HEADER SIGNALING PROTEIN 30-JAN-17 5UNG TITLE XFEL STRUCTURE OF HUMAN ANGIOTENSIN II TYPE 2 RECEPTOR (ORTHORHOMBIC TITLE 2 FORM) IN COMPLEX WITH COMPOUND 1 (N-BENZYL-N-(2-ETHYL-4-OXO-3-{[2'- TITLE 3 (2H-TETRAZOL-5-YL)[1,1'-BIPHENYL]-4-YL] METHYL}-3,4- TITLE 4 DIHYDROQUINAZOLIN-6-YL)THIOPHENE-2-CARBOXAMIDE) COMPND MOL_ID: 1; COMPND 2 MOLECULE: CHIMERA PROTEIN OF TYPE-2 ANGIOTENSIN II RECEPTOR AND COMPND 3 SOLUBLE CYTOCHROME B562; COMPND 4 CHAIN: B; COMPND 5 FRAGMENT: UNP P0ABE7 RESIDUES 23-128 AND UNP P50052 35-335 LINKED VIA COMPND 6 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 KEYWDS HUMAN ANGIOTENSIN II RECEPTOR COMPLEX, GPCR SIGNALING, GPCR, BRIL, KEYWDS 2 MEMBRANE PROTEIN, LCP, XFEL, BLOOD PRESSURE REGULATION, ORTHORHOMBIC KEYWDS 3 CRYSTAL, COMPOUND 1 (CPD 1), 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 3 28-NOV-18 5UNG 1 REMARK REVDAT 2 10-MAY-17 5UNG 1 JRNL REMARK REVDAT 1 05-APR-17 5UNG 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. 2.80 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) : 2.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.96 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 13269 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) : 0.242 REMARK 3 R VALUE (WORKING SET) : 0.241 REMARK 3 FREE R VALUE : 0.262 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.210 REMARK 3 FREE R VALUE TEST SET COUNT : 691 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 : 7 REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.02 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.89 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2693 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2400 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2544 REMARK 3 BIN R VALUE (WORKING SET) : 0.2390 REMARK 3 BIN FREE R VALUE : 0.2630 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.53 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 149 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 : 3195 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 70 REMARK 3 SOLVENT ATOMS : 1 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 80.91 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 82.84 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -2.17680 REMARK 3 B22 (A**2) : 4.93740 REMARK 3 B33 (A**2) : -2.76060 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.490 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 2.894 REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.357 REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 2.685 REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.363 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 : 0.912 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.881 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 3351 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 4557 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 1105 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : 61 ; 2.000 ; HARMONIC REMARK 3 GENERAL PLANES : 483 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 3351 ; 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 : 441 ; 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 : 3803 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.009 REMARK 3 BOND ANGLES (DEGREES) : 0.92 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 1.81 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 20.37 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 2 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: { B| 1001 - 1110 } REMARK 3 ORIGIN FOR THE GROUP (A): 22.6292 36.8452 -13.5705 REMARK 3 T TENSOR REMARK 3 T11: -0.0262 T22: -0.1488 REMARK 3 T33: -0.0310 T12: -0.0029 REMARK 3 T13: 0.0075 T23: -0.0382 REMARK 3 L TENSOR REMARK 3 L11: 1.3494 L22: 2.9298 REMARK 3 L33: 3.5237 L12: 0.7639 REMARK 3 L13: 1.7428 L23: -0.3012 REMARK 3 S TENSOR REMARK 3 S11: -0.0137 S12: 0.0173 S13: -0.0525 REMARK 3 S21: -0.0295 S22: 0.0197 S23: 0.1097 REMARK 3 S31: -0.0332 S32: 0.0294 S33: -0.0061 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: { B| 35 - 334 } REMARK 3 ORIGIN FOR THE GROUP (A): 9.7938 -1.6740 -19.1740 REMARK 3 T TENSOR REMARK 3 T11: -0.2334 T22: -0.2102 REMARK 3 T33: -0.0545 T12: -0.0055 REMARK 3 T13: -0.0540 T23: 0.0207 REMARK 3 L TENSOR REMARK 3 L11: 1.3717 L22: 3.2587 REMARK 3 L33: 1.9040 L12: 0.6911 REMARK 3 L13: 0.0630 L23: 0.0219 REMARK 3 S TENSOR REMARK 3 S11: 0.0973 S12: -0.1024 S13: 0.0360 REMARK 3 S21: 0.2630 S22: 0.0820 S23: 0.0795 REMARK 3 S31: 0.0691 S32: -0.1515 S33: -0.1793 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 5UNG 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_1000226079. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 09-DEC-15 REMARK 200 TEMPERATURE (KELVIN) : 294 REMARK 200 PH : 8.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : FREE ELECTRON LASER REMARK 200 BEAMLINE : CXI REMARK 200 X-RAY GENERATOR MODEL : SLAC LCLS BEAMLINE CXI REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.3 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : K-B MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : CS-PAD CXI-1 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTFEL REMARK 200 DATA SCALING SOFTWARE : CRYSTFEL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13330 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800 REMARK 200 RESOLUTION RANGE LOW (A) : 28.960 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 85.50 REMARK 200 R MERGE (I) : 0.14800 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 4.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 27.20 REMARK 200 R MERGE FOR SHELL (I) : 1.24000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.000 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 (%): 55.75 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78 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 21 2 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,-Y,-Z+1/2 REMARK 290 4555 -X+1/2,-Y,Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 35.13000 REMARK 290 SMTRY2 3 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 46.70500 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 35.13000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 46.70500 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 300 REMARK: AUTHORS STATE THAT THE BIOLOGICAL UNIT IS UNKNOWN REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 330 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20630 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 LYS B1042 CE NZ REMARK 470 SER B 36 OG REMARK 470 LYS B 38 CG CD CE NZ REMARK 470 ASP B 41 CG OD1 OD2 REMARK 470 HIS B 43 CG ND1 CD2 CE1 NE2 REMARK 470 LEU B 44 CG CD1 CD2 REMARK 470 GLN B 72 CG CD OE1 NE2 REMARK 470 LYS B 77 CG CD CE NZ REMARK 470 ARG B 154 CD NE CZ NH1 NH2 REMARK 470 ARG B 155 CZ NH1 NH2 REMARK 470 TRP B 158 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP B 158 CZ3 CH2 REMARK 470 GLU B 188 CG CD OE1 OE2 REMARK 470 THR B 241 OG1 CG2 REMARK 470 GLN B 326 CG CD OE1 NE2 REMARK 470 ARG B 330 CG CD NE CZ NH1 NH2 REMARK 470 PHE B 333 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG B 334 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 GLN B 72 -10.03 -153.37 REMARK 500 LYS B 73 -62.72 -133.55 REMARK 500 LYS B 77 142.35 70.76 REMARK 500 LEU B 111 43.75 -106.71 REMARK 500 PRO B 157 59.27 -94.07 REMARK 500 PHE B 220 -51.38 -140.15 REMARK 500 ASN B 242 71.61 56.83 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 OLC B 1202 REMARK 610 OLA B 1203 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue 8ES B 1201 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC B 1202 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 5UNF RELATED DB: PDB REMARK 900 RELATED ID: 5UNH RELATED DB: PDB DBREF 5UNG B 1001 1106 UNP P0ABE7 C562_ECOLX 23 128 DBREF 5UNG B 35 335 UNP P50052 AGTR2_HUMAN 35 335 SEQADV 5UNG TRP B 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION SEQADV 5UNG ILE B 1102 UNP P0ABE7 HIS 124 ENGINEERED MUTATION SEQADV 5UNG LEU B 1106 UNP P0ABE7 ARG 128 ENGINEERED MUTATION SEQADV 5UNG GLY B 1107 UNP P0ABE7 LINKER SEQADV 5UNG SER B 1108 UNP P0ABE7 LINKER SEQADV 5UNG GLY B 1109 UNP P0ABE7 LINKER SEQADV 5UNG SER B 1110 UNP P0ABE7 LINKER 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 8ES B1201 46 HET OLC B1202 14 HET OLA B1203 10 HETNAM 8ES N-BENZYL-N-(2-ETHYL-4-OXO-3-{[2'-(2H-TETRAZOL-5-YL)[1, HETNAM 2 8ES 1'-BIPHENYL]-4-YL]METHYL}-3,4-DIHYDROQUINAZOLIN-6-YL) HETNAM 3 8ES THIOPHENE-2-CARBOXAMIDE HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETNAM OLA OLEIC ACID HETSYN OLC 1-OLEOYL-R-GLYCEROL FORMUL 2 8ES C36 H29 N7 O2 S FORMUL 3 OLC C21 H40 O4 FORMUL 4 OLA C18 H34 O2 FORMUL 5 HOH *(H2 O) HELIX 1 AA1 ASP B 1002 ALA B 1020 1 19 HELIX 2 AA2 ASN B 1022 ALA B 1043 1 22 HELIX 3 AA3 SER B 1055 GLU B 1081 1 27 HELIX 4 AA4 LYS B 1083 ALA B 1091 1 9 HELIX 5 AA5 GLN B 1093 TYR B 1105 1 13 HELIX 6 AA6 ASP B 45 GLN B 72 1 28 HELIX 7 AA7 LYS B 77 ALA B 95 1 19 HELIX 8 AA8 THR B 96 TYR B 106 1 11 HELIX 9 AA9 GLY B 113 TYR B 148 1 36 HELIX 10 AB1 PRO B 149 SER B 152 5 4 HELIX 11 AB2 GLN B 159 SER B 175 1 17 HELIX 12 AB3 SER B 175 PHE B 181 1 7 HELIX 13 AB4 PRO B 200 GLU B 202 5 3 HELIX 14 AB5 LYS B 203 PHE B 220 1 18 HELIX 15 AB6 PHE B 220 LYS B 240 1 21 HELIX 16 AB7 GLY B 245 GLY B 285 1 41 HELIX 17 AB8 SER B 289 CYS B 319 1 31 HELIX 18 AB9 PHE B 320 ASN B 323 5 4 HELIX 19 AC1 ARG B 324 ARG B 334 1 11 SHEET 1 AA1 2 ARG B 182 ILE B 187 0 SHEET 2 AA1 2 VAL B 192 MET B 197 -1 O VAL B 192 N ILE B 187 SSBOND 1 CYS B 35 CYS B 290 1555 1555 2.04 SSBOND 2 CYS B 117 CYS B 195 1555 1555 2.03 SITE 1 AC1 14 TYR B 51 TRP B 100 TYR B 103 LEU B 124 SITE 2 AC1 14 THR B 125 MET B 128 PHE B 129 THR B 178 SITE 3 AC1 14 ARG B 182 LYS B 215 TRP B 269 PHE B 272 SITE 4 AC1 14 ILE B 304 PHE B 308 SITE 1 AC2 6 PRO B 48 TYR B 52 THR B 102 SER B 105 SITE 2 AC2 6 ALA B 228 THR B 229 CRYST1 70.260 78.790 93.410 90.00 90.00 90.00 P 21 2 21 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.014233 0.000000 0.000000 0.00000 SCALE2 0.000000 0.012692 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010705 0.00000 ATOM 1 N ALA B1001 34.597 36.407 -20.660 1.00 91.15 N ANISOU 1 N ALA B1001 11097 12158 11379 -104 769 -608 N ATOM 2 CA ALA B1001 34.274 36.679 -22.057 1.00 91.70 C ANISOU 2 CA ALA B1001 11276 12291 11274 -194 859 -634 C ATOM 3 C ALA B1001 33.303 35.644 -22.642 1.00 94.85 C ANISOU 3 C ALA B1001 11854 12533 11653 -45 851 -750 C ATOM 4 O ALA B1001 32.336 36.025 -23.305 1.00 93.86 O ANISOU 4 O ALA B1001 11922 12301 11440 -144 805 -726 O ATOM 5 CB ALA B1001 35.547 36.746 -22.889 1.00 95.11 C ANISOU 5 CB ALA B1001 11512 13030 11595 -231 1041 -663 C ATOM 6 N ASP B1002 33.560 34.342 -22.392 1.00 91.46 N ANISOU 6 N ASP B1002 11371 12073 11306 187 869 -870 N ATOM 7 CA ASP B1002 32.738 33.229 -22.874 1.00 90.84 C ANISOU 7 CA ASP B1002 11473 11830 11213 333 835 -981 C ATOM 8 C ASP B1002 31.467 33.061 -22.032 1.00 91.31 C ANISOU 8 C ASP B1002 11682 11630 11382 321 660 -922 C ATOM 9 O ASP B1002 31.484 33.342 -20.831 1.00 89.68 O ANISOU 9 O ASP B1002 11406 11373 11295 300 582 -846 O ATOM 10 CB ASP B1002 33.558 31.928 -22.883 1.00 94.56 C ANISOU 10 CB ASP B1002 11846 12352 11729 590 895 -1132 C ATOM 11 CG ASP B1002 32.935 30.811 -23.691 1.00106.07 C ANISOU 11 CG ASP B1002 13513 13671 13117 732 879 -1265 C ATOM 12 OD1 ASP B1002 32.105 30.067 -23.130 1.00105.53 O ANISOU 12 OD1 ASP B1002 13587 13370 13142 799 724 -1268 O ATOM 13 OD2 ASP B1002 33.282 30.676 -24.883 1.00114.25 O ANISOU 13 OD2 ASP B1002 14583 14835 13992 764 1017 -1364 O ATOM 14 N LEU B1003 30.374 32.593 -22.670 1.00 86.67 N ANISOU 14 N LEU B1003 11296 10889 10745 326 599 -956 N ATOM 15 CA LEU B1003 29.063 32.360 -22.049 1.00 84.37 C ANISOU 15 CA LEU B1003 11133 10381 10545 302 447 -900 C ATOM 16 C LEU B1003 29.118 31.308 -20.931 1.00 87.17 C ANISOU 16 C LEU B1003 11459 10627 11035 439 366 -926 C ATOM 17 O LEU B1003 28.423 31.460 -19.924 1.00 85.34 O ANISOU 17 O LEU B1003 11239 10291 10895 384 273 -843 O ATOM 18 CB LEU B1003 28.027 31.971 -23.122 1.00 84.56 C ANISOU 18 CB LEU B1003 11361 10287 10480 274 393 -933 C ATOM 19 CG LEU B1003 26.548 32.066 -22.735 1.00 87.57 C ANISOU 19 CG LEU B1003 11843 10490 10937 191 244 -847 C ATOM 20 CD1 LEU B1003 26.024 33.489 -22.876 1.00 86.85 C ANISOU 20 CD1 LEU B1003 11750 10422 10828 30 224 -744 C ATOM 21 CD2 LEU B1003 25.717 31.142 -23.588 1.00 90.48 C ANISOU 21 CD2 LEU B1003 12401 10724 11254 211 159 -896 C ATOM 22 N GLU B1004 29.947 30.255 -21.106 1.00 84.73 N ANISOU 22 N GLU B1004 11121 10344 10729 618 398 -1043 N ATOM 23 CA GLU B1004 30.144 29.189 -20.119 1.00 84.45 C ANISOU 23 CA GLU B1004 11079 10193 10814 758 296 -1073 C ATOM 24 C GLU B1004 30.910 29.747 -18.910 1.00 87.13 C ANISOU 24 C GLU B1004 11236 10613 11257 735 294 -997 C ATOM 25 O GLU B1004 30.572 29.424 -17.770 1.00 85.51 O ANISOU 25 O GLU B1004 11061 10283 11146 726 177 -939 O ATOM 26 CB GLU B1004 30.898 28.001 -20.747 1.00 88.05 C ANISOU 26 CB GLU B1004 11560 10651 11243 983 321 -1236 C ATOM 27 CG GLU B1004 30.935 26.752 -19.881 1.00 99.47 C ANISOU 27 CG GLU B1004 13073 11918 12804 1131 162 -1273 C ATOM 28 CD GLU B1004 32.017 25.748 -20.233 1.00124.00 C ANISOU 28 CD GLU B1004 16141 15051 15921 1400 182 -1440 C ATOM 29 OE1 GLU B1004 33.204 26.142 -20.297 1.00120.02 O ANISOU 29 OE1 GLU B1004 15406 14761 15435 1483 313 -1483 O ATOM 30 OE2 GLU B1004 31.681 24.553 -20.397 1.00119.82 O ANISOU 30 OE2 GLU B1004 15810 14325 15391 1530 54 -1526 O ATOM 31 N ASP B1005 31.924 30.599 -19.172 1.00 84.27 N ANISOU 31 N ASP B1005 10697 10461 10861 700 416 -988 N ATOM 32 CA ASP B1005 32.755 31.251 -18.157 1.00 83.79 C ANISOU 32 CA ASP B1005 10461 10494 10882 652 407 -906 C ATOM 33 C ASP B1005 31.957 32.290 -17.364 1.00 85.16 C ANISOU 33 C ASP B1005 10699 10591 11068 465 341 -771 C ATOM 34 O ASP B1005 32.175 32.431 -16.158 1.00 84.29 O ANISOU 34 O ASP B1005 10548 10438 11040 443 263 -706 O ATOM 35 CB ASP B1005 33.994 31.901 -18.804 1.00 87.24 C ANISOU 35 CB ASP B1005 10691 11193 11263 631 552 -920 C ATOM 36 CG ASP B1005 34.886 30.965 -19.609 1.00100.11 C ANISOU 36 CG ASP B1005 12218 12947 12871 840 656 -1073 C ATOM 37 OD1 ASP B1005 34.701 29.729 -19.510 1.00101.29 O ANISOU 37 OD1 ASP B1005 12460 12950 13075 1033 581 -1175 O ATOM 38 OD2 ASP B1005 35.776 31.468 -20.327 1.00107.62 O ANISOU 38 OD2 ASP B1005 13001 14145 13747 810 809 -1092 O ATOM 39 N ASN B1006 31.032 33.007 -18.040 1.00 80.24 N ANISOU 39 N ASN B1006 10186 9942 10358 341 364 -736 N ATOM 40 CA ASN B1006 30.175 34.026 -17.428 1.00 78.23 C ANISOU 40 CA ASN B1006 10000 9612 10110 197 306 -633 C ATOM 41 C ASN B1006 29.154 33.412 -16.470 1.00 80.68 C ANISOU 41 C ASN B1006 10408 9750 10497 225 207 -613 C ATOM 42 O ASN B1006 28.944 33.957 -15.385 1.00 79.20 O ANISOU 42 O ASN B1006 10222 9522 10347 165 163 -544 O ATOM 43 CB ASN B1006 29.491 34.889 -18.493 1.00 78.07 C ANISOU 43 CB ASN B1006 10070 9605 9990 82 334 -610 C ATOM 44 CG ASN B1006 30.403 35.903 -19.142 1.00 99.19 C ANISOU 44 CG ASN B1006 12667 12448 12573 -28 410 -576 C ATOM 45 OD1 ASN B1006 31.073 36.701 -18.476 1.00 92.34 O ANISOU 45 OD1 ASN B1006 11716 11645 11724 -107 397 -505 O ATOM 46 ND2 ASN B1006 30.417 35.923 -20.465 1.00 92.49 N ANISOU 46 ND2 ASN B1006 11864 11671 11608 -60 480 -616 N ATOM 47 N TRP B1007 28.539 32.273 -16.854 1.00 77.70 N ANISOU 47 N TRP B1007 10122 9273 10126 304 170 -670 N ATOM 48 CA TRP B1007 27.571 31.581 -16.002 1.00 77.06 C ANISOU 48 CA TRP B1007 10129 9045 10104 300 74 -638 C ATOM 49 C TRP B1007 28.243 30.832 -14.853 1.00 79.94 C ANISOU 49 C TRP B1007 10466 9366 10540 368 8 -636 C ATOM 50 O TRP B1007 27.599 30.586 -13.831 1.00 78.82 O ANISOU 50 O TRP B1007 10382 9134 10431 316 -60 -578 O ATOM 51 CB TRP B1007 26.617 30.685 -16.806 1.00 76.52 C ANISOU 51 CB TRP B1007 10188 8874 10013 318 24 -676 C ATOM 52 CG TRP B1007 25.389 31.423 -17.253 1.00 77.12 C ANISOU 52 CG TRP B1007 10308 8929 10064 206 21 -622 C ATOM 53 CD1 TRP B1007 25.115 31.868 -18.512 1.00 80.33 C ANISOU 53 CD1 TRP B1007 10759 9363 10400 171 46 -643 C ATOM 54 CD2 TRP B1007 24.326 31.906 -16.416 1.00 76.23 C ANISOU 54 CD2 TRP B1007 10187 8779 9998 120 -10 -541 C ATOM 55 NE1 TRP B1007 23.932 32.571 -18.520 1.00 79.26 N ANISOU 55 NE1 TRP B1007 10641 9191 10283 78 7 -576 N ATOM 56 CE2 TRP B1007 23.421 32.602 -17.248 1.00 80.12 C ANISOU 56 CE2 TRP B1007 10703 9270 10467 57 -16 -520 C ATOM 57 CE3 TRP B1007 24.037 31.799 -15.043 1.00 77.20 C ANISOU 57 CE3 TRP B1007 10287 8874 10170 93 -32 -488 C ATOM 58 CZ2 TRP B1007 22.244 33.183 -16.755 1.00 79.02 C ANISOU 58 CZ2 TRP B1007 10537 9110 10375 -4 -40 -458 C ATOM 59 CZ3 TRP B1007 22.880 32.387 -14.555 1.00 78.28 C ANISOU 59 CZ3 TRP B1007 10406 9008 10330 20 -29 -430 C ATOM 60 CH2 TRP B1007 21.996 33.064 -15.406 1.00 78.84 C ANISOU 60 CH2 TRP B1007 10473 9086 10399 -14 -31 -420 C ATOM 61 N GLU B1008 29.547 30.513 -15.003 1.00 76.76 N ANISOU 61 N GLU B1008 9966 9040 10159 478 28 -694 N ATOM 62 CA GLU B1008 30.358 29.878 -13.965 1.00 76.74 C ANISOU 62 CA GLU B1008 9921 9000 10237 555 -58 -691 C ATOM 63 C GLU B1008 30.626 30.934 -12.886 1.00 78.38 C ANISOU 63 C GLU B1008 10067 9253 10460 439 -63 -592 C ATOM 64 O GLU B1008 30.554 30.619 -11.701 1.00 77.81 O ANISOU 64 O GLU B1008 10049 9090 10427 414 -160 -541 O ATOM 65 CB GLU B1008 31.677 29.347 -14.549 1.00 79.95 C ANISOU 65 CB GLU B1008 10202 9502 10674 724 -28 -790 C ATOM 66 CG GLU B1008 32.367 28.315 -13.672 1.00 92.22 C ANISOU 66 CG GLU B1008 11746 10965 12329 855 -165 -812 C ATOM 67 CD GLU B1008 33.703 27.831 -14.200 1.00115.46 C ANISOU 67 CD GLU B1008 14526 14021 15324 1057 -133 -922 C ATOM 68 OE1 GLU B1008 33.764 26.685 -14.701 1.00110.12 O ANISOU 68 OE1 GLU B1008 13925 13256 14660 1236 -181 -1036 O ATOM 69 OE2 GLU B1008 34.692 28.595 -14.113 1.00110.67 O ANISOU 69 OE2 GLU B1008 13712 13594 14744 1038 -64 -894 O ATOM 70 N THR B1009 30.885 32.193 -13.308 1.00 73.58 N ANISOU 70 N THR B1009 9381 8773 9805 352 27 -562 N ATOM 71 CA THR B1009 31.122 33.350 -12.437 1.00 72.49 C ANISOU 71 CA THR B1009 9218 8666 9658 232 12 -473 C ATOM 72 C THR B1009 29.840 33.694 -11.662 1.00 74.50 C ANISOU 72 C THR B1009 9614 8806 9887 147 -16 -422 C ATOM 73 O THR B1009 29.914 33.980 -10.467 1.00 74.29 O ANISOU 73 O THR B1009 9628 8735 9866 95 -71 -368 O ATOM 74 CB THR B1009 31.648 34.548 -13.260 1.00 80.17 C ANISOU 74 CB THR B1009 10104 9786 10571 148 95 -452 C ATOM 75 OG1 THR B1009 32.736 34.122 -14.081 1.00 81.89 O ANISOU 75 OG1 THR B1009 10170 10145 10798 230 156 -510 O ATOM 76 CG2 THR B1009 32.095 35.721 -12.388 1.00 77.73 C ANISOU 76 CG2 THR B1009 9785 9499 10251 22 48 -360 C ATOM 77 N LEU B1010 28.673 33.651 -12.341 1.00 69.59 N ANISOU 77 N LEU B1010 9063 8145 9234 136 22 -443 N ATOM 78 CA LEU B1010 27.365 33.944 -11.747 1.00 68.26 C ANISOU 78 CA LEU B1010 8985 7901 9050 73 17 -406 C ATOM 79 C LEU B1010 26.966 32.930 -10.670 1.00 71.73 C ANISOU 79 C LEU B1010 9489 8250 9514 74 -47 -383 C ATOM 80 O LEU B1010 26.449 33.329 -9.626 1.00 71.08 O ANISOU 80 O LEU B1010 9458 8143 9407 10 -45 -339 O ATOM 81 CB LEU B1010 26.274 34.048 -12.830 1.00 67.87 C ANISOU 81 CB LEU B1010 8964 7842 8981 63 50 -427 C ATOM 82 CG LEU B1010 26.249 35.349 -13.639 1.00 72.15 C ANISOU 82 CG LEU B1010 9493 8441 9478 16 90 -421 C ATOM 83 CD1 LEU B1010 25.705 35.115 -15.034 1.00 72.33 C ANISOU 83 CD1 LEU B1010 9541 8463 9478 23 100 -455 C ATOM 84 CD2 LEU B1010 25.447 36.432 -12.929 1.00 74.08 C ANISOU 84 CD2 LEU B1010 9780 8653 9715 -31 86 -383 C ATOM 85 N ASN B1011 27.229 31.632 -10.915 1.00 68.38 N ANISOU 85 N ASN B1011 9083 7773 9125 143 -107 -416 N ATOM 86 CA ASN B1011 26.918 30.551 -9.980 1.00 68.37 C ANISOU 86 CA ASN B1011 9172 7667 9140 125 -202 -385 C ATOM 87 C ASN B1011 27.858 30.520 -8.777 1.00 72.37 C ANISOU 87 C ASN B1011 9687 8151 9661 119 -274 -348 C ATOM 88 O ASN B1011 27.388 30.322 -7.654 1.00 72.05 O ANISOU 88 O ASN B1011 9738 8051 9587 32 -317 -288 O ATOM 89 CB ASN B1011 26.893 29.200 -10.695 1.00 69.83 C ANISOU 89 CB ASN B1011 9411 7768 9352 205 -279 -435 C ATOM 90 CG ASN B1011 25.649 28.975 -11.515 1.00 91.51 C ANISOU 90 CG ASN B1011 12206 10488 12074 160 -260 -437 C ATOM 91 OD1 ASN B1011 24.521 29.061 -11.019 1.00 85.48 O ANISOU 91 OD1 ASN B1011 11475 9712 11292 48 -254 -372 O ATOM 92 ND2 ASN B1011 25.827 28.650 -12.784 1.00 83.94 N ANISOU 92 ND2 ASN B1011 11253 9529 11111 242 -253 -511 N ATOM 93 N ASP B1012 29.177 30.714 -9.008 1.00 69.20 N ANISOU 93 N ASP B1012 9184 7806 9302 198 -290 -377 N ATOM 94 CA ASP B1012 30.202 30.723 -7.959 1.00 69.52 C ANISOU 94 CA ASP B1012 9210 7831 9375 194 -386 -336 C ATOM 95 C ASP B1012 30.007 31.876 -6.977 1.00 72.58 C ANISOU 95 C ASP B1012 9646 8235 9697 66 -362 -266 C ATOM 96 O ASP B1012 30.170 31.675 -5.774 1.00 72.74 O ANISOU 96 O ASP B1012 9757 8182 9699 8 -455 -212 O ATOM 97 CB ASP B1012 31.622 30.748 -8.558 1.00 72.22 C ANISOU 97 CB ASP B1012 9384 8268 9789 306 -395 -381 C ATOM 98 CG ASP B1012 32.201 29.375 -8.859 1.00 83.68 C ANISOU 98 CG ASP B1012 10816 9658 11321 469 -491 -450 C ATOM 99 OD1 ASP B1012 31.670 28.688 -9.759 1.00 84.15 O ANISOU 99 OD1 ASP B1012 10921 9683 11370 544 -460 -521 O ATOM 100 OD2 ASP B1012 33.206 29.001 -8.216 1.00 91.06 O ANISOU 100 OD2 ASP B1012 11697 10571 12332 530 -611 -437 O ATOM 101 N ASN B1013 29.630 33.067 -7.486 1.00 68.05 N ANISOU 101 N ASN B1013 9039 7739 9077 22 -253 -271 N ATOM 102 CA ASN B1013 29.397 34.261 -6.671 1.00 67.32 C ANISOU 102 CA ASN B1013 9018 7648 8913 -75 -232 -226 C ATOM 103 C ASN B1013 28.062 34.230 -5.908 1.00 70.83 C ANISOU 103 C ASN B1013 9588 8037 9287 -131 -188 -213 C ATOM 104 O ASN B1013 27.929 34.940 -4.910 1.00 70.51 O ANISOU 104 O ASN B1013 9642 7974 9172 -195 -188 -185 O ATOM 105 CB ASN B1013 29.546 35.534 -7.498 1.00 66.57 C ANISOU 105 CB ASN B1013 8863 7636 8796 -96 -166 -235 C ATOM 106 CG ASN B1013 30.986 35.923 -7.709 1.00 85.87 C ANISOU 106 CG ASN B1013 11197 10157 11274 -109 -216 -209 C ATOM 107 OD1 ASN B1013 31.653 36.442 -6.808 1.00 80.59 O ANISOU 107 OD1 ASN B1013 10562 9471 10590 -178 -297 -153 O ATOM 108 ND2 ASN B1013 31.504 35.669 -8.899 1.00 76.98 N ANISOU 108 ND2 ASN B1013 9934 9128 10188 -53 -169 -246 N ATOM 109 N LEU B1014 27.093 33.396 -6.349 1.00 67.32 N ANISOU 109 N LEU B1014 9147 7576 8857 -113 -154 -232 N ATOM 110 CA LEU B1014 25.805 33.233 -5.661 1.00 67.37 C ANISOU 110 CA LEU B1014 9230 7565 8802 -180 -102 -210 C ATOM 111 C LEU B1014 26.016 32.508 -4.327 1.00 72.10 C ANISOU 111 C LEU B1014 9947 8097 9352 -255 -184 -155 C ATOM 112 O LEU B1014 25.357 32.838 -3.338 1.00 72.19 O ANISOU 112 O LEU B1014 10043 8118 9268 -334 -130 -130 O ATOM 113 CB LEU B1014 24.790 32.467 -6.529 1.00 67.35 C ANISOU 113 CB LEU B1014 9188 7566 8834 -169 -74 -224 C ATOM 114 CG LEU B1014 23.859 33.310 -7.404 1.00 71.64 C ANISOU 114 CG LEU B1014 9660 8173 9387 -147 23 -256 C ATOM 115 CD1 LEU B1014 23.258 32.474 -8.515 1.00 71.79 C ANISOU 115 CD1 LEU B1014 9643 8179 9456 -131 2 -267 C ATOM 116 CD2 LEU B1014 22.746 33.959 -6.583 1.00 74.64 C ANISOU 116 CD2 LEU B1014 10055 8597 9709 -192 115 -244 C ATOM 117 N LYS B1015 26.960 31.543 -4.304 1.00 68.95 N ANISOU 117 N LYS B1015 9558 7628 9011 -224 -319 -142 N ATOM 118 CA LYS B1015 27.346 30.769 -3.121 1.00 69.65 C ANISOU 118 CA LYS B1015 9776 7623 9066 -293 -450 -82 C ATOM 119 C LYS B1015 28.145 31.638 -2.143 1.00 73.73 C ANISOU 119 C LYS B1015 10347 8134 9531 -337 -490 -51 C ATOM 120 O LYS B1015 28.114 31.380 -0.939 1.00 74.23 O ANISOU 120 O LYS B1015 10561 8134 9510 -439 -558 6 O ATOM 121 CB LYS B1015 28.160 29.528 -3.522 1.00 72.88 C ANISOU 121 CB LYS B1015 10172 7942 9575 -207 -609 -92 C ATOM 122 CG LYS B1015 27.333 28.444 -4.200 1.00 88.74 C ANISOU 122 CG LYS B1015 12210 9903 11605 -197 -625 -106 C ATOM 123 CD LYS B1015 28.202 27.290 -4.685 1.00100.43 C ANISOU 123 CD LYS B1015 13696 11279 13184 -69 -789 -144 C ATOM 124 CE LYS B1015 27.425 26.277 -5.492 1.00112.29 C ANISOU 124 CE LYS B1015 15254 12713 14698 -52 -823 -168 C ATOM 125 NZ LYS B1015 27.070 26.791 -6.843 1.00121.06 N ANISOU 125 NZ LYS B1015 16243 13924 15830 24 -680 -242 N ATOM 126 N VAL B1016 28.857 32.664 -2.667 1.00 69.65 N ANISOU 126 N VAL B1016 9729 7680 9054 -282 -460 -80 N ATOM 127 CA VAL B1016 29.660 33.621 -1.895 1.00 69.81 C ANISOU 127 CA VAL B1016 9800 7693 9030 -334 -516 -45 C ATOM 128 C VAL B1016 28.738 34.505 -1.028 1.00 73.69 C ANISOU 128 C VAL B1016 10442 8184 9372 -418 -418 -44 C ATOM 129 O VAL B1016 29.036 34.703 0.153 1.00 74.14 O ANISOU 129 O VAL B1016 10652 8180 9338 -503 -491 -1 O ATOM 130 CB VAL B1016 30.624 34.446 -2.803 1.00 73.49 C ANISOU 130 CB VAL B1016 10110 8240 9574 -280 -516 -63 C ATOM 131 CG1 VAL B1016 31.327 35.562 -2.031 1.00 73.85 C ANISOU 131 CG1 VAL B1016 10229 8271 9561 -366 -586 -14 C ATOM 132 CG2 VAL B1016 31.654 33.543 -3.474 1.00 73.81 C ANISOU 132 CG2 VAL B1016 9994 8302 9749 -183 -602 -74 C ATOM 133 N ILE B1017 27.609 34.995 -1.604 1.00 69.48 N ANISOU 133 N ILE B1017 9870 7716 8815 -385 -261 -97 N ATOM 134 CA ILE B1017 26.607 35.831 -0.914 1.00 69.54 C ANISOU 134 CA ILE B1017 9986 7743 8694 -417 -142 -124 C ATOM 135 C ILE B1017 25.991 35.067 0.276 1.00 74.43 C ANISOU 135 C ILE B1017 10739 8342 9200 -514 -124 -87 C ATOM 136 O ILE B1017 25.773 35.660 1.333 1.00 74.84 O ANISOU 136 O ILE B1017 10943 8383 9110 -568 -85 -92 O ATOM 137 CB ILE B1017 25.524 36.401 -1.889 1.00 71.96 C ANISOU 137 CB ILE B1017 10185 8125 9032 -338 0 -188 C ATOM 138 CG1 ILE B1017 26.165 37.132 -3.091 1.00 71.51 C ANISOU 138 CG1 ILE B1017 10025 8083 9062 -274 -32 -210 C ATOM 139 CG2 ILE B1017 24.547 37.338 -1.158 1.00 73.45 C ANISOU 139 CG2 ILE B1017 10468 8340 9101 -328 121 -236 C ATOM 140 CD1 ILE B1017 25.332 37.139 -4.388 1.00 77.43 C ANISOU 140 CD1 ILE B1017 10647 8888 9885 -206 48 -251 C ATOM 141 N GLU B1018 25.750 33.751 0.105 1.00 71.17 N ANISOU 141 N GLU B1018 10290 7916 8834 -547 -164 -49 N ATOM 142 CA GLU B1018 25.202 32.863 1.136 1.00 72.13 C ANISOU 142 CA GLU B1018 10542 8017 8846 -677 -174 10 C ATOM 143 C GLU B1018 26.176 32.689 2.308 1.00 76.90 C ANISOU 143 C GLU B1018 11330 8516 9372 -766 -332 71 C ATOM 144 O GLU B1018 25.737 32.579 3.452 1.00 77.76 O ANISOU 144 O GLU B1018 11607 8620 9318 -892 -303 108 O ATOM 145 CB GLU B1018 24.868 31.484 0.543 1.00 73.54 C ANISOU 145 CB GLU B1018 10663 8172 9107 -698 -236 47 C ATOM 146 CG GLU B1018 23.618 31.452 -0.317 1.00 83.04 C ANISOU 146 CG GLU B1018 11729 9477 10346 -673 -92 16 C ATOM 147 CD GLU B1018 23.220 30.058 -0.757 1.00102.23 C ANISOU 147 CD GLU B1018 14152 11863 12828 -731 -179 67 C ATOM 148 OE1 GLU B1018 23.388 29.744 -1.957 1.00 96.96 O ANISOU 148 OE1 GLU B1018 13385 11172 12284 -631 -223 31 O ATOM 149 OE2 GLU B1018 22.754 29.273 0.100 1.00 96.98 O ANISOU 149 OE2 GLU B1018 13603 11181 12065 -887 -212 145 O ATOM 150 N LYS B1019 27.491 32.658 2.012 1.00 73.19 N ANISOU 150 N LYS B1019 10821 7972 9016 -707 -499 85 N ATOM 151 CA LYS B1019 28.573 32.477 2.985 1.00 74.09 C ANISOU 151 CA LYS B1019 11077 7976 9100 -778 -696 151 C ATOM 152 C LYS B1019 29.145 33.806 3.519 1.00 78.21 C ANISOU 152 C LYS B1019 11679 8491 9547 -796 -706 143 C ATOM 153 O LYS B1019 29.953 33.791 4.452 1.00 78.74 O ANISOU 153 O LYS B1019 11891 8464 9564 -880 -873 205 O ATOM 154 CB LYS B1019 29.693 31.608 2.379 1.00 76.73 C ANISOU 154 CB LYS B1019 11295 8244 9617 -692 -888 172 C ATOM 155 CG LYS B1019 29.289 30.158 2.133 1.00 91.67 C ANISOU 155 CG LYS B1019 13198 10076 11556 -691 -956 191 C ATOM 156 CD LYS B1019 30.339 29.412 1.328 1.00102.58 C ANISOU 156 CD LYS B1019 14442 11405 13129 -543 -1114 170 C ATOM 157 CE LYS B1019 29.913 27.995 1.034 1.00114.89 C ANISOU 157 CE LYS B1019 16051 12874 14728 -529 -1203 178 C ATOM 158 NZ LYS B1019 30.924 27.275 0.218 1.00125.08 N ANISOU 158 NZ LYS B1019 17215 14111 16200 -343 -1347 129 N ATOM 159 N ALA B1020 28.713 34.946 2.938 1.00 74.08 N ANISOU 159 N ALA B1020 11083 8050 9015 -727 -553 72 N ATOM 160 CA ALA B1020 29.157 36.295 3.300 1.00 74.14 C ANISOU 160 CA ALA B1020 11184 8035 8949 -740 -571 56 C ATOM 161 C ALA B1020 28.779 36.705 4.725 1.00 79.42 C ANISOU 161 C ALA B1020 12129 8650 9397 -844 -552 60 C ATOM 162 O ALA B1020 27.678 36.401 5.189 1.00 79.35 O ANISOU 162 O ALA B1020 12192 8689 9269 -873 -403 32 O ATOM 163 CB ALA B1020 28.617 37.307 2.305 1.00 73.88 C ANISOU 163 CB ALA B1020 11037 8081 8953 -638 -426 -23 C ATOM 164 N ASP B1021 29.703 37.410 5.406 1.00 76.89 N ANISOU 164 N ASP B1021 11962 8238 9014 -909 -705 98 N ATOM 165 CA ASP B1021 29.536 37.895 6.778 1.00 78.14 C ANISOU 165 CA ASP B1021 12426 8321 8942 -1013 -718 98 C ATOM 166 C ASP B1021 29.082 39.359 6.818 1.00 81.48 C ANISOU 166 C ASP B1021 12961 8746 9252 -950 -608 4 C ATOM 167 O ASP B1021 28.122 39.679 7.522 1.00 82.17 O ANISOU 167 O ASP B1021 13213 8856 9151 -944 -449 -70 O ATOM 168 CB ASP B1021 30.839 37.722 7.582 1.00 81.15 C ANISOU 168 CB ASP B1021 12948 8570 9314 -1137 -996 206 C ATOM 169 CG ASP B1021 31.296 36.287 7.725 1.00 91.92 C ANISOU 169 CG ASP B1021 14254 9895 10776 -1188 -1144 294 C ATOM 170 OD1 ASP B1021 31.937 35.771 6.783 1.00 91.78 O ANISOU 170 OD1 ASP B1021 13986 9907 10979 -1105 -1225 317 O ATOM 171 OD2 ASP B1021 31.034 35.686 8.787 1.00 98.78 O ANISOU 171 OD2 ASP B1021 15342 10701 11491 -1310 -1188 339 O ATOM 172 N ASN B1022 29.779 40.242 6.074 1.00 76.63 N ANISOU 172 N ASN B1022 12263 8108 8743 -907 -698 5 N ATOM 173 CA ASN B1022 29.499 41.680 6.026 1.00 76.33 C ANISOU 173 CA ASN B1022 12357 8032 8614 -850 -657 -75 C ATOM 174 C ASN B1022 29.046 42.178 4.642 1.00 77.82 C ANISOU 174 C ASN B1022 12326 8302 8942 -718 -550 -135 C ATOM 175 O ASN B1022 28.961 41.391 3.699 1.00 75.72 O ANISOU 175 O ASN B1022 11804 8131 8837 -675 -497 -117 O ATOM 176 CB ASN B1022 30.705 42.483 6.545 1.00 77.44 C ANISOU 176 CB ASN B1022 12682 8037 8704 -965 -902 -3 C ATOM 177 CG ASN B1022 32.027 42.142 5.898 1.00 96.88 C ANISOU 177 CG ASN B1022 14931 10514 11365 -1034 -1099 118 C ATOM 178 OD1 ASN B1022 32.189 42.180 4.673 1.00 88.52 O ANISOU 178 OD1 ASN B1022 13616 9547 10472 -971 -1062 119 O ATOM 179 ND2 ASN B1022 33.016 41.838 6.719 1.00 90.57 N ANISOU 179 ND2 ASN B1022 14236 9630 10547 -1167 -1315 221 N ATOM 180 N ALA B1023 28.747 43.490 4.542 1.00 74.72 N ANISOU 180 N ALA B1023 12064 7852 8473 -655 -536 -210 N ATOM 181 CA ALA B1023 28.288 44.170 3.329 1.00 73.59 C ANISOU 181 CA ALA B1023 11780 7750 8432 -541 -470 -267 C ATOM 182 C ALA B1023 29.336 44.189 2.212 1.00 76.16 C ANISOU 182 C ALA B1023 11908 8101 8926 -604 -605 -172 C ATOM 183 O ALA B1023 28.965 44.114 1.039 1.00 74.48 O ANISOU 183 O ALA B1023 11496 7971 8833 -530 -524 -194 O ATOM 184 CB ALA B1023 27.858 45.588 3.664 1.00 75.57 C ANISOU 184 CB ALA B1023 12279 7888 8545 -468 -481 -363 C ATOM 185 N ALA B1024 30.636 44.290 2.576 1.00 73.04 N ANISOU 185 N ALA B1024 11566 7649 8535 -746 -808 -65 N ATOM 186 CA ALA B1024 31.770 44.323 1.645 1.00 72.15 C ANISOU 186 CA ALA B1024 11251 7593 8569 -828 -933 35 C ATOM 187 C ALA B1024 31.887 43.039 0.821 1.00 74.26 C ANISOU 187 C ALA B1024 11211 8002 9004 -777 -848 54 C ATOM 188 O ALA B1024 32.217 43.106 -0.363 1.00 73.43 O ANISOU 188 O ALA B1024 10902 7988 9009 -767 -832 73 O ATOM 189 CB ALA B1024 33.063 44.583 2.401 1.00 74.17 C ANISOU 189 CB ALA B1024 11613 7774 8795 -993 -1167 149 C ATOM 190 N GLN B1025 31.603 41.879 1.442 1.00 70.23 N ANISOU 190 N GLN B1025 10691 7501 8494 -751 -801 47 N ATOM 191 CA GLN B1025 31.639 40.571 0.782 1.00 69.05 C ANISOU 191 CA GLN B1025 10303 7447 8486 -691 -743 54 C ATOM 192 C GLN B1025 30.449 40.390 -0.164 1.00 72.13 C ANISOU 192 C GLN B1025 10584 7911 8912 -574 -550 -31 C ATOM 193 O GLN B1025 30.586 39.714 -1.185 1.00 71.23 O ANISOU 193 O GLN B1025 10263 7880 8923 -521 -512 -33 O ATOM 194 CB GLN B1025 31.684 39.437 1.811 1.00 70.75 C ANISOU 194 CB GLN B1025 10594 7613 8674 -724 -795 86 C ATOM 195 CG GLN B1025 33.035 39.279 2.489 1.00 83.18 C ANISOU 195 CG GLN B1025 12196 9128 10279 -826 -1022 188 C ATOM 196 CD GLN B1025 33.005 38.183 3.517 1.00102.10 C ANISOU 196 CD GLN B1025 14708 11452 12635 -866 -1098 223 C ATOM 197 OE1 GLN B1025 32.449 38.335 4.610 1.00 97.83 O ANISOU 197 OE1 GLN B1025 14422 10831 11919 -934 -1084 216 O ATOM 198 NE2 GLN B1025 33.604 37.049 3.188 1.00 95.07 N ANISOU 198 NE2 GLN B1025 13646 10583 11896 -824 -1184 259 N ATOM 199 N VAL B1026 29.288 40.991 0.175 1.00 68.84 N ANISOU 199 N VAL B1026 10307 7465 8384 -526 -434 -107 N ATOM 200 CA VAL B1026 28.061 40.937 -0.630 1.00 67.90 C ANISOU 200 CA VAL B1026 10088 7413 8300 -418 -268 -184 C ATOM 201 C VAL B1026 28.235 41.834 -1.866 1.00 70.91 C ANISOU 201 C VAL B1026 10382 7813 8747 -388 -286 -195 C ATOM 202 O VAL B1026 27.987 41.378 -2.983 1.00 69.58 O ANISOU 202 O VAL B1026 10040 7719 8679 -340 -227 -205 O ATOM 203 CB VAL B1026 26.782 41.292 0.190 1.00 72.65 C ANISOU 203 CB VAL B1026 10834 8000 8771 -362 -136 -265 C ATOM 204 CG1 VAL B1026 25.520 41.189 -0.664 1.00 71.89 C ANISOU 204 CG1 VAL B1026 10592 7986 8738 -252 17 -333 C ATOM 205 CG2 VAL B1026 26.649 40.408 1.428 1.00 73.29 C ANISOU 205 CG2 VAL B1026 11019 8073 8753 -432 -116 -240 C ATOM 206 N LYS B1027 28.687 43.095 -1.653 1.00 68.03 N ANISOU 206 N LYS B1027 10167 7369 8311 -434 -387 -184 N ATOM 207 CA LYS B1027 28.941 44.111 -2.685 1.00 67.57 C ANISOU 207 CA LYS B1027 10087 7303 8282 -450 -445 -174 C ATOM 208 C LYS B1027 29.928 43.608 -3.750 1.00 70.66 C ANISOU 208 C LYS B1027 10256 7802 8788 -516 -482 -99 C ATOM 209 O LYS B1027 29.701 43.838 -4.938 1.00 69.68 O ANISOU 209 O LYS B1027 10034 7730 8711 -495 -442 -111 O ATOM 210 CB LYS B1027 29.453 45.415 -2.039 1.00 71.22 C ANISOU 210 CB LYS B1027 10790 7638 8632 -530 -596 -151 C ATOM 211 CG LYS B1027 29.516 46.608 -2.989 1.00 86.18 C ANISOU 211 CG LYS B1027 12729 9490 10525 -558 -678 -141 C ATOM 212 CD LYS B1027 30.185 47.809 -2.347 1.00 97.79 C ANISOU 212 CD LYS B1027 14455 10817 11883 -670 -871 -96 C ATOM 213 CE LYS B1027 30.397 48.923 -3.341 1.00108.75 C ANISOU 213 CE LYS B1027 15894 12159 13268 -744 -988 -56 C ATOM 214 NZ LYS B1027 31.023 50.113 -2.707 1.00119.28 N ANISOU 214 NZ LYS B1027 17509 13328 14482 -871 -1207 -4 N ATOM 215 N ASP B1028 31.005 42.914 -3.320 1.00 67.39 N ANISOU 215 N ASP B1028 9766 7425 8415 -587 -557 -29 N ATOM 216 CA ASP B1028 32.033 42.355 -4.199 1.00 67.05 C ANISOU 216 CA ASP B1028 9489 7505 8481 -624 -580 28 C ATOM 217 C ASP B1028 31.474 41.261 -5.109 1.00 70.20 C ANISOU 217 C ASP B1028 9717 7990 8966 -510 -444 -31 C ATOM 218 O ASP B1028 31.775 41.257 -6.302 1.00 69.88 O ANISOU 218 O ASP B1028 9530 8047 8974 -509 -404 -29 O ATOM 219 CB ASP B1028 33.223 41.825 -3.380 1.00 69.58 C ANISOU 219 CB ASP B1028 9765 7833 8840 -694 -708 105 C ATOM 220 CG ASP B1028 34.300 41.166 -4.220 1.00 78.29 C ANISOU 220 CG ASP B1028 10593 9084 10068 -695 -717 145 C ATOM 221 OD1 ASP B1028 35.061 41.898 -4.888 1.00 79.16 O ANISOU 221 OD1 ASP B1028 10608 9284 10187 -792 -756 203 O ATOM 222 OD2 ASP B1028 34.367 39.919 -4.224 1.00 83.53 O ANISOU 222 OD2 ASP B1028 11142 9780 10816 -597 -685 116 O ATOM 223 N ALA B1029 30.669 40.341 -4.546 1.00 66.39 N ANISOU 223 N ALA B1029 9271 7468 8485 -431 -380 -77 N ATOM 224 CA ALA B1029 30.060 39.229 -5.276 1.00 65.52 C ANISOU 224 CA ALA B1029 9041 7408 8445 -338 -282 -125 C ATOM 225 C ALA B1029 28.988 39.683 -6.270 1.00 68.86 C ANISOU 225 C ALA B1029 9453 7851 8862 -288 -182 -179 C ATOM 226 O ALA B1029 28.861 39.076 -7.333 1.00 68.08 O ANISOU 226 O ALA B1029 9234 7811 8822 -242 -130 -203 O ATOM 227 CB ALA B1029 29.488 38.213 -4.303 1.00 66.27 C ANISOU 227 CB ALA B1029 9207 7448 8525 -313 -271 -135 C ATOM 228 N LEU B1030 28.231 40.749 -5.935 1.00 65.72 N ANISOU 228 N LEU B1030 9189 7392 8391 -288 -169 -203 N ATOM 229 CA LEU B1030 27.184 41.301 -6.801 1.00 65.40 C ANISOU 229 CA LEU B1030 9145 7350 8355 -231 -107 -252 C ATOM 230 C LEU B1030 27.772 42.066 -7.989 1.00 70.01 C ANISOU 230 C LEU B1030 9691 7964 8946 -285 -156 -224 C ATOM 231 O LEU B1030 27.228 41.975 -9.089 1.00 69.43 O ANISOU 231 O LEU B1030 9553 7921 8906 -253 -114 -248 O ATOM 232 CB LEU B1030 26.201 42.190 -6.018 1.00 65.97 C ANISOU 232 CB LEU B1030 9368 7344 8354 -181 -85 -302 C ATOM 233 CG LEU B1030 25.230 41.489 -5.058 1.00 70.88 C ANISOU 233 CG LEU B1030 10007 7975 8951 -127 14 -342 C ATOM 234 CD1 LEU B1030 24.641 42.476 -4.077 1.00 72.02 C ANISOU 234 CD1 LEU B1030 10316 8055 8992 -79 35 -398 C ATOM 235 CD2 LEU B1030 24.104 40.782 -5.808 1.00 72.83 C ANISOU 235 CD2 LEU B1030 10117 8283 9271 -63 107 -371 C ATOM 236 N THR B1031 28.880 42.812 -7.768 1.00 67.45 N ANISOU 236 N THR B1031 9413 7633 8582 -390 -256 -163 N ATOM 237 CA THR B1031 29.589 43.580 -8.801 1.00 67.82 C ANISOU 237 CA THR B1031 9428 7728 8613 -492 -312 -110 C ATOM 238 C THR B1031 30.184 42.625 -9.851 1.00 71.89 C ANISOU 238 C THR B1031 9738 8388 9188 -493 -241 -103 C ATOM 239 O THR B1031 30.110 42.913 -11.048 1.00 71.85 O ANISOU 239 O THR B1031 9697 8435 9167 -527 -216 -101 O ATOM 240 CB THR B1031 30.618 44.530 -8.157 1.00 77.12 C ANISOU 240 CB THR B1031 10703 8867 9730 -629 -450 -31 C ATOM 241 OG1 THR B1031 29.950 45.349 -7.194 1.00 76.55 O ANISOU 241 OG1 THR B1031 10856 8642 9586 -596 -508 -65 O ATOM 242 CG2 THR B1031 31.318 45.428 -9.175 1.00 77.08 C ANISOU 242 CG2 THR B1031 10683 8917 9688 -778 -520 44 C ATOM 243 N LYS B1032 30.734 41.478 -9.397 1.00 68.31 N ANISOU 243 N LYS B1032 9171 7988 8796 -447 -215 -107 N ATOM 244 CA LYS B1032 31.294 40.425 -10.251 1.00 68.18 C ANISOU 244 CA LYS B1032 8971 8095 8839 -400 -147 -128 C ATOM 245 C LYS B1032 30.184 39.787 -11.099 1.00 71.26 C ANISOU 245 C LYS B1032 9362 8469 9244 -305 -59 -200 C ATOM 246 O LYS B1032 30.409 39.479 -12.272 1.00 71.33 O ANISOU 246 O LYS B1032 9285 8567 9251 -295 -2 -223 O ATOM 247 CB LYS B1032 31.999 39.353 -9.403 1.00 70.84 C ANISOU 247 CB LYS B1032 9227 8444 9247 -345 -180 -125 C ATOM 248 CG LYS B1032 33.374 39.766 -8.900 1.00 83.98 C ANISOU 248 CG LYS B1032 10815 10170 10925 -440 -275 -45 C ATOM 249 CD LYS B1032 33.977 38.698 -8.005 1.00 92.94 C ANISOU 249 CD LYS B1032 11886 11286 12139 -373 -340 -42 C ATOM 250 CE LYS B1032 35.361 39.074 -7.546 1.00103.39 C ANISOU 250 CE LYS B1032 13104 12681 13497 -467 -453 46 C ATOM 251 NZ LYS B1032 35.965 38.014 -6.703 1.00112.97 N ANISOU 251 NZ LYS B1032 14256 13863 14803 -391 -547 51 N ATOM 252 N MET B1033 28.985 39.613 -10.499 1.00 66.60 N ANISOU 252 N MET B1033 8872 7775 8658 -246 -49 -233 N ATOM 253 CA MET B1033 27.790 39.060 -11.142 1.00 65.65 C ANISOU 253 CA MET B1033 8755 7629 8559 -175 9 -284 C ATOM 254 C MET B1033 27.219 40.039 -12.165 1.00 69.47 C ANISOU 254 C MET B1033 9285 8105 9007 -208 6 -286 C ATOM 255 O MET B1033 26.776 39.610 -13.230 1.00 68.94 O ANISOU 255 O MET B1033 9187 8058 8948 -185 37 -313 O ATOM 256 CB MET B1033 26.718 38.739 -10.093 1.00 67.58 C ANISOU 256 CB MET B1033 9067 7796 8812 -131 22 -300 C ATOM 257 CG MET B1033 26.868 37.380 -9.467 1.00 70.98 C ANISOU 257 CG MET B1033 9470 8219 9280 -100 21 -302 C ATOM 258 SD MET B1033 25.622 37.108 -8.190 1.00 74.93 S ANISOU 258 SD MET B1033 10054 8661 9754 -99 51 -301 S ATOM 259 CE MET B1033 24.202 36.714 -9.200 1.00 71.38 C ANISOU 259 CE MET B1033 9552 8225 9347 -64 104 -330 C ATOM 260 N ARG B1034 27.221 41.348 -11.828 1.00 66.24 N ANISOU 260 N ARG B1034 8973 7645 8550 -263 -54 -257 N ATOM 261 CA ARG B1034 26.732 42.448 -12.663 1.00 66.28 C ANISOU 261 CA ARG B1034 9060 7606 8516 -301 -103 -250 C ATOM 262 C ARG B1034 27.553 42.564 -13.953 1.00 70.87 C ANISOU 262 C ARG B1034 9593 8282 9053 -402 -103 -214 C ATOM 263 O ARG B1034 26.979 42.776 -15.022 1.00 70.57 O ANISOU 263 O ARG B1034 9589 8231 8995 -415 -113 -222 O ATOM 264 CB ARG B1034 26.783 43.769 -11.876 1.00 66.65 C ANISOU 264 CB ARG B1034 9253 7558 8512 -338 -197 -227 C ATOM 265 CG ARG B1034 25.785 44.811 -12.349 1.00 76.08 C ANISOU 265 CG ARG B1034 10566 8646 9693 -306 -268 -249 C ATOM 266 CD ARG B1034 26.007 46.138 -11.653 1.00 84.55 C ANISOU 266 CD ARG B1034 11819 9605 10702 -342 -387 -232 C ATOM 267 NE ARG B1034 25.086 47.167 -12.134 1.00 93.40 N ANISOU 267 NE ARG B1034 13068 10601 11817 -289 -485 -261 N ATOM 268 CZ ARG B1034 25.329 47.976 -13.161 1.00109.20 C ANISOU 268 CZ ARG B1034 15158 12561 13774 -399 -603 -206 C ATOM 269 NH1 ARG B1034 26.471 47.883 -13.834 1.00 96.83 N ANISOU 269 NH1 ARG B1034 13545 11096 12150 -579 -609 -120 N ATOM 270 NH2 ARG B1034 24.434 48.882 -13.525 1.00 97.89 N ANISOU 270 NH2 ARG B1034 13857 10988 12348 -331 -720 -237 N ATOM 271 N ALA B1035 28.890 42.411 -13.846 1.00 68.16 N ANISOU 271 N ALA B1035 9163 8045 8691 -476 -90 -172 N ATOM 272 CA ALA B1035 29.824 42.474 -14.972 1.00 68.92 C ANISOU 272 CA ALA B1035 9175 8280 8730 -580 -56 -138 C ATOM 273 C ALA B1035 29.685 41.250 -15.878 1.00 72.83 C ANISOU 273 C ALA B1035 9576 8853 9245 -491 51 -207 C ATOM 274 O ALA B1035 29.746 41.392 -17.101 1.00 73.08 O ANISOU 274 O ALA B1035 9613 8950 9203 -553 85 -207 O ATOM 275 CB ALA B1035 31.252 42.592 -14.462 1.00 70.52 C ANISOU 275 CB ALA B1035 9271 8594 8929 -667 -70 -77 C ATOM 276 N ALA B1036 29.487 40.057 -15.276 1.00 68.74 N ANISOU 276 N ALA B1036 8998 8312 8807 -357 90 -263 N ATOM 277 CA ALA B1036 29.323 38.784 -15.981 1.00 68.49 C ANISOU 277 CA ALA B1036 8912 8315 8797 -255 162 -336 C ATOM 278 C ALA B1036 27.987 38.711 -16.726 1.00 71.70 C ANISOU 278 C ALA B1036 9422 8630 9190 -234 149 -365 C ATOM 279 O ALA B1036 27.942 38.162 -17.827 1.00 71.48 O ANISOU 279 O ALA B1036 9398 8640 9120 -218 192 -407 O ATOM 280 CB ALA B1036 29.443 37.625 -15.003 1.00 68.95 C ANISOU 280 CB ALA B1036 8919 8336 8942 -140 158 -370 C ATOM 281 N ALA B1037 26.909 39.267 -16.126 1.00 67.76 N ANISOU 281 N ALA B1037 9006 8015 8726 -230 87 -345 N ATOM 282 CA ALA B1037 25.559 39.298 -16.699 1.00 67.29 C ANISOU 282 CA ALA B1037 9016 7871 8681 -209 52 -360 C ATOM 283 C ALA B1037 25.491 40.167 -17.955 1.00 72.13 C ANISOU 283 C ALA B1037 9704 8488 9214 -301 12 -336 C ATOM 284 O ALA B1037 24.851 39.772 -18.929 1.00 72.00 O ANISOU 284 O ALA B1037 9728 8446 9182 -297 -2 -356 O ATOM 285 CB ALA B1037 24.559 39.789 -15.665 1.00 67.53 C ANISOU 285 CB ALA B1037 9078 7810 8769 -168 11 -351 C ATOM 286 N LEU B1038 26.162 41.337 -17.939 1.00 69.45 N ANISOU 286 N LEU B1038 9405 8170 8812 -403 -26 -284 N ATOM 287 CA LEU B1038 26.210 42.261 -19.075 1.00 70.26 C ANISOU 287 CA LEU B1038 9606 8272 8817 -528 -86 -240 C ATOM 288 C LEU B1038 27.132 41.738 -20.181 1.00 75.72 C ANISOU 288 C LEU B1038 10251 9113 9406 -601 8 -248 C ATOM 289 O LEU B1038 26.948 42.090 -21.348 1.00 76.06 O ANISOU 289 O LEU B1038 10388 9158 9352 -696 -21 -230 O ATOM 290 CB LEU B1038 26.636 43.670 -18.626 1.00 70.81 C ANISOU 290 CB LEU B1038 9759 8301 8844 -634 -182 -171 C ATOM 291 CG LEU B1038 25.618 44.459 -17.794 1.00 75.15 C ANISOU 291 CG LEU B1038 10406 8686 9463 -555 -292 -179 C ATOM 292 CD1 LEU B1038 26.304 45.521 -16.960 1.00 75.68 C ANISOU 292 CD1 LEU B1038 10549 8714 9492 -628 -369 -129 C ATOM 293 CD2 LEU B1038 24.540 45.086 -18.673 1.00 78.21 C ANISOU 293 CD2 LEU B1038 10914 8956 9848 -556 -410 -175 C ATOM 294 N ASP B1039 28.112 40.891 -19.810 1.00 73.15 N ANISOU 294 N ASP B1039 9785 8912 9098 -549 117 -282 N ATOM 295 CA ASP B1039 29.061 40.262 -20.729 1.00 74.38 C ANISOU 295 CA ASP B1039 9859 9235 9167 -568 238 -318 C ATOM 296 C ASP B1039 28.385 39.098 -21.461 1.00 78.37 C ANISOU 296 C ASP B1039 10408 9698 9671 -457 275 -406 C ATOM 297 O ASP B1039 28.609 38.920 -22.660 1.00 79.12 O ANISOU 297 O ASP B1039 10546 9871 9644 -503 336 -436 O ATOM 298 CB ASP B1039 30.299 39.769 -19.963 1.00 76.75 C ANISOU 298 CB ASP B1039 9978 9668 9517 -516 316 -330 C ATOM 299 CG ASP B1039 31.571 39.798 -20.777 1.00 89.68 C ANISOU 299 CG ASP B1039 11493 11532 11049 -596 434 -328 C ATOM 300 OD1 ASP B1039 31.730 38.927 -21.660 1.00 91.41 O ANISOU 300 OD1 ASP B1039 11685 11834 11213 -517 541 -416 O ATOM 301 OD2 ASP B1039 32.417 40.681 -20.523 1.00 96.52 O ANISOU 301 OD2 ASP B1039 12291 12501 11883 -740 420 -239 O ATOM 302 N ALA B1040 27.550 38.318 -20.736 1.00 73.94 N ANISOU 302 N ALA B1040 9853 9013 9228 -328 233 -443 N ATOM 303 CA ALA B1040 26.792 37.179 -21.266 1.00 73.83 C ANISOU 303 CA ALA B1040 9899 8924 9227 -237 226 -511 C ATOM 304 C ALA B1040 25.649 37.643 -22.174 1.00 77.87 C ANISOU 304 C ALA B1040 10554 9337 9697 -311 135 -483 C ATOM 305 O ALA B1040 25.289 36.930 -23.113 1.00 77.78 O ANISOU 305 O ALA B1040 10628 9296 9629 -296 130 -529 O ATOM 306 CB ALA B1040 26.246 36.339 -20.124 1.00 73.66 C ANISOU 306 CB ALA B1040 9842 8808 9338 -126 188 -526 C ATOM 307 N GLN B1041 25.094 38.844 -21.891 1.00 74.52 N ANISOU 307 N GLN B1041 10168 8847 9299 -385 44 -411 N ATOM 308 CA GLN B1041 24.015 39.505 -22.639 1.00 74.79 C ANISOU 308 CA GLN B1041 10327 8773 9317 -451 -80 -372 C ATOM 309 C GLN B1041 24.462 39.820 -24.080 1.00 81.15 C ANISOU 309 C GLN B1041 11249 9634 9951 -580 -74 -362 C ATOM 310 O GLN B1041 23.646 39.763 -25.003 1.00 81.04 O ANISOU 310 O GLN B1041 11357 9534 9899 -619 -165 -355 O ATOM 311 CB GLN B1041 23.603 40.795 -21.910 1.00 75.61 C ANISOU 311 CB GLN B1041 10444 8802 9483 -474 -176 -313 C ATOM 312 CG GLN B1041 22.246 41.364 -22.314 1.00 87.72 C ANISOU 312 CG GLN B1041 12063 10195 11070 -473 -329 -285 C ATOM 313 CD GLN B1041 21.922 42.630 -21.556 1.00104.35 C ANISOU 313 CD GLN B1041 14192 12222 13234 -456 -421 -252 C ATOM 314 OE1 GLN B1041 22.622 43.646 -21.652 1.00100.06 O ANISOU 314 OE1 GLN B1041 13730 11680 12608 -554 -463 -209 O ATOM 315 NE2 GLN B1041 20.842 42.603 -20.793 1.00 95.17 N ANISOU 315 NE2 GLN B1041 12965 10990 12207 -334 -459 -273 N ATOM 316 N LYS B1042 25.759 40.145 -24.259 1.00 79.55 N ANISOU 316 N LYS B1042 11003 9583 9639 -660 31 -353 N ATOM 317 CA LYS B1042 26.379 40.453 -25.549 1.00 81.41 C ANISOU 317 CA LYS B1042 11328 9924 9680 -806 79 -340 C ATOM 318 C LYS B1042 26.616 39.183 -26.375 1.00 87.49 C ANISOU 318 C LYS B1042 12112 10766 10364 -732 195 -442 C ATOM 319 O LYS B1042 26.529 39.231 -27.603 1.00 88.44 O ANISOU 319 O LYS B1042 12378 10902 10324 -831 195 -447 O ATOM 320 CB LYS B1042 27.704 41.209 -25.346 1.00 84.71 C ANISOU 320 CB LYS B1042 11655 10514 10019 -928 162 -286 C ATOM 321 CG LYS B1042 27.537 42.639 -24.840 1.00 97.98 C ANISOU 321 CG LYS B1042 13401 12104 11722 -1049 14 -177 C ATOM 322 CD LYS B1042 28.880 43.293 -24.554 1.00108.31 C ANISOU 322 CD LYS B1042 14612 13581 12959 -1189 78 -110 C ATOM 323 N ALA B1043 26.919 38.055 -25.701 1.00 84.60 N ANISOU 323 N ALA B1043 11622 10428 10094 -559 281 -525 N ATOM 324 CA ALA B1043 27.187 36.755 -26.326 1.00 85.89 C ANISOU 324 CA ALA B1043 11810 10632 10192 -444 376 -643 C ATOM 325 C ALA B1043 25.929 36.082 -26.898 1.00 90.53 C ANISOU 325 C ALA B1043 12573 11037 10786 -414 253 -669 C ATOM 326 O ALA B1043 24.813 36.403 -26.488 1.00 88.82 O ANISOU 326 O ALA B1043 12390 10672 10686 -436 104 -601 O ATOM 327 CB ALA B1043 27.874 35.830 -25.330 1.00 86.33 C ANISOU 327 CB ALA B1043 11697 10739 10366 -267 456 -712 C ATOM 328 N THR B1044 26.123 35.148 -27.853 1.00 89.43 N ANISOU 328 N THR B1044 12544 10917 10519 -360 313 -769 N ATOM 329 CA THR B1044 25.054 34.385 -28.505 1.00 89.91 C ANISOU 329 CA THR B1044 12798 10804 10560 -344 187 -798 C ATOM 330 C THR B1044 25.070 32.934 -27.975 1.00 94.87 C ANISOU 330 C THR B1044 13407 11361 11276 -156 189 -895 C ATOM 331 O THR B1044 26.124 32.293 -28.022 1.00 95.54 O ANISOU 331 O THR B1044 13438 11558 11305 -30 330 -1005 O ATOM 332 CB THR B1044 25.187 34.464 -30.042 1.00 99.39 C ANISOU 332 CB THR B1044 14205 12041 11517 -447 218 -837 C ATOM 333 OG1 THR B1044 25.402 35.821 -30.437 1.00 99.44 O ANISOU 333 OG1 THR B1044 14222 12132 11430 -635 222 -740 O ATOM 334 CG2 THR B1044 23.969 33.905 -30.771 1.00 97.84 C ANISOU 334 CG2 THR B1044 14239 11642 11295 -478 37 -835 C ATOM 335 N PRO B1045 23.927 32.401 -27.468 1.00 91.31 N ANISOU 335 N PRO B1045 12997 10732 10964 -138 26 -853 N ATOM 336 CA PRO B1045 23.927 31.021 -26.940 1.00 91.60 C ANISOU 336 CA PRO B1045 13048 10681 11075 10 -4 -927 C ATOM 337 C PRO B1045 24.090 29.929 -28.009 1.00 98.26 C ANISOU 337 C PRO B1045 14106 11461 11767 87 -9 -1053 C ATOM 338 O PRO B1045 23.823 30.218 -29.178 1.00 98.71 O ANISOU 338 O PRO B1045 14330 11506 11669 -9 -28 -1059 O ATOM 339 CB PRO B1045 22.574 30.923 -26.224 1.00 92.04 C ANISOU 339 CB PRO B1045 13091 10588 11293 -51 -178 -820 C ATOM 340 CG PRO B1045 21.707 31.892 -26.924 1.00 96.19 C ANISOU 340 CG PRO B1045 13680 11080 11789 -200 -270 -733 C ATOM 341 CD PRO B1045 22.598 33.030 -27.320 1.00 91.89 C ANISOU 341 CD PRO B1045 13092 10684 11138 -252 -143 -733 C ATOM 342 N PRO B1046 24.513 28.677 -27.654 1.00 96.44 N ANISOU 342 N PRO B1046 13905 11171 11565 259 -10 -1157 N ATOM 343 CA PRO B1046 24.643 27.622 -28.684 1.00 98.65 C ANISOU 343 CA PRO B1046 14428 11364 11689 354 -31 -1296 C ATOM 344 C PRO B1046 23.324 27.338 -29.406 1.00103.55 C ANISOU 344 C PRO B1046 15294 11787 12264 220 -238 -1238 C ATOM 345 O PRO B1046 23.325 27.146 -30.621 1.00104.74 O ANISOU 345 O PRO B1046 15667 11907 12222 202 -238 -1313 O ATOM 346 CB PRO B1046 25.147 26.405 -27.897 1.00100.91 C ANISOU 346 CB PRO B1046 14697 11575 12068 558 -57 -1388 C ATOM 347 CG PRO B1046 24.777 26.678 -26.480 1.00103.28 C ANISOU 347 CG PRO B1046 14807 11857 12578 504 -124 -1256 C ATOM 348 CD PRO B1046 24.881 28.162 -26.318 1.00 97.37 C ANISOU 348 CD PRO B1046 13870 11278 11848 374 -15 -1156 C ATOM 349 N LYS B1047 22.199 27.363 -28.660 1.00 99.41 N ANISOU 349 N LYS B1047 14719 11144 11909 114 -410 -1098 N ATOM 350 CA LYS B1047 20.843 27.205 -29.185 1.00 99.81 C ANISOU 350 CA LYS B1047 14934 11026 11963 -39 -628 -1005 C ATOM 351 C LYS B1047 20.485 28.516 -29.886 1.00104.49 C ANISOU 351 C LYS B1047 15510 11692 12500 -191 -618 -925 C ATOM 352 O LYS B1047 20.996 29.565 -29.484 1.00103.28 O ANISOU 352 O LYS B1047 15167 11694 12381 -201 -483 -892 O ATOM 353 CB LYS B1047 19.864 26.928 -28.036 1.00101.03 C ANISOU 353 CB LYS B1047 14964 11094 12328 -103 -774 -876 C ATOM 354 CG LYS B1047 18.920 25.769 -28.319 1.00116.58 C ANISOU 354 CG LYS B1047 17147 12852 14299 -167 -1009 -847 C ATOM 355 CD LYS B1047 18.469 25.052 -27.049 1.00125.56 C ANISOU 355 CD LYS B1047 18182 13924 15600 -180 -1103 -769 C ATOM 356 CE LYS B1047 19.356 23.878 -26.702 1.00137.20 C ANISOU 356 CE LYS B1047 19773 15319 17036 -12 -1095 -891 C ATOM 357 NZ LYS B1047 18.815 23.093 -25.563 1.00146.43 N ANISOU 357 NZ LYS B1047 20905 16394 18338 -70 -1233 -796 N ATOM 358 N LEU B1048 19.627 28.461 -30.934 1.00102.63 N ANISOU 358 N LEU B1048 15493 11330 12172 -316 -785 -888 N ATOM 359 CA LEU B1048 19.204 29.600 -31.776 1.00102.92 C ANISOU 359 CA LEU B1048 15580 11389 12135 -473 -833 -810 C ATOM 360 C LEU B1048 20.422 30.459 -32.249 1.00107.46 C ANISOU 360 C LEU B1048 16131 12156 12542 -460 -606 -877 C ATOM 361 O LEU B1048 20.371 31.693 -32.272 1.00106.16 O ANISOU 361 O LEU B1048 15875 12067 12393 -564 -592 -790 O ATOM 362 CB LEU B1048 18.060 30.458 -31.154 1.00101.67 C ANISOU 362 CB LEU B1048 15237 11202 12189 -582 -976 -642 C ATOM 363 CG LEU B1048 18.220 31.065 -29.749 1.00104.44 C ANISOU 363 CG LEU B1048 15280 11668 12733 -520 -870 -593 C ATOM 364 CD1 LEU B1048 18.281 32.578 -29.803 1.00103.90 C ANISOU 364 CD1 LEU B1048 15113 11686 12676 -586 -835 -528 C ATOM 365 CD2 LEU B1048 17.093 30.625 -28.836 1.00106.22 C ANISOU 365 CD2 LEU B1048 15372 11817 13169 -539 -1008 -498 C ATOM 366 N GLU B1049 21.510 29.760 -32.648 1.00105.76 N ANISOU 366 N GLU B1049 16006 12017 12162 -331 -437 -1036 N ATOM 367 CA GLU B1049 22.773 30.329 -33.129 1.00106.65 C ANISOU 367 CA GLU B1049 16079 12346 12095 -311 -193 -1117 C ATOM 368 C GLU B1049 22.590 31.001 -34.490 1.00112.30 C ANISOU 368 C GLU B1049 17022 13068 12578 -493 -223 -1090 C ATOM 369 O GLU B1049 23.014 32.145 -34.660 1.00111.89 O ANISOU 369 O GLU B1049 16889 13160 12463 -612 -133 -1027 O ATOM 370 CB GLU B1049 23.852 29.234 -33.204 1.00109.59 C ANISOU 370 CB GLU B1049 16480 12790 12369 -93 -22 -1308 C ATOM 371 CG GLU B1049 25.279 29.752 -33.186 1.00121.54 C ANISOU 371 CG GLU B1049 17803 14583 13792 -29 260 -1381 C ATOM 372 CD GLU B1049 26.331 28.666 -33.283 1.00145.32 C ANISOU 372 CD GLU B1049 20815 17676 16724 220 426 -1584 C ATOM 373 OE1 GLU B1049 26.931 28.516 -34.371 1.00141.70 O ANISOU 373 OE1 GLU B1049 20498 17328 16014 247 576 -1710 O ATOM 374 OE2 GLU B1049 26.550 27.956 -32.274 1.00139.70 O ANISOU 374 OE2 GLU B1049 19971 16915 16195 395 402 -1623 O ATOM 375 N ASP B1050 21.953 30.297 -35.450 1.00110.61 N ANISOU 375 N ASP B1050 17114 12684 12227 -533 -369 -1130 N ATOM 376 CA ASP B1050 21.686 30.814 -36.792 1.00112.25 C ANISOU 376 CA ASP B1050 17593 12863 12194 -720 -435 -1102 C ATOM 377 C ASP B1050 20.370 31.612 -36.783 1.00115.15 C ANISOU 377 C ASP B1050 17973 13073 12707 -908 -716 -910 C ATOM 378 O ASP B1050 19.375 31.213 -37.397 1.00115.56 O ANISOU 378 O ASP B1050 18249 12924 12735 -997 -956 -867 O ATOM 379 CB ASP B1050 21.683 29.675 -37.831 1.00116.59 C ANISOU 379 CB ASP B1050 18492 13298 12509 -668 -464 -1246 C ATOM 380 CG ASP B1050 21.813 30.156 -39.262 1.00128.80 C ANISOU 380 CG ASP B1050 20332 14878 13730 -841 -442 -1262 C ATOM 381 OD1 ASP B1050 22.956 30.410 -39.701 1.00130.55 O ANISOU 381 OD1 ASP B1050 20538 15330 13735 -816 -166 -1364 O ATOM 382 OD2 ASP B1050 20.775 30.265 -39.948 1.00135.42 O ANISOU 382 OD2 ASP B1050 21414 15518 14521 -1012 -705 -1167 O ATOM 383 N LYS B1051 20.376 32.737 -36.044 1.00110.04 N ANISOU 383 N LYS B1051 17076 12514 12220 -957 -697 -798 N ATOM 384 CA LYS B1051 19.242 33.644 -35.877 1.00108.85 C ANISOU 384 CA LYS B1051 16877 12243 12238 -1087 -938 -630 C ATOM 385 C LYS B1051 19.740 35.080 -35.730 1.00112.06 C ANISOU 385 C LYS B1051 17167 12779 12631 -1181 -864 -554 C ATOM 386 O LYS B1051 20.710 35.326 -35.008 1.00110.85 O ANISOU 386 O LYS B1051 16813 12800 12506 -1101 -650 -593 O ATOM 387 CB LYS B1051 18.403 33.238 -34.651 1.00109.57 C ANISOU 387 CB LYS B1051 16740 12250 12642 -985 -1047 -575 C ATOM 388 CG LYS B1051 16.893 33.256 -34.895 1.00124.61 C ANISOU 388 CG LYS B1051 18706 13959 14680 -1087 -1359 -453 C ATOM 389 CD LYS B1051 16.347 31.906 -35.385 1.00135.76 C ANISOU 389 CD LYS B1051 20324 15217 16042 -1089 -1499 -491 C ATOM 390 CE LYS B1051 15.908 31.000 -34.258 1.00144.90 C ANISOU 390 CE LYS B1051 21295 16340 17420 -984 -1525 -482 C ATOM 391 NZ LYS B1051 15.442 29.681 -34.759 1.00155.05 N ANISOU 391 NZ LYS B1051 22817 17457 18637 -1005 -1684 -514 N ATOM 392 N SER B1052 19.075 36.023 -36.421 1.00109.16 N ANISOU 392 N SER B1052 16943 12311 12221 -1358 -1067 -439 N ATOM 393 CA SER B1052 19.401 37.453 -36.417 1.00108.82 C ANISOU 393 CA SER B1052 16860 12335 12150 -1481 -1071 -347 C ATOM 394 C SER B1052 19.172 38.099 -35.032 1.00109.93 C ANISOU 394 C SER B1052 16699 12488 12581 -1377 -1085 -288 C ATOM 395 O SER B1052 18.321 37.608 -34.288 1.00108.29 O ANISOU 395 O SER B1052 16349 12191 12606 -1258 -1179 -278 O ATOM 396 CB SER B1052 18.580 38.180 -37.480 1.00114.07 C ANISOU 396 CB SER B1052 17784 12835 12721 -1682 -1349 -236 C ATOM 397 OG SER B1052 17.188 38.059 -37.236 1.00122.76 O ANISOU 397 OG SER B1052 18843 13738 14064 -1645 -1626 -161 O ATOM 398 N PRO B1053 19.885 39.198 -34.662 1.00105.77 N ANISOU 398 N PRO B1053 16084 12069 12035 -1430 -1002 -244 N ATOM 399 CA PRO B1053 19.646 39.816 -33.342 1.00103.67 C ANISOU 399 CA PRO B1053 15569 11795 12025 -1323 -1025 -201 C ATOM 400 C PRO B1053 18.285 40.511 -33.210 1.00106.90 C ANISOU 400 C PRO B1053 15978 12009 12628 -1324 -1314 -104 C ATOM 401 O PRO B1053 17.839 40.749 -32.089 1.00105.10 O ANISOU 401 O PRO B1053 15540 11763 12631 -1192 -1333 -93 O ATOM 402 CB PRO B1053 20.808 40.809 -33.188 1.00105.65 C ANISOU 402 CB PRO B1053 15790 12194 12159 -1417 -892 -174 C ATOM 403 CG PRO B1053 21.773 40.484 -34.292 1.00111.89 C ANISOU 403 CG PRO B1053 16742 13126 12645 -1546 -733 -221 C ATOM 404 CD PRO B1053 20.943 39.922 -35.394 1.00108.69 C ANISOU 404 CD PRO B1053 16581 12578 12141 -1605 -886 -228 C ATOM 405 N ASP B1054 17.622 40.815 -34.346 1.00104.74 N ANISOU 405 N ASP B1054 15939 11596 12261 -1466 -1540 -39 N ATOM 406 CA ASP B1054 16.304 41.461 -34.394 1.00104.86 C ANISOU 406 CA ASP B1054 15961 11419 12461 -1464 -1848 53 C ATOM 407 C ASP B1054 15.153 40.492 -34.058 1.00107.44 C ANISOU 407 C ASP B1054 16152 11668 13000 -1345 -1947 45 C ATOM 408 O ASP B1054 14.034 40.944 -33.805 1.00107.27 O ANISOU 408 O ASP B1054 16032 11532 13193 -1293 -2164 110 O ATOM 409 CB ASP B1054 16.071 42.120 -35.768 1.00108.92 C ANISOU 409 CB ASP B1054 16792 11804 12788 -1678 -2079 136 C ATOM 410 CG ASP B1054 17.037 43.240 -36.104 1.00120.27 C ANISOU 410 CG ASP B1054 18374 13300 14025 -1839 -2038 181 C ATOM 411 OD1 ASP B1054 16.973 44.299 -35.441 1.00120.52 O ANISOU 411 OD1 ASP B1054 18320 13287 14185 -1801 -2123 229 O ATOM 412 OD2 ASP B1054 17.829 43.074 -37.056 1.00127.60 O ANISOU 412 OD2 ASP B1054 19513 14313 14655 -2013 -1933 170 O ATOM 413 N SER B1055 15.432 39.169 -34.062 1.00102.92 N ANISOU 413 N SER B1055 15576 11160 12368 -1304 -1798 -32 N ATOM 414 CA SER B1055 14.482 38.087 -33.778 1.00102.23 C ANISOU 414 CA SER B1055 15391 11010 12441 -1232 -1882 -33 C ATOM 415 C SER B1055 13.879 38.192 -32.360 1.00103.85 C ANISOU 415 C SER B1055 15263 11256 12939 -1075 -1857 -16 C ATOM 416 O SER B1055 14.611 38.554 -31.434 1.00102.25 O ANISOU 416 O SER B1055 14916 11170 12766 -984 -1663 -59 O ATOM 417 CB SER B1055 15.164 36.734 -33.958 1.00105.84 C ANISOU 417 CB SER B1055 15938 11528 12750 -1208 -1708 -135 C ATOM 418 OG SER B1055 14.235 35.663 -33.984 1.00115.40 O ANISOU 418 OG SER B1055 17150 12637 14059 -1199 -1847 -118 O ATOM 419 N PRO B1056 12.566 37.879 -32.163 1.00100.04 N ANISOU 419 N PRO B1056 14653 10693 12664 -1051 -2045 48 N ATOM 420 CA PRO B1056 11.968 37.989 -30.815 1.00 98.53 C ANISOU 420 CA PRO B1056 14136 10572 12729 -908 -1994 60 C ATOM 421 C PRO B1056 12.597 37.106 -29.737 1.00 99.52 C ANISOU 421 C PRO B1056 14120 10826 12867 -818 -1742 -11 C ATOM 422 O PRO B1056 12.610 37.506 -28.572 1.00 98.14 O ANISOU 422 O PRO B1056 13727 10739 12823 -705 -1626 -25 O ATOM 423 CB PRO B1056 10.494 37.631 -31.043 1.00101.70 C ANISOU 423 CB PRO B1056 14443 10888 13312 -940 -2242 149 C ATOM 424 CG PRO B1056 10.265 37.839 -32.499 1.00107.93 C ANISOU 424 CG PRO B1056 15514 11525 13968 -1089 -2479 200 C ATOM 425 CD PRO B1056 11.554 37.458 -33.153 1.00103.21 C ANISOU 425 CD PRO B1056 15192 10948 13073 -1164 -2317 121 C ATOM 426 N GLU B1057 13.112 35.917 -30.115 1.00 95.07 N ANISOU 426 N GLU B1057 13698 10260 12163 -860 -1672 -60 N ATOM 427 CA GLU B1057 13.771 34.995 -29.181 1.00 93.26 C ANISOU 427 CA GLU B1057 13375 10125 11935 -776 -1467 -128 C ATOM 428 C GLU B1057 15.129 35.524 -28.716 1.00 94.20 C ANISOU 428 C GLU B1057 13474 10361 11958 -705 -1238 -204 C ATOM 429 O GLU B1057 15.503 35.304 -27.562 1.00 92.59 O ANISOU 429 O GLU B1057 13104 10243 11832 -612 -1090 -234 O ATOM 430 CB GLU B1057 13.869 33.555 -29.730 1.00 95.46 C ANISOU 430 CB GLU B1057 13831 10335 12102 -820 -1499 -166 C ATOM 431 CG GLU B1057 14.314 33.431 -31.178 1.00108.14 C ANISOU 431 CG GLU B1057 15750 11864 13473 -907 -1555 -208 C ATOM 432 CD GLU B1057 13.172 33.265 -32.161 1.00131.33 C ANISOU 432 CD GLU B1057 18837 14647 16417 -1040 -1838 -123 C ATOM 433 OE1 GLU B1057 12.466 34.264 -32.429 1.00126.59 O ANISOU 433 OE1 GLU B1057 18187 14008 15904 -1093 -1992 -37 O ATOM 434 OE2 GLU B1057 12.989 32.138 -32.674 1.00127.04 O ANISOU 434 OE2 GLU B1057 18474 14005 15789 -1088 -1928 -143 O ATOM 435 N MET B1058 15.848 36.241 -29.605 1.00 90.07 N ANISOU 435 N MET B1058 13119 9843 11261 -771 -1220 -223 N ATOM 436 CA MET B1058 17.140 36.865 -29.301 1.00 88.68 C ANISOU 436 CA MET B1058 12922 9789 10984 -744 -1026 -272 C ATOM 437 C MET B1058 16.946 38.085 -28.401 1.00 90.40 C ANISOU 437 C MET B1058 12979 10028 11341 -700 -1037 -224 C ATOM 438 O MET B1058 17.785 38.346 -27.536 1.00 88.88 O ANISOU 438 O MET B1058 12679 9936 11155 -639 -877 -257 O ATOM 439 CB MET B1058 17.884 37.249 -30.586 1.00 92.18 C ANISOU 439 CB MET B1058 13597 10247 11182 -866 -1012 -288 C ATOM 440 CG MET B1058 18.813 36.166 -31.085 1.00 96.39 C ANISOU 440 CG MET B1058 14240 10852 11534 -845 -853 -393 C ATOM 441 SD MET B1058 20.545 36.460 -30.650 1.00100.20 S ANISOU 441 SD MET B1058 14616 11551 11903 -800 -566 -466 S ATOM 442 CE MET B1058 20.626 35.689 -29.060 1.00 95.19 C ANISOU 442 CE MET B1058 13736 10949 11482 -618 -475 -504 C ATOM 443 N LYS B1059 15.827 38.815 -28.600 1.00 86.65 N ANISOU 443 N LYS B1059 12494 9448 10981 -720 -1240 -152 N ATOM 444 CA LYS B1059 15.427 39.985 -27.813 1.00 85.71 C ANISOU 444 CA LYS B1059 12245 9316 11007 -647 -1290 -120 C ATOM 445 C LYS B1059 15.069 39.549 -26.388 1.00 87.69 C ANISOU 445 C LYS B1059 12249 9638 11432 -510 -1179 -145 C ATOM 446 O LYS B1059 15.351 40.275 -25.432 1.00 86.58 O ANISOU 446 O LYS B1059 12009 9541 11345 -428 -1099 -163 O ATOM 447 CB LYS B1059 14.225 40.687 -28.466 1.00 89.36 C ANISOU 447 CB LYS B1059 12750 9638 11564 -675 -1558 -49 C ATOM 448 CG LYS B1059 14.575 41.511 -29.696 1.00104.08 C ANISOU 448 CG LYS B1059 14875 11414 13257 -821 -1697 -8 C ATOM 449 CD LYS B1059 13.338 42.158 -30.296 1.00115.57 C ANISOU 449 CD LYS B1059 16373 12709 14830 -835 -1999 67 C ATOM 450 CE LYS B1059 13.689 43.205 -31.321 1.00128.48 C ANISOU 450 CE LYS B1059 18275 14238 16302 -981 -2161 120 C ATOM 451 NZ LYS B1059 12.475 43.837 -31.897 1.00140.04 N ANISOU 451 NZ LYS B1059 19788 15524 17896 -983 -2491 195 N ATOM 452 N ASP B1060 14.457 38.354 -26.259 1.00 83.75 N ANISOU 452 N ASP B1060 11674 9145 11001 -502 -1183 -141 N ATOM 453 CA ASP B1060 14.053 37.742 -24.995 1.00 82.73 C ANISOU 453 CA ASP B1060 11332 9090 11010 -416 -1085 -148 C ATOM 454 C ASP B1060 15.271 37.268 -24.193 1.00 84.41 C ANISOU 454 C ASP B1060 11533 9396 11143 -375 -873 -211 C ATOM 455 O ASP B1060 15.222 37.270 -22.960 1.00 83.60 O ANISOU 455 O ASP B1060 11276 9361 11127 -299 -772 -221 O ATOM 456 CB ASP B1060 13.085 36.579 -25.252 1.00 85.48 C ANISOU 456 CB ASP B1060 11644 9405 11427 -471 -1188 -103 C ATOM 457 CG ASP B1060 12.396 36.081 -24.001 1.00 96.55 C ANISOU 457 CG ASP B1060 12812 10892 12980 -419 -1121 -80 C ATOM 458 OD1 ASP B1060 11.389 36.698 -23.593 1.00 98.13 O ANISOU 458 OD1 ASP B1060 12830 11121 13335 -369 -1178 -43 O ATOM 459 OD2 ASP B1060 12.872 35.085 -23.422 1.00101.94 O ANISOU 459 OD2 ASP B1060 13494 11615 13622 -427 -1011 -102 O ATOM 460 N PHE B1061 16.358 36.863 -24.893 1.00 79.64 N ANISOU 460 N PHE B1061 11087 8801 10371 -422 -808 -256 N ATOM 461 CA PHE B1061 17.618 36.425 -24.284 1.00 77.93 C ANISOU 461 CA PHE B1061 10854 8673 10082 -375 -627 -318 C ATOM 462 C PHE B1061 18.297 37.610 -23.596 1.00 79.84 C ANISOU 462 C PHE B1061 11035 8978 10324 -345 -546 -320 C ATOM 463 O PHE B1061 18.740 37.473 -22.456 1.00 78.73 O ANISOU 463 O PHE B1061 10787 8898 10228 -280 -437 -339 O ATOM 464 CB PHE B1061 18.544 35.779 -25.335 1.00 80.23 C ANISOU 464 CB PHE B1061 11313 8975 10196 -415 -580 -376 C ATOM 465 CG PHE B1061 19.886 35.310 -24.815 1.00 81.32 C ANISOU 465 CG PHE B1061 11411 9215 10271 -347 -404 -447 C ATOM 466 CD1 PHE B1061 20.001 34.112 -24.119 1.00 84.19 C ANISOU 466 CD1 PHE B1061 11728 9573 10687 -270 -364 -484 C ATOM 467 CD2 PHE B1061 21.037 36.053 -25.046 1.00 83.56 C ANISOU 467 CD2 PHE B1061 11704 9599 10444 -371 -299 -468 C ATOM 468 CE1 PHE B1061 21.242 33.676 -23.643 1.00 84.96 C ANISOU 468 CE1 PHE B1061 11782 9753 10745 -190 -229 -551 C ATOM 469 CE2 PHE B1061 22.277 35.618 -24.567 1.00 86.30 C ANISOU 469 CE2 PHE B1061 11979 10055 10754 -303 -148 -529 C ATOM 470 CZ PHE B1061 22.373 34.429 -23.877 1.00 84.17 C ANISOU 470 CZ PHE B1061 11659 9768 10553 -199 -118 -575 C ATOM 471 N ARG B1062 18.348 38.773 -24.279 1.00 75.87 N ANISOU 471 N ARG B1062 10623 8442 9764 -406 -624 -290 N ATOM 472 CA ARG B1062 18.929 40.009 -23.750 1.00 74.98 C ANISOU 472 CA ARG B1062 10498 8354 9637 -404 -597 -278 C ATOM 473 C ARG B1062 18.072 40.575 -22.619 1.00 77.70 C ANISOU 473 C ARG B1062 10716 8665 10141 -300 -632 -269 C ATOM 474 O ARG B1062 18.623 41.116 -21.659 1.00 76.97 O ANISOU 474 O ARG B1062 10579 8610 10056 -257 -557 -284 O ATOM 475 CB ARG B1062 19.127 41.055 -24.857 1.00 75.78 C ANISOU 475 CB ARG B1062 10766 8404 9622 -523 -709 -236 C ATOM 476 CG ARG B1062 20.262 40.722 -25.823 1.00 85.38 C ANISOU 476 CG ARG B1062 12097 9705 10639 -636 -618 -252 C ATOM 477 CD ARG B1062 20.583 41.872 -26.762 1.00 94.56 C ANISOU 477 CD ARG B1062 13429 10839 11660 -791 -715 -194 C ATOM 478 NE ARG B1062 19.474 42.181 -27.669 1.00101.15 N ANISOU 478 NE ARG B1062 14397 11527 12508 -842 -926 -148 N ATOM 479 CZ ARG B1062 19.315 41.646 -28.875 1.00114.45 C ANISOU 479 CZ ARG B1062 16228 13187 14070 -934 -973 -147 C ATOM 480 NH1 ARG B1062 20.194 40.769 -29.343 1.00 99.92 N ANISOU 480 NH1 ARG B1062 14423 11466 12078 -967 -805 -205 N ATOM 481 NH2 ARG B1062 18.275 41.987 -29.624 1.00102.74 N ANISOU 481 NH2 ARG B1062 14865 11555 12615 -985 -1198 -93 N ATOM 482 N HIS B1063 16.731 40.426 -22.719 1.00 73.92 N ANISOU 482 N HIS B1063 10173 8127 9787 -258 -742 -248 N ATOM 483 CA HIS B1063 15.786 40.885 -21.697 1.00 73.65 C ANISOU 483 CA HIS B1063 9988 8090 9907 -140 -755 -253 C ATOM 484 C HIS B1063 15.903 40.063 -20.406 1.00 76.32 C ANISOU 484 C HIS B1063 10185 8525 10287 -82 -592 -280 C ATOM 485 O HIS B1063 15.677 40.599 -19.320 1.00 75.71 O ANISOU 485 O HIS B1063 10019 8478 10270 10 -534 -304 O ATOM 486 CB HIS B1063 14.343 40.895 -22.225 1.00 75.51 C ANISOU 486 CB HIS B1063 10155 8264 10271 -118 -917 -216 C ATOM 487 CG HIS B1063 13.362 41.489 -21.262 1.00 79.55 C ANISOU 487 CG HIS B1063 10489 8796 10940 25 -921 -233 C ATOM 488 ND1 HIS B1063 13.282 42.856 -21.064 1.00 81.95 N ANISOU 488 ND1 HIS B1063 10835 9031 11272 120 -995 -260 N ATOM 489 CD2 HIS B1063 12.475 40.877 -20.444 1.00 81.57 C ANISOU 489 CD2 HIS B1063 10533 9142 11316 87 -851 -233 C ATOM 490 CE1 HIS B1063 12.344 43.031 -20.148 1.00 82.10 C ANISOU 490 CE1 HIS B1063 10661 9103 11430 265 -956 -293 C ATOM 491 NE2 HIS B1063 11.830 41.869 -19.745 1.00 82.29 N ANISOU 491 NE2 HIS B1063 10515 9240 11510 240 -857 -273 N ATOM 492 N GLY B1064 16.272 38.786 -20.544 1.00 72.32 N ANISOU 492 N GLY B1064 9686 8057 9737 -136 -530 -281 N ATOM 493 CA GLY B1064 16.487 37.870 -19.427 1.00 71.46 C ANISOU 493 CA GLY B1064 9486 8018 9647 -110 -405 -295 C ATOM 494 C GLY B1064 17.579 38.364 -18.500 1.00 74.28 C ANISOU 494 C GLY B1064 9855 8420 9949 -73 -292 -328 C ATOM 495 O GLY B1064 17.433 38.299 -17.275 1.00 73.75 O ANISOU 495 O GLY B1064 9703 8398 9922 -25 -213 -336 O ATOM 496 N PHE B1065 18.664 38.908 -19.087 1.00 70.20 N ANISOU 496 N PHE B1065 9446 7897 9331 -112 -291 -339 N ATOM 497 CA PHE B1065 19.781 39.480 -18.341 1.00 69.33 C ANISOU 497 CA PHE B1065 9350 7826 9165 -105 -215 -354 C ATOM 498 C PHE B1065 19.445 40.864 -17.787 1.00 73.54 C ANISOU 498 C PHE B1065 9900 8316 9726 -62 -261 -352 C ATOM 499 O PHE B1065 20.018 41.252 -16.770 1.00 73.10 O ANISOU 499 O PHE B1065 9843 8279 9652 -38 -206 -363 O ATOM 500 CB PHE B1065 21.071 39.488 -19.175 1.00 71.01 C ANISOU 500 CB PHE B1065 9641 8080 9258 -182 -190 -356 C ATOM 501 CG PHE B1065 21.629 38.102 -19.398 1.00 72.29 C ANISOU 501 CG PHE B1065 9785 8291 9393 -173 -120 -389 C ATOM 502 CD1 PHE B1065 22.356 37.458 -18.403 1.00 74.90 C ANISOU 502 CD1 PHE B1065 10050 8669 9740 -128 -40 -408 C ATOM 503 CD2 PHE B1065 21.413 37.434 -20.596 1.00 74.78 C ANISOU 503 CD2 PHE B1065 10169 8586 9660 -203 -154 -404 C ATOM 504 CE1 PHE B1065 22.858 36.170 -18.604 1.00 75.93 C ANISOU 504 CE1 PHE B1065 10177 8819 9855 -94 -4 -448 C ATOM 505 CE2 PHE B1065 21.914 36.145 -20.796 1.00 77.76 C ANISOU 505 CE2 PHE B1065 10555 8984 10006 -168 -104 -452 C ATOM 506 CZ PHE B1065 22.634 35.522 -19.800 1.00 75.51 C ANISOU 506 CZ PHE B1065 10198 8741 9753 -105 -33 -477 C ATOM 507 N ASP B1066 18.492 41.588 -18.425 1.00 70.56 N ANISOU 507 N ASP B1066 9550 7864 9397 -43 -380 -340 N ATOM 508 CA ASP B1066 18.031 42.907 -17.973 1.00 70.90 C ANISOU 508 CA ASP B1066 9624 7836 9478 35 -454 -355 C ATOM 509 C ASP B1066 17.275 42.797 -16.643 1.00 75.02 C ANISOU 509 C ASP B1066 10020 8398 10087 162 -368 -397 C ATOM 510 O ASP B1066 17.356 43.711 -15.820 1.00 75.04 O ANISOU 510 O ASP B1066 10065 8367 10079 237 -363 -433 O ATOM 511 CB ASP B1066 17.172 43.603 -19.044 1.00 73.62 C ANISOU 511 CB ASP B1066 10027 8080 9866 38 -628 -334 C ATOM 512 CG ASP B1066 17.953 44.185 -20.210 1.00 82.78 C ANISOU 512 CG ASP B1066 11365 9182 10903 -100 -731 -289 C ATOM 513 OD1 ASP B1066 18.964 44.880 -19.962 1.00 83.12 O ANISOU 513 OD1 ASP B1066 11507 9223 10853 -159 -721 -278 O ATOM 514 OD2 ASP B1066 17.515 44.002 -21.365 1.00 88.54 O ANISOU 514 OD2 ASP B1066 12147 9870 11626 -163 -834 -257 O ATOM 515 N ILE B1067 16.565 41.666 -16.429 1.00 71.53 N ANISOU 515 N ILE B1067 9437 8028 9711 170 -301 -390 N ATOM 516 CA ILE B1067 15.839 41.354 -15.190 1.00 71.78 C ANISOU 516 CA ILE B1067 9333 8139 9803 251 -192 -417 C ATOM 517 C ILE B1067 16.889 41.031 -14.111 1.00 74.97 C ANISOU 517 C ILE B1067 9784 8584 10117 222 -75 -429 C ATOM 518 O ILE B1067 16.782 41.521 -12.984 1.00 74.87 O ANISOU 518 O ILE B1067 9767 8592 10089 295 -4 -469 O ATOM 519 CB ILE B1067 14.823 40.183 -15.396 1.00 75.29 C ANISOU 519 CB ILE B1067 9625 8651 10330 215 -181 -377 C ATOM 520 CG1 ILE B1067 13.786 40.518 -16.495 1.00 76.75 C ANISOU 520 CG1 ILE B1067 9760 8787 10614 234 -329 -354 C ATOM 521 CG2 ILE B1067 14.120 39.801 -14.080 1.00 76.62 C ANISOU 521 CG2 ILE B1067 9645 8934 10535 260 -48 -390 C ATOM 522 CD1 ILE B1067 13.197 39.321 -17.232 1.00 83.94 C ANISOU 522 CD1 ILE B1067 10608 9716 11569 131 -388 -290 C ATOM 523 N LEU B1068 17.916 40.232 -14.485 1.00 70.71 N ANISOU 523 N LEU B1068 9299 8053 9516 125 -63 -400 N ATOM 524 CA LEU B1068 19.024 39.810 -13.626 1.00 69.83 C ANISOU 524 CA LEU B1068 9226 7972 9335 90 12 -401 C ATOM 525 C LEU B1068 19.848 41.003 -13.113 1.00 73.77 C ANISOU 525 C LEU B1068 9828 8434 9770 103 -2 -417 C ATOM 526 O LEU B1068 20.095 41.072 -11.908 1.00 73.62 O ANISOU 526 O LEU B1068 9826 8428 9717 123 57 -432 O ATOM 527 CB LEU B1068 19.911 38.780 -14.357 1.00 69.24 C ANISOU 527 CB LEU B1068 9173 7910 9226 17 6 -381 C ATOM 528 CG LEU B1068 20.926 37.988 -13.517 1.00 73.52 C ANISOU 528 CG LEU B1068 9721 8483 9732 -3 61 -378 C ATOM 529 CD1 LEU B1068 20.248 36.908 -12.691 1.00 73.96 C ANISOU 529 CD1 LEU B1068 9725 8557 9820 -8 98 -363 C ATOM 530 CD2 LEU B1068 21.963 37.336 -14.405 1.00 75.65 C ANISOU 530 CD2 LEU B1068 10013 8765 9967 -33 48 -383 C ATOM 531 N VAL B1069 20.239 41.947 -14.010 1.00 70.26 N ANISOU 531 N VAL B1069 9469 7932 9294 74 -94 -407 N ATOM 532 CA VAL B1069 21.003 43.159 -13.653 1.00 70.30 C ANISOU 532 CA VAL B1069 9598 7882 9232 55 -148 -406 C ATOM 533 C VAL B1069 20.155 44.061 -12.733 1.00 74.84 C ANISOU 533 C VAL B1069 10212 8395 9827 177 -159 -460 C ATOM 534 O VAL B1069 20.675 44.595 -11.750 1.00 74.53 O ANISOU 534 O VAL B1069 10263 8327 9728 186 -151 -476 O ATOM 535 CB VAL B1069 21.589 43.910 -14.889 1.00 74.40 C ANISOU 535 CB VAL B1069 10213 8360 9696 -43 -257 -364 C ATOM 536 CG1 VAL B1069 22.300 45.200 -14.483 1.00 74.69 C ANISOU 536 CG1 VAL B1069 10395 8324 9659 -88 -344 -346 C ATOM 537 CG2 VAL B1069 22.550 43.018 -15.671 1.00 73.73 C ANISOU 537 CG2 VAL B1069 10081 8366 9565 -146 -208 -331 C ATOM 538 N GLY B1070 18.858 44.160 -13.035 1.00 72.16 N ANISOU 538 N GLY B1070 9799 8044 9574 277 -176 -492 N ATOM 539 CA GLY B1070 17.887 44.913 -12.247 1.00 73.29 C ANISOU 539 CA GLY B1070 9937 8156 9755 434 -165 -565 C ATOM 540 C GLY B1070 17.741 44.360 -10.841 1.00 77.60 C ANISOU 540 C GLY B1070 10423 8790 10272 475 -7 -600 C ATOM 541 O GLY B1070 17.650 45.130 -9.880 1.00 78.29 O ANISOU 541 O GLY B1070 10596 8842 10310 569 17 -665 O ATOM 542 N GLN B1071 17.758 43.014 -10.714 1.00 73.27 N ANISOU 542 N GLN B1071 9758 8345 9736 394 87 -557 N ATOM 543 CA GLN B1071 17.683 42.293 -9.438 1.00 73.05 C ANISOU 543 CA GLN B1071 9689 8404 9664 384 223 -566 C ATOM 544 C GLN B1071 18.986 42.443 -8.637 1.00 76.15 C ANISOU 544 C GLN B1071 10233 8755 9946 318 220 -555 C ATOM 545 O GLN B1071 18.926 42.564 -7.411 1.00 76.27 O ANISOU 545 O GLN B1071 10301 8788 9889 346 297 -589 O ATOM 546 CB GLN B1071 17.347 40.812 -9.663 1.00 73.80 C ANISOU 546 CB GLN B1071 9649 8588 9803 295 273 -507 C ATOM 547 CG GLN B1071 15.854 40.542 -9.847 1.00 87.02 C ANISOU 547 CG GLN B1071 11146 10345 11572 346 314 -512 C ATOM 548 CD GLN B1071 15.525 39.105 -10.193 1.00103.31 C ANISOU 548 CD GLN B1071 13108 12471 13676 229 319 -438 C ATOM 549 OE1 GLN B1071 16.323 38.178 -10.010 1.00 98.20 O ANISOU 549 OE1 GLN B1071 12524 11810 12976 128 318 -397 O ATOM 550 NE2 GLN B1071 14.316 38.884 -10.683 1.00 95.39 N ANISOU 550 NE2 GLN B1071 11948 11527 12771 241 306 -418 N ATOM 551 N ILE B1072 20.154 42.440 -9.333 1.00 71.58 N ANISOU 551 N ILE B1072 9717 8131 9349 224 131 -505 N ATOM 552 CA ILE B1072 21.491 42.620 -8.745 1.00 70.97 C ANISOU 552 CA ILE B1072 9755 8022 9190 145 97 -476 C ATOM 553 C ILE B1072 21.579 44.021 -8.112 1.00 75.69 C ANISOU 553 C ILE B1072 10516 8525 9717 197 40 -519 C ATOM 554 O ILE B1072 22.031 44.150 -6.970 1.00 75.48 O ANISOU 554 O ILE B1072 10592 8478 9609 181 57 -527 O ATOM 555 CB ILE B1072 22.621 42.350 -9.796 1.00 73.20 C ANISOU 555 CB ILE B1072 10019 8314 9480 43 28 -416 C ATOM 556 CG1 ILE B1072 22.817 40.836 -10.024 1.00 72.91 C ANISOU 556 CG1 ILE B1072 9869 8350 9484 7 80 -391 C ATOM 557 CG2 ILE B1072 23.959 43.011 -9.401 1.00 73.92 C ANISOU 557 CG2 ILE B1072 10215 8371 9499 -41 -46 -378 C ATOM 558 CD1 ILE B1072 23.415 40.437 -11.389 1.00 79.55 C ANISOU 558 CD1 ILE B1072 10658 9221 10346 -41 48 -367 C ATOM 559 N ASP B1073 21.109 45.052 -8.852 1.00 72.74 N ANISOU 559 N ASP B1073 10193 8076 9369 260 -46 -547 N ATOM 560 CA ASP B1073 21.087 46.456 -8.434 1.00 73.55 C ANISOU 560 CA ASP B1073 10483 8052 9412 328 -139 -596 C ATOM 561 C ASP B1073 20.233 46.693 -7.187 1.00 78.49 C ANISOU 561 C ASP B1073 11144 8679 10000 478 -39 -697 C ATOM 562 O ASP B1073 20.621 47.498 -6.339 1.00 79.11 O ANISOU 562 O ASP B1073 11416 8663 9977 500 -85 -734 O ATOM 563 CB ASP B1073 20.634 47.362 -9.591 1.00 75.77 C ANISOU 563 CB ASP B1073 10805 8241 9743 370 -273 -603 C ATOM 564 CG ASP B1073 21.658 47.563 -10.698 1.00 84.16 C ANISOU 564 CG ASP B1073 11917 9280 10781 197 -393 -506 C ATOM 565 OD1 ASP B1073 22.609 46.753 -10.788 1.00 83.21 O ANISOU 565 OD1 ASP B1073 11723 9253 10640 67 -341 -441 O ATOM 566 OD2 ASP B1073 21.497 48.517 -11.487 1.00 91.35 O ANISOU 566 OD2 ASP B1073 12935 10082 11690 193 -540 -497 O ATOM 567 N ASP B1074 19.088 45.983 -7.069 1.00 75.18 N ANISOU 567 N ASP B1074 10543 8373 9648 568 99 -737 N ATOM 568 CA ASP B1074 18.184 46.073 -5.916 1.00 76.59 C ANISOU 568 CA ASP B1074 10707 8609 9784 704 240 -833 C ATOM 569 C ASP B1074 18.868 45.552 -4.646 1.00 80.68 C ANISOU 569 C ASP B1074 11321 9162 10172 610 323 -815 C ATOM 570 O ASP B1074 18.739 46.169 -3.586 1.00 81.70 O ANISOU 570 O ASP B1074 11596 9256 10189 691 369 -896 O ATOM 571 CB ASP B1074 16.871 45.310 -6.177 1.00 78.89 C ANISOU 571 CB ASP B1074 10741 9050 10182 771 365 -847 C ATOM 572 CG ASP B1074 15.952 45.933 -7.215 1.00 89.36 C ANISOU 572 CG ASP B1074 11972 10342 11641 903 280 -883 C ATOM 573 OD1 ASP B1074 15.805 47.177 -7.213 1.00 90.64 O ANISOU 573 OD1 ASP B1074 12268 10379 11794 1046 186 -964 O ATOM 574 OD2 ASP B1074 15.326 45.171 -7.985 1.00 95.01 O ANISOU 574 OD2 ASP B1074 12490 11142 12467 868 293 -832 O ATOM 575 N ALA B1075 19.616 44.434 -4.768 1.00 75.89 N ANISOU 575 N ALA B1075 10650 8609 9574 445 325 -714 N ATOM 576 CA ALA B1075 20.369 43.818 -3.674 1.00 75.48 C ANISOU 576 CA ALA B1075 10688 8573 9417 334 360 -674 C ATOM 577 C ALA B1075 21.610 44.652 -3.335 1.00 79.08 C ANISOU 577 C ALA B1075 11363 8897 9788 272 218 -654 C ATOM 578 O ALA B1075 21.961 44.762 -2.159 1.00 79.33 O ANISOU 578 O ALA B1075 11550 8895 9695 241 230 -667 O ATOM 579 CB ALA B1075 20.772 42.400 -4.046 1.00 74.91 C ANISOU 579 CB ALA B1075 10483 8574 9406 206 367 -579 C ATOM 580 N LEU B1076 22.258 45.247 -4.368 1.00 74.88 N ANISOU 580 N LEU B1076 10849 8292 9310 234 76 -612 N ATOM 581 CA LEU B1076 23.444 46.103 -4.233 1.00 74.79 C ANISOU 581 CA LEU B1076 11022 8165 9229 141 -83 -569 C ATOM 582 C LEU B1076 23.142 47.372 -3.436 1.00 80.38 C ANISOU 582 C LEU B1076 11972 8741 9826 238 -134 -657 C ATOM 583 O LEU B1076 24.008 47.838 -2.697 1.00 80.66 O ANISOU 583 O LEU B1076 12204 8686 9758 153 -236 -629 O ATOM 584 CB LEU B1076 24.019 46.473 -5.610 1.00 74.04 C ANISOU 584 CB LEU B1076 10877 8051 9205 66 -203 -502 C ATOM 585 CG LEU B1076 25.434 45.979 -5.918 1.00 77.73 C ANISOU 585 CG LEU B1076 11285 8565 9683 -107 -272 -391 C ATOM 586 CD1 LEU B1076 25.665 45.909 -7.411 1.00 77.20 C ANISOU 586 CD1 LEU B1076 11092 8552 9690 -162 -302 -343 C ATOM 587 CD2 LEU B1076 26.488 46.867 -5.277 1.00 80.81 C ANISOU 587 CD2 LEU B1076 11867 8858 9979 -218 -421 -341 C ATOM 588 N LYS B1077 21.917 47.922 -3.584 1.00 77.78 N ANISOU 588 N LYS B1077 11635 8397 9521 423 -76 -766 N ATOM 589 CA LYS B1077 21.466 49.119 -2.872 1.00 79.58 C ANISOU 589 CA LYS B1077 12091 8494 9650 573 -113 -885 C ATOM 590 C LYS B1077 21.306 48.830 -1.369 1.00 84.51 C ANISOU 590 C LYS B1077 12821 9158 10132 603 22 -949 C ATOM 591 O LYS B1077 21.669 49.674 -0.547 1.00 85.72 O ANISOU 591 O LYS B1077 13250 9174 10145 623 -60 -1000 O ATOM 592 CB LYS B1077 20.163 49.657 -3.484 1.00 83.23 C ANISOU 592 CB LYS B1077 12468 8952 10205 790 -81 -991 C ATOM 593 CG LYS B1077 19.776 51.048 -2.973 1.00101.17 C ANISOU 593 CG LYS B1077 14998 11050 12391 977 -169 -1125 C ATOM 594 CD LYS B1077 18.277 51.186 -2.658 1.00113.65 C ANISOU 594 CD LYS B1077 16460 12710 14010 1254 -4 -1286 C ATOM 595 CE LYS B1077 17.814 50.402 -1.444 1.00126.87 C ANISOU 595 CE LYS B1077 18054 14560 15590 1285 252 -1345 C ATOM 596 NZ LYS B1077 17.199 49.100 -1.824 1.00134.97 N ANISOU 596 NZ LYS B1077 18736 15815 16733 1224 424 -1279 N ATOM 597 N LEU B1078 20.787 47.631 -1.021 1.00 80.35 N ANISOU 597 N LEU B1078 12097 8807 9625 586 213 -938 N ATOM 598 CA LEU B1078 20.624 47.171 0.364 1.00 81.03 C ANISOU 598 CA LEU B1078 12268 8958 9561 571 355 -976 C ATOM 599 C LEU B1078 22.008 46.929 0.980 1.00 84.09 C ANISOU 599 C LEU B1078 12831 9264 9856 370 225 -872 C ATOM 600 O LEU B1078 22.220 47.244 2.152 1.00 84.99 O ANISOU 600 O LEU B1078 13180 9316 9798 356 228 -914 O ATOM 601 CB LEU B1078 19.789 45.878 0.423 1.00 80.74 C ANISOU 601 CB LEU B1078 11971 9129 9577 550 555 -954 C ATOM 602 CG LEU B1078 18.310 45.990 0.051 1.00 86.48 C ANISOU 602 CG LEU B1078 12492 9979 10388 736 709 -1051 C ATOM 603 CD1 LEU B1078 17.825 44.722 -0.616 1.00 85.47 C ANISOU 603 CD1 LEU B1078 12072 10008 10393 648 786 -961 C ATOM 604 CD2 LEU B1078 17.455 46.302 1.268 1.00 91.41 C ANISOU 604 CD2 LEU B1078 13187 10686 10859 867 902 -1184 C ATOM 605 N ALA B1079 22.951 46.393 0.170 1.00 78.59 N ANISOU 605 N ALA B1079 12019 8570 9272 220 106 -741 N ATOM 606 CA ALA B1079 24.339 46.130 0.554 1.00 77.73 C ANISOU 606 CA ALA B1079 12009 8401 9123 35 -41 -628 C ATOM 607 C ALA B1079 25.099 47.441 0.788 1.00 82.54 C ANISOU 607 C ALA B1079 12885 8834 9643 1 -234 -627 C ATOM 608 O ALA B1079 25.903 47.517 1.717 1.00 82.82 O ANISOU 608 O ALA B1079 13108 8793 9567 -112 -333 -583 O ATOM 609 CB ALA B1079 25.033 45.305 -0.518 1.00 76.65 C ANISOU 609 CB ALA B1079 11643 8337 9144 -67 -96 -515 C ATOM 610 N ASN B1080 24.829 48.475 -0.039 1.00 79.41 N ANISOU 610 N ASN B1080 12525 8358 9290 85 -311 -670 N ATOM 611 CA ASN B1080 25.451 49.797 0.081 1.00 80.45 C ANISOU 611 CA ASN B1080 12934 8299 9334 45 -523 -666 C ATOM 612 C ASN B1080 24.907 50.570 1.285 1.00 86.65 C ANISOU 612 C ASN B1080 14023 8962 9940 176 -503 -803 C ATOM 613 O ASN B1080 25.616 51.414 1.836 1.00 87.57 O ANISOU 613 O ASN B1080 14431 8907 9933 99 -689 -786 O ATOM 614 CB ASN B1080 25.273 50.610 -1.204 1.00 80.48 C ANISOU 614 CB ASN B1080 12904 8244 9432 84 -628 -663 C ATOM 615 CG ASN B1080 26.193 50.207 -2.332 1.00 98.22 C ANISOU 615 CG ASN B1080 14955 10570 11793 -97 -709 -514 C ATOM 616 OD1 ASN B1080 27.412 50.076 -2.167 1.00 91.94 O ANISOU 616 OD1 ASN B1080 14175 9778 10979 -289 -823 -395 O ATOM 617 ND2 ASN B1080 25.635 50.052 -3.521 1.00 88.47 N ANISOU 617 ND2 ASN B1080 13534 9404 10676 -40 -658 -519 N ATOM 618 N GLU B1081 23.657 50.276 1.693 1.00 83.90 N ANISOU 618 N GLU B1081 13603 8708 9567 369 -279 -938 N ATOM 619 CA GLU B1081 22.997 50.909 2.836 1.00 86.14 C ANISOU 619 CA GLU B1081 14140 8920 9668 530 -200 -1097 C ATOM 620 C GLU B1081 23.415 50.311 4.190 1.00 91.15 C ANISOU 620 C GLU B1081 14925 9581 10128 410 -139 -1076 C ATOM 621 O GLU B1081 23.110 50.891 5.235 1.00 93.02 O ANISOU 621 O GLU B1081 15438 9736 10168 504 -101 -1198 O ATOM 622 CB GLU B1081 21.471 50.893 2.659 1.00 88.32 C ANISOU 622 CB GLU B1081 14242 9320 9997 790 27 -1251 C ATOM 623 CG GLU B1081 20.958 52.091 1.879 1.00 99.12 C ANISOU 623 CG GLU B1081 15675 10549 11436 985 -90 -1347 C ATOM 624 CD GLU B1081 19.529 52.034 1.372 1.00118.01 C ANISOU 624 CD GLU B1081 17814 13071 13952 1231 85 -1467 C ATOM 625 OE1 GLU B1081 19.163 52.915 0.561 1.00113.57 O ANISOU 625 OE1 GLU B1081 17278 12390 13485 1375 -48 -1520 O ATOM 626 OE2 GLU B1081 18.777 51.115 1.770 1.00110.23 O ANISOU 626 OE2 GLU B1081 16604 12305 12972 1268 336 -1496 O ATOM 627 N GLY B1082 24.121 49.180 4.153 1.00 86.34 N ANISOU 627 N GLY B1082 14152 9070 9583 210 -146 -926 N ATOM 628 CA GLY B1082 24.606 48.486 5.342 1.00 86.74 C ANISOU 628 CA GLY B1082 14331 9136 9489 65 -130 -874 C ATOM 629 C GLY B1082 23.831 47.232 5.691 1.00 90.54 C ANISOU 629 C GLY B1082 14613 9819 9969 67 111 -880 C ATOM 630 O GLY B1082 24.290 46.436 6.515 1.00 90.45 O ANISOU 630 O GLY B1082 14672 9829 9868 -88 103 -803 O ATOM 631 N LYS B1083 22.647 47.051 5.071 1.00 86.85 N ANISOU 631 N LYS B1083 13903 9495 9600 226 305 -960 N ATOM 632 CA LYS B1083 21.763 45.903 5.288 1.00 86.66 C ANISOU 632 CA LYS B1083 13664 9679 9585 218 534 -959 C ATOM 633 C LYS B1083 22.366 44.634 4.659 1.00 88.23 C ANISOU 633 C LYS B1083 13642 9941 9941 46 465 -795 C ATOM 634 O LYS B1083 22.244 44.416 3.450 1.00 86.31 O ANISOU 634 O LYS B1083 13161 9741 9890 81 445 -761 O ATOM 635 CB LYS B1083 20.348 46.191 4.744 1.00 89.90 C ANISOU 635 CB LYS B1083 13866 10219 10074 438 728 -1084 C ATOM 636 CG LYS B1083 19.608 47.316 5.464 1.00106.22 C ANISOU 636 CG LYS B1083 16126 12251 11981 653 834 -1275 C ATOM 637 CD LYS B1083 18.305 47.660 4.756 1.00116.15 C ANISOU 637 CD LYS B1083 17138 13626 13370 893 980 -1392 C ATOM 638 CE LYS B1083 17.590 48.824 5.393 1.00128.63 C ANISOU 638 CE LYS B1083 18899 15162 14813 1154 1071 -1602 C ATOM 639 NZ LYS B1083 16.350 49.173 4.654 1.00138.07 N ANISOU 639 NZ LYS B1083 19826 16466 16167 1406 1183 -1714 N ATOM 640 N VAL B1084 23.048 43.820 5.487 1.00 84.50 N ANISOU 640 N VAL B1084 13274 9455 9378 -134 410 -700 N ATOM 641 CA VAL B1084 23.720 42.588 5.059 1.00 82.43 C ANISOU 641 CA VAL B1084 12849 9223 9249 -282 316 -557 C ATOM 642 C VAL B1084 22.710 41.460 4.827 1.00 85.63 C ANISOU 642 C VAL B1084 13028 9798 9709 -288 492 -543 C ATOM 643 O VAL B1084 22.644 40.928 3.719 1.00 83.67 O ANISOU 643 O VAL B1084 12548 9598 9647 -271 474 -500 O ATOM 644 CB VAL B1084 24.871 42.160 6.017 1.00 86.67 C ANISOU 644 CB VAL B1084 13590 9655 9686 -463 144 -454 C ATOM 645 CG1 VAL B1084 25.677 41.002 5.431 1.00 84.77 C ANISOU 645 CG1 VAL B1084 13168 9422 9618 -567 12 -323 C ATOM 646 CG2 VAL B1084 25.789 43.335 6.352 1.00 87.19 C ANISOU 646 CG2 VAL B1084 13898 9553 9676 -479 -39 -461 C ATOM 647 N LYS B1085 21.935 41.098 5.873 1.00 83.66 N ANISOU 647 N LYS B1085 12860 9643 9285 -330 658 -574 N ATOM 648 CA LYS B1085 20.931 40.028 5.846 1.00 83.54 C ANISOU 648 CA LYS B1085 12655 9801 9283 -383 823 -543 C ATOM 649 C LYS B1085 19.784 40.281 4.867 1.00 86.57 C ANISOU 649 C LYS B1085 12769 10316 9807 -224 971 -616 C ATOM 650 O LYS B1085 19.227 39.323 4.331 1.00 85.61 O ANISOU 650 O LYS B1085 12436 10303 9789 -281 1019 -553 O ATOM 651 CB LYS B1085 20.398 39.739 7.261 1.00 88.35 C ANISOU 651 CB LYS B1085 13435 10498 9636 -487 975 -558 C ATOM 652 CG LYS B1085 21.005 38.498 7.919 1.00101.89 C ANISOU 652 CG LYS B1085 15261 12172 11279 -728 858 -411 C ATOM 653 CD LYS B1085 22.390 38.745 8.521 1.00110.74 C ANISOU 653 CD LYS B1085 16654 13089 12333 -812 620 -360 C ATOM 654 CE LYS B1085 23.065 37.458 8.923 1.00120.71 C ANISOU 654 CE LYS B1085 17986 14286 13592 -1020 449 -208 C ATOM 655 NZ LYS B1085 24.506 37.663 9.221 1.00129.26 N ANISOU 655 NZ LYS B1085 19251 15173 14691 -1077 177 -144 N ATOM 656 N GLU B1086 19.441 41.562 4.628 1.00 83.34 N ANISOU 656 N GLU B1086 12381 9880 9403 -29 1014 -745 N ATOM 657 CA GLU B1086 18.381 41.965 3.700 1.00 83.01 C ANISOU 657 CA GLU B1086 12099 9937 9503 146 1118 -822 C ATOM 658 C GLU B1086 18.828 41.781 2.248 1.00 83.94 C ANISOU 658 C GLU B1086 12057 9986 9849 149 958 -752 C ATOM 659 O GLU B1086 18.020 41.373 1.413 1.00 83.09 O ANISOU 659 O GLU B1086 11709 9983 9880 187 1017 -741 O ATOM 660 CB GLU B1086 17.937 43.415 3.958 1.00 86.06 C ANISOU 660 CB GLU B1086 12601 10281 9818 369 1179 -988 C ATOM 661 CG GLU B1086 17.187 43.612 5.269 1.00 99.60 C ANISOU 661 CG GLU B1086 14423 12115 11306 418 1401 -1095 C ATOM 662 CD GLU B1086 18.021 44.018 6.470 1.00120.31 C ANISOU 662 CD GLU B1086 17417 14605 13692 346 1341 -1117 C ATOM 663 OE1 GLU B1086 17.658 45.023 7.123 1.00116.95 O ANISOU 663 OE1 GLU B1086 17169 14153 13115 511 1429 -1273 O ATOM 664 OE2 GLU B1086 19.026 43.332 6.771 1.00111.81 O ANISOU 664 OE2 GLU B1086 16461 13442 12578 133 1196 -985 O ATOM 665 N ALA B1087 20.115 42.072 1.955 1.00 78.76 N ANISOU 665 N ALA B1087 11534 9168 9223 96 756 -701 N ATOM 666 CA ALA B1087 20.717 41.924 0.626 1.00 76.41 C ANISOU 666 CA ALA B1087 11111 8815 9107 82 612 -635 C ATOM 667 C ALA B1087 20.910 40.449 0.264 1.00 78.91 C ANISOU 667 C ALA B1087 11285 9191 9508 -49 591 -527 C ATOM 668 O ALA B1087 20.772 40.093 -0.907 1.00 77.53 O ANISOU 668 O ALA B1087 10940 9037 9479 -30 559 -500 O ATOM 669 CB ALA B1087 22.046 42.660 0.561 1.00 76.53 C ANISOU 669 CB ALA B1087 11298 8675 9106 42 423 -607 C ATOM 670 N GLN B1088 21.226 39.598 1.269 1.00 75.52 N ANISOU 670 N GLN B1088 10951 8768 8973 -183 592 -466 N ATOM 671 CA GLN B1088 21.408 38.149 1.113 1.00 74.40 C ANISOU 671 CA GLN B1088 10728 8652 8889 -310 545 -365 C ATOM 672 C GLN B1088 20.059 37.482 0.826 1.00 78.90 C ANISOU 672 C GLN B1088 11118 9364 9495 -316 687 -363 C ATOM 673 O GLN B1088 19.997 36.555 0.017 1.00 77.36 O ANISOU 673 O GLN B1088 10798 9178 9417 -359 631 -303 O ATOM 674 CB GLN B1088 22.053 37.534 2.368 1.00 76.32 C ANISOU 674 CB GLN B1088 11161 8842 8994 -456 482 -299 C ATOM 675 CG GLN B1088 23.526 37.891 2.557 1.00 84.80 C ANISOU 675 CG GLN B1088 12374 9774 10071 -485 290 -265 C ATOM 676 CD GLN B1088 24.070 37.444 3.894 1.00101.00 C ANISOU 676 CD GLN B1088 14642 11762 11972 -625 213 -204 C ATOM 677 OE1 GLN B1088 23.564 37.808 4.962 1.00 97.42 O ANISOU 677 OE1 GLN B1088 14352 11333 11330 -661 314 -241 O ATOM 678 NE2 GLN B1088 25.147 36.678 3.868 1.00 91.25 N ANISOU 678 NE2 GLN B1088 13421 10440 10811 -700 24 -116 N ATOM 679 N ALA B1089 18.983 37.968 1.483 1.00 77.70 N ANISOU 679 N ALA B1089 10952 9329 9241 -269 869 -431 N ATOM 680 CA ALA B1089 17.610 37.486 1.310 1.00 78.78 C ANISOU 680 CA ALA B1089 10886 9640 9408 -278 1023 -428 C ATOM 681 C ALA B1089 17.072 37.887 -0.068 1.00 82.29 C ANISOU 681 C ALA B1089 11125 10101 10041 -142 1005 -465 C ATOM 682 O ALA B1089 16.350 37.105 -0.688 1.00 81.86 O ANISOU 682 O ALA B1089 10891 10129 10081 -196 1020 -409 O ATOM 683 CB ALA B1089 16.714 38.041 2.408 1.00 81.84 C ANISOU 683 CB ALA B1089 11300 10167 9630 -238 1236 -509 C ATOM 684 N ALA B1090 17.443 39.098 -0.548 1.00 78.59 N ANISOU 684 N ALA B1090 10706 9537 9617 14 949 -547 N ATOM 685 CA ALA B1090 17.062 39.627 -1.862 1.00 77.85 C ANISOU 685 CA ALA B1090 10469 9425 9686 137 897 -580 C ATOM 686 C ALA B1090 17.783 38.864 -2.976 1.00 80.44 C ANISOU 686 C ALA B1090 10757 9677 10131 55 745 -494 C ATOM 687 O ALA B1090 17.246 38.738 -4.078 1.00 79.62 O ANISOU 687 O ALA B1090 10508 9593 10153 90 715 -485 O ATOM 688 CB ALA B1090 17.394 41.109 -1.947 1.00 78.72 C ANISOU 688 CB ALA B1090 10703 9427 9780 291 847 -677 C ATOM 689 N ALA B1091 18.991 38.338 -2.673 1.00 76.63 N ANISOU 689 N ALA B1091 10404 9108 9603 -47 648 -437 N ATOM 690 CA ALA B1091 19.826 37.557 -3.590 1.00 75.13 C ANISOU 690 CA ALA B1091 10189 8852 9504 -105 516 -373 C ATOM 691 C ALA B1091 19.255 36.160 -3.876 1.00 79.13 C ANISOU 691 C ALA B1091 10597 9409 10060 -198 516 -306 C ATOM 692 O ALA B1091 19.704 35.505 -4.818 1.00 77.86 O ANISOU 692 O ALA B1091 10403 9197 9982 -213 417 -275 O ATOM 693 CB ALA B1091 21.244 37.452 -3.050 1.00 75.42 C ANISOU 693 CB ALA B1091 10372 8797 9487 -164 412 -340 C ATOM 694 N GLU B1092 18.265 35.709 -3.074 1.00 77.13 N ANISOU 694 N GLU B1092 10304 9260 9743 -268 625 -283 N ATOM 695 CA GLU B1092 17.598 34.416 -3.249 1.00 77.48 C ANISOU 695 CA GLU B1092 10267 9354 9816 -392 612 -201 C ATOM 696 C GLU B1092 16.684 34.432 -4.483 1.00 81.65 C ANISOU 696 C GLU B1092 10617 9930 10476 -342 609 -206 C ATOM 697 O GLU B1092 16.410 33.376 -5.053 1.00 81.46 O ANISOU 697 O GLU B1092 10552 9892 10506 -434 531 -138 O ATOM 698 CB GLU B1092 16.811 34.031 -1.988 1.00 80.63 C ANISOU 698 CB GLU B1092 10672 9877 10087 -512 739 -163 C ATOM 699 CG GLU B1092 17.087 32.617 -1.496 1.00 91.43 C ANISOU 699 CG GLU B1092 12142 11200 11397 -705 645 -52 C ATOM 700 CD GLU B1092 18.436 32.349 -0.847 1.00110.58 C ANISOU 700 CD GLU B1092 14781 13482 13755 -741 521 -33 C ATOM 701 OE1 GLU B1092 19.071 33.306 -0.346 1.00106.21 O ANISOU 701 OE1 GLU B1092 14316 12896 13144 -661 547 -94 O ATOM 702 OE2 GLU B1092 18.840 31.165 -0.809 1.00102.87 O ANISOU 702 OE2 GLU B1092 13889 12414 12782 -854 379 48 O ATOM 703 N GLN B1093 16.234 35.636 -4.901 1.00 78.41 N ANISOU 703 N GLN B1093 10124 9553 10115 -198 665 -284 N ATOM 704 CA GLN B1093 15.393 35.844 -6.084 1.00 78.28 C ANISOU 704 CA GLN B1093 9951 9565 10228 -137 636 -292 C ATOM 705 C GLN B1093 16.201 35.663 -7.377 1.00 80.16 C ANISOU 705 C GLN B1093 10246 9674 10539 -123 486 -284 C ATOM 706 O GLN B1093 15.617 35.369 -8.422 1.00 79.56 O ANISOU 706 O GLN B1093 10081 9596 10552 -131 423 -260 O ATOM 707 CB GLN B1093 14.724 37.229 -6.051 1.00 80.62 C ANISOU 707 CB GLN B1093 10169 9913 10551 30 717 -385 C ATOM 708 CG GLN B1093 13.622 37.357 -4.998 1.00101.31 C ANISOU 708 CG GLN B1093 12668 12707 13119 43 894 -409 C ATOM 709 CD GLN B1093 12.851 38.655 -5.090 1.00124.86 C ANISOU 709 CD GLN B1093 15550 15737 16155 248 959 -517 C ATOM 710 OE1 GLN B1093 13.406 39.738 -5.322 1.00120.46 O ANISOU 710 OE1 GLN B1093 15116 15057 15597 382 896 -595 O ATOM 711 NE2 GLN B1093 11.548 38.579 -4.865 1.00119.80 N ANISOU 711 NE2 GLN B1093 14682 15277 15558 276 1080 -523 N ATOM 712 N LEU B1094 17.543 35.831 -7.300 1.00 75.46 N ANISOU 712 N LEU B1094 9794 8982 9897 -109 430 -301 N ATOM 713 CA LEU B1094 18.473 35.661 -8.424 1.00 73.88 C ANISOU 713 CA LEU B1094 9642 8690 9739 -96 318 -302 C ATOM 714 C LEU B1094 18.533 34.199 -8.857 1.00 77.27 C ANISOU 714 C LEU B1094 10079 9087 10193 -181 244 -249 C ATOM 715 O LEU B1094 18.776 33.922 -10.033 1.00 76.71 O ANISOU 715 O LEU B1094 10013 8967 10168 -163 168 -257 O ATOM 716 CB LEU B1094 19.885 36.156 -8.063 1.00 73.27 C ANISOU 716 CB LEU B1094 9680 8555 9606 -75 289 -324 C ATOM 717 CG LEU B1094 20.067 37.665 -7.870 1.00 78.05 C ANISOU 717 CG LEU B1094 10329 9145 10180 0 309 -374 C ATOM 718 CD1 LEU B1094 21.295 37.959 -7.040 1.00 77.94 C ANISOU 718 CD1 LEU B1094 10434 9089 10092 -26 281 -369 C ATOM 719 CD2 LEU B1094 20.166 38.384 -9.201 1.00 80.20 C ANISOU 719 CD2 LEU B1094 10585 9384 10504 45 246 -393 C ATOM 720 N LYS B1095 18.299 33.270 -7.907 1.00 73.89 N ANISOU 720 N LYS B1095 9676 8678 9721 -278 255 -196 N ATOM 721 CA LYS B1095 18.273 31.825 -8.143 1.00 73.78 C ANISOU 721 CA LYS B1095 9705 8609 9719 -373 157 -137 C ATOM 722 C LYS B1095 17.106 31.441 -9.058 1.00 78.11 C ANISOU 722 C LYS B1095 10159 9184 10335 -417 123 -103 C ATOM 723 O LYS B1095 17.251 30.520 -9.858 1.00 77.67 O ANISOU 723 O LYS B1095 10164 9042 10305 -447 7 -85 O ATOM 724 CB LYS B1095 18.200 31.052 -6.816 1.00 76.88 C ANISOU 724 CB LYS B1095 10167 9012 10030 -496 163 -72 C ATOM 725 CG LYS B1095 19.484 31.107 -5.996 1.00 85.95 C ANISOU 725 CG LYS B1095 11444 10094 11120 -473 131 -87 C ATOM 726 CD LYS B1095 19.330 30.380 -4.673 1.00 94.52 C ANISOU 726 CD LYS B1095 12624 11181 12108 -616 123 -13 C ATOM 727 CE LYS B1095 20.566 30.491 -3.820 1.00101.87 C ANISOU 727 CE LYS B1095 13686 12036 12983 -600 68 -21 C ATOM 728 NZ LYS B1095 20.444 29.692 -2.575 1.00110.71 N ANISOU 728 NZ LYS B1095 14934 13135 13994 -760 29 62 N ATOM 729 N THR B1096 15.966 32.166 -8.956 1.00 75.38 N ANISOU 729 N THR B1096 9668 8953 10019 -410 214 -100 N ATOM 730 CA THR B1096 14.759 31.969 -9.774 1.00 75.93 C ANISOU 730 CA THR B1096 9611 9068 10172 -453 176 -59 C ATOM 731 C THR B1096 15.044 32.344 -11.242 1.00 78.62 C ANISOU 731 C THR B1096 9980 9319 10573 -367 81 -104 C ATOM 732 O THR B1096 14.618 31.624 -12.149 1.00 78.21 O ANISOU 732 O THR B1096 9938 9218 10561 -430 -31 -63 O ATOM 733 CB THR B1096 13.568 32.747 -9.175 1.00 84.93 C ANISOU 733 CB THR B1096 10560 10371 11337 -432 308 -59 C ATOM 734 OG1 THR B1096 13.504 32.508 -7.768 1.00 85.16 O ANISOU 734 OG1 THR B1096 10597 10491 11269 -508 423 -34 O ATOM 735 CG2 THR B1096 12.233 32.376 -9.819 1.00 84.85 C ANISOU 735 CG2 THR B1096 10379 10437 11423 -509 259 10 C ATOM 736 N THR B1097 15.778 33.458 -11.459 1.00 74.35 N ANISOU 736 N THR B1097 9475 8753 10022 -244 115 -180 N ATOM 737 CA THR B1097 16.186 33.949 -12.783 1.00 73.53 C ANISOU 737 CA THR B1097 9420 8576 9941 -181 39 -220 C ATOM 738 C THR B1097 17.229 32.987 -13.379 1.00 76.57 C ANISOU 738 C THR B1097 9940 8870 10282 -203 -35 -229 C ATOM 739 O THR B1097 17.226 32.755 -14.590 1.00 76.33 O ANISOU 739 O THR B1097 9959 8783 10260 -205 -116 -239 O ATOM 740 CB THR B1097 16.703 35.401 -12.697 1.00 81.87 C ANISOU 740 CB THR B1097 10492 9634 10979 -78 87 -281 C ATOM 741 OG1 THR B1097 15.882 36.159 -11.804 1.00 83.03 O ANISOU 741 OG1 THR B1097 10541 9859 11147 -29 172 -294 O ATOM 742 CG2 THR B1097 16.745 36.093 -14.057 1.00 80.24 C ANISOU 742 CG2 THR B1097 10318 9372 10795 -43 4 -302 C ATOM 743 N ARG B1098 18.105 32.421 -12.515 1.00 72.20 N ANISOU 743 N ARG B1098 9452 8300 9680 -212 -13 -232 N ATOM 744 CA ARG B1098 19.134 31.442 -12.875 1.00 71.52 C ANISOU 744 CA ARG B1098 9478 8131 9564 -199 -82 -255 C ATOM 745 C ARG B1098 18.463 30.136 -13.328 1.00 75.81 C ANISOU 745 C ARG B1098 10078 8605 10122 -277 -192 -212 C ATOM 746 O ARG B1098 18.898 29.542 -14.316 1.00 75.66 O ANISOU 746 O ARG B1098 10154 8506 10089 -242 -269 -252 O ATOM 747 CB ARG B1098 20.077 31.190 -11.680 1.00 71.13 C ANISOU 747 CB ARG B1098 9473 8075 9479 -190 -59 -255 C ATOM 748 CG ARG B1098 21.306 30.348 -12.010 1.00 78.07 C ANISOU 748 CG ARG B1098 10440 8878 10347 -129 -131 -297 C ATOM 749 CD ARG B1098 21.199 28.933 -11.478 1.00 84.45 C ANISOU 749 CD ARG B1098 11342 9594 11150 -185 -237 -257 C ATOM 750 NE ARG B1098 21.752 28.811 -10.129 1.00 91.29 N ANISOU 750 NE ARG B1098 12240 10454 11994 -210 -240 -226 N ATOM 751 CZ ARG B1098 21.029 28.597 -9.035 1.00105.65 C ANISOU 751 CZ ARG B1098 14074 12290 13777 -332 -231 -149 C ATOM 752 NH1 ARG B1098 21.621 28.492 -7.853 1.00 93.43 N ANISOU 752 NH1 ARG B1098 12586 10724 12189 -362 -248 -121 N ATOM 753 NH2 ARG B1098 19.712 28.456 -9.117 1.00 92.54 N ANISOU 753 NH2 ARG B1098 12368 10675 12117 -438 -211 -92 N ATOM 754 N ASN B1099 17.404 29.701 -12.606 1.00 72.70 N ANISOU 754 N ASN B1099 9632 8247 9745 -391 -200 -131 N ATOM 755 CA ASN B1099 16.634 28.494 -12.917 1.00 73.32 C ANISOU 755 CA ASN B1099 9762 8261 9833 -511 -326 -62 C ATOM 756 C ASN B1099 15.784 28.674 -14.181 1.00 77.20 C ANISOU 756 C ASN B1099 10217 8744 10373 -530 -393 -52 C ATOM 757 O ASN B1099 15.482 27.689 -14.852 1.00 77.27 O ANISOU 757 O ASN B1099 10329 8653 10376 -600 -534 -22 O ATOM 758 CB ASN B1099 15.770 28.064 -11.726 1.00 74.22 C ANISOU 758 CB ASN B1099 9812 8451 9937 -662 -303 40 C ATOM 759 CG ASN B1099 16.546 27.601 -10.511 1.00 94.48 C ANISOU 759 CG ASN B1099 12473 10989 12437 -687 -291 51 C ATOM 760 OD1 ASN B1099 17.701 27.163 -10.589 1.00 87.75 O ANISOU 760 OD1 ASN B1099 11754 10023 11563 -606 -358 -1 O ATOM 761 ND2 ASN B1099 15.922 27.696 -9.347 1.00 86.74 N ANISOU 761 ND2 ASN B1099 11420 10119 11420 -798 -204 119 N ATOM 762 N ALA B1100 15.418 29.930 -14.512 1.00 73.37 N ANISOU 762 N ALA B1100 9608 8341 9929 -466 -316 -77 N ATOM 763 CA ALA B1100 14.650 30.264 -15.713 1.00 