HEADER SIGNALING PROTEIN, ELECTRON TRANSPORT 07-DEC-12 4IAR TITLE CRYSTAL STRUCTURE OF THE CHIMERIC PROTEIN OF 5-HT1B-BRIL IN COMPLEX TITLE 2 WITH ERGOTAMINE (PSI COMMUNITY TARGET) COMPND MOL_ID: 1; COMPND 2 MOLECULE: CHIMERA PROTEIN OF HUMAN 5-HYDROXYTRYPTAMINE RECEPTOR 1B COMPND 3 AND E. COLI SOLUBLE CYTOCHROME B562; COMPND 4 CHAIN: A; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ESCHERICHIA COLI; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606, 562; SOURCE 5 GENE: HTR1B, HTR1DB, CYBC; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SF9; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC KEYWDS ERGOTAMINE, NOVEL PROTEIN ENGINEERING, GPCR NETWORK, MEMBRANE KEYWDS 2 PROTEIN, PSI-BIOLOGY, STRUCTURAL GENOMICS, GPCR, SIGNALING PROTEIN, KEYWDS 3 ELECTRON TRANSPORT, GPCR DOCK EXPDTA X-RAY DIFFRACTION AUTHOR C.WANG,Y.JIANG,J.MA,H.WU,D.WACKER,V.KATRITCH,G.W.HAN,W.LIU,X.HUANG, AUTHOR 2 E.VARDY,J.D.MCCORVY,X.GAO,E.X.ZHOU,K.MELCHER,C.ZHANG,F.BAI,H.YANG, AUTHOR 3 L.YANG,H.JIANG,B.L.ROTH,V.CHEREZOV,R.C.STEVENS,H.E.XU,GPCR NETWORK AUTHOR 4 (GPCR) REVDAT 7 02-FEB-22 4IAR 1 REMARK DBREF SEQADV REVDAT 6 15-NOV-17 4IAR 1 REMARK REVDAT 5 07-JUN-17 4IAR 1 COMPND SOURCE REMARK REVDAT 4 18-DEC-13 4IAR 1 REMARK REVDAT 3 15-MAY-13 4IAR 1 JRNL REVDAT 2 10-APR-13 4IAR 1 JRNL REVDAT 1 13-MAR-13 4IAR 0 JRNL AUTH C.WANG,Y.JIANG,J.MA,H.WU,D.WACKER,V.KATRITCH,G.W.HAN,W.LIU, JRNL AUTH 2 X.P.HUANG,E.VARDY,J.D.MCCORVY,X.GAO,X.E.ZHOU,K.MELCHER, JRNL AUTH 3 C.ZHANG,F.BAI,H.YANG,L.YANG,H.JIANG,B.L.ROTH,V.CHEREZOV, JRNL AUTH 4 R.C.STEVENS,H.E.XU JRNL TITL STRUCTURAL BASIS FOR MOLECULAR RECOGNITION AT SEROTONIN JRNL TITL 2 RECEPTORS. JRNL REF SCIENCE V. 340 610 2013 JRNL REFN ISSN 0036-8075 JRNL PMID 23519210 JRNL DOI 10.1126/SCIENCE.1232807 REMARK 2 REMARK 2 RESOLUTION. 2.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.62 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 92.4 REMARK 3 NUMBER OF REFLECTIONS : 16860 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) : 0.225 REMARK 3 R VALUE (WORKING SET) : 0.223 REMARK 3 FREE R VALUE : 0.261 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.170 REMARK 3 FREE R VALUE TEST SET COUNT : 871 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 8 REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.89 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.39 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2292 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2415 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2183 REMARK 3 BIN R VALUE (WORKING SET) : 0.2369 REMARK 3 BIN FREE R VALUE : 0.3322 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.76 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 109 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 2933 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 57 REMARK 3 SOLVENT ATOMS : 9 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 56.86 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 81.05 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 7.56300 REMARK 3 B22 (A**2) : -12.46720 REMARK 3 B33 (A**2) : 4.90420 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 1.67270 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.463 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.485 REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL REMARK 3 REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797 REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.914 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 3072 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 4216 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 1343 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : 51 ; 2.000 ; HARMONIC REMARK 3 GENERAL PLANES : 443 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 3072 ; 20.000 ; HARMONIC REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : 428 ; 5.000 ; SEMIHARMONIC REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL REMARK 3 IDEAL-DIST CONTACT TERM : 3656 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.010 REMARK 3 BOND ANGLES (DEGREES) : 1.02 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.16 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 3.34 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 2 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: { A|38 - A|387 } REMARK 3 ORIGIN FOR THE GROUP (A): 1.9397 -18.0322 19.7124 REMARK 3 T TENSOR REMARK 3 T11: -0.3290 T22: 0.3376 REMARK 3 T33: -0.2563 T12: 0.0148 REMARK 3 T13: -0.0732 T23: -0.0708 REMARK 3 L TENSOR REMARK 3 L11: 3.0075 L22: 0.4167 REMARK 3 L33: 3.4459 L12: 0.0904 REMARK 3 L13: 1.2079 L23: 0.2018 REMARK 3 S TENSOR REMARK 3 S11: -0.0383 S12: -0.0165 S13: -0.0560 REMARK 3 S21: -0.0124 S22: -0.0611 S23: -0.0628 REMARK 3 S31: 0.0785 S32: -0.5177 S33: 0.0994 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: { A|1001- A|1106 } REMARK 3 ORIGIN FOR THE GROUP (A): 44.0764 -10.1092 30.2923 REMARK 3 T TENSOR REMARK 3 T11: -0.2838 T22: 0.2092 REMARK 3 T33: -0.0663 T12: -0.0201 REMARK 3 T13: -0.1142 T23: 0.0612 REMARK 3 L TENSOR REMARK 3 L11: 6.4547 L22: 0.8755 REMARK 3 L33: 1.5313 L12: 1.2405 REMARK 3 L13: -0.0933 L23: 0.6230 REMARK 3 S TENSOR REMARK 3 S11: -0.0426 S12: 0.2053 S13: -0.1141 REMARK 3 S21: -0.0777 S22: 0.0003 S23: -0.0007 REMARK 3 S31: 0.0541 S32: 0.2384 S33: 0.0423 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 4IAR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JAN-13. REMARK 100 THE DEPOSITION ID IS D_1000076518. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-AUG-12; 01-AUG-12 REMARK 200 TEMPERATURE (KELVIN) : 100; NULL REMARK 200 PH : 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 47 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y; Y REMARK 200 RADIATION SOURCE : APS; APS REMARK 200 BEAMLINE : 23-ID-D; 21-ID-D REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0330; 1.0330 REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL; DOUBLE CRYSTAL REMARK 200 OPTICS : MIRRORS; MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : CCD; CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD; MARMOSAIC REMARK 200 300 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16979 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 92.0 REMARK 200 DATA REDUNDANCY : 9.600 REMARK 200 R MERGE (I) : 0.16000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 18.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90 REMARK 200 COMPLETENESS FOR SHELL (%) : 64.6 REMARK 200 DATA REDUNDANCY IN SHELL : 4.30 REMARK 200 R MERGE FOR SHELL (I) : 0.62000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.700 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: PDB ENTRY 4EIY REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 66.10 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.63 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS PH 7.5, 30% (V/V) PEG400, REMARK 280 400 MM LITHIUM CHLORIDE , LIPID CUBIC PHASE (LCP), TEMPERATURE REMARK 280 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z REMARK 290 4555 -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 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 97.64500 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 22.75000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 97.64500 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 22.75000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 300 REMARK: AUTHORS STATE THAT THE BIOLOGICAL UNIT IS UNKNOWN REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY A 30 REMARK 465 GLY A 31 REMARK 465 THR A 32 REMARK 465 CYS A 33 REMARK 465 SER A 34 REMARK 465 ALA A 35 REMARK 465 LYS A 36 REMARK 465 ASP A 37 REMARK 465 LYS A 191 REMARK 465 ALA A 192 REMARK 465 GLU A 193 REMARK 465 GLU A 194 REMARK 465 GLU A 195 REMARK 465 VAL A 196 REMARK 465 CYS A 340 REMARK 465 LYS A 341 REMARK 465 ASP A 342 REMARK 465 ALA A 343 REMARK 465 CYS A 344 REMARK 465 CYS A 388 REMARK 465 THR A 389 REMARK 465 SER A 390 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 ILE A 39 CG1 CG2 CD1 REMARK 470 ARG A 76 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 78 CD NE CZ NH1 NH2 REMARK 470 ARG A 114 NE CZ NH1 NH2 REMARK 470 LYS A 160 CD CE NZ REMARK 470 LYS A 164 CD CE NZ REMARK 470 ARG A 188 CG CD NE CZ NH1 NH2 REMARK 470 GLN A 189 CG CD OE1 NE2 REMARK 470 SER A 197 OG REMARK 470 GLU A 198 CG CD OE1 OE2 REMARK 470 ARG A 230 CD NE CZ NH1 NH2 REMARK 470 LYS A1042 CG CD CE NZ REMARK 470 LYS A1051 CG CD CE NZ REMARK 470 GLU A1057 CG CD OE1 OE2 REMARK 470 LYS A1059 CG CD CE NZ REMARK 470 ARG A1062 CG CD NE CZ NH1 NH2 REMARK 470 ASP A1074 CG OD1 OD2 REMARK 470 LYS A1083 CG CD CE NZ REMARK 470 LYS A1085 CG CD CE NZ REMARK 470 LYS A1104 CD CE NZ REMARK 470 LYS A 314 CG CD CE NZ REMARK 470 TRP A 345 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP A 345 CZ3 CH2 REMARK 470 GLN A 378 CG CD OE1 NE2 REMARK 470 ARG A 385 CG CD NE CZ NH1 NH2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASP A 153 45.09 -148.40 REMARK 500 TRP A 187 62.31 -67.33 REMARK 500 GLN A 189 -32.18 -148.55 REMARK 500 PHE A 217 -64.32 -125.54 REMARK 500 GLU A1057 67.39 -104.23 REMARK 500 ARG A 310 66.03 36.09 REMARK 500 PHE A 346 -177.39 -66.86 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 OLB A 2002 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ERM A 2001 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLB A 2002 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: GPCR-118 RELATED DB: TARGETTRACK REMARK 900 RELATED ID: 4IAQ RELATED DB: PDB DBREF 4IAR A 33 239 UNP P28222 5HT1B_HUMAN 33 239 DBREF 4IAR A 1001 1106 UNP P0ABE7 C562_ECOLX 23 128 DBREF 4IAR A 306 390 UNP P28222 5HT1B_HUMAN 306 390 SEQADV 4IAR GLY A 30 UNP P28222 EXPRESSION TAG SEQADV 4IAR GLY A 31 UNP P28222 EXPRESSION TAG SEQADV 4IAR THR A 32 UNP P28222 EXPRESSION TAG SEQADV 4IAR TRP A 138 UNP P28222 LEU 138 ENGINEERED MUTATION SEQADV 4IAR TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION SEQADV 4IAR ILE A 1102 UNP P0ABE7 HIS 124 ENGINEERED MUTATION SEQADV 4IAR LEU A 1106 UNP P0ABE7 ARG 128 ENGINEERED MUTATION SEQRES 1 A 401 GLY GLY THR CYS SER ALA LYS ASP TYR ILE TYR GLN ASP SEQRES 2 A 401 SER ILE SER LEU PRO TRP LYS VAL LEU LEU VAL MET LEU SEQRES 3 A 401 LEU ALA LEU ILE THR LEU ALA THR THR LEU SER ASN ALA SEQRES 4 A 401 PHE VAL ILE ALA THR VAL TYR ARG THR ARG LYS LEU HIS SEQRES 5 A 401 THR PRO ALA ASN TYR LEU ILE ALA SER LEU ALA VAL THR SEQRES 6 A 401 ASP LEU LEU VAL SER ILE LEU VAL MET PRO ILE SER THR SEQRES 7 A 401 MET TYR THR VAL THR GLY ARG TRP THR LEU GLY GLN VAL SEQRES 8 A 401 VAL CYS ASP PHE TRP LEU SER SER ASP ILE THR CYS CYS SEQRES 9 A 401 THR ALA SER ILE TRP HIS LEU CYS VAL ILE ALA LEU ASP SEQRES 10 A 401 ARG TYR TRP ALA ILE THR ASP ALA VAL GLU TYR SER ALA SEQRES 11 A 401 LYS ARG THR PRO LYS ARG ALA ALA VAL MET ILE ALA LEU SEQRES 12 A 401 VAL TRP VAL PHE SER ILE SER ILE SER LEU PRO PRO PHE SEQRES 13 A 401 PHE TRP ARG GLN ALA LYS ALA GLU GLU GLU VAL SER GLU SEQRES 14 A 401 CYS VAL VAL ASN THR ASP HIS ILE LEU TYR THR VAL TYR SEQRES 15 A 401 SER THR VAL GLY ALA PHE TYR PHE PRO THR LEU LEU LEU SEQRES 16 A 401 ILE ALA LEU TYR GLY ARG ILE TYR VAL GLU ALA ARG SER SEQRES 17 A 401 ARG ILE ALA ASP LEU GLU ASP ASN TRP GLU THR LEU ASN SEQRES 18 A 401 ASP ASN LEU LYS VAL ILE GLU LYS ALA ASP ASN ALA ALA SEQRES 19 A 401 GLN VAL LYS ASP ALA LEU THR LYS MET ARG ALA ALA ALA SEQRES 20 A 401 LEU ASP ALA GLN LYS ALA THR PRO PRO LYS LEU GLU ASP SEQRES 21 A 401 LYS SER PRO ASP SER PRO GLU MET LYS ASP PHE ARG HIS SEQRES 22 A 401 GLY PHE ASP ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU SEQRES 23 A 401 LYS LEU ALA ASN GLU GLY LYS VAL LYS GLU ALA GLN ALA SEQRES 24 A 401 ALA ALA GLU GLN LEU LYS THR THR ARG ASN ALA TYR ILE SEQRES 25 A 401 GLN LYS TYR LEU ALA ALA ARG GLU ARG LYS ALA THR LYS SEQRES 26 A 401 THR LEU GLY ILE ILE LEU GLY ALA PHE ILE VAL CYS TRP SEQRES 27 A 401 LEU PRO PHE PHE ILE ILE SER LEU VAL MET PRO ILE CYS SEQRES 28 A 401 LYS ASP ALA CYS TRP PHE HIS LEU ALA ILE PHE ASP PHE SEQRES 29 A 401 PHE THR TRP LEU GLY TYR LEU ASN SER LEU ILE ASN PRO SEQRES 30 A 401 ILE ILE TYR THR MET SER ASN GLU ASP PHE LYS GLN ALA SEQRES 31 A 401 PHE HIS LYS LEU ILE ARG PHE LYS CYS THR SER HET ERM A2001 43 HET OLB A2002 14 HETNAM ERM ERGOTAMINE HETNAM OLB (2S)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE FORMUL 2 ERM C33 H35 N5 O5 FORMUL 3 OLB C21 H40 O4 FORMUL 4 HOH *9(H2 O) HELIX 1 1 ILE A 39 ILE A 44 5 6 HELIX 2 2 SER A 45 THR A 77 1 33 HELIX 3 3 ARG A 78 HIS A 81 5 4 HELIX 4 4 THR A 82 VAL A 102 1 21 HELIX 5 5 MET A 103 GLY A 113 1 11 HELIX 6 6 LEU A 117 ASP A 153 1 37 HELIX 7 7 ASP A 153 ALA A 159 1 7 HELIX 8 8 THR A 162 LEU A 182 1 21 HELIX 9 9 HIS A 205 PHE A 217 1 13 HELIX 10 10 PHE A 217 ALA A 1020 1 43 HELIX 11 11 ASN A 1022 THR A 1044 1 23 HELIX 12 12 ASP A 1060 GLY A 1082 1 23 HELIX 13 13 LYS A 1083 ALA A 1090 1 8 HELIX 14 14 ALA A 1090 TYR A 1101 1 12 HELIX 15 15 TYR A 1101 ARG A 308 1 9 HELIX 16 16 ARG A 310 MET A 337 1 28 HELIX 17 17 LEU A 348 ASN A 373 1 26 HELIX 18 18 ASN A 373 ILE A 384 1 12 SSBOND 1 CYS A 122 CYS A 199 1555 1555 2.04 SITE 1 AC1 16 ASP A 129 ILE A 130 CYS A 133 THR A 134 SITE 2 AC1 16 CYS A 199 VAL A 200 VAL A 201 ALA A 216 SITE 3 AC1 16 TRP A 327 PHE A 330 SER A 334 LEU A 348 SITE 4 AC1 16 PHE A 351 ASP A 352 THR A 355 TYR A 359 SITE 1 AC2 4 ILE A 367 ILE A 368 MET A 371 SER A 372 CRYST1 195.290 45.500 74.280 90.00 95.45 90.00 C 1 2 1 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.005121 0.000000 0.000489 0.00000 SCALE2 0.000000 0.021978 0.000000 0.00000 SCALE3 0.000000 0.000000 0.013524 0.00000 ATOM 1 N TYR A 38 -27.660 -11.221 13.640 1.00119.29 N ANISOU 1 N TYR A 38 8128 27900 9296 2455 -1431 -2469 N ATOM 2 CA TYR A 38 -27.091 -10.061 12.955 1.00118.47 C ANISOU 2 CA TYR A 38 8270 27362 9381 2845 -1555 -2433 C ATOM 3 C TYR A 38 -25.587 -10.250 12.679 1.00115.86 C ANISOU 3 C TYR A 38 8332 26335 9354 2658 -1519 -2269 C ATOM 4 O TYR A 38 -24.845 -10.658 13.578 1.00115.26 O ANISOU 4 O TYR A 38 8376 26026 9390 2461 -1441 -2245 O ATOM 5 CB TYR A 38 -27.330 -8.771 13.783 1.00122.21 C ANISOU 5 CB TYR A 38 8710 27874 9851 3352 -1672 -2585 C ATOM 6 CG TYR A 38 -26.460 -7.589 13.391 1.00124.38 C ANISOU 6 CG TYR A 38 9316 27559 10383 3703 -1807 -2528 C ATOM 7 CD1 TYR A 38 -26.671 -6.906 12.193 1.00127.44 C ANISOU 7 CD1 TYR A 38 9764 27867 10792 3946 -1928 -2463 C ATOM 8 CD2 TYR A 38 -25.430 -7.147 14.222 1.00123.91 C ANISOU 8 CD2 TYR A 38 9506 27036 10540 3778 -1822 -2530 C ATOM 9 CE1 TYR A 38 -25.866 -5.828 11.821 1.00127.85 C ANISOU 9 CE1 TYR A 38 10129 27369 11079 4233 -2063 -2381 C ATOM 10 CE2 TYR A 38 -24.622 -6.067 13.863 1.00124.46 C ANISOU 10 CE2 TYR A 38 9883 26560 10847 4064 -1955 -2467 C ATOM 11 CZ TYR A 38 -24.849 -5.405 12.664 1.00133.62 C ANISOU 11 CZ TYR A 38 11109 27634 12028 4284 -2078 -2385 C ATOM 12 OH TYR A 38 -24.061 -4.337 12.305 1.00135.00 O ANISOU 12 OH TYR A 38 11593 27267 12434 4537 -2221 -2296 O ATOM 13 N ILE A 39 -25.141 -9.912 11.452 1.00106.87 N ANISOU 13 N ILE A 39 7378 24894 8333 2734 -1579 -2155 N ATOM 14 CA ILE A 39 -23.738 -9.965 11.062 1.00101.90 C ANISOU 14 CA ILE A 39 7098 23649 7971 2600 -1557 -2003 C ATOM 15 C ILE A 39 -23.320 -8.563 10.635 1.00103.70 C ANISOU 15 C ILE A 39 7523 23534 8342 3011 -1709 -1952 C ATOM 16 O ILE A 39 -23.874 -8.033 9.672 1.00104.38 O ANISOU 16 O ILE A 39 7550 23763 8348 3215 -1804 -1925 O ATOM 17 CB ILE A 39 -23.485 -11.023 9.965 1.00103.39 C ANISOU 17 CB ILE A 39 7328 23796 8159 2219 -1473 -1895 C ATOM 18 N TYR A 40 -22.374 -7.943 11.376 1.00 98.32 N ANISOU 18 N TYR A 40 7075 22413 7868 3135 -1744 -1938 N ATOM 19 CA TYR A 40 -21.853 -6.594 11.100 1.00 98.36 C ANISOU 19 CA TYR A 40 7309 22020 8044 3493 -1902 -1880 C ATOM 20 C TYR A 40 -21.087 -6.551 9.765 1.00102.17 C ANISOU 20 C TYR A 40 7999 22176 8644 3381 -1920 -1671 C ATOM 21 O TYR A 40 -20.889 -5.477 9.192 1.00102.78 O ANISOU 21 O TYR A 40 8223 22023 8808 3655 -2068 -1584 O ATOM 22 CB TYR A 40 -20.953 -6.090 12.258 1.00 97.98 C ANISOU 22 CB TYR A 40 7458 21581 8188 3575 -1922 -1919 C ATOM 23 CG TYR A 40 -19.556 -6.686 12.318 1.00 95.89 C ANISOU 23 CG TYR A 40 7434 20876 8122 3239 -1818 -1782 C ATOM 24 CD1 TYR A 40 -18.533 -6.207 11.499 1.00 96.81 C ANISOU 24 CD1 TYR A 40 7821 20534 8428 3230 -1872 -1605 C ATOM 25 CD2 TYR A 40 -19.234 -7.668 13.252 1.00 94.30 C ANISOU 25 CD2 TYR A 40 7190 20722 7917 2950 -1679 -1826 C ATOM 26 CE1 TYR A 40 -17.248 -6.744 11.556 1.00 95.07 C ANISOU 26 CE1 TYR A 40 7797 19950 8375 2940 -1778 -1492 C ATOM 27 CE2 TYR A 40 -17.949 -8.202 13.328 1.00 92.04 C ANISOU 27 CE2 TYR A 40 7120 20040 7812 2675 -1595 -1709 C ATOM 28 CZ TYR A 40 -16.959 -7.737 12.478 1.00 96.48 C ANISOU 28 CZ TYR A 40 7928 20177 8551 2679 -1642 -1553 C ATOM 29 OH TYR A 40 -15.691 -8.260 12.538 1.00 90.06 O ANISOU 29 OH TYR A 40 7305 19013 7902 2423 -1560 -1448 O ATOM 30 N GLN A 41 -20.623 -7.728 9.313 1.00 97.31 N ANISOU 30 N GLN A 41 7403 21538 8033 2973 -1777 -1591 N ATOM 31 CA GLN A 41 -19.861 -7.939 8.090 1.00 96.01 C ANISOU 31 CA GLN A 41 7399 21135 7948 2805 -1759 -1417 C ATOM 32 C GLN A 41 -20.724 -7.738 6.846 1.00104.01 C ANISOU 32 C GLN A 41 8269 22461 8789 2913 -1827 -1378 C ATOM 33 O GLN A 41 -20.183 -7.375 5.803 1.00103.39 O ANISOU 33 O GLN A 41 8333 22181 8770 2926 -1877 -1220 O ATOM 34 CB GLN A 41 -19.234 -9.331 8.103 1.00 94.51 C ANISOU 34 CB GLN A 41 7237 20881 7790 2367 -1592 -1397 C ATOM 35 CG GLN A 41 -18.085 -9.435 9.103 1.00 95.05 C ANISOU 35 CG GLN A 41 7502 20551 8060 2264 -1539 -1380 C ATOM 36 CD GLN A 41 -18.351 -10.356 10.268 1.00103.17 C ANISOU 36 CD GLN A 41 8407 21756 9035 2067 -1435 -1499 C ATOM 37 OE1 GLN A 41 -17.474 -11.114 10.691 1.00 98.35 O ANISOU 37 OE1 GLN A 41 7912 20918 8537 1811 -1341 -1466 O ATOM 38 NE2 GLN A 41 -19.536 -10.288 10.849 1.00 88.61 N ANISOU 38 NE2 GLN A 41 6324 20330 7014 2188 -1455 -1632 N ATOM 39 N ASP A 42 -22.061 -7.924 6.966 1.00104.54 N ANISOU 39 N ASP A 42 8044 23044 8633 2998 -1836 -1516 N ATOM 40 CA ASP A 42 -23.047 -7.720 5.892 1.00107.27 C ANISOU 40 CA ASP A 42 8209 23765 8784 3129 -1909 -1504 C ATOM 41 C ASP A 42 -23.096 -6.246 5.430 1.00113.14 C ANISOU 41 C ASP A 42 9069 24335 9585 3565 -2104 -1414 C ATOM 42 O ASP A 42 -23.543 -5.972 4.314 1.00114.65 O ANISOU 42 O ASP A 42 9200 24696 9667 3663 -2180 -1328 O ATOM 43 CB ASP A 42 -24.460 -8.161 6.346 1.00111.47 C ANISOU 43 CB ASP A 42 8386 24905 9062 3146 -1882 -1688 C ATOM 44 CG ASP A 42 -24.688 -9.653 6.555 1.00123.06 C ANISOU 44 CG ASP A 42 9701 26627 10428 2696 -1716 -1760 C ATOM 45 OD1 ASP A 42 -24.079 -10.463 5.814 1.00122.39 O ANISOU 45 OD1 ASP A 42 9717 26392 10393 2373 -1634 -1677 O ATOM 46 OD2 ASP A 42 -25.548 -10.008 7.392 1.00131.21 O ANISOU 46 OD2 ASP A 42 10496 28047 11312 2670 -1679 -1902 O ATOM 47 N SER A 43 -22.655 -5.308 6.298 1.00109.72 N ANISOU 47 N SER A 43 8804 23564 9319 3822 -2197 -1433 N ATOM 48 CA SER A 43 -22.620 -3.868 6.028 1.00111.54 C ANISOU 48 CA SER A 43 9190 23545 9644 4236 -2407 -1352 C ATOM 49 C SER A 43 -21.331 -3.448 5.287 1.00113.15 C ANISOU 49 C SER A 43 9720 23218 10055 4136 -2448 -1104 C ATOM 50 O SER A 43 -21.359 -2.431 4.588 1.00115.36 O ANISOU 50 O SER A 43 10116 23342 10372 4391 -2620 -963 O ATOM 51 CB SER A 43 -22.773 -3.069 7.321 1.00117.06 C ANISOU 51 CB SER A 43 9918 24138 10423 4559 -2502 -1516 C ATOM 52 OG SER A 43 -21.623 -3.140 8.152 1.00125.17 O ANISOU 52 OG SER A 43 11193 24686 11679 4438 -2465 -1487 O ATOM 53 N ILE A 44 -20.218 -4.228 5.431 1.00104.83 N ANISOU 53 N ILE A 44 8801 21904 9124 3767 -2298 -1042 N ATOM 54 CA ILE A 44 -18.919 -3.974 4.776 1.00102.15 C ANISOU 54 CA ILE A 44 8736 21115 8960 3622 -2309 -817 C ATOM 55 C ILE A 44 -19.071 -4.095 3.238 1.00105.69 C ANISOU 55 C ILE A 44 9143 21732 9282 3547 -2327 -648 C ATOM 56 O ILE A 44 -19.610 -5.090 2.734 1.00104.76 O ANISOU 56 O ILE A 44 8822 21995 8987 3347 -2214 -712 O ATOM 57 CB ILE A 44 -17.781 -4.895 5.316 1.00101.66 C ANISOU 57 CB ILE A 44 8782 20817 9028 3257 -2137 -821 C ATOM 58 CG1 ILE A 44 -17.714 -4.874 6.864 1.00100.99 C ANISOU 58 CG1 ILE A 44 8706 20631 9033 3314 -2110 -992 C ATOM 59 CG2 ILE A 44 -16.426 -4.500 4.703 1.00101.44 C ANISOU 59 CG2 ILE A 44 9021 20350 9171 3143 -2163 -594 C ATOM 60 CD1 ILE A 44 -16.730 -5.889 7.524 1.00102.22 C ANISOU 60 CD1 ILE A 44 8931 20618 9291 2964 -1938 -1015 C ATOM 61 N SER A 45 -18.605 -3.061 2.510 1.00102.36 N ANISOU 61 N SER A 45 8914 21030 8947 3702 -2480 -431 N ATOM 62 CA SER A 45 -18.675 -2.998 1.051 1.00102.59 C ANISOU 62 CA SER A 45 8923 21199 8857 3659 -2521 -237 C ATOM 63 C SER A 45 -17.749 -4.034 0.408 1.00104.16 C ANISOU 63 C SER A 45 9147 21385 9045 3249 -2346 -161 C ATOM 64 O SER A 45 -16.851 -4.559 1.071 1.00101.67 O ANISOU 64 O SER A 45 8934 20829 8868 3035 -2230 -205 O ATOM 65 CB SER A 45 -18.334 -1.595 0.552 1.00107.20 C ANISOU 65 CB SER A 45 9734 21445 9554 3906 -2739 2 C ATOM 66 OG SER A 45 -16.944 -1.319 0.599 1.00112.82 O ANISOU 66 OG SER A 45 10706 21696 10464 3727 -2730 174 O ATOM 67 N LEU A 46 -17.992 -4.328 -0.883 1.00101.33 N ANISOU 67 N LEU A 46 8684 21305 8511 3158 -2335 -60 N ATOM 68 CA LEU A 46 -17.250 -5.266 -1.722 1.00 99.36 C ANISOU 68 CA LEU A 46 8428 21118 8207 2813 -2192 -2 C ATOM 69 C LEU A 46 -15.744 -4.879 -1.785 1.00102.62 C ANISOU 69 C LEU A 46 9101 21079 8811 2687 -2190 193 C ATOM 70 O LEU A 46 -14.927 -5.751 -1.465 1.00100.17 O ANISOU 70 O LEU A 46 8827 20660 8574 2424 -2038 119 O ATOM 71 CB LEU A 46 -17.911 -5.313 -3.123 1.00101.35 C ANISOU 71 CB LEU A 46 8525 21761 8222 2829 -2234 89 C ATOM 72 CG LEU A 46 -17.345 -6.171 -4.276 1.00105.47 C ANISOU 72 CG LEU A 46 9003 22446 8626 2527 -2118 147 C ATOM 73 CD1 LEU A 46 -16.273 -5.439 -5.076 1.00106.51 C ANISOU 73 CD1 