1085 141.719 -63.517 22.992 1.00116.79 N ANISOU 3628 N LYS B1085 13514 19443 11418 615 -903 -1645 N ATOM 3629 CA LYS B1085 140.818 -64.674 22.918 1.00118.85 C ANISOU 3629 CA LYS B1085 13482 20007 11667 310 -1315 -1975 C ATOM 3630 C LYS B1085 141.371 -65.913 23.649 1.00120.56 C ANISOU 3630 C LYS B1085 13618 19904 12283 -164 -1181 -2206 C ATOM 3631 O LYS B1085 140.597 -66.679 24.223 1.00120.58 O ANISOU 3631 O LYS B1085 13271 20040 12504 -476 -1391 -2397 O ATOM 3632 CB LYS B1085 140.525 -65.022 21.448 1.00126.37 C ANISOU 3632 CB LYS B1085 14718 21251 12047 423 -1602 -2159 C ATOM 3633 CG LYS B1085 139.229 -64.421 20.902 1.00141.05 C ANISOU 3633 CG LYS B1085 16352 23700 13541 736 -2061 -2085 C ATOM 3634 CD LYS B1085 139.392 -63.000 20.364 1.00148.58 C ANISOU 3634 CD LYS B1085 17621 24676 14155 1344 -1894 -1678 C ATOM 3635 CE LYS B1085 138.058 -62.405 19.988 1.00159.21 C ANISOU 3635 CE LYS B1085 18663 26630 15197 1721 -2354 -1549 C ATOM 3636 NZ LYS B1085 138.163 -60.958 19.674 1.00166.75 N ANISOU 3636 NZ LYS B1085 19927 27534 15896 2358 -2112 -1089 N ATOM 3637 N GLU B1086 142.703 -66.087 23.636 1.00115.37 N ANISOU 3637 N GLU B1086 13272 18826 11738 -191 -801 -2161 N ATOM 3638 CA GLU B1086 143.403 -67.202 24.271 1.00113.45 C ANISOU 3638 CA GLU B1086 13008 18248 11850 -524 -620 -2308 C ATOM 3639 C GLU B1086 143.520 -66.976 25.782 1.00114.46 C ANISOU 3639 C GLU B1086 12824 18229 12437 -640 -507 -2145 C ATOM 3640 O GLU B1086 143.319 -67.926 26.544 1.00113.52 O ANISOU 3640 O GLU B1086 12528 18018 12587 -930 -542 -2276 O ATOM 3641 CB GLU B1086 144.787 -67.419 23.639 1.00114.77 C ANISOU 3641 CB GLU B1086 13571 18073 11965 -438 -250 -2285 C ATOM 3642 CG GLU B1086 144.734 -67.844 22.181 1.00131.78 C ANISOU 3642 CG GLU B1086 16129 20311 13629 -355 -309 -2490 C ATOM 3643 CD GLU B1086 144.783 -66.711 21.172 1.00162.90 C ANISOU 3643 CD GLU B1086 20372 24402 17123 42 -263 -2300 C ATOM 3644 OE1 GLU B1086 145.792 -66.625 20.436 1.00165.71 O ANISOU 3644 OE1 GLU B1086 21123 24512 17327 201 103 -2237 O ATOM 3645 OE2 GLU B1086 143.820 -65.912 21.109 1.00160.16 O ANISOU 3645 OE2 GLU B1086 19875 24402 16575 225 -553 -2190 O ATOM 3646 N ALA B1087 143.828 -65.725 26.215 1.00109.29 N ANISOU 3646 N ALA B1087 12155 17528 11842 -422 -351 -1869 N ATOM 3647 CA ALA B1087 143.934 -65.355 27.634 1.00105.80 C ANISOU 3647 CA ALA B1087 11489 16959 11750 -518 -256 -1728 C ATOM 3648 C ALA B1087 142.555 -65.361 28.306 1.00110.26 C ANISOU 3648 C ALA B1087 11725 17787 12381 -586 -491 -1760 C ATOM 3649 O ALA B1087 142.461 -65.717 29.480 1.00108.07 O ANISOU 3649 O ALA B1087 11269 17406 12385 -782 -451 -1756 O ATOM 3650 CB ALA B1087 144.583 -63.991 27.786 1.00105.37 C ANISOU 3650 CB ALA B1087 11573 16765 11698 -308 -14 -1483 C ATOM 3651 N GLN B1088 141.488 -64.990 27.554 1.00109.75 N ANISOU 3651 N GLN B1088 11570 18081 12048 -404 -730 -1780 N ATOM 3652 CA GLN B1088 140.098 -64.995 28.029 1.00111.01 C ANISOU 3652 CA GLN B1088 11329 18564 12285 -440 -956 -1808 C ATOM 3653 C GLN B1088 139.593 -66.441 28.197 1.00116.58 C ANISOU 3653 C GLN B1088 11818 19326 13153 -858 -1120 -2102 C ATOM 3654 O GLN B1088 138.772 -66.705 29.079 1.00115.98 O ANISOU 3654 O GLN B1088 11401 19340 13325 -1032 -1150 -2125 O ATOM 3655 CB GLN B1088 139.188 -64.212 27.072 1.00116.01 C ANISOU 3655 CB GLN B1088 11888 19615 12574 -79 -1196 -1726 C ATOM 3656 CG GLN B1088 139.316 -62.691 27.192 1.00124.07 C ANISOU 3656 CG GLN B1088 13071 20567 13503 356 -980 -1392 C ATOM 3657 CD GLN B1088 138.487 -61.927 26.178 1.00143.68 C ANISOU 3657 CD GLN B1088 15541 23449 15603 808 -1198 -1254 C ATOM 3658 OE1 GLN B1088 138.173 -62.408 25.082 1.00144.27 O ANISOU 3658 OE1 GLN B1088 15633 23827 15355 840 -1512 -1401 O ATOM 3659 NE2 GLN B1088 138.152 -60.690 26.507 1.00131.16 N ANISOU 3659 NE2 GLN B1088 13974 21854 14007 1198 -1025 -958 N ATOM 3660 N ALA B1089 140.103 -67.368 27.356 1.00115.39 N ANISOU 3660 N ALA B1089 11905 19073 12864 -1023 -1164 -2328 N ATOM 3661 CA ALA B1089 139.790 -68.800 27.389 1.00117.46 C ANISOU 3661 CA ALA B1089 12094 19275 13261 -1448 -1247 -2639 C ATOM 3662 C ALA B1089 140.434 -69.464 28.610 1.00118.66 C ANISOU 3662 C ALA B1089 12280 19010 13795 -1661 -951 -2585 C ATOM 3663 O ALA B1089 139.828 -70.352 29.213 1.00118.71 O ANISOU 3663 O ALA B1089 12104 18970 14032 -1987 -952 -2727 O ATOM 3664 CB ALA B1089 140.270 -69.472 26.109 1.00120.82 C ANISOU 3664 CB ALA B1089 12886 19642 13379 -1502 -1306 -2881 C ATOM 3665 N ALA B1090 141.663 -69.027 28.972 1.00113.21 N ANISOU 3665 N ALA B1090 11817 18029 13168 -1477 -697 -2371 N ATOM 3666 CA ALA B1090 142.420 -69.522 30.125 1.00111.16 C ANISOU 3666 CA ALA B1090 11598 17426 13211 -1589 -463 -2266 C ATOM 3667 C ALA B1090 141.787 -69.047 31.439 1.00115.39 C ANISOU 3667 C ALA B1090 11884 18025 13935 -1618 -445 -2112 C ATOM 3668 O ALA B1090 141.947 -69.706 32.468 1.00113.82 O ANISOU 3668 O ALA B1090 11680 17612 13953 -1777 -314 -2073 O ATOM 3669 CB ALA B1090 143.868 -69.065 30.036 1.00109.74 C ANISOU 3669 CB ALA B1090 11642 17025 13030 -1383 -263 -2094 C ATOM 3670 N ALA B1091 141.058 -67.910 31.390 1.00113.88 N ANISOU 3670 N ALA B1091 11526 18109 13634 -1427 -545 -2008 N ATOM 3671 CA ALA B1091 140.335 -67.326 32.519 1.00113.84 C ANISOU 3671 CA ALA B1091 11310 18178 13765 -1401 -486 -1866 C ATOM 3672 C ALA B1091 139.094 -68.160 32.869 1.00121.81 C ANISOU 3672 C ALA B1091 12003 19338 14941 -1668 -551 -2012 C ATOM 3673 O ALA B1091 138.698 -68.196 34.035 1.00121.13 O ANISOU 3673 O ALA B1091 11809 19175 15040 -1750 -395 -1920 O ATOM 3674 CB ALA B1091 139.931 -65.900 32.197 1.00115.00 C ANISOU 3674 CB ALA B1091 11412 18542 13739 -1065 -521 -1709 C ATOM 3675 N GLU B1092 138.495 -68.840 31.865 1.00122.47 N ANISOU 3675 N GLU B1092 11954 19627 14951 -1830 -764 -2254 N ATOM 3676 CA GLU B1092 137.338 -69.727 32.041 1.00126.37 C ANISOU 3676 CA GLU B1092 12110 20270 15635 -2180 -835 -2456 C ATOM 3677 C GLU B1092 137.726 -70.969 32.865 1.00130.02 C ANISOU 3677 C GLU B1092 12744 20311 16345 -2515 -580 -2524 C ATOM 3678 O GLU B1092 136.866 -71.552 33.529 1.00132.13 O ANISOU 3678 O GLU B1092 12773 20577 16854 -2796 -475 -2589 O ATOM 3679 CB GLU B1092 136.757 -70.159 30.677 1.00132.24 C ANISOU 3679 CB GLU B1092 12726 21332 16188 -2317 -1172 -2752 C ATOM 3680 CG GLU B1092 136.018 -69.066 29.916 1.00146.66 C ANISOU 3680 CG GLU B1092 14284 23670 17771 -1983 -1471 -2675 C ATOM 3681 CD GLU B1092 135.489 -69.419 28.535 1.00173.71 C ANISOU 3681 CD GLU B1092 17615 27477 20910 -2076 -1879 -2960 C ATOM 3682 OE1 GLU B1092 135.713 -70.558 28.064 1.00169.59 O ANISOU 3682 OE1 GLU B1092 17282 26791 20363 -2453 -1923 -3277 O ATOM 3683 OE2 GLU B1092 134.848 -68.539 27.916 1.00172.12 O ANISOU 3683 OE2 GLU B1092 17182 27737 20477 -1747 -2156 -2863 O ATOM 3684 N GLN B1093 139.016 -71.373 32.807 1.00123.95 N ANISOU 3684 N GLN B1093 12384 19184 15527 -2461 -451 -2487 N ATOM 3685 CA GLN B1093 139.565 -72.512 33.539 1.00123.32 C ANISOU 3685 CA GLN B1093 12539 18678 15640 -2659 -194 -2486 C ATOM 3686 C GLN B1093 139.678 -72.195 35.033 1.00125.29 C ANISOU 3686 C GLN B1093 12793 18787 16025 -2570 11 -2212 C ATOM 3687 O GLN B1093 139.577 -73.114 35.846 1.00125.87 O ANISOU 3687 O GLN B1093 12962 18590 16274 -2763 230 -2191 O ATOM 3688 CB GLN B1093 140.926 -72.926 32.962 1.00123.31 C ANISOU 3688 CB GLN B1093 12917 18396 15540 -2532 -124 -2489 C ATOM 3689 CG GLN B1093 140.808 -73.882 31.774 1.00138.75 C ANISOU 3689 CG GLN B1093 15024 20287 17408 -2752 -180 -2819 C ATOM 3690 CD GLN B1093 142.067 -73.998 30.934 1.00152.36 C ANISOU 3690 CD GLN B1093 17097 21819 18972 -2537 -105 -2820 C ATOM 3691 OE1 GLN B1093 142.014 -73.984 29.698 1.00146.89 O ANISOU 3691 OE1 GLN B1093 16519 21257 18036 -2536 -241 -3029 O ATOM 3692 NE2 GLN B1093 143.223 -74.148 31.566 1.00141.61 N ANISOU 3692 NE2 GLN B1093 15909 20163 17733 -2343 118 -2588 N ATOM 3693 N LEU B1094 139.871 -70.900 35.393 1.00119.83 N ANISOU 3693 N LEU B1094 12054 18251 15223 -2281 -35 -2008 N ATOM 3694 CA LEU B1094 139.948 -70.421 36.779 1.00118.35 C ANISOU 3694 CA LEU B1094 11921 17965 15081 -2187 130 -1779 C ATOM 3695 C LEU B1094 138.604 -70.613 37.499 1.00126.19 C ANISOU 3695 C LEU B1094 12662 19049 16234 -2362 272 -1789 C ATOM 3696 O LEU B1094 138.587 -70.900 38.701 1.00125.62 O ANISOU 3696 O LEU B1094 12722 18776 16233 -2410 500 -1653 O ATOM 3697 CB LEU B1094 140.365 -68.941 36.830 1.00115.90 C ANISOU 3697 CB LEU B1094 11649 17784 14604 -1889 64 -1628 C ATOM 3698 CG LEU B1094 141.849 -68.640 36.630 1.00117.75 C ANISOU 3698 CG LEU B1094 12130 17868 14742 -1744 26 -1549 C ATOM 3699 CD1 LEU B1094 142.041 -67.328 35.918 1.00116.70 C ANISOU 3699 CD1 LEU B1094 11996 17890 14455 -1525 -51 -1512 C ATOM 3700 CD2 LEU B1094 142.589 -68.623 37.953 1.00118.59 C ANISOU 3700 CD2 LEU B1094 12417 17782 14859 -1727 121 -1384 C ATOM 3701 N LYS B1095 137.480 -70.473 36.752 1.00126.73 N ANISOU 3701 N LYS B1095 12356 19442 16352 -2449 138 -1944 N ATOM 3702 CA LYS B1095 136.100 -70.666 37.226 1.00130.34 C ANISOU 3702 CA LYS B1095 12434 20066 17024 -2640 264 -1983 C ATOM 3703 C LYS B1095 135.946 -72.086 37.800 1.00137.12 C ANISOU 3703 C LYS B1095 13390 20601 18108 -3029 515 -2072 C ATOM 3704 O LYS B1095 135.370 -72.248 38.873 1.00137.97 O ANISOU 3704 O LYS B1095 13447 20603 18371 -3121 816 -1957 O ATOM 3705 CB LYS B1095 135.103 -70.417 36.067 1.00136.14 C ANISOU 3705 CB LYS B1095 12704 21265 17759 -2676 -30 -2171 C ATOM 3706 CG LYS B1095 133.620 -70.423 36.452 1.00153.06 C ANISOU 3706 CG LYS B1095 14300 23695 20160 -2828 62 -2197 C ATOM 3707 CD LYS B1095 132.684 -70.267 35.246 1.00165.00 C ANISOU 3707 CD LYS B1095 15295 25741 21656 -2865 -320 -2395 C ATOM 3708 CE LYS B1095 132.228 -68.841 35.024 1.00171.80 C ANISOU 3708 CE LYS B1095 15905 26994 22378 -2366 -449 -2184 C ATOM 3709 NZ LYS B1095 131.089 -68.766 34.070 1.00181.53 N ANISOU 3709 NZ LYS B1095 16516 28819 23637 -2388 -814 -2335 N ATOM 3710 N THR B1096 136.531 -73.090 37.108 1.00135.13 N ANISOU 3710 N THR B1096 13355 20138 17852 -3224 451 -2255 N ATOM 3711 CA THR B1096 136.533 -74.514 37.471 1.00138.08 C ANISOU 3711 CA THR B1096 13931 20112 18419 -3576 722 -2352 C ATOM 3712 C THR B1096 137.368 -74.736 38.748 1.00140.92 C ANISOU 3712 C THR B1096 14713 20079 18750 -3397 1014 -2050 C ATOM 3713 O THR B1096 137.046 -75.632 39.532 1.00142.65 O ANISOU 3713 O THR B1096 15070 19992 19139 -3613 1351 -2005 O ATOM 3714 CB THR B1096 137.048 -75.378 36.287 1.00149.04 C ANISOU 3714 CB THR B1096 15518 21358 19753 -3748 586 -2626 C ATOM 3715 OG1 THR B1096 136.452 -74.935 35.061 1.00151.79 O ANISOU 3715 OG1 THR B1096 15537 22143 19992 -3809 221 -2874 O ATOM 3716 CG2 THR B1096 136.768 -76.871 36.469 1.00150.69 C ANISOU 3716 CG2 THR B1096 15907 21153 20196 -4189 890 -2803 C ATOM 3717 N THR B1097 138.428 -73.924 38.955 1.00134.79 N ANISOU 3717 N THR B1097 14143 19321 17750 -3015 884 -1847 N ATOM 3718 CA THR B1097 139.295 -74.006 40.141 1.00133.56 C ANISOU 3718 CA THR B1097 14351 18894 17501 -2812 1049 -1565 C ATOM 3719 C THR B1097 138.555 -73.406 41.347 1.00138.53 C ANISOU 3719 C THR B1097 14927 19593 18114 -2772 1241 -1396 C ATOM 3720 O THR B1097 138.617 -73.975 42.441 1.00139.44 O ANISOU 3720 O THR B1097 15319 19439 18225 -2783 1515 -1222 O ATOM 3721 CB THR B1097 140.654 -73.332 39.890 1.00138.74 C ANISOU 3721 CB THR B1097 15165 19595 17954 -2489 814 -1456 C ATOM 3722 OG1 THR B1097 141.141 -73.722 38.606 1.00138.43 O ANISOU 3722 OG1 THR B1097 15123 19546 17929 -2515 676 -1635 O ATOM 3723 CG2 THR B1097 141.692 -73.689 40.954 1.00136.90 C ANISOU 3723 CG2 THR B1097 15277 19111 17629 -2303 905 -1199 C ATOM 3724 N ARG B1098 137.835 -72.279 41.125 1.00135.18 N ANISOU 3724 N ARG B1098 14183 19514 17665 -2693 1133 -1434 N ATOM 3725 CA ARG B1098 137.031 -71.566 42.123 1.00136.44 C ANISOU 3725 CA ARG B1098 14265 19764 17813 -2616 1352 -1296 C ATOM 3726 C ARG B1098 135.921 -72.474 42.690 1.00145.62 C ANISOU 3726 C ARG B1098 15292 20801 19235 -2919 1726 -1315 C ATOM 3727 O ARG B1098 135.634 -72.417 43.890 1.00146.63 O ANISOU 3727 O ARG B1098 15608 20782 19322 -2872 2054 -1133 O ATOM 3728 CB ARG B1098 136.422 -70.297 41.499 1.00136.11 C ANISOU 3728 CB ARG B1098 13869 20106 17742 -2444 1182 -1346 C ATOM 3729 CG ARG B1098 135.777 -69.349 42.510 1.00148.26 C ANISOU 3729 CG ARG B1098 15404 21704 19223 -2262 1434 -1183 C ATOM 3730 CD ARG B1098 134.281 -69.210 42.339 1.00164.20 C ANISOU 3730 CD ARG B1098 16896 23998 21495 -2335 1588 -1234 C ATOM 3731 NE ARG B1098 133.942 -68.300 41.245 1.00176.17 N ANISOU 3731 NE ARG B1098 18060 25889 22989 -2130 1300 -1300 N ATOM 3732 CZ ARG B1098 133.567 -68.694 40.033 1.00194.57 C ANISOU 3732 CZ ARG B1098 20009 28486 25432 -2271 1010 -1492 C ATOM 3733 NH1 ARG B1098 133.279 -67.799 39.098 1.00183.38 N ANISOU 3733 NH1 ARG B1098 18331 27421 23925 -2010 748 -1502 N ATOM 3734 NH2 ARG B1098 133.468 -69.986 39.750 1.00184.16 N ANISOU 3734 NH2 ARG B1098 18613 27071 24289 -2670 992 -1676 N ATOM 3735 N ASN B1099 135.319 -73.316 41.821 1.00145.31 N ANISOU 3735 N ASN B1099 14955 20806 19449 -3255 1694 -1553 N ATOM 3736 CA ASN B1099 134.245 -74.256 42.167 1.00149.96 C ANISOU 3736 CA ASN B1099 15346 21273 20358 -3650 2052 -1636 C ATOM 3737 C ASN B1099 134.801 -75.494 42.888 1.00155.13 C ANISOU 3737 C ASN B1099 16519 21391 21033 -3788 2387 -1530 C ATOM 3738 O ASN B1099 134.121 -76.048 43.753 1.00158.45 O ANISOU 3738 O ASN B1099 16989 21591 21622 -3984 2838 -1441 O ATOM 3739 CB ASN B1099 133.462 -74.669 40.909 1.00153.32 C ANISOU 3739 CB ASN B1099 15269 21966 21021 -4007 1833 -1980 C ATOM 3740 CG ASN B1099 132.815 -73.524 40.155 1.00175.45 C ANISOU 3740 CG ASN B1099 17537 25334 23793 -3829 1492 -2053 C ATOM 3741 OD1 ASN B1099 132.530 -72.453 40.702 1.00167.84 O ANISOU 3741 OD1 ASN B1099 16462 24556 22754 -3507 1561 -1851 O ATOM 3742 ND2 ASN B1099 132.586 -73.719 38.866 1.00169.68 N ANISOU 3742 ND2 ASN B1099 16512 24877 23083 -4003 1122 -2337 N ATOM 3743 N ALA B1100 136.035 -75.915 42.538 1.00148.87 N ANISOU 3743 N ALA B1100 16114 20379 20070 -3648 2208 -1511 N ATOM 3744 CA ALA B1100 136.708 -77.064 43.145 1.00149.88 C ANISOU 3744 CA ALA B1100 16767 19998 20184 -3661 2497 -1363 C ATOM 3745 C ALA B1100 137.186 -76.761 44.561 1.00153.02 C ANISOU 3745 C ALA B1100 17566 20248 20326 -3333 2679 -996 C ATOM 3746 O ALA B1100 137.289 -77.692 45.362 1.00155.61 O ANISOU 3746 O ALA B1100 18296 20171 20659 -3360 3050 -816 O ATOM 3747 CB ALA B1100 137.885 -77.498 42.289 1.00148.63 C ANISOU 3747 CB ALA B1100 16836 19707 19930 -3535 2246 -1434 C ATOM 3748 N TYR B1101 137.504 -75.479 44.864 1.00146.11 N ANISOU 3748 N TYR B1101 16639 19679 19197 -3023 2426 -890 N ATOM 3749 CA TYR B1101 137.980 -75.005 46.172 1.00175.13 C ANISOU 3749 CA TYR B1101 20705 23287 22550 -2724 2511 -598 C ATOM 3750 C TYR B1101 137.099 -75.553 47.313 1.00218.36 C ANISOU 3750 C TYR B1101 26389 28505 28074 -2849 3058 -438 C ATOM 3751 O TYR B1101 137.530 -76.428 48.062 1.00183.96 O ANISOU 3751 O TYR B1101 22502 23792 23603 -2776 3297 -223 O ATOM 3752 CB TYR B1101 138.041 -73.455 46.193 1.00173.14 C ANISOU 3752 CB TYR B1101 20288 23400 22096 -2510 2239 -615 C ATOM 3753 CG TYR B1101 137.368 -72.791 47.378 1.00176.33 C ANISOU 3753 CG TYR B1101 20835 23821 22341 -2420 2535 -470 C ATOM 3754 CD1 TYR B1101 138.042 -72.620 48.584 1.00178.78 C ANISOU 3754 CD1 TYR B1101 21664 23997 22267 -2195 2575 -247 C ATOM 3755 CD2 TYR B1101 136.064 -72.310 47.285 1.00178.66 C ANISOU 3755 CD2 TYR B1101 20743 24291 22849 -2537 2770 -556 C ATOM 3756 CE1 TYR B1101 137.423 -72.025 49.682 1.00181.61 C ANISOU 3756 CE1 TYR B1101 22240 24338 22424 -2109 2888 -131 C ATOM 3757 CE2 TYR B1101 135.436 -71.709 48.376 1.00181.54 C ANISOU 3757 CE2 TYR B1101 21266 24637 23073 -2423 3121 -416 C ATOM 3758 CZ TYR B1101 136.122 -71.563 49.572 1.00188.90 C ANISOU 3758 CZ TYR B1101 22802 25383 23586 -2216 3195 -214 C ATOM 3759 OH TYR B1101 135.518 -70.962 50.651 1.00191.43 O ANISOU 3759 OH TYR B1101 23364 25660 23711 -2097 3570 -94 O ATOM 3760 N LEU B 44 123.626 -94.338 53.492 1.00170.75 N ANISOU 3760 N LEU B 44 18868 33776 12234 8851 -1268 2372 N ATOM 3761 CA LEU B 44 122.386 -94.679 54.185 1.00170.79 C ANISOU 3761 CA LEU B 44 19173 33561 12158 8917 -918 2763 C ATOM 3762 C LEU B 44 121.817 -95.983 53.637 1.00172.48 C ANISOU 3762 C LEU B 44 19490 33295 12748 8930 -544 3406 C ATOM 3763 O LEU B 44 121.720 -96.140 52.418 1.00171.42 O ANISOU 3763 O LEU B 44 19115 33230 12785 9035 -410 3532 O ATOM 3764 CB LEU B 44 121.339 -93.546 54.054 1.00170.37 C ANISOU 3764 CB LEU B 44 19093 33654 11986 8877 -792 2490 C ATOM 3765 CG LEU B 44 121.570 -92.256 54.853 1.00174.21 C ANISOU 3765 CG LEU B 44 19733 34010 12448 8457 -1110 1832 C ATOM 3766 CD1 LEU B 44 120.892 -91.068 54.181 1.00173.58 C ANISOU 3766 CD1 LEU B 44 19468 34132 12351 8420 -1070 1448 C ATOM 3767 CD2 LEU B 44 121.094 -92.395 56.299 1.00176.81 C ANISOU 3767 CD2 LEU B 44 20493 33995 12692 8278 -1035 1954 C ATOM 3768 N ASP B 45 121.434 -96.915 54.533 1.00170.06 N ANISOU 3768 N ASP B 45 19400 32930 12284 9170 -328 3902 N ATOM 3769 CA ASP B 45 120.836 -98.197 54.153 1.00169.05 C ANISOU 3769 CA ASP B 45 19329 32494 12409 9338 67 4573 C ATOM 3770 C ASP B 45 119.387 -97.996 53.678 1.00169.62 C ANISOU 3770 C ASP B 45 19430 32357 12661 9285 465 4787 C ATOM 3771 O ASP B 45 118.882 -98.802 52.894 1.00168.86 O ANISOU 3771 O ASP B 45 19271 32018 12870 9385 787 5260 O ATOM 3772 CB ASP B 45 120.893 -99.196 55.326 1.00171.42 C ANISOU 3772 CB ASP B 45 19981 32350 12799 9193 85 4861 C ATOM 3773 CG ASP B 45 121.728-100.445 55.055 1.00178.46 C ANISOU 3773 CG ASP B 45 21021 32453 14333 8754 -67 4969 C ATOM 3774 OD1 ASP B 45 121.519-101.085 53.994 1.00177.73 O ANISOU 3774 OD1 ASP B 45 20785 32206 14538 8866 160 5271 O ATOM 3775 OD2 ASP B 45 122.506-100.857 55.963 1.00183.97 O ANISOU 3775 OD2 ASP B 45 21981 32709 15209 8348 -378 4810 O ATOM 3776 N ALA B 46 118.730 -96.927 54.162 1.00166.24 N ANISOU 3776 N ALA B 46 18973 32394 11797 9469 509 4570 N ATOM 3777 CA ALA B 46 117.354 -96.591 53.818 1.00164.85 C ANISOU 3777 CA ALA B 46 18769 32208 11659 9555 891 4784 C ATOM 3778 C ALA B 46 117.161 -96.376 52.313 1.00161.68 C ANISOU 3778 C ALA B 46 18228 31361 11841 9145 902 4640 C ATOM 3779 O ALA B 46 116.126 -96.787 51.793 1.00159.05 O ANISOU 3779 O ALA B 46 17972 30501 11958 8938 1230 4963 O ATOM 3780 CB ALA B 46 116.923 -95.348 54.573 1.00165.81 C ANISOU 3780 CB ALA B 46 18997 32500 11504 9418 770 4295 C ATOM 3781 N ILE B 47 118.144 -95.755 51.619 1.00153.92 N ANISOU 3781 N ILE B 47 17095 30394 10994 8859 518 4100 N ATOM 3782 CA ILE B 47 118.061 -95.458 50.187 1.00147.41 C ANISOU 3782 CA ILE B 47 16208 28982 10820 8290 463 3850 C ATOM 3783 C ILE B 47 117.914 -96.761 49.351 1.00148.99 C ANISOU 3783 C ILE B 47 16434 28652 11522 8207 700 4347 C ATOM 3784 O ILE B 47 116.898 -96.847 48.664 1.00146.13 O ANISOU 3784 O ILE B 47 16140 27764 11618 7905 934 4483 O ATOM 3785 CB ILE B 47 119.216 -94.544 49.707 1.00148.72 C ANISOU 3785 CB ILE B 47 16195 29318 10992 8046 26 3204 C ATOM 3786 CG1 ILE B 47 118.902 -93.084 50.065 1.00148.92 C ANISOU 3786 CG1 ILE B 47 16213 29545 10825 7894 -130 2659 C ATOM 3787 CG2 ILE B 47 119.463 -94.668 48.190 1.00144.26 C ANISOU 3787 CG2 ILE B 47 15556 28190 11067 7572 -15 3096 C ATOM 3788 CD1 ILE B 47 120.049 -92.339 50.647 1.00158.57 C ANISOU 3788 CD1 ILE B 47 17284 31330 11636 8030 -536 2146 C ATOM 3789 N PRO B 48 118.789 -97.803 49.423 1.00146.71 N ANISOU 3789 N PRO B 48 16099 28467 11177 8482 669 4641 N ATOM 3790 CA PRO B 48 118.558 -99.005 48.594 1.00144.62 C ANISOU 3790 CA PRO B 48 15868 27641 11441 8381 910 5078 C ATOM 3791 C PRO B 48 117.202 -99.697 48.824 1.00148.00 C ANISOU 3791 C PRO B 48 16443 27716 12074 8446 1357 5626 C ATOM 3792 O PRO B 48 116.570-100.117 47.847 1.00144.00 O ANISOU 3792 O PRO B 48 15958 26605 12150 8118 1529 5751 O ATOM 3793 CB PRO B 48 119.714 -99.925 48.990 1.00149.78 C ANISOU 3793 CB PRO B 48 16455 28596 11857 8787 810 5320 C ATOM 3794 CG PRO B 48 120.793 -99.002 49.403 1.00155.41 C ANISOU 3794 CG PRO B 48 17029 29889 12129 8868 396 4797 C ATOM 3795 CD PRO B 48 120.078 -97.912 50.139 1.00151.81 C ANISOU 3795 CD PRO B 48 16639 29710 11332 8864 387 4542 C ATOM 3796 N ILE B 49 116.746 -99.789 50.097 1.00148.52 N ANISOU 3796 N ILE B 49 16598 28163 11669 8864 1543 5936 N ATOM 3797 CA ILE B 49 115.463-100.404 50.488 1.00149.81 C ANISOU 3797 CA ILE B 49 16882 28060 11978 8975 1998 6487 C ATOM 3798 C ILE B 49 114.305 -99.667 49.808 1.00150.02 C ANISOU 3798 C ILE B 49 16928 27658 12416 8505 2102 6261 C ATOM 3799 O ILE B 49 113.398-100.309 49.281 1.00148.98 O ANISOU 3799 O ILE B 49 16825 26983 12796 8323 2399 6593 O ATOM 3800 CB ILE B 49 115.295-100.424 52.042 1.00158.42 C ANISOU 3800 CB ILE B 49 18059 29751 12382 9535 2144 6786 C ATOM 3801 CG1 ILE B 49 116.392-101.281 52.755 1.00162.04 C ANISOU 3801 CG1 ILE B 49 18566 30448 12554 9866 2004 6985 C ATOM 3802 CG2 ILE B 49 113.880-100.831 52.487 1.00160.61 C ANISOU 3802 CG2 ILE B 49 18446 29785 12793 9621 2632 7305 C ATOM 3803 CD1 ILE B 49 116.601-102.787 52.290 1.00167.22 C ANISOU 3803 CD1 ILE B 49 19363 30241 13932 9512 2063 7258 C ATOM 3804 N LEU B 50 114.369 -98.324 49.800 1.00144.21 N ANISOU 3804 N LEU B 50 16160 27156 11477 8310 1845 5685 N ATOM 3805 CA LEU B 50 113.373 -97.433 49.215 1.00140.21 C ANISOU 3805 CA LEU B 50 15663 26321 11291 7891 1891 5403 C ATOM 3806 C LEU B 50 113.325 -97.542 47.697 1.00137.91 C ANISOU 3806 C LEU B 50 15313 25423 11663 7391 1818 5241 C ATOM 3807 O LEU B 50 112.264 -97.355 47.110 1.00135.27 O ANISOU 3807 O LEU B 50 14997 24659 11739 7086 1981 5259 O ATOM 3808 CB LEU B 50 113.674 -95.995 49.634 1.00140.34 C ANISOU 3808 CB LEU B 50 15653 26772 10897 7855 1601 4810 C ATOM 3809 CG LEU B 50 112.798 -95.393 50.740 1.00148.02 C ANISOU 3809 CG LEU B 50 16713 28064 11465 8091 1781 4845 C ATOM 3810 CD1 LEU B 50 112.740 -96.279 51.985 1.00153.56 C ANISOU 3810 CD1 LEU B 50 17497 29147 11702 8662 2033 5395 C ATOM 3811 CD2 LEU B 50 113.299 -94.020 51.125 1.00151.21 C ANISOU 3811 CD2 LEU B 50 17079 28900 11473 8067 1444 4200 C ATOM 3812 N TYR B 51 114.459 -97.867 47.071 1.00132.25 N ANISOU 3812 N TYR B 51 14521 24686 11040 7329 1579 5094 N ATOM 3813 CA TYR B 51 114.565 -98.037 45.626 1.00127.39 C ANISOU 3813 CA TYR B 51 13856 23549 10998 6903 1497 4938 C ATOM 3814 C TYR B 51 113.876 -99.334 45.202 1.00131.56 C ANISOU 3814 C TYR B 51 14430 23562 11996 6890 1815 5452 C ATOM 3815 O TYR B 51 113.155 -99.354 44.202 1.00127.87 O ANISOU 3815 O TYR B 51 13961 22586 12038 6520 1887 5402 O ATOM 3816 CB TYR B 51 116.043 -98.008 45.201 1.00127.51 C ANISOU 3816 CB TYR B 51 13767 23757 10923 6895 1166 4640 C ATOM 3817 CG TYR B 51 116.566 -96.607 44.954 1.00126.58 C ANISOU 3817 CG TYR B 51 13568 23865 10662 6652 840 4018 C ATOM 3818 CD1 TYR B 51 116.420 -95.605 45.910 1.00130.27 C ANISOU 3818 CD1 TYR B 51 14045 24763 10691 6781 754 3774 C ATOM 3819 CD2 TYR B 51 117.230 -96.288 43.771 1.00123.74 C ANISOU 3819 CD2 TYR B 51 13118 23285 10611 6303 626 3671 C ATOM 3820 CE1 TYR B 51 116.874 -94.309 45.676 1.00129.40 C ANISOU 3820 CE1 TYR B 51 13851 24809 10506 6541 466 3194 C ATOM 3821 CE2 TYR B 51 117.704 -94.999 43.533 1.00122.92 C ANISOU 3821 CE2 TYR B 51 12929 23352 10423 6070 354 3126 C ATOM 3822 CZ TYR B 51 117.530 -94.016 44.492 1.00131.01 C ANISOU 3822 CZ TYR B 51 13957 24765 11055 6183 271 2885 C ATOM 3823 OH TYR B 51 117.998 -92.748 44.262 1.00128.77 O ANISOU 3823 OH TYR B 51 13579 24611 10735 5944 10 2340 O ATOM 3824 N TYR B 52 114.027-100.387 46.017 1.00132.44 N ANISOU 3824 N TYR B 52 14579 23809 11934 7305 2015 5952 N ATOM 3825 CA TYR B 52 113.404-101.675 45.754 1.00133.18 C ANISOU 3825 CA TYR B 52 14707 23415 12479 7333 2342 6474 C ATOM 3826 C TYR B 52 111.914-101.670 46.094 1.00137.79 C ANISOU 3826 C TYR B 52 15340 23767 13248 7282 2687 6760 C ATOM 3827 O TYR B 52 111.134-102.192 45.301 1.00135.68 O ANISOU 3827 O TYR B 52 15059 22932 13562 7009 2856 6902 O ATOM 3828 CB TYR B 52 114.121-102.793 46.520 1.00138.58 C ANISOU 3828 CB TYR B 52 15410 24314 12928 7814 2451 6936 C ATOM 3829 N ILE B 53 111.506-101.126 47.256 1.00137.48 N ANISOU 3829 N ILE B 53 15348 24155 12733 7549 2798 6847 N ATOM 3830 CA ILE B 53 110.087-101.146 47.646 1.00138.93 C ANISOU 3830 CA ILE B 53 15563 24142 13082 7533 3161 7154 C ATOM 3831 C ILE B 53 109.204-100.454 46.591 1.00139.33 C ANISOU 3831 C ILE B 53 15566 23751 13621 7015 3113 6818 C ATOM 3832 O ILE B 53 108.099-100.934 46.341 1.00139.14 O ANISOU 3832 O ILE B 53 15522 23291 14055 6874 3402 7110 O ATOM 3833 CB ILE B 53 109.790-100.606 49.076 1.00145.89 C ANISOU 3833 CB ILE B 53 16510 25593 13330 7925 3294 7274 C ATOM 3834 CG1 ILE B 53 110.319 -99.177 49.297 1.00145.05 C ANISOU 3834 CG1 ILE B 53 16400 25966 12747 7879 2933 6649 C ATOM 3835 CG2 ILE B 53 110.295-101.569 50.154 1.00151.63 C ANISOU 3835 CG2 ILE B 53 17293 26659 13661 8477 3475 7802 C ATOM 3836 CD1 ILE B 53 109.278 -98.162 49.528 1.00153.09 C ANISOU 3836 CD1 ILE B 53 17435 27010 13722 7742 3027 6452 C ATOM 3837 N ILE B 54 109.711 -99.390 45.927 1.00132.65 N ANISOU 3837 N ILE B 54 14691 22993 12717 6731 2751 6224 N ATOM 3838 CA ILE B 54 108.918 -98.685 44.916 1.00128.52 C ANISOU 3838 CA ILE B 54 14128 22081 12622 6267 2690 5910 C ATOM 3839 C ILE B 54 109.081 -99.352 43.543 1.00128.67 C ANISOU 3839 C ILE B 54 14104 21570 13215 5944 2607 5866 C ATOM 3840 O ILE B 54 108.318 -99.043 42.623 1.00125.59 O ANISOU 3840 O ILE B 54 13679 20786 13252 5578 2595 5701 O ATOM 3841 CB ILE B 54 109.178 -97.148 44.845 1.00129.60 C ANISOU 3841 CB ILE B 54 14259 22509 12475 6101 2394 5324 C ATOM 3842 CG1 ILE B 54 110.475 -96.808 44.110 1.00127.79 C ANISOU 3842 CG1 ILE B 54 13989 22367 12198 5949 2018 4902 C ATOM 3843 CG2 ILE B 54 109.108 -96.454 46.206 1.00133.74 C ANISOU 3843 CG2 ILE B 54 14829 23586 12399 6436 2440 5294 C ATOM 3844 CD1 ILE B 54 110.216 -96.152 42.815 1.00132.05 C ANISOU 3844 CD1 ILE B 54 14491 22534 13147 5484 1859 4537 C ATOM 3845 N PHE B 55 110.080-100.231 43.397 1.00125.19 N ANISOU 3845 N PHE B 55 13662 21135 12768 6093 2537 5992 N ATOM 3846 CA PHE B 55 110.302-100.934 42.145 1.00122.53 C ANISOU 3846 CA PHE B 55 13293 20321 12941 5834 2466 5946 C ATOM 3847 C PHE B 55 109.182-101.944 41.949 1.00129.02 C ANISOU 3847 C PHE B 55 14104 20626 14293 5769 2796 6368 C ATOM 3848 O PHE B 55 108.459-101.849 40.962 1.00126.31 O ANISOU 3848 O PHE B 55 13723 19856 14415 5409 2779 6214 O ATOM 3849 CB PHE B 55 111.698-101.597 42.118 1.00124.98 C ANISOU 3849 CB PHE B 55 13598 20801 13086 6047 2316 5970 C ATOM 3850 CG PHE B 55 111.860-102.837 41.266 1.00125.95 C ANISOU 3850 CG PHE B 55 13709 20441 13704 5972 2390 6161 C ATOM 3851 CD1 PHE B 55 111.921-102.747 39.880 1.00125.39 C ANISOU 3851 CD1 PHE B 55 13611 20001 14030 5593 2220 5830 C ATOM 3852 CD2 PHE B 55 111.982-104.092 41.852 1.00131.08 C ANISOU 3852 CD2 PHE B 55 14380 21012 14411 6301 2630 6669 C ATOM 3853 CE1 PHE B 55 112.083-103.892 39.094 1.00126.29 C ANISOU 3853 CE1 PHE B 55 13719 19678 14589 5538 2278 5967 C ATOM 3854 CE2 PHE B 55 112.143-105.236 41.065 1.00133.92 C ANISOU 3854 CE2 PHE B 55 14729 20899 15256 6234 2697 6819 C ATOM 3855 CZ PHE B 55 112.196-105.128 39.694 1.00128.62 C ANISOU 3855 CZ PHE B 55 14031 19871 14969 5853 2514 6448 C ATOM 3856 N VAL B 56 109.011-102.869 42.912 1.00130.56 N ANISOU 3856 N VAL B 56 14323 20870 14415 6123 3096 6899 N ATOM 3857 CA VAL B 56 108.023-103.951 42.868 1.00132.53 C ANISOU 3857 CA VAL B 56 14543 20625 15187 6106 3451 7365 C ATOM 3858 C VAL B 56 106.595-103.408 42.757 1.00136.03 C ANISOU 3858 C VAL B 56 14935 20844 15907 5853 3608 7345 C ATOM 3859 O VAL B 56 105.802-103.942 41.978 1.00135.16 O ANISOU 3859 O VAL B 56 14756 20195 16405 5582 3714 7414 O ATOM 3860 CB VAL B 56 108.167-104.928 44.058 1.00141.25 C ANISOU 3860 CB VAL B 56 15687 21890 16092 6579 3765 7969 C ATOM 3861 CG1 VAL B 56 109.341-105.875 43.835 1.00142.10 C ANISOU 3861 CG1 VAL B 56 15815 21959 16219 6760 3672 8076 C ATOM 3862 CG2 VAL B 56 108.303-104.192 45.393 1.00143.33 C ANISOU 3862 CG2 VAL B 56 16008 22805 15644 6937 3802 8035 C ATOM 3863 N ILE B 57 106.294-102.331 43.498 1.00132.52 N ANISOU 3863 N ILE B 57 14513 20813 15026 5940 3601 7216 N ATOM 3864 CA ILE B 57 104.990-101.673 43.514 1.00131.62 C ANISOU 3864 CA ILE B 57 14346 20567 15094 5746 3743 7179 C ATOM 3865 C ILE B 57 104.682-101.126 42.117 1.00131.44 C ANISOU 3865 C ILE B 57 14267 20186 15490 5268 3490 6725 C ATOM 3866 O ILE B 57 103.633-101.452 41.554 1.00130.27 O ANISOU 3866 O ILE B 57 14032 19583 15883 5026 3630 6824 O ATOM 3867 CB ILE B 57 104.963-100.574 44.624 1.00135.79 C ANISOU 3867 CB ILE B 57 14930 21678 14986 5983 3745 7070 C ATOM 3868 CG1 ILE B 57 104.882-101.184 46.051 1.00141.21 C ANISOU 3868 CG1 ILE B 57 15667 22679 15309 6471 4088 7612 C ATOM 3869 CG2 ILE B 57 103.874 -99.507 44.407 1.00134.91 C ANISOU 3869 CG2 ILE B 57 14769 21488 15002 5725 3755 6818 C ATOM 3870 CD1 ILE B 57 103.639-102.109 46.394 1.00151.33 C ANISOU 3870 CD1 ILE B 57 16882 23587 17030 6525 4572 8204 C ATOM 3871 N GLY B 58 105.616-100.328 41.587 1.00125.91 N ANISOU 3871 N GLY B 58 13605 19700 14534 5150 3124 6247 N ATOM 3872 CA GLY B 58 105.540 -99.704 40.271 1.00121.84 C ANISOU 3872 CA GLY B 58 13058 18928 14307 4740 2854 5798 C ATOM 3873 C GLY B 58 105.427-100.693 39.131 1.00124.80 C ANISOU 3873 C GLY B 58 13388 18773 15256 4515 2838 5844 C ATOM 3874 O GLY B 58 104.762-100.412 38.133 1.00121.94 O ANISOU 3874 O GLY B 58 12975 18084 15273 4183 2744 5626 O ATOM 3875 N PHE B 59 106.085-101.851 39.271 1.00123.72 N ANISOU 3875 N PHE B 59 13273 18556 15178 4710 2921 6115 N ATOM 3876 CA PHE B 59 106.049-102.920 38.283 1.00123.81 C ANISOU 3876 CA PHE B 59 13249 18060 15733 4543 2926 6170 C ATOM 3877 C PHE B 59 104.710-103.616 38.338 1.00129.82 C ANISOU 3877 C PHE B 59 13921 18383 17020 4456 3228 6506 C ATOM 3878 O PHE B 59 104.156-103.945 37.293 1.00128.14 O ANISOU 3878 O PHE B 59 13642 17719 17325 4159 3170 6371 O ATOM 3879 CB PHE B 59 107.188-103.913 38.524 1.00128.01 C ANISOU 3879 CB PHE B 59 13830 18656 16153 4817 2939 6370 C ATOM 3880 CG PHE B 59 107.950-104.273 37.271 1.00128.13 C ANISOU 3880 CG PHE B 59 13853 18434 16399 4630 2696 6069 C ATOM 3881 CD1 PHE B 59 108.965-103.449 36.791 1.00129.17 C ANISOU 3881 CD1 PHE B 59 14017 18865 16198 4560 2378 5646 C ATOM 3882 CD2 PHE B 59 107.658-105.438 36.571 1.00131.96 C ANISOU 3882 CD2 PHE B 59 14304 18390 17444 4528 2794 6204 C ATOM 3883 CE1 PHE B 59 109.668-103.781 35.626 1.00128.56 C ANISOU 3883 CE1 PHE B 59 13946 18584 16317 4405 2179 5381 C ATOM 3884 CE2 PHE B 59 108.365-105.771 35.408 1.00133.40 C ANISOU 3884 CE2 PHE B 59 14503 18370 17813 4377 2574 5906 C ATOM 3885 CZ PHE B 59 109.362-104.938 34.941 1.00128.73 C ANISOU 3885 CZ PHE B 59 13951 18104 16857 4324 2276 5507 C ATOM 3886 N LEU B 60 104.177-103.803 39.561 1.00129.76 N ANISOU 3886 N LEU B 60 13903 18528 16873 4719 3550 6932 N ATOM 3887 CA LEU B 60 102.884-104.428 39.790 1.00132.16 C ANISOU 3887 CA LEU B 60 14099 18453 17663 4667 3891 7306 C ATOM 3888 C LEU B 60 101.750-103.557 39.244 1.00133.67 C ANISOU 3888 C LEU B 60 14194 18496 18098 4338 3829 7044 C ATOM 3889 O LEU B 60 100.938-104.074 38.475 1.00133.51 O ANISOU 3889 O LEU B 60 14058 17983 18686 4075 3872 7050 O ATOM 3890 CB LEU B 60 102.660-104.738 41.283 1.00136.52 C ANISOU 3890 CB LEU B 60 14671 19273 17928 5065 4266 7837 C ATOM 3891 CG LEU B 60 103.225-106.067 41.820 1.00145.07 C ANISOU 3891 CG LEU B 60 15789 20260 19070 5378 4495 8320 C ATOM 3892 CD1 LEU B 60 103.020-106.176 43.316 1.00149.55 C ANISOU 3892 CD1 LEU B 60 16394 21184 19245 5798 4847 8824 C ATOM 3893 CD2 LEU B 60 102.582-107.275 41.147 1.00148.85 C ANISOU 3893 CD2 LEU B 60 16158 20054 20345 5181 4677 8544 C ATOM 3894 N VAL B 61 101.683-102.251 39.604 1.00127.99 N ANISOU 3894 N VAL B 61 13513 18181 16936 4349 3716 6798 N ATOM 3895 CA VAL B 61 100.606-101.359 39.123 1.00125.60 C ANISOU 3895 CA VAL B 61 13119 17756 16846 4065 3660 6559 C ATOM 3896 C VAL B 61 100.656-101.176 37.574 1.00125.44 C ANISOU 3896 C VAL B 61 13070 17419 17172 3684 3324 6123 C ATOM 3897 O VAL B 61 99.595-101.123 36.949 1.00124.28 O ANISOU 3897 O VAL B 61 12800 16941 17481 3427 3335 6062 O ATOM 3898 CB VAL B 61 100.505 -99.982 39.855 1.00128.46 C ANISOU 3898 CB VAL B 61 13532 18595 16681 4172 3624 6382 C ATOM 3899 CG1 VAL B 61 99.985-100.147 41.278 1.00132.09 C ANISOU 3899 CG1 VAL B 61 13984 19291 16915 4503 4009 6825 C ATOM 3900 CG2 VAL B 61 101.822 -99.206 39.840 1.00126.06 C ANISOU 3900 CG2 VAL B 61 13361 18709 15827 4249 3307 6014 C ATOM 3901 N ASN B 62 101.867-101.126 36.966 1.00119.69 N ANISOU 3901 N ASN B 62 12443 16797 16236 3663 3038 5838 N ATOM 3902 CA ASN B 62 102.024-100.962 35.517 1.00116.33 C ANISOU 3902 CA ASN B 62 12011 16122 16067 3346 2731 5438 C ATOM 3903 C ASN B 62 101.832-102.280 34.751 1.00121.89 C ANISOU 3903 C ASN B 62 12652 16322 17336 3228 2772 5548 C ATOM 3904 O ASN B 62 101.452-102.222 33.580 1.00119.99 O ANISOU 3904 O ASN B 62 12364 15796 17432 2943 2582 5269 O ATOM 3905 CB ASN B 62 103.359-100.326 35.155 1.00113.26 C ANISOU 3905 CB ASN B 62 11740 16050 15245 3365 2433 5090 C ATOM 3906 CG ASN B 62 103.361 -98.826 35.299 1.00130.21 C ANISOU 3906 CG ASN B 62 13918 18534 17021 3309 2284 4795 C ATOM 3907 OD1 ASN B 62 102.858 -98.089 34.442 1.00121.53 O ANISOU 3907 OD1 ASN B 62 12789 17307 16079 3047 2122 4514 O ATOM 3908 ND2 ASN B 62 103.929 -98.338 36.387 1.00122.25 N ANISOU 3908 ND2 ASN B 62 12968 17963 15516 3563 2329 4846 N ATOM 3909 N ILE B 63 102.065-103.457 35.389 1.00121.56 N ANISOU 3909 N ILE B 63 12610 16164 17412 3450 3017 5945 N