73.57 C ANISOU 763 CA ALA B1100 9601 8350 10004 -477 -396 -66 C ATOM 764 C ALA B1100 15.516 30.103 -16.973 1.00 77.11 C ANISOU 764 C ALA B1100 10219 8685 10393 -415 -466 -138 C ATOM 765 O ALA B1100 15.000 29.702 -18.016 1.00 77.19 O ANISOU 765 O ALA B1100 10300 8623 10406 -468 -590 -119 O ATOM 766 CB ALA B1100 14.119 31.685 -15.617 1.00 74.15 C ANISOU 766 CB ALA B1100 9516 8521 10137 -406 -314 -81 C ATOM 767 N TYR B1101 16.832 30.399 -16.861 1.00 72.89 N ANISOU 767 N TYR B1101 9749 8146 9798 -313 -385 -219 N ATOM 768 CA TYR B1101 17.813 30.294 -17.945 1.00 72.46 C ANISOU 768 CA TYR B1101 9829 8032 9670 -243 -403 -300 C ATOM 769 C TYR B1101 18.124 28.833 -18.310 1.00 77.35 C ANISOU 769 C TYR B1101 10610 8535 10244 -247 -505 -325 C ATOM 770 O TYR B1101 18.228 28.522 -19.499 1.00 77.45 O ANISOU 770 O TYR B1101 10750 8478 10198 -232 -570 -371 O ATOM 771 CB TYR B1101 19.099 31.082 -17.603 1.00 72.74 C ANISOU 771 CB TYR B1101 9839 8131 9666 -148 -281 -363 C ATOM 772 CG TYR B1101 20.230 30.897 -18.595 1.00 74.66 C ANISOU 772 CG TYR B1101 10184 8358 9825 -78 -265 -449 C ATOM 773 CD1 TYR B1101 20.294 31.655 -19.761 1.00 76.62 C ANISOU 773 CD1 TYR B1101 10470 8626 10016 -87 -257 -473 C ATOM 774 CD2 TYR B1101 21.240 29.966 -18.366 1.00 75.81 C ANISOU 774 CD2 TYR B1101 10386 8476 9942 -1 -258 -508 C ATOM 775 CE1 TYR B1101 21.323 31.477 -20.684 1.00 77.76 C ANISOU 775 CE1 TYR B1101 10699 8788 10059 -34 -215 -554 C ATOM 776 CE2 TYR B1101 22.267 29.770 -19.288 1.00 77.20 C ANISOU 776 CE2 TYR B1101 10628 8667 10039 85 -220 -602 C ATOM 777 CZ TYR B1101 22.306 30.529 -20.445 1.00 84.08 C ANISOU 777 CZ TYR B1101 11527 9584 10835 62 -183 -625 C ATOM 778 OH TYR B1101 23.328 30.348 -21.343 1.00 85.23 O ANISOU 778 OH TYR B1101 11727 9777 10881 136 -116 -720 O ATOM 779 N ILE B1102 18.299 27.952 -17.297 1.00 74.37 N ANISOU 779 N ILE B1102 10254 8124 9879 -265 -529 -300 N ATOM 780 CA ILE B1102 18.612 26.528 -17.505 1.00 75.36 C ANISOU 780 CA ILE B1102 10558 8108 9966 -256 -657 -326 C ATOM 781 C ILE B1102 17.429 25.779 -18.156 1.00 80.24 C ANISOU 781 C ILE B1102 11271 8629 10588 -388 -823 -257 C ATOM 782 O ILE B1102 17.644 24.827 -18.909 1.00 80.60 O ANISOU 782 O ILE B1102 11515 8533 10577 -363 -947 -305 O ATOM 783 CB ILE B1102 19.156 25.807 -16.226 1.00 78.82 C ANISOU 783 CB ILE B1102 11021 8512 10415 -248 -675 -308 C ATOM 784 CG1 ILE B1102 18.109 25.692 -15.100 1.00 79.82 C ANISOU 784 CG1 ILE B1102 11065 8683 10580 -417 -692 -177 C ATOM 785 CG2 ILE B1102 20.445 26.449 -15.709 1.00 78.56 C ANISOU 785 CG2 ILE B1102 10914 8556 10378 -116 -548 -379 C ATOM 786 CD1 ILE B1102 17.584 24.284 -14.878 1.00 89.75 C ANISOU 786 CD1 ILE B1102 12473 9807 11823 -546 -876 -101 C ATOM 787 N GLN B1103 16.192 26.233 -17.875 1.00 76.99 N ANISOU 787 N GLN B1103 10714 8295 10243 -522 -828 -147 N ATOM 788 CA GLN B1103 14.946 25.666 -18.394 1.00 78.05 C ANISOU 788 CA GLN B1103 10880 8372 10404 -679 -990 -50 C ATOM 789 C GLN B1103 14.639 26.136 -19.815 1.00 81.75 C ANISOU 789 C GLN B1103 11400 8804 10856 -664 -1049 -81 C ATOM 790 O GLN B1103 14.018 25.392 -20.575 1.00 82.60 O ANISOU 790 O GLN B1103 11643 8796 10945 -763 -1227 -40 O ATOM 791 CB GLN B1103 13.771 26.035 -17.472 1.00 79.87 C ANISOU 791 CB GLN B1103 10880 8743 10723 -816 -950 77 C ATOM 792 CG GLN B1103 13.681 25.199 -16.196 1.00 98.87 C ANISOU 792 CG GLN B1103 13289 11160 13119 -927 -960 155 C ATOM 793 CD GLN B1103 12.885 25.873 -15.097 1.00120.12 C ANISOU 793 CD GLN B1103 15726 14048 15865 -1003 -821 235 C ATOM 794 OE1 GLN B1103 11.961 26.664 -15.334 1.00115.47 O ANISOU 794 OE1 GLN B1103 14942 13579 15353 -1020 -776 270 O ATOM 795 NE2 GLN B1103 13.226 25.562 -13.855 1.00113.63 N ANISOU 795 NE2 GLN B1103 14909 13264 15002 -1043 -754 261 N ATOM 796 N LYS B1104 15.047 27.373 -20.163 1.00 77.02 N ANISOU 796 N LYS B1104 10715 8293 10256 -561 -921 -143 N ATOM 797 CA LYS B1104 14.776 27.979 -21.466 1.00 76.98 C ANISOU 797 CA LYS B1104 10765 8260 10224 -562 -977 -163 C ATOM 798 C LYS B1104 15.893 27.847 -22.496 1.00 80.77 C ANISOU 798 C LYS B1104 11451 8671 10567 -461 -954 -287 C ATOM 799 O LYS B1104 15.639 27.349 -23.593 1.00 81.47 O ANISOU 799 O LYS B1104 11723 8648 10583 -503 -1084 -302 O ATOM 800 CB LYS B1104 14.390 29.458 -21.307 1.00 78.82 C ANISOU 800 CB LYS B1104 10800 8615 10531 -536 -887 -139 C ATOM 801 CG LYS B1104 12.888 29.698 -21.280 1.00 94.93 C ANISOU 801 CG LYS B1104 12682 10692 12695 -643 -991 -25 C ATOM 802 CD LYS B1104 12.532 31.141 -20.912 1.00104.19 C ANISOU 802 CD LYS B1104 13652 11979 13955 -573 -900 -21 C ATOM 803 CE LYS B1104 12.520 32.086 -22.093 1.00114.86 C ANISOU 803 CE LYS B1104 15076 13281 15286 -545 -973 -46 C ATOM 804 NZ LYS B1104 11.331 31.889 -22.965 1.00125.19 N ANISOU 804 NZ LYS B1104 16381 14526 16660 -649 -1177 38 N ATOM 805 N TYR B1105 17.111 28.316 -22.165 1.00 76.44 N ANISOU 805 N TYR B1105 10868 8201 9976 -335 -789 -375 N ATOM 806 CA TYR B1105 18.235 28.356 -23.104 1.00 76.59 C ANISOU 806 CA TYR B1105 11024 8214 9862 -236 -721 -494 C ATOM 807 C TYR B1105 19.160 27.134 -23.030 1.00 81.87 C ANISOU 807 C TYR B1105 11829 8809 10467 -126 -722 -593 C ATOM 808 O TYR B1105 19.739 26.768 -24.055 1.00 82.30 O ANISOU 808 O TYR B1105 12050 8822 10398 -57 -718 -697 O ATOM 809 CB TYR B1105 19.002 29.683 -22.968 1.00 76.48 C ANISOU 809 CB TYR B1105 10882 8342 9836 -184 -558 -521 C ATOM 810 CG TYR B1105 18.090 30.869 -23.210 1.00 77.40 C ANISOU 810 CG TYR B1105 10913 8489 10005 -270 -596 -440 C ATOM 811 CD1 TYR B1105 17.739 31.252 -24.503 1.00 79.97 C ANISOU 811 CD1 TYR B1105 11361 8769 10256 -332 -678 -437 C ATOM 812 CD2 TYR B1105 17.488 31.540 -22.148 1.00 77.27 C ANISOU 812 CD2 TYR B1105 10711 8533 10113 -285 -571 -369 C ATOM 813 CE1 TYR B1105 16.844 32.295 -24.732 1.00 80.70 C ANISOU 813 CE1 TYR B1105 11385 8863 10414 -399 -755 -360 C ATOM 814 CE2 TYR B1105 16.590 32.584 -22.365 1.00 78.17 C ANISOU 814 CE2 TYR B1105 10747 8662 10294 -329 -626 -308 C ATOM 815 CZ TYR B1105 16.274 32.961 -23.660 1.00 86.32 C ANISOU 815 CZ TYR B1105 11894 9634 11268 -384 -730 -301 C ATOM 816 OH TYR B1105 15.394 33.993 -23.881 1.00 87.73 O ANISOU 816 OH TYR B1105 12001 9807 11524 -414 -816 -242 O ATOM 817 N LEU B1106 19.268 26.482 -21.858 1.00 78.89 N ANISOU 817 N LEU B1106 11400 8409 10163 -108 -738 -567 N ATOM 818 CA LEU B1106 20.050 25.250 -21.724 1.00 79.96 C ANISOU 818 CA LEU B1106 11682 8441 10259 5 -788 -655 C ATOM 819 C LEU B1106 19.149 24.043 -21.996 1.00 85.76 C ANISOU 819 C LEU B1106 12616 8987 10982 -90 -1009 -609 C ATOM 820 O LEU B1106 19.626 23.012 -22.473 1.00 86.46 O ANISOU 820 O LEU B1106 12919 8936 10995 6 -1099 -707 O ATOM 821 CB LEU B1106 20.716 25.138 -20.347 1.00 79.40 C ANISOU 821 CB LEU B1106 11491 8416 10263 65 -729 -644 C ATOM 822 CG LEU B1106 22.156 25.638 -20.264 1.00 83.86 C ANISOU 822 CG LEU B1106 11960 9098 10805 226 -566 -747 C ATOM 823 CD1 LEU B1106 22.498 26.066 -18.860 1.00 82.98 C ANISOU 823 CD1 LEU B1106 11683 9065 10779 218 -505 -687 C ATOM 824 CD2 LEU B1106 23.143 24.579 -20.744 1.00 88.15 C ANISOU 824 CD2 LEU B1106 12648 9557 11289 408 -599 -890 C ATOM 825 N GLY B1107 17.856 24.208 -21.710 1.00 82.97 N ANISOU 825 N GLY B1107 12187 8635 10702 -275 -1099 -464 N ATOM 826 CA GLY B1107 16.822 23.204 -21.926 1.00 84.57 C ANISOU 826 CA GLY B1107 12543 8684 10907 -426 -1325 -378 C ATOM 827 C GLY B1107 16.052 23.407 -23.218 1.00 90.15 C ANISOU 827 C GLY B1107 13350 9337 11567 -513 -1430 -357 C ATOM 828 O GLY B1107 16.558 24.027 -24.159 1.00 89.60 O ANISOU 828 O GLY B1107 13326 9302 11415 -424 -1344 -452 O ATOM 829 N SER B1108 14.811 22.891 -23.263 1.00 88.30 N ANISOU 829 N SER B1108 13148 9023 11379 -710 -1628 -222 N ATOM 830 CA SER B1108 13.927 22.942 -24.433 1.00 89.39 C ANISOU 830 CA SER B1108 13394 9083 11486 -829 -1789 -173 C ATOM 831 C SER B1108 12.877 24.074 -24.418 1.00 93.28 C ANISOU 831 C SER B1108 13619 9722 12100 -942 -1768 -51 C ATOM 832 O SER B1108 12.056 24.150 -25.337 1.00 93.96 O ANISOU 832 O SER B1108 13772 9744 12184 -1055 -1930 10 O ATOM 833 CB SER B1108 13.241 21.591 -24.622 1.00 94.84 C ANISOU 833 CB SER B1108 14314 9571 12148 -982 -2065 -97 C ATOM 834 OG SER B1108 12.444 21.251 -23.500 1.00103.79 O ANISOU 834 OG SER B1108 15280 10758 13398 -1153 -2126 63 O ATOM 835 N GLY B1109 12.925 24.932 -23.397 1.00 88.75 N ANISOU 835 N GLY B1109 12764 9330 11629 -901 -1586 -23 N ATOM 836 CA GLY B1109 11.991 26.037 -23.193 1.00 88.45 C ANISOU 836 CA GLY B1109 12451 9438 11719 -959 -1547 70 C ATOM 837 C GLY B1109 11.821 27.003 -24.349 1.00 92.89 C ANISOU 837 C GLY B1109 13039 9994 12263 -935 -1579 45 C ATOM 838 O GLY B1109 10.693 27.258 -24.778 1.00 93.50 O ANISOU 838 O GLY B1109 13032 10068 12425 -1049 -1725 148 O ATOM 839 N SER B1110 12.940 27.549 -24.856 1.00 89.08 N ANISOU 839 N SER B1110 12666 9514 11668 -798 -1452 -82 N ATOM 840 CA SER B1110 12.952 28.515 -25.960 1.00 89.19 C ANISOU 840 CA SER B1110 12741 9519 11627 -787 -1473 -108 C ATOM 841 C SER B1110 12.611 27.904 -27.323 1.00 94.95 C ANISOU 841 C SER B1110 13747 10084 12245 -880 -1678 -107 C ATOM 842 O SER B1110 12.052 28.599 -28.174 1.00 94.97 O ANISOU 842 O SER B1110 13776 10059 12248 -945 -1788 -63 O ATOM 843 CB SER B1110 14.293 29.236 -26.027 1.00 91.78 C ANISOU 843 CB SER B1110 13098 9923 11852 -648 -1268 -229 C ATOM 844 OG SER B1110 14.551 29.930 -24.818 1.00100.46 O ANISOU 844 OG SER B1110 13963 11158 13050 -577 -1108 -221 O ATOM 845 N CYS B 35 12.956 26.620 -27.532 1.00 91.09 N ANISOU 845 N CYS B 35 12399 8607 13605 41 181 558 N ATOM 846 CA CYS B 35 12.713 25.915 -28.790 1.00 90.49 C ANISOU 846 CA CYS B 35 12287 8648 13448 21 104 705 C ATOM 847 C CYS B 35 11.258 25.502 -28.964 1.00 96.39 C ANISOU 847 C CYS B 35 12934 9441 14247 223 12 805 C ATOM 848 O CYS B 35 10.598 25.980 -29.889 1.00 97.08 O ANISOU 848 O CYS B 35 13099 9429 14357 287 -74 967 O ATOM 849 CB CYS B 35 13.657 24.727 -28.946 1.00 88.48 C ANISOU 849 CB CYS B 35 11925 8613 13079 -129 126 637 C ATOM 850 SG CYS B 35 15.383 25.181 -29.253 1.00 92.47 S ANISOU 850 SG CYS B 35 12525 9075 13534 -391 221 574 S ATOM 851 N SER B 36 10.769 24.605 -28.083 1.00 93.58 N ANISOU 851 N SER B 36 12406 9236 13913 314 22 713 N ATOM 852 CA SER B 36 9.408 24.065 -28.101 1.00 94.16 C ANISOU 852 CA SER B 36 12341 9383 14051 491 -50 786 C ATOM 853 C SER B 36 8.348 25.147 -27.930 1.00101.69 C ANISOU 853 C SER B 36 13328 10138 15170 680 -61 849 C ATOM 854 O SER B 36 8.514 26.051 -27.106 1.00102.04 O ANISOU 854 O SER B 36 13455 10025 15290 716 33 753 O ATOM 855 CB SER B 36 9.245 22.989 -27.033 1.00 96.12 C ANISOU 855 CB SER B 36 12423 9811 14288 523 -2 657 C ATOM 856 N GLN B 37 7.271 25.061 -28.733 1.00100.59 N ANISOU 856 N GLN B 37 13128 9998 15092 799 -186 1009 N ATOM 857 CA GLN B 37 6.159 26.009 -28.695 1.00103.26 C ANISOU 857 CA GLN B 37 13464 10152 15620 1003 -221 1092 C ATOM 858 C GLN B 37 5.335 25.802 -27.422 1.00108.42 C ANISOU 858 C GLN B 37 13946 10841 16408 1166 -119 970 C ATOM 859 O GLN B 37 4.686 24.764 -27.255 1.00107.16 O ANISOU 859 O GLN B 37 13595 10866 16255 1212 -144 970 O ATOM 860 CB GLN B 37 5.299 25.920 -29.971 1.00105.75 C ANISOU 860 CB GLN B 37 13753 10466 15961 1069 -415 1308 C ATOM 861 CG GLN B 37 5.868 26.725 -31.138 1.00121.89 C ANISOU 861 CG GLN B 37 16035 12356 17921 964 -499 1450 C ATOM 862 CD GLN B 37 6.262 25.863 -32.313 1.00140.11 C ANISOU 862 CD GLN B 37 18385 14821 20030 800 -606 1548 C ATOM 863 OE1 GLN B 37 7.226 25.089 -32.261 1.00133.44 O ANISOU 863 OE1 GLN B 37 17542 14129 19032 630 -525 1448 O ATOM 864 NE2 GLN B 37 5.550 26.012 -33.420 1.00133.88 N ANISOU 864 NE2 GLN B 37 17645 13985 19239 847 -792 1747 N ATOM 865 N LYS B 38 5.425 26.782 -26.503 1.00106.74 N ANISOU 865 N LYS B 38 13821 10447 16287 1235 12 857 N ATOM 866 CA LYS B 38 4.755 26.799 -25.201 1.00107.18 C ANISOU 866 CA LYS B 38 13771 10496 16455 1378 154 717 C ATOM 867 C LYS B 38 3.207 26.759 -25.264 1.00112.81 C ANISOU 867 C LYS B 38 14284 11204 17375 1611 120 806 C ATOM 868 O LYS B 38 2.643 26.005 -24.465 1.00111.84 O ANISOU 868 O LYS B 38 13990 11223 17280 1668 207 722 O ATOM 869 CB LYS B 38 5.232 27.988 -24.352 1.00111.08 C ANISOU 869 CB LYS B 38 14450 10764 16993 1389 293 581 C ATOM 870 N PRO B 39 2.488 27.518 -26.150 1.00111.42 N ANISOU 870 N PRO B 39 14114 10868 17352 1746 -5 976 N ATOM 871 CA PRO B 39 1.012 27.445 -26.142 1.00112.79 C ANISOU 871 CA PRO B 39 14056 11045 17755 1974 -43 1053 C ATOM 872 C PRO B 39 0.452 26.053 -26.430 1.00114.89 C ANISOU 872 C PRO B 39 14089 11583 17982 1942 -135 1111 C ATOM 873 O PRO B 39 0.769 25.446 -27.457 1.00113.41 O ANISOU 873 O PRO B 39 13926 11508 17657 1813 -304 1229 O ATOM 874 CB PRO B 39 0.592 28.472 -27.202 1.00116.98 C ANISOU 874 CB PRO B 39 14670 11355 18420 2084 -210 1246 C ATOM 875 CG PRO B 39 1.762 29.376 -27.348 1.00121.52 C ANISOU 875 CG PRO B 39 15546 11749 18877 1953 -174 1216 C ATOM 876 CD PRO B 39 2.950 28.491 -27.163 1.00114.20 C ANISOU 876 CD PRO B 39 14679 11023 17691 1702 -119 1109 C ATOM 877 N SER B 40 -0.354 25.538 -25.485 1.00111.24 N ANISOU 877 N SER B 40 13415 11221 17629 2048 -6 1015 N ATOM 878 CA SER B 40 -0.972 24.218 -25.562 1.00109.74 C ANISOU 878 CA SER B 40 12992 11278 17426 2021 -63 1050 C ATOM 879 C SER B 40 -2.478 24.319 -25.798 1.00115.08 C ANISOU 879 C SER B 40 13407 11935 18382 2232 -135 1163 C ATOM 880 O SER B 40 -3.191 24.938 -25.002 1.00116.73 O ANISOU 880 O SER B 40 13518 12031 18801 2416 23 1090 O ATOM 881 CB SER B 40 -0.673 23.409 -24.301 1.00111.77 C ANISOU 881 CB SER B 40 13208 11684 17573 1942 138 861 C ATOM 882 OG SER B 40 -1.133 24.068 -23.132 1.00122.07 O ANISOU 882 OG SER B 40 14490 12873 19016 2086 359 725 O ATOM 883 N ASP B 41 -2.955 23.721 -26.905 1.00110.75 N ANISOU 883 N ASP B 41 12746 11493 17842 2204 -374 1338 N ATOM 884 CA ASP B 41 -4.370 23.703 -27.274 1.00112.48 C ANISOU 884 CA ASP B 41 12691 11718 18329 2382 -497 1468 C ATOM 885 C ASP B 41 -5.034 22.473 -26.639 1.00114.11 C ANISOU 885 C ASP B 41 12631 12155 18570 2357 -412 1401 C ATOM 886 O ASP B 41 -5.363 21.501 -27.330 1.00113.12 O ANISOU 886 O ASP B 41 12385 12198 18397 2266 -591 1502 O ATOM 887 CB ASP B 41 -4.535 23.731 -28.805 1.00115.18 C ANISOU 887 CB ASP B 41 13072 12044 18646 2348 -823 1696 C ATOM 888 N LYS B 42 -5.195 22.514 -25.302 1.00109.42 N ANISOU 888 N LYS B 42 11971 11562 18041 2422 -130 1225 N ATOM 889 CA LYS B 42 -5.775 21.423 -24.522 1.00107.89 C ANISOU 889 CA LYS B 42 11555 11567 17870 2390 2 1144 C ATOM 890 C LYS B 42 -7.305 21.448 -24.513 1.00112.95 C ANISOU 890 C LYS B 42 11847 12220 18849 2580 -9 1219 C ATOM 891 O LYS B 42 -7.927 22.276 -23.840 1.00114.83 O ANISOU 891 O LYS B 42 11989 12321 19320 2777 170 1155 O ATOM 892 CB LYS B 42 -5.187 21.379 -23.097 1.00109.02 C ANISOU 892 CB LYS B 42 11819 11716 17885 2342 307 923 C ATOM 893 CG LYS B 42 -4.616 20.013 -22.696 1.00117.18 C ANISOU 893 CG LYS B 42 12881 12972 18670 2129 343 851 C ATOM 894 CD LYS B 42 -3.250 19.696 -23.332 1.00122.49 C ANISOU 894 CD LYS B 42 13802 13679 19058 1931 201 866 C ATOM 895 CE LYS B 42 -2.079 20.286 -22.581 1.00130.12 C ANISOU 895 CE LYS B 42 15034 14543 19861 1868 348 715 C ATOM 896 NZ LYS B 42 -0.791 20.016 -23.273 1.00136.43 N ANISOU 896 NZ LYS B 42 16035 15376 20427 1684 212 739 N ATOM 897 N HIS B 43 -7.896 20.538 -25.298 1.00108.13 N ANISOU 897 N HIS B 43 11044 11769 18272 2517 -224 1355 N ATOM 898 CA HIS B 43 -9.334 20.336 -25.442 1.00109.90 C ANISOU 898 CA HIS B 43 10899 12047 18812 2654 -289 1449 C ATOM 899 C HIS B 43 -9.541 18.839 -25.670 1.00110.76 C ANISOU 899 C HIS B 43 10872 12405 18808 2466 -387 1483 C ATOM 900 O HIS B 43 -9.750 18.400 -26.808 1.00110.61 O ANISOU 900 O HIS B 43 10808 12452 18768 2394 -687 1641 O ATOM 901 CB HIS B 43 -9.898 21.180 -26.600 1.00113.13 C ANISOU 901 CB HIS B 43 11246 12311 19429 2803 -575 1648 C ATOM 902 N LEU B 44 -9.426 18.053 -24.572 1.00104.37 N ANISOU 902 N LEU B 44 10031 11722 17901 2374 -135 1331 N ATOM 903 CA LEU B 44 -9.504 16.587 -24.544 1.00101.76 C ANISOU 903 CA LEU B 44 9611 11613 17439 2181 -170 1330 C ATOM 904 C LEU B 44 -8.456 16.001 -25.509 1.00101.13 C ANISOU 904 C LEU B 44 9782 11591 17052 1982 -402 1390 C ATOM 905 O LEU B 44 -8.792 15.257 -26.437 1.00100.94 O ANISOU 905 O LEU B 44 9670 11671 17012 1888 -646 1512 O ATOM 906 CB LEU B 44 -10.931 16.071 -24.824 1.00104.13 C ANISOU 906 CB LEU B 44 9521 12018 18026 2234 -269 1436 C ATOM 907 N ASP B 45 -7.180 16.399 -25.295 1.00 93.83 N ANISOU 907 N ASP B 45 9172 10588 15892 1921 -321 1299 N ATOM 908 CA ASP B 45 -5.998 16.021 -26.081 1.00 90.36 C ANISOU 908 CA ASP B 45 8996 10176 15161 1745 -476 1324 C ATOM 909 C ASP B 45 -5.818 14.503 -26.203 1.00 90.18 C ANISOU 909 C ASP B 45 8951 10348 14965 1550 -536 1315 C ATOM 910 O ASP B 45 -6.278 13.758 -25.338 1.00 89.63 O ANISOU 910 O ASP B 45 8736 10384 14936 1523 -389 1244 O ATOM 911 CB ASP B 45 -4.733 16.680 -25.492 1.00 90.66 C ANISOU 911 CB ASP B 45 9317 10105 15022 1718 -313 1193 C ATOM 912 CG ASP B 45 -3.524 16.661 -26.409 1.00 97.95 C ANISOU 912 CG ASP B 45 10502 11010 15704 1576 -461 1230 C ATOM 913 OD1 ASP B 45 -3.561 17.346 -27.454 1.00 99.91 O ANISOU 913 OD1 ASP B 45 10818 11158 15987 1615 -640 1358 O ATOM 914 OD2 ASP B 45 -2.537 15.973 -26.074 1.00100.00 O ANISOU 914 OD2 ASP B 45 10901 11351 15745 1426 -393 1133 O ATOM 915 N ALA B 46 -5.164 14.056 -27.292 1.00 83.79 N ANISOU 915 N ALA B 46 8298 9576 13964 1412 -744 1388 N ATOM 916 CA ALA B 46 -4.909 12.645 -27.586 1.00 81.25 C ANISOU 916 CA ALA B 46 7992 9413 13468 1226 -826 1383 C ATOM 917 C ALA B 46 -4.104 11.917 -26.505 1.00 81.47 C ANISOU 917 C ALA B 46 8116 9509 13328 1127 -617 1225 C ATOM 918 O ALA B 46 -4.364 10.739 -26.272 1.00 80.59 O ANISOU 918 O ALA B 46 7919 9526 13176 1025 -614 1208 O ATOM 919 CB ALA B 46 -4.228 12.503 -28.937 1.00 81.24 C ANISOU 919 CB ALA B 46 8185 9404 13278 1112 -1050 1469 C ATOM 920 N ILE B 47 -3.152 12.613 -25.838 1.00 75.73 N ANISOU 920 N ILE B 47 7570 8692 12512 1151 -457 1116 N ATOM 921 CA ILE B 47 -2.301 12.040 -24.785 1.00 73.05 C ANISOU 921 CA ILE B 47 7344 8401 12009 1062 -284 971 C ATOM 922 C ILE B 47 -3.146 11.553 -23.571 1.00 76.30 C ANISOU 922 C ILE B 47 7586 8884 12522 1095 -101 907 C ATOM 923 O ILE B 47 -3.118 10.344 -23.343 1.00 74.70 O ANISOU 923 O ILE B 47 7359 8800 12224 976 -103 889 O ATOM 924 CB ILE B 47 -1.108 12.972 -24.394 1.00 75.25 C ANISOU 924 CB ILE B 47 7849 8561 12181 1073 -183 876 C ATOM 925 CG1 ILE B 47 -0.081 13.114 -25.550 1.00 74.60 C ANISOU 925 CG1 ILE B 47 7948 8444 11951 982 -337 925 C ATOM 926 CG2 ILE B 47 -0.429 12.566 -23.070 1.00 74.71 C ANISOU 926 CG2 ILE B 47 7872 8527 11988 1013 1 724 C ATOM 927 CD1 ILE B 47 0.551 11.786 -26.120 1.00 79.99 C ANISOU 927 CD1 ILE B 47 8688 9254 12452 814 -440 928 C ATOM 928 N PRO B 48 -3.935 12.384 -22.824 1.00 73.79 N ANISOU 928 N PRO B 48 7148 8495 12393 1246 62 875 N ATOM 929 CA PRO B 48 -4.719 11.827 -21.703 1.00 74.00 C ANISOU 929 CA PRO B 48 7024 8600 12495 1253 258 811 C ATOM 930 C PRO B 48 -5.720 10.739 -22.101 1.00 77.26 C ANISOU 930 C PRO B 48 7202 9149 13006 1189 161 905 C ATOM 931 O PRO B 48 -5.940 9.824 -21.314 1.00 76.76 O ANISOU 931 O PRO B 48 7093 9181 12893 1102 284 855 O ATOM 932 CB PRO B 48 -5.418 13.052 -21.105 1.00 78.10 C ANISOU 932 CB PRO B 48 7449 8998 13226 1444 434 772 C ATOM 933 CG PRO B 48 -4.608 14.211 -21.549 1.00 82.29 C ANISOU 933 CG PRO B 48 8175 9375 13717 1508 372 766 C ATOM 934 CD PRO B 48 -4.127 13.847 -22.915 1.00 76.71 C ANISOU 934 CD PRO B 48 7531 8702 12915 1414 96 886 C ATOM 935 N ILE B 49 -6.292 10.817 -23.324 1.00 73.78 N ANISOU 935 N ILE B 49 6631 8713 12690 1216 -72 1044 N ATOM 936 CA ILE B 49 -7.245 9.828 -23.852 1.00 74.02 C ANISOU 936 CA ILE B 49 6438 8865 12820 1142 -211 1143 C ATOM 937 C ILE B 49 -6.544 8.474 -24.065 1.00 74.88 C ANISOU 937 C ILE B 49 6686 9078 12686 937 -297 1127 C ATOM 938 O ILE B 49 -7.022 7.460 -23.558 1.00 74.48 O ANISOU 938 O ILE B 49 6528 9128 12643 843 -231 1112 O ATOM 939 CB ILE B 49 -7.984 10.349 -25.131 1.00 78.77 C ANISOU 939 CB ILE B 49 6894 9431 13605 1223 -471 1300 C ATOM 940 CG1 ILE B 49 -8.823 11.635 -24.856 1.00 81.62 C ANISOU 940 CG1 ILE B 49 7075 9678 14257 1449 -382 1322 C ATOM 941 CG2 ILE B 49 -8.827 9.260 -25.818 1.00 80.28 C ANISOU 941 CG2 ILE B 49 6890 9750 13864 1110 -668 1404 C ATOM 942 CD1 ILE B 49 -10.018 11.535 -23.850 1.00 90.75 C ANISOU 942 CD1 ILE B 49 7928 10884 15671 1534 -159 1280 C ATOM 943 N LEU B 50 -5.397 8.475 -24.779 1.00 69.06 N ANISOU 943 N LEU B 50 6192 8307 11743 868 -426 1125 N ATOM 944 CA LEU B 50 -4.590 7.286 -25.074 1.00 66.65 C ANISOU 944 CA LEU B 50 6039 8074 11211 694 -507 1101 C ATOM 945 C LEU B 50 -3.947 6.678 -23.821 1.00 68.55 C ANISOU 945 C LEU B 50 6387 8345 11315 630 -308 975 C ATOM 946 O LEU B 50 -3.712 5.469 -23.786 1.00 67.00 O ANISOU 946 O LEU B 50 6233 8222 11001 496 -344 962 O ATOM 947 CB LEU B 50 -3.522 7.610 -26.135 1.00 65.56 C ANISOU 947 CB LEU B 50 6121 7877 10910 657 -659 1121 C ATOM 948 CG LEU B 50 -3.821 7.197 -27.587 1.00 70.90 C ANISOU 948 CG LEU B 50 6789 8585 11562 583 -921 1239 C ATOM 949 CD1 LEU B 50 -4.950 8.021 -28.198 1.00 73.44 C ANISOU 949 CD1 LEU B 50 6933 8870 12102 697 -1053 1366 C ATOM 950 CD2 LEU B 50 -2.589 7.351 -28.452 1.00 72.10 C ANISOU 950 CD2 LEU B 50 7197 8689 11507 518 -1005 1228 C ATOM 951 N TYR B 51 -3.671 7.513 -22.799 1.00 65.04 N ANISOU 951 N TYR B 51 5999 7832 10880 722 -108 885 N ATOM 952 CA TYR B 51 -3.089 7.088 -21.523 1.00 63.79 C ANISOU 952 CA TYR B 51 5962 7690 10586 669 75 769 C ATOM 953 C TYR B 51 -4.105 6.286 -20.706 1.00 68.55 C ANISOU 953 C TYR B 51 6402 8377 11265 628 204 770 C ATOM 954 O TYR B 51 -3.730 5.287 -20.093 1.00 67.23 O ANISOU 954 O TYR B 51 6326 8263 10954 512 251 727 O ATOM 955 CB TYR B 51 -2.554 8.300 -20.732 1.00 65.16 C ANISOU 955 CB TYR B 51 6259 7756 10744 772 235 673 C ATOM 956 CG TYR B 51 -1.091 8.616 -20.979 1.00 65.33 C ANISOU 956 CG TYR B 51 6514 7716 10590 731 169 620 C ATOM 957 CD1 TYR B 51 -0.608 8.822 -22.270 1.00 66.51 C ANISOU 957 CD1 TYR B 51 6714 7840 10717 714 -16 688 C ATOM 958 CD2 TYR B 51 -0.203 8.777 -19.921 1.00 65.63 C ANISOU 958 CD2 TYR B 51 6725 7719 10492 707 294 502 C ATOM 959 CE1 TYR B 51 0.735 9.109 -22.505 1.00 65.71 C ANISOU 959 CE1 TYR B 51 6808 7688 10472 668 -54 637 C ATOM 960 CE2 TYR B 51 1.142 9.073 -20.142 1.00 65.30 C ANISOU 960 CE2 TYR B 51 6869 7626 10318 663 229 454 C ATOM 961 CZ TYR B 51 1.605 9.243 -21.437 1.00 72.08 C ANISOU 961 CZ TYR B 51 7751 8464 11170 645 66 520 C ATOM 962 OH TYR B 51 2.928 9.534 -21.668 1.00 72.29 O ANISOU 962 OH TYR B 51 7940 8444 11082 594 23 470 O ATOM 963 N TYR B 52 -5.392 6.702 -20.727 1.00 67.04 N ANISOU 963 N TYR B 52 5965 8195 11310 719 256 824 N ATOM 964 CA TYR B 52 -6.480 6.009 -20.030 1.00 68.25 C ANISOU 964 CA TYR B 52 5923 8432 11575 678 394 832 C ATOM 965 C TYR B 52 -6.913 4.727 -20.755 1.00 71.79 C ANISOU 965 C TYR B 52 6267 8981 12028 532 215 923 C ATOM 966 O TYR B 52 -7.399 3.804 -20.101 1.00 72.07 O ANISOU 966 O TYR B 52 6234 9089 12060 430 319 916 O ATOM 967 CB TYR B 52 -7.682 6.938 -19.777 1.00 71.95 C ANISOU 967 CB TYR B 52 6140 8872 12326 836 529 848 C ATOM 968 CG TYR B 52 -7.564 7.772 -18.518 1.00 74.24 C ANISOU 968 CG TYR B 52 6515 9089 12605 934 819 724 C ATOM 969 CD1 TYR B 52 -7.724 7.198 -17.260 1.00 76.63 C ANISOU 969 CD1 TYR B 52 6856 9439 12820 858 1062 643 C ATOM 970 CD2 TYR B 52 -7.346 9.144 -18.586 1.00 75.48 C ANISOU 970 CD2 TYR B 52 6724 9119 12836 1098 855 688 C ATOM 971 CE1 TYR B 52 -7.627 7.963 -16.098 1.00 78.32 C ANISOU 971 CE1 TYR B 52 7176 9582 12999 938 1332 520 C ATOM 972 CE2 TYR B 52 -7.251 9.920 -17.432 1.00 77.27 C ANISOU 972 CE2 TYR B 52 7048 9266 13046 1183 1124 562 C ATOM 973 CZ TYR B 52 -7.388 9.324 -16.189 1.00 85.13 C ANISOU 973 CZ TYR B 52 8094 10317 13935 1101 1363 474 C ATOM 974 OH TYR B 52 -7.294 10.085 -15.049 1.00 87.37 O ANISOU 974 OH TYR B 52 8502 10518 14176 1173 1631 341 O ATOM 975 N ILE B 53 -6.742 4.672 -22.098 1.00 67.50 N ANISOU 975 N ILE B 53 5730 8436 11483 512 -49 1007 N ATOM 976 CA ILE B 53 -7.065 3.499 -22.926 1.00 67.07 C ANISOU 976 CA ILE B 53 5615 8459 11409 365 -249 1085 C ATOM 977 C ILE B 53 -6.076 2.364 -22.590 1.00 68.96 C ANISOU 977 C ILE B 53 6083 8720 11400 218 -239 1022 C ATOM 978 O ILE B 53 -6.503 1.245 -22.304 1.00 69.14 O ANISOU 978 O ILE B 53 6052 8806 11413 91 -225 1036 O ATOM 979 CB ILE B 53 -7.119 3.856 -24.450 1.00 70.17 C ANISOU 979 CB ILE B 53 5990 8830 11839 386 -530 1185 C ATOM 980 CG1 ILE B 53 -8.393 4.672 -24.781 1.00 72.95 C ANISOU 980 CG1 ILE B 53 6055 9177 12484 512 -580 1277 C ATOM 981 CG2 ILE B 53 -7.033 2.602 -25.343 1.00 70.09 C ANISOU 981 CG2 ILE B 53 6035 8880 11717 211 -741 1232 C ATOM 982 CD1 ILE B 53 -8.342 5.498 -26.071 1.00 79.00 C ANISOU 982 CD1 ILE B 53 6849 9881 13288 588 -822 1372 C ATOM 983 N ILE B 54 -4.768 2.680 -22.575 1.00 63.20 N ANISOU 983 N ILE B 54 5598 7929 10488 238 -240 954 N ATOM 984 CA ILE B 54 -3.687 1.748 -22.247 1.00 61.24 C ANISOU 984 CA ILE B 54 5566 7681 10021 130 -238 890 C ATOM 985 C ILE B 54 -3.774 1.302 -20.769 1.00 65.22 C ANISOU 985 C ILE B 54 6099 8203 10477 94 -25 828 C ATOM 986 O ILE B 54 -3.481 0.142 -20.474 1.00 64.14 O ANISOU 986 O ILE B 54 6054 8092 10226 -27 -40 818 O ATOM 987 CB ILE B 54 -2.306 2.362 -22.663 1.00 62.85 C ANISOU 987 CB ILE B 54 5982 7814 10085 173 -294 837 C ATOM 988 CG1 ILE B 54 -2.149 2.435 -24.215 1.00 63.12 C ANISOU 988 CG1 ILE B 54 6036 7839 10110 154 -512 904 C ATOM 989 CG2 ILE B 54 -1.085 1.690 -21.999 1.00 62.17 C ANISOU 989 CG2 ILE B 54 6103 7713 9807 106 -247 750 C ATOM 990 CD1 ILE B 54 -2.197 1.076 -25.038 1.00 70.57 C ANISOU 990 CD1 ILE B 54 7006 8831 10977 9 -674 941 C ATOM 991 N PHE B 55 -4.232 2.204 -19.867 1.00 62.86 N ANISOU 991 N PHE B 55 5732 7885 10268 195 172 790 N ATOM 992 CA PHE B 55 -4.388 1.939 -18.432 1.00 63.12 C ANISOU 992 CA PHE B 55 5810 7930 10243 163 399 728 C ATOM 993 C PHE B 55 -5.377 0.813 -18.130 1.00 68.34 C ANISOU 993 C PHE B 55 6334 8669 10962 41 450 781 C ATOM 994 O PHE B 55 -4.980 -0.176 -17.520 1.00 67.22 O ANISOU 994 O PHE B 55 6334 8539 10666 -76 479 763 O ATOM 995 CB PHE B 55 -4.742 3.226 -17.645 1.00 66.02 C ANISOU 995 CB PHE B 55 6133 8249 10701 303 612 667 C ATOM 996 CG PHE B 55 -5.344 3.007 -16.271 1.00 68.86 C ANISOU 996 CG PHE B 55 6480 8635 11050 272 877 617 C ATOM 997 CD1 PHE B 55 -4.560 2.568 -15.209 1.00 71.02 C ANISOU 997 CD1 PHE B 55 6996 8892 11094 193 971 545 C ATOM 998 CD2 PHE B 55 -6.696 3.238 -16.041 1.00 73.18 C ANISOU 998 CD2 PHE B 55 6769 9219 11814 316 1032 644 C ATOM 999 CE1 PHE B 55 -5.120 2.351 -13.946 1.00 73.47 C ANISOU 999 CE1 PHE B 55 7327 9224 11364 147 1222 504 C ATOM 1000 CE2 PHE B 55 -7.255 3.020 -14.778 1.00 77.51 C ANISOU 1000 CE2 PHE B 55 7314 9793 12342 274 1308 594 C ATOM 1001 CZ PHE B 55 -6.463 2.582 -13.738 1.00 74.79 C ANISOU 1001 CZ PHE B 55 7247 9432 11739 185 1405 524 C ATOM 1002 N VAL B 56 -6.653 0.973 -18.535 1.00 67.20 N ANISOU 1002 N VAL B 56 5912 8572 11049 66 455 850 N ATOM 1003 CA VAL B 56 -7.725 0.007 -18.274 1.00 68.91 C ANISOU 1003 CA VAL B 56 5952 8866 11364 -56 515 904 C ATOM 1004 C VAL B 56 -7.478 -1.339 -19.007 1.00 72.38 C ANISOU 1004 C VAL B 56 6459 9334 11710 -221 299 960 C ATOM 1005 O VAL B 56 -7.762 -2.384 -18.423 1.00 72.54 O ANISOU 1005 O VAL B 56 6497 9385 11679 -362 372 972 O ATOM 1006 CB VAL B 56 -9.144 0.607 -18.519 1.00 75.27 C ANISOU 1006 CB VAL B 56 6409 9714 12477 24 570 961 C ATOM 1007 CG1 VAL B 56 -9.363 1.001 -19.974 1.00 75.04 C ANISOU 1007 CG1 VAL B 56 6249 9681 12582 83 296 1044 C ATOM 1008 CG2 VAL B 56 -10.253 -0.316 -18.018 1.00 77.08 C ANISOU 1008 CG2 VAL B 56 6442 10024 12819 -110 693 1002 C ATOM 1009 N ILE B 57 -6.905 -1.317 -20.236 1.00 67.88 N ANISOU 1009 N ILE B 57 5953 8740 11098 -211 51 988 N ATOM 1010 CA ILE B 57 -6.587 -2.534 -20.999 1.00 66.89 C ANISOU 1010 CA ILE B 57 5920 8622 10870 -357 -148 1022 C ATOM 1011 C ILE B 57 -5.488 -3.326 -20.274 1.00 69.58 C ANISOU 1011 C ILE B 57 6533 8921 10982 -427 -96 957 C ATOM 1012 O ILE B 57 -5.660 -4.520 -20.026 1.00 69.33 O ANISOU 1012 O ILE B 57 6542 8900 10899 -570 -104 978 O ATOM 1013 CB ILE B 57 -6.259 -2.234 -22.496 1.00 69.26 C ANISOU 1013 CB ILE B 57 6241 8904 11170 -326 -402 1059 C ATOM 1014 CG1 ILE B 57 -7.541 -1.841 -23.267 1.00 71.90 C ANISOU 1014 CG1 ILE B 57 6294 9288 11738 -305 -512 1153 C ATOM 1015 CG2 ILE B 57 -5.551 -3.425 -23.182 1.00 68.53 C ANISOU 1015 CG2 ILE B 57 6334 8793 10913 -460 -571 1053 C ATOM 1016 CD1 ILE B 57 -7.314 -1.106 -24.602 1.00 80.08 C ANISOU 1016 CD1 ILE B 57 7348 10293 12784 -232 -732 1198 C ATOM 1017 N GLY B 58 -4.409 -2.634 -19.909 1.00 65.29 N ANISOU 1017 N GLY B 58 6165 8324 10319 -329 -46 884 N ATOM 1018 CA GLY B 58 -3.268 -3.198 -19.199 1.00 63.96 C ANISOU 1018 CA GLY B 58 6245 8109 9949 -368 -17 823 C ATOM 1019 C GLY B 58 -3.582 -3.666 -17.792 1.00 69.31 C ANISOU 1019 C GLY B 58 6971 8796 10569 -433 175 809 C ATOM 1020 O GLY B 58 -3.080 -4.711 -17.369 1.00 68.65 O ANISOU 1020 O GLY B 58 7049 8685 10351 -531 149 807 O ATOM 1021 N PHE B 59 -4.412 -2.899 -17.056 1.00 67.61 N ANISOU 1021 N PHE B 59 6627 8609 10453 -377 376 800 N ATOM 1022 CA PHE B 59 -4.820 -3.228 -15.688 1.00 68.95 C ANISOU 1022 CA PHE B 59 6845 8791 10562 -443 599 784 C ATOM 1023 C PHE B 59 -5.672 -4.499 -15.668 1.00 74.44 C ANISOU 1023 C PHE B 59 7453 9529 11300 -610 601 860 C ATOM 1024 O PHE B 59 -5.456 -5.353 -14.810 1.00 74.38 O ANISOU 1024 O PHE B 59 7612 9501 11148 -721 671 863 O ATOM 1025 CB PHE B 59 -5.580 -2.057 -15.038 1.00 72.42 C ANISOU 1025 CB PHE B 59 7148 9248 11121 -336 832 747 C ATOM 1026 CG PHE B 59 -5.653 -2.102 -13.529 1.00 75.23 C ANISOU 1026 CG PHE B 59 7641 9596 11349 -379 1087 695 C ATOM 1027 CD1 PHE B 59 -4.662 -1.515 -12.751 1.00 77.68 C ANISOU 1027 CD1 PHE B 59 8195 9846 11476 -322 1144 609 C ATOM 1028 CD2 PHE B 59 -6.726 -2.710 -12.886 1.00 79.37 C ANISOU 1028 CD2 PHE B 59 8055 10172 11930 -489 1274 733 C ATOM 1029 CE1 PHE B 59 -4.731 -1.555 -11.355 1.00 79.93 C ANISOU 1029 CE1 PHE B 59 8638 10119 11612 -374 1370 560 C ATOM 1030 CE2 PHE B 59 -6.793 -2.750 -11.490 1.00 83.50 C ANISOU 1030 CE2 PHE B 59 8735 10685 12306 -542 1524 685 C ATOM 1031 CZ PHE B 59 -5.797 -2.171 -10.735 1.00 80.90 C ANISOU 1031 CZ PHE B 59 8672 10293 11773 -483 1566 599 C ATOM 1032 N LEU B 60 -6.616 -4.629 -16.624 1.00 71.95 N ANISOU 1032 N LEU B 60 6891 9266 11182 -637 507 927 N ATOM 1033 CA LEU B 60 -7.513 -5.780 -16.751 1.00 73.10 C ANISOU 1033 CA LEU B 60 6919 9453 11403 -808 486 1001 C ATOM 1034 C LEU B 60 -6.786 -7.077 -17.114 1.00 75.89 C ANISOU 1034 C LEU B 60 7479 9755 11602 -936 304 1020 C ATOM 1035 O LEU B 60 -7.090 -8.110 -16.519 1.00 76.39 O ANISOU 1035 O LEU B 60 7602 9811 11613 -1087 369 1054 O ATOM 1036 CB LEU B 60 -8.646 -5.484 -17.751 1.00 74.47 C ANISOU 1036 CB LEU B 60 6770 9691 11835 -796 393 1065 C ATOM 1037 CG LEU B 60 -10.034 -5.176 -17.166 1.00 81.86 C ANISOU 1037 CG LEU B 60 7414 10698 12990 -807 611 1094 C ATOM 1038 CD1 LEU B 60 -10.058 -3.846 -16.418 1.00 82.54 C ANISOU 1038 CD1 LEU B 60 7466 10777 13120 -630 837 1025 C ATOM 1039 CD2 LEU B 60 -11.077 -5.141 -18.258 1.00 85.66 C ANISOU 1039 CD2 LEU B 60 7580 11240 13728 -824 449 1173 C ATOM 1040 N VAL B 61 -5.823 -7.027 -18.064 1.00 70.61 N ANISOU 1040 N VAL B 61 6926 9041 10860 -877 93 996 N ATOM 1041 CA VAL B 61 -5.062 -8.212 -18.492 1.00 69.43 C ANISOU 1041 CA VAL B 61 6973 8828 10580 -975 -75 998 C ATOM 1042 C VAL B 61 -4.074 -8.683 -17.408 1.00 73.27 C ANISOU 1042 C VAL B 61 7726 9244 10868 -987 -4 959 C ATOM 1043 O VAL B 61 -3.868 -9.890 -17.273 1.00 73.30 O ANISOU 1043 O VAL B 61 7866 9195 10791 -1105 -64 984 O ATOM 1044 CB VAL B 61 -4.382 -8.093 -19.888 1.00 71.73 C ANISOU 1044 CB VAL B 61 7304 9092 10857 -921 -302 979 C ATOM 1045 CG1 VAL B 61 -5.418 -7.960 -21.001 1.00 72.52 C ANISOU 1045 CG1 VAL B 61 7178 9250 11125 -957 -424 1038 C ATOM 1046 CG2 VAL B 61 -3.359 -6.959 -19.946 1.00 70.02 C ANISOU 1046 CG2 VAL B 61 7173 8852 10578 -754 -295 912 C ATOM 1047 N ASN B 62 -3.483 -7.743 -16.636 1.00 69.24 N ANISOU 1047 N ASN B 62 7298 8726 10285 -868 112 902 N ATOM 1048 CA ASN B 62 -2.538 -8.067 -15.564 1.00 68.54 C ANISOU 1048 CA ASN B 62 7462 8574 10007 -874 158 868 C ATOM 1049 C ASN B 62 -3.232 -8.534 -14.283 1.00 74.77 C ANISOU 1049 C ASN B 62 8298 9374 10738 -986 353 904 C ATOM 1050 O ASN B 62 -2.633 -9.300 -13.527 1.00 74.63 O ANISOU 1050 O ASN B 62 8506 9291 10559 -1051 341 914 O ATOM 1051 CB ASN B 62 -1.566 -6.923 -15.300 1.00 67.24 C ANISOU 1051 CB ASN B 62 7384 8390 9774 -725 174 789 C ATOM 1052 CG ASN B 62 -0.445 -6.865 -16.305 1.00 85.47 C ANISOU 1052 CG ASN B 62 9755 10657 12064 -654 -23 752 C ATOM 1053 OD1 ASN B 62 0.551 -7.590 -16.208 1.00 79.08 O ANISOU 1053 OD1 ASN B 62 9119 9782 11147 -672 -128 736 O ATOM 1054 ND2 ASN B 62 -0.589 -6.016 -17.308 1.00 75.86 N ANISOU 1054 ND2 ASN B 62 8396 9471 10957 -572 -73 741 N ATOM 1055 N ILE B 63 -4.495 -8.099 -14.052 1.00 73.26 N ANISOU 1055 N ILE B 63 7895 9258 10683 -1010 532 928 N ATOM 1056 CA ILE B 63 -5.311 -8.514 -12.901 1.00 75.24 C ANISOU 1056 CA ILE B 63 8159 9530 10898 -1131 758 963 C ATOM 1057 C ILE B 63 -5.626 -10.012 -13.024 1.00 80.31 C ANISOU 1057 C ILE B 63 8852 10142 11522 -1319 679 1044 C ATOM 1058 O ILE B 63 -5.558 -10.728 -12.026 1.00 81.01 O ANISOU 1058 O ILE B 63 9130 10187 11463 -1432 773 1074 O ATOM 1059 CB ILE B 63 -6.576 -7.604 -12.723 1.00 80.08 C ANISOU 1059 CB ILE B 63 8493 10233 11703 -1091 982 957 C ATOM 1060 CG1 ILE B 63 -6.315 -6.436 -11.728 1.00 80.72 C ANISOU 1060 CG1 ILE B 63 8661 10309 11700 -971 1189 873 C ATOM 1061 CG2 ILE B 63 -7.872 -8.369 -12.373 1.00 83.35 C ANISOU 1061 CG2 ILE B 63 8750 10698 12222 -1263 1138 1028 C ATOM 1062 CD1 ILE B 63 -5.971 -6.796 -10.216 1.00 88.50 C ANISOU 1062 CD1 ILE B 63 9937 11254 12436 -1060 1366 854 C ATOM 1063 N VAL B 64 -5.915 -10.476 -14.262 1.00 76.87 N ANISOU 1063 N VAL B 64 8272 9715 11220 -1356 493 1078 N ATOM 1064 CA VAL B 64 -6.217 -11.868 -14.616 1.00 77.58 C ANISOU 1064 CA VAL B 64 8398 9763 11316 -1534 383 1145 C ATOM 1065 C VAL B 64 -5.047 -12.784 -14.225 1.00 81.67 C ANISOU 1065 C VAL B 64 9246 10159 11626 -1564 274 1143 C ATOM 1066 O VAL B 64 -5.272 -13.785 -13.547 1.00 82.75 O ANISOU 1066 O VAL B 64 9514 10243 11684 -1715 327 1201 O ATOM 1067 CB VAL B 64 -6.622 -12.001 -16.115 1.00 80.93 C ANISOU 1067 CB VAL B 64 8629 10214 11905 -1546 180 1161 C ATOM 1068 CG1 VAL B 64 -6.713 -13.461 -16.560 1.00 81.10 C ANISOU 1068 CG1 VAL B 64 8743 10165 11906 -1724 34 1211 C ATOM 1069 CG2 VAL B 64 -7.936 -11.279 -16.390 1.00 82.33 C ANISOU 1069 CG2 VAL B 64 8464 10505 12311 -1543 276 1189 C ATOM 1070 N VAL B 65 -3.807 -12.408 -14.613 1.00 76.74 N ANISOU 1070 N VAL B 65 8748 9487 10924 -1419 129 1080 N ATOM 1071 CA VAL B 65 -2.569 -13.148 -14.328 1.00 76.00 C ANISOU 1071 CA VAL B 65 8935 9276 10667 -1407 2 1068 C ATOM 1072 C VAL B 65 -2.311 -13.234 -12.810 1.00 81.87 C ANISOU 1072 C VAL B 65 9885 9984 11238 -1440 139 1088 C ATOM 1073 O VAL B 65 -1.976 -14.313 -12.314 1.00 82.16 O ANISOU 1073 O VAL B 65 10131 9922 11164 -1533 83 1138 O ATOM 1074 CB VAL B 65 -1.348 -12.579 -15.110 1.00 77.88 C ANISOU 1074 CB VAL B 65 9210 9488 10893 -1239 -157 989 C ATOM 1075 CG1 VAL B 65 -0.120 -13.474 -14.954 1.00 77.15 C ANISOU 1075 CG1 VAL B 65 9364 9269 10682 -1226 -305 979 C ATOM 1076 CG2 VAL B 65 -1.674 -12.391 -16.589 1.00 77.04 C ANISOU 1076 CG2 VAL B 65 8921 9422 10929 -1218 -273 973 C ATOM 1077 N VAL B 66 -2.499 -12.110 -12.082 1.00 79.60 N ANISOU 1077 N VAL B 66 9553 9766 10924 -1368 316 1049 N ATOM 1078 CA VAL B 66 -2.316 -12.019 -10.626 1.00 81.02 C ANISOU 1078 CA VAL B 66 9942 9924 10920 -1402 464 1056 C ATOM 1079 C VAL B 66 -3.367 -12.878 -9.884 1.00 88.53 C ANISOU 1079 C VAL B 66 10923 10874 11838 -1600 632 1143 C ATOM 1080 O VAL B 66 -2.992 -13.665 -9.011 1.00 89.12 O ANISOU 1080 O VAL B 66 11261 10865 11735 -1692 625 1194 O ATOM 1081 CB VAL B 66 -2.253 -10.542 -10.130 1.00 84.76 C ANISOU 1081 CB VAL B 66 10367 10462 11376 -1273 615 974 C ATOM 1082 CG1 VAL B 66 -2.323 -10.443 -8.606 1.00 86.25 C ANISOU 1082 CG1 VAL B 66 10767 10637 11365 -1339 808 978 C ATOM 1083 CG2 VAL B 66 -0.996 -9.844 -10.647 1.00 82.45 C ANISOU 1083 CG2 VAL B 66 10118 10142 11069 -1108 439 898 C ATOM 1084 N THR B 67 -4.661 -12.759 -10.264 1.00 87.07 N ANISOU 1084 N THR B 67 10470 10779 11835 -1670 769 1166 N ATOM 1085 CA THR B 67 -5.762 -13.532 -9.668 1.00 89.77 C ANISOU 1085 CA THR B 67 10788 11135 12187 -1873 949 1247 C ATOM 1086 C THR B 67 -5.685 -15.030 -10.006 1.00 95.30 C ANISOU 1086 C THR B 67 11609 11734 12865 -2028 783 1330 C ATOM 1087 O THR B 67 -6.177 -15.848 -9.226 1.00 96.95 O ANISOU 1087 O THR B 67 11941 11906 12992 -2208 903 1407 O ATOM 1088 CB THR B 67 -7.138 -12.935 -10.010 1.00 98.31 C ANISOU 1088 CB THR B 67 11509 12342 13503 -1894 1132 1244 C ATOM 1089 OG1 THR B 67 -7.255 -12.775 -11.424 1.00 96.64 O ANISOU 1089 OG1 THR B 67 11065 12162 13490 -1824 933 1232 O ATOM 1090 CG2 THR B 67 -7.402 -11.612 -9.301 1.00 97.06 C ANISOU 1090 CG2 THR B 67 11275 12258 13346 -1778 1377 1172 C ATOM 1091 N LEU B 68 -5.066 -15.385 -11.157 1.00 91.13 N ANISOU 1091 N LEU B 68 11065 11155 12404 -1964 520 1312 N ATOM 1092 CA LEU B 68 -4.887 -16.773 -11.597 1.00 91.72 C ANISOU 1092 CA LEU B 68 11268 11113 12467 -2087 344 1370 C ATOM 1093 C LEU B 68 -3.849 -17.483 -10.729 1.00 96.94 C ANISOU 1093 C LEU B 68 12289 11634 12910 -2094 269 1403 C ATOM 1094 O LEU B 68 -4.055 -18.635 -10.361 1.00 97.86 O ANISOU 1094 O LEU B 68 12566 11652 12965 -2257 256 1486 O ATOM 1095 CB LEU B 68 -4.464 -16.838 -13.074 1.00 90.04 C ANISOU 1095 CB LEU B 68 10953 10884 12375 -2000 106 1321 C ATOM 1096 CG LEU B 68 -5.180 -17.869 -13.945 1.00 95.85 C ANISOU 1096 CG LEU B 68 11603 11584 13230 -2163 3 1367 C ATOM 1097 CD1 LEU B 68 -5.235 -17.411 -15.386 1.00 94.75 C ANISOU 1097 CD1 LEU B 68 11261 11501 13236 -2080 -150 1309 C ATOM 1098 CD2 LEU B 68 -4.514 -19.238 -13.858 1.00 99.07 C ANISOU 1098 CD2 LEU B 68 12295 11815 13530 -2246 -142 1404 C ATOM 1099 N PHE B 69 -2.743 -16.794 -10.398 1.00 93.22 N ANISOU 1099 N PHE B 69 11943 11149 12329 -1924 209 1342 N ATOM 1100 CA PHE B 69 -1.668 -17.332 -9.562 1.00 93.70 C ANISOU 1100 CA PHE B 69 12328 11082 12193 -1904 105 1371 C ATOM 1101 C PHE B 69 -2.115 -17.492 -8.102 1.00101.40 C ANISOU 1101 C PHE B 69 13494 12048 12985 -2039 301 1444 C ATOM 1102 O PHE B 69 -1.621 -18.383 -7.409 1.00102.08 O ANISOU 1102 O PHE B 69 13865 12005 12916 -2110 219 1518 O ATOM 1103 CB PHE B 69 -0.430 -16.426 -9.653 1.00 93.49 C ANISOU 1103 CB PHE B 69 12336 11061 12125 -1693 -12 1281 C ATOM 1104 CG PHE B 69 0.846 -17.003 -9.088 1.00 94.86 C ANISOU 1104 CG PHE B 69 12795 11097 12150 -1640 -195 1302 C ATOM 1105 CD1 PHE B 69 1.690 -17.773 -9.880 1.00 97.01 C ANISOU 1105 CD1 PHE B 69 13114 11256 12490 -1575 -425 1293 C ATOM 1106 CD2 PHE B 69 1.228 -16.740 -7.778 1.00 97.84 C ANISOU 1106 CD2 PHE B 69 13394 11454 12327 -1648 -144 1327 C ATOM 1107 CE1 PHE B 69 2.878 -18.295 -9.361 1.00 98.08 C ANISOU 1107 CE1 PHE B 69 13486 11259 12522 -1509 -604 1315 C ATOM 1108 CE2 PHE B 69 2.415 -17.264 -7.259 1.00100.78 C ANISOU 1108 CE2 PHE B 69 14019 11697 12576 -1595 -346 1356 C ATOM 1109 CZ PHE B 69 3.233 -18.036 -8.054 1.00 98.06 C ANISOU 1109 CZ PHE B 69 13689 11241 12329 -1519 -578 1353 C ATOM 1110 N CYS B 70 -3.051 -16.636 -7.646 1.00100.09 N ANISOU 1110 N CYS B 70 13179 12012 12841 -2074 564 1422 N ATOM 1111 CA CYS B 70 -3.571 -16.633 -6.280 1.00102.84 C ANISOU 1111 CA CYS B 70 13692 12370 13012 -2204 805 1472 C ATOM 1112 C CYS B 70 -4.543 -17.784 -5.981 1.00110.66 C ANISOU 1112 C CYS B 70 14725 13318 14001 -2448 919 1586 C ATOM 1113 O CYS B 70 -4.319 -18.511 -5.011 1.00111.86 O ANISOU 1113 O CYS B 70 15188 13370 13945 -2568 935 1670 O ATOM 1114 CB CYS B 70 -4.186 -15.279 -5.933 1.00103.46 C ANISOU 1114 CB CYS B 70 13590 12591 13128 -2138 1064 1391 C ATOM 1115 SG CYS B 70 -2.975 -13.956 -5.667 1.00105.48 S ANISOU 1115 SG CYS B 70 13942 12862 13275 -1907 985 1273 S ATOM 1116 N CYS B 71 -5.623 -17.940 -6.783 1.00108.89 N ANISOU 1116 N CYS B 71 14199 13168 14006 -2533 992 1595 N ATOM 1117 CA CYS B 71 -6.648 -18.962 -6.531 1.00111.77 C ANISOU 1117 CA CYS B 71 14563 13505 14399 -2785 1120 1698 C ATOM 1118 C CYS B 71 -7.125 -19.723 -7.793 1.00116.60 C ANISOU 1118 C CYS B 71 14970 14097 15236 -2863 960 1722 C ATOM 1119 O CYS B 71 -8.312 -20.054 -7.894 1.00118.07 O ANISOU 1119 O CYS B 71 14963 14339 15559 -3041 1108 1768 O ATOM 1120 CB CYS B 71 -7.823 -18.349 -5.769 1.00114.33 C ANISOU 1120 CB CYS B 71 14733 13959 14749 -2885 1489 1696 C ATOM 1121 SG CYS B 71 -8.614 -16.952 -6.613 1.00117.34 S ANISOU 1121 SG CYS B 71 14629 14530 15425 -2730 1607 1587 S ATOM 1122 N GLN B 72 -6.200 -20.047 -8.723 1.00112.00 N ANISOU 1122 N GLN B 72 14442 13428 14686 -2744 662 1688 N ATOM 1123 CA GLN B 72 -6.524 -20.789 -9.953 1.00111.93 C ANISOU 1123 CA GLN B 72 14291 13380 14856 -2814 487 1696 C ATOM 1124 C GLN B 72 -5.346 -21.601 -10.534 1.00115.04 C ANISOU 1124 C GLN B 72 14911 13604 15193 -2736 193 1685 C ATOM 1125 O GLN B 72 -5.560 -22.408 -11.443 1.00114.87 O ANISOU 1125 O GLN B 72 14848 13514 15281 -2820 50 1694 O ATOM 1126 CB GLN B 72 -7.119 -19.851 -11.022 1.00112.28 C ANISOU 1126 CB GLN B 72 13955 13580 15128 -2722 485 1620 C ATOM 1127 N LYS B 73 -4.118 -21.398 -10.008 1.00110.75 N ANISOU 1127 N LYS B 73 14602 12988 14489 -2580 102 1663 N ATOM 1128 CA LYS B 73 -2.910 -22.080 -10.484 1.00109.46 C ANISOU 1128 CA LYS B 73 14634 12665 14292 -2475 -162 1644 C ATOM 1129 C LYS B 73 -2.054 -22.637 -9.332 1.00114.34 C ANISOU 1129 C LYS B 73 15608 13136 14700 -2470 -216 1715 C ATOM 1130 O LYS B 73 -1.874 -23.853 -9.246 1.00115.13 O ANISOU 1130 O LYS B 73 15919 13062 14763 -2567 -328 1789 O ATOM 1131 CB LYS B 73 -2.103 -21.145 -11.407 1.00109.41 C ANISOU 1131 CB LYS B 73 14478 12725 14366 -2240 -285 1521 C ATOM 1132 CG LYS B 73 -1.029 -21.833 -12.249 1.00122.36 C ANISOU 1132 CG LYS B 73 16232 14220 16037 -2135 -534 1477 C ATOM 1133 CD LYS B 73 -0.742 -21.090 -13.566 1.00130.21 C ANISOU 1133 CD LYS B 73 17008 15300 17165 -1988 -618 1361 C ATOM 1134 CE LYS B 73 -0.026 -19.760 -13.419 1.00139.46 C ANISOU 1134 CE LYS B 73 18104 16576 18310 -1790 -592 1285 C ATOM 1135 NZ LYS B 73 1.372 -19.922 -12.945 1.00147.93 N ANISOU 1135 NZ LYS B 73 19385 17536 19284 -1654 -720 1267 N ATOM 1136 N GLY B 74 -1.546 -21.750 -8.474 1.00110.49 N ANISOU 1136 N GLY B 74 15194 12710 14078 -2362 -150 1693 N ATOM 1137 CA GLY B 74 -0.713 -22.118 -7.331 1.00111.21 C ANISOU 1137 CA GLY B 74 15622 12679 13955 -2350 -221 1760 C ATOM 1138 C GLY B 74 0.709 -21.578 -7.371 1.00112.98 C ANISOU 1138 C GLY B 74 15913 12874 14142 -2117 -414 1688 C ATOM 1139 O GLY B 74 1.091 -20.913 -8.340 1.00110.44 O ANISOU 1139 O GLY B 74 15377 12625 13961 -1962 -482 1579 O ATOM 1140 N PRO B 75 1.540 -21.866 -6.335 1.00110.20 N ANISOU 1140 N PRO B 75 15860 12411 13601 -2093 -519 1751 N ATOM 1141 CA PRO B 75 2.915 -21.336 -6.321 1.00108.42 C ANISOU 1141 CA PRO B 75 15677 12161 13356 -1879 -715 1684 C ATOM 1142 C PRO B 75 3.988 -22.287 -6.879 1.00111.20 C ANISOU 1142 C PRO B 75 16124 12333 13796 -1768 -997 1692 C ATOM 1143 O PRO B 75 5.177 -22.085 -6.619 1.00110.51 O ANISOU 1143 O PRO B 75 16120 12190 13677 -1615 -1177 1668 O ATOM 1144 CB PRO B 75 3.137 -21.020 -4.836 1.00111.81 C ANISOU 1144 CB PRO B 75 16368 12586 13529 -1924 -669 1746 C ATOM 1145 CG PRO B 75 2.179 -21.951 -4.088 1.00118.95 C ANISOU 1145 CG PRO B 75 17473 13420 14303 -2164 -532 1884 C ATOM 1146 CD PRO B 75 1.260 -22.610 -5.091 1.00114.37 C ANISOU 1146 CD PRO B 75 16701 12838 13918 -2267 -464 1890 C ATOM 1147 N LYS B 76 3.577 -23.312 -7.649 1.00107.39 N ANISOU 1147 N LYS B 76 15618 11751 13435 -1845 -1034 1719 N ATOM 1148 CA LYS B 76 4.478 -24.309 -8.248 1.00106.80 C ANISOU 1148 CA LYS B 76 15633 11484 13462 -1747 -1272 1717 C ATOM 1149 C LYS B 76 5.178 -23.760 -9.510 1.00107.46 C ANISOU 1149 C LYS B 76 15475 11623 13731 -1552 -1354 1567 C ATOM 1150 O LYS B 76 4.759 -22.725 -10.032 1.00105.48 O ANISOU 1150 O LYS B 76 14987 11554 13536 -1527 -1225 1481 O ATOM 1151 CB LYS B 76 3.717 -25.615 -8.571 1.00110.75 C ANISOU 1151 CB LYS B 76 16227 11844 14008 -1923 -1265 1795 C ATOM 1152 CG LYS B 76 2.972 -26.236 -7.387 1.00125.71 C ANISOU 1152 CG LYS B 76 18368 13672 15723 -2143 -1165 1952 C ATOM 1153 CD LYS B 76 1.465 -26.031 -7.506 1.00135.21 C ANISOU 1153 CD LYS B 76 19409 15018 16947 -2355 -906 1966 C ATOM 1154 CE LYS B 76 0.742 -26.297 -6.210 1.00147.18 C ANISOU 1154 CE LYS B 76 21136 16522 18264 -2565 -742 2102 C ATOM 1155 NZ LYS B 76 -0.722 -26.081 -6.344 1.00155.98 N ANISOU 1155 NZ LYS B 76 22051 17782 19434 -2766 -475 2108 N ATOM 1156 N LYS B 77 6.248 -24.457 -9.982 1.00103.21 N ANISOU 1156 N LYS B 77 15005 10921 13289 -1413 -1561 1539 N ATOM 1157 CA LYS B 77 7.079 -24.173 -11.172 1.00100.90 C ANISOU 1157 CA LYS B 77 14529 10637 13169 -1229 -1647 1400 C ATOM 1158 C LYS B 77 7.989 -22.939 -11.036 1.00102.45 C ANISOU 1158 C LYS B 77 14600 10957 13370 -1057 -1674 1317 C ATOM 1159 O LYS B 77 7.591 -21.925 -10.460 1.00101.32 O ANISOU 1159 O LYS B 77 14401 10970 13127 -1094 -1552 1319 O ATOM 1160 CB LYS B 77 6.247 -24.091 -12.465 1.00102.27 C ANISOU 1160 CB LYS B 77 14503 10895 13460 -1295 -1538 1320 C ATOM 1161 N VAL B 78 9.215 -23.042 -11.599 1.00 97.98 N ANISOU 1161 N VAL B 78 13985 10312 12930 -871 -1824 1237 N ATOM 1162 CA VAL B 78 10.270 -22.013 -11.592 1.00 96.23 C ANISOU 1162 CA VAL B 78 13636 10178 12751 -701 -1879 1151 C ATOM 1163 C VAL B 78 9.851 -20.773 -12.387 1.00 96.87 C ANISOU 1163 C VAL B 78 13471 10461 12873 -693 -1717 1045 C ATOM 1164 O VAL B 78 9.848 -19.669 -11.838 1.00 95.86 O ANISOU 1164 O VAL B 78 13287 10466 12668 -683 -1654 1032 O ATOM 1165 CB VAL B 78 11.650 -22.541 -12.089 1.00100.52 C ANISOU 1165 CB VAL B 78 14161 10576 13456 -512 -2062 1088 C ATOM 1166 CG1 VAL B 78 12.795 -21.925 -11.294 1.00100.75 C ANISOU 1166 CG1 VAL B 78 14189 10619 13471 -382 -2200 1086 C ATOM 1167 CG2 VAL B 78 11.730 -24.068 -12.065 1.00102.02 C ANISOU 1167 CG2 VAL B 78 14543 10531 13688 -527 -2182 1159 C ATOM 1168 N SER B 79 9.509 -20.966 -13.680 1.00 91.47 N ANISOU 1168 N SER B 79 12660 9789 12306 -699 -1661 970 N ATOM 1169 CA SER B 79 9.091 -19.920 -14.619 1.00 88.97 C ANISOU 1169 CA SER B 79 12124 9641 12039 -692 -1532 879 C ATOM 1170 C SER B 79 7.839 -19.171 -14.163 1.00 91.06 C ANISOU 1170 C SER B 79 12331 10058 12209 -823 -1369 929 C ATOM 1171 O SER B 79 7.769 -17.956 -14.343 1.00 89.43 O ANISOU 1171 O SER B 79 11974 9995 12009 -779 -1283 874 O ATOM 1172 CB SER B 79 8.874 -20.508 -16.010 1.00 92.22 C ANISOU 1172 CB SER B 79 12473 10006 12560 -706 -1527 811 C ATOM 1173 OG SER B 79 7.921 -21.558 -15.983 1.00102.21 O ANISOU 1173 OG SER B 79 13851 11187 13798 -862 -1518 887 O ATOM 1174 N SER B 80 6.871 -19.893 -13.555 1.00 87.72 N ANISOU 1174 N SER B 80 12026 9594 11708 -983 -1320 1033 N ATOM 1175 CA SER B 80 5.601 -19.363 -13.048 1.00 87.13 C ANISOU 1175 CA SER B 80 11898 9649 11560 -1121 -1145 1087 C ATOM 1176 C SER B 80 5.762 -18.267 -11.988 1.00 88.85 C ANISOU 1176 C SER B 80 12127 9966 11665 -1083 -1068 1091 C ATOM 1177 O SER B 80 4.922 -17.367 -11.927 1.00 88.21 O ANISOU 1177 O SER B 80 11915 10026 11576 -1126 -905 1078 O ATOM 1178 CB SER B 80 4.726 -20.491 -12.514 1.00 92.63 C ANISOU 1178 CB SER B 80 12745 10255 12195 -1304 -1114 1201 C ATOM 1179 OG SER B 80 4.364 -21.393 -13.547 1.00101.91 O ANISOU 1179 OG SER B 80 13894 11353 13476 -1368 -1163 1189 O ATOM 1180 N ILE B 81 6.833 -18.341 -11.162 1.00 84.02 N ANISOU 1180 N ILE B 81 11675 9275 10974 -1001 -1193 1106 N ATOM 1181 CA ILE B 81 7.150 -17.353 -10.120 1.00 83.06 C ANISOU 1181 CA ILE B 81 11606 9226 10726 -967 -1156 1101 C ATOM 1182 C ILE B 81 7.489 -16.003 -10.781 1.00 83.13 C ANISOU 1182 C ILE B 81 11399 9364 10821 -848 -1108 983 C ATOM 1183 O ILE B 81 7.036 -14.957 -10.309 1.00 82.25 O ANISOU 1183 O ILE B 81 11241 9365 10645 -865 -969 961 O ATOM 1184 CB ILE B 81 8.280 -17.863 -9.162 1.00 87.29 C ANISOU 1184 CB ILE B 81 12369 9631 11165 -913 -1353 1152 C ATOM 1185 CG1 ILE B 81 7.927 -19.223 -8.493 1.00 89.90 C ANISOU 1185 CG1 ILE B 81 12943 9813 11400 -1037 -1407 1286 C ATOM 1186 CG2 ILE B 81 8.691 -16.813 -8.116 1.00 88.02 C ANISOU 1186 CG2 ILE B 81 12533 9796 11116 -885 -1341 1135 C ATOM 1187 CD1 ILE B 81 6.709 -19.251 -7.484 1.00 99.13 C ANISOU 1187 CD1 ILE B 81 14249 11030 12387 -1232 -1215 1380 C ATOM 1188 N TYR B 82 8.251 -16.046 -11.893 1.00 77.12 N ANISOU 1188 N TYR B 82 10517 8577 10208 -734 -1209 906 N ATOM 1189 CA TYR B 82 8.640 -14.865 -12.663 1.00 74.48 C ANISOU 1189 CA TYR B 82 9989 8346 9963 -629 -1172 800 C ATOM 1190 C TYR B 82 7.447 -14.252 -13.394 1.00 75.76 C ANISOU 1190 C TYR B 82 9981 8628 10175 -688 -1006 783 C ATOM 1191 O TYR B 82 7.397 -13.030 -13.521 1.00 74.48 O ANISOU 1191 O TYR B 82 9702 8568 10029 -638 -924 728 O ATOM 1192 CB TYR B 82 9.791 -15.179 -13.639 1.00 74.94 C ANISOU 1192 CB TYR B 82 9982 8335 10158 -506 -1307 726 C ATOM 1193 CG TYR B 82 11.017 -15.786 -12.987 1.00 77.59 C ANISOU 1193 CG TYR B 82 10446 8546 10489 -427 -1490 741 C ATOM 1194 CD1 TYR B 82 11.733 -15.090 -12.016 1.00 79.90 C ANISOU 1194 CD1 TYR B 82 10789 8859 10709 -380 -1554 738 C ATOM 1195 CD2 TYR B 82 11.485 -17.039 -13.368 1.00 79.15 C ANISOU 1195 CD2 TYR B 82 10711 8596 10766 -393 -1611 756 C ATOM 1196 CE1 TYR B 82 12.861 -15.644 -11.413 1.00 81.85 C ANISOU 1196 CE1 TYR B 82 11141 8992 10965 -306 -1753 762 C ATOM 1197 CE2 TYR B 82 12.619 -17.598 -12.781 1.00 81.20 C ANISOU 1197 CE2 TYR B 82 11071 8732 11049 -302 -1795 776 C ATOM 1198 CZ TYR B 82 13.305 -16.896 -11.803 1.00 88.82 C ANISOU 1198 CZ TYR B 82 12072 9728 11946 -259 -1875 784 C ATOM 1199 OH TYR B 82 14.423 -17.441 -11.220 1.00 91.16 O ANISOU 1199 OH TYR B 82 12455 9904 12279 -169 -2086 813 O ATOM 1200 N ILE B 83 6.483 -15.093 -13.849 1.00 71.58 N ANISOU 1200 N ILE B 83 9439 8078 9678 -796 -969 833 N ATOM 1201 CA ILE B 83 5.251 -14.671 -14.539 1.00 70.58 C ANISOU 1201 CA ILE B 83 9142 8058 9617 -866 -841 834 C ATOM 1202 C ILE B 83 4.435 -13.764 -13.607 1.00 73.21 C ANISOU 1202 C ILE B 83 9440 8496 9882 -910 -670 861 C ATOM 1203 O ILE B 83 4.038 -12.672 -14.019 1.00 72.28 O ANISOU 1203 O ILE B 83 9157 8481 9824 -865 -579 818 O ATOM 1204 CB ILE B 83 4.400 -15.887 -15.047 1.00 74.84 C ANISOU 1204 CB ILE B 83 9697 8541 10198 -1000 -858 892 C ATOM 1205 CG1 ILE B 83 5.208 -16.869 -15.951 1.00 75.24 C ANISOU 1205 CG1 ILE B 83 9815 8465 10309 -957 -1015 853 C ATOM 1206 CG2 ILE B 83 3.093 -15.446 -15.733 1.00 75.59 C ANISOU 1206 CG2 ILE B 83 9594 8751 10374 -1080 -751 901 C ATOM 1207 CD1 ILE B 83 5.781 -16.343 -17.290 1.00 81.48 C ANISOU 1207 CD1 ILE B 83 10479 9289 11193 -851 -1059 750 C ATOM 1208 N PHE B 84 4.211 -14.215 -12.352 1.00 69.55 N ANISOU 1208 N PHE B 84 9145 7992 9289 -995 -622 931 N ATOM 1209 CA PHE B 84 3.469 -13.482 -11.325 1.00 69.58 C ANISOU 1209 CA PHE B 84 9159 8077 9203 -1048 -435 951 C ATOM 1210 C PHE B 84 4.179 -12.185 -10.933 1.00 71.07 C ANISOU 1210 C PHE B 84 9342 8314 9345 -927 -416 873 C ATOM 1211 O PHE B 84 3.523 -11.147 -10.840 1.00 70.63 O ANISOU 1211 O PHE B 84 9169 8355 9314 -913 -255 838 O ATOM 1212 CB PHE B 84 3.202 -14.373 -10.093 1.00 73.26 C ANISOU 1212 CB PHE B 84 9854 8470 9510 -1180 -399 1046 C ATOM 1213 CG PHE B 84 2.564 -13.677 -8.911 1.00 76.07 C ANISOU 1213 CG PHE B 84 10271 8895 9737 -1240 -190 1058 C ATOM 1214 CD1 PHE B 84 1.231 -13.282 -8.951 1.00 80.01 C ANISOU 1214 CD1 PHE B 84 10602 9495 10302 -1317 34 1066 C ATOM 1215 CD2 PHE B 84 3.290 -13.435 -7.752 1.00 78.89 C ANISOU 1215 CD2 PHE B 84 10856 9213 9907 -1224 -218 1058 C ATOM 1216 CE1 PHE B 84 0.640 -12.642 -7.857 1.00 82.41 C ANISOU 1216 CE1 PHE B 84 10963 9856 10491 -1368 258 1063 C ATOM 1217 CE2 PHE B 84 2.699 -12.795 -6.658 1.00 83.25 C ANISOU 1217 CE2 PHE B 84 11494 9821 10316 -1288 -8 1057 C ATOM 1218 CZ PHE B 84 1.378 -12.403 -6.717 1.00 82.14 C ANISOU 1218 CZ PHE B 84 11184 9778 10247 -1356 244 1054 C ATOM 1219 N ASN B 85 5.511 -12.245 -10.723 1.00 65.87 N ANISOU 1219 N ASN B 85 8804 7584 8638 -841 -584 842 N ATOM 1220 CA ASN B 85 6.343 -11.097 -10.357 1.00 64.53 C ANISOU 1220 CA ASN B 85 8645 7446 8429 -739 -602 766 C ATOM 1221 C ASN B 85 6.357 -10.024 -11.445 1.00 66.26 C ANISOU 1221 C ASN B 85 8641 7742 8791 -644 -562 682 C ATOM 1222 O ASN B 85 6.301 -8.836 -11.123 1.00 65.45 O ANISOU 1222 O ASN B 85 8502 7699 8668 -602 -464 629 O ATOM 1223 CB ASN B 85 7.754 -11.539 -9.995 1.00 64.17 C ANISOU 1223 CB ASN B 85 8744 7303 8336 -678 -818 761 C ATOM 1224 CG ASN B 85 7.898 -11.924 -8.547 1.00 82.40 C ANISOU 1224 CG ASN B 85 11308 9553 10446 -750 -849 826 C ATOM 1225 OD1 ASN B 85 7.997 -11.070 -7.658 1.00 74.20 O ANISOU 1225 OD1 ASN B 85 10358 8552 9283 -755 -790 796 O ATOM 1226 ND2 ASN B 85 7.910 -13.220 -8.278 1.00 74.87 N ANISOU 1226 ND2 ASN B 85 10499 8498 9449 -814 -945 917 N ATOM 1227 N LEU B 86 6.396 -10.446 -12.729 1.00 61.67 N ANISOU 1227 N LEU B 86 7932 7154 8347 -618 -633 673 N ATOM 1228 CA LEU B 86 6.348 -9.550 -13.888 1.00 59.95 C ANISOU 1228 CA LEU B 86 7524 7002 8254 -544 -606 611 C ATOM 1229 C LEU B 86 4.964 -8.894 -13.964 1.00 64.28 C ANISOU 1229 C LEU B 86 7938 7642 8844 -586 -432 633 C ATOM 1230 O LEU B 86 4.883 -7.695 -14.218 1.00 63.45 O ANISOU 1230 O LEU B 86 7729 7592 8787 -517 -363 585 O ATOM 1231 CB LEU B 86 6.679 -10.320 -15.189 1.00 59.15 C ANISOU 1231 CB LEU B 86 7361 6858 8253 -529 -721 601 C ATOM 1232 CG LEU B 86 6.571 -9.584 -16.537 1.00 62.46 C ANISOU 1232 CG LEU B 86 7614 7336 8783 -477 -707 552 C ATOM 1233 CD1 LEU B 86 7.502 -8.382 -16.607 1.00 61.67 C ANISOU 1233 CD1 LEU B 86 7478 7258 8696 -373 -709 477 C ATOM 1234 CD2 LEU B 86 6.864 -10.524 -17.686 1.00 64.09 C ANISOU 1234 CD2 LEU B 86 7814 7487 9048 -486 -810 539 C ATOM 1235 N ALA B 87 3.890 -9.675 -13.695 1.00 61.87 N ANISOU 1235 N ALA B 87 7634 7343 8530 -700 -360 706 N ATOM 1236 CA ALA B 87 2.498 -9.217 -13.686 1.00 62.24 C ANISOU 1236 CA ALA B 87 7532 7476 8643 -750 -190 735 C ATOM 1237 C ALA B 87 2.236 -8.187 -12.587 1.00 66.37 C ANISOU 1237 C ALA B 87 8084 8039 9094 -724 -17 706 C ATOM 1238 O ALA B 87 1.478 -7.248 -12.821 1.00 66.29 O ANISOU 1238 O ALA B 87 7911 8098 9179 -684 107 687 O ATOM 1239 CB ALA B 87 1.555 -10.397 -13.530 1.00 64.27 C ANISOU 1239 CB ALA B 87 7797 7719 8902 -896 -157 820 C ATOM 1240 N VAL B 88 2.864 -8.356 -11.400 1.00 63.01 N ANISOU 1240 N VAL B 88 7875 7563 8501 -745 -17 703 N ATOM 1241 CA VAL B 88 2.743 -7.427 -10.266 1.00 63.47 C ANISOU 1241 CA VAL B 88 8020 7645 8451 -732 141 661 C ATOM 1242 C VAL B 88 3.496 -6.123 -10.602 1.00 65.75 C ANISOU 1242 C VAL B 88 8258 7944 8781 -599 107 568 C ATOM 1243 O VAL B 88 2.940 -5.037 -10.422 1.00 65.73 O ANISOU 1243 O VAL B 88 8175 7984 8814 -554 266 522 O ATOM 1244 CB VAL B 88 3.182 -8.070 -8.917 1.00 68.54 C ANISOU 1244 CB VAL B 88 8942 8224 8875 -815 127 695 C ATOM 1245 CG1 VAL B 88 3.307 -7.031 -7.802 1.00 69.21 C ANISOU 1245 CG1 VAL B 88 9157 8321 8819 -795 257 630 C ATOM 1246 CG2 VAL B 88 2.217 -9.177 -8.500 1.00 69.91 C ANISOU 1246 CG2 VAL B 88 9165 8391 9007 -963 221 791 C ATOM 1247 N ALA B 89 4.732 -6.245 -11.142 1.00 60.38 N ANISOU 1247 N ALA B 89 7610 7217 8113 -538 -93 539 N ATOM 1248 CA ALA B 89 5.570 -5.119 -11.566 1.00 58.77 C ANISOU 1248 CA ALA B 89 7357 7014 7957 -431 -145 457 C ATOM 1249 C ALA B 89 4.901 -4.314 -12.687 1.00 61.31 C ANISOU 1249 C ALA B 89 7460 7390 8444 -370 -75 442 C ATOM 1250 O ALA B 89 4.994 -3.087 -12.685 1.00 60.69 O ANISOU 1250 O ALA B 89 7342 7321 8395 -299 -8 383 O ATOM 1251 CB ALA B 89 6.931 -5.619 -12.021 1.00 58.52 C ANISOU 1251 CB ALA B 89 7373 6928 7937 -393 -358 439 C ATOM 1252 N ASP B 90 4.209 -5.003 -13.624 1.00 57.14 N ANISOU 1252 N ASP B 90 6803 6888 8021 -403 -100 499 N ATOM 1253 CA ASP B 90 3.493 -4.368 -14.732 1.00 56.39 C ANISOU 1253 CA ASP B 90 6507 6842 8077 -358 -67 506 C ATOM 1254 C ASP B 90 2.218 -3.678 -14.256 1.00 61.78 C ANISOU 1254 C ASP B 90 7082 7575 8815 -356 128 519 C ATOM 1255 O ASP B 90 1.972 -2.541 -14.656 1.00 61.48 O ANISOU 1255 O ASP B 90 6936 7554 8870 -270 182 490 O ATOM 1256 CB ASP B 90 3.176 -5.374 -15.852 1.00 57.64 C ANISOU 1256 CB ASP B 90 6581 7006 8312 -410 -178 561 C ATOM 1257 CG ASP B 90 4.367 -5.810 -16.684 1.00 64.87 C ANISOU 1257 CG ASP B 90 7554 7874 9221 -382 -346 529 C ATOM 1258 OD1 ASP B 90 5.258 -4.970 -16.938 1.00 63.92 O ANISOU 1258 OD1 ASP B 90 7443 7741 9105 -302 -376 469 O ATOM 1259 OD2 ASP B 90 4.390 -6.980 -17.115 1.00 71.49 O ANISOU 1259 OD2 ASP B 90 8422 8682 10058 -444 -436 561 O ATOM 1260 N LEU B 91 1.419 -4.356 -13.395 1.00 59.52 N ANISOU 1260 N LEU B 91 6830 7307 8479 -449 243 563 N ATOM 1261 CA LEU B 91 0.165 -3.833 -12.838 1.00 60.81 C ANISOU 1261 CA LEU B 91 6883 7519 8704 -457 463 571 C ATOM 1262 C LEU B 91 0.391 -2.540 -12.054 1.00 65.26 C ANISOU 1262 C LEU B 91 7514 8066 9217 -370 600 487 C ATOM 1263 O LEU B 91 -0.359 -1.585 -12.246 1.00 65.48 O ANISOU 1263 O LEU B 91 7386 8118 9375 -294 726 467 O ATOM 1264 CB LEU B 91 -0.525 -4.892 -11.955 1.00 62.33 C ANISOU 1264 CB LEU B 91 7143 7722 8818 -595 569 629 C ATOM 1265 CG LEU B 91 -1.925 -4.565 -11.429 1.00 68.93 C ANISOU 1265 CG LEU B 91 7833 8617 9739 -626 820 644 C ATOM 1266 CD1 LEU B 91 -2.988 -4.835 -12.480 1.00 69.41 C ANISOU 1266 CD1 LEU B 91 7617 8736 10019 -649 792 709 C ATOM 1267 CD2 LEU B 91 -2.229 -5.366 -10.179 1.00 72.94 C ANISOU 1267 CD2 LEU B 91 8509 9115 10089 -763 962 674 C ATOM 1268 N LEU B 92 1.430 -2.512 -11.193 1.00 61.86 N ANISOU 1268 N LEU B 92 7317 7584 8605 -380 563 437 N ATOM 1269 CA LEU B 92 1.790 -1.347 -10.378 1.00 62.16 C ANISOU 1269 CA LEU B 92 7467 7591 8562 -318 670 346 C ATOM 1270 C LEU B 92 2.327 -0.195 -11.234 1.00 64.94 C ANISOU 1270 C LEU B 92 7730 7921 9024 -197 596 291 C ATOM 1271 O LEU B 92 2.089 0.966 -10.898 1.00 65.32 O ANISOU 1271 O LEU B 92 7771 7949 9098 -126 732 225 O ATOM 1272 CB LEU B 92 2.792 -1.721 -9.267 1.00 62.43 C ANISOU 1272 CB LEU B 92 7781 7574 8365 -380 604 317 C ATOM 1273 CG LEU B 92 2.304 -2.663 -8.152 1.00 68.55 C ANISOU 1273 CG LEU B 92 8714 8353 8980 -507 706 366 C ATOM 1274 CD1 LEU B 92 3.463 -3.135 -7.302 1.00 68.67 C ANISOU 1274 CD1 LEU B 92 9005 8308 8780 -560 554 360 C ATOM 1275 CD2 LEU B 92 1.244 -2.008 -7.272 1.00 73.02 C ANISOU 1275 CD2 LEU B 92 9286 8943 9514 -521 1003 326 C ATOM 1276 N LEU B 93 3.031 -0.520 -12.345 1.00 59.73 N ANISOU 1276 N LEU B 93 7012 7256 8427 -179 395 317 N ATOM 1277 CA LEU B 93 3.572 0.454 -13.299 1.00 58.33 C ANISOU 1277 CA LEU B 93 6757 7056 8349 -85 317 281 C ATOM 1278 C LEU B 93 2.437 1.110 -14.097 1.00 62.45 C ANISOU 1278 C LEU B 93 7067 7608 9053 -19 400 315 C ATOM 1279 O LEU B 93 2.427 2.332 -14.232 1.00 62.43 O ANISOU 1279 O LEU B 93 7033 7572 9117 70 458 271 O ATOM 1280 CB LEU B 93 4.604 -0.209 -14.240 1.00 56.83 C ANISOU 1280 CB LEU B 93 6574 6854 8163 -99 106 299 C ATOM 1281 CG LEU B 93 5.255 0.658 -15.332 1.00 60.32 C ANISOU 1281 CG LEU B 93 6951 7275 8693 -27 24 270 C ATOM 1282 CD1 LEU B 93 6.190 1.707 -14.739 1.00 60.44 C ANISOU 1282 CD1 LEU B 93 7076 7237 8651 10 37 183 C ATOM 1283 CD2 LEU B 93 6.019 -0.204 -16.313 1.00 61.55 C ANISOU 1283 CD2 LEU B 93 7096 7431 8861 -54 -141 292 C ATOM 1284 N LEU B 94 1.476 0.304 -14.600 1.00 59.10 N ANISOU 1284 N LEU B 94 6501 7239 8717 -65 395 396 N ATOM 1285 CA LEU B 94 0.314 0.792 -15.353 1.00 59.58 C ANISOU 1285 CA LEU B 94 6338 7334 8967 -10 444 445 C ATOM 1286 C LEU B 94 -0.633 1.593 -14.454 1.00 65.44 C ANISOU 1286 C LEU B 94 7017 8077 9769 44 678 412 C ATOM 1287 O LEU B 94 -1.327 2.478 -14.951 1.00 65.91 O ANISOU 1287 O LEU B 94 6914 8133 9996 140 726 424 O ATOM 1288 CB LEU B 94 -0.449 -0.361 -16.032 1.00 59.79 C ANISOU 1288 CB LEU B 94 6233 7418 9064 -96 364 536 C ATOM 1289 CG LEU B 94 0.271 -1.108 -17.157 1.00 62.99 C ANISOU 1289 CG LEU B 94 6672 7817 9444 -139 145 566 C ATOM 1290 CD1 LEU B 94 -0.192 -2.540 -17.227 1.00 63.68 C ANISOU 1290 CD1 LEU B 94 6744 7935 9515 -263 93 626 C ATOM 1291 CD2 LEU B 94 0.073 -0.435 -18.500 1.00 64.62 C ANISOU 1291 CD2 LEU B 94 6750 8028 9774 -73 41 598 C ATOM 1292 N ALA B 95 -0.635 1.303 -13.131 1.00 62.93 N ANISOU 1292 N ALA B 95 6842 7756 9311 -16 826 370 N ATOM 1293 CA ALA B 95 -1.453 1.982 -12.119 1.00 64.66 C ANISOU 1293 CA ALA B 95 7046 7970 9551 21 1087 319 C ATOM 1294 C ALA B 95 -1.082 3.463 -11.947 1.00 69.07 C ANISOU 1294 C ALA B 95 7660 8454 10129 146 1157 226 C ATOM 1295 O ALA B 95 -1.865 4.220 -11.369 1.00 70.76 O ANISOU 1295 O ALA B 95 7819 8650 10415 213 1377 178 O ATOM 1296 CB ALA B 95 -1.342 1.259 -10.785 1.00 66.24 C ANISOU 1296 CB ALA B 95 7449 8174 9544 -94 1204 295 C ATOM 1297 N THR B 96 0.103 3.874 -12.448 1.00 63.86 N ANISOU 1297 N THR B 96 7105 7743 9414 176 982 198 N ATOM 1298 CA THR B 96 0.584 5.256 -12.370 1.00 63.76 C ANISOU 1298 CA THR B 96 7162 7645 9416 277 1019 113 C ATOM 1299 C THR B 96 0.104 6.115 -13.558 1.00 67.25 C ANISOU 1299 C THR B 96 7408 8064 10081 395 974 156 C ATOM 1300 O THR B 96 0.164 7.341 -13.465 1.00 67.68 O ANISOU 1300 O THR B 96 7489 8035 10190 493 1049 95 O ATOM 1301 CB THR B 96 2.113 5.317 -12.181 1.00 70.47 C ANISOU 1301 CB THR B 96 8229 8449 10099 233 870 57 C ATOM 1302 OG1 THR B 96 2.769 4.868 -13.366 1.00 67.80 O ANISOU 1302 OG1 THR B 96 7828 8129 9803 218 652 117 O ATOM 1303 CG2 THR B 96 2.598 4.538 -10.962 1.00 69.48 C ANISOU 1303 CG2 THR B 96 8313 8334 9753 124 887 23 C ATOM 1304 N LEU B 97 -0.390 5.479 -14.653 1.00 62.60 N ANISOU 1304 N LEU B 97 6637 7536 9611 382 846 262 N ATOM 1305 CA LEU B 97 -0.898 6.160 -15.857 1.00 62.23 C ANISOU 1305 CA LEU B 97 6411 7473 9762 480 764 327 C ATOM 1306 C LEU B 97 -1.976 7.235 -15.574 1.00 67.72 C ANISOU 1306 C LEU B 97 6966 8123 10642 613 946 309 C ATOM 1307 O LEU B 97 -1.837 8.319 -16.145 1.00 67.19 O ANISOU 1307 O LEU B 97 6885 7974 10669 719 904 308 O ATOM 1308 CB LEU B 97 -1.389 5.171 -16.928 1.00 61.76 C ANISOU 1308 CB LEU B 97 6194 7493 9778 420 602 440 C ATOM 1309 CG LEU B 97 -0.307 4.496 -17.772 1.00 64.52 C ANISOU 1309 CG LEU B 97 6650 7853 10012 341 388 464 C ATOM 1310 CD1 LEU B 97 -0.774 3.161 -18.271 1.00 64.56 C ANISOU 1310 CD1 LEU B 97 6568 7937 10023 238 287 541 C ATOM 1311 CD2 LEU B 97 0.088 5.352 -18.957 1.00 66.41 C ANISOU 1311 CD2 LEU B 97 6877 8041 10315 409 257 492 C ATOM 1312 N PRO B 98 -3.004 7.030 -14.691 1.00 66.03 N ANISOU 1312 N PRO B 98 6657 7947 10486 616 1159 290 N ATOM 1313 CA PRO B 98 -3.972 8.118 -14.435 1.00 68.04 C ANISOU 1313 CA PRO B 98 6768 8144 10940 764 1348 260 C ATOM 1314 C PRO B 98 -3.358 9.375 -13.810 1.00 72.05 C ANISOU 1314 C PRO B 98 7465 8524 11386 853 1463 140 C ATOM 1315 O PRO B 98 -3.901 10.461 -14.006 1.00 73.21 O ANISOU 1315 O PRO B 98 7512 8588 11718 1002 1541 126 O ATOM 1316 CB PRO B 98 -5.000 7.475 -13.495 1.00 71.55 C ANISOU 1316 CB PRO B 98 7108 8662 11415 715 1577 248 C ATOM 1317 CG PRO B 98 -4.823 6.017 -13.660 1.00 74.65 C ANISOU 1317 CG PRO B 98 7516 9156 11689 548 1449 319 C ATOM 1318 CD PRO B 98 -3.365 5.829 -13.911 1.00 67.83 C ANISOU 1318 CD PRO B 98 6896 8261 10616 488 1252 298 C ATOM 1319 N LEU B 99 -2.231 9.235 -13.074 1.00 67.23 N ANISOU 1319 N LEU B 99 7128 7890 10526 763 1459 55 N ATOM 1320 CA LEU B 99 -1.520 10.357 -12.450 1.00 67.49 C ANISOU 1320 CA LEU B 99 7373 7800 10471 814 1542 -67 C ATOM 1321 C LEU B 99 -0.868 11.235 -13.517 1.00 70.13 C ANISOU 1321 C LEU B 99 7715 8047 10884 884 1362 -39 C ATOM 1322 O LEU B 99 -1.040 12.454 -13.480 1.00 71.02 O ANISOU 1322 O LEU B 99 7842 8040 11102 1004 1451 -91 O ATOM 1323 CB LEU B 99 -0.450 9.876 -11.449 1.00 66.91 C ANISOU 1323 CB LEU B 99 7580 7734 10111 679 1534 -150 C ATOM 1324 CG LEU B 99 -0.932 9.172 -10.186 1.00 73.42 C ANISOU 1324 CG LEU B 99 8485 8613 10797 596 1732 -195 C ATOM 1325 CD1 LEU B 99 0.124 8.213 -9.671 1.00 72.41 C ANISOU 1325 CD1 LEU B 99 8574 8528 10410 441 1598 -199 C ATOM 1326 CD2 LEU B 99 -1.322 10.173 -9.103 1.00 78.63 C ANISOU 1326 CD2 LEU B 99 9262 9182 11432 663 2008 -329 C ATOM 1327 N TRP B 100 -0.133 10.611 -14.470 1.00 64.11 N ANISOU 1327 N TRP B 100 6952 7337 10071 806 1122 41 N ATOM 1328 CA TRP B 100 0.555 11.302 -15.567 1.00 62.64 C ANISOU 1328 CA TRP B 100 6786 7080 9932 842 949 79 C ATOM 1329 C TRP B 100 -0.423 11.971 -16.531 1.00 67.58 C ANISOU 1329 C TRP B 100 7212 7666 10799 975 923 171 C ATOM 1330 O TRP B 100 -0.151 13.081 -16.991 1.00 67.68 O ANISOU 1330 O TRP B 100 7272 7560 10882 1055 890 168 O ATOM 1331 CB TRP B 100 1.524 10.365 -16.314 1.00 59.07 C ANISOU 1331 CB TRP B 100 6379 6702 9363 721 733 133 C ATOM 1332 CG TRP B 100 2.326 9.443 -15.437 1.00 59.03 C ANISOU 1332 CG TRP B 100 6523 6752 9154 597 726 73 C ATOM 1333 CD1 TRP B 100 2.409 8.086 -15.543 1.00 60.95 C ANISOU 1333 CD1 TRP B 100 6740 7098 9323 500 638 124 C ATOM 1334 CD2 TRP B 100 3.152 9.809 -14.318 1.00 58.98 C ANISOU 1334 CD2 TRP B 100 6726 6690 8994 557 793 -45 C ATOM 1335 NE1 TRP B 100 3.225 7.581 -14.557 1.00 59.96 N ANISOU 1335 NE1 TRP B 100 6788 6980 9014 412 643 55 N ATOM 1336 CE2 TRP B 100 3.692 8.616 -13.789 1.00 62.05 C ANISOU 1336 CE2 TRP B 100 7198 7155 9222 441 730 -48 C ATOM 1337 CE3 TRP B 100 3.483 11.031 -13.704 1.00 61.07 C ANISOU 1337 CE3 TRP B 100 7127 6838 9238 603 891 -148 C ATOM 1338 CZ2 TRP B 100 4.542 8.607 -12.676 1.00 61.49 C ANISOU 1338 CZ2 TRP B 100 7336 7057 8971 371 743 -142 C ATOM 1339 CZ3 TRP B 100 4.314 11.019 -12.595 1.00 62.56 C ANISOU 1339 CZ3 TRP B 100 7527 7002 9241 523 913 -252 C ATOM 1340 CH2 TRP B 100 4.844 9.821 -12.100 1.00 62.42 C ANISOU 1340 CH2 TRP B 100 7582 7070 9064 408 830 -243 C ATOM 1341 N ALA B 101 -1.574 11.316 -16.802 1.00 64.54 N ANISOU 1341 N ALA B 101 6604 7371 10547 994 932 256 N ATOM 1342 CA ALA B 101 -2.635 11.838 -17.667 1.00 65.62 C ANISOU 1342 CA ALA B 101 6517 7482 10933 1120 886 356 C ATOM 1343 C ALA B 101 -3.245 13.114 -17.070 1.00 71.44 C ANISOU 1343 C ALA B 101 7224 8092 11830 1286 1084 288 C ATOM 1344 O ALA B 101 -3.538 14.050 -17.812 1.00 71.99 O ANISOU 1344 O ALA B 101 7225 8062 12067 1411 1013 345 O ATOM 1345 CB ALA B 101 -3.710 10.784 -17.874 1.00 66.95 C ANISOU 1345 CB ALA B 101 6451 7782 11205 1082 866 443 C ATOM 1346 N THR B 102 -3.396 13.155 -15.728 1.00 68.84 N ANISOU 1346 N THR B 102 6969 7754 11435 1285 1332 163 N ATOM 1347 CA THR B 102 -3.908 14.308 -14.979 1.00 70.94 C ANISOU 1347 CA THR B 102 7244 7889 11821 1433 1566 64 C ATOM 1348 C THR B 102 -2.822 15.395 -14.942 1.00 74.46 C ANISOU 1348 C THR B 102 7945 8180 12168 1455 1533 -16 C ATOM 1349 O THR B 102 -3.135 16.574 -15.101 1.00 75.52 O ANISOU 1349 O THR B 102 8064 8165 12466 1605 1590 -33 O ATOM 1350 CB THR B 102 -4.375 13.872 -13.574 1.00 79.34 C ANISOU 1350 CB THR B 102 8337 9004 12804 1393 1848 -47 C ATOM 1351 OG1 THR B 102 -5.285 12.779 -13.700 1.00 79.56 O ANISOU 1351 OG1 THR B 102 8132 9181 12916 1341 1857 40 O ATOM 1352 CG2 THR B 102 -5.050 14.999 -12.798 1.00 80.21 C ANISOU 1352 CG2 THR B 102 8439 8983 13055 1554 2128 -160 C ATOM 1353 N TYR B 103 -1.546 14.981 -14.757 1.00 69.28 N ANISOU 1353 N TYR B 103 7512 7552 11259 1302 1432 -59 N ATOM 1354 CA TYR B 103 -0.360 15.843 -14.718 1.00 68.50 C ANISOU 1354 CA TYR B 103 7654 7328 11046 1276 1376 -134 C ATOM 1355 C TYR B 103 -0.160 16.564 -16.057 1.00 72.23 C ANISOU 1355 C TYR B 103 8081 7715 11649 1340 1192 -29 C ATOM 1356 O TYR B 103 0.214 17.735 -16.064 1.00 72.28 O ANISOU 1356 O TYR B 103 8215 7559 11691 1402 1218 -80 O ATOM 1357 CB TYR B 103 0.883 15.012 -14.331 1.00 67.55 C ANISOU 1357 CB TYR B 103 7716 7289 10661 1092 1277 -178 C ATOM 1358 CG TYR B 103 2.173 15.784 -14.136 1.00 68.58 C ANISOU 1358 CG TYR B 103 8084 7308 10665 1034 1221 -267 C ATOM 1359 CD1 TYR B 103 2.236 16.871 -13.266 1.00 72.20 C ANISOU 1359 CD1 TYR B 103 8704 7620 11109 1086 1382 -400 C ATOM 1360 CD2 TYR B 103 3.356 15.361 -14.733 1.00 67.32 C ANISOU 1360 CD2 TYR B 103 7993 7193 10395 913 1019 -232 C ATOM 1361 CE1 TYR B 103 3.428 17.562 -13.056 1.00 72.71 C ANISOU 1361 CE1 TYR B 103 8987 7581 11059 1012 1321 -485 C ATOM 1362 CE2 TYR B 103 4.556 16.038 -14.524 1.00 68.00 C ANISOU 1362 CE2 TYR B 103 8272 7184 10380 845 968 -315 C ATOM 1363 CZ TYR B 103 4.588 17.139 -13.685 1.00 77.42 C ANISOU 1363 CZ TYR B 103 9622 8231 11564 888 1110 -439 C ATOM 1364 OH TYR B 103 5.770 17.809 -13.482 1.00 78.31 O ANISOU 1364 OH TYR B 103 9922 8248 11584 803 1047 -521 O ATOM 1365 N TYR B 104 -0.453 15.874 -17.178 1.00 68.34 N ANISOU 1365 N TYR B 104 7423 7322 11222 1320 1010 117 N ATOM 1366 CA TYR B 104 -0.364 16.417 -18.535 1.00 68.20 C ANISOU 1366 CA TYR B 104 7367 7239 11308 1366 822 239 C ATOM 1367 C TYR B 104 -1.479 17.448 -18.762 1.00 75.18 C ANISOU 1367 C TYR B 104 8113 7998 12454 1565 884 284 C ATOM 1368 O TYR B 104 -1.206 18.534 -19.277 1.00 75.42 O ANISOU 1368 O TYR B 104 8232 7872 12552 1636 830 308 O ATOM 1369 CB TYR B 104 -0.448 15.279 -19.573 1.00 67.89 C ANISOU 1369 CB TYR B 104 7205 7349 11241 1277 621 370 C ATOM 1370 CG TYR B 104 -0.106 15.692 -20.989 1.00 69.18 C ANISOU 1370 CG TYR B 104 7394 7460 11432 1275 413 489 C ATOM 1371 CD1 TYR B 104 1.196 15.592 -21.470 1.00 69.46 C ANISOU 1371 CD1 TYR B 104 7605 7493 11294 1148 309 478 C ATOM 1372 CD2 TYR B 104 -1.091 16.141 -21.863 1.00 71.50 C ANISOU 1372 CD2 TYR B 104 7533 7709 11924 1394 317 618 C ATOM 1373 CE1 TYR B 104 1.515 15.956 -22.777 1.00 70.21 C ANISOU 1373 CE1 TYR B 104 7743 7541 11393 1130 142 587 C ATOM 1374 CE2 TYR B 104 -0.783 16.520 -23.168 1.00 72.34 C ANISOU 1374 CE2 TYR B 104 7696 7762 12028 1381 119 737 C ATOM 1375 CZ TYR B 104 0.521 16.423 -23.623 1.00 78.58 C ANISOU 1375 CZ TYR B 104 8683 8551 12623 1243 44 719 C ATOM 1376 OH TYR B 104 0.825 16.788 -24.913 1.00 80.38 O ANISOU 1376 OH TYR B 104 8985 8725 12829 1215 -128 836 O ATOM 1377 N SER B 105 -2.728 17.103 -18.362 1.00 73.83 N ANISOU 1377 N SER B 105 7721 7890 12442 1653 1002 296 N ATOM 1378 CA SER B 105 -3.936 17.929 -18.489 1.00 76.56 C ANISOU 1378 CA SER B 105 7874 8135 13079 1858 1076 338 C ATOM 1379 C SER B 105 -3.847 19.275 -17.769 1.00 82.80 C ANISOU 1379 C SER B 105 8806 8720 13936 1988 1265 215 C ATOM 1380 O SER B 105 -4.428 20.253 -18.244 1.00 84.38 O ANISOU 1380 O SER B 105 8925 8774 14363 2161 1245 271 O ATOM 1381 CB SER B 105 -5.158 17.166 -17.990 1.00 81.50 C ANISOU 1381 CB SER B 105 8237 8888 13842 1894 1208 345 C ATOM 1382 OG SER B 105 -5.438 16.044 -18.809 1.00 90.30 O ANISOU 1382 OG SER B 105 9193 10165 14951 1795 1010 476 O ATOM 1383 N TYR B 106 -3.133 19.324 -16.627 1.00 79.31 N ANISOU 1383 N TYR B 106 8582 8256 13296 1906 1439 49 N ATOM 1384 CA TYR B 106 -2.973 20.546 -15.841 1.00 81.10 C ANISOU 1384 CA TYR B 106 8983 8284 13547 2003 1629 -93 C ATOM 1385 C TYR B 106 -1.728 21.367 -16.240 1.00 84.75 C ANISOU 1385 C TYR B 106 9707 8603 13890 1940 1500 -111 C ATOM 1386 O TYR B 106 -1.282 22.216 -15.466 1.00 85.48 O ANISOU 1386 O TYR B 106 10009 8546 13924 1953 1640 -254 O ATOM 1387 CB TYR B 106 -3.012 20.237 -14.332 1.00 82.90 C ANISOU 1387 CB TYR B 106 9315 8552 13631 1951 1900 -270 C ATOM 1388 CG TYR B 106 -4.416 20.024 -13.807 1.00 87.11 C ANISOU 1388 CG TYR B 106 9605 9131 14361 2078 2125 -286 C ATOM 1389 CD1 TYR B 106 -5.243 21.104 -13.510 1.00 92.09 C ANISOU 1389 CD1 TYR B 106 10165 9592 15231 2289 2323 -349 C ATOM 1390 CD2 TYR B 106 -4.920 18.743 -13.609 1.00 87.35 C ANISOU 1390 CD2 TYR B 106 9470 9368 14351 1986 2150 -241 C ATOM 1391 CE1 TYR B 106 -6.541 20.914 -13.038 1.00 95.40 C ANISOU 1391 CE1 TYR B 106 10331 10057 15859 2410 2549 -369 C ATOM 1392 CE2 TYR B 106 -6.215 18.539 -13.134 1.00 90.68 C ANISOU 1392 CE2 TYR B 106 9649 9838 14968 2087 2371 -255 C ATOM 1393 CZ TYR B 106 -7.022 19.628 -12.849 1.00101.58 C ANISOU 1393 CZ TYR B 106 10941 11059 16598 2301 2576 -321 C ATOM 1394 OH TYR B 106 -8.299 19.434 -12.378 1.00105.84 O ANISOU 1394 OH TYR B 106 11214 11647 17352 2404 2815 -341 O ATOM 1395 N ARG B 107 -1.217 21.154 -17.480 1.00 80.01 N ANISOU 1395 N ARG B 107 9095 8042 13265 1869 1240 33 N ATOM 1396 CA ARG B 107 -0.058 21.838 -18.080 1.00 78.98 C ANISOU 1396 CA ARG B 107 9178 7795 13037 1790 1102 48 C ATOM 1397 C ARG B 107 1.221 21.679 -17.230 1.00 81.38 C ANISOU 1397 C ARG B 107 9722 8116 13084 1615 1150 -100 C ATOM 1398 O ARG B 107 1.978 22.635 -17.045 1.00 81.66 O ANISOU 1398 O ARG B 107 9962 7989 13075 1589 1170 -176 O ATOM 1399 CB ARG B 107 -0.375 23.323 -18.404 1.00 81.94 C ANISOU 1399 CB ARG B 107 9609 7917 13607 1958 1125 66 C ATOM 1400 CG ARG B 107 -1.311 23.556 -19.601 1.00 94.29 C ANISOU 1400 CG ARG B 107 10975 9446 15405 2102 971 258 C ATOM 1401 CD ARG B 107 -2.797 23.471 -19.264 1.00108.90 C ANISOU 1401 CD ARG B 107 12555 11316 17505 2294 1092 273 C ATOM 1402 NE ARG B 107 -3.223 24.487 -18.298 1.00122.52 N ANISOU 1402 NE ARG B 107 14334 12854 19365 2455 1340 131 N ATOM 1403 CZ ARG B 107 -4.404 24.496 -17.686 1.00140.45 C ANISOU 1403 CZ ARG B 107 16397 15126 21842 2618 1531 85 C ATOM 1404 NH1 ARG B 107 -5.293 23.540 -17.928 1.00128.26 N ANISOU 1404 NH1 ARG B 107 14564 13768 20401 2634 1492 177 N ATOM 1405 NH2 ARG B 107 -4.703 25.457 -16.823 1.00130.41 N ANISOU 1405 NH2 ARG B 107 15205 13666 20678 2761 1773 -60 N ATOM 1406 N TYR B 108 1.447 20.446 -16.732 1.00 76.34 N ANISOU 1406 N TYR B 108 9052 7670 12284 1490 1154 -132 N ATOM 1407 CA TYR B 108 2.566 20.012 -15.883 1.00 74.90 C ANISOU 1407 CA TYR B 108 9057 7543 11859 1321 1170 -254 C ATOM 1408 C TYR B 108 2.567 20.713 -14.507 1.00 81.00 C ANISOU 1408 C TYR B 108 10006 8197 12573 1348 1385 -435 C ATOM 1409 O TYR B 108 3.607 21.184 -14.041 1.00 80.25 O ANISOU 1409 O TYR B 108 10130 8021 12340 1246 1371 -539 O ATOM 1410 CB TYR B 108 3.930 20.110 -16.604 1.00 74.21 C ANISOU 1410 CB TYR B 108 9094 7441 11661 1180 984 -224 C ATOM 1411 CG TYR B 108 4.021 19.255 -17.850 1.00 73.95 C ANISOU 1411 CG TYR B 108 8923 7541 11634 1127 795 -70 C ATOM 1412 CD1 TYR B 108 4.303 17.895 -17.768 1.00 74.17 C ANISOU 1412 CD1 TYR B 108 8890 7756 11536 1016 730 -55 C ATOM 1413 CD2 TYR B 108 3.837 19.808 -19.113 1.00 74.97 C ANISOU 1413 CD2 TYR B 108 9004 7596 11884 1184 680 61 C ATOM 1414 CE1 TYR B 108 4.388 17.103 -18.912 1.00 73.51 C ANISOU 1414 CE1 TYR B 108 8699 7781 11449 965 568 71 C ATOM 1415 CE2 TYR B 108 3.922 19.027 -20.264 1.00 74.51 C ANISOU 1415 CE2 TYR B 108 8849 7655 11805 1123 512 194 C ATOM 1416 CZ TYR B 108 4.197 17.674 -20.159 1.00 79.91 C ANISOU 1416 CZ TYR B 108 9473 8524 12365 1015 463 191 C ATOM 1417 OH TYR B 108 4.285 16.901 -21.291 1.00 79.28 O ANISOU 1417 OH TYR B 108 9317 8547 12258 953 308 306 O ATOM 1418 N ASP B 109 1.390 20.741 -13.846 1.00 79.87 N ANISOU 1418 N ASP B 109 9764 8049 12533 1475 1588 -478 N ATOM 1419 CA ASP B 109 1.214 21.310 -12.509 1.00 81.71 C ANISOU 1419 CA ASP B 109 10162 8179 12705 1507 1831 -658 C ATOM 1420 C ASP B 109 1.016 20.174 -11.508 1.00 85.31 C ANISOU 1420 C ASP B 109 10621 8804 12989 1413 1940 -715 C ATOM 1421 O ASP B 109 -0.066 19.582 -11.443 1.00 85.46 O ANISOU 1421 O ASP B 109 10437 8921 13113 1484 2048 -666 O ATOM 1422 CB ASP B 109 0.030 22.295 -12.465 1.00 86.41 C ANISOU 1422 CB ASP B 109 10658 8618 13556 1732 2021 -680 C ATOM 1423 CG ASP B 109 0.017 23.214 -11.256 1.00 99.22 C ANISOU 1423 CG ASP B 109 12505 10068 15125 1776 2268 -881 C ATOM 1424 OD1 ASP B 109 0.992 23.981 -11.079 1.00 99.34 O ANISOU 1424 OD1 ASP B 109 12771 9944 15032 1703 2218 -967 O ATOM 1425 OD2 ASP B 109 -0.991 23.207 -10.517 1.00107.87 O ANISOU 1425 OD2 ASP B 109 13526 11161 16297 1884 2519 -956 O ATOM 1426 N TRP B 110 2.081 19.844 -10.759 1.00 81.22 N ANISOU 1426 N TRP B 110 10330 8319 12210 1243 1895 -808 N ATOM 1427 CA TRP B 110 2.068 18.786 -9.753 1.00 81.03 C ANISOU 1427 CA TRP B 110 10368 8437 11982 1130 1970 -859 C ATOM 1428 C TRP B 110 1.295 19.274 -8.526 1.00 88.59 C ANISOU 1428 C TRP B 110 11435 9312 12911 1199 2281 -1008 C ATOM 1429 O TRP B 110 1.758 20.170 -7.813 1.00 89.49 O ANISOU 1429 O TRP B 110 11797 9278 12926 1183 2366 -1156 O ATOM 1430 CB TRP B 110 3.501 18.345 -9.401 1.00 78.02 C ANISOU 1430 CB TRP B 110 10195 8102 11348 936 1788 -899 C ATOM 1431 CG TRP B 110 3.573 17.103 -8.562 1.00 78.41 C ANISOU 1431 CG TRP B 110 10299 8303 11189 813 1798 -908 C ATOM 1432 CD1 TRP B 110 3.695 17.038 -7.207 1.00 82.70 C ANISOU 1432 CD1 TRP B 110 11077 8833 11514 733 1930 -1038 C ATOM 1433 CD2 TRP B 110 3.517 15.746 -9.026 1.00 76.42 C ANISOU 1433 CD2 TRP B 110 9888 8229 10920 750 1668 -778 C ATOM 1434 NE1 TRP B 110 3.744 15.726 -6.797 1.00 81.27 N ANISOU 1434 NE1 TRP B 110 10895 8807 11178 624 1881 -986 N ATOM 1435 CE2 TRP B 110 3.624 14.911 -7.892 1.00 80.68 C ANISOU 1435 CE2 TRP B 110 10575 8847 11232 636 1725 -830 C ATOM 1436 CE3 TRP B 110 3.402 15.152 -10.294 1.00 75.88 C ANISOU 1436 CE3 TRP B 110 9588 8250 10993 772 1505 -625 C ATOM 1437 CZ2 TRP B 110 3.606 13.514 -7.985 1.00 78.65 C ANISOU 1437 CZ2 TRP B 110 10233 8746 10906 552 1627 -729 C ATOM 1438 CZ3 TRP B 110 3.383 13.768 -10.385 1.00 76.02 C ANISOU 1438 CZ3 TRP B 110 9521 8424 10938 687 1414 -540 C ATOM 1439 CH2 TRP B 110 3.486 12.965 -9.242 1.00 77.04 C ANISOU 1439 CH2 TRP B 110 9793 8619 10859 581 1474 -589 C ATOM 1440 N LEU B 111 0.085 18.719 -8.327 1.00 86.88 N ANISOU 1440 N LEU B 111 11029 9187 12796 1274 2458 -973 N ATOM 1441 CA LEU B 111 -0.815 19.074 -7.227 1.00 89.89 C ANISOU 1441 CA LEU B 111 11467 9509 13177 1349 2797 -1108 C ATOM 1442 C LEU B 111 -0.868 17.970 -6.154 1.00 94.47 C ANISOU 1442 C LEU B 111 12157 10232 13504 1199 2906 -1149 C ATOM 1443 O LEU B 111 -1.947 17.630 -5.656 1.00 95.99 O ANISOU 1443 O LEU B 111 12235 10480 13757 1247 3156 -1165 O ATOM 1444 CB LEU B 111 -2.223 19.407 -7.770 1.00 91.72 C ANISOU 1444 CB LEU B 111 11381 9716 13751 1560 2951 -1045 C ATOM 1445 CG LEU B 111 -2.353 20.685 -8.604 1.00 97.37 C ANISOU 1445 CG LEU B 111 12028 10245 14725 1738 2901 -1025 C ATOM 1446 CD1 LEU B 111 -3.410 20.527 -9.676 1.00 97.83 C ANISOU 1446 CD1 LEU B 111 11710 10354 15107 1890 2844 -860 C ATOM 1447 CD2 LEU B 111 -2.653 21.896 -7.729 1.00102.91 C ANISOU 1447 CD2 LEU B 111 12905 10736 15461 1856 3183 -1212 C ATOM 1448 N PHE B 112 0.312 17.422 -5.793 1.00 89.46 N ANISOU 1448 N PHE B 112 11748 9652 12592 1014 2718 -1162 N ATOM 1449 CA PHE B 112 0.446 16.363 -4.787 1.00 89.43 C ANISOU 1449 CA PHE B 112 11896 9768 12315 854 2767 -1185 C ATOM 1450 C PHE B 112 1.540 16.650 -3.743 1.00 93.72 C ANISOU 1450 C PHE B 112 12827 10238 12543 711 2722 -1324 C ATOM 1451 O PHE B 112 1.633 15.932 -2.743 1.00 93.98 O ANISOU 1451 O PHE B 112 13046 10341 12322 580 2783 -1362 O ATOM 1452 CB PHE B 112 0.660 14.988 -5.451 1.00 88.80 C ANISOU 1452 CB PHE B 112 11650 9868 12224 761 2536 -1015 C ATOM 1453 CG PHE B 112 -0.359 14.614 -6.502 1.00 90.00 C ANISOU 1453 CG PHE B 112 11435 10100 12663 872 2538 -873 C ATOM 1454 CD1 PHE B 112 -1.607 14.120 -6.140 1.00 94.91 C ANISOU 1454 CD1 PHE B 112 11896 10797 13369 907 2775 -854 C ATOM 1455 CD2 PHE B 112 -0.065 14.744 -7.854 1.00 90.44 C ANISOU 1455 CD2 PHE B 112 11309 10156 12897 927 2298 -757 C ATOM 1456 CE1 PHE B 112 -2.548 13.774 -7.114 1.00 95.72 C ANISOU 1456 CE1 PHE B 112 11647 10974 13747 998 2750 -721 C ATOM 1457 CE2 PHE B 112 -1.006 14.394 -8.827 1.00 93.12 C ANISOU 1457 CE2 PHE B 112 11328 10568 13486 1018 2273 -624 C ATOM 1458 CZ PHE B 112 -2.240 13.911 -8.450 1.00 92.91 C ANISOU 1458 CZ PHE B 112 11131 10616 13555 1053 2487 -606 C ATOM 1459 N GLY B 113 2.339 17.691 -3.981 1.00 90.12 N ANISOU 1459 N GLY B 113 12495 9640 12106 727 2610 -1394 N ATOM 1460 CA GLY B 113 3.415 18.108 -3.086 1.00 90.69 C ANISOU 1460 CA GLY B 113 12921 9627 11910 590 2536 -1530 C ATOM 1461 C GLY B 113 4.796 17.598 -3.463 1.00 92.32 C ANISOU 1461 C GLY B 113 13173 9896 12007 444 2177 -1459 C ATOM 1462 O GLY B 113 4.912 16.685 -4.288 1.00 89.52 O ANISOU 1462 O GLY B 113 12601 9674 11737 433 2003 -1306 O ATOM 1463 N PRO B 114 5.879 18.155 -2.858 1.00 89.80 N ANISOU 1463 N PRO B 114 13134 9483 11503 326 2058 -1574 N ATOM 1464 CA PRO B 114 7.238 17.689 -3.198 1.00 87.69 C ANISOU 1464 CA PRO B 114 12883 9276 11160 190 1715 -1512 C ATOM 1465 C PRO B 114 7.571 16.294 -2.673 1.00 90.68 C ANISOU 1465 C PRO B 114 13308 9811 11334 62 1582 -1441 C ATOM 1466 O PRO B 114 8.459 15.637 -3.221 1.00 88.33 O ANISOU 1466 O PRO B 114 12914 9595 11051 -6 1312 -1345 O ATOM 1467 CB PRO B 114 8.156 18.757 -2.584 1.00 90.94 C ANISOU 1467 CB PRO B 114 13580 9530 11445 99 1652 -1668 C ATOM 1468 CG PRO B 114 7.253 19.871 -2.135 1.00 97.91 C ANISOU 1468 CG PRO B 114 14578 10251 12372 213 1963 -1805 C ATOM 1469 CD PRO B 114 5.931 19.239 -1.860 1.00 94.17 C ANISOU 1469 CD PRO B 114 13995 9866 11921 308 2224 -1770 C ATOM 1470 N VAL B 115 6.863 15.847 -1.616 1.00 88.69 N ANISOU 1470 N VAL B 115 13209 9593 10895 31 1780 -1487 N ATOM 1471 CA VAL B 115 7.044 14.528 -0.999 1.00 88.11 C ANISOU 1471 CA VAL B 115 13219 9650 10608 -92 1683 -1416 C ATOM 1472 C VAL B 115 6.554 13.438 -1.968 1.00 89.55 C ANISOU 1472 C VAL B 115 13081 9975 10971 -33 1630 -1238 C ATOM 1473 O VAL B 115 7.301 12.501 -2.247 1.00 87.48 O ANISOU 1473 O VAL B 115 12770 9799 10667 -110 1376 -1138 O ATOM 1474 CB VAL B 115 6.378 14.426 0.405 1.00 94.74 C ANISOU 1474 CB VAL B 115 14341 10473 11182 -155 1939 -1517 C ATOM 1475 CG1 VAL B 115 6.671 13.079 1.065 1.00 94.34 C ANISOU 1475 CG1 VAL B 115 14417 10540 10888 -298 1807 -1432 C ATOM 1476 CG2 VAL B 115 6.823 15.571 1.316 1.00 96.94 C ANISOU 1476 CG2 VAL B 115 14956 10596 11280 -212 2000 -1710 C ATOM 1477 N MET B 116 5.327 13.593 -2.514 1.00 86.02 N ANISOU 1477 N MET B 116 12406 9540 10736 106 1858 -1201 N ATOM 1478 CA MET B 116 4.734 12.641 -3.459 1.00 83.94 C ANISOU 1478 CA MET B 116 11837 9402 10654 159 1820 -1040 C ATOM 1479 C MET B 116 5.385 12.681 -4.850 1.00 83.82 C ANISOU 1479 C MET B 116 11603 9402 10842 204 1570 -944 C ATOM 1480 O MET B 116 5.200 11.745 -5.629 1.00 81.86 O ANISOU 1480 O MET B 116 11149 9260 10694 210 1468 -812 O ATOM 1481 CB MET B 116 3.213 12.800 -3.533 1.00 87.86 C ANISOU 1481 CB MET B 116 12156 9909 11316 281 2129 -1034 C ATOM 1482 CG MET B 116 2.486 11.832 -2.631 1.00 93.23 C ANISOU 1482 CG MET B 116 12907 10679 11839 201 2305 -1016 C ATOM 1483 SD MET B 116 0.708 12.137 -2.563 1.00100.19 S ANISOU 1483 SD MET B 116 13574 11564 12928 337 2710 -1036 S ATOM 1484 CE MET B 116 0.150 10.584 -1.915 1.00 97.48 C ANISOU 1484 CE MET B 116 13250 11369 12421 195 2794 -944 C ATOM 1485 N CYS B 117 6.175 13.736 -5.144 1.00 78.99 N ANISOU 1485 N CYS B 117 11055 8680 10277 219 1474 -1014 N ATOM 1486 CA CYS B 117 6.947 13.883 -6.384 1.00 76.16 C ANISOU 1486 CA CYS B 117 10536 8321 10078 236 1250 -939 C ATOM 1487 C CYS B 117 8.085 12.849 -6.338 1.00 78.52 C ANISOU 1487 C CYS B 117 10877 8710 10248 106 985 -886 C ATOM 1488 O CYS B 117 8.416 12.248 -7.362 1.00 76.11 O ANISOU 1488 O CYS B 117 10384 8476 10060 113 828 -779 O ATOM 1489 CB CYS B 117 7.476 15.311 -6.515 1.00 76.83 C ANISOU 1489 CB CYS B 117 10719 8251 10223 263 1248 -1039 C ATOM 1490 SG CYS B 117 8.705 15.558 -7.830 1.00 78.39 S ANISOU 1490 SG CYS B 117 10790 8435 10558 232 975 -969 S ATOM 1491 N LYS B 118 8.637 12.615 -5.125 1.00 76.20 N ANISOU 1491 N LYS B 118 10836 8408 9711 -11 941 -960 N ATOM 1492 CA LYS B 118 9.695 11.643 -4.839 1.00 75.05 C ANISOU 1492 CA LYS B 118 10758 8330 9426 -131 688 -918 C ATOM 1493 C LYS B 118 9.120 10.227 -4.743 1.00 77.89 C ANISOU 1493 C LYS B 118 11052 8808 9736 -146 696 -806 C ATOM 1494 O LYS B 118 9.740 9.295 -5.252 1.00 75.87 O ANISOU 1494 O LYS B 118 10693 8622 9512 -178 491 -714 O ATOM 1495 CB LYS B 118 10.419 11.988 -3.523 1.00 79.29 C ANISOU 1495 CB LYS B 118 11613 8801 9711 -251 625 -1036 C ATOM 1496 CG LYS B 118 11.260 13.249 -3.576 1.00 92.27 C ANISOU 1496 CG LYS B 118 13341 10327 11390 -277 551 -1145 C ATOM 1497 CD LYS B 118 12.090 13.431 -2.313 1.00103.19 C ANISOU 1497 CD LYS B 118 15035 11657 12515 -421 428 -1250 C ATOM 1498 CE LYS B 118 13.001 14.635 -2.385 1.00113.36 C ANISOU 1498 CE LYS B 118 16399 12827 13845 -470 327 -1358 C ATOM 1499 NZ LYS B 118 14.154 14.417 -3.301 1.00119.63 N ANISOU 1499 NZ LYS B 118 16993 13661 14801 -503 62 -1289 N ATOM 1500 N VAL B 119 7.949 10.069 -4.076 1.00 75.52 N ANISOU 1500 N VAL B 119 10812 8523 9359 -129 943 -818 N ATOM 1501 CA VAL B 119 7.271 8.782 -3.863 1.00 75.07 C ANISOU 1501 CA VAL B 119 10714 8566 9243 -162 990 -717 C ATOM 1502 C VAL B 119 6.801 8.170 -5.190 1.00 76.13 C ANISOU 1502 C VAL B 119 10533 8778 9616 -85 951 -590 C ATOM 1503 O VAL B 119 7.274 7.088 -5.540 1.00 74.23 O ANISOU 1503 O VAL B 119 10236 8601 9367 -133 764 -497 O ATOM 1504 CB VAL B 119 6.137 8.860 -2.798 1.00 81.45 C ANISOU 1504 CB VAL B 119 11666 9366 9916 -176 1297 -773 C ATOM 1505 CG1 VAL B 119 5.380 7.536 -2.685 1.00 81.24 C ANISOU 1505 CG1 VAL B 119 11571 9441 9855 -221 1359 -657 C ATOM 1506 CG2 VAL B 119 6.685 9.275 -1.434 1.00 83.38 C ANISOU 1506 CG2 VAL B 119 12274 9539 9869 -282 1308 -894 C ATOM 1507 N PHE B 120 5.893 8.858 -5.925 1.00 72.20 N ANISOU 1507 N PHE B 120 9840 8264 9328 33 1114 -588 N ATOM 1508 CA PHE B 120 5.364 8.387 -7.214 1.00 70.30 C ANISOU 1508 CA PHE B 120 9311 8091 9309 103 1071 -470 C ATOM 1509 C PHE B 120 6.444 8.246 -8.288 1.00 71.51 C ANISOU 1509 C PHE B 120 9371 8251 9548 100 812 -421 C ATOM 1510 O PHE B 120 6.368 7.329 -9.107 1.00 69.95 O ANISOU 1510 O PHE B 120 9019 8127 9431 96 707 -319 O ATOM 1511 CB PHE B 120 4.205 9.267 -7.720 1.00 72.88 C ANISOU 1511 CB PHE B 120 9462 8386 9844 235 1276 -478 C ATOM 1512 CG PHE B 120 2.930 9.219 -6.907 1.00 76.53 C ANISOU 1512 CG PHE B 120 9923 8864 10290 255 1560 -505 C ATOM 1513 CD1 PHE B 120 2.301 8.008 -6.636 1.00 79.87 C ANISOU 1513 CD1 PHE B 120 10297 9387 10664 184 1610 -426 C ATOM 1514 CD2 PHE B 120 2.323 10.389 -6.468 1.00 80.68 C ANISOU 1514 CD2 PHE B 120 10484 9299 10872 346 1792 -609 C ATOM 1515 CE1 PHE B 120 1.116 7.967 -5.894 1.00 82.98 C ANISOU 1515 CE1 PHE B 120 10675 9800 11055 191 1898 -452 C ATOM 1516 CE2 PHE B 120 1.132 10.348 -5.735 1.00 85.67 C ANISOU 1516 CE2 PHE B 120 11095 9947 11509 370 2085 -643 C ATOM 1517 CZ PHE B 120 0.538 9.137 -5.451 1.00 83.97 C ANISOU 1517 CZ PHE B 120 10824 9843 11240 287 2141 -563 C ATOM 1518 N GLY B 121 7.432 9.143 -8.260 1.00 67.22 N ANISOU 1518 N GLY B 121 8927 7629 8984 92 722 -500 N ATOM 1519 CA GLY B 121 8.564 9.142 -9.179 1.00 65.09 C ANISOU 1519 CA GLY B 121 8584 7358 8791 76 503 -474 C ATOM 1520 C GLY B 121 9.425 7.904 -9.033 1.00 67.59 C ANISOU 1520 C GLY B 121 8931 7738 9011 -11 303 -426 C ATOM 1521 O GLY B 121 9.778 7.277 -10.035 1.00 65.69 O ANISOU 1521 O GLY B 121 8542 7545 8873 -2 178 -352 O ATOM 1522 N SER B 122 9.749 7.533 -7.775 1.00 64.93 N ANISOU 1522 N SER B 122 8802 7395 8472 -93 274 -467 N ATOM 1523 CA SER B 122 10.554 6.351 -7.449 1.00 64.19 C ANISOU 1523 CA SER B 122 8768 7345 8278 -171 73 -418 C ATOM 1524 C SER B 122 9.778 5.062 -7.684 1.00 67.21 C ANISOU 1524 C SER B 122 9063 7803 8672 -170 101 -309 C ATOM 1525 O SER B 122 10.356 4.101 -8.185 1.00 65.50 O ANISOU 1525 O SER B 122 8774 7620 8495 -185 -69 -243 O ATOM 1526 CB SER B 122 11.045 6.409 -6.008 1.00 69.27 C ANISOU 1526 CB SER B 122 9685 7949 8687 -263 24 -486 C ATOM 1527 OG SER B 122 11.802 7.586 -5.791 1.00 78.64 O ANISOU 1527 OG SER B 122 10957 9059 9863 -281 -21 -592 O ATOM 1528 N PHE B 123 8.470 5.050 -7.333 1.00 64.82 N ANISOU 1528 N PHE B 123 8761 7520 8347 -154 323 -295 N ATOM 1529 CA PHE B 123 7.551 3.917 -7.508 1.00 64.47 C ANISOU 1529 CA PHE B 123 8628 7544 8323 -168 385 -195 C ATOM 1530 C PHE B 123 7.438 3.545 -8.989 1.00 67.22 C ANISOU 1530 C PHE B 123 8728 7934 8879 -111 305 -119 C ATOM 1531 O PHE B 123 7.353 2.361 -9.320 1.00 66.20 O ANISOU 1531 O PHE B 123 8545 7848 8761 -145 222 -35 O ATOM 1532 CB PHE B 123 6.167 4.258 -6.922 1.00 67.65 C ANISOU 1532 CB PHE B 123 9041 7957 8707 -155 668 -213 C ATOM 1533 CG PHE B 123 5.148 3.144 -6.934 1.00 69.35 C ANISOU 1533 CG PHE B 123 9173 8240 8936 -194 758 -116 C ATOM 1534 CD1 PHE B 123 5.154 2.162 -5.949 1.00 73.41 C ANISOU 1534 CD1 PHE B 123 9873 8767 9253 -304 753 -79 C ATOM 1535 CD2 PHE B 123 4.150 3.103 -7.901 1.00 70.81 C ANISOU 1535 CD2 PHE B 123 9104 8472 9329 -132 845 -58 C ATOM 1536 CE1 PHE B 123 4.201 1.139 -5.953 1.00 74.67 C ANISOU 1536 CE1 PHE B 123 9961 8980 9429 -358 845 12 C ATOM 1537 CE2 PHE B 123 3.198 2.080 -7.903 1.00 74.04 C ANISOU 1537 CE2 PHE B 123 9428 8943 9761 -186 923 29 C ATOM 1538 CZ PHE B 123 3.227 1.108 -6.927 1.00 73.06 C ANISOU 1538 CZ PHE B 123 9488 8827 9445 -302 933 61 C ATOM 1539 N LEU B 124 7.465 4.563 -9.871 1.00 63.54 N ANISOU 1539 N LEU B 124 8135 7444 8564 -31 326 -148 N ATOM 1540 CA LEU B 124 7.422 4.411 -11.323 1.00 62.05 C ANISOU 1540 CA LEU B 124 7742 7284 8551 18 249 -85 C ATOM 1541 C LEU B 124 8.709 3.725 -11.814 1.00 64.59 C ANISOU 1541 C LEU B 124 8066 7609 8865 -18 29 -71 C ATOM 1542 O LEU B 124 8.619 2.712 -12.504 1.00 63.45 O ANISOU 1542 O LEU B 124 7833 7507 8770 -30 -47 0 O ATOM 1543 CB LEU B 124 7.238 5.795 -11.985 1.00 62.12 C ANISOU 1543 CB LEU B 124 7668 7244 8691 104 321 -123 C ATOM 1544 CG LEU B 124 7.359 5.883 -13.508 1.00 65.51 C ANISOU 1544 CG LEU B 124 7931 7686 9275 147 230 -65 C ATOM 1545 CD1 LEU B 124 6.052 5.516 -14.187 1.00 65.84 C ANISOU 1545 CD1 LEU B 124 7805 7780 9431 186 297 22 C ATOM 1546 CD2 LEU B 124 7.789 7.270 -13.924 1.00 67.84 C ANISOU 1546 CD2 LEU B 124 8232 7903 9641 198 243 -117 C ATOM 1547 N THR B 125 9.889 4.262 -11.423 1.00 60.92 N ANISOU 1547 N THR B 125 7704 7096 8347 -38 -68 -143 N ATOM 1548 CA THR B 125 11.218 3.761 -11.795 1.00 59.94 C ANISOU 1548 CA THR B 125 7565 6968 8241 -65 -266 -146 C ATOM 1549 C THR B 125 11.471 2.343 -11.254 1.00 64.34 C ANISOU 1549 C THR B 125 8190 7548 8708 -114 -381 -95 C ATOM 1550 O THR B 125 12.024 1.511 -11.979 1.00 63.37 O ANISOU 1550 O THR B 125 7982 7439 8658 -108 -502 -58 O ATOM 1551 CB THR B 125 12.304 4.772 -11.387 1.00 68.24 C ANISOU 1551 CB THR B 125 8697 7962 9270 -85 -332 -238 C ATOM 1552 OG1 THR B 125 11.904 6.082 -11.794 1.00 68.62 O ANISOU 1552 OG1 THR B 125 8710 7970 9392 -42 -205 -278 O ATOM 1553 CG2 THR B 125 13.662 4.458 -11.996 1.00 65.81 C ANISOU 1553 CG2 THR B 125 8311 7653 9041 -101 -511 -246 C ATOM 1554 N LEU B 126 11.051 2.070 -9.999 1.00 61.88 N ANISOU 1554 N LEU B 126 8045 7231 8237 -162 -335 -94 N ATOM 1555 CA LEU B 126 11.192 0.770 -9.331 1.00 61.92 C ANISOU 1555 CA LEU B 126 8156 7240 8130 -218 -437 -34 C ATOM 1556 C LEU B 126 10.449 -0.322 -10.113 1.00 64.26 C ANISOU 1556 C LEU B 126 8333 7575 8506 -211 -413 57 C ATOM 1557 O LEU B 126 11.060 -1.322 -10.483 1.00 63.43 O ANISOU 1557 O LEU B 126 8203 7460 8437 -214 -564 98 O ATOM 1558 CB LEU B 126 10.664 0.855 -7.882 1.00 63.68 C ANISOU 1558 CB LEU B 126 8600 7448 8147 -283 -340 -47 C ATOM 1559 CG LEU B 126 11.097 -0.238 -6.909 1.00 69.56 C ANISOU 1559 CG LEU B 126 9532 8172 8726 -357 -482 5 C ATOM 1560 CD1 LEU B 126 11.370 0.344 -5.538 1.00 71.62 C ANISOU 1560 CD1 LEU B 126 10044 8395 8774 -422 -482 -56 C ATOM 1561 CD2 LEU B 126 10.045 -1.333 -6.799 1.00 72.33 C ANISOU 1561 CD2 LEU B 126 9896 8549 9035 -398 -386 100 C ATOM 1562 N ASN B 127 9.144 -0.112 -10.382 1.00 60.06 N ANISOU 1562 N ASN B 127 7722 7081 8018 -199 -228 83 N ATOM 1563 CA ASN B 127 8.295 -1.056 -11.108 1.00 58.79 C ANISOU 1563 CA ASN B 127 7443 6959 7936 -210 -199 167 C ATOM 1564 C ASN B 127 8.669 -1.193 -12.579 1.00 60.79 C ANISOU 1564 C ASN B 127 7530 7223 8345 -162 -294 179 C ATOM 1565 O ASN B 127 8.464 -2.267 -13.148 1.00 60.31 O ANISOU 1565 O ASN B 127 7419 7172 8323 -185 -352 238 O ATOM 1566 CB ASN B 127 6.817 -0.717 -10.932 1.00 58.38 C ANISOU 1566 CB ASN B 127 7330 6947 7905 -214 17 188 C ATOM 1567 CG ASN B 127 6.321 -0.945 -9.528 1.00 75.19 C ANISOU 1567 CG ASN B 127 9632 9071 9866 -285 135 190 C ATOM 1568 OD1 ASN B 127 6.411 -2.048 -8.975 1.00 68.90 O ANISOU 1568 OD1 ASN B 127 8953 8264 8961 -362 73 246 O ATOM 1569 ND2 ASN B 127 5.771 0.092 -8.922 1.00 66.25 N ANISOU 1569 ND2 ASN B 127 8533 7936 8702 -263 318 129 N ATOM 1570 N MET B 128 9.235 -0.126 -13.189 1.00 56.00 N ANISOU 1570 N MET B 128 6856 6604 7816 -105 -305 121 N ATOM 1571 CA MET B 128 9.680 -0.152 -14.585 1.00 54.38 C ANISOU 1571 CA MET B 128 6520 6405 7736 -70 -379 125 C ATOM 1572 C MET B 128 10.906 -1.059 -14.710 1.00 57.50 C ANISOU 1572 C MET B 128 6946 6773 8129 -82 -543 116 C ATOM 1573 O MET B 128 10.939 -1.901 -15.607 1.00 56.65 O ANISOU 1573 O MET B 128 6772 6671 8081 -82 -597 148 O ATOM 1574 CB MET B 128 9.987 1.261 -15.109 1.00 56.33 C ANISOU 1574 CB MET B 128 6714 6635 8053 -22 -335 72 C ATOM 1575 CG MET B 128 10.285 1.298 -16.596 1.00 58.98 C ANISOU 1575 CG MET B 128 6932 6979 8497 2 -382 86 C ATOM 1576 SD MET B 128 11.356 2.667 -17.087 1.00 62.88 S ANISOU 1576 SD MET B 128 7412 7430 9049 27 -390 15 S ATOM 1577 CE MET B 128 12.929 2.129 -16.427 1.00 59.69 C ANISOU 1577 CE MET B 128 7069 7001 8609 -6 -528 -45 C ATOM 1578 N PHE B 129 11.895 -0.903 -13.800 1.00 54.09 N ANISOU 1578 N PHE B 129 6615 6306 7631 -92 -628 70 N ATOM 1579 CA PHE B 129 13.101 -1.728 -13.787 1.00 53.71 C ANISOU 1579 CA PHE B 129 6580 6224 7602 -90 -797 61 C ATOM 1580 C PHE B 129 12.788 -3.164 -13.400 1.00 58.63 C ANISOU 1580 C PHE B 129 7276 6830 8170 -118 -860 131 C ATOM 1581 O PHE B 129 13.340 -4.075 -14.010 1.00 58.59 O ANISOU 1581 O PHE B 129 7225 6800 8238 -97 -957 143 O ATOM 1582 CB PHE B 129 14.211 -1.130 -12.908 1.00 56.01 C ANISOU 1582 CB PHE B 129 6946 6482 7851 -98 -897 -1 C ATOM 1583 CG PHE B 129 15.050 -0.086 -13.607 1.00 56.95 C ANISOU 1583 CG PHE B 129 6960 6598 8079 -74 -899 -72 C ATOM 1584 CD1 PHE B 129 15.786 -0.405 -14.743 1.00 59.40 C ANISOU 1584 CD1 PHE B 129 7135 6910 8526 -43 -944 -86 C ATOM 1585 CD2 PHE B 129 15.118 1.213 -13.121 1.00 59.48 C ANISOU 1585 CD2 PHE B 129 7330 6906 8363 -91 -845 -130 C ATOM 1586 CE1 PHE B 129 16.558 0.563 -15.392 1.00 60.11 C ANISOU 1586 CE1 PHE B 129 7133 6995 8711 -39 -926 -147 C ATOM 1587 CE2 PHE B 129 15.900 2.177 -13.763 1.00 62.11 C ANISOU 1587 CE2 PHE B 129 7575 7227 8799 -86 -845 -190 C ATOM 1588 CZ PHE B 129 16.611 1.847 -14.897 1.00 59.59 C ANISOU 1588 CZ PHE B 129 7115 6915 8612 -64 -882 -194 C ATOM 1589 N ALA B 130 11.857 -3.369 -12.442 1.00 55.63 N ANISOU 1589 N ALA B 130 7013 6459 7665 -169 -786 176 N ATOM 1590 CA ALA B 130 11.408 -4.699 -12.019 1.00 55.93 C ANISOU 1590 CA ALA B 130 7140 6474 7637 -217 -823 256 C ATOM 1591 C ALA B 130 10.766 -5.448 -13.197 1.00 59.14 C ANISOU 1591 C ALA B 130 7428 6896 8148 -217 -792 298 C ATOM 1592 O ALA B 130 10.977 -6.650 -13.331 1.00 59.06 O ANISOU 1592 O ALA B 130 7455 6839 8148 -231 -889 340 O ATOM 1593 CB ALA B 130 10.423 -4.584 -10.868 1.00 57.72 C ANISOU 1593 CB ALA B 130 7501 6716 7713 -285 -699 289 C ATOM 1594 N SER B 131 10.033 -4.724 -14.072 1.00 54.90 N ANISOU 1594 N SER B 131 6758 6413 7689 -200 -674 286 N ATOM 1595 CA SER B 131 9.402 -5.269 -15.275 1.00 54.08 C ANISOU 1595 CA SER B 131 6544 6329 7676 -208 -658 320 C ATOM 1596 C SER B 131 10.480 -5.703 -16.280 1.00 57.37 C ANISOU 1596 C SER B 131 6914 6709 8176 -165 -774 281 C ATOM 1597 O SER B 131 10.473 -6.855 -16.713 1.00 57.15 O ANISOU 1597 O SER B 131 6901 6645 8170 -185 -836 309 O ATOM 1598 CB SER B 131 8.465 -4.237 -15.901 1.00 56.93 C ANISOU 1598 CB SER B 131 6782 6751 8099 -192 -533 319 C ATOM 1599 OG SER B 131 7.968 -4.647 -17.165 1.00 64.13 O ANISOU 1599 OG SER B 131 7591 7681 9093 -202 -550 348 O ATOM 1600 N ILE B 132 11.418 -4.788 -16.611 1.00 53.14 N ANISOU 1600 N ILE B 132 6328 6175 7688 -110 -790 213 N ATOM 1601 CA ILE B 132 12.525 -5.001 -17.551 1.00 52.45 C ANISOU 1601 CA ILE B 132 6180 6059 7690 -68 -862 161 C ATOM 1602 C ILE B 132 13.443 -6.152 -17.096 1.00 57.32 C ANISOU 1602 C ILE B 132 6858 6605 8315 -50 -995 158 C ATOM 1603 O ILE B 132 13.768 -7.024 -17.905 1.00 56.57 O ANISOU 1603 O ILE B 132 6736 6472 8285 -33 -1035 147 O ATOM 1604 CB ILE B 132 13.288 -3.661 -17.814 1.00 55.12 C ANISOU 1604 CB ILE B 132 6455 6413 8074 -33 -832 93 C ATOM 1605 CG1 ILE B 132 12.394 -2.650 -18.574 1.00 54.89 C ANISOU 1605 CG1 ILE B 132 6363 6431 8061 -37 -716 107 C ATOM 1606 CG2 ILE B 132 14.609 -3.883 -18.564 1.00 55.82 C ANISOU 1606 CG2 ILE B 132 6478 6471 8259 4 -893 31 C ATOM 1607 CD1 ILE B 132 12.763 -1.170 -18.383 1.00 60.59 C ANISOU 1607 CD1 ILE B 132 7069 7158 8796 -18 -664 60 C ATOM 1608 N PHE B 133 13.829 -6.165 -15.803 1.00 55.23 N ANISOU 1608 N PHE B 133 6688 6315 7982 -55 -1068 169 N ATOM 1609 CA PHE B 133 14.707 -7.187 -15.231 1.00 56.06 C ANISOU 1609 CA PHE B 133 6861 6344 8097 -30 -1223 181 C ATOM 1610 C PHE B 133 14.062 -8.575 -15.152 1.00 60.15 C ANISOU 1610 C PHE B 133 7468 6809 8579 -64 -1253 255 C ATOM 1611 O PHE B 133 14.776 -9.568 -15.296 1.00 60.15 O ANISOU 1611 O PHE B 133 7481 6727 8644 -22 -1367 255 O ATOM 1612 CB PHE B 133 15.274 -6.757 -13.865 1.00 58.90 C ANISOU 1612 CB PHE B 133 7318 6688 8371 -38 -1316 181 C ATOM 1613 CG PHE B 133 16.123 -5.502 -13.823 1.00 60.42 C ANISOU 1613 CG PHE B 133 7438 6911 8609 -15 -1325 102 C ATOM 1614 CD1 PHE B 133 16.895 -5.123 -14.918 1.00 63.10 C ANISOU 1614 CD1 PHE B 133 7618 7259 9096 31 -1309 35 C ATOM 1615 CD2 PHE B 133 16.202 -4.735 -12.667 1.00 63.28 C ANISOU 1615 CD2 PHE B 133 7904 7281 8858 -52 -1351 93 C ATOM 1616 CE1 PHE B 133 17.688 -3.972 -14.872 1.00 64.04 C ANISOU 1616 CE1 PHE B 133 7671 7399 9263 35 -1314 -34 C ATOM 1617 CE2 PHE B 133 17.001 -3.589 -12.619 1.00 66.21 C ANISOU 1617 CE2 PHE B 133 8217 7668 9274 -46 -1370 17 C ATOM 1618 CZ PHE B 133 17.741 -3.217 -13.721 1.00 63.69 C ANISOU 1618 CZ PHE B 133 7725 7359 9115 -5 -1353 -43 C ATOM 1619 N PHE B 134 12.730 -8.658 -14.938 1.00 56.86 N ANISOU 1619 N PHE B 134 7102 6429 8075 -139 -1150 316 N ATOM 1620 CA PHE B 134 12.042 -9.955 -14.900 1.00 57.25 C ANISOU 1620 CA PHE B 134 7233 6425 8095 -195 -1168 389 C ATOM 1621 C PHE B 134 11.849 -10.534 -16.310 1.00 61.33 C ANISOU 1621 C PHE B 134 7662 6928 8713 -188 -1151 368 C ATOM 1622 O PHE B 134 11.760 -11.754 -16.451 1.00 61.59 O ANISOU 1622 O PHE B 134 7763 6881 8758 -211 -1211 402 O ATOM 1623 CB PHE B 134 10.736 -9.922 -14.085 1.00 59.38 C ANISOU 1623 CB PHE B 134 7582 6735 8244 -292 -1061 463 C ATOM 1624 CG PHE B 134 10.935 -10.168 -12.603 1.00 62.05 C ANISOU 1624 CG PHE B 134 8101 7031 8445 -328 -1118 512 C ATOM 1625 CD1 PHE B 134 11.485 -11.361 -12.144 1.00 66.02 C ANISOU 1625 CD1 PHE B 134 8735 7425 8922 -331 -1268 565 C ATOM 1626 CD2 PHE B 134 10.549 -9.217 -11.665 1.00 64.48 C ANISOU 1626 CD2 PHE B 134 8466 7395 8638 -361 -1022 507 C ATOM 1627 CE1 PHE B 134 11.679 -11.581 -10.777 1.00 68.26 C ANISOU 1627 CE1 PHE B 134 9213 7665 9059 -372 -1341 622 C ATOM 1628 CE2 PHE B 134 10.738 -9.441 -10.298 1.00 68.64 C ANISOU 1628 CE2 PHE B 134 9193 7881 9007 -409 -1076 551 C ATOM 1629 CZ PHE B 134 11.305 -10.620 -9.863 1.00 67.71 C ANISOU 1629 CZ PHE B 134 9212 7661 8854 -417 -1244 614 C ATOM 1630 N ILE B 135 11.837 -9.662 -17.348 1.00 57.57 N ANISOU 1630 N ILE B 135 7056 6517 8299 -161 -1075 310 N ATOM 1631 CA ILE B 135 11.773 -10.040 -18.768 1.00 57.24 C ANISOU 1631 CA ILE B 135 6949 6467 8332 -158 -1059 276 C ATOM 1632 C ILE B 135 13.135 -10.680 -19.113 1.00 62.74 C ANISOU 1632 C ILE B 135 7647 7077 9114 -79 -1148 211 C ATOM 1633 O ILE B 135 13.182 -11.708 -19.794 1.00 62.88 O ANISOU 1633 O ILE B 135 7696 7024 9171 -80 -1176 198 O ATOM 1634 CB ILE B 135 11.433 -8.802 -19.662 1.00 59.27 C ANISOU 1634 CB ILE B 135 7093 6815 8612 -154 -962 244 C ATOM 1635 CG1 ILE B 135 9.931 -8.453 -19.575 1.00 59.58 C ANISOU 1635 CG1 ILE B 135 7106 6924 8608 -226 -882 312 C ATOM 1636 CG2 ILE B 135 11.867 -8.998 -21.128 1.00 59.50 C ANISOU 1636 CG2 ILE B 135 7077 6828 8703 -136 -957 184 C ATOM 1637 CD1 ILE B 135 9.565 -7.006 -19.966 1.00 65.26 C ANISOU 1637 CD1 ILE B 135 7729 7722 9345 -204 -796 300 C ATOM 1638 N THR B 136 14.230 -10.071 -18.596 1.00 60.11 N ANISOU 1638 N THR B 136 7278 6743 8817 -10 -1193 168 N ATOM 1639 CA THR B 136 15.624 -10.505 -18.734 1.00 60.86 C ANISOU 1639 CA THR B 136 7335 6764 9024 78 -1280 105 C ATOM 1640 C THR B 136 15.801 -11.888 -18.074 1.00 67.03 C ANISOU 1640 C THR B 136 8229 7429 9810 96 -1407 155 C ATOM 1641 O THR B 136 16.439 -12.760 -18.666 1.00 66.98 O ANISOU 1641 O THR B 136 8208 7333 9906 157 -1447 112 O ATOM 1642 CB THR B 136 16.567 -9.432 -18.144 1.00 67.03 C ANISOU 1642 CB THR B 136 8047 7584 9837 120 -1313 65 C ATOM 1643 OG1 THR B 136 16.249 -8.158 -18.704 1.00 65.29 O ANISOU 1643 OG1 THR B 136 7752 7456 9600 92 -1190 33 O ATOM 1644 CG2 THR B 136 18.038 -9.738 -18.375 1.00 65.79 C ANISOU 1644 CG2 THR B 136 7799 7366 9832 213 -1393 -7 C ATOM 1645 N CYS B 137 15.213 -12.081 -16.866 1.00 65.08 N ANISOU 1645 N CYS B 137 8105 7174 9448 41 -1459 245 N ATOM 1646 CA CYS B 137 15.238 -13.338 -16.107 1.00 66.65 C ANISOU 1646 CA CYS B 137 8448 7257 9620 37 -1582 318 C ATOM 1647 C CYS B 137 14.505 -14.445 -16.854 1.00 71.28 C ANISOU 1647 C CYS B 137 9089 7778 10218 -9 -1547 339 C ATOM 1648 O CYS B 137 14.966 -15.587 -16.847 1.00 71.95 O ANISOU 1648 O CYS B 137 9245 7730 10363 34 -1647 350 O ATOM 1649 CB CYS B 137 14.669 -13.144 -14.706 1.00 67.73 C ANISOU 1649 CB CYS B 137 8722 7415 9598 -37 -1609 409 C ATOM 1650 SG CYS B 137 15.783 -12.284 -13.569 1.00 72.45 S ANISOU 1650 SG CYS B 137 9330 8029 10170 15 -1734 392 S ATOM 1651 N MET B 138 13.370 -14.101 -17.502 1.00 67.43 N ANISOU 1651 N MET B 138 8566 7373 9680 -97 -1417 345 N ATOM 1652 CA MET B 138 12.564 -15.016 -18.309 1.00 67.60 C ANISOU 1652 CA MET B 138 8628 7349 9706 -166 -1384 359 C ATOM 1653 C MET B 138 13.381 -15.522 -19.501 1.00 71.08 C ANISOU 1653 C MET B 138 9026 7716 10264 -88 -1397 261 C ATOM 1654 O MET B 138 13.375 -16.721 -19.768 1.00 71.62 O ANISOU 1654 O MET B 138 9187 7662 10364 -95 -1446 263 O ATOM 1655 CB MET B 138 11.271 -14.332 -18.794 1.00 69.37 C ANISOU 1655 CB MET B 138 8787 7696 9874 -266 -1262 381 C ATOM 1656 CG MET B 138 10.114 -14.407 -17.805 1.00 73.88 C ANISOU 1656 CG MET B 138 9423 8302 10345 -375 -1223 484 C ATOM 1657 SD MET B 138 9.561 -16.083 -17.360 1.00 80.19 S ANISOU 1657 SD MET B 138 10395 8964 11109 -475 -1290 572 S ATOM 1658 CE MET B 138 9.127 -16.754 -18.981 1.00 76.75 C ANISOU 1658 CE MET B 138 9919 8495 10748 -521 -1283 519 C ATOM 1659 N SER B 139 14.114 -14.611 -20.182 1.00 66.52 N ANISOU 1659 N SER B 139 8321 7205 9750 -18 -1342 171 N ATOM 1660 CA SER B 139 14.977 -14.927 -21.324 1.00 66.46 C ANISOU 1660 CA SER B 139 8262 7140 9848 56 -1315 63 C ATOM 1661 C SER B 139 16.118 -15.867 -20.921 1.00 71.71 C ANISOU 1661 C SER B 139 8955 7663 10630 169 -1423 36 C ATOM 1662 O SER B 139 16.423 -16.797 -21.668 1.00 72.13 O ANISOU 1662 O SER B 139 9044 7605 10755 206 -1416 -24 O ATOM 1663 CB SER B 139 15.530 -13.652 -21.953 1.00 68.80 C ANISOU 1663 CB SER B 139 8421 7542 10178 92 -1224 -12 C ATOM 1664 OG SER B 139 14.509 -12.927 -22.619 1.00 76.00 O ANISOU 1664 OG SER B 139 9315 8557 11003 3 -1133 6 O ATOM 1665 N VAL B 140 16.718 -15.641 -19.727 1.00 68.60 N ANISOU 1665 N VAL B 140 8552 7260 10253 222 -1530 82 N ATOM 1666 CA VAL B 140 17.801 -16.460 -19.163 1.00 69.68 C ANISOU 1666 CA VAL B 140 8705 7261 10509 337 -1672 79 C ATOM 1667 C VAL B 140 17.266 -17.862 -18.808 1.00 74.23 C ANISOU 1667 C VAL B 140 9462 7690 11053 306 -1758 156 C ATOM 1668 O VAL B 140 17.900 -18.858 -19.165 1.00 74.79 O ANISOU 1668 O VAL B 140 9556 7613 11249 396 -1809 114 O ATOM 1669 CB VAL B 140 18.520 -15.746 -17.978 1.00 73.62 C ANISOU 1669 CB VAL B 140 9158 7801 11014 382 -1789 116 C ATOM 1670 CG1 VAL B 140 19.456 -16.689 -17.223 1.00 75.20 C ANISOU 1670 CG1 VAL B 140 9400 7851 11321 488 -1983 150 C ATOM 1671 CG2 VAL B 140 19.288 -14.521 -18.466 1.00 72.69 C ANISOU 1671 CG2 VAL B 140 8852 7792 10976 423 -1712 21 C ATOM 1672 N ASP B 141 16.081 -17.927 -18.157 1.00 70.43 N ANISOU 1672 N ASP B 141 9106 7243 10413 176 -1755 264 N ATOM 1673 CA ASP B 141 15.406 -19.172 -17.772 1.00 71.31 C ANISOU 1673 CA ASP B 141 9400 7224 10470 108 -1818 353 C ATOM 1674 C ASP B 141 14.983 -19.988 -19.001 1.00 74.94 C ANISOU 1674 C ASP B 141 9892 7609 10973 73 -1746 291 C ATOM 1675 O ASP B 141 15.081 -21.217 -18.974 1.00 75.57 O ANISOU 1675 O ASP B 141 10099 7515 11099 90 -1822 310 O ATOM 1676 CB ASP B 141 14.194 -18.883 -16.869 1.00 72.89 C ANISOU 1676 CB ASP B 141 9696 7506 10493 -42 -1787 470 C ATOM 1677 CG ASP B 141 13.557 -20.129 -16.284 1.00 85.29 C ANISOU 1677 CG ASP B 141 11467 8941 12000 -130 -1854 578 C ATOM 1678 OD1 ASP B 141 14.104 -20.668 -15.296 1.00 87.29 O ANISOU 1678 OD1 ASP B 141 11841 9083 12243 -85 -1997 651 O ATOM 1679 OD2 ASP B 141 12.513 -20.567 -16.816 1.00 91.17 O ANISOU 1679 OD2 ASP B 141 12251 9684 12705 -250 -1774 595 O ATOM 1680 N ARG B 142 14.523 -19.304 -20.073 1.00 70.32 N ANISOU 1680 N ARG B 142 9209 7143 10366 23 -1610 219 N ATOM 1681 CA ARG B 142 14.118 -19.936 -21.332 1.00 70.36 C ANISOU 1681 CA ARG B 142 9254 7094 10387 -25 -1544 149 C ATOM 1682 C ARG B 142 15.334 -20.505 -22.060 1.00 75.34 C ANISOU 1682 C ARG B 142 9863 7597 11166 119 -1546 26 C ATOM 1683 O ARG B 142 15.250 -21.602 -22.616 1.00 76.18 O ANISOU 1683 O ARG B 142 10083 7557 11306 111 -1553 -13 O ATOM 1684 CB ARG B 142 13.355 -18.952 -22.232 1.00 69.24 C ANISOU 1684 CB ARG B 142 9019 7118 10171 -114 -1422 116 C ATOM 1685 CG ARG B 142 11.880 -18.828 -21.879 1.00 78.90 C ANISOU 1685 CG ARG B 142 10277 8422 11278 -275 -1407 222 C ATOM 1686 CD ARG B 142 11.170 -17.851 -22.793 1.00 87.74 C ANISOU 1686 CD ARG B 142 11293 9693 12349 -344 -1314 196 C ATOM 1687 NE ARG B 142 9.716 -17.965 -22.681 1.00 96.46 N ANISOU 1687 NE ARG B 142 12416 10854 13381 -500 -1305 285 N ATOM 1688 CZ ARG B 142 8.848 -17.379 -23.500 1.00110.74 C ANISOU 1688 CZ ARG B 142 14150 12771 15156 -582 -1259 285 C ATOM 1689 NH1 ARG B 142 9.279 -16.628 -24.508 1.00 97.72 N ANISOU 1689 NH1 ARG B 142 12433 11182 13513 -531 -1214 205 N ATOM 1690 NH2 ARG B 142 7.545 -17.542 -23.324 1.00 98.25 N ANISOU 1690 NH2 ARG B 142 12557 11234 13537 -721 -1261 370 N ATOM 1691 N TYR B 143 16.468 -19.770 -22.031 1.00 71.63 N ANISOU 1691 N TYR B 143 9246 7176 10794 247 -1533 -39 N ATOM 1692 CA TYR B 143 17.733 -20.182 -22.641 1.00 72.57 C ANISOU 1692 CA TYR B 143 9300 7189 11086 398 -1513 -161 C ATOM 1693 C TYR B 143 18.318 -21.391 -21.903 1.00 78.09 C ANISOU 1693 C TYR B 143 10087 7686 11898 502 -1663 -124 C ATOM 1694 O TYR B 143 18.749 -22.343 -22.552 1.00 78.90 O ANISOU 1694 O TYR B 143 10238 7630 12109 576 -1643 -208 O ATOM 1695 CB TYR B 143 18.733 -19.006 -22.686 1.00 73.22 C ANISOU 1695 CB TYR B 143 9180 7389 11252 486 -1464 -225 C ATOM 1696 CG TYR B 143 20.139 -19.398 -23.089 1.00 76.50 C ANISOU 1696 CG TYR B 143 9487 7699 11880 653 -1449 -341 C ATOM 1697 CD1 TYR B 143 20.453 -19.680 -24.416 1.00 79.02 C ANISOU 1697 CD1 TYR B 143 9792 7975 12256 681 -1293 -481 C ATOM 1698 CD2 TYR B 143 21.159 -19.479 -22.146 1.00 78.32 C ANISOU 1698 CD2 TYR B 143 9626 7874 12259 782 -1590 -315 C ATOM 1699 CE1 TYR B 143 21.742 -20.057 -24.789 1.00 81.35 C ANISOU 1699 CE1 TYR B 143 9972 8171 12766 841 -1250 -599 C ATOM 1700 CE2 TYR B 143 22.451 -19.853 -22.508 1.00 80.85 C ANISOU 1700 CE2 TYR B 143 9812 8096 12810 946 -1577 -422 C ATOM 1701 CZ TYR B 143 22.740 -20.136 -23.832 1.00 88.61 C ANISOU 1701 CZ TYR B 143 10768 9037 13862 978 -1392 -568 C ATOM 1702 OH TYR B 143 24.014 -20.499 -24.199 1.00 91.14 O ANISOU 1702 OH TYR B 143 10940 9260 14427 1145 -1349 -685 O ATOM 1703 N GLN B 144 18.312 -21.349 -20.552 1.00 74.93 N ANISOU 1703 N GLN B 144 9724 7282 11465 504 -1812 3 N ATOM 1704 CA GLN B 144 18.811 -22.404 -19.665 1.00 76.66 C ANISOU 1704 CA GLN B 144 10047 7311 11767 592 -1991 76 C ATOM 1705 C GLN B 144 18.045 -23.722 -19.833 1.00 81.61 C ANISOU 1705 C GLN B 144 10889 7767 12352 520 -2013 117 C ATOM 1706 O GLN B 144 18.644 -24.790 -19.710 1.00 82.86 O ANISOU 1706 O GLN B 144 11124 7718 12640 630 -2113 113 O ATOM 1707 CB GLN B 144 18.761 -21.940 -18.205 1.00 77.89 C ANISOU 1707 CB GLN B 144 10237 7525 11831 564 -2135 214 C ATOM 1708 CG GLN B 144 20.126 -21.908 -17.533 1.00 94.94 C ANISOU 1708 CG GLN B 144 12298 9622 14153 732 -2299 214 C ATOM 1709 CD GLN B 144 20.372 -20.626 -16.775 1.00114.64 C ANISOU 1709 CD GLN B 144 14690 12289 16580 709 -2337 245 C ATOM 1710 OE1 GLN B 144 21.270 -19.849 -17.111 1.00111.24 O ANISOU 1710 OE1 GLN B 144 14056 11937 16273 793 -2307 153 O ATOM 1711 NE2 GLN B 144 19.597 -20.381 -15.724 1.00105.80 N ANISOU 1711 NE2 GLN B 144 13715 11222 15261 588 -2396 371 N ATOM 1712 N SER B 145 16.729 -23.639 -20.127 1.00 77.40 N ANISOU 1712 N SER B 145 10443 7314 11652 336 -1925 155 N ATOM 1713 CA SER B 145 15.835 -24.781 -20.347 1.00 78.17 C ANISOU 1713 CA SER B 145 10737 7272 11693 221 -1934 194 C ATOM 1714 C SER B 145 16.187 -25.557 -21.623 1.00 83.48 C ANISOU 1714 C SER B 145 11441 7805 12474 280 -1862 48 C ATOM 1715 O SER B 145 15.961 -26.767 -21.680 1.00 84.79 O ANISOU 1715 O SER B 145 11781 7770 12663 258 -1915 62 O ATOM 1716 CB SER B 145 14.385 -24.312 -20.424 1.00 80.02 C ANISOU 1716 CB SER B 145 10997 7658 11748 10 -1850 258 C ATOM 1717 OG SER B 145 13.964 -23.706 -19.213 1.00 87.70 O ANISOU 1717 OG SER B 145 11971 8740 12613 -54 -1892 388 O ATOM 1718 N VAL B 146 16.724 -24.856 -22.643 1.00 79.44 N ANISOU 1718 N VAL B 146 10777 7391 12015 345 -1731 -94 N ATOM 1719 CA VAL B 146 17.102 -25.422 -23.942 1.00 80.28 C ANISOU 1719 CA VAL B 146 10912 7390 12201 396 -1624 -256 C ATOM 1720 C VAL B 146 18.464 -26.138 -23.875 1.00 86.75 C ANISOU 1720 C VAL B 146 11699 8015 13247 618 -1667 -334 C ATOM 1721 O VAL B 146 18.541 -27.325 -24.200 1.00 88.13 O ANISOU 1721 O VAL B 146 12022 7972 13493 656 -1683 -382 O ATOM 1722 CB VAL B 146 17.035 -24.357 -25.079 1.00 82.67 C ANISOU 1722 CB VAL B 146 11092 7879 12439 350 -1453 -366 C ATOM 1723 CG1 VAL B 146 17.524 -24.921 -26.410 1.00 83.77 C ANISOU 1723 CG1 VAL B 146 11281 7905 12643 403 -1324 -544 C ATOM 1724 CG2 VAL B 146 15.626 -23.790 -25.227 1.00 80.88 C ANISOU 1724 CG2 VAL B 146 10902 7814 12016 141 -1430 -287 C ATOM 1725 N ILE B 147 19.529 -25.412 -23.474 1.00 83.69 N ANISOU 1725 N ILE B 147 11111 7702 12985 764 -1686 -351 N ATOM 1726 CA ILE B 147 20.902 -25.926 -23.376 1.00 85.62 C ANISOU 1726 CA ILE B 147 11260 7790 13481 991 -1732 -424 C ATOM 1727 C ILE B 147 21.013 -27.011 -22.276 1.00 91.08 C ANISOU 1727 C ILE B 147 12092 8269 14245 1060 -1953 -297 C ATOM 1728 O ILE B 147 21.679 -28.026 -22.493 1.00 92.70 O ANISOU 1728 O ILE B 147 12339 8248 14633 1208 -1982 -362 O ATOM 1729 CB ILE B 147 21.953 -24.767 -23.249 1.00 88.37 C ANISOU 1729 CB ILE B 147 11334 8296 13946 1100 -1701 -471 C ATOM 1730 CG1 ILE B 147 23.418 -25.281 -23.258 1.00 91.47 C ANISOU 1730 CG1 ILE B 147 11580 8534 14641 1341 -1735 -561 C ATOM 1731 CG2 ILE B 147 21.700 -23.835 -22.060 1.00 87.53 C ANISOU 1731 CG2 ILE B 147 11174 8351 13732 1033 -1833 -322 C ATOM 1732 CD1 ILE B 147 24.031 -25.443 -24.642 1.00101.67 C ANISOU 1732 CD1 ILE B 147 12793 9780 16058 1422 -1502 -769 C ATOM 1733 N TYR B 148 20.321 -26.813 -21.134 1.00 86.86 N ANISOU 1733 N TYR B 148 11647 7796 13560 947 -2095 -119 N ATOM 1734 CA TYR B 148 20.290 -27.766 -20.022 1.00 88.30 C ANISOU 1734 CA TYR B 148 12001 7789 13758 974 -2307 28 C ATOM 1735 C TYR B 148 18.844 -28.233 -19.773 1.00 91.70 C ANISOU 1735 C TYR B 148 12670 8203 13969 750 -2310 143 C ATOM 1736 O TYR B 148 18.148 -27.662 -18.926 1.00 90.11 O ANISOU 1736 O TYR B 148 12504 8139 13595 616 -2353 273 O ATOM 1737 CB TYR B 148 20.914 -27.185 -18.741 1.00 89.52 C ANISOU 1737 CB TYR B 148 12067 8010 13935 1047 -2491 146 C ATOM 1738 CG TYR B 148 22.219 -26.442 -18.940 1.00 91.38 C ANISOU 1738 CG TYR B 148 12025 8325 14371 1223 -2482 42 C ATOM 1739 CD1 TYR B 148 23.383 -27.119 -19.297 1.00 95.48 C ANISOU 1739 CD1 TYR B 148 12441 8665 15171 1442 -2518 -53 C ATOM 1740 CD2 TYR B 148 22.305 -25.073 -18.708 1.00 90.48 C ANISOU 1740 CD2 TYR B 148 11745 8453 14181 1172 -2443 42 C ATOM 1741 CE1 TYR B 148 24.588 -26.442 -19.471 1.00 96.76 C ANISOU 1741 CE1 TYR B 148 12321 8904 15539 1595 -2502 -149 C ATOM 1742 CE2 TYR B 148 23.505 -24.384 -18.877 1.00 91.81 C ANISOU 1742 CE2 TYR B 148 11653 8692 14540 1314 -2436 -50 C ATOM 1743 CZ TYR B 148 24.645 -25.074 -19.257 1.00101.90 C ANISOU 1743 CZ TYR B 148 12811 9803 16103 1521 -2465 -144 C ATOM 1744 OH TYR B 148 25.834 -24.401 -19.417 1.00103.98 O ANISOU 1744 OH TYR B 148 12792 10140 16576 1653 -2450 -236 O ATOM 1745 N PRO B 149 18.372 -29.275 -20.499 1.00 89.40 N ANISOU 1745 N PRO B 149 12544 7739 13684 698 -2257 90 N ATOM 1746 CA PRO B 149 16.993 -29.750 -20.288 1.00 88.88 C ANISOU 1746 CA PRO B 149 12688 7654 13429 468 -2261 197 C ATOM 1747 C PRO B 149 16.775 -30.505 -18.971 1.00 94.84 C ANISOU 1747 C PRO B 149 13639 8256 14141 433 -2449 388 C ATOM 1748 O PRO B 149 15.625 -30.742 -18.597 1.00 94.21 O ANISOU 1748 O PRO B 149 13710 8192 13894 225 -2445 499 O ATOM 1749 CB PRO B 149 16.721 -30.631 -21.519 1.00 91.61 C ANISOU 1749 CB PRO B 149 13148 7846 13813 433 -2159 63 C ATOM 1750 CG PRO B 149 17.905 -30.441 -22.440 1.00 96.56 C ANISOU 1750 CG PRO B 149 13615 8451 14624 638 -2060 -126 C ATOM 1751 CD PRO B 149 19.040 -30.060 -21.554 1.00 92.63 C ANISOU 1751 CD PRO B 149 12962 7962 14272 834 -2179 -78 C ATOM 1752 N PHE B 150 17.863 -30.857 -18.256 1.00 93.53 N ANISOU 1752 N PHE B 150 13468 7945 14123 628 -2616 432 N ATOM 1753 CA PHE B 150 17.791 -31.556 -16.971 1.00 95.28 C ANISOU 1753 CA PHE B 150 13894 8008 14299 610 -2820 624 C ATOM 1754 C PHE B 150 17.286 -30.662 -15.829 1.00 99.03 C ANISOU 1754 C PHE B 150 14373 8687 14569 479 -2866 774 C ATOM 1755 O PHE B 150 16.841 -31.191 -14.809 1.00 99.92 O ANISOU 1755 O PHE B 150 14702 8702 14562 382 -2986 945 O ATOM 1756 CB PHE B 150 19.145 -32.201 -16.608 1.00 99.39 C ANISOU 1756 CB PHE B 150 14402 8304 15059 872 -3008 627 C ATOM 1757 CG PHE B 150 20.316 -31.250 -16.509 1.00100.27 C ANISOU 1757 CG PHE B 150 14233 8553 15311 1060 -3047 560 C ATOM 1758 CD1 PHE B 150 21.212 -31.113 -17.561 1.00103.40 C ANISOU 1758 CD1 PHE B 150 14414 8943 15930 1236 -2935 366 C ATOM 1759 CD2 PHE B 150 20.536 -30.507 -15.354 1.00101.77 C ANISOU 1759 CD2 PHE B 150 14386 8874 15410 1049 -3192 687 C ATOM 1760 CE1 PHE B 150 22.305 -30.246 -17.461 1.00103.96 C ANISOU 1760 CE1 PHE B 150 14212 9139 16148 1395 -2966 306 C ATOM 1761 CE2 PHE B 150 21.619 -29.629 -15.264 1.00104.24 C ANISOU 1761 CE2 PHE B 150 14437 9309 15860 1205 -3239 624 C ATOM 1762 CZ PHE B 150 22.498 -29.508 -16.316 1.00102.51 C ANISOU 1762 CZ PHE B 150 13984 9084 15880 1375 -3127 437 C ATOM 1763 N LEU B 151 17.382 -29.319 -15.985 1.00 94.33 N ANISOU 1763 N LEU B 151 13553 8360 13928 477 -2765 710 N ATOM 1764 CA LEU B 151 16.948 -28.334 -14.986 1.00 93.44 C ANISOU 1764 CA LEU B 151 13428 8451 13626 365 -2779 820 C ATOM 1765 C LEU B 151 15.449 -28.407 -14.691 1.00 98.37 C ANISOU 1765 C LEU B 151 14206 9143 14026 108 -2679 921 C ATOM 1766 O LEU B 151 15.048 -28.221 -13.541 1.00 98.31 O ANISOU 1766 O LEU B 151 14320 9177 13856 7 -2738 1065 O ATOM 1767 CB LEU B 151 17.357 -26.907 -15.393 1.00 91.35 C ANISOU 1767 CB LEU B 151 12891 8436 13382 419 -2673 707 C ATOM 1768 CG LEU B 151 18.824 -26.523 -15.155 1.00 96.64 C ANISOU 1768 CG LEU B 151 13393 9095 14230 637 -2802 659 C ATOM 1769 CD1 LEU B 151 19.192 -25.291 -15.945 1.00 96.88 C ANISOU 1769 CD1 LEU B 151 13157 9337 14315 678 -2650 514 C ATOM 1770 CD2 LEU B 151 19.105 -26.269 -13.676 1.00 97.70 C ANISOU 1770 CD2 LEU B 151 13617 9239 14267 634 -3003 810 C ATOM 1771 N SER B 152 14.630 -28.699 -15.721 1.00 95.41 N ANISOU 1771 N SER B 152 13831 8774 13645 -4 -2530 846 N ATOM 1772 CA SER B 152 13.175 -28.837 -15.599 1.00 95.41 C ANISOU 1772 CA SER B 152 13940 8834 13475 -254 -2429 928 C ATOM 1773 C SER B 152 12.775 -30.133 -14.876 1.00102.74 C ANISOU 1773 C SER B 152 15154 9529 14355 -352 -2537 1073 C ATOM 1774 O SER B 152 11.698 -30.186 -14.277 1.00102.69 O ANISOU 1774 O SER B 152 15258 9573 14188 -561 -2482 1191 O ATOM 1775 CB SER B 152 12.504 -28.750 -16.966 1.00 97.80 C ANISOU 1775 CB SER B 152 14147 9211 13802 -340 -2272 801 C ATOM 1776 OG SER B 152 13.011 -29.724 -17.864 1.00107.65 O ANISOU 1776 OG SER B 152 15458 10251 15194 -248 -2300 697 O ATOM 1777 N GLN B 153 13.649 -31.164 -14.922 1.00101.92 N ANISOU 1777 N GLN B 153 15167 9161 14397 -201 -2683 1067 N ATOM 1778 CA GLN B 153 13.443 -32.461 -14.265 1.00104.55 C ANISOU 1778 CA GLN B 153 15791 9227 14707 -265 -2811 1206 C ATOM 1779 C GLN B 153 13.652 -32.382 -12.742 1.00110.60 C ANISOU 1779 C GLN B 153 16702 9973 15348 -274 -2961 1393 C ATOM 1780 O GLN B 153 13.185 -33.266 -12.020 1.00112.10 O ANISOU 1780 O GLN B 153 17157 9992 15446 -397 -3037 1546 O ATOM 1781 CB GLN B 153 14.348 -33.552 -14.880 1.00107.71 C ANISOU 1781 CB GLN B 153 16260 9336 15327 -76 -2915 1125 C ATOM 1782 CG GLN B 153 14.010 -33.945 -16.328 1.00119.80 C ANISOU 1782 CG GLN B 153 17751 10823 16946 -110 -2773 955 C ATOM 1783 CD GLN B 153 12.576 -34.387 -16.535 1.00136.64 C ANISOU 1783 CD GLN B 153 20024 12956 18938 -396 -2676 1006 C ATOM 1784 OE1 GLN B 153 11.850 -33.835 -17.366 1.00130.78 O ANISOU 1784 OE1 GLN B 153 19152 12397 18142 -520 -2524 914 O ATOM 1785 NE2 GLN B 153 12.130 -35.382 -15.784 1.00129.19 N ANISOU 1785 NE2 GLN B 153 19344 11807 17934 -516 -2770 1160 N ATOM 1786 N ARG B 154 14.349 -31.322 -12.268 1.00106.92 N ANISOU 1786 N ARG B 154 16080 9678 14869 -157 -3006 1380 N ATOM 1787 CA ARG B 154 14.643 -31.061 -10.856 1.00108.14 C ANISOU 1787 CA ARG B 154 16359 9842 14886 -159 -3156 1536 C ATOM 1788 C ARG B 154 13.370 -30.769 -10.069 1.00112.73 C ANISOU 1788 C ARG B 154 17080 10552 15201 -425 -3033 1661 C ATOM 1789 O ARG B 154 12.647 -29.823 -10.393 1.00110.17 O ANISOU 1789 O ARG B 154 16592 10468 14799 -531 -2835 1594 O ATOM 1790 CB ARG B 154 15.642 -29.903 -10.707 1.00107.28 C ANISOU 1790 CB ARG B 154 16022 9904 14835 11 -3213 1460 C ATOM 1791 CG ARG B 154 17.081 -30.303 -10.985 1.00118.91 C ANISOU 1791 CG ARG B 154 17401 11213 16565 282 -3400 1396 C ATOM 1792 N ARG B 155 13.111 -31.593 -9.034 1.00112.47 N ANISOU 1792 N ARG B 155 17351 10346 15035 -530 -3147 1845 N ATOM 1793 CA ARG B 155 11.936 -31.503 -8.155 1.00113.09 C ANISOU 1793 CA ARG B 155 17608 10505 14855 -794 -3027 1983 C ATOM 1794 C ARG B 155 11.941 -30.229 -7.275 1.00116.91 C ANISOU 1794 C ARG B 155 18036 11228 15157 -822 -2982 2006 C ATOM 1795 O ARG B 155 10.880 -29.804 -6.811 1.00116.21 O ANISOU 1795 O ARG B 155 17992 11283 14878 -1029 -2796 2058 O ATOM 1796 CB ARG B 155 11.797 -32.764 -7.266 1.00116.27 C ANISOU 1796 CB ARG B 155 18382 10635 15160 -891 -3174 2181 C ATOM 1797 CG ARG B 155 11.945 -34.110 -7.985 1.00127.87 C ANISOU 1797 CG ARG B 155 19957 11814 16812 -843 -3259 2171 C ATOM 1798 CD ARG B 155 10.630 -34.806 -8.283 1.00138.48 C ANISOU 1798 CD ARG B 155 21421 13104 18090 -1108 -3089 2214 C ATOM 1799 NE ARG B 155 10.104 -34.455 -9.600 1.00145.31 N ANISOU 1799 NE ARG B 155 22026 14112 19074 -1138 -2901 2034 N ATOM 1800 N ASN B 156 13.134 -29.621 -7.073 1.00113.64 N ANISOU 1800 N ASN B 156 17514 10850 14813 -615 -3144 1957 N ATOM 1801 CA ASN B 156 13.340 -28.432 -6.238 1.00112.99 C ANISOU 1801 CA ASN B 156 17395 10964 14573 -619 -3143 1966 C ATOM 1802 C ASN B 156 13.915 -27.231 -7.027 1.00114.85 C ANISOU 1802 C ASN B 156 17284 11402 14953 -469 -3077 1780 C ATOM 1803 O ASN B 156 15.017 -27.342 -7.573 1.00114.41 O ANISOU 1803 O ASN B 156 17085 11272 15114 -260 -3222 1698 O ATOM 1804 CB ASN B 156 14.251 -28.791 -5.054 1.00116.72 C ANISOU 1804 CB ASN B 156 18103 11283 14961 -544 -3438 2107 C ATOM 1805 CG ASN B 156 13.991 -28.016 -3.782 1.00142.38 C ANISOU 1805 CG ASN B 156 21515 14664 17918 -673 -3426 2197 C ATOM 1806 OD1 ASN B 156 14.914 -27.492 -3.158 1.00138.08 O ANISOU 1806 OD1 ASN B 156 20978 14144 17342 -566 -3621 2207 O ATOM 1807 ND2 ASN B 156 12.742 -27.964 -3.332 1.00134.69 N ANISOU 1807 ND2 ASN B 156 20687 13767 16721 -912 -3203 2266 N ATOM 1808 N PRO B 157 13.192 -26.076 -7.094 1.00110.18 N ANISOU 1808 N PRO B 157 16553 11059 14254 -571 -2854 1713 N ATOM 1809 CA PRO B 157 13.705 -24.903 -7.835 1.00107.85 C ANISOU 1809 CA PRO B 157 15948 10946 14084 -444 -2788 1548 C ATOM 1810 C PRO B 157 14.460 -23.926 -6.914 1.00111.94 C ANISOU 1810 C PRO B 157 16467 11560 14507 -382 -2903 1553 C ATOM 1811 O PRO B 157 14.073 -22.764 -6.769 1.00110.08 O ANISOU 1811 O PRO B 157 16134 11523 14170 -441 -2752 1497 O ATOM 1812 CB PRO B 157 12.416 -24.292 -8.410 1.00107.93 C ANISOU 1812 CB PRO B 157 15832 11141 14037 -595 -2498 1488 C ATOM 1813 CG PRO B 157 11.296 -24.753 -7.473 1.00113.79 C ANISOU 1813 CG PRO B 157 16821 11855 14557 -816 -2408 1636 C ATOM 1814 CD PRO B 157 11.861 -25.787 -6.526 1.00111.84 C ANISOU 1814 CD PRO B 157 16871 11385 14238 -806 -2640 1783 C ATOM 1815 N TRP B 158 15.530 -24.433 -6.267 1.00110.29 N ANISOU 1815 N TRP B 158 16378 11196 14332 -267 -3185 1627 N ATOM 1816 CA TRP B 158 16.372 -23.761 -5.267 1.00111.17 C ANISOU 1816 CA TRP B 158 16541 11347 14351 -214 -3373 1659 C ATOM 1817 C TRP B 158 16.812 -22.311 -5.570 1.00113.13 C ANISOU 1817 C TRP B 158 16527 11806 14649 -149 -3300 1513 C ATOM 1818 O TRP B 158 16.793 -21.492 -4.648 1.00113.05 O ANISOU 1818 O TRP B 158 16612 11897 14447 -221 -3317 1537 O ATOM 1819 CB TRP B 158 17.607 -24.605 -4.956 1.00112.16 C ANISOU 1819 CB TRP B 158 16735 11261 14619 -47 -3710 1728 C ATOM 1820 N GLN B 159 17.190 -21.987 -6.824 1.00108.03 N ANISOU 1820 N GLN B 159 15581 11219 14245 -28 -3213 1363 N ATOM 1821 CA GLN B 159 17.667 -20.637 -7.173 1.00106.26 C ANISOU 1821 CA GLN B 159 15111 11176 14085 32 -3147 1228 C ATOM 1822 C GLN B 159 16.582 -19.544 -7.214 1.00108.04 C ANISOU 1822 C GLN B 159 15299 11604 14148 -111 -2874 1179 C ATOM 1823 O GLN B 159 16.892 -18.380 -6.935 1.00107.18 O ANISOU 1823 O GLN B 159 15105 11625 13994 -105 -2857 1116 O ATOM 1824 CB GLN B 159 18.474 -20.622 -8.494 1.00106.70 C ANISOU 1824 CB GLN B 159 14871 11225 14443 201 -3131 1086 C ATOM 1825 CG GLN B 159 17.714 -21.066 -9.753 1.00121.62 C ANISOU 1825 CG GLN B 159 16675 13113 16423 177 -2917 1020 C ATOM 1826 CD GLN B 159 17.711 -22.560 -9.989 1.00143.40 C ANISOU 1826 CD GLN B 159 19562 15652 19270 213 -3005 1080 C ATOM 1827 OE1 GLN B 159 18.431 -23.338 -9.345 1.00141.23 O ANISOU 1827 OE1 GLN B 159 19411 15207 19043 297 -3240 1166 O ATOM 1828 NE2 GLN B 159 16.908 -22.991 -10.948 1.00134.79 N ANISOU 1828 NE2 GLN B 159 18449 14553 18212 153 -2829 1035 N ATOM 1829 N ALA B 160 15.333 -19.908 -7.586 1.00103.29 N ANISOU 1829 N ALA B 160 14745 11021 13478 -234 -2666 1204 N ATOM 1830 CA ALA B 160 14.195 -18.987 -7.712 1.00101.32 C ANISOU 1830 CA ALA B 160 14436 10948 13112 -360 -2400 1163 C ATOM 1831 C ALA B 160 13.895 -18.153 -6.460 1.00104.64 C ANISOU 1831 C ALA B 160 15008 11459 13290 -460 -2363 1205 C ATOM 1832 O ALA B 160 13.560 -16.975 -6.592 1.00102.79 O ANISOU 1832 O ALA B 160 14651 11380 13026 -480 -2202 1121 O ATOM 1833 CB ALA B 160 12.956 -19.737 -8.159 1.00101.94 C ANISOU 1833 CB ALA B 160 14561 11002 13169 -484 -2236 1209 C ATOM 1834 N SER B 161 14.044 -18.749 -5.256 1.00102.69 N ANISOU 1834 N SER B 161 15043 11105 12868 -521 -2515 1333 N ATOM 1835 CA SER B 161 13.800 -18.091 -3.964 1.00103.20 C ANISOU 1835 CA SER B 161 15315 11230 12664 -631 -2492 1380 C ATOM 1836 C SER B 161 14.835 -17.009 -3.613 1.00105.66 C ANISOU 1836 C SER B 161 15558 11611 12977 -543 -2627 1299 C ATOM 1837 O SER B 161 14.602 -16.219 -2.694 1.00105.76 O ANISOU 1837 O SER B 161 15712 11699 12774 -632 -2571 1297 O ATOM 1838 CB SER B 161 13.716 -19.129 -2.849 1.00109.47 C ANISOU 1838 CB SER B 161 16457 11874 13262 -727 -2635 1548 C ATOM 1839 OG SER B 161 14.866 -19.958 -2.821 1.00119.73 O ANISOU 1839 OG SER B 161 17799 13007 14685 -598 -2952 1604 O ATOM 1840 N TYR B 162 15.970 -16.977 -4.341 1.00100.73 N ANISOU 1840 N TYR B 162 14720 10958 12597 -377 -2795 1226 N ATOM 1841 CA TYR B 162 17.061 -16.021 -4.143 1.00100.11 C ANISOU 1841 CA TYR B 162 14531 10934 12571 -292 -2943 1145 C ATOM 1842 C TYR B 162 17.168 -14.995 -5.282 1.00100.15 C ANISOU 1842 C TYR B 162 14217 11072 12763 -220 -2776 987 C ATOM 1843 O TYR B 162 17.624 -13.875 -5.044 1.00 99.31 O ANISOU 1843 O TYR B 162 14044 11055 12635 -213 -2789 910 O ATOM 1844 CB TYR B 162 18.396 -16.757 -3.922 1.00103.21 C ANISOU 1844 CB TYR B 162 14932 11183 13101 -163 -3291 1196 C ATOM 1845 CG TYR B 162 18.407 -17.637 -2.689 1.00107.99 C ANISOU 1845 CG TYR B 162 15880 11649 13501 -233 -3499 1363 C ATOM 1846 CD1 TYR B 162 18.692 -17.110 -1.433 1.00111.72 C ANISOU 1846 CD1 TYR B 162 16572 12138 13737 -311 -3646 1410 C ATOM 1847 CD2 TYR B 162 18.141 -19.001 -2.779 1.00109.87 C ANISOU 1847 CD2 TYR B 162 16246 11728 13771 -229 -3556 1475 C ATOM 1848 CE1 TYR B 162 18.700 -17.914 -0.294 1.00115.22 C ANISOU 1848 CE1 TYR B 162 17363 12450 13965 -386 -3846 1574 C ATOM 1849 CE2 TYR B 162 18.147 -19.817 -1.647 1.00113.45 C ANISOU 1849 CE2 TYR B 162 17039 12040 14027 -300 -3752 1643 C ATOM 1850 CZ TYR B 162 18.428 -19.268 -0.406 1.00122.61 C ANISOU 1850 CZ TYR B 162 18421 13227 14940 -379 -3899 1696 C ATOM 1851 OH TYR B 162 18.437 -20.067 0.713 1.00126.58 O ANISOU 1851 OH TYR B 162 19286 13585 15222 -459 -4101 1871 O ATOM 1852 N ILE B 163 16.726 -15.365 -6.504 1.00 94.07 N ANISOU 1852 N ILE B 163 13272 10310 12160 -182 -2623 944 N ATOM 1853 CA ILE B 163 16.746 -14.494 -7.688 1.00 91.14 C ANISOU 1853 CA ILE B 163 12623 10053 11954 -124 -2459 810 C ATOM 1854 C ILE B 163 15.684 -13.382 -7.580 1.00 92.60 C ANISOU 1854 C ILE B 163 12805 10382 11997 -229 -2210 770 C ATOM 1855 O ILE B 163 16.003 -12.219 -7.828 1.00 91.14 O ANISOU 1855 O ILE B 163 12483 10292 11855 -199 -2154 674 O ATOM 1856 CB ILE B 163 16.655 -15.323 -9.011 1.00 93.27 C ANISOU 1856 CB ILE B 163 12745 10269 12426 -56 -2399 779 C ATOM 1857 CG1 ILE B 163 17.988 -16.062 -9.279 1.00 94.76 C ANISOU 1857 CG1 ILE B 163 12856 10329 12818 93 -2626 766 C ATOM 1858 CG2 ILE B 163 16.257 -14.456 -10.225 1.00 91.75 C ANISOU 1858 CG2 ILE B 163 12326 10203 12332 -46 -2182 665 C ATOM 1859 CD1 ILE B 163 17.905 -17.264 -10.229 1.00102.64 C ANISOU 1859 CD1 ILE B 163 13819 11211 13969 150 -2610 766 C ATOM 1860 N VAL B 164 14.439 -13.742 -7.197 1.00 88.58 N ANISOU 1860 N VAL B 164 12443 9883 11332 -351 -2058 844 N ATOM 1861 CA VAL B 164 13.303 -12.819 -7.046 1.00 87.27 C ANISOU 1861 CA VAL B 164 12271 9840 11048 -446 -1805 816 C ATOM 1862 C VAL B 164 13.622 -11.660 -6.045 1.00 91.18 C ANISOU 1862 C VAL B 164 12862 10394 11389 -471 -1812 773 C ATOM 1863 O VAL B 164 13.480 -10.509 -6.467 1.00 89.48 O ANISOU 1863 O VAL B 164 12499 10276 11223 -447 -1678 677 O ATOM 1864 CB VAL B 164 11.968 -13.558 -6.732 1.00 91.60 C ANISOU 1864 CB VAL B 164 12954 10376 11475 -579 -1650 911 C ATOM 1865 CG1 VAL B 164 10.841 -12.586 -6.385 1.00 91.14 C ANISOU 1865 CG1 VAL B 164 12890 10439 11299 -669 -1388 883 C ATOM 1866 CG2 VAL B 164 11.557 -14.449 -7.900 1.00 90.49 C ANISOU 1866 CG2 VAL B 164 12684 10198 11501 -565 -1615 923 C ATOM 1867 N PRO B 165 14.099 -11.885 -4.784 1.00 89.21 N ANISOU 1867 N PRO B 165 12859 10079 10958 -516 -1978 837 N ATOM 1868 CA PRO B 165 14.407 -10.736 -3.907 1.00 89.38 C ANISOU 1868 CA PRO B 165 12978 10154 10827 -550 -1987 779 C ATOM 1869 C PRO B 165 15.572 -9.875 -4.399 1.00 91.54 C ANISOU 1869 C PRO B 165 13057 10457 11267 -444 -2115 672 C ATOM 1870 O PRO B 165 15.597 -8.681 -4.111 1.00 90.98 O ANISOU 1870 O PRO B 165 12983 10454 11131 -467 -2038 588 O ATOM 1871 CB PRO B 165 14.727 -11.386 -2.554 1.00 93.68 C ANISOU 1871 CB PRO B 165 13846 10605 11143 -626 -2180 887 C ATOM 1872 CG PRO B 165 14.200 -12.776 -2.645 1.00 98.80 C ANISOU 1872 CG PRO B 165 14584 11164 11789 -661 -2185 1010 C ATOM 1873 CD PRO B 165 14.357 -13.156 -4.077 1.00 92.56 C ANISOU 1873 CD PRO B 165 13506 10371 11290 -548 -2172 967 C ATOM 1874 N LEU B 166 16.520 -10.476 -5.149 1.00 87.12 N ANISOU 1874 N LEU B 166 12333 9840 10928 -332 -2294 669 N ATOM 1875 CA LEU B 166 17.689 -9.798 -5.715 1.00 86.11 C ANISOU 1875 CA LEU B 166 11988 9735 10994 -234 -2410 571 C ATOM 1876 C LEU B 166 17.273 -8.797 -6.800 1.00 87.28 C ANISOU 1876 C LEU B 166 11913 9987 11263 -210 -2173 464 C ATOM 1877 O LEU B 166 17.789 -7.680 -6.821 1.00 86.49 O ANISOU 1877 O LEU B 166 11729 9938 11195 -201 -2173 376 O ATOM 1878 CB LEU B 166 18.686 -10.838 -6.283 1.00 86.65 C ANISOU 1878 CB LEU B 166 11933 9708 11283 -117 -2620 598 C ATOM 1879 CG LEU B 166 20.213 -10.590 -6.146 1.00 92.62 C ANISOU 1879 CG LEU B 166 12572 10433 12188 -31 -2882 555 C ATOM 1880 CD1 LEU B 166 20.728 -9.540 -7.128 1.00 91.44 C ANISOU 1880 CD1 LEU B 166 12143 10369 12230 21 -2779 422 C ATOM 1881 CD2 LEU B 166 20.645 -10.326 -4.701 1.00 97.09 C ANISOU 1881 CD2 LEU B 166 13365 10972 12554 -101 -3098 603 C ATOM 1882 N VAL B 167 16.329 -9.197 -7.681 1.00 82.17 N ANISOU 1882 N VAL B 167 11182 9363 10676 -210 -1986 478 N ATOM 1883 CA VAL B 167 15.797 -8.385 -8.784 1.00 79.95 C ANISOU 1883 CA VAL B 167 10706 9171 10502 -190 -1773 400 C ATOM 1884 C VAL B 167 15.030 -7.165 -8.252 1.00 83.35 C ANISOU 1884 C VAL B 167 11199 9679 10791 -258 -1596 361 C ATOM 1885 O VAL B 167 15.218 -6.058 -8.764 1.00 82.10 O ANISOU 1885 O VAL B 167 10910 9575 10711 -228 -1518 275 O ATOM 1886 CB VAL B 167 14.973 -9.247 -9.782 1.00 82.97 C ANISOU 1886 CB VAL B 167 11010 9547 10969 -186 -1659 437 C ATOM 1887 CG1 VAL B 167 14.181 -8.390 -10.766 1.00 81.17 C ANISOU 1887 CG1 VAL B 167 10623 9412 10805 -188 -1445 380 C ATOM 1888 CG2 VAL B 167 15.877 -10.217 -10.534 1.00 82.86 C ANISOU 1888 CG2 VAL B 167 10900 9453 11131 -97 -1807 434 C ATOM 1889 N TRP B 168 14.196 -7.367 -7.210 1.00 80.58 N ANISOU 1889 N TRP B 168 11060 9324 10235 -350 -1525 422 N ATOM 1890 CA TRP B 168 13.427 -6.300 -6.565 1.00 80.47 C ANISOU 1890 CA TRP B 168 11133 9368 10075 -412 -1338 380 C ATOM 1891 C TRP B 168 14.345 -5.296 -5.863 1.00 85.14 C ANISOU 1891 C TRP B 168 11799 9953 10596 -414 -1446 305 C ATOM 1892 O TRP B 168 14.043 -4.101 -5.854 1.00 84.61 O ANISOU 1892 O TRP B 168 11705 9932 10512 -419 -1299 224 O ATOM 1893 CB TRP B 168 12.386 -6.875 -5.595 1.00 80.42 C ANISOU 1893 CB TRP B 168 11343 9351 9863 -519 -1226 462 C ATOM 1894 CG TRP B 168 11.150 -7.386 -6.275 1.00 80.53 C ANISOU 1894 CG TRP B 168 11252 9401 9947 -542 -1035 509 C ATOM 1895 CD1 TRP B 168 10.807 -8.689 -6.479 1.00 83.67 C ANISOU 1895 CD1 TRP B 168 11677 9752 10363 -576 -1074 604 C ATOM 1896 CD2 TRP B 168 10.103 -6.598 -6.857 1.00 79.43 C ANISOU 1896 CD2 TRP B 168 10957 9342 9880 -536 -792 464 C ATOM 1897 NE1 TRP B 168 9.605 -8.764 -7.144 1.00 82.43 N ANISOU 1897 NE1 TRP B 168 11387 9651 10282 -606 -874 618 N ATOM 1898 CE2 TRP B 168 9.150 -7.495 -7.389 1.00 83.07 C ANISOU 1898 CE2 TRP B 168 11346 9813 10403 -576 -704 537 C ATOM 1899 CE3 TRP B 168 9.875 -5.216 -6.983 1.00 80.16 C ANISOU 1899 CE3 TRP B 168 10964 9491 10002 -499 -649 372 C ATOM 1900 CZ2 TRP B 168 7.987 -7.057 -8.034 1.00 81.69 C ANISOU 1900 CZ2 TRP B 168 11001 9712 10325 -579 -494 525 C ATOM 1901 CZ3 TRP B 168 8.721 -4.783 -7.617 1.00 80.99 C ANISOU 1901 CZ3 TRP B 168 10909 9658 10204 -489 -435 363 C ATOM 1902 CH2 TRP B 168 7.794 -5.697 -8.139 1.00 81.46 C ANISOU 1902 CH2 TRP B 168 10882 9737 10331 -528 -367 441 C ATOM 1903 N CYS B 169 15.475 -5.778 -5.306 1.00 82.63 N ANISOU 1903 N CYS B 169 11570 9572 10253 -407 -1713 331 N ATOM 1904 CA CYS B 169 16.476 -4.939 -4.649 1.00 83.48 C ANISOU 1904 CA CYS B 169 11741 9668 10309 -420 -1870 264 C ATOM 1905 C CYS B 169 17.303 -4.172 -5.683 1.00 85.65 C ANISOU 1905 C CYS B 169 11752 9972 10820 -340 -1897 171 C ATOM 1906 O CYS B 169 17.692 -3.032 -5.420 1.00 85.49 O ANISOU 1906 O CYS B 169 11737 9968 10776 -365 -1896 85 O ATOM 1907 CB CYS B 169 17.356 -5.758 -3.711 1.00 85.85 C ANISOU 1907 CB CYS B 169 12216 9890 10514 -441 -2169 338 C ATOM 1908 SG CYS B 169 16.556 -6.198 -2.145 1.00 92.03 S ANISOU 1908 SG CYS B 169 13399 10636 10932 -578 -2144 427 S ATOM 1909 N MET B 170 17.546 -4.787 -6.865 1.00 80.64 N ANISOU 1909 N MET B 170 10900 9337 10403 -257 -1907 184 N ATOM 1910 CA MET B 170 18.270 -4.170 -7.983 1.00 79.22 C ANISOU 1910 CA MET B 170 10467 9184 10447 -188 -1898 102 C ATOM 1911 C MET B 170 17.440 -3.020 -8.561 1.00 81.19 C ANISOU 1911 C MET B 170 10649 9498 10703 -201 -1646 40 C ATOM 1912 O MET B 170 18.002 -1.992 -8.939 1.00 80.50 O ANISOU 1912 O MET B 170 10455 9427 10704 -192 -1631 -41 O ATOM 1913 CB MET B 170 18.581 -5.199 -9.081 1.00 80.88 C ANISOU 1913 CB MET B 170 10504 9372 10854 -105 -1933 130 C ATOM 1914 CG MET B 170 19.838 -6.005 -8.825 1.00 85.97 C ANISOU 1914 CG MET B 170 11116 9948 11603 -51 -2199 152 C ATOM 1915 SD MET B 170 20.452 -6.862 -10.302 1.00 89.55 S ANISOU 1915 SD MET B 170 11317 10371 12335 65 -2201 131 S ATOM 1916 CE MET B 170 19.268 -8.198 -10.438 1.00 85.88 C ANISOU 1916 CE MET B 170 10983 9863 11785 56 -2123 231 C ATOM 1917 N ALA B 171 16.103 -3.198 -8.609 1.00 76.69 N ANISOU 1917 N ALA B 171 10136 8954 10046 -225 -1454 83 N ATOM 1918 CA ALA B 171 15.139 -2.207 -9.088 1.00 75.25 C ANISOU 1918 CA ALA B 171 9894 8823 9874 -226 -1218 43 C ATOM 1919 C ALA B 171 15.020 -1.053 -8.089 1.00 79.71 C ANISOU 1919 C ALA B 171 10606 9385 10294 -277 -1157 -20 C ATOM 1920 O ALA B 171 14.801 0.089 -8.497 1.00 78.71 O ANISOU 1920 O ALA B 171 10409 9275 10221 -260 -1028 -86 O ATOM 1921 CB ALA B 171 13.783 -2.861 -9.293 1.00 75.54 C ANISOU 1921 CB ALA B 171 9941 8886 9874 -242 -1060 114 C ATOM 1922 N CYS B 172 15.176 -1.355 -6.784 1.00 77.68 N ANISOU 1922 N CYS B 172 10574 9095 9845 -342 -1254 0 N ATOM 1923 CA CYS B 172 15.122 -0.375 -5.700 1.00 78.76 C ANISOU 1923 CA CYS B 172 10903 9216 9805 -406 -1211 -67 C ATOM 1924 C CYS B 172 16.387 0.488 -5.681 1.00 82.69 C ANISOU 1924 C CYS B 172 11361 9689 10369 -409 -1373 -152 C ATOM 1925 O CYS B 172 16.291 1.700 -5.479 1.00 82.36 O ANISOU 1925 O CYS B 172 11363 9638 10291 -431 -1272 -240 O ATOM 1926 CB CYS B 172 14.887 -1.059 -4.357 1.00 80.91 C ANISOU 1926 CB CYS B 172 11453 9459 9829 -490 -1269 -10 C ATOM 1927 SG CYS B 172 14.546 0.085 -2.995 1.00 86.75 S ANISOU 1927 SG CYS B 172 12479 10178 10305 -583 -1152 -100 S ATOM 1928 N LEU B 173 17.566 -0.138 -5.900 1.00 79.27 N ANISOU 1928 N LEU B 173 10835 9237 10046 -385 -1620 -128 N ATOM 1929 CA LEU B 173 18.865 0.539 -5.951 1.00 79.46 C ANISOU 1929 CA LEU B 173 10775 9242 10173 -393 -1795 -201 C ATOM 1930 C LEU B 173 18.964 1.452 -7.178 1.00 81.57 C ANISOU 1930 C LEU B 173 10817 9535 10640 -348 -1657 -268 C ATOM 1931 O LEU B 173 19.570 2.521 -7.093 1.00 81.61 O ANISOU 1931 O LEU B 173 10809 9523 10677 -386 -1685 -352 O ATOM 1932 CB LEU B 173 20.016 -0.482 -5.952 1.00 80.21 C ANISOU 1932 CB LEU B 173 10790 9312 10376 -362 -2076 -150 C ATOM 1933 CG LEU B 173 20.441 -1.031 -4.588 1.00 87.13 C ANISOU 1933 CG LEU B 173 11900 10141 11063 -424 -2317 -101 C ATOM 1934 CD1 LEU B 173 20.984 -2.437 -4.713 1.00 87.63 C ANISOU 1934 CD1 LEU B 173 11901 10170 11225 -361 -2520 -4 C ATOM 1935 CD2 LEU B 173 21.482 -0.135 -3.928 1.00 91.38 C ANISOU 1935 CD2 LEU B 173 12484 10658 11578 -491 -2510 -178 C ATOM 1936 N SER B 174 18.352 1.033 -8.306 1.00 76.21 N ANISOU 1936 N SER B 174 9982 8890 10085 -280 -1513 -228 N ATOM 1937 CA SER B 174 18.322 1.783 -9.566 1.00 74.42 C ANISOU 1937 CA SER B 174 9563 8684 10027 -240 -1375 -270 C ATOM 1938 C SER B 174 17.384 2.992 -9.484 1.00 77.83 C ANISOU 1938 C SER B 174 10068 9114 10389 -255 -1166 -315 C ATOM 1939 O SER B 174 17.549 3.942 -10.253 1.00 76.70 O ANISOU 1939 O SER B 174 9818 8964 10358 -243 -1086 -363 O ATOM 1940 CB SER B 174 17.910 0.875 -10.719 1.00 76.25 C ANISOU 1940 CB SER B 174 9646 8947 10377 -174 -1308 -208 C ATOM 1941 OG SER B 174 18.799 -0.221 -10.861 1.00 84.21 O ANISOU 1941 OG SER B 174 10582 9941 11473 -144 -1485 -178 O ATOM 1942 N SER B 175 16.402 2.953 -8.559 1.00 75.06 N ANISOU 1942 N SER B 175 9900 8761 9859 -282 -1068 -299 N ATOM 1943 CA SER B 175 15.433 4.028 -8.339 1.00 75.18 C ANISOU 1943 CA SER B 175 9992 8762 9810 -283 -854 -346 C ATOM 1944 C SER B 175 15.899 5.046 -7.275 1.00 80.46 C ANISOU 1944 C SER B 175 10847 9374 10350 -351 -890 -442 C ATOM 1945 O SER B 175 15.163 5.990 -6.977 1.00 80.61 O ANISOU 1945 O SER B 175 10956 9364 10311 -350 -709 -499 O ATOM 1946 CB SER B 175 14.063 3.453 -7.989 1.00 79.24 C ANISOU 1946 CB SER B 175 10579 9306 10223 -274 -690 -286 C ATOM 1947 OG SER B 175 14.090 2.755 -6.755 1.00 90.61 O ANISOU 1947 OG SER B 175 12226 10736 11466 -340 -768 -262 O ATOM 1948 N LEU B 176 17.117 4.857 -6.713 1.00 77.72 N ANISOU 1948 N LEU B 176 10555 9006 9968 -410 -1128 -465 N ATOM 1949 CA LEU B 176 17.707 5.756 -5.714 1.00 79.06 C ANISOU 1949 CA LEU B 176 10906 9119 10012 -495 -1212 -558 C ATOM 1950 C LEU B 176 18.002 7.175 -6.256 1.00 82.23 C ANISOU 1950 C LEU B 176 11237 9476 10532 -500 -1133 -652 C ATOM 1951 O LEU B 176 17.644 8.127 -5.555 1.00 82.79 O ANISOU 1951 O LEU B 176 11489 9490 10478 -541 -1032 -734 O ATOM 1952 CB LEU B 176 18.953 5.152 -5.039 1.00 80.40 C ANISOU 1952 CB LEU B 176 11129 9280 10140 -558 -1522 -546 C ATOM 1953 CG LEU B 176 18.707 4.168 -3.889 1.00 86.41 C ANISOU 1953 CG LEU B 176 12116 10041 10676 -601 -1623 -482 C ATOM 1954 CD1 LEU B 176 19.954 3.369 -3.591 1.00 87.49 C ANISOU 1954 CD1 LEU B 176 12221 10170 10851 -623 -1955 -437 C ATOM 1955 CD2 LEU B 176 18.249 4.886 -2.621 1.00 90.60 C ANISOU 1955 CD2 LEU B 176 12960 10526 10936 -692 -1547 -553 C ATOM 1956 N PRO B 177 18.589 7.380 -7.477 1.00 77.31 N ANISOU 1956 N PRO B 177 10374 8865 10133 -463 -1153 -646 N ATOM 1957 CA PRO B 177 18.806 8.760 -7.960 1.00 77.00 C ANISOU 1957 CA PRO B 177 10297 8769 10190 -481 -1066 -725 C ATOM 1958 C PRO B 177 17.501 9.512 -8.229 1.00 80.12 C ANISOU 1958 C PRO B 177 10738 9133 10570 -418 -800 -735 C ATOM 1959 O PRO B 177 17.490 10.743 -8.187 1.00 80.64 O ANISOU 1959 O PRO B 177 10870 9120 10648 -440 -717 -813 O ATOM 1960 CB PRO B 177 19.623 8.570 -9.246 1.00 77.62 C ANISOU 1960 CB PRO B 177 10115 8879 10496 -457 -1127 -694 C ATOM 1961 CG PRO B 177 20.145 7.175 -9.184 1.00 82.01 C ANISOU 1961 CG PRO B 177 10591 9496 11073 -440 -1299 -628 C ATOM 1962 CD PRO B 177 19.088 6.405 -8.469 1.00 77.63 C ANISOU 1962 CD PRO B 177 10190 8963 10344 -411 -1241 -572 C ATOM 1963 N THR B 178 16.401 8.773 -8.483 1.00 75.21 N ANISOU 1963 N THR B 178 10078 8565 9932 -342 -673 -656 N ATOM 1964 CA THR B 178 15.067 9.329 -8.703 1.00 74.73 C ANISOU 1964 CA THR B 178 10030 8485 9878 -270 -431 -652 C ATOM 1965 C THR B 178 14.548 9.927 -7.384 1.00 80.34 C ANISOU 1965 C THR B 178 10989 9137 10401 -305 -326 -736 C ATOM 1966 O THR B 178 14.023 11.036 -7.392 1.00 80.57 O ANISOU 1966 O THR B 178 11067 9092 10455 -271 -164 -799 O ATOM 1967 CB THR B 178 14.118 8.266 -9.288 1.00 82.12 C ANISOU 1967 CB THR B 178 10843 9503 10857 -200 -355 -544 C ATOM 1968 OG1 THR B 178 14.768 7.573 -10.356 1.00 80.70 O ANISOU 1968 OG1 THR B 178 10479 9371 10812 -186 -477 -482 O ATOM 1969 CG2 THR B 178 12.807 8.860 -9.784 1.00 80.38 C ANISOU 1969 CG2 THR B 178 10563 9268 10707 -114 -132 -526 C ATOM 1970 N PHE B 179 14.735 9.211 -6.256 1.00 77.82 N ANISOU 1970 N PHE B 179 10839 8838 9891 -374 -419 -739 N ATOM 1971 CA PHE B 179 14.320 9.660 -4.923 1.00 79.58 C ANISOU 1971 CA PHE B 179 11336 9007 9892 -428 -325 -822 C ATOM 1972 C PHE B 179 15.153 10.848 -4.428 1.00 84.52 C ANISOU 1972 C PHE B 179 12108 9534 10469 -505 -399 -948 C ATOM 1973 O PHE B 179 14.648 11.672 -3.664 1.00 85.65 O ANISOU 1973 O PHE B 179 12454 9602 10487 -522 -245 -1046 O ATOM 1974 CB PHE B 179 14.394 8.497 -3.915 1.00 82.32 C ANISOU 1974 CB PHE B 179 11844 9401 10032 -498 -436 -774 C ATOM 1975 CG PHE B 179 13.728 8.764 -2.584 1.00 86.07 C ANISOU 1975 CG PHE B 179 12616 9836 10251 -556 -288 -843 C ATOM 1976 CD1 PHE B 179 12.352 8.628 -2.436 1.00 89.50 C ANISOU 1976 CD1 PHE B 179 13066 10292 10650 -503 -9 -825 C ATOM 1977 CD2 PHE B 179 14.479 9.133 -1.474 1.00 90.26 C ANISOU 1977 CD2 PHE B 179 13412 10308 10574 -671 -428 -928 C ATOM 1978 CE1 PHE B 179 11.737 8.875 -1.204 1.00 92.69 C ANISOU 1978 CE1 PHE B 179 13748 10657 10812 -560 162 -898 C ATOM 1979 CE2 PHE B 179 13.863 9.380 -0.243 1.00 95.36 C ANISOU 1979 CE2 PHE B 179 14365 10913 10956 -734 -275 -1000 C ATOM 1980 CZ PHE B 179 12.497 9.248 -0.116 1.00 93.71 C ANISOU 1980 CZ PHE B 179 14169 10724 10711 -677 33 -988 C ATOM 1981 N TYR B 180 16.422 10.928 -4.863 1.00 80.39 N ANISOU 1981 N TYR B 180 11482 9010 10054 -555 -624 -952 N ATOM 1982 CA TYR B 180 17.368 11.972 -4.471 1.00 81.42 C ANISOU 1982 CA TYR B 180 11720 9051 10163 -651 -737 -1063 C ATOM 1983 C TYR B 180 17.216 13.277 -5.256 1.00 84.62 C ANISOU 1983 C TYR B 180 12053 9371 10729 -612 -589 -1121 C ATOM 1984 O TYR B 180 17.361 14.349 -4.665 1.00 85.77 O ANISOU 1984 O TYR B 180 12381 9408 10799 -673 -554 -1237 O ATOM 1985 CB TYR B 180 18.811 11.442 -4.580 1.00 82.58 C ANISOU 1985 CB TYR B 180 11758 9237 10380 -727 -1047 -1036 C ATOM 1986 CG TYR B 180 19.850 12.296 -3.885 1.00 86.22 C ANISOU 1986 CG TYR B 180 12359 9620 10782 -861 -1220 -1146 C ATOM 1987 CD1 TYR B 180 20.113 12.141 -2.527 1.00 90.39 C ANISOU 1987 CD1 TYR B 180 13156 10125 11065 -964 -1364 -1194 C ATOM 1988 CD2 TYR B 180 20.606 13.225 -4.594 1.00 86.87 C ANISOU 1988 CD2 TYR B 180 12310 9650 11048 -899 -1254 -1197 C ATOM 1989 CE1 TYR B 180 21.078 12.915 -1.883 1.00 93.42 C ANISOU 1989 CE1 TYR B 180 13672 10435 11388 -1102 -1550 -1298 C ATOM 1990 CE2 TYR B 180 21.573 14.006 -3.961 1.00 89.78 C ANISOU 1990 CE2 TYR B 180 12797 9943 11373 -1039 -1424 -1300 C ATOM 1991 CZ TYR B 180 21.807 13.846 -2.605 1.00 99.75 C ANISOU 1991 CZ TYR B 180 14323 11185 12393 -1140 -1581 -1352 C ATOM 1992 OH TYR B 180 22.760 14.610 -1.975 1.00103.08 O ANISOU 1992 OH TYR B 180 14868 11532 12766 -1292 -1772 -1455 O ATOM 1993 N PHE B 181 16.955 13.198 -6.579 1.00 79.03 N ANISOU 1993 N PHE B 181 11099 8698 10231 -519 -513 -1041 N ATOM 1994 CA PHE B 181 16.885 14.386 -7.429 1.00 78.36 C ANISOU 1994 CA PHE B 181 10943 8526 10304 -485 -399 -1072 C ATOM 1995 C PHE B 181 15.474 14.924 -7.719 1.00 81.63 C ANISOU 1995 C PHE B 181 11368 8893 10756 -360 -133 -1062 C ATOM 1996 O PHE B 181 15.354 16.136 -7.888 1.00 82.23 O ANISOU 1996 O PHE B 181 11503 8848 10893 -347 -33 -1127 O ATOM 1997 CB PHE B 181 17.653 14.170 -8.741 1.00 78.61 C ANISOU 1997 CB PHE B 181 10723 8605 10541 -483 -497 -999 C ATOM 1998 CG PHE B 181 19.153 14.088 -8.562 1.00 80.72 C ANISOU 1998 CG PHE B 181 10954 8881 10837 -607 -733 -1036 C ATOM 1999 CD1 PHE B 181 19.897 15.221 -8.248 1.00 85.21 C ANISOU 1999 CD1 PHE B 181 11618 9344 11415 -714 -787 -1138 C ATOM 2000 CD2 PHE B 181 19.824 12.882 -8.723 1.00 82.07 C ANISOU 2000 CD2 PHE B 181 10982 9157 11044 -617 -904 -970 C ATOM 2001 CE1 PHE B 181 21.283 15.144 -8.081 1.00 86.89 C ANISOU 2001 CE1 PHE B 181 11767 9570 11678 -837 -1016 -1171 C ATOM 2002 CE2 PHE B 181 21.211 12.807 -8.559 1.00 85.66 C ANISOU 2002 CE2 PHE B 181 11370 9619 11559 -721 -1127 -1004 C ATOM 2003 CZ PHE B 181 21.930 13.938 -8.237 1.00 85.28 C ANISOU 2003 CZ PHE B 181 11400 9479 11525 -834 -1184 -1102 C ATOM 2004 N ARG B 182 14.423 14.070 -7.776 1.00 76.84 N ANISOU 2004 N ARG B 182 10698 8370 10128 -271 -23 -984 N ATOM 2005 CA ARG B 182 13.049 14.541 -8.044 1.00 76.54 C ANISOU 2005 CA ARG B 182 10633 8295 10156 -146 221 -970 C ATOM 2006 C ARG B 182 12.531 15.463 -6.938 1.00 82.57 C ANISOU 2006 C ARG B 182 11634 8944 10795 -146 387 -1098 C ATOM 2007 O ARG B 182 12.613 15.113 -5.761 1.00 83.21 O ANISOU 2007 O ARG B 182 11908 9038 10671 -220 375 -1159 O ATOM 2008 CB ARG B 182 12.063 13.377 -8.273 1.00 74.87 C ANISOU 2008 CB ARG B 182 10293 8203 9953 -74 292 -862 C ATOM 2009 CG ARG B 182 12.170 12.706 -9.639 1.00 79.98 C ANISOU 2009 CG ARG B 182 10694 8934 10762 -33 203 -738 C ATOM 2010 CD ARG B 182 11.241 13.319 -10.669 1.00 84.69 C ANISOU 2010 CD ARG B 182 11151 9496 11533 84 340 -684 C ATOM 2011 NE ARG B 182 11.704 13.064 -12.033 1.00 86.39 N ANISOU 2011 NE ARG B 182 11189 9753 11884 89 229 -595 N ATOM 2012 CZ ARG B 182 11.151 13.586 -13.123 1.00 96.57 C ANISOU 2012 CZ ARG B 182 12362 11010 13320 170 288 -531 C ATOM 2013 NH1 ARG B 182 10.104 14.395 -13.022 1.00 84.41 N ANISOU 2013 NH1 ARG B 182 10836 9393 11841 268 446 -541 N ATOM 2014 NH2 ARG B 182 11.642 13.306 -14.322 1.00 80.11 N ANISOU 2014 NH2 ARG B 182 10151 8964 11322 155 188 -456 N ATOM 2015 N ASP B 183 12.038 16.658 -7.323 1.00 79.89 N ANISOU 2015 N ASP B 183 11297 8480 10575 -65 538 -1142 N ATOM 2016 CA ASP B 183 11.487 17.680 -6.424 1.00 81.92 C ANISOU 2016 CA ASP B 183 11770 8600 10754 -40 729 -1276 C ATOM 2017 C ASP B 183 10.678 18.702 -7.218 1.00 85.84 C ANISOU 2017 C ASP B 183 12173 8983 11459 105 898 -1265 C ATOM 2018 O ASP B 183 11.016 18.992 -8.367 1.00 84.01 O ANISOU 2018 O ASP B 183 11789 8734 11397 129 810 -1187 O ATOM 2019 CB ASP B 183 12.601 18.388 -5.625 1.00 85.26 C ANISOU 2019 CB ASP B 183 12435 8921 11040 -185 609 -1410 C ATOM 2020 CG ASP B 183 12.103 19.172 -4.424 1.00 98.57 C ANISOU 2020 CG ASP B 183 14405 10480 12568 -191 794 -1568 C ATOM 2021 OD1 ASP B 183 11.571 18.543 -3.481 1.00 99.79 O ANISOU 2021 OD1 ASP B 183 14683 10693 12539 -205 887 -1595 O ATOM 2022 OD2 ASP B 183 12.272 20.410 -4.413 1.00106.91 O ANISOU 2022 OD2 ASP B 183 15579 11369 13675 -191 850 -1669 O ATOM 2023 N VAL B 184 9.617 19.252 -6.602 1.00 84.34 N ANISOU 2023 N VAL B 184 12078 8708 11258 202 1144 -1343 N ATOM 2024 CA VAL B 184 