LEU A 46 9325 22326 8816 2499 -2185 441 C ATOM 74 CD2 LEU A 46 -16.951 -7.559 -3.847 1.00104.96 C ANISOU 74 CD2 LEU A 46 8888 22405 8588 2215 -1923 -61 C ATOM 75 N PRO A 47 -15.332 -3.617 -2.117 1.00100.60 N ANISOU 75 N PRO A 47 9031 20549 8645 2858 -2359 437 N ATOM 76 CA PRO A 47 -13.885 -3.314 -2.157 1.00 99.27 C ANISOU 76 CA PRO A 47 9088 19988 8643 2693 -2349 623 C ATOM 77 C PRO A 47 -13.168 -3.512 -0.816 1.00101.17 C ANISOU 77 C PRO A 47 9446 19900 9095 2615 -2274 492 C ATOM 78 O PRO A 47 -12.050 -4.029 -0.810 1.00 99.41 O ANISOU 78 O PRO A 47 9293 19535 8942 2360 -2156 524 O ATOM 79 CB PRO A 47 -13.838 -1.845 -2.595 1.00103.61 C ANISOU 79 CB PRO A 47 9809 20304 9253 2922 -2580 892 C ATOM 80 CG PRO A 47 -15.135 -1.605 -3.276 1.00110.11 C ANISOU 80 CG PRO A 47 10467 21490 9880 3146 -2680 892 C ATOM 81 CD PRO A 47 -16.122 -2.434 -2.526 1.00104.73 C ANISOU 81 CD PRO A 47 9569 21106 9118 3192 -2575 570 C ATOM 82 N TRP A 48 -13.805 -3.139 0.311 1.00 97.94 N ANISOU 82 N TRP A 48 9039 19404 8769 2837 -2339 334 N ATOM 83 CA TRP A 48 -13.193 -3.299 1.636 1.00 96.09 C ANISOU 83 CA TRP A 48 8903 18888 8717 2782 -2277 203 C ATOM 84 C TRP A 48 -13.174 -4.760 2.079 1.00 95.53 C ANISOU 84 C TRP A 48 8686 19017 8592 2532 -2065 -2 C ATOM 85 O TRP A 48 -12.293 -5.145 2.859 1.00 93.06 O ANISOU 85 O TRP A 48 8467 18473 8419 2380 -1977 -51 O ATOM 86 CB TRP A 48 -13.877 -2.423 2.695 1.00 96.68 C ANISOU 86 CB TRP A 48 9013 18842 8876 3108 -2417 82 C ATOM 87 CG TRP A 48 -13.437 -0.993 2.626 1.00100.09 C ANISOU 87 CG TRP A 48 9689 18876 9466 3303 -2630 275 C ATOM 88 CD1 TRP A 48 -14.160 0.065 2.155 1.00106.19 C ANISOU 88 CD1 TRP A 48 10500 19640 10209 3606 -2838 377 C ATOM 89 CD2 TRP A 48 -12.130 -0.483 2.934 1.00 99.39 C ANISOU 89 CD2 TRP A 48 9844 18336 9584 3180 -2664 416 C ATOM 90 NE1 TRP A 48 -13.396 1.210 2.182 1.00107.27 N ANISOU 90 NE1 TRP A 48 10910 19313 10536 3676 -3011 574 N ATOM 91 CE2 TRP A 48 -12.145 0.902 2.657 1.00106.32 C ANISOU 91 CE2 TRP A 48 10913 18924 10559 3406 -2905 600 C ATOM 92 CE3 TRP A 48 -10.948 -1.062 3.432 1.00 98.35 C ANISOU 92 CE3 TRP A 48 9787 18016 9565 2901 -2523 403 C ATOM 93 CZ2 TRP A 48 -11.024 1.717 2.858 1.00105.97 C ANISOU 93 CZ2 TRP A 48 11132 18412 10720 3332 -3008 775 C ATOM 94 CZ3 TRP A 48 -9.840 -0.254 3.629 1.00100.19 C ANISOU 94 CZ3 TRP A 48 10259 17819 9988 2844 -2616 568 C ATOM 95 CH2 TRP A 48 -9.882 1.117 3.340 1.00103.66 C ANISOU 95 CH2 TRP A 48 10887 17979 10521 3042 -2854 753 C ATOM 96 N LYS A 49 -14.117 -5.576 1.564 1.00 90.14 N ANISOU 96 N LYS A 49 7782 18756 7710 2480 -1993 -114 N ATOM 97 CA LYS A 49 -14.172 -6.993 1.892 1.00 87.01 C ANISOU 97 CA LYS A 49 7257 18544 7260 2226 -1813 -298 C ATOM 98 C LYS A 49 -13.039 -7.749 1.187 1.00 88.38 C ANISOU 98 C LYS A 49 7495 18634 7453 1937 -1697 -221 C ATOM 99 O LYS A 49 -12.345 -8.519 1.845 1.00 85.42 O ANISOU 99 O LYS A 49 7167 18113 7177 1752 -1583 -307 O ATOM 100 CB LYS A 49 -15.545 -7.590 1.566 1.00 89.64 C ANISOU 100 CB LYS A 49 7336 19348 7376 2247 -1790 -442 C ATOM 101 CG LYS A 49 -16.393 -7.774 2.823 1.00 90.76 C ANISOU 101 CG LYS A 49 7361 19615 7508 2341 -1778 -641 C ATOM 102 CD LYS A 49 -17.723 -8.413 2.530 1.00 91.31 C ANISOU 102 CD LYS A 49 7162 20179 7352 2325 -1751 -779 C ATOM 103 CE LYS A 49 -18.300 -9.053 3.756 1.00 90.45 C ANISOU 103 CE LYS A 49 6924 20224 7221 2257 -1675 -974 C ATOM 104 NZ LYS A 49 -19.698 -9.510 3.515 1.00101.17 N ANISOU 104 NZ LYS A 49 7999 22099 8343 2252 -1668 -1100 N ATOM 105 N VAL A 50 -12.806 -7.476 -0.118 1.00 86.18 N ANISOU 105 N VAL A 50 7220 18445 7078 1914 -1735 -54 N ATOM 106 CA VAL A 50 -11.743 -8.120 -0.907 1.00 84.81 C ANISOU 106 CA VAL A 50 7085 18248 6891 1666 -1633 14 C ATOM 107 C VAL A 50 -10.348 -7.684 -0.382 1.00 88.20 C ANISOU 107 C VAL A 50 7722 18266 7524 1605 -1630 134 C ATOM 108 O VAL A 50 -9.456 -8.532 -0.288 1.00 85.64 O ANISOU 108 O VAL A 50 7423 17870 7249 1396 -1507 78 O ATOM 109 CB VAL A 50 -11.915 -7.886 -2.426 1.00 89.73 C ANISOU 109 CB VAL A 50 7637 19128 7329 1667 -1681 166 C ATOM 110 CG1 VAL A 50 -10.837 -8.612 -3.229 1.00 88.65 C ANISOU 110 CG1 VAL A 50 7508 19024 7151 1420 -1568 200 C ATOM 111 CG2 VAL A 50 -13.294 -8.346 -2.878 1.00 90.70 C ANISOU 111 CG2 VAL A 50 7542 19671 7247 1724 -1686 32 C ATOM 112 N LEU A 51 -10.186 -6.396 0.013 1.00 86.66 N ANISOU 112 N LEU A 51 7674 17801 7451 1790 -1773 281 N ATOM 113 CA LEU A 51 -8.944 -5.880 0.613 1.00 85.80 C ANISOU 113 CA LEU A 51 7763 17297 7541 1737 -1792 390 C ATOM 114 C LEU A 51 -8.647 -6.607 1.909 1.00 85.98 C ANISOU 114 C LEU A 51 7798 17183 7687 1657 -1686 191 C ATOM 115 O LEU A 51 -7.510 -7.016 2.117 1.00 83.88 O ANISOU 115 O LEU A 51 7608 16748 7514 1483 -1602 209 O ATOM 116 CB LEU A 51 -9.025 -4.370 0.890 1.00 88.01 C ANISOU 116 CB LEU A 51 8201 17306 7933 1967 -1991 548 C ATOM 117 CG LEU A 51 -8.709 -3.426 -0.261 1.00 95.03 C ANISOU 117 CG LEU A 51 9178 18152 8778 1984 -2119 845 C ATOM 118 CD1 LEU A 51 -9.394 -2.083 -0.053 1.00 97.68 C ANISOU 118 CD1 LEU A 51 9626 18306 9182 2282 -2343 943 C ATOM 119 CD2 LEU A 51 -7.213 -3.224 -0.401 1.00 96.96 C ANISOU 119 CD2 LEU A 51 9563 18150 9126 1769 -2092 1024 C ATOM 120 N LEU A 52 -9.683 -6.803 2.758 1.00 82.83 N ANISOU 120 N LEU A 52 7306 16896 7269 1781 -1687 3 N ATOM 121 CA LEU A 52 -9.594 -7.510 4.045 1.00 81.42 C ANISOU 121 CA LEU A 52 7116 16642 7177 1713 -1595 -183 C ATOM 122 C LEU A 52 -9.172 -8.957 3.871 1.00 83.11 C ANISOU 122 C LEU A 52 7258 16967 7351 1447 -1428 -283 C ATOM 123 O LEU A 52 -8.471 -9.485 4.738 1.00 81.26 O ANISOU 123 O LEU A 52 7083 16561 7232 1336 -1352 -354 O ATOM 124 CB LEU A 52 -10.925 -7.470 4.808 1.00 82.49 C ANISOU 124 CB LEU A 52 7122 16974 7245 1889 -1631 -350 C ATOM 125 CG LEU A 52 -10.905 -6.723 6.138 1.00 87.56 C ANISOU 125 CG LEU A 52 7854 17392 8024 2061 -1706 -412 C ATOM 126 CD1 LEU A 52 -12.311 -6.363 6.565 1.00 89.99 C ANISOU 126 CD1 LEU A 52 8019 17946 8225 2307 -1784 -544 C ATOM 127 CD2 LEU A 52 -10.192 -7.521 7.223 1.00 86.89 C ANISOU 127 CD2 LEU A 52 7803 17171 8040 1883 -1586 -514 C ATOM 128 N VAL A 53 -9.608 -9.598 2.760 1.00 79.02 N ANISOU 128 N VAL A 53 6618 16735 6671 1354 -1383 -297 N ATOM 129 CA VAL A 53 -9.251 -10.976 2.422 1.00 77.22 C ANISOU 129 CA VAL A 53 6329 16613 6397 1115 -1246 -408 C ATOM 130 C VAL A 53 -7.776 -11.000 2.008 1.00 80.65 C ANISOU 130 C VAL A 53 6883 16845 6915 997 -1203 -296 C ATOM 131 O VAL A 53 -7.043 -11.877 2.454 1.00 78.12 O ANISOU 131 O VAL A 53 6597 16411 6674 850 -1108 -385 O ATOM 132 CB VAL A 53 -10.186 -11.580 1.344 1.00 81.54 C ANISOU 132 CB VAL A 53 6706 17539 6738 1065 -1228 -478 C ATOM 133 CG1 VAL A 53 -9.674 -12.931 0.838 1.00 80.25 C ANISOU 133 CG1 VAL A 53 6508 17445 6537 827 -1109 -592 C ATOM 134 CG2 VAL A 53 -11.602 -11.716 1.882 1.00 81.96 C ANISOU 134 CG2 VAL A 53 6617 17820 6705 1146 -1253 -611 C ATOM 135 N MET A 54 -7.344 -10.012 1.205 1.00 80.01 N ANISOU 135 N MET A 54 6862 16724 6815 1063 -1282 -93 N ATOM 136 CA MET A 54 -5.965 -9.871 0.734 1.00 80.61 C ANISOU 136 CA MET A 54 7027 16660 6941 951 -1254 45 C ATOM 137 C MET A 54 -4.988 -9.605 1.887 1.00 83.14 C ANISOU 137 C MET A 54 7491 16635 7465 930 -1247 63 C ATOM 138 O MET A 54 -3.888 -10.166 1.875 1.00 82.27 O ANISOU 138 O MET A 54 7409 16449 7403 787 -1161 51 O ATOM 139 CB MET A 54 -5.863 -8.751 -0.299 1.00 85.36 C ANISOU 139 CB MET A 54 7661 17304 7468 1021 -1363 292 C ATOM 140 CG MET A 54 -6.148 -9.208 -1.700 1.00 91.27 C ANISOU 140 CG MET A 54 8272 18405 8002 955 -1331 308 C ATOM 141 SD MET A 54 -5.717 -7.913 -2.894 1.00 99.12 S ANISOU 141 SD MET A 54 9319 19431 8910 987 -1454 652 S ATOM 142 CE MET A 54 -7.306 -7.041 -3.028 1.00 97.59 C ANISOU 142 CE MET A 54 9087 19355 8637 1240 -1611 701 C ATOM 143 N LEU A 55 -5.385 -8.765 2.879 1.00 78.47 N ANISOU 143 N LEU A 55 6980 15852 6985 1084 -1341 76 N ATOM 144 CA LEU A 55 -4.547 -8.439 4.039 1.00 76.62 C ANISOU 144 CA LEU A 55 6876 15300 6936 1080 -1350 80 C ATOM 145 C LEU A 55 -4.347 -9.669 4.926 1.00 76.95 C ANISOU 145 C LEU A 55 6879 15330 7027 968 -1225 -113 C ATOM 146 O LEU A 55 -3.225 -9.941 5.343 1.00 75.52 O ANISOU 146 O LEU A 55 6769 14977 6949 863 -1172 -102 O ATOM 147 CB LEU A 55 -5.154 -7.282 4.865 1.00 77.58 C ANISOU 147 CB LEU A 55 7078 15254 7145 1295 -1491 98 C ATOM 148 CG LEU A 55 -4.419 -6.924 6.175 1.00 81.15 C ANISOU 148 CG LEU A 55 7657 15396 7780 1306 -1511 68 C ATOM 149 CD1 LEU A 55 -3.325 -5.900 5.943 1.00 81.66 C ANISOU 149 CD1 LEU A 55 7880 15194 7954 1273 -1603 275 C ATOM 150 CD2 LEU A 55 -5.383 -6.435 7.224 1.00 84.48 C ANISOU 150 CD2 LEU A 55 8075 15787 8238 1513 -1591 -61 C ATOM 151 N LEU A 56 -5.435 -10.397 5.209 1.00 72.36 N ANISOU 151 N LEU A 56 6185 14941 6367 984 -1187 -275 N ATOM 152 CA LEU A 56 -5.466 -11.592 6.049 1.00 70.50 C ANISOU 152 CA LEU A 56 5911 14713 6162 869 -1087 -444 C ATOM 153 C LEU A 56 -4.703 -12.750 5.397 1.00 73.64 C ANISOU 153 C LEU A 56 6291 15151 6537 682 -981 -488 C ATOM 154 O LEU A 56 -3.909 -13.413 6.072 1.00 71.52 O ANISOU 154 O LEU A 56 6076 14728 6369 587 -919 -543 O ATOM 155 CB LEU A 56 -6.929 -11.976 6.332 1.00 71.13 C ANISOU 155 CB LEU A 56 5857 15038 6132 916 -1091 -575 C ATOM 156 CG LEU A 56 -7.544 -11.455 7.642 1.00 76.17 C ANISOU 156 CG LEU A 56 6491 15632 6817 1053 -1143 -637 C ATOM 157 CD1 LEU A 56 -7.271 -9.963 7.876 1.00 77.15 C ANISOU 157 CD1 LEU A 56 6729 15554 7032 1254 -1266 -526 C ATOM 158 CD2 LEU A 56 -9.030 -11.706 7.679 1.00 79.50 C ANISOU 158 CD2 LEU A 56 6746 16371 7089 1109 -1156 -745 C ATOM 159 N ALA A 57 -4.899 -12.950 4.078 1.00 71.78 N ANISOU 159 N ALA A 57 5982 15124 6168 646 -971 -465 N ATOM 160 CA ALA A 57 -4.210 -13.974 3.294 1.00 71.69 C ANISOU 160 CA ALA A 57 5941 15187 6110 500 -885 -528 C ATOM 161 C ALA A 57 -2.704 -13.686 3.207 1.00 76.03 C ANISOU 161 C ALA A 57 6581 15560 6748 462 -864 -420 C ATOM 162 O ALA A 57 -1.920 -14.641 3.195 1.00 75.64 O ANISOU 162 O ALA A 57 6536 15476 6729 362 -787 -513 O ATOM 163 CB ALA A 57 -4.809 -14.066 1.901 1.00 73.78 C ANISOU 163 CB ALA A 57 6095 15749 6189 493 -894 -525 C ATOM 164 N LEU A 58 -2.287 -12.389 3.180 1.00 73.02 N ANISOU 164 N LEU A 58 6270 15066 6409 539 -941 -229 N ATOM 165 CA LEU A 58 -0.855 -12.104 3.143 1.00 73.22 C ANISOU 165 CA LEU A 58 6365 14947 6509 475 -924 -118 C ATOM 166 C LEU A 58 -0.232 -12.338 4.536 1.00 72.36 C ANISOU 166 C LEU A 58 6344 14578 6573 461 -901 -179 C ATOM 167 O LEU A 58 0.848 -12.903 4.582 1.00 71.35 O ANISOU 167 O LEU A 58 6228 14393 6489 378 -838 -198 O ATOM 168 CB LEU A 58 -0.470 -10.730 2.531 1.00 75.64 C ANISOU 168 CB LEU A 58 6722 15221 6796 509 -1018 128 C ATOM 169 CG LEU A 58 -0.781 -9.422 3.270 1.00 82.16 C ANISOU 169 CG LEU A 58 7664 15820 7735 631 -1147 247 C ATOM 170 CD1 LEU A 58 0.392 -8.994 4.171 1.00 81.78 C ANISOU 170 CD1 LEU A 58 7731 15491 7849 581 -1161 313 C ATOM 171 CD2 LEU A 58 -1.079 -8.299 2.274 1.00 87.35 C ANISOU 171 CD2 LEU A 58 8337 16545 8306 691 -1261 458 C ATOM 172 N ILE A 59 -0.928 -11.994 5.648 1.00 66.47 N ANISOU 172 N ILE A 59 5640 13710 5907 549 -948 -223 N ATOM 173 CA ILE A 59 -0.449 -12.254 7.018 1.00 64.43 C ANISOU 173 CA ILE A 59 5449 13241 5789 536 -927 -288 C ATOM 174 C ILE A 59 -0.213 -13.773 7.191 1.00 64.12 C ANISOU 174 C ILE A 59 5370 13242 5751 426 -823 -442 C ATOM 175 O ILE A 59 0.838 -14.178 7.682 1.00 62.47 O ANISOU 175 O ILE A 59 5207 12897 5631 370 -782 -453 O ATOM 176 CB ILE A 59 -1.425 -11.689 8.123 1.00 68.25 C ANISOU 176 CB ILE A 59 5955 13659 6319 661 -996 -333 C ATOM 177 CG1 ILE A 59 -1.569 -10.139 8.085 1.00 70.92 C ANISOU 177 CG1 ILE A 59 6366 13888 6690 799 -1126 -197 C ATOM 178 CG2 ILE A 59 -1.085 -12.189 9.555 1.00 66.51 C ANISOU 178 CG2 ILE A 59 5774 13289 6208 632 -960 -424 C ATOM 179 CD1 ILE A 59 -0.278 -9.269 8.484 1.00 85.33 C ANISOU 179 CD1 ILE A 59 8322 15445 8654 775 -1178 -69 C ATOM 180 N THR A 60 -1.187 -14.596 6.766 1.00 60.13 N ANISOU 180 N THR A 60 4782 12920 5146 394 -793 -557 N ATOM 181 CA THR A 60 -1.166 -16.059 6.860 1.00 59.29 C ANISOU 181 CA THR A 60 4651 12839 5039 284 -721 -710 C ATOM 182 C THR A 60 0.029 -16.609 6.076 1.00 63.84 C ANISOU 182 C THR A 60 5231 13413 5612 226 -668 -727 C ATOM 183 O THR A 60 0.780 -17.432 6.607 1.00 62.44 O ANISOU 183 O THR A 60 5098 13105 5521 177 -628 -800 O ATOM 184 CB THR A 60 -2.511 -16.633 6.363 1.00 65.90 C ANISOU 184 CB THR A 60 5391 13896 5750 251 -721 -813 C ATOM 185 OG1 THR A 60 -3.593 -16.020 7.070 1.00 62.04 O ANISOU 185 OG1 THR A 60 4873 13454 5245 328 -772 -797 O ATOM 186 CG2 THR A 60 -2.601 -18.140 6.511 1.00 64.51 C ANISOU 186 CG2 THR A 60 5211 13713 5586 118 -670 -970 C ATOM 187 N LEU A 61 0.219 -16.124 4.828 1.00 61.94 N ANISOU 187 N LEU A 61 4938 13334 5262 240 -674 -653 N ATOM 188 CA LEU A 61 1.326 -16.540 3.967 1.00 61.71 C ANISOU 188 CA LEU A 61 4880 13377 5191 197 -624 -669 C ATOM 189 C LEU A 61 2.693 -16.111 4.585 1.00 65.81 C ANISOU 189 C LEU A 61 5463 13716 5824 199 -617 -571 C ATOM 190 O LEU A 61 3.600 -16.944 4.675 1.00 66.21 O ANISOU 190 O LEU A 61 5513 13731 5912 171 -565 -661 O ATOM 191 CB LEU A 61 1.139 -15.985 2.535 1.00 62.33 C ANISOU 191 CB LEU A 61 4871 13712 5100 205 -638 -584 C ATOM 192 CG LEU A 61 2.256 -16.266 1.501 1.00 66.97 C ANISOU 192 CG LEU A 61 5395 14454 5599 165 -588 -584 C ATOM 193 CD1 LEU A 61 2.280 -17.725 1.064 1.00 67.34 C ANISOU 193 CD1 LEU A 61 5392 14592 5601 133 -528 -827 C ATOM 194 CD2 LEU A 61 2.094 -15.391 0.295 1.00 69.21 C ANISOU 194 CD2 LEU A 61 5602 14978 5717 167 -618 -430 C ATOM 195 N ALA A 62 2.816 -14.838 5.033 1.00 61.18 N ANISOU 195 N ALA A 62 4933 13017 5295 238 -679 -401 N ATOM 196 CA ALA A 62 4.030 -14.289 5.635 1.00 60.39 C ANISOU 196 CA ALA A 62 4893 12754 5300 223 -688 -297 C ATOM 197 C ALA A 62 4.432 -15.081 6.885 1.00 63.72 C ANISOU 197 C ALA A 62 5366 12994 5852 218 -654 -412 C ATOM 198 O ALA A 62 5.624 -15.260 7.109 1.00 63.59 O ANISOU 198 O ALA A 62 5354 12921 5885 190 -624 -403 O ATOM 199 CB ALA A 62 3.838 -12.820 5.974 1.00 61.30 C ANISOU 199 CB ALA A 62 5079 12749 5464 266 -784 -124 C ATOM 200 N THR A 63 3.443 -15.595 7.656 1.00 59.54 N ANISOU 200 N THR A 63 4860 12403 5359 239 -661 -514 N ATOM 201 CA THR A 63 3.655 -16.419 8.861 1.00 58.28 C ANISOU 201 CA THR A 63 4750 12088 5307 223 -638 -607 C ATOM 202 C THR A 63 4.206 -17.801 8.464 1.00 62.00 C ANISOU 202 C THR A 63 5200 12586 5771 178 -578 -740 C ATOM 203 O THR A 63 5.067 -18.339 9.151 1.00 61.38 O ANISOU 203 O THR A 63 5162 12376 5784 175 -561 -773 O ATOM 204 CB THR A 63 2.323 -16.568 9.667 1.00 61.27 C ANISOU 204 CB THR A 63 5135 12456 5689 235 -663 -664 C ATOM 205 OG1 THR A 63 1.755 -15.283 9.913 1.00 58.91 O ANISOU 205 OG1 THR A 63 4847 12154 5384 314 -729 -571 O ATOM 206 CG2 THR A 63 2.503 -17.310 11.005 1.00 55.67 C ANISOU 206 CG2 THR A 63 4477 11598 5079 204 -650 -722 C ATOM 207 N THR A 64 3.671 -18.381 7.382 1.00 59.06 N ANISOU 207 N THR A 64 4768 12382 5292 156 -557 -827 N ATOM 208 CA THR A 64 4.046 -19.703 6.890 1.00 59.11 C ANISOU 208 CA THR A 64 4760 12413 5286 130 -519 -988 C ATOM 209 C THR A 64 5.480 -19.680 6.405 1.00 62.51 C ANISOU 209 C THR A 64 5160 12881 5711 164 -487 -977 C ATOM 210 O THR A 64 6.258 -20.536 6.807 1.00 62.82 O ANISOU 210 O THR A 64 5231 12814 5826 184 -471 -1070 O ATOM 211 CB THR A 64 3.070 -20.154 5.778 1.00 66.50 C ANISOU 211 CB THR A 64 5631 13546 6092 97 -516 -1091 C ATOM 212 OG1 THR A 64 1.733 -20.153 6.286 1.00 67.09 O ANISOU 212 OG1 THR A 64 5714 13616 6161 59 -546 -1097 O ATOM 213 CG2 THR A 64 3.400 -21.529 5.218 1.00 63.39 C ANISOU 213 CG2 THR A 64 5234 13164 5687 78 -493 -1289 C ATOM 214 N LEU A 65 5.839 -18.695 5.578 1.00 58.41 N ANISOU 214 N LEU A 65 4573 12521 5097 170 -483 -854 N ATOM 215 CA LEU A 65 7.182 -18.623 5.019 1.00 58.40 C ANISOU 215 CA LEU A 65 4509 12627 5055 182 -448 -833 C ATOM 216 C LEU A 65 8.211 -18.210 6.071 1.00 61.27 C ANISOU 216 C LEU A 65 4918 12821 5540 188 -456 -739 C ATOM 217 O LEU A 65 9.292 -18.820 6.109 1.00 61.73 O ANISOU 217 O LEU A 65 4945 12890 5618 219 -424 -814 O ATOM 218 CB LEU A 65 7.241 -17.707 3.777 1.00 59.22 C ANISOU 218 CB LEU A 65 4517 12985 5000 154 -447 -705 C ATOM 219 CG LEU A 65 6.404 -18.191 2.558 1.00 64.48 C ANISOU 219 CG LEU A 65 5106 13880 5512 152 -433 -816 C ATOM 220 CD1 LEU A 65 6.305 -17.124 1.493 1.00 65.42 C ANISOU 220 CD1 LEU A 65 5149 14228 5479 120 -451 -639 C ATOM 221 CD2 LEU A 65 6.953 -19.490 1.967 1.00 66.33 C ANISOU 221 CD2 LEU A 65 5278 14233 5691 186 -383 -1042 C ATOM 222 N SER A 66 7.878 -17.233 6.953 1.00 55.00 N ANISOU 222 N SER A 66 4195 11875 4825 173 -504 -599 N ATOM 223 CA SER A 66 8.834 -16.787 7.970 1.00 53.47 C ANISOU 223 CA SER A 66 4044 11529 4742 169 -520 -518 C ATOM 224 C SER A 66 9.185 -17.921 8.947 1.00 56.49 C ANISOU 224 C SER A 66 4473 11763 5230 207 -502 -650 C ATOM 225 O SER A 66 10.354 -18.054 9.323 1.00 55.88 O ANISOU 225 O SER A 66 4377 11660 5196 221 -488 -644 O ATOM 226 CB SER A 66 8.330 -15.559 8.715 1.00 55.14 C ANISOU 226 CB SER A 66 4331 11600 5017 160 -588 -381 C ATOM 227 OG SER A 66 7.278 -15.897 9.596 1.00 65.43 O ANISOU 227 OG SER A 66 5697 12780 6383 193 -607 -458 O ATOM 228 N ASN A 67 8.196 -18.765 9.299 1.00 51.75 N ANISOU 228 N ASN A 67 3922 11082 4659 215 -507 -760 N ATOM 229 CA ASN A 67 8.421 -19.900 10.184 1.00 51.17 C ANISOU 229 CA ASN A 67 3907 10852 4682 235 -505 -864 C ATOM 230 C ASN A 67 9.088 -21.048 9.438 1.00 57.58 C ANISOU 230 C ASN A 67 4684 11725 5468 280 -476 -1014 C ATOM 231 O ASN A 67 9.941 -21.704 10.025 1.00 57.29 O ANISOU 231 O ASN A 67 4674 11584 5510 330 -479 -1061 O ATOM 232 CB ASN A 67 7.140 -20.346 10.867 1.00 49.99 C ANISOU 232 CB ASN A 67 3822 10606 4566 197 -531 -904 C ATOM 233 CG ASN A 67 6.750 -19.446 12.015 1.00 62.85 C ANISOU 233 CG ASN A 67 5489 12145 6245 189 -564 -794 C ATOM 234 OD1 ASN A 67 7.365 -19.448 13.087 1.00 57.59 O ANISOU 234 OD1 ASN A 67 4865 11354 5665 201 -577 -761 O ATOM 235 ND2 ASN A 67 5.726 -18.645 11.821 1.00 54.08 N ANISOU 235 ND2 ASN A 67 4360 11111 5077 183 -586 -745 N ATOM 236 N ALA A 68 8.762 -21.256 8.135 1.00 57.37 N ANISOU 236 N ALA A 68 4592 11880 5326 278 -454 -1095 N ATOM 237 CA ALA A 68 9.410 -22.285 7.291 1.00 58.77 C ANISOU 237 CA ALA A 68 4721 12151 5457 343 -432 -1270 C ATOM 238 C ALA A 68 10.929 -22.041 7.205 1.00 64.89 C ANISOU 238 C ALA A 68 5416 13022 6218 409 -404 -1241 C ATOM 239 O ALA A 68 11.711 -22.996 7.258 1.00 65.66 O ANISOU 239 O ALA A 68 5509 13086 6351 502 -404 -1380 O ATOM 240 CB ALA A 68 8.810 -22.294 5.901 1.00 60.09 C ANISOU 240 CB ALA A 68 4809 12549 5475 324 -412 -1344 C ATOM 241 N PHE A 69 11.330 -20.750 7.112 1.00 61.57 N ANISOU 241 N PHE A 69 4934 12713 5747 358 -392 -1056 N ATOM 242 CA PHE A 69 12.720 -20.297 7.080 1.00 61.99 C ANISOU 242 CA PHE A 69 4896 12886 5773 375 -369 -985 C ATOM 243 C PHE A 69 13.434 -20.669 8.399 1.00 65.48 C ANISOU 243 C PHE A 69 5400 13121 6358 425 -390 -994 C ATOM 244 O PHE A 69 14.496 -21.283 8.350 1.00 65.57 O ANISOU 244 O PHE A 69 5347 13201 6364 514 -374 -1087 O ATOM 245 CB PHE A 69 12.776 -18.776 6.824 1.00 63.78 C ANISOU 245 CB PHE A 69 5082 13214 5939 268 -377 -757 C ATOM 246 CG PHE A 69 14.088 -18.124 7.177 1.00 66.15 C ANISOU 246 CG PHE A 69 5318 13569 6246 235 -373 -638 C ATOM 247 CD1 PHE A 69 15.214 -18.311 6.382 1.00 71.51 C ANISOU 247 CD1 PHE A 69 5843 14524 6805 253 -327 -672 C ATOM 248 CD2 PHE A 69 14.211 -17.349 8.322 1.00 67.71 C ANISOU 248 CD2 PHE A 69 5597 13568 6561 184 -418 -507 C ATOM 249 CE1 PHE A 69 16.443 -17.735 6.728 1.00 72.58 C ANISOU 249 CE1 PHE A 69 5899 14741 6936 204 -325 -561 C ATOM 250 CE2 PHE A 69 15.444 -16.777 8.667 1.00 71.24 C ANISOU 250 CE2 PHE A 69 5981 14073 7014 136 -421 -406 C ATOM 251 CZ PHE A 69 16.548 -16.974 7.869 1.00 70.42 C ANISOU 251 CZ PHE A 69 5718 14250 6790 138 -374 -426 C ATOM 252 N VAL A 70 12.828 -20.332 9.562 1.00 60.84 N ANISOU 252 N VAL A 70 4926 12304 5885 383 -430 -907 N ATOM 253 CA VAL A 70 13.377 -20.613 10.895 1.00 60.27 C ANISOU 253 CA VAL A 70 4917 12044 5939 417 -457 -893 C ATOM 254 C VAL A 70 13.565 -22.134 11.106 1.00 65.10 C ANISOU 254 C VAL A 70 5576 12546 6613 519 -469 -1065 C ATOM 255 O VAL A 70 14.588 -22.530 11.667 1.00 64.81 O ANISOU 255 O VAL A 70 5527 12467 6631 596 -479 -1086 O ATOM 256 CB VAL A 70 12.536 -19.976 12.031 1.00 63.34 C ANISOU 256 CB VAL A 70 5406 12251 6408 352 -497 -785 C ATOM 257 CG1 VAL A 70 13.162 -20.244 13.397 1.00 62.87 C ANISOU 257 CG1 VAL A 70 5397 12034 6458 384 -525 -766 C ATOM 258 CG2 VAL A 70 12.386 -18.474 11.826 1.00 63.05 C ANISOU 258 CG2 VAL A 70 5344 12281 6329 276 -510 -630 C ATOM 259 N ILE A 71 12.607 -22.976 10.638 1.00 62.46 N ANISOU 259 N ILE A 71 5297 12164 6271 520 -478 -1187 N ATOM 260 CA ILE A 71 12.696 -24.444 10.761 1.00 62.98 C ANISOU 260 CA ILE A 71 5436 12086 6408 606 -512 -1354 C ATOM 261 C ILE A 71 13.860 -24.978 9.901 1.00 68.14 C ANISOU 261 C ILE A 71 5988 12899 7002 745 -493 -1500 C ATOM 262 O ILE A 71 14.688 -25.734 10.406 1.00 68.69 O ANISOU 262 O ILE A 71 6082 12868 7147 862 -525 -1571 O ATOM 263 CB ILE A 71 11.367 -25.180 10.416 1.00 66.20 C ANISOU 263 CB ILE A 71 5928 12406 6818 542 -538 -1451 C ATOM 264 CG1 ILE A 71 10.212 -24.754 11.346 1.00 64.58 C ANISOU 264 CG1 ILE A 71 5800 12081 6656 415 -557 -1320 C ATOM 265 CG2 ILE A 71 11.557 -26.709 10.460 1.00 68.71 C ANISOU 265 CG2 ILE A 71 6340 12544 7222 625 -595 -1628 C ATOM 266 CD1 ILE A 71 8.864 -24.803 10.696 1.00 63.48 C ANISOU 266 CD1 ILE A 71 5665 12007 6448 322 -556 -1361 C ATOM 267 N ALA A 72 13.910 -24.588 8.617 1.00 64.96 N ANISOU 267 N ALA A 72 5464 12765 6454 740 -445 -1544 N ATOM 268 CA ALA A 72 14.932 -25.026 7.668 1.00 66.39 C ANISOU 268 CA ALA A 72 5513 13179 6535 869 -417 -1695 C ATOM 269 C ALA A 72 16.339 -24.594 8.105 1.00 70.87 C ANISOU 269 C ALA A 72 5976 13854 7096 931 -399 -1621 C ATOM 270 O ALA A 72 17.276 -25.388 7.996 1.00 