ATOM 3910 CA ILE B 63 101.816-104.730 34.708 1.00123.09 C ANISOU 3910 CA ILE B 63 12735 15833 18202 3335 3079 6048 C ATOM 3911 C ILE B 63 100.297-104.965 34.717 1.00129.51 C ANISOU 3911 C ILE B 63 13372 16281 19553 3162 3285 6225 C ATOM 3912 O ILE B 63 99.795-105.651 33.833 1.00129.07 O ANISOU 3912 O ILE B 63 13219 15762 20060 2937 3237 6135 O ATOM 3913 CB ILE B 63 102.644-105.948 35.234 1.00129.16 C ANISOU 3913 CB ILE B 63 13560 16538 18976 3617 3253 6390 C ATOM 3914 CG1 ILE B 63 102.743-107.084 34.181 1.00130.23 C ANISOU 3914 CG1 ILE B 63 13660 16149 19671 3460 3185 6300 C ATOM 3915 CG2 ILE B 63 102.160-106.478 36.585 1.00133.86 C ANISOU 3915 CG2 ILE B 63 14115 17171 19574 3893 3666 6960 C ATOM 3916 CD1 ILE B 63 103.894-106.961 33.167 1.00132.07 C ANISOU 3916 CD1 ILE B 63 13999 16461 19720 3394 2844 5876 C ATOM 3917 N VAL B 64 99.572-104.333 35.675 1.00128.66 N ANISOU 3917 N VAL B 64 13216 16399 19268 3260 3495 6436 N ATOM 3918 CA VAL B 64 98.112-104.381 35.788 1.00131.10 C ANISOU 3918 CA VAL B 64 13339 16434 20041 3112 3707 6607 C ATOM 3919 C VAL B 64 97.495-103.579 34.616 1.00134.33 C ANISOU 3919 C VAL B 64 13671 16715 20652 2763 3399 6147 C ATOM 3920 O VAL B 64 96.542-104.060 34.005 1.00135.63 O ANISOU 3920 O VAL B 64 13664 16455 21412 2534 3420 6135 O ATOM 3921 CB VAL B 64 97.633-103.897 37.189 1.00136.82 C ANISOU 3921 CB VAL B 64 14051 17495 20441 3364 4029 6961 C ATOM 3922 CG1 VAL B 64 96.226-103.306 37.160 1.00136.89 C ANISOU 3922 CG1 VAL B 64 13883 17389 20742 3179 4129 6949 C ATOM 3923 CG2 VAL B 64 97.711-105.030 38.204 1.00141.00 C ANISOU 3923 CG2 VAL B 64 14573 17947 21055 3654 4425 7530 C ATOM 3924 N VAL B 65 98.090-102.410 34.269 1.00128.53 N ANISOU 3924 N VAL B 65 13059 16334 19442 2728 3107 5768 N ATOM 3925 CA VAL B 65 97.661-101.529 33.169 1.00126.01 C ANISOU 3925 CA VAL B 65 12703 15959 19217 2441 2802 5340 C ATOM 3926 C VAL B 65 97.800-102.267 31.820 1.00131.28 C ANISOU 3926 C VAL B 65 13345 16241 20295 2217 2569 5092 C ATOM 3927 O VAL B 65 96.814-102.359 31.087 1.00131.55 O ANISOU 3927 O VAL B 65 13229 15965 20790 1982 2494 4972 O ATOM 3928 CB VAL B 65 98.416-100.166 33.170 1.00126.34 C ANISOU 3928 CB VAL B 65 12894 16457 18653 2483 2574 5031 C ATOM 3929 CG1 VAL B 65 98.094 -99.344 31.924 1.00123.26 C ANISOU 3929 CG1 VAL B 65 12483 15983 18368 2203 2258 4613 C ATOM 3930 CG2 VAL B 65 98.089 -99.363 34.419 1.00126.88 C ANISOU 3930 CG2 VAL B 65 12968 16876 18364 2678 2782 5208 C ATOM 3931 N VAL B 66 99.003-102.811 31.516 1.00128.48 N ANISOU 3931 N VAL B 66 13126 15914 19778 2305 2457 5011 N ATOM 3932 CA VAL B 66 99.301-103.563 30.284 1.00128.59 C ANISOU 3932 CA VAL B 66 13145 15596 20118 2141 2246 4763 C ATOM 3933 C VAL B 66 98.342-104.765 30.164 1.00137.91 C ANISOU 3933 C VAL B 66 14147 16255 21996 2036 2422 4963 C ATOM 3934 O VAL B 66 97.848-105.042 29.066 1.00137.66 O ANISOU 3934 O VAL B 66 14031 15906 22368 1798 2229 4692 O ATOM 3935 CB VAL B 66 100.794-104.014 30.210 1.00131.57 C ANISOU 3935 CB VAL B 66 13689 16115 20188 2314 2166 4715 C ATOM 3936 CG1 VAL B 66 101.080-104.829 28.949 1.00131.34 C ANISOU 3936 CG1 VAL B 66 13668 15737 20498 2166 1971 4452 C ATOM 3937 CG2 VAL B 66 101.740-102.820 30.287 1.00128.19 C ANISOU 3937 CG2 VAL B 66 13400 16178 19127 2389 1984 4495 C ATOM 3938 N THR B 67 98.046-105.441 31.292 1.00138.92 N ANISOU 3938 N THR B 67 14211 16303 22270 2213 2790 5431 N ATOM 3939 CA THR B 67 97.167-106.601 31.251 1.00143.22 C ANISOU 3939 CA THR B 67 14570 16328 23520 2114 2995 5655 C ATOM 3940 C THR B 67 95.708-106.207 31.107 1.00150.05 C ANISOU 3940 C THR B 67 15213 17021 24777 1893 3032 5635 C ATOM 3941 O THR B 67 95.013-106.855 30.331 1.00151.66 O ANISOU 3941 O THR B 67 15255 16785 25585 1666 2959 5506 O ATOM 3942 CB THR B 67 97.360-107.513 32.459 1.00154.20 C ANISOU 3942 CB THR B 67 15962 17659 24967 2387 3401 6200 C ATOM 3943 OG1 THR B 67 97.350-106.736 33.660 1.00153.12 O ANISOU 3943 OG1 THR B 67 15877 17972 24330 2614 3601 6467 O ATOM 3944 CG2 THR B 67 98.632-108.349 32.364 1.00153.57 C ANISOU 3944 CG2 THR B 67 16039 17545 24767 2564 3368 6229 C ATOM 3945 N LEU B 68 95.234-105.167 31.822 1.00146.87 N ANISOU 3945 N LEU B 68 14791 16955 24059 1959 3134 5738 N ATOM 3946 CA LEU B 68 93.826-104.811 31.710 1.00148.20 C ANISOU 3946 CA LEU B 68 14727 16959 24622 1765 3186 5738 C ATOM 3947 C LEU B 68 93.538-104.244 30.314 1.00150.28 C ANISOU 3947 C LEU B 68 14953 17143 25003 1485 2764 5222 C ATOM 3948 O LEU B 68 92.508-104.593 29.740 1.00151.48 O ANISOU 3948 O LEU B 68 14882 16941 25731 1263 2719 5140 O ATOM 3949 CB LEU B 68 93.330-103.906 32.851 1.00148.57 C ANISOU 3949 CB LEU B 68 14752 17360 24339 1926 3432 5991 C ATOM 3950 CG LEU B 68 93.689-102.427 32.884 1.00150.01 C ANISOU 3950 CG LEU B 68 15080 18023 23894 1976 3229 5724 C ATOM 3951 CD1 LEU B 68 92.544-101.598 32.310 1.00149.63 C ANISOU 3951 CD1 LEU B 68 14862 17911 24079 1751 3091 5502 C ATOM 3952 CD2 LEU B 68 93.896-101.972 34.316 1.00153.72 C ANISOU 3952 CD2 LEU B 68 15637 18894 23876 2282 3525 6046 C ATOM 3953 N PHE B 69 94.488-103.476 29.732 1.00144.09 N ANISOU 3953 N PHE B 69 14379 16664 23705 1501 2456 4880 N ATOM 3954 CA PHE B 69 94.385-102.938 28.370 1.00141.92 C ANISOU 3954 CA PHE B 69 14109 16355 23459 1278 2055 4407 C ATOM 3955 C PHE B 69 94.346-104.080 27.351 1.00147.71 C ANISOU 3955 C PHE B 69 14774 16652 24698 1117 1901 4220 C ATOM 3956 O PHE B 69 93.711-103.953 26.303 1.00147.73 O ANISOU 3956 O PHE B 69 14668 16486 24976 902 1639 3906 O ATOM 3957 CB PHE B 69 95.554-101.990 28.057 1.00139.90 C ANISOU 3957 CB PHE B 69 14100 16507 22550 1360 1820 4146 C ATOM 3958 N CYS B 70 95.004-105.201 27.684 1.00145.35 N ANISOU 3958 N CYS B 70 14532 16172 24524 1238 2067 4414 N ATOM 3959 CA CYS B 70 95.047-106.397 26.857 1.00166.43 C ANISOU 3959 CA CYS B 70 17146 18398 27691 1118 1967 4260 C ATOM 3960 C CYS B 70 93.718-107.127 26.931 1.00185.37 C ANISOU 3960 C CYS B 70 19251 20341 30840 948 2126 4407 C ATOM 3961 O CYS B 70 93.172-107.502 25.895 1.00143.84 O ANISOU 3961 O CYS B 70 13860 14771 26021 725 1891 4087 O ATOM 3962 CB CYS B 70 96.199-107.296 27.283 1.00167.64 C ANISOU 3962 CB CYS B 70 17456 18513 27726 1331 2119 4450 C ATOM 3963 SG CYS B 70 97.562-107.346 26.089 1.00168.90 S ANISOU 3963 SG CYS B 70 17849 18781 27546 1344 1755 3995 S ATOM 3964 N LYS B 77 90.843 -97.291 21.430 1.00113.27 N ANISOU 3964 N LYS B 77 10201 13091 19747 305 -54 2273 N ATOM 3965 CA LYS B 77 90.808 -95.831 21.454 1.00110.62 C ANISOU 3965 CA LYS B 77 9949 13052 19031 361 -109 2249 C ATOM 3966 C LYS B 77 92.213 -95.232 21.387 1.00111.70 C ANISOU 3966 C LYS B 77 10388 13467 18587 470 -143 2176 C ATOM 3967 O LYS B 77 93.179 -95.865 21.812 1.00110.99 O ANISOU 3967 O LYS B 77 10425 13391 18355 546 -15 2253 O ATOM 3968 CB LYS B 77 90.080 -95.328 22.708 1.00113.63 C ANISOU 3968 CB LYS B 77 10196 13490 19487 428 195 2543 C ATOM 3969 N VAL B 78 92.313 -94.002 20.855 1.00106.75 N ANISOU 3969 N VAL B 78 9860 13052 17647 480 -309 2039 N ATOM 3970 CA VAL B 78 93.552 -93.226 20.697 1.00103.73 C ANISOU 3970 CA VAL B 78 9734 12932 16746 559 -353 1956 C ATOM 3971 C VAL B 78 94.205 -92.952 22.061 1.00106.28 C ANISOU 3971 C VAL B 78 10141 13424 16815 687 -63 2168 C ATOM 3972 O VAL B 78 95.408 -93.169 22.211 1.00104.49 O ANISOU 3972 O VAL B 78 10080 13315 16307 757 -28 2152 O ATOM 3973 CB VAL B 78 93.322 -91.909 19.909 1.00106.41 C ANISOU 3973 CB VAL B 78 10126 13422 16884 540 -555 1810 C ATOM 3974 CG1 VAL B 78 93.316 -92.170 18.409 1.00106.84 C ANISOU 3974 CG1 VAL B 78 10212 13419 16964 470 -875 1558 C ATOM 3975 CG2 VAL B 78 92.033 -91.200 20.336 1.00107.16 C ANISOU 3975 CG2 VAL B 78 10033 13488 17195 529 -494 1918 C ATOM 3976 N SER B 79 93.386 -92.521 23.053 1.00103.45 N ANISOU 3976 N SER B 79 9657 13085 16564 730 140 2359 N ATOM 3977 CA SER B 79 93.783 -92.233 24.436 1.00102.47 C ANISOU 3977 CA SER B 79 9586 13138 16210 874 421 2560 C ATOM 3978 C SER B 79 94.381 -93.473 25.081 1.00104.90 C ANISOU 3978 C SER B 79 9916 13381 16559 949 597 2726 C ATOM 3979 O SER B 79 95.379 -93.354 25.783 1.00103.72 O ANISOU 3979 O SER B 79 9908 13438 16063 1078 707 2785 O ATOM 3980 CB SER B 79 92.586 -91.753 25.258 1.00108.30 C ANISOU 3980 CB SER B 79 10151 13864 17134 907 609 2731 C ATOM 3981 OG SER B 79 91.865 -90.699 24.637 1.00118.24 O ANISOU 3981 OG SER B 79 11355 15139 18434 843 450 2599 O ATOM 3982 N SER B 80 93.792 -94.665 24.799 1.00101.35 N ANISOU 3982 N SER B 80 9321 12639 16551 870 609 2788 N ATOM 3983 CA SER B 80 94.220 -95.970 25.313 1.00101.24 C ANISOU 3983 CA SER B 80 9303 12485 16679 933 782 2967 C ATOM 3984 C SER B 80 95.549 -96.416 24.702 1.00100.33 C ANISOU 3984 C SER B 80 9378 12417 16325 958 635 2804 C ATOM 3985 O SER B 80 96.282 -97.181 25.335 1.00100.50 O ANISOU 3985 O SER B 80 9463 12445 16275 1077 796 2963 O ATOM 3986 CB SER B 80 93.148 -97.025 25.058 1.00107.38 C ANISOU 3986 CB SER B 80 9850 12891 18058 812 816 3040 C ATOM 3987 OG SER B 80 91.952 -96.714 25.755 1.00116.83 O ANISOU 3987 OG SER B 80 10846 14045 19499 807 1005 3237 O ATOM 3988 N ILE B 81 95.865 -95.932 23.484 1.00 92.47 N ANISOU 3988 N ILE B 81 8472 11467 15197 865 343 2505 N ATOM 3989 CA ILE B 81 97.119 -96.263 22.806 1.00 89.58 C ANISOU 3989 CA ILE B 81 8281 11165 14590 891 203 2333 C ATOM 3990 C ILE B 81 98.267 -95.497 23.488 1.00 87.73 C ANISOU 3990 C ILE B 81 8210 11266 13858 1026 289 2375 C ATOM 3991 O ILE B 81 99.365 -96.043 23.588 1.00 87.32 O ANISOU 3991 O ILE B 81 8263 11279 13633 1115 317 2378 O ATOM 3992 CB ILE B 81 97.036 -96.030 21.264 1.00 91.95 C ANISOU 3992 CB ILE B 81 8617 11415 14903 765 -119 2015 C ATOM 3993 CG1 ILE B 81 95.961 -96.934 20.591 1.00 94.99 C ANISOU 3993 CG1 ILE B 81 8826 11467 15801 637 -234 1931 C ATOM 3994 CG2 ILE B 81 98.392 -96.182 20.556 1.00 90.58 C ANISOU 3994 CG2 ILE B 81 8637 11362 14417 811 -242 1837 C ATOM 3995 CD1 ILE B 81 95.852 -98.440 21.081 1.00107.63 C ANISOU 3995 CD1 ILE B 81 10325 12765 17804 646 -64 2079 C ATOM 3996 N TYR B 82 98.004 -94.284 24.015 1.00 80.76 N ANISOU 3996 N TYR B 82 7330 10584 12772 1049 338 2405 N ATOM 3997 CA TYR B 82 99.028 -93.528 24.735 1.00 78.29 C ANISOU 3997 CA TYR B 82 7144 10579 12022 1169 412 2417 C ATOM 3998 C TYR B 82 99.249 -94.129 26.134 1.00 84.25 C ANISOU 3998 C TYR B 82 7880 11410 12723 1340 677 2684 C ATOM 3999 O TYR B 82 100.383 -94.096 26.619 1.00 84.19 O ANISOU 3999 O TYR B 82 7976 11619 12391 1462 713 2689 O ATOM 4000 CB TYR B 82 98.713 -92.018 24.831 1.00 77.31 C ANISOU 4000 CB TYR B 82 7035 10625 11714 1143 373 2331 C ATOM 4001 CG TYR B 82 98.569 -91.296 23.508 1.00 76.90 C ANISOU 4001 CG TYR B 82 7020 10535 11662 1009 129 2106 C ATOM 4002 CD1 TYR B 82 99.644 -91.187 22.629 1.00 77.55 C ANISOU 4002 CD1 TYR B 82 7237 10702 11528 983 -26 1930 C ATOM 4003 CD2 TYR B 82 97.383 -90.645 23.172 1.00 78.01 C ANISOU 4003 CD2 TYR B 82 7061 10584 11994 931 68 2086 C ATOM 4004 CE1 TYR B 82 99.519 -90.515 21.415 1.00 77.77 C ANISOU 4004 CE1 TYR B 82 7309 10715 11526 887 -229 1756 C ATOM 4005 CE2 TYR B 82 97.249 -89.953 21.972 1.00 78.08 C ANISOU 4005 CE2 TYR B 82 7111 10581 11975 840 -154 1907 C ATOM 4006 CZ TYR B 82 98.320 -89.886 21.096 1.00 83.82 C ANISOU 4006 CZ TYR B 82 7984 11391 12472 821 -297 1750 C ATOM 4007 OH TYR B 82 98.176 -89.202 19.912 1.00 81.50 O ANISOU 4007 OH TYR B 82 7739 11100 12128 755 -496 1606 O ATOM 4008 N ILE B 83 98.186 -94.709 26.763 1.00 82.61 N ANISOU 4008 N ILE B 83 7526 11029 12832 1359 865 2914 N ATOM 4009 CA ILE B 83 98.274 -95.363 28.088 1.00 84.18 C ANISOU 4009 CA ILE B 83 7701 11285 13000 1542 1150 3222 C ATOM 4010 C ILE B 83 99.242 -96.547 28.013 1.00 88.16 C ANISOU 4010 C ILE B 83 8272 11718 13505 1622 1165 3284 C ATOM 4011 O ILE B 83 100.110 -96.668 28.876 1.00 87.47 O ANISOU 4011 O ILE B 83 8267 11855 13113 1810 1281 3409 O ATOM 4012 CB ILE B 83 96.920 -95.832 28.710 1.00 89.63 C ANISOU 4012 CB ILE B 83 8205 11772 14079 1542 1381 3491 C ATOM 4013 CG1 ILE B 83 95.741 -94.849 28.466 1.00 89.84 C ANISOU 4013 CG1 ILE B 83 8116 11769 14250 1425 1331 3405 C ATOM 4014 CG2 ILE B 83 97.083 -96.149 30.208 1.00 91.52 C ANISOU 4014 CG2 ILE B 83 8452 12179 14144 1779 1698 3821 C ATOM 4015 CD1 ILE B 83 95.650 -93.590 29.301 1.00 96.28 C ANISOU 4015 CD1 ILE B 83 8972 12881 14729 1532 1423 3409 C ATOM 4016 N PHE B 84 99.097 -97.403 26.977 1.00 85.47 N ANISOU 4016 N PHE B 84 7895 11076 13502 1491 1037 3181 N ATOM 4017 CA PHE B 84 99.960 -98.562 26.758 1.00 86.33 C ANISOU 4017 CA PHE B 84 8066 11067 13669 1557 1039 3207 C ATOM 4018 C PHE B 84 101.427 -98.144 26.665 1.00 88.25 C ANISOU 4018 C PHE B 84 8474 11613 13444 1656 929 3060 C ATOM 4019 O PHE B 84 102.267 -98.681 27.396 1.00 89.30 O ANISOU 4019 O PHE B 84 8660 11864 13408 1840 1055 3222 O ATOM 4020 CB PHE B 84 99.545 -99.321 25.487 1.00 88.99 C ANISOU 4020 CB PHE B 84 8346 11051 14415 1381 863 3017 C ATOM 4021 CG PHE B 84 100.434-100.499 25.165 1.00 91.75 C ANISOU 4021 CG PHE B 84 8764 11254 14843 1449 855 3002 C ATOM 4022 CD1 PHE B 84 100.342-101.681 25.892 1.00 97.82 C ANISOU 4022 CD1 PHE B 84 9471 11807 15891 1556 1091 3293 C ATOM 4023 CD2 PHE B 84 101.370-100.425 24.141 1.00 92.95 C ANISOU 4023 CD2 PHE B 84 9042 11480 14797 1422 631 2713 C ATOM 4024 CE1 PHE B 84 101.177-102.766 25.604 1.00100.11 C ANISOU 4024 CE1 PHE B 84 9825 11943 16270 1635 1091 3283 C ATOM 4025 CE2 PHE B 84 102.201-101.513 23.850 1.00 97.05 C ANISOU 4025 CE2 PHE B 84 9621 11863 15391 1502 634 2691 C ATOM 4026 CZ PHE B 84 102.093-102.678 24.579 1.00 97.76 C ANISOU 4026 CZ PHE B 84 9649 11723 15772 1608 857 2968 C ATOM 4027 N ASN B 85 101.730 -97.184 25.776 1.00 81.55 N ANISOU 4027 N ASN B 85 7694 10892 12399 1541 703 2769 N ATOM 4028 CA ASN B 85 103.088 -96.701 25.571 1.00 79.28 C ANISOU 4028 CA ASN B 85 7535 10876 11712 1602 595 2609 C ATOM 4029 C ASN B 85 103.681 -96.116 26.843 1.00 82.16 C ANISOU 4029 C ASN B 85 7931 11574 11713 1773 727 2736 C ATOM 4030 O ASN B 85 104.833 -96.422 27.150 1.00 81.71 O ANISOU 4030 O ASN B 85 7934 11687 11424 1909 738 2749 O ATOM 4031 CB ASN B 85 103.130 -95.695 24.455 1.00 76.86 C ANISOU 4031 CB ASN B 85 7279 10627 11296 1447 372 2324 C ATOM 4032 CG ASN B 85 103.155 -96.356 23.113 1.00 98.39 C ANISOU 4032 CG ASN B 85 10028 13135 14219 1343 202 2142 C ATOM 4033 OD1 ASN B 85 102.116 -96.598 22.492 1.00 97.20 O ANISOU 4033 OD1 ASN B 85 9803 12747 14380 1223 125 2089 O ATOM 4034 ND2 ASN B 85 104.344 -96.739 22.676 1.00 86.28 N ANISOU 4034 ND2 ASN B 85 8586 11681 12515 1404 145 2038 N ATOM 4035 N LEU B 86 102.897 -95.320 27.599 1.00 77.87 N ANISOU 4035 N LEU B 86 7338 11127 11122 1782 824 2820 N ATOM 4036 CA LEU B 86 103.345 -94.726 28.857 1.00 77.82 C ANISOU 4036 CA LEU B 86 7358 11449 10761 1956 943 2911 C ATOM 4037 C LEU B 86 103.630 -95.832 29.895 1.00 84.03 C ANISOU 4037 C LEU B 86 8132 12268 11527 2182 1152 3215 C ATOM 4038 O LEU B 86 104.637 -95.745 30.594 1.00 83.57 O ANISOU 4038 O LEU B 86 8128 12501 11124 2357 1169 3235 O ATOM 4039 CB LEU B 86 102.310 -93.699 29.377 1.00 77.88 C ANISOU 4039 CB LEU B 86 7312 11516 10763 1924 1014 2925 C ATOM 4040 CG LEU B 86 102.458 -93.128 30.807 1.00 84.06 C ANISOU 4040 CG LEU B 86 8107 12617 11214 2123 1170 3029 C ATOM 4041 CD1 LEU B 86 103.755 -92.376 30.984 1.00 83.58 C ANISOU 4041 CD1 LEU B 86 8133 12877 10747 2182 1041 2816 C ATOM 4042 CD2 LEU B 86 101.302 -92.212 31.151 1.00 86.82 C ANISOU 4042 CD2 LEU B 86 8396 12960 11630 2080 1246 3030 C ATOM 4043 N ALA B 87 102.773 -96.872 29.966 1.00 82.88 N ANISOU 4043 N ALA B 87 7907 11822 11762 2180 1304 3450 N ATOM 4044 CA ALA B 87 102.928 -98.008 30.879 1.00 85.44 C ANISOU 4044 CA ALA B 87 8214 12113 12137 2393 1533 3789 C ATOM 4045 C ALA B 87 104.168 -98.834 30.527 1.00 89.77 C ANISOU 4045 C ALA B 87 8835 12661 12612 2481 1455 3756 C ATOM 4046 O ALA B 87 104.853 -99.325 31.431 1.00 90.48 O ANISOU 4046 O ALA B 87 8956 12930 12492 2724 1584 3968 O ATOM 4047 CB ALA B 87 101.689 -98.884 30.840 1.00 88.27 C ANISOU 4047 CB ALA B 87 8449 12084 13006 2320 1704 4017 C ATOM 4048 N VAL B 88 104.462 -98.970 29.212 1.00 85.61 N ANISOU 4048 N VAL B 88 8335 11955 12238 2304 1245 3490 N ATOM 4049 CA VAL B 88 105.642 -99.688 28.709 1.00 85.73 C ANISOU 4049 CA VAL B 88 8415 11961 12196 2374 1157 3410 C ATOM 4050 C VAL B 88 106.918 -98.893 29.085 1.00 88.71 C ANISOU 4050 C VAL B 88 8863 12772 12073 2494 1063 3283 C ATOM 4051 O VAL B 88 107.859 -99.483 29.614 1.00 89.80 O ANISOU 4051 O VAL B 88 9024 13051 12045 2701 1118 3405 O ATOM 4052 CB VAL B 88 105.545 -99.976 27.186 1.00 88.49 C ANISOU 4052 CB VAL B 88 8778 12028 12818 2163 963 3138 C ATOM 4053 CG1 VAL B 88 106.907-100.324 26.583 1.00 87.46 C ANISOU 4053 CG1 VAL B 88 8728 11986 12515 2230 842 2975 C ATOM 4054 CG2 VAL B 88 104.534-101.084 26.904 1.00 90.32 C ANISOU 4054 CG2 VAL B 88 8925 11817 13576 2086 1054 3264 C ATOM 4055 N ALA B 89 106.934 -97.566 28.826 1.00 82.99 N ANISOU 4055 N ALA B 89 8155 12243 11134 2367 924 3042 N ATOM 4056 CA ALA B 89 108.040 -96.660 29.146 1.00 81.70 C ANISOU 4056 CA ALA B 89 8028 12465 10550 2436 824 2880 C ATOM 4057 C ALA B 89 108.298 -96.597 30.663 1.00 87.90 C ANISOU 4057 C ALA B 89 8800 13556 11043 2688 966 3085 C ATOM 4058 O ALA B 89 109.454 -96.486 31.078 1.00 87.25 O ANISOU 4058 O ALA B 89 8729 13769 10654 2833 908 3030 O ATOM 4059 CB ALA B 89 107.742 -95.270 28.608 1.00 80.26 C ANISOU 4059 CB ALA B 89 7854 12351 10291 2236 687 2620 C ATOM 4060 N ASP B 90 107.225 -96.680 31.483 1.00 87.16 N ANISOU 4060 N ASP B 90 8673 13407 11038 2752 1151 3318 N ATOM 4061 CA ASP B 90 107.313 -96.691 32.943 1.00 89.51 C ANISOU 4061 CA ASP B 90 8966 13993 11049 3020 1314 3545 C ATOM 4062 C ASP B 90 107.911 -98.008 33.418 1.00 96.07 C ANISOU 4062 C ASP B 90 9805 14813 11885 3261 1437 3832 C ATOM 4063 O ASP B 90 108.791 -97.991 34.271 1.00 96.55 O ANISOU 4063 O ASP B 90 9884 15221 11582 3501 1440 3890 O ATOM 4064 CB ASP B 90 105.933 -96.457 33.594 1.00 92.67 C ANISOU 4064 CB ASP B 90 9324 14314 11574 3023 1509 3734 C ATOM 4065 CG ASP B 90 105.460 -95.005 33.613 1.00106.28 C ANISOU 4065 CG ASP B 90 11045 16176 13161 2894 1425 3491 C ATOM 4066 OD1 ASP B 90 106.296 -94.107 33.875 1.00106.84 O ANISOU 4066 OD1 ASP B 90 11151 16566 12878 2933 1290 3261 O ATOM 4067 OD2 ASP B 90 104.241 -94.771 33.423 1.00113.54 O ANISOU 4067 OD2 ASP B 90 11913 16883 14344 2764 1503 3535 O ATOM 4068 N LEU B 91 107.475 -99.135 32.829 1.00 94.29 N ANISOU 4068 N LEU B 91 9561 14188 12078 3200 1522 3988 N ATOM 4069 CA LEU B 91 107.942-100.476 33.171 1.00 97.26 C ANISOU 4069 CA LEU B 91 9942 14462 12551 3415 1659 4279 C ATOM 4070 C LEU B 91 109.454-100.625 32.934 1.00101.02 C ANISOU 4070 C LEU B 91 10456 15155 12772 3529 1497 4130 C ATOM 4071 O LEU B 91 110.154-101.167 33.799 1.00103.69 O ANISOU 4071 O LEU B 91 10802 15702 12891 3819 1585 4353 O ATOM 4072 CB LEU B 91 107.150-101.516 32.349 1.00 98.37 C ANISOU 4072 CB LEU B 91 10044 14073 13259 3259 1737 4373 C ATOM 4073 CG LEU B 91 106.620-102.796 33.033 1.00107.21 C ANISOU 4073 CG LEU B 91 11124 14933 14679 3429 2030 4820 C ATOM 4074 CD1 LEU B 91 106.187-102.558 34.478 1.00109.40 C ANISOU 4074 CD1 LEU B 91 11387 15472 14708 3659 2268 5153 C ATOM 4075 CD2 LEU B 91 105.460-103.379 32.243 1.00111.03 C ANISOU 4075 CD2 LEU B 91 11529 14900 15758 3186 2084 4828 C ATOM 4076 N LEU B 92 109.962-100.102 31.798 1.00 93.84 N ANISOU 4076 N LEU B 92 9561 14222 11870 3318 1268 3765 N ATOM 4077 CA LEU B 92 111.386-100.198 31.454 1.00 92.63 C ANISOU 4077 CA LEU B 92 9422 14262 11512 3400 1119 3601 C ATOM 4078 C LEU B 92 112.261 -99.324 32.353 1.00 97.35 C ANISOU 4078 C LEU B 92 10000 15363 11624 3557 1039 3519 C ATOM 4079 O LEU B 92 113.417 -99.669 32.608 1.00 97.79 O ANISOU 4079 O LEU B 92 10037 15639 11478 3747 986 3528 O ATOM 4080 CB LEU B 92 111.633 -99.838 29.981 1.00 89.73 C ANISOU 4080 CB LEU B 92 9072 13740 11282 3135 925 3252 C ATOM 4081 CG LEU B 92 110.954-100.710 28.911 1.00 93.78 C ANISOU 4081 CG LEU B 92 9602 13782 12249 2981 942 3241 C ATOM 4082 CD1 LEU B 92 111.313-100.241 27.527 1.00 91.46 C ANISOU 4082 CD1 LEU B 92 9338 13431 11982 2767 742 2889 C ATOM 4083 CD2 LEU B 92 111.325-102.174 29.047 1.00 98.32 C ANISOU 4083 CD2 LEU B 92 10180 14155 13022 3173 1065 3468 C ATOM 4084 N LEU B 93 111.706 -98.200 32.821 1.00 94.19 N ANISOU 4084 N LEU B 93 9595 15139 11054 3481 1022 3420 N ATOM 4085 CA LEU B 93 112.391 -97.246 33.683 1.00 94.92 C ANISOU 4085 CA LEU B 93 9663 15692 10710 3603 930 3285 C ATOM 4086 C LEU B 93 112.530 -97.813 35.103 1.00103.14 C ANISOU 4086 C LEU B 93 10703 16995 11491 3963 1080 3605 C ATOM 4087 O LEU B 93 113.596 -97.692 35.715 1.00104.72 O ANISOU 4087 O LEU B 93 10870 17571 11346 4167 985 3552 O ATOM 4088 CB LEU B 93 111.606 -95.921 33.675 1.00 93.50 C ANISOU 4088 CB LEU B 93 9487 15548 10491 3404 885 3079 C ATOM 4089 CG LEU B 93 112.165 -94.744 34.473 1.00 98.98 C ANISOU 4089 CG LEU B 93 10152 16670 10784 3474 774 2860 C ATOM 4090 CD1 LEU B 93 113.440 -94.197 33.855 1.00 98.13 C ANISOU 4090 CD1 LEU B 93 9997 16722 10566 3374 554 2539 C ATOM 4091 CD2 LEU B 93 111.138 -93.637 34.578 1.00101.69 C ANISOU 4091 CD2 LEU B 93 10510 16973 11153 3316 794 2734 C ATOM 4092 N LEU B 94 111.466 -98.470 35.600 1.00101.14 N ANISOU 4092 N LEU B 94 10473 16541 11413 4050 1318 3947 N ATOM 4093 CA LEU B 94 111.442 -99.080 36.928 1.00104.09 C ANISOU 4093 CA LEU B 94 10857 17130 11563 4408 1511 4320 C ATOM 4094 C LEU B 94 112.371-100.280 36.989 1.00110.69 C ANISOU 4094 C LEU B 94 11690 17958 12407 4641 1539 4535 C ATOM 4095 O LEU B 94 113.035-100.480 38.007 1.00112.98 O ANISOU 4095 O LEU B 94 11978 18617 12333 4970 1562 4697 O ATOM 4096 CB LEU B 94 110.017 -99.480 37.319 1.00105.19 C ANISOU 4096 CB LEU B 94 11007 17005 11957 4410 1788 4647 C ATOM 4097 CG LEU B 94 109.058 -98.309 37.520 1.00108.42 C ANISOU 4097 CG LEU B 94 11410 17478 12307 4257 1798 4490 C ATOM 4098 CD1 LEU B 94 107.631 -98.747 37.413 1.00109.08 C ANISOU 4098 CD1 LEU B 94 11467 17175 12804 4148 2033 4742 C ATOM 4099 CD2 LEU B 94 109.315 -97.576 38.819 1.00112.33 C ANISOU 4099 CD2 LEU B 94 11923 18482 12275 4517 1810 4482 C ATOM 4100 N ALA B 95 112.475-101.028 35.873 1.00106.40 N ANISOU 4100 N ALA B 95 11147 17020 12260 4481 1516 4504 N ATOM 4101 CA ALA B 95 113.344-102.193 35.734 1.00108.19 C ANISOU 4101 CA ALA B 95 11371 17166 12569 4673 1540 4671 C ATOM 4102 C ALA B 95 114.838-101.860 35.975 1.00112.49 C ANISOU 4102 C ALA B 95 11874 18159 12707 4846 1334 4486 C ATOM 4103 O ALA B 95 115.603-102.765 36.304 1.00113.94 O ANISOU 4103 O ALA B 95 12046 18412 12834 5120 1376 4698 O ATOM 4104 CB ALA B 95 113.164-102.803 34.353 1.00107.40 C ANISOU 4104 CB ALA B 95 11279 16578 12949 4422 1508 4549 C ATOM 4105 N THR B 96 115.255-100.587 35.829 1.00107.40 N ANISOU 4105 N THR B 96 11193 17807 11806 4695 1118 4102 N ATOM 4106 CA THR B 96 116.656-100.193 36.043 1.00107.49 C ANISOU 4106 CA THR B 96 11129 18241 11470 4828 910 3892 C ATOM 4107 C THR B 96 116.944 -99.843 37.535 1.00113.60 C ANISOU 4107 C THR B 96 11878 19526 11757 5151 905 4001 C ATOM 4108 O THR B 96 118.113 -99.627 37.876 1.00113.78 O ANISOU 4108 O THR B 96 11817 19935 11480 5312 730 3857 O ATOM 4109 CB THR B 96 117.055 -99.033 35.103 1.00110.32 C ANISOU 4109 CB THR B 96 11441 18640 11836 4501 686 3422 C ATOM 4110 OG1 THR B 96 116.309 -97.859 35.430 1.00107.17 O ANISOU 4110 OG1 THR B 96 11058 18340 11321 4349 662 3261 O ATOM 4111 CG2 THR B 96 116.881 -99.381 33.626 1.00106.60 C ANISOU 4111 CG2 THR B 96 11000 17730 11773 4227 677 3306 C ATOM 4112 N LEU B 97 115.901 -99.818 38.421 1.00111.17 N ANISOU 4112 N LEU B 97 11634 19238 11369 5264 1095 4253 N ATOM 4113 CA LEU B 97 116.062 -99.486 39.849 1.00113.52 C ANISOU 4113 CA LEU B 97 11928 20034 11172 5594 1106 4359 C ATOM 4114 C LEU B 97 117.014-100.435 40.588 1.00121.73 C ANISOU 4114 C LEU B 97 12940 21348 11964 6015 1121 4643 C ATOM 4115 O LEU B 97 117.829 -99.910 41.349 1.00122.94 O ANISOU 4115 O LEU B 97 13033 22011 11668 6223 945 4489 O ATOM 4116 CB LEU B 97 114.733 -99.393 40.606 1.00114.32 C ANISOU 4116 CB LEU B 97 12105 20081 11252 5656 1352 4618 C ATOM 4117 CG LEU B 97 114.047 -98.050 40.487 1.00116.36 C ANISOU 4117 CG LEU B 97 12367 20369 11475 5388 1276 4280 C ATOM 4118 CD1 LEU B 97 112.554 -98.202 40.539 1.00116.46 C ANISOU 4118 CD1 LEU B 97 12437 20054 11759 5293 1543 4527 C ATOM 4119 CD2 LEU B 97 114.532 -97.082 41.551 1.00119.69 C ANISOU 4119 CD2 LEU B 97 12765 21358 11353 5584 1130 4061 C ATOM 4120 N PRO B 98 116.993-101.789 40.385 1.00120.50 N ANISOU 4120 N PRO B 98 12816 20881 12087 6156 1307 5029 N ATOM 4121 CA PRO B 98 117.956-102.648 41.104 1.00124.30 C ANISOU 4121 CA PRO B 98 13268 21643 12318 6585 1313 5306 C ATOM 4122 C PRO B 98 119.423-102.289 40.820 1.00128.15 C ANISOU 4122 C PRO B 98 13632 22461 12597 6613 1000 4955 C ATOM 4123 O PRO B 98 120.259-102.414 41.711 1.00130.57 O ANISOU 4123 O PRO B 98 13881 23228 12501 6974 907 5040 O ATOM 4124 CB PRO B 98 117.627-104.054 40.586 1.00126.89 C ANISOU 4124 CB PRO B 98 13645 21443 13124 6617 1552 5689 C ATOM 4125 CG PRO B 98 116.209-103.980 40.156 1.00129.31 C ANISOU 4125 CG PRO B 98 14017 21298 13816 6320 1743 5748 C ATOM 4126 CD PRO B 98 116.087-102.614 39.552 1.00121.02 C ANISOU 4126 CD PRO B 98 12939 20330 12714 5954 1517 5233 C ATOM 4127 N LEU B 99 119.717-101.819 39.595 1.00121.80 N ANISOU 4127 N LEU B 99 12778 21439 12061 6241 842 4567 N ATOM 4128 CA LEU B 99 121.055-101.420 39.163 1.00121.32 C ANISOU 4128 CA LEU B 99 12580 21634 11882 6204 569 4216 C ATOM 4129 C LEU B 99 121.563-100.221 39.970 1.00127.59 C ANISOU 4129 C LEU B 99 13279 22988 12211 6263 340 3903 C ATOM 4130 O LEU B 99 122.692-100.274 40.461 1.00129.49 O ANISOU 4130 O LEU B 99 13396 23640 12164 6513 168 3840 O ATOM 4131 CB LEU B 99 121.073-101.104 37.653 1.00117.25 C ANISOU 4131 CB LEU B 99 12051 20740 11761 5777 497 3893 C ATOM 4132 CG LEU B 99 121.238-102.292 36.704 1.00121.21 C ANISOU 4132 CG LEU B 99 12581 20809 12662 5761 607 4053 C ATOM 4133 CD1 LEU B 99 119.920-103.043 36.492 1.00120.91 C ANISOU 4133 CD1 LEU B 99 12683 20268 12988 5686 869 4357 C ATOM 4134 CD2 LEU B 99 121.756-101.832 35.365 1.00120.83 C ANISOU 4134 CD2 LEU B 99 12477 20609 12825 5435 461 3665 C ATOM 4135 N TRP B 100 120.733 -99.166 40.138 1.00123.77 N ANISOU 4135 N TRP B 100 12844 22522 11662 6051 332 3705 N ATOM 4136 CA TRP B 100 121.121 -97.967 40.899 1.00125.07 C ANISOU 4136 CA TRP B 100 12925 23178 11418 6085 116 3364 C ATOM 4137 C TRP B 100 121.142 -98.221 42.409 1.00133.66 C ANISOU 4137 C TRP B 100 14036 24729 12019 6546 152 3613 C ATOM 4138 O TRP B 100 121.886 -97.539 43.121 1.00135.21 O ANISOU 4138 O TRP B 100 14124 25427 11820 6692 -80 3346 O ATOM 4139 CB TRP B 100 120.216 -96.766 40.573 1.00121.34 C ANISOU 4139 CB TRP B 100 12503 22548 11053 5724 110 3071 C ATOM 4140 CG TRP B 100 119.822 -96.651 39.127 1.00118.49 C ANISOU 4140 CG TRP B 100 12171 21675 11174 5306 149 2945 C ATOM 4141 CD1 TRP B 100 118.557 -96.532 38.637 1.00119.37 C ANISOU 4141 CD1 TRP B 100 12398 21385 11573 5071 316 3023 C ATOM 4142 CD2 TRP B 100 120.695 -96.691 37.983 1.00116.48 C ANISOU 4142 CD2 TRP B 100 11827 21274 11158 5102 22 2734 C ATOM 4143 NE1 TRP B 100 118.583 -96.484 37.259 1.00115.79 N ANISOU 4143 NE1 TRP B 100 11940 20558 11497 4741 282 2863 N ATOM 4144 CE2 TRP B 100 119.884 -96.575 36.832 1.00117.43 C ANISOU 4144 CE2 TRP B 100 12031 20914 11674 4755 115 2689 C ATOM 4145 CE3 TRP B 100 122.086 -96.813 37.818 1.00118.63 C ANISOU 4145 CE3 TRP B 100 11945 21788 11342 5190 -158 2581 C ATOM 4146 CZ2 TRP B 100 120.420 -96.570 35.534 1.00114.65 C ANISOU 4146 CZ2 TRP B 100 11634 20334 11596 4510 42 2500 C ATOM 4147 CZ3 TRP B 100 122.614 -96.815 36.538 1.00117.84 C ANISOU 4147 CZ3 TRP B 100 11789 21444 11541 4937 -210 2403 C ATOM 4148 CH2 TRP B 100 121.787 -96.696 35.413 1.00115.55 C ANISOU 4148 CH2 TRP B 100 11605 20691 11610 4607 -107 2367 C ATOM 4149 N ALA B 101 120.374 -99.228 42.887 1.00132.46 N ANISOU 4149 N ALA B 101 14013 24417 11900 6786 439 4126 N ATOM 4150 CA ALA B 101 120.341 -99.629 44.299 1.00136.98 C ANISOU 4150 CA ALA B 101 14628 25407 12011 7269 528 4458 C ATOM 4151 C ALA B 101 121.659-100.325 44.684 1.00144.58 C ANISOU 4151 C ALA B 101 15483 26720 12732 7638 381 4568 C ATOM 4152 O ALA B 101 122.207-100.056 45.756 1.00147.81 O ANISOU 4152 O ALA B 101 15838 27699 12624 7978 233 4526 O ATOM 4153 CB ALA B 101 119.159-100.552 44.561 1.00138.73 C ANISOU 4153 CB ALA B 101 15002 25288 12422 7389 912 5006 C ATOM 4154 N THR B 102 122.172-101.198 43.783 1.00139.94 N ANISOU 4154 N THR B 102 14856 25798 12518 7573 410 4683 N ATOM 4155 CA THR B 102 123.430-101.934 43.934 1.00142.20 C ANISOU 4155 CA THR B 102 15026 26329 12677 7888 285 4789 C ATOM 4156 C THR B 102 124.608-100.948 43.785 1.00146.24 C ANISOU 4156 C THR B 102 15333 27245 12988 7778 -96 4239 C ATOM 4157 O THR B 102 125.566-101.028 44.554 1.00149.18 O ANISOU 4157 O THR B 102 15582 28127 12975 8127 -284 4225 O ATOM 4158 CB THR B 102 123.491-103.101 42.926 1.00145.69 C ANISOU 4158 CB THR B 102 15498 26225 13633 7812 456 5041 C ATOM 4159 OG1 THR B 102 122.254-103.820 42.950 1.00143.78 O ANISOU 4159 OG1 THR B 102 15427 25539 13663 7807 801 5466 O ATOM 4160 CG2 THR B 102 124.638-104.062 43.208 1.00146.40 C ANISOU 4160 CG2 THR B 102 15493 26527 13607 8214 398 5269 C ATOM 4161 N TYR B 103 124.508 -99.998 42.824 1.00139.57 N ANISOU 4161 N TYR B 103 14442 26179 12408 7299 -207 3794 N ATOM 4162 CA TYR B 103 125.501 -98.947 42.556 1.00139.05 C ANISOU 4162 CA TYR B 103 14174 26406 12251 7109 -533 3253 C ATOM 4163 C TYR B 103 125.710 -98.068 43.798 1.00144.92 C ANISOU 4163 C TYR B 103 14850 27748 12467 7314 -739 3025 C ATOM 4164 O TYR B 103 126.840 -97.662 44.072 1.00146.01 O ANISOU 4164 O TYR B 103 14780 28307 12389 7408 -1027 2725 O ATOM 4165 CB TYR B 103 125.059 -98.091 41.350 1.00136.46 C ANISOU 4165 CB TYR B 103 13861 25669 12319 6565 -535 2906 C ATOM 4166 CG TYR B 103 126.028 -97.001 40.932 1.00138.97 C ANISOU 4166 CG TYR B 103 13968 26198 12638 6318 -824 2373 C ATOM 4167 CD1 TYR B 103 127.102 -97.279 40.089 1.00140.75 C ANISOU 4167 CD1 TYR B 103 14032 26372 13076 6237 -923 2253 C ATOM 4168 CD2 TYR B 103 125.823 -95.677 41.309 1.00139.97 C ANISOU 4168 CD2 TYR B 103 14054 26527 12602 6141 -973 1987 C ATOM 4169 CE1 TYR B 103 127.980 -96.274 39.678 1.00141.36 C ANISOU 4169 CE1 TYR B 103 13894 26616 13198 5993 -1157 1784 C ATOM 4170 CE2 TYR B 103 126.692 -94.665 40.903 1.00140.53 C ANISOU 4170 CE2 TYR B 103 13918 26743 12735 5891 -1218 1503 C ATOM 4171 CZ TYR B 103 127.768 -94.966 40.085 1.00147.62 C ANISOU 4171 CZ TYR B 103 14642 27596 13850 5812 -1303 1414 C ATOM 4172 OH TYR B 103 128.615 -93.961 39.683 1.00148.25 O ANISOU 4172 OH TYR B 103 14500 27803 14026 5555 -1518 958 O ATOM 4173 N TYR B 104 124.624 -97.790 44.547 1.00141.99 N ANISOU 4173 N TYR B 104 14641 27415 11893 7390 -593 3157 N ATOM 4174 CA TYR B 104 124.672 -96.990 45.768 1.00144.85 C ANISOU 4174 CA TYR B 104 14974 28335 11728 7612 -760 2949 C ATOM 4175 C TYR B 104 125.130 -97.842 46.967 1.00155.00 C ANISOU 4175 C TYR B 104 16258 30101 12533 8206 -765 3313 C ATOM 4176 O TYR B 104 125.742 -97.293 47.887 1.00158.11 O ANISOU 4176 O TYR B 104 16543 31078 12454 8448 -1023 3061 O ATOM 4177 CB TYR B 104 123.311 -96.331 46.051 1.00144.24 C ANISOU 4177 CB TYR B 104 15072 28105 11628 7465 -582 2939 C ATOM 4178 CG TYR B 104 123.352 -95.305 47.164 1.00148.15 C ANISOU 4178 CG TYR B 104 15534 29139 11618 7624 -775 2605 C ATOM 4179 CD1 TYR B 104 123.781 -94.002 46.924 1.00148.72 C ANISOU 4179 CD1 TYR B 104 15467 29327 11714 7322 -1053 1993 C ATOM 4180 CD2 TYR B 104 122.959 -95.635 48.459 1.00152.91 C ANISOU 4180 CD2 TYR B 104 16245 30132 11721 8087 -670 2899 C ATOM 4181 CE1 TYR B 104 123.823 -93.053 47.946 1.00152.14 C ANISOU 4181 CE1 TYR B 104 15866 30239 11700 7466 -1243 1640 C ATOM 4182 CE2 TYR B 104 122.994 -94.695 49.488 1.00156.58 C ANISOU 4182 CE2 TYR B 104 16689 31114 11692 8255 -856 2560 C ATOM 4183 CZ TYR B 104 123.427 -93.405 49.227 1.00162.05 C ANISOU 4183 CZ TYR B 104 17238 31900 12432 7939 -1152 1911 C ATOM 4184 OH TYR B 104 123.460 -92.476 50.239 1.00165.10 O ANISOU 4184 OH TYR B 104 17601 32779 12350 8103 -1346 1535 O ATOM 4185 N SER B 105 124.849 -99.171 46.953 1.00152.99 N ANISOU 4185 N SER B 105 16118 29604 12407 8446 -489 3896 N ATOM 4186 CA SER B 105 125.238-100.114 48.017 1.00157.97 C ANISOU 4186 CA SER B 105 16766 30629 12627 9033 -443 4337 C ATOM 4187 C SER B 105 126.765-100.277 48.103 1.00164.21 C ANISOU 4187 C SER B 105 17323 31831 13239 9248 -767 4158 C ATOM 4188 O SER B 105 127.290-100.584 49.177 1.00168.03 O ANISOU 4188 O SER B 105 17795 32763 13285 9666 -887 4295 O ATOM 4189 CB SER B 105 124.582-101.475 47.801 1.00161.83 C ANISOU 4189 CB SER B 105 17418 30650 13421 9170 -53 4985 C ATOM 4190 OG SER B 105 123.188-101.430 48.060 1.00170.67 O ANISOU 4190 OG SER B 105 18732 31516 14600 9101 256 5233 O ATOM 4191 N TYR B 106 127.464-100.055 46.970 1.00157.80 N ANISOU 4191 N TYR B 106 16353 30775 12827 8888 -917 3826 N ATOM 4192 CA TYR B 106 128.913-100.120 46.852 1.00159.43 C ANISOU 4192 CA TYR B 106 16301 31307 12969 9006 -1218 3601 C ATOM 4193 C TYR B 106 129.490 -98.693 46.908 1.00163.29 C ANISOU 4193 C TYR B 106 16585 32145 13314 8755 -1580 2924 C ATOM 4194 O TYR B 106 130.643 -98.481 46.542 1.00163.43 O ANISOU 4194 O TYR B 106 16348 32339 13408 8690 -1837 2616 O ATOM 4195 CB TYR B 106 129.311-100.868 45.562 1.00157.94 C ANISOU 4195 CB TYR B 106 16066 30613 13331 8796 -1109 3705 C ATOM 4196 CG TYR B 106 129.081-102.359 45.652 1.00161.94 C ANISOU 4196 CG TYR B 106 16712 30870 13946 9135 -819 4340 C ATOM 4197 CD1 TYR B 106 