8.757 20.256 -7.233 1.00 84.93 C ANISOU 2024 CA VAL B 184 12071 8655 11543 362 1312 -1338 C ATOM 2025 C VAL B 184 9.478 21.606 -7.259 1.00 90.11 C ANISOU 2025 C VAL B 184 12892 9115 12232 322 1280 -1438 C ATOM 2026 O VAL B 184 9.830 22.145 -6.207 1.00 91.28 O ANISOU 2026 O VAL B 184 13300 9163 12221 241 1325 -1591 O ATOM 2027 CB VAL B 184 7.343 20.339 -6.588 1.00 90.54 C ANISOU 2027 CB VAL B 184 12792 9342 12266 495 1602 -1387 C ATOM 2028 CG1 VAL B 184 6.501 21.443 -7.227 1.00 91.49 C ANISOU 2028 CG1 VAL B 184 12819 9309 12633 676 1757 -1383 C ATOM 2029 CG2 VAL B 184 6.617 19.004 -6.681 1.00 89.21 C ANISOU 2029 CG2 VAL B 184 12437 9367 12094 520 1628 -1273 C ATOM 2030 N ARG B 185 9.720 22.125 -8.473 1.00 86.16 N ANISOU 2030 N ARG B 185 12255 8557 11924 363 1196 -1349 N ATOM 2031 CA ARG B 185 10.380 23.411 -8.703 1.00 87.22 C ANISOU 2031 CA ARG B 185 12522 8496 12122 322 1161 -1416 C ATOM 2032 C ARG B 185 9.515 24.272 -9.614 1.00 92.26 C ANISOU 2032 C ARG B 185 13059 9001 12996 499 1277 -1348 C ATOM 2033 O ARG B 185 8.963 23.769 -10.596 1.00 90.32 O ANISOU 2033 O ARG B 185 12582 8850 12885 594 1250 -1195 O ATOM 2034 CB ARG B 185 11.793 23.225 -9.297 1.00 86.17 C ANISOU 2034 CB ARG B 185 12349 8414 11978 156 913 -1368 C ATOM 2035 CG ARG B 185 12.795 22.526 -8.370 1.00 96.97 C ANISOU 2035 CG ARG B 185 13824 9883 13136 -22 761 -1441 C ATOM 2036 CD ARG B 185 13.365 23.444 -7.301 1.00108.88 C ANISOU 2036 CD ARG B 185 15623 11235 14511 -136 765 -1620 C ATOM 2037 NE ARG B 185 13.924 22.690 -6.179 1.00117.70 N ANISOU 2037 NE ARG B 185 16872 12453 15397 -270 653 -1690 N ATOM 2038 CZ ARG B 185 15.209 22.377 -6.043 1.00132.66 C ANISOU 2038 CZ ARG B 185 18775 14404 17226 -442 411 -1699 C ATOM 2039 NH1 ARG B 185 15.624 21.689 -4.989 1.00121.72 N ANISOU 2039 NH1 ARG B 185 17520 13100 15628 -549 298 -1753 N ATOM 2040 NH2 ARG B 185 16.092 22.753 -6.963 1.00118.61 N ANISOU 2040 NH2 ARG B 185 16871 12598 15599 -509 280 -1651 N ATOM 2041 N THR B 186 9.384 25.564 -9.274 1.00 91.78 N ANISOU 2041 N THR B 186 13181 8710 12981 544 1396 -1461 N ATOM 2042 CA THR B 186 8.572 26.519 -10.028 1.00 93.05 C ANISOU 2042 CA THR B 186 13281 8702 13373 724 1503 -1407 C ATOM 2043 C THR B 186 9.199 26.892 -11.366 1.00 96.87 C ANISOU 2043 C THR B 186 13676 9141 13989 685 1332 -1271 C ATOM 2044 O THR B 186 10.356 27.316 -11.413 1.00 96.62 O ANISOU 2044 O THR B 186 13768 9045 13897 520 1211 -1314 O ATOM 2045 CB THR B 186 8.238 27.762 -9.188 1.00104.00 C ANISOU 2045 CB THR B 186 14911 9836 14767 789 1694 -1581 C ATOM 2046 OG1 THR B 186 9.445 28.326 -8.675 1.00104.93 O ANISOU 2046 OG1 THR B 186 15275 9851 14744 595 1596 -1705 O ATOM 2047 CG2 THR B 186 7.265 27.466 -8.054 1.00103.97 C ANISOU 2047 CG2 THR B 186 14961 9862 14681 883 1930 -1696 C ATOM 2048 N ILE B 187 8.426 26.720 -12.452 1.00 93.30 N ANISOU 2048 N ILE B 187 13010 8727 13714 828 1322 -1105 N ATOM 2049 CA ILE B 187 8.820 27.074 -13.816 1.00 92.63 C ANISOU 2049 CA ILE B 187 12849 8596 13751 810 1182 -956 C ATOM 2050 C ILE B 187 8.389 28.538 -13.986 1.00 99.78 C ANISOU 2050 C ILE B 187 13882 9213 14814 932 1279 -980 C ATOM 2051 O ILE B 187 7.191 28.827 -14.018 1.00100.72 O ANISOU 2051 O ILE B 187 13926 9260 15083 1140 1404 -953 O ATOM 2052 CB ILE B 187 8.181 26.116 -14.873 1.00 94.00 C ANISOU 2052 CB ILE B 187 12755 8951 14008 893 1104 -766 C ATOM 2053 CG1 ILE B 187 8.355 24.604 -14.509 1.00 92.41 C ANISOU 2053 CG1 ILE B 187 12435 9016 13660 807 1049 -760 C ATOM 2054 CG2 ILE B 187 8.674 26.419 -16.291 1.00 94.05 C ANISOU 2054 CG2 ILE B 187 12717 8919 14097 847 956 -614 C ATOM 2055 CD1 ILE B 187 9.821 24.013 -14.407 1.00 97.74 C ANISOU 2055 CD1 ILE B 187 13161 9803 14172 584 895 -795 C ATOM 2056 N GLU B 188 9.373 29.456 -14.020 1.00 97.64 N ANISOU 2056 N GLU B 188 13807 8773 14520 800 1226 -1040 N ATOM 2057 CA GLU B 188 9.176 30.906 -14.097 1.00100.16 C ANISOU 2057 CA GLU B 188 14300 8787 14969 880 1306 -1081 C ATOM 2058 C GLU B 188 8.370 31.388 -15.311 1.00104.75 C ANISOU 2058 C GLU B 188 14768 9262 15770 1058 1285 -898 C ATOM 2059 O GLU B 188 7.458 32.200 -15.137 1.00106.50 O ANISOU 2059 O GLU B 188 15035 9287 16144 1252 1414 -924 O ATOM 2060 CB GLU B 188 10.523 31.639 -14.024 1.00102.12 C ANISOU 2060 CB GLU B 188 14759 8903 15140 658 1218 -1159 C ATOM 2061 N TYR B 189 8.702 30.903 -16.526 1.00 99.62 N ANISOU 2061 N TYR B 189 13982 8734 15136 994 1123 -716 N ATOM 2062 CA TYR B 189 8.027 31.321 -17.758 1.00 99.96 C ANISOU 2062 CA TYR B 189 13941 8683 15357 1135 1064 -523 C ATOM 2063 C TYR B 189 6.623 30.719 -17.917 1.00103.18 C ANISOU 2063 C TYR B 189 14117 9199 15888 1360 1103 -434 C ATOM 2064 O TYR B 189 5.697 31.448 -18.283 1.00104.76 O ANISOU 2064 O TYR B 189 14293 9226 16284 1560 1138 -362 O ATOM 2065 CB TYR B 189 8.899 31.080 -19.008 1.00 99.70 C ANISOU 2065 CB TYR B 189 13882 8726 15275 971 889 -368 C ATOM 2066 CG TYR B 189 9.283 29.641 -19.278 1.00 98.73 C ANISOU 2066 CG TYR B 189 13580 8914 15021 859 797 -318 C ATOM 2067 CD1 TYR B 189 10.393 29.067 -18.664 1.00 99.47 C ANISOU 2067 CD1 TYR B 189 13704 9139 14950 660 773 -435 C ATOM 2068 CD2 TYR B 189 8.598 28.882 -20.223 1.00 98.44 C ANISOU 2068 CD2 TYR B 189 13350 9023 15028 945 714 -149 C ATOM 2069 CE1 TYR B 189 10.780 27.757 -18.943 1.00 98.13 C ANISOU 2069 CE1 TYR B 189 13374 9234 14678 568 686 -388 C ATOM 2070 CE2 TYR B 189 8.975 27.571 -20.510 1.00 97.03 C ANISOU 2070 CE2 TYR B 189 13026 9110 14731 840 632 -109 C ATOM 2071 CZ TYR B 189 10.063 27.009 -19.863 1.00103.16 C ANISOU 2071 CZ TYR B 189 13833 10005 15357 659 625 -230 C ATOM 2072 OH TYR B 189 10.436 25.715 -20.139 1.00101.45 O ANISOU 2072 OH TYR B 189 13474 10031 15040 571 547 -194 O ATOM 2073 N LEU B 190 6.457 29.414 -17.624 1.00 97.06 N ANISOU 2073 N LEU B 190 13170 8696 15013 1328 1096 -439 N ATOM 2074 CA LEU B 190 5.160 28.736 -17.724 1.00 96.47 C ANISOU 2074 CA LEU B 190 12858 8745 15050 1510 1133 -361 C ATOM 2075 C LEU B 190 4.203 29.075 -16.576 1.00101.17 C ANISOU 2075 C LEU B 190 13455 9254 15733 1681 1356 -504 C ATOM 2076 O LEU B 190 2.991 28.910 -16.733 1.00101.66 O ANISOU 2076 O LEU B 190 13321 9340 15966 1873 1411 -435 O ATOM 2077 CB LEU B 190 5.335 27.213 -17.837 1.00 93.96 C ANISOU 2077 CB LEU B 190 12371 8734 14595 1402 1049 -315 C ATOM 2078 CG LEU B 190 5.608 26.659 -19.233 1.00 97.24 C ANISOU 2078 CG LEU B 190 12680 9266 15001 1332 851 -125 C ATOM 2079 CD1 LEU B 190 6.314 25.324 -19.155 1.00 94.84 C ANISOU 2079 CD1 LEU B 190 12305 9215 14514 1162 779 -138 C ATOM 2080 CD2 LEU B 190 4.321 26.518 -20.040 1.00100.98 C ANISOU 2080 CD2 LEU B 190 12953 9758 15655 1516 799 38 C ATOM 2081 N GLY B 191 4.753 29.535 -15.447 1.00 97.65 N ANISOU 2081 N GLY B 191 13225 8709 15169 1604 1483 -702 N ATOM 2082 CA GLY B 191 3.996 29.875 -14.243 1.00 99.03 C ANISOU 2082 CA GLY B 191 13455 8793 15379 1734 1725 -871 C ATOM 2083 C GLY B 191 3.335 28.649 -13.649 1.00100.27 C ANISOU 2083 C GLY B 191 13431 9196 15472 1756 1814 -891 C ATOM 2084 O GLY B 191 2.172 28.696 -13.237 1.00101.50 O ANISOU 2084 O GLY B 191 13468 9329 15767 1940 1994 -923 O ATOM 2085 N VAL B 192 4.079 27.531 -13.638 1.00 93.03 N ANISOU 2085 N VAL B 192 12481 8510 14354 1566 1688 -866 N ATOM 2086 CA VAL B 192 3.605 26.231 -13.187 1.00 90.99 C ANISOU 2086 CA VAL B 192 12064 8498 14010 1548 1732 -859 C ATOM 2087 C VAL B 192 4.583 25.567 -12.197 1.00 92.18 C ANISOU 2087 C VAL B 192 12379 8766 13878 1339 1720 -986 C ATOM 2088 O VAL B 192 5.787 25.826 -12.248 1.00 90.76 O ANISOU 2088 O VAL B 192 12360 8547 13580 1178 1591 -1022 O ATOM 2089 CB VAL B 192 3.279 25.363 -14.440 1.00 92.91 C ANISOU 2089 CB VAL B 192 12043 8914 14343 1566 1553 -645 C ATOM 2090 CG1 VAL B 192 4.404 24.397 -14.814 1.00 89.88 C ANISOU 2090 CG1 VAL B 192 11669 8713 13769 1353 1359 -594 C ATOM 2091 CG2 VAL B 192 1.952 24.644 -14.290 1.00 93.25 C ANISOU 2091 CG2 VAL B 192 11842 9084 14503 1702 1662 -598 C ATOM 2092 N ASN B 193 4.051 24.739 -11.283 1.00 88.07 N ANISOU 2092 N ASN B 193 11821 8384 13258 1339 1852 -1051 N ATOM 2093 CA ASN B 193 4.844 24.008 -10.294 1.00 86.62 C ANISOU 2093 CA ASN B 193 11792 8319 12802 1153 1831 -1154 C ATOM 2094 C ASN B 193 4.996 22.566 -10.778 1.00 86.53 C ANISOU 2094 C ASN B 193 11593 8556 12727 1068 1674 -1019 C ATOM 2095 O ASN B 193 4.092 21.749 -10.595 1.00 85.84 O ANISOU 2095 O ASN B 193 11353 8600 12663 1128 1766 -976 O ATOM 2096 CB ASN B 193 4.194 24.083 -8.902 1.00 89.84 C ANISOU 2096 CB ASN B 193 12332 8691 13110 1193 2094 -1319 C ATOM 2097 CG ASN B 193 4.203 25.460 -8.281 1.00116.16 C ANISOU 2097 CG ASN B 193 15905 11769 16462 1249 2253 -1486 C ATOM 2098 OD1 ASN B 193 3.869 26.470 -8.914 1.00111.89 O ANISOU 2098 OD1 ASN B 193 15331 11047 16135 1387 2281 -1459 O ATOM 2099 ND2 ASN B 193 4.549 25.524 -7.005 1.00109.89 N ANISOU 2099 ND2 ASN B 193 15373 10943 15436 1143 2361 -1663 N ATOM 2100 N ALA B 194 6.123 22.275 -11.447 1.00 80.37 N ANISOU 2100 N ALA B 194 10819 7834 11885 931 1447 -953 N ATOM 2101 CA ALA B 194 6.396 20.963 -12.031 1.00 77.47 C ANISOU 2101 CA ALA B 194 10288 7678 11468 852 1285 -830 C ATOM 2102 C ALA B 194 7.309 20.074 -11.199 1.00 79.42 C ANISOU 2102 C ALA B 194 10646 8045 11484 680 1202 -896 C ATOM 2103 O ALA B 194 8.307 20.546 -10.650 1.00 79.24 O ANISOU 2103 O ALA B 194 10817 7948 11344 566 1146 -1001 O ATOM 2104 CB ALA B 194 6.966 21.126 -13.432 1.00 76.83 C ANISOU 2104 CB ALA B 194 10114 7589 11489 827 1103 -702 C ATOM 2105 N CYS B 195 6.966 18.774 -11.129 1.00 74.46 N ANISOU 2105 N CYS B 195 9895 7599 10798 659 1176 -827 N ATOM 2106 CA CYS B 195 7.751 17.743 -10.455 1.00 73.38 C ANISOU 2106 CA CYS B 195 9836 7586 10458 512 1070 -855 C ATOM 2107 C CYS B 195 8.853 17.377 -11.456 1.00 74.39 C ANISOU 2107 C CYS B 195 9882 7772 10612 423 840 -773 C ATOM 2108 O CYS B 195 8.604 16.662 -12.430 1.00 72.42 O ANISOU 2108 O CYS B 195 9446 7622 10448 452 767 -647 O ATOM 2109 CB CYS B 195 6.872 16.544 -10.092 1.00 73.72 C ANISOU 2109 CB CYS B 195 9777 7777 10456 532 1144 -801 C ATOM 2110 SG CYS B 195 7.781 15.061 -9.572 1.00 76.41 S ANISOU 2110 SG CYS B 195 10172 8275 10584 369 967 -780 S ATOM 2111 N ILE B 196 10.040 17.975 -11.266 1.00 70.45 N ANISOU 2111 N ILE B 196 9522 7193 10053 317 741 -850 N ATOM 2112 CA ILE B 196 11.197 17.812 -12.152 1.00 68.40 C ANISOU 2112 CA ILE B 196 9191 6966 9829 223 553 -796 C ATOM 2113 C ILE B 196 12.413 17.214 -11.438 1.00 70.84 C ANISOU 2113 C ILE B 196 9586 7340 9992 72 400 -858 C ATOM 2114 O ILE B 196 12.451 17.161 -10.207 1.00 71.36 O ANISOU 2114 O ILE B 196 9814 7392 9906 26 426 -954 O ATOM 2115 CB ILE B 196 11.554 19.144 -12.892 1.00 72.03 C ANISOU 2115 CB ILE B 196 9687 7267 10414 230 556 -801 C ATOM 2116 CG1 ILE B 196 11.812 20.319 -11.918 1.00 74.30 C ANISOU 2116 CG1 ILE B 196 10202 7383 10644 195 630 -952 C ATOM 2117 CG2 ILE B 196 10.507 19.509 -13.946 1.00 72.71 C ANISOU 2117 CG2 ILE B 196 9644 7314 10668 376 633 -689 C ATOM 2118 CD1 ILE B 196 13.261 20.713 -11.792 1.00 80.97 C ANISOU 2118 CD1 ILE B 196 11143 8180 11441 28 487 -1020 C ATOM 2119 N MET B 197 13.409 16.778 -12.224 1.00 65.57 N ANISOU 2119 N MET B 197 8807 6735 9369 -4 241 -803 N ATOM 2120 CA MET B 197 14.658 16.216 -11.723 1.00 64.94 C ANISOU 2120 CA MET B 197 8759 6714 9202 -137 69 -847 C ATOM 2121 C MET B 197 15.580 17.391 -11.358 1.00 69.71 C ANISOU 2121 C MET B 197 9500 7185 9802 -239 25 -956 C ATOM 2122 O MET B 197 16.285 17.925 -12.217 1.00 69.06 O ANISOU 2122 O MET B 197 9348 7059 9834 -287 -22 -936 O ATOM 2123 CB MET B 197 15.285 15.301 -12.785 1.00 65.51 C ANISOU 2123 CB MET B 197 8635 6898 9356 -160 -53 -751 C ATOM 2124 CG MET B 197 16.135 14.212 -12.207 1.00 68.78 C ANISOU 2124 CG MET B 197 9033 7411 9688 -239 -215 -763 C ATOM 2125 SD MET B 197 15.202 12.770 -11.666 1.00 72.21 S ANISOU 2125 SD MET B 197 9457 7965 10014 -176 -197 -700 S ATOM 2126 CE MET B 197 16.530 11.634 -11.389 1.00 68.62 C ANISOU 2126 CE MET B 197 8953 7595 9526 -267 -430 -696 C ATOM 2127 N ALA B 198 15.512 17.828 -10.089 1.00 67.53 N ANISOU 2127 N ALA B 198 9434 6838 9388 -278 57 -1071 N ATOM 2128 CA ALA B 198 16.269 18.964 -9.561 1.00 68.88 C ANISOU 2128 CA ALA B 198 9775 6868 9531 -384 19 -1193 C ATOM 2129 C ALA B 198 17.751 18.656 -9.288 1.00 72.58 C ANISOU 2129 C ALA B 198 10229 7381 9969 -548 -213 -1229 C ATOM 2130 O ALA B 198 18.157 18.434 -8.143 1.00 73.33 O ANISOU 2130 O ALA B 198 10472 7484 9906 -635 -316 -1308 O ATOM 2131 CB ALA B 198 15.583 19.527 -8.320 1.00 71.49 C ANISOU 2131 CB ALA B 198 10352 7098 9710 -365 151 -1312 C ATOM 2132 N PHE B 199 18.555 18.656 -10.363 1.00 67.89 N ANISOU 2132 N PHE B 199 9451 6813 9529 -592 -295 -1168 N ATOM 2133 CA PHE B 199 19.999 18.424 -10.318 1.00 67.87 C ANISOU 2133 CA PHE B 199 9372 6852 9563 -738 -502 -1195 C ATOM 2134 C PHE B 199 20.707 19.703 -9.827 1.00 74.17 C ANISOU 2134 C PHE B 199 10326 7498 10356 -875 -544 -1315 C ATOM 2135 O PHE B 199 20.086 20.770 -9.899 1.00 74.38 O ANISOU 2135 O PHE B 199 10483 7382 10395 -837 -391 -1354 O ATOM 2136 CB PHE B 199 20.516 18.087 -11.732 1.00 68.10 C ANISOU 2136 CB PHE B 199 9152 6950 9771 -735 -519 -1096 C ATOM 2137 CG PHE B 199 20.016 16.817 -12.378 1.00 67.67 C ANISOU 2137 CG PHE B 199 8934 7038 9739 -626 -501 -982 C ATOM 2138 CD1 PHE B 199 20.262 15.578 -11.798 1.00 70.10 C ANISOU 2138 CD1 PHE B 199 9198 7463 9974 -625 -629 -967 C ATOM 2139 CD2 PHE B 199 19.395 16.851 -13.620 1.00 68.49 C ANISOU 2139 CD2 PHE B 199 8931 7152 9941 -537 -376 -887 C ATOM 2140 CE1 PHE B 199 19.833 14.404 -12.416 1.00 69.39 C ANISOU 2140 CE1 PHE B 199 8966 7488 9909 -534 -615 -868 C ATOM 2141 CE2 PHE B 199 18.969 15.674 -14.239 1.00 69.56 C ANISOU 2141 CE2 PHE B 199 8926 7412 10091 -454 -372 -790 C ATOM 2142 CZ PHE B 199 19.208 14.458 -13.642 1.00 67.23 C ANISOU 2142 CZ PHE B 199 8590 7224 9728 -454 -486 -786 C ATOM 2143 N PRO B 200 21.999 19.660 -9.379 1.00 72.00 N ANISOU 2143 N PRO B 200 10032 7240 10086 -1034 -751 -1374 N ATOM 2144 CA PRO B 200 22.675 20.910 -8.986 1.00 73.96 C ANISOU 2144 CA PRO B 200 10423 7335 10343 -1182 -797 -1489 C ATOM 2145 C PRO B 200 22.687 21.901 -10.159 1.00 78.13 C ANISOU 2145 C PRO B 200 10885 7756 11045 -1185 -662 -1455 C ATOM 2146 O PRO B 200 23.146 21.538 -11.246 1.00 76.47 O ANISOU 2146 O PRO B 200 10449 7622 10983 -1189 -669 -1365 O ATOM 2147 CB PRO B 200 24.087 20.451 -8.600 1.00 76.58 C ANISOU 2147 CB PRO B 200 10649 7743 10706 -1340 -1062 -1519 C ATOM 2148 CG PRO B 200 23.949 19.009 -8.288 1.00 79.80 C ANISOU 2148 CG PRO B 200 10968 8311 11040 -1260 -1159 -1451 C ATOM 2149 CD PRO B 200 22.905 18.503 -9.228 1.00 73.15 C ANISOU 2149 CD PRO B 200 10017 7529 10247 -1085 -963 -1339 C ATOM 2150 N PRO B 201 22.100 23.115 -9.984 1.00 76.36 N ANISOU 2150 N PRO B 201 10868 7348 10796 -1171 -522 -1521 N ATOM 2151 CA PRO B 201 21.999 24.068 -11.109 1.00 76.25 C ANISOU 2151 CA PRO B 201 10820 7213 10938 -1161 -392 -1471 C ATOM 2152 C PRO B 201 23.311 24.476 -11.781 1.00 81.19 C ANISOU 2152 C PRO B 201 11318 7819 11712 -1341 -488 -1465 C ATOM 2153 O PRO B 201 23.302 24.747 -12.983 1.00 80.32 O ANISOU 2153 O PRO B 201 11099 7686 11732 -1324 -395 -1372 O ATOM 2154 CB PRO B 201 21.284 25.273 -10.494 1.00 79.67 C ANISOU 2154 CB PRO B 201 11531 7433 11306 -1130 -263 -1570 C ATOM 2155 CG PRO B 201 21.454 25.120 -9.023 1.00 85.45 C ANISOU 2155 CG PRO B 201 12450 8166 11850 -1202 -360 -1704 C ATOM 2156 CD PRO B 201 21.459 23.658 -8.770 1.00 79.48 C ANISOU 2156 CD PRO B 201 11552 7629 11018 -1155 -462 -1642 C ATOM 2157 N GLU B 202 24.428 24.502 -11.026 1.00 79.31 N ANISOU 2157 N GLU B 202 11088 7590 11455 -1521 -676 -1561 N ATOM 2158 CA GLU B 202 25.760 24.852 -11.540 1.00 80.19 C ANISOU 2158 CA GLU B 202 11051 7693 11724 -1713 -777 -1569 C ATOM 2159 C GLU B 202 26.283 23.854 -12.587 1.00 82.71 C ANISOU 2159 C GLU B 202 11055 8190 12180 -1692 -795 -1454 C ATOM 2160 O GLU B 202 27.054 24.245 -13.465 1.00 82.86 O ANISOU 2160 O GLU B 202 10938 8189 12356 -1805 -768 -1424 O ATOM 2161 CB GLU B 202 26.784 25.071 -10.403 1.00 83.75 C ANISOU 2161 CB GLU B 202 11574 8119 12128 -1909 -1000 -1700 C ATOM 2162 CG GLU B 202 26.874 23.955 -9.369 1.00 94.59 C ANISOU 2162 CG GLU B 202 12940 9637 13362 -1879 -1181 -1725 C ATOM 2163 CD GLU B 202 25.914 24.021 -8.193 1.00117.09 C ANISOU 2163 CD GLU B 202 16090 12429 15972 -1801 -1150 -1801 C ATOM 2164 OE1 GLU B 202 25.046 24.925 -8.165 1.00109.00 O ANISOU 2164 OE1 GLU B 202 15273 11247 14894 -1738 -963 -1841 O ATOM 2165 OE2 GLU B 202 26.036 23.162 -7.290 1.00113.84 O ANISOU 2165 OE2 GLU B 202 15709 12121 15425 -1801 -1308 -1820 O ATOM 2166 N LYS B 203 25.853 22.580 -12.500 1.00 77.78 N ANISOU 2166 N LYS B 203 10328 7731 11494 -1552 -824 -1394 N ATOM 2167 CA LYS B 203 26.229 21.509 -13.428 1.00 76.12 C ANISOU 2167 CA LYS B 203 9843 7684 11394 -1506 -830 -1296 C ATOM 2168 C LYS B 203 24.980 20.720 -13.869 1.00 77.49 C ANISOU 2168 C LYS B 203 10012 7936 11495 -1297 -706 -1196 C ATOM 2169 O LYS B 203 25.011 19.487 -13.926 1.00 76.03 O ANISOU 2169 O LYS B 203 9684 7900 11303 -1225 -768 -1148 O ATOM 2170 CB LYS B 203 27.293 20.587 -12.793 1.00 79.47 C ANISOU 2170 CB LYS B 203 10106 8236 11851 -1583 -1059 -1334 C ATOM 2171 CG LYS B 203 28.696 21.183 -12.762 1.00 99.15 C ANISOU 2171 CG LYS B 203 12487 10690 14493 -1796 -1182 -1402 C ATOM 2172 CD LYS B 203 29.687 20.258 -12.071 1.00111.63 C ANISOU 2172 CD LYS B 203 13900 12393 16121 -1851 -1434 -1433 C ATOM 2173 CE LYS B 203 31.064 20.867 -11.985 1.00125.72 C ANISOU 2173 CE LYS B 203 15552 14143 18075 -2070 -1571 -1505 C ATOM 2174 NZ LYS B 203 32.011 19.987 -11.251 1.00136.21 N ANISOU 2174 NZ LYS B 203 16710 15581 19462 -2114 -1848 -1531 N ATOM 2175 N TYR B 204 23.885 21.444 -14.194 1.00 73.41 N ANISOU 2175 N TYR B 204 9646 7309 10937 -1202 -537 -1164 N ATOM 2176 CA TYR B 204 22.600 20.864 -14.603 1.00 71.30 C ANISOU 2176 CA TYR B 204 9378 7097 10615 -1011 -419 -1072 C ATOM 2177 C TYR B 204 22.658 20.091 -15.926 1.00 73.57 C ANISOU 2177 C TYR B 204 9460 7501 10993 -963 -373 -954 C ATOM 2178 O TYR B 204 22.127 18.982 -15.989 1.00 71.57 O ANISOU 2178 O TYR B 204 9128 7371 10694 -852 -381 -898 O ATOM 2179 CB TYR B 204 21.484 21.928 -14.640 1.00 72.65 C ANISOU 2179 CB TYR B 204 9740 7107 10756 -921 -264 -1068 C ATOM 2180 CG TYR B 204 20.092 21.338 -14.558 1.00 72.86 C ANISOU 2180 CG TYR B 204 9786 7188 10709 -730 -172 -1009 C ATOM 2181 CD1 TYR B 204 19.410 20.944 -15.706 1.00 73.33 C ANISOU 2181 CD1 TYR B 204 9731 7303 10828 -620 -91 -880 C ATOM 2182 CD2 TYR B 204 19.457 21.168 -13.332 1.00 74.03 C ANISOU 2182 CD2 TYR B 204 10072 7332 10725 -673 -165 -1082 C ATOM 2183 CE1 TYR B 204 18.139 20.375 -15.634 1.00 72.68 C ANISOU 2183 CE1 TYR B 204 9641 7277 10697 -457 -20 -823 C ATOM 2184 CE2 TYR B 204 18.185 20.602 -13.248 1.00 73.97 C ANISOU 2184 CE2 TYR B 204 10060 7381 10666 -510 -66 -1027 C ATOM 2185 CZ TYR B 204 17.528 20.211 -14.403 1.00 78.81 C ANISOU 2185 CZ TYR B 204 10530 8052 11362 -403 0 -897 C ATOM 2186 OH TYR B 204 16.270 19.664 -14.331 1.00 78.12 O ANISOU 2186 OH TYR B 204 10418 8021 11243 -254 88 -842 O ATOM 2187 N ALA B 205 23.275 20.679 -16.974 1.00 70.70 N ANISOU 2187 N ALA B 205 9029 7088 10746 -1054 -316 -919 N ATOM 2188 CA ALA B 205 23.400 20.075 -18.307 1.00 69.47 C ANISOU 2188 CA ALA B 205 8711 7024 10660 -1031 -251 -818 C ATOM 2189 C ALA B 205 24.192 18.759 -18.294 1.00 72.93 C ANISOU 2189 C ALA B 205 8943 7631 11138 -1047 -351 -827 C ATOM 2190 O ALA B 205 23.796 17.801 -18.964 1.00 71.01 O ANISOU 2190 O ALA B 205 8605 7491 10883 -952 -315 -753 O ATOM 2191 CB ALA B 205 24.032 21.064 -19.274 1.00 71.25 C ANISOU 2191 CB ALA B 205 8937 7148 10985 -1160 -166 -793 C ATOM 2192 N GLN B 206 25.292 18.716 -17.516 1.00 70.91 N ANISOU 2192 N GLN B 206 8620 7392 10932 -1164 -487 -918 N ATOM 2193 CA GLN B 206 26.176 17.556 -17.358 1.00 70.63 C ANISOU 2193 CA GLN B 206 8380 7494 10963 -1179 -610 -936 C ATOM 2194 C GLN B 206 25.438 16.397 -16.678 1.00 73.28 C ANISOU 2194 C GLN B 206 8739 7921 11182 -1037 -688 -914 C ATOM 2195 O GLN B 206 25.563 15.251 -17.114 1.00 72.00 O ANISOU 2195 O GLN B 206 8430 7870 11056 -971 -705 -871 O ATOM 2196 CB GLN B 206 27.441 17.932 -16.560 1.00 73.90 C ANISOU 2196 CB GLN B 206 8733 7885 11462 -1339 -768 -1036 C ATOM 2197 CG GLN B 206 28.322 18.995 -17.225 1.00 91.56 C ANISOU 2197 CG GLN B 206 10913 10037 13837 -1509 -696 -1062 C ATOM 2198 CD GLN B 206 28.024 20.401 -16.749 1.00111.69 C ANISOU 2198 CD GLN B 206 13694 12417 16328 -1591 -671 -1110 C ATOM 2199 OE1 GLN B 206 26.907 20.916 -16.880 1.00105.53 O ANISOU 2199 OE1 GLN B 206 13104 11548 15443 -1498 -556 -1071 O ATOM 2200 NE2 GLN B 206 29.039 21.073 -16.228 1.00107.46 N ANISOU 2200 NE2 GLN B 206 13137 11819 15873 -1770 -776 -1197 N ATOM 2201 N TRP B 207 24.655 16.708 -15.626 1.00 69.77 N ANISOU 2201 N TRP B 207 8493 7421 10596 -994 -719 -946 N ATOM 2202 CA TRP B 207 23.860 15.745 -14.866 1.00 68.56 C ANISOU 2202 CA TRP B 207 8402 7337 10310 -878 -771 -925 C ATOM 2203 C TRP B 207 22.703 15.185 -15.702 1.00 70.12 C ANISOU 2203 C TRP B 207 8582 7583 10478 -736 -633 -825 C ATOM 2204 O TRP B 207 22.426 13.985 -15.628 1.00 68.57 O ANISOU 2204 O TRP B 207 8322 7486 10246 -658 -677 -782 O ATOM 2205 CB TRP B 207 23.326 16.392 -13.583 1.00 68.34 C ANISOU 2205 CB TRP B 207 8609 7222 10134 -888 -796 -997 C ATOM 2206 CG TRP B 207 24.198 16.192 -12.380 1.00 70.81 C ANISOU 2206 CG TRP B 207 8960 7546 10398 -987 -1005 -1078 C ATOM 2207 CD1 TRP B 207 24.995 17.122 -11.782 1.00 75.54 C ANISOU 2207 CD1 TRP B 207 9637 8057 11009 -1132 -1100 -1174 C ATOM 2208 CD2 TRP B 207 24.340 14.988 -11.616 1.00 70.61 C ANISOU 2208 CD2 TRP B 207 8914 7619 10297 -953 -1162 -1064 C ATOM 2209 NE1 TRP B 207 25.627 16.573 -10.691 1.00 76.14 N ANISOU 2209 NE1 TRP B 207 9737 8175 11016 -1193 -1320 -1220 N ATOM 2210 CE2 TRP B 207 25.247 15.262 -10.568 1.00 76.40 C ANISOU 2210 CE2 TRP B 207 9715 8320 10994 -1081 -1363 -1150 C ATOM 2211 CE3 TRP B 207 23.796 13.696 -11.720 1.00 70.57 C ANISOU 2211 CE3 TRP B 207 8849 7716 10250 -836 -1163 -984 C ATOM 2212 CZ2 TRP B 207 25.622 14.293 -9.630 1.00 76.36 C ANISOU 2212 CZ2 TRP B 207 9723 8382 10908 -1085 -1574 -1147 C ATOM 2213 CZ3 TRP B 207 24.171 12.736 -10.793 1.00 72.66 C ANISOU 2213 CZ3 TRP B 207 9128 8039 10439 -841 -1356 -984 C ATOM 2214 CH2 TRP B 207 25.074 13.036 -9.764 1.00 75.24 C ANISOU 2214 CH2 TRP B 207 9527 8332 10728 -961 -1563 -1060 C ATOM 2215 N SER B 208 22.038 16.055 -16.498 1.00 66.10 N ANISOU 2215 N SER B 208 8133 6995 9987 -708 -481 -783 N ATOM 2216 CA SER B 208 20.917 15.700 -17.377 1.00 64.32 C ANISOU 2216 CA SER B 208 7893 6801 9743 -586 -365 -682 C ATOM 2217 C SER B 208 21.347 14.751 -18.492 1.00 66.82 C ANISOU 2217 C SER B 208 8037 7221 10131 -582 -362 -621 C ATOM 2218 O SER B 208 20.576 13.867 -18.862 1.00 64.89 O ANISOU 2218 O SER B 208 7759 7050 9846 -486 -339 -554 O ATOM 2219 CB SER B 208 20.276 16.951 -17.970 1.00 67.87 C ANISOU 2219 CB SER B 208 8449 7124 10215 -569 -237 -649 C ATOM 2220 OG SER B 208 19.687 17.756 -16.964 1.00 76.36 O ANISOU 2220 OG SER B 208 9693 8094 11225 -543 -212 -709 O ATOM 2221 N ALA B 209 22.576 14.936 -19.017 1.00 63.99 N ANISOU 2221 N ALA B 209 7570 6865 9880 -693 -376 -651 N ATOM 2222 CA ALA B 209 23.164 14.104 -20.068 1.00 63.20 C ANISOU 2222 CA ALA B 209 7304 6851 9856 -703 -349 -617 C ATOM 2223 C ALA B 209 23.681 12.775 -19.497 1.00 66.40 C ANISOU 2223 C ALA B 209 7588 7361 10281 -670 -477 -647 C ATOM 2224 O ALA B 209 23.613 11.750 -20.178 1.00 65.10 O ANISOU 2224 O ALA B 209 7330 7272 10131 -612 -453 -607 O ATOM 2225 CB ALA B 209 24.290 14.856 -20.759 1.00 65.12 C ANISOU 2225 CB ALA B 209 7473 7051 10217 -840 -293 -647 C ATOM 2226 N GLY B 210 24.184 12.815 -18.261 1.00 63.64 N ANISOU 2226 N GLY B 210 7256 7001 9924 -708 -618 -716 N ATOM 2227 CA GLY B 210 24.705 11.653 -17.547 1.00 63.44 C ANISOU 2227 CA GLY B 210 7140 7052 9914 -679 -775 -738 C ATOM 2228 C GLY B 210 23.626 10.664 -17.154 1.00 65.77 C ANISOU 2228 C GLY B 210 7513 7394 10082 -559 -794 -683 C ATOM 2229 O GLY B 210 23.792 9.457 -17.351 1.00 64.57 O ANISOU 2229 O GLY B 210 7261 7311 9960 -502 -844 -656 O ATOM 2230 N ILE B 211 22.504 11.177 -16.607 1.00 62.18 N ANISOU 2230 N ILE B 211 7235 6895 9495 -521 -743 -667 N ATOM 2231 CA ILE B 211 21.348 10.376 -16.185 1.00 61.15 C ANISOU 2231 CA ILE B 211 7187 6804 9243 -422 -733 -614 C ATOM 2232 C ILE B 211 20.605 9.814 -17.414 1.00 64.06 C ANISOU 2232 C ILE B 211 7489 7218 9633 -347 -621 -531 C ATOM 2233 O ILE B 211 20.127 8.680 -17.359 1.00 62.88 O ANISOU 2233 O ILE B 211 7321 7129 9442 -284 -650 -487 O ATOM 2234 CB ILE B 211 20.447 11.166 -15.182 1.00 64.64 C ANISOU 2234 CB ILE B 211 7824 7180 9554 -412 -691 -640 C ATOM 2235 CG1 ILE B 211 21.164 11.379 -13.812 1.00 66.57 C ANISOU 2235 CG1 ILE B 211 8167 7395 9733 -491 -838 -723 C ATOM 2236 CG2 ILE B 211 19.040 10.565 -15.003 1.00 64.24 C ANISOU 2236 CG2 ILE B 211 7841 7165 9403 -311 -613 -576 C ATOM 2237 CD1 ILE B 211 21.593 10.093 -12.965 1.00 73.83 C ANISOU 2237 CD1 ILE B 211 9074 8383 10597 -485 -1018 -714 C ATOM 2238 N ALA B 212 20.572 10.572 -18.532 1.00 60.68 N ANISOU 2238 N ALA B 212 7035 6757 9266 -367 -507 -509 N ATOM 2239 CA ALA B 212 19.959 10.129 -19.788 1.00 59.73 C ANISOU 2239 CA ALA B 212 6868 6672 9154 -317 -418 -431 C ATOM 2240 C ALA B 212 20.751 8.960 -20.383 1.00 64.09 C ANISOU 2240 C ALA B 212 7284 7297 9772 -321 -456 -435 C ATOM 2241 O ALA B 212 20.150 8.043 -20.947 1.00 62.91 O ANISOU 2241 O ALA B 212 7116 7196 9591 -263 -437 -383 O ATOM 2242 CB ALA B 212 19.893 11.275 -20.778 1.00 60.78 C ANISOU 2242 CB ALA B 212 7031 6739 9324 -355 -307 -404 C ATOM 2243 N LEU B 213 22.096 8.986 -20.229 1.00 62.09 N ANISOU 2243 N LEU B 213 6929 7043 9618 -388 -513 -504 N ATOM 2244 CA LEU B 213 23.007 7.927 -20.669 1.00 62.20 C ANISOU 2244 CA LEU B 213 6792 7112 9729 -382 -547 -527 C ATOM 2245 C LEU B 213 22.784 6.682 -19.805 1.00 65.86 C ANISOU 2245 C LEU B 213 7258 7614 10151 -308 -678 -517 C ATOM 2246 O LEU B 213 22.794 5.572 -20.332 1.00 65.19 O ANISOU 2246 O LEU B 213 7109 7567 10091 -255 -675 -498 O ATOM 2247 CB LEU B 213 24.475 8.398 -20.563 1.00 63.71 C ANISOU 2247 CB LEU B 213 6855 7288 10065 -474 -584 -605 C ATOM 2248 CG LEU B 213 25.305 8.543 -21.860 1.00 69.16 C ANISOU 2248 CG LEU B 213 7417 7987 10873 -533 -450 -625 C ATOM 2249 CD1 LEU B 213 25.644 7.192 -22.482 1.00 69.17 C ANISOU 2249 CD1 LEU B 213 7298 8046 10938 -468 -433 -632 C ATOM 2250 CD2 LEU B 213 24.667 9.512 -22.860 1.00 71.57 C ANISOU 2250 CD2 LEU B 213 7833 8250 11111 -575 -290 -574 C ATOM 2251 N MET B 214 22.541 6.882 -18.486 1.00 62.68 N ANISOU 2251 N MET B 214 6954 7192 9671 -309 -784 -528 N ATOM 2252 CA MET B 214 22.252 5.834 -17.499 1.00 62.30 C ANISOU 2252 CA MET B 214 6955 7167 9549 -255 -912 -507 C ATOM 2253 C MET B 214 20.926 5.141 -17.844 1.00 63.87 C ANISOU 2253 C MET B 214 7224 7393 9652 -185 -836 -432 C ATOM 2254 O MET B 214 20.821 3.925 -17.688 1.00 63.59 O ANISOU 2254 O MET B 214 7175 7382 9603 -138 -903 -402 O ATOM 2255 CB MET B 214 22.200 6.432 -16.078 1.00 65.64 C ANISOU 2255 CB MET B 214 7510 7554 9875 -295 -1010 -538 C ATOM 2256 CG MET B 214 22.117 5.398 -14.970 1.00 69.91 C ANISOU 2256 CG MET B 214 8121 8110 10330 -264 -1162 -517 C ATOM 2257 SD MET B 214 21.387 6.064 -13.455 1.00 75.06 S ANISOU 2257 SD MET B 214 9014 8724 10781 -302 -1190 -533 S ATOM 2258 CE MET B 214 21.345 4.593 -12.452 1.00 72.21 C ANISOU 2258 CE MET B 214 8728 8386 10322 -270 -1359 -482 C ATOM 2259 N LYS B 215 19.929 5.916 -18.328 1.00 58.71 N ANISOU 2259 N LYS B 215 6639 6726 8944 -180 -705 -397 N ATOM 2260 CA LYS B 215 18.614 5.411 -18.742 1.00 57.03 C ANISOU 2260 CA LYS B 215 6469 6540 8660 -124 -634 -323 C ATOM 2261 C LYS B 215 18.763 4.436 -19.910 1.00 59.58 C ANISOU 2261 C LYS B 215 6703 6899 9037 -103 -615 -297 C ATOM 2262 O LYS B 215 18.132 3.381 -19.901 1.00 58.77 O ANISOU 2262 O LYS B 215 6616 6824 8892 -65 -639 -253 O ATOM 2263 CB LYS B 215 17.680 6.563 -19.152 1.00 59.01 C ANISOU 2263 CB LYS B 215 6779 6759 8884 -119 -514 -292 C ATOM 2264 CG LYS B 215 17.219 7.453 -18.011 1.00 70.08 C ANISOU 2264 CG LYS B 215 8293 8115 10219 -120 -499 -319 C ATOM 2265 CD LYS B 215 16.409 8.624 -18.534 1.00 77.22 C ANISOU 2265 CD LYS B 215 9238 8968 11135 -99 -382 -292 C ATOM 2266 CE LYS B 215 16.217 9.693 -17.493 1.00 86.15 C ANISOU 2266 CE LYS B 215 10482 10027 12223 -106 -350 -346 C ATOM 2267 NZ LYS B 215 15.326 10.774 -17.983 1.00 95.12 N ANISOU 2267 NZ LYS B 215 11655 11099 13389 -61 -236 -312 N ATOM 2268 N ASN B 216 19.615 4.786 -20.900 1.00 55.82 N ANISOU 2268 N ASN B 216 6144 6415 8648 -139 -562 -329 N ATOM 2269 CA ASN B 216 19.879 3.985 -22.096 1.00 55.09 C ANISOU 2269 CA ASN B 216 5984 6348 8600 -130 -515 -325 C ATOM 2270 C ASN B 216 20.624 2.691 -21.786 1.00 59.33 C ANISOU 2270 C ASN B 216 6446 6897 9199 -95 -607 -360 C ATOM 2271 O ASN B 216 20.202 1.631 -22.243 1.00 58.36 O ANISOU 2271 O ASN B 216 6333 6788 9054 -57 -605 -333 O ATOM 2272 CB ASN B 216 20.648 4.801 -23.150 1.00 54.55 C ANISOU 2272 CB ASN B 216 5864 6264 8600 -191 -410 -357 C ATOM 2273 CG ASN B 216 19.936 6.014 -23.711 1.00 70.68 C ANISOU 2273 CG ASN B 216 7992 8276 10586 -223 -320 -308 C ATOM 2274 OD1 ASN B 216 20.574 6.964 -24.173 1.00 63.56 O ANISOU 2274 OD1 ASN B 216 7079 7342 9731 -288 -252 -331 O ATOM 2275 ND2 ASN B 216 18.607 6.008 -23.729 1.00 61.14 N ANISOU 2275 ND2 ASN B 216 6866 7073 9291 -179 -319 -234 N ATOM 2276 N ILE B 217 21.724 2.778 -21.010 1.00 57.08 N ANISOU 2276 N ILE B 217 6088 6598 9001 -107 -698 -417 N ATOM 2277 CA ILE B 217 22.586 1.648 -20.647 1.00 57.56 C ANISOU 2277 CA ILE B 217 6059 6656 9155 -62 -810 -449 C ATOM 2278 C ILE B 217 21.850 0.612 -19.773 1.00 61.87 C ANISOU 2278 C ILE B 217 6700 7197 9608 -9 -922 -394 C ATOM 2279 O ILE B 217 21.778 -0.561 -20.149 1.00 61.47 O ANISOU 2279 O ILE B 217 6635 7140 9580 41 -936 -381 O ATOM 2280 CB ILE B 217 23.936 2.129 -20.018 1.00 61.65 C ANISOU 2280 CB ILE B 217 6462 7161 9803 -96 -905 -516 C ATOM 2281 CG1 ILE B 217 24.739 3.001 -21.022 1.00 62.45 C ANISOU 2281 CG1 ILE B 217 6447 7264 10015 -162 -770 -570 C ATOM 2282 CG2 ILE B 217 24.785 0.945 -19.525 1.00 62.97 C ANISOU 2282 CG2 ILE B 217 6529 7316 10083 -32 -1055 -536 C ATOM 2283 CD1 ILE B 217 25.802 3.942 -20.409 1.00 67.91 C ANISOU 2283 CD1 ILE B 217 7049 7941 10812 -237 -839 -629 C ATOM 2284 N LEU B 218 21.303 1.048 -18.630 1.00 58.72 N ANISOU 2284 N LEU B 218 6414 6794 9102 -27 -988 -366 N ATOM 2285 CA LEU B 218 20.633 0.177 -17.665 1.00 58.63 C ANISOU 2285 CA LEU B 218 6514 6776 8986 1 -1083 -312 C ATOM 2286 C LEU B 218 19.237 -0.306 -18.085 1.00 61.24 C ANISOU 2286 C LEU B 218 6925 7126 9218 16 -991 -243 C ATOM 2287 O LEU B 218 18.894 -1.460 -17.822 1.00 61.33 O ANISOU 2287 O LEU B 218 6981 7126 9197 43 -1050 -201 O ATOM 2288 CB LEU B 218 20.579 0.872 -16.292 1.00 59.41 C ANISOU 2288 CB LEU B 218 6722 6862 8987 -38 -1165 -317 C ATOM 2289 CG LEU B 218 20.564 -0.023 -15.053 1.00 65.13 C ANISOU 2289 CG LEU B 218 7551 7566 9628 -27 -1323 -279 C ATOM 2290 CD1 LEU B 218 21.914 -0.696 -14.833 1.00 66.60 C ANISOU 2290 CD1 LEU B 218 7635 7726 9946 1 -1502 -305 C ATOM 2291 CD2 LEU B 218 20.206 0.782 -13.824 1.00 68.38 C ANISOU 2291 CD2 LEU B 218 8118 7968 9893 -81 -1350 -286 C ATOM 2292 N GLY B 219 18.451 0.570 -18.709 1.00 56.22 N ANISOU 2292 N GLY B 219 6305 6510 8545 -5 -860 -228 N ATOM 2293 CA GLY B 219 17.081 0.270 -19.111 1.00 54.87 C ANISOU 2293 CA GLY B 219 6186 6363 8300 2 -784 -161 C ATOM 2294 C GLY B 219 16.863 -0.290 -20.503 1.00 57.58 C ANISOU 2294 C GLY B 219 6480 6718 8679 9 -727 -146 C ATOM 2295 O GLY B 219 15.751 -0.733 -20.808 1.00 56.79 O ANISOU 2295 O GLY B 219 6416 6637 8525 7 -697 -87 O ATOM 2296 N PHE B 220 17.898 -0.271 -21.370 1.00 53.73 N ANISOU 2296 N PHE B 220 5912 6221 8282 8 -704 -201 N ATOM 2297 CA PHE B 220 17.750 -0.777 -22.735 1.00 53.13 C ANISOU 2297 CA PHE B 220 5818 6152 8217 4 -637 -199 C ATOM 2298 C PHE B 220 18.954 -1.569 -23.252 1.00 57.50 C ANISOU 2298 C PHE B 220 6295 6680 8872 26 -642 -270 C ATOM 2299 O PHE B 220 18.759 -2.675 -23.745 1.00 57.05 O ANISOU 2299 O PHE B 220 6260 6607 8811 45 -648 -268 O ATOM 2300 CB PHE B 220 17.382 0.357 -23.707 1.00 54.69 C ANISOU 2300 CB PHE B 220 6026 6364 8390 -34 -531 -182 C ATOM 2301 CG PHE B 220 16.916 -0.109 -25.065 1.00 56.20 C ANISOU 2301 CG PHE B 220 6245 6565 8542 -54 -476 -160 C ATOM 2302 CD1 PHE B 220 15.661 -0.685 -25.229 1.00 59.16 C ANISOU 2302 CD1 PHE B 220 6676 6957 8845 -56 -506 -92 C ATOM 2303 CD2 PHE B 220 17.725 0.040 -26.184 1.00 58.78 C ANISOU 2303 CD2 PHE B 220 6551 6884 8900 -84 -392 -210 C ATOM 2304 CE1 PHE B 220 15.233 -1.123 -26.485 1.00 60.23 C ANISOU 2304 CE1 PHE B 220 6854 7099 8933 -89 -478 -74 C ATOM 2305 CE2 PHE B 220 17.294 -0.393 -27.441 1.00 61.87 C ANISOU 2305 CE2 PHE B 220 7003 7279 9225 -114 -344 -195 C ATOM 2306 CZ PHE B 220 16.052 -0.973 -27.582 1.00 59.76 C ANISOU 2306 CZ PHE B 220 6799 7026 8879 -117 -400 -126 C ATOM 2307 N ILE B 221 20.179 -1.010 -23.153 1.00 54.72 N ANISOU 2307 N ILE B 221 5849 6319 8623 22 -635 -336 N ATOM 2308 CA ILE B 221 21.427 -1.611 -23.645 1.00 55.45 C ANISOU 2308 CA ILE B 221 5830 6389 8850 49 -617 -414 C ATOM 2309 C ILE B 221 21.711 -2.990 -23.013 1.00 59.22 C ANISOU 2309 C ILE B 221 6292 6825 9382 122 -741 -419 C ATOM 2310 O ILE B 221 21.731 -3.980 -23.746 1.00 58.85 O ANISOU 2310 O ILE B 221 6251 6751 9360 154 -702 -442 O ATOM 2311 CB ILE B 221 22.626 -0.618 -23.506 1.00 59.58 C ANISOU 2311 CB ILE B 221 6232 6915 9490 17 -596 -477 C ATOM 2312 CG1 ILE B 221 22.483 0.625 -24.439 1.00 59.90 C ANISOU 2312 CG1 ILE B 221 6294 6974 9489 -61 -446 -475 C ATOM 2313 CG2 ILE B 221 23.995 -1.292 -23.668 1.00 61.84 C ANISOU 2313 CG2 ILE B 221 6359 7179 9959 60 -606 -559 C ATOM 2314 CD1 ILE B 221 22.198 0.377 -25.965 1.00 69.02 C ANISOU 2314 CD1 ILE B 221 7496 8136 10594 -86 -297 -478 C ATOM 2315 N ILE B 222 21.926 -3.054 -21.679 1.00 55.93 N ANISOU 2315 N ILE B 222 5879 6396 8978 144 -891 -398 N ATOM 2316 CA ILE B 222 22.223 -4.302 -20.963 1.00 56.48 C ANISOU 2316 CA ILE B 222 5953 6412 9094 212 -1035 -385 C ATOM 2317 C ILE B 222 21.070 -5.332 -21.136 1.00 60.44 C ANISOU 2317 C ILE B 222 6587 6892 9486 221 -1032 -323 C ATOM 2318 O ILE B 222 21.377 -6.439 -21.586 1.00 60.61 O ANISOU 2318 O ILE B 222 6593 6858 9578 273 -1042 -348 O ATOM 2319 CB ILE B 222 22.647 -4.074 -19.478 1.00 60.04 C ANISOU 2319 CB ILE B 222 6414 6852 9546 216 -1213 -363 C ATOM 2320 CG1 ILE B 222 23.923 -3.198 -19.395 1.00 61.10 C ANISOU 2320 CG1 ILE B 222 6393 6999 9822 200 -1236 -435 C ATOM 2321 CG2 ILE B 222 22.853 -5.408 -18.736 1.00 61.50 C ANISOU 2321 CG2 ILE B 222 6637 6969 9760 285 -1380 -327 C ATOM 2322 CD1 ILE B 222 24.126 -2.468 -18.074 1.00 67.90 C ANISOU 2322 CD1 ILE B 222 7299 7867 10634 158 -1380 -419 C ATOM 2323 N PRO B 223 19.764 -5.015 -20.885 1.00 56.53 N ANISOU 2323 N PRO B 223 6209 6432 8837 169 -1006 -250 N ATOM 2324 CA PRO B 223 18.719 -6.037 -21.094 1.00 55.93 C ANISOU 2324 CA PRO B 223 6235 6336 8681 161 -1006 -194 C ATOM 2325 C PRO B 223 18.596 -6.557 -22.529 1.00 59.61 C ANISOU 2325 C PRO B 223 6693 6790 9168 158 -906 -231 C ATOM 2326 O PRO B 223 18.506 -7.773 -22.691 1.00 59.95 O ANISOU 2326 O PRO B 223 6782 6772 9226 182 -945 -229 O ATOM 2327 CB PRO B 223 17.437 -5.359 -20.607 1.00 56.87 C ANISOU 2327 CB PRO B 223 6435 6508 8666 103 -974 -122 C ATOM 2328 CG PRO B 223 17.726 -3.913 -20.654 1.00 61.09 C ANISOU 2328 CG PRO B 223 6916 7086 9209 84 -912 -152 C ATOM 2329 CD PRO B 223 19.176 -3.768 -20.347 1.00 57.43 C ANISOU 2329 CD PRO B 223 6365 6598 8860 117 -976 -220 C ATOM 2330 N LEU B 224 18.639 -5.669 -23.561 1.00 55.25 N ANISOU 2330 N LEU B 224 6100 6282 8611 123 -783 -265 N ATOM 2331 CA LEU B 224 18.547 -6.075 -24.975 1.00 55.00 C ANISOU 2331 CA LEU B 224 6090 6240 8568 104 -683 -304 C ATOM 2332 C LEU B 224 19.653 -7.051 -25.380 1.00 59.93 C ANISOU 2332 C LEU B 224 6662 6794 9313 167 -670 -393 C ATOM 2333 O LEU B 224 19.370 -7.991 -26.120 1.00 60.06 O ANISOU 2333 O LEU B 224 6748 6766 9305 165 -640 -415 O ATOM 2334 CB LEU B 224 18.491 -4.867 -25.940 1.00 54.63 C ANISOU 2334 CB LEU B 224 6030 6247 8481 48 -562 -315 C ATOM 2335 CG LEU B 224 17.877 -5.041 -27.361 1.00 59.21 C ANISOU 2335 CG LEU B 224 6693 6833 8969 -7 -476 -315 C ATOM 2336 CD1 LEU B 224 18.911 -5.448 -28.391 1.00 60.30 C ANISOU 2336 CD1 LEU B 224 6812 6936 9164 2 -366 -418 C ATOM 2337 CD2 LEU B 224 16.638 -5.941 -27.378 1.00 61.47 C ANISOU 2337 CD2 LEU B 224 7077 7110 9168 -33 -549 -251 C ATOM 2338 N ILE B 225 20.893 -6.843 -24.883 1.00 56.93 N ANISOU 2338 N ILE B 225 6158 6399 9075 223 -696 -447 N ATOM 2339 CA ILE B 225 22.031 -7.733 -25.152 1.00 58.02 C ANISOU 2339 CA ILE B 225 6207 6464 9372 305 -687 -535 C ATOM 2340 C ILE B 225 21.754 -9.114 -24.538 1.00 61.74 C ANISOU 2340 C ILE B 225 6754 6848 9855 366 -819 -501 C ATOM 2341 O ILE B 225 21.977 -10.123 -25.204 1.00 62.26 O ANISOU 2341 O ILE B 225 6844 6839 9975 410 -775 -557 O ATOM 2342 CB ILE B 225 23.393 -7.104 -24.721 1.00 62.10 C ANISOU 2342 CB ILE B 225 6541 6992 10060 345 -702 -593 C ATOM 2343 CG1 ILE B 225 23.749 -5.913 -25.642 1.00 62.52 C ANISOU 2343 CG1 ILE B 225 6531 7109 10113 273 -529 -642 C ATOM 2344 CG2 ILE B 225 24.533 -8.145 -24.716 1.00 64.42 C ANISOU 2344 CG2 ILE B 225 6717 7201 10558 456 -734 -670 C ATOM 2345 CD1 ILE B 225 24.694 -4.875 -25.058 1.00 70.83 C ANISOU 2345 CD1 ILE B 225 7435 8197 11280 257 -556 -666 C ATOM 2346 N PHE B 226 21.203 -9.147 -23.306 1.00 57.34 N ANISOU 2346 N PHE B 226 6260 6295 9232 357 -965 -408 N ATOM 2347 CA PHE B 226 20.833 -10.378 -22.606 1.00 57.26 C ANISOU 2347 CA PHE B 226 6350 6199 9207 393 -1097 -351 C ATOM 2348 C PHE B 226 19.698 -11.109 -23.328 1.00 60.59 C ANISOU 2348 C PHE B 226 6909 6597 9515 337 -1040 -325 C ATOM 2349 O PHE B 226 19.807 -12.313 -23.548 1.00 61.22 O ANISOU 2349 O PHE B 226 7044 6574 9643 380 -1070 -346 O ATOM 2350 CB PHE B 226 20.450 -10.091 -21.146 1.00 58.64 C ANISOU 2350 CB PHE B 226 6582 6395 9302 370 -1239 -255 C ATOM 2351 CG PHE B 226 21.587 -10.182 -20.155 1.00 61.31 C ANISOU 2351 CG PHE B 226 6844 6689 9761 446 -1394 -261 C ATOM 2352 CD1 PHE B 226 22.030 -11.417 -19.690 1.00 65.44 C ANISOU 2352 CD1 PHE B 226 7397 7096 10369 528 -1532 -241 C ATOM 2353 CD2 PHE B 226 22.193 -9.033 -19.661 1.00 63.22 C ANISOU 2353 CD2 PHE B 226 6992 6997 10032 430 -1420 -280 C ATOM 2354 CE1 PHE B 226 23.077 -11.500 -18.768 1.00 67.53 C ANISOU 2354 CE1 PHE B 226 7588 7318 10753 601 -1708 -235 C ATOM 2355 CE2 PHE B 226 23.238 -9.117 -18.735 1.00 67.23 C ANISOU 2355 CE2 PHE B 226 7426 7466 10652 489 -1593 -281 C ATOM 2356 CZ PHE B 226 23.673 -10.350 -18.294 1.00 66.60 C ANISOU 2356 CZ PHE B 226 7367 7277 10661 577 -1744 -255 C ATOM 2357 N ILE B 227 18.635 -10.375 -23.727 1.00 55.82 N ANISOU 2357 N ILE B 227 6355 6081 8774 241 -966 -283 N ATOM 2358 CA ILE B 227 17.468 -10.909 -24.442 1.00 55.21 C ANISOU 2358 CA ILE B 227 6391 5999 8587 167 -929 -251 C ATOM 2359 C ILE B 227 17.874 -11.475 -25.822 1.00 59.08 C ANISOU 2359 C ILE B 227 6899 6438 9111 176 -830 -350 C ATOM 2360 O ILE B 227 17.440 -12.576 -26.169 1.00 59.19 O ANISOU 2360 O ILE B 227 7017 6374 9099 159 -851 -354 O ATOM 2361 CB ILE B 227 16.303 -9.864 -24.507 1.00 57.23 C ANISOU 2361 CB ILE B 227 6662 6364 8719 77 -888 -179 C ATOM 2362 CG1 ILE B 227 15.773 -9.534 -23.089 1.00 57.23 C ANISOU 2362 CG1 ILE B 227 6676 6396 8675 64 -966 -90 C ATOM 2363 CG2 ILE B 227 15.148 -10.345 -25.400 1.00 57.90 C ANISOU 2363 CG2 ILE B 227 6837 6453 8711 -7 -864 -150 C ATOM 2364 CD1 ILE B 227 15.140 -8.141 -22.930 1.00 63.92 C ANISOU 2364 CD1 ILE B 227 7486 7343 9459 23 -910 -50 C ATOM 2365 N ALA B 228 18.728 -10.746 -26.577 1.00 55.51 N ANISOU 2365 N ALA B 228 6359 6020 8712 196 -714 -433 N ATOM 2366 CA ALA B 228 19.214 -11.170 -27.896 1.00 56.27 C ANISOU 2366 CA ALA B 228 6481 6072 8828 200 -585 -541 C ATOM 2367 C ALA B 228 20.131 -12.400 -27.818 1.00 62.26 C ANISOU 2367 C ALA B 228 7220 6701 9734 307 -600 -623 C ATOM 2368 O ALA B 228 19.930 -13.340 -28.589 1.00 62.71 O ANISOU 2368 O ALA B 228 7387 6678 9763 298 -555 -677 O ATOM 2369 CB ALA B 228 19.916 -10.023 -28.605 1.00 56.96 C ANISOU 2369 CB ALA B 228 6479 6230 8935 183 -444 -600 C ATOM 2370 N THR B 229 21.106 -12.414 -26.872 1.00 59.54 N ANISOU 2370 N THR B 229 6744 6328 9550 408 -677 -630 N ATOM 2371 CA THR B 229 22.037 -13.536 -26.665 1.00 61.12 C ANISOU 2371 CA THR B 229 6899 6396 9928 534 -718 -695 C ATOM 2372 C THR B 229 21.263 -14.821 -26.361 1.00 65.75 C ANISOU 2372 C THR B 229 7651 6870 10459 533 -827 -642 C ATOM 2373 O THR B 229 21.571 -15.869 -26.931 1.00 66.75 O ANISOU 2373 O THR B 229 7832 6874 10657 590 -785 -722 O ATOM 2374 CB THR B 229 23.093 -13.186 -25.599 1.00 68.80 C ANISOU 2374 CB THR B 229 7697 7372 11070 628 -827 -684 C ATOM 2375 OG1 THR B 229 23.770 -11.992 -25.992 1.00 66.71 O ANISOU 2375 OG1 THR B 229 7285 7206 10855 605 -711 -739 O ATOM 2376 CG2 THR B 229 24.121 -14.298 -25.386 1.00 69.72 C ANISOU 2376 CG2 THR B 229 7739 7346 11406 777 -888 -746 C ATOM 2377 N CYS B 230 20.233 -14.718 -25.500 1.00 61.57 N ANISOU 2377 N CYS B 230 7209 6381 9803 460 -949 -514 N ATOM 2378 CA CYS B 230 19.360 -15.826 -25.126 1.00 61.71 C ANISOU 2378 CA CYS B 230 7389 6306 9753 425 -1050 -443 C ATOM 2379 C CYS B 230 18.556 -16.327 -26.326 1.00 66.26 C ANISOU 2379 C CYS B 230 8097 6857 10222 335 -956 -486 C ATOM 2380 O CYS B 230 18.410 -17.538 -26.477 1.00 67.04 O ANISOU 2380 O CYS B 230 8312 6819 10341 347 -992 -505 O ATOM 2381 CB CYS B 230 18.457 -15.436 -23.960 1.00 60.91 C ANISOU 2381 CB CYS B 230 7332 6273 9537 352 -1163 -303 C ATOM 2382 SG CYS B 230 19.334 -15.205 -22.390 1.00 65.21 S ANISOU 2382 SG CYS B 230 7798 6804 10175 444 -1324 -244 S ATOM 2383 N TYR B 231 18.084 -15.407 -27.204 1.00 62.29 N ANISOU 2383 N TYR B 231 7585 6473 9608 245 -846 -503 N ATOM 2384 CA TYR B 231 17.337 -15.764 -28.415 1.00 62.40 C ANISOU 2384 CA TYR B 231 7732 6476 9503 145 -774 -543 C ATOM 2385 C TYR B 231 18.228 -16.469 -29.445 1.00 67.69 C ANISOU 2385 C TYR B 231 8440 7036 10245 208 -655 -695 C ATOM 2386 O TYR B 231 17.848 -17.535 -29.933 1.00 68.27 O ANISOU 2386 O TYR B 231 8661 6996 10281 176 -662 -734 O ATOM 2387 CB TYR B 231 16.604 -14.551 -29.035 1.00 62.56 C ANISOU 2387 CB TYR B 231 7740 6645 9385 37 -715 -504 C ATOM 2388 CG TYR B 231 16.111 -14.808 -30.447 1.00 65.18 C ANISOU 2388 CG TYR B 231 8204 6965 9595 -59 -641 -563 C ATOM 2389 CD1 TYR B 231 15.054 -15.683 -30.690 1.00 67.45 C ANISOU 2389 CD1 TYR B 231 8635 7201 9793 -156 -719 -528 C ATOM 2390 CD2 TYR B 231 16.734 -14.217 -31.543 1.00 66.51 C ANISOU 2390 CD2 TYR B 231 8370 7167 9733 -63 -493 -657 C ATOM 2391 CE1 TYR B 231 14.631 -15.964 -31.988 1.00 68.92 C ANISOU 2391 CE1 TYR B 231 8962 7368 9856 -254 -673 -589 C ATOM 2392 CE2 TYR B 231 16.313 -14.485 -32.845 1.00 68.29 C ANISOU 2392 CE2 TYR B 231 8751 7374 9820 -160 -431 -714 C ATOM 2393 CZ TYR B 231 15.257 -15.355 -33.062 1.00 75.91 C ANISOU 2393 CZ TYR B 231 9863 8288 10692 -255 -532 -681 C ATOM 2394 OH TYR B 231 14.829 -15.615 -34.341 1.00 78.14 O ANISOU 2394 OH TYR B 231 10316 8551 10823 -364 -494 -738 O ATOM 2395 N PHE B 232 19.396 -15.873 -29.781 1.00 64.59 N ANISOU 2395 N PHE B 232 7915 6669 9956 290 -533 -787 N ATOM 2396 CA PHE B 232 20.348 -16.449 -30.737 1.00 66.18 C ANISOU 2396 CA PHE B 232 8127 6774 10246 360 -380 -946 C ATOM 2397 C PHE B 232 20.944 -17.766 -30.232 1.00 71.71 C ANISOU 2397 C PHE B 232 8833 7295 11118 493 -445 -991 C ATOM 2398 O PHE B 232 21.301 -18.620 -31.044 1.00 72.86 O ANISOU 2398 O PHE B 232 9065 7317 11301 531 -340 -1115 O ATOM 2399 CB PHE B 232 21.446 -15.443 -31.131 1.00 68.28 C ANISOU 2399 CB PHE B 232 8224 7120 10601 405 -223 -1025 C ATOM 2400 CG PHE B 232 20.979 -14.326 -32.038 1.00 69.04 C ANISOU 2400 CG PHE B 232 8367 7347 10520 274 -112 -1015 C ATOM 2401 CD1 PHE B 232 20.704 -14.565 -33.380 1.00 73.07 C ANISOU 2401 CD1 PHE B 232 9043 7835 10886 189 22 -1098 C ATOM 2402 CD2 PHE B 232 20.847 -13.028 -31.559 1.00 69.65 C ANISOU 2402 CD2 PHE B 232 8338 7557 10569 234 -146 -925 C ATOM 2403 CE1 PHE B 232 20.270 -13.531 -34.217 1.00 73.40 C ANISOU 2403 CE1 PHE B 232 9148 7988 10754 66 102 -1073 C ATOM 2404 CE2 PHE B 232 20.417 -11.995 -32.397 1.00 71.86 C ANISOU 2404 CE2 PHE B 232 8671 7938 10693 120 -56 -905 C ATOM 2405 CZ PHE B 232 20.133 -12.253 -33.720 1.00 70.84 C ANISOU 2405 CZ PHE B 232 8709 7788 10419 37 61 -972 C ATOM 2406 N GLY B 233 21.003 -17.921 -28.907 1.00 68.08 N ANISOU 2406 N GLY B 233 8306 6815 10748 556 -621 -887 N ATOM 2407 CA GLY B 233 21.475 -19.127 -28.235 1.00 69.50 C ANISOU 2407 CA GLY B 233 8503 6819 11084 681 -733 -889 C ATOM 2408 C GLY B 233 20.509 -20.283 -28.408 1.00 74.40 C ANISOU 2408 C GLY B 233 9351 7314 11602 610 -794 -864 C ATOM 2409 O GLY B 233 20.936 -21.408 -28.682 1.00 75.57 O ANISOU 2409 O GLY B 233 9574 7282 11858 697 -779 -947 O ATOM 2410 N ILE B 234 19.190 -20.003 -28.268 1.00 70.25 N ANISOU 2410 N ILE B 234 8933 6879 10882 449 -859 -753 N ATOM 2411 CA ILE B 234 18.105 -20.974 -28.470 1.00 70.78 C ANISOU 2411 CA ILE B 234 9206 6852 10834 337 -920 -717 C ATOM 2412 C ILE B 234 18.074 -21.356 -29.964 1.00 76.86 C ANISOU 2412 C ILE B 234 10098 7567 11537 288 -771 -863 C ATOM 2413 O ILE B 234 17.925 -22.535 -30.291 1.00 78.04 O ANISOU 2413 O ILE B 234 10409 7546 11696 283 -784 -918 O ATOM 2414 CB ILE B 234 16.735 -20.432 -27.943 1.00 72.13 C ANISOU 2414 CB ILE B 234 9411 7157 10839 177 -1012 -563 C ATOM 2415 CG1 ILE B 234 16.732 -20.338 -26.398 1.00 71.94 C ANISOU 2415 CG1 ILE B 234 9328 7144 10861 218 -1154 -428 C ATOM 2416 CG2 ILE B 234 15.549 -21.287 -28.431 1.00 73.41 C ANISOU 2416 CG2 ILE B 234 9764 7251 10878 26 -1050 -542 C ATOM 2417 CD1 ILE B 234 15.667 -19.400 -25.785 1.00 76.47 C ANISOU 2417 CD1 ILE B 234 9866 7888 11302 96 -1192 -297 C ATOM 2418 N ARG B 235 18.271 -20.357 -30.854 1.00 73.51 N ANISOU 2418 N ARG B 235 9612 7276 11042 251 -629 -928 N ATOM 2419 CA ARG B 235 18.315 -20.529 -32.310 1.00 74.68 C ANISOU 2419 CA ARG B 235 9887 7394 11095 193 -470 -1069 C ATOM 2420 C ARG B 235 19.498 -21.408 -32.745 1.00 81.47 C ANISOU 2420 C ARG B 235 10759 8078 12118 342 -343 -1237 C ATOM 2421 O ARG B 235 19.366 -22.168 -33.702 1.00 82.39 O ANISOU 2421 O ARG B 235 11059 8081 12164 299 -257 -1353 O ATOM 2422 CB ARG B 235 18.378 -19.166 -33.018 1.00 73.69 C ANISOU 2422 CB ARG B 235 9686 7448 10864 129 -350 -1081 C ATOM 2423 CG ARG B 235 17.501 -19.105 -34.256 1.00 83.45 C ANISOU 2423 CG ARG B 235 11114 8719 11874 -40 -305 -1112 C ATOM 2424 CD ARG B 235 17.819 -17.934 -35.165 1.00 93.81 C ANISOU 2424 CD ARG B 235 12394 10161 13089 -86 -154 -1154 C ATOM 2425 NE ARG B 235 16.740 -17.696 -36.129 1.00103.23 N ANISOU 2425 NE ARG B 235 13765 11414 14044 -265 -183 -1125 N ATOM 2426 CZ ARG B 235 16.648 -18.273 -37.325 1.00117.99 C ANISOU 2426 CZ ARG B 235 15850 13206 15775 -347 -99 -1241 C ATOM 2427 NH1 ARG B 235 17.576 -19.133 -37.729 1.00107.37 N ANISOU 2427 NH1 ARG B 235 14571 11714 14512 -258 50 -1407 N ATOM 2428 NH2 ARG B 235 15.628 -17.995 -38.125 1.00103.18 N ANISOU 2428 NH2 ARG B 235 14130 11394 13681 -518 -168 -1194 N ATOM 2429 N LYS B 236 20.642 -21.306 -32.034 1.00 79.16 N ANISOU 2429 N LYS B 236 10269 7759 12049 517 -336 -1254 N ATOM 2430 CA LYS B 236 21.867 -22.068 -32.303 1.00 81.62 C ANISOU 2430 CA LYS B 236 10530 7907 12575 692 -220 -1407 C ATOM 2431 C LYS B 236 21.702 -23.555 -31.967 1.00 87.81 C ANISOU 2431 C LYS B 236 11466 8459 13438 754 -328 -1415 C ATOM 2432 O LYS B 236 22.198 -24.403 -32.710 1.00 89.47 O ANISOU 2432 O LYS B 236 11769 8504 13722 827 -198 -1571 O ATOM 2433 CB LYS B 236 23.053 -21.467 -31.525 1.00 84.21 C ANISOU 2433 CB LYS B 236 10573 8286 13135 851 -228 -1395 C ATOM 2434 CG LYS B 236 24.425 -21.859 -32.068 1.00101.87 C ANISOU 2434 CG LYS B 236 12688 10413 15607 1022 -42 -1575 C ATOM 2435 CD LYS B 236 25.566 -21.231 -31.268 1.00113.24 C ANISOU 2435 CD LYS B 236 13821 11914 17293 1164 -79 -1553 C ATOM 2436 CE LYS B 236 26.056 -22.113 -30.142 1.00126.86 C ANISOU 2436 CE LYS B 236 15470 13482 19248 1336 -285 -1495 C ATOM 2437 NZ LYS B 236 27.174 -21.480 -29.395 1.00137.07 N ANISOU 2437 NZ LYS B 236 16460 14840 20781 1462 -345 -1474 N ATOM 2438 N HIS B 237 21.015 -23.862 -30.850 1.00 84.24 N ANISOU 2438 N HIS B 237 11052 7986 12969 723 -553 -1250 N ATOM 2439 CA HIS B 237 20.773 -25.223 -30.365 1.00 85.85 C