HEADER MEMBRANE PROTEIN 06-JUN-22 8A2O TITLE ROOM-TEMPERATURE STRUCTURE OF THE STABILISED A2A-THEOPHYLLINE COMPLEX TITLE 2 DETERMINED BY SYNCHROTRON SERIAL CRYSTALLOGRAPHY COMPND MOL_ID: 1; COMPND 2 MOLECULE: ADENOSINE RECEPTOR A2A,SOLUBLE CYTOCHROME B562; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: CYTOCHROME B-562; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: ADORA2A, ADORA2, CYBC; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: BAC TO BAC KEYWDS ADENOSINE RECEPTOR A2A, SOLUBLE CYTOCHROME B562, MEMBRANE PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR I.MORAES,T.O.C.KWAN,D.AXFORD REVDAT 2 18-OCT-23 8A2O 1 JRNL REVDAT 1 30-AUG-23 8A2O 0 JRNL AUTH J.BIRCH,T.O.C.KWAN,P.J.JUDGE,D.AXFORD,P.ALLER,A.BUTRYN, JRNL AUTH 2 R.I.REIS,J.F.BADA JUAREZ,J.VINALS,R.L.OWEN,E.NANGO,R.TANAKA, JRNL AUTH 3 K.TONO,Y.JOTI,T.TANAKA,S.OWADA,M.SUGAHARA,S.IWATA, JRNL AUTH 4 A.M.ORVILLE,A.WATTS,I.MORAES JRNL TITL A VERSATILE APPROACH TO HIGH-DENSITY MICROCRYSTALS IN JRNL TITL 2 LIPIDIC CUBIC PHASE FOR ROOM-TEMPERATURE SERIAL JRNL TITL 3 CRYSTALLOGRAPHY. JRNL REF J.APPL.CRYSTALLOGR. V. 56 1361 2023 JRNL REFN ISSN 0021-8898 JRNL PMID 37791355 JRNL DOI 10.1107/S1600576723006428 REMARK 2 REMARK 2 RESOLUTION. 3.45 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0258 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.45 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.63 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 3 NUMBER OF REFLECTIONS : 7034 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) : 0.220 REMARK 3 R VALUE (WORKING SET) : 0.219 REMARK 3 FREE R VALUE : 0.241 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 370 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.45 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.54 REMARK 3 REFLECTION IN BIN (WORKING SET) : 489 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.31 REMARK 3 BIN R VALUE (WORKING SET) : 0.3320 REMARK 3 BIN FREE R VALUE SET COUNT : 33 REMARK 3 BIN FREE R VALUE : 0.2830 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 2986 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 176 REMARK 3 SOLVENT ATOMS : 20 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 88.00 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 129.7 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.25000 REMARK 3 B22 (A**2) : -0.25000 REMARK 3 B33 (A**2) : 0.00000 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 OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 0.571 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.423 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 26.482 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.940 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.937 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3239 ; 0.002 ; 0.012 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4401 ; 0.638 ; 1.623 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 384 ; 4.228 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 144 ;32.714 ;21.597 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 500 ;13.587 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;15.118 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 441 ; 0.065 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2326 ; 0.002 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : NULL 0 NULL 0 REMARK 3 ORIGIN FOR THE GROUP (A): -17.0690 -17.1710 18.8370 REMARK 3 T TENSOR REMARK 3 T11: 0.3414 T22: 0.3647 REMARK 3 T33: 0.4003 T12: -0.0098 REMARK 3 T13: 0.0282 T23: 0.0010 REMARK 3 L TENSOR REMARK 3 L11: 0.1364 L22: 0.2423 REMARK 3 L33: 0.1508 L12: 0.0227 REMARK 3 L13: 0.1128 L23: 0.0988 REMARK 3 S TENSOR REMARK 3 S11: -0.0245 S12: -0.0368 S13: -0.0240 REMARK 3 S21: -0.0623 S22: 0.0253 S23: -0.1880 REMARK 3 S31: -0.0517 S32: -0.0606 S33: -0.0007 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: U VALUES : WITH TLS ADDED HYDROGENS REMARK 3 HAVE BEEN USED IF PRESENT IN THE INPUT REMARK 4 REMARK 4 8A2O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-JUN-22. REMARK 100 THE DEPOSITION ID IS D_1292123458. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 10-OCT-19 REMARK 200 TEMPERATURE (KELVIN) : 293 REMARK 200 PH : 4.0-5.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I24 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.96862 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DIALS 1.10.1 REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 7416 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.450 REMARK 200 RESOLUTION RANGE LOW (A) : 23.630 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4 REMARK 200 DATA REDUNDANCY : 233.6 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.6400 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.45 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.54 REMARK 200 COMPLETENESS FOR SHELL (%) : 96.9 REMARK 200 DATA REDUNDANCY IN SHELL : 17.30 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.480 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER V3.24 REMARK 200 STARTING MODEL: 5MZJ REMARK 200 REMARK 200 REMARK: PLATES REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 58.02 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.93 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRI-SODIUM CITRATE PH 4.5, 0.05 REMARK 280 M SODIUM THIOCYANATE, 29% (V/V) POLYETHYLENE GLYCOL 400, 2% (V/V) REMARK 280 2,5-HEXANEDIOL, LIPIDIC CUBIC PHASE, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -X,Y,-Z+1/2 REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 72.13350 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 72.13350 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 20.26550 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 91.15550 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 20.26550 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 91.15550 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 72.13350 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 20.26550 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 91.15550 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 72.13350 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 20.26550 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 91.15550 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 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 ALA A 1043 REMARK 465 THR A 1044 REMARK 465 PRO A 1045 REMARK 465 PRO A 1046 REMARK 465 LYS A 1047 REMARK 465 LEU A 1048 REMARK 465 GLU A 1049 REMARK 465 ASP A 1050 REMARK 465 LYS A 1051 REMARK 465 SER A 1052 REMARK 465 PRO A 1053 REMARK 465 ASP A 1054 REMARK 465 SER A 1055 REMARK 465 PRO A 1056 REMARK 465 GLU A 1057 REMARK 465 MET A 1058 REMARK 465 HIS A 306 REMARK 465 VAL A 307 REMARK 465 LEU A 308 REMARK 465 ARG A 309 REMARK 465 GLN A 310 REMARK 465 GLN A 311 REMARK 465 GLU A 312 REMARK 465 PRO A 313 REMARK 465 PHE A 314 REMARK 465 LYS A 315 REMARK 465 ALA A 316 REMARK 465 HIS A 317 REMARK 465 HIS A 318 REMARK 465 HIS A 319 REMARK 465 HIS A 320 REMARK 465 HIS A 321 REMARK 465 HIS A 322 REMARK 465 HIS A 323 REMARK 465 HIS A 324 REMARK 465 HIS A 325 REMARK 465 HIS A 326 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 LEU A 58 -51.71 -128.86 REMARK 500 VAL A 178 -62.27 -91.73 REMARK 500 TYR A1101 -48.69 -135.88 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 OLC A 2406 REMARK 610 OLC A 2407 REMARK 610 OLA A 2408 REMARK 610 OLA A 2409 REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA A2410 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 52 OD1 REMARK 620 2 SER A 91 OG 118.0 REMARK 620 N 1 DBREF 8A2O A 2 208 UNP P29274 AA2AR_HUMAN 2 208 DBREF 8A2O A 1001 1106 UNP P0ABE7 C562_ECOLX 23 128 DBREF 8A2O A 219 316 UNP P29274 AA2AR_HUMAN 219 316 SEQADV 8A2O ALA A 0 UNP P29274 EXPRESSION TAG SEQADV 8A2O PRO A 1 UNP P29274 EXPRESSION TAG SEQADV 8A2O LEU A 54 UNP P29274 ALA 54 ENGINEERED MUTATION SEQADV 8A2O ALA A 88 UNP P29274 THR 88 ENGINEERED MUTATION SEQADV 8A2O ALA A 107 UNP P29274 ARG 107 ENGINEERED MUTATION SEQADV 8A2O ALA A 122 UNP P29274 LYS 122 ENGINEERED MUTATION SEQADV 8A2O ALA A 154 UNP P29274 ASN 154 ENGINEERED MUTATION SEQADV 8A2O ALA A 202 UNP P29274 LEU 202 ENGINEERED MUTATION SEQADV 8A2O TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION SEQADV 8A2O ILE A 1102 UNP P0ABE7 HIS 124 ENGINEERED MUTATION SEQADV 8A2O LEU A 1106 UNP P0ABE7 ARG 128 ENGINEERED MUTATION SEQADV 8A2O ALA A 235 UNP P29274 LEU 235 ENGINEERED MUTATION SEQADV 8A2O ALA A 239 UNP P29274 VAL 239 ENGINEERED MUTATION SEQADV 8A2O ALA A 277 UNP P29274 SER 277 ENGINEERED MUTATION SEQADV 8A2O HIS A 317 UNP P29274 EXPRESSION TAG SEQADV 8A2O HIS A 318 UNP P29274 EXPRESSION TAG SEQADV 8A2O HIS A 319 UNP P29274 EXPRESSION TAG SEQADV 8A2O HIS A 320 UNP P29274 EXPRESSION TAG SEQADV 8A2O HIS A 321 UNP P29274 EXPRESSION TAG SEQADV 8A2O HIS A 322 UNP P29274 EXPRESSION TAG SEQADV 8A2O HIS A 323 UNP P29274 EXPRESSION TAG SEQADV 8A2O HIS A 324 UNP P29274 EXPRESSION TAG SEQADV 8A2O HIS A 325 UNP P29274 EXPRESSION TAG SEQADV 8A2O HIS A 326 UNP P29274 EXPRESSION TAG SEQRES 1 A 423 ALA PRO PRO ILE MET GLY SER SER VAL TYR ILE THR VAL SEQRES 2 A 423 GLU LEU ALA ILE ALA VAL LEU ALA ILE LEU GLY ASN VAL SEQRES 3 A 423 LEU VAL CYS TRP ALA VAL TRP LEU ASN SER ASN LEU GLN SEQRES 4 A 423 ASN VAL THR ASN TYR PHE VAL VAL SER LEU ALA ALA ALA SEQRES 5 A 423 ASP ILE LEU VAL GLY VAL LEU ALA ILE PRO PHE ALA ILE SEQRES 6 A 423 THR ILE SER THR GLY PHE CYS ALA ALA CYS HIS GLY CYS SEQRES 7 A 423 LEU PHE ILE ALA CYS PHE VAL LEU VAL LEU ALA GLN SER SEQRES 8 A 423 SER ILE PHE SER LEU LEU ALA ILE ALA ILE ASP ARG TYR SEQRES 9 A 423 ILE ALA ILE ALA ILE PRO LEU ARG TYR ASN GLY LEU VAL SEQRES 10 A 423 THR GLY THR ARG ALA ALA GLY ILE ILE ALA ILE CYS TRP SEQRES 11 A 423 VAL LEU SER PHE ALA ILE GLY LEU THR PRO MET LEU GLY SEQRES 12 A 423 TRP ASN ASN CYS GLY GLN PRO LYS GLU GLY LYS ALA HIS SEQRES 13 A 423 SER GLN GLY CYS GLY GLU GLY GLN VAL ALA CYS LEU PHE SEQRES 14 A 423 GLU ASP VAL VAL PRO MET ASN TYR MET VAL TYR PHE ASN SEQRES 15 A 423 PHE PHE ALA CYS VAL LEU VAL PRO LEU LEU LEU MET LEU SEQRES 16 A 423 GLY VAL TYR LEU ARG ILE PHE ALA ALA ALA ARG ARG GLN SEQRES 17 A 423 LEU ALA ASP LEU GLU ASP ASN TRP GLU THR LEU ASN ASP SEQRES 18 A 423 ASN LEU LYS VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN SEQRES 19 A 423 VAL LYS ASP ALA LEU THR LYS MET ARG ALA ALA ALA LEU SEQRES 20 A 423 ASP ALA GLN LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SEQRES 21 A 423 SER PRO ASP SER PRO GLU MET LYS ASP PHE ARG HIS GLY SEQRES 22 A 423 PHE ASP ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS SEQRES 23 A 423 LEU ALA ASN GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA SEQRES 24 A 423 ALA GLU GLN LEU LYS THR THR ARG ASN ALA TYR ILE GLN SEQRES 25 A 423 LYS TYR LEU GLU ARG ALA ARG SER THR LEU GLN LYS GLU SEQRES 26 A 423 VAL HIS ALA ALA LYS SER ALA ALA ILE ILE ALA GLY LEU SEQRES 27 A 423 PHE ALA LEU CYS TRP LEU PRO LEU HIS ILE ILE ASN CYS SEQRES 28 A 423 PHE THR PHE PHE CYS PRO ASP CYS SER HIS ALA PRO LEU SEQRES 29 A 423 TRP LEU MET TYR LEU ALA ILE VAL LEU ALA HIS THR ASN SEQRES 30 A 423 SER VAL VAL ASN PRO PHE ILE TYR ALA TYR ARG ILE ARG SEQRES 31 A 423 GLU PHE ARG GLN THR PHE ARG LYS ILE ILE ARG SER HIS SEQRES 32 A 423 VAL LEU ARG GLN GLN GLU PRO PHE LYS ALA HIS HIS HIS SEQRES 33 A 423 HIS HIS HIS HIS HIS HIS HIS HET TEP A2401 13 HET CLR A2402 28 HET CLR A2403 28 HET CLR A2404 28 HET OLA A2405 20 HET OLC A2406 23 HET OLC A2407 16 HET OLA A2408 8 HET OLA A2409 11 HET NA A2410 1 HETNAM TEP THEOPHYLLINE HETNAM CLR CHOLESTEROL HETNAM OLA OLEIC ACID HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETNAM NA SODIUM ION HETSYN OLC 1-OLEOYL-R-GLYCEROL FORMUL 2 TEP C7 H8 N4 O2 FORMUL 3 CLR 3(C27 H46 O) FORMUL 6 OLA 3(C18 H34 O2) FORMUL 7 OLC 2(C21 H40 O4) FORMUL 11 NA NA 1+ FORMUL 12 HOH *20(H2 O) HELIX 1 AA1 PRO A 1 ASN A 34 1 34 HELIX 2 AA2 ASN A 39 LEU A 58 1 20 HELIX 3 AA3 LEU A 58 GLY A 69 1 12 HELIX 4 AA4 CYS A 74 ILE A 108 1 35 HELIX 5 AA5 ARG A 111 VAL A 116 1 6 HELIX 6 AA6 THR A 117 LEU A 137 1 21 HELIX 7 AA7 THR A 138 GLY A 142 5 5 HELIX 8 AA8 LYS A 150 GLN A 157 1 8 HELIX 9 AA9 LEU A 167 VAL A 172 1 6 HELIX 10 AB1 PRO A 173 TYR A 179 1 7 HELIX 11 AB2 VAL A 186 LEU A 208 1 23 HELIX 12 AB3 ASP A 1002 LYS A 1019 1 18 HELIX 13 AB4 ASN A 1022 LYS A 1042 1 21 HELIX 14 AB5 ASP A 1060 GLY A 1082 1 23 HELIX 15 AB6 LYS A 1083 ALA A 1091 1 9 HELIX 16 AB7 GLN A 1093 LEU A 1106 1 14 HELIX 17 AB8 ARG A 220 CYS A 259 1 40 HELIX 18 AB9 PRO A 266 THR A 279 1 14 HELIX 19 AC1 THR A 279 ILE A 292 1 14 HELIX 20 AC2 ILE A 292 ARG A 304 1 13 SHEET 1 AA1 2 CYS A 71 ALA A 73 0 SHEET 2 AA1 2 GLN A 163 ALA A 165 -1 O VAL A 164 N ALA A 72 SSBOND 1 CYS A 71 CYS A 159 1555 1555 2.03 SSBOND 2 CYS A 74 CYS A 146 1555 1555 2.03 SSBOND 3 CYS A 77 CYS A 166 1555 1555 2.03 SSBOND 4 CYS A 259 CYS A 262 1555 1555 2.03 LINK OD1 ASP A 52 NA NA A2410 1555 1555 2.57 LINK OG SER A 91 NA NA A2410 1555 1555 3.02 CRYST1 40.531 182.311 144.267 90.00 90.00 90.00 C 2 2 21 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.024672 0.000000 0.000000 0.00000 SCALE2 0.000000 0.005485 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006932 0.00000 ATOM 1 N ALA A 0 -22.437 23.808 1.259 1.00184.30 N ANISOU 1 N ALA A 0 24778 22449 22798 80 -190 -102 N ATOM 2 CA ALA A 0 -23.031 22.532 0.694 1.00184.77 C ANISOU 2 CA ALA A 0 24830 22547 22827 77 -149 -102 C ATOM 3 C ALA A 0 -24.247 22.104 1.514 1.00185.10 C ANISOU 3 C ALA A 0 24832 22655 22842 131 -199 -128 C ATOM 4 O ALA A 0 -24.237 22.231 2.737 1.00187.34 O ANISOU 4 O ALA A 0 25060 22968 23153 160 -235 -142 O ATOM 5 CB ALA A 0 -21.997 21.435 0.637 1.00183.06 C ANISOU 5 CB ALA A 0 24563 22332 22658 36 -69 -87 C ATOM 6 N PRO A 1 -25.330 21.604 0.868 1.00184.12 N ANISOU 6 N PRO A 1 24736 22557 22664 146 -203 -135 N ATOM 7 CA PRO A 1 -26.515 21.126 1.585 1.00181.28 C ANISOU 7 CA PRO A 1 24338 22263 22278 195 -246 -160 C ATOM 8 C PRO A 1 -26.191 19.963 2.522 1.00178.07 C ANISOU 8 C PRO A 1 23843 21905 21911 196 -215 -161 C ATOM 9 O PRO A 1 -25.509 19.018 2.128 1.00176.84 O ANISOU 9 O PRO A 1 23667 21744 21779 159 -148 -145 O ATOM 10 CB PRO A 1 -27.464 20.659 0.469 1.00180.86 C ANISOU 10 CB PRO A 1 24334 22217 22167 196 -236 -161 C ATOM 11 CG PRO A 1 -26.989 21.404 -0.761 1.00183.00 C ANISOU 11 CG PRO A 1 24688 22420 22423 161 -217 -142 C ATOM 12 CD PRO A 1 -25.487 21.510 -0.593 1.00184.05 C ANISOU 12 CD PRO A 1 24800 22516 22616 118 -169 -121 C ATOM 13 N PRO A 2 -26.652 20.013 3.794 1.00175.07 N ANISOU 13 N PRO A 2 23408 21572 21539 237 -264 -182 N ATOM 14 CA PRO A 2 -26.373 18.955 4.767 1.00172.71 C ANISOU 14 CA PRO A 2 23027 21319 21276 239 -240 -183 C ATOM 15 C PRO A 2 -27.116 17.650 4.485 1.00170.15 C ANISOU 15 C PRO A 2 22681 21043 20925 242 -212 -186 C ATOM 16 O PRO A 2 -26.600 16.572 4.773 1.00172.53 O ANISOU 16 O PRO A 2 22930 21363 21258 223 -165 -177 O ATOM 17 CB PRO A 2 -26.864 19.539 6.104 1.00172.81 C ANISOU 17 CB PRO A 2 23000 21368 21291 287 -309 -207 C ATOM 18 CG PRO A 2 -27.056 21.019 5.839 1.00174.46 C ANISOU 18 CG PRO A 2 23270 21536 21480 302 -363 -214 C ATOM 19 CD PRO A 2 -27.434 21.112 4.377 1.00175.16 C ANISOU 19 CD PRO A 2 23435 21593 21526 283 -344 -205 C ATOM 20 N ILE A 3 -28.323 17.763 3.916 1.00165.48 N ANISOU 20 N ILE A 3 22131 20468 20277 266 -242 -199 N ATOM 21 CA ILE A 3 -29.220 16.627 3.754 1.00160.38 C ANISOU 21 CA ILE A 3 21464 19871 19601 277 -228 -206 C ATOM 22 C ILE A 3 -28.730 15.714 2.629 1.00157.26 C ANISOU 22 C ILE A 3 21089 19454 19209 232 -155 -185 C ATOM 23 O ILE A 3 -29.022 14.520 2.638 1.00155.87 O ANISOU 23 O ILE A 3 20878 19315 19030 229 -124 -184 O ATOM 24 CB ILE A 3 -30.684 17.085 3.559 1.00159.59 C ANISOU 24 CB ILE A 3 21399 19797 19441 319 -288 -231 C ATOM 25 CG1 ILE A 3 -31.675 15.929 3.732 1.00158.15 C ANISOU 25 CG1 ILE A 3 21180 19678 19234 338 -283 -243 C ATOM 26 CG2 ILE A 3 -30.870 17.808 2.231 1.00160.07 C ANISOU 26 CG2 ILE A 3 21548 19805 19465 307 -291 -224 C ATOM 27 CD1 ILE A 3 -33.106 16.365 3.960 1.00157.33 C ANISOU 27 CD1 ILE A 3 21087 19611 19082 387 -350 -272 C ATOM 28 N MET A 4 -27.980 16.280 1.675 1.00155.83 N ANISOU 28 N MET A 4 20964 19211 19032 198 -126 -167 N ATOM 29 CA MET A 4 -27.529 15.539 0.506 1.00154.48 C ANISOU 29 CA MET A 4 20821 19014 18860 156 -58 -148 C ATOM 30 C MET A 4 -26.542 14.452 0.924 1.00150.66 C ANISOU 30 C MET A 4 20272 18542 18430 127 1 -135 C ATOM 31 O MET A 4 -26.689 13.297 0.527 1.00150.05 O ANISOU 31 O MET A 4 20178 18486 18349 114 43 -131 O ATOM 32 CB MET A 4 -26.883 16.461 -0.533 1.00159.86 C ANISOU 32 CB MET A 4 21576 19627 19535 124 -41 -132 C ATOM 33 CG MET A 4 -27.887 17.323 -1.279 1.00165.27 C ANISOU 33 CG MET A 4 22339 20296 20161 145 -90 -141 C ATOM 34 SD MET A 4 -27.190 18.123 -2.748 1.00173.56 S ANISOU 34 SD MET A 4 23484 21267 21196 100 -57 -119 S ATOM 35 CE MET A 4 -27.092 16.734 -3.878 1.00170.38 C ANISOU 35 CE MET A 4 23089 20868 20779 64 23 -105 C ATOM 36 N GLY A 5 -25.549 14.832 1.738 1.00145.87 N ANISOU 36 N GLY A 5 19628 17919 17876 118 2 -131 N ATOM 37 CA GLY A 5 -24.598 13.886 2.300 1.00138.35 C ANISOU 37 CA GLY A 5 18608 16977 16980 95 50 -121 C ATOM 38 C GLY A 5 -25.272 12.879 3.231 1.00132.88 C ANISOU 38 C GLY A 5 17851 16352 16287 123 35 -134 C ATOM 39 O GLY A 5 -24.824 11.739 3.344 1.00131.16 O ANISOU 39 O GLY A 5 17588 16150 16099 104 80 -126 O ATOM 40 N ASER A 6 -26.355 13.320 3.881 0.65130.94 N ANISOU 40 N ASER A 6 17602 16143 16007 168 -30 -153 N ATOM 41 N BSER A 6 -26.353 13.321 3.884 0.35130.88 N ANISOU 41 N BSER A 6 17594 16136 16000 168 -30 -153 N ATOM 42 CA ASER A 6 -27.103 12.503 4.824 0.65129.07 C ANISOU 42 CA ASER A 6 17306 15972 15764 197 -51 -167 C ATOM 43 CA BSER A 6 -27.102 12.501 4.824 0.35128.65 C ANISOU 43 CA BSER A 6 17253 15918 15711 197 -51 -166 C ATOM 44 C ASER A 6 -27.958 11.474 4.089 0.65126.48 C ANISOU 44 C ASER A 6 16987 15672 15398 196 -28 -168 C ATOM 45 C BSER A 6 -27.946 11.466 4.084 0.35126.27 C ANISOU 45 C BSER A 6 16961 15645 15371 196 -27 -167 C ATOM 46 O ASER A 6 -28.290 10.433 4.652 0.65125.96 O ANISOU 46 O ASER A 6 16869 15653 15337 204 -20 -171 O ATOM 47 O BSER A 6 -28.258 10.415 4.639 0.35125.70 O ANISOU 47 O BSER A 6 16836 15620 15305 203 -18 -170 O ATOM 48 CB ASER A 6 -27.941 13.363 5.736 0.65130.44 C ANISOU 48 CB ASER A 6 17473 16175 15915 245 -125 -189 C ATOM 49 CB BSER A 6 -27.953 13.357 5.727 0.35129.49 C ANISOU 49 CB BSER A 6 17353 16055 15794 245 -125 -189 C ATOM 50 OG ASER A 6 -27.118 14.170 6.566 0.65132.04 O ANISOU 50 OG ASER A 6 17655 16356 16157 247 -146 -188 O ATOM 51 OG BSER A 6 -28.781 12.552 6.553 0.35130.10 O ANISOU 51 OG BSER A 6 17377 16197 15858 272 -144 -202 O ATOM 52 N SER A 7 -28.305 11.777 2.831 1.00124.70 N ANISOU 52 N SER A 7 16830 15416 15134 186 -18 -164 N ATOM 53 CA SER A 7 -29.166 10.923 2.024 1.00120.08 C ANISOU 53 CA SER A 7 16264 14854 14509 187 -1 -166 C ATOM 54 C SER A 7 -28.507 9.572 1.755 1.00114.51 C ANISOU 54 C SER A 7 15523 14151 13833 152 67 -151 C ATOM 55 O SER A 7 -29.187 8.549 1.737 1.00111.15 O ANISOU 55 O SER A 7 15074 13766 13391 160 76 -155 O ATOM 56 CB SER A 7 -29.561 11.599 0.738 1.00121.63 C ANISOU 56 CB SER A 7 16544 15011 14660 182 -5 -165 C ATOM 57 OG SER A 7 -30.227 12.824 1.002 1.00125.72 O ANISOU 57 OG SER A 7 17093 15526 15149 216 -72 -181 O ATOM 58 N VAL A 8 -27.184 9.588 1.556 1.00110.93 N ANISOU 58 N VAL A 8 15067 13656 13427 115 114 -134 N ATOM 59 CA VAL A 8 -26.418 8.381 1.290 1.00107.33 C ANISOU 59 CA VAL A 8 14577 13197 13006 80 179 -120 C ATOM 60 C VAL A 8 -26.371 7.528 2.556 1.00104.66 C ANISOU 60 C VAL A 8 14157 12906 12701 93 172 -124 C ATOM 61 O VAL A 8 -26.582 6.318 2.493 1.00102.12 O ANISOU 61 O VAL A 8 13806 12613 12381 87 199 -122 O ATOM 62 CB VAL A 8 -25.005 8.705 0.761 1.00106.71 C ANISOU 62 CB VAL A 8 14515 13059 12969 37 229 -103 C ATOM 63 CG1 VAL A 8 -24.148 7.457 0.601 1.00105.86 C ANISOU 63 CG1 VAL A 8 14366 12951 12905 3 294 -92 C ATOM 64 CG2 VAL A 8 -25.056 9.483 -0.546 1.00106.86 C ANISOU 64 CG2 VAL A 8 14618 13031 12952 21 239 -97 C ATOM 65 N TYR A 9 -26.109 8.178 3.698 1.00103.18 N ANISOU 65 N TYR A 9 13938 12727 12539 112 133 -130 N ATOM 66 CA TYR A 9 -25.952 7.492 4.972 1.00101.30 C ANISOU 66 CA TYR A 9 13625 12530 12335 123 124 -133 C ATOM 67 C TYR A 9 -27.231 6.739 5.333 1.00 99.54 C ANISOU 67 C TYR A 9 13379 12368 12073 152 99 -145 C ATOM 68 O TYR A 9 -27.168 5.588 5.757 1.00 99.78 O ANISOU 68 O TYR A 9 13360 12429 12123 145 120 -141 O ATOM 69 CB TYR A 9 -25.517 8.461 6.078 1.00101.22 C ANISOU 69 CB TYR A 9 13592 12514 12352 140 82 -139 C ATOM 70 CG TYR A 9 -25.657 7.919 7.480 1.00100.71 C ANISOU 70 CG TYR A 9 13458 12500 12308 162 57 -146 C ATOM 71 CD1 TYR A 9 -24.772 6.974 7.978 1.00 99.99 C ANISOU 71 CD1 TYR A 9 13312 12410 12268 140 93 -135 C ATOM 72 CD2 TYR A 9 -26.685 8.344 8.307 1.00 99.87 C ANISOU 72 CD2 TYR A 9 13341 12438 12169 204 -3 -164 C ATOM 73 CE1 TYR A 9 -24.902 6.468 9.262 1.00 99.30 C ANISOU 73 CE1 TYR A 9 13164 12368 12198 158 68 -141 C ATOM 74 CE2 TYR A 9 -26.830 7.847 9.593 1.00 99.08 C ANISOU 74 CE2 TYR A 9 13179 12384 12084 222 -26 -170 C ATOM 75 CZ TYR A 9 -25.936 6.906 10.072 1.00 99.08 C ANISOU 75 CZ TYR A 9 13127 12385 12134 199 10 -157 C ATOM 76 OH TYR A 9 -26.077 6.418 11.339 1.00 99.61 O ANISOU 76 OH TYR A 9 13137 12496 12214 216 -13 -162 O ATOM 77 N ILE A 10 -28.382 7.397 5.155 1.00 97.08 N ANISOU 77 N ILE A 10 13104 12073 11708 183 52 -160 N ATOM 78 CA ILE A 10 -29.663 6.818 5.526 1.00 95.95 C ANISOU 78 CA ILE A 10 12940 11990 11527 213 23 -175 C ATOM 79 C ILE A 10 -29.966 5.629 4.615 1.00 95.86 C ANISOU 79 C ILE A 10 12936 11987 11501 193 67 -167 C ATOM 80 O ILE A 10 -30.510 4.627 5.074 1.00 95.81 O ANISOU 80 O ILE A 10 12887 12027 11489 201 68 -170 O ATOM 81 CB ILE A 10 -30.785 7.881 5.523 1.00 95.82 C ANISOU 81 CB ILE A 10 12961 11987 11460 251 -39 -195 C ATOM 82 CG1 ILE A 10 -30.518 8.981 6.555 1.00 94.79 C ANISOU 82 CG1 ILE A 10 12816 11854 11346 274 -86 -205 C ATOM 83 CG2 ILE A 10 -32.153 7.241 5.728 1.00 95.52 C ANISOU 83 CG2 ILE A 10 12905 12008 11380 279 -64 -211 C ATOM 84 CD1 ILE A 10 -31.473 10.150 6.481 1.00 94.81 C ANISOU 84 CD1 ILE A 10 12861 11860 11303 310 -146 -226 C ATOM 85 N THR A 11 -29.586 5.740 3.335 1.00 96.26 N ANISOU 85 N THR A 11 13040 11990 11543 166 104 -157 N ATOM 86 CA THR A 11 -29.870 4.705 2.351 1.00 95.39 C ANISOU 86 CA THR A 11 12945 11883 11416 148 146 -150 C ATOM 87 C THR A 11 -29.073 3.440 2.665 1.00 95.16 C ANISOU 87 C THR A 11 12860 11862 11435 121 194 -138 C ATOM 88 O THR A 11 -29.608 2.336 2.580 1.00 94.50 O ANISOU 88 O THR A 11 12754 11811 11340 121 208 -138 O ATOM 89 CB THR A 11 -29.619 5.191 0.917 1.00 94.67 C ANISOU 89 CB THR A 11 12928 11738 11305 125 174 -143 C ATOM 90 OG1 THR A 11 -30.140 6.514 0.789 1.00 95.09 O ANISOU 90 OG1 THR A 11 13030 11776 11323 149 124 -154 O ATOM 91 CG2 THR A 11 -30.256 4.298 -0.125 1.00 93.78 C ANISOU 91 CG2 THR A 11 12841 11633 11158 117 201 -142 C ATOM 92 N VAL A 12 -27.796 3.614 3.026 1.00 94.82 N ANISOU 92 N VAL A 12 12795 11788 11445 99 219 -127 N ATOM 93 CA VAL A 12 -26.927 2.494 3.352 1.00 94.42 C ANISOU 93 CA VAL A 12 12692 11740 11445 73 262 -116 C ATOM 94 C VAL A 12 -27.412 1.845 4.648 1.00 94.25 C ANISOU 94 C VAL A 12 12605 11774 11431 96 232 -122 C ATOM 95 O VAL A 12 -27.440 0.620 4.751 1.00 95.38 O ANISOU 95 O VAL A 12 12713 11941 11587 86 256 -117 O ATOM 96 CB VAL A 12 -25.444 2.915 3.421 1.00 94.63 C ANISOU 96 CB VAL A 12 12710 11718 11528 45 293 -105 C ATOM 97 CG1 VAL A 12 -24.534 1.762 3.822 1.00 93.95 C ANISOU 97 CG1 VAL A 12 12566 11634 11497 21 334 -96 C ATOM 98 CG2 VAL A 12 -24.971 3.525 2.110 1.00 95.29 C ANISOU 98 CG2 VAL A 12 12859 11747 11602 19 327 -98 C ATOM 99 N GLU A 13 -27.821 2.676 5.616 1.00 93.05 N ANISOU 99 N GLU A 13 12441 11645 11269 127 178 -133 N ATOM 100 CA GLU A 13 -28.273 2.204 6.916 1.00 91.88 C ANISOU 100 CA GLU A 13 12235 11550 11126 150 145 -139 C ATOM 101 C GLU A 13 -29.507 1.318 6.761 1.00 90.64 C ANISOU 101 C GLU A 13 12070 11441 10926 164 138 -146 C ATOM 102 O GLU A 13 -29.602 0.276 7.408 1.00 89.96 O ANISOU 102 O GLU A 13 11934 11391 10855 162 144 -143 O ATOM 103 CB GLU A 13 -28.550 3.375 7.862 1.00 93.41 C ANISOU 103 CB GLU A 13 12425 11757 11311 182 88 -153 C ATOM 104 CG GLU A 13 -27.296 3.953 8.495 1.00 95.84 C ANISOU 104 CG GLU A 13 12713 12031 11671 171 90 -146 C ATOM 105 CD GLU A 13 -26.677 3.138 9.620 1.00 97.07 C ANISOU 105 CD GLU A 13 12800 12207 11873 165 97 -140 C ATOM 106 OE1 GLU A 13 -26.435 1.927 9.420 1.00 97.03 O ANISOU 106 OE1 GLU A 13 12771 12210 11887 143 135 -129 O ATOM 107 OE2 GLU A 13 -26.437 3.719 10.695 1.00 97.87 O ANISOU 107 OE2 GLU A 13 12876 12318 11992 182 61 -145 O ATOM 108 N LEU A 14 -30.439 1.739 5.897 1.00 89.95 N ANISOU 108 N LEU A 14 12034 11354 10788 177 124 -156 N ATOM 109 CA LEU A 14 -31.676 1.005 5.683 1.00 89.32 C ANISOU 109 CA LEU A 14 11952 11318 10666 192 113 -164 C ATOM 110 C LEU A 14 -31.383 -0.309 4.963 1.00 89.34 C ANISOU 110 C LEU A 14 11948 11315 10684 161 167 -151 C ATOM 111 O LEU A 14 -32.015 -1.322 5.252 1.00 90.34 O ANISOU 111 O LEU A 14 12041 11483 10801 165 167 -152 O ATOM 112 CB LEU A 14 -32.669 1.867 4.893 1.00 89.64 C ANISOU 112 CB LEU A 14 12053 11354 10651 214 83 -179 C ATOM 113 CG LEU A 14 -33.313 3.028 5.654 1.00 90.36 C ANISOU 113 CG LEU A 14 12148 11466 10720 252 20 -198 C ATOM 114 CD1 LEU A 14 -34.424 3.663 4.830 1.00 90.35 C ANISOU 114 CD1 LEU A 14 12202 11464 10662 274 -10 -214 C ATOM 115 CD2 LEU A 14 -33.851 2.582 7.007 1.00 90.54 C ANISOU 115 CD2 LEU A 14 12107 11550 10744 274 -10 -207 C ATOM 116 N ALA A 15 -30.414 -0.278 4.039 1.00 88.70 N ANISOU 116 N ALA A 15 11896 11180 10625 130 213 -138 N ATOM 117 CA ALA A 15 -30.009 -1.452 3.281 1.00 87.73 C ANISOU 117 CA ALA A 15 11769 11044 10518 100 267 -126 C ATOM 118 C ALA A 15 -29.406 -2.501 4.213 1.00 87.42 C ANISOU 118 C ALA A 15 11662 11026 10527 88 284 -118 C ATOM 119 O ALA A 15 -29.687 -3.690 4.071 1.00 86.16 O ANISOU 119 O ALA A 15 11480 10888 10368 79 303 -114 O ATOM 120 CB ALA A 15 -29.041 -1.058 2.194 1.00 87.36 C ANISOU 120 CB ALA A 15 11769 10938 10488 70 311 -117 C ATOM 121 N ILE A 16 -28.583 -2.039 5.165 1.00 88.69 N ANISOU 121 N ILE A 16 11792 11179 10729 87 273 -115 N ATOM 122 CA ILE A 16 -27.932 -2.907 6.136 1.00 89.39 C ANISOU 122 CA ILE A 16 11817 11282 10865 77 283 -107 C ATOM 123 C ILE A 16 -28.991 -3.542 7.038 1.00 89.19 C ANISOU 123 C ILE A 16 11753 11320 10816 101 248 -113 C ATOM 124 O ILE A 16 -28.901 -4.727 7.352 1.00 88.82 O ANISOU 124 O ILE A 16 11665 11292 10788 89 265 -105 O ATOM 125 CB ILE A 16 -26.847 -2.147 6.933 1.00 89.67 C ANISOU 125 CB ILE A 16 11832 11293 10947 74 275 -104 C ATOM 126 CG1 ILE A 16 -25.645 -1.794 6.052 1.00 89.47 C ANISOU 126 CG1 ILE A 16 11835 11206 10956 43 320 -96 C ATOM 127 CG2 ILE A 16 -26.421 -2.931 8.168 1.00 90.11 C ANISOU 127 CG2 ILE A 16 11821 11374 11044 73 268 -99 C ATOM 128 CD1 ILE A 16 -24.662 -0.834 6.691 1.00 90.36 C ANISOU 128 CD1 ILE A 16 11937 11288 11108 41 309 -95 C ATOM 129 N ALA A 17 -29.997 -2.745 7.425 1.00 88.05 N ANISOU 129 N ALA A 17 11621 11205 10628 133 199 -127 N ATOM 130 CA ALA A 17 -31.083 -3.194 8.283 1.00 87.38 C ANISOU 130 CA ALA A 17 11502 11182 10515 157 163 -135 C ATOM 131 C ALA A 17 -31.857 -4.333 7.622 1.00 87.69 C ANISOU 131 C ALA A 17 11543 11244 10530 150 183 -134 C ATOM 132 O ALA A 17 -32.266 -5.274 8.297 1.00 87.31 O ANISOU 132 O ALA A 17 11452 11239 10484 151 177 -131 O ATOM 133 CB ALA A 17 -31.988 -2.035 8.622 1.00 86.60 C ANISOU 133 CB ALA A 17 11424 11106 10374 193 111 -154 C ATOM 134 N VAL A 18 -32.046 -4.234 6.299 1.00 87.97 N ANISOU 134 N VAL A 18 11631 11252 10543 141 205 -135 N ATOM 135 CA VAL A 18 -32.802 -5.220 5.544 1.00 87.69 C ANISOU 135 CA VAL A 18 11603 11233 10481 135 222 -135 C ATOM 136 C VAL A 18 -32.063 -6.557 5.581 1.00 89.11 C ANISOU 136 C VAL A 18 11745 11407 10704 106 265 -119 C ATOM 137 O VAL A 18 -32.674 -7.591 5.848 1.00 89.40 O ANISOU 137 O VAL A 18 11752 11482 10733 106 263 -117 O ATOM 138 CB VAL A 18 -33.083 -4.750 4.102 1.00 87.07 C ANISOU 138 CB VAL A 18 11592 11121 10370 132 236 -139 C ATOM 139 CG1 VAL A 18 -33.634 -5.870 3.231 1.00 87.09 C ANISOU 139 CG1 VAL A 18 11603 11132 10354 121 262 -137 C ATOM 140 CG2 VAL A 18 -34.023 -3.555 4.077 1.00 86.91 C ANISOU 140 CG2 VAL A 18 11608 11112 10303 165 188 -157 C ATOM 141 N LEU A 19 -30.747 -6.516 5.336 1.00 89.87 N ANISOU 141 N LEU A 19 11843 11458 10847 80 301 -108 N ATOM 142 CA LEU A 19 -29.923 -7.715 5.297 1.00 90.53 C ANISOU 142 CA LEU A 19 11893 11528 10975 52 342 -95 C ATOM 143 C LEU A 19 -29.725 -8.268 6.708 1.00 92.31 C ANISOU 143 C LEU A 19 12055 11788 11232 55 323 -89 C ATOM 144 O LEU A 19 -29.503 -9.466 6.878 1.00 93.42 O ANISOU 144 O LEU A 19 12162 11938 11397 39 342 -80 O ATOM 145 CB LEU A 19 -28.578 -7.390 4.637 1.00 89.14 C ANISOU 145 CB LEU A 19 11737 11294 10840 25 385 -87 C ATOM 146 CG LEU A 19 -28.639 -6.910 3.187 1.00 88.01 C ANISOU 146 CG LEU A 19 11658 11113 10669 16 411 -90 C ATOM 147 CD1 LEU A 19 -27.239 -6.741 2.617 1.00 87.19 C ANISOU 147 CD1 LEU A 19 11566 10954 10610 -15 458 -83 C ATOM 148 CD2 LEU A 19 -29.449 -7.866 2.325 1.00 87.38 C ANISOU 148 CD2 LEU A 19 11594 11048 10557 13 426 -92 C ATOM 149 N ALA A 20 -29.805 -7.381 7.710 1.00 92.49 N ANISOU 149 N ALA A 20 12065 11826 11252 77 283 -95 N ATOM 150 CA ALA A 20 -29.650 -7.764 9.104 1.00 91.94 C ANISOU 150 CA ALA A 20 11939 11788 11206 83 260 -91 C ATOM 151 C ALA A 20 -30.835 -8.618 9.545 1.00 91.33 C ANISOU 151 C ALA A 20 11838 11769 11096 94 239 -93 C ATOM 152 O ALA A 20 -30.648 -9.681 10.134 1.00 90.80 O ANISOU 152 O ALA A 20 11728 11720 11053 82 246 -83 O ATOM 153 CB ALA A 20 -29.499 -6.539 9.973 1.00 91.37 C ANISOU 153 CB ALA A 20 11864 11718 11134 104 222 -99 C ATOM 154 N ILE A 21 -32.048 -8.144 9.241 1.00 92.60 N ANISOU 154 N ILE A 21 12025 11957 11201 117 213 -107 N ATOM 155 CA ILE A 21 -33.269 -8.791 9.697 1.00 94.74 C ANISOU 155 CA ILE A 21 12273 12286 11437 131 189 -112 C ATOM 156 C ILE A 21 -33.452 -10.116 8.958 1.00 95.06 C ANISOU 156 C ILE A 21 12312 12328 11480 110 222 -103 C ATOM 157 O ILE A 21 -33.662 -11.148 9.593 1.00 96.09 O ANISOU 157 O ILE A 21 12401 12490 11620 103 221 -95 O ATOM 158 CB ILE A 21 -34.492 -7.853 9.570 1.00 95.02 C ANISOU 158 CB ILE A 21 12338 12350 11416 163 150 -132 C ATOM 159 CG1 ILE A 21 -34.315 -6.573 10.394 1.00 94.85 C ANISOU 159 CG1 ILE A 21 12315 12329 11393 186 114 -142 C ATOM 160 CG2 ILE A 21 -35.777 -8.581 9.944 1.00 94.91 C ANISOU 160 CG2 ILE A 21 12300 12395 11366 175 130 -139 C ATOM 161 CD1 ILE A 21 -35.252 -5.449 10.007 1.00 94.62 C ANISOU 161 CD1 ILE A 21 12327 12308 11316 215 81 -163 C ATOM 162 N LEU A 22 -33.345 -10.083 7.622 1.00 93.22 N ANISOU 162 N LEU A 22 12122 12058 11239 99 252 -104 N ATOM 163 CA LEU A 22 -33.632 -11.247 6.797 1.00 92.23 C ANISOU 163 CA LEU A 22 12001 11932 11110 82 281 -98 C ATOM 164 C LEU A 22 -32.661 -12.384 7.108 1.00 91.27 C ANISOU 164 C LEU A 22 11840 11797 11041 54 312 -82 C ATOM 165 O LEU A 22 -33.089 -13.504 7.378 1.00 89.32 O ANISOU 165 O LEU A 22 11563 11580 10794 47 313 -76 O ATOM 166 CB LEU A 22 -33.574 -10.864 5.314 1.00 92.39 C ANISOU 166 CB LEU A 22 12080 11910 11112 75 308 -103 C ATOM 167 CG LEU A 22 -34.906 -10.478 4.670 1.00 92.83 C ANISOU 167 CG LEU A 22 12174 11988 11109 97 284 -118 C ATOM 168 CD1 LEU A 22 -34.706 -10.116 3.207 1.00 92.42 C ANISOU 168 CD1 LEU A 22 12183 11889 11043 88 312 -120 C ATOM 169 CD2 LEU A 22 -35.927 -11.601 4.797 1.00 92.75 C ANISOU 169 CD2 LEU A 22 12138 12023 11078 100 276 -119 C ATOM 170 N GLY A 23 -31.359 -12.076 7.067 1.00 92.19 N ANISOU 170 N GLY A 23 11956 11868 11203 38 336 -75 N ATOM 171 CA GLY A 23 -30.306 -13.069 7.209 1.00 93.01 C ANISOU 171 CA GLY A 23 12027 11951 11362 12 368 -62 C ATOM 172 C GLY A 23 -30.389 -13.832 8.529 1.00 93.35 C ANISOU 172 C GLY A 23 12013 12032 11422 13 345 -54 C ATOM 173 O GLY A 23 -30.209 -15.048 8.554 1.00 92.42 O ANISOU 173 O GLY A 23 11869 11917 11328 -5 362 -44 O ATOM 174 N ASN A 24 -30.675 -13.100 9.613 1.00 95.07 N ANISOU 174 N ASN A 24 12215 12278 11628 33 305 -58 N ATOM 175 CA ASN A 24 -30.641 -13.648 10.959 1.00 96.75 C ANISOU 175 CA ASN A 24 12377 12525 11859 35 281 -50 C ATOM 176 C ASN A 24 -31.953 -14.354 11.289 1.00 97.82 C ANISOU 176 C ASN A 24 12497 12717 11953 44 259 -51 C ATOM 177 O ASN A 24 -31.971 -15.243 12.138 1.00 99.18 O ANISOU 177 O ASN A 24 12629 12915 12140 36 251 -41 O ATOM 178 CB ASN A 24 -30.261 -12.592 11.999 1.00 97.20 C ANISOU 178 CB ASN A 24 12422 12585 11925 51 250 -54 C ATOM 179 CG ASN A 24 -28.791 -12.237 11.948 1.00 99.22 C ANISOU 179 CG ASN A 24 12676 12787 12237 36 273 -49 C ATOM 180 OD1 ASN A 24 -27.965 -12.894 12.577 1.00 99.40 O ANISOU 180 OD1 ASN A 24 12662 12799 12305 22 279 -39 O ATOM 181 ND2 ASN A 24 -28.457 -11.196 11.203 1.00101.69 N ANISOU 181 ND2 ASN A 24 13028 13064 12546 39 283 -57 N ATOM 182 N VAL A 25 -33.040 -13.951 10.619 1.00 98.42 N ANISOU 182 N VAL A 25 12606 12811 11978 60 250 -64 N ATOM 183 CA VAL A 25 -34.327 -14.615 10.771 1.00 98.85 C ANISOU 183 CA VAL A 25 12649 12918 11993 67 233 -67 C ATOM 184 C VAL A 25 -34.228 -16.028 10.195 1.00 99.74 C ANISOU 184 C VAL A 25 12752 13022 12124 42 263 -55 C ATOM 185 O VAL A 25 -34.838 -16.958 10.720 1.00 99.52 O ANISOU 185 O VAL A 25 12694 13032 12087 38 253 -48 O ATOM 186 CB VAL A 25 -35.476 -13.798 10.143 1.00 97.68 C ANISOU 186 CB VAL A 25 12538 12786 11788 92 214 -85 C ATOM 187 CG1 VAL A 25 -36.646 -14.668 9.710 1.00 97.32 C ANISOU 187 CG1 VAL A 25 12492 12775 11708 91 213 -88 C ATOM 188 CG2 VAL A 25 -35.954 -12.696 11.075 1.00 97.08 C ANISOU 188 CG2 VAL A 25 12457 12743 11688 120 171 -99 C ATOM 189 N LEU A 26 -33.429 -16.177 9.132 1.00100.76 N ANISOU 189 N LEU A 26 12906 13100 12279 25 302 -51 N ATOM 190 CA LEU A 26 -33.234 -17.459 8.473 1.00100.71 C ANISOU 190 CA LEU A 26 12893 13079 12291 1 333 -42 C ATOM 191 C LEU A 26 -32.515 -18.430 9.408 1.00100.37 C ANISOU 191 C LEU A 26 12801 13039 12295 -16 335 -26 C ATOM 192 O LEU A 26 -32.774 -19.630 9.361 1.00100.60 O ANISOU 192 O LEU A 26 12811 13081 12330 -30 343 -18 O ATOM 193 CB LEU A 26 -32.447 -17.247 7.175 1.00102.43 C ANISOU 193 CB LEU A 26 13150 13240 12527 -12 374 -44 C ATOM 194 CG LEU A 26 -32.388 -18.447 6.228 1.00103.26 C ANISOU 194 CG LEU A 26 13260 13329 12643 -33 408 -40 C ATOM 195 CD1 LEU A 26 -33.782 -18.847 5.768 1.00102.85 C ANISOU 195 CD1 LEU A 26 13224 13314 12542 -22 395 -46 C ATOM 196 CD2 LEU A 26 -31.494 -18.154 5.031 1.00103.12 C ANISOU 196 CD2 LEU A 26 13280 13256 12645 -47 450 -43 C ATOM 197 N VAL A 27 -31.621 -17.902 10.254 1.00100.08 N ANISOU 197 N VAL A 27 12745 12989 12292 -16 327 -23 N ATOM 198 CA VAL A 27 -30.866 -18.712 11.198 1.00101.82 C ANISOU 198 CA VAL A 27 12921 13208 12558 -31 325 -9 C ATOM 199 C VAL A 27 -31.813 -19.250 12.270 1.00104.08 C ANISOU 199 C VAL A 27 13175 13552 12818 -24 290 -3 C ATOM 200 O VAL A 27 -31.783 -20.439 12.585 1.00103.43 O ANISOU 200 O VAL A 27 13065 13480 12754 -40 293 10 O ATOM 201 CB VAL A 27 -29.684 -17.930 11.809 1.00101.04 C ANISOU 201 CB VAL A 27 12812 13079 12500 -30 322 -8 C ATOM 202 CG1 VAL A 27 -29.021 -18.679 12.956 1.00100.60 C ANISOU 202 CG1 VAL A 27 12709 13028 12487 -41 310 5 C ATOM 203 CG2 VAL A 27 -28.652 -17.554 10.758 1.00102.03 C ANISOU 203 CG2 VAL A 27 12965 13146 12658 -43 361 -12 C ATOM 204 N CYS A 28 -32.658 -18.364 12.812 1.00107.35 N ANISOU 204 N CYS A 28 13594 14004 13189 0 257 -13 N ATOM 205 CA CYS A 28 -33.570 -18.706 13.891 1.00109.32 C ANISOU 205 CA CYS A 28 13814 14313 13411 8 224 -10 C ATOM 206 C CYS A 28 -34.623 -19.694 13.395 1.00113.38 C ANISOU 206 C CYS A 28 14328 14855 13895 1 229 -8 C ATOM 207 O CYS A 28 -35.042 -20.576 14.141 1.00118.91 O ANISOU 207 O CYS A 28 14996 15591 14592 -7 215 3 O ATOM 208 CB CYS A 28 -34.243 -17.460 14.454 1.00107.20 C ANISOU 208 CB CYS A 28 13553 14075 13101 37 191 -25 C ATOM 209 SG CYS A 28 -33.069 -16.249 15.117 1.00103.99 S ANISOU 209 SG CYS A 28 13146 13637 12728 48 180 -28 S ATOM 210 N TRP A 29 -35.032 -19.545 12.130 1.00116.58 N ANISOU 210 N TRP A 29 14770 15245 14280 4 247 -18 N ATOM 211 CA TRP A 29 -36.020 -20.433 11.539 1.00120.24 C ANISOU 211 CA TRP A 29 15237 15732 14716 -2 252 -18 C ATOM 212 C TRP A 29 -35.406 -21.805 11.271 1.00118.36 C ANISOU 212 C TRP A 29 14982 15470 14518 -30 278 -2 C ATOM 213 O TRP A 29 -36.100 -22.816 11.346 1.00115.35 O ANISOU 213 O TRP A 29 14584 15117 14126 -40 274 5 O ATOM 214 CB TRP A 29 -36.634 -19.812 10.277 1.00128.85 C ANISOU 214 CB TRP A 29 16375 16811 15772 12 262 -35 C ATOM 215 CG TRP A 29 -37.860 -20.519 9.783 1.00137.63 C ANISOU 215 CG TRP A 29 17491 17955 16847 12 258 -39 C ATOM 216 CD1 TRP A 29 -38.036 -21.100 8.559 1.00139.50 C ANISOU 216 CD1 TRP A 29 17753 18170 17081 3 282 -41 C ATOM 217 CD2 TRP A 29 -39.087 -20.730 10.506 1.00142.86 C ANISOU 217 CD2 TRP A 29 18131 18679 17473 23 227 -43 C ATOM 218 NE1 TRP A 29 -39.285 -21.652 8.469 1.00143.71 N ANISOU 218 NE1 TRP A 29 18281 18744 17578 7 268 -45 N ATOM 219 CE2 TRP A 29 -39.953 -21.444 9.647 1.00145.17 C ANISOU 219 CE2 TRP A 29 18435 18981 17742 19 235 -47 C ATOM 220 CE3 TRP A 29 -39.541 -20.390 11.787 1.00144.21 C ANISOU 220 CE3 TRP A 29 18270 18896 17626 35 195 -45 C ATOM 221 CZ2 TRP A 29 -41.241 -21.819 10.033 1.00146.29 C ANISOU 221 CZ2 TRP A 29 18559 19179 17848 25 212 -52 C ATOM 222 CZ3 TRP A 29 -40.812 -20.762 12.167 1.00145.21 C ANISOU 222 CZ3 TRP A 29 18380 19079 17715 41 173 -50 C ATOM 223 CH2 TRP A 29 -41.650 -21.466 11.300 1.00145.99 C ANISOU 223 CH2 TRP A 29 18489 19186 17793 36 182 -54 C ATOM 224 N ALA A 30 -34.099 -21.826 10.977 1.00120.18 N ANISOU 224 N ALA A 30 15215 15649 14798 -44 304 4 N ATOM 225 CA ALA A 30 -33.381 -23.049 10.650 1.00121.04 C ANISOU 225 CA ALA A 30 15310 15729 14951 -69 330 16 C ATOM 226 C ALA A 30 -33.252 -23.941 11.883 1.00121.12 C ANISOU 226 C ALA A 30 15274 15764 14983 -81 310 33 C ATOM 227 O ALA A 30 -33.419 -25.156 11.792 1.00121.46 O ANISOU 227 O ALA A 30 15301 15811 15036 -98 316 43 O ATOM 228 CB ALA A 30 -32.028 -22.719 10.064 1.00119.31 C ANISOU 228 CB ALA A 30 15105 15451 14777 -79 362 15 C ATOM 229 N VAL A 31 -32.958 -23.320 13.032 1.00121.16 N ANISOU 229 N VAL A 31 15260 15783 14994 -72 285 35 N ATOM 230 CA VAL A 31 -32.748 -24.041 14.277 1.00120.56 C ANISOU 230 CA VAL A 31 15143 15727 14938 -83 264 51 C ATOM 231 C VAL A 31 -34.077 -24.628 14.752 1.00121.16 C ANISOU 231 C VAL A 31 15204 15861 14969 -82 242 56 C ATOM 232 O VAL A 31 -34.096 -25.694 15.363 1.00121.16 O ANISOU 232 O VAL A 31 15176 15875 14983 -99 233 72 O ATOM 233 CB VAL A 31 -32.081 -23.154 15.349 1.00120.18 C ANISOU 233 CB VAL A 31 15080 15677 14906 -72 244 51 C ATOM 234 CG1 VAL A 31 -31.893 -23.885 16.672 1.00119.85 C ANISOU 234 CG1 VAL A 31 14999 15658 14882 -82 219 68 C ATOM 235 CG2 VAL A 31 -30.749 -22.598 14.869 1.00119.53 C ANISOU 235 CG2 VAL A 31 15010 15536 14870 -75 267 46 C ATOM 236 N TRP A 32 -35.182 -23.936 14.447 1.00123.24 N ANISOU 236 N TRP A 32 15487 16157 15180 -62 231 41 N ATOM 237 CA TRP A 32 -36.505 -24.390 14.845 1.00127.25 C ANISOU 237 CA TRP A 32 15983 16723 15644 -60 211 42 C ATOM 238 C TRP A 32 -36.869 -25.684 14.117 1.00126.12 C ANISOU 238 C TRP A 32 15838 16576 15505 -80 228 50 C ATOM 239 O TRP A 32 -37.360 -26.622 14.741 1.00125.29 O ANISOU 239 O TRP A 32 15706 16503 15394 -94 215 63 O ATOM 240 CB TRP A 32 -37.560 -23.297 14.629 1.00133.73 C ANISOU 240 CB TRP A 32 16825 17576 16411 -32 195 21 C ATOM 241 CG TRP A 32 -38.944 -23.718 15.024 1.00141.78 C ANISOU 241 CG TRP A 32 17829 18656 17385 -30 175 19 C ATOM 242 CD1 TRP A 32 -39.895 -24.273 14.218 1.00143.95 C ANISOU 242 CD1 TRP A 32 18114 18946 17634 -32 182 14 C ATOM 243 CD2 TRP A 32 -39.533 -23.632 16.335 1.00146.46 C ANISOU 243 CD2 TRP A 32 18391 19304 17954 -24 145 21 C ATOM 244 NE1 TRP A 32 -41.035 -24.532 14.931 1.00147.38 N ANISOU 244 NE1 TRP A 32 18526 19441 18031 -30 159 12 N ATOM 245 CE2 TRP A 32 -40.844 -24.149 16.233 1.00148.29 C ANISOU 245 CE2 TRP A 32 18616 19582 18145 -25 137 17 C ATOM 246 CE3 TRP A 32 -39.089 -23.165 17.580 1.00147.65 C ANISOU 246 CE3 TRP A 32 18521 19469 18112 -19 124 26 C ATOM 247 CZ2 TRP A 32 -41.707 -24.212 17.328 1.00149.03 C ANISOU 247 CZ2 TRP A 32 18681 19737 18207 -22 111 17 C ATOM 248 CZ3 TRP A 32 -39.943 -23.228 18.660 1.00148.82 C ANISOU 248 CZ3 TRP A 32 18643 19677 18226 -15 98 26 C ATOM 249 CH2 TRP A 32 -41.234 -23.746 18.534 1.00149.37 C ANISOU 249 CH2 TRP A 32 18704 19792 18256 -17 92 21 C ATOM 250 N LEU A 33 -36.620 -25.720 12.802 1.00125.14 N ANISOU 250 N LEU A 33 15745 16413 15391 -82 256 43 N ATOM 251 CA LEU A 33 -37.001 -26.854 11.973 1.00123.95 C ANISOU 251 CA LEU A 33 15598 16257 15242 -98 273 47 C ATOM 252 C LEU A 33 -36.119 -28.057 12.299 1.00123.99 C ANISOU 252 C LEU A 33 15576 16237 15297 -124 282 67 C ATOM 253 O LEU A 33 -36.601 -29.053 12.835 1.00122.73 O ANISOU 253 O LEU A 33 15392 16106 15135 -138 269 80 O ATOM 254 CB LEU A 33 -36.892 -26.478 10.490 1.00123.93 C ANISOU 254 CB LEU A 33 15637 16216 15234 -92 301 33 C ATOM 255 CG LEU A 33 -37.810 -25.355 10.005 1.00125.86 C ANISOU 255 CG LEU A 33 15914 16480 15428 -67 292 13 C ATOM 256 CD1 LEU A 33 -37.679 -25.167 8.500 1.00125.16 C ANISOU 256 CD1 LEU A 33 15869 16352 15336 -65 321 1 C ATOM 257 CD2 LEU A 33 -39.262 -25.620 10.382 1.00126.66 C ANISOU 257 CD2 LEU A 33 16002 16640 15483 -59 265 9 C ATOM 258 N ASN A 34 -34.826 -27.940 11.972 1.00125.71 N ANISOU 258 N ASN A 34 15800 16403 15562 -131 304 67 N ATOM 259 CA ASN A 34 -33.879 -29.037 12.088 1.00127.09 C ANISOU 259 CA ASN A 34 15953 16545 15791 -154 316 82 C ATOM 260 C ASN A 34 -33.655 -29.369 13.560 1.00129.31 C ANISOU 260 C ASN A 34 16196 16849 16087 -161 287 98 C ATOM 261 O ASN A 34 -33.543 -28.475 14.395 1.00130.64 O ANISOU 261 O ASN A 34 16359 17033 16247 -148 268 96 O ATOM 262 CB ASN A 34 -32.563 -28.729 11.368 1.00126.57 C ANISOU 262 CB ASN A 34 15901 16419 15770 -158 347 75 C ATOM 263 CG ASN A 34 -31.711 -29.955 11.113 1.00127.30 C ANISOU 263 CG ASN A 34 15978 16476 15917 -181 365 84 C ATOM 264 OD1 ASN A 34 -31.705 -30.897 11.902 1.00127.72 O ANISOU 264 OD1 ASN A 34 16000 16541 15986 -195 347 100 O ATOM 265 ND2 ASN A 34 -30.981 -29.952 10.009 1.00127.65 N ANISOU 265 ND2 ASN A 34 16041 16473 15986 -186 400 74 N ATOM 266 N SER A 35 -33.585 -30.672 13.853 1.00131.40 N ANISOU 266 N SER A 35 16437 17114 16374 -183 282 114 N ATOM 267 CA SER A 35 -33.366 -31.163 15.203 1.00132.08 C ANISOU 267 CA SER A 35 16489 17218 16475 -193 255 132 C ATOM 268 C SER A 35 -31.872 -31.235 15.509 1.00132.79 C ANISOU 268 C SER A 35 16567 17260 16628 -201 261 137 C ATOM 269 O SER A 35 -31.464 -31.037 16.652 1.00134.38 O ANISOU 269 O SER A 35 16748 17470 16842 -200 238 146 O ATOM 270 CB SER A 35 -34.041 -32.494 15.411 1.00132.86 C ANISOU 270 CB SER A 35 16571 17341 16568 -213 244 148 C ATOM 271 OG SER A 35 -33.622 -33.433 14.430 1.00133.49 O ANISOU 271 OG SER A 35 16657 17382 16681 -228 268 149 O ATOM 272 N ASN A 36 -31.065 -31.510 14.476 1.00132.79 N ANISOU 272 N ASN A 36 16578 17209 16666 -208 292 130 N ATOM 273 CA ASN A 36 -29.623 -31.639 14.618 1.00132.45 C ANISOU 273 CA ASN A 36 16523 17117 16687 -216 302 131 C ATOM 274 C ASN A 36 -29.011 -30.308 15.052 1.00131.47 C ANISOU 274 C ASN A 36 16402 16983 16568 -200 299 122 C ATOM 275 O ASN A 36 -27.980 -30.298 15.719 1.00131.57 O ANISOU 275 O ASN A 36 16395 16970 16626 -204 291 126 O ATOM 276 CB ASN A 36 -28.962 -32.177 13.344 1.00133.91 C ANISOU 276 CB ASN A 36 16720 17253 16908 -227 340 122 C ATOM 277 CG ASN A 36 -29.357 -33.602 13.017 1.00136.25 C ANISOU 277 CG ASN A 36 17007 17551 17210 -245 340 131 C ATOM 278 OD1 ASN A 36 -29.517 -34.432 13.909 1.00139.13 O ANISOU 278 OD1 ASN A 36 17347 17934 17583 -257 313 149 O ATOM 279 ND2 ASN A 36 -29.508 -33.897 11.736 1.00136.45 N ANISOU 279 ND2 ASN A 36 17054 17558 17233 -247 370 121 N ATOM 280 N LEU A 37 -29.669 -29.200 14.676 1.00129.50 N ANISOU 280 N LEU A 37 16179 16753 16274 -181 302 109 N ATOM 281 CA LEU A 37 -29.225 -27.844 14.973 1.00128.18 C ANISOU 281 CA LEU A 37 16020 16577 16104 -163 299 99 C ATOM 282 C LEU A 37 -29.702 -27.396 16.352 1.00128.05 C ANISOU 282 C LEU A 37 15986 16606 16062 -152 259 106 C ATOM 283 O LEU A 37 -29.416 -26.271 16.760 1.00129.68 O ANISOU 283 O LEU A 37 16197 16811 16263 -136 250 98 O ATOM 284 CB LEU A 37 -29.827 -26.877 13.951 1.00127.54 C ANISOU 284 CB LEU A 37 15978 16500 15983 -147 316 82 C ATOM 285 CG LEU A 37 -29.375 -26.990 12.500 1.00125.48 C ANISOU 285 CG LEU A 37 15743 16195 15740 -154 357 71 C ATOM 286 CD1 LEU A 37 -30.087 -25.927 11.678 1.00126.27 C ANISOU 286 CD1 LEU A 37 15882 16303 15791 -136 366 56 C ATOM 287 CD2 LEU A 37 -27.866 -26.835 12.376 1.00124.26 C ANISOU 287 CD2 LEU A 37 15581 15985 15646 -163 379 68 C ATOM 288 N GLN A 38 -30.500 -28.238 17.018 1.00125.09 N ANISOU 288 N GLN A 38 15593 16272 15664 -160 237 119 N ATOM 289 CA GLN A 38 -30.960 -27.957 18.368 1.00122.96 C ANISOU 289 CA GLN A 38 15304 16047 15368 -153 200 127 C ATOM 290 C GLN A 38 -29.973 -28.563 19.362 1.00123.61 C ANISOU 290 C GLN A 38 15358 16110 15499 -167 184 143 C ATOM 291 O GLN A 38 -30.120 -29.713 19.771 1.00126.00 O ANISOU 291 O GLN A 38 15642 16422 15810 -185 173 159 O ATOM 292 CB GLN A 38 -32.379 -28.487 18.589 1.00120.78 C ANISOU 292 CB GLN A 38 15024 15827 15039 -155 185 133 C ATOM 293 CG GLN A 38 -33.445 -27.763 17.780 1.00119.43 C ANISOU 293 CG GLN A 38 14880 15682 14816 -137 194 116 C ATOM 294 CD GLN A 38 -34.796 -28.426 17.884 1.00120.67 C ANISOU 294 CD GLN A 38 15030 15890 14927 -143 182 121 C ATOM 295 OE1 GLN A 38 -34.907 -29.620 18.159 1.00122.24 O ANISOU 295 OE1 GLN A 38 15210 16096 15137 -164 178 138 O ATOM 296 NE2 GLN A 38 -35.843 -27.651 17.655 1.00120.56 N ANISOU 296 NE2 GLN A 38 15032 15914 14863 -123 176 105 N ATOM 297 N ASN A 39 -28.958 -27.771 19.723 1.00123.08 N ANISOU 297 N ASN A 39 15287 16013 15464 -158 182 137 N ATOM 298 CA ASN A 39 -27.959 -28.159 20.704 1.00122.81 C ANISOU 298 CA ASN A 39 15227 15957 15477 -167 163 149 C ATOM 299 C ASN A 39 -27.493 -26.913 21.452 1.00121.54 C ANISOU 299 C ASN A 39 15065 15796 15317 -148 146 141 C ATOM 300 O ASN A 39 -27.873 -25.797 21.101 1.00121.07 O ANISOU 300 O ASN A 39 15026 15747 15227 -129 151 126 O ATOM 301 CB ASN A 39 -26.814 -28.957 20.070 1.00123.49 C ANISOU 301 CB ASN A 39 15306 15985 15628 -185 186 150 C ATOM 302 CG ASN A 39 -26.002 -28.151 19.079 1.00123.13 C ANISOU 302 CG ASN A 39 15279 15894 15612 -177 219 132 C ATOM 303 OD1 ASN A 39 -25.086 -27.428 19.461 1.00124.51 O ANISOU 303 OD1 ASN A 39 15449 16043 15818 -170 215 126 O ATOM 304 ND2 ASN A 39 -26.323 -28.279 17.802 1.00122.13 N ANISOU 304 ND2 ASN A 39 15174 15756 15473 -180 251 123 N ATOM 305 N VAL A 40 -26.649 -27.127 22.469 1.00121.45 N ANISOU 305 N VAL A 40 15031 15769 15344 -153 124 151 N ATOM 306 CA VAL A 40 -26.262 -26.099 23.423 1.00120.12 C ANISOU 306 CA VAL A 40 14857 15606 15176 -136 99 146 C ATOM 307 C VAL A 40 -25.490 -24.986 22.716 1.00117.03 C ANISOU 307 C VAL A 40 14482 15174 14810 -123 121 127 C ATOM 308 O VAL A 40 -25.597 -23.824 23.103 1.00117.79 O ANISOU 308 O VAL A 40 14586 15283 14886 -103 108 117 O ATOM 309 CB VAL A 40 -25.465 -26.691 24.605 1.00122.26 C ANISOU 309 CB VAL A 40 15102 15865 15488 -146 71 161 C ATOM 310 CG1 VAL A 40 -25.279 -25.682 25.729 1.00121.66 C ANISOU 310 CG1 VAL A 40 15020 15805 15401 -127 40 158 C ATOM 311 CG2 VAL A 40 -26.102 -27.964 25.143 1.00123.51 C ANISOU 311 CG2 VAL A 40 15246 16054 15628 -165 53 182 C ATOM 312 N THR A 41 -24.722 -25.346 21.679 1.00112.63 N ANISOU 312 N THR A 41 13930 14567 14297 -135 155 122 N ATOM 313 CA THR A 41 -23.875 -24.389 20.984 1.00110.50 C ANISOU 313 CA THR A 41 13674 14254 14057 -127 179 106 C ATOM 314 C THR A 41 -24.730 -23.423 20.166 1.00108.83 C ANISOU 314 C THR A 41 13496 14061 13793 -111 194 92 C ATOM 315 O THR A 41 -24.456 -22.225 20.144 1.00109.52 O ANISOU 315 O THR A 41 13596 14138 13878 -96 193 81 O ATOM 316 CB THR A 41 -22.816 -25.081 20.115 1.00110.47 C ANISOU 316 CB THR A 41 13665 14194 14114 -146 212 103 C ATOM 317 OG1 THR A 41 -22.189 -26.106 20.888 1.00111.85 O ANISOU 317 OG1 THR A 41 13810 14356 14333 -160 194 116 O ATOM 318 CG2 THR A 41 -21.765 -24.126 19.591 1.00109.68 C ANISOU 318 CG2 THR A 41 13574 14046 14053 -141 235 87 C ATOM 319 N ASN A 42 -25.766 -23.956 19.509 1.00107.32 N ANISOU 319 N ASN A 42 13317 13897 13561 -115 205 94 N ATOM 320 CA ASN A 42 -26.590 -23.180 18.595 1.00107.75 C ANISOU 320 CA ASN A 42 13405 13965 13568 -102 220 81 C ATOM 321 C ASN A 42 -27.541 -22.264 19.364 1.00107.30 C ANISOU 321 C ASN A 42 13353 13959 13456 -79 188 76 C ATOM 322 O ASN A 42 -28.069 -21.309 18.798 1.00108.57 O ANISOU 322 O ASN A 42 13541 14128 13582 -63 193 62 O ATOM 323 CB ASN A 42 -27.344 -24.069 17.604 1.00109.24 C ANISOU 323 CB ASN A 42 13607 14164 13735 -113 242 83 C ATOM 324 CG ASN A 42 -26.457 -24.653 16.524 1.00110.37 C ANISOU 324 CG ASN A 42 13756 14254 13926 -131 281 80 C ATOM 325 OD1 ASN A 42 -25.238 -24.708 16.673 1.00112.16 O ANISOU 325 OD1 ASN A 42 13967 14438 14209 -139 289 80 O ATOM 326 ND2 ASN A 42 -27.062 -25.094 15.432 1.00110.58 N ANISOU 326 ND2 ASN A 42 13803 14282 13931 -137 305 77 N ATOM 327 N TYR A 43 -27.759 -22.562 20.649 1.00106.20 N ANISOU 327 N TYR A 43 13188 13854 13309 -78 154 87 N ATOM 328 CA TYR A 43 -28.630 -21.739 21.473 1.00104.85 C ANISOU 328 CA TYR A 43 13019 13734 13088 -57 123 82 C ATOM 329 C TYR A 43 -27.977 -20.383 21.723 1.00103.02 C ANISOU 329 C TYR A 43 12794 13480 12867 -37 114 69 C ATOM 330 O TYR A 43 -28.668 -19.370 21.809 1.00102.19 O ANISOU 330 O TYR A 43 12705 13402 12719 -15 100 56 O ATOM 331 CB TYR A 43 -29.023 -22.466 22.761 1.00108.39 C ANISOU 331 CB TYR A 43 13438 14223 13522 -63 91 97 C ATOM 332 CG TYR A 43 -29.892 -23.679 22.544 1.00112.09 C ANISOU 332 CG TYR A 43 13900 14721 13968 -80 96 109 C ATOM 333 CD1 TYR A 43 -30.792 -23.733 21.489 1.00112.95 C ANISOU 333 CD1 TYR A 43 14030 14843 14042 -78 116 101 C ATOM 334 CD2 TYR A 43 -29.826 -24.770 23.397 1.00113.24 C ANISOU 334 CD2 TYR A 43 14021 14881 14126 -98 80 129 C ATOM 335 CE1 TYR A 43 -31.595 -24.842 21.278 1.00113.51 C ANISOU 335 CE1 TYR A 43 14095 14940 14093 -94 120 111 C ATOM 336 CE2 TYR A 43 -30.622 -25.888 23.200 1.00114.41 C ANISOU 336 CE2 TYR A 43 14163 15054 14254 -115 84 140 C ATOM 337 CZ TYR A 43 -31.509 -25.923 22.138 1.00114.71 C ANISOU 337 CZ TYR A 43 14221 15105 14259 -113 104 131 C ATOM 338 OH TYR A 43 -32.299 -27.017 21.938 1.00117.90 O ANISOU 338 OH TYR A 43 14618 15533 14644 -130 107 142 O ATOM 339 N PHE A 44 -26.642 -20.381 21.819 1.00101.31 N ANISOU 339 N PHE A 44 12568 13213 12711 -46 122 71 N ATOM 340 CA PHE A 44 -25.880 -19.149 21.929 1.00 99.91 C ANISOU 340 CA PHE A 44 12399 13007 12555 -31 118 60 C ATOM 341 C PHE A 44 -25.841 -18.445 20.575 1.00 98.24 C ANISOU 341 C PHE A 44 12222 12766 12339 -28 150 46 C ATOM 342 O PHE A 44 -25.685 -17.226 20.514 1.00 99.45 O ANISOU 342 O PHE A 44 12392 12910 12486 -11 145 33 O ATOM 343 CB PHE A 44 -24.475 -19.421 22.475 1.00100.17 C ANISOU 343 CB PHE A 44 12407 12996 12655 -43 115 66 C ATOM 344 CG PHE A 44 -24.424 -19.849 23.921 1.00100.89 C ANISOU 344 CG PHE A 44 12470 13113 12751 -42 77 78 C ATOM 345 CD1 PHE A 44 -24.853 -19.001 24.933 1.00101.29 C ANISOU 345 CD1 PHE A 44 12518 13199 12768 -21 42 74 C ATOM 346 CD2 PHE A 44 -23.935 -21.098 24.272 1.00100.24 C ANISOU 346 CD2 PHE A 44 12364 13018 12706 -63 76 94 C ATOM 347 CE1 PHE A 44 -24.803 -19.396 26.263 1.00100.47 C ANISOU 347 CE1 PHE A 44 12389 13119 12665 -21 8 85 C ATOM 348 CE2 PHE A 44 -23.883 -21.492 25.601 1.00100.84 C ANISOU 348 CE2 PHE A 44 12416 13116 12783 -64 40 106 C ATOM 349 CZ PHE A 44 -24.317 -20.640 26.594 1.00101.28 C ANISOU 349 CZ PHE A 44 12470 13208 12803 -43 6 102 C ATOM 350 N VAL A 45 -25.992 -19.226 19.498 1.00 95.04 N ANISOU 350 N VAL A 45 11827 12347 11936 -44 183 48 N ATOM 351 CA VAL A 45 -26.000 -18.695 18.144 1.00 92.47 C ANISOU 351 CA VAL A 45 11537 11994 11603 -43 216 36 C ATOM 352 C VAL A 45 -27.301 -17.929 17.913 1.00 91.35 C ANISOU 352 C VAL A 45 11421 11894 11393 -22 202 26 C ATOM 353 O VAL A 45 -27.287 -16.854 17.316 1.00 90.88 O ANISOU 353 O VAL A 45 11391 11817 11320 -9 209 13 O ATOM 354 CB VAL A 45 -25.781 -19.801 17.092 1.00 91.89 C ANISOU 354 CB VAL A 45 11467 11894 11551 -66 253 41 C ATOM 355 CG1 VAL A 45 -26.111 -19.337 15.680 1.00 92.30 C ANISOU 355 CG1 VAL A 45 11559 11930 11580 -65 284 30 C ATOM 356 CG2 VAL A 45 -24.369 -20.364 17.151 1.00 92.27 C ANISOU 356 CG2 VAL A 45 11492 11894 11672 -85 270 46 C ATOM 357 N VAL A 46 -28.415 -18.489 18.401 1.00 91.08 N ANISOU 357 N VAL A 46 11377 11913 11318 -18 181 31 N ATOM 358 CA VAL A 46 -29.726 -17.873 18.257 1.00 90.59 C ANISOU 358 CA VAL A 46 11334 11894 11191 3 166 19 C ATOM 359 C VAL A 46 -29.784 -16.609 19.114 1.00 91.29 C ANISOU 359 C VAL A 46 11423 12000 11263 28 133 9 C ATOM 360 O VAL A 46 -30.373 -15.609 18.704 1.00 92.20 O ANISOU 360 O VAL A 46 11565 12124 11341 48 127 -7 O ATOM 361 CB VAL A 46 -30.869 -18.854 18.588 1.00 89.23 C ANISOU 361 CB VAL A 46 11146 11775 10982 -2 154 27 C ATOM 362 CG1 VAL A 46 -32.222 -18.159 18.640 1.00 88.44 C ANISOU 362 CG1 VAL A 46 11061 11726 10818 22 132 12 C ATOM 363 CG2 VAL A 46 -30.913 -20.017 17.608 1.00 89.15 C ANISOU 363 CG2 VAL A 46 11140 11748 10984 -24 185 35 C ATOM 364 N SER A 47 -29.155 -16.665 20.296 1.00 90.88 N ANISOU 364 N SER A 47 11341 11950 11238 27 112 17 N ATOM 365 CA SER A 47 -29.019 -15.506 21.165 1.00 89.98 C ANISOU 365 CA SER A 47 11226 11846 11117 49 81 7 C ATOM 366 C SER A 47 -28.236 -14.409 20.448 1.00 89.24 C ANISOU 366 C SER A 47 11158 11701 11046 56 95 -4 C ATOM 367 O SER A 47 -28.551 -13.227 20.589 1.00 89.31 O ANISOU 367 O SER A 47 11184 11720 11029 79 76 -18 O ATOM 368 CB SER A 47 -28.375 -15.876 22.479 1.00 88.98 C ANISOU 368 CB SER A 47 11064 11723 11020 45 58 19 C ATOM 369 OG SER A 47 -28.192 -14.727 23.294 1.00 87.51 O ANISOU 369 OG SER A 47 10877 11544 10828 67 28 8 O ATOM 370 N LEU A 48 -27.224 -14.821 19.675 1.00 87.28 N ANISOU 370 N LEU A 48 10915 11401 10848 35 130 2 N ATOM 371 CA LEU A 48 -26.409 -13.895 18.907 1.00 85.98 C ANISOU 371 CA LEU A 48 10775 11185 10708 36 150 -7 C ATOM 372 C LEU A 48 -27.238 -13.314 17.764 1.00 85.10 C ANISOU 372 C LEU A 48 10706 11077 10552 45 163 -19 C ATOM 373 O LEU A 48 -27.183 -12.114 17.511 1.00 84.46 O ANISOU 373 O LEU A 48 10650 10981 10459 60 157 -31 O ATOM 374 CB LEU A 48 -25.163 -14.622 18.388 1.00 85.20 C ANISOU 374 CB LEU A 48 10666 11033 10673 8 186 1 C ATOM 375 CG LEU A 48 -24.068 -13.727 17.810 1.00 85.03 C ANISOU 375 CG LEU A 48 10661 10954 10690 5 207 -6 C ATOM 376 CD1 LEU A 48 -23.226 -13.112 18.917 1.00 84.50 C ANISOU 376 CD1 LEU A 48 10572 10876 10659 13 180 -7 C ATOM 377 CD2 LEU A 48 -23.185 -14.508 16.850 1.00 85.69 C ANISOU 377 CD2 LEU A 48 10745 10992 10821 -23 253 -2 C ATOM 378 N ALA A 49 -28.013 -14.177 17.094 1.00 85.21 N ANISOU 378 N ALA A 49 10727 11110 10540 36 180 -16 N ATOM 379 CA ALA A 49 -28.841 -13.775 15.967 1.00 86.55 C ANISOU 379 CA ALA A 49 10936 11283 10667 44 192 -26 C ATOM 380 C ALA A 49 -29.942 -12.823 16.429 1.00 87.62 C ANISOU 380 C ALA A 49 11083 11463 10747 74 154 -40 C ATOM 381 O ALA A 49 -30.379 -11.965 15.664 1.00 87.77 O ANISOU 381 O ALA A 49 11139 11474 10735 87 155 -53 O ATOM 382 CB ALA A 49 -29.412 -14.989 15.275 1.00 85.77 C ANISOU 382 CB ALA A 49 10837 11195 10555 28 214 -20 C ATOM 383 N ALA A 50 -30.374 -12.988 17.686 1.00 88.80 N ANISOU 383 N ALA A 50 11200 11657 10882 84 121 -38 N ATOM 384 CA ALA A 50 -31.396 -12.142 18.282 1.00 90.32 C ANISOU 384 CA ALA A 50 11396 11896 11024 113 83 -53 C ATOM 385 C ALA A 50 -30.878 -10.711 18.410 1.00 91.83 C ANISOU 385 C ALA A 50 11606 12062 11222 132 67 -65 C ATOM 386 O ALA A 50 -31.626 -9.759 18.194 1.00 90.71 O ANISOU 386 O ALA A 50 11489 11936 11041 155 48 -82 O ATOM 387 CB ALA A 50 -31.817 -12.704 19.618 1.00 89.63 C ANISOU 387 CB ALA A 50 11270 11861 10926 116 55 -47 C ATOM 388 N ALA A 51 -29.589 -10.580 18.750 1.00 92.91 N ANISOU 388 N ALA A 51 11731 12158 11413 121 75 -57 N ATOM 389 CA ALA A 51 -28.940 -9.286 18.887 1.00 94.21 C ANISOU 389 CA ALA A 51 11910 12292 11593 135 62 -67 C ATOM 390 C ALA A 51 -28.821 -8.606 17.524 1.00 94.68 C ANISOU 390 C ALA A 51 12016 12311 11648 133 86 -74 C ATOM 391 O ALA A 51 -28.943 -7.387 17.431 1.00 94.54 O ANISOU 391 O ALA A 51 12024 12285 11613 153 68 -87 O ATOM 392 CB ALA A 51 -27.592 -9.449 19.547 1.00 95.16 C ANISOU 392 CB ALA A 51 12004 12379 11775 121 65 -56 C ATOM 393 N ASP A 52 -28.593 -9.410 16.477 1.00 94.87 N ANISOU 393 N ASP A 52 12052 12308 11686 109 127 -66 N ATOM 394 CA ASP A 52 -28.395 -8.901 15.129 1.00 94.61 C ANISOU 394 CA ASP A 52 12063 12233 11650 103 156 -70 C ATOM 395 C ASP A 52 -29.729 -8.476 14.519 1.00 94.07 C ANISOU 395 C ASP A 52 12029 12195 11519 122 142 -83 C ATOM 396 O ASP A 52 -29.776 -7.516 13.752 1.00 94.26 O ANISOU 396 O ASP A 52 12094 12193 11527 130 144 -93 O ATOM 397 CB ASP A 52 -27.644 -9.903 14.247 1.00 96.02 C ANISOU 397 CB ASP A 52 12242 12375 11867 71 204 -58 C ATOM 398 CG ASP A 52 -26.192 -10.113 14.646 1.00 97.83 C ANISOU 398 CG ASP A 52 12445 12564 12164 52 221 -49 C ATOM 399 OD1 ASP A 52 -25.575 -9.156 15.162 1.00 97.81 O ANISOU 399 OD1 ASP A 52 12440 12542 12180 61 204 -53 O ATOM 400 OD2 ASP A 52 -25.687 -11.233 14.434 1.00 99.42 O ANISOU 400 OD2 ASP A 52 12626 12751 12398 29 249 -39 O ATOM 401 N ILE A 53 -30.803 -9.202 14.861 1.00 92.90 N ANISOU 401 N ILE A 53 11864 12099 11336 129 127 -84 N ATOM 402 CA ILE A 53 -32.144 -8.866 14.403 1.00 91.92 C ANISOU 402 CA ILE A 53 11765 12008 11153 149 110 -99 C ATOM 403 C ILE A 53 -32.551 -7.518 14.997 1.00 89.84 C ANISOU 403 C ILE A 53 11511 11761 10862 181 68 -116 C ATOM 404 O ILE A 53 -33.077 -6.662 14.288 1.00 89.26 O ANISOU 404 O ILE A 53 11477 11680 10756 197 59 -130 O ATOM 405 CB ILE A 53 -33.159 -9.986 14.731 1.00 92.18 C ANISOU 405 CB ILE A 53 11771 12094 11158 148 104 -96 C ATOM 406 CG1 ILE A 53 -32.946 -11.221 13.850 1.00 92.25 C ANISOU 406 CG1 ILE A 53 11782 12084 11186 119 145 -82 C ATOM 407 CG2 ILE A 53 -34.592 -9.476 14.630 1.00 91.78 C ANISOU 407 CG2 ILE A 53 11737 12088 11047 175 75 -115 C ATOM 408 CD1 ILE A 53 -33.799 -12.414 14.228 1.00 92.10 C ANISOU 408 CD1 ILE A 53 11732 12113 11147 114 140 -76 C ATOM 409 N LEU A 54 -32.273 -7.335 16.294 1.00 87.51 N ANISOU 409 N LEU A 54 11182 11487 10582 190 41 -115 N ATOM 410 CA LEU A 54 -32.710 -6.163 17.037 1.00 86.08 C ANISOU 410 CA LEU A 54 11003 11330 10375 221 -2 -133 C ATOM 411 C LEU A 54 -31.933 -4.919 16.605 1.00 85.33 C ANISOU 411 C LEU A 54 10941 11183 10298 227 -3 -138 C ATOM 412 O LEU A 54 -32.318 -3.804 16.954 1.00 83.91 O ANISOU 412 O LEU A 54 10774 11013 10094 254 -39 -155 O ATOM 413 CB LEU A 54 -32.547 -6.427 18.539 1.00 85.80 C ANISOU 413 CB LEU A 54 10919 11328 10351 227 -27 -129 C ATOM 414 CG LEU A 54 -33.604 -7.327 19.180 1.00 84.60 C ANISOU 414 CG LEU A 54 10736 11241 10166 230 -40 -129 C ATOM 415 CD1 LEU A 54 -33.139 -7.820 20.542 1.00 84.60 C ANISOU 415 CD1 LEU A 54 10692 11262 10189 224 -53 -118 C ATOM 416 CD2 LEU A 54 -34.938 -6.607 19.307 1.00 83.75 C ANISOU 416 CD2 LEU A 54 10641 11181 10001 261 -74 -152 C ATOM 417 N VAL A 55 -30.843 -5.115 15.852 1.00 85.10 N ANISOU 417 N VAL A 55 10925 11097 10311 201 35 -125 N ATOM 418 CA VAL A 55 -30.062 -4.005 15.328 1.00 84.89 C ANISOU 418 CA VAL A 55 10933 11018 10305 201 40 -129 C ATOM 419 C VAL A 55 -30.826 -3.361 14.171 1.00 86.76 C ANISOU 419 C VAL A 55 11223 11246 10498 211 40 -140 C ATOM 420 O VAL A 55 -30.995 -2.144 14.140 1.00 88.45 O ANISOU 420 O VAL A 55 11463 11449 10694 232 13 -154 O ATOM 421 CB VAL A 55 -28.636 -4.434 14.922 1.00 83.40 C ANISOU 421 CB VAL A 55 10739 10774 10176 168 83 -112 C ATOM 422 CG1 VAL A 55 -27.940 -3.384 14.069 1.00 83.35 C ANISOU 422 CG1 VAL A 55 10775 10710 10183 162 97 -115 C ATOM 423 CG2 VAL A 55 -27.785 -4.773 16.135 1.00 83.10 C ANISOU 423 CG2 VAL A 55 10652 10737 10183 162 74 -103 C ATOM 424 N GLY A 56 -31.302 -4.195 13.239 1.00 87.29 N ANISOU 424 N GLY A 56 11304 11316 10548 197 68 -136 N ATOM 425 CA GLY A 56 -32.009 -3.728 12.058 1.00 87.53 C ANISOU 425 CA GLY A 56 11385 11334 10537 205 71 -146 C ATOM 426 C GLY A 56 -33.367 -3.116 12.392 1.00 87.41 C ANISOU 426 C GLY A 56 11378 11367 10468 240 24 -167 C ATOM 427 O GLY A 56 -33.850 -2.250 11.667 1.00 89.98 O ANISOU 427 O GLY A 56 11748 11678 10762 255 11 -179 O ATOM 428 N VAL A 57 -33.967 -3.568 13.499 1.00 87.07 N ANISOU 428 N VAL A 57 11291 11379 10413 253 -1 -171 N ATOM 429 CA VAL A 57 -35.322 -3.183 13.859 1.00 88.51 C ANISOU 429 CA VAL A 57 11472 11613 10543 285 -42 -192 C ATOM 430 C VAL A 57 -35.299 -1.885 14.665 1.00 90.35 C ANISOU 430 C VAL A 57 11707 11852 10771 314 -85 -208 C ATOM 431 O VAL A 57 -36.187 -1.049 14.505 1.00 92.54 O ANISOU 431 O VAL A 57 12007 12145 11007 342 -118 -230 O ATOM 432 CB VAL A 57 -36.060 -4.318 14.600 1.00 87.87 C ANISOU 432 CB VAL A 57 11346 11593 10449 284 -46 -190 C ATOM 433 CG1 VAL A 57 -37.395 -3.869 15.178 1.00 86.96 C ANISOU 433 CG1 VAL A 57 11221 11536 10284 318 -90 -214 C ATOM 434 CG2 VAL A 57 -36.254 -5.537 13.712 1.00 88.00 C ANISOU 434 CG2 VAL A 57 11366 11606 10466 259 -8 -178 C ATOM 435 N LEU A 58 -34.288 -1.719 15.528 1.00 91.03 N ANISOU 435 N LEU A 58 11766 11924 10897 308 -87 -199 N ATOM 436 CA LEU A 58 -34.289 -0.612 16.475 1.00 90.50 C ANISOU 436 CA LEU A 58 11692 11868 10825 336 -131 -214 C ATOM 437 C LEU A 58 -32.979 0.174 16.426 1.00 89.17 C ANISOU 437 C LEU A 58 11538 11640 10701 326 -124 -206 C ATOM 438 O LEU A 58 -33.003 1.396 16.298 1.00 88.57 O ANISOU 438 O LEU A 58 11493 11546 10615 346 -151 -220 O ATOM 439 CB LEU A 58 -34.562 -1.145 17.886 1.00 90.83 C ANISOU 439 CB LEU A 58 11680 11966 10866 344 -151 -215 C ATOM 440 CG LEU A 58 -35.973 -1.673 18.143 1.00 90.43 C ANISOU 440 CG LEU A 58 11611 11981 10766 359 -168 -228 C ATOM 441 CD1 LEU A 58 -36.030 -2.424 19.464 1.00 89.78 C ANISOU 441 CD1 LEU A 58 11476 11947 10690 357 -177 -222 C ATOM 442 CD2 LEU A 58 -36.993 -0.543 18.124 1.00 90.38 C ANISOU 442 CD2 LEU A 58 11628 11998 10715 397 -210 -258 C ATOM 443 N ALA A 59 -31.847 -0.532 16.537 1.00 87.52 N ANISOU 443 N ALA A 59 11307 11403 10542 296 -90 -185 N ATOM 444 CA ALA A 59 -30.546 0.101 16.696 1.00 87.51 C ANISOU 444 CA ALA A 59 11309 11351 10589 286 -84 -177 C ATOM 445 C ALA A 59 -30.204 0.980 15.494 1.00 87.77 C ANISOU 445 C ALA A 59 11397 11328 10622 280 -71 -179 C ATOM 446 O ALA A 59 -29.637 2.059 15.663 1.00 86.94 O ANISOU 446 O ALA A 59 11308 11193 10534 288 -88 -184 O ATOM 447 CB ALA A 59 -29.484 -0.940 16.953 1.00 87.22 C ANISOU 447 CB ALA A 59 11238 11296 10606 255 -49 -156 C ATOM 448 N ILE A 60 -30.546 0.509 14.287 1.00 88.82 N ANISOU 448 N ILE A 60 11560 11448 10737 265 -39 -174 N ATOM 449 CA ILE A 60 -30.277 1.255 13.066 1.00 88.71 C ANISOU 449 CA ILE A 60 11603 11384 10720 257 -23 -174 C ATOM 450 C ILE A 60 -31.258 2.423 12.944 1.00 89.56 C ANISOU 450 C ILE A 60 11746 11504 10778 291 -69 -196 C ATOM 451 O ILE A 60 -30.827 3.543 12.676 1.00 90.78 O ANISOU 451 O ILE A 60 11935 11620 10939 295 -81 -200 O ATOM 452 CB ILE A 60 -30.230 0.350 11.816 1.00 87.53 C ANISOU 452 CB ILE A 60 11474 11213 10568 228 27 -162 C ATOM 453 CG1 ILE A 60 -28.998 -0.560 11.844 1.00 88.27 C ANISOU 453 CG1 ILE A 60 11540 11280 10720 193 73 -143 C ATOM 454 CG2 ILE A 60 -30.284 1.185 10.543 1.00 87.18 C ANISOU 454 CG2 ILE A 60 11496 11127 10504 225 35 -166 C ATOM 455 CD1 ILE A 60 -28.959 -1.615 10.757 1.00 88.68 C ANISOU 455 CD1 ILE A 60 11603 11318 10773 166 121 -132 C ATOM 456 N PRO A 61 -32.590 2.222 13.115 1.00 89.12 N ANISOU 456 N PRO A 61 11686 11502 10674 315 -96 -211 N ATOM 457 CA PRO A 61 -33.516 3.346 13.287 1.00 89.98 C ANISOU 457 CA PRO A 61 11818 11630 10741 353 -148 -236 C ATOM 458 C PRO A 61 -33.088 4.365 14.344 1.00 92.18 C ANISOU 458 C PRO A 61 12081 11907 11036 373 -187 -245 C ATOM 459 O PRO A 61 -33.290 5.563 14.159 1.00 92.68 O ANISOU 459 O PRO A 61 12180 11952 11083 394 -219 -259 O ATOM 460 CB PRO A 61 -34.828 2.650 13.679 1.00 88.10 C ANISOU 460 CB PRO A 61 11553 11459 10462 371 -166 -249 C ATOM 461 CG PRO A 61 -34.756 1.334 12.943 1.00 86.89 C ANISOU 461 CG PRO A 61 11396 11303 10316 340 -117 -231 C ATOM 462 CD PRO A 61 -33.299 0.931 13.048 1.00 87.68 C ANISOU 462 CD PRO A 61 11479 11361 10474 308 -78 -207 C ATOM 463 N PHE A 62 -32.486 3.883 15.439 1.00 94.73 N ANISOU 463 N PHE A 62 12353 12246 11392 367 -184 -236 N ATOM 464 CA PHE A 62 -32.007 4.751 16.505 1.00 97.98 C ANISOU 464 CA PHE A 62 12748 12657 11824 385 -220 -244 C ATOM 465 C PHE A 62 -30.774 5.523 16.040 1.00 99.49 C ANISOU 465 C PHE A 62 12967 12779 12056 367 -205 -233 C ATOM 466 O PHE A 62 -30.604 6.686 16.397 1.00 99.63 O ANISOU 466 O PHE A 62 12999 12781 12076 387 -241 -245 O ATOM 467 CB PHE A 62 -31.705 3.945 17.771 1.00101.16 C ANISOU 467 CB PHE A 62 13090 13096 12250 381 -220 -237 C ATOM 468 CG PHE A 62 -32.906 3.574 18.606 1.00103.18 C ANISOU 468 CG PHE A 62 13315 13425 12465 407 -250 -252 C ATOM 469 CD1 PHE A 62 -34.196 3.845 18.170 1.00103.91 C ANISOU 469 CD1 PHE A 62 13429 13548 12504 430 -272 -272 C ATOM 470 CD2 PHE A 62 -32.747 2.917 19.818 1.00103.55 C ANISOU 470 CD2 PHE A 62 13310 13508 12526 406 -256 -247 C ATOM 471 CE1 PHE A 62 -35.296 3.493 18.939 1.00104.89 C ANISOU 471 CE1 PHE A 62 13522 13741 12591 451 -297 -288 C ATOM 472 CE2 PHE A 62 -33.847 2.563 20.585 1.00103.69 C ANISOU 472 CE2 PHE A 62 13299 13594 12505 427 -281 -261 C ATOM 473 CZ PHE A 62 -35.119 2.849 20.143 1.00104.78 C ANISOU 473 CZ PHE A 62 13456 13763 12590 449 -300 -282 C ATOM 474 N ALA A 63 -29.927 4.860 15.241 1.00100.04 N ANISOU 474 N ALA A 63 13045 12808 12159 330 -153 -212 N ATOM 475 CA ALA A 63 -28.683 5.437 14.756 1.00100.28 C ANISOU 475 CA ALA A 63 13098 12773 12232 308 -130 -200 C ATOM 476 C ALA A 63 -28.965 6.577 13.779 1.00100.44 C ANISOU 476 C ALA A 63 13180 12758 12224 316 -143 -209 C ATOM 477 O ALA A 63 -28.207 7.543 13.724 1.00100.49 O ANISOU 477 O ALA A 63 13207 12719 12254 312 -151 -207 O ATOM 478 CB ALA A 63 -27.820 4.371 14.128 1.00100.64 C ANISOU 478 CB ALA A 63 13134 12790 12315 267 -70 -179 C ATOM 479 N ILE A 64 -30.057 6.452 13.014 1.00101.31 N ANISOU 479 N ILE A 64 13321 12887 12284 326 -147 -217 N ATOM 480 CA ILE A 64 -30.446 7.467 12.047 1.00102.82 C ANISOU 480 CA ILE A 64 13575 13047 12444 334 -162 -226 C ATOM 481 C ILE A 64 -30.982 8.693 12.788 1.00103.62 C ANISOU 481 C ILE A 64 13682 13164 12524 374 -226 -248 C ATOM 482 O ILE A 64 -30.619 9.821 12.459 1.00103.21 O ANISOU 482 O ILE A 64 13669 13069 12475 378 -243 -251 O ATOM 483 CB ILE A 64 -31.448 6.909 11.011 1.00102.30 C ANISOU 483 CB ILE A 64 13540 12996 12333 334 -148 -229 C ATOM 484 CG1 ILE A 64 -30.780 5.910 10.060 1.00102.51 C ANISOU 484 CG1 ILE A 64 13573 12993 12382 292 -84 -207 C ATOM 485 CG2 ILE A 64 -32.134 8.034 10.246 1.00101.13 C ANISOU 485 CG2 ILE A 64 13454 12829 12143 354 -181 -244 C ATOM 486 CD1 ILE A 64 -31.746 5.019 9.307 1.00101.98 C ANISOU 486 CD1 ILE A 64 13518 12953 12276 291 -67 -209 C ATOM 487 N THR A 65 -31.823 8.456 13.803 1.00104.08 N ANISOU 487 N THR A 65 13701 13284 12560 404 -260 -265 N ATOM 488 CA THR A 65 -32.529 9.514 14.512 1.00104.44 C ANISOU 488 CA THR A 65 13748 13354 12579 445 -322 -291 C ATOM 489 C THR A 65 -31.550 10.404 15.277 1.00106.51 C ANISOU 489 C THR A 65 14001 13587 12880 449 -343 -290 C ATOM 490 O THR A 65 -31.813 11.591 15.461 1.00107.22 O ANISOU 490 O THR A 65 14115 13669 12956 476 -389 -307 O ATOM 491 CB THR A 65 -33.617 8.943 15.432 1.00102.84 C ANISOU 491 CB THR A 65 13502 13228 12346 472 -348 -308 C ATOM 492 OG1 THR A 65 -34.290 7.897 14.733 1.00101.89 O ANISOU 492 OG1 THR A 65 13383 13129 12201 460 -318 -303 O ATOM 493 CG2 THR A 65 -34.626 9.980 15.874 1.00103.50 C ANISOU 493 CG2 THR A 65 13595 13340 12389 517 -410 -339 C ATOM 494 N ILE A 66 -30.425 9.823 15.714 1.00108.86 N ANISOU 494 N ILE A 66 14264 13869 13229 422 -310 -270 N ATOM 495 CA ILE A 66 -29.421 10.529 16.497 1.00109.64 C ANISOU 495 CA ILE A 66 14348 13941 13371 423 -327 -268 C ATOM 496 C ILE A 66 -28.753 11.601 15.636 1.00108.16 C ANISOU 496 C ILE A 66 14214 13685 13198 411 -324 -263 C ATOM 497 O ILE A 66 -28.480 12.700 16.118 1.00106.54 O ANISOU 497 O ILE A 66 14017 13462 13003 429 -363 -273 O ATOM 498 CB ILE A 66 -28.403 9.537 17.106 1.00112.59 C ANISOU 498 CB ILE A 66 14670 14312 13795 396 -291 -248 C ATOM 499 CG1 ILE A 66 -28.944 8.852 18.366 1.00114.14 C ANISOU 499 CG1 ILE A 66 14812 14575 13981 416 -312 -257 C ATOM 500 CG2 ILE A 66 -27.053 10.196 17.363 1.00114.38 C ANISOU 500 CG2 ILE A 66 14896 14486 14077 381 -288 -239 C ATOM 501 CD1 ILE A 66 -28.822 9.672 19.636 1.00113.76 C ANISOU 501 CD1 ILE A 66 14740 14542 13942 445 -362 -272 C ATOM 502 N SER A 67 -28.522 11.274 14.357 1.00107.21 N ANISOU 502 N SER A 67 14130 13528 13076 381 -279 -247 N ATOM 503 CA SER A 67 -27.736 12.096 13.449 1.00107.45 C ANISOU 503 CA SER A 67 14210 13491 13125 359 -264 -237 C ATOM 504 C SER A 67 -28.418 13.432 13.157 1.00108.23 C ANISOU 504 C SER A 67 14360 13577 13185 388 -315 -255 C ATOM 505 O SER A 67 -27.757 14.378 12.732 1.00109.71 O ANISOU 505 O SER A 67 14585 13711 13390 377 -319 -250 O ATOM 506 CB SER A 67 -27.429 11.355 12.176 1.00107.04 C ANISOU 506 CB SER A 67 14185 13410 13076 321 -204 -218 C ATOM 507 OG SER A 67 -28.612 11.145 11.419 1.00106.47 O ANISOU 507 OG SER A 67 14145 13361 12948 333 -209 -227 O ATOM 508 N THR A 68 -29.737 13.500 13.381 1.00107.84 N ANISOU 508 N THR A 68 14311 13577 13086 424 -355 -277 N ATOM 509 CA THR A 68 -30.505 14.709 13.120 1.00107.46 C ANISOU 509 CA THR A 68 14310 13522 13000 455 -408 -298 C ATOM 510 C THR A 68 -30.173 15.774 14.164 1.00108.41 C ANISOU 510 C THR A 68 14415 13636 13138 481 -458 -311 C ATOM 511 O THR A 68 -30.068 16.956 13.840 1.00108.68 O ANISOU 511 O THR A 68 14494 13631 13168 490 -489 -317 O ATOM 512 CB THR A 68 -32.012 14.422 13.047 1.00106.39 C ANISOU 512 CB THR A 68 14176 13441 12807 487 -435 -319 C ATOM 513 OG1 THR A 68 -32.475 14.041 14.344 1.00106.02 O ANISOU 513 OG1 THR A 68 14069 13456 12757 513 -460 -335 O ATOM 514 CG2 THR A 68 -32.374 13.354 12.037 1.00105.01 C ANISOU 514 CG2 THR A 68 14015 13272 12613 463 -388 -307 C ATOM 515 N GLY A 69 -30.002 15.338 15.418 1.00108.30 N ANISOU 515 N GLY A 69 14340 13663 13145 492 -467 -315 N ATOM 516 CA GLY A 69 -29.769 16.243 16.531 1.00108.76 C ANISOU 516 CA GLY A 69 14379 13726 13220 519 -517 -330 C ATOM 517 C GLY A 69 -31.058 16.925 16.980 1.00109.75 C ANISOU 517 C GLY A 69 14510 13894 13296 568 -580 -364 C ATOM 518 O GLY A 69 -31.050 18.101 17.338 1.00110.03 O ANISOU 518 O GLY A 69 14562 13913 13330 593 -629 -380 O ATOM 519 N PHE A 70 -32.156 16.159 16.961 1.00110.10 N ANISOU 519 N PHE A 70 14539 13994 13300 582 -578 -375 N ATOM 520 CA PHE A 70 -33.483 16.646 17.305 1.00111.64 C ANISOU 520 CA PHE A 70 14736 14237 13446 627 -633 -408 C ATOM 521 C PHE A 70 -33.550 16.972 18.795 1.00111.85 C ANISOU 521 C PHE A 70 14714 14304 13479 659 -675 -427 C ATOM 522 O PHE A 70 -32.685 16.563 19.567 1.00111.26 O ANISOU 522 O PHE A 70 14600 14230 13443 644 -657 -413 O ATOM 523 CB PHE A 70 -34.544 15.613 16.910 1.00111.59 C ANISOU 523 CB PHE A 70 14719 14278 13400 628 -613 -412 C ATOM 524 CG PHE A 70 -34.643 14.412 17.818 1.00112.03 C ANISOU 524 CG PHE A 70 14712 14393 13464 623 -591 -408 C ATOM 525 CD1 PHE A 70 -33.527 13.639 18.104 1.00112.83 C ANISOU 525 CD1 PHE A 70 14783 14478 13611 588 -546 -380 C ATOM 526 CD2 PHE A 70 -35.857 14.043 18.380 1.00112.93 C ANISOU 526 CD2 PHE A 70 14795 14575 13537 652 -615 -432 C ATOM 527 CE1 PHE A 70 -33.617 12.536 18.940 1.00112.05 C ANISOU 527 CE1 PHE A 70 14627 14429 13517 583 -529 -375 C ATOM 528 CE2 PHE A 70 -35.948 12.936 19.213 1.00113.46 C ANISOU 528 CE2 PHE A 70 14806 14694 13609 645 -594 -426 C ATOM 529 CZ PHE A 70 -34.828 12.184 19.492 1.00112.16 C ANISOU 529 CZ PHE A 70 14614 14512 13489 611 -552 -397 C ATOM 530 N CYS A 71 -34.596 17.711 19.179 1.00113.93 N ANISOU 530 N CYS A 71 14983 14603 13704 703 -731 -461 N ATOM 531 CA CYS A 71 -34.818 18.089 20.564 1.00116.31 C ANISOU 531 CA CYS A 71 15241 14947 14004 737 -776 -485 C ATOM 532 C CYS A 71 -35.478 16.934 21.311 1.00115.37 C ANISOU 532 C CYS A 71 15066 14902 13866 742 -761 -490 C ATOM 533 O CYS A 71 -36.422 16.324 20.810 1.00117.55 O ANISOU 533 O CYS A 71 15345 15211 14107 744 -749 -496 O ATOM 534 CB CYS A 71 -35.703 19.327 20.649 1.00120.13 C ANISOU 534 CB CYS A 71 15752 15440 14454 783 -842 -521 C ATOM 535 SG CYS A 71 -34.967 20.781 19.860 1.00124.42 S ANISOU 535 SG CYS A 71 16363 15896 15017 780 -868 -516 S ATOM 536 N ALA A 72 -34.958 16.648 22.510 1.00112.30 N ANISOU 536 N ALA A 72 14629 14538 13502 743 -763 -487 N ATOM 537 CA ALA A 72 -35.484 15.607 23.378 1.00111.30 C ANISOU 537 CA ALA A 72 14448 14481 13359 747 -752 -491 C ATOM 538 C ALA A 72 -34.939 15.806 24.788 1.00111.63 C ANISOU 538 C ALA A 72 14448 14543 13424 760 -775 -496 C ATOM 539 O ALA A 72 -33.918 16.469 24.973 1.00110.80 O ANISOU 539 O ALA A 72 14352 14389 13358 754 -784 -487 O ATOM 540 CB ALA A 72 -35.112 14.246 22.841 1.00110.34 C ANISOU 540 CB ALA A 72 14314 14355 13253 704 -688 -458 C ATOM 541 N ALA A 73 -35.644 15.231 25.771 1.00111.59 N ANISOU 541 N ALA A 73 14396 14608 13393 777 -785 -510 N ATOM 542 CA ALA A 73 -35.177 15.171 27.146 1.00110.64 C ANISOU 542 CA ALA A 73 14233 14514 13291 785 -800 -512 C ATOM 543 C ALA A 73 -33.874 14.379 27.186 1.00110.89 C ANISOU 543 C ALA A 73 14249 14509 13376 743 -754 -474 C ATOM 544 O ALA A 73 -33.714 13.412 26.444 1.00112.31 O ANISOU 544 O ALA A 73 14431 14677 13563 709 -706 -450 O ATOM 545 CB ALA A 73 -36.230 14.540 28.022 1.00110.32 C ANISOU 545 CB ALA A 73 14150 14558 13210 804 -810 -531 C ATOM 546 N CYS A 74 -32.955 14.806 28.060 1.00110.32 N ANISOU 546 N CYS A 74 14159 14417 13338 747 -772 -471 N ATOM 547 CA CYS A 74 -31.603 14.271 28.096 1.00108.28 C ANISOU 547 CA CYS A 74 13889 14114 13136 710 -736 -439 C ATOM 548 C CYS A 74 -31.622 12.782 28.437 1.00107.19 C ANISOU 548 C CYS A 74 13713 14015 13001 685 -696 -419 C ATOM 549 O CYS A 74 -30.822 12.018 27.905 1.00105.80 O ANISOU 549 O CYS A 74 13536 13803 12860 647 -650 -390 O ATOM 550 CB CYS A 74 -30.741 15.028 29.097 1.00108.67 C ANISOU 550 CB CYS A 74 13924 14144 13220 724 -770 -444 C ATOM 551 SG CYS A 74 -28.974 14.669 28.925 1.00109.17 S ANISOU 551 SG CYS A 74 13984 14136 13361 680 -730 -407 S ATOM 552 N HIS A 75 -32.544 12.385 29.323 1.00108.48 N ANISOU 552 N HIS A 75 13843 14250 13125 706 -714 -436 N ATOM 553 CA HIS A 75 -32.683 10.996 29.733 1.00109.09 C ANISOU 553 CA HIS A 75 13883 14368 13197 684 -682 -419 C ATOM 554 C HIS A 75 -33.226 10.154 28.582 1.00106.59 C ANISOU 554 C HIS A 75 13582 14054 12863 660 -640 -406 C ATOM 555 O HIS A 75 -32.793 9.022 28.382 1.00105.53 O ANISOU 555 O HIS A 75 13432 13914 12750 626 -597 -379 O ATOM 556 CB HIS A 75 -33.531 10.890 31.008 1.00112.46 C ANISOU 556 CB HIS A 75 14273 14871 13585 712 -714 -441 C ATOM 557 CG HIS A 75 -32.721 10.942 32.260 1.00115.80 C ANISOU 557 CG HIS A 75 14666 15296 14036 716 -732 -437 C ATOM 558 ND1 HIS A 75 -32.108 12.102 32.697 1.00117.35 N ANISOU 558 ND1 HIS A 75 14873 15461 14256 737 -770 -449 N ATOM 559 CD2 HIS A 75 -32.415 9.986 33.164 1.00118.05 C ANISOU 559 CD2 HIS A 75 14913 15610 14331 701 -719 -421 C ATOM 560 CE1 HIS A 75 -31.460 11.859 33.818 1.00120.20 C ANISOU 560 CE1 HIS A 75 15202 15830 14639 736 -780 -443 C ATOM 561 NE2 HIS A 75 -31.633 10.566 34.126 1.00121.18 N ANISOU 561 NE2 HIS A 75 15297 15991 14755 714 -749 -425 N ATOM 562 N GLY A 76 -34.173 10.726 27.832 1.00105.72 N ANISOU 562 N GLY A 76 13502 13951 12715 680 -654 -426 N ATOM 563 CA GLY A 76 -34.738 10.072 26.663 1.00105.95 C ANISOU 563 CA GLY A 76 13552 13980 12726 661 -620 -418 C ATOM 564 C GLY A 76 -33.705 9.912 25.549 1.00105.88 C ANISOU 564 C GLY A 76 13574 13897 12758 625 -579 -390 C ATOM 565 O GLY A 76 -33.706 8.909 24.838 1.00105.38 O ANISOU 565 O GLY A 76 13511 13829 12698 596 -535 -370 O ATOM 566 N CYS A 77 -32.826 10.914 25.421 1.00104.78 N ANISOU 566 N CYS A 77 13459 13702 12652 627 -593 -389 N ATOM 567 CA CYS A 77 -31.768 10.920 24.424 1.00101.84 C ANISOU 567 CA CYS A 77 13115 13257 12321 594 -556 -364 C ATOM 568 C CYS A 77 -30.730 9.849 24.753 1.00100.32 C ANISOU 568 C CYS A 77 12890 13052 12176 558 -516 -335 C ATOM 569 O CYS A 77 -30.101 9.308 23.848 1.00102.07 O ANISOU 569 O CYS A 77 13126 13233 12425 524 -470 -313 O ATOM 570 CB CYS A 77 -31.114 12.295 24.340 1.00103.09 C ANISOU 570 CB CYS A 77 13304 13363 12502 606 -586 -372 C ATOM 571 SG CYS A 77 -29.696 12.379 23.212 1.00105.81 S ANISOU 571 SG CYS A 77 13682 13619 12903 562 -540 -342 S ATOM 572 N LEU A 78 -30.569 9.543 26.048 1.00 98.25 N ANISOU 572 N LEU A 78 12583 12825 11922 568 -533 -337 N ATOM 573 CA LEU A 78 -29.573 8.582 26.500 1.00 96.70 C ANISOU 573 CA LEU A 78 12354 12617 11772 538 -502 -312 C ATOM 574 C LEU A 78 -29.942 7.169 26.054 1.00 96.54 C ANISOU 574 C LEU A 78 12320 12621 11741 511 -459 -295 C ATOM 575 O LEU A 78 -29.060 6.381 25.721 1.00 97.27 O ANISOU 575 O LEU A 78 12404 12681 11874 477 -418 -271 O ATOM 576 CB LEU A 78 -29.431 8.652 28.025 1.00 95.14 C ANISOU 576 CB LEU A 78 12117 12455 11579 557 -537 -320 C ATOM 577 CG LEU A 78 -28.307 9.546 28.546 1.00 95.43 C ANISOU 577 CG LEU A 78 12153 12445 11662 562 -560 -321 C ATOM 578 CD1 LEU A 78 -28.417 9.723 30.052 1.00 94.44 C ANISOU 578 CD1 LEU A 78 11993 12363 11528 589 -602 -335 C ATOM 579 CD2 LEU A 78 -26.941 8.986 28.171 1.00 95.55 C ANISOU 579 CD2 LEU A 78 12162 12402 11740 523 -518 -293 C ATOM 580 N PHE A 79 -31.245 6.861 26.053 1.00 94.85 N ANISOU 580 N PHE A 79 12102 12464 11472 527 -468 -309 N ATOM 581 CA PHE A 79 -31.705 5.514 25.756 1.00 92.39 C ANISOU 581 CA PHE A 79 11774 12182 11147 505 -432 -295 C ATOM 582 C PHE A 79 -31.421 5.162 24.297 1.00 91.72 C ANISOU 582 C PHE A 79 11722 12050 11076 476 -387 -278 C ATOM 583 O PHE A 79 -30.900 4.084 24.013 1.00 90.56 O ANISOU 583 O PHE A 79 11561 11890 10956 444 -347 -256 O ATOM 584 CB PHE A 79 -33.180 5.329 26.122 1.00 90.86 C ANISOU 584 CB PHE A 79 11568 12062 10893 530 -454 -315 C ATOM 585 CG PHE A 79 -33.683 3.921 25.925 1.00 90.49 C ANISOU 585 CG PHE A 79 11501 12048 10832 507 -420 -301 C ATOM 586 CD1 PHE A 79 -33.409 2.933 26.860 1.00 90.20 C ANISOU 586 CD1 PHE A 79 11422 12040 10809 492 -411 -286 C ATOM 587 CD2 PHE A 79 -34.411 3.577 24.795 1.00 90.06 C ANISOU 587 CD2 PHE A 79 11471 11996 10752 499 -398 -301 C ATOM 588 CE1 PHE A 79 -33.859 1.634 26.674 1.00 90.13 C ANISOU 588 CE1 PHE A 79 11396 12061 10788 470 -380 -271 C ATOM 589 CE2 PHE A 79 -34.863 2.278 24.609 1.00 89.67 C ANISOU 589 CE2 PHE A 79 11403 11977 10692 478 -368 -288 C ATOM 590 CZ PHE A 79 -34.586 1.309 25.549 1.00 90.24 C ANISOU 590 CZ PHE A 79 11433 12077 10778 463 -359 -273 C ATOM 591 N ILE A 80 -31.755 6.084 23.385 1.00 91.92 N ANISOU 591 N ILE A 80 11793 12051 11083 488 -397 -291 N ATOM 592 CA ILE A 80 -31.642 5.835 21.956 1.00 92.16 C ANISOU 592 CA ILE A 80 11860 12041 11117 464 -358 -279 C ATOM 593 C ILE A 80 -30.170 5.800 21.548 1.00 92.06 C ANISOU 593 C ILE A 80 11854 11960 11164 432 -324 -256 C ATOM 594 O ILE A 80 -29.830 5.231 20.512 1.00 93.79 O ANISOU 594 O ILE A 80 12091 12147 11397 403 -281 -240 O ATOM 595 CB ILE A 80 -32.459 6.846 21.121 1.00 91.86 C ANISOU 595 CB ILE A 80 11870 11994 11039 487 -381 -299 C ATOM 596 CG1 ILE A 80 -31.986 8.289 21.324 1.00 92.79 C ANISOU 596 CG1 ILE A 80 12011 12076 11170 507 -418 -312 C ATOM 597 CG2 ILE A 80 -33.950 6.691 21.387 1.00 91.23 C ANISOU 597 CG2 ILE A 80 11781 11982 10902 515 -407 -322 C ATOM 598 CD1 ILE A 80 -32.604 9.282 20.364 1.00 95.38 C ANISOU 598 CD1 ILE A 80 12392 12383 11466 524 -437 -328 C ATOM 599 N ALA A 81 -29.312 6.398 22.384 1.00 89.71 N ANISOU 599 N ALA A 81 11541 11643 10901 438 -345 -257 N ATOM 600 CA ALA A 81 -27.887 6.484 22.108 1.00 88.27 C ANISOU 600 CA ALA A 81 11362 11397 10778 410 -318 -239 C ATOM 601 C ALA A 81 -27.150 5.276 22.683 1.00 88.34 C ANISOU 601 C ALA A 81 11326 11411 10828 385 -290 -219 C ATOM 602 O ALA A 81 -26.111 4.884 22.155 1.00 88.04 O ANISOU 602 O ALA A 81 11289 11325 10836 354 -251 -201 O ATOM 603 CB ALA A 81 -27.331 7.778 22.645 1.00 87.04 C ANISOU 603 CB ALA A 81 11214 11213 10642 429 -356 -250 C ATOM 604 N CYS A 82 -27.700 4.690 23.756 1.00 89.11 N ANISOU 604 N CYS A 82 11386 11566 10907 399 -310 -223 N ATOM 605 CA CYS A 82 -26.990 3.680 24.527 1.00 89.36 C ANISOU 605 CA CYS A 82 11373 11602 10975 380 -295 -207 C ATOM 606 C CYS A 82 -27.575 2.282 24.327 1.00 88.91 C ANISOU 606 C CYS A 82 11299 11582 10900 363 -266 -195 C ATOM 607 O CYS A 82 -27.003 1.307 24.815 1.00 89.44 O ANISOU 607 O CYS A 82 11333 11650 10998 343 -250 -179 O ATOM 608 CB CYS A 82 -26.992 4.018 26.013 1.00 89.44 C ANISOU 608 CB CYS A 82 11352 11646 10984 405 -340 -217 C ATOM 609 SG CYS A 82 -25.843 5.349 26.445 1.00 91.66 S ANISOU 609 SG CYS A 82 11640 11873 11311 416 -368 -223 S ATOM 610 N PHE A 83 -28.706 2.176 23.616 1.00 86.85 N ANISOU 610 N PHE A 83 11060 11350 10590 370 -262 -203 N ATOM 611 CA PHE A 83 -29.362 0.884 23.482 1.00 85.82 C ANISOU 611 CA PHE A 83 10911 11257 10438 356 -239 -193 C ATOM 612 C PHE A 83 -28.512 -0.068 22.643 1.00 84.76 C ANISOU 612 C PHE A 83 10779 11080 10346 317 -187 -171 C ATOM 613 O PHE A 83 -28.559 -1.281 22.846 1.00 84.06 O ANISOU 613 O PHE A 83 10663 11011 10263 299 -168 -157 O ATOM 614 CB PHE A 83 -30.785 1.013 22.933 1.00 87.77 C ANISOU 614 CB PHE A 83 11181 11544 10624 374 -248 -210 C ATOM 615 CG PHE A 83 -31.504 -0.308 22.804 1.00 89.18 C ANISOU 615 CG PHE A 83 11341 11764 10781 359 -226 -200 C ATOM 616 CD1 PHE A 83 -31.980 -0.972 23.927 1.00 89.09 C ANISOU 616 CD1 PHE A 83 11289 11808 10753 365 -242 -200 C ATOM 617 CD2 PHE A 83 -31.683 -0.902 21.563 1.00 89.08 C ANISOU 617 CD2 PHE A 83 11351 11732 10764 339 -189 -192 C ATOM 618 CE1 PHE A 83 -32.628 -2.193 23.811 1.00 88.72 C ANISOU 618 CE1 PHE A 83 11224 11797 10687 349 -222 -191 C ATOM 619 CE2 PHE A 83 -32.331 -2.123 21.448 1.00 89.07 C ANISOU 619 CE2 PHE A 83 11332 11766 10744 325 -169 -183 C ATOM 620 CZ PHE A 83 -32.803 -2.766 22.571 1.00 88.91 C ANISOU 620 CZ PHE A 83 11271 11801 10709 330 -186 -182 C ATOM 621 N VAL A 84 -27.738 0.493 21.705 1.00 83.98 N ANISOU 621 N VAL A 84 10712 10922 10276 304 -165 -167 N ATOM 622 CA VAL A 84 -26.877 -0.294 20.835 1.00 82.14 C ANISOU 622 CA VAL A 84 10481 10643 10083 268 -115 -148 C ATOM 623 C VAL A 84 -25.749 -0.917 21.659 1.00 82.36 C ANISOU 623 C VAL A 84 10469 10656 10169 250 -107 -134 C ATOM 624 O VAL A 84 -25.210 -1.954 21.277 1.00 82.87 O ANISOU 624 O VAL A 84 10520 10702 10264 222 -69 -119 O ATOM 625 CB VAL A 84 -26.349 0.527 19.639 1.00 80.51 C ANISOU 625 CB VAL A 84 10320 10378 9890 257 -93 -149 C ATOM 626 CG1 VAL A 84 -25.452 1.681 20.064 1.00 79.60 C ANISOU 626 CG1 VAL A 84 10210 10225 9809 265 -114 -154 C ATOM 627 CG2 VAL A 84 -25.655 -0.345 18.605 1.00 78.98 C ANISOU 627 CG2 VAL A 84 10133 10145 9729 221 -37 -132 C ATOM 628 N LEU A 85 -25.417 -0.285 22.794 1.00 81.18 N ANISOU 628 N LEU A 85 10299 10513 10032 269 -144 -141 N ATOM 629 CA LEU A 85 -24.373 -0.772 23.683 1.00 80.06 C ANISOU 629 CA LEU A 85 10120 10357 9943 256 -145 -130 C ATOM 630 C LEU A 85 -24.843 -2.042 24.389 1.00 80.25 C ANISOU 630 C LEU A 85 10108 10428 9954 251 -146 -120 C ATOM 631 O LEU A 85 -24.032 -2.908 24.710 1.00 79.75 O ANISOU 631 O LEU A 85 10018 10350 9936 230 -130 -106 O ATOM 632 CB LEU A 85 -23.997 0.319 24.691 1.00 79.17 C ANISOU 632 CB LEU A 85 9999 10239 9841 281 -189 -141 C ATOM 633 CG LEU A 85 -23.445 1.617 24.099 1.00 79.16 C ANISOU 633 CG LEU A 85 10031 10188 9857 285 -192 -150 C ATOM 634 CD1 LEU A 85 -23.242 2.663 25.185 1.00 79.65 C ANISOU 634 CD1 LEU A 85 10084 10254 9925 313 -241 -163 C ATOM 635 CD2 LEU A 85 -22.145 1.375 23.346 1.00 78.63 C ANISOU 635 CD2 LEU A 85 9968 10057 9853 251 -148 -136 C ATOM 636 N VAL A 86 -26.159 -2.142 24.618 1.00 80.82 N ANISOU 636 N VAL A 86 10182 10559 9967 270 -166 -129 N ATOM 637 CA VAL A 86 -26.752 -3.320 25.230 1.00 81.03 C ANISOU 637 CA VAL A 86 10178 10635 9973 264 -166 -121 C ATOM 638 C VAL A 86 -26.622 -4.499 24.268 1.00 82.44 C ANISOU 638 C VAL A 86 10359 10797 10167 232 -120 -104 C ATOM 639 O VAL A 86 -26.302 -5.608 24.691 1.00 82.05 O ANISOU 639 O VAL A 86 10281 10755 10141 214 -109 -89 O ATOM 640 CB VAL A 86 -28.217 -3.075 25.649 1.00 79.88 C ANISOU 640 CB VAL A 86 10035 10557 9760 291 -197 -136 C ATOM 641 CG1 VAL A 86 -28.922 -4.356 26.070 1.00 78.93 C ANISOU 641 CG1 VAL A 86 9887 10486 9615 280 -191 -126 C ATOM 642 CG2 VAL A 86 -28.318 -2.031 26.750 1.00 80.60 C ANISOU 642 CG2 VAL A 86 10118 10668 9837 322 -244 -153 C ATOM 643 N LEU A 87 -26.853 -4.239 22.974 1.00 85.27 N ANISOU 643 N LEU A 87 10753 11132 10513 227 -94 -108 N ATOM 644 CA LEU A 87 -26.849 -5.275 21.951 1.00 87.10 C ANISOU 644 CA LEU A 87 10991 11349 10752 200 -50 -95 C ATOM 645 C LEU A 87 -25.424 -5.752 21.681 1.00 89.28 C ANISOU 645 C LEU A 87 11256 11569 11097 171 -18 -81 C ATOM 646 O LEU A 87 -25.222 -6.903 21.298 1.00 90.62 O ANISOU 646 O LEU A 87 11414 11733 11285 147 13 -68 O ATOM 647 CB LEU A 87 -27.500 -4.740 20.670 1.00 86.21 C ANISOU 647 CB LEU A 87 10923 11227 10605 204 -35 -105 C ATOM 648 CG LEU A 87 -28.988 -4.402 20.760 1.00 85.90 C ANISOU 648 CG LEU A 87 10896 11243 10499 231 -64 -121 C ATOM 649 CD1 LEU A 87 -29.471 -3.776 19.462 1.00 87.06 C ANISOU 649 CD1 LEU A 87 11091 11370 10618 236 -51 -131 C ATOM 650 CD2 LEU A 87 -29.815 -5.635 21.094 1.00 85.16 C ANISOU 650 CD2 LEU A 87 10777 11201 10380 225 -61 -114 C ATOM 651 N ALA A 88 -24.447 -4.856 21.876 1.00 89.58 N ANISOU 651 N ALA A 88 11298 11566 11173 174 -25 -85 N ATOM 652 CA ALA A 88 -23.046 -5.178 21.662 1.00 89.21 C ANISOU 652 CA ALA A 88 11238 11464 11194 148 4 -75 C ATOM 653 C ALA A 88 -22.531 -6.048 22.806 1.00 90.38 C ANISOU 653 C ALA A 88 11341 11624 11376 141 -9 -64 C ATOM 654 O ALA A 88 -21.773 -6.988 22.575 1.00 90.58 O ANISOU 654 O ALA A 88 11348 11623 11446 116 19 -53 O ATOM 655 CB ALA A 88 -22.236 -3.913 21.511 1.00 88.30 C ANISOU 655 CB ALA A 88 11140 11302 11106 154 -1 -83 C ATOM 656 N GLN A 89 -22.963 -5.734 24.035 1.00 91.54 N ANISOU 656 N GLN A 89 11471 11812 11501 165 -54 -69 N ATOM 657 CA GLN A 89 -22.517 -6.450 25.220 1.00 92.59 C ANISOU 657 CA GLN A 89 11564 11957 11661 161 -73 -60 C ATOM 658 C GLN A 89 -23.107 -7.859 25.235 1.00 93.83 C ANISOU 658 C GLN A 89 11704 12148 11800 146 -59 -47 C ATOM 659 O GLN A 89 -22.481 -8.784 25.749 1.00 95.00 O ANISOU 659 O GLN A 89 11823 12288 11986 129 -56 -34 O ATOM 660 CB GLN A 89 -22.875 -5.683 26.495 1.00 92.23 C ANISOU 660 CB GLN A 89 11507 11946 11589 190 -123 -70 C ATOM 661 CG GLN A 89 -21.963 -6.009 27.671 1.00 92.33 C ANISOU 661 CG GLN A 89 11484 11949 11647 187 -145 -62 C ATOM 662 CD GLN A 89 -20.522 -5.657 27.390 1.00 92.63 C ANISOU 662 CD GLN A 89 11520 11919 11755 174 -130 -62 C ATOM 663 OE1 GLN A 89 -20.208 -4.562 26.929 1.00 93.14 O ANISOU 663 OE1 GLN A 89 11607 11954 11829 182 -129 -72 O ATOM 664 NE2 GLN A 89 -19.629 -6.594 27.667 1.00 92.51 N ANISOU 664 NE2 GLN A 89 11477 11880 11792 153 -118 -49 N ATOM 665 N SER A 90 -24.309 -8.006 24.665 1.00 94.77 N ANISOU 665 N SER A 90 11842 12304 11864 151 -53 -50 N ATOM 666 CA SER A 90 -24.979 -9.294 24.585 1.00 95.09 C ANISOU 666 CA SER A 90 11869 12377 11883 137 -40 -39 C ATOM 667 C SER A 90 -24.220 -10.221 23.638 1.00 95.20 C ANISOU 667 C SER A 90 11882 12347 11942 106 5 -27 C ATOM 668 O SER A 90 -24.111 -11.419 23.894 1.00 94.92 O ANISOU 668 O SER A 90 11823 12319 11922 88 13 -13 O ATOM 669 CB SER A 90 -26.418 -9.136 24.167 1.00 95.53 C ANISOU 669 CB SER A 90 11945 12480 11871 151 -44 -48 C ATOM 670 OG SER A 90 -27.101 -10.377 24.256 1.00 98.32 O ANISOU 670 OG SER A 90 12283 12871 12205 138 -36 -37 O ATOM 671 N SER A 91 -23.688 -9.641 22.556 1.00 96.03 N ANISOU 671 N SER A 91 12014 12406 12068 99 33 -33 N ATOM 672 CA SER A 91 -23.001 -10.393 21.520 1.00 97.03 C ANISOU 672 CA SER A 91 12144 12489 12233 71 79 -25 C ATOM 673 C SER A 91 -21.665 -10.924 22.036 1.00 97.52 C ANISOU 673 C SER A 91 12175 12514 12366 54 85 -17 C ATOM 674 O SER A 91 -21.280 -12.044 21.709 1.00 98.51 O ANISOU 674 O SER A 91 12285 12625 12520 31 110 -7 O ATOM 675 CB SER A 91 -22.827 -9.568 20.272 1.00 96.92 C ANISOU 675 CB SER A 91 12169 12439 12218 69 107 -34 C ATOM 676 OG SER A 91 -24.088 -9.216 19.721 1.00 96.81 O ANISOU 676 OG SER A 91 12185 12458 12139 84 102 -42 O ATOM 677 N ILE A 92 -20.973 -10.110 22.844 1.00 97.05 N ANISOU 677 N ILE A 92 12103 12438 12332 66 59 -22 N ATOM 678 CA ILE A 92 -19.675 -10.476 23.391 1.00 96.87 C ANISOU 678 CA ILE A 92 12050 12378 12378 52 59 -16 C ATOM 679 C ILE A 92 -19.843 -11.675 24.324 1.00 97.84 C ANISOU 679 C ILE A 92 12140 12530 12503 46 41 -3 C ATOM 680 O ILE A 92 -19.072 -12.629 24.243 1.00 99.09 O ANISOU 680 O ILE A 92 12278 12662 12711 25 58 5 O ATOM 681 CB ILE A 92 -18.987 -9.270 24.068 1.00 96.35 C ANISOU 681 CB ILE A 92 11982 12290 12336 68 32 -25 C ATOM 682 CG1 ILE A 92 -18.411 -8.305 23.028 1.00 95.95 C ANISOU 682 CG1 ILE A 92 11959 12192 12305 64 60 -35 C ATOM 683 CG2 ILE A 92 -17.922 -9.727 25.056 1.00 95.79 C ANISOU 683 CG2 ILE A 92 11873 12198 12324 62 15 -20 C ATOM 684 CD1 ILE A 92 -17.977 -6.965 23.583 1.00 96.63 C ANISOU 684 CD1 ILE A 92 12051 12262 12403 82 30 -46 C ATOM 685 N PHE A 93 -20.869 -11.624 25.183 1.00 97.92 N ANISOU 685 N PHE A 93 12146 12597 12461 65 5 -2 N ATOM 686 CA PHE A 93 -21.155 -12.705 26.113 1.00 97.41 C ANISOU 686 CA PHE A 93 12055 12566 12391 59 -15 11 C ATOM 687 C PHE A 93 -21.508 -13.978 25.346 1.00 96.38 C ANISOU 687 C PHE A 93 11924 12441 12257 36 17 22 C ATOM 688 O PHE A 93 -21.135 -15.073 25.764 1.00 96.58 O ANISOU 688 O PHE A 93 11925 12462 12311 20 15 35 O ATOM 689 CB PHE A 93 -22.254 -12.309 27.103 1.00 98.16 C ANISOU 689 CB PHE A 93 12148 12723 12424 83 -55 8 C ATOM 690 CG PHE A 93 -21.884 -11.209 28.068 1.00 99.09 C ANISOU 690 CG PHE A 93 12263 12841 12548 106 -92 -2 C ATOM 691 CD1 PHE A 93 -20.560 -10.970 28.408 1.00 99.55 C ANISOU 691 CD1 PHE A 93 12306 12849 12669 101 -97 -2 C ATOM 692 CD2 PHE A 93 -22.865 -10.424 28.658 1.00 99.54 C ANISOU 692 CD2 PHE A 93 12327 12946 12546 132 -123 -12 C ATOM 693 CE1 PHE A 93 -20.226 -9.960 29.299 1.00100.46 C ANISOU 693 CE1 PHE A 93 12417 12962 12789 122 -132 -11 C ATOM 694 CE2 PHE A 93 -22.530 -9.416 29.551 1.00 98.87 C ANISOU 694 CE2 PHE A 93 12239 12860 12466 154 -159 -22 C ATOM 695 CZ PHE A 93 -21.211 -9.185 29.870 1.00 99.27 C ANISOU 695 CZ PHE A 93 12277 12861 12581 149 -163 -21 C ATOM 696 N SER A 94 -22.218 -13.815 24.222 1.00 93.74 N ANISOU 696 N SER A 94 11617 12112 11887 36 43 17 N ATOM 697 CA SER A 94 -22.604 -14.933 23.374 1.00 91.64 C ANISOU 697 CA SER A 94 11354 11849 11615 16 74 25 C ATOM 698 C SER A 94 -21.377 -15.534 22.692 1.00 90.35 C ANISOU 698 C SER A 94 11182 11627 11518 -8 109 28 C ATOM 699 O SER A 94 -21.272 -16.753 22.572 1.00 89.93 O ANISOU 699 O SER A 94 11113 11571 11484 -27 122 39 O ATOM 700 CB SER A 94 -23.651 -14.527 22.370 1.00 91.63 C ANISOU 700 CB SER A 94 11387 11868 11559 24 91 16 C ATOM 701 OG SER A 94 -24.917 -14.377 22.993 1.00 91.62 O ANISOU 701 OG SER A 94 11387 11928 11497 42 61 14 O ATOM 702 N LEU A 95 -20.455 -14.664 22.259 1.00 88.59 N ANISOU 702 N LEU A 95 10970 11358 11332 -7 124 18 N ATOM 703 CA LEU A 95 -19.236 -15.092 21.591 1.00 86.81 C ANISOU 703 CA LEU A 95 10736 11076 11173 -30 160 18 C ATOM 704 C LEU A 95 -18.299 -15.766 22.591 1.00 86.82 C ANISOU 704 C LEU A 95 10697 11060 11229 -38 141 25 C ATOM 705 O LEU A 95 -17.605 -16.718 22.239 1.00 87.23 O ANISOU 705 O LEU A 95 10733 11082 11328 -59 163 29 O ATOM 706 CB LEU A 95 -18.563 -13.887 20.926 1.00 85.15 C ANISOU 706 CB LEU A 95 10547 10824 10982 -27 179 5 C ATOM 707 CG LEU A 95 -19.141 -13.465 19.576 1.00 83.95 C ANISOU 707 CG LEU A 95 10435 10668 10793 -29 212 -2 C ATOM 708 CD1 LEU A 95 -18.559 -12.131 19.134 1.00 83.96 C ANISOU 708 CD1 LEU A 95 10461 10634 10808 -24 221 -13 C ATOM 709 CD2 LEU A 95 -18.887 -14.530 18.522 1.00 83.88 C ANISOU 709 CD2 LEU A 95 10428 10637 10806 -54 256 2 C ATOM 710 N LEU A 96 -18.296 -15.267 23.834 1.00 86.03 N ANISOU 710 N LEU A 96 10584 10979 11124 -21 97 26 N ATOM 711 CA LEU A 96 -17.443 -15.804 24.882 1.00 86.41 C ANISOU 711 CA LEU A 96 10598 11013 11222 -26 73 33 C ATOM 712 C LEU A 96 -17.955 -17.176 25.319 1.00 86.65 C ANISOU 712 C LEU A 96 10611 11074 11240 -37 62 48 C ATOM 713 O LEU A 96 -17.163 -18.049 25.667 1.00 86.53 O ANISOU 713 O LEU A 96 10570 11033 11275 -51 59 55 O ATOM 714 CB LEU A 96 -17.396 -14.812 26.052 1.00 86.79 C ANISOU 714 CB LEU A 96 10641 11076 11260 -3 29 28 C ATOM 715 CG LEU A 96 -16.468 -15.168 27.216 1.00 87.24 C ANISOU 715 CG LEU A 96 10665 11115 11367 -4 -2 33 C ATOM 716 CD1 LEU A 96 -15.047 -15.432 26.738 1.00 87.66 C ANISOU 716 CD1 LEU A 96 10702 11104 11502 -22 23 29 C ATOM 717 CD2 LEU A 96 -16.477 -14.067 28.264 1.00 87.26 C ANISOU 717 CD2 LEU A 96 10667 11132 11356 21 -44 27 C ATOM 718 N ALA A 97 -19.282 -17.357 25.280 1.00 86.33 N ANISOU 718 N ALA A 97 10585 11086 11132 -30 56 54 N ATOM 719 CA ALA A 97 -19.911 -18.605 25.682 1.00 86.43 C ANISOU 719 CA ALA A 97 10583 11131 11124 -41 46 69 C ATOM 720 C ALA A 97 -19.608 -19.702 24.664 1.00 87.06 C ANISOU 720 C ALA A 97 10661 11182 11234 -66 84 74 C ATOM 721 O ALA A 97 -19.337 -20.841 25.039 1.00 87.60 O ANISOU 721 O ALA A 97 10708 11246 11329 -81 77 86 O ATOM 722 CB ALA A 97 -21.395 -18.406 25.853 1.00 85.67 C ANISOU 722 CB ALA A 97 10503 11098 10950 -28 32 71 C ATOM 723 N ILE A 98 -19.656 -19.341 23.376 1.00 87.46 N ANISOU 723 N ILE A 98 10736 11214 11282 -69 123 63 N ATOM 724 CA ILE A 98 -19.412 -20.286 22.297 1.00 88.06 C ANISOU 724 CA ILE A 98 10814 11264 11382 -90 162 65 C ATOM 725 C ILE A 98 -17.978 -20.805 22.397 1.00 88.81 C ANISOU 725 C ILE A 98 10882 11304 11557 -106 170 64 C ATOM 726 O ILE A 98 -17.742 -21.998 22.217 1.00 88.65 O ANISOU 726 O ILE A 98 10847 11273 11565 -123 180 71 O ATOM 727 CB ILE A 98 -19.742 -19.667 20.921 1.00 88.09 C ANISOU 727 CB ILE A 98 10852 11257 11362 -89 200 53 C ATOM 728 CG1 ILE A 98 -21.255 -19.504 20.738 1.00 87.99 C ANISOU 728 CG1 ILE A 98 10863 11299 11272 -77 192 55 C ATOM 729 CG2 ILE A 98 -19.128 -20.479 19.788 1.00 87.91 C ANISOU 729 CG2 ILE A 98 10830 11194 11380 -112 244 51 C ATOM 730 CD1 ILE A 98 -21.660 -18.656 19.552 1.00 88.36 C ANISOU 730 CD1 ILE A 98 10947 11339 11288 -71 220 42 C ATOM 731 N ALA A 99 -17.040 -19.903 22.713 1.00 90.18 N ANISOU 731 N ALA A 99 11050 11447 11769 -98 164 54 N ATOM 732 CA ALA A 99 -15.630 -20.235 22.850 1.00 91.00 C ANISOU 732 CA ALA A 99 11126 11497 11951 -111 170 50 C ATOM 733 C ALA A 99 -15.428 -21.241 23.982 1.00 92.70 C ANISOU 733 C ALA A 99 11311 11721 12189 -115 134 63 C ATOM 734 O ALA A 99 -14.674 -22.202 23.828 1.00 94.71 O ANISOU 734 O ALA A 99 11545 11944 12497 -132 144 64 O ATOM 735 CB ALA A 99 -14.822 -18.980 23.070 1.00 89.66 C ANISOU 735 CB ALA A 99 10957 11299 11810 -100 166 37 C ATOM 736 N ILE A 100 -16.115 -21.010 25.110 1.00 92.82 N ANISOU 736 N ILE A 100 11325 11780 12163 -100 91 73 N ATOM 737 CA ILE A 100 -15.999 -21.863 26.284 1.00 92.90 C ANISOU 737 CA ILE A 100 11310 11801 12185 -104 52 87 C ATOM 738 C ILE A 100 -16.677 -23.203 26.004 1.00 94.56 C ANISOU 738 C ILE A 100 11519 12033 12377 -121 60 101 C ATOM 739 O ILE A 100 -16.156 -24.250 26.382 1.00 93.78 O ANISOU 739 O ILE A 100 11398 11916 12317 -134 48 110 O ATOM 740 CB ILE A 100 -16.547 -21.163 27.549 1.00 90.76 C ANISOU 740 CB ILE A 100 11040 11572 11872 -84 7 92 C ATOM 741 CG1 ILE A 100 -15.684 -19.961 27.943 1.00 90.16 C ANISOU 741 CG1 ILE A 100 10961 11468 11829 -69 -6 78 C ATOM 742 CG2 ILE A 100 -16.692 -22.148 28.701 1.00 89.29 C ANISOU 742 CG2 ILE A 100 10834 11407 11684 -90 -32 110 C ATOM 743 CD1 ILE A 100 -16.150 -19.236 29.187 1.00 90.33 C ANISOU 743 CD1 ILE A 100 10984 11528 11811 -47 -51 81 C ATOM 744 N ASP A 101 -17.827 -23.155 25.320 1.00 98.18 N ANISOU 744 N ASP A 101 12001 12528 12775 -119 78 102 N ATOM 745 CA ASP A 101 -18.582 -24.352 24.984 1.00102.00 C ANISOU 745 CA ASP A 101 12485 13034 13235 -134 86 115 C ATOM 746 C ASP A 101 -17.746 -25.260 24.083 1.00104.72 C ANISOU 746 C ASP A 101 12820 13330 13638 -154 118 111 C