HEADER SIGNALING PROTEIN 25-MAR-18 5ZKP TITLE CRYSTAL STRUCTURE OF THE HUMAN PLATELET-ACTIVATING FACTOR RECEPTOR IN TITLE 2 COMPLEX WITH SR 27417 COMPND MOL_ID: 1; COMPND 2 MOLECULE: PLATELET-ACTIVATING FACTOR RECEPTOR,FLAVODOXIN,PLATELET- COMPND 3 ACTIVATING FACTOR RECEPTOR; COMPND 4 CHAIN: A; COMPND 5 SYNONYM: PAFR,PAFR; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES; COMPND 8 OTHER_DETAILS: THE FUSION PROTEIN OF PLATELET-ACTIVATING FACTOR COMPND 9 RECEPTOR (UNP RESIDUES 2-216), FLAVODOXIN (UNP RESIDUES 2-148), COMPND 10 PLATELET-ACTIVATING FACTOR RECEPTOR (UNP RESIDUES 224-316), AND TAGS SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, DESULFOVIBRIO VULGARIS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606, 882; SOURCE 5 STRAIN: HILDENBOROUGH / ATCC 29579 / DSM 644 / NCIMB 8303; SOURCE 6 GENE: PTAFR, PAFR, DVU_2680; SOURCE 7 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS G PROTEIN-COUPLED RECEPTOR, PLATELET-ACTIVATING FACTOR RECEPTOR, KEYWDS 2 COMPLEX, SIGNALING PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR C.CAO,Q.ZHAO,X.C.ZHANG,B.WU REVDAT 1 20-JUN-18 5ZKP 0 JRNL AUTH C.CAO,Q.TAN,C.XU,L.HE,L.YANG,Y.ZHOU,Y.ZHOU,A.QIAO,M.LU,C.YI, JRNL AUTH 2 G.W.HAN,X.WANG,X.LI,H.YANG,Z.RAO,H.JIANG,Y.ZHAO,J.LIU, JRNL AUTH 3 R.C.STEVENS,Q.ZHAO,X.C.ZHANG,B.WU JRNL TITL STRUCTURAL BASIS FOR SIGNAL RECOGNITION AND TRANSDUCTION BY JRNL TITL 2 PLATELET-ACTIVATING-FACTOR RECEPTOR. JRNL REF NAT. STRUCT. MOL. BIOL. V. 25 488 2018 JRNL REFN ESSN 1545-9985 JRNL PMID 29808000 JRNL DOI 10.1038/S41594-018-0068-Y REMARK 2 REMARK 2 RESOLUTION. 2.81 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.10.3 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) : 2.81 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 93.5 REMARK 3 NUMBER OF REFLECTIONS : 17489 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) : 0.224 REMARK 3 R VALUE (WORKING SET) : 0.222 REMARK 3 FREE R VALUE : 0.259 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070 REMARK 3 FREE R VALUE TEST SET COUNT : 887 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 9 REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.81 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.98 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 62.88 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 1843 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2303 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1756 REMARK 3 BIN R VALUE (WORKING SET) : 0.2271 REMARK 3 BIN FREE R VALUE : 0.2950 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.72 REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3386 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 64 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 78.45 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 105.3 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 2.11510 REMARK 3 B22 (A**2) : 2.11510 REMARK 3 B33 (A**2) : -4.23020 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) : NULL REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.628 REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.326 REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.617 REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.330 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 : 0.926 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.900 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 3546 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 4844 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 1143 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : 68 ; 2.000 ; HARMONIC REMARK 3 GENERAL PLANES : 524 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 3546 ; 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 : 469 ; 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 : 4129 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.010 REMARK 3 BOND ANGLES (DEGREES) : 1.08 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.41 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 21.14 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: { A|* } REMARK 3 ORIGIN FOR THE GROUP (A): 39.1429 -10.5284 -16.3195 REMARK 3 T TENSOR REMARK 3 T11: 0.0161 T22: 0.0325 REMARK 3 T33: -0.3040 T12: -0.3182 REMARK 3 T13: -0.0220 T23: -0.0042 REMARK 3 L TENSOR REMARK 3 L11: 0.4856 L22: 2.3774 REMARK 3 L33: 6.0666 L12: -0.1872 REMARK 3 L13: -0.6358 L23: 2.0032 REMARK 3 S TENSOR REMARK 3 S11: 0.3252 S12: 0.0616 S13: -0.0851 REMARK 3 S21: 0.1469 S22: -0.4022 S23: -0.1049 REMARK 3 S31: 0.0147 S32: 0.4768 S33: 0.0770 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 5ZKP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-MAR-18. REMARK 100 THE DEPOSITION ID IS D_1300007241. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 26-MAY-15 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SPRING-8 REMARK 200 BEAMLINE : BL41XU REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18902 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4 REMARK 200 DATA REDUNDANCY : 7.600 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 16.9000 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) : 2.95 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 4XNV, 1F4P REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 64.54 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.47 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: HEPES, PEG 400, NASCN, NA CITRATE, REMARK 280 LIPIDIC CUBIC PHASE, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+2/3 REMARK 290 3555 -X+Y,-X,Z+1/3 REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z+1/3 REMARK 290 6555 -X,-X+Y,-Z+2/3 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 186.83333 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 93.41667 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 93.41667 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 186.83333 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY A -1 REMARK 465 ALA A 0 REMARK 465 PRO A 1 REMARK 465 GLU A 2 REMARK 465 PRO A 3 REMARK 465 HIS A 4 REMARK 465 ASP A 5 REMARK 465 LYS A 124 REMARK 465 THR A 125 REMARK 465 ALA A 126 REMARK 465 GLN A 127 REMARK 465 ALA A 128 REMARK 465 ASN A 129 REMARK 465 THR A 130 REMARK 465 ARG A 131 REMARK 465 LYS A 132 REMARK 465 ARG A 133 REMARK 465 GLY A 134 REMARK 465 ILE A 135 REMARK 465 SER A 136 REMARK 465 LEU A 137 REMARK 465 LYS A 316 REMARK 465 GLU A 317 REMARK 465 PHE A 318 REMARK 465 LEU A 319 REMARK 465 GLU A 320 REMARK 465 VAL A 321 REMARK 465 LEU A 322 REMARK 465 PHE A 323 REMARK 465 GLN A 324 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 SER A 6 OG REMARK 470 HIS A 8 CG ND1 CD2 CE1 NE2 REMARK 470 GLU A 12 CG CD OE1 OE2 REMARK 470 LYS A 47 CG CD CE NZ REMARK 470 ARG A 121 CG CD NE CZ NH1 NH2 REMARK 470 ILE A 123 CG1 CG2 CD1 REMARK 470 LEU A 139 CG CD1 CD2 REMARK 470 VAL A 143 CG1 CG2 REMARK 470 LYS A 179 CG CD CE NZ REMARK 470 LYS A1002 CG CD CE NZ REMARK 470 ILE A1064 CG1 CG2 CD1 REMARK 470 ASP A1068 CG OD1 OD2 REMARK 470 ASP A 264 CG OD1 OD2 REMARK 470 LYS A 266 CG CD CE NZ REMARK 470 LYS A 302 CG CD CE NZ REMARK 470 GLU A 306 CG CD OE1 OE2 REMARK 470 ARG A 312 CG CD NE CZ NH1 NH2 REMARK 470 SER A 314 OG REMARK 470 ARG A 315 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 ASN A 79 38.16 -95.31 REMARK 500 LEU A 139 -47.59 -139.23 REMARK 500 ILE A 145 -6.12 -59.71 REMARK 500 ALA A 165 -75.67 -100.57 REMARK 500 THR A1010 -70.41 -94.48 REMARK 500 ASP A1062 -76.65 -94.35 REMARK 500 SER A 314 -53.58 -124.94 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue 9ER A 1201 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue FMN A 1202 DBREF 5ZKP A 2 216 UNP P25105 PTAFR_HUMAN 2 216 DBREF 5ZKP A 1001 1147 UNP P00323 FLAV_DESVH 2 148 DBREF 5ZKP A 224 316 UNP P25105 PTAFR_HUMAN 224 316 SEQADV 5ZKP GLY A -1 UNP P25105 EXPRESSION TAG SEQADV 5ZKP ALA A 0 UNP P25105 EXPRESSION TAG SEQADV 5ZKP PRO A 1 UNP P25105 EXPRESSION TAG SEQADV 5ZKP TYR A 116 UNP P25105 PHE 116 ENGINEERED MUTATION SEQADV 5ZKP ASP A 169 UNP P25105 ASN 169 ENGINEERED MUTATION SEQADV 5ZKP ALA A 1001 UNP P00323 PRO 2 ENGINEERED MUTATION SEQADV 5ZKP TRP A 1097 UNP P00323 TYR 98 ENGINEERED MUTATION SEQADV 5ZKP ASP A 230 UNP P25105 ALA 230 ENGINEERED MUTATION SEQADV 5ZKP ALA A 234 UNP P25105 VAL 234 ENGINEERED MUTATION SEQADV 5ZKP ASN A 289 UNP P25105 ASP 289 ENGINEERED MUTATION SEQADV 5ZKP GLU A 317 UNP P25105 EXPRESSION TAG SEQADV 5ZKP PHE A 318 UNP P25105 EXPRESSION TAG SEQADV 5ZKP LEU A 319 UNP P25105 EXPRESSION TAG SEQADV 5ZKP GLU A 320 UNP P25105 EXPRESSION TAG SEQADV 5ZKP VAL A 321 UNP P25105 EXPRESSION TAG SEQADV 5ZKP LEU A 322 UNP P25105 EXPRESSION TAG SEQADV 5ZKP PHE A 323 UNP P25105 EXPRESSION TAG SEQADV 5ZKP GLN A 324 UNP P25105 EXPRESSION TAG SEQRES 1 A 466 GLY ALA PRO GLU PRO HIS ASP SER SER HIS MET ASP SER SEQRES 2 A 466 GLU PHE ARG TYR THR LEU PHE PRO ILE VAL TYR SER ILE SEQRES 3 A 466 ILE PHE VAL LEU GLY VAL ILE ALA ASN GLY TYR VAL LEU SEQRES 4 A 466 TRP VAL PHE ALA ARG LEU TYR PRO CYS LYS LYS PHE ASN SEQRES 5 A 466 GLU ILE LYS ILE PHE MET VAL ASN LEU THR MET ALA ASP SEQRES 6 A 466 MET LEU PHE LEU ILE THR LEU PRO LEU TRP ILE VAL TYR SEQRES 7 A 466 TYR GLN ASN GLN GLY ASN TRP ILE LEU PRO LYS PHE LEU SEQRES 8 A 466 CYS ASN VAL ALA GLY CYS LEU PHE PHE ILE ASN THR TYR SEQRES 9 A 466 CYS SER VAL ALA PHE LEU GLY VAL ILE THR TYR ASN ARG SEQRES 10 A 466 TYR GLN ALA VAL THR ARG PRO ILE LYS THR ALA GLN ALA SEQRES 11 A 466 ASN THR ARG LYS ARG GLY ILE SER LEU SER LEU VAL ILE SEQRES 12 A 466 TRP VAL ALA ILE VAL GLY ALA ALA SER TYR PHE LEU ILE SEQRES 13 A 466 LEU ASP SER THR ASN THR VAL PRO ASP SER ALA GLY SER SEQRES 14 A 466 GLY ASP VAL THR ARG CYS PHE GLU HIS TYR GLU LYS GLY SEQRES 15 A 466 SER VAL PRO VAL LEU ILE ILE HIS ILE PHE ILE VAL PHE SEQRES 16 A 466 SER PHE PHE LEU VAL PHE LEU ILE ILE LEU PHE CYS ASN SEQRES 17 A 466 LEU VAL ILE ILE ARG THR LEU LEU MET GLN ALA LYS ALA SEQRES 18 A 466 LEU ILE VAL TYR GLY SER THR THR GLY ASN THR GLU TYR SEQRES 19 A 466 THR ALA GLU THR ILE ALA ARG GLU LEU ALA ASP ALA GLY SEQRES 20 A 466 TYR GLU VAL ASP SER ARG ASP ALA ALA SER VAL GLU ALA SEQRES 21 A 466 GLY GLY LEU PHE GLU GLY PHE ASP LEU VAL LEU LEU GLY SEQRES 22 A 466 CYS SER THR TRP GLY ASP ASP SER ILE GLU LEU GLN ASP SEQRES 23 A 466 ASP PHE ILE PRO LEU PHE ASP SER LEU GLU GLU THR GLY SEQRES 24 A 466 ALA GLN GLY ARG LYS VAL ALA CYS PHE GLY CYS GLY ASP SEQRES 25 A 466 SER SER TRP GLU TYR PHE CYS GLY ALA VAL ASP ALA ILE SEQRES 26 A 466 GLU GLU LYS LEU LYS ASN LEU GLY ALA GLU ILE VAL GLN SEQRES 27 A 466 ASP GLY LEU ARG ILE ASP GLY ASP PRO ARG ALA ALA ARG SEQRES 28 A 466 ASP ASP ILE VAL GLY TRP ALA HIS ASP VAL ARG GLY ALA SEQRES 29 A 466 ILE ALA GLU VAL LYS ARG ARG ASP LEU TRP MET ALA CYS SEQRES 30 A 466 THR VAL LEU ALA VAL PHE ILE ILE CYS PHE VAL PRO HIS SEQRES 31 A 466 HIS VAL VAL GLN LEU PRO TRP THR LEU ALA GLU LEU GLY SEQRES 32 A 466 PHE GLN ASP SER LYS PHE HIS GLN ALA ILE ASN ASP ALA SEQRES 33 A 466 HIS GLN VAL THR LEU CYS LEU LEU SER THR ASN CYS VAL SEQRES 34 A 466 LEU ASN PRO VAL ILE TYR CYS PHE LEU THR LYS LYS PHE SEQRES 35 A 466 ARG LYS HIS LEU THR GLU LYS PHE TYR SER MET ARG SER SEQRES 36 A 466 SER ARG LYS GLU PHE LEU GLU VAL LEU PHE GLN HET 9ER A1201 33 HET FMN A1202 31 HETNAM 9ER N1,N1-DIMETHYL-N2-[(PYRIDIN-3-YL)METHYL]-N2-{4-[2,4,6- HETNAM 2 9ER TRI(PROPAN-2-YL)PHENYL]-1,3-THIAZOL-2-YL}ETHANE-1,2- HETNAM 3 9ER DIAMINE HETNAM FMN FLAVIN MONONUCLEOTIDE HETSYN FMN RIBOFLAVIN MONOPHOSPHATE FORMUL 2 9ER C28 H40 N4 S FORMUL 3 FMN C17 H21 N4 O9 P HELIX 1 AA1 PHE A 13 TYR A 44 1 32 HELIX 2 AA2 CYS A 46 LYS A 48 5 3 HELIX 3 AA3 PHE A 49 ILE A 68 1 20 HELIX 4 AA4 THR A 69 ASN A 79 1 11 HELIX 5 AA5 PRO A 86 THR A 120 1 35 HELIX 6 AA6 ILE A 141 LEU A 155 1 15 HELIX 7 AA7 PRO A 183 MET A 215 1 33 HELIX 8 AA8 GLY A 1012 ALA A 1028 1 17 HELIX 9 AA9 PHE A 1070 SER A 1076 1 7 HELIX 10 AB1 CYS A 1101 ASN A 1113 1 13 HELIX 11 AB2 PRO A 1129 ALA A 1131 5 3 HELIX 12 AB3 ALA A 1132 CYS A 244 1 37 HELIX 13 AB4 CYS A 244 GLY A 261 1 18 HELIX 14 AB5 ASP A 264 SER A 283 1 20 HELIX 15 AB6 THR A 284 SER A 313 1 30 SHEET 1 AA1 2 THR A 158 PRO A 162 0 SHEET 2 AA1 2 ASP A 169 CYS A 173 -1 O ARG A 172 N ASN A 159 SHEET 1 AA2 5 GLU A1031 ASP A1036 0 SHEET 2 AA2 5 LYS A1002 GLY A1008 1 N ILE A1005 O ARG A1035 SHEET 3 AA2 5 LEU A1051 CYS A1056 1 O LEU A1053 N LEU A1004 SHEET 4 AA2 5 LYS A1086 GLY A1093 1 O ALA A1088 N LEU A1054 SHEET 5 AA2 5 GLU A1117 ILE A1118 1 O GLU A1117 N VAL A1087 SHEET 1 AA3 5 GLU A1031 ASP A1036 0 SHEET 2 AA3 5 LYS A1002 GLY A1008 1 N ILE A1005 O ARG A1035 SHEET 3 AA3 5 LEU A1051 CYS A1056 1 O LEU A1053 N LEU A1004 SHEET 4 AA3 5 LYS A1086 GLY A1093 1 O ALA A1088 N LEU A1054 SHEET 5 AA3 5 LEU A1123 ASP A1126 1 O ILE A1125 N GLY A1091 SHEET 1 AA4 2 THR A1058 TRP A1059 0 SHEET 2 AA4 2 GLU A1065 LEU A1066 -1 O GLU A1065 N TRP A1059 SSBOND 1 CYS A 90 CYS A 173 1555 1555 2.03 SITE 1 AC1 12 TYR A 22 TRP A 73 TYR A 77 GLY A 94 SITE 2 AC1 12 PHE A 97 PHE A 98 TYR A 102 PHE A 174 SITE 3 AC1 12 ILE A 191 TRP A 255 HIS A 275 LEU A 279 SITE 1 AC2 19 GLU A 51 SER A1009 THR A1010 THR A1011 SITE 2 AC2 19 GLY A1012 ASN A1013 THR A1014 SER A1057 SITE 3 AC2 19 THR A1058 TRP A1059 GLY A1060 CYS A1092 SITE 4 AC2 19 GLY A1093 ASP A1094 TRP A1097 TYR A1099 SITE 5 AC2 19 PHE A1100 CYS A1101 GLY A1127 CRYST1 67.050 67.050 280.250 90.00 90.00 120.00 P 32 2 1 6 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 0.014914 0.008611 0.000000 0.00000 SCALE2 0.000000 0.017221 0.000000 0.00000 SCALE3 0.000000 0.000000 0.003568 0.00000 ATOM 1 N SER A 6 34.981 -3.992 30.853 1.00147.38 N ANISOU 1 N SER A 6 29700 15496 10801 -9749 471 -18 N ATOM 2 CA SER A 6 35.470 -5.041 31.750 1.00150.75 C ANISOU 2 CA SER A 6 30714 15722 10842 -9651 298 89 C ATOM 3 C SER A 6 35.985 -6.244 30.952 1.00154.06 C ANISOU 3 C SER A 6 31082 16173 11280 -9330 102 191 C ATOM 4 O SER A 6 37.142 -6.632 31.130 1.00155.44 O ANISOU 4 O SER A 6 31346 16453 11260 -9049 -301 307 O ATOM 5 CB SER A 6 34.396 -5.453 32.755 1.00157.28 C ANISOU 5 CB SER A 6 32120 16188 11449 -9921 673 16 C ATOM 6 N SER A 7 35.140 -6.813 30.053 1.00147.75 N ANISOU 6 N SER A 7 30121 15308 10711 -9355 377 133 N ATOM 7 CA SER A 7 35.505 -7.909 29.143 1.00146.10 C ANISOU 7 CA SER A 7 29829 15122 10561 -9067 239 212 C ATOM 8 C SER A 7 36.387 -7.285 28.040 1.00143.92 C ANISOU 8 C SER A 7 28857 15247 10578 -8828 -53 249 C ATOM 9 O SER A 7 35.921 -7.018 26.925 1.00140.32 O ANISOU 9 O SER A 7 27920 14928 10467 -8841 98 182 O ATOM 10 CB SER A 7 34.255 -8.565 28.556 1.00148.75 C ANISOU 10 CB SER A 7 30185 15280 11052 -9238 654 104 C ATOM 11 OG SER A 7 34.568 -9.439 27.482 1.00154.79 O ANISOU 11 OG SER A 7 30766 16107 11941 -8972 535 164 O ATOM 12 N HIS A 8 37.659 -7.004 28.400 1.00139.28 N ANISOU 12 N HIS A 8 28225 14863 9831 -8630 -467 337 N ATOM 13 CA HIS A 8 38.669 -6.355 27.560 1.00135.80 C ANISOU 13 CA HIS A 8 27173 14829 9594 -8447 -766 359 C ATOM 14 C HIS A 8 39.177 -7.262 26.421 1.00132.82 C ANISOU 14 C HIS A 8 26528 14591 9347 -8100 -934 423 C ATOM 15 O HIS A 8 40.390 -7.438 26.240 1.00133.15 O ANISOU 15 O HIS A 8 26383 14900 9309 -7807 -1318 486 O ATOM 16 CB HIS A 8 39.819 -5.798 28.430 1.00138.87 C ANISOU 16 CB HIS A 8 27618 15416 9731 -8395 -1133 391 C ATOM 17 N MET A 9 38.237 -7.814 25.637 1.00123.18 N ANISOU 17 N MET A 9 25263 13214 8327 -8139 -640 388 N ATOM 18 CA MET A 9 38.594 -8.651 24.506 1.00120.49 C ANISOU 18 CA MET A 9 24682 12975 8123 -7838 -754 438 C ATOM 19 C MET A 9 39.122 -7.754 23.412 1.00118.19 C ANISOU 19 C MET A 9 23684 13067 8155 -7774 -869 414 C ATOM 20 O MET A 9 38.386 -6.958 22.822 1.00114.70 O ANISOU 20 O MET A 9 22925 12666 7991 -7979 -620 326 O ATOM 21 CB MET A 9 37.445 -9.558 24.030 1.00121.86 C ANISOU 21 CB MET A 9 25052 12866 8383 -7926 -408 392 C ATOM 22 CG MET A 9 37.884 -10.559 22.978 1.00124.67 C ANISOU 22 CG MET A 9 25267 13284 8819 -7593 -547 456 C ATOM 23 SD MET A 9 39.361 -11.500 23.446 1.00131.91 S ANISOU 23 SD MET A 9 26512 14243 9365 -7117 -1033 608 S ATOM 24 CE MET A 9 40.500 -10.957 22.207 1.00126.59 C ANISOU 24 CE MET A 9 25032 14090 8974 -6827 -1348 623 C ATOM 25 N ASP A 10 40.435 -7.837 23.219 1.00113.66 N ANISOU 25 N ASP A 10 22888 12787 7509 -7489 -1256 479 N ATOM 26 CA ASP A 10 41.175 -7.019 22.283 1.00110.92 C ANISOU 26 CA ASP A 10 21906 12835 7403 -7434 -1406 455 C ATOM 27 C ASP A 10 42.454 -7.733 21.827 1.00114.69 C ANISOU 27 C ASP A 10 22184 13597 7796 -7024 -1787 517 C ATOM 28 O ASP A 10 42.935 -8.653 22.497 1.00116.78 O ANISOU 28 O ASP A 10 22830 13783 7756 -6769 -2005 579 O ATOM 29 CB ASP A 10 41.502 -5.682 22.981 1.00112.91 C ANISOU 29 CB ASP A 10 22061 13236 7604 -7699 -1457 401 C ATOM 30 CG ASP A 10 42.214 -4.644 22.152 1.00119.16 C ANISOU 30 CG ASP A 10 22268 14399 8608 -7754 -1555 355 C ATOM 31 OD1 ASP A 10 41.719 -4.324 21.051 1.00115.28 O ANISOU 31 OD1 ASP A 10 21463 13927 8412 -7799 -1355 325 O ATOM 32 OD2 ASP A 10 43.237 -4.112 22.629 1.00128.72 O ANISOU 32 OD2 ASP A 10 23356 15881 9672 -7778 -1818 334 O ATOM 33 N SER A 11 42.978 -7.311 20.660 1.00108.27 N ANISOU 33 N SER A 11 20787 13112 7239 -6945 -1857 492 N ATOM 34 CA SER A 11 44.230 -7.782 20.075 1.00107.93 C ANISOU 34 CA SER A 11 20415 13430 7164 -6581 -2197 516 C ATOM 35 C SER A 11 45.142 -6.559 20.048 1.00109.97 C ANISOU 35 C SER A 11 20210 14104 7468 -6745 -2355 439 C ATOM 36 O SER A 11 44.955 -5.677 19.209 1.00107.52 O ANISOU 36 O SER A 11 19519 13906 7426 -6954 -2186 391 O ATOM 37 CB SER A 11 43.998 -8.322 18.670 1.00106.81 C ANISOU 37 CB SER A 11 19988 13309 7285 -6404 -2091 532 C ATOM 38 OG SER A 11 43.020 -9.345 18.680 1.00111.59 O ANISOU 38 OG SER A 11 21028 13512 7860 -6348 -1886 576 O ATOM 39 N GLU A 12 46.084 -6.478 21.010 1.00107.22 N ANISOU 39 N GLU A 12 19938 13967 6832 -6675 -2666 416 N ATOM 40 CA GLU A 12 47.013 -5.356 21.171 1.00107.36 C ANISOU 40 CA GLU A 12 19564 14397 6831 -6878 -2830 316 C ATOM 41 C GLU A 12 47.877 -5.062 19.933 1.00108.59 C ANISOU 41 C GLU A 12 19065 15002 7194 -6803 -2925 254 C ATOM 42 O GLU A 12 48.269 -3.908 19.723 1.00108.27 O ANISOU 42 O GLU A 12 18687 15207 7243 -7119 -2888 162 O ATOM 43 CB GLU A 12 47.891 -5.557 22.415 1.00112.98 C ANISOU 43 CB GLU A 12 20479 15284 7162 -6746 -3188 288 C ATOM 44 N PHE A 13 48.148 -6.096 19.107 1.00102.58 N ANISOU 44 N PHE A 13 18159 14324 6492 -6407 -3024 298 N ATOM 45 CA PHE A 13 48.961 -5.987 17.900 1.00100.65 C ANISOU 45 CA PHE A 13 17316 14499 6427 -6288 -3109 240 C ATOM 46 C PHE A 13 48.285 -5.174 16.790 1.00100.08 C ANISOU 46 C PHE A 13 16995 14332 6701 -6584 -2765 232 C ATOM 47 O PHE A 13 48.986 -4.695 15.892 1.00 99.95 O ANISOU 47 O PHE A 13 16483 14675 6819 -6630 -2794 161 O ATOM 48 CB PHE A 13 49.416 -7.380 17.400 1.00103.32 C ANISOU 48 CB PHE A 13 17634 14923 6700 -5741 -3315 290 C ATOM 49 CG PHE A 13 48.370 -8.277 16.764 1.00102.03 C ANISOU 49 CG PHE A 13 17757 14327 6683 -5588 -3080 401 C ATOM 50 CD1 PHE A 13 48.157 -8.261 15.387 1.00102.01 C ANISOU 50 CD1 PHE A 13 17407 14373 6979 -5575 -2907 402 C ATOM 51 CD2 PHE A 13 47.647 -9.186 17.531 1.00104.25 C ANISOU 51 CD2 PHE A 13 18668 14165 6776 -5457 -3037 491 C ATOM 52 CE1 PHE A 13 47.200 -9.104 14.796 1.00100.52 C ANISOU 52 CE1 PHE A 13 17468 13812 6913 -5449 -2699 482 C ATOM 53 CE2 PHE A 13 46.701 -10.035 16.937 1.00104.81 C ANISOU 53 CE2 PHE A 13 18999 13859 6965 -5361 -2808 566 C ATOM 54 CZ PHE A 13 46.481 -9.984 15.572 1.00 99.88 C ANISOU 54 CZ PHE A 13 17991 13308 6649 -5357 -2647 555 C ATOM 55 N ARG A 14 46.937 -5.014 16.843 1.00 92.49 N ANISOU 55 N ARG A 14 16372 12905 5863 -6775 -2441 290 N ATOM 56 CA ARG A 14 46.190 -4.278 15.817 1.00 88.24 C ANISOU 56 CA ARG A 14 15650 12253 5626 -6996 -2127 277 C ATOM 57 C ARG A 14 46.534 -2.773 15.789 1.00 92.30 C ANISOU 57 C ARG A 14 15939 12948 6182 -7391 -2054 188 C ATOM 58 O ARG A 14 46.567 -2.179 14.715 1.00 90.79 O ANISOU 58 O ARG A 14 15446 12858 6190 -7492 -1917 158 O ATOM 59 CB ARG A 14 44.672 -4.529 15.911 1.00 82.64 C ANISOU 59 CB ARG A 14 15326 11059 5013 -7066 -1819 325 C ATOM 60 CG ARG A 14 43.952 -3.799 17.036 1.00 84.49 C ANISOU 60 CG ARG A 14 15926 11036 5143 -7383 -1666 301 C ATOM 61 CD ARG A 14 42.484 -4.134 17.019 1.00 83.42 C ANISOU 61 CD ARG A 14 16092 10496 5110 -7432 -1356 313 C ATOM 62 NE ARG A 14 41.756 -3.469 18.096 1.00 81.26 N ANISOU 62 NE ARG A 14 16163 9984 4729 -7718 -1192 275 N ATOM 63 CZ ARG A 14 40.659 -2.734 17.930 1.00 90.18 C ANISOU 63 CZ ARG A 14 17339 10920 6004 -7924 -887 216 C ATOM 64 NH1 ARG A 14 40.151 -2.551 16.721 1.00 70.48 N ANISOU 64 NH1 ARG A 14 14576 8438 3765 -7872 -723 188 N ATOM 65 NH2 ARG A 14 40.063 -2.180 18.971 1.00 85.86 N ANISOU 65 NH2 ARG A 14 17115 10175 5335 -8158 -750 175 N ATOM 66 N TYR A 15 46.856 -2.190 16.939 1.00 91.19 N ANISOU 66 N TYR A 15 15965 12851 5831 -7607 -2154 143 N ATOM 67 CA TYR A 15 47.218 -0.778 17.050 1.00 92.40 C ANISOU 67 CA TYR A 15 15980 13153 5975 -8015 -2088 48 C ATOM 68 C TYR A 15 48.548 -0.429 16.374 1.00101.17 C ANISOU 68 C TYR A 15 16570 14779 7090 -8058 -2259 -49 C ATOM 69 O TYR A 15 48.824 0.745 16.140 1.00101.72 O ANISOU 69 O TYR A 15 16500 14961 7187 -8423 -2146 -133 O ATOM 70 CB TYR A 15 47.198 -0.332 18.518 1.00 94.90 C ANISOU 70 CB TYR A 15 16644 13371 6041 -8233 -2156 18 C ATOM 71 CG TYR A 15 45.897 -0.671 19.208 1.00 94.65 C ANISOU 71 CG TYR A 15 17122 12850 5988 -8219 -1961 94 C ATOM 72 CD1 TYR A 15 44.671 -0.326 18.639 1.00 94.26 C ANISOU 72 CD1 TYR A 15 17185 12473 6156 -8313 -1618 115 C ATOM 73 CD2 TYR A 15 45.885 -1.398 20.390 1.00 96.38 C ANISOU 73 CD2 TYR A 15 17709 12953 5959 -8091 -2118 132 C ATOM 74 CE1 TYR A 15 43.468 -0.668 19.252 1.00 94.64 C ANISOU 74 CE1 TYR A 15 17651 12125 6183 -8316 -1421 150 C ATOM 75 CE2 TYR A 15 44.689 -1.733 21.019 1.00 95.88 C ANISOU 75 CE2 TYR A 15 18120 12449 5862 -8117 -1907 185 C ATOM 76 CZ TYR A 15 43.484 -1.347 20.460 1.00101.01 C ANISOU 76 CZ TYR A 15 18825 12814 6739 -8249 -1551 183 C ATOM 77 OH TYR A 15 42.308 -1.668 21.093 1.00100.93 O ANISOU 77 OH TYR A 15 19239 12421 6690 -8301 -1327 200 O ATOM 78 N THR A 16 49.357 -1.449 16.054 1.00100.38 N ANISOU 78 N THR A 16 16203 14987 6949 -7689 -2516 -49 N ATOM 79 CA THR A 16 50.639 -1.314 15.364 1.00102.38 C ANISOU 79 CA THR A 16 15908 15786 7205 -7670 -2687 -162 C ATOM 80 C THR A 16 50.514 -1.889 13.929 1.00104.47 C ANISOU 80 C THR A 16 15915 16071 7709 -7413 -2586 -111 C ATOM 81 O THR A 16 51.067 -1.307 12.988 1.00105.55 O ANISOU 81 O THR A 16 15665 16482 7958 -7572 -2511 -190 O ATOM 82 CB THR A 16 51.788 -1.918 16.207 1.00115.26 C ANISOU 82 CB THR A 16 17397 17838 8558 -7437 -3095 -244 C ATOM 83 OG1 THR A 16 51.632 -3.332 16.309 1.00119.58 O ANISOU 83 OG1 THR A 16 18124 18268 9044 -6912 -3261 -141 O ATOM 84 CG2 THR A 16 51.868 -1.323 17.609 1.00114.65 C ANISOU 84 CG2 THR A 16 17599 17728 8237 -7700 -3193 -297 C ATOM 85 N LEU A 17 49.746 -2.995 13.763 1.00 97.05 N ANISOU 85 N LEU A 17 15224 14815 6835 -7053 -2558 15 N ATOM 86 CA LEU A 17 49.518 -3.656 12.479 1.00 94.22 C ANISOU 86 CA LEU A 17 14688 14425 6687 -6788 -2466 69 C ATOM 87 C LEU A 17 48.705 -2.808 11.507 1.00 94.25 C ANISOU 87 C LEU A 17 14661 14210 6941 -7047 -2124 83 C ATOM 88 O LEU A 17 49.039 -2.778 10.318 1.00 93.79 O ANISOU 88 O LEU A 17 14270 14337 7031 -6988 -2069 62 O ATOM 89 CB LEU A 17 48.827 -5.018 12.695 1.00 93.56 C ANISOU 89 CB LEU A 17 14966 14011 6571 -6402 -2500 186 C ATOM 90 CG LEU A 17 48.491 -5.871 11.462 1.00 95.99 C ANISOU 90 CG LEU A 17 15167 14235 7071 -6106 -2411 245 C ATOM 91 CD1 LEU A 17 49.643 -6.788 11.094 1.00 98.48 C ANISOU 91 CD1 LEU A 17 15186 14939 7291 -5692 -2702 218 C ATOM 92 CD2 LEU A 17 47.221 -6.679 11.690 1.00 96.29 C ANISOU 92 CD2 LEU A 17 15680 13771 7133 -5994 -2254 344 C ATOM 93 N PHE A 18 47.621 -2.166 11.980 1.00 87.82 N ANISOU 93 N PHE A 18 14206 13003 6160 -7296 -1897 114 N ATOM 94 CA PHE A 18 46.767 -1.398 11.077 1.00 84.84 C ANISOU 94 CA PHE A 18 13842 12400 5992 -7468 -1590 122 C ATOM 95 C PHE A 18 47.398 -0.083 10.606 1.00 90.15 C ANISOU 95 C PHE A 18 14293 13284 6677 -7817 -1504 35 C ATOM 96 O PHE A 18 47.471 0.056 9.386 1.00 89.04 O ANISOU 96 O PHE A 18 13929 13215 6688 -7778 -1395 31 O ATOM 97 CB PHE A 18 45.354 -1.204 11.621 1.00 84.72 C ANISOU 97 CB PHE A 18 14254 11925 6012 -7560 -1370 160 C ATOM 98 CG PHE A 18 44.513 -2.433 11.343 1.00 84.88 C ANISOU 98 CG PHE A 18 14410 11717 6125 -7248 -1324 229 C ATOM 99 CD1 PHE A 18 43.932 -2.632 10.091 1.00 85.49 C ANISOU 99 CD1 PHE A 18 14350 11714 6418 -7114 -1166 241 C ATOM 100 CD2 PHE A 18 44.369 -3.430 12.306 1.00 87.56 C ANISOU 100 CD2 PHE A 18 15029 11930 6308 -7091 -1446 272 C ATOM 101 CE1 PHE A 18 43.207 -3.789 9.815 1.00 84.83 C ANISOU 101 CE1 PHE A 18 14383 11444 6406 -6861 -1123 283 C ATOM 102 CE2 PHE A 18 43.631 -4.580 12.034 1.00 89.08 C ANISOU 102 CE2 PHE A 18 15383 11902 6560 -6849 -1383 322 C ATOM 103 CZ PHE A 18 43.051 -4.749 10.792 1.00 85.27 C ANISOU 103 CZ PHE A 18 14736 11359 6304 -6750 -1220 320 C ATOM 104 N PRO A 19 47.942 0.840 11.453 1.00 88.54 N ANISOU 104 N PRO A 19 14138 13202 6302 -8161 -1550 -44 N ATOM 105 CA PRO A 19 48.580 2.047 10.895 1.00 89.33 C ANISOU 105 CA PRO A 19 14051 13494 6396 -8526 -1438 -139 C ATOM 106 C PRO A 19 49.632 1.791 9.808 1.00 94.70 C ANISOU 106 C PRO A 19 14246 14601 7134 -8450 -1518 -199 C ATOM 107 O PRO A 19 49.594 2.475 8.792 1.00 93.62 O ANISOU 107 O PRO A 19 14033 14441 7096 -8615 -1314 -220 O ATOM 108 CB PRO A 19 49.172 2.734 12.131 1.00 93.61 C ANISOU 108 CB PRO A 19 14694 14168 6705 -8861 -1548 -230 C ATOM 109 CG PRO A 19 48.294 2.310 13.230 1.00 96.91 C ANISOU 109 CG PRO A 19 15510 14255 7057 -8736 -1576 -154 C ATOM 110 CD PRO A 19 47.977 0.877 12.931 1.00 91.46 C ANISOU 110 CD PRO A 19 14772 13519 6460 -8265 -1683 -59 C ATOM 111 N ILE A 20 50.519 0.789 9.978 1.00 93.84 N ANISOU 111 N ILE A 20 13836 14864 6954 -8169 -1804 -228 N ATOM 112 CA ILE A 20 51.549 0.478 8.978 1.00 95.64 C ANISOU 112 CA ILE A 20 13570 15543 7228 -8061 -1888 -305 C ATOM 113 C ILE A 20 50.919 -0.076 7.669 1.00 98.81 C ANISOU 113 C ILE A 20 13935 15750 7858 -7777 -1734 -206 C ATOM 114 O ILE A 20 51.151 0.508 6.606 1.00 98.79 O ANISOU 114 O ILE A 20 13748 15842 7947 -7941 -1563 -248 O ATOM 115 CB ILE A 20 52.723 -0.403 9.519 1.00102.32 C ANISOU 115 CB ILE A 20 14081 16889 7906 -7796 -2256 -392 C ATOM 116 CG1 ILE A 20 52.325 -1.869 9.809 1.00102.12 C ANISOU 116 CG1 ILE A 20 14221 16702 7878 -7243 -2442 -270 C ATOM 117 CG2 ILE A 20 53.383 0.223 10.743 1.00106.53 C ANISOU 117 CG2 ILE A 20 14615 17659 8202 -8100 -2414 -517 C ATOM 118 CD1 ILE A 20 52.839 -2.890 8.755 1.00107.24 C ANISOU 118 CD1 ILE A 20 14519 17611 8616 -6817 -2545 -269 C ATOM 119 N VAL A 21 50.090 -1.155 7.752 1.00 93.85 N ANISOU 119 N VAL A 21 13522 14830 7306 -7386 -1776 -83 N ATOM 120 CA VAL A 21 49.436 -1.788 6.590 1.00 90.73 C ANISOU 120 CA VAL A 21 13113 14246 7113 -7104 -1649 1 C ATOM 121 C VAL A 21 48.598 -0.771 5.824 1.00 92.64 C ANISOU 121 C VAL A 21 13507 14197 7496 -7349 -1336 19 C ATOM 122 O VAL A 21 48.815 -0.603 4.629 1.00 92.60 O ANISOU 122 O VAL A 21 13291 14295 7597 -7336 -1230 4 O ATOM 123 CB VAL A 21 48.647 -3.084 6.961 1.00 92.71 C ANISOU 123 CB VAL A 21 13629 14213 7382 -6718 -1729 107 C ATOM 124 CG1 VAL A 21 47.671 -3.504 5.864 1.00 88.79 C ANISOU 124 CG1 VAL A 21 13201 13438 7097 -6535 -1538 178 C ATOM 125 CG2 VAL A 21 49.598 -4.228 7.294 1.00 95.12 C ANISOU 125 CG2 VAL A 21 13765 14827 7549 -6360 -2041 95 C ATOM 126 N TYR A 22 47.701 -0.049 6.525 1.00 87.80 N ANISOU 126 N TYR A 22 13266 13238 6856 -7562 -1195 39 N ATOM 127 CA TYR A 22 46.812 0.949 5.933 1.00 85.62 C ANISOU 127 CA TYR A 22 13201 12654 6675 -7739 -915 49 C ATOM 128 C TYR A 22 47.568 2.138 5.332 1.00 92.51 C ANISOU 128 C TYR A 22 13952 13701 7497 -8085 -798 -29 C ATOM 129 O TYR A 22 47.102 2.700 4.342 1.00 91.46 O ANISOU 129 O TYR A 22 13905 13393 7451 -8115 -592 -16 O ATOM 130 CB TYR A 22 45.721 1.376 6.918 1.00 85.26 C ANISOU 130 CB TYR A 22 13572 12234 6587 -7846 -809 69 C ATOM 131 CG TYR A 22 44.529 0.439 6.933 1.00 84.61 C ANISOU 131 CG TYR A 22 13656 11872 6620 -7544 -766 132 C ATOM 132 CD1 TYR A 22 44.676 -0.920 6.649 1.00 86.11 C ANISOU 132 CD1 TYR A 22 13694 12157 6865 -7216 -909 176 C ATOM 133 CD2 TYR A 22 43.251 0.909 7.225 1.00 83.70 C ANISOU 133 CD2 TYR A 22 13855 11406 6541 -7594 -573 127 C ATOM 134 CE1 TYR A 22 43.579 -1.778 6.618 1.00 83.67 C ANISOU 134 CE1 TYR A 22 13556 11589 6647 -6996 -841 214 C ATOM 135 CE2 TYR A 22 42.146 0.058 7.202 1.00 82.68 C ANISOU 135 CE2 TYR A 22 13840 11064 6512 -7363 -510 147 C ATOM 136 CZ TYR A 22 42.316 -1.284 6.894 1.00 88.03 C ANISOU 136 CZ TYR A 22 14377 11828 7242 -7090 -637 190 C ATOM 137 OH TYR A 22 41.239 -2.130 6.867 1.00 86.03 O ANISOU 137 OH TYR A 22 14256 11364 7068 -6918 -554 191 O ATOM 138 N SER A 23 48.763 2.462 5.847 1.00 92.11 N ANISOU 138 N SER A 23 13694 14012 7291 -8336 -928 -123 N ATOM 139 CA SER A 23 49.538 3.530 5.226 1.00 94.18 C ANISOU 139 CA SER A 23 13834 14462 7487 -8715 -791 -219 C ATOM 140 C SER A 23 50.317 2.999 4.003 1.00 98.71 C ANISOU 140 C SER A 23 13985 15374 8147 -8563 -815 -251 C ATOM 141 O SER A 23 50.588 3.764 3.071 1.00 99.27 O ANISOU 141 O SER A 23 14029 15470 8221 -8792 -618 -294 O ATOM 142 CB SER A 23 50.411 4.283 6.235 1.00100.68 C ANISOU 142 CB SER A 23 14633 15525 8097 -9137 -867 -342 C ATOM 143 OG SER A 23 51.615 3.621 6.581 1.00111.50 O ANISOU 143 OG SER A 23 15563 17421 9379 -9080 -1133 -439 O ATOM 144 N ILE A 24 50.627 1.683 3.980 1.00 94.47 N ANISOU 144 N ILE A 24 13166 15063 7666 -8161 -1041 -225 N ATOM 145 CA ILE A 24 51.310 1.071 2.832 1.00 94.27 C ANISOU 145 CA ILE A 24 12745 15350 7723 -7956 -1072 -254 C ATOM 146 C ILE A 24 50.285 0.866 1.709 1.00 93.53 C ANISOU 146 C ILE A 24 12824 14897 7817 -7726 -886 -143 C ATOM 147 O ILE A 24 50.568 1.208 0.564 1.00 93.03 O ANISOU 147 O ILE A 24 12632 14914 7801 -7803 -735 -170 O ATOM 148 CB ILE A 24 52.118 -0.219 3.193 1.00 98.88 C ANISOU 148 CB ILE A 24 12983 16324 8265 -7583 -1388 -284 C ATOM 149 CG1 ILE A 24 53.316 0.114 4.111 1.00103.25 C ANISOU 149 CG1 ILE A 24 13270 17349 8612 -7827 -1577 -444 C ATOM 150 CG2 ILE A 24 52.602 -0.965 1.933 1.00 99.22 C ANISOU 150 CG2 ILE A 24 12675 16610 8414 -7286 -1400 -294 C ATOM 151 CD1 ILE A 24 54.064 -1.101 4.715 1.00111.99 C ANISOU 151 CD1 ILE A 24 14103 18829 9618 -7414 -1935 -484 C ATOM 152 N ILE A 25 49.076 0.388 2.044 1.00 87.61 N ANISOU 152 N ILE A 25 12379 13754 7153 -7481 -881 -34 N ATOM 153 CA ILE A 25 48.036 0.163 1.036 1.00 85.24 C ANISOU 153 CA ILE A 25 12226 13141 7022 -7253 -725 45 C ATOM 154 C ILE A 25 47.429 1.485 0.562 1.00 88.07 C ANISOU 154 C ILE A 25 12866 13219 7377 -7519 -463 39 C ATOM 155 O ILE A 25 46.835 1.519 -0.514 1.00 87.13 O ANISOU 155 O ILE A 25 12810 12930 7366 -7367 -327 74 O ATOM 156 CB ILE A 25 46.963 -0.897 1.407 1.00 86.44 C ANISOU 156 CB ILE A 25 12563 13016 7264 -6909 -790 128 C ATOM 157 CG1 ILE A 25 46.042 -0.425 2.544 1.00 86.67 C ANISOU 157 CG1 ILE A 25 12962 12732 7238 -7059 -735 142 C ATOM 158 CG2 ILE A 25 47.615 -2.251 1.709 1.00 87.95 C ANISOU 158 CG2 ILE A 25 12541 13448 7428 -6602 -1039 142 C ATOM 159 CD1 ILE A 25 44.563 -0.579 2.215 1.00 93.96 C ANISOU 159 CD1 ILE A 25 14133 13278 8290 -6896 -580 179 C ATOM 160 N PHE A 26 47.626 2.572 1.316 1.00 85.08 N ANISOU 160 N PHE A 26 12673 12799 6855 -7900 -398 -11 N ATOM 161 CA PHE A 26 47.187 3.893 0.877 1.00 84.39 C ANISOU 161 CA PHE A 26 12907 12441 6715 -8154 -149 -24 C ATOM 162 C PHE A 26 48.121 4.406 -0.237 1.00 88.22 C ANISOU 162 C PHE A 26 13217 13145 7156 -8355 -30 -81 C ATOM 163 O PHE A 26 47.618 4.813 -1.285 1.00 85.97 O ANISOU 163 O PHE A 26 13106 12645 6913 -8285 147 -48 O ATOM 164 CB PHE A 26 47.131 4.880 2.039 1.00 87.47 C ANISOU 164 CB PHE A 26 13593 12698 6942 -8509 -106 -65 C ATOM 165 CG PHE A 26 46.630 6.250 1.667 1.00 88.82 C ANISOU 165 CG PHE A 26 14182 12542 7024 -8741 150 -77 C ATOM 166 CD1 PHE A 26 45.280 6.471 1.423 1.00 89.11 C ANISOU 166 CD1 PHE A 26 14553 12177 7129 -8501 270 -23 C ATOM 167 CD2 PHE A 26 47.502 7.333 1.605 1.00 93.58 C ANISOU 167 CD2 PHE A 26 14866 13242 7449 -9202 273 -159 C ATOM 168 CE1 PHE A 26 44.813 7.749 1.110 1.00 90.99 C ANISOU 168 CE1 PHE A 26 15226 12098 7249 -8657 490 -37 C ATOM 169 CE2 PHE A 26 47.037 8.610 1.282 1.00 97.01 C ANISOU 169 CE2 PHE A 26 15778 13321 7760 -9407 518 -165 C ATOM 170 CZ PHE A 26 45.695 8.812 1.044 1.00 93.12 C ANISOU 170 CZ PHE A 26 15641 12414 7327 -9103 615 -97 C ATOM 171 N VAL A 27 49.464 4.329 -0.043 1.00 87.48 N ANISOU 171 N VAL A 27 12768 13501 6970 -8582 -129 -177 N ATOM 172 CA VAL A 27 50.433 4.779 -1.066 1.00 90.15 C ANISOU 172 CA VAL A 27 12899 14103 7252 -8823 4 -262 C ATOM 173 C VAL A 27 50.430 3.829 -2.284 1.00 94.60 C ANISOU 173 C VAL A 27 13199 14771 7973 -8433 -18 -214 C ATOM 174 O VAL A 27 50.352 4.307 -3.425 1.00 94.06 O ANISOU 174 O VAL A 27 13238 14591 7909 -8488 185 -207 O ATOM 175 CB VAL A 27 51.868 5.070 -0.542 1.00 97.64 C ANISOU 175 CB VAL A 27 13509 15551 8038 -9230 -67 -426 C ATOM 176 CG1 VAL A 27 52.671 5.854 -1.571 1.00 99.51 C ANISOU 176 CG1 VAL A 27 13670 15960 8180 -9608 168 -531 C ATOM 177 CG2 VAL A 27 51.838 5.835 0.783 1.00 98.82 C ANISOU 177 CG2 VAL A 27 13906 15608 8034 -9571 -92 -473 C ATOM 178 N LEU A 28 50.457 2.491 -2.040 1.00 91.15 N ANISOU 178 N LEU A 28 12480 14505 7646 -8028 -256 -177 N ATOM 179 CA LEU A 28 50.394 1.478 -3.109 1.00 88.95 C ANISOU 179 CA LEU A 28 11982 14300 7513 -7627 -292 -130 C ATOM 180 C LEU A 28 49.062 1.553 -3.829 1.00 88.87 C ANISOU 180 C LEU A 28 12315 13829 7622 -7408 -148 -24 C ATOM 181 O LEU A 28 49.037 1.389 -5.045 1.00 87.61 O ANISOU 181 O LEU A 28 12088 13669 7532 -7262 -54 -7 O ATOM 182 CB LEU A 28 50.641 0.046 -2.595 1.00 88.56 C ANISOU 182 CB LEU A 28 11660 14470 7520 -7233 -574 -110 C ATOM 183 CG LEU A 28 52.055 -0.317 -2.101 1.00 96.37 C ANISOU 183 CG LEU A 28 12208 16013 8394 -7288 -773 -234 C ATOM 184 CD1 LEU A 28 52.141 -1.791 -1.793 1.00 96.13 C ANISOU 184 CD1 LEU A 28 12013 16108 8406 -6795 -1038 -193 C ATOM 185 CD2 LEU A 28 53.144 0.037 -3.123 1.00100.47 C ANISOU 185 CD2 LEU A 28 12367 16931 8875 -7480 -660 -357 C ATOM 186 N GLY A 29 47.984 1.834 -3.082 1.00 83.70 N ANISOU 186 N GLY A 29 12013 12811 6976 -7391 -130 29 N ATOM 187 CA GLY A 29 46.639 1.999 -3.629 1.00 81.48 C ANISOU 187 CA GLY A 29 12049 12122 6786 -7186 -4 94 C ATOM 188 C GLY A 29 46.560 3.137 -4.631 1.00 86.65 C ANISOU 188 C GLY A 29 12937 12616 7371 -7359 230 81 C ATOM 189 O GLY A 29 46.144 2.931 -5.776 1.00 85.01 O ANISOU 189 O GLY A 29 12749 12309 7240 -7124 302 111 O ATOM 190 N VAL A 30 47.028 4.338 -4.204 1.00 84.86 N ANISOU 190 N VAL A 30 12908 12363 6970 -7785 350 30 N ATOM 191 CA VAL A 30 47.082 5.581 -4.987 1.00 84.77 C ANISOU 191 CA VAL A 30 13223 12166 6821 -8034 595 10 C ATOM 192 C VAL A 30 47.967 5.391 -6.227 1.00 89.32 C ANISOU 192 C VAL A 30 13546 12995 7396 -8069 671 -18 C ATOM 193 O VAL A 30 47.502 5.683 -7.330 1.00 89.15 O ANISOU 193 O VAL A 30 13742 12760 7370 -7934 814 17 O ATOM 194 CB VAL A 30 47.473 6.820 -4.118 1.00 89.89 C ANISOU 194 CB VAL A 30 14154 12740 7260 -8528 704 -52 C ATOM 195 CG1 VAL A 30 47.666 8.068 -4.970 1.00 91.48 C ANISOU 195 CG1 VAL A 30 14737 12743 7277 -8822 977 -78 C ATOM 196 CG2 VAL A 30 46.434 7.087 -3.029 1.00 88.12 C ANISOU 196 CG2 VAL A 30 14247 12205 7029 -8451 664 -20 C ATOM 197 N ILE A 31 49.206 4.862 -6.057 1.00 86.50 N ANISOU 197 N ILE A 31 12725 13107 7036 -8214 567 -92 N ATOM 198 CA ILE A 31 50.145 4.571 -7.161 1.00 87.34 C ANISOU 198 CA ILE A 31 12510 13532 7142 -8245 631 -146 C ATOM 199 C ILE A 31 49.500 3.635 -8.211 1.00 89.64 C ANISOU 199 C ILE A 31 12730 13723 7606 -7744 588 -59 C ATOM 200 O ILE A 31 49.540 3.945 -9.402 1.00 89.30 O ANISOU 200 O ILE A 31 12791 13608 7532 -7743 758 -54 O ATOM 201 CB ILE A 31 51.489 4.006 -6.617 1.00 92.48 C ANISOU 201 CB ILE A 31 12615 14755 7767 -8395 472 -264 C ATOM 202 CG1 ILE A 31 52.348 5.118 -5.977 1.00 96.06 C ANISOU 202 CG1 ILE A 31 13109 15378 8011 -9000 584 -397 C ATOM 203 CG2 ILE A 31 52.270 3.243 -7.705 1.00 93.80 C ANISOU 203 CG2 ILE A 31 12357 15286 7996 -8227 466 -310 C ATOM 204 CD1 ILE A 31 53.402 4.626 -5.015 1.00103.06 C ANISOU 204 CD1 ILE A 31 13513 16787 8857 -9111 363 -523 C ATOM 205 N ALA A 32 48.891 2.508 -7.753 1.00 85.01 N ANISOU 205 N ALA A 32 12006 13114 7179 -7341 373 2 N ATOM 206 CA ALA A 32 48.205 1.521 -8.583 1.00 82.49 C ANISOU 206 CA ALA A 32 11627 12695 7020 -6879 314 70 C ATOM 207 C ALA A 32 47.131 2.208 -9.421 1.00 87.19 C ANISOU 207 C ALA A 32 12635 12884 7609 -6782 486 118 C ATOM 208 O ALA A 32 47.180 2.104 -10.645 1.00 87.42 O ANISOU 208 O ALA A 32 12648 12911 7655 -6647 573 128 O ATOM 209 CB ALA A 32 47.585 0.437 -7.713 1.00 80.99 C ANISOU 209 CB ALA A 32 11358 12462 6952 -6571 98 114 C ATOM 210 N ASN A 33 46.217 2.967 -8.769 1.00 83.77 N ANISOU 210 N ASN A 33 12582 12122 7126 -6849 536 135 N ATOM 211 CA ASN A 33 45.142 3.730 -9.411 1.00 83.18 C ANISOU 211 CA ASN A 33 12935 11661 7007 -6721 677 161 C ATOM 212 C ASN A 33 45.667 4.770 -10.413 1.00 91.53 C ANISOU 212 C ASN A 33 14239 12647 7890 -6953 900 147 C ATOM 213 O ASN A 33 45.064 4.972 -11.471 1.00 91.38 O ANISOU 213 O ASN A 33 14446 12422 7852 -6726 986 172 O ATOM 214 CB ASN A 33 44.290 4.414 -8.361 1.00 82.21 C ANISOU 214 CB ASN A 33 13141 11266 6829 -6787 687 157 C ATOM 215 CG ASN A 33 43.022 3.678 -8.060 1.00104.30 C ANISOU 215 CG ASN A 33 15930 13921 9777 -6413 573 167 C ATOM 216 OD1 ASN A 33 42.129 3.571 -8.905 1.00 99.90 O ANISOU 216 OD1 ASN A 33 15485 13204 9270 -6103 602 166 O ATOM 217 ND2 ASN A 33 42.905 3.175 -6.840 1.00 94.95 N ANISOU 217 ND2 ASN A 33 14627 12800 8651 -6448 448 162 N ATOM 218 N GLY A 34 46.781 5.408 -10.072 1.00 91.29 N ANISOU 218 N GLY A 34 14175 12795 7717 -7411 993 94 N ATOM 219 CA GLY A 34 47.420 6.397 -10.927 1.00 94.09 C ANISOU 219 CA GLY A 34 14774 13103 7873 -7732 1237 62 C ATOM 220 C GLY A 34 48.023 5.776 -12.166 1.00 99.61 C ANISOU 220 C GLY A 34 15193 14031 8623 -7616 1276 55 C ATOM 221 O GLY A 34 47.956 6.364 -13.251 1.00100.85 O ANISOU 221 O GLY A 34 15662 13999 8657 -7634 1465 68 O ATOM 222 N TYR A 35 48.608 4.568 -12.010 1.00 95.43 N ANISOU 222 N TYR A 35 14105 13899 8256 -7471 1094 32 N ATOM 223 CA TYR A 35 49.226 3.828 -13.111 1.00 95.36 C ANISOU 223 CA TYR A 35 13772 14154 8308 -7321 1107 15 C ATOM 224 C TYR A 35 48.168 3.336 -14.120 1.00 94.48 C ANISOU 224 C TYR A 35 13821 13776 8302 -6841 1084 98 C ATOM 225 O TYR A 35 48.485 3.159 -15.287 1.00 94.13 O ANISOU 225 O TYR A 35 13726 13801 8240 -6759 1179 95 O ATOM 226 CB TYR A 35 50.113 2.690 -12.578 1.00 97.34 C ANISOU 226 CB TYR A 35 13422 14887 8675 -7248 901 -39 C ATOM 227 CG TYR A 35 51.035 2.101 -13.619 1.00101.39 C ANISOU 227 CG TYR A 35 13570 15748 9204 -7188 947 -95 C ATOM 228 CD1 TYR A 35 52.299 2.638 -13.844 1.00107.14 C ANISOU 228 CD1 TYR A 35 14101 16822 9786 -7622 1108 -222 C ATOM 229 CD2 TYR A 35 50.656 0.988 -14.365 1.00100.68 C ANISOU 229 CD2 TYR A 35 13324 15663 9267 -6714 837 -39 C ATOM 230 CE1 TYR A 35 53.154 2.099 -14.807 1.00111.04 C ANISOU 230 CE1 TYR A 35 14237 17665 10287 -7566 1166 -293 C ATOM 231 CE2 TYR A 35 51.494 0.447 -15.340 1.00103.42 C ANISOU 231 CE2 TYR A 35 13351 16323 9620 -6639 887 -93 C ATOM 232 CZ TYR A 35 52.745 1.004 -15.558 1.00116.30 C ANISOU 232 CZ TYR A 35 14773 18307 11108 -7056 1053 -221 C ATOM 233 OH TYR A 35 53.574 0.461 -16.519 1.00118.47 O ANISOU 233 OH TYR A 35 14709 18919 11384 -6978 1115 -293 O ATOM 234 N VAL A 36 46.909 3.174 -13.677 1.00 87.83 N ANISOU 234 N VAL A 36 13178 12643 7550 -6546 970 154 N ATOM 235 CA VAL A 36 45.777 2.775 -14.512 1.00 84.99 C ANISOU 235 CA VAL A 36 12969 12045 7277 -6105 934 200 C ATOM 236 C VAL A 36 45.445 3.952 -15.415 1.00 91.01 C ANISOU 236 C VAL A 36 14234 12498 7848 -6162 1143 212 C ATOM 237 O VAL A 36 45.569 3.825 -16.630 1.00 91.20 O ANISOU 237 O VAL A 36 14291 12519 7841 -6026 1220 222 O ATOM 238 CB VAL A 36 44.560 2.343 -13.655 1.00 85.87 C ANISOU 238 CB VAL A 36 13125 11984 7518 -5840 772 216 C ATOM 239 CG1 VAL A 36 43.321 2.123 -14.509 1.00 83.68 C ANISOU 239 CG1 VAL A 36 13022 11476 7297 -5426 753 223 C ATOM 240 CG2 VAL A 36 44.880 1.096 -12.850 1.00 84.74 C ANISOU 240 CG2 VAL A 36 12560 12103 7533 -5755 574 213 C ATOM 241 N LEU A 37 45.070 5.101 -14.817 1.00 89.63 N ANISOU 241 N LEU A 37 14483 12053 7520 -6361 1238 210 N ATOM 242 CA LEU A 37 44.715 6.327 -15.529 1.00 91.86 C ANISOU 242 CA LEU A 37 15354 11980 7568 -6405 1436 223 C ATOM 243 C LEU A 37 45.733 6.745 -16.602 1.00102.54 C ANISOU 243 C LEU A 37 16806 13402 8752 -6673 1653 213 C ATOM 244 O LEU A 37 45.327 7.069 -17.716 1.00102.57 O ANISOU 244 O LEU A 37 17153 13179 8641 -6471 1751 240 O ATOM 245 CB LEU A 37 44.484 7.472 -14.538 1.00 92.77 C ANISOU 245 CB LEU A 37 15878 11848 7521 -6669 1516 211 C ATOM 246 CG LEU A 37 43.042 7.864 -14.264 1.00 95.58 C ANISOU 246 CG LEU A 37 16599 11857 7859 -6308 1452 220 C ATOM 247 CD1 LEU A 37 42.978 8.907 -13.178 1.00 96.85 C ANISOU 247 CD1 LEU A 37 17116 11819 7865 -6601 1530 203 C ATOM 248 CD2 LEU A 37 42.360 8.402 -15.511 1.00 97.89 C ANISOU 248 CD2 LEU A 37 17349 11850 7994 -5990 1542 237 C ATOM 249 N TRP A 38 47.046 6.714 -16.266 1.00104.38 N ANISOU 249 N TRP A 38 16730 13971 8960 -7122 1727 158 N ATOM 250 CA TRP A 38 48.183 7.059 -17.138 1.00108.50 C ANISOU 250 CA TRP A 38 17248 14655 9324 -7476 1956 109 C ATOM 251 C TRP A 38 48.205 6.157 -18.375 1.00111.84 C ANISOU 251 C TRP A 38 17440 15204 9850 -7127 1926 132 C ATOM 252 O TRP A 38 48.307 6.647 -19.502 1.00113.34 O ANISOU 252 O TRP A 38 17964 15231 9868 -7162 2123 141 O ATOM 253 CB TRP A 38 49.509 6.915 -16.348 1.00109.93 C ANISOU 253 CB TRP A 38 16956 15296 9516 -7947 1965 6 C ATOM 254 CG TRP A 38 50.761 6.952 -17.178 1.00114.48 C ANISOU 254 CG TRP A 38 17316 16195 9987 -8281 2165 -85 C ATOM 255 CD1 TRP A 38 51.225 5.977 -18.017 1.00117.14 C ANISOU 255 CD1 TRP A 38 17220 16842 10446 -8061 2122 -104 C ATOM 256 CD2 TRP A 38 51.747 7.992 -17.187 1.00118.85 C ANISOU 256 CD2 TRP A 38 18049 16825 10285 -8928 2452 -193 C ATOM 257 NE1 TRP A 38 52.398 6.382 -18.610 1.00120.51 N ANISOU 257 NE1 TRP A 38 17551 17531 10707 -8510 2374 -218 N ATOM 258 CE2 TRP A 38 52.749 7.612 -18.111 1.00124.89 C ANISOU 258 CE2 TRP A 38 18467 17958 11027 -9070 2586 -281 C ATOM 259 CE3 TRP A 38 51.873 9.224 -16.518 1.00122.66 C ANISOU 259 CE3 TRP A 38 18973 17094 10539 -9421 2626 -236 C ATOM 260 CZ2 TRP A 38 53.864 8.416 -18.377 1.00128.60 C ANISOU 260 CZ2 TRP A 38 18990 18614 11256 -9714 2898 -425 C ATOM 261 CZ3 TRP A 38 52.972 10.023 -16.792 1.00128.54 C ANISOU 261 CZ3 TRP A 38 19810 17993 11039 -10067 2933 -370 C ATOM 262 CH2 TRP A 38 53.964 9.607 -17.692 1.00131.16 C ANISOU 262 CH2 TRP A 38 19752 18724 11357 -10225 3068 -472 C ATOM 263 N VAL A 39 48.153 4.839 -18.140 1.00105.99 N ANISOU 263 N VAL A 39 16160 14745 9368 -6810 1686 137 N ATOM 264 CA VAL A 39 48.174 3.802 -19.155 1.00104.91 C ANISOU 264 CA VAL A 39 15744 14760 9358 -6456 1618 151 C ATOM 265 C VAL A 39 46.927 3.898 -20.053 1.00108.16 C ANISOU 265 C VAL A 39 16559 14786 9749 -6029 1604 217 C ATOM 266 O VAL A 39 47.081 3.899 -21.275 1.00108.52 O ANISOU 266 O VAL A 39 16726 14794 9711 -5937 1721 225 O ATOM 267 CB VAL A 39 48.401 2.421 -18.481 1.00107.01 C ANISOU 267 CB VAL A 39 15411 15376 9871 -6243 1361 137 C ATOM 268 CG1 VAL A 39 47.783 1.260 -19.262 1.00104.69 C ANISOU 268 CG1 VAL A 39 14959 15076 9744 -5733 1219 176 C ATOM 269 CG2 VAL A 39 49.887 2.187 -18.226 1.00109.10 C ANISOU 269 CG2 VAL A 39 15218 16122 10116 -6572 1400 43 C ATOM 270 N PHE A 40 45.719 4.045 -19.459 1.00103.32 N ANISOU 270 N PHE A 40 16164 13904 9188 -5782 1473 248 N ATOM 271 CA PHE A 40 44.473 4.167 -20.217 1.00102.45 C ANISOU 271 CA PHE A 40 16401 13477 9048 -5351 1431 275 C ATOM 272 C PHE A 40 44.406 5.442 -21.077 1.00109.81 C ANISOU 272 C PHE A 40 17967 14077 9678 -5440 1656 294 C ATOM 273 O PHE A 40 44.215 5.336 -22.289 1.00109.89 O ANISOU 273 O PHE A 40 18135 14001 9619 -5198 1698 308 O ATOM 274 CB PHE A 40 43.245 4.040 -19.310 1.00102.48 C ANISOU 274 CB PHE A 40 16437 13334 9168 -5093 1250 266 C ATOM 275 CG PHE A 40 41.955 3.772 -20.053 1.00103.51 C ANISOU 275 CG PHE A 40 16714 13285 9330 -4586 1144 250 C ATOM 276 CD1 PHE A 40 41.492 2.473 -20.229 1.00105.07 C ANISOU 276 CD1 PHE A 40 16515 13655 9751 -4274 964 224 C ATOM 277 CD2 PHE A 40 41.200 4.819 -20.574 1.00107.35 C ANISOU 277 CD2 PHE A 40 17751 13436 9602 -4413 1220 246 C ATOM 278 CE1 PHE A 40 40.290 2.227 -20.901 1.00105.23 C ANISOU 278 CE1 PHE A 40 16636 13552 9794 -3835 863 176 C ATOM 279 CE2 PHE A 40 40.007 4.571 -21.262 1.00109.47 C ANISOU 279 CE2 PHE A 40 18116 13593 9886 -3917 1098 202 C ATOM 280 CZ PHE A 40 39.559 3.278 -21.419 1.00105.51 C ANISOU 280 CZ PHE A 40 17166 13303 9622 -3650 921 158 C ATOM 281 N ALA A 41 44.585 6.636 -20.470 1.00108.99 N ANISOU 281 N ALA A 41 18267 13772 9373 -5787 1806 292 N ATOM 282 CA ALA A 41 44.551 7.918 -21.194 1.00111.91 C ANISOU 282 CA ALA A 41 19344 13771 9406 -5902 2041 312 C ATOM 283 C ALA A 41 45.566 7.981 -22.332 1.00117.89 C ANISOU 283 C ALA A 41 20148 14623 10021 -6140 2261 309 C ATOM 284 O ALA A 41 45.413 8.801 -23.235 1.00119.92 O ANISOU 284 O ALA A 41 21005 14556 10001 -6116 2438 335 O ATOM 285 CB ALA A 41 44.765 9.078 -20.237 1.00114.81 C ANISOU 285 CB ALA A 41 20092 13945 9585 -6317 2179 300 C ATOM 286 N ARG A 42 46.587 7.106 -22.288 1.00114.24 N ANISOU 286 N ARG A 42 19069 14606 9730 -6346 2249 270 N ATOM 287 CA ARG A 42 47.637 6.964 -23.296 1.00116.37 C ANISOU 287 CA ARG A 42 19229 15076 9909 -6574 2448 239 C ATOM 288 C ARG A 42 47.141 6.093 -24.461 1.00117.93 C ANISOU 288 C ARG A 42 19322 15281 10205 -6065 2341 274 C ATOM 289 O ARG A 42 47.292 6.482 -25.616 1.00119.65 O ANISOU 289 O ARG A 42 19903 15339 10218 -6065 2525 288 O ATOM 290 CB ARG A 42 48.915 6.387 -22.641 1.00118.87 C ANISOU 290 CB ARG A 42 18886 15916 10365 -6965 2451 154 C ATOM 291 CG ARG A 42 49.853 5.574 -23.539 1.00133.80 C ANISOU 291 CG ARG A 42 20337 18189 12314 -6988 2520 101 C ATOM 292 CD ARG A 42 50.693 4.613 -22.714 1.00149.66 C ANISOU 292 CD ARG A 42 21588 20730 14547 -7074 2360 25 C ATOM 293 NE ARG A 42 52.099 4.614 -23.126 1.00165.61 N ANISOU 293 NE ARG A 42 23279 23169 16478 -7478 2566 -98 N ATOM 294 CZ ARG A 42 53.114 4.253 -22.346 1.00180.35 C ANISOU 294 CZ ARG A 42 24576 25527 18422 -7740 2513 -214 C ATOM 295 NH1 ARG A 42 52.895 3.862 -21.095 1.00163.78 N ANISOU 295 NH1 ARG A 42 22217 23529 16482 -7644 2260 -205 N ATOM 296 NH2 ARG A 42 54.358 4.288 -22.807 1.00169.47 N ANISOU 296 NH2 ARG A 42 22884 24560 16946 -8096 2715 -356 N ATOM 297 N LEU A 43 46.537 4.934 -24.155 1.00110.95 N ANISOU 297 N LEU A 43 17984 14561 9612 -5652 2055 283 N ATOM 298 CA LEU A 43 46.038 3.973 -25.143 1.00108.89 C ANISOU 298 CA LEU A 43 17565 14339 9471 -5177 1925 300 C ATOM 299 C LEU A 43 44.816 4.456 -25.948 1.00112.92 C ANISOU 299 C LEU A 43 18621 14447 9836 -4762 1891 334 C ATOM 300 O LEU A 43 44.469 3.838 -26.961 1.00112.48 O ANISOU 300 O LEU A 43 18525 14399 9814 -4410 1824 337 O ATOM 301 CB LEU A 43 45.756 2.616 -24.477 1.00105.69 C ANISOU 301 CB LEU A 43 16563 14204 9389 -4914 1647 285 C ATOM 302 CG LEU A 43 46.989 1.860 -23.976 1.00110.66 C ANISOU 302 CG LEU A 43 16612 15279 10156 -5165 1634 244 C ATOM 303 CD1 LEU A 43 46.626 0.922 -22.850 1.00108.29 C ANISOU 303 CD1 LEU A 43 15917 15127 10100 -4997 1376 241 C ATOM 304 CD2 LEU A 43 47.696 1.114 -25.111 1.00113.49 C ANISOU 304 CD2 LEU A 43 16718 15871 10531 -5066 1697 223 C ATOM 305 N TYR A 44 44.167 5.545 -25.497 1.00109.54 N ANISOU 305 N TYR A 44 18703 13682 9235 -4781 1927 349 N ATOM 306 CA TYR A 44 43.006 6.158 -26.149 1.00109.25 C ANISOU 306 CA TYR A 44 19233 13265 9014 -4362 1885 363 C ATOM 307 C TYR A 44 43.255 7.674 -26.168 1.00114.17 C ANISOU 307 C TYR A 44 20582 13525 9274 -4664 2138 391 C ATOM 308 O TYR A 44 42.602 8.399 -25.418 1.00113.81 O ANISOU 308 O TYR A 44 20849 13248 9146 -4615 2098 388 O ATOM 309 CB TYR A 44 41.705 5.828 -25.384 1.00108.24 C ANISOU 309 CB TYR A 44 18962 13103 9063 -3968 1616 325 C ATOM 310 CG TYR A 44 41.435 4.352 -25.195 1.00107.87 C ANISOU 310 CG TYR A 44 18249 13380 9355 -3741 1388 286 C ATOM 311 CD1 TYR A 44 42.013 3.646 -24.143 1.00108.48 C ANISOU 311 CD1 TYR A 44 17811 13743 9664 -4001 1328 282 C ATOM 312 CD2 TYR A 44 40.535 3.677 -26.014 1.00107.93 C ANISOU 312 CD2 TYR A 44 18184 13395 9431 -3258 1226 244 C ATOM 313 CE1 TYR A 44 41.767 2.287 -23.961 1.00107.01 C ANISOU 313 CE1 TYR A 44 17098 13808 9752 -3794 1133 251 C ATOM 314 CE2 TYR A 44 40.249 2.325 -25.815 1.00106.65 C ANISOU 314 CE2 TYR A 44 17468 13498 9557 -3084 1036 199 C ATOM 315 CZ TYR A 44 40.860 1.636 -24.779 1.00111.75 C ANISOU 315 CZ TYR A 44 17658 14386 10414 -3352 997 209 C ATOM 316 OH TYR A 44 40.591 0.306 -24.565 1.00108.42 O ANISOU 316 OH TYR A 44 16774 14180 10241 -3186 825 169 O ATOM 317 N PRO A 45 44.228 8.184 -26.960 1.00112.60 N ANISOU 317 N PRO A 45 20675 13269 8838 -5013 2420 410 N ATOM 318 CA PRO A 45 44.514 9.629 -26.907 1.00115.65 C ANISOU 318 CA PRO A 45 21803 13286 8853 -5372 2692 429 C ATOM 319 C PRO A 45 43.481 10.538 -27.572 1.00119.84 C ANISOU 319 C PRO A 45 23164 13307 9062 -4952 2695 467 C ATOM 320 O PRO A 45 43.347 11.698 -27.174 1.00122.56 O ANISOU 320 O PRO A 45 24136 13297 9134 -5116 2832 481 O ATOM 321 CB PRO A 45 45.889 9.741 -27.571 1.00120.15 C ANISOU 321 CB PRO A 45 22359 14009 9284 -5898 3001 411 C ATOM 322 CG PRO A 45 45.945 8.595 -28.514 1.00123.17 C ANISOU 322 CG PRO A 45 22299 14653 9846 -5581 2894 409 C ATOM 323 CD PRO A 45 45.120 7.490 -27.916 1.00114.70 C ANISOU 323 CD PRO A 45 20637 13798 9145 -5125 2527 401 C ATOM 324 N CYS A 46 42.743 10.003 -28.555 1.00113.12 N ANISOU 324 N CYS A 46 22324 12425 8231 -4392 2533 473 N ATOM 325 CA CYS A 46 41.765 10.705 -29.381 1.00113.85 C ANISOU 325 CA CYS A 46 23153 12094 8010 -3890 2495 492 C ATOM 326 C CYS A 46 40.447 11.034 -28.680 1.00112.63 C ANISOU 326 C CYS A 46 23150 11773 7870 -3420 2251 454 C ATOM 327 O CYS A 46 39.928 10.211 -27.927 1.00108.44 O ANISOU 327 O CYS A 46 21985 11532 7684 -3246 2009 401 O ATOM 328 CB CYS A 46 41.533 9.920 -30.665 1.00114.04 C ANISOU 328 CB CYS A 46 23047 12218 8065 -3486 2396 489 C ATOM 329 SG CYS A 46 43.046 9.616 -31.614 1.00119.91 S ANISOU 329 SG CYS A 46 23680 13138 8744 -3997 2711 519 S ATOM 330 N LYS A 47 39.884 12.232 -28.984 1.00110.31 N ANISOU 330 N LYS A 47 23733 11005 7175 -3188 2321 473 N ATOM 331 CA LYS A 47 38.615 12.754 -28.438 1.00109.42 C ANISOU 331 CA LYS A 47 23898 10690 6985 -2687 2115 420 C ATOM 332 C LYS A 47 37.382 11.863 -28.750 1.00109.96 C ANISOU 332 C LYS A 47 23517 10992 7272 -1983 1755 324 C ATOM 333 O LYS A 47 36.368 11.952 -28.046 1.00106.85 O ANISOU 333 O LYS A 47 23029 10617 6953 -1632 1554 239 O ATOM 334 CB LYS A 47 38.380 14.216 -28.875 1.00115.43 C ANISOU 334 CB LYS A 47 25772 10875 7212 -2549 2281 461 C ATOM 335 N LYS A 48 37.487 10.994 -29.796 1.00106.90 N ANISOU 335 N LYS A 48 22835 10801 6981 -1807 1687 320 N ATOM 336 CA LYS A 48 36.454 10.031 -30.210 1.00104.79 C ANISOU 336 CA LYS A 48 22096 10796 6922 -1224 1369 212 C ATOM 337 C LYS A 48 36.219 8.974 -29.116 1.00107.52 C ANISOU 337 C LYS A 48 21568 11555 7731 -1330 1196 139 C ATOM 338 O LYS A 48 35.226 8.248 -29.171 1.00107.01 O ANISOU 338 O LYS A 48 21110 11705 7843 -893 937 18 O ATOM 339 CB LYS A 48 36.801 9.365 -31.559 1.00106.08 C ANISOU 339 CB LYS A 48 22181 11056 7066 -1108 1377 234 C ATOM 340 CG LYS A 48 38.141 8.642 -31.599 1.00110.51 C ANISOU 340 CG LYS A 48 22301 11857 7830 -1693 1571 310 C ATOM 341 CD LYS A 48 38.395 8.012 -32.951 1.00121.28 C ANISOU 341 CD LYS A 48 23610 13310 9163 -1526 1573 320 C ATOM 342 CE LYS A 48 39.808 7.495 -33.074 1.00132.70 C ANISOU 342 CE LYS A 48 24725 14963 10734 -2097 1807 386 C ATOM 343 NZ LYS A 48 40.197 7.265 -34.491 1.00141.52 N ANISOU 343 NZ LYS A 48 26048 16041 11684 -2000 1908 414 N ATOM 344 N PHE A 49 37.132 8.910 -28.122 1.00102.59 N ANISOU 344 N PHE A 49 20667 11039 7275 -1918 1344 201 N ATOM 345 CA PHE A 49 37.092 7.991 -26.994 1.00 98.85 C ANISOU 345 CA PHE A 49 19456 10910 7194 -2091 1218 155 C ATOM 346 C PHE A 49 37.000 8.743 -25.655 1.00101.20 C ANISOU 346 C PHE A 49 19895 11086 7470 -2323 1266 154 C ATOM 347 O PHE A 49 37.533 8.267 -24.646 1.00 98.87 O ANISOU 347 O PHE A 49 19143 11006 7417 -2710 1281 169 O ATOM 348 CB PHE A 49 38.333 7.083 -27.024 1.00 99.68 C ANISOU 348 CB PHE A 49 19044 11305 7524 -2542 1317 218 C ATOM 349 CG PHE A 49 38.382 6.076 -28.150 1.00101.15 C ANISOU 349 CG PHE A 49 18942 11680 7811 -2313 1238 203 C ATOM 350 CD1 PHE A 49 37.584 4.932 -28.120 1.00102.42 C ANISOU 350 CD1 PHE A 49 18577 12096 8242 -1982 992 109 C ATOM 351 CD2 PHE A 49 39.277 6.229 -29.202 1.00105.39 C ANISOU 351 CD2 PHE A 49 19720 12150 8172 -2478 1431 274 C ATOM 352 CE1 PHE A 49 37.644 3.986 -29.152 1.00102.44 C ANISOU 352 CE1 PHE A 49 18334 12262 8327 -1788 924 91 C ATOM 353 CE2 PHE A 49 39.348 5.275 -30.224 1.00107.64 C ANISOU 353 CE2 PHE A 49 19736 12612 8549 -2271 1363 258 C ATOM 354 CZ PHE A 49 38.531 4.159 -30.191 1.00103.01 C ANISOU 354 CZ PHE A 49 18651 12261 8228 -1921 1103 170 C ATOM 355 N ASN A 50 36.319 9.912 -25.641 1.00 98.58 N ANISOU 355 N ASN A 50 20221 10405 6831 -2060 1284 133 N ATOM 356 CA ASN A 50 36.153 10.714 -24.424 1.00 98.07 C ANISOU 356 CA ASN A 50 20373 10184 6705 -2235 1334 125 C ATOM 357 C ASN A 50 35.225 10.027 -23.440 1.00 99.99 C ANISOU 357 C ASN A 50 20045 10694 7251 -2030 1110 9 C ATOM 358 O ASN A 50 35.453 10.150 -22.240 1.00 99.83 O ANISOU 358 O ASN A 50 19875 10715 7343 -2367 1154 18 O ATOM 359 CB ASN A 50 35.642 12.133 -24.718 1.00 99.40 C ANISOU 359 CB ASN A 50 21448 9885 6434 -1953 1410 127 C ATOM 360 CG ASN A 50 36.684 13.212 -24.999 1.00109.09 C ANISOU 360 CG ASN A 50 23395 10743 7310 -2409 1728 247 C ATOM 361 OD1 ASN A 50 37.899 12.975 -25.131 1.00 97.07 O ANISOU 361 OD1 ASN A 50 21710 9327 5846 -2969 1920 322 O ATOM 362 ND2 ASN A 50 36.206 14.439 -25.149 1.00100.04 N ANISOU 362 ND2 ASN A 50 23096 9152 5763 -2161 1795 250 N ATOM 363 N GLU A 51 34.194 9.298 -23.930 1.00 95.10 N ANISOU 363 N GLU A 51 19109 10268 6756 -1510 881 -114 N ATOM 364 CA GLU A 51 33.239 8.581 -23.069 1.00 92.63 C ANISOU 364 CA GLU A 51 18244 10231 6719 -1328 687 -256 C ATOM 365 C GLU A 51 33.853 7.344 -22.390 1.00 91.47 C ANISOU 365 C GLU A 51 17391 10415 6947 -1739 673 -228 C ATOM 366 O GLU A 51 33.488 7.049 -21.248 1.00 88.62 O ANISOU 366 O GLU A 51 16716 10186 6768 -1843 615 -290 O ATOM 367 CB GLU A 51 31.928 8.231 -23.802 1.00 94.72 C ANISOU 367 CB GLU A 51 18389 10628 6972 -680 461 -433 C ATOM 368 CG GLU A 51 30.721 8.195 -22.870 1.00106.29 C ANISOU 368 CG GLU A 51 19609 12240 8538 -420 316 -618 C ATOM 369 CD GLU A 51 29.403 7.729 -23.463 1.00124.80 C ANISOU 369 CD GLU A 51 21698 14819 10903 173 85 -846 C ATOM 370 OE1 GLU A 51 29.052 6.541 -23.271 1.00106.86 O ANISOU 370 OE1 GLU A 51 18784 12892 8928 126 -20 -957 O ATOM 371 OE2 GLU A 51 28.692 8.568 -24.065 1.00118.03 O ANISOU 371 OE2 GLU A 51 21295 13805 9748 686 7 -930 O ATOM 372 N ILE A 52 34.791 6.640 -23.065 1.00 87.06 N ANISOU 372 N ILE A 52 16617 9980 6483 -1959 729 -137 N ATOM 373 CA ILE A 52 35.450 5.482 -22.454 1.00 84.24 C ANISOU 373 CA ILE A 52 15649 9918 6441 -2305 709 -106 C ATOM 374 C ILE A 52 36.495 5.946 -21.402 1.00 88.74 C ANISOU 374 C ILE A 52 16266 10444 7007 -2852 865 -4 C ATOM 375 O ILE A 52 36.712 5.246 -20.412 1.00 86.26 O ANISOU 375 O ILE A 52 15520 10333 6921 -3082 814 -7 O ATOM 376 CB ILE A 52 35.999 4.460 -23.486 1.00 86.01 C ANISOU 376 CB ILE A 52 15575 10328 6777 -2284 688 -73 C ATOM 377 CG1 ILE A 52 36.115 3.048 -22.848 1.00 83.79 C ANISOU 377 CG1 ILE A 52 14643 10362 6830 -2417 580 -102 C ATOM 378 CG2 ILE A 52 37.305 4.929 -24.143 1.00 87.33 C ANISOU 378 CG2 ILE A 52 16010 10394 6778 -2600 895 60 C ATOM 379 CD1 ILE A 52 36.196 1.853 -23.823 1.00 89.99 C ANISOU 379 CD1 ILE A 52 15101 11342 7749 -2248 497 -124 C ATOM 380 N LYS A 53 37.103 7.140 -21.609 1.00 87.84 N ANISOU 380 N LYS A 53 16707 10059 6611 -3059 1055 75 N ATOM 381 CA LYS A 53 38.082 7.745 -20.700 1.00 87.82 C ANISOU 381 CA LYS A 53 16817 10000 6549 -3599 1220 147 C ATOM 382 C LYS A 53 37.370 8.321 -19.483 1.00 91.55 C ANISOU 382 C LYS A 53 17427 10352 7006 -3583 1179 96 C ATOM 383 O LYS A 53 37.855 8.121 -18.375 1.00 90.14 O ANISOU 383 O LYS A 53 16989 10302 6958 -3943 1190 112 O ATOM 384 CB LYS A 53 38.906 8.836 -21.401 1.00 92.72 C ANISOU 384 CB LYS A 53 18033 10354 6842 -3851 1464 224 C ATOM 385 CG LYS A 53 39.951 8.333 -22.398 1.00 99.05 C ANISOU 385 CG LYS A 53 18671 11312 7652 -4044 1571 277 C ATOM 386 CD LYS A 53 40.793 9.483 -22.988 1.00106.23 C ANISOU 386 CD LYS A 53 20204 11949 8210 -4389 1860 335 C ATOM 387 CE LYS A 53 40.147 10.262 -24.118 1.00105.73 C ANISOU 387 CE LYS A 53 20842 11509 7822 -4005 1913 347 C ATOM 388 NZ LYS A 53 41.109 11.196 -24.771 1.00110.50 N ANISOU 388 NZ LYS A 53 22030 11869 8085 -4408 2227 405 N ATOM 389 N ILE A 54 36.217 9.019 -19.684 1.00 90.05 N ANISOU 389 N ILE A 54 17639 9933 6644 -3139 1121 24 N ATOM 390 CA ILE A 54 35.376 9.610 -18.624 1.00 90.98 C ANISOU 390 CA ILE A 54 17916 9931 6721 -3028 1078 -51 C ATOM 391 C ILE A 54 34.864 8.508 -17.671 1.00 95.20 C ANISOU 391 C ILE A 54 17794 10785 7594 -3017 918 -134 C ATOM 392 O ILE A 54 34.758 8.737 -16.457 1.00 95.07 O ANISOU 392 O ILE A 54 17744 10756 7620 -3214 932 -153 O ATOM 393 CB ILE A 54 34.253 10.520 -19.224 1.00 96.19 C ANISOU 393 CB ILE A 54 19127 10318 7102 -2466 1032 -132 C ATOM 394 CG1 ILE A 54 34.787 11.933 -19.570 1.00100.04 C ANISOU 394 CG1 ILE A 54 20448 10373 7187 -2606 1243 -40 C ATOM 395 CG2 ILE A 54 32.968 10.593 -18.381 1.00 96.46 C ANISOU 395 CG2 ILE A 54 19049 10405 7197 -2121 892 -285 C ATOM 396 CD1 ILE A 54 35.177 12.847 -18.400 1.00106.39 C ANISOU 396 CD1 ILE A 54 21593 10967 7865 -3010 1394 -3 C ATOM 397 N PHE A 55 34.607 7.302 -18.221 1.00 90.86 N ANISOU 397 N PHE A 55 16757 10502 7264 -2822 783 -182 N ATOM 398 CA PHE A 55 34.207 6.133 -17.450 1.00 88.70 C ANISOU 398 CA PHE A 55 15896 10515 7291 -2848 656 -257 C ATOM 399 C PHE A 55 35.398 5.728 -16.568 1.00 91.30 C ANISOU 399 C PHE A 55 15981 10958 7751 -3375 721 -146 C ATOM 400 O PHE A 55 35.217 5.537 -15.365 1.00 90.59 O ANISOU 400 O PHE A 55 15715 10934 7772 -3537 692 -176 O ATOM 401 CB PHE A 55 33.783 4.987 -18.393 1.00 89.94 C ANISOU 401 CB PHE A 55 15676 10891 7606 -2557 525 -327 C ATOM 402 CG PHE A 55 33.853 3.601 -17.792 1.00 89.85 C ANISOU 402 CG PHE A 55 15096 11155 7888 -2717 441 -353 C ATOM 403 CD1 PHE A 55 32.780 3.079 -17.076 1.00 92.31 C ANISOU 403 CD1 PHE A 55 15144 11594 8336 -2586 348 -505 C ATOM 404 CD2 PHE A 55 35.001 2.821 -17.930 1.00 91.31 C ANISOU 404 CD2 PHE A 55 15033 11470 8190 -2997 466 -237 C ATOM 405 CE1 PHE A 55 32.854 1.806 -16.502 1.00 91.30 C ANISOU 405 CE1 PHE A 55 14578 11672 8441 -2757 293 -526 C ATOM 406 CE2 PHE A 55 35.080 1.555 -17.343 1.00 92.49 C ANISOU 406 CE2 PHE A 55 14738 11832 8571 -3113 387 -256 C ATOM 407 CZ PHE A 55 34.002 1.053 -16.640 1.00 89.73 C ANISOU 407 CZ PHE A 55 14194 11560 8338 -3002 306 -393 C ATOM 408 N MET A 56 36.613 5.641 -17.159 1.00 87.78 N ANISOU 408 N MET A 56 15535 10547 7271 -3632 811 -33 N ATOM 409 CA MET A 56 37.835 5.267 -16.447 1.00 87.44 C ANISOU 409 CA MET A 56 15233 10666 7324 -4097 858 49 C ATOM 410 C MET A 56 38.222 6.240 -15.342 1.00 89.89 C ANISOU 410 C MET A 56 15806 10841 7509 -4455 961 77 C ATOM 411 O MET A 56 38.794 5.810 -14.339 1.00 89.40 O ANISOU 411 O MET A 56 15460 10943 7563 -4755 931 97 O ATOM 412 CB MET A 56 38.998 5.028 -17.404 1.00 91.32 C ANISOU 412 CB MET A 56 15649 11264 7785 -4263 942 126 C ATOM 413 CG MET A 56 39.071 3.593 -17.852 1.00 94.84 C ANISOU 413 CG MET A 56 15600 11977 8458 -4101 814 115 C ATOM 414 SD MET A 56 39.498 2.425 -16.527 1.00 99.23 S ANISOU 414 SD MET A 56 15635 12809 9260 -4317 692 119 S ATOM 415 CE MET A 56 38.703 0.918 -17.156 1.00 94.19 C ANISOU 415 CE MET A 56 14639 12317 8833 -3921 529 55 C ATOM 416 N VAL A 57 37.876 7.531 -15.507 1.00 85.31 N ANISOU 416 N VAL A 57 15791 9950 6672 -4401 1072 71 N ATOM 417 CA VAL A 57 38.093 8.586 -14.520 1.00 85.30 C ANISOU 417 CA VAL A 57 16143 9759 6510 -4708 1182 84 C ATOM 418 C VAL A 57 37.104 8.340 -13.355 1.00 87.21 C ANISOU 418 C VAL A 57 16223 10032 6881 -4564 1063 4 C ATOM 419 O VAL A 57 37.526 8.315 -12.190 1.00 85.11 O ANISOU 419 O VAL A 57 15834 9834 6669 -4899 1069 19 O ATOM 420 CB VAL A 57 37.927 9.990 -15.165 1.00 91.29 C ANISOU 420 CB VAL A 57 17630 10133 6923 -4631 1340 99 C ATOM 421 CG1 VAL A 57 37.668 11.074 -14.123 1.00 92.36 C ANISOU 421 CG1 VAL A 57 18195 10015 6883 -4782 1420 80 C ATOM 422 CG2 VAL A 57 39.135 10.345 -16.016 1.00 92.91 C ANISOU 422 CG2 VAL A 57 18030 10302 6969 -4967 1519 177 C ATOM 423 N ASN A 58 35.801 8.105 -13.692 1.00 83.08 N ANISOU 423 N ASN A 58 15669 9492 6405 -4069 954 -97 N ATOM 424 CA ASN A 58 34.714 7.862 -12.730 1.00 81.63 C ANISOU 424 CA ASN A 58 15322 9362 6333 -3893 861 -212 C ATOM 425 C ASN A 58 34.942 6.588 -11.878 1.00 83.00 C ANISOU 425 C ASN A 58 14935 9818 6781 -4104 769 -213 C ATOM 426 O ASN A 58 34.487 6.518 -10.724 1.00 81.10 O ANISOU 426 O ASN A 58 14616 9597 6601 -4186 749 -269 O ATOM 427 CB ASN A 58 33.343 7.870 -13.428 1.00 80.22 C ANISOU 427 CB ASN A 58 15186 9168 6126 -3325 769 -354 C ATOM 428 CG ASN A 58 32.891 9.231 -13.936 1.00105.59 C ANISOU 428 CG ASN A 58 19027 12066 9024 -3043 838 -377 C ATOM 429 OD1 ASN A 58 33.542 10.262 -13.743 1.00105.80 O ANISOU 429 OD1 ASN A 58 19533 11832 8833 -3292 979 -285 O ATOM 430 ND2 ASN A 58 31.757 9.271 -14.614 1.00 98.03 N ANISOU 430 ND2 ASN A 58 18109 11126 8013 -2505 736 -513 N ATOM 431 N LEU A 59 35.700 5.617 -12.434 1.00 78.77 N ANISOU 431 N LEU A 59 14061 9481 6386 -4194 724 -149 N ATOM 432 CA LEU A 59 36.081 4.384 -11.754 1.00 76.77 C ANISOU 432 CA LEU A 59 13349 9468 6351 -4371 636 -132 C ATOM 433 C LEU A 59 37.182 4.725 -10.771 1.00 80.82 C ANISOU 433 C LEU A 59 13895 9996 6815 -4820 688 -44 C ATOM 434 O LEU A 59 37.079 4.346 -9.610 1.00 79.78 O ANISOU 434 O LEU A 59 13616 9930 6765 -4961 638 -61 O ATOM 435 CB LEU A 59 36.556 3.335 -12.766 1.00 76.08 C ANISOU 435 CB LEU A 59 12954 9566 6387 -4272 574 -96 C ATOM 436 CG LEU A 59 36.581 1.889 -12.293 1.00 79.29 C ANISOU 436 CG LEU A 59 12930 10189 7008 -4297 461 -109 C ATOM 437 CD1 LEU A 59 35.162 1.319 -12.143 1.00 78.41 C ANISOU 437 CD1 LEU A 59 12695 10097 7001 -4026 395 -254 C ATOM 438 CD2 LEU A 59 37.357 1.041 -13.261 1.00 81.85 C ANISOU 438 CD2 LEU A 59 13024 10671 7406 -4253 424 -50 C ATOM 439 N THR A 60 38.187 5.515 -11.204 1.00 79.35 N ANISOU 439 N THR A 60 13936 9744 6470 -5059 800 32 N ATOM 440 CA THR A 60 39.283 5.968 -10.335 1.00 80.51 C ANISOU 440 CA THR A 60 14120 9932 6536 -5522 860 85 C ATOM 441 C THR A 60 38.770 6.847 -9.178 1.00 85.08 C ANISOU 441 C THR A 60 15005 10315 7008 -5643 905 49 C ATOM 442 O THR A 60 39.219 6.679 -8.043 1.00 84.68 O ANISOU 442 O THR A 60 14819 10363 6991 -5920 867 58 O ATOM 443 CB THR A 60 40.373 6.655 -11.142 1.00 88.13 C ANISOU 443 CB THR A 60 15272 10878 7334 -5774 1003 137 C ATOM 444 OG1 THR A 60 40.632 5.876 -12.310 1.00 86.44 O ANISOU 444 OG1 THR A 60 14817 10816 7211 -5585 970 157 O ATOM 445 CG2 THR A 60 41.655 6.826 -10.340 1.00 87.15 C ANISOU 445 CG2 THR A 60 15023 10927 7163 -6273 1040 158 C ATOM 446 N MET A 61 37.809 7.753 -9.471 1.00 81.87 N ANISOU 446 N MET A 61 15015 9634 6458 -5399 975 1 N ATOM 447 CA MET A 61 37.162 8.630 -8.498 1.00 81.92 C ANISOU 447 CA MET A 61 15356 9428 6344 -5425 1024 -49 C ATOM 448 C MET A 61 36.522 7.809 -7.385 1.00 85.00 C ANISOU 448 C MET A 61 15422 9957 6918 -5378 913 -109 C ATOM 449 O MET A 61 36.731 8.122 -6.212 1.00 84.67 O ANISOU 449 O MET A 61 15460 9880 6832 -5650 934 -106 O ATOM 450 CB MET A 61 36.108 9.506 -9.168 1.00 85.10 C ANISOU 450 CB MET A 61 16196 9560 6577 -5025 1078 -112 C ATOM 451 CG MET A 61 36.683 10.674 -9.873 1.00 91.28 C ANISOU 451 CG MET A 61 17518 10082 7083 -5148 1234 -53 C ATOM 452 SD MET A 61 35.395 11.905 -10.064 1.00 97.88 S ANISOU 452 SD MET A 61 18988 10545 7658 -4693 1285 -139 S ATOM 453 CE MET A 61 36.201 13.059 -11.164 1.00 97.34 C ANISOU 453 CE MET A 61 19584 10154 7248 -4836 1478 -48 C ATOM 454 N ALA A 62 35.783 6.732 -7.758 1.00 80.65 N ANISOU 454 N ALA A 62 14521 9565 6559 -5064 805 -169 N ATOM 455 CA ALA A 62 35.125 5.811 -6.828 1.00 78.96 C ANISOU 455 CA ALA A 62 14005 9484 6513 -5028 722 -240 C ATOM 456 C ALA A 62 36.154 5.149 -5.908 1.00 82.77 C ANISOU 456 C ALA A 62 14261 10120 7070 -5398 668 -156 C ATOM 457 O ALA A 62 36.030 5.263 -4.693 1.00 80.75 O ANISOU 457 O ALA A 62 14057 9830 6794 -5575 672 -174 O ATOM 458 CB ALA A 62 34.347 4.759 -7.596 1.00 78.10 C ANISOU 458 CB ALA A 62 13582 9525 6569 -4692 638 -321 C ATOM 459 N ASP A 63 37.213 4.540 -6.489 1.00 81.63 N ANISOU 459 N ASP A 63 13888 10144 6984 -5502 618 -70 N ATOM 460 CA ASP A 63 38.318 3.905 -5.756 1.00 82.47 C ANISOU 460 CA ASP A 63 13759 10439 7135 -5794 540 0 C ATOM 461 C ASP A 63 38.944 4.898 -4.774 1.00 89.01 C ANISOU 461 C ASP A 63 14823 11193 7803 -6161 600 22 C ATOM 462 O ASP A 63 39.217 4.532 -3.625 1.00 89.19 O ANISOU 462 O ASP A 63 14749 11297 7840 -6344 529 29 O ATOM 463 CB ASP A 63 39.390 3.384 -6.740 1.00 84.90 C ANISOU 463 CB ASP A 63 13831 10944 7483 -5813 504 65 C ATOM 464 CG ASP A 63 38.876 2.461 -7.840 1.00 97.43 C ANISOU 464 CG ASP A 63 15221 12593 9206 -5465 454 46 C ATOM 465 OD1 ASP A 63 37.714 2.001 -7.741 1.00 96.91 O ANISOU 465 OD1 ASP A 63 15129 12466 9226 -5229 427 -29 O ATOM 466 OD2 ASP A 63 39.630 2.213 -8.810 1.00105.26 O ANISOU 466 OD2 ASP A 63 16080 13707 10207 -5443 453 90 O ATOM 467 N MET A 64 39.113 6.168 -5.225 1.00 86.51 N ANISOU 467 N MET A 64 14861 10698 7310 -6262 735 27 N ATOM 468 CA MET A 64 39.662 7.266 -4.435 1.00 88.17 C ANISOU 468 CA MET A 64 15372 10795 7332 -6633 825 33 C ATOM 469 C MET A 64 38.800 7.670 -3.254 1.00 87.18 C ANISOU 469 C MET A 64 15462 10498 7163 -6631 838 -19 C ATOM 470 O MET A 64 39.355 8.015 -2.222 1.00 87.25 O ANISOU 470 O MET A 64 15540 10522 7088 -6961 837 -12 O ATOM 471 CB MET A 64 39.975 8.470 -5.312 1.00 93.59 C ANISOU 471 CB MET A 64 16455 11288 7816 -6730 991 46 C ATOM 472 CG MET A 64 41.310 8.346 -5.980 1.00 99.93 C ANISOU 472 CG MET A 64 17075 12301 8592 -6996 1019 86 C ATOM 473 SD MET A 64 42.677 8.597 -4.825 1.00107.77 S ANISOU 473 SD MET A 64 17943 13512 9492 -7574 1008 74 S ATOM 474 CE MET A 64 43.957 7.737 -5.708 1.00104.90 C ANISOU 474 CE MET A 64 17085 13554 9219 -7659 954 87 C ATOM 475 N LEU A 65 37.456 7.610 -3.399 1.00 80.11 N ANISOU 475 N LEU A 65 14648 9471 6321 -6263 848 -89 N ATOM 476 CA LEU A 65 36.454 7.889 -2.358 1.00 78.31 C ANISOU 476 CA LEU A 65 14578 9108 6066 -6195 872 -169 C ATOM 477 C LEU A 65 36.618 6.895 -1.190 1.00 80.62 C ANISOU 477 C LEU A 65 14582 9572 6479 -6359 769 -163 C ATOM 478 O LEU A 65 36.317 7.232 -0.036 1.00 79.15 O ANISOU 478 O LEU A 65 14554 9295 6226 -6496 797 -199 O ATOM 479 CB LEU A 65 35.033 7.849 -2.961 1.00 77.07 C ANISOU 479 CB LEU A 65 14448 8876 5958 -5731 888 -278 C ATOM 480 CG LEU A 65 33.806 7.934 -2.051 1.00 80.97 C ANISOU 480 CG LEU A 65 15000 9307 6459 -5581 916 -407 C ATOM 481 CD1 LEU A 65 33.779 9.213 -1.248 1.00 83.48 C ANISOU 481 CD1 LEU A 65 15770 9386 6564 -5734 1022 -419 C ATOM 482 CD2 LEU A 65 32.544 7.872 -2.858 1.00 82.48 C ANISOU 482 CD2 LEU A 65 15141 9507 6691 -5113 917 -542 C ATOM 483 N PHE A 66 37.150 5.690 -1.494 1.00 76.95 N ANISOU 483 N PHE A 66 13736 9338 6165 -6343 652 -115 N ATOM 484 CA PHE A 66 37.445 4.686 -0.480 1.00 76.38 C ANISOU 484 CA PHE A 66 13440 9412 6170 -6474 541 -94 C ATOM 485 C PHE A 66 38.811 4.933 0.127 1.00 79.78 C ANISOU 485 C PHE A 66 13859 9957 6497 -6835 484 -23 C ATOM 486 O PHE A 66 38.925 4.923 1.348 1.00 80.26 O ANISOU 486 O PHE A 66 13983 10012 6498 -7024 446 -27 O ATOM 487 CB PHE A 66 37.334 3.241 -1.010 1.00 77.16 C ANISOU 487 CB PHE A 66 13191 9679 6446 -6260 439 -86 C ATOM 488 CG PHE A 66 37.736 2.213 0.031 1.00 79.10 C ANISOU 488 CG PHE A 66 13289 10042 6725 -6382 322 -53 C ATOM 489 CD1 PHE A 66 36.988 2.043 1.194 1.00 81.80 C ANISOU 489 CD1 PHE A 66 13750 10284 7046 -6437 348 -108 C ATOM 490 CD2 PHE A 66 38.880 1.442 -0.133 1.00 81.80 C ANISOU 490 CD2 PHE A 66 13398 10591 7090 -6428 189 26 C ATOM 491 CE1 PHE A 66 37.370 1.108 2.155 1.00 82.65 C ANISOU 491 CE1 PHE A 66 13793 10464 7145 -6538 243 -70 C ATOM 492 CE2 PHE A 66 39.261 0.509 0.843 1.00 84.41 C ANISOU 492 CE2 PHE A 66 13650 11011 7411 -6490 63 57 C ATOM 493 CZ PHE A 66 38.509 0.355 1.979 1.00 81.88 C ANISOU 493 CZ PHE A 66 13498 10556 7057 -6549 91 16 C ATOM 494 N LEU A 67 39.844 5.151 -0.715 1.00 75.86 N ANISOU 494 N LEU A 67 13272 9584 5967 -6939 482 24 N ATOM 495 CA LEU A 67 41.219 5.410 -0.277 1.00 76.89 C ANISOU 495 CA LEU A 67 13326 9897 5990 -7298 432 53 C ATOM 496 C LEU A 67 41.326 6.568 0.734 1.00 82.75 C ANISOU 496 C LEU A 67 14406 10490 6547 -7627 512 23 C ATOM 497 O LEU A 67 42.125 6.463 1.663 1.00 84.42 O ANISOU 497 O LEU A 67 14522 10862 6690 -7889 417 22 O ATOM 498 CB LEU A 67 42.169 5.610 -1.466 1.00 77.54 C ANISOU 498 CB LEU A 67 13281 10130 6051 -7371 471 74 C ATOM 499 CG LEU A 67 42.395 4.391 -2.380 1.00 79.81 C ANISOU 499 CG LEU A 67 13190 10630 6502 -7099 369 105 C ATOM 500 CD1 LEU A 67 42.698 4.827 -3.796 1.00 79.68 C ANISOU 500 CD1 LEU A 67 13199 10610 6464 -7059 483 113 C ATOM 501 CD2 LEU A 67 43.507 3.480 -1.847 1.00 81.35 C ANISOU 501 CD2 LEU A 67 13023 11166 6721 -7194 191 117 C ATOM 502 N ILE A 68 40.463 7.615 0.623 1.00 78.85 N ANISOU 502 N ILE A 68 14313 9687 5960 -7579 670 -10 N ATOM 503 CA ILE A 68 40.430 8.728 1.596 1.00 79.87 C ANISOU 503 CA ILE A 68 14825 9624 5899 -7860 760 -43 C ATOM 504 C ILE A 68 39.820 8.316 2.953 1.00 81.76 C ANISOU 504 C ILE A 68 15073 9828 6165 -7844 691 -69 C ATOM 505 O ILE A 68 39.936 9.088 3.896 1.00 83.05 O ANISOU 505 O ILE A 68 15508 9876 6174 -8104 739 -95 O ATOM 506 CB ILE A 68 39.803 10.064 1.101 1.00 83.91 C ANISOU 506 CB ILE A 68 15837 9793 6250 -7809 954 -73 C ATOM 507 CG1 ILE A 68 38.484 9.829 0.295 1.00 82.30 C ANISOU 507 CG1 ILE A 68 15661 9455 6155 -7304 982 -102 C ATOM 508 CG2 ILE A 68 40.840 10.899 0.339 1.00 86.43 C ANISOU 508 CG2 ILE A 68 16324 10105 6410 -8106 1063 -54 C ATOM 509 CD1 ILE A 68 37.367 10.959 0.357 1.00 83.89 C ANISOU 509 CD1 ILE A 68 16360 9311 6204 -7105 1122 -171 C ATOM 510 N THR A 69 39.189 7.129 3.071 1.00 75.15 N ANISOU 510 N THR A 69 13975 9077 5501 -7573 597 -69 N ATOM 511 CA THR A 69 38.645 6.708 4.362 1.00 74.20 C ANISOU 511 CA THR A 69 13894 8915 5382 -7595 556 -98 C ATOM 512 C THR A 69 39.764 6.117 5.207 1.00 77.41 C ANISOU 512 C THR A 69 14119 9545 5748 -7838 390 -52 C ATOM 513 O THR A 69 39.737 6.248 6.436 1.00 77.28 O ANISOU 513 O THR A 69 14254 9478 5632 -8012 366 -68 O ATOM 514 CB THR A 69 37.403 5.788 4.254 1.00 87.68 C ANISOU 514 CB THR A 69 15476 10591 7249 -7259 566 -146 C ATOM 515 OG1 THR A 69 37.782 4.416 4.056 1.00 89.48 O ANISOU 515 OG1 THR A 69 15368 11022 7607 -7162 426 -99 O ATOM 516 CG2 THR A 69 36.398 6.247 3.199 1.00 87.97 C ANISOU 516 CG2 THR A 69 15596 10497 7333 -6957 686 -212 C ATOM 517 N LEU A 70 40.764 5.493 4.544 1.00 73.13 N ANISOU 517 N LEU A 70 13258 9262 5265 -7832 271 -5 N ATOM 518 CA LEU A 70 41.909 4.852 5.201 1.00 73.76 C ANISOU 518 CA LEU A 70 13111 9618 5298 -7985 80 21 C ATOM 519 C LEU A 70 42.647 5.764 6.225 1.00 80.15 C ANISOU 519 C LEU A 70 14089 10460 5904 -8383 64 -13 C ATOM 520 O LEU A 70 42.838 5.275 7.345 1.00 81.58 O ANISOU 520 O LEU A 70 14262 10711 6023 -8440 -70 -11 O ATOM 521 CB LEU A 70 42.882 4.235 4.190 1.00 73.83 C ANISOU 521 CB LEU A 70 12752 9919 5381 -7902 -21 50 C ATOM 522 CG LEU A 70 42.281 3.215 3.204 1.00 75.98 C ANISOU 522 CG LEU A 70 12842 10185 5841 -7521 -30 83 C ATOM 523 CD1 LEU A 70 43.198 3.014 2.029 1.00 77.16 C ANISOU 523 CD1 LEU A 70 12705 10576 6038 -7478 -64 98 C ATOM 524 CD2 LEU A 70 42.006 1.876 3.861 1.00 74.82 C ANISOU 524 CD2 LEU A 70 12600 10073 5754 -7324 -171 108 C ATOM 525 N PRO A 71 42.974 7.073 5.965 1.00 76.85 N ANISOU 525 N PRO A 71 13884 9958 5357 -8666 205 -51 N ATOM 526 CA PRO A 71 43.621 7.893 7.027 1.00 78.22 C ANISOU 526 CA PRO A 71 14238 10157 5326 -9074 194 -101 C ATOM 527 C PRO A 71 42.837 7.967 8.351 1.00 81.42 C ANISOU 527 C PRO A 71 14924 10350 5664 -9085 193 -110 C ATOM 528 O PRO A 71 43.458 7.983 9.412 1.00 82.71 O ANISOU 528 O PRO A 71 15090 10640 5697 -9318 73 -136 O ATOM 529 CB PRO A 71 43.796 9.279 6.382 1.00 81.04 C ANISOU 529 CB PRO A 71 14887 10351 5555 -9333 404 -139 C ATOM 530 CG PRO A 71 43.698 9.065 4.940 1.00 84.49 C ANISOU 530 CG PRO A 71 15185 10802 6116 -9104 472 -105 C ATOM 531 CD PRO A 71 42.833 7.849 4.711 1.00 77.84 C ANISOU 531 CD PRO A 71 14132 9955 5487 -8646 381 -54 C ATOM 532 N LEU A 72 41.481 7.958 8.292 1.00 75.69 N ANISOU 532 N LEU A 72 14406 9333 5019 -8823 320 -105 N ATOM 533 CA LEU A 72 40.608 7.965 9.468 1.00 74.67 C ANISOU 533 CA LEU A 72 14527 9007 4839 -8806 354 -131 C ATOM 534 C LEU A 72 40.873 6.723 10.294 1.00 80.28 C ANISOU 534 C LEU A 72 15033 9893 5577 -8748 159 -98 C ATOM 535 O LEU A 72 41.001 6.835 11.514 1.00 83.24 O ANISOU 535 O LEU A 72 15574 10242 5813 -8932 105 -115 O ATOM 536 CB LEU A 72 39.118 8.012 9.085 1.00 72.69 C ANISOU 536 CB LEU A 72 14423 8503 4692 -8490 518 -163 C ATOM 537 CG LEU A 72 38.641 9.165 8.207 1.00 77.12 C ANISOU 537 CG LEU A 72 15238 8852 5211 -8423 702 -198 C ATOM 538 CD1 LEU A 72 37.257 8.887 7.666 1.00 75.40 C ANISOU 538 CD1 LEU A 72 15015 8508 5126 -8023 800 -248 C ATOM 539 CD2 LEU A 72 38.636 10.471 8.965 1.00 81.31 C ANISOU 539 CD2 LEU A 72 16212 9160 5521 -8688 819 -242 C ATOM 540 N TRP A 73 40.999 5.550 9.642 1.00 74.84 N ANISOU 540 N TRP A 73 14023 9371 5041 -8492 50 -52 N ATOM 541 CA TRP A 73 41.296 4.302 10.346 1.00 75.04 C ANISOU 541 CA TRP A 73 13909 9540 5064 -8395 -141 -15 C ATOM 542 C TRP A 73 42.711 4.340 10.908 1.00 79.79 C ANISOU 542 C TRP A 73 14377 10426 5513 -8615 -348 -14 C ATOM 543 O TRP A 73 42.907 3.998 12.072 1.00 79.58 O ANISOU 543 O TRP A 73 14456 10423 5357 -8680 -474 -13 O ATOM 544 CB TRP A 73 41.096 3.073 9.444 1.00 72.69 C ANISOU 544 CB TRP A 73 13345 9330 4946 -8063 -196 28 C ATOM 545 CG TRP A 73 39.695 2.908 8.937 1.00 71.50 C ANISOU 545 CG TRP A 73 13277 8955 4936 -7849 -14 -3 C ATOM 546 CD1 TRP A 73 39.269 3.072 7.654 1.00 72.89 C ANISOU 546 CD1 TRP A 73 13335 9108 5252 -7672 88 -17 C ATOM 547 CD2 TRP A 73 38.526 2.634 9.718 1.00 70.95 C ANISOU 547 CD2 TRP A 73 13421 8676 4862 -7808 97 -50 C ATOM 548 NE1 TRP A 73 37.907 2.919 7.583 1.00 70.95 N ANISOU 548 NE1 TRP A 73 13187 8680 5091 -7507 236 -82 N ATOM 549 CE2 TRP A 73 37.424 2.625 8.830 1.00 73.21 C ANISOU 549 CE2 TRP A 73 13661 8860 5297 -7599 255 -110 C ATOM 550 CE3 TRP A 73 38.298 2.399 11.089 1.00 73.15 C ANISOU 550 CE3 TRP A 73 13928 8856 5011 -7936 83 -61 C ATOM 551 CZ2 TRP A 73 36.116 2.341 9.256 1.00 72.63 C ANISOU 551 CZ2 TRP A 73 13708 8631 5256 -7524 403 -200 C ATOM 552 CZ3 TRP A 73 36.999 2.142 11.519 1.00 74.38 C ANISOU 552 CZ3 TRP A 73 14246 8820 5195 -7879 250 -135 C ATOM 553 CH2 TRP A 73 35.925 2.115 10.611 1.00 73.99 C ANISOU 553 CH2 TRP A 73 14098 8711 5304 -7683 412 -214 C ATOM 554 N ILE A 74 43.686 4.804 10.106 1.00 77.03 N ANISOU 554 N ILE A 74 13806 10304 5159 -8743 -375 -34 N ATOM 555 CA ILE A 74 45.074 4.952 10.563 1.00 79.41 C ANISOU 555 CA ILE A 74 13919 10947 5308 -8986 -560 -80 C ATOM 556 C ILE A 74 45.118 5.738 11.894 1.00 85.21 C ANISOU 556 C ILE A 74 14956 11585 5836 -9305 -562 -130 C ATOM 557 O ILE A 74 45.678 5.240 12.868 1.00 85.96 O ANISOU 557 O ILE A 74 15000 11856 5805 -9330 -773 -143 O ATOM 558 CB ILE A 74 45.984 5.585 9.477 1.00 83.01 C ANISOU 558 CB ILE A 74 14134 11634 5771 -9167 -509 -129 C ATOM 559 CG1 ILE A 74 46.037 4.686 8.213 1.00 81.50 C ANISOU 559 CG1 ILE A 74 13623 11573 5770 -8832 -535 -80 C ATOM 560 CG2 ILE A 74 47.391 5.879 10.041 1.00 85.87 C ANISOU 560 CG2 ILE A 74 14283 12391 5951 -9487 -678 -226 C ATOM 561 CD1 ILE A 74 46.412 5.368 6.912 1.00 85.63 C ANISOU 561 CD1 ILE A 74 14036 12161 6337 -8949 -381 -108 C ATOM 562 N VAL A 75 44.481 6.924 11.936 1.00 81.87 N ANISOU 562 N VAL A 75 14877 10863 5366 -9508 -333 -158 N ATOM 563 CA VAL A 75 44.411 7.787 13.123 1.00 83.54 C ANISOU 563 CA VAL A 75 15433 10928 5378 -9817 -294 -210 C ATOM 564 C VAL A 75 43.597 7.086 14.235 1.00 88.32 C ANISOU 564 C VAL A 75 16236 11359 5964 -9646 -344 -174 C ATOM 565 O VAL A 75 44.045 7.067 15.388 1.00 89.77 O ANISOU 565 O VAL A 75 16516 11621 5973 -9814 -482 -200 O ATOM 566 CB VAL A 75 43.922 9.224 12.762 1.00 87.08 C ANISOU 566 CB VAL A 75 16243 11077 5767 -10033 -22 -250 C ATOM 567 CG1 VAL A 75 43.518 10.029 13.989 1.00 87.94 C ANISOU 567 CG1 VAL A 75 16782 10941 5691 -10262 55 -293 C ATOM 568 CG2 VAL A 75 44.986 9.975 11.966 1.00 88.86 C ANISOU 568 CG2 VAL A 75 16343 11498 5920 -10341 17 -306 C ATOM 569 N TYR A 76 42.456 6.448 13.872 1.00 82.65 N ANISOU 569 N TYR A 76 15559 10432 5411 -9322 -238 -126 N ATOM 570 CA TYR A 76 41.615 5.691 14.813 1.00 81.81 C ANISOU 570 CA TYR A 76 15637 10156 5291 -9175 -242 -105 C ATOM 571 C TYR A 76 42.407 4.605 15.553 1.00 85.80 C ANISOU 571 C TYR A 76 16018 10883 5699 -9113 -515 -67 C ATOM 572 O TYR A 76 42.275 4.490 16.757 1.00 86.29 O ANISOU 572 O TYR A 76 16326 10856 5603 -9200 -566 -73 O ATOM 573 CB TYR A 76 40.404 5.089 14.087 1.00 80.61 C ANISOU 573 CB TYR A 76 15454 9832 5342 -8862 -88 -90 C ATOM 574 CG TYR A 76 39.642 4.055 14.879 1.00 81.54 C ANISOU 574 CG TYR A 76 15699 9828 5455 -8721 -88 -78 C ATOM 575 CD1 TYR A 76 38.802 4.430 15.923 1.00 85.04 C ANISOU 575 CD1 TYR A 76 16481 10037 5794 -8836 53 -129 C ATOM 576 CD2 TYR A 76 39.721 2.702 14.557 1.00 80.59 C ANISOU 576 CD2 TYR A 76 15394 9807 5421 -8482 -204 -24 C ATOM 577 CE1 TYR A 76 38.081 3.480 16.648 1.00 86.26 C ANISOU 577 CE1 TYR A 76 16780 10071 5923 -8750 89 -132 C ATOM 578 CE2 TYR A 76 39.008 1.745 15.275 1.00 80.94 C ANISOU 578 CE2 TYR A 76 15618 9704 5430 -8393 -173 -20 C ATOM 579 CZ TYR A 76 38.193 2.141 16.323 1.00 88.43 C ANISOU 579 CZ TYR A 76 16898 10431 6270 -8544 -20 -77 C ATOM 580 OH TYR A 76 37.478 1.224 17.037 1.00 89.10 O ANISOU 580 OH TYR A 76 17189 10365 6302 -8501 46 -86 O ATOM 581 N TYR A 77 43.232 3.838 14.835 1.00 83.16 N ANISOU 581 N TYR A 77 15326 10833 5436 -8943 -692 -34 N ATOM 582 CA TYR A 77 44.087 2.790 15.382 1.00 84.78 C ANISOU 582 CA TYR A 77 15396 11284 5533 -8807 -980 -5 C ATOM 583 C TYR A 77 45.313 3.367 16.084 1.00 91.57 C ANISOU 583 C TYR A 77 16179 12434 6181 -9073 -1176 -74 C ATOM 584 O TYR A 77 45.726 2.819 17.105 1.00 93.08 O ANISOU 584 O TYR A 77 16457 12715 6192 -9027 -1388 -72 O ATOM 585 CB TYR A 77 44.497 1.791 14.289 1.00 85.78 C ANISOU 585 CB TYR A 77 15167 11618 5807 -8494 -1089 39 C ATOM 586 CG TYR A 77 43.441 0.743 14.004 1.00 86.40 C ANISOU 586 CG TYR A 77 15356 11454 6020 -8196 -993 102 C ATOM 587 CD1 TYR A 77 43.235 -0.322 14.876 1.00 89.37 C ANISOU 587 CD1 TYR A 77 15948 11728 6281 -8035 -1102 146 C ATOM 588 CD2 TYR A 77 42.674 0.792 12.842 1.00 85.18 C ANISOU 588 CD2 TYR A 77 15104 11176 6084 -8083 -794 107 C ATOM 589 CE1 TYR A 77 42.278 -1.302 14.614 1.00 88.68 C ANISOU 589 CE1 TYR A 77 15984 11416 6295 -7819 -989 185 C ATOM 590 CE2 TYR A 77 41.713 -0.184 12.566 1.00 84.86 C ANISOU 590 CE2 TYR A 77 15139 10946 6156 -7847 -703 136 C ATOM 591 CZ TYR A 77 41.510 -1.225 13.465 1.00 94.21 C ANISOU 591 CZ TYR A 77 16545 12025 7224 -7741 -787 171 C ATOM 592 OH TYR A 77 40.562 -2.199 13.243 1.00 94.78 O ANISOU 592 OH TYR A 77 16728 11901 7382 -7568 -671 181 O ATOM 593 N GLN A 78 45.883 4.483 15.556 1.00 89.50 N ANISOU 593 N GLN A 78 15780 12312 5916 -9366 -1100 -147 N ATOM 594 CA GLN A 78 47.059 5.165 16.121 1.00 92.30 C ANISOU 594 CA GLN A 78 16028 12976 6067 -9700 -1251 -252 C ATOM 595 C GLN A 78 46.793 5.618 17.539 1.00 98.93 C ANISOU 595 C GLN A 78 17250 13640 6699 -9912 -1266 -279 C ATOM 596 O GLN A 78 47.669 5.476 18.393 1.00101.90 O ANISOU 596 O GLN A 78 17554 14290 6875 -10003 -1513 -340 O ATOM 597 CB GLN A 78 47.491 6.352 15.262 1.00 94.15 C ANISOU 597 CB GLN A 78 16154 13291 6327 -10033 -1080 -330 C ATOM 598 CG GLN A 78 48.526 5.983 14.199 1.00113.21 C ANISOU 598 CG GLN A 78 18065 16131 8819 -9969 -1190 -373 C ATOM 599 CD GLN A 78 48.999 7.141 13.337 1.00126.37 C ANISOU 599 CD GLN A 78 19662 17872 10481 -10343 -995 -459 C ATOM 600 OE1 GLN A 78 48.556 8.293 13.457 1.00116.80 O ANISOU 600 OE1 GLN A 78 18814 16359 9203 -10643 -767 -480 O ATOM 601 NE2 GLN A 78 49.922 6.849 12.433 1.00120.97 N ANISOU 601 NE2 GLN A 78 18532 17584 9847 -10328 -1071 -517 N ATOM 602 N ASN A 79 45.570 6.113 17.808 1.00 94.15 N ANISOU 602 N ASN A 79 17046 12597 6129 -9960 -1013 -244 N ATOM 603 CA ASN A 79 45.193 6.528 19.148 1.00 95.40 C ANISOU 603 CA ASN A 79 17604 12548 6094 -10143 -992 -267 C ATOM 604 C ASN A 79 44.445 5.395 19.910 1.00100.05 C ANISOU 604 C ASN A 79 18400 12948 6666 -9852 -1045 -188 C ATOM 605 O ASN A 79 43.526 5.646 20.701 1.00101.10 O ANISOU 605 O ASN A 79 18918 12762 6735 -9916 -889 -185 O ATOM 606 CB ASN A 79 44.460 7.872 19.148 1.00 95.58 C ANISOU 606 CB ASN A 79 17969 12243 6104 -10408 -694 -309 C ATOM 607 CG ASN A 79 43.216 7.937 18.327 1.00114.40 C ANISOU 607 CG ASN A 79 20455 14315 8696 -10191 -427 -263 C ATOM 608 OD1 ASN A 79 42.327 7.095 18.441 1.00112.76 O ANISOU 608 OD1 ASN A 79 20307 13950 8587 -9914 -382 -210 O ATOM 609 ND2 ASN A 79 43.098 8.986 17.535 1.00102.75 N ANISOU 609 ND2 ASN A 79 19039 12736 7264 -10328 -236 -297 N ATOM 610 N GLN A 80 44.915 4.143 19.688 1.00 95.38 N ANISOU 610 N GLN A 80 17567 12567 6105 -9542 -1266 -135 N ATOM 611 CA GLN A 80 44.529 2.876 20.330 1.00 93.88 C ANISOU 611 CA GLN A 80 17559 12258 5852 -9253 -1370 -60 C ATOM 612 C GLN A 80 43.036 2.484 20.220 1.00 94.72 C ANISOU 612 C GLN A 80 17929 11960 6099 -9123 -1090 -10 C ATOM 613 O GLN A 80 42.487 1.868 21.133 1.00 94.40 O ANISOU 613 O GLN A 80 18218 11711 5937 -9064 -1075 20 O ATOM 614 CB GLN A 80 44.997 2.856 21.798 1.00 96.86 C ANISOU 614 CB GLN A 80 18200 12676 5926 -9366 -1571 -86 C ATOM 615 CG GLN A 80 46.354 2.172 21.985 1.00 98.69 C ANISOU 615 CG GLN A 80 18161 13339 5999 -9197 -1964 -106 C ATOM 616 CD GLN A 80 47.504 2.847 21.260 1.00123.35 C ANISOU 616 CD GLN A 80 20807 16901 9160 -9362 -2077 -207 C ATOM 617 OE1 GLN A 80 48.296 2.205 20.560 1.00118.82 O ANISOU 617 OE1 GLN A 80 19841 16667 8639 -9127 -2266 -216 O ATOM 618 NE2 GLN A 80 47.640 4.154 21.425 1.00124.88 N ANISOU 618 NE2 GLN A 80 21041 17100 9309 -9783 -1951 -298 N ATOM 619 N GLY A 81 42.445 2.707 19.056 1.00 88.90 N ANISOU 619 N GLY A 81 17021 11151 5605 -9055 -887 -9 N ATOM 620 CA GLY A 81 41.056 2.337 18.813 1.00 86.52 C ANISOU 620 CA GLY A 81 16878 10546 5449 -8925 -630 1 C ATOM 621 C GLY A 81 40.067 3.254 19.502 1.00 89.90 C ANISOU 621 C GLY A 81 17643 10691 5826 -9132 -378 -64 C ATOM 622 O GLY A 81 39.147 2.784 20.172 1.00 86.32 O ANISOU 622 O GLY A 81 17453 10014 5330 -9103 -246 -75 O ATOM 623 N ASN A 82 40.237 4.581 19.301 1.00 89.39 N ANISOU 623 N ASN A 82 17584 10627 5752 -9346 -292 -117 N ATOM 624 CA ASN A 82 39.373 5.620 19.856 1.00 90.17 C ANISOU 624 CA ASN A 82 18009 10463 5788 -9521 -54 -189 C ATOM 625 C ASN A 82 38.837 6.590 18.761 1.00 95.19 C ANISOU 625 C ASN A 82 18582 11009 6578 -9491 159 -236 C ATOM 626 O ASN A 82 39.581 7.440 18.285 1.00 97.09 O ANISOU 626 O ASN A 82 18758 11344 6789 -9645 125 -244 O ATOM 627 CB ASN A 82 40.096 6.346 20.999 1.00 91.92 C ANISOU 627 CB ASN A 82 18464 10708 5752 -9827 -163 -216 C ATOM 628 CG ASN A 82 39.271 7.364 21.747 1.00107.30 C ANISOU 628 CG ASN A 82 20803 12374 7593 -10009 66 -289 C ATOM 629 OD1 ASN A 82 38.043 7.240 21.907 1.00 89.58 O ANISOU 629 OD1 ASN A 82 18721 9905 5409 -9894 288 -326 O ATOM 630 ND2 ASN A 82 39.948 8.392 22.249 1.00102.93 N ANISOU 630 ND2 ASN A 82 20405 11843 6859 -10308 18 -329 N ATOM 631 N TRP A 83 37.555 6.452 18.355 1.00 90.57 N ANISOU 631 N TRP A 83 18025 10251 6136 -9293 379 -280 N ATOM 632 CA TRP A 83 36.924 7.310 17.344 1.00 89.70 C ANISOU 632 CA TRP A 83 17890 10047 6146 -9187 566 -335 C ATOM 633 C TRP A 83 36.535 8.676 17.940 1.00 92.73 C ANISOU 633 C TRP A 83 18647 10214 6373 -9362 731 -411 C ATOM 634 O TRP A 83 35.405 8.864 18.408 1.00 91.51 O ANISOU 634 O TRP A 83 18690 9879 6202 -9287 920 -497 O ATOM 635 CB TRP A 83 35.731 6.611 16.659 1.00 87.58 C ANISOU 635 CB TRP A 83 17468 9734 6075 -8884 711 -383 C ATOM 636 CG TRP A 83 35.290 7.304 15.401 1.00 88.57 C ANISOU 636 CG TRP A 83 17495 9830 6327 -8701 830 -426 C ATOM 637 CD1 TRP A 83 34.443 8.370 15.308 1.00 92.23 C ANISOU 637 CD1 TRP A 83 18176 10115 6753 -8635 1026 -524 C ATOM 638 CD2 TRP A 83 35.717 7.013 14.060 1.00 87.56 C ANISOU 638 CD2 TRP A 83 17065 9850 6354 -8538 751 -373 C ATOM 639 NE1 TRP A 83 34.328 8.774 13.998 1.00 91.28 N ANISOU 639 NE1 TRP A 83 17932 10010 6739 -8432 1063 -531 N ATOM 640 CE2 TRP A 83 35.089 7.950 13.207 1.00 91.70 C ANISOU 640 CE2 TRP A 83 17662 10262 6918 -8384 904 -438 C ATOM 641 CE3 TRP A 83 36.568 6.049 13.494 1.00 88.16 C ANISOU 641 CE3 TRP A 83 16833 10140 6523 -8484 564 -282 C ATOM 642 CZ2 TRP A 83 35.277 7.944 11.816 1.00 90.02 C ANISOU 642 CZ2 TRP A 83 17237 10134 6832 -8201 881 -409 C ATOM 643 CZ3 TRP A 83 36.739 6.033 12.113 1.00 88.67 C ANISOU 643 CZ3 TRP A 83 16659 10300 6730 -8309 554 -259 C ATOM 644 CH2 TRP A 83 36.091 6.966 11.291 1.00 89.07 C ANISOU 644 CH2 TRP A 83 16799 10227 6818 -8180 713 -319 C ATOM 645 N ILE A 84 37.486 9.628 17.907 1.00 90.01 N ANISOU 645 N ILE A 84 18400 9897 5902 -9606 669 -396 N ATOM 646 CA ILE A 84 37.325 10.978 18.461 1.00 91.47 C ANISOU 646 CA ILE A 84 18993 9863 5900 -9814 810 -461 C ATOM 647 C ILE A 84 36.448 11.858 17.567 1.00 94.41 C ANISOU 647 C ILE A 84 19509 10034 6328 -9611 1030 -521 C ATOM 648 O ILE A 84 35.687 12.687 18.076 1.00 95.07 O ANISOU 648 O ILE A 84 19946 9880 6296 -9603 1204 -602 O ATOM 649 CB ILE A 84 38.716 11.628 18.783 1.00 96.42 C ANISOU 649 CB ILE A 84 19688 10607 6341 -10204 666 -443 C ATOM 650 CG1 ILE A 84 39.459 10.840 19.886 1.00 97.43 C ANISOU 650 CG1 ILE A 84 19737 10923 6359 -10363 437 -413 C ATOM 651 CG2 ILE A 84 38.602 13.115 19.164 1.00 98.45 C ANISOU 651 CG2 ILE A 84 20409 10606 6393 -10443 834 -513 C ATOM 652 CD1 ILE A 84 40.947 10.653 19.627 1.00102.03 C ANISOU 652 CD1 ILE A 84 20023 11848 6898 -10553 191 -387 C ATOM 653 N LEU A 85 36.554 11.680 16.245 1.00 89.03 N ANISOU 653 N LEU A 85 18574 9448 5805 -9420 1015 -488 N ATOM 654 CA LEU A 85 35.813 12.484 15.273 1.00 88.64 C ANISOU 654 CA LEU A 85 18665 9225 5790 -9181 1190 -539 C ATOM 655 C LEU A 85 34.284 12.280 15.368 1.00 92.90 C ANISOU 655 C LEU A 85 19229 9655 6414 -8834 1347 -644 C ATOM 656 O LEU A 85 33.877 11.324 16.025 1.00 91.35 O ANISOU 656 O LEU A 85 18874 9547 6287 -8805 1323 -662 O ATOM 657 CB LEU A 85 36.364 12.234 13.859 1.00 87.27 C ANISOU 657 CB LEU A 85 18203 9201 5755 -9067 1119 -475 C ATOM 658 CG LEU A 85 37.810 12.707 13.646 1.00 92.68 C ANISOU 658 CG LEU A 85 18890 9995 6328 -9429 1022 -417 C ATOM 659 CD1 LEU A 85 38.412 12.084 12.419 1.00 91.58 C ANISOU 659 CD1 LEU A 85 18366 10080 6351 -9319 926 -354 C ATOM 660 CD2 LEU A 85 37.916 14.232 13.610 1.00 96.11 C ANISOU 660 CD2 LEU A 85 19816 10164 6538 -9632 1182 -460 C ATOM 661 N PRO A 86 33.415 13.178 14.810 1.00 91.16 N ANISOU 661 N PRO A 86 19229 9249 6158 -8576 1515 -731 N ATOM 662 CA PRO A 86 31.955 12.974 14.937 1.00 90.79 C ANISOU 662 CA PRO A 86 19142 9171 6182 -8238 1657 -873 C ATOM 663 C PRO A 86 31.489 11.557 14.641 1.00 93.26 C ANISOU 663 C PRO A 86 18991 9717 6725 -8069 1606 -891 C ATOM 664 O PRO A 86 32.093 10.855 13.831 1.00 91.49 O ANISOU 664 O PRO A 86 18468 9652 6641 -8045 1473 -798 O ATOM 665 CB PRO A 86 31.374 13.981 13.949 1.00 93.40 C ANISOU 665 CB PRO A 86 19676 9348 6463 -7914 1769 -942 C ATOM 666 CG PRO A 86 32.364 15.076 13.947 1.00 99.43 C ANISOU 666 CG PRO A 86 20839 9920 7020 -8195 1765 -859 C ATOM 667 CD PRO A 86 33.704 14.408 14.042 1.00 94.13 C ANISOU 667 CD PRO A 86 19921 9441 6404 -8566 1586 -722 C ATOM 668 N LYS A 87 30.452 11.118 15.347 1.00 90.18 N ANISOU 668 N LYS A 87 18560 9346 6359 -7985 1722 -1019 N ATOM 669 CA LYS A 87 29.954 9.755 15.229 1.00 88.21 C ANISOU 669 CA LYS A 87 17935 9290 6291 -7895 1711 -1060 C ATOM 670 C LYS A 87 29.483 9.423 13.824 1.00 91.60 C ANISOU 670 C LYS A 87 18044 9855 6903 -7555 1702 -1109 C ATOM 671 O LYS A 87 29.861 8.376 13.304 1.00 90.78 O ANISOU 671 O LYS A 87 17640 9905 6947 -7556 1591 -1036 O ATOM 672 CB LYS A 87 28.888 9.470 16.292 1.00 91.35 C ANISOU 672 CB LYS A 87 18395 9671 6642 -7921 1886 -1219 C ATOM 673 CG LYS A 87 29.477 9.419 17.706 1.00101.43 C ANISOU 673 CG LYS A 87 19946 10841 7750 -8285 1857 -1143 C ATOM 674 CD LYS A 87 28.416 9.460 18.792 1.00108.41 C ANISOU 674 CD LYS A 87 20990 11663 8540 -8324 2070 -1312 C ATOM 675 CE LYS A 87 29.021 9.781 20.139 1.00110.04 C ANISOU 675 CE LYS A 87 21563 11715 8532 -8657 2045 -1239 C ATOM 676 NZ LYS A 87 28.017 10.356 21.070 1.00116.06 N ANISOU 676 NZ LYS A 87 22572 12367 9161 -8659 2278 -1414 N ATOM 677 N PHE A 88 28.754 10.345 13.168 1.00 88.41 N ANISOU 677 N PHE A 88 17735 9387 6470 -7248 1799 -1223 N ATOM 678 CA PHE A 88 28.247 10.145 11.804 1.00 87.12 C ANISOU 678 CA PHE A 88 17298 9353 6451 -6883 1781 -1287 C ATOM 679 C PHE A 88 29.360 9.875 10.773 1.00 90.58 C ANISOU 679 C PHE A 88 17606 9837 6972 -6926 1612 -1102 C ATOM 680 O PHE A 88 29.087 9.263 9.744 1.00 91.35 O ANISOU 680 O PHE A 88 17400 10085 7224 -6696 1567 -1128 O ATOM 681 CB PHE A 88 27.341 11.307 11.385 1.00 90.57 C ANISOU 681 CB PHE A 88 17940 9691 6782 -6513 1896 -1442 C ATOM 682 CG PHE A 88 26.636 11.118 10.068 1.00 91.94 C ANISOU 682 CG PHE A 88 17835 10019 7077 -6085 1876 -1550 C ATOM 683 CD1 PHE A 88 25.556 10.246 9.956 1.00 95.39 C ANISOU 683 CD1 PHE A 88 17878 10709 7659 -5905 1936 -1749 C ATOM 684 CD2 PHE A 88 27.063 11.795 8.929 1.00 93.72 C ANISOU 684 CD2 PHE A 88 18206 10147 7258 -5883 1802 -1465 C ATOM 685 CE1 PHE A 88 24.920 10.051 8.721 1.00 96.23 C ANISOU 685 CE1 PHE A 88 17706 10990 7869 -5511 1898 -1866 C ATOM 686 CE2 PHE A 88 26.414 11.618 7.703 1.00 96.11 C ANISOU 686 CE2 PHE A 88 18270 10593 7653 -5465 1767 -1567 C ATOM 687 CZ PHE A 88 25.352 10.743 7.604 1.00 94.27 C ANISOU 687 CZ PHE A 88 17614 10635 7571 -5274 1803 -1769 C ATOM 688 N LEU A 89 30.610 10.277 11.064 1.00 85.46 N ANISOU 688 N LEU A 89 17160 9091 6219 -7236 1521 -935 N ATOM 689 CA LEU A 89 31.767 10.000 10.216 1.00 83.23 C ANISOU 689 CA LEU A 89 16731 8891 6000 -7331 1371 -776 C ATOM 690 C LEU A 89 32.144 8.533 10.288 1.00 87.13 C ANISOU 690 C LEU A 89 16856 9595 6653 -7416 1247 -711 C ATOM 691 O LEU A 89 32.616 7.999 9.294 1.00 85.60 O ANISOU 691 O LEU A 89 16415 9530 6579 -7326 1147 -639 O ATOM 692 CB LEU A 89 32.954 10.845 10.636 1.00 83.93 C ANISOU 692 CB LEU A 89 17118 8862 5911 -7676 1328 -664 C ATOM 693 CG LEU A 89 33.506 11.801 9.607 1.00 88.82 C ANISOU 693 CG LEU A 89 17923 9377 6446 -7651 1343 -611 C ATOM 694 CD1 LEU A 89 32.397 12.537 8.872 1.00 89.38 C ANISOU 694 CD1 LEU A 89 18179 9298 6483 -7241 1471 -723 C ATOM 695 CD2 LEU A 89 34.439 12.787 10.265 1.00 93.14 C ANISOU 695 CD2 LEU A 89 18840 9777 6771 -8043 1360 -558 C ATOM 696 N CYS A 90 31.924 7.878 11.454 1.00 85.67 N ANISOU 696 N CYS A 90 16672 9428 6449 -7578 1260 -737 N ATOM 697 CA CYS A 90 32.180 6.447 11.663 1.00 85.29 C ANISOU 697 CA CYS A 90 16371 9529 6508 -7644 1158 -684 C ATOM 698 C CYS A 90 31.214 5.623 10.789 1.00 85.59 C ANISOU 698 C CYS A 90 16111 9683 6728 -7362 1217 -789 C ATOM 699 O CYS A 90 31.649 4.679 10.123 1.00 82.62 O ANISOU 699 O CYS A 90 15488 9434 6472 -7306 1105 -716 O ATOM 700 CB CYS A 90 32.086 6.088 13.147 1.00 87.63 C ANISOU 700 CB CYS A 90 16846 9762 6689 -7879 1187 -698 C ATOM 701 SG CYS A 90 32.019 4.310 13.502 1.00 91.72 S ANISOU 701 SG CYS A 90 17179 10385 7287 -7914 1128 -674 S ATOM 702 N ASN A 91 29.928 6.056 10.729 1.00 81.74 N ANISOU 702 N ASN A 91 15642 9168 6250 -7169 1389 -976 N ATOM 703 CA ASN A 91 28.872 5.477 9.900 1.00 80.04 C ANISOU 703 CA ASN A 91 15134 9094 6183 -6895 1460 -1131 C ATOM 704 C ASN A 91 29.295 5.586 8.446 1.00 84.00 C ANISOU 704 C ASN A 91 15473 9662 6780 -6671 1350 -1059 C ATOM 705 O ASN A 91 29.156 4.614 7.708 1.00 84.31 O ANISOU 705 O ASN A 91 15225 9845 6965 -6563 1303 -1073 O ATOM 706 CB ASN A 91 27.554 6.244 10.095 1.00 80.34 C ANISOU 706 CB ASN A 91 15238 9120 6168 -6697 1643 -1362 C ATOM 707 CG ASN A 91 26.905 6.150 11.468 1.00104.82 C ANISOU 707 CG ASN A 91 18473 12179 9175 -6889 1799 -1483 C ATOM 708 OD1 ASN A 91 27.539 5.864 12.493 1.00100.05 O ANISOU 708 OD1 ASN A 91 18053 11477 8485 -7199 1772 -1369 O ATOM 709 ND2 ASN A 91 25.616 6.463 11.526 1.00 95.18 N ANISOU 709 ND2 ASN A 91 17174 11043 7948 -6690 1968 -1733 N ATOM 710 N VAL A 92 29.846 6.763 8.043 1.00 80.12 N ANISOU 710 N VAL A 92 15203 9050 6189 -6625 1320 -981 N ATOM 711 CA VAL A 92 30.315 7.073 6.683 1.00 78.26 C ANISOU 711 CA VAL A 92 14906 8834 5996 -6439 1239 -906 C ATOM 712 C VAL A 92 31.527 6.236 6.291 1.00 79.39 C ANISOU 712 C VAL A 92 14856 9083 6224 -6601 1084 -732 C ATOM 713 O VAL A 92 31.491 5.617 5.240 1.00 78.25 O ANISOU 713 O VAL A 92 14459 9061 6211 -6415 1028 -727 O ATOM 714 CB VAL A 92 30.557 8.592 6.487 1.00 83.05 C ANISOU 714 CB VAL A 92 15895 9237 6423 -6399 1287 -880 C ATOM 715 CG1 VAL A 92 31.144 8.893 5.116 1.00 81.77 C ANISOU 715 CG1 VAL A 92 15723 9072 6275 -6261 1221 -789 C ATOM 716 CG2 VAL A 92 29.270 9.385 6.696 1.00 84.59 C ANISOU 716 CG2 VAL A 92 16269 9344 6528 -6123 1427 -1072 C ATOM 717 N ALA A 93 32.587 6.222 7.120 1.00 76.27 N ANISOU 717 N ALA A 93 14572 8664 5745 -6924 1007 -604 N ATOM 718 CA ALA A 93 33.831 5.475 6.891 1.00 75.80 C ANISOU 718 CA ALA A 93 14326 8740 5733 -7068 843 -456 C ATOM 719 C ALA A 93 33.605 3.984 6.692 1.00 79.87 C ANISOU 719 C ALA A 93 14549 9398 6401 -6962 780 -460 C ATOM 720 O ALA A 93 34.094 3.420 5.700 1.00 79.46 O ANISOU 720 O ALA A 93 14273 9467 6451 -6845 688 -398 O ATOM 721 CB ALA A 93 34.806 5.700 8.033 1.00 77.57 C ANISOU 721 CB ALA A 93 14713 8946 5815 -7406 768 -371 C ATOM 722 N GLY A 94 32.869 3.381 7.631 1.00 76.49 N ANISOU 722 N GLY A 94 14158 8937 5966 -7018 845 -540 N ATOM 723 CA GLY A 94 32.504 1.968 7.634 1.00 75.92 C ANISOU 723 CA GLY A 94 13906 8946 5994 -6970 830 -567 C ATOM 724 C GLY A 94 31.556 1.585 6.513 1.00 79.28 C ANISOU 724 C GLY A 94 14098 9454 6569 -6705 901 -690 C ATOM 725 O GLY A 94 31.776 0.575 5.839 1.00 77.94 O ANISOU 725 O GLY A 94 13730 9379 6502 -6619 825 -652 O ATOM 726 N CYS A 95 30.509 2.406 6.282 1.00 76.25 N ANISOU 726 N CYS A 95 13741 9045 6185 -6552 1037 -849 N ATOM 727 CA CYS A 95 29.554 2.209 5.191 1.00 75.76 C ANISOU 727 CA CYS A 95 13448 9096 6241 -6265 1090 -999 C ATOM 728 C CYS A 95 30.295 2.118 3.838 1.00 76.57 C ANISOU 728 C CYS A 95 13405 9264 6424 -6098 959 -882 C ATOM 729 O CYS A 95 29.983 1.249 3.026 1.00 76.86 O ANISOU 729 O CYS A 95 13203 9420 6582 -5955 935 -933 O ATOM 730 CB CYS A 95 28.506 3.319 5.188 1.00 77.87 C ANISOU 730 CB CYS A 95 13805 9333 6447 -6079 1218 -1177 C ATOM 731 SG CYS A 95 27.790 3.665 3.559 1.00 82.19 S ANISOU 731 SG CYS A 95 14154 10002 7072 -5636 1203 -1306 S ATOM 732 N LEU A 96 31.289 2.992 3.622 1.00 70.03 N ANISOU 732 N LEU A 96 12731 8359 5515 -6149 888 -737 N ATOM 733 CA LEU A 96 32.114 3.009 2.418 1.00 68.07 C ANISOU 733 CA LEU A 96 12381 8168 5314 -6043 787 -622 C ATOM 734 C LEU A 96 33.039 1.797 2.340 1.00 69.87 C ANISOU 734 C LEU A 96 12417 8512 5620 -6143 658 -500 C ATOM 735 O LEU A 96 33.408 1.410 1.244 1.00 67.79 O ANISOU 735 O LEU A 96 11978 8340 5441 -5996 592 -456 O ATOM 736 CB LEU A 96 32.922 4.321 2.311 1.00 68.56 C ANISOU 736 CB LEU A 96 12699 8114 5237 -6139 787 -525 C ATOM 737 CG LEU A 96 32.137 5.563 1.887 1.00 72.96 C ANISOU 737 CG LEU A 96 13488 8535 5700 -5926 894 -626 C ATOM 738 CD1 LEU A 96 32.834 6.809 2.335 1.00 73.97 C ANISOU 738 CD1 LEU A 96 13977 8487 5641 -6135 935 -549 C ATOM 739 CD2 LEU A 96 31.905 5.589 0.371 1.00 72.84 C ANISOU 739 CD2 LEU A 96 13367 8569 5742 -5606 872 -649 C ATOM 740 N PHE A 97 33.420 1.200 3.487 1.00 67.77 N ANISOU 740 N PHE A 97 12206 8235 5307 -6365 617 -448 N ATOM 741 CA PHE A 97 34.268 0.006 3.482 1.00 67.76 C ANISOU 741 CA PHE A 97 12066 8334 5346 -6405 480 -341 C ATOM 742 C PHE A 97 33.442 -1.128 2.896 1.00 74.14 C ANISOU 742 C PHE A 97 12704 9188 6280 -6236 517 -432 C ATOM 743 O PHE A 97 33.885 -1.764 1.941 1.00 73.49 O ANISOU 743 O PHE A 97 12444 9200 6279 -6097 433 -379 O ATOM 744 CB PHE A 97 34.760 -0.346 4.891 1.00 70.00 C ANISOU 744 CB PHE A 97 12509 8575 5513 -6638 423 -281 C ATOM 745 CG PHE A 97 35.917 -1.321 4.959 1.00 71.25 C ANISOU 745 CG PHE A 97 12576 8844 5652 -6649 240 -153 C ATOM 746 CD1 PHE A 97 35.689 -2.694 5.036 1.00 73.26 C ANISOU 746 CD1 PHE A 97 12804 9093 5940 -6568 210 -155 C ATOM 747 CD2 PHE A 97 37.233 -0.863 5.028 1.00 73.58 C ANISOU 747 CD2 PHE A 97 12835 9253 5867 -6749 102 -49 C ATOM 748 CE1 PHE A 97 36.758 -3.596 5.135 1.00 74.30 C ANISOU 748 CE1 PHE A 97 12894 9316 6022 -6521 27 -42 C ATOM 749 CE2 PHE A 97 38.304 -1.765 5.094 1.00 76.61 C ANISOU 749 CE2 PHE A 97 13104 9787 6219 -6708 -84 43 C ATOM 750 CZ PHE A 97 38.057 -3.126 5.158 1.00 74.50 C ANISOU 750 CZ PHE A 97 12836 9493 5978 -6566 -129 52 C ATOM 751 N PHE A 98 32.200 -1.299 3.413 1.00 71.77 N ANISOU 751 N PHE A 98 12451 8834 5986 -6257 659 -592 N ATOM 752 CA PHE A 98 31.194 -2.273 2.992 1.00 71.19 C ANISOU 752 CA PHE A 98 12227 8813 6009 -6163 741 -738 C ATOM 753 C PHE A 98 30.891 -2.139 1.509 1.00 74.16 C ANISOU 753 C PHE A 98 12382 9298 6498 -5893 723 -796 C ATOM 754 O PHE A 98 30.959 -3.141 0.791 1.00 75.50 O ANISOU 754 O PHE A 98 12401 9536 6750 -5806 676 -791 O ATOM 755 CB PHE A 98 29.914 -2.071 3.808 1.00 74.37 C ANISOU 755 CB PHE A 98 12700 9181 6375 -6256 925 -938 C ATOM 756 CG PHE A 98 28.894 -3.176 3.703 1.00 76.93 C ANISOU 756 CG PHE A 98 12899 9570 6763 -6279 1042 -1118 C ATOM 757 CD1 PHE A 98 27.986 -3.213 2.644 1.00 79.33 C ANISOU 757 CD1 PHE A 98 12947 10023 7172 -6074 1094 -1299 C ATOM 758 CD2 PHE A 98 28.794 -4.149 4.694 1.00 80.29 C ANISOU 758 CD2 PHE A 98 13485 9904 7116 -6523 1111 -1126 C ATOM 759 CE1 PHE A 98 27.026 -4.230 2.557 1.00 80.80 C ANISOU 759 CE1 PHE A 98 13000 10295 7404 -6148 1217 -1499 C ATOM 760 CE2 PHE A 98 27.825 -5.164 4.609 1.00 83.53 C ANISOU 760 CE2 PHE A 98 13816 10362 7560 -6606 1255 -1313 C ATOM 761 CZ PHE A 98 26.951 -5.197 3.540 1.00 81.11 C ANISOU 761 CZ PHE A 98 13216 10232 7372 -6436 1311 -1506 C ATOM 762 N ILE A 99 30.555 -0.906 1.045 1.00 67.73 N ANISOU 762 N ILE A 99 11588 8482 5665 -5745 759 -850 N ATOM 763 CA ILE A 99 30.243 -0.624 -0.365 1.00 64.87 C ANISOU 763 CA ILE A 99 11072 8204 5372 -5455 736 -908 C ATOM 764 C ILE A 99 31.447 -0.955 -1.223 1.00 66.68 C ANISOU 764 C ILE A 99 11232 8465 5638 -5413 603 -724 C ATOM 765 O ILE A 99 31.295 -1.745 -2.142 1.00 67.06 O ANISOU 765 O ILE A 99 11093 8606 5781 -5265 566 -756 O ATOM 766 CB ILE A 99 29.655 0.795 -0.605 1.00 67.39 C ANISOU 766 CB ILE A 99 11514 8478 5614 -5273 798 -1000 C ATOM 767 CG1 ILE A 99 28.288 0.929 0.126 1.00 68.51 C ANISOU 767 CG1 ILE A 99 11637 8658 5735 -5254 935 -1238 C ATOM 768 CG2 ILE A 99 29.514 1.103 -2.102 1.00 65.28 C ANISOU 768 CG2 ILE A 99 11152 8273 5380 -4952 747 -1027 C ATOM 769 CD1 ILE A 99 27.683 2.336 0.226 1.00 74.99 C ANISOU 769 CD1 ILE A 99 12637 9415 6441 -5069 1002 -1342 C ATOM 770 N ASN A 100 32.645 -0.475 -0.864 1.00 62.12 N ANISOU 770 N ASN A 100 10784 7836 4984 -5568 535 -551 N ATOM 771 CA ASN A 100 33.862 -0.809 -1.609 1.00 61.95 C ANISOU 771 CA ASN A 100 10660 7892 4988 -5550 418 -398 C ATOM 772 C ASN A 100 34.135 -2.320 -1.670 1.00 68.05 C ANISOU 772 C ASN A 100 11273 8746 5839 -5536 338 -364 C ATOM 773 O ASN A 100 34.402 -2.834 -2.750 1.00 68.35 O ANISOU 773 O ASN A 100 11153 8867 5949 -5374 283 -335 O ATOM 774 CB ASN A 100 35.076 -0.049 -1.083 1.00 61.40 C ANISOU 774 CB ASN A 100 10721 7802 4805 -5765 370 -262 C ATOM 775 CG ASN A 100 36.394 -0.497 -1.661 1.00 78.07 C ANISOU 775 CG ASN A 100 12679 10053 6932 -5782 251 -133 C ATOM 776 OD1 ASN A 100 36.808 -0.059 -2.736 1.00 73.89 O ANISOU 776 OD1 ASN A 100 12098 9567 6408 -5695 256 -100 O ATOM 777 ND2 ASN A 100 37.095 -1.357 -0.935 1.00 70.50 N ANISOU 777 ND2 ASN A 100 11659 9170 5957 -5887 144 -66 N ATOM 778 N THR A 101 34.045 -3.020 -0.533 1.00 65.80 N ANISOU 778 N THR A 101 11070 8413 5517 -5694 339 -368 N ATOM 779 CA THR A 101 34.289 -4.461 -0.409 1.00 65.74 C ANISOU 779 CA THR A 101 11019 8425 5533 -5688 272 -332 C ATOM 780 C THR A 101 33.430 -5.278 -1.389 1.00 70.24 C ANISOU 780 C THR A 101 11442 9032 6214 -5519 324 -450 C ATOM 781 O THR A 101 33.993 -6.001 -2.221 1.00 69.91 O ANISOU 781 O THR A 101 11287 9056 6221 -5383 237 -384 O ATOM 782 CB THR A 101 34.119 -4.883 1.073 1.00 72.93 C ANISOU 782 CB THR A 101 12139 9227 6342 -5898 300 -337 C ATOM 783 OG1 THR A 101 35.059 -4.152 1.869 1.00 69.23 O ANISOU 783 OG1 THR A 101 11784 8756 5764 -6040 221 -226 O ATOM 784 CG2 THR A 101 34.296 -6.383 1.301 1.00 72.17 C ANISOU 784 CG2 THR A 101 12105 9094 6222 -5887 246 -302 C ATOM 785 N TYR A 102 32.081 -5.121 -1.330 1.00 66.99 N ANISOU 785 N TYR A 102 11012 8604 5835 -5522 465 -641 N ATOM 786 CA TYR A 102 31.160 -5.909 -2.157 1.00 66.76 C ANISOU 786 CA TYR A 102 10827 8644 5897 -5406 524 -800 C ATOM 787 C TYR A 102 31.026 -5.404 -3.597 1.00 71.63 C ANISOU 787 C TYR A 102 11259 9367 6589 -5140 486 -836 C ATOM 788 O TYR A 102 30.491 -6.135 -4.438 1.00 71.08 O ANISOU 788 O TYR A 102 11041 9375 6591 -5024 496 -945 O ATOM 789 CB TYR A 102 29.801 -6.091 -1.457 1.00 68.24 C ANISOU 789 CB TYR A 102 11032 8825 6073 -5545 693 -1025 C ATOM 790 CG TYR A 102 30.007 -6.826 -0.148 1.00 69.46 C ANISOU 790 CG TYR A 102 11417 8843 6131 -5810 735 -974 C ATOM 791 CD1 TYR A 102 30.745 -8.009 -0.102 1.00 71.01 C ANISOU 791 CD1 TYR A 102 11724 8964 6294 -5842 655 -849 C ATOM 792 CD2 TYR A 102 29.603 -6.264 1.061 1.00 70.42 C ANISOU 792 CD2 TYR A 102 11694 8893 6167 -5999 836 -1026 C ATOM 793 CE1 TYR A 102 31.048 -8.625 1.105 1.00 72.65 C ANISOU 793 CE1 TYR A 102 12210 9020 6373 -6041 667 -779 C ATOM 794 CE2 TYR A 102 29.884 -6.884 2.277 1.00 71.61 C ANISOU 794 CE2 TYR A 102 12106 8899 6201 -6231 862 -959 C ATOM 795 CZ TYR A 102 30.607 -8.066 2.293 1.00 78.14 C ANISOU 795 CZ TYR A 102 13061 9644 6983 -6244 772 -833 C ATOM 796 OH TYR A 102 30.914 -8.685 3.476 1.00 78.19 O ANISOU 796 OH TYR A 102 13381 9488 6840 -6430 781 -760 O ATOM 797 N CYS A 103 31.586 -4.213 -3.904 1.00 68.42 N ANISOU 797 N CYS A 103 10897 8954 6148 -5059 441 -740 N ATOM 798 CA CYS A 103 31.622 -3.697 -5.270 1.00 67.75 C ANISOU 798 CA CYS A 103 10713 8934 6096 -4809 402 -743 C ATOM 799 C CYS A 103 32.851 -4.268 -5.946 1.00 69.86 C ANISOU 799 C CYS A 103 10919 9238 6388 -4773 294 -569 C ATOM 800 O CYS A 103 32.811 -4.579 -7.132 1.00 67.99 O ANISOU 800 O CYS A 103 10556 9070 6207 -4578 261 -590 O ATOM 801 CB CYS A 103 31.619 -2.178 -5.288 1.00 68.75 C ANISOU 801 CB CYS A 103 10985 8999 6137 -4749 434 -734 C ATOM 802 SG CYS A 103 29.965 -1.455 -5.191 1.00 73.82 S ANISOU 802 SG CYS A 103 11622 9669 6756 -4578 539 -998 S ATOM 803 N SER A 104 33.929 -4.455 -5.155 1.00 66.84 N ANISOU 803 N SER A 104 10610 8830 5954 -4950 232 -415 N ATOM 804 CA SER A 104 35.193 -5.077 -5.546 1.00 66.96 C ANISOU 804 CA SER A 104 10543 8923 5977 -4916 120 -269 C ATOM 805 C SER A 104 34.952 -6.553 -5.811 1.00 70.17 C ANISOU 805 C SER A 104 10880 9340 6442 -4834 91 -306 C ATOM 806 O SER A 104 35.668 -7.146 -6.611 1.00 67.94 O ANISOU 806 O SER A 104 10494 9131 6188 -4699 15 -236 O ATOM 807 CB SER A 104 36.197 -4.972 -4.404 1.00 73.53 C ANISOU 807 CB SER A 104 11459 9762 6718 -5111 49 -144 C ATOM 808 OG SER A 104 36.822 -3.702 -4.354 1.00 88.92 O ANISOU 808 OG SER A 104 13465 11724 8597 -5217 65 -90 O ATOM 809 N VAL A 105 33.989 -7.159 -5.073 1.00 68.73 N ANISOU 809 N VAL A 105 10781 9076 6258 -4938 167 -421 N ATOM 810 CA VAL A 105 33.610 -8.563 -5.204 1.00 69.55 C ANISOU 810 CA VAL A 105 10893 9147 6385 -4918 178 -482 C ATOM 811 C VAL A 105 32.807 -8.741 -6.494 1.00 73.82 C ANISOU 