129.921-103.169 46.410 1.00168.99 C ANISOU 4197 CD1 TYR B 106 17516 32158 14534 9664 -895 4632 C ATOM 4198 CD2 TYR B 106 128.027-102.963 44.976 1.00159.93 C ANISOU 4198 CD2 TYR B 106 16668 29975 14121 8933 -474 4647 C ATOM 4199 CE1 TYR B 106 129.707-104.543 46.507 1.00171.37 C ANISOU 4199 CE1 TYR B 106 17989 32076 15049 9881 -631 5192 C ATOM 4200 CE2 TYR B 106 127.799-104.336 45.068 1.00162.81 C ANISOU 4200 CE2 TYR B 106 17153 30069 14638 9233 -197 5223 C ATOM 4201 CZ TYR B 106 128.643-105.124 45.834 1.00174.91 C ANISOU 4201 CZ TYR B 106 18642 31871 15946 9667 -277 5483 C ATOM 4202 OH TYR B 106 128.434-106.481 45.914 1.00176.15 O ANISOU 4202 OH TYR B 106 19012 31435 16483 9695 -65 5917 O ATOM 4203 N ARG B 107 128.680 -97.725 47.410 1.00159.82 N ANISOU 4203 N ARG B 107 16247 31804 12674 8629 -1589 2698 N ATOM 4204 CA ARG B 107 128.984 -96.297 47.597 1.00159.91 C ANISOU 4204 CA ARG B 107 16106 32105 12549 8393 -1894 2060 C ATOM 4205 C ARG B 107 129.583 -95.652 46.318 1.00161.19 C ANISOU 4205 C ARG B 107 16081 31953 13212 7876 -2023 1631 C ATOM 4206 O ARG B 107 130.709 -95.130 46.341 1.00162.10 O ANISOU 4206 O ARG B 107 15918 32396 13277 7843 -2340 1227 O ATOM 4207 CB ARG B 107 129.901 -96.087 48.818 1.00165.50 C ANISOU 4207 CB ARG B 107 16634 33575 12673 8825 -2233 1864 C ATOM 4208 N TYR B 108 128.775 -95.623 45.222 1.00154.18 N ANISOU 4208 N TYR B 108 15340 30438 12802 7469 -1773 1710 N ATOM 4209 CA TYR B 108 129.097 -95.078 43.887 1.00150.36 C ANISOU 4209 CA TYR B 108 14744 29570 12816 6970 -1807 1397 C ATOM 4210 C TYR B 108 130.282 -95.846 43.266 1.00154.87 C ANISOU 4210 C TYR B 108 15122 30144 13576 7046 -1877 1470 C ATOM 4211 O TYR B 108 131.393 -95.316 43.177 1.00155.51 O ANISOU 4211 O TYR B 108 14925 30502 13659 6978 -2144 1098 O ATOM 4212 CB TYR B 108 129.376 -93.554 43.927 1.00151.57 C ANISOU 4212 CB TYR B 108 14734 29896 12959 6662 -2062 783 C ATOM 4213 CG TYR B 108 128.152 -92.668 44.038 1.00151.73 C ANISOU 4213 CG TYR B 108 14945 29712 12994 6429 -1949 654 C ATOM 4214 CD1 TYR B 108 127.600 -92.360 45.279 1.00156.50 C ANISOU 4214 CD1 TYR B 108 15649 30667 13146 6698 -1982 641 C ATOM 4215 CD2 TYR B 108 127.616 -92.045 42.915 1.00148.49 C ANISOU 4215 CD2 TYR B 108 14593 28796 13031 5948 -1831 505 C ATOM 4216 CE1 TYR B 108 126.500 -91.508 45.391 1.00155.82 C ANISOU 4216 CE1 TYR B 108 15723 30403 13081 6495 -1877 500 C ATOM 4217 CE2 TYR B 108 126.509 -91.201 43.013 1.00147.84 C ANISOU 4217 CE2 TYR B 108 14669 28529 12975 5746 -1736 381 C ATOM 4218 CZ TYR B 108 125.958 -90.930 44.254 1.00158.56 C ANISOU 4218 CZ TYR B 108 16121 30219 13904 6015 -1757 372 C ATOM 4219 OH TYR B 108 124.877 -90.087 44.352 1.00159.36 O ANISOU 4219 OH TYR B 108 16369 30140 14041 5828 -1655 240 O ATOM 4220 N ASP B 109 130.033 -97.107 42.855 1.00151.08 N ANISOU 4220 N ASP B 109 14782 29350 13273 7193 -1628 1949 N ATOM 4221 CA ASP B 109 131.027 -98.001 42.256 1.00151.58 C ANISOU 4221 CA ASP B 109 14703 29360 13530 7308 -1638 2085 C ATOM 4222 C ASP B 109 130.467 -98.733 41.051 1.00152.02 C ANISOU 4222 C ASP B 109 14927 28779 14054 7090 -1347 2338 C ATOM 4223 O ASP B 109 129.426 -99.384 41.167 1.00150.85 O ANISOU 4223 O ASP B 109 15024 28337 13956 7170 -1093 2715 O ATOM 4224 CB ASP B 109 131.504 -99.031 43.283 1.00158.11 C ANISOU 4224 CB ASP B 109 15507 30573 13996 7886 -1666 2458 C ATOM 4225 CG ASP B 109 132.852 -98.726 43.875 1.00173.85 C ANISOU 4225 CG ASP B 109 17184 33168 15703 8111 -2018 2177 C ATOM 4226 OD1 ASP B 109 132.911 -97.919 44.818 1.00177.53 O ANISOU 4226 OD1 ASP B 109 17577 34090 15786 8207 -2240 1911 O ATOM 4227 OD2 ASP B 109 133.852 -99.302 43.397 1.00180.26 O ANISOU 4227 OD2 ASP B 109 17811 34001 16679 8201 -2078 2210 O ATOM 4228 N TRP B 110 131.163 -98.656 39.902 1.00146.78 N ANISOU 4228 N TRP B 110 14124 27910 13737 6826 -1381 2133 N ATOM 4229 CA TRP B 110 130.715 -99.361 38.698 1.00143.45 C ANISOU 4229 CA TRP B 110 13853 26910 13743 6634 -1130 2326 C ATOM 4230 C TRP B 110 131.544-100.631 38.471 1.00148.76 C ANISOU 4230 C TRP B 110 14451 27560 14510 6940 -1076 2595 C ATOM 4231 O TRP B 110 132.748-100.553 38.221 1.00149.62 O ANISOU 4231 O TRP B 110 14309 27902 14637 6978 -1240 2397 O ATOM 4232 CB TRP B 110 130.760 -98.451 37.465 1.00138.54 C ANISOU 4232 CB TRP B 110 13175 26016 13447 6136 -1151 1950 C ATOM 4233 N LEU B 111 130.891-101.801 38.598 1.00145.24 N ANISOU 4233 N LEU B 111 14212 26831 14142 7166 -838 3052 N ATOM 4234 CA LEU B 111 131.495-103.132 38.436 1.00146.74 C ANISOU 4234 CA LEU B 111 14378 26922 14454 7488 -738 3371 C ATOM 4235 C LEU B 111 130.833-103.932 37.299 1.00146.27 C ANISOU 4235 C LEU B 111 14510 26210 14856 7303 -470 3540 C ATOM 4236 O LEU B 111 131.045-105.145 37.206 1.00147.52 O ANISOU 4236 O LEU B 111 14710 26180 15161 7572 -330 3859 O ATOM 4237 CB LEU B 111 131.374-103.925 39.759 1.00151.07 C ANISOU 4237 CB LEU B 111 14991 27734 14673 8002 -688 3810 C ATOM 4238 CG LEU B 111 132.301-103.531 40.904 1.00160.04 C ANISOU 4238 CG LEU B 111 15913 29567 15329 8336 -969 3709 C ATOM 4239 CD1 LEU B 111 131.738-103.988 42.245 1.00163.77 C ANISOU 4239 CD1 LEU B 111 16527 30283 15417 8762 -888 4120 C ATOM 4240 CD2 LEU B 111 133.708-104.056 40.679 1.00165.15 C ANISOU 4240 CD2 LEU B 111 16308 30429 16012 8564 -1109 3675 C ATOM 4241 N PHE B 112 130.035-103.250 36.442 1.00137.65 N ANISOU 4241 N PHE B 112 13529 24777 13993 6856 -409 3317 N ATOM 4242 CA PHE B 112 129.279-103.854 35.337 1.00134.25 C ANISOU 4242 CA PHE B 112 13283 23743 13982 6639 -190 3410 C ATOM 4243 C PHE B 112 129.965-103.702 33.968 1.00134.42 C ANISOU 4243 C PHE B 112 13210 23593 14272 6384 -226 3107 C ATOM 4244 O PHE B 112 129.654-104.460 33.047 1.00133.01 O ANISOU 4244 O PHE B 112 13152 22968 14418 6310 -66 3188 O ATOM 4245 CB PHE B 112 127.870-103.250 35.270 1.00133.29 C ANISOU 4245 CB PHE B 112 13352 23360 13931 6339 -94 3386 C ATOM 4246 N GLY B 113 130.876-102.738 33.846 1.00129.18 N ANISOU 4246 N GLY B 113 12328 23276 13477 6258 -428 2760 N ATOM 4247 CA GLY B 113 131.593-102.491 32.602 1.00126.77 C ANISOU 4247 CA GLY B 113 11910 22863 13394 6028 -448 2482 C ATOM 4248 C GLY B 113 131.314-101.125 32.005 1.00126.55 C ANISOU 4248 C GLY B 113 11862 22814 13407 5590 -521 2126 C ATOM 4249 O GLY B 113 130.204-100.605 32.152 1.00124.45 O ANISOU 4249 O GLY B 113 11762 22393 13129 5400 -481 2126 O ATOM 4250 N PRO B 114 132.301-100.526 31.294 1.00122.08 N ANISOU 4250 N PRO B 114 11087 22384 12912 5426 -608 1832 N ATOM 4251 CA PRO B 114 132.086 -99.188 30.712 1.00119.27 C ANISOU 4251 CA PRO B 114 10703 21996 12617 5013 -660 1514 C ATOM 4252 C PRO B 114 131.060 -99.141 29.579 1.00119.75 C ANISOU 4252 C PRO B 114 11005 21575 12917 4720 -495 1510 C ATOM 4253 O PRO B 114 130.552 -98.056 29.280 1.00117.19 O ANISOU 4253 O PRO B 114 10719 21189 12620 4406 -521 1321 O ATOM 4254 CB PRO B 114 133.474 -98.799 30.200 1.00122.07 C ANISOU 4254 CB PRO B 114 10762 22588 13031 4962 -749 1271 C ATOM 4255 CG PRO B 114 134.191-100.077 29.997 1.00128.54 C ANISOU 4255 CG PRO B 114 11532 23392 13917 5277 -676 1461 C ATOM 4256 CD PRO B 114 133.673-101.011 31.039 1.00125.81 C ANISOU 4256 CD PRO B 114 11324 23059 13420 5620 -654 1792 C ATOM 4257 N VAL B 115 130.766-100.301 28.954 1.00115.65 N ANISOU 4257 N VAL B 115 10643 20721 12578 4829 -337 1706 N ATOM 4258 CA VAL B 115 129.782-100.423 27.877 1.00112.41 C ANISOU 4258 CA VAL B 115 10462 19858 12393 4592 -199 1701 C ATOM 4259 C VAL B 115 128.390-100.325 28.515 1.00112.58 C ANISOU 4259 C VAL B 115 10679 19712 12384 4539 -164 1853 C ATOM 4260 O VAL B 115 127.559 -99.567 28.026 1.00109.61 O ANISOU 4260 O VAL B 115 10411 19158 12078 4246 -151 1734 O ATOM 4261 CB VAL B 115 129.969-101.707 27.015 1.00117.37 C ANISOU 4261 CB VAL B 115 11175 20186 13235 4734 -60 1812 C ATOM 4262 CG1 VAL B 115 128.971-101.744 25.857 1.00114.94 C ANISOU 4262 CG1 VAL B 115 11087 19446 13141 4479 44 1747 C ATOM 4263 CG2 VAL B 115 131.395-101.815 26.481 1.00118.59 C ANISOU 4263 CG2 VAL B 115 11113 20544 13401 4826 -82 1674 C ATOM 4264 N MET B 116 128.173-101.024 29.650 1.00109.49 N ANISOU 4264 N MET B 116 10317 19409 11874 4834 -145 2125 N ATOM 4265 CA MET B 116 126.917-100.992 30.408 1.00107.99 C ANISOU 4265 CA MET B 116 10288 19105 11636 4833 -86 2311 C ATOM 4266 C MET B 116 126.621 -99.579 30.926 1.00108.82 C ANISOU 4266 C MET B 116 10347 19454 11546 4636 -208 2107 C ATOM 4267 O MET B 116 125.454 -99.231 31.080 1.00106.80 O ANISOU 4267 O MET B 116 10235 19023 11321 4496 -150 2155 O ATOM 4268 CB MET B 116 126.969-101.977 31.588 1.00113.33 C ANISOU 4268 CB MET B 116 10974 19908 12180 5235 -33 2660 C ATOM 4269 N CYS B 117 127.678 -98.775 31.193 1.00105.06 N ANISOU 4269 N CYS B 117 9656 19369 10893 4628 -375 1869 N ATOM 4270 CA CYS B 117 127.591 -97.388 31.672 1.00103.56 C ANISOU 4270 CA CYS B 117 9387 19421 10542 4443 -512 1618 C ATOM 4271 C CYS B 117 126.932 -96.509 30.591 1.00103.46 C ANISOU 4271 C CYS B 117 9465 19108 10737 4040 -468 1423 C ATOM 4272 O CYS B 117 126.091 -95.672 30.919 1.00102.02 O ANISOU 4272 O CYS B 117 9359 18897 10508 3883 -483 1352 O ATOM 4273 CB CYS B 117 128.974 -96.866 32.072 1.00105.65 C ANISOU 4273 CB CYS B 117 9369 20130 10644 4521 -702 1393 C ATOM 4274 SG CYS B 117 128.999 -95.164 32.717 1.00109.25 S ANISOU 4274 SG CYS B 117 9693 20883 10933 4303 -891 1031 S ATOM 4275 N LYS B 118 127.273 -96.744 29.304 1.00 97.82 N ANISOU 4275 N LYS B 118 8756 18169 10243 3899 -403 1355 N ATOM 4276 CA LYS B 118 126.683 -96.027 28.173 1.00 94.38 C ANISOU 4276 CA LYS B 118 8419 17452 9990 3557 -352 1206 C ATOM 4277 C LYS B 118 125.314 -96.603 27.815 1.00 97.40 C ANISOU 4277 C LYS B 118 9048 17439 10520 3508 -225 1390 C ATOM 4278 O LYS B 118 124.388 -95.830 27.584 1.00 95.88 O ANISOU 4278 O LYS B 118 8954 17094 10381 3281 -216 1321 O ATOM 4279 CB LYS B 118 127.600 -96.056 26.938 1.00 95.29 C ANISOU 4279 CB LYS B 118 8443 17517 10244 3455 -323 1068 C ATOM 4280 CG LYS B 118 128.658 -94.968 26.941 1.00 96.96 C ANISOU 4280 CG LYS B 118 8411 18022 10407 3326 -428 813 C ATOM 4281 CD LYS B 118 129.268 -94.758 25.569 1.00 99.48 C ANISOU 4281 CD LYS B 118 8678 18232 10889 3154 -351 689 C ATOM 4282 CE LYS B 118 130.497 -93.879 25.567 1.00105.68 C ANISOU 4282 CE LYS B 118 9174 19304 11674 3058 -428 469 C ATOM 4283 NZ LYS B 118 130.247 -92.500 26.071 1.00113.76 N ANISOU 4283 NZ LYS B 118 10127 20423 12674 2835 -524 286 N ATOM 4284 N VAL B 119 125.192 -97.956 27.766 1.00 94.53 N ANISOU 4284 N VAL B 119 8769 16899 10249 3721 -129 1618 N ATOM 4285 CA VAL B 119 123.975 -98.696 27.390 1.00 92.98 C ANISOU 4285 CA VAL B 119 8776 16298 10253 3689 -7 1790 C ATOM 4286 C VAL B 119 122.842 -98.457 28.405 1.00 95.65 C ANISOU 4286 C VAL B 119 9199 16621 10524 3702 22 1943 C ATOM 4287 O VAL B 119 121.787 -97.961 28.006 1.00 93.81 O ANISOU 4287 O VAL B 119 9073 16167 10405 3480 48 1899 O ATOM 4288 CB VAL B 119 124.242-100.213 27.175 1.00 98.44 C ANISOU 4288 CB VAL B 119 9510 16800 11091 3928 91 1983 C ATOM 4289 CG1 VAL B 119 122.940-100.999 27.020 1.00 97.86 C ANISOU 4289 CG1 VAL B 119 9618 16311 11252 3906 212 2170 C ATOM 4290 CG2 VAL B 119 125.136-100.439 25.963 1.00 98.13 C ANISOU 4290 CG2 VAL B 119 9424 16709 11151 3885 91 1810 C ATOM 4291 N PHE B 120 123.051 -98.800 29.690 1.00 93.29 N ANISOU 4291 N PHE B 120 8847 16567 10030 3976 22 2127 N ATOM 4292 CA PHE B 120 122.025 -98.632 30.724 1.00 92.99 C ANISOU 4292 CA PHE B 120 8887 16550 9896 4034 77 2298 C ATOM 4293 C PHE B 120 121.846 -97.158 31.118 1.00 95.00 C ANISOU 4293 C PHE B 120 9093 17034 9969 3856 -34 2065 C ATOM 4294 O PHE B 120 120.764 -96.786 31.580 1.00 93.90 O ANISOU 4294 O PHE B 120 9042 16818 9819 3797 23 2134 O ATOM 4295 CB PHE B 120 122.333 -99.496 31.955 1.00 97.78 C ANISOU 4295 CB PHE B 120 9464 17367 10321 4418 127 2592 C ATOM 4296 N GLY B 121 122.878 -96.341 30.899 1.00 90.91 N ANISOU 4296 N GLY B 121 8428 16767 9346 3766 -178 1787 N ATOM 4297 CA GLY B 121 122.827 -94.906 31.156 1.00 89.60 C ANISOU 4297 CA GLY B 121 8198 16780 9063 3574 -288 1523 C ATOM 4298 C GLY B 121 121.873 -94.210 30.204 1.00 89.33 C ANISOU 4298 C GLY B 121 8279 16419 9244 3248 -241 1419 C ATOM 4299 O GLY B 121 121.050 -93.408 30.640 1.00 88.29 O ANISOU 4299 O GLY B 121 8197 16281 9068 3148 -242 1368 O ATOM 4300 N SER B 122 121.956 -94.541 28.900 1.00 83.90 N ANISOU 4300 N SER B 122 7636 15465 8778 3105 -197 1392 N ATOM 4301 CA SER B 122 121.097 -94.000 27.841 1.00 81.25 C ANISOU 4301 CA SER B 122 7412 14819 8640 2822 -160 1309 C ATOM 4302 C SER B 122 119.691 -94.586 27.897 1.00 84.17 C ANISOU 4302 C SER B 122 7942 14891 9148 2829 -55 1518 C ATOM 4303 O SER B 122 118.726 -93.852 27.682 1.00 80.97 O ANISOU 4303 O SER B 122 7607 14339 8820 2643 -47 1466 O ATOM 4304 CB SER B 122 121.696 -94.272 26.470 1.00 83.57 C ANISOU 4304 CB SER B 122 7703 14970 9079 2720 -149 1220 C ATOM 4305 OG SER B 122 123.028 -93.800 26.444 1.00 94.47 O ANISOU 4305 OG SER B 122 8908 16625 10362 2723 -223 1052 O ATOM 4306 N PHE B 123 119.575 -95.908 28.174 1.00 83.05 N ANISOU 4306 N PHE B 123 7844 14645 9066 3042 32 1757 N ATOM 4307 CA PHE B 123 118.295 -96.618 28.274 1.00 83.00 C ANISOU 4307 CA PHE B 123 7959 14335 9243 3060 151 1979 C ATOM 4308 C PHE B 123 117.423 -95.962 29.344 1.00 86.81 C ANISOU 4308 C PHE B 123 8455 14921 9607 3072 183 2053 C ATOM 4309 O PHE B 123 116.217 -95.800 29.141 1.00 84.52 O ANISOU 4309 O PHE B 123 8243 14390 9481 2937 243 2104 O ATOM 4310 CB PHE B 123 118.518 -98.118 28.571 1.00 86.87 C ANISOU 4310 CB PHE B 123 8465 14727 9816 3319 250 2236 C ATOM 4311 CG PHE B 123 117.281 -98.993 28.489 1.00 89.04 C ANISOU 4311 CG PHE B 123 8842 14620 10369 3314 386 2457 C ATOM 4312 CD1 PHE B 123 116.722 -99.329 27.257 1.00 91.04 C ANISOU 4312 CD1 PHE B 123 9168 14511 10913 3129 387 2369 C ATOM 4313 CD2 PHE B 123 116.695 -99.511 29.640 1.00 93.32 C ANISOU 4313 CD2 PHE B 123 9397 15171 10889 3507 517 2754 C ATOM 4314 CE1 PHE B 123 115.582-100.143 27.182 1.00 92.56 C ANISOU 4314 CE1 PHE B 123 9424 14339 11405 3109 498 2545 C ATOM 4315 CE2 PHE B 123 115.559-100.331 29.562 1.00 96.81 C ANISOU 4315 CE2 PHE B 123 9905 15237 11640 3488 661 2968 C ATOM 4316 CZ PHE B 123 115.013-100.644 28.333 1.00 93.71 C ANISOU 4316 CZ PHE B 123 9564 14470 11571 3279 642 2849 C ATOM 4317 N LEU B 124 118.056 -95.535 30.451 1.00 85.85 N ANISOU 4317 N LEU B 124 8250 15176 9195 3234 132 2031 N ATOM 4318 CA LEU B 124 117.405 -94.842 31.559 1.00 86.93 C ANISOU 4318 CA LEU B 124 8393 15486 9152 3284 152 2060 C ATOM 4319 C LEU B 124 116.803 -93.508 31.089 1.00 89.56 C ANISOU 4319 C LEU B 124 8745 15738 9548 2996 95 1821 C ATOM 4320 O LEU B 124 115.636 -93.241 31.367 1.00 88.49 O ANISOU 4320 O LEU B 124 8676 15469 9478 2944 177 1903 O ATOM 4321 CB LEU B 124 118.420 -94.609 32.695 1.00 89.35 C ANISOU 4321 CB LEU B 124 8590 16251 9106 3519 60 2008 C ATOM 4322 CG LEU B 124 117.965 -93.742 33.863 1.00 95.43 C ANISOU 4322 CG LEU B 124 9356 17280 9624 3589 46 1954 C ATOM 4323 CD1 LEU B 124 117.111 -94.532 34.836 1.00 97.83 C ANISOU 4323 CD1 LEU B 124 9741 17576 9854 3837 222 2308 C ATOM 4324 CD2 LEU B 124 119.149 -93.142 34.576 1.00100.14 C ANISOU 4324 CD2 LEU B 124 9812 18323 9911 3709 -129 1729 C ATOM 4325 N THR B 125 117.599 -92.695 30.362 1.00 85.53 N ANISOU 4325 N THR B 125 8167 15293 9038 2818 -29 1545 N ATOM 4326 CA THR B 125 117.226 -91.374 29.846 1.00 83.54 C ANISOU 4326 CA THR B 125 7920 14965 8855 2550 -84 1316 C ATOM 4327 C THR B 125 116.151 -91.495 28.734 1.00 85.40 C ANISOU 4327 C THR B 125 8271 14808 9370 2358 -21 1379 C ATOM 4328 O THR B 125 115.214 -90.694 28.722 1.00 84.86 O ANISOU 4328 O THR B 125 8246 14630 9366 2224 -6 1334 O ATOM 4329 CB THR B 125 118.492 -90.631 29.380 1.00 88.79 C ANISOU 4329 CB THR B 125 8463 15800 9472 2438 -206 1051 C ATOM 4330 OG1 THR B 125 119.452 -90.658 30.437 1.00 85.00 O ANISOU 4330 OG1 THR B 125 7857 15691 8747 2637 -285 994 O ATOM 4331 CG2 THR B 125 118.230 -89.188 29.009 1.00 87.64 C ANISOU 4331 CG2 THR B 125 8307 15598 9395 2185 -253 823 C ATOM 4332 N LEU B 126 116.276 -92.499 27.833 1.00 80.37 N ANISOU 4332 N LEU B 126 7676 13969 8892 2362 8 1471 N ATOM 4333 CA LEU B 126 115.348 -92.761 26.724 1.00 78.08 C ANISOU 4333 CA LEU B 126 7484 13329 8855 2205 38 1504 C ATOM 4334 C LEU B 126 113.916 -93.004 27.216 1.00 79.91 C ANISOU 4334 C LEU B 126 7774 13376 9213 2218 130 1683 C ATOM 4335 O LEU B 126 112.980 -92.484 26.619 1.00 77.76 O ANISOU 4335 O LEU B 126 7547 12908 9089 2044 119 1636 O ATOM 4336 CB LEU B 126 115.827 -93.981 25.917 1.00 78.56 C ANISOU 4336 CB LEU B 126 7570 13245 9034 2271 54 1563 C ATOM 4337 CG LEU B 126 115.205 -94.180 24.533 1.00 82.10 C ANISOU 4337 CG LEU B 126 8106 13385 9702 2106 35 1505 C ATOM 4338 CD1 LEU B 126 116.244 -94.643 23.560 1.00 82.35 C ANISOU 4338 CD1 LEU B 126 8135 13425 9729 2122 3 1401 C ATOM 4339 CD2 LEU B 126 114.070 -95.192 24.569 1.00 85.42 C ANISOU 4339 CD2 LEU B 126 8587 13513 10357 2144 107 1683 C ATOM 4340 N ASN B 127 113.756 -93.817 28.277 1.00 77.17 N ANISOU 4340 N ASN B 127 7417 13091 8815 2433 228 1904 N ATOM 4341 CA ASN B 127 112.456 -94.172 28.848 1.00 76.49 C ANISOU 4341 CA ASN B 127 7362 12838 8861 2473 355 2119 C ATOM 4342 C ASN B 127 111.940 -93.123 29.822 1.00 78.32 C ANISOU 4342 C ASN B 127 7577 13257 8925 2485 380 2090 C ATOM 4343 O ASN B 127 110.726 -93.033 30.000 1.00 77.16 O ANISOU 4343 O ASN B 127 7450 12945 8921 2438 470 2198 O ATOM 4344 CB ASN B 127 112.521 -95.535 29.525 1.00 77.80 C ANISOU 4344 CB ASN B 127 7527 12970 9062 2713 484 2405 C ATOM 4345 CG ASN B 127 112.680 -96.661 28.541 1.00 93.57 C ANISOU 4345 CG ASN B 127 9553 14684 11317 2690 487 2444 C ATOM 4346 OD1 ASN B 127 113.706 -97.339 28.505 1.00 84.57 O ANISOU 4346 OD1 ASN B 127 8396 13627 10108 2832 473 2465 O ATOM 4347 ND2 ASN B 127 111.685 -96.856 27.688 1.00 86.82 N ANISOU 4347 ND2 ASN B 127 8733 13492 10762 2514 491 2427 N ATOM 4348 N MET B 128 112.839 -92.339 30.454 1.00 74.73 N ANISOU 4348 N MET B 128 7073 13140 8182 2549 301 1930 N ATOM 4349 CA MET B 128 112.429 -91.270 31.367 1.00 75.01 C ANISOU 4349 CA MET B 128 7094 13364 8043 2564 307 1843 C ATOM 4350 C MET B 128 111.743 -90.171 30.547 1.00 76.20 C ANISOU 4350 C MET B 128 7269 13323 8362 2298 257 1661 C ATOM 4351 O MET B 128 110.653 -89.739 30.920 1.00 75.21 O ANISOU 4351 O MET B 128 7165 13118 8294 2275 334 1712 O ATOM 4352 CB MET B 128 113.618 -90.724 32.176 1.00 78.71 C ANISOU 4352 CB MET B 128 7488 14231 8185 2690 203 1668 C ATOM 4353 CG MET B 128 113.250 -89.609 33.135 1.00 83.24 C ANISOU 4353 CG MET B 128 8049 15009 8569 2718 195 1527 C ATOM 4354 SD MET B 128 114.570 -88.381 33.348 1.00 88.52 S ANISOU 4354 SD MET B 128 8609 15997 9027 2656 -7 1125 S ATOM 4355 CE MET B 128 114.522 -87.544 31.755 1.00 82.82 C ANISOU 4355 CE MET B 128 7895 14953 8620 2289 -69 934 C ATOM 4356 N PHE B 129 112.345 -89.782 29.401 1.00 71.21 N ANISOU 4356 N PHE B 129 6633 12607 7819 2114 145 1479 N ATOM 4357 CA PHE B 129 111.784 -88.783 28.493 1.00 69.87 C ANISOU 4357 CA PHE B 129 6491 12249 7806 1877 98 1335 C ATOM 4358 C PHE B 129 110.521 -89.306 27.806 1.00 73.14 C ANISOU 4358 C PHE B 129 6964 12340 8485 1799 154 1488 C ATOM 4359 O PHE B 129 109.555 -88.555 27.712 1.00 73.05 O ANISOU 4359 O PHE B 129 6967 12212 8575 1697 168 1462 O ATOM 4360 CB PHE B 129 112.808 -88.328 27.444 1.00 71.17 C ANISOU 4360 CB PHE B 129 6637 12423 7983 1731 -7 1146 C ATOM 4361 CG PHE B 129 113.775 -87.268 27.918 1.00 73.95 C ANISOU 4361 CG PHE B 129 6905 13023 8170 1703 -79 921 C ATOM 4362 CD1 PHE B 129 113.318 -86.031 28.361 1.00 77.99 C ANISOU 4362 CD1 PHE B 129 7407 13557 8670 1622 -87 783 C ATOM 4363 CD2 PHE B 129 115.146 -87.487 27.878 1.00 77.04 C ANISOU 4363 CD2 PHE B 129 7212 13610 8448 1750 -141 829 C ATOM 4364 CE1 PHE B 129 114.219 -85.043 28.785 1.00 80.19 C ANISOU 4364 CE1 PHE B 129 7594 14036 8839 1580 -163 540 C ATOM 4365 CE2 PHE B 129 116.045 -86.494 28.293 1.00 81.20 C ANISOU 4365 CE2 PHE B 129 7631 14354 8867 1704 -220 596 C ATOM 4366 CZ PHE B 129 115.577 -85.282 28.749 1.00 79.89 C ANISOU 4366 CZ PHE B 129 7458 14193 8705 1614 -234 445 C ATOM 4367 N ALA B 130 110.508 -90.586 27.358 1.00 69.07 N ANISOU 4367 N ALA B 130 6469 11675 8098 1852 182 1634 N ATOM 4368 CA ALA B 130 109.341 -91.207 26.713 1.00 68.35 C ANISOU 4368 CA ALA B 130 6409 11270 8290 1778 217 1755 C ATOM 4369 C ALA B 130 108.133 -91.246 27.661 1.00 74.28 C ANISOU 4369 C ALA B 130 7134 11967 9121 1844 347 1932 C ATOM 4370 O ALA B 130 107.003 -91.112 27.206 1.00 73.21 O ANISOU 4370 O ALA B 130 6995 11612 9211 1731 355 1961 O ATOM 4371 CB ALA B 130 109.679 -92.604 26.240 1.00 69.57 C ANISOU 4371 CB ALA B 130 6579 11287 8567 1846 229 1854 C ATOM 4372 N SER B 131 108.376 -91.384 28.980 1.00 73.46 N ANISOU 4372 N SER B 131 7006 12086 8820 2039 450 2047 N ATOM 4373 CA SER B 131 107.331 -91.351 30.008 1.00 74.52 C ANISOU 4373 CA SER B 131 7115 12227 8973 2138 605 2225 C ATOM 4374 C SER B 131 106.780 -89.921 30.156 1.00 76.27 C ANISOU 4374 C SER B 131 7332 12507 9139 2038 575 2060 C ATOM 4375 O SER B 131 105.565 -89.757 30.229 1.00 75.71 O ANISOU 4375 O SER B 131 7239 12281 9248 1995 659 2151 O ATOM 4376 CB SER B 131 107.874 -91.853 31.344 1.00 80.76 C ANISOU 4376 CB SER B 131 7894 13288 9501 2406 715 2386 C ATOM 4377 OG SER B 131 106.959 -91.619 32.403 1.00 90.56 O ANISOU 4377 OG SER B 131 9119 14602 10689 2522 874 2535 O ATOM 4378 N ILE B 132 107.678 -88.896 30.180 1.00 71.29 N ANISOU 4378 N ILE B 132 6711 12085 8292 1998 460 1813 N ATOM 4379 CA ILE B 132 107.346 -87.468 30.308 1.00 70.16 C ANISOU 4379 CA ILE B 132 6566 11989 8104 1904 424 1619 C ATOM 4380 C ILE B 132 106.593 -86.978 29.059 1.00 71.42 C ANISOU 4380 C ILE B 132 6742 11860 8533 1684 360 1561 C ATOM 4381 O ILE B 132 105.578 -86.286 29.187 1.00 70.73 O ANISOU 4381 O ILE B 132 6644 11680 8549 1640 406 1560 O ATOM 4382 CB ILE B 132 108.617 -86.598 30.567 1.00 73.50 C ANISOU 4382 CB ILE B 132 6974 12671 8282 1900 310 1358 C ATOM 4383 CG1 ILE B 132 109.330 -86.992 31.878 1.00 76.00 C ANISOU 4383 CG1 ILE B 132 7263 13322 8294 2144 344 1390 C ATOM 4384 CG2 ILE B 132 108.264 -85.118 30.595 1.00 74.45 C ANISOU 4384 CG2 ILE B 132 7093 12778 8419 1783 276 1145 C ATOM 4385 CD1 ILE B 132 110.810 -86.541 31.987 1.00 82.43 C ANISOU 4385 CD1 ILE B 132 8025 14392 8901 2147 200 1148 C ATOM 4386 N PHE B 133 107.096 -87.335 27.863 1.00 65.87 N ANISOU 4386 N PHE B 133 6065 11035 7930 1567 256 1516 N ATOM 4387 CA PHE B 133 106.535 -86.921 26.582 1.00 63.99 C ANISOU 4387 CA PHE B 133 5853 10565 7896 1386 172 1457 C ATOM 4388 C PHE B 133 105.178 -87.581 26.309 1.00 68.66 C ANISOU 4388 C PHE B 133 6422 10915 8751 1367 218 1625 C ATOM 4389 O PHE B 133 104.390 -87.000 25.566 1.00 68.31 O ANISOU 4389 O PHE B 133 6378 10712 8864 1249 160 1584 O ATOM 4390 CB PHE B 133 107.511 -87.195 25.424 1.00 64.55 C ANISOU 4390 CB PHE B 133 5962 10612 7953 1303 61 1365 C ATOM 4391 CG PHE B 133 108.871 -86.515 25.426 1.00 65.10 C ANISOU 4391 CG PHE B 133 6025 10883 7827 1280 9 1192 C ATOM 4392 CD1 PHE B 133 109.148 -85.465 26.299 1.00 67.78 C ANISOU 4392 CD1 PHE B 133 6329 11389 8035 1293 24 1069 C ATOM 4393 CD2 PHE B 133 109.858 -86.899 24.526 1.00 66.20 C ANISOU 4393 CD2 PHE B 133 6181 11037 7934 1241 -55 1134 C ATOM 4394 CE1 PHE B 133 110.399 -84.840 26.295 1.00 68.59 C ANISOU 4394 CE1 PHE B 133 6394 11659 8007 1253 -32 891 C ATOM 4395 CE2 PHE B 133 111.106 -86.266 24.517 1.00 68.70 C ANISOU 4395 CE2 PHE B 133 6462 11532 8110 1209 -90 982 C ATOM 4396 CZ PHE B 133 111.370 -85.244 25.405 1.00 67.11 C ANISOU 4396 CZ PHE B 133 6206 11483 7809 1206 -83 859 C ATOM 4397 N PHE B 134 104.886 -88.762 26.908 1.00 66.10 N ANISOU 4397 N PHE B 134 6064 10556 8494 1487 324 1818 N ATOM 4398 CA PHE B 134 103.579 -89.404 26.721 1.00 66.43 C ANISOU 4398 CA PHE B 134 6050 10352 8838 1457 382 1976 C ATOM 4399 C PHE B 134 102.562 -88.841 27.726 1.00 73.85 C ANISOU 4399 C PHE B 134 6930 11325 9804 1519 523 2074 C ATOM 4400 O PHE B 134 101.364 -88.863 27.432 1.00 74.37 O ANISOU 4400 O PHE B 134 6929 11195 10134 1450 544 2146 O ATOM 4401 CB PHE B 134 103.641 -90.945 26.767 1.00 68.62 C ANISOU 4401 CB PHE B 134 6307 10508 9258 1532 446 2147 C ATOM 4402 CG PHE B 134 103.986 -91.607 25.443 1.00 68.88 C ANISOU 4402 CG PHE B 134 6375 10370 9425 1431 301 2049 C ATOM 4403 CD1 PHE B 134 103.167 -91.445 24.327 1.00 70.80 C ANISOU 4403 CD1 PHE B 134 6603 10407 9891 1279 177 1959 C ATOM 4404 CD2 PHE B 134 105.103 -92.428 25.326 1.00 70.17 C ANISOU 4404 CD2 PHE B 134 6583 10591 9488 1509 287 2043 C ATOM 4405 CE1 PHE B 134 103.491 -92.049 23.107 1.00 70.87 C ANISOU 4405 CE1 PHE B 134 6655 10288 9984 1209 36 1843 C ATOM 4406 CE2 PHE B 134 105.427 -93.027 24.106 1.00 72.21 C ANISOU 4406 CE2 PHE B 134 6881 10702 9853 1434 162 1931 C ATOM 4407 CZ PHE B 134 104.620 -92.833 23.006 1.00 69.91 C ANISOU 4407 CZ PHE B 134 6587 10222 9753 1286 37 1824 C ATOM 4408 N ILE B 135 103.032 -88.280 28.874 1.00 72.12 N ANISOU 4408 N ILE B 135 6727 11365 9309 1652 608 2053 N ATOM 4409 CA ILE B 135 102.169 -87.612 29.869 1.00 73.50 C ANISOU 4409 CA ILE B 135 6860 11615 9451 1736 748 2107 C ATOM 4410 C ILE B 135 101.598 -86.346 29.206 1.00 76.37 C ANISOU 4410 C ILE B 135 7222 11875 9918 1587 654 1936 C ATOM 4411 O ILE B 135 100.422 -86.017 29.390 1.00 76.90 O ANISOU 4411 O ILE B 135 7226 11836 10155 1583 736 2009 O ATOM 4412 CB ILE B 135 102.940 -87.300 31.195 1.00 78.02 C ANISOU 4412 CB ILE B 135 7464 12524 9658 1930 827 2073 C ATOM 4413 CG1 ILE B 135 103.070 -88.559 32.066 1.00 80.71 C ANISOU 4413 CG1 ILE B 135 7789 12953 9924 2131 983 2337 C ATOM 4414 CG2 ILE B 135 102.295 -86.153 32.003 1.00 79.10 C ANISOU 4414 CG2 ILE B 135 7587 12769 9699 1988 910 1989 C ATOM 4415 CD1 ILE B 135 104.241 -88.515 33.084 1.00 92.09 C ANISOU 4415 CD1 ILE B 135 9271 14757 10961 2331 985 2283 C ATOM 4416 N THR B 136 102.449 -85.672 28.403 1.00 71.18 N ANISOU 4416 N THR B 136 6628 11241 9176 1471 492 1728 N ATOM 4417 CA THR B 136 102.153 -84.464 27.637 1.00 69.95 C ANISOU 4417 CA THR B 136 6491 10984 9105 1333 393 1574 C ATOM 4418 C THR B 136 101.094 -84.777 26.567 1.00 75.83 C ANISOU 4418 C THR B 136 7196 11467 10149 1225 329 1660 C ATOM 4419 O THR B 136 100.109 -84.045 26.473 1.00 76.30 O ANISOU 4419 O THR B 136 7214 11426 10353 1194 342 1661 O ATOM 4420 CB THR B 136 103.445 -83.906 27.054 1.00 68.85 C ANISOU 4420 CB THR B 136 6417 10932 8810 1251 268 1382 C ATOM 4421 OG1 THR B 136 104.402 -83.782 28.108 1.00 68.16 O ANISOU 4421 OG1 THR B 136 6334 11100 8464 1361 310 1297 O ATOM 4422 CG2 THR B 136 103.256 -82.565 26.413 1.00 65.19 C ANISOU 4422 CG2 THR B 136 5977 10375 8418 1130 200 1243 C ATOM 4423 N CYS B 137 101.268 -85.889 25.811 1.00 73.01 N ANISOU 4423 N CYS B 137 6842 11006 9893 1185 259 1723 N ATOM 4424 CA CYS B 137 100.325 -86.372 24.795 1.00 73.31 C ANISOU 4424 CA CYS B 137 6830 10811 10212 1092 169 1774 C ATOM 4425 C CYS B 137 98.942 -86.563 25.413 1.00 78.65 C ANISOU 4425 C CYS B 137 7382 11378 11123 1131 292 1930 C ATOM 4426 O CYS B 137 97.942 -86.126 24.845 1.00 77.51 O ANISOU 4426 O CYS B 137 7174 11096 11182 1061 227 1923 O ATOM 4427 CB CYS B 137 100.830 -87.674 24.175 1.00 73.94 C ANISOU 4427 CB CYS B 137 6931 10818 10346 1077 103 1798 C ATOM 4428 SG CYS B 137 102.238 -87.472 23.059 1.00 76.82 S ANISOU 4428 SG CYS B 137 7421 11267 10498 1013 -56 1615 S ATOM 4429 N MET B 138 98.908 -87.202 26.598 1.00 78.29 N ANISOU 4429 N MET B 138 7295 11410 11042 1258 478 2083 N ATOM 4430 CA MET B 138 97.705 -87.492 27.371 1.00 80.70 C ANISOU 4430 CA MET B 138 7472 11638 11552 1322 654 2272 C ATOM 4431 C MET B 138 96.967 -86.221 27.789 1.00 85.48 C ANISOU 4431 C MET B 138 8042 12292 12145 1344 711 2225 C ATOM 4432 O MET B 138 95.734 -86.207 27.762 1.00 86.08 O ANISOU 4432 O MET B 138 7990 12225 12491 1324 767 2322 O ATOM 4433 CB MET B 138 98.048 -88.330 28.613 1.00 84.67 C ANISOU 4433 CB MET B 138 7969 12267 11934 1490 864 2459 C ATOM 4434 CG MET B 138 98.036 -89.835 28.370 1.00 89.80 C ANISOU 4434 CG MET B 138 8572 12745 12802 1482 894 2619 C ATOM 4435 SD MET B 138 96.598 -90.474 27.447 1.00 95.94 S ANISOU 4435 SD MET B 138 9180 13160 14113 1322 839 2685 S ATOM 4436 CE MET B 138 95.205 -89.988 28.548 1.00 94.52 C ANISOU 4436 CE MET B 138 8843 12987 14082 1406 1091 2881 C ATOM 4437 N SER B 139 97.713 -85.164 28.166 1.00 81.67 N ANISOU 4437 N SER B 139 7660 11996 11376 1385 698 2067 N ATOM 4438 CA SER B 139 97.136 -83.882 28.574 1.00 81.91 C ANISOU 4438 CA SER B 139 7674 12063 11386 1415 751 1986 C ATOM 4439 C SER B 139 96.566 -83.120 27.367 1.00 83.90 C ANISOU 4439 C SER B 139 7909 12132 11836 1276 587 1895 C ATOM 4440 O SER B 139 95.511 -82.495 27.494 1.00 84.47 O ANISOU 4440 O SER B 139 7899 12126 12070 1294 642 1925 O ATOM 4441 CB SER B 139 98.163 -83.031 29.314 1.00 85.94 C ANISOU 4441 CB SER B 139 8288 12806 11561 1491 769 1811 C ATOM 4442 OG SER B 139 98.160 -83.329 30.702 1.00 95.99 O ANISOU 4442 OG SER B 139 9545 14273 12654 1677 961 1900 O ATOM 4443 N VAL B 140 97.242 -83.203 26.201 1.00 78.32 N ANISOU 4443 N VAL B 140 7279 11369 11112 1159 396 1801 N ATOM 4444 CA VAL B 140 96.814 -82.563 24.949 1.00 77.57 C ANISOU 4444 CA VAL B 140 7187 11126 11159 1049 227 1736 C ATOM 4445 C VAL B 140 95.537 -83.251 24.426 1.00 83.55 C ANISOU 4445 C VAL B 140 7803 11704 12237 1014 181 1857 C ATOM 4446 O VAL B 140 94.632 -82.566 23.944 1.00 83.55 O ANISOU 4446 O VAL B 140 7739 11604 12403 991 118 1855 O ATOM 4447 CB VAL B 140 97.941 -82.549 23.883 1.00 79.65 C ANISOU 4447 CB VAL B 140 7573 11411 11280 960 62 1621 C ATOM 4448 CG1 VAL B 140 97.447 -81.979 22.551 1.00 79.18 C ANISOU 4448 CG1 VAL B 140 7524 11218 11342 878 -106 1589 C ATOM 4449 CG2 VAL B 140 99.158 -81.768 24.379 1.00 78.76 C ANISOU 4449 CG2 VAL B 140 7561 11460 10905 975 104 1487 C ATOM 4450 N ASP B 141 95.460 -84.591 24.550 1.00 81.63 N ANISOU 4450 N ASP B 141 7500 11414 12103 1015 214 1961 N ATOM 4451 CA ASP B 141 94.311 -85.386 24.111 1.00 83.49 C ANISOU 4451 CA ASP B 141 7574 11462 12686 966 171 2058 C ATOM 4452 C ASP B 141 93.066 -85.081 24.965 1.00 89.02 C ANISOU 4452 C ASP B 141 8110 12121 13590 1030 345 2190 C ATOM 4453 O ASP B 141 91.997 -84.824 24.402 1.00 88.41 O ANISOU 4453 O ASP B 141 7902 11917 13771 984 259 2198 O ATOM 4454 CB ASP B 141 94.645 -86.887 24.147 1.00 86.27 C ANISOU 4454 CB ASP B 141 7904 11749 13125 953 194 2133 C ATOM 4455 CG ASP B 141 93.843 -87.702 23.152 1.00 99.23 C ANISOU 4455 CG ASP B 141 9421 13176 15104 850 35 2121 C ATOM 4456 OD1 ASP B 141 94.121 -87.597 21.935 1.00 98.67 O ANISOU 4456 OD1 ASP B 141 9422 13079 14990 777 -198 1969 O ATOM 4457 OD2 ASP B 141 92.936 -88.440 23.588 1.00108.37 O ANISOU 4457 OD2 ASP B 141 10405 14197 16574 846 144 2260 O ATOM 4458 N ARG B 142 93.222 -85.069 26.314 1.00 86.69 N ANISOU 4458 N ARG B 142 7821 11957 13161 1154 589 2288 N ATOM 4459 CA ARG B 142 92.160 -84.751 27.274 1.00 88.17 C ANISOU 4459 CA ARG B 142 7870 12149 13483 1250 803 2419 C ATOM 4460 C ARG B 142 91.629 -83.336 27.045 1.00 93.14 C ANISOU 4460 C ARG B 142 8494 12776 14120 1258 750 2310 C ATOM 4461 O ARG B 142 90.433 -83.105 27.220 1.00 94.25 O ANISOU 4461 O ARG B 142 8469 12833 14510 1286 831 2397 O ATOM 4462 CB ARG B 142 92.650 -84.904 28.722 1.00 88.58 C ANISOU 4462 CB ARG B 142 7977 12399 13282 1413 1057 2513 C ATOM 4463 CG ARG B 142 92.645 -86.342 29.219 1.00101.78 C ANISOU 4463 CG ARG B 142 9582 14032 15059 1454 1205 2730 C ATOM 4464 CD ARG B 142 93.104 -86.448 30.663 1.00112.08 C ANISOU 4464 CD ARG B 142 10947 15569 16070 1653 1457 2847 C ATOM 4465 NE ARG B 142 92.756 -87.745 31.247 1.00121.84 N ANISOU 4465 NE ARG B 142 12080 16736 17478 1719 1665 3130 N ATOM 4466 CZ ARG B 142 92.813 -88.032 32.547 1.00139.16 C ANISOU 4466 CZ ARG B 142 14281 19106 19489 1920 1938 3323 C ATOM 4467 NH1 ARG B 142 93.205 -87.114 33.422 1.00127.55 N ANISOU 4467 NH1 ARG B 142 12915 17911 17637 2078 2015 3226 N ATOM 4468 NH2 ARG B 142 92.470 -89.238 32.981 1.00127.22 N ANISOU 4468 NH2 ARG B 142 12668 17492 18176 1972 2138 3614 N ATOM 4469 N TYR B 143 92.506 -82.401 26.632 1.00 89.17 N ANISOU 4469 N TYR B 143 8157 12347 13375 1233 624 2129 N ATOM 4470 CA TYR B 143 92.121 -81.025 26.330 1.00 89.66 C ANISOU 4470 CA TYR B 143 8235 12378 13456 1239 571 2027 C ATOM 4471 C TYR B 143 91.359 -80.970 25.009 1.00 94.91 C ANISOU 4471 C TYR B 143 8814 12871 14376 1143 359 2034 C ATOM 4472 O TYR B 143 90.348 -80.274 24.930 1.00 95.99 O ANISOU 4472 O TYR B 143 8842 12931 14700 1179 368 2061 O ATOM 4473 CB TYR B 143 93.344 -80.099 26.303 1.00 90.15 C ANISOU 4473 CB TYR B 143 8487 12546 13220 1231 519 1845 C ATOM 4474 CG TYR B 143 93.062 -78.737 25.706 1.00 92.98 C ANISOU 4474 CG TYR B 143 8877 12814 13638 1211 434 1750 C ATOM 4475 CD1 TYR B 143 92.372 -77.767 26.426 1.00 96.44 C ANISOU 4475 CD1 TYR B 143 9265 13241 14135 1312 572 1727 C ATOM 4476 CD2 TYR B 143 93.467 -78.424 24.410 1.00 93.11 C ANISOU 4476 CD2 TYR B 143 8973 12752 13652 1110 231 1695 C ATOM 4477 CE1 TYR B 143 92.095 -76.517 25.874 1.00 98.29 C ANISOU 4477 CE1 TYR B 143 9527 13363 14456 1305 506 1655 C ATOM 4478 CE2 TYR B 143 93.194 -77.180 23.847 1.00 94.47 C ANISOU 4478 CE2 TYR B 143 9175 12827 13890 1109 170 1648 C ATOM 4479 CZ TYR B 143 92.514 -76.227 24.585 1.00105.68 C ANISOU 4479 CZ TYR B 143 10544 14213 15399 1203 307 1629 C ATOM 4480 OH TYR B 143 92.246 -75.001 24.029 1.00111.08 O ANISOU 4480 OH TYR B 143 11258 14774 16173 1213 257 1596 O ATOM 4481 N GLN B 144 91.845 -81.704 23.983 1.00 91.12 N ANISOU 4481 N GLN B 144 8383 12347 13893 1040 166 2000 N ATOM 4482 CA GLN B 144 91.258 -81.790 22.638 1.00 91.37 C ANISOU 4482 CA GLN B 144 8352 12254 14110 962 -74 1979 C ATOM 