72.11 O ANISOU 270 O ALA A 72 6081 14062 7255 1094 -411 -1774 O ATOM 271 CB ALA A 72 14.620 -24.484 6.280 1.00 67.69 C ANISOU 271 CB ALA A 72 5550 13651 6517 811 -365 -1701 C ATOM 272 N THR A 73 16.476 -23.354 8.625 1.00 65.56 N ANISOU 272 N THR A 73 5277 13210 6422 808 -382 -1396 N ATOM 273 CA THR A 73 17.745 -22.796 9.088 1.00 65.02 C ANISOU 273 CA THR A 73 5108 13251 6345 820 -370 -1298 C ATOM 274 C THR A 73 18.318 -23.659 10.230 1.00 68.09 C ANISOU 274 C THR A 73 5572 13426 6872 946 -419 -1363 C ATOM 275 O THR A 73 19.518 -23.942 10.209 1.00 69.72 O ANISOU 275 O THR A 73 5664 13779 7046 1062 -413 -1424 O ATOM 276 CB THR A 73 17.566 -21.323 9.483 1.00 69.75 C ANISOU 276 CB THR A 73 5711 13849 6942 643 -366 -1055 C ATOM 277 OG1 THR A 73 17.100 -20.611 8.338 1.00 64.58 O ANISOU 277 OG1 THR A 73 4988 13395 6154 545 -334 -990 O ATOM 278 CG2 THR A 73 18.855 -20.684 9.967 1.00 71.15 C ANISOU 278 CG2 THR A 73 5785 14140 7109 617 -362 -946 C ATOM 279 N VAL A 74 17.477 -24.099 11.188 1.00 61.62 N ANISOU 279 N VAL A 74 4930 12292 6192 925 -470 -1346 N ATOM 280 CA VAL A 74 17.942 -24.949 12.287 1.00 61.59 C ANISOU 280 CA VAL A 74 5010 12076 6316 1034 -529 -1381 C ATOM 281 C VAL A 74 18.311 -26.336 11.722 1.00 71.57 C ANISOU 281 C VAL A 74 6285 13317 7593 1226 -563 -1613 C ATOM 282 O VAL A 74 19.412 -26.826 11.996 1.00 74.56 O ANISOU 282 O VAL A 74 6608 13729 7991 1386 -588 -1681 O ATOM 283 CB VAL A 74 16.943 -25.034 13.473 1.00 62.73 C ANISOU 283 CB VAL A 74 5327 11924 6583 940 -577 -1279 C ATOM 284 CG1 VAL A 74 17.433 -25.994 14.554 1.00 62.83 C ANISOU 284 CG1 VAL A 74 5430 11726 6716 1050 -647 -1301 C ATOM 285 CG2 VAL A 74 16.690 -23.658 14.073 1.00 60.54 C ANISOU 285 CG2 VAL A 74 5033 11677 6293 792 -556 -1086 C ATOM 286 N TYR A 75 17.435 -26.915 10.882 1.00 69.62 N ANISOU 286 N TYR A 75 6093 13036 7324 1220 -568 -1745 N ATOM 287 CA TYR A 75 17.606 -28.235 10.267 1.00 72.28 C ANISOU 287 CA TYR A 75 6465 13319 7679 1394 -616 -1995 C ATOM 288 C TYR A 75 18.872 -28.317 9.400 1.00 76.88 C ANISOU 288 C TYR A 75 6850 14224 8136 1572 -580 -2141 C ATOM 289 O TYR A 75 19.630 -29.276 9.535 1.00 77.42 O ANISOU 289 O TYR A 75 6928 14229 8258 1783 -639 -2297 O ATOM 290 CB TYR A 75 16.357 -28.609 9.426 1.00 74.75 C ANISOU 290 CB TYR A 75 6850 13586 7963 1311 -621 -2101 C ATOM 291 CG TYR A 75 16.430 -29.982 8.786 1.00 81.10 C ANISOU 291 CG TYR A 75 7715 14300 8799 1478 -688 -2381 C ATOM 292 CD1 TYR A 75 15.868 -31.093 9.407 1.00 84.03 C ANISOU 292 CD1 TYR A 75 8299 14294 9335 1491 -796 -2444 C ATOM 293 CD2 TYR A 75 17.063 -30.170 7.557 1.00 84.55 C ANISOU 293 CD2 TYR A 75 7998 15033 9095 1620 -654 -2587 C ATOM 294 CE1 TYR A 75 15.942 -32.363 8.828 1.00 88.51 C ANISOU 294 CE1 TYR A 75 8947 14733 9949 1648 -881 -2712 C ATOM 295 CE2 TYR A 75 17.162 -31.437 6.978 1.00 88.30 C ANISOU 295 CE2 TYR A 75 8531 15418 9601 1800 -730 -2879 C ATOM 296 CZ TYR A 75 16.590 -32.529 7.610 1.00 98.29 C ANISOU 296 CZ TYR A 75 10032 16259 11053 1815 -849 -2945 C ATOM 297 OH TYR A 75 16.681 -33.775 7.030 1.00102.50 O ANISOU 297 OH TYR A 75 10646 16665 11633 1992 -944 -3244 O ATOM 298 N ARG A 76 19.068 -27.339 8.494 1.00 73.46 N ANISOU 298 N ARG A 76 6237 14146 7530 1490 -492 -2089 N ATOM 299 CA ARG A 76 20.177 -27.295 7.540 1.00 74.92 C ANISOU 299 CA ARG A 76 6196 14722 7548 1619 -443 -2211 C ATOM 300 C ARG A 76 21.532 -26.967 8.181 1.00 79.88 C ANISOU 300 C ARG A 76 6697 15486 8167 1696 -435 -2134 C ATOM 301 O ARG A 76 22.530 -27.557 7.762 1.00 82.17 O ANISOU 301 O ARG A 76 6851 15986 8386 1904 -439 -2314 O ATOM 302 CB ARG A 76 19.887 -26.283 6.421 1.00 73.82 C ANISOU 302 CB ARG A 76 5909 14924 7216 1463 -357 -2124 C ATOM 303 N THR A 77 21.584 -26.027 9.156 1.00 74.53 N ANISOU 303 N THR A 77 6050 14717 7551 1538 -428 -1885 N ATOM 304 CA THR A 77 22.832 -25.585 9.801 1.00 74.59 C ANISOU 304 CA THR A 77 5929 14870 7542 1569 -422 -1791 C ATOM 305 C THR A 77 23.206 -26.503 10.983 1.00 79.65 C ANISOU 305 C THR A 77 6688 15227 8347 1736 -507 -1842 C ATOM 306 O THR A 77 22.525 -26.513 12.015 1.00 78.09 O ANISOU 306 O THR A 77 6672 14705 8293 1650 -553 -1723 O ATOM 307 CB THR A 77 22.739 -24.105 10.238 1.00 80.55 C ANISOU 307 CB THR A 77 6660 15666 8278 1314 -386 -1514 C ATOM 308 OG1 THR A 77 21.925 -23.373 9.323 1.00 82.44 O ANISOU 308 OG1 THR A 77 6885 16016 8421 1149 -339 -1440 O ATOM 309 CG2 THR A 77 24.082 -23.440 10.327 1.00 79.58 C ANISOU 309 CG2 THR A 77 6333 15844 8059 1292 -358 -1427 C ATOM 310 N ARG A 78 24.319 -27.252 10.818 1.00 79.05 N ANISOU 310 N ARG A 78 6493 15308 8234 1980 -531 -2015 N ATOM 311 CA ARG A 78 24.896 -28.186 11.797 1.00 79.83 C ANISOU 311 CA ARG A 78 6672 15197 8465 2189 -623 -2081 C ATOM 312 C ARG A 78 25.335 -27.446 13.067 1.00 82.38 C ANISOU 312 C ARG A 78 6984 15478 8839 2078 -630 -1854 C ATOM 313 O ARG A 78 25.250 -28.006 14.164 1.00 81.63 O ANISOU 313 O ARG A 78 7038 15087 8889 2145 -711 -1813 O ATOM 314 CB ARG A 78 26.084 -28.947 11.184 1.00 82.12 C ANISOU 314 CB ARG A 78 6783 15756 8662 2488 -639 -2322 C ATOM 315 CG ARG A 78 26.410 -30.254 11.901 1.00 94.16 C ANISOU 315 CG ARG A 78 8448 16985 10344 2766 -766 -2460 C ATOM 316 N LYS A 79 25.788 -26.180 12.901 1.00 77.91 N ANISOU 316 N LYS A 79 6244 15208 8149 1896 -552 -1702 N ATOM 317 CA LYS A 79 26.208 -25.245 13.954 1.00 75.94 C ANISOU 317 CA LYS A 79 5964 14967 7924 1746 -553 -1490 C ATOM 318 C LYS A 79 25.035 -24.950 14.913 1.00 76.92 C ANISOU 318 C LYS A 79 6321 14711 8192 1584 -587 -1340 C ATOM 319 O LYS A 79 25.263 -24.670 16.095 1.00 75.68 O ANISOU 319 O LYS A 79 6209 14439 8108 1544 -627 -1222 O ATOM 320 CB LYS A 79 26.695 -23.943 13.288 1.00 78.13 C ANISOU 320 CB LYS A 79 6037 15611 8037 1544 -471 -1368 C ATOM 321 CG LYS A 79 27.424 -22.951 14.196 1.00 91.80 C ANISOU 321 CG LYS A 79 7688 17427 9765 1395 -478 -1183 C ATOM 322 CD LYS A 79 27.052 -21.487 13.882 1.00102.26 C ANISOU 322 CD LYS A 79 8996 18824 11032 1088 -437 -984 C ATOM 323 CE LYS A 79 27.651 -20.930 12.604 1.00115.46 C ANISOU 323 CE LYS A 79 10440 20923 12508 993 -369 -964 C ATOM 324 NZ LYS A 79 27.053 -19.616 12.240 1.00123.52 N ANISOU 324 NZ LYS A 79 11500 21933 13498 702 -352 -760 N ATOM 325 N LEU A 80 23.782 -25.029 14.393 1.00 71.62 N ANISOU 325 N LEU A 80 5785 13881 7547 1496 -574 -1357 N ATOM 326 CA LEU A 80 22.550 -24.763 15.144 1.00 69.11 C ANISOU 326 CA LEU A 80 5664 13258 7336 1345 -599 -1235 C ATOM 327 C LEU A 80 21.897 -26.037 15.751 1.00 71.43 C ANISOU 327 C LEU A 80 6157 13215 7769 1454 -677 -1310 C ATOM 328 O LEU A 80 20.811 -25.942 16.321 1.00 68.91 O ANISOU 328 O LEU A 80 5988 12673 7521 1328 -697 -1221 O ATOM 329 CB LEU A 80 21.530 -24.026 14.249 1.00 68.29 C ANISOU 329 CB LEU A 80 5577 13202 7168 1175 -544 -1193 C ATOM 330 CG LEU A 80 21.898 -22.603 13.791 1.00 72.43 C ANISOU 330 CG LEU A 80 5959 13983 7579 1007 -489 -1056 C ATOM 331 CD1 LEU A 80 20.815 -22.028 12.910 1.00 71.33 C ANISOU 331 CD1 LEU A 80 5857 13860 7385 873 -454 -1017 C ATOM 332 CD2 LEU A 80 22.168 -21.667 14.982 1.00 73.94 C ANISOU 332 CD2 LEU A 80 6170 14099 7826 885 -515 -884 C ATOM 333 N HIS A 81 22.569 -27.206 15.678 1.00 69.13 N ANISOU 333 N HIS A 81 5866 12888 7512 1684 -732 -1464 N ATOM 334 CA HIS A 81 22.033 -28.445 16.247 1.00 68.67 C ANISOU 334 CA HIS A 81 6012 12483 7595 1778 -828 -1517 C ATOM 335 C HIS A 81 22.340 -28.505 17.745 1.00 71.91 C ANISOU 335 C HIS A 81 6489 12739 8094 1782 -892 -1368 C ATOM 336 O HIS A 81 23.273 -29.185 18.192 1.00 72.42 O ANISOU 336 O HIS A 81 6532 12789 8196 1978 -957 -1413 O ATOM 337 CB HIS A 81 22.547 -29.681 15.488 1.00 71.53 C ANISOU 337 CB HIS A 81 6373 12833 7970 2037 -883 -1758 C ATOM 338 CG HIS A 81 22.035 -29.769 14.083 1.00 75.30 C ANISOU 338 CG HIS A 81 6812 13434 8364 2027 -834 -1921 C ATOM 339 ND1 HIS A 81 22.645 -30.580 13.145 1.00 79.29 N ANISOU 339 ND1 HIS A 81 7247 14053 8825 2262 -858 -2171 N ATOM 340 CD2 HIS A 81 21.005 -29.114 13.491 1.00 75.14 C ANISOU 340 CD2 HIS A 81 6804 13460 8285 1823 -767 -1871 C ATOM 341 CE1 HIS A 81 21.971 -30.397 12.022 1.00 78.28 C ANISOU 341 CE1 HIS A 81 7088 14048 8609 2179 -801 -2262 C ATOM 342 NE2 HIS A 81 20.976 -29.523 12.184 1.00 76.29 N ANISOU 342 NE2 HIS A 81 6883 13757 8345 1916 -746 -2079 N ATOM 343 N THR A 82 21.575 -27.706 18.511 1.00 67.00 N ANISOU 343 N THR A 82 5931 12037 7489 1569 -872 -1191 N ATOM 344 CA THR A 82 21.662 -27.592 19.975 1.00 66.18 C ANISOU 344 CA THR A 82 5887 11815 7445 1526 -922 -1033 C ATOM 345 C THR A 82 20.259 -27.578 20.556 1.00 69.36 C ANISOU 345 C THR A 82 6453 12003 7900 1348 -937 -930 C ATOM 346 O THR A 82 19.364 -27.016 19.915 1.00 68.40 O ANISOU 346 O THR A 82 6335 11920 7736 1212 -879 -935 O ATOM 347 CB THR A 82 22.446 -26.335 20.448 1.00 69.86 C ANISOU 347 CB THR A 82 6194 12512 7836 1448 -875 -926 C ATOM 348 OG1 THR A 82 21.637 -25.157 20.340 1.00 68.63 O ANISOU 348 OG1 THR A 82 6036 12402 7637 1234 -814 -840 O ATOM 349 CG2 THR A 82 23.780 -26.157 19.764 1.00 65.52 C ANISOU 349 CG2 THR A 82 5444 12248 7201 1573 -843 -1012 C ATOM 350 N PRO A 83 20.053 -28.105 21.789 1.00 66.11 N ANISOU 350 N PRO A 83 6156 11402 7560 1338 -1013 -822 N ATOM 351 CA PRO A 83 18.702 -28.093 22.386 1.00 64.64 C ANISOU 351 CA PRO A 83 6099 11064 7397 1155 -1024 -717 C ATOM 352 C PRO A 83 18.030 -26.719 22.412 1.00 64.61 C ANISOU 352 C PRO A 83 6027 11205 7316 978 -944 -652 C ATOM 353 O PRO A 83 16.831 -26.670 22.183 1.00 64.15 O ANISOU 353 O PRO A 83 6034 11090 7249 854 -926 -647 O ATOM 354 CB PRO A 83 18.927 -28.613 23.811 1.00 67.23 C ANISOU 354 CB PRO A 83 6501 11267 7775 1173 -1109 -583 C ATOM 355 CG PRO A 83 20.417 -28.609 24.012 1.00 72.87 C ANISOU 355 CG PRO A 83 7106 12095 8485 1357 -1132 -608 C ATOM 356 CD PRO A 83 21.006 -28.812 22.664 1.00 69.02 C ANISOU 356 CD PRO A 83 6541 11703 7982 1497 -1099 -786 C ATOM 357 N ALA A 84 18.783 -25.623 22.647 1.00 59.29 N ANISOU 357 N ALA A 84 5226 10714 6589 968 -905 -612 N ATOM 358 CA ALA A 84 18.236 -24.258 22.688 1.00 57.45 C ANISOU 358 CA ALA A 84 4943 10590 6297 820 -852 -557 C ATOM 359 C ALA A 84 17.627 -23.835 21.335 1.00 62.85 C ANISOU 359 C ALA A 84 5603 11339 6937 768 -792 -629 C ATOM 360 O ALA A 84 16.526 -23.278 21.328 1.00 62.23 O ANISOU 360 O ALA A 84 5565 11243 6838 653 -773 -597 O ATOM 361 CB ALA A 84 19.308 -23.267 23.111 1.00 57.75 C ANISOU 361 CB ALA A 84 4858 10786 6298 821 -843 -513 C ATOM 362 N ASN A 85 18.317 -24.131 20.198 1.00 59.88 N ANISOU 362 N ASN A 85 5154 11063 6536 861 -765 -729 N ATOM 363 CA ASN A 85 17.829 -23.809 18.856 1.00 59.00 C ANISOU 363 CA ASN A 85 5006 11047 6365 821 -710 -796 C ATOM 364 C ASN A 85 16.697 -24.747 18.472 1.00 63.62 C ANISOU 364 C ASN A 85 5709 11483 6981 808 -727 -867 C ATOM 365 O ASN A 85 15.885 -24.402 17.603 1.00 63.65 O ANISOU 365 O ASN A 85 5707 11543 6935 736 -688 -898 O ATOM 366 CB ASN A 85 18.950 -23.876 17.817 1.00 60.05 C ANISOU 366 CB ASN A 85 5004 11375 6436 926 -678 -888 C ATOM 367 CG ASN A 85 20.059 -22.861 17.994 1.00 82.93 C ANISOU 367 CG ASN A 85 7759 14471 9279 897 -655 -813 C ATOM 368 OD1 ASN A 85 19.836 -21.644 18.025 1.00 81.87 O ANISOU 368 OD1 ASN A 85 7598 14399 9110 756 -634 -714 O ATOM 369 ND2 ASN A 85 21.295 -23.336 18.056 1.00 70.09 N ANISOU 369 ND2 ASN A 85 6035 12956 7641 1030 -667 -864 N ATOM 370 N TYR A 86 16.631 -25.935 19.117 1.00 60.38 N ANISOU 370 N TYR A 86 5409 10880 6653 868 -793 -883 N ATOM 371 CA TYR A 86 15.569 -26.903 18.848 1.00 60.80 C ANISOU 371 CA TYR A 86 5589 10766 6747 826 -827 -940 C ATOM 372 C TYR A 86 14.248 -26.359 19.363 1.00 63.83 C ANISOU 372 C TYR A 86 6018 11127 7108 649 -813 -839 C ATOM 373 O TYR A 86 13.213 -26.565 18.727 1.00 63.79 O ANISOU 373 O TYR A 86 6052 11106 7081 569 -803 -888 O ATOM 374 CB TYR A 86 15.877 -28.278 19.464 1.00 63.34 C ANISOU 374 CB TYR A 86 6032 10862 7171 919 -922 -958 C ATOM 375 CG TYR A 86 17.033 -29.035 18.839 1.00 66.48 C ANISOU 375 CG TYR A 86 6401 11262 7598 1133 -954 -1104 C ATOM 376 CD1 TYR A 86 17.715 -30.017 19.550 1.00 70.16 C ANISOU 376 CD1 TYR A 86 6948 11555 8155 1271 -1050 -1099 C ATOM 377 CD2 TYR A 86 17.429 -28.790 17.524 1.00 67.00 C ANISOU 377 CD2 TYR A 86 6351 11518 7587 1209 -895 -1249 C ATOM 378 CE1 TYR A 86 18.785 -30.708 18.988 1.00 72.20 C ANISOU 378 CE1 TYR A 86 7169 11828 8435 1502 -1088 -1254 C ATOM 379 CE2 TYR A 86 18.497 -29.479 16.951 1.00 69.34 C ANISOU 379 CE2 TYR A 86 6595 11862 7889 1426 -923 -1405 C ATOM 380 CZ TYR A 86 19.166 -30.441 17.686 1.00 78.29 C ANISOU 380 CZ TYR A 86 7810 12815 9121 1583 -1022 -1418 C ATOM 381 OH TYR A 86 20.211 -31.135 17.137 1.00 84.46 O ANISOU 381 OH TYR A 86 8535 13649 9906 1830 -1060 -1592 O ATOM 382 N LEU A 87 14.301 -25.616 20.488 1.00 59.07 N ANISOU 382 N LEU A 87 5394 10554 6496 596 -814 -713 N ATOM 383 CA LEU A 87 13.145 -24.972 21.107 1.00 57.81 C ANISOU 383 CA LEU A 87 5251 10417 6298 457 -804 -630 C ATOM 384 C LEU A 87 12.647 -23.849 20.212 1.00 61.81 C ANISOU 384 C LEU A 87 5684 11068 6732 412 -745 -657 C ATOM 385 O LEU A 87 11.437 -23.687 20.086 1.00 62.29 O ANISOU 385 O LEU A 87 5765 11148 6755 322 -735 -652 O ATOM 386 CB LEU A 87 13.475 -24.454 22.516 1.00 57.38 C ANISOU 386 CB LEU A 87 5179 10380 6242 442 -826 -519 C ATOM 387 CG LEU A 87 13.997 -25.471 23.543 1.00 62.75 C ANISOU 387 CG LEU A 87 5926 10936 6981 486 -894 -457 C ATOM 388 CD1 LEU A 87 14.495 -24.773 24.775 1.00 62.73 C ANISOU 388 CD1 LEU A 87 5873 11008 6954 483 -907 -365 C ATOM 389 CD2 LEU A 87 12.944 -26.505 23.920 1.00 64.64 C ANISOU 389 CD2 LEU A 87 6279 11039 7242 388 -940 -414 C ATOM 390 N ILE A 88 13.568 -23.109 19.547 1.00 58.56 N ANISOU 390 N ILE A 88 5184 10770 6295 470 -711 -678 N ATOM 391 CA ILE A 88 13.231 -22.072 18.552 1.00 58.17 C ANISOU 391 CA ILE A 88 5072 10854 6178 429 -668 -685 C ATOM 392 C ILE A 88 12.510 -22.747 17.368 1.00 62.08 C ANISOU 392 C ILE A 88 5583 11364 6640 422 -648 -782 C ATOM 393 O ILE A 88 11.443 -22.285 16.935 1.00 60.10 O ANISOU 393 O ILE A 88 5332 11165 6339 354 -633 -777 O ATOM 394 CB ILE A 88 14.473 -21.264 18.042 1.00 61.52 C ANISOU 394 CB ILE A 88 5393 11409 6573 466 -644 -666 C ATOM 395 CG1 ILE A 88 15.472 -20.833 19.159 1.00 62.12 C ANISOU 395 CG1 ILE A 88 5442 11475 6685 481 -672 -595 C ATOM 396 CG2 ILE A 88 14.070 -20.101 17.114 1.00 61.20 C ANISOU 396 CG2 ILE A 88 5304 11487 6462 401 -617 -630 C ATOM 397 CD1 ILE A 88 14.922 -19.924 20.275 1.00 73.44 C ANISOU 397 CD1 ILE A 88 6912 12860 8130 410 -703 -516 C ATOM 398 N ALA A 89 13.107 -23.856 16.869 1.00 60.19 N ANISOU 398 N ALA A 89 5356 11086 6427 507 -656 -884 N ATOM 399 CA ALA A 89 12.593 -24.640 15.743 1.00 61.14 C ANISOU 399 CA ALA A 89 5494 11214 6521 517 -649 -1012 C ATOM 400 C ALA A 89 11.212 -25.226 16.040 1.00 64.31 C ANISOU 400 C ALA A 89 5994 11499 6943 411 -680 -1015 C ATOM 401 O ALA A 89 10.384 -25.209 15.137 1.00 64.09 O ANISOU 401 O ALA A 89 5951 11545 6854 359 -660 -1075 O ATOM 402 CB ALA A 89 13.571 -25.747 15.372 1.00 63.59 C ANISOU 402 CB ALA A 89 5812 11477 6872 655 -675 -1138 C ATOM 403 N SER A 90 10.937 -25.699 17.291 1.00 60.90 N ANISOU 403 N SER A 90 5647 10914 6578 365 -728 -939 N ATOM 404 CA SER A 90 9.603 -26.234 17.633 1.00 60.90 C ANISOU 404 CA SER A 90 5722 10838 6578 231 -757 -919 C ATOM 405 C SER A 90 8.580 -25.107 17.803 1.00 62.90 C ANISOU 405 C SER A 90 5912 11240 6747 141 -720 -848 C ATOM 406 O SER A 90 7.411 -25.314 17.474 1.00 62.69 O ANISOU 406 O SER A 90 5891 11254 6674 44 -720 -875 O ATOM 407 CB SER A 90 9.635 -27.116 18.871 1.00 65.17 C ANISOU 407 CB SER A 90 6365 11200 7198 194 -824 -840 C ATOM 408 OG SER A 90 10.123 -26.378 19.974 1.00 81.05 O ANISOU 408 OG SER A 90 8336 13255 9205 214 -817 -724 O ATOM 409 N LEU A 91 9.021 -23.906 18.260 1.00 58.17 N ANISOU 409 N LEU A 91 5249 10726 6127 181 -697 -772 N ATOM 410 CA LEU A 91 8.151 -22.726 18.354 1.00 57.24 C ANISOU 410 CA LEU A 91 5076 10735 5938 139 -677 -726 C ATOM 411 C LEU A 91 7.722 -22.329 16.955 1.00 62.33 C ANISOU 411 C LEU A 91 5671 11495 6516 143 -645 -786 C ATOM 412 O LEU A 91 6.565 -21.967 16.755 1.00 63.65 O ANISOU 412 O LEU A 91 5814 11752 6619 91 -642 -786 O ATOM 413 CB LEU A 91 8.839 -21.538 19.066 1.00 56.40 C ANISOU 413 CB LEU A 91 4933 10658 5840 188 -679 -652 C ATOM 414 CG LEU A 91 8.121 -20.155 19.001 1.00 59.68 C ANISOU 414 CG LEU A 91 5302 11177 6195 184 -678 -623 C ATOM 415 CD1 LEU A 91 6.768 -20.176 19.715 1.00 59.51 C ANISOU 415 CD1 LEU A 91 5280 11208 6125 128 -693 -619 C ATOM 416 CD2 LEU A 91 9.000 -19.042 19.558 1.00 60.25 C ANISOU 416 CD2 LEU A 91 5357 11239 6296 228 -697 -568 C ATOM 417 N ALA A 92 8.654 -22.430 15.988 1.00 58.73 N ANISOU 417 N ALA A 92 5188 11066 6061 209 -624 -838 N ATOM 418 CA ALA A 92 8.442 -22.122 14.577 1.00 58.43 C ANISOU 418 CA ALA A 92 5091 11167 5945 216 -593 -891 C ATOM 419 C ALA A 92 7.524 -23.147 13.946 1.00 62.86 C ANISOU 419 C ALA A 92 5679 11726 6477 164 -598 -997 C ATOM 420 O ALA A 92 6.725 -22.773 13.100 1.00 63.22 O ANISOU 420 O ALA A 92 5678 11905 6439 134 -583 -1019 O ATOM 421 CB ALA A 92 9.769 -22.061 13.839 1.00 59.70 C ANISOU 421 CB ALA A 92 5196 11391 6096 295 -568 -919 C ATOM 422 N VAL A 93 7.585 -24.420 14.394 1.00 60.32 N ANISOU 422 N VAL A 93 5440 11249 6228 145 -633 -1055 N ATOM 423 CA VAL A 93 6.702 -25.499 13.927 1.00 61.35 C ANISOU 423 CA VAL A 93 5621 11337 6352 66 -659 -1157 C ATOM 424 C VAL A 93 5.259 -25.235 14.412 1.00 66.21 C ANISOU 424 C VAL A 93 6227 12014 6916 -65 -666 -1095 C ATOM 425 O VAL A 93 4.324 -25.401 13.627 1.00 66.62 O ANISOU 425 O VAL A 93 6249 12166 6896 -132 -663 -1162 O ATOM 426 CB VAL A 93 7.216 -26.899 14.362 1.00 66.28 C ANISOU 426 CB VAL A 93 6360 11736 7088 79 -718 -1217 C ATOM 427 CG1 VAL A 93 6.115 -27.960 14.307 1.00 67.15 C ANISOU 427 CG1 VAL A 93 6553 11750 7212 -61 -770 -1275 C ATOM 428 CG2 VAL A 93 8.406 -27.325 13.513 1.00 66.99 C ANISOU 428 CG2 VAL A 93 6436 11818 7198 227 -714 -1344 C ATOM 429 N THR A 94 5.077 -24.817 15.688 1.00 63.46 N ANISOU 429 N THR A 94 5887 11637 6587 -95 -676 -978 N ATOM 430 CA THR A 94 3.733 -24.549 16.221 1.00 64.04 C ANISOU 430 CA THR A 94 5926 11815 6592 -204 -682 -928 C ATOM 431 C THR A 94 3.094 -23.403 15.449 1.00 67.90 C ANISOU 431 C THR A 94 6316 12505 6979 -163 -651 -936 C ATOM 432 O THR A 94 1.956 -23.542 15.004 1.00 67.43 O ANISOU 432 O THR A 94 6212 12569 6839 -241 -652 -975 O ATOM 433 CB THR A 94 3.725 -24.269 17.741 1.00 72.88 C ANISOU 433 CB THR A 94 7055 12905 7732 -225 -699 -815 C ATOM 434 OG1 THR A 94 4.492 -23.104 18.036 1.00 73.22 O ANISOU 434 OG1 THR A 94 7060 12979 7783 -107 -681 -768 O ATOM 435 CG2 THR A 94 4.230 -25.425 18.546 1.00 72.10 C ANISOU 435 CG2 THR A 94 7056 12614 7723 -273 -742 -779 C ATOM 436 N ASP A 95 3.863 -22.306 15.235 1.00 63.88 N ANISOU 436 N ASP A 95 5774 12025 6473 -48 -632 -895 N ATOM 437 CA ASP A 95 3.424 -21.103 14.533 1.00 63.65 C ANISOU 437 CA ASP A 95 5673 12149 6363 6 -621 -874 C ATOM 438 C ASP A 95 3.094 -21.410 13.047 1.00 68.33 C ANISOU 438 C ASP A 95 6226 12854 6882 -8 -603 -955 C ATOM 439 O ASP A 95 2.245 -20.735 12.445 1.00 67.81 O ANISOU 439 O ASP A 95 6097 12943 6725 1 -606 -947 O ATOM 440 CB ASP A 95 4.490 -19.996 14.665 1.00 65.32 C ANISOU 440 CB ASP A 95 5883 12322 6614 99 -622 -797 C ATOM 441 CG ASP A 95 4.707 -19.405 16.070 1.00 82.89 C ANISOU 441 CG ASP A 95 8132 14471 8891 124 -648 -730 C ATOM 442 OD1 ASP A 95 3.765 -19.465 16.900 1.00 85.17 O ANISOU 442 OD1 ASP A 95 8411 14798 9152 89 -664 -731 O ATOM 443 OD2 ASP A 95 5.794 -18.819 16.312 1.00 88.61 O ANISOU 443 OD2 ASP A 95 8872 15128 9670 173 -654 -679 O ATOM 444 N LEU A 96 3.734 -22.459 12.480 1.00 65.00 N ANISOU 444 N LEU A 96 5840 12363 6495 -20 -594 -1043 N ATOM 445 CA LEU A 96 3.496 -22.906 11.109 1.00 65.42 C ANISOU 445 CA LEU A 96 5855 12529 6474 -31 -580 -1152 C ATOM 446 C LEU A 96 2.157 -23.633 11.022 1.00 69.68 C ANISOU 446 C LEU A 96 6392 13116 6965 -151 -602 -1222 C ATOM 447 O LEU A 96 1.430 -23.440 10.041 1.00 70.38 O ANISOU 447 O LEU A 96 6412 13382 6948 -169 -595 -1270 O ATOM 448 CB LEU A 96 4.642 -23.806 10.612 1.00 66.10 C ANISOU 448 CB LEU A 96 5976 12528 6611 19 -574 -1254 C ATOM 449 CG LEU A 96 4.538 -24.338 9.177 1.00 71.52 C ANISOU 449 CG LEU A 96 6617 13346 7212 25 -562 -1401 C ATOM 450 CD1 LEU A 96 4.895 -23.276 8.174 1.00 70.99 C ANISOU 450 CD1 LEU A 96 6445 13495 7035 89 -523 -1350 C ATOM 451 CD2 LEU A 96 5.441 -25.523 8.992 1.00 75.33 C ANISOU 451 CD2 LEU A 96 7160 13698 7766 77 -580 -1545 C ATOM 452 N LEU A 97 1.828 -24.461 12.048 1.00 65.11 N ANISOU 452 N LEU A 97 5884 12398 6456 -245 -633 -1215 N ATOM 453 CA LEU A 97 0.558 -25.201 12.123 1.00 65.26 C ANISOU 453 CA LEU A 97 5901 12465 6430 -401 -661 -1259 C ATOM 454 C LEU A 97 -0.617 -24.244 12.277 1.00 67.97 C ANISOU 454 C LEU A 97 6135 13031 6660 -418 -650 -1197 C ATOM 455 O LEU A 97 -1.656 -24.474 11.671 1.00 68.64 O ANISOU 455 O LEU A 97 6157 13272 6650 -504 -658 -1256 O ATOM 456 CB LEU A 97 0.558 -26.218 13.266 1.00 65.84 C ANISOU 456 CB LEU A 97 6076 12342 6599 -515 -704 -1227 C ATOM 457 CG LEU A 97 1.555 -27.363 13.153 1.00 70.83 C ANISOU 457 CG LEU A 97 6834 12727 7353 -495 -741 -1303 C ATOM 458 CD1 LEU A 97 1.802 -27.981 14.506 1.00 71.13 C ANISOU 458 CD1 LEU A 97 6971 12565 7492 -559 -786 -1204 C ATOM 459 CD2 LEU A 97 1.100 -28.408 12.154 1.00 72.78 C ANISOU 459 CD2 LEU A 97 7117 12946 7588 -584 -779 -1461 C ATOM 460 N VAL A 98 -0.434 -23.147 13.048 1.00 63.17 N ANISOU 460 N VAL A 98 5500 12446 6057 -323 -640 -1090 N ATOM 461 CA VAL A 98 -1.422 -22.073 13.243 1.00 62.95 C ANISOU 461 CA VAL A 98 5371 12616 5929 -280 -643 -1043 C ATOM 462 C VAL A 98 -1.717 -21.445 11.865 1.00 67.90 C ANISOU 462 C VAL A 98 5928 13407 6464 -209 -636 -1076 C ATOM 463 O VAL A 98 -2.874 -21.236 11.513 1.00 69.34 O ANISOU 463 O VAL A 98 6020 13791 6535 -232 -647 -1099 O ATOM 464 CB VAL A 98 -0.940 -21.000 14.277 1.00 66.05 C ANISOU 464 