ATOM 747 O ASP A 101 -17.815 -26.482 24.199 1.00103.91 O ANISOU 747 O ASP A 101 12705 13229 13548 -169 112 123 O ATOM 748 CB ASP A 101 -19.933 -24.012 24.349 1.00102.33 C ANISOU 748 CB ASP A 101 12554 13121 13204 -127 100 114 C ATOM 749 CG ASP A 101 -20.762 -25.241 24.022 1.00103.79 C ANISOU 749 CG ASP A 101 12741 13332 13364 -142 107 126 C ATOM 750 OD1 ASP A 101 -21.290 -25.861 24.967 1.00106.57 O ANISOU 750 OD1 ASP A 101 13081 13718 13694 -146 75 142 O ATOM 751 OD2 ASP A 101 -20.852 -25.581 22.829 1.00103.22 O ANISOU 751 OD2 ASP A 101 12681 13243 13296 -151 143 121 O ATOM 752 N ARG A 102 -16.957 -24.644 23.193 1.00108.74 N ANISOU 752 N ARG A 102 13335 13797 14183 -154 152 94 N ATOM 753 CA ARG A 102 -16.105 -25.376 22.268 1.00110.75 C ANISOU 753 CA ARG A 102 13581 14004 14494 -172 188 86 C ATOM 754 C ARG A 102 -14.855 -25.880 22.985 1.00112.03 C ANISOU 754 C ARG A 102 13709 14126 14730 -179 168 86 C ATOM 755 O ARG A 102 -14.258 -26.867 22.561 1.00112.72 O ANISOU 755 O ARG A 102 13782 14183 14865 -195 183 84 O ATOM 756 CB ARG A 102 -15.744 -24.519 21.050 1.00111.63 C ANISOU 756 CB ARG A 102 13713 14088 14614 -171 233 68 C ATOM 757 CG ARG A 102 -16.851 -24.393 20.011 1.00113.55 C ANISOU 757 CG ARG A 102 13989 14359 14796 -170 261 67 C ATOM 758 CD ARG A 102 -17.286 -25.710 19.395 1.00115.80 C ANISOU 758 CD ARG A 102 14273 14649 15076 -186 277 74 C ATOM 759 NE ARG A 102 -18.306 -26.379 20.193 1.00118.89 N ANISOU 759 NE ARG A 102 14660 15089 15425 -185 242 92 N ATOM 760 CZ ARG A 102 -18.620 -27.669 20.107 1.00122.12 C ANISOU 760 CZ ARG A 102 15059 15504 15836 -199 240 103 C ATOM 761 NH1 ARG A 102 -17.987 -28.456 19.253 1.00125.52 N ANISOU 761 NH1 ARG A 102 15483 15896 16310 -215 270 96 N ATOM 762 NH2 ARG A 102 -19.567 -28.168 20.880 1.00121.84 N ANISOU 762 NH2 ARG A 102 15021 15515 15759 -199 207 120 N ATOM 763 N TYR A 103 -14.469 -25.198 24.069 1.00113.98 N ANISOU 763 N TYR A 103 13946 14374 14988 -166 133 86 N ATOM 764 CA TYR A 103 -13.291 -25.595 24.823 1.00117.43 C ANISOU 764 CA TYR A 103 14351 14772 15493 -171 110 85 C ATOM 765 C TYR A 103 -13.601 -26.806 25.701 1.00117.51 C ANISOU 765 C TYR A 103 14347 14801 15500 -179 73 104 C ATOM 766 O TYR A 103 -12.762 -27.691 25.842 1.00117.28 O ANISOU 766 O TYR A 103 14295 14737 15530 -190 66 104 O ATOM 767 CB TYR A 103 -12.719 -24.432 25.637 1.00121.34 C ANISOU 767 CB TYR A 103 14842 15258 16004 -154 85 78 C ATOM 768 CG TYR A 103 -11.565 -24.825 26.525 1.00125.01 C ANISOU 768 CG TYR A 103 15275 15687 16538 -157 55 77 C ATOM 769 CD1 TYR A 103 -10.342 -25.194 25.985 1.00126.29 C ANISOU 769 CD1 TYR A 103 15415 15792 16776 -169 78 62 C ATOM 770 CD2 TYR A 103 -11.700 -24.850 27.904 1.00127.22 C ANISOU 770 CD2 TYR A 103 15546 15988 16806 -147 3 89 C ATOM 771 CE1 TYR A 103 -9.279 -25.567 26.791 1.00129.58 C ANISOU 771 CE1 TYR A 103 15802 16173 17259 -170 48 59 C ATOM 772 CE2 TYR A 103 -10.646 -25.219 28.726 1.00130.91 C ANISOU 772 CE2 TYR A 103 15985 16419 17335 -149 -28 88 C ATOM 773 CZ TYR A 103 -9.431 -25.578 28.167 1.00132.16 C ANISOU 773 CZ TYR A 103 16122 16521 17573 -160 -6 72 C ATOM 774 OH TYR A 103 -8.387 -25.943 28.968 1.00136.48 O ANISOU 774 OH TYR A 103 16641 17031 18184 -160 -39 69 O ATOM 775 N ILE A 104 -14.804 -26.828 26.288 1.00117.46 N ANISOU 775 N ILE A 104 14354 14850 15424 -173 49 120 N ATOM 776 CA ILE A 104 -15.230 -27.929 27.139 1.00116.54 C ANISOU 776 CA ILE A 104 14227 14757 15295 -182 14 141 C ATOM 777 C ILE A 104 -15.430 -29.174 26.277 1.00117.33 C ANISOU 777 C ILE A 104 14326 14848 15405 -201 38 146 C ATOM 778 O ILE A 104 -15.172 -30.288 26.727 1.00119.74 O ANISOU 778 O ILE A 104 14615 15142 15738 -214 16 157 O ATOM 779 CB ILE A 104 -16.498 -27.564 27.942 1.00115.78 C ANISOU 779 CB ILE A 104 14145 14725 15119 -171 -14 155 C ATOM 780 CG1 ILE A 104 -16.266 -26.362 28.862 1.00115.33 C ANISOU 780 CG1 ILE A 104 14089 14677 15055 -150 -41 150 C ATOM 781 CG2 ILE A 104 -17.015 -28.768 28.718 1.00116.68 C ANISOU 781 CG2 ILE A 104 14251 14865 15216 -184 -45 178 C ATOM 782 CD1 ILE A 104 -17.527 -25.806 29.487 1.00114.49 C ANISOU 782 CD1 ILE A 104 13998 14634 14868 -137 -62 158 C ATOM 783 N ALA A 105 -15.870 -28.967 25.031 1.00118.50 N ANISOU 783 N ALA A 105 14493 15000 15531 -203 82 136 N ATOM 784 CA ALA A 105 -16.169 -30.059 24.118 1.00119.69 C ANISOU 784 CA ALA A 105 14647 15146 15685 -220 107 139 C ATOM 785 C ALA A 105 -14.890 -30.759 23.662 1.00119.86 C ANISOU 785 C ALA A 105 14646 15107 15787 -232 123 127 C ATOM 786 O ALA A 105 -14.932 -31.933 23.299 1.00120.43 O ANISOU 786 O ALA A 105 14711 15169 15876 -247 128 132 O ATOM 787 CB ALA A 105 -16.978 -29.553 22.947 1.00120.50 C ANISOU 787 CB ALA A 105 14777 15268 15740 -216 147 131 C ATOM 788 N ILE A 106 -13.759 -30.040 23.688 1.00120.55 N ANISOU 788 N ILE A 106 14722 15154 15927 -226 130 111 N ATOM 789 CA ILE A 106 -12.513 -30.587 23.168 1.00122.89 C ANISOU 789 CA ILE A 106 14997 15394 16304 -237 149 95 C ATOM 790 C ILE A 106 -11.578 -31.001 24.306 1.00125.38 C ANISOU 790 C ILE A 106 15281 15681 16675 -238 106 98 C ATOM 791 O ILE A 106 -10.719 -31.857 24.109 1.00127.36 O ANISOU 791 O ILE A 106 15510 15891 16990 -248 109 90 O ATOM 792 CB ILE A 106 -11.834 -29.635 22.160 1.00121.42 C ANISOU 792 CB ILE A 106 14816 15176 16143 -234 196 71 C ATOM 793 CG1 ILE A 106 -11.045 -30.418 21.105 1.00120.54 C ANISOU 793 CG1 ILE A 106 14692 15019 16088 -250 234 55 C ATOM 794 CG2 ILE A 106 -10.967 -28.603 22.870 1.00121.54 C ANISOU 794 CG2 ILE A 106 14819 15169 16191 -222 179 62 C ATOM 795 CD1 ILE A 106 -10.580 -29.593 19.926 1.00123.08 C ANISOU 795 CD1 ILE A 106 15025 15316 16423 -251 288 33 C ATOM 796 N ALA A 107 -11.743 -30.389 25.485 1.00126.77 N ANISOU 796 N ALA A 107 15458 15880 16830 -225 66 108 N ATOM 797 CA ALA A 107 -10.871 -30.672 26.614 1.00129.28 C ANISOU 797 CA ALA A 107 15750 16173 17198 -223 22 111 C ATOM 798 C ALA A 107 -11.286 -31.985 27.271 1.00131.97 C ANISOU 798 C ALA A 107 16084 16527 17530 -235 -14 133 C ATOM 799 O ALA A 107 -10.523 -32.949 27.272 1.00135.80 O ANISOU 799 O ALA A 107 16549 16975 18075 -246 -23 130 O ATOM 800 CB ALA A 107 -10.887 -29.523 27.593 1.00129.63 C ANISOU 800 CB ALA A 107 15798 16234 17221 -205 -8 113 C ATOM 801 N ILE A 108 -12.505 -32.004 27.819 1.00133.15 N ANISOU 801 N ILE A 108 16252 16732 17606 -233 -35 154 N ATOM 802 CA ILE A 108 -13.045 -33.171 28.497 1.00136.37 C ANISOU 802 CA ILE A 108 16658 17161 17995 -245 -69 178 C ATOM 803 C ILE A 108 -14.347 -33.582 27.811 1.00140.57 C ANISOU 803 C ILE A 108 17211 17736 18463 -254 -46 189 C ATOM 804 O ILE A 108 -15.432 -33.245 28.283 1.00140.09 O ANISOU 804 O ILE A 108 17167 17729 18334 -249 -59 203 O ATOM 805 CB ILE A 108 -13.224 -32.895 30.006 1.00135.68 C ANISOU 805 CB ILE A 108 16571 17100 17883 -237 -122 194 C ATOM 806 CG1 ILE A 108 -13.746 -31.479 30.270 1.00133.84 C ANISOU 806 CG1 ILE A 108 16353 16902 17598 -218 -119 190 C ATOM 807 CG2 ILE A 108 -11.925 -33.165 30.752 1.00137.48 C ANISOU 807 CG2 ILE A 108 16774 17278 18185 -237 -156 189 C ATOM 808 CD1 ILE A 108 -14.143 -31.213 31.706 1.00135.99 C ANISOU 808 CD1 ILE A 108 16628 17210 17832 -210 -168 206 C ATOM 809 N PRO A 109 -14.285 -34.315 26.672 1.00144.75 N ANISOU 809 N PRO A 109 17740 18244 19014 -266 -12 181 N ATOM 810 CA PRO A 109 -15.493 -34.739 25.959 1.00148.75 C ANISOU 810 CA PRO A 109 18266 18789 19463 -274 10 190 C ATOM 811 C PRO A 109 -16.375 -35.709 26.745 1.00153.23 C ANISOU 811 C PRO A 109 18836 19393 19992 -286 -26 218 C ATOM 812 O PRO A 109 -17.550 -35.875 26.425 1.00154.57 O ANISOU 812 O PRO A 109 19022 19605 20101 -290 -16 228 O ATOM 813 CB PRO A 109 -14.958 -35.398 24.676 1.00146.88 C ANISOU 813 CB PRO A 109 18024 18511 19273 -285 49 174 C ATOM 814 CG PRO A 109 -13.539 -35.802 25.016 1.00145.47 C ANISOU 814 CG PRO A 109 17818 18276 19179 -288 34 164 C ATOM 815 CD PRO A 109 -13.052 -34.759 26.000 1.00144.63 C ANISOU 815 CD PRO A 109 17705 18168 19079 -272 8 162 C ATOM 816 N LEU A 110 -15.799 -36.338 27.777 1.00158.93 N ANISOU 816 N LEU A 110 19541 20097 20747 -293 -69 230 N ATOM 817 CA LEU A 110 -16.530 -37.267 28.624 1.00162.69 C ANISOU 817 CA LEU A 110 20020 20604 21191 -306 -107 257 C ATOM 818 C LEU A 110 -17.430 -36.490 29.583 1.00164.69 C ANISOU 818 C LEU A 110 20286 20915 21374 -297 -129 271 C ATOM 819 O LEU A 110 -18.579 -36.869 29.799 1.00165.50 O ANISOU 819 O LEU A 110 20400 21065 21417 -306 -137 290 O ATOM 820 CB LEU A 110 -15.538 -38.155 29.383 1.00163.59 C ANISOU 820 CB LEU A 110 20113 20675 21367 -316 -147 264 C ATOM 821 CG LEU A 110 -14.684 -39.088 28.523 1.00164.21 C ANISOU 821 CG LEU A 110 20177 20698 21516 -326 -131 251 C ATOM 822 CD1 LEU A 110 -13.662 -39.827 29.373 1.00164.14 C ANISOU 822 CD1 LEU A 110 20148 20646 21570 -332 -175 255 C ATOM 823 CD2 LEU A 110 -15.551 -40.075 27.754 1.00163.06 C ANISOU 823 CD2 LEU A 110 20042 20571 21344 -343 -113 261 C ATOM 824 N ARG A 111 -16.895 -35.395 30.137 1.00167.41 N ANISOU 824 N ARG A 111 20628 21254 21728 -279 -139 261 N ATOM 825 CA ARG A 111 -17.590 -34.602 31.139 1.00169.64 C ANISOU 825 CA ARG A 111 20920 21586 21950 -267 -164 271 C ATOM 826 C ARG A 111 -18.535 -33.599 30.477 1.00170.33 C ANISOU 826 C ARG A 111 21026 21715 21979 -254 -131 260 C ATOM 827 O ARG A 111 -19.289 -32.918 31.171 1.00169.84 O ANISOU 827 O ARG A 111 20972 21699 21859 -244 -146 266 O ATOM 828 CB ARG A 111 -16.584 -33.881 32.043 1.00171.79 C ANISOU 828 CB ARG A 111 21181 21832 22260 -253 -193 263 C ATOM 829 CG ARG A 111 -15.797 -34.790 32.978 1.00173.39 C ANISOU 829 CG ARG A 111 21368 22002 22509 -264 -237 276 C ATOM 830 CD ARG A 111 -16.642 -35.446 34.055 1.00176.60 C ANISOU 830 CD ARG A 111 21783 22453 22865 -276 -276 305 C ATOM 831 NE ARG A 111 -17.344 -34.483 34.896 1.00179.90 N ANISOU 831 NE ARG A 111 22212 22923 23219 -262 -291 310 N ATOM 832 CZ ARG A 111 -18.331 -34.781 35.737 1.00181.21 C ANISOU 832 CZ ARG A 111 22388 23141 23322 -270 -315 333 C ATOM 833 NH1 ARG A 111 -18.901 -33.824 36.449 1.00179.06 N ANISOU 833 NH1 ARG A 111 22124 22914 22996 -255 -327 333 N ATOM 834 NH2 ARG A 111 -18.749 -36.028 35.863 1.00184.15 N ANISOU 834 NH2 ARG A 111 22762 23522 23686 -294 -328 355 N ATOM 835 N TYR A 112 -18.498 -33.520 29.140 1.00169.97 N ANISOU 835 N TYR A 112 20985 21650 21945 -254 -86 244 N ATOM 836 CA TYR A 112 -19.260 -32.521 28.403 1.00168.60 C ANISOU 836 CA TYR A 112 20830 21506 21723 -241 -54 232 C ATOM 837 C TYR A 112 -20.762 -32.753 28.564 1.00167.92 C ANISOU 837 C TYR A 112 20759 21485 21560 -245 -59 247 C ATOM 838 O TYR A 112 -21.539 -31.803 28.531 1.00167.58 O ANISOU 838 O TYR A 112 20729 21480 21463 -230 -52 241 O ATOM 839 CB TYR A 112 -18.846 -32.475 26.928 1.00167.92 C ANISOU 839 CB TYR A 112 20749 21383 21669 -242 -6 212 C ATOM 840 CG TYR A 112 -19.605 -31.472 26.093 1.00166.57 C ANISOU 840 CG TYR A 112 20601 21239 21449 -229 27 199 C ATOM 841 CD1 TYR A 112 -19.240 -30.134 26.071 1.00163.94 C ANISOU 841 CD1 TYR A 112 20274 20899 21117 -210 35 183 C ATOM 842 CD2 TYR A 112 -20.696 -31.857 25.329 1.00167.13 C ANISOU 842 CD2 TYR A 112 20687 21341 21473 -235 48 203 C ATOM 843 CE1 TYR A 112 -19.933 -29.206 25.310 1.00163.10 C ANISOU 843 CE1 TYR A 112 20190 20814 20965 -197 62 172 C ATOM 844 CE2 TYR A 112 -21.402 -30.941 24.565 1.00166.70 C ANISOU 844 CE2 TYR A 112 20655 21310 21374 -222 75 191 C ATOM 845 CZ TYR A 112 -21.019 -29.610 24.554 1.00164.30 C ANISOU 845 CZ TYR A 112 20358 20997 21070 -203 81 175 C ATOM 846 OH TYR A 112 -21.710 -28.703 23.804 1.00163.53 O ANISOU 846 OH TYR A 112 20285 20920 20929 -190 105 163 O ATOM 847 N ASN A 113 -21.156 -34.019 28.745 1.00169.73 N ANISOU 847 N ASN A 113 20983 21723 21784 -266 -72 267 N ATOM 848 CA ASN A 113 -22.560 -34.396 28.806 1.00172.35 C ANISOU 848 CA ASN A 113 21325 22112 22047 -274 -74 281 C ATOM 849 C ASN A 113 -23.165 -33.998 30.152 1.00171.50 C ANISOU 849 C ASN A 113 21218 22054 21890 -269 -110 295 C ATOM 850 O ASN A 113 -24.378 -33.821 30.258 1.00169.73 O ANISOU 850 O ASN A 113 21003 21886 21601 -268 -109 300 O ATOM 851 CB ASN A 113 -22.754 -35.886 28.515 1.00174.30 C ANISOU 851 CB ASN A 113 21567 22350 22308 -299 -75 297 C ATOM 852 CG ASN A 113 -22.249 -36.283 27.145 1.00175.95 C ANISOU 852 CG ASN A 113 21778 22515 22562 -304 -38 282 C ATOM 853 OD1 ASN A 113 -22.940 -36.103 26.145 1.00178.51 O ANISOU 853 OD1 ASN A 113 22115 22854 22856 -301 -6 273 O ATOM 854 ND2 ASN A 113 -21.042 -36.822 27.091 1.00176.79 N ANISOU 854 ND2 ASN A 113 21868 22564 22738 -310 -43 278 N ATOM 855 N GLY A 114 -22.308 -33.856 31.169 1.00169.81 N ANISOU 855 N GLY A 114 20993 21820 21707 -265 -142 299 N ATOM 856 CA GLY A 114 -22.752 -33.585 32.527 1.00167.72 C ANISOU 856 CA GLY A 114 20728 21597 21400 -262 -180 313 C ATOM 857 C GLY A 114 -22.619 -32.113 32.913 1.00167.16 C ANISOU 857 C GLY A 114 20662 21540 21313 -234 -183 296 C ATOM 858 O GLY A 114 -23.370 -31.626 33.757 1.00168.73 O ANISOU 858 O GLY A 114 20865 21789 21456 -227 -203 301 O ATOM 859 N LEU A 115 -21.659 -31.418 32.290 1.00163.41 N ANISOU 859 N LEU A 115 20183 21017 20886 -221 -165 275 N ATOM 860 CA LEU A 115 -21.357 -30.036 32.630 1.00157.64 C ANISOU 860 CA LEU A 115 19456 20288 20151 -195 -170 258 C ATOM 861 C LEU A 115 -22.359 -29.087 31.975 1.00154.14 C ANISOU 861 C LEU A 115 19029 19885 19650 -180 -144 244 C ATOM 862 O LEU A 115 -22.872 -28.187 32.637 1.00153.02 O ANISOU 862 O LEU A 115 18893 19782 19464 -163 -160 240 O ATOM 863 CB LEU A 115 -19.914 -29.707 32.227 1.00156.85 C ANISOU 863 CB LEU A 115 19346 20121 20128 -189 -160 242 C ATOM 864 CG LEU A 115 -18.913 -29.603 33.379 1.00155.53 C ANISOU 864 CG LEU A 115 19165 19927 20002 -185 -200 245 C ATOM 865 CD1 LEU A 115 -18.607 -30.970 33.973 1.00155.25 C ANISOU 865 CD1 LEU A 115 19118 19876 19993 -206 -228 266 C ATOM 866 CD2 LEU A 115 -17.629 -28.924 32.924 1.00154.50 C ANISOU 866 CD2 LEU A 115 19026 19738 19939 -173 -187 224 C ATOM 867 N VAL A 116 -22.628 -29.294 30.679 1.00150.27 N ANISOU 867 N VAL A 116 18549 19385 19163 -185 -105 237 N ATOM 868 CA VAL A 116 -23.540 -28.434 29.937 1.00146.80 C ANISOU 868 CA VAL A 116 18127 18978 18673 -171 -80 222 C ATOM 869 C VAL A 116 -24.814 -29.207 29.603 1.00143.33 C ANISOU 869 C VAL A 116 17694 18583 18182 -184 -71 233 C ATOM 870 O VAL A 116 -24.762 -30.389 29.265 1.00142.63 O ANISOU 870 O VAL A 116 17600 18480 18115 -205 -64 246 O ATOM 871 CB VAL A 116 -22.888 -27.820 28.679 1.00145.84 C ANISOU 871 CB VAL A 116 18015 18811 18588 -163 -42 201 C ATOM 872 CG1 VAL A 116 -21.632 -27.025 29.008 1.00145.11 C ANISOU 872 CG1 VAL A 116 17915 18674 18548 -150 -50 189 C ATOM 873 CG2 VAL A 116 -22.603 -28.853 27.599 1.00145.71 C ANISOU 873 CG2 VAL A 116 17997 18759 18607 -182 -12 203 C ATOM 874 N THR A 117 -25.956 -28.516 29.715 1.00140.14 N ANISOU 874 N THR A 117 17301 18234 17713 -170 -72 228 N ATOM 875 CA THR A 117 -27.259 -29.071 29.381 1.00139.04 C ANISOU 875 CA THR A 117 17167 18141 17519 -180 -63 235 C ATOM 876 C THR A 117 -28.097 -28.013 28.667 1.00135.49 C ANISOU 876 C THR A 117 16736 17719 17024 -159 -43 214 C ATOM 877 O THR A 117 -27.607 -26.928 28.359 1.00134.80 O ANISOU 877 O THR A 117 16657 17610 16949 -139 -35 196 O ATOM 878 CB THR A 117 -27.988 -29.608 30.622 1.00142.29 C ANISOU 878 CB THR A 117 17568 18604 17890 -191 -95 254 C ATOM 879 OG1 THR A 117 -28.061 -28.565 31.594 1.00145.61 O ANISOU 879 OG1 THR A 117 17989 19053 18284 -170 -119 247 O ATOM 880 CG2 THR A 117 -27.340 -30.836 31.225 1.00143.54 C ANISOU 880 CG2 THR A 117 17714 18738 18088 -215 -115 277 C ATOM 881 N GLY A 118 -29.369 -28.348 28.419 1.00133.60 N ANISOU 881 N GLY A 118 16502 17529 16732 -164 -37 217 N ATOM 882 CA GLY A 118 -30.294 -27.476 27.714 1.00132.52 C ANISOU 882 CA GLY A 118 16381 17420 16548 -145 -21 198 C ATOM 883 C GLY A 118 -30.794 -26.331 28.591 1.00133.17 C ANISOU 883 C GLY A 118 16465 17547 16587 -122 -44 187 C ATOM 884 O GLY A 118 -30.848 -25.188 28.141 1.00132.17 O ANISOU 884 O GLY A 118 16353 17417 16449 -98 -36 166 O ATOM 885 N THR A 119 -31.150 -26.654 29.841 1.00135.46 N ANISOU 885 N THR A 119 16739 17877 16852 -128 -73 201 N ATOM 886 CA THR A 119 -31.760 -25.699 30.755 1.00136.39 C ANISOU 886 CA THR A 119 16856 18045 16922 -107 -96 191 C ATOM 887 C THR A 119 -30.696 -24.781 31.355 1.00134.87 C ANISOU 887 C THR A 119 16662 17821 16761 -89 -113 183 C ATOM 888 O THR A 119 -30.948 -23.594 31.556 1.00133.83 O ANISOU 888 O THR A 119 16538 17710 16604 -63 -122 164 O ATOM 889 CB THR A 119 -32.598 -26.402 31.832 1.00137.45 C ANISOU 889 CB THR A 119 16975 18237 17013 -122 -118 208 C ATOM 890 OG1 THR A 119 -33.441 -27.360 31.192 1.00141.07 O ANISOU 890 OG1 THR A 119 17434 18715 17453 -142 -101 216 O ATOM 891 CG2 THR A 119 -33.453 -25.446 32.636 1.00137.26 C ANISOU 891 CG2 THR A 119 16949 18273 16931 -100 -137 194 C ATOM 892 N ARG A 120 -29.512 -25.341 31.637 1.00134.32 N ANISOU 892 N ARG A 120 16583 17703 16749 -103 -120 196 N ATOM 893 CA ARG A 120 -28.421 -24.591 32.240 1.00134.62 C ANISOU 893 CA ARG A 120 16617 17708 16823 -88 -138 190 C ATOM 894 C ARG A 120 -27.972 -23.472 31.303 1.00132.61 C ANISOU 894 C ARG A 120 16379 17418 16589 -68 -117 167 C ATOM 895 O ARG A 120 -27.512 -22.430 31.762 1.00133.43 O ANISOU 895 O ARG A 120 16484 17514 16699 -47 -133 155 O ATOM 896 CB ARG A 120 -27.250 -25.511 32.598 1.00138.15 C ANISOU 896 CB ARG A 120 17052 18106 17332 -109 -147 208 C ATOM 897 CG ARG A 120 -27.449 -26.308 33.880 1.00142.64 C ANISOU 897 CG ARG A 120 17606 18705 17884 -124 -180 231 C ATOM 898 CD ARG A 120 -26.287 -27.249 34.134 1.00145.37 C ANISOU 898 CD ARG A 120 17941 18998 18294 -143 -190 247 C ATOM 899 NE ARG A 120 -26.476 -28.093 35.306 1.00148.56 N ANISOU 899 NE ARG A 120 18336 19428 18683 -160 -222 270 N ATOM 900 CZ ARG A 120 -25.609 -29.008 35.732 1.00150.81 C ANISOU 900 CZ ARG A 120 18611 19674 19014 -179 -239 287 C ATOM 901 NH1 ARG A 120 -25.879 -29.720 36.813 1.00152.91 N ANISOU 901 NH1 ARG A 120 18873 19968 19259 -194 -269 309 N ATOM 902 NH2 ARG A 120 -24.477 -29.209 35.081 1.00149.92 N ANISOU 902 NH2 ARG A 120 18495 19497 18971 -181 -227 282 N ATOM 903 N ALA A 121 -28.120 -23.702 29.993 1.00130.20 N ANISOU 903 N ALA A 121 16085 17093 16292 -74 -83 162 N ATOM 904 CA ALA A 121 -27.741 -22.731 28.978 1.00126.79 C ANISOU 904 CA ALA A 121 15672 16627 15877 -59 -60 142 C ATOM 905 C ALA A 121 -28.725 -21.562 28.972 1.00124.71 C ANISOU 905 C ALA A 121 15422 16406 15554 -32 -66 123 C ATOM 906 O ALA A 121 -28.312 -20.411 28.850 1.00126.77 O ANISOU 906 O ALA A 121 15695 16649 15824 -12 -68 107 O ATOM 907 CB ALA A 121 -27.664 -23.397 27.626 1.00126.37 C ANISOU 907 CB ALA A 121 15629 16542 15845 -74 -22 142 C ATOM 908 N ALA A 122 -30.020 -21.876 29.110 1.00119.59 N ANISOU 908 N ALA A 122 14773 15816 14848 -33 -71 125 N ATOM 909 CA ALA A 122 -31.084 -20.885 29.071 1.00115.27 C ANISOU 909 CA ALA A 122 14238 15315 14244 -9 -77 106 C ATOM 910 C ALA A 122 -30.919 -19.886 30.215 1.00113.46 C ANISOU 910 C ALA A 122 14003 15104 14001 13 -110 97 C ATOM 911 O ALA A 122 -31.134 -18.689 30.030 1.00112.69 O ANISOU 911 O ALA A 122 13919 15012 13885 39 -115 76 O ATOM 912 CB ALA A 122 -32.431 -21.565 29.117 1.00114.16 C ANISOU 912 CB ALA A 122 14093 15233 14050 -18 -77 111 C ATOM 913 N GLY A 123 -30.537 -20.398 31.391 1.00111.38 N ANISOU 913 N GLY A 123 13720 14850 13749 3 -134 113 N ATOM 914 CA GLY A 123 -30.267 -19.574 32.557 1.00108.59 C ANISOU 914 CA GLY A 123 13360 14511 13388 23 -167 106 C ATOM 915 C GLY A 123 -29.062 -18.662 32.340 1.00106.03 C ANISOU 915 C GLY A 123 13043 14129 13113 37 -167 95 C ATOM 916 O GLY A 123 -29.060 -17.519 32.793 1.00106.23 O ANISOU 916 O GLY A 123 13073 14165 13125 62 -187 79 O ATOM 917 N ILE A 124 -28.051 -19.184 31.633 1.00102.40 N ANISOU 917 N ILE A 124 12584 13609 12713 20 -145 104 N ATOM 918 CA ILE A 124 -26.830 -18.448 31.343 1.00100.31 C ANISOU 918 CA ILE A 124 12325 13286 12503 28 -141 95 C ATOM 919 C ILE A 124 -27.152 -17.275 30.419 1.00 99.10 C ANISOU 919 C ILE A 124 12195 13127 12331 49 -126 72 C ATOM 920 O ILE A 124 -26.674 -16.164 30.646 1.00 97.81 O ANISOU 920 O ILE A 124 12038 12947 12179 69 -139 59 O ATOM 921 CB ILE A 124 -25.741 -19.378 30.764 1.00100.95 C ANISOU 921 CB ILE A 124 12398 13307 12650 3 -119 107 C ATOM 922 CG1 ILE A 124 -25.108 -20.248 31.856 1.00102.75 C ANISOU 922 CG1 ILE A 124 12603 13528 12908 -12 -144 126 C ATOM 923 CG2 ILE A 124 -24.688 -18.587 29.998 1.00100.55 C ANISOU 923 CG2 ILE A 124 12359 13197 12650 10 -100 94 C ATOM 924 CD1 ILE A 124 -24.160 -21.309 31.339 1.00104.53 C ANISOU 924 CD1 ILE A 124 12819 13701 13196 -37 -125 138 C ATOM 925 N ILE A 125 -27.975 -17.535 29.393 1.00 98.14 N ANISOU 925 N ILE A 125 12088 13019 12181 44 -100 69 N ATOM 926 CA ILE A 125 -28.319 -16.546 28.381 1.00 96.45 C ANISOU 926 CA ILE A 125 11900 12797 11949 61 -83 50 C ATOM 927 C ILE A 125 -29.077 -15.389 29.031 1.00 97.23 C ANISOU 927 C ILE A 125 12005 12940 11999 91 -113 32 C ATOM 928 O ILE A 125 -28.800 -14.227 28.739 1.00 96.85 O ANISOU 928 O ILE A 125 11972 12870 11954 110 -116 15 O ATOM 929 CB ILE A 125 -29.096 -17.186 27.208 1.00 94.88 C ANISOU 929 CB ILE A 125 11715 12606 11729 48 -52 51 C ATOM 930 CG1 ILE A 125 -28.238 -18.214 26.463 1.00 94.06 C ANISOU 930 CG1 ILE A 125 11608 12452 11679 21 -22 65 C ATOM 931 CG2 ILE A 125 -29.644 -16.121 26.266 1.00 94.49 C ANISOU 931 CG2 ILE A 125 11695 12556 11649 68 -42 30 C ATOM 932 CD1 ILE A 125 -28.964 -18.978 25.376 1.00 93.69 C ANISOU 932 CD1 ILE A 125 11572 12412 11612 7 7 68 C ATOM 933 N ALA A 126 -30.018 -15.726 29.923 1.00 98.17 N ANISOU 933 N ALA A 126 12109 13120 12071 94 -135 35 N ATOM 934 CA ALA A 126 -30.838 -14.748 30.621 1.00 97.36 C ANISOU 934 CA ALA A 126 12008 13067 11917 122 -163 17 C ATOM 935 C ALA A 126 -29.957 -13.797 31.429 1.00 98.45 C ANISOU 935 C ALA A 126 12143 13184 12081 140 -190 10 C ATOM 936 O ALA A 126 -30.147 -12.584 31.371 1.00 98.62 O ANISOU 936 O ALA A 126 12179 13209 12085 166 -203 -11 O ATOM 937 CB ALA A 126 -31.849 -15.450 31.493 1.00 96.06 C ANISOU 937 CB ALA A 126 11825 12969 11706 116 -179 25 C ATOM 938 N ILE A 127 -28.989 -14.363 32.166 1.00 99.51 N ANISOU 938 N ILE A 127 12259 13293 12257 125 -199 26 N ATOM 939 CA ILE A 127 -28.087 -13.593 33.010 1.00100.47 C ANISOU 939 CA ILE A 127 12374 13392 12406 140 -226 21 C ATOM 940 C ILE A 127 -27.287 -12.619 32.145 1.00101.77 C ANISOU 940 C ILE A 127 12559 13500 12610 150 -213 8 C ATOM 941 O ILE A 127 -27.095 -11.465 32.527 1.00102.08 O ANISOU 941 O ILE A 127 12604 13536 12647 175 -235 -8 O ATOM 942 CB ILE A 127 -27.182 -14.514 33.859 1.00 99.22 C ANISOU 942 CB ILE A 127 12194 13214 12291 120 -238 43 C ATOM 943 CG1 ILE A 127 -27.989 -15.287 34.906 1.00 99.27 C ANISOU 943 CG1 ILE A 127 12185 13281 12253 113 -257 55 C ATOM 944 CG2 ILE A 127 -26.046 -13.730 34.504 1.00 97.28 C ANISOU 944 CG2 ILE A 127 11945 12930 12088 134 -261 37 C ATOM 945 CD1 ILE A 127 -27.252 -16.460 35.517 1.00100.66 C ANISOU 945 CD1 ILE A 127 12342 13437 12466 87 -264 80 C ATOM 946 N CYS A 128 -26.846 -13.089 30.972 1.00101.80 N ANISOU 946 N CYS A 128 12572 13461 12648 131 -176 14 N ATOM 947 CA CYS A 128 -26.032 -12.286 30.074 1.00102.37 C ANISOU 947 CA CYS A 128 12663 13476 12759 135 -158 4 C ATOM 948 C CYS A 128 -26.849 -11.133 29.495 1.00101.73 C ANISOU 948 C CYS A 128 12608 13412 12633 159 -160 -17 C ATOM 949 O CYS A 128 -26.317 -10.043 29.299 1.00103.07 O ANISOU 949 O CYS A 128 12791 13550 12821 174 -165 -30 O ATOM 950 CB CYS A 128 -25.432 -13.137 28.961 1.00103.83 C ANISOU 950 CB CYS A 128 12851 13615 12987 108 -117 15 C ATOM 951 SG CYS A 128 -24.265 -14.380 29.573 1.00107.39 S ANISOU 951 SG CYS A 128 13271 14032 13501 81 -117 37 S ATOM 952 N TRP A 129 -28.141 -11.378 29.237 1.00 98.51 N ANISOU 952 N TRP A 129 12206 13054 12168 164 -157 -21 N ATOM 953 CA TRP A 129 -29.022 -10.349 28.707 1.00 96.05 C ANISOU 953 CA TRP A 129 11919 12763 11811 188 -162 -42 C ATOM 954 C TRP A 129 -29.312 -9.290 29.767 1.00 95.01 C ANISOU 954 C TRP A 129 11784 12664 11653 218 -204 -59 C ATOM 955 O TRP A 129 -29.386 -8.105 29.449 1.00 94.79 O ANISOU 955 O TRP A 129 11776 12624 11615 240 -214 -77 O ATOM 956 CB TRP A 129 -30.309 -10.951 28.132 1.00 95.48 C ANISOU 956 CB TRP A 129 11853 12734 11690 183 -148 -43 C ATOM 957 CG TRP A 129 -30.205 -11.318 26.684 1.00 96.54 C ANISOU 957 CG TRP A 129 12009 12831 11839 167 -109 -40 C ATOM 958 CD1 TRP A 129 -30.062 -12.571 26.163 1.00 97.46 C ANISOU 958 CD1 TRP A 129 12118 12935 11975 138 -80 -22 C ATOM 959 CD2 TRP A 129 -30.233 -10.420 25.559 1.00 96.52 C ANISOU 959 CD2 TRP A 129 12041 12799 11833 177 -95 -54 C ATOM 960 NE1 TRP A 129 -30.001 -12.518 24.796 1.00 97.07 N ANISOU 960 NE1 TRP A 129 12096 12852 11933 131 -48 -25 N ATOM 961 CE2 TRP A 129 -30.105 -11.212 24.396 1.00 97.05 C ANISOU 961 CE2 TRP A 129 12121 12838 11917 154 -56 -44 C ATOM 962 CE3 TRP A 129 -30.356 -9.032 25.417 1.00 96.67 C ANISOU 962 CE3 TRP A 129 12082 12811 11835 204 -112 -74 C ATOM 963 CZ2 TRP A 129 -30.095 -10.659 23.114 1.00 97.46 C ANISOU 963 CZ2 TRP A 129 12208 12857 11968 156 -33 -53 C ATOM 964 CZ3 TRP A 129 -30.346 -8.487 24.151 1.00 97.55 C ANISOU 964 CZ3 TRP A 129 12229 12888 11947 205 -91 -82 C ATOM 965 CH2 TRP A 129 -30.217 -9.291 23.016 1.00 97.55 C ANISOU 965 CH2 TRP A 129 12242 12861 11961 181 -51 -72 C ATOM 966 N VAL A 130 -29.463 -9.732 31.023 1.00 94.47 N ANISOU 966 N VAL A 130 11689 12634 11572 219 -228 -52 N ATOM 967 CA VAL A 130 -29.721 -8.831 32.138 1.00 93.81 C ANISOU 967 CA VAL A 130 11598 12584 11462 247 -268 -67 C ATOM 968 C VAL A 130 -28.474 -7.984 32.393 1.00 92.67 C ANISOU 968 C VAL A 130 11457 12386 11368 256 -282 -71 C ATOM 969 O VAL A 130 -28.578 -6.775 32.596 1.00 91.19 O ANISOU 969 O VAL A 130 11281 12201 11166 283 -305 -91 O ATOM 970 CB VAL A 130 -30.191 -9.581 33.404 1.00 92.67 C ANISOU 970 CB VAL A 130 11426 12494 11289 242 -289 -57 C ATOM 971 CG1 VAL A 130 -30.267 -8.668 34.619 1.00 91.87 C ANISOU 971 CG1 VAL A 130 11317 12422 11168 270 -330 -73 C ATOM 972 CG2 VAL A 130 -31.528 -10.275 33.190 1.00 91.80 C ANISOU 972 CG2 VAL A 130 11313 12441 11126 236 -278 -57 C ATOM 973 N LEU A 131 -27.301 -8.628 32.358 1.00 91.66 N ANISOU 973 N LEU A 131 11319 12209 11299 232 -267 -53 N ATOM 974 CA LEU A 131 -26.040 -7.941 32.588 1.00 91.95 C ANISOU 974 CA LEU A 131 11355 12193 11390 237 -278 -55 C ATOM 975 C LEU A 131 -25.755 -6.962 31.449 1.00 92.50 C ANISOU 975 C LEU A 131 11454 12219 11475 244 -261 -68 C ATOM 976 O LEU A 131 -25.175 -5.902 31.679 1.00 92.98 O ANISOU 976 O LEU A 131 11521 12253 11555 261 -279 -80 O ATOM 977 CB LEU A 131 -24.908 -8.964 32.741 1.00 90.94 C ANISOU 977 CB LEU A 131 11208 12024 11323 209 -264 -34 C ATOM 978 CG LEU A 131 -24.850 -9.703 34.079 1.00 89.62 C ANISOU 978 CG LEU A 131 11014 11886 11153 204 -291 -21 C ATOM 979 CD1 LEU A 131 -23.546 -10.475 34.208 1.00 89.86 C ANISOU 979 CD1 LEU A 131 11027 11863 11251 181 -283 -4 C ATOM 980 CD2 LEU A 131 -25.011 -8.745 35.249 1.00 89.02 C ANISOU 980 CD2 LEU A 131 10934 11839 11052 234 -335 -35 C ATOM 981 N SER A 132 -26.179 -7.322 30.230 1.00 91.19 N ANISOU 981 N SER A 132 11306 12046 11298 231 -226 -66 N ATOM 982 CA SER A 132 -25.948 -6.498 29.053 1.00 90.50 C ANISOU 982 CA SER A 132 11248 11916 11221 234 -206 -76 C ATOM 983 C SER A 132 -26.732 -5.191 29.147 1.00 90.92 C ANISOU 983 C SER A 132 11321 11995 11228 268 -234 -99 C ATOM 984 O SER A 132 -26.261 -4.153 28.683 1.00 91.25 O ANISOU 984 O SER A 132 11385 11999 11288 277 -236 -110 O ATOM 985 CB SER A 132 -26.266 -7.243 27.784 1.00 89.67 C ANISOU 985 CB SER A 132 11157 11800 11111 213 -164 -68 C ATOM 986 OG SER A 132 -25.400 -8.357 27.628 1.00 88.81 O ANISOU 986 OG SER A 132 11032 11660 11053 183 -137 -49 O ATOM 987 N PHE A 133 -27.926 -5.254 29.751 1.00 89.69 N ANISOU 987 N PHE A 133 11158 11904 11015 284 -257 -108 N ATOM 988 CA PHE A 133 -28.755 -4.073 29.932 1.00 88.78 C ANISOU 988 CA PHE A 133 11058 11819 10854 318 -287 -133 C ATOM 989 C PHE A 133 -28.136 -3.147 30.975 1.00 89.54 C ANISOU 989 C PHE A 133 11145 11907 10967 339 -325 -142 C ATOM 990 O PHE A 133 -28.155 -1.929 30.806 1.00 89.92 O ANISOU 990 O PHE A 133 11215 11942 11010 362 -343 -161 O ATOM 991 CB PHE A 133 -30.198 -4.453 30.271 1.00 87.25 C ANISOU 991 CB PHE A 133 10857 11699 10596 329 -298 -141 C ATOM 992 CG PHE A 133 -31.092 -4.609 29.067 1.00 87.34 C ANISOU 992 CG PHE A 133 10890 11719 10576 326 -274 -146 C ATOM 993 CD1 PHE A 133 -31.675 -3.502 28.467 1.00 86.76 C ANISOU 993 CD1 PHE A 133 10847 11646 10474 351 -286 -169 C ATOM 994 CD2 PHE A 133 -31.346 -5.861 28.527 1.00 87.68 C ANISOU 994 CD2 PHE A 133 10927 11769 10618 299 -242 -129 C ATOM 995 CE1 PHE A 133 -32.493 -3.644 27.356 1.00 86.32 C ANISOU 995 CE1 PHE A 133 10813 11596 10389 348 -267 -174 C ATOM 996 CE2 PHE A 133 -32.166 -6.003 27.418 1.00 87.35 C ANISOU 996 CE2 PHE A 133 10907 11734 10548 297 -222 -134 C ATOM 997 CZ PHE A 133 -32.738 -4.895 26.834 1.00 86.55 C ANISOU 997 CZ PHE A 133 10835 11632 10417 322 -234 -157 C ATOM 998 N ALA A 134 -27.587 -3.743 32.042 1.00 89.33 N ANISOU 998 N ALA A 134 11090 11888 10964 331 -337 -130 N ATOM 999 CA ALA A 134 -26.949 -2.997 33.116 1.00 88.43 C ANISOU 999 CA ALA A 134 10965 11766 10868 349 -374 -137 C ATOM 1000 C ALA A 134 -25.710 -2.281 32.585 1.00 88.47 C ANISOU 1000 C ALA A 134 10984 11698 10932 345 -366 -137 C ATOM 1001 O ALA A 134 -25.543 -1.084 32.813 1.00 89.05 O ANISOU 1001 O ALA A 134 11069 11759 11006 369 -393 -154 O ATOM 1002 CB ALA A 134 -26.608 -3.919 34.261 1.00 87.45 C ANISOU 1002 CB ALA A 134 10810 11662 10757 338 -385 -121 C ATOM 1003 N ILE A 135 -24.863 -3.030 31.866 1.00 87.59 N ANISOU 1003 N ILE A 135 10871 11539 10869 314 -329 -119 N ATOM 1004 CA ILE A 135 -23.606 -2.511 31.349 1.00 87.46 C ANISOU 1004 CA ILE A 135 10863 11453 10914 305 -316 -117 C ATOM 1005 C ILE A 135 -23.893 -1.443 30.294 1.00 88.82 C ANISOU 1005 C ILE A 135 11073 11605 11071 316 -308 -132 C ATOM 1006 O ILE A 135 -23.293 -0.370 30.321 1.00 88.47 O ANISOU 1006 O ILE A 135 11039 11524 11049 328 -324 -142 O ATOM 1007 CB ILE A 135 -22.702 -3.647 30.821 1.00 85.67 C ANISOU 1007 CB ILE A 135 10625 11186 10742 269 -276 -96 C ATOM 1008 CG1 ILE A 135 -22.200 -4.538 31.960 1.00 85.30 C ANISOU 1008 CG1 ILE A 135 10543 11149 10720 260 -292 -83 C ATOM 1009 CG2 ILE A 135 -21.548 -3.092 29.997 1.00 84.77 C ANISOU 1009 CG2 ILE A 135 10524 11001 10685 256 -254 -97 C ATOM 1010 CD1 ILE A 135 -21.491 -5.794 31.502 1.00 86.18 C ANISOU 1010 CD1 ILE A 135 10639 11228 10877 226 -257 -63 C ATOM 1011 N GLY A 136 -24.827 -1.743 29.383 1.00 89.85 N ANISOU 1011 N GLY A 136 11222 11756 11161 312 -285 -133 N ATOM 1012 CA GLY A 136 -25.135 -0.871 28.260 1.00 91.41 C ANISOU 1012 CA GLY A 136 11457 11931 11342 319 -274 -144 C ATOM 1013 C GLY A 136 -25.749 0.456 28.699 1.00 92.86 C ANISOU 1013 C GLY A 136 11656 12137 11489 355 -317 -168 C ATOM 1014 O GLY A 136 -25.369 1.511 28.194 1.00 94.26 O ANISOU 1014 O GLY A 136 11859 12275 11679 363 -322 -177 O ATOM 1015 N LEU A 137 -26.692 0.388 29.648 1.00 92.60 N ANISOU 1015 N LEU A 137 11607 12168 11410 377 -349 -178 N ATOM 1016 CA LEU A 137 -27.484 1.546 30.035 1.00 91.35 C ANISOU 1016 CA LEU A 137 11461 12040 11207 414 -390 -203 C ATOM 1017 C LEU A 137 -26.957 2.155 31.334 1.00 91.30 C ANISOU 1017 C LEU A 137 11435 12037 11217 434 -431 -211 C ATOM 1018 O LEU A 137 -27.707 2.807 32.060 1.00 90.58 O ANISOU 1018 O LEU A 137 11341 11990 11086 465 -469 -232 O ATOM 1019 CB LEU A 137 -28.956 1.135 30.165 1.00 88.72 C ANISOU 1019 CB LEU A 137 11123 11777 10809 427 -397 -213 C ATOM 1020 CG LEU A 137 -29.645 0.699 28.872 1.00 86.87 C ANISOU 1020 CG LEU A 137 10912 11543 10551 414 -363 -211 C ATOM 1021 CD1 LEU A 137 -31.023 0.125 29.156 1.00 85.65 C ANISOU 1021 CD1 LEU A 137 10745 11461 10339 423 -370 -219 C ATOM 1022 CD2 LEU A 137 -29.741 1.853 27.885 1.00 86.61 C ANISOU 1022 CD2 LEU A 137 10920 11475 10511 428 -367 -225 C ATOM 1023 N THR A 138 -25.657 1.965 31.599 1.00 91.22 N ANISOU 1023 N THR A 138 11411 11980 11268 416 -423 -197 N ATOM 1024 CA THR A 138 -25.014 2.497 32.792 1.00 91.90 C ANISOU 1024 CA THR A 138 11480 12062 11378 433 -461 -202 C ATOM 1025 C THR A 138 -25.094 4.025 32.817 1.00 90.64 C ANISOU 1025 C THR A 138 11342 11889 11208 464 -496 -226 C ATOM 1026 O THR A 138 -25.363 4.596 33.872 1.00 91.29 O ANISOU 1026 O THR A 138 11413 12002 11270 492 -538 -241 O ATOM 1027 CB THR A 138 -23.585 1.960 32.968 1.00 93.18 C ANISOU 1027 CB THR A 138 11622 12171 11610 406 -445 -183 C ATOM 1028 OG1 THR A 138 -23.639 0.534 33.015 1.00 94.12 O ANISOU 1028 OG1 THR A 138 11721 12309 11733 381 -418 -163 O ATOM 1029 CG2 THR A 138 -22.905 2.472 34.220 1.00 92.95 C ANISOU 1029 CG2 THR A 138 11574 12137 11606 423 -485 -189 C ATOM 1030 N PRO A 139 -24.861 4.743 31.689 1.00 89.06 N ANISOU 1030 N PRO A 139 11175 11642 11021 460 -480 -229 N ATOM 1031 CA PRO A 139 -24.955 6.206 31.681 1.00 88.98 C ANISOU 1031 CA PRO A 139 11190 11617 11002 489 -515 -251 C ATOM 1032 C PRO A 139 -26.266 6.775 32.220 1.00 89.23 C ANISOU 1032 C PRO A 139 11225 11712 10968 526 -555 -276 C ATOM 1033 O PRO A 139 -26.287 7.888 32.736 1.00 88.12 O ANISOU 1033 O PRO A 139 11091 11570 10821 556 -596 -296 O ATOM 1034 CB PRO A 139 -24.796 6.563 30.196 1.00 87.68 C ANISOU 1034 CB PRO A 139 11063 11404 10848 472 -483 -247 C ATOM 1035 CG PRO A 139 -23.945 5.443 29.653 1.00 87.44 C ANISOU 1035 CG PRO A 139 11021 11340 10864 432 -433 -221 C ATOM 1036 CD PRO A 139 -24.442 4.211 30.381 1.00 87.57 C ANISOU 1036 CD PRO A 139 11004 11410 10859 427 -430 -212 C ATOM 1037 N MET A 140 -27.347 5.992 32.117 1.00 91.21 N ANISOU 1037 N MET A 140 11468 12016 11171 525 -542 -277 N ATOM 1038 CA MET A 140 -28.675 6.450 32.497 1.00 93.63 C ANISOU 1038 CA MET A 140 11776 12384 11413 559 -574 -302 C ATOM 1039 C MET A 140 -28.820 6.498 34.018 1.00 94.84 C ANISOU 1039 C MET A 140 11899 12585 11552 581 -613 -313 C ATOM 1040 O MET A 140 -29.760 7.103 34.531 1.00 95.60 O ANISOU 1040 O MET A 140 11993 12728 11600 613 -647 -339 O ATOM 1041 CB MET A 140 -29.761 5.550 31.900 1.00 94.08 C ANISOU 1041 CB MET A 140 11834 12484 11427 548 -547 -299 C ATOM 1042 CG MET A 140 -29.991 5.802 30.422 1.00 96.01 C ANISOU 1042 CG MET A 140 12117 12695 11667 539 -522 -299 C ATOM 1043 SD MET A 140 -31.445 4.952 29.761 1.00 96.88 S ANISOU 1043 SD MET A 140 12230 12860 11720 536 -501 -302 S ATOM 1044 CE MET A 140 -32.739 5.663 30.778 1.00 98.76 C ANISOU 1044 CE MET A 140 12456 13173 11896 582 -553 -338 C ATOM 1045 N LEU A 141 -27.875 5.868 34.729 1.00 95.21 N ANISOU 1045 N LEU A 141 11919 12616 11639 563 -607 -294 N ATOM 1046 CA LEU A 141 -27.921 5.794 36.181 1.00 94.42 C ANISOU 1046 CA LEU A 141 11790 12558 11527 579 -641 -301 C ATOM 1047 C LEU A 141 -27.274 7.032 36.802 1.00 95.68 C ANISOU 1047 C LEU A 141 11954 12689 11710 605 -683 -317 C ATOM 1048 O LEU A 141 -27.332 7.211 38.017 1.00 97.49 O ANISOU 1048 O LEU A 141 12164 12952 11926 625 -717 -327 O ATOM 1049 CB LEU A 141 -27.242 4.503 36.655 1.00 92.25 C ANISOU 1049 CB LEU A 141 11488 12280 11284 548 -618 -273 C ATOM 1050 CG LEU A 141 -27.894 3.194 36.207 1.00 90.05 C ANISOU 1050 CG LEU A 141 11200 12034 10981 522 -580 -256 C ATOM 1051 CD1 LEU A 141 -27.075 1.995 36.658 1.00 89.65 C ANISOU 1051 CD1 LEU A 141 11124 11969 10968 492 -561 -228 C ATOM 1052 CD2 LEU A 141 -29.323 3.082 36.716 1.00 89.90 C ANISOU 1052 CD2 LEU A 141 11173 12095 10892 542 -596 -273 C ATOM 1053 N GLY A 142 -26.654 7.878 35.969 1.00 95.72 N ANISOU 1053 N GLY A 142 11987 12633 11748 604 -680 -319 N ATOM 1054 CA GLY A 142 -26.142 9.154 36.441 1.00 97.12 C ANISOU 1054 CA GLY A 142 12173 12783 11945 630 -722 -336 C ATOM 1055 C GLY A 142 -24.821 9.560 35.791 1.00 98.23 C ANISOU 1055 C GLY A 142 12328 12841 12152 610 -706 -323 C ATOM 1056 O GLY A 142 -24.414 10.715 35.897 1.00 99.63 O ANISOU 1056 O GLY A 142 12521 12987 12348 629 -737 -337 O ATOM 1057 N TRP A 143 -24.157 8.607 35.127 1.00 98.00 N ANISOU 1057 N TRP A 143 12295 12780 12162 572 -659 -296 N ATOM 1058 CA TRP A 143 -22.866 8.866 34.509 1.00 99.30 C ANISOU 1058 CA TRP A 143 12469 12868 12392 549 -639 -283 C ATOM 1059 C TRP A 143 -23.066 9.389 33.088 1.00100.34 C ANISOU 1059 C TRP A 143 12640 12965 12518 540 -615 -284 C ATOM 1060 O TRP A 143 -22.893 8.655 32.115 1.00101.53 O ANISOU 1060 O TRP A 143 12799 13095 12682 509 -568 -266 O ATOM 1061 CB TRP A 143 -21.978 7.615 34.560 1.00 99.45 C ANISOU 1061 CB TRP A 143 12462 12866 12458 513 -603 -256 C ATOM 1062 CG TRP A 143 -20.538 7.863 34.229 1.00 99.71 C ANISOU 1062 CG TRP A 143 12496 12826 12565 491 -588 -245 C ATOM 1063 CD1 TRP A 143 -19.945 9.065 33.966 1.00100.14 C ANISOU 1063 CD1 TRP A 143 12570 12832 12648 500 -605 -255 C ATOM 1064 CD2 TRP A 143 -19.489 6.880 34.168 1.00100.70 C ANISOU 1064 CD2 TRP A 143 12598 12916 12747 458 -556 -224 C ATOM 1065 NE1 TRP A 143 -18.609 8.895 33.722 1.00100.64 N ANISOU 1065 NE1 TRP A 143 12624 12833 12781 472 -582 -241 N ATOM 1066 CE2 TRP A 143 -18.298 7.566 33.842 1.00101.19 C ANISOU 1066 CE2 TRP A 143 12667 12911 12871 447 -552 -223 C ATOM 1067 CE3 TRP A 143 -19.438 5.491 34.348 1.00100.97 C ANISOU 1067 CE3 TRP A 143 12607 12969 12788 435 -530 -206 C ATOM 1068 CZ2 TRP A 143 -17.075 6.908 33.695 1.00101.14 C ANISOU 1068 CZ2 TRP A 143 12640 12856 12931 416 -523 -206 C ATOM 1069 CZ3 TRP A 143 -18.230 4.842 34.200 1.00101.00 C ANISOU 1069 CZ3 TRP A 143 12593 12925 12858 405 -503 -189 C ATOM 1070 CH2 TRP A 143 -17.066 5.543 33.877 1.00100.68 C ANISOU 1070 CH2 TRP A 143 12557 12818 12878 396 -500 -190 C ATOM 1071 N ASN A 144 -23.415 10.676 32.989 1.00100.69 N ANISOU 1071 N ASN A 144 12711 13004 12543 568 -649 -305 N ATOM 1072 CA ASN A 144 -23.749 11.305 31.722 1.00102.12 C ANISOU 1072 CA ASN A 144 12934 13157 12710 565 -636 -309 C ATOM 1073 C ASN A 144 -23.483 12.806 31.811 1.00104.80 C ANISOU 1073 C ASN A 144 13297 13463 13060 590 -677 -327 C ATOM 1074 O ASN A 144 -23.064 13.306 32.853 1.00105.51 O ANISOU 1074 O ASN A 144 13369 13554 13167 609 -715 -337 O ATOM 1075 CB ASN A 144 -25.191 11.000 31.309 1.00100.70 C ANISOU 1075 CB ASN A 144 12766 13033 12463 578 -632 -319 C ATOM 1076 CG ASN A 144 -26.187 11.280 32.414 1.00100.60 C ANISOU 1076 CG ASN A 144 12736 13087 12400 617 -679 -344 C ATOM 1077 OD1 ASN A 144 -26.408 12.431 32.781 1.00 99.86 O ANISOU 1077 OD1 ASN A 144 12654 12994 12293 649 -723 -367 O ATOM 1078 ND2 ASN A 144 -26.790 10.235 32.953 1.00102.68 N ANISOU 1078 ND2 ASN A 144 12971 13408 12636 614 -669 -339 N ATOM 1079 N ASN A 145 -23.747 13.512 30.704 1.00108.69 N ANISOU 1079 N ASN A 145 13832 13927 13540 589 -671 -332 N ATOM 1080 CA ASN A 145 -23.450 14.931 30.582 1.00110.79 C ANISOU 1080 CA ASN A 145 14126 14151 13817 607 -706 -346 C ATOM 1081 C ASN A 145 -24.743 15.744 30.587 1.00110.95 C ANISOU 1081 C ASN A 145 14169 14211 13775 646 -748 -374 C ATOM 1082 O ASN A 145 -24.803 16.815 29.989 1.00111.88 O ANISOU 1082 O ASN A 145 14326 14296 13890 657 -767 -384 O ATOM 1083 CB ASN A 145 -22.627 15.231 29.325 1.00112.82 C ANISOU 1083 CB ASN A 145 14417 14337 14113 574 -670 -329 C ATOM 1084 CG ASN A 145 -21.231 14.642 29.350 1.00114.99 C ANISOU 1084 CG ASN A 145 14669 14565 14457 538 -634 -306 C ATOM 1085 OD1 ASN A 145 -20.595 14.570 30.400 1.00116.38 O ANISOU 1085 OD1 ASN A 145 14812 14743 14666 544 -654 -306 O ATOM 1086 ND2 ASN A 145 -20.740 14.233 28.192 1.00115.96 N ANISOU 1086 ND2 ASN A 145 14809 14647 14603 501 -582 -286 N ATOM 1087 N CYS A 146 -25.768 15.240 31.282 1.00111.41 N ANISOU 1087 N CYS A 146 14205 14341 13786 668 -763 -387 N ATOM 1088 CA CYS A 146 -27.046 15.931 31.364 1.00113.00 C ANISOU 1088 CA CYS A 146 14421 14586 13927 707 -802 -417 C ATOM 1089 C CYS A 146 -26.944 17.122 32.315 1.00115.75 C ANISOU 1089 C CYS A 146 14767 14934 14278 745 -863 -442 C ATOM 1090 O CYS A 146 -27.724 18.065 32.209 1.00116.51 O ANISOU 1090 O CYS A 146 14886 15042 14339 777 -901 -468 O ATOM 1091 CB CYS A 146 -28.152 14.988 31.822 1.00112.77 C ANISOU 1091 CB CYS A 146 14365 14634 13848 716 -797 -424 C ATOM 1092 SG CYS A 146 -28.510 13.670 30.632 1.00113.35 S ANISOU 1092 SG CYS A 146 14445 14712 13909 678 -732 -399 S ATOM 1093 N GLY A 147 -25.966 17.067 33.229 1.00119.48 N ANISOU 1093 N GLY A 147 15212 15392 14794 741 -872 -435 N ATOM 1094 CA GLY A 147 -25.779 18.082 34.256 1.00121.69 C ANISOU 1094 CA GLY A 147 15485 15673 15080 775 -929 -457 C ATOM 1095 C GLY A 147 -25.209 19.388 33.705 1.00123.50 C ANISOU 1095 C GLY A 147 15750 15836 15337 781 -952 -463 C ATOM 1096 O GLY A 147 -25.456 20.456 34.265 1.00125.25 O ANISOU 1096 O GLY A 147 15980 16063 15547 817 -1005 -489 O ATOM 1097 N GLN A 148 -24.437 19.284 32.616 1.00123.86 N ANISOU 1097 N GLN A 148 15820 15820 15422 743 -911 -438 N ATOM 1098 CA GLN A 148 -23.829 20.433 31.964 1.00126.27 C ANISOU 1098 CA GLN A 148 16162 16058 15756 740 -925 -439 C ATOM 1099 C GLN A 148 -24.184 20.405 30.478 1.00126.46 C ANISOU 1099 C GLN A 148 16229 16057 15763 719 -890 -428 C ATOM 1100 O GLN A 148 -23.355 20.043 29.645 1.00125.96 O ANISOU 1100 O GLN A 148 16178 15944 15738 678 -843 -402 O ATOM 1101 CB GLN A 148 -22.315 20.441 32.190 1.00129.30 C ANISOU 1101 CB GLN A 148 16531 16383 16212 714 -911 -419 C ATOM 1102 CG GLN A 148 -21.910 20.697 33.636 1.00132.55 C ANISOU 1102 CG GLN A 148 16909 16812 16644 739 -954 -432 C ATOM 1103 CD GLN A 148 -20.416 20.657 33.847 0.50132.27 C ANISOU 1103 CD GLN A 148 16856 16718 16682 712 -940 -414 C ATOM 1104 OE1 GLN A 148 -19.670 20.066 33.069 0.50132.71 O ANISOU 1104 OE1 GLN A 148 16914 16734 16775 671 -889 -388 O ATOM 1105 NE2 GLN A 148 -19.965 21.289 34.918 0.50131.78 N ANISOU 1105 NE2 GLN A 148 16776 16651 16641 736 -987 -428 N ATOM 1106 N PRO A 149 -25.435 20.765 30.107 1.00127.23 N ANISOU 1106 N PRO A 149 16351 16188 15802 745 -911 -449 N ATOM 1107 CA PRO A 149 -25.876 20.692 28.714 1.00127.99 C ANISOU 1107 CA PRO A 149 16489 16265 15877 726 -881 -440 C ATOM 1108 C PRO A 149 -25.413 21.898 27.903 1.00129.37 C ANISOU 1108 C PRO A 149 16714 16371 16071 722 -896 -439 C ATOM 1109 O PRO A 149 -25.045 22.925 28.470 1.00131.02 O ANISOU 1109 O PRO A 149 16926 16558 16297 743 -941 -453 O ATOM 1110 CB PRO A 149 -27.405 20.689 28.853 1.00126.62 C ANISOU 1110 CB PRO A 149 16318 16158 15635 762 -908 -467 C ATOM 1111 CG PRO A 149 -27.671 21.506 30.099 1.00125.86 C ANISOU 1111 CG PRO A 149 16202 16091 15528 807 -971 -497 C ATOM 1112 CD PRO A 149 -26.495 21.235 31.014 1.00126.71 C ANISOU 1112 CD PRO A 149 16273 16183 15688 793 -966 -483 C ATOM 1113 N LYS A 150 -25.430 21.743 26.574 1.00129.27 N ANISOU 1113 N LYS A 150 16739 16324 16052 694 -857 -423 N ATOM 1114 CA LYS A 150 -25.120 22.821 25.649 1.00130.07 C ANISOU 1114 CA LYS A 150 16894 16362 16163 686 -868 -420 C ATOM 1115 C LYS A 150 -26.395 23.615 25.378 1.00133.42 C ANISOU 1115 C LYS A 150 17354 16811 16530 725 -915 -448 C ATOM 1116 O LYS A 150 -27.267 23.161 24.639 1.00133.71 O ANISOU 1116 O LYS A 150 17408 16869 16525 723 -897 -449 O ATOM 1117 CB LYS A 150 -24.509 22.258 24.361 1.00127.12 C ANISOU 1117 CB LYS A 150 16547 15943 15812 636 -802 -389 C ATOM 1118 CG LYS A 150 -23.052 21.830 24.471 1.00125.81 C ANISOU 1118 CG LYS A 150 16357 15733 15713 597 -762 -364 C ATOM 1119 CD LYS A 150 -22.514 21.183 23.212 1.00123.78 C ANISOU 1119 CD LYS A 150 16121 15436 15473 548 -694 -336 C ATOM 1120 CE LYS A 150 -21.003 21.222 23.116 1.00123.65 C ANISOU 1120 CE LYS A 150 16095 15359 15527 511 -663 -315 C ATOM 1121 NZ LYS A 150 -20.347 20.541 24.258 1.00122.60 N ANISOU 1121 NZ LYS A 150 15903 15247 15435 510 -659 -312 N ATOM 1122 N GLU A 151 -26.486 24.799 25.996 1.00137.59 N ANISOU 1122 N GLU A 151 17889 17331 17056 760 -977 -472 N ATOM 1123 CA GLU A 151 -27.677 25.631 25.926 1.00140.06 C ANISOU 1123 CA GLU A 151 18231 17669 17318 803 -1031 -504 C ATOM 1124 C GLU A 151 -27.711 26.397 24.606 1.00142.61 C ANISOU 1124 C GLU A 151 18619 17933 17633 790 -1032 -497 C ATOM 1125 O GLU A 151 -28.787 26.712 24.103 1.00144.29 O ANISOU 1125 O GLU A 151 18861 18163 17797 812 -1055 -516 O ATOM 1126 CB GLU A 151 -27.750 26.581 27.124 1.00141.77 C ANISOU 1126 CB GLU A 151 18429 17901 17537 847 -1098 -533 C ATOM 1127 CG GLU A 151 -28.236 25.915 28.401 1.00144.69 C ANISOU 1127 CG GLU A 151 18741 18345 17889 872 -1110 -550 C ATOM 1128 CD GLU A 151 -29.689 25.464 28.421 1.00147.18 C ANISOU 1128 CD GLU A 151 19048 18732 18141 899 -1118 -573 C ATOM 1129 OE1 GLU A 151 -30.448 25.832 27.497 1.00148.55 O ANISOU 1129 OE1 GLU A 151 19263 18898 18282 906 -1127 -583 O ATOM 1130 OE2 GLU A 151 -30.062 24.743 29.368 1.00149.07 O ANISOU 1130 OE2 GLU A 151 19240 19033 18365 911 -1116 -582 O ATOM 1131 N GLY A 152 -26.524 26.691 24.062 1.00144.20 N ANISOU 1131 N GLY A 152 18843 18065 17883 753 -1006 -471 N ATOM 1132 CA GLY A 152 -26.399 27.369 22.781 1.00144.68 C ANISOU 1132 CA GLY A 152 18968 18064 17940 733 -999 -460 C ATOM 1133 C GLY A 152 -27.012 26.554 21.646 1.00143.93 C ANISOU 1133 C GLY A 152 18897 17980 17810 711 -953 -447 C ATOM 1134 O GLY A 152 -27.679 27.104 20.773 1.00141.49 O ANISOU 1134 O GLY A 152 18639 17655 17466 719 -971 -454 O ATOM 1135 N LYS A 153 -26.788 25.236 21.688 1.00144.93 N ANISOU 1135 N LYS A 153 18985 18134 17947 685 -897 -429 N ATOM 1136 CA LYS A 153 -27.312 24.322 20.688 1.00147.28 C ANISOU 1136 CA LYS A 153 19300 18445 18216 663 -849 -416 C ATOM 1137 C LYS A 153 -28.804 24.092 20.925 1.00148.61 C ANISOU 1137 C LYS A 153 19460 18681 18324 703 -879 -444 C ATOM 1138 O LYS A 153 -29.544 23.826 19.981 1.00149.49 O ANISOU 1138 O LYS A 153 19603 18798 18398 699 -865 -444 O ATOM 1139 CB LYS A 153 -26.530 23.006 20.706 1.00148.31 C ANISOU 1139 CB LYS A 153 19390 18580 18380 623 -781 -389 C ATOM 1140 CG LYS A 153 -26.708 22.134 19.470 1.00150.87 C ANISOU 1140 CG LYS A 153 19739 18897 18688 589 -723 -369 C ATOM 1141 CD LYS A 153 -25.748 20.967 19.410 1.00151.45 C ANISOU 1141 CD LYS A 153 19778 18962 18805 546 -657 -341 C ATOM 1142 CE LYS A 153 -24.334 21.371 19.047 1.00150.58 C ANISOU 1142 CE LYS A 153 19682 18781 18752 509 -630 -319 C ATOM 1143 NZ LYS A 153 -23.415 20.209 19.045 1.00151.65 N ANISOU 1143 NZ LYS A 153 19778 18910 18930 470 -567 -295 N ATOM 1144 N ALA A 154 -29.230 24.196 22.190 1.00150.82 N ANISOU 1144 N ALA A 154 19696 19013 18595 741 -921 -469 N ATOM 1145 CA ALA A 154 -30.622 23.999 22.561 1.00153.67 C ANISOU 1145 CA ALA A 154 20043 19444 18902 780 -952 -499 C ATOM 1146 C ALA A 154 -31.474 25.159 22.049 1.00157.16 C ANISOU 1146 C ALA A 154 20536 19873 19307 813 -1006 -525 C ATOM 1147 O ALA A 154 -32.583 24.946 21.563 1.00159.38 O ANISOU 1147 O ALA A 154 20831 20186 19542 828 -1013 -540 O ATOM 1148 CB ALA A 154 -30.746 23.833 24.056 1.00152.23 C ANISOU 1148 CB ALA A 154 19802 19317 18723 809 -979 -517 C ATOM 1149 N HIS A 155 -30.938 26.382 22.154 1.00158.90 N ANISOU 1149 N HIS A 155 20782 20044 19548 823 -1047 -530 N ATOM 1150 CA HIS A 155 -31.648 27.577 21.726 1.00158.28 C ANISOU 1150 CA HIS A 155 20754 19947 19440 855 -1104 -555 C ATOM 1151 C HIS A 155 -31.552 27.740 20.211 1.00156.07 C ANISOU 1151 C HIS A 155 20539 19609 19152 824 -1078 -534 C ATOM 1152 O HIS A 155 -32.469 28.270 19.586 1.00157.31 O ANISOU 1152 O HIS A 155 20737 19764 19268 846 -1111 -553 O ATOM 1153 CB HIS A 155 -31.152 28.817 22.485 1.00160.67 C ANISOU 1153 CB HIS A 155 21059 20221 19767 879 -1162 -571 C ATOM 1154 CG HIS A 155 -31.390 28.765 23.958 1.00162.53 C ANISOU 1154 CG HIS A 155 21237 20515 20003 916 -1195 -596 C ATOM 1155 ND1 HIS A 155 -30.718 29.588 24.842 1.00164.19 N ANISOU 1155 ND1 HIS A 155 21433 20705 20245 932 -1234 -605 N ATOM 1156 CD2 HIS A 155 -32.205 27.989 24.707 1.00163.09 C ANISOU 1156 CD2 HIS A 155 21259 20664 20044 938 -1194 -615 C ATOM 1157 CE1 HIS A 155 -31.118 29.330 26.071 1.00165.33 C ANISOU 1157 CE1 HIS A 155 21526 20913 20380 963 -1257 -628 C ATOM 1158 NE2 HIS A 155 -32.029 28.351 26.015 1.00164.71 N ANISOU 1158 NE2 HIS A 155 21425 20896 20263 966 -1232 -634 N ATOM 1159 N SER A 156 -30.430 27.287 19.637 1.00151.77 N ANISOU 1159 N SER A 156 20003 19018 18647 773 -1020 -497 N ATOM 1160 CA SER A 156 -30.229 27.311 18.197 1.00149.69 C ANISOU 1160 CA SER A 156 19798 18700 18377 738 -985 -473 C ATOM 1161 C SER A 156 -31.230 26.377 17.520 1.00147.77 C ANISOU 1161 C SER A 156 19560 18498 18090 736 -957 -475 C ATOM 1162 O SER A 156 -31.867 