4483 C GLN B 144 89.834 -82.355 22.686 1.00 96.98 C ANISOU 4483 C GLN B 144 8813 12840 15194 959 -63 2090 C ATOM 4484 O GLN B 144 88.974 -81.900 21.930 1.00 96.97 O ANISOU 4484 O GLN B 144 8711 12762 15374 950 -213 2080 O ATOM 4485 CB GLN B 144 92.143 -82.669 21.734 1.00 91.83 C ANISOU 4485 CB GLN B 144 8515 12318 14059 877 -245 1907 C ATOM 4486 CG GLN B 144 92.279 -82.148 20.307 1.00105.82 C ANISOU 4486 CG GLN B 144 10368 14069 15768 833 -493 1815 C ATOM 4487 CD GLN B 144 93.351 -82.839 19.489 1.00124.81 C ANISOU 4487 CD GLN B 144 12913 16518 17989 777 -626 1725 C ATOM 4488 OE1 GLN B 144 94.212 -83.573 20.000 1.00122.21 O ANISOU 4488 OE1 GLN B 144 12647 16245 17542 769 -533 1716 O ATOM 4489 NE2 GLN B 144 93.347 -82.574 18.189 1.00112.04 N ANISOU 4489 NE2 GLN B 144 11354 14895 16322 757 -843 1660 N ATOM 4490 N SER B 145 89.595 -83.337 23.587 1.00 94.64 N ANISOU 4490 N SER B 145 8407 12527 15023 975 121 2208 N ATOM 4491 CA SER B 145 88.301 -83.989 23.781 1.00 96.26 C ANISOU 4491 CA SER B 145 8349 12602 15624 961 183 2335 C ATOM 4492 C SER B 145 87.327 -83.090 24.570 1.00102.36 C ANISOU 4492 C SER B 145 8990 13391 16511 1066 368 2423 C ATOM 4493 O SER B 145 86.125 -83.111 24.288 1.00103.42 O ANISOU 4493 O SER B 145 8895 13415 16984 1050 326 2478 O ATOM 4494 CB SER B 145 88.482 -85.328 24.489 1.00 98.91 C ANISOU 4494 CB SER B 145 8627 12900 16052 950 353 2462 C ATOM 4495 OG SER B 145 88.900 -85.157 25.833 1.00104.09 O ANISOU 4495 OG SER B 145 9357 13698 16493 1075 639 2564 O ATOM 4496 N VAL B 146 87.849 -82.306 25.548 1.00 98.85 N ANISOU 4496 N VAL B 146 8680 13089 15789 1180 564 2415 N ATOM 4497 CA VAL B 146 87.081 -81.390 26.405 1.00100.07 C ANISOU 4497 CA VAL B 146 8749 13282 15992 1308 766 2466 C ATOM 4498 C VAL B 146 86.455 -80.263 25.554 1.00105.29 C ANISOU 4498 C VAL B 146 9371 13865 16770 1308 593 2384 C ATOM 4499 O VAL B 146 85.331 -79.851 25.846 1.00107.41 O ANISOU 4499 O VAL B 146 9453 14083 17274 1380 689 2460 O ATOM 4500 CB VAL B 146 87.959 -80.858 27.583 1.00103.22 C ANISOU 4500 CB VAL B 146 9330 13866 16022 1432 976 2418 C ATOM 4501 CG1 VAL B 146 87.709 -79.388 27.903 1.00103.20 C ANISOU 4501 CG1 VAL B 146 9370 13898 15942 1534 1036 2314 C ATOM 4502 CG2 VAL B 146 87.783 -81.714 28.831 1.00104.49 C ANISOU 4502 CG2 VAL B 146 9413 14113 16177 1530 1265 2593 C ATOM 4503 N ILE B 147 87.146 -79.807 24.490 1.00100.51 N ANISOU 4503 N ILE B 147 8927 13249 16014 1240 348 2254 N ATOM 4504 CA ILE B 147 86.632 -78.744 23.619 1.00100.67 C ANISOU 4504 CA ILE B 147 8931 13197 16121 1259 181 2207 C ATOM 4505 C ILE B 147 85.743 -79.318 22.486 1.00105.98 C ANISOU 4505 C ILE B 147 9418 13766 17082 1188 -66 2241 C ATOM 4506 O ILE B 147 84.627 -78.827 22.288 1.00107.01 O ANISOU 4506 O ILE B 147 9367 13833 17460 1245 -102 2292 O ATOM 4507 CB ILE B 147 87.775 -77.858 23.031 1.00101.95 C ANISOU 4507 CB ILE B 147 9353 13398 15985 1239 66 2079 C ATOM 4508 CG1 ILE B 147 88.852 -77.446 24.081 1.00101.02 C ANISOU 4508 CG1 ILE B 147 9415 13393 15576 1279 262 1995 C ATOM 4509 CG2 ILE B 147 87.216 -76.630 22.300 1.00103.86 C ANISOU 4509 CG2 ILE B 147 9587 13557 16320 1295 -48 2072 C ATOM 4510 CD1 ILE B 147 88.405 -76.604 25.324 1.00105.31 C ANISOU 4510 CD1 ILE B 147 9919 13968 16127 1417 513 1984 C ATOM 4511 N TYR B 148 86.270 -80.296 21.707 1.00102.46 N ANISOU 4511 N TYR B 148 9022 13314 16595 1076 -252 2191 N ATOM 4512 CA TYR B 148 85.594 -80.872 20.536 1.00103.73 C ANISOU 4512 CA TYR B 148 9035 13397 16979 1007 -532 2163 C ATOM 4513 C TYR B 148 85.497 -82.415 20.549 1.00111.09 C ANISOU 4513 C TYR B 148 9842 14262 18107 900 -556 2169 C ATOM 4514 O TYR B 148 86.535 -83.088 20.531 1.00109.24 O ANISOU 4514 O TYR B 148 9771 14059 17675 845 -552 2119 O ATOM 4515 CB TYR B 148 86.295 -80.465 19.204 1.00103.03 C ANISOU 4515 CB TYR B 148 9143 13353 16649 988 -809 2051 C ATOM 4516 CG TYR B 148 87.240 -79.280 19.251 1.00101.71 C ANISOU 4516 CG TYR B 148 9228 13256 16162 1044 -738 2025 C ATOM 4517 CD1 TYR B 148 88.520 -79.405 19.782 1.00101.31 C ANISOU 4517 CD1 TYR B 148 9379 13279 15836 1012 -603 1978 C ATOM 4518 CD2 TYR B 148 86.901 -78.070 18.652 1.00102.88 C ANISOU 4518 CD2 TYR B 148 9408 13388 16295 1125 -830 2043 C ATOM 4519 CE1 TYR B 148 89.395 -78.322 19.824 1.00100.36 C ANISOU 4519 CE1 TYR B 148 9460 13205 15469 1043 -542 1935 C ATOM 4520 CE2 TYR B 148 87.778 -76.987 18.662 1.00102.41 C ANISOU 4520 CE2 TYR B 148 9568 13352 15992 1161 -755 2022 C ATOM 4521 CZ TYR B 148 89.018 -77.113 19.263 1.00106.88 C ANISOU 4521 CZ TYR B 148 10309 13981 16318 1109 -610 1958 C ATOM 4522 OH TYR B 148 89.890 -76.053 19.266 1.00106.94 O ANISOU 4522 OH TYR B 148 10505 13996 16131 1125 -542 1919 O ATOM 4523 N PRO B 149 84.278 -83.000 20.427 1.00112.29 N ANISOU 4523 N PRO B 149 9695 14303 18668 862 -611 2215 N ATOM 4524 CA PRO B 149 84.174 -84.465 20.321 1.00113.70 C ANISOU 4524 CA PRO B 149 9742 14371 19086 743 -653 2202 C ATOM 4525 C PRO B 149 84.129 -84.898 18.835 1.00119.59 C ANISOU 4525 C PRO B 149 10477 15085 19877 664 -1044 2020 C ATOM 4526 O PRO B 149 83.199 -85.594 18.412 1.00121.39 O ANISOU 4526 O PRO B 149 10442 15197 20485 590 -1194 1977 O ATOM 4527 CB PRO B 149 82.869 -84.768 21.072 1.00117.76 C ANISOU 4527 CB PRO B 149 9920 14778 20048 745 -472 2350 C ATOM 4528 CG PRO B 149 82.086 -83.449 21.058 1.00122.68 C ANISOU 4528 CG PRO B 149 10461 15456 20697 859 -479 2382 C ATOM 4529 CD PRO B 149 82.936 -82.386 20.407 1.00116.10 C ANISOU 4529 CD PRO B 149 9922 14740 19450 923 -630 2277 C ATOM 4530 N PHE B 150 85.138 -84.449 18.038 1.00114.96 N ANISOU 4530 N PHE B 150 10169 14610 18898 688 -1209 1905 N ATOM 4531 CA PHE B 150 85.278 -84.715 16.598 1.00143.01 C ANISOU 4531 CA PHE B 150 13776 18189 22373 655 -1569 1727 C ATOM 4532 C PHE B 150 86.603 -85.403 16.293 1.00172.79 C ANISOU 4532 C PHE B 150 17794 21999 25860 608 -1594 1626 C ATOM 4533 O PHE B 150 86.615 -86.476 15.695 1.00136.61 O ANISOU 4533 O PHE B 150 13160 17345 21402 531 -1764 1493 O ATOM 4534 CB PHE B 150 85.174 -83.409 15.791 1.00144.63 C ANISOU 4534 CB PHE B 150 14080 18510 22361 763 -1738 1715 C ATOM 4535 N ALA B 160 97.433 -90.939 15.248 1.00 79.58 N ANISOU 4535 N ALA B 160 7541 10568 12128 606 -1309 1033 N ATOM 4536 CA ALA B 160 98.001 -91.528 16.461 1.00 78.35 C ANISOU 4536 CA ALA B 160 7375 10386 12009 635 -1072 1168 C ATOM 4537 C ALA B 160 99.033 -92.604 16.132 1.00 81.30 C ANISOU 4537 C ALA B 160 7845 10739 12308 671 -1079 1072 C ATOM 4538 O ALA B 160 99.719 -93.093 17.035 1.00 79.81 O ANISOU 4538 O ALA B 160 7673 10562 12090 723 -895 1183 O ATOM 4539 CB ALA B 160 96.900 -92.110 17.327 1.00 80.48 C ANISOU 4539 CB ALA B 160 7446 10465 12670 600 -965 1303 C ATOM 4540 N SER B 161 99.142 -92.971 14.837 1.00 78.85 N ANISOU 4540 N SER B 161 7598 10409 11954 663 -1293 863 N ATOM 4541 CA SER B 161 100.130 -93.945 14.361 1.00 78.79 C ANISOU 4541 CA SER B 161 7692 10386 11859 711 -1314 735 C ATOM 4542 C SER B 161 101.398 -93.213 13.900 1.00 80.17 C ANISOU 4542 C SER B 161 8046 10813 11603 775 -1297 696 C ATOM 4543 O SER B 161 102.376 -93.855 13.516 1.00 80.42 O ANISOU 4543 O SER B 161 8172 10879 11505 834 -1290 601 O ATOM 4544 CB SER B 161 99.556 -94.804 13.238 1.00 84.45 C ANISOU 4544 CB SER B 161 8376 10945 12768 681 -1550 500 C ATOM 4545 OG SER B 161 99.311 -94.042 12.068 1.00 93.42 O ANISOU 4545 OG SER B 161 9579 12220 13698 689 -1766 357 O ATOM 4546 N TYR B 162 101.363 -91.865 13.947 1.00 74.10 N ANISOU 4546 N TYR B 162 7310 10203 10643 763 -1276 774 N ATOM 4547 CA TYR B 162 102.444 -90.948 13.591 1.00 71.78 C ANISOU 4547 CA TYR B 162 7154 10130 9991 799 -1233 773 C ATOM 4548 C TYR B 162 103.074 -90.340 14.861 1.00 71.83 C ANISOU 4548 C TYR B 162 7146 10237 9910 805 -1018 928 C ATOM 4549 O TYR B 162 104.293 -90.145 14.907 1.00 70.73 O ANISOU 4549 O TYR B 162 7084 10245 9544 842 -934 919 O ATOM 4550 CB TYR B 162 101.887 -89.842 12.659 1.00 73.31 C ANISOU 4550 CB TYR B 162 7388 10398 10070 784 -1372 747 C ATOM 4551 CG TYR B 162 102.746 -88.600 12.549 1.00 73.91 C ANISOU 4551 CG TYR B 162 7566 10658 9860 797 -1277 816 C ATOM 4552 CD1 TYR B 162 102.471 -87.467 13.312 1.00 74.84 C ANISOU 4552 CD1 TYR B 162 7640 10796 9999 760 -1173 947 C ATOM 4553 CD2 TYR B 162 103.835 -88.556 11.684 1.00 74.90 C ANISOU 4553 CD2 TYR B 162 7820 10923 9715 847 -1279 746 C ATOM 4554 CE1 TYR B 162 103.286 -86.339 13.247 1.00 75.36 C ANISOU 4554 CE1 TYR B 162 7784 10992 9856 755 -1076 997 C ATOM 4555 CE2 TYR B 162 104.639 -87.425 11.591 1.00 75.01 C ANISOU 4555 CE2 TYR B 162 7904 11080 9515 843 -1170 822 C ATOM 4556 CZ TYR B 162 104.367 -86.321 12.379 1.00 82.67 C ANISOU 4556 CZ TYR B 162 8823 12043 10543 789 -1072 943 C ATOM 4557 OH TYR B 162 105.174 -85.216 12.286 1.00 85.07 O ANISOU 4557 OH TYR B 162 9183 12453 10687 772 -962 1003 O ATOM 4558 N ILE B 163 102.233 -90.031 15.877 1.00 66.55 N ANISOU 4558 N ILE B 163 6367 9500 9418 777 -935 1055 N ATOM 4559 CA ILE B 163 102.649 -89.406 17.137 1.00 64.76 C ANISOU 4559 CA ILE B 163 6120 9380 9107 796 -751 1177 C ATOM 4560 C ILE B 163 103.507 -90.379 17.971 1.00 68.33 C ANISOU 4560 C ILE B 163 6566 9862 9533 868 -621 1226 C ATOM 4561 O ILE B 163 104.620 -90.009 18.349 1.00 67.95 O ANISOU 4561 O ILE B 163 6568 9986 9263 907 -541 1223 O ATOM 4562 CB ILE B 163 101.439 -88.835 17.934 1.00 67.75 C ANISOU 4562 CB ILE B 163 6387 9686 9671 771 -694 1290 C ATOM 4563 CG1 ILE B 163 100.850 -87.613 17.203 1.00 68.30 C ANISOU 4563 CG1 ILE B 163 6476 9770 9707 726 -799 1258 C ATOM 4564 CG2 ILE B 163 101.829 -88.444 19.372 1.00 67.37 C ANISOU 4564 CG2 ILE B 163 6313 9750 9535 821 -498 1396 C ATOM 4565 CD1 ILE B 163 99.363 -87.586 17.146 1.00 81.26 C ANISOU 4565 CD1 ILE B 163 7991 11265 11618 697 -870 1299 C ATOM 4566 N VAL B 164 103.013 -91.601 18.239 1.00 64.82 N ANISOU 4566 N VAL B 164 6053 9248 9329 890 -602 1273 N ATOM 4567 CA VAL B 164 103.741 -92.596 19.024 1.00 65.04 C ANISOU 4567 CA VAL B 164 6074 9280 9359 981 -472 1354 C ATOM 4568 C VAL B 164 105.196 -92.780 18.460 1.00 68.48 C ANISOU 4568 C VAL B 164 6617 9859 9544 1034 -498 1242 C ATOM 4569 O VAL B 164 106.106 -92.550 19.261 1.00 68.08 O ANISOU 4569 O VAL B 164 6575 9983 9310 1103 -387 1303 O ATOM 4570 CB VAL B 164 102.975 -93.944 19.214 1.00 70.87 C ANISOU 4570 CB VAL B 164 6721 9759 10447 989 -444 1425 C ATOM 4571 CG1 VAL B 164 103.918 -95.081 19.614 1.00 70.94 C ANISOU 4571 CG1 VAL B 164 6758 9749 10446 1098 -344 1479 C ATOM 4572 CG2 VAL B 164 101.862 -93.804 20.251 1.00 71.57 C ANISOU 4572 CG2 VAL B 164 6682 9765 10745 978 -318 1611 C ATOM 4573 N PRO B 165 105.485 -93.071 17.146 1.00 64.22 N ANISOU 4573 N PRO B 165 6153 9286 8960 1015 -637 1075 N ATOM 4574 CA PRO B 165 106.900 -93.179 16.716 1.00 63.27 C ANISOU 4574 CA PRO B 165 6119 9325 8596 1080 -622 991 C ATOM 4575 C PRO B 165 107.694 -91.872 16.867 1.00 65.39 C ANISOU 4575 C PRO B 165 6417 9831 8596 1060 -573 997 C ATOM 4576 O PRO B 165 108.889 -91.953 17.148 1.00 65.01 O ANISOU 4576 O PRO B 165 6379 9936 8387 1123 -497 992 O ATOM 4577 CB PRO B 165 106.815 -93.612 15.252 1.00 65.53 C ANISOU 4577 CB PRO B 165 6481 9535 8884 1068 -780 809 C ATOM 4578 CG PRO B 165 105.467 -93.270 14.826 1.00 70.30 C ANISOU 4578 CG PRO B 165 7048 10013 9649 982 -906 783 C ATOM 4579 CD PRO B 165 104.581 -93.379 16.024 1.00 66.12 C ANISOU 4579 CD PRO B 165 6396 9363 9362 954 -813 947 C ATOM 4580 N LEU B 166 107.045 -90.694 16.739 1.00 60.73 N ANISOU 4580 N LEU B 166 5825 9262 7987 975 -608 1009 N ATOM 4581 CA LEU B 166 107.710 -89.402 16.927 1.00 59.52 C ANISOU 4581 CA LEU B 166 5686 9286 7642 940 -551 1012 C ATOM 4582 C LEU B 166 108.147 -89.192 18.399 1.00 63.39 C ANISOU 4582 C LEU B 166 6105 9890 8091 980 -421 1090 C ATOM 4583 O LEU B 166 109.228 -88.640 18.640 1.00 62.57 O ANISOU 4583 O LEU B 166 5995 9959 7819 986 -369 1052 O ATOM 4584 CB LEU B 166 106.772 -88.270 16.509 1.00 59.21 C ANISOU 4584 CB LEU B 166 5657 9196 7643 856 -612 1023 C ATOM 4585 CG LEU B 166 107.231 -87.193 15.562 1.00 64.39 C ANISOU 4585 CG LEU B 166 6387 9940 8140 811 -638 982 C ATOM 4586 CD1 LEU B 166 106.209 -86.117 15.579 1.00 64.34 C ANISOU 4586 CD1 LEU B 166 6365 9862 8219 753 -666 1036 C ATOM 4587 CD2 LEU B 166 108.499 -86.496 16.066 1.00 66.73 C ANISOU 4587 CD2 LEU B 166 6669 10400 8285 798 -518 973 C ATOM 4588 N VAL B 167 107.303 -89.622 19.368 1.00 59.42 N ANISOU 4588 N VAL B 167 5537 9301 7740 1015 -370 1197 N ATOM 4589 CA VAL B 167 107.568 -89.480 20.803 1.00 59.31 C ANISOU 4589 CA VAL B 167 5462 9412 7660 1087 -249 1280 C ATOM 4590 C VAL B 167 108.796 -90.331 21.199 1.00 63.49 C ANISOU 4590 C VAL B 167 5986 10071 8067 1202 -199 1288 C ATOM 4591 O VAL B 167 109.583 -89.924 22.060 1.00 63.27 O ANISOU 4591 O VAL B 167 5922 10245 7873 1259 -143 1283 O ATOM 4592 CB VAL B 167 106.315 -89.821 21.648 1.00 64.10 C ANISOU 4592 CB VAL B 167 6004 9893 8457 1117 -182 1421 C ATOM 4593 CG1 VAL B 167 106.620 -89.771 23.144 1.00 64.28 C ANISOU 4593 CG1 VAL B 167 5979 10080 8363 1232 -48 1516 C ATOM 4594 CG2 VAL B 167 105.161 -88.879 21.317 1.00 63.67 C ANISOU 4594 CG2 VAL B 167 5935 9738 8519 1018 -230 1408 C ATOM 4595 N TRP B 168 108.968 -91.485 20.547 1.00 60.77 N ANISOU 4595 N TRP B 168 5671 9613 7807 1242 -231 1283 N ATOM 4596 CA TRP B 168 110.111 -92.357 20.784 1.00 61.71 C ANISOU 4596 CA TRP B 168 5785 9829 7835 1366 -187 1294 C ATOM 4597 C TRP B 168 111.356 -91.797 20.092 1.00 67.34 C ANISOU 4597 C TRP B 168 6522 10717 8347 1341 -223 1155 C ATOM 4598 O TRP B 168 112.455 -91.910 20.642 1.00 68.01 O ANISOU 4598 O TRP B 168 6561 10988 8292 1430 -177 1154 O ATOM 4599 CB TRP B 168 109.816 -93.792 20.332 1.00 61.34 C ANISOU 4599 CB TRP B 168 5757 9562 7986 1422 -197 1326 C ATOM 4600 CG TRP B 168 108.869 -94.498 21.260 1.00 62.89 C ANISOU 4600 CG TRP B 168 5898 9603 8394 1475 -108 1507 C ATOM 4601 CD1 TRP B 168 107.535 -94.699 21.069 1.00 66.07 C ANISOU 4601 CD1 TRP B 168 6273 9773 9058 1393 -129 1548 C ATOM 4602 CD2 TRP B 168 109.173 -95.016 22.570 1.00 63.44 C ANISOU 4602 CD2 TRP B 168 5919 9760 8427 1629 30 1692 C ATOM 4603 NE1 TRP B 168 106.992 -95.340 22.161 1.00 66.56 N ANISOU 4603 NE1 TRP B 168 6268 9749 9273 1476 9 1757 N ATOM 4604 CE2 TRP B 168 107.974 -95.543 23.099 1.00 68.16 C ANISOU 4604 CE2 TRP B 168 6468 10151 9279 1632 112 1859 C ATOM 4605 CE3 TRP B 168 110.347 -95.101 23.340 1.00 64.76 C ANISOU 4605 CE3 TRP B 168 6068 10169 8367 1777 89 1738 C ATOM 4606 CZ2 TRP B 168 107.913 -96.145 24.362 1.00 68.55 C ANISOU 4606 CZ2 TRP B 168 6470 10229 9346 1787 276 2096 C ATOM 4607 CZ3 TRP B 168 110.290 -95.719 24.580 1.00 67.40 C ANISOU 4607 CZ3 TRP B 168 6360 10546 8703 1943 222 1956 C ATOM 4608 CH2 TRP B 168 109.082 -96.220 25.085 1.00 68.97 C ANISOU 4608 CH2 TRP B 168 6529 10538 9139 1952 325 2145 C ATOM 4609 N CYS B 169 111.182 -91.154 18.917 1.00 63.71 N ANISOU 4609 N CYS B 169 6121 10212 7873 1228 -300 1051 N ATOM 4610 CA CYS B 169 112.277 -90.533 18.177 1.00 63.24 C ANISOU 4610 CA CYS B 169 6081 10304 7644 1194 -305 947 C ATOM 4611 C CYS B 169 112.837 -89.342 18.965 1.00 66.21 C ANISOU 4611 C CYS B 169 6384 10863 7911 1147 -255 934 C ATOM 4612 O CYS B 169 114.059 -89.210 19.050 1.00 66.19 O ANISOU 4612 O CYS B 169 6327 11034 7789 1174 -220 879 O ATOM 4613 CB CYS B 169 111.831 -90.119 16.779 1.00 63.70 C ANISOU 4613 CB CYS B 169 6228 10273 7703 1109 -382 877 C ATOM 4614 SG CYS B 169 113.071 -89.161 15.869 1.00 67.92 S ANISOU 4614 SG CYS B 169 6781 10986 8040 1060 -342 801 S ATOM 4615 N MET B 170 111.948 -88.502 19.560 1.00 62.36 N ANISOU 4615 N MET B 170 5881 10331 7481 1080 -253 968 N ATOM 4616 CA MET B 170 112.314 -87.343 20.385 1.00 62.27 C ANISOU 4616 CA MET B 170 5802 10461 7396 1034 -216 922 C ATOM 4617 C MET B 170 113.033 -87.780 21.664 1.00 69.10 C ANISOU 4617 C MET B 170 6580 11513 8161 1158 -176 932 C ATOM 4618 O MET B 170 113.919 -87.063 22.134 1.00 70.15 O ANISOU 4618 O MET B 170 6636 11824 8192 1140 -168 835 O ATOM 4619 CB MET B 170 111.079 -86.510 20.741 1.00 64.03 C ANISOU 4619 CB MET B 170 6037 10572 7719 967 -219 955 C ATOM 4620 CG MET B 170 110.629 -85.581 19.627 1.00 67.44 C ANISOU 4620 CG MET B 170 6530 10886 8208 843 -257 929 C ATOM 4621 SD MET B 170 109.184 -84.563 20.076 1.00 71.51 S ANISOU 4621 SD MET B 170 7044 11268 8858 785 -256 969 S ATOM 4622 CE MET B 170 107.846 -85.763 19.879 1.00 68.11 C ANISOU 4622 CE MET B 170 6633 10662 8584 841 -306 1081 C ATOM 4623 N ALA B 171 112.665 -88.960 22.213 1.00 66.18 N ANISOU 4623 N ALA B 171 6216 11102 7829 1289 -151 1050 N ATOM 4624 CA ALA B 171 113.288 -89.541 23.402 1.00 67.54 C ANISOU 4624 CA ALA B 171 6319 11456 7888 1452 -108 1105 C ATOM 4625 C ALA B 171 114.703 -90.076 23.074 1.00 75.12 C ANISOU 4625 C ALA B 171 7235 12561 8747 1523 -121 1048 C ATOM 4626 O ALA B 171 115.600 -89.987 23.917 1.00 75.87 O ANISOU 4626 O ALA B 171 7238 12890 8699 1617 -121 1015 O ATOM 4627 CB ALA B 171 112.414 -90.651 23.955 1.00 68.66 C ANISOU 4627 CB ALA B 171 6484 11467 8135 1570 -51 1288 C ATOM 4628 N CYS B 172 114.897 -90.606 21.844 1.00 73.09 N ANISOU 4628 N CYS B 172 7035 12178 8558 1490 -139 1024 N ATOM 4629 CA CYS B 172 116.180 -91.114 21.351 1.00 74.43 C ANISOU 4629 CA CYS B 172 7167 12463 8651 1558 -135 966 C ATOM 4630 C CYS B 172 117.167 -89.962 21.143 1.00 77.48 C ANISOU 4630 C CYS B 172 7468 13033 8936 1456 -143 828 C ATOM 4631 O CYS B 172 118.351 -90.114 21.457 1.00 78.31 O ANISOU 4631 O CYS B 172 7466 13339 8950 1534 -136 782 O ATOM 4632 CB CYS B 172 115.995 -91.920 20.070 1.00 75.66 C ANISOU 4632 CB CYS B 172 7419 12429 8898 1555 -147 955 C ATOM 4633 SG CYS B 172 115.326 -93.579 20.335 1.00 81.01 S ANISOU 4633 SG CYS B 172 8147 12894 9737 1705 -125 1088 S ATOM 4634 N LEU B 173 116.681 -88.825 20.615 1.00 71.84 N ANISOU 4634 N LEU B 173 6791 12241 8264 1285 -153 772 N ATOM 4635 CA LEU B 173 117.454 -87.611 20.360 1.00 71.02 C ANISOU 4635 CA LEU B 173 6608 12248 8128 1157 -140 658 C ATOM 4636 C LEU B 173 117.869 -86.910 21.662 1.00 74.13 C ANISOU 4636 C LEU B 173 6872 12826 8468 1159 -159 577 C ATOM 4637 O LEU B 173 119.008 -86.452 21.767 1.00 73.56 O ANISOU 4637 O LEU B 173 6667 12924 8359 1128 -157 467 O ATOM 4638 CB LEU B 173 116.628 -86.648 19.485 1.00 70.09 C ANISOU 4638 CB LEU B 173 6583 11954 8092 998 -136 659 C ATOM 4639 CG LEU B 173 116.933 -86.624 17.988 1.00 74.66 C ANISOU 4639 CG LEU B 173 7232 12473 8662 949 -106 661 C ATOM 4640 CD1 LEU B 173 116.556 -87.921 17.310 1.00 74.64 C ANISOU 4640 CD1 LEU B 173 7335 12373 8652 1058 -137 707 C ATOM 4641 CD2 LEU B 173 116.162 -85.523 17.321 1.00 77.35 C ANISOU 4641 CD2 LEU B 173 7648 12675 9065 814 -102 683 C ATOM 4642 N SER B 174 116.959 -86.856 22.656 1.00 70.73 N ANISOU 4642 N SER B 174 6468 12373 8033 1205 -176 621 N ATOM 4643 CA SER B 174 117.187 -86.216 23.955 1.00 71.47 C ANISOU 4643 CA SER B 174 6460 12652 8044 1236 -205 526 C ATOM 4644 C SER B 174 118.160 -87.011 24.838 1.00 76.14 C ANISOU 4644 C SER B 174 6944 13501 8485 1424 -234 523 C ATOM 4645 O SER B 174 118.688 -86.454 25.808 1.00 77.93 O ANISOU 4645 O SER B 174 7055 13944 8610 1457 -284 396 O ATOM 4646 CB SER B 174 115.866 -86.022 24.695 1.00 75.18 C ANISOU 4646 CB SER B 174 7003 13027 8533 1262 -192 594 C ATOM 4647 OG SER B 174 114.929 -85.249 23.965 1.00 83.42 O ANISOU 4647 OG SER B 174 8131 13847 9718 1108 -177 600 O ATOM 4648 N SER B 175 118.388 -88.307 24.516 1.00 71.06 N ANISOU 4648 N SER B 175 6335 12835 7831 1560 -210 654 N ATOM 4649 CA SER B 175 119.295 -89.179 25.274 1.00 71.72 C ANISOU 4649 CA SER B 175 6323 13146 7782 1770 -230 690 C ATOM 4650 C SER B 175 120.646 -89.383 24.561 1.00 73.14 C ANISOU 4650 C SER B 175 6396 13435 7958 1768 -238 608 C ATOM 4651 O SER B 175 121.428 -90.224 25.001 1.00 74.86 O ANISOU 4651 O SER B 175 6535 13820 8089 1956 -252 654 O ATOM 4652 CB SER B 175 118.640 -90.530 25.560 1.00 76.59 C ANISOU 4652 CB SER B 175 7036 13651 8412 1952 -177 912 C ATOM 4653 OG SER B 175 118.300 -91.217 24.368 1.00 88.18 O ANISOU 4653 OG SER B 175 8608 14866 10031 1904 -138 976 O ATOM 4654 N LEU B 176 120.935 -88.591 23.497 1.00 65.62 N ANISOU 4654 N LEU B 176 5433 12401 7100 1572 -217 503 N ATOM 4655 CA LEU B 176 122.194 -88.656 22.756 1.00 64.82 C ANISOU 4655 CA LEU B 176 5217 12401 7010 1554 -194 429 C ATOM 4656 C LEU B 176 123.371 -88.069 23.574 1.00 71.17 C ANISOU 4656 C LEU B 176 5789 13499 7753 1564 -259 272 C ATOM 4657 O LEU B 176 124.422 -88.710 23.577 1.00 70.59 O ANISOU 4657 O LEU B 176 5591 13594 7634 1689 -264 265 O ATOM 4658 CB LEU B 176 122.083 -87.975 21.394 1.00 63.58 C ANISOU 4658 CB LEU B 176 5125 12073 6960 1359 -126 399 C ATOM 4659 CG LEU B 176 121.455 -88.833 20.311 1.00 66.38 C ANISOU 4659 CG LEU B 176 5659 12216 7345 1398 -80 511 C ATOM 4660 CD1 LEU B 176 121.036 -87.987 19.140 1.00 66.04 C ANISOU 4660 CD1 LEU B 176 5708 12016 7368 1220 -33 498 C ATOM 4661 CD2 LEU B 176 122.393 -89.962 19.867 1.00 67.85 C ANISOU 4661 CD2 LEU B 176 5807 12482 7492 1556 -43 532 C ATOM 4662 N PRO B 177 123.235 -86.940 24.342 1.00 70.41 N ANISOU 4662 N PRO B 177 5618 13481 7656 1457 -320 130 N ATOM 4663 CA PRO B 177 124.369 -86.475 25.176 1.00 72.75 C ANISOU 4663 CA PRO B 177 5672 14072 7897 1481 -414 -56 C ATOM 4664 C PRO B 177 124.699 -87.461 26.308 1.00 79.83 C ANISOU 4664 C PRO B 177 6512 15223 8596 1764 -497 0 C ATOM 4665 O PRO B 177 125.817 -87.461 26.816 1.00 82.41 O ANISOU 4665 O PRO B 177 6628 15826 8860 1844 -583 -121 O ATOM 4666 CB PRO B 177 123.878 -85.134 25.733 1.00 74.46 C ANISOU 4666 CB PRO B 177 5869 14258 8165 1318 -462 -224 C ATOM 4667 CG PRO B 177 122.730 -84.750 24.861 1.00 76.79 C ANISOU 4667 CG PRO B 177 6367 14228 8583 1168 -366 -118 C ATOM 4668 CD PRO B 177 122.077 -86.041 24.519 1.00 71.04 C ANISOU 4668 CD PRO B 177 5810 13390 7790 1323 -318 109 C ATOM 4669 N THR B 178 123.728 -88.321 26.682 1.00 75.78 N ANISOU 4669 N THR B 178 6178 14617 7999 1922 -466 200 N ATOM 4670 CA THR B 178 123.929 -89.374 27.675 1.00 77.33 C ANISOU 4670 CA THR B 178 6353 15014 8015 2217 -505 327 C ATOM 4671 C THR B 178 124.853 -90.447 27.067 1.00 82.08 C ANISOU 4671 C THR B 178 6895 15649 8642 2349 -470 418 C ATOM 4672 O THR B 178 125.791 -90.880 27.736 1.00 83.63 O ANISOU 4672 O THR B 178 6937 16125 8715 2544 -543 404 O ATOM 4673 CB THR B 178 122.591 -89.973 28.135 1.00 89.08 C ANISOU 4673 CB THR B 178 8043 16341 9463 2326 -440 543 C ATOM 4674 OG1 THR B 178 121.584 -88.957 28.216 1.00 92.39 O ANISOU 4674 OG1 THR B 178 8547 16623 9934 2149 -430 469 O ATOM 4675 CG2 THR B 178 122.712 -90.724 29.456 1.00 87.47 C ANISOU 4675 CG2 THR B 178 7808 16388 9038 2631 -475 670 C ATOM 4676 N PHE B 179 124.608 -90.850 25.794 1.00 77.12 N ANISOU 4676 N PHE B 179 6383 14751 8167 2256 -366 497 N ATOM 4677 CA PHE B 179 125.444 -91.842 25.118 1.00 78.06 C ANISOU 4677 CA PHE B 179 6461 14876 8321 2381 -316 560 C ATOM 4678 C PHE B 179 126.810 -91.250 24.754 1.00 85.03 C ANISOU 4678 C PHE B 179 7111 15965 9232 2302 -343 380 C ATOM 4679 O PHE B 179 127.802 -91.977 24.725 1.00 86.91 O ANISOU 4679 O PHE B 179 7223 16356 9444 2470 -343 400 O ATOM 4680 CB PHE B 179 124.765 -92.421 23.860 1.00 78.40 C ANISOU 4680 CB PHE B 179 6701 14587 8501 2316 -208 658 C ATOM 4681 CG PHE B 179 125.142 -93.865 23.602 1.00 81.39 C ANISOU 4681 CG PHE B 179 7111 14917 8898 2542 -156 788 C ATOM 4682 CD1 PHE B 179 124.266 -94.897 23.912 1.00 84.87 C ANISOU 4682 CD1 PHE B 179 7703 15168 9376 2685 -119 975 C ATOM 4683 CD2 PHE B 179 126.394 -94.196 23.088 1.00 85.59 C ANISOU 4683 CD2 PHE B 179 7503 15583 9433 2620 -132 727 C ATOM 4684 CE1 PHE B 179 124.628 -96.233 23.715 1.00 87.37 C ANISOU 4684 CE1 PHE B 179 8044 15408 9744 2900 -64 1091 C ATOM 4685 CE2 PHE B 179 126.756 -95.532 22.887 1.00 89.92 C ANISOU 4685 CE2 PHE B 179 8080 16077 10010 2849 -79 839 C ATOM 4686 CZ PHE B 179 125.869 -96.542 23.200 1.00 88.06 C ANISOU 4686 CZ PHE B 179 8007 15629 9823 2987 -48 1017 C ATOM 4687 N TYR B 180 126.871 -89.942 24.481 1.00 81.41 N ANISOU 4687 N TYR B 180 6582 15500 8851 2051 -355 211 N ATOM 4688 CA TYR B 180 128.124 -89.307 24.100 1.00 82.78 C ANISOU 4688 CA TYR B 180 6515 15835 9104 1943 -357 46 C ATOM 4689 C TYR B 180 129.090 -89.129 25.289 1.00 88.53 C ANISOU 4689 C TYR B 180 6979 16921 9738 2058 -506 -96 C ATOM 4690 O TYR B 180 130.295 -89.314 25.105 1.00 88.91 O ANISOU 4690 O TYR B 180 6806 17155 9823 2110 -514 -162 O ATOM 4691 CB TYR B 180 127.873 -87.937 23.427 1.00 83.65 C ANISOU 4691 CB TYR B 180 6627 15789 9367 1633 -303 -71 C ATOM 4692 CG TYR B 180 127.101 -87.942 22.115 1.00 84.27 C ANISOU 4692 CG TYR B 180 6928 15561 9528 1514 -166 46 C ATOM 4693 CD1 TYR B 180 127.075 -89.068 21.295 1.00 85.84 C ANISOU 4693 CD1 TYR B 180 7252 15664 9700 1648 -85 181 C ATOM 4694 CD2 TYR B 180 126.441 -86.798 21.667 1.00 84.01 C ANISOU 4694 CD2 TYR B 180 6974 15344 9601 1280 -124 6 C ATOM 4695 CE1 TYR B 180 126.372 -89.070 20.090 1.00 85.32 C ANISOU 4695 CE1 TYR B 180 7386 15349 9681 1556 13 257 C ATOM 4696 CE2 TYR B 180 125.754 -86.785 20.451 1.00 83.10 C ANISOU 4696 CE2 TYR B 180 7056 14983 9534 1195 -16 116 C ATOM 4697 CZ TYR B 180 125.715 -87.927 19.671 1.00 90.00 C ANISOU 4697 CZ TYR B 180 8053 15791 10351 1336 42 232 C ATOM 4698 OH TYR B 180 125.042 -87.933 18.475 1.00 91.03 O ANISOU 4698 OH TYR B 180 8376 15711 10500 1272 123 311 O ATOM 4699 N PHE B 181 128.575 -88.789 26.493 1.00 85.83 N ANISOU 4699 N PHE B 181 6650 16695 9265 2112 -627 -150 N ATOM 4700 CA PHE B 181 129.418 -88.458 27.640 1.00 88.43 C ANISOU 4700 CA PHE B 181 6732 17387 9482 2210 -800 -333 C ATOM 4701 C PHE B 181 129.573 -89.532 28.729 1.00 94.12 C ANISOU 4701 C PHE B 181 7442 18363 9955 2568 -893 -204 C ATOM 4702 O PHE B 181 130.662 -89.599 29.310 1.00 96.31 O ANISOU 4702 O PHE B 181 7469 18970 10154 2700 -1023 -323 O ATOM 4703 CB PHE B 181 128.914 -87.166 28.292 1.00 90.65 C ANISOU 4703 CB PHE B 181 6997 17678 9768 2034 -889 -545 C ATOM 4704 CG PHE B 181 129.203 -85.963 27.434 1.00 92.46 C ANISOU 4704 CG PHE B 181 7125 17745 10261 1701 -829 -720 C ATOM 4705 CD1 PHE B 181 130.439 -85.328 27.494 1.00 98.70 C ANISOU 4705 CD1 PHE B 181 7597 18728 11176 1597 -907 -955 C ATOM 4706 CD2 PHE B 181 128.262 -85.494 26.524 1.00 92.40 C ANISOU 4706 CD2 PHE B 181 7327 17388 10395 1498 -687 -632 C ATOM 4707 CE1 PHE B 181 130.726 -84.246 26.660 1.00100.16 C ANISOU 4707 CE1 PHE B 181 7682 18733 11643 1289 -816 -1079 C ATOM 4708 CE2 PHE B 181 128.547 -84.410 25.694 1.00 95.69 C ANISOU 4708 CE2 PHE B 181 7657 17644 11055 1213 -607 -747 C ATOM 4709 CZ PHE B 181 129.781 -83.800 25.760 1.00 96.77 C ANISOU 4709 CZ PHE B 181 7483 17952 11333 1107 -657 -958 C ATOM 4710 N ARG B 182 128.524 -90.325 29.049 1.00 89.82 N ANISOU 4710 N ARG B 182 7144 17684 9298 2729 -830 36 N ATOM 4711 CA ARG B 182 128.614 -91.335 30.120 1.00 91.49 C ANISOU 4711 CA ARG B 182 7360 18125 9277 3086 -890 206 C ATOM 4712 C ARG B 182 129.741 -92.343 29.879 1.00 98.32 C ANISOU 4712 C ARG B 182 8081 19131 10144 3299 -890 296 C ATOM 4713 O ARG B 182 129.822 -92.926 28.803 1.00 97.65 O ANISOU 4713 O ARG B 182 8066 18813 10225 3257 -758 398 O ATOM 4714 CB ARG B 182 127.285 -92.095 30.305 1.00 89.40 C ANISOU 4714 CB ARG B 182 7380 17619 8968 3198 -768 491 C ATOM 4715 CG ARG B 182 126.226 -91.346 31.105 1.00 95.71 C ANISOU 4715 CG ARG B 182 8292 18415 9659 3139 -793 450 C ATOM 4716 CD ARG B 182 126.337 -91.569 32.599 1.00102.64 C ANISOU 4716 CD ARG B 182 9117 19654 10227 3440 -898 492 C ATOM 4717 NE ARG B 182 125.621 -90.539 33.349 1.00110.38 N ANISOU 4717 NE ARG B 182 10141 20706 11092 3356 -953 336 N ATOM 4718 CZ ARG B 182 125.721 -90.365 34.663 1.00135.21 C ANISOU 4718 CZ ARG B 182 13228 24209 13936 3577 -1071 274 C ATOM 4719 NH1 ARG B 182 126.509 -91.146 35.385 1.00127.64 N ANISOU 4719 NH1 ARG B 182 12162 23582 12753 3901 -1156 373 N ATOM 4720 NH2 ARG B 182 125.034 -89.403 35.264 1.00127.79 N ANISOU 4720 NH2 ARG B 182 12339 23310 12905 3494 -1107 107 N ATOM 4721 N ASP B 183 130.628 -92.512 30.875 1.00 97.32 N ANISOU 4721 N ASP B 183 7746 19403 9827 3537 -1047 238 N ATOM 4722 CA ASP B 183 131.743 -93.468 30.858 1.00 98.70 C ANISOU 4722 CA ASP B 183 7755 19771 9977 3793 -1072 328 C ATOM 4723 C ASP B 183 132.286 -93.733 32.272 1.00105.10 C ANISOU 4723 C ASP B 183 8412 21029 10492 4127 -1259 334 C ATOM 4724 O ASP B 183 132.105 -92.912 33.179 1.00105.94 O ANISOU 4724 O ASP B 183 8466 21360 10428 4104 -1407 157 O ATOM 4725 CB ASP B 183 132.893 -93.017 29.931 1.00101.00 C ANISOU 4725 CB ASP B 183 7796 20103 10477 3610 -1075 119 C ATOM 4726 CG ASP B 183 133.676 -94.195 29.368 1.00111.06 C ANISOU 4726 CG ASP B 183 9007 21371 11817 3824 -989 283 C ATOM 4727 OD1 ASP B 183 133.064 -95.271 29.161 1.00110.67 O ANISOU 4727 OD1 ASP B 183 9189 21094 11767 3989 -860 551 O ATOM 4728 OD2 ASP B 183 134.902 -94.047 29.145 1.00117.08 O ANISOU 4728 OD2 ASP B 183 9480 22351 12656 3830 -1047 138 O ATOM 4729 N VAL B 184 132.940 -94.901 32.444 1.00102.51 N ANISOU 4729 N VAL B 184 8020 20831 10097 4456 -1252 539 N ATOM 4730 CA VAL B 184 133.562 -95.333 33.693 1.00105.26 C ANISOU 4730 CA VAL B 184 8218 21622 10153 4833 -1423 596 C ATOM 4731 C VAL B 184 134.866 -94.537 33.855 1.00111.58 C ANISOU 4731 C VAL B 184 8639 22801 10957 4765 -1644 244 C ATOM 4732 O VAL B 184 135.743 -94.605 32.994 1.00111.51 O ANISOU 4732 O VAL B 184 8447 22753 11169 4670 -1609 161 O ATOM 4733 CB VAL B 184 133.767 -96.878 33.720 1.00109.92 C ANISOU 4733 CB VAL B 184 8882 22165 10718 5206 -1313 967 C ATOM 4734 CG1 VAL B 184 134.815 -97.300 34.746 1.00113.93 C ANISOU 4734 CG1 VAL B 184 9148 23170 10970 5598 -1506 995 C ATOM 4735 CG2 VAL B 184 132.450 -97.595 33.988 1.00108.41 C ANISOU 4735 CG2 VAL B 184 9028 21684 10480 5319 -1138 1307 C ATOM 4736 N ARG B 185 134.963 -93.748 34.942 1.00110.11 N ANISOU 4736 N ARG B 185 8327 22971 10538 4804 -1867 19 N ATOM 4737 CA ARG B 185 136.123 -92.908 35.231 1.00112.65 C ANISOU 4737 CA ARG B 185 8267 23661 10873 4727 -2111 -362 C ATOM 4738 C ARG B 185 136.585 -93.067 36.677 1.00121.97 C ANISOU 4738 C ARG B 185 9297 25381 11667 5103 -2376 -413 C ATOM 4739 O ARG B 185 135.825 -93.516 37.538 1.00121.75 O ANISOU 4739 O ARG B 185 9490 25436 11334 5367 -2364 -193 O ATOM 4740 CB ARG B 185 135.810 -91.428 34.932 1.00110.23 C ANISOU 4740 CB ARG B 185 7922 23214 10747 4288 -2145 -719 C ATOM 4741 CG ARG B 185 136.629 -90.803 33.801 1.00116.87 C ANISOU 4741 CG ARG B 185 8524 23910 11971 3948 -2095 -935 C ATOM 4742 CD ARG B 185 136.258 -91.356 32.434 1.00117.82 C ANISOU 4742 CD ARG B 185 8848 23581 12335 3814 -1800 -683 C ATOM 4743 NE ARG B 185 136.758 -90.539 31.331 1.00119.30 N ANISOU 4743 NE ARG B 185 8875 23586 12869 3447 -1709 -877 N ATOM 4744 CZ ARG B 185 137.021 -91.000 30.113 1.00130.00 C ANISOU 4744 CZ ARG B 185 10257 24701 14436 3372 -1499 -735 C ATOM 4745 NH1 ARG B 185 137.463 -90.178 29.168 1.00116.61 N ANISOU 4745 NH1 ARG B 185 8412 22863 13032 3048 -1403 -897 N ATOM 4746 NH2 ARG B 185 136.872 -92.288 29.838 1.00114.06 N ANISOU 4746 NH2 ARG B 185 8409 22584 12344 3632 -1377 -432 N ATOM 4747 N THR B 186 137.854 -92.689 36.931 1.00123.11 N ANISOU 4747 N THR B 186 9047 25905 11825 5133 -2614 -705 N ATOM 4748 CA THR B 186 138.501 -92.777 38.236 1.00127.81 C ANISOU 4748 CA THR B 186 9429 27073 12058 5492 -2917 -816 C ATOM 4749 C THR B 186 138.548 -91.379 38.878 1.00133.76 C ANISOU 4749 C THR B 186 10016 28056 12749 5277 -3168 -1306 C ATOM 4750 O THR B 186 139.271 -90.502 38.407 1.00134.26 O ANISOU 4750 O THR B 186 9784 28118 13110 4962 -3264 -1669 O ATOM 4751 CB THR B 186 139.902 -93.419 38.102 1.00140.16 C ANISOU 4751 CB THR B 186 10644 28921 13689 5711 -3029 -805 C ATOM 4752 OG1 THR B 186 140.784 -92.509 37.439 1.00142.67 O ANISOU 4752 OG1 THR B 186 10615 29238 14356 5355 -3110 -1188 O ATOM 4753 CG2 THR B 186 139.886 -94.735 37.329 1.00136.80 C ANISOU 4753 CG2 THR B 186 10379 28208 13392 5886 -2761 -365 C ATOM 4754 N ILE B 187 137.741 -91.179 39.939 1.00131.01 N ANISOU 4754 N ILE B 187 9864 27883 12031 5448 -3253 -1310 N ATOM 4755 CA ILE B 187 137.683 -89.926 40.689 1.00132.73 C ANISOU 4755 CA ILE B 187 9963 28335 12133 5304 -3498 -1779 C ATOM 4756 C ILE B 187 138.821 -89.922 41.704 1.00142.26 C ANISOU 4756 C ILE B 187 10810 30179 13063 5612 -3875 -2038 C ATOM 4757 O ILE B 187 138.698 -90.569 42.742 1.00144.80 O ANISOU 4757 O ILE B 187 11223 30876 12920 6065 -3981 -1852 O ATOM 4758 CB ILE B 187 136.300 -89.751 41.361 1.00134.42 C ANISOU 4758 CB ILE B 187 10552 28467 12056 5379 -3404 -1664 C ATOM 4759 N GLU B 188 139.939 -89.224 41.395 1.00140.32 N ANISOU 4759 N GLU B 188 10145 30062 13107 5379 -4073 -2450 N ATOM 4760 CA GLU B 188 141.138 -89.155 42.243 1.00145.35 C ANISOU 4760 CA GLU B 188 10368 31302 13556 5627 -4462 -2755 C ATOM 4761 C GLU B 188 140.844 -88.625 43.655 1.00152.90 C ANISOU 4761 C GLU B 188 11344 32716 14035 5854 -4764 -3047 C ATOM 4762 O GLU B 188 141.517 -89.036 44.608 1.00156.79 O ANISOU 4762 O GLU B 188 11646 33776 14151 6270 -5054 -3100 O ATOM 4763 CB GLU B 188 142.221 -88.302 41.574 1.00147.92 C ANISOU 4763 CB GLU B 188 10241 31592 14369 5236 -4583 -3186 C ATOM 4764 N TYR B 189 139.834 -87.727 43.786 1.00147.88 N ANISOU 4764 N TYR B 189 10944 31845 13399 5605 -4695 -3233 N ATOM 4765 CA TYR B 189 139.389 -87.120 45.046 1.00150.53 C ANISOU 4765 CA TYR B 189 11349 32548 13296 5784 -4935 -3533 C ATOM 4766 C TYR B 189 138.918 -88.176 46.056 1.00155.41 C ANISOU 4766 C TYR B 189 12229 33527 13293 6370 -4927 -3116 C ATOM 4767 O TYR B 189 139.240 -88.063 47.239 1.00160.08 O ANISOU 4767 O TYR B 189 12704 34696 13422 6713 -5246 -3343 O ATOM 4768 CB TYR B 189 138.253 -86.115 44.770 1.00148.39 C ANISOU 4768 CB TYR B 189 11340 31834 13207 5400 -4758 -3696 C ATOM 4769 N LEU B 190 138.184 -89.216 45.583 