CB VAL A 98 5773 12956 6366 -166 -650 -949 C ATOM 465 CG1 VAL A 98 -1.999 -19.929 14.511 1.00 66.17 C ANISOU 465 CG1 VAL A 98 5692 13167 6283 -95 -670 -931 C ATOM 466 CG2 VAL A 98 -0.543 -21.631 15.609 1.00 65.62 C ANISOU 466 CG2 VAL A 98 5782 12760 6392 -231 -657 -910 C ATOM 467 N SER A 99 -0.665 -21.212 11.074 1.00 63.64 N ANISOU 467 N SER A 99 5420 12805 5957 -132 -619 -1075 N ATOM 468 CA SER A 99 -0.751 -20.619 9.749 1.00 63.35 C ANISOU 468 CA SER A 99 5319 12926 5825 -71 -614 -1080 C ATOM 469 C SER A 99 -1.343 -21.578 8.712 1.00 68.05 C ANISOU 469 C SER A 99 5873 13646 6337 -162 -607 -1207 C ATOM 470 O SER A 99 -1.758 -21.115 7.652 1.00 68.05 O ANISOU 470 O SER A 99 5796 13836 6225 -127 -608 -1213 O ATOM 471 CB SER A 99 0.627 -20.129 9.300 1.00 65.01 C ANISOU 471 CB SER A 99 5561 13060 6080 13 -596 -1025 C ATOM 472 OG SER A 99 1.457 -21.158 8.786 1.00 68.04 O ANISOU 472 OG SER A 99 5978 13376 6500 -16 -571 -1121 O ATOM 473 N ILE A 100 -1.365 -22.895 8.986 1.00 65.41 N ANISOU 473 N ILE A 100 5595 13200 6056 -280 -612 -1306 N ATOM 474 CA ILE A 100 -1.898 -23.859 8.011 1.00 66.87 C ANISOU 474 CA ILE A 100 5758 13476 6175 -378 -621 -1451 C ATOM 475 C ILE A 100 -3.276 -24.389 8.463 1.00 71.06 C ANISOU 475 C ILE A 100 6253 14092 6656 -537 -650 -1479 C ATOM 476 O ILE A 100 -4.202 -24.390 7.657 1.00 71.04 O ANISOU 476 O ILE A 100 6156 14306 6528 -586 -658 -1540 O ATOM 477 CB ILE A 100 -0.881 -25.007 7.718 1.00 70.49 C ANISOU 477 CB ILE A 100 6314 13741 6727 -390 -625 -1572 C ATOM 478 CG1 ILE A 100 0.306 -24.471 6.886 1.00 70.07 C ANISOU 478 CG1 ILE A 100 6237 13730 6657 -244 -590 -1573 C ATOM 479 CG2 ILE A 100 -1.554 -26.204 7.003 1.00 72.96 C ANISOU 479 CG2 ILE A 100 6638 14080 7003 -523 -660 -1746 C ATOM 480 CD1 ILE A 100 1.531 -25.317 6.917 1.00 75.43 C ANISOU 480 CD1 ILE A 100 7000 14220 7441 -195 -592 -1661 C ATOM 481 N LEU A 101 -3.397 -24.839 9.729 1.00 67.79 N ANISOU 481 N LEU A 101 5900 13533 6324 -626 -667 -1427 N ATOM 482 CA LEU A 101 -4.622 -25.408 10.291 1.00 68.95 C ANISOU 482 CA LEU A 101 6008 13772 6420 -809 -695 -1431 C ATOM 483 C LEU A 101 -5.639 -24.386 10.771 1.00 73.22 C ANISOU 483 C LEU A 101 6413 14561 6846 -771 -687 -1349 C ATOM 484 O LEU A 101 -6.819 -24.737 10.860 1.00 73.69 O ANISOU 484 O LEU A 101 6383 14810 6805 -914 -704 -1374 O ATOM 485 CB LEU A 101 -4.302 -26.316 11.502 1.00 69.33 C ANISOU 485 CB LEU A 101 6174 13579 6590 -933 -723 -1384 C ATOM 486 CG LEU A 101 -3.778 -27.743 11.286 1.00 75.43 C ANISOU 486 CG LEU A 101 7091 14093 7474 -1042 -770 -1479 C ATOM 487 CD1 LEU A 101 -4.342 -28.411 10.018 1.00 76.61 C ANISOU 487 CD1 LEU A 101 7217 14335 7557 -1137 -795 -1641 C ATOM 488 CD2 LEU A 101 -2.294 -27.782 11.326 1.00 77.95 C ANISOU 488 CD2 LEU A 101 7516 14181 7921 -881 -761 -1484 C ATOM 489 N VAL A 102 -5.199 -23.173 11.188 1.00 68.49 N ANISOU 489 N VAL A 102 5799 13961 6263 -587 -670 -1257 N ATOM 490 CA VAL A 102 -6.130 -22.227 11.809 1.00 67.74 C ANISOU 490 CA VAL A 102 5589 14077 6074 -521 -677 -1201 C ATOM 491 C VAL A 102 -6.373 -20.905 11.033 1.00 70.71 C ANISOU 491 C VAL A 102 5885 14614 6368 -326 -686 -1180 C ATOM 492 O VAL A 102 -7.544 -20.515 10.908 1.00 71.41 O ANISOU 492 O VAL A 102 5843 14963 6325 -307 -704 -1198 O ATOM 493 CB VAL A 102 -5.701 -21.911 13.256 1.00 70.18 C ANISOU 493 CB VAL A 102 5942 14265 6458 -482 -677 -1116 C ATOM 494 CG1 VAL A 102 -6.789 -21.140 13.981 1.00 70.29 C ANISOU 494 CG1 VAL A 102 5821 14530 6356 -429 -691 -1096 C ATOM 495 CG2 VAL A 102 -5.353 -23.184 14.020 1.00 70.25 C ANISOU 495 CG2 VAL A 102 6046 14092 6554 -664 -681 -1104 C ATOM 496 N MET A 103 -5.307 -20.196 10.588 1.00 63.81 N ANISOU 496 N MET A 103 5083 13597 5564 -185 -681 -1131 N ATOM 497 CA MET A 103 -5.460 -18.887 9.954 1.00 63.06 C ANISOU 497 CA MET A 103 4940 13611 5410 -10 -708 -1074 C ATOM 498 C MET A 103 -6.158 -18.880 8.569 1.00 72.50 C ANISOU 498 C MET A 103 6042 15036 6468 -11 -717 -1117 C ATOM 499 O MET A 103 -6.982 -17.979 8.380 1.00 73.66 O ANISOU 499 O MET A 103 6103 15361 6523 106 -757 -1084 O ATOM 500 CB MET A 103 -4.132 -18.146 9.851 1.00 63.68 C ANISOU 500 CB MET A 103 5117 13485 5592 100 -709 -988 C ATOM 501 CG MET A 103 -3.794 -17.329 11.085 1.00 65.67 C ANISOU 501 CG MET A 103 5417 13606 5927 199 -736 -919 C ATOM 502 SD MET A 103 -2.160 -16.524 11.007 1.00 67.59 S ANISOU 502 SD MET A 103 5777 13608 6298 282 -743 -814 S ATOM 503 CE MET A 103 -1.228 -17.693 11.771 1.00 63.37 C ANISOU 503 CE MET A 103 5314 12893 5869 167 -694 -853 C ATOM 504 N PRO A 104 -5.894 -19.779 7.579 1.00 71.17 N ANISOU 504 N PRO A 104 5880 14888 6273 -117 -691 -1196 N ATOM 505 CA PRO A 104 -6.572 -19.620 6.270 1.00 72.16 C ANISOU 505 CA PRO A 104 5901 15267 6249 -101 -705 -1231 C ATOM 506 C PRO A 104 -8.087 -19.786 6.352 1.00 78.07 C ANISOU 506 C PRO A 104 6516 16281 6867 -160 -729 -1289 C ATOM 507 O PRO A 104 -8.836 -18.970 5.818 1.00 79.25 O ANISOU 507 O PRO A 104 6562 16655 6896 -50 -763 -1256 O ATOM 508 CB PRO A 104 -5.930 -20.697 5.386 1.00 74.14 C ANISOU 508 CB PRO A 104 6191 15473 6506 -208 -674 -1338 C ATOM 509 CG PRO A 104 -5.305 -21.652 6.308 1.00 78.09 C ANISOU 509 CG PRO A 104 6802 15721 7149 -310 -655 -1385 C ATOM 510 CD PRO A 104 -4.958 -20.923 7.566 1.00 72.59 C ANISOU 510 CD PRO A 104 6157 14870 6551 -231 -659 -1268 C ATOM 511 N ILE A 105 -8.521 -20.818 7.068 1.00 74.97 N ANISOU 511 N ILE A 105 6122 15866 6496 -335 -717 -1362 N ATOM 512 CA ILE A 105 -9.907 -21.223 7.334 1.00 75.93 C ANISOU 512 CA ILE A 105 6111 16242 6497 -456 -734 -1420 C ATOM 513 C ILE A 105 -10.614 -20.178 8.273 1.00 78.70 C ANISOU 513 C ILE A 105 6370 16734 6798 -312 -758 -1348 C ATOM 514 O ILE A 105 -11.842 -20.168 8.358 1.00 78.69 O ANISOU 514 O ILE A 105 6213 17031 6656 -346 -776 -1386 O ATOM 515 CB ILE A 105 -9.819 -22.676 7.908 1.00 79.76 C ANISOU 515 CB ILE A 105 6669 16579 7057 -710 -723 -1487 C ATOM 516 CG1 ILE A 105 -11.097 -23.200 8.566 1.00 81.30 C ANISOU 516 CG1 ILE A 105 6744 16995 7151 -894 -739 -1513 C ATOM 517 CG2 ILE A 105 -8.552 -22.880 8.781 1.00 80.99 C ANISOU 517 CG2 ILE A 105 6994 16382 7399 -693 -704 -1429 C ATOM 518 CD1 ILE A 105 -11.099 -24.726 8.781 1.00 90.73 C ANISOU 518 CD1 ILE A 105 8022 18045 8408 -1185 -751 -1577 C ATOM 519 N SER A 106 -9.831 -19.265 8.905 1.00 74.58 N ANISOU 519 N SER A 106 5935 16019 6381 -138 -764 -1258 N ATOM 520 CA SER A 106 -10.314 -18.182 9.771 1.00 74.10 C ANISOU 520 CA SER A 106 5814 16045 6294 40 -799 -1213 C ATOM 521 C SER A 106 -10.581 -16.891 8.980 1.00 79.00 C ANISOU 521 C SER A 106 6392 16775 6850 279 -856 -1166 C ATOM 522 O SER A 106 -11.528 -16.186 9.308 1.00 79.32 O ANISOU 522 O SER A 106 6319 17021 6799 420 -902 -1179 O ATOM 523 CB SER A 106 -9.308 -17.893 10.883 1.00 75.38 C ANISOU 523 CB SER A 106 6105 15925 6609 94 -790 -1154 C ATOM 524 OG SER A 106 -9.807 -16.964 11.833 1.00 81.81 O ANISOU 524 OG SER A 106 6861 16829 7395 261 -830 -1144 O ATOM 525 N THR A 107 -9.733 -16.567 7.967 1.00 76.01 N ANISOU 525 N THR A 107 6101 16266 6515 330 -861 -1105 N ATOM 526 CA THR A 107 -9.824 -15.352 7.129 1.00 76.12 C ANISOU 526 CA THR A 107 6103 16340 6479 534 -928 -1019 C ATOM 527 C THR A 107 -11.218 -15.171 6.544 1.00 81.75 C ANISOU 527 C THR A 107 6641 17411 7008 596 -969 -1065 C ATOM 528 O THR A 107 -11.745 -14.057 6.533 1.00 81.95 O ANISOU 528 O THR A 107 6627 17520 6989 816 -1049 -1016 O ATOM 529 CB THR A 107 -8.804 -15.359 5.967 1.00 77.93 C ANISOU 529 CB THR A 107 6416 16459 6736 504 -911 -950 C ATOM 530 OG1 THR A 107 -9.166 -16.378 5.043 1.00 77.47 O ANISOU 530 OG1 THR A 107 6278 16587 6571 348 -870 -1044 O ATOM 531 CG2 THR A 107 -7.371 -15.560 6.415 1.00 71.80 C ANISOU 531 CG2 THR A 107 5790 15366 6124 448 -870 -907 C ATOM 532 N MET A 108 -11.804 -16.270 6.045 1.00 79.42 N ANISOU 532 N MET A 108 6246 17321 6608 405 -927 -1164 N ATOM 533 CA MET A 108 -13.130 -16.275 5.438 1.00 80.95 C ANISOU 533 CA MET A 108 6252 17894 6610 421 -959 -1222 C ATOM 534 C MET A 108 -14.212 -16.088 6.500 1.00 83.62 C ANISOU 534 C MET A 108 6456 18439 6877 475 -981 -1277 C ATOM 535 O MET A 108 -15.101 -15.267 6.304 1.00 84.74 O ANISOU 535 O MET A 108 6475 18819 6902 671 -1047 -1272 O ATOM 536 CB MET A 108 -13.349 -17.562 4.642 1.00 84.40 C ANISOU 536 CB MET A 108 6635 18466 6968 172 -911 -1326 C ATOM 537 CG MET A 108 -12.654 -17.548 3.300 1.00 89.19 C ANISOU 537 CG MET A 108 7299 19029 7560 176 -907 -1295 C ATOM 538 SD MET A 108 -13.594 -16.627 2.046 1.00 96.55 S ANISOU 538 SD MET A 108 8078 20322 8286 354 -981 -1242 S ATOM 539 CE MET A 108 -12.532 -15.268 1.806 1.00 92.50 C ANISOU 539 CE MET A 108 7715 19555 7878 577 -1027 -1045 C ATOM 540 N TYR A 109 -14.106 -16.798 7.642 1.00 77.55 N ANISOU 540 N TYR A 109 5708 17584 6172 319 -932 -1321 N ATOM 541 CA TYR A 109 -15.053 -16.702 8.752 1.00 77.06 C ANISOU 541 CA TYR A 109 5505 17745 6029 343 -941 -1371 C ATOM 542 C TYR A 109 -15.049 -15.290 9.381 1.00 78.96 C ANISOU 542 C TYR A 109 5761 17937 6303 665 -1008 -1334 C ATOM 543 O TYR A 109 -16.103 -14.820 9.797 1.00 80.04 O ANISOU 543 O TYR A 109 5729 18375 6309 806 -1050 -1391 O ATOM 544 CB TYR A 109 -14.750 -17.784 9.812 1.00 77.45 C ANISOU 544 CB TYR A 109 5603 17674 6151 89 -879 -1392 C ATOM 545 CG TYR A 109 -15.784 -17.926 10.918 1.00 80.71 C ANISOU 545 CG TYR A 109 5840 18386 6441 40 -876 -1440 C ATOM 546 CD1 TYR A 109 -17.146 -17.802 10.650 1.00 84.17 C ANISOU 546 CD1 TYR A 109 6040 19270 6669 67 -903 -1506 C ATOM 547 CD2 TYR A 109 -15.404 -18.252 12.216 1.00 81.21 C ANISOU 547 CD2 TYR A 109 5955 18322 6577 -52 -844 -1417 C ATOM 548 CE1 TYR A 109 -18.096 -17.939 11.659 1.00 86.21 C ANISOU 548 CE1 TYR A 109 6108 19857 6789 14 -896 -1551 C ATOM 549 CE2 TYR A 109 -16.348 -18.413 13.229 1.00 83.33 C ANISOU 549 CE2 TYR A 109 6042 18911 6707 -117 -837 -1453 C ATOM 550 CZ TYR A 109 -17.693 -18.251 12.947 1.00 91.29 C ANISOU 550 CZ TYR A 109 6806 20379 7502 -85 -861 -1522 C ATOM 551 OH TYR A 109 -18.623 -18.396 13.950 1.00 91.41 O ANISOU 551 OH TYR A 109 6616 20761 7357 -151 -850 -1558 O ATOM 552 N THR A 110 -13.881 -14.620 9.429 1.00 73.00 N ANISOU 552 N THR A 110 5202 16817 5719 784 -1026 -1248 N ATOM 553 CA THR A 110 -13.719 -13.270 9.985 1.00 72.55 C ANISOU 553 CA THR A 110 5203 16637 5727 1077 -1108 -1215 C ATOM 554 C THR A 110 -14.306 -12.201 9.063 1.00 79.17 C ANISOU 554 C THR A 110 5989 17609 6481 1330 -1209 -1180 C ATOM 555 O THR A 110 -14.824 -11.200 9.560 1.00 80.74 O ANISOU 555 O THR A 110 6142 17884 6653 1591 -1295 -1213 O ATOM 556 CB THR A 110 -12.242 -12.975 10.241 1.00 73.62 C ANISOU 556 CB THR A 110 5565 16342 6067 1080 -1101 -1125 C ATOM 557 OG1 THR A 110 -11.669 -14.071 10.945 1.00 72.70 O ANISOU 557 OG1 THR A 110 5498 16103 6021 839 -1011 -1146 O ATOM 558 CG2 THR A 110 -12.021 -11.679 11.013 1.00 70.10 C ANISOU 558 CG2 THR A 110 5193 15735 5706 1341 -1189 -1112 C ATOM 559 N VAL A 111 -14.185 -12.387 7.736 1.00 75.71 N ANISOU 559 N VAL A 111 5567 17196 6004 1267 -1207 -1114 N ATOM 560 CA VAL A 111 -14.657 -11.427 6.734 1.00 76.94 C ANISOU 560 CA VAL A 111 5687 17470 6078 1487 -1308 -1046 C ATOM 561 C VAL A 111 -16.169 -11.655 6.448 1.00 84.70 C ANISOU 561 C VAL A 111 6418 18924 6839 1526 -1327 -1148 C ATOM 562 O VAL A 111 -16.913 -10.679 6.364 1.00 87.13 O ANISOU 562 O VAL A 111 6651 19382 7073 1804 -1433 -1148 O ATOM 563 CB VAL A 111 -13.769 -11.473 5.446 1.00 79.32 C ANISOU 563 CB VAL A 111 6103 17623 6413 1399 -1299 -917 C ATOM 564 CG1 VAL A 111 -14.392 -10.701 4.279 1.00 80.19 C ANISOU 564 CG1 VAL A 111 6145 17926 6396 1580 -1398 -835 C ATOM 565 CG2 VAL A 111 -12.360 -10.949 5.740 1.00 77.59 C ANISOU 565 CG2 VAL A 111 6108 16979 6394 1410 -1306 -802 C ATOM 566 N THR A 112 -16.622 -12.918 6.318 1.00 80.25 N ANISOU 566 N THR A 112 5729 18590 6173 1254 -1236 -1238 N ATOM 567 CA THR A 112 -18.028 -13.209 6.017 1.00 80.70 C ANISOU 567 CA THR A 112 5534 19121 6009 1246 -1250 -1333 C ATOM 568 C THR A 112 -18.889 -13.142 7.287 1.00 83.77 C ANISOU 568 C THR A 112 5767 19736 6326 1311 -1253 -1439 C ATOM 569 O THR A 112 -19.945 -12.505 7.268 1.00 85.43 O ANISOU 569 O THR A 112 5799 20272 6387 1534 -1326 -1492 O ATOM 570 CB THR A 112 -18.182 -14.560 5.297 1.00 86.29 C ANISOU 570 CB THR A 112 6173 19982 6633 912 -1170 -1389 C ATOM 571 OG1 THR A 112 -17.804 -15.622 6.173 1.00 84.64 O ANISOU 571 OG1 THR A 112 6015 19636 6508 640 -1082 -1441 O ATOM 572 CG2 THR A 112 -17.375 -14.636 4.003 1.00 84.39 C ANISOU 572 CG2 THR A 112 6054 19581 6430 865 -1166 -1308 C ATOM 573 N GLY A 113 -18.438 -13.796 8.357 1.00 77.88 N ANISOU 573 N GLY A 113 5079 18842 5670 1127 -1178 -1469 N ATOM 574 CA GLY A 113 -19.144 -13.853 9.633 1.00 78.12 C ANISOU 574 CA GLY A 113 4958 19103 5620 1145 -1166 -1561 C ATOM 575 C GLY A 113 -20.086 -15.035 9.761 1.00 83.92 C ANISOU 575 C GLY A 113 5477 20229 6178 846 -1102 -1638 C ATOM 576 O GLY A 113 -20.885 -15.087 10.700 1.00 85.17 O ANISOU 576 O GLY A 113 5449 20701 6210 853 -1096 -1712 O ATOM 577 N ARG A 114 -20.015 -15.990 8.811 1.00 80.24 N ANISOU 577 N ARG A 114 5028 19767 5694 575 -1061 -1626 N ATOM 578 CA ARG A 114 -20.881 -17.173 8.806 1.00 81.10 C ANISOU 578 CA ARG A 114 4954 20212 5649 247 -1015 -1694 C ATOM 579 C ARG A 114 -20.070 -18.435 8.534 1.00 83.69 C ANISOU 579 C ARG A 114 5453 20242 6103 -108 -953 -1672 C ATOM 580 O ARG A 114 -19.161 -18.421 7.700 1.00 82.55 O ANISOU 580 O ARG A 114 5486 19799 6078 -86 -953 -1634 O ATOM 581 CB ARG A 114 -22.019 -17.028 7.771 1.00 82.41 C ANISOU 581 CB ARG A 114 4895 20820 5598 306 -1062 -1751 C ATOM 582 CG ARG A 114 -23.321 -17.696 8.202 1.00 92.53 C ANISOU 582 CG ARG A 114 5890 22611 6657 94 -1044 -1837 C ATOM 583 CD ARG A 114 -24.152 -18.150 7.020 1.00104.21 C ANISOU 583 CD ARG A 114 7202 24432 7960 -31 -1066 -1892 C ATOM 584 N TRP A 115 -20.395 -19.522 9.253 1.00 80.64 N ANISOU 584 N TRP A 115 5012 19943 5684 -431 -909 -1694 N ATOM 585 CA TRP A 115 -19.732 -20.817 9.110 1.00 79.74 C ANISOU 585 CA TRP A 115 5063 19543 5693 -775 -870 -1684 C ATOM 586 C TRP A 115 -20.437 -21.647 8.038 1.00 86.87 C ANISOU 586 C TRP A 115 5861 20675 6471 -1010 -884 -1763 C ATOM 587 O TRP A 115 -21.665 -21.815 8.078 1.00 88.62 O ANISOU 587 O TRP A 115 5838 21347 6488 -1113 -899 -1813 O ATOM 588 CB TRP A 115 -19.679 -21.570 10.447 1.00 77.99 C ANISOU 588 CB TRP A 115 4859 19263 5510 -1017 -836 -1645 C ATOM 589 CG TRP A 115 -18.771 -22.757 10.401 1.00 77.53 C ANISOU 589 CG TRP A 115 5027 18802 5627 -1299 -816 -1619 C ATOM 590 CD1 TRP A 115 -19.128 -24.052 10.171 1.00 81.59 C ANISOU 590 CD1 TRP A 115 5541 19340 6118 -1670 -823 -1651 C ATOM 591 CD2 TRP A 115 -17.338 -22.742 10.495 1.00 75.20 C ANISOU 591 CD2 TRP A 115 4998 18013 5563 -1214 -799 -1567 C ATOM 592 NE1 TRP A 115 -18.012 -24.854 10.155 1.00 80.24 N ANISOU 592 NE1 TRP A 115 5629 18703 6156 -1802 -818 -1629 N ATOM 593 CE2 TRP A 115 -16.897 -24.075 10.355 1.00 79.63 C ANISOU 593 CE2 TRP A 115 5706 18321 6229 -1523 -797 -1578 C ATOM 594 CE3 TRP A 115 -16.384 -21.731 10.716 1.00 74.14 C ANISOU 594 CE3 TRP A 115 4989 17627 5555 -913 -793 -1515 C ATOM 595 CZ2 TRP A 115 -15.540 -24.422 10.400 1.00 77.07 C ANISOU 595 CZ2 TRP A 115 5633 17528 6122 -1510 -786 -1546 C ATOM 596 CZ3 TRP A 115 -15.045 -22.078 10.768 1.00 73.78 C ANISOU 596 CZ3 TRP A 115 5182 17135 5716 -932 -774 -1473 C ATOM 597 CH2 TRP A 115 -14.634 -23.409 10.620 1.00 74.75 C ANISOU 597 CH2 TRP A 115 5432 17040 5930 -1215 -768 -1492 C ATOM 598 N THR A 116 -19.654 -22.156 7.068 1.00 83.12 N ANISOU 598 N THR A 116 5560 19915 6107 -1091 -881 -1785 N ATOM 599 CA THR A 116 -20.196 -22.917 5.941 1.00 84.41 C ANISOU 599 CA THR A 116 5647 20262 6163 -1295 -901 -1883 C ATOM 600 C THR A 116 -19.480 -24.268 5.721 1.00 89.04 C ANISOU 600 C THR A 116 6432 20503 6895 -1604 -892 -1933 C ATOM 601 O THR A 116 -19.798 -24.959 4.746 1.00 90.79 O ANISOU 601 O THR A 116 6623 20825 7050 -1776 -916 -2039 O ATOM 602 CB THR A 116 -20.118 -22.058 4.664 1.00 88.91 C ANISOU 602 CB THR A 116 6188 20926 6668 -1026 -927 -1896 C ATOM 603 OG1 THR A 116 -18.790 -21.559 4.506 1.00 82.37 O ANISOU 603 OG1 THR A 116 5582 19691 6023 -831 -911 -1825 O ATOM 604 CG2 THR A 116 -21.120 -20.902 4.662 1.00 90.08 C ANISOU 604 CG2 THR A 116 6106 21488 6632 -755 -966 -1876 C ATOM 605 N LEU A 117 -18.564 -24.667 6.631 1.00 83.58 N ANISOU 605 N LEU A 117 5938 19423 6395 -1673 -868 -1870 N ATOM 606 CA LEU A 117 -17.795 -25.910 6.491 1.00 83.29 C ANISOU 606 CA LEU A 117 6113 19016 6519 -1920 -876 -1917 C ATOM 607 C LEU A 117 -18.343 -27.131 7.292 1.00 88.59 C ANISOU 607 C LEU A 117 6782 19685 7192 -2312 -901 -1910 C ATOM 608 O LEU A 117 -17.723 -28.201 7.273 1.00 88.30 O ANISOU 608 O LEU A 117 6943 19299 7307 -2516 -926 -1942 O ATOM 609 CB LEU A 117 -16.335 -25.657 6.887 1.00 81.13 C ANISOU 609 CB LEU A 117 6073 18287 6464 -1746 -847 -1848 C ATOM 610 CG LEU A 117 -15.578 -24.614 6.076 1.00 84.40 C ANISOU 610 CG LEU A 117 6532 18631 6905 -1419 -829 -1836 C ATOM 611 CD1 LEU A 117 -14.228 -24.324 6.712 1.00 82.45 C ANISOU 611 CD1 LEU A 117 6483 17986 6858 -1272 -801 -1749 C ATOM 612 CD2 LEU A 117 -15.410 -25.043 4.619 1.00 86.69 C ANISOU 612 CD2 LEU A 117 6842 18937 7157 -1458 -845 -1959 C ATOM 613 N GLY A 118 -19.492 -26.979 7.944 1.00 86.44 N ANISOU 613 N GLY A 118 6288 19809 6747 -2417 -902 -1869 N ATOM 614 CA GLY A 118 -20.099 -28.062 8.712 1.00 88.46 C ANISOU 614 CA GLY A 118 6513 20124 6972 -2816 -930 -1833 C ATOM 615 C GLY A 118 -19.575 -28.197 10.130 1.00 92.56 C ANISOU 615 C GLY A 118 7140 20422 7606 -2864 -910 -1690 C ATOM 616 O GLY A 118 -18.572 -27.569 10.487 1.00 90.14 O ANISOU 616 O GLY A 118 6970 19841 7438 -2596 -876 -1637 O ATOM 617 N GLN A 119 -20.254 -29.037 10.946 1.00 91.13 N ANISOU 617 N GLN A 119 6893 20373 7358 -3228 -935 -1618 N ATOM 618 CA GLN A 119 -19.943 -29.259 12.363 1.00 90.68 C ANISOU 618 CA GLN A 119 6900 20191 7364 -3332 -923 -1462 C ATOM 619 C GLN A 119 -18.589 -29.979 12.608 1.00 93.40 C ANISOU 619 C GLN A 119 7583 19920 7985 -3372 -947 -1411 C ATOM 620 O GLN A 119 -17.853 -29.545 13.491 1.00 91.76 O ANISOU 620 O GLN A 119 7458 19540 7868 -3203 -914 -1314 O ATOM 621 CB GLN A 119 -21.086 -30.025 13.057 1.00 94.73 C ANISOU 621 CB GLN A 119 7240 21046 7709 -3754 -953 -1383 C ATOM 622 CG GLN A 119 -20.954 -30.149 14.585 1.00108.94 C ANISOU 622 CG GLN A 119 9040 22847 9507 -3864 -936 -1203 C ATOM 623 CD GLN A 119 -20.971 -28.823 15.311 1.00124.52 C ANISOU 623 CD GLN A 119 10852 25080 11381 -3490 -866 -1183 C ATOM 624 OE1 GLN A 119 -19.926 -28.270 15.671 1.00119.26 O ANISOU 624 OE1 GLN A 119 10347 24094 10870 -3212 -838 -1156 O ATOM 625 NE2 GLN A 119 -22.158 -28.293 15.557 1.00115.92 N ANISOU 625 NE2 GLN A 119 9436 24581 10027 -3474 -843 -1207 N ATOM 626 N VAL A 120 -18.279 -31.061 11.861 1.00 90.68 N ANISOU 626 N VAL A 120 7425 19262 7767 -3583 -1012 -1488 N ATOM 627 CA VAL A 120 -17.053 -31.868 12.015 1.00 90.06 C ANISOU 627 CA VAL A 120 7664 18606 7946 -3623 -1054 -1464 C ATOM 628 C VAL A 120 -15.774 -30.996 11.844 1.00 91.47 C ANISOU 628 C VAL A 120 7969 18519 8266 -3200 -998 -1486 C ATOM 629 O VAL A 120 -14.919 -31.011 12.735 1.00 89.90 O ANISOU 629 O VAL A 120 7913 18041 8203 -3131 -989 -1377 O ATOM 630 CB VAL A 120 -17.057 -33.099 11.063 1.00 96.05 C ANISOU 630 CB VAL A 120 8577 19124 8794 -3883 -1147 -1596 C ATOM 631 CG1 VAL A 120 -15.721 -33.844 11.087 1.00 95.26 C ANISOU 631 CG1 VAL A 120 8803 18428 8963 -3835 -1197 -1615 C ATOM 632 CG2 VAL A 120 -18.202 -34.052 11.404 1.00 99.02 C ANISOU 632 CG2 VAL A 120 8874 19683 9067 -4358 -1221 -1536 C ATOM 633 N VAL A 121 -15.670 -30.232 10.727 1.00 87.04 N ANISOU 633 N VAL A 121 7345 18067 7659 -2937 -964 -1614 N ATOM 634 CA VAL A 121 -14.545 -29.331 10.416 1.00 84.09 C ANISOU 634 CA VAL A 121 7062 17499 7389 -2561 -915 -1630 C ATOM 635 C VAL A 121 -14.484 -28.221 11.485 1.00 87.42 C ANISOU 635 C VAL A 121 7395 18046 7775 -2349 -860 -1499 C ATOM 636 O VAL A 121 -13.383 -27.834 11.880 1.00 86.47 O ANISOU 636 O VAL A 121 7416 17642 7798 -2161 -837 -1446 O ATOM 637 CB VAL A 121 -14.621 -28.770 8.958 1.00 87.28 C ANISOU 637 CB VAL A 121 7387 18064 7712 -2372 -901 -1768 C ATOM 638 CG1 VAL A 121 -13.678 -27.587 8.738 1.00 84.71 C ANISOU 638 CG1 VAL A 121 7098 17645 7442 -1996 -849 -1739 C ATOM 639 CG2 VAL A 121 -14.328 -29.864 7.940 1.00 88.18 C ANISOU 639 CG2 VAL A 121 7633 17974 7898 -2528 -955 -1922 C ATOM 640 N CYS A 122 -15.653 -27.761 11.986 1.00 84.40 N ANISOU 640 N CYS A 122 6777 18094 7197 -2389 -846 -1461 N ATOM 641 CA CYS A 122 -15.763 -26.757 13.053 1.00 83.28 C ANISOU 641 CA CYS A 122 6525 18125 6993 -2200 -806 -1369 C ATOM 642 C CYS A 122 -15.096 -27.282 14.344 1.00 86.37 C ANISOU 642 C CYS A 122 7055 18257 7504 -2322 -808 -1240 C ATOM 643 O CYS A 122 -14.333 -26.546 14.980 1.00 83.40 O ANISOU 643 O CYS A 122 6738 17745 7205 -2091 -779 -1186 O ATOM 644 CB CYS A 122 -17.227 -26.381 13.283 1.00 85.44 C ANISOU 644 CB CYS A 122 6503 18946 7015 -2254 -802 -1380 C ATOM 645 SG CYS A 122 -17.529 -25.341 14.736 1.00 89.08 S ANISOU 645 SG CYS A 122 6802 19678 7368 -2059 -766 -1298 S ATOM 646 N ASP A 123 -15.347 -28.569 14.687 1.00 85.13 N ANISOU 646 N ASP A 123 6963 18014 7370 -2691 -853 -1187 N ATOM 647 CA ASP A 123 -14.801 -29.228 15.878 1.00 85.33 C ANISOU 647 CA ASP A 123 7125 17798 7499 -2853 -873 -1042 C ATOM 648 C ASP A 123 -13.275 -29.274 15.847 1.00 86.42 C ANISOU 648 C ASP A 123 7523 17436 7876 -2667 -875 -1036 C ATOM 649 O ASP A 123 -12.642 -28.933 16.846 1.00 84.86 O ANISOU 649 O ASP A 123 7377 17129 7737 -2561 -855 -934 O ATOM 650 CB ASP A 123 -15.368 -30.652 16.033 1.00 90.21 C ANISOU 650 CB ASP A 123 7790 18375 8109 -3303 -946 -983 C ATOM 651 CG ASP A 123 -16.869 -30.730 16.246 1.00106.05 C ANISOU 651 CG ASP A 123 9524 20905 9865 -3553 -946 -957 C ATOM 652 OD1 ASP A 123 -17.398 -29.952 17.083 1.00107.00 O ANISOU 652 OD1 ASP A 123 9434 21400 