26.755 16.540 1.00148.85 O ANISOU 1162 O SER A 156 19751 18615 18192 740 -970 -480 O ATOM 1163 CB SER A 156 -28.809 26.954 17.838 1.00149.91 C ANISOU 1163 CB SER A 156 19824 18676 18457 684 -926 -436 C ATOM 1164 OG SER A 156 -28.630 26.933 16.429 1.00151.89 O ANISOU 1164 OG SER A 156 20133 18878 18700 649 -888 -413 O ATOM 1165 N GLN A 157 -31.370 25.167 18.075 1.00146.40 N ANISOU 1165 N GLN A 157 19330 18379 17917 731 -922 -472 N ATOM 1166 CA GLN A 157 -32.237 24.141 17.520 1.00144.75 C ANISOU 1166 CA GLN A 157 19117 18211 17671 727 -891 -472 C ATOM 1167 C GLN A 157 -33.698 24.475 17.817 1.00143.10 C ANISOU 1167 C GLN A 157 18908 18055 17410 778 -947 -511 C ATOM 1168 O GLN A 157 -34.602 23.888 17.225 1.00142.79 O ANISOU 1168 O GLN A 157 18878 18044 17333 780 -935 -517 O ATOM 1169 CB GLN A 157 -31.869 22.771 18.091 1.00144.88 C ANISOU 1169 CB GLN A 157 19072 18267 17708 705 -839 -455 C ATOM 1170 CG GLN A 157 -31.958 21.643 17.074 1.00145.78 C ANISOU 1170 CG GLN A 157 19197 18381 17813 669 -776 -433 C ATOM 1171 CD GLN A 157 -30.819 21.671 16.083 1.00148.56 C ANISOU 1171 CD GLN A 157 19587 18662 18199 621 -728 -399 C ATOM 1172 OE1 GLN A 157 -29.753 22.225 16.342 1.00148.80 O ANISOU 1172 OE1 GLN A 157 19617 18648 18271 607 -728 -388 O ATOM 1173 NE2 GLN A 157 -31.039 21.060 14.930 1.00151.44 N ANISOU 1173 NE2 GLN A 157 19982 19014 18544 596 -686 -385 N ATOM 1174 N GLY A 158 -33.911 25.419 18.741 1.00140.88 N ANISOU 1174 N GLY A 158 18614 17786 17127 818 -1009 -539 N ATOM 1175 CA GLY A 158 -35.245 25.844 19.134 1.00139.51 C ANISOU 1175 CA GLY A 158 18436 17664 16908 869 -1067 -581 C ATOM 1176 C GLY A 158 -35.888 24.871 20.118 1.00137.94 C ANISOU 1176 C GLY A 158 18170 17547 16693 886 -1059 -596 C ATOM 1177 O GLY A 158 -37.112 24.815 20.224 1.00138.41 O ANISOU 1177 O GLY A 158 18221 17658 16710 919 -1087 -626 O ATOM 1178 N CYS A 159 -35.046 24.113 20.833 1.00137.30 N ANISOU 1178 N CYS A 159 18041 17479 16648 863 -1020 -575 N ATOM 1179 CA CYS A 159 -35.507 23.159 21.828 1.00136.46 C ANISOU 1179 CA CYS A 159 17871 17447 16530 874 -1009 -584 C ATOM 1180 C CYS A 159 -36.183 23.904 22.974 1.00138.54 C ANISOU 1180 C CYS A 159 18108 17756 16773 926 -1074 -625 C ATOM 1181 O CYS A 159 -35.693 24.941 23.418 1.00140.23 O ANISOU 1181 O CYS A 159 18332 17941 17008 942 -1115 -635 O ATOM 1182 CB CYS A 159 -34.352 22.337 22.391 1.00132.06 C ANISOU 1182 CB CYS A 159 17273 16885 16019 839 -962 -553 C ATOM 1183 SG CYS A 159 -33.500 21.324 21.155 1.00127.33 S ANISOU 1183 SG CYS A 159 16695 16237 15447 777 -881 -507 S ATOM 1184 N GLY A 160 -37.313 23.355 23.433 1.00139.24 N ANISOU 1184 N GLY A 160 18163 17918 16823 950 -1083 -650 N ATOM 1185 CA GLY A 160 -38.014 23.873 24.596 1.00140.81 C ANISOU 1185 CA GLY A 160 18328 18173 17001 998 -1137 -690 C ATOM 1186 C GLY A 160 -37.178 23.713 25.863 1.00142.56 C ANISOU 1186 C GLY A 160 18502 18408 17254 995 -1135 -682 C ATOM 1187 O GLY A 160 -36.113 23.098 25.837 1.00142.90 O ANISOU 1187 O GLY A 160 18535 18423 17337 956 -1089 -646 O ATOM 1188 N GLU A 161 -37.674 24.283 26.966 1.00144.74 N ANISOU 1188 N GLU A 161 18750 18730 17515 1038 -1186 -718 N ATOM 1189 CA GLU A 161 -36.998 24.190 28.250 1.00145.88 C ANISOU 1189 CA GLU A 161 18850 18894 17685 1042 -1191 -716 C ATOM 1190 C GLU A 161 -36.940 22.728 28.685 1.00141.92 C ANISOU 1190 C GLU A 161 18301 18439 17184 1014 -1137 -695 C ATOM 1191 O GLU A 161 -37.943 22.018 28.633 1.00140.52 O ANISOU 1191 O GLU A 161 18105 18318 16968 1020 -1124 -706 O ATOM 1192 CB GLU A 161 -37.693 25.066 29.294 1.00150.48 C ANISOU 1192 CB GLU A 161 19413 19520 18242 1096 -1257 -762 C ATOM 1193 CG GLU A 161 -37.395 26.546 29.130 1.00155.17 C ANISOU 1193 CG GLU A 161 20048 20059 18850 1121 -1312 -779 C ATOM 1194 CD GLU A 161 -37.719 27.410 30.337 1.00159.29 C ANISOU 1194 CD GLU A 161 20546 20616 19361 1170 -1375 -820 C ATOM 1195 OE1 GLU A 161 -37.784 26.865 31.458 1.00162.38 O ANISOU 1195 OE1 GLU A 161 20886 21063 19747 1178 -1370 -827 O ATOM 1196 OE2 GLU A 161 -37.900 28.630 30.153 1.00161.74 O ANISOU 1196 OE2 GLU A 161 20890 20896 19669 1200 -1429 -845 O ATOM 1197 N GLY A 162 -35.742 22.290 29.086 1.00137.64 N ANISOU 1197 N GLY A 162 17740 17870 16686 984 -1107 -663 N ATOM 1198 CA GLY A 162 -35.532 20.936 29.572 1.00133.10 C ANISOU 1198 CA GLY A 162 17120 17333 16117 956 -1059 -641 C ATOM 1199 C GLY A 162 -35.043 19.991 28.477 1.00130.72 C ANISOU 1199 C GLY A 162 16836 16997 15837 907 -996 -602 C ATOM 1200 O GLY A 162 -34.530 18.914 28.774 1.00131.45 O ANISOU 1200 O GLY A 162 16896 17099 15948 877 -953 -576 O ATOM 1201 N GLN A 163 -35.210 20.405 27.215 1.00127.40 N ANISOU 1201 N GLN A 163 16465 16532 15409 900 -991 -598 N ATOM 1202 CA GLN A 163 -34.803 19.598 26.075 1.00122.86 C ANISOU 1202 CA GLN A 163 15911 15921 14849 855 -933 -564 C ATOM 1203 C GLN A 163 -33.392 19.990 25.645 1.00121.14 C ANISOU 1203 C GLN A 163 15719 15624 14685 825 -915 -536 C ATOM 1204 O GLN A 163 -32.941 21.103 25.909 1.00120.16 O ANISOU 1204 O GLN A 163 15611 15465 14580 842 -954 -546 O ATOM 1205 CB GLN A 163 -35.786 19.764 24.915 1.00121.97 C ANISOU 1205 CB GLN A 163 15840 15805 14697 863 -936 -576 C ATOM 1206 CG GLN A 163 -37.166 19.187 25.194 1.00121.64 C ANISOU 1206 CG GLN A 163 15772 15842 14605 886 -944 -600 C ATOM 1207 CD GLN A 163 -38.122 19.416 24.050 1.00122.03 C ANISOU 1207 CD GLN A 163 15864 15885 14618 895 -952 -614 C ATOM 1208 OE1 GLN A 163 -37.961 20.336 23.251 1.00122.64 O ANISOU 1208 OE1 GLN A 163 15992 15907 14698 899 -972 -616 O ATOM 1209 NE2 GLN A 163 -39.134 18.568 23.964 1.00122.34 N ANISOU 1209 NE2 GLN A 163 15882 15980 14621 898 -937 -623 N ATOM 1210 N VAL A 164 -32.711 19.050 24.979 1.00119.90 N ANISOU 1210 N VAL A 164 15562 15439 14554 780 -855 -501 N ATOM 1211 CA VAL A 164 -31.378 19.267 24.439 1.00118.79 C ANISOU 1211 CA VAL A 164 15445 15225 14466 745 -827 -472 C ATOM 1212 C VAL A 164 -31.337 18.737 23.008 1.00117.05 C ANISOU 1212 C VAL A 164 15261 14971 14243 710 -777 -450 C ATOM 1213 O VAL A 164 -32.144 17.886 22.635 1.00117.55 O ANISOU 1213 O VAL A 164 15318 15072 14274 706 -755 -450 O ATOM 1214 CB VAL A 164 -30.289 18.606 25.310 1.00118.87 C ANISOU 1214 CB VAL A 164 15409 15233 14525 723 -802 -452 C ATOM 1215 CG1 VAL A 164 -30.122 19.307 26.648 1.00119.74 C ANISOU 1215 CG1 VAL A 164 15491 15362 14644 756 -853 -472 C ATOM 1216 CG2 VAL A 164 -30.521 17.113 25.505 1.00116.92 C ANISOU 1216 CG2 VAL A 164 15122 15032 14270 703 -758 -438 C ATOM 1217 N ALA A 165 -30.388 19.255 22.217 1.00114.34 N ANISOU 1217 N ALA A 165 14955 14555 13933 683 -760 -431 N ATOM 1218 CA ALA A 165 -30.089 18.691 20.911 1.00113.81 C ANISOU 1218 CA ALA A 165 14919 14450 13871 643 -705 -405 C ATOM 1219 C ALA A 165 -29.415 17.337 21.111 1.00113.89 C ANISOU 1219 C ALA A 165 14888 14471 13914 608 -649 -379 C ATOM 1220 O ALA A 165 -28.290 17.263 21.602 1.00116.66 O ANISOU 1220 O ALA A 165 15215 14795 14315 590 -635 -364 O ATOM 1221 CB ALA A 165 -29.226 19.639 20.115 1.00111.82 C ANISOU 1221 CB ALA A 165 14718 14121 13648 624 -703 -392 C ATOM 1222 N CYS A 166 -30.136 16.272 20.743 1.00110.95 N ANISOU 1222 N CYS A 166 14505 14137 13512 600 -619 -375 N ATOM 1223 CA CYS A 166 -29.717 14.908 21.016 1.00107.91 C ANISOU 1223 CA CYS A 166 14077 13774 13151 572 -571 -355 C ATOM 1224 C CYS A 166 -28.601 14.506 20.055 1.00108.89 C ANISOU 1224 C CYS A 166 14219 13836 13316 525 -514 -325 C ATOM 1225 O CYS A 166 -28.844 14.265 18.873 1.00110.15 O ANISOU 1225 O CYS A 166 14416 13977 13459 507 -484 -316 O ATOM 1226 CB CYS A 166 -30.902 13.955 20.907 1.00106.44 C ANISOU 1226 CB CYS A 166 13877 13648 12919 580 -561 -362 C ATOM 1227 SG CYS A 166 -30.515 12.243 21.357 1.00105.54 S ANISOU 1227 SG CYS A 166 13706 13565 12827 548 -509 -338 S ATOM 1228 N LEU A 167 -27.373 14.460 20.587 1.00107.87 N ANISOU 1228 N LEU A 167 14066 13678 13243 506 -501 -310 N ATOM 1229 CA LEU A 167 -26.203 13.988 19.864 1.00106.09 C ANISOU 1229 CA LEU A 167 13846 13399 13065 461 -445 -283 C ATOM 1230 C LEU A 167 -25.387 13.091 20.791 1.00104.97 C ANISOU 1230 C LEU A 167 13647 13269 12968 446 -425 -271 C ATOM 1231 O LEU A 167 -25.360 13.316 22.000 1.00104.93 O ANISOU 1231 O LEU A 167 13608 13290 12970 469 -462 -282 O ATOM 1232 CB LEU A 167 -25.382 15.192 19.387 1.00105.19 C ANISOU 1232 CB LEU A 167 13771 13217 12978 452 -453 -280 C ATOM 1233 CG LEU A 167 -26.053 16.103 18.358 1.00102.98 C ANISOU 1233 CG LEU A 167 13555 12916 12658 462 -471 -289 C ATOM 1234 CD1 LEU A 167 -25.258 17.386 18.173 1.00101.48 C ANISOU 1234 CD1 LEU A 167 13399 12664 12497 458 -491 -287 C ATOM 1235 CD2 LEU A 167 -26.233 15.391 17.025 1.00102.58 C ANISOU 1235 CD2 LEU A 167 13535 12849 12590 432 -419 -273 C ATOM 1236 N PHE A 168 -24.720 12.085 20.208 1.00103.26 N ANISOU 1236 N PHE A 168 13422 13032 12782 407 -367 -248 N ATOM 1237 CA PHE A 168 -24.061 11.034 20.971 1.00101.74 C ANISOU 1237 CA PHE A 168 13176 12854 12628 391 -345 -236 C ATOM 1238 C PHE A 168 -23.004 11.617 21.908 1.00100.52 C ANISOU 1238 C PHE A 168 12996 12672 12524 394 -367 -236 C ATOM 1239 O PHE A 168 -23.065 11.406 23.118 1.00 98.67 O ANISOU 1239 O PHE A 168 12722 12475 12295 413 -396 -243 O ATOM 1240 CB PHE A 168 -23.467 9.959 20.055 1.00100.92 C ANISOU 1240 CB PHE A 168 13070 12724 12550 348 -280 -213 C ATOM 1241 CG PHE A 168 -22.893 8.773 20.792 1.00100.76 C ANISOU 1241 CG PHE A 168 12997 12721 12567 332 -258 -201 C ATOM 1242 CD1 PHE A 168 -21.591 8.793 21.274 1.00100.49 C ANISOU 1242 CD1 PHE A 168 12936 12649 12596 316 -249 -193 C ATOM 1243 CD2 PHE A 168 -23.660 7.639 21.023 1.00100.48 C ANISOU 1243 CD2 PHE A 168 12936 12738 12503 335 -249 -199 C ATOM 1244 CE1 PHE A 168 -21.069 7.706 21.961 1.00 99.64 C ANISOU 1244 CE1 PHE A 168 12780 12556 12523 302 -233 -182 C ATOM 1245 CE2 PHE A 168 -23.137 6.552 21.708 1.00 99.38 C ANISOU 1245 CE2 PHE A 168 12750 12614 12398 320 -232 -188 C ATOM 1246 CZ PHE A 168 -21.842 6.587 22.176 1.00 99.20 C ANISOU 1246 CZ PHE A 168 12703 12552 12438 304 -225 -179 C ATOM 1247 N GLU A 169 -22.039 12.347 21.336 1.00100.00 N ANISOU 1247 N GLU A 169 12955 12542 12496 374 -354 -229 N ATOM 1248 CA GLU A 169 -20.874 12.813 22.074 1.00100.81 C ANISOU 1248 CA GLU A 169 13035 12611 12657 370 -367 -227 C ATOM 1249 C GLU A 169 -21.256 13.937 23.036 1.00101.25 C ANISOU 1249 C GLU A 169 13091 12684 12696 412 -434 -248 C ATOM 1250 O GLU A 169 -20.412 14.418 23.791 1.00101.93 O ANISOU 1250 O GLU A 169 13157 12746 12825 415 -455 -250 O ATOM 1251 CB GLU A 169 -19.769 13.260 21.113 1.00100.93 C ANISOU 1251 CB GLU A 169 13078 12554 12717 335 -331 -213 C ATOM 1252 CG GLU A 169 -19.189 12.130 20.280 1.00100.32 C ANISOU 1252 CG GLU A 169 12994 12458 12667 293 -264 -193 C ATOM 1253 CD GLU A 169 -17.923 12.480 19.516 1.00100.38 C ANISOU 1253 CD GLU A 169 13017 12395 12728 256 -225 -180 C ATOM 1254 OE1 GLU A 169 -17.310 13.520 19.831 1.00101.19 O ANISOU 1254 OE1 GLU A 169 13127 12463 12858 260 -251 -185 O ATOM 1255 OE2 GLU A 169 -17.551 11.711 18.608 1.00 99.72 O ANISOU 1255 OE2 GLU A 169 12939 12293 12658 221 -169 -166 O ATOM 1256 N ASP A 170 -22.530 14.343 23.007 1.00101.89 N ANISOU 1256 N ASP A 170 13194 12805 12716 444 -468 -266 N ATOM 1257 CA ASP A 170 -23.010 15.424 23.853 1.00103.85 C ANISOU 1257 CA ASP A 170 13445 13072 12943 485 -532 -290 C ATOM 1258 C ASP A 170 -23.572 14.874 25.163 1.00103.28 C ANISOU 1258 C ASP A 170 13325 13066 12852 513 -561 -302 C ATOM 1259 O ASP A 170 -23.511 15.550 26.189 1.00103.57 O ANISOU 1259 O ASP A 170 13346 13114 12893 541 -608 -317 O ATOM 1260 CB ASP A 170 -24.016 16.315 23.119 1.00105.06 C ANISOU 1260 CB ASP A 170 13648 13225 13043 507 -559 -305 C ATOM 1261 CG ASP A 170 -23.376 17.333 22.187 1.00105.98 C ANISOU 1261 CG ASP A 170 13814 13272 13180 491 -554 -299 C ATOM 1262 OD1 ASP A 170 -22.129 17.403 22.153 1.00105.69 O ANISOU 1262 OD1 ASP A 170 13770 13187 13201 463 -531 -283 O ATOM 1263 OD2 ASP A 170 -24.132 18.050 21.504 1.00106.81 O ANISOU 1263 OD2 ASP A 170 13965 13372 13245 505 -575 -310 O ATOM 1264 N VAL A 171 -24.115 13.649 25.121 1.00101.50 N ANISOU 1264 N VAL A 171 13078 12883 12604 503 -532 -294 N ATOM 1265 CA VAL A 171 -24.832 13.095 26.261 1.00 99.04 C ANISOU 1265 CA VAL A 171 12726 12640 12264 528 -556 -306 C ATOM 1266 C VAL A 171 -24.048 11.941 26.886 1.00 98.36 C ANISOU 1266 C VAL A 171 12594 12559 12219 504 -528 -287 C ATOM 1267 O VAL A 171 -24.257 11.622 28.054 1.00 98.24 O ANISOU 1267 O VAL A 171 12543 12588 12197 521 -553 -294 O ATOM 1268 CB VAL A 171 -26.282 12.697 25.912 1.00 97.31 C ANISOU 1268 CB VAL A 171 12518 12477 11980 543 -558 -317 C ATOM 1269 CG1 VAL A 171 -27.103 13.885 25.437 1.00 96.72 C ANISOU 1269 CG1 VAL A 171 12486 12400 11865 572 -595 -339 C ATOM 1270 CG2 VAL A 171 -26.357 11.554 24.908 1.00 96.99 C ANISOU 1270 CG2 VAL A 171 12482 12432 11937 509 -501 -297 C ATOM 1271 N VAL A 172 -23.156 11.321 26.102 1.00 97.32 N ANISOU 1271 N VAL A 172 12465 12382 12129 464 -476 -264 N ATOM 1272 CA VAL A 172 -22.363 10.198 26.579 1.00 97.16 C ANISOU 1272 CA VAL A 172 12403 12361 12151 439 -448 -246 C ATOM 1273 C VAL A 172 -20.936 10.682 26.834 1.00 98.00 C ANISOU 1273 C VAL A 172 12501 12409 12326 425 -448 -239 C ATOM 1274 O VAL A 172 -20.292 11.205 25.927 1.00 99.96 O ANISOU 1274 O VAL A 172 12777 12601 12601 405 -426 -233 O ATOM 1275 CB VAL A 172 -22.403 9.008 25.595 1.00 95.71 C ANISOU 1275 CB VAL A 172 12222 12174 11969 405 -390 -227 C ATOM 1276 CG1 VAL A 172 -21.555 7.837 26.074 1.00 94.73 C ANISOU 1276 CG1 VAL A 172 12055 12046 11891 379 -362 -210 C ATOM 1277 CG2 VAL A 172 -23.825 8.547 25.314 1.00 94.98 C ANISOU 1277 CG2 VAL A 172 12139 12139 11810 418 -391 -235 C ATOM 1278 N PRO A 173 -20.404 10.535 28.073 1.00 97.11 N ANISOU 1278 N PRO A 173 12349 12307 12243 434 -473 -241 N ATOM 1279 CA PRO A 173 -19.023 10.920 28.374 1.00 96.73 C ANISOU 1279 CA PRO A 173 12288 12204 12263 421 -474 -235 C ATOM 1280 C PRO A 173 -18.040 9.946 27.731 1.00 95.65 C ANISOU 1280 C PRO A 173 12137 12028 12178 378 -416 -214 C ATOM 1281 O PRO A 173 -18.311 8.749 27.653 1.00 94.77 O ANISOU 1281 O PRO A 173 12008 11944 12057 363 -388 -203 O ATOM 1282 CB PRO A 173 -18.924 10.805 29.905 1.00 97.19 C ANISOU 1282 CB PRO A 173 12305 12294 12327 444 -516 -243 C ATOM 1283 CG PRO A 173 -20.357 10.689 30.383 1.00 96.14 C ANISOU 1283 CG PRO A 173 12172 12233 12122 475 -544 -257 C ATOM 1284 CD PRO A 173 -21.101 10.008 29.256 1.00 95.87 C ANISOU 1284 CD PRO A 173 12159 12215 12054 458 -502 -249 C ATOM 1285 N MET A 174 -16.894 10.474 27.288 1.00 96.14 N ANISOU 1285 N MET A 174 12207 12026 12296 357 -400 -208 N ATOM 1286 CA MET A 174 -15.914 9.681 26.564 1.00 97.64 C ANISOU 1286 CA MET A 174 12387 12175 12538 315 -344 -191 C ATOM 1287 C MET A 174 -15.114 8.797 27.518 1.00 98.70 C ANISOU 1287 C MET A 174 12470 12310 12720 307 -344 -184 C ATOM 1288 O MET A 174 -14.529 7.807 27.086 1.00100.80 O ANISOU 1288 O MET A 174 12720 12559 13021 276 -299 -170 O ATOM 1289 CB MET A 174 -14.965 10.559 25.741 1.00 98.19 C ANISOU 1289 CB MET A 174 12482 12176 12651 294 -324 -188 C ATOM 1290 CG MET A 174 -15.519 10.913 24.376 1.00 98.88 C ANISOU 1290 CG MET A 174 12620 12250 12701 282 -296 -185 C ATOM 1291 SD MET A 174 -15.837 9.435 23.378 1.00100.26 S ANISOU 1291 SD MET A 174 12793 12440 12860 252 -233 -170 S ATOM 1292 CE MET A 174 -17.293 9.957 22.474 1.00 99.75 C ANISOU 1292 CE MET A 174 12785 12403 12714 269 -241 -177 C ATOM 1293 N ASN A 175 -15.101 9.155 28.810 1.00 98.37 N ANISOU 1293 N ASN A 175 12406 12289 12681 335 -395 -194 N ATOM 1294 CA ASN A 175 -14.433 8.353 29.826 1.00 97.11 C ANISOU 1294 CA ASN A 175 12201 12135 12562 331 -403 -189 C ATOM 1295 C ASN A 175 -15.180 7.034 30.022 1.00 95.78 C ANISOU 1295 C ASN A 175 12014 12019 12358 328 -389 -180 C ATOM 1296 O ASN A 175 -14.572 6.024 30.369 1.00 94.77 O ANISOU 1296 O ASN A 175 11854 11887 12269 310 -373 -170 O ATOM 1297 CB ASN A 175 -14.216 9.119 31.135 1.00 97.24 C ANISOU 1297 CB ASN A 175 12200 12157 12588 362 -462 -203 C ATOM 1298 CG ASN A 175 -15.413 9.942 31.560 1.00 98.44 C ANISOU 1298 CG ASN A 175 12374 12357 12673 401 -508 -220 C ATOM 1299 OD1 ASN A 175 -16.492 9.407 31.803 1.00 98.13 O ANISOU 1299 OD1 ASN A 175 12332 12376 12577 415 -514 -222 O ATOM 1300 ND2 ASN A 175 -15.230 11.248 31.657 1.00100.50 N ANISOU 1300 ND2 ASN A 175 12653 12591 12939 419 -541 -233 N ATOM 1301 N TYR A 176 -16.499 7.058 29.786 1.00 94.36 N ANISOU 1301 N TYR A 176 11856 11889 12109 345 -395 -186 N ATOM 1302 CA TYR A 176 -17.312 5.854 29.846 1.00 92.69 C ANISOU 1302 CA TYR A 176 11631 11729 11859 341 -380 -178 C ATOM 1303 C TYR A 176 -17.008 4.963 28.643 1.00 92.50 C ANISOU 1303 C TYR A 176 11613 11678 11855 304 -319 -162 C ATOM 1304 O TYR A 176 -16.825 3.759 28.798 1.00 91.92 O ANISOU 1304 O TYR A 176 11513 11615 11797 286 -298 -150 O ATOM 1305 CB TYR A 176 -18.805 6.188 29.930 1.00 91.58 C ANISOU 1305 CB TYR A 176 11511 11647 11640 370 -405 -190 C ATOM 1306 CG TYR A 176 -19.709 4.990 29.771 1.00 90.81 C ANISOU 1306 CG TYR A 176 11404 11599 11501 362 -383 -182 C ATOM 1307 CD1 TYR A 176 -19.972 4.146 30.839 1.00 90.76 C ANISOU 1307 CD1 TYR A 176 11364 11638 11483 368 -400 -178 C ATOM 1308 CD2 TYR A 176 -20.282 4.684 28.545 1.00 90.03 C ANISOU 1308 CD2 TYR A 176 11332 11500 11375 348 -346 -177 C ATOM 1309 CE1 TYR A 176 -20.789 3.035 30.698 1.00 90.57 C ANISOU 1309 CE1 TYR A 176 11332 11658 11423 359 -380 -169 C ATOM 1310 CE2 TYR A 176 -21.099 3.575 28.386 1.00 89.77 C ANISOU 1310 CE2 TYR A 176 11291 11512 11307 340 -326 -169 C ATOM 1311 CZ TYR A 176 -21.353 2.748 29.466 1.00 90.50 C ANISOU 1311 CZ TYR A 176 11348 11648 11389 345 -343 -165 C ATOM 1312 OH TYR A 176 -22.159 1.656 29.320 1.00 90.77 O ANISOU 1312 OH TYR A 176 11374 11724 11389 336 -325 -157 O ATOM 1313 N MET A 177 -16.962 5.570 27.451 1.00 93.06 N ANISOU 1313 N MET A 177 11720 11714 11923 292 -293 -163 N ATOM 1314 CA MET A 177 -16.822 4.826 26.210 1.00 94.35 C ANISOU 1314 CA MET A 177 11897 11857 12096 259 -236 -150 C ATOM 1315 C MET A 177 -15.426 4.215 26.106 1.00 94.95 C ANISOU 1315 C MET A 177 11945 11883 12247 228 -203 -139 C ATOM 1316 O MET A 177 -15.260 3.161 25.496 1.00 95.82 O ANISOU 1316 O MET A 177 12047 11989 12372 201 -160 -128 O ATOM 1317 CB MET A 177 -17.079 5.712 24.987 1.00 96.67 C ANISOU 1317 CB MET A 177 12239 12123 12368 255 -219 -154 C ATOM 1318 CG MET A 177 -18.541 6.075 24.786 1.00 99.14 C ANISOU 1318 CG MET A 177 12581 12483 12604 281 -241 -164 C ATOM 1319 SD MET A 177 -19.675 4.659 24.842 1.00103.32 S ANISOU 1319 SD MET A 177 13095 13078 13084 281 -227 -158 S ATOM 1320 CE MET A 177 -19.069 3.670 23.475 1.00100.35 C ANISOU 1320 CE MET A 177 12727 12663 12740 237 -156 -140 C ATOM 1321 N VAL A 178 -14.433 4.883 26.705 1.00 94.38 N ANISOU 1321 N VAL A 178 11858 11775 12227 230 -224 -144 N ATOM 1322 CA VAL A 178 -13.047 4.463 26.583 1.00 94.04 C ANISOU 1322 CA VAL A 178 11790 11681 12261 201 -194 -137 C ATOM 1323 C VAL A 178 -12.684 3.520 27.729 1.00 94.00 C ANISOU 1323 C VAL A 178 11738 11694 12284 204 -213 -132 C ATOM 1324 O VAL A 178 -12.351 2.360 27.490 1.00 94.69 O ANISOU 1324 O VAL A 178 11804 11777 12395 181 -180 -122 O ATOM 1325 CB VAL A 178 -12.086 5.665 26.483 1.00 94.43 C ANISOU 1325 CB VAL A 178 11849 11674 12356 198 -202 -144 C ATOM 1326 CG1 VAL A 178 -10.632 5.251 26.653 1.00 94.93 C ANISOU 1326 CG1 VAL A 178 11877 11689 12503 173 -182 -140 C ATOM 1327 CG2 VAL A 178 -12.273 6.423 25.176 1.00 94.82 C ANISOU 1327 CG2 VAL A 178 11945 11697 12386 186 -174 -144 C ATOM 1328 N TYR A 179 -12.755 4.023 28.969 1.00 93.24 N ANISOU 1328 N TYR A 179 11628 11618 12183 232 -267 -141 N ATOM 1329 CA TYR A 179 -12.272 3.283 30.124 1.00 91.86 C ANISOU 1329 CA TYR A 179 11410 11452 12039 235 -289 -138 C ATOM 1330 C TYR A 179 -13.222 2.140 30.470 1.00 90.55 C ANISOU 1330 C TYR A 179 11233 11344 11826 239 -290 -129 C ATOM 1331 O TYR A 179 -12.784 1.005 30.640 1.00 89.64 O ANISOU 1331 O TYR A 179 11092 11227 11742 221 -273 -119 O ATOM 1332 CB TYR A 179 -12.023 4.211 31.317 1.00 92.60 C ANISOU 1332 CB TYR A 179 11495 11547 12143 264 -346 -150 C ATOM 1333 CG TYR A 179 -10.862 5.159 31.148 1.00 94.27 C ANISOU 1333 CG TYR A 179 11707 11696 12416 257 -347 -156 C ATOM 1334 CD1 TYR A 179 -9.735 4.789 30.429 1.00 95.14 C ANISOU 1334 CD1 TYR A 179 11806 11752 12593 223 -304 -150 C ATOM 1335 CD2 TYR A 179 -10.877 6.422 31.723 1.00 94.38 C ANISOU 1335 CD2 TYR A 179 11732 11705 12424 284 -393 -170 C ATOM 1336 CE1 TYR A 179 -8.661 5.651 30.270 1.00 95.04 C ANISOU 1336 CE1 TYR A 179 11792 11681 12637 215 -303 -156 C ATOM 1337 CE2 TYR A 179 -9.811 7.295 31.577 1.00 94.72 C ANISOU 1337 CE2 TYR A 179 11775 11689 12524 277 -395 -176 C ATOM 1338 CZ TYR A 179 -8.700 6.909 30.848 1.00 95.29 C ANISOU 1338 CZ TYR A 179 11836 11709 12662 241 -349 -168 C ATOM 1339 OH TYR A 179 -7.646 7.762 30.694 1.00 96.08 O ANISOU 1339 OH TYR A 179 11935 11751 12821 231 -349 -174 O ATOM 1340 N PHE A 180 -14.519 2.450 30.560 1.00 90.72 N ANISOU 1340 N PHE A 180 11277 11419 11775 262 -310 -135 N ATOM 1341 CA PHE A 180 -15.495 1.484 31.034 1.00 90.59 C ANISOU 1341 CA PHE A 180 11248 11461 11709 269 -317 -129 C ATOM 1342 C PHE A 180 -15.905 0.540 29.907 1.00 88.82 C ANISOU 1342 C PHE A 180 11035 11243 11470 243 -266 -117 C ATOM 1343 O PHE A 180 -15.793 -0.675 30.051 1.00 88.67 O ANISOU 1343 O PHE A 180 10993 11233 11463 226 -250 -105 O ATOM 1344 CB PHE A 180 -16.703 2.180 31.669 1.00 93.12 C ANISOU 1344 CB PHE A 180 11583 11838 11960 304 -360 -142 C ATOM 1345 CG PHE A 180 -17.599 1.261 32.461 1.00 94.56 C ANISOU 1345 CG PHE A 180 11747 12084 12096 313 -375 -137 C ATOM 1346 CD1 PHE A 180 -17.351 1.011 33.803 1.00 94.84 C ANISOU 1346 CD1 PHE A 180 11754 12138 12141 324 -412 -136 C ATOM 1347 CD2 PHE A 180 -18.684 0.632 31.864 1.00 94.73 C ANISOU 1347 CD2 PHE A 180 11781 12147 12067 308 -353 -132 C ATOM 1348 CE1 PHE A 180 -18.170 0.160 34.531 1.00 94.99 C ANISOU 1348 CE1 PHE A 180 11758 12216 12117 329 -425 -130 C ATOM 1349 CE2 PHE A 180 -19.502 -0.218 32.594 1.00 94.53 C ANISOU 1349 CE2 PHE A 180 11738 12179 12000 313 -366 -127 C ATOM 1350 CZ PHE A 180 -19.244 -0.452 33.925 1.00 94.20 C ANISOU 1350 CZ PHE A 180 11669 12156 11966 323 -401 -126 C ATOM 1351 N ASN A 181 -16.377 1.110 28.794 1.00 87.96 N ANISOU 1351 N ASN A 181 10962 11126 11333 241 -244 -122 N ATOM 1352 CA ASN A 181 -16.993 0.331 27.732 1.00 88.12 C ANISOU 1352 CA ASN A 181 10998 11158 11325 223 -202 -113 C ATOM 1353 C ASN A 181 -15.925 -0.406 26.926 1.00 86.95 C ANISOU 1353 C ASN A 181 10840 10959 11238 187 -152 -102 C ATOM 1354 O ASN A 181 -15.971 -1.629 26.810 1.00 85.11 O ANISOU 1354 O ASN A 181 10589 10738 11010 170 -129 -91 O ATOM 1355 CB ASN A 181 -17.906 1.180 26.842 1.00 89.22 C ANISOU 1355 CB ASN A 181 11180 11307 11411 235 -198 -122 C ATOM 1356 CG ASN A 181 -18.891 0.353 26.043 1.00 89.63 C ANISOU 1356 CG ASN A 181 11247 11392 11418 226 -169 -116 C ATOM 1357 OD1 ASN A 181 -18.661 0.066 24.869 1.00 89.12 O ANISOU 1357 OD1 ASN A 181 11200 11298 11365 202 -125 -110 O ATOM 1358 ND2 ASN A 181 -19.985 -0.048 26.673 1.00 89.67 N ANISOU 1358 ND2 ASN A 181 11242 11457 11369 244 -193 -118 N ATOM 1359 N PHE A 182 -14.967 0.352 26.377 1.00 86.25 N ANISOU 1359 N PHE A 182 10762 10815 11195 175 -136 -106 N ATOM 1360 CA PHE A 182 -13.998 -0.202 25.445 1.00 86.31 C ANISOU 1360 CA PHE A 182 10765 10773 11256 141 -84 -99 C ATOM 1361 C PHE A 182 -13.028 -1.140 26.158 1.00 85.94 C ANISOU 1361 C PHE A 182 10673 10710 11270 127 -83 -92 C ATOM 1362 O PHE A 182 -12.874 -2.287 25.746 1.00 85.43 O ANISOU 1362 O PHE A 182 10594 10643 11221 105 -50 -83 O ATOM 1363 CB PHE A 182 -13.270 0.898 24.667 1.00 87.49 C ANISOU 1363 CB PHE A 182 10940 10869 11435 131 -66 -105 C ATOM 1364 CG PHE A 182 -12.243 0.397 23.680 1.00 88.27 C ANISOU 1364 CG PHE A 182 11033 10916 11590 94 -10 -99 C ATOM 1365 CD1 PHE A 182 -12.492 -0.722 22.897 1.00 88.05 C ANISOU 1365 CD1 PHE A 182 11006 10897 11553 73 32 -91 C ATOM 1366 CD2 PHE A 182 -11.032 1.054 23.521 1.00 88.61 C ANISOU 1366 CD2 PHE A 182 11071 10903 11694 80 1 -104 C ATOM 1367 CE1 PHE A 182 -11.550 -1.180 21.988 1.00 87.79 C ANISOU 1367 CE1 PHE A 182 10967 10818 11570 40 85 -88 C ATOM 1368 CE2 PHE A 182 -10.092 0.597 22.609 1.00 89.11 C ANISOU 1368 CE2 PHE A 182 11129 10922 11808 45 55 -100 C ATOM 1369 CZ PHE A 182 -10.352 -0.518 21.844 1.00 88.57 C ANISOU 1369 CZ PHE A 182 11061 10863 11729 26 97 -93 C ATOM 1370 N PHE A 183 -12.381 -0.644 27.219 1.00 85.89 N ANISOU 1370 N PHE A 183 10645 10692 11299 141 -122 -98 N ATOM 1371 CA PHE A 183 -11.316 -1.385 27.878 1.00 85.10 C ANISOU 1371 CA PHE A 183 10502 10567 11263 128 -124 -94 C ATOM 1372 C PHE A 183 -11.886 -2.564 28.662 1.00 83.83 C ANISOU 1372 C PHE A 183 10320 10453 11080 133 -142 -85 C ATOM 1373 O PHE A 183 -11.567 -3.714 28.369 1.00 83.67 O ANISOU 1373 O PHE A 183 10281 10424 11086 111 -113 -76 O ATOM 1374 CB PHE A 183 -10.446 -0.463 28.739 1.00 85.69 C ANISOU 1374 CB PHE A 183 10563 10612 11383 142 -161 -104 C ATOM 1375 CG PHE A 183 -9.573 0.497 27.969 1.00 86.94 C ANISOU 1375 CG PHE A 183 10735 10713 11584 128 -138 -111 C ATOM 1376 CD1 PHE A 183 -9.278 0.280 26.630 1.00 87.44 C ANISOU 1376 CD1 PHE A 183 10814 10746 11662 99 -81 -108 C ATOM 1377 CD2 PHE A 183 -9.022 1.609 28.590 1.00 87.63 C ANISOU 1377 CD2 PHE A 183 10820 10777 11697 144 -174 -121 C ATOM 1378 CE1 PHE A 183 -8.468 1.161 25.927 1.00 88.19 C ANISOU 1378 CE1 PHE A 183 10923 10789 11796 85 -59 -114 C ATOM 1379 CE2 PHE A 183 -8.212 2.489 27.887 1.00 88.33 C ANISOU 1379 CE2 PHE A 183 10923 10813 11827 129 -152 -127 C ATOM 1380 CZ PHE A 183 -7.936 2.265 26.556 1.00 88.22 C ANISOU 1380 CZ PHE A 183 10925 10769 11825 99 -94 -123 C ATOM 1381 N ALA A 184 -12.744 -2.263 29.643 1.00 82.11 N ANISOU 1381 N ALA A 184 10103 10284 10811 162 -188 -87 N ATOM 1382 CA ALA A 184 -13.226 -3.266 30.577 1.00 82.39 C ANISOU 1382 CA ALA A 184 10116 10363 10825 167 -211 -79 C ATOM 1383 C ALA A 184 -14.171 -4.251 29.890 1.00 82.95 C ANISOU 1383 C ALA A 184 10196 10469 10851 155 -181 -69 C ATOM 1384 O ALA A 184 -13.975 -5.460 29.983 1.00 81.66 O ANISOU 1384 O ALA A 184 10012 10308 10707 137 -167 -57 O ATOM 1385 CB ALA A 184 -13.872 -2.598 31.766 1.00 82.15 C ANISOU 1385 CB ALA A 184 10086 10376 10752 200 -266 -86 C ATOM 1386 N CYS A 185 -15.178 -3.727 29.182 1.00 85.94 N ANISOU 1386 N CYS A 185 10608 10873 11172 164 -171 -73 N ATOM 1387 CA CYS A 185 -16.320 -4.529 28.767 1.00 88.48 C ANISOU 1387 CA CYS A 185 10940 11240 11438 160 -155 -66 C ATOM 1388 C CYS A 185 -16.112 -5.165 27.392 1.00 89.02 C ANISOU 1388 C CYS A 185 11020 11281 11524 131 -99 -59 C ATOM 1389 O CYS A 185 -16.728 -6.186 27.092 1.00 87.41 O ANISOU 1389 O CYS A 185 10814 11103 11295 121 -81 -50 O ATOM 1390 CB CYS A 185 -17.602 -3.706 28.787 1.00 90.40 C ANISOU 1390 CB CYS A 185 11210 11530 11607 187 -177 -76 C ATOM 1391 SG CYS A 185 -18.014 -3.075 30.435 1.00 94.16 S ANISOU 1391 SG CYS A 185 11672 12050 12055 222 -242 -85 S ATOM 1392 N VAL A 186 -15.252 -4.560 26.560 1.00 90.87 N ANISOU 1392 N VAL A 186 11267 11461 11800 119 -71 -65 N ATOM 1393 CA VAL A 186 -15.055 -5.043 25.200 1.00 91.81 C ANISOU 1393 CA VAL A 186 11401 11552 11932 92 -17 -61 C ATOM 1394 C VAL A 186 -13.672 -5.678 25.048 1.00 92.21 C ANISOU 1394 C VAL A 186 11423 11551 12062 66 10 -57 C ATOM 1395 O VAL A 186 -13.569 -6.832 24.635 1.00 91.65 O ANISOU 1395 O VAL A 186 11340 11478 12006 46 39 -49 O ATOM 1396 CB VAL A 186 -15.315 -3.953 24.139 1.00 91.79 C ANISOU 1396 CB VAL A 186 11441 11532 11905 94 2 -69 C ATOM 1397 CG1 VAL A 186 -14.984 -4.433 22.731 1.00 90.94 C ANISOU 1397 CG1 VAL A 186 11349 11391 11814 65 60 -65 C ATOM 1398 CG2 VAL A 186 -16.743 -3.431 24.197 1.00 92.56 C ANISOU 1398 CG2 VAL A 186 11566 11681 11923 120 -24 -74 C ATOM 1399 N LEU A 187 -12.616 -4.923 25.376 1.00 92.08 N ANISOU 1399 N LEU A 187 11395 11492 12097 66 0 -65 N ATOM 1400 CA LEU A 187 -11.259 -5.333 25.048 1.00 92.04 C ANISOU 1400 CA LEU A 187 11367 11432 12171 41 31 -65 C ATOM 1401 C LEU A 187 -10.832 -6.520 25.908 1.00 92.23 C ANISOU 1401 C LEU A 187 11350 11462 12232 35 16 -58 C ATOM 1402 O LEU A 187 -10.201 -7.445 25.400 1.00 92.38 O ANISOU 1402 O LEU A 187 11352 11455 12293 11 50 -55 O ATOM 1403 CB LEU A 187 -10.300 -4.148 25.207 1.00 92.90 C ANISOU 1403 CB LEU A 187 11476 11497 12325 44 21 -76 C ATOM 1404 CG LEU A 187 -8.996 -4.247 24.414 1.00 93.53 C ANISOU 1404 CG LEU A 187 11544 11516 12477 14 66 -80 C ATOM 1405 CD1 LEU A 187 -9.271 -4.331 22.920 1.00 93.32 C ANISOU 1405 CD1 LEU A 187 11549 11479 12430 -7 121 -78 C ATOM 1406 CD2 LEU A 187 -8.081 -3.072 24.723 1.00 93.65 C ANISOU 1406 CD2 LEU A 187 11556 11490 12537 18 50 -90 C ATOM 1407 N VAL A 188 -11.190 -6.487 27.199 1.00 92.57 N ANISOU 1407 N VAL A 188 11379 11539 12256 57 -35 -56 N ATOM 1408 CA VAL A 188 -10.800 -7.522 28.147 1.00 92.92 C ANISOU 1408 CA VAL A 188 11387 11588 12331 54 -57 -49 C ATOM 1409 C VAL A 188 -11.397 -8.872 27.740 1.00 94.88 C ANISOU 1409 C VAL A 188 11632 11862 12557 39 -34 -37 C ATOM 1410 O VAL A 188 -10.652 -9.842 27.615 1.00 95.21 O ANISOU 1410 O VAL A 188 11650 11877 12650 19 -16 -33 O ATOM 1411 CB VAL A 188 -11.121 -7.139 29.608 1.00 90.89 C ANISOU 1411 CB VAL A 188 11119 11363 12050 82 -117 -49 C ATOM 1412 CG1 VAL A 188 -11.113 -8.346 30.535 1.00 89.52 C ANISOU 1412 CG1 VAL A 188 10917 11210 11886 79 -140 -38 C ATOM 1413 CG2 VAL A 188 -10.176 -6.068 30.128 1.00 90.54 C ANISOU 1413 CG2 VAL A 188 11067 11281 12052 93 -142 -61 C ATOM 1414 N PRO A 189 -12.731 -9.003 27.524 1.00 96.27 N ANISOU 1414 N PRO A 189 11831 12090 12659 48 -35 -31 N ATOM 1415 CA PRO A 189 -13.310 -10.272 27.073 1.00 95.96 C ANISOU 1415 CA PRO A 189 11790 12072 12598 32 -12 -20 C ATOM 1416 C PRO A 189 -12.793 -10.748 25.716 1.00 95.09 C ANISOU 1416 C PRO A 189 11685 11923 12521 6 45 -21 C ATOM 1417 O PRO A 189 -12.753 -11.950 25.464 1.00 94.82 O ANISOU 1417 O PRO A 189 11637 11889 12501 -12 63 -13 O ATOM 1418 CB PRO A 189 -14.817 -9.989 26.982 1.00 96.79 C ANISOU 1418 CB PRO A 189 11923 12236 12618 49 -22 -18 C ATOM 1419 CG PRO A 189 -15.027 -8.801 27.894 1.00 97.21 C ANISOU 1419 CG PRO A 189 11981 12305 12648 77 -66 -27 C ATOM 1420 CD PRO A 189 -13.765 -7.977 27.746 1.00 96.85 C ANISOU 1420 CD PRO A 189 11931 12201 12665 74 -60 -37 C ATOM 1421 N LEU A 190 -12.402 -9.801 24.853 1.00 94.19 N ANISOU 1421 N LEU A 190 11592 11776 12420 2 71 -32 N ATOM 1422 CA LEU A 190 -11.908 -10.140 23.527 1.00 94.15 C ANISOU 1422 CA LEU A 190 11596 11734 12443 -23 127 -34 C ATOM 1423 C LEU A 190 -10.536 -10.802 23.626 1.00 94.35 C ANISOU 1423 C LEU A 190 11584 11711 12552 -43 141 -37 C ATOM 1424 O LEU A 190 -10.261 -11.751 22.896 1.00 93.93 O ANISOU 1424 O LEU A 190 11523 11642 12522 -64 178 -35 O ATOM 1425 CB LEU A 190 -11.871 -8.896 22.632 1.00 93.71 C ANISOU 1425 CB LEU A 190 11575 11656 12374 -23 149 -44 C ATOM 1426 CG LEU A 190 -13.170 -8.572 21.892 1.00 93.08 C ANISOU 1426 CG LEU A 190 11536 11612 12217 -14 159 -42 C ATOM 1427 CD1 LEU A 190 -12.952 -7.460 20.877 1.00 93.37 C ANISOU 1427 CD1 LEU A 190 11609 11617 12251 -19 186 -50 C ATOM 1428 CD2 LEU A 190 -13.742 -9.806 21.209 1.00 91.77 C ANISOU 1428 CD2 LEU A 190 11373 11465 12030 -29 188 -34 C ATOM 1429 N LEU A 191 -9.691 -10.298 24.535 1.00 95.68 N ANISOU 1429 N LEU A 191 11730 11857 12765 -35 111 -43 N ATOM 1430 CA LEU A 191 -8.374 -10.873 24.765 1.00 96.83 C ANISOU 1430 CA LEU A 191 11839 11958 12994 -50 118 -47 C ATOM 1431 C LEU A 191 -8.520 -12.277 25.346 1.00 97.55 C ANISOU 1431 C LEU A 191 11904 12069 13092 -55 102 -37 C ATOM 1432 O LEU A 191 -7.705 -13.152 25.062 1.00 98.85 O ANISOU 1432 O LEU A 191 12043 12201 13313 -74 124 -39 O ATOM 1433 CB LEU A 191 -7.562 -9.973 25.704 1.00 95.83 C ANISOU 1433 CB LEU A 191 11695 11808 12908 -37 82 -56 C ATOM 1434 CG LEU A 191 -7.163 -8.602 25.156 1.00 96.10 C ANISOU 1434 CG LEU A 191 11750 11812 12952 -36 97 -67 C ATOM 1435 CD1 LEU A 191 -6.119 -7.950 26.050 1.00 94.71 C ANISOU 1435 CD1 LEU A 191 11548 11602 12834 -28 65 -76 C ATOM 1436 CD2 LEU A 191 -6.653 -8.701 23.724 1.00 97.52 C ANISOU 1436 CD2 LEU A 191 11940 11955 13158 -64 160 -72 C ATOM 1437 N LEU A 192 -9.568 -12.480 26.154 1.00 96.96 N ANISOU 1437 N LEU A 192 11835 12046 12959 -38 64 -26 N ATOM 1438 CA LEU A 192 -9.830 -13.777 26.757 1.00 97.25 C ANISOU 1438 CA LEU A 192 11851 12105 12994 -42 46 -13 C ATOM 1439 C LEU A 192 -10.181 -14.788 25.669 1.00 97.76 C ANISOU 1439 C LEU A 192 11923 12172 13048 -62 89 -9 C ATOM 1440 O LEU A 192 -9.692 -15.914 25.696 1.00 97.66 O ANISOU 1440 O LEU A 192 11886 12143 13077 -77 95 -5 O ATOM 1441 CB LEU A 192 -10.953 -13.656 27.793 1.00 97.65 C ANISOU 1441 CB LEU A 192 11911 12215 12977 -20 -1 -3 C ATOM 1442 CG LEU A 192 -10.628 -12.845 29.048 1.00 97.78 C ANISOU 1442 CG LEU A 192 11916 12233 13003 1 -50 -7 C ATOM 1443 CD1 LEU A 192 -11.707 -13.036 30.103 1.00 96.79 C ANISOU 1443 CD1 LEU A 192 11795 12168 12814 19 -93 4 C ATOM 1444 CD2 LEU A 192 -9.264 -13.216 29.612 1.00 98.23 C ANISOU 1444 CD2 LEU A 192 11939 12242 13142 -7 -64 -11 C ATOM 1445 N MET A 193 -11.011 -14.367 24.706 1.00 99.13 N ANISOU 1445 N MET A 193 12131 12365 13170 -62 118 -9 N ATOM 1446 CA MET A 193 -11.411 -15.229 23.606 1.00100.93 C ANISOU 1446 CA MET A 193 12370 12596 13384 -80 160 -6 C ATOM 1447 C MET A 193 -10.183 -15.646 22.802 1.00101.87 C ANISOU 1447 C MET A 193 12472 12658 13575 -103 202 -16 C ATOM 1448 O MET A 193 -10.146 -16.754 22.273 1.00103.84 O ANISOU 1448 O MET A 193 12713 12903 13839 -119 226 -13 O ATOM 1449 CB MET A 193 -12.418 -14.545 22.677 1.00102.60 C ANISOU 1449 CB MET A 193 12623 12831 13529 -74 182 -7 C ATOM 1450 CG MET A 193 -13.766 -14.304 23.325 1.00104.99 C ANISOU 1450 CG MET A 193 12942 13194 13756 -53 146 1 C ATOM 1451 SD MET A 193 -14.949 -13.541 22.190 1.00108.42 S ANISOU 1451 SD MET A 193 13425 13653 14116 -45 170 -3 S ATOM 1452 CE MET A 193 -15.824 -12.458 23.320 1.00107.54 C ANISOU 1452 CE MET A 193 13323 13589 13948 -12 116 -5 C ATOM 1453 N LEU A 194 -9.183 -14.756 22.727 1.00101.23 N ANISOU 1453 N LEU A 194 12386 12536 13541 -104 210 -29 N ATOM 1454 CA LEU A 194 -7.932 -15.072 22.055 1.00100.46 C ANISOU 1454 CA LEU A 194 12268 12385 13518 -126 249 -41 C ATOM 1455 C LEU A 194 -7.248 -16.222 22.789 1.00100.18 C ANISOU 1455 C LEU A 194 12190 12334 13538 -133 229 -39 C ATOM 1456 O LEU A 194 -6.900 -17.227 22.176 1.00 99.82 O ANISOU 1456 O LEU A 194 12132 12272 13524 -151 258 -42 O ATOM 1457 CB LEU A 194 -7.033 -13.831 22.012 1.00100.23 C ANISOU 1457 CB LEU A 194 12238 12317 13527 -125 255 -54 C ATOM 1458 CG LEU A 194 -5.702 -14.016 21.284 1.00100.29 C ANISOU 1458 CG LEU A 194 12225 12268 13613 -149 298 -69 C ATOM 1459 CD1 LEU A 194 -5.864 -13.788 19.789 1.00100.32 C ANISOU 1459 CD1 LEU A 194 12260 12261 13596 -166 357 -74 C ATOM 1460 CD2 LEU A 194 -4.642 -13.087 21.853 1.00101.37 C ANISOU 1460 CD2 LEU A 194 12343 12369 13805 -145 282 -80 C ATOM 1461 N GLY A 195 -7.086 -16.063 24.108 1.00 99.90 N ANISOU 1461 N GLY A 195 12136 12307 13514 -117 176 -35 N ATOM 1462 CA GLY A 195 -6.437 -17.056 24.948 1.00101.23 C ANISOU 1462 CA GLY A 195 12267 12461 13734 -120 148 -33 C ATOM 1463 C GLY A 195 -7.221 -18.364 25.016 1.00101.05 C ANISOU 1463 C GLY A 195 12243 12470 13679 -126 142 -18 C ATOM 1464 O GLY A 195 -6.629 -19.434 25.143 1.00101.84 O ANISOU 1464 O GLY A 195 12317 12550 13829 -138 140 -18 O ATOM 1465 N VAL A 196 -8.554 -18.262 24.929 1.00101.04 N ANISOU 1465 N VAL A 196 12272 12521 13598 -117 137 -5 N ATOM 1466 CA VAL A 196 -9.428 -19.421 25.012 1.00101.85 C ANISOU 1466 CA VAL A 196 12377 12659 13663 -122 129 10 C ATOM 1467 C VAL A 196 -9.263 -20.270 23.753 1.00103.00 C ANISOU 1467 C VAL A 196 12523 12784 13829 -143 179 5 C ATOM 1468 O VAL A 196 -9.151 -21.489 23.849 1.00103.33 O ANISOU 1468 O VAL A 196 12547 12822 13893 -154 175 11 O ATOM 1469 CB VAL A 196 -10.899 -19.033 25.272 1.00102.04 C ANISOU 1469 CB VAL A 196 12429 12743 13597 -106 111 22 C ATOM 1470 CG1 VAL A 196 -11.862 -20.161 24.931 1.00101.04 C ANISOU 1470 CG1 VAL A 196 12310 12651 13429 -116 119 36 C ATOM 1471 CG2 VAL A 196 -11.115 -18.574 26.707 1.00101.65 C ANISOU 1471 CG2 VAL A 196 12373 12721 13528 -86 55 29 C ATOM 1472 N TYR A 197 -9.234 -19.616 22.584 1.00105.19 N ANISOU 1472 N TYR A 197 12822 13046 14098 -149 225 -5 N ATOM 1473 CA TYR A 197 -9.099 -20.323 21.320 1.00108.17 C ANISOU 1473 CA TYR A 197 13204 13405 14489 -169 276 -11 C ATOM 1474 C TYR A 197 -7.679 -20.859 21.152 1.00109.96 C ANISOU 1474 C TYR A 197 13396 13577 14805 -184 293 -26 C ATOM 1475 O TYR A 197 -7.479 -21.867 20.477 1.00111.83 O ANISOU 1475 O TYR A 197 13624 13800 15066 -200 321 -29 O ATOM 1476 CB TYR A 197 -9.532 -19.457 20.134 1.00109.41 C ANISOU 1476 CB TYR A 197 13400 13565 14607 -170 318 -18 C ATOM 1477 CG TYR A 197 -11.024 -19.352 19.937 1.00111.36 C ANISOU 1477 CG TYR A 197 13681 13864 14768 -160 312 -6 C ATOM 1478 CD1 TYR A 197 -11.776 -20.451 19.547 1.00112.68 C ANISOU 1478 CD1 TYR A 197 13853 14055 14906 -168 320 3 C ATOM 1479 CD2 TYR A 197 -11.686 -18.150 20.129 1.00111.75 C ANISOU 1479 CD2 TYR A 197 13757 13939 14765 -142 296 -5 C ATOM 1480 CE1 TYR A 197 -13.148 -20.361 19.365 1.00112.87 C ANISOU 1480 CE1 TYR A 197 13905 14127 14852 -158 314 13 C ATOM 1481 CE2 TYR A 197 -13.056 -18.042 19.949 1.00112.92 C ANISOU 1481 CE2 TYR A 197 13935 14135 14836 -131 289 4 C ATOM 1482 CZ TYR A 197 -13.790 -19.151 19.566 1.00112.50 C ANISOU 1482 CZ TYR A 197 13885 14106 14756 -140 299 12 C ATOM 1483 OH TYR A 197 -15.140 -19.052 19.388 1.00111.27 O ANISOU 1483 OH TYR A 197 13756 13996 14526 -130 291 19 O ATOM 1484 N LEU A 198 -6.703 -20.184 21.773 1.00110.13 N ANISOU 1484 N LEU A 198 13398 13569 14878 -179 277 -35 N ATOM 1485 CA LEU A 198 -5.316 -20.619 21.710 1.00111.39 C ANISOU 1485 CA LEU A 198 13521 13676 15127 -193 289 -51 C ATOM 1486 C LEU A 198 -5.163 -21.969 22.407 1.00112.74 C ANISOU 1486 C LEU A 198 13662 13847 15327 -196 258 -44 C ATOM 1487 O LEU A 198 -4.496 -22.859 21.887 1.00114.65 O ANISOU 1487 O LEU A 198 13883 14059 15621 -211 282 -55 O ATOM 1488 CB LEU A 198 -4.407 -19.556 22.337 1.00111.05 C ANISOU 1488 CB LEU A 198 13463 13604 15126 -184 271 -62 C ATOM 1489 CG LEU A 198 -3.983 -18.419 21.407 1.00111.77 C ANISOU 1489 CG LEU A 198 13571 13671 15226 -191 315 -76 C ATOM 1490 CD1 LEU A 198 -3.334 -17.289 22.191 1.00112.96 C ANISOU 1490 CD1 LEU A 198 13711 13802 15404 -179 287 -83 C ATOM 1491 CD2 LEU A 198 -3.046 -18.920 20.316 1.00111.46 C ANISOU 1491 CD2 LEU A 198 13516 13589 15246 -215 370 -94 C ATOM 1492 N ARG A 199 -5.807 -22.113 23.572 1.00114.33 N ANISOU 1492 N ARG A 199 13864 14083 15493 -181 205 -27 N ATOM 1493 CA ARG A 199 -5.754 -23.343 24.345 1.00116.08 C ANISOU 1493 CA ARG A 199 14062 14307 15735 -183 169 -17 C ATOM 1494 C ARG A 199 -6.540 -24.446 23.638 1.00115.72 C ANISOU 1494 C ARG A 199 14029 14284 15657 -195 190 -7 C ATOM 1495 O ARG A 199 -6.324 -25.623 23.912 1.00118.14 O ANISOU 1495 O ARG A 199 14314 14580 15992 -204 174 -3 O ATOM 1496 CB ARG A 199 -6.280 -23.116 25.766 1.00119.69 C ANISOU 1496 CB ARG A 199 14522 14799 16157 -166 108 0 C ATOM 1497 CG ARG A 199 -5.327 -22.350 26.672 1.00125.80 C ANISOU 1497 CG ARG A 199 15275 15545 16979 -154 77 -9 C ATOM 1498 CD ARG A 199 -6.068 -21.726 27.838 1.00131.71 C ANISOU 1498 CD ARG A 199 16037 16334 17672 -134 28 5 C ATOM 1499 NE ARG A 199 -5.223 -20.866 28.655 1.00136.17 N ANISOU 1499 NE ARG A 199 16587 16875 18277 -121 -2 -5 N ATOM 1500 CZ ARG A 199 -5.669 -19.939 29.499 1.00139.34 C ANISOU 1500 CZ ARG A 199 17002 17304 18638 -102 -37 1 C ATOM 1501 NH1 ARG A 199 -6.968 -19.733 29.641 1.00139.26 N ANISOU 1501 NH1 ARG A 199 17019 17349 18545 -92 -45 15 N ATOM 1502 NH2 ARG A 199 -4.811 -19.215 30.195 1.00141.67 N ANISOU 1502 NH2 ARG A 199 17281 17571 18977 -91 -63 -10 N ATOM 1503 N ILE A 200 -7.446 -24.058 22.731 1.00113.84 N ANISOU 1503 N ILE A 200 13823 14072 15357 -196 224 -5 N ATOM 1504 CA ILE A 200 -8.253 -25.019 21.995 1.00112.80 C ANISOU 1504 CA ILE A 200 13706 13963 15191 -207 245 4 C ATOM 1505 C ILE A 200 -7.389 -25.702 20.935 1.00112.44 C ANISOU 1505 C ILE A 200 13645 13872 15204 -225 290 -14 C ATOM 1506 O ILE A 200 -7.358 -26.928 20.862 1.00114.04 O ANISOU 1506 O ILE A 200 13833 14070 15427 -235 287 -11 O ATOM 1507 CB ILE A 200 -9.528 -24.374 21.405 1.00112.05 C ANISOU 1507 CB ILE A 200 13652 13911 15011 -200 262 11 C ATOM 1508 CG1 ILE A 200 -10.584 -24.126 22.486 1.00111.32 C ANISOU 1508 CG1 ILE A 200 13571 13871 14856 -183 215 30 C ATOM 1509 CG2 ILE A 200 -10.087 -25.212 20.262 1.00112.20 C ANISOU 1509 CG2 ILE A 200 13686 13937 15008 -213 300 12 C ATOM 1510 CD1 ILE A 200 -11.806 -23.368 22.010 1.00110.93 C ANISOU 1510 CD1 ILE A 200 13559 13864 14727 -174 227 35 C ATOM 1511 N PHE A 201 -6.684 -24.898 20.130 1.00111.70 N ANISOU 1511 N PHE A 201 13555 13748 15139 -230 332 -33 N ATOM 1512 CA PHE A 201 -5.891 -25.419 19.027 1.00113.32 C ANISOU 1512 CA PHE A 201 13748 13913 15395 -248 381 -52 C ATOM 1513 C PHE A 201 -4.669 -26.169 19.552 1.00115.54 C ANISOU 1513 C PHE A 201 13984 14153 15763 -254 364 -64 C ATOM 1514 O PHE A 201 -4.230 -27.140 18.938 1.00116.89 O ANISOU 1514 O PHE A 201 14138 14300 15973 -268 388 -75 O ATOM 1515 CB PHE A 201 -5.508 -24.304 18.051 1.00112.17 C ANISOU 1515 CB PHE A 201 13621 13748 15251 -253 430 -67 C ATOM 1516 CG PHE A 201 -6.668 -23.705 17.297 1.00110.49 C ANISOU 1516 CG PHE A 201 13454 13570 14957 -250 453 -58 C ATOM 1517 CD1 PHE A 201 -7.409 -24.468 16.405 1.00110.58 C ANISOU 1517 CD1 PHE A 201 13485 13599 14931 -258 479 -54 C ATOM 1518 CD2 PHE A 201 -7.018 -22.375 17.473 1.00109.33 C ANISOU 1518 CD2 PHE A 201 13333 13438 14771 -237 446 -55 C ATOM 1519 CE1 PHE A 201 -8.477 -23.916 15.713 1.00109.42 C ANISOU 1519 CE1 PHE A 201 13382 13484 14711 -254 497 -47 C ATOM 1520 CE2 PHE A 201 -8.086 -21.823 16.781 1.00108.92 C ANISOU 1520 CE2 PHE A 201 13324 13417 14645 -233 464 -48 C ATOM 1521 CZ PHE A 201 -8.813 -22.595 15.902 1.00108.83 C ANISOU 1521 CZ PHE A 201 13330 13422 14597 -241 489 -44 C ATOM 1522 N ALA A 202 -4.130 -25.705 20.687 1.00116.90 N ANISOU 1522 N ALA A 202 14137 14316 15966 -243 322 -63 N ATOM 1523 CA ALA A 202 -2.979 -26.330 21.318 1.00119.33 C ANISOU 1523 CA ALA A 202 14402 14583 16356 -246 298 -74 C ATOM 1524 C ALA A 202 -3.363 -27.703 21.868 1.00122.80 C ANISOU 1524 C ALA A 202 14830 15036 16793 -248 262 -60 C ATOM 1525 O ALA A 202 -2.567 -28.639 21.809 1.00125.74 O ANISOU 1525 O ALA A 202 15173 15374 17230 -257 261 -72 O ATOM 1526 CB ALA A 202 -2.425 -25.430 22.396 1.00116.84 C ANISOU 1526 CB ALA A 202 14073 14257 16064 -233 260 -76 C ATOM 1527 N ALA A 203 -4.592 -27.808 22.390 1.00124.22 N ANISOU 1527 N ALA A 203 15034 15265 16899 -240 233 -35 N ATOM 1528 CA ALA A 203 -5.106 -29.048 22.950 1.00126.11 C ANISOU 1528 CA ALA A 203 15268 15522 17125 -242 197 -17 C ATOM 1529 C ALA A 203 -5.335 -30.071 21.840 1.00128.10 C ANISOU 1529 C ALA A 203 15524 15770 17379 -257 234 -21 C ATOM 1530 O ALA A 203 -5.122 -31.265 22.042 1.00130.69 O ANISOU 1530 O ALA A 203 15833 16085 17739 -265 216 -19 O ATOM 1531 CB ALA A 203 -6.375 -28.785 23.724 1.00125.17 C ANISOU 1531 CB ALA A 203 15174 15458 16925 -231 162 9 C ATOM 1532 N ALA A 204 -5.772 -29.586 20.673 1.00129.13 N ANISOU 1532 N ALA A 204 15680 15911 17474 -262 286 -28 N ATOM 1533 CA ALA A 204 -6.019 -30.437 19.522 1.00131.83 C ANISOU 1533 CA ALA A 204 16029 16249 17811 -275 325 -34 C ATOM 1534 C ALA A 204 -4.695 -30.861 18.891 1.00136.15 C ANISOU 1534 C ALA A 204 16545 16742 18444 -287 357 -61 C ATOM 1535 O ALA A 204 -4.618 -31.918 18.269 1.00136.86 O ANISOU 1535 O ALA A 204 16626 16819 18554 -298 373 -68 O ATOM 1536 CB ALA A 204 -6.901 -29.720 18.531 1.00130.92 C ANISOU 1536 CB ALA A 204 15953 16162 17629 -275 367 -32 C ATOM 1537 N ARG A 205 -3.662 -30.028 19.064 1.00142.14 N ANISOU 1537 N ARG A 205 17286 17468 19253 -284 363 -79 N ATOM 1538 CA ARG A 205 -2.348 -30.285 18.495 1.00147.75 C ANISOU 1538 CA ARG A 205 17964 18127 20047 -295 395 -108 C ATOM 1539 C ARG A 205 -1.681 -31.442 19.235 1.00148.24 C ANISOU 1539 C ARG A 205 17989 18164 20174 -296 354 -112 C ATOM 1540 O ARG A 205 -1.013 -32.266 18.614 1.00150.66 O ANISOU 1540 O ARG A 205 18273 18439 20534 -307 377 -132 O ATOM 1541 CB ARG A 205 -1.484 -29.019 18.527 1.00153.20 C ANISOU 1541 CB ARG A 205 18646 18792 20771 -293 411 -124 C ATOM 1542 CG ARG A 205 -0.138 -29.154 17.830 1.00157.98 C ANISOU 1542 CG ARG A 205 19219 19346 21460 -306 452 -157 C ATOM 1543 CD ARG A 205 0.759 -27.948 18.048 1.00163.32 C ANISOU 1543 CD ARG A 205 19883 19996 22175 -304 460 -172 C ATOM 1544 NE ARG A 205 1.037 -27.701 19.459 1.00168.94 N ANISOU 1544 NE ARG A 205 20577 20705 22909 -289 398 -163 N ATOM 1545 CZ ARG A 205 1.848 -26.755 19.927 1.00171.88 C ANISOU 1545 CZ ARG A 205 20932 21053 23321 -285 390 -174 C ATOM 1546 NH1 ARG A 205 2.484 -25.946 19.097 1.00172.80 N ANISOU 1546 NH1 ARG A 205 21049 21147 23462 -295 441 -194 N ATOM 1547 NH2 ARG A 205 2.022 -26.624 21.230 1.00172.55 N ANISOU 1547 NH2 ARG A 205 21003 21138 23421 -270 330 -165 N ATOM 1548 N ARG A 206 -1.876 -31.492 20.559 1.00148.24 N ANISOU 1548 N ARG A 206 17983 18177 20166 -285 293 -93 N ATOM 1549 CA ARG A 206 -1.254 -32.500 21.405 1.00150.04 C ANISOU 1549 CA ARG A 206 18178 18379 20452 -285 246 -94 C ATOM 1550 C ARG A 206 -1.861 -33.872 21.120 1.00146.17 C ANISOU 1550 C ARG A 206 17692 17901 19945 -293 240 -84 C ATOM 1551 O ARG A 206 -1.138 -34.861 21.025 1.00148.99 O ANISOU 1551 O ARG A 206 18021 18224 20366 -299 234 -98 O ATOM 1552 CB ARG A 206 -1.399 -32.134 22.886 1.00156.49 C ANISOU 1552 CB ARG A 206 18993 19210 21255 -271 183 -75 C ATOM 1553 CG ARG A 206 -0.963 -33.232 23.848 1.00163.99 C ANISOU 1553 CG ARG A 206 19916 20140 22251 -270 127 -70 C ATOM 1554 CD ARG A 206 -1.377 -32.956 25.281 1.00171.67 C ANISOU 1554 CD ARG A 206 20898 21138 23192 -257 64 -46 C ATOM 1555 NE ARG A 206 -0.554 -31.935 25.918 1.00178.94 N ANISOU 1555 NE ARG A 206 21803 22036 24149 -246 48 -58 N ATOM 1556 CZ ARG A 206 0.329 -32.159 26.888 1.00181.45 C ANISOU 1556 CZ ARG A 206 22093 22322 24527 -240 1 -64 C ATOM 1557 NH1 ARG A 206 1.023 -31.154 27.392 1.00181.57 N ANISOU 1557 NH1 ARG A 206 22097 22320 24573 -230 -10 -75 N ATOM 1558 NH2 ARG A 206 0.510 -33.382 27.357 1.00183.00 N ANISOU 1558 NH2 ARG A 206 22274 22503 24754 -244 -37 -58 N ATOM 1559 N GLN A 207 -3.192 -33.915 20.992 1.00141.21 N ANISOU 1559 N GLN A 207 17099 17321 19234 -292 240 -59 N ATOM 1560 CA GLN A 207 -3.922 -35.163 20.830 1.00138.04 C ANISOU 1560 CA GLN A 207 16705 16937 18808 -300 229 -45 C ATOM 1561 C GLN A 207 -3.675 -35.744 19.440 1.00139.03 C ANISOU 1561 C GLN A 207 16827 17041 18957 -312 283 -66 C ATOM 1562 O GLN A 207 -3.683 -36.961 19.269 1.00140.23 O ANISOU 1562 O GLN A 207 16969 17183 19129 -320 273 -66 O ATOM 1563 CB GLN A 207 -5.419 -34.942 21.052 1.00134.98 C ANISOU 1563 CB GLN A 207 16354 16607 18323 -296 216 -15 C ATOM 1564 CG GLN A 207 -5.779 -34.569 22.483 1.00133.27 C ANISOU 1564 CG GLN A 207 16141 16416 18078 -285 159 8 C ATOM 1565 CD GLN A 207 -7.249 -34.269 22.649 1.00132.01 C ANISOU 1565 CD GLN A 207 16016 16316 17824 -281 152 34 C ATOM 1566 OE1 GLN A 207 -7.980 -34.074 21.680 1.00130.28 O ANISOU 1566 OE1 GLN A 207 15822 16120 17560 -284 192 33 O ATOM 1567 NE2 GLN A 207 -7.695 -34.229 23.893 1.00133.12 N ANISOU 1567 NE2 GLN A 207 16160 16484 17936 -274 100 56 N ATOM 1568 N LEU A 208 -3.461 -34.861 18.457 1.00138.97 N ANISOU 1568 N LEU A 208 16831 17028 18944 -314 339 -84 N ATOM 1569 CA LEU A 208 -3.314 -35.261 17.067 1.00138.01 C ANISOU 1569 CA LEU A 208 16712 16892 18834 -326 396 -104 C ATOM 1570 C LEU A 208 -1.908 -35.827 16.841 1.00134.38 C ANISOU 1570 C LEU A 208 16210 16377 18471 -332 407 -135 C ATOM 1571 O LEU A 208 -1.803 -37.064 16.733 1.00133.10 O ANISOU 1571 O LEU A 208 16033 16202 18339 -338 395 -139 O ATOM 1572 CB LEU A 208 -3.570 -34.044 16.171 1.00142.47 C ANISOU 1572 CB LEU A 208 17306 17468 19357 -326 448 -110 C ATOM 1573 CG LEU A 208 -3.964 -34.351 14.726 1.00146.93 C ANISOU 1573 CG LEU A 208 17892 18038 19896 -337 505 -120 C ATOM 1574 CD1 LEU A 208 -5.352 -34.974 14.658 1.00145.48 C ANISOU 1574 CD1 LEU A 208 17738 17897 19639 -335 489 -95 C ATOM 1575 CD2 LEU A 208 -3.907 -33.092 13.873 1.00148.56 C ANISOU 1575 CD2 