ANISOU 2439 CA HIS B 237 11412 7969 13238 763 -685 -1220 C ATOM 2440 C HIS B 237 19.667 -25.954 -31.144 1.00 90.60 C ANISOU 2440 C HIS B 237 12287 8489 13648 591 -676 -1250 C ATOM 2441 O HIS B 237 19.720 -27.180 -31.269 1.00 92.02 O ANISOU 2441 O HIS B 237 12627 8442 13894 634 -695 -1311 O ATOM 2442 CB HIS B 237 20.448 -25.194 -28.861 1.00 85.80 C ANISOU 2442 CB HIS B 237 11356 7982 13260 770 -918 -1023 C ATOM 2443 CG HIS B 237 20.497 -26.537 -28.201 1.00 91.17 C ANISOU 2443 CG HIS B 237 12168 8418 14053 849 -1062 -980 C ATOM 2444 ND1 HIS B 237 19.381 -27.353 -28.140 1.00 93.23 N ANISOU 2444 ND1 HIS B 237 12662 8581 14179 703 -1149 -912 N ATOM 2445 CD2 HIS B 237 21.531 -27.165 -27.594 1.00 94.85 C ANISOU 2445 CD2 HIS B 237 12560 8719 14760 1056 -1138 -992 C ATOM 2446 CE1 HIS B 237 19.770 -28.447 -27.504 1.00 94.49 C ANISOU 2446 CE1 HIS B 237 12902 8511 14488 820 -1267 -882 C ATOM 2447 NE2 HIS B 237 21.055 -28.380 -27.156 1.00 95.89 N ANISOU 2447 NE2 HIS B 237 12901 8637 14895 1041 -1273 -926 N ATOM 2448 N LEU B 238 18.671 -25.205 -31.654 1.00 85.99 N ANISOU 2448 N LEU B 238 11754 8081 12837 396 -659 -1205 N ATOM 2449 CA LEU B 238 17.520 -25.741 -32.385 1.00 86.37 C ANISOU 2449 CA LEU B 238 12039 8088 12690 202 -681 -1216 C ATOM 2450 C LEU B 238 17.770 -26.006 -33.874 1.00 92.47 C ANISOU 2450 C LEU B 238 12961 8795 13377 168 -495 -1413 C ATOM 2451 O LEU B 238 17.379 -27.065 -34.367 1.00 93.78 O ANISOU 2451 O LEU B 238 13353 8787 13491 103 -505 -1485 O ATOM 2452 CB LEU B 238 16.299 -24.816 -32.200 1.00 84.32 C ANISOU 2452 CB LEU B 238 11748 8045 12245 14 -774 -1064 C ATOM 2453 CG LEU B 238 15.244 -25.227 -31.159 1.00 88.36 C ANISOU 2453 CG LEU B 238 12304 8544 12726 -88 -966 -889 C ATOM 2454 CD1 LEU B 238 15.774 -25.120 -29.737 1.00 87.88 C ANISOU 2454 CD1 LEU B 238 12100 8477 12812 47 -1060 -778 C ATOM 2455 CD2 LEU B 238 14.012 -24.357 -31.272 1.00 89.21 C ANISOU 2455 CD2 LEU B 238 12381 8855 12660 -276 -1018 -778 C ATOM 2456 N LEU B 239 18.403 -25.050 -34.586 1.00 89.31 N ANISOU 2456 N LEU B 239 12456 8528 12951 199 -320 -1500 N ATOM 2457 CA LEU B 239 18.666 -25.131 -36.030 1.00 90.99 C ANISOU 2457 CA LEU B 239 12820 8705 13048 151 -116 -1685 C ATOM 2458 C LEU B 239 19.710 -26.176 -36.452 1.00 98.04 C ANISOU 2458 C LEU B 239 13783 9364 14103 313 43 -1882 C ATOM 2459 O LEU B 239 19.658 -26.637 -37.595 1.00 99.44 O ANISOU 2459 O LEU B 239 14178 9451 14154 243 182 -2039 O ATOM 2460 CB LEU B 239 19.043 -23.748 -36.606 1.00 90.15 C ANISOU 2460 CB LEU B 239 12584 8808 12860 127 31 -1703 C ATOM 2461 CG LEU B 239 17.921 -22.852 -37.192 1.00 93.63 C ANISOU 2461 CG LEU B 239 13109 9434 13031 -91 -26 -1613 C ATOM 2462 CD1 LEU B 239 17.181 -23.524 -38.351 1.00 95.50 C ANISOU 2462 CD1 LEU B 239 13652 9586 13048 -260 -14 -1703 C ATOM 2463 CD2 LEU B 239 16.965 -22.345 -36.124 1.00 93.72 C ANISOU 2463 CD2 LEU B 239 13006 9573 13031 -156 -250 -1396 C ATOM 2464 N LYS B 240 20.650 -26.545 -35.558 1.00 95.45 N ANISOU 2464 N LYS B 240 13281 8933 14054 529 20 -1878 N ATOM 2465 CA LYS B 240 21.698 -27.531 -35.861 1.00 98.19 C ANISOU 2465 CA LYS B 240 13654 9046 14609 718 165 -2059 C ATOM 2466 C LYS B 240 21.167 -28.975 -35.978 1.00104.52 C ANISOU 2466 C LYS B 240 14735 9588 15391 687 86 -2106 C ATOM 2467 O LYS B 240 21.816 -29.814 -36.610 1.00106.73 O ANISOU 2467 O LYS B 240 15122 9662 15769 795 247 -2295 O ATOM 2468 CB LYS B 240 22.874 -27.441 -34.863 1.00100.76 C ANISOU 2468 CB LYS B 240 13684 9342 15257 964 136 -2028 C ATOM 2469 CG LYS B 240 22.532 -27.766 -33.409 1.00111.26 C ANISOU 2469 CG LYS B 240 14957 10632 16687 1007 -153 -1827 C ATOM 2470 CD LYS B 240 23.772 -27.722 -32.531 1.00120.49 C ANISOU 2470 CD LYS B 240 15852 11757 18172 1251 -193 -1811 C ATOM 2471 CE LYS B 240 23.467 -28.091 -31.101 1.00129.07 C ANISOU 2471 CE LYS B 240 16922 12786 19332 1288 -484 -1612 C ATOM 2472 NZ LYS B 240 24.686 -28.045 -30.253 1.00138.62 N ANISOU 2472 NZ LYS B 240 17872 13952 20846 1521 -557 -1590 N ATOM 2473 N THR B 241 19.990 -29.249 -35.377 1.00100.13 N ANISOU 2473 N THR B 241 14294 9037 14712 535 -148 -1939 N ATOM 2474 CA THR B 241 19.335 -30.559 -35.364 1.00101.53 C ANISOU 2474 CA THR B 241 14737 8980 14860 465 -258 -1949 C ATOM 2475 C THR B 241 18.849 -31.036 -36.739 1.00107.05 C ANISOU 2475 C THR B 241 15732 9594 15347 305 -135 -2118 C ATOM 2476 O THR B 241 18.885 -32.243 -36.994 1.00108.98 O ANISOU 2476 O THR B 241 16192 9575 15640 331 -123 -2226 O ATOM 2477 CB THR B 241 18.195 -30.565 -34.343 1.00108.18 C ANISOU 2477 CB THR B 241 15592 9887 15625 322 -520 -1716 C ATOM 2478 N ASN B 242 18.389 -30.098 -37.612 1.00102.31 N ANISOU 2478 N ASN B 242 15160 9205 14508 137 -58 -2137 N ATOM 2479 CA ASN B 242 17.850 -30.353 -38.961 1.00103.36 C ANISOU 2479 CA ASN B 242 15585 9301 14388 -49 35 -2279 C ATOM 2480 C ASN B 242 16.660 -31.333 -38.903 1.00106.97 C ANISOU 2480 C ASN B 242 16294 9618 14729 -239 -167 -2225 C ATOM 2481 O ASN B 242 16.776 -32.504 -39.276 1.00108.76 O ANISOU 2481 O ASN B 242 16755 9585 14985 -225 -127 -2364 O ATOM 2482 CB ASN B 242 18.953 -30.788 -39.954 1.00107.42 C ANISOU 2482 CB ASN B 242 16204 9657 14954 82 328 -2546 C ATOM 2483 CG ASN B 242 18.528 -30.827 -41.406 1.00132.82 C ANISOU 2483 CG ASN B 242 19723 12870 17873 -114 455 -2702 C ATOM 2484 OD1 ASN B 242 17.922 -29.888 -41.939 1.00126.08 O ANISOU 2484 OD1 ASN B 242 18891 12233 16781 -292 430 -2639 O ATOM 2485 ND2 ASN B 242 18.887 -31.900 -42.096 1.00127.77 N ANISOU 2485 ND2 ASN B 242 19334 11975 17240 -77 599 -2916 N ATOM 2486 N SER B 243 15.526 -30.836 -38.379 1.00100.92 N ANISOU 2486 N SER B 243 15466 9024 13854 -413 -380 -2019 N ATOM 2487 CA SER B 243 14.294 -31.596 -38.166 1.00100.67 C ANISOU 2487 CA SER B 243 15610 8907 13732 -616 -591 -1926 C ATOM 2488 C SER B 243 13.404 -31.739 -39.408 1.00104.43 C ANISOU 2488 C SER B 243 16352 9392 13934 -873 -613 -2011 C ATOM 2489 O SER B 243 13.504 -30.946 -40.347 1.00103.69 O ANISOU 2489 O SER B 243 16280 9444 13674 -928 -504 -2083 O ATOM 2490 CB SER B 243 13.500 -31.000 -37.005 1.00101.76 C ANISOU 2490 CB SER B 243 15539 9227 13899 -681 -789 -1672 C ATOM 2491 OG SER B 243 14.243 -31.014 -35.796 1.00109.72 O ANISOU 2491 OG SER B 243 16350 10199 15138 -469 -804 -1587 O ATOM 2492 N TYR B 244 12.531 -32.764 -39.390 1.00101.55 N ANISOU 2492 N TYR B 244 16200 8864 13521 -1040 -766 -1995 N ATOM 2493 CA TYR B 244 11.560 -33.085 -40.439 1.00102.54 C ANISOU 2493 CA TYR B 244 16594 8967 13399 -1312 -847 -2060 C ATOM 2494 C TYR B 244 10.205 -33.408 -39.793 1.00105.84 C ANISOU 2494 C TYR B 244 17002 9411 13800 -1529 -1110 -1870 C ATOM 2495 O TYR B 244 10.164 -33.933 -38.678 1.00105.08 O ANISOU 2495 O TYR B 244 16825 9218 13883 -1463 -1189 -1758 O ATOM 2496 CB TYR B 244 12.028 -34.294 -41.273 1.00106.78 C ANISOU 2496 CB TYR B 244 17467 9199 13906 -1302 -725 -2304 C ATOM 2497 CG TYR B 244 13.378 -34.135 -41.939 1.00109.23 C ANISOU 2497 CG TYR B 244 17800 9450 14252 -1089 -432 -2516 C ATOM 2498 CD1 TYR B 244 13.499 -33.506 -43.174 1.00111.76 C ANISOU 2498 CD1 TYR B 244 18243 9885 14338 -1176 -291 -2646 C ATOM 2499 CD2 TYR B 244 14.527 -34.676 -41.368 1.00110.69 C ANISOU 2499 CD2 TYR B 244 17900 9450 14707 -809 -293 -2593 C ATOM 2500 CE1 TYR B 244 14.736 -33.379 -43.805 1.00113.77 C ANISOU 2500 CE1 TYR B 244 18520 10083 14624 -995 10 -2849 C ATOM 2501 CE2 TYR B 244 15.769 -34.556 -41.989 1.00112.93 C ANISOU 2501 CE2 TYR B 244 18178 9677 15051 -613 -6 -2797 C ATOM 2502 CZ TYR B 244 15.870 -33.907 -43.209 1.00120.61 C ANISOU 2502 CZ TYR B 244 19266 10774 15786 -711 160 -2928 C ATOM 2503 OH TYR B 244 17.092 -33.787 -43.825 1.00122.70 O ANISOU 2503 OH TYR B 244 19522 10986 16111 -531 471 -3133 O ATOM 2504 N GLY B 245 9.122 -33.105 -40.505 1.00102.56 N ANISOU 2504 N GLY B 245 16674 9121 13173 -1788 -1242 -1834 N ATOM 2505 CA GLY B 245 7.757 -33.360 -40.052 1.00102.17 C ANISOU 2505 CA GLY B 245 16601 9115 13104 -2024 -1484 -1666 C ATOM 2506 C GLY B 245 7.293 -32.434 -38.949 1.00103.16 C ANISOU 2506 C GLY B 245 16385 9479 13334 -1995 -1571 -1429 C ATOM 2507 O GLY B 245 7.570 -31.232 -38.996 1.00100.80 O ANISOU 2507 O GLY B 245 15889 9401 13008 -1904 -1507 -1382 O ATOM 2508 N LYS B 246 6.585 -32.995 -37.942 1.00 99.64 N ANISOU 2508 N LYS B 246 15879 8979 13002 -2080 -1707 -1280 N ATOM 2509 CA LYS B 246 6.058 -32.258 -36.784 1.00 97.24 C ANISOU 2509 CA LYS B 246 15275 8875 12797 -2070 -1781 -1057 C ATOM 2510 C LYS B 246 7.179 -31.685 -35.910 1.00 99.48 C ANISOU 2510 C LYS B 246 15365 9207 13226 -1781 -1646 -1025 C ATOM 2511 O LYS B 246 6.982 -30.646 -35.281 1.00 96.86 O ANISOU 2511 O LYS B 246 14781 9098 12925 -1738 -1656 -886 O ATOM 2512 CB LYS B 246 5.114 -33.136 -35.948 1.00100.61 C ANISOU 2512 CB LYS B 246 15728 9198 13302 -2238 -1925 -925 C ATOM 2513 CG LYS B 246 4.082 -32.337 -35.157 1.00113.74 C ANISOU 2513 CG LYS B 246 17115 11104 14996 -2346 -2023 -709 C ATOM 2514 CD LYS B 246 3.411 -33.171 -34.079 1.00125.04 C ANISOU 2514 CD LYS B 246 18549 12427 16535 -2462 -2108 -571 C ATOM 2515 CE LYS B 246 2.475 -32.339 -33.236 1.00134.99 C ANISOU 2515 CE LYS B 246 19522 13929 17837 -2545 -2159 -369 C ATOM 2516 NZ LYS B 246 1.878 -33.129 -32.128 1.00145.02 N ANISOU 2516 NZ LYS B 246 20801 15096 19204 -2660 -2208 -232 N ATOM 2517 N ASN B 247 8.355 -32.354 -35.891 1.00 97.25 N ANISOU 2517 N ASN B 247 15200 8711 13041 -1583 -1524 -1159 N ATOM 2518 CA ASN B 247 9.547 -31.928 -35.150 1.00 95.80 C ANISOU 2518 CA ASN B 247 14845 8544 13013 -1303 -1408 -1151 C ATOM 2519 C ASN B 247 10.069 -30.594 -35.688 1.00 97.75 C ANISOU 2519 C ASN B 247 14925 9019 13196 -1209 -1289 -1192 C ATOM 2520 O ASN B 247 10.625 -29.811 -34.923 1.00 95.48 O ANISOU 2520 O ASN B 247 14413 8856 13011 -1049 -1246 -1113 O ATOM 2521 CB ASN B 247 10.644 -32.993 -35.221 1.00 99.11 C ANISOU 2521 CB ASN B 247 15429 8668 13558 -1122 -1310 -1306 C ATOM 2522 CG ASN B 247 10.277 -34.301 -34.566 1.00125.78 C ANISOU 2522 CG ASN B 247 18974 11792 17023 -1182 -1425 -1253 C ATOM 2523 OD1 ASN B 247 10.122 -34.394 -33.343 1.00120.55 O ANISOU 2523 OD1 ASN B 247 18207 11128 16467 -1150 -1515 -1084 O ATOM 2524 ND2 ASN B 247 10.154 -35.349 -35.367 1.00120.15 N ANISOU 2524 ND2 ASN B 247 18546 10846 16259 -1275 -1420 -1399 N ATOM 2525 N ARG B 248 9.879 -30.343 -37.000 1.00 95.07 N ANISOU 2525 N ARG B 248 14716 8727 12679 -1321 -1242 -1312 N ATOM 2526 CA ARG B 248 10.264 -29.115 -37.696 1.00 93.79 C ANISOU 2526 CA ARG B 248 14450 8767 12418 -1276 -1132 -1353 C ATOM 2527 C ARG B 248 9.202 -28.030 -37.462 1.00 95.57 C ANISOU 2527 C ARG B 248 14491 9256 12565 -1412 -1264 -1169 C ATOM 2528 O ARG B 248 9.556 -26.864 -37.282 1.00 93.11 O ANISOU 2528 O ARG B 248 13981 9128 12267 -1313 -1200 -1114 O ATOM 2529 CB ARG B 248 10.449 -29.392 -39.200 1.00 96.56 C ANISOU 2529 CB ARG B 248 15066 9038 12586 -1360 -1036 -1553 C ATOM 2530 CG ARG B 248 11.099 -28.254 -39.977 1.00107.99 C ANISOU 2530 CG ARG B 248 16450 10647 13933 -1292 -876 -1622 C ATOM 2531 CD ARG B 248 11.209 -28.569 -41.457 1.00122.48 C ANISOU 2531 CD ARG B 248 18585 12398 15553 -1401 -779 -1815 C ATOM 2532 NE ARG B 248 11.482 -27.365 -42.245 1.00132.91 N ANISOU 2532 NE ARG B 248 19868 13908 16722 -1410 -673 -1833 N ATOM 2533 CZ ARG B 248 12.698 -26.917 -42.545 1.00148.46 C ANISOU 2533 CZ ARG B 248 21789 15887 18733 -1241 -428 -1951 C ATOM 2534 NH1 ARG B 248 13.776 -27.571 -42.131 1.00137.24 N ANISOU 2534 NH1 ARG B 248 20328 14299 17516 -1034 -268 -2065 N ATOM 2535 NH2 ARG B 248 12.844 -25.811 -43.263 1.00135.27 N ANISOU 2535 NH2 ARG B 248 20102 14387 16907 -1280 -343 -1949 N ATOM 2536 N ILE B 249 7.906 -28.421 -37.464 1.00 92.93 N ANISOU 2536 N ILE B 249 14217 8930 12163 -1637 -1445 -1076 N ATOM 2537 CA ILE B 249 6.756 -27.531 -37.244 1.00 91.44 C ANISOU 2537 CA ILE B 249 13847 8969 11928 -1777 -1584 -902 C ATOM 2538 C ILE B 249 6.790 -26.972 -35.810 1.00 93.18 C ANISOU 2538 C ILE B 249 13797 9297 12309 -1655 -1582 -739 C ATOM 2539 O ILE B 249 6.683 -25.757 -35.634 1.00 91.19 O ANISOU 2539 O ILE B 249 13345 9252 12051 -1611 -1568 -653 O ATOM 2540 CB ILE B 249 5.402 -28.226 -37.606 1.00 96.18 C ANISOU 2540 CB ILE B 249 14567 9529 12446 -2053 -1777 -856 C ATOM 2541 CG1 ILE B 249 5.382 -28.679 -39.088 1.00 98.80 C ANISOU 2541 CG1 ILE B 249 15192 9764 12585 -2186 -1790 -1025 C ATOM 2542 CG2 ILE B 249 4.196 -27.318 -37.301 1.00 95.81 C ANISOU 2542 CG2 ILE B 249 14289 9717 12397 -2181 -1918 -669 C ATOM 2543 CD1 ILE B 249 4.470 -29.881 -39.401 1.00108.61 C ANISOU 2543 CD1 ILE B 249 16644 10845 13777 -2427 -1949 -1050 C ATOM 2544 N THR B 250 6.978 -27.853 -34.802 1.00 89.98 N ANISOU 2544 N THR B 250 13409 8740 12038 -1600 -1594 -702 N ATOM 2545 CA THR B 250 7.062 -27.475 -33.384 1.00 88.16 C ANISOU 2545 CA THR B 250 12975 8582 11941 -1493 -1594 -556 C ATOM 2546 C THR B 250 8.323 -26.659 -33.082 1.00 90.21 C ANISOU 2546 C THR B 250 13100 8906 12271 -1249 -1461 -594 C ATOM 2547 O THR B 250 8.293 -25.820 -32.183 1.00 88.21 O ANISOU 2547 O THR B 250 12646 8798 12072 -1182 -1459 -476 O ATOM 2548 CB THR B 250 6.911 -28.690 -32.456 1.00 98.61 C ANISOU 2548 CB THR B 250 14397 9709 13362 -1520 -1656 -500 C ATOM 2549 OG1 THR B 250 7.821 -29.717 -32.854 1.00100.99 O ANISOU 2549 OG1 THR B 250 14907 9761 13702 -1423 -1601 -652 O ATOM 2550 CG2 THR B 250 5.485 -29.231 -32.422 1.00 98.49 C ANISOU 2550 CG2 THR B 250 14429 9689 13302 -1785 -1792 -405 C ATOM 2551 N ARG B 251 9.416 -26.891 -33.846 1.00 87.29 N ANISOU 2551 N ARG B 251 12837 8426 11901 -1124 -1341 -766 N ATOM 2552 CA ARG B 251 10.690 -26.173 -33.728 1.00 86.03 C ANISOU 2552 CA ARG B 251 12548 8317 11822 -904 -1202 -827 C ATOM 2553 C ARG B 251 10.493 -24.711 -34.148 1.00 88.33 C ANISOU 2553 C ARG B 251 12689 8854 12020 -929 -1165 -786 C ATOM 2554 O ARG B 251 10.872 -23.815 -33.395 1.00 86.37 O ANISOU 2554 O ARG B 251 12241 8729 11845 -817 -1136 -710 O ATOM 2555 CB ARG B 251 11.770 -26.845 -34.597 1.00 87.89 C ANISOU 2555 CB ARG B 251 12942 8372 12081 -795 -1065 -1033 C ATOM 2556 CG ARG B 251 13.180 -26.285 -34.430 1.00 97.02 C ANISOU 2556 CG ARG B 251 13949 9549 13364 -562 -914 -1107 C ATOM 2557 CD ARG B 251 14.118 -26.791 -35.512 1.00107.80 C ANISOU 2557 CD ARG B 251 15459 10770 14732 -481 -741 -1325 C ATOM 2558 NE ARG B 251 13.851 -26.164 -36.809 1.00116.29 N ANISOU 2558 NE ARG B 251 16626 11956 15603 -607 -656 -1405 N ATOM 2559 CZ ARG B 251 14.386 -26.558 -37.961 1.00133.59 C ANISOU 2559 CZ ARG B 251 19000 14040 17719 -604 -499 -1598 C ATOM 2560 NH1 ARG B 251 15.221 -27.590 -37.996 1.00123.49 N ANISOU 2560 NH1 ARG B 251 17814 12533 16574 -468 -399 -1742 N ATOM 2561 NH2 ARG B 251 14.084 -25.928 -39.089 1.00121.00 N ANISOU 2561 NH2 ARG B 251 17507 12557 15910 -736 -439 -1650 N ATOM 2562 N ASP B 252 9.872 -24.483 -35.331 1.00 85.50 N ANISOU 2562 N ASP B 252 12438 8554 11494 -1083 -1181 -831 N ATOM 2563 CA ASP B 252 9.586 -23.160 -35.894 1.00 84.33 C ANISOU 2563 CA ASP B 252 12189 8614 11237 -1126 -1166 -788 C ATOM 2564 C ASP B 252 8.634 -22.338 -35.023 1.00 86.71 C ANISOU 2564 C ASP B 252 12283 9091 11572 -1177 -1278 -597 C ATOM 2565 O ASP B 252 8.803 -21.121 -34.927 1.00 84.74 O ANISOU 2565 O ASP B 252 11879 8998 11321 -1114 -1233 -545 O ATOM 2566 CB ASP B 252 9.043 -23.276 -37.329 1.00 87.72 C ANISOU 2566 CB ASP B 252 12822 9040 11467 -1299 -1199 -866 C ATOM 2567 CG ASP B 252 10.036 -23.807 -38.350 1.00 99.86 C ANISOU 2567 CG ASP B 252 14570 10435 12936 -1248 -1041 -1073 C ATOM 2568 OD1 ASP B 252 11.222 -23.408 -38.294 1.00100.05 O ANISOU 2568 OD1 ASP B 252 14518 10459 13037 -1073 -867 -1150 O ATOM 2569 OD2 ASP B 252 9.615 -24.577 -39.240 1.00107.70 O ANISOU 2569 OD2 ASP B 252 15803 11321 13796 -1392 -1085 -1162 O ATOM 2570 N GLN B 253 7.648 -23.004 -34.385 1.00 83.84 N ANISOU 2570 N GLN B 253 11920 8693 11244 -1292 -1408 -497 N ATOM 2571 CA GLN B 253 6.674 -22.367 -33.492 1.00 82.67 C ANISOU 2571 CA GLN B 253 11576 8694 11142 -1348 -1492 -324 C ATOM 2572 C GLN B 253 7.349 -21.823 -32.224 1.00 85.34 C ANISOU 2572 C GLN B 253 11746 9078 11600 -1174 -1420 -262 C ATOM 2573 O GLN B 253 6.974 -20.747 -31.756 1.00 83.66 O ANISOU 2573 O GLN B 253 11357 9028 11403 -1157 -1419 -163 O ATOM 2574 CB GLN B 253 5.524 -23.327 -33.149 1.00 85.17 C ANISOU 2574 CB GLN B 253 11944 8945 11473 -1527 -1623 -246 C ATOM 2575 CG GLN B 253 4.534 -23.520 -34.298 1.00102.57 C ANISOU 2575 CG GLN B 253 14245 11168 13558 -1735 -1741 -261 C ATOM 2576 CD GLN B 253 3.518 -24.600 -34.020 1.00123.48 C ANISOU 2576 CD GLN B 253 16958 13725 16234 -1924 -1865 -205 C ATOM 2577 OE1 GLN B 253 2.351 -24.325 -33.721 1.00119.43 O ANISOU 2577 OE1 GLN B 253 16300 13327 15751 -2058 -1962 -78 O ATOM 2578 NE2 GLN B 253 3.930 -25.855 -34.126 1.00116.88 N ANISOU 2578 NE2 GLN B 253 16336 12672 15399 -1943 -1858 -301 N ATOM 2579 N VAL B 254 8.363 -22.549 -31.697 1.00 82.33 N ANISOU 2579 N VAL B 254 11428 8546 11307 -1043 -1365 -325 N ATOM 2580 CA VAL B 254 9.155 -22.159 -30.521 1.00 81.05 C ANISOU 2580 CA VAL B 254 11137 8402 11255 -876 -1320 -280 C ATOM 2581 C VAL B 254 10.019 -20.933 -30.879 1.00 84.16 C ANISOU 2581 C VAL B 254 11411 8916 11649 -751 -1213 -334 C ATOM 2582 O VAL B 254 10.105 -19.991 -30.087 1.00 82.23 O ANISOU 2582 O VAL B 254 11008 8792 11444 -686 -1200 -255 O ATOM 2583 CB VAL B 254 9.987 -23.357 -29.965 1.00 85.85 C ANISOU 2583 CB VAL B 254 11857 8797 11967 -773 -1323 -330 C ATOM 2584 CG1 VAL B 254 11.095 -22.903 -29.015 1.00 84.80 C ANISOU 2584 CG1 VAL B 254 11600 8675 11946 -579 -1283 -317 C ATOM 2585 CG2 VAL B 254 9.087 -24.372 -29.274 1.00 86.54 C ANISOU 2585 CG2 VAL B 254 12038 8783 12061 -900 -1430 -232 C ATOM 2586 N LEU B 255 10.619 -20.943 -32.090 1.00 81.85 N ANISOU 2586 N LEU B 255 11210 8587 11304 -732 -1130 -471 N ATOM 2587 CA LEU B 255 11.464 -19.864 -32.615 1.00 81.09 C ANISOU 2587 CA LEU B 255 11028 8586 11195 -639 -1009 -535 C ATOM 2588 C LEU B 255 10.675 -18.576 -32.861 1.00 84.26 C ANISOU 2588 C LEU B 255 11328 9180 11507 -719 -1036 -440 C ATOM 2589 O LEU B 255 11.233 -17.490 -32.710 1.00 82.76 O ANISOU 2589 O LEU B 255 11012 9089 11344 -634 -963 -431 O ATOM 2590 CB LEU B 255 12.196 -20.302 -33.899 1.00 82.54 C ANISOU 2590 CB LEU B 255 11366 8672 11324 -626 -895 -707 C ATOM 2591 CG LEU B 255 13.173 -21.477 -33.772 1.00 88.52 C ANISOU 2591 CG LEU B 255 12208 9227 12199 -507 -835 -827 C ATOM 2592 CD1 LEU B 255 13.348 -22.182 -35.096 1.00 90.58 C ANISOU 2592 CD1 LEU B 255 12684 9369 12362 -564 -751 -987 C ATOM 2593 CD2 LEU B 255 14.511 -21.042 -33.204 1.00 90.43 C ANISOU 2593 CD2 LEU B 255 12286 9472 12602 -310 -735 -868 C ATOM 2594 N LYS B 256 9.381 -18.697 -33.233 1.00 81.54 N ANISOU 2594 N LYS B 256 11032 8878 11071 -883 -1147 -368 N ATOM 2595 CA LYS B 256 8.486 -17.558 -33.466 1.00 80.66 C ANISOU 2595 CA LYS B 256 10818 8933 10895 -958 -1200 -265 C ATOM 2596 C LYS B 256 8.106 -16.901 -32.137 1.00 83.31 C ANISOU 2596 C LYS B 256 10960 9365 11330 -907 -1222 -137 C ATOM 2597 O LYS B 256 7.999 -15.675 -32.072 1.00 81.94 O ANISOU 2597 O LYS B 256 10664 9317 11154 -872 -1198 -82 O ATOM 2598 CB LYS B 256 7.231 -17.988 -34.242 1.00 84.37 C ANISOU 2598 CB LYS B 256 11383 9410 11265 -1148 -1333 -229 C ATOM 2599 CG LYS B 256 7.464 -18.132 -35.741 1.00100.71 C ANISOU 2599 CG LYS B 256 13645 11437 13181 -1219 -1316 -340 C ATOM 2600 CD LYS B 256 6.222 -18.646 -36.459 1.00112.56 C ANISOU 2600 CD LYS B 256 15252 12934 14582 -1421 -1482 -304 C ATOM 2601 CE LYS B 256 6.450 -18.862 -37.937 1.00125.66 C ANISOU 2601 CE LYS B 256 17147 14540 16059 -1508 -1474 -421 C ATOM 2602 NZ LYS B 256 7.259 -20.081 -38.210 1.00136.24 N ANISOU 2602 NZ LYS B 256 18686 15694 17386 -1485 -1380 -583 N ATOM 2603 N MET B 257 7.924 -17.719 -31.079 1.00 80.07 N ANISOU 2603 N MET B 257 10543 8884 10998 -904 -1260 -92 N ATOM 2604 CA MET B 257 7.595 -17.263 -29.724 1.00 79.02 C ANISOU 2604 CA MET B 257 10265 8821 10938 -866 -1267 20 C ATOM 2605 C MET B 257 8.812 -16.599 -29.076 1.00 80.84 C ANISOU 2605 C MET B 257 10419 9065 11230 -697 -1180 -14 C ATOM 2606 O MET B 257 8.659 -15.607 -28.362 1.00 79.71 O ANISOU 2606 O MET B 257 10148 9029 11111 -657 -1158 55 O ATOM 2607 CB MET B 257 7.092 -18.430 -28.857 1.00 82.38 C ANISOU 2607 CB MET B 257 10748 9149 11404 -932 -1328 75 C ATOM 2608 CG MET B 257 5.724 -18.938 -29.260 1.00 87.52 C ANISOU 2608 CG MET B 257 11424 9811 12018 -1119 -1420 135 C ATOM 2609 SD MET B 257 5.335 -20.548 -28.534 1.00 93.55 S ANISOU 2609 SD MET B 257 12319 10410 12818 -1219 -1482 171 S ATOM 2610 CE MET B 257 4.315 -20.040 -27.189 1.00 89.86 C ANISOU 2610 CE MET B 257 11684 10064 12396 -1273 -1471 330 C ATOM 2611 N ALA B 258 10.016 -17.145 -29.338 1.00 76.71 N ANISOU 2611 N ALA B 258 9972 8430 10743 -602 -1131 -126 N ATOM 2612 CA ALA B 258 11.286 -16.633 -28.827 1.00 75.50 C ANISOU 2612 CA ALA B 258 9738 8276 10671 -447 -1062 -172 C ATOM 2613 C ALA B 258 11.666 -15.308 -29.492 1.00 77.60 C ANISOU 2613 C ALA B 258 9920 8659 10907 -416 -977 -204 C ATOM 2614 O ALA B 258 12.289 -14.466 -28.847 1.00 76.57 O ANISOU 2614 O ALA B 258 9676 8585 10833 -327 -940 -192 O ATOM 2615 CB ALA B 258 12.386 -17.661 -29.036 1.00 77.38 C ANISOU 2615 CB ALA B 258 10064 8355 10983 -356 -1034 -285 C ATOM 2616 N ALA B 259 11.296 -15.126 -30.776 1.00 73.72 N ANISOU 2616 N ALA B 259 9498 8195 10316 -499 -954 -241 N ATOM 2617 CA ALA B 259 11.568 -13.900 -31.535 1.00 72.66 C ANISOU 2617 CA ALA B 259 9319 8158 10129 -492 -878 -260 C ATOM 2618 C ALA B 259 10.566 -12.799 -31.192 1.00 74.22 C ANISOU 2618 C ALA B 259 9412 8486 10301 -537 -930 -134 C ATOM 2619 O ALA B 259 10.885 -11.621 -31.339 1.00 72.81 O ANISOU 2619 O ALA B 259 9163 8384 10118 -499 -873 -125 O ATOM 2620 CB ALA B 259 11.535 -14.186 -33.029 1.00 74.56 C ANISOU 2620 CB ALA B 259 9712 8366 10251 -574 -844 -342 C ATOM 2621 N ALA B 260 9.355 -13.184 -30.749 1.00 70.33 N ANISOU 2621 N ALA B 260 8907 8013 9803 -619 -1031 -40 N ATOM 2622 CA ALA B 260 8.279 -12.262 -30.385 1.00 69.30 C ANISOU 2622 CA ALA B 260 8661 7996 9674 -657 -1077 78 C ATOM 2623 C ALA B 260 8.624 -11.388 -29.178 1.00 71.52 C ANISOU 2623 C ALA B 260 8814 8329 10030 -556 -1023 117 C ATOM 2624 O ALA B 260 8.258 -10.214 -29.171 1.00 70.45 O ANISOU 2624 O ALA B 260 8590 8280 9896 -542 -1007 170 O ATOM 2625 CB ALA B 260 6.994 -13.030 -30.130 1.00 70.69 C ANISOU 2625 CB ALA B 260 8837 8170 9853 -771 -1177 156 C ATOM 2626 N VAL B 261 9.340 -11.947 -28.176 1.00 67.71 N ANISOU 2626 N VAL B 261 8336 7784 9607 -488 -1006 91 N ATOM 2627 CA VAL B 261 9.732 -11.223 -26.955 1.00 66.49 C ANISOU 2627 CA VAL B 261 8092 7667 9506 -404 -972 120 C ATOM 2628 C VAL B 261 10.843 -10.186 -27.229 1.00 69.43 C ANISOU 2628 C VAL B 261 8416 8065 9899 -318 -897 55 C ATOM 2629 O VAL B 261 10.810 -9.106 -26.636 1.00 68.35 O ANISOU 2629 O VAL B 261 8199 7992 9779 -283 -868 91 O ATOM 2630 CB VAL B 261 10.064 -12.139 -25.739 1.00 70.42 C ANISOU 2630 CB VAL B 261 8626 8088 10043 -372 -1008 131 C ATOM 2631 CG1 VAL B 261 8.832 -12.911 -25.278 1.00 70.80 C ANISOU 2631 CG1 VAL B 261 8706 8127 10069 -475 -1061 217 C ATOM 2632 CG2 VAL B 261 11.225 -13.089 -26.024 1.00 70.75 C ANISOU 2632 CG2 VAL B 261 8744 8010 10126 -311 -1016 38 C ATOM 2633 N VAL B 262 11.804 -10.504 -28.129 1.00 65.95 N ANISOU 2633 N VAL B 262 8027 7570 9461 -292 -854 -43 N ATOM 2634 CA VAL B 262 12.893 -9.590 -28.494 1.00 65.30 C ANISOU 2634 CA VAL B 262 7894 7508 9407 -230 -766 -109 C ATOM 2635 C VAL B 262 12.357 -8.466 -29.415 1.00 68.01 C ANISOU 2635 C VAL B 262 8235 7929 9676 -285 -731 -74 C ATOM 2636 O VAL B 262 12.754 -7.311 -29.251 1.00 67.22 O ANISOU 2636 O VAL B 262 8068 7875 9599 -250 -680 -68 O ATOM 2637 CB VAL B 262 14.168 -10.314 -29.038 1.00 70.11 C ANISOU 2637 CB VAL B 262 8539 8031 10069 -177 -704 -232 C ATOM 2638 CG1 VAL B 262 13.922 -11.040 -30.358 1.00 70.97 C ANISOU 2638 CG1 VAL B 262 8776 8094 10096 -245 -678 -287 C ATOM 2639 CG2 VAL B 262 15.360 -9.366 -29.147 1.00 69.78 C ANISOU 2639 CG2 VAL B 262 8408 8016 10091 -115 -607 -295 C ATOM 2640 N LEU B 263 11.418 -8.798 -30.327 1.00 64.24 N ANISOU 2640 N LEU B 263 7836 7460 9111 -375 -777 -43 N ATOM 2641 CA LEU B 263 10.794 -7.844 -31.246 1.00 63.87 C ANISOU 2641 CA LEU B 263 7805 7475 8986 -431 -783 9 C ATOM 2642 C LEU B 263 9.889 -6.854 -30.507 1.00 65.74 C ANISOU 2642 C LEU B 263 7933 7785 9261 -417 -823 118 C ATOM 2643 O LEU B 263 9.951 -5.658 -30.791 1.00 65.06 O ANISOU 2643 O LEU B 263 7817 7736 9166 -399 -789 146 O ATOM 2644 CB LEU B 263 10.014 -8.575 -32.352 1.00 65.05 C ANISOU 2644 CB LEU B 263 8075 7607 9033 -539 -855 16 C ATOM 2645 CG LEU B 263 10.619 -8.529 -33.759 1.00 70.92 C ANISOU 2645 CG LEU B 263 8956 8324 9666 -584 -791 -61 C ATOM 2646 CD1 LEU B 263 11.769 -9.520 -33.910 1.00 71.75 C ANISOU 2646 CD1 LEU B 263 9130 8339 9793 -546 -695 -198 C ATOM 2647 CD2 LEU B 263 9.566 -8.831 -34.803 1.00 74.53 C ANISOU 2647 CD2 LEU B 263 9530 8791 9998 -707 -902 -16 C ATOM 2648 N ALA B 264 9.073 -7.346 -29.545 1.00 61.16 N ANISOU 2648 N ALA B 264 7297 7215 8726 -424 -881 177 N ATOM 2649 CA ALA B 264 8.170 -6.513 -28.742 1.00 60.04 C ANISOU 2649 CA ALA B 264 7045 7136 8632 -405 -893 268 C ATOM 2650 C ALA B 264 8.939 -5.544 -27.842 1.00 61.64 C ANISOU 2650 C ALA B 264 7189 7347 8883 -315 -814 245 C ATOM 2651 O ALA B 264 8.486 -4.417 -27.651 1.00 60.94 O ANISOU 2651 O ALA B 264 7037 7300 8819 -288 -793 295 O ATOM 2652 CB ALA B 264 7.239 -7.378 -27.911 1.00 60.95 C ANISOU 2652 CB ALA B 264 7126 7255 8779 -447 -942 321 C ATOM 2653 N PHE B 265 10.107 -5.971 -27.317 1.00 56.82 N ANISOU 2653 N PHE B 265 6602 6689 8296 -268 -780 168 N ATOM 2654 CA PHE B 265 10.972 -5.146 -26.468 1.00 55.58 C ANISOU 2654 CA PHE B 265 6399 6533 8184 -197 -727 136 C ATOM 2655 C PHE B 265 11.563 -3.979 -27.273 1.00 58.61 C ANISOU 2655 C PHE B 265 6775 6931 8565 -185 -665 109 C ATOM 2656 O PHE B 265 11.703 -2.883 -26.730 1.00 57.73 O ANISOU 2656 O PHE B 265 6618 6835 8481 -150 -629 119 O ATOM 2657 CB PHE B 265 12.087 -5.996 -25.830 1.00 57.32 C ANISOU 2657 CB PHE B 265 6638 6696 8444 -155 -739 66 C ATOM 2658 CG PHE B 265 12.851 -5.307 -24.721 1.00 58.56 C ANISOU 2658 CG PHE B 265 6750 6854 8645 -97 -725 44 C ATOM 2659 CD1 PHE B 265 12.378 -5.323 -23.413 1.00 61.52 C ANISOU 2659 CD1 PHE B 265 7128 7238 9009 -90 -756 91 C ATOM 2660 CD2 PHE B 265 14.053 -4.657 -24.981 1.00 60.58 C ANISOU 2660 CD2 PHE B 265 6968 7101 8950 -63 -681 -26 C ATOM 2661 CE1 PHE B 265 13.085 -4.683 -22.389 1.00 62.28 C ANISOU 2661 CE1 PHE B 265 7208 7331 9124 -49 -758 65 C ATOM 2662 CE2 PHE B 265 14.756 -4.014 -23.957 1.00 63.16 C ANISOU 2662 CE2 PHE B 265 7254 7426 9318 -24 -690 -48 C ATOM 2663 CZ PHE B 265 14.269 -4.034 -22.668 1.00 61.16 C ANISOU 2663 CZ PHE B 265 7023 7179 9037 -18 -737 -4 C ATOM 2664 N ILE B 266 11.887 -4.215 -28.567 1.00 55.00 N ANISOU 2664 N ILE B 266 6378 6457 8061 -223 -646 73 N ATOM 2665 CA ILE B 266 12.441 -3.204 -29.473 1.00 54.65 C ANISOU 2665 CA ILE B 266 6355 6418 7992 -235 -575 53 C ATOM 2666 C ILE B 266 11.371 -2.165 -29.845 1.00 58.48 C ANISOU 2666 C ILE B 266 6837 6938 8442 -256 -606 153 C ATOM 2667 O ILE B 266 11.560 -0.990 -29.551 1.00 57.87 O ANISOU 2667 O ILE B 266 6725 6864 8398 -224 -565 170 O ATOM 2668 CB ILE B 266 13.157 -3.834 -30.711 1.00 58.28 C ANISOU 2668 CB ILE B 266 6904 6845 8397 -277 -523 -24 C ATOM 2669 CG1 ILE B 266 14.436 -4.596 -30.282 1.00 58.67 C ANISOU 2669 CG1 ILE B 266 6917 6847 8527 -225 -471 -131 C ATOM 2670 CG2 ILE B 266 13.487 -2.769 -31.777 1.00 59.38 C ANISOU 2670 CG2 ILE B 266 7096 6992 8475 -317 -447 -20 C ATOM 2671 CD1 ILE B 266 14.960 -5.646 -31.279 1.00 64.60 C ANISOU 2671 CD1 ILE B 266 7754 7548 9243 -250 -420 -220 C ATOM 2672 N ILE B 267 10.245 -2.600 -30.453 1.00 55.40 N ANISOU 2672 N ILE B 267 6481 6568 8000 -308 -690 219 N ATOM 2673 CA ILE B 267 9.134 -1.735 -30.888 1.00 55.57 C ANISOU 2673 CA ILE B 267 6486 6620 8009 -322 -751 325 C ATOM 2674 C ILE B 267 8.644 -0.794 -29.765 1.00 58.81 C ANISOU 2674 C ILE B 267 6786 7047 8513 -249 -733 374 C ATOM 2675 O ILE B 267 8.423 0.392 -30.015 1.00 58.76 O ANISOU 2675 O ILE B 267 6770 7034 8522 -222 -724 425 O ATOM 2676 CB ILE B 267 7.971 -2.578 -31.513 1.00 59.37 C ANISOU 2676 CB ILE B 267 6991 7123 8446 -394 -871 384 C ATOM 2677 CG1 ILE B 267 8.445 -3.349 -32.771 1.00 60.42 C ANISOU 2677 CG1 ILE B 267 7272 7226 8457 -476 -882 327 C ATOM 2678 CG2 ILE B 267 6.735 -1.713 -31.840 1.00 60.67 C ANISOU 2678 CG2 ILE B 267 7099 7319 8634 -395 -961 505 C ATOM 2679 CD1 ILE B 267 7.660 -4.647 -33.083 1.00 68.34 C ANISOU 2679 CD1 ILE B 267 8316 8227 9421 -556 -988 335 C ATOM 2680 N CYS B 268 8.511 -1.323 -28.537 1.00 54.49 N ANISOU 2680 N CYS B 268 6175 6509 8019 -218 -721 356 N ATOM 2681 CA CYS B 268 8.010 -0.598 -27.372 1.00 53.81 C ANISOU 2681 CA CYS B 268 6005 6436 8005 -157 -684 387 C ATOM 2682 C CYS B 268 9.019 0.342 -26.710 1.00 58.12 C ANISOU 2682 C CYS B 268 6557 6951 8574 -104 -603 329 C ATOM 2683 O CYS B 268 8.604 1.396 -26.226 1.00 58.26 O ANISOU 2683 O CYS B 268 6537 6963 8637 -56 -566 358 O ATOM 2684 CB CYS B 268 7.425 -1.571 -26.355 1.00 53.74 C ANISOU 2684 CB CYS B 268 5955 6447 8017 -168 -697 396 C ATOM 2685 SG CYS B 268 5.924 -2.418 -26.915 1.00 58.27 S ANISOU 2685 SG CYS B 268 6479 7061 8601 -240 -791 484 S ATOM 2686 N TRP B 269 10.313 -0.034 -26.641 1.00 54.68 N ANISOU 2686 N TRP B 269 6162 6490 8122 -110 -576 244 N ATOM 2687 CA TRP B 269 11.306 0.782 -25.934 1.00 54.29 C ANISOU 2687 CA TRP B 269 6107 6415 8106 -75 -519 185 C ATOM 2688 C TRP B 269 12.300 1.565 -26.810 1.00 58.93 C ANISOU 2688 C TRP B 269 6724 6974 8692 -95 -469 147 C ATOM 2689 O TRP B 269 12.746 2.626 -26.370 1.00 58.91 O ANISOU 2689 O TRP B 269 6713 6946 8723 -76 -425 127 O ATOM 2690 CB TRP B 269 12.069 -0.061 -24.909 1.00 52.66 C ANISOU 2690 CB TRP B 269 5897 6199 7913 -63 -537 122 C ATOM 2691 CG TRP B 269 11.249 -0.432 -23.709 1.00 53.45 C ANISOU 2691 CG TRP B 269 5989 6315 8005 -48 -557 156 C ATOM 2692 CD1 TRP B 269 10.758 -1.666 -23.400 1.00 56.37 C ANISOU 2692 CD1 TRP B 269 6370 6693 8353 -70 -602 181 C ATOM 2693 CD2 TRP B 269 10.811 0.448 -22.663 1.00 53.34 C ANISOU 2693 CD2 TRP B 269 5966 6302 7998 -17 -514 168 C ATOM 2694 NE1 TRP B 269 10.056 -1.615 -22.218 1.00 55.94 N ANISOU 2694 NE1 TRP B 269 6315 6653 8287 -62 -584 212 N ATOM 2695 CE2 TRP B 269 10.071 -0.328 -21.745 1.00 57.34 C ANISOU 2695 CE2 TRP B 269 6481 6827 8478 -26 -524 199 C ATOM 2696 CE3 TRP B 269 10.979 1.822 -22.408 1.00 54.59 C ANISOU 2696 CE3 TRP B 269 6126 6438 8179 12 -459 150 C ATOM 2697 CZ2 TRP B 269 9.503 0.220 -20.589 1.00 56.92 C ANISOU 2697 CZ2 TRP B 269 6438 6778 8411 -6 -466 207 C ATOM 2698 CZ3 TRP B 269 10.412 2.364 -21.266 1.00 56.28 C ANISOU 2698 CZ3 TRP B 269 6351 6647 8386 40 -411 152 C ATOM 2699 CH2 TRP B 269 9.693 1.566 -20.366 1.00 57.13 C ANISOU 2699 CH2 TRP B 269 6467 6781 8458 31 -407 177 C ATOM 2700 N LEU B 270 12.651 1.070 -28.019 1.00 55.80 N ANISOU 2700 N LEU B 270 6373 6577 8252 -141 -463 132 N ATOM 2701 CA LEU B 270 13.585 1.763 -28.924 1.00 56.03 C ANISOU 2701 CA LEU B 270 6441 6581 8267 -177 -389 97 C ATOM 2702 C LEU B 270 13.185 3.237 -29.212 1.00 60.89 C ANISOU 2702 C LEU B 270 7084 7172 8878 -178 -368 164 C ATOM 2703 O LEU B 270 14.080 4.077 -29.114 1.00 61.15 O ANISOU 2703 O LEU B 270 7115 7173 8945 -189 -299 123 O ATOM 2704 CB LEU B 270 13.832 0.983 -30.233 1.00 56.45 C ANISOU 2704 CB LEU B 270 6569 6636 8246 -235 -370 74 C ATOM 2705 CG LEU B 270 14.972 1.467 -31.130 1.00 61.74 C ANISOU 2705 CG LEU B 270 7280 7280 8896 -284 -258 17 C ATOM 2706 CD1 LEU B 270 16.252 0.707 -30.850 1.00 62.09 C ANISOU 2706 CD1 LEU B 270 7262 7315 9014 -270 -194 -100 C ATOM 2707 CD2 LEU B 270 14.608 1.317 -32.588 1.00 64.99 C ANISOU 2707 CD2 LEU B 270 7821 7691 9181 -356 -247 51 C ATOM 2708 N PRO B 271 11.900 3.612 -29.502 1.00 57.45 N ANISOU 2708 N PRO B 271 6664 6743 8422 -163 -429 265 N ATOM 2709 CA PRO B 271 11.601 5.038 -29.749 1.00 57.65 C ANISOU 2709 CA PRO B 271 6718 6723 8463 -148 -414 329 C ATOM 2710 C PRO B 271 11.949 5.959 -28.582 1.00 60.98 C ANISOU 2710 C PRO B 271 7098 7106 8965 -99 -361 291 C ATOM 2711 O PRO B 271 12.507 7.031 -28.815 1.00 61.29 O ANISOU 2711 O PRO B 271 7182 7089 9017 -117 -308 288 O ATOM 2712 CB PRO B 271 10.098 5.045 -30.057 1.00 59.77 C ANISOU 2712 CB PRO B 271 6970 7008 8730 -120 -511 440 C ATOM 2713 CG PRO B 271 9.792 3.664 -30.500 1.00 64.04 C ANISOU 2713 CG PRO B 271 7517 7602 9214 -165 -573 435 C ATOM 2714 CD PRO B 271 10.682 2.792 -29.669 1.00 58.90 C ANISOU 2714 CD PRO B 271 6831 6965 8582 -163 -521 329 C ATOM 2715 N PHE B 272 11.665 5.523 -27.334 1.00 56.52 N ANISOU 2715 N PHE B 272 6467 6566 8442 -51 -373 260 N ATOM 2716 CA PHE B 272 11.947 6.291 -26.118 1.00 55.97 C ANISOU 2716 CA PHE B 272 6380 6460 8424 -12 -330 212 C ATOM 2717 C PHE B 272 13.443 6.525 -25.895 1.00 59.33 C ANISOU 2717 C PHE B 272 6817 6861 8864 -57 -289 119 C ATOM 2718 O PHE B 272 13.849 7.667 -25.690 1.00 59.23 O ANISOU 2718 O PHE B 272 6833 6789 8883 -64 -246 101 O ATOM 2719 CB PHE B 272 11.295 5.644 -24.873 1.00 57.38 C ANISOU 2719 CB PHE B 272 6513 6676 8614 31 -347 201 C ATOM 2720 CG PHE B 272 11.655 6.328 -23.572 1.00 58.93 C ANISOU 2720 CG PHE B 272 6724 6834 8830 56 -305 139 C ATOM 2721 CD1 PHE B 272 10.987 7.478 -23.164 1.00 62.53 C ANISOU 2721 CD1 PHE B 272 7197 7238 9324 108 -254 158 C ATOM 2722 CD2 PHE B 272 12.687 5.846 -22.774 1.00 60.44 C ANISOU 2722 CD2 PHE B 272 6925 7034 9007 29 -323 58 C ATOM 2723 CE1 PHE B 272 11.345 8.131 -21.981 1.00 63.52 C ANISOU 2723 CE1 PHE B 272 7365 7318 9451 120 -209 87 C ATOM 2724 CE2 PHE B 272 13.048 6.504 -21.597 1.00 63.39 C ANISOU 2724 CE2 PHE B 272 7335 7369 9380 36 -303 -2 C ATOM 2725 CZ PHE B 272 12.373 7.641 -21.208 1.00 62.05 C ANISOU 2725 CZ PHE B 272 7201 7147 9228 76 -240 8 C ATOM 2726 N HIS B 273 14.247 5.447 -25.912 1.00 55.58 N ANISOU 2726 N HIS B 273 6312 6424 8382 -86 -305 61 N ATOM 2727 CA HIS B 273 15.692 5.503 -25.677 1.00 55.41 C ANISOU 2727 CA HIS B 273 6261 6388 8404 -123 -279 -30 C ATOM 2728 C HIS B 273 16.456 6.273 -26.761 1.00 59.73 C ANISOU 2728 C HIS B 273 6833 6901 8961 -187 -202 -39 C ATOM 2729 O HIS B 273 17.474 6.889 -26.444 1.00 60.21 O ANISOU 2729 O HIS B 273 6866 6933 9080 -225 -167 -100 O ATOM 2730 CB HIS B 273 16.264 4.103 -25.444 1.00 55.75 C ANISOU 2730 CB HIS B 273 6254 6469 8460 -117 -323 -82 C ATOM 2731 CG HIS B 273 15.800 3.523 -24.146 1.00 58.75 C ANISOU 2731 CG HIS B 273 6627 6864 8831 -72 -395 -80 C ATOM 2732 ND1 HIS B 273 16.474 3.770 -22.965 1.00 60.67 N ANISOU 2732 ND1 HIS B 273 6857 7091 9104 -67 -432 -135 N ATOM 2733 CD2 HIS B 273 14.697 2.789 -23.872 1.00 60.23 C ANISOU 2733 CD2 HIS B 273 6832 7079 8972 -44 -433 -26 C ATOM 2734 CE1 HIS B 273 15.782 3.156 -22.020 1.00 59.91 C ANISOU 2734 CE1 HIS B 273 6788 7011 8964 -36 -484 -110 C ATOM 2735 NE2 HIS B 273 14.705 2.550 -22.518 1.00 59.98 N ANISOU 2735 NE2 HIS B 273 6809 7047 8934 -23 -477 -45 N ATOM 2736 N VAL B 274 15.943 6.286 -28.012 1.00 55.79 N ANISOU 2736 N VAL B 274 6395 6404 8398 -212 -178 26 N ATOM 2737 CA VAL B 274 16.523 7.052 -29.120 1.00 56.17 C ANISOU 2737 CA VAL B 274 6504 6415 8424 -286 -95 36 C ATOM 2738 C VAL B 274 16.297 8.548 -28.819 1.00 59.97 C ANISOU 2738 C VAL B 274 7030 6822 8933 -285 -80 78 C ATOM 2739 O VAL B 274 17.249 9.327 -28.872 1.00 59.83 O ANISOU 2739 O VAL B 274 7018 6758 8956 -347 -11 37 O ATOM 2740 CB VAL B 274 15.966 6.601 -30.505 1.00 60.44 C ANISOU 2740 CB VAL B 274 7133 6974 8859 -321 -94 100 C ATOM 2741 CG1 VAL B 274 16.175 7.662 -31.588 1.00 61.21 C ANISOU 2741 CG1 VAL B 274 7341 7016 8902 -395 -25 153 C ATOM 2742 CG2 VAL B 274 16.586 5.276 -30.936 1.00 60.26 C ANISOU 2742 CG2 VAL B 274 7084 6996 8816 -344 -65 26 C ATOM 2743 N LEU B 275 15.056 8.919 -28.436 1.00 56.48 N ANISOU 2743 N LEU B 275 6611 6362 8487 -213 -140 152 N ATOM 2744 CA LEU B 275 14.681 10.291 -28.079 1.00 56.92 C ANISOU 2744 CA LEU B 275 6715 6331 8582 -185 -126 189 C ATOM 2745 C LEU B 275 15.375 10.775 -26.803 1.00 61.12 C ANISOU 2745 C LEU B 275 7213 6829 9179 -185 -104 96 C ATOM 2746 O LEU B 275 15.677 11.964 -26.700 1.00 61.43 O ANISOU 2746 O LEU B 275 7308 6780 9254 -210 -63 91 O ATOM 2747 CB LEU B 275 13.154 10.456 -27.973 1.00 56.98 C ANISOU 2747 CB LEU B 275 6726 6331 8594 -92 -188 283 C ATOM 2748 CG LEU B 275 12.371 10.413 -29.291 1.00 62.28 C ANISOU 2748 CG LEU B 275 7452 7004 9207 -99 -240 398 C ATOM 2749 CD1 LEU B 275 10.910 10.157 -29.040 1.00 62.49 C ANISOU 2749 CD1 LEU B 275 7421 7057 9267 -7 -320 473 C ATOM 2750 CD2 LEU B 275 12.538 11.701 -30.093 1.00 65.97 C ANISOU 2750 CD2 LEU B 275 8032 7367 9665 -133 -214 465 C ATOM 2751 N THR B 276 15.645 9.852 -25.848 1.00 57.15 N ANISOU 2751 N THR B 276 6638 6390 8688 -164 -140 26 N ATOM 2752 CA THR B 276 16.353 10.137 -24.592 1.00 56.99 C ANISOU 2752 CA THR B 276 6596 6347 8709 -175 -150 -65 C ATOM 2753 C THR B 276 17.822 10.450 -24.910 1.00 61.17 C ANISOU 2753 C THR B 276 7095 6858 9289 -272 -114 -132 C ATOM 2754 O THR B 276 18.391 11.378 -24.325 1.00 61.22 O ANISOU 2754 O THR B 276 7123 6801 9338 -315 -103 -182 O ATOM 2755 CB THR B 276 16.164 8.981 -23.589 1.00 64.09 C ANISOU 2755 CB THR B 276 7447 7317 9589 -130 -217 -99 C ATOM 2756 OG1 THR B 276 14.767 8.794 -23.364 1.00 63.81 O ANISOU 2756 OG1 THR B 276 7430 7296 9519 -56 -224 -33 O ATOM 2757 CG2 THR B 276 16.857 9.231 -22.251 1.00 62.54 C ANISOU 2757 CG2 THR B 276 7255 7099 9410 -148 -253 -185 C ATOM 2758 N PHE B 277 18.414 9.696 -25.864 1.00 57.68 N ANISOU 2758 N PHE B 277 6604 6465 8846 -314 -86 -137 N ATOM 2759 CA PHE B 277 19.788 9.891 -26.329 1.00 58.25 C ANISOU 2759 CA PHE B 277 6620 6530 8982 -408 -22 -200 C ATOM 2760 C PHE B 277 19.909 11.208 -27.105 1.00 63.30 C ANISOU 2760 C PHE B 277 7347 7087 9616 -484 65 -159 C ATOM 2761 O PHE B 277 20.888 11.929 -26.912 1.00 63.83 O ANISOU 2761 O PHE B 277 7387 7110 9756 -568 105 -214 O ATOM 2762 CB PHE B 277 20.270 8.695 -27.173 1.00 59.87 C ANISOU 2762 CB PHE B 277 6760 6803 9184 -419 12 -223 C ATOM 2763 CG PHE B 277 21.719 8.772 -27.600 1.00 62.35 C ANISOU 2763 CG PHE B 277 6982 7119 9590 -508 99 -300 C ATOM 2764 CD1 PHE B 277 22.743 8.502 -26.699 1.00 65.74 C ANISOU 2764 CD1 PHE B 277 7276 7564 10139 -514 47 -390 C ATOM 2765 CD2 PHE B 277 22.059 9.105 -28.906 1.00 65.20 C ANISOU 2765 CD2 PHE B 277 7389 7465 9921 -590 233 -282 C ATOM 2766 CE1 PHE B 277 24.082 8.585 -27.091 1.00 67.92 C ANISOU 2766 CE1 PHE B 277 7430 7844 10532 -595 131 -463 C ATOM 2767 CE2 PHE B 277 23.398 9.181 -29.299 1.00 69.31 C ANISOU 2767 CE2 PHE B 277 7808 7989 10539 -679 342 -359 C ATOM 2768 CZ PHE B 277 24.400 8.918 -28.390 1.00 67.84 C ANISOU 2768 CZ PHE B 277 7453 7823 10500 -678 292 -451 C ATOM 2769 N LEU B 278 18.905 11.531 -27.956 1.00 60.07 N ANISOU 2769 N LEU B 278 7047 6650 9127 -460 82 -56 N ATOM 2770 CA LEU B 278 18.863 12.778 -28.730 1.00 61.07 C ANISOU 2770 CA LEU B 278 7288 6681 9234 -523 147 9 C ATOM 2771 C LEU B 278 18.707 13.989 -27.805 1.00 66.27 C ANISOU 2771 C LEU B 278 7994 7238 9948 -508 128 -1 C ATOM 2772 O LEU B 278 19.272 15.047 -28.086 1.00 66.98 O ANISOU 2772 O LEU B 278 8147 7236 10067 -595 190 1 O ATOM 2773 CB LEU B 278 17.739 12.759 -29.784 1.00 61.11 C ANISOU 2773 CB LEU B 278 7400 6678 9140 -486 127 133 C ATOM 2774 CG LEU B 278 17.904 11.814 -30.985 1.00 65.77 C ANISOU 2774 CG LEU B 278 8009 7339 9643 -534 163 150 C ATOM 2775 CD1 LEU B 278 16.608 11.695 -31.757 1.00 65.92 C ANISOU 2775 CD1 LEU B 278 8124 7357 9563 -485 86 273 C ATOM 2776 CD2 LEU B 278 19.025 12.260 -31.918 1.00 69.20 C ANISOU 2776 CD2 LEU B 278 8491 7742 10059 -671 297 130 C ATOM 2777 N ASP B 279 17.960 13.818 -26.692 1.00 62.76 N ANISOU 2777 N ASP B 279 7529 6803 9513 -406 55 -18 N ATOM 2778 CA ASP B 279 17.741 14.846 -25.670 1.00 63.19 C ANISOU 2778 CA ASP B 279 7640 6761 9609 -379 45 -50 C ATOM 2779 C ASP B 279 19.021 15.071 -24.853 1.00 67.80 C ANISOU 2779 C ASP B 279 8176 7332 10251 -471 42 -167 C ATOM 2780 O ASP B 279 19.272 16.196 -24.425 1.00 68.20 O ANISOU 2780 O ASP B 279 8300 7274 10339 -516 61 -198 O ATOM 2781 CB ASP B 279 16.571 14.456 -24.749 1.00 64.27 C ANISOU 2781 CB ASP B 279 7768 6925 9726 -251 -7 -42 C ATOM 2782 CG ASP B 279 16.112 15.560 -23.820 1.00 73.82 C ANISOU 2782 CG ASP B 279 9062 8022 10965 -205 10 -69 C ATOM 2783 OD1 ASP B 279 15.449 16.505 -24.302 1.00 75.04 O ANISOU 2783 OD1 ASP B 279 9297 8073 11142 -164 42 2 O ATOM 2784 OD2 ASP B 279 16.385 15.464 -22.606 1.00 79.29 O ANISOU 2784 OD2 ASP B 279 9751 8722 11655 -206 -11 -162 O ATOM 2785 N ALA B 280 19.825 14.002 -24.646 1.00 64.50 N ANISOU 2785 N ALA B 280 7635 7018 9853 -500 8 -230 N ATOM 2786 CA ALA B 280 21.099 14.045 -23.915 1.00 65.22 C ANISOU 2786 CA ALA B 280 7646 7115 10020 -586 -27 -336 C ATOM 2787 C ALA B 280 22.127 14.876 -24.676 1.00 70.75 C ANISOU 2787 C ALA B 280 8336 7757 10789 -723 59 -350 C ATOM 2788 O ALA B 280 22.917 15.593 -24.057 1.00 71.48 O ANISOU 2788 O ALA B 280 8418 7793 10949 -812 40 -420 O ATOM 2789 CB ALA B 280 21.630 12.636 -23.702 1.00 65.39 C ANISOU 2789 CB ALA B 280 7529 7253 10063 -563 -88 -379 C ATOM 2790 N LEU B 281 22.103 14.785 -26.020 1.00 67.57 N ANISOU 2790 N LEU B 281 7948 7366 10359 -754 155 -284 N ATOM 2791 CA LEU B 281 22.992 15.528 -26.913 1.00 68.72 C ANISOU 2791 CA LEU B 281 8104 7458 10549 -895 269 -281 C ATOM 2792 C LEU B 281 22.602 17.001 -26.970 1.00 73.71 C ANISOU 2792 C LEU B 281 8899 7940 11167 -936 299 -229 C ATOM 2793 O LEU B 281 23.467 17.848 -27.188 1.00 74.69 O ANISOU 2793 O LEU B 281 9036 7991 11353 -1073 366 -254 O ATOM 2794 CB LEU B 281 22.995 14.913 -28.321 1.00 68.70 C ANISOU 2794 CB LEU B 281 8104 7511 10486 -916 369 -224 C ATOM 2795 CG LEU B 281 23.538 13.488 -28.442 1.00 72.69 C ANISOU 2795 CG LEU B 281 8454 8143 11022 -888 371 -287 C ATOM 2796 CD1 LEU B 281 23.137 12.868 -29.759 1.00 72.63 C ANISOU 2796 CD1 LEU B 281 8511 8177 10909 -881 453 -224 C ATOM 2797 CD2 LEU B 281 25.046 13.452 -28.264 1.00 76.25 C ANISOU 2797 CD2 LEU B 281 8735 8617 11618 -994 422 -391 C ATOM 2798 N ALA B 282 21.303 17.302 -26.758 1.00 70.03 N ANISOU 2798 N ALA B 282 8551 7421 10635 -815 251 -159 N ATOM 2799 CA ALA B 282 20.761 18.661 -26.727 1.00 70.81 C ANISOU 2799 CA ALA B 282 8811 7360 10733 -813 268 -107 C ATOM 2800 C ALA B 282 21.229 19.396 -25.466 1.00 75.85 C ANISOU 2800 C ALA B 282 9463 7918 11439 -854 231 -212 C ATOM 2801 O ALA B 282 21.423 20.613 -25.509 1.00 76.91 O ANISOU 2801 O ALA B 282 9712 7904 11606 -928 270 -207 O ATOM 2802 CB ALA B 282 19.243 18.625 -26.787 1.00 70.81 C ANISOU 2802 CB ALA B 282 8889 7340 10674 -653 223 -14 C ATOM 2803 N TRP B 283 21.427 18.652 -24.354 1.00 71.90 N ANISOU 2803 N TRP B 283 8864 7505 10949 -815 148 -305 N ATOM 2804 CA TRP B 283 21.915 19.192 -23.083 1.00 72.60 C ANISOU 2804 CA TRP B 283 8974 7535 11076 -864 88 -415 C ATOM 2805 C TRP B 283 23.411 19.505 -23.167 1.00 78.42 C ANISOU 2805 C TRP B 283 9624 8263 11909 -1046 97 -486 C ATOM 2806 O TRP B 283 23.835 20.555 -22.680 1.00 79.37 O ANISOU 2806 O TRP B 283 9825 8263 12071 -1143 90 -540 O ATOM 2807 CB TRP B 283 21.626 18.230 -21.917 1.00 70.27 C ANISOU 2807 CB TRP B 283 8623 7339 10739 -773 -14 -476 C ATOM 2808 CG TRP B 283 20.230 18.325 -21.371 1.00 70.55 C ANISOU 2808 CG TRP B 283 8767 7340 10701 -625 -12 -445 C ATOM 2809 CD1 TRP B 283 19.238 17.398 -21.495 1.00 72.17 C ANISOU 2809 CD1 TRP B 283 8933 7636 10851 -496 -19 -383 C ATOM 2810 CD2 TRP B 283 19.680 19.401 -20.597 1.00 71.23 C ANISOU 2810 CD2 TRP B 283 9007 7285 10774 -594 9 -483 C ATOM 2811 NE1 TRP B 283 18.100 17.833 -20.858 1.00 71.68 N ANISOU 2811 NE1 TRP B 283 8973 7508 10754 -387 4 -376 N ATOM 2812 CE2 TRP B 283 18.343 19.060 -20.297 1.00 74.37 C ANISOU 2812 CE2 TRP B 283 9435 7703 11117 -436 28 -441 C ATOM 2813 CE3 TRP B 283 20.188 20.625 -20.129 1.00 73.93 C ANISOU 2813 CE3 TRP B 283 9464 7476 11149 -688 20 -555 C ATOM 2814 CZ2 TRP B 283 17.506 19.898 -19.550 1.00 74.43 C ANISOU 2814 CZ2 TRP B 283 9579 7590 11113 -357 75 -472 C ATOM 2815 CZ3 TRP B 283 19.358 21.454 -19.390 1.00 76.09 C ANISOU 2815 CZ3 TRP B 283 9896 7620 11396 -612 56 -589 C ATOM 2816 CH2 TRP B 283 18.034 21.091 -19.110 1.00 76.02 C ANISOU 2816 CH2 TRP B 283 9906 7637 11340 -441 92 -550 C ATOM 2817 N MET B 284 24.203 18.599 -23.793 1.00 75.27 N ANISOU 2817 N MET B 284 9057 7987 11555 -1094 117 -490 N ATOM 2818 CA MET B 284 25.654 18.739 -23.990 1.00 76.70 C ANISOU 2818 CA MET B 284 9103 8184 11857 -1262 143 -556 C ATOM 2819 C MET B 284 25.996 19.920 -24.909 1.00 81.18 C ANISOU 2819 C MET B 284 9763 8629 12454 -1402 274 -511 C ATOM 2820 O MET B 284 27.003 20.595 -24.688 1.00 82.33 O ANISOU 2820 O MET B 284 9862 8718 12701 -1560 282 -574 O ATOM 2821 CB MET B 284 26.261 17.444 -24.561 1.00 78.88 C ANISOU 2821 CB MET B 284 9179 8611 12179 -1249 167 -566 C ATOM 2822 CG MET B 284 26.509 16.367 -23.526 1.00 82.40 C ANISOU 2822 CG MET B 284 9492 9161 12656 -1173 18 -637 C ATOM 2823 SD MET B 284 27.182 14.857 -24.275 1.00 86.74 S ANISOU 2823 SD MET B 284 9820 9859 13279 -1138 59 -649 S ATOM 2824 CE MET B 284 27.363 13.830 -22.833 1.00 83.01 C ANISOU 2824 CE MET B 284 9243 9462 12836 -1046 -158 -715 C ATOM 2825 N GLY B 285 25.158 20.143 -25.922 1.00 76.69 N ANISOU 2825 N GLY B 285 9326 8017 11797 -1350 364 -396 N ATOM 2826 CA GLY B 285 25.321 21.210 -26.903 1.00 77.71 C ANISOU 2826 CA GLY B 285 9584 8021 11922 -1470 487 -323 C ATOM 2827 C GLY B 285 25.589 20.717 -28.311 1.00 81.56 C ANISOU 2827 C GLY B 285 10041 8577 12370 -1524 618 -254 C ATOM 2828 O GLY B 285 25.995 21.502 -29.172 1.00 82.55 O ANISOU 2828 O GLY B 285 10256 8615 12494 -1663 738 -202 O ATOM 2829 N VAL B 286 25.364 19.410 -28.556 1.00 76.74 N ANISOU 2829 N VAL B 286 9323 8118 11718 -1422 603 -256 N ATOM 2830 CA VAL B 286 25.566 18.762 -29.857 1.00 76.68 C ANISOU 2830 CA VAL B 286 9297 8187 11652 -1459 728 -208 C ATOM 2831 C VAL B 286 24.398 19.109 -30.799 1.00 80.69 C ANISOU 2831 C VAL B 286 10027 8628 12005 -1401 745 -62 C ATOM 2832 O VAL B 286 24.640 19.535 -31.931 1.00 81.60 O ANISOU 2832 O VAL B 286 10251 8695 12058 -1514 870 8 O ATOM 2833 CB VAL B 286 25.822 17.234 -29.728 1.00 79.36 C ANISOU 2833 CB VAL B 286 9446 8693 12014 -1375 701 -277 C ATOM 2834 CG1 VAL B 286 26.123 16.601 -31.085 1.00 79.65 C ANISOU 2834 CG1 VAL B 286 9479 8796 11990 -1427 855 -250 C ATOM 2835 CG2 VAL B 286 26.958 16.947 -28.746 1.00 79.55 C ANISOU 2835 CG2 VAL B 286 9249 8770 12207 -1422 648 -408 C ATOM 2836 N ILE B 287 23.145 18.943 -30.325 1.00 76.13 N ANISOU 2836 N ILE B 287 9514 8043 11369 -1231 618 -13 N ATOM 2837 CA ILE B 287 21.939 19.285 -31.085 1.00 76.08 C ANISOU 2837 CA ILE B 287 9692 7969 11245 -1155 592 131 C ATOM 2838 C ILE B 287 21.424 20.622 -30.545 1.00 81.61 C ANISOU 2838 C ILE B 287 10529 8496 11984 -1128 545 171 C ATOM 2839 O ILE B 287 20.991 20.699 -29.393 1.00 80.51 O ANISOU 2839 O ILE B 287 10351 8341 11899 -1025 459 114 O ATOM 2840 CB ILE B 287 20.859 18.157 -31.075 1.00 77.39 C ANISOU 2840 CB ILE B 287 9820 8247 11338 -990 494 165 C ATOM 2841 CG1 ILE B 287 21.401 16.863 -31.726 1.00 77.28 C ANISOU 2841 CG1 ILE B 287 9703 8380 11281 -1025 552 123 C ATOM 2842 CG2 ILE B 287 19.562 18.620 -31.771 1.00 78.09 C ANISOU 2842 CG2 ILE B 287 10079 8257 11334 -908 434 318 C ATOM 2843 CD1 ILE B 287 20.731 15.575 -31.263 1.00 82.02 C ANISOU 2843 CD1 ILE B 287 10202 9101 11862 -885 452 97 C ATOM 2844 N ASN B 288 21.513 21.676 -31.371 1.00 80.45 N ANISOU 2844 N ASN B 288 10553 8209 11805 -1228 613 264 N ATOM 2845 CA ASN B 288 21.095 23.030 -31.005 1.00 81.65 C ANISOU 2845 CA ASN B 288 10859 8162 12001 -1213 583 309 C ATOM 2846 C ASN B 288 19.907 23.527 -31.836 1.00 86.88 C ANISOU 2846 C ASN B 288 11709 8719 12583 -1118 531 480 C ATOM 2847 O ASN B 288 19.307 24.550 -31.493 1.00 87.16 O ANISOU 2847 O ASN B 288 11866 8584 12667 -1050 486 526 O ATOM 2848 CB ASN B 288 22.280 23.996 -31.106 1.00 83.98 C ANISOU 2848 CB ASN B 288 11204 8345 12359 -1421 689 271 C ATOM 2849 CG ASN B 288 23.452 23.638 -30.222 1.00104.72 C ANISOU 2849 CG ASN B 288 13634 11059 15095 -1517 711 105 C ATOM 2850 OD1 ASN B 288 23.337 23.534 -28.994 1.00 97.87 O ANISOU 2850 OD1 ASN B 288 12689 10205 14291 -1438 619 8 O ATOM 2851 ND2 ASN B 288 24.615 23.464 -30.828 1.00 97.42 N ANISOU 2851 ND2 ASN B 288 12627 10191 14197 -1695 833 72 N ATOM 2852 N SER B 289 19.562 22.794 -32.915 1.00 83.90 N ANISOU 2852 N SER B 289 11357 8436 12085 -1111 528 572 N ATOM 2853 CA SER B 289 18.457 23.114 -33.817 1.00 84.85 C ANISOU 2853 