9820 -3457 -895 -898 O ATOM 653 OD2 ASP A 123 -17.513 -31.589 15.606 1.00114.27 O ANISOU 653 OD2 ASP A 123 10555 21993 10869 -3849 -1003 -1005 O ATOM 654 N PHE A 124 -12.692 -29.667 14.700 1.00 82.42 N ANISOU 654 N PHE A 124 7161 16665 7491 -2619 -899 -1154 N ATOM 655 CA PHE A 124 -11.248 -29.760 14.532 1.00 80.66 C ANISOU 655 CA PHE A 124 7163 16008 7478 -2439 -903 -1171 C ATOM 656 C PHE A 124 -10.592 -28.382 14.455 1.00 80.35 C ANISOU 656 C PHE A 124 7082 16003 7446 -2069 -836 -1180 C ATOM 657 O PHE A 124 -9.505 -28.215 15.016 1.00 78.61 O ANISOU 657 O PHE A 124 6986 15526 7356 -1935 -825 -1118 O ATOM 658 CB PHE A 124 -10.881 -30.599 13.302 1.00 83.97 C ANISOU 658 CB PHE A 124 7720 16190 7995 -2494 -951 -1320 C ATOM 659 CG PHE A 124 -11.283 -32.058 13.365 1.00 89.26 C ANISOU 659 CG PHE A 124 8502 16695 8717 -2855 -1045 -1319 C ATOM 660 CD1 PHE A 124 -11.911 -32.670 12.287 1.00 95.10 C ANISOU 660 CD1 PHE A 124 9220 17507 9406 -3022 -1093 -1465 C ATOM 661 CD2 PHE A 124 -11.011 -32.827 14.493 1.00 93.13 C ANISOU 661 CD2 PHE A 124 9130 16944 9309 -3033 -1099 -1170 C ATOM 662 CE1 PHE A 124 -12.265 -34.024 12.336 1.00 98.97 C ANISOU 662 CE1 PHE A 124 9836 17807 9960 -3370 -1199 -1470 C ATOM 663 CE2 PHE A 124 -11.379 -34.176 14.547 1.00 98.99 C ANISOU 663 CE2 PHE A 124 10000 17498 10113 -3381 -1207 -1151 C ATOM 664 CZ PHE A 124 -12.004 -34.765 13.468 1.00 99.00 C ANISOU 664 CZ PHE A 124 9990 17550 10076 -3552 -1260 -1305 C ATOM 665 N TRP A 125 -11.248 -27.397 13.794 1.00 74.93 N ANISOU 665 N TRP A 125 6221 15631 6618 -1911 -801 -1247 N ATOM 666 CA TRP A 125 -10.722 -26.028 13.658 1.00 72.05 C ANISOU 666 CA TRP A 125 5822 15297 6258 -1573 -758 -1247 C ATOM 667 C TRP A 125 -10.607 -25.313 15.014 1.00 74.62 C ANISOU 667 C TRP A 125 6106 15674 6573 -1467 -737 -1142 C ATOM 668 O TRP A 125 -9.571 -24.690 15.256 1.00 72.77 O ANISOU 668 O TRP A 125 5968 15233 6449 -1262 -721 -1112 O ATOM 669 CB TRP A 125 -11.572 -25.185 12.691 1.00 70.53 C ANISOU 669 CB TRP A 125 5455 15434 5908 -1442 -748 -1325 C ATOM 670 CG TRP A 125 -11.098 -23.768 12.532 1.00 69.30 C ANISOU 670 CG TRP A 125 5281 15286 5762 -1112 -726 -1308 C ATOM 671 CD1 TRP A 125 -9.940 -23.350 11.945 1.00 70.66 C ANISOU 671 CD1 TRP A 125 5583 15210 6055 -937 -716 -1309 C ATOM 672 CD2 TRP A 125 -11.768 -22.584 12.986 1.00 68.68 C ANISOU 672 CD2 TRP A 125 5050 15476 5568 -924 -725 -1285 C ATOM 673 NE1 TRP A 125 -9.866 -21.976 11.965 1.00 68.96 N ANISOU 673 NE1 TRP A 125 5316 15071 5812 -677 -714 -1272 N ATOM 674 CE2 TRP A 125 -10.970 -21.480 12.609 1.00 70.74 C ANISOU 674 CE2 TRP A 125 5380 15594 5903 -648 -725 -1267 C ATOM 675 CE3 TRP A 125 -12.984 -22.345 13.653 1.00 70.92 C ANISOU 675 CE3 TRP A 125 5137 16124 5685 -957 -731 -1287 C ATOM 676 CZ2 TRP A 125 -11.339 -20.161 12.885 1.00 69.59 C ANISOU 676 CZ2 TRP A 125 5142 15606 5692 -401 -745 -1253 C ATOM 677 CZ3 TRP A 125 -13.362 -21.036 13.904 1.00 72.06 C ANISOU 677 CZ3 TRP A 125 5169 16460 5750 -684 -742 -1295 C ATOM 678 CH2 TRP A 125 -12.540 -19.962 13.531 1.00 71.34 C ANISOU 678 CH2 TRP A 125 5178 16168 5758 -406 -756 -1279 C ATOM 679 N LEU A 126 -11.658 -25.391 15.878 1.00 71.85 N ANISOU 679 N LEU A 126 5600 15624 6078 -1607 -738 -1094 N ATOM 680 CA LEU A 126 -11.683 -24.769 17.212 1.00 71.03 C ANISOU 680 CA LEU A 126 5426 15635 5928 -1519 -721 -1015 C ATOM 681 C LEU A 126 -10.636 -25.384 18.107 1.00 74.29 C ANISOU 681 C LEU A 126 6017 15717 6492 -1597 -729 -914 C ATOM 682 O LEU A 126 -9.919 -24.655 18.789 1.00 72.84 O ANISOU 682 O LEU A 126 5871 15442 6364 -1406 -713 -880 O ATOM 683 CB LEU A 126 -13.058 -24.905 17.897 1.00 73.15 C ANISOU 683 CB LEU A 126 5467 16345 5980 -1688 -720 -992 C ATOM 684 CG LEU A 126 -14.265 -24.198 17.290 1.00 78.58 C ANISOU 684 CG LEU A 126 5923 17458 6474 -1591 -716 -1088 C ATOM 685 CD1 LEU A 126 -15.528 -24.623 18.005 1.00 81.28 C ANISOU 685 CD1 LEU A 126 6044 18235 6605 -1827 -716 -1054 C ATOM 686 CD2 LEU A 126 -14.127 -22.688 17.355 1.00 79.42 C ANISOU 686 CD2 LEU A 126 5967 17650 6559 -1205 -708 -1142 C ATOM 687 N SER A 127 -10.534 -26.726 18.099 1.00 72.15 N ANISOU 687 N SER A 127 5863 15258 6292 -1877 -765 -867 N ATOM 688 CA SER A 127 -9.559 -27.444 18.917 1.00 72.02 C ANISOU 688 CA SER A 127 6028 14913 6424 -1960 -791 -759 C ATOM 689 C SER A 127 -8.120 -27.190 18.438 1.00 73.70 C ANISOU 689 C SER A 127 6421 14756 6827 -1730 -785 -802 C ATOM 690 O SER A 127 -7.260 -26.961 19.283 1.00 72.58 O ANISOU 690 O SER A 127 6354 14458 6767 -1633 -780 -727 O ATOM 691 CB SER A 127 -9.868 -28.935 18.966 1.00 78.56 C ANISOU 691 CB SER A 127 6951 15614 7286 -2313 -854 -698 C ATOM 692 OG SER A 127 -10.132 -29.460 17.678 1.00 92.68 O ANISOU 692 OG SER A 127 8784 17328 9105 -2388 -881 -821 O ATOM 693 N SER A 128 -7.864 -27.156 17.108 1.00 69.99 N ANISOU 693 N SER A 128 5995 14191 6406 -1638 -782 -922 N ATOM 694 CA SER A 128 -6.514 -26.872 16.588 1.00 68.11 C ANISOU 694 CA SER A 128 5894 13665 6319 -1423 -771 -965 C ATOM 695 C SER A 128 -6.145 -25.397 16.841 1.00 70.95 C ANISOU 695 C SER A 128 6183 14118 6656 -1151 -727 -950 C ATOM 696 O SER A 128 -4.956 -25.078 16.933 1.00 69.58 O ANISOU 696 O SER A 128 6111 13724 6601 -1000 -719 -933 O ATOM 697 CB SER A 128 -6.368 -27.249 15.114 1.00 70.51 C ANISOU 697 CB SER A 128 6243 13896 6653 -1410 -779 -1098 C ATOM 698 OG SER A 128 -7.094 -26.396 14.248 1.00 77.44 O ANISOU 698 OG SER A 128 6969 15059 7396 -1319 -751 -1166 O ATOM 699 N ASP A 129 -7.162 -24.518 17.027 1.00 67.09 N ANISOU 699 N ASP A 129 5522 13954 6015 -1093 -711 -957 N ATOM 700 CA ASP A 129 -6.954 -23.115 17.392 1.00 65.63 C ANISOU 700 CA ASP A 129 5277 13850 5808 -842 -694 -950 C ATOM 701 C ASP A 129 -6.523 -23.032 18.864 1.00 69.59 C ANISOU 701 C ASP A 129 5803 14299 6340 -839 -695 -864 C ATOM 702 O ASP A 129 -5.562 -22.335 19.180 1.00 68.43 O ANISOU 702 O ASP A 129 5725 13993 6283 -668 -692 -846 O ATOM 703 CB ASP A 129 -8.229 -22.291 17.152 1.00 67.89 C ANISOU 703 CB ASP A 129 5373 14501 5921 -765 -694 -1002 C ATOM 704 CG ASP A 129 -8.071 -20.780 17.212 1.00 74.80 C ANISOU 704 CG ASP A 129 6209 15426 6787 -475 -701 -1022 C ATOM 705 OD1 ASP A 129 -8.789 -20.085 16.474 1.00 75.73 O ANISOU 705 OD1 ASP A 129 6224 15741 6809 -360 -715 -1076 O ATOM 706 OD2 ASP A 129 -7.233 -20.292 18.004 1.00 79.39 O ANISOU 706 OD2 ASP A 129 6867 15841 7457 -365 -704 -982 O ATOM 707 N ILE A 130 -7.228 -23.748 19.759 1.00 67.13 N ANISOU 707 N ILE A 130 5428 14134 5943 -1045 -702 -804 N ATOM 708 CA ILE A 130 -6.894 -23.752 21.179 1.00 67.15 C ANISOU 708 CA ILE A 130 5436 14131 5945 -1066 -705 -713 C ATOM 709 C ILE A 130 -5.537 -24.439 21.396 1.00 71.75 C ANISOU 709 C ILE A 130 6219 14332 6711 -1093 -721 -645 C ATOM 710 O ILE A 130 -4.680 -23.833 22.038 1.00 71.32 O ANISOU 710 O ILE A 130 6206 14175 6718 -942 -717 -619 O ATOM 711 CB ILE A 130 -8.014 -24.378 22.072 1.00 71.98 C ANISOU 711 CB ILE A 130 5914 15040 6395 -1306 -710 -643 C ATOM 712 CG1 ILE A 130 -9.349 -23.598 21.947 1.00 72.88 C ANISOU 712 CG1 ILE A 130 5796 15589 6305 -1241 -694 -726 C ATOM 713 CG2 ILE A 130 -7.569 -24.444 23.542 1.00 72.56 C ANISOU 713 CG2 ILE A 130 5998 15112 6460 -1335 -715 -534 C ATOM 714 CD1 ILE A 130 -10.562 -24.280 22.587 1.00 79.88 C ANISOU 714 CD1 ILE A 130 6517 16830 7004 -1514 -696 -666 C ATOM 715 N THR A 131 -5.336 -25.672 20.854 1.00 69.06 N ANISOU 715 N THR A 131 5999 13783 6457 -1270 -749 -628 N ATOM 716 CA THR A 131 -4.115 -26.474 21.057 1.00 69.00 C ANISOU 716 CA THR A 131 6180 13416 6620 -1289 -781 -572 C ATOM 717 C THR A 131 -2.834 -25.818 20.553 1.00 70.63 C ANISOU 717 C THR A 131 6467 13420 6950 -1043 -761 -629 C ATOM 718 O THR A 131 -1.854 -25.791 21.297 1.00 69.76 O ANISOU 718 O THR A 131 6431 13152 6924 -971 -770 -566 O ATOM 719 CB THR A 131 -4.200 -27.873 20.429 1.00 82.99 C ANISOU 719 CB THR A 131 8074 14991 8468 -1494 -833 -581 C ATOM 720 OG1 THR A 131 -4.462 -27.745 19.039 1.00 93.23 O ANISOU 720 OG1 THR A 131 9353 16310 9759 -1440 -818 -721 O ATOM 721 CG2 THR A 131 -5.245 -28.748 21.064 1.00 81.08 C ANISOU 721 CG2 THR A 131 7792 14883 8132 -1795 -872 -484 C ATOM 722 N CYS A 132 -2.816 -25.323 19.302 1.00 66.03 N ANISOU 722 N CYS A 132 5863 12857 6368 -928 -738 -737 N ATOM 723 CA CYS A 132 -1.598 -24.746 18.726 1.00 64.40 C ANISOU 723 CA CYS A 132 5721 12485 6262 -728 -721 -778 C ATOM 724 C CYS A 132 -1.254 -23.398 19.370 1.00 66.24 C ANISOU 724 C CYS A 132 5896 12795 6476 -553 -702 -746 C ATOM 725 O CYS A 132 -0.076 -23.156 19.648 1.00 64.74 O ANISOU 725 O CYS A 132 5777 12439 6384 -450 -702 -719 O ATOM 726 CB CYS A 132 -1.696 -24.638 17.208 1.00 64.69 C ANISOU 726 CB CYS A 132 5744 12549 6285 -678 -706 -884 C ATOM 727 SG CYS A 132 -2.000 -26.216 16.367 1.00 70.07 S ANISOU 727 SG CYS A 132 6509 13112 7003 -866 -743 -966 S ATOM 728 N CYS A 133 -2.265 -22.551 19.660 1.00 62.13 N ANISOU 728 N CYS A 133 5249 12526 5833 -517 -695 -757 N ATOM 729 CA CYS A 133 -1.995 -21.263 20.301 1.00 60.81 C ANISOU 729 CA CYS A 133 5041 12410 5655 -343 -697 -750 C ATOM 730 C CYS A 133 -1.488 -21.456 21.726 1.00 63.60 C ANISOU 730 C CYS A 133 5421 12710 6034 -370 -708 -678 C ATOM 731 O CYS A 133 -0.559 -20.752 22.110 1.00 63.35 O ANISOU 731 O CYS A 133 5429 12571 6069 -240 -715 -669 O ATOM 732 CB CYS A 133 -3.211 -20.355 20.262 1.00 61.65 C ANISOU 732 CB CYS A 133 5007 12792 5623 -265 -703 -802 C ATOM 733 SG CYS A 133 -3.598 -19.704 18.618 1.00 65.52 S ANISOU 733 SG CYS A 133 5469 13341 6087 -160 -704 -869 S ATOM 734 N THR A 134 -2.034 -22.438 22.481 1.00 59.38 N ANISOU 734 N THR A 134 4868 12246 5445 -553 -715 -616 N ATOM 735 CA THR A 134 -1.548 -22.755 23.830 1.00 59.02 C ANISOU 735 CA THR A 134 4848 12164 5411 -600 -730 -525 C ATOM 736 C THR A 134 -0.097 -23.286 23.720 1.00 61.98 C ANISOU 736 C THR A 134 5377 12222 5951 -569 -744 -483 C ATOM 737 O THR A 134 0.753 -22.846 24.492 1.00 61.33 O ANISOU 737 O THR A 134 5316 12078 5909 -479 -752 -449 O ATOM 738 CB THR A 134 -2.485 -23.734 24.570 1.00 66.21 C ANISOU 738 CB THR A 134 5706 13236 6215 -833 -742 -439 C ATOM 739 OG1 THR A 134 -3.833 -23.254 24.521 1.00 60.70 O ANISOU 739 OG1 THR A 134 4841 12871 5350 -855 -725 -494 O ATOM 740 CG2 THR A 134 -2.068 -23.960 26.028 1.00 63.29 C ANISOU 740 CG2 THR A 134 5341 12884 5824 -881 -760 -328 C ATOM 741 N ALA A 135 0.195 -24.169 22.723 1.00 58.54 N ANISOU 741 N ALA A 135 5036 11603 5603 -627 -751 -504 N ATOM 742 CA ALA A 135 1.545 -24.699 22.460 1.00 57.72 C ANISOU 742 CA ALA A 135 5062 11224 5647 -568 -768 -495 C ATOM 743 C ALA A 135 2.514 -23.555 22.121 1.00 61.19 C ANISOU 743 C ALA A 135 5490 11626 6135 -368 -744 -542 C ATOM 744 O ALA A 135 3.645 -23.552 22.589 1.00 59.19 O ANISOU 744 O ALA A 135 5288 11241 5959 -297 -756 -506 O ATOM 745 CB ALA A 135 1.510 -25.716 21.325 1.00 58.95 C ANISOU 745 CB ALA A 135 5298 11237 5862 -641 -784 -554 C ATOM 746 N SER A 136 2.033 -22.551 21.363 1.00 59.29 N ANISOU 746 N SER A 136 5176 11512 5837 -289 -719 -609 N ATOM 747 CA SER A 136 2.787 -21.361 20.958 1.00 58.30 C ANISOU 747 CA SER A 136 5042 11362 5748 -131 -709 -635 C ATOM 748 C SER A 136 3.212 -20.537 22.183 1.00 61.45 C ANISOU 748 C SER A 136 5421 11779 6147 -59 -727 -596 C ATOM 749 O SER A 136 4.382 -20.161 22.284 1.00 61.27 O ANISOU 749 O SER A 136 5436 11642 6201 17 -733 -580 O ATOM 750 CB SER A 136 1.949 -20.512 20.002 1.00 61.36 C ANISOU 750 CB SER A 136 5363 11890 6063 -80 -698 -691 C ATOM 751 OG SER A 136 2.705 -19.496 19.369 1.00 68.69 O ANISOU 751 OG SER A 136 6302 12764 7033 40 -699 -694 O ATOM 752 N ILE A 137 2.268 -20.288 23.117 1.00 57.28 N ANISOU 752 N ILE A 137 4822 11418 5523 -88 -737 -591 N ATOM 753 CA ILE A 137 2.478 -19.518 24.353 1.00 56.60 C ANISOU 753 CA ILE A 137 4701 11395 5410 -19 -759 -583 C ATOM 754 C ILE A 137 3.434 -20.261 25.309 1.00 59.70 C ANISOU 754 C ILE A 137 5148 11679 5858 -69 -771 -502 C ATOM 755 O ILE A 137 4.329 -19.646 25.877 1.00 57.28 O ANISOU 755 O ILE A 137 4854 11316 5593 14 -789 -499 O ATOM 756 CB ILE A 137 1.103 -19.230 25.052 1.00 60.33 C ANISOU 756 CB ILE A 137 5057 12133 5733 -38 -764 -615 C ATOM 757 CG1 ILE A 137 0.135 -18.385 24.163 1.00 60.66 C ANISOU 757 CG1 ILE A 137 5033 12302 5714 51 -766 -702 C ATOM 758 CG2 ILE A 137 1.276 -18.622 26.452 1.00 59.37 C ANISOU 758 CG2 ILE A 137 4887 12110 5561 22 -789 -622 C ATOM 759 CD1 ILE A 137 -1.372 -18.660 24.428 1.00 63.00 C ANISOU 759 CD1 ILE A 137 5199 12890 5849 -19 -757 -730 C ATOM 760 N TRP A 138 3.212 -21.569 25.502 1.00 58.75 N ANISOU 760 N TRP A 138 5061 11529 5734 -210 -771 -434 N ATOM 761 CA TRP A 138 3.983 -22.397 26.422 1.00 59.76 C ANISOU 761 CA TRP A 138 5247 11554 5905 -263 -797 -336 C ATOM 762 C TRP A 138 5.411 -22.683 25.928 1.00 63.03 C ANISOU 762 C TRP A 138 5754 11738 6457 -184 -806 -333 C ATOM 763 O TRP A 138 6.269 -23.024 26.746 1.00 63.07 O ANISOU 763 O TRP A 138 5794 11669 6503 -170 -833 -265 O ATOM 764 CB TRP A 138 3.228 -23.690 26.728 1.00 60.41 C ANISOU 764 CB TRP A 138 5352 11657 5945 -451 -815 -249 C ATOM 765 CG TRP A 138 2.371 -23.566 27.954 1.00 62.63 C ANISOU 765 CG TRP A 138 5531 12187 6077 -538 -819 -190 C ATOM 766 CD1 TRP A 138 1.032 -23.316 27.996 1.00 66.24 C ANISOU 766 CD1 TRP A 138 5873 12901 6394 -611 -800 -222 C ATOM 767 CD2 TRP A 138 2.824 -23.573 29.318 1.00 62.98 C ANISOU 767 CD2 TRP A 138 5555 12297 6079 -544 -843 -103 C ATOM 768 NE1 TRP A 138 0.609 -23.224 29.306 1.00 66.83 N ANISOU 768 NE1 TRP A 138 5851 13208 6333 -668 -807 -160 N ATOM 769 CE2 TRP A 138 1.687 -23.390 30.137 1.00 67.94 C ANISOU 769 CE2 TRP A 138 6051 13233 6529 -634 -834 -82 C ATOM 770 CE3 TRP A 138 4.078 -23.755 29.930 1.00 64.32 C ANISOU 770 CE3 TRP A 138 5792 12320 6328 -483 -873 -39 C ATOM 771 CZ2 TRP A 138 1.764 -23.375 31.535 1.00 68.22 C ANISOU 771 CZ2 TRP A 138 6021 13441 6459 -668 -852 -1 C ATOM 772 CZ3 TRP A 138 4.157 -23.739 31.318 1.00 66.67 C ANISOU 772 CZ3 TRP A 138 6032 12770 6529 -517 -895 47 C ATOM 773 CH2 TRP A 138 3.011 -23.552 32.105 1.00 68.32 C ANISOU 773 CH2 TRP A 138 6112 13290 6556 -611 -883 66 C ATOM 774 N HIS A 139 5.672 -22.505 24.612 1.00 58.68 N ANISOU 774 N HIS A 139 5225 11107 5962 -127 -783 -407 N ATOM 775 CA HIS A 139 6.991 -22.664 24.001 1.00 57.41 C ANISOU 775 CA HIS A 139 5117 10790 5905 -39 -783 -425 C ATOM 776 C HIS A 139 7.876 -21.518 24.439 1.00 64.17 C ANISOU 776 C HIS A 139 5935 11672 6776 62 -785 -425 C ATOM 777 O HIS A 139 9.064 -21.717 24.723 1.00 63.44 O ANISOU 777 O HIS A 139 5863 11494 6745 114 -799 -398 O ATOM 778 CB HIS A 139 6.891 -22.727 22.476 1.00 56.78 C ANISOU 778 CB HIS A 139 5046 10684 5844 -19 -755 -507 C ATOM 779 CG HIS A 139 6.857 -24.128 21.968 1.00 60.60 C ANISOU 779 CG HIS A 139 5607 11042 6377 -77 -773 -526 C ATOM 780 ND1 HIS A 139 5.665 -24.816 21.813 1.00 63.06 N ANISOU 780 ND1 HIS A 139 5935 11381 6645 -208 -783 -532 N ATOM 781 CD2 HIS A 139 7.877 -24.948 21.641 1.00 62.57 C ANISOU 781 CD2 HIS A 139 5921 11137 6714 -16 -794 -551 C ATOM 782 CE1 HIS A 139 5.996 -26.024 21.396 1.00 63.29 C ANISOU 782 CE1 HIS A 139 6057 11241 6750 -233 -818 -559 C ATOM 783 NE2 HIS A 139 7.317 -26.145 21.266 1.00 63.59 N ANISOU 783 NE2 HIS A 139 6128 11165 6869 -102 -826 -580 N ATOM 784 N LEU A 140 7.267 -20.324 24.539 1.00 63.02 N ANISOU 784 N LEU A 140 5731 11644 6569 90 -781 -459 N ATOM 785 CA LEU A 140 7.893 -19.085 24.977 1.00 63.79 C ANISOU 785 CA LEU A 140 5801 11758 6677 170 -801 -472 C ATOM 786 C LEU A 140 8.431 -19.221 26.407 1.00 70.21 C ANISOU 786 C LEU A 140 6607 12586 7484 168 -830 -427 C ATOM 787 O LEU A 140 9.607 -18.896 26.620 1.00 70.56 O ANISOU 787 O LEU A 140 6657 12569 7584 214 -846 -414 O ATOM 788 CB LEU A 140 6.861 -17.960 24.891 1.00 64.04 C ANISOU 788 CB LEU A 140 5789 11900 6643 206 -812 -530 C ATOM 789 CG LEU A 140 7.241 -16.690 24.171 1.00 68.98 C ANISOU 789 CG LEU A 140 6422 12480 7306 280 -832 -560 C ATOM 790 CD1 LEU A 140 7.550 -16.952 22.706 1.00 69.02 C ANISOU 790 CD1 LEU A 140 6447 12432 7344 266 -799 -548 C ATOM 791 CD2 LEU A 140 6.086 -15.716 24.229 1.00 72.43 C ANISOU 791 CD2 LEU A 140 6828 13016 7679 340 -863 -621 C ATOM 792 N CYS A 141 7.615 -19.745 27.379 1.00 66.88 N ANISOU 792 N CYS A 141 6161 12268 6983 105 -838 -393 N ATOM 793 CA CYS A 141 8.148 -19.895 28.736 1.00 67.35 C ANISOU 793 CA CYS A 141 6204 12367 7019 101 -869 -338 C ATOM 794 C CYS A 141 9.138 -21.067 28.832 1.00 69.40 C ANISOU 794 C CYS A 141 6526 12489 7352 81 -882 -249 C ATOM 795 O CYS A 141 10.037 -20.989 29.665 1.00 70.28 O ANISOU 795 O CYS A 141 6628 12601 7475 117 -910 -212 O ATOM 796 CB CYS A 141 7.093 -19.955 29.844 1.00 69.27 C ANISOU 796 CB CYS A 141 6381 12809 7130 44 -878 -321 C ATOM 797 SG CYS A 141 5.412 -20.363 29.313 1.00 74.25 S ANISOU 797 SG CYS A 141 6972 13572 7667 -53 -848 -335 S ATOM 798 N VAL A 142 9.029 -22.103 27.975 1.00 63.34 N ANISOU 798 N VAL A 142 5825 11603 6640 40 -872 -230 N ATOM 799 CA VAL A 142 9.992 -23.219 27.972 1.00 63.13 C ANISOU 799 CA VAL A 142 5870 11419 6698 59 -901 -169 C ATOM 800 C VAL A 142 11.381 -22.698 27.447 1.00 64.82 C ANISOU 800 C VAL A 142 6066 11577 6985 182 -894 -220 C ATOM 801 O VAL A 142 12.425 -23.145 27.930 1.00 64.05 O ANISOU 801 O VAL A 142 5980 11426 6928 238 -927 -175 O ATOM 802 CB VAL A 142 9.445 -24.445 27.193 1.00 68.01 C ANISOU 802 CB VAL A 142 6572 11912 7358 -10 -909 -162 C ATOM 803 CG1 VAL A 142 10.559 -25.364 26.688 1.00 68.72 C ANISOU 803 CG1 VAL A 142 6737 11812 7559 76 -940 -170 C ATOM 804 CG2 VAL A 142 8.467 -25.225 28.058 1.00 68.78 C ANISOU 804 CG2 VAL A 142 6694 12046 7393 -159 -942 -57 C ATOM 805 N ILE A 143 11.368 -21.718 26.510 1.00 59.68 N ANISOU 805 N ILE A 143 5379 10961 6336 215 -857 -302 N ATOM 806 CA ILE A 143 12.557 -21.041 25.974 1.00 58.08 C ANISOU 806 CA ILE A 143 5139 10753 6176 291 -848 -337 C ATOM 807 C ILE A 143 13.153 -20.179 27.109 1.00 61.15 C ANISOU 807 C ILE A 143 5481 11210 6545 307 -878 -313 C ATOM 808 O ILE A 143 14.377 -20.165 27.300 1.00 61.30 O ANISOU 808 O ILE A 143 5471 11224 6597 355 -894 -298 O ATOM 809 CB ILE A 143 12.192 -20.212 24.697 1.00 60.02 C ANISOU 809 CB ILE A 143 5364 11028 6413 289 -811 -399 C ATOM 810 CG1 ILE A 143 12.057 -21.119 23.460 1.00 60.58 C ANISOU 810 CG1 ILE A 143 5464 11047 6506 296 -782 -441 C ATOM 811 CG2 ILE A 143 13.187 -19.073 24.425 1.00 59.73 C ANISOU 811 CG2 ILE A 143 5278 11026 6393 319 -814 -406 C ATOM 812 CD1 ILE A 143 11.099 -20.576 22.331 1.00 67.71 C ANISOU 812 CD1 ILE A 143 6355 12005 7367 265 -750 -489 C ATOM 813 N ALA A 144 12.272 -19.492 27.873 1.00 56.40 N ANISOU 813 N ALA A 144 4861 10692 5878 272 -891 -324 N ATOM 814 CA ALA A 144 12.661 -18.648 29.002 1.00 56.01 C ANISOU 814 CA ALA A 144 4768 10718 5796 287 -929 -331 C ATOM 815 C ALA A 144 13.218 -19.494 30.155 1.00 60.64 C ANISOU 815 C ALA A 144 5347 11329 6364 287 -958 -253 C ATOM 816 O ALA A 144 14.242 -19.116 30.728 1.00 61.43 O ANISOU 816 O ALA A 144 5410 11457 6473 319 -988 -248 O ATOM 817 CB ALA A 144 11.484 -17.818 29.473 1.00 56.58 C ANISOU 817 CB ALA A 144 4818 10890 5792 276 -940 -388 C ATOM 818 N LEU A 145 12.577 -20.652 30.468 1.00 55.54 N ANISOU 818 N LEU A 145 4740 10671 5693 240 -959 -180 N ATOM 819 CA LEU A 145 13.035 -21.579 31.508 1.00 54.86 C ANISOU 819 CA LEU A 145 4664 10589 5590 232 -1000 -73 C ATOM 820 C LEU A 145 14.454 -22.006 31.207 1.00 57.93 C ANISOU 820 C LEU A 145 5065 10882 6065 319 -1019 -55 C ATOM 821 O LEU A 145 15.299 -21.943 32.093 1.00 59.08 O ANISOU 821 O LEU A 145 5170 11084 6192 357 -1056 -15 O ATOM 822 CB LEU A 145 12.109 -22.812 31.635 1.00 55.25 C ANISOU 822 CB LEU A 145 4777 10599 5617 142 -1009 21 C ATOM 823 CG LEU A 145 10.852 -22.620 32.486 1.00 60.05 C ANISOU 823 CG LEU A 145 5337 11387 6093 42 -1006 51 C ATOM 824 CD1 LEU A 145 9.782 -23.630 32.135 1.00 60.74 C ANISOU 824 CD1 LEU A 145 5479 11435 6165 -80 -1003 117 C ATOM 825 CD2 LEU A 145 11.168 -22.622 33.990 1.00 61.82 C ANISOU 825 CD2 LEU A 145 5508 11753 6227 31 -1048 134 C ATOM 826 N ASP A 146 14.720 -22.350 29.933 1.00 53.12 N ANISOU 826 N ASP A 146 4491 10158 5534 360 -993 -101 N ATOM 827 CA ASP A 146 16.002 -22.776 29.404 1.00 53.09 C ANISOU 827 CA ASP A 146 4479 10092 5600 462 -1003 -114 C ATOM 828 C ASP A 146 17.041 -21.664 29.553 1.00 58.92 C ANISOU 828 C ASP A 146 5121 10939 6327 496 -1001 -152 C ATOM 829 O ASP A 146 18.151 -21.951 30.014 1.00 60.22 O ANISOU 829 O ASP A 146 5245 11133 6504 567 -1035 -121 O ATOM 830 CB ASP A 146 15.849 -23.203 27.940 1.00 54.48 C ANISOU 830 CB ASP A 146 4692 10178 5831 488 -966 -187 C ATOM 831 CG ASP A 146 17.126 -23.704 27.298 1.00 65.67 C ANISOU 831 CG ASP A 146 6082 11566 7302 613 -974 -227 C ATOM 832 OD1 ASP A 146 17.674 -22.985 26.441 1.00 66.95 O ANISOU 832 OD1 ASP A 146 6170 11809 7459 634 -933 -293 O ATOM 833 OD2 ASP A 146 17.586 -24.813 27.662 1.00 68.23 O ANISOU 833 OD2 ASP A 146 6457 11799 7670 692 -1027 -189 O ATOM 834 N ARG A 147 16.679 -20.397 29.222 1.00 54.29 N ANISOU 834 N ARG A 147 4500 10409 5717 443 -974 -212 N ATOM 835 CA ARG A 147 17.575 -19.237 29.368 1.00 53.42 C ANISOU 835 CA ARG A 147 4314 10380 5602 437 -987 -243 C ATOM 836 C ARG A 147 17.836 -18.923 30.854 1.00 58.93 C ANISOU 836 C ARG A 147 4976 11165 6250 428 -1037 -219 C ATOM 837 O ARG A 147 18.981 -18.644 31.214 1.00 60.95 O ANISOU 837 O ARG A 147 5164 11487 6507 447 -1065 -215 O ATOM 838 CB ARG A 147 17.014 -18.000 28.652 1.00 50.80 C ANISOU 838 CB ARG A 147 3988 10044 5270 378 -968 -302 C ATOM 839 CG ARG A 147 17.043 -18.108 27.135 1.00 57.76 C ANISOU 839 CG ARG A 147 4876 10887 6184 382 -922 -321 C ATOM 840 CD ARG A 147 18.049 -17.169 26.511 1.00 63.90 C ANISOU 840 CD ARG A 147 5588 11717 6973 351 -924 -325 C ATOM 841 NE ARG A 147 18.484 -17.650 25.201 1.00 68.43 N ANISOU 841 NE ARG A 147 6131 12316 7555 378 -877 -331 N ATOM 842 CZ ARG A 147 19.725 -17.559 24.729 1.00 88.68 C ANISOU 842 CZ ARG A 147 8603 14980 10112 382 -868 -323 