1.00147.54 N ANISOU 4769 N LEU B 190 11572 32195 12292 6492 -4564 -2505 N ATOM 4770 CA LEU B 190 137.651 -90.295 46.421 1.00148.40 C ANISOU 4770 CA LEU B 190 11952 32545 11887 7025 -4475 -2019 C ATOM 4771 C LEU B 190 138.338 -91.666 46.191 1.00153.27 C ANISOU 4771 C LEU B 190 12499 33249 12488 7365 -4406 -1557 C ATOM 4772 O LEU B 190 138.119 -92.596 46.968 1.00155.60 O ANISOU 4772 O LEU B 190 12955 33812 12353 7857 -4371 -1157 O ATOM 4773 CB LEU B 190 136.141 -90.431 46.199 1.00144.05 C ANISOU 4773 CB LEU B 190 11859 31532 11343 6929 -4102 -1670 C ATOM 4774 N GLY B 191 139.155 -91.765 45.145 1.00147.58 N ANISOU 4774 N GLY B 191 11539 32302 12233 7113 -4372 -1608 N ATOM 4775 CA GLY B 191 139.860 -92.990 44.756 1.00147.57 C ANISOU 4775 CA GLY B 191 11448 32317 12306 7380 -4288 -1216 C ATOM 4776 C GLY B 191 138.920 -94.130 44.401 1.00147.43 C ANISOU 4776 C GLY B 191 11836 31894 12288 7538 -3895 -586 C ATOM 4777 O GLY B 191 139.106 -95.250 44.882 1.00148.95 O ANISOU 4777 O GLY B 191 12084 32291 12221 8008 -3864 -177 O ATOM 4778 N VAL B 192 137.912 -93.863 43.544 1.00138.95 N ANISOU 4778 N VAL B 192 11037 30232 11527 7149 -3593 -502 N ATOM 4779 CA VAL B 192 136.888 -94.853 43.169 1.00135.28 C ANISOU 4779 CA VAL B 192 10957 29329 11114 7239 -3219 48 C ATOM 4780 C VAL B 192 136.609 -94.880 41.626 1.00133.42 C ANISOU 4780 C VAL B 192 10813 28447 11433 6795 -2938 108 C ATOM 4781 O VAL B 192 136.941 -93.913 40.949 1.00131.21 O ANISOU 4781 O VAL B 192 10360 28040 11452 6382 -3004 -279 O ATOM 4782 CB VAL B 192 135.608 -94.545 43.999 1.00138.48 C ANISOU 4782 CB VAL B 192 11678 29744 11195 7315 -3137 137 C ATOM 4783 CG1 VAL B 192 134.898 -93.270 43.541 1.00134.71 C ANISOU 4783 CG1 VAL B 192 11276 28960 10950 6810 -3099 -231 C ATOM 4784 CG2 VAL B 192 134.670 -95.725 44.038 1.00137.07 C ANISOU 4784 CG2 VAL B 192 11845 29282 10952 7564 -2806 746 C ATOM 4785 N ASN B 193 136.036 -95.998 41.092 1.00128.15 N ANISOU 4785 N ASN B 193 10405 27388 10898 6898 -2631 588 N ATOM 4786 CA ASN B 193 135.639 -96.153 39.678 1.00124.06 C ANISOU 4786 CA ASN B 193 10021 26269 10846 6535 -2358 677 C ATOM 4787 C ASN B 193 134.139 -95.909 39.534 1.00125.95 C ANISOU 4787 C ASN B 193 10614 26108 11131 6328 -2137 805 C ATOM 4788 O ASN B 193 133.334 -96.781 39.870 1.00125.86 O ANISOU 4788 O ASN B 193 10860 25953 11007 6563 -1949 1215 O ATOM 4789 CB ASN B 193 136.012 -97.517 39.102 1.00125.15 C ANISOU 4789 CB ASN B 193 10193 26213 11148 6760 -2182 1059 C ATOM 4790 CG ASN B 193 137.438 -97.631 38.633 1.00158.84 C ANISOU 4790 CG ASN B 193 14107 30672 15574 6788 -2317 888 C ATOM 4791 OD1 ASN B 193 138.337 -96.938 39.110 1.00161.96 O ANISOU 4791 OD1 ASN B 193 14183 31502 15854 6798 -2599 549 O ATOM 4792 ND2 ASN B 193 137.688 -98.578 37.749 1.00150.09 N ANISOU 4792 ND2 ASN B 193 13037 29263 14728 6837 -2121 1127 N ATOM 4793 N ALA B 194 133.770 -94.718 39.043 1.00120.57 N ANISOU 4793 N ALA B 194 9932 25243 10636 5893 -2153 463 N ATOM 4794 CA ALA B 194 132.372 -94.362 38.921 1.00117.66 C ANISOU 4794 CA ALA B 194 9866 24524 10316 5689 -1969 544 C ATOM 4795 C ALA B 194 131.943 -94.114 37.481 1.00118.40 C ANISOU 4795 C ALA B 194 10060 24076 10849 5263 -1773 511 C ATOM 4796 O ALA B 194 132.725 -93.644 36.655 1.00116.65 O ANISOU 4796 O ALA B 194 9641 23801 10878 5016 -1826 266 O ATOM 4797 CB ALA B 194 132.086 -93.138 39.770 1.00119.51 C ANISOU 4797 CB ALA B 194 10060 25023 10325 5600 -2151 194 C ATOM 4798 N CYS B 195 130.665 -94.447 37.209 1.00114.15 N ANISOU 4798 N CYS B 195 9829 23148 10394 5194 -1541 773 N ATOM 4799 CA CYS B 195 129.948 -94.247 35.947 1.00110.79 C ANISOU 4799 CA CYS B 195 9562 22204 10330 4826 -1349 782 C ATOM 4800 C CYS B 195 129.442 -92.800 35.976 1.00112.03 C ANISOU 4800 C CYS B 195 9721 22327 10518 4498 -1419 448 C ATOM 4801 O CYS B 195 128.510 -92.492 36.716 1.00111.66 O ANISOU 4801 O CYS B 195 9826 22306 10296 4546 -1397 486 O ATOM 4802 CB CYS B 195 128.816 -95.270 35.815 1.00110.35 C ANISOU 4802 CB CYS B 195 9798 21795 10336 4936 -1105 1197 C ATOM 4803 SG CYS B 195 127.771 -95.076 34.341 1.00110.14 S ANISOU 4803 SG CYS B 195 9980 21153 10714 4519 -895 1209 S ATOM 4804 N ILE B 196 130.153 -91.891 35.279 1.00107.00 N ANISOU 4804 N ILE B 196 8890 21675 10091 4198 -1510 113 N ATOM 4805 CA ILE B 196 129.865 -90.448 35.283 1.00105.77 C ANISOU 4805 CA ILE B 196 8693 21486 10010 3882 -1588 -236 C ATOM 4806 C ILE B 196 129.891 -89.831 33.875 1.00107.29 C ANISOU 4806 C ILE B 196 8873 21304 10588 3479 -1478 -355 C ATOM 4807 O ILE B 196 130.387 -90.454 32.936 1.00106.17 O ANISOU 4807 O ILE B 196 8698 21016 10624 3455 -1381 -234 O ATOM 4808 CB ILE B 196 130.864 -89.684 36.211 1.00112.13 C ANISOU 4808 CB ILE B 196 9201 22765 10638 3949 -1872 -607 C ATOM 4809 CG1 ILE B 196 132.346 -89.992 35.882 1.00114.02 C ANISOU 4809 CG1 ILE B 196 9128 23221 10973 4002 -1987 -705 C ATOM 4810 CG2 ILE B 196 130.561 -89.916 37.687 1.00115.94 C ANISOU 4810 CG2 ILE B 196 9739 23626 10686 4309 -1991 -554 C ATOM 4811 CD1 ILE B 196 133.051 -88.903 35.178 1.00117.71 C ANISOU 4811 CD1 ILE B 196 9355 23620 11749 3637 -2050 -1061 C ATOM 4812 N MET B 197 129.412 -88.568 33.760 1.00102.61 N ANISOU 4812 N MET B 197 8296 20579 10111 3182 -1496 -605 N ATOM 4813 CA MET B 197 129.420 -87.782 32.520 1.00100.25 C ANISOU 4813 CA MET B 197 7980 19952 10159 2802 -1397 -729 C ATOM 4814 C MET B 197 130.843 -87.229 32.304 1.00106.01 C ANISOU 4814 C MET B 197 8361 20884 11033 2683 -1524 -1013 C ATOM 4815 O MET B 197 131.206 -86.193 32.872 1.00107.60 O ANISOU 4815 O MET B 197 8378 21256 11247 2568 -1685 -1346 O ATOM 4816 CB MET B 197 128.365 -86.655 32.567 1.00101.16 C ANISOU 4816 CB MET B 197 8237 19850 10350 2563 -1363 -865 C ATOM 4817 CG MET B 197 126.929 -87.153 32.571 1.00102.41 C ANISOU 4817 CG MET B 197 8714 19757 10440 2632 -1208 -578 C ATOM 4818 SD MET B 197 126.387 -87.811 30.978 1.00103.17 S ANISOU 4818 SD MET B 197 9004 19394 10801 2483 -979 -296 S ATOM 4819 CE MET B 197 125.763 -86.338 30.210 1.00 98.08 C ANISOU 4819 CE MET B 197 8412 18439 10413 2090 -922 -485 C ATOM 4820 N ALA B 198 131.651 -87.955 31.509 1.00102.11 N ANISOU 4820 N ALA B 198 7766 20372 10659 2724 -1451 -889 N ATOM 4821 CA ALA B 198 133.057 -87.660 31.249 1.00104.09 C ANISOU 4821 CA ALA B 198 7667 20823 11061 2652 -1541 -1099 C ATOM 4822 C ALA B 198 133.248 -86.473 30.290 1.00107.85 C ANISOU 4822 C ALA B 198 8040 21056 11884 2246 -1455 -1297 C ATOM 4823 O ALA B 198 133.699 -86.653 29.155 1.00106.72 O ANISOU 4823 O ALA B 198 7852 20748 11950 2130 -1298 -1206 O ATOM 4824 CB ALA B 198 133.744 -88.903 30.707 1.00104.98 C ANISOU 4824 CB ALA B 198 7735 20976 11178 2860 -1456 -866 C ATOM 4825 N PHE B 199 132.935 -85.251 30.769 1.00105.65 N ANISOU 4825 N PHE B 199 7717 20761 11665 2046 -1550 -1569 N ATOM 4826 CA PHE B 199 133.052 -84.020 29.986 1.00105.46 C ANISOU 4826 CA PHE B 199 7596 20486 11988 1663 -1465 -1753 C ATOM 4827 C PHE B 199 134.522 -83.641 29.766 1.00112.52 C ANISOU 4827 C PHE B 199 8079 21561 13111 1549 -1533 -1974 C ATOM 4828 O PHE B 199 135.344 -83.948 30.629 1.00115.08 O ANISOU 4828 O PHE B 199 8161 22267 13296 1744 -1742 -2122 O ATOM 4829 CB PHE B 199 132.313 -82.863 30.684 1.00107.59 C ANISOU 4829 CB PHE B 199 7927 20688 12266 1513 -1558 -1997 C ATOM 4830 N PRO B 200 134.876 -82.948 28.651 1.00108.76 N ANISOU 4830 N PRO B 200 7503 20831 12991 1243 -1360 -1998 N ATOM 4831 CA PRO B 200 136.284 -82.550 28.455 1.00111.39 C ANISOU 4831 CA PRO B 200 7410 21328 13585 1119 -1404 -2205 C ATOM 4832 C PRO B 200 136.749 -81.484 29.461 1.00117.55 C ANISOU 4832 C PRO B 200 7894 22297 14474 992 -1652 -2637 C ATOM 4833 O PRO B 200 135.932 -80.676 29.891 1.00116.32 O ANISOU 4833 O PRO B 200 7880 21996 14319 870 -1699 -2781 O ATOM 4834 CB PRO B 200 136.294 -81.984 27.027 1.00112.02 C ANISOU 4834 CB PRO B 200 7518 21041 14004 819 -1117 -2083 C ATOM 4835 CG PRO B 200 134.902 -81.543 26.771 1.00113.80 C ANISOU 4835 CG PRO B 200 8115 20927 14196 708 -1010 -1968 C ATOM 4836 CD PRO B 200 134.030 -82.507 27.516 1.00107.63 C ANISOU 4836 CD PRO B 200 7614 20256 13025 1013 -1111 -1822 C ATOM 4837 N PRO B 201 138.078 -81.357 29.732 1.00117.27 N ANISOU 4837 N PRO B 201 7423 22546 14589 980 -1797 -2873 N ATOM 4838 CA PRO B 201 138.554 -80.306 30.658 1.00123.12 C ANISOU 4838 CA PRO B 201 7853 23457 15469 839 -2054 -3336 C ATOM 4839 C PRO B 201 138.218 -78.881 30.212 1.00151.15 C ANISOU 4839 C PRO B 201 11387 26622 19420 430 -1939 -3518 C ATOM 4840 O PRO B 201 137.666 -78.103 30.987 1.00111.12 O ANISOU 4840 O PRO B 201 6374 21524 14323 360 -2087 -3785 O ATOM 4841 CB PRO B 201 140.073 -80.505 30.658 1.00128.13 C ANISOU 4841 CB PRO B 201 8008 24395 16280 862 -2161 -3488 C ATOM 4842 CG PRO B 201 140.366 -81.244 29.386 1.00129.61 C ANISOU 4842 CG PRO B 201 8251 24424 16571 874 -1861 -3114 C ATOM 4843 CD PRO B 201 139.209 -82.179 29.258 1.00120.56 C ANISOU 4843 CD PRO B 201 7592 23157 15058 1109 -1749 -2754 C ATOM 4844 N TYR B 204 134.978 -78.231 31.752 1.00138.79 N ANISOU 4844 N TYR B 204 10683 24786 17263 585 -2048 -3553 N ATOM 4845 CA TYR B 204 134.187 -79.193 32.517 1.00136.88 C ANISOU 4845 CA TYR B 204 10729 24752 16529 946 -2124 -3367 C ATOM 4846 C TYR B 204 133.042 -78.496 33.262 1.00139.81 C ANISOU 4846 C TYR B 204 11329 25022 16769 937 -2180 -3518 C ATOM 4847 O TYR B 204 131.935 -79.038 33.300 1.00136.53 O ANISOU 4847 O TYR B 204 11261 24506 16107 1093 -2071 -3234 O ATOM 4848 CB TYR B 204 135.072 -79.978 33.513 1.00141.05 C ANISOU 4848 CB TYR B 204 11032 25810 16751 1270 -2390 -3481 C ATOM 4849 CG TYR B 204 134.402 -81.204 34.101 1.00141.17 C ANISOU 4849 CG TYR B 204 11333 26022 16285 1671 -2404 -3172 C ATOM 4850 CD1 TYR B 204 133.629 -81.116 35.255 1.00143.67 C ANISOU 4850 CD1 TYR B 204 11819 26515 16256 1869 -2543 -3271 C ATOM 4851 CD2 TYR B 204 134.559 -82.457 33.515 1.00140.32 C ANISOU 4851 CD2 TYR B 204 11316 25919 16078 1860 -2264 -2781 C ATOM 4852 CE1 TYR B 204 132.995 -82.238 35.790 1.00143.34 C ANISOU 4852 CE1 TYR B 204 12032 26632 15797 2235 -2519 -2950 C ATOM 4853 CE2 TYR B 204 133.930 -83.586 34.039 1.00140.14 C ANISOU 4853 CE2 TYR B 204 11550 26031 15667 2216 -2253 -2479 C ATOM 4854 CZ TYR B 204 133.151 -83.473 35.181 1.00148.77 C ANISOU 4854 CZ TYR B 204 12805 27288 16434 2400 -2374 -2549 C ATOM 4855 OH TYR B 204 132.529 -84.585 35.701 1.00149.55 O ANISOU 4855 OH TYR B 204 13145 27503 16172 2751 -2332 -2219 O ATOM 4856 N ALA B 205 133.317 -77.326 33.882 1.00138.96 N ANISOU 4856 N ALA B 205 11015 24949 16835 766 -2352 -3975 N ATOM 4857 CA ALA B 205 132.330 -76.548 34.638 1.00138.62 C ANISOU 4857 CA ALA B 205 11154 24823 16693 756 -2417 -4188 C ATOM 4858 C ALA B 205 131.229 -76.013 33.717 1.00138.29 C ANISOU 4858 C ALA B 205 11400 24259 16884 531 -2135 -3964 C ATOM 4859 O ALA B 205 130.054 -76.056 34.084 1.00135.89 O ANISOU 4859 O ALA B 205 11398 23874 16360 650 -2086 -3856 O ATOM 4860 CB ALA B 205 133.012 -75.402 35.368 1.00143.88 C ANISOU 4860 CB ALA B 205 11497 25608 17562 596 -2661 -4762 C ATOM 4861 N GLN B 206 131.617 -75.541 32.515 1.00134.00 N ANISOU 4861 N GLN B 206 10758 23380 16777 226 -1944 -3873 N ATOM 4862 CA GLN B 206 130.732 -75.011 31.474 1.00130.89 C ANISOU 4862 CA GLN B 206 10601 22496 16635 6 -1671 -3638 C ATOM 4863 C GLN B 206 129.752 -76.100 30.988 1.00128.08 C ANISOU 4863 C GLN B 206 10609 22067 15991 208 -1507 -3164 C ATOM 4864 O GLN B 206 128.551 -75.838 30.862 1.00125.55 O ANISOU 4864 O GLN B 206 10570 21495 15640 191 -1398 -3033 O ATOM 4865 CB GLN B 206 131.582 -74.450 30.303 1.00133.55 C ANISOU 4865 CB GLN B 206 10714 22577 17452 -309 -1502 -3605 C ATOM 4866 CG GLN B 206 130.814 -74.088 29.023 1.00152.28 C ANISOU 4866 CG GLN B 206 13327 24482 20051 -496 -1196 -3275 C ATOM 4867 CD GLN B 206 131.401 -72.913 28.276 1.00179.98 C ANISOU 4867 CD GLN B 206 16617 27676 24092 -852 -1054 -3386 C ATOM 4868 OE1 GLN B 206 130.801 -71.836 28.216 1.00176.67 O ANISOU 4868 OE1 GLN B 206 16272 26930 23923 -1039 -984 -3488 O ATOM 4869 NE2 GLN B 206 132.571 -73.083 27.659 1.00176.42 N ANISOU 4869 NE2 GLN B 206 15888 27293 23850 -951 -983 -3346 N ATOM 4870 N TRP B 207 130.271 -77.321 30.760 1.00121.50 N ANISOU 4870 N TRP B 207 9751 21452 14959 403 -1502 -2928 N ATOM 4871 CA TRP B 207 129.506 -78.477 30.302 1.00116.63 C ANISOU 4871 CA TRP B 207 9435 20779 14100 600 -1364 -2506 C ATOM 4872 C TRP B 207 128.497 -78.963 31.338 1.00117.10 C ANISOU 4872 C TRP B 207 9726 20982 13784 867 -1448 -2451 C ATOM 4873 O TRP B 207 127.376 -79.292 30.964 1.00113.63 O ANISOU 4873 O TRP B 207 9578 20322 13277 906 -1303 -2178 O ATOM 4874 CB TRP B 207 130.442 -79.623 29.913 1.00115.28 C ANISOU 4874 CB TRP B 207 9143 20819 13840 754 -1353 -2325 C ATOM 4875 CG TRP B 207 130.730 -79.671 28.445 1.00114.66 C ANISOU 4875 CG TRP B 207 9069 20475 14023 574 -1125 -2108 C ATOM 4876 CD1 TRP B 207 131.896 -79.333 27.828 1.00119.45 C ANISOU 4876 CD1 TRP B 207 9386 21094 14907 405 -1076 -2198 C ATOM 4877 CD2 TRP B 207 129.820 -80.051 27.407 1.00111.16 C ANISOU 4877 CD2 TRP B 207 8928 19727 13580 552 -911 -1772 C ATOM 4878 NE1 TRP B 207 131.779 -79.504 26.469 1.00116.86 N ANISOU 4878 NE1 TRP B 207 9179 20502 14720 300 -829 -1920 N ATOM 4879 CE2 TRP B 207 130.513 -79.941 26.183 1.00115.02 C ANISOU 4879 CE2 TRP B 207 9312 20077 14313 390 -739 -1669 C ATOM 4880 CE3 TRP B 207 128.486 -80.500 27.394 1.00109.58 C ANISOU 4880 CE3 TRP B 207 9067 19370 13199 664 -851 -1550 C ATOM 4881 CZ2 TRP B 207 129.917 -80.245 24.959 1.00111.82 C ANISOU 4881 CZ2 TRP B 207 9144 19404 13938 351 -528 -1372 C ATOM 4882 CZ3 TRP B 207 127.894 -80.798 26.177 1.00108.53 C ANISOU 4882 CZ3 TRP B 207 9148 18955 13133 604 -656 -1269 C ATOM 4883 CH2 TRP B 207 128.603 -80.661 24.978 1.00109.31 C ANISOU 4883 CH2 TRP B 207 9153 18941 13440 456 -505 -1191 C ATOM 4884 N SER B 208 128.884 -79.008 32.626 1.00115.00 N ANISOU 4884 N SER B 208 9325 21096 13274 1058 -1678 -2704 N ATOM 4885 CA SER B 208 128.009 -79.440 33.719 1.00114.06 C ANISOU 4885 CA SER B 208 9404 21166 12768 1342 -1750 -2655 C ATOM 4886 C SER B 208 126.835 -78.473 33.898 1.00116.21 C ANISOU 4886 C SER B 208 9865 21175 13115 1215 -1684 -2754 C ATOM 4887 O SER B 208 125.722 -78.931 34.147 1.00113.39 O ANISOU 4887 O SER B 208 9771 20760 12553 1373 -1593 -2523 O ATOM 4888 CB SER B 208 128.791 -79.574 35.019 1.00120.59 C ANISOU 4888 CB SER B 208 10021 22487 13311 1576 -2021 -2937 C ATOM 4889 OG SER B 208 129.803 -80.557 34.890 1.00129.22 O ANISOU 4889 OG SER B 208 10950 23831 14316 1736 -2077 -2807 O ATOM 4890 N ALA B 209 127.076 -77.151 33.721 1.00113.95 N ANISOU 4890 N ALA B 209 9437 20702 13157 927 -1711 -3080 N ATOM 4891 CA ALA B 209 126.054 -76.102 33.815 1.00113.04 C ANISOU 4891 CA ALA B 209 9474 20299 13179 785 -1643 -3203 C ATOM 4892 C ALA B 209 125.120 -76.140 32.595 1.00112.78 C ANISOU 4892 C ALA B 209 9682 19830 13341 642 -1384 -2835 C ATOM 4893 O ALA B 209 123.904 -76.036 32.768 1.00111.35 O ANISOU 4893 O ALA B 209 9736 19498 13074 701 -1300 -2720 O ATOM 4894 CB ALA B 209 126.706 -74.733 33.945 1.00116.92 C ANISOU 4894 CB ALA B 209 9718 20698 14009 519 -1745 -3657 C ATOM 4895 N GLY B 210 125.695 -76.321 31.397 1.00107.17 N ANISOU 4895 N GLY B 210 8903 18949 12868 477 -1264 -2654 N ATOM 4896 CA GLY B 210 124.968 -76.419 30.133 1.00103.38 C ANISOU 4896 CA GLY B 210 8630 18101 12551 358 -1038 -2311 C ATOM 4897 C GLY B 210 124.055 -77.628 30.050 1.00103.89 C ANISOU 4897 C GLY B 210 8953 18185 12337 587 -965 -1951 C ATOM 4898 O GLY B 210 122.917 -77.506 29.590 1.00101.82 O ANISOU 4898 O GLY B 210 8913 17652 12123 549 -839 -1763 O ATOM 4899 N ILE B 211 124.541 -78.799 30.522 1.00100.10 N ANISOU 4899 N ILE B 211 8432 18020 11582 831 -1046 -1856 N ATOM 4900 CA ILE B 211 123.789 -80.060 30.543 1.00 97.67 C ANISOU 4900 CA ILE B 211 8339 17739 11032 1065 -979 -1519 C ATOM 4901 C ILE B 211 122.705 -80.002 31.641 1.00103.31 C ANISOU 4901 C ILE B 211 9205 18524 11523 1233 -1009 -1534 C ATOM 4902 O ILE B 211 121.590 -80.484 31.399 1.00100.72 O ANISOU 4902 O ILE B 211 9096 18018 11155 1295 -888 -1268 O ATOM 4903 CB ILE B 211 124.728 -81.306 30.670 1.00100.81 C ANISOU 4903 CB ILE B 211 8633 18425 11247 1277 -1037 -1401 C ATOM 4904 CG1 ILE B 211 125.563 -81.530 29.363 1.00100.21 C ANISOU 4904 CG1 ILE B 211 8461 18221 11390 1129 -944 -1303 C ATOM 4905 CG2 ILE B 211 123.971 -82.603 31.090 1.00 99.63 C ANISOU 4905 CG2 ILE B 211 8680 18346 10827 1565 -993 -1094 C ATOM 4906 CD1 ILE B 211 124.774 -81.755 27.986 1.00100.96 C ANISOU 4906 CD1 ILE B 211 8777 17943 11638 1009 -745 -1019 C ATOM 4907 N ALA B 212 123.006 -79.389 32.819 1.00103.65 N ANISOU 4907 N ALA B 212 9127 18823 11432 1304 -1166 -1856 N ATOM 4908 CA ALA B 212 122.029 -79.244 33.917 1.00104.20 C ANISOU 4908 CA ALA B 212 9333 18994 11266 1482 -1184 -1900 C ATOM 4909 C ALA B 212 120.823 -78.417 33.461 1.00105.72 C ANISOU 4909 C ALA B 212 9693 18806 11669 1308 -1046 -1866 C ATOM 4910 O ALA B 212 119.687 -78.762 33.793 1.00104.31 O ANISOU 4910 O ALA B 212 9702 18577 11356 1446 -954 -1675 O ATOM 4911 CB ALA B 212 122.673 -78.603 35.136 1.00108.69 C ANISOU 4911 CB ALA B 212 9725 19903 11668 1569 -1393 -2312 C ATOM 4912 N LEU B 213 121.085 -77.358 32.661 1.00101.36 N ANISOU 4912 N LEU B 213 9064 17982 11466 1011 -1018 -2024 N ATOM 4913 CA LEU B 213 120.099 -76.462 32.062 1.00 99.31 C ANISOU 4913 CA LEU B 213 8936 17335 11461 825 -889 -1992 C ATOM 4914 C LEU B 213 119.236 -77.201 31.032 1.00 97.48 C ANISOU 4914 C LEU B 213 8902 16857 11280 822 -726 -1579 C ATOM 4915 O LEU B 213 118.040 -76.946 30.983 1.00 95.79 O ANISOU 4915 O LEU B 213 8848 16443 11105 825 -635 -1470 O ATOM 4916 CB LEU B 213 120.814 -75.266 31.413 1.00100.90 C ANISOU 4916 CB LEU B 213 8979 17324 12034 524 -892 -2226 C ATOM 4917 CG LEU B 213 120.725 -73.918 32.150 1.00108.83 C ANISOU 4917 CG LEU B 213 9905 18270 13174 426 -965 -2626 C ATOM 4918 CD1 LEU B 213 121.441 -73.948 33.499 1.00112.14 C ANISOU 4918 CD1 LEU B 213 10162 19104 13341 588 -1180 -2979 C ATOM 4919 CD2 LEU B 213 121.312 -72.801 31.307 1.00113.16 C ANISOU 4919 CD2 LEU B 213 10316 18516 14165 107 -913 -2769 C ATOM 4920 N MET B 214 119.820 -78.138 30.248 1.00 91.53 N ANISOU 4920 N MET B 214 8129 16129 10520 831 -697 -1366 N ATOM 4921 CA MET B 214 119.085 -78.935 29.253 1.00 88.11 C ANISOU 4921 CA MET B 214 7870 15484 10124 840 -569 -1012 C ATOM 4922 C MET B 214 118.159 -79.963 29.922 1.00 89.89 C ANISOU 4922 C MET B 214 8239 15803 10113 1085 -543 -800 C ATOM 4923 O MET B 214 117.134 -80.314 29.340 1.00 87.73 O ANISOU 4923 O MET B 214 8121 15305 9907 1078 -443 -566 O ATOM 4924 CB MET B 214 120.042 -79.644 28.285 1.00 89.84 C ANISOU 4924 CB MET B 214 8021 15723 10393 801 -548 -888 C ATOM 4925 N LYS B 215 118.517 -80.440 31.133 1.00 87.21 N ANISOU 4925 N LYS B 215 7837 15795 9504 1306 -631 -874 N ATOM 4926 CA LYS B 215 117.724 -81.388 31.924 1.00 86.69 C ANISOU 4926 CA LYS B 215 7889 15846 9204 1563 -586 -661 C ATOM 4927 C LYS B 215 116.398 -80.752 32.390 1.00 90.66 C ANISOU 4927 C LYS B 215 8511 16214 9721 1569 -511 -666 C ATOM 4928 O LYS B 215 115.369 -81.428 32.386 1.00 89.19 O ANISOU 4928 O LYS B 215 8455 15920 9513 1667 -400 -400 O ATOM 4929 CB LYS B 215 118.533 -81.879 33.141 1.00 91.35 C ANISOU 4929 CB LYS B 215 8370 16857 9480 1812 -702 -757 C ATOM 4930 N ASN B 216 116.433 -79.451 32.779 1.00 88.41 N ANISOU 4930 N ASN B 216 8169 15923 9500 1462 -565 -977 N ATOM 4931 CA ASN B 216 115.287 -78.676 33.273 1.00 88.18 C ANISOU 4931 CA ASN B 216 8232 15777 9494 1471 -500 -1043 C ATOM 4932 C ASN B 216 114.340 -78.232 32.154 1.00 90.56 C ANISOU 4932 C ASN B 216 8638 15669 10100 1276 -385 -894 C ATOM 4933 O ASN B 216 113.127 -78.321 32.332 1.00 90.63 O ANISOU 4933 O ASN B 216 8760 15565 10112 1349 -284 -741 O ATOM 4934 CB ASN B 216 115.745 -77.430 34.044 1.00 89.16 C ANISOU 4934 CB ASN B 216 8250 16020 9605 1425 -610 -1466 C ATOM 4935 CG ASN B 216 116.555 -77.678 35.288 1.00108.06 C ANISOU 4935 CG ASN B 216 10537 18852 11668 1641 -754 -1675 C ATOM 4936 OD1 ASN B 216 117.508 -76.950 35.568 1.00101.30 O ANISOU 4936 OD1 ASN B 216 9524 18122 10844 1557 -900 -2028 O ATOM 4937 ND2 ASN B 216 116.171 -78.655 36.100 1.00 99.16 N ANISOU 4937 ND2 ASN B 216 9485 17970 10222 1929 -716 -1471 N ATOM 4938 N ILE B 217 114.880 -77.718 31.033 1.00 85.03 N ANISOU 4938 N ILE B 217 7893 14763 9652 1042 -395 -938 N ATOM 4939 CA ILE B 217 114.086 -77.223 29.911 1.00 82.66 C ANISOU 4939 CA ILE B 217 7686 14099 9621 870 -302 -801 C ATOM 4940 C ILE B 217 113.307 -78.374 29.247 1.00 82.43 C ANISOU 4940 C ILE B 217 7777 13964 9580 939 -228 -449 C ATOM 4941 O ILE B 217 112.082 -78.303 29.170 1.00 80.63 O ANISOU 4941 O ILE B 217 7646 13567 9423 961 -154 -316 O ATOM 4942 CB ILE B 217 114.982 -76.448 28.896 1.00 86.31 C ANISOU 4942 CB ILE B 217 8063 14403 10326 629 -314 -908 C ATOM 4943 CG1 ILE B 217 115.757 -75.258 29.554 1.00 89.42 C ANISOU 4943 CG1 ILE B 217 8310 14861 10804 532 -390 -1287 C ATOM 4944 CG2 ILE B 217 114.205 -75.991 27.655 1.00 85.80 C ANISOU 4944 CG2 ILE B 217 8106 13987 10506 482 -217 -726 C ATOM 4945 CD1 ILE B 217 114.939 -74.204 30.408 1.00 97.50 C ANISOU 4945 CD1 ILE B 217 9368 15805 11872 552 -382 -1500 C ATOM 4946 N LEU B 218 114.007 -79.426 28.796 1.00 77.94 N ANISOU 4946 N LEU B 218 7188 13490 8937 978 -250 -317 N ATOM 4947 CA LEU B 218 113.404 -80.566 28.100 1.00 75.87 C ANISOU 4947 CA LEU B 218 7024 13112 8690 1031 -196 -25 C ATOM 4948 C LEU B 218 112.611 -81.507 28.997 1.00 79.11 C ANISOU 4948 C LEU B 218 7488 13618 8953 1243 -149 142 C ATOM 4949 O LEU B 218 111.670 -82.141 28.518 1.00 77.64 O ANISOU 4949 O LEU B 218 7384 13255 8861 1257 -87 360 O ATOM 4950 CB LEU B 218 114.484 -81.386 27.386 1.00 75.55 C ANISOU 4950 CB LEU B 218 6940 13144 8622 1022 -229 32 C ATOM 4951 CG LEU B 218 114.800 -80.991 25.947 1.00 79.37 C ANISOU 4951 CG LEU B 218 7439 13431 9286 832 -212 51 C ATOM 4952 CD1 LEU B 218 116.117 -81.606 25.503 1.00 79.96 C ANISOU 4952 CD1 LEU B 218 7429 13647 9305 840 -239 37 C ATOM 4953 CD2 LEU B 218 113.673 -81.401 24.991 1.00 79.47 C ANISOU 4953 CD2 LEU B 218 7591 13197 9408 808 -165 264 C ATOM 4954 N GLY B 219 113.021 -81.632 30.257 1.00 76.41 N ANISOU 4954 N GLY B 219 7088 13559 8385 1412 -177 48 N ATOM 4955 CA GLY B 219 112.399 -82.551 31.202 1.00 76.44 C ANISOU 4955 CA GLY B 219 7134 13691 8218 1644 -107 235 C ATOM 4956 C GLY B 219 111.394 -81.973 32.175 1.00 81.03 C ANISOU 4956 C GLY B 219 7750 14305 8732 1737 -36 201 C ATOM 4957 O GLY B 219 110.695 -82.747 32.832 1.00 80.94 O ANISOU 4957 O GLY B 219 7782 14354 8620 1920 65 412 O ATOM 4958 N PHE B 220 111.307 -80.628 32.301 1.00 78.61 N ANISOU 4958 N PHE B 220 7423 13953 8491 1625 -69 -57 N ATOM 4959 CA PHE B 220 110.361 -80.035 33.250 1.00 80.11 C ANISOU 4959 CA PHE B 220 7648 14182 8610 1733 5 -117 C ATOM 4960 C PHE B 220 109.660 -78.775 32.725 1.00 82.17 C ANISOU 4960 C PHE B 220 7933 14164 9124 1552 29 -246 C ATOM 4961 O PHE B 220 108.432 -78.739 32.761 1.00 80.82 O ANISOU 4961 O PHE B 220 7819 13844 9045 1588 139 -101 O ATOM 4962 CB PHE B 220 111.041 -79.729 34.595 1.00 85.29 C ANISOU 4962 CB PHE B 220 8245 15206 8957 1911 -64 -362 C ATOM 4963 CG PHE B 220 110.091 -79.430 35.735 1.00 89.36 C ANISOU 4963 CG PHE B 220 8809 15838 9308 2103 37 -381 C ATOM 4964 CD1 PHE B 220 109.436 -80.458 36.405 1.00 93.38 C ANISOU 4964 CD1 PHE B 220 9368 16473 9640 2339 172 -84 C ATOM 4965 CD2 PHE B 220 109.877 -78.122 36.160 1.00 93.31 C ANISOU 4965 CD2 PHE B 220 9298 16320 9834 2058 13 -696 C ATOM 4966 CE1 PHE B 220 108.567 -80.181 37.465 1.00 96.31 C ANISOU 4966 CE1 PHE B 220 9779 16971 9843 2533 293 -86 C ATOM 4967 CE2 PHE B 220 109.006 -77.847 37.219 1.00 97.83 C ANISOU 4967 CE2 PHE B 220 9918 17016 10236 2257 119 -726 C ATOM 4968 CZ PHE B 220 108.358 -78.879 37.863 1.00 96.48 C ANISOU 4968 CZ PHE B 220 9797 16994 9869 2498 263 -414 C ATOM 4969 N ILE B 221 110.414 -77.754 32.263 1.00 78.57 N ANISOU 4969 N ILE B 221 7423 13631 8798 1367 -62 -502 N ATOM 4970 CA ILE B 221 109.863 -76.478 31.795 1.00 78.37 C ANISOU 4970 CA ILE B 221 7418 13331 9028 1205 -35 -628 C ATOM 4971 C ILE B 221 108.872 -76.697 30.642 1.00 79.64 C ANISOU 4971 C ILE B 221 7656 13183 9420 1111 40 -349 C ATOM 4972 O ILE B 221 107.683 -76.444 30.838 1.00 79.57 O ANISOU 4972 O ILE B 221 7693 13053 9486 1164 126 -268 O ATOM 4973 CB ILE B 221 110.977 -75.451 31.425 1.00 82.64 C ANISOU 4973 CB ILE B 221 7871 13821 9707 1012 -129 -916 C ATOM 4974 CG1 ILE B 221 111.939 -75.164 32.614 1.00 86.04 C ANISOU 4974 CG1 ILE B 221 8197 14569 9924 1103 -237 -1249 C ATOM 4975 CG2 ILE B 221 110.414 -74.146 30.824 1.00 83.39 C ANISOU 4975 CG2 ILE B 221 7993 13581 10109 842 -79 -1000 C ATOM 4976 CD1 ILE B 221 111.282 -74.794 34.011 1.00 98.10 C ANISOU 4976 CD1 ILE B 221 9752 16274 11247 1308 -214 -1422 C ATOM 4977 N ILE B 222 109.348 -77.164 29.465 1.00 73.92 N ANISOU 4977 N ILE B 222 6939 12351 8797 987 3 -215 N ATOM 4978 CA ILE B 222 108.510 -77.389 28.278 1.00 71.61 C ANISOU 4978 CA ILE B 222 6715 11794 8698 903 39 20 C ATOM 4979 C ILE B 222 107.374 -78.360 28.625 1.00 75.46 C ANISOU 4979 C ILE B 222 7241 12284 9147 1049 108 250 C ATOM 4980 O ILE B 222 106.230 -77.980 28.393 1.00 74.63 O ANISOU 4980 O ILE B 222 7165 11993 9199 1035 160 334 O ATOM 4981 CB ILE B 222 109.312 -77.825 27.020 1.00 72.90 C ANISOU 4981 CB ILE B 222 6885 11897 8918 782 -13 104 C ATOM 4982 CG1 ILE B 222 110.140 -76.635 26.479 1.00 73.95 C ANISOU 4982 CG1 ILE B 222 6976 11937 9185 607 -35 -74 C ATOM 4983 CG2 ILE B 222 108.392 -78.402 25.933 1.00 71.36 C ANISOU 4983 CG2 ILE B 222 6766 11502 8847 756 0 349 C ATOM 4984 CD1 ILE B 222 111.261 -76.989 25.530 1.00 81.04 C ANISOU 4984 CD1 ILE B 222 7846 12862 10085 512 -67 -43 C ATOM 4985 N PRO B 223 107.609 -79.545 29.242 1.00 72.82 N ANISOU 4985 N PRO B 223 6895 12145 8630 1196 122 359 N ATOM 4986 CA PRO B 223 106.475 -80.417 29.578 1.00 72.53 C ANISOU 4986 CA PRO B 223 6877 12070 8613 1321 218 595 C ATOM 4987 C PRO B 223 105.454 -79.721 30.482 1.00 77.52 C ANISOU 4987 C PRO B 223 7504 12701 9248 1412 317 559 C ATOM 4988 O PRO B 223 104.283 -79.702 30.114 1.00 77.00 O ANISOU 4988 O PRO B 223 7444 12440 9372 1390 377 700 O ATOM 4989 CB PRO B 223 107.136 -81.609 30.271 1.00 74.90 C ANISOU 4989 CB PRO B 223 7158 12603 8695 1480 230 688 C ATOM 4990 CG PRO B 223 108.518 -81.625 29.741 1.00 78.93 C ANISOU 4990 CG PRO B 223 7647 13198 9144 1396 117 559 C ATOM 4991 CD PRO B 223 108.888 -80.189 29.610 1.00 74.98 C ANISOU 4991 CD PRO B 223 7125 12664 8700 1261 63 299 C ATOM 4992 N LEU B 224 105.894 -79.076 31.591 1.00 75.34 N ANISOU 4992 N LEU B 224 7210 12639 8777 1510 324 345 N ATOM 4993 CA LEU B 224 104.993 -78.392 32.525 1.00 76.83 C ANISOU 4993 CA LEU B 224 7399 12857 8933 1626 428 277 C ATOM 4994 C LEU B 224 104.181 -77.277 31.851 1.00 80.50 C ANISOU 4994 C LEU B 224 7876 13034 9675 1489 441 217 C ATOM 4995 O LEU B 224 103.032 -77.092 32.241 1.00 81.60 O ANISOU 4995 O LEU B 224 8012 13107 9885 1576 555 299 O ATOM 4996 CB LEU B 224 105.742 -77.838 33.751 1.00 79.35 C ANISOU 4996 CB LEU B 224 7701 13473 8977 1753 399 -5 C ATOM 4997 CG LEU B 224 104.981 -77.701 35.092 1.00 86.29 C ANISOU 4997 CG LEU B 224 8590 14535 9661 1989 532 -23 C ATOM 4998 CD1 LEU B 224 104.437 -76.301 35.286 1.00 87.86 C ANISOU 4998 CD1 LEU B 224 8796 14609 9980 1950 557 -269 C ATOM 4999 CD2 LEU B 224 103.901 -78.763 35.269 1.00 87.77 C ANISOU 4999 CD2 LEU B 224 8785 14692 9871 2120 700 346 C ATOM 5000 N ILE B 225 104.745 -76.565 30.834 1.00 75.25 N ANISOU 5000 N ILE B 225 7220 12198 9175 1292 341 103 N ATOM 5001 CA ILE B 225 104.027 -75.528 30.074 1.00 74.09 C ANISOU 5001 CA ILE B 225 7090 11762 9299 1172 352 87 C ATOM 5002 C ILE B 225 102.755 -76.165 29.521 1.00 76.61 C ANISOU 5002 C ILE B 225 7412 11923 9772 1196 406 374 C ATOM 5003 O ILE B 225 101.675 -75.664 29.821 1.00 77.32 O ANISOU 5003 O ILE B 225 7488 11915 9975 1257 491 400 O ATOM 5004 CB ILE B 225 104.907 -74.883 28.963 1.00 76.27 C ANISOU 5004 CB ILE B 225 7377 11888 9715 969 257 -2 C ATOM 5005 CG1 ILE B 225 105.879 -73.847 29.570 1.00 78.70 C ANISOU 5005 CG1 ILE B 225 7649 12270 9983 923 223 -333 C ATOM 5006 CG2 ILE B 225 104.065 -74.255 27.837 1.00 75.67 C ANISOU 5006 CG2 ILE B 225 7334 11505 9911 868 266 124 C ATOM 5007 CD1 ILE B 225 107.088 -73.434 28.667 1.00 86.58 C ANISOU 5007 CD1 ILE B 225 8622 13191 11083 730 146 -422 C ATOM 5008 N PHE B 226 102.892 -77.316 28.810 1.00 70.85 N ANISOU 5008 N PHE B 226 6687 11186 9047 1161 358 569 N ATOM 5009 CA PHE B 226 101.818 -78.096 28.205 1.00 69.47 C ANISOU 5009 CA PHE B 226 6494 10866 9034 1165 375 816 C ATOM 5010 C PHE B 226 100.817 -78.597 29.221 1.00 73.94 C ANISOU 5010 C PHE B 226 7007 11498 9587 1325 515 944 C ATOM 5011 O PHE B 226 99.625 -78.383 29.014 1.00 73.70 O ANISOU 5011 O PHE B 226 6934 11311 9757 1331 564 1046 O ATOM 5012 CB PHE B 226 102.378 -79.286 27.429 1.00 70.16 C ANISOU 5012 CB PHE B 226 6597 10964 9097 1114 294 938 C ATOM 5013 CG PHE B 226 103.003 -78.943 26.102 1.00 70.87 C ANISOU 5013 CG PHE B 226 6735 10940 9253 960 174 894 C ATOM 5014 CD1 PHE B 226 104.332 -78.555 26.023 1.00 73.76 C ANISOU 5014 CD1 PHE B 226 7122 11408 9494 898 128 736 C ATOM 5015 CD2 PHE B 226 102.275 -79.050 24.924 1.00 72.90 C ANISOU 5015 CD2 PHE B 226 7004 11006 9690 889 107 1014 C ATOM 5016 CE1 PHE B 226 104.916 -78.250 24.792 1.00 74.18 C ANISOU 5016 CE1 PHE B 226 7215 11364 9606 767 52 724 C ATOM 5017 CE2 PHE B 226 102.855 -78.734 23.695 1.00 74.99 C ANISOU 5017 CE2 PHE B 226 7325 11194 9975 777 12 992 C ATOM 5018 CZ PHE B 226 104.173 -78.340 23.636 1.00 73.04 C ANISOU 5018 CZ PHE B 226 7105 11041 9606 717 1 861 C ATOM 5019 N ILE B 227 101.280 -79.271 30.303 1.00 71.83 N ANISOU 5019 N ILE B 227 6735 11468 9088 1466 588 956 N ATOM 5020 CA ILE B 227 100.409 -79.826 31.354 1.00 73.58 C ANISOU 5020 CA ILE B 227 6910 11783 9265 1645 759 1114 C ATOM 5021 C ILE B 227 99.546 -78.710 31.966 1.00 80.22 C ANISOU 5021 C ILE B 227 7730 12597 10152 1716 861 1013 C ATOM 5022 O ILE B 227 98.339 -78.899 32.133 1.00 80.66 O ANISOU 5022 O ILE B 227 7720 12561 10365 1778 984 1182 O ATOM 5023 CB ILE B 227 101.161 -80.619 32.474 1.00 77.83 C ANISOU 5023 CB ILE B 227 7461 12618 9494 1821 825 1146 C ATOM 5024 CG1 ILE B 227 102.436 -81.377 31.980 1.00 77.25 C ANISOU 5024 CG1 ILE B 227 7418 12619 9314 1762 696 1138 C ATOM 5025 CG2 ILE B 227 100.210 -81.570 33.206 1.00 80.23 C ANISOU 5025 CG2 ILE B 227 7711 12955 9818 1984 1020 1428 C ATOM 5026 CD1 ILE B 227 102.282 -82.541 30.919 1.00 84.94 C ANISOU 5026 CD1 ILE B 227 8381 13402 10492 1665 652 1352 C ATOM 5027 N ALA B 228 100.165 -77.555 32.270 1.00 78.15 N ANISOU 5027 N ALA B 228 7511 12400 9782 1702 811 729 N ATOM 5028 CA ALA B 228 99.502 -76.399 32.864 1.00 80.01 C ANISOU 5028 CA ALA B 228 7740 12605 10055 1774 898 575 C ATOM 5029 C ALA B 228 98.552 -75.706 31.881 1.00 84.62 C ANISOU 5029 C ALA B 228 8299 12878 10976 1658 880 631 C ATOM 5030 O ALA B 228 97.456 -75.340 32.304 1.00 86.19 O ANISOU 5030 O ALA B 228 8450 13019 11278 1758 1007 678 O ATOM 5031 CB ALA B 228 100.531 -75.406 33.381 1.00 81.79 C ANISOU 5031 CB ALA B 228 8011 12957 10109 1771 826 226 C ATOM 5032 N THR B 229 98.949 -75.520 30.590 1.00 79.29 N ANISOU 5032 N THR B 229 7650 12018 10458 1470 732 637 N ATOM 5033 CA THR B 229 98.092 -74.877 29.576 1.00 78.51 C ANISOU 5033 CA THR B 229 7532 11643 10654 1380 695 711 C ATOM 5034 C THR B 229 96.821 -75.700 29.341 1.00 81.31 C ANISOU 5034 C THR B 229 7798 11919 11179 1427 749 976 C ATOM 5035 O THR B 229 95.728 -75.127 29.258 1.00 82.15 O ANISOU 5035 O THR B 229 7844 11884 11486 1466 804 1025 O ATOM 5036 CB THR B 229 98.823 -74.601 28.255 1.00 89.55 C ANISOU 5036 CB THR B 229 8985 12901 12137 1200 539 692 C ATOM 5037 OG1 THR B 229 99.809 -75.582 27.962 1.00 93.99 O ANISOU 5037 OG1 THR B 229 9575 13589 12546 1144 459 728 O ATOM 5038 CG2 THR B 229 99.456 -73.222 28.210 1.00 90.51 C ANISOU 5038 CG2 THR B 229 9156 12936 12296 1131 520 459 C ATOM 5039 N CYS B 230 96.963 -77.042 29.301 1.00 75.85 N ANISOU 5039 N CYS B 230 7080 11311 10426 1430 740 1139 N ATOM 5040 CA CYS B 230 95.861 -77.984 29.110 1.00 74.96 C ANISOU 5040 CA CYS B 230 6861 11116 10506 1455 789 1381 C ATOM 5041 C CYS B 230 94.913 -77.984 30.307 1.00 79.18 C ANISOU 5041 C CYS B 230 7308 11726 11049 1626 1006 1459 C ATOM 5042 O CYS B 230 93.710 -77.986 30.083 1.00 78.65 O ANISOU 5042 O CYS B 230 7127 11521 11235 1638 1056 1591 O ATOM 5043 CB CYS B 230 96.384 -79.386 28.811 1.00 74.04 C ANISOU 5043 CB CYS B 230 6747 11048 10338 1414 736 1508 C ATOM 5044 SG CYS B 230 97.153 -79.550 27.181 1.00 75.72 S ANISOU 5044 SG CYS B 230 7034 11140 10597 1227 495 1463 S ATOM 5045 N TYR B 231 95.434 -77.947 31.558 1.00 77.05 N ANISOU 5045 N TYR B 231 7085 11690 10501 1770 1132 1374 N ATOM 5046 CA TYR B 231 94.584 -77.918 32.749 1.00 79.58 C ANISOU 5046 CA TYR B 231 7338 12121 10779 1964 1363 1449 C ATOM 5047 C TYR B 231 93.719 -76.650 32.784 1.00 86.36 C ANISOU 5047 C TYR B 231 8160 12856 11796 1999 1415 1338 C ATOM 5048 O TYR B 231 92.513 -76.744 33.018 1.00 86.76 O ANISOU 5048 O TYR B 231 8090 12842 12034 2079 1560 1495 O ATOM 5049 CB TYR B 231 95.390 -78.039 34.061 1.00 82.29 C ANISOU 5049 CB TYR B 231 7755 12776 10733 2139 1465 1351 C ATOM 5050 CG TYR B 231 94.557 -77.686 35.282 1.00 86.88 C ANISOU 5050 CG TYR B 231 8294 13493 11224 2363 1705 1368 C ATOM 5051 CD1 TYR B 231 93.486 -78.487 35.677 1.00 90.15 C ANISOU 5051 CD1 TYR B 231 8588 13896 11768 2467 1915 1668 C ATOM 5052 CD2 TYR B 231 94.780 -76.502 35.983 1.00 88.99 C ANISOU 5052 CD2 TYR B 231 8626 13873 11312 2464 1729 1075 C ATOM 5053 CE1 TYR B 231 92.667 -78.127 36.743 1.00 93.43 C