LEU A 208 18123 18245 20077 -339 557 -131 C ATOM 1576 N ALA A1001 0.353 -35.144 18.977 1.00161.38 N ANISOU 1576 N ALA A1001 19558 19729 22031 -318 331 -156 N ATOM 1577 CA ALA A1001 1.079 -36.295 18.390 1.00162.25 C ANISOU 1577 CA ALA A1001 19638 19802 22206 -327 345 -180 C ATOM 1578 C ALA A1001 0.766 -37.572 19.169 1.00163.73 C ANISOU 1578 C ALA A1001 19817 19992 22400 -325 287 -163 C ATOM 1579 O ALA A1001 1.388 -38.603 18.932 1.00167.14 O ANISOU 1579 O ALA A1001 20223 20392 22892 -330 284 -182 O ATOM 1580 CB ALA A1001 2.561 -36.005 18.362 1.00161.71 C ANISOU 1580 CB ALA A1001 19528 19684 22230 -328 359 -215 C ATOM 1581 N ASP A1002 -0.214 -37.493 20.080 1.00163.58 N ANISOU 1581 N ASP A1002 19823 20012 22318 -319 242 -129 N ATOM 1582 CA ASP A1002 -0.576 -38.597 20.956 1.00162.32 C ANISOU 1582 CA ASP A1002 19661 19858 22157 -318 182 -108 C ATOM 1583 C ASP A1002 -1.034 -39.799 20.132 1.00161.61 C ANISOU 1583 C ASP A1002 19575 19770 22058 -329 199 -108 C ATOM 1584 O ASP A1002 -0.524 -40.903 20.312 1.00163.42 O ANISOU 1584 O ASP A1002 19781 19970 22341 -332 172 -116 O ATOM 1585 CB ASP A1002 -1.620 -38.179 21.997 1.00163.32 C ANISOU 1585 CB ASP A1002 19815 20031 22209 -311 139 -71 C ATOM 1586 CG ASP A1002 -1.060 -37.331 23.128 1.00165.06 C ANISOU 1586 CG ASP A1002 20023 20242 22450 -299 102 -69 C ATOM 1587 OD1 ASP A1002 0.179 -37.286 23.273 1.00166.72 O ANISOU 1587 OD1 ASP A1002 20200 20406 22741 -297 97 -94 O ATOM 1588 OD2 ASP A1002 -1.869 -36.722 23.858 1.00164.61 O ANISOU 1588 OD2 ASP A1002 19990 20225 22330 -291 77 -43 O ATOM 1589 N LEU A1003 -1.991 -39.566 19.225 1.00160.30 N ANISOU 1589 N LEU A1003 19442 19639 21826 -333 241 -100 N ATOM 1590 CA LEU A1003 -2.535 -40.625 18.389 1.00161.87 C ANISOU 1590 CA LEU A1003 19651 19845 22009 -343 259 -99 C ATOM 1591 C LEU A1003 -1.491 -41.091 17.377 1.00165.40 C ANISOU 1591 C LEU A1003 20070 20246 22528 -349 301 -138 C ATOM 1592 O LEU A1003 -1.640 -42.158 16.786 1.00170.54 O ANISOU 1592 O LEU A1003 20718 20889 23188 -356 308 -143 O ATOM 1593 CB LEU A1003 -3.805 -40.130 17.687 1.00160.62 C ANISOU 1593 CB LEU A1003 19534 19734 21760 -344 294 -82 C ATOM 1594 CG LEU A1003 -5.083 -40.134 18.528 1.00160.20 C ANISOU 1594 CG LEU A1003 19509 19730 21629 -341 252 -44 C ATOM 1595 CD1 LEU A1003 -6.262 -39.622 17.716 1.00159.71 C ANISOU 1595 CD1 LEU A1003 19486 19712 21485 -342 290 -33 C ATOM 1596 CD2 LEU A1003 -5.382 -41.525 19.068 1.00159.57 C ANISOU 1596 CD2 LEU A1003 19422 19650 21558 -347 205 -27 C ATOM 1597 N GLU A1004 -0.435 -40.290 17.192 1.00168.37 N ANISOU 1597 N GLU A1004 20425 20593 22956 -347 328 -165 N ATOM 1598 CA GLU A1004 0.623 -40.638 16.257 1.00171.50 C ANISOU 1598 CA GLU A1004 20792 20946 23423 -353 371 -204 C ATOM 1599 C GLU A1004 1.798 -41.273 16.998 1.00173.10 C ANISOU 1599 C GLU A1004 20950 21103 23718 -350 330 -223 C ATOM 1600 O GLU A1004 2.530 -42.073 16.418 1.00174.17 O ANISOU 1600 O GLU A1004 21057 21204 23915 -355 345 -252 O ATOM 1601 CB GLU A1004 1.046 -39.423 15.428 1.00172.36 C ANISOU 1601 CB GLU A1004 20906 21051 23531 -356 435 -225 C ATOM 1602 CG GLU A1004 1.506 -39.785 14.026 1.00174.17 C ANISOU 1602 CG GLU A1004 21128 21260 23789 -367 498 -257 C ATOM 1603 CD GLU A1004 0.458 -40.465 13.160 1.00175.86 C ANISOU 1603 CD GLU A1004 21373 21501 23944 -372 520 -246 C ATOM 1604 OE1 GLU A1004 0.793 -41.481 12.519 1.00176.29 O ANISOU 1604 OE1 GLU A1004 21411 21534 24036 -378 534 -266 O ATOM 1605 OE2 GLU A1004 -0.690 -39.978 13.126 1.00177.14 O ANISOU 1605 OE2 GLU A1004 21576 21706 24024 -370 521 -218 O ATOM 1606 N ASP A1005 1.970 -40.915 18.276 1.00175.16 N ANISOU 1606 N ASP A1005 21202 21363 23988 -341 276 -208 N ATOM 1607 CA ASP A1005 3.055 -41.450 19.084 1.00177.51 C ANISOU 1607 CA ASP A1005 21459 21616 24370 -336 229 -224 C ATOM 1608 C ASP A1005 2.766 -42.903 19.446 1.00178.73 C ANISOU 1608 C ASP A1005 21610 21765 24536 -338 181 -212 C ATOM 1609 O ASP A1005 3.684 -43.718 19.491 1.00183.46 O ANISOU 1609 O ASP A1005 22174 22320 25212 -338 164 -237 O ATOM 1610 CB ASP A1005 3.343 -40.584 20.314 1.00179.97 C ANISOU 1610 CB ASP A1005 21766 21928 24688 -326 186 -212 C ATOM 1611 CG ASP A1005 4.319 -39.451 20.041 1.00184.02 C ANISOU 1611 CG ASP A1005 22258 22416 25244 -324 224 -240 C ATOM 1612 OD1 ASP A1005 5.311 -39.690 19.320 1.00185.32 O ANISOU 1612 OD1 ASP A1005 22392 22543 25480 -329 259 -277 O ATOM 1613 OD2 ASP A1005 4.081 -38.339 20.551 1.00188.21 O ANISOU 1613 OD2 ASP A1005 22805 22967 25739 -317 218 -225 O ATOM 1614 N ASN A1006 1.486 -43.213 19.689 1.00176.83 N ANISOU 1614 N ASN A1006 21406 21567 24216 -341 161 -175 N ATOM 1615 CA ASN A1006 1.066 -44.554 20.063 1.00176.83 C ANISOU 1615 CA ASN A1006 21406 21565 24214 -345 114 -158 C ATOM 1616 C ASN A1006 1.119 -45.480 18.851 1.00177.11 C ANISOU 1616 C ASN A1006 21436 21587 24272 -353 152 -180 C ATOM 1617 O ASN A1006 1.440 -46.660 18.989 1.00179.54 O ANISOU 1617 O ASN A1006 21726 21867 24625 -355 119 -187 O ATOM 1618 CB ASN A1006 -0.311 -44.561 20.733 1.00176.68 C ANISOU 1618 CB ASN A1006 21427 21598 24106 -346 81 -112 C ATOM 1619 CG ASN A1006 -0.258 -44.189 22.199 1.00178.42 C ANISOU 1619 CG ASN A1006 21647 21824 24322 -338 20 -90 C ATOM 1620 OD1 ASN A1006 0.746 -44.419 22.871 1.00178.88 O ANISOU 1620 OD1 ASN A1006 21676 21842 24450 -333 -17 -104 O ATOM 1621 ND2 ASN A1006 -1.338 -43.619 22.708 1.00178.38 N ANISOU 1621 ND2 ASN A1006 21675 21868 24235 -337 9 -57 N ATOM 1622 N TRP A1007 0.795 -44.933 17.672 1.00175.21 N ANISOU 1622 N TRP A1007 21212 21364 23996 -357 219 -191 N ATOM 1623 CA TRP A1007 0.863 -45.680 16.426 1.00174.90 C ANISOU 1623 CA TRP A1007 21169 21312 23973 -364 263 -214 C ATOM 1624 C TRP A1007 2.308 -46.084 16.146 1.00176.41 C ANISOU 1624 C TRP A1007 21313 21448 24267 -363 272 -259 C ATOM 1625 O TRP A1007 2.567 -47.215 15.741 1.00177.93 O ANISOU 1625 O TRP A1007 21490 21617 24500 -366 267 -275 O ATOM 1626 CB TRP A1007 0.261 -44.873 15.267 1.00175.15 C ANISOU 1626 CB TRP A1007 21231 21374 23944 -369 333 -217 C ATOM 1627 CG TRP A1007 0.435 -45.518 13.926 1.00177.49 C ANISOU 1627 CG TRP A1007 21523 21656 24260 -376 383 -245 C ATOM 1628 CD1 TRP A1007 1.473 -45.340 13.057 1.00179.12 C ANISOU 1628 CD1 TRP A1007 21703 21829 24524 -378 435 -287 C ATOM 1629 CD2 TRP A1007 -0.456 -46.456 13.295 1.00177.18 C ANISOU 1629 CD2 TRP A1007 21506 21635 24181 -381 388 -235 C ATOM 1630 NE1 TRP A1007 1.289 -46.097 11.931 1.00177.91 N ANISOU 1630 NE1 TRP A1007 21555 21673 24369 -385 471 -303 N ATOM 1631 CE2 TRP A1007 0.115 -46.793 12.048 1.00176.85 C ANISOU 1631 CE2 TRP A1007 21450 21569 24175 -386 442 -272 C ATOM 1632 CE3 TRP A1007 -1.677 -47.040 13.657 1.00177.28 C ANISOU 1632 CE3 TRP A1007 21547 21682 24131 -383 352 -198 C ATOM 1633 CZ2 TRP A1007 -0.494 -47.686 11.167 1.00175.93 C ANISOU 1633 CZ2 TRP A1007 21350 21461 24035 -391 460 -274 C ATOM 1634 CZ3 TRP A1007 -2.278 -47.923 12.786 1.00176.33 C ANISOU 1634 CZ3 TRP A1007 21440 21569 23988 -389 369 -200 C ATOM 1635 CH2 TRP A1007 -1.693 -48.239 11.559 1.00175.87 C ANISOU 1635 CH2 TRP A1007 21370 21486 23968 -392 421 -237 C ATOM 1636 N GLU A1008 3.236 -45.146 16.370 1.00177.66 N ANISOU 1636 N GLU A1008 21449 21586 24468 -359 286 -279 N ATOM 1637 CA GLU A1008 4.656 -45.381 16.161 1.00178.89 C ANISOU 1637 CA GLU A1008 21557 21689 24723 -357 296 -323 C ATOM 1638 C GLU A1008 5.188 -46.323 17.238 1.00178.54 C ANISOU 1638 C GLU A1008 21485 21612 24739 -351 221 -322 C ATOM 1639 O GLU A1008 6.071 -47.130 16.965 1.00180.59 O ANISOU 1639 O GLU A1008 21709 21831 25076 -350 217 -356 O ATOM 1640 CB GLU A1008 5.432 -44.062 16.143 1.00182.30 C ANISOU 1640 CB GLU A1008 21976 22111 25180 -355 330 -341 C ATOM 1641 CG GLU A1008 5.219 -43.251 14.877 1.00186.58 C ANISOU 1641 CG GLU A1008 22537 22671 25683 -364 411 -353 C ATOM 1642 CD GLU A1008 6.078 -42.003 14.747 1.00190.56 C ANISOU 1642 CD GLU A1008 23025 23160 26218 -365 449 -375 C ATOM 1643 OE1 GLU A1008 7.135 -41.936 15.409 1.00193.52 O ANISOU 1643 OE1 GLU A1008 23361 23499 26669 -359 422 -394 O ATOM 1644 OE2 GLU A1008 5.687 -41.100 13.981 1.00192.40 O ANISOU 1644 OE2 GLU A1008 23285 23416 26401 -371 504 -372 O ATOM 1645 N THR A1009 4.635 -46.214 18.453 1.00178.07 N ANISOU 1645 N THR A1009 21443 21573 24644 -346 161 -285 N ATOM 1646 CA THR A1009 5.030 -47.069 19.563 1.00178.95 C ANISOU 1646 CA THR A1009 21535 21656 24803 -340 84 -279 C ATOM 1647 C THR A1009 4.615 -48.512 19.279 1.00179.30 C ANISOU 1647 C THR A1009 21583 21694 24848 -346 62 -274 C ATOM 1648 O THR A1009 5.262 -49.446 19.747 1.00182.65 O ANISOU 1648 O THR A1009 21981 22080 25338 -343 14 -286 O ATOM 1649 CB THR A1009 4.484 -46.552 20.902 1.00178.79 C ANISOU 1649 CB THR A1009 21537 21661 24735 -335 29 -238 C ATOM 1650 OG1 THR A1009 4.845 -45.177 21.033 1.00180.51 O ANISOU 1650 OG1 THR A1009 21752 21884 24950 -330 55 -245 O ATOM 1651 CG2 THR A1009 5.012 -47.314 22.099 1.00178.19 C ANISOU 1651 CG2 THR A1009 21441 21552 24712 -329 -51 -233 C ATOM 1652 N LEU A1010 3.543 -48.682 18.496 1.00176.74 N ANISOU 1652 N LEU A1010 21293 21408 24454 -354 97 -257 N ATOM 1653 CA LEU A1010 3.009 -50.005 18.213 1.00174.85 C ANISOU 1653 CA LEU A1010 21062 21168 24206 -360 76 -249 C ATOM 1654 C LEU A1010 3.833 -50.688 17.122 1.00175.15 C ANISOU 1654 C LEU A1010 21069 21168 24313 -361 113 -295 C ATOM 1655 O LEU A1010 4.168 -51.863 17.250 1.00176.76 O ANISOU 1655 O LEU A1010 21254 21341 24567 -361 75 -305 O ATOM 1656 CB LEU A1010 1.533 -49.888 17.818 1.00173.13 C ANISOU 1656 CB LEU A1010 20890 21005 23886 -368 97 -213 C ATOM 1657 CG LEU A1010 0.706 -51.164 17.974 1.00173.64 C ANISOU 1657 CG LEU A1010 20972 21079 23924 -375 56 -188 C ATOM 1658 CD1 LEU A1010 0.586 -51.564 19.439 1.00173.16 C ANISOU 1658 CD1 LEU A1010 20913 21015 23865 -374 -24 -157 C ATOM 1659 CD2 LEU A1010 -0.673 -50.992 17.355 1.00174.85 C ANISOU 1659 CD2 LEU A1010 21167 21285 23984 -382 89 -162 C ATOM 1660 N ASN A1011 4.159 -49.942 16.058 1.00174.74 N ANISOU 1660 N ASN A1011 21012 21118 24263 -363 187 -323 N ATOM 1661 CA ASN A1011 4.850 -50.495 14.903 1.00174.53 C ANISOU 1661 CA ASN A1011 20960 21062 24292 -365 233 -367 C ATOM 1662 C ASN A1011 6.322 -50.743 15.228 1.00174.82 C ANISOU 1662 C ASN A1011 20943 21044 24436 -358 213 -408 C ATOM 1663 O ASN A1011 6.857 -51.801 14.900 1.00174.29 O ANISOU 1663 O ASN A1011 20850 20943 24429 -356 202 -436 O ATOM 1664 CB ASN A1011 4.693 -49.617 13.658 1.00174.63 C ANISOU 1664 CB ASN A1011 20988 21097 24268 -371 319 -383 C ATOM 1665 CG ASN A1011 3.302 -49.657 13.061 1.00174.51 C ANISOU 1665 CG ASN A1011 21020 21128 24157 -377 342 -352 C ATOM 1666 OD1 ASN A1011 2.561 -50.620 13.253 1.00174.48 O ANISOU 1666 OD1 ASN A1011 21032 21134 24127 -379 304 -330 O ATOM 1667 ND2 ASN A1011 2.939 -48.619 12.326 1.00173.53 N ANISOU 1667 ND2 ASN A1011 20921 21032 23981 -381 402 -351 N ATOM 1668 N ASP A1012 6.959 -49.762 15.880 1.00176.18 N ANISOU 1668 N ASP A1012 21100 21206 24632 -353 208 -412 N ATOM 1669 CA ASP A1012 8.395 -49.778 16.114 1.00178.25 C ANISOU 1669 CA ASP A1012 21312 21419 24998 -346 198 -454 C ATOM 1670 C ASP A1012 8.766 -50.859 17.127 1.00177.52 C ANISOU 1670 C ASP A1012 21198 21292 24960 -339 115 -452 C ATOM 1671 O ASP A1012 9.920 -51.278 17.183 1.00180.77 O ANISOU 1671 O ASP A1012 21564 21656 25463 -333 101 -491 O ATOM 1672 CB ASP A1012 8.919 -48.398 16.525 1.00180.53 C ANISOU 1672 CB ASP A1012 21591 21708 25294 -343 215 -458 C ATOM 1673 CG ASP A1012 8.774 -47.337 15.446 1.00181.99 C ANISOU 1673 CG ASP A1012 21791 21917 25440 -352 300 -468 C ATOM 1674 OD1 ASP A1012 8.317 -47.680 14.335 1.00180.82 O ANISOU 1674 OD1 ASP A1012 21659 21784 25260 -359 349 -475 O ATOM 1675 OD2 ASP A1012 9.116 -46.171 15.726 1.00184.17 O ANISOU 1675 OD2 ASP A1012 22065 22197 25716 -350 316 -468 O ATOM 1676 N ASN A1013 7.784 -51.302 17.921 1.00173.95 N ANISOU 1676 N ASN A1013 20779 20864 24450 -340 59 -405 N ATOM 1677 CA ASN A1013 8.013 -52.349 18.903 1.00172.51 C ANISOU 1677 CA ASN A1013 20584 20651 24309 -335 -24 -397 C ATOM 1678 C ASN A1013 7.670 -53.716 18.312 1.00174.12 C ANISOU 1678 C ASN A1013 20791 20846 24519 -339 -33 -402 C ATOM 1679 O ASN A1013 8.097 -54.737 18.844 1.00173.64 O ANISOU 1679 O ASN A1013 20712 20749 24513 -335 -93 -408 O ATOM 1680 CB ASN A1013 7.278 -52.082 20.219 1.00169.11 C ANISOU 1680 CB ASN A1013 20185 20246 23822 -334 -85 -346 C ATOM 1681 CG ASN A1013 7.871 -50.943 21.021 1.00169.27 C ANISOU 1681 CG ASN A1013 20194 20261 23861 -326 -96 -347 C ATOM 1682 OD1 ASN A1013 9.065 -50.664 20.932 1.00170.65 O ANISOU 1682 OD1 ASN A1013 20327 20396 24114 -319 -85 -387 O ATOM 1683 ND2 ASN A1013 7.044 -50.283 21.815 1.00169.74 N ANISOU 1683 ND2 ASN A1013 20288 20359 23847 -327 -117 -304 N ATOM 1684 N LEU A1014 6.907 -53.726 17.212 1.00177.05 N ANISOU 1684 N LEU A1014 21187 21250 24836 -347 25 -399 N ATOM 1685 CA LEU A1014 6.527 -54.972 16.563 1.00178.64 C ANISOU 1685 CA LEU A1014 21393 21444 25037 -352 21 -404 C ATOM 1686 C LEU A1014 7.706 -55.544 15.779 1.00180.59 C ANISOU 1686 C LEU A1014 21593 21644 25378 -346 45 -462 C ATOM 1687 O LEU A1014 7.971 -56.742 15.852 1.00182.84 O ANISOU 1687 O LEU A1014 21862 21897 25711 -343 3 -475 O ATOM 1688 CB LEU A1014 5.317 -54.748 15.648 1.00179.69 C ANISOU 1688 CB LEU A1014 21567 21627 25078 -361 74 -382 C ATOM 1689 CG LEU A1014 3.983 -55.291 16.161 1.00180.60 C ANISOU 1689 CG LEU A1014 21725 21777 25117 -368 31 -330 C ATOM 1690 CD1 LEU A1014 2.884 -55.080 15.132 1.00180.82 C ANISOU 1690 CD1 LEU A1014 21790 21851 25064 -376 88 -316 C ATOM 1691 CD2 LEU A1014 4.087 -56.766 16.521 1.00181.02 C ANISOU 1691 CD2 LEU A1014 21767 21798 25213 -369 -33 -330 C ATOM 1692 N LYS A1015 8.411 -54.673 15.046 1.00181.88 N ANISOU 1692 N LYS A1015 21735 21802 25568 -345 112 -498 N ATOM 1693 CA LYS A1015 9.436 -55.096 14.104 1.00182.60 C ANISOU 1693 CA LYS A1015 21785 21857 25738 -343 152 -556 C ATOM 1694 C LYS A1015 10.729 -55.474 14.827 1.00183.19 C ANISOU 1694 C LYS A1015 21809 21878 25919 -332 102 -589 C ATOM 1695 O LYS A1015 11.624 -56.056 14.217 1.00184.40 O ANISOU 1695 O LYS A1015 21922 21994 26147 -327 118 -639 O ATOM 1696 CB LYS A1015 9.662 -54.028 13.029 1.00181.75 C ANISOU 1696 CB LYS A1015 21676 21767 25614 -348 244 -580 C ATOM 1697 CG LYS A1015 8.540 -53.893 12.007 1.00184.00 C ANISOU 1697 CG LYS A1015 22005 22096 25810 -358 300 -561 C ATOM 1698 CD LYS A1015 8.757 -52.778 11.006 1.00184.80 C ANISOU 1698 CD LYS A1015 22109 22214 25892 -365 388 -582 C ATOM 1699 CE LYS A1015 7.581 -52.591 10.071 1.00183.81 C ANISOU 1699 CE LYS A1015 22032 22133 25673 -373 437 -560 C ATOM 1700 NZ LYS A1015 7.756 -51.408 9.195 1.00183.02 N ANISOU 1700 NZ LYS A1015 21940 22049 25548 -381 518 -575 N ATOM 1701 N VAL A1016 10.821 -55.151 16.124 1.00182.32 N ANISOU 1701 N VAL A1016 21700 21761 25813 -327 41 -563 N ATOM 1702 CA VAL A1016 12.005 -55.491 16.901 1.00181.63 C ANISOU 1702 CA VAL A1016 21568 21621 25823 -315 -14 -592 C ATOM 1703 C VAL A1016 11.789 -56.815 17.633 1.00184.83 C ANISOU 1703 C VAL A1016 21977 22003 26246 -311 -99 -575 C ATOM 1704 O VAL A1016 12.708 -57.325 18.271 1.00188.61 O ANISOU 1704 O VAL A1016 22422 22435 26808 -301 -154 -598 O ATOM 1705 CB VAL A1016 12.450 -54.359 17.853 1.00178.46 C ANISOU 1705 CB VAL A1016 21158 21218 25430 -310 -30 -583 C ATOM 1706 CG1 VAL A1016 12.693 -53.048 17.120 1.00177.18 C ANISOU 1706 CG1 VAL A1016 20992 21076 25252 -316 53 -600 C ATOM 1707 CG2 VAL A1016 11.498 -54.165 19.023 1.00174.40 C ANISOU 1707 CG2 VAL A1016 20687 20733 24843 -312 -89 -522 C ATOM 1708 N ILE A1017 10.571 -57.365 17.539 1.00186.56 N ANISOU 1708 N ILE A1017 22241 22256 26390 -320 -111 -535 N ATOM 1709 CA ILE A1017 10.289 -58.690 18.072 1.00189.27 C ANISOU 1709 CA ILE A1017 22591 22578 26745 -319 -185 -518 C ATOM 1710 C ILE A1017 10.698 -59.732 17.032 1.00193.98 C ANISOU 1710 C ILE A1017 23162 23146 27395 -317 -165 -562 C ATOM 1711 O ILE A1017 11.142 -60.822 17.387 1.00200.12 O ANISOU 1711 O ILE A1017 23920 23883 28234 -310 -225 -576 O ATOM 1712 CB ILE A1017 8.810 -58.840 18.493 1.00186.12 C ANISOU 1712 CB ILE A1017 22248 22226 26243 -330 -210 -455 C ATOM 1713 CG1 ILE A1017 8.410 -57.808 19.551 1.00186.67 C ANISOU 1713 CG1 ILE A1017 22342 22325 26259 -332 -231 -414 C ATOM 1714 CG2 ILE A1017 8.522 -60.258 18.970 1.00184.17 C ANISOU 1714 CG2 ILE A1017 22010 21957 26011 -332 -285 -438 C ATOM 1715 CD1 ILE A1017 6.917 -57.665 19.747 1.00188.10 C ANISOU 1715 CD1 ILE A1017 22577 22563 26331 -344 -233 -357 C ATOM 1716 N GLU A1018 10.551 -59.374 15.750 1.00192.94 N ANISOU 1716 N GLU A1018 23032 23037 27241 -321 -81 -584 N ATOM 1717 CA GLU A1018 10.817 -60.279 14.642 1.00192.93 C ANISOU 1717 CA GLU A1018 23011 23016 27278 -320 -52 -624 C ATOM 1718 C GLU A1018 12.302 -60.631 14.602 1.00194.90 C ANISOU 1718 C GLU A1018 23200 23209 27645 -307 -63 -685 C ATOM 1719 O GLU A1018 12.660 -61.801 14.471 1.00195.48 O ANISOU 1719 O GLU A1018 23252 23246 27774 -301 -99 -710 O ATOM 1720 CB GLU A1018 10.383 -59.650 13.316 1.00190.93 C ANISOU 1720 CB GLU A1018 22774 22801 26972 -328 44 -635 C ATOM 1721 CG GLU A1018 8.901 -59.325 13.245 1.00190.48 C ANISOU 1721 CG GLU A1018 22774 22799 26800 -339 57 -579 C ATOM 1722 CD GLU A1018 8.456 -58.685 11.941 1.00191.16 C ANISOU 1722 CD GLU A1018 22880 22921 26831 -347 149 -589 C ATOM 1723 OE1 GLU A1018 8.880 -59.167 10.870 1.00192.28 O ANISOU 1723 OE1 GLU A1018 23002 23047 27009 -345 191 -631 O ATOM 1724 OE2 GLU A1018 7.691 -57.702 11.999 1.00190.78 O ANISOU 1724 OE2 GLU A1018 22866 22916 26704 -353 177 -554 O ATOM 1725 N LYS A1019 13.151 -59.604 14.725 1.00195.28 N ANISOU 1725 N LYS A1019 23220 23248 27730 -304 -32 -709 N ATOM 1726 CA LYS A1019 14.593 -59.752 14.613 1.00196.58 C ANISOU 1726 CA LYS A1019 23323 23362 28005 -293 -31 -770 C ATOM 1727 C LYS A1019 15.225 -59.776 16.004 1.00198.89 C ANISOU 1727 C LYS A1019 23597 23619 28353 -283 -114 -764 C ATOM 1728 O LYS A1019 16.392 -59.419 16.162 1.00198.80 O ANISOU 1728 O LYS A1019 23540 23575 28423 -274 -111 -806 O ATOM 1729 CB LYS A1019 15.175 -58.610 13.772 1.00195.16 C ANISOU 1729 CB LYS A1019 23123 23195 27836 -297 60 -805 C ATOM 1730 CG LYS A1019 14.772 -58.600 12.303 1.00195.53 C ANISOU 1730 CG LYS A1019 23182 23269 27843 -306 146 -822 C ATOM 1731 CD LYS A1019 15.237 -57.365 11.554 1.00196.93 C ANISOU 1731 CD LYS A1019 23346 23461 28016 -314 235 -847 C ATOM 1732 CE LYS A1019 16.732 -57.327 11.316 1.00200.02 C ANISOU 1732 CE LYS A1019 23673 23808 28517 -307 255 -913 C ATOM 1733 NZ LYS A1019 17.158 -56.049 10.698 1.00202.72 N ANISOU 1733 NZ LYS A1019 24005 24166 28853 -316 339 -932 N ATOM 1734 N ALA A1020 14.448 -60.215 17.004 1.00202.70 N ANISOU 1734 N ALA A1020 24116 24110 28791 -284 -188 -712 N ATOM 1735 CA ALA A1020 14.889 -60.231 18.391 1.00205.66 C ANISOU 1735 CA ALA A1020 24482 24456 29203 -276 -270 -698 C ATOM 1736 C ALA A1020 15.944 -61.315 18.607 1.00209.37 C ANISOU 1736 C ALA A1020 24906 24862 29782 -262 -327 -743 C ATOM 1737 O ALA A1020 16.168 -62.154 17.735 1.00212.50 O ANISOU 1737 O ALA A1020 25284 25242 30216 -260 -309 -778 O ATOM 1738 CB ALA A1020 13.707 -60.402 19.315 1.00202.03 C ANISOU 1738 CB ALA A1020 24077 24026 28659 -283 -327 -629 C ATOM 1739 N ASP A1021 16.584 -61.280 19.783 1.00209.44 N ANISOU 1739 N ASP A1021 24899 24837 29841 -252 -399 -741 N ATOM 1740 CA ASP A1021 17.706 -62.153 20.090 1.00206.96 C ANISOU 1740 CA ASP A1021 24538 24459 29638 -237 -456 -787 C ATOM 1741 C ASP A1021 17.324 -63.153 21.179 1.00204.43 C ANISOU 1741 C ASP A1021 24244 24117 29313 -235 -561 -750 C ATOM 1742 O ASP A1021 17.731 -64.312 21.122 1.00204.70 O ANISOU 1742 O ASP A1021 24258 24108 29409 -227 -607 -775 O ATOM 1743 CB ASP A1021 18.951 -61.349 20.476 1.00208.65 C ANISOU 1743 CB ASP A1021 24705 24643 29931 -226 -454 -826 C ATOM 1744 CG ASP A1021 19.666 -60.708 19.297 1.00210.01 C ANISOU 1744 CG ASP A1021 24836 24818 30142 -227 -358 -882 C ATOM 1745 OD1 ASP A1021 19.300 -61.018 18.144 1.00210.44 O ANISOU 1745 OD1 ASP A1021 24894 24891 30171 -234 -298 -895 O ATOM 1746 OD2 ASP A1021 20.589 -59.906 19.541 1.00211.02 O ANISOU 1746 OD2 ASP A1021 24927 24927 30323 -221 -345 -910 O ATOM 1747 N ASN A1022 16.546 -62.694 22.167 1.00202.13 N ANISOU 1747 N ASN A1022 23997 23854 28949 -242 -597 -690 N ATOM 1748 CA ASN A1022 16.242 -63.501 23.338 1.00200.72 C ANISOU 1748 CA ASN A1022 23844 23655 28765 -242 -698 -652 C ATOM 1749 C ASN A1022 14.857 -63.150 23.878 1.00199.80 C ANISOU 1749 C ASN A1022 23791 23594 28530 -258 -705 -579 C ATOM 1750 O ASN A1022 14.150 -62.322 23.306 1.00201.98 O ANISOU 1750 O ASN A1022 24089 23923 28732 -268 -634 -561 O ATOM 1751 CB ASN A1022 17.331 -63.369 24.408 1.00199.64 C ANISOU 1751 CB ASN A1022 23677 23468 28708 -227 -765 -671 C ATOM 1752 CG ASN A1022 17.544 -61.945 24.880 1.00198.40 C ANISOU 1752 CG ASN A1022 23518 23333 28533 -225 -738 -663 C ATOM 1753 OD1 ASN A1022 17.305 -60.991 24.141 1.00195.65 O ANISOU 1753 OD1 ASN A1022 23171 23024 28144 -232 -654 -666 O ATOM 1754 ND2 ASN A1022 18.002 -61.791 26.111 1.00198.27 N ANISOU 1754 ND2 ASN A1022 23500 23288 28545 -217 -811 -652 N ATOM 1755 N ALA A1023 14.494 -63.793 24.995 1.00196.75 N ANISOU 1755 N ALA A1023 23434 23195 28128 -261 -794 -538 N ATOM 1756 CA ALA A1023 13.200 -63.617 25.634 1.00193.94 C ANISOU 1756 CA ALA A1023 23137 22888 27665 -277 -812 -469 C ATOM 1757 C ALA A1023 13.112 -62.247 26.304 1.00194.28 C ANISOU 1757 C ALA A1023 23192 22962 27665 -276 -796 -446 C ATOM 1758 O ALA A1023 12.017 -61.729 26.508 1.00196.97 O ANISOU 1758 O ALA A1023 23575 23357 27908 -289 -778 -397 O ATOM 1759 CB ALA A1023 12.961 -64.734 26.621 1.00191.18 C ANISOU 1759 CB ALA A1023 22811 22511 27319 -280 -912 -437 C ATOM 1760 N ALA A1024 14.273 -61.669 26.639 1.00192.37 N ANISOU 1760 N ALA A1024 22909 22684 27497 -261 -804 -484 N ATOM 1761 CA ALA A1024 14.333 -60.382 27.316 1.00187.68 C ANISOU 1761 CA ALA A1024 22321 22113 26874 -258 -794 -467 C ATOM 1762 C ALA A1024 13.975 -59.253 26.351 1.00185.84 C ANISOU 1762 C ALA A1024 22090 21929 26592 -264 -693 -473 C ATOM 1763 O ALA A1024 13.377 -58.259 26.760 1.00184.54 O ANISOU 1763 O ALA A1024 21953 21806 26356 -268 -675 -438 O ATOM 1764 CB ALA A1024 15.695 -60.179 27.933 1.00187.98 C ANISOU 1764 CB ALA A1024 22316 22096 27012 -240 -836 -507 C ATOM 1765 N GLN A1025 14.341 -59.422 25.074 1.00184.91 N ANISOU 1765 N GLN A1025 21942 21804 26510 -263 -628 -517 N ATOM 1766 CA GLN A1025 14.090 -58.417 24.051 1.00184.55 C ANISOU 1766 CA GLN A1025 21897 21800 26425 -269 -530 -527 C ATOM 1767 C GLN A1025 12.601 -58.352 23.721 1.00184.99 C ANISOU 1767 C GLN A1025 22006 21916 26365 -284 -500 -477 C ATOM 1768 O GLN A1025 12.055 -57.267 23.534 1.00183.54 O ANISOU 1768 O GLN A1025 21843 21778 26116 -290 -448 -457 O ATOM 1769 CB GLN A1025 14.910 -58.693 22.789 1.00183.20 C ANISOU 1769 CB GLN A1025 21680 21603 26326 -264 -471 -589 C ATOM 1770 CG GLN A1025 16.168 -57.843 22.684 1.00182.64 C ANISOU 1770 CG GLN A1025 21559 21504 26332 -254 -441 -639 C ATOM 1771 CD GLN A1025 16.424 -57.363 21.276 1.00181.96 C ANISOU 1771 CD GLN A1025 21451 21432 26255 -259 -341 -678 C ATOM 1772 OE1 GLN A1025 15.749 -57.758 20.327 1.00179.92 O ANISOU 1772 OE1 GLN A1025 21211 21199 25951 -268 -296 -674 O ATOM 1773 NE2 GLN A1025 17.410 -56.494 21.129 1.00182.52 N ANISOU 1773 NE2 GLN A1025 21483 21486 26381 -253 -304 -717 N ATOM 1774 N VAL A1026 11.960 -59.526 23.651 1.00188.40 N ANISOU 1774 N VAL A1026 22459 22347 26776 -291 -534 -457 N ATOM 1775 CA VAL A1026 10.551 -59.633 23.306 1.00189.97 C ANISOU 1775 CA VAL A1026 22707 22600 26873 -307 -510 -412 C ATOM 1776 C VAL A1026 9.714 -59.014 24.427 1.00189.57 C ANISOU 1776 C VAL A1026 22698 22588 26742 -313 -544 -354 C ATOM 1777 O VAL A1026 8.648 -58.459 24.169 1.00192.76 O ANISOU 1777 O VAL A1026 23138 23047 27056 -323 -504 -321 O ATOM 1778 CB VAL A1026 10.144 -61.093 23.012 1.00191.23 C ANISOU 1778 CB VAL A1026 22876 22744 27038 -313 -544 -407 C ATOM 1779 CG1 VAL A1026 8.667 -61.224 22.671 1.00191.65 C ANISOU 1779 CG1 VAL A1026 22978 22853 26986 -329 -521 -360 C ATOM 1780 CG2 VAL A1026 10.991 -61.707 21.906 1.00190.83 C ANISOU 1780 CG2 VAL A1026 22783 22656 27068 -305 -510 -467 C ATOM 1781 N LYS A1027 10.222 -59.100 25.663 1.00186.19 N ANISOU 1781 N LYS A1027 22264 22129 26349 -306 -619 -345 N ATOM 1782 CA LYS A1027 9.529 -58.578 26.830 1.00184.72 C ANISOU 1782 CA LYS A1027 22116 21974 26093 -311 -659 -293 C ATOM 1783 C LYS A1027 9.424 -57.057 26.741 1.00185.24 C ANISOU 1783 C LYS A1027 22186 22079 26118 -308 -601 -290 C ATOM 1784 O LYS A1027 8.339 -56.508 26.912 1.00183.38 O ANISOU 1784 O LYS A1027 21990 21898 25790 -317 -583 -249 O ATOM 1785 CB LYS A1027 10.229 -59.016 28.120 1.00184.59 C ANISOU 1785 CB LYS A1027 22092 21913 26133 -303 -752 -290 C ATOM 1786 CG LYS A1027 9.592 -58.513 29.410 1.00184.02 C ANISOU 1786 CG LYS A1027 22057 21869 25992 -307 -798 -237 C ATOM 1787 CD LYS A1027 10.354 -58.911 30.658 1.00183.42 C ANISOU 1787 CD LYS A1027 21973 21744 25974 -298 -889 -237 C ATOM 1788 CE LYS A1027 10.355 -60.404 30.906 1.00183.23 C ANISOU 1788 CE LYS A1027 21955 21683 25980 -304 -957 -230 C ATOM 1789 NZ LYS A1027 11.191 -60.768 32.074 1.00185.26 N ANISOU 1789 NZ LYS A1027 22202 21887 26299 -293 -1046 -234 N ATOM 1790 N ASP A1028 10.554 -56.396 26.462 1.00187.36 N ANISOU 1790 N ASP A1028 22413 22318 26458 -296 -572 -336 N ATOM 1791 CA ASP A1028 10.632 -54.942 26.458 1.00187.55 C ANISOU 1791 CA ASP A1028 22435 22369 26455 -292 -524 -338 C ATOM 1792 C ASP A1028 9.741 -54.362 25.361 1.00186.88 C ANISOU 1792 C ASP A1028 22373 22337 26295 -302 -439 -329 C ATOM 1793 O ASP A1028 9.076 -53.351 25.577 1.00188.02 O ANISOU 1793 O ASP A1028 22545 22527 26369 -305 -416 -300 O ATOM 1794 CB ASP A1028 12.078 -54.450 26.349 1.00188.22 C ANISOU 1794 CB ASP A1028 22468 22407 26639 -278 -512 -391 C ATOM 1795 CG ASP A1028 12.883 -54.633 27.626 1.00189.75 C ANISOU 1795 CG ASP A1028 22645 22557 26894 -266 -596 -394 C ATOM 1796 OD1 ASP A1028 12.266 -54.675 28.710 1.00191.13 O ANISOU 1796 OD1 ASP A1028 22854 22748 27017 -269 -654 -349 O ATOM 1797 OD2 ASP A1028 14.121 -54.732 27.526 1.00190.73 O ANISOU 1797 OD2 ASP A1028 22721 22630 27116 -255 -603 -443 O ATOM 1798 N ALA A1029 9.734 -55.017 24.195 1.00186.74 N ANISOU 1798 N ALA A1029 22344 22314 26295 -307 -397 -354 N ATOM 1799 CA ALA A1029 8.983 -54.548 23.042 1.00186.52 C ANISOU 1799 CA ALA A1029 22336 22330 26204 -316 -315 -351 C ATOM 1800 C ALA A1029 7.482 -54.718 23.271 1.00185.73 C ANISOU 1800 C ALA A1029 22289 22283 25999 -328 -326 -295 C ATOM 1801 O ALA A1029 6.694 -53.876 22.844 1.00185.64 O ANISOU 1801 O ALA A1029 22303 22319 25912 -333 -275 -277 O ATOM 1802 CB ALA A1029 9.442 -55.270 21.802 1.00186.81 C ANISOU 1802 CB ALA A1029 22345 22342 26292 -316 -273 -395 C ATOM 1803 N LEU A1030 7.098 -55.805 23.950 1.00186.21 N ANISOU 1803 N LEU A1030 22364 22334 26054 -332 -395 -269 N ATOM 1804 CA LEU A1030 5.692 -56.115 24.163 1.00186.22 C ANISOU 1804 CA LEU A1030 22413 22382 25961 -345 -408 -218 C ATOM 1805 C LEU A1030 5.132 -55.320 25.342 1.00184.80 C ANISOU 1805 C LEU A1030 22262 22236 25719 -346 -441 -175 C ATOM 1806 O LEU A1030 3.974 -54.911 25.306 1.00184.16 O ANISOU 1806 O LEU A1030 22217 22209 25547 -355 -419 -139 O ATOM 1807 CB LEU A1030 5.509 -57.623 24.366 1.00189.20 C ANISOU 1807 CB LEU A1030 22795 22734 26358 -352 -466 -208 C ATOM 1808 CG LEU A1030 5.356 -58.451 23.090 1.00189.28 C ANISOU 1808 CG LEU A1030 22798 22738 26381 -357 -427 -231 C ATOM 1809 CD1 LEU A1030 5.287 -59.934 23.416 1.00189.18 C ANISOU 1809 CD1 LEU A1030 22788 22694 26396 -362 -494 -222 C ATOM 1810 CD2 LEU A1030 4.125 -58.026 22.300 1.00188.39 C ANISOU 1810 CD2 LEU A1030 22720 22684 26174 -367 -366 -207 C ATOM 1811 N THR A1031 5.955 -55.111 26.379 1.00183.97 N ANISOU 1811 N THR A1031 22140 22099 25663 -337 -493 -180 N ATOM 1812 CA THR A1031 5.530 -54.370 27.559 1.00181.06 C ANISOU 1812 CA THR A1031 21796 21758 25242 -336 -528 -143 C ATOM 1813 C THR A1031 5.332 -52.896 27.213 1.00176.79 C ANISOU 1813 C THR A1031 21260 21255 24658 -331 -465 -145 C ATOM 1814 O THR A1031 4.482 -52.231 27.802 1.00171.51 O ANISOU 1814 O THR A1031 20623 20631 23911 -334 -470 -108 O ATOM 1815 CB THR A1031 6.484 -54.562 28.746 1.00181.80 C ANISOU 1815 CB THR A1031 21870 21804 25401 -326 -603 -149 C ATOM 1816 OG1 THR A1031 7.828 -54.397 28.293 1.00185.25 O ANISOU 1816 OG1 THR A1031 22260 22192 25936 -313 -585 -203 O ATOM 1817 CG2 THR A1031 6.326 -55.904 29.428 1.00179.58 C ANISOU 1817 CG2 THR A1031 21601 21499 25131 -333 -680 -127 C ATOM 1818 N LYS A1032 6.124 -52.401 26.252 1.00175.67 N ANISOU 1818 N LYS A1032 21086 21093 24566 -325 -406 -190 N ATOM 1819 CA LYS A1032 6.011 -51.030 25.782 1.00174.24 C ANISOU 1819 CA LYS A1032 20909 20943 24350 -322 -341 -196 C ATOM 1820 C LYS A1032 4.797 -50.892 24.865 1.00174.20 C ANISOU 1820 C LYS A1032 20937 20991 24260 -333 -285 -176 C ATOM 1821 O LYS A1032 4.213 -49.815 24.769 1.00176.54 O ANISOU 1821 O LYS A1032 21255 21328 24493 -333 -248 -161 O ATOM 1822 CB LYS A1032 7.304 -50.578 25.093 1.00171.61 C ANISOU 1822 CB LYS A1032 20531 20570 24103 -313 -299 -250 C ATOM 1823 CG LYS A1032 8.435 -50.184 26.033 1.00170.10 C ANISOU 1823 CG LYS A1032 20310 20338 23984 -300 -343 -268 C ATOM 1824 CD LYS A1032 9.680 -49.717 25.312 1.00170.54 C ANISOU 1824 CD LYS A1032 20319 20356 24123 -294 -297 -322 C ATOM 1825 CE LYS A1032 10.807 -49.362 26.258 1.00171.32 C ANISOU 1825 CE LYS A1032 20385 20412 24295 -281 -343 -341 C ATOM 1826 NZ LYS A1032 12.002 -48.877 25.528 1.00172.76 N ANISOU 1826 NZ LYS A1032 20521 20560 24559 -276 -295 -395 N ATOM 1827 N MET A1033 4.426 -51.993 24.199 1.00172.70 N ANISOU 1827 N MET A1033 20752 20798 24070 -341 -280 -177 N ATOM 1828 CA MET A1033 3.250 -52.021 23.344 1.00170.41 C ANISOU 1828 CA MET A1033 20494 20554 23701 -352 -233 -159 C ATOM 1829 C MET A1033 1.989 -52.088 24.201 1.00169.35 C ANISOU 1829 C MET A1033 20401 20467 23479 -360 -272 -105 C ATOM 1830 O MET A1033 0.976 -51.484 23.854 1.00169.83 O ANISOU 1830 O MET A1033 20491 20577 23459 -364 -235 -83 O ATOM 1831 CB MET A1033 3.280 -53.219 22.390 1.00171.33 C ANISOU 1831 CB MET A1033 20600 20650 23847 -358 -220 -178 C ATOM 1832 CG MET A1033 3.998 -52.935 21.086 1.00171.65 C ANISOU 1832 CG MET A1033 20614 20671 23933 -354 -148 -226 C ATOM 1833 SD MET A1033 4.369 -54.438 20.144 1.00171.38 S ANISOU 1833 SD MET A1033 20559 20599 23959 -357 -145 -258 S ATOM 1834 CE MET A1033 2.718 -54.941 19.661 1.00169.77 C ANISOU 1834 CE MET A1033 20403 20448 23654 -371 -133 -217 C ATOM 1835 N ARG A1034 2.068 -52.824 25.317 1.00168.99 N ANISOU 1835 N ARG A1034 20357 20402 23448 -361 -348 -84 N ATOM 1836 CA ARG A1034 0.938 -53.011 26.214 1.00168.34 C ANISOU 1836 CA ARG A1034 20313 20361 23289 -371 -390 -33 C ATOM 1837 C ARG A1034 0.613 -51.696 26.920 1.00169.38 C ANISOU 1837 C ARG A1034 20461 20530 23367 -365 -386 -14 C ATOM 1838 O ARG A1034 -0.548 -51.426 27.221 1.00170.11 O ANISOU 1838 O ARG A1034 20587 20674 23373 -372 -386 23 O ATOM 1839 CB ARG A1034 1.221 -54.128 27.224 1.00166.30 C ANISOU 1839 CB ARG A1034 20051 20068 23066 -375 -473 -18 C ATOM 1840 CG ARG A1034 -0.022 -54.653 27.926 1.00164.04 C ANISOU 1840 CG ARG A1034 19804 19822 22701 -390 -512 33 C ATOM 1841 CD ARG A1034 0.296 -55.655 29.019 1.00163.85 C ANISOU 1841 CD ARG A1034 19781 19763 22710 -395 -597 50 C ATOM 1842 NE ARG A1034 -0.889 -56.394 29.435 1.00163.96 N ANISOU 1842 NE ARG A1034 19831 19811 22655 -414 -627 96 N ATOM 1843 CZ ARG A1034 -1.754 -55.996 30.364 1.00162.18 C ANISOU 1843 CZ ARG A1034 19636 19630 22354 -422 -651 138 C ATOM 1844 NH1 ARG A1034 -1.577 -54.848 30.996 1.00161.48 N ANISOU 1844 NH1 ARG A1034 19549 19559 22248 -411 -648 140 N ATOM 1845 NH2 ARG A1034 -2.798 -56.751 30.656 1.00161.75 N ANISOU 1845 NH2 ARG A1034 19611 19604 22242 -441 -676 177 N ATOM 1846 N ALA A1035 1.651 -50.890 27.178 1.00168.30 N ANISOU 1846 N ALA A1035 20298 20365 23283 -351 -383 -40 N ATOM 1847 CA ALA A1035 1.491 -49.582 27.791 1.00164.87 C ANISOU 1847 CA ALA A1035 19875 19960 22808 -343 -377 -28 C ATOM 1848 C ALA A1035 0.737 -48.654 26.841 1.00161.46 C ANISOU 1848 C ALA A1035 19461 19574 22312 -345 -304 -27 C ATOM 1849 O ALA A1035 -0.164 -47.933 27.263 1.00159.78 O ANISOU 1849 O ALA A1035 19277 19410 22022 -345 -302 2 O ATOM 1850 CB ALA A1035 2.840 -49.017 28.169 1.00165.17 C ANISOU 1850 CB ALA A1035 19879 19953 22927 -329 -390 -60 C ATOM 1851 N ALA A1036 1.108 -48.703 25.555 1.00160.75 N ANISOU 1851 N ALA A1036 19354 19469 22254 -345 -245 -60 N ATOM 1852 CA ALA A1036 0.521 -47.854 24.530 1.00161.44 C ANISOU 1852 CA ALA A1036 19458 19593 22289 -347 -173 -65 C ATOM 1853 C ALA A1036 -0.863 -48.367 24.136 1.00161.83 C ANISOU 1853 C ALA A1036 19542 19688 22258 -359 -163 -34 C ATOM 1854 O ALA A1036 -1.673 -47.608 23.607 1.00162.61 O ANISOU 1854 O ALA A1036 19665 19830 22291 -359 -118 -25 O ATOM 1855 CB ALA A1036 1.442 -47.772 23.336 1.00162.34 C ANISOU 1855 CB ALA A1036 19543 19672 22467 -344 -117 -111 C ATOM 1856 N ALA A1037 -1.120 -49.655 24.398 1.00162.77 N ANISOU 1856 N ALA A1037 19664 19796 22385 -368 -205 -20 N ATOM 1857 CA ALA A1037 -2.389 -50.284 24.065 1.00163.34 C ANISOU 1857 CA ALA A1037 19766 19907 22387 -380 -201 8 C ATOM 1858 C ALA A1037 -3.508 -49.702 24.926 1.00164.61 C ANISOU 1858 C ALA A1037 19960 20123 22460 -383 -221 50 C ATOM 1859 O ALA A1037 -4.575 -49.370 24.415 1.00165.22 O ANISOU 1859 O ALA A1037 20063 20247 22465 -388 -187 66 O ATOM 1860 CB ALA A1037 -2.287 -51.781 24.224 1.00163.03 C ANISOU 1860 CB ALA A1037 19720 19838 22385 -389 -247 13 C ATOM 1861 N LEU A1038 -3.244 -49.580 26.233 1.00167.03 N ANISOU 1861 N LEU A1038 20265 20424 22774 -380 -278 67 N ATOM 1862 CA LEU A1038 -4.210 -49.038 27.176 1.00169.77 C ANISOU 1862 CA LEU A1038 20641 20822 23042 -382 -302 105 C ATOM 1863 C LEU A1038 -4.218 -47.513 27.097 1.00172.62 C ANISOU 1863 C LEU A1038 21006 21207 23374 -369 -264 97 C ATOM 1864 O LEU A1038 -5.242 -46.885 27.360 1.00174.09 O ANISOU 1864 O LEU A1038 21218 21446 23481 -370 -257 122 O ATOM 1865 CB LEU A1038 -3.862 -49.516 28.591 1.00170.15 C ANISOU 1865 CB LEU A1038 20687 20851 23112 -383 -379 125 C ATOM 1866 CG LEU A1038 -4.026 -51.013 28.856 1.00169.64 C ANISOU 1866 CG LEU A1038 20625 20767 23063 -398 -426 142 C ATOM 1867 CD1 LEU A1038 -3.590 -51.362 30.271 1.00168.50 C ANISOU 1867 CD1 LEU A1038 20480 20601 22941 -398 -501 159 C ATOM 1868 CD2 LEU A1038 -5.460 -51.462 28.615 1.00170.16 C ANISOU 1868 CD2 LEU A1038 20723 20885 23047 -414 -416 174 C ATOM 1869 N ASP A1039 -3.068 -46.932 26.734 1.00174.76 N ANISOU 1869 N ASP A1039 21250 21440 23711 -357 -240 61 N ATOM 1870 CA ASP A1039 -2.910 -45.489 26.652 1.00174.26 C ANISOU 1870 CA ASP A1039 21188 21392 23632 -345 -206 50 C ATOM 1871 C ASP A1039 -3.757 -44.934 25.509 1.00174.65 C ANISOU 1871 C ASP A1039 21258 21480 23622 -348 -140 49 C ATOM 1872 O ASP A1039 -4.419 -43.913 25.672 1.00174.44 O ANISOU 1872 O ASP A1039 21252 21494 23533 -342 -125 62 O ATOM 1873 CB ASP A1039 -1.437 -45.091 26.518 1.00174.77 C ANISOU 1873 CB ASP A1039 21216 21402 23786 -335 -197 12 C ATOM 1874 CG ASP A1039 -1.223 -43.607 26.274 1.00175.53 C ANISOU 1874 CG ASP A1039 21313 21511 23870 -324 -156 -2 C ATOM 1875 OD1 ASP A1039 -1.704 -42.801 27.096 1.00178.25 O ANISOU 1875 OD1 ASP A1039 21675 21888 24165 -318 -176 19 O ATOM 1876 OD2 ASP A1039 -0.584 -43.269 25.260 1.00174.79 O ANISOU 1876 OD2 ASP A1039 21202 21394 23816 -323 -103 -35 O ATOM 1877 N ALA A1040 -3.729 -45.624 24.361 1.00177.29 N ANISOU 1877 N ALA A1040 21587 21799 23975 -355 -104 32 N ATOM 1878 CA ALA A1040 -4.410 -45.175 23.156 1.00180.54 C ANISOU 1878 CA ALA A1040 22018 22241 24339 -357 -40 26 C ATOM 1879 C ALA A1040 -5.924 -45.327 23.294 1.00183.41 C ANISOU 1879 C ALA A1040 22416 22661 24610 -364 -47 62 C ATOM 1880 O ALA A1040 -6.676 -44.650 22.596 1.00183.22 O ANISOU 1880 O ALA A1040 22414 22672 24529 -363 -3 63 O ATOM 1881 CB ALA A1040 -3.886 -45.920 21.952 1.00179.31 C ANISOU 1881 CB ALA A1040 21846 22050 24234 -363 -3 -4 C ATOM 1882 N GLN A1041 -6.356 -46.214 24.201 1.00187.28 N ANISOU 1882 N GLN A1041 22911 23159 25086 -373 -103 89 N ATOM 1883 CA GLN A1041 -7.771 -46.467 24.431 1.00188.99 C ANISOU 1883 CA GLN A1041 23158 23429 25219 -382 -114 124 C ATOM 1884 C GLN A1041 -8.431 -45.227 25.032 1.00188.22 C ANISOU 1884 C GLN A1041 23081 23379 25055 -373 -113 141 C ATOM 1885 O GLN A1041 -9.598 -44.952 24.759 1.00189.01 O ANISOU 1885 O GLN A1041 23206 23527 25081 -376 -93 158 O ATOM 1886 CB GLN A1041 -7.966 -47.703 25.313 1.00192.13 C ANISOU 1886 CB GLN A1041 23556 23820 25623 -394 -176 150 C ATOM 1887 CG GLN A1041 -9.427 -48.100 25.491 1.00196.29 C ANISOU 1887 CG GLN A1041 24112 24400 26067 -407 -186 185 C ATOM 1888 CD GLN A1041 -9.615 -49.455 26.128 1.00199.15 C ANISOU 1888 CD GLN A1041 24476 24753 26440 -423 -240 208 C ATOM 1889 OE1 GLN A1041 -8.700 -50.274 26.186 1.00199.94 O ANISOU 1889 OE1 GLN A1041 24555 24802 26611 -425 -265 195 O ATOM 1890 NE2 GLN A1041 -10.823 -49.706 26.607 1.00199.51 N ANISOU 1890 NE2 GLN A1041 24545 24846 26414 -435 -258 243 N ATOM 1891 N LYS A1042 -7.669 -44.485 25.844 1.00185.52 N ANISOU 1891 N LYS A1042 22726 23021 24742 -362 -134 135 N ATOM 1892 CA LYS A1042 -8.138 -43.248 26.448 1.00182.03 C ANISOU 1892 CA LYS A1042 22300 22618 24245 -351 -135 147 C ATOM 1893 C LYS A1042 -8.020 -42.106 25.430 1.00178.64 C ANISOU 1893 C LYS A1042 21874 22192 23808 -341 -74 122 C ATOM 1894 O LYS A1042 -8.611 -42.243 24.340 1.00175.39 O ANISOU 1894 O LYS A1042 21476 21797 23369 -347 -30 118 O ATOM 1895 CB LYS A1042 -7.328 -42.923 27.707 1.00182.07 C ANISOU 1895 CB LYS A1042 22290 22602 24287 -343 -184 148 C ATOM 1896 CG LYS A1042 -7.438 -43.933 28.842 1.00180.83 C ANISOU 1896 CG LYS A1042 22133 22441 24132 -352 -249 175 C ATOM 1897 CD LYS A1042 -6.682 -43.517 30.085 1.00179.35 C ANISOU 1897 CD LYS A1042 21936 22235 23976 -342 -298 176 C ATOM 1898 CE LYS A1042 -6.833 -44.501 31.226 1.00179.81 C ANISOU 1898 CE LYS A1042 21999 22291 24031 -353 -363 204 C ATOM 1899 NZ LYS A1042 -6.160 -44.023 32.456 1.00180.52 N ANISOU 1899 NZ LYS A1042 22082 22365 24143 -342 -411 207 N ATOM 1900 N LYS A1059 -19.630 -50.731 20.525 1.00209.36 N ANISOU 1900 N LYS A1059 25936 26382 27228 -483 -30 294 N ATOM 1901 CA LYS A1059 -18.996 -51.855 21.268 1.00207.47 C ANISOU 1901 CA LYS A1059 25681 26106 27040 -497 -78 306 C ATOM 1902 C LYS A1059 -17.830 -52.410 20.453 1.00208.56 C ANISOU 1902 C LYS A1059 25803 26183 27258 -492 -64 277 C ATOM 1903 O LYS A1059 -17.004 -53.154 20.980 1.00209.93 O ANISOU 1903 O LYS A1059 25959 26316 27488 -498 -100 278 O ATOM 1904 CB LYS A1059 -20.028 -52.945 21.578 1.00205.22 C ANISOU 1904 CB LYS A1059 25406 25847 26720 -519 -109 337 C ATOM 1905 CG LYS A1059 -21.241 -52.489 22.379 1.00203.63 C ANISOU 1905 CG LYS A1059 25220 25710 26441 -526 -122 366 C ATOM 1906 CD LYS A1059 -22.319 -53.547 22.484 1.00201.97 C ANISOU 1906 CD LYS A1059 25020 25526 26195 -550 -143 393 C ATOM 1907 CE LYS A1059 -23.630 -53.023 23.034 1.00199.52 C ANISOU 1907 CE LYS A1059 24723 25283 25802 -556 -145 415 C ATOM 1908 NZ LYS A1059 -24.303 -52.105 22.084 1.00198.90 N ANISOU 1908 NZ LYS A1059 24656 25236 25680 -540 -96 397 N ATOM 1909 N ASP A1060 -17.779 -52.031 19.169 1.00207.51 N ANISOU 1909 N ASP A1060 25675 26044 27127 -482 -12 250 N ATOM 1910 CA ASP A1060 -16.706 -52.413 18.262 1.00206.12 C ANISOU 1910 CA ASP A1060 25482 25813 27020 -476 11 217 C ATOM 1911 C ASP A1060 -15.368 -51.928 18.811 1.00208.34 C ANISOU 1911 C ASP A1060 25742 26057 27362 -466 2 201 C ATOM 1912 O ASP A1060 -14.338 -52.562 18.590 1.00206.84 O ANISOU 1912 O ASP A1060 25531 25816 27244 -465 -4 181 O ATOM 1913 CB ASP A1060 -16.941 -51.865 16.851 1.00203.17 C ANISOU 1913 CB ASP A1060 25122 25446 26627 -466 73 192 C ATOM 1914 CG ASP A1060 -17.668 -52.827 15.926 1.00201.84 C ANISOU 1914 CG ASP A1060 24965 25283 26444 -476 84 192 C ATOM 1915 OD1 ASP A1060 -17.558 -54.050 16.146 1.00201.32 O ANISOU 1915 OD1 ASP A1060 24889 25194 26409 -488 49 201 O ATOM 1916 OD2 ASP A1060 -18.334 -52.344 14.989 1.00201.71 O ANISOU 1916 OD2 ASP A1060 24968 25290 26384 -470 125 183 O ATOM 1917 N PHE A1061 -15.409 -50.798 19.528 1.00212.61 N ANISOU 1917 N PHE A1061 26286 26622 27874 -457 0 208 N ATOM 1918 CA PHE A1061 -14.236 -50.185 20.128 1.00215.81 C ANISOU 1918 CA PHE A1061 26672 26996 28329 -446 -10 194 C ATOM 1919 C PHE A1061 -13.613 -51.139 21.146 1.00217.39 C ANISOU 1919 C PHE A1061 26855 27165 28580 -455 -69 207 C ATOM 1920 O PHE A1061 -12.471 -51.561 20.976 1.00218.43 O ANISOU 1920 O PHE A1061 26963 27244 28786 -452 -74 184 O ATOM 1921 CB PHE A1061 -14.598 -48.814 20.713 1.00216.77 C ANISOU 1921 CB PHE A1061 26805 27157 28401 -435 -4 203 C ATOM 1922 CG PHE A1061 -13.492 -48.088 21.441 1.00216.81 C ANISOU 1922 CG PHE A1061 26792 27135 28451 -424 -18 192 C ATOM 1923 CD1 PHE A1061 -12.157 -48.352 21.167 1.00218.18 C ANISOU 1923 CD1 PHE A1061 26940 27251 28707 -419 -14 165 C ATOM 1924 CD2 PHE A1061 -13.788 -47.113 22.383 1.00216.06 C ANISOU 1924 CD2 PHE A1061 26705 27073 28316 -416 -34 207 C ATOM 1925 CE1 PHE A1061 -11.147 -47.679 21.838 1.00218.29 C ANISOU 1925 CE1 PHE A1061 26936 27240 28763 -409 -27 153 C ATOM 1926 CE2 PHE A1061 -12.777 -46.434 23.047 1.00215.53 C ANISOU 1926 CE2 PHE A1061 26621 26980 28289 -405 -48 196 C ATOM 1927 CZ PHE A1061 -11.458 -46.716 22.771 1.00216.66 C ANISOU 1927 CZ PHE A1061 26739 27066 28516 -402 -45 170 C ATOM 1928 N ARG A1062 -14.385 -51.488 22.183 1.00216.87 N ANISOU 1928 N ARG A1062 26799 27129 28471 -467 -114 242 N ATOM 1929 CA ARG A1062 -13.895 -52.288 23.295 1.00214.84 C ANISOU 1929 CA ARG A1062 26531 26847 28250 -476 -174 259 C ATOM 1930 C ARG A1062 -13.594 -53.721 22.856 1.00212.66 C ANISOU 1930 C ARG A1062 26246 26532 28025 -488 -192 255 C ATOM 1931 O ARG A1062 -12.796 -54.401 23.497 1.00211.91 O ANISOU 1931 O ARG A1062 26136 26396 27985 -492 -236 256 O ATOM 1932 CB ARG A1062 -14.887 -52.267 24.464 1.00215.91 C ANISOU 1932 CB ARG A1062 26685 27031 28321 -488 -213 299 C ATOM 1933 CG ARG A1062 -14.544 -51.265 25.557 1.00217.67 C ANISOU 1933 CG ARG A1062 26905 27265 28534 -477 -233 306 C ATOM 1934 CD ARG A1062 -15.304 -51.557 26.838 1.00219.43 C ANISOU 1934 CD ARG A1062 27142 27524 28707 -492 -282 345 C ATOM 1935 NE ARG A1062 -15.082 -50.560 27.878 1.00222.16 N ANISOU 1935 NE ARG A1062 27489 27886 29037 -481 -300 351 N ATOM 1936 CZ ARG A1062 -14.264 -50.703 28.918 1.00223.49 C ANISOU 1936 CZ ARG A1062 27647 28025 29244 -481 -346 357 C ATOM 1937 NH1 ARG A1062 -14.146 -49.725 29.800 1.00223.52 N ANISOU 1937 NH1 ARG A1062 27653 28047 29226 -470 -359 361 N ATOM 1938 NH2 ARG A1062 -13.570 -51.816 29.079 1.00223.52 N ANISOU 1938 NH2 ARG A1062 27640 27980 29307 -490 -382 357 N ATOM 1939 N HIS A1063 -14.232 -54.169 21.766 1.00211.00 N ANISOU 1939 N HIS A1063 26045 26332 27794 -493 -160 249 N ATOM 1940 CA HIS A1063 -14.094 -55.545 21.314 1.00209.87 C ANISOU 1940 CA HIS A1063 25895 26155 27690 -505 -177 246 C ATOM 1941 C HIS A1063 -12.755 -55.751 20.609 1.00205.94 C ANISOU 1941 C HIS A1063 25372 25598 27278 -493 -159 205 C ATOM 1942 O HIS A1063 -12.116 -56.785 20.788 1.00206.21 O ANISOU 1942 O HIS A1063 25391 25589 27371 -499 -195 201 O ATOM 1943 CB HIS A1063 -15.281 -55.970 20.437 1.00213.44 C ANISOU 1943 CB HIS A1063 26367 26640 28091 -514 -151 254 C ATOM 1944 CG HIS A1063 -15.342 -57.442 20.198 1.00217.40 C ANISOU 1944 CG HIS A1063 26866 27115 28623 -529 -179 260 C ATOM 1945 ND1 HIS A1063 -14.506 -58.081 19.301 1.00218.89 N ANISOU 1945 ND1 HIS A1063 27037 27253 28877 -524 -165 228 N ATOM 1946 CD2 HIS A1063 -16.127 -58.402 20.734 1.00218.42 C ANISOU 1946 CD2 HIS A1063 27007 27259 28726 -550 -221 293 C ATOM 1947 CE1 HIS A1063 -14.775 -59.371 19.295 1.00219.78 C ANISOU 1947 CE1 HIS A1063 27152 27351 29004 -539 -199 240 C ATOM 1948 NE2 HIS A1063 -15.766 -59.593 20.166 1.00220.38 N ANISOU 1948 NE2 HIS A1063 27246 27465 29024 -556 -234 281 N ATOM 1949 N GLY A1064 -12.350 -54.761 19.804 1.00201.34 N ANISOU 1949 N GLY A1064 24785 25013 26701 -478 -104 176 N ATOM 1950 CA GLY A1064 -11.116 -54.827 19.038 1.00195.57 C ANISOU 1950 CA GLY A1064 24029 24231 26047 -467 -78 134 C ATOM 1951 C GLY A1064 -9.875 -54.830 19.928 1.00191.47 C ANISOU 1951 C GLY A1064 23484 23669 25598 -461 -116 124 C ATOM 1952 O GLY A1064 -8.858 -55.422 19.572 1.00189.28 O ANISOU 1952 O GLY A1064 23182 23341 25395 -457 -119 96 O ATOM 1953 N PHE A1065 -9.983 -54.172 21.089 1.00188.84 N ANISOU 1953 N PHE A1065 23156 23356 25239 -459 -146 147 N ATOM 1954 CA PHE A1065 -8.871 -54.015 22.014 1.00185.33 C ANISOU 1954 CA PHE A1065 22689 22876 24853 -452 -183 140 C ATOM 1955 C PHE A1065 -8.734 -55.246 22.907 1.00184.26 C ANISOU 1955 C PHE A1065 22549 22714 24746 -465 -252 160 C ATOM 1956 O PHE A1065 -7.632 -55.566 23.347 1.00182.43 O ANISOU 1956 O PHE A1065 22293 22434 24586 -459 -284 144 O ATOM 1957 CB PHE A1065 -9.018 -52.724 22.824 1.00181.97 C ANISOU 1957 CB PHE A1065 22272 22482 24387 -444 -184 153 C ATOM 1958 CG PHE A1065 -8.505 -51.489 22.127 1.00178.52 C ANISOU 1958 CG PHE A1065 21828 22043 23959 -429 -127 122 C ATOM 1959 CD1 PHE A1065 -9.215 -50.912 21.084 1.00177.45 C ANISOU 1959 CD1 PHE A1065 21710 21940 23773 -427 -69 116 C ATOM 1960 CD2 PHE A1065 -7.307 -50.905 22.511 1.00176.78 C ANISOU 1960 CD2 PHE A1065 21583 21787 23798 -416 -132 100 C ATOM 1961 CE1 PHE A1065 -8.738 -49.780 20.441 1.00176.55 C ANISOU 1961 CE1 PHE A1065 21592 21823 23667 -414 -18 90 C ATOM 1962 CE2 PHE A1065 -6.832 -49.771 21.868 1.00175.97 C ANISOU 1962 CE2 PHE A1065 21474 21682 23704 -404 -80 73 C ATOM 1963 CZ PHE A1065 -7.548 -49.210 20.835 1.00175.74 C ANISOU 1963 CZ PHE A1065 21465 21686 23624 -404 -23 69 C ATOM 1964 N ASP A1066 -9.857 -55.928 23.164 1.00184.88 N ANISOU 1964 N ASP A1066 22650 22825 24770 -481 -276 194 N ATOM 1965 CA ASP A1066 -9.857 -57.146 23.959 1.00185.58 C ANISOU 1965 CA ASP A1066 22740 22893 24879 -496 -341 217 C ATOM 1966 C ASP A1066 -9.111 -58.251 23.214 1.00184.36 C ANISOU 1966 C ASP A1066 22565 22683 24799 -496 -346 190 C ATOM 1967 O ASP A1066 -8.560 -59.157 23.836 1.00184.37 O ANISOU 1967 O ASP A1066 22557 22645 24850 -502 -401 194 O ATOM 1968 CB ASP A1066 -11.276 -57.561 24.359 1.00189.05 C ANISOU 1968 CB ASP A1066 23209 23382 25239 -516 -360 261 C ATOM 1969 CG ASP A1066 -11.880 -56.706 25.461 1.00191.70 C ANISOU 1969 CG ASP A1066 23561 23764 25511 -518 -376 291 C ATOM 1970 OD1 ASP A1066 -11.122 -55.952 26.108 1.00191.66 O ANISOU 1970 OD1 ASP A1066 23545 23746 25529 -505 -387 283 O ATOM 1971 OD2 ASP A1066 -13.107 -56.799 25.664 1.00193.54 O ANISOU 1971 OD2 ASP A1066 23818 24047 25672 -532 -378 322 O ATOM 1972 N ILE A1067 -9.099 -58.158 21.878 1.00181.18 N ANISOU 1972 N ILE A1067 22157 22278 24404 -489 -288 161 N ATOM 1973 CA ILE A1067 -8.371 -59.100 21.044 1.00177.09 C ANISOU 1973 CA ILE A1067 21619 21711 23956 -487 -284 129 C ATOM 1974 C ILE A1067 -6.911 -58.660 20.951 1.00175.38 C ANISOU 1974 C ILE A1067 21369 21447 23820 -470 -273 88 C ATOM 1975 O ILE A1067 -6.016 -59.500 20.963 1.00172.95 O ANISOU 1975 O ILE A1067 21038 21087 23587 -468 -303 67 O ATOM 1976 CB ILE A1067 -9.032 -59.258 19.657 1.00177.08 C ANISOU 1976 CB ILE A1067 21629 21728 23926 -488 -228 115 C ATOM 1977 CG1 ILE A1067 -10.516 -59.625 19.773 1.00177.32 C ANISOU 1977 CG1 ILE A1067 21691 21808 23876 -505 -239 156 C ATOM 1978 CG2 ILE A1067 -8.271 -60.265 18.804 1.00176.78 C ANISOU 1978 CG2 ILE A1067 21570 21639 23961 -485 -225 81 C ATOM 1979 CD1 ILE A1067 -11.304 -59.455 18.493 1.00176.17 C ANISOU 1979 CD1 ILE A1067 21560 21690 23685 -505 -180 146 C ATOM 1980 N LEU A1068 -6.681 -57.341 20.877 1.00176.69 N ANISOU 1980 N LEU A1068 21533 21630 23971 -458 -233 76 N ATOM 1981 CA LEU A1068 -5.338 -56.805 20.705 1.00176.98 C ANISOU 1981 CA LEU A1068 21538 21626 24080 -442 -215 36 C ATOM 1982 C LEU A1068 -4.492 -57.073 21.949 1.00176.51 C ANISOU 1982 C LEU A1068 21461 21530 24074 -440 -280 41 C ATOM 1983 O LEU A1068 -3.405 -57.636 21.840 1.00177.63 O ANISOU 1983 O LEU A1068 21574 21620 24300 -434 -297 10 O ATOM 1984 CB LEU A1068 -5.401 -55.306 20.387 1.00175.70 C ANISOU 1984 CB LEU A1068 21382 21495 23882 -433 -159 27 C ATOM 1985 CG LEU A1068 -4.049 -54.596 20.301 1.00174.41 C ANISOU 1985 CG LEU A1068 21186 21293 23788 -418 -139 -11 C ATOM 1986 CD1 LEU A1068 -3.273 -55.036 19.067 1.00174.29 C ANISOU 1986 CD1 LEU A1068 21147 21240 23835 -414 -97 -56 C ATOM 1987 CD2 LEU A1068 -4.224 -53.086 20.314 1.00174.52 C ANISOU 1987 CD2 LEU A1068 21211 21340 23758 -410 -99 -9 C ATOM 1988 N VAL A1069 -5.000 -56.663 23.118 1.00174.51 N ANISOU 1988 N VAL A1069 21226 21307 23774 -444 -318 77 N ATOM 1989 CA VAL A1069 -4.277 -56.794 24.375 1.00173.43 C ANISOU 1989 CA VAL A1069 21078 21140 23679 -442 -381 85 C ATOM 1990 C VAL A1069 -4.213 -58.270 24.764 1.00172.55 C ANISOU 1990 C VAL A1069 20965 20995 23601 -453 -443 97 C ATOM 1991 O VAL A1069 -3.222 -58.719 25.337 1.00173.61 O ANISOU 1991 O VAL A1069 21078 21081 23806 -448 -489 84 O ATOM 1992 CB VAL A1069 -4.896 -55.922 25.489 1.00174.09 C ANISOU 1992 CB VAL A1069 21183 21266 23696 -443 -402 121 C ATOM 1993 CG1 VAL A1069 -4.140 -56.046 26.805 1.00173.34 C ANISOU 1993 CG1 VAL A1069 21078 21140 23642 -440 -469 129 C ATOM 1994 CG2 VAL A1069 -4.994 -54.461 25.076 1.00174.98 C ANISOU 1994 CG2 VAL A1069 21298 21411 23774 -431 -343 109 C ATOM 1995 N GLY A1070 -5.274 -59.014 24.428 1.00170.38 N ANISOU 1995 N GLY A1070 20714 20747 23277 -469 -443 121 N ATOM 1996 CA GLY A1070 -5.346 -60.446 24.672 1.00168.43 C ANISOU 1996 CA GLY A1070 20469 20471 23055 -482 -498 135 C ATOM 1997 C GLY A1070 -4.227 -61.211 23.967 1.00167.72 C ANISOU 1997 C GLY A1070 20347 20320 23060 -473 -499 90 C ATOM 1998 O GLY A1070 -3.732 -62.204 24.494 1.00168.21 O ANISOU 1998 O GLY A1070 20400 20339 23173 -476 -559 92 O ATOM 1999 N GLN A1071 -3.840 -60.734 22.777 1.00168.03 N ANISOU 1999 N GLN A1071 20369 20355 23121 -461 -433 51 N ATOM 2000 CA GLN A1071 -2.793 -61.357 21.982 1.00168.47 C ANISOU 2000 CA GLN A1071 20392 20356 23264 -451 -423 4 C ATOM 2001 C GLN A1071 -1.415 -60.960 22.511 1.00167.35 C ANISOU 2001 C GLN A1071 20216 20169 23200 -435 -442 -26 C ATOM 2002 O GLN A1071 -0.454 -61.710 22.348 1.00169.14 O ANISOU 2002 O GLN A1071 20414 20342 23509 -429 -466 -58 O ATOM 2003 CB GLN A1071 -2.934 -60.989 20.503 1.00168.85 C ANISOU 2003 CB GLN A1071 20436 20420 23301 -445 -342 -26 C ATOM 2004 CG GLN A1071 -4.205 -61.516 19.851 1.00169.62 C ANISOU 2004 CG GLN A1071 20562 20553 23332 -459 -324 -3 C ATOM 2005 CD GLN A1071 -4.315 -61.126 18.396 1.00170.37 C ANISOU 2005 CD GLN A1071 20656 20661 23416 -453 -246 -34 C ATOM 2006 OE1 GLN A1071 -3.467 -60.422 17.851 1.00170.79 O ANISOU 2006 OE1 GLN A1071 20687 20699 23507 -440 -202 -71 O ATOM 2007 NE2 GLN A1071 -5.369 -61.595 17.748 1.00171.47 N ANISOU 2007 NE2 GLN A1071 20819 20829 23502 -463 -229 -18 N ATOM 2008 N ILE A1072 -1.326 -59.772 23.125 1.00164.80 N ANISOU 2008 N ILE A1072 19896 19868 22852 -429 -433 -17 N ATOM 2009 CA ILE A1072 -0.086 -59.301 23.724 1.00162.75 C ANISOU 2009 CA ILE A1072 19607 19570 22662 -415 -454 -42 C ATOM 2010 C ILE A1072 0.164 -60.075 25.017 1.00163.41 C ANISOU 2010 C ILE A1072 19693 19624 22773 -419 -543 -19 C ATOM 2011 O ILE A1072 1.305 -60.413 25.323 1.00163.50 O ANISOU 2011 O ILE A1072 19674 19581 22867 -409 -578 -47 O ATOM 2012 CB ILE A1072 -0.101 -57.771 23.940 1.00161.11 C ANISOU 2012 CB ILE A1072 19403 19395 22418 -407 -416 -40 C ATOM 2013 CG1 ILE A1072 -0.192 -57.012 22.612 1.00160.81 C ANISOU 2013 CG1 ILE A1072 19361 19377 22362 -402 -329 -67 C ATOM 2014 CG2 ILE A1072 1.103 -57.320 24.756 1.00161.23 C ANISOU 2014 CG2 ILE A1072 19390 19370 22500 -394 -448 -59 C ATOM 2015 CD1 ILE A1072 -0.532 -55.544 22.755 1.00160.72 C ANISOU 2015 CD1 ILE A1072 19363 19408 22295 -398 -290 -56 C ATOM 2016 N ASP A1073 -0.917 -60.364 25.755 1.00163.75 N ANISOU 2016 N ASP A1073 19772 19702 22744 -435 -579 31 N ATOM 2017 CA ASP A1073 -0.847 -61.124 26.994 1.00163.28 C ANISOU 2017 CA ASP A1073 19723 19620 22696 -443 -663 60 C ATOM 2018 C ASP A1073 -0.340 -62.538 26.715 1.00162.82 C ANISOU 2018 C ASP A1073 19649 19508 22706 -446 -703 42 C ATOM 2019 O ASP A1073 0.484 -63.056 27.466 1.00162.96 O ANISOU 2019 O ASP A1073 19653 19477 22786 -441 -765 36 O ATOM 2020 CB ASP A1073 -2.192 -61.134 27.729 1.00163.18 C ANISOU 2020 CB ASP A1073 19752 19661 22586 -462 -685 117 C ATOM 2021 CG ASP A1073 -2.394 -59.958 28.670 1.00163.33 C ANISOU 2021 CG ASP A1073 19785 19716 22557 -458 -688 139 C ATOM 2022 OD1 ASP A1073 -1.543 -59.045 28.667 1.00164.31 O ANISOU 2022 OD1 ASP A1073 19886 19825 22718 -441 -667 110 O ATOM 2023 OD2 ASP A1073 -3.403 -59.966 29.402 1.00162.64 O ANISOU 2023 OD2 ASP A1073 19730 19670 22394 -474 -712 184 O ATOM 2024 N ASP A1074 -0.838 -63.142 25.629 1.00162.07 N ANISOU 2024 N ASP A1074 19558 19422 22601 -452 -668 34 N ATOM 2025 CA ASP A1074 -0.477 -64.499 25.250 1.00162.25 C ANISOU 2025 CA ASP A1074 19568 19397 22683 -455 -701 17 C ATOM 2026 C ASP A1074 0.985 -64.544 24.814 1.00166.03 C ANISOU 2026 C ASP A1074 20001 19818 23266 -434 -695 -41 C ATOM 2027 O ASP A1074 1.715 -65.461 25.185 1.00168.53 O ANISOU 2027 O ASP A1074 20301 20081 23652 -431 -754 -54 O ATOM 2028 CB ASP A1074 -1.412 -65.049 24.168 1.00157.51 C ANISOU 2028 CB ASP A1074 18983 18823 22041 -466 -662 22 C ATOM 2029 CG ASP A1074 -2.830 -65.310 24.647 1.00154.65 C ANISOU 2029 CG ASP A1074 18664 18511 21587 -488 -681 79 C ATOM 2030 OD1 ASP A1074 -3.081 -65.169 25.861 1.00153.82 O ANISOU 2030 OD1 ASP A1074 18576 18416 21451 -497 -729 116 O ATOM 2031 OD2 ASP A1074 -3.673 -65.656 23.799 1.00152.40 O ANISOU 2031 OD2 ASP A1074 18392 18251 21261 -497 -647 85 O ATOM 2032 N ALA A1075 1.398 -63.542 24.029 1.00169.41 N ANISOU 2032 N ALA A1075 20408 20257 23703 -421 -624 -75 N ATOM 2033 CA ALA A1075 2.755 -63.469 23.512 1.00172.31 C ANISOU 2033 CA ALA A1075 20731 20575 24166 -403 -606 -133 C ATOM 2034 C ALA A1075 3.734 -63.120 24.631 1.00175.36 C ANISOU 2034 C ALA A1075 21097 20925 24605 -393 -657 -139 C ATOM 2035 O ALA A1075 4.909 -63.473 24.555 1.00176.83 O ANISOU 2035 O ALA A1075 21246 21058 24884 -379 -676 -182 O ATOM 2036 CB ALA A1075 2.826 -62.480 22.373 1.00170.92 C ANISOU 2036 CB ALA A1075 20542 20424 23977 -396 -514 -163 C ATOM 2037 N LEU A1076 3.236 -62.436 25.670 1.00178.49 N ANISOU 2037 N LEU A1076 21519 21354 24944 -398 -681 -99 N ATOM 2038 CA LEU A1076 4.062 -62.025 26.796 1.00181.40 C ANISOU 2038 CA LEU A1076 21875 21695 25354 -388 -731 -101 C ATOM 2039 C LEU A1076 4.408 -63.234 27.662 1.00183.12 C ANISOU 2039 C LEU A1076 22095 21865 25618 -391 -822 -90 C ATOM 2040 O LEU A1076 5.550 -63.372 28.096 1.00182.56 O ANISOU 2040 O LEU A1076 21994 21741 25628 -378 -862 -119 O ATOM 2041 CB LEU A1076 3.325 -60.958 27.613 1.00181.43 C ANISOU 2041 CB LEU A1076 21910 21751 25275 -393 -727 -59 C ATOM 2042 CG LEU A1076 4.033 -60.491 28.885 1.00181.76 C ANISOU 2042 CG LEU A1076 21945 21769 25346 -384 -782 -54 C ATOM 2043 CD1 LEU A1076 5.044 -59.398 28.572 1.00183.05 C ANISOU 2043 CD1 LEU A1076 22072 21918 25560 -365 -739 -97 C ATOM 2044 CD2 LEU A1076 3.025 -60.005 29.914 1.00180.55 C ANISOU 2044 CD2 LEU A1076 21834 21667 25102 -395 -807 1 C ATOM 2045 N LYS A1077 3.416 -64.101 27.902 1.00185.15 N ANISOU 2045 N LYS A1077 22387 22140 25822 -410 -856 -48 N ATOM 2046 CA LYS A1077 3.575 -65.229 28.809 1.00186.79 C ANISOU 2046 CA LYS A1077 22605 22308 26060 -417 -946 -29 C ATOM 2047 C LYS A1077 4.533 -66.259 28.212 1.00188.25 C ANISOU 2047 C LYS A1077 22755 22430 26343 -407 -967 -75 C ATOM 2048 O LYS A1077 5.140 -67.035 28.948 1.00190.68 O ANISOU 2048 O LYS A1077 23057 22687 26706 -404 -1043 -77 O ATOM 2049 CB LYS A1077 2.217 -65.831 29.187 1.00187.58 C ANISOU 2049 CB LYS A1077 22752 22448 26073 -442 -972 29 C ATOM 2050 CG LYS A1077 1.555 -66.703 28.128 1.00189.02 C ANISOU 2050 CG LYS A1077 22941 22639 26240 -453 -944 27 C ATOM 2051 CD LYS A1077 0.304 -67.398 28.620 1.00188.95 C ANISOU 2051 CD LYS A1077 22976 22661 26156 -479 -980 84 C ATOM 2052 CE LYS A1077 -0.271 -68.372 27.613 1.00188.42 C ANISOU 2052 CE LYS A1077 22914 22595 26083 -489 -962 81 C ATOM 2053 NZ LYS A1077 -1.448 -69.089 28.157 1.00186.79 N ANISOU 2053 NZ LYS A1077 22749 22415 25806 -516 -1002 137 N ATOM 2054 N LEU A1078 4.662 -66.256 26.879 1.00187.31 N ANISOU 2054 N LEU A1078 22613 22313 26245 -400 -899 -113 N ATOM 2055 CA LEU A1078 5.595 -67.143 26.204 1.00187.08 C ANISOU 2055 CA LEU A1078 22547 22226 26310 -389 -909 -164 C ATOM 2056 C LEU A1078 7.022 -66.634 26.396 1.00190.36 C ANISOU 2056 C LEU A1078 22918 22596 26815 -367 -914 -212 C ATOM 2057 O LEU A1078 7.965 -67.418 26.337 1.00192.42 O ANISOU 2057 O LEU A1078 23147 22798 27165 -356 -953 -249 O ATOM 2058 CB LEU A1078 5.234 -67.256 24.718 1.00182.93 C ANISOU 2058 CB LEU A1078 22013 21721 25771 -389 -833 -188 C ATOM 2059 CG LEU A1078 3.938 -68.002 24.397 1.00179.81 C ANISOU 2059 CG LEU A1078 21657 21359 25305 -409 -834 -149 C ATOM 2060 CD1 LEU A1078 3.834 -68.281 22.907 1.00178.37 C ANISOU 2060 CD1 LEU A1078 21461 21182 25131 -406 -768 -184 C ATOM 2061 CD2 LEU A1078 3.837 -69.302 25.182 1.00179.70 C ANISOU 2061 CD2 LEU A1078 21659 21309 25310 -420 -925 -124 C ATOM 2062 N ALA A1079 7.164 -65.324 26.633 1.00192.13 N ANISOU 2062 N ALA A1079 23138 22848 27017 -361 -877 -212 N ATOM 2063 CA ALA A1079 8.463 -64.716 26.873 1.00194.65 C ANISOU 2063 CA ALA A1079 23415 23128 27415 -341 -879 -255 C ATOM 2064 C ALA A1079 8.923 -64.997 28.303 1.00196.98 C ANISOU 2064 C ALA A1079 23716 23387 27741 -338 -973 -236 C ATOM 2065 O ALA A1079 10.111 -65.207 28.542 1.00198.24 O ANISOU 2065 O ALA A1079 23839 23491 27994 -322 -1008 -276 O ATOM 2066 CB ALA A1079 8.410 -63.235 26.584 1.00193.23 C ANISOU 2066 CB ALA A1079 23232 22990 27198 -337 -806 -259 C ATOM 2067 N ASN A1080 7.968 -65.000 29.244 1.00196.54 N ANISOU 2067 N ASN A1080 23707 23364 27606 -353 -1013 -177 N ATOM 2068 CA ASN A1080 8.247 -65.272 30.646 1.00194.28 C ANISOU 2068 CA ASN A1080 23435 23050 27334 -353 -1103 -152 C ATOM 2069 C ASN A1080 8.614 -66.743 30.828 1.00191.82 C ANISOU 2069 C ASN A1080 23119 22681 27082 -355 -1177 -159 C ATOM 2070 O ASN A1080 9.414 -67.080 31.698 1.00190.36 O ANISOU 2070 O ASN A1080 22924 22446 26957 -346 -1250 -167 O ATOM 2071 CB ASN A1080 7.090 -64.847 31.556 1.00196.40 C ANISOU 2071 CB ASN A1080 23755 23372 27497 -371 -1119 -87 C ATOM 2072 CG ASN A1080 7.007 -63.350 31.772 1.00197.45 C ANISOU 2072 CG ASN A1080 23888 23547 27587 -364 -1072 -82 C ATOM 2073 OD1 ASN A1080 8.020 -62.654 31.760 1.00197.46 O ANISOU 2073 OD1 ASN A1080 23855 23523 27649 -346 -1058 -121 O ATOM 2074 ND2 ASN A1080 5.802 -62.845 31.983 1.00196.78 N ANISOU 2074 ND2 ASN A1080 23842 23525 27399 -379 -1048 -36 N ATOM 2075 N GLU A1081 8.022 -67.607 29.993 1.00190.02 N ANISOU 2075 N GLU A1081 22899 22460 26839 -366 -1159 -157 N ATOM 2076 CA GLU A1081 8.300 -69.035 30.006 1.00189.05 C ANISOU 2076 CA GLU A1081 22774 22285 26771 -367 -1224 -166 C ATOM 2077 C GLU A1081 9.631 -69.318 29.311 1.00188.21 C ANISOU 2077 C GLU A1081 22610 22120 26779 -344 -1216 -236 C ATOM 2078 O GLU A1081 10.233 -70.368 29.529 1.00188.59 O ANISOU 2078 O GLU A1081 22646 22111 26897 -339 -1282 -255 O ATOM 2079 CB GLU A1081 7.163 -69.816 29.344 1.00189.33 C ANISOU 2079 CB GLU A1081 22838 22351 26747 -387 -1205 -138 C ATOM 2080 CG GLU A1081 5.999 -70.103 30.277 1.00189.71 C ANISOU 2080 CG GLU A1081 22941 22432 26706 -412 -1251 -68 C ATOM 2081 CD GLU A1081 4.965 -71.081 29.742 1.00189.30 C ANISOU 2081 CD GLU A1081 22917 22400 26609 -432 -1249 -41 C ATOM 2082 OE1 GLU A1081 4.899 -71.263 28.509 1.00189.21 O ANISOU 2082 OE1 GLU A1081 22888 22394 26610 -428 -1192 -72 O ATOM 2083 OE2 GLU A1081 4.226 -71.661 30.562 1.00188.83 O ANISOU 2083 OE2 GLU A1081 22899 22349 26500 -453 -1306 11 O ATOM 2084 N GLY A1082 10.069 -68.381 28.461 1.00187.52 N ANISOU 2084 N GLY A1082 22490 22049 26710 -332 -1134 -277 N ATOM 2085 CA GLY A1082 11.362 -68.472 27.799 1.00187.13 C ANISOU 2085 CA GLY A1082 22384 21950 26767 -311 -1117 -347 C ATOM 2086 C GLY A1082 11.261 -68.929 26.344 1.00187.39 C ANISOU 2086 C GLY A1082 22398 21988 26814 -310 -1054 -382 C ATOM 2087 O GLY A1082 12.281 -69.065 25.670 1.00188.38 O ANISOU 2087 O GLY A1082 22475 22076 27026 -294 -1032 -442 O ATOM 2088 N LYS A1083 10.027 -69.153 25.868 1.00184.95 N ANISOU 2088 N LYS A1083 22127 21727 26420 -328 -1023 -344 N ATOM 2089 CA LYS A1083 9.756 -69.619 24.512 1.00182.60 C ANISOU 2089 CA LYS A1083 21819 21439 26123 -330 -965 -370 C ATOM 2090 C LYS A1083 9.952 -68.491 23.499 1.00182.85 C ANISOU 2090 C LYS A1083 21828 21502 26145 -323 -862 -403 C ATOM 2091 O LYS A1083 9.023 -67.736 23.212 1.00182.25 O ANISOU 2091 O LYS A1083 21780 21484 25982 -334 -807 -372 O ATOM 2092 CB LYS A1083 8.323 -70.152 24.406 1.00180.05 C ANISOU 2092 CB LYS A1083 21547 21158 25708 -352 -967 -316 C ATOM 2093 CG LYS A1083 7.984 -71.333 25.305 1.00177.09 C ANISOU 2093 CG LYS A1083 21200 20756 25332 -363 -1064 -279 C ATOM 2094 CD LYS A1083 8.644 -72.623 24.872 1.00177.91 C ANISOU 2094 CD LYS A1083 21277 20799 25521 -354 -1105 -319 C ATOM 2095 CE LYS A1083 8.207 -73.816 25.695 1.00178.32 C ANISOU 2095 CE LYS A1083 21362 20825 25566 -368 -1199 -278 C ATOM 2096 NZ LYS A1083 8.898 -75.056 25.270 1.00177.26 N ANISOU 2096 NZ LYS A1083 21202 20630 25520 -357 -1242 -320 N ATOM 2097 N VAL A1084 11.150 -68.435 22.903 1.00183.28 N ANISOU 2097 N VAL A1084 21829 21517 26290 -305 -837 -467 N ATOM 2098 CA VAL A1084 11.577 -67.301 22.097 1.00182.14 C ANISOU 2098 CA VAL A1084 21659 21395 26152 -298 -747 -503 C ATOM 2099 C VAL A1084 10.824 -67.289 20.767 1.00181.79 C ANISOU 2099 C VAL A1084 21627 21391 26054 -307 -666 -506 C ATOM 2100 O VAL A1084 10.154 -66.309 20.447 1.00182.17 O ANISOU 2100 O VAL A1084 21697 21492 26028 -315 -604 -485 O ATOM 2101 CB VAL A1084 13.106 -67.285 21.890 1.00183.22 C ANISOU 2101 CB VAL A1084 21734 21476 26405 -278 -746 -571 C ATOM 2102 CG1 VAL A1084 13.574 -65.994 21.233 1.00182.29 C ANISOU 2102 CG1 VAL A1084 21590 21381 26291 -273 -658 -603 C ATOM 2103 CG2 VAL A1084 13.861 -67.521 23.190 1.00184.37 C ANISOU 2103 CG2 VAL A1084 21868 21574 26611 -268 -838 -570 C ATOM 2104 N LYS A1085 10.938 -68.386 20.008 1.00182.36 N ANISOU 2104 N LYS A1085 21685 21437 26165 -304 -670 -535 N ATOM 2105 CA LYS A1085 10.424 -68.455 18.648 1.00181.39 C ANISOU 2105 CA LYS A1085 21568 21344 26008 -309 -594 -550 C ATOM 2106 C LYS A1085 8.897 -68.443 18.644 1.00181.42 C ANISOU 2106 C LYS A1085 21628 21403 25900 -328 -585 -488 C ATOM 2107 O LYS A1085 8.288 -67.938 17.704 1.00180.64 O ANISOU 2107 O LYS A1085 21543 21347 25744 -334 -510 -487 O ATOM 2108 CB LYS A1085 10.985 -69.677 17.913 1.00182.05 C ANISOU 2108 CB LYS A1085 21621 21382 26167 -299 -608 -598 C ATOM 2109 CG LYS A1085 12.476 -69.630 17.599 1.00182.02 C ANISOU 2109 CG LYS A1085 21556 21329 26273 -280 -596 -669 C ATOM 2110 CD LYS A1085 12.864 -68.521 16.641 1.00180.50 C ANISOU 2110 CD LYS A1085 21340 21162 26078 -277 -495 -705 C ATOM 2111 CE LYS A1085 14.350 -68.473 16.360 1.00179.96 C ANISOU 2111 CE LYS A1085 21209 21046 26121 -260 -482 -776 C ATOM 2112 NZ LYS A1085 14.702 -67.358 15.449 1.00178.65 N ANISOU 2112 NZ LYS A1085 21022 20906 25949 -260 -382 -808 N ATOM 2113 N GLU A1086 8.292 -68.994 19.703 1.00182.25 N ANISOU 2113 N GLU A1086 21766 21507 25973 -338 -662 -438 N ATOM 2114 CA GLU A1086 6.842 -69.061 19.812 1.00181.74 C ANISOU 2114 CA GLU A1086 21754 21494 25805 -357 -661 -379 C ATOM 2115 C GLU A1086 6.279 -67.702 20.222 1.00180.79 C ANISOU 2115 C GLU A1086 21657 21426 25607 -364 -623 -344 C ATOM 2116 O GLU A1086 5.131 -67.393 19.911 1.00180.18 O ANISOU 2116 O GLU A1086 21616 21402 25442 -377 -588 -308 O ATOM 2117 CB GLU A1086 6.408 -70.174 20.767 1.00182.71 C ANISOU 2117 CB GLU A1086 21902 21596 25924 -368 -755 -339 C ATOM 2118 CG GLU A1086 6.374 -71.543 20.108 1.00184.29 C ANISOU 2118 CG GLU A1086 22097 21765 26160 -368 -779 -358 C ATOM 2119 CD GLU A1086 5.491 -72.581 20.778 1.00184.61 C ANISOU 2119 CD GLU A1086 22176 21803 26162 -385 -852 -306 C ATOM 2120 OE1 GLU A1086 4.931 -72.284 21.854 1.00185.85 O ANISOU 2120 OE1 GLU A1086 22365 21982 26266 -398 -890 -255 O ATOM 2121 OE2 GLU A1086 5.363 -73.689 20.220 1.00184.18 O ANISOU 2121 OE2 GLU A1086 22122 21727 26132 -387 -871 -319 O ATOM 2122 N ALA A1087 7.098 -66.902 20.916 1.00181.32 N ANISOU 2122 N ALA A1087 21704 21479 25711 -354 -634 -355 N ATOM 2123 CA ALA A1087 6.705 -65.566 21.336 1.00179.27 C ANISOU 2123 CA ALA A1087 21462 21265 25388 -357 -600 -327 C ATOM 2124 C ALA A1087 6.768 -64.604 20.152 1.00175.96 C ANISOU 2124 C ALA A1087 21030 20874 24952 -353 -501 -357 C ATOM 2125 O ALA A1087 5.952 -63.689 20.054 1.00176.82 O ANISOU 2125 O ALA A1087 21168 21037 24980 -361 -457 -328 O ATOM 2126 CB ALA A1087 7.574 -65.097 22.478 1.00179.90 C ANISOU 2126 CB ALA A1087 21524 21315 25514 -348 -649 -331 C ATOM 2127 N GLN A1088 7.746 -64.825 19.264 1.00172.56 N ANISOU 2127 N GLN A1088 20558 20408 24598 -342 -467 -416 N ATOM 2128 CA GLN A1088 7.924 -64.016 18.068 1.00171.02 C ANISOU 2128 CA GLN A1088 20349 20234 24396 -339 -373 -450 C ATOM 2129 C GLN A1088 6.767 -64.268 17.104 1.00170.84 C ANISOU 2129 C GLN A1088 20360 20254 24298 -350 -327 -431 C ATOM 2130 O GLN A1088 6.284 -63.339 16.458 1.00172.81 O ANISOU 2130 O GLN A1088 20625 20546 24489 -354 -257 -426 O ATOM 2131 CB GLN A1088 9.260 -64.337 17.393 1.00170.90 C ANISOU 2131 CB GLN A1088 20280 20170 24486 -324 -353 -519 C ATOM 2132 CG GLN A1088 10.482 -63.943 18.212 1.00171.31 C ANISOU 2132 CG GLN A1088 20292 20180 24617 -312 -387 -545 C ATOM 2133 CD GLN A1088 11.783 -64.341 17.558 1.00172.06 C ANISOU 2133 CD GLN A1088 20332 20225 24818 -298 -371 -614 C ATOM 2134 OE1 GLN A1088 12.697 -64.846 18.208 1.00174.45 O ANISOU 2134 OE1 GLN A1088 20603 20478 25203 -287 -431 -638 O ATOM 2135 NE2 GLN A1088 11.881 -64.118 16.257 1.00170.19 N ANISOU 2135 NE2 GLN A1088 20081 20001 24580 -299 -289 -649 N ATOM 2136 N ALA A1089 6.330 -65.531 17.028 1.00169.69 N ANISOU 2136 N ALA A1089 20226 20095 24155 -355 -370 -421 N ATOM 2137 CA ALA A1089 5.297 -65.959 16.097 1.00168.37 C ANISOU 2137 CA ALA A1089 20088 19960 23926 -365 -334 -408 C ATOM 2138 C ALA A1089 3.912 -65.570 16.610 1.00168.24 C ANISOU 2138 C ALA A1089 20122 19998 23803 -380 -341 -344 C ATOM 2139 O ALA A1089 3.019 -65.278 15.816 1.00168.88 O ANISOU 2139 O ALA A1089 20229 20122 23816 -387 -288 -331 O ATOM 2140 CB ALA A1089 5.402 -67.445 15.857 1.00167.21 C ANISOU 2140 CB ALA A1089 19933 19775 23826 -363 -380 -423 C ATOM 2141 N ALA A1090 3.743 -65.574 17.939 1.00167.75 N ANISOU 2141 N ALA A1090 20073 19935 23728 -385 -408 -305 N ATOM 2142 CA ALA A1090 2.477 -65.217 18.560 1.00167.43 C ANISOU 2142 CA ALA A1090 20078 19946 23590 -400 -421 -244 C ATOM 2143 C ALA A1090 2.206 -63.726 18.372 1.00167.93 C ANISOU 2143 C ALA A1090 20152 20055 23598 -398 -356 -238 C ATOM 2144 O ALA A1090 1.056 -63.316 18.234 1.00167.62 O ANISOU 2144 O ALA A1090 20149 20068 23472 -409 -330 -202 O ATOM 2145 CB ALA A1090 2.485 -65.597 20.020 1.00166.48 C ANISOU 2145 CB ALA A1090 19969 19810 23477 -405 -508 -209 C ATOM 2146 N ALA A1091 3.283 -62.932 18.361 1.00170.45 N ANISOU 2146 N ALA A1091 20439 20353 23971 -385 -331 -274 N ATOM 2147 CA ALA A1091 3.196 -61.488 18.211 1.00172.74 C ANISOU 2147 CA ALA A1091 20735 20679 24219 -383 -272 -272 C ATOM 2148 C ALA A1091 2.963 -61.114 16.749 1.00174.19 C ANISOU 2148 C ALA A1091 20921 20886 24379 -383 -185 -297 C ATOM 2149 O ALA A1091 2.658 -59.961 16.448 1.00176.10 O ANISOU 2149 O ALA A1091 21175 21163 24570 -384 -131 -292 O ATOM 2150 CB ALA A1091 4.443 -60.837 18.758 1.00172.77 C ANISOU 2150 CB ALA A1091 20703 20650 24293 -371 -281 -301 C ATOM 2151 N GLU A1092 3.106 -62.094 15.848 1.00175.19 N ANISOU 2151 N GLU A1092 21036 20989 24539 -383 -174 -325 N ATOM 2152 CA GLU A1092 2.922 -61.859 14.424 1.00176.05 C ANISOU 2152 CA GLU A1092 21148 21117 24628 -383 -95 -352 C ATOM 2153 C GLU A1092 1.431 -61.783 14.099 1.00175.30 C ANISOU 2153 C GLU A1092 21100 21075 24430 -394 -76 -310 C ATOM 2154 O GLU A1092 1.041 -61.164 13.110 1.00175.14 O ANISOU 2154 O GLU A1092 21094 21085 24367 -396 -7 -318 O ATOM 2155 CB GLU A1092 3.637 -62.931 13.597 1.00176.54 C ANISOU 2155 CB GLU A1092 21178 21134 24764 -376 -91 -399 C ATOM 2156 CG GLU A1092 3.873 -62.534 12.149 1.00175.74 C ANISOU 2156 CG GLU A1092 21068 21040 24664 -373 -3 -441 C ATOM 2157 CD GLU A1092 4.925 -61.461 11.915 1.00175.90 C ANISOU 2157 CD GLU A1092 21058 21050 24727 -366 48 -478 C ATOM 2158 OE1 GLU A1092 5.743 -61.219 12.828 1.00175.09 O ANISOU 2158 OE1 GLU A1092 20930 20920 24678 -360 10 -484 O ATOM 2159 OE2 GLU A1092 4.926 -60.873 10.816 1.00176.50 O ANISOU 2159 OE2 GLU A1092 21137 21143 24782 -367 125 -501 O ATOM 2160 N GLN A1093 0.606 -62.406 14.951 1.00173.11 N ANISOU 2160 N GLN A1093 20848 20810 24116 -404 -138 -264 N ATOM 2161 CA GLN A1093 -0.837 -62.425 14.768 1.00170.60 C ANISOU 2161 CA GLN A1093 20573 20542 23704 -416 -129 -222 C ATOM 2162 C GLN A1093 -1.428 -61.051 15.078 1.00167.99 C ANISOU 2162 C GLN A1093 20266 20261 23301 -418 -97 -195 C ATOM 2163 O GLN A1093 -2.606 -60.811 14.820 1.00166.78 O ANISOU 2163 O GLN A1093 20148 20155 23066 -426 -77 -165 O ATOM 2164 CB GLN A1093 -1.477 -63.516 15.632 1.00171.96 C ANISOU 2164 CB GLN A1093 20763 20712 23863 -427 -206 -183 C ATOM 2165 CG GLN A1093 -1.171 -64.935 15.168 1.00172.67 C ANISOU 2165 CG GLN A1093 20837 20760 24008 -427 -234 -205 C ATOM 2166 CD GLN A1093 -1.734 -65.265 13.806 1.00173.98 C ANISOU 2166 CD GLN A1093 21016 20942 24148 -429 -181 -221 C ATOM 2167 OE1 GLN A1093 -2.712 -64.676 13.350 1.00174.16 O ANISOU 2167 OE1 GLN A1093 21069 21013 24093 -435 -138 -200 O ATOM 2168 NE2 GLN A1093 -1.116 -66.229 13.142 1.00175.48 N ANISOU 2168 NE2 GLN A1093 21181 21090 24402 -422 -185 -259 N ATOM 2169 N LEU A1094 -0.596 -60.153 15.621 1.00166.98 N ANISOU 2169 N LEU A1094 20118 20121 23204 -410 -94 -207 N ATOM 2170 CA LEU A1094 -1.025 -58.812 15.990 1.00166.75 C ANISOU 2170 CA LEU A1094 20109 20134 23115 -410 -69 -185 C ATOM 2171 C LEU A1094 -1.250 -57.967 14.738 1.00167.36 C ANISOU 2171 C LEU A1094 20196 20237 23156 -408 16 -204 C ATOM 2172 O LEU A1094 -2.056 -57.039 14.759 1.00167.36 O ANISOU 2172 O LEU A1094 20224 20282 23082 -411 42 -179 O ATOM 2173 CB LEU A1094 0.030 -58.175 16.903 1.00164.99 C ANISOU 2173 CB LEU A1094 19859 19884 22945 -401 -93 -196 C ATOM 2174 CG LEU A1094 0.074 -58.696 18.340 1.00163.54 C ANISOU 2174 CG LEU A1094 19675 19686 22776 -403 -178 -166 C ATOM 2175 CD1 LEU A1094 1.382 -58.316 19.016 1.00162.37 C ANISOU 2175 CD1 LEU A1094 19493 19497 22706 -392 -202 -192 C ATOM 2176 CD2 LEU A1094 -1.107 -58.177 19.146 1.00162.85 C ANISOU 2176 CD2 LEU A1094 19626 19650 22597 -412 -197 -113 C ATOM 2177 N LYS A1095 -0.532 -58.303 13.657 1.00170.16 N ANISOU 2177 N LYS A1095 20528 20562 23564 -403 57 -250 N ATOM 2178 CA LYS A1095 -0.549 -57.523 12.429 1.00172.45 C ANISOU 2178 CA LYS A1095 20824 20869 23830 -401 139 -274 C ATOM 2179 C LYS A1095 -1.942 -57.535 11.803 1.00173.78 C ANISOU 2179 C LYS A1095 21035 21085 23908 -409 165 -247 C ATOM 2180 O LYS A1095 -2.469 -56.481 11.459 1.00174.55 O ANISOU 2180 O LYS A1095 21157 21219 23945 -410 210 -236 O ATOM 2181 CB LYS A1095 0.547 -57.984 11.461 1.00172.83 C ANISOU 2181 CB LYS A1095 20837 20875 23957 -395 174 -330 C ATOM 2182 CG LYS A1095 1.966 -57.608 11.868 1.00173.44 C ANISOU 2182 CG LYS A1095 20870 20910 24118 -387 170 -364 C ATOM 2183 CD LYS A1095 3.006 -57.995 10.840 1.00175.44 C ANISOU 2183 CD LYS A1095 21089 21126 24445 -382 213 -422 C ATOM 2184 CE LYS A1095 4.407 -57.585 11.239 1.00176.82 C ANISOU 2184 CE LYS A1095 21217 21261 24704 -374 210 -457 C ATOM 2185 NZ LYS A1095 5.408 -57.993 10.225 1.00175.52 N ANISOU 2185 NZ LYS A1095 21016 21061 24612 -370 253 -515 N ATOM 2186 N THR A1096 -2.548 -58.719 11.671 1.00175.25 N ANISOU 2186 N THR A1096 21233 21270 24085 -415 133 -234 N ATOM 2187 CA THR A1096 -3.897 -58.796 11.134 1.00175.31 C ANISOU 2187 CA THR A1096 21280 21321 24009 -423 152 -207 C ATOM 2188 C THR A1096 -4.830 -57.989 12.034 1.00173.70 C ANISOU 2188 C THR A1096 21104 21163 23730 -427 133 -161 C ATOM 2189 O THR A1096 -5.622 -57.172 11.561 1.00176.57 O ANISOU 2189 O THR A1096 21496 21568 24025 -429 175 -148 O ATOM 2190 CB THR A1096 -4.369 -60.249 11.019 1.00176.10 C ANISOU 2190 CB THR A1096 21385 21410 24117 -429 111 -199 C ATOM 2191 OG1 THR A1096 -4.733 -60.671 12.334 1.00178.36 O ANISOU 2191 OG1 THR A1096 21675 21699 24394 -436 39 -159 O ATOM 2192 CG2 THR A1096 -3.317 -61.170 10.440 1.00174.88 C ANISOU 2192 CG2 THR A1096 21195 21202 24048 -423 111 -244 C ATOM 2193 N THR A1097 -4.691 -58.223 13.343 1.00171.20 N ANISOU 2193 N THR A1097 20780 20838 23431 -430 68 -136 N ATOM 2194 CA THR A1097 -5.485 -57.565 14.364 1.00172.49 C ANISOU 2194 CA THR A1097 20966 21042 23530 -434 41 -93 C ATOM 2195 C THR A1097 -5.365 -56.052 14.209 1.00172.15 C ANISOU 2195 C THR A1097 20929 21022 23458 -427 91 -99 C ATOM 2196 O THR A1097 -6.372 -55.351 14.223 1.00172.19 O ANISOU 2196 O THR A1097 20964 21074 23385 -429 108 -73 O ATOM 2197 CB THR A1097 -5.062 -58.016 15.768 1.00174.59 C ANISOU 2197 CB THR A1097 21218 21286 23834 -436 -33 -74 C ATOM 2198 OG1 THR A1097 -4.785 -59.416 15.709 1.00177.92 O ANISOU 2198 OG1 THR A1097 21625 21670 24305 -440 -72 -82 O ATOM 2199 CG2 THR A1097 -6.110 -57.733 16.822 1.00172.84 C ANISOU 2199 CG2 THR A1097 21024 21107 23539 -445 -71 -24 C ATOM 2200 N ARG A1098 -4.126 -55.568 14.049 1.00172.56 N ANISOU 2200 N ARG A1098 20950 21039 23575 -418 114 -136 N ATOM 2201 CA ARG A1098 -3.860 -54.149 13.883 1.00173.04 C ANISOU 2201 CA ARG A1098 21014 21114 23618 -411 160 -145 C ATOM 2202 C ARG A1098 -4.751 -53.579 12.781 1.00174.83 C ANISOU 2202 C ARG A1098 21273 21380 23775 -413 221 -143 C ATOM 2203 O ARG A1098 -5.508 -52.647 13.027 1.00176.66 O ANISOU 2203 O ARG A1098 21531 21653 23939 -413 232 -119 O ATOM 2204 CB ARG A1098 -2.376 -53.883 13.606 1.00171.52 C ANISOU 2204 CB ARG A1098 20782 20875 23511 -403 184 -191 C ATOM 2205 CG ARG A1098 -2.083 -52.470 13.118 1.00168.89 C ANISOU 2205 CG ARG A1098 20452 20555 23162 -399 244 -206 C ATOM 2206 CD ARG A1098 -1.873 -52.343 11.617 1.00166.41 C ANISOU 2206 CD ARG A1098 20140 20235 22852 -400 318 -241 C ATOM 2207 NE ARG A1098 -0.884 -53.272 11.080 1.00165.22 N ANISOU 2207 NE ARG A1098 19954 20038 22783 -398 323 -281 N ATOM 2208 CZ ARG A1098 0.345 -53.446 11.560 1.00163.65 C ANISOU 2208 CZ ARG A1098 19714 19796 22669 -393 301 -307 C ATOM 2209 NH1 ARG A1098 0.747 -52.770 12.622 1.00162.81 N ANISOU 2209 NH1 ARG A1098 19597 19686 22578 -389 270 -296 N ATOM 2210 NH2 ARG A1098 1.156 -54.320 10.992 1.00161.95 N ANISOU 2210 NH2 ARG A1098 19467 19540 22524 -391 308 -346 N ATOM 2211 N ASN A1099 -4.663 -54.154 11.576 1.00176.27 N ANISOU 2211 N ASN A1099 21454 21549 23972 -415 260 -170 N ATOM 2212 CA ASN A1099 -5.304 -53.576 10.403 1.00176.96 C ANISOU 2212 CA ASN A1099 21570 21665 24002 -415 323 -176 C ATOM 2213 C ASN A1099 -6.743 -54.066 10.220 1.00176.60 C ANISOU 2213 C ASN A1099 21560 21659 23882 -422 311 -144 C ATOM 2214 O ASN A1099 -7.301 -53.922 9.134 1.00176.10 O ANISOU 2214 O ASN A1099 21519 21613 23777 -423 358 -151 O ATOM 2215 CB ASN A1099 -4.478 -53.774 9.127 1.00177.64 C ANISOU 2215 CB ASN A1099 21639 21719 24136 -413 379 -223 C ATOM 2216 CG ASN A1099 -3.976 -55.190 8.936 1.00178.39 C ANISOU 2216 CG ASN A1099 21709 21777 24296 -414 353 -244 C ATOM 2217 OD1 ASN A1099 -2.867 -55.392 8.449 1.00178.19 O ANISOU 2217 OD1 ASN A1099 21652 21712 24339 -410 376 -285 O ATOM 2218 ND2 ASN A1099 -4.773 -56.177 9.313 1.00179.74 N ANISOU 2218 ND2 ASN A1099 21892 21956 24444 -419 305 -217 N ATOM 2219 N ALA A1100 -7.360 -54.627 11.264 1.00177.52 N ANISOU 2219 N ALA A1100 21682 21789 23979 -427 250 -108 N ATOM 2220 CA ALA A1100 -8.757 -55.008 11.114 1.00178.98 C ANISOU 2220 CA ALA A1100 21900 22015 24091 -435 240 -77 C ATOM 2221 C ALA A1100 -9.678 -54.180 12.012 1.00180.96 C ANISOU 2221 C ALA A1100 22173 22312 24271 -436 221 -38 C ATOM 2222 O ALA A1100 -10.868 -54.064 11.721 1.00183.55 O ANISOU 2222 O ALA A1100 22532 22681 24528 -440 230 -17 O ATOM 2223 CB ALA A1100 -8.946 -56.498 11.277 1.00178.10 C ANISOU 2223 CB ALA A1100 21781 21885 24005 -443 194 -69 C ATOM 2224 N TYR A1101 -9.118 -53.573 13.070 1.00182.76 N ANISOU 2224 N TYR A1101 22387 22534 24519 -433 195 -31 N ATOM 2225 CA TYR A1101 -9.905 -52.847 14.058 1.00184.66 C ANISOU 2225 CA TYR A1101 22646 22817 24698 -433 170 5 C ATOM 2226 C TYR A1101 -9.250 -51.516 14.418 1.00185.01 C ANISOU 2226 C TYR A1101 22683 22861 24752 -423 188 -5 C ATOM 2227 O TYR A1101 -9.906 -50.474 14.436 1.00185.98 O ANISOU 2227 O TYR A1101 22828 23022 24813 -419 209 8 O ATOM 2228 CB TYR A1101 -10.046 -53.677 15.336 1.00185.43 C ANISOU 2228 CB TYR A1101 22737 22912 24808 -442 98 34 C ATOM 2229 CG TYR A1101 -10.769 -54.986 15.156 1.00184.29 C ANISOU 2229 CG TYR A1101 22601 22771 24651 -454 72 50 C ATOM 2230 CD1 TYR A1101 -12.147 -55.059 15.276 1.00183.95 C ANISOU 2230 CD1 TYR A1101 22586 22776 24530 -463 63 83 C ATOM 2231 CD2 TYR A1101 -10.078 -56.152 14.864 1.00183.35 C ANISOU 2231 CD2 TYR A1101 22461 22606 24599 -457 54 31 C ATOM 2232 CE1 TYR A1101 -12.824 -56.257 15.114 1.00184.65 C ANISOU 2232 CE1 TYR A1101 22683 22867 24609 -475 39 98 C ATOM 2233 CE2 TYR A1101 -10.739 -57.359 14.700 1.00184.43 C ANISOU 2233 CE2 TYR A1101 22607 22744 24726 -468 28 45 C ATOM 2234 CZ TYR A1101 -12.117 -57.410 14.824 1.00185.70 C ANISOU 2234 CZ TYR A1101 22796 22952 24808 -478 21 80 C ATOM 2235 OH TYR A1101 -12.778 -58.593 14.661 1.00188.02 O ANISOU 2235 OH TYR A1101 23099 23248 25093 -491 -5 94 O ATOM 2236 N ILE A1102 -7.949 -51.576 14.713 1.00184.43 N ANISOU 2236 N ILE A1102 22577 22742 24756 -418 178 -29 N ATOM 2237 CA ILE A1102 -7.210 -50.458 15.272 1.00185.29 C ANISOU 2237 CA ILE A1102 22674 22844 24885 -410 183 -37 C ATOM 2238 C ILE A1102 -7.078 -49.366 14.217 1.00187.51 C ANISOU 2238 C ILE A1102 22964 23132 25148 -404 252 -60 C ATOM 2239 O ILE A1102 -7.490 -48.235 14.453 1.00188.53 O ANISOU 2239 O ILE A1102 23112 23292 25229 -399 265 -47 O ATOM 2240 CB ILE A1102 -5.841 -50.927 15.806 1.00185.68 C ANISOU 2240 CB ILE A1102 22684 22840 25028 -406 152 -58 C ATOM 2241 CG1 ILE A1102 -5.965 -52.193 16.660 1.00185.99 C ANISOU 2241 CG1 ILE A1102 22715 22866 25088 -414 85 -38 C ATOM 2242 CG2 ILE A1102 -5.122 -49.805 16.540 1.00186.12 C ANISOU 2242 CG2 ILE A1102 22726 22888 25104 -398 148 -63 C ATOM 2243 CD1 ILE A1102 -7.260 -52.303 17.443 1.00185.29 C ANISOU 2243 CD1 ILE A1102 22656 22824 24922 -421 47 8 C ATOM 2244 N GLN A1103 -6.532 -49.729 13.050 1.00189.23 N ANISOU 2244 N GLN A1103 23172 23323 25404 -405 296 -93 N ATOM 2245 CA GLN A1103 -6.249 -48.769 11.994 1.00189.88 C ANISOU 2245 CA GLN A1103 23263 23406 25478 -401 363 -118 C ATOM 2246 C GLN A1103 -7.509 -47.983 11.632 1.00190.03 C ANISOU 2246 C GLN A1103 23324 23475 25404 -401 388 -96 C ATOM 2247 O GLN A1103 -7.416 -46.853 11.159 1.00192.58 O ANISOU 2247 O GLN A1103 23659 23807 25705 -397 432 -106 O ATOM 2248 CB GLN A1103 -5.627 -49.450 10.772 1.00191.99 C ANISOU 2248 CB GLN A1103 23516 23639 25792 -404 405 -155 C ATOM 2249 CG GLN A1103 -5.066 -48.467 9.752 1.00196.47 C ANISOU 2249 CG GLN A1103 24087 24199 26365 -402 474 -186 C ATOM 2250 CD GLN A1103 -4.347 -49.121 8.596 1.00199.75 C ANISOU 2250 CD GLN A1103 24485 24580 26830 -405 516 -225 C ATOM 2251 OE1 GLN A1103 -4.013 -50.304 8.628 1.00202.64 O ANISOU 2251 OE1 GLN A1103 24829 24921 27245 -406 490 -236 O ATOM 2252 NE2 GLN A1103 -4.092 -48.342 7.558 1.00200.33 N ANISOU 2252 NE2 GLN A1103 24569 24653 26893 -406 581 -248 N ATOM 2253 N LYS A1104 -8.681 -48.584 11.870 1.00189.43 N ANISOU 2253 N LYS A1104 23269 23431 25273 -405 359 -66 N ATOM 2254 CA LYS A1104 -9.949 -47.927 11.598 1.00188.56 C ANISOU 2254 CA LYS A1104 23198 23371 25076 -405 376 -45 C ATOM 2255 C LYS A1104 -10.270 -46.931 12.711 1.00189.92 C ANISOU 2255 C LYS A1104 23377 23572 25211 -399 349 -20 C ATOM 2256 O LYS A1104 -10.906 -45.908 12.460 1.00194.51 O ANISOU 2256 O LYS A1104 23985 24187 25735 -394 374 -14 O ATOM 2257 CB LYS A1104 -11.069 -48.955 11.407 1.00187.86 C ANISOU 2257 CB LYS A1104 23126 23306 24945 -412 356 -25 C ATOM 2258 CG LYS A1104 -10.986 -49.776 10.126 1.00187.53 C ANISOU 2258 CG LYS A1104 23086 23243 24921 -416 390 -48 C ATOM 2259 CD LYS A1104 -12.214 -50.629 9.863 1.00188.12 C ANISOU 2259 CD LYS A1104 23183 23346 24947 -423 374 -28 C ATOM 2260 CE LYS A1104 -13.429 -49.836 9.425 1.00187.41 C ANISOU 2260 CE LYS A1104 23132 23304 24771 -420 399 -12 C ATOM 2261 NZ LYS A1104 -13.230 -49.200 8.101 1.00186.68 N ANISOU 2261 NZ LYS A1104 23055 23205 24669 -415 463 -40 N ATOM 2262 N TYR A1105 -9.815 -47.233 13.933 1.00189.80 N ANISOU 2262 N TYR A1105 23340 23545 25232 -399 297 -8 N ATOM 2263 CA TYR A1105 -10.037 -46.360 15.076 1.00189.57 C ANISOU 2263 CA TYR A1105 23315 23541 25174 -394 267 13 C ATOM 2264 C TYR A1105 -8.950 -45.287 15.154 1.00188.81 C ANISOU 2264 C TYR A1105 23202 23420 25119 -385 288 -9 C ATOM 2265 O TYR A1105 -9.073 -44.344 15.933 1.00187.51 O ANISOU 2265 O TYR A1105 23043 23275 24929 -378 274 4 O ATOM 2266 CB TYR A1105 -10.140 -47.169 16.375 1.00190.67 C ANISOU 2266 CB TYR A1105 23441 23680 25325 -399 199 39 C ATOM 2267 CG TYR A1105 -10.204 -46.330 17.628 1.00193.19 C ANISOU 2267 CG TYR A1105 23761 24020 25623 -393 165 59 C ATOM 2268 CD1 TYR A1105 -11.363 -45.654 17.980 1.00194.40 C ANISOU 2268 CD1 TYR A1105 23941 24226 25695 -390 161 84 C ATOM 2269 CD2 TYR A1105 -9.098 -46.191 18.453 1.00194.87 C ANISOU 2269 CD2 TYR A1105 23947 24199 25897 -388 137 50 C ATOM 2270 CE1 TYR A1105 -11.425 -44.869 19.121 1.00194.09 C ANISOU 2270 CE1 TYR A1105 23903 24207 25636 -384 131 101 C ATOM 2271 CE2 TYR A1105 -9.143 -45.410 19.598 1.00193.85 C ANISOU 2271 CE2 TYR A1105 23819 24087 25748 -381 106 68 C ATOM 2272 CZ TYR A1105 -10.311 -44.747 19.935 1.00192.47 C ANISOU 2272 CZ TYR A1105 23672 23966 25491 -379 103 93 C ATOM 2273 OH TYR A1105 -10.365 -43.978 21.062 1.00188.32 O ANISOU 2273 OH TYR A1105 23148 23459 24945 -372 72 108 O ATOM 2274 N LEU A1106 -7.901 -45.430 14.331 1.00189.98 N ANISOU 2274 N LEU A1106 23330 23524 25328 -385 324 -43 N ATOM 2275 CA LEU A1106 -6.724 -44.571 14.365 1.00190.47 C ANISOU 2275 CA LEU A1106 23371 23557 25443 -380 345 -68 C ATOM 2276 C LEU A1106 -7.121 -43.091 14.261 1.00189.59 C ANISOU 2276 C LEU A1106 23284 23475 25277 -373 374 -62 C ATOM 2277 O LEU A1106 -8.213 -42.814 13.731 1.00187.80 O ANISOU 2277 O LEU A1106 23092 23286 24979 -373 394 -49 O ATOM 2278 CB LEU A1106 -5.777 -44.980 13.230 1.00192.70 C ANISOU 2278 CB LEU A1106 23634 23798 25786 -383 391 -107 C ATOM 2279 CG LEU A1106 -4.673 -43.986 12.860 1.00191.70 C ANISOU 2279 CG LEU A1106 23491 23643 25703 -380 433 -137 C ATOM 2280 CD1 LEU A1106 -3.635 -43.873 13.968 1.00190.67 C ANISOU 2280 CD1 LEU A1106 23325 23482 25639 -375 393 -142 C ATOM 2281 CD2 LEU A1106 -4.006 -44.390 11.554 1.00190.17 C ANISOU 2281 CD2 LEU A1106 23286 23419 25551 -386 487 -173 C ATOM 2282 N GLU A 219 -8.927 -44.361 11.656 1.00170.30 N ANISOU 2282 N GLU A 219 20896 21066 22745 -386 447 -66 N ATOM 2283 CA GLU A 219 -9.241 -43.079 10.969 1.00169.56 C ANISOU 2283 CA GLU A 219 20830 20992 22602 -381 495 -71 C ATOM 2284 C GLU A 219 -10.649 -42.621 11.348 1.00166.57 C ANISOU 2284 C GLU A 219 20485 20667 22137 -377 475 -40 C ATOM 2285 O GLU A 219 -11.298 -41.912 10.581 1.00168.11 O ANISOU 2285 O GLU A 219 20712 20885 22278 -375 511 -40 O ATOM 2286 CB GLU A 219 -9.068 -43.230 9.456 1.00174.15 C ANISOU 2286 CB GLU A 219 21424 21558 23188 -386 555 -98 C ATOM 2287 CG GLU A 219 -7.624 -43.432 9.028 1.00177.96 C ANISOU 2287 CG GLU A 219 21873 21990 23755 -390 582 -133 C ATOM 2288 CD GLU A 219 -7.394 -43.581 7.532 1.00181.96 C ANISOU 2288 CD GLU A 219 22390 22481 24266 -396 644 -162 C ATOM 2289 OE1 GLU A 219 -8.379 -43.795 6.795 1.00185.20 O ANISOU 2289 OE1 GLU A 219 22832 22916 24618 -397 660 -153 O ATOM 2290 OE2 GLU A 219 -6.226 -43.483 7.107 1.00184.72 O ANISOU 2290 OE2 GLU A 219 22715 22793 24677 -399 676 -193 O ATOM 2291 N ARG A 220 -11.109 -43.028 12.538 1.00163.16 N ANISOU 2291 N ARG A 220 20046 20254 21693 -377 419 -13 N ATOM 2292 CA ARG A 220 -12.405 -42.605 13.048 1.00161.44 C ANISOU 2292 CA ARG A 220 19855 20088 21396 -373 397 16 C ATOM 2293 C ARG A 220 -12.215 -41.551 14.136 1.00160.63 C ANISOU 2293 C ARG A 220 19748 19998 21287 -364 373 27 C ATOM 2294 O ARG A 220 -12.948 -40.565 14.175 1.00161.24 O ANISOU 2294 O ARG A 220 19850 20110 21304 -357 380 37 O ATOM 2295 CB ARG A 220 -13.223 -43.794 13.565 1.00162.19 C ANISOU 2295 CB ARG A 220 19950 20203 21472 -381 354 41 C ATOM 2296 CG ARG A 220 -14.614 -43.415 14.059 1.00162.66 C ANISOU 2296 CG ARG A 220 20034 20319 21449 -379 333 70 C ATOM 2297 CD ARG A 220 -15.515 -44.599 14.357 1.00164.81 C ANISOU 2297 CD ARG A 220 20310 20613 21698 -389 299 93 C ATOM 2298 NE ARG A 220 -15.864 -45.353 13.159 1.00167.83 N ANISOU 2298 NE ARG A 220 20704 20989 22075 -395 328 82 N ATOM 2299 CZ ARG A 220 -16.692 -46.393 13.123 1.00167.95 C ANISOU 2299 CZ ARG A 220 20725 21020 22068 -405 307 98 C ATOM 2300 NH1 ARG A 220 -17.278 -46.820 14.230 1.00167.39 N ANISOU 2300 NH1 ARG A 220 20650 20975 21976 -411 258 127 N ATOM 2301 NH2 ARG A 220 -16.933 -47.004 11.977 1.00167.85 N ANISOU 2301 NH2 ARG A 220 20723 21000 22054 -409 335 85 N ATOM 2302 N ALA A 221 -11.236 -41.780 15.021 1.00159.66 N ANISOU 2302 N ALA A 221 19593 19844 21224 -364 341 24 N ATOM 2303 CA ALA A 221 -10.921 -40.839 16.084 1.00156.93 C ANISOU 2303 CA ALA A 221 19241 19505 20881 -355 316 32 C ATOM 2304 C ALA A 221 -10.247 -39.600 15.499 1.00154.01 C ANISOU 2304 C ALA A 221 18875 19119 20525 -348 360 9 C ATOM 2305 O ALA A 221 -10.477 -38.490 15.972 1.00154.02 O ANISOU 2305 O ALA A 221 18887 19141 20493 -339 355 16 O ATOM 2306 CB ALA A 221 -10.063 -41.498 17.136 1.00157.86 C ANISOU 2306 CB ALA A 221 19325 19592 21061 -357 269 34 C ATOM 2307 N ARG A 222 -9.422 -39.808 14.463 1.00151.91 N ANISOU 2307 N ARG A 222 18597 18814 20306 -354 403 -20 N ATOM 2308 CA ARG A 222 -8.748 -38.724 13.767 1.00151.26 C ANISOU 2308 CA ARG A 222 18519 18713 20239 -351 451 -43 C ATOM 2309 C ARG A 222 -9.773 -37.900 12.991 1.00149.99 C ANISOU 2309 C ARG A 222 18400 18589 20000 -347 485 -36 C ATOM 2310 O ARG A 222 -9.625 -36.687 12.866 1.00151.19 O ANISOU 2310 O ARG A 222 18565 18744 20138 -342 506 -42 O ATOM 2311 CB ARG A 222 -7.671 -39.269 12.824 1.00154.38 C ANISOU 2311 CB ARG A 222 18893 19062 20703 -359 491 -75 C ATOM 2312 CG ARG A 222 -6.855 -38.194 12.118 1.00156.99 C ANISOU 2312 CG ARG A 222 19224 19370 21056 -360 542 -100 C ATOM 2313 CD ARG A 222 -5.966 -38.745 11.020 1.00161.45 C ANISOU 2313 CD ARG A 222 19773 19896 21677 -369 589 -132 C ATOM 2314 NE ARG A 222 -4.952 -39.655 11.536 1.00167.94 N ANISOU 2314 NE ARG A 222 20551 20680 22581 -372 562 -146 N ATOM 2315 CZ ARG A 222 -4.042 -40.284 10.798 1.00172.13 C ANISOU 2315 CZ ARG A 222 21057 21172 23173 -379 593 -177 C ATOM 2316 NH1 ARG A 222 -4.005 -40.108 9.487 1.00172.98 N ANISOU 2316 NH1 ARG A 222 21181 21275 23269 -386 653 -196 N ATOM 2317 NH2 ARG A 222 -3.169 -41.090 11.376 1.00173.34 N ANISOU 2317 NH2 ARG A 222 21169 21291 23399 -379 561 -189 N ATOM 2318 N SER A 223 -10.805 -38.578 12.474 1.00148.73 N ANISOU 2318 N SER A 223 18262 18455 19793 -351 488 -25 N ATOM 2319 CA SER A 223 -11.855 -37.931 11.704 1.00147.10 C ANISOU 2319 CA SER A 223 18096 18283 19513 -348 516 -20 C ATOM 2320 C SER A 223 -12.688 -37.014 12.597 1.00145.08 C ANISOU 2320 C SER A 223 17857 18068 19198 -336 485 3 C ATOM 2321 O SER A 223 -13.133 -35.958 12.152 1.00145.07 O ANISOU 2321 O SER A 223 17884 18085 19151 -330 509 1 O ATOM 2322 CB SER A 223 -12.718 -38.945 10.996 1.00148.06 C ANISOU 2322 CB SER A 223 18233 18420 19604 -354 522 -15 C ATOM 2323 OG SER A 223 -13.688 -38.305 10.178 1.00149.03 O ANISOU 2323 OG SER A 223 18395 18571 19656 -350 551 -12 O ATOM 2324 N THR A 224 -12.884 -37.427 13.857 1.00142.58 N ANISOU 2324 N THR A 224 17523 17767 18884 -335 432 23 N ATOM 2325 CA THR A 224 -13.711 -36.692 14.803 1.00140.08 C ANISOU 2325 CA THR A 224 17219 17493 18511 -324 399 44 C ATOM 2326 C THR A 224 -12.981 -35.439 15.284 1.00139.74 C ANISOU 2326 C THR A 224 17171 17437 18487 -314 399 36 C ATOM 2327 O THR A 224 -13.619 -34.432 15.585 1.00140.79 O ANISOU 2327 O THR A 224 17323 17602 18568 -304 393 44 O ATOM 2328 CB THR A 224 -14.184 -37.594 15.953 1.00138.56 C ANISOU 2328 CB THR A 224 17013 17321 18312 -328 344 68 C ATOM 2329 OG1 THR A 224 -14.767 -38.765 15.381 1.00137.47 O ANISOU 2329 OG1 THR A 224 16879 17189 18163 -338 347 74 O ATOM 2330 CG2 THR A 224 -15.194 -36.926 16.861 1.00137.38 C ANISOU 2330 CG2 THR A 224 16878 17222 18097 -318 312 90 C ATOM 2331 N LEU A 225 -11.645 -35.509 15.350 1.00137.81 N ANISOU 2331 N LEU A 225 16897 17145 18317 -318 406 18 N ATOM 2332 CA LEU A 225 -10.841 -34.381 15.797 1.00136.01 C ANISOU 2332 CA LEU A 225 16661 16901 18116 -310 406 9 C ATOM 2333 C LEU A 225 -10.894 -33.252 14.770 1.00136.89 C ANISOU 2333 C LEU A 225 16800 17012 18201 -307 456 -5 C ATOM 2334 O LEU A 225 -10.907 -32.082 15.143 1.00137.25 O ANISOU 2334 O LEU A 225 16855 17067 18227 -297 451 -4 O ATOM 2335 CB LEU A 225 -9.399 -34.833 16.051 1.00135.44 C ANISOU 2335 CB LEU A 225 16549 16777 18135 -316 402 -9 C ATOM 2336 CG LEU A 225 -9.100 -35.345 17.460 1.00135.42 C ANISOU 2336 CG LEU A 225 16520 16771 18162 -313 343 5 C ATOM 2337 CD1 LEU A 225 -7.618 -35.650 17.618 1.00135.75 C ANISOU 2337 CD1 LEU A 225 16523 16758 18296 -317 341 -17 C ATOM 2338 CD2 LEU A 225 -9.549 -34.344 18.516 1.00134.80 C ANISOU 2338 CD2 LEU A 225 16452 16725 18043 -300 309 21 C ATOM 2339 N GLN A 226 -10.936 -33.615 13.482 1.00137.82 N ANISOU 2339 N GLN A 226 16930 17117 18317 -316 502 -19 N ATOM 2340 CA GLN A 226 -10.958 -32.640 12.403 1.00137.80 C ANISOU 2340 CA GLN A 226 16958 17111 18290 -316 552 -32 C ATOM 2341 C GLN A 226 -12.312 -31.935 12.357 1.00137.96 C ANISOU 2341 C GLN A 226 17016 17178 18223 -306 545 -16 C ATOM 2342 O GLN A 226 -12.406 -30.814 11.862 1.00139.06 O ANISOU 2342 O GLN A 226 17182 17321 18335 -301 570 -22 O ATOM 2343 CB GLN A 226 -10.625 -33.294 11.061 1.00140.01 C ANISOU 2343 CB GLN A 226 17242 17366 18592 -329 602 -51 C ATOM 2344 CG GLN A 226 -9.167 -33.715 10.931 1.00143.02 C ANISOU 2344 CG GLN A 226 17585 17696 19060 -339 619 -75 C ATOM 2345 CD GLN A 226 -8.787 -34.126 9.528 1.00146.23 C ANISOU 2345 CD GLN A 226 17999 18078 19485 -351 676 -97 C ATOM 2346 OE1 GLN A 226 -9.104 -33.450 8.551 1.00149.07 O ANISOU 2346 OE1 GLN A 226 18392 18443 19805 -353 717 -103 O ATOM 2347 NE2 GLN A 226 -8.083 -35.241 9.417 1.00147.11 N ANISOU 2347 NE2 GLN A 226 18079 18160 19657 -359 677 -111 N ATOM 2348 N LYS A 227 -13.351 -32.601 12.876 1.00138.19 N ANISOU 2348 N LYS A 227 17050 17245 18211 -302 510 5 N ATOM 2349 CA LYS A 227 -14.693 -32.041 12.916 1.00138.62 C ANISOU 2349 CA LYS A 227 17136 17348 18184 -292 498 20 C ATOM 2350 C LYS A 227 -14.775 -30.974 14.005 1.00139.36 C ANISOU 2350 C LYS A 227 17229 17461 18261 -278 465 28 C ATOM 2351 O LYS A 227 -15.391 -29.930 13.801 1.00140.48 O ANISOU 2351 O LYS A 227 17400 17626 18352 -267 472 29 O ATOM 2352 CB LYS A 227 -15.739 -33.140 13.133 1.00139.95 C ANISOU 2352 CB LYS A 227 17307 17551 18319 -295 472 37 C ATOM 2353 CG LYS A 227 -15.979 -34.058 11.942 1.00142.10 C ANISOU 2353 CG LYS A 227 17589 17813 18588 -306 505 30 C ATOM 2354 CD LYS A 227 -16.992 -35.147 12.220 1.00144.68 C ANISOU 2354 CD LYS A 227 17916 18172 18884 -310 476 48 C ATOM 2355 CE LYS A 227 -17.149 -36.115 11.067 1.00147.56 C ANISOU 2355 CE LYS A 227 18289 18523 19254 -320 506 39 C ATOM 2356 NZ LYS A 227 -18.058 -37.234 11.409 1.00150.70 N ANISOU 2356 NZ LYS A 227 18683 18949 19628 -326 475 57 N ATOM 2357 N GLU A 228 -14.142 -31.247 15.152 1.00139.67 N ANISOU 2357 N GLU A 228 17236 17489 18342 -277 429 34 N ATOM 2358 CA GLU A 228 -14.190 -30.360 16.305 1.00139.15 C ANISOU 2358 CA GLU A 228 17166 17442 18264 -264 392 43 C ATOM 2359 C GLU A 228 -13.285 -29.149 16.082 1.00135.74 C ANISOU 2359 C GLU A 228 16735 16979 17860 -259 415 26 C ATOM 2360 O GLU A 228 -13.529 -28.087 16.650 1.00136.73 O ANISOU 2360 O GLU A 228 16871 17123 17957 -245 397 30 O ATOM 2361 CB GLU A 228 -13.810 -31.107 17.585 1.00144.13 C ANISOU 2361 CB GLU A 228 17763 18070 18929 -266 344 55 C ATOM 2362 CG GLU A 228 -14.882 -32.069 18.069 1.00149.37 C ANISOU 2362 CG GLU A 228 18429 18773 19551 -269 313 77 C ATOM 2363 CD GLU A 228 -14.483 -32.954 19.239 1.00153.42 C ANISOU 2363 CD GLU A 228 18912 19279 20101 -274 267 90 C ATOM 2364 OE1 GLU A 228 -13.270 -33.052 19.526 1.00156.28 O ANISOU 2364 OE1 GLU A 228 19249 19599 20532 -277 262 79 O ATOM 2365 OE2 GLU A 228 -15.387 -33.547 19.861 1.00154.93 O ANISOU 2365 OE2 GLU A 228 19106 19507 20252 -276 235 110 O ATOM 2366 N VAL A 229 -12.242 -29.320 15.259 1.00130.36 N ANISOU 2366 N VAL A 229 16044 16252 17235 -271 454 7 N ATOM 2367 CA VAL A 229 -11.318 -28.237 14.956 1.00126.30 C ANISOU 2367 CA VAL A 229 15530 15706 16753 -270 480 -10 C ATOM 2368 C VAL A 229 -11.938 -27.330 13.894 1.00126.65 C ANISOU 2368 C VAL A 229 15617 15763 16743 -267 518 -15 C ATOM 2369 O VAL A 229 -11.807 -26.110 13.973 1.00127.91 O ANISOU 2369 O VAL A 229 15790 15920 16889 -259 521 -18 O ATOM 2370 CB VAL A 229 -9.922 -28.751 14.548 1.00123.53 C ANISOU 2370 CB VAL A 229 15149 15302 16486 -284 507 -30 C ATOM 2371 CG1 VAL A 229 -9.033 -27.639 14.005 1.00121.75 C ANISOU 2371 CG1 VAL A 229 14927 15043 16288 -287 544 -49 C ATOM 2372 CG2 VAL A 229 -9.227 -29.458 15.701 1.00122.01 C ANISOU 2372 CG2 VAL A 229 14914 15093 16350 -284 464 -27 C ATOM 2373 N HIS A 230 -12.618 -27.935 12.911 1.00127.00 N ANISOU 2373 N HIS A 230 15682 15818 16754 -274 544 -15 N ATOM 2374 CA HIS A 230 -13.302 -27.180 11.872 1.00128.31 C ANISOU 2374 CA HIS A 230 15891 15996 16863 -272 577 -18 C ATOM 2375 C HIS A 230 -14.446 -26.370 12.479 1.00127.25 C ANISOU 2375 C HIS A 230 15781 15909 16660 -253 543 -3 C ATOM 2376 O HIS A 230 -14.780 -25.299 11.977 1.00129.32 O ANISOU 2376 O HIS A 230 16075 16176 16884 -247 559 -7 O ATOM 2377 CB HIS A 230 -13.776 -28.097 10.735 1.00131.98 C ANISOU 2377 CB HIS A 230 16373 16463 17310 -282 608 -22 C ATOM 2378 CG HIS A 230 -14.505 -27.379 9.647 1.00134.26 C ANISOU 2378 CG HIS A 230 16708 16764 17540 -279 640 -25 C ATOM 2379 ND1 HIS A 230 -13.851 -26.607 8.705 1.00135.97 N ANISOU 2379 ND1 HIS A 230 16945 16950 17770 -287 686 -41 N ATOM 2380 CD2 HIS A 230 -15.821 -27.303 9.351 1.00133.56 C ANISOU 2380 CD2 HIS A 230 16652 16714 17380 -271 632 -15 C ATOM 2381 CE1 HIS A 230 -14.732 -26.089 7.874 1.00135.17 C ANISOU 2381 CE1 HIS A 230 16887 16866 17605 -282 703 -40 C ATOM 2382 NE2 HIS A 230 -15.949 -26.501 8.249 1.00134.34 N ANISOU 2382 NE2 HIS A 230 16789 16803 17449 -272 670 -25 N ATOM 2383 N ALA A 231 -15.033 -26.895 13.561 1.00124.63 N ANISOU 2383 N ALA A 231 15433 15609 16312 -246 496 13 N ATOM 2384 CA ALA A 231 -16.101 -26.216 14.276 1.00123.51 C ANISOU 2384 CA ALA A 231 15306 15514 16108 -229 461 26 C ATOM 2385 C ALA A 231 -15.539 -25.041 15.073 1.00122.31 C ANISOU 2385 C ALA A 231 15148 15353 15970 -217 441 23 C ATOM 2386 O ALA A 231 -16.219 -24.033 15.258 1.00121.94 O ANISOU 2386 O ALA A 231 15124 15333 15874 -202 428 25 O ATOM 2387 CB ALA A 231 -16.828 -27.193 15.168 1.00124.19 C ANISOU 2387 CB ALA A 231 15376 15636 16176 -228 420 44 C ATOM 2388 N ALA A 232 -14.292 -25.184 15.539 1.00121.74 N ANISOU 2388 N ALA A 232 15043 15243 15968 -224 438 16 N ATOM 2389 CA ALA A 232 -13.641 -24.169 16.351 1.00119.56 C ANISOU 2389 CA ALA A 232 14756 14955 15715 -213 418 13 C ATOM 2390 C ALA A 232 -13.249 -22.975 15.485 1.00118.33 C ANISOU 2390 C ALA A 232 14625 14775 15558 -213 454 -1 C ATOM 2391 O ALA A 232 -13.455 -21.831 15.884 1.00118.88 O ANISOU 2391 O ALA A 232 14710 14857 15604 -199 438 -1 O ATOM 2392 CB ALA A 232 -12.446 -24.757 17.062 1.00120.28 C ANISOU 2392 CB ALA A 232 14806 15012 15884 -221 403 10 C ATOM 2393 N LYS A 233 -12.695 -23.259 14.298 1.00116.83 N ANISOU 2393 N LYS A 233 14443 14552 15397 -230 504 -14 N ATOM 2394 CA LYS A 233 -12.240 -22.228 13.378 1.00116.77 C ANISOU 2394 CA LYS A 233 14459 14517 15391 -234 544 -27 C ATOM 2395 C LYS A 233 -13.433 -21.434 12.852 1.00114.75 C ANISOU 2395 C LYS A 233 14251 14294 15057 -223 547 -22 C ATOM 2396 O LYS A 233 -13.328 -20.226 12.654 1.00113.54 O ANISOU 2396 O LYS A 233 14119 14132 14889 -217 554 -28 O ATOM 2397 CB LYS A 233 -11.424 -22.833 12.231 1.00120.72 C ANISOU 2397 CB LYS A 