CA SER B 289 11646 8478 12116 -1031 447 746 C ATOM 2854 C SER B 289 17.112 22.950 -33.112 1.00 88.69 C ANISOU 2854 C SER B 289 12074 8965 12658 -805 305 771 C ATOM 2855 O SER B 289 16.780 21.849 -32.665 1.00 86.61 O ANISOU 2855 O SER B 289 11652 8860 12395 -716 260 708 O ATOM 2856 CB SER B 289 18.519 22.242 -35.069 1.00 88.61 C ANISOU 2856 CB SER B 289 12161 9074 12435 -1099 474 813 C ATOM 2857 OG SER B 289 17.447 22.518 -35.957 1.00 98.67 O ANISOU 2857 OG SER B 289 13604 10277 13611 -1031 364 988 O ATOM 2858 N CYS B 290 16.345 24.055 -33.012 1.00 87.29 N ANISOU 2858 N CYS B 290 12024 8602 12540 -714 244 861 N ATOM 2859 CA CYS B 290 15.023 24.088 -32.379 1.00 87.07 C ANISOU 2859 CA CYS B 290 11941 8546 12594 -494 131 891 C ATOM 2860 C CYS B 290 13.993 23.233 -33.109 1.00 88.64 C ANISOU 2860 C CYS B 290 12101 8857 12721 -394 14 1004 C ATOM 2861 O CYS B 290 13.047 22.763 -32.480 1.00 86.99 O ANISOU 2861 O CYS B 290 11761 8711 12579 -233 -59 987 O ATOM 2862 CB CYS B 290 14.532 25.521 -32.192 1.00 89.95 C ANISOU 2862 CB CYS B 290 12455 8666 13057 -420 108 959 C ATOM 2863 SG CYS B 290 15.362 26.431 -30.861 1.00 94.81 S ANISOU 2863 SG CYS B 290 13084 9149 13790 -476 212 787 S ATOM 2864 N GLU B 291 14.188 23.026 -34.428 1.00 84.94 N ANISOU 2864 N GLU B 291 11751 8413 12109 -504 1 1113 N ATOM 2865 CA GLU B 291 13.331 22.203 -35.285 1.00 84.03 C ANISOU 2865 CA GLU B 291 11632 8401 11894 -452 -121 1223 C ATOM 2866 C GLU B 291 13.389 20.741 -34.831 1.00 84.76 C ANISOU 2866 C GLU B 291 11525 8712 11967 -432 -112 1103 C ATOM 2867 O GLU B 291 12.355 20.078 -34.787 1.00 83.90 O ANISOU 2867 O GLU B 291 11324 8684 11872 -311 -230 1144 O ATOM 2868 CB GLU B 291 13.751 22.318 -36.762 1.00 86.79 C ANISOU 2868 CB GLU B 291 12191 8723 12060 -613 -109 1342 C ATOM 2869 CG GLU B 291 13.470 23.670 -37.394 1.00 99.29 C ANISOU 2869 CG GLU B 291 14004 10084 13637 -624 -163 1506 C ATOM 2870 CD GLU B 291 14.596 24.672 -37.245 1.00119.83 C ANISOU 2870 CD GLU B 291 16719 12546 16265 -771 -5 1460 C ATOM 2871 OE1 GLU B 291 15.475 24.713 -38.135 1.00116.91 O ANISOU 2871 OE1 GLU B 291 16490 12178 15754 -968 102 1485 O ATOM 2872 OE2 GLU B 291 14.606 25.412 -36.234 1.00112.02 O ANISOU 2872 OE2 GLU B 291 15681 11444 15437 -698 20 1392 O ATOM 2873 N VAL B 292 14.595 20.259 -34.469 1.00 79.29 N ANISOU 2873 N VAL B 292 10758 8106 11261 -549 23 958 N ATOM 2874 CA VAL B 292 14.841 18.893 -33.993 1.00 76.78 C ANISOU 2874 CA VAL B 292 10262 7974 10935 -539 42 836 C ATOM 2875 C VAL B 292 14.312 18.742 -32.556 1.00 78.43 C ANISOU 2875 C VAL B 292 10313 8207 11278 -393 3 750 C ATOM 2876 O VAL B 292 13.598 17.779 -32.271 1.00 76.78 O ANISOU 2876 O VAL B 292 9990 8113 11071 -302 -67 741 O ATOM 2877 CB VAL B 292 16.343 18.489 -34.115 1.00 80.36 C ANISOU 2877 CB VAL B 292 10682 8497 11355 -703 193 717 C ATOM 2878 CG1 VAL B 292 16.558 17.018 -33.765 1.00 78.41 C ANISOU 2878 CG1 VAL B 292 10266 8426 11098 -681 196 609 C ATOM 2879 CG2 VAL B 292 16.889 18.787 -35.511 1.00 81.78 C ANISOU 2879 CG2 VAL B 292 11039 8635 11397 -860 271 797 C ATOM 2880 N ILE B 293 14.652 19.707 -31.670 1.00 74.73 N ANISOU 2880 N ILE B 293 9857 7624 10913 -384 55 688 N ATOM 2881 CA ILE B 293 14.268 19.748 -30.251 1.00 73.50 C ANISOU 2881 CA ILE B 293 9596 7466 10865 -268 46 594 C ATOM 2882 C ILE B 293 12.729 19.793 -30.071 1.00 77.17 C ANISOU 2882 C ILE B 293 10027 7908 11385 -85 -49 679 C ATOM 2883 O ILE B 293 12.209 19.096 -29.194 1.00 75.58 O ANISOU 2883 O ILE B 293 9696 7799 11222 6 -65 616 O ATOM 2884 CB ILE B 293 15.021 20.894 -29.505 1.00 77.33 C ANISOU 2884 CB ILE B 293 10148 7808 11427 -325 121 511 C ATOM 2885 CG1 ILE B 293 16.548 20.634 -29.502 1.00 77.45 C ANISOU 2885 CG1 ILE B 293 10128 7882 11418 -503 205 407 C ATOM 2886 CG2 ILE B 293 14.509 21.084 -28.070 1.00 77.74 C ANISOU 2886 CG2 ILE B 293 10141 7831 11567 -203 116 418 C ATOM 2887 CD1 ILE B 293 17.435 21.874 -29.323 1.00 86.42 C ANISOU 2887 CD1 ILE B 293 11368 8861 12609 -624 277 367 C ATOM 2888 N ALA B 294 12.010 20.568 -30.918 1.00 74.93 N ANISOU 2888 N ALA B 294 9854 7505 11110 -37 -114 828 N ATOM 2889 CA ALA B 294 10.543 20.662 -30.874 1.00 75.07 C ANISOU 2889 CA ALA B 294 9817 7496 11211 140 -217 924 C ATOM 2890 C ALA B 294 9.885 19.311 -31.182 1.00 77.54 C ANISOU 2890 C ALA B 294 10000 7990 11471 170 -302 954 C ATOM 2891 O ALA B 294 8.879 18.974 -30.556 1.00 76.99 O ANISOU 2891 O ALA B 294 9796 7965 11492 303 -341 951 O ATOM 2892 CB ALA B 294 10.045 21.722 -31.843 1.00 77.75 C ANISOU 2892 CB ALA B 294 10308 7667 11567 172 -295 1090 C ATOM 2893 N VAL B 295 10.474 18.533 -32.123 1.00 73.10 N ANISOU 2893 N VAL B 295 9480 7529 10766 39 -317 973 N ATOM 2894 CA VAL B 295 10.008 17.198 -32.519 1.00 71.76 C ANISOU 2894 CA VAL B 295 9219 7522 10524 35 -394 991 C ATOM 2895 C VAL B 295 10.203 16.218 -31.349 1.00 73.63 C ANISOU 2895 C VAL B 295 9295 7885 10798 59 -334 846 C ATOM 2896 O VAL B 295 9.270 15.489 -31.021 1.00 72.83 O ANISOU 2896 O VAL B 295 9071 7866 10734 142 -399 859 O ATOM 2897 CB VAL B 295 10.655 16.709 -33.852 1.00 75.79 C ANISOU 2897 CB VAL B 295 9855 8082 10860 -117 -402 1035 C ATOM 2898 CG1 VAL B 295 10.337 15.241 -34.136 1.00 74.60 C ANISOU 2898 CG1 VAL B 295 9619 8095 10632 -135 -463 1016 C ATOM 2899 CG2 VAL B 295 10.213 17.576 -35.026 1.00 77.48 C ANISOU 2899 CG2 VAL B 295 10246 8178 11016 -133 -497 1206 C ATOM 2900 N ILE B 296 11.388 16.249 -30.693 1.00 69.30 N ANISOU 2900 N ILE B 296 8745 7340 10244 -17 -220 715 N ATOM 2901 CA ILE B 296 11.733 15.407 -29.535 1.00 67.78 C ANISOU 2901 CA ILE B 296 8428 7247 10076 -6 -175 581 C ATOM 2902 C ILE B 296 10.726 15.605 -28.384 1.00 72.08 C ANISOU 2902 C ILE B 296 8890 7774 10726 135 -183 563 C ATOM 2903 O ILE B 296 10.293 14.623 -27.778 1.00 70.72 O ANISOU 2903 O ILE B 296 8608 7708 10555 175 -199 525 O ATOM 2904 CB ILE B 296 13.220 15.618 -29.092 1.00 70.52 C ANISOU 2904 CB ILE B 296 8796 7579 10418 -116 -78 459 C ATOM 2905 CG1 ILE B 296 14.201 15.183 -30.207 1.00 71.14 C ANISOU 2905 CG1 ILE B 296 8921 7704 10405 -253 -40 461 C ATOM 2906 CG2 ILE B 296 13.546 14.889 -27.774 1.00 69.77 C ANISOU 2906 CG2 ILE B 296 8591 7565 10353 -94 -60 332 C ATOM 2907 CD1 ILE B 296 15.569 15.904 -30.201 1.00 79.75 C ANISOU 2907 CD1 ILE B 296 10058 8728 11514 -377 62 391 C ATOM 2908 N ASP B 297 10.329 16.868 -28.126 1.00 70.25 N ANISOU 2908 N ASP B 297 8716 7396 10578 207 -161 592 N ATOM 2909 CA ASP B 297 9.384 17.250 -27.076 1.00 70.68 C ANISOU 2909 CA ASP B 297 8708 7406 10742 347 -134 567 C ATOM 2910 C ASP B 297 7.960 16.729 -27.290 1.00 74.60 C ANISOU 2910 C ASP B 297 9084 7963 11296 461 -210 661 C ATOM 2911 O ASP B 297 7.384 16.179 -26.349 1.00 73.81 O ANISOU 2911 O ASP B 297 8874 7932 11238 525 -173 606 O ATOM 2912 CB ASP B 297 9.383 18.775 -26.872 1.00 74.27 C ANISOU 2912 CB ASP B 297 9274 7665 11281 395 -85 571 C ATOM 2913 CG ASP B 297 10.422 19.285 -25.890 1.00 86.82 C ANISOU 2913 CG ASP B 297 10934 9193 12861 326 12 427 C ATOM 2914 OD1 ASP B 297 11.539 18.714 -25.849 1.00 86.48 O ANISOU 2914 OD1 ASP B 297 10890 9233 12737 196 23 355 O ATOM 2915 OD2 ASP B 297 10.131 20.273 -25.182 1.00 95.15 O ANISOU 2915 OD2 ASP B 297 12047 10110 13996 401 71 385 O ATOM 2916 N LEU B 298 7.387 16.903 -28.502 1.00 71.88 N ANISOU 2916 N LEU B 298 8762 7593 10955 477 -319 805 N ATOM 2917 CA LEU B 298 6.020 16.451 -28.790 1.00 72.27 C ANISOU 2917 CA LEU B 298 8681 7698 11078 576 -420 906 C ATOM 2918 C LEU B 298 5.921 14.934 -29.008 1.00 73.61 C ANISOU 2918 C LEU B 298 8761 8045 11161 504 -476 898 C ATOM 2919 O LEU B 298 4.859 14.363 -28.756 1.00 73.47 O ANISOU 2919 O LEU B 298 8598 8098 11218 575 -520 930 O ATOM 2920 CB LEU B 298 5.345 17.238 -29.941 1.00 74.35 C ANISOU 2920 CB LEU B 298 9002 7858 11390 628 -551 1073 C ATOM 2921 CG LEU B 298 6.022 17.276 -31.318 1.00 79.73 C ANISOU 2921 CG LEU B 298 9851 8524 11920 496 -634 1160 C ATOM 2922 CD1 LEU B 298 5.462 16.199 -32.241 1.00 80.02 C ANISOU 2922 CD1 LEU B 298 9841 8688 11874 449 -780 1246 C ATOM 2923 CD2 LEU B 298 5.809 18.624 -31.976 1.00 84.32 C ANISOU 2923 CD2 LEU B 298 10564 8921 12552 546 -693 1283 C ATOM 2924 N ALA B 299 7.011 14.287 -29.465 1.00 68.08 N ANISOU 2924 N ALA B 299 8141 7409 10315 366 -467 851 N ATOM 2925 CA ALA B 299 7.043 12.839 -29.693 1.00 66.43 C ANISOU 2925 CA ALA B 299 7874 7346 10020 295 -511 829 C ATOM 2926 C ALA B 299 7.257 12.052 -28.401 1.00 68.52 C ANISOU 2926 C ALA B 299 8046 7690 10299 302 -427 706 C ATOM 2927 O ALA B 299 6.856 10.889 -28.332 1.00 67.40 O ANISOU 2927 O ALA B 299 7823 7654 10132 284 -468 703 O ATOM 2928 CB ALA B 299 8.124 12.484 -30.702 1.00 66.75 C ANISOU 2928 CB ALA B 299 8039 7408 9914 157 -515 820 C ATOM 2929 N LEU B 300 7.889 12.684 -27.385 1.00 64.72 N ANISOU 2929 N LEU B 300 7593 7149 9848 319 -319 609 N ATOM 2930 CA LEU B 300 8.209 12.082 -26.086 1.00 63.56 C ANISOU 2930 CA LEU B 300 7398 7059 9693 317 -246 493 C ATOM 2931 C LEU B 300 7.003 11.452 -25.346 1.00 66.86 C ANISOU 2931 C LEU B 300 7691 7544 10169 393 -241 505 C ATOM 2932 O LEU B 300 7.143 10.286 -24.972 1.00 65.63 O ANISOU 2932 O LEU B 300 7495 7484 9957 346 -250 466 O ATOM 2933 CB LEU B 300 8.949 13.069 -25.170 1.00 63.92 C ANISOU 2933 CB LEU B 300 7518 7010 9760 321 -152 397 C ATOM 2934 CG LEU B 300 10.050 12.466 -24.304 1.00 67.81 C ANISOU 2934 CG LEU B 300 8025 7553 10187 245 -118 276 C ATOM 2935 CD1 LEU B 300 11.398 12.548 -25.000 1.00 67.76 C ANISOU 2935 CD1 LEU B 300 8078 7535 10133 136 -127 247 C ATOM 2936 CD2 LEU B 300 10.130 13.167 -22.966 1.00 71.00 C ANISOU 2936 CD2 LEU B 300 8471 7889 10616 282 -40 183 C ATOM 2937 N PRO B 301 5.826 12.120 -25.142 1.00 63.99 N ANISOU 2937 N PRO B 301 7258 7131 9925 506 -224 561 N ATOM 2938 CA PRO B 301 4.717 11.446 -24.432 1.00 63.74 C ANISOU 2938 CA PRO B 301 7089 7174 9956 562 -195 567 C ATOM 2939 C PRO B 301 4.153 10.214 -25.146 1.00 66.32 C ANISOU 2939 C PRO B 301 7324 7614 10260 510 -306 642 C ATOM 2940 O PRO B 301 3.618 9.329 -24.480 1.00 65.43 O ANISOU 2940 O PRO B 301 7124 7583 10156 502 -275 622 O ATOM 2941 CB PRO B 301 3.669 12.551 -24.262 1.00 67.26 C ANISOU 2941 CB PRO B 301 7469 7527 10561 700 -149 613 C ATOM 2942 CG PRO B 301 4.399 13.829 -24.488 1.00 72.22 C ANISOU 2942 CG PRO B 301 8236 8016 11191 716 -128 596 C ATOM 2943 CD PRO B 301 5.441 13.500 -25.502 1.00 66.88 C ANISOU 2943 CD PRO B 301 7659 7364 10389 593 -220 619 C ATOM 2944 N PHE B 302 4.295 10.148 -26.489 1.00 62.69 N ANISOU 2944 N PHE B 302 6906 7155 9758 461 -431 724 N ATOM 2945 CA PHE B 302 3.876 9.009 -27.314 1.00 62.00 C ANISOU 2945 CA PHE B 302 6772 7162 9624 392 -553 787 C ATOM 2946 C PHE B 302 4.883 7.868 -27.149 1.00 64.11 C ANISOU 2946 C PHE B 302 7104 7495 9759 285 -535 700 C ATOM 2947 O PHE B 302 4.486 6.702 -27.120 1.00 63.48 O ANISOU 2947 O PHE B 302 6966 7496 9657 239 -578 705 O ATOM 2948 CB PHE B 302 3.771 9.407 -28.796 1.00 64.47 C ANISOU 2948 CB PHE B 302 7151 7439 9906 367 -690 896 C ATOM 2949 CG PHE B 302 2.658 10.375 -29.121 1.00 67.65 C ANISOU 2949 CG PHE B 302 7476 7775 10452 476 -760 1010 C ATOM 2950 CD1 PHE B 302 1.380 9.916 -29.417 1.00 71.69 C ANISOU 2950 CD1 PHE B 302 7834 8345 11061 505 -875 1102 C ATOM 2951 CD2 PHE B 302 2.895 11.743 -29.164 1.00 70.40 C ANISOU 2951 CD2 PHE B 302 7901 7996 10853 549 -722 1028 C ATOM 2952 CE1 PHE B 302 0.353 10.811 -29.729 1.00 74.45 C ANISOU 2952 CE1 PHE B 302 8087 8629 11570 620 -955 1212 C ATOM 2953 CE2 PHE B 302 1.869 12.637 -29.479 1.00 75.09 C ANISOU 2953 CE2 PHE B 302 8422 8512 11597 667 -797 1139 C ATOM 2954 CZ PHE B 302 0.605 12.165 -29.763 1.00 74.33 C ANISOU 2954 CZ PHE B 302 8155 8478 11609 708 -917 1232 C ATOM 2955 N ALA B 303 6.186 8.214 -27.039 1.00 59.63 N ANISOU 2955 N ALA B 303 6651 6885 9121 248 -473 621 N ATOM 2956 CA ALA B 303 7.288 7.270 -26.840 1.00 58.12 C ANISOU 2956 CA ALA B 303 6510 6739 8835 166 -452 531 C ATOM 2957 C ALA B 303 7.218 6.666 -25.436 1.00 61.49 C ANISOU 2957 C ALA B 303 6886 7204 9275 184 -391 462 C ATOM 2958 O ALA B 303 7.514 5.478 -25.270 1.00 60.84 O ANISOU 2958 O ALA B 303 6801 7177 9138 132 -416 429 O ATOM 2959 CB ALA B 303 8.620 7.968 -27.046 1.00 58.54 C ANISOU 2959 CB ALA B 303 6664 6731 8847 128 -400 472 C ATOM 2960 N ILE B 304 6.810 7.486 -24.434 1.00 57.73 N ANISOU 2960 N ILE B 304 6386 6686 8863 257 -309 441 N ATOM 2961 CA ILE B 304 6.626 7.078 -23.037 1.00 57.18 C ANISOU 2961 CA ILE B 304 6295 6642 8787 272 -235 380 C ATOM 2962 C ILE B 304 5.466 6.066 -22.979 1.00 61.35 C ANISOU 2962 C ILE B 304 6719 7248 9344 267 -260 440 C ATOM 2963 O ILE B 304 5.594 5.034 -22.311 1.00 60.56 O ANISOU 2963 O ILE B 304 6627 7196 9187 220 -253 407 O ATOM 2964 CB ILE B 304 6.428 8.315 -22.099 1.00 60.86 C ANISOU 2964 CB ILE B 304 6785 7031 9306 348 -125 336 C ATOM 2965 CG1 ILE B 304 7.745 9.112 -21.948 1.00 60.86 C ANISOU 2965 CG1 ILE B 304 6902 6958 9264 320 -107 257 C ATOM 2966 CG2 ILE B 304 5.881 7.916 -20.717 1.00 61.63 C ANISOU 2966 CG2 ILE B 304 6866 7160 9392 366 -30 290 C ATOM 2967 CD1 ILE B 304 7.577 10.605 -21.604 1.00 67.62 C ANISOU 2967 CD1 ILE B 304 7806 7702 10186 390 -27 234 C ATOM 2968 N LEU B 305 4.368 6.344 -23.732 1.00 58.40 N ANISOU 2968 N LEU B 305 6248 6881 9061 307 -305 534 N ATOM 2969 CA LEU B 305 3.172 5.498 -23.849 1.00 58.73 C ANISOU 2969 CA LEU B 305 6163 6995 9158 292 -346 603 C ATOM 2970 C LEU B 305 3.527 4.101 -24.375 1.00 62.15 C ANISOU 2970 C LEU B 305 6629 7486 9497 185 -442 606 C ATOM 2971 O LEU B 305 2.964 3.113 -23.898 1.00 61.93 O ANISOU 2971 O LEU B 305 6545 7513 9472 142 -436 615 O ATOM 2972 CB LEU B 305 2.120 6.172 -24.755 1.00 59.99 C ANISOU 2972 CB LEU B 305 6214 7138 9440 353 -420 709 C ATOM 2973 CG LEU B 305 0.796 5.427 -24.980 1.00 65.61 C ANISOU 2973 CG LEU B 305 6761 7924 10244 335 -484 791 C ATOM 2974 CD1 LEU B 305 -0.148 5.599 -23.807 1.00 66.81 C ANISOU 2974 CD1 LEU B 305 6777 8092 10517 401 -340 776 C ATOM 2975 CD2 LEU B 305 0.127 5.888 -26.250 1.00 68.99 C ANISOU 2975 CD2 LEU B 305 7126 8338 10749 360 -637 904 C ATOM 2976 N LEU B 306 4.475 4.028 -25.335 1.00 58.14 N ANISOU 2976 N LEU B 306 6223 6960 8909 140 -514 594 N ATOM 2977 CA LEU B 306 4.968 2.781 -25.922 1.00 57.44 C ANISOU 2977 CA LEU B 306 6190 6905 8730 48 -589 578 C ATOM 2978 C LEU B 306 5.672 1.906 -24.878 1.00 60.52 C ANISOU 2978 C LEU B 306 6623 7305 9066 20 -537 497 C ATOM 2979 O LEU B 306 5.548 0.683 -24.929 1.00 59.89 O ANISOU 2979 O LEU B 306 6549 7256 8952 -41 -584 499 O ATOM 2980 CB LEU B 306 5.893 3.066 -27.114 1.00 57.30 C ANISOU 2980 CB LEU B 306 6277 6854 8639 14 -635 568 C ATOM 2981 CG LEU B 306 5.200 3.257 -28.455 1.00 62.83 C ANISOU 2981 CG LEU B 306 6981 7559 9334 -11 -746 662 C ATOM 2982 CD1 LEU B 306 5.893 4.321 -29.274 1.00 63.32 C ANISOU 2982 CD1 LEU B 306 7141 7561 9356 -5 -739 671 C ATOM 2983 CD2 LEU B 306 5.135 1.952 -29.227 1.00 65.21 C ANISOU 2983 CD2 LEU B 306 7324 7899 9555 -107 -836 664 C ATOM 2984 N GLY B 307 6.362 2.544 -23.930 1.00 56.89 N ANISOU 2984 N GLY B 307 6204 6812 8601 62 -454 432 N ATOM 2985 CA GLY B 307 7.030 1.866 -22.824 1.00 56.45 C ANISOU 2985 CA GLY B 307 6199 6757 8492 42 -424 365 C ATOM 2986 C GLY B 307 6.031 1.182 -21.909 1.00 61.45 C ANISOU 2986 C GLY B 307 6787 7428 9134 28 -389 396 C ATOM 2987 O GLY B 307 6.259 0.051 -21.468 1.00 60.99 O ANISOU 2987 O GLY B 307 6770 7381 9023 -22 -416 383 O ATOM 2988 N PHE B 308 4.894 1.864 -21.653 1.00 59.06 N ANISOU 2988 N PHE B 308 6395 7137 8906 73 -322 440 N ATOM 2989 CA PHE B 308 3.778 1.366 -20.850 1.00 59.69 C ANISOU 2989 CA PHE B 308 6404 7258 9018 57 -255 474 C ATOM 2990 C PHE B 308 3.014 0.279 -21.610 1.00 64.07 C ANISOU 2990 C PHE B 308 6882 7860 9601 -14 -344 545 C ATOM 2991 O PHE B 308 2.434 -0.607 -20.980 1.00 64.23 O ANISOU 2991 O PHE B 308 6879 7912 9614 -71 -313 565 O ATOM 2992 CB PHE B 308 2.813 2.508 -20.495 1.00 62.59 C ANISOU 2992 CB PHE B 308 6674 7617 9491 140 -145 492 C ATOM 2993 CG PHE B 308 3.243 3.410 -19.363 1.00 64.28 C ANISOU 2993 CG PHE B 308 6972 7782 9671 194 -18 413 C ATOM 2994 CD1 PHE B 308 3.178 2.977 -18.043 1.00 67.79 C ANISOU 2994 CD1 PHE B 308 7482 8238 10038 162 83 372 C ATOM 2995 CD2 PHE B 308 3.646 4.717 -19.610 1.00 66.30 C ANISOU 2995 CD2 PHE B 308 7256 7972 9963 268 1 383 C ATOM 2996 CE1 PHE B 308 3.550 3.822 -16.993 1.00 69.12 C ANISOU 2996 CE1 PHE B 308 7753 8356 10153 200 194 292 C ATOM 2997 CE2 PHE B 308 4.002 5.565 -18.558 1.00 69.57 C ANISOU 2997 CE2 PHE B 308 7762 8331 10342 308 115 301 C ATOM 2998 CZ PHE B 308 3.960 5.109 -17.258 1.00 68.12 C ANISOU 2998 CZ PHE B 308 7650 8162 10069 273 208 252 C ATOM 2999 N THR B 309 3.000 0.359 -22.963 1.00 60.54 N ANISOU 2999 N THR B 309 6411 7414 9177 -23 -456 585 N ATOM 3000 CA THR B 309 2.327 -0.602 -23.847 1.00 60.81 C ANISOU 3000 CA THR B 309 6393 7486 9226 -102 -568 647 C ATOM 3001 C THR B 309 2.991 -1.987 -23.740 1.00 64.33 C ANISOU 3001 C THR B 309 6946 7923 9575 -187 -612 608 C ATOM 3002 O THR B 309 2.299 -2.997 -23.871 1.00 64.52 O ANISOU 3002 O THR B 309 6935 7972 9610 -268 -661 648 O ATOM 3003 CB THR B 309 2.220 -0.042 -25.281 1.00 67.74 C ANISOU 3003 CB THR B 309 7258 8356 10123 -92 -680 694 C ATOM 3004 OG1 THR B 309 1.533 1.210 -25.227 1.00 68.58 O ANISOU 3004 OG1 THR B 309 7261 8455 10339 -1 -642 739 O ATOM 3005 CG2 THR B 309 1.471 -0.971 -26.235 1.00 66.30 C ANISOU 3005 CG2 THR B 309 7035 8210 9945 -186 -817 757 C ATOM 3006 N ASN B 310 4.310 -2.031 -23.440 1.00 59.94 N ANISOU 3006 N ASN B 310 6511 7324 8940 -167 -594 531 N ATOM 3007 CA ASN B 310 5.065 -3.275 -23.254 1.00 59.41 C ANISOU 3007 CA ASN B 310 6543 7228 8801 -220 -635 490 C ATOM 3008 C ASN B 310 4.500 -4.089 -22.083 1.00 64.64 C ANISOU 3008 C ASN B 310 7208 7900 9454 -264 -593 513 C ATOM 3009 O ASN B 310 4.506 -5.318 -22.136 1.00 64.75 O ANISOU 3009 O ASN B 310 7272 7893 9436 -334 -649 521 O ATOM 3010 CB ASN B 310 6.551 -2.986 -23.044 1.00 57.99 C ANISOU 3010 CB ASN B 310 6454 7004 8576 -173 -622 408 C ATOM 3011 CG ASN B 310 7.433 -4.205 -23.152 1.00 72.24 C ANISOU 3011 CG ASN B 310 8345 8766 10336 -205 -682 363 C ATOM 3012 OD1 ASN B 310 7.986 -4.687 -22.160 1.00 67.83 O ANISOU 3012 OD1 ASN B 310 7841 8178 9752 -197 -680 336 O ATOM 3013 ND2 ASN B 310 7.594 -4.726 -24.360 1.00 60.48 N ANISOU 3013 ND2 ASN B 310 6881 7264 8835 -240 -740 353 N ATOM 3014 N SER B 311 3.972 -3.396 -21.053 1.00 61.80 N ANISOU 3014 N SER B 311 6802 7561 9117 -230 -484 524 N ATOM 3015 CA SER B 311 3.344 -4.004 -19.881 1.00 62.43 C ANISOU 3015 CA SER B 311 6891 7653 9175 -280 -408 550 C ATOM 3016 C SER B 311 1.974 -4.619 -20.226 1.00 68.11 C ANISOU 3016 C SER B 311 7490 8419 9970 -359 -413 627 C ATOM 3017 O SER B 311 1.486 -5.464 -19.474 1.00 68.25 O ANISOU 3017 O SER B 311 7528 8441 9965 -437 -369 657 O ATOM 3018 CB SER B 311 3.216 -2.983 -18.757 1.00 65.88 C ANISOU 3018 CB SER B 311 7330 8097 9604 -221 -269 523 C ATOM 3019 OG SER B 311 4.493 -2.556 -18.313 1.00 73.01 O ANISOU 3019 OG SER B 311 8355 8954 10430 -174 -284 451 O ATOM 3020 N CYS B 312 1.364 -4.197 -21.359 1.00 65.75 N ANISOU 3020 N CYS B 312 7071 8152 9761 -349 -477 665 N ATOM 3021 CA CYS B 312 0.085 -4.717 -21.859 1.00 67.14 C ANISOU 3021 CA CYS B 312 7108 8374 10027 -429 -520 741 C ATOM 3022 C CYS B 312 0.345 -5.951 -22.721 1.00 70.83 C ANISOU 3022 C CYS B 312 7657 8814 10441 -528 -664 745 C ATOM 3023 O CYS B 312 -0.498 -6.846 -22.775 1.00 71.40 O ANISOU 3023 O CYS B 312 7677 8904 10550 -636 -698 794 O ATOM 3024 CB CYS B 312 -0.681 -3.655 -22.647 1.00 68.31 C ANISOU 3024 CB CYS B 312 7096 8561 10299 -366 -549 786 C ATOM 3025 SG CYS B 312 -0.880 -2.073 -21.787 1.00 72.70 S ANISOU 3025 SG CYS B 312 7574 9118 10930 -224 -380 765 S ATOM 3026 N VAL B 313 1.500 -5.975 -23.418 1.00 66.50 N ANISOU 3026 N VAL B 313 7236 8219 9814 -496 -738 688 N ATOM 3027 CA VAL B 313 1.934 -7.059 -24.310 1.00 66.38 C ANISOU 3027 CA VAL B 313 7325 8158 9736 -571 -856 667 C ATOM 3028 C VAL B 313 2.489 -8.255 -23.500 1.00 70.32 C ANISOU 3028 C VAL B 313 7950 8595 10173 -616 -842 638 C ATOM 3029 O VAL B 313 2.271 -9.402 -23.895 1.00 70.42 O ANISOU 3029 O VAL B 313 8017 8570 10168 -712 -917 647 O ATOM 3030 CB VAL B 313 2.924 -6.550 -25.407 1.00 69.52 C ANISOU 3030 CB VAL B 313 7802 8529 10082 -517 -910 613 C ATOM 3031 CG1 VAL B 313 3.325 -7.664 -26.370 1.00 69.51 C ANISOU 3031 CG1 VAL B 313 7919 8478 10014 -595 -1008 576 C ATOM 3032 CG2 VAL B 313 2.332 -5.380 -26.188 1.00 69.68 C ANISOU 3032 CG2 VAL B 313 7722 8597 10155 -480 -940 660 C ATOM 3033 N ASN B 314 3.179 -7.980 -22.365 1.00 66.53 N ANISOU 3033 N ASN B 314 7527 8095 9657 -551 -757 606 N ATOM 3034 CA ASN B 314 3.780 -8.984 -21.475 1.00 66.42 C ANISOU 3034 CA ASN B 314 7644 8013 9580 -577 -758 591 C ATOM 3035 C ASN B 314 2.824 -10.117 -21.035 1.00 72.17 C ANISOU 3035 C ASN B 314 8381 8729 10312 -702 -759 657 C ATOM 3036 O ASN B 314 3.232 -11.269 -21.182 1.00 72.00 O ANISOU 3036 O ASN B 314 8476 8627 10255 -751 -834 646 O ATOM 3037 CB ASN B 314 4.443 -8.341 -20.252 1.00 65.41 C ANISOU 3037 CB ASN B 314 7565 7881 9409 -500 -680 564 C ATOM 3038 CG ASN B 314 5.780 -7.693 -20.511 1.00 80.68 C ANISOU 3038 CG ASN B 314 9541 9787 11326 -401 -707 487 C ATOM 3039 OD1 ASN B 314 6.556 -8.098 -21.386 1.00 73.52 O ANISOU 3039 OD1 ASN B 314 8673 8839 10423 -386 -780 442 O ATOM 3040 ND2 ASN B 314 6.093 -6.681 -19.722 1.00 71.98 N ANISOU 3040 ND2 ASN B 314 8435 8705 10208 -338 -638 464 N ATOM 3041 N PRO B 315 1.574 -9.877 -20.536 1.00 70.41 N ANISOU 3041 N PRO B 315 8039 8572 10141 -759 -674 722 N ATOM 3042 CA PRO B 315 0.715 -11.016 -20.151 1.00 71.84 C ANISOU 3042 CA PRO B 315 8230 8737 10330 -900 -668 785 C ATOM 3043 C PRO B 315 0.398 -11.966 -21.306 1.00 77.17 C ANISOU 3043 C PRO B 315 8909 9377 11033 -1000 -802 796 C ATOM 3044 O PRO B 315 0.297 -13.170 -21.086 1.00 77.55 O ANISOU 3044 O PRO B 315 9058 9354 11052 -1104 -838 818 O ATOM 3045 CB PRO B 315 -0.554 -10.344 -19.612 1.00 74.56 C ANISOU 3045 CB PRO B 315 8397 9175 10758 -928 -535 840 C ATOM 3046 CG PRO B 315 -0.138 -8.972 -19.251 1.00 78.14 C ANISOU 3046 CG PRO B 315 8816 9665 11208 -788 -450 797 C ATOM 3047 CD PRO B 315 0.883 -8.599 -20.273 1.00 72.23 C ANISOU 3047 CD PRO B 315 8116 8887 10439 -701 -567 739 C ATOM 3048 N PHE B 316 0.274 -11.427 -22.533 1.00 74.22 N ANISOU 3048 N PHE B 316 8452 9043 10703 -973 -881 778 N ATOM 3049 CA PHE B 316 -0.010 -12.208 -23.734 1.00 74.91 C ANISOU 3049 CA PHE B 316 8565 9101 10798 -1070 -1019 777 C ATOM 3050 C PHE B 316 1.165 -13.083 -24.164 1.00 79.93 C ANISOU 3050 C PHE B 316 9403 9621 11345 -1057 -1090 702 C ATOM 3051 O PHE B 316 0.964 -14.268 -24.408 1.00 80.54 O ANISOU 3051 O PHE B 316 9569 9624 11408 -1167 -1159 705 O ATOM 3052 CB PHE B 316 -0.483 -11.303 -24.881 1.00 76.62 C ANISOU 3052 CB PHE B 316 8655 9391 11065 -1046 -1090 789 C ATOM 3053 CG PHE B 316 -1.843 -10.691 -24.647 1.00 79.32 C ANISOU 3053 CG PHE B 316 8772 9833 11535 -1077 -1054 872 C ATOM 3054 CD1 PHE B 316 -3.003 -11.393 -24.957 1.00 83.98 C ANISOU 3054 CD1 PHE B 316 9260 10448 12203 -1227 -1128 934 C ATOM 3055 CD2 PHE B 316 -1.966 -9.412 -24.120 1.00 81.18 C ANISOU 3055 CD2 PHE B 316 8887 10129 11827 -956 -945 883 C ATOM 3056 CE1 PHE B 316 -4.263 -10.828 -24.735 1.00 86.22 C ANISOU 3056 CE1 PHE B 316 9298 10824 12636 -1248 -1090 1010 C ATOM 3057 CE2 PHE B 316 -3.226 -8.846 -23.902 1.00 85.32 C ANISOU 3057 CE2 PHE B 316 9186 10737 12496 -967 -898 953 C ATOM 3058 CZ PHE B 316 -4.366 -9.558 -24.210 1.00 84.99 C ANISOU 3058 CZ PHE B 316 9018 10727 12547 -1109 -970 1017 C ATOM 3059 N LEU B 317 2.385 -12.516 -24.227 1.00 76.28 N ANISOU 3059 N LEU B 317 9008 9137 10839 -924 -1067 632 N ATOM 3060 CA LEU B 317 3.594 -13.233 -24.652 1.00 76.14 C ANISOU 3060 CA LEU B 317 9153 9012 10766 -885 -1114 548 C ATOM 3061 C LEU B 317 4.121 -14.286 -23.675 1.00 81.28 C ANISOU 3061 C LEU B 317 9931 9557 11395 -890 -1111 547 C ATOM 3062 O LEU B 317 4.804 -15.214 -24.113 1.00 81.17 O ANISOU 3062 O LEU B 317 10046 9433 11362 -889 -1168 491 O ATOM 3063 CB LEU B 317 4.730 -12.251 -24.993 1.00 75.12 C ANISOU 3063 CB LEU B 317 9024 8898 10620 -748 -1080 477 C ATOM 3064 CG LEU B 317 4.582 -11.360 -26.226 1.00 79.77 C ANISOU 3064 CG LEU B 317 9557 9549 11203 -737 -1102 462 C ATOM 3065 CD1 LEU B 317 5.806 -10.496 -26.390 1.00 79.03 C ANISOU 3065 CD1 LEU B 317 9481 9455 11094 -617 -1047 392 C ATOM 3066 CD2 LEU B 317 4.372 -12.176 -27.501 1.00 83.11 C ANISOU 3066 CD2 LEU B 317 10068 9927 11583 -832 -1195 432 C ATOM 3067 N TYR B 318 3.853 -14.132 -22.366 1.00 78.80 N ANISOU 3067 N TYR B 318 9597 9266 11078 -889 -1043 606 N ATOM 3068 CA TYR B 318 4.381 -15.047 -21.354 1.00 79.58 C ANISOU 3068 CA TYR B 318 9838 9261 11139 -891 -1053 621 C ATOM 3069 C TYR B 318 3.342 -15.948 -20.682 1.00 86.25 C ANISOU 3069 C TYR B 318 10717 10077 11976 -1040 -1038 711 C ATOM 3070 O TYR B 318 3.632 -17.125 -20.461 1.00 86.63 O ANISOU 3070 O TYR B 318 10915 9999 12002 -1086 -1097 721 O ATOM 3071 CB TYR B 318 5.178 -14.274 -20.290 1.00 80.14 C ANISOU 3071 CB TYR B 318 9921 9351 11177 -778 -1000 611 C ATOM 3072 CG TYR B 318 6.364 -13.502 -20.830 1.00 80.82 C ANISOU 3072 CG TYR B 318 9983 9445 11280 -642 -1016 522 C ATOM 3073 CD1 TYR B 318 7.572 -14.139 -21.100 1.00 82.78 C ANISOU 3073 CD1 TYR B 318 10323 9588 11541 -570 -1087 456 C ATOM 3074 CD2 TYR B 318 6.293 -12.127 -21.030 1.00 80.78 C ANISOU 3074 CD2 TYR B 318 9858 9545 11290 -584 -952 504 C ATOM 3075 CE1 TYR B 318 8.671 -13.431 -21.584 1.00 82.91 C ANISOU 3075 CE1 TYR B 318 10298 9616 11587 -456 -1083 373 C ATOM 3076 CE2 TYR B 318 7.384 -11.408 -21.516 1.00 80.89 C ANISOU 3076 CE2 TYR B 318 9852 9562 11319 -478 -957 426 C ATOM 3077 CZ TYR B 318 8.573 -12.064 -21.786 1.00 88.65 C ANISOU 3077 CZ TYR B 318 10914 10452 12318 -420 -1016 360 C ATOM 3078 OH TYR B 318 9.649 -11.358 -22.268 1.00 89.43 O ANISOU 3078 OH TYR B 318 10974 10559 12447 -327 -1003 282 O ATOM 3079 N CYS B 319 2.160 -15.406 -20.331 1.00 84.45 N ANISOU 3079 N CYS B 319 10353 9958 11777 -1114 -952 776 N ATOM 3080 CA CYS B 319 1.123 -16.167 -19.633 1.00 86.34 C ANISOU 3080 CA CYS B 319 10602 10185 12017 -1269 -906 864 C ATOM 3081 C CYS B 319 0.069 -16.774 -20.562 1.00 92.86 C ANISOU 3081 C CYS B 319 11348 11021 12915 -1419 -966 891 C ATOM 3082 O CYS B 319 -0.175 -17.977 -20.471 1.00 93.66 O ANISOU 3082 O CYS B 319 11560 11022 13004 -1544 -1012 924 O ATOM 3083 CB CYS B 319 0.481 -15.331 -18.528 1.00 86.98 C ANISOU 3083 CB CYS B 319 10588 10367 12093 -1271 -749 914 C ATOM 3084 SG CYS B 319 -0.704 -16.239 -17.498 1.00 92.95 S ANISOU 3084 SG CYS B 319 11371 11109 12838 -1470 -646 1022 S ATOM 3085 N PHE B 320 -0.575 -15.959 -21.421 1.00 90.58 N ANISOU 3085 N PHE B 320 10874 10843 12700 -1414 -978 885 N ATOM 3086 CA PHE B 320 -1.645 -16.432 -22.305 1.00 92.28 C ANISOU 3086 CA PHE B 320 10993 11082 12989 -1563 -1060 918 C ATOM 3087 C PHE B 320 -1.132 -17.293 -23.473 1.00 97.92 C ANISOU 3087 C PHE B 320 11853 11690 13663 -1601 -1213 854 C ATOM 3088 O PHE B 320 -1.406 -18.495 -23.491 1.00 98.65 O ANISOU 3088 O PHE B 320 12052 11684 13749 -1738 -1267 871 O ATOM 3089 CB PHE B 320 -2.540 -15.271 -22.788 1.00 94.16 C ANISOU 3089 CB PHE B 320 10982 11466 13327 -1541 -1044 945 C ATOM 3090 CG PHE B 320 -3.184 -14.461 -21.682 1.00 96.01 C ANISOU 3090 CG PHE B 320 11062 11797 13622 -1510 -873 998 C ATOM 3091 CD1 PHE B 320 -4.078 -15.050 -20.793 1.00100.66 C ANISOU 3091 CD1 PHE B 320 11602 12394 14250 -1648 -771 1068 C ATOM 3092 CD2 PHE B 320 -2.926 -13.102 -21.552 1.00 96.98 C ANISOU 3092 CD2 PHE B 320 11092 11995 13763 -1352 -800 973 C ATOM 3093 CE1 PHE B 320 -4.671 -14.300 -19.771 1.00102.08 C ANISOU 3093 CE1 PHE B 320 11649 12660 14478 -1620 -582 1103 C ATOM 3094 CE2 PHE B 320 -3.522 -12.353 -20.532 1.00100.26 C ANISOU 3094 CE2 PHE B 320 11379 12486 14231 -1319 -625 1006 C ATOM 3095 CZ PHE B 320 -4.391 -12.957 -19.650 1.00 99.95 C ANISOU 3095 CZ PHE B 320 11295 12458 14223 -1450 -510 1067 C ATOM 3096 N VAL B 321 -0.393 -16.696 -24.429 1.00 94.77 N ANISOU 3096 N VAL B 321 11473 11301 13233 -1488 -1269 778 N ATOM 3097 CA VAL B 321 0.163 -17.404 -25.592 1.00 95.34 C ANISOU 3097 CA VAL B 321 11698 11276 13253 -1512 -1385 698 C ATOM 3098 C VAL B 321 1.370 -18.259 -25.169 1.00 99.87 C ANISOU 3098 C VAL B 321 12479 11697 13771 -1443 -1373 638 C ATOM 3099 O VAL B 321 1.426 -19.443 -25.506 1.00100.43 O ANISOU 3099 O VAL B 321 12698 11638 13823 -1530 -1442 611 O ATOM 3100 CB VAL B 321 0.481 -16.448 -26.784 1.00 98.68 C ANISOU 3100 CB VAL B 321 12078 11765 13650 -1431 -1431 643 C ATOM 3101 CG1 VAL B 321 1.127 -17.189 -27.955 1.00 98.85 C ANISOU 3101 CG1 VAL B 321 12285 11679 13593 -1457 -1519 546 C ATOM 3102 CG2 VAL B 321 -0.772 -15.706 -27.249 1.00 99.21 C ANISOU 3102 CG2 VAL B 321 11945 11964 13786 -1502 -1481 717 C ATOM 3103 N GLY B 322 2.281 -17.664 -24.397 1.00 96.12 N ANISOU 3103 N GLY B 322 12009 11230 13280 -1290 -1295 621 N ATOM 3104 CA GLY B 322 3.496 -18.310 -23.906 1.00 96.15 C ANISOU 3104 CA GLY B 322 12176 11101 13256 -1196 -1296 572 C ATOM 3105 C GLY B 322 3.321 -19.397 -22.860 1.00102.02 C ANISOU 3105 C GLY B 322 13037 11734 13991 -1272 -1302 638 C ATOM 3106 O GLY B 322 4.254 -19.669 -22.099 1.00101.37 O ANISOU 3106 O GLY B 322 13059 11566 13892 -1175 -1301 630 O ATOM 3107 N ASN B 323 2.136 -20.037 -22.820 1.00100.73 N ANISOU 3107 N ASN B 323 12861 11566 13844 -1452 -1317 709 N ATOM 3108 CA ASN B 323 1.816 -21.128 -21.899 1.00102.33 C ANISOU 3108 CA ASN B 323 13189 11657 14034 -1562 -1317 785 C ATOM 3109 C ASN B 323 2.178 -22.467 -22.544 1.00108.20 C ANISOU 3109 C ASN B 323 14125 12211 14777 -1615 -1421 734 C ATOM 3110 O ASN B 323 2.596 -23.396 -21.848 1.00108.64 O ANISOU 3110 O ASN B 323 14351 12113 14816 -1618 -1444 764 O ATOM 3111 CB ASN B 323 0.328 -21.099 -21.528 1.00104.15 C ANISOU 3111 CB ASN B 323 13289 11983 14299 -1744 -1261 885 C ATOM 3112 CG ASN B 323 0.031 -21.376 -20.070 1.00126.18 C ANISOU 3112 CG ASN B 323 16134 14753 17055 -1805 -1167 985 C ATOM 3113 OD1 ASN B 323 0.767 -20.974 -19.158 1.00118.33 O ANISOU 3113 OD1 ASN B 323 15201 13757 16003 -1685 -1116 992 O ATOM 3114 ND2 ASN B 323 -1.095 -22.025 -19.816 1.00120.07 N ANISOU 3114 ND2 ASN B 323 15337 13972 16310 -2006 -1138 1066 N ATOM 3115 N ARG B 324 2.025 -22.551 -23.880 1.00105.48 N ANISOU 3115 N ARG B 324 13769 11867 14443 -1654 -1486 657 N ATOM 3116 CA ARG B 324 2.334 -23.732 -24.689 1.00106.67 C ANISOU 3116 CA ARG B 324 14107 11837 14585 -1706 -1574 582 C ATOM 3117 C ARG B 324 3.816 -23.795 -25.112 1.00110.17 C ANISOU 3117 C ARG B 324 14660 12179 15021 -1510 -1577 461 C ATOM 3118 O ARG B 324 4.216 -24.748 -25.786 1.00110.85 O ANISOU 3118 O ARG B 324 14912 12101 15106 -1522 -1628 378 O ATOM 3119 CB ARG B 324 1.377 -23.853 -25.898 1.00108.34 C ANISOU 3119 CB ARG B 324 14278 12094 14795 -1871 -1648 556 C ATOM 3120 CG ARG B 324 1.246 -22.596 -26.759 1.00119.83 C ANISOU 3120 CG ARG B 324 15569 13725 16237 -1815 -1645 521 C ATOM 3121 CD ARG B 324 0.121 -22.736 -27.768 1.00133.74 C ANISOU 3121 CD ARG B 324 17281 15536 17998 -2002 -1748 530 C ATOM 3122 NE ARG B 324 -0.288 -21.446 -28.328 1.00143.75 N ANISOU 3122 NE ARG B 324 18358 16989 19270 -1967 -1756 547 N ATOM 3123 CZ ARG B 324 0.195 -20.922 -29.451 1.00158.91 C ANISOU 3123 CZ ARG B 324 20318 18937 21125 -1902 -1793 463 C ATOM 3124 NH1 ARG B 324 1.122 -21.566 -30.149 1.00147.13 N ANISOU 3124 NH1 ARG B 324 19039 17307 19559 -1862 -1804 343 N ATOM 3125 NH2 ARG B 324 -0.245 -19.748 -29.884 1.00145.66 N ANISOU 3125 NH2 ARG B 324 18473 17416 19455 -1875 -1811 500 N ATOM 3126 N PHE B 325 4.630 -22.796 -24.687 1.00105.28 N ANISOU 3126 N PHE B 325 13947 11649 14406 -1333 -1515 447 N ATOM 3127 CA PHE B 325 6.067 -22.713 -24.973 1.00104.54 C ANISOU 3127 CA PHE B 325 13907 11482 14332 -1141 -1503 339 C ATOM 3128 C PHE B 325 6.831 -23.857 -24.303 1.00109.73 C ANISOU 3128 C PHE B 325 14734 11931 15029 -1077 -1548 339 C ATOM 3129 O PHE B 325 7.675 -24.475 -24.950 1.00109.97 O ANISOU 3129 O PHE B 325 14869 11819 15095 -992 -1565 231 O ATOM 3130 CB PHE B 325 6.642 -21.348 -24.540 1.00104.67 C ANISOU 3130 CB PHE B 325 13767 11648 14353 -998 -1436 341 C ATOM 3131 CG PHE B 325 8.087 -21.117 -24.926 1.00105.65 C ANISOU 3131 CG PHE B 325 13902 11724 14517 -814 -1413 228 C ATOM 3132 CD1 PHE B 325 8.419 -20.641 -26.189 1.00108.31 C ANISOU 3132 CD1 PHE B 325 14209 12106 14839 -783 -1373 122 C ATOM 3133 CD2 PHE B 325 9.114 -21.361 -24.021 1.00107.79 C ANISOU 3133 CD2 PHE B 325 14210 11906 14840 -679 -1432 231 C ATOM 3134 CE1 PHE B 325 9.754 -20.429 -26.546 1.00108.94 C ANISOU 3134 CE1 PHE B 325 14283 12144 14967 -624 -1325 13 C ATOM 3135 CE2 PHE B 325 10.449 -21.155 -24.381 1.00110.36 C ANISOU 3135 CE2 PHE B 325 14510 12191 15232 -512 -1409 124 C ATOM 3136 CZ PHE B 325 10.760 -20.686 -25.639 1.00108.10 C ANISOU 3136 CZ PHE B 325 14180 11953 14941 -487 -1342 13 C ATOM 3137 N GLN B 326 6.539 -24.126 -23.013 1.00106.89 N ANISOU 3137 N GLN B 326 14407 11545 14660 -1115 -1562 460 N ATOM 3138 CA GLN B 326 7.167 -25.191 -22.227 1.00107.99 C ANISOU 3138 CA GLN B 326 14721 11481 14829 -1064 -1628 494 C ATOM 3139 C GLN B 326 6.755 -26.574 -22.734 1.00113.93 C ANISOU 3139 C GLN B 326 15655 12039 15595 -1188 -1687 479 C ATOM 3140 O GLN B 326 7.576 -27.493 -22.722 1.00114.71 O ANISOU 3140 O GLN B 326 15906 11931 15749 -1095 -1743 436 O ATOM 3141 CB GLN B 326 6.828 -25.038 -20.737 1.00109.47 C ANISOU 3141 CB GLN B 326 14919 11706 14968 -1104 -1623 639 C ATOM 3142 N GLN B 327 5.490 -26.713 -23.189 1.00111.03 N ANISOU 3142 N GLN B 327 15265 11732 15191 -1397 -1680 511 N ATOM 3143 CA GLN B 327 4.941 -27.958 -23.731 1.00112.69 C ANISOU 3143 CA GLN B 327 15641 11769 15405 -1555 -1741 495 C ATOM 3144 C GLN B 327 5.571 -28.313 -25.078 1.00117.05 C ANISOU 3144 C GLN B 327 16278 12221 15976 -1489 -1759 328 C ATOM 3145 O GLN B 327 5.866 -29.485 -25.318 1.00118.31 O ANISOU 3145 O GLN B 327 16637 12151 16166 -1500 -1809 278 O ATOM 3146 CB GLN B 327 3.409 -27.882 -23.846 1.00114.52 C ANISOU 3146 CB GLN B 327 15786 12119 15606 -1803 -1736 576 C ATOM 3147 CG GLN B 327 2.670 -28.618 -22.732 1.00131.56 C ANISOU 3147 CG GLN B 327 18028 14201 17758 -1964 -1740 722 C ATOM 3148 CD GLN B 327 2.654 -30.115 -22.939 1.00153.17 C ANISOU 3148 CD GLN B 327 21010 16672 20513 -2068 -1821 709 C ATOM 3149 OE1 GLN B 327 3.525 -30.845 -22.455 1.00149.24 O ANISOU 3149 OE1 GLN B 327 20694 15974 20035 -1957 -1860 710 O ATOM 3150 NE2 GLN B 327 1.661 -30.605 -23.666 1.00146.50 N ANISOU 3150 NE2 GLN B 327 20180 15813 19672 -2286 -1860 697 N ATOM 3151 N LYS B 328 5.785 -27.303 -25.947 1.00112.36 N ANISOU 3151 N LYS B 328 15547 11786 15359 -1420 -1711 240 N ATOM 3152 CA LYS B 328 6.406 -27.482 -27.263 1.00112.57 C ANISOU 3152 CA LYS B 328 15653 11741 15376 -1360 -1697 75 C ATOM 3153 C LYS B 328 7.922 -27.688 -27.156 1.00116.68 C ANISOU 3153 C LYS B 328 16228 12131 15975 -1120 -1659 -20 C ATOM 3154 O LYS B 328 8.512 -28.315 -28.037 1.00117.41 O ANISOU 3154 O LYS B 328 16451 12074 16085 -1069 -1640 -159 O ATOM 3155 CB LYS B 328 6.062 -26.323 -28.210 1.00113.85 C ANISOU 3155 CB LYS B 328 15670 12116 15473 -1388 -1661 31 C ATOM 3156 CG LYS B 328 4.648 -26.394 -28.770 1.00128.42 C ANISOU 3156 CG LYS B 328 17498 14037 17258 -1628 -1730 79 C ATOM 3157 CD LYS B 328 4.507 -25.568 -30.039 1.00137.68 C ANISOU 3157 CD LYS B 328 18614 15344 18353 -1649 -1727 1 C ATOM 3158 CE LYS B 328 3.093 -25.565 -30.563 1.00149.27 C ANISOU 3158 CE LYS B 328 20038 16899 19777 -1881 -1828 62 C ATOM 3159 NZ LYS B 328 2.230 -24.607 -29.825 1.00157.58 N ANISOU 3159 NZ LYS B 328 20846 18154 20873 -1917 -1823 207 N ATOM 3160 N LEU B 329 8.543 -27.174 -26.072 1.00112.41 N ANISOU 3160 N LEU B 329 15585 11640 15485 -977 -1647 52 N ATOM 3161 CA LEU B 329 9.974 -27.327 -25.792 1.00112.54 C ANISOU 3161 CA LEU B 329 15613 11543 15604 -746 -1636 -14 C ATOM 3162 C LEU B 329 10.248 -28.758 -25.321 1.00118.59 C ANISOU 3162 C LEU B 329 16583 12035 16441 -726 -1717 5 C ATOM 3163 O LEU B 329 11.327 -29.296 -25.576 1.00119.16 O ANISOU 3163 O LEU B 329 16716 11940 16618 -557 -1712 -97 O ATOM 3164 CB LEU B 329 10.423 -26.325 -24.720 1.00111.20 C ANISOU 3164 CB LEU B 329 15281 11517 15454 -633 -1631 72 C ATOM 3165 CG LEU B 329 11.852 -25.814 -24.846 1.00115.54 C ANISOU 3165 CG LEU B 329 15729 12071 16101 -407 -1590 -27 C ATOM 3166 CD1 LEU B 329 11.887 -24.471 -25.560 1.00114.13 C ANISOU 3166 CD1 LEU B 329 15379 12110 15876 -398 -1489 -87 C ATOM 3167 CD2 LEU B 329 12.500 -25.687 -23.484 1.00117.93 C ANISOU 3167 CD2 LEU B 329 15993 12354 16462 -289 -1665 69 C ATOM 3168 N ARG B 330 9.264 -29.367 -24.629 1.00116.06 N ANISOU 3168 N ARG B 330 16362 11662 16073 -898 -1785 138 N ATOM 3169 CA ARG B 330 9.322 -30.745 -24.144 1.00117.99 C ANISOU 3169 CA ARG B 330 16827 11638 16367 -920 -1871 183 C ATOM 3170 C ARG B 330 8.990 -31.715 -25.285 1.00123.30 C ANISOU 3170 C ARG B 330 17671 12141 17037 -1026 -1872 66 C ATOM 3171 O ARG B 330 9.377 -32.883 -25.222 1.00124.80 O ANISOU 3171 O ARG B 330 18057 12064 17298 -985 -1925 40 O ATOM 3172 CB ARG B 330 8.357 -30.946 -22.965 1.00118.75 C ANISOU 3172 CB ARG B 330 16967 11754 16396 -1089 -1922 375 C ATOM 3173 N SER B 331 8.277 -31.225 -26.326 1.00119.08 N ANISOU 3173 N SER B 331 17074 11754 16417 -1162 -1824 -3 N ATOM 3174 CA SER B 331 7.888 -31.993 -27.511 1.00120.30 C ANISOU 3174 CA SER B 331 17394 11781 16535 -1289 -1830 -124 C ATOM 3175 C SER B 331 9.079 -32.222 -28.448 1.00124.65 C ANISOU 3175 C SER B 331 18018 12203 17141 -1100 -1758 -322 C ATOM 3176 O SER B 331 9.235 -33.330 -28.964 1.00126.33 O ANISOU 3176 O SER B 331 18446 12171 17382 -1117 -1772 -421 O ATOM 3177 CB SER B 331 6.750 -31.299 -28.254 1.00123.00 C ANISOU 3177 CB SER B 331 17635 12338 16762 -1494 -1827 -117 C ATOM 3178 OG SER B 331 5.573 -31.254 -27.464 1.00131.48 O ANISOU 3178 OG SER B 331 18643 13503 17809 -1685 -1880 52 O ATOM 3179 N VAL B 332 9.917 -31.181 -28.661 1.00119.43 N ANISOU 3179 N VAL B 332 17180 11697 16502 -923 -1668 -385 N ATOM 3180 CA VAL B 332 11.115 -31.256 -29.511 1.00119.79 C ANISOU 3180 CA VAL B 332 17253 11648 16612 -734 -1564 -574 C ATOM 3181 C VAL B 332 12.223 -32.094 -28.852 1.00124.90 C ANISOU 3181 C VAL B 332 17965 12055 17438 -518 -1584 -594 C ATOM 3182 O VAL B 332 13.025 -32.706 -29.560 1.00126.08 O ANISOU 3182 O VAL B 332 18216 12023 17667 -395 -1510 -758 O ATOM 3183 CB VAL B 332 11.637 -29.877 -30.007 1.00121.83 C ANISOU 3183 CB VAL B 332 17304 12146 16840 -638 -1451 -634 C ATOM 3184 CG1 VAL B 332 10.718 -29.285 -31.069 1.00121.07 C ANISOU 3184 CG1 VAL B 332 17212 12214 16573 -830 -1428 -668 C ATOM 3185 CG2 VAL B 332 11.854 -28.894 -28.858 1.00119.73 C ANISOU 3185 CG2 VAL B 332 16816 12057 16619 -547 -1476 -495 C ATOM 3186 N PHE B 333 12.252 -32.124 -27.504 1.00120.93 N ANISOU 3186 N PHE B 333 17410 11545 16995 -473 -1684 -427 N ATOM 3187 CA PHE B 333 13.216 -32.886 -26.706 1.00122.10 C ANISOU 3187 CA PHE B 333 17615 11469 17310 -276 -1752 -402 C ATOM 3188 C PHE B 333 12.739 -34.325 -26.455 1.00127.93 C ANISOU 3188 C PHE B 333 18621 11921 18067 -373 -1850 -356 C ATOM 3189 O PHE B 333 13.575 -35.216 -26.290 1.00129.38 O ANISOU 3189 O PHE B 333 18913 11844 18401 -204 -1886 -401 O ATOM 3190 CB PHE B 333 13.499 -32.174 -25.376 1.00122.60 C ANISOU 3190 CB PHE B 333 17518 11664 17402 -191 -1828 -240 C ATOM 3191 N ARG B 334 11.398 -34.539 -26.429 1.00124.28 N ANISOU 3191 N ARG B 334 18254 11500 17465 -645 -1894 -265 N ATOM 3192 CA ARG B 334 10.701 -35.818 -26.213 1.00155.05 C ANISOU 3192 CA ARG B 334 22406 15154 21352 -807 -1984 -204 C ATOM 3193 C ARG B 334 11.131 -36.539 -24.936 1.00183.17 C ANISOU 3193 C ARG B 334 26070 18513 25012 -707 -2102 -60 C ATOM 3194 O ARG B 334 10.439 -36.463 -23.924 1.00143.05 O ANISOU 3194 O ARG B 334 20995 13497 19861 -840 -2171 127 O ATOM 3195 CB ARG B 334 10.815 -36.742 -27.437 1.00157.28 C ANISOU 3195 CB ARG B 334 22893 15212 21654 -829 -1939 -397 C TER 3196 ARG B 334 HETATM 3197 N1 8ES B1201 9.214 6.699 -18.180 1.00 58.29 N ANISOU 3197 N1 8ES B1201 6741 6742 8664 185 -86 40 N HETATM 3198 N3 8ES B1201 12.670 10.401 -13.572 1.00 68.30 N ANISOU 3198 N3 8ES B1201 8611 7693 9646 31 -55 -418 N HETATM 3199 C4 8ES B1201 7.262 4.017 -19.037 1.00 56.47 C ANISOU 3199 C4 8ES B1201 6328 6674 8456 148 -150 212 C HETATM 3200 C5 8ES B1201 9.271 8.088 -18.170 1.00 58.98 C ANISOU 3200 C5 8ES B1201 6865 6748 8795 224 -24 7 C HETATM 3201 C6 8ES B1201 10.376 5.920 -18.609 1.00 57.65 C ANISOU 3201 C6 8ES B1201 6665 6684 8553 126 -198 24 C HETATM 3202 C7 8ES B1201 11.527 6.062 -17.608 1.00 58.84 C ANISOU 3202 C7 8ES B1201 6909 6805 8643 86 -237 -63 C HETATM 3203 C8 8ES B1201 12.760 6.109 -18.076 1.00 58.93 C ANISOU 3203 C8 8ES B1201 6908 6803 8681 49 -310 -100 C HETATM 3204 C10 8ES B1201 13.736 6.333 -15.808 1.00 61.69 C ANISOU 3204 C10 8ES B1201 7429 7109 8902 -5 -373 -217 C HETATM 3205 C13 8ES B1201 14.122 8.832 -14.154 1.00 66.78 C ANISOU 3205 C13 8ES B1201 8303 7601 9469 -43 -285 -377 C HETATM 3206 C15 8ES B1201 17.206 6.794 -13.253 1.00 66.49 C ANISOU 3206 C15 8ES B1201 8228 7632 9402 -183 -729 -429 C HETATM 3207 C17 8ES B1201 15.913 5.500 -14.827 1.00 64.13 C ANISOU 3207 C17 8ES B1201 7774 7416 9177 -90 -620 -296 C HETATM 3208 C20 8ES B1201 5.832 8.831 -16.807 1.00 61.87 C ANISOU 3208 C20 8ES B1201 7117 7105 9284 403 303 52 C HETATM 3209 C21 8ES B1201 5.861 10.239 -16.761 1.00 63.07 C ANISOU 3209 C21 8ES B1201 7317 7150 9497 471 373 8 C HETATM 3210 C22 8ES B1201 6.996 10.970 -17.195 1.00 62.53 C ANISOU 3210 C22 8ES B1201 7335 7010 9415 442 301 -28 C HETATM 3211 C24 8ES B1201 7.360 13.110 -15.864 1.00 65.52 C ANISOU 3211 C24 8ES B1201 7933 7179 9782 492 470 -196 C HETATM 3212 C26 8ES B1201 8.414 11.143 -14.412 1.00 64.72 C ANISOU 3212 C26 8ES B1201 7944 7231 9415 321 369 -262 C HETATM 3213 C28 8ES B1201 7.941 11.695 -12.093 1.00 67.35 C ANISOU 3213 C28 8ES B1201 8526 7495 9571 313 582 -420 C HETATM 3214 O1 8ES B1201 7.373 14.297 -15.829 1.00 66.38 O ANISOU 3214 O1 8ES B1201 8108 7167 9947 540 530 -237 O HETATM 3215 C25 8ES B1201 7.684 12.373 -14.555 1.00 66.03 C ANISOU 3215 C25 8ES B1201 8103 7298 9688 418 492 -275 C HETATM 3216 S 8ES B1201 7.262 12.981 -13.007 1.00 68.67 S ANISOU 3216 S 8ES B1201 8596 7562 9933 437 670 -397 S HETATM 3217 C27 8ES B1201 8.554 10.731 -12.956 1.00 65.40 C ANISOU 3217 C27 8ES B1201 8175 7332 9340 264 410 -339 C HETATM 3218 N6 8ES B1201 7.026 12.424 -17.118 1.00 64.50 N ANISOU 3218 N6 8ES B1201 7652 7130 9727 502 373 -73 N HETATM 3219 C29 8ES B1201 6.729 13.193 -18.325 1.00 65.81 C ANISOU 3219 C29 8ES B1201 7755 7231 10018 564 337 8 C HETATM 3220 C30 8ES B1201 5.252 13.049 -18.697 1.00 67.80 C ANISOU 3220 C30 8ES B1201 7851 7515 10396 667 376 100 C HETATM 3221 C35 8ES B1201 4.166 13.472 -17.698 1.00 69.96 C ANISOU 3221 C35 8ES B1201 8091 7751 10740 767 549 54 C HETATM 3222 C34 8ES B1201 2.889 13.345 -18.023 1.00 71.29 C ANISOU 3222 C34 8ES B1201 8088 7950 11048 857 583 134 C HETATM 3223 C33 8ES B1201 2.495 12.767 -19.390 1.00 70.70 C ANISOU 3223 C33 8ES B1201 7871 7948 11046 850 420 275 C HETATM 3224 C32 8ES B1201 3.432 12.402 -20.252 1.00 68.93 C ANISOU 3224 C32 8ES B1201 7707 7750 10732 758 272 310 C HETATM 3225 C31 8ES B1201 4.914 12.548 -19.876 1.00 67.78 C ANISOU 3225 C31 8ES B1201 7739 7571 10444 664 262 213 C HETATM 3226 C1 8ES B1201 6.949 8.149 -17.264 1.00 60.28 C ANISOU 3226 C1 8ES B1201 6953 6937 9014 323 164 53 C HETATM 3227 C23 8ES B1201 8.109 10.247 -17.650 1.00 60.63 C ANISOU 3227 C23 8ES B1201 7112 6818 9107 351 169 -24 C HETATM 3228 C 8ES B1201 8.097 8.870 -17.676 1.00 59.83 C ANISOU 3228 C 8ES B1201 6963 6818 8952 301 103 11 C HETATM 3229 O 8ES B1201 10.420 8.784 -18.586 1.00 58.91 O ANISOU 3229 O 8ES B1201 6899 6685 8797 190 -67 -36 O HETATM 3230 C2 8ES B1201 8.008 6.055 -17.750 1.00 58.43 C ANISOU 3230 C2 8ES B1201 6713 6809 8679 202 -29 87 C HETATM 3231 C3 8ES B1201 7.877 4.525 -17.734 1.00 57.43 C ANISOU 3231 C3 8ES B1201 6562 6753 8504 148 -95 129 C HETATM 3232 N 8ES B1201 6.919 6.743 -17.300 1.00 59.51 N ANISOU 3232 N 8ES B1201 6822 6926 8864 264 95 93 N HETATM 3233 C19 8ES B1201 11.279 6.149 -16.090 1.00 60.48 C ANISOU 3233 C19 8ES B1201 7223 6998 8758 79 -194 -109 C HETATM 3234 C18 8ES B1201 12.302 6.270 -15.256 1.00 61.43 C ANISOU 3234 C18 8ES B1201 7435 7090 8815 34 -260 -180 C HETATM 3235 C9 8ES B1201 13.939 6.261 -17.114 1.00 60.29 C ANISOU 3235 C9 8ES B1201 7148 6946 8814 3 -379 -182 C HETATM 3236 C11 8ES B1201 14.945 6.508 -14.879 1.00 63.79 C ANISOU 3236 C11 8ES B1201 7771 7344 9122 -63 -478 -295 C HETATM 3237 C16 8ES B1201 17.033 5.638 -14.010 1.00 65.44 C ANISOU 3237 C16 8ES B1201 7987 7555 9320 -141 -746 -359 C HETATM 3238 C14 8ES B1201 16.257 7.813 -13.312 1.00 66.44 C ANISOU 3238 C14 8ES B1201 8280 7587 9377 -156 -570 -438 C HETATM 3239 C12 8ES B1201 15.134 7.682 -14.130 1.00 65.58 C ANISOU 3239 C12 8ES B1201 8103 7504 9309 -89 -445 -369 C HETATM 3240 N5 8ES B1201 13.611 9.498 -15.301 1.00 66.78 N ANISOU 3240 N5 8ES B1201 8220 7577 9577 7 -199 -334 N HETATM 3241 N4 8ES B1201 12.719 10.465 -14.939 1.00 67.70 N ANISOU 3241 N4 8ES B1201 8402 7629 9692 57 -70 -353 N HETATM 3242 N2 8ES B1201 13.533 9.398 -13.083 1.00 67.73 N1- ANISOU 3242 N2 8ES B1201 8559 7677 9498 -37 -198 -427 N1- HETATM 3243 C24 OLC B1202 -8.519 14.832 -17.508 1.00 90.24 C HETATM 3244 C7 OLC B1202 -12.777 3.755 -17.674 1.00 88.04 C HETATM 3245 C6 OLC B1202 -11.720 4.820 -17.403 1.00 87.90 C HETATM 3246 C5 OLC B1202 -12.341 6.211 -17.379 1.00 87.87 C HETATM 3247 C4 OLC B1202 -11.622 7.111 -16.383 1.00 88.06 C HETATM 3248 C3 OLC B1202 -11.221 8.431 -17.030 1.00 88.18 C HETATM 3249 C2 OLC B1202 -11.631 9.614 -16.158 1.00 88.75 C HETATM 3250 C21 OLC B1202 -10.157 13.161 -16.652 1.00 89.79 C HETATM 3251 C1 OLC B1202 -11.322 10.918 -16.858 1.00 89.35 C HETATM 3252 C22 OLC B1202 -8.693 13.586 -16.648 1.00 90.26 C HETATM 3253 O19 OLC B1202 -11.973 11.259 -17.835 1.00 89.65 O HETATM 3254 O25 OLC B1202 -7.792 14.498 -18.696 1.00 90.00 O HETATM 3255 O23 OLC B1202 -8.282 13.869 -15.305 1.00 90.51 O HETATM 3256 O20 OLC B1202 -10.242 11.763 -16.360 1.00 89.60 O HETATM 3257 C9 OLA B1203 6.294 -11.710 -35.691 1.00 77.19 C HETATM 3258 C10 OLA B1203 5.725 -11.616 -34.492 1.00 77.48 C HETATM 3259 C11 OLA B1203 6.162 -10.542 -33.521 1.00 77.59 C HETATM 3260 C12 OLA B1203 4.941 -9.783 -33.009 1.00 77.32 C HETATM 3261 C13 OLA B1203 5.326 -8.791 -31.915 1.00 76.95 C HETATM 3262 C14 OLA B1203 4.696 -7.425 -32.165 1.00 76.65 C HETATM 3263 C15 OLA B1203 4.085 -6.855 -30.890 1.00 76.29 C HETATM 3264 C16 OLA B1203 3.199 -5.654 -31.200 1.00 76.19 C HETATM 3265 C17 OLA B1203 2.947 -4.815 -29.953 1.00 75.93 C HETATM 3266 C18 OLA B1203 2.309 -3.477 -30.308 1.00 75.39 C HETATM 3267 O HOH B1301 15.063 -14.093 -25.485 1.00 50.86 O CONECT 850 2863 CONECT 1490 2110 CONECT 2110 1490 CONECT 2863 850 CONECT 3197 3200 3201 3230 CONECT 3198 3241 3242 CONECT 3199 3231 CONECT 3200 3197 3228 3229 CONECT 3201 3197 3202 CONECT 3202 3201 3203 3233 CONECT 3203 3202 3235 CONECT 3204 3234 3235 3236 CONECT 3205 3239 3240 3242 CONECT 3206 3237 3238 CONECT 3207 3236 3237 CONECT 3208 3209 3226 CONECT 3209 3208 3210 CONECT 3210 3209 3218 3227 CONECT 3211 3214 3215 3218 CONECT 3212 3215 3217 CONECT 3213 3216 3217 CONECT 3214 3211 CONECT 3215 3211 3212 3216 CONECT 3216 3213 3215 CONECT 3217 3212 3213 CONECT 3218 3210 3211 3219 CONECT 3219 3218 3220 CONECT 3220 3219 3221 3225 CONECT 3221 3220 3222 CONECT 3222 3221 3223 CONECT 3223 3222 3224 CONECT 3224 3223 3225 CONECT 3225 3220 3224 CONECT 3226 3208 3228 3232 CONECT 3227 3210 3228 CONECT 3228 3200 3226 3227 CONECT 3229 3200 CONECT 3230 3197 3231 3232 CONECT 3231 3199 3230 CONECT 3232 3226 3230 CONECT 3233 3202 3234 CONECT 3234 3204 3233 CONECT 3235 3203 3204 CONECT 3236 3204 3207 3239 CONECT 3237 3206 3207 CONECT 3238 3206 3239 CONECT 3239 3205 3236 3238 CONECT 3240 3205 3241 CONECT 3241 3198 3240 CONECT 3242 3198 3205 CONECT 3243 3252 3254 CONECT 3244 3245 CONECT 3245 3244 3246 CONECT 3246 3245 3247 CONECT 3247 3246 3248 CONECT 3248 3247 3249 CONECT 3249 3248 3251 CONECT 3250 3252 3256 CONECT 3251 3249 3253 3256 CONECT 3252 3243 3250 3255 CONECT 3253 3251 CONECT 3254 3243 CONECT 3255 3252 CONECT 3256 3250 3251 CONECT 3257 3258 CONECT 3258 3257 3259 CONECT 3259 3258 3260 CONECT 3260 3259 3261 CONECT 3261 3260 3262 CONECT 3262 3261 3263 CONECT 3263 3262 3264 CONECT 3264 3263 3265 CONECT 3265 3264 3266 CONECT 3266 3265 MASTER 326 0 3 19 2 0 6 6 3266 1 74 32 END