C ATOM 843 NH1 ARG A 147 20.687 -16.996 25.465 1.00 68.04 N ANISOU 843 NH1 ARG A 147 5922 12438 7491 347 -907 -299 N ATOM 844 NH2 ARG A 147 20.020 -18.034 23.527 1.00 83.95 N ANISOU 844 NH2 ARG A 147 7962 14438 9498 419 -822 -346 N ATOM 845 N TYR A 148 16.789 -18.998 31.709 1.00 54.44 N ANISOU 845 N TYR A 148 4436 10628 5622 394 -1050 -205 N ATOM 846 CA TYR A 148 16.849 -18.761 33.153 1.00 54.67 C ANISOU 846 CA TYR A 148 4422 10775 5574 384 -1095 -189 C ATOM 847 C TYR A 148 17.854 -19.725 33.779 1.00 62.16 C ANISOU 847 C TYR A 148 5348 11748 6523 435 -1129 -96 C ATOM 848 O TYR A 148 18.830 -19.259 34.367 1.00 63.34 O ANISOU 848 O TYR A 148 5426 11987 6652 453 -1164 -108 O ATOM 849 CB TYR A 148 15.440 -18.880 33.786 1.00 55.76 C ANISOU 849 CB TYR A 148 4579 10979 5627 339 -1091 -183 C ATOM 850 CG TYR A 148 15.408 -19.085 35.284 1.00 57.96 C ANISOU 850 CG TYR A 148 4810 11412 5800 326 -1132 -131 C ATOM 851 CD1 TYR A 148 15.560 -18.012 36.161 1.00 60.09 C ANISOU 851 CD1 TYR A 148 5013 11817 6001 332 -1167 -220 C ATOM 852 CD2 TYR A 148 15.199 -20.349 35.830 1.00 59.23 C ANISOU 852 CD2 TYR A 148 4996 11584 5923 301 -1144 7 C ATOM 853 CE1 TYR A 148 15.560 -18.201 37.546 1.00 59.77 C ANISOU 853 CE1 TYR A 148 4911 11956 5842 323 -1204 -179 C ATOM 854 CE2 TYR A 148 15.220 -20.553 37.211 1.00 60.72 C ANISOU 854 CE2 TYR A 148 5133 11941 5998 280 -1185 79 C ATOM 855 CZ TYR A 148 15.381 -19.474 38.066 1.00 65.31 C ANISOU 855 CZ TYR A 148 5628 12694 6494 293 -1209 -19 C ATOM 856 OH TYR A 148 15.359 -19.677 39.426 1.00 64.79 O ANISOU 856 OH TYR A 148 5495 12830 6292 272 -1248 44 O ATOM 857 N TRP A 149 17.679 -21.050 33.580 1.00 59.16 N ANISOU 857 N TRP A 149 5031 11276 6173 462 -1129 -7 N ATOM 858 CA TRP A 149 18.590 -22.071 34.121 1.00 60.15 C ANISOU 858 CA TRP A 149 5155 11388 6310 536 -1179 92 C ATOM 859 C TRP A 149 20.037 -21.915 33.628 1.00 65.56 C ANISOU 859 C TRP A 149 5772 12092 7047 629 -1186 50 C ATOM 860 O TRP A 149 20.971 -22.203 34.378 1.00 66.31 O ANISOU 860 O TRP A 149 5810 12266 7117 692 -1235 102 O ATOM 861 CB TRP A 149 18.098 -23.472 33.755 1.00 59.32 C ANISOU 861 CB TRP A 149 5160 11122 6256 548 -1192 175 C ATOM 862 CG TRP A 149 16.809 -23.874 34.406 1.00 60.53 C ANISOU 862 CG TRP A 149 5368 11288 6342 436 -1200 259 C ATOM 863 CD1 TRP A 149 16.457 -23.694 35.711 1.00 63.93 C ANISOU 863 CD1 TRP A 149 5754 11878 6658 373 -1228 332 C ATOM 864 CD2 TRP A 149 15.745 -24.624 33.802 1.00 60.43 C ANISOU 864 CD2 TRP A 149 5451 11150 6358 363 -1186 287 C ATOM 865 NE1 TRP A 149 15.217 -24.235 35.944 1.00 63.95 N ANISOU 865 NE1 TRP A 149 5808 11884 6607 259 -1225 410 N ATOM 866 CE2 TRP A 149 14.760 -24.824 34.793 1.00 65.09 C ANISOU 866 CE2 TRP A 149 6043 11846 6843 243 -1203 387 C ATOM 867 CE3 TRP A 149 15.507 -25.112 32.503 1.00 61.24 C ANISOU 867 CE3 TRP A 149 5628 11086 6553 380 -1161 227 C ATOM 868 CZ2 TRP A 149 13.562 -25.503 34.533 1.00 64.79 C ANISOU 868 CZ2 TRP A 149 6076 11749 6793 122 -1197 442 C ATOM 869 CZ3 TRP A 149 14.329 -25.796 32.251 1.00 63.04 C ANISOU 869 CZ3 TRP A 149 5938 11236 6778 270 -1160 269 C ATOM 870 CH2 TRP A 149 13.372 -25.987 33.256 1.00 64.35 C ANISOU 870 CH2 TRP A 149 6102 11505 6842 134 -1179 381 C ATOM 871 N ALA A 150 20.212 -21.476 32.367 1.00 61.87 N ANISOU 871 N ALA A 150 5293 11579 6634 636 -1137 -36 N ATOM 872 CA ALA A 150 21.509 -21.267 31.724 1.00 61.73 C ANISOU 872 CA ALA A 150 5188 11622 6646 703 -1131 -80 C ATOM 873 C ALA A 150 22.275 -20.081 32.323 1.00 66.59 C ANISOU 873 C ALA A 150 5695 12391 7215 648 -1151 -109 C ATOM 874 O ALA A 150 23.499 -20.151 32.416 1.00 67.94 O ANISOU 874 O ALA A 150 5769 12668 7377 707 -1175 -104 O ATOM 875 CB ALA A 150 21.318 -21.047 30.237 1.00 61.56 C ANISOU 875 CB ALA A 150 5177 11547 6668 692 -1071 -152 C ATOM 876 N ILE A 151 21.570 -18.995 32.705 1.00 62.29 N ANISOU 876 N ILE A 151 5165 11864 6639 541 -1151 -150 N ATOM 877 CA ILE A 151 22.193 -17.791 33.270 1.00 62.16 C ANISOU 877 CA ILE A 151 5070 11959 6590 472 -1188 -197 C ATOM 878 C ILE A 151 22.214 -17.824 34.831 1.00 69.10 C ANISOU 878 C ILE A 151 5918 12946 7390 478 -1245 -174 C ATOM 879 O ILE A 151 23.027 -17.124 35.427 1.00 69.99 O ANISOU 879 O ILE A 151 5948 13176 7469 445 -1289 -207 O ATOM 880 CB ILE A 151 21.490 -16.508 32.717 1.00 63.50 C ANISOU 880 CB ILE A 151 5282 12065 6781 372 -1177 -274 C ATOM 881 CG1 ILE A 151 22.388 -15.253 32.825 1.00 63.64 C ANISOU 881 CG1 ILE A 151 5231 12149 6801 282 -1222 -322 C ATOM 882 CG2 ILE A 151 20.091 -16.295 33.314 1.00 63.54 C ANISOU 882 CG2 ILE A 151 5360 12033 6748 356 -1183 -307 C ATOM 883 CD1 ILE A 151 21.876 -13.986 32.118 1.00 63.51 C ANISOU 883 CD1 ILE A 151 5273 12031 6827 185 -1233 -379 C ATOM 884 N THR A 152 21.337 -18.628 35.473 1.00 67.09 N ANISOU 884 N THR A 152 5724 12673 7096 503 -1248 -112 N ATOM 885 CA THR A 152 21.191 -18.703 36.930 1.00 67.88 C ANISOU 885 CA THR A 152 5790 12905 7095 498 -1297 -76 C ATOM 886 C THR A 152 21.877 -19.941 37.547 1.00 73.80 C ANISOU 886 C THR A 152 6521 13697 7822 583 -1336 56 C ATOM 887 O THR A 152 22.172 -19.906 38.737 1.00 74.62 O ANISOU 887 O THR A 152 6563 13954 7834 585 -1387 93 O ATOM 888 CB THR A 152 19.675 -18.629 37.312 1.00 76.49 C ANISOU 888 CB THR A 152 6940 13997 8125 446 -1280 -87 C ATOM 889 OG1 THR A 152 19.504 -17.791 38.450 1.00 81.05 O ANISOU 889 OG1 THR A 152 7456 14740 8598 414 -1320 -155 O ATOM 890 CG2 THR A 152 19.014 -20.002 37.566 1.00 73.98 C ANISOU 890 CG2 THR A 152 6686 13640 7785 456 -1275 54 C ATOM 891 N ASP A 153 22.126 -21.017 36.763 1.00 71.42 N ANISOU 891 N ASP A 153 6273 13264 7600 664 -1324 121 N ATOM 892 CA ASP A 153 22.686 -22.281 37.274 1.00 72.67 C ANISOU 892 CA ASP A 153 6443 13410 7756 768 -1381 252 C ATOM 893 C ASP A 153 23.568 -22.994 36.209 1.00 75.52 C ANISOU 893 C ASP A 153 6808 13669 8216 900 -1378 238 C ATOM 894 O ASP A 153 23.473 -24.211 36.039 1.00 76.31 O ANISOU 894 O ASP A 153 6999 13627 8369 988 -1412 318 O ATOM 895 CB ASP A 153 21.490 -23.179 37.683 1.00 75.26 C ANISOU 895 CB ASP A 153 6888 13645 8063 723 -1394 368 C ATOM 896 CG ASP A 153 21.748 -24.217 38.754 1.00 94.41 C ANISOU 896 CG ASP A 153 9332 16102 10437 769 -1476 540 C ATOM 897 OD1 ASP A 153 22.552 -23.938 39.675 1.00 98.88 O ANISOU 897 OD1 ASP A 153 9797 16849 10925 802 -1521 563 O ATOM 898 OD2 ASP A 153 21.074 -25.273 38.728 1.00100.60 O ANISOU 898 OD2 ASP A 153 10234 16739 11250 753 -1503 660 O ATOM 899 N ALA A 154 24.441 -22.231 35.529 1.00 70.23 N ANISOU 899 N ALA A 154 6036 13085 7564 911 -1348 136 N ATOM 900 CA ALA A 154 25.304 -22.647 34.412 1.00 69.88 C ANISOU 900 CA ALA A 154 5949 13019 7583 1026 -1331 86 C ATOM 901 C ALA A 154 26.050 -23.995 34.584 1.00 74.67 C ANISOU 901 C ALA A 154 6564 13589 8218 1222 -1398 153 C ATOM 902 O ALA A 154 26.085 -24.770 33.633 1.00 73.87 O ANISOU 902 O ALA A 154 6515 13362 8188 1330 -1389 117 O ATOM 903 CB ALA A 154 26.312 -21.555 34.102 1.00 70.49 C ANISOU 903 CB ALA A 154 5873 13283 7629 979 -1310 5 C ATOM 904 N VAL A 155 26.652 -24.274 35.749 1.00 73.18 N ANISOU 904 N VAL A 155 6323 13508 7972 1282 -1473 241 N ATOM 905 CA VAL A 155 27.406 -25.526 35.911 1.00 75.19 C ANISOU 905 CA VAL A 155 6591 13718 8259 1493 -1555 309 C ATOM 906 C VAL A 155 26.466 -26.733 36.019 1.00 79.83 C ANISOU 906 C VAL A 155 7378 14041 8913 1523 -1605 418 C ATOM 907 O VAL A 155 26.624 -27.686 35.253 1.00 79.96 O ANISOU 907 O VAL A 155 7472 13888 9021 1671 -1635 392 O ATOM 908 CB VAL A 155 28.456 -25.535 37.056 1.00 80.49 C ANISOU 908 CB VAL A 155 7136 14600 8846 1574 -1633 380 C ATOM 909 CG1 VAL A 155 29.859 -25.348 36.507 1.00 80.85 C ANISOU 909 CG1 VAL A 155 7001 14839 8877 1704 -1631 282 C ATOM 910 CG2 VAL A 155 28.147 -24.501 38.135 1.00 79.95 C ANISOU 910 CG2 VAL A 155 7010 14696 8672 1394 -1626 404 C ATOM 911 N GLU A 156 25.492 -26.687 36.948 1.00 76.71 N ANISOU 911 N GLU A 156 7060 13619 8466 1377 -1618 531 N ATOM 912 CA GLU A 156 24.536 -27.772 37.176 1.00 77.69 C ANISOU 912 CA GLU A 156 7366 13518 8634 1349 -1671 666 C ATOM 913 C GLU A 156 23.664 -28.033 35.935 1.00 79.68 C ANISOU 913 C GLU A 156 7736 13557 8982 1303 -1615 581 C ATOM 914 O GLU A 156 23.381 -29.195 35.637 1.00 81.25 O ANISOU 914 O GLU A 156 8083 13520 9268 1363 -1678 640 O ATOM 915 CB GLU A 156 23.652 -27.459 38.393 1.00 79.33 C ANISOU 915 CB GLU A 156 7585 13830 8728 1171 -1678 790 C ATOM 916 CG GLU A 156 23.053 -28.686 39.061 1.00 97.48 C ANISOU 916 CG GLU A 156 10034 15972 11033 1144 -1771 1000 C ATOM 917 CD GLU A 156 21.800 -28.416 39.875 1.00127.89 C ANISOU 917 CD GLU A 156 13909 19908 14774 924 -1745 1095 C ATOM 918 OE1 GLU A 156 20.728 -28.176 39.270 1.00118.24 O ANISOU 918 OE1 GLU A 156 12740 18613 13574 801 -1673 1028 O ATOM 919 OE2 GLU A 156 21.889 -28.470 41.123 1.00127.26 O ANISOU 919 OE2 GLU A 156 13785 19994 14573 881 -1799 1240 O ATOM 920 N TYR A 157 23.293 -26.966 35.193 1.00 72.37 N ANISOU 920 N TYR A 157 6748 12707 8043 1201 -1508 442 N ATOM 921 CA TYR A 157 22.442 -27.069 34.015 1.00 70.64 C ANISOU 921 CA TYR A 157 6618 12331 7893 1147 -1449 356 C ATOM 922 C TYR A 157 23.169 -27.539 32.744 1.00 75.90 C ANISOU 922 C TYR A 157 7279 12914 8647 1313 -1442 233 C ATOM 923 O TYR A 157 22.536 -28.223 31.941 1.00 76.58 O ANISOU 923 O TYR A 157 7483 12808 8806 1317 -1441 196 O ATOM 924 CB TYR A 157 21.712 -25.748 33.736 1.00 69.24 C ANISOU 924 CB TYR A 157 6383 12265 7662 985 -1351 270 C ATOM 925 CG TYR A 157 20.575 -25.879 32.742 1.00 68.83 C ANISOU 925 CG TYR A 157 6427 12070 7655 903 -1298 215 C ATOM 926 CD1 TYR A 157 20.541 -25.105 31.587 1.00 69.59 C ANISOU 926 CD1 TYR A 157 6475 12197 7768 884 -1220 82 C ATOM 927 CD2 TYR A 157 19.552 -26.805 32.939 1.00 69.48 C ANISOU 927 CD2 TYR A 157 6646 11995 7759 834 -1333 307 C ATOM 928 CE1 TYR A 157 19.487 -25.207 30.681 1.00 69.70 C ANISOU 928 CE1 TYR A 157 6567 12104 7811 813 -1174 32 C ATOM 929 CE2 TYR A 157 18.515 -26.944 32.021 1.00 69.34 C ANISOU 929 CE2 TYR A 157 6705 11865 7775 751 -1289 251 C ATOM 930 CZ TYR A 157 18.483 -26.141 30.891 1.00 72.61 C ANISOU 930 CZ TYR A 157 7062 12325 8200 751 -1208 107 C ATOM 931 OH TYR A 157 17.458 -26.273 29.982 1.00 65.70 O ANISOU 931 OH TYR A 157 6254 11362 7348 675 -1167 52 O ATOM 932 N SER A 158 24.459 -27.196 32.545 1.00 73.03 N ANISOU 932 N SER A 158 6769 12713 8264 1442 -1439 161 N ATOM 933 CA SER A 158 25.239 -27.610 31.359 1.00 73.32 C ANISOU 933 CA SER A 158 6762 12744 8355 1617 -1429 28 C ATOM 934 C SER A 158 25.101 -29.123 31.065 1.00 78.17 C ANISOU 934 C SER A 158 7536 13093 9072 1776 -1518 34 C ATOM 935 O SER A 158 24.903 -29.503 29.909 1.00 77.63 O ANISOU 935 O SER A 158 7513 12923 9059 1832 -1493 -89 O ATOM 936 CB SER A 158 26.716 -27.248 31.521 1.00 77.14 C ANISOU 936 CB SER A 158 7054 13473 8783 1746 -1441 -12 C ATOM 937 OG SER A 158 27.320 -27.913 32.618 1.00 86.01 O ANISOU 937 OG SER A 158 8180 14603 9897 1868 -1545 99 O ATOM 938 N ALA A 159 25.151 -29.962 32.131 1.00 75.64 N ANISOU 938 N ALA A 159 7310 12655 8774 1836 -1632 183 N ATOM 939 CA ALA A 159 25.030 -31.424 32.101 1.00 76.91 C ANISOU 939 CA ALA A 159 7654 12522 9046 1976 -1754 228 C ATOM 940 C ALA A 159 23.593 -31.912 31.807 1.00 79.23 C ANISOU 940 C ALA A 159 8144 12560 9402 1802 -1755 268 C ATOM 941 O ALA A 159 23.422 -33.043 31.344 1.00 81.11 O ANISOU 941 O ALA A 159 8539 12528 9749 1901 -1841 239 O ATOM 942 CB ALA A 159 25.490 -31.992 33.434 1.00 79.33 C ANISOU 942 CB ALA A 159 7996 12806 9340 2051 -1878 416 C ATOM 943 N LYS A 160 22.576 -31.074 32.081 1.00 71.83 N ANISOU 943 N LYS A 160 7191 11709 8391 1551 -1670 324 N ATOM 944 CA LYS A 160 21.163 -31.415 31.903 1.00 70.66 C ANISOU 944 CA LYS A 160 7192 11386 8271 1358 -1662 373 C ATOM 945 C LYS A 160 20.560 -30.900 30.564 1.00 73.11 C ANISOU 945 C LYS A 160 7479 11707 8591 1294 -1554 195 C ATOM 946 O LYS A 160 19.584 -31.487 30.079 1.00 73.29 O ANISOU 946 O LYS A 160 7636 11542 8667 1202 -1569 186 O ATOM 947 CB LYS A 160 20.342 -30.867 33.083 1.00 71.73 C ANISOU 947 CB LYS A 160 7309 11648 8299 1137 -1640 535 C ATOM 948 CG LYS A 160 20.700 -31.467 34.442 1.00 78.56 C ANISOU 948 CG LYS A 160 8215 12497 9135 1156 -1754 745 C ATOM 949 N ARG A 161 21.118 -29.804 29.990 1.00 66.88 N ANISOU 949 N ARG A 161 6522 11144 7744 1323 -1452 69 N ATOM 950 CA ARG A 161 20.659 -29.162 28.746 1.00 63.86 C ANISOU 950 CA ARG A 161 6095 10819 7351 1262 -1349 -78 C ATOM 951 C ARG A 161 20.999 -30.046 27.523 1.00 70.17 C ANISOU 951 C ARG A 161 6944 11487 8230 1426 -1374 -230 C ATOM 952 O ARG A 161 22.001 -29.813 26.839 1.00 70.82 O ANISOU 952 O ARG A 161 6902 11711 8296 1574 -1342 -353 O ATOM 953 CB ARG A 161 21.297 -27.766 28.621 1.00 57.78 C ANISOU 953 CB ARG A 161 5138 10319 6497 1241 -1261 -132 C ATOM 954 CG ARG A 161 20.438 -26.780 27.889 1.00 57.80 C ANISOU 954 CG ARG A 161 5110 10391 6458 1089 -1164 -195 C ATOM 955 CD ARG A 161 21.165 -26.062 26.789 1.00 59.67 C ANISOU 955 CD ARG A 161 5218 10786 6669 1141 -1096 -316 C ATOM 956 NE ARG A 161 21.880 -24.874 27.256 1.00 67.05 N ANISOU 956 NE ARG A 161 6012 11924 7538 1096 -1069 -290 N ATOM 957 CZ ARG A 161 21.414 -23.627 27.196 1.00 77.22 C ANISOU 957 CZ ARG A 161 7259 13300 8780 947 -1016 -285 C ATOM 958 NH1 ARG A 161 20.190 -23.388 26.744 1.00 48.51 N ANISOU 958 NH1 ARG A 161 3699 9588 5145 841 -980 -297 N ATOM 959 NH2 ARG A 161 22.167 -22.612 27.595 1.00 70.81 N ANISOU 959 NH2 ARG A 161 6333 12648 7923 905 -1011 -270 N ATOM 960 N THR A 162 20.156 -31.068 27.265 1.00 67.64 N ANISOU 960 N THR A 162 6800 10911 7990 1392 -1436 -225 N ATOM 961 CA THR A 162 20.337 -32.056 26.189 1.00 68.88 C ANISOU 961 CA THR A 162 7041 10897 8235 1546 -1485 -383 C ATOM 962 C THR A 162 19.128 -32.106 25.209 1.00 72.27 C ANISOU 962 C THR A 162 7542 11246 8671 1397 -1435 -470 C ATOM 963 O THR A 162 18.022 -31.719 25.605 1.00 69.67 O ANISOU 963 O THR A 162 7247 10921 8302 1173 -1400 -364 O ATOM 964 CB THR A 162 20.551 -33.457 26.808 1.00 78.83 C ANISOU 964 CB THR A 162 8481 11864 9608 1663 -1649 -304 C ATOM 965 OG1 THR A 162 19.368 -33.859 27.516 1.00 79.49 O ANISOU 965 OG1 THR A 162 8720 11768 9714 1437 -1698 -134 O ATOM 966 CG2 THR A 162 21.776 -33.529 27.713 1.00 76.56 C ANISOU 966 CG2 THR A 162 8122 11657 9312 1839 -1713 -222 C ATOM 967 N PRO A 163 19.300 -32.633 23.952 1.00 70.45 N ANISOU 967 N PRO A 163 7331 10957 8481 1523 -1440 -669 N ATOM 968 CA PRO A 163 18.154 -32.719 23.024 1.00 69.49 C ANISOU 968 CA PRO A 163 7272 10773 8357 1379 -1400 -756 C ATOM 969 C PRO A 163 17.041 -33.662 23.511 1.00 73.91 C ANISOU 969 C PRO A 163 8041 11045 8995 1216 -1496 -650 C ATOM 970 O PRO A 163 15.897 -33.503 23.085 1.00 72.08 O ANISOU 970 O PRO A 163 7837 10818 8732 1024 -1450 -657 O ATOM 971 CB PRO A 163 18.788 -33.229 21.723 1.00 72.50 C ANISOU 971 CB PRO A 163 7626 11157 8762 1590 -1409 -999 C ATOM 972 CG PRO A 163 20.029 -33.920 22.141 1.00 78.80 C ANISOU 972 CG PRO A 163 8432 11883 9623 1849 -1508 -1025 C ATOM 973 CD PRO A 163 20.537 -33.127 23.303 1.00 73.49 C ANISOU 973 CD PRO A 163 7656 11372 8895 1809 -1477 -841 C ATOM 974 N LYS A 164 17.368 -34.639 24.394 1.00 72.75 N ANISOU 974 N LYS A 164 8037 10659 8944 1282 -1635 -541 N ATOM 975 CA LYS A 164 16.375 -35.548 24.981 1.00 73.80 C ANISOU 975 CA LYS A 164 8374 10518 9148 1096 -1743 -397 C ATOM 976 C LYS A 164 15.499 -34.736 25.934 1.00 75.94 C ANISOU 976 C LYS A 164 8583 10958 9311 835 -1671 -192 C ATOM 977 O LYS A 164 14.278 -34.828 25.849 1.00 75.65 O ANISOU 977 O LYS A 164 8605 10885 9252 606 -1661 -145 O ATOM 978 CB LYS A 164 17.047 -36.734 25.696 1.00 78.81 C ANISOU 978 CB LYS A 164 9175 10862 9907 1241 -1921 -307 C ATOM 979 CG LYS A 164 16.077 -37.834 26.113 1.00 91.15 C ANISOU 979 CG LYS A 164 10976 12094 11562 1042 -2059 -162 C ATOM 980 N ARG A 165 16.137 -33.890 26.787 1.00 71.10 N ANISOU 980 N ARG A 165 7833 10561 8619 879 -1620 -93 N ATOM 981 CA ARG A 165 15.497 -32.965 27.733 1.00 69.08 C ANISOU 981 CA ARG A 165 7486 10518 8244 685 -1548 62 C ATOM 982 C ARG A 165 14.549 -32.017 26.983 1.00 69.44 C ANISOU 982 C ARG A 165 7435 10743 8205 545 -1421 -33 C ATOM 983 O ARG A 165 13.428 -31.807 27.436 1.00 68.26 O ANISOU 983 O ARG A 165 7290 10658 7988 336 -1398 64 O ATOM 984 CB ARG A 165 16.576 -32.165 28.515 1.00 69.61 C ANISOU 984 CB ARG A 165 7410 10788 8251 807 -1518 112 C ATOM 985 CG ARG A 165 16.073 -31.110 29.522 1.00 80.03 C ANISOU 985 CG ARG A 165 8618 12348 9441 647 -1450 232 C ATOM 986 CD ARG A 165 15.570 -31.721 30.823 1.00 96.58 C ANISOU 986 CD ARG A 165 10799 14389 11508 510 -1534 456 C ATOM 987 NE ARG A 165 15.576 -30.771 31.939 1.00110.51 N ANISOU 987 NE ARG A 165 12433 16413 13144 446 -1489 549 N ATOM 988 CZ ARG A 165 16.181 -30.988 33.105 1.00133.11 C ANISOU 988 CZ ARG A 165 15284 19318 15974 486 -1558 696 C ATOM 989 NH1 ARG A 165 16.833 -32.125 33.324 1.00124.62 N ANISOU 989 NH1 ARG A 165 14329 18029 14992 598 -1680 785 N ATOM 990 NH2 ARG A 165 16.134 -30.070 34.064 1.00121.31 N ANISOU 990 NH2 ARG A 165 13661 18081 14350 426 -1514 749 N ATOM 991 N ALA A 166 15.000 -31.476 25.830 1.00 64.90 N ANISOU 991 N ALA A 166 6769 10264 7625 666 -1345 -219 N ATOM 992 CA ALA A 166 14.242 -30.559 24.978 1.00 63.02 C ANISOU 992 CA ALA A 166 6440 10193 7312 572 -1235 -315 C ATOM 993 C ALA A 166 12.982 -31.230 24.419 1.00 69.22 C ANISOU 993 C ALA A 166 7332 10853 8115 415 -1256 -343 C ATOM 994 O ALA A 166 11.926 -30.604 24.406 1.00 67.93 O ANISOU 994 O ALA A 166 7117 10824 7868 253 -1195 -316 O ATOM 995 CB ALA A 166 15.119 -30.052 23.845 1.00 62.99 C ANISOU 995 CB ALA A 166 6331 10300 7302 737 -1173 -486 C ATOM 996 N ALA A 167 13.089 -32.511 24.002 1.00 68.64 N ANISOU 996 N ALA A 167 7407 10523 8150 464 -1356 -401 N ATOM 997 CA ALA A 167 11.988 -33.304 23.458 1.00 69.58 C ANISOU 997 CA ALA A 167 7646 10489 8301 308 -1400 -437 C ATOM 998 C ALA A 167 10.916 -33.556 24.513 1.00 75.65 C ANISOU 998 C ALA A 167 8477 11231 9035 56 -1440 -231 C ATOM 999 O ALA A 167 9.739 -33.323 24.242 1.00 74.60 O ANISOU 999 O ALA A 167 8316 11196 8831 -134 -1396 -232 O ATOM 1000 CB ALA A 167 12.511 -34.625 22.922 1.00 72.57 C ANISOU 1000 CB ALA A 167 8186 10567 8819 440 -1524 -550 C ATOM 1001 N VAL A 168 11.328 -33.991 25.720 1.00 75.19 N ANISOU 1001 N VAL A 168 8484 11078 9007 54 -1522 -51 N ATOM 1002 CA VAL A 168 10.441 -34.299 26.847 1.00 77.12 C ANISOU 1002 CA VAL A 168 8778 11324 9201 -188 -1569 174 C ATOM 1003 C VAL A 168 9.626 -33.046 27.241 1.00 82.74 C ANISOU 1003 C VAL A 168 9309 12384 9744 -320 -1443 216 C ATOM 1004 O VAL A 168 8.413 -33.154 27.472 1.00 83.26 O ANISOU 1004 O VAL A 168 9372 12528 9736 -553 -1438 296 O ATOM 1005 CB VAL A 168 11.235 -34.896 28.040 1.00 82.05 C ANISOU 1005 CB VAL A 168 9486 11817 9874 -127 -1678 362 C ATOM 1006 CG1 VAL A 168 10.386 -34.977 29.306 1.00 82.32 C ANISOU 1006 CG1 VAL A 168 9519 11953 9806 -381 -1704 614 C ATOM 1007 CG2 VAL A 168 11.785 -36.275 27.682 1.00 84.41 C ANISOU 1007 CG2 VAL A 168 9996 11728 10346 -19 -1835 333 C ATOM 1008 N MET A 169 10.277 -31.869 27.256 1.00 78.70 N ANISOU 1008 N MET A 169 8648 12080 9176 -171 -1348 147 N ATOM 1009 CA MET A 169 9.615 -30.605 27.572 1.00 77.33 C ANISOU 1009 CA MET A 169 8314 12208 8860 -248 -1244 152 C ATOM 1010 C MET A 169 8.632 -30.195 26.472 1.00 79.94 C ANISOU 1010 C MET A 169 8596 12631 9146 -323 -1174 21 C ATOM 1011 O MET A 169 7.583 -29.641 26.792 1.00 78.89 O ANISOU 1011 O MET A 169 8380 12695 8899 -463 -1130 60 O ATOM 1012 CB MET A 169 10.636 -29.495 27.806 1.00 78.53 C ANISOU 1012 CB MET A 169 8346 12507 8986 -74 -1186 105 C ATOM 1013 CG MET A 169 11.430 -29.680 29.069 1.00 83.59 C ANISOU 1013 CG MET A 169 8992 13146 9623 -26 -1243 245 C ATOM 1014 SD MET A 169 12.209 -28.138 29.584 1.00 87.03 S ANISOU 1014 SD MET A 169 9259 13830 9981 91 -1170 202 S ATOM 1015 CE MET A 169 11.028 -27.605 30.826 1.00 83.74 C ANISOU 1015 CE MET A 169 8764 13650 9405 -90 -1150 313 C ATOM 1016 N ILE A 170 8.961 -30.480 25.188 1.00 76.41 N ANISOU 1016 N ILE A 170 8188 12066 8777 -222 -1168 -139 N ATOM 1017 CA ILE A 170 8.112 -30.162 24.033 1.00 75.64 C ANISOU 1017 CA ILE A 170 8047 12055 8637 -278 -1109 -269 C ATOM 1018 C ILE A 170 6.867 -31.060 24.036 1.00 79.90 C ANISOU 1018 C ILE A 170 8666 12527 9164 -506 -1161 -220 C ATOM 1019 O ILE A 170 5.765 -30.562 23.789 1.00 79.21 O ANISOU 1019 O ILE A 170 8494 12629 8975 -629 -1107 -238 O ATOM 1020 CB ILE A 170 8.901 -30.244 22.686 1.00 79.11 C ANISOU 1020 CB ILE A 170 8495 12419 9145 -105 -1092 -452 C ATOM 1021 CG1 ILE A 170 10.017 -29.163 22.590 1.00 78.42 C ANISOU 1021 CG1 ILE A 170 8293 12463 9039 78 -1028 -491 C ATOM 1022 CG2 ILE A 170 7.983 -30.209 21.438 1.00 79.62 C ANISOU 1022 CG2 ILE A 170 8536 12550 9167 -177 -1053 -584 C ATOM 1023 CD1 ILE A 170 9.659 -27.736 23.108 1.00 86.80 C ANISOU 1023 CD1 ILE A 170 9225 13759 9996 42 -953 -436 C ATOM 1024 N ALA A 171 7.039 -32.365 24.331 1.00 77.22 N ANISOU 1024 N ALA A 171 8490 11923 8927 -564 -1275 -152 N ATOM 1025 CA ALA A 171 5.939 -33.332 24.398 1.00 78.07 C ANISOU 1025 CA ALA A 171 8696 11929 9037 -814 -1348 -82 C ATOM 1026 C ALA A 171 4.942 -32.924 25.479 1.00 80.05 C ANISOU 1026 C ALA A 171 8850 12420 9143 -1024 -1319 94 C ATOM 1027 O ALA A 171 3.746 -32.872 25.213 1.00 79.91 O ANISOU 1027 O ALA A 171 8773 12554 9034 -1210 -1292 86 O ATOM 1028 CB ALA A 171 6.481 -34.727 24.669 1.00 81.24 C ANISOU 1028 CB ALA A 171 9310 11968 9590 -819 -1497 -16 C ATOM 1029 N LEU A 172 5.447 -32.563 26.669 1.00 75.48 N ANISOU 1029 N LEU A 172 8230 11921 8526 -980 -1319 236 N ATOM 1030 CA LEU A 172 4.654 -32.095 27.808 1.00 74.84 C ANISOU 1030 CA LEU A 172 8033 12115 8287 -1140 -1288 391 C ATOM 1031 C LEU A 172 3.789 -30.882 27.408 1.00 75.34 C ANISOU 1031 C LEU A 172 7910 12506 8209 -1141 -1172 277 C ATOM 1032 O LEU A 172 2.610 -30.853 27.746 1.00 75.94 O ANISOU 1032 O LEU A 172 7903 12795 8155 -1337 -1157 341 O ATOM 