ANISOU 5053 CE1 TYR B 231 8955 14433 12110 2681 2159 1699 C ATOM 5054 CE2 TYR B 231 93.974 -76.138 37.059 1.00 92.57 C ANISOU 5054 CE2 TYR B 231 9045 14452 11676 2685 1955 1073 C ATOM 5055 CZ TYR B 231 92.920 -76.955 37.438 1.00102.02 C ANISOU 5055 CZ TYR B 231 10128 15659 12977 2801 2178 1397 C ATOM 5056 OH TYR B 231 92.126 -76.614 38.506 1.00106.51 O ANISOU 5056 OH TYR B 231 10656 16368 13444 3036 2429 1413 O ATOM 5057 N PHE B 232 94.339 -75.476 32.589 1.00 84.65 N ANISOU 5057 N PHE B 232 8037 12601 11525 1944 1311 1071 N ATOM 5058 CA PHE B 232 93.643 -74.191 32.607 1.00 86.82 C ANISOU 5058 CA PHE B 232 8294 12734 11959 1982 1357 942 C ATOM 5059 C PHE B 232 92.793 -73.994 31.339 1.00 91.10 C ANISOU 5059 C PHE B 232 8760 12996 12857 1863 1259 1086 C ATOM 5060 O PHE B 232 91.860 -73.187 31.349 1.00 91.96 O ANISOU 5060 O PHE B 232 8807 12975 13158 1928 1328 1078 O ATOM 5061 CB PHE B 232 94.635 -73.034 32.804 1.00 89.37 C ANISOU 5061 CB PHE B 232 8734 13075 12148 1952 1281 608 C ATOM 5062 CG PHE B 232 95.176 -72.956 34.214 1.00 92.91 C ANISOU 5062 CG PHE B 232 9231 13811 12260 2122 1385 412 C ATOM 5063 CD1 PHE B 232 94.407 -72.431 35.244 1.00 98.60 C ANISOU 5063 CD1 PHE B 232 9925 14612 12927 2324 1572 332 C ATOM 5064 CD2 PHE B 232 96.455 -73.406 34.512 1.00 94.41 C ANISOU 5064 CD2 PHE B 232 9490 14210 12172 2098 1292 300 C ATOM 5065 CE1 PHE B 232 94.905 -72.373 36.549 1.00101.46 C ANISOU 5065 CE1 PHE B 232 10341 15276 12934 2509 1657 138 C ATOM 5066 CE2 PHE B 232 96.950 -73.346 35.818 1.00 99.19 C ANISOU 5066 CE2 PHE B 232 10135 15115 12438 2279 1364 111 C ATOM 5067 CZ PHE B 232 96.173 -72.830 36.826 1.00 99.92 C ANISOU 5067 CZ PHE B 232 10213 15299 12453 2486 1542 26 C ATOM 5068 N GLY B 233 93.110 -74.747 30.285 1.00 86.37 N ANISOU 5068 N GLY B 233 8163 12324 12328 1713 1097 1212 N ATOM 5069 CA GLY B 233 92.357 -74.760 29.039 1.00 85.65 C ANISOU 5069 CA GLY B 233 7999 12016 12527 1614 972 1353 C ATOM 5070 C GLY B 233 91.108 -75.611 29.181 1.00 90.39 C ANISOU 5070 C GLY B 233 8424 12591 13330 1673 1064 1581 C ATOM 5071 O GLY B 233 90.145 -75.434 28.431 1.00 90.41 O ANISOU 5071 O GLY B 233 8316 12430 13606 1646 997 1680 O ATOM 5072 N ILE B 234 91.126 -76.548 30.154 1.00 87.66 N ANISOU 5072 N ILE B 234 8039 12408 12860 1761 1222 1676 N ATOM 5073 CA ILE B 234 90.014 -77.443 30.508 1.00 88.72 C ANISOU 5073 CA ILE B 234 7991 12528 13192 1824 1369 1911 C ATOM 5074 C ILE B 234 89.168 -76.748 31.602 1.00 94.11 C ANISOU 5074 C ILE B 234 8599 13273 13884 2014 1614 1906 C ATOM 5075 O ILE B 234 87.937 -76.823 31.580 1.00 94.65 O ANISOU 5075 O ILE B 234 8485 13244 14234 2056 1709 2056 O ATOM 5076 CB ILE B 234 90.547 -78.850 30.942 1.00 91.57 C ANISOU 5076 CB ILE B 234 8359 13013 13421 1827 1432 2050 C ATOM 5077 CG1 ILE B 234 91.094 -79.635 29.722 1.00 90.25 C ANISOU 5077 CG1 ILE B 234 8223 12737 13332 1644 1196 2074 C ATOM 5078 CG2 ILE B 234 89.483 -79.681 31.681 1.00 94.04 C ANISOU 5078 CG2 ILE B 234 8488 13335 13906 1930 1672 2302 C ATOM 5079 CD1 ILE B 234 92.154 -80.750 30.050 1.00 95.62 C ANISOU 5079 CD1 ILE B 234 8989 13549 13792 1642 1207 2121 C ATOM 5080 N ARG B 235 89.841 -76.064 32.542 1.00 91.05 N ANISOU 5080 N ARG B 235 8345 13056 13196 2132 1709 1715 N ATOM 5081 CA ARG B 235 89.211 -75.324 33.631 1.00 93.01 C ANISOU 5081 CA ARG B 235 8559 13394 13386 2334 1937 1649 C ATOM 5082 C ARG B 235 88.388 -74.166 33.095 1.00 97.94 C ANISOU 5082 C ARG B 235 9122 13810 14281 2331 1901 1573 C ATOM 5083 O ARG B 235 87.274 -73.984 33.578 1.00100.35 O ANISOU 5083 O ARG B 235 9287 14100 14742 2467 2088 1669 O ATOM 5084 CB ARG B 235 90.259 -74.805 34.627 1.00 93.45 C ANISOU 5084 CB ARG B 235 8785 13678 13042 2447 1985 1394 C ATOM 5085 CG ARG B 235 89.671 -74.306 35.943 1.00104.85 C ANISOU 5085 CG ARG B 235 10206 15287 14345 2700 2249 1331 C ATOM 5086 CD ARG B 235 90.739 -73.818 36.896 1.00113.48 C ANISOU 5086 CD ARG B 235 11463 16627 15027 2814 2255 1038 C ATOM 5087 NE ARG B 235 90.497 -72.437 37.316 1.00124.14 N ANISOU 5087 NE ARG B 235 12853 17938 16376 2919 2306 750 N ATOM 5088 CZ ARG B 235 91.246 -71.776 38.194 1.00139.11 C ANISOU 5088 CZ ARG B 235 14872 20025 17960 3036 2312 425 C ATOM 5089 NH1 ARG B 235 92.295 -72.363 38.758 1.00123.01 N ANISOU 5089 NH1 ARG B 235 12922 18257 15560 3074 2262 358 N ATOM 5090 NH2 ARG B 235 90.953 -70.521 38.512 1.00129.14 N ANISOU 5090 NH2 ARG B 235 13636 18681 16751 3123 2359 151 N ATOM 5091 N LYS B 236 88.918 -73.385 32.122 1.00 92.76 N ANISOU 5091 N LYS B 236 8564 12995 13687 2194 1681 1423 N ATOM 5092 CA LYS B 236 88.208 -72.234 31.548 1.00 93.51 C ANISOU 5092 CA LYS B 236 8615 12874 14039 2204 1638 1368 C ATOM 5093 C LYS B 236 86.925 -72.661 30.812 1.00 99.66 C ANISOU 5093 C LYS B 236 9185 13508 15172 2181 1607 1615 C ATOM 5094 O LYS B 236 85.883 -72.038 31.017 1.00101.02 O ANISOU 5094 O LYS B 236 9236 13600 15548 2301 1720 1645 O ATOM 5095 CB LYS B 236 89.115 -71.419 30.614 1.00 93.90 C ANISOU 5095 CB LYS B 236 8816 12783 14080 2061 1424 1206 C ATOM 5096 N HIS B 237 86.996 -73.740 30.000 1.00 96.42 N ANISOU 5096 N HIS B 237 8722 13073 14842 2038 1455 1775 N ATOM 5097 CA HIS B 237 85.879 -74.269 29.206 1.00 97.42 C ANISOU 5097 CA HIS B 237 8637 13070 15309 1989 1372 1976 C ATOM 5098 C HIS B 237 84.754 -74.820 30.084 1.00105.15 C ANISOU 5098 C HIS B 237 9395 14101 16455 2112 1620 2146 C ATOM 5099 O HIS B 237 83.588 -74.496 29.849 1.00106.47 O ANISOU 5099 O HIS B 237 9369 14160 16925 2166 1644 2234 O ATOM 5100 CB HIS B 237 86.372 -75.360 28.236 1.00 96.43 C ANISOU 5100 CB HIS B 237 8527 12922 15192 1811 1153 2052 C ATOM 5101 CG HIS B 237 85.368 -75.773 27.200 1.00100.43 C ANISOU 5101 CG HIS B 237 8835 13286 16036 1741 988 2188 C ATOM 5102 ND1 HIS B 237 85.354 -75.197 25.939 1.00101.76 N ANISOU 5102 ND1 HIS B 237 9041 13338 16284 1676 735 2148 N ATOM 5103 CD2 HIS B 237 84.391 -76.708 27.262 1.00103.53 C ANISOU 5103 CD2 HIS B 237 8989 13648 16702 1730 1038 2356 C ATOM 5104 CE1 HIS B 237 84.370 -75.791 25.282 1.00102.15 C ANISOU 5104 CE1 HIS B 237 8875 13311 16626 1638 615 2268 C ATOM 5105 NE2 HIS B 237 83.762 -76.707 26.037 1.00103.61 N ANISOU 5105 NE2 HIS B 237 8877 13529 16960 1655 788 2386 N ATOM 5106 N LEU B 238 85.096 -75.639 31.089 1.00103.46 N ANISOU 5106 N LEU B 238 9200 14057 16051 2168 1812 2209 N ATOM 5107 CA LEU B 238 84.099 -76.248 31.963 1.00106.38 C ANISOU 5107 CA LEU B 238 9364 14487 16569 2289 2088 2411 C ATOM 5108 C LEU B 238 83.515 -75.254 32.986 1.00114.46 C ANISOU 5108 C LEU B 238 10362 15588 17539 2513 2344 2342 C ATOM 5109 O LEU B 238 82.489 -75.557 33.603 1.00116.69 O ANISOU 5109 O LEU B 238 10441 15898 17999 2630 2587 2518 O ATOM 5110 CB LEU B 238 84.671 -77.492 32.665 1.00106.35 C ANISOU 5110 CB LEU B 238 9397 14636 16375 2294 2222 2541 C ATOM 5111 CG LEU B 238 84.544 -78.852 31.935 1.00110.29 C ANISOU 5111 CG LEU B 238 9772 15021 17114 2122 2106 2728 C ATOM 5112 CD1 LEU B 238 83.147 -79.078 31.348 1.00112.05 C ANISOU 5112 CD1 LEU B 238 9694 15057 17823 2067 2087 2879 C ATOM 5113 CD2 LEU B 238 85.597 -79.025 30.872 1.00109.55 C ANISOU 5113 CD2 LEU B 238 9846 14870 16906 1944 1789 2594 C ATOM 5114 N LEU B 239 84.134 -74.066 33.133 1.00111.77 N ANISOU 5114 N LEU B 239 10213 15265 16987 2570 2297 2083 N ATOM 5115 CA LEU B 239 83.647 -73.014 34.030 1.00114.52 C ANISOU 5115 CA LEU B 239 10561 15664 17287 2785 2514 1959 C ATOM 5116 C LEU B 239 82.619 -72.124 33.313 1.00120.88 C ANISOU 5116 C LEU B 239 11223 16248 18459 2802 2449 1966 C ATOM 5117 O LEU B 239 81.702 -71.608 33.957 1.00123.31 O ANISOU 5117 O LEU B 239 11407 16565 18881 2987 2671 1982 O ATOM 5118 CB LEU B 239 84.814 -72.166 34.552 1.00114.16 C ANISOU 5118 CB LEU B 239 10777 15723 16875 2834 2487 1644 C ATOM 5119 CG LEU B 239 84.947 -72.067 36.067 1.00121.05 C ANISOU 5119 CG LEU B 239 11714 16858 17421 3068 2764 1545 C ATOM 5120 CD1 LEU B 239 86.100 -72.912 36.571 1.00119.88 C ANISOU 5120 CD1 LEU B 239 11710 16942 16896 3045 2744 1529 C ATOM 5121 CD2 LEU B 239 85.154 -70.630 36.491 1.00125.78 C ANISOU 5121 CD2 LEU B 239 12438 17433 17918 3188 2789 1211 C ATOM 5122 N LYS B 240 82.767 -71.969 31.976 1.00116.49 N ANISOU 5122 N LYS B 240 10679 15505 18075 2627 2151 1968 N ATOM 5123 CA LYS B 240 81.902 -71.160 31.108 1.00117.45 C ANISOU 5123 CA LYS B 240 10680 15418 18526 2639 2033 1995 C ATOM 5124 C LYS B 240 80.515 -71.808 30.890 1.00124.15 C ANISOU 5124 C LYS B 240 11202 16220 19747 2661 2084 2243 C ATOM 5125 O LYS B 240 79.609 -71.144 30.382 1.00124.61 O ANISOU 5125 O LYS B 240 11112 16141 20092 2724 2031 2281 O ATOM 5126 CB LYS B 240 82.595 -70.920 29.753 1.00117.56 C ANISOU 5126 CB LYS B 240 10826 15294 18549 2461 1701 1945 C ATOM 5127 N THR B 241 80.353 -73.086 31.289 1.00122.60 N ANISOU 5127 N THR B 241 10884 16131 19569 2615 2191 2412 N ATOM 5128 CA THR B 241 79.117 -73.869 31.147 1.00125.03 C ANISOU 5128 CA THR B 241 10856 16389 20259 2604 2255 2648 C ATOM 5129 C THR B 241 78.026 -73.447 32.161 1.00133.11 C ANISOU 5129 C THR B 241 11683 17461 21430 2828 2597 2726 C ATOM 5130 O THR B 241 76.844 -73.428 31.801 1.00134.65 O ANISOU 5130 O THR B 241 11588 17557 22017 2854 2598 2856 O ATOM 5131 CB THR B 241 79.413 -75.374 31.279 1.00134.29 C ANISOU 5131 CB THR B 241 11979 17627 21416 2473 2282 2802 C ATOM 5132 OG1 THR B 241 79.953 -75.645 32.576 1.00135.88 O ANISOU 5132 OG1 THR B 241 12308 18022 21296 2594 2574 2811 O ATOM 5133 CG2 THR B 241 80.355 -75.892 30.189 1.00129.80 C ANISOU 5133 CG2 THR B 241 11564 17000 20754 2258 1944 2734 C ATOM 5134 N ASN B 242 78.428 -73.130 33.419 1.00130.82 N ANISOU 5134 N ASN B 242 11544 17342 20820 3001 2880 2640 N ATOM 5135 CA ASN B 242 77.575 -72.711 34.545 1.00134.10 C ANISOU 5135 CA ASN B 242 11829 17855 21269 3251 3247 2684 C ATOM 5136 C ASN B 242 76.503 -73.773 34.889 1.00138.92 C ANISOU 5136 C ASN B 242 12102 18491 22188 3267 3477 2997 C ATOM 5137 O ASN B 242 75.315 -73.625 34.570 1.00140.30 O ANISOU 5137 O ASN B 242 11979 18554 22774 3300 3510 3117 O ATOM 5138 CB ASN B 242 76.940 -71.329 34.315 1.00139.85 C ANISOU 5138 CB ASN B 242 12515 18452 22168 3387 3229 2547 C ATOM 5139 CG ASN B 242 77.506 -70.254 35.212 1.00173.29 C ANISOU 5139 CG ASN B 242 16998 22779 26065 3577 3382 2277 C ATOM 5140 OD1 ASN B 242 78.586 -69.699 34.962 1.00168.46 O ANISOU 5140 OD1 ASN B 242 16660 22137 25211 3505 3198 2045 O ATOM 5141 ND2 ASN B 242 76.785 -69.940 36.281 1.00168.55 N ANISOU 5141 ND2 ASN B 242 16296 22291 25453 3827 3728 2290 N ATOM 5142 N SER B 243 76.963 -74.840 35.562 1.00134.20 N ANISOU 5142 N SER B 243 11550 18042 21399 3249 3643 3134 N ATOM 5143 CA SER B 243 76.176 -75.980 36.040 1.00135.39 C ANISOU 5143 CA SER B 243 11422 18223 21798 3256 3910 3454 C ATOM 5144 C SER B 243 75.598 -75.673 37.421 1.00140.04 C ANISOU 5144 C SER B 243 11946 19002 22259 3552 4368 3540 C ATOM 5145 O SER B 243 76.286 -75.074 38.249 1.00139.28 O ANISOU 5145 O SER B 243 12115 19097 21708 3730 4487 3360 O ATOM 5146 CB SER B 243 77.048 -77.229 36.085 1.00137.45 C ANISOU 5146 CB SER B 243 11796 18536 21893 3114 3872 3568 C ATOM 5147 OG SER B 243 78.321 -76.945 36.641 1.00144.26 O ANISOU 5147 OG SER B 243 13016 19585 22213 3189 3861 3382 O ATOM 5148 N TYR B 244 74.344 -76.081 37.672 1.00138.40 N ANISOU 5148 N TYR B 244 11380 18753 22452 3610 4626 3803 N ATOM 5149 CA TYR B 244 73.652 -75.759 38.923 1.00141.45 C ANISOU 5149 CA TYR B 244 11668 19319 22756 3910 5088 3906 C ATOM 5150 C TYR B 244 73.228 -76.976 39.759 1.00145.94 C ANISOU 5150 C TYR B 244 12045 19993 23412 3965 5483 4282 C ATOM 5151 O TYR B 244 73.402 -76.948 40.980 1.00147.16 O ANISOU 5151 O TYR B 244 12321 20403 23191 4219 5842 4342 O ATOM 5152 CB TYR B 244 72.423 -74.851 38.672 1.00145.16 C ANISOU 5152 CB TYR B 244 11870 19673 23614 4016 5138 3879 C ATOM 5153 CG TYR B 244 71.708 -75.020 37.342 1.00146.58 C ANISOU 5153 CG TYR B 244 11759 19585 24352 3786 4818 3937 C ATOM 5154 CD1 TYR B 244 72.225 -74.464 36.173 1.00145.74 C ANISOU 5154 CD1 TYR B 244 11806 19325 24244 3625 4360 3708 C ATOM 5155 CD2 TYR B 244 70.460 -75.633 37.272 1.00150.19 C ANISOU 5155 CD2 TYR B 244 11773 19953 25340 3755 4983 4212 C ATOM 5156 CE1 TYR B 244 71.562 -74.593 34.955 1.00146.64 C ANISOU 5156 CE1 TYR B 244 11661 19232 24823 3448 4051 3751 C ATOM 5157 CE2 TYR B 244 69.776 -75.749 36.061 1.00150.96 C ANISOU 5157 CE2 TYR B 244 11586 19830 25943 3562 4662 4231 C ATOM 5158 CZ TYR B 244 70.329 -75.222 34.905 1.00156.16 C ANISOU 5158 CZ TYR B 244 12424 20367 26544 3420 4188 3996 C ATOM 5159 OH TYR B 244 69.660 -75.332 33.708 1.00158.20 O ANISOU 5159 OH TYR B 244 12411 20444 27254 3259 3855 4008 O ATOM 5160 N GLY B 245 72.655 -77.996 39.120 1.00141.80 N ANISOU 5160 N GLY B 245 11221 19275 23383 3744 5425 4528 N ATOM 5161 CA GLY B 245 72.177 -79.199 39.796 1.00143.98 C ANISOU 5161 CA GLY B 245 11270 19582 23853 3762 5801 4918 C ATOM 5162 C GLY B 245 73.280 -80.168 40.167 1.00144.90 C ANISOU 5162 C GLY B 245 11637 19798 23620 3713 5827 5020 C ATOM 5163 O GLY B 245 74.317 -79.756 40.697 1.00142.84 O ANISOU 5163 O GLY B 245 11743 19755 22775 3851 5807 4838 O ATOM 5164 N LYS B 246 73.069 -81.474 39.876 1.00141.18 N ANISOU 5164 N LYS B 246 10956 19158 23529 3516 5862 5302 N ATOM 5165 CA LYS B 246 74.062 -82.528 40.135 1.00139.36 C ANISOU 5165 CA LYS B 246 10927 18974 23049 3456 5883 5438 C ATOM 5166 C LYS B 246 75.220 -82.419 39.122 1.00136.47 C ANISOU 5166 C LYS B 246 10849 18528 22476 3245 5363 5121 C ATOM 5167 O LYS B 246 76.242 -83.088 39.274 1.00134.35 O ANISOU 5167 O LYS B 246 10809 18324 21914 3212 5316 5152 O ATOM 5168 CB LYS B 246 73.423 -83.939 40.138 1.00144.69 C ANISOU 5168 CB LYS B 246 11271 19448 24256 3312 6106 5840 C ATOM 5169 CG LYS B 246 72.893 -84.469 38.792 1.00158.61 C ANISOU 5169 CG LYS B 246 12741 20850 26675 2963 5756 5799 C ATOM 5170 CD LYS B 246 73.927 -85.285 37.966 1.00166.08 C ANISOU 5170 CD LYS B 246 13876 21648 27577 2714 5386 5694 C ATOM 5171 CE LYS B 246 74.424 -86.569 38.604 1.00180.57 C ANISOU 5171 CE LYS B 246 15766 23476 29368 2722 5654 6010 C ATOM 5172 NZ LYS B 246 73.341 -87.578 38.762 1.00196.72 N ANISOU 5172 NZ LYS B 246 17380 25291 32075 2627 5962 6379 N ATOM 5173 N ASN B 247 75.033 -81.579 38.086 1.00129.90 N ANISOU 5173 N ASN B 247 9992 17559 21805 3117 4990 4837 N ATOM 5174 CA ASN B 247 76.012 -81.276 37.050 1.00125.15 C ANISOU 5174 CA ASN B 247 9642 16883 21026 2936 4509 4530 C ATOM 5175 C ASN B 247 77.132 -80.423 37.650 1.00126.84 C ANISOU 5175 C ASN B 247 10258 17348 20588 3112 4493 4288 C ATOM 5176 O ASN B 247 78.257 -80.495 37.163 1.00123.55 O ANISOU 5176 O ASN B 247 10100 16937 19907 2995 4206 4110 O ATOM 5177 CB ASN B 247 75.367 -80.590 35.828 1.00125.02 C ANISOU 5177 CB ASN B 247 9461 16665 21377 2790 4161 4346 C ATOM 5178 CG ASN B 247 74.011 -79.945 36.057 1.00157.75 C ANISOU 5178 CG ASN B 247 13292 20782 25862 2922 4359 4421 C ATOM 5179 OD1 ASN B 247 73.023 -80.605 36.400 1.00156.15 O ANISOU 5179 OD1 ASN B 247 12748 20517 26065 2927 4629 4695 O ATOM 5180 ND2 ASN B 247 73.913 -78.648 35.802 1.00150.00 N ANISOU 5180 ND2 ASN B 247 12400 19823 24771 3021 4221 4185 N ATOM 5181 N ARG B 248 76.834 -79.640 38.721 1.00125.32 N ANISOU 5181 N ARG B 248 10107 17366 20142 3396 4805 4268 N ATOM 5182 CA ARG B 248 77.816 -78.834 39.461 1.00124.40 C ANISOU 5182 CA ARG B 248 10344 17509 19415 3592 4826 4019 C ATOM 5183 C ARG B 248 78.729 -79.767 40.265 1.00129.79 C ANISOU 5183 C ARG B 248 11209 18399 19706 3670 4982 4168 C ATOM 5184 O ARG B 248 79.922 -79.493 40.417 1.00127.60 O ANISOU 5184 O ARG B 248 11238 18275 18970 3698 4818 3943 O ATOM 5185 CB ARG B 248 77.126 -77.819 40.379 1.00126.72 C ANISOU 5185 CB ARG B 248 10599 17960 19587 3887 5128 3952 C ATOM 5186 N ILE B 249 78.157 -80.886 40.759 1.00129.29 N ANISOU 5186 N ILE B 249 10939 18330 19854 3704 5300 4561 N ATOM 5187 CA ILE B 249 78.856 -81.953 41.477 1.00129.53 C ANISOU 5187 CA ILE B 249 11091 18519 19607 3783 5486 4798 C ATOM 5188 C ILE B 249 79.705 -82.755 40.477 1.00128.58 C ANISOU 5188 C ILE B 249 11055 18208 19591 3495 5125 4760 C ATOM 5189 O ILE B 249 80.851 -83.099 40.785 1.00127.05 O ANISOU 5189 O ILE B 249 11117 18175 18980 3542 5060 4719 O ATOM 5190 CB ILE B 249 77.847 -82.853 42.228 1.00136.90 C ANISOU 5190 CB ILE B 249 11741 19449 20827 3899 5964 5263 C ATOM 5191 N THR B 250 79.150 -83.008 39.265 1.00122.85 N ANISOU 5191 N THR B 250 10115 17156 19407 3214 4877 4749 N ATOM 5192 CA THR B 250 79.801 -83.747 38.181 1.00119.51 C ANISOU 5192 CA THR B 250 9739 16525 19143 2935 4522 4689 C ATOM 5193 C THR B 250 80.980 -82.950 37.582 1.00118.79 C ANISOU 5193 C THR B 250 9966 16505 18665 2869 4131 4302 C ATOM 5194 O THR B 250 82.039 -83.544 37.379 1.00116.08 O ANISOU 5194 O THR B 250 9808 16185 18112 2792 3978 4268 O ATOM 5195 CB THR B 250 78.783 -84.159 37.102 1.00126.88 C ANISOU 5195 CB THR B 250 10338 17124 20747 2685 4367 4754 C ATOM 5196 N ARG B 251 80.817 -81.626 37.331 1.00114.42 N ANISOU 5196 N ARG B 251 9468 15977 18030 2909 3993 4026 N ATOM 5197 CA ARG B 251 81.885 -80.789 36.766 1.00111.01 C ANISOU 5197 CA ARG B 251 9315 15585 17279 2843 3652 3673 C ATOM 5198 C ARG B 251 83.078 -80.682 37.732 1.00114.47 C ANISOU 5198 C ARG B 251 10046 16319 17129 3016 3738 3572 C ATOM 5199 O ARG B 251 84.218 -80.732 37.275 1.00111.28 O ANISOU 5199 O ARG B 251 9847 15936 16500 2908 3479 3400 O ATOM 5200 CB ARG B 251 81.381 -79.394 36.333 1.00110.75 C ANISOU 5200 CB ARG B 251 9262 15483 17336 2862 3524 3434 C ATOM 5201 CG ARG B 251 81.077 -78.389 37.445 1.00122.62 C ANISOU 5201 CG ARG B 251 10815 17183 18592 3140 3796 3343 C ATOM 5202 CD ARG B 251 82.031 -77.206 37.431 1.00125.65 C ANISOU 5202 CD ARG B 251 11482 17654 18604 3181 3607 2972 C ATOM 5203 NE ARG B 251 81.679 -76.212 38.447 1.00130.08 N ANISOU 5203 NE ARG B 251 12082 18378 18965 3446 3851 2841 N ATOM 5204 CZ ARG B 251 82.139 -76.206 39.697 1.00139.61 C ANISOU 5204 CZ ARG B 251 13432 19879 19734 3677 4083 2803 C ATOM 5205 NH1 ARG B 251 82.989 -77.143 40.104 1.00114.29 N ANISOU 5205 NH1 ARG B 251 10343 16842 16241 3681 4106 2910 N ATOM 5206 NH2 ARG B 251 81.754 -75.266 40.548 1.00132.19 N ANISOU 5206 NH2 ARG B 251 12521 19077 18630 3923 4290 2652 N ATOM 5207 N ASP B 252 82.815 -80.580 39.052 1.00114.03 N ANISOU 5207 N ASP B 252 9996 16505 16825 3291 4100 3684 N ATOM 5208 CA ASP B 252 83.843 -80.497 40.093 1.00114.43 C ANISOU 5208 CA ASP B 252 10300 16884 16294 3500 4198 3594 C ATOM 5209 C ASP B 252 84.715 -81.760 40.099 1.00117.66 C ANISOU 5209 C ASP B 252 10792 17334 16580 3438 4160 3777 C ATOM 5210 O ASP B 252 85.939 -81.653 40.189 1.00115.87 O ANISOU 5210 O ASP B 252 10798 17266 15962 3451 3983 3582 O ATOM 5211 CB ASP B 252 83.196 -80.284 41.473 1.00120.18 C ANISOU 5211 CB ASP B 252 10982 17866 16814 3829 4624 3731 C ATOM 5212 N GLN B 253 84.081 -82.946 39.955 1.00115.00 N ANISOU 5212 N GLN B 253 10249 16829 16617 3360 4317 4141 N ATOM 5213 CA GLN B 253 84.731 -84.260 39.909 1.00114.07 C ANISOU 5213 CA GLN B 253 10169 16681 16491 3297 4316 4363 C ATOM 5214 C GLN B 253 85.674 -84.389 38.689 1.00113.43 C ANISOU 5214 C GLN B 253 10210 16438 16452 3033 3883 4133 C ATOM 5215 O GLN B 253 86.772 -84.933 38.827 1.00111.95 O ANISOU 5215 O GLN B 253 10196 16365 15976 3053 3803 4129 O ATOM 5216 CB GLN B 253 83.671 -85.369 39.887 1.00117.78 C ANISOU 5216 CB GLN B 253 10347 16926 17477 3235 4571 4771 C ATOM 5217 N VAL B 254 85.252 -83.866 37.511 1.00107.64 N ANISOU 5217 N VAL B 254 9387 15458 16055 2809 3611 3947 N ATOM 5218 CA VAL B 254 86.030 -83.870 36.255 1.00103.76 C ANISOU 5218 CA VAL B 254 9001 14813 15611 2568 3206 3723 C ATOM 5219 C VAL B 254 87.258 -82.964 36.429 1.00105.65 C ANISOU 5219 C VAL B 254 9520 15273 15350 2633 3037 3407 C ATOM 5220 O VAL B 254 88.361 -83.326 36.008 1.00102.83 O ANISOU 5220 O VAL B 254 9314 14937 14820 2542 2833 3310 O ATOM 5221 CB VAL B 254 85.165 -83.440 35.037 1.00106.29 C ANISOU 5221 CB VAL B 254 9149 14858 16378 2364 2984 3622 C ATOM 5222 CG1 VAL B 254 85.993 -83.336 33.757 1.00102.75 C ANISOU 5222 CG1 VAL B 254 8834 14293 15913 2152 2582 3387 C ATOM 5223 CG2 VAL B 254 83.998 -84.390 34.841 1.00108.22 C ANISOU 5223 CG2 VAL B 254 9088 14881 17150 2279 3122 3903 C ATOM 5224 N LEU B 255 87.047 -81.801 37.080 1.00103.39 N ANISOU 5224 N LEU B 255 9286 15144 14856 2795 3135 3243 N ATOM 5225 CA LEU B 255 88.063 -80.795 37.378 1.00102.12 C ANISOU 5225 CA LEU B 255 9354 15182 14266 2869 3005 2914 C ATOM 5226 C LEU B 255 89.122 -81.323 38.354 1.00105.49 C ANISOU 5226 C LEU B 255 9944 15911 14228 3038 3095 2941 C ATOM 5227 O LEU B 255 90.288 -80.933 38.249 1.00103.16 O ANISOU 5227 O LEU B 255 9826 15731 13638 3008 2887 2685 O ATOM 5228 CB LEU B 255 87.392 -79.531 37.956 1.00104.06 C ANISOU 5228 CB LEU B 255 9583 15500 14457 3028 3139 2754 C ATOM 5229 CG LEU B 255 87.278 -78.290 37.040 1.00107.62 C ANISOU 5229 CG LEU B 255 10055 15761 15075 2892 2898 2472 C ATOM 5230 CD1 LEU B 255 88.651 -77.768 36.612 1.00105.87 C ANISOU 5230 CD1 LEU B 255 10052 15580 14592 2786 2618 2170 C ATOM 5231 CD2 LEU B 255 86.395 -78.549 35.832 1.00108.94 C ANISOU 5231 CD2 LEU B 255 10032 15619 15741 2691 2768 2607 C ATOM 5232 N LYS B 256 88.711 -82.207 39.294 1.00103.73 N ANISOU 5232 N LYS B 256 9647 15817 13951 3222 3409 3263 N ATOM 5233 CA LYS B 256 89.586 -82.837 40.281 1.00104.24 C ANISOU 5233 CA LYS B 256 9845 16184 13579 3427 3529 3363 C ATOM 5234 C LYS B 256 90.549 -83.808 39.586 1.00106.00 C ANISOU 5234 C LYS B 256 10131 16314 13831 3263 3319 3419 C ATOM 5235 O LYS B 256 91.723 -83.858 39.953 1.00104.74 O ANISOU 5235 O LYS B 256 10137 16385 13274 3349 3216 3295 O ATOM 5236 CB LYS B 256 88.770 -83.551 41.371 1.00109.80 C ANISOU 5236 CB LYS B 256 10436 17013 14269 3669 3950 3752 C ATOM 5237 N MET B 257 90.062 -84.538 38.559 1.00101.64 N ANISOU 5237 N MET B 257 9437 15427 13752 3032 3239 3576 N ATOM 5238 CA MET B 257 90.848 -85.483 37.757 1.00 99.51 C ANISOU 5238 CA MET B 257 9210 15018 13580 2862 3039 3616 C ATOM 5239 C MET B 257 91.855 -84.732 36.876 1.00 98.64 C ANISOU 5239 C MET B 257 9249 14901 13328 2700 2674 3243 C ATOM 5240 O MET B 257 92.955 -85.231 36.636 1.00 96.51 O ANISOU 5240 O MET B 257 9092 14688 12889 2662 2525 3193 O ATOM 5241 CB MET B 257 89.925 -86.358 36.903 1.00102.23 C ANISOU 5241 CB MET B 257 9348 15003 14493 2664 3048 3833 C ATOM 5242 CG MET B 257 89.102 -87.329 37.728 1.00109.72 C ANISOU 5242 CG MET B 257 10137 15923 15629 2800 3421 4245 C ATOM 5243 SD MET B 257 87.607 -87.912 36.894 1.00115.61 S ANISOU 5243 SD MET B 257 10561 16250 17115 2578 3470 4437 S ATOM 5244 CE MET B 257 88.292 -89.165 35.879 1.00110.70 C ANISOU 5244 CE MET B 257 9958 15374 16729 2362 3242 4462 C ATOM 5245 N ALA B 258 91.481 -83.528 36.412 1.00 93.76 N ANISOU 5245 N ALA B 258 8624 14209 12789 2616 2550 2997 N ATOM 5246 CA ALA B 258 92.342 -82.661 35.612 1.00 90.89 C ANISOU 5246 CA ALA B 258 8392 13825 12318 2471 2245 2661 C ATOM 5247 C ALA B 258 93.429 -82.031 36.488 1.00 96.08 C ANISOU 5247 C ALA B 258 9218 14799 12489 2626 2230 2435 C ATOM 5248 O ALA B 258 94.568 -81.874 36.043 1.00 94.28 O ANISOU 5248 O ALA B 258 9105 14616 12101 2533 2011 2238 O ATOM 5249 CB ALA B 258 91.515 -81.577 34.943 1.00 90.96 C ANISOU 5249 CB ALA B 258 8331 13647 12581 2366 2159 2515 C ATOM 5250 N ALA B 259 93.077 -81.685 37.740 1.00 95.44 N ANISOU 5250 N ALA B 259 9141 14947 12173 2871 2464 2456 N ATOM 5251 CA ALA B 259 93.985 -81.060 38.698 1.00 96.34 C ANISOU 5251 CA ALA B 259 9398 15393 11815 3052 2454 2214 C ATOM 5252 C ALA B 259 95.041 -82.033 39.208 1.00100.79 C ANISOU 5252 C ALA B 259 10042 16191 12062 3164 2447 2320 C ATOM 5253 O ALA B 259 96.160 -81.612 39.484 1.00100.03 O ANISOU 5253 O ALA B 259 10059 16309 11637 3205 2292 2059 O ATOM 5254 CB ALA B 259 93.195 -80.504 39.869 1.00100.19 C ANISOU 5254 CB ALA B 259 9861 16066 12140 3307 2719 2219 C ATOM 5255 N ALA B 260 94.681 -83.324 39.343 1.00 98.63 N ANISOU 5255 N ALA B 260 9696 15870 11910 3216 2618 2703 N ATOM 5256 CA ALA B 260 95.532 -84.396 39.863 1.00 99.24 C ANISOU 5256 CA ALA B 260 9834 16142 11731 3355 2660 2887 C ATOM 5257 C ALA B 260 96.766 -84.639 39.011 1.00101.18 C ANISOU 5257 C ALA B 260 10155 16338 11949 3181 2363 2725 C ATOM 5258 O ALA B 260 97.860 -84.704 39.568 1.00101.30 O ANISOU 5258 O ALA B 260 10267 16638 11583 3315 2287 2621 O ATOM 5259 CB ALA B 260 94.736 -85.684 39.987 1.00101.36 C ANISOU 5259 CB ALA B 260 9985 16261 12266 3400 2914 3345 C ATOM 5260 N VAL B 261 96.604 -84.747 37.674 1.00 95.78 N ANISOU 5260 N VAL B 261 9422 15318 11652 2899 2191 2693 N ATOM 5261 CA VAL B 261 97.702 -85.032 36.737 1.00 93.38 C ANISOU 5261 CA VAL B 261 9180 14940 11358 2727 1930 2561 C ATOM 5262 C VAL B 261 98.773 -83.917 36.721 1.00 95.41 C ANISOU 5262 C VAL B 261 9540 15379 11332 2695 1717 2169 C ATOM 5263 O VAL B 261 99.949 -84.236 36.556 1.00 94.43 O ANISOU 5263 O VAL B 261 9476 15367 11037 2680 1570 2083 O ATOM 5264 CB VAL B 261 97.218 -85.370 35.301 1.00 95.59 C ANISOU 5264 CB VAL B 261 9390 14841 12090 2456 1800 2604 C ATOM 5265 CG1 VAL B 261 96.443 -86.682 35.284 1.00 96.59 C ANISOU 5265 CG1 VAL B 261 9405 14782 12512 2469 1974 2964 C ATOM 5266 CG2 VAL B 261 96.385 -84.243 34.691 1.00 94.67 C ANISOU 5266 CG2 VAL B 261 9226 14551 12194 2317 1731 2438 C ATOM 5267 N VAL B 262 98.382 -82.640 36.916 1.00 91.67 N ANISOU 5267 N VAL B 262 9074 14925 10831 2691 1709 1936 N ATOM 5268 CA VAL B 262 99.331 -81.524 36.907 1.00 90.69 C ANISOU 5268 CA VAL B 262 9027 14927 10504 2642 1521 1551 C ATOM 5269 C VAL B 262 100.011 -81.399 38.288 1.00 96.98 C ANISOU 5269 C VAL B 262 9880 16130 10837 2906 1575 1434 C ATOM 5270 O VAL B 262 101.211 -81.131 38.338 1.00 96.40 O ANISOU 5270 O VAL B 262 9853 16225 10549 2890 1396 1195 O ATOM 5271 CB VAL B 262 98.710 -80.184 36.400 1.00 93.87 C ANISOU 5271 CB VAL B 262 9417 15130 11120 2507 1468 1331 C ATOM 5272 CG1 VAL B 262 97.694 -79.597 37.371 1.00 96.00 C ANISOU 5272 CG1 VAL B 262 9658 15483 11337 2693 1678 1329 C ATOM 5273 CG2 VAL B 262 99.783 -79.158 36.051 1.00 92.88 C ANISOU 5273 CG2 VAL B 262 9354 15031 10904 2383 1253 962 C ATOM 5274 N LEU B 263 99.269 -81.632 39.387 1.00 96.28 N ANISOU 5274 N LEU B 263 9777 16214 10590 3156 1818 1607 N ATOM 5275 CA LEU B 263 99.810 -81.543 40.744 1.00 98.96 C ANISOU 5275 CA LEU B 263 10177 16977 10447 3451 1880 1512 C ATOM 5276 C LEU B 263 100.763 -82.705 41.044 1.00103.60 C ANISOU 5276 C LEU B 263 10792 17776 10797 3574 1850 1697 C ATOM 5277 O LEU B 263 101.779 -82.476 41.693 1.00104.96 O ANISOU 5277 O LEU B 263 11014 18275 10591 3713 1728 1480 O ATOM 5278 CB LEU B 263 98.688 -81.477 41.789 1.00101.82 C ANISOU 5278 CB LEU B 263 10519 17468 10698 3704 2179 1677 C ATOM 5279 CG LEU B 263 98.389 -80.088 42.389 1.00108.06 C ANISOU 5279 CG LEU B 263 11342 18375 11342 3792 2189 1317 C ATOM 5280 CD1 LEU B 263 97.636 -79.185 41.405 1.00105.93 C ANISOU 5280 CD1 LEU B 263 11019 17718 11510 3538 2135 1186 C ATOM 5281 CD2 LEU B 263 97.579 -80.214 43.661 1.00114.11 C ANISOU 5281 CD2 LEU B 263 12110 19399 11848 4127 2495 1486 C ATOM 5282 N ALA B 264 100.470 -83.928 40.538 1.00 98.47 N ANISOU 5282 N ALA B 264 10098 16927 10388 3520 1942 2074 N ATOM 5283 CA ALA B 264 101.319 -85.115 40.729 1.00 98.16 C ANISOU 5283 CA ALA B 264 10080 17028 10187 3636 1930 2288 C ATOM 5284 C ALA B 264 102.659 -84.979 39.988 1.00 99.47 C ANISOU 5284 C ALA B 264 10272 17204 10318 3469 1628 2024 C ATOM 5285 O ALA B 264 103.665 -85.509 40.459 1.00100.66 O ANISOU 5285 O ALA B 264 10450 17618 10177 3625 1562 2042 O ATOM 5286 CB ALA B 264 100.595 -86.371 40.264 1.00 98.37 C ANISOU 5286 CB ALA B 264 10044 16766 10567 3583 2103 2719 C ATOM 5287 N PHE B 265 102.673 -84.269 38.840 1.00 91.59 N ANISOU 5287 N PHE B 265 9258 15930 9613 3168 1455 1797 N ATOM 5288 CA PHE B 265 103.891 -84.053 38.070 1.00 88.67 C ANISOU 5288 CA PHE B 265 8900 15549 9242 2996 1197 1554 C ATOM 5289 C PHE B 265 104.857 -83.134 38.828 1.00 93.94 C ANISOU 5289 C PHE B 265 9588 16555 9548 3095 1055 1185 C ATOM 5290 O PHE B 265 106.047 -83.445 38.883 1.00 93.87 O ANISOU 5290 O PHE B 265 9574 16737 9356 3131 909 1096 O ATOM 5291 CB PHE B 265 103.575 -83.480 36.677 1.00 87.28 C ANISOU 5291 CB PHE B 265 8706 15001 9454 2675 1080 1436 C ATOM 5292 CG PHE B 265 104.765 -83.333 35.752 1.00 86.57 C ANISOU 5292 CG PHE B 265 8623 14869 9402 2489 853 1238 C ATOM 5293 CD1 PHE B 265 105.202 -84.402 34.975 1.00 87.75 C ANISOU 5293 CD1 PHE B 265 8767 14900 9674 2419 806 1412 C ATOM 5294 CD2 PHE B 265 105.431 -82.117 35.635 1.00 88.04 C ANISOU 5294 CD2 PHE B 265 8811 15114 9528 2381 700 876 C ATOM 5295 CE1 PHE B 265 106.295 -84.262 34.116 1.00 86.91 C ANISOU 5295 CE1 PHE B 265 8660 14766 9594 2262 620 1238 C ATOM 5296 CE2 PHE B 265 106.530 -81.983 34.783 1.00 89.32 C ANISOU 5296 CE2 PHE B 265 8960 15235 9743 2209 521 719 C ATOM 5297 CZ PHE B 265 106.954 -83.055 34.028 1.00 85.92 C ANISOU 5297 CZ PHE B 265 8527 14715 9403 2157 486 905 C ATOM 5298 N ILE B 266 104.361 -82.015 39.408 1.00 91.34 N ANISOU 5298 N ILE B 266 9271 16300 9135 3142 1090 955 N ATOM 5299 CA ILE B 266 105.234 -81.069 40.118 1.00 92.58 C ANISOU 5299 CA ILE B 266 9435 16754 8985 3221 939 548 C ATOM 5300 C ILE B 266 105.665 -81.626 41.493 1.00 99.94 C ANISOU 5300 C ILE B 266 10391 18149 9433 3580 992 609 C ATOM 5301 O ILE B 266 106.755 -81.286 41.945 1.00101.14 O ANISOU 5301 O ILE B 266 10528 18590 9312 3649 806 317 O ATOM 5302 CB ILE B 266 104.695 -79.614 40.228 1.00 95.90 C ANISOU 5302 CB ILE B 266 9863 17080 9494 3143 930 218 C ATOM 5303 CG1 ILE B 266 103.376 -79.520 41.009 1.00 98.15 C ANISOU 5303 CG1 ILE B 266 10172 17395 9726 3340 1182 370 C ATOM 5304 CG2 ILE B 266 104.582 -78.970 38.853 1.00 93.71 C ANISOU 5304 CG2 ILE B 266 9564 16393 9648 2801 830 122 C ATOM 5305 CD1 ILE B 266 103.133 -78.149 41.706 1.00109.84 C ANISOU 5305 CD1 ILE B 266 11674 18976 11086 3413 1175 -24 C ATOM 5306 N ILE B 267 104.863 -82.492 42.136 1.00 97.95 N ANISOU 5306 N ILE B 267 10164 17974 9077 3811 1240 992 N ATOM 5307 CA ILE B 267 105.267 -83.069 43.424 1.00101.14 C ANISOU 5307 CA ILE B 267 10601 18831 8996 4184 1309 1102 C ATOM 5308 C ILE B 267 106.437 -84.058 43.194 1.00105.75 C ANISOU 5308 C ILE B 267 11164 19528 9486 4214 1173 1227 C ATOM 5309 O ILE B 267 107.401 -84.051 43.961 1.00107.86 O ANISOU 5309 O ILE B 267 11432 20197 9355 4421 1039 1067 O ATOM 5310 CB ILE B 267 104.060 -83.716 44.175 1.00105.97 C ANISOU 5310 CB ILE B 267 11240 19481 9541 4432 1654 1521 C ATOM 5311 CG1 ILE B 267 103.037 -82.655 44.656 1.00107.84 C ANISOU 5311 CG1 ILE B 267 11493 19715 9766 4479 1787 1346 C ATOM 5312 CG2 ILE B 267 104.486 -84.634 45.333 1.00109.72 C ANISOU 5312 CG2 ILE B 267 11755 20382 9551 4827 1762 1779 C ATOM 5313 CD1 ILE B 267 103.591 -81.394 45.450 1.00119.28 C ANISOU 5313 CD1 ILE B 267 12977 21497 10846 4597 1619 815 C ATOM 5314 N CYS B 268 106.372 -84.843 42.107 1.00 99.96 N ANISOU 5314 N CYS B 268 10406 18446 9127 4006 1186 1474 N ATOM 5315 CA CYS B 268 107.355 -85.864 41.758 1.00 99.70 C ANISOU 5315 CA CYS B 268 10354 18450 9078 4023 1091 1628 C ATOM 5316 C CYS B 268 108.644 -85.311 41.122 1.00103.00 C ANISOU 5316 C CYS B 268 10722 18908 9507 3832 787 1250 C ATOM 5317 O CYS B 268 109.721 -85.835 41.415 1.00104.34 O ANISOU 5317 O CYS B 268 10863 19336 9447 3972 670 1247 O ATOM 5318 CB CYS B 268 106.717 -86.907 40.848 1.00 98.17 C ANISOU 5318 CB CYS B 268 10153 17852 9296 3881 1232 2009 C ATOM 5319 SG CYS B 268 105.467 -87.934 41.663 1.00104.46 S ANISOU 5319 SG CYS B 268 10970 18620 10099 4140 1608 2541 S ATOM 5320 N TRP B 269 108.552 -84.301 40.241 1.00 97.35 N ANISOU 5320 N TRP B 269 9984 17934 9072 3522 673 962 N ATOM 5321 CA TRP B 269 109.726 -83.817 39.519 1.00 96.08 C ANISOU 5321 CA TRP B 269 9761 17758 8987 3314 426 652 C ATOM 5322 C TRP B 269 110.300 -82.448 39.960 1.00 99.69 C ANISOU 5322 C TRP B 269 10174 18408 9297 3270 249 163 C ATOM 5323 O TRP B 269 111.476 -82.215 39.678 1.00 99.70 O ANISOU 5323 O TRP B 269 10095 18507 9279 3175 49 -75 O ATOM 5324 CB TRP B 269 109.428 -83.775 38.016 1.00 92.17 C ANISOU 5324 CB TRP B 269 9264 16812 8944 2981 413 704 C ATOM 5325 CG TRP B 269 109.438 -85.135 37.382 1.00 92.45 C ANISOU 5325 CG TRP B 269 9311 16685 9133 2981 481 1057 C ATOM 5326 CD1 TRP B 269 108.355 -85.871 36.998 1.00 94.62 C ANISOU 5326 CD1 TRP B 269 9621 16681 9649 2957 656 1384 C ATOM 5327 CD2 TRP B 269 110.592 -85.942 37.106 1.00 92.39 C ANISOU 5327 CD2 TRP B 269 9264 16780 9058 3019 377 1105 C ATOM 5328 NE1 TRP B 269 108.764 -87.072 36.460 1.00 93.49 N ANISOU 5328 NE1 TRP B 269 9475 16438 9611 2964 661 1612 N ATOM 5329 CE2 TRP B 269 110.132 -87.148 36.529 1.00 95.38 C ANISOU 5329 CE2 TRP B 269 9675 16912 9653 3015 499 1457 C ATOM 5330 CE3 TRP B 269 111.978 -85.762 37.293 1.00 94.56 C ANISOU 5330 CE3 TRP B 269 9467 17331 9131 3059 188 872 C ATOM 5331 CZ2 TRP B 269 111.006 -88.168 36.136 1.00 94.45 C ANISOU 5331 CZ2 TRP B 269 9536 16805 9545 3060 450 1582 C ATOM 5332 CZ3 TRP B 269 112.841 -86.772 36.906 1.00 95.63 C ANISOU 5332 CZ3 TRP B 269 9568 17496 9271 3107 141 1014 C ATOM 5333 CH2 TRP B 269 112.356 -87.954 36.328 1.00 95.15 C ANISOU 5333 CH2 TRP B 269 9558 17176 9418 3112 275 1364 C ATOM 5334 N LEU B 270 109.528 -81.556 40.619 1.00 96.14 N ANISOU 5334 N LEU B 270 9761 18001 8768 3333 321 -1 N ATOM 5335 CA LEU B 270 110.059 -80.245 41.035 1.00 97.14 C ANISOU 5335 CA LEU B 270 9842 18274 8791 3285 150 -500 C ATOM 5336 C LEU B 270 111.220 -80.386 42.054 1.00103.85 C ANISOU 5336 C LEU B 270 10631 19619 9207 3525 -24 -712 C ATOM 5337 O LEU B 270 112.238 -79.739 41.813 1.00103.12 O ANISOU 5337 O LEU B 270 10439 19574 9167 3373 -244 -1072 O ATOM 5338 CB LEU B 270 108.972 -79.285 41.575 1.00 