233 14954 14977 15936 -256 598 -42 C ATOM 2398 CG LYS A 233 -10.010 -23.270 12.595 1.00124.84 C ANISOU 2398 CG LYS A 233 15432 15457 16545 -267 603 -54 C ATOM 2399 CD LYS A 233 -9.151 -23.630 11.401 1.00127.52 C ANISOU 2399 CD LYS A 233 15769 15757 16928 -288 660 -73 C ATOM 2400 CE LYS A 233 -7.742 -24.029 11.788 1.00130.32 C ANISOU 2400 CE LYS A 233 16076 16068 17370 -298 663 -87 C ATOM 2401 NZ LYS A 233 -6.889 -24.265 10.598 1.00132.25 N ANISOU 2401 NZ LYS A 233 16318 16275 17656 -318 723 -108 N ATOM 2402 N SER A 234 -14.560 -22.126 12.641 1.00113.54 N ANISOU 2402 N SER A 234 14111 14177 14852 -220 540 -13 N ATOM 2403 CA SER A 234 -15.783 -21.507 12.150 1.00112.81 C ANISOU 2403 CA SER A 234 14061 14118 14684 -208 539 -9 C ATOM 2404 C SER A 234 -16.319 -20.504 13.169 1.00111.41 C ANISOU 2404 C SER A 234 13888 13970 14472 -186 495 -3 C ATOM 2405 O SER A 234 -16.839 -19.456 12.793 1.00113.28 O ANISOU 2405 O SER A 234 14160 14217 14665 -175 497 -6 O ATOM 2406 CB SER A 234 -16.822 -22.540 11.798 1.00112.19 C ANISOU 2406 CB SER A 234 13990 14070 14565 -209 537 -1 C ATOM 2407 OG SER A 234 -16.430 -23.276 10.648 1.00113.79 O ANISOU 2407 OG SER A 234 14199 14245 14791 -227 583 -10 O ATOM 2408 N ALA A 235 -16.183 -20.843 14.456 1.00108.84 N ANISOU 2408 N ALA A 235 13528 13659 14166 -179 453 6 N ATOM 2409 CA ALA A 235 -16.611 -19.978 15.543 1.00105.80 C ANISOU 2409 CA ALA A 235 13143 13302 13753 -159 409 11 C ATOM 2410 C ALA A 235 -15.590 -18.862 15.755 1.00104.36 C ANISOU 2410 C ALA A 235 12958 13085 13610 -156 411 1 C ATOM 2411 O ALA A 235 -15.954 -17.754 16.144 1.00104.22 O ANISOU 2411 O ALA A 235 12956 13083 13561 -139 389 0 O ATOM 2412 CB ALA A 235 -16.814 -20.792 16.797 1.00105.68 C ANISOU 2412 CB ALA A 235 13094 13314 13744 -155 367 24 C ATOM 2413 N ALA A 236 -14.314 -19.169 15.490 1.00103.09 N ANISOU 2413 N ALA A 236 12775 12877 13518 -173 437 -7 N ATOM 2414 CA ALA A 236 -13.223 -18.228 15.688 1.00101.86 C ANISOU 2414 CA ALA A 236 12610 12683 13409 -174 442 -17 C ATOM 2415 C ALA A 236 -13.344 -17.065 14.707 1.00100.57 C ANISOU 2415 C ALA A 236 12489 12508 13217 -173 471 -25 C ATOM 2416 O ALA A 236 -12.964 -15.941 15.030 1.00100.38 O ANISOU 2416 O ALA A 236 12470 12470 13200 -165 460 -30 O ATOM 2417 CB ALA A 236 -11.895 -18.932 15.546 1.00102.40 C ANISOU 2417 CB ALA A 236 12645 12706 13558 -193 466 -26 C ATOM 2418 N ILE A 237 -13.877 -17.353 13.513 1.00 98.33 N ANISOU 2418 N ILE A 237 12235 12226 12899 -182 508 -26 N ATOM 2419 CA ILE A 237 -14.041 -16.350 12.474 1.00 97.84 C ANISOU 2419 CA ILE A 237 12217 12152 12807 -184 538 -33 C ATOM 2420 C ILE A 237 -15.065 -15.309 12.923 1.00 98.40 C ANISOU 2420 C ILE A 237 12315 12257 12814 -160 500 -29 C ATOM 2421 O ILE A 237 -14.851 -14.116 12.718 1.00 98.59 O ANISOU 2421 O ILE A 237 12363 12265 12833 -155 503 -34 O ATOM 2422 CB ILE A 237 -14.380 -16.990 11.109 1.00 97.40 C ANISOU 2422 CB ILE A 237 12187 12090 12730 -199 583 -36 C ATOM 2423 CG1 ILE A 237 -13.165 -17.717 10.524 1.00 97.37 C ANISOU 2423 CG1 ILE A 237 12159 12042 12793 -224 627 -46 C ATOM 2424 CG2 ILE A 237 -14.938 -15.957 10.137 1.00 96.77 C ANISOU 2424 CG2 ILE A 237 12161 12010 12598 -196 602 -39 C ATOM 2425 CD1 ILE A 237 -13.440 -18.484 9.251 1.00 97.10 C ANISOU 2425 CD1 ILE A 237 12147 12004 12744 -239 671 -49 C ATOM 2426 N ILE A 238 -16.154 -15.759 13.558 1.00 98.77 N ANISOU 2426 N ILE A 238 12358 12353 12817 -144 464 -19 N ATOM 2427 CA ILE A 238 -17.217 -14.848 13.958 1.00 99.14 C ANISOU 2427 CA ILE A 238 12430 12438 12802 -120 429 -17 C ATOM 2428 C ILE A 238 -16.647 -13.800 14.910 1.00 98.45 C ANISOU 2428 C ILE A 238 12330 12340 12736 -107 399 -20 C ATOM 2429 O ILE A 238 -16.847 -12.606 14.698 1.00 99.10 O ANISOU 2429 O ILE A 238 12443 12419 12793 -96 393 -26 O ATOM 2430 CB ILE A 238 -18.425 -15.591 14.568 1.00 99.54 C ANISOU 2430 CB ILE A 238 12471 12543 12805 -107 396 -8 C ATOM 2431 CG1 ILE A 238 -18.599 -16.992 13.977 1.00 99.96 C ANISOU 2431 CG1 ILE A 238 12516 12598 12864 -124 421 -3 C ATOM 2432 CG2 ILE A 238 -19.697 -14.761 14.442 1.00101.19 C ANISOU 2432 CG2 ILE A 238 12717 12790 12941 -85 376 -10 C ATOM 2433 CD1 ILE A 238 -19.110 -17.011 12.553 1.00100.02 C ANISOU 2433 CD1 ILE A 238 12565 12601 12838 -131 459 -8 C ATOM 2434 N ALA A 239 -15.911 -14.254 15.934 1.00 97.04 N ANISOU 2434 N ALA A 239 12109 12154 12608 -109 378 -17 N ATOM 2435 CA ALA A 239 -15.357 -13.354 16.934 1.00 96.36 C ANISOU 2435 CA ALA A 239 12008 12060 12546 -96 345 -20 C ATOM 2436 C ALA A 239 -14.336 -12.417 16.291 1.00 95.99 C ANISOU 2436 C ALA A 239 11974 11962 12537 -106 375 -31 C ATOM 2437 O ALA A 239 -14.205 -11.266 16.701 1.00 96.40 O ANISOU 2437 O ALA A 239 12035 12007 12584 -93 353 -35 O ATOM 2438 CB ALA A 239 -14.762 -14.140 18.077 1.00 96.60 C ANISOU 2438 CB ALA A 239 11992 12090 12622 -97 319 -15 C ATOM 2439 N GLY A 240 -13.632 -12.925 15.272 1.00 94.61 N ANISOU 2439 N GLY A 240 11799 11750 12397 -131 424 -35 N ATOM 2440 CA GLY A 240 -12.663 -12.145 14.518 1.00 93.51 C ANISOU 2440 CA GLY A 240 11673 11561 12293 -146 460 -45 C ATOM 2441 C GLY A 240 -13.325 -11.009 13.742 1.00 92.96 C ANISOU 2441 C GLY A 240 11657 11496 12169 -139 469 -47 C ATOM 2442 O GLY A 240 -12.864 -9.872 13.795 1.00 93.44 O ANISOU 2442 O GLY A 240 11730 11534 12241 -136 465 -52 O ATOM 2443 N LEU A 241 -14.416 -11.335 13.036 1.00 92.44 N ANISOU 2443 N LEU A 241 11622 11459 12044 -136 478 -43 N ATOM 2444 CA LEU A 241 -15.141 -10.368 12.226 1.00 93.50 C ANISOU 2444 CA LEU A 241 11809 11597 12121 -129 485 -45 C ATOM 2445 C LEU A 241 -15.840 -9.348 13.122 1.00 94.53 C ANISOU 2445 C LEU A 241 11949 11757 12213 -99 432 -45 C ATOM 2446 O LEU A 241 -16.022 -8.199 12.725 1.00 96.02 O ANISOU 2446 O LEU A 241 12174 11934 12375 -92 429 -49 O ATOM 2447 CB LEU A 241 -16.148 -11.095 11.328 1.00 92.82 C ANISOU 2447 CB LEU A 241 11748 11535 11984 -131 504 -42 C ATOM 2448 CG LEU A 241 -15.556 -12.041 10.281 1.00 92.83 C ANISOU 2448 CG LEU A 241 11748 11508 12016 -159 559 -44 C ATOM 2449 CD1 LEU A 241 -16.653 -12.626 9.405 1.00 92.78 C ANISOU 2449 CD1 LEU A 241 11772 11527 11953 -158 572 -42 C ATOM 2450 CD2 LEU A 241 -14.511 -11.338 9.427 1.00 93.12 C ANISOU 2450 CD2 LEU A 241 11803 11493 12087 -180 602 -52 C ATOM 2451 N PHE A 242 -16.229 -9.781 14.328 1.00 94.16 N ANISOU 2451 N PHE A 242 11869 11746 12162 -83 389 -40 N ATOM 2452 CA PHE A 242 -16.840 -8.885 15.297 1.00 93.09 C ANISOU 2452 CA PHE A 242 11737 11640 11993 -54 337 -42 C ATOM 2453 C PHE A 242 -15.833 -7.816 15.710 1.00 93.19 C ANISOU 2453 C PHE A 242 11744 11616 12048 -53 328 -48 C ATOM 2454 O PHE A 242 -16.185 -6.643 15.820 1.00 92.64 O ANISOU 2454 O PHE A 242 11700 11550 11949 -35 304 -53 O ATOM 2455 CB PHE A 242 -17.355 -9.651 16.520 1.00 92.70 C ANISOU 2455 CB PHE A 242 11652 11636 11935 -40 298 -35 C ATOM 2456 CG PHE A 242 -17.949 -8.770 17.590 1.00 92.45 C ANISOU 2456 CG PHE A 242 11619 11637 11870 -10 244 -38 C ATOM 2457 CD1 PHE A 242 -19.271 -8.357 17.519 1.00 92.14 C ANISOU 2457 CD1 PHE A 242 11608 11641 11761 11 223 -41 C ATOM 2458 CD2 PHE A 242 -17.180 -8.336 18.661 1.00 92.88 C ANISOU 2458 CD2 PHE A 242 11647 11680 11965 -3 216 -40 C ATOM 2459 CE1 PHE A 242 -19.813 -7.538 18.498 1.00 92.27 C ANISOU 2459 CE1 PHE A 242 11623 11688 11748 39 174 -46 C ATOM 2460 CE2 PHE A 242 -17.721 -7.514 19.637 1.00 93.08 C ANISOU 2460 CE2 PHE A 242 11672 11735 11959 25 167 -44 C ATOM 2461 CZ PHE A 242 -19.037 -7.118 19.555 1.00 92.97 C ANISOU 2461 CZ PHE A 242 11684 11765 11875 46 147 -48 C ATOM 2462 N ALA A 243 -14.584 -8.246 15.933 1.00 93.89 N ANISOU 2462 N ALA A 243 11798 11669 12208 -71 345 -48 N ATOM 2463 CA ALA A 243 -13.515 -7.367 16.379 1.00 94.87 C ANISOU 2463 CA ALA A 243 11910 11756 12382 -72 337 -54 C ATOM 2464 C ALA A 243 -13.167 -6.364 15.282 1.00 95.69 C ANISOU 2464 C ALA A 243 12053 11821 12483 -85 370 -59 C ATOM 2465 O ALA A 243 -13.005 -5.177 15.556 1.00 96.69 O ANISOU 2465 O ALA A 243 12195 11935 12609 -74 348 -64 O ATOM 2466 CB ALA A 243 -12.313 -8.179 16.800 1.00 93.16 C ANISOU 2466 CB ALA A 243 11645 11510 12241 -90 349 -54 C ATOM 2467 N LEU A 244 -13.081 -6.851 14.039 1.00 95.39 N ANISOU 2467 N LEU A 244 12035 11765 12443 -108 421 -59 N ATOM 2468 CA LEU A 244 -12.637 -6.025 12.928 1.00 96.54 C ANISOU 2468 CA LEU A 244 12218 11871 12592 -125 459 -63 C ATOM 2469 C LEU A 244 -13.675 -4.948 12.617 1.00 96.67 C ANISOU 2469 C LEU A 244 12286 11905 12539 -106 437 -63 C ATOM 2470 O LEU A 244 -13.313 -3.848 12.206 1.00 97.26 O ANISOU 2470 O LEU A 244 12389 11949 12616 -110 443 -66 O ATOM 2471 CB LEU A 244 -12.369 -6.910 11.706 1.00 97.41 C ANISOU 2471 CB LEU A 244 12337 11963 12712 -153 518 -63 C ATOM 2472 CG LEU A 244 -11.346 -6.361 10.712 1.00 98.04 C ANISOU 2472 CG LEU A 244 12435 11989 12827 -181 569 -69 C ATOM 2473 CD1 LEU A 244 -9.926 -6.580 11.217 1.00 97.15 C ANISOU 2473 CD1 LEU A 244 12273 11840 12799 -198 581 -75 C ATOM 2474 CD2 LEU A 244 -11.528 -7.003 9.345 1.00 98.74 C ANISOU 2474 CD2 LEU A 244 12551 12070 12895 -203 622 -69 C ATOM 2475 N CYS A 245 -14.958 -5.272 12.824 1.00 95.66 N ANISOU 2475 N CYS A 245 12169 11827 12352 -84 409 -60 N ATOM 2476 CA CYS A 245 -16.046 -4.361 12.506 1.00 94.77 C ANISOU 2476 CA CYS A 245 12103 11734 12171 -64 386 -62 C ATOM 2477 C CYS A 245 -16.125 -3.233 13.533 1.00 93.33 C ANISOU 2477 C CYS A 245 11917 11559 11983 -38 334 -67 C ATOM 2478 O CYS A 245 -16.416 -2.094 13.173 1.00 93.88 O ANISOU 2478 O CYS A 245 12027 11618 12023 -29 322 -71 O ATOM 2479 CB CYS A 245 -17.383 -5.091 12.456 1.00 96.05 C ANISOU 2479 CB CYS A 245 12273 11947 12274 -49 372 -60 C ATOM 2480 SG CYS A 245 -17.614 -6.083 10.958 1.00 98.77 S ANISOU 2480 SG CYS A 245 12643 12284 12603 -74 430 -56 S ATOM 2481 N TRP A 246 -15.856 -3.560 14.804 1.00 90.83 N ANISOU 2481 N TRP A 246 11555 11261 11697 -27 302 -66 N ATOM 2482 CA TRP A 246 -16.149 -2.655 15.905 1.00 89.70 C ANISOU 2482 CA TRP A 246 11405 11136 11539 3 246 -71 C ATOM 2483 C TRP A 246 -14.945 -1.796 16.284 1.00 89.82 C ANISOU 2483 C TRP A 246 11410 11108 11612 -3 241 -75 C ATOM 2484 O TRP A 246 -15.123 -0.696 16.804 1.00 89.96 O ANISOU 2484 O TRP A 246 11439 11127 11614 18 203 -81 O ATOM 2485 CB TRP A 246 -16.704 -3.413 17.117 1.00 88.58 C ANISOU 2485 CB TRP A 246 11225 11044 11386 22 208 -69 C ATOM 2486 CG TRP A 246 -18.193 -3.569 17.085 1.00 88.34 C ANISOU 2486 CG TRP A 246 11215 11068 11284 42 187 -70 C ATOM 2487 CD1 TRP A 246 -18.893 -4.686 16.730 1.00 88.85 C ANISOU 2487 CD1 TRP A 246 11275 11162 11321 36 204 -64 C ATOM 2488 CD2 TRP A 246 -19.175 -2.565 17.401 1.00 87.31 C ANISOU 2488 CD2 TRP A 246 11109 10967 11097 73 145 -78 C ATOM 2489 NE1 TRP A 246 -20.239 -4.452 16.812 1.00 87.86 N ANISOU 2489 NE1 TRP A 246 11170 11084 11129 60 175 -69 N ATOM 2490 CE2 TRP A 246 -20.443 -3.159 17.218 1.00 87.32 C ANISOU 2490 CE2 TRP A 246 11119 11017 11042 84 139 -78 C ATOM 2491 CE3 TRP A 246 -19.110 -1.231 17.821 1.00 86.60 C ANISOU 2491 CE3 TRP A 246 11035 10869 11003 93 111 -88 C ATOM 2492 CZ2 TRP A 246 -21.631 -2.463 17.444 1.00 86.67 C ANISOU 2492 CZ2 TRP A 246 11059 10973 10898 113 101 -88 C ATOM 2493 CZ3 TRP A 246 -20.285 -0.544 18.043 1.00 86.21 C ANISOU 2493 CZ3 TRP A 246 11008 10857 10892 123 72 -97 C ATOM 2494 CH2 TRP A 246 -21.527 -1.154 17.857 1.00 86.13 C ANISOU 2494 CH2 TRP A 246 11004 10895 10826 133 68 -98 C ATOM 2495 N LEU A 247 -13.732 -2.301 16.026 1.00 89.93 N ANISOU 2495 N LEU A 247 11399 11081 11690 -32 279 -73 N ATOM 2496 CA LEU A 247 -12.526 -1.665 16.537 1.00 90.14 C ANISOU 2496 CA LEU A 247 11404 11067 11779 -38 273 -77 C ATOM 2497 C LEU A 247 -12.334 -0.258 15.970 1.00 90.01 C ANISOU 2497 C LEU A 247 11428 11017 11754 -39 275 -82 C ATOM 2498 O LEU A 247 -11.982 0.644 16.726 1.00 89.82 O ANISOU 2498 O LEU A 247 11397 10982 11749 -25 240 -86 O ATOM 2499 CB LEU A 247 -11.303 -2.561 16.310 1.00 90.59 C ANISOU 2499 CB LEU A 247 11425 11088 11908 -68 316 -76 C ATOM 2500 CG LEU A 247 -11.018 -3.572 17.422 1.00 90.51 C ANISOU 2500 CG LEU A 247 11361 11096 11933 -62 293 -75 C ATOM 2501 CD1 LEU A 247 -9.782 -4.397 17.100 1.00 91.64 C ANISOU 2501 CD1 LEU A 247 11470 11200 12149 -92 336 -76 C ATOM 2502 CD2 LEU A 247 -10.856 -2.880 18.767 1.00 90.43 C ANISOU 2502 CD2 LEU A 247 11330 11095 11936 -38 237 -78 C ATOM 2503 N PRO A 248 -12.542 -0.001 14.653 1.00 89.66 N ANISOU 2503 N PRO A 248 11430 10955 11683 -56 314 -80 N ATOM 2504 CA PRO A 248 -12.396 1.350 14.107 1.00 90.17 C ANISOU 2504 CA PRO A 248 11537 10987 11736 -58 314 -83 C ATOM 2505 C PRO A 248 -13.141 2.426 14.896 1.00 91.30 C ANISOU 2505 C PRO A 248 11696 11153 11840 -23 251 -88 C ATOM 2506 O PRO A 248 -12.576 3.481 15.178 1.00 91.91 O ANISOU 2506 O PRO A 248 11780 11202 11942 -20 233 -92 O ATOM 2507 CB PRO A 248 -12.968 1.228 12.688 1.00 89.51 C ANISOU 2507 CB PRO A 248 11503 10899 11606 -74 354 -79 C ATOM 2508 CG PRO A 248 -12.703 -0.212 12.319 1.00 89.46 C ANISOU 2508 CG PRO A 248 11469 10898 11623 -95 397 -75 C ATOM 2509 CD PRO A 248 -12.887 -0.982 13.610 1.00 89.05 C ANISOU 2509 CD PRO A 248 11366 10883 11585 -75 360 -75 C ATOM 2510 N LEU A 249 -14.399 2.143 15.262 1.00 91.80 N ANISOU 2510 N LEU A 249 11765 11270 11845 5 219 -89 N ATOM 2511 CA LEU A 249 -15.239 3.108 15.956 1.00 92.17 C ANISOU 2511 CA LEU A 249 11827 11344 11848 41 161 -96 C ATOM 2512 C LEU A 249 -14.674 3.395 17.347 1.00 92.28 C ANISOU 2512 C LEU A 249 11799 11361 11902 57 119 -101 C ATOM 2513 O LEU A 249 -14.779 4.516 17.837 1.00 90.58 O ANISOU 2513 O LEU A 249 11597 11142 11677 78 78 -108 O ATOM 2514 CB LEU A 249 -16.679 2.585 16.028 1.00 92.10 C ANISOU 2514 CB LEU A 249 11827 11393 11772 63 141 -98 C ATOM 2515 CG LEU A 249 -17.709 3.526 16.659 1.00 92.26 C ANISOU 2515 CG LEU A 249 11865 11449 11740 102 82 -108 C ATOM 2516 CD1 LEU A 249 -17.782 4.854 15.918 1.00 92.84 C ANISOU 2516 CD1 LEU A 249 11993 11490 11793 105 76 -113 C ATOM 2517 CD2 LEU A 249 -19.082 2.875 16.707 1.00 91.82 C ANISOU 2517 CD2 LEU A 249 11813 11452 11623 121 68 -111 C ATOM 2518 N HIS A 250 -14.066 2.376 17.966 1.00 94.29 N ANISOU 2518 N HIS A 250 12005 11620 12202 47 128 -97 N ATOM 2519 CA HIS A 250 -13.517 2.506 19.306 1.00 96.36 C ANISOU 2519 CA HIS A 250 12225 11885 12503 62 89 -101 C ATOM 2520 C HIS A 250 -12.255 3.366 19.298 1.00 98.36 C ANISOU 2520 C HIS A 250 12474 12081 12816 48 95 -104 C ATOM 2521 O HIS A 250 -12.002 4.089 20.259 1.00100.51 O ANISOU 2521 O HIS A 250 12733 12351 13105 67 52 -111 O ATOM 2522 CB HIS A 250 -13.282 1.130 19.941 1.00 95.67 C ANISOU 2522 CB HIS A 250 12089 11819 12444 56 95 -95 C ATOM 2523 CG HIS A 250 -14.532 0.459 20.406 1.00 95.59 C ANISOU 2523 CG HIS A 250 12075 11870 12376 77 71 -94 C ATOM 2524 ND1 HIS A 250 -15.276 0.934 21.468 1.00 94.66 N ANISOU 2524 ND1 HIS A 250 11951 11793 12221 111 16 -100 N ATOM 2525 CD2 HIS A 250 -15.163 -0.652 19.970 1.00 96.10 C ANISOU 2525 CD2 HIS A 250 12138 11963 12414 68 95 -87 C ATOM 2526 CE1 HIS A 250 -16.316 0.148 21.662 1.00 94.94 C ANISOU 2526 CE1 HIS A 250 11982 11880 12209 121 8 -97 C ATOM 2527 NE2 HIS A 250 -16.270 -0.833 20.754 1.00 95.30 N ANISOU 2527 NE2 HIS A 250 12030 11919 12261 95 55 -88 N ATOM 2528 N ILE A 251 -11.471 3.278 18.214 1.00 99.60 N ANISOU 2528 N ILE A 251 12645 12193 13007 14 149 -100 N ATOM 2529 CA ILE A 251 -10.215 4.007 18.101 1.00100.23 C ANISOU 2529 CA ILE A 251 12719 12217 13148 -5 163 -103 C ATOM 2530 C ILE A 251 -10.508 5.499 17.938 1.00100.40 C ANISOU 2530 C ILE A 251 12783 12223 13140 8 135 -107 C ATOM 2531 O ILE A 251 -9.811 6.331 18.514 1.00100.83 O ANISOU 2531 O ILE A 251 12828 12250 13232 13 110 -112 O ATOM 2532 CB ILE A 251 -9.332 3.454 16.960 1.00100.82 C ANISOU 2532 CB ILE A 251 12793 12249 13263 -47 232 -99 C ATOM 2533 CG1 ILE A 251 -9.036 1.957 17.110 1.00100.71 C ANISOU 2533 CG1 ILE A 251 12736 12248 13280 -60 257 -96 C ATOM 2534 CG2 ILE A 251 -8.052 4.265 16.801 1.00100.92 C ANISOU 2534 CG2 ILE A 251 12803 12205 13339 -69 248 -102 C ATOM 2535 CD1 ILE A 251 -8.235 1.584 18.340 1.00102.29 C ANISOU 2535 CD1 ILE A 251 12881 12445 13541 -54 231 -100 C ATOM 2536 N ILE A 252 -11.547 5.822 17.157 1.00 99.70 N ANISOU 2536 N ILE A 252 12745 12153 12986 16 137 -106 N ATOM 2537 CA ILE A 252 -11.938 7.206 16.934 1.00 99.71 C ANISOU 2537 CA ILE A 252 12791 12141 12953 30 109 -110 C ATOM 2538 C ILE A 252 -12.401 7.816 18.256 1.00100.17 C ANISOU 2538 C ILE A 252 12834 12230 12997 70 39 -120 C ATOM 2539 O ILE A 252 -12.212 9.007 18.489 1.00102.57 O ANISOU 2539 O ILE A 252 13155 12511 13305 82 8 -126 O ATOM 2540 CB ILE A 252 -13.006 7.328 15.825 1.00 99.28 C ANISOU 2540 CB ILE A 252 12792 12101 12830 31 123 -108 C ATOM 2541 CG1 ILE A 252 -12.556 6.653 14.525 1.00 98.60 C ANISOU 2541 CG1 ILE A 252 12721 11987 12756 -9 193 -98 C ATOM 2542 CG2 ILE A 252 -13.380 8.787 15.603 1.00 98.50 C ANISOU 2542 CG2 ILE A 252 12742 11985 12698 46 90 -113 C ATOM 2543 CD1 ILE A 252 -13.639 6.527 13.475 1.00 96.70 C ANISOU 2543 CD1 ILE A 252 12529 11764 12447 -8 208 -96 C ATOM 2544 N ASN A 253 -12.995 6.983 19.119 1.00 98.79 N ANISOU 2544 N ASN A 253 12626 12105 12805 91 16 -122 N ATOM 2545 CA ASN A 253 -13.387 7.407 20.454 1.00 98.64 C ANISOU 2545 CA ASN A 253 12586 12119 12774 128 -47 -131 C ATOM 2546 C ASN A 253 -12.146 7.639 21.314 1.00 98.91 C ANISOU 2546 C ASN A 253 12582 12120 12879 124 -60 -133 C ATOM 2547 O ASN A 253 -12.153 8.501 22.188 1.00 99.82 O ANISOU 2547 O ASN A 253 12692 12238 12995 149 -110 -143 O ATOM 2548 CB ASN A 253 -14.367 6.428 21.104 1.00 98.45 C ANISOU 2548 CB ASN A 253 12539 12158 12709 148 -65 -131 C ATOM 2549 CG ASN A 253 -15.803 6.641 20.671 1.00 98.59 C ANISOU 2549 CG ASN A 253 12595 12216 12648 169 -79 -136 C ATOM 2550 OD1 ASN A 253 -16.080 7.436 19.775 1.00 98.29 O ANISOU 2550 OD1 ASN A 253 12603 12158 12584 167 -73 -138 O ATOM 2551 ND2 ASN A 253 -16.726 5.936 21.305 1.00 98.60 N ANISOU 2551 ND2 ASN A 253 12577 12275 12611 189 -100 -138 N ATOM 2552 N CYS A 254 -11.084 6.866 21.053 1.00 99.76 N ANISOU 2552 N CYS A 254 12661 12196 13047 91 -16 -126 N ATOM 2553 CA CYS A 254 -9.842 6.983 21.800 1.00100.93 C ANISOU 2553 CA CYS A 254 12769 12310 13269 84 -25 -129 C ATOM 2554 C CYS A 254 -9.077 8.231 21.365 1.00102.84 C ANISOU 2554 C CYS A 254 13034 12497 13542 72 -22 -133 C ATOM 2555 O CYS A 254 -8.364 8.828 22.168 1.00104.95 O ANISOU 2555 O CYS A 254 13280 12743 13852 80 -53 -139 O ATOM 2556 CB CYS A 254 -8.969 5.746 21.621 1.00100.57 C ANISOU 2556 CB CYS A 254 12685 12248 13278 54 20 -123 C ATOM 2557 SG CYS A 254 -9.571 4.303 22.538 1.00 99.57 S ANISOU 2557 SG CYS A 254 12518 12179 13135 70 3 -119 S ATOM 2558 N PHE A 255 -9.230 8.614 20.091 1.00103.23 N ANISOU 2558 N PHE A 255 13130 12525 13569 52 15 -128 N ATOM 2559 CA PHE A 255 -8.594 9.815 19.573 1.00104.08 C ANISOU 2559 CA PHE A 255 13266 12581 13700 38 20 -129 C ATOM 2560 C PHE A 255 -9.293 11.058 20.121 1.00103.63 C ANISOU 2560 C PHE A 255 13237 12536 13602 73 -42 -137 C ATOM 2561 O PHE A 255 -8.630 12.004 20.543 1.00104.94 O ANISOU 2561 O PHE A 255 13400 12669 13804 76 -67 -143 O ATOM 2562 CB PHE A 255 -8.535 9.796 18.043 1.00106.00 C ANISOU 2562 CB PHE A 255 13551 12796 13929 3 80 -120 C ATOM 2563 CG PHE A 255 -7.246 9.258 17.472 1.00107.61 C ANISOU 2563 CG PHE A 255 13731 12955 14201 -39 140 -116 C ATOM 2564 CD1 PHE A 255 -7.095 7.903 17.208 1.00107.61 C ANISOU 2564 CD1 PHE A 255 13702 12968 14216 -57 181 -112 C ATOM 2565 CD2 PHE A 255 -6.182 10.105 17.197 1.00108.13 C ANISOU 2565 CD2 PHE A 255 13801 12965 14318 -63 154 -117 C ATOM 2566 CE1 PHE A 255 -5.908 7.410 16.687 1.00107.36 C ANISOU 2566 CE1 PHE A 255 13647 12896 14249 -95 236 -111 C ATOM 2567 CE2 PHE A 255 -4.994 9.611 16.679 1.00107.86 C ANISOU 2567 CE2 PHE A 255 13743 12892 14349 -102 211 -116 C ATOM 2568 CZ PHE A 255 -4.861 8.264 16.422 1.00108.04 C ANISOU 2568 CZ PHE A 255 13737 12930 14385 -117 251 -113 C ATOM 2569 N THR A 256 -10.632 11.037 20.116 1.00101.70 N ANISOU 2569 N THR A 256 13017 12339 13284 101 -67 -140 N ATOM 2570 CA THR A 256 -11.435 12.143 20.614 1.00100.74 C ANISOU 2570 CA THR A 256 12922 12236 13118 138 -127 -150 C ATOM 2571 C THR A 256 -11.133 12.361 22.094 1.00102.04 C ANISOU 2571 C THR A 256 13045 12414 13311 165 -179 -160 C ATOM 2572 O THR A 256 -11.071 13.498 22.559 1.00103.83 O ANISOU 2572 O THR A 256 13284 12627 13540 185 -224 -169 O ATOM 2573 CB THR A 256 -12.931 11.907 20.361 1.00 98.20 C ANISOU 2573 CB THR A 256 12628 11968 12716 161 -140 -153 C ATOM 2574 OG1 THR A 256 -13.127 11.689 18.964 1.00 98.64 O ANISOU 2574 OG1 THR A 256 12723 12007 12749 134 -90 -144 O ATOM 2575 CG2 THR A 256 -13.805 13.060 20.805 1.00 98.10 C ANISOU 2575 CG2 THR A 256 12643 11974 12655 200 -202 -167 C ATOM 2576 N PHE A 257 -10.928 11.255 22.818 1.00103.73 N ANISOU 2576 N PHE A 257 13210 12654 13547 166 -175 -158 N ATOM 2577 CA PHE A 257 -10.774 11.300 24.261 1.00105.60 C ANISOU 2577 CA PHE A 257 13408 12912 13804 193 -226 -167 C ATOM 2578 C PHE A 257 -9.349 11.696 24.639 1.00107.69 C ANISOU 2578 C PHE A 257 13646 13122 14148 178 -226 -168 C ATOM 2579 O PHE A 257 -9.156 12.610 25.438 1.00108.32 O ANISOU 2579 O PHE A 257 13722 13193 14240 200 -275 -178 O ATOM 2580 CB PHE A 257 -11.190 9.968 24.893 1.00104.93 C ANISOU 2580 CB PHE A 257 13286 12876 13706 200 -224 -164 C ATOM 2581 CG PHE A 257 -11.093 9.926 26.396 1.00104.51 C ANISOU 2581 CG PHE A 257 13195 12849 13667 228 -276 -172 C ATOM 2582 CD1 PHE A 257 -11.827 10.805 27.180 1.00104.43 C ANISOU 2582 CD1 PHE A 257 13196 12868 13616 267 -335 -185 C ATOM 2583 CD2 PHE A 257 -10.271 9.005 27.028 1.00104.22 C ANISOU 2583 CD2 PHE A 257 13111 12805 13682 216 -268 -167 C ATOM 2584 CE1 PHE A 257 -11.739 10.766 28.563 1.00104.63 C ANISOU 2584 CE1 PHE A 257 13187 12917 13650 293 -382 -193 C ATOM 2585 CE2 PHE A 257 -10.184 8.966 28.412 1.00104.85 C ANISOU 2585 CE2 PHE A 257 13159 12908 13773 241 -317 -174 C ATOM 2586 CZ PHE A 257 -10.918 9.846 29.176 1.00105.44 C ANISOU 2586 CZ PHE A 257 13246 13013 13805 280 -373 -186 C ATOM 2587 N PHE A 258 -8.363 11.006 24.051 1.00109.40 N ANISOU 2587 N PHE A 258 13845 13303 14420 139 -172 -159 N ATOM 2588 CA PHE A 258 -6.983 11.105 24.501 1.00110.21 C ANISOU 2588 CA PHE A 258 13911 13360 14605 124 -170 -162 C ATOM 2589 C PHE A 258 -6.259 12.281 23.851 1.00113.00 C ANISOU 2589 C PHE A 258 14291 13655 14989 105 -159 -163 C ATOM 2590 O PHE A 258 -5.359 12.851 24.462 1.00115.94 O ANISOU 2590 O PHE A 258 14642 13994 15416 106 -182 -169 O ATOM 2591 CB PHE A 258 -6.234 9.788 24.285 1.00108.00 C ANISOU 2591 CB PHE A 258 13592 13070 14373 93 -121 -155 C ATOM 2592 CG PHE A 258 -6.530 8.716 25.304 1.00107.08 C ANISOU 2592 CG PHE A 258 13436 12998 14252 112 -144 -155 C ATOM 2593 CD1 PHE A 258 -6.231 8.906 26.646 1.00106.71 C ANISOU 2593 CD1 PHE A 258 13357 12958 14230 136 -196 -163 C ATOM 2594 CD2 PHE A 258 -7.093 7.509 24.920 1.00106.85 C ANISOU 2594 CD2 PHE A 258 13402 13002 14194 103 -112 -147 C ATOM 2595 CE1 PHE A 258 -6.496 7.917 27.581 1.00105.47 C ANISOU 2595 CE1 PHE A 258 13167 12842 14067 151 -217 -162 C ATOM 2596 CE2 PHE A 258 -7.356 6.519 25.855 1.00106.33 C ANISOU 2596 CE2 PHE A 258 13301 12976 14124 117 -134 -145 C ATOM 2597 CZ PHE A 258 -7.060 6.725 27.185 1.00105.82 C ANISOU 2597 CZ PHE A 258 13207 12918 14082 141 -186 -152 C ATOM 2598 N CYS A 259 -6.637 12.631 22.615 1.00115.65 N ANISOU 2598 N CYS A 259 14675 13978 15290 87 -125 -156 N ATOM 2599 CA CYS A 259 -5.967 13.716 21.914 1.00119.44 C ANISOU 2599 CA CYS A 259 15183 14401 15796 65 -111 -155 C ATOM 2600 C CYS A 259 -6.941 14.862 21.641 1.00121.29 C ANISOU 2600 C CYS A 259 15473 14644 15967 88 -147 -158 C ATOM 2601 O CYS A 259 -7.692 14.822 20.668 1.00120.97 O ANISOU 2601 O CYS A 259 15475 14615 15874 81 -123 -152 O ATOM 2602 CB CYS A 259 -5.329 13.239 20.614 1.00122.49 C ANISOU 2602 CB CYS A 259 15580 14752 16208 18 -36 -145 C ATOM 2603 SG CYS A 259 -4.307 14.512 19.828 1.00128.03 S ANISOU 2603 SG CYS A 259 16311 15381 16953 -16 -14 -143 S ATOM 2604 N PRO A 260 -6.963 15.915 22.492 1.00123.85 N ANISOU 2604 N PRO A 260 15799 14964 16294 117 -207 -169 N ATOM 2605 CA PRO A 260 -7.729 17.127 22.197 1.00127.17 C ANISOU 2605 CA PRO A 260 16274 15383 16663 137 -243 -173 C ATOM 2606 C PRO A 260 -7.004 18.093 21.259 1.00131.45 C ANISOU 2606 C PRO A 260 16852 15861 17232 105 -219 -166 C ATOM 2607 O PRO A 260 -7.628 18.985 20.688 1.00134.55 O ANISOU 2607 O PRO A 260 17297 16247 17580 112 -235 -166 O ATOM 2608 CB PRO A 260 -7.922 17.753 23.585 1.00126.42 C ANISOU 2608 CB PRO A 260 16157 15307 16568 180 -316 -188 C ATOM 2609 CG PRO A 260 -6.693 17.327 24.364 1.00126.18 C ANISOU 2609 CG PRO A 260 16071 15254 16616 168 -312 -189 C ATOM 2610 CD PRO A 260 -6.299 15.975 23.804 1.00124.78 C ANISOU 2610 CD PRO A 260 15869 15079 16462 135 -248 -178 C ATOM 2611 N ASP A 261 -5.686 17.902 21.107 1.00134.35 N ANISOU 2611 N ASP A 261 17191 16183 17674 69 -180 -162 N ATOM 2612 CA ASP A 261 -4.868 18.734 20.238 1.00136.45 C ANISOU 2612 CA ASP A 261 17486 16387 17973 33 -151 -155 C ATOM 2613 C ASP A 261 -5.071 18.324 18.782 1.00134.58 C ANISOU 2613 C ASP A 261 17287 16141 17706 -2 -86 -141 C ATOM 2614 O ASP A 261 -4.938 19.150 17.881 1.00135.89 O ANISOU 2614 O ASP A 261 17500 16268 17863 -25 -70 -135 O ATOM 2615 CB ASP A 261 -3.394 18.700 20.652 1.00142.00 C ANISOU 2615 CB ASP A 261 18141 17046 18767 9 -136 -157 C ATOM 2616 CG ASP A 261 -3.088 19.544 21.878 1.00146.65 C ANISOU 2616 CG ASP A 261 18709 17626 19386 39 -203 -169 C ATOM 2617 OD1 ASP A 261 -4.014 20.219 22.377 1.00149.19 O ANISOU 2617 OD1 ASP A 261 19055 17975 19657 78 -261 -177 O ATOM 2618 OD2 ASP A 261 -1.923 19.524 22.324 1.00148.33 O ANISOU 2618 OD2 ASP A 261 18880 17804 19673 23 -197 -173 O ATOM 2619 N CYS A 262 -5.388 17.041 18.571 1.00130.94 N ANISOU 2619 N CYS A 262 16806 15714 17230 -8 -50 -138 N ATOM 2620 CA CYS A 262 -5.731 16.522 17.257 1.00128.90 C ANISOU 2620 CA CYS A 262 16583 15457 16937 -36 8 -127 C ATOM 2621 C CYS A 262 -7.061 17.126 16.815 1.00127.84 C ANISOU 2621 C CYS A 262 16508 15346 16719 -12 -22 -126 C ATOM 2622 O CYS A 262 -7.908 17.445 17.647 1.00127.34 O ANISOU 2622 O CYS A 262 16445 15320 16618 32 -82 -136 O ATOM 2623 CB CYS A 262 -5.895 15.007 17.302 1.00127.68 C ANISOU 2623 CB CYS A 262 16391 15340 16782 -39 42 -125 C ATOM 2624 SG CYS A 262 -4.416 14.111 17.842 1.00126.41 S ANISOU 2624 SG CYS A 262 16156 15156 16718 -64 74 -128 S ATOM 2625 N SER A 263 -7.229 17.284 15.497 1.00126.86 N ANISOU 2625 N SER A 263 16436 15201 16565 -40 21 -116 N ATOM 2626 CA SER A 263 -8.517 17.644 14.928 1.00126.66 C ANISOU 2626 CA SER A 263 16467 15199 16458 -20 1 -115 C ATOM 2627 C SER A 263 -9.495 16.497 15.161 1.00125.76 C ANISOU 2627 C SER A 263 16334 15147 16301 3 0 -118 C ATOM 2628 O SER A 263 -9.083 15.346 15.270 1.00127.62 O ANISOU 2628 O SER A 263 16526 15396 16567 -11 37 -116 O ATOM 2629 CB SER A 263 -8.392 17.957 13.461 1.00128.83 C ANISOU 2629 CB SER A 263 16799 15436 16715 -58 50 -102 C ATOM 2630 OG SER A 263 -7.293 18.824 13.221 1.00133.62 O ANISOU 2630 OG SER A 263 17415 15984 17372 -88 64 -97 O ATOM 2631 N HIS A 264 -10.788 16.820 15.262 1.00124.03 N ANISOU 2631 N HIS A 264 16146 14966 16014 39 -44 -125 N ATOM 2632 CA HIS A 264 -11.800 15.784 15.383 1.00121.96 C ANISOU 2632 CA HIS A 264 15871 14762 15705 59 -44 -128 C ATOM 2633 C HIS A 264 -11.983 15.103 14.029 1.00119.82 C ANISOU 2633 C HIS A 264 15631 14485 15409 28 18 -116 C ATOM 2634 O HIS A 264 -11.879 15.750 12.988 1.00120.18 O ANISOU 2634 O HIS A 264 15730 14493 15441 5 39 -109 O ATOM 2635 CB HIS A 264 -13.111 16.350 15.947 1.00124.07 C ANISOU 2635 CB HIS A 264 16158 15073 15911 108 -111 -141 C ATOM 2636 CG HIS A 264 -14.082 15.293 16.353 1.00125.01 C ANISOU 2636 CG HIS A 264 16252 15256 15991 132 -118 -146 C ATOM 2637 ND1 HIS A 264 -14.877 14.628 15.438 1.00126.52 N ANISOU 2637 ND1 HIS A 264 16470 15469 16134 125 -87 -141 N ATOM 2638 CD2 HIS A 264 -14.384 14.775 17.563 1.00123.80 C ANISOU 2638 CD2 HIS A 264 16051 15149 15840 161 -151 -155 C ATOM 2639 CE1 HIS A 264 -15.629 13.748 16.067 1.00124.93 C ANISOU 2639 CE1 HIS A 264 16237 15324 15908 148 -101 -146 C ATOM 2640 NE2 HIS A 264 -15.347 13.820 17.374 1.00123.44 N ANISOU 2640 NE2 HIS A 264 16001 15152 15747 170 -139 -155 N ATOM 2641 N ALA A 265 -12.244 13.791 14.067 1.00116.65 N ANISOU 2641 N ALA A 265 15198 14120 15003 26 46 -114 N ATOM 2642 CA ALA A 265 -12.445 12.990 12.870 1.00114.46 C ANISOU 2642 CA ALA A 265 14944 13842 14702 -2 104 -104 C ATOM 2643 C ALA A 265 -13.602 13.559 12.051 1.00114.34 C ANISOU 2643 C ALA A 265 14995 13837 14613 12 88 -105 C ATOM 2644 O ALA A 265 -14.638 13.917 12.611 1.00114.79 O ANISOU 2644 O ALA A 265 15060 13931 14624 52 32 -115 O ATOM 2645 CB ALA A 265 -12.699 11.554 13.254 1.00113.84 C ANISOU 2645 CB ALA A 265 14819 13808 14626 3 121 -105 C ATOM 2646 N PRO A 266 -13.459 13.654 10.707 1.00114.18 N ANISOU 2646 N PRO A 266 15024 13783 14577 -21 135 -95 N ATOM 2647 CA PRO A 266 -14.514 14.191 9.843 1.00113.85 C ANISOU 2647 CA PRO A 266 15048 13744 14464 -10 121 -95 C ATOM 2648 C PRO A 266 -15.822 13.417 9.986 1.00112.29 C ANISOU 2648 C PRO A 266 14847 13608 14212 20 102 -102 C ATOM 2649 O PRO A 266 -15.816 12.265 10.414 1.00113.95 O ANISOU 2649 O PRO A 266 15008 13850 14437 21 119 -102 O ATOM 2650 CB PRO A 266 -13.955 13.991 8.427 1.00114.89 C ANISOU 2650 CB PRO A 266 15218 13835 14600 -58 189 -81 C ATOM 2651 CG PRO A 266 -12.455 13.938 8.615 1.00115.41 C ANISOU 2651 CG PRO A 266 15247 13861 14744 -92 227 -75 C ATOM 2652 CD PRO A 266 -12.262 13.252 9.950 1.00114.25 C ANISOU 2652 CD PRO A 266 15025 13748 14635 -70 204 -84 C ATOM 2653 N LEU A 267 -16.935 14.060 9.612 1.00110.05 N ANISOU 2653 N LEU A 267 14613 13336 13864 45 65 -108 N ATOM 2654 CA LEU A 267 -18.260 13.498 9.830 1.00109.13 C ANISOU 2654 CA LEU A 267 14493 13277 13693 78 38 -117 C ATOM 2655 C LEU A 267 -18.476 12.273 8.942 1.00110.02 C ANISOU 2655 C LEU A 267 14609 13404 13790 56 94 -109 C ATOM 2656 O LEU A 267 -19.194 11.352 9.329 1.00110.15 O ANISOU 2656 O LEU A 267 14596 13471 13787 73 87 -114 O ATOM 2657 CB LEU A 267 -19.327 14.569 9.579 1.00107.02 C ANISOU 2657 CB LEU A 267 14282 13015 13366 109 -15 -128 C ATOM 2658 CG LEU A 267 -20.762 14.169 9.927 1.00104.08 C ANISOU 2658 CG LEU A 267 13905 12704 12937 148 -53 -142 C ATOM 2659 CD1 LEU A 267 -20.897 13.834 11.406 1.00103.82 C ANISOU 2659 CD1 LEU A 267 13806 12717 12922 178 -89 -154 C ATOM 2660 CD2 LEU A 267 -21.744 15.262 9.535 1.00103.21 C ANISOU 2660 CD2 LEU A 267 13854 12591 12771 176 -102 -153 C ATOM 2661 N TRP A 268 -17.848 12.267 7.760 1.00110.54 N ANISOU 2661 N TRP A 268 14710 13424 13864 16 148 -96 N ATOM 2662 CA TRP A 268 -17.999 11.159 6.831 1.00110.81 C ANISOU 2662 CA TRP A 268 14752 13467 13884 -7 202 -89 C ATOM 2663 C TRP A 268 -17.275 9.919 7.353 1.00110.43 C ANISOU 2663 C TRP A 268 14637 13433 13889 -23 239 -86 C ATOM 2664 O TRP A 268 -17.695 8.798 7.075 1.00110.55 O ANISOU 2664 O TRP A 268 14638 13477 13888 -26 264 -84 O ATOM 2665 CB TRP A 268 -17.541 11.542 5.418 1.00113.24 C ANISOU 2665 CB TRP A 268 15121 13723 14184 -45 250 -77 C ATOM 2666 CG TRP A 268 -16.104 11.952 5.327 1.00114.78 C ANISOU 2666 CG TRP A 268 15307 13865 14440 -82 285 -68 C ATOM 2667 CD1 TRP A 268 -15.607 13.217 5.445 1.00115.21 C ANISOU 2667 CD1 TRP A 268 15384 13879 14509 -85 261 -67 C ATOM 2668 CD2 TRP A 268 -14.972 11.095 5.092 1.00116.21 C ANISOU 2668 CD2 TRP A 268 15450 14027 14677 -120 349 -61 C ATOM 2669 NE1 TRP A 268 -14.246 13.208 5.301 1.00116.35 N ANISOU 2669 NE1 TRP A 268 15509 13982 14716 -124 308 -59 N ATOM 2670 CE2 TRP A 268 -13.827 11.922 5.086 1.00116.94 C ANISOU 2670 CE2 TRP A 268 15545 14069 14817 -146 362 -56 C ATOM 2671 CE3 TRP A 268 -14.810 9.718 4.889 1.00116.45 C ANISOU 2671 CE3 TRP A 268 15445 14078 14723 -135 395 -59 C ATOM 2672 CZ2 TRP A 268 -12.543 11.413 4.885 1.00118.10 C ANISOU 2672 CZ2 TRP A 268 15659 14186 15027 -185 421 -51 C ATOM 2673 CZ3 TRP A 268 -13.541 9.216 4.694 1.00117.24 C ANISOU 2673 CZ3 TRP A 268 15513 14148 14884 -173 452 -54 C ATOM 2674 CH2 TRP A 268 -12.424 10.055 4.691 1.00117.73 C ANISOU 2674 CH2 TRP A 268 15578 14162 14994 -198 465 -51 C ATOM 2675 N LEU A 269 -16.190 10.130 8.110 1.00110.69 N ANISOU 2675 N LEU A 269 14628 13444 13983 -32 239 -85 N ATOM 2676 CA LEU A 269 -15.451 9.022 8.699 1.00110.08 C ANISOU 2676 CA LEU A 269 14485 13379 13961 -45 268 -83 C ATOM 2677 C LEU A 269 -16.232 8.452 9.881 1.00109.69 C ANISOU 2677 C LEU A 269 14392 13389 13898 -7 222 -92 C ATOM 2678 O LEU A 269 -16.182 7.249 10.132 1.00109.01 O ANISOU 2678 O LEU A 269 14263 13327 13827 -12 244 -90 O ATOM 2679 CB LEU A 269 -14.047 9.479 9.112 1.00108.87 C ANISOU 2679 CB LEU A 269 14305 13183 13880 -67 280 -81 C ATOM 2680 CG LEU A 269 -13.085 8.359 9.513 1.00107.80 C ANISOU 2680 CG LEU A 269 14105 13046 13807 -87 318 -79 C ATOM 2681 CD1 LEU A 269 -12.844 7.397 8.359 1.00108.16 C ANISOU 2681 CD1 LEU A 269 14161 13080 13854 -122 386 -72 C ATOM 2682 CD2 LEU A 269 -11.765 8.921 10.011 1.00107.39 C ANISOU 2682 CD2 LEU A 269 14025 12952 13826 -104 322 -79 C ATOM 2683 N MET A 270 -16.954 9.328 10.592 1.00109.20 N ANISOU 2683 N MET A 270 14339 13346 13804 29 160 -101 N ATOM 2684 CA MET A 270 -17.826 8.919 11.681 1.00108.25 C ANISOU 2684 CA MET A 270 14183 13285 13662 67 114 -111 C ATOM 2685 C MET A 270 -18.928 8.017 11.132 1.00108.02 C ANISOU 2685 C MET A 270 14166 13296 13581 73 126 -111 C ATOM 2686 O MET A 270 -19.211 6.969 11.706 1.00107.95 O ANISOU 2686 O MET A 270 14114 13328 13574 81 127 -112 O ATOM 2687 CB MET A 270 -18.458 10.128 12.378 1.00109.63 C ANISOU 2687 CB MET A 270 14375 13473 13808 105 46 -124 C ATOM 2688 CG MET A 270 -17.478 10.945 13.204 1.00111.05 C ANISOU 2688 CG MET A 270 14532 13622 14039 106 23 -126 C ATOM 2689 SD MET A 270 -16.619 9.977 14.473 1.00113.06 S ANISOU 2689 SD MET A 270 14705 13893 14358 103 27 -125 S ATOM 2690 CE MET A 270 -18.002 9.329 15.411 1.00112.40 C ANISOU 2690 CE MET A 270 14596 13889 14224 145 -17 -135 C ATOM 2691 N TYR A 271 -19.527 8.432 10.008 1.00108.48 N ANISOU 2691 N TYR A 271 14284 13342 13592 70 135 -111 N ATOM 2692 CA TYR A 271 -20.583 7.671 9.360 1.00108.10 C ANISOU 2692 CA TYR A 271 14254 13326 13492 75 146 -111 C ATOM 2693 C TYR A 271 -20.052 6.315 8.903 1.00105.98 C ANISOU 2693 C TYR A 271 13960 13056 13252 43 206 -101 C ATOM 2694 O TYR A 271 -20.753 5.311 9.011 1.00106.13 O ANISOU 2694 O TYR A 271 13958 13117 13250 52 209 -102 O ATOM 2695 CB TYR A 271 -21.177 8.444 8.180 1.00111.51 C ANISOU 2695 CB TYR A 271 14759 13736 13873 74 145 -112 C ATOM 2696 CG TYR A 271 -22.064 9.609 8.541 1.00115.85 C ANISOU 2696 CG TYR A 271 15339 14299 14381 112 80 -126 C ATOM 2697 CD1 TYR A 271 -22.723 9.667 9.761 1.00117.33 C ANISOU 2697 CD1 TYR A 271 15489 14533 14556 150 27 -140 C ATOM 2698 CD2 TYR A 271 -22.274 10.645 7.643 1.00118.99 C ANISOU 2698 CD2 TYR A 271 15803 14660 14747 110 71 -126 C ATOM 2699 CE1 TYR A 271 -23.545 10.734 10.089 1.00120.13 C ANISOU 2699 CE1 TYR A 271 15870 14901 14873 186 -33 -155 C ATOM 2700 CE2 TYR A 271 -23.097 11.716 7.952 1.00121.88 C ANISOU 2700 CE2 TYR A 271 16197 15036 15075 146 9 -140 C ATOM 2701 CZ TYR A 271 -23.735 11.762 9.180 1.00122.68 C ANISOU 2701 CZ TYR A 271 16258 15186 15167 185 -43 -156 C ATOM 2702 OH TYR A 271 -24.543 12.817 9.492 1.00124.75 O ANISOU 2702 OH TYR A 271 16546 15459 15393 221 -104 -172 O ATOM 2703 N LEU A 272 -18.809 6.301 8.406 1.00103.84 N ANISOU 2703 N LEU A 272 13687 12736 13030 7 253 -91 N ATOM 2704 CA LEU A 272 -18.216 5.112 7.815 1.00102.71 C ANISOU 2704 CA LEU A 272 13525 12583 12915 -26 314 -83 C ATOM 2705 C LEU A 272 -17.948 4.059 8.889 1.00100.60 C ANISOU 2705 C LEU A 272 13187 12348 12687 -20 311 -83 C ATOM 2706 O LEU A 272 -18.061 2.864 8.623 1.00 98.33 O ANISOU 2706 O LEU A 272 12881 12078 12402 -32 341 -80 O ATOM 2707 CB LEU A 272 -16.932 5.505 7.074 1.00103.54 C ANISOU 2707 CB LEU A 272 13647 12629 13066 -65 363 -75 C ATOM 2708 CG LEU A 272 -16.249 4.401 6.265 1.00103.11 C ANISOU 2708 CG LEU A 272 13580 12558 13041 -102 432 -68 C ATOM 2709 CD1 LEU A 272 -17.213 3.760 5.277 1.00101.74 C ANISOU 2709 CD1 LEU A 272 13442 12404 12810 -102 451 -67 C ATOM 2710 CD2 LEU A 272 -15.028 4.943 5.540 1.00103.11 C ANISOU 2710 CD2 LEU A 272 13599 12498 13080 -140 477 -63 C ATOM 2711 N ALA A 273 -17.602 4.517 10.099 1.00 99.44 N ANISOU 2711 N ALA A 273 13005 12207 12571 -3 271 -88 N ATOM 2712 CA ALA A 273 -17.277 3.628 11.204 1.00 98.39 C ANISOU 2712 CA ALA A 273 12808 12100 12476 3 262 -88 C ATOM 2713 C ALA A 273 -18.547 3.019 11.794 1.00 97.01 C ANISOU 2713 C ALA A 273 12618 11988 12253 33 227 -93 C ATOM 2714 O ALA A 273 -18.534 1.870 12.232 1.00 97.38 O ANISOU 2714 O ALA A 273 12624 12061 12317 30 237 -89 O ATOM 2715 CB ALA A 273 -16.477 4.364 12.250 1.00 98.07 C ANISOU 2715 CB ALA A 273 12738 12042 12481 11 232 -92 C ATOM 2716 N ILE A 274 -19.635 3.799 11.797 1.00 95.00 N ANISOU 2716 N ILE A 274 12398 11757 11942 62 186 -101 N ATOM 2717 CA ILE A 274 -20.901 3.378 12.380 1.00 93.84 C ANISOU 2717 CA ILE A 274 12239 11671 11746 92 150 -108 C ATOM 2718 C ILE A 274 -21.504 2.263 11.528 1.00 93.52 C ANISOU 2718 C ILE A 274 12208 11649 11678 80 185 -103 C ATOM 2719 O ILE A 274 -21.936 1.241 12.061 1.00 93.38 O ANISOU 2719 O ILE A 274 12153 11672 11656 86 181 -102 O ATOM 2720 CB ILE A 274 -21.866 4.572 12.549 1.00 94.08 C ANISOU 2720 CB ILE A 274 12305 11718 11725 127 97 -121 C ATOM 2721 CG1 ILE A 274 -21.316 5.614 13.526 1.00 93.58 C ANISOU 2721 CG1 ILE A 274 12226 11640 11689 143 57 -127 C ATOM 2722 CG2 ILE A 274 -23.252 4.096 12.966 1.00 95.02 C ANISOU 2722 CG2 ILE A 274 12414 11900 11790 156 65 -130 C ATOM 2723 CD1 ILE A 274 -22.039 6.942 13.487 1.00 93.05 C ANISOU 2723 CD1 ILE A 274 12202 11574 11579 171 10 -140 C ATOM 2724 N VAL A 275 -21.518 2.469 10.204 1.00 93.43 N ANISOU 2724 N VAL A 275 12246 11606 11648 62 218 -100 N ATOM 2725 CA VAL A 275 -22.093 1.504 9.279 1.00 92.44 C ANISOU 2725 CA VAL A 275 12136 11494 11494 50 252 -96 C ATOM 2726 C VAL A 275 -21.229 0.242 9.244 1.00 91.85 C ANISOU 2726 C VAL A 275 12019 11409 11469 21 299 -86 C ATOM 2727 O VAL A 275 -21.741 -0.845 8.989 1.00 90.41 O ANISOU 2727 O VAL A 275 11827 11254 11272 17 315 -83 O ATOM 2728 CB VAL A 275 -22.334 2.090 7.871 1.00 91.62 C ANISOU 2728 CB VAL A 275 12099 11357 11355 39 274 -95 C ATOM 2729 CG1 VAL A 275 -23.346 3.227 7.894 1.00 91.05 C ANISOU 2729 CG1 VAL A 275 12069 11299 11229 71 222 -106 C ATOM 2730 CG2 VAL A 275 -21.046 2.528 7.188 1.00 91.11 C ANISOU 2730 CG2 VAL A 275 12054 11232 11333 5 317 -87 C ATOM 2731 N LEU A 276 -19.927 0.398 9.519 1.00 91.26 N ANISOU 2731 N LEU A 276 11921 11297 11456 1 318 -82 N ATOM 2732 CA LEU A 276 -19.012 -0.733 9.555 1.00 90.75 C ANISOU 2732 CA LEU A 276 11815 11221 11446 -26 359 -75 C ATOM 2733 C LEU A 276 -19.279 -1.573 10.802 1.00 91.12 C ANISOU 2733 C LEU A 276 11806 11312 11504 -9 330 -75 C ATOM 2734 O LEU A 276 -19.126 -2.793 10.770 1.00 92.25 O ANISOU 2734 O LEU A 276 11919 11465 11666 -23 355 -70 O ATOM 2735 CB LEU A 276 -17.564 -0.235 9.509 1.00 89.50 C ANISOU 2735 CB LEU A 276 11648 11009 11351 -50 385 -73 C ATOM 2736 CG LEU A 276 -16.495 -1.324 9.399 1.00 88.88 C ANISOU 2736 CG LEU A 276 11528 10909 11332 -80 432 -68 C ATOM 2737 CD1 LEU A 276 -16.635 -2.108 8.103 1.00 86.80 C ANISOU 2737 CD1 LEU A 276 11290 10637 11053 -104 484 -65 C ATOM 2738 CD2 LEU A 276 -15.102 -0.725 9.509 1.00 90.07 C ANISOU 2738 CD2 LEU A 276 11666 11011 11547 -101 450 -69 C ATOM 2739 N ALA A 277 -19.679 -0.908 11.893 1.00 90.74 N ANISOU 2739 N ALA A 277 11744 11289 11443 20 276 -81 N ATOM 2740 CA ALA A 277 -20.064 -1.595 13.115 1.00 91.09 C ANISOU 2740 CA ALA A 277 11741 11380 11489 38 243 -81 C ATOM 2741 C ALA A 277 -21.393 -2.319 12.908 1.00 91.63 C ANISOU 2741 C ALA A 277 11817 11498 11500 51 235 -82 C ATOM 2742 O ALA A 277 -21.599 -3.402 13.452 1.00 91.65 O ANISOU 2742 O ALA A 277 11782 11531 11508 50 234 -77 O ATOM 2743 CB ALA A 277 -20.133 -0.620 14.265 1.00 90.79 C ANISOU 2743 CB ALA A 277 11691 11354 11449 66 190 -88 C ATOM 2744 N HIS A 278 -22.280 -1.711 12.108 1.00 91.66 N ANISOU 2744 N HIS A 278 11869 11506 11450 62 230 -88 N ATOM 2745 CA HIS A 278 -23.606 -2.252 11.854 1.00 91.68 C ANISOU 2745 CA HIS A 278 11884 11555 11396 76 219 -91 C ATOM 2746 C HIS A 278 -23.530 -3.484 10.954 1.00 92.71 C ANISOU 2746 C HIS A 278 12014 11678 11532 50 268 -82 C ATOM 2747 O HIS A 278 -24.385 -4.363 11.041 1.00 92.87 O ANISOU 2747 O HIS A 278 12022 11740 11526 56 263 -82 O ATOM 2748 CB HIS A 278 -24.532 -1.181 11.261 1.00 91.04 C ANISOU 2748 CB HIS A 278 11856 11477 11258 97 196 -102 C ATOM 2749 CG HIS A 278 -24.958 -0.138 12.238 1.00 91.30 C ANISOU 2749 CG HIS A 278 11885 11532 11273 130 140 -113 C ATOM 2750 ND1 HIS A 278 -25.678 0.975 11.856 1.00 91.79 N ANISOU 2750 ND1 HIS A 278 11993 11593 11290 151 111 -125 N ATOM 2751 CD2 HIS A 278 -24.763 -0.024 13.570 1.00 90.84 C ANISOU 2751 CD2 HIS A 278 11785 11496 11234 145 106 -116 C ATOM 2752 CE1 HIS A 278 -25.921 1.724 12.911 1.00 91.55 C ANISOU 2752 CE1 HIS A 278 11947 11585 11253 179 62 -135 C ATOM 2753 NE2 HIS A 278 -25.366 1.136 13.975 1.00 91.47 N ANISOU 2753 NE2 HIS A 278 11883 11589 11281 176 59 -130 N ATOM 2754 N THR A 279 -22.497 -3.534 10.102 1.00 93.44 N ANISOU 2754 N THR A 279 12120 11720 11663 20 315 -76 N ATOM 2755 CA THR A 279 -22.361 -4.563 9.081 1.00 93.80 C ANISOU 2755 CA THR A 279 12173 11753 11713 -5 364 -70 C ATOM 2756 C THR A 279 -22.153 -5.933 9.726 1.00 94.28 C ANISOU 2756 C THR A 279 12179 11836 11806 -14 372 -64 C ATOM 2757 O THR A 279 -22.468 -6.955 9.120 1.00 94.22 O ANISOU 2757 O THR A 279 12172 11838 11789 -26 398 -60 O ATOM 2758 CB THR A 279 -21.261 -4.198 8.074 1.00 93.10 C ANISOU 2758 CB THR A 279 12111 11605 11657 -35 412 -68 C ATOM 2759 OG1 THR A 279 -21.496 -2.854 7.652 1.00 92.53 O ANISOU 2759 OG1 THR A 279 12089 11515 11555 -25 396 -73 O ATOM 2760 CG2 THR A 279 -21.223 -5.104 6.863 1.00 92.83 C ANISOU 2760 CG2 THR A 279 12095 11557 11620 -59 463 -64 C ATOM 2761 N ASN A 280 -21.638 -5.939 10.962 1.00 94.78 N ANISOU 2761 N ASN A 280 12199 11908 11907 -7 347 -62 N ATOM 2762 CA ASN A 280 -21.370 -7.166 11.697 1.00 96.57 C ANISOU 2762 CA ASN A 280 12374 12153 12166 -15 348 -56 C ATOM 2763 C ASN A 280 -22.636 -8.020 11.776 1.00 96.97 C ANISOU 2763 C ASN A 280 12419 12255 12168 -3 334 -54 C ATOM 2764 O ASN A 280 -22.559 -9.248 11.791 1.00 96.18 O ANISOU 2764 O ASN A 280 12293 12165 12087 -17 351 -47 O ATOM 2765 CB ASN A 280 -20.766 -6.880 13.076 1.00 97.31 C ANISOU 2765 CB ASN A 280 12426 12250 12297 -5 314 -55 C ATOM 2766 CG ASN A 280 -20.765 -8.082 13.997 1.00 97.80 C ANISOU 2766 CG ASN A 280 12438 12341 12380 -6 303 -48 C ATOM 2767 OD1 ASN A 280 -21.429 -8.074 15.031 1.00 96.83 O ANISOU 2767 OD1 ASN A 280 12297 12262 12234 15 261 -48 O ATOM 2768 ND2 ASN A 280 -20.038 -9.124 13.623 1.00 98.67 N ANISOU 2768 ND2 ASN A 280 12528 12428 12532 -32 340 -42 N ATOM 2769 N SER A 281 -23.797 -7.356 11.804 1.00 98.69 N ANISOU 2769 N SER A 281 12664 12506 12327 22 301 -61 N ATOM 2770 CA SER A 281 -25.084 -8.024 11.922 1.00101.26 C ANISOU 2770 CA SER A 281 12986 12883 12605 36 283 -62 C ATOM 2771 C SER A 281 -25.400 -8.839 10.668 1.00103.50 C ANISOU 2771 C SER A 281 13293 13159 12873 18 323 -59 C ATOM 2772 O SER A 281 -26.205 -9.766 10.719 1.00103.28 O ANISOU 2772 O SER A 281 13253 13168 12822 20 319 -57 O ATOM 2773 CB SER A 281 -26.181 -7.034 12.226 1.00 99.93 C ANISOU 2773 CB SER A 281 12840 12749 12381 67 240 -74 C ATOM 2774 OG SER A 281 -25.913 -6.340 13.436 1.00 99.56 O ANISOU 2774 OG SER A 281 12769 12712 12347 85 202 -77 O ATOM 2775 N VAL A 282 -24.751 -8.494 9.549 1.00106.01 N ANISOU 2775 N VAL A 282 13646 13429 13205 0 361 -60 N ATOM 2776 CA VAL A 282 -25.053 -9.099 8.261 1.00106.69 C ANISOU 2776 CA VAL A 282 13763 13504 13272 -15 398 -59 C ATOM 2777 C VAL A 282 -24.121 -10.285 8.007 1.00108.63 C ANISOU 2777 C VAL A 282 13979 13726 13569 -44 440 -51 C ATOM 2778 O VAL A 282 -24.509 -11.239 7.335 1.00109.33 O ANISOU 2778 O VAL A 282 14072 13822 13645 -54 463 -49 O ATOM 2779 CB VAL A 282 -24.993 -8.061 7.119 1.00105.53 C ANISOU 2779 CB VAL A 282 13674 13320 13101 -17 415 -65 C ATOM 2780 CG1 VAL A 282 -25.202 -8.690 5.750 1.00105.23 C ANISOU 2780 CG1 VAL A 282 13669 13267 13045 -35 456 -64 C ATOM 2781 CG2 VAL A 282 -25.980 -6.922 7.333 1.00104.45 C ANISOU 2781 CG2 VAL A 282 13567 13206 12912 13 370 -75 C ATOM 2782 N VAL A 283 -22.905 -10.231 8.565 1.00109.20 N ANISOU 2782 N VAL A 283 14020 13770 13700 -56 449 -48 N ATOM 2783 CA VAL A 283 -21.832 -11.133 8.169 1.00110.28 C ANISOU 2783 CA VAL A 283 14136 13874 13892 -85 493 -43 C ATOM 2784 C VAL A 283 -21.990 -12.505 8.823 1.00112.92 C ANISOU 2784 C VAL A 283 14424 14236 14244 -88 486 -37 C ATOM 2785 O VAL A 283 -21.373 -13.469 8.374 1.00114.37 O ANISOU 2785 O VAL A 283 14593 14400 14464 -110 521 -34 O ATOM 2786 CB VAL A 283 -20.434 -10.536 8.438 1.00109.70 C ANISOU 2786 CB VAL A 283 14048 13756 13878 -98 507 -44 C ATOM 2787 CG1 VAL A 283 -20.251 -9.181 7.773 1.00110.35 C ANISOU 2787 CG1 VAL A 283 14176 13807 13943 -97 515 -50 C ATOM 2788 CG2 VAL A 283 -20.105 -10.459 9.922 1.00110.65 C ANISOU 2788 CG2 VAL A 283 14121 13892 14028 -85 468 -42 C ATOM 2789 N ASN A 284 -22.812 -12.589 9.876 1.00117.35 N ANISOU 2789 N ASN A 284 14963 14844 14779 -67 440 -34 N ATOM 2790 CA ASN A 284 -22.898 -13.788 10.699 1.00121.25 C ANISOU 2790 CA ASN A 284 15413 15366 15292 -70 427 -26 C ATOM 2791 C ASN A 284 -23.495 -14.963 9.919 1.00124.24 C ANISOU 2791 C ASN A 284 15796 15756 15652 -82 450 -23 C ATOM 2792 O ASN A 284 -22.882 -16.030 9.872 1.00120.92 O ANISOU 2792 O ASN A 284 15349 15322 15273 -101 471 -17 O ATOM 2793 CB ASN A 284 -23.567 -13.522 12.053 1.00120.39 C ANISOU 2793 CB ASN A 284 15280 15302 15160 -47 374 -24 C ATOM 2794 CG ASN A 284 -22.669 -12.789 13.029 1.00119.70 C ANISOU 2794 CG ASN A 284 15170 15198 15111 -41 354 -25 C ATOM 2795 OD1 ASN A 284 -21.452 -12.754 12.863 1.00120.28 O ANISOU 2795 OD1 ASN A 284 15233 15227 15239 -58 379 -25 O ATOM 2796 ND2 ASN A 284 -23.263 -12.194 14.050 1.00119.86 N ANISOU 2796 ND2 ASN A 284 15182 15255 15104 -18 309 -26 N ATOM 2797 N PRO A 285 -24.695 -14.831 9.297 1.00127.67 N ANISOU 2797 N PRO A 285 16264 16217 16026 -70 444 -26 N ATOM 2798 CA PRO A 285 -25.319 -15.950 8.582 1.00127.89 C ANISOU 2798 CA PRO A 285 16299 16259 16036 -79 462 -24 C ATOM 2799 C PRO A 285 -24.557 -16.445 7.354 1.00127.67 C ANISOU 2799 C PRO A 285 16287 16186 16037 -104 515 -26 C ATOM 2800 O PRO A 285 -24.718 -17.595 6.951 1.00127.09 O ANISOU 2800 O PRO A 285 16203 16116 15968 -116 532 -22 O ATOM 2801 CB PRO A 285 -26.700 -15.416 8.166 1.00128.32 C ANISOU 2801 CB PRO A 285 16389 16345 16020 -59 442 -31 C ATOM 2802 CG PRO A 285 -26.543 -13.911 8.173 1.00129.67 C ANISOU 2802 CG PRO A 285 16589 16501 16178 -44 430 -39 C ATOM 2803 CD PRO A 285 -25.536 -13.622 9.267 1.00129.18 C ANISOU 2803 CD PRO A 285 16490 16427 16165 -46 417 -35 C ATOM 2804 N PHE A 286 -23.728 -15.571 6.769 1.00129.18 N ANISOU 2804 N PHE A 286 16503 16335 16246 -111 540 -31 N ATOM 2805 CA PHE A 286 -22.946 -15.924 5.595 1.00130.57 C ANISOU 2805 CA PHE A 286 16696 16468 16448 -135 593 -35 C ATOM 2806 C PHE A 286 -21.837 -16.905 5.965 1.00130.43 C ANISOU 2806 C PHE A 286 16631 16429 16498 -155 612 -31 C ATOM 2807 O PHE A 286 -21.420 -17.706 5.130 1.00133.48 O ANISOU 2807 O PHE A 286 17019 16793 16905 -174 651 -34 O ATOM 2808 CB PHE A 286 -22.379 -14.677 4.912 1.00131.18 C ANISOU 2808 CB PHE A 286 16813 16506 16524 -139 614 -41 C ATOM 2809 CG PHE A 286 -23.308 -14.031 3.915 1.00130.61 C ANISOU 2809 CG PHE A 286 16799 16438 16389 -130 616 -46 C ATOM 2810 CD1 PHE A 286 -24.228 -13.074 4.319 1.00130.78 C ANISOU 2810 CD1 PHE A 286 16842 16488 16363 -104 574 -48 C ATOM 2811 CD2 PHE A 286 -23.265 -14.383 2.573 1.00129.77 C ANISOU 2811 CD2 PHE A 286 16727 16309 16270 -146 659 -49 C ATOM 2812 CE1 PHE A 286 -25.084 -12.482 3.402 1.00130.90 C ANISOU 2812 CE1 PHE A 286 16910 16504 16320 -94 572 -54 C ATOM 2813 CE2 PHE A 286 -24.121 -13.790 1.657 1.00130.01 C ANISOU 2813 CE2 PHE A 286 16814 16342 16242 -137 658 -54 C ATOM 2814 CZ PHE A 286 -25.028 -12.841 2.074 1.00131.11 C ANISOU 2814 CZ PHE A 286 16974 16507 16337 -111 614 -56 C ATOM 2815 N ILE A 287 -21.369 -16.836 7.217 