1033 CB LEU A 172 5.599 -31.727 28.974 1.00 74.50 C ANISOU 1033 CB LEU A 172 7959 12117 8229 -1017 -1296 501 C ATOM 1034 CG LEU A 172 5.788 -32.718 30.148 1.00 81.55 C ANISOU 1034 CG LEU A 172 8962 12884 9140 -1136 -1408 738 C ATOM 1035 CD1 LEU A 172 5.969 -34.165 29.688 1.00 84.48 C ANISOU 1035 CD1 LEU A 172 9556 12867 9673 -1203 -1539 779 C ATOM 1036 CD2 LEU A 172 6.984 -32.332 30.975 1.00 82.23 C ANISOU 1036 CD2 LEU A 172 9025 12975 9242 -943 -1417 786 C ATOM 1037 N VAL A 173 4.366 -29.917 26.656 1.00 67.97 N ANISOU 1037 N VAL A 173 6912 11613 7300 -925 -1099 113 N ATOM 1038 CA VAL A 173 3.694 -28.704 26.186 1.00 65.74 C ANISOU 1038 CA VAL A 173 6476 11594 6909 -882 -1007 1 C ATOM 1039 C VAL A 173 2.520 -29.087 25.282 1.00 70.45 C ANISOU 1039 C VAL A 173 7062 12241 7465 -1031 -1001 -65 C ATOM 1040 O VAL A 173 1.432 -28.547 25.457 1.00 71.23 O ANISOU 1040 O VAL A 173 7032 12609 7424 -1118 -959 -66 O ATOM 1041 CB VAL A 173 4.693 -27.733 25.488 1.00 67.55 C ANISOU 1041 CB VAL A 173 6670 11802 7193 -640 -955 -129 C ATOM 1042 CG1 VAL A 173 3.997 -26.782 24.506 1.00 66.36 C ANISOU 1042 CG1 VAL A 173 6419 11818 6976 -599 -887 -259 C ATOM 1043 CG2 VAL A 173 5.494 -26.947 26.515 1.00 66.10 C ANISOU 1043 CG2 VAL A 173 6430 11698 6987 -528 -944 -75 C ATOM 1044 N TRP A 174 2.727 -30.040 24.358 1.00 67.09 N ANISOU 1044 N TRP A 174 6766 11573 7153 -1056 -1049 -129 N ATOM 1045 CA TRP A 174 1.700 -30.508 23.421 1.00 67.12 C ANISOU 1045 CA TRP A 174 6772 11603 7128 -1204 -1056 -208 C ATOM 1046 C TRP A 174 0.627 -31.345 24.104 1.00 73.64 C ANISOU 1046 C TRP A 174 7614 12480 7886 -1499 -1113 -66 C ATOM 1047 O TRP A 174 -0.533 -31.224 23.730 1.00 74.11 O ANISOU 1047 O TRP A 174 7577 12747 7835 -1642 -1086 -101 O ATOM 1048 CB TRP A 174 2.329 -31.291 22.269 1.00 65.92 C ANISOU 1048 CB TRP A 174 6757 11174 7117 -1128 -1101 -342 C ATOM 1049 CG TRP A 174 2.821 -30.407 21.157 1.00 64.89 C ANISOU 1049 CG TRP A 174 6552 11120 6984 -916 -1025 -509 C ATOM 1050 CD1 TRP A 174 4.117 -30.094 20.866 1.00 66.84 C ANISOU 1050 CD1 TRP A 174 6816 11272 7308 -692 -1008 -569 C ATOM 1051 CD2 TRP A 174 2.013 -29.684 20.221 1.00 63.76 C ANISOU 1051 CD2 TRP A 174 6289 11196 6740 -919 -959 -616 C ATOM 1052 NE1 TRP A 174 4.169 -29.251 19.783 1.00 64.89 N ANISOU 1052 NE1 TRP A 174 6476 11165 7015 -576 -936 -697 N ATOM 1053 CE2 TRP A 174 2.890 -28.983 19.364 1.00 66.40 C ANISOU 1053 CE2 TRP A 174 6589 11539 7101 -704 -909 -726 C ATOM 1054 CE3 TRP A 174 0.630 -29.610 19.979 1.00 65.26 C ANISOU 1054 CE3 TRP A 174 6396 11588 6814 -1089 -945 -628 C ATOM 1055 CZ2 TRP A 174 2.427 -28.220 18.281 1.00 64.81 C ANISOU 1055 CZ2 TRP A 174 6285 11521 6817 -655 -850 -830 C ATOM 1056 CZ3 TRP A 174 0.174 -28.828 18.930 1.00 65.74 C ANISOU 1056 CZ3 TRP A 174 6348 11837 6795 -1018 -885 -745 C ATOM 1057 CH2 TRP A 174 1.065 -28.133 18.104 1.00 65.14 C ANISOU 1057 CH2 TRP A 174 6253 11747 6751 -803 -841 -837 C ATOM 1058 N VAL A 175 1.004 -32.185 25.094 1.00 72.27 N ANISOU 1058 N VAL A 175 7554 12136 7768 -1597 -1196 104 N ATOM 1059 CA VAL A 175 0.073 -33.017 25.870 1.00 74.60 C ANISOU 1059 CA VAL A 175 7871 12479 7994 -1908 -1263 286 C ATOM 1060 C VAL A 175 -0.812 -32.083 26.714 1.00 78.64 C ANISOU 1060 C VAL A 175 8162 13427 8290 -1981 -1182 357 C ATOM 1061 O VAL A 175 -2.018 -32.297 26.782 1.00 79.77 O ANISOU 1061 O VAL A 175 8218 13787 8306 -2218 -1181 404 O ATOM 1062 CB VAL A 175 0.803 -34.103 26.724 1.00 79.99 C ANISOU 1062 CB VAL A 175 8741 12857 8794 -1972 -1384 471 C ATOM 1063 CG1 VAL A 175 -0.114 -34.707 27.787 1.00 81.70 C ANISOU 1063 CG1 VAL A 175 8943 13204 8896 -2301 -1441 714 C ATOM 1064 CG2 VAL A 175 1.374 -35.205 25.834 1.00 81.07 C ANISOU 1064 CG2 VAL A 175 9103 12565 9134 -1937 -1490 383 C ATOM 1065 N PHE A 176 -0.221 -31.026 27.301 1.00 74.19 N ANISOU 1065 N PHE A 176 7500 13008 7680 -1771 -1118 343 N ATOM 1066 CA PHE A 176 -0.944 -30.025 28.079 1.00 73.99 C ANISOU 1066 CA PHE A 176 7264 13392 7456 -1776 -1047 363 C ATOM 1067 C PHE A 176 -1.833 -29.182 27.171 1.00 77.64 C ANISOU 1067 C PHE A 176 7583 14089 7827 -1722 -973 192 C ATOM 1068 O PHE A 176 -2.930 -28.798 27.582 1.00 78.57 O ANISOU 1068 O PHE A 176 7530 14561 7763 -1824 -938 207 O ATOM 1069 CB PHE A 176 0.013 -29.115 28.873 1.00 74.69 C ANISOU 1069 CB PHE A 176 7308 13527 7542 -1550 -1015 362 C ATOM 1070 CG PHE A 176 -0.705 -28.090 29.724 1.00 76.76 C ANISOU 1070 CG PHE A 176 7361 14203 7602 -1530 -956 353 C ATOM 1071 CD1 PHE A 176 -0.542 -26.731 29.488 1.00 78.59 C ANISOU 1071 CD1 PHE A 176 7491 14562 7807 -1292 -893 189 C ATOM 1072 CD2 PHE A 176 -1.603 -28.485 30.717 1.00 81.06 C ANISOU 1072 CD2 PHE A 176 7805 15021 7974 -1755 -970 502 C ATOM 1073 CE1 PHE A 176 -1.233 -25.782 30.257 1.00 79.86 C ANISOU 1073 CE1 PHE A 176 7466 15093 7786 -1246 -854 149 C ATOM 1074 CE2 PHE A 176 -2.300 -27.537 31.475 1.00 83.97 C ANISOU 1074 CE2 PHE A 176 7959 15810 8137 -1714 -916 462 C ATOM 1075 CZ PHE A 176 -2.104 -26.192 31.248 1.00 80.47 C ANISOU 1075 CZ PHE A 176 7428 15464 7682 -1445 -862 273 C ATOM 1076 N SER A 177 -1.366 -28.907 25.938 1.00 72.36 N ANISOU 1076 N SER A 177 6974 13247 7273 -1557 -952 32 N ATOM 1077 CA SER A 177 -2.110 -28.132 24.949 1.00 71.19 C ANISOU 1077 CA SER A 177 6709 13287 7052 -1487 -894 -122 C ATOM 1078 C SER A 177 -3.379 -28.859 24.500 1.00 76.91 C ANISOU 1078 C SER A 177 7392 14137 7692 -1740 -914 -117 C ATOM 1079 O SER A 177 -4.443 -28.245 24.503 1.00 76.67 O ANISOU 1079 O SER A 177 7185 14445 7501 -1768 -871 -160 O ATOM 1080 CB SER A 177 -1.228 -27.814 23.751 1.00 72.27 C ANISOU 1080 CB SER A 177 6929 13207 7325 -1280 -877 -263 C ATOM 1081 OG SER A 177 -0.216 -26.907 24.148 1.00 77.49 O ANISOU 1081 OG SER A 177 7580 13836 8026 -1059 -848 -276 O ATOM 1082 N ILE A 178 -3.278 -30.165 24.159 1.00 75.58 N ANISOU 1082 N ILE A 178 7383 13704 7630 -1923 -989 -70 N ATOM 1083 CA ILE A 178 -4.417 -30.977 23.718 1.00 78.03 C ANISOU 1083 CA ILE A 178 7679 14092 7879 -2202 -1027 -62 C ATOM 1084 C ILE A 178 -5.395 -31.177 24.885 1.00 85.70 C ANISOU 1084 C ILE A 178 8524 15361 8675 -2457 -1037 112 C ATOM 1085 O ILE A 178 -6.605 -31.178 24.655 1.00 86.42 O ANISOU 1085 O ILE A 178 8476 15740 8620 -2635 -1022 96 O ATOM 1086 CB ILE A 178 -4.017 -32.323 23.028 1.00 82.79 C ANISOU 1086 CB ILE A 178 8507 14292 8658 -2323 -1125 -81 C ATOM 1087 CG1 ILE A 178 -3.274 -33.298 23.966 1.00 85.04 C ANISOU 1087 CG1 ILE A 178 8977 14269 9064 -2414 -1222 96 C ATOM 1088 CG2 ILE A 178 -3.204 -32.081 21.753 1.00 81.88 C ANISOU 1088 CG2 ILE A 178 8465 13979 8667 -2072 -1104 -282 C ATOM 1089 CD1 ILE A 178 -4.089 -34.518 24.421 1.00 94.41 C ANISOU 1089 CD1 ILE A 178 10241 15398 10231 -2795 -1326 261 C ATOM 1090 N SER A 179 -4.875 -31.274 26.136 1.00 83.67 N ANISOU 1090 N SER A 179 8294 15085 8413 -2464 -1056 273 N ATOM 1091 CA SER A 179 -5.679 -31.458 27.347 1.00 85.74 C ANISOU 1091 CA SER A 179 8426 15660 8490 -2701 -1064 456 C ATOM 1092 C SER A 179 -6.583 -30.248 27.640 1.00 90.76 C ANISOU 1092 C SER A 179 8782 16806 8898 -2608 -969 373 C ATOM 1093 O SER A 179 -7.594 -30.418 28.315 1.00 92.44 O ANISOU 1093 O SER A 179 8834 17375 8913 -2831 -965 480 O ATOM 1094 CB SER A 179 -4.789 -31.745 28.555 1.00 89.20 C ANISOU 1094 CB SER A 179 8958 15960 8975 -2690 -1107 636 C ATOM 1095 OG SER A 179 -4.265 -30.569 29.153 1.00 95.93 O ANISOU 1095 OG SER A 179 9699 16982 9769 -2420 -1036 579 O ATOM 1096 N ILE A 180 -6.203 -29.039 27.171 1.00 86.11 N ANISOU 1096 N ILE A 180 8133 16255 8329 -2282 -902 191 N ATOM 1097 CA ILE A 180 -6.969 -27.805 27.384 1.00 86.05 C ANISOU 1097 CA ILE A 180 7885 16678 8132 -2134 -832 83 C ATOM 1098 C ILE A 180 -8.196 -27.786 26.461 1.00 91.46 C ANISOU 1098 C ILE A 180 8440 17603 8708 -2232 -813 -15 C ATOM 1099 O ILE A 180 -9.262 -27.364 26.890 1.00 91.72 O ANISOU 1099 O ILE A 180 8249 18076 8525 -2284 -783 -27 O ATOM 1100 CB ILE A 180 -6.075 -26.531 27.195 1.00 87.01 C ANISOU 1100 CB ILE A 180 8022 16700 8337 -1759 -792 -60 C ATOM 1101 CG1 ILE A 180 -4.972 -26.396 28.293 1.00 86.94 C ANISOU 1101 CG1 ILE A 180 8089 16555 8390 -1663 -806 29 C ATOM 1102 CG2 ILE A 180 -6.897 -25.226 27.048 1.00 87.31 C ANISOU 1102 CG2 ILE A 180 7850 17103 8221 -1566 -742 -213 C ATOM 1103 CD1 ILE A 180 -5.399 -25.892 29.693 1.00 93.09 C ANISOU 1103 CD1 ILE A 180 8691 17709 8969 -1669 -789 84 C ATOM 1104 N SER A 181 -8.045 -28.224 25.206 1.00 89.24 N ANISOU 1104 N SER A 181 8284 17062 8561 -2246 -834 -96 N ATOM 1105 CA SER A 181 -9.126 -28.203 24.221 1.00 90.56 C ANISOU 1105 CA SER A 181 8336 17439 8633 -2326 -821 -202 C ATOM 1106 C SER A 181 -10.032 -29.447 24.267 1.00 99.27 C ANISOU 1106 C SER A 181 9427 18627 9664 -2729 -874 -93 C ATOM 1107 O SER A 181 -11.085 -29.443 23.625 1.00100.33 O ANISOU 1107 O SER A 181 9422 19023 9676 -2835 -864 -167 O ATOM 1108 CB SER A 181 -8.545 -28.064 22.819 1.00 92.53 C ANISOU 1108 CB SER A 181 8714 17403 9042 -2155 -820 -349 C ATOM 1109 OG SER A 181 -8.028 -29.302 22.360 1.00102.23 O ANISOU 1109 OG SER A 181 10151 18260 10432 -2326 -885 -313 O ATOM 1110 N LEU A 182 -9.611 -30.515 24.962 1.00 98.56 N ANISOU 1110 N LEU A 182 9490 18303 9655 -2957 -940 85 N ATOM 1111 CA LEU A 182 -10.357 -31.771 25.025 1.00102.05 C ANISOU 1111 CA LEU A 182 9965 18750 10060 -3371 -1014 215 C ATOM 1112 C LEU A 182 -11.630 -31.687 25.911 1.00111.55 C ANISOU 1112 C LEU A 182 10901 20502 10981 -3612 -989 330 C ATOM 1113 O LEU A 182 -12.654 -32.216 25.464 1.00113.06 O ANISOU 1113 O LEU A 182 11002 20887 11070 -3881 -1012 329 O ATOM 1114 CB LEU A 182 -9.444 -32.930 25.473 1.00102.91 C ANISOU 1114 CB LEU A 182 10349 18390 10362 -3521 -1114 382 C ATOM 1115 CG LEU A 182 -8.903 -33.911 24.392 1.00107.89 C ANISOU 1115 CG LEU A 182 11245 18518 11229 -3564 -1202 303 C ATOM 1116 CD1 LEU A 182 -9.743 -35.163 24.306 1.00111.40 C ANISOU 1116 CD1 LEU A 182 11753 18915 11660 -3995 -1304 406 C ATOM 1117 CD2 LEU A 182 -8.752 -33.265 23.006 1.00108.12 C ANISOU 1117 CD2 LEU A 182 11258 18504 11317 -3291 -1146 44 C ATOM 1118 N PRO A 183 -11.649 -31.025 27.108 1.00110.65 N ANISOU 1118 N PRO A 183 10636 20687 10718 -3527 -942 411 N ATOM 1119 CA PRO A 183 -12.890 -30.990 27.904 1.00113.74 C ANISOU 1119 CA PRO A 183 10748 21651 10816 -3762 -918 507 C ATOM 1120 C PRO A 183 -14.128 -30.358 27.224 1.00120.90 C ANISOU 1120 C PRO A 183 11387 23023 11527 -3725 -863 337 C ATOM 1121 O PRO A 183 -15.188 -30.942 27.447 1.00122.92 O ANISOU 1121 O PRO A 183 11485 23620 11597 -4070 -880 438 O ATOM 1122 CB PRO A 183 -12.492 -30.195 29.153 1.00114.64 C ANISOU 1122 CB PRO A 183 10755 21977 10824 -3565 -871 552 C ATOM 1123 CG PRO A 183 -11.023 -30.361 29.255 1.00117.07 C ANISOU 1123 CG PRO A 183 11343 21750 11389 -3402 -907 592 C ATOM 1124 CD PRO A 183 -10.554 -30.351 27.837 1.00110.70 C ANISOU 1124 CD PRO A 183 10709 20551 10801 -3241 -917 422 C ATOM 1125 N PRO A 184 -14.100 -29.262 26.400 1.00118.00 N ANISOU 1125 N PRO A 184 10955 22699 11180 -3358 -808 105 N ATOM 1126 CA PRO A 184 -15.362 -28.744 25.836 1.00119.94 C ANISOU 1126 CA PRO A 184 10932 23421 11218 -3341 -771 -31 C ATOM 1127 C PRO A 184 -15.946 -29.638 24.735 1.00129.88 C ANISOU 1127 C PRO A 184 12237 24601 12511 -3617 -816 -50 C ATOM 1128 O PRO A 184 -16.224 -29.184 23.619 1.00128.96 O ANISOU 1128 O PRO A 184 12076 24521 12403 -3454 -799 -224 O ATOM 1129 CB PRO A 184 -14.972 -27.359 25.313 1.00118.72 C ANISOU 1129 CB PRO A 184 10753 23238 11115 -2861 -723 -242 C ATOM 1130 CG PRO A 184 -13.561 -27.493 24.954 1.00120.57 C ANISOU 1130 CG PRO A 184 11292 22881 11636 -2719 -745 -238 C ATOM 1131 CD PRO A 184 -12.971 -28.397 26.003 1.00116.79 C ANISOU 1131 CD PRO A 184 10949 22209 11217 -2949 -783 -29 C ATOM 1132 N PHE A 185 -16.151 -30.918 25.075 1.00131.87 N ANISOU 1132 N PHE A 185 12580 24749 12775 -4048 -884 137 N ATOM 1133 CA PHE A 185 -16.740 -31.915 24.200 1.00134.98 C ANISOU 1133 CA PHE A 185 13027 25061 13196 -4381 -948 138 C ATOM 1134 C PHE A 185 -18.062 -32.372 24.809 1.00146.62 C ANISOU 1134 C PHE A 185 14242 27076 14392 -4784 -957 272 C ATOM 1135 O PHE A 185 -18.490 -33.511 24.608 1.00148.97 O ANISOU 1135 O PHE A 185 14616 27282 14706 -5210 -1038 388 O ATOM 1136 CB PHE A 185 -15.760 -33.066 23.918 1.00136.74 C ANISOU 1136 CB PHE A 185 13619 24628 13707 -4539 -1045 223 C ATOM 1137 CG PHE A 185 -15.095 -32.923 22.567 1.00136.26 C ANISOU 1137 CG PHE A 185 13737 24180 13856 -4287 -1052 14 C ATOM 1138 CD1 PHE A 185 -14.240 -31.858 22.301 1.00136.06 C ANISOU 1138 CD1 PHE A 185 13744 24032 13921 -3835 -985 -121 C ATOM 1139 CD2 PHE A 185 -15.340 -33.841 21.553 1.00139.97 C ANISOU 1139 CD2 PHE A 185 14333 24429 14419 -4514 -1129 -51 C ATOM 1140 CE1 PHE A 185 -13.650 -31.711 21.043 1.00135.28 C ANISOU 1140 CE1 PHE A 185 13784 23630 13984 -3621 -987 -299 C ATOM 1141 CE2 PHE A 185 -14.746 -33.694 20.295 1.00140.95 C ANISOU 1141 CE2 PHE A 185 14597 24252 14707 -4277 -1130 -255 C ATOM 1142 CZ PHE A 185 -13.903 -32.632 20.050 1.00135.87 C ANISOU 1142 CZ PHE A 185 13968 23522 14134 -3835 -1056 -368 C ATOM 1143 N PHE A 186 -18.735 -31.433 25.519 1.00146.82 N ANISOU 1143 N PHE A 186 13946 27688 14152 -4638 -877 241 N ATOM 1144 CA PHE A 186 -20.048 -31.621 26.144 1.00151.54 C ANISOU 1144 CA PHE A 186 14215 28937 14425 -4954 -863 338 C ATOM 1145 C PHE A 186 -21.183 -31.291 25.132 1.00161.33 C ANISOU 1145 C PHE A 186 15216 30575 15506 -4947 -841 155 C ATOM 1146 O PHE A 186 -22.358 -31.281 25.516 1.00163.29 O ANISOU 1146 O PHE A 186 15140 31446 15456 -5153 -819 189 O ATOM 1147 CB PHE A 186 -20.213 -30.749 27.421 1.00153.27 C ANISOU 1147 CB PHE A 186 14183 29637 14415 -4767 -790 365 C ATOM 1148 CG PHE A 186 -18.994 -30.312 28.210 1.00152.41 C ANISOU 1148 CG PHE A 186 14245 29214 14448 -4487 -774 404 C ATOM 1149 CD1 PHE A 186 -18.486 -29.023 28.082 1.00152.51 C ANISOU 1149 CD1 PHE A 186 14238 29197 14511 -3971 -717 195 C ATOM 1150 CD2 PHE A 186 -18.423 -31.152 29.160 1.00155.24 C ANISOU 1150 CD2 PHE A 186 14763 29354 14866 -4750 -822 658 C ATOM 1151 CE1 PHE A 186 -17.392 -28.600 28.850 1.00151.29 C ANISOU 1151 CE1 PHE A 186 14223 28787 14472 -3733 -706 224 C ATOM 1152 CE2 PHE A 186 -17.326 -30.730 29.924 1.00156.01 C ANISOU 1152 CE2 PHE A 186 14994 29211 15073 -4491 -808 690 C ATOM 1153 CZ PHE A 186 -16.821 -29.456 29.764 1.00151.21 C ANISOU 1153 CZ PHE A 186 14359 28579 14514 -3990 -748 466 C ATOM 1154 N TRP A 187 -20.824 -31.030 23.843 1.00160.90 N ANISOU 1154 N TRP A 187 15310 30189 15636 -4713 -849 -35 N ATOM 1155 CA TRP A 187 -21.733 -30.650 22.751 1.00163.62 C ANISOU 1155 CA TRP A 187 15464 30844 15862 -4644 -834 -222 C ATOM 1156 C TRP A 187 -22.703 -31.799 22.345 1.00173.45 C ANISOU 1156 C TRP A 187 16636 32262 17004 -5171 -899 -147 C ATOM 1157 O TRP A 187 -22.729 -32.237 21.188 1.00173.34 O ANISOU 1157 O TRP A 187 16737 32022 17102 -5245 -945 -253 O ATOM 1158 CB TRP A 187 -20.954 -30.098 21.525 1.00160.11 C ANISOU 1158 CB TRP A 187 15220 29969 15646 -4263 -831 -416 C ATOM 1159 CG TRP A 187 -19.922 -31.018 20.934 1.00160.67 C ANISOU 1159 CG TRP A 187 15668 29359 16021 -4382 -897 -384 C ATOM 1160 CD1 TRP A 187 -18.706 -31.328 21.462 1.00162.39 C ANISOU 1160 CD1 TRP A 187 16163 29076 16461 -4332 -919 -281 C ATOM 1161 CD2 TRP A 187 -19.975 -31.659 19.650 1.00161.27 C ANISOU 1161 CD2 TRP A 187 15873 29194 16210 -4513 -953 -488 C ATOM 1162 NE1 TRP A 187 -18.023 -32.173 20.620 1.00161.71 N ANISOU 1162 NE1 TRP A 187 16369 28457 16617 -4430 -989 -312 N ATOM 1163 CE2 TRP A 187 -18.776 -32.391 19.498 1.00164.34 C ANISOU 1163 CE2 TRP A 187 16621 28934 16888 -4542 -1011 -446 C ATOM 1164 CE3 TRP A 187 -20.933 -31.709 18.621 1.00164.05 C ANISOU 1164 CE3 TRP A 187 16062 29835 16434 -4608 -965 -622 C ATOM 1165 CZ2 TRP A 187 -18.508 -33.163 18.362 1.00164.25 C ANISOU 1165 CZ2 TRP A 187 16812 28555 17042 -4654 -1081 -549 C ATOM 1166 CZ3 TRP A 187 -20.663 -32.471 17.493 1.00165.97 C ANISOU 1166 CZ3 TRP A 187 16508 29715 16840 -4736 -1031 -715 C ATOM 1167 CH2 TRP A 187 -19.473 -33.202 17.381 1.00165.79 C ANISOU 1167 CH2 TRP A 187 16844 29047 17103 -4761 -1090 -684 C ATOM 1168 N ARG A 188 -23.559 -32.221 23.296 1.00173.07 N ANISOU 1168 N ARG A 188 16367 32676 16716 -5538 -903 26 N ATOM 1169 CA ARG A 188 -24.566 -33.258 23.078 1.00176.48 C ANISOU 1169 CA ARG A 188 16691 33352 17012 -6083 -967 125 C ATOM 1170 C ARG A 188 -25.804 -32.622 22.421 1.00178.97 C ANISOU 1170 C ARG A 188 16952 33557 17490 -5635 -917 -71 C ATOM 1171 O ARG A 188 -26.874 -32.532 23.032 1.00179.13 O ANISOU 1171 O ARG A 188 16825 33771 17464 -5602 -883 -24 O ATOM 1172 CB ARG A 188 -24.910 -33.969 24.399 1.00178.07 C ANISOU 1172 CB ARG A 188 16934 33483 17243 -6351 -985 394 C ATOM 1173 N GLN A 189 -25.629 -32.151 21.169 1.00176.89 N ANISOU 1173 N GLN A 189 16515 33683 17011 -5618 -919 -281 N ATOM 1174 CA GLN A 189 -26.660 -31.488 20.367 1.00175.89 C ANISOU 1174 CA GLN A 189 16281 33623 16926 -5271 -890 -461 C ATOM 1175 C GLN A 189 -26.466 -31.762 18.872 1.00178.89 C ANISOU 1175 C GLN A 189 16904 33503 17564 -5171 -943 -606 C ATOM 1176 O GLN A 189 -27.452 -31.815 18.130 1.00178.86 O ANISOU 1176 O GLN A 189 16765 33700 17495 -5213 -961 -695 O ATOM 1177 CB GLN A 189 -26.650 -29.974 20.628 1.00175.77 C ANISOU 1177 CB GLN A 189 16044 33991 16748 -4757 -807 -598 C ATOM 1178 N ALA A 190 -25.199 -31.918 18.433 1.00176.68 N ANISOU 1178 N ALA A 190 16663 33302 17167 -5351 -962 -658 N ATOM 1179 CA ALA A 190 -24.844 -32.197 17.040 1.00210.39 C ANISOU 1179 CA ALA A 190 22041 35076 22821 -4305 -1038 -715 C ATOM 1180 C ALA A 190 -23.935 -33.425 16.922 1.00239.70 C ANISOU 1180 C ALA A 190 26887 36237 27952 -3488 -1144 -591 C ATOM 1181 O ALA A 190 -23.479 -33.972 17.927 1.00210.75 O ANISOU 1181 O ALA A 190 22340 34773 22962 -4902 -1131 -522 O ATOM 1182 CB ALA A 190 -24.166 -30.988 16.421 1.00209.90 C ANISOU 1182 CB ALA A 190 21862 35307 22583 -4005 -981 -863 C ATOM 1183 N SER A 197 -24.097 -22.564 10.937 1.00 96.35 N ANISOU 1183 N SER A 197 6263 23282 7063 -1556 -865 -1793 N ATOM 1184 CA SER A 197 -23.993 -21.137 10.630 1.00 95.52 C ANISOU 1184 CA SER A 197 6131 23212 6952 -1072 -891 -1824 C ATOM 1185 C SER A 197 -23.010 -20.404 11.563 1.00 97.94 C ANISOU 1185 C SER A 197 6614 23168 7429 -818 -877 -1766 C ATOM 1186 O SER A 197 -22.440 -19.384 11.171 1.00 96.35 O ANISOU 1186 O SER A 197 6526 22758 7326 -467 -907 -1764 O ATOM 1187 CB SER A 197 -25.362 -20.473 10.711 1.00101.16 C ANISOU 1187 CB SER A 197 6494 24553 7389 -905 -920 -1900 C ATOM 1188 N GLU A 198 -22.834 -20.907 12.797 1.00 94.50 N ANISOU 1188 N GLU A 198 6197 22686 7021 -1005 -839 -1711 N ATOM 1189 CA GLU A 198 -21.931 -20.335 13.802 1.00 92.25 C ANISOU 1189 CA GLU A 198 6064 22103 6883 -811 -825 -1662 C ATOM 1190 C GLU A 198 -20.994 -21.396 14.341 1.00 93.32 C ANISOU 1190 C GLU A 198 6427 21833 7197 -1121 -787 -1564 C ATOM 1191 O GLU A 198 -21.419 -22.530 14.593 1.00 93.53 O ANISOU 1191 O GLU A 198 6400 21975 7160 -1506 -774 -1526 O ATOM 1192 CB GLU A 198 -22.719 -19.698 14.958 1.00 95.24 C ANISOU 1192 CB GLU A 198 6197 22912 7076 -660 -825 -1704 C ATOM 1193 N CYS A 199 -19.717 -21.020 14.523 1.00 87.02 N ANISOU 1193 N CYS A 199 5883 20560 6622 -954 -782 -1518 N ATOM 1194 CA CYS A 199 -18.666 -21.898 15.032 1.00 85.00 C ANISOU 1194 CA CYS A 199 5862 19879 6555 -1177 -756 -1427 C ATOM 1195 C CYS A 199 -17.874 -21.160 16.128 1.00 86.91 C ANISOU 1195 C CYS A 199 6199 19926 6899 -960 -745 -1385 C ATOM 1196 O CYS A 199 -17.059 -20.284 15.839 1.00 84.59 O ANISOU 1196 O CYS A 199 6048 19351 6743 -679 -759 -1394 O ATOM 1197 CB CYS A 199 -17.775 -22.371 13.888 1.00 83.72 C ANISOU 1197 CB CYS A 199 5927 19312 6572 -1230 -762 -1429 C ATOM 1198 SG CYS A 199 -16.534 -23.608 14.351 1.00 86.49 S ANISOU 1198 SG CYS A 199 6563 19147 7153 -1500 -748 -1340 S ATOM 1199 N VAL A 200 -18.200 -21.467 17.394 1.00 84.12 N ANISOU 1199 N VAL A 200 5741 19767 6453 -1098 -726 -1340 N ATOM 1200 CA VAL A 200 -17.610 -20.861 18.596 1.00 82.78 C ANISOU 1200 CA VAL A 200 5617 19501 6334 -929 -716 -1312 C ATOM 1201 C VAL A 200 -17.392 -21.957 19.659 1.00 88.46 C ANISOU 1201 C VAL A 200 6376 20175 7059 -1270 -690 -1190 C ATOM 1202 O VAL A 200 -18.134 -22.950 19.668 1.00 89.73 O ANISOU 1202 O VAL A 200 6435 20551 7107 -1610 -686 -1142 O ATOM 1203 CB VAL A 200 -18.447 -19.670 19.151 1.00 86.91 C ANISOU 1203 CB VAL A 200 5902 20446 6672 -619 -734 -1416 C ATOM 1204 CG1 VAL A 200 -18.192 -18.387 18.363 1.00 85.49 C ANISOU 1204 CG1 VAL A 200 5788 20123 6572 -214 -782 -1502 C ATOM 1205 CG2 VAL A 200 -19.934 -19.993 19.185 1.00 89.23 C ANISOU 1205 CG2 VAL A 200 5881 21332 6689 -766 -729 -1462 C ATOM 1206 N VAL A 201 -16.363 -21.795 20.533 1.00 84.62 N ANISOU 1206 N VAL A 201 6044 19400 6707 -1193 -682 -1129 N ATOM 1207 CA VAL A 201 -16.051 -22.810 21.555 1.00 85.37 C ANISOU 1207 CA VAL A 201 6198 19419 6818 -1496 -668 -991 C ATOM 1208 C VAL A 201 -17.119 -22.781 22.672 1.00 92.91 C ANISOU 1208 C VAL A 201 6870 20923 7507 -1597 -651 -975 C ATOM 1209 O VAL A 201 -17.694 -21.723 22.967 1.00 92.61 O ANISOU 1209 O VAL A 201 6638 21227 7322 -1319 -649 -1092 O ATOM 1210 CB VAL A 201 -14.592 -22.782 22.125 1.00 86.76 C ANISOU 1210 CB VAL A 201 6623 19129 7212 -1410 -667 -919 C ATOM 1211 CG1 VAL A 201 -13.545 -22.657 21.021 1.00 84.26 C ANISOU 1211 CG1 VAL A 201 6544 18343 7127 -1275 -679 -950 C ATOM 1212 CG2 VAL A 201 -14.397 -21.710 23.177 1.00 86.01 C ANISOU 1212 CG2 VAL A 201 6452 19164 7064 -1136 -661 -964 C ATOM 1213 N ASN A 202 -17.397 -23.970 23.255 1.00 92.52 N ANISOU 1213 N ASN A 202 6798 20963 7392 -2000 -648 -831 N ATOM 1214 CA ASN A 202 -18.387 -24.163 24.315 1.00 95.45 C ANISOU 1214 CA ASN A 202 6896 21878 7493 -2182 -630 -777 C ATOM 1215 C ASN A 202 -18.071 -23.252 25.505 1.00100.23 C ANISOU 1215 C ASN A 202 7426 22626 8033 -1912 -610 -813 C ATOM 1216 O ASN A 202 -16.957 -23.267 26.041 1.00 98.88 O ANISOU 1216 O ASN A 202 7459 