98.18 C ANISOU 5338 CB LEU B 270 10031 18351 8923 3332 271 -647 C ATOM 5339 CG LEU B 270 109.408 -77.872 42.007 1.00104.36 C ANISOU 5339 CG LEU B 270 10772 19231 9649 3277 108 -1193 C ATOM 5340 CD1 LEU B 270 109.537 -76.936 40.821 1.00101.99 C ANISOU 5340 CD1 LEU B 270 10427 18517 9806 2901 23 -1391 C ATOM 5341 CD2 LEU B 270 108.443 -77.286 43.014 1.00109.36 C ANISOU 5341 CD2 LEU B 270 11475 19989 10088 3491 248 -1299 C ATOM 5342 N PRO B 271 111.156 -81.219 43.132 1.00103.83 N ANISOU 5342 N PRO B 271 10672 19985 8793 3892 61 -494 N ATOM 5343 CA PRO B 271 112.304 -81.306 44.060 1.00107.30 C ANISOU 5343 CA PRO B 271 11044 20921 8804 4132 -140 -716 C ATOM 5344 C PRO B 271 113.657 -81.600 43.381 1.00111.14 C ANISOU 5344 C PRO B 271 11404 21423 9403 3980 -363 -813 C ATOM 5345 O PRO B 271 114.641 -80.927 43.702 1.00112.51 O ANISOU 5345 O PRO B 271 11462 21835 9452 3963 -606 -1237 O ATOM 5346 CB PRO B 271 111.896 -82.435 45.008 1.00111.11 C ANISOU 5346 CB PRO B 271 11610 21696 8911 4532 46 -294 C ATOM 5347 CG PRO B 271 110.418 -82.366 45.030 1.00114.66 C ANISOU 5347 CG PRO B 271 12163 21899 9504 4535 332 -55 C ATOM 5348 CD PRO B 271 110.042 -82.066 43.609 1.00106.07 C ANISOU 5348 CD PRO B 271 11056 20270 8977 4121 345 -41 C ATOM 5349 N PHE B 272 113.696 -82.545 42.413 1.00105.66 N ANISOU 5349 N PHE B 272 10715 20459 8971 3857 -282 -453 N ATOM 5350 CA PHE B 272 114.913 -82.897 41.671 1.00104.67 C ANISOU 5350 CA PHE B 272 10474 20319 8978 3717 -453 -506 C ATOM 5351 C PHE B 272 115.384 -81.756 40.748 1.00107.47 C ANISOU 5351 C PHE B 272 10733 20420 9681 3337 -600 -887 C ATOM 5352 O PHE B 272 116.586 -81.481 40.696 1.00108.52 O ANISOU 5352 O PHE B 272 10719 20724 9792 3275 -810 -1164 O ATOM 5353 CB PHE B 272 114.704 -84.193 40.854 1.00103.97 C ANISOU 5353 CB PHE B 272 10435 19975 9093 3692 -303 -32 C ATOM 5354 CG PHE B 272 115.751 -84.452 39.794 1.00103.73 C ANISOU 5354 CG PHE B 272 10302 19813 9296 3485 -435 -81 C ATOM 5355 CD1 PHE B 272 117.014 -84.923 40.140 1.00108.56 C ANISOU 5355 CD1 PHE B 272 10796 20758 9693 3643 -600 -145 C ATOM 5356 CD2 PHE B 272 115.484 -84.195 38.455 1.00102.84 C ANISOU 5356 CD2 PHE B 272 10204 19266 9605 3148 -395 -68 C ATOM 5357 CE1 PHE B 272 117.993 -85.134 39.161 1.00108.04 C ANISOU 5357 CE1 PHE B 272 10621 20579 9851 3458 -704 -196 C ATOM 5358 CE2 PHE B 272 116.466 -84.396 37.479 1.00104.41 C ANISOU 5358 CE2 PHE B 272 10309 19366 9996 2973 -498 -118 C ATOM 5359 CZ PHE B 272 117.711 -84.873 37.838 1.00104.10 C ANISOU 5359 CZ PHE B 272 10147 19648 9759 3126 -642 -180 C ATOM 5360 N HIS B 273 114.454 -81.130 40.001 1.00101.59 N ANISOU 5360 N HIS B 273 10060 19268 9273 3090 -481 -877 N ATOM 5361 CA HIS B 273 114.783 -80.064 39.054 1.00 99.97 C ANISOU 5361 CA HIS B 273 9782 18774 9427 2737 -574 -1167 C ATOM 5362 C HIS B 273 115.234 -78.785 39.771 1.00106.29 C ANISOU 5362 C HIS B 273 10493 19754 10138 2714 -738 -1679 C ATOM 5363 O HIS B 273 116.025 -78.039 39.198 1.00105.30 O ANISOU 5363 O HIS B 273 10245 19515 10250 2466 -872 -1964 O ATOM 5364 CB HIS B 273 113.618 -79.797 38.098 1.00 97.86 C ANISOU 5364 CB HIS B 273 9622 18045 9516 2524 -403 -982 C ATOM 5365 CG HIS B 273 113.511 -80.839 37.025 1.00 98.46 C ANISOU 5365 CG HIS B 273 9737 17884 9789 2436 -316 -609 C ATOM 5366 ND1 HIS B 273 114.242 -80.747 35.855 1.00 98.45 N ANISOU 5366 ND1 HIS B 273 9672 17690 10045 2190 -391 -653 N ATOM 5367 CD2 HIS B 273 112.800 -81.989 37.003 1.00 99.31 C ANISOU 5367 CD2 HIS B 273 9932 17932 9867 2575 -163 -209 C ATOM 5368 CE1 HIS B 273 113.935 -81.826 35.152 1.00 95.83 C ANISOU 5368 CE1 HIS B 273 9402 17196 9812 2195 -295 -305 C ATOM 5369 NE2 HIS B 273 113.069 -82.602 35.801 1.00 96.58 N ANISOU 5369 NE2 HIS B 273 9584 17348 9764 2411 -161 -36 N ATOM 5370 N VAL B 274 114.787 -78.564 41.032 1.00106.10 N ANISOU 5370 N VAL B 274 10520 20020 9772 2980 -728 -1802 N ATOM 5371 CA VAL B 274 115.197 -77.422 41.867 1.00109.53 C ANISOU 5371 CA VAL B 274 10875 20673 10070 3009 -900 -2327 C ATOM 5372 C VAL B 274 116.668 -77.628 42.240 1.00116.02 C ANISOU 5372 C VAL B 274 11518 21865 10697 3081 -1156 -2565 C ATOM 5373 O VAL B 274 117.473 -76.713 42.074 1.00116.74 O ANISOU 5373 O VAL B 274 11457 21929 10970 2877 -1340 -2988 O ATOM 5374 CB VAL B 274 114.280 -77.230 43.114 1.00116.11 C ANISOU 5374 CB VAL B 274 11825 21747 10545 3316 -803 -2374 C ATOM 5375 CG1 VAL B 274 114.957 -76.425 44.222 1.00120.16 C ANISOU 5375 CG1 VAL B 274 12246 22651 10757 3461 -1029 -2914 C ATOM 5376 CG2 VAL B 274 112.963 -76.577 42.722 1.00114.44 C ANISOU 5376 CG2 VAL B 274 11730 21140 10611 3180 -599 -2307 C ATOM 5377 N LEU B 275 117.010 -78.851 42.689 1.00113.70 N ANISOU 5377 N LEU B 275 11234 21892 10074 3363 -1158 -2271 N ATOM 5378 CA LEU B 275 118.352 -79.288 43.075 1.00115.96 C ANISOU 5378 CA LEU B 275 11353 22570 10134 3496 -1387 -2405 C ATOM 5379 C LEU B 275 119.341 -79.208 41.903 1.00118.56 C ANISOU 5379 C LEU B 275 11520 22670 10858 3172 -1487 -2473 C ATOM 5380 O LEU B 275 120.503 -78.848 42.107 1.00120.54 O ANISOU 5380 O LEU B 275 11566 23150 11085 3135 -1725 -2822 O ATOM 5381 CB LEU B 275 118.272 -80.733 43.597 1.00116.43 C ANISOU 5381 CB LEU B 275 11497 22909 9833 3861 -1291 -1943 C ATOM 5382 CG LEU B 275 118.305 -80.950 45.111 1.00125.42 C ANISOU 5382 CG LEU B 275 12663 24600 10390 4302 -1361 -2010 C ATOM 5383 CD1 LEU B 275 117.248 -80.119 45.833 1.00127.24 C ANISOU 5383 CD1 LEU B 275 13021 24845 10479 4385 -1261 -2187 C ATOM 5384 CD2 LEU B 275 118.095 -82.409 45.437 1.00127.48 C ANISOU 5384 CD2 LEU B 275 13024 25026 10386 4630 -1200 -1456 C ATOM 5385 N THR B 276 118.865 -79.528 40.681 1.00111.63 N ANISOU 5385 N THR B 276 10724 21350 10339 2944 -1304 -2150 N ATOM 5386 CA THR B 276 119.628 -79.502 39.434 1.00109.85 C ANISOU 5386 CA THR B 276 10381 20865 10491 2643 -1337 -2143 C ATOM 5387 C THR B 276 119.923 -78.038 39.026 1.00116.12 C ANISOU 5387 C THR B 276 11059 21439 11623 2314 -1426 -2576 C ATOM 5388 O THR B 276 121.023 -77.762 38.542 1.00116.44 O ANISOU 5388 O THR B 276 10905 21479 11859 2133 -1553 -2769 O ATOM 5389 CB THR B 276 118.863 -80.301 38.360 1.00115.10 C ANISOU 5389 CB THR B 276 11201 21157 11374 2551 -1110 -1672 C ATOM 5390 OG1 THR B 276 118.861 -81.678 38.745 1.00115.08 O ANISOU 5390 OG1 THR B 276 11258 21363 11105 2844 -1052 -1312 O ATOM 5391 CG2 THR B 276 119.468 -80.170 36.960 1.00111.85 C ANISOU 5391 CG2 THR B 276 10706 20440 11353 2236 -1106 -1656 C ATOM 5392 N PHE B 277 118.964 -77.108 39.231 1.00114.16 N ANISOU 5392 N PHE B 277 10917 20996 11463 2242 -1348 -2722 N ATOM 5393 CA PHE B 277 119.176 -75.690 38.903 1.00115.36 C ANISOU 5393 CA PHE B 277 10968 20904 11961 1945 -1414 -3125 C ATOM 5394 C PHE B 277 120.146 -75.046 39.890 1.00124.81 C ANISOU 5394 C PHE B 277 11964 22452 13004 2008 -1674 -3647 C ATOM 5395 O PHE B 277 120.949 -74.213 39.476 1.00125.25 O ANISOU 5395 O PHE B 277 11833 22374 13381 1743 -1784 -3966 O ATOM 5396 CB PHE B 277 117.862 -74.897 38.853 1.00116.21 C ANISOU 5396 CB PHE B 277 11243 20693 12217 1874 -1254 -3129 C ATOM 5397 CG PHE B 277 118.031 -73.484 38.360 1.00118.42 C ANISOU 5397 CG PHE B 277 11434 20643 12917 1558 -1284 -3476 C ATOM 5398 CD1 PHE B 277 118.261 -73.224 37.016 1.00119.44 C ANISOU 5398 CD1 PHE B 277 11527 20387 13470 1250 -1201 -3338 C ATOM 5399 CD2 PHE B 277 117.979 -72.413 39.243 1.00123.69 C ANISOU 5399 CD2 PHE B 277 12055 21383 13557 1579 -1388 -3944 C ATOM 5400 CE1 PHE B 277 118.436 -71.918 36.561 1.00121.55 C ANISOU 5400 CE1 PHE B 277 11708 20330 14146 965 -1205 -3623 C ATOM 5401 CE2 PHE B 277 118.149 -71.105 38.788 1.00127.71 C ANISOU 5401 CE2 PHE B 277 12475 21546 14502 1281 -1404 -4262 C ATOM 5402 CZ PHE B 277 118.376 -70.866 37.450 1.00123.81 C ANISOU 5402 CZ PHE B 277 11942 20655 14444 975 -1303 -4081 C ATOM 5403 N LEU B 278 120.077 -75.438 41.183 1.00125.35 N ANISOU 5403 N LEU B 278 12065 22974 12588 2362 -1771 -3732 N ATOM 5404 CA LEU B 278 120.969 -74.961 42.244 1.00130.31 C ANISOU 5404 CA LEU B 278 12509 24022 12980 2489 -2052 -4235 C ATOM 5405 C LEU B 278 122.396 -75.431 41.982 1.00137.06 C ANISOU 5405 C LEU B 278 13119 25088 13871 2445 -2241 -4292 C ATOM 5406 O LEU B 278 123.344 -74.686 42.236 1.00139.37 O ANISOU 5406 O LEU B 278 13173 25505 14278 2326 -2472 -4768 O ATOM 5407 CB LEU B 278 120.499 -75.444 43.624 1.00132.81 C ANISOU 5407 CB LEU B 278 12948 24807 12708 2931 -2082 -4219 C ATOM 5408 CG LEU B 278 119.268 -74.764 44.213 1.00138.16 C ANISOU 5408 CG LEU B 278 13812 25396 13288 3022 -1952 -4326 C ATOM 5409 CD1 LEU B 278 118.750 -75.539 45.402 1.00140.34 C ANISOU 5409 CD1 LEU B 278 14232 26124 12968 3485 -1905 -4139 C ATOM 5410 CD2 LEU B 278 119.563 -73.326 44.613 1.00143.84 C ANISOU 5410 CD2 LEU B 278 14407 26080 14164 2869 -2134 -4977 C ATOM 5411 N ASP B 279 122.536 -76.666 41.452 1.00133.14 N ANISOU 5411 N ASP B 279 12670 24612 13307 2536 -2137 -3815 N ATOM 5412 CA ASP B 279 123.810 -77.282 41.079 1.00134.28 C ANISOU 5412 CA ASP B 279 12600 24927 13495 2517 -2268 -3777 C ATOM 5413 C ASP B 279 124.416 -76.568 39.866 1.00138.21 C ANISOU 5413 C ASP B 279 12933 25035 14547 2088 -2249 -3908 C ATOM 5414 O ASP B 279 125.633 -76.402 39.810 1.00140.02 O ANISOU 5414 O ASP B 279 12887 25422 14891 1997 -2433 -4161 O ATOM 5415 CB ASP B 279 123.621 -78.786 40.791 1.00133.92 C ANISOU 5415 CB ASP B 279 12686 24936 13260 2734 -2118 -3210 C ATOM 5416 CG ASP B 279 124.828 -79.470 40.179 1.00145.91 C ANISOU 5416 CG ASP B 279 14009 26541 14890 2693 -2197 -3109 C ATOM 5417 OD1 ASP B 279 125.848 -79.621 40.886 1.00149.76 O ANISOU 5417 OD1 ASP B 279 14287 27456 15158 2865 -2435 -3334 O ATOM 5418 OD2 ASP B 279 124.755 -79.843 38.993 1.00149.73 O ANISOU 5418 OD2 ASP B 279 14541 26677 15673 2501 -2027 -2818 O ATOM 5419 N ALA B 280 123.570 -76.149 38.902 1.00132.68 N ANISOU 5419 N ALA B 280 12387 23837 14187 1838 -2022 -3724 N ATOM 5420 CA ALA B 280 123.994 -75.434 37.696 1.00131.82 C ANISOU 5420 CA ALA B 280 12161 23326 14597 1446 -1954 -3787 C ATOM 5421 C ALA B 280 124.636 -74.087 38.051 1.00139.58 C ANISOU 5421 C ALA B 280 12915 24293 15827 1238 -2129 -4352 C ATOM 5422 O ALA B 280 125.648 -73.716 37.451 1.00139.94 O ANISOU 5422 O ALA B 280 12718 24248 16204 998 -2185 -4503 O ATOM 5423 CB ALA B 280 122.809 -75.218 36.769 1.00129.10 C ANISOU 5423 CB ALA B 280 12057 22503 14493 1285 -1693 -3484 C ATOM 5424 N LEU B 281 124.064 -73.382 39.054 1.00139.08 N ANISOU 5424 N LEU B 281 12915 24324 15606 1342 -2213 -4674 N ATOM 5425 CA LEU B 281 124.546 -72.091 39.557 1.00143.11 C ANISOU 5425 CA LEU B 281 13226 24822 16328 1177 -2395 -5267 C ATOM 5426 C LEU B 281 125.888 -72.248 40.277 1.00151.12 C ANISOU 5426 C LEU B 281 13933 26302 17185 1275 -2704 -5629 C ATOM 5427 O LEU B 281 126.684 -71.310 40.276 1.00153.50 O ANISOU 5427 O LEU B 281 13970 26532 17821 1037 -2855 -6078 O ATOM 5428 CB LEU B 281 123.516 -71.441 40.493 1.00144.71 C ANISOU 5428 CB LEU B 281 13604 25041 16336 1323 -2397 -5503 C ATOM 5429 CG LEU B 281 122.138 -71.155 39.901 1.00146.20 C ANISOU 5429 CG LEU B 281 14072 24785 16694 1240 -2112 -5203 C ATOM 5430 CD1 LEU B 281 121.106 -71.022 40.988 1.00147.70 C ANISOU 5430 CD1 LEU B 281 14456 25146 16516 1521 -2098 -5305 C ATOM 5431 CD2 LEU B 281 122.148 -69.929 38.993 1.00148.62 C ANISOU 5431 CD2 LEU B 281 14307 24557 17605 842 -2017 -5362 C ATOM 5432 N ALA B 282 126.139 -73.434 40.880 1.00148.29 N ANISOU 5432 N ALA B 282 13597 26410 16338 1627 -2797 -5426 N ATOM 5433 CA ALA B 282 127.395 -73.760 41.559 1.00152.07 C ANISOU 5433 CA ALA B 282 13789 27383 16609 1779 -3098 -5701 C ATOM 5434 C ALA B 282 128.535 -73.819 40.543 1.00156.99 C ANISOU 5434 C ALA B 282 14135 27858 17654 1501 -3103 -5663 C ATOM 5435 O ALA B 282 129.585 -73.226 40.789 1.00160.25 O ANISOU 5435 O ALA B 282 14218 28414 18257 1370 -3336 -6111 O ATOM 5436 CB ALA B 282 127.272 -75.080 42.312 1.00152.64 C ANISOU 5436 CB ALA B 282 13989 27929 16078 2237 -3137 -5383 C ATOM 5437 N TRP B 283 128.299 -74.450 39.366 1.00150.77 N ANISOU 5437 N TRP B 283 13474 26760 17051 1390 -2839 -5153 N ATOM 5438 CA TRP B 283 129.290 -74.543 38.287 1.00150.75 C ANISOU 5438 CA TRP B 283 13244 26593 17442 1137 -2786 -5058 C ATOM 5439 C TRP B 283 129.489 -73.182 37.608 1.00157.85 C ANISOU 5439 C TRP B 283 13992 27054 18930 704 -2723 -5342 C ATOM 5440 O TRP B 283 130.566 -72.929 37.065 1.00158.80 O ANISOU 5440 O TRP B 283 13811 27127 19400 483 -2762 -5466 O ATOM 5441 CB TRP B 283 128.917 -75.614 37.247 1.00144.83 C ANISOU 5441 CB TRP B 283 12698 25650 16681 1174 -2521 -4454 C ATOM 5442 CG TRP B 283 128.808 -77.009 37.795 1.00145.02 C ANISOU 5442 CG TRP B 283 12847 26044 16208 1577 -2553 -4136 C ATOM 5443 CD1 TRP B 283 127.672 -77.749 37.919 1.00145.20 C ANISOU 5443 CD1 TRP B 283 13199 26020 15949 1793 -2391 -3754 C ATOM 5444 CD2 TRP B 283 129.877 -77.832 38.286 1.00147.15 C ANISOU 5444 CD2 TRP B 283 12904 26771 16236 1816 -2747 -4157 C ATOM 5445 NE1 TRP B 283 127.960 -78.977 38.467 1.00145.14 N ANISOU 5445 NE1 TRP B 283 13206 26391 15548 2148 -2457 -3525 N ATOM 5446 CE2 TRP B 283 129.307 -79.057 38.700 1.00149.45 C ANISOU 5446 CE2 TRP B 283 13430 27259 16097 2182 -2679 -3760 C ATOM 5447 CE3 TRP B 283 131.266 -77.655 38.414 1.00151.75 C ANISOU 5447 CE3 TRP B 283 13102 27611 16944 1760 -2969 -4467 C ATOM 5448 CZ2 TRP B 283 130.074 -80.099 39.232 1.00150.49 C ANISOU 5448 CZ2 TRP B 283 13443 27826 15909 2506 -2820 -3647 C ATOM 5449 CZ3 TRP B 283 132.024 -78.687 38.946 1.00154.96 C ANISOU 5449 CZ3 TRP B 283 13382 28476 17021 2085 -3127 -4372 C ATOM 5450 CH2 TRP B 283 131.429 -79.892 39.346 1.00153.96 C ANISOU 5450 CH2 TRP B 283 13513 28529 16456 2460 -3050 -3958 C ATOM 5451 N MET B 284 128.458 -72.310 37.644 1.00155.39 N ANISOU 5451 N MET B 284 13880 26418 18745 591 -2613 -5431 N ATOM 5452 CA MET B 284 128.528 -70.952 37.092 1.00156.94 C ANISOU 5452 CA MET B 284 13959 26165 19504 203 -2540 -5696 C ATOM 5453 C MET B 284 129.378 -70.033 37.983 1.00166.37 C ANISOU 5453 C MET B 284 14827 27545 20841 116 -2837 -6357 C ATOM 5454 O MET B 284 130.012 -69.104 37.481 1.00167.74 O ANISOU 5454 O MET B 284 14754 27430 21550 -226 -2824 -6602 O ATOM 5455 CB MET B 284 127.124 -70.346 36.936 1.00157.33 C ANISOU 5455 CB MET B 284 14327 25829 19621 155 -2342 -5587 C ATOM 5456 CG MET B 284 126.412 -70.747 35.669 1.00156.56 C ANISOU 5456 CG MET B 284 14467 25358 19659 63 -2030 -5027 C ATOM 5457 SD MET B 284 127.088 -69.993 34.160 1.00160.97 S ANISOU 5457 SD MET B 284 14846 25432 20885 -375 -1834 -4933 S ATOM 5458 CE MET B 284 125.809 -70.426 32.993 1.00152.58 C ANISOU 5458 CE MET B 284 14164 24000 19810 -370 -1510 -4323 C ATOM 5459 N GLY B 285 129.371 -70.310 39.289 1.00165.77 N ANISOU 5459 N GLY B 285 14750 27948 20286 433 -3095 -6634 N ATOM 5460 CA GLY B 285 130.086 -69.543 40.302 1.00171.33 C ANISOU 5460 CA GLY B 285 15168 28915 21015 422 -3425 -7302 C ATOM 5461 C GLY B 285 129.178 -68.644 41.119 1.00177.48 C ANISOU 5461 C GLY B 285 16115 29611 21708 475 -3474 -7666 C ATOM 5462 O GLY B 285 129.665 -67.768 41.839 1.00181.88 O ANISOU 5462 O GLY B 285 16447 30266 22392 400 -3725 -8282 O ATOM 5463 N VAL B 286 127.849 -68.857 41.017 1.00170.64 N ANISOU 5463 N VAL B 286 15635 28564 20637 607 -3237 -7306 N ATOM 5464 CA VAL B 286 126.840 -68.076 41.737 1.00171.83 C ANISOU 5464 CA VAL B 286 15984 28619 20686 689 -3230 -7581 C ATOM 5465 C VAL B 286 126.873 -68.476 43.218 1.00180.15 C ANISOU 5465 C VAL B 286 17053 30302 21095 1108 -3504 -7876 C ATOM 5466 O VAL B 286 127.229 -67.654 44.066 1.00185.08 O ANISOU 5466 O VAL B 286 17514 31084 21725 1110 -3758 -8500 O ATOM 5467 CB VAL B 286 125.420 -68.225 41.128 1.00170.66 C ANISOU 5467 CB VAL B 286 16215 28095 20534 706 -2884 -7076 C ATOM 5468 CG1 VAL B 286 124.469 -67.172 41.688 1.00172.09 C ANISOU 5468 CG1 VAL B 286 16547 28068 20772 709 -2850 -7403 C ATOM 5469 CG2 VAL B 286 125.452 -68.162 39.603 1.00166.75 C ANISOU 5469 CG2 VAL B 286 15723 27089 20545 373 -2620 -6670 C ATOM 5470 N ILE B 287 126.525 -69.739 43.517 1.00174.99 N ANISOU 5470 N ILE B 287 16589 30005 19893 1468 -3452 -7431 N ATOM 5471 CA ILE B 287 126.546 -70.286 44.872 1.00178.15 C ANISOU 5471 CA ILE B 287 17028 31036 19623 1918 -3673 -7592 C ATOM 5472 C ILE B 287 127.926 -70.933 45.079 1.00184.61 C ANISOU 5472 C ILE B 287 17538 32302 20304 2011 -3947 -7688 C ATOM 5473 O ILE B 287 128.352 -71.761 44.268 1.00180.88 O ANISOU 5473 O ILE B 287 17018 31770 19937 1955 -3837 -7251 O ATOM 5474 CB ILE B 287 125.330 -71.232 45.177 1.00178.19 C ANISOU 5474 CB ILE B 287 17411 31166 19127 2276 -3442 -7055 C ATOM 5475 CG1 ILE B 287 125.466 -71.956 46.547 1.00181.98 C ANISOU 5475 CG1 ILE B 287 17923 32346 18874 2781 -3648 -7131 C ATOM 5476 CG2 ILE B 287 125.026 -72.224 44.049 1.00173.43 C ANISOU 5476 CG2 ILE B 287 16948 30294 18653 2205 -3154 -6352 C ATOM 5477 CD1 ILE B 287 125.018 -71.145 47.740 1.00192.80 C ANISOU 5477 CD1 ILE B 287 19485 33757 20016 2890 -3753 -7489 C ATOM 5478 N ASN B 288 128.648 -70.492 46.126 1.00186.83 N ANISOU 5478 N ASN B 288 17588 33014 20384 2141 -4312 -8293 N ATOM 5479 CA ASN B 288 130.000 -70.968 46.427 1.00187.69 C ANISOU 5479 CA ASN B 288 17586 33255 20472 2108 -4557 -8169 C ATOM 5480 C ASN B 288 130.137 -71.512 47.854 1.00190.97 C ANISOU 5480 C ASN B 288 18537 33618 20403 2286 -4676 -7677 C ATOM 5481 O ASN B 288 131.180 -72.094 48.175 1.00191.08 O ANISOU 5481 O ASN B 288 18500 33763 20337 2311 -4868 -7491 O ATOM 5482 CB ASN B 288 131.016 -69.846 46.208 1.00189.57 C ANISOU 5482 CB ASN B 288 17710 32952 21368 1578 -4698 -8379 C ATOM 5483 N SER B 289 129.117 -71.311 48.712 1.00188.91 N ANISOU 5483 N SER B 289 18524 33533 19723 2552 -4634 -7812 N ATOM 5484 CA SER B 289 129.164 -71.811 50.085 1.00189.50 C ANISOU 5484 CA SER B 289 18990 33735 19275 2784 -4745 -7525 C ATOM 5485 C SER B 289 129.005 -73.331 50.073 1.00190.56 C ANISOU 5485 C SER B 289 19240 34149 19017 3131 -4608 -6933 C ATOM 5486 O SER B 289 127.955 -73.843 49.674 1.00189.06 O ANISOU 5486 O SER B 289 19027 34229 18577 3434 -4365 -6819 O ATOM 5487 CB SER B 289 128.109 -71.138 50.958 1.00192.42 C ANISOU 5487 CB SER B 289 19873 33743 19495 2747 -4601 -7456 C ATOM 5488 OG SER B 289 126.813 -71.284 50.404 1.00197.28 O ANISOU 5488 OG SER B 289 20764 34001 20191 2738 -4206 -7060 O ATOM 5489 N CYS B 290 130.087 -74.041 50.458 1.00188.47 N ANISOU 5489 N CYS B 290 18835 34206 18568 3265 -4846 -6846 N ATOM 5490 CA CYS B 290 130.202 -75.504 50.496 1.00187.44 C ANISOU 5490 CA CYS B 290 18701 34468 18049 3649 -4790 -6389 C ATOM 5491 C CYS B 290 129.131 -76.155 51.388 1.00189.91 C ANISOU 5491 C CYS B 290 19546 34696 17916 3902 -4560 -5883 C ATOM 5492 O CYS B 290 128.734 -77.291 51.113 1.00188.47 O ANISOU 5492 O CYS B 290 19331 34843 17436 4263 -4388 -5521 O ATOM 5493 CB CYS B 290 131.605 -75.922 50.927 1.00188.61 C ANISOU 5493 CB CYS B 290 18824 34564 18275 3537 -5061 -6214 C ATOM 5494 SG CYS B 290 132.111 -75.281 52.545 1.00193.37 S ANISOU 5494 SG CYS B 290 19977 34628 18865 3207 -5286 -6071 S ATOM 5495 N GLU B 291 128.668 -75.440 52.442 1.00188.59 N ANISOU 5495 N GLU B 291 19619 34532 17504 3935 -4624 -6128 N ATOM 5496 CA GLU B 291 127.635 -75.894 53.388 1.00188.17 C ANISOU 5496 CA GLU B 291 19947 34611 16940 4257 -4436 -5848 C ATOM 5497 C GLU B 291 126.319 -76.194 52.645 1.00188.77 C ANISOU 5497 C GLU B 291 20038 34703 16982 4434 -4067 -5641 C ATOM 5498 O GLU B 291 125.706 -77.234 52.880 1.00187.83 O ANISOU 5498 O GLU B 291 20057 34831 16480 4797 -3867 -5203 O ATOM 5499 CB GLU B 291 127.395 -74.848 54.501 1.00190.63 C ANISOU 5499 CB GLU B 291 20660 34527 17242 4001 -4492 -6024 C ATOM 5500 CG GLU B 291 128.641 -74.369 55.240 1.00199.17 C ANISOU 5500 CG GLU B 291 22168 34757 18752 3332 -4701 -5739 C ATOM 5501 CD GLU B 291 129.229 -75.269 56.312 1.00212.74 C ANISOU 5501 CD GLU B 291 24729 35402 20700 2774 -4594 -4663 C ATOM 5502 OE1 GLU B 291 130.464 -75.209 56.512 1.00207.01 O ANISOU 5502 OE1 GLU B 291 23622 35187 19845 2898 -5006 -5030 O ATOM 5503 OE2 GLU B 291 128.462 -76.000 56.980 1.00208.64 O ANISOU 5503 OE2 GLU B 291 24294 35349 19629 3223 -4477 -4595 O ATOM 5504 N VAL B 292 125.920 -75.294 51.725 1.00185.60 N ANISOU 5504 N VAL B 292 19262 34456 16803 4392 -4055 -6189 N ATOM 5505 CA VAL B 292 124.715 -75.391 50.889 1.00183.92 C ANISOU 5505 CA VAL B 292 18899 34453 16528 4609 -3775 -6185 C ATOM 5506 C VAL B 292 124.931 -76.476 49.808 1.00183.55 C ANISOU 5506 C VAL B 292 18633 34563 16543 4703 -3655 -5794 C ATOM 5507 O VAL B 292 124.009 -77.249 49.543 1.00179.47 O ANISOU 5507 O VAL B 292 18368 33865 15957 4809 -3330 -5209 O ATOM 5508 CB VAL B 292 124.339 -74.000 50.278 1.00187.00 C ANISOU 5508 CB VAL B 292 19266 34294 17492 4156 -3723 -6585 C ATOM 5509 CG1 VAL B 292 123.154 -74.093 49.322 1.00183.58 C ANISOU 5509 CG1 VAL B 292 18858 33670 17226 4145 -3384 -6347 C ATOM 5510 CG2 VAL B 292 124.047 -72.977 51.371 1.00188.43 C ANISOU 5510 CG2 VAL B 292 19799 34133 17662 4002 -3773 -6806 C ATOM 5511 N ILE B 293 126.149 -76.538 49.211 1.00179.30 N ANISOU 5511 N ILE B 293 17803 34011 16312 4486 -3853 -5926 N ATOM 5512 CA ILE B 293 126.536 -77.504 48.164 1.00174.72 C ANISOU 5512 CA ILE B 293 17184 33202 16001 4361 -3704 -5409 C ATOM 5513 C ILE B 293 126.438 -78.951 48.710 1.00178.08 C ANISOU 5513 C ILE B 293 17750 34019 15896 4841 -3623 -4862 C ATOM 5514 O ILE B 293 125.987 -79.843 47.987 1.00173.82 O ANISOU 5514 O ILE B 293 17363 33188 15491 4819 -3340 -4284 O ATOM 5515 CB ILE B 293 127.950 -77.182 47.570 1.00178.76 C ANISOU 5515 CB ILE B 293 17315 33693 16911 4070 -3956 -5737 C ATOM 5516 CG1 ILE B 293 127.961 -75.789 46.868 1.00178.50 C ANISOU 5516 CG1 ILE B 293 17161 33165 17497 3558 -3959 -6179 C ATOM 5517 CG2 ILE B 293 128.416 -78.280 46.594 1.00175.89 C ANISOU 5517 CG2 ILE B 293 16910 33175 16744 4016 -3812 -5208 C ATOM 5518 CD1 ILE B 293 129.313 -75.087 46.794 1.00188.28 C ANISOU 5518 CD1 ILE B 293 18033 34426 19079 3288 -4271 -6680 C ATOM 5519 N ALA B 294 126.823 -79.164 49.983 1.00178.68 N ANISOU 5519 N ALA B 294 17777 34739 15375 5280 -3864 -5047 N ATOM 5520 CA ALA B 294 126.769 -80.469 50.646 1.00178.51 C ANISOU 5520 CA ALA B 294 17948 34991 14886 5705 -3779 -4486 C ATOM 5521 C ALA B 294 125.326 -80.983 50.766 1.00179.43 C ANISOU 5521 C ALA B 294 18364 35056 14756 5951 -3399 -4014 C ATOM 5522 O ALA B 294 125.079 -82.170 50.533 1.00176.73 O ANISOU 5522 O ALA B 294 18149 34656 14343 6126 -3174 -3399 O ATOM 5523 CB ALA B 294 127.409 -80.378 52.022 1.00180.54 C ANISOU 5523 CB ALA B 294 18544 34986 15067 5577 -3991 -4441 C ATOM 5524 N VAL B 295 124.376 -80.077 51.094 1.00175.59 N ANISOU 5524 N VAL B 295 18030 34435 14251 5881 -3304 -4259 N ATOM 5525 CA VAL B 295 122.943 -80.371 51.251 1.00173.25 C ANISOU 5525 CA VAL B 295 18051 33945 13830 6014 -2927 -3831 C ATOM 5526 C VAL B 295 122.366 -80.900 49.917 1.00170.40 C ANISOU 5526 C VAL B 295 17793 32939 14010 5686 -2601 -3318 C ATOM 5527 O VAL B 295 121.646 -81.905 49.932 1.00168.73 O ANISOU 5527 O VAL B 295 17773 32664 13671 5889 -2316 -2730 O ATOM 5528 CB VAL B 295 122.159 -79.133 51.784 1.00178.99 C ANISOU 5528 CB VAL B 295 18874 34634 14501 5961 -2922 -4290 C ATOM 5529 CG1 VAL B 295 120.659 -79.411 51.884 1.00176.77 C ANISOU 5529 CG1 VAL B 295 18894 34129 14142 6076 -2516 -3840 C ATOM 5530 CG2 VAL B 295 122.699 -78.681 53.138 1.00181.29 C ANISOU 5530 CG2 VAL B 295 19421 34821 14640 5868 -3141 -4499 C ATOM 5531 N ILE B 296 122.708 -80.250 48.777 1.00162.84 N ANISOU 5531 N ILE B 296 16702 31520 13650 5195 -2645 -3538 N ATOM 5532 CA ILE B 296 122.253 -80.657 47.438 1.00156.65 C ANISOU 5532 CA ILE B 296 15998 30144 13378 4871 -2378 -3121 C ATOM 5533 C ILE B 296 122.657 -82.122 47.193 1.00159.80 C ANISOU 5533 C ILE B 296 16403 30635 13679 5072 -2297 -2583 C ATOM 5534 O ILE B 296 121.807 -82.944 46.840 1.00156.21 O ANISOU 5534 O ILE B 296 16140 29925 13287 5123 -2001 -2058 O ATOM 5535 CB ILE B 296 122.792 -79.707 46.322 1.00157.23 C ANISOU 5535 CB ILE B 296 15893 29800 14049 4357 -2477 -3473 C ATOM 5536 CG1 ILE B 296 122.384 -78.234 46.576 1.00158.79 C ANISOU 5536 CG1 ILE B 296 16084 29865 14385 4161 -2546 -4005 C ATOM 5537 CG2 ILE B 296 122.341 -80.175 44.927 1.00152.50 C ANISOU 5537 CG2 ILE B 296 15386 28635 13920 4062 -2211 -3035 C ATOM 5538 CD1 ILE B 296 123.171 -77.162 45.768 1.00164.21 C ANISOU 5538 CD1 ILE B 296 16536 30253 15603 3707 -2708 -4458 C ATOM 5539 N ASP B 297 123.943 -82.438 47.449 1.00159.85 N ANISOU 5539 N ASP B 297 16189 31019 13529 5207 -2567 -2733 N ATOM 5540 CA ASP B 297 124.562 -83.753 47.288 1.00159.59 C ANISOU 5540 CA ASP B 297 16113 31126 13397 5422 -2547 -2304 C ATOM 5541 C ASP B 297 123.871 -84.835 48.136 1.00164.17 C ANISOU 5541 C ASP B 297 16912 31953 13513 5894 -2347 -1787 C ATOM 5542 O ASP B 297 123.650 -85.940 47.639 1.00161.72 O ANISOU 5542 O ASP B 297 16697 31430 13318 5955 -2128 -1257 O ATOM 5543 CB ASP B 297 126.063 -83.680 47.641 1.00165.19 C ANISOU 5543 CB ASP B 297 16515 32284 13964 5522 -2919 -2659 C ATOM 5544 CG ASP B 297 126.883 -82.717 46.793 1.00175.81 C ANISOU 5544 CG ASP B 297 17601 33394 15804 5063 -3102 -3130 C ATOM 5545 OD1 ASP B 297 126.620 -82.622 45.572 1.00172.69 O ANISOU 5545 OD1 ASP B 297 17243 32461 15911 4687 -2911 -2984 O ATOM 5546 OD2 ASP B 297 127.825 -82.100 47.339 1.00184.70 O ANISOU 5546 OD2 ASP B 297 18474 34886 16817 5090 -3436 -3632 O ATOM 5547 N LEU B 298 123.521 -84.516 49.390 1.00163.76 N ANISOU 5547 N LEU B 298 16937 32332 12952 6227 -2409 -1940 N ATOM 5548 CA LEU B 298 122.876 -85.455 50.309 1.00165.33 C ANISOU 5548 CA LEU B 298 17337 32813 12668 6708 -2207 -1455 C ATOM 5549 C LEU B 298 121.413 -85.757 49.892 1.00164.50 C ANISOU 5549 C LEU B 298 17487 32226 12789 6603 -1786 -1005 C ATOM 5550 O LEU B 298 120.974 -86.914 49.965 1.00163.72 O ANISOU 5550 O LEU B 298 17522 32076 12609 6835 -1532 -417 O ATOM 5551 CB LEU B 298 122.988 -84.954 51.778 1.00171.19 C ANISOU 5551 CB LEU B 298 18078 34203 12763 7111 -2411 -1791 C ATOM 5552 CG LEU B 298 122.031 -83.939 52.416 1.00177.24 C ANISOU 5552 CG LEU B 298 18995 34978 13370 7103 -2344 -2092 C ATOM 5553 CD1 LEU B 298 120.818 -84.635 53.005 1.00177.32 C ANISOU 5553 CD1 LEU B 298 19323 34889 13159 7350 -1958 -1520 C ATOM 5554 CD2 LEU B 298 122.712 -83.219 53.587 1.00180.38 C ANISOU 5554 CD2 LEU B 298 19663 35025 13848 6746 -2622 -2440 C ATOM 5555 N ALA B 299 120.680 -84.715 49.462 1.00157.73 N ANISOU 5555 N ALA B 299 16681 31012 12237 6258 -1718 -1285 N ATOM 5556 CA ALA B 299 119.270 -84.790 49.083 1.00154.00 C ANISOU 5556 CA ALA B 299 16417 30097 11999 6133 -1358 -952 C ATOM 5557 C ALA B 299 119.032 -85.429 47.702 1.00151.37 C ANISOU 5557 C ALA B 299 16106 29180 12227 5805 -1169 -585 C ATOM 5558 O ALA B 299 117.961 -86.009 47.482 1.00148.98 O ANISOU 5558 O ALA B 299 15966 28583 12057 5817 -856 -143 O ATOM 5559 CB ALA B 299 118.660 -83.399 49.113 1.00154.52 C ANISOU 5559 CB ALA B 299 16508 30010 12192 5897 -1384 -1416 C ATOM 5560 N LEU B 300 120.028 -85.333 46.795 1.00145.06 N ANISOU 5560 N LEU B 300 15136 28231 11749 5527 -1358 -774 N ATOM 5561 CA LEU B 300 119.999 -85.826 45.411 1.00139.98 C ANISOU 5561 CA LEU B 300 14491 27072 11622 5204 -1232 -524 C ATOM 5562 C LEU B 300 119.397 -87.262 45.234 1.00139.89 C ANISOU 5562 C LEU B 300 14626 26882 11645 5385 -944 125 C ATOM 5563 O LEU B 300 118.499 -87.372 44.400 1.00135.97 O ANISOU 5563 O LEU B 300 14235 25907 11521 5144 -731 332 O ATOM 5564 CB LEU B 300 121.404 -85.762 44.786 1.00140.17 C ANISOU 5564 CB LEU B 300 14288 27147 11821 5038 -1486 -773 C ATOM 5565 CG LEU B 300 121.487 -85.882 43.260 1.00140.81 C ANISOU 5565 CG LEU B 300 14343 26706 12451 4641 -1401 -677 C ATOM 5566 CD1 LEU B 300 121.382 -84.516 42.592 1.00139.26 C ANISOU 5566 CD1 LEU B 300 14089 26225 12600 4223 -1469 -1098 C ATOM 5567 CD2 LEU B 300 122.776 -86.576 42.841 1.00143.77 C ANISOU 5567 CD2 LEU B 300 14543 27203 12880 4677 -1541 -634 C ATOM 5568 N PRO B 301 119.801 -88.351 45.957 1.00137.20 N ANISOU 5568 N PRO B 301 14293 26876 10960 5794 -923 457 N ATOM 5569 CA PRO B 301 119.187 -89.670 45.691 1.00134.83 C ANISOU 5569 CA PRO B 301 14124 26314 10791 5918 -628 1064 C ATOM 5570 C PRO B 301 117.719 -89.786 46.124 1.00135.17 C ANISOU 5570 C PRO B 301 14356 26203 10798 6009 -315 1371 C ATOM 5571 O PRO B 301 117.021 -90.661 45.618 1.00132.54 O ANISOU 5571 O PRO B 301 14116 25499 10746 5966 -58 1805 O ATOM 5572 CB PRO B 301 120.069 -90.646 46.479 1.00140.51 C ANISOU 5572 CB PRO B 301 14790 27476 11121 6359 -705 1299 C ATOM 5573 CG PRO B 301 121.324 -89.884 46.798 1.00147.43 C ANISOU 5573 CG PRO B 301 15464 28776 11777 6375 -1082 782 C ATOM 5574 CD PRO B 301 120.863 -88.475 46.977 1.00142.96 C ANISOU 5574 CD PRO B 301 14901 28212 11204 6158 -1170 307 C ATOM 5575 N PHE B 302 117.252 -88.919 47.046 1.00131.81 N ANISOU 5575 N PHE B 302 13976 26057 10050 6134 -333 1137 N ATOM 5576 CA PHE B 302 115.855 -88.891 47.502 1.00130.81 C ANISOU 5576 CA PHE B 302 14008 25814 9880 6223 -31 1387 C ATOM 5577 C PHE B 302 114.975 -88.165 46.465 1.00128.07 C ANISOU 5577 C PHE B 302 13691 24928 10044 5769 59 1245 C ATOM 5578 O PHE B 302 113.807 -88.519 46.277 1.00126.27 O ANISOU 5578 O PHE B 302 13565 24387 10025 5726 347 1580 O ATOM 5579 CB PHE B 302 115.765 -88.207 48.875 1.00136.83 C ANISOU 5579 CB PHE B 302 14804 27110 10076 6553 -97 1152 C ATOM 5580 N ALA B 303 115.557 -87.165 45.782 1.00121.01 N ANISOU 5580 N ALA B 303 12691 23925 9362 5435 -185 760 N ATOM 5581 CA ALA B 303 114.906 -86.410 44.718 1.00116.28 C ANISOU 5581 CA ALA B 303 12106 22836 9241 5007 -140 601 C ATOM 5582 C ALA B 303 114.774 -87.280 43.456 1.00115.38 C ANISOU 5582 C ALA B 303 12002 22256 9582 4778 -26 927 C ATOM 5583 O ALA B 303 113.758 -87.188 42.761 1.00112.76 O ANISOU 5583 O ALA B 303 11738 21508 9596 4555 142 1055 O ATOM 5584 CB ALA B 303 115.701 -85.153 44.421 1.00116.67 C ANISOU 5584 CB ALA B 303 12030 22932 9367 4756 -426 20 C ATOM 5585 N ILE B 304 115.791 -88.150 43.194 1.00110.63 N ANISOU 5585 N ILE B 304 11329 21741 8965 4857 -122 1054 N ATOM 5586 CA ILE B 304 115.886 -89.104 42.068 1.00107.06 C ANISOU 5586 CA ILE B 304 10878 20909 8889 4697 -41 1337 C ATOM 5587 C ILE B 304 114.808 -90.212 42.219 1.00110.01 C ANISOU 5587 C ILE B 304 11376 21069 9353 4851 269 1870 C ATOM 5588 O ILE B 304 114.297 -90.719 41.213 1.00106.56 O ANISOU 5588 O ILE B 304 10974 20189 9324 4636 388 2061 O ATOM 5589 CB ILE B 304 117.345 -89.681 41.973 1.00110.87 C ANISOU 5589 CB ILE B 304 11236 21624 9265 4810 -233 1297 C ATOM 5590 CG1 ILE B 304 118.305 -88.650 41.336 1.00109.90 C ANISOU 5590 CG1 ILE B 304 10965 21521 9271 4521 -496 805 C ATOM 5591 CG2 ILE B 304 117.421 -91.025 41.221 1.00109.97 C ANISOU 5591 CG2 ILE B 304 11151 21221 9410 4819 -100 1696 C ATOM 5592 CD1 ILE B 304 119.789 -88.843 41.641 1.00116.60 C ANISOU 5592 CD1 ILE B 304 11643 22755 9905 4678 -734 639 C ATOM 5593 N LEU B 305 114.475 -90.573 43.472 1.00109.79 N ANISOU 5593 N LEU B 305 11407 21362 8948 5225 399 2099 N ATOM 5594 CA LEU B 305 113.470 -91.587 43.788 1.00110.51 C ANISOU 5594 CA LEU B 305 11597 21285 9106 5403 721 2623 C ATOM 5595 C LEU B 305 112.046 -91.083 43.485 1.00113.94 C ANISOU 5595 C LEU B 305 12094 21375 9822 5187 914 2655 C ATOM 5596 O LEU B 305 111.218 -91.869 43.015 1.00112.93 O ANISOU 5596 O LEU B 305 12003 20870 10034 5112 1137 3010 O ATOM 5597 CB LEU B 305 113.595 -92.020 45.264 1.00114.86 C ANISOU 5597 CB LEU B 305 12188 22329 9125 5894 810 2857 C ATOM 5598 CG LEU B 305 112.693 -93.171 45.705 1.00120.93 C ANISOU 5598 CG LEU B 305 13045 22959 9943 6129 1171 3459 C ATOM 5599 CD1 LEU B 305 113.100 -94.478 45.055 1.00120.35 C ANISOU 5599 CD1 LEU B 305 12955 22607 10165 6131 1235 3804 C ATOM 5600 CD2 LEU B 305 112.686 -93.297 47.193 1.00128.05 C ANISOU 5600 CD2 LEU B 305 14000 24380 10273 6606 1269 3642 C ATOM 5601 N LEU B 306 111.770 -89.781 43.740 1.00110.82 N ANISOU 5601 N LEU B 306 11697 21099 9312 5086 822 2273 N ATOM 5602 CA LEU B 306 110.471 -89.145 43.482 1.00109.47 C ANISOU 5602 CA LEU B 306 11569 20634 9389 4893 979 2253 C ATOM 5603 C LEU B 306 110.106 -89.184 41.993 1.00109.62 C ANISOU 5603 C LEU B 306 11568 20118 9964 4488 968 2246 C ATOM 5604 O LEU B 306 108.931 -89.324 41.655 1.00108.01 O ANISOU 5604 O LEU B 306 11393 19590 10055 4375 1164 2447 O ATOM 5605 CB LEU B 306 110.460 -87.695 43.990 1.00110.39 C ANISOU 5605 CB LEU B 306 11680 20983 9281 4866 843 1787 C ATOM 5606 CG LEU B 306 110.176 -87.495 45.473 1.00118.98 C ANISOU 5606 CG LEU B 306 12821 22522 9864 5253 945 1811 C ATOM 5607 CD1 LEU B 306 110.534 -86.090 45.894 1.00120.21 C ANISOU 5607 CD1 LEU B 306 12950 22929 9793 5218 727 1250 C ATOM 5608 CD2 LEU B 306 108.712 -87.773 45.801 1.00121.61 C ANISOU 5608 CD2 LEU B 306 13224 22683 10298 5341 1296 2173 C ATOM 5609 N GLY B 307 111.122 -89.084 41.134 1.00104.83 N ANISOU 5609 N GLY B 307 10904 19445 9483 4293 741 2021 N ATOM 5610 CA GLY B 307 110.981 -89.178 39.686 1.00101.46 C ANISOU 5610 CA GLY B 307 10462 18569 9519 3946 704 2001 C ATOM 5611 C GLY B 307 110.463 -90.541 39.265 1.00105.56 C ANISOU 5611 C GLY B 307 11012 18791 10306 3974 892 2436 C ATOM 5612 O GLY B 307 109.583 -90.631 38.404 1.00103.42 O ANISOU 5612 O GLY B 307 10754 18123 10417 3747 975 2518 O ATOM 5613 N PHE B 308 110.982 -91.611 39.909 1.00104.56 N ANISOU 5613 N PHE B 308 10889 18855 9984 4267 962 2717 N ATOM 5614 CA PHE B 308 110.581 -93.003 39.682 1.00104.78 C ANISOU 5614 CA PHE B 308 10940 18614 10259 4343 1160 3153 C ATOM 5615 C PHE B 308 109.188 -93.276 40.263 1.00110.44 C ANISOU 5615 C PHE B 308 11694 19200 11070 4435 1453 3479 C ATOM 5616 O PHE B 308 108.463 -94.115 39.730 1.00108.93 O ANISOU 5616 O PHE B 308 11501 18625 11265 4342 1616 3755 O ATOM 5617 CB PHE B 