811 C VAL A 105 11263 9765 7020 -4745 218 -620 C ATOM 812 O VAL A 105 33.169 -9.585 -7.310 1.00 73.56 O ANISOU 812 O VAL A 105 11172 9760 7019 -4615 162 -586 O ATOM 813 CB VAL A 105 32.905 -9.101 -3.922 1.00 74.53 C ANISOU 813 CB VAL A 105 11712 9654 6951 -5146 275 -567 C ATOM 814 CG1 VAL A 105 32.120 -10.386 -4.197 1.00 75.07 C ANISOU 814 CG1 VAL A 105 11808 9677 7037 -5171 354 -701 C ATOM 815 CG2 VAL A 105 33.919 -9.332 -2.809 1.00 74.70 C ANISOU 815 CG2 VAL A 105 11931 9596 6857 -5253 186 -404 C ATOM 816 N ALA A 106 31.768 -7.900 -6.698 1.00 70.99 N ANISOU 816 N ALA A 106 10828 9455 6691 -4712 301 -778 N ATOM 817 CA ALA A 106 30.913 -7.873 -7.884 1.00 71.39 C ANISOU 817 CA ALA A 106 10704 9613 6807 -4518 322 -940 C ATOM 818 C ALA A 106 31.713 -7.675 -9.171 1.00 80.04 C ANISOU 818 C ALA A 106 11722 10762 7928 -4289 223 -822 C ATOM 819 O ALA A 106 31.459 -8.359 -10.165 1.00 80.63 O ANISOU 819 O ALA A 106 11686 10900 8052 -4149 201 -891 O ATOM 820 CB ALA A 106 29.883 -6.764 -7.754 1.00 72.34 C ANISOU 820 CB ALA A 106 10784 9787 6913 -4468 395 -1105 C ATOM 821 N PHE A 107 32.687 -6.760 -9.150 1.00 79.48 N ANISOU 821 N PHE A 107 11719 10668 7811 -4278 177 -655 N ATOM 822 CA PHE A 107 33.499 -6.446 -10.323 1.00 80.41 C ANISOU 822 CA PHE A 107 11786 10837 7931 -4104 115 -548 C ATOM 823 C PHE A 107 34.430 -7.588 -10.696 1.00 82.09 C ANISOU 823 C PHE A 107 11933 11086 8170 -4072 40 -439 C ATOM 824 O PHE A 107 34.486 -7.924 -11.880 1.00 81.76 O ANISOU 824 O PHE A 107 11800 11102 8163 -3887 13 -452 O ATOM 825 CB PHE A 107 34.220 -5.100 -10.160 1.00 83.93 C ANISOU 825 CB PHE A 107 12346 11247 8295 -4161 123 -433 C ATOM 826 CG PHE A 107 33.268 -3.925 -10.000 1.00 87.83 C ANISOU 826 CG PHE A 107 12953 11682 8736 -4115 194 -544 C ATOM 827 CD1 PHE A 107 31.898 -4.065 -10.265 1.00 92.09 C ANISOU 827 CD1 PHE A 107 13417 12262 9310 -3963 226 -751 C ATOM 828 CD2 PHE A 107 33.735 -2.682 -9.578 1.00 91.86 C ANISOU 828 CD2 PHE A 107 13649 12109 9146 -4219 229 -463 C ATOM 829 CE1 PHE A 107 31.019 -2.988 -10.105 1.00 94.28 C ANISOU 829 CE1 PHE A 107 13791 12511 9521 -3864 277 -872 C ATOM 830 CE2 PHE A 107 32.855 -1.599 -9.430 1.00 96.08 C ANISOU 830 CE2 PHE A 107 14335 12564 9606 -4135 293 -567 C ATOM 831 CZ PHE A 107 31.504 -1.759 -9.700 1.00 94.57 C ANISOU 831 CZ PHE A 107 14055 12428 9449 -3930 308 -770 C ATOM 832 N LEU A 108 35.061 -8.263 -9.703 1.00 76.86 N ANISOU 832 N LEU A 108 11335 10389 7479 -4219 3 -352 N ATOM 833 CA LEU A 108 35.873 -9.453 -9.979 1.00 76.50 C ANISOU 833 CA LEU A 108 11260 10372 7434 -4136 -78 -267 C ATOM 834 C LEU A 108 34.976 -10.614 -10.444 1.00 81.52 C ANISOU 834 C LEU A 108 11898 10961 8115 -4066 -44 -396 C ATOM 835 O LEU A 108 35.434 -11.521 -11.146 1.00 81.43 O ANISOU 835 O LEU A 108 11857 10969 8112 -3924 -96 -359 O ATOM 836 CB LEU A 108 36.696 -9.874 -8.772 1.00 76.90 C ANISOU 836 CB LEU A 108 11418 10393 7407 -4260 -145 -158 C ATOM 837 CG LEU A 108 38.023 -9.166 -8.605 1.00 81.65 C ANISOU 837 CG LEU A 108 11950 11117 7955 -4286 -222 -22 C ATOM 838 CD1 LEU A 108 38.626 -9.496 -7.288 1.00 82.48 C ANISOU 838 CD1 LEU A 108 12166 11206 7967 -4409 -298 48 C ATOM 839 CD2 LEU A 108 38.994 -9.553 -9.685 1.00 84.61 C ANISOU 839 CD2 LEU A 108 12169 11636 8344 -4092 -292 46 C ATOM 840 N GLY A 109 33.697 -10.535 -10.079 1.00 77.78 N ANISOU 840 N GLY A 109 11449 10444 7661 -4173 52 -566 N ATOM 841 CA GLY A 109 32.677 -11.481 -10.494 1.00 77.84 C ANISOU 841 CA GLY A 109 11434 10440 7702 -4172 114 -744 C ATOM 842 C GLY A 109 32.306 -11.287 -11.947 1.00 80.59 C ANISOU 842 C GLY A 109 11610 10901 8109 -3952 94 -830 C ATOM 843 O GLY A 109 32.234 -12.260 -12.708 1.00 80.73 O ANISOU 843 O GLY A 109 11605 10925 8145 -3868 79 -875 O ATOM 844 N VAL A 110 32.079 -10.017 -12.338 1.00 75.79 N ANISOU 844 N VAL A 110 10922 10366 7510 -3848 92 -853 N ATOM 845 CA VAL A 110 31.707 -9.608 -13.703 1.00 75.01 C ANISOU 845 CA VAL A 110 10703 10365 7432 -3602 63 -933 C ATOM 846 C VAL A 110 32.848 -9.913 -14.708 1.00 75.70 C ANISOU 846 C VAL A 110 10778 10464 7519 -3444 -11 -769 C ATOM 847 O VAL A 110 32.572 -10.443 -15.783 1.00 75.01 O ANISOU 847 O VAL A 110 10614 10431 7454 -3284 -35 -844 O ATOM 848 CB VAL A 110 31.211 -8.134 -13.738 1.00 79.33 C ANISOU 848 CB VAL A 110 11259 10943 7941 -3511 80 -987 C ATOM 849 CG1 VAL A 110 31.184 -7.572 -15.154 1.00 79.43 C ANISOU 849 CG1 VAL A 110 11236 11016 7929 -3223 30 -1002 C ATOM 850 CG2 VAL A 110 29.835 -7.999 -13.084 1.00 79.76 C ANISOU 850 CG2 VAL A 110 11254 11051 7999 -3588 152 -1223 C ATOM 851 N ILE A 111 34.117 -9.641 -14.330 1.00 70.81 N ANISOU 851 N ILE A 111 10219 9819 6868 -3501 -43 -566 N ATOM 852 CA ILE A 111 35.297 -9.953 -15.148 1.00 69.68 C ANISOU 852 CA ILE A 111 10034 9726 6716 -3375 -98 -425 C ATOM 853 C ILE A 111 35.309 -11.448 -15.457 1.00 72.40 C ANISOU 853 C ILE A 111 10367 10055 7086 -3308 -129 -454 C ATOM 854 O ILE A 111 35.438 -11.808 -16.615 1.00 71.59 O ANISOU 854 O ILE A 111 10205 10000 6997 -3129 -150 -465 O ATOM 855 CB ILE A 111 36.623 -9.448 -14.500 1.00 72.73 C ANISOU 855 CB ILE A 111 10441 10142 7052 -3489 -124 -248 C ATOM 856 CG1 ILE A 111 36.658 -7.908 -14.489 1.00 73.31 C ANISOU 856 CG1 ILE A 111 10570 10210 7075 -3554 -72 -224 C ATOM 857 CG2 ILE A 111 37.873 -10.016 -15.210 1.00 72.64 C ANISOU 857 CG2 ILE A 111 10339 10233 7027 -3366 -179 -135 C ATOM 858 CD1 ILE A 111 37.575 -7.289 -13.456 1.00 81.93 C ANISOU 858 CD1 ILE A 111 11704 11317 8108 -3766 -75 -112 C ATOM 859 N THR A 112 35.092 -12.296 -14.435 1.00 70.27 N ANISOU 859 N THR A 112 10198 9697 6804 -3455 -120 -477 N ATOM 860 CA THR A 112 35.030 -13.764 -14.514 1.00 70.74 C ANISOU 860 CA THR A 112 10349 9681 6850 -3430 -129 -511 C ATOM 861 C THR A 112 33.872 -14.249 -15.384 1.00 75.33 C ANISOU 861 C THR A 112 10880 10272 7470 -3389 -79 -709 C ATOM 862 O THR A 112 34.097 -15.062 -16.281 1.00 74.79 O ANISOU 862 O THR A 112 10816 10203 7399 -3246 -106 -711 O ATOM 863 CB THR A 112 34.947 -14.360 -13.111 1.00 77.29 C ANISOU 863 CB THR A 112 11371 10377 7619 -3631 -105 -500 C ATOM 864 OG1 THR A 112 36.056 -13.887 -12.354 1.00 74.09 O ANISOU 864 OG1 THR A 112 10987 9998 7165 -3646 -176 -330 O ATOM 865 CG2 THR A 112 34.952 -15.865 -13.123 1.00 77.43 C ANISOU 865 CG2 THR A 112 11577 10264 7577 -3609 -104 -519 C ATOM 866 N TYR A 113 32.646 -13.753 -15.126 1.00 72.99 N ANISOU 866 N TYR A 113 10525 10008 7200 -3507 -8 -891 N ATOM 867 CA TYR A 113 31.453 -14.137 -15.879 1.00 73.88 C ANISOU 867 CA TYR A 113 10539 10192 7341 -3487 33 -1128 C ATOM 868 C TYR A 113 31.564 -13.842 -17.368 1.00 76.40 C ANISOU 868 C TYR A 113 10731 10619 7681 -3214 -35 -1136 C ATOM 869 O TYR A 113 31.178 -14.679 -18.187 1.00 76.91 O ANISOU 869 O TYR A 113 10767 10708 7747 -3153 -38 -1253 O ATOM 870 CB TYR A 113 30.194 -13.494 -15.292 1.00 76.56 C ANISOU 870 CB TYR A 113 10786 10610 7694 -3629 110 -1338 C ATOM 871 CG TYR A 113 28.924 -13.894 -16.013 1.00 81.60 C ANISOU 871 CG TYR A 113 11267 11386 8349 -3620 146 -1629 C ATOM 872 CD1 TYR A 113 28.381 -15.168 -15.861 1.00 84.80 C ANISOU 872 CD1 TYR A 113 11737 11749 8735 -3831 230 -1783 C ATOM 873 CD2 TYR A 113 28.265 -12.999 -16.851 1.00 83.66 C ANISOU 873 CD2 TYR A 113 11337 11827 8623 -3401 95 -1765 C ATOM 874 CE1 TYR A 113 27.209 -15.540 -16.522 1.00 87.46 C ANISOU 874 CE1 TYR A 113 11898 12255 9079 -3863 269 -2085 C ATOM 875 CE2 TYR A 113 27.092 -13.359 -17.515 1.00 86.43 C ANISOU 875 CE2 TYR A 113 11504 12359 8978 -3373 106 -2063 C ATOM 876 CZ TYR A 113 26.567 -14.632 -17.349 1.00 95.11 C ANISOU 876 CZ TYR A 113 12616 13449 10071 -3624 195 -2232 C ATOM 877 OH TYR A 113 25.399 -14.975 -17.994 1.00 97.38 O ANISOU 877 OH TYR A 113 12690 13957 10354 -3636 211 -2559 O ATOM 878 N ASN A 114 32.069 -12.651 -17.713 1.00 71.16 N ANISOU 878 N ASN A 114 10022 10004 7011 -3068 -77 -1021 N ATOM 879 CA ASN A 114 32.225 -12.217 -19.096 1.00 70.01 C ANISOU 879 CA ASN A 114 9811 9936 6853 -2809 -130 -1012 C ATOM 880 C ASN A 114 33.353 -12.971 -19.808 1.00 70.90 C ANISOU 880 C ASN A 114 9958 10022 6958 -2698 -166 -860 C ATOM 881 O ASN A 114 33.177 -13.337 -20.977 1.00 70.15 O ANISOU 881 O ASN A 114 9824 9974 6858 -2524 -194 -924 O ATOM 882 CB ASN A 114 32.355 -10.695 -19.182 1.00 72.10 C ANISOU 882 CB ASN A 114 10095 10221 7077 -2720 -134 -948 C ATOM 883 CG ASN A 114 31.060 -9.978 -18.841 1.00104.36 C ANISOU 883 CG ASN A 114 14134 14365 11152 -2713 -116 -1147 C ATOM 884 OD1 ASN A 114 31.064 -8.946 -18.171 1.00 98.16 O ANISOU 884 OD1 ASN A 114 13421 13543 10333 -2762 -90 -1103 O ATOM 885 ND2 ASN A 114 29.910 -10.511 -19.280 1.00100.47 N ANISOU 885 ND2 ASN A 114 13513 13985 10677 -2652 -128 -1391 N ATOM 886 N ARG A 115 34.473 -13.269 -19.091 1.00 65.87 N ANISOU 886 N ARG A 115 9391 9328 6310 -2782 -173 -680 N ATOM 887 CA ARG A 115 35.559 -14.089 -19.642 1.00 65.51 C ANISOU 887 CA ARG A 115 9362 9283 6244 -2653 -212 -557 C ATOM 888 C ARG A 115 35.036 -15.508 -19.802 1.00 72.26 C ANISOU 888 C ARG A 115 10300 10059 7097 -2653 -207 -667 C ATOM 889 O ARG A 115 35.434 -16.195 -20.739 1.00 73.07 O ANISOU 889 O ARG A 115 10411 10168 7183 -2484 -232 -650 O ATOM 890 CB ARG A 115 36.838 -14.088 -18.777 1.00 61.92 C ANISOU 890 CB ARG A 115 8935 8833 5758 -2711 -241 -374 C ATOM 891 CG ARG A 115 37.663 -12.799 -18.776 1.00 66.90 C ANISOU 891 CG ARG A 115 9486 9564 6369 -2732 -234 -257 C ATOM 892 CD ARG A 115 37.657 -11.994 -20.075 1.00 70.87 C ANISOU 892 CD ARG A 115 9939 10130 6859 -2595 -202 -267 C ATOM 893 NE ARG A 115 38.268 -12.734 -21.173 1.00 65.09 N ANISOU 893 NE ARG A 115 9159 9456 6115 -2401 -219 -238 N ATOM 894 CZ ARG A 115 37.846 -12.697 -22.428 1.00 76.20 C ANISOU 894 CZ ARG A 115 10568 10871 7513 -2237 -207 -305 C ATOM 895 NH1 ARG A 115 36.821 -11.925 -22.768 1.00 71.08 N ANISOU 895 NH1 ARG A 115 9960 10191 6858 -2215 -193 -409 N ATOM 896 NH2 ARG A 115 38.449 -13.424 -23.357 1.00 57.72 N ANISOU 896 NH2 ARG A 115 8197 8579 5156 -2067 -217 -276 N ATOM 897 N TYR A 116 34.102 -15.928 -18.906 1.00 68.88 N ANISOU 897 N TYR A 116 9950 9549 6671 -2864 -157 -796 N ATOM 898 CA TYR A 116 33.439 -17.229 -18.978 1.00 68.78 C ANISOU 898 CA TYR A 116 10059 9440 6633 -2945 -115 -938 C ATOM 899 C TYR A 116 32.574 -17.320 -20.241 1.00 73.38 C ANISOU 899 C TYR A 116 10520 10123 7240 -2845 -114 -1126 C ATOM 900 O TYR A 116 32.710 -18.290 -20.977 1.00 73.44 O ANISOU 900 O TYR A 116 10605 10083 7216 -2758 -122 -1152 O ATOM 901 CB TYR A 116 32.638 -17.538 -17.694 1.00 68.67 C ANISOU 901 CB TYR A 116 10167 9327 6597 -3246 -28 -1047 C ATOM 902 CG TYR A 116 31.929 -18.873 -17.733 1.00 68.28 C ANISOU 902 CG TYR A 116 10289 9160 6493 -3398 51 -1214 C ATOM 903 CD1 TYR A 116 32.638 -20.066 -17.603 1.00 70.37 C ANISOU 903 CD1 TYR A 116 10837 9235 6666 -3363 46 -1110 C ATOM 904 CD2 TYR A 116 30.551 -18.947 -17.924 1.00 68.68 C ANISOU 904 CD2 TYR A 116 10230 9300 6565 -3575 136 -1494 C ATOM 905 CE1 TYR A 116 31.995 -21.298 -17.661 1.00 72.78 C ANISOU 905 CE1 TYR A 116 11371 9392 6891 -3528 140 -1266 C ATOM 906 CE2 TYR A 116 29.893 -20.173 -17.977 1.00 71.01 C ANISOU 906 CE2 TYR A 116 10692 9495 6794 -3775 234 -1673 C ATOM 907 CZ TYR A 116 30.621 -21.349 -17.854 1.00 81.08 C ANISOU 907 CZ TYR A 116 12307 10532 7969 -3765 244 -1550 C ATOM 908 OH TYR A 116 29.984 -22.568 -17.923 1.00 85.00 O ANISOU 908 OH TYR A 116 13037 10889 8371 -3987 360 -1728 O ATOM 909 N GLN A 117 31.736 -16.291 -20.511 1.00 71.11 N ANISOU 909 N GLN A 117 10054 9975 6988 -2825 -117 -1256 N ATOM 910 CA GLN A 117 30.878 -16.188 -21.701 1.00 72.97 C ANISOU 910 CA GLN A 117 10150 10350 7228 -2684 -146 -1452 C ATOM 911 C GLN A 117 31.710 -16.059 -23.024 1.00 80.74 C ANISOU 911 C GLN A 117 11129 11359 8191 -2391 -218 -1324 C ATOM 912 O GLN A 117 31.159 -16.167 -24.125 1.00 80.50 O ANISOU 912 O GLN A 117 11026 11419 8141 -2245 -256 -1465 O ATOM 913 CB GLN A 117 29.919 -14.988 -21.569 1.00 74.32 C ANISOU 913 CB GLN A 117 10159 10668 7411 -2662 -155 -1600 C ATOM 914 CG GLN A 117 28.741 -15.192 -20.626 1.00 98.22 C ANISOU 914 CG GLN A 117 13118 13750 10452 -2925 -74 -1835 C ATOM 915 CD GLN A 117 27.653 -14.165 -20.856 1.00128.84 C ANISOU 915 CD GLN A 117 16792 17837 14324 -2807 -106 -2051 C ATOM 916 OE1 GLN A 117 27.834 -12.959 -20.625 1.00128.71 O ANISOU 916 OE1 GLN A 117 16778 17829 14296 -2680 -136 -1958 O ATOM 917 NE2 GLN A 117 26.486 -14.623 -21.294 1.00121.87 N ANISOU 917 NE2 GLN A 117 15737 17135 13432 -2841 -100 -2362 N ATOM 918 N ALA A 118 33.028 -15.825 -22.896 1.00 79.52 N ANISOU 918 N ALA A 118 11042 11145 8028 -2317 -231 -1074 N ATOM 919 CA ALA A 118 33.953 -15.663 -24.005 1.00 79.84 C ANISOU 919 CA ALA A 118 11078 11218 8039 -2084 -266 -943 C ATOM 920 C ALA A 118 34.748 -16.939 -24.257 1.00 86.81 C ANISOU 920 C ALA A 118 12058 12026 8899 -2022 -269 -864 C ATOM 921 O ALA A 118 34.741 -17.411 -25.390 1.00 88.25 O ANISOU 921 O ALA A 118 12248 12229 9055 -1859 -287 -912 O ATOM 922 CB ALA A 118 34.887 -14.487 -23.742 1.00 79.87 C ANISOU 922 CB ALA A 118 11065 11250 8030 -2065 -258 -755 C ATOM 923 N VAL A 119 35.426 -17.499 -23.227 1.00 84.73 N ANISOU 923 N VAL A 119 11892 11674 8626 -2122 -261 -751 N ATOM 924 CA VAL A 119 36.226 -18.734 -23.338 1.00 86.43 C ANISOU 924 CA VAL A 119 12246 11804 8790 -2016 -276 -673 C ATOM 925 C VAL A 119 35.313 -19.951 -23.577 1.00 96.82 C ANISOU 925 C VAL A 119 13720 12994 10072 -2086 -245 -847 C ATOM 926 O VAL A 119 35.688 -20.863 -24.316 1.00 98.69 O ANISOU 926 O VAL A 119 14067 13174 10257 -1931 -255 -839 O ATOM 927 CB VAL A 119 37.228 -18.939 -22.169 1.00 89.70 C ANISOU 927 CB VAL A 119 12738 12173 9169 -2050 -302 -512 C ATOM 928 CG1 VAL A 119 38.120 -20.152 -22.403 1.00 90.33 C ANISOU 928 CG1 VAL A 119 12966 12188 9168 -1847 -338 -436 C ATOM 929 CG2 VAL A 119 38.090 -17.702 -21.973 1.00 88.67 C ANISOU 929 CG2 VAL A 119 12430 12197 9063 -2035 -320 -376 C ATOM 930 N THR A 120 34.107 -19.937 -22.994 1.00 96.19 N ANISOU 930 N THR A 120 13648 12886 10014 -2331 -195 -1022 N ATOM 931 CA THR A 120 33.086 -20.973 -23.193 1.00 98.53 C ANISOU 931 CA THR A 120 14067 13098 10272 -2483 -136 -1240 C ATOM 932 C THR A 120 31.917 -20.278 -23.867 1.00106.85 C ANISOU 932 C THR A 120 14885 14338 11376 -2510 -141 -1459 C ATOM 933 O THR A 120 31.779 -19.063 -23.720 1.00106.14 O ANISOU 933 O THR A 120 14617 14374 11337 -2469 -172 -1437 O ATOM 934 CB THR A 120 32.615 -21.599 -21.855 1.00101.16 C ANISOU 934 CB THR A 120 14608 13268 10560 -2792 -49 -1301 C ATOM 935 OG1 THR A 120 31.575 -20.805 -21.265 1.00 92.10 O ANISOU 935 OG1 THR A 120 13289 12234 9470 -3012 -1 -1456 O ATOM 936 CG2 THR A 120 33.757 -21.860 -20.872 1.00 99.63 C ANISOU 936 CG2 THR A 120 14616 12928 10309 -2742 -75 -1068 C ATOM 937 N ARG A 121 31.064 -21.034 -24.571 1.00107.24 N ANISOU 937 N ARG A 121 14947 14406 11392 -2574 -117 -1684 N ATOM 938 CA ARG A 121 29.864 -20.515 -25.231 1.00109.07 C ANISOU 938 CA ARG A 121 14938 14856 11648 -2580 -142 -1943 C ATOM 939 C ARG A 121 30.075 -19.204 -26.053 1.00115.37 C ANISOU 939 C ARG A 121 15543 15819 12474 -2273 -246 -1869 C ATOM 940 O ARG A 121 29.277 -18.275 -25.893 1.00114.89 O ANISOU 940 O ARG A 121 15302 15916 12436 -2274 -271 -1999 O ATOM 941 CB ARG A 121 28.722 -20.344 -24.202 1.00110.84 C ANISOU 941 CB ARG A 121 15067 15156 11893 -2895 -62 -2159 C ATOM 942 N PRO A 122 31.099 -19.083 -26.943 1.00114.54 N ANISOU 942 N PRO A 122 15492 15681 12347 -2005 -298 -1677 N ATOM 943 CA PRO A 122 31.211 -17.852 -27.745 1.00114.85 C ANISOU 943 CA PRO A 122 15416 15846 12377 -1750 -370 -1627 C ATOM 944 C PRO A 122 30.321 -17.904 -29.019 1.00121.92 C ANISOU 944 C PRO A 122 16221 16885 13219 -1587 -443 -1852 C ATOM 945 O PRO A 122 30.807 -18.083 -30.152 1.00121.66 O ANISOU 945 O PRO A 122 16249 16844 13133 -1373 -480 -1794 O ATOM 946 CB PRO A 122 32.722 -17.746 -28.029 1.00115.74 C ANISOU 946 CB PRO A 122 15629 15872 12475 -1594 -362 -1341 C ATOM 947 CG PRO A 122 33.290 -19.144 -27.758 1.00120.43 C ANISOU 947 CG PRO A 122 16376 16324 13058 -1668 -323 -1287 C ATOM 948 CD PRO A 122 32.159 -20.042 -27.320 1.00116.87 C ANISOU 948 CD PRO A 122 15970 15831 12603 -1906 -286 -1519 C ATOM 949 N ILE A 123 28.986 -17.769 -28.807 1.00119.69 N ANISOU 949 N ILE A 123 15779 16759 12939 -1692 -464 -2133 N ATOM 950 CA ILE A 123 27.949 -17.762 -29.844 1.00135.44 C ANISOU 950 CA ILE A 123 17632 18956 14873 -1551 -555 -2410 C ATOM 951 C ILE A 123 27.120 -16.469 -29.788 1.00145.38 C ANISOU 951 C ILE A 123 18719 20411 16107 -1393 -636 -2543 C ATOM 952 O ILE A 123 27.389 -15.576 -28.977 1.00 95.80 O ANISOU 952 O ILE A 123 12464 14079 9858 -1403 -608 -2401 O ATOM 953 CB ILE A 123 27.050 -19.012 -29.726 1.00140.13 C ANISOU 953 CB ILE A 123 18170 19609 15463 -1831 -505 -2697 C ATOM 954 N SER A 138 15.717 -7.431 -14.520 1.00151.53 N ANISOU 954 N SER A 138 17346 23340 16889 -2654 360 -5129 N ATOM 955 CA SER A 138 16.541 -6.812 -13.487 1.00149.20 C ANISOU 955 CA SER A 138 17429 22659 16600 -2757 439 -4781 C ATOM 956 C SER A 138 18.006 -7.242 -13.638 1.00150.14 C ANISOU 956 C SER A 138 17950 22316 16781 -2921 417 -4304 C ATOM 957 O SER A 138 18.277 -8.443 -13.739 1.00148.69 O ANISOU 957 O SER A 138 17770 22062 16664 -3266 489 -4273 O ATOM 958 CB SER A 138 16.007 -7.164 -12.101 1.00153.72 C ANISOU 958 CB SER A 138 17909 23300 17197 -3225 686 -4954 C ATOM 959 OG SER A 138 14.637 -6.819 -11.971 1.00165.66 O ANISOU 959 OG SER A 138 18997 25294 18650 -3089 722 -5433 O ATOM 960 N LEU A 139 18.946 -6.260 -13.672 1.00145.77 N ANISOU 960 N LEU A 139 17739 21458 16188 -2672 324 -3951 N ATOM 961 CA LEU A 139 20.389 -6.505 -13.840 1.00142.97 C ANISOU 961 CA LEU A 139 17729 20715 15877 -2787 293 -3517 C ATOM 962 C LEU A 139 21.313 -5.629 -12.956 1.00145.89 C ANISOU 962 C LEU A 139 18452 20760 16218 -2844 328 -3189 C ATOM 963 O LEU A 139 22.244 -6.163 -12.345 1.00143.31 O ANISOU 963 O LEU A 139 18319 20187 15945 -3169 395 -2935 O ATOM 964 CB LEU A 139 20.782 -6.373 -15.317 1.00142.55 C ANISOU 964 CB LEU A 139 17719 20651 15794 -2418 113 -3418 C ATOM 965 N VAL A 140 21.077 -4.299 -12.911 1.00144.28 N ANISOU 965 N VAL A 140 18354 20556 15912 -2515 275 -3201 N ATOM 966 CA VAL A 140 21.882 -3.350 -12.119 1.00143.34 C ANISOU 966 CA VAL A 140 18584 20140 15738 -2563 310 -2924 C ATOM 967 C VAL A 140 21.434 -3.374 -10.636 1.00148.85 C ANISOU 967 C VAL A 140 19251 20854 16451 -2882 473 -3029 C ATOM 968 O VAL A 140 20.236 -3.301 -10.344 1.00150.74 O ANISOU 968 O VAL A 140 19233 21372 16669 -2825 531 -3370 O ATOM 969 CB VAL A 140 21.921 -1.920 -12.755 1.00147.91 C ANISOU 969 CB VAL A 140 19390 20645 16165 -2086 197 -2868 C ATOM 970 CG1 VAL A 140 22.560 -0.884 -11.825 1.00147.07 C ANISOU 970 CG1 VAL A 140 19645 20256 15979 -2171 261 -2647 C ATOM 971 CG2 VAL A 140 22.643 -1.936 -14.103 1.00146.76 C ANISOU 971 CG2 VAL A 140 19370 20399 15992 -1861 68 -2690 C ATOM 972 N ILE A 141 22.415 -3.497 -9.715 1.00144.13 N ANISOU 972 N ILE A 141 18906 19979 15879 -3216 545 -2749 N ATOM 973 CA ILE A 141 22.221 -3.570 -8.260 1.00144.40 C ANISOU 973 CA ILE A 141 18992 19960 15913 -3556 699 -2784 C ATOM 974 C ILE A 141 22.215 -2.177 -7.565 1.00149.59 C ANISOU 974 C ILE A 141 19872 20506 16460 -3420 720 -2737 C ATOM 975 O ILE A 141 22.571 -2.079 -6.382 1.00148.64 O ANISOU 975 O ILE A 141 19926 20226 16325 -3710 819 -2626 O ATOM 976 CB ILE A 141 23.232 -4.558 -7.598 1.00145.50 C ANISOU 976 CB ILE A 141 19295 19874 16113 -3976 752 -2532 C ATOM 977 CG1 ILE A 141 24.692 -4.338 -8.083 1.00143.69 C ANISOU 977 CG1 ILE A 141 19306 19407 15883 -3913 629 -2164 C ATOM 978 CG2 ILE A 141 22.787 -6.009 -7.787 1.00146.38 C ANISOU 978 CG2 ILE A 141 19207 20113 16299 -4204 816 -2693 C ATOM 979 CD1 ILE A 141 25.543 -3.417 -7.219 1.00148.74 C ANISOU 979 CD1 ILE A 141 20245 19819 16451 -4009 636 -1925 C ATOM 980 N TRP A 142 21.770 -1.119 -8.285 1.00147.84 N ANISOU 980 N TRP A 142 19672 20360 16140 -2968 628 -2833 N ATOM 981 CA TRP A 142 21.650 0.241 -7.745 1.00148.69 C ANISOU 981 CA TRP A 142 20032 20353 16110 -2779 647 -2818 C ATOM 982 C TRP A 142 20.619 0.245 -6.596 1.00152.33 C ANISOU 982 C TRP A 142 20326 20989 16562 -2919 796 -3093 C ATOM 983 O TRP A 142 20.893 0.804 -5.533 1.00151.53 O ANISOU 983 O TRP A 142 20463 20705 16406 -3094 886 -2987 O ATOM 984 CB TRP A 142 21.239 1.235 -8.853 1.00149.45 C ANISOU 984 CB TRP A 142 20208 20504 16071 -2213 513 -2904 C ATOM 985 CG TRP A 142 21.250 2.676 -8.422 1.00152.01 C ANISOU 985 CG TRP A 142 20903 20637 16218 -1991 527 -2849 C ATOM 986 CD1 TRP A 142 22.289 3.552 -8.528 1.00154.15 C ANISOU 986 CD1 TRP A 142 21634 20557 16379 -1981 506 -2545 C ATOM 987 CD2 TRP A 142 20.167 3.407 -7.816 1.00154.66 C ANISOU 987 CD2 TRP A 142 21196 21122 16446 -1756 580 -3122 C ATOM 988 NE1 TRP A 142 21.928 4.782 -8.020 1.00155.66 N ANISOU 988 NE1 TRP A 142 22118 20632 16394 -1767 544 -2599 N ATOM 989 CE2 TRP A 142 20.632 4.720 -7.573 1.00159.26 C ANISOU 989 CE2 TRP A 142 22273 21390 16849 -1599 583 -2946 C ATOM 990 CE3 TRP A 142 18.848 3.078 -7.444 1.00158.18 C ANISOU 990 CE3 TRP A 142 21230 21952 16919 -1677 638 -3517 C ATOM 991 CZ2 TRP A 142 19.827 5.704 -6.977 1.00161.19 C ANISOU 991 CZ2 TRP A 142 22640 21667 16938 -1326 629 -3136 C ATOM 992 CZ3 TRP A 142 18.052 4.052 -6.855 1.00162.27 C ANISOU 992 CZ3 TRP A 142 21817 22546 17294 -1405 684 -3719 C ATOM 993 CH2 TRP A 142 18.540 5.349 -6.631 1.00163.33 C ANISOU 993 CH2 TRP A 142 22474 22337 17247 -1210 673 -3523 C ATOM 994 N VAL A 143 19.458 -0.425 -6.811 1.00149.25 N ANISOU 994 N VAL A 143 19518 20969 16221 -2879 834 -3456 N ATOM 995 CA VAL A 143 18.344 -0.560 -5.862 1.00150.57 C ANISOU 995 CA VAL A 143 19437 21391 16381 -3026 998 -3791 C ATOM 996 C VAL A 143 18.768 -1.182 -4.530 1.00151.32 C ANISOU 996 C VAL A 143 19664 21304 16528 -3588 1177 -3665 C ATOM 997 O VAL A 143 18.242 -0.805 -3.478 1.00152.18 O ANISOU 997 O VAL A 143 19784 21457 16581 -3705 1320 -3805 O ATOM 998 CB VAL A 143 17.187 -1.359 -6.497 1.00156.63 C ANISOU 998 CB VAL A 143 19701 22610 17201 -2962 1006 -4199 C ATOM 999 N ALA A 144 19.723 -2.132 -4.591 1.00143.91 N ANISOU 999 N ALA A 144 18843 20160 15675 -3907 1163 -3405 N ATOM 1000 CA ALA A 144 20.266 -2.854 -3.443 1.00141.49 C ANISOU 1000 CA ALA A 144 18715 19650 15395 -4406 1296 -3251 C ATOM 1001 C ALA A 144 21.108 -1.957 -2.555 1.00140.12 C ANISOU 1001 C ALA A 144 18924 19170 15145 -4468 1293 -2974 C ATOM 1002 O ALA A 144 20.706 -1.689 -1.425 1.00140.43 O ANISOU 1002 O ALA A 144 19036 19194 15126 -4651 1435 -3064 O ATOM 1003 CB ALA A 144 21.085 -4.051 -3.913 1.00140.51 C ANISOU 1003 CB ALA A 144 18628 19402 15356 -4615 1243 -3058 C ATOM 1004 N ILE A 145 22.242 -1.452 -3.082 1.00132.62 N ANISOU 1004 N ILE A 145 18212 17995 14183 -4325 1140 -2659 N ATOM 1005 CA ILE A 145 23.203 -0.603 -2.362 1.00130.64 C ANISOU 1005 CA ILE A 145 18329 17458 13851 -4413 1121 -2383 C ATOM 1006 C ILE A 145 22.586 0.718 -1.831 1.00133.61 C ANISOU 1006 C ILE A 145 18836 17826 14101 -4220 1180 -2506 C ATOM 1007 O ILE A 145 23.259 1.435 -1.092 1.00133.00 O ANISOU 1007 O ILE A 145 19077 17518 13941 -4337 1192 -2317 O ATOM 1008 CB ILE A 145 24.515 -0.352 -3.169 1.00132.04 C ANISOU 1008 CB ILE A 145 18690 17448 14031 -4320 965 -2066 C ATOM 1009 CG1 ILE A 145 24.253 0.259 -4.570 1.00133.11 C ANISOU 1009 CG1 ILE A 145 18765 17669 14141 -3876 855 -2126 C ATOM 1010 CG2 ILE A 145 25.374 -1.622 -3.255 1.00131.01 C ANISOU 1010 CG2 ILE A 145 18517 17266 13996 -4575 921 -1894 C ATOM 1011 CD1 ILE A 145 24.566 1.744 -4.674 1.00140.77 C ANISOU 1011 CD1 ILE A 145 20064 18460 14963 -3653 821 -2019 C ATOM 1012 N VAL A 146 21.315 1.014 -2.176 1.00130.00 N ANISOU 1012 N VAL A 146 18137 17637 13620 -3924 1214 -2837 N ATOM 1013 CA VAL A 146 20.588 2.187 -1.685 1.00130.72 C ANISOU 1013 CA VAL A 146 18328 17761 13579 -3683 1273 -3003 C ATOM 1014 C VAL A 146 19.992 1.853 -0.310 1.00133.51 C ANISOU 1014 C VAL A 146 18613 18187 13928 -4022 1473 -3170 C ATOM 1015 O VAL A 146 20.158 2.630 0.632 1.00133.55 O ANISOU 1015 O VAL A 146 18896 18015 13830 -4094 1542 -3099 O ATOM 1016 CB VAL A 146 19.568 2.731 -2.726 1.00136.58 C ANISOU 1016 CB VAL A 146 18857 18772 14264 -3134 1189 -3282 C ATOM 1017 CG1 VAL A 146 18.388 3.452 -2.073 1.00139.30 C ANISOU 1017 CG1 VAL A 146 19112 19316 14501 -2921 1293 -3606 C ATOM 1018 CG2 VAL A 146 20.265 3.645 -3.727 1.00135.79 C ANISOU 1018 CG2 VAL A 146 19069 18455 14068 -2773 1025 -3063 C ATOM 1019 N GLY A 147 19.362 0.681 -0.202 1.00129.05 N ANISOU 1019 N GLY A 147 17718 17856 13459 -4262 1575 -3380 N ATOM 1020 CA GLY A 147 18.792 0.186 1.047 1.00129.43 C ANISOU 1020 CA GLY A 147 17708 17974 13495 -4646 1794 -3551 C ATOM 1021 C GLY A 147 19.862 -0.135 2.074 1.00129.38 C ANISOU 1021 C GLY A 147 18065 17622 13472 -5070 1835 -3232 C ATOM 1022 O GLY A 147 19.686 0.142 3.265 1.00129.22 O ANISOU 1022 O GLY A 147 18206 17522 13372 -5284 1978 -3265 O ATOM 1023 N ALA A 148 20.994 -0.704 1.598 1.00122.60 N ANISOU 1023 N ALA A 148 17335 16571 12676 -5167 1697 -2929 N ATOM 1024 CA ALA A 148 22.166 -1.073 2.395 1.00120.27 C ANISOU 1024 CA ALA A 148 17362 15976 12358 -5503 1676 -2612 C ATOM 1025 C ALA A 148 22.840 0.159 2.985 1.00122.80 C ANISOU 1025 C ALA A 148 18016 16073 12572 -5450 1628 -2415 C ATOM 1026 O ALA A 148 23.168 0.146 4.170 1.00123.47 O ANISOU 1026 O ALA A 148 18332 15998 12582 -5741 1703 -2324 O ATOM 1027 CB ALA A 148 23.157 -1.851 1.545 1.00118.91 C ANISOU 1027 CB ALA A 148 17191 15720 12271 -5509 1518 -2379 C ATOM 1028 N ALA A 149 23.024 1.228 2.177 1.00116.98 N ANISOU 1028 N ALA A 149 17336 15310 11802 -5092 1511 -2361 N ATOM 1029 CA ALA A 149 23.629 2.483 2.629 1.00115.84 C ANISOU 1029 CA ALA A 149 17545 14939 11531 -5045 1480 -2195 C ATOM 1030 C ALA A 149 22.724 3.242 3.625 1.00119.21 C ANISOU 1030 C ALA A 149 18064 15386 11844 -5026 1635 -2398 C ATOM 1031 O ALA A 149 23.215 3.711 4.654 1.00118.34 O ANISOU 1031 O ALA A 149 18255 15073 11637 -5243 1679 -2270 O ATOM 1032 CB ALA A 149 23.967 3.365 1.438 1.00116.30 C ANISOU 1032 CB ALA A 149 17687 14947 11554 -4675 1345 -2108 C ATOM 1033 N SER A 150 21.404 3.326 3.336 1.00116.07 N ANISOU 1033 N SER A 150 17389 15259 11453 -4769 1718 -2734 N ATOM 1034 CA SER A 150 20.418 4.003 4.188 1.00117.75 C ANISOU 1034 CA SER A 150 17621 15560 11560 -4695 1875 -2984 C ATOM 1035 C SER A 150 20.266 3.326 5.557 1.00120.77 C ANISOU 1035 C SER A 150 18034 15919 11935 -5161 2058 -3029 C ATOM 1036 O SER A 150 19.827 3.964 6.516 1.00121.83 O ANISOU 1036 O SER A 150 18314 16020 11957 -5199 2190 -3136 O ATOM 1037 CB SER A 150 19.073 4.097 3.479 1.00124.00 C ANISOU 1037 CB SER A 150 18029 16721 12365 -4303 1902 -3363 C ATOM 1038 OG SER A 150 19.220 4.722 2.214 1.00133.72 O ANISOU 1038 OG SER A 150 19285 17949 13572 -3846 1723 -3313 O ATOM 1039 N TYR A 151 20.647 2.038 5.640 1.00115.07 N ANISOU 1039 N TYR A 151 17219 15193 11311 -5506 2069 -2942 N ATOM 1040 CA TYR A 151 20.653 1.230 6.859 1.00114.55 C ANISOU 1040 CA TYR A 151 17257 15052 11215 -5969 2229 -2942 C ATOM 1041 C TYR A 151 21.787 1.754 7.759 1.00114.81 C ANISOU 1041 C TYR A 151 17731 14747 11144 -6158 2166 -2628 C ATOM 1042 O TYR A 151 21.534 2.058 8.928 1.00114.94 O ANISOU 1042 O TYR A 151 17938 14685 11051 -6350 2308 -2684 O ATOM 1043 CB TYR A 151 20.771 -0.275 6.484 1.00115.23 C ANISOU 1043 CB TYR A 151 17173 15202 11408 -6210 2234 -2932 C ATOM 1044 CG TYR A 151 21.380 -1.217 7.507 1.00116.46 C ANISOU 1044 CG TYR A 151 17595 15142 11512 -6660 2300 -2766 C ATOM 1045 CD1 TYR A 151 20.715 -1.514 8.694 1.00120.08 C ANISOU 1045 CD1 TYR A 151 18146 15604 11876 -6979 2539 -2936 C ATOM 1046 CD2 TYR A 151 22.554 -1.915 7.226 1.00115.42 C ANISOU 1046 CD2 TYR A 151 17611 14829 11414 -6750 2133 -2467 C ATOM 1047 CE1 TYR A 151 21.257 -2.401 9.625 1.00121.03 C ANISOU 1047 CE1 TYR A 151 18573 15501 11914 -7369 2597 -2782 C ATOM 1048 CE2 TYR A 151 23.099 -2.815 8.141 1.00116.40 C ANISOU 1048 CE2 TYR A 151 18009 14757 11460 -7102 2172 -2324 C ATOM 1049 CZ TYR A 151 22.453 -3.046 9.347 1.00126.89 C ANISOU 1049 CZ TYR A 151 19489 16048 12674 -7408 2401 -2474 C ATOM 1050 OH TYR A 151 22.998 -3.913 10.265 1.00129.68 O ANISOU 1050 OH TYR A 151 20180 16177 12914 -7731 2434 -2325 O ATOM 1051 N PHE A 152 22.994 1.967 7.174 1.00108.23 N ANISOU 1051 N PHE A 152 17046 13744 10332 -6084 1957 -2328 N ATOM 1052 CA PHE A 152 24.174 2.519 7.851 1.00106.67 C ANISOU 1052 CA PHE A 152 17219 13276 10034 -6249 1865 -2044 C ATOM 1053 C PHE A 152 23.958 3.946 8.341 1.00109.61 C ANISOU 1053 C PHE A 152 17835 13542 10268 -6123 1918 -2085 C ATOM 1054 O PHE A 152 24.423 4.279 9.424 1.00109.44 O ANISOU 1054 O PHE A 152 18110 13343 10131 -6364 1948 -1978 O ATOM 1055 CB PHE A 152 25.389 2.514 6.925 1.00106.86 C ANISOU 1055 CB PHE A 152 17268 13221 10113 -6167 1650 -1781 C ATOM 1056 CG PHE A 152 26.101 1.199 6.745 1.00107.20 C ANISOU 1056 CG PHE A 152 17220 13270 10240 -6348 1558 -1636 C ATOM 1057 CD1 PHE A 152 27.086 0.796 7.640 1.00110.21 C ANISOU 1057 CD1 PHE A 152 17825 13501 10550 -6634 1495 -1434 C ATOM 1058 CD2 PHE A 152 25.875 0.419 5.620 1.00108.09 C ANISOU 1058 CD2 PHE A 152 17048 13535 10487 -6193 1510 -1691 C ATOM 1059 CE1 PHE A 152 27.780 -0.402 7.448 1.00110.07 C ANISOU 1059 CE1 PHE A 152 17757 13482 10582 -6736 1392 -1300 C ATOM 1060 CE2 PHE A 152 26.574 -0.772 5.425 1.00109.90 C ANISOU 1060 CE2 PHE A 152 17237 13746 10774 -6328 1422 -1551 C ATOM 1061 CZ PHE A 152 27.519 -1.176 6.342 1.00107.92 C ANISOU 1061 CZ PHE A 152 17222 13341 10441 -6582 1363 -1356 C ATOM 1062 N LEU A 153 23.271 4.786 7.543 1.00106.10 N ANISOU 1062 N LEU A 153 17302 13198 9815 -5728 1919 -2241 N ATOM 1063 CA LEU A 153 22.961 6.187 7.853 1.00107.14 C ANISOU 1063 CA LEU A 153 17699 13219 9791 -5520 1969 -2305 C ATOM 1064 C LEU A 153 22.245 6.348 9.206 1.00112.56 C ANISOU 1064 C LEU A 153 18484 13907 10378 -5694 2166 -2475 C ATOM 1065 O LEU A 153 22.491 7.331 9.903 1.00114.08 O ANISOU 1065 O LEU A 153 19032 13896 10417 -5723 2199 -2412 O ATOM 1066 CB LEU A 153 22.180 6.831 6.672 1.00108.32 C ANISOU 1066 CB LEU A 153 17701 13518 9939 -4998 1930 -2486 C ATOM 1067 CG LEU A 153 21.088 7.899 6.926 1.00115.38 C ANISOU 1067 CG LEU A 153 18675 14473 10690 -4646 2039 -2748 C ATOM 1068 CD1 LEU A 153 21.689 9.283 7.120 1.00115.89 C ANISOU 1068 CD1 LEU A 153 19263 14210 10561 -4543 2005 -2583 C ATOM 1069 CD2 LEU A 153 20.104 7.953 5.761 1.00118.72 C ANISOU 1069 CD2 LEU A 153 18772 15184 11154 -4147 1991 -3002 C ATOM 1070 N ILE A 154 21.422 5.364 9.602 1.00109.15 N ANISOU 1070 N ILE A 154 17768 13688 10017 -5852 2311 -2686 N ATOM 1071 CA ILE A 154 20.686 5.385 10.874 1.00110.55 C ANISOU 1071 CA ILE A 154 18011 13895 10099 -6055 2531 -2874 C ATOM 1072 C ILE A 154 21.436 4.570 11.979 1.00112.42 C ANISOU 1072 C ILE A 154 18469 13943 10301 -6562 2565 -2682 C ATOM 1073 O ILE A 154 21.311 4.905 13.163 1.00112.86 O ANISOU 1073 O ILE A 154 18774 13883 10224 -6760 2695 -2709 O ATOM 1074 CB ILE A 154 19.201 4.957 10.635 1.00115.82 C ANISOU 1074 CB ILE A 154 18239 14942 10826 -5910 2703 -3282 C ATOM 1075 CG1 ILE A 154 18.459 6.029 9.805 1.00117.74 C ANISOU 1075 CG1 ILE A 154 18354 15350 11031 -5345 2657 -3484 C ATOM 1076 CG2 ILE A 154 18.433 4.679 11.936 1.00118.80 C ANISOU 1076 CG2 ILE A 154 18627 15391 11119 -6214 2971 -3499 C ATOM 1077 CD1 ILE A 154 17.747 5.500 8.588 1.00124.29 C ANISOU 1077 CD1 ILE A 154 18712 16523 11988 -5067 2603 -3702 C ATOM 1078 N LEU A 155 22.258 3.562 11.582 1.00106.66 N ANISOU 1078 N LEU A 155 17687 13171 9669 -6734 2434 -2481 N ATOM 1079 CA LEU A 155 23.047 2.708 12.486 1.00105.58 C ANISOU 1079 CA LEU A 155 17775 12860 9482 -7137 2419 -2287 C ATOM 1080 C LEU A 155 23.880 3.501 13.473 1.00110.31 C ANISOU 1080 C LEU A 155 18785 13206 9923 -7290 2363 -2091 C ATOM 1081 O LEU A 155 24.678 4.340 13.066 1.00110.62 O ANISOU 1081 O LEU A 155 18952 13138 9940 -7158 2202 -1920 O ATOM 1082 CB LEU A 155 24.015 1.784 11.709 1.00103.47 C ANISOU 1082 CB LEU A 155 17423 12568 9322 -7166 2220 -2065 C ATOM 1083 CG LEU A 155 23.510 0.450 11.138 1.00108.11 C ANISOU 1083 CG LEU A 155 17733 13317 10027 -7223 2278 -2186 C ATOM 1084 CD1 LEU A 155 24.612 -0.234 10.327 1.00105.82 C ANISOU 1084 CD1 LEU A 155 17411 12973 9822 -7184 2053 -1937 C ATOM 1085 CD2 LEU A 155 23.019 -0.498 12.234 1.00112.13 C ANISOU 1085 CD2 LEU A 155 18373 13783 10447 -7594 2485 -2293 C ATOM 1086 N ASP A 156 23.716 3.220 14.761 1.00107.32 N ANISOU 1086 N ASP A 156 18628 12730 9418 -7593 2503 -2123 N ATOM 1087 CA ASP A 156 24.526 3.825 15.801 1.00107.12 C ANISOU 1087 CA ASP A 156 19002 12473 9227 -7783 2445 -1945 C ATOM 1088 C ASP A 156 25.732 2.886 15.960 1.00108.84 C ANISOU 1088 C ASP A 156 19333 12588 9435 -7991 2253 -1683 C ATOM 1089 O ASP A 156 25.709 1.922 16.730 1.00110.00 O ANISOU 1089 O ASP A 156 19607 12677 9511 -8238 2319 -1674 O ATOM 1090 CB ASP A 156 23.731 4.006 17.105 1.00111.37 C ANISOU 1090 CB ASP A 156 19740 12962 9615 -7982 2689 -2119 C ATOM 1091 CG ASP A 156 24.600 4.445 18.264 1.00125.92 C ANISOU 1091 CG ASP A 156 22014 14562 11269 -8223 2621 -1931 C ATOM 1092 OD1 ASP A 156 25.069 5.615 18.251 1.00126.44 O ANISOU 1092 OD1 ASP A 156 22253 14523 11265 -8124 2532 -1848 O ATOM 1093 OD2 ASP A 156 24.867 3.605 19.152 1.00135.39 O ANISOU 1093 OD2 ASP A 156 23403 15666 12372 -8514 2647 -1863 O ATOM 1094 N SER A 157 26.754 3.151 15.157 1.00102.25 N ANISOU 1094 N SER A 157 18448 11743 8660 -7864 2021 -1487 N ATOM 1095 CA SER A 157 28.004 2.407 15.029 1.00100.64 C ANISOU 1095 CA SER A 157 18274 11504 8462 -7959 1795 -1248 C ATOM 1096 C SER A 157 28.932 2.495 16.222 1.00105.19 C ANISOU 1096 C SER A 157 19189 11929 8850 -8209 1692 -1089 C ATOM 1097 O SER A 157 29.865 1.694 16.325 1.00104.66 O ANISOU 1097 O SER A 157 19158 11854 8754 -8282 1511 -924 O ATOM 1098 CB SER A 157 28.769 2.968 13.843 1.00103.40 C ANISOU 1098 CB SER A 157 18464 11914 8909 -7751 1612 -1127 C ATOM 1099 OG SER A 157 29.071 4.335 14.082 1.00112.98 O ANISOU 1099 OG SER A 157 19881 13029 10018 -7752 1601 -1097 O ATOM 1100 N THR A 158 28.743 3.515 17.068 1.00102.84 N ANISOU 1100 N THR A 158 19139 11522 8413 -8308 1783 -1138 N ATOM 1101 CA THR A 158 29.663 3.825 18.157 1.00103.01 C ANISOU 1101 CA THR A 158 19486 11413 8241 -8539 1668 -999 C ATOM 1102 C THR A 158 29.202 3.407 19.555 1.00109.36 C ANISOU 1102 C THR A 158 20584 12095 8874 -8772 1811 -1062 C ATOM 1103 O THR A 158 28.051 3.606 19.954 1.00110.58 O ANISOU 1103 O THR A 158 20780 12228 9008 -8793 2065 -1255 O ATOM 1104 CB THR A 158 30.047 5.319 18.121 1.00 99.06 C ANISOU 1104 CB THR A 158 19123 10846 7667 -8527 1633 -974 C ATOM 1105 OG1 THR A 158 28.869 6.118 17.970 1.00 93.13 O ANISOU 1105 OG1 THR A 158 18376 10073 6937 -8373 1854 -1168 O ATOM 1106 CG2 THR A 158 31.015 5.633 16.987 1.00 92.62 C ANISOU 1106 CG2 THR A 158 18129 10119 6945 -8414 1435 -842 C ATOM 1107 N ASN A 159 30.163 2.847 20.300 1.00105.89 N ANISOU 1107 N ASN A 159 20355 11588 8290 -8938 1635 -902 N ATOM 1108 CA ASN A 159 30.051 2.399 21.683 1.00106.81 C ANISOU 1108 CA ASN A 159 20833 11558 8193 -9170 1706 -906 C ATOM 1109 C ASN A 159 31.296 2.860 22.424 1.00110.94 C ANISOU 1109 C ASN A 159 21594 12029 8528 -9297 1465 -746 C ATOM 1110 O ASN A 159 32.387 2.884 21.847 1.00108.12 O ANISOU 1110 O ASN A 159 21082 11786 8214 -9220 1207 -610 O ATOM 1111 CB ASN A 159 29.953 0.872 21.756 1.00105.85 C ANISOU 1111 CB ASN A 159 20745 11416 8058 -9200 1710 -877 C ATOM 1112 CG ASN A 159 31.170 0.149 21.221 1.00127.42 C ANISOU 1112 CG ASN A 159 23380 14221 10812 -9082 1398 -681 C ATOM 1113 OD1 ASN A 159 31.585 0.344 20.067 1.00127.56 O ANISOU 1113 OD1 ASN A 159 23069 14389 11010 -8895 1272 -634 O ATOM 1114 ND2 ASN A 159 31.752 -0.719 22.041 1.00114.58 N ANISOU 1114 ND2 ASN A 159 22054 12494 8988 -9166 1272 -572 N ATOM 1115 N THR A 160 31.146 3.198 23.705 1.00111.20 N ANISOU 1115 N THR A 160 21991 11915 8346 -9501 1548 -777 N ATOM 1116 CA THR A 160 32.295 3.602 24.503 1.00112.74 C ANISOU 1116 CA THR A 160 22422 12077 8335 -9643 1314 -650 C ATOM 1117 C THR A 160 32.617 2.469 25.491 1.00119.00 C ANISOU 1117 C THR A 160 23512 12781 8921 -9741 1221 -571 C ATOM 1118 O THR A 160 31.707 1.793 25.979 1.00119.45 O ANISOU 1118 O THR A 160 23751 12711 8925 -9811 1446 -655 O ATOM 1119 CB THR A 160 32.104 5.024 25.081 1.00120.11 C ANISOU 1119 CB THR A 160 23560 12915 9162 -9775 1422 -726 C ATOM 1120 OG1 THR A 160 33.265 5.820 24.806 1.00116.36 O ANISOU 1120 OG1 THR A 160 23030 12526 8655 -9816 1187 -630 O ATOM 1121 CG2 THR A 160 31.741 5.046 26.562 1.00121.01 C ANISOU 1121 CG2 THR A 160 24104 12848 9025 -9993 1546 -776 C ATOM 1122 N VAL A 161 33.916 2.207 25.685 1.00117.43 N ANISOU 1122 N VAL A 161 23347 12667 8603 -9728 890 -423 N ATOM 1123 CA VAL A 161 34.452 1.191 26.594 1.00120.29 C ANISOU 1123 CA VAL A 161 24022 12958 8724 -9753 724 -328 C ATOM 1124 C VAL A 161 35.716 1.739 27.255 1.00129.65 C ANISOU 1124 C VAL A 161 25315 14241 9705 -9830 413 -246 C ATOM 1125 O VAL A 161 36.482 2.421 26.573 1.00128.14 O ANISOU 1125 O VAL A 161 24817 14251 9618 -9798 248 -222 O ATOM 1126 CB VAL A 161 34.714 -0.196 25.950 1.00123.42 C ANISOU 1126 CB VAL A 161 24303 13407 9185 -9543 601 -244 C ATOM 1127 CG1 VAL A 161 33.418 -0.965 25.701 1.00122.80 C ANISOU 1127 CG1 VAL A 161 24268 13184 9206 -9554 927 -345 C ATOM 1128 CG2 VAL A 161 35.559 -0.093 24.686 1.00121.49 C ANISOU 1128 CG2 VAL A 161 23592 13419 9148 -9341 377 -176 C ATOM 1129 N PRO A 162 35.989 1.446 28.551 1.00132.10 N ANISOU 1129 N PRO A 162 26053 14430 9710 -9942 325 -213 N ATOM 1130 CA PRO A 162 37.212 1.984 29.177 1.00135.21 C ANISOU 1130 CA PRO A 162 26514 14964 9897 -10017 7 -162 C ATOM 1131 C PRO A 162 38.520 1.554 28.497 1.00143.31 C ANISOU 1131 C PRO A 162 27201 16294 10955 -9814 -369 -72 C ATOM 1132 O PRO A 162 38.568 0.495 27.861 1.00142.97 O ANISOU 1132 O PRO A 162 27032 16290 11001 -9578 -433 -11 O ATOM 1133 CB PRO A 162 37.107 1.500 30.624 1.00139.24 C ANISOU 1133 CB PRO A 162 27571 15266 10068 -10117 -4 -145 C ATOM 1134 CG PRO A 162 35.645 1.244 30.824 1.00142.28 C ANISOU 1134 CG PRO A 162 28175 15379 10504 -10210 413 -231 C ATOM 1135 CD PRO A 162 35.195 0.677 29.527 1.00135.02 C ANISOU 1135 CD PRO A 162 26881 14534 9886 -10029 520 -238 C ATOM 1136 N ASP A 163 39.566 2.409 28.605 1.00142.40 N ANISOU 1136 N ASP A 163 26932 16410 10766 -9921 -603 -83 N ATOM 1137 CA ASP A 163 40.904 2.226 28.020 1.00143.09 C ANISOU 1137 CA ASP A 163 26643 16862 10864 -9781 -959 -43 C ATOM 1138 C ASP A 163 41.644 0.990 28.563 1.00151.04 C ANISOU 1138 C ASP A 163 27792 17960 11637 -9533 -1281 35 C ATOM 1139 O ASP A 163 41.180 0.372 29.530 1.00152.32 O ANISOU 1139 O ASP A 163 28422 17868 11583 -9516 -1234 65 O ATOM 1140 CB ASP A 163 41.760 3.517 28.169 1.00145.70 C ANISOU 1140 CB ASP A 163 26826 17410 11124 -10042 -1085 -115 C ATOM 1141 CG ASP A 163 41.976 4.057 29.579 1.00152.11 C ANISOU 1141 CG ASP A 163 28030 18146 11621 -10282 -1157 -161 C ATOM 1142 OD1 ASP A 163 41.032 3.991 30.397 1.00152.00 O ANISOU 1142 OD1 ASP A 163 28444 17806 11503 -10352 -944 -162 O ATOM 1143 OD2 ASP A 163 43.060 4.626 29.837 1.00156.80 O ANISOU 1143 OD2 ASP A 163 28489 19015 12074 -10430 -1404 -213 O ATOM 1144 N SER A 164 42.799 0.637 27.940 1.00149.79 N ANISOU 1144 N SER A 164 27247 18164 11501 -9328 -1603 57 N ATOM 1145 CA SER A 164 43.654 -0.503 28.316 1.00152.77 C ANISOU 1145 CA SER A 164 27702 18694 11649 -9009 -1961 117 C ATOM 1146 C SER A 164 44.000 -0.555 29.820 1.00161.23 C ANISOU 1146 C SER A 164 29228 19707 12325 -9065 -2154 109 C ATOM 1147 O SER A 164 44.334 -1.623 30.340 1.00163.30 O ANISOU 1147 O SER A 164 29766 19937 12342 -8777 -2377 173 O ATOM 1148 CB SER A 164 44.917 -0.539 27.460 1.00157.44 C ANISOU 1148 CB SER A 164 27736 19764 12319 -8833 -2271 92 C ATOM 1149 OG SER A 164 45.672 0.654 27.591 1.00167.77 O ANISOU 1149 OG SER A 164 28785 21366 13595 -9120 -2374 -15 O ATOM 1150 N ALA A 165 43.883 0.594 30.509 1.00159.74 N ANISOU 1150 N ALA A 165 29161 19475 12057 -9422 -2059 32 N ATOM 1151 CA ALA A 165 44.100 0.727 31.940 1.00163.17 C ANISOU 1151 CA ALA A 165 30042 19830 12127 -9534 -2197 10 C ATOM 1152 C ALA A 165 42.730 0.752 32.664 1.00167.33 C ANISOU 1152 C ALA A 165 31117 19858 12604 -9711 -1814 31 C ATOM 1153 O ALA A 165 42.322 -0.268 33.226 1.00167.45 O ANISOU 1153 O ALA A 165 31510 19634 12481 -9493 -1786 98 O ATOM 1154 CB ALA A 165 44.906 1.990 32.234 1.00165.43 C ANISOU 1154 CB ALA A 165 30113 20404 12339 -9841 -2337 -108 C ATOM 1155 N GLY A 166 42.024 1.886 32.585 1.00163.09 N ANISOU 1155 N GLY A 166 30562 19186 12221 -10033 -1500 -41 N ATOM 1156 CA GLY A 166 40.722 2.108 33.215 1.00162.53 C ANISOU 1156 CA GLY A 166 30926 18705 12122 -10225 -1112 -64 C ATOM 1157 C GLY A 166 40.450 3.570 33.540 1.00164.36 C ANISOU 1157 C GLY A 166 30843 18955 12652 -10204 -907 -177 C ATOM 1158 O GLY A 166 41.364 4.404 33.473 1.00164.81 O ANISOU 1158 O GLY A 166 30587 19281 12754 -10229 -1096 -234 O ATOM 1159 N SER A 167 39.179 3.887 33.906 1.00160.77 N ANISOU 1159 N SER A 167 30921 18120 12044 -10600 -528 -214 N ATOM 1160 CA SER A 167 38.681 5.239 34.234 1.00159.48 C ANISOU 1160 CA SER A 167 30790 17849 11956 -10797 -290 -315 C ATOM 1161 C SER A 167 38.976 6.267 33.117 1.00161.43 C ANISOU 1161 C SER A 167 30773 18242 12321 -11032 -272 -360 C ATOM 1162 O SER A 167 39.465 7.370 33.380 1.00161.26 O ANISOU 1162 O SER A 167 30579 18318 12375 -11043 -319 -423 O ATOM 1163 CB SER A 167 39.182 5.706 35.601 1.00161.60 C ANISOU 1163 CB SER A 167 30740 18233 12429 -10287 -422 -353 C ATOM 1164 OG SER A 167 38.647 4.900 36.638 1.00166.46 O ANISOU 1164 OG SER A 167 31188 18769 13289 -9665 -339 -324 O ATOM 1165 N GLY A 168 38.677 5.865 31.880 1.00154.08 N ANISOU 1165 N GLY A 168 29503 17379 11662 -10864 -194 -331 N ATOM 1166 CA GLY A 168 38.867 6.668 30.679 1.00151.24 C ANISOU 1166 CA GLY A 168 28750 17166 11549 -10874 -154 -361 C ATOM 1167 C GLY A 168 38.201 6.032 29.480 1.00149.57 C ANISOU 1167 C GLY A 168 28234 16952 11644 -10622 -2 -335 C ATOM 1168 O GLY A 168 38.692 5.026 28.967 1.00149.49 O ANISOU 1168 O GLY A 168 27985 17107 11706 -10414 -193 -258 O ATOM 1169 N ASP A 169 37.070 6.612 29.029 1.00140.83 N ANISOU 1169 N ASP A 169 27137 15667 10704 -10619 335 -411 N ATOM 1170 CA ASP A 169 36.285 6.114 27.896 1.00135.77 C ANISOU 1170 CA ASP A 169 26212 15025 10350 -10389 508 -420 C ATOM 1171 C ASP A 169 36.966 6.271 26.539 1.00131.54 C ANISOU 1171 C ASP A 169 25236 14718 10026 -10266 369 -377 C ATOM 1172 O ASP A 169 37.316 7.377 26.123 1.00131.31 O ANISOU 1172 O ASP A 169 25138 14732 10023 -10376 378 -410 O ATOM 1173 CB ASP A 169 34.884 6.742 27.868 1.00137.07 C ANISOU 1173 CB ASP A 169 26499 14982 10601 -10394 886 -547 C ATOM 1174 CG ASP A 169 33.997 6.330 29.021 1.00149.44 C ANISOU 1174 CG ASP A 169 28433 16342 12006 -10483 1088 -610 C ATOM 1175 OD1 ASP A 169 33.783 5.106 29.202 1.00150.42 O ANISOU 1175 OD1 ASP A 169 28595 16446 12111 -10414 1081 -572 O ATOM 1176 OD2 ASP A 169 33.470 7.228 29.708 1.00157.62 O ANISOU 1176 OD2 ASP A 169 29737 17223 12928 -10621 1278 -706 O ATOM 1177 N VAL A 170 37.121 5.140 25.849 1.00122.09 N ANISOU 1177 N VAL A 170 23779 13645 8963 -10045 259 -308 N ATOM 1178 CA VAL A 170 37.695 4.999 24.515 1.00117.82 C ANISOU 1178 CA VAL A 170 22808 13325 8632 -9884 136 -263 C ATOM 1179 C VAL A 170 36.540 4.535 23.607 1.00114.27 C ANISOU 1179 C VAL A 170 22199 12788 8429 -9676 376 -300 C ATOM 1180 O VAL A 170 35.958 3.483 23.860 1.00112.83 O ANISOU 1180 O VAL A 170 22101 12521 8247 -9581 442 -295 O ATOM 1181 CB VAL A 170 38.925 4.041 24.580 1.00122.36 C ANISOU 1181 CB VAL A 170 23235 14140 9117 -9782 -218 -166 C ATOM 1182 CG1 VAL A 170 39.159 3.282 23.289 1.00120.22 C ANISOU 1182 CG1 VAL A 170 22568 14039 9070 -9524 -295 -114 C ATOM 1183 CG2 VAL A 170 40.183 4.796 24.987 1.00124.34 C ANISOU 1183 CG2 VAL A 170 23448 14601 9194 -9983 -462 -175 C ATOM 1184 N THR A 171 36.155 5.373 22.613 1.00107.25 N ANISOU 1184 N THR A 171 21128 11904 7718 -9623 521 -355 N ATOM 1185 CA THR A 171 35.058 5.124 21.661 1.00103.77 C ANISOU 1185 CA THR A 171 20501 11422 7506 -9412 736 -420 C ATOM 1186 C THR A 171 35.484 4.195 20.518 1.00102.52 C ANISOU 1186 C THR A 171 19977 11444 7530 -9198 595 -345 C ATOM 1187 O THR A 171 36.468 4.449 19.837 1.00 99.86 O ANISOU 1187 O THR A 171 19428 11278 7236 -9180 415 -279 O ATOM 1188 CB THR A 171 34.445 6.451 21.168 1.00109.28 C ANISOU 1188 CB THR A 171 21224 12031 8267 -9400 933 -517 C ATOM 1189 OG1 THR A 171 33.751 7.058 22.256 1.00112.53 O ANISOU 1189 OG1 THR A 171 21984 12252 8519 -9541 1113 -609 O ATOM 1190 CG2 THR A 171 33.467 6.266 20.014 1.00102.95 C ANISOU 1190 CG2 THR A 171 20169 11252 7697 -9134 1098 -593 C ATOM 1191 N ARG A 172 34.724 3.112 20.324 1.00 97.99 N ANISOU 1191 N ARG A 172 19345 10833 7053 -9057 695 -371 N ATOM 1192 CA ARG A 172 34.969 2.120 19.279 1.00 95.62 C ANISOU 1192 CA ARG A 172 18744 10669 6918 -8845 591 -312 C ATOM 1193 C ARG A 172 34.052 2.367 18.091 1.00 97.50 C ANISOU 1193 C ARG A 172 18729 10928 7388 -8676 777 -406 C ATOM 1194 O ARG A 172 32.930 2.844 18.273 1.00 97.20 O ANISOU 1194 O ARG A 172 18776 10785 7372 -8691 1018 -541 O ATOM 1195 CB ARG A 172 34.797 0.684 19.821 1.00 93.33 C ANISOU 1195 CB ARG A 172 18605 10310 6547 -8812 567 -279 C ATOM 1196 CG ARG A 172 35.608 0.348 21.075 1.00 92.58 C ANISOU 1196 CG ARG A 172 18823 10174 6181 -8930 376 -193 C ATOM 1197 CD ARG A 172 37.105 0.441 20.860 1.00 92.73 C ANISOU 1197 CD ARG A 172 18669 10418 6144 -8871 38 -84 C ATOM 1198 NE ARG A 172 37.839 -0.625 21.540 1.00101.74 N ANISOU 1198 NE ARG A 172 19991 11580 7084 -8787 -197 6 N ATOM 1199 CZ ARG A 172 39.166 -0.684 21.635 1.00109.80 C ANISOU 1199 CZ ARG A 172 20899 12828 7991 -8721 -521 76 C ATOM 1200 NH1 ARG A 172 39.921 0.265 21.094 1.00 93.25 N ANISOU 1200 NH1 ARG A 172 18499 10962 5969 -8789 -623 61 N ATOM 1201 NH2 ARG A 172 39.748 -1.702 22.255 1.00 89.84 N ANISOU 1201 NH2 ARG A 172 18569 10309 5256 -8580 -740 147 N ATOM 1202 N CYS A 173 34.544 2.053 16.873 1.00 92.47 N ANISOU 1202 N CYS A 173 17777 10447 6910 -8497 657 -346 N ATOM 1203 CA CYS A 173 33.847 2.222 15.591 1.00 89.87 C ANISOU 1203 CA CYS A 173 17185 10168 6795 -8298 779 -420 C ATOM 1204 C CYS A 173 33.594 0.847 14.944 1.00 92.73 C ANISOU 1204 C CYS A 173 17356 10594 7283 -8135 762 -413 C ATOM 1205 O CYS A 173 34.539 0.156 14.533 1.00 90.38 O ANISOU 1205 O CYS A 173 16930 10407 7002 -8053 558 -295 O ATOM 1206 CB CYS A 173 34.644 3.157 14.682 1.00 89.24 C ANISOU 1206 CB CYS A 173 16948 10191 6768 -8254 676 -363 C ATOM 1207 SG CYS A 173 33.855 3.537 13.093 1.00 91.32 S ANISOU 1207 SG CYS A 173 16955 10495 7248 -7981 807 -446 S ATOM 1208 N PHE A 174 32.298 0.441 14.922 1.00 91.64 N ANISOU 1208 N PHE A 174 17214 10392 7212 -8103 988 -558 N ATOM 1209 CA PHE A 174 31.755 -0.836 14.418 1.00 92.30 C ANISOU 1209 CA PHE A 174 17171 10502 7395 -8011 1047 -605 C ATOM 1210 C PHE A 174 32.327 -2.073 15.145 1.00100.79 C ANISOU 1210 C PHE A 174 18468 11499 8328 -8092 934 -497 C ATOM 1211 O PHE A 174 32.404 -3.153 14.545 1.00100.43 O ANISOU 1211 O PHE A 174 18331 11482 8346 -7980 886 -467 O ATOM 1212 CB PHE A 174 31.888 -0.978 12.873 1.00 92.43 C ANISOU 1212 CB PHE A 174 16832 10671 7615 -7768 974 -591 C ATOM 1213 CG PHE A 174 30.955 -0.106 12.066 1.00 92.96 C ANISOU 1213 CG PHE A 174 16711 10797 7814 -7629 1126 -742 C ATOM 1214 CD1 PHE A 174 29.596 -0.394 11.991 1.00 96.01 C ANISOU 1214 CD1 PHE A 174 17015 11203 8263 -7604 1347 -949 C ATOM 1215 CD2 PHE A 174 31.432 1.006 11.385 1.00 94.15 C ANISOU 1215 CD2 PHE A 174 16781 10993 8000 -7521 1049 -692 C ATOM 1216 CE1 PHE A 174 28.729 0.430 11.273 1.00 96.65 C ANISOU 1216 CE1 PHE A 174 16916 11368 8438 -7420 1461 -1108 C ATOM 1217 CE2 PHE A 174 30.564 1.823 10.662 1.00 96.78 C ANISOU 1217 CE2 PHE A 174 17004 11355 8413 -7343 1175 -830 C ATOM 1218 CZ PHE A 174 29.221 1.525 10.602 1.00 95.17 C ANISOU 1218 CZ PHE A 174 16697 11193 8271 -7264 1364 -1038 C ATOM 1219 N GLU A 175 32.663 -1.936 16.449 1.00101.19 N ANISOU 1219 N GLU A 175 18850 11433 8166 -8273 899 -449 N ATOM 1220 CA GLU A 175 33.248 -3.044 17.216 1.00103.54 C ANISOU 1220 CA GLU A 175 19430 11634 8277 -8313 769 -342 C ATOM 1221 C GLU A 175 32.256 -3.813 18.111 1.00113.66 C ANISOU 1221 C GLU A 175 21050 12711 9426 -8494 1008 -441 C ATOM 1222 O GLU A 175 32.533 -4.959 18.481 1.00112.08 O ANISOU 1222 O GLU A 175 21105 12395 9083 -8489 945 -369 O ATOM 1223 CB GLU A 175 34.453 -2.559 18.023 1.00105.57 C ANISOU 1223 CB GLU A 175 19841 11921 8349 -8366 522 -213 C ATOM 1224 CG GLU A 175 35.621 -2.190 17.128 1.00110.91 C ANISOU 1224 CG GLU A 175 20192 12826 9122 -8209 269 -115 C ATOM 1225 CD GLU A 175 36.997 -2.323 17.743 1.00124.51 C ANISOU 1225 CD GLU A 175 22000 14655 10653 -8193 -40 7 C ATOM 1226 OE1 GLU A 175 37.310 -3.398 18.303 1.00126.66 O ANISOU 1226 OE1 GLU A 175 22496 14864 10767 -8110 -161 72 O ATOM 1227 OE2 GLU A 175 37.793 -1.371 17.591 1.00106.63 O ANISOU 1227 OE2 GLU A 175 19572 12554 8387 -8250 -168 27 O ATOM 1228 N HIS A 176 31.099 -3.196 18.415 1.00117.75 N ANISOU 1228 N HIS A 176 21577 13186 9976 -8643 1290 -618 N ATOM 1229 CA HIS A 176 30.051 -3.762 19.266 1.00123.09 C ANISOU 1229 CA HIS A 176 22538 13701 10528 -8868 1573 -758 C ATOM 1230 C HIS A 176 28.817 -4.198 18.502 1.00130.95 C ANISOU 1230 C HIS A 176 23291 14771 11692 -8878 1838 -964 C ATOM 1231 O HIS A 176 28.482 -3.625 17.467 1.00129.34 O ANISOU 1231 O HIS A 176 22691 14748 11703 -8712 1852 -1047 O ATOM 1232 CB HIS A 176 29.628 -2.743 20.350 1.00126.38 C ANISOU 1232 CB HIS A 176 23154 14044 10821 -9056 1720 -842 C ATOM 1233 CG HIS A 176 28.563 -1.762 19.919 1.00130.38 C ANISOU 1233 CG HIS A 176 23381 14668 11488 -9030 1947 -1050 C ATOM 1234 ND1 HIS A 176 27.350 -1.672 20.590 1.00134.25 N ANISOU 1234 ND1 HIS A 176 23975 15116 11918 -9215 2272 -1268 N ATOM 1235 CD2 HIS A 176 28.562 -0.868 18.897 1.00131.18 C ANISOU 1235 CD2 HIS A 176 23132 14930 11781 -8819 1887 -1076 C ATOM 1236 CE1 HIS A 176 26.659 -0.732 19.960 1.00133.25 C ANISOU 1236 CE1 HIS A 176 23535 15145 11948 -9074 2378 -1425 C ATOM 1237 NE2 HIS A 176 27.343 -0.226 18.929 1.00131.69 N ANISOU 1237 NE2 HIS A 176 23085 15052 11897 -8828 2153 -1310 N ATOM 1238 N TYR A 177 28.095 -5.151 19.069 1.00132.97 N ANISOU 1238 N TYR A 177 23805 14892 11827 -9093 2063 -1069 N ATOM 1239 CA TYR A 177 26.830 -5.574 18.515 1.00135.34 C ANISOU 1239 CA TYR A 177 23886 15287 12251 -9181 2354 -1317 C ATOM 1240 C TYR A 177 25.781 -5.398 19.586 1.00146.13 C ANISOU 1240 C TYR A 177 25462 16584 13479 -9484 2688 -1525 C ATOM 1241 O TYR A 177 25.844 -6.032 20.651 1.00148.30 O ANISOU 1241 O TYR A 177 26207 16630 13509 -9723 2780 -1486 O ATOM 1242 CB TYR A 177 26.871 -7.009 17.968 1.00137.28 C ANISOU 1242 CB TYR A 177 24203 15466 12494 -9192 2357 -1294 C ATOM 1243 CG TYR A 177 27.801 -7.194 16.789 1.00137.71 C ANISOU 1243 CG TYR A 177 23994 15625 12706 -8873 2056 -1124 C ATOM 1244 CD1 TYR A 177 27.804 -6.291 15.726 1.00137.52 C ANISOU 1244 CD1 TYR A 177 23495 15836 12921 -8639 1963 -1154 C ATOM 1245 CD2 TYR A 177 28.640 -8.300 16.706 1.00139.15 C ANISOU 1245 CD2 TYR A 177 24424 15667 12781 -8791 1879 -945 C ATOM 1246 CE1 TYR A 177 28.667 -6.450 14.644 1.00136.12 C ANISOU 1246 CE1 TYR A 177 23087 15756 12875 -8367 1707 -1003 C ATOM 1247 CE2 TYR A 177 29.485 -8.486 15.614 1.00138.35 C ANISOU 1247 CE2 TYR A 177 24063 15684 12820 -8492 1616 -806 C ATOM 1248 CZ TYR A 177 29.500 -7.554 14.589 1.00143.13 C ANISOU 1248 CZ TYR A 177 24183 16530 13669 -8299 1539 -836 C ATOM 1249 OH TYR A 177 30.336 -7.730 13.516 1.00143.60 O ANISOU 1249 OH TYR A 177 23999 16707 13856 -8026 1302 -706 O ATOM 1250 N GLU A 178 24.866 -4.454 19.337 1.00144.89 N ANISOU 1250 N GLU A 178 24976 16623 13454 -9449 2859 -1744 N ATOM 1251 CA GLU A 178 23.741 -4.186 20.227 1.00147.67 C ANISOU 1251 CA GLU A 178 25425 16982 13701 -9706 3204 -1995 C ATOM 1252 C GLU A 178 22.679 -5.240 19.889 1.00152.44 C ANISOU 1252 C GLU A 178 25906 17678 14338 -9914 3497 -2250 C ATOM 1253 O GLU A 178 21.997 -5.144 18.859 1.00151.24 O ANISOU 1253 O GLU A 178 25283 17793 14390 -9777 3562 -2445 O ATOM 1254 CB GLU A 178 23.220 -2.727 20.108 1.00148.95 C ANISOU 1254 CB GLU A 178 25300 17329 13966 -9535 3254 -2140 C ATOM 1255 CG GLU A 178 23.300 -2.105 18.715 1.00158.79 C ANISOU 1255 CG GLU A 178 26076 18798 15459 -9166 3084 -2148 C ATOM 1256 CD GLU A 178 22.025 -1.518 18.134 1.00180.13 C ANISOU 1256 CD GLU A 178 28362 21786 18295 -9029 3292 -2478 C ATOM 1257 OE1 GLU A 178 20.924 -1.813 18.654 1.00179.68 O ANISOU 1257 OE1 GLU A 178 28278 21820 18173 -9250 3607 -2756 O ATOM 1258 OE2 GLU A 178 22.129 -0.807 17.109 1.00170.26 O ANISOU 1258 OE2 GLU A 178 26805 20684 17203 -8692 3139 -2471 O ATOM 1259 N LYS A 179 22.626 -6.305 20.720 1.00150.43 N ANISOU 1259 N LYS A 179 26109 17188 13860 -10243 3657 -2237 N ATOM 1260 CA LYS A 179 21.719 -7.445 20.568 1.00151.80 C ANISOU 1260 CA LYS A 179 26298 17381 13997 -10540 3965 -2467 C ATOM 1261 C LYS A 179 20.244 -7.023 20.539 1.00156.65 C ANISOU 1261 C LYS A 179 26526 18300 14694 -10702 4331 -2881 C ATOM 1262 O LYS A 179 19.425 -7.701 19.911 1.00157.86 O ANISOU 1262 O LYS A 179 26424 18631 14924 -10849 4537 -3131 O ATOM 1263 CB LYS A 179 21.966 -8.473 21.683 1.00156.86 C ANISOU 1263 CB LYS A 179 27629 17653 14315 -10882 4092 -2368 C ATOM 1264 N GLY A 180 19.954 -5.891 21.188 1.00152.16 N ANISOU 1264 N GLY A 180 25910 17806 14100 -10658 4395 -2958 N ATOM 1265 CA GLY A 180 18.636 -5.282 21.333 1.00153.16 C ANISOU 1265 CA GLY A 180 25689 18234 14272 -10745 4716 -3347 C ATOM 1266 C GLY A 180 17.794 -5.033 20.093 1.00154.24 C ANISOU 1266 C GLY A 180 25156 18792 14657 -10527 4759 -3634 C ATOM 1267 O GLY A 180 16.774 -5.702 19.916 1.00156.99 O ANISOU 1267 O GLY A 180 25294 19346 15008 -10791 5060 -3961 O ATOM 1268 N SER A 181 18.168 -4.043 19.253 1.00145.25 N ANISOU 1268 N SER A 181 23689 17796 13705 -10059 4474 -3538 N ATOM 1269 CA SER A 181 17.361 -3.639 18.095 1.00143.56 C ANISOU 1269 CA SER A 181 22858 17988 13702 -9771 4482 -3811 C ATOM 1270 C SER A 181 17.797 -4.169 16.727 1.00141.16 C ANISOU 1270 C SER A 181 22301 17753 13581 -9544 4238 -3696 C ATOM 1271 O SER A 181 16.927 -4.401 15.883 1.00141.35 O ANISOU 1271 O SER A 181 21865 18110 13730 -9476 4334 -3987 O ATOM 1272 CB SER A 181 17.260 -2.118 18.026 1.00147.16 C ANISOU 1272 CB SER A 181 23133 18574 14209 -9378 4380 -3848 C ATOM 1273 OG SER A 181 16.586 -1.582 19.153 1.00159.15 O ANISOU 1273 OG SER A 181 24774 20121 15575 -9552 4651 -4052 O ATOM 1274 N VAL A 182 19.112 -4.300 16.471 1.00132.00 N ANISOU 1274 N VAL A 182 21398 16320 12435 -9403 3920 -3298 N ATOM 1275 CA VAL A 182 19.581 -4.736 15.150 1.00128.10 C ANISOU 1275 CA VAL A 182 20665 15895 12113 -9162 3685 -3182 C ATOM 1276 C VAL A 182 19.706 -6.276 15.042 1.00127.86 C ANISOU 1276 C VAL A 182 20818 15731 12030 -9458 3758 -3151 C ATOM 1277 O VAL A 182 20.416 -6.886 15.849 1.00127.72 O ANISOU 1277 O VAL A 182 21297 15389 11842 -9670 3735 -2929 O ATOM 1278 CB VAL A 182 20.864 -4.006 14.649 1.00129.32 C ANISOU 1278 CB VAL A 182 20885 15913 12339 -8802 3305 -2824 C ATOM 1279 CG1 VAL A 182 20.555 -2.566 14.260 1.00128.79 C ANISOU 1279 CG1 VAL A 182 20553 16025 12355 -8450 3241 -2914 C ATOM 1280 CG2 VAL A 182 22.000 -4.055 15.669 1.00128.71 C ANISOU 1280 CG2 VAL A 182 21322 15492 12089 -8944 3176 -2505 C ATOM 1281 N PRO A 183 19.026 -6.920 14.047 1.00120.97 N ANISOU 1281 N PRO A 183 19581 15099 11282 -9462 3840 -3377 N ATOM 1282 CA PRO A 183 19.157 -8.383 13.889 1.00119.56 C ANISOU 1282 CA PRO A 183 19625 14765 11037 -9744 3915 -3347 C ATOM 1283 C PRO A 183 20.459 -8.784 13.177 1.00114.73 C ANISOU 1283 C PRO A 183 19159 13950 10484 -9484 3564 -2977 C ATOM 1284 O PRO A 183 20.439 -9.242 12.031 1.00113.15 O ANISOU 1284 O PRO A 183 18691 13879 10421 -9341 3473 -3012 O ATOM 1285 CB PRO A 183 17.894 -8.774 13.110 1.00123.30 C ANISOU 1285 CB PRO A 183 19617 15614 11617 -9852 4140 -3765 C ATOM 1286 CG PRO A 183 17.495 -7.545 12.375 1.00127.14 C ANISOU 1286 CG PRO A 183 19573 16450 12285 -9421 4011 -3900 C ATOM 1287 CD PRO A 183 18.141 -6.346 13.008 1.00122.00 C ANISOU 1287 CD PRO A 183 19111 15648 11597 -9190 3852 -3669 C ATOM 1288 N VAL A 184 21.597 -8.607 13.890 1.00105.71 N ANISOU 1288 N VAL A 184 18435 12508 9223 -9426 3368 -2637 N ATOM 1289 CA VAL A 184 22.980 -8.883 13.475 1.00101.15 C ANISOU 1289 CA VAL A 184 18032 11743 8657 -9179 3024 -2275 C ATOM 1290 C VAL A 184 23.118 -10.259 12.829 1.00 99.93 C ANISOU 1290 C VAL A 184 17983 11495 8490 -9248 3022 -2251 C ATOM 1291 O VAL A 184 23.573 -10.361 11.692 1.00 96.99 O ANISOU 1291 O VAL A 184 17359 11220 8274 -8968 2815 -2160 O ATOM 1292 CB VAL A 184 23.968 -8.711 14.669 1.00105.37 C ANISOU 1292 CB VAL A 184 19063 11984 8987 -9227 2892 -1999 C ATOM 1293 CG1 VAL A 184 25.403 -9.033 14.264 1.00103.45 C ANISOU 1293 CG1 VAL A 184 18960 11606 8740 -8965 2534 -1662 C ATOM 1294 CG2 VAL A 184 23.886 -7.311 15.263 1.00104.92 C ANISOU 1294 CG2 VAL A 184 18921 12005 8939 -9156 2883 -2015 C ATOM 1295 N LEU A 185 22.707 -11.305 13.560 1.00 95.83 N ANISOU 1295 N LEU A 185 17873 10772 7767 -9632 3270 -2340 N ATOM 1296 CA LEU A 185 22.775 -12.703 13.161 1.00 94.62 C ANISOU 1296 CA LEU A 185 17967 10452 7531 -9769 3324 -2330 C ATOM 1297 C LEU A 185 22.300 -12.986 11.743 1.00 93.83 C ANISOU 1297 C LEU A 185 17390 10616 7647 -9650 3318 -2500 C ATOM 1298 O LEU A 185 23.085 -13.515 10.965 1.00 92.09 O ANISOU 1298 O LEU A 185 17201 10315 7475 -9412 3090 -2307 O ATOM 1299 CB LEU A 185 22.026 -13.579 14.165 1.00 98.21 C ANISOU 1299 CB LEU A 185 18888 10699 7728 -10283 3699 -2508 C ATOM 1300 CG LEU A 185 22.832 -14.058 15.359 1.00104.39 C ANISOU 1300 CG LEU A 185 20397 11058 8207 -10381 3648 -2249 C ATOM 1301 CD1 LEU A 185 21.926 -14.336 16.556 1.00108.38 C ANISOU 1301 CD1 LEU A 185 21280 11426 8474 -10890 4053 -2462 C ATOM 1302 CD2 LEU A 185 23.687 -15.276 15.008 1.00106.06 C ANISOU 1302 CD2 LEU A 185 21038 10975 8286 -10268 3481 -2025 C ATOM 1303 N ILE A 186 21.053 -12.619 11.388 1.00 89.03 N ANISOU 1303 N ILE A 186 16325 10342 7160 -9782 3550 -2865 N ATOM 1304 CA ILE A 186 20.506 -12.915 10.060 1.00 87.84 C ANISOU 1304 CA ILE A 186 15709 10471 7193 -9684 3552 -3068 C ATOM 1305 C ILE A 186 21.187 -12.095 8.958 1.00 88.42 C ANISOU 1305 C ILE A 186 15394 10710 7491 -9156 3197 -2890 C ATOM 1306 O ILE A 186 21.477 -12.659 7.901 1.00 86.91 O ANISOU 1306 O ILE A 186 15084 10547 7392 -8997 3064 -2838 O ATOM 1307 CB ILE A 186 18.956 -12.839 10.000 1.00 93.14 C ANISOU 1307 CB ILE A 186 15982 11502 7906 -9974 3894 -3549 C ATOM 1308 CG1 ILE A 186 18.410 -13.641 8.805 1.00 93.92 C ANISOU 1308 CG1 ILE A 186 15778 11805 8103 -10029 3950 -3775 C ATOM 1309 CG2 ILE A 186 18.389 -11.408 10.059 1.00 92.99 C ANISOU 1309 CG2 ILE A 186 15498 11820 8014 -9744 3880 -3712 C ATOM 1310 CD1 ILE A 186 18.220 -15.095 9.109 1.00102.36 C ANISOU 1310 CD1 ILE A 186 17307 12614 8970 -10507 4199 -3847 C ATOM 1311 N ILE A 187 21.461 -10.792 9.222 1.00 82.36 N ANISOU 1311 N ILE A 187 14481 10025 6788 -8906 3058 -2794 N ATOM 1312 CA ILE A 187 22.132 -9.875 8.313 1.00 78.96 C ANISOU 1312 CA ILE A 187 13758 9715 6530 -8444 2752 -2620 C ATOM 1313 C ILE A 187 23.514 -10.444 7.971 1.00 83.55 C ANISOU 1313 C ILE A 187 14595 10058 7093 -8272 2480 -2261 C ATOM 1314 O ILE A 187 23.857 -10.538 6.786 1.00 83.17 O ANISOU 1314 O ILE A 187 14305 10114 7183 -8006 2307 -2201 O ATOM 1315 CB ILE A 187 22.190 -8.441 8.917 1.00 81.27 C ANISOU 1315 CB ILE A 187 13996 10057 6825 -8298 2704 -2581 C ATOM 1316 CG1 ILE A 187 20.769 -7.830 9.049 1.00 83.50 C ANISOU 1316 CG1 ILE A 187 13944 10641 7141 -8367 2951 -2971 C ATOM 1317 CG2 ILE A 187 23.122 -7.519 8.114 1.00 79.08 C ANISOU 1317 CG2 ILE A 187 13562 9814 6671 -7875 2390 -2345 C ATOM 1318 CD1 ILE A 187 20.638 -6.529 9.947 1.00 83.51 C ANISOU 1318 CD1 ILE A 187 14001 10646 7083 -8305 2986 -2979 C ATOM 1319 N HIS A 188 24.273 -10.881 8.996 1.00 81.20 N ANISOU 1319 N HIS A 188 14788 9456 6607 -8415 2446 -2044 N ATOM 1320 CA HIS A 188 25.611 -11.463 8.833 1.00 80.62 C ANISOU 1320 CA HIS A 188 14981 9174 6475 -8236 2183 -1722 C ATOM 1321 C HIS A 188 25.594 -12.794 8.103 1.00 81.47 C ANISOU 1321 C HIS A 188 15182 9204 6569 -8267 2207 -1745 C ATOM 1322 O HIS A 188 26.426 -12.988 7.212 1.00 77.14 O ANISOU 1322 O HIS A 188 14536 8670 6103 -7974 1971 -1571 O ATOM 1323 CB HIS A 188 26.325 -11.576 10.178 1.00 83.97 C ANISOU 1323 CB HIS A 188 15911 9324 6671 -8357 2137 -1524 C ATOM 1324 CG HIS A 188 26.846 -10.266 10.678 1.00 87.78 C ANISOU 1324 CG HIS A 188 16316 9864 7173 -8226 1993 -1404 C ATOM 1325 ND1 HIS A 188 28.122 -10.152 11.189 1.00 89.96 N ANISOU 1325 ND1 HIS A 188 16841 10004 7335 -8096 1740 -1126 N ATOM 1326 CD2 HIS A 188 26.258 -9.043 10.693 1.00 90.09 C ANISOU 1326 CD2 HIS A 188 16318 10342 7571 -8200 2066 -1539 C ATOM 1327 CE1 HIS A 188 28.262 -8.878 11.521 1.00 89.09 C ANISOU 1327 CE1 HIS A 188 16596 9988 7265 -8046 1685 -1104 C ATOM 1328 NE2 HIS A 188 27.168 -8.171 11.234 1.00 89.31 N ANISOU 1328 NE2 HIS A 188 16326 10189 7420 -8093 1877 -1338 N ATOM 1329 N ILE A 189 24.621 -13.697 8.463 1.00 79.92 N ANISOU 1329 N ILE A 189 15179 8930 6259 -8645 2513 -1978 N ATOM 1330 CA ILE A 189 24.399 -15.016 7.844 1.00 79.95 C ANISOU 1330 CA ILE A 189 15326 8835 6215 -8767 2606 -2056 C ATOM 1331 C ILE A 189 24.080 -14.829 6.341 1.00 82.25 C ANISOU 1331 C ILE A 189 15066 9434 6753 -8538 2524 -2183 C ATOM 1332 O ILE A 189 24.786 -15.389 5.497 1.00 80.63 O ANISOU 1332 O ILE A 189 14881 9168 6586 -8309 2340 -2029 O ATOM 1333 CB ILE A 189 23.334 -15.844 8.614 1.00 85.84 C ANISOU 1333 CB ILE A 189 16391 9453 6770 -9292 2996 -2318 C ATOM 1334 CG1 ILE A 189 23.919 -16.421 9.924 1.00 87.02 C ANISOU 1334 CG1 ILE A 189 17260 9189 6617 -9464 3030 -2119 C ATOM 1335 CG2 ILE A 189 22.795 -16.969 7.749 1.00 88.20 C ANISOU 1335 CG2 ILE A 189 16683 9760 7070 -9459 3140 -2502 C ATOM 1336 CD1 ILE A 189 22.902 -16.955 10.933 1.00 85.45 C ANISOU 1336 CD1 ILE A 189 17422 8846 6198 -10012 3438 -2362 C ATOM 1337 N PHE A 190 23.078 -13.975 6.021 1.00 78.85 N ANISOU 1337 N PHE A 190 14146 9338 6473 -8552 2638 -2455 N ATOM 1338 CA PHE A 190 22.704 -13.635 4.653 1.00 77.86 C ANISOU 1338 CA PHE A 190 13493 9530 6562 -8299 2548 -2594 C ATOM 1339 C PHE A 190 23.946 -13.198 3.817 1.00 77.57 C ANISOU 1339 C PHE A 190 13358 9475 6641 -7837 2194 -2278 C ATOM 1340 O PHE A 190 24.263 -13.853 2.821 1.00 74.52 O ANISOU 1340 O PHE A 190 12911 9092 6312 -7694 2091 -2231 O ATOM 1341 CB PHE A 190 21.563 -12.580 4.626 1.00 81.03 C ANISOU 1341 CB PHE A 190 13430 10289 7068 -8297 2679 -2907 C ATOM 1342 CG PHE A 190 21.318 -11.963 3.266 1.00 82.51 C ANISOU 1342 CG PHE A 190 13101 10795 7453 -7925 2522 -3006 C ATOM 1343 CD1 PHE A 190 20.581 -12.638 2.300 1.00 87.33 C ANISOU 1343 CD1 PHE A 190 13440 11614 8129 -7974 2594 -3260 C ATOM 1344 CD2 PHE A 190 21.885 -10.738 2.927 1.00 83.99 C ANISOU 1344 CD2 PHE A 190 13123 11051 7738 -7530 2295 -2835 C ATOM 1345 CE1 PHE A 190 20.412 -12.099 1.022 1.00 87.68 C ANISOU 1345 CE1 PHE A 190 13048 11936 8332 -7600 2425 -3337 C ATOM 1346 CE2 PHE A 190 21.720 -10.201 1.644 1.00 85.98 C ANISOU 1346 CE2 PHE A 190 12979 11551 8138 -7168 2144 -2905 C ATOM 1347 CZ PHE A 190 20.987 -10.886 0.700 1.00 85.15 C ANISOU 1347 CZ PHE A 190 12602 11656 8094 -7188 2201 -3152 C ATOM 1348 N ILE A 191 24.666 -12.144 4.260 1.00 73.86 N ANISOU 1348 N ILE A 191 12902 8977 6184 -7641 2029 -2070 N ATOM 1349 CA ILE A 191 25.849 -11.631 3.548 1.00 72.43 C ANISOU 1349 CA ILE A 191 12623 8803 6095 -7261 1727 -1795 C ATOM 1350 C ILE A 191 26.939 -12.698 3.342 1.00 78.66 C ANISOU 1350 C ILE A 191 13699 9380 6807 -7179 1572 -1555 C ATOM 1351 O ILE A 191 27.408 -12.870 2.211 1.00 78.62 O ANISOU 1351 O ILE A 191 13510 9454 6907 -6924 1418 -1478 O ATOM 1352 CB ILE A 191 26.449 -10.328 4.170 1.00 74.08 C ANISOU 1352 CB ILE A 191 12843 9007 6297 -7140 1605 -1634 C ATOM 1353 CG1 ILE A 191 25.433 -9.140 4.192 1.00 75.05 C ANISOU 1353 CG1 ILE A 191 12675 9346 6496 -7115 1724 -1861 C ATOM 1354 CG2 ILE A 191 27.764 -9.934 3.498 1.00 70.75 C ANISOU 1354 CG2 ILE A 191 12360 8585 5936 -6826 1321 -1359 C ATOM 1355 CD1 ILE A 191 24.841 -8.632 2.829 1.00 78.72 C ANISOU 1355 CD1 ILE A 191 12700 10086 7126 -6837 1682 -2027 C ATOM 1356 N VAL A 192 27.355 -13.388 4.414 1.00 76.40 N ANISOU 1356 N VAL A 192 13878 8828 6323 -7361 1605 -1438 N ATOM 1357 CA VAL A 192 28.400 -14.410 4.306 1.00 76.16 C ANISOU 1357 CA VAL A 192 14166 8591 6180 -7231 1445 -1217 C ATOM 1358 C VAL A 192 27.969 -15.510 3.316 1.00 80.88 C ANISOU 1358 C VAL A 192 14743 9179 6810 -7247 1524 -1339 C ATOM 1359 O VAL A 192 28.794 -15.929 2.500 1.00 80.01 O ANISOU 1359 O VAL A 192 14603 9060 6736 -6970 1333 -1187 O ATOM 1360 CB VAL A 192 28.883 -14.953 5.681 1.00 81.30 C ANISOU 1360 CB VAL A 192 15375 8944 6570 -7385 1454 -1079 C ATOM 1361 CG1 VAL A 192 29.924 -16.053 5.504 1.00 81.49 C ANISOU 1361 CG1 VAL A 192 15740 8768 6455 -7182 1275 -874 C ATOM 1362 CG2 VAL A 192 29.451 -13.831 6.551 1.00 80.12 C ANISOU 1362 CG2 VAL A 192 15215 8831 6395 -7333 1331 -945 C ATOM 1363 N PHE A 193 26.674 -15.902 3.320 1.00 78.33 N ANISOU 1363 N PHE A 193 14386 8895 6480 -7570 1807 -1633 N ATOM 1364 CA PHE A 193 26.189 -16.891 2.367 1.00 79.16 C ANISOU 1364 CA PHE A 193 14451 9016 6612 -7631 1898 -1786 C ATOM 1365 C PHE A 193 26.118 -16.321 0.930 1.00 79.69 C ANISOU 1365 C PHE A 193 13970 9390 6917 -7328 1759 -1844 C ATOM 1366 O PHE A 193 26.461 -17.031 -0.032 1.00 78.94 O ANISOU 1366 O PHE A 193 13870 9273 6853 -7175 1671 -1802 O ATOM 1367 CB PHE A 193 24.857 -17.490 2.813 1.00 84.57 C ANISOU 1367 CB PHE A 193 15249 9685 7201 -8110 2252 -2113 C ATOM 1368 CG PHE A 193 24.972 -18.667 3.756 1.00 90.10 C ANISOU 1368 CG PHE A 193 16625 9991 7617 -8413 2410 -2061 C ATOM 1369 CD1 PHE A 193 24.720 -18.517 5.116 1.00 94.73 C ANISOU 1369 CD1 PHE A 193 17536 10424 8035 -8702 2578 -2081 C ATOM 1370 CD2 PHE A 193 25.268 -19.939 3.277 1.00 95.18 C ANISOU 1370 CD2 PHE A 193 17624 10400 8140 -8418 2411 -2010 C ATOM 1371 CE1 PHE A 193 24.788 -19.610 5.985 1.00 98.46 C ANISOU 1371 CE1 PHE A 193 18698 10504 8210 -8985 2738 -2038 C ATOM 1372 CE2 PHE A 193 25.324 -21.038 4.150 1.00101.27 C ANISOU 1372 CE2 PHE A 193 19102 10767 8607 -8694 2574 -1970 C ATOM 1373 CZ PHE A 193 25.092 -20.861 5.501 1.00100.14 C ANISOU 1373 CZ PHE A 193 19296 10466 8289 -8974 2735 -1980 C ATOM 1374 N SER A 194 25.724 -15.023 0.791 1.00 72.89 N ANISOU 1374 N SER A 194 12696 8794 6204 -7216 1731 -1929 N ATOM 1375 CA SER A 194 25.677 -14.330 -0.504 1.00 69.15 C ANISOU 1375 CA SER A 194 11759 8592 5925 -6896 1589 -1969 C ATOM 1376 C SER A 194 27.076 -14.285 -1.091 1.00 69.62 C ANISOU 1376 C SER A 194 11864 8571 6017 -6551 1316 -1652 C ATOM 1377 O SER A 194 27.230 -14.590 -2.275 1.00 68.85 O ANISOU 1377 O SER A 194 11591 8561 6007 -6352 1225 -1653 O ATOM 1378 CB SER A 194 25.098 -12.929 -0.370 1.00 70.22 C ANISOU 1378 CB SER A 194 11570 8958 6153 -6814 1605 -2088 C ATOM 1379 OG SER A 194 23.744 -12.970 0.052 1.00 79.85 O ANISOU 1379 OG SER A 194 12665 10324 7350 -7098 1858 -2428 O ATOM 1380 N PHE A 195 28.110 -14.027 -0.252 1.00 65.07 N ANISOU 1380 N PHE A 195 11536 7836 5352 -6499 1193 -1397 N ATOM 1381 CA PHE A 195 29.500 -14.063 -0.709 1.00 64.02 C ANISOU 1381 CA PHE A 195 11434 7664 5227 -6198 943 -1120 C ATOM 1382 C PHE A 195 29.881 -15.454 -1.212 1.00 68.63 C ANISOU 1382 C PHE A 195 12233 8103 5740 -6136 909 -1067 C ATOM 1383 O PHE A 195 30.452 -15.563 -2.293 1.00 66.94 O ANISOU 1383 O PHE A 195 11844 7979 5613 -5869 768 -987 O ATOM 1384 CB PHE A 195 30.488 -13.641 0.379 1.00 66.20 C ANISOU 1384 CB PHE A 195 11934 7829 5389 -6186 821 -901 C ATOM 1385 CG PHE A 195 31.932 -13.967 0.047 1.00 68.11 C ANISOU 1385 CG PHE A 195 12236 8047 5594 -5909 578 -654 C ATOM 1386 CD1 PHE A 195 32.716 -13.074 -0.676 1.00 70.09 C ANISOU 1386 CD1 PHE A 195 12184 8486 5959 -5672 412 -543 C ATOM 1387 CD2 PHE A 195 32.512 -15.163 0.468 1.00 72.78 C ANISOU 1387 CD2 PHE A 195 13206 8433 6014 -5880 521 -546 C ATOM 1388 CE1 PHE A 195 34.058 -13.367 -0.966 1.00 71.39 C ANISOU 1388 CE1 PHE A 195 12357 8682 6084 -5432 201 -348 C ATOM 1389 CE2 PHE A 195 33.850 -15.462 0.162 1.00 75.89 C ANISOU 1389 CE2 PHE A 195 13619 8853 6362 -5579 285 -345 C ATOM 1390 CZ PHE A 195 34.618 -14.556 -0.540 1.00 72.24 C ANISOU 1390 CZ PHE A 195 12789 8627 6031 -5369 129 -256 C ATOM 1391 N PHE A 196 29.599 -16.512 -0.424 1.00 67.06 N ANISOU 1391 N PHE A 196 12456 7662 5363 -6378 1044 -1106 N ATOM 1392 CA PHE A 196 29.996 -17.862 -0.816 1.00 67.06 C ANISOU 1392 CA PHE A 196 12760 7469 5252 -6309 1018 -1047 C ATOM 1393 C PHE A 196 29.277 -18.335 -2.071 1.00 70.31 C ANISOU 1393 C PHE A 196 12945 7993 5775 -6316 1104 -1238 C ATOM 1394 O PHE A 196 29.906 -19.042 -2.870 1.00 69.90 O ANISOU 1394 O PHE A 196 12963 7884 5712 -6093 989 -1141 O ATOM 1395 CB PHE A 196 29.918 -18.850 0.341 1.00 70.84 C ANISOU 1395 CB PHE A 196 13831 7614 5470 -6555 1144 -1030 C ATOM 1396 CG PHE A 196 31.119 -18.697 1.252 1.00 71.93 C ANISOU 1396 CG PHE A 196 14236 7628 5464 -6369 941 -766 C ATOM 1397 CD1 PHE A 196 32.398 -19.021 0.809 1.00 74.48 C ANISOU 1397 CD1 PHE A 196 14598 7949 5753 -5980 679 -550 C ATOM 1398 CD2 PHE A 196 30.978 -18.200 2.539 1.00 73.86 C ANISOU 1398 CD2 PHE A 196 14665 7796 5604 -6572 1005 -754 C ATOM 1399 CE1 PHE A 196 33.511 -18.859 1.645 1.00 75.37 C ANISOU 1399 CE1 PHE A 196 14904 8011 5724 -5793 473 -341 C ATOM 1400 CE2 PHE A 196 32.092 -18.048 3.377 1.00 76.77 C ANISOU 1400 CE2 PHE A 196 15263 8079 5825 -6394 798 -528 C ATOM 1401 CZ PHE A 196 33.349 -18.384 2.926 1.00 74.55 C ANISOU 1401 CZ PHE A 196 14992 7825 5509 -6004 527 -331 C ATOM 1402 N LEU A 197 28.033 -17.841 -2.321 1.00 66.47 N ANISOU 1402 N LEU A 197 12139 7712 5404 -6520 1276 -1513 N ATOM 1403 CA LEU A 197 27.320 -18.120 -3.574 1.00 66.21 C ANISOU 1403 CA LEU A 197 11810 7858 5487 -6497 1327 -1721 C ATOM 1404 C LEU A 197 28.155 -17.515 -4.725 1.00 71.26 C ANISOU 1404 C LEU A 197 12134 8663 6278 -6064 1080 -1558 C ATOM 1405 O LEU A 197 28.500 -18.231 -5.666 1.00 70.17 O ANISOU 1405 O LEU A 197 12014 8498 6151 -5906 1009 -1523 O ATOM 1406 CB LEU A 197 25.890 -17.524 -3.562 1.00 66.15 C ANISOU 1406 CB LEU A 197 11458 8110 5566 -6735 1521 -2060 C ATOM 1407 CG LEU A 197 25.150 -17.457 -4.925 1.00 69.18 C ANISOU 1407 CG LEU A 197 11411 8782 6091 -6627 1515 -2293 C ATOM 1408 CD1 LEU A 197 25.052 -18.818 -5.600 1.00 70.14 C ANISOU 1408 CD1 LEU A 197 11722 8784 6143 -6735 1578 -2373 C ATOM 1409 CD2 LEU A 197 23.767 -16.845 -4.787 1.00 70.94 C ANISOU 1409 CD2 LEU A 197 11279 9303 6372 -6819 1685 -2647 C ATOM 1410 N VAL A 198 28.516 -16.207 -4.597 1.00 68.88 N ANISOU 1410 N VAL A 198 11591 8510 6071 -5894 964 -1455 N ATOM 1411 CA VAL A 198 29.337 -15.451 -5.553 1.00 67.13 C ANISOU 1411 CA VAL A 198 11103 8435 5968 -5532 758 -1298 C ATOM 1412 C VAL A 198 30.681 -16.156 -5.734 1.00 73.97 C ANISOU 1412 C VAL A 198 12181 9160 6765 -5326 595 -1044 C ATOM 1413 O VAL A 198 31.003 -16.502 -6.867 1.00 74.68 O ANISOU 1413 O VAL A 198 12151 9310 6912 -5113 513 -1019 O ATOM 1414 CB VAL A 198 29.459 -13.932 -5.210 1.00 68.38 C ANISOU 1414 CB VAL A 198 11065 8724 6191 -5457 703 -1244 C ATOM 1415 CG1 VAL A 198 30.365 -13.199 -6.191 1.00 65.76 C ANISOU 1415 CG1 VAL A 198 10528 8512 5947 -5133 522 -1082 C ATOM 1416 CG2 VAL A 198 28.086 -13.267 -5.179 1.00 68.64 C ANISOU 1416 CG2 VAL A 198 10871 8928 6283 -5580 852 -1523 C ATOM 1417 N PHE A 199 31.403 -16.469 -4.635 1.00 71.90 N ANISOU 1417 N PHE A 199 12244 8714 6361 -5380 551 -881 N ATOM 1418 CA PHE A 199 32.675 -17.192 -4.710 1.00 72.70 C ANISOU 1418 CA PHE A 199 12554 8706 6364 -5146 382 -664 C ATOM 1419 C PHE A 199 32.540 -18.527 -5.458 1.00 78.96 C ANISOU 1419 C PHE A 199 13530 9371 7102 -5090 419 -718 C ATOM 1420 O PHE A 199 33.422 -18.854 -6.251 1.00 79.77 O ANISOU 1420 O PHE A 199 13579 9513 7216 -4793 271 -595 O ATOM 1421 CB PHE A 199 33.319 -17.402 -3.328 1.00 75.69 C ANISOU 1421 CB PHE A 199 13293 8907 6560 -5207 329 -520 C ATOM 1422 CG PHE A 199 34.494 -18.362 -3.335 1.00 78.70 C ANISOU 1422 CG PHE A 199 13942 9169 6793 -4939 159 -340 C ATOM 1423 CD1 PHE A 199 35.674 -18.045 -4.006 1.00 80.97 C ANISOU 1423 CD1 PHE A 199 13981 9645 7138 -4606 -50 -194 C ATOM 1424 CD2 PHE A 199 34.410 -19.597 -2.697 1.00 83.57 C ANISOU 1424 CD2 PHE A 199 15077 9486 7191 -5011 218 -334 C ATOM 1425 CE1 PHE A 199 36.755 -18.937 -4.018 1.00 83.32 C ANISOU 1425 CE1 PHE A 199 14494 9876 7289 -4314 -216 -54 C ATOM 1426 CE2 PHE A 199 35.495 -20.488 -2.709 1.00 87.66 C ANISOU 1426 CE2 PHE A 199 15872 9890 7543 -4697 44 -175 C ATOM 1427 CZ PHE A 199 36.662 -20.149 -3.363 1.00 84.58 C ANISOU 1427 CZ PHE A 199 15179 9732 7225 -4333 -181 -42 C ATOM 1428 N LEU A 200 31.447 -19.279 -5.222 1.00 75.22 N ANISOU 1428 N LEU A 200 13271 8751 6557 -5389 628 -913 N ATOM 1429 CA LEU A 200 31.227 -20.558 -5.890 1.00 75.85 C ANISOU 1429 CA LEU A 200 13576 8683 6562 -5397 694 -990 C ATOM 1430 C LEU A 200 31.125 -20.378 -7.395 1.00 76.78 C ANISOU 1430 C LEU A 200 13305 9019 6850 -5195 633 -1059 C ATOM 1431 O LEU A 200 31.750 -21.129 -8.143 1.00 76.25 O ANISOU 1431 O LEU A 200 13342 8884 6745 -4966 543 -974 O ATOM 1432 CB LEU A 200 29.972 -21.246 -5.340 1.00 78.07 C ANISOU 1432 CB LEU A 200 14119 8808 6737 -5841 968 -1232 C ATOM 1433 CG LEU A 200 30.220 -22.619 -4.771 1.00 84.65 C ANISOU 1433 CG LEU A 200 15594 9261 7309 -5943 1043 -1177 C ATOM 1434 CD1 LEU A 200 30.239 -22.573 -3.265 1.00 85.89 C ANISOU 1434 CD1 LEU A 200 16125 9217 7292 -6150 1116 -1115 C ATOM 1435 CD2 LEU A 200 29.215 -23.603 -5.296 1.00 87.77 C ANISOU 1435 CD2 LEU A 200 16144 9560 7646 -6244 1269 -1431 C ATOM 1436 N ILE A 201 30.363 -19.352 -7.826 1.00 71.39 N ANISOU 1436 N ILE A 201 12192 8597 6335 -5248 674 -1211 N ATOM 1437 CA ILE A 201 30.172 -18.958 -9.221 1.00 69.25 C ANISOU 1437 CA ILE A 201 11538 8557 6218 -5046 609 -1289 C ATOM 1438 C ILE A 201 31.543 -18.622 -9.866 1.00 71.58 C ANISOU 1438 C ILE A 201 11732 8910 6557 -4658 394 -1035 C ATOM 1439 O ILE A 201 31.833 -19.125 -10.946 1.00 70.37 O ANISOU 1439 O ILE A 201 11532 8781 6426 -4463 335 -1023 O ATOM 1440 CB ILE A 201 29.118 -17.814 -9.348 1.00 70.94 C ANISOU 1440 CB ILE A 201 11368 9026 6559 -5136 677 -1494 C ATOM 1441 CG1 ILE A 201 27.697 -18.317 -8.954 1.00 71.86 C ANISOU 1441 CG1 ILE A 201 11513 9158 6634 -5517 906 -1812 C ATOM 1442 CG2 ILE A 201 29.134 -17.208 -10.763 1.00 71.16 C ANISOU 1442 CG2 ILE A 201 11040 9281 6719 -4842 564 -1522 C ATOM 1443 CD1 ILE A 201 26.577 -17.237 -8.838 1.00 71.61 C ANISOU 1443 CD1 ILE A 201 11121 9396 6694 -5608 985 -2049 C ATOM 1444 N ILE A 202 32.387 -17.829 -9.174 1.00 68.09 N ANISOU 1444 N ILE A 202 11269 8494 6109 -4574 290 -848 N ATOM 1445 CA ILE A 202 33.747 -17.462 -9.608 1.00 67.53 C ANISOU 1445 CA ILE A 202 11087 8513 6059 -4267 105 -629 C ATOM 1446 C ILE A 202 34.609 -18.711 -9.702 1.00 73.90 C ANISOU 1446 C ILE A 202 12169 9170 6741 -4091 25 -510 C ATOM 1447 O ILE A 202 35.327 -18.875 -10.678 1.00 73.67 O ANISOU 1447 O ILE A 202 12014 9233 6743 -3823 -76 -434 O ATOM 1448 CB ILE A 202 34.367 -16.374 -8.665 1.00 69.95 C ANISOU 1448 CB ILE A 202 11336 8885 6359 -4299 37 -497 C ATOM 1449 CG1 ILE A 202 34.013 -14.975 -9.162 1.00 69.10 C ANISOU 1449 CG1 ILE A 202 10906 8969 6382 -4289 50 -550 C ATOM 1450 CG2 ILE A 202 35.897 -16.508 -8.446 1.00 69.81 C ANISOU 1450 CG2 ILE A 202 11371 8893 6261 -4083 -139 -279 C ATOM 1451 CD1 ILE A 202 33.398 -14.106 -8.121 1.00 74.82 C ANISOU 1451 CD1 ILE A 202 11644 9683 7100 -4513 130 -609 C ATOM 1452 N LEU A 203 34.536 -19.579 -8.692 1.00 73.30 N ANISOU 1452 N LEU A 203 12493 8856 6502 -4227 74 -500 N ATOM 1453 CA LEU A 203 35.316 -20.803 -8.618 1.00 75.53 C ANISOU 1453 CA LEU A 203 13135 8948 6614 -4035 -4 -390 C ATOM 1454 C LEU A 203 35.062 -21.728 -9.803 1.00 80.68 C ANISOU 1454 C LEU A 203 13837 9544 7272 -3929 36 -474 C ATOM 1455 O LEU A 203 36.015 -22.111 -10.477 1.00 80.81 O ANISOU 1455 O LEU A 203 13831 9608 7267 -3598 -97 -361 O ATOM 1456 CB LEU A 203 35.072 -21.545 -7.285 1.00 77.56 C ANISOU 1456 CB LEU A 203 13899 8910 6661 -4238 75 -387 C ATOM 1457 CG LEU A 203 36.014 -22.717 -7.019 1.00 84.54 C ANISOU 1457 CG LEU A 203 15231 9574 7316 -3973 -41 -247 C ATOM 1458 CD1 LEU A 203 37.423 -22.234 -6.642 1.00 84.47 C ANISOU 1458 CD1 LEU A 203 15090 9735 7269 -3646 -285 -48 C ATOM 1459 CD2 LEU A 203 35.456 -23.626 -5.958 1.00 90.19 C ANISOU 1459 CD2 LEU A 203 16540 9928 7799 -4223 101 -293 C ATOM 1460 N PHE A 204 33.797 -22.075 -10.065 1.00 77.52 N ANISOU 1460 N PHE A 204 13487 9071 6896 -4212 221 -688 N ATOM 1461 CA PHE A 204 33.500 -22.995 -11.150 1.00 78.54 C ANISOU 1461 CA PHE A 204 13691 9137 7012 -4153 268 -789 C ATOM 1462 C PHE A 204 33.583 -22.325 -12.537 1.00 81.28 C ANISOU 1462 C PHE A 204 13572 9765 7547 -3941 190 -815 C ATOM 1463 O PHE A 204 33.911 -23.025 -13.492 1.00 81.68 O ANISOU 1463 O PHE A 204 13676 9785 7574 -3740 150 -804 O ATOM 1464 CB PHE A 204 32.175 -23.748 -10.918 1.00 82.21 C ANISOU 1464 CB PHE A 204 14406 9430 7399 -4561 501 -1033 C ATOM 1465 CG PHE A 204 32.260 -24.702 -9.744 1.00 86.22 C ANISOU 1465 CG PHE A 204 15516 9582 7661 -4730 588 -987 C ATOM 1466 CD1 PHE A 204 32.943 -25.909 -9.853 1.00 90.91 C ANISOU 1466 CD1 PHE A 204 16590 9899 8055 -4528 541 -878 C ATOM 1467 CD2 PHE A 204 31.705 -24.368 -8.512 1.00 88.62 C ANISOU 1467 CD2 PHE A 204 15944 9816 7910 -5060 714 -1046 C ATOM 1468 CE1 PHE A 204 33.068 -26.761 -8.752 1.00 94.21 C ANISOU 1468 CE1 PHE A 204 17635 9955 8205 -4642 610 -821 C ATOM 1469 CE2 PHE A 204 31.820 -25.226 -7.417 1.00 93.31 C ANISOU 1469 CE2 PHE A 204 17147 10058 8248 -5207 797 -992 C ATOM 1470 CZ PHE A 204 32.508 -26.411 -7.542 1.00 93.40 C ANISOU 1470 CZ PHE A 204 17662 9778 8046 -4989 740 -875 C ATOM 1471 N CYS A 205 33.350 -20.981 -12.649 1.00 74.83 N ANISOU 1471 N CYS A 205 12346 9196 6889 -3961 166 -837 N ATOM 1472 CA CYS A 205 33.478 -20.253 -13.918 1.00 71.62 C ANISOU 1472 CA CYS A 205 11558 9028 6626 -3746 92 -845 C ATOM 1473 C CYS A 205 34.913 -20.326 -14.347 1.00 74.68 C ANISOU 1473 C CYS A 205 11926 9459 6991 -3406 -61 -628 C ATOM 1474 O CYS A 205 35.181 -20.701 -15.487 1.00 76.22 O ANISOU 1474 O CYS A 205 12052 9702 7206 -3201 -98 -631 O ATOM 1475 CB CYS A 205 33.021 -18.806 -13.794 1.00 70.27 C ANISOU 1475 CB CYS A 205 11066 9058 6577 -3818 99 -893 C ATOM 1476 SG CYS A 205 31.274 -18.534 -14.177 1.00 74.77 S ANISOU 1476 SG CYS A 205 11435 9752 7221 -4040 237 -1220 S ATOM 1477 N ASN A 206 35.836 -20.032 -13.424 1.00 70.54 N ANISOU 1477 N ASN A 206 11462 8930 6410 -3348 -148 -459 N ATOM 1478 CA ASN A 206 37.266 -20.044 -13.693 1.00 71.50 C ANISOU 1478 CA ASN A 206 11514 9156 6497 -3036 -298 -279 C ATOM 1479 C ASN A 206 37.815 -21.436 -13.946 1.00 79.37 C ANISOU 1479 C ASN A 206 12806 9997 7356 -2812 -345 -234 C ATOM 1480 O ASN A 206 38.575 -21.593 -14.902 1.00 80.29 O ANISOU 1480 O ASN A 206 12784 10234 7487 -2532 -420 -178 O ATOM 1481 CB ASN A 206 38.072 -19.305 -12.621 1.00 72.72 C ANISOU 1481 CB ASN A 206 11617 9396 6618 -3051 -386 -146 C ATOM 1482 CG ASN A 206 37.991 -17.795 -12.738 1.00 98.05 C ANISOU 1482 CG ASN A 206 14492 12809 9956 -3156 -373 -146 C ATOM 1483 OD1 ASN A 206 38.069 -17.211 -13.824 1.00 95.94 O ANISOU 1483 OD1 ASN A 206 13977 12694 9782 -3058 -368 -161 O ATOM 1484 ND2 ASN A 206 37.831 -17.119 -11.618 1.00 90.94 N ANISOU 1484 ND2 ASN A 206 13621 11891 9039 -3357 -359 -130 N ATOM 1485 N LEU A 207 37.407 -22.450 -13.161 1.00 77.46 N ANISOU 1485 N LEU A 207 12996 9474 6962 -2931 -287 -268 N ATOM 1486 CA LEU A 207 37.892 -23.816 -13.394 1.00 79.50 C ANISOU 1486 CA LEU A 207 13626 9531 7050 -2700 -325 -228 C ATOM 1487 C LEU A 207 37.461 -24.367 -14.769 1.00 83.00 C ANISOU 1487 C LEU A 207 14032 9961 7543 -2634 -261 -337 C ATOM 1488 O LEU A 207 38.247 -25.069 -15.410 1.00 83.43 O ANISOU 1488 O LEU A 207 14182 9997 7520 -2309 -341 -270 O ATOM 1489 CB LEU A 207 37.529 -24.777 -12.248 1.00 81.88 C ANISOU 1489 CB LEU A 207 14488 9485 7138 -2861 -256 -241 C ATOM 1490 CG LEU A 207 38.181 -24.470 -10.885 1.00 87.75 C ANISOU 1490 CG LEU A 207 15362 10210 7770 -2831 -359 -108 C ATOM 1491 CD1 LEU A 207 37.414 -25.129 -9.751 1.00 89.97 C ANISOU 1491 CD1 LEU A 207 16170 10144 7870 -3132 -224 -165 C ATOM 1492 CD2 LEU A 207 39.682 -24.830 -10.854 1.00 90.95 C ANISOU 1492 CD2 LEU A 207 15810 10703 8046 -2357 -580 57 C ATOM 1493 N VAL A 208 36.245 -23.998 -15.240 1.00 78.13 N ANISOU 1493 N VAL A 208 13247 9387 7051 -2918 -128 -517 N ATOM 1494 CA VAL A 208 35.715 -24.391 -16.553 1.00 77.82 C ANISOU 1494 CA VAL A 208 13128 9376 7066 -2887 -73 -650 C ATOM 1495 C VAL A 208 36.539 -23.660 -17.634 1.00 81.05 C ANISOU 1495 C VAL A 208 13145 10057 7594 -2573 -190 -555 C ATOM 1496 O VAL A 208 36.878 -24.275 -18.653 1.00 81.80 O ANISOU 1496 O VAL A 208 13274 10144 7660 -2349 -215 -555 O ATOM 1497 CB VAL A 208 34.181 -24.156 -16.680 1.00 81.20 C ANISOU 1497 CB VAL A 208 13448 9831 7575 -3263 81 -898 C ATOM 1498 CG1 VAL A 208 33.687 -24.429 -18.090 1.00 80.83 C ANISOU 1498 CG1 VAL A 208 13257 9870 7584 -3203 104 -1045 C ATOM 1499 CG2 VAL A 208 33.413 -25.025 -15.695 1.00 83.23 C ANISOU 1499 CG2 VAL A 208 14125 9812 7685 -3609 233 -1014 C ATOM 1500 N ILE A 209 36.903 -22.369 -17.381 1.00 74.54 N ANISOU 1500 N ILE A 209 11988 9454 6879 -2567 -247 -474 N ATOM 1501 CA ILE A 209 37.761 -21.577 -18.267 1.00 72.53 C ANISOU 1501 CA ILE A 209 11399 9449 6710 -2324 -329 -380 C ATOM 1502 C ILE A 209 39.135 -22.273 -18.373 1.00 76.30 C ANISOU 1502 C ILE A 209 11968 9941 7080 -1990 -437 -235 C ATOM 1503 O ILE A 209 39.566 -22.558 -19.488 1.00 75.52 O ANISOU 1503 O ILE A 209 11787 9920 6987 -1760 -456 -230 O ATOM 1504 CB ILE A 209 37.866 -20.079 -17.817 1.00 74.09 C ANISOU 1504 CB ILE A 209 11310 9835 7007 -2440 -344 -329 C ATOM 1505 CG1 ILE A 209 36.613 -19.272 -18.230 1.00 73.01 C ANISOU 1505 CG1 ILE A 209 11010 9754 6978 -2627 -260 -485 C ATOM 1506 CG2 ILE A 209 39.167 -19.389 -18.324 1.00 73.96 C ANISOU 1506 CG2 ILE A 209 11039 10049 7011 -2218 -427 -191 C ATOM 1507 CD1 ILE A 209 36.522 -17.908 -17.572 1.00 73.00 C ANISOU 1507 CD1 ILE A 209 10843 9858 7037 -2771 -254 -455 C ATOM 1508 N ILE A 210 39.797 -22.578 -17.225 1.00 73.84 N ANISOU 1508 N ILE A 210 11835 9565 6656 -1941 -511 -133 N ATOM 1509 CA ILE A 210 41.111 -23.243 -17.228 1.00 76.01 C ANISOU 1509 CA ILE A 210 12184 9892 6803 -1575 -637 -19 C ATOM 1510 C ILE A 210 41.039 -24.542 -18.060 1.00 87.26 C ANISOU 1510 C ILE A 210 13892 11134 8130 -1365 -615 -64 C ATOM 1511 O ILE A 210 41.825 -24.711 -19.003 1.00 87.94 O ANISOU 1511 O ILE A 210 13825 11374 8215 -1067 -665 -33 O ATOM 1512 CB ILE A 210 41.715 -23.450 -15.803 1.00 79.33 C ANISOU 1512 CB ILE A 210 12807 10255 7080 -1532 -740 75 C ATOM 1513 CG1 ILE A 210 41.789 -22.130 -15.006 1.00 77.68 C ANISOU 1513 CG1 ILE A 210 12322 10230 6965 -1760 -756 111 C ATOM 1514 CG2 ILE A 210 43.100 -24.092 -15.882 1.00 81.11 C ANISOU 1514 CG2 ILE A 210 13054 10602 7163 -1087 -897 166 C ATOM 1515 CD1 ILE A 210 41.610 -22.262 -13.469 1.00 81.14 C ANISOU 1515 CD1 ILE A 210 13051 10495 7283 -1915 -785 145 C ATOM 1516 N ARG A 211 40.026 -25.396 -17.760 1.00 87.38 N ANISOU 1516 N ARG A 211 14311 10826 8062 -1565 -516 -159 N ATOM 1517 CA ARG A 211 39.744 -26.673 -18.420 1.00 89.38 C ANISOU 1517 CA ARG A 211 14927 10837 8196 -1461 -461 -229 C ATOM 1518 C ARG A 211 39.528 -26.531 -19.927 1.00 91.80 C ANISOU 1518 C ARG A 211 14978 11282 8620 -1388 -422 -308 C ATOM 1519 O ARG A 211 40.182 -27.258 -20.670 1.00 92.89 O ANISOU 1519 O ARG A 211 15221 11401 8674 -1068 -465 -276 O ATOM 1520 CB ARG A 211 38.556 -27.391 -17.745 1.00 92.93 C ANISOU 1520 CB ARG A 211 15821 10943 8546 -1821 -318 -350 C ATOM 1521 CG ARG A 211 38.341 -28.836 -18.208 1.00109.37 C ANISOU 1521 CG ARG A 211 18406 12706 10442 -1747 -250 -418 C ATOM 1522 CD ARG A 211 36.931 -29.346 -17.932 1.00123.49 C ANISOU 1522 CD ARG A 211 20506 14236 12181 -2220 -53 -609 C ATOM 1523 NE ARG A 211 35.910 -28.659 -18.732 1.00133.34 N ANISOU 1523 NE ARG A 211 21339 15693 13632 -2494 35 -789 N ATOM 1524 CZ ARG A 211 35.577 -28.978 -19.981 1.00148.76 C ANISOU 1524 CZ ARG A 211 23207 17690 15624 -2454 68 -906 C ATOM 1525 NH1 ARG A 211 36.185 -29.983 -20.601 1.00142.96 N ANISOU 1525 NH1 ARG A 211 22778 16792 14748 -2169 38 -859 N ATOM 1526 NH2 ARG A 211 34.633 -28.299 -20.618 1.00129.60 N ANISOU 1526 NH2 ARG A 211 20404 15478 13362 -2676 123 -1078 N ATOM 1527 N THR A 212 38.646 -25.601 -20.382 1.00 86.66 N ANISOU 1527 N THR A 212 14009 10775 8144 -1647 -350 -413 N ATOM 1528 CA THR A 212 38.382 -25.403 -21.824 1.00 86.20 C ANISOU 1528 CA THR A 212 13724 10848 8178 -1570 -324 -496 C ATOM 1529 C THR A 212 39.579 -24.793 -22.570 1.00 89.13 C ANISOU 1529 C THR A 212 13775 11489 8600 -1250 -410 -370 C ATOM 1530 O THR A 212 39.629 -24.903 -23.783 1.00 88.46 O ANISOU 1530 O THR A 212 13603 11472 8537 -1101 -396 -410 O ATOM 1531 CB THR A 212 37.070 -24.629 -22.134 1.00 98.97 C ANISOU 1531 CB THR A 212 15124 12549 9930 -1881 -242 -664 C ATOM 1532 OG1 THR A 212 37.192 -23.256 -21.786 1.00101.24 O ANISOU 1532 OG1 THR A 212 15081 13049 10337 -1943 -273 -603 O ATOM 1533 CG2 THR A 212 35.829 -25.244 -21.493 1.00100.71 C ANISOU 1533 CG2 THR A 212 15607 12560 10098 -2237 -128 -837 C ATOM 1534 N LEU A 213 40.528 -24.152 -21.866 1.00 86.84 N ANISOU 1534 N LEU A 213 13311 11364 8319 -1167 -487 -237 N ATOM 1535 CA LEU A 213 41.733 -23.599 -22.495 1.00 87.06 C ANISOU 1535 CA LEU A 213 13027 11677 8375 -910 -545 -143 C ATOM 1536 C LEU A 213 42.757 -24.714 -22.665 1.00 93.72 C ANISOU 1536 C LEU A 213 14041 12498 9070 -531 -619 -87 C ATOM 1537 O LEU A 213 43.357 -24.839 -23.737 1.00 94.38 O ANISOU 1537 O LEU A 213 13989 12721 9150 -290 -617 -85 O ATOM 1538 CB LEU A 213 42.351 -22.457 -21.669 1.00 86.53 C ANISOU 1538 CB LEU A 213 12691 11827 8360 -1006 -591 -54 C ATOM 1539 CG LEU A 213 41.652 -21.099 -21.680 1.00 88.99 C ANISOU 1539 CG LEU A 213 12780 12225 8806 -1300 -524 -88 C ATOM 1540 CD1 LEU A 213 42.199 -20.223 -20.574 1.00 88.96 C ANISOU 1540 CD1 LEU A 213 12636 12353 8812 -1429 -568 -7 C ATOM 1541 CD2 LEU A 213 41.786 -20.399 -23.023 1.00 89.54 C ANISOU 1541 CD2 LEU A 213 12612 12466 8943 -1230 -473 -105 C ATOM 1542 N LEU A 214 42.936 -25.535 -21.610 1.00 91.67 N ANISOU 1542 N LEU A 214 14111 12052 8669 -460 -681 -48 N ATOM 1543 CA LEU A 214 43.859 -26.671 -21.592 1.00 94.19 C ANISOU 1543 CA LEU A 214 14678 12307 8801 -51 -771 0 C ATOM 1544 C LEU A 214 43.392 -27.843 -22.496 1.00 99.39 C ANISOU 1544 C LEU A 214 15692 12703 9370 67 -704 -76 C ATOM 1545 O LEU A 214 44.141 -28.806 -22.686 1.00 99.73 O ANISOU 1545 O LEU A 214 15960 12684 9248 452 -769 -45 O ATOM 1546 CB LEU A 214 44.139 -27.134 -20.144 1.00 95.86 C ANISOU 1546 CB LEU A 214 15198 12370 8853 1 -867 65 C ATOM 1547 CG LEU A 214 44.863 -26.162 -19.186 1.00 99.55 C ANISOU 1547 CG LEU A 214 15348 13119 9358 -32 -970 142 C ATOM 1548 CD1 LEU A 214 44.838 -26.694 -17.778 1.00100.85 C ANISOU 1548 CD1 LEU A 214 15908 13059 9350 -31 -1048 189 C ATOM 1549 CD2 LEU A 214 46.318 -25.920 -19.600 1.00103.19 C ANISOU 1549 CD2 LEU A 214 15428 13985 9797 339 -1083 182 C ATOM 1550 N MET A 215 42.165 -27.733 -23.066 1.00 97.18 N ANISOU 1550 N MET A 215 15447 12289 9187 -250 -581 -190 N ATOM 1551 CA MET A 215 41.572 -28.674 -24.024 1.00 99.56 C ANISOU 1551 CA MET A 215 16027 12375 9425 -225 -502 -296 C ATOM 1552 C MET A 215 42.483 -28.695 -25.248 1.00106.25 C ANISOU 1552 C MET A 215 16651 13438 10279 141 -536 -264 C ATOM 1553 O MET A 215 42.862 -27.616 -25.741 1.00104.54 O ANISOU 1553 O MET A 215 15981 13537 10204 143 -543 -235 O ATOM 1554 CB MET A 215 40.208 -28.153 -24.506 1.00100.45 C ANISOU 1554 CB MET A 215 16013 12474 9681 -621 -392 -444 C ATOM 1555 CG MET A 215 39.010 -28.685 -23.769 1.00105.53 C ANISOU 1555 CG MET A 215 17002 12829 10266 -995 -297 -565 C ATOM 1556 SD MET A 215 37.530 -28.225 -24.724 1.00109.18 S ANISOU 1556 SD MET A 215 17244 13369 10870 -1340 -192 -792 S ATOM 1557 CE MET A 215 36.274 -28.398 -23.488 1.00106.28 C ANISOU 1557 CE MET A 215 17100 12806 10475 -1835 -79 -931 C ATOM 1558 N GLN A 216 42.835 -29.905 -25.742 1.00106.13 N ANISOU 1558 N GLN A 216 16984 13244 10097 443 -543 -276 N ATOM 1559 CA GLN A 216 43.702 -30.047 -26.918 1.00106.90 C ANISOU 1559 CA GLN A 216 16904 13534 10178 812 -561 -261 C ATOM 1560 C GLN A 216 43.014 -29.486 -28.154 1.00108.25 C ANISOU 1560 C GLN A 216 16836 13802 10493 628 -472 -353 C ATOM 1561 O GLN A 216 41.875 -29.862 -28.454 1.00106.95 O ANISOU 1561 O GLN A 216 16889 13417 10330 373 -397 -473 O ATOM 1562 CB GLN A 216 44.145 -31.499 -27.133 1.00111.48 C ANISOU 1562 CB GLN A 216 17966 13864 10527 1183 -584 -264 C ATOM 1563 CG GLN A 216 45.438 -31.610 -27.940 1.00124.70 C ANISOU 1563 CG GLN A 216 19413 15815 12154 1670 -640 -221 C ATOM 1564 CD GLN A 216 45.377 -32.683 -28.994 1.00135.17 C ANISOU 1564 CD GLN A 216 21080 16934 13345 1905 -587 -287 C ATOM 1565 OE1 GLN A 216 44.453 -32.739 -29.816 1.00124.40 O ANISOU 1565 OE1 GLN A 216 19790 15437 12040 1660 -487 -383 O ATOM 1566 NE2 GLN A 216 46.389 -33.539 -29.012 1.00130.26 N ANISOU 1566 NE2 GLN A 216 20660 16303 12529 2409 -663 -249 N ATOM 1567 N ALA A1001 43.693 -28.539 -28.826 1.00104.05 N ANISOU 1567 N ALA A1001 15855 13613 10065 737 -476 -309 N ATOM 1568 CA ALA A1001 43.177 -27.841 -30.001 1.00102.51 C ANISOU 1568 CA ALA A1001 15429 13535 9984 608 -404 -376 C ATOM 1569 C ALA A1001 43.032 -28.719 -31.246 1.00107.71 C ANISOU 1569 C ALA A1001 16296 14072 10556 790 -359 -458 C ATOM 1570 O ALA A1001 43.955 -29.450 -31.627 1.00109.29 O ANISOU 1570 O ALA A1001 16594 14292 10639 1153 -376 -422 O ATOM 1571 CB ALA A1001 44.018 -26.613 -30.304 1.00102.35 C ANISOU 1571 CB ALA A1001 14952 13878 10057 655 -398 -301 C ATOM 1572 N LYS A1002 41.841 -28.654 -31.853 1.00102.90 N ANISOU 1572 N LYS A1002 15753 13350 9993 545 -309 -584 N ATOM 1573 CA LYS A1002 41.498 -29.388 -33.059 1.00103.56 C ANISOU 1573 CA LYS A1002 16028 13320 10001 646 -267 -689 C ATOM 1574 C LYS A1002 41.425 -28.375 -34.196 1.00105.88 C ANISOU 1574 C LYS A1002 15993 13849 10386 646 -242 -710 C ATOM 1575 O LYS A1002 40.679 -27.390 -34.096 1.00104.78 O ANISOU 1575 O LYS A1002 15654 13800 10358 393 -245 -751 O ATOM 1576 CB LYS A1002 40.166 -30.137 -32.877 1.00106.43 C ANISOU 1576 CB LYS A1002 16727 13394 10318 349 -232 -851 C ATOM 1577 N ALA A1003 42.254 -28.575 -35.239 1.00101.09 N ANISOU 1577 N ALA A1003 15346 13348 9716 951 -215 -679 N ATOM 1578 CA ALA A1003 42.312 -27.682 -36.391 1.00 99.07 C ANISOU 1578 CA ALA A1003 14846 13292 9504 984 -174 -688 C ATOM 1579 C ALA A1003 41.861 -28.374 -37.667 1.00102.98 C ANISOU 1579 C ALA A1003 15545 13674 9909 1088 -147 -804 C ATOM 1580 O ALA A1003 42.097 -29.572 -37.836 1.00104.47 O ANISOU 1580 O ALA A1003 16017 13695 9980 1272 -140 -831 O ATOM 1581 CB ALA A1003 43.716 -27.128 -36.560 1.00100.17 C ANISOU 1581 CB ALA A1003 14716 13703 9641 1205 -136 -563 C ATOM 1582 N LEU A1004 41.212 -27.614 -38.569 1.00 97.52 N ANISOU 1582 N LEU A1004 14735 13067 9252 989 -139 -877 N ATOM 1583 CA LEU A1004 40.726 -28.105 -39.863 1.00 97.50 C ANISOU 1583 CA LEU A1004 14894 12993 9160 1075 -128 -1000 C ATOM 1584 C LEU A1004 41.367 -27.320 -41.005 1.00 98.72 C ANISOU 1584 C LEU A1004 14881 13341 9286 1255 -73 -943 C ATOM 1585 O LEU A1004 41.296 -26.088 -41.035 1.00 97.68 O ANISOU 1585 O LEU A1004 14538 13359 9216 1154 -66 -898 O ATOM 1586 CB LEU A1004 39.183 -28.027 -39.939 1.00 97.17 C ANISOU 1586 CB LEU A1004 14904 12871 9144 797 -186 -1187 C ATOM 1587 CG LEU A1004 38.514 -28.131 -41.318 1.00102.67 C ANISOU 1587 CG LEU A1004 15674 13575 9759 850 -205 -1338 C ATOM 1588 CD1 LEU A1004 38.316 -29.577 -41.742 1.00104.69 C ANISOU 1588 CD1 LEU A1004 16265 13620 9892 895 -188 -1456 C ATOM 1589 CD2 LEU A1004 37.189 -27.400 -41.322 1.00104.82 C ANISOU 1589 CD2 LEU A1004 15810 13932 10085 621 -284 -1495 C ATOM 1590 N ILE A1005 41.985 -28.033 -41.944 1.00 93.59 N ANISOU 1590 N ILE A1005 14365 12671 8523 1516 -20 -948 N ATOM 1591 CA ILE A1005 42.610 -27.384 -43.084 1.00 92.16 C ANISOU 1591 CA ILE A1005 14068 12660 8289 1677 60 -905 C ATOM 1592 C ILE A1005 41.849 -27.758 -44.344 1.00 96.12 C ANISOU 1592 C ILE A1005 14772 13060 8689 1728 42 -1042 C ATOM 1593 O ILE A1005 41.698 -28.944 -44.643 1.00 97.20 O ANISOU 1593 O ILE A1005 15160 13031 8742 1827 32 -1126 O ATOM 1594 CB ILE A1005 44.132 -27.676 -43.187 1.00 95.85 C ANISOU 1594 CB ILE A1005 14442 13273 8702 1952 157 -799 C ATOM 1595 CG1 ILE A1005 44.841 -27.541 -41.807 1.00 94.39 C ANISOU 1595 CG1 ILE A1005 14075 13190 8599 1920 137 -696 C ATOM 1596 CG2 ILE A1005 44.773 -26.779 -44.274 1.00 97.02 C ANISOU 1596 CG2 ILE A1005 14438 13628 8798 2030 278 -759 C ATOM 1597 CD1 ILE A1005 46.310 -27.899 -41.757 1.00 92.73 C ANISOU 1597 CD1 ILE A1005 13726 13178 8329 2211 202 -628 C ATOM 1598 N VAL A1006 41.342 -26.750 -45.066 1.00 91.69 N ANISOU 1598 N VAL A1006 14136 12586 8116 1665 32 -1073 N ATOM 1599 CA VAL A1006 40.604 -26.978 -46.315 1.00 92.37 C ANISOU 1599 CA VAL A1006 14398 12610 8087 1733 -7 -1213 C ATOM 1600 C VAL A1006 41.354 -26.314 -47.487 1.00 95.10 C ANISOU 1600 C VAL A1006 14730 13076 8327 1920 99 -1140 C ATOM 1601 O VAL A1006 41.530 -25.087 -47.490 1.00 94.30 O ANISOU 1601 O VAL A1006 14496 13093 8242 1856 138 -1057 O ATOM 1602 CB VAL A1006 39.097 -26.584 -46.256 1.00 95.99 C ANISOU 1602 CB VAL A1006 14852 13047 8573 1530 -146 -1376 C ATOM 1603 CG1 VAL A1006 38.322 -27.219 -47.406 1.00 97.16 C ANISOU 1603 CG1 VAL A1006 15197 13131 8589 1603 -209 -1562 C ATOM 1604 CG2 VAL A1006 38.461 -26.962 -44.921 1.00 95.21 C ANISOU 1604 CG2 VAL A1006 14716 12868 8589 1285 -208 -1434 C ATOM 1605 N TYR A1007 41.816 -27.130 -48.459 1.00 90.89 N ANISOU 1605 N TYR A1007 14369 12497 7669 2138 162 -1172 N ATOM 1606 CA TYR A1007 42.584 -26.633 -49.603 1.00 91.05 C ANISOU 1606 CA TYR A1007 14406 12623 7567 2311 292 -1114 C ATOM 1607 C TYR A1007 41.976 -26.931 -50.970 1.00 96.05 C ANISOU 1607 C TYR A1007 15284 13171 8039 2434 257 -1239 C ATOM 1608 O TYR A1007 41.449 -28.021 -51.202 1.00 96.64 O ANISOU 1608 O TYR A1007 15542 13106 8069 2477 185 -1365 O ATOM 1609 CB TYR A1007 44.039 -27.142 -49.557 1.00 92.93 C ANISOU 1609 CB TYR A1007 14563 12963 7784 2503 446 -1017 C ATOM 1610 CG TYR A1007 44.183 -28.647 -49.672 1.00 95.43 C ANISOU 1610 CG TYR A1007 15080 13136 8040 2698 428 -1086 C ATOM 1611 CD1 TYR A1007 44.129 -29.462 -48.543 1.00 97.33 C ANISOU 1611 CD1 TYR A1007 15352 13271 8359 2671 356 -1086 C ATOM 1612 CD2 TYR A1007 44.402 -29.256 -50.907 1.00 97.08 C ANISOU 1612 CD2 TYR A1007 15498 13296 8093 2918 494 -1149 C ATOM 1613 CE1 TYR A1007 44.283 -30.845 -48.640 1.00100.00 C ANISOU 1613 CE1 TYR A1007 15954 13436 8606 2864 351 -1145 C ATOM 1614 CE2 TYR A1007 44.531 -30.639 -51.018 1.00 99.25 C ANISOU 1614 CE2 TYR A1007 16010 13411 8291 3106 484 -1215 C ATOM 1615 CZ TYR A1007 44.484 -31.429 -49.880 1.00108.16 C ANISOU 1615 CZ TYR A1007 17195 14415 9484 3083 415 -1211 C ATOM 1616 OH TYR A1007 44.629 -32.793 -49.973 1.00113.00 O ANISOU 1616 OH TYR A1007 18118 14829 9987 3281 415 -1272 O ATOM 1617 N GLY A1008 42.118 -25.967 -51.873 1.00 92.56 N ANISOU 1617 N GLY A1008 14874 12805 7489 2485 320 -1204 N ATOM 1618 CA GLY A1008 41.703 -26.075 -53.267 1.00 93.33 C ANISOU 1618 CA GLY A1008 15215 12845 7401 2633 300 -1303 C ATOM 1619 C GLY A1008 42.932 -26.002 -54.146 1.00 96.65 C ANISOU 1619 C GLY A1008 15689 13339 7694 2809 515 -1212 C ATOM 1620 O GLY A1008 43.496 -24.914 -54.312 1.00 95.54 O ANISOU 1620 O GLY A1008 15486 13303 7512 2762 646 -1105 O ATOM 1621 N SER A1009 43.390 -27.171 -54.666 1.00 94.01 N ANISOU 1621 N SER A1009 15478 12952 7288 2997 573 -1260 N ATOM 1622 CA SER A1009 44.605 -27.265 -55.481 1.00 95.61 C ANISOU 1622 CA SER A1009 15707 13252 7368 3185 792 -1199 C ATOM 1623 C SER A1009 44.430 -27.988 -56.819 1.00102.41 C ANISOU 1623 C SER A1009 16870 14004 8035 3390 804 -1304 C ATOM 1624 O SER A1009 43.868 -29.084 -56.844 1.00103.84 O ANISOU 1624 O SER A1009 17210 14036 8209 3449 686 -1418 O ATOM 1625 CB SER A1009 45.726 -27.923 -54.683 1.00 98.72 C ANISOU 1625 CB SER A1009 15897 13754 7858 3273 896 -1134 C ATOM 1626 OG SER A1009 46.934 -27.921 -55.424 1.00107.88 O ANISOU 1626 OG SER A1009 17015 15073 8903 3448 1121 -1098 O ATOM 1627 N THR A1010 44.965 -27.391 -57.919 1.00 99.05 N ANISOU 1627 N THR A1010 16549 13646 7438 3482 968 -1270 N ATOM 1628 CA THR A1010 44.942 -27.956 -59.277 1.00100.07 C ANISOU 1628 CA THR A1010 16975 13689 7357 3686 1012 -1357 C ATOM 1629 C THR A1010 46.253 -28.718 -59.518 1.00104.70 C ANISOU 1629 C THR A1010 17510 14373 7900 3892 1229 -1329 C ATOM 1630 O THR A1010 46.230 -29.951 -59.562 1.00105.06 O ANISOU 1630 O THR A1010 17678 14312 7930 4057 1181 -1408 O ATOM 1631 CB THR A1010 44.693 -26.857 -60.354 1.00108.13 C ANISOU 1631 CB THR A1010 18199 14705 8182 3677 1059 -1344 C ATOM 1632 OG1 THR A1010 43.505 -26.122 -60.061 1.00108.86 O ANISOU 1632 OG1 THR A1010 18323 14734 8304 3542 841 -1380 O ATOM 1633 CG2 THR A1010 44.593 -27.415 -61.765 1.00106.87 C ANISOU 1633 CG2 THR A1010 18371 14447 7787 3887 1088 -1439 C ATOM 1634 N THR A1011 47.394 -27.979 -59.647 1.00101.46 N ANISOU 1634 N THR A1011 16918 14175 7455 3876 1475 -1234 N ATOM 1635 CA THR A1011 48.745 -28.510 -59.928 1.00102.92 C ANISOU 1635 CA THR A1011 16980 14542 7581 4075 1712 -1229 C ATOM 1636 C THR A1011 49.414 -29.175 -58.701 1.00104.32 C ANISOU 1636 C THR A1011 16856 14849 7933 4152 1692 -1206 C ATOM 1637 O THR A1011 50.489 -29.757 -58.845 1.00105.42 O ANISOU 1637 O THR A1011 16876 15157 8023 4381 1848 -1229 O ATOM 1638 CB THR A1011 49.664 -27.433 -60.567 1.00115.98 C ANISOU 1638 CB THR A1011 18550 16406 9110 3980 2002 -1172 C ATOM 1639 OG1 THR A1011 48.895 -26.351 -61.103 1.00116.88 O ANISOU 1639 OG1 THR A1011 18900 16390 9118 3802 1967 -1142 O ATOM 1640 CG2 THR A1011 50.566 -28.002 -61.656 1.00119.73 C ANISOU 1640 CG2 THR A1011 19113 16981 9399 4220 2235 -1233 C ATOM 1641 N GLY A1012 48.771 -29.095 -57.530 1.00 97.81 N ANISOU 1641 N GLY A1012 15923 13951 7291 3987 1498 -1173 N ATOM 1642 CA GLY A1012 49.240 -29.721 -56.296 1.00 96.77 C ANISOU 1642 CA GLY A1012 15570 13894 7306 4059 1439 -1149 C ATOM 1643 C GLY A1012 50.093 -28.879 -55.367 1.00 98.43 C ANISOU 1643 C GLY A1012 15366 14395 7638 3916 1533 -1062 C ATOM 1644 O GLY A1012 50.600 -29.405 -54.368 1.00 97.88 O ANISOU 1644 O GLY A1012 15104 14419 7665 4018 1482 -1048 O ATOM 1645 N ASN A1013 50.252 -27.574 -55.670 1.00 93.46 N ANISOU 1645 N ASN A1013 14627 13900 6983 3676 1669 -1010 N ATOM 1646 CA ASN A1013 51.069 -26.653 -54.877 1.00 92.94 C ANISOU 1646 CA ASN A1013 14184 14122 7008 3476 1788 -943 C ATOM 1647 C ASN A1013 50.436 -26.257 -53.539 1.00 94.56 C ANISOU 1647 C ASN A1013 14266 14258 7404 3254 1596 -880 C ATOM 1648 O ASN A1013 51.130 -26.275 -52.523 1.00 93.80 O ANISOU 1648 O ASN A1013 13856 14367 7416 3237 1599 -853 O ATOM 1649 CB ASN A1013 51.463 -25.434 -55.690 1.00 93.06 C ANISOU 1649 CB ASN A1013 14204 14262 6893 3268 2028 -918 C ATOM 1650 CG ASN A1013 52.506 -25.720 -56.735 1.00113.07 C ANISOU 1650 CG ASN A1013 16716 16993 9255 3445 2289 -985 C ATOM 1651 OD1 ASN A1013 53.172 -26.758 -56.733 1.00107.32 O ANISOU 1651 OD1 ASN A1013 15870 16390 8518 3745 2310 -1050 O ATOM 1652 ND2 ASN A1013 52.681 -24.790 -57.651 1.00107.37 N ANISOU 1652 ND2 ASN A1013 16128 16297 8370 3271 2505 -974 N ATOM 1653 N THR A1014 49.130 -25.916 -53.528 1.00 90.11 N ANISOU 1653 N THR A1014 13937 13430 6872 3100 1425 -871 N ATOM 1654 CA THR A1014 48.390 -25.575 -52.302 1.00 87.65 C ANISOU 1654 CA THR A1014 13536 13034 6732 2892 1240 -828 C ATOM 1655 C THR A1014 48.274 -26.836 -51.454 1.00 91.99 C ANISOU 1655 C THR A1014 14077 13497 7379 3047 1086 -860 C ATOM 1656 O THR A1014 48.366 -26.747 -50.231 1.00 91.88 O ANISOU 1656 O THR A1014 13869 13539 7502 2943 1011 -813 O ATOM 1657 CB THR A1014 47.010 -24.963 -52.607 1.00 90.79 C ANISOU 1657 CB THR A1014 14176 13207 7112 2739 1097 -848 C ATOM 1658 OG1 THR A1014 47.142 -23.917 -53.578 1.00 91.89 O ANISOU 1658 OG1 THR A1014 14438 13378 7098 2668 1244 -821 O ATOM 1659 CG2 THR A1014 46.314 -24.434 -51.356 1.00 81.91 C ANISOU 1659 CG2 THR A1014 12929 12038 6156 2508 942 -811 C ATOM 1660 N GLU A1015 48.112 -28.005 -52.112 1.00 89.05 N ANISOU 1660 N GLU A1015 13951 12973 6912 3296 1052 -941 N ATOM 1661 CA GLU A1015 48.046 -29.319 -51.477 1.00 89.58 C ANISOU 1661 CA GLU A1015 14127 12902 7009 3475 935 -980 C ATOM 1662 C GLU A1015 49.305 -29.540 -50.640 1.00 94.49 C ANISOU 1662 C GLU A1015 14459 13769 7674 3634 1000 -928 C ATOM 1663 O GLU A1015 49.175 -29.898 -49.474 1.00 93.07 O ANISOU 1663 O GLU A1015 14242 13530 7590 3611 875 -902 O ATOM 1664 CB GLU A1015 47.889 -30.425 -52.537 1.00 93.05 C ANISOU 1664 CB GLU A1015 14903 13162 7289 3729 945 -1077 C ATOM 1665 CG GLU A1015 47.795 -31.832 -51.967 1.00105.60 C ANISOU 1665 CG GLU A1015 16713 14548 8863 3916 843 -1124 C ATOM 1666 CD GLU A1015 47.238 -32.868 -52.922 1.00131.71 C ANISOU 1666 CD GLU A1015 20434 17593 12017 4059 817 -1239 C ATOM 1667 OE1 GLU A1015 46.185 -33.463 -52.597 1.00129.44 O ANISOU 1667 OE1 GLU A1015 20404 17037 11740 3915 679 -1313 O ATOM 1668 OE2 GLU A1015 47.849 -33.084 -53.994 1.00126.82 O ANISOU 1668 OE2 GLU A1015 19886 17043 11257 4291 947 -1268 O ATOM 1669 N TYR A1016 50.509 -29.281 -51.224 1.00 93.34 N ANISOU 1669 N TYR A1016 14099 13920 7446 3783 1196 -929 N ATOM 1670 CA TYR A1016 51.807 -29.414 -50.553 1.00 94.92 C ANISOU 1670 CA TYR A1016 13952 14449 7664 3958 1267 -919 C ATOM 1671 C TYR A1016 51.914 -28.478 -49.343 1.00 93.71 C ANISOU 1671 C TYR A1016 13482 14461 7663 3674 1222 -845 C ATOM 1672 O TYR A1016 52.333 -28.912 -48.268 1.00 94.10 O ANISOU 1672 O TYR A1016 13384 14600 7771 3792 1123 -832 O ATOM 1673 CB TYR A1016 52.980 -29.181 -51.529 1.00100.51 C ANISOU 1673 CB TYR A1016 14460 15485 8244 4109 1515 -971 C ATOM 1674 CG TYR A1016 54.318 -29.049 -50.831 1.00107.55 C ANISOU 1674 CG TYR A1016 14888 16818 9158 4220 1598 -993 C ATOM 1675 CD1 TYR A1016 54.918 -30.144 -50.217 1.00112.55 C ANISOU 1675 CD1 TYR A1016 15466 17532 9765 4618 1497 -1035 C ATOM 1676 CD2 TYR A1016 54.956 -27.817 -50.732 1.00109.48 C ANISOU 1676 CD2 TYR A1016 14763 17400 9433 3922 1769 -983 C ATOM 1677 CE1 TYR A1016 56.122 -30.017 -49.521 1.00117.47 C ANISOU 1677 CE1 TYR A1016 15629 18605 10399 4749 1538 -1079 C ATOM 1678 CE2 TYR A1016 56.159 -27.676 -50.039 1.00113.21 C ANISOU 1678 CE2 TYR A1016 14765 18325 9925 3990 1833 -1034 C ATOM 1679 CZ TYR A1016 56.743 -28.781 -49.439 1.00125.15 C ANISOU 1679 CZ TYR A1016 16180 19955 11417 4421 1706 -1088 C ATOM 1680 OH TYR A1016 57.941 -28.664 -48.773 1.00129.58 O ANISOU 1680 OH TYR A1016 16247 21010 11979 4533 1746 -1165 O ATOM 1681 N THR A1017 51.544 -27.202 -49.523 1.00 85.16 N ANISOU 1681 N THR A1017 12330 13405 6622 3317 1292 -799 N ATOM 1682 CA THR A1017 51.586 -26.210 -48.462 1.00 82.11 C ANISOU 1682 CA THR A1017 11686 13149 6364 3014 1266 -732 C ATOM 1683 C THR A1017 50.668 -26.660 -47.336 1.00 84.30 C ANISOU 1683 C THR A1017 12090 13174 6766 2962 1027 -699 C ATOM 1684 O THR A1017 51.079 -26.645 -46.176 1.00 84.68 O ANISOU 1684 O THR A1017 11920 13353 6900 2936 959 -666 O ATOM 1685 CB THR A1017 51.236 -24.834 -49.006 1.00 83.69 C ANISOU 1685 CB THR A1017 11916 13342 6541 2678 1386 -693 C ATOM 1686 OG1 THR A1017 51.881 -24.637 -50.265 1.00 82.41 O ANISOU 1686 OG1 THR A1017 11775 13317 6221 2745 1613 -736 O ATOM 1687 CG2 THR A1017 51.635 -23.732 -48.061 1.00 81.87 C ANISOU 1687 CG2 THR A1017 11393 13315 6401 2370 1432 -637 C ATOM 1688 N ALA A1018 49.455 -27.133 -47.683 1.00 78.87 N ANISOU 1688 N ALA A1018 11755 12140 6070 2952 905 -727 N ATOM 1689 CA ALA A1018 48.479 -27.644 -46.719 1.00 76.63 C ANISOU 1689 CA ALA A1018 11633 11601 5883 2866 707 -727 C ATOM 1690 C ALA A1018 49.039 -28.824 -45.916 1.00 81.28 C ANISOU 1690 C ALA A1018 12251 12173 6458 3133 632 -731 C ATOM 1691 O ALA A1018 48.784 -28.906 -44.722 1.00 78.97 O ANISOU 1691 O ALA A1018 11938 11814 6255 3031 515 -695 O ATOM 1692 CB ALA A1018 47.206 -28.050 -47.436 1.00 76.41 C ANISOU 1692 CB ALA A1018 11955 11269 5810 2823 623 -804 C ATOM 1693 N GLU A1019 49.827 -29.710 -46.576 1.00 81.42 N ANISOU 1693 N GLU A1019 12339 12253 6345 3496 702 -778 N ATOM 1694 CA GLU A1019 50.487 -30.877 -45.982 1.00 83.57 C ANISOU 1694 CA GLU