1.00126.21 N ANISOU 2815 N ILE A 287 16055 15901 15997 -150 584 -27 N ATOM 2816 CA ILE A 287 -20.272 -17.677 7.666 1.00124.16 C ANISOU 2816 CA ILE A 287 15751 15619 15806 -167 596 -25 C ATOM 2817 C ILE A 287 -20.781 -19.095 7.919 1.00125.05 C ANISOU 2817 C ILE A 287 15836 15759 15918 -170 587 -17 C ATOM 2818 O ILE A 287 -20.105 -20.061 7.573 1.00126.25 O ANISOU 2818 O ILE A 287 15968 15887 16112 -189 615 -19 O ATOM 2819 CB ILE A 287 -19.552 -17.069 8.888 1.00123.06 C ANISOU 2819 CB ILE A 287 15579 15473 15703 -160 568 -23 C ATOM 2820 CG1 ILE A 287 -18.912 -15.714 8.567 1.00122.17 C ANISOU 2820 CG1 ILE A 287 15492 15328 15599 -160 581 -30 C ATOM 2821 CG2 ILE A 287 -18.537 -18.045 9.467 1.00123.71 C ANISOU 2821 CG2 ILE A 287 15612 15538 15855 -175 573 -20 C ATOM 2822 CD1 ILE A 287 -17.976 -15.720 7.373 1.00118.83 C ANISOU 2822 CD1 ILE A 287 15086 14856 15207 -184 637 -38 C ATOM 2823 N TYR A 288 -21.980 -19.208 8.504 1.00124.86 N ANISOU 2823 N TYR A 288 15812 15782 15846 -153 549 -11 N ATOM 2824 CA TYR A 288 -22.562 -20.504 8.817 1.00123.87 C ANISOU 2824 CA TYR A 288 15663 15687 15716 -156 536 -3 C ATOM 2825 C TYR A 288 -22.809 -21.296 7.535 1.00122.37 C ANISOU 2825 C TYR A 288 15494 15485 15515 -169 573 -6 C ATOM 2826 O TYR A 288 -22.447 -22.466 7.454 1.00120.60 O ANISOU 2826 O TYR A 288 15246 15252 15325 -184 586 -3 O ATOM 2827 CB TYR A 288 -23.852 -20.356 9.629 1.00125.26 C ANISOU 2827 CB TYR A 288 15836 15918 15838 -135 490 4 C ATOM 2828 CG TYR A 288 -23.736 -19.509 10.871 1.00126.64 C ANISOU 2828 CG TYR A 288 15994 16108 16015 -119 452 6 C ATOM 2829 CD1 TYR A 288 -22.679 -19.669 11.755 1.00126.89 C ANISOU 2829 CD1 TYR A 288 15989 16121 16103 -126 444 10 C ATOM 2830 CD2 TYR A 288 -24.698 -18.558 11.175 1.00126.13 C ANISOU 2830 CD2 TYR A 288 15950 16078 15897 -96 422 2 C ATOM 2831 CE1 TYR A 288 -22.574 -18.896 12.901 1.00128.34 C ANISOU 2831 CE1 TYR A 288 16156 16318 16287 -111 408 11 C ATOM 2832 CE2 TYR A 288 -24.608 -17.776 12.316 1.00126.33 C ANISOU 2832 CE2 TYR A 288 15960 16118 15922 -81 387 3 C ATOM 2833 CZ TYR A 288 -23.541 -17.945 13.181 1.00127.77 C ANISOU 2833 CZ TYR A 288 16106 16281 16160 -88 379 8 C ATOM 2834 OH TYR A 288 -23.447 -17.180 14.307 1.00126.89 O ANISOU 2834 OH TYR A 288 15979 16183 16048 -72 343 8 O ATOM 2835 N ALA A 289 -23.415 -20.640 6.539 1.00124.19 N ANISOU 2835 N ALA A 289 15771 15715 15699 -163 588 -13 N ATOM 2836 CA ALA A 289 -23.806 -21.286 5.296 1.00128.33 C ANISOU 2836 CA ALA A 289 16323 16232 16203 -172 619 -18 C ATOM 2837 C ALA A 289 -22.579 -21.758 4.517 1.00131.64 C ANISOU 2837 C ALA A 289 16739 16604 16676 -196 668 -24 C ATOM 2838 O ALA A 289 -22.617 -22.807 3.875 1.00132.39 O ANISOU 2838 O ALA A 289 16831 16692 16779 -208 689 -25 O ATOM 2839 CB ALA A 289 -24.659 -20.351 4.475 1.00127.94 C ANISOU 2839 CB ALA A 289 16327 16191 16094 -159 620 -24 C ATOM 2840 N TYR A 290 -21.493 -20.981 4.587 1.00134.51 N ANISOU 2840 N TYR A 290 17099 16932 17076 -202 684 -29 N ATOM 2841 CA TYR A 290 -20.300 -21.262 3.803 1.00136.54 C ANISOU 2841 CA TYR A 290 17354 17143 17383 -225 733 -37 C ATOM 2842 C TYR A 290 -19.419 -22.303 4.490 1.00135.20 C ANISOU 2842 C TYR A 290 17130 16961 17280 -237 732 -36 C ATOM 2843 O TYR A 290 -18.616 -22.955 3.826 1.00137.85 O ANISOU 2843 O TYR A 290 17456 17265 17655 -255 771 -44 O ATOM 2844 CB TYR A 290 -19.526 -19.977 3.496 1.00142.05 C ANISOU 2844 CB TYR A 290 18074 17807 18092 -229 754 -44 C ATOM 2845 CG TYR A 290 -19.762 -19.410 2.118 1.00148.28 C ANISOU 2845 CG TYR A 290 18920 18579 18842 -234 789 -51 C ATOM 2846 CD1 TYR A 290 -20.888 -18.650 1.838 1.00151.46 C ANISOU 2846 CD1 TYR A 290 19366 19005 19177 -217 769 -49 C ATOM 2847 CD2 TYR A 290 -18.856 -19.628 1.091 1.00150.40 C ANISOU 2847 CD2 TYR A 290 19199 18807 19140 -257 843 -61 C ATOM 2848 CE1 TYR A 290 -21.111 -18.124 0.575 1.00153.86 C ANISOU 2848 CE1 TYR A 290 19725 19290 19443 -222 799 -55 C ATOM 2849 CE2 TYR A 290 -19.063 -19.110 -0.178 1.00153.09 C ANISOU 2849 CE2 TYR A 290 19595 19131 19443 -264 877 -67 C ATOM 2850 CZ TYR A 290 -20.195 -18.355 -0.437 1.00154.17 C ANISOU 2850 CZ TYR A 290 19776 19289 19511 -246 853 -63 C ATOM 2851 OH TYR A 290 -20.410 -17.841 -1.683 1.00155.04 O ANISOU 2851 OH TYR A 290 19944 19382 19582 -252 883 -68 O ATOM 2852 N ARG A 291 -19.574 -22.461 5.812 1.00130.72 N ANISOU 2852 N ARG A 291 16526 16418 16722 -226 688 -26 N ATOM 2853 CA ARG A 291 -18.642 -23.272 6.582 1.00128.58 C ANISOU 2853 CA ARG A 291 16205 16132 16517 -236 682 -24 C ATOM 2854 C ARG A 291 -19.340 -24.476 7.210 1.00127.72 C ANISOU 2854 C ARG A 291 16070 16056 16401 -233 651 -13 C ATOM 2855 O ARG A 291 -18.833 -25.593 7.120 1.00129.20 O ANISOU 2855 O ARG A 291 16231 16228 16631 -247 662 -14 O ATOM 2856 CB ARG A 291 -17.892 -22.418 7.609 1.00126.44 C ANISOU 2856 CB ARG A 291 15912 15850 16279 -230 660 -23 C ATOM 2857 CG ARG A 291 -16.877 -21.464 6.995 1.00124.84 C ANISOU 2857 CG ARG A 291 15725 15605 16105 -240 696 -35 C ATOM 2858 CD ARG A 291 -15.910 -20.907 8.020 1.00124.18 C ANISOU 2858 CD ARG A 291 15608 15504 16071 -238 677 -36 C ATOM 2859 NE ARG A 291 -15.121 -21.952 8.658 1.00126.12 N ANISOU 2859 NE ARG A 291 15805 15736 16380 -247 671 -36 N ATOM 2860 CZ ARG A 291 -13.925 -22.363 8.247 1.00128.23 C ANISOU 2860 CZ ARG A 291 16051 15962 16711 -266 706 -48 C ATOM 2861 NH1 ARG A 291 -13.357 -21.813 7.187 1.00130.14 N ANISOU 2861 NH1 ARG A 291 16315 16171 16961 -279 753 -60 N ATOM 2862 NH2 ARG A 291 -13.298 -23.323 8.903 1.00127.23 N ANISOU 2862 NH2 ARG A 291 15878 15824 16638 -271 692 -48 N ATOM 2863 N ILE A 292 -20.487 -24.242 7.858 1.00127.67 N ANISOU 2863 N ILE A 292 16070 16095 16343 -216 611 -2 N ATOM 2864 CA ILE A 292 -21.243 -25.315 8.486 1.00128.95 C ANISOU 2864 CA ILE A 292 16210 16292 16492 -215 580 10 C ATOM 2865 C ILE A 292 -22.116 -25.980 7.424 1.00131.02 C ANISOU 2865 C ILE A 292 16499 16567 16717 -218 599 8 C ATOM 2866 O ILE A 292 -22.898 -25.313 6.750 1.00131.12 O ANISOU 2866 O ILE A 292 16551 16592 16676 -209 605 4 O ATOM 2867 CB ILE A 292 -22.071 -24.802 9.684 1.00127.90 C ANISOU 2867 CB ILE A 292 16070 16204 16321 -196 531 20 C ATOM 2868 CG1 ILE A 292 -21.185 -24.153 10.754 1.00126.57 C ANISOU 2868 CG1 ILE A 292 15876 16024 16192 -192 510 22 C ATOM 2869 CG2 ILE A 292 -22.930 -25.918 10.263 1.00126.49 C ANISOU 2869 CG2 ILE A 292 15872 16065 16125 -197 502 34 C ATOM 2870 CD1 ILE A 292 -21.940 -23.332 11.778 1.00125.47 C ANISOU 2870 CD1 ILE A 292 15737 15924 16011 -171 467 28 C ATOM 2871 N ARG A 293 -21.974 -27.304 7.298 1.00136.09 N ANISOU 2871 N ARG A 293 17120 17203 17387 -232 605 11 N ATOM 2872 CA ARG A 293 -22.631 -28.054 6.241 1.00139.94 C ANISOU 2872 CA ARG A 293 17629 17695 17848 -237 625 8 C ATOM 2873 C ARG A 293 -24.111 -28.250 6.565 1.00136.84 C ANISOU 2873 C ARG A 293 17245 17354 17395 -225 592 18 C ATOM 2874 O ARG A 293 -24.940 -28.264 5.658 1.00136.25 O ANISOU 2874 O ARG A 293 17203 17290 17276 -222 604 14 O ATOM 2875 CB ARG A 293 -21.923 -29.391 6.001 1.00147.24 C ANISOU 2875 CB ARG A 293 18526 18594 18826 -255 642 6 C ATOM 2876 CG ARG A 293 -22.284 -30.050 4.677 1.00153.87 C ANISOU 2876 CG ARG A 293 19392 19424 19649 -263 675 -2 C ATOM 2877 CD ARG A 293 -21.555 -31.359 4.441 1.00159.06 C ANISOU 2877 CD ARG A 293 20021 20054 20361 -280 690 -7 C ATOM 2878 NE ARG A 293 -20.107 -31.197 4.430 1.00161.95 N ANISOU 2878 NE ARG A 293 20367 20377 20791 -290 716 -18 N ATOM 2879 CZ ARG A 293 -19.236 -32.150 4.114 1.00163.47 C ANISOU 2879 CZ ARG A 293 20535 20537 21039 -304 736 -27 C ATOM 2880 NH1 ARG A 293 -17.940 -31.893 4.141 1.00164.05 N ANISOU 2880 NH1 ARG A 293 20589 20572 21170 -312 758 -39 N ATOM 2881 NH2 ARG A 293 -19.659 -33.355 3.772 1.00165.02 N ANISOU 2881 NH2 ARG A 293 20727 20739 21235 -310 734 -26 N ATOM 2882 N GLU A 294 -24.430 -28.406 7.856 1.00133.26 N ANISOU 2882 N GLU A 294 16763 16932 16940 -220 550 32 N ATOM 2883 CA GLU A 294 -25.798 -28.672 8.271 1.00130.16 C ANISOU 2883 CA GLU A 294 16372 16590 16494 -210 517 41 C ATOM 2884 C GLU A 294 -26.658 -27.430 8.055 1.00128.11 C ANISOU 2884 C GLU A 294 16147 16354 16174 -191 510 35 C ATOM 2885 O GLU A 294 -27.787 -27.541 7.584 1.00126.91 O ANISOU 2885 O GLU A 294 16016 16231 15973 -184 505 34 O ATOM 2886 CB GLU A 294 -25.854 -29.172 9.716 1.00132.66 C ANISOU 2886 CB GLU A 294 16648 16932 16824 -212 477 57 C ATOM 2887 CG GLU A 294 -27.211 -29.742 10.107 1.00135.16 C ANISOU 2887 CG GLU A 294 16962 17300 17093 -208 447 68 C ATOM 2888 CD GLU A 294 -27.600 -31.061 9.458 1.00135.13 C ANISOU 2888 CD GLU A 294 16957 17295 17092 -222 458 72 C ATOM 2889 OE1 GLU A 294 -26.694 -31.802 9.025 1.00137.75 O ANISOU 2889 OE1 GLU A 294 17277 17587 17473 -237 480 69 O ATOM 2890 OE2 GLU A 294 -28.811 -31.348 9.390 1.00132.34 O ANISOU 2890 OE2 GLU A 294 16612 16980 16692 -218 443 76 O ATOM 2891 N PHE A 295 -26.108 -26.256 8.392 1.00127.08 N ANISOU 2891 N PHE A 295 16022 16212 16051 -182 508 30 N ATOM 2892 CA PHE A 295 -26.800 -24.989 8.208 1.00125.67 C ANISOU 2892 CA PHE A 295 15877 16051 15821 -162 499 23 C ATOM 2893 C PHE A 295 -27.023 -24.717 6.723 1.00127.36 C ANISOU 2893 C PHE A 295 16136 16245 16011 -163 534 11 C ATOM 2894 O PHE A 295 -28.031 -24.121 6.349 1.00127.43 O ANISOU 2894 O PHE A 295 16176 16278 15965 -148 524 6 O ATOM 2895 CB PHE A 295 -26.022 -23.836 8.849 1.00123.59 C ANISOU 2895 CB PHE A 295 15609 15773 15578 -154 491 20 C ATOM 2896 CG PHE A 295 -26.456 -23.477 10.248 1.00121.88 C ANISOU 2896 CG PHE A 295 15368 15595 15346 -140 445 28 C ATOM 2897 CD1 PHE A 295 -27.720 -22.959 10.490 1.00121.92 C ANISOU 2897 CD1 PHE A 295 15388 15647 15291 -121 418 26 C ATOM 2898 CD2 PHE A 295 -25.595 -23.640 11.324 1.00120.75 C ANISOU 2898 CD2 PHE A 295 15188 15443 15249 -145 430 35 C ATOM 2899 CE1 PHE A 295 -28.119 -22.631 11.777 1.00121.82 C ANISOU 2899 CE1 PHE A 295 15353 15671 15262 -108 378 32 C ATOM 2900 CE2 PHE A 295 -25.992 -23.308 12.610 1.00119.54 C ANISOU 2900 CE2 PHE A 295 15014 15326 15079 -132 388 42 C ATOM 2901 CZ PHE A 295 -27.253 -22.804 12.835 1.00120.43 C ANISOU 2901 CZ PHE A 295 15142 15486 15130 -114 363 40 C ATOM 2902 N ARG A 296 -26.072 -25.166 5.893 1.00129.99 N ANISOU 2902 N ARG A 296 16473 16535 16385 -181 574 6 N ATOM 2903 CA ARG A 296 -26.089 -24.919 4.460 1.00131.14 C ANISOU 2903 CA ARG A 296 16662 16655 16512 -184 612 -6 C ATOM 2904 C ARG A 296 -27.289 -25.619 3.825 1.00130.09 C ANISOU 2904 C ARG A 296 16547 16548 16334 -181 608 -6 C ATOM 2905 O ARG A 296 -28.096 -24.974 3.158 1.00128.90 O ANISOU 2905 O ARG A 296 16436 16408 16132 -169 608 -12 O ATOM 2906 CB ARG A 296 -24.760 -25.350 3.833 1.00134.19 C ANISOU 2906 CB ARG A 296 17040 16990 16955 -205 656 -12 C ATOM 2907 CG ARG A 296 -24.706 -25.238 2.315 1.00138.22 C ANISOU 2907 CG ARG A 296 17595 17473 17449 -212 699 -24 C ATOM 2908 CD ARG A 296 -23.282 -25.250 1.793 1.00141.59 C ANISOU 2908 CD ARG A 296 18016 17850 17931 -231 743 -32 C ATOM 2909 NE ARG A 296 -22.370 -25.947 2.690 1.00144.32 N ANISOU 2909 NE ARG A 296 18309 18184 18340 -241 736 -28 N ATOM 2910 CZ ARG A 296 -21.182 -26.434 2.346 1.00147.71 C ANISOU 2910 CZ ARG A 296 18720 18575 18827 -259 770 -36 C ATOM 2911 NH1 ARG A 296 -20.438 -27.051 3.249 1.00145.12 N ANISOU 2911 NH1 ARG A 296 18345 18240 18556 -265 756 -33 N ATOM 2912 NH2 ARG A 296 -20.740 -26.305 1.107 1.00151.54 N ANISOU 2912 NH2 ARG A 296 19235 19028 19314 -270 817 -49 N ATOM 2913 N GLN A 297 -27.399 -26.933 4.058 1.00130.53 N ANISOU 2913 N GLN A 297 16573 16613 16409 -192 603 2 N ATOM 2914 CA GLN A 297 -28.441 -27.758 3.464 1.00131.72 C ANISOU 2914 CA GLN A 297 16736 16785 16526 -192 600 2 C ATOM 2915 C GLN A 297 -29.799 -27.403 4.063 1.00129.08 C ANISOU 2915 C GLN A 297 16405 16504 16137 -174 560 7 C ATOM 2916 O GLN A 297 -30.831 -27.624 3.432 1.00128.16 O ANISOU 2916 O GLN A 297 16312 16407 15978 -168 556 3 O ATOM 2917 CB GLN A 297 -28.126 -29.244 3.652 1.00135.63 C ANISOU 2917 CB GLN A 297 17196 17275 17062 -209 602 10 C ATOM 2918 CG GLN A 297 -26.962 -29.732 2.799 1.00141.17 C ANISOU 2918 CG GLN A 297 17899 17927 17813 -226 646 1 C ATOM 2919 CD GLN A 297 -26.372 -31.032 3.289 1.00144.02 C ANISOU 2919 CD GLN A 297 18217 18277 18226 -242 642 8 C ATOM 2920 OE1 GLN A 297 -26.309 -31.303 4.487 1.00146.17 O ANISOU 2920 OE1 GLN A 297 18454 18568 18517 -242 610 20 O ATOM 2921 NE2 GLN A 297 -25.918 -31.851 2.354 1.00145.71 N ANISOU 2921 NE2 GLN A 297 18435 18462 18466 -255 674 -1 N ATOM 2922 N THR A 298 -29.786 -26.855 5.285 1.00128.47 N ANISOU 2922 N THR A 298 16304 16448 16060 -165 529 13 N ATOM 2923 CA THR A 298 -31.011 -26.447 5.953 1.00128.61 C ANISOU 2923 CA THR A 298 16321 16517 16028 -147 490 16 C ATOM 2924 C THR A 298 -31.609 -25.238 5.237 1.00128.96 C ANISOU 2924 C THR A 298 16411 16565 16024 -129 492 2 C ATOM 2925 O THR A 298 -32.823 -25.166 5.064 1.00127.00 O ANISOU 2925 O THR A 298 16177 16350 15726 -116 473 -2 O ATOM 2926 CB THR A 298 -30.793 -26.191 7.451 1.00128.10 C ANISOU 2926 CB THR A 298 16219 16475 15977 -143 458 26 C ATOM 2927 OG1 THR A 298 -30.146 -27.332 8.017 1.00128.49 O ANISOU 2927 OG1 THR A 298 16230 16516 16076 -161 457 38 O ATOM 2928 CG2 THR A 298 -32.083 -25.925 8.195 1.00126.56 C ANISOU 2928 CG2 THR A 298 16018 16337 15732 -126 419 27 C ATOM 2929 N PHE A 299 -30.742 -24.310 4.811 1.00130.65 N ANISOU 2929 N PHE A 299 16648 16741 16253 -128 514 -5 N ATOM 2930 CA PHE A 299 -31.175 -23.051 4.226 1.00131.63 C ANISOU 2930 CA PHE A 299 16817 16863 16335 -111 513 -17 C ATOM 2931 C PHE A 299 -31.865 -23.283 2.884 1.00135.81 C ANISOU 2931 C PHE A 299 17387 17385 16828 -110 531 -26 C ATOM 2932 O PHE A 299 -32.810 -22.572 2.550 1.00138.34 O ANISOU 2932 O PHE A 299 17739 17725 17099 -92 514 -34 O ATOM 2933 CB PHE A 299 -30.003 -22.076 4.078 1.00128.87 C ANISOU 2933 CB PHE A 299 16480 16470 16014 -114 533 -21 C ATOM 2934 CG PHE A 299 -29.497 -21.474 5.366 1.00126.26 C ANISOU 2934 CG PHE A 299 16118 16148 15706 -108 508 -16 C ATOM 2935 CD1 PHE A 299 -30.289 -21.455 6.506 1.00126.85 C ANISOU 2935 CD1 PHE A 299 16167 16270 15759 -93 466 -11 C ATOM 2936 CD2 PHE A 299 -28.235 -20.904 5.433 1.00124.47 C ANISOU 2936 CD2 PHE A 299 15890 15882 15523 -116 527 -17 C ATOM 2937 CE1 PHE A 299 -29.823 -20.896 7.687 1.00126.66 C ANISOU 2937 CE1 PHE A 299 16116 16254 15755 -87 442 -7 C ATOM 2938 CE2 PHE A 299 -27.770 -20.342 6.614 1.00124.22 C ANISOU 2938 CE2 PHE A 299 15830 15856 15513 -109 503 -13 C ATOM 2939 CZ PHE A 299 -28.565 -20.339 7.738 1.00125.09 C ANISOU 2939 CZ PHE A 299 15916 16013 15599 -94 459 -8 C ATOM 2940 N ARG A 300 -31.391 -24.286 2.135 1.00139.40 N ANISOU 2940 N ARG A 300 17841 17814 17310 -129 563 -24 N ATOM 2941 CA ARG A 300 -31.843 -24.525 0.773 1.00142.09 C ANISOU 2941 CA ARG A 300 18224 18141 17623 -131 587 -33 C ATOM 2942 C ARG A 300 -33.324 -24.898 0.761 1.00143.13 C ANISOU 2942 C ARG A 300 18360 18317 17707 -118 557 -35 C ATOM 2943 O ARG A 300 -34.107 -24.289 0.034 1.00141.36 O ANISOU 2943 O ARG A 300 18177 18098 17435 -104 552 -45 O ATOM 2944 CB ARG A 300 -30.979 -25.586 0.084 1.00143.39 C ANISOU 2944 CB ARG A 300 18381 18270 17830 -154 626 -33 C ATOM 2945 CG ARG A 300 -29.504 -25.224 -0.002 1.00145.82 C ANISOU 2945 CG ARG A 300 18684 18533 18188 -168 659 -34 C ATOM 2946 CD ARG A 300 -28.835 -25.827 -1.221 1.00148.33 C ANISOU 2946 CD ARG A 300 19021 18810 18526 -186 706 -41 C ATOM 2947 NE ARG A 300 -27.392 -25.624 -1.202 1.00151.44 N ANISOU 2947 NE ARG A 300 19402 19164 18974 -201 738 -43 N ATOM 2948 CZ ARG A 300 -26.587 -25.769 -2.250 1.00154.39 C ANISOU 2948 CZ ARG A 300 19795 19497 19368 -217 784 -52 C ATOM 2949 NH1 ARG A 300 -27.080 -26.115 -3.428 1.00155.28 N ANISOU 2949 NH1 ARG A 300 19945 19603 19449 -219 805 -60 N ATOM 2950 NH2 ARG A 300 -25.289 -25.557 -2.118 1.00155.78 N ANISOU 2950 NH2 ARG A 300 19954 19639 19595 -231 811 -55 N ATOM 2951 N LYS A 301 -33.694 -25.883 1.588 1.00144.16 N ANISOU 2951 N LYS A 301 18448 18479 17849 -123 536 -25 N ATOM 2952 CA LYS A 301 -35.043 -26.429 1.611 1.00144.07 C ANISOU 2952 CA LYS A 301 18433 18509 17798 -114 510 -25 C ATOM 2953 C LYS A 301 -36.026 -25.414 2.194 1.00142.11 C ANISOU 2953 C LYS A 301 18191 18301 17503 -90 473 -31 C ATOM 2954 O LYS A 301 -37.229 -25.523 1.970 1.00143.41 O ANISOU 2954 O LYS A 301 18366 18497 17626 -79 454 -38 O ATOM 2955 CB LYS A 301 -35.068 -27.777 2.340 1.00145.85 C ANISOU 2955 CB LYS A 301 18611 18753 18052 -130 500 -11 C ATOM 2956 CG LYS A 301 -34.546 -28.951 1.522 1.00149.05 C ANISOU 2956 CG LYS A 301 19016 19127 18490 -150 531 -10 C ATOM 2957 CD LYS A 301 -34.466 -30.253 2.289 1.00149.76 C ANISOU 2957 CD LYS A 301 19059 19231 18612 -166 519 5 C ATOM 2958 CE LYS A 301 -33.967 -31.402 1.437 1.00149.22 C ANISOU 2958 CE LYS A 301 18991 19129 18575 -183 548 4 C ATOM 2959 NZ LYS A 301 -33.727 -32.622 2.243 1.00148.38 N ANISOU 2959 NZ LYS A 301 18840 19032 18508 -200 535 19 N ATOM 2960 N ILE A 302 -35.504 -24.426 2.931 1.00141.40 N ANISOU 2960 N ILE A 302 18095 18209 17422 -82 463 -31 N ATOM 2961 CA ILE A 302 -36.326 -23.339 3.439 1.00143.00 C ANISOU 2961 CA ILE A 302 18307 18445 17583 -58 429 -39 C ATOM 2962 C ILE A 302 -36.597 -22.356 2.301 1.00143.51 C ANISOU 2962 C ILE A 302 18427 18486 17612 -44 438 -54 C ATOM 2963 O ILE A 302 -37.725 -21.896 2.140 1.00145.31 O ANISOU 2963 O ILE A 302 18675 18743 17793 -25 413 -66 O ATOM 2964 CB ILE A 302 -35.688 -22.658 4.671 1.00144.29 C ANISOU 2964 CB ILE A 302 18442 18614 17769 -54 413 -34 C ATOM 2965 CG1 ILE A 302 -35.487 -23.644 5.827 1.00146.08 C ANISOU 2965 CG1 ILE A 302 18614 18864 18026 -67 400 -18 C ATOM 2966 CG2 ILE A 302 -36.506 -21.450 5.108 1.00143.40 C ANISOU 2966 CG2 ILE A 302 18341 18532 17612 -27 378 -45 C ATOM 2967 CD1 ILE A 302 -34.709 -23.083 6.998 1.00145.92 C ANISOU 2967 CD1 ILE A 302 18566 18843 18033 -65 386 -11 C ATOM 2968 N ILE A 303 -35.556 -22.055 1.513 1.00145.49 N ANISOU 2968 N ILE A 303 18706 18687 17886 -56 474 -55 N ATOM 2969 CA ILE A 303 -35.655 -21.106 0.414 1.00147.01 C ANISOU 2969 CA ILE A 303 18955 18852 18048 -46 486 -67 C ATOM 2970 C ILE A 303 -36.541 -21.693 -0.685 1.00150.13 C ANISOU 2970 C ILE A 303 19382 19251 18411 -45 492 -75 C ATOM 2971 O ILE A 303 -37.363 -20.982 -1.262 1.00150.22 O ANISOU 2971 O ILE A 303 19433 19268 18376 -27 477 -87 O ATOM 2972 CB ILE A 303 -34.256 -20.696 -0.098 1.00145.40 C ANISOU 2972 CB ILE A 303 18770 18594 17881 -62 525 -65 C ATOM 2973 CG1 ILE A 303 -33.488 -19.887 0.952 1.00144.21 C ANISOU 2973 CG1 ILE A 303 18595 18439 17757 -59 513 -60 C ATOM 2974 CG2 ILE A 303 -34.351 -19.942 -1.419 1.00144.80 C ANISOU 2974 CG2 ILE A 303 18758 18487 17773 -58 543 -76 C ATOM 2975 CD1 ILE A 303 -31.989 -19.850 0.741 1.00144.47 C ANISOU 2975 CD1 ILE A 303 18625 18424 17841 -81 552 -55 C ATOM 2976 N ARG A 304 -36.385 -22.999 -0.939 1.00153.32 N ANISOU 2976 N ARG A 304 19766 19651 18838 -63 511 -68 N ATOM 2977 CA ARG A 304 -37.095 -23.692 -2.005 1.00154.87 C ANISOU 2977 CA ARG A 304 19988 19846 19010 -64 520 -75 C ATOM 2978 C ARG A 304 -38.557 -23.917 -1.623 1.00154.47 C ANISOU 2978 C ARG A 304 19925 19846 18919 -47 480 -80 C ATOM 2979 O ARG A 304 -39.365 -24.293 -2.471 1.00157.35 O ANISOU 2979 O ARG A 304 20315 20215 19255 -43 479 -88 O ATOM 2980 CB ARG A 304 -36.407 -25.022 -2.331 1.00157.16 C ANISOU 2980 CB ARG A 304 20257 20115 19341 -89 552 -66 C ATOM 2981 CG ARG A 304 -35.058 -24.878 -3.021 1.00160.59 C ANISOU 2981 CG ARG A 304 20711 20496 19810 -106 597 -66 C ATOM 2982 CD ARG A 304 -34.250 -26.159 -2.944 1.00163.95 C ANISOU 2982 CD ARG A 304 21100 20906 20287 -129 622 -58 C ATOM 2983 NE ARG A 304 -32.927 -26.018 -3.537 1.00167.40 N ANISOU 2983 NE ARG A 304 21550 21294 20761 -145 666 -60 N ATOM 2984 CZ ARG A 304 -31.981 -26.953 -3.522 1.00169.37 C ANISOU 2984 CZ ARG A 304 21771 21521 21062 -165 692 -56 C ATOM 2985 NH1 ARG A 304 -30.812 -26.717 -4.093 1.00168.68 N ANISOU 2985 NH1 ARG A 304 21696 21391 21005 -180 733 -60 N ATOM 2986 NH2 ARG A 304 -32.202 -28.117 -2.936 1.00170.47 N ANISOU 2986 NH2 ARG A 304 21868 21681 21222 -172 677 -48 N ATOM 2987 N SER A 305 -38.886 -23.691 -0.345 1.00152.30 N ANISOU 2987 N SER A 305 19612 19611 18645 -38 448 -75 N ATOM 2988 CA SER A 305 -40.241 -23.865 0.155 1.00148.50 C ANISOU 2988 CA SER A 305 19113 19182 18128 -23 410 -81 C ATOM 2989 C SER A 305 -40.574 -22.753 1.160 1.00147.29 C ANISOU 2989 C SER A 305 18948 19059 17955 -3 377 -86 C ATOM 2990 O SER A 305 -41.307 -23.043 2.128 1.00145.42 O ANISOU 2990 O SER A 305 18674 18871 17709 3 348 -84 O ATOM 2991 CB SER A 305 -40.423 -25.239 0.752 1.00146.16 C ANISOU 2991 CB SER A 305 18769 18911 17854 -40 407 -68 C ATOM 2992 OG SER A 305 -40.059 -26.246 -0.182 1.00144.56 O ANISOU 2992 OG SER A 305 18578 18678 17671 -58 438 -64 O TER 2993 SER A 305 HETATM 2994 C1 TEP A2401 -21.366 3.395 19.481 1.00 97.41 C ANISOU 2994 C1 TEP A2401 12480 12294 12239 211 -67 -137 C HETATM 2995 N1 TEP A2401 -21.289 4.787 19.010 1.00 98.27 N ANISOU 2995 N1 TEP A2401 12631 12369 12339 220 -83 -145 N HETATM 2996 C2 TEP A2401 -22.382 5.253 18.266 1.00 98.24 C ANISOU 2996 C2 TEP A2401 12671 12380 12275 235 -92 -154 C HETATM 2997 O2 TEP A2401 -23.340 4.531 18.026 1.00 97.44 O ANISOU 2997 O2 TEP A2401 12570 12319 12133 240 -86 -155 O HETATM 2998 N3 TEP A2401 -22.331 6.554 17.817 1.00 98.95 N ANISOU 2998 N3 TEP A2401 12803 12438 12356 244 -109 -162 N HETATM 2999 C3 TEP A2401 -23.446 7.093 17.034 1.00 98.01 C ANISOU 2999 C3 TEP A2401 12732 12331 12177 260 -123 -171 C HETATM 3000 C4 TEP A2401 -21.233 7.328 18.110 1.00100.43 C ANISOU 3000 C4 TEP A2401 12987 12580 12591 237 -115 -160 C HETATM 3001 C5 TEP A2401 -20.183 6.840 18.838 1.00 99.58 C ANISOU 3001 C5 TEP A2401 12835 12459 12543 222 -105 -153 C HETATM 3002 C6 TEP A2401 -20.138 5.518 19.345 1.00 98.59 C ANISOU 3002 C6 TEP A2401 12664 12363 12431 214 -89 -145 C HETATM 3003 O6 TEP A2401 -19.229 5.017 20.007 1.00 99.26 O ANISOU 3003 O6 TEP A2401 12709 12437 12567 202 -81 -138 O HETATM 3004 N7 TEP A2401 -19.286 7.883 18.929 1.00100.40 N ANISOU 3004 N7 TEP A2401 12948 12515 12683 219 -116 -154 N HETATM 3005 C8 TEP A2401 -19.838 8.908 18.270 1.00102.03 C ANISOU 3005 C8 TEP A2401 13205 12710 12853 231 -132 -162 C HETATM 3006 N9 TEP A2401 -21.033 8.621 17.744 1.00101.80 N ANISOU 3006 N9 TEP A2401 13200 12716 12764 242 -133 -166 N HETATM 3007 C1 CLR A2402 -38.628 10.830 22.576 1.00135.80 C ANISOU 3007 C1 CLR A2402 17466 17774 16358 701 -633 -475 C HETATM 3008 C2 CLR A2402 -38.359 12.297 22.911 1.00134.86 C ANISOU 3008 C2 CLR A2402 17369 17629 16245 731 -682 -495 C HETATM 3009 C3 CLR A2402 -38.909 12.674 24.263 1.00134.48 C ANISOU 3009 C3 CLR A2402 17281 17639 16177 767 -725 -524 C HETATM 3010 C4 CLR A2402 -38.362 11.752 25.339 1.00135.23 C ANISOU 3010 C4 CLR A2402 17324 17764 16293 749 -703 -506 C HETATM 3011 C5 CLR A2402 -38.544 10.280 25.023 1.00136.30 C ANISOU 3011 C5 CLR A2402 17439 17923 16426 716 -653 -482 C HETATM 3012 C6 CLR A2402 -39.028 9.445 25.935 1.00136.33 C ANISOU 3012 C6 CLR A2402 17396 17989 16413 716 -649 -485 C HETATM 3013 C7 CLR A2402 -39.313 7.990 25.719 1.00136.06 C ANISOU 3013 C7 CLR A2402 17339 17984 16373 686 -604 -464 C HETATM 3014 C8 CLR A2402 -38.669 7.421 24.455 1.00135.99 C ANISOU 3014 C8 CLR A2402 17360 17917 16391 649 -558 -434 C HETATM 3015 C9 CLR A2402 -38.755 8.446 23.305 1.00135.58 C ANISOU 3015 C9 CLR A2402 17365 17816 16334 661 -571 -445 C HETATM 3016 C10 CLR A2402 -38.114 9.822 23.631 1.00136.58 C ANISOU 3016 C10 CLR A2402 17511 17904 16479 682 -609 -456 C HETATM 3017 C11 CLR A2402 -38.245 7.878 21.972 1.00134.37 C ANISOU 3017 C11 CLR A2402 17244 17610 16201 624 -524 -417 C HETATM 3018 C12 CLR A2402 -38.930 6.566 21.589 1.00135.11 C ANISOU 3018 C12 CLR A2402 17322 17740 16275 605 -490 -408 C HETATM 3019 C13 CLR A2402 -38.820 5.519 22.702 1.00135.68 C ANISOU 3019 C13 CLR A2402 17338 17858 16355 592 -476 -396 C HETATM 3020 C14 CLR A2402 -39.366 6.141 24.005 1.00136.26 C ANISOU 3020 C14 CLR A2402 17381 17985 16406 628 -523 -424 C HETATM 3021 C15 CLR A2402 -39.484 4.951 24.957 1.00137.93 C ANISOU 3021 C15 CLR A2402 17542 18250 16617 612 -506 -411 C HETATM 3022 C16 CLR A2402 -39.846 3.770 24.027 1.00137.04 C ANISOU 3022 C16 CLR A2402 17433 18139 16497 583 -463 -393 C HETATM 3023 C17 CLR A2402 -39.789 4.315 22.573 1.00135.59 C ANISOU 3023 C17 CLR A2402 17304 17900 16316 582 -455 -394 C HETATM 3024 C18 CLR A2402 -37.371 5.013 22.842 1.00135.86 C ANISOU 3024 C18 CLR A2402 17351 17837 16434 558 -442 -362 C HETATM 3025 C19 CLR A2402 -36.574 9.759 23.588 1.00137.07 C ANISOU 3025 C19 CLR A2402 17577 17905 16598 651 -582 -425 C HETATM 3026 C20 CLR A2402 -39.483 3.247 21.510 1.00135.22 C ANISOU 3026 C20 CLR A2402 17270 17823 16285 544 -404 -366 C HETATM 3027 C21 CLR A2402 -40.046 3.601 20.135 1.00135.74 C ANISOU 3027 C21 CLR A2402 17385 17862 16329 549 -401 -376 C HETATM 3028 C22 CLR A2402 -39.975 1.869 21.970 1.00135.63 C ANISOU 3028 C22 CLR A2402 17279 17927 16326 526 -382 -356 C HETATM 3029 C23 CLR A2402 -39.841 0.770 20.953 1.00135.69 C ANISOU 3029 C23 CLR A2402 17299 17913 16346 492 -336 -332 C HETATM 3030 C24 CLR A2402 -41.053 -0.122 20.889 1.00135.26 C ANISOU 3030 C24 CLR A2402 17224 17915 16254 492 -330 -339 C HETATM 3031 C25 CLR A2402 -40.783 -1.553 20.441 1.00135.55 C ANISOU 3031 C25 CLR A2402 17249 17945 16310 454 -284 -311 C HETATM 3032 C26 CLR A2402 -41.424 -2.560 21.385 1.00136.46 C ANISOU 3032 C26 CLR A2402 17315 18126 16408 447 -284 -308 C HETATM 3033 C27 CLR A2402 -41.251 -1.785 19.012 1.00133.86 C ANISOU 3033 C27 CLR A2402 17073 17708 16082 446 -264 -311 C HETATM 3034 O1 CLR A2402 -38.530 14.027 24.549 1.00133.87 O ANISOU 3034 O1 CLR A2402 17224 17530 16110 793 -770 -540 O HETATM 3035 C1 CLR A2403 -2.767 8.895 22.339 1.00137.26 C ANISOU 3035 C1 CLR A2403 17248 16633 18273 -21 33 -149 C HETATM 3036 C2 CLR A2403 -2.521 10.405 22.412 1.00136.97 C ANISOU 3036 C2 CLR A2403 17236 16563 18243 -15 4 -153 C HETATM 3037 C3 CLR A2403 -1.685 10.918 21.261 1.00137.32 C ANISOU 3037 C3 CLR A2403 17300 16552 18322 -56 57 -151 C HETATM 3038 C4 CLR A2403 -2.265 10.475 19.930 1.00136.16 C ANISOU 3038 C4 CLR A2403 17192 16415 18128 -79 112 -141 C HETATM 3039 C5 CLR A2403 -2.491 8.979 19.880 1.00137.35 C ANISOU 3039 C5 CLR A2403 17315 16598 18275 -83 140 -138 C HETATM 3040 C6 CLR A2403 -1.913 8.237 18.947 1.00137.20 C ANISOU 3040 C6 CLR A2403 17288 16558 18284 -119 205 -135 C HETATM 3041 C7 CLR A2403 -1.915 6.743 18.947 1.00135.68 C ANISOU 3041 C7 CLR A2403 17061 16390 18103 -126 232 -134 C HETATM 3042 C8 CLR A2403 -3.169 6.199 19.622 1.00136.96 C ANISOU 3042 C8 CLR A2403 17225 16612 18201 -90 190 -131 C HETATM 3043 C9 CLR A2403 -3.354 6.850 21.007 1.00136.96 C ANISOU 3043 C9 CLR A2403 17210 16628 18199 -53 117 -136 C HETATM 3044 C10 CLR A2403 -3.365 8.408 20.997 1.00137.91 C ANISOU 3044 C10 CLR A2403 17365 16724 18308 -43 88 -139 C HETATM 3045 C11 CLR A2403 -4.570 6.263 21.743 1.00135.99 C ANISOU 3045 C11 CLR A2403 17085 16568 18015 -18 77 -134 C HETATM 3046 C12 CLR A2403 -4.568 4.732 21.816 1.00136.95 C ANISOU 3046 C12 CLR A2403 17173 16713 18149 -27 101 -130 C HETATM 3047 C13 CLR A2403 -4.359 4.065 20.451 1.00138.55 C ANISOU 3047 C13 CLR A2403 17388 16897 18356 -63 172 -125 C HETATM 3048 C14 CLR A2403 -3.100 4.690 19.814 1.00138.61 C ANISOU 3048 C14 CLR A2403 17395 16844 18428 -95 209 -130 C HETATM 3049 C15 CLR A2403 -2.780 3.780 18.630 1.00138.97 C ANISOU 3049 C15 CLR A2403 17440 16875 18486 -131 280 -127 C HETATM 3050 C16 CLR A2403 -3.202 2.380 19.122 1.00138.48 C ANISOU 3050 C16 CLR A2403 17347 16853 18417 -120 273 -124 C HETATM 3051 C17 CLR A2403 -3.906 2.577 20.494 1.00137.70 C ANISOU 3051 C17 CLR A2403 17238 16794 18288 -79 201 -124 C HETATM 3052 C18 CLR A2403 -5.619 4.222 19.574 1.00140.59 C ANISOU 3052 C18 CLR A2403 17700 17186 18531 -58 184 -118 C HETATM 3053 C19 CLR A2403 -4.795 8.961 20.833 1.00139.02 C ANISOU 3053 C19 CLR A2403 17557 16906 18360 -16 59 -136 C HETATM 3054 C20 CLR A2403 -4.931 1.473 20.817 1.00135.54 C ANISOU 3054 C20 CLR A2403 16958 16576 17965 -62 188 -117 C HETATM 3055 C21 CLR A2403 -5.500 1.569 22.231 1.00133.25 C ANISOU 3055 C21 CLR A2403 16652 16324 17652 -25 120 -118 C HETATM 3056 C22 CLR A2403 -4.316 0.085 20.589 1.00135.93 C ANISOU 3056 C22 CLR A2403 16970 16616 18060 -85 226 -117 C HETATM 3057 C23 CLR A2403 -5.186 -0.886 19.832 1.00134.76 C ANISOU 3057 C23 CLR A2403 16840 16501 17863 -92 257 -109 C HETATM 3058 C24 CLR A2403 -6.053 -1.738 20.737 1.00132.73 C ANISOU 3058 C24 CLR A2403 16565 16295 17569 -68 218 -103 C HETATM 3059 C25 CLR A2403 -6.116 -3.237 20.413 1.00132.53 C ANISOU 3059 C25 CLR A2403 16520 16284 17553 -83 248 -98 C HETATM 3060 C26 CLR A2403 -4.977 -4.008 21.066 1.00131.92 C ANISOU 3060 C26 CLR A2403 16389 16181 17554 -93 246 -103 C HETATM 3061 C27 CLR A2403 -6.165 -3.504 18.915 1.00133.43 C ANISOU 3061 C27 CLR A2403 16662 16382 17654 -110 311 -97 C HETATM 3062 O1 CLR A2403 -1.636 12.350 21.311 1.00138.39 O ANISOU 3062 O1 CLR A2403 17466 16662 18453 -49 26 -153 O HETATM 3063 C1 CLR A2404 -8.412 10.699 14.211 1.00132.57 C ANISOU 3063 C1 CLR A2404 17052 16075 17245 -78 208 -100 C HETATM 3064 C2 CLR A2404 -8.508 12.219 14.314 1.00133.01 C ANISOU 3064 C2 CLR A2404 17146 16107 17286 -66 166 -103 C HETATM 3065 C3 CLR A2404 -7.192 12.876 13.975 1.00133.97 C ANISOU 3065 C3 CLR A2404 17266 16166 17469 -100 194 -100 C HETATM 3066 C4 CLR A2404 -6.724 12.466 12.591 1.00134.48 C ANISOU 3066 C4 CLR A2404 17355 16201 17541 -146 270 -91 C HETATM 3067 C5 CLR A2404 -6.701 10.965 12.388 1.00135.33 C ANISOU 3067 C5 CLR A2404 17428 16334 17657 -158 313 -90 C HETATM 3068 C6 CLR A2404 -5.655 10.371 11.825 1.00137.37 C ANISOU 3068 C6 CLR A2404 17664 16562 17969 -197 375 -88 C HETATM 3069 C7 CLR A2404 -5.567 8.913 11.487 1.00138.31 C ANISOU 3069 C7 CLR A2404 17753 16701 18099 -212 422 -88 C HETATM 3070 C8 CLR A2404 -6.892 8.176 11.677 1.00138.28 C ANISOU 3070 C8 CLR A2404 17755 16754 18031 -181 397 -87 C HETATM 3071 C9 CLR A2404 -7.579 8.693 12.957 1.00136.11 C ANISOU 3071 C9 CLR A2404 17469 16512 17734 -135 320 -92 C HETATM 3072 C10 CLR A2404 -7.944 10.194 12.827 1.00134.26 C ANISOU 3072 C10 CLR A2404 17287 16260 17467 -123 283 -92 C HETATM 3073 C11 CLR A2404 -8.776 7.843 13.413 1.00137.13 C ANISOU 3073 C11 CLR A2404 17589 16703 17812 -103 293 -93 C HETATM 3074 C12 CLR A2404 -8.525 6.333 13.390 1.00137.34 C ANISOU 3074 C12 CLR A2404 17572 16746 17864 -117 330 -92 C HETATM 3075 C13 CLR A2404 -7.978 5.862 12.040 1.00139.11 C ANISOU 3075 C13 CLR A2404 17814 16939 18102 -159 404 -87 C HETATM 3076 C14 CLR A2404 -6.692 6.669 11.766 1.00139.75 C ANISOU 3076 C14 CLR A2404 17894 16961 18242 -189 429 -88 C HETATM 3077 C15 CLR A2404 -5.997 5.929 10.621 1.00142.12 C ANISOU 3077 C15 CLR A2404 18195 17236 18568 -231 505 -86 C HETATM 3078 C16 CLR A2404 -6.442 4.461 10.790 1.00141.95 C ANISOU 3078 C16 CLR A2404 18141 17255 18539 -223 515 -87 C HETATM 3079 C17 CLR A2404 -7.383 4.429 12.025 1.00140.32 C ANISOU 3079 C17 CLR A2404 17918 17096 18300 -178 445 -88 C HETATM 3080 C18 CLR A2404 -9.046 6.014 10.935 1.00138.38 C ANISOU 3080 C18 CLR A2404 17784 16860 17933 -159 418 -81 C HETATM 3081 C19 CLR A2404 -9.047 10.428 11.777 1.00134.54 C ANISOU 3081 C19 CLR A2404 17387 16308 17424 -120 291 -86 C HETATM 3082 C20 CLR A2404 -8.338 3.223 12.065 1.00141.26 C ANISOU 3082 C20 CLR A2404 18028 17265 18379 -163 443 -86 C HETATM 3083 C21 CLR A2404 -8.508 2.664 13.476 1.00142.74 C ANISOU 3083 C21 CLR A2404 18164 17488 18582 -135 395 -89 C HETATM 3084 C22 CLR A2404 -7.885 2.134 11.081 1.00141.71 C ANISOU 3084 C22 CLR A2404 18078 17310 18456 -197 510 -84 C HETATM 3085 C23 CLR A2404 -8.468 0.762 11.304 1.00140.49 C ANISOU 3085 C23 CLR A2404 17897 17197 18288 -187 510 -83 C HETATM 3086 C24 CLR A2404 -7.443 -0.237 11.796 1.00138.85 C ANISOU 3086 C24 CLR A2404 17626 16976 18152 -201 529 -88 C HETATM 3087 C25 CLR A2404 -7.930 -1.677 11.987 1.00137.16 C ANISOU 3087 C25 CLR A2404 17385 16799 17930 -195 531 -86 C HETATM 3088 C26 CLR A2404 -8.598 -1.874 13.339 1.00135.25 C ANISOU 3088 C26 CLR A2404 17117 16601 17671 -160 468 -84 C HETATM 3089 C27 CLR A2404 -8.847 -2.128 10.857 1.00135.86 C ANISOU 3089 C27 CLR A2404 17263 16654 17705 -201 562 -81 C HETATM 3090 O1 CLR A2404 -7.350 14.300 14.007 1.00134.40 O ANISOU 3090 O1 CLR A2404 17362 16198 17507 -89 154 -102 O HETATM 3091 C1 OLA A2405 -37.430 14.256 13.490 1.00148.55 C ANISOU 3091 C1 OLA A2405 19503 18983 17958 622 -573 -423 C HETATM 3092 O1 OLA A2405 -36.860 15.360 13.367 1.00149.26 O ANISOU 3092 O1 OLA A2405 19626 19024 18060 625 -596 -423 O HETATM 3093 O2 OLA A2405 -38.140 13.954 14.471 1.00149.84 O ANISOU 3093 O2 OLA A2405 19618 19209 18106 647 -597 -443 O HETATM 3094 C2 OLA A2405 -37.252 13.228 12.386 1.00147.27 C ANISOU 3094 C2 OLA A2405 19358 18801 17795 584 -515 -399 C HETATM 3095 C3 OLA A2405 -37.055 11.821 12.860 1.00143.88 C ANISOU 3095 C3 OLA A2405 18873 18410 17384 562 -470 -383 C HETATM 3096 C4 OLA A2405 -35.887 11.131 12.176 1.00141.68 C ANISOU 3096 C4 OLA A2405 18604 18085 17144 514 -407 -348 C HETATM 3097 C5 OLA A2405 -36.213 9.774 11.602 1.00138.91 C ANISOU 3097 C5 OLA A2405 18241 17754 16783 491 -362 -335 C HETATM 3098 C6 OLA A2405 -36.966 8.861 12.544 1.00135.65 C ANISOU 3098 C6 OLA A2405 17768 17413 16358 505 -368 -346 C HETATM 3099 C7 OLA A2405 -36.971 7.395 12.132 1.00133.22 C ANISOU 3099 C7 OLA A2405 17440 17121 16056 476 -316 -327 C HETATM 3100 C8 OLA A2405 -37.232 7.161 10.677 1.00131.05 C ANISOU 3100 C8 OLA A2405 17217 16816 15761 460 -290 -320 C HETATM 3101 C9 OLA A2405 -36.211 6.274 10.035 1.00130.05 C ANISOU 3101 C9 OLA A2405 17092 16652 15669 415 -228 -290 C HETATM 3102 C10 OLA A2405 -36.251 4.966 9.987 1.00131.37 C ANISOU 3102 C10 OLA A2405 17228 16843 15844 395 -191 -278 C HETATM 3103 C11 OLA A2405 -37.291 4.090 10.613 1.00132.24 C ANISOU 3103 C11 OLA A2405 17293 17020 15930 410 -203 -289 C HETATM 3104 C12 OLA A2405 -38.295 3.568 9.634 1.00134.40 C ANISOU 3104 C12 OLA A2405 17593 17307 16166 412 -195 -295 C HETATM 3105 C13 OLA A2405 -38.195 2.074 9.372 1.00137.18 C ANISOU 3105 C13 OLA A2405 17918 17672 16530 382 -148 -277 C HETATM 3106 C14 OLA A2405 -38.472 1.205 10.580 1.00138.21 C ANISOU 3106 C14 OLA A2405 17982 17862 16668 386 -152 -277 C HETATM 3107 C15 OLA A2405 -38.280 -0.274 10.345 1.00137.59 C ANISOU 3107 C15 OLA A2405 17879 17793 16608 355 -107 -257 C HETATM 3108 C16 OLA A2405 -36.837 -0.712 10.247 1.00135.65 C ANISOU 3108 C16 OLA A2405 17625 17502 16414 320 -62 -231 C HETATM 3109 C17 OLA A2405 -36.604 -1.882 9.325 1.00133.71 C ANISOU 3109 C17 OLA A2405 17386 17240 16179 288 -13 -213 C HETATM 3110 C18 OLA A2405 -36.073 -1.492 7.966 1.00132.61 C ANISOU 3110 C18 OLA A2405 17305 17040 16042 271 16 -206 C HETATM 3111 C10 OLC A2406 -42.949 4.539 13.539 1.00138.23 C ANISOU 3111 C10 OLC A2406 17941 18058 16523 562 -389 -414 C HETATM 3112 C9 OLC A2406 -42.617 5.744 13.077 1.00138.26 C ANISOU 3112 C9 OLC A2406 17991 18013 16526 575 -411 -421 C HETATM 3113 C11 OLC A2406 -44.092 4.309 14.505 1.00138.07 C ANISOU 3113 C11 OLC A2406 17873 18114 16473 589 -419 -439 C HETATM 3114 C8 OLC A2406 -43.350 7.004 13.474 1.00139.50 C ANISOU 3114 C8 OLC A2406 18160 18187 16656 619 -472 -456 C HETATM 3115 C24 OLC A2406 -40.627 17.970 16.998 1.00163.60 C ANISOU 3115 C24 OLC A2406 21355 21036 19771 820 -842 -577 C HETATM 3116 C16 OLC A2406 -44.452 -1.391 16.219 1.00133.05 C ANISOU 3116 C16 OLC A2406 17053 17632 15869 488 -290 -368 C HETATM 3117 C12 OLC A2406 -44.003 2.889 15.056 1.00137.34 C ANISOU 3117 C12 OLC A2406 17729 18059 16395 562 -382 -419 C HETATM 3118 C7 OLC A2406 -42.466 8.200 13.150 1.00140.42 C ANISOU 3118 C7 OLC A2406 18322 18240 16791 620 -486 -451 C HETATM 3119 C15 OLC A2406 -45.151 -0.142 15.692 1.00135.82 C ANISOU 3119 C15 OLC A2406 17442 17974 16188 523 -329 -400 C HETATM 3120 C13 OLC A2406 -44.829 1.902 14.233 1.00136.89 C ANISOU 3120 C13 OLC A2406 17676 18020 16316 551 -361 -418 C HETATM 3121 C6 OLC A2406 -41.944 8.857 14.421 1.00138.77 C ANISOU 3121 C6 OLC A2406 18081 18043 16603 636 -512 -457 C HETATM 3122 C14 OLC A2406 -44.405 0.459 14.502 1.00135.66 C ANISOU 3122 C14 OLC A2406 17482 17880 16184 515 -316 -389 C HETATM 3123 C5 OLC A2406 -42.419 10.302 14.504 1.00138.74 C ANISOU 3123 C5 OLC A2406 18107 18031 16578 676 -572 -488 C HETATM 3124 C4 OLC A2406 -41.302 11.281 14.151 1.00141.74 C ANISOU 3124 C4 OLC A2406 18529 18339 16986 666 -575 -474 C HETATM 3125 C3 OLC A2406 -41.846 12.588 13.579 1.00145.31 C ANISOU 3125 C3 OLC A2406 19036 18764 17411 697 -625 -499 C HETATM 3126 C2 OLC A2406 -42.795 13.278 14.553 1.00148.71 C ANISOU 3126 C2 OLC A2406 19440 19248 17817 744 -685 -539 C HETATM 3127 C21 OLC A2406 -41.869 16.119 15.899 1.00160.79 C ANISOU 3127 C21 OLC A2406 20991 20729 19374 797 -786 -569 C HETATM 3128 C1 OLC A2406 -42.991 14.719 14.148 1.00153.15 C ANISOU 3128 C1 OLC A2406 20055 19771 18364 773 -737 -560 C HETATM 3129 C22 OLC A2406 -41.760 17.636 16.034 1.00162.48 C ANISOU 3129 C22 OLC A2406 21239 20908 19587 827 -843 -590 C HETATM 3130 O19 OLC A2406 -43.969 15.050 13.496 1.00152.37 O ANISOU 3130 O19 OLC A2406 19987 19676 18230 795 -766 -583 O HETATM 3131 O25 OLC A2406 -41.127 18.000 18.341 1.00162.47 O ANISOU 3131 O25 OLC A2406 21155 20956 19618 852 -874 -603 O HETATM 3132 O23 OLC A2406 -41.495 18.241 14.761 1.00162.53 O ANISOU 3132 O23 OLC A2406 21317 20847 19592 814 -843 -578 O HETATM 3133 O20 OLC A2406 -42.016 15.731 14.532 1.00157.95 O ANISOU 3133 O20 OLC A2406 20678 20336 19002 775 -756 -554 O HETATM 3134 C9 OLC A2407 -4.062 -1.067 25.008 1.00131.64 C ANISOU 3134 C9 OLC A2407 16311 16132 17572 -14 60 -120 C HETATM 3135 C8 OLC A2407 -2.715 -0.461 25.321 1.00132.15 C ANISOU 3135 C8 OLC A2407 16350 16144 17716 -22 55 -131 C HETATM 3136 C24 OLC A2407 -2.883 12.082 27.146 1.00148.92 C ANISOU 3136 C24 OLC A2407 18685 18132 19765 114 -236 -185 C HETATM 3137 C7 OLC A2407 -2.872 0.583 26.419 1.00132.75 C ANISOU 3137 C7 OLC A2407 16429 16229 17781 9 -7 -136 C HETATM 3138 C6 OLC A2407 -2.604 1.979 25.871 1.00131.64 C ANISOU 3138 C6 OLC A2407 16317 16056 17644 4 1 -142 C HETATM 3139 C5 OLC A2407 -3.076 3.062 26.837 1.00130.60 C ANISOU 3139 C5 OLC A2407 16199 15943 17481 39 -62 -145 C HETATM 3140 C4 OLC A2407 -3.641 4.268 26.092 1.00131.84 C ANISOU 3140 C4 OLC A2407 16405 16096 17591 42 -56 -146 C HETATM 3141 C3 OLC A2407 -2.531 5.080 25.432 1.00134.13 C ANISOU 3141 C3 OLC A2407 16699 16326 17941 17 -27 -152 C HETATM 3142 C2 OLC A2407 -2.963 6.515 25.149 1.00137.38 C ANISOU 3142 C2 OLC A2407 17154 16730 18315 28 -45 -154 C HETATM 3143 C21 OLC A2407 -2.100 9.737 27.079 1.00144.93 C ANISOU 3143 C21 OLC A2407 18115 17633 19319 80 -175 -177 C HETATM 3144 C1 OLC A2407 -2.506 7.430 26.260 1.00139.83 C ANISOU 3144 C1 OLC A2407 17449 17025 18655 51 -102 -163 C HETATM 3145 C22 OLC A2407 -1.805 11.152 26.604 1.00147.86 C ANISOU 3145 C22 OLC A2407 18518 17963 19697 74 -178 -181 C HETATM 3146 O19 OLC A2407 -2.416 7.008 27.406 1.00139.84 O ANISOU 3146 O19 OLC A2407 17418 17045 18671 72 -142 -167 O HETATM 3147 O25 OLC A2407 -2.503 13.446 26.927 1.00151.57 O ANISOU 3147 O25 OLC A2407 19046 18427 20117 112 -252 -190 O HETATM 3148 O23 OLC A2407 -0.536 11.565 27.121 1.00150.70 O ANISOU 3148 O23 OLC A2407 18845 18276 20139 66 -191 -190 O HETATM 3149 O20 OLC A2407 -2.175 8.824 25.982 1.00142.20 O ANISOU 3149 O20 OLC A2407 17775 17288 18965 50 -111 -168 O HETATM 3150 C1 OLA A2408 -15.816 14.740 1.322 1.00152.00 C ANISOU 3150 C1 OLA A2408 20271 18424 19058 -165 346 -37 C HETATM 3151 O1 OLA A2408 -15.206 15.827 1.204 1.00153.06 O ANISOU 3151 O1 OLA A2408 20435 18513 19209 -182 338 -31 O HETATM 3152 O2 OLA A2408 -17.039 14.660 1.560 1.00152.69 O ANISOU 3152 O2 OLA A2408 20368 18551 19096 -126 299 -47 O HETATM 3153 C2 OLA A2408 -15.023 13.450 1.178 1.00150.31 C ANISOU 3153 C2 OLA A2408 20006 18216 18888 -196 414 -33 C HETATM 3154 C3 OLA A2408 -15.793 12.252 0.694 1.00150.07 C ANISOU 3154 C3 OLA A2408 19974 18224 18821 -189 437 -35 C HETATM 3155 C4 OLA A2408 -15.079 10.942 0.986 1.00150.71 C ANISOU 3155 C4 OLA A2408 19988 18322 18955 -207 486 -36 C HETATM 3156 C5 OLA A2408 -13.810 10.730 0.194 1.00151.32 C ANISOU 3156 C5 OLA A2408 20065 18354 19074 -259 560 -26 C HETATM 3157 C6 OLA A2408 -13.070 9.461 0.536 1.00150.28 C ANISOU 3157 C6 OLA A2408 19864 18237 18999 -274 604 -29 C HETATM 3158 C8 OLA A2409 -7.919 -17.787 15.171 1.00128.58 C ANISOU 3158 C8 OLA A2409 15901 15877 17076 -228 530 -67 C HETATM 3159 C9 OLA A2409 -8.335 -17.090 16.429 1.00128.16 C ANISOU 3159 C9 OLA A2409 15846 15849 16998 -205 473 -57 C HETATM 3160 C10 OLA A2409 -8.945 -15.935 16.490 1.00128.29 C ANISOU 3160 C10 OLA A2409 15894 15884 16966 -191 460 -54 C HETATM 3161 C11 OLA A2409 -9.428 -15.263 17.737 1.00126.83 C ANISOU 3161 C11 OLA A2409 15708 15729 16754 -166 403 -46 C HETATM 3162 C12 OLA A2409 -10.584 -14.337 17.501 1.00124.95 C ANISOU 3162 C12 OLA A2409 15513 15524 16438 -150 393 -41 C HETATM 3163 C13 OLA A2409 -10.675 -13.180 18.479 1.00124.40 C ANISOU 3163 C13 OLA A2409 15446 15465 16355 -128 349 -40 C HETATM 3164 C14 OLA A2409 -9.857 -11.976 18.082 1.00125.59 C ANISOU 3164 C14 OLA A2409 15609 15575 16535 -133 367 -51 C HETATM 3165 C15 OLA A2409 -10.326 -10.679 18.693 1.00126.83 C ANISOU 3165 C15 OLA A2409 15785 15749 16654 -109 329 -51 C HETATM 3166 C16 OLA A2409 -9.326 -9.546 18.607 1.00127.03 C ANISOU 3166 C16 OLA A2409 15812 15730 16722 -114 337 -61 C HETATM 3167 C17 OLA A2409 -8.225 -9.588 19.642 1.00128.09 C ANISOU 3167 C17 OLA A2409 15903 15839 16927 -112 311 -66 C HETATM 3168 C18 OLA A2409 -7.728 -8.232 20.090 1.00128.19 C ANISOU 3168 C18 OLA A2409 15920 15830 16956 -102 289 -73 C HETATM 3169 NA NA A2410 -24.573 -7.798 17.097 1.00130.78 NA ANISOU 3169 NA NA A2410 16582 16712 16397 84 148 -58 NA HETATM 3170 O HOH A3801 -15.355 9.735 18.584 1.00124.20 O ANISOU 3170 O HOH A3801 15961 15351 15879 154 -74 -141 O HETATM 3171 O HOH A3802 -26.416 -12.096 21.796 1.00 81.92 O ANISOU 3171 O HOH A3802 10226 10723 10177 84 55 -18 O HETATM 3172 O HOH A3803 -25.645 8.003 14.458 1.00 83.58 O ANISOU 3172 O HOH A3803 11031 10501 10224 276 -124 -186 O HETATM 3173 O HOH A3804 -16.292 0.629 13.169 1.00 89.33 O ANISOU 3173 O HOH A3804 11511 11003 11428 -8 279 -81 O HETATM 3174 O HOH A3805 -25.963 5.790 19.534 1.00 69.09 O ANISOU 3174 O HOH A3805 8983 8841 8426 328 -204 -197 O HETATM 3175 O HOH A3806 -34.134 15.069 30.613 1.00119.31 O ANISOU 3175 O HOH A3806 15227 15680 14424 812 -847 -521 O HETATM 3176 O HOH A3807 -15.108 3.518 22.606 1.00 76.40 O ANISOU 3176 O HOH A3807 9659 9463 9906 156 -68 -120 O HETATM 3177 O HOH A3808 -22.071 12.679 18.514 1.00121.13 O ANISOU 3177 O HOH A3808 15730 15145 15149 328 -285 -212 O HETATM 3178 O HOH A3809 -26.649 19.043 23.214 1.00103.91 O ANISOU 3178 O HOH A3809 13580 13125 12775 611 -702 -374 O HETATM 3179 O HOH A3810 -20.927 -2.164 24.812 1.00 96.64 O ANISOU 3179 O HOH A3810 12139 12360 12218 201 -111 -98 O HETATM 3180 O HOH A3811 -23.297 -5.313 14.995 1.00 82.57 O ANISOU 3180 O HOH A3811 10567 10492 10312 74 190 -72 O HETATM 3181 O HOH A3812 -33.293 24.314 26.188 1.00108.85 O ANISOU 3181 O HOH A3812 14244 13979 13134 920 -1092 -605 O HETATM 3182 O HOH A3813 -11.283 11.740 16.433 1.00 91.82 O ANISOU 3182 O HOH A3813 11905 11029 11952 41 36 -121 O HETATM 3183 O HOH A3814 -13.223 14.128 24.789 1.00121.83 O ANISOU 3183 O HOH A3814 15551 15020 15717 283 -356 -199 O HETATM 3184 O HOH A3815 -25.549 -14.692 14.517 1.00 86.88 O ANISOU 3184 O HOH A3815 10972 11182 10857 -17 286 -12 O HETATM 3185 O HOH A3816 -26.872 -13.115 26.063 1.00101.32 O ANISOU 3185 O HOH A3816 12589 13294 12614 101 -49 2 O HETATM 3186 O HOH A3817 -24.623 11.975 16.643 1.00102.25 O ANISOU 3186 O HOH A3817 13409 12812 12631 342 -269 -220 O HETATM 3187 O HOH A3818 -19.443 12.525 33.642 1.00103.23 O ANISOU 3187 O HOH A3818 13023 13141 13059 547 -679 -294 O HETATM 3188 O HOH A3819 -30.742 20.805 3.915 1.00114.52 O ANISOU 3188 O HOH A3819 15793 14002 13716 369 -434 -255 O HETATM 3189 O HOH A3820 -20.354 -22.124 14.862 1.00 66.64 O ANISOU 3189 O HOH A3820 8220 8468 8634 -153 391 36 O CONECT 399 3169 CONECT 535 1183 CONECT 551 1092 CONECT 571 1227 CONECT 676 3169 CONECT 1092 551 CONECT 1183 535 CONECT 1227 571 CONECT 2603 2624 CONECT 2624 2603 CONECT 2994 2995 CONECT 2995 2994 2996 3002 CONECT 2996 2995 2997 2998 CONECT 2997 2996 CONECT 2998 2996 2999 3000 CONECT 2999 2998 CONECT 3000 2998 3001 3006 CONECT 3001 3000 3002 3004 CONECT 3002 2995 3001 3003 CONECT 3003 3002 CONECT 3004 3001 3005 CONECT 3005 3004 3006 CONECT 3006 3000 3005 CONECT 3007 3008 3016 CONECT 3008 3007 3009 CONECT 3009 3008 3010 3034 CONECT 3010 3009 3011 CONECT 3011 3010 3012 3016 CONECT 3012 3011 3013 CONECT 3013 3012 3014 CONECT 3014 3013 3015 3020 CONECT 3015 3014 3016 3017 CONECT 3016 3007 3011 3015 3025 CONECT 3017 3015 3018 CONECT 3018 3017 3019 CONECT 3019 3018 3020 3023 3024 CONECT 3020 3014 3019 3021 CONECT 3021 3020 3022 CONECT 3022 3021 3023 CONECT 3023 3019 3022 3026 CONECT 3024 3019 CONECT 3025 3016 CONECT 3026 3023 3027 3028 CONECT 3027 3026 CONECT 3028 3026 3029 CONECT 3029 3028 3030 CONECT 3030 3029 3031 CONECT 3031 3030 3032 3033 CONECT 3032 3031 CONECT 3033 3031 CONECT 3034 3009 CONECT 3035 3036 3044 CONECT 3036 3035 3037 CONECT 3037 3036 3038 3062 CONECT 3038 3037 3039 CONECT 3039 3038 3040 3044 CONECT 3040 3039 3041 CONECT 3041 3040 3042 CONECT 3042 3041 3043 3048 CONECT 3043 3042 3044 3045 CONECT 3044 3035 3039 3043 3053 CONECT 3045 3043 3046 CONECT 3046 3045 3047 CONECT 3047 3046 3048 3051 3052 CONECT 3048 3042 3047 3049 CONECT 3049 3048 3050 CONECT 3050 3049 3051 CONECT 3051 3047 3050 3054 CONECT 3052 3047 CONECT 3053 3044 CONECT 3054 3051 3055 3056 CONECT 3055 3054 CONECT 3056 3054 3057 CONECT 3057 3056 3058 CONECT 3058 3057 3059 CONECT 3059 3058 3060 3061 CONECT 3060 3059 CONECT 3061 3059 CONECT 3062 3037 CONECT 3063 3064 3072 CONECT 3064 3063 3065 CONECT 3065 3064 3066 3090 CONECT 3066 3065 3067 CONECT 3067 3066 3068 3072 CONECT 3068 3067 3069 CONECT 3069 3068 3070 CONECT 3070 3069 3071 3076 CONECT 3071 3070 3072 3073 CONECT 3072 3063 3067 3071 3081 CONECT 3073 3071 3074 CONECT 3074 3073 3075 CONECT 3075 3074 3076 3079 3080 CONECT 3076 3070 3075 3077 CONECT 3077 3076 3078 CONECT 3078 3077 3079 CONECT 3079 3075 3078 3082 CONECT 3080 3075 CONECT 3081 3072 CONECT 3082 3079 3083 3084 CONECT 3083 3082 CONECT 3084 3082 3085 CONECT 3085 3084 3086 CONECT 3086 3085 3087 CONECT 3087 3086 3088 3089 CONECT 3088 3087 CONECT 3089 3087 CONECT 3090 3065 CONECT 3091 3092 3093 3094 CONECT 3092 3091 CONECT 3093 3091 CONECT 3094 3091 3095 CONECT 3095 3094 3096 CONECT 3096 3095 3097 CONECT 3097 3096 3098 CONECT 3098 3097 3099 CONECT 3099 3098 3100 CONECT 3100 3099 3101 CONECT 3101 3100 3102 CONECT 3102 3101 3103 CONECT 3103 3102 3104 CONECT 3104 3103 3105 CONECT 3105 3104 3106 CONECT 3106 3105 3107 CONECT 3107 3106 3108 CONECT 3108 3107 3109 CONECT 3109 3108 3110 CONECT 3110 3109 CONECT 3111 3112 3113 CONECT 3112 3111 3114 CONECT 3113 3111 3117 CONECT 3114 3112 3118 CONECT 3115 3129 3131 CONECT 3116 3119 CONECT 3117 3113 3120 CONECT 3118 3114 3121 CONECT 3119 3116 3122 CONECT 3120 3117 3122 CONECT 3121 3118 3123 CONECT 3122 3119 3120 CONECT 3123 3121 3124 CONECT 3124 3123 3125 CONECT 3125 3124 3126 CONECT 3126 3125 3128 CONECT 3127 3129 3133 CONECT 3128 3126 3130 3133 CONECT 3129 3115 3127 3132 CONECT 3130 3128 CONECT 3131 3115 CONECT 3132 3129 CONECT 3133 3127 3128 CONECT 3134 3135 CONECT 3135 3134 3137 CONECT 3136 3145 3147 CONECT 3137 3135 3138 CONECT 3138 3137 3139 CONECT 3139 3138 3140 CONECT 3140 3139 3141 CONECT 3141 3140 3142 CONECT 3142 3141 3144 CONECT 3143 3145 3149 CONECT 3144 3142 3146 3149 CONECT 3145 3136 3143 3148 CONECT 3146 3144 CONECT 3147 3136 CONECT 3148 3145 CONECT 3149 3143 3144 CONECT 3150 3151 3152 3153 CONECT 3151 3150 CONECT 3152 3150 CONECT 3153 3150 3154 CONECT 3154 3153 3155 CONECT 3155 3154 3156 CONECT 3156 3155 3157 CONECT 3157 3156 CONECT 3158 3159 CONECT 3159 3158 3160 CONECT 3160 3159 3161 CONECT 3161 3160 3162 CONECT 3162 3161 3163 CONECT 3163 3162 3164 CONECT 3164 3163 3165 CONECT 3165 3164 3166 CONECT 3166 3165 3167 CONECT 3167 3166 3168 CONECT 3168 3167 CONECT 3169 399 676 MASTER 354 0 10 20 2 0 0 6 3182 1 186 33 END