308 111.607 -93.973 40.291 1.00108.93 C ANISOU 5617 CB PHE B 308 11456 19407 10525 4662 1150 3359 C ATOM 5618 N THR B 309 108.824 -92.563 41.356 1.00110.10 N ANISOU 5618 N THR B 309 11674 19478 10683 4621 1522 3431 N ATOM 5619 CA THR B 309 107.534 -92.671 42.055 1.00112.48 C ANISOU 5619 CA THR B 309 11999 19729 11009 4745 1818 3721 C ATOM 5620 C THR B 309 106.383 -92.217 41.134 1.00114.81 C ANISOU 5620 C THR B 309 12265 19590 11768 4402 1870 3647 C ATOM 5621 O THR B 309 105.273 -92.745 41.242 1.00115.05 O ANISOU 5621 O THR B 309 12276 19388 12049 4415 2129 3970 O ATOM 5622 CB THR B 309 107.571 -91.864 43.371 1.00123.92 C ANISOU 5622 CB THR B 309 13483 21671 11931 5025 1835 3594 C ATOM 5623 OG1 THR B 309 108.748 -92.211 44.095 1.00125.41 O ANISOU 5623 OG1 THR B 309 13683 22281 11685 5324 1720 3599 O ATOM 5624 CG2 THR B 309 106.351 -92.110 44.257 1.00125.16 C ANISOU 5624 CG2 THR B 309 13667 21849 12040 5235 2184 3953 C ATOM 5625 N ASN B 310 106.664 -91.271 40.210 1.00109.20 N ANISOU 5625 N ASN B 310 11538 18767 11187 4104 1627 3239 N ATOM 5626 CA ASN B 310 105.704 -90.765 39.224 1.00106.76 C ANISOU 5626 CA ASN B 310 11200 18069 11293 3783 1624 3135 C ATOM 5627 C ASN B 310 105.148 -91.913 38.359 1.00110.24 C ANISOU 5627 C ASN B 310 11608 18079 12199 3645 1729 3424 C ATOM 5628 O ASN B 310 103.981 -91.871 37.976 1.00109.19 O ANISOU 5628 O ASN B 310 11432 17654 12400 3498 1844 3517 O ATOM 5629 CB ASN B 310 106.366 -89.695 38.350 1.00105.36 C ANISOU 5629 CB ASN B 310 11020 17869 11144 3523 1339 2688 C ATOM 5630 CG ASN B 310 105.460 -89.026 37.344 1.00130.84 C ANISOU 5630 CG ASN B 310 14227 20744 14743 3220 1310 2559 C ATOM 5631 OD1 ASN B 310 105.709 -89.066 36.133 1.00123.38 O ANISOU 5631 OD1 ASN B 310 13274 19552 14054 2980 1166 2451 O ATOM 5632 ND2 ASN B 310 104.415 -88.356 37.819 1.00124.53 N ANISOU 5632 ND2 ASN B 310 13419 19937 13960 3242 1440 2560 N ATOM 5633 N SER B 311 105.977 -92.949 38.099 1.00107.76 N ANISOU 5633 N SER B 311 11303 17730 11912 3708 1689 3559 N ATOM 5634 CA SER B 311 105.625 -94.152 37.337 1.00107.64 C ANISOU 5634 CA SER B 311 11260 17316 12324 3608 1775 3809 C ATOM 5635 C SER B 311 104.615 -95.020 38.094 1.00115.11 C ANISOU 5635 C SER B 311 12174 18144 13421 3778 2103 4256 C ATOM 5636 O SER B 311 103.877 -95.780 37.468 1.00113.88 O ANISOU 5636 O SER B 311 11963 17587 13721 3636 2204 4434 O ATOM 5637 CB SER B 311 106.875 -94.971 37.029 1.00111.46 C ANISOU 5637 CB SER B 311 11765 17842 12744 3685 1660 3823 C ATOM 5638 OG SER B 311 107.798 -94.230 36.247 1.00119.02 O ANISOU 5638 OG SER B 311 12731 18878 13612 3512 1383 3434 O ATOM 5639 N CYS B 312 104.604 -94.922 39.435 1.00116.09 N ANISOU 5639 N CYS B 312 12324 18620 13164 4088 2270 4434 N ATOM 5640 CA CYS B 312 103.681 -95.662 40.301 1.00119.72 C ANISOU 5640 CA CYS B 312 12755 19026 13708 4292 2623 4892 C ATOM 5641 C CYS B 312 102.340 -94.920 40.370 1.00123.99 C ANISOU 5641 C CYS B 312 13236 19451 14422 4168 2756 4867 C ATOM 5642 O CYS B 312 101.298 -95.552 40.550 1.00125.80 O ANISOU 5642 O CYS B 312 13391 19438 14971 4179 3032 5208 O ATOM 5643 CB CYS B 312 104.269 -95.874 41.697 1.00123.53 C ANISOU 5643 CB CYS B 312 13301 19974 13663 4713 2749 5105 C ATOM 5644 SG CYS B 312 106.003 -96.409 41.720 1.00127.67 S ANISOU 5644 SG CYS B 312 13881 20758 13869 4891 2524 5037 S ATOM 5645 N VAL B 313 102.377 -93.580 40.248 1.00118.30 N ANISOU 5645 N VAL B 313 12538 18898 13513 4057 2571 4469 N ATOM 5646 CA VAL B 313 101.199 -92.714 40.308 1.00117.71 C ANISOU 5646 CA VAL B 313 12410 18745 13567 3954 2667 4392 C ATOM 5647 C VAL B 313 100.399 -92.824 38.997 1.00118.47 C ANISOU 5647 C VAL B 313 12416 18357 14242 3601 2601 4339 C ATOM 5648 O VAL B 313 99.181 -92.983 39.056 1.00118.89 O ANISOU 5648 O VAL B 313 12369 18197 14606 3555 2809 4541 O ATOM 5649 CB VAL B 313 101.579 -91.237 40.629 1.00121.07 C ANISOU 5649 CB VAL B 313 12896 19499 13608 3969 2486 3970 C ATOM 5650 CG1 VAL B 313 100.335 -90.368 40.793 1.00121.21 C ANISOU 5650 CG1 VAL B 313 12861 19443 13751 3908 2617 3915 C ATOM 5651 CG2 VAL B 313 102.447 -91.143 41.880 1.00123.59 C ANISOU 5651 CG2 VAL B 313 13297 20323 13340 4320 2501 3966 C ATOM 5652 N ASN B 314 101.093 -92.756 37.830 1.00112.14 N ANISOU 5652 N ASN B 314 11638 17399 13571 3368 2314 4071 N ATOM 5653 CA ASN B 314 100.537 -92.802 36.466 1.00109.67 C ANISOU 5653 CA ASN B 314 11259 16677 13732 3045 2181 3954 C ATOM 5654 C ASN B 314 99.370 -93.812 36.269 1.00115.64 C ANISOU 5654 C ASN B 314 11891 17060 14989 2978 2395 4282 C ATOM 5655 O ASN B 314 98.342 -93.368 35.752 1.00114.93 O ANISOU 5655 O ASN B 314 11708 16760 15201 2796 2387 4213 O ATOM 5656 CB ASN B 314 101.630 -93.062 35.424 1.00107.51 C ANISOU 5656 CB ASN B 314 11043 16325 13482 2902 1914 3742 C ATOM 5657 CG ASN B 314 102.543 -91.891 35.163 1.00125.53 C ANISOU 5657 CG ASN B 314 13399 18843 15452 2838 1666 3356 C ATOM 5658 OD1 ASN B 314 102.257 -90.734 35.513 1.00115.72 O ANISOU 5658 OD1 ASN B 314 12165 17754 14050 2833 1647 3177 O ATOM 5659 ND2 ASN B 314 103.677 -92.175 34.540 1.00117.12 N ANISOU 5659 ND2 ASN B 314 12382 17800 14320 2789 1482 3217 N ATOM 5660 N PRO B 315 99.441 -95.114 36.681 1.00114.59 N ANISOU 5660 N PRO B 315 11734 16825 14979 3120 2592 4637 N ATOM 5661 CA PRO B 315 98.279 -96.014 36.478 1.00116.25 C ANISOU 5661 CA PRO B 315 11797 16641 15731 3026 2801 4928 C ATOM 5662 C PRO B 315 96.964 -95.522 37.111 1.00121.57 C ANISOU 5662 C PRO B 315 12355 17317 16519 3057 3042 5081 C ATOM 5663 O PRO B 315 95.891 -95.752 36.547 1.00121.24 O ANISOU 5663 O PRO B 315 12160 16937 16971 2864 3090 5137 O ATOM 5664 CB PRO B 315 98.729 -97.313 37.148 1.00120.72 C ANISOU 5664 CB PRO B 315 12383 17191 16294 3251 3019 5312 C ATOM 5665 CG PRO B 315 100.204 -97.280 37.074 1.00123.81 C ANISOU 5665 CG PRO B 315 12919 17833 16289 3351 2805 5130 C ATOM 5666 CD PRO B 315 100.563 -95.850 37.302 1.00117.48 C ANISOU 5666 CD PRO B 315 12192 17401 15045 3365 2634 4796 C ATOM 5667 N PHE B 316 97.057 -94.833 38.265 1.00119.32 N ANISOU 5667 N PHE B 316 12135 17424 15777 3305 3180 5127 N ATOM 5668 CA PHE B 316 95.919 -94.287 39.010 1.00120.82 C ANISOU 5668 CA PHE B 316 12234 17688 15984 3391 3432 5264 C ATOM 5669 C PHE B 316 95.376 -92.995 38.382 1.00122.41 C ANISOU 5669 C PHE B 316 12400 17859 16250 3187 3239 4899 C ATOM 5670 O PHE B 316 94.204 -92.671 38.584 1.00123.36 O ANISOU 5670 O PHE B 316 12390 17889 16591 3164 3414 4995 O ATOM 5671 CB PHE B 316 96.319 -94.024 40.474 1.00124.99 C ANISOU 5671 CB PHE B 316 12867 18683 15939 3765 3634 5411 C ATOM 5672 CG PHE B 316 96.629 -95.269 41.274 1.00129.84 C ANISOU 5672 CG PHE B 316 13501 19348 16483 4026 3900 5863 C ATOM 5673 CD1 PHE B 316 97.918 -95.785 41.316 1.00132.60 C ANISOU 5673 CD1 PHE B 316 13975 19848 16559 4146 3758 5849 C ATOM 5674 CD2 PHE B 316 95.635 -95.915 42.001 1.00136.00 C ANISOU 5674 CD2 PHE B 316 14167 20029 17479 4165 4308 6321 C ATOM 5675 CE1 PHE B 316 98.203 -96.941 42.052 1.00136.91 C ANISOU 5675 CE1 PHE B 316 14541 20432 17046 4409 4010 6293 C ATOM 5676 CE2 PHE B 316 95.920 -97.072 42.735 1.00142.19 C ANISOU 5676 CE2 PHE B 316 14972 20840 18213 4419 4578 6778 C ATOM 5677 CZ PHE B 316 97.202 -97.578 42.755 1.00139.79 C ANISOU 5677 CZ PHE B 316 14804 20680 17631 4545 4422 6763 C ATOM 5678 N LEU B 317 96.220 -92.260 37.635 1.00115.56 N ANISOU 5678 N LEU B 317 11640 17064 15204 3051 2897 4502 N ATOM 5679 CA LEU B 317 95.855 -90.986 37.013 1.00113.03 C ANISOU 5679 CA LEU B 317 11309 16719 14916 2874 2703 4158 C ATOM 5680 C LEU B 317 95.191 -91.121 35.655 1.00115.93 C ANISOU 5680 C LEU B 317 11564 16691 15792 2570 2537 4066 C ATOM 5681 O LEU B 317 94.410 -90.242 35.284 1.00115.20 O ANISOU 5681 O LEU B 317 11403 16523 15844 2456 2480 3918 O ATOM 5682 CB LEU B 317 97.096 -90.094 36.827 1.00110.79 C ANISOU 5682 CB LEU B 317 11184 16685 14224 2867 2427 3786 C ATOM 5683 CG LEU B 317 97.759 -89.494 38.059 1.00116.89 C ANISOU 5683 CG LEU B 317 12066 17896 14452 3137 2492 3713 C ATOM 5684 CD1 LEU B 317 99.037 -88.778 37.669 1.00115.14 C ANISOU 5684 CD1 LEU B 317 11960 17846 13944 3071 2190 3338 C ATOM 5685 CD2 LEU B 317 96.838 -88.521 38.770 1.00120.44 C ANISOU 5685 CD2 LEU B 317 12478 18466 14816 3235 2650 3671 C ATOM 5686 N TYR B 318 95.545 -92.150 34.878 1.00112.36 N ANISOU 5686 N TYR B 318 11101 16004 15588 2447 2435 4118 N ATOM 5687 CA TYR B 318 95.032 -92.240 33.520 1.00111.16 C ANISOU 5687 CA TYR B 318 10859 15516 15859 2170 2227 3968 C ATOM 5688 C TYR B 318 94.243 -93.514 33.227 1.00118.55 C ANISOU 5688 C TYR B 318 11630 16097 17318 2082 2351 4220 C ATOM 5689 O TYR B 318 93.153 -93.415 32.662 1.00118.84 O ANISOU 5689 O TYR B 318 11502 15899 17752 1920 2324 4198 O ATOM 5690 CB TYR B 318 96.187 -92.097 32.515 1.00109.39 C ANISOU 5690 CB TYR B 318 10774 15308 15481 2050 1907 3674 C ATOM 5691 CG TYR B 318 96.885 -90.754 32.563 1.00109.35 C ANISOU 5691 CG TYR B 318 10898 15581 15070 2071 1752 3385 C ATOM 5692 CD1 TYR B 318 96.280 -89.614 32.043 1.00110.39 C ANISOU 5692 CD1 TYR B 318 11000 15671 15273 1946 1635 3184 C ATOM 5693 CD2 TYR B 318 98.158 -90.626 33.112 1.00109.74 C ANISOU 5693 CD2 TYR B 318 11085 15920 14691 2214 1718 3309 C ATOM 5694 CE1 TYR B 318 96.913 -88.375 32.087 1.00110.04 C ANISOU 5694 CE1 TYR B 318 11066 15837 14907 1956 1510 2923 C ATOM 5695 CE2 TYR B 318 98.803 -89.391 33.160 1.00109.25 C ANISOU 5695 CE2 TYR B 318 11117 16086 14306 2214 1575 3024 C ATOM 5696 CZ TYR B 318 98.179 -88.270 32.638 1.00116.16 C ANISOU 5696 CZ TYR B 318 11967 16883 15285 2078 1479 2834 C ATOM 5697 OH TYR B 318 98.804 -87.047 32.672 1.00116.58 O ANISOU 5697 OH TYR B 318 12106 17117 15072 2067 1353 2557 O ATOM 5698 N CYS B 319 94.781 -94.696 33.575 1.00117.05 N ANISOU 5698 N CYS B 319 11467 15849 17156 2182 2477 4446 N ATOM 5699 CA CYS B 319 94.125 -95.967 33.266 1.00119.18 C ANISOU 5699 CA CYS B 319 11578 15736 17967 2086 2594 4669 C ATOM 5700 C CYS B 319 92.968 -96.273 34.200 1.00127.66 C ANISOU 5700 C CYS B 319 12474 16733 19299 2178 2961 5032 C ATOM 5701 O CYS B 319 91.892 -96.649 33.720 1.00128.65 O ANISOU 5701 O CYS B 319 12389 16534 19957 2004 2995 5088 O ATOM 5702 CB CYS B 319 95.129 -97.115 33.256 1.00119.86 C ANISOU 5702 CB CYS B 319 11759 15754 18027 2164 2603 4781 C ATOM 5703 SG CYS B 319 94.434 -98.689 32.697 1.00126.25 S ANISOU 5703 SG CYS B 319 12383 16026 19559 2012 2700 4981 S ATOM 5704 N PHE B 320 93.189 -96.150 35.525 1.00126.63 N ANISOU 5704 N PHE B 320 12413 16904 18796 2458 3238 5281 N ATOM 5705 CA PHE B 320 92.180 -96.512 36.518 1.00130.19 C ANISOU 5705 CA PHE B 320 12707 17315 19443 2592 3642 5680 C ATOM 5706 C PHE B 320 91.002 -95.507 36.564 1.00135.64 C ANISOU 5706 C PHE B 320 13253 18029 20256 2523 3692 5599 C ATOM 5707 O PHE B 320 89.947 -95.857 37.086 1.00138.18 O ANISOU 5707 O PHE B 320 13380 18221 20901 2557 4003 5902 O ATOM 5708 CB PHE B 320 92.809 -96.737 37.913 1.00133.80 C ANISOU 5708 CB PHE B 320 13298 18117 19421 2950 3926 5984 C ATOM 5709 CG PHE B 320 93.908 -97.793 37.994 1.00135.45 C ANISOU 5709 CG PHE B 320 13630 18308 19526 3062 3920 6130 C ATOM 5710 CD1 PHE B 320 93.960 -98.852 37.084 1.00138.14 C ANISOU 5710 CD1 PHE B 320 13900 18231 20356 2868 3826 6145 C ATOM 5711 CD2 PHE B 320 94.878 -97.734 38.986 1.00137.88 C ANISOU 5711 CD2 PHE B 320 14115 19021 19253 3377 4004 6242 C ATOM 5712 CE1 PHE B 320 94.987 -99.807 37.147 1.00139.38 C ANISOU 5712 CE1 PHE B 320 14171 18361 20427 2986 3824 6272 C ATOM 5713 CE2 PHE B 320 95.895 -98.694 39.055 1.00140.97 C ANISOU 5713 CE2 PHE B 320 14608 19402 19551 3500 3992 6384 C ATOM 5714 CZ PHE B 320 95.942 -99.722 38.136 1.00138.84 C ANISOU 5714 CZ PHE B 320 14273 18700 19781 3305 3912 6405 C ATOM 5715 N VAL B 321 91.149 -94.310 35.962 1.00130.64 N ANISOU 5715 N VAL B 321 12694 17525 19417 2419 3396 5206 N ATOM 5716 CA VAL B 321 90.071 -93.306 35.892 1.00131.02 C ANISOU 5716 CA VAL B 321 12608 17577 19595 2354 3409 5099 C ATOM 5717 C VAL B 321 89.825 -92.896 34.410 1.00133.54 C ANISOU 5717 C VAL B 321 12870 17666 20203 2059 3028 4753 C ATOM 5718 O VAL B 321 89.363 -91.781 34.131 1.00131.63 O ANISOU 5718 O VAL B 321 12603 17492 19917 2009 2910 4545 O ATOM 5719 CB VAL B 321 90.305 -92.071 36.818 1.00134.79 C ANISOU 5719 CB VAL B 321 13223 18469 19522 2576 3485 4995 C ATOM 5720 CG1 VAL B 321 90.112 -92.426 38.290 1.00138.03 C ANISOU 5720 CG1 VAL B 321 13629 19099 19719 2881 3907 5369 C ATOM 5721 CG2 VAL B 321 91.661 -91.401 36.574 1.00131.76 C ANISOU 5721 CG2 VAL B 321 13089 18330 18643 2597 3190 4659 C ATOM 5722 N GLY B 322 90.115 -93.824 33.494 1.00130.67 N ANISOU 5722 N GLY B 322 12485 17032 20132 1887 2851 4706 N ATOM 5723 CA GLY B 322 89.976 -93.625 32.054 1.00128.70 C ANISOU 5723 CA GLY B 322 12197 16578 20127 1633 2484 4391 C ATOM 5724 C GLY B 322 88.545 -93.558 31.567 1.00134.13 C ANISOU 5724 C GLY B 322 12607 17017 21340 1473 2476 4400 C ATOM 5725 O GLY B 322 88.149 -92.591 30.900 1.00132.41 O ANISOU 5725 O GLY B 322 12362 16826 21120 1381 2258 4160 O ATOM 5726 N ASN B 323 87.766 -94.602 31.892 1.00133.64 N ANISOU 5726 N ASN B 323 12323 16702 21752 1443 2716 4686 N ATOM 5727 CA ASN B 323 86.360 -94.719 31.499 1.00135.76 C ANISOU 5727 CA ASN B 323 12273 16709 22602 1285 2735 4724 C ATOM 5728 C ASN B 323 85.505 -93.621 32.151 1.00139.93 C ANISOU 5728 C ASN B 323 12701 17425 23042 1393 2906 4786 C ATOM 5729 O ASN B 323 84.639 -93.050 31.483 1.00139.08 O ANISOU 5729 O ASN B 323 12422 17227 23194 1266 2738 4627 O ATOM 5730 CB ASN B 323 85.815 -96.105 31.864 1.00142.57 C ANISOU 5730 CB ASN B 323 12916 17257 23996 1243 3011 5051 C ATOM 5731 CG ASN B 323 86.575 -97.274 31.265 1.00172.59 C ANISOU 5731 CG ASN B 323 16796 20824 27955 1145 2874 5002 C ATOM 5732 OD1 ASN B 323 87.282 -97.154 30.255 1.00164.08 O ANISOU 5732 OD1 ASN B 323 15871 19749 26725 1044 2510 4670 O ATOM 5733 ND2 ASN B 323 86.433 -98.445 31.873 1.00169.78 N ANISOU 5733 ND2 ASN B 323 16333 20250 27924 1184 3183 5343 N ATOM 5734 N ARG B 324 85.782 -93.320 33.445 1.00137.28 N ANISOU 5734 N ARG B 324 12480 17366 22316 1646 3228 5004 N ATOM 5735 CA ARG B 324 85.113 -92.310 34.276 1.00137.78 C ANISOU 5735 CA ARG B 324 12488 17651 22210 1808 3447 5076 C ATOM 5736 C ARG B 324 85.210 -90.896 33.671 1.00137.59 C ANISOU 5736 C ARG B 324 12573 17780 21927 1772 3145 4707 C ATOM 5737 O ARG B 324 84.217 -90.171 33.688 1.00138.10 O ANISOU 5737 O ARG B 324 12469 17839 22165 1772 3192 4687 O ATOM 5738 CB ARG B 324 85.707 -92.311 35.697 1.00139.45 C ANISOU 5738 CB ARG B 324 12874 18176 21935 2109 3785 5315 C ATOM 5739 N PHE B 325 86.390 -90.518 33.134 1.00130.11 N ANISOU 5739 N PHE B 325 11891 16953 20592 1745 2851 4434 N ATOM 5740 CA PHE B 325 86.634 -89.211 32.520 1.00126.91 C ANISOU 5740 CA PHE B 325 11610 16670 19940 1707 2570 4101 C ATOM 5741 C PHE B 325 85.751 -88.986 31.289 1.00130.12 C ANISOU 5741 C PHE B 325 11828 16839 20773 1498 2307 3945 C ATOM 5742 O PHE B 325 85.137 -87.928 31.176 1.00129.29 O ANISOU 5742 O PHE B 325 11664 16785 20674 1519 2262 3839 O ATOM 5743 CB PHE B 325 88.113 -89.060 32.140 1.00125.71 C ANISOU 5743 CB PHE B 325 11749 16656 19358 1699 2332 3879 C ATOM 5744 N GLN B 326 85.676 -89.984 30.387 1.00126.94 N ANISOU 5744 N GLN B 326 11324 16180 20725 1312 2131 3925 N ATOM 5745 CA GLN B 326 84.896 -89.932 29.145 1.00126.75 C ANISOU 5745 CA GLN B 326 11117 15943 21100 1117 1838 3756 C ATOM 5746 C GLN B 326 83.374 -89.914 29.404 1.00132.86 C ANISOU 5746 C GLN B 326 11543 16584 22356 1099 2007 3917 C ATOM 5747 O GLN B 326 82.659 -89.135 28.764 1.00132.07 O ANISOU 5747 O GLN B 326 11323 16462 22396 1047 1821 3771 O ATOM 5748 CB GLN B 326 85.265 -91.121 28.241 1.00128.18 C ANISOU 5748 CB GLN B 326 11285 15896 21522 947 1630 3680 C ATOM 5749 N GLN B 327 82.891 -90.771 30.335 1.00131.57 N ANISOU 5749 N GLN B 327 11208 16332 22449 1151 2368 4232 N ATOM 5750 CA GLN B 327 81.477 -90.890 30.699 1.00134.10 C ANISOU 5750 CA GLN B 327 11170 16519 23264 1137 2592 4432 C ATOM 5751 C GLN B 327 80.946 -89.621 31.380 1.00136.63 C ANISOU 5751 C GLN B 327 11475 17065 23374 1315 2761 4457 C ATOM 5752 O GLN B 327 79.796 -89.248 31.141 1.00137.75 O ANISOU 5752 O GLN B 327 11340 17118 23881 1271 2754 4459 O ATOM 5753 CB GLN B 327 81.253 -92.105 31.610 1.00138.56 C ANISOU 5753 CB GLN B 327 11592 16950 24104 1174 2986 4802 C ATOM 5754 N LYS B 328 81.773 -88.965 32.218 1.00130.74 N ANISOU 5754 N LYS B 328 11014 16606 22057 1519 2904 4457 N ATOM 5755 CA LYS B 328 81.386 -87.742 32.923 1.00130.51 C ANISOU 5755 CA LYS B 328 11006 16795 21785 1708 3069 4442 C ATOM 5756 C LYS B 328 81.514 -86.494 32.020 1.00131.58 C ANISOU 5756 C LYS B 328 11253 16979 21762 1660 2713 4105 C ATOM 5757 O LYS B 328 80.874 -85.479 32.303 1.00131.41 O ANISOU 5757 O LYS B 328 11164 17042 21722 1769 2794 4068 O ATOM 5758 CB LYS B 328 82.203 -87.565 34.209 1.00132.72 C ANISOU 5758 CB LYS B 328 11535 17368 21525 1956 3354 4550 C ATOM 5759 N LEU B 329 82.321 -86.576 30.934 1.00125.80 N ANISOU 5759 N LEU B 329 10685 16186 20928 1509 2339 3876 N ATOM 5760 CA LEU B 329 82.510 -85.480 29.973 1.00123.37 C ANISOU 5760 CA LEU B 329 10491 15905 20478 1459 2002 3590 C ATOM 5761 C LEU B 329 81.371 -85.464 28.956 1.00128.54 C ANISOU 5761 C LEU B 329 10861 16360 21618 1321 1785 3541 C ATOM 5762 O LEU B 329 80.881 -84.387 28.612 1.00127.95 O ANISOU 5762 O LEU B 329 10751 16317 21548 1365 1675 3430 O ATOM 5763 CB LEU B 329 83.876 -85.595 29.257 1.00120.30 C ANISOU 5763 CB LEU B 329 10395 15557 19758 1375 1723 3391 C ATOM 5764 CG LEU B 329 84.499 -84.342 28.602 1.00122.10 C ANISOU 5764 CG LEU B 329 10842 15885 19666 1380 1469 3130 C ATOM 5765 CD1 LEU B 329 84.086 -84.186 27.149 1.00121.76 C ANISOU 5765 CD1 LEU B 329 10713 15691 19858 1232 1112 2983 C ATOM 5766 CD2 LEU B 329 84.285 -83.072 29.425 1.00124.47 C ANISOU 5766 CD2 LEU B 329 11195 16339 19761 1555 1650 3103 C ATOM 5767 N ARG B 330 80.946 -86.660 28.484 1.00126.57 N ANISOU 5767 N ARG B 330 10401 15901 21790 1163 1720 3616 N ATOM 5768 CA ARG B 330 79.839 -86.825 27.534 1.00127.92 C ANISOU 5768 CA ARG B 330 10259 15881 22464 1023 1495 3556 C ATOM 5769 C ARG B 330 78.488 -86.498 28.211 1.00134.35 C ANISOU 5769 C ARG B 330 10746 16674 23629 1107 1762 3740 C ATOM 5770 O ARG B 330 77.474 -86.357 27.523 1.00135.83 O ANISOU 5770 O ARG B 330 10650 16747 24211 1030 1585 3684 O ATOM 5771 CB ARG B 330 79.833 -88.250 26.952 1.00129.23 C ANISOU 5771 CB ARG B 330 10290 15819 22991 831 1370 3559 C ATOM 5772 N SER B 331 78.494 -86.355 29.558 1.00131.11 N ANISOU 5772 N SER B 331 10372 16393 23050 1282 2183 3953 N ATOM 5773 CA SER B 331 77.337 -86.024 30.392 1.00133.46 C ANISOU 5773 CA SER B 331 10395 16712 23602 1406 2514 4154 C ATOM 5774 C SER B 331 77.132 -84.502 30.479 1.00135.30 C ANISOU 5774 C SER B 331 10716 17108 23585 1568 2485 4019 C ATOM 5775 O SER B 331 76.026 -84.028 30.212 1.00136.64 O ANISOU 5775 O SER B 331 10610 17216 24093 1579 2457 4024 O ATOM 5776 CB SER B 331 77.505 -86.620 31.790 1.00138.57 C ANISOU 5776 CB SER B 331 11069 17446 24136 1547 2989 4450 C ATOM 5777 OG SER B 331 76.493 -86.188 32.684 1.00150.36 O ANISOU 5777 OG SER B 331 12340 19007 25781 1708 3348 4643 O ATOM 5778 N VAL B 332 78.196 -83.745 30.854 1.00128.76 N ANISOU 5778 N VAL B 332 10257 16476 22189 1694 2492 3893 N ATOM 5779 CA VAL B 332 78.193 -82.279 31.021 1.00147.18 C ANISOU 5779 CA VAL B 332 12724 18947 24250 1854 2483 3743 C ATOM 5780 C VAL B 332 77.975 -81.579 29.664 1.00152.08 C ANISOU 5780 C VAL B 332 13322 19465 24995 1752 2068 3531 C ATOM 5781 O VAL B 332 77.252 -80.587 29.588 1.00104.72 O ANISOU 5781 O VAL B 332 7220 13472 19096 1853 2064 3489 O ATOM 5782 CB VAL B 332 79.493 -81.773 31.718 1.00148.89 C ANISOU 5782 CB VAL B 332 13332 19376 23862 1982 2566 3632 C ATOM 5783 CG1 VAL B 332 79.530 -80.252 31.825 1.00148.10 C ANISOU 5783 CG1 VAL B 332 13371 19374 23527 2125 2537 3441 C ATOM 5784 CG2 VAL B 332 79.658 -82.394 33.101 1.00150.26 C ANISOU 5784 CG2 VAL B 332 13530 19696 23868 2131 2976 3852 C TER 5785 VAL B 332 HETATM 5786 N1 8EM A1501 107.434 -74.005 4.783 1.00 54.22 N ANISOU 5786 N1 8EM A1501 5435 5628 9540 -233 -432 -127 N HETATM 5787 N3 8EM A1501 102.828 -70.418 7.519 1.00 76.88 N ANISOU 5787 N3 8EM A1501 8031 8501 12678 -66 -303 -206 N HETATM 5788 C4 8EM A1501 110.211 -75.937 4.687 1.00 47.00 C ANISOU 5788 C4 8EM A1501 4618 4729 8510 -243 -398 -114 C HETATM 5789 C5 8EM A1501 111.452 -76.546 5.297 1.00 46.52 C ANISOU 5789 C5 8EM A1501 4564 4699 8412 -225 -371 -109 C HETATM 5790 C6 8EM A1501 106.120 -73.850 4.318 1.00 54.66 C ANISOU 5790 C6 8EM A1501 5456 5674 9637 -239 -457 -94 C HETATM 5791 C7 8EM A1501 108.292 -72.803 4.811 1.00 55.20 C ANISOU 5791 C7 8EM A1501 5550 5719 9704 -217 -424 -164 C HETATM 5792 C8 8EM A1501 107.917 -71.789 5.872 1.00 54.92 C ANISOU 5792 C8 8EM A1501 5462 5686 9720 -188 -403 -234 C HETATM 5793 C10 8EM A1501 107.904 -69.509 6.653 1.00 54.07 C ANISOU 5793 C10 8EM A1501 5280 5492 9771 -150 -375 -362 C HETATM 5794 C13 8EM A1501 105.436 -68.523 9.127 1.00 69.80 C ANISOU 5794 C13 8EM A1501 7177 7566 11778 -29 -280 -521 C HETATM 5795 C15 8EM A1501 105.149 -67.426 9.948 1.00 69.79 C ANISOU 5795 C15 8EM A1501 7140 7537 11838 21 -240 -650 C HETATM 5796 C17 8EM A1501 107.488 -66.949 10.156 1.00 69.20 C ANISOU 5796 C17 8EM A1501 7090 7429 11775 -37 -309 -809 C HETATM 5797 C20 8EM A1501 107.195 -72.145 7.012 1.00 55.76 C ANISOU 5797 C20 8EM A1501 5542 5859 9787 -163 -378 -262 C HETATM 5798 C21 8EM A1501 104.979 -77.331 5.116 1.00 54.79 C ANISOU 5798 C21 8EM A1501 5455 5715 9649 -305 -430 -30 C HETATM 5799 C22 8EM A1501 103.632 -77.250 4.803 1.00 58.33 C ANISOU 5799 C22 8EM A1501 5840 6155 10166 -328 -463 -9 C HETATM 5800 C24 8EM A1501 103.909 -74.950 4.131 1.00 58.02 C ANISOU 5800 C24 8EM A1501 5809 6120 10115 -277 -495 -35 C HETATM 5801 C26 8EM A1501 100.955 -75.608 6.395 1.00 63.07 C ANISOU 5801 C26 8EM A1501 6239 6822 10904 -248 -388 59 C HETATM 5802 C28 8EM A1501 100.248 -75.845 8.697 1.00 64.33 C ANISOU 5802 C28 8EM A1501 6313 7079 11052 -158 -226 113 C HETATM 5803 O1 8EM A1501 99.546 -76.292 4.669 1.00 68.58 O ANISOU 5803 O1 8EM A1501 6865 7478 11714 -341 -522 101 O HETATM 5804 C25 8EM A1501 100.690 -76.005 4.970 1.00 64.90 C ANISOU 5804 C25 8EM A1501 6478 7016 11165 -311 -487 63 C HETATM 5805 C31 8EM A1501 102.093 -74.927 6.840 1.00 63.72 C ANISOU 5805 C31 8EM A1501 6383 6921 10909 -208 -361 -1 C HETATM 5806 C30 8EM A1501 102.295 -74.703 8.195 1.00 65.33 C ANISOU 5806 C30 8EM A1501 6575 7186 11063 -148 -285 -26 C HETATM 5807 C29 8EM A1501 101.376 -75.166 9.125 1.00 65.59 C ANISOU 5807 C29 8EM A1501 6541 7270 11112 -117 -216 31 C HETATM 5808 C27 8EM A1501 100.032 -76.062 7.344 1.00 62.65 C ANISOU 5808 C27 8EM A1501 6106 6800 10900 -230 -321 116 C HETATM 5809 N6 8EM A1501 101.680 -75.974 4.024 1.00 63.12 N ANISOU 5809 N6 8EM A1501 6338 6773 10871 -328 -536 24 N HETATM 5810 C32 8EM A1501 101.284 -76.040 2.622 1.00 64.67 C ANISOU 5810 C32 8EM A1501 6537 6968 11066 -363 -635 23 C HETATM 5811 C33 8EM A1501 101.462 -77.419 2.088 1.00 67.78 C ANISOU 5811 C33 8EM A1501 6967 7337 11449 -424 -675 -15 C HETATM 5812 O2 8EM A1501 100.704 -78.405 2.659 1.00 69.27 O ANISOU 5812 O2 8EM A1501 7089 7496 11734 -466 -658 0 O HETATM 5813 C36 8EM A1501 101.054 -79.573 2.028 1.00 68.99 C ANISOU 5813 C36 8EM A1501 7099 7414 11700 -520 -695 -55 C HETATM 5814 C35 8EM A1501 101.980 -79.345 1.114 1.00 68.16 C ANISOU 5814 C35 8EM A1501 7090 7325 11483 -504 -730 -105 C HETATM 5815 C34 8EM A1501 102.250 -77.946 1.142 1.00 68.40 C ANISOU 5815 C34 8EM A1501 7129 7407 11454 -443 -715 -66 C HETATM 5816 C23 8EM A1501 103.080 -76.056 4.323 1.00 60.69 C ANISOU 5816 C23 8EM A1501 6112 6463 10487 -311 -499 -11 C HETATM 5817 C1 8EM A1501 105.807 -76.221 4.952 1.00 53.81 C ANISOU 5817 C1 8EM A1501 5360 5598 9488 -277 -436 -65 C HETATM 5818 C 8EM A1501 105.266 -75.035 4.443 1.00 55.22 C ANISOU 5818 C 8EM A1501 5512 5765 9704 -266 -465 -67 C HETATM 5819 O 8EM A1501 105.760 -72.798 3.815 1.00 55.49 O ANISOU 5819 O 8EM A1501 5536 5751 9796 -223 -469 -79 O HETATM 5820 C2 8EM A1501 107.865 -75.246 5.262 1.00 53.26 C ANISOU 5820 C2 8EM A1501 5337 5537 9364 -241 -414 -119 C HETATM 5821 C3 8EM A1501 109.272 -75.379 5.736 1.00 49.32 C ANISOU 5821 C3 8EM A1501 4857 5059 8822 -227 -394 -140 C HETATM 5822 N 8EM A1501 107.137 -76.311 5.353 1.00 54.27 N ANISOU 5822 N 8EM A1501 5457 5670 9493 -259 -409 -85 N HETATM 5823 C19 8EM A1501 106.830 -71.196 7.952 1.00 56.26 C ANISOU 5823 C19 8EM A1501 5563 5932 9880 -124 -352 -344 C HETATM 5824 C11 8EM A1501 107.168 -69.854 7.786 1.00 56.95 C ANISOU 5824 C11 8EM A1501 5630 5939 10071 -118 -353 -410 C HETATM 5825 C9 8EM A1501 108.273 -70.458 5.719 1.00 52.47 C ANISOU 5825 C9 8EM A1501 5123 5304 9508 -179 -397 -271 C HETATM 5826 C12 8EM A1501 106.774 -68.819 8.785 1.00 64.13 C ANISOU 5826 C12 8EM A1501 6496 6842 11029 -73 -322 -529 C HETATM 5827 C18 8EM A1501 107.786 -68.021 9.331 1.00 67.09 C ANISOU 5827 C18 8EM A1501 6859 7190 11441 -76 -334 -664 C HETATM 5828 C16 8EM A1501 106.176 -66.650 10.458 1.00 69.89 C ANISOU 5828 C16 8EM A1501 7152 7517 11885 16 -256 -804 C HETATM 5829 C14 8EM A1501 104.256 -69.371 8.708 1.00 74.47 C ANISOU 5829 C14 8EM A1501 7755 8193 12348 -30 -272 -390 C HETATM 5830 N5 8EM A1501 103.369 -69.905 9.560 1.00 76.21 N ANISOU 5830 N5 8EM A1501 7947 8498 12512 8 -227 -374 N HETATM 5831 N4 8EM A1501 102.483 -70.557 8.776 1.00 77.51 N ANISOU 5831 N4 8EM A1501 8088 8651 12711 -21 -245 -251 N HETATM 5832 N2 8EM A1501 103.953 -69.668 7.440 1.00 75.97 N ANISOU 5832 N2 8EM A1501 7949 8337 12579 -68 -312 -278 N HETATM 5833 N1 8EM B1501 117.592 -89.460 36.963 1.00108.33 N ANISOU 5833 N1 8EM B1501 10862 19885 10416 3596 -262 1087 N HETATM 5834 N3 8EM B1501 122.998 -88.050 33.755 1.00117.64 N ANISOU 5834 N3 8EM B1501 11340 21262 12096 2908 -876 57 N HETATM 5835 C4 8EM B1501 114.482 -90.748 37.408 1.00103.22 C ANISOU 5835 C4 8EM B1501 10509 18716 9994 3745 263 1849 C HETATM 5836 C5 8EM B1501 113.191 -91.334 36.906 1.00101.28 C ANISOU 5836 C5 8EM B1501 10350 18062 10068 3650 469 2137 C HETATM 5837 C6 8EM B1501 118.870 -89.350 37.531 1.00110.09 C ANISOU 5837 C6 8EM B1501 10941 20504 10383 3747 -447 896 C HETATM 5838 C7 8EM B1501 117.004 -88.248 36.363 1.00109.57 C ANISOU 5838 C7 8EM B1501 11039 19812 10779 3282 -278 839 C HETATM 5839 C8 8EM B1501 117.658 -87.812 35.070 1.00110.71 C ANISOU 5839 C8 8EM B1501 11115 19754 11197 2981 -371 643 C HETATM 5840 C10 8EM B1501 118.185 -86.057 33.495 1.00109.26 C ANISOU 5840 C10 8EM B1501 10835 19292 11389 2458 -497 191 C HETATM 5841 C13 8EM B1501 120.953 -86.538 31.200 1.00109.94 C ANISOU 5841 C13 8EM B1501 10650 19335 11787 2194 -628 38 C HETATM 5842 C15 8EM B1501 121.506 -85.914 30.077 1.00109.01 C ANISOU 5842 C15 8EM B1501 10462 19067 11891 1941 -632 -99 C HETATM 5843 C17 8EM B1501 119.329 -85.207 29.374 1.00105.86 C ANISOU 5843 C17 8EM B1501 10341 18166 11717 1718 -477 33 C HETATM 5844 C20 8EM B1501 118.365 -88.701 34.267 1.00110.80 C ANISOU 5844 C20 8EM B1501 11092 19676 11329 2974 -375 765 C HETATM 5845 C21 8EM B1501 119.291 -93.002 38.326 1.00111.64 C ANISOU 5845 C21 8EM B1501 11226 20813 10379 4505 -176 1891 C HETATM 5846 C22 8EM B1501 120.598 -93.027 38.788 1.00113.83 C ANISOU 5846 C22 8EM B1501 11355 21490 10404 4691 -367 1748 C HETATM 5847 C24 8EM B1501 120.762 -90.632 38.501 1.00112.93 C ANISOU 5847 C24 8EM B1501 11120 21459 10327 4240 -620 1016 C HETATM 5848 C26 8EM B1501 123.658 -92.599 37.096 1.00114.70 C ANISOU 5848 C26 8EM B1501 11044 21771 10764 4395 -782 1153 C HETATM 5849 C28 8EM B1501 124.453 -93.827 35.172 1.00113.16 C ANISOU 5849 C28 8EM B1501 10819 21140 11037 4246 -681 1313 C HETATM 5850 O1 8EM B1501 124.774 -92.781 39.138 1.00121.13 O ANISOU 5850 O1 8EM B1501 11681 23415 10928 4962 -1022 1115 O HETATM 5851 C25 8EM B1501 123.735 -92.452 38.592 1.00117.46 C ANISOU 5851 C25 8EM B1501 11364 22582 10685 4715 -876 1144 C HETATM 5852 C31 8EM B1501 122.726 -91.967 36.270 1.00112.30 C ANISOU 5852 C31 8EM B1501 10854 21083 10734 4057 -685 1076 C HETATM 5853 C30 8EM B1501 122.665 -92.265 34.917 1.00109.98 C ANISOU 5853 C30 8EM B1501 10601 20403 10784 3825 -599 1122 C HETATM 5854 C29 8EM B1501 123.523 -93.196 34.369 1.00110.93 C ANISOU 5854 C29 8EM B1501 10655 20502 10993 3920 -596 1231 C HETATM 5855 C27 8EM B1501 124.528 -93.531 36.524 1.00115.24 C ANISOU 5855 C27 8EM B1501 11036 21805 10944 4484 -781 1279 C HETATM 5856 N6 8EM B1501 122.713 -91.887 39.305 1.00117.17 N ANISOU 5856 N6 8EM B1501 11447 22576 10495 4733 -812 1135 N HETATM 5857 C32 8EM B1501 122.990 -91.451 40.671 1.00121.02 C ANISOU 5857 C32 8EM B1501 11873 23570 10540 5007 -959 990 C HETATM 5858 C33 8EM B1501 122.497 -92.460 41.649 1.00123.70 C ANISOU 5858 C33 8EM B1501 12338 24071 10592 5417 -805 1420 C HETATM 5859 O2 8EM B1501 123.077 -93.698 41.599 1.00125.05 O ANISOU 5859 O2 8EM B1501 12486 24271 10757 5661 -758 1744 O HETATM 5860 C36 8EM B1501 122.461 -94.454 42.565 1.00127.77 C ANISOU 5860 C36 8EM B1501 12962 24744 10842 6023 -587 2143 C HETATM 5861 C35 8EM B1501 121.539 -93.738 43.196 1.00127.96 C ANISOU 5861 C35 8EM B1501 13083 24835 10699 6013 -525 2072 C HETATM 5862 C34 8EM B1501 121.558 -92.437 42.606 1.00125.26 C ANISOU 5862 C34 8EM B1501 12674 24387 10533 5621 -674 1590 C HETATM 5863 C23 8EM B1501 121.349 -91.847 38.866 1.00114.61 C ANISOU 5863 C23 8EM B1501 11310 21841 10397 4553 -598 1301 C HETATM 5864 C1 8EM B1501 118.711 -91.795 37.922 1.00110.25 C ANISOU 5864 C1 8EM B1501 11068 20489 10333 4197 -211 1606 C HETATM 5865 C 8EM B1501 119.452 -90.611 38.017 1.00111.09 C ANISOU 5865 C 8EM B1501 11048 20830 10330 4071 -425 1178 C HETATM 5866 O 8EM B1501 119.415 -88.261 37.629 1.00110.54 O ANISOU 5866 O 8EM B1501 10892 20717 10392 3619 -613 522 O HETATM 5867 C2 8EM B1501 116.950 -90.697 36.942 1.00105.88 C ANISOU 5867 C2 8EM B1501 10651 19392 10185 3741 -74 1497 C HETATM 5868 C3 8EM B1501 115.580 -90.783 36.361 1.00102.26 C ANISOU 5868 C3 8EM B1501 10310 18522 10020 3571 102 1668 C HETATM 5869 N 8EM B1501 117.428 -91.814 37.382 1.00107.90 N ANISOU 5869 N 8EM B1501 10897 19790 10308 4016 -34 1753 N HETATM 5870 C19 8EM B1501 118.974 -88.275 33.096 1.00109.55 C ANISOU 5870 C19 8EM B1501 10871 19359 11392 2719 -438 594 C HETATM 5871 C11 8EM B1501 118.905 -86.940 32.690 1.00109.08 C ANISOU 5871 C11 8EM B1501 10778 19209 11459 2457 -495 316 C HETATM 5872 C9 8EM B1501 117.571 -86.488 34.658 1.00110.48 C ANISOU 5872 C9 8EM B1501 11054 19620 11304 2717 -438 341 C HETATM 5873 C12 8EM B1501 119.561 -86.466 31.436 1.00108.35 C ANISOU 5873 C12 8EM B1501 10618 18951 11600 2197 -531 172 C HETATM 5874 C18 8EM B1501 118.766 -85.807 30.490 1.00106.62 C ANISOU 5874 C18 8EM B1501 10492 18401 11618 1951 -462 159 C HETATM 5875 C16 8EM B1501 120.692 -85.251 29.173 1.00106.89 C ANISOU 5875 C16 8EM B1501 10305 18473 11834 1710 -549 -92 C HETATM 5876 C14 8EM B1501 121.915 -87.320 32.067 1.00113.07 C ANISOU 5876 C14 8EM B1501 10926 20093 11945 2472 -717 65 C HETATM 5877 N5 8EM B1501 122.712 -88.300 31.615 1.00112.81 N ANISOU 5877 N5 8EM B1501 10836 20098 11928 2574 -709 191 N HETATM 5878 N4 8EM B1501 123.378 -88.739 32.706 1.00115.77 N ANISOU 5878 N4 8EM B1501 11104 20839 12044 2848 -808 191 N HETATM 5879 N2 8EM B1501 122.069 -87.134 33.381 1.00116.24 N ANISOU 5879 N2 8EM B1501 11264 20825 12077 2669 -815 -32 N CONECT 1439 1954 CONECT 1954 1439 CONECT 4274 4803 CONECT 4803 4274 CONECT 5786 5790 5791 5820 CONECT 5787 5831 5832 CONECT 5788 5789 5821 CONECT 5789 5788 CONECT 5790 5786 5818 5819 CONECT 5791 5786 5792 CONECT 5792 5791 5797 5825 CONECT 5793 5824 5825 CONECT 5794 5795 5826 5829 CONECT 5795 5794 5828 CONECT 5796 5827 5828 CONECT 5797 5792 5823 CONECT 5798 5799 5817 CONECT 5799 5798 5816 CONECT 5800 5816 5818 CONECT 5801 5804 5805 5808 CONECT 5802 5807 5808 CONECT 5803 5804 CONECT 5804 5801 5803 5809 CONECT 5805 5801 5806 CONECT 5806 5805 5807 CONECT 5807 5802 5806 CONECT 5808 5801 5802 CONECT 5809 5804 5810 5816 CONECT 5810 5809 5811 CONECT 5811 5810 5812 5815 CONECT 5812 5811 5813 CONECT 5813 5812 5814 CONECT 5814 5813 5815 CONECT 5815 5811 5814 CONECT 5816 5799 5800 5809 CONECT 5817 5798 5818 5822 CONECT 5818 5790 5800 5817 CONECT 5819 5790 CONECT 5820 5786 5821 5822 CONECT 5821 5788 5820 CONECT 5822 5817 5820 CONECT 5823 5797 5824 CONECT 5824 5793 5823 5826 CONECT 5825 5792 5793 CONECT 5826 5794 5824 5827 CONECT 5827 5796 5826 CONECT 5828 5795 5796 CONECT 5829 5794 5830 5832 CONECT 5830 5829 5831 CONECT 5831 5787 5830 CONECT 5832 5787 5829 CONECT 5833 5837 5838 5867 CONECT 5834 5878 5879 CONECT 5835 5836 5868 CONECT 5836 5835 CONECT 5837 5833 5865 5866 CONECT 5838 5833 5839 CONECT 5839 5838 5844 5872 CONECT 5840 5871 5872 CONECT 5841 5842 5873 5876 CONECT 5842 5841 5875 CONECT 5843 5874 5875 CONECT 5844 5839 5870 CONECT 5845 5846 5864 CONECT 5846 5845 5863 CONECT 5847 5863 5865 CONECT 5848 5851 5852 5855 CONECT 5849 5854 5855 CONECT 5850 5851 CONECT 5851 5848 5850 5856 CONECT 5852 5848 5853 CONECT 5853 5852 5854 CONECT 5854 5849 5853 CONECT 5855 5848 5849 CONECT 5856 5851 5857 5863 CONECT 5857 5856 5858 CONECT 5858 5857 5859 5862 CONECT 5859 5858 5860 CONECT 5860 5859 5861 CONECT 5861 5860 5862 CONECT 5862 5858 5861 CONECT 5863 5846 5847 5856 CONECT 5864 5845 5865 5869 CONECT 5865 5837 5847 5864 CONECT 5866 5837 CONECT 5867 5833 5868 5869 CONECT 5868 5835 5867 CONECT 5869 5864 5867 CONECT 5870 5844 5871 CONECT 5871 5840 5870 5873 CONECT 5872 5839 5840 CONECT 5873 5841 5871 5874 CONECT 5874 5843 5873 CONECT 5875 5842 5843 CONECT 5876 5841 5877 5879 CONECT 5877 5876 5878 CONECT 5878 5834 5877 CONECT 5879 5834 5876 MASTER 444 0 2 33 4 0 8 6 5877 2 98 64 END