A1019 12688 12515 6549 3852 637 -792 C ATOM 1695 C GLU A1019 51.575 -30.419 -45.030 1.00 88.93 C ANISOU 1695 C GLU A1019 12953 13557 7281 3907 643 -748 C ATOM 1696 O GLU A1019 51.614 -30.907 -43.904 1.00 89.37 O ANISOU 1696 O GLU A1019 13057 13546 7355 3993 508 -720 O ATOM 1697 CB GLU A1019 51.077 -31.794 -47.064 1.00 87.92 C ANISOU 1697 CB GLU A1019 13405 13073 6930 4245 728 -865 C ATOM 1698 CG GLU A1019 50.051 -32.680 -47.758 1.00102.01 C ANISOU 1698 CG GLU A1019 15685 14449 8627 4271 680 -927 C ATOM 1699 CD GLU A1019 50.362 -33.169 -49.164 1.00127.91 C ANISOU 1699 CD GLU A1019 19124 17726 11751 4522 803 -1001 C ATOM 1700 OE1 GLU A1019 51.485 -32.923 -49.663 1.00126.48 O ANISOU 1700 OE1 GLU A1019 18667 17874 11514 4728 946 -1009 O ATOM 1701 OE2 GLU A1019 49.465 -33.797 -49.772 1.00123.31 O ANISOU 1701 OE2 GLU A1019 18936 16823 11095 4493 763 -1065 O ATOM 1702 N THR A1020 52.432 -29.459 -45.463 1.00 86.08 N ANISOU 1702 N THR A1020 12200 13579 6928 3828 803 -753 N ATOM 1703 CA THR A1020 53.515 -28.879 -44.654 1.00 87.30 C ANISOU 1703 CA THR A1020 11892 14153 7124 3819 832 -745 C ATOM 1704 C THR A1020 52.958 -28.215 -43.391 1.00 90.15 C ANISOU 1704 C THR A1020 12179 14443 7630 3487 707 -666 C ATOM 1705 O THR A1020 53.535 -28.387 -42.315 1.00 91.18 O ANISOU 1705 O THR A1020 12122 14742 7778 3596 609 -657 O ATOM 1706 CB THR A1020 54.343 -27.883 -45.472 1.00 94.76 C ANISOU 1706 CB THR A1020 12487 15479 8036 3679 1068 -785 C ATOM 1707 OG1 THR A1020 54.564 -28.413 -46.774 1.00 99.04 O ANISOU 1707 OG1 THR A1020 13179 16006 8446 3919 1196 -852 O ATOM 1708 CG2 THR A1020 55.677 -27.556 -44.817 1.00 94.26 C ANISOU 1708 CG2 THR A1020 11915 15929 7970 3746 1121 -838 C ATOM 1709 N ILE A1021 51.845 -27.465 -43.527 1.00 84.67 N ANISOU 1709 N ILE A1021 11636 13512 7023 3111 703 -618 N ATOM 1710 CA ILE A1021 51.171 -26.782 -42.421 1.00 82.86 C ANISOU 1710 CA ILE A1021 11371 13184 6928 2780 597 -551 C ATOM 1711 C ILE A1021 50.575 -27.825 -41.483 1.00 89.78 C ANISOU 1711 C ILE A1021 12522 13771 7819 2901 407 -540 C ATOM 1712 O ILE A1021 50.732 -27.698 -40.262 1.00 89.76 O ANISOU 1712 O ILE A1021 12401 13829 7876 2836 310 -497 O ATOM 1713 CB ILE A1021 50.126 -25.749 -42.933 1.00 83.16 C ANISOU 1713 CB ILE A1021 11523 13053 7022 2418 642 -527 C ATOM 1714 CG1 ILE A1021 50.824 -24.549 -43.620 1.00 83.77 C ANISOU 1714 CG1 ILE A1021 11357 13410 7061 2246 846 -521 C ATOM 1715 CG2 ILE A1021 49.172 -25.281 -41.812 1.00 80.85 C ANISOU 1715 CG2 ILE A1021 11279 12583 6858 2125 507 -478 C ATOM 1716 CD1 ILE A1021 49.970 -23.813 -44.641 1.00 84.14 C ANISOU 1716 CD1 ILE A1021 11629 13272 7069 2064 916 -519 C ATOM 1717 N ALA A1022 49.939 -28.878 -42.055 1.00 88.50 N ANISOU 1717 N ALA A1022 12752 13296 7579 3069 366 -586 N ATOM 1718 CA ALA A1022 49.355 -29.979 -41.280 1.00 89.64 C ANISOU 1718 CA ALA A1022 13251 13116 7693 3164 223 -592 C ATOM 1719 C ALA A1022 50.420 -30.720 -40.452 1.00 98.33 C ANISOU 1719 C ALA A1022 14303 14349 8708 3528 151 -575 C ATOM 1720 O ALA A1022 50.190 -30.952 -39.269 1.00 97.79 O ANISOU 1720 O ALA A1022 14342 14153 8661 3478 32 -535 O ATOM 1721 CB ALA A1022 48.615 -30.945 -42.190 1.00 90.92 C ANISOU 1721 CB ALA A1022 13837 12953 7754 3265 228 -668 C ATOM 1722 N ARG A1023 51.601 -31.024 -41.049 1.00 98.95 N ANISOU 1722 N ARG A1023 14204 14712 8680 3902 223 -614 N ATOM 1723 CA ARG A1023 52.709 -31.685 -40.355 1.00102.35 C ANISOU 1723 CA ARG A1023 14538 15344 9005 4324 143 -625 C ATOM 1724 C ARG A1023 53.303 -30.785 -39.261 1.00107.68 C ANISOU 1724 C ARG A1023 14773 16364 9775 4171 92 -586 C ATOM 1725 O ARG A1023 53.793 -31.306 -38.260 1.00109.62 O ANISOU 1725 O ARG A1023 15036 16661 9953 4424 -47 -577 O ATOM 1726 CB ARG A1023 53.792 -32.165 -41.345 1.00106.25 C ANISOU 1726 CB ARG A1023 14901 16108 9359 4762 244 -709 C ATOM 1727 CG ARG A1023 54.975 -32.944 -40.724 1.00122.49 C ANISOU 1727 CG ARG A1023 16857 18413 11271 5303 144 -753 C ATOM 1728 CD ARG A1023 54.575 -34.242 -40.032 1.00136.81 C ANISOU 1728 CD ARG A1023 19241 19796 12946 5600 -24 -726 C ATOM 1729 NE ARG A1023 55.701 -34.857 -39.324 1.00154.71 N ANISOU 1729 NE ARG A1023 21407 22319 15059 6140 -150 -764 N ATOM 1730 CZ ARG A1023 55.582 -35.796 -38.388 1.00172.63 C ANISOU 1730 CZ ARG A1023 24115 24292 17185 6422 -321 -729 C ATOM 1731 NH1 ARG A1023 54.382 -36.227 -38.017 1.00162.59 N ANISOU 1731 NH1 ARG A1023 23403 22459 15914 6158 -361 -661 N ATOM 1732 NH2 ARG A1023 56.661 -36.291 -37.796 1.00158.79 N ANISOU 1732 NH2 ARG A1023 22246 22816 15270 6966 -452 -775 N ATOM 1733 N GLU A1024 53.225 -29.446 -39.431 1.00102.28 N ANISOU 1733 N GLU A1024 13746 15890 9228 3758 198 -566 N ATOM 1734 CA GLU A1024 53.741 -28.486 -38.455 1.00101.52 C ANISOU 1734 CA GLU A1024 13243 16113 9219 3543 172 -540 C ATOM 1735 C GLU A1024 52.884 -28.455 -37.194 1.00103.30 C ANISOU 1735 C GLU A1024 13674 16051 9523 3321 17 -461 C ATOM 1736 O GLU A1024 53.432 -28.502 -36.092 1.00103.97 O ANISOU 1736 O GLU A1024 13613 16299 9593 3417 -100 -447 O ATOM 1737 CB GLU A1024 53.866 -27.089 -39.072 1.00101.63 C ANISOU 1737 CB GLU A1024 12924 16372 9318 3151 357 -544 C ATOM 1738 CG GLU A1024 55.043 -26.280 -38.540 1.00113.32 C ANISOU 1738 CG GLU A1024 13875 18372 10808 3069 408 -586 C ATOM 1739 CD GLU A1024 54.940 -25.674 -37.149 1.00125.44 C ANISOU 1739 CD GLU A1024 15272 19954 12434 2814 287 -532 C ATOM 1740 OE1 GLU A1024 53.823 -25.275 -36.744 1.00117.44 O ANISOU 1740 OE1 GLU A1024 14498 18601 11522 2496 242 -447 O ATOM 1741 OE2 GLU A1024 55.996 -25.542 -36.488 1.00112.83 O ANISOU 1741 OE2 GLU A1024 13300 18771 10801 2925 244 -590 O ATOM 1742 N LEU A1025 51.549 -28.397 -37.353 1.00 97.45 N ANISOU 1742 N LEU A1025 13265 14906 8854 3037 15 -426 N ATOM 1743 CA LEU A1025 50.615 -28.369 -36.223 1.00 95.56 C ANISOU 1743 CA LEU A1025 13235 14384 8688 2787 -104 -372 C ATOM 1744 C LEU A1025 50.533 -29.727 -35.523 1.00101.62 C ANISOU 1744 C LEU A1025 14404 14876 9330 3085 -238 -370 C ATOM 1745 O LEU A1025 50.510 -29.764 -34.288 1.00100.55 O ANISOU 1745 O LEU A1025 14313 14694 9198 3038 -351 -325 O ATOM 1746 CB LEU A1025 49.201 -27.920 -36.645 1.00 92.68 C ANISOU 1746 CB LEU A1025 13069 13723 8423 2406 -61 -374 C ATOM 1747 CG LEU A1025 49.020 -26.693 -37.547 1.00 95.46 C ANISOU 1747 CG LEU A1025 13195 14223 8851 2147 71 -379 C ATOM 1748 CD1 LEU A1025 47.552 -26.456 -37.809 1.00 92.71 C ANISOU 1748 CD1 LEU A1025 13086 13571 8569 1866 57 -404 C ATOM 1749 CD2 LEU A1025 49.635 -25.442 -36.938 1.00 97.57 C ANISOU 1749 CD2 LEU A1025 13072 14806 9195 1924 112 -332 C ATOM 1750 N ALA A1026 50.472 -30.840 -36.309 1.00100.75 N ANISOU 1750 N ALA A1026 14635 14557 9088 3386 -220 -419 N ATOM 1751 CA ALA A1026 50.405 -32.209 -35.776 1.00103.04 C ANISOU 1751 CA ALA A1026 15412 14527 9209 3693 -324 -422 C ATOM 1752 C ALA A1026 51.634 -32.513 -34.916 1.00110.70 C ANISOU 1752 C ALA A1026 16231 15762 10067 4101 -442 -402 C ATOM 1753 O ALA A1026 51.468 -33.032 -33.810 1.00110.53 O ANISOU 1753 O ALA A1026 16502 15530 9966 4164 -565 -362 O ATOM 1754 CB ALA A1026 50.267 -33.225 -36.899 1.00105.16 C ANISOU 1754 CB ALA A1026 16041 14574 9343 3951 -263 -488 C ATOM 1755 N ASP A1027 52.849 -32.109 -35.395 1.00109.93 N ANISOU 1755 N ASP A1027 15653 16155 9959 4349 -400 -444 N ATOM 1756 CA ASP A1027 54.138 -32.220 -34.696 1.00113.39 C ANISOU 1756 CA ASP A1027 15794 16993 10298 4741 -511 -469 C ATOM 1757 C ASP A1027 54.057 -31.505 -33.356 1.00117.71 C ANISOU 1757 C ASP A1027 16162 17628 10933 4467 -618 -409 C ATOM 1758 O ASP A1027 54.611 -31.984 -32.366 1.00119.80 O ANISOU 1758 O ASP A1027 16486 17960 11071 4779 -783 -403 O ATOM 1759 CB ASP A1027 55.250 -31.531 -35.505 1.00116.77 C ANISOU 1759 CB ASP A1027 15619 17994 10756 4833 -391 -553 C ATOM 1760 CG ASP A1027 56.119 -32.422 -36.365 1.00133.92 C ANISOU 1760 CG ASP A1027 17797 20335 12750 5401 -363 -650 C ATOM 1761 OD1 ASP A1027 56.117 -33.653 -36.142 1.00137.55 O ANISOU 1761 OD1 ASP A1027 18724 20510 13029 5838 -479 -649 O ATOM 1762 OD2 ASP A1027 56.843 -31.883 -37.230 1.00141.83 O ANISOU 1762 OD2 ASP A1027 18351 21762 13775 5416 -218 -733 O ATOM 1763 N ALA A1028 53.371 -30.342 -33.345 1.00111.89 N ANISOU 1763 N ALA A1028 15226 16892 10396 3907 -529 -368 N ATOM 1764 CA ALA A1028 53.169 -29.474 -32.191 1.00110.35 C ANISOU 1764 CA ALA A1028 14850 16769 10309 3560 -595 -312 C ATOM 1765 C ALA A1028 51.941 -29.830 -31.315 1.00113.45 C ANISOU 1765 C ALA A1028 15730 16656 10720 3320 -670 -242 C ATOM 1766 O ALA A1028 51.606 -29.070 -30.403 1.00111.80 O ANISOU 1766 O ALA A1028 15405 16461 10613 2982 -705 -195 O ATOM 1767 CB ALA A1028 53.107 -28.029 -32.648 1.00108.76 C ANISOU 1767 CB ALA A1028 14215 16827 10282 3110 -447 -315 C ATOM 1768 N GLY A1029 51.307 -30.976 -31.585 1.00111.05 N ANISOU 1768 N GLY A1029 15968 15923 10304 3479 -679 -248 N ATOM 1769 CA GLY A1029 50.192 -31.504 -30.800 1.00110.02 C ANISOU 1769 CA GLY A1029 16350 15309 10145 3266 -723 -212 C ATOM 1770 C GLY A1029 48.780 -31.024 -31.090 1.00110.95 C ANISOU 1770 C GLY A1029 16578 15160 10416 2742 -618 -226 C ATOM 1771 O GLY A1029 47.998 -30.821 -30.157 1.00108.20 O ANISOU 1771 O GLY A1029 16378 14614 10119 2422 -644 -201 O ATOM 1772 N TYR A1030 48.418 -30.890 -32.375 1.00107.80 N ANISOU 1772 N TYR A1030 16130 14756 10073 2670 -503 -281 N ATOM 1773 CA TYR A1030 47.060 -30.488 -32.762 1.00105.19 C ANISOU 1773 CA TYR A1030 15895 14208 9864 2232 -424 -326 C ATOM 1774 C TYR A1030 46.303 -31.694 -33.319 1.00111.66 C ANISOU 1774 C TYR A1030 17229 14635 10562 2283 -390 -405 C ATOM 1775 O TYR A1030 46.929 -32.656 -33.782 1.00113.42 O ANISOU 1775 O TYR A1030 17677 14795 10624 2677 -397 -418 O ATOM 1776 CB TYR A1030 47.094 -29.372 -33.829 1.00104.26 C ANISOU 1776 CB TYR A1030 15371 14363 9879 2086 -326 -344 C ATOM 1777 CG TYR A1030 47.318 -27.964 -33.314 1.00103.33 C ANISOU 1777 CG TYR A1030 14827 14531 9903 1827 -318 -288 C ATOM 1778 CD1 TYR A1030 48.578 -27.548 -32.894 1.00106.61 C ANISOU 1778 CD1 TYR A1030 14903 15302 10304 1990 -344 -242 C ATOM 1779 CD2 TYR A1030 46.300 -27.013 -33.356 1.00100.84 C ANISOU 1779 CD2 TYR A1030 14437 14157 9720 1431 -277 -303 C ATOM 1780 CE1 TYR A1030 48.800 -26.248 -32.450 1.00105.88 C ANISOU 1780 CE1 TYR A1030 14446 15461 10323 1715 -319 -204 C ATOM 1781 CE2 TYR A1030 46.514 -25.704 -32.928 1.00100.04 C ANISOU 1781 CE2 TYR A1030 14001 14287 9725 1200 -257 -252 C ATOM 1782 CZ TYR A1030 47.768 -25.327 -32.476 1.00109.40 C ANISOU 1782 CZ TYR A1030 14886 15791 10892 1321 -269 -200 C ATOM 1783 OH TYR A1030 48.005 -24.048 -32.042 1.00111.04 O ANISOU 1783 OH TYR A1030 14791 16214 11184 1059 -235 -161 O ATOM 1784 N GLU A1031 44.958 -31.640 -33.271 1.00108.28 N ANISOU 1784 N GLU A1031 16984 13959 10198 1881 -349 -476 N ATOM 1785 CA GLU A1031 44.096 -32.677 -33.839 1.00109.85 C ANISOU 1785 CA GLU A1031 17641 13809 10289 1821 -298 -588 C ATOM 1786 C GLU A1031 43.733 -32.163 -35.238 1.00113.33 C ANISOU 1786 C GLU A1031 17861 14388 10812 1750 -232 -664 C ATOM 1787 O GLU A1031 42.658 -31.590 -35.450 1.00111.33 O ANISOU 1787 O GLU A1031 17515 14118 10665 1396 -207 -749 O ATOM 1788 CB GLU A1031 42.851 -32.938 -32.961 1.00110.82 C ANISOU 1788 CB GLU A1031 18063 13629 10414 1401 -281 -659 C ATOM 1789 CG GLU A1031 42.265 -34.332 -33.143 1.00124.17 C ANISOU 1789 CG GLU A1031 20361 14907 11911 1383 -227 -764 C ATOM 1790 CD GLU A1031 40.799 -34.423 -33.536 1.00143.05 C ANISOU 1790 CD GLU A1031 22871 17141 14342 927 -146 -948 C ATOM 1791 OE1 GLU A1031 40.081 -35.251 -32.930 1.00130.76 O ANISOU 1791 OE1 GLU A1031 21768 15252 12663 682 -90 -1034 O ATOM 1792 OE2 GLU A1031 40.379 -33.711 -34.478 1.00137.06 O ANISOU 1792 OE2 GLU A1031 21776 16592 13710 822 -135 -1021 O ATOM 1793 N VAL A1032 44.692 -32.319 -36.174 1.00111.46 N ANISOU 1793 N VAL A1032 17518 14317 10514 2116 -210 -638 N ATOM 1794 CA VAL A1032 44.630 -31.842 -37.561 1.00110.42 C ANISOU 1794 CA VAL A1032 17189 14340 10424 2132 -143 -688 C ATOM 1795 C VAL A1032 43.715 -32.696 -38.452 1.00115.02 C ANISOU 1795 C VAL A1032 18145 14646 10913 2070 -106 -826 C ATOM 1796 O VAL A1032 43.839 -33.923 -38.500 1.00116.17 O ANISOU 1796 O VAL A1032 18709 14538 10893 2265 -100 -859 O ATOM 1797 CB VAL A1032 46.039 -31.668 -38.188 1.00115.38 C ANISOU 1797 CB VAL A1032 17551 15277 11011 2519 -107 -623 C ATOM 1798 CG1 VAL A1032 45.973 -30.839 -39.462 1.00114.09 C ANISOU 1798 CG1 VAL A1032 17139 15304 10907 2450 -22 -654 C ATOM 1799 CG2 VAL A1032 47.017 -31.036 -37.200 1.00115.20 C ANISOU 1799 CG2 VAL A1032 17190 15538 11044 2591 -151 -519 C ATOM 1800 N ASP A1033 42.814 -32.006 -39.173 1.00110.83 N ANISOU 1800 N ASP A1033 17465 14173 10471 1809 -86 -913 N ATOM 1801 CA ASP A1033 41.841 -32.551 -40.115 1.00111.53 C ANISOU 1801 CA ASP A1033 17798 14085 10491 1694 -64 -1074 C ATOM 1802 C ASP A1033 42.092 -31.860 -41.465 1.00114.82 C ANISOU 1802 C ASP A1033 17981 14722 10923 1825 -30 -1081 C ATOM 1803 O ASP A1033 41.494 -30.816 -41.738 1.00112.41 O ANISOU 1803 O ASP A1033 17430 14563 10718 1625 -49 -1112 O ATOM 1804 CB ASP A1033 40.408 -32.260 -39.598 1.00112.42 C ANISOU 1804 CB ASP A1033 17917 14109 10688 1244 -96 -1203 C ATOM 1805 CG ASP A1033 39.277 -33.031 -40.259 1.00126.80 C ANISOU 1805 CG ASP A1033 20023 15736 12418 1051 -81 -1417 C ATOM 1806 OD1 ASP A1033 39.104 -32.898 -41.496 1.00129.09 O ANISOU 1806 OD1 ASP A1033 20258 16113 12677 1135 -81 -1494 O ATOM 1807 OD2 ASP A1033 38.508 -33.694 -39.530 1.00132.14 O ANISOU 1807 OD2 ASP A1033 20965 16191 13051 779 -66 -1523 O ATOM 1808 N SER A1034 43.014 -32.405 -42.282 1.00113.67 N ANISOU 1808 N SER A1034 17925 14602 10661 2181 23 -1049 N ATOM 1809 CA SER A1034 43.314 -31.814 -43.589 1.00114.07 C ANISOU 1809 CA SER A1034 17802 14843 10696 2309 79 -1055 C ATOM 1810 C SER A1034 42.465 -32.458 -44.691 1.00119.70 C ANISOU 1810 C SER A1034 18801 15377 11301 2279 79 -1214 C ATOM 1811 O SER A1034 42.560 -33.669 -44.914 1.00121.66 O ANISOU 1811 O SER A1034 19406 15407 11411 2433 99 -1271 O ATOM 1812 CB SER A1034 44.803 -31.899 -43.908 1.00119.63 C ANISOU 1812 CB SER A1034 18376 15739 11338 2687 156 -952 C ATOM 1813 OG SER A1034 45.102 -31.194 -45.104 1.00128.10 O ANISOU 1813 OG SER A1034 19273 17005 12393 2755 238 -953 O ATOM 1814 N ARG A1035 41.607 -31.648 -45.351 1.00114.96 N ANISOU 1814 N ARG A1035 18068 14865 10746 2087 49 -1296 N ATOM 1815 CA ARG A1035 40.689 -32.119 -46.392 1.00115.84 C ANISOU 1815 CA ARG A1035 18398 14860 10756 2029 22 -1475 C ATOM 1816 C ARG A1035 40.650 -31.236 -47.649 1.00120.01 C ANISOU 1816 C ARG A1035 18780 15566 11251 2115 31 -1489 C ATOM 1817 O ARG A1035 40.715 -30.011 -47.546 1.00117.84 O ANISOU 1817 O ARG A1035 18232 15478 11063 2053 25 -1410 O ATOM 1818 CB ARG A1035 39.271 -32.307 -45.816 1.00115.95 C ANISOU 1818 CB ARG A1035 18488 14755 10812 1657 -63 -1645 C ATOM 1819 CG ARG A1035 39.146 -33.485 -44.842 1.00130.31 C ANISOU 1819 CG ARG A1035 20620 16307 12587 1547 -44 -1680 C ATOM 1820 CD ARG A1035 37.707 -33.859 -44.540 1.00142.18 C ANISOU 1820 CD ARG A1035 22247 17691 14084 1146 -87 -1906 C ATOM 1821 NE ARG A1035 37.117 -33.015 -43.500 1.00145.62 N ANISOU 1821 NE ARG A1035 22406 18247 14675 867 -134 -1905 N ATOM 1822 CZ ARG A1035 35.825 -33.000 -43.188 1.00157.33 C ANISOU 1822 CZ ARG A1035 23853 19737 16187 500 -174 -2115 C ATOM 1823 NH1 ARG A1035 34.967 -33.780 -43.838 1.00143.80 N ANISOU 1823 NH1 ARG A1035 22350 17931 14355 336 -174 -2355 N ATOM 1824 NH2 ARG A1035 35.377 -32.201 -42.230 1.00143.35 N ANISOU 1824 NH2 ARG A1035 21824 18088 14554 286 -207 -2104 N ATOM 1825 N ASP A1036 40.531 -31.876 -48.835 1.00118.75 N ANISOU 1825 N ASP A1036 18853 15324 10943 2258 49 -1593 N ATOM 1826 CA ASP A1036 40.441 -31.234 -50.152 1.00119.03 C ANISOU 1826 CA ASP A1036 18850 15480 10895 2365 55 -1627 C ATOM 1827 C ASP A1036 39.058 -30.604 -50.288 1.00122.72 C ANISOU 1827 C ASP A1036 19241 15998 11390 2125 -84 -1782 C ATOM 1828 O ASP A1036 38.075 -31.195 -49.839 1.00122.03 O ANISOU 1828 O ASP A1036 19239 15808 11318 1901 -166 -1945 O ATOM 1829 CB ASP A1036 40.646 -32.288 -51.263 1.00123.45 C ANISOU 1829 CB ASP A1036 19726 15905 11274 2577 104 -1713 C ATOM 1830 CG ASP A1036 41.047 -31.778 -52.645 1.00136.43 C ANISOU 1830 CG ASP A1036 21374 17664 12799 2786 165 -1696 C ATOM 1831 OD1 ASP A1036 40.416 -30.810 -53.134 1.00136.74 O ANISOU 1831 OD1 ASP A1036 21311 17813 12831 2700 96 -1737 O ATOM 1832 OD2 ASP A1036 41.923 -32.408 -53.278 1.00143.59 O ANISOU 1832 OD2 ASP A1036 22430 18536 13594 3048 278 -1658 O ATOM 1833 N ALA A1037 38.979 -29.425 -50.934 1.00120.50 N ANISOU 1833 N ALA A1037 18817 15878 11088 2180 -103 -1749 N ATOM 1834 CA ALA A1037 37.736 -28.670 -51.154 1.00120.84 C ANISOU 1834 CA ALA A1037 18776 16012 11127 2044 -253 -1896 C ATOM 1835 C ALA A1037 36.652 -29.437 -51.939 1.00129.74 C ANISOU 1835 C ALA A1037 20080 17084 12131 1998 -369 -2158 C ATOM 1836 O ALA A1037 35.467 -29.113 -51.815 1.00129.50 O ANISOU 1836 O ALA A1037 19944 17146 12115 1837 -515 -2340 O ATOM 1837 CB ALA A1037 38.037 -27.336 -51.823 1.00121.04 C ANISOU 1837 CB ALA A1037 18724 16172 11095 2183 -232 -1790 C ATOM 1838 N ALA A1038 37.059 -30.458 -52.727 1.00130.06 N ANISOU 1838 N ALA A1038 20380 16995 12041 2140 -303 -2194 N ATOM 1839 CA ALA A1038 36.166 -31.309 -53.522 1.00132.54 C ANISOU 1839 CA ALA A1038 20901 17243 12215 2087 -392 -2448 C ATOM 1840 C ALA A1038 35.590 -32.487 -52.701 1.00138.52 C ANISOU 1840 C ALA A1038 21783 17839 13007 1809 -396 -2599 C ATOM 1841 O ALA A1038 34.728 -33.219 -53.197 1.00140.24 O ANISOU 1841 O ALA A1038 22158 18011 13115 1672 -463 -2846 O ATOM 1842 CB ALA A1038 36.897 -31.823 -54.760 1.00134.93 C ANISOU 1842 CB ALA A1038 21461 17462 12343 2364 -303 -2414 C ATOM 1843 N SER A1039 36.054 -32.659 -51.451 1.00134.62 N ANISOU 1843 N SER A1039 21243 17259 12647 1710 -319 -2461 N ATOM 1844 CA SER A1039 35.578 -33.715 -50.558 1.00135.78 C ANISOU 1844 CA SER A1039 21564 17217 12808 1434 -297 -2578 C ATOM 1845 C SER A1039 34.822 -33.141 -49.349 1.00140.11 C ANISOU 1845 C SER A1039 21854 17867 13516 1123 -357 -2625 C ATOM 1846 O SER A1039 34.404 -33.905 -48.472 1.00140.15 O ANISOU 1846 O SER A1039 21997 17719 13535 850 -320 -2716 O ATOM 1847 CB SER A1039 36.733 -34.611 -50.117 1.00139.41 C ANISOU 1847 CB SER A1039 22288 17445 13235 1606 -159 -2402 C ATOM 1848 OG SER A1039 37.718 -33.878 -49.409 1.00144.76 O ANISOU 1848 OG SER A1039 22742 18219 14042 1761 -111 -2149 O ATOM 1849 N VAL A1040 34.621 -31.799 -49.321 1.00136.85 N ANISOU 1849 N VAL A1040 21102 17696 13200 1161 -440 -2573 N ATOM 1850 CA VAL A1040 33.922 -31.084 -48.237 1.00136.11 C ANISOU 1850 CA VAL A1040 20734 17728 13253 910 -500 -2614 C ATOM 1851 C VAL A1040 32.529 -30.575 -48.656 1.00142.80 C ANISOU 1851 C VAL A1040 21387 18800 14072 769 -658 -2896 C ATOM 1852 O VAL A1040 32.272 -30.360 -49.843 1.00143.54 O ANISOU 1852 O VAL A1040 21498 18997 14043 946 -744 -2995 O ATOM 1853 CB VAL A1040 34.756 -29.940 -47.573 1.00137.44 C ANISOU 1853 CB VAL A1040 20676 17987 13558 1034 -466 -2340 C ATOM 1854 CG1 VAL A1040 36.051 -30.458 -46.953 1.00136.94 C ANISOU 1854 CG1 VAL A1040 20738 17764 13530 1147 -332 -2105 C ATOM 1855 CG2 VAL A1040 35.019 -28.780 -48.531 1.00136.52 C ANISOU 1855 CG2 VAL A1040 20439 18038 13396 1288 -508 -2256 C ATOM 1856 N GLU A1041 31.651 -30.366 -47.656 1.00140.33 N ANISOU 1856 N GLU A1041 20880 18579 13862 468 -698 -3031 N ATOM 1857 CA GLU A1041 30.296 -29.831 -47.801 1.00141.39 C ANISOU 1857 CA GLU A1041 20754 18981 13985 328 -852 -3322 C ATOM 1858 C GLU A1041 30.159 -28.631 -46.851 1.00144.99 C ANISOU 1858 C GLU A1041 20917 19583 14590 308 -888 -3221 C ATOM 1859 O GLU A1041 30.509 -28.739 -45.668 1.00143.19 O ANISOU 1859 O GLU A1041 20683 19239 14483 133 -787 -3090 O ATOM 1860 CB GLU A1041 29.235 -30.912 -47.514 1.00144.84 C ANISOU 1860 CB GLU A1041 21243 19412 14376 -75 -840 -3658 C ATOM 1861 CG GLU A1041 29.077 -31.924 -48.642 1.00156.15 C ANISOU 1861 CG GLU A1041 22941 20762 15629 -64 -844 -3832 C ATOM 1862 CD GLU A1041 28.164 -33.112 -48.395 1.00173.16 C ANISOU 1862 CD GLU A1041 25233 22858 17704 -508 -789 -4161 C ATOM 1863 OE1 GLU A1041 27.933 -33.883 -49.356 1.00163.76 O ANISOU 1863 OE1 GLU A1041 24254 21618 16351 -520 -801 -4335 O ATOM 1864 OE2 GLU A1041 27.688 -33.285 -47.249 1.00163.41 O ANISOU 1864 OE2 GLU A1041 23919 21616 16553 -865 -718 -4251 O ATOM 1865 N ALA A1042 29.678 -27.483 -47.385 1.00142.72 N ANISOU 1865 N ALA A1042 20425 19533 14270 509 -1035 -3278 N ATOM 1866 CA ALA A1042 29.507 -26.200 -46.676 1.00141.53 C ANISOU 1866 CA ALA A1042 20032 19524 14219 554 -1088 -3193 C ATOM 1867 C ALA A1042 28.602 -26.244 -45.425 1.00146.68 C ANISOU 1867 C ALA A1042 20457 20284 14991 205 -1092 -3374 C ATOM 1868 O ALA A1042 28.602 -25.291 -44.640 1.00144.97 O ANISOU 1868 O ALA A1042 20075 20133 14873 214 -1100 -3268 O ATOM 1869 CB ALA A1042 29.010 -25.133 -47.642 1.00142.98 C ANISOU 1869 CB ALA A1042 20131 19916 14278 867 -1261 -3277 C ATOM 1870 N GLY A1043 27.855 -27.339 -45.258 1.00145.43 N ANISOU 1870 N GLY A1043 20315 20133 14809 -115 -1067 -3645 N ATOM 1871 CA GLY A1043 26.954 -27.551 -44.132 1.00145.82 C ANISOU 1871 CA GLY A1043 20180 20280 14945 -505 -1033 -3855 C ATOM 1872 C GLY A1043 27.677 -27.734 -42.813 1.00147.48 C ANISOU 1872 C GLY A1043 20496 20251 15288 -685 -869 -3604 C ATOM 1873 O GLY A1043 28.098 -28.849 -42.485 1.00147.40 O ANISOU 1873 O GLY A1043 20765 19980 15259 -867 -733 -3549 O ATOM 1874 N GLY A1044 27.832 -26.624 -42.083 1.00141.92 N ANISOU 1874 N GLY A1044 19599 19629 14696 -615 -891 -3458 N ATOM 1875 CA GLY A1044 28.487 -26.555 -40.776 1.00139.66 C ANISOU 1875 CA GLY A1044 19367 19162 14534 -757 -765 -3221 C ATOM 1876 C GLY A1044 29.830 -27.253 -40.696 1.00141.68 C ANISOU 1876 C GLY A1044 19937 19112 14784 -663 -645 -2928 C ATOM 1877 O GLY A1044 30.108 -27.952 -39.717 1.00141.32 O ANISOU 1877 O GLY A1044 20054 18869 14771 -880 -530 -2860 O ATOM 1878 N LEU A1045 30.654 -27.088 -41.750 1.00136.72 N ANISOU 1878 N LEU A1045 19407 18450 14092 -321 -671 -2765 N ATOM 1879 CA LEU A1045 31.978 -27.698 -41.900 1.00135.48 C ANISOU 1879 CA LEU A1045 19508 18064 13906 -155 -570 -2513 C ATOM 1880 C LEU A1045 32.957 -27.324 -40.770 1.00136.00 C ANISOU 1880 C LEU A1045 19555 18038 14082 -145 -492 -2232 C ATOM 1881 O LEU A1045 33.714 -28.185 -40.306 1.00135.95 O ANISOU 1881 O LEU A1045 19766 17829 14060 -160 -404 -2116 O ATOM 1882 CB LEU A1045 32.555 -27.330 -43.288 1.00135.55 C ANISOU 1882 CB LEU A1045 19564 18121 13818 197 -610 -2433 C ATOM 1883 CG LEU A1045 33.928 -27.888 -43.676 1.00139.87 C ANISOU 1883 CG LEU A1045 20327 18497 14319 426 -506 -2199 C ATOM 1884 CD1 LEU A1045 33.856 -29.366 -43.990 1.00141.88 C ANISOU 1884 CD1 LEU A1045 20883 18557 14468 370 -455 -2313 C ATOM 1885 CD2 LEU A1045 34.492 -27.144 -44.857 1.00141.31 C ANISOU 1885 CD2 LEU A1045 20483 18778 14431 740 -523 -2089 C ATOM 1886 N PHE A1046 32.914 -26.059 -40.318 1.00129.37 N ANISOU 1886 N PHE A1046 18477 17344 13332 -124 -532 -2144 N ATOM 1887 CA PHE A1046 33.811 -25.532 -39.289 1.00126.88 C ANISOU 1887 CA PHE A1046 18106 16986 13115 -127 -472 -1896 C ATOM 1888 C PHE A1046 33.373 -25.847 -37.848 1.00128.59 C ANISOU 1888 C PHE A1046 18320 17127 13411 -438 -435 -1940 C ATOM 1889 O PHE A1046 34.136 -25.572 -36.922 1.00126.87 O ANISOU 1889 O PHE A1046 18086 16858 13259 -447 -391 -1742 O ATOM 1890 CB PHE A1046 34.033 -24.013 -39.477 1.00127.41 C ANISOU 1890 CB PHE A1046 17980 17213 13217 18 -511 -1778 C ATOM 1891 CG PHE A1046 34.528 -23.498 -40.820 1.00129.37 C ANISOU 1891 CG PHE A1046 18265 17522 13366 307 -524 -1711 C ATOM 1892 CD1 PHE A1046 34.918 -24.379 -41.829 1.00133.68 C ANISOU 1892 CD1 PHE A1046 18983 17998 13813 461 -499 -1731 C ATOM 1893 CD2 PHE A1046 34.620 -22.133 -41.067 1.00130.81 C ANISOU 1893 CD2 PHE A1046 18357 17810 13535 420 -546 -1626 C ATOM 1894 CE1 PHE A1046 35.360 -23.900 -43.066 1.00134.95 C ANISOU 1894 CE1 PHE A1046 19199 18209 13868 714 -495 -1672 C ATOM 1895 CE2 PHE A1046 35.075 -21.656 -42.301 1.00134.17 C ANISOU 1895 CE2 PHE A1046 18877 18264 13840 666 -535 -1562 C ATOM 1896 CZ PHE A1046 35.443 -22.543 -43.290 1.00133.37 C ANISOU 1896 CZ PHE A1046 18921 18107 13647 807 -508 -1586 C ATOM 1897 N GLU A1047 32.170 -26.435 -37.659 1.00125.24 N ANISOU 1897 N GLU A1047 17913 16707 12966 -706 -443 -2210 N ATOM 1898 CA GLU A1047 31.622 -26.771 -36.337 1.00124.77 C ANISOU 1898 CA GLU A1047 17874 16575 12957 -1048 -383 -2290 C ATOM 1899 C GLU A1047 32.514 -27.745 -35.547 1.00126.00 C ANISOU 1899 C GLU A1047 18341 16453 13081 -1087 -285 -2117 C ATOM 1900 O GLU A1047 32.891 -28.804 -36.056 1.00126.53 O ANISOU 1900 O GLU A1047 18690 16345 13041 -1005 -245 -2117 O ATOM 1901 CB GLU A1047 30.168 -27.294 -36.424 1.00128.40 C ANISOU 1901 CB GLU A1047 18295 17118 13371 -1361 -383 -2655 C ATOM 1902 CG GLU A1047 29.152 -26.343 -37.055 1.00142.06 C ANISOU 1902 CG GLU A1047 19690 19169 15116 -1313 -506 -2877 C ATOM 1903 CD GLU A1047 28.750 -25.103 -36.277 1.00168.23 C ANISOU 1903 CD GLU A1047 22722 22665 18533 -1333 -551 -2865 C ATOM 1904 OE1 GLU A1047 28.341 -25.235 -35.101 1.00170.48 O ANISOU 1904 OE1 GLU A1047 22972 22927 18874 -1635 -476 -2931 O ATOM 1905 OE2 GLU A1047 28.783 -24.001 -36.873 1.00160.60 O ANISOU 1905 OE2 GLU A1047 21596 21857 17569 -1052 -657 -2812 O ATOM 1906 N GLY A1048 32.854 -27.345 -34.321 1.00119.59 N ANISOU 1906 N GLY A1048 17493 15602 12344 -1181 -256 -1975 N ATOM 1907 CA GLY A1048 33.702 -28.113 -33.414 1.00118.64 C ANISOU 1907 CA GLY A1048 17656 15242 12181 -1180 -191 -1804 C ATOM 1908 C GLY A1048 35.192 -27.956 -33.657 1.00118.10 C ANISOU 1908 C GLY A1048 17596 15170 12106 -810 -216 -1532 C ATOM 1909 O GLY A1048 35.989 -28.771 -33.177 1.00118.32 O ANISOU 1909 O GLY A1048 17886 15013 12057 -704 -185 -1409 O ATOM 1910 N PHE A1049 35.576 -26.910 -34.412 1.00110.53 N ANISOU 1910 N PHE A1049 16365 14424 11207 -606 -267 -1452 N ATOM 1911 CA PHE A1049 36.968 -26.614 -34.743 1.00108.29 C ANISOU 1911 CA PHE A1049 16024 14205 10917 -295 -268 -1229 C ATOM 1912 C PHE A1049 37.397 -25.288 -34.160 1.00108.01 C ANISOU 1912 C PHE A1049 15714 14341 10984 -309 -284 -1088 C ATOM 1913 O PHE A1049 36.694 -24.282 -34.304 1.00106.47 O ANISOU 1913 O PHE A1049 15335 14271 10848 -410 -312 -1155 O ATOM 1914 CB PHE A1049 37.222 -26.658 -36.265 1.00110.09 C ANISOU 1914 CB PHE A1049 16247 14502 11080 -49 -272 -1253 C ATOM 1915 CG PHE A1049 37.252 -28.050 -36.845 1.00112.70 C ANISOU 1915 CG PHE A1049 16890 14647 11285 44 -244 -1334 C ATOM 1916 CD1 PHE A1049 38.294 -28.924 -36.547 1.00116.41 C ANISOU 1916 CD1 PHE A1049 17572 14981 11677 243 -210 -1206 C ATOM 1917 CD2 PHE A1049 36.243 -28.489 -37.689 1.00115.21 C ANISOU 1917 CD2 PHE A1049 17300 14931 11543 -48 -257 -1550 C ATOM 1918 CE1 PHE A1049 38.316 -30.216 -37.072 1.00119.12 C ANISOU 1918 CE1 PHE A1049 18261 15118 11880 348 -179 -1280 C ATOM 1919 CE2 PHE A1049 36.269 -29.779 -38.222 1.00120.02 C ANISOU 1919 CE2 PHE A1049 18235 15347 12020 15 -220 -1631 C ATOM 1920 CZ PHE A1049 37.307 -30.634 -37.911 1.00119.14 C ANISOU 1920 CZ PHE A1049 18376 15063 11827 215 -175 -1488 C ATOM 1921 N ASP A1050 38.556 -25.296 -33.493 1.00102.79 N ANISOU 1921 N ASP A1050 15039 13690 10325 -197 -272 -905 N ATOM 1922 CA ASP A1050 39.123 -24.110 -32.859 1.00100.59 C ANISOU 1922 CA ASP A1050 14520 13573 10126 -234 -276 -768 C ATOM 1923 C ASP A1050 39.745 -23.183 -33.901 1.00100.51 C ANISOU 1923 C ASP A1050 14329 13748 10111 -74 -248 -700 C ATOM 1924 O ASP A1050 39.401 -21.994 -33.954 1.00 98.74 O ANISOU 1924 O ASP A1050 13962 13622 9933 -176 -246 -698 O ATOM 1925 CB ASP A1050 40.137 -24.516 -31.776 1.00103.37 C ANISOU 1925 CB ASP A1050 14913 13902 10459 -172 -286 -629 C ATOM 1926 CG ASP A1050 39.533 -25.376 -30.677 1.00116.62 C ANISOU 1926 CG ASP A1050 16839 15360 12111 -345 -299 -684 C ATOM 1927 OD1 ASP A1050 38.564 -24.918 -30.024 1.00115.68 O ANISOU 1927 OD1 ASP A1050 16683 15212 12058 -626 -295 -762 O ATOM 1928 OD2 ASP A1050 40.024 -26.509 -30.473 1.00126.60 O ANISOU 1928 OD2 ASP A1050 18360 16474 13269 -193 -305 -655 O ATOM 1929 N LEU A1051 40.615 -23.763 -34.766 1.00 94.72 N ANISOU 1929 N LEU A1051 13644 13046 9301 180 -215 -656 N ATOM 1930 CA LEU A1051 41.346 -23.092 -35.840 1.00 92.19 C ANISOU 1930 CA LEU A1051 13197 12888 8942 337 -155 -597 C ATOM 1931 C LEU A1051 41.016 -23.705 -37.194 1.00 93.84 C ANISOU 1931 C LEU A1051 13556 13034 9066 502 -144 -695 C ATOM 1932 O LEU A1051 41.110 -24.922 -37.359 1.00 94.68 O ANISOU 1932 O LEU A1051 13842 13019 9112 626 -153 -738 O ATOM 1933 CB LEU A1051 42.858 -23.170 -35.547 1.00 92.48 C ANISOU 1933 CB LEU A1051 13101 13082 8955 490 -109 -464 C ATOM 1934 CG LEU A1051 43.853 -22.692 -36.604 1.00 96.97 C ANISOU 1934 CG LEU A1051 13538 13846 9461 649 -8 -415 C ATOM 1935 CD1 LEU A1051 43.724 -21.189 -36.899 1.00 95.77 C ANISOU 1935 CD1 LEU A1051 13267 13797 9326 474 58 -383 C ATOM 1936 CD2 LEU A1051 45.259 -23.027 -36.182 1.00100.13 C ANISOU 1936 CD2 LEU A1051 13781 14434 9831 809 20 -338 C ATOM 1937 N VAL A1052 40.618 -22.855 -38.159 1.00 87.56 N ANISOU 1937 N VAL A1052 12722 12303 8242 510 -128 -733 N ATOM 1938 CA VAL A1052 40.310 -23.269 -39.533 1.00 86.94 C ANISOU 1938 CA VAL A1052 12781 12188 8067 672 -125 -828 C ATOM 1939 C VAL A1052 41.313 -22.606 -40.492 1.00 88.99 C ANISOU 1939 C VAL A1052 12977 12584 8249 829 -20 -729 C ATOM 1940 O VAL A1052 41.416 -21.378 -40.527 1.00 88.03 O ANISOU 1940 O VAL A1052 12768 12552 8129 745 21 -669 O ATOM 1941 CB VAL A1052 38.841 -23.016 -39.969 1.00 89.99 C ANISOU 1941 CB VAL A1052 13226 12525 8441 580 -215 -1002 C ATOM 1942 CG1 VAL A1052 38.522 -23.792 -41.244 1.00 90.88 C ANISOU 1942 CG1 VAL A1052 13505 12583 8443 741 -231 -1122 C ATOM 1943 CG2 VAL A1052 37.852 -23.378 -38.863 1.00 89.16 C ANISOU 1943 CG2 VAL A1052 13118 12340 8420 346 -285 -1111 C ATOM 1944 N LEU A1053 42.063 -23.407 -41.246 1.00 84.81 N ANISOU 1944 N LEU A1053 12520 12066 7638 1045 40 -719 N ATOM 1945 CA LEU A1053 43.038 -22.846 -42.173 1.00 84.90 C ANISOU 1945 CA LEU A1053 12471 12224 7564 1172 169 -646 C ATOM 1946 C LEU A1053 42.593 -23.049 -43.619 1.00 89.30 C ANISOU 1946 C LEU A1053 13218 12714 7998 1321 177 -734 C ATOM 1947 O LEU A1053 42.590 -24.175 -44.120 1.00 89.68 O ANISOU 1947 O LEU A1053 13405 12679 7991 1482 161 -801 O ATOM 1948 CB LEU A1053 44.458 -23.389 -41.927 1.00 85.89 C ANISOU 1948 CB LEU A1053 12466 12492 7675 1321 257 -565 C ATOM 1949 CG LEU A1053 45.048 -23.159 -40.548 1.00 88.95 C ANISOU 1949 CG LEU A1053 12650 12988 8157 1208 240 -483 C ATOM 1950 CD1 LEU A1053 44.989 -24.421 -39.746 1.00 89.56 C ANISOU 1950 CD1 LEU A1053 12831 12942 8256 1312 142 -506 C ATOM 1951 CD2 LEU A1053 46.484 -22.745 -40.640 1.00 91.27 C ANISOU 1951 CD2 LEU A1053 12704 13561 8414 1269 373 -413 C ATOM 1952 N LEU A1054 42.194 -21.958 -44.277 1.00 85.89 N ANISOU 1952 N LEU A1054 12831 12302 7503 1277 195 -738 N ATOM 1953 CA LEU A1054 41.722 -22.013 -45.656 1.00 87.36 C ANISOU 1953 CA LEU A1054 13216 12430 7548 1429 184 -824 C ATOM 1954 C LEU A1054 42.806 -21.641 -46.670 1.00 90.73 C ANISOU 1954 C LEU A1054 13682 12951 7842 1551 364 -744 C ATOM 1955 O LEU A1054 43.423 -20.577 -46.572 1.00 89.06 O ANISOU 1955 O LEU A1054 13399 12834 7605 1444 487 -645 O ATOM 1956 CB LEU A1054 40.444 -21.171 -45.839 1.00 87.44 C ANISOU 1956 CB LEU A1054 13310 12386 7527 1365 60 -912 C ATOM 1957 CG LEU A1054 39.229 -21.561 -44.966 1.00 91.99 C ANISOU 1957 CG LEU A1054 13829 12905 8216 1232 -108 -1043 C ATOM 1958 CD1 LEU A1054 38.165 -20.478 -45.007 1.00 92.24 C ANISOU 1958 CD1 LEU A1054 13877 12953 8215 1194 -215 -1120 C ATOM 1959 CD2 LEU A1054 38.625 -22.903 -45.394 1.00 95.19 C ANISOU 1959 CD2 LEU A1054 14346 13228 8595 1297 -189 -1205 C ATOM 1960 N GLY A1055 43.035 -22.543 -47.619 1.00 88.50 N ANISOU 1960 N GLY A1055 13524 12637 7464 1753 395 -799 N ATOM 1961 CA GLY A1055 44.060 -22.373 -48.639 1.00 90.33 C ANISOU 1961 CA GLY A1055 13799 12964 7558 1880 582 -748 C ATOM 1962 C GLY A1055 43.562 -22.440 -50.061 1.00 96.09 C ANISOU 1962 C GLY A1055 14799 13598 8112 2038 572 -829 C ATOM 1963 O GLY A1055 42.859 -23.384 -50.434 1.00 95.51 O ANISOU 1963 O GLY A1055 14857 13412 8019 2151 448 -945 O ATOM 1964 N CYS A1056 43.954 -21.455 -50.877 1.00 95.10 N ANISOU 1964 N CYS A1056 14784 13510 7837 2034 715 -774 N ATOM 1965 CA CYS A1056 43.523 -21.419 -52.267 1.00 97.32 C ANISOU 1965 CA CYS A1056 15361 13697 7918 2199 710 -841 C ATOM 1966 C CYS A1056 44.513 -20.734 -53.209 1.00102.04 C ANISOU 1966 C CYS A1056 16077 14361 8331 2215 963 -764 C ATOM 1967 O CYS A1056 45.046 -19.671 -52.891 1.00101.60 O ANISOU 1967 O CYS A1056 15974 14372 8255 2032 1108 -669 O ATOM 1968 CB CYS A1056 42.133 -20.801 -52.372 1.00 97.82 C ANISOU 1968 CB CYS A1056 15586 13644 7936 2192 505 -919 C ATOM 1969 SG CYS A1056 41.482 -20.739 -54.056 1.00104.19 S ANISOU 1969 SG CYS A1056 16772 14346 8470 2435 444 -1024 S ATOM 1970 N SER A1057 44.716 -21.335 -54.390 1.00 99.80 N ANISOU 1970 N SER A1057 15978 14047 7895 2413 1027 -818 N ATOM 1971 CA SER A1057 45.574 -20.798 -55.446 1.00101.91 C ANISOU 1971 CA SER A1057 16408 14361 7952 2436 1282 -771 C ATOM 1972 C SER A1057 44.809 -19.773 -56.294 1.00108.56 C ANISOU 1972 C SER A1057 17632 15040 8575 2458 1242 -773 C ATOM 1973 O SER A1057 43.612 -19.946 -56.520 1.00107.75 O ANISOU 1973 O SER A1057 17683 14811 8447 2586 994 -864 O ATOM 1974 CB SER A1057 46.090 -21.922 -56.337 1.00105.18 C ANISOU 1974 CB SER A1057 16877 14804 8283 2660 1364 -835 C ATOM 1975 OG SER A1057 45.047 -22.774 -56.786 1.00107.34 O ANISOU 1975 OG SER A1057 17331 14919 8533 2841 1137 -950 O ATOM 1976 N THR A1058 45.489 -18.709 -56.756 1.00108.21 N ANISOU 1976 N THR A1058 17756 15006 8354 2333 1487 -688 N ATOM 1977 CA THR A1058 44.861 -17.679 -57.593 1.00110.12 C ANISOU 1977 CA THR A1058 18446 15061 8335 2382 1471 -676 C ATOM 1978 C THR A1058 44.895 -18.105 -59.066 1.00118.63 C ANISOU 1978 C THR A1058 19845 16060 9168 2609 1530 -733 C ATOM 1979 O THR A1058 45.845 -18.763 -59.495 1.00119.76 O ANISOU 1979 O THR A1058 19887 16320 9297 2629 1731 -739 O ATOM 1980 CB THR A1058 45.453 -16.284 -57.316 1.00120.37 C ANISOU 1980 CB THR A1058 19859 16346 9528 2111 1703 -559 C ATOM 1981 OG1 THR A1058 45.496 -16.068 -55.904 1.00119.05 O ANISOU 1981 OG1 THR A1058 19348 16277 9609 1904 1645 -517 O ATOM 1982 CG2 THR A1058 44.640 -15.164 -57.959 1.00119.89 C ANISOU 1982 CG2 THR A1058 20316 16043 9192 2191 1637 -540 C ATOM 1983 N TRP A1059 43.821 -17.786 -59.817 1.00116.98 N ANISOU 1983 N TRP A1059 20009 15674 8765 2808 1332 -793 N ATOM 1984 CA TRP A1059 43.654 -18.144 -61.227 1.00119.07 C ANISOU 1984 CA TRP A1059 20627 15842 8772 3050 1333 -861 C ATOM 1985 C TRP A1059 43.026 -17.014 -62.042 1.00128.19 C ANISOU 1985 C TRP A1059 22308 16798 9599 3171 1283 -846 C ATOM 1986 O TRP A1059 42.740 -15.945 -61.501 1.00126.93 O ANISOU 1986 O TRP A1059 22252 16566 9411 3071 1256 -781 O ATOM 1987 CB TRP A1059 42.826 -19.433 -61.346 1.00116.24 C ANISOU 1987 CB TRP A1059 20140 15500 8525 3258 1052 -1015 C ATOM 1988 CG TRP A1059 43.541 -20.629 -60.800 1.00116.03 C ANISOU 1988 CG TRP A1059 19736 15613 8736 3201 1132 -1028 C ATOM 1989 CD1 TRP A1059 43.548 -21.053 -59.506 1.00116.68 C ANISOU 1989 CD1 TRP A1059 19432 15791 9110 3067 1052 -1020 C ATOM 1990 CD2 TRP A1059 44.423 -21.507 -61.516 1.00117.43 C ANISOU 1990 CD2 TRP A1059 19921 15845 8851 3301 1323 -1045 C ATOM 1991 NE1 TRP A1059 44.369 -22.145 -59.370 1.00116.39 N ANISOU 1991 NE1 TRP A1059 19184 15854 9184 3100 1166 -1029 N ATOM 1992 CE2 TRP A1059 44.905 -22.458 -60.591 1.00119.97 C ANISOU 1992 CE2 TRP A1059 19861 16292 9430 3253 1329 -1050 C ATOM 1993 CE3 TRP A1059 44.829 -21.605 -62.860 1.00121.16 C ANISOU 1993 CE3 TRP A1059 20710 16266 9059 3447 1484 -1063 C ATOM 1994 CZ2 TRP A1059 45.775 -23.490 -60.963 1.00120.47 C ANISOU 1994 CZ2 TRP A1059 19846 16437 9492 3377 1482 -1078 C ATOM 1995 CZ3 TRP A1059 45.686 -22.632 -63.229 1.00123.66 C ANISOU 1995 CZ3 TRP A1059 20922 16673 9389 3541 1649 -1093 C ATOM 1996 CH2 TRP A1059 46.150 -23.560 -62.287 1.00123.19 C ANISOU 1996 CH2 TRP A1059 20476 16744 9586 3521 1642 -1103 C ATOM 1997 N GLY A1060 42.853 -17.255 -63.341 1.00130.48 N ANISOU 1997 N GLY A1060 22961 16992 9624 3400 1275 -905 N ATOM 1998 CA GLY A1060 42.231 -16.313 -64.262 1.00133.92 C ANISOU 1998 CA GLY A1060 23964 17225 9697 3593 1199 -907 C ATOM 1999 C GLY A1060 43.160 -15.567 -65.198 1.00143.96 C ANISOU 1999 C GLY A1060 25695 18365 10638 3514 1561 -797 C ATOM 2000 O GLY A1060 44.057 -14.846 -64.744 1.00144.27 O ANISOU 2000 O GLY A1060 25715 18416 10687 3209 1865 -676 O ATOM 2001 N ASP A1061 42.907 -15.707 -66.527 1.00144.55 N ANISOU 2001 N ASP A1061 26213 18313 10396 3773 1532 -854 N ATOM 2002 CA ASP A1061 43.627 -15.022 -67.610 1.00148.34 C ANISOU 2002 CA ASP A1061 27246 18626 10492 3737 1860 -770 C ATOM 2003 C ASP A1061 43.314 -13.528 -67.527 1.00156.17 C ANISOU 2003 C ASP A1061 28727 19388 11222 3705 1881 -673 C ATOM 2004 O ASP A1061 44.195 -12.689 -67.734 1.00158.25 O ANISOU 2004 O ASP A1061 29305 19540 11282 3447 2259 -557 O ATOM 2005 CB ASP A1061 43.151 -15.520 -69.001 1.00151.67 C ANISOU 2005 CB ASP A1061 28067 18941 10619 4087 1730 -871 C ATOM 2006 CG ASP A1061 43.377 -16.984 -69.323 1.00156.57 C ANISOU 2006 CG ASP A1061 28355 19726 11407 4170 1707 -979 C ATOM 2007 OD1 ASP A1061 43.924 -17.273 -70.405 1.00158.32 O ANISOU 2007 OD1 ASP A1061 28863 19895 11396 4239 1910 -987 O ATOM 2008 OD2 ASP A1061 42.928 -17.842 -68.537 1.00159.53 O ANISOU 2008 OD2 ASP A1061 28238 20258 12117 4183 1474 -1064 O ATOM 2009 N ASP A1062 42.037 -13.215 -67.226 1.00153.00 N ANISOU 2009 N ASP A1062 28399 18922 10813 3968 1478 -739 N ATOM 2010 CA ASP A1062 41.481 -11.870 -67.186 1.00154.76 C ANISOU 2010 CA ASP A1062 29131 18910 10760 4068 1401 -676 C ATOM 2011 C ASP A1062 41.504 -11.254 -65.774 1.00156.65 C ANISOU 2011 C ASP A1062 29062 19200 11259 3806 1411 -603 C ATOM 2012 O ASP A1062 42.378 -10.426 -65.509 1.00157.11 O ANISOU 2012 O ASP A1062 29301 19158 11234 3473 1761 -467 O ATOM 2013 CB ASP A1062 40.070 -11.867 -67.830 1.00157.87 C ANISOU 2013 CB ASP A1062 29819 19231 10932 4581 944 -821 C ATOM 2014 CG ASP A1062 40.009 -12.519 -69.221 1.00170.11 C ANISOU 2014 CG ASP A1062 31666 20744 12225 4845 908 -908 C ATOM 2015 OD1 ASP A1062 40.228 -13.754 -69.318 1.00168.04 O ANISOU 2015 OD1 ASP A1062 30972 20678 12198 4802 895 -995 O ATOM 2016 OD2 ASP A1062 39.727 -11.801 -70.204 1.00180.16 O ANISOU 2016 OD2 ASP A1062 33633 21777 13043 5107 886 -891 O ATOM 2017 N SER A1063 40.581 -11.663 -64.873 1.00150.90 N ANISOU 2017 N SER A1063 27871 18632 10832 3922 1050 -706 N ATOM 2018 CA SER A1063 40.478 -11.135 -63.500 1.00148.78 C ANISOU 2018 CA SER A1063 27298 18418 10815 3707 1018 -653 C ATOM 2019 C SER A1063 41.039 -12.099 -62.428 1.00149.86 C ANISOU 2019 C SER A1063 26685 18828 11427 3403 1084 -659 C ATOM 2020 O SER A1063 41.534 -13.179 -62.775 1.00149.94 O ANISOU 2020 O SER A1063 26433 18976 11559 3376 1160 -703 O ATOM 2021 CB SER A1063 39.032 -10.747 -63.187 1.00151.63 C ANISOU 2021 CB SER A1063 27719 18757 11136 4052 588 -768 C ATOM 2022 OG SER A1063 38.917 -10.016 -61.976 1.00156.17 O ANISOU 2022 OG SER A1063 28137 19328 11871 3873 580 -706 O ATOM 2023 N ILE A1064 40.979 -11.691 -61.133 1.00142.94 N ANISOU 2023 N ILE A1064 25506 18013 10792 3192 1057 -614 N ATOM 2024 CA ILE A1064 41.453 -12.470 -59.986 1.00139.26 C ANISOU 2024 CA ILE A1064 24381 17782 10748 2921 1097 -610 C ATOM 2025 C ILE A1064 40.406 -13.508 -59.542 1.00139.57 C ANISOU 2025 C ILE A1064 24011 17976 11045 3110 725 -773 C ATOM 2026 O ILE A1064 39.623 -13.264 -58.613 1.00137.80 O ANISOU 2026 O ILE A1064 23595 17790 10973 3117 508 -820 O ATOM 2027 CB ILE A1064 41.919 -11.543 -58.831 1.00141.53 C ANISOU 2027 CB ILE A1064 24566 18060 11148 2587 1256 -491 C ATOM 2028 N GLU A1065 40.407 -14.673 -60.221 1.00134.82 N ANISOU 2028 N GLU A1065 23295 17458 10475 3243 673 -870 N ATOM 2029 CA GLU A1065 39.495 -15.799 -59.971 1.00132.46 C ANISOU 2029 CA GLU A1065 22660 17291 10379 3379 366 -1046 C ATOM 2030 C GLU A1065 40.093 -16.844 -59.006 1.00132.83 C ANISOU 2030 C GLU A1065 22188 17498 10785 3145 445 -1034 C ATOM 2031 O GLU A1065 41.317 -16.958 -58.904 1.00132.97 O ANISOU 2031 O GLU A1065 22107 17558 10857 2961 735 -916 O ATOM 2032 CB GLU A1065 39.086 -16.464 -61.296 1.00135.49 C ANISOU 2032 CB GLU A1065 23285 17645 10549 3666 249 -1175 C ATOM 2033 CG GLU A1065 38.203 -15.590 -62.173 1.00147.50 C ANISOU 2033 CG GLU A1065 25289 19037 11717 3981 60 -1238 C ATOM 2034 CD GLU A1065 38.706 -15.397 -63.590 1.00170.21 C ANISOU 2034 CD GLU A1065 28675 21762 14234 4138 224 -1191 C ATOM 2035 OE1 GLU A1065 38.979 -14.235 -63.971 1.00160.03 O ANISOU 2035 OE1 GLU A1065 27853 20289 12664 4165 368 -1071 O ATOM 2036 OE2 GLU A1065 38.819 -16.404 -64.327 1.00167.89 O ANISOU 2036 OE2 GLU A1065 28352 21516 13920 4228 217 -1276 O ATOM 2037 N LEU A1066 39.223 -17.604 -58.306 1.00125.73 N ANISOU 2037 N LEU A1066 20969 16696 10108 3156 190 -1171 N ATOM 2038 CA LEU A1066 39.617 -18.653 -57.356 1.00122.47 C ANISOU 2038 CA LEU A1066 20133 16395 10004 2971 223 -1175 C ATOM 2039 C LEU A1066 39.696 -20.036 -58.020 1.00125.40 C ANISOU 2039 C LEU A1066 20481 16787 10378 3084 202 -1282 C ATOM 2040 O LEU A1066 39.241 -20.201 -59.155 1.00126.56 O ANISOU 2040 O LEU A1066 20896 16881 10310 3297 113 -1382 O ATOM 2041 CB LEU A1066 38.655 -18.672 -56.155 1.00120.28 C ANISOU 2041 CB LEU A1066 19573 16183 9945 2873 -3 -1262 C ATOM 2042 CG LEU A1066 39.134 -17.953 -54.894 1.00123.40 C ANISOU 2042 CG LEU A1066 19769 16605 10513 2627 106 -1119 C ATOM 2043 CD1 LEU A1066 39.078 -16.440 -55.046 1.00124.46 C ANISOU 2043 CD1 LEU A1066 20186 16646 10458 2645 156 -1027 C ATOM 2044 CD2 LEU A1066 38.313 -18.369 -53.690 1.00123.95 C ANISOU 2044 CD2 LEU A1066 19518 16750 10828 2510 -87 -1219 C ATOM 2045 N GLN A1067 40.303 -21.016 -57.318 1.00119.76 N ANISOU 2045 N GLN A1067 19481 16137 9884 2959 285 -1260 N ATOM 2046 CA GLN A1067 40.472 -22.401 -57.773 1.00119.75 C ANISOU 2046 CA GLN A1067 19471 16130 9897 3054 286 -1351 C ATOM 2047 C GLN A1067 39.090 -23.059 -57.906 1.00125.22 C ANISOU 2047 C GLN A1067 20184 16803 10591 3118 -5 -1572 C ATOM 2048 O GLN A1067 38.241 -22.840 -57.048 1.00123.41 O ANISOU 2048 O GLN A1067 19782 16616 10492 3003 -174 -1643 O ATOM 2049 CB GLN A1067 41.383 -23.164 -56.794 1.00119.26 C ANISOU 2049 CB GLN A1067 19122 16132 10058 2927 418 -1272 C ATOM 2050 CG GLN A1067 42.075 -24.385 -57.383 1.00115.56 C ANISOU 2050 CG GLN A1067 18709 15651 9549 3067 528 -1302 C ATOM 2051 CD GLN A1067 41.235 -25.634 -57.289 1.00117.02 C ANISOU 2051 CD GLN A1067 18923 15753 9787 3101 339 -1470 C ATOM 2052 OE1 GLN A1067 40.276 -25.720 -56.517 1.00105.33 O ANISOU 2052 OE1 GLN A1067 17334 14259 8429 2967 153 -1559 O ATOM 2053 NE2 GLN A1067 41.597 -26.645 -58.062 1.00106.77 N ANISOU 2053 NE2 GLN A1067 17784 14397 8387 3261 403 -1527 N ATOM 2054 N ASP A1068 38.859 -23.822 -58.995 1.00125.42 N ANISOU 2054 N ASP A1068 20416 16782 10455 3285 -53 -1696 N ATOM 2055 CA ASP A1068 37.573 -24.455 -59.320 1.00126.82 C ANISOU 2055 CA ASP A1068 20631 16969 10585 3334 -317 -1943 C ATOM 2056 C ASP A1068 36.913 -25.205 -58.149 1.00131.95 C ANISOU 2056 C ASP A1068 21011 17656 11468 3117 -441 -2062 C ATOM 2057 O ASP A1068 35.752 -24.915 -57.859 1.00131.83 O ANISOU 2057 O ASP A1068 20893 17726 11470 3064 -658 -2226 O ATOM 2058 CB ASP A1068 37.671 -25.356 -60.558 1.00130.37 C ANISOU 2058 CB ASP A1068 21333 17353 10848 3504 -301 -2044 C ATOM 2059 N ASP A1069 37.638 -26.126 -57.465 1.00129.10 N ANISOU 2059 N ASP A1069 20548 17238 11265 3002 -304 -1991 N ATOM 2060 CA ASP A1069 37.097 -26.898 -56.331 1.00128.53 C ANISOU 2060 CA ASP A1069 20294 17157 11386 2780 -387 -2090 C ATOM 2061 C ASP A1069 36.767 -26.022 -55.117 1.00132.06 C ANISOU 2061 C ASP A1069 20486 17686 12006 2603 -441 -2031 C ATOM 2062 O ASP A1069 35.894 -26.390 -54.330 1.00131.40 O ANISOU 2062 O ASP A1069 20263 17628 12037 2412 -563 -2174 O ATOM 2063 CB ASP A1069 38.056 -28.035 -55.900 1.00130.45 C ANISOU 2063 CB ASP A1069 20562 17290 11713 2759 -223 -2003 C ATOM 2064 CG ASP A1069 38.425 -29.068 -56.958 1.00141.38 C ANISOU 2064 CG ASP A1069 22213 18569 12936 2933 -155 -2065 C ATOM 2065 OD1 ASP A1069 37.564 -29.387 -57.810 1.00143.14 O ANISOU 2065 OD1 ASP A1069 22594 18776 13015 2967 -287 -2261 O ATOM 2066 OD2 ASP A1069 39.548 -29.617 -56.884 1.00145.88 O ANISOU 2066 OD2 ASP A1069 22824 19085 13519 3039 21 -1938 O ATOM 2067 N PHE A1070 37.459 -24.868 -54.973 1.00129.21 N ANISOU 2067 N PHE A1070 20082 17364 11650 2644 -332 -1832 N ATOM 2068 CA PHE A1070 37.328 -23.923 -53.855 1.00127.98 C ANISOU 2068 CA PHE A1070 19718 17270 11639 2490 -351 -1745 C ATOM 2069 C PHE A1070 36.182 -22.891 -53.982 1.00133.90 C ANISOU 2069 C PHE A1070 20469 18096 12312 2532 -543 -1858 C ATOM 2070 O PHE A1070 35.698 -22.420 -52.949 1.00131.77 O ANISOU 2070 O PHE A1070 20007 17881 12178 2384 -614 -1869 O ATOM 2071 CB PHE A1070 38.664 -23.204 -53.602 1.00129.10 C ANISOU 2071 CB PHE A1070 19825 17419 11808 2479 -125 -1494 C ATOM 2072 CG PHE A1070 38.853 -22.769 -52.171 1.00128.83 C ANISOU 2072 CG PHE A1070 19544 17428 11977 2268 -100 -1393 C ATOM 2073 CD1 PHE A1070 39.366 -23.647 -51.223 1.00131.34 C ANISOU 2073 CD1 PHE A1070 19705 17736 12461 2157 -43 -1350 C ATOM 2074 CD2 PHE A1070 38.513 -21.484 -51.766 1.00130.02 C ANISOU 2074 CD2 PHE A1070 19655 17614 12131 2201 -137 -1342 C ATOM 2075 CE1 PHE A1070 39.526 -23.248 -49.891 1.00130.62 C ANISOU 2075 CE1 PHE A1070 19401 17686 12543 1968 -31 -1261 C ATOM 2076 CE2 PHE A1070 38.665 -21.090 -50.434 1.00131.15 C ANISOU 2076 CE2 PHE A1070 19582 17793 12455 1998 -116 -1255 C ATOM 2077 CZ PHE A1070 39.181 -21.970 -49.508 1.00128.49 C ANISOU 2077 CZ PHE A1070 19071 17462 12288 1877 -64 -1214 C ATOM 2078 N ILE A1071 35.758 -22.536 -55.223 1.00134.19 N ANISOU 2078 N ILE A1071 20732 18139 12116 2759 -634 -1947 N ATOM 2079 CA ILE A1071 34.658 -21.580 -55.474 1.00135.49 C ANISOU 2079 CA ILE A1071 20937 18388 12156 2889 -846 -2076 C ATOM 2080 C ILE A1071 33.314 -22.062 -54.820 1.00141.76 C ANISOU 2080 C ILE A1071 21473 19326 13062 2764 -1076 -2347 C ATOM 2081 O ILE A1071 32.707 -21.228 -54.136 1.00141.33 O ANISOU 2081 O ILE A1071 21281 19360 13059 2739 -1177 -2380 O ATOM 2082 CB ILE A1071 34.489 -21.170 -56.976 1.00140.66 C ANISOU 2082 CB ILE A1071 21927 19016 12500 3197 -913 -2125 C ATOM 2083 CG1 ILE A1071 35.835 -20.769 -57.615 1.00141.45 C ANISOU 2083 CG1 ILE A1071 22285 18979 12479 3266 -643 -1879 C ATOM 2084 CG2 ILE A1071 33.471 -20.023 -57.132 1.00142.19 C ANISOU 2084 CG2 ILE A1071 22195 19290 12540 3391 -1131 -2228 C ATOM 2085 CD1 ILE A1071 35.952 -21.049 -59.110 1.00150.91 C ANISOU 2085 CD1 ILE A1071 23812 20119 13409 3505 -639 -1931 C ATOM 2086 N PRO A1072 32.856 -23.360 -54.930 1.00139.90 N ANISOU 2086 N PRO A1072 21172 19118 12866 2653 -1137 -2548 N ATOM 2087 CA PRO A1072 31.598 -23.760 -54.256 1.00140.19 C ANISOU 2087 CA PRO A1072 20953 19314 13000 2467 -1316 -2825 C ATOM 2088 C PRO A1072 31.583 -23.497 -52.747 1.00142.37 C ANISOU 2088 C PRO A1072 20980 19605 13511 2214 -1261 -2749 C ATOM 2089 O PRO A1072 30.539 -23.143 -52.197 1.00142.27 O ANISOU 2089 O PRO A1072 20753 19761 13544 2137 -1412 -2937 O ATOM 2090 CB PRO A1072 31.487 -25.259 -54.565 1.00142.94 C ANISOU 2090 CB PRO A1072 21355 19610 13344 2327 -1296 -2986 C ATOM 2091 CG PRO A1072 32.268 -25.452 -55.796 1.00148.27 C ANISOU 2091 CG PRO A1072 22327 20163 13844 2562 -1212 -2877 C ATOM 2092 CD PRO A1072 33.422 -24.505 -55.676 1.00142.44 C ANISOU 2092 CD PRO A1072 21668 19328 13124 2677 -1036 -2552 C ATOM 2093 N LEU A1073 32.750 -23.637 -52.096 1.00137.21 N ANISOU 2093 N LEU A1073 20345 18796 12992 2103 -1049 -2485 N ATOM 2094 CA LEU A1073 32.935 -23.379 -50.672 1.00135.21 C ANISOU 2094 CA LEU A1073 19894 18533 12947 1878 -978 -2375 C ATOM 2095 C LEU A1073 32.900 -21.870 -50.389 1.00138.90 C ANISOU 2095 C LEU A1073 20317 19058 13401 1973 -1007 -2260 C ATOM 2096 O LEU A1073 32.282 -21.468 -49.404 1.00137.71 O ANISOU 2096 O LEU A1073 19968 18990 13366 1831 -1072 -2322 O ATOM 2097 CB LEU A1073 34.269 -23.992 -50.203 1.00134.13 C ANISOU 2097 CB LEU A1073 19809 18239 12916 1794 -763 -2140 C ATOM 2098 CG LEU A1073 34.648 -23.846 -48.728 1.00136.81 C ANISOU 2098 CG LEU A1073 19972 18554 13456 1575 -681 -2004 C ATOM 2099 CD1 LEU A1073 34.007 -24.932 -47.883 1.00137.17 C ANISOU 2099 CD1 LEU A1073 19943 18565 13609 1320 -715 -2165 C ATOM 2100 CD2 LEU A1073 36.143 -23.904 -48.558 1.00138.13 C ANISOU 2100 CD2 LEU A1073 20186 18636 13661 1623 -487 -1742 C ATOM 2101 N PHE A1074 33.555 -21.048 -51.247 1.00136.57 N ANISOU 2101 N PHE A1074 20239 18705 12947 2201 -943 -2100 N ATOM 2102 CA PHE A1074 33.639 -19.585 -51.104 1.00136.61 C ANISOU 2102 CA PHE A1074 20315 18707 12885 2300 -937 -1972 C ATOM 2103 C PHE A1074 32.276 -18.901 -51.058 1.00143.81 C ANISOU 2103 C PHE A1074 21158 19761 13721 2424 -1176 -2187 C ATOM 2104 O PHE A1074 32.043 -18.061 -50.185 1.00142.71 O ANISOU 2104 O PHE A1074 20920 19649 13653 2363 -1194 -2145 O ATOM 2105 CB PHE A1074 34.518 -18.964 -52.208 1.00139.17 C ANISOU 2105 CB PHE A1074 20961 18920 12997 2504 -808 -1801 C ATOM 2106 CG PHE A1074 34.766 -17.476 -52.069 1.00140.41 C ANISOU 2106 CG PHE A1074 21280 19016 13052 2565 -750 -1646 C ATOM 2107 CD1 PHE A1074 35.766 -16.995 -51.227 1.00141.91 C ANISOU 2107 CD1 PHE A1074 21412 19147 13361 2354 -542 -1425 C ATOM 2108 CD2 PHE A1074 34.021 -16.558 -52.798 1.00143.89 C ANISOU 2108 CD2 PHE A1074 21966 19455 13252 2841 -902 -1730 C ATOM 2109 CE1 PHE A1074 36.002 -15.621 -51.105 1.00142.87 C ANISOU 2109 CE1 PHE A1074 21729 19188 13365 2370 -468 -1292 C ATOM 2110 CE2 PHE A1074 34.256 -15.184 -52.671 1.00146.96 C ANISOU 2110 CE2 PHE A1074 22587 19740 13511 2900 -835 -1584 C ATOM 2111 CZ PHE A1074 35.247 -14.726 -51.828 1.00143.56 C ANISOU 2111 CZ PHE A1074 22111 19231 13205 2641 -606 -1365 C ATOM 2112 N ASP A1075 31.390 -19.255 -52.002 1.00143.92 N ANISOU 2112 N ASP A1075 21221 19884 13577 2615 -1365 -2429 N ATOM 2113 CA ASP A1075 30.045 -18.693 -52.127 1.00146.06 C ANISOU 2113 CA ASP A1075 21402 20354 13739 2800 -1627 -2689 C ATOM 2114 C ASP A1075 29.161 -18.989 -50.899 1.00150.56 C ANISOU 2114 C ASP A1075 21589 21100 14516 2547 -1709 -2882 C ATOM 2115 O ASP A1075 28.388 -18.121 -50.484 1.00150.59 O ANISOU 2115 O ASP A1075 21484 21242 14492 2656 -1847 -2988 O ATOM 2116 CB ASP A1075 29.382 -19.180 -53.434 1.00150.49 C ANISOU 2116 CB ASP A1075 22068 21026 14084 3037 -1810 -2928 C ATOM 2117 CG ASP A1075 30.224 -19.023 -54.702 1.00160.41 C ANISOU 2117 CG ASP A1075 23723 22105 15121 3270 -1718 -2758 C ATOM 2118 OD1 ASP A1075 31.183 -18.213 -54.691 1.00160.03 O ANISOU 2118 OD1 ASP A1075 23903 21872 15029 3310 -1538 -2476 O ATOM 2119 OD2 ASP A1075 29.916 -19.702 -55.707 1.00166.72 O ANISOU 2119 OD2 ASP A1075 24610 22955 15780 3392 -1815 -2921 O ATOM 2120 N SER A1076 29.314 -20.192 -50.302 1.00146.97 N ANISOU 2120 N SER A1076 20966 20623 14251 2216 -1609 -2921 N ATOM 2121 CA SER A1076 28.550 -20.644 -49.133 1.00146.55 C ANISOU 2121 CA SER A1076 20593 20705 14386 1909 -1639 -3104 C ATOM 2122 C SER A1076 29.439 -20.791 -47.872 1.00147.98 C ANISOU 2122 C SER A1076 20726 20712 14787 1620 -1427 -2852 C ATOM 2123 O SER A1076 29.364 -21.800 -47.164 1.00146.93 O ANISOU 2123 O SER A1076 20483 20551 14793 1319 -1355 -2920 O ATOM 2124 CB SER A1076 27.811 -21.942 -49.458 1.00152.16 C ANISOU 2124 CB SER A1076 21195 21532 15085 1740 -1709 -3411 C ATOM 2125 OG SER A1076 27.063 -21.841 -50.661 1.00163.68 O ANISOU 2125 OG SER A1076 22693 23169 16327 2013 -1914 -3648 O ATOM 2126 N LEU A1077 30.258 -19.755 -47.591 1.00143.62 N ANISOU 2126 N LEU A1077 20280 20043 14245 1711 -1330 -2574 N ATOM 2127 CA LEU A1077 31.205 -19.682 -46.465 1.00141.45 C ANISOU 2127 CA LEU A1077 19965 19630 14148 1486 -1145 -2322 C ATOM 2128 C LEU A1077 30.534 -19.277 -45.130 1.00144.99 C ANISOU 2128 C LEU A1077 20176 20170 14742 1287 -1182 -2397 C ATOM 2129 O LEU A1077 31.132 -19.441 -44.058 1.00142.65 O ANISOU 2129 O LEU A1077 19814 19782 14605 1054 -1053 -2245 O ATOM 2130 CB LEU A1077 32.352 -18.715 -46.834 1.00140.91 