22082 8028 -1857 -614 -745 O ATOM 1217 CB ASN A 202 -18.468 -25.629 24.738 1.00 98.19 C ANISOU 1217 CB ASN A 202 7305 22171 7833 -2679 -646 -571 C ATOM 1218 CG ASN A 202 -19.692 -25.952 25.556 1.00125.80 C ANISOU 1218 CG ASN A 202 10486 26295 11017 -2949 -631 -500 C ATOM 1219 OD1 ASN A 202 -19.608 -26.201 26.762 1.00120.89 O ANISOU 1219 OD1 ASN A 202 9807 25829 10297 -3083 -620 -370 O ATOM 1220 ND2 ASN A 202 -20.857 -25.953 24.920 1.00120.95 N ANISOU 1220 ND2 ASN A 202 9645 26088 10222 -3038 -629 -580 N ATOM 1221 N THR A 203 -19.055 -22.415 25.853 1.00 98.24 N ANISOU 1221 N THR A 203 6874 22918 7535 -1717 -597 -945 N ATOM 1222 CA THR A 203 -19.009 -21.383 26.886 1.00 97.91 C ANISOU 1222 CA THR A 203 6704 23112 7385 -1405 -589 -1048 C ATOM 1223 C THR A 203 -20.022 -21.719 28.032 1.00103.86 C ANISOU 1223 C THR A 203 7130 24526 7807 -1615 -559 -999 C ATOM 1224 O THR A 203 -20.334 -20.855 28.861 1.00105.12 O ANISOU 1224 O THR A 203 7092 25054 7795 -1353 -552 -1128 O ATOM 1225 CB THR A 203 -19.276 -20.022 26.175 1.00107.05 C ANISOU 1225 CB THR A 203 7801 24324 8549 -936 -619 -1275 C ATOM 1226 OG1 THR A 203 -18.896 -18.928 27.001 1.00107.22 O ANISOU 1226 OG1 THR A 203 7798 24383 8558 -579 -635 -1399 O ATOM 1227 CG2 THR A 203 -20.723 -19.860 25.662 1.00108.95 C ANISOU 1227 CG2 THR A 203 7735 25119 8543 -923 -621 -1379 C ATOM 1228 N ASP A 204 -20.510 -22.982 28.075 1.00 99.97 N ANISOU 1228 N ASP A 204 6585 24175 7223 -2095 -548 -814 N ATOM 1229 CA ASP A 204 -21.495 -23.466 29.048 1.00101.71 C ANISOU 1229 CA ASP A 204 6493 25032 7118 -2384 -521 -722 C ATOM 1230 C ASP A 204 -20.948 -23.522 30.481 1.00104.77 C ANISOU 1230 C ASP A 204 6883 25479 7446 -2426 -505 -613 C ATOM 1231 O ASP A 204 -21.623 -23.055 31.396 1.00106.09 O ANISOU 1231 O ASP A 204 6744 26240 7324 -2346 -477 -680 O ATOM 1232 CB ASP A 204 -22.041 -24.853 28.641 1.00104.67 C ANISOU 1232 CB ASP A 204 6864 25454 7452 -2927 -533 -526 C ATOM 1233 CG ASP A 204 -23.025 -24.861 27.474 1.00109.63 C ANISOU 1233 CG ASP A 204 7343 26314 7996 -2963 -542 -636 C ATOM 1234 OD1 ASP A 204 -23.795 -23.881 27.332 1.00109.37 O ANISOU 1234 OD1 ASP A 204 7048 26728 7781 -2642 -527 -838 O ATOM 1235 OD2 ASP A 204 -23.064 -25.870 26.739 1.00113.54 O ANISOU 1235 OD2 ASP A 204 7975 26569 8596 -3315 -572 -524 O ATOM 1236 N HIS A 205 -19.738 -24.078 30.673 1.00 99.83 N ANISOU 1236 N HIS A 205 6584 24270 7077 -2536 -524 -456 N ATOM 1237 CA HIS A 205 -19.110 -24.243 31.989 1.00 99.73 C ANISOU 1237 CA HIS A 205 6604 24263 7028 -2602 -517 -324 C ATOM 1238 C HIS A 205 -18.097 -23.109 32.257 1.00 99.55 C ANISOU 1238 C HIS A 205 6719 23945 7162 -2135 -522 -490 C ATOM 1239 O HIS A 205 -17.039 -23.053 31.626 1.00 97.31 O ANISOU 1239 O HIS A 205 6746 23043 7184 -2014 -547 -491 O ATOM 1240 CB HIS A 205 -18.463 -25.645 32.106 1.00100.88 C ANISOU 1240 CB HIS A 205 7008 23985 7336 -3041 -552 -27 C ATOM 1241 CG HIS A 205 -19.432 -26.782 31.892 1.00107.59 C ANISOU 1241 CG HIS A 205 7747 25090 8044 -3536 -567 149 C ATOM 1242 ND1 HIS A 205 -19.887 -27.557 32.951 1.00112.72 N ANISOU 1242 ND1 HIS A 205 8241 26123 8464 -3930 -569 382 N ATOM 1243 CD2 HIS A 205 -20.024 -27.220 30.753 1.00109.80 C ANISOU 1243 CD2 HIS A 205 8039 25312 8368 -3699 -587 120 C ATOM 1244 CE1 HIS A 205 -20.724 -28.438 32.421 1.00114.02 C ANISOU 1244 CE1 HIS A 205 8341 26425 8555 -4331 -594 494 C ATOM 1245 NE2 HIS A 205 -20.835 -28.276 31.103 1.00112.76 N ANISOU 1245 NE2 HIS A 205 8279 26007 8556 -4206 -606 333 N ATOM 1246 N ILE A 206 -18.458 -22.187 33.177 1.00 95.43 N ANISOU 1246 N ILE A 206 5952 23892 6417 -1873 -502 -644 N ATOM 1247 CA ILE A 206 -17.657 -21.018 33.584 1.00 93.10 C ANISOU 1247 CA ILE A 206 5742 23409 6224 -1432 -518 -829 C ATOM 1248 C ILE A 206 -16.301 -21.460 34.195 1.00 94.38 C ANISOU 1248 C ILE A 206 6176 23101 6582 -1532 -531 -658 C ATOM 1249 O ILE A 206 -15.289 -20.786 33.999 1.00 91.27 O ANISOU 1249 O ILE A 206 5998 22262 6419 -1248 -556 -756 O ATOM 1250 CB ILE A 206 -18.478 -20.110 34.568 1.00 98.38 C ANISOU 1250 CB ILE A 206 6054 24765 6563 -1183 -502 -1031 C ATOM 1251 CG1 ILE A 206 -17.769 -18.770 34.900 1.00 97.57 C ANISOU 1251 CG1 ILE A 206 6034 24470 6568 -686 -540 -1278 C ATOM 1252 CG2 ILE A 206 -18.898 -20.843 35.847 1.00100.71 C ANISOU 1252 CG2 ILE A 206 6121 25584 6562 -1509 -465 -858 C ATOM 1253 CD1 ILE A 206 -18.107 -17.612 33.980 1.00107.89 C ANISOU 1253 CD1 ILE A 206 7322 25731 7940 -266 -583 -1547 C ATOM 1254 N LEU A 207 -16.307 -22.590 34.928 1.00 92.30 N ANISOU 1254 N LEU A 207 5896 22951 6222 -1943 -520 -394 N ATOM 1255 CA LEU A 207 -15.165 -23.179 35.615 1.00 91.21 C ANISOU 1255 CA LEU A 207 5981 22448 6227 -2081 -540 -196 C ATOM 1256 C LEU A 207 -14.099 -23.631 34.612 1.00 93.16 C ANISOU 1256 C LEU A 207 6603 21944 6849 -2096 -575 -124 C ATOM 1257 O LEU A 207 -12.922 -23.378 34.846 1.00 90.36 O ANISOU 1257 O LEU A 207 6452 21195 6685 -1929 -594 -127 O ATOM 1258 CB LEU A 207 -15.643 -24.347 36.501 1.00 93.95 C ANISOU 1258 CB LEU A 207 6205 23131 6358 -2549 -535 93 C ATOM 1259 CG LEU A 207 -14.668 -24.970 37.518 1.00 98.52 C ANISOU 1259 CG LEU A 207 6939 23503 6992 -2707 -561 325 C ATOM 1260 CD1 LEU A 207 -13.896 -23.917 38.307 1.00 97.30 C ANISOU 1260 CD1 LEU A 207 6786 23334 6849 -2321 -556 152 C ATOM 1261 CD2 LEU A 207 -15.411 -25.882 38.477 1.00103.89 C ANISOU 1261 CD2 LEU A 207 7408 24696 7370 -3130 -556 583 C ATOM 1262 N TYR A 208 -14.500 -24.264 33.490 1.00 90.66 N ANISOU 1262 N TYR A 208 6363 21455 6628 -2281 -585 -79 N ATOM 1263 CA TYR A 208 -13.530 -24.666 32.471 1.00 88.15 C ANISOU 1263 CA TYR A 208 6379 20468 6647 -2271 -617 -45 C ATOM 1264 C TYR A 208 -13.058 -23.419 31.711 1.00 88.92 C ANISOU 1264 C TYR A 208 6552 20335 6899 -1829 -613 -293 C ATOM 1265 O TYR A 208 -11.859 -23.273 31.486 1.00 87.30 O ANISOU 1265 O TYR A 208 6590 19642 6937 -1689 -632 -292 O ATOM 1266 CB TYR A 208 -14.092 -25.737 31.508 1.00 90.53 C ANISOU 1266 CB TYR A 208 6740 20662 6996 -2601 -638 58 C ATOM 1267 CG TYR A 208 -13.380 -25.750 30.171 1.00 90.84 C ANISOU 1267 CG TYR A 208 7037 20149 7328 -2467 -659 -28 C ATOM 1268 CD1 TYR A 208 -12.085 -26.255 30.051 1.00 91.44 C ANISOU 1268 CD1 TYR A 208 7416 19657 7672 -2471 -695 65 C ATOM 1269 CD2 TYR A 208 -13.964 -25.176 29.042 1.00 91.38 C ANISOU 1269 CD2 TYR A 208 7032 20294 7393 -2303 -644 -211 C ATOM 1270 CE1 TYR A 208 -11.391 -26.188 28.844 1.00 90.52 C ANISOU 1270 CE1 TYR A 208 7508 19086 7798 -2320 -708 -31 C ATOM 1271 CE2 TYR A 208 -13.286 -25.119 27.825 1.00 90.50 C ANISOU 1271 CE2 TYR A 208 7140 19719 7527 -2167 -660 -291 C ATOM 1272 CZ TYR A 208 -11.997 -25.621 27.731 1.00 97.49 C ANISOU 1272 CZ TYR A 208 8311 20066 8663 -2177 -689 -205 C ATOM 1273 OH TYR A 208 -11.335 -25.567 26.526 1.00 97.18 O ANISOU 1273 OH TYR A 208 8462 19623 8840 -2044 -700 -290 O ATOM 1274 N THR A 209 -14.002 -22.536 31.310 1.00 84.09 N ANISOU 1274 N THR A 209 5730 20078 6142 -1617 -596 -493 N ATOM 1275 CA THR A 209 -13.726 -21.281 30.602 1.00 81.19 C ANISOU 1275 CA THR A 209 5416 19537 5895 -1202 -608 -718 C ATOM 1276 C THR A 209 -12.586 -20.509 31.304 1.00 82.49 C ANISOU 1276 C THR A 209 5707 19457 6180 -940 -626 -777 C ATOM 1277 O THR A 209 -11.640 -20.096 30.636 1.00 79.40 O ANISOU 1277 O THR A 209 5532 18609 6027 -756 -648 -828 O ATOM 1278 CB THR A 209 -15.023 -20.467 30.487 1.00 88.91 C ANISOU 1278 CB THR A 209 6099 21047 6636 -1017 -600 -907 C ATOM 1279 OG1 THR A 209 -15.887 -21.139 29.564 1.00 92.83 O ANISOU 1279 OG1 THR A 209 6522 21674 7075 -1244 -591 -861 O ATOM 1280 CG2 THR A 209 -14.793 -19.021 30.030 1.00 83.04 C ANISOU 1280 CG2 THR A 209 5395 20166 5989 -556 -635 -1138 C ATOM 1281 N VAL A 210 -12.642 -20.376 32.642 1.00 80.80 N ANISOU 1281 N VAL A 210 5354 19554 5792 -947 -617 -761 N ATOM 1282 CA VAL A 210 -11.587 -19.676 33.353 1.00 79.79 C ANISOU 1282 CA VAL A 210 5335 19220 5763 -718 -640 -825 C ATOM 1283 C VAL A 210 -10.331 -20.587 33.463 1.00 82.11 C ANISOU 1283 C VAL A 210 5891 19036 6269 -916 -648 -612 C ATOM 1284 O VAL A 210 -9.235 -20.082 33.237 1.00 80.44 O ANISOU 1284 O VAL A 210 5873 18421 6271 -726 -673 -664 O ATOM 1285 CB VAL A 210 -12.037 -19.060 34.697 1.00 86.14 C ANISOU 1285 CB VAL A 210 5892 20533 6303 -593 -635 -933 C ATOM 1286 CG1 VAL A 210 -12.360 -20.125 35.734 1.00 88.72 C ANISOU 1286 CG1 VAL A 210 6085 21204 6420 -950 -604 -717 C ATOM 1287 CG2 VAL A 210 -10.999 -18.081 35.229 1.00 84.63 C ANISOU 1287 CG2 VAL A 210 5817 20108 6232 -294 -674 -1067 C ATOM 1288 N TYR A 211 -10.478 -21.916 33.695 1.00 78.89 N ANISOU 1288 N TYR A 211 5502 18651 5821 -1291 -639 -377 N ATOM 1289 CA TYR A 211 -9.314 -22.816 33.766 1.00 77.34 C ANISOU 1289 CA TYR A 211 5562 17993 5832 -1456 -664 -180 C ATOM 1290 C TYR A 211 -8.521 -22.770 32.452 1.00 78.81 C ANISOU 1290 C TYR A 211 5993 17640 6309 -1342 -680 -231 C ATOM 1291 O TYR A 211 -7.290 -22.731 32.488 1.00 77.81 O ANISOU 1291 O TYR A 211 6061 17128 6377 -1249 -701 -201 O ATOM 1292 CB TYR A 211 -9.706 -24.272 34.129 1.00 80.45 C ANISOU 1292 CB TYR A 211 5951 18473 6142 -1884 -675 85 C ATOM 1293 CG TYR A 211 -8.719 -25.320 33.649 1.00 81.65 C ANISOU 1293 CG TYR A 211 6399 18068 6555 -2045 -719 255 C ATOM 1294 CD1 TYR A 211 -8.986 -26.090 32.521 1.00 83.10 C ANISOU 1294 CD1 TYR A 211 6697 18021 6858 -2216 -737 290 C ATOM 1295 CD2 TYR A 211 -7.486 -25.494 34.284 1.00 82.15 C ANISOU 1295 CD2 TYR A 211 6628 17834 6750 -1996 -750 354 C ATOM 1296 CE1 TYR A 211 -8.061 -27.016 32.041 1.00 83.84 C ANISOU 1296 CE1 TYR A 211 7064 17597 7195 -2320 -788 406 C ATOM 1297 CE2 TYR A 211 -6.547 -26.413 33.806 1.00 82.26 C ANISOU 1297 CE2 TYR A 211 6910 17339 7008 -2094 -799 483 C ATOM 1298 CZ TYR A 211 -6.843 -27.176 32.685 1.00 90.32 C ANISOU 1298 CZ TYR A 211 8042 18131 8143 -2250 -820 502 C ATOM 1299 OH TYR A 211 -5.943 -28.099 32.200 1.00 90.26 O ANISOU 1299 OH TYR A 211 8295 17628 8371 -2325 -878 601 O ATOM 1300 N SER A 212 -9.222 -22.761 31.310 1.00 74.28 N ANISOU 1300 N SER A 212 5394 17079 5749 -1350 -670 -309 N ATOM 1301 CA SER A 212 -8.608 -22.716 29.988 1.00 71.83 C ANISOU 1301 CA SER A 212 5281 16336 5676 -1252 -681 -365 C ATOM 1302 C SER A 212 -7.832 -21.407 29.779 1.00 74.53 C ANISOU 1302 C SER A 212 5689 16493 6136 -890 -688 -527 C ATOM 1303 O SER A 212 -6.753 -21.435 29.199 1.00 71.71 O ANISOU 1303 O SER A 212 5533 15719 5994 -820 -702 -514 O ATOM 1304 CB SER A 212 -9.667 -22.884 28.902 1.00 74.67 C ANISOU 1304 CB SER A 212 5554 16842 5974 -1332 -670 -425 C ATOM 1305 OG SER A 212 -10.431 -21.702 28.740 1.00 80.83 O ANISOU 1305 OG SER A 212 6149 17940 6621 -1083 -658 -608 O ATOM 1306 N THR A 213 -8.379 -20.278 30.265 1.00 73.04 N ANISOU 1306 N THR A 213 5328 16620 5802 -667 -689 -680 N ATOM 1307 CA THR A 213 -7.794 -18.942 30.133 1.00 72.33 C ANISOU 1307 CA THR A 213 5292 16380 5808 -328 -717 -844 C ATOM 1308 C THR A 213 -6.537 -18.804 31.053 1.00 75.79 C ANISOU 1308 C THR A 213 5850 16603 6346 -277 -735 -800 C ATOM 1309 O THR A 213 -5.555 -18.161 30.673 1.00 74.19 O ANISOU 1309 O THR A 213 5798 16067 6324 -108 -761 -852 O ATOM 1310 CB THR A 213 -8.910 -17.892 30.381 1.00 86.05 C ANISOU 1310 CB THR A 213 6806 18541 7349 -113 -729 -1032 C ATOM 1311 OG1 THR A 213 -8.883 -16.898 29.361 1.00 89.29 O ANISOU 1311 OG1 THR A 213 7280 18779 7869 142 -765 -1167 O ATOM 1312 CG2 THR A 213 -8.876 -17.254 31.764 1.00 84.40 C ANISOU 1312 CG2 THR A 213 6477 18589 7003 24 -745 -1120 C ATOM 1313 N VAL A 214 -6.570 -19.440 32.231 1.00 72.88 N ANISOU 1313 N VAL A 214 5404 16438 5850 -442 -723 -690 N ATOM 1314 CA VAL A 214 -5.485 -19.416 33.210 1.00 71.75 C ANISOU 1314 CA VAL A 214 5341 16159 5760 -418 -742 -635 C ATOM 1315 C VAL A 214 -4.370 -20.368 32.760 1.00 76.49 C ANISOU 1315 C VAL A 214 6168 16317 6577 -564 -747 -466 C ATOM 1316 O VAL A 214 -3.208 -19.961 32.694 1.00 76.05 O ANISOU 1316 O VAL A 214 6252 15958 6685 -432 -769 -489 O ATOM 1317 CB VAL A 214 -6.003 -19.764 34.634 1.00 76.17 C ANISOU 1317 CB VAL A 214 5717 17150 6074 -549 -730 -565 C ATOM 1318 CG1 VAL A 214 -4.848 -20.003 35.600 1.00 75.42 C ANISOU 1318 CG1 VAL A 214 5717 16905 6035 -580 -751 -457 C ATOM 1319 CG2 VAL A 214 -6.945 -18.684 35.167 1.00 76.77 C ANISOU 1319 CG2 VAL A 214 5560 17676 5935 -340 -732 -778 C ATOM 1320 N GLY A 215 -4.737 -21.616 32.464 1.00 73.40 N ANISOU 1320 N GLY A 215 5808 15901 6180 -831 -737 -308 N ATOM 1321 CA GLY A 215 -3.812 -22.661 32.045 1.00 72.31 C ANISOU 1321 CA GLY A 215 5879 15363 6233 -972 -756 -157 C ATOM 1322 C GLY A 215 -3.066 -22.325 30.775 1.00 74.67 C ANISOU 1322 C GLY A 215 6336 15288 6749 -821 -758 -246 C ATOM 1323 O GLY A 215 -1.886 -22.657 30.657 1.00 73.58 O ANISOU 1323 O GLY A 215 6359 14821 6778 -802 -777 -186 O ATOM 1324 N ALA A 216 -3.745 -21.622 29.838 1.00 70.93 N ANISOU 1324 N ALA A 216 5801 14892 6257 -704 -740 -389 N ATOM 1325 CA ALA A 216 -3.211 -21.216 28.535 1.00 69.00 C ANISOU 1325 CA ALA A 216 5677 14359 6182 -570 -740 -469 C ATOM 1326 C ALA A 216 -2.542 -19.846 28.526 1.00 71.06 C ANISOU 1326 C ALA A 216 5959 14531 6510 -302 -756 -590 C ATOM 1327 O ALA A 216 -1.615 -19.673 27.737 1.00 71.14 O ANISOU 1327 O ALA A 216 6100 14248 6682 -226 -762 -599 O ATOM 1328 CB ALA A 216 -4.308 -21.226 27.485 1.00 70.20 C ANISOU 1328 CB ALA A 216 5757 14643 6273 -605 -724 -535 C ATOM 1329 N PHE A 217 -3.003 -18.868 29.331 1.00 65.79 N ANISOU 1329 N PHE A 217 5165 14113 5719 -160 -770 -690 N ATOM 1330 CA PHE A 217 -2.394 -17.545 29.264 1.00 63.84 C ANISOU 1330 CA PHE A 217 4961 13743 5553 84 -806 -812 C ATOM 1331 C PHE A 217 -1.886 -17.003 30.599 1.00 68.04 C ANISOU 1331 C PHE A 217 5460 14351 6041 169 -835 -849 C ATOM 1332 O PHE A 217 -0.687 -16.756 30.712 1.00 68.10 O ANISOU 1332 O PHE A 217 5584 14107 6183 218 -856 -830 O ATOM 1333 CB PHE A 217 -3.363 -16.542 28.637 1.00 65.92 C ANISOU 1333 CB PHE A 217 5137 14159 5750 257 -827 -956 C ATOM 1334 CG PHE A 217 -2.880 -15.111 28.603 1.00 67.27 C ANISOU 1334 CG PHE A 217 5362 14196 6001 508 -889 -1082 C ATOM 1335 CD1 PHE A 217 -3.305 -14.192 29.561 1.00 71.85 C ANISOU 1335 CD1 PHE A 217 5839 14987 6473 677 -935 -1223 C ATOM 1336 CD2 PHE A 217 -2.026 -14.671 27.596 1.00 68.00 C ANISOU 1336 CD2 PHE A 217 5605 13962 6271 571 -912 -1064 C ATOM 1337 CE1 PHE A 217 -2.862 -12.868 29.532 1.00 72.70 C ANISOU 1337 CE1 PHE A 217 6020 14930 6671 902 -1014 -1346 C ATOM 1338 CE2 PHE A 217 -1.589 -13.345 27.562 1.00 71.09 C ANISOU 1338 CE2 PHE A 217 6059 14210 6741 771 -985 -1160 C ATOM 1339 CZ PHE A 217 -2.015 -12.451 28.527 1.00 70.82 C ANISOU 1339 CZ PHE A 217 5946 14341 6620 936 -1043 -1303 C ATOM 1340 N TYR A 218 -2.777 -16.756 31.575 1.00 64.29 N ANISOU 1340 N TYR A 218 4815 14243 5369 198 -837 -918 N ATOM 1341 CA TYR A 218 -2.426 -16.123 32.845 1.00 63.41 C ANISOU 1341 CA TYR A 218 4645 14262 5184 306 -870 -996 C ATOM 1342 C TYR A 218 -1.340 -16.859 33.620 1.00 68.20 C ANISOU 1342 C TYR A 218 5328 14743 5840 174 -865 -851 C ATOM 1343 O TYR A 218 -0.481 -16.184 34.198 1.00 68.14 O ANISOU 1343 O TYR A 218 5360 14647 5882 291 -904 -917 O ATOM 1344 CB TYR A 218 -3.662 -15.913 33.710 1.00 65.25 C ANISOU 1344 CB TYR A 218 4654 14976 5163 339 -864 -1092 C ATOM 1345 CG TYR A 218 -4.646 -14.947 33.088 1.00 65.81 C ANISOU 1345 CG TYR A 218 4640 15181 5182 546 -891 -1275 C ATOM 1346 CD1 TYR A 218 -4.454 -13.570 33.174 1.00 67.22 C ANISOU 1346 CD1 TYR A 218 4849 15279 5414 828 -966 -1472 C ATOM 1347 CD2 TYR A 218 -5.780 -15.407 32.428 1.00 66.95 C ANISOU 1347 CD2 TYR A 218 4679 15533 5225 460 -855 -1253 C ATOM 1348 CE1 TYR A 218 -5.368 -12.676 32.619 1.00 68.57 C ANISOU 1348 CE1 TYR A 218 4954 15557 5543 1042 -1009 -1637 C ATOM 1349 CE2 TYR A 218 -6.707 -14.523 31.877 1.00 68.31 C ANISOU 1349 CE2 TYR A 218 4761 15854 5339 669 -887 -1419 C ATOM 1350 CZ TYR A 218 -6.499 -13.158 31.974 1.00 73.84 C ANISOU 1350 CZ TYR A 218 5501 16457 6099 971 -967 -1609 C ATOM 1351 OH TYR A 218 -7.412 -12.295 31.412 1.00 71.57 O ANISOU 1351 OH TYR A 218 5139 16292 5762 1198 -1016 -1767 O ATOM 1352 N PHE A 219 -1.336 -18.208 33.619 1.00 65.79 N ANISOU 1352 N PHE A 219 5054 14411 5533 -63 -830 -659 N ATOM 1353 CA PHE A 219 -0.257 -18.942 34.286 1.00 66.40 C ANISOU 1353 CA PHE A 219 5220 14337 5673 -168 -840 -509 C ATOM 1354 C PHE A 219 1.052 -18.696 33.472 1.00 70.79 C ANISOU 1354 C PHE A 219 5956 14475 6467 -77 -857 -516 C ATOM 1355 O PHE A 219 1.950 -18.086 34.060 1.00 70.94 O ANISOU 1355 O PHE A 219 6000 14426 6527 28 -889 -562 O ATOM 1356 CB PHE A 219 -0.590 -20.439 34.510 1.00 69.15 C ANISOU 1356 CB PHE A 219 5571 14737 5964 -439 -822 -294 C ATOM 1357 CG PHE A 219 0.480 -21.331 35.120 1.00 70.65 C ANISOU 1357 CG PHE A 219 5874 14739 6233 -544 -847 -116 C ATOM 1358 CD1 PHE A 219 1.453 -20.808 35.969 1.00 73.17 C ANISOU 1358 CD1 PHE A 219 6196 15045 6560 -430 -874 -140 C ATOM 1359 CD2 PHE A 219 0.476 -22.702 34.892 1.00 73.36 C ANISOU 1359 CD2 PHE A 219 6313 14927 6631 -755 -857 74 C ATOM 1360 CE1 PHE A 219 2.434 -21.636 36.532 1.00 74.30 C ANISOU 1360 CE1 PHE A 219 6432 15034 6766 -512 -905 29 C ATOM 1361 CE2 PHE A 219 1.451 -23.528 35.464 1.00 76.50 C ANISOU 1361 CE2 PHE A 219 6820 15141 7104 -826 -897 241 C ATOM 1362 CZ PHE A 219 2.423 -22.990 36.282 1.00 73.98 C ANISOU 1362 CZ PHE A 219 6493 14829 6786 -699 -918 222 C ATOM 1363 N PRO A 220 1.139 -18.968 32.131 1.00 66.27 N ANISOU 1363 N PRO A 220 5485 13664 6031 -95 -841 -500 N ATOM 1364 CA PRO A 220 2.376 -18.652 31.398 1.00 64.98 C ANISOU 1364 CA PRO A 220 5460 13172 6060 -6 -854 -513 C ATOM 1365 C PRO A 220 2.874 -17.203 31.476 1.00 70.23 C ANISOU 1365 C PRO A 220 6128 13786 6769 186 -892 -653 C ATOM 1366 O PRO A 220 4.091 -17.036 31.458 1.00 70.82 O ANISOU 1366 O PRO A 220 6285 13660 6961 220 -912 -631 O ATOM 1367 CB PRO A 220 2.013 -18.967 29.953 1.00 65.78 C ANISOU 1367 CB PRO A 220 5616 13142 6236 -39 -828 -515 C ATOM 1368 CG PRO A 220 1.017 -19.994 30.036 1.00 70.85 C ANISOU 1368 CG PRO A 220 6206 13939 6777 -212 -807 -437 C ATOM 1369 CD PRO A 220 0.205 -19.706 31.254 1.00 68.01 C ANISOU 1369 CD PRO A 220 5696 13917 6228 -223 -811 -459 C ATOM 1370 N THR A 221 1.997 -16.165 31.525 1.00 66.48 N ANISOU 1370 N THR A 221 5571 13479 6210 312 -914 -797 N ATOM 1371 CA THR A 221 2.518 -14.779 31.589 1.00 65.62 C ANISOU 1371 CA THR A 221 5496 13269 6166 490 -975 -931 C ATOM 1372 C THR A 221 3.160 -14.495 32.937 1.00 69.14 C ANISOU 1372 C THR A 221 5912 13791 6568 521 -1010 -965 C ATOM 1373 O THR A 221 4.236 -13.904 32.962 1.00 68.69 O ANISOU 1373 O THR A 221 5934 13540 6624 576 -1053 -992 O ATOM 1374 CB THR A 221 1.494 -13.681 31.263 1.00 69.13 C ANISOU 1374 CB THR A 221 5884 13828 6553 653 -1014 -1089 C ATOM 1375 OG1 THR A 221 0.804 -13.249 32.435 1.00 69.87 O ANISOU 1375 OG1 THR A 221 5845 14221 6481 736 -1039 -1208 O ATOM 1376 CG2 THR A 221 0.557 -14.068 30.214 1.00 64.77 C ANISOU 1376 CG2 THR A 221 5309 13324 5978 616 -976 -1062 C ATOM 1377 N LEU A 222 2.510 -14.908 34.050 1.00 65.68 N ANISOU 1377 N LEU A 222 5347 13656 5954 473 -995 -960 N ATOM 1378 CA LEU A 222 3.065 -14.718 35.394 1.00 65.85 C ANISOU 1378 CA LEU A 222 5319 13803 5900 494 -1027 -989 C ATOM 1379 C LEU A 222 4.426 -15.426 35.529 1.00 66.01 C ANISOU 1379 C LEU A 222 5435 13613 6033 393 -1022 -838 C ATOM 1380 O LEU A 222 5.322 -14.903 36.185 1.00 65.93 O ANISOU 1380 O LEU A 222 5438 13565 6048 450 -1067 -888 O ATOM 1381 CB LEU A 222 2.093 -15.196 36.488 1.00 67.58 C ANISOU 1381 CB LEU A 222 5368 14425 5883 429 -1002 -976 C ATOM 1382 CG LEU A 222 0.898 -14.283 36.768 1.00 74.02 C ANISOU 1382 CG LEU A 222 6044 15537 6545 584 -1024 -1181 C ATOM 1383 CD1 LEU A 222 -0.203 -15.032 37.491 1.00 76.05 C ANISOU 1383 CD1 LEU A 222 6117 16220 6559 467 -976 -1124 C ATOM 1384 CD2 LEU A 222 1.306 -13.053 37.554 1.00 76.74 C ANISOU 1384 CD2 LEU A 222 6372 15910 6875 775 -1101 -1386 C ATOM 1385 N LEU A 223 4.577 -16.588 34.881 1.00 59.88 N ANISOU 1385 N LEU A 223 4724 12703 5324 257 -978 -671 N ATOM 1386 CA LEU A 223 5.806 -17.358 34.872 1.00 59.25 C ANISOU 1386 CA LEU A 223 4736 12421 5356 185 -978 -531 C ATOM 1387 C LEU A 223 6.890 -16.588 34.097 1.00 63.76 C ANISOU 1387 C LEU A 223 5401 12726 6098 277 -1002 -593 C ATOM 1388 O LEU A 223 8.025 -16.489 34.579 1.00 63.86 O ANISOU 1388 O LEU A 223 5438 12664 6161 292 -1030 -570 O ATOM 1389 CB LEU A 223 5.548 -18.753 34.264 1.00 59.09 C ANISOU 1389 CB LEU A 223 4768 12315 5367 38 -940 -371 C ATOM 1390 CG LEU A 223 6.747 -19.669 33.959 1.00 63.00 C ANISOU 1390 CG LEU A 223 5377 12557 6002 -7 -946 -242 C ATOM 1391 CD1 LEU A 223 7.587 -19.978 35.218 1.00 63.72 C ANISOU 1391 CD1 LEU A 223 5451 12706 6053 -21 -983 -152 C ATOM 1392 CD2 LEU A 223 6.276 -20.949 33.337 1.00 65.85 C ANISOU 1392 CD2 LEU A 223 5798 12829 6392 -137 -926 -127 C ATOM 1393 N LEU A 224 6.519 -16.007 32.935 1.00 58.95 N ANISOU 1393 N LEU A 224 4834 12003 5561 330 -994 -663 N ATOM 1394 CA LEU A 224 7.409 -15.226 32.079 1.00 57.48 C ANISOU 1394 CA LEU A 224 4730 11589 5520 392 -1018 -702 C ATOM 1395 C LEU A 224 7.882 -13.947 32.746 1.00 61.29 C ANISOU 1395 C LEU A 224 5207 12069 6012 487 -1090 -823 C ATOM 1396 O LEU A 224 9.065 -13.635 32.651 1.00 60.87 O ANISOU 1396 O LEU A 224 5204 11868 6057 482 -1117 -806 O ATOM 1397 CB LEU A 224 6.743 -14.897 30.750 1.00 57.05 C ANISOU 1397 CB LEU A 224 4710 11458 5509 420 -1002 -734 C ATOM 1398 CG LEU A 224 6.835 -15.988 29.699 1.00 61.71 C ANISOU 1398 CG LEU A 224 5346 11946 6157 331 -945 -630 C ATOM 1399 CD1 LEU A 224 5.900 -15.698 28.543 1.00 62.34 C ANISOU 1399 CD1 LEU A 224 5430 12024 6233 355 -929 -672 C ATOM 1400 CD2 LEU A 224 8.255 -16.148 29.183 1.00 63.53 C ANISOU 1400 CD2 LEU A 224 5642 11987 6509 318 -943 -570 C ATOM 1401 N ILE A 225 6.988 -13.223 33.431 1.00 59.04 N ANISOU 1401 N ILE A 225 4855 11957 5620 574 -1126 -956 N ATOM 1402 CA ILE A 225 7.355 -12.001 34.144 1.00 60.41 C ANISOU 1402 CA ILE A 225 5029 12127 5798 676