C ANISOU 2130 CB LEU A1077 20114 19428 13997 1639 -1015 -2028 C ATOM 2131 CG LEU A1077 33.713 -18.874 -46.150 1.00143.84 C ANISOU 2131 CG LEU A1077 20484 19670 14498 1460 -799 -1757 C ATOM 2132 CD1 LEU A1077 34.469 -20.078 -46.688 1.00144.23 C ANISOU 2132 CD1 LEU A1077 20604 19648 14549 1458 -702 -1717 C ATOM 2133 CD2 LEU A1077 34.559 -17.641 -46.372 1.00145.88 C ANISOU 2133 CD2 LEU A1077 20912 19856 14658 1552 -682 -1534 C ATOM 2134 N GLU A1078 29.291 -18.760 -45.204 1.00143.38 N ANISOU 2134 N GLU A1078 19843 20166 14470 1397 -1365 -2646 N ATOM 2135 CA GLU A1078 28.492 -18.358 -44.039 1.00142.92 C ANISOU 2135 CA GLU A1078 19541 20238 14524 1239 -1412 -2771 C ATOM 2136 C GLU A1078 27.894 -19.580 -43.332 1.00146.42 C ANISOU 2136 C GLU A1078 19768 20760 15103 886 -1389 -2986 C ATOM 2137 O GLU A1078 27.851 -19.622 -42.100 1.00144.64 O ANISOU 2137 O GLU A1078 19413 20516 15027 622 -1307 -2959 O ATOM 2138 CB GLU A1078 27.388 -17.347 -44.434 1.00146.23 C ANISOU 2138 CB GLU A1078 19895 20874 14792 1538 -1622 -2986 C ATOM 2139 CG GLU A1078 26.419 -17.797 -45.523 1.00159.20 C ANISOU 2139 CG GLU A1078 21473 22738 16277 1731 -1819 -3310 C ATOM 2140 CD GLU A1078 26.596 -17.117 -46.866 1.00181.94 C ANISOU 2140 CD GLU A1078 24642 25579 18906 2166 -1926 -3252 C ATOM 2141 OE1 GLU A1078 25.671 -16.383 -47.282 1.00178.65 O ANISOU 2141 OE1 GLU A1078 24191 25365 18323 2485 -2138 -3459 O ATOM 2142 OE2 GLU A1078 27.654 -17.320 -47.506 1.00176.05 O ANISOU 2142 OE2 GLU A1078 24168 24609 18113 2205 -1799 -3012 O ATOM 2143 N GLU A1079 27.458 -20.573 -44.134 1.00144.41 N ANISOU 2143 N GLU A1079 19517 20577 14775 870 -1447 -3199 N ATOM 2144 CA GLU A1079 26.824 -21.831 -43.736 1.00145.10 C ANISOU 2144 CA GLU A1079 19475 20728 14930 524 -1417 -3448 C ATOM 2145 C GLU A1079 27.715 -22.742 -42.863 1.00148.07 C ANISOU 2145 C GLU A1079 19978 20839 15444 220 -1211 -3244 C ATOM 2146 O GLU A1079 27.185 -23.584 -42.134 1.00148.82 O ANISOU 2146 O GLU A1079 19996 20943 15605 -125 -1151 -3417 O ATOM 2147 CB GLU A1079 26.312 -22.580 -44.981 1.00148.57 C ANISOU 2147 CB GLU A1079 19958 21275 15218 613 -1524 -3696 C ATOM 2148 CG GLU A1079 25.178 -21.857 -45.697 1.00159.56 C ANISOU 2148 CG GLU A1079 21168 22995 16460 884 -1762 -3990 C ATOM 2149 CD GLU A1079 24.961 -22.209 -47.157 1.00177.07 C ANISOU 2149 CD GLU A1079 23500 25296 18483 1120 -1896 -4145 C ATOM 2150 OE1 GLU A1079 24.783 -21.272 -47.969 1.00166.12 O ANISOU 2150 OE1 GLU A1079 22171 24013 16933 1527 -2059 -4153 O ATOM 2151 OE2 GLU A1079 24.944 -23.416 -47.490 1.00170.69 O ANISOU 2151 OE2 GLU A1079 22756 24434 17663 903 -1838 -4264 O ATOM 2152 N THR A1080 29.054 -22.571 -42.932 1.00142.34 N ANISOU 2152 N THR A1080 19455 19887 14739 348 -1100 -2894 N ATOM 2153 CA THR A1080 30.025 -23.354 -42.154 1.00140.33 C ANISOU 2153 CA THR A1080 19331 19400 14587 158 -931 -2683 C ATOM 2154 C THR A1080 30.036 -22.925 -40.681 1.00141.34 C ANISOU 2154 C THR A1080 19334 19509 14858 -60 -869 -2596 C ATOM 2155 O THR A1080 29.911 -23.774 -39.798 1.00141.10 O ANISOU 2155 O THR A1080 19328 19387 14896 -347 -788 -2644 O ATOM 2156 CB THR A1080 31.434 -23.248 -42.764 1.00147.78 C ANISOU 2156 CB THR A1080 20474 20186 15490 395 -845 -2381 C ATOM 2157 OG1 THR A1080 31.815 -21.871 -42.819 1.00147.27 O ANISOU 2157 OG1 THR A1080 20370 20172 15416 577 -859 -2213 O ATOM 2158 CG2 THR A1080 31.535 -23.881 -44.146 1.00147.46 C ANISOU 2158 CG2 THR A1080 20598 20123 15305 579 -875 -2458 C ATOM 2159 N GLY A1081 30.193 -21.621 -40.443 1.00135.74 N ANISOU 2159 N GLY A1081 18538 18867 14172 79 -901 -2468 N ATOM 2160 CA GLY A1081 30.264 -21.022 -39.115 1.00133.67 C ANISOU 2160 CA GLY A1081 18169 18590 14031 -90 -849 -2366 C ATOM 2161 C GLY A1081 31.508 -20.170 -38.964 1.00134.70 C ANISOU 2161 C GLY A1081 18385 18616 14179 42 -775 -2040 C ATOM 2162 O GLY A1081 32.326 -20.410 -38.070 1.00132.78 O ANISOU 2162 O GLY A1081 18168 18256 14026 -101 -671 -1858 O ATOM 2163 N ALA A1082 31.654 -19.175 -39.865 1.00130.94 N ANISOU 2163 N ALA A1082 17972 18186 13593 312 -825 -1980 N ATOM 2164 CA ALA A1082 32.794 -18.255 -39.951 1.00129.41 C ANISOU 2164 CA ALA A1082 17889 17909 13374 419 -734 -1703 C ATOM 2165 C ALA A1082 32.845 -17.206 -38.843 1.00130.37 C ANISOU 2165 C ALA A1082 17940 18031 13565 305 -705 -1602 C ATOM 2166 O ALA A1082 33.937 -16.863 -38.389 1.00128.54 O ANISOU 2166 O ALA A1082 17747 17722 13371 235 -590 -1375 O ATOM 2167 CB ALA A1082 32.814 -17.578 -41.312 1.00131.35 C ANISOU 2167 CB ALA A1082 18296 18171 13440 717 -780 -1696 C ATOM 2168 N GLN A1083 31.675 -16.682 -38.428 1.00126.22 N ANISOU 2168 N GLN A1083 17300 17613 13045 290 -809 -1786 N ATOM 2169 CA GLN A1083 31.571 -15.674 -37.372 1.00124.43 C ANISOU 2169 CA GLN A1083 17020 17386 12870 195 -790 -1720 C ATOM 2170 C GLN A1083 32.037 -16.254 -36.034 1.00124.47 C ANISOU 2170 C GLN A1083 16930 17325 13039 -115 -692 -1625 C ATOM 2171 O GLN A1083 31.646 -17.369 -35.669 1.00124.25 O ANISOU 2171 O GLN A1083 16821 17307 13082 -281 -693 -1752 O ATOM 2172 CB GLN A1083 30.140 -15.115 -37.279 1.00126.99 C ANISOU 2172 CB GLN A1083 17224 17875 13151 290 -932 -1981 C ATOM 2173 CG GLN A1083 30.077 -13.735 -36.631 1.00143.31 C ANISOU 2173 CG GLN A1083 19341 19919 15190 336 -928 -1896 C ATOM 2174 CD GLN A1083 28.740 -13.065 -36.814 1.00163.52 C ANISOU 2174 CD GLN A1083 21824 22655 17651 558 -1088 -2153 C ATOM 2175 OE1 GLN A1083 28.434 -12.504 -37.873 1.00159.86 O ANISOU 2175 OE1 GLN A1083 21508 22225 17007 893 -1194 -2210 O ATOM 2176 NE2 GLN A1083 27.932 -13.070 -35.765 1.00155.58 N ANISOU 2176 NE2 GLN A1083 20597 21773 16744 395 -1108 -2319 N ATOM 2177 N GLY A1084 32.922 -15.513 -35.364 1.00117.84 N ANISOU 2177 N GLY A1084 16135 16408 12232 -193 -602 -1402 N ATOM 2178 CA GLY A1084 33.517 -15.887 -34.083 1.00115.41 C ANISOU 2178 CA GLY A1084 15761 16040 12050 -448 -521 -1284 C ATOM 2179 C GLY A1084 34.494 -17.046 -34.159 1.00115.96 C ANISOU 2179 C GLY A1084 15865 16042 12153 -485 -456 -1176 C ATOM 2180 O GLY A1084 34.880 -17.602 -33.122 1.00113.80 O ANISOU 2180 O GLY A1084 15562 15715 11962 -661 -415 -1112 O ATOM 2181 N ARG A1085 34.912 -17.404 -35.402 1.00111.79 N ANISOU 2181 N ARG A1085 15425 15511 11541 -290 -450 -1159 N ATOM 2182 CA ARG A1085 35.825 -18.508 -35.707 1.00110.43 C ANISOU 2182 CA ARG A1085 15306 15286 11368 -248 -394 -1077 C ATOM 2183 C ARG A1085 37.251 -18.029 -35.981 1.00110.80 C ANISOU 2183 C ARG A1085 15369 15353 11378 -167 -294 -862 C ATOM 2184 O ARG A1085 37.446 -17.148 -36.824 1.00110.34 O ANISOU 2184 O ARG A1085 15374 15326 11226 -50 -264 -820 O ATOM 2185 CB ARG A1085 35.288 -19.330 -36.898 1.00109.84 C ANISOU 2185 CB ARG A1085 15312 15208 11216 -101 -446 -1235 C ATOM 2186 CG ARG A1085 35.873 -20.734 -37.029 1.00118.37 C ANISOU 2186 CG ARG A1085 16482 16200 12294 -82 -404 -1213 C ATOM 2187 CD ARG A1085 35.284 -21.732 -36.046 1.00126.13 C ANISOU 2187 CD ARG A1085 17490 17095 13338 -297 -415 -1322 C ATOM 2188 NE ARG A1085 33.838 -21.874 -36.212 1.00134.48 N ANISOU 2188 NE ARG A1085 18508 18203 14385 -407 -487 -1585 N ATOM 2189 CZ ARG A1085 33.098 -22.798 -35.608 1.00151.11 C ANISOU 2189 CZ ARG A1085 20660 20246 16511 -633 -478 -1749 C ATOM 2190 NH1 ARG A1085 33.663 -23.687 -34.798 1.00135.47 N ANISOU 2190 NH1 ARG A1085 18828 18100 14544 -744 -407 -1656 N ATOM 2191 NH2 ARG A1085 31.790 -22.849 -35.817 1.00143.55 N ANISOU 2191 NH2 ARG A1085 19611 19395 15535 -748 -536 -2021 N ATOM 2192 N LYS A1086 38.242 -18.623 -35.267 1.00104.71 N ANISOU 2192 N LYS A1086 14550 14575 10659 -228 -240 -742 N ATOM 2193 CA LYS A1086 39.667 -18.340 -35.448 1.00103.76 C ANISOU 2193 CA LYS A1086 14381 14537 10505 -168 -141 -576 C ATOM 2194 C LYS A1086 40.087 -18.954 -36.795 1.00107.29 C ANISOU 2194 C LYS A1086 14909 14996 10860 55 -103 -592 C ATOM 2195 O LYS A1086 40.106 -20.179 -36.934 1.00107.06 O ANISOU 2195 O LYS A1086 14937 14910 10829 149 -131 -642 O ATOM 2196 CB LYS A1086 40.504 -18.918 -34.293 1.00105.35 C ANISOU 2196 CB LYS A1086 14492 14765 10773 -244 -131 -484 C ATOM 2197 CG LYS A1086 40.452 -18.102 -33.012 1.00115.78 C ANISOU 2197 CG LYS A1086 15724 16105 12164 -465 -139 -428 C ATOM 2198 CD LYS A1086 41.350 -18.705 -31.934 1.00126.18 C ANISOU 2198 CD LYS A1086 16964 17464 13516 -499 -148 -341 C ATOM 2199 CE LYS A1086 41.474 -17.834 -30.701 1.00132.92 C ANISOU 2199 CE LYS A1086 17724 18358 14422 -718 -151 -277 C ATOM 2200 NZ LYS A1086 42.442 -18.390 -29.710 1.00136.35 N ANISOU 2200 NZ LYS A1086 18079 18864 14863 -712 -178 -197 N ATOM 2201 N VAL A1087 40.337 -18.100 -37.806 1.00103.64 N ANISOU 2201 N VAL A1087 14500 14580 10298 138 -36 -560 N ATOM 2202 CA VAL A1087 40.702 -18.552 -39.157 1.00104.24 C ANISOU 2202 CA VAL A1087 14674 14667 10267 345 13 -578 C ATOM 2203 C VAL A1087 42.040 -18.012 -39.644 1.00106.98 C ANISOU 2203 C VAL A1087 14977 15136 10537 370 175 -455 C ATOM 2204 O VAL A1087 42.427 -16.902 -39.284 1.00106.78 O ANISOU 2204 O VAL A1087 14910 15164 10496 216 255 -375 O ATOM 2205 CB VAL A1087 39.604 -18.302 -40.225 1.00108.82 C ANISOU 2205 CB VAL A1087 15418 15178 10751 466 -61 -705 C ATOM 2206 CG1 VAL A1087 38.400 -19.213 -40.016 1.00108.67 C ANISOU 2206 CG1 VAL A1087 15411 15092 10786 457 -203 -880 C ATOM 2207 CG2 VAL A1087 39.194 -16.832 -40.292 1.00108.42 C ANISOU 2207 CG2 VAL A1087 15442 15120 10633 420 -57 -684 C ATOM 2208 N ALA A1088 42.714 -18.794 -40.503 1.00102.88 N ANISOU 2208 N ALA A1088 14477 14661 9952 550 238 -458 N ATOM 2209 CA ALA A1088 43.986 -18.446 -41.137 1.00103.52 C ANISOU 2209 CA ALA A1088 14499 14893 9941 587 414 -382 C ATOM 2210 C ALA A1088 43.869 -18.695 -42.639 1.00106.48 C ANISOU 2210 C ALA A1088 15063 15218 10177 785 459 -434 C ATOM 2211 O ALA A1088 43.170 -19.625 -43.048 1.00105.31 O ANISOU 2211 O ALA A1088 15024 14962 10028 936 351 -526 O ATOM 2212 CB ALA A1088 45.104 -19.286 -40.552 1.00105.13 C ANISOU 2212 CB ALA A1088 14492 15254 10200 646 447 -345 C ATOM 2213 N CYS A1089 44.518 -17.863 -43.467 1.00103.76 N ANISOU 2213 N CYS A1089 14786 14941 9697 762 629 -386 N ATOM 2214 CA CYS A1089 44.400 -18.052 -44.913 1.00104.72 C ANISOU 2214 CA CYS A1089 15124 15001 9664 951 677 -433 C ATOM 2215 C CYS A1089 45.738 -18.058 -45.665 1.00106.10 C ANISOU 2215 C CYS A1089 15244 15341 9728 988 905 -393 C ATOM 2216 O CYS A1089 46.409 -17.034 -45.752 1.00107.54 O ANISOU 2216 O CYS A1089 15428 15608 9824 809 1084 -334 O ATOM 2217 CB CYS A1089 43.419 -17.053 -45.518 1.00105.74 C ANISOU 2217 CB CYS A1089 15529 14976 9671 949 630 -456 C ATOM 2218 SG CYS A1089 41.683 -17.549 -45.364 1.00108.69 S ANISOU 2218 SG CYS A1089 15988 15202 10109 1062 348 -601 S ATOM 2219 N PHE A1090 46.105 -19.216 -46.228 1.00 98.63 N ANISOU 2219 N PHE A1090 14270 14438 8766 1210 910 -441 N ATOM 2220 CA PHE A1090 47.328 -19.369 -47.007 1.00 98.80 C ANISOU 2220 CA PHE A1090 14220 14641 8677 1287 1124 -435 C ATOM 2221 C PHE A1090 46.955 -19.532 -48.485 1.00103.62 C ANISOU 2221 C PHE A1090 15134 15121 9115 1466 1162 -484 C ATOM 2222 O PHE A1090 45.771 -19.640 -48.802 1.00103.51 O ANISOU 2222 O PHE A1090 15344 14903 9083 1545 994 -533 O ATOM 2223 CB PHE A1090 48.156 -20.554 -46.491 1.00100.39 C ANISOU 2223 CB PHE A1090 14167 15011 8965 1451 1108 -457 C ATOM 2224 CG PHE A1090 47.520 -21.910 -46.661 1.00100.60 C ANISOU 2224 CG PHE A1090 14334 14868 9020 1707 941 -524 C ATOM 2225 CD1 PHE A1090 46.606 -22.388 -45.734 1.00101.45 C ANISOU 2225 CD1 PHE A1090 14479 14814 9253 1673 737 -542 C ATOM 2226 CD2 PHE A1090 47.875 -22.733 -47.721 1.00103.45 C ANISOU 2226 CD2 PHE A1090 14804 15233 9268 1960 1008 -579 C ATOM 2227 CE1 PHE A1090 46.036 -23.652 -45.880 1.00102.18 C ANISOU 2227 CE1 PHE A1090 14740 14737 9348 1856 612 -618 C ATOM 2228 CE2 PHE A1090 47.305 -23.998 -47.865 1.00105.75 C ANISOU 2228 CE2 PHE A1090 15267 15348 9566 2171 868 -648 C ATOM 2229 CZ PHE A1090 46.389 -24.449 -46.946 1.00102.19 C ANISOU 2229 CZ PHE A1090 14872 14725 9230 2102 676 -670 C ATOM 2230 N GLY A1091 47.942 -19.541 -49.374 1.00100.30 N ANISOU 2230 N GLY A1091 14709 14840 8560 1524 1379 -488 N ATOM 2231 CA GLY A1091 47.676 -19.710 -50.794 1.00100.45 C ANISOU 2231 CA GLY A1091 15030 14739 8396 1698 1430 -532 C ATOM 2232 C GLY A1091 48.887 -19.580 -51.682 1.00106.63 C ANISOU 2232 C GLY A1091 15787 15705 9023 1706 1719 -535 C ATOM 2233 O GLY A1091 49.840 -18.874 -51.341 1.00106.37 O ANISOU 2233 O GLY A1091 15558 15883 8976 1484 1923 -501 O ATOM 2234 N CYS A1092 48.826 -20.259 -52.845 1.00105.75 N ANISOU 2234 N CYS A1092 15877 15523 8781 1946 1746 -593 N ATOM 2235 CA CYS A1092 49.849 -20.288 -53.895 1.00108.89 C ANISOU 2235 CA CYS A1092 16301 16070 9001 1999 2022 -620 C ATOM 2236 C CYS A1092 49.508 -19.348 -55.054 1.00115.55 C ANISOU 2236 C CYS A1092 17563 16742 9600 1929 2147 -600 C ATOM 2237 O CYS A1092 48.335 -19.128 -55.356 1.00113.51 O ANISOU 2237 O CYS A1092 17614 16225 9289 2002 1955 -600 O ATOM 2238 CB CYS A1092 50.076 -21.713 -54.388 1.00109.81 C ANISOU 2238 CB CYS A1092 16391 16216 9117 2332 1980 -698 C ATOM 2239 SG CYS A1092 51.024 -22.745 -53.248 1.00113.87 S ANISOU 2239 SG CYS A1092 16442 17006 9818 2463 1947 -726 S ATOM 2240 N GLY A1093 50.547 -18.815 -55.690 1.00116.45 N ANISOU 2240 N GLY A1093 17683 17014 9548 1793 2472 -599 N ATOM 2241 CA GLY A1093 50.415 -17.897 -56.811 1.00118.79 C ANISOU 2241 CA GLY A1093 18424 17144 9565 1706 2647 -575 C ATOM 2242 C GLY A1093 51.694 -17.690 -57.591 1.00128.25 C ANISOU 2242 C GLY A1093 19591 18558 10580 1585 3037 -611 C ATOM 2243 O GLY A1093 52.568 -18.562 -57.594 1.00129.24 O ANISOU 2243 O GLY A1093 19377 18955 10774 1704 3133 -684 O ATOM 2244 N ASP A1094 51.798 -16.527 -58.270 1.00128.10 N ANISOU 2244 N ASP A1094 19953 18414 10304 1354 3272 -571 N ATOM 2245 CA ASP A1094 52.950 -16.123 -59.081 1.00132.24 C ANISOU 2245 CA ASP A1094 20529 19114 10603 1151 3695 -613 C ATOM 2246 C ASP A1094 53.005 -14.596 -59.210 1.00139.31 C ANISOU 2246 C ASP A1094 21811 19852 11270 762 3928 -546 C ATOM 2247 O ASP A1094 51.991 -13.975 -59.545 1.00138.11 O ANISOU 2247 O ASP A1094 22170 19331 10973 831 3782 -471 O ATOM 2248 CB ASP A1094 52.876 -16.771 -60.478 1.00135.74 C ANISOU 2248 CB ASP A1094 21276 19453 10848 1441 3752 -663 C ATOM 2249 CG ASP A1094 54.206 -16.907 -61.197 1.00149.69 C ANISOU 2249 CG ASP A1094 22897 21516 12462 1331 4163 -754 C ATOM 2250 OD1 ASP A1094 54.891 -15.875 -61.389 1.00152.72 O ANISOU 2250 OD1 ASP A1094 23393 21975 12660 943 4513 -754 O ATOM 2251 OD2 ASP A1094 54.536 -18.036 -61.620 1.00156.23 O ANISOU 2251 OD2 ASP A1094 23538 22489 13331 1627 4148 -836 O ATOM 2252 N SER A1095 54.194 -13.997 -58.967 1.00139.69 N ANISOU 2252 N SER A1095 21630 20185 11262 358 4294 -588 N ATOM 2253 CA SER A1095 54.423 -12.546 -59.055 1.00142.28 C ANISOU 2253 CA SER A1095 22335 20378 11347 -90 4583 -540 C ATOM 2254 C SER A1095 54.362 -11.972 -60.489 1.00151.12 C ANISOU 2254 C SER A1095 24141 21214 12063 -122 4837 -522 C ATOM 2255 O SER A1095 54.365 -10.749 -60.649 1.00153.10 O ANISOU 2255 O SER A1095 24866 21244 12060 -449 5050 -466 O ATOM 2256 CB SER A1095 55.733 -12.153 -58.375 1.00147.73 C ANISOU 2256 CB SER A1095 22545 21496 12089 -548 4909 -627 C ATOM 2257 OG SER A1095 56.828 -12.911 -58.861 1.00159.04 O ANISOU 2257 OG SER A1095 23576 23335 13515 -514 5146 -768 O ATOM 2258 N SER A1096 54.291 -12.842 -61.522 1.00149.05 N ANISOU 2258 N SER A1096 23980 20933 11719 219 4815 -568 N ATOM 2259 CA SER A1096 54.191 -12.441 -62.929 1.00152.06 C ANISOU 2259 CA SER A1096 25024 21042 11711 251 5024 -554 C ATOM 2260 C SER A1096 52.833 -11.796 -63.257 1.00156.90 C ANISOU 2260 C SER A1096 26324 21148 12142 457 4751 -439 C ATOM 2261 O SER A1096 52.753 -11.010 -64.203 1.00159.13 O ANISOU 2261 O SER A1096 27274 21145 12043 377 4955 -400 O ATOM 2262 CB SER A1096 54.445 -13.632 -63.845 1.00155.60 C ANISOU 2262 CB SER A1096 25354 21620 12147 592 5033 -641 C ATOM 2263 OG SER A1096 53.483 -14.652 -63.635 1.00159.17 O ANISOU 2263 OG SER A1096 25674 21979 12824 1057 4573 -631 O ATOM 2264 N TRP A1097 51.777 -12.126 -62.477 1.00151.63 N ANISOU 2264 N TRP A1097 25503 20382 11728 730 4295 -399 N ATOM 2265 CA TRP A1097 50.420 -11.581 -62.630 1.00151.08 C ANISOU 2265 CA TRP A1097 25965 19910 11527 975 3978 -325 C ATOM 2266 C TRP A1097 50.239 -10.335 -61.742 1.00156.80 C ANISOU 2266 C TRP A1097 26856 20494 12227 675 4005 -241 C ATOM 2267 O TRP A1097 51.015 -10.139 -60.805 1.00155.93 O ANISOU 2267 O TRP A1097 26318 20632 12298 316 4172 -247 O ATOM 2268 CB TRP A1097 49.346 -12.642 -62.324 1.00146.29 C ANISOU 2268 CB TRP A1097 25092 19302 11188 1413 3490 -364 C ATOM 2269 CG TRP A1097 49.635 -14.001 -62.892 1.00147.17 C ANISOU 2269 CG TRP A1097 24922 19598 11398 1661 3461 -455 C ATOM 2270 CD1 TRP A1097 50.281 -15.024 -62.265 1.00148.93 C ANISOU 2270 CD1 TRP A1097 24516 20149 11922 1657 3465 -514 C ATOM 2271 CD2 TRP A1097 49.280 -14.489 -64.194 1.00148.43 C ANISOU 2271 CD2 TRP A1097 25455 19609 11332 1973 3414 -501 C ATOM 2272 NE1 TRP A1097 50.351 -16.121 -63.092 1.00148.91 N ANISOU 2272 NE1 TRP A1097 24488 20196 11894 1947 3434 -592 N ATOM 2273 CE2 TRP A1097 49.749 -15.819 -64.286 1.00151.82 C ANISOU 2273 CE2 TRP A1097 25454 20282 11950 2127 3407 -587 C ATOM 2274 CE3 TRP A1097 48.625 -13.926 -65.305 1.00151.67 C ANISOU 2274 CE3 TRP A1097 26552 19700 11376 2155 3375 -481 C ATOM 2275 CZ2 TRP A1097 49.578 -16.598 -65.440 1.00152.28 C ANISOU 2275 CZ2 TRP A1097 25737 20270 11854 2427 3372 -655 C ATOM 2276 CZ3 TRP A1097 48.466 -14.696 -66.453 1.00154.18 C ANISOU 2276 CZ3 TRP A1097 27074 19967 11541 2453 3332 -550 C ATOM 2277 CH2 TRP A1097 48.933 -16.016 -66.510 1.00154.10 C ANISOU 2277 CH2 TRP A1097 26615 20199 11736 2572 3335 -636 C ATOM 2278 N GLU A1098 49.229 -9.493 -62.050 1.00155.84 N ANISOU 2278 N GLU A1098 27367 19984 11860 841 3836 -174 N ATOM 2279 CA GLU A1098 48.950 -8.232 -61.346 1.00157.04 C ANISOU 2279 CA GLU A1098 27822 19928 11920 616 3856 -91 C ATOM 2280 C GLU A1098 48.526 -8.420 -59.881 1.00158.83 C ANISOU 2280 C GLU A1098 27499 20308 12543 598 3570 -88 C ATOM 2281 O GLU A1098 49.062 -7.740 -58.999 1.00158.44 O ANISOU 2281 O GLU A1098 27315 20326 12558 206 3745 -52 O ATOM 2282 CB GLU A1098 47.921 -7.380 -62.122 1.00160.26 C ANISOU 2282 CB GLU A1098 29075 19881 11935 908 3710 -36 C ATOM 2283 CG GLU A1098 48.065 -5.878 -61.906 1.00174.17 C ANISOU 2283 CG GLU A1098 31428 21351 13397 592 3946 56 C ATOM 2284 CD GLU A1098 47.471 -4.989 -62.985 1.00198.07 C ANISOU 2284 CD GLU A1098 35435 23915 15906 826 3960 112 C ATOM 2285 OE1 GLU A1098 46.436 -4.337 -62.714 1.00195.74 O ANISOU 2285 OE1 GLU A1098 35513 23356 15502 1102 3670 151 O ATOM 2286 OE2 GLU A1098 48.061 -4.913 -64.088 1.00191.08 O ANISOU 2286 OE2 GLU A1098 34966 22932 14703 738 4271 112 O ATOM 2287 N TYR A1099 47.576 -9.337 -59.625 1.00153.60 N ANISOU 2287 N TYR A1099 26534 19699 12128 993 3147 -136 N ATOM 2288 CA TYR A1099 47.073 -9.612 -58.275 1.00150.40 C ANISOU 2288 CA TYR A1099 25634 19424 12089 1002 2862 -143 C ATOM 2289 C TYR A1099 47.812 -10.823 -57.687 1.00152.12 C ANISOU 2289 C TYR A1099 25117 20021 12661 928 2877 -202 C ATOM 2290 O TYR A1099 47.286 -11.944 -57.739 1.00150.22 O ANISOU 2290 O TYR A1099 24617 19858 12602 1235 2611 -268 O ATOM 2291 CB TYR A1099 45.537 -9.842 -58.274 1.00149.96 C ANISOU 2291 CB TYR A1099 25705 19204 12069 1445 2401 -186 C ATOM 2292 CG TYR A1099 44.751 -8.922 -59.185 1.00154.27 C ANISOU 2292 CG TYR A1099 27002 19401 12214 1688 2331 -163 C ATOM 2293 CD1 TYR A1099 44.510 -9.262 -60.515 1.00158.05 C ANISOU 2293 CD1 TYR A1099 27844 19771 12438 1988 2300 -207 C ATOM 2294 CD2 TYR A1099 44.223 -7.724 -58.712 1.00155.54 C ANISOU 2294 CD2 TYR A1099 27534 19334 12229 1656 2279 -103 C ATOM 2295 CE1 TYR A1099 43.794 -8.417 -61.360 1.00161.12 C ANISOU 2295 CE1 TYR A1099 28955 19838 12425 2255 2216 -190 C ATOM 2296 CE2 TYR A1099 43.501 -6.872 -59.547 1.00158.87 C ANISOU 2296 CE2 TYR A1099 28693 19424 12246 1939 2198 -85 C ATOM 2297 CZ TYR A1099 43.287 -7.224 -60.870 1.00167.61 C ANISOU 2297 CZ TYR A1099 30155 20435 13095 2247 2159 -130 C ATOM 2298 OH TYR A1099 42.570 -6.391 -61.696 1.00170.38 O ANISOU 2298 OH TYR A1099 31259 20460 13019 2569 2056 -118 O ATOM 2299 N PHE A1100 49.047 -10.609 -57.158 1.00148.51 N ANISOU 2299 N PHE A1100 24345 19806 12276 527 3194 -193 N ATOM 2300 CA PHE A1100 49.826 -11.703 -56.567 1.00146.53 C ANISOU 2300 CA PHE A1100 23410 19937 12328 494 3206 -256 C ATOM 2301 C PHE A1100 49.095 -12.263 -55.358 1.00145.40 C ANISOU 2301 C PHE A1100 22878 19846 12523 631 2841 -258 C ATOM 2302 O PHE A1100 48.904 -11.567 -54.358 1.00143.64 O ANISOU 2302 O PHE A1100 22592 19594 12391 429 2790 -211 O ATOM 2303 CB PHE A1100 51.283 -11.317 -56.243 1.00150.52 C ANISOU 2303 CB PHE A1100 23623 20745 12822 51 3602 -280 C ATOM 2304 CG PHE A1100 52.003 -12.364 -55.419 1.00150.73 C ANISOU 2304 CG PHE A1100 22925 21179 13165 69 3550 -350 C ATOM 2305 CD1 PHE A1100 52.329 -13.599 -55.966 1.00153.78 C ANISOU 2305 CD1 PHE A1100 23069 21742 13619 361 3521 -426 C ATOM 2306 CD2 PHE A1100 52.311 -12.131 -54.083 1.00151.53 C ANISOU 2306 CD2 PHE A1100 22624 21472 13480 -170 3509 -342 C ATOM 2307 CE1 PHE A1100 52.953 -14.579 -55.194 1.00153.89 C ANISOU 2307 CE1 PHE A1100 22475 22102 13893 442 3449 -490 C ATOM 2308 CE2 PHE A1100 52.948 -13.108 -53.316 1.00153.49 C ANISOU 2308 CE2 PHE A1100 22245 22085 13990 -99 3433 -409 C ATOM 2309 CZ PHE A1100 53.270 -14.323 -53.878 1.00152.00 C ANISOU 2309 CZ PHE A1100 21847 22055 13849 220 3403 -481 C ATOM 2310 N CYS A1101 48.664 -13.528 -55.489 1.00139.65 N ANISOU 2310 N CYS A1101 21933 19172 11955 966 2601 -319 N ATOM 2311 CA CYS A1101 47.864 -14.273 -54.526 1.00135.79 C ANISOU 2311 CA CYS A1101 21137 18702 11755 1129 2254 -343 C ATOM 2312 C CYS A1101 46.593 -13.495 -54.207 1.00138.34 C ANISOU 2312 C CYS A1101 21752 18767 12042 1181 2018 -315 C ATOM 2313 O CYS A1101 46.373 -13.061 -53.077 1.00136.77 O ANISOU 2313 O CYS A1101 21386 18583 11996 1020 1932 -280 O ATOM 2314 CB CYS A1101 48.660 -14.655 -53.281 1.00134.78 C ANISOU 2314 CB CYS A1101 20458 18860 11891 944 2288 -342 C ATOM 2315 SG CYS A1101 49.635 -16.169 -53.470 1.00139.25 S ANISOU 2315 SG CYS A1101 20605 19726 12579 1131 2351 -422 S ATOM 2316 N GLY A1102 45.813 -13.268 -55.259 1.00135.87 N ANISOU 2316 N GLY A1102 21897 18230 11497 1417 1928 -338 N ATOM 2317 CA GLY A1102 44.545 -12.554 -55.209 1.00135.38 C ANISOU 2317 CA GLY A1102 22163 17939 11339 1567 1685 -343 C ATOM 2318 C GLY A1102 43.490 -13.306 -54.429 1.00137.59 C ANISOU 2318 C GLY A1102 22134 18266 11879 1734 1328 -428 C ATOM 2319 O GLY A1102 42.667 -12.677 -53.760 1.00136.49 O ANISOU 2319 O GLY A1102 22044 18042 11774 1737 1156 -431 O ATOM 2320 N ALA A1103 43.522 -14.662 -54.489 1.00133.51 N ANISOU 2320 N ALA A1103 21313 17882 11532 1859 1232 -507 N ATOM 2321 CA ALA A1103 42.598 -15.542 -53.765 1.00131.33 C ANISOU 2321 CA ALA A1103 20751 17654 11495 1964 934 -606 C ATOM 2322 C ALA A1103 42.744 -15.397 -52.246 1.00134.00 C ANISOU 2322 C ALA A1103 20738 18088 12089 1725 911 -557 C ATOM 2323 O ALA A1103 41.735 -15.440 -51.545 1.00131.99 O ANISOU 2323 O ALA A1103 20386 17807 11958 1757 678 -621 O ATOM 2324 CB ALA A1103 42.800 -16.987 -54.180 1.00132.02 C ANISOU 2324 CB ALA A1103 20670 17827 11665 2107 901 -686 C ATOM 2325 N VAL A1104 43.985 -15.188 -51.746 1.00131.67 N ANISOU 2325 N VAL A1104 20249 17923 11857 1482 1156 -459 N ATOM 2326 CA VAL A1104 44.286 -14.976 -50.318 1.00130.49 C ANISOU 2326 CA VAL A1104 19777 17880 11922 1240 1157 -406 C ATOM 2327 C VAL A1104 43.534 -13.725 -49.833 1.00134.92 C ANISOU 2327 C VAL A1104 20543 18294 12425 1144 1082 -372 C ATOM 2328 O VAL A1104 42.773 -13.805 -48.872 1.00132.58 O ANISOU 2328 O VAL A1104 20087 17991 12297 1128 886 -404 O ATOM 2329 CB VAL A1104 45.816 -14.871 -50.035 1.00135.56 C ANISOU 2329 CB VAL A1104 20184 18732 12590 1005 1444 -336 C ATOM 2330 CG1 VAL A1104 46.097 -14.576 -48.562 1.00133.93 C ANISOU 2330 CG1 VAL A1104 19666 18641 12581 759 1425 -289 C ATOM 2331 CG2 VAL A1104 46.551 -16.132 -50.474 1.00136.18 C ANISOU 2331 CG2 VAL A1104 20051 18974 12717 1159 1503 -384 C ATOM 2332 N ASP A1105 43.720 -12.593 -50.542 1.00134.32 N ANISOU 2332 N ASP A1105 20864 18086 12087 1096 1245 -314 N ATOM 2333 CA ASP A1105 43.091 -11.296 -50.277 1.00134.77 C ANISOU 2333 CA ASP A1105 21237 17958 12010 1048 1207 -276 C ATOM 2334 C ASP A1105 41.561 -11.355 -50.455 1.00138.32 C ANISOU 2334 C ASP A1105 21836 18288 12430 1369 879 -382 C ATOM 2335 O ASP A1105 40.848 -10.611 -49.779 1.00137.45 O ANISOU 2335 O ASP A1105 21802 18098 12327 1364 758 -386 O ATOM 2336 CB ASP A1105 43.695 -10.201 -51.189 1.00139.64 C ANISOU 2336 CB ASP A1105 22340 18423 12294 948 1482 -198 C ATOM 2337 CG ASP A1105 45.192 -10.310 -51.483 1.00152.54 C ANISOU 2337 CG ASP A1105 23851 20218 13891 678 1831 -149 C ATOM 2338 OD1 ASP A1105 45.936 -10.832 -50.619 1.00152.72 O ANISOU 2338 OD1 ASP A1105 23394 20482 14149 482 1890 -147 O ATOM 2339 OD2 ASP A1105 45.619 -9.853 -52.569 1.00159.95 O ANISOU 2339 OD2 ASP A1105 25176 21052 14547 666 2048 -127 O ATOM 2340 N ALA A1106 41.067 -12.245 -51.353 1.00135.19 N ANISOU 2340 N ALA A1106 21466 17906 11995 1646 738 -486 N ATOM 2341 CA ALA A1106 39.644 -12.445 -51.649 1.00134.81 C ANISOU 2341 CA ALA A1106 21504 17814 11905 1954 423 -635 C ATOM 2342 C ALA A1106 38.884 -13.055 -50.480 1.00137.10 C ANISOU 2342 C ALA A1106 21385 18224 12482 1905 206 -733 C ATOM 2343 O ALA A1106 37.827 -12.539 -50.123 1.00136.49 O ANISOU 2343 O ALA A1106 21353 18121 12386 2018 8 -818 O ATOM 2344 CB ALA A1106 39.474 -13.309 -52.888 1.00136.60 C ANISOU 2344 CB ALA A1106 21839 18048 12014 2202 361 -729 C ATOM 2345 N ILE A1107 39.414 -14.145 -49.887 1.00132.93 N ANISOU 2345 N ILE A1107 20482 17827 12199 1751 248 -729 N ATOM 2346 CA ILE A1107 38.788 -14.823 -48.744 1.00130.97 C ANISOU 2346 CA ILE A1107 19882 17670 12210 1664 79 -816 C ATOM 2347 C ILE A1107 39.035 -14.047 -47.441 1.00133.70 C ANISOU 2347 C ILE A1107 20092 18025 12682 1416 140 -716 C ATOM 2348 O ILE A1107 38.178 -14.085 -46.562 1.00132.25 O ANISOU 2348 O ILE A1107 19747 17871 12633 1380 -23 -799 O ATOM 2349 CB ILE A1107 39.152 -16.339 -48.617 1.00133.48 C ANISOU 2349 CB ILE A1107 19939 18078 12698 1634 80 -861 C ATOM 2350 CG1 ILE A1107 39.294 -17.035 -49.988 1.00135.38 C ANISOU 2350 CG1 ILE A1107 20354 18297 12785 1845 99 -919 C ATOM 2351 CG2 ILE A1107 38.135 -17.088 -47.741 1.00132.95 C ANISOU 2351 CG2 ILE A1107 19638 18058 12819 1587 -127 -1006 C ATOM 2352 CD1 ILE A1107 40.425 -18.063 -50.043 1.00142.02 C ANISOU 2352 CD1 ILE A1107 21051 19201 13708 1803 258 -859 C ATOM 2353 N GLU A1108 40.184 -13.336 -47.320 1.00131.02 N ANISOU 2353 N GLU A1108 19819 17673 12290 1227 381 -557 N ATOM 2354 CA GLU A1108 40.523 -12.542 -46.128 1.00130.15 C ANISOU 2354 CA GLU A1108 19605 17573 12275 965 457 -463 C ATOM 2355 C GLU A1108 39.556 -11.367 -45.881 1.00135.18 C ANISOU 2355 C GLU A1108 20485 18076 12801 1025 348 -486 C ATOM 2356 O GLU A1108 39.084 -11.203 -44.751 1.00133.03 O ANISOU 2356 O GLU A1108 20034 17830 12681 917 251 -506 O ATOM 2357 CB GLU A1108 41.981 -12.066 -46.152 1.00132.38 C ANISOU 2357 CB GLU A1108 19896 17905 12497 723 752 -325 C ATOM 2358 CG GLU A1108 42.960 -13.100 -45.622 1.00138.77 C ANISOU 2358 CG GLU A1108 20310 18915 13501 604 827 -303 C ATOM 2359 CD GLU A1108 44.325 -12.577 -45.215 1.00153.22 C ANISOU 2359 CD GLU A1108 22012 20882 15322 314 1081 -205 C ATOM 2360 OE1 GLU A1108 44.799 -11.581 -45.809 1.00142.39 O ANISOU 2360 OE1 GLU A1108 20910 19448 13744 191 1284 -153 O ATOM 2361 OE2 GLU A1108 44.932 -13.183 -44.303 1.00145.06 O ANISOU 2361 OE2 GLU A1108 20618 20025 14473 204 1079 -194 O ATOM 2362 N GLU A1109 39.242 -10.572 -46.934 1.00134.38 N ANISOU 2362 N GLU A1109 20812 17827 12418 1223 357 -490 N ATOM 2363 CA GLU A1109 38.293 -9.458 -46.818 1.00135.16 C ANISOU 2363 CA GLU A1109 21204 17788 12363 1368 234 -524 C ATOM 2364 C GLU A1109 36.840 -9.963 -46.671 1.00139.54 C ANISOU 2364 C GLU A1109 21589 18429 13000 1627 -85 -724 C ATOM 2365 O GLU A1109 36.033 -9.299 -46.019 1.00138.81 O ANISOU 2365 O GLU A1109 21516 18317 12909 1685 -212 -781 O ATOM 2366 CB GLU A1109 38.458 -8.418 -47.950 1.00139.10 C ANISOU 2366 CB GLU A1109 22282 18077 12494 1516 348 -461 C ATOM 2367 CG GLU A1109 38.040 -8.862 -49.344 1.00149.18 C ANISOU 2367 CG GLU A1109 23774 19326 13580 1854 247 -550 C ATOM 2368 CD GLU A1109 38.033 -7.751 -50.377 1.00167.81 C ANISOU 2368 CD GLU A1109 26778 21442 15539 2040 329 -494 C ATOM 2369 OE1 GLU A1109 37.185 -6.836 -50.265 1.00153.70 O ANISOU 2369 OE1 GLU A1109 25288 19527 13583 2258 182 -534 O ATOM 2370 OE2 GLU A1109 38.864 -7.803 -51.313 1.00164.11 O ANISOU 2370 OE2 GLU A1109 26542 20907 14906 1988 541 -419 O ATOM 2371 N LYS A1110 36.534 -11.155 -47.248 1.00136.88 N ANISOU 2371 N LYS A1110 21073 18205 12730 1762 -199 -846 N ATOM 2372 CA LYS A1110 35.232 -11.839 -47.193 1.00136.62 C ANISOU 2372 CA LYS A1110 20830 18302 12778 1945 -474 -1074 C ATOM 2373 C LYS A1110 34.971 -12.421 -45.791 1.00139.21 C ANISOU 2373 C LYS A1110 20739 18750 13406 1700 -523 -1124 C ATOM 2374 O LYS A1110 33.819 -12.469 -45.354 1.00139.06 O ANISOU 2374 O LYS A1110 20567 18830 13441 1778 -718 -1304 O ATOM 2375 CB LYS A1110 35.170 -12.960 -48.244 1.00139.47 C ANISOU 2375 CB LYS A1110 21164 18724 13103 2092 -532 -1177 C ATOM 2376 CG LYS A1110 33.769 -13.262 -48.755 1.00150.34 C ANISOU 2376 CG LYS A1110 22508 20213 14401 2372 -816 -1438 C ATOM 2377 CD LYS A1110 33.180 -14.530 -48.153 1.00155.10 C ANISOU 2377 CD LYS A1110 22705 20983 15243 2227 -928 -1617 C ATOM 2378 CE LYS A1110 31.926 -14.914 -48.895 1.00163.23 C ANISOU 2378 CE LYS A1110 23700 22159 16160 2479 -1182 -1902 C ATOM 2379 NZ LYS A1110 31.201 -16.025 -48.236 1.00168.59 N ANISOU 2379 NZ LYS A1110 24006 23004 17045 2287 -1280 -2112 N ATOM 2380 N LEU A1111 36.035 -12.883 -45.105 1.00134.35 N ANISOU 2380 N LEU A1111 19938 18141 12967 1413 -347 -980 N ATOM 2381 CA LEU A1111 35.927 -13.422 -43.753 1.00132.45 C ANISOU 2381 CA LEU A1111 19362 17982 12982 1176 -372 -999 C ATOM 2382 C LEU A1111 35.789 -12.287 -42.740 1.00137.08 C ANISOU 2382 C LEU A1111 19968 18526 13590 1050 -352 -933 C ATOM 2383 O LEU A1111 35.164 -12.482 -41.696 1.00136.03 O ANISOU 2383 O LEU A1111 19612 18458 13616 935 -441 -1014 O ATOM 2384 CB LEU A1111 37.119 -14.324 -43.407 1.00131.41 C ANISOU 2384 CB LEU A1111 19053 17881 12996 980 -218 -878 C ATOM 2385 CG LEU A1111 37.072 -15.741 -43.968 1.00135.77 C ANISOU 2385 CG LEU A1111 19518 18476 13593 1063 -265 -975 C ATOM 2386 CD1 LEU A1111 38.451 -16.328 -44.029 1.00135.70 C ANISOU 2386 CD1 LEU A1111 19451 18484 13625 986 -87 -833 C ATOM 2387 CD2 LEU A1111 36.149 -16.636 -43.152 1.00137.17 C ANISOU 2387 CD2 LEU A1111 19478 18705 13934 969 -407 -1134 C ATOM 2388 N LYS A1112 36.363 -11.098 -43.054 1.00134.87 N ANISOU 2388 N LYS A1112 19990 18124 13132 1057 -221 -793 N ATOM 2389 CA LYS A1112 36.276 -9.887 -42.229 1.00134.54 C ANISOU 2389 CA LYS A1112 20065 18000 13056 951 -184 -725 C ATOM 2390 C LYS A1112 34.818 -9.404 -42.208 1.00139.01 C ANISOU 2390 C LYS A1112 20702 18574 13541 1214 -408 -902 C ATOM 2391 O LYS A1112 34.298 -9.083 -41.136 1.00137.50 O ANISOU 2391 O LYS A1112 20372 18415 13456 1122 -468 -946 O ATOM 2392 CB LYS A1112 37.211 -8.792 -42.764 1.00138.44 C ANISOU 2392 CB LYS A1112 20941 18335 13327 889 30 -556 C ATOM 2393 CG LYS A1112 38.639 -8.897 -42.246 1.00150.70 C ANISOU 2393 CG LYS A1112 22343 19932 14982 535 268 -397 C ATOM 2394 CD LYS A1112 39.486 -7.719 -42.721 1.00162.53 C ANISOU 2394 CD LYS A1112 24231 21285 16240 407 505 -263 C ATOM 2395 CE LYS A1112 40.519 -7.281 -41.706 1.00173.04 C ANISOU 2395 CE LYS A1112 25422 22664 17660 7 698 -148 C ATOM 2396 NZ LYS A1112 41.724 -8.153 -41.709 1.00181.15 N ANISOU 2396 NZ LYS A1112 26126 23890 18813 -175 839 -104 N ATOM 2397 N ASN A1113 34.150 -9.431 -43.394 1.00137.45 N ANISOU 2397 N ASN A1113 20694 18378 13153 1555 -542 -1025 N ATOM 2398 CA ASN A1113 32.734 -9.097 -43.606 1.00138.71 C ANISOU 2398 CA ASN A1113 20889 18612 13202 1885 -791 -1244 C ATOM 2399 C ASN A1113 31.834 -10.129 -42.903 1.00141.28 C ANISOU 2399 C ASN A1113 20747 19168 13766 1805 -947 -1460 C ATOM 2400 O ASN A1113 30.677 -9.832 -42.592 1.00142.02 O ANISOU 2400 O ASN A1113 20737 19385 13841 1968 -1126 -1658 O ATOM 2401 CB ASN A1113 32.401 -9.073 -45.109 1.00142.46 C ANISOU 2401 CB ASN A1113 21652 19063 13414 2256 -895 -1326 C ATOM 2402 CG ASN A1113 33.067 -7.984 -45.926 1.00168.90 C ANISOU 2402 CG ASN A1113 25552 22164 16459 2379 -754 -1150 C ATOM 2403 OD1 ASN A1113 33.909 -7.208 -45.450 1.00161.89 O ANISOU 2403 OD1 ASN A1113 24858 21111 15542 2153 -544 -956 O ATOM 2404 ND2 ASN A1113 32.706 -7.917 -47.199 1.00164.21 N ANISOU 2404 ND2 ASN A1113 25247 21535 15611 2725 -857 -1224 N ATOM 2405 N LEU A1114 32.376 -11.344 -42.677 1.00135.39 N ANISOU 2405 N LEU A1114 19741 18477 13222 1557 -868 -1433 N ATOM 2406 CA LEU A1114 31.718 -12.450 -41.988 1.00133.64 C ANISOU 2406 CA LEU A1114 19140 18422 13215 1398 -957 -1611 C ATOM 2407 C LEU A1114 31.996 -12.431 -40.473 1.00134.03 C ANISOU 2407 C LEU A1114 18992 18460 13474 1071 -863 -1524 C ATOM 2408 O LEU A1114 31.418 -13.236 -39.740 1.00133.00 O ANISOU 2408 O LEU A1114 18589 18438 13505 905 -914 -1666 O ATOM 2409 CB LEU A1114 32.152 -13.790 -42.605 1.00133.49 C ANISOU 2409 CB LEU A1114 19041 18422 13255 1337 -921 -1627 C ATOM 2410 CG LEU A1114 31.256 -14.337 -43.706 1.00139.89 C ANISOU 2410 CG LEU A1114 19855 19352 13946 1580 -1094 -1866 C ATOM 2411 CD1 LEU A1114 32.019 -15.300 -44.596 1.00140.21 C ANISOU 2411 CD1 LEU A1114 19979 19330 13963 1582 -1011 -1800 C ATOM 2412 CD2 LEU A1114 30.016 -15.004 -43.121 1.00142.42 C ANISOU 2412 CD2 LEU A1114 19858 19874 14381 1484 -1241 -2157 C ATOM 2413 N GLY A1115 32.866 -11.515 -40.034 1.00128.67 N ANISOU 2413 N GLY A1115 18473 17644 12770 965 -719 -1302 N ATOM 2414 CA GLY A1115 33.241 -11.324 -38.635 1.00126.37 C ANISOU 2414 CA GLY A1115 18041 17331 12644 670 -628 -1198 C ATOM 2415 C GLY A1115 34.056 -12.444 -38.019 1.00127.48 C ANISOU 2415 C GLY A1115 17971 17489 12976 402 -531 -1112 C ATOM 2416 O GLY A1115 33.857 -12.783 -36.848 1.00125.94 O ANISOU 2416 O GLY A1115 17584 17330 12940 193 -536 -1138 O ATOM 2417 N ALA A1116 35.000 -13.004 -38.801 1.00123.16 N ANISOU 2417 N ALA A1116 17485 16914 12396 428 -441 -1009 N ATOM 2418 CA ALA A1116 35.900 -14.097 -38.408 1.00121.36 C ANISOU 2418 CA ALA A1116 17103 16704 12306 260 -355 -924 C ATOM 2419 C ALA A1116 37.197 -13.577 -37.754 1.00122.36 C ANISOU 2419 C ALA A1116 17216 16811 12465 69 -195 -711 C ATOM 2420 O ALA A1116 37.603 -12.442 -38.024 1.00122.67 O ANISOU 2420 O ALA A1116 17426 16801 12383 67 -107 -615 O ATOM 2421 CB ALA A1116 36.229 -14.941 -39.627 1.00122.93 C ANISOU 2421 CB ALA A1116 17368 16907 12433 424 -344 -947 C ATOM 2422 N GLU A1117 37.848 -14.404 -36.906 1.00115.96 N ANISOU 2422 N GLU A1117 16225 16040 11795 -92 -156 -651 N ATOM 2423 CA GLU A1117 39.083 -14.008 -36.216 1.00114.74 C ANISOU 2423 CA GLU A1117 15998 15926 11673 -271 -28 -484 C ATOM 2424 C GLU A1117 40.366 -14.419 -36.976 1.00115.80 C ANISOU 2424 C GLU A1117 16113 16136 11751 -211 96 -393 C ATOM 2425 O GLU A1117 40.940 -15.484 -36.727 1.00115.45 O ANISOU 2425 O GLU A1117 15933 16153 11780 -190 93 -380 O ATOM 2426 CB GLU A1117 39.102 -14.494 -34.747 1.00115.32 C ANISOU 2426 CB GLU A1117 15895 16020 11901 -460 -68 -470 C ATOM 2427 CG GLU A1117 40.069 -13.716 -33.861 1.00127.86 C ANISOU 2427 CG GLU A1117 17411 17663 13506 -666 27 -332 C ATOM 2428 CD GLU A1117 40.160 -14.144 -32.407 1.00151.82 C ANISOU 2428 CD GLU A1117 20299 20718 16666 -834 -19 -310 C ATOM 2429 OE1 GLU A1117 39.215 -13.849 -31.639 1.00152.30 O ANISOU 2429 OE1 GLU A1117 20376 20712 16779 -930 -85 -371 O ATOM 2430 OE2 GLU A1117 41.204 -14.718 -32.021 1.00144.22 O ANISOU 2430 OE2 GLU A1117 19212 19851 15734 -858 12 -236 O ATOM 2431 N ILE A1118 40.826 -13.540 -37.878 1.00110.15 N ANISOU 2431 N ILE A1118 15555 15412 10884 -179 214 -337 N ATOM 2432 CA ILE A1118 42.050 -13.760 -38.644 1.00109.65 C ANISOU 2432 CA ILE A1118 15469 15447 10745 -149 366 -268 C ATOM 2433 C ILE A1118 43.251 -13.511 -37.713 1.00110.27 C ANISOU 2433 C ILE A1118 15339 15677 10881 -380 480 -172 C ATOM 2434 O ILE A1118 43.699 -12.376 -37.537 1.00109.97 O ANISOU 2434 O ILE A1118 15365 15652 10766 -576 604 -109 O ATOM 2435 CB ILE A1118 42.048 -12.972 -39.988 1.00114.06 C ANISOU 2435 CB ILE A1118 16313 15930 11095 -46 466 -261 C ATOM 2436 CG1 ILE A1118 40.940 -13.504 -40.924 1.00114.62 C ANISOU 2436 CG1 ILE A1118 16533 15904 11112 227 319 -382 C ATOM 2437 CG2 ILE A1118 43.405 -13.031 -40.700 1.00116.03 C ANISOU 2437 CG2 ILE A1118 16531 16304 11253 -83 674 -196 C ATOM 2438 CD1 ILE A1118 39.666 -12.668 -40.992 1.00122.80 C ANISOU 2438 CD1 ILE A1118 17770 16818 12071 318 190 -459 C ATOM 2439 N VAL A1119 43.717 -14.595 -37.074 1.00104.59 N ANISOU 2439 N VAL A1119 14391 15067 10282 -350 425 -174 N ATOM 2440 CA VAL A1119 44.791 -14.609 -36.079 1.00104.14 C ANISOU 2440 CA VAL A1119 14088 15194 10287 -508 474 -113 C ATOM 2441 C VAL A1119 46.208 -14.286 -36.643 1.00107.93 C ANISOU 2441 C VAL A1119 14442 15899 10667 -569 670 -78 C ATOM 2442 O VAL A1119 47.085 -13.885 -35.872 1.00108.41 O ANISOU 2442 O VAL A1119 14301 16145 10743 -765 736 -46 O ATOM 2443 CB VAL A1119 44.766 -15.950 -35.297 1.00107.67 C ANISOU 2443 CB VAL A1119 14399 15660 10852 -388 334 -137 C ATOM 2444 CG1 VAL A1119 45.375 -17.103 -36.097 1.00108.74 C ANISOU 2444 CG1 VAL A1119 14491 15875 10950 -132 351 -164 C ATOM 2445 CG2 VAL A1119 45.419 -15.812 -33.923 1.00107.54 C ANISOU 2445 CG2 VAL A1119 14181 15773 10905 -556 311 -86 C ATOM 2446 N GLN A1120 46.436 -14.467 -37.954 1.00103.52 N ANISOU 2446 N GLN A1120 13987 15347 9998 -420 768 -101 N ATOM 2447 CA GLN A1120 47.752 -14.213 -38.549 1.00104.35 C ANISOU 2447 CA GLN A1120 13963 15687 9998 -490 980 -95 C ATOM 2448 C GLN A1120 47.633 -13.640 -39.963 1.00106.41 C ANISOU 2448 C GLN A1120 14508 15840 10083 -460 1131 -100 C ATOM 2449 O GLN A1120 46.626 -13.873 -40.637 1.00104.59 O ANISOU 2449 O GLN A1120 14525 15393 9823 -265 1030 -123 O ATOM 2450 CB GLN A1120 48.580 -15.516 -38.538 1.00106.47 C ANISOU 2450 CB GLN A1120 13966 16172 10317 -265 946 -133 C ATOM 2451 CG GLN A1120 50.058 -15.398 -38.945 1.00115.98 C ANISOU 2451 CG GLN A1120 14916 17719 11431 -323 1151 -164 C ATOM 2452 CD GLN A1120 50.939 -14.769 -37.898 1.00126.24 C ANISOU 2452 CD GLN A1120 15923 19285 12755 -599 1210 -164 C ATOM 2453 OE1 GLN A1120 50.635 -14.768 -36.704 1.00119.31 O ANISOU 2453 OE1 GLN A1120 14973 18373 11985 -670 1059 -135 O ATOM 2454 NE2 GLN A1120 52.068 -14.238 -38.328 1.00118.47 N ANISOU 2454 NE2 GLN A1120 14757 18594 11662 -777 1438 -213 N ATOM 2455 N ASP A1121 48.660 -12.874 -40.399 1.00103.76 N ANISOU 2455 N ASP A1121 14146 15665 9612 -670 1378 -91 N ATOM 2456 CA ASP A1121 48.736 -12.296 -41.745 1.00104.56 C ANISOU 2456 CA ASP A1121 14549 15671 9506 -675 1567 -93 C ATOM 2457 C ASP A1121 48.909 -13.443 -42.730 1.00105.21 C ANISOU 2457 C ASP A1121 14588 15813 9574 -360 1555 -143 C ATOM 2458 O ASP A1121 49.897 -14.173 -42.650 1.00106.07 O ANISOU 2458 O ASP A1121 14374 16201 9727 -302 1612 -183 O ATOM 2459 CB ASP A1121 49.924 -11.314 -41.864 1.00109.57 C ANISOU 2459 CB ASP A1121 15135 16501 9997 -1036 1871 -94 C ATOM 2460 CG ASP A1121 49.539 -9.849 -41.936 1.00122.68 C ANISOU 2460 CG ASP A1121 17196 17922 11493 -1308 1995 -41 C ATOM 2461 OD1 ASP A1121 48.828 -9.466 -42.897 1.00123.57 O ANISOU 2461 OD1 ASP A1121 17745 17759 11449 -1175 2007 -19 O ATOM 2462 OD2 ASP A1121 49.993 -9.073 -41.064 1.00130.29 O ANISOU 2462 OD2 ASP A1121 18066 18979 12460 -1647 2085 -30 O ATOM 2463 N GLY A1122 47.924 -13.612 -43.605 1.00 98.29 N ANISOU 2463 N GLY A1122 14030 14687 8630 -138 1462 -152 N ATOM 2464 CA GLY A1122 47.876 -14.664 -44.614 1.00 97.54 C ANISOU 2464 CA GLY A1122 13975 14586 8501 168 1431 -204 C ATOM 2465 C GLY A1122 49.169 -15.011 -45.330 1.00100.77 C ANISOU 2465 C GLY A1122 14225 15245 8819 186 1657 -236 C ATOM 2466 O GLY A1122 49.962 -14.124 -45.657 1.00102.15 O ANISOU 2466 O GLY A1122 14426 15531 8854 -59 1910 -226 O ATOM 2467 N LEU A1123 49.392 -16.320 -45.555 1.00 95.19 N ANISOU 2467 N LEU A1123 13361 14632 8178 468 1578 -287 N ATOM 2468 CA LEU A1123 50.575 -16.842 -46.231 1.00 96.30 C ANISOU 2468 CA LEU A1123 13319 15033 8238 564 1767 -341 C ATOM 2469 C LEU A1123 50.366 -16.771 -47.726 1.00100.77 C ANISOU 2469 C LEU A1123 14220 15456 8613 681 1886 -359 C ATOM 2470 O LEU A1123 49.372 -17.288 -48.237 1.00 98.82 O ANISOU 2470 O LEU A1123 14226 14965 8357 908 1718 -371 O ATOM 2471 CB LEU A1123 50.872 -18.284 -45.776 1.00 95.83 C ANISOU 2471 CB LEU A1123 13002 15104 8307 860 1617 -387 C ATOM 2472 CG LEU A1123 52.115 -18.991 -46.326 1.00102.63 C ANISOU 2472 CG LEU A1123 13621 16276 9097 1040 1775 -462 C ATOM 2473 CD1 LEU A1123 53.406 -18.324 -45.869 1.00104.75 C ANISOU 2473 CD1 LEU A1123 13513 16946 9343 788 1979 -498 C ATOM 2474 CD2 LEU A1123 52.121 -20.440 -45.915 1.00104.49 C ANISOU 2474 CD2 LEU A1123 13750 16525 9427 1399 1582 -497 C ATOM 2475 N ARG A1124 51.296 -16.094 -48.421 1.00100.12 N ANISOU 2475 N ARG A1124 14149 15532 8360 499 2187 -375 N ATOM 2476 CA ARG A1124 51.277 -15.896 -49.873 1.00101.23 C ANISOU 2476 CA ARG A1124 14633 15553 8276 568 2356 -390 C ATOM 2477 C ARG A1124 52.595 -16.425 -50.461 1.00107.46 C ANISOU 2477 C ARG A1124 15160 16679 8990 615 2601 -474 C ATOM 2478 O ARG A1124 53.660 -15.863 -50.193 1.00109.19 O ANISOU 2478 O ARG A1124 15126 17193 9166 333 2842 -511 O ATOM 2479 CB ARG A1124 51.045 -14.405 -50.210 1.00101.49 C ANISOU 2479 CB ARG A1124 15045 15398 8117 265 2521 -331 C ATOM 2480 CG ARG A1124 49.690 -13.870 -49.735 1.00105.69 C ANISOU 2480 CG ARG A1124 15859 15606 8693 287 2272 -267 C ATOM 2481 CD ARG A1124 49.647 -12.359 -49.646 1.00116.12 C ANISOU 2481 CD ARG A1124 17491 16781 9848 -36 2430 -205 C ATOM 2482 NE ARG A1124 48.440 -11.900 -48.953 1.00127.82 N ANISOU 2482 NE ARG A1124 19149 18016 11402 7 2177 -160 N ATOM 2483 CZ ARG A1124 48.392 -11.532 -47.674 1.00147.96 C ANISOU 2483 CZ ARG A1124 21491 20618 14110 -188 2099 -130 C ATOM 2484 NH1 ARG A1124 49.493 -11.543 -46.929 1.00134.25 N ANISOU 2484 NH1 ARG A1124 19361 19175 12473 -443 2240 -140 N ATOM 2485 NH2 ARG A1124 47.247 -11.139 -47.132 1.00140.54 N ANISOU 2485 NH2 ARG A1124 20722 19458 13219 -120 1876 -105 N ATOM 2486 N ILE A1125 52.520 -17.541 -51.217 1.00103.84 N ANISOU 2486 N ILE A1125 14741 16198 8517 973 2535 -523 N ATOM 2487 CA ILE A1125 53.674 -18.227 -51.830 1.00105.94 C ANISOU 2487 CA ILE A1125 14768 16775 8711 1114 2736 -619 C ATOM 2488 C ILE A1125 53.893 -17.824 -53.287 1.00110.22 C ANISOU 2488 C ILE A1125 15635 17248 8995 1076 3002 -643 C ATOM 2489 O ILE A1125 52.963 -17.862 -54.096 1.00108.23 O ANISOU 2489 O ILE A1125 15817 16663 8642 1225 2906 -607 O ATOM 2490 CB ILE A1125 53.578 -19.778 -51.661 1.00108.29 C ANISOU 2490 CB ILE A1125 14917 17095 9133 1547 2514 -665 C ATOM 2491 CG1 ILE A1125 53.518 -20.181 -50.179 1.00106.81 C ANISOU 2491 CG1 ILE A1125 14425 16992 9167 1575 2285 -645 C ATOM 2492 CG2 ILE A1125 54.711 -20.524 -52.378 1.00111.98 C ANISOU 2492 CG2 ILE A1125 15177 17868 9504 1763 2711 -774 C ATOM 2493 CD1 ILE A1125 52.195 -20.597 -49.757 1.00109.78 C ANISOU 2493 CD1 ILE A1125 15043 17012 9657 1688 1984 -590 C ATOM 2494 N ASP A1126 55.141 -17.465 -53.612 1.00109.73 N ANISOU 2494 N ASP A1126 15350 17528 8816 875 3339 -722 N ATOM 2495 CA ASP A1126 55.537 -17.083 -54.957 1.00112.31 C ANISOU 2495 CA ASP A1126 15959 17837 8876 794 3652 -760 C ATOM 2496 C ASP A1126 56.085 -18.308 -55.680 1.00118.00 C ANISOU 2496 C ASP A1126 16523 18743 9569 1163 3697 -862 C ATOM 2497 O ASP A1126 57.180 -18.781 -55.360 1.00119.69 O ANISOU 2497 O ASP A1126 16250 19389 9836 1206 3816 -974 O ATOM 2498 CB ASP A1126 56.569 -15.947 -54.912 1.00117.24 C ANISOU 2498 CB ASP A1126 16453 18730 9364 300 4034 -811 C ATOM 2499 CG ASP A1126 56.333 -14.844 -55.921 1.00131.17 C ANISOU 2499 CG ASP A1126 18795 20211 10831 31 4294 -764 C ATOM 2500 OD1 ASP A1126 56.108 -15.162 -57.116 1.00132.43 O ANISOU 2500 OD1 ASP A1126 19310 20187 10820 248 4347 -766 O ATOM 2501 OD2 ASP A1126 56.404 -13.662 -55.528 1.00139.49 O ANISOU 2501 OD2 ASP A1126 19977 21222 11799 -397 4454 -729 O ATOM 2502 N GLY A1127 55.291 -18.835 -56.609 1.00113.64 N ANISOU 2502 N GLY A1127 16378 17871 8929 1452 3580 -835 N ATOM 2503 CA GLY A1127 55.636 -20.011 -57.399 1.00114.80 C ANISOU 2503 CA GLY A1127 16489 18106 9025 1827 3604 -921 C ATOM 2504 C GLY A1127 55.598 -21.307 -56.616 1.00117.57 C ANISOU 2504 C GLY A1127 16538 18543 9591 2189 3326 -953 C ATOM 2505 O GLY A1127 54.579 -21.630 -55.992 1.00114.24 O ANISOU 2505 O GLY A1127 16241 17851 9315 2293 3007 -884 O ATOM 2506 N ASP A1128 56.726 -22.058 -56.646 1.00116.50 N ANISOU 2506 N ASP A1128 16018 18792 9456 2387 3458 -1071 N ATOM 2507 CA ASP A1128 56.873 -23.360 -55.991 1.00115.60 C ANISOU 2507 CA ASP A1128 15660 18774 9488 2790 3229 -1115 C ATOM 2508 C ASP A1128 56.971 -23.272 -54.464 1.00118.39 C ANISOU 2508 C ASP A1128 15656 19276 10051 2703 3044 -1084 C ATOM 2509 O ASP A1128 57.792 -22.513 -53.939 1.00119.11 O ANISOU 2509 O ASP A1128 15382 19716 10157 2419 3209 -1124 O ATOM 2510 CB ASP A1128 58.045 -24.163 -56.576 1.00120.65 C ANISOU 2510 CB ASP A1128 16039 19780 10022 3090 3426 -1264 C ATOM 2511 CG ASP A1128 57.789 -25.656 -56.563 1.00126.93 C ANISOU 2511 CG ASP A1128 16934 20437 10857 3610 3193 -1290 C ATOM 2512 OD1 ASP A1128 58.013 -26.288 -55.509 1.00126.05 O ANISOU 2512 OD1 ASP A1128 16557 20456 10880 3816 3005 -1306 O ATOM 2513 OD2 ASP A1128 57.325 -26.186 -57.596 1.00133.24 O ANISOU 2513 OD2 ASP A1128 18122 20968 11536 3807 3193 -1295 O ATOM 2514 N PRO A1129 56.153 -24.063 -53.737 1.00112.96 N ANISOU 2514 N PRO A1129 15077 18333 9510 2928 2712 -1026 N ATOM 2515 CA PRO A1129 56.207 -24.011 -52.271 1.00111.98 C ANISOU 2515 CA PRO A1129 14657 18322 9568 2855 2531 -992 C ATOM 2516 C PRO A1129 57.417 -24.707 -51.645 1.00120.29 C ANISOU 2516 C PRO A1129 15237 19820 10647 3119 2543 -1100 C ATOM 2517 O PRO A1129 57.838 -24.306 -50.555 1.00120.70 O ANISOU 2517 O PRO A1129 14942 20116 10801 2966 2494 -1102 O ATOM 2518 CB PRO A1129 54.875 -24.625 -51.828 1.00110.22 C ANISOU 2518 CB PRO A1129 14773 17650 9457 2979 2208 -908 C ATOM 2519 CG PRO A1129 54.194 -25.100 -53.061 1.00114.23 C ANISOU 2519 CG PRO A1129 15709 17852 9841 3145 2207 -920 C ATOM 2520 CD PRO A1129 55.133 -25.022 -54.204 1.00112.92 C ANISOU 2520 CD PRO A1129 15486 17923 9496 3219 2501 -1002 C ATOM 2521 N ARG A1130 57.994 -25.721 -52.323 1.00119.25 N ANISOU 2521 N ARG A1130 15087 19812 10409 3533 2601 -1200 N ATOM 2522 CA ARG A1130 59.177 -26.438 -51.827 1.00122.27 C ANISOU 2522 CA ARG A1130 15030 20647 10780 3876 2603 -1327 C ATOM 2523 C ARG A1130 60.389 -25.504 -51.679 1.00129.59 C ANISOU 2523 C ARG A1130 15411 22155 11671 3591 2867 -1445 C ATOM 2524 O ARG A1130 61.212 -25.718 -50.786 1.00131.14 O ANISOU 2524 O ARG A1130 15153 22763 11911 3734 2803 -1537 O ATOM 2525 CB ARG A1130 59.518 -27.631 -52.728 1.00124.24 C ANISOU 2525 CB ARG A1130 15421 20894 10891 4379 2641 -1419 C ATOM 2526 CG ARG A1130 58.714 -28.885 -52.414 1.00127.31 C ANISOU 2526 CG ARG A1130 16208 20852 11311 4766 2343 -1357 C ATOM 2527 CD ARG A1130 58.530 -29.741 -53.653 1.00127.52 C ANISOU 2527 CD ARG A1130 16611 20656 11185 5074 2410 -1401 C ATOM 2528 NE ARG A1130 57.521 -29.168 -54.545 1.00122.65 N ANISOU 2528 NE ARG A1130 16391 19669 10543 4759 2465 -1322 N ATOM 2529 CZ ARG A1130 56.226 -29.465 -54.503 1.00125.92 C ANISOU 2529 CZ ARG A1130 17246 19591 11006 4710 2253 -1235 C ATOM 2530 NH1 ARG A1130 55.769 -30.351 -53.623 1.00116.65 N ANISOU 2530 NH1 ARG A1130 16214 18199 9908 4915 1999 -1208 N ATOM 2531 NH2 ARG A1130 55.379 -28.884 -55.341 1.00 95.88 N ANISOU 2531 NH2 ARG A1130 13755 15519 7156 4457 2296 -1189 N ATOM 2532 N ALA A1131 60.460 -24.445 -52.526 1.00126.72 N ANISOU 2532 N ALA A1131 15119 21817 11213 3171 3162 -1450 N ATOM 2533 CA ALA A1131 61.508 -23.418 -52.550 1.00129.54 C ANISOU 2533 CA ALA A1131 15046 22672 11501 2774 3477 -1571 C ATOM 2534 C ALA A1131 61.630 -22.660 -51.226 1.00133.05 C ANISOU 2534 C ALA A1131 15175 23297 12082 2446 3381 -1548 C ATOM 2535 O ALA A1131 62.720 -22.196 -50.883 1.00136.09 O ANISOU 2535 O ALA A1131 15040 24233 12436 2258 3558 -1703 O ATOM 2536 CB ALA A1131 61.236 -22.434 -53.676 1.00130.31 C ANISOU 2536 CB ALA A1131 15488 22573 11450 2364 3775 -1533 C ATOM 2537 N ALA A1132 60.516 -22.534 -50.491 1.00125.50 N ANISOU 2537 N ALA A1132 14518 21899 11266 2366 3108 -1373 N ATOM 2538 CA ALA A1132 60.478 -21.822 -49.224 1.00124.37 C ANISOU 2538 CA ALA A1132 14153 21851 11253 2059 2996 -1331 C ATOM 2539 C ALA A1132 59.667 -22.577 -48.153 1.00124.99 C ANISOU 2539 C ALA A1132 14369 21625 11496 2334 2601 -1216 C ATOM 2540 O ALA A1132 58.747 -22.012 -47.554 1.00121.18 O ANISOU 2540 O ALA A1132 14114 20812 11116 2075 2465 -1082 O ATOM 2541 CB ALA A1132 59.924 -20.422 -49.449 1.00123.73 C ANISOU 2541 CB ALA A1132 14341 21533 11139 1489 3162 -1236 C ATOM 2542 N ARG A1133 60.027 -23.857 -47.905 1.00122.67 N ANISOU 2542 N ARG A1133 13958 21445 11206 2865 2428 -1278 N ATOM 2543 CA ARG A1133 59.374 -24.715 -46.906 1.00120.12 C ANISOU 2543 CA ARG A1133 13802 20841 10997 3157 2079 -1188 C ATOM 2544 C ARG A1133 59.519 -24.125 -45.499 1.00123.54 C ANISOU 2544 C ARG A1133 13947 21445 11547 2917 1950 -1163 C ATOM 2545 O ARG A1133 58.568 -24.184 -44.721 1.00120.37 O ANISOU 2545 O ARG A1133 13804 20672 11258 2856 1727 -1034 O ATOM 2546 CB ARG A1133 59.923 -26.157 -46.960 1.00123.00 C ANISOU 2546 CB ARG A1133 14121 21327 11286 3788 1961 -1279 C ATOM 2547 CG ARG A1133 59.170 -27.153 -46.070 1.00131.11 C ANISOU 2547 CG ARG A1133 15465 21970 12382 4096 1628 -1182 C ATOM 2548 CD ARG A1133 59.901 -28.473 -45.885 1.00143.01 C ANISOU 2548 CD ARG A1133 16898 23654 13784 4728 1503 -1281 C ATOM 2549 NE ARG A1133 59.046 -29.483 -45.251 1.00147.00 N ANISOU 2549 NE ARG A1133 17869 23674 14309 4993 1229 -1180 N ATOM 2550 CZ ARG A1133 59.136 -29.868 -43.980 1.00157.53 C ANISOU 2550 CZ ARG A1133 19165 25019 15672 5162 1000 -1154 C ATOM 2551 NH1 ARG A1133 58.312 -30.790 -43.500 1.00140.64 N ANISOU 2551 NH1 ARG A1133 17523 22393 13522 5357 792 -1067 N ATOM 2552 NH2 ARG A1133 60.059 -29.343 -43.183 1.00144.11 N ANISOU 2552 NH2 ARG A1133 16946 23819 13992 5126 983 -1228 N ATOM 2553 N ASP A1134 60.702 -23.545 -45.184 1.00123.35 N ANISOU 2553 N ASP A1134 13381 22000 11488 2762 2098 -1302 N ATOM 2554 CA ASP A1134 61.014 -22.906 -43.891 1.00122.83 C ANISOU 2554 CA ASP A1134 12979 22182 11508 2505 2003 -1311 C ATOM 2555 C ASP A1134 60.180 -21.653 -43.637 1.00122.09 C ANISOU 2555 C ASP A1134 13112 21782 11495 1925 2057 -1177 C ATOM 2556 O ASP A1134 59.878 -21.349 -42.484 1.00119.70 O ANISOU 2556 O ASP A1134 12767 21417 11297 1776 1882 -1111 O ATOM 2557 CB ASP A1134 62.530 -22.623 -43.714 1.00129.52 C ANISOU 2557 CB ASP A1134 13155 23783 12273 2472 2163 -1537 C ATOM 2558 CG ASP A1134 63.343 -22.188 -44.936 1.00143.22 C ANISOU 2558 CG ASP A1134 14679 25870 13869 2287 2544 -1693 C ATOM 2559 OD1 ASP A1134 62.730 -21.845 -45.981 1.00142.50 O ANISOU 2559 OD1 ASP A1134 14999 25412 13733 2098 2720 -1605 O ATOM 2560 OD2 ASP A1134 64.590 -22.175 -44.842 1.00152.46 O ANISOU 2560 OD2 ASP A1134 15271 27697 14960 2326 2669 -1916 O ATOM 2561 N ASP A1135 59.796 -20.945 -44.723 1.00117.59 N ANISOU 2561 N ASP A1135 12819 21004 10856 1630 2295 -1138 N ATOM 2562 CA ASP A1135 58.946 -19.751 -44.705 1.00114.31 C ANISOU 2562 CA ASP A1135 12716 20247 10470 1140 2363 -1013 C ATOM 2563 C ASP A1135 57.491 -20.166 -44.431 1.00111.42 C ANISOU 2563 C ASP A1135 12823 19297 10214 1285 2088 -847 C ATOM 2564 O ASP A1135 56.784 -19.454 -43.717 1.00108.70 O ANISOU 2564 O ASP A1135 12617 18729 9954 1000 1998 -750 O ATOM 2565 CB ASP A1135 59.053 -18.979 -46.036 1.00117.94 C ANISOU 2565 CB ASP A1135 13374 20666 10772 863 2700 -1037 C ATOM 2566 CG ASP A1135 60.446 -18.465 -46.373 1.00133.76 C ANISOU 2566 CG ASP A1135 14934 23243 12647 616 3030 -1222 C ATOM 2567 OD1 ASP A1135 61.316 -19.293 -46.735 1.00136.22 O ANISOU 2567 OD1 ASP A1135 14922 23933 12902 944 3086 -1368 O ATOM 2568 OD2 ASP A1135 60.654 -17.232 -46.315 1.00142.34 O ANISOU 2568 OD2 ASP A1135 16018 24395 13670 86 3249 -1232 O ATOM 2569 N ILE A1136 57.065 -21.335 -44.981 1.00105.48 N ANISOU 2569 N ILE A1136 12307 18320 9450 1718 1965 -836 N ATOM 2570 CA ILE A1136 55.739 -21.946 -44.798 1.00101.10 C ANISOU 2570 CA ILE A1136 12175 17258 8979 1878 1715 -725 C ATOM 2571 C ILE A1136 55.591 -22.355 -43.327 1.00104.51 C ANISOU 2571 C ILE A1136 12489 17680 9540 1955 1459 -688 C ATOM 2572 O ILE A1136 54.619 -21.957 -42.680 1.00102.00 O ANISOU 2572 O ILE A1136 12369 17065 9321 1749 1327 -594 O ATOM 2573 CB ILE A1136 55.527 -23.148 -45.774 1.00104.06 C ANISOU 2573 CB ILE A1136 12804 17456 9278 2301 1682 -757 C ATOM 2574 CG1 ILE A1136 55.400 -22.659 -47.227 1.00104.93 C ANISOU 2574 CG1 ILE A1136 13133 17481 9257 2193 1910 -771 C ATOM 2575 CG2 ILE A1136 54.322 -24.016 -45.377 1.00101.05 C ANISOU 2575 CG2 ILE A1136 12791 16628 8977 2481 1412 -686 C ATOM 2576 CD1 ILE A1136 55.818 -23.654 -48.256 1.00112.67 C ANISOU 2576 CD1 ILE A1136 14179 18511 10118 2577 1983 -853 C ATOM 2577 N VAL A1137 56.573 -23.126 -42.803 1.00102.90 N ANISOU 2577 N VAL A1137 11966 17814 9315 2267 1392 -772 N ATOM 2578 CA VAL A1137 56.626 -23.608 -41.421 1.00102.08 C ANISOU 2578 CA VAL A1137 11752 17747 9288 2409 1152 -751 C ATOM 2579 C VAL A1137 56.582 -22.429 -40.441 1.00104.93 C ANISOU 2579 C VAL A1137 11924 18205 9738 1959 1150 -708 C ATOM 2580 O VAL A1137 55.829 -22.479 -39.462 1.00102.40 O ANISOU 2580 O VAL A1137 11769 17623 9514 1889 958 -619 O ATOM 2581 CB VAL A1137 57.829 -24.570 -41.212 1.00109.48 C ANISOU 2581 CB VAL A1137 12374 19089 10135 2881 1099 -874 C ATOM 2582 CG1 VAL A1137 58.242 -24.682 -39.744 1.00109.84 C ANISOU 2582 CG1 VAL A1137 12171 19342 10223 2952 897 -883 C ATOM 2583 CG2 VAL A1137 57.525 -25.946 -41.796 1.00109.70 C ANISOU 2583 CG2 VAL A1137 12754 18839 10087 3372 1004 -875 C ATOM 2584 N GLY A1138 57.327 -21.365 -40.764 1.00102.52 N ANISOU 2584 N GLY A1138 11322 18244 9387 1627 1384 -775 N ATOM 2585 CA GLY A1138 57.370 -20.132 -39.985 1.00101.18 C ANISOU 2585 CA GLY A1138 10996 18178 9270 1150 1434 -751 C ATOM 2586 C GLY A1138 55.987 -19.568 -39.739 1.00 99.52 C ANISOU 2586 C GLY A1138 11206 17459 9149 895 1351 -603 C ATOM 2587 O GLY A1138 55.648 -19.236 -38.602 1.00 97.39 O ANISOU 2587 O GLY A1138 10916 17119 8969 732 1211 -547 O ATOM 2588 N TRP A1139 55.160 -19.525 -40.804 1.00 93.30 N ANISOU 2588 N TRP A1139 10799 16325 8327 901 1420 -552 N ATOM 2589 CA TRP A1139 53.778 -19.051 -40.766 1.00 89.17 C ANISOU 2589 CA TRP A1139 10677 15340 7863 727 1336 -442 C ATOM 2590 C TRP A1139 52.895 -19.942 -39.897 1.00 91.33 C ANISOU 2590 C TRP A1139 11111 15337 8252 932 1055 -390 C ATOM 2591 O TRP A1139 52.033 -19.414 -39.207 1.00 88.40 O ANISOU 2591 O TRP A1139 10882 14743 7964 719 958 -324 O ATOM 2592 CB TRP A1139 53.201 -18.947 -42.188 1.00 87.06 C ANISOU 2592 CB TRP A1139 10749 14829 7500 765 1455 -433 C ATOM 2593 CG TRP A1139 51.801 -18.405 -42.260 1.00 84.73 C ANISOU 2593 CG TRP A1139 10838 14117 7237 625 1365 -353 C ATOM 2594 CD1 TRP A1139 51.433 -17.094 -42.258 1.00 86.86 C ANISOU 2594 CD1 TRP A1139 11254 14279 7469 287 1460 -306 C ATOM 2595 CD2 TRP A1139 50.584 -19.164 -42.358 1.00 82.19 C ANISOU 2595 CD2 TRP A1139 10805 13451 6974 830 1162 -335 C ATOM 2596 NE1 TRP A1139 50.065 -16.984 -42.368 1.00 83.76 N ANISOU 2596 NE1 TRP A1139 11199 13518 7106 317 1313 -263 N ATOM 2597 CE2 TRP A1139 49.520 -18.239 -42.447 1.00 84.02 C ANISOU 2597 CE2 TRP A1139 11300 13421 7203 626 1135 -291 C ATOM 2598 CE3 TRP A1139 50.291 -20.538 -42.420 1.00 82.92 C ANISOU 2598 CE3 TRP A1139 10979 13431 7097 1161 1011 -368 C ATOM 2599 CZ2 TRP A1139 48.185 -18.643 -42.588 1.00 80.98 C ANISOU 2599 CZ2 TRP A1139 11185 12726 6858 737 956 -300 C ATOM 2600 CZ3 TRP A1139 48.966 -20.935 -42.539 1.00 81.93 C ANISOU 2600 CZ3 TRP A1139 11156 12966 7010 1218 854 -369 C ATOM 2601 CH2 TRP A1139 47.932 -19.994 -42.621 1.00 80.64 C ANISOU 2601 CH2 TRP A1139 11181 12605 6856 1006 825 -346 C ATOM 2602 N ALA A1140 53.093 -21.280 -39.936 1.00 89.74 N ANISOU 2602 N ALA A1140 10921 15138 8039 1336 939 -427 N ATOM 2603 CA ALA A1140 52.314 -22.233 -39.134 1.00 88.38 C ANISOU 2603 CA ALA A1140 10960 14684 7939 1519 702 -389 C ATOM 2604 C ALA A1140 52.734 -22.172 -37.664 1.00 94.90 C ANISOU 2604 C ALA A1140 11562 15669 8824 1466 574 -370 C ATOM 2605 O ALA A1140 51.904 -22.373 -36.772 1.00 92.79 O ANISOU 2605 O ALA A1140 11481 15142 8634 1404 416 -316 O ATOM 2606 CB ALA A1140 52.484 -23.637 -39.675 1.00 90.45 C ANISOU 2606 CB ALA A1140 11364 14878 8125 1958 646 -437 C ATOM 2607 N HIS A1141 54.020 -21.864 -37.419 1.00 95.30 N ANISOU 2607 N HIS A1141 11206 16173 8830 1472 650 -432 N ATOM 2608 CA HIS A1141 54.609 -21.688 -36.094 1.00 96.41 C ANISOU 2608 CA HIS A1141 11070 16560 9002 1418 538 -439 C ATOM 2609 C HIS A1141 54.029 -20.414 -35.453 1.00 96.19 C ANISOU 2609 C HIS A1141 11061 16425 9060 933 566 -372 C ATOM 2610 O HIS A1141 53.615 -20.443 -34.295 1.00 93.72 O ANISOU 2610 O HIS A1141 10806 15989 8815 867 406 -320 O ATOM 2611 CB HIS A1141 56.139 -21.604 -36.236 1.00101.82 C ANISOU 2611 CB HIS A1141 11271 17819 9596 1527 642 -567 C ATOM 2612 CG HIS A1141 56.843 -21.014 -35.057 1.00107.04 C ANISOU 2612 CG HIS A1141 11564 18831 10273 1342 585 -607 C ATOM 2613 ND1 HIS A1141 56.945 -19.644 -34.889 1.00108.73 N ANISOU 2613 ND1 HIS A1141 11621 19177 10516 832 739 -610 N ATOM 2614 CD2 HIS A1141 57.488 -21.628 -34.042 1.00111.03 C ANISOU 2614 CD2 HIS A1141 11858 19580 10748 1614 391 -655 C ATOM 2615 CE1 HIS A1141 57.624 -19.470 -33.771 1.00109.79 C ANISOU 2615 CE1 HIS A1141 11432 19636 10649 781 635 -664 C ATOM 2616 NE2 HIS A1141 57.978 -20.636 -33.229 1.00111.62 N ANISOU 2616 NE2 HIS A1141 11608 19959 10844 1258 416 -694 N ATOM 2617 N ASP A1142 54.018 -19.301 -36.221 1.00 92.43 N ANISOU 2617 N ASP A1142 10574 15984 8561 607 780 -375 N ATOM 2618 CA ASP A1142 53.482 -18.003 -35.815 1.00 90.62 C ANISOU 2618 CA ASP A1142 10426 15628 8377 163 841 -316 C ATOM 2619 C ASP A1142 51.983 -18.113 -35.542 1.00 91.79 C ANISOU 2619 C ASP A1142 10963 15299 8612 144 696 -227 C ATOM 2620 O ASP A1142 51.528 -17.585 -34.529 1.00 90.54 O ANISOU 2620 O ASP A1142 10833 15043 8523 -76 616 -181 O ATOM 2621 CB ASP A1142 53.767 -16.920 -36.877 1.00 93.48 C ANISOU 2621 CB ASP A1142 10805 16069 8643 -123 1116 -340 C ATOM 2622 CG ASP A1142 55.215 -16.451 -36.996 1.00108.05 C ANISOU 2622 CG ASP A1142 12237 18421 10397 -286 1314 -452 C ATOM 2623 OD1 ASP A1142 56.120 -17.175 -36.519 1.00110.31 O ANISOU 2623 OD1 ASP A1142 12168 19065 10681 -54 1232 -537 O ATOM 2624 OD2 ASP A1142 55.445 -15.377 -37.603 1.00115.78 O ANISOU 2624 OD2 ASP A1142 13261 19445 11284 -636 1558 -470 O ATOM 2625 N VAL A1143 51.227 -18.832 -36.415 1.00 87.29 N ANISOU 2625 N VAL A1143 10674 14460 8033 372 662 -224 N ATOM 2626 CA VAL A1143 49.784 -19.072 -36.257 1.00 84.40 C ANISOU 2626 CA VAL A1143 10642 13690 7738 370 527 -186 C ATOM 2627 C VAL A1143 49.524 -19.696 -34.881 1.00 89.66 C ANISOU 2627 C VAL A1143 11304 14280 8484 414 337 -163 C ATOM 2628 O VAL A1143 48.635 -19.221 -34.170 1.00 88.51 O ANISOU 2628 O VAL A1143 11276 13943 8412 203 268 -130 O ATOM 2629 CB VAL A1143 49.150 -19.891 -37.423 1.00 86.87 C ANISOU 2629 CB VAL A1143 11214 13787 8006 617 519 -221 C ATOM 2630 CG1 VAL A1143 47.783 -20.453 -37.050 1.00 84.13 C ANISOU 2630 CG1 VAL A1143 11139 13097 7728 637 355 -226 C ATOM 2631 CG2 VAL A1143 49.028 -19.047 -38.674 1.00 86.82 C ANISOU 2631 CG2 VAL A1143 11314 13759 7914 516 685 -228 C ATOM 2632 N ARG A1144 50.326 -20.717 -34.486 1.00 88.10 N ANISOU 2632 N ARG A1144 10983 14237 8253 696 256 -186 N ATOM 2633 CA ARG A1144 50.201 -21.352 -33.169 1.00 87.84 C ANISOU 2633 CA ARG A1144 10993 14129 8254 769 78 -162 C ATOM 2634 C ARG A1144 50.432 -20.290 -32.096 1.00 90.57 C ANISOU 2634 C ARG A1144 11135 14626 8652 455 71 -128 C ATOM 2635 O ARG A1144 49.525 -20.025 -31.313 1.00 86.46 O ANISOU 2635 O ARG A1144 10774 13876 8202 263 -4 -87 O ATOM 2636 CB ARG A1144 51.210 -22.502 -32.994 1.00 91.61 C ANISOU 2636 CB ARG A1144 11374 14794 8640 1176 -3 -198 C ATOM 2637 CG ARG A1144 50.970 -23.712 -33.880 1.00 99.87 C ANISOU 2637 CG ARG A1144 12687 15645 9616 1516 -16 -231 C ATOM 2638 CD ARG A1144 51.895 -24.860 -33.526 1.00108.58 C ANISOU 2638 CD ARG A1144 13761 16889 10605 1956 -122 -263 C ATOM 2639 NE ARG A1144 53.298 -24.604 -33.870 1.00119.01 N ANISOU 2639 NE ARG A1144 14658 18701 11861 2116 -45 -331 N ATOM 2640 CZ ARG A1144 54.299 -24.572 -32.992 1.00137.34 C ANISOU 2640 CZ ARG A1144 16669 21375 14137 2239 -132 -365 C ATOM 2641 NH1 ARG A1144 54.068 -24.778 -31.701 1.00131.98 N ANISOU 2641 NH1 ARG A1144 16099 20583 13466 2236 -305 -317 N ATOM 2642 NH2 ARG A1144 55.538 -24.336 -33.399 1.00123.62 N ANISOU 2642 NH2 ARG A1144 14507 20129 12335 2362 -44 -464 N ATOM 2643 N GLY A1145 51.603 -19.639 -32.158 1.00 90.71 N ANISOU 2643 N GLY A1145 10806 15035 8626 375 172 -162 N ATOM 2644 CA GLY A1145 52.041 -18.574 -31.258 1.00 91.41 C ANISOU 2644 CA GLY A1145 10664 15333 8736 53 194 -154 C ATOM 2645 C GLY A1145 50.991 -17.525 -30.961 1.00 94.10 C ANISOU 2645 C GLY A1145 11204 15402 9148 -314 229 -92 C ATOM 2646 O GLY A1145 50.751 -17.194 -29.795 1.00 94.17 O ANISOU 2646 O GLY A1145 11210 15367 9203 -483 137 -59 O ATOM 2647 N ALA A1146 50.336 -17.026 -32.011 1.00 89.78 N ANISOU 2647 N ALA A1146 10852 14666 8593 -406 351 -83 N ATOM 2648 CA ALA A1146 49.281 -16.026 -31.909 1.00 88.14 C ANISOU 2648 CA ALA A1146 10868 14198 8425 -682 382 -41 C ATOM 2649 C ALA A1146 48.037 -16.564 -31.199 1.00 92.35 C ANISOU 2649 C ALA A1146 11626 14416 9046 -631 213 -20 C ATOM 2650 O ALA A1146 47.398 -15.805 -30.464 1.00 91.58 O ANISOU 2650 O ALA A1146 11606 14194 8994 -864 190 6 O ATOM 2651 CB ALA A1146 48.926 -15.495 -33.286 1.00 88.66 C ANISOU 2651 CB ALA A1146 11112 14151 8424 -704 530 -49 C ATOM 2652 N ILE A1147 47.703 -17.867 -31.387 1.00 89.36 N ANISOU 2652 N ILE A1147 11364 13910 8678 -347 111 -44 N ATOM 2653 CA ILE A1147 46.537 -18.462 -30.714 1.00 87.83 C ANISOU 2653 CA ILE A1147 11395 13429 8549 -343 -20 -51 C ATOM 2654 C ILE A1147 46.888 -18.776 -29.237 1.00 92.29 C ANISOU 2654 C ILE A1147 11890 14041 9134 -377 -133 -18 C ATOM 2655 O ILE A1147 46.022 -18.665 -28.366 1.00 90.99 O ANISOU 2655 O ILE A1147 11858 13689 9025 -536 -197 -11 O ATOM 2656 CB ILE A1147 45.858 -19.661 -31.474 1.00 90.80 C ANISOU 2656 CB ILE A1147 11997 13596 8907 -105 -65 -107 C ATOM 2657 CG1 ILE A1147 46.672 -20.975 -31.411 1.00 93.10 C ANISOU 2657 CG1 ILE A1147 12288 13953 9134 208 -125 -111 C ATOM 2658 CG2 ILE A1147 45.493 -19.318 -32.926 1.00 90.31 C ANISOU 2658 CG2 ILE A1147 12011 13494 8809 -63 30 -146 C ATOM 2659 CD1 ILE A1147 46.104 -21.993 -30.449 1.00 98.82 C ANISOU 2659 CD1 ILE A1147 13241 14446 9858 261 -249 -117 C ATOM 2660 N ALA A 224 48.170 -19.144 -28.979 1.00 90.01 N ANISOU 2660 N ALA A 224 11386 14026 8786 -215 -158 -10 N ATOM 2661 CA ALA A 224 48.742 -19.470 -27.673 1.00 90.18 C ANISOU 2661 CA ALA A 224 11319 14158 8787 -175 -283 12 C ATOM 2662 C ALA A 224 48.710 -18.265 -26.727 1.00 94.50 C ANISOU 2662 C ALA A 224 11747 14778 9379 -528 -270 43 C ATOM 2663 O ALA A 224 48.413 -18.429 -25.538 1.00 93.45 O ANISOU 2663 O ALA A 224 11702 14544 9260 -591 -379 70 O ATOM 2664 CB ALA A 224 50.170 -19.965 -27.844 1.00 93.45 C ANISOU 2664 CB ALA A 224 11470 14927 9108 107 -304 -21 C ATOM 2665 N GLU A 225 48.994 -17.054 -27.258 1.00 91.86 N ANISOU 2665 N GLU A 225 11259 14594 9050 -765 -124 37 N ATOM 2666 CA GLU A 225 48.972 -15.813 -26.484 1.00 91.37 C ANISOU 2666 CA GLU A 225 11126 14580 9009 -1122 -84 61 C ATOM 2667 C GLU A 225 47.582 -15.480 -25.953 1.00 91.86 C ANISOU 2667 C GLU A 225 11459 14299 9145 -1289 -120 90 C ATOM 2668 O GLU A 225 47.458 -15.160 -24.774 1.00 90.79 O ANISOU 2668 O GLU A 225 11325 14142 9030 -1457 -184 113 O ATOM 2669 CB GLU A 225 49.552 -14.647 -27.288 1.00 93.93 C ANISOU 2669 CB GLU A 225 11313 15091 9285 -1344 108 42 C ATOM 2670 CG GLU A 225 51.025 -14.394 -27.004 1.00109.63 C ANISOU 2670 CG GLU A 225 12933 17519 11203 -1414 149 -10 C ATOM 2671 CD GLU A 225 51.384 -13.954 -25.595 1.00135.45 C ANISOU 2671 CD GLU A 225 16063 20928 14474 -1616 58 -9 C ATOM 2672 OE1 GLU A 225 52.444 -14.398 -25.098 1.00137.97 O ANISOU 2672 OE1 GLU A 225 16087 21593 14743 -1488 -28 -65 O ATOM 2673 OE2 GLU A 225 50.617 -13.168 -24.988 1.00124.26 O ANISOU 2673 OE2 GLU A 225 14828 19290 13095 -1880 66 38 O ATOM 2674 N VAL A 226 46.541 -15.604 -26.807 1.00 86.96 N ANISOU 2674 N VAL A 226 11052 13434 8554 -1229 -85 71 N ATOM 2675 CA VAL A 226 45.128 -15.373 -26.459 1.00 85.02 C ANISOU 2675 CA VAL A 226 11031 12904 8371 -1348 -118 55 C ATOM 2676 C VAL A 226 44.700 -16.343 -25.336 1.00 88.41 C ANISOU 2676 C VAL A 226 11561 13199 8832 -1303 -248 51 C ATOM 2677 O VAL A 226 43.943 -15.953 -24.436 1.00 87.67 O ANISOU 2677 O VAL A 226 11558 12972 8780 -1492 -274 48 O ATOM 2678 CB VAL A 226 44.201 -15.484 -27.704 1.00 88.32 C ANISOU 2678 CB VAL A 226 11611 13158 8791 -1237 -76 1 C ATOM 2679 CG1 VAL A 226 42.736 -15.203 -27.354 1.00 86.25 C ANISOU 2679 CG1 VAL A 226 11520 12670 8583 -1346 -115 -56 C ATOM 2680 CG2 VAL A 226 44.671 -14.558 -28.826 1.00 89.08 C ANISOU 2680 CG2 VAL A 226 11673 13357 8818 -1267 61 13 C ATOM 2681 N LYS A 227 45.203 -17.598 -25.395 1.00 84.26 N ANISOU 2681 N LYS A 227 11051 12698 8266 -1048 -318 49 N ATOM 2682 CA LYS A 227 44.936 -18.629 -24.394 1.00 83.24 C ANISOU 2682 CA LYS A 227 11094 12417 8118 -976 -429 52 C ATOM 2683 C LYS A 227 45.625 -18.238 -23.085 1.00 85.26 C ANISOU 2683 C LYS A 227 11234 12811 8349 -1083 -498 105 C ATOM 2684 O LYS A 227 44.958 -18.186 -22.050 1.00 84.55 O ANISOU 2684 O LYS A 227 11290 12558 8278 -1247 -538 111 O ATOM 2685 CB LYS A 227 45.381 -20.027 -24.884 1.00 87.03 C ANISOU 2685 CB LYS A 227 11678 12870 8521 -635 -481 38 C ATOM 2686 CG LYS A 227 44.437 -20.665 -25.909 1.00 91.41 C ANISOU 2686 CG LYS A 227 12438 13206 9087 -562 -435 -33 C ATOM 2687 CD LYS A 227 44.762 -22.132 -26.139 1.00101.05 C ANISOU 2687 CD LYS A 227 13857 14328 10209 -253 -489 -46 C ATOM 2688 CE LYS A 227 43.648 -22.866 -26.847 1.00114.58 C ANISOU 2688 CE LYS A 227 15837 15778 11922 -259 -452 -135 C ATOM 2689 NZ LYS A 227 43.827 -24.345 -26.795 1.00126.59 N ANISOU 2689 NZ LYS A 227 17662 17117 13321 -13 -499 -149 N ATOM 2690 N ARG A 228 46.931 -17.878 -23.152 1.00 80.78 N ANISOU 2690 N ARG A 228 10388 12569 7735 -1020 -501 126 N ATOM 2691 CA ARG A 228 47.753 -17.431 -22.018 1.00 80.38 C ANISOU 2691 CA ARG A 228 10163 12733 7644 -1120 -573 152 C ATOM 2692 C ARG A 228 47.100 -16.242 -21.309 1.00 79.64 C ANISOU 2692 C ARG A 228 10103 12545 7610 -1496 -523 170 C ATOM 2693 O ARG A 228 47.081 -16.203 -20.084 1.00 76.91 O ANISOU 2693 O ARG A 228 9804 12175 7245 -1595 -608 193 O ATOM 2694 CB ARG A 228 49.165 -17.062 -22.500 1.00 82.29 C ANISOU 2694 CB ARG A 228 10043 13393 7831 -1051 -538 123 C ATOM 2695 CG ARG A 228 50.276 -17.548 -21.595 1.00 96.28 C ANISOU 2695 CG ARG A 228 11632 15444 9504 -866 -690 109 C ATOM 2696 CD ARG A 228 51.640 -17.387 -22.242 1.00117.91 C ANISOU 2696 CD ARG A 228 13976 18642 12181 -751 -648 36 C ATOM 2697 NE ARG A 228 51.968 -18.514 -23.121 1.00136.73 N ANISOU 2697 NE ARG A 228 16381 21057 14514 -337 -670 7 N ATOM 2698 CZ ARG A 228 52.044 -18.449 -24.449 1.00152.63 C ANISOU 2698 CZ ARG A 228 18332 23113 16547 -294 -523 -23 C ATOM 2699 NH1 ARG A 228 51.831 -17.299 -25.079 1.00139.51 N ANISOU 2699 NH1 ARG A 228 16604 21464 14941 -634 -342 -25 N ATOM 2700 NH2 ARG A 228 52.345 -19.529 -25.155 1.00140.90 N ANISOU 2700 NH2 ARG A 228 16890 21645 15003 99 -554 -51 N ATOM 2701 N ARG A 229 46.521 -15.306 -22.094 1.00 76.27 N ANISOU 2701 N ARG A 229 9695 12044 7239 -1675 -388 157 N ATOM 2702 CA ARG A 229 45.793 -14.118 -21.631 1.00 75.48 C ANISOU 2702 CA ARG A 229 9675 11825 7181 -1986 -324 165 C ATOM 2703 C ARG A 229 44.720 -14.514 -20.628 1.00 78.50 C ANISOU 2703 C ARG A 229 10274 11950 7602 -2048 -397 159 C ATOM 2704 O ARG A 229 44.745 -14.037 -19.503 1.00 77.29 O ANISOU 2704 O ARG A 229 10128 11799 7441 -2234 -429 181 O ATOM 2705 CB ARG A 229 45.123 -13.400 -22.824 1.00 76.60 C ANISOU 2705 CB ARG A 229 9900 11860 7343 -2033 -196 140 C ATOM 2706 CG ARG A 229 45.749 -12.074 -23.204 1.00 89.44 C ANISOU 2706 CG ARG A 229 11435 13632 8917 -2244 -64 155 C ATOM 2707 CD ARG A 229 45.582 -11.802 -24.691 1.00 99.61 C ANISOU 2707 CD ARG A 229 12790 14884 10173 -2153 51 136 C ATOM 2708 NE ARG A 229 46.255 -10.570 -25.110 1.00107.20 N ANISOU 2708 NE ARG A 229 13722 15963 11046 -2375 208 149 N ATOM 2709 CZ ARG A 229 47.557 -10.461 -25.362 1.00119.99 C ANISOU 2709 CZ ARG A 229 15115 17877 12601 -2444 287 139 C ATOM 2710 NH1 ARG A 229 48.360 -11.510 -25.222 1.00111.00 N ANISOU 2710 NH1 ARG A 229 13736 16964 11477 -2252 199 119 N ATOM 2711 NH2 ARG A 229 48.070 -9.298 -25.736 1.00102.80 N ANISOU 2711 NH2 ARG A 229 12962 15774 10324 -2708 462 135 N ATOM 2712 N ASP A 230 43.808 -15.426 -21.031 1.00 76.16 N ANISOU 2712 N ASP A 230 10158 11444 7335 -1908 -412 115 N ATOM 2713 CA ASP A 230 42.681 -15.918 -20.235 1.00 75.40 C ANISOU 2713 CA ASP A 230 10281 11102 7265 -1992 -444 75 C ATOM 2714 C ASP A 230 43.072 -16.892 -19.109 1.00 80.84 C ANISOU 2714 C ASP A 230 11088 11743 7886 -1924 -550 111 C ATOM 2715 O ASP A 230 42.378 -16.950 -18.090 1.00 79.34 O ANISOU 2715 O ASP A 230 11061 11391 7696 -2087 -560 96 O ATOM 2716 CB ASP A 230 41.618 -16.515 -21.152 1.00 76.45 C ANISOU 2716 CB ASP A 230 10546 11066 7434 -1906 -405 -16 C ATOM 2717 CG ASP A 230 40.767 -15.443 -21.810 1.00 86.00 C ANISOU 2717 CG ASP A 230 11724 12257 8696 -2013 -326 -76 C ATOM 2718 OD1 ASP A 230 39.928 -14.841 -21.104 1.00 85.51 O ANISOU 2718 OD1 ASP A 230 11716 12110 8666 -2199 -308 -120 O ATOM 2719 OD2 ASP A 230 40.932 -15.216 -23.041 1.00 89.92 O ANISOU 2719 OD2 ASP A 230 12161 12820 9183 -1886 -285 -85 O ATOM 2720 N LEU A 231 44.185 -17.627 -19.279 1.00 79.81 N ANISOU 2720 N LEU A 231 10888 11758 7678 -1668 -627 151 N ATOM 2721 CA LEU A 231 44.702 -18.557 -18.281 1.00 81.68 C ANISOU 2721 CA LEU A 231 11263 11964 7807 -1520 -752 188 C ATOM 2722 C LEU A 231 45.138 -17.753 -17.066 1.00 86.44 C ANISOU 2722 C LEU A 231 11765 12693 8387 -1707 -807 230 C ATOM 2723 O LEU A 231 44.684 -18.020 -15.959 1.00 86.53 O ANISOU 2723 O LEU A 231 11998 12527 8354 -1805 -851 242 O ATOM 2724 CB LEU A 231 45.891 -19.331 -18.868 1.00 84.18 C ANISOU 2724 CB LEU A 231 11470 12479 8036 -1155 -828 204 C ATOM 2725 CG LEU A 231 46.622 -20.254 -17.901 1.00 91.97 C ANISOU 2725 CG LEU A 231 12588 13486 8870 -907 -988 239 C ATOM 2726 CD1 LEU A 231 46.278 -21.711 -18.176 1.00 93.53 C ANISOU 2726 CD1 LEU A 231 13157 13408 8971 -639 -1015 228 C ATOM 2727 CD2 LEU A 231 48.125 -20.004 -17.937 1.00 96.47 C ANISOU 2727 CD2 LEU A 231 12795 14484 9376 -707 -1079 241 C ATOM 2728 N TRP A 232 45.993 -16.745 -17.300 1.00 83.72 N ANISOU 2728 N TRP A 232 11103 12646 8059 -1788 -787 240 N ATOM 2729 CA TRP A 232 46.540 -15.811 -16.326 1.00 83.51 C ANISOU 2729 CA TRP A 232 10928 12794 8007 -2001 -822 261 C ATOM 2730 C TRP A 232 45.452 -15.007 -15.647 1.00 85.19 C ANISOU 2730 C TRP A 232 11302 12786 8282 -2325 -750 261 C ATOM 2731 O TRP A 232 45.549 -14.796 -14.446 1.00 85.62 O ANISOU 2731 O TRP A 232 11413 12832 8287 -2452 -817 283 O ATOM 2732 CB TRP A 232 47.540 -14.879 -17.005 1.00 83.13 C ANISOU 2732 CB TRP A 232 10533 13089 7963 -2078 -757 243 C ATOM 2733 CG TRP A 232 48.939 -15.412 -17.018 1.00 87.08 C ANISOU 2733 CG TRP A 232 10777 13945 8366 -1827 -868 220 C ATOM 2734 CD1 TRP A 232 49.602 -15.970 -18.075 1.00 91.26 C ANISOU 2734 CD1 TRP A 232 11148 14654 8872 -1557 -854 187 C ATOM 2735 CD2 TRP A 232 49.858 -15.413 -15.917 1.00 89.32 C ANISOU 2735 CD2 TRP A 232 10911 14481 8546 -1802 -1016 208 C ATOM 2736 NE1 TRP A 232 50.886 -16.305 -17.706 1.00 93.67 N ANISOU 2736 NE1 TRP A 232 11188 15332 9068 -1354 -981 145 N ATOM 2737 CE2 TRP A 232 51.070 -15.976 -16.384 1.00 96.11 C ANISOU 2737 CE2 TRP A 232 11493 15702 9323 -1494 -1094 153 C ATOM 2738 CE3 TRP A 232 49.777 -14.985 -14.576 1.00 90.54 C ANISOU 2738 CE3 TRP A 232 11135 14609 8658 -2000 -1098 227 C ATOM 2739 CZ2 TRP A 232 52.190 -16.129 -15.553 1.00 98.46 C ANISOU 2739 CZ2 TRP A 232 11556 16360 9493 -1359 -1265 103 C ATOM 2740 CZ3 TRP A 232 50.879 -15.149 -13.753 1.00 94.73 C ANISOU 2740 CZ3 TRP A 232 11465 15467 9061 -1881 -1268 192 C ATOM 2741 CH2 TRP A 232 52.071 -15.704 -14.242 1.00 98.29 C ANISOU 2741 CH2 TRP A 232 11614 16302 9428 -1557 -1358 124 C ATOM 2742 N MET A 233 44.409 -14.582 -16.386 1.00 80.15 N ANISOU 2742 N MET A 233 10741 11977 7737 -2431 -625 226 N ATOM 2743 CA MET A 233 43.297 -13.839 -15.803 1.00 79.41 C ANISOU 2743 CA MET A 233 10787 11690 7694 -2691 -556 200 C ATOM 2744 C MET A 233 42.487 -14.699 -14.829 1.00 84.22 C ANISOU 2744 C MET A 233 11656 12062 8281 -2715 -597 180 C ATOM 2745 O MET A 233 42.190 -14.240 -13.723 1.00 85.08 O ANISOU 2745 O MET A 233 11850 12104 8373 -2916 -600 186 O ATOM 2746 CB MET A 233 42.395 -13.219 -16.875 1.00 81.02 C ANISOU 2746 CB MET A 233 11003 11806 7976 -2731 -436 144 C ATOM 2747 CG MET A 233 41.199 -12.451 -16.303 1.00 85.15 C ANISOU 2747 CG MET A 233 11653 12161 8538 -2947 -373 92 C ATOM 2748 SD MET A 233 41.519 -10.707 -15.889 1.00 91.48 S ANISOU 2748 SD MET A 233 12404 13044 9312 -3202 -306 128 S ATOM 2749 CE MET A 233 42.324 -10.847 -14.294 1.00 89.42 C ANISOU 2749 CE MET A 233 12132 12858 8986 -3343 -404 188 C ATOM 2750 N ALA A 234 42.143 -15.940 -15.234 1.00 79.66 N ANISOU 2750 N ALA A 234 11232 11348 7687 -2530 -614 150 N ATOM 2751 CA ALA A 234 41.386 -16.886 -14.417 1.00 78.70 C ANISOU 2751 CA ALA A 234 11415 10975 7513 -2574 -621 118 C ATOM 2752 C ALA A 234 42.122 -17.190 -13.113 1.00 81.94 C ANISOU 2752 C ALA A 234 11941 11394 7800 -2555 -736 194 C ATOM 2753 O ALA A 234 41.499 -17.142 -12.053 1.00 81.23 O ANISOU 2753 O ALA A 234 12045 11140 7677 -2753 -712 180 O ATOM 2754 CB ALA A 234 41.130 -18.167 -15.197 1.00 80.01 C ANISOU 2754 CB ALA A 234 11742 11009 7649 -2371 -614 76 C ATOM 2755 N CYS A 235 43.449 -17.437 -13.187 1.00 79.19 N ANISOU 2755 N CYS A 235 11453 11262 7373 -2315 -861 259 N ATOM 2756 CA CYS A 235 44.302 -17.716 -12.032 1.00 81.45 C ANISOU 2756 CA CYS A 235 11807 11623 7516 -2225 -1011 318 C ATOM 2757 C CYS A 235 44.348 -16.545 -11.060 1.00 85.70 C ANISOU 2757 C CYS A 235 12240 12253 8069 -2513 -1011 333 C ATOM 2758 O CYS A 235 44.218 -16.759 -9.850 1.00 85.95 O ANISOU 2758 O CYS A 235 12496 12160 8002 -2586 -1071 356 O ATOM 2759 CB CYS A 235 45.702 -18.125 -12.475 1.00 84.22 C ANISOU 2759 CB CYS A 235 11945 12268 7785 -1882 -1146 345 C ATOM 2760 SG CYS A 235 45.756 -19.671 -13.412 1.00 89.58 S ANISOU 2760 SG CYS A 235 12835 12807 8394 -1483 -1170 335 S ATOM 2761 N THR A 236 44.516 -15.309 -11.602 1.00 81.21 N ANISOU 2761 N THR A 236 11377 11875 7605 -2684 -934 318 N ATOM 2762 CA THR A 236 44.578 -14.044 -10.864 1.00 80.00 C ANISOU 2762 CA THR A 236 11126 11808 7465 -2980 -907 324 C ATOM 2763 C THR A 236 43.308 -13.807 -10.059 1.00 82.25 C ANISOU 2763 C THR A 236 11671 11803 7777 -3220 -822 300 C ATOM 2764 O THR A 236 43.409 -13.645 -8.838 1.00 83.34 O ANISOU 2764 O THR A 236 11922 11910 7834 -3345 -880 323 O ATOM 2765 CB THR A 236 44.933 -12.902 -11.810 1.00 84.37 C ANISOU 2765 CB THR A 236 11402 12560 8095 -3097 -809 307 C ATOM 2766 OG1 THR A 236 46.292 -13.074 -12.203 1.00 83.03 O ANISOU 2766 OG1 THR A 236 10962 12720 7865 -2929 -894 312 O ATOM 2767 CG2 THR A 236 44.749 -11.529 -11.180 1.00 83.11 C ANISOU 2767 CG2 THR A 236 11228 12406 7945 -3433 -739 303 C ATOM 2768 N VAL A 237 42.120 -13.836 -10.719 1.00 75.47 N ANISOU 2768 N VAL A 237 10901 10757 7019 -3273 -691 237 N ATOM 2769 CA VAL A 237 40.821 -13.643 -10.051 1.00 74.20 C ANISOU 2769 CA VAL A 237 10943 10364 6887 -3493 -590 173 C ATOM 2770 C VAL A 237 40.592 -14.685 -8.931 1.00 80.25 C ANISOU 2770 C VAL A 237 12017 10936 7538 -3503 -635 182 C ATOM 2771 O VAL A 237 39.956 -14.371 -7.908 1.00 79.83 O ANISOU 2771 O VAL A 237 12121 10753 7458 -3726 -582 155 O ATOM 2772 CB VAL A 237 39.641 -13.556 -11.041 1.00 76.41 C ANISOU 2772 CB VAL A 237 11208 10545 7277 -3507 -461 69 C ATOM 2773 CG1 VAL A 237 38.325 -13.301 -10.311 1.00 75.39 C ANISOU 2773 CG1 VAL A 237 11229 10246 7171 -3734 -355 -33 C ATOM 2774 CG2 VAL A 237 39.888 -12.458 -12.073 1.00 75.41 C ANISOU 2774 CG2 VAL A 237 10856 10575 7222 -3485 -420 72 C ATOM 2775 N LEU A 238 41.173 -15.892 -9.093 1.00 78.13 N ANISOU 2775 N LEU A 238 11865 10641 7178 -3253 -731 222 N ATOM 2776 CA LEU A 238 41.095 -16.921 -8.058 1.00 78.99 C ANISOU 2776 CA LEU A 238 12344 10539 7129 -3224 -781 245 C ATOM 2777 C LEU A 238 42.076 -16.620 -6.930 1.00 83.38 C ANISOU 2777 C LEU A 238 12907 11217 7556 -3201 -934 328 C ATOM 2778 O LEU A 238 41.673 -16.649 -5.773 1.00 82.80 O ANISOU 2778 O LEU A 238 13091 10977 7392 -3369 -920 331 O ATOM 2779 CB LEU A 238 41.330 -18.331 -8.616 1.00 79.92 C ANISOU 2779 CB LEU A 238 12664 10545 7158 -2937 -829 254 C ATOM 2780 CG LEU A 238 40.225 -18.952 -9.456 1.00 82.76 C ANISOU 2780 CG LEU A 238 13149 10711 7587 -2997 -677 151 C ATOM 2781 CD1 LEU A 238 40.565 -20.377 -9.770 1.00 84.60 C ANISOU 2781 CD1 LEU A 238 13676 10789 7679 -2726 -731 173 C ATOM 2782 CD2 LEU A 238 38.861 -18.878 -8.769 1.00 83.39 C ANISOU 2782 CD2 LEU A 238 13436 10569 7680 -3349 -511 46 C ATOM 2783 N ALA A 239 43.346 -16.299 -7.263 1.00 81.05 N ANISOU 2783 N ALA A 239 12314 11235 7246 -3013 -1072 377 N ATOM 2784 CA ALA A 239 44.379 -15.970 -6.279 1.00 83.06 C ANISOU 2784 CA ALA A 239 12497 11689 7373 -2980 -1239 425 C ATOM 2785 C ALA A 239 43.973 -14.764 -5.425 1.00 87.57 C ANISOU 2785 C ALA A 239 13042 12250 7980 -3344 -1171 414 C ATOM 2786 O ALA A 239 44.216 -14.771 -4.214 1.00 89.74 O ANISOU 2786 O ALA A 239 13485 12495 8118 -3397 -1267 442 O ATOM 2787 CB ALA A 239 45.707 -15.714 -6.962 1.00 84.92 C ANISOU 2787 CB ALA A 239 12333 12323 7612 -2775 -1356 430 C ATOM 2788 N VAL A 240 43.298 -13.766 -6.031 1.00 81.12 N ANISOU 2788 N VAL A 240 12065 11431 7327 -3574 -1008 369 N ATOM 2789 CA VAL A 240 42.789 -12.614 -5.288 1.00 79.47 C ANISOU 2789 CA VAL A 240 11876 11173 7145 -3900 -922 349 C ATOM 2790 C VAL A 240 41.691 -13.103 -4.360 1.00 82.03 C ANISOU 2790 C VAL A 240 12562 11183 7420 -4032 -846 322 C ATOM 2791 O VAL A 240 41.822 -12.907 -3.170 1.00 83.83 O ANISOU 2791 O VAL A 240 12941 11370 7539 -4157 -897 346 O ATOM 2792 CB VAL A 240 42.349 -11.433 -6.191 1.00 82.15 C ANISOU 2792 CB VAL A 240 12013 11567 7635 -4056 -773 305 C ATOM 2793 CG1 VAL A 240 41.657 -10.335 -5.384 1.00 80.94 C ANISOU 2793 CG1 VAL A 240 11958 11305 7489 -4357 -674 274 C ATOM 2794 CG2 VAL A 240 43.545 -10.861 -6.946 1.00 82.95 C ANISOU 2794 CG2 VAL A 240 11794 11977 7744 -3997 -824 327 C ATOM 2795 N PHE A 241 40.690 -13.833 -4.867 1.00 77.25 N ANISOU 2795 N PHE A 241 12107 10373 6872 -4007 -729 263 N ATOM 2796 CA PHE A 241 39.597 -14.357 -4.045 1.00 77.28 C ANISOU 2796 CA PHE A 241 12450 10092 6819 -4179 -617 205 C ATOM 2797 C PHE A 241 40.043 -15.244 -2.869 1.00 82.72 C ANISOU 2797 C PHE A 241 13494 10642 7294 -4117 -728 272 C ATOM 2798 O PHE A 241 39.602 -15.004 -1.749 1.00 82.92 O ANISOU 2798 O PHE A 241 13733 10535 7240 -4333 -678 260 O ATOM 2799 CB PHE A 241 38.548 -15.076 -4.902 1.00 78.53 C ANISOU 2799 CB PHE A 241 12675 10103 7059 -4172 -475 102 C ATOM 2800 CG PHE A 241 37.305 -14.244 -5.097 1.00 78.68 C ANISOU 2800 CG PHE A 241 12584 10102 7211 -4403 -297 -30 C ATOM 2801 CD1 PHE A 241 36.175 -14.460 -4.313 1.00 81.11 C ANISOU 2801 CD1 PHE A 241 13113 10224 7482 -4646 -147 -141 C ATOM 2802 CD2 PHE A 241 37.272 -13.221 -6.045 1.00 79.92 C ANISOU 2802 CD2 PHE A 241 12428 10432 7505 -4365 -276 -54 C ATOM 2803 CE1 PHE A 241 35.029 -13.674 -4.474 1.00 81.08 C ANISOU 2803 CE1 PHE A 241 12969 10251 7588 -4818 6 -290 C ATOM 2804 CE2 PHE A 241 36.125 -12.432 -6.204 1.00 81.79 C ANISOU 2804 CE2 PHE A 241 12582 10658 7835 -4514 -136 -185 C ATOM 2805 CZ PHE A 241 35.017 -12.654 -5.406 1.00 79.98 C ANISOU 2805 CZ PHE A 241 12525 10286 7578 -4725 -4 -309 C ATOM 2806 N ILE A 242 40.938 -16.216 -3.110 1.00 80.18 N ANISOU 2806 N ILE A 242 13249 10354 6860 -3804 -882 340 N ATOM 2807 CA ILE A 242 41.439 -17.153 -2.096 1.00 82.27 C ANISOU 2807 CA ILE A 242 13902 10478 6881 -3653 -1016 408 C ATOM 2808 C ILE A 242 42.286 -16.469 -1.019 1.00 88.22 C ANISOU 2808 C ILE A 242 14597 11400 7521 -3674 -1179 467 C ATOM 2809 O ILE A 242 42.255 -16.907 0.131 1.00 89.26 O ANISOU 2809 O ILE A 242 15112 11349 7456 -3697 -1228 499 O ATOM 2810 CB ILE A 242 42.193 -18.343 -2.766 1.00 86.71 C ANISOU 2810 CB ILE A 242 14552 11051 7342 -3242 -1150 452 C ATOM 2811 CG1 ILE A 242 41.235 -19.213 -3.616 1.00 86.45 C ANISOU 2811 CG1 ILE A 242 14712 10769 7366 -3264 -975 384 C ATOM 2812 CG2 ILE A 242 42.983 -19.210 -1.756 1.00 89.97 C ANISOU 2812 CG2 ILE A 242 15346 11375 7462 -2976 -1350 531 C ATOM 2813 CD1 ILE A 242 41.912 -19.901 -4.847 1.00 92.31 C ANISOU 2813 CD1 ILE A 242 15318 11627 8127 -2896 -1062 403 C ATOM 2814 N ILE A 243 43.041 -15.419 -1.373 1.00 85.51 N ANISOU 2814 N ILE A 243 13812 11398 7280 -3685 -1255 472 N ATOM 2815 CA ILE A 243 43.926 -14.774 -0.396 1.00 87.70 C ANISOU 2815 CA ILE A 243 14002 11880 7440 -3721 -1420 505 C ATOM 2816 C ILE A 243 43.282 -13.508 0.258 1.00 92.72 C ANISOU 2816 C ILE A 243 14608 12473 8149 -4128 -1286 472 C ATOM 2817 O ILE A 243 43.445 -13.305 1.472 1.00 92.92 O ANISOU 2817 O ILE A 243 14818 12462 8027 -4232 -1361 492 O ATOM 2818 CB ILE A 243 45.346 -14.519 -1.006 1.00 91.51 C ANISOU 2818 CB ILE A 243 14049 12798 7924 -3487 -1605 511 C ATOM 2819 CG1 ILE A 243 45.924 -15.855 -1.570 1.00 93.15 C ANISOU 2819 CG1 ILE A 243 14336 13025 8032 -3038 -1739 535 C ATOM 2820 CG2 ILE A 243 46.318 -13.896 0.034 1.00 93.35 C ANISOU 2820 CG2 ILE A 243 14162 13296 8012 -3535 -1793 512 C ATOM 2821 CD1 ILE A 243 47.075 -15.763 -2.524 1.00 98.65 C ANISOU 2821 CD1 ILE A 243 14579 14131 8772 -2792 -1853 511 C ATOM 2822 N CYS A 244 42.513 -12.716 -0.512 1.00 88.99 N ANISOU 2822 N CYS A 244 13950 11983 7879 -4327 -1092 417 N ATOM 2823 CA CYS A 244 41.909 -11.484 -0.007 1.00 89.20 C ANISOU 2823 CA CYS A 244 13958 11969 7967 -4660 -963 377 C ATOM 2824 C CYS A 244 40.565 -11.655 0.667 1.00 92.40 C ANISOU 2824 C CYS A 244 14687 12058 8363 -4863 -788 322 C ATOM 2825 O CYS A 244 40.465 -11.399 1.869 1.00 93.28 O ANISOU 2825 O CYS A 244 15009 12077 8354 -5027 -796 331 O ATOM 2826 CB CYS A 244 41.828 -10.422 -1.099 1.00 88.98 C ANISOU 2826 CB CYS A 244 13605 12087 8115 -4743 -858 339 C ATOM 2827 SG CYS A 244 43.418 -9.675 -1.515 1.00 94.69 S ANISOU 2827 SG CYS A 244 13948 13213 8816 -4704 -1004 371 S ATOM 2828 N PHE A 245 39.521 -11.993 -0.114 1.00 87.12 N ANISOU 2828 N PHE A 245 14029 11254 7820 -4874 -620 246 N ATOM 2829 CA PHE A 245 38.139 -12.047 0.352 1.00 86.67 C ANISOU 2829 CA PHE A 245 14187 10964 7780 -5098 -416 143 C ATOM 2830 C PHE A 245 37.746 -13.289 1.157 1.00 90.12 C ANISOU 2830 C PHE A 245 15046 11143 8052 -5127 -382 137 C ATOM 2831 O PHE A 245 37.126 -13.140 2.211 1.00 89.80 O ANISOU 2831 O PHE A 245 15247 10948 7925 -5357 -280 96 O ATOM 2832 CB PHE A 245 37.170 -11.857 -0.820 1.00 87.60 C ANISOU 2832 CB PHE A 245 14109 11094 8082 -5103 -258 28 C ATOM 2833 CG PHE A 245 37.492 -10.692 -1.726 1.00 89.01 C ANISOU 2833 CG PHE A 245 13951 11477 8393 -5052 -274 35 C ATOM 2834 CD1 PHE A 245 37.222 -9.387 -1.332 1.00 92.28 C ANISOU 2834 CD1 PHE A 245 14313 11919 8829 -5225 -207 5 C ATOM 2835 CD2 PHE A 245 38.041 -10.901 -2.985 1.00 91.52 C ANISOU 2835 CD2 PHE A 245 14048 11934 8790 -4833 -340 68 C ATOM 2836 CE1 PHE A 245 37.510 -8.310 -2.179 1.00 92.55 C ANISOU 2836 CE1 PHE A 245 14122 12095 8948 -5187 -203 13 C ATOM 2837 CE2 PHE A 245 38.331 -9.825 -3.825 1.00 93.70 C ANISOU 2837 CE2 PHE A 245 14075 12370 9158 -4809 -332 73 C ATOM 2838 CZ PHE A 245 38.064 -8.537 -3.417 1.00 91.45 C ANISOU 2838 CZ PHE A 245 13782 12086 8877 -4989 -261 48 C ATOM 2839 N VAL A 246 38.054 -14.495 0.650 1.00 86.33 N ANISOU 2839 N VAL A 246 14690 10595 7515 -4908 -445 170 N ATOM 2840 CA VAL A 246 37.683 -15.775 1.272 1.00 86.78 C ANISOU 2840 CA VAL A 246 15226 10360 7386 -4927 -392 164 C ATOM 2841 C VAL A 246 38.125 -15.879 2.758 1.00 90.33 C ANISOU 2841 C VAL A 246 16037 10687 7596 -4975 -487 244 C ATOM 2842 O VAL A 246 37.251 -16.181 3.584 1.00 91.24 O ANISOU 2842 O VAL A 246 16508 10552 7607 -5227 -316 180 O ATOM 2843 CB VAL A 246 38.138 -17.000 0.420 1.00 90.61 C ANISOU 2843 CB VAL A 246 15810 10794 7822 -4626 -475 203 C ATOM 2844 CG1 VAL A 246 38.172 -18.295 1.233 1.00 92.69 C ANISOU 2844 CG1 VAL A 246 16663 10743 7810 -4572 -488 245 C ATOM 2845 CG2 VAL A 246 37.253 -17.156 -0.814 1.00 88.75 C ANISOU 2845 CG2 VAL A 246 15382 10564 7774 -4681 -308 80 C ATOM 2846 N PRO A 247 39.410 -15.635 3.144 1.00 84.90 N ANISOU 2846 N PRO A 247 15272 10180 6806 -4762 -743 361 N ATOM 2847 CA PRO A 247 39.789 -15.816 4.558 1.00 86.32 C ANISOU 2847 CA PRO A 247 15831 10238 6731 -4783 -849 425 C ATOM 2848 C PRO A 247 38.934 -15.048 5.560 1.00 88.89 C ANISOU 2848 C PRO A 247 16286 10440 7047 -5165 -676 364 C ATOM 2849 O PRO A 247 38.521 -15.632 6.550 1.00 90.99 O ANISOU 2849 O PRO A 247 17029 10434 7109 -5283 -606 364 O ATOM 2850 CB PRO A 247 41.258 -15.404 4.588 1.00 88.89 C ANISOU 2850 CB PRO A 247 15875 10894 7004 -4518 -1147 511 C ATOM 2851 CG PRO A 247 41.738 -15.688 3.203 1.00 92.16 C ANISOU 2851 CG PRO A 247 15953 11503 7562 -4256 -1207 514 C ATOM 2852 CD PRO A 247 40.593 -15.286 2.331 1.00 85.08 C ANISOU 2852 CD PRO A 247 14878 10539 6910 -4488 -948 421 C ATOM 2853 N HIS A 248 38.598 -13.790 5.271 1.00 82.29 N ANISOU 2853 N HIS A 248 15074 9777 6416 -5356 -585 303 N ATOM 2854 CA HIS A 248 37.753 -12.988 6.146 1.00 81.41 C ANISOU 2854 CA HIS A 248 15061 9567 6304 -5692 -411 230 C ATOM 2855 C HIS A 248 36.326 -13.524 6.275 1.00 85.79 C ANISOU 2855 C HIS A 248 15863 9867 6868 -5931 -122 97 C ATOM 2856 O HIS A 248 35.791 -13.565 7.379 1.00 87.25 O ANISOU 2856 O HIS A 248 16380 9863 6909 -6160 -2 60 O ATOM 2857 CB HIS A 248 37.737 -11.530 5.683 1.00 80.15 C ANISOU 2857 CB HIS A 248 14473 9638 6341 -5791 -384 192 C ATOM 2858 CG HIS A 248 37.314 -10.586 6.760 1.00 83.49 C ANISOU 2858 CG HIS A 248 15010 10002 6710 -6065 -291 153 C ATOM 2859 ND1 HIS A 248 38.161 -10.266 7.810 1.00 86.44 N ANISOU 2859 ND1 HIS A 248 15521 10414 6907 -6091 -458 236 N ATOM 2860 CD2 HIS A 248 36.145 -9.924 6.921 1.00 84.28 C ANISOU 2860 CD2 HIS A 248 15099 10024 6898 -6301 -56 26 C ATOM 2861 CE1 HIS A 248 37.480 -9.427 8.574 1.00 85.80 C ANISOU 2861 CE1 HIS A 248 15535 10249 6815 -6357 -309 170 C ATOM 2862 NE2 HIS A 248 36.262 -9.191 8.082 1.00 84.90 N ANISOU 2862 NE2 HIS A 248 15335 10066 6857 -6480 -63 42 N ATOM 2863 N HIS A 249 35.726 -13.955 5.155 1.00 81.61 N ANISOU 2863 N HIS A 249 15171 9347 6491 -5891 -6 11 N ATOM 2864 CA HIS A 249 34.352 -14.447 5.089 1.00 81.69 C ANISOU 2864 CA HIS A 249 15322 9189 6529 -6135 277 -161 C ATOM 2865 C HIS A 249 34.189 -15.829 5.728 1.00 87.67 C ANISOU 2865 C HIS A 249 16639 9632 7041 -6200 346 -152 C ATOM 2866 O HIS A 249 33.065 -16.233 6.012 1.00 88.54 O ANISOU 2866 O HIS A 249 16951 9577 7112 -6495 610 -307 O ATOM 2867 CB HIS A 249 33.815 -14.378 3.641 1.00 81.05 C ANISOU 2867 CB HIS A 249 14851 9262 6681 -6062 353 -272 C ATOM 2868 CG HIS A 249 33.461 -12.973 3.238 1.00 82.87 C ANISOU 2868 CG HIS A 249 14664 9716 7108 -6100 391 -343 C ATOM 2869 ND1 HIS A 249 34.436 -12.071 2.793 1.00 83.46 N ANISOU 2869 ND1 HIS A 249 14458 9991 7264 -5910 202 -223 N ATOM 2870 CD2 HIS A 249 32.279 -12.318 3.335 1.00 84.09 C ANISOU 2870 CD2 HIS A 249 14690 9909 7351 -6307 597 -526 C ATOM 2871 CE1 HIS A 249 33.806 -10.921 2.605 1.00 81.53 C ANISOU 2871 CE1 HIS A 249 13980 9854 7144 -6002 302 -321 C ATOM 2872 NE2 HIS A 249 32.509 -11.016 2.922 1.00 82.36 N ANISOU 2872 NE2 HIS A 249 14154 9879 7260 -6210 527 -504 N ATOM 2873 N VAL A 250 35.303 -16.526 6.005 1.00 85.13 N ANISOU 2873 N VAL A 250 16588 9228 6528 -5932 118 16 N ATOM 2874 CA VAL A 250 35.300 -17.819 6.702 1.00 87.27 C ANISOU 2874 CA VAL A 250 17498 9156 6506 -5939 153 54 C ATOM 2875 C VAL A 250 35.235 -17.487 8.207 1.00 91.93 C ANISOU 2875 C VAL A 250 18436 9602 6890 -6141 181 81 C ATOM 2876 O VAL A 250 34.379 -18.007 8.923 1.00 93.26 O ANISOU 2876 O VAL A 250 19045 9491 6899 -6439 419 -5 O ATOM 2877 CB VAL A 250 36.552 -18.665 6.320 1.00 91.83 C ANISOU 2877 CB VAL A 250 18218 9729 6945 -5486 -132 214 C ATOM 2878 CG1 VAL A 250 36.775 -19.825 7.283 1.00 94.83 C ANISOU 2878 CG1 VAL A 250 19339 9740 6950 -5421 -160 289 C ATOM 2879 CG2 VAL A 250 36.462 -19.167 4.884 1.00 90.28 C ANISOU 2879 CG2 VAL A 250 17778 9607 6915 -5327 -110 170 C ATOM 2880 N VAL A 251 36.110 -16.554 8.639 1.00 87.16 N ANISOU 2880 N VAL A 251 17608 9210 6297 -6010 -44 184 N ATOM 2881 CA VAL A 251 36.301 -16.018 9.997 1.00 87.45 C ANISOU 2881 CA VAL A 251 17882 9188 6157 -6142 -90 229 C ATOM 2882 C VAL A 251 35.073 -15.267 10.554 1.00 89.25 C ANISOU 2882 C VAL A 251 18093 9356 6462 -6574 213 78 C ATOM 2883 O VAL A 251 34.846 -15.326 11.761 1.00 90.57 O ANISOU 2883 O VAL A 251 18678 9323 6413 -6763 288 80 O ATOM 2884 CB VAL A 251 37.586 -15.121 10.031 1.00 90.22 C ANISOU 2884 CB VAL A 251 17869 9862 6546 -5901 -410 343 C ATOM 2885 CG1 VAL A 251 37.737 -14.372 11.350 1.00 90.92 C ANISOU 2885 CG1 VAL A 251 18120 9936 6488 -6075 -451 365 C ATOM 2886 CG2 VAL A 251 38.843 -15.938 9.744 1.00 91.52 C ANISOU 2886 CG2 VAL A 251 18109 10101 6564 -5459 -720 471 C ATOM 2887 N GLN A 252 34.317 -14.546 9.697 1.00 82.86 N ANISOU 2887 N GLN A 252 16812 8731 5941 -6699 373 -57 N ATOM 2888 CA GLN A 252 33.184 -13.692 10.078 1.00 81.57 C ANISOU 2888 CA GLN A 252 16528 8590 5876 -7035 635 -223 C ATOM 2889 C GLN A 252 32.121 -14.356 10.955 1.00 87.07 C ANISOU 2889 C GLN A 252 17682 9007 6394 -7384 935 -355 C ATOM 2890 O GLN A 252 31.936 -13.882 12.084 1.00 86.89 O ANISOU 2890 O GLN A 252 17874 8899 6240 -7580 1007 -366 O ATOM 2891 CB GLN A 252 32.527 -13.029 8.862 1.00 80.53 C ANISOU 2891 CB GLN A 252 15853 8695 6049 -7028 738 -361 C ATOM 2892 CG GLN A 252 31.670 -11.804 9.218 1.00 93.89 C ANISOU 2892 CG GLN A 252 17334 10493 7846 -7246 914 -506 C ATOM 2893 CD GLN A 252 32.397 -10.710 9.987 1.00111.70 C ANISOU 2893 CD GLN A 252 19580 12813 10050 -7228 763 -392 C ATOM 2894 OE1 GLN A 252 33.611 -10.475 9.843 1.00104.77 O ANISOU 2894 OE1 GLN A 252 18619 12035 9155 -7015 495 -224 O ATOM 2895 NE2 GLN A 252 31.652 -9.998 10.814 1.00105.90 N ANISOU 2895 NE2 GLN A 252 18915 12042 9282 -7467 943 -504 N ATOM 2896 N LEU A 253 31.415 -15.419 10.455 1.00 84.37 N ANISOU 2896 N LEU A 253 17496 8527 6035 -7494 1128 -470 N ATOM 2897 CA LEU A 253 30.360 -16.132 11.224 1.00 85.59 C ANISOU 2897 CA LEU A 253 18100 8417 6001 -7891 1461 -628 C ATOM 2898 C LEU A 253 30.839 -16.621 12.616 1.00 90.67 C ANISOU 2898 C LEU A 253 19420 8742 6288 -7953 1421 -493 C ATOM 2899 O LEU A 253 30.190 -16.249 13.599 1.00 91.84 O ANISOU 2899 O LEU A 253 19752 8807 6337 -8267 1629 -591 O ATOM 2900 CB LEU A 253 29.708 -17.270 10.426 1.00 86.45 C ANISOU 2900 CB LEU A 253 18311 8421 6115 -8001 1649 -762 C ATOM 2901 CG LEU A 253 28.897 -16.892 9.183 1.00 88.39 C ANISOU 2901 CG LEU A 253 17950 8964 6671 -8028 1760 -964 C ATOM 2902 CD1 LEU A 253 28.500 -18.125 8.424 1.00 89.06 C ANISOU 2902 CD1 LEU A 253 18193 8926 6719 -8097 1883 -1060 C ATOM 2903 CD2 LEU A 253 27.646 -16.106 9.551 1.00 90.58 C ANISOU 2903 CD2 LEU A 253 17969 9401 7047 -8370 2048 -1227 C ATOM 2904 N PRO A 254 31.986 -17.352 12.765 1.00 87.35 N ANISOU 2904 N PRO A 254 19362 8166 5662 -7631 1145 -277 N ATOM 2905 CA PRO A 254 32.455 -17.707 14.121 1.00 89.56 C ANISOU 2905 CA PRO A 254 20286 8164 5580 -7644 1075 -153 C ATOM 2906 C PRO A 254 32.711 -16.486 15.007 1.00 94.18 C ANISOU 2906 C PRO A 254 20714 8895 6174 -7696 981 -114 C ATOM 2907 O PRO A 254 32.299 -16.507 16.174 1.00 95.65 O ANISOU 2907 O PRO A 254 21342 8864 6136 -7962 1141 -147 O ATOM 2908 CB PRO A 254 33.765 -18.457 13.863 1.00 92.03 C ANISOU 2908 CB PRO A 254 20813 8421 5735 -7163 715 59 C ATOM 2909 CG PRO A 254 33.682 -18.934 12.467 1.00 95.24 C ANISOU 2909 CG PRO A 254 20907 8932 6349 -7018 722 15 C ATOM 2910 CD PRO A 254 32.898 -17.896 11.733 1.00 87.89 C ANISOU 2910 CD PRO A 254 19289 8316 5792 -7217 880 -148 C ATOM 2911 N TRP A 255 33.362 -15.414 14.440 1.00 88.60 N ANISOU 2911 N TRP A 255 19404 8544 5716 -7471 745 -56 N ATOM 2912 CA TRP A 255 33.694 -14.156 15.126 1.00 87.62 C ANISOU 2912 CA TRP A 255 19084 8586 5621 -7512 639 -23 C ATOM 2913 C TRP A 255 32.465 -13.400 15.605 1.00 86.71 C ANISOU 2913 C TRP A 255 18896 8463 5587 -7910 972 -210 C ATOM 2914 O TRP A 255 32.479 -12.913 16.719 1.00 87.19 O ANISOU 2914 O TRP A 255 19198 8440 5488 -8059 992 -194 O ATOM 2915 CB TRP A 255 34.581 -13.248 14.257 1.00 85.47 C ANISOU 2915 CB TRP A 255 18207 8678 5591 -7236 368 53 C ATOM 2916 CG TRP A 255 35.079 -12.023 14.975 1.00 87.29 C ANISOU 2916 CG TRP A 255 18300 9059 5807 -7280 236 96 C ATOM 2917 CD1 TRP A 255 36.251 -11.898 15.663 1.00 91.94 C ANISOU 2917 CD1 TRP A 255 19027 9704 6201 -7105 -68 235 C ATOM 2918 CD2 TRP A 255 34.386 -10.775 15.132 1.00 86.03 C ANISOU 2918 CD2 TRP A 255 17880 9005 5804 -7521 410 -19 C ATOM 2919 NE1 TRP A 255 36.329 -10.653 16.246 1.00 91.28 N ANISOU 2919 NE1 TRP A 255 18793 9744 6146 -7266 -81 214 N ATOM 2920 CE2 TRP A 255 35.194 -9.946 15.943 1.00 90.88 C ANISOU 2920 CE2 TRP A 255 18523 9704 6303 -7514 214 67 C ATOM 2921 CE3 TRP A 255 33.150 -10.279 14.679 1.00 85.99 C ANISOU 2921 CE3 TRP A 255 17626 9042 6006 -7725 708 -201 C ATOM 2922 CZ2 TRP A 255 34.811 -8.649 16.303 1.00 89.20 C ANISOU 2922 CZ2 TRP A 255 18144 9575 6175 -7713 320 -8 C ATOM 2923 CZ3 TRP A 255 32.769 -9.001 15.050 1.00 86.67 C ANISOU 2923 CZ3 TRP A 255 17541 9221 6167 -7878 799 -278 C ATOM 2924 CH2 TRP A 255 33.591 -8.202 15.852 1.00 87.72 C ANISOU 2924 CH2 TRP A 255 17753 9396 6181 -7878 615 -175 C ATOM 2925 N THR A 256 31.430 -13.256 14.766 1.00 80.59 N ANISOU 2925 N THR A 256 17768 7800 5051 -8058 1219 -396 N ATOM 2926 CA THR A 256 30.176 -12.589 15.143 1.00 80.17 C ANISOU 2926 CA THR A 256 17598 7787 5076 -8401 1547 -617 C ATOM 2927 C THR A 256 29.515 -13.317 16.335 1.00 89.05 C ANISOU 2927 C THR A 256 19332 8596 5907 -8751 1817 -696 C ATOM 2928 O THR A 256 29.065 -12.644 17.256 1.00 90.48 O ANISOU 2928 O THR A 256 19604 8757 6017 -8974 1963 -773 O ATOM 2929 CB THR A 256 29.204 -12.535 13.952 1.00 79.39 C ANISOU 2929 CB THR A 256 17028 7885 5249 -8448 1737 -825 C ATOM 2930 OG1 THR A 256 29.867 -12.021 12.799 1.00 73.62 O ANISOU 2930 OG1 THR A 256 15823 7399 4752 -8115 1490 -734 O ATOM 2931 CG2 THR A 256 27.939 -11.728 14.252 1.00 74.90 C ANISOU 2931 CG2 THR A 256 16242 7442 4775 -8727 2042 -1080 C ATOM 2932 N LEU A 257 29.460 -14.676 16.315 1.00 87.75 N ANISOU 2932 N LEU A 257 19616 8172 5554 -8807 1897 -682 N ATOM 2933 CA LEU A 257 28.869 -15.476 17.397 1.00 91.75 C ANISOU 2933 CA LEU A 257 20789 8331 5740 -9160 2174 -752 C ATOM 2934 C LEU A 257 29.606 -15.279 18.713 1.00 98.30 C ANISOU 2934 C LEU A 257 22103 8970 6278 -9113 2012 -576 C ATOM 2935 O LEU A 257 28.964 -15.003 19.725 1.00 98.44 O ANISOU 2935 O LEU A 257 22382 8870 6151 -9439 2253 -678 O ATOM 2936 CB LEU A 257 28.802 -16.970 17.041 1.00 93.79 C ANISOU 2936 CB LEU A 257 21497 8314 5825 -9191 2262 -747 C ATOM 2937 CG LEU A 257 27.820 -17.339 15.950 1.00 97.26 C ANISOU 2937 CG LEU A 257 21584 8889 6480 -9376 2516 -980 C ATOM 2938 CD1 LEU A 257 28.230 -18.607 15.285 1.00 98.77 C ANISOU 2938 CD1 LEU A 257 22084 8878 6566 -9216 2437 -894 C ATOM 2939 CD2 LEU A 257 26.412 -17.435 16.484 1.00 99.46 C ANISOU 2939 CD2 LEU A 257 21981 9118 6692 -9926 2990 -1279 C ATOM 2940 N ALA A 258 30.958 -15.376 18.675 1.00 96.35 N ANISOU 2940 N ALA A 258 21932 8729 5948 -8696 1598 -330 N ATOM 2941 CA ALA A 258 31.876 -15.172 19.802 1.00 98.05 C ANISOU 2941 CA ALA A 258 22535 8831 5887 -8556 1348 -153 C ATOM 2942 C ALA A 258 31.628 -13.809 20.444 1.00100.67 C ANISOU 2942 C ALA A 258 22601 9336 6314 -8732 1398 -216 C ATOM 2943 O ALA A 258 31.453 -13.742 21.664 1.00103.34 O ANISOU 2943 O ALA A 258 23401 9472 6392 -8934 1495 -216 O ATOM 2944 CB ALA A 258 33.322 -15.271 19.326 1.00 98.16 C ANISOU 2944 CB ALA A 258 22400 8996 5902 -8052 883 58 C ATOM 2945 N GLU A 259 31.552 -12.744 19.606 1.00 93.22 N ANISOU 2945 N GLU A 259 20956 8740 5724 -8664 1355 -279 N ATOM 2946 CA GLU A 259 31.267 -11.361 19.989 1.00 91.56 C ANISOU 2946 CA GLU A 259 20441 8709 5640 -8798 1411 -354 C ATOM 2947 C GLU A 259 29.915 -11.264 20.692 1.00 96.96 C ANISOU 2947 C GLU A 259 21316 9263 6261 -9219 1839 -570 C ATOM 2948 O GLU A 259 29.804 -10.592 21.716 1.00 97.26 O ANISOU 2948 O GLU A 259 21535 9248 6170 -9378 1898 -586 O ATOM 2949 CB GLU A 259 31.297 -10.437 18.762 1.00 89.54 C ANISOU 2949 CB GLU A 259 19471 8796 5754 -8634 1331 -399 C ATOM 2950 CG GLU A 259 32.182 -9.211 18.947 1.00100.27 C ANISOU 2950 CG GLU A 259 20586 10348 7166 -8497 1072 -295 C ATOM 2951 CD GLU A 259 31.789 -8.205 20.018 1.00125.84 C ANISOU 2951 CD GLU A 259 23950 13548 10314 -8735 1202 -365 C ATOM 2952 OE1 GLU A 259 30.580 -7.913 20.171 1.00122.89 O ANISOU 2952 OE1 GLU A 259 23537 13149 10006 -8975 1536 -559 O ATOM 2953 OE2 GLU A 259 32.707 -7.684 20.690 1.00123.52 O ANISOU 2953 OE2 GLU A 259 23775 13275 9882 -8676 967 -241 O ATOM 2954 N LEU A 260 28.906 -11.992 20.176 1.00 94.77 N ANISOU 2954 N LEU A 260 21018 8941 6051 -9413 2142 -748 N ATOM 2955 CA LEU A 260 27.557 -12.054 20.750 1.00 96.28 C ANISOU 2955 CA LEU A 260 21352 9052 6179 -9844 2587 -1002 C ATOM 2956 C LEU A 260 27.493 -12.902 22.048 1.00103.96 C ANISOU 2956 C LEU A 260 23128 9630 6741 -10108 2743 -965 C ATOM 2957 O LEU A 260 26.472 -12.898 22.747 1.00103.36 O ANISOU 2957 O LEU A 260 23245 9469 6557 -10503 3120 -1167 O ATOM 2958 CB LEU A 260 26.539 -12.544 19.693 1.00 95.44 C ANISOU 2958 CB LEU A 260 20899 9084 6278 -9975 2846 -1235 C ATOM 2959 CG LEU A 260 26.138 -11.560 18.579 1.00 96.15 C ANISOU 2959 CG LEU A 260 20218 9569 6744 -9813 2822 -1370 C ATOM 2960 CD1 LEU A 260 25.229 -12.228 17.581 1.00 95.67 C ANISOU 2960 CD1 LEU A 260 19882 9634 6835 -9929 3043 -1596 C ATOM 2961 CD2 LEU A 260 25.470 -10.282 19.138 1.00 97.99 C ANISOU 2961 CD2 LEU A 260 20221 9967 7044 -9937 2980 -1529 C ATOM 2962 N GLY A 261 28.595 -13.598 22.341 1.00104.05 N ANISOU 2962 N GLY A 261 23599 9421 6516 -9867 2447 -717 N ATOM 2963 CA GLY A 261 28.777 -14.429 23.522 1.00109.11 C ANISOU 2963 CA GLY A 261 25076 9657 6723 -10005 2505 -629 C ATOM 2964 C GLY A 261 28.175 -15.810 23.425 1.00120.40 C ANISOU 2964 C GLY A 261 27005 10782 7959 -10242 2791 -715 C ATOM 2965 O GLY A 261 27.509 -16.255 24.370 1.00123.95 O ANISOU 2965 O GLY A 261 28027 10946 8124 -10628 3119 -815 O ATOM 2966 N PHE A 262 28.446 -16.504 22.303 1.00118.16 N ANISOU 2966 N PHE A 262 26553 10540 7804 -10021 2672 -673 N ATOM 2967 CA PHE A 262 27.960 -17.854 21.996 1.00122.11 C ANISOU 2967 CA PHE A 262 27502 10756 8139 -10214 2916 -750 C ATOM 2968 C PHE A 262 29.088 -18.906 22.018 1.00128.88 C ANISOU 2968 C PHE A 262 28960 11307 8703 -9829 2600 -490 C ATOM 2969 O PHE A 262 28.826 -20.072 21.684 1.00130.95 O ANISOU 2969 O PHE A 262 29653 11297 8805 -9928 2761 -524 O ATOM 2970 CB PHE A 262 27.297 -17.879 20.602 1.00122.75 C ANISOU 2970 CB PHE A 262 26922 11126 8591 -10263 3048 -938 C ATOM 2971 CG PHE A 262 25.920 -17.277 20.432 1.00124.97 C ANISOU 2971 CG PHE A 262 26715 11670 9100 -10684 3448 -1271 C ATOM 2972 CD1 PHE A 262 25.725 -15.904 20.538 1.00126.29 C ANISOU 2972 CD1 PHE A 262 26318 12166 9502 -10643 3409 -1339 C ATOM 2973 CD2 PHE A 262 24.847 -18.064 20.031 1.00129.69 C ANISOU 2973 CD2 PHE A 262 27358 12227 9690 -11083 3841 -1534 C ATOM 2974 CE1 PHE A 262 24.463 -15.339 20.327 1.00127.35 C ANISOU 2974 CE1 PHE A 262 25973 12577 9838 -10956 3752 -1662 C ATOM 2975 CE2 PHE A 262 23.592 -17.493 19.793 1.00132.71 C ANISOU 2975 CE2 PHE A 262 27200 12932 10292 -11424 4181 -1875 C ATOM 2976 CZ PHE A 262 23.408 -16.135 19.951 1.00128.91 C ANISOU 2976 CZ PHE A 262 26178 12775 10027 -11331 4126 -1936 C ATOM 2977 N GLN A 263 30.339 -18.505 22.373 1.00125.46 N ANISOU 2977 N GLN A 263 28545 10935 8190 -9379 2148 -249 N ATOM 2978 CA GLN A 263 31.489 -19.424 22.382 1.00127.72 C ANISOU 2978 CA GLN A 263 29331 11002 8195 -8921 1794 -15 C ATOM 2979 C GLN A 263 32.395 -19.321 23.638 1.00134.94 C ANISOU 2979 C GLN A 263 30782 11753 8737 -8692 1506 172 C ATOM 2980 O GLN A 263 32.065 -18.612 24.598 1.00135.65 O ANISOU 2980 O GLN A 263 30950 11837 8754 -8951 1623 124 O ATOM 2981 CB GLN A 263 32.321 -19.258 21.092 1.00126.24 C ANISOU 2981 CB GLN A 263 28484 11161 8321 -8451 1438 78 C ATOM 2982 CG GLN A 263 31.563 -19.485 19.769 1.00145.48 C ANISOU 2982 CG GLN A 263 30439 13746 11090 -8594 1662 -85 C ATOM 2983 CD GLN A 263 31.337 -20.937 19.389 1.00167.55 C ANISOU 2983 CD GLN A 263 33803 16185 13672 -8627 1813 -98 C ATOM 2984 OE1 GLN A 263 30.798 -21.749 20.155 1.00160.60 O ANISOU 2984 OE1 GLN A 263 33512 14953 12555 -8815 2066 -135 O ATOM 2985 NE2 GLN A 263 31.672 -21.272 18.149 1.00158.96 N ANISOU 2985 NE2 GLN A 263 32348 15254 12795 -8349 1670 -76 N ATOM 2986 N ASP A 264 33.531 -20.062 23.628 1.00133.79 N ANISOU 2986 N ASP A 264 31018 11481 8336 -8186 1125 374 N ATOM 2987 CA ASP A 264 34.518 -20.091 24.713 1.00135.97 C ANISOU 2987 CA ASP A 264 31799 11636 8228 -7865 780 549 C ATOM 2988 C ASP A 264 35.372 -18.807 24.768 1.00137.96 C ANISOU 2988 C ASP A 264 31347 12368 8703 -7621 406 608 C ATOM 2989 O ASP A 264 35.329 -17.982 23.846 1.00135.13 O ANISOU 2989 O ASP A 264 30146 12413 8787 -7630 381 542 O ATOM 2990 CB ASP A 264 35.419 -21.330 24.576 1.00140.44 C ANISOU 2990 CB ASP A 264 32962 11949 8447 -7352 489 715 C ATOM 2991 N SER A 265 36.151 -18.652 25.855 1.00136.41 N ANISOU 2991 N SER A 265 31535 12121 8175 -7411 120 723 N ATOM 2992 CA SER A 265 37.055 -17.521 26.090 1.00134.48 C ANISOU 2992 CA SER A 265 30749 12299 8047 -7201 -251 772 C ATOM 2993 C SER A 265 38.333 -17.665 25.239 1.00137.88 C ANISOU 2993 C SER A 265 30736 13078 8573 -6620 -722 873 C ATOM 2994 O SER A 265 38.753 -16.697 24.589 1.00134.67 O ANISOU 2994 O SER A 265 29520 13129 8518 -6561 -880 843 O ATOM 2995 CB SER A 265 37.404 -17.432 27.574 1.00142.06 C ANISOU 2995 CB SER A 265 32336 13068 8574 -7189 -385 839 C ATOM 2996 OG SER A 265 38.254 -16.330 27.844 1.00153.35 O ANISOU 2996 OG SER A 265 33257 14911 10098 -7037 -729 863 O ATOM 2997 N LYS A 266 38.928 -18.888 25.237 1.00137.47 N ANISOU 2997 N LYS A 266 31248 12797 8187 -6194 -928 982 N ATOM 2998 CA LYS A 266 40.132 -19.257 24.480 1.00137.15 C ANISOU 2998 CA LYS A 266 30902 13047 8163 -5588 -1365 1067 C ATOM 2999 C LYS A 266 39.901 -19.078 22.984 1.00136.04 C ANISOU 2999 C LYS A 266 30014 13172 8501 -5626 -1251 1002 C ATOM 3000 O LYS A 266 40.773 -18.553 22.286 1.00134.00 O ANISOU 3000 O LYS A 266 29062 13380 8474 -5336 -1550 1013 O ATOM 3001 CB LYS A 266 40.543 -20.707 24.785 1.00144.13 C ANISOU 3001 CB LYS A 266 32673 13529 8562 -5163 -1513 1177 C ATOM 3002 N PHE A 267 38.710 -19.493 22.504 1.00129.99 N ANISOU 3002 N PHE A 267 29388 12127 7876 -6007 -808 918 N ATOM 3003 CA PHE A 267 38.301 -19.364 21.110 1.00125.75 C ANISOU 3003 CA PHE A 267 28205 11798 7775 -6092 -653 837 C ATOM 3004 C PHE A 267 38.089 -17.893 20.749 1.00124.46 C ANISOU 3004 C PHE A 267 27189 12059 8042 -6348 -599 745 C ATOM 3005 O PHE A 267 38.499 -17.482 19.658 1.00120.52 O ANISOU 3005 O PHE A 267 26006 11921 7867 -6174 -731 736 O ATOM 3006 CB PHE A 267 37.035 -20.200 20.817 1.00127.81 C ANISOU 3006 CB PHE A 267 28877 11659 8028 -6469 -188 739 C ATOM 3007 CG PHE A 267 36.411 -19.938 19.464 1.00125.45 C ANISOU 3007 CG PHE A 267 27892 11587 8186 -6637 15 618 C ATOM 3008 CD1 PHE A 267 36.950 -20.497 18.310 1.00127.62 C ANISOU 3008 CD1 PHE A 267 27920 11985 8584 -6269 -157 664 C ATOM 3009 CD2 PHE A 267 35.300 -19.112 19.340 1.00124.70 C ANISOU 3009 CD2 PHE A 267 27394 11602 8386 -7131 363 451 C ATOM 3010 CE1 PHE A 267 36.388 -20.233 17.058 1.00125.08 C ANISOU 3010 CE1 PHE A 267 26976 11879 8670 -6412 16 552 C ATOM 3011 CE2 PHE A 267 34.737 -18.852 18.086 1.00124.28 C ANISOU 3011 CE2 PHE A 267 26712 11778 8732 -7241 520 332 C ATOM 3012 CZ PHE A 267 35.284 -19.415 16.956 1.00121.57 C ANISOU 3012 CZ PHE A 267 26149 11539 8502 -6890 345 387 C ATOM 3013 N HIS A 268 37.450 -17.103 21.657 1.00120.42 N ANISOU 3013 N HIS A 268 26753 11487 7513 -6753 -396 676 N ATOM 3014 CA HIS A 268 37.194 -15.679 21.403 1.00116.79 C ANISOU 3014 CA HIS A 268 25581 11376 7416 -6995 -327 586 C ATOM 3015 C HIS A 268 38.487 -14.933 21.030 1.00117.36 C ANISOU 3015 C HIS A 268 25077 11901 7614 -6648 -750 659 C ATOM 3016 O HIS A 268 38.510 -14.261 20.001 1.00112.78 O ANISOU 3016 O HIS A 268 23827 11630 7396 -6655 -744 610 O ATOM 3017 CB HIS A 268 36.439 -14.998 22.566 1.00118.37 C ANISOU 3017 CB HIS A 268 26038 11426 7511 -7419 -85 511 C ATOM 3018 CG HIS A 268 35.821 -13.667 22.212 1.00118.65 C ANISOU 3018 CG HIS A 268 25441 11725 7915 -7715 103 383 C ATOM 3019 ND1 HIS A 268 35.025 -12.982 23.117 1.00120.82 N ANISOU 3019 ND1 HIS A 268 25872 11893 8143 -8100 364 285 N ATOM 3020 CD2 HIS A 268 35.893 -12.940 21.068 1.00117.11 C ANISOU 3020 CD2 HIS A 268 24519 11871 8104 -7652 65 338 C ATOM 3021 CE1 HIS A 268 34.646 -11.872 22.500 1.00117.11 C ANISOU 3021 CE1 HIS A 268 24777 11697 8021 -8229 464 185 C ATOM 3022 NE2 HIS A 268 35.152 -11.798 21.270 1.00115.26 N ANISOU 3022 NE2 HIS A 268 24017 11729 8049 -7972 289 217 N ATOM 3023 N GLN A 269 39.569 -15.130 21.825 1.00115.75 N ANISOU 3023 N GLN A 269 25153 11738 7087 -6335 -1117 763 N ATOM 3024 CA GLN A 269 40.905 -14.558 21.612 1.00114.35 C ANISOU 3024 CA GLN A 269 24480 12016 6953 -6002 -1542 808 C ATOM 3025 C GLN A 269 41.487 -14.960 20.242 1.00115.27 C ANISOU 3025 C GLN A 269 24125 12388 7284 -5658 -1694 826 C ATOM 3026 O GLN A 269 42.031 -14.102 19.547 1.00112.90 O ANISOU 3026 O GLN A 269 23142 12503 7253 -5628 -1817 793 O ATOM 3027 CB GLN A 269 41.850 -14.962 22.768 1.00119.49 C ANISOU 3027 CB GLN A 269 25621 12630 7151 -5694 -1899 892 C ATOM 3028 CG GLN A 269 43.324 -14.535 22.623 1.00128.72 C ANISOU 3028 CG GLN A 269 26297 14313 8297 -5310 -2374 907 C ATOM 3029 CD GLN A 269 43.570 -13.056 22.812 1.00144.62 C ANISOU 3029 CD GLN A 269 27758 16686 10503 -5596 -2414 832 C ATOM 3030 OE1 GLN A 269 43.195 -12.456 23.825 1.00141.35 O ANISOU 3030 OE1 GLN A 269 27591 16142 9974 -5903 -2313 808 O ATOM 3031 NE2 GLN A 269 44.267 -12.446 21.865 1.00134.53 N ANISOU 3031 NE2 GLN A 269 25756 15866 9493 -5498 -2567 789 N ATOM 3032 N ALA A 270 41.350 -16.247 19.855 1.00111.80 N ANISOU 3032 N ALA A 270 24082 11684 6712 -5422 -1663 874 N ATOM 3033 CA ALA A 270 41.871 -16.793 18.595 1.00110.13 C ANISOU 3033 CA ALA A 270 23523 11661 6659 -5068 -1796 894 C ATOM 3034 C ALA A 270 41.177 -16.223 17.360 1.00107.07 C ANISOU 3034 C ALA A 270 22533 11421 6729 -5327 -1530 809 C ATOM 3035 O ALA A 270 41.856 -15.754 16.442 1.00103.81 O ANISOU 3035 O ALA A 270 21493 11399 6552 -5151 -1695 800 O ATOM 3036 CB ALA A 270 41.776 -18.312 18.602 1.00113.84 C ANISOU 3036 CB ALA A 270 24685 11735 6834 -4794 -1787 961 C ATOM 3037 N ILE A 271 39.825 -16.257 17.350 1.00101.31 N ANISOU 3037 N ILE A 271 21993 10393 6106 -5745 -1119 731 N ATOM 3038 CA ILE A 271 39.002 -15.756 16.254 1.00 96.88 C ANISOU 3038 CA ILE A 271 20921 9946 5944 -5989 -851 627 C ATOM 3039 C ILE A 271 39.114 -14.220 16.141 1.00 97.81 C ANISOU 3039 C ILE A 271 20427 10412 6324 -6171 -871 575 C ATOM 3040 O ILE A 271 39.012 -13.699 15.032 1.00 95.92 O ANISOU 3040 O ILE A 271 19642 10402 6401 -6180 -817 527 O ATOM 3041 CB ILE A 271 37.535 -16.292 16.313 1.00 99.69 C ANISOU 3041 CB ILE A 271 21646 9930 6304 -6369 -418 521 C ATOM 3042 CG1 ILE A 271 36.904 -16.390 14.910 1.00 97.59 C ANISOU 3042 CG1 ILE A 271 20946 9762 6371 -6425 -229 426 C ATOM 3043 CG2 ILE A 271 36.630 -15.533 17.289 1.00100.22 C ANISOU 3043 CG2 ILE A 271 21852 9881 6348 -6816 -156 428 C ATOM 3044 CD1 ILE A 271 37.325 -17.629 14.113 1.00107.46 C ANISOU 3044 CD1 ILE A 271 22367 10914 7548 -6091 -336 487 C ATOM 3045 N ASN A 272 39.380 -13.511 17.258 1.00 93.90 N ANISOU 3045 N ASN A 272 20055 9947 5674 -6297 -958 589 N ATOM 3046 CA ASN A 272 39.570 -12.059 17.249 1.00 91.44 C ANISOU 3046 CA ASN A 272 19254 9932 5557 -6473 -986 544 C ATOM 3047 C ASN A 272 40.916 -11.737 16.604 1.00 95.17 C ANISOU 3047 C ASN A 272 19238 10820 6102 -6166 -1331 593 C ATOM 3048 O ASN A 272 40.971 -10.855 15.753 1.00 91.90 O ANISOU 3048 O ASN A 272 18293 10658 5965 -6248 -1291 546 O ATOM 3049 CB ASN A 272 39.497 -11.471 18.663 1.00 90.90 C ANISOU 3049 CB ASN A 272 19510 9758 5271 -6701 -979 538 C ATOM 3050 CG ASN A 272 39.212 -9.990 18.699 1.00 98.46 C ANISOU 3050 CG ASN A 272 20095 10888 6429 -6996 -866 460 C ATOM 3051 OD1 ASN A 272 38.065 -9.549 18.566 1.00 86.41 O ANISOU 3051 OD1 ASN A 272 18527 9238 5067 -7278 -539 362 O ATOM 3052 ND2 ASN A 272 40.246 -9.189 18.911 1.00 89.89 N ANISOU 3052 ND2 ASN A 272 18751 10095 5309 -6938 -1130 486 N ATOM 3053 N ASP A 273 41.985 -12.485 16.978 1.00 95.30 N ANISOU 3053 N ASP A 273 19446 10911 5853 -5800 -1662 673 N ATOM 3054 CA ASP A 273 43.344 -12.329 16.445 1.00 96.29 C ANISOU 3054 CA ASP A 273 19111 11475 6000 -5474 -2008 692 C ATOM 3055 C ASP A 273 43.410 -12.574 14.928 1.00 99.14 C ANISOU 3055 C ASP A 273 19035 11994 6640 -5313 -1963 681 C ATOM 3056 O ASP A 273 43.965 -11.748 14.204 1.00 98.37 O ANISOU 3056 O ASP A 273 18370 12257 6749 -5337 -2029 641 O ATOM 3057 CB ASP A 273 44.353 -13.219 17.203 1.00102.31 C ANISOU 3057 CB ASP A 273 20222 12269 6380 -5059 -2368 758 C ATOM 3058 CG ASP A 273 44.703 -12.776 18.622 1.00119.84 C ANISOU 3058 CG ASP A 273 22724 14494 8314 -5149 -2528 759 C ATOM 3059 OD1 ASP A 273 44.034 -11.853 19.146 1.00120.27 O ANISOU 3059 OD1 ASP A 273 22803 14449 8446 -5572 -2318 717 O ATOM 3060 OD2 ASP A 273 45.614 -13.384 19.227 1.00130.43 O ANISOU 3060 OD2 ASP A 273 24294 15930 9335 -4774 -2866 796 O ATOM 3061 N ALA A 274 42.812 -13.677 14.449 1.00 95.25 N ANISOU 3061 N ALA A 274 18831 11218 6143 -5185 -1829 707 N ATOM 3062 CA ALA A 274 42.779 -14.024 13.029 1.00 93.07 C ANISOU 3062 CA ALA A 274 18210 11045 6109 -5030 -1771 695 C ATOM 3063 C ALA A 274 41.964 -13.000 12.236 1.00 93.54 C ANISOU 3063 C ALA A 274 17844 11174 6523 -5371 -1497 615 C ATOM 3064 O ALA A 274 42.258 -12.757 11.064 1.00 91.31 O ANISOU 3064 O ALA A 274 17098 11130 6466 -5270 -1514 597 O ATOM 3065 CB ALA A 274 42.194 -15.413 12.848 1.00 94.77 C ANISOU 3065 CB ALA A 274 18921 10883 6204 -4890 -1652 726 C ATOM 3066 N HIS A 275 40.953 -12.391 12.888 1.00 89.22 N ANISOU 3066 N HIS A 275 17471 10423 6003 -5753 -1248 560 N ATOM 3067 CA HIS A 275 40.086 -11.371 12.305 1.00 86.30 C ANISOU 3067 CA HIS A 275 16772 10097 5922 -6050 -990 469 C ATOM 3068 C HIS A 275 40.894 -10.111 11.982 1.00 90.20 C ANISOU 3068 C HIS A 275 16779 10950 6544 -6082 -1126 463 C ATOM 3069 O HIS A 275 40.595 -9.417 11.006 1.00 87.60 O ANISOU 3069 O HIS A 275 16081 10741 6463 -6158 -1002 414 O ATOM 3070 CB HIS A 275 38.952 -11.035 13.271 1.00 87.19 C ANISOU 3070 CB HIS A 275 17217 9937 5975 -6405 -728 401 C ATOM 3071 CG HIS A 275 37.939 -10.117 12.688 1.00 88.22 C ANISOU 3071 CG HIS A 275 17055 10093 6370 -6649 -458 287 C ATOM 3072 ND1 HIS A 275 37.983 -8.757 12.925 1.00 89.03 N ANISOU 3072 ND1 HIS A 275 16945 10334 6549 -6827 -439 253 N ATOM 3073 CD2 HIS A 275 36.917 -10.388 11.844 1.00 88.71 C ANISOU 3073 CD2 HIS A 275 17009 10079 6617 -6707 -222 192 C ATOM 3074 CE1 HIS A 275 36.970 -8.248 12.250 1.00 86.68 C ANISOU 3074 CE1 HIS A 275 16445 10021 6467 -6952 -196 145 C ATOM 3075 NE2 HIS A 275 36.293 -9.196 11.592 1.00 86.80 N ANISOU 3075 NE2 HIS A 275 16491 9930 6559 -6886 -65 96 N ATOM 3076 N GLN A 276 41.927 -9.821 12.796 1.00 88.66 N ANISOU 3076 N GLN A 276 16601 10930 6156 -6029 -1379 503 N ATOM 3077 CA GLN A 276 42.801 -8.672 12.559 1.00 87.65 C ANISOU 3077 CA GLN A 276 16036 11160 6106 -6103 -1509 478 C ATOM 3078 C GLN A 276 43.650 -8.909 11.301 1.00 92.91 C ANISOU 3078 C GLN A 276 16261 12137 6905 -5840 -1648 487 C ATOM 3079 O GLN A 276 43.832 -7.987 10.507 1.00 92.19 O ANISOU 3079 O GLN A 276 15778 12252 6996 -5963 -1589 446 O ATOM 3080 CB GLN A 276 43.683 -8.362 13.785 1.00 90.58 C ANISOU 3080 CB GLN A 276 16530 11670 6216 -6132 -1750 488 C ATOM 3081 CG GLN A 276 42.941 -8.119 15.106 1.00 80.22 C ANISOU 3081 CG GLN A 276 15684 10057 4738 -6386 -1628 482 C ATOM 3082 CD GLN A 276 41.659 -7.298 15.059 1.00 91.71 C ANISOU 3082 CD GLN A 276 17184 11292 6369 -6731 -1279 420 C ATOM 3083 OE1 GLN A 276 41.571 -6.216 14.463 1.00 80.70 O ANISOU 3083 OE1 GLN A 276 15465 10030 5166 -6895 -1176 369 O ATOM 3084 NE2 GLN A 276 40.651 -7.758 15.780 1.00 92.75 N ANISOU 3084 NE2 GLN A 276 17754 11081 6404 -6852 -1088 409 N ATOM 3085 N VAL A 277 44.106 -10.161 11.098 1.00 90.57 N ANISOU 3085 N VAL A 277 16071 11842 6499 -5476 -1812 537 N ATOM 3086 CA VAL A 277 44.918 -10.593 9.955 1.00 90.16 C ANISOU 3086 CA VAL A 277 15648 12070 6538 -5169 -1951 543 C ATOM 3087 C VAL A 277 44.080 -10.619 8.660 1.00 90.34 C ANISOU 3087 C VAL A 277 15505 11981 6840 -5213 -1702 526 C ATOM 3088 O VAL A 277 44.511 -10.082 7.634 1.00 88.61 O ANISOU 3088 O VAL A 277 14851 12021 6795 -5204 -1697 497 O ATOM 3089 CB VAL A 277 45.602 -11.961 10.259 1.00 96.84 C ANISOU 3089 CB VAL A 277 16750 12910 7135 -4727 -2207 599 C ATOM 3090 CG1 VAL A 277 46.282 -12.555 9.019 1.00 96.77 C ANISOU 3090 CG1 VAL A 277 16406 13138 7222 -4377 -2313 599 C ATOM 3091 CG2 VAL A 277 46.593 -11.838 11.415 1.00 99.69 C ANISOU 3091 CG2 VAL A 277 17181 13481 7214 -4626 -2507 595 C ATOM 3092 N THR A 278 42.892 -11.243 8.718 1.00 85.82 N ANISOU 3092 N THR A 278 15285 11033 6289 -5275 -1491 528 N ATOM 3093 CA THR A 278 41.992 -11.384 7.576 1.00 82.79 C ANISOU 3093 CA THR A 278 14781 10537 6140 -5310 -1263 489 C ATOM 3094 C THR A 278 41.412 -10.030 7.155 1.00 85.08 C ANISOU 3094 C THR A 278 14790 10893 6645 -5601 -1071 420 C ATOM 3095 O THR A 278 41.245 -9.812 5.954 1.00 84.00 O ANISOU 3095 O THR A 278 14361 10850 6706 -5552 -989 392 O ATOM 3096 CB THR A 278 40.932 -12.482 7.811 1.00 87.99 C ANISOU 3096 CB THR A 278 15891 10812 6729 -5327 -1092 477 C ATOM 3097 OG1 THR A 278 40.033 -12.122 8.856 1.00 87.10 O ANISOU 3097 OG1 THR A 278 16081 10468 6544 -5642 -916 433 O ATOM 3098 CG2 THR A 278 41.546 -13.855 8.084 1.00 87.46 C ANISOU 3098 CG2 THR A 278 16167 10642 6423 -4996 -1277 552 C ATOM 3099 N LEU A 279 41.179 -9.102 8.109 1.00 82.42 N ANISOU 3099 N LEU A 279 14557 10510 6248 -5873 -1016 395 N ATOM 3100 CA LEU A 279 40.670 -7.757 7.799 1.00 80.96 C ANISOU 3100 CA LEU A 279 14177 10363 6223 -6121 -845 331 C ATOM 3101 C LEU A 279 41.677 -6.919 7.007 1.00 88.90 C ANISOU 3101 C LEU A 279 14780 11688 7311 -6097 -951 340 C ATOM 3102 O LEU A 279 41.262 -6.191 6.108 1.00 87.30 O ANISOU 3102 O LEU A 279 14387 11505 7277 -6164 -804 299 O ATOM 3103 CB LEU A 279 40.193 -6.994 9.056 1.00 80.63 C ANISOU 3103 CB LEU A 279 14388 10176 6070 -6407 -755 299 C ATOM 3104 CG LEU A 279 39.531 -5.615 8.849 1.00 81.89 C ANISOU 3104 CG LEU A 279 14441 10315 6358 -6639 -559 223 C ATOM 3105 CD1 LEU A 279 38.315 -5.682 7.928 1.00 79.25 C ANISOU 3105 CD1 LEU A 279 14035 9863 6215 -6607 -331 141 C ATOM 3106 CD2 LEU A 279 39.133 -5.019 10.154 1.00 83.53 C ANISOU 3106 CD2 LEU A 279 14934 10375 6428 -6885 -487 194 C ATOM 3107 N CYS A 280 42.983 -7.022 7.315 1.00 90.02 N ANISOU 3107 N CYS A 280 14796 12089 7319 -6001 -1198 377 N ATOM 3108 CA CYS A 280 43.961 -6.246 6.570 1.00 91.65 C ANISOU 3108 CA CYS A 280 14607 12627 7587 -6030 -1271 357 C ATOM 3109 C CYS A 280 44.376 -6.929 5.263 1.00 93.82 C ANISOU 3109 C CYS A 280 14607 13060 7979 -5751 -1315 372 C ATOM 3110 O CYS A 280 44.889 -6.251 4.372 1.00 93.78 O ANISOU 3110 O CYS A 280 14288 13272 8070 -5805 -1286 344 O ATOM 3111 CB CYS A 280 45.155 -5.834 7.427 1.00 96.24 C ANISOU 3111 CB CYS A 280 15097 13486 7982 -6115 -1489 342 C ATOM 3112 SG CYS A 280 46.115 -7.211 8.095 1.00103.97 S ANISOU 3112 SG CYS A 280 16149 14621 8733 -5743 -1819 381 S ATOM 3113 N LEU A 281 44.051 -8.232 5.096 1.00 89.26 N ANISOU 3113 N LEU A 281 14188 12335 7390 -5479 -1348 410 N ATOM 3114 CA LEU A 281 44.272 -8.992 3.848 1.00 86.89 C ANISOU 3114 CA LEU A 281 13692 12125 7198 -5198 -1368 422 C ATOM 3115 C LEU A 281 43.153 -8.643 2.867 1.00 87.80 C ANISOU 3115 C LEU A 281 13770 12063 7526 -5293 -1117 388 C ATOM 3116 O LEU A 281 43.402 -8.514 1.673 1.00 85.92 O ANISOU 3116 O LEU A 281 13262 11970 7415 -5196 -1087 379 O ATOM 3117 CB LEU A 281 44.279 -10.502 4.137 1.00 87.69 C ANISOU 3117 CB LEU A 281 14066 12083 7168 -4892 -1486 470 C ATOM 3118 CG LEU A 281 45.499 -11.330 3.687 1.00 93.61 C ANISOU 3118 CG LEU A 281 14626 13110 7831 -4510 -1725 493 C ATOM 3119 CD1 LEU A 281 46.818 -10.758 4.195 1.00 95.92 C ANISOU 3119 CD1 LEU A 281 14644 13805 7995 -4505 -1951 463 C ATOM 3120 CD2 LEU A 281 45.385 -12.753 4.186 1.00 97.00 C ANISOU 3120 CD2 LEU A 281 15468 13309 8077 -4218 -1828 544 C ATOM 3121 N LEU A 282 41.920 -8.454 3.386 1.00 85.10 N ANISOU 3121 N LEU A 282 13692 11432 7209 -5478 -937 355 N ATOM 3122 CA LEU A 282 40.721 -8.054 2.628 1.00 83.80 C ANISOU 3122 CA LEU A 282 13502 11117 7221 -5563 -707 289 C ATOM 3123 C LEU A 282 40.841 -6.608 2.148 1.00 87.43 C ANISOU 3123 C LEU A 282 13761 11695 7762 -5725 -630 261 C ATOM 3124 O LEU A 282 40.193 -6.239 1.176 1.00 86.18 O ANISOU 3124 O LEU A 282 13505 11499 7741 -5699 -494 215 O ATOM 3125 CB LEU A 282 39.465 -8.216 3.510 1.00 84.12 C ANISOU 3125 CB LEU A 282 13862 10873 7226 -5727 -549 231 C ATOM 3126 CG LEU A 282 38.126 -7.718 2.954 1.00 87.54 C ANISOU 3126 CG LEU A 282 14263 11188 7810 -5825 -316 119 C ATOM 3127 CD1 LEU A 282 37.358 -8.834 2.316 1.00 87.38 C ANISOU 3127 CD1 LEU A 282 14278 11061 7860 -5704 -230 61 C ATOM 3128 CD2 LEU A 282 37.290 -7.101 4.044 1.00 91.36 C ANISOU 3128 CD2 LEU A 282 14965 11517 8231 -6069 -181 53 C ATOM 3129 N SER A 283 41.667 -5.796 2.836 1.00 85.76 N ANISOU 3129 N SER A 283 13521 11620 7443 -5892 -716 281 N ATOM 3130 CA SER A 283 41.943 -4.389 2.523 1.00 85.43 C ANISOU 3130 CA SER A 283 13362 11672 7423 -6095 -641 256 C ATOM 3131 C SER A 283 42.896 -4.253 1.350 1.00 90.56 C ANISOU 3131 C SER A 283 13700 12579 8128 -6004 -692 268 C ATOM 3132 O SER A 283 42.936 -3.189 0.745 1.00 91.28 O ANISOU 3132 O SER A 283 13731 12697 8255 -6145 -578 244 O ATOM 3133 CB SER A 283 42.549 -3.684 3.728 1.00 90.22 C ANISOU 3133 CB SER A 283 14065 12343 7871 -6339 -717 256 C ATOM 3134 OG SER A 283 41.725 -3.824 4.873 1.00 96.77 O ANISOU 3134 OG SER A 283 15202 12937 8629 -6429 -668 245 O ATOM 3135 N THR A 284 43.637 -5.329 1.004 1.00 87.13 N ANISOU 3135 N THR A 284 13099 12322 7685 -5762 -848 301 N ATOM 3136 CA THR A 284 44.603 -5.365 -0.096 1.00 87.15 C ANISOU 3136 CA THR A 284 12779 12603 7730 -5650 -899 300 C ATOM 3137 C THR A 284 43.872 -5.302 -1.457 1.00 90.61 C ANISOU 3137 C THR A 284 13174 12924 8329 -5544 -736 291 C ATOM 3138 O THR A 284 44.523 -5.145 -2.498 1.00 91.29 O ANISOU 3138 O THR A 284 13028 13202 8457 -5489 -724 286 O ATOM 3139 CB THR A 284 45.568 -6.547 0.103 1.00 95.11 C ANISOU 3139 CB THR A 284 13651 13834 8650 -5384 -1127 323 C ATOM 3140 OG1 THR A 284 46.070 -6.452 1.435 1.00101.04 O ANISOU 3140 OG1 THR A 284 14493 14663 9234 -5488 -1274 320 O ATOM 3141 CG2 THR A 284 46.764 -6.511 -0.825 1.00 94.35 C ANISOU 3141 CG2 THR A 284 13174 14110 8563 -5295 -1196 295 C ATOM 3142 N ASN A 285 42.520 -5.304 -1.445 1.00 85.81 N ANISOU 3142 N ASN A 285 12781 12024 7797 -5540 -599 270 N ATOM 3143 CA ASN A 285 41.726 -5.167 -2.666 1.00 84.41 C ANISOU 3143 CA ASN A 285 12573 11746 7753 -5431 -460 238 C ATOM 3144 C ASN A 285 42.024 -3.810 -3.342 1.00 89.38 C ANISOU 3144 C ASN A 285 13145 12436 8378 -5585 -355 225 C ATOM 3145 O ASN A 285 42.046 -3.733 -4.563 1.00 88.36 O ANISOU 3145 O ASN A 285 12907 12351 8316 -5467 -299 221 O ATOM 3146 CB ASN A 285 40.233 -5.398 -2.390 1.00 84.44 C ANISOU 3146 CB ASN A 285 12782 11487 7816 -5414 -344 178 C ATOM 3147 CG ASN A 285 39.483 -4.233 -1.804 1.00108.54 C ANISOU 3147 CG ASN A 285 16008 14392 10838 -5616 -218 126 C ATOM 3148 OD1 ASN A 285 38.877 -3.440 -2.528 1.00108.00 O ANISOU 3148 OD1 ASN A 285 15955 14260 10820 -5594 -100 77 O ATOM 3149 ND2 ASN A 285 39.464 -4.124 -0.487 1.00 97.47 N ANISOU 3149 ND2 ASN A 285 14770 12924 9339 -5786 -242 131 N ATOM 3150 N CYS A 286 42.353 -2.780 -2.517 1.00 88.00 N ANISOU 3150 N CYS A 286 13074 12264 8098 -5859 -332 220 N ATOM 3151 CA CYS A 286 42.764 -1.401 -2.838 1.00 88.55 C ANISOU 3151 CA CYS A 286 13184 12361 8101 -6092 -224 205 C ATOM 3152 C CYS A 286 43.772 -1.355 -3.942 1.00 88.86 C ANISOU 3152 C CYS A 286 12987 12631 8144 -6073 -224 214 C ATOM 3153 O CYS A 286 43.695 -0.500 -4.817 1.00 87.69 O ANISOU 3153 O CYS A 286 12916 12419 7983 -6140 -83 202 O ATOM 3154 CB CYS A 286 43.357 -0.750 -1.594 1.00 91.62 C ANISOU 3154 CB CYS A 286 13656 12806 8349 -6393 -267 197 C ATOM 3155 SG CYS A 286 42.198 0.261 -0.665 1.00 95.84 S ANISOU 3155 SG CYS A 286 14573 13013 8829 -6562 -133 164 S ATOM 3156 N VAL A 287 44.790 -2.203 -3.803 1.00 84.80 N ANISOU 3156 N VAL A 287 12211 12396 7614 -5998 -382 225 N ATOM 3157 CA VAL A 287 45.945 -2.321 -4.671 1.00 85.64 C ANISOU 3157 CA VAL A 287 12020 12812 7708 -5981 -408 211 C ATOM 3158 C VAL A 287 45.734 -3.383 -5.770 1.00 88.59 C ANISOU 3158 C VAL A 287 12261 13197 8200 -5627 -431 235 C ATOM 3159 O VAL A 287 46.169 -3.170 -6.901 1.00 88.71 O ANISOU 3159 O VAL A 287 12143 13328 8234 -5607 -349 223 O ATOM 3160 CB VAL A 287 47.205 -2.622 -3.813 1.00 91.27 C ANISOU 3160 CB VAL A 287 12496 13873 8310 -6071 -588 179 C ATOM 3161 CG1 VAL A 287 48.488 -2.493 -4.631 1.00 93.12 C ANISOU 3161 CG1 VAL A 287 12382 14494 8505 -6135 -585 120 C ATOM 3162 CG2 VAL A 287 47.263 -1.716 -2.592 1.00 92.07 C ANISOU 3162 CG2 VAL A 287 12762 13931 8291 -6405 -586 152 C ATOM 3163 N LEU A 288 45.059 -4.500 -5.452 1.00 83.10 N ANISOU 3163 N LEU A 288 11635 12370 7569 -5372 -523 263 N ATOM 3164 CA LEU A 288 44.910 -5.598 -6.404 1.00 81.11 C ANISOU 3164 CA LEU A 288 11282 12126 7410 -5050 -554 277 C ATOM 3165 C LEU A 288 43.894 -5.348 -7.503 1.00 82.50 C ANISOU 3165 C LEU A 288 11569 12089 7688 -4964 -403 265 C ATOM 3166 O LEU A 288 44.202 -5.684 -8.651 1.00 82.18 O ANISOU 3166 O LEU A 288 11389 12143 7695 -4802 -381 265 O ATOM 3167 CB LEU A 288 44.651 -6.923 -5.696 1.00 80.83 C ANISOU 3167 CB LEU A 288 11323 12021 7368 -4833 -698 301 C ATOM 3168 CG LEU A 288 45.751 -7.333 -4.695 1.00 87.60 C ANISOU 3168 CG LEU A 288 12083 13109 8094 -4823 -890 311 C ATOM 3169 CD1 LEU A 288 45.463 -8.669 -4.105 1.00 88.13 C ANISOU 3169 CD1 LEU A 288 12320 13046 8121 -4578 -1016 343 C ATOM 3170 CD2 LEU A 288 47.156 -7.322 -5.326 1.00 91.18 C ANISOU 3170 CD2 LEU A 288 12177 13964 8503 -4759 -969 282 C ATOM 3171 N ASN A 289 42.715 -4.752 -7.193 1.00 77.50 N ANISOU 3171 N ASN A 289 11173 11196 7078 -5049 -304 239 N ATOM 3172 CA AASN A 289 41.707 -4.505 -8.230 0.50 76.17 C ANISOU 3172 CA AASN A 289 11091 10862 6986 -4920 -187 202 C ATOM 3173 CA BASN A 289 41.717 -4.477 -8.226 0.50 76.28 C ANISOU 3173 CA BASN A 289 11093 10893 6996 -4926 -191 206 C ATOM 3174 C ASN A 289 42.242 -3.513 -9.318 1.00 81.11 C ANISOU 3174 C ASN A 289 11693 11556 7570 -4986 -79 210 C ATOM 3175 O ASN A 289 42.100 -3.831 -10.515 1.00 80.00 O ANISOU 3175 O ASN A 289 11485 11429 7483 -4787 -52 204 O ATOM 3176 CB AASN A 289 40.301 -4.134 -7.673 0.50 75.23 C ANISOU 3176 CB AASN A 289 11194 10500 6891 -4947 -113 140 C ATOM 3177 CB BASN A 289 40.398 -4.032 -7.627 0.50 75.38 C ANISOU 3177 CB BASN A 289 11203 10532 6906 -4953 -118 146 C ATOM 3178 CG AASN A 289 40.096 -2.768 -7.053 0.50 97.00 C ANISOU 3178 CG AASN A 289 14146 13146 9563 -5167 -22 124 C ATOM 3179 CG BASN A 289 39.635 -5.192 -7.048 0.50 95.35 C ANISOU 3179 CG BASN A 289 13776 12966 9488 -4863 -165 108 C ATOM 3180 OD1AASN A 289 40.121 -1.740 -7.729 0.50 92.59 O ANISOU 3180 OD1AASN A 289 13680 12545 8956 -5205 74 121 O ATOM 3181 OD1BASN A 289 39.842 -6.359 -7.391 0.50 88.19 O ANISOU 3181 OD1BASN A 289 12779 12111 8617 -4704 -241 124 O ATOM 3182 ND2AASN A 289 39.749 -2.738 -5.774 0.50 87.28 N ANISOU 3182 ND2AASN A 289 13037 11828 8299 -5301 -35 107 N ATOM 3183 ND2BASN A 289 38.783 -4.913 -6.099 0.50 88.69 N ANISOU 3183 ND2BASN A 289 13101 11976 8622 -4989 -111 57 N ATOM 3184 N PRO A 290 42.966 -2.390 -8.994 1.00 78.79 N ANISOU 3184 N PRO A 290 11447 11327 7164 -5269 -18 220 N ATOM 3185 CA PRO A 290 43.505 -1.552 -10.081 1.00 79.33 C ANISOU 3185 CA PRO A 290 11528 11446 7166 -5353 108 222 C ATOM 3186 C PRO A 290 44.534 -2.318 -10.918 1.00 84.66 C ANISOU 3186 C PRO A 290 11901 12396 7868 -5245 62 232 C ATOM 3187 O PRO A 290 44.554 -2.146 -12.139 1.00 83.86 O ANISOU 3187 O PRO A 290 11814 12282 7765 -5154 157 231 O ATOM 3188 CB PRO A 290 44.130 -0.364 -9.340 1.00 82.55 C ANISOU 3188 CB PRO A 290 12056 11878 7431 -5735 181 213 C ATOM 3189 CG PRO A 290 43.476 -0.365 -8.020 1.00 86.63 C ANISOU 3189 CG PRO A 290 12708 12255 7951 -5792 120 208 C ATOM 3190 CD PRO A 290 43.317 -1.799 -7.690 1.00 80.96 C ANISOU 3190 CD PRO A 290 11805 11612 7346 -5551 -38 220 C ATOM 3191 N VAL A 291 45.335 -3.214 -10.273 1.00 82.68 N ANISOU 3191 N VAL A 291 11396 12388 7631 -5213 -90 236 N ATOM 3192 CA VAL A 291 46.312 -4.078 -10.966 1.00 83.70 C ANISOU 3192 CA VAL A 291 11215 12807 7779 -5049 -158 230 C ATOM 3193 C VAL A 291 45.570 -4.969 -11.986 1.00 87.43 C ANISOU 3193 C VAL A 291 11711 13147 8362 -4703 -161 247 C ATOM 3194 O VAL A 291 45.994 -5.053 -13.147 1.00 87.60 O ANISOU 3194 O VAL A 291 11620 13276 8387 -4610 -97 240 O ATOM 3195 CB VAL A 291 47.193 -4.893 -9.987 1.00 88.35 C ANISOU 3195 CB VAL A 291 11574 13661 8333 -5006 -351 221 C ATOM 3196 CG1 VAL A 291 47.957 -6.003 -10.701 1.00 88.98 C ANISOU 3196 CG1 VAL A 291 11374 13997 8439 -4712 -445 210 C ATOM 3197 CG2 VAL A 291 48.164 -3.986 -9.256 1.00 90.40 C ANISOU 3197 CG2 VAL A 291 11726 14153 8467 -5361 -343 172 C ATOM 3198 N ILE A 292 44.430 -5.568 -11.563 1.00 82.45 N ANISOU 3198 N ILE A 292 11240 12281 7806 -4548 -215 253 N ATOM 3199 CA ILE A 292 43.570 -6.376 -12.434 1.00 81.31 C ANISOU 3199 CA ILE A 292 11138 11998 7756 -4266 -212 242 C ATOM 3200 C ILE A 292 43.052 -5.505 -13.601 1.00 84.65 C ANISOU 3200 C ILE A 292 11681 12305 8178 -4255 -68 222 C ATOM 3201 O ILE A 292 43.197 -5.913 -14.753 1.00 83.29 O ANISOU 3201 O ILE A 292 11431 12185 8033 -4073 -47 219 O ATOM 3202 CB ILE A 292 42.461 -7.123 -11.621 1.00 83.52 C ANISOU 3202 CB ILE A 292 11565 12076 8093 -4185 -274 220 C ATOM 3203 CG1 ILE A 292 43.081 -8.295 -10.827 1.00 84.89 C ANISOU 3203 CG1 ILE A 292 11664 12351 8241 -4090 -425 251 C ATOM 3204 CG2 ILE A 292 41.290 -7.628 -12.497 1.00 82.10 C ANISOU 3204 CG2 ILE A 292 11461 11732 7999 -3981 -230 164 C ATOM 3205 CD1 ILE A 292 42.459 -8.548 -9.504 1.00 91.31 C ANISOU 3205 CD1 ILE A 292 12656 13008 9031 -4184 -468 245 C ATOM 3206 N TYR A 293 42.548 -4.274 -13.300 1.00 82.02 N ANISOU 3206 N TYR A 293 11563 11816 7786 -4440 29 209 N ATOM 3207 CA TYR A 293 42.063 -3.310 -14.303 1.00 81.69 C ANISOU 3207 CA TYR A 293 11718 11630 7691 -4412 160 192 C ATOM 3208 C TYR A 293 43.162 -2.971 -15.314 1.00 83.99 C ANISOU 3208 C TYR A 293 11930 12075 7905 -4480 249 219 C ATOM 3209 O TYR A 293 42.844 -2.745 -16.474 1.00 82.74 O ANISOU 3209 O TYR A 293 11884 11831 7722 -4335 324 212 O ATOM 3210 CB TYR A 293 41.588 -1.979 -13.665 1.00 84.22 C ANISOU 3210 CB TYR A 293 12322 11765 7914 -4612 249 180 C ATOM 3211 CG TYR A 293 40.469 -2.010 -12.640 1.00 86.12 C ANISOU 3211 CG TYR A 293 12673 11849 8200 -4587 205 133 C ATOM 3212 CD1 TYR A 293 39.495 -3.007 -12.665 1.00 86.85 C ANISOU 3212 CD1 TYR A 293 12686 11904 8409 -4358 131 76 C ATOM 3213 CD2 TYR A 293 40.318 -0.977 -11.718 1.00 88.24 C ANISOU 3213 CD2 TYR A 293 13152 11999 8377 -4804 261 129 C ATOM 3214 CE1 TYR A 293 38.449 -3.023 -11.736 1.00 87.73 C ANISOU 3214 CE1 TYR A 293 12886 11896 8550 -4367 120 7 C ATOM 3215 CE2 TYR A 293 39.278 -0.981 -10.785 1.00 88.85 C ANISOU 3215 CE2 TYR A 293 13326 11945 8487 -4781 238 72 C ATOM 3216 CZ TYR A 293 38.344 -2.005 -10.798 1.00 96.75 C ANISOU 3216 CZ TYR A 293 14213 12939 9608 -4567 173 7 C ATOM 3217 OH TYR A 293 37.330 -2.008 -9.866 1.00 99.54 O ANISOU 3217 OH TYR A 293 14647 13191 9984 -4580 177 -72 O ATOM 3218 N CYS A 294 44.440 -2.899 -14.863 1.00 81.38 N ANISOU 3218 N CYS A 294 11412 11987 7523 -4709 246 234 N ATOM 3219 CA CYS A 294 45.618 -2.592 -15.699 1.00 82.81 C ANISOU 3219 CA CYS A 294 11461 12383 7619 -4840 351 229 C ATOM 3220 C CYS A 294 45.855 -3.717 -16.713 1.00 88.73 C ANISOU 3220 C CYS A 294 11995 13270 8448 -4538 301 229 C ATOM 3221 O CYS A 294 45.849 -3.463 -17.917 1.00 87.81 O ANISOU 3221 O CYS A 294 11965 13108 8291 -4468 414 228 O ATOM 3222 CB CYS A 294 46.850 -2.346 -14.829 1.00 83.99 C ANISOU 3222 CB CYS A 294 11395 12819 7697 -5150 334 203 C ATOM 3223 SG CYS A 294 48.258 -1.619 -15.701 1.00 89.98 S ANISOU 3223 SG CYS A 294 12021 13856 8311 -5458 527 149 S ATOM 3224 N PHE A 295 45.995 -4.967 -16.216 1.00 87.39 N ANISOU 3224 N PHE A 295 11600 13232 8373 -4341 131 231 N ATOM 3225 CA PHE A 295 46.166 -6.197 -16.999 1.00 87.67 C ANISOU 3225 CA PHE A 295 11460 13372 8478 -4023 59 229 C ATOM 3226 C PHE A 295 44.974 -6.403 -17.954 1.00 88.61 C ANISOU 3226 C PHE A 295 11779 13231 8656 -3791 93 227 C ATOM 3227 O PHE A 295 45.164 -6.840 -19.087 1.00 88.00 O ANISOU 3227 O PHE A 295 11640 13209 8586 -3611 126 220 O ATOM 3228 CB PHE A 295 46.373 -7.382 -16.028 1.00 90.14 C ANISOU 3228 CB PHE A 295 11624 13785 8841 -3871 -132 235 C ATOM 3229 CG PHE A 295 46.213 -8.813 -16.498 1.00 92.25 C ANISOU 3229 CG PHE A 295 11827 14050 9174 -3514 -235 238 C ATOM 3230 CD1 PHE A 295 46.731 -9.228 -17.722 1.00 96.84 C ANISOU 3230 CD1 PHE A 295 12276 14765 9755 -3335 -190 224 C ATOM 3231 CD2 PHE A 295 45.657 -9.775 -15.663 1.00 94.49 C ANISOU 3231 CD2 PHE A 295 12201 14205 9495 -3376 -368 249 C ATOM 3232 CE1 PHE A 295 46.596 -10.554 -18.147 1.00 97.65 C ANISOU 3232 CE1 PHE A 295 12356 14846 9900 -3006 -281 223 C ATOM 3233 CE2 PHE A 295 45.556 -11.105 -16.071 1.00 97.65 C ANISOU 3233 CE2 PHE A 295 12601 14578 9925 -3070 -449 248 C ATOM 3234 CZ PHE A 295 46.021 -11.485 -17.312 1.00 96.46 C ANISOU 3234 CZ PHE A 295 12328 14545 9779 -2879 -410 235 C ATOM 3235 N LEU A 296 43.769 -6.020 -17.513 1.00 83.97 N ANISOU 3235 N LEU A 296 11420 12388 8097 -3801 88 216 N ATOM 3236 CA LEU A 296 42.544 -6.087 -18.300 1.00 82.91 C ANISOU 3236 CA LEU A 296 11455 12045 8002 -3592 106 178 C ATOM 3237 C LEU A 296 42.582 -5.094 -19.459 1.00 87.42 C ANISOU 3237 C LEU A 296 12193 12551 8471 -3599 244 180 C ATOM 3238 O LEU A 296 42.191 -5.449 -20.563 1.00 86.81 O ANISOU 3238 O LEU A 296 12146 12432 8405 -3371 250 157 O ATOM 3239 CB LEU A 296 41.344 -5.801 -17.405 1.00 82.44 C ANISOU 3239 CB LEU A 296 11559 11790 7975 -3627 75 136 C ATOM 3240 CG LEU A 296 40.041 -6.410 -17.844 1.00 87.31 C ANISOU 3240 CG LEU A 296 12229 12279 8667 -3391 32 52 C ATOM 3241 CD1 LEU A 296 40.019 -7.899 -17.566 1.00 87.47 C ANISOU 3241 CD1 LEU A 296 12106 12352 8777 -3280 -68 36 C ATOM 3242 CD2 LEU A 296 38.873 -5.722 -17.159 1.00 91.06 C ANISOU 3242 CD2 LEU A 296 12867 12595 9135 -3442 48 -18 C ATOM 3243 N THR A 297 43.066 -3.859 -19.213 1.00 85.03 N ANISOU 3243 N THR A 297 12033 12226 8048 -3869 360 205 N ATOM 3244 CA THR A 297 43.206 -2.808 -20.224 1.00 85.66 C ANISOU 3244 CA THR A 297 12359 12207 7981 -3926 521 215 C ATOM 3245 C THR A 297 44.281 -3.252 -21.211 1.00 90.50 C ANISOU 3245 C THR A 297 12784 13033 8568 -3914 586 227 C ATOM 3246 O THR A 297 44.007 -3.388 -22.396 1.00 90.72 O ANISOU 3246 O THR A 297 12911 12994 8565 -3711 628 221 O ATOM 3247 CB THR A 297 43.507 -1.451 -19.541 1.00 95.00 C ANISOU 3247 CB THR A 297 13774 13299 9024 -4271 640 231 C ATOM 3248 OG1 THR A 297 42.342 -1.030 -18.835 1.00 95.74 O ANISOU 3248 OG1 THR A 297 14082 13167 9128 -4204 588 209 O ATOM 3249 CG2 THR A 297 43.919 -0.351 -20.524 1.00 94.64 C ANISOU 3249 CG2 THR A 297 14031 13150 8779 -4408 842 246 C ATOM 3250 N LYS A 298 45.478 -3.538 -20.696 1.00 87.46 N ANISOU 3250 N LYS A 298 12110 12929 8193 -4107 583 228 N ATOM 3251 CA LYS A 298 46.658 -3.987 -21.432 1.00 88.40 C ANISOU 3251 CA LYS A 298 11970 13332 8285 -4120 644 212 C ATOM 3252 C LYS A 298 46.427 -5.218 -22.347 1.00 89.64 C ANISOU 3252 C LYS A 298 11997 13525 8536 -3739 560 208 C ATOM 3253 O LYS A 298 46.985 -5.248 -23.444 1.00 91.10 O ANISOU 3253 O LYS A 298 12147 13808 8658 -3699 671 197 O ATOM 3254 CB LYS A 298 47.786 -4.267 -20.416 1.00 92.41 C ANISOU 3254 CB LYS A 298 12133 14172 8806 -4316 582 185 C ATOM 3255 CG LYS A 298 49.188 -4.420 -20.984 1.00111.99 C ANISOU 3255 CG LYS A 298 14302 17027 11220 -4421 674 129 C ATOM 3256 CD LYS A 298 50.188 -4.576 -19.850 1.00124.01 C ANISOU 3256 CD LYS A 298 15488 18895 12735 -4603 584 75 C ATOM 3257 CE LYS A 298 51.489 -5.182 -20.307 1.00138.02 C ANISOU 3257 CE LYS A 298 16840 21119 14483 -4554 594 -9 C ATOM 3258 NZ LYS A 298 52.303 -5.635 -19.148 1.00149.91 N ANISOU 3258 NZ LYS A 298 17993 22973 15994 -4575 422 -70 N ATOM 3259 N LYS A 299 45.619 -6.219 -21.912 1.00 81.69 N ANISOU 3259 N LYS A 299 10944 12432 7661 -3486 385 209 N ATOM 3260 CA LYS A 299 45.464 -7.464 -22.671 1.00 79.47 C ANISOU 3260 CA LYS A 299 10552 12185 7456 -3156 306 196 C ATOM 3261 C LYS A 299 44.030 -7.829 -23.145 1.00 81.30 C ANISOU 3261 C LYS A 299 10985 12157 7748 -2912 244 169 C ATOM 3262 O LYS A 299 43.880 -8.785 -23.918 1.00 80.38 O ANISOU 3262 O LYS A 299 10815 12053 7673 -2664 199 147 O ATOM 3263 CB LYS A 299 46.059 -8.632 -21.866 1.00 80.51 C ANISOU 3263 CB LYS A 299 10419 12511 7659 -3056 158 194 C ATOM 3264 CG LYS A 299 47.477 -8.401 -21.312 1.00 79.64 C ANISOU 3264 CG LYS A 299 10041 12732 7486 -3250 174 185 C ATOM 3265 CD LYS A 299 48.555 -8.444 -22.366 1.00 87.27 C ANISOU 3265 CD LYS A 299 10810 13965 8385 -3230 288 150 C ATOM 3266 CE LYS A 299 49.888 -8.864 -21.804 1.00101.17 C ANISOU 3266 CE LYS A 299 12198 16130 10113 -3250 222 101 C ATOM 3267 NZ LYS A 299 50.915 -8.992 -22.878 1.00114.62 N ANISOU 3267 NZ LYS A 299 13669 18129 11751 -3205 343 40 N ATOM 3268 N PHE A 300 42.993 -7.099 -22.705 1.00 76.82 N ANISOU 3268 N PHE A 300 10632 11378 7176 -2975 241 152 N ATOM 3269 CA PHE A 300 41.606 -7.387 -23.114 1.00 75.28 C ANISOU 3269 CA PHE A 300 10576 11000 7028 -2751 177 86 C ATOM 3270 C PHE A 300 40.954 -6.146 -23.717 1.00 79.73 C ANISOU 3270 C PHE A 300 11424 11394 7476 -2736 260 67 C ATOM 3271 O PHE A 300 39.723 -6.049 -23.820 1.00 76.98 O ANISOU 3271 O PHE A 300 11197 10911 7140 -2578 202 -12 O ATOM 3272 CB PHE A 300 40.792 -8.012 -21.947 1.00 75.89 C ANISOU 3272 CB PHE A 300 10610 11013 7211 -2760 63 41 C ATOM 3273 CG PHE A 300 41.409 -9.296 -21.442 1.00 77.23 C ANISOU 3273 CG PHE A 300 10589 11303 7451 -2723 -23 64 C ATOM 3274 CD1 PHE A 300 41.135 -10.508 -22.064 1.00 80.12 C ANISOU 3274 CD1 PHE A 300 10912 11663 7867 -2500 -81 22 C ATOM 3275 CD2 PHE A 300 42.352 -9.278 -20.419 1.00 79.85 C ANISOU 3275 CD2 PHE A 300 10808 11760 7772 -2892 -47 123 C ATOM 3276 CE1 PHE A 300 41.767 -11.685 -21.648 1.00 81.56 C ANISOU 3276 CE1 PHE A 300 10985 11927 8075 -2427 -158 48 C ATOM 3277 CE2 PHE A 300 42.986 -10.452 -20.009 1.00 83.22 C ANISOU 3277 CE2 PHE A 300 11095 12300 8227 -2793 -143 143 C ATOM 3278 CZ PHE A 300 42.682 -11.650 -20.619 1.00 81.10 C ANISOU 3278 CZ PHE A 300 10830 11989 7996 -2552 -195 110 C ATOM 3279 N ARG A 301 41.834 -5.227 -24.182 1.00 80.40 N ANISOU 3279 N ARG A 301 11621 11500 7426 -2894 404 125 N ATOM 3280 CA ARG A 301 41.560 -3.928 -24.797 1.00 82.14 C ANISOU 3280 CA ARG A 301 12197 11540 7474 -2918 522 133 C ATOM 3281 C ARG A 301 40.492 -3.997 -25.879 1.00 87.48 C ANISOU 3281 C ARG A 301 13054 12079 8107 -2576 469 71 C ATOM 3282 O ARG A 301 39.449 -3.361 -25.722 1.00 87.29 O ANISOU 3282 O ARG A 301 13246 11892 8030 -2460 428 17 O ATOM 3283 CB ARG A 301 42.854 -3.321 -25.359 1.00 85.13 C ANISOU 3283 CB ARG A 301 12630 12005 7711 -3150 707 191 C ATOM 3284 CG ARG A 301 43.045 -1.840 -25.026 1.00102.08 C ANISOU 3284 CG ARG A 301 15111 13996 9678 -3432 859 221 C ATOM 3285 CD ARG A 301 44.181 -1.197 -25.813 1.00122.26 C ANISOU 3285 CD ARG A 301 17793 16606 12055 -3678 1083 251 C ATOM 3286 NE ARG A 301 45.506 -1.647 -25.375 1.00137.18 N ANISOU 3286 NE ARG A 301 19288 18827 14005 -3950 1130 246 N ATOM 3287 CZ ARG A 301 46.256 -2.539 -26.021 1.00154.82 C ANISOU 3287 CZ ARG A 301 21218 21312 16296 -3867 1137 230 C ATOM 3288 NH1 ARG A 301 45.820 -3.094 -27.148 1.00141.85 N ANISOU 3288 NH1 ARG A 301 19633 19603 14660 -3546 1109 227 N ATOM 3289 NH2 ARG A 301 47.444 -2.884 -25.545 1.00143.47 N ANISOU 3289 NH2 ARG A 301 19408 20209 14896 -4084 1164 202 N ATOM 3290 N LYS A 302 40.731 -4.790 -26.953 1.00 85.14 N ANISOU 3290 N LYS A 302 12658 11866 7825 -2394 460 61 N ATOM 3291 CA LYS A 302 39.802 -4.927 -28.082 1.00 85.77 C ANISOU 3291 CA LYS A 302 12892 11847 7848 -2062 399 -9 C ATOM 3292 C LYS A 302 38.402 -5.355 -27.636 1.00 90.84 C ANISOU 3292 C LYS A 302 13466 12453 8594 -1869 232 -130 C ATOM 3293 O LYS A 302 37.417 -4.673 -27.953 1.00 90.99 O ANISOU 3293 O LYS A 302 13709 12351 8513 -1677 190 -205 O ATOM 3294 CB LYS A 302 40.364 -5.869 -29.159 1.00 88.03 C ANISOU 3294 CB LYS A 302 13041 12252 8153 -1928 411 -3 C ATOM 3295 N HIS A 303 38.329 -6.441 -26.842 1.00 87.44 N ANISOU 3295 N HIS A 303 12746 12135 8344 -1929 146 -161 N ATOM 3296 CA HIS A 303 37.076 -6.980 -26.337 1.00 86.89 C ANISOU 3296 CA HIS A 303 12578 12059 8376 -1823 21 -296 C ATOM 3297 C HIS A 303 36.307 -5.969 -25.485 1.00 86.92 C ANISOU 3297 C HIS A 303 12715 11969 8341 -1879 16 -343 C ATOM 3298 O HIS A 303 35.115 -5.752 -25.721 1.00 85.91 O ANISOU 3298 O HIS A 303 12643 11816 8183 -1673 -59 -485 O ATOM 3299 CB HIS A 303 37.315 -8.287 -25.570 1.00 88.15 C ANISOU 3299 CB HIS A 303 12483 12316 8696 -1931 -32 -299 C ATOM 3300 CG HIS A 303 36.160 -9.231 -25.677 1.00 92.58 C ANISOU 3300 CG HIS A 303 12948 12892 9335 -1794 -131 -461 C ATOM 3301 ND1 HIS A 303 34.959 -8.989 -25.017 1.00 94.91 N ANISOU 3301 ND1 HIS A 303 13236 13166 9658 -1805 -177 -600 N ATOM 3302 CD2 HIS A 303 36.040 -10.370 -26.399 1.00 95.40 C ANISOU 3302 CD2 HIS A 303 13220 13296 9733 -1663 -177 -522 C ATOM 3303 CE1 HIS A 303 34.159 -9.989 -25.352 1.00 94.83 C ANISOU 3303 CE1 HIS A 303 13117 13210 9705 -1712 -242 -752 C ATOM 3304 NE2 HIS A 303 34.766 -10.849 -26.178 1.00 95.30 N ANISOU 3304 NE2 HIS A 303 13144 13294 9771 -1629 -246 -706 N ATOM 3305 N LEU A 304 37.003 -5.318 -24.537 1.00 81.37 N ANISOU 3305 N LEU A 304 12062 11233 7623 -2143 94 -240 N ATOM 3306 CA LEU A 304 36.408 -4.338 -23.633 1.00 80.84 C ANISOU 3306 CA LEU A 304 12143 11062 7508 -2222 105 -270 C ATOM 3307 C LEU A 304 35.847 -3.091 -24.317 1.00 83.71 C ANISOU 3307 C LEU A 304 12854 11273 7678 -2028 135 -302 C ATOM 3308 O LEU A 304 34.701 -2.714 -24.032 1.00 82.14 O ANISOU 3308 O LEU A 304 12720 11034 7456 -1862 67 -427 O ATOM 3309 CB LEU A 304 37.397 -3.952 -22.539 1.00 81.29 C ANISOU 3309 CB LEU A 304 12188 11124 7575 -2564 182 -152 C ATOM 3310 CG LEU A 304 37.639 -5.008 -21.471 1.00 85.87 C ANISOU 3310 CG LEU A 304 12493 11819 8316 -2721 121 -145 C ATOM 3311 CD1 LEU A 304 38.984 -4.811 -20.838 1.00 86.80 C ANISOU 3311 CD1 LEU A 304 12553 12012 8415 -3003 183 -21 C ATOM 3312 CD2 LEU A 304 36.538 -4.995 -20.412 1.00 88.97 C ANISOU 3312 CD2 LEU A 304 12874 12161 8769 -2747 69 -247 C ATOM 3313 N THR A 305 36.650 -2.459 -25.224 1.00 81.09 N ANISOU 3313 N THR A 305 12759 10861 7189 -2038 241 -201 N ATOM 3314 CA THR A 305 36.289 -1.257 -26.000 1.00 81.75 C ANISOU 3314 CA THR A 305 13277 10751 7033 -1848 290 -206 C ATOM 3315 C THR A 305 35.019 -1.497 -26.809 1.00 83.21 C ANISOU 3315 C THR A 305 13481 10951 7185 -1414 142 -361 C ATOM 3316 O THR A 305 34.150 -0.619 -26.854 1.00 82.20 O ANISOU 3316 O THR A 305 13620 10704 6908 -1182 99 -440 O ATOM 3317 CB THR A 305 37.470 -0.773 -26.865 1.00 91.83 C ANISOU 3317 CB THR A 305 14788 11956 8149 -1987 455 -77 C ATOM 3318 OG1 THR A 305 38.657 -0.801 -26.082 1.00 95.80 O ANISOU 3318 OG1 THR A 305 15136 12545 8716 -2399 568 23 O ATOM 3319 CG2 THR A 305 37.271 0.648 -27.402 1.00 91.14 C ANISOU 3319 CG2 THR A 305 15264 11599 7766 -1887 551 -52 C ATOM 3320 N GLU A 306 34.901 -2.709 -27.408 1.00 79.44 N ANISOU 3320 N GLU A 306 12712 10636 6838 -1299 56 -421 N ATOM 3321 CA GLU A 306 33.736 -3.136 -28.186 1.00 80.24 C ANISOU 3321 CA GLU A 306 12749 10812 6925 -925 -96 -599 C ATOM 3322 C GLU A 306 32.488 -3.217 -27.288 1.00 84.08 C ANISOU 3322 C GLU A 306 13055 11390 7501 -848 -207 -781 C ATOM 3323 O GLU A 306 31.456 -2.615 -27.604 1.00 84.11 O ANISOU 3323 O GLU A 306 13193 11386 7377 -530 -300 -927 O ATOM 3324 CB GLU A 306 34.018 -4.477 -28.887 1.00 80.95 C ANISOU 3324 CB GLU A 306 12570 11048 7139 -901 -137 -616 C ATOM 3325 N LYS A 307 32.627 -3.909 -26.134 1.00 80.64 N ANISOU 3325 N LYS A 307 12337 11040 7263 -1136 -190 -777 N ATOM 3326 CA LYS A 307 31.598 -4.115 -25.117 1.00 80.86 C ANISOU 3326 CA LYS A 307 12167 11164 7393 -1165 -251 -943 C ATOM 3327 C LYS A 307 31.017 -2.781 -24.605 1.00 87.04 C ANISOU 3327 C LYS A 307 13193 11842 8036 -1057 -243 -986 C ATOM 3328 O LYS A 307 29.790 -2.622 -24.620 1.00 87.81 O ANISOU 3328 O LYS A 307 13223 12041 8099 -802 -341 -1201 O ATOM 3329 CB LYS A 307 32.166 -4.972 -23.969 1.00 82.48 C ANISOU 3329 CB LYS A 307 12143 11411 7783 -1533 -199 -869 C ATOM 3330 CG LYS A 307 31.120 -5.827 -23.240 1.00100.80 C ANISOU 3330 CG LYS A 307 14190 13871 10239 -1588 -255 -1069 C ATOM 3331 CD LYS A 307 31.742 -6.945 -22.381 1.00107.38 C ANISOU 3331 CD LYS A 307 14856 14719 11223 -1902 -213 -988 C ATOM 3332 CE LYS A 307 31.955 -8.244 -23.129 1.00114.38 C ANISOU 3332 CE LYS A 307 15608 15673 12178 -1867 -247 -1007 C ATOM 3333 NZ LYS A 307 32.741 -9.220 -22.328 1.00118.65 N ANISOU 3333 NZ LYS A 307 16076 16189 12817 -2120 -210 -897 N ATOM 3334 N PHE A 308 31.899 -1.812 -24.218 1.00 83.71 N ANISOU 3334 N PHE A 308 13062 11230 7513 -1237 -125 -801 N ATOM 3335 CA PHE A 308 31.510 -0.485 -23.725 1.00 85.17 C ANISOU 3335 CA PHE A 308 13565 11260 7535 -1159 -93 -812 C ATOM 3336 C PHE A 308 30.660 0.316 -24.698 1.00 93.28 C ANISOU 3336 C PHE A 308 14885 12221 8337 -693 -175 -926 C ATOM 3337 O PHE A 308 29.661 0.909 -24.292 1.00 93.00 O ANISOU 3337 O PHE A 308 14917 12195 8223 -468 -238 -1076 O ATOM 3338 CB PHE A 308 32.744 0.361 -23.323 1.00 87.16 C ANISOU 3338 CB PHE A 308 14115 11310 7692 -1479 67 -592 C ATOM 3339 CG PHE A 308 32.414 1.784 -22.896 1.00 90.15 C ANISOU 3339 CG PHE A 308 14915 11475 7862 -1408 121 -591 C ATOM 3340 CD1 PHE A 308 31.936 2.053 -21.612 1.00 92.67 C ANISOU 3340 CD1 PHE A 308 15174 11797 8239 -1524 123 -652 C ATOM 3341 CD2 PHE A 308 32.541 2.845 -23.789 1.00 93.45 C ANISOU 3341 CD2 PHE A 308 15836 11668 8004 -1209 174 -536 C ATOM 3342 CE1 PHE A 308 31.587 3.355 -21.236 1.00 95.14 C ANISOU 3342 CE1 PHE A 308 15903 11902 8345 -1425 170 -661 C ATOM 3343 CE2 PHE A 308 32.188 4.145 -23.415 1.00 98.09 C ANISOU 3343 CE2 PHE A 308 16878 12024 8367 -1108 222 -541 C ATOM 3344 CZ PHE A 308 31.720 4.393 -22.140 1.00 96.26 C ANISOU 3344 CZ PHE A 308 16563 11807 8205 -1211 218 -604 C ATOM 3345 N TYR A 309 31.100 0.405 -25.961 1.00 94.13 N ANISOU 3345 N TYR A 309 15201 12253 8312 -532 -170 -854 N ATOM 3346 CA TYR A 309 30.420 1.223 -26.962 1.00 97.49 C ANISOU 3346 CA TYR A 309 15992 12578 8472 -63 -251 -938 C ATOM 3347 C TYR A 309 29.158 0.554 -27.537 1.00106.12 C ANISOU 3347 C TYR A 309 16788 13929 9604 337 -456 -1199 C ATOM 3348 O TYR A 309 28.358 1.234 -28.186 1.00108.25 O ANISOU 3348 O TYR A 309 17307 14173 9652 795 -570 -1325 O ATOM 3349 CB TYR A 309 31.401 1.699 -28.046 1.00 99.14 C ANISOU 3349 CB TYR A 309 16622 12569 8478 -69 -141 -755 C ATOM 3350 CG TYR A 309 32.139 2.964 -27.642 1.00101.49 C ANISOU 3350 CG TYR A 309 17423 12563 8576 -284 40 -588 C ATOM 3351 CD1 TYR A 309 31.466 4.179 -27.521 1.00105.82 C ANISOU 3351 CD1 TYR A 309 18433 12904 8868 0 20 -640 C ATOM 3352 CD2 TYR A 309 33.508 2.946 -27.378 1.00101.19 C ANISOU 3352 CD2 TYR A 309 17404 12457 8588 -770 232 -396 C ATOM 3353 CE1 TYR A 309 32.132 5.343 -27.134 1.00108.54 C ANISOU 3353 CE1 TYR A 309 19293 12940 9008 -229 203 -493 C ATOM 3354 CE2 TYR A 309 34.187 4.107 -26.993 1.00103.62 C ANISOU 3354 CE2 TYR A 309 18170 12501 8700 -1025 414 -267 C ATOM 3355 CZ TYR A 309 33.492 5.306 -26.874 1.00113.86 C ANISOU 3355 CZ TYR A 309 19970 13553 9739 -769 407 -310 C ATOM 3356 OH TYR A 309 34.125 6.472 -26.501 1.00115.20 O ANISOU 3356 OH TYR A 309 20655 13429 9688 -1034 599 -192 O ATOM 3357 N SER A 310 28.929 -0.735 -27.219 1.00103.99 N ANISOU 3357 N SER A 310 16003 13912 9595 165 -505 -1303 N ATOM 3358 CA SER A 310 27.718 -1.446 -27.625 1.00105.78 C ANISOU 3358 CA SER A 310 15892 14424 9876 448 -677 -1587 C ATOM 3359 C SER A 310 26.550 -1.088 -26.676 1.00113.30 C ANISOU 3359 C SER A 310 16679 15528 10844 560 -740 -1816 C ATOM 3360 O SER A 310 25.435 -0.855 -27.151 1.00114.67 O ANISOU 3360 O SER A 310 16791 15878 10898 981 -895 -2067 O ATOM 3361 CB SER A 310 27.959 -2.952 -27.642 1.00107.62 C ANISOU 3361 CB SER A 310 15709 14832 10351 176 -672 -1610 C ATOM 3362 OG SER A 310 26.773 -3.661 -27.960 1.00118.03 O ANISOU 3362 OG SER A 310 16690 16438 11718 374 -816 -1910 O ATOM 3363 N MET A 311 26.812 -1.033 -25.345 1.00111.06 N ANISOU 3363 N MET A 311 16316 15191 10690 199 -624 -1743 N ATOM 3364 CA MET A 311 25.793 -0.708 -24.333 1.00113.03 C ANISOU 3364 CA MET A 311 16408 15577 10962 249 -648 -1950 C ATOM 3365 C MET A 311 25.283 0.731 -24.447 1.00121.54 C ANISOU 3365 C MET A 311 17880 16529 11771 665 -698 -1999 C ATOM 3366 O MET A 311 24.072 0.958 -24.388 1.00123.33 O ANISOU 3366 O MET A 311 17953 16976 11930 1007 -816 -2281 O ATOM 3367 CB MET A 311 26.256 -1.036 -22.890 1.00113.50 C ANISOU 3367 CB MET A 311 16325 15589 11210 -248 -507 -1847 C ATOM 3368 CG MET A 311 27.502 -0.272 -22.432 1.00116.53 C ANISOU 3368 CG MET A 311 17082 15658 11536 -507 -369 -1538 C ATOM 3369 SD MET A 311 27.430 0.544 -20.802 1.00120.94 S ANISOU 3369 SD MET A 311 17757 16102 12094 -743 -262 -1509 S ATOM 3370 CE MET A 311 26.266 1.869 -21.122 1.00120.83 C ANISOU 3370 CE MET A 311 18031 16066 11812 -185 -353 -1704 C ATOM 3371 N ARG A 312 26.210 1.690 -24.633 1.00119.64 N ANISOU 3371 N ARG A 312 18157 15943 11358 638 -602 -1741 N ATOM 3372 CA ARG A 312 25.921 3.118 -24.742 1.00122.59 C ANISOU 3372 CA ARG A 312 19047 16098 11432 998 -617 -1737 C ATOM 3373 C ARG A 312 25.228 3.494 -26.058 1.00130.42 C ANISOU 3373 C ARG A 312 20248 17131 12173 1607 -791 -1880 C ATOM 3374 O ARG A 312 24.592 4.548 -26.121 1.00132.85 O ANISOU 3374 O ARG A 312 20908 17346 12222 2039 -861 -1973 O ATOM 3375 CB ARG A 312 27.203 3.939 -24.527 1.00122.25 C ANISOU 3375 CB ARG A 312 19513 15665 11274 688 -427 -1423 C ATOM 3376 N SER A 313 25.317 2.616 -27.086 1.00127.21 N ANISOU 3376 N SER A 313 19637 16870 11828 1667 -871 -1908 N ATOM 3377 CA SER A 313 24.726 2.803 -28.420 1.00129.88 C ANISOU 3377 CA SER A 313 20140 17272 11936 2225 -1052 -2043 C ATOM 3378 C SER A 313 23.190 2.980 -28.426 1.00137.15 C ANISOU 3378 C SER A 313 20825 18523 12764 2756 -1272 -2416 C ATOM 3379 O SER A 313 22.649 3.471 -29.419 1.00139.67 O ANISOU 3379 O SER A 313 21398 18858 12813 3317 -1441 -2532 O ATOM 3380 CB SER A 313 25.142 1.670 -29.353 1.00131.95 C ANISOU 3380 CB SER A 313 20152 17656 12328 2101 -1080 -2011 C ATOM 3381 OG SER A 313 24.735 1.926 -30.686 1.00143.43 O ANISOU 3381 OG SER A 313 21846 19122 13529 2619 -1241 -2102 O ATOM 3382 N SER A 314 22.502 2.605 -27.325 1.00133.45 N ANISOU 3382 N SER A 314 19882 18325 12497 2588 -1267 -2615 N ATOM 3383 CA SER A 314 21.051 2.751 -27.175 1.00136.06 C ANISOU 3383 CA SER A 314 19904 19033 12760 3031 -1447 -3006 C ATOM 3384 C SER A 314 20.688 3.547 -25.905 1.00140.75 C ANISOU 3384 C SER A 314 20568 19579 13332 3010 -1367 -3055 C ATOM 3385 O SER A 314 19.962 4.541 -25.993 1.00143.58 O ANISOU 3385 O SER A 314 21179 19946 13427 3553 -1483 -3206 O ATOM 3386 CB SER A 314 20.369 1.385 -27.175 1.00138.81 C ANISOU 3386 CB SER A 314 19530 19848 13361 2852 -1516 -3289 C ATOM 3387 N ARG A 315 21.203 3.116 -24.734 1.00134.30 N ANISOU 3387 N ARG A 315 19557 18701 12769 2412 -1175 -2927 N ATOM 3388 CA ARG A 315 20.944 3.756 -23.446 1.00160.06 C ANISOU 3388 CA ARG A 315 22866 21911 16037 2308 -1076 -2957 C ATOM 3389 C ARG A 315 22.235 3.913 -22.656 1.00188.11 C ANISOU 3389 C ARG A 315 26698 25084 19692 1742 -854 -2593 C ATOM 3390 O ARG A 315 23.185 4.516 -23.151 1.00151.03 O ANISOU 3390 O ARG A 315 22515 20023 14845 1718 -790 -2316 O ATOM 3391 CB ARG A 315 19.911 2.952 -22.644 1.00160.23 C ANISOU 3391 CB ARG A 315 22219 22391 16271 2173 -1090 -3298 C TER 3392 ARG A 315 HETATM 3393 CAK 9ER A1201 29.137 -3.382 9.551 1.00 77.84 C HETATM 3394 CAJ 9ER A1201 29.930 -4.672 9.842 1.00 77.71 C HETATM 3395 CAL 9ER A1201 30.747 -4.715 11.145 1.00 77.04 C HETATM 3396 CAH 9ER A1201 30.474 -5.334 8.722 1.00 77.92 C HETATM 3397 CAI 9ER A1201 29.784 -6.500 8.431 1.00 78.40 C HETATM 3398 CAD 9ER A1201 30.105 -7.331 7.366 1.00 77.41 C HETATM 3399 CAB 9ER A1201 29.328 -8.497 7.241 1.00 74.09 C HETATM 3400 CAA 9ER A1201 27.939 -8.199 6.692 1.00 73.63 C HETATM 3401 CAC 9ER A1201 30.006 -9.671 6.530 1.00 72.65 C HETATM 3402 CAE 9ER A1201 31.200 -6.974 6.557 1.00 78.07 C HETATM 3403 CAF 9ER A1201 31.948 -5.792 6.809 1.00 75.72 C HETATM 3404 CBE 9ER A1201 33.030 -5.437 5.959 1.00 66.61 C HETATM 3405 CBF 9ER A1201 34.186 -6.433 5.981 1.00 61.97 C HETATM 3406 CBG 9ER A1201 32.564 -5.165 4.539 1.00 66.10 C HETATM 3407 CAG 9ER A1201 31.556 -4.934 7.883 1.00 78.99 C HETATM 3408 CAM 9ER A1201 32.283 -3.832 8.176 1.00 80.59 C HETATM 3409 NAQ 9ER A1201 33.360 -3.928 8.977 1.00 79.39 N HETATM 3410 CAN 9ER A1201 31.981 -2.587 7.766 1.00 80.40 C HETATM 3411 SAO 9ER A1201 33.123 -1.589 8.438 1.00 78.65 S HETATM 3412 CAP 9ER A1201 33.964 -2.767 9.211 1.00 78.02 C HETATM 3413 NAR 9ER A1201 35.023 -2.633 10.020 1.00 76.88 N HETATM 3414 CAS 9ER A1201 35.582 -3.838 10.697 1.00 77.90 C HETATM 3415 CAT 9ER A1201 34.956 -3.968 12.096 1.00 80.43 C HETATM 3416 NAU 9ER A1201 35.121 -5.302 12.682 1.00 82.78 N HETATM 3417 CAV 9ER A1201 33.814 -5.702 13.230 1.00 83.15 C HETATM 3418 CAW 9ER A1201 36.097 -5.245 13.782 1.00 84.24 C HETATM 3419 CAX 9ER A1201 35.607 -1.288 10.378 1.00 72.39 C HETATM 3420 CAY 9ER A1201 36.972 -1.251 10.103 1.00 67.30 C HETATM 3421 CBD 9ER A1201 37.412 -1.056 8.789 1.00 66.40 C HETATM 3422 CBC 9ER A1201 38.776 -1.125 8.486 1.00 65.33 C HETATM 3423 CBB 9ER A1201 39.713 -1.384 9.492 1.00 64.39 C HETATM 3424 NBA 9ER A1201 39.267 -1.572 10.813 1.00 64.69 N HETATM 3425 CAZ 9ER A1201 37.895 -1.494 11.123 1.00 64.87 C HETATM 3426 N1 FMN A1202 48.809 -16.505 -59.457 1.00132.87 N ANISOU 3426 N1 FMN A1202 21514 18271 10701 1900 2654 -540 N HETATM 3427 C2 FMN A1202 48.614 -15.267 -58.825 1.00133.88 C ANISOU 3427 C2 FMN A1202 21764 18304 10798 1645 2682 -461 C HETATM 3428 O2 FMN A1202 49.262 -14.971 -57.823 1.00132.87 O ANISOU 3428 O2 FMN A1202 21292 18363 10830 1374 2790 -431 O HETATM 3429 N3 FMN A1202 47.671 -14.364 -59.343 1.00136.18 N ANISOU 3429 N3 FMN A1202 22596 18289 10857 1722 2576 -424 N HETATM 3430 C4 FMN A1202 46.928 -14.688 -60.500 1.00137.73 C ANISOU 3430 C4 FMN A1202 23182 18300 10851 2049 2432 -475 C HETATM 3431 O4 FMN A1202 46.100 -13.873 -60.922 1.00139.60 O ANISOU 3431 O4 FMN A1202 23891 18286 10864 2159 2316 -453 O HETATM 3432 C4A FMN A1202 47.113 -15.940 -61.113 1.00135.74 C ANISOU 3432 C4A FMN A1202 22780 18151 10645 2268 2404 -558 C HETATM 3433 N5 FMN A1202 46.405 -16.266 -62.214 1.00135.21 N ANISOU 3433 N5 FMN A1202 23080 17917 10378 2567 2260 -618 N HETATM 3434 C5A FMN A1202 46.756 -17.330 -62.954 1.00134.65 C ANISOU 3434 C5A FMN A1202 22952 17924 10287 2739 2309 -691 C HETATM 3435 C6 FMN A1202 46.170 -17.504 -64.210 1.00135.80 C ANISOU 3435 C6 FMN A1202 23538 17893 10166 3008 2218 -749 C HETATM 3436 C7 FMN A1202 46.528 -18.586 -65.018 1.00136.42 C ANISOU 3436 C7 FMN A1202 23599 18032 10202 3186 2278 -827 C HETATM 3437 C7M FMN A1202 45.904 -18.698 -66.264 1.00137.22 C ANISOU 3437 C7M FMN A1202 24164 17954 10021 3447 2173 -888 C HETATM 3438 C8 FMN A1202 47.480 -19.514 -64.548 1.00136.19 C ANISOU 3438 C8 FMN A1202 23108 18244 10396 3126 2426 -848 C HETATM 3439 C8M FMN A1202 47.894 -20.622 -65.294 1.00137.48 C ANISOU 3439 C8M FMN A1202 23253 18468 10514 3324 2498 -929 C HETATM 3440 C9 FMN A1202 48.060 -19.330 -63.289 1.00134.60 C ANISOU 3440 C9 FMN A1202 22461 18230 10449 2887 2501 -794 C HETATM 3441 C9A FMN A1202 47.695 -18.255 -62.460 1.00133.68 C ANISOU 3441 C9A FMN A1202 22346 18056 10389 2676 2440 -715 C HETATM 3442 N10 FMN A1202 48.276 -18.040 -61.239 1.00131.95 N ANISOU 3442 N10 FMN A1202 21708 18025 10404 2430 2514 -667 N HETATM 3443 C10 FMN A1202 48.043 -16.865 -60.590 1.00133.34 C ANISOU 3443 C10 FMN A1202 21964 18126 10574 2199 2517 -587 C HETATM 3444 C1' FMN A1202 49.363 -18.948 -60.726 1.00128.00 C ANISOU 3444 C1' FMN A1202 20706 17824 10103 2403 2652 -702 C HETATM 3445 C2' FMN A1202 48.893 -20.126 -59.862 1.00120.39 C ANISOU 3445 C2' FMN A1202 19414 16905 9426 2580 2355 -751 C HETATM 3446 O2' FMN A1202 48.302 -19.611 -58.668 1.00117.84 O ANISOU 3446 O2' FMN A1202 18938 16548 9288 2421 2169 -701 O HETATM 3447 C3' FMN A1202 50.131 -21.016 -59.594 1.00117.52 C ANISOU 3447 C3' FMN A1202 18646 16834 9172 2633 2530 -793 C HETATM 3448 O3' FMN A1202 50.291 -21.949 -60.668 1.00119.66 O ANISOU 3448 O3' FMN A1202 19078 17076 9311 2908 2574 -871 O HETATM 3449 C4' FMN A1202 50.131 -21.731 -58.221 1.00111.68 C ANISOU 3449 C4' FMN A1202 17491 16213 8729 2657 2339 -796 C HETATM 3450 O4' FMN A1202 51.443 -21.655 -57.645 1.00112.25 O ANISOU 3450 O4' FMN A1202 17155 16622 8873 2531 2564 -795 O HETATM 3451 C5' FMN A1202 49.715 -23.202 -58.331 1.00108.16 C ANISOU 3451 C5' FMN A1202 17059 15681 8356 2975 2136 -875 C HETATM 3452 O5' FMN A1202 48.814 -23.536 -57.274 1.00103.86 O ANISOU 3452 O5' FMN A1202 16425 15021 8015 2957 1844 -870 O HETATM 3453 P FMN A1202 47.945 -24.896 -57.315 1.00101.98 P ANISOU 3453 P FMN A1202 16325 14591 7831 3193 1589 -962 P HETATM 3454 O1P FMN A1202 46.664 -24.775 -58.036 1.00100.87 O ANISOU 3454 O1P FMN A1202 16530 14215 7582 3226 1409 -1023 O HETATM 3455 O2P FMN A1202 48.892 -26.031 -57.877 1.00105.61 O ANISOU 3455 O2P FMN A1202 16754 15152 8220 3466 1729 -1019 O HETATM 3456 O3P FMN A1202 47.731 -25.344 -55.813 1.00 99.64 O ANISOU 3456 O3P FMN A1202 15772 14308 7779 3123 1411 -945 O CONECT 701 1207 CONECT 1207 701 CONECT 3393 3394 CONECT 3394 3393 3395 3396 CONECT 3395 3394 CONECT 3396 3394 3397 3407 CONECT 3397 3396 3398 CONECT 3398 3397 3399 3402 CONECT 3399 3398 3400 3401 CONECT 3400 3399 CONECT 3401 3399 CONECT 3402 3398 3403 CONECT 3403 3402 3404 3407 CONECT 3404 3403 3405 3406 CONECT 3405 3404 CONECT 3406 3404 CONECT 3407 3396 3403 3408 CONECT 3408 3407 3409 3410 CONECT 3409 3408 3412 CONECT 3410 3408 3411 CONECT 3411 3410 3412 CONECT 3412 3409 3411 3413 CONECT 3413 3412 3414 3419 CONECT 3414 3413 3415 CONECT 3415 3414 3416 CONECT 3416 3415 3417 3418 CONECT 3417 3416 CONECT 3418 3416 CONECT 3419 3413 3420 CONECT 3420 3419 3421 3425 CONECT 3421 3420 3422 CONECT 3422 3421 3423 CONECT 3423 3422 3424 CONECT 3424 3423 3425 CONECT 3425 3420 3424 CONECT 3426 3427 3443 CONECT 3427 3426 3428 3429 CONECT 3428 3427 CONECT 3429 3427 3430 CONECT 3430 3429 3431 3432 CONECT 3431 3430 CONECT 3432 3430 3433 3443 CONECT 3433 3432 3434 CONECT 3434 3433 3435 3441 CONECT 3435 3434 3436 CONECT 3436 3435 3437 3438 CONECT 3437 3436 CONECT 3438 3436 3439 3440 CONECT 3439 3438 CONECT 3440 3438 3441 CONECT 3441 3434 3440 3442 CONECT 3442 3441 3443 3444 CONECT 3443 3426 3432 3442 CONECT 3444 3442 3445 CONECT 3445 3444 3446 3447 CONECT 3446 3445 CONECT 3447 3445 3448 3449 CONECT 3448 3447 CONECT 3449 3447 3450 3451 CONECT 3450 3449 CONECT 3451 3449 3452 CONECT 3452 3451 3453 CONECT 3453 3452 3454 3455 3456 CONECT 3454 3453 CONECT 3455 3453 CONECT 3456 3453 MASTER 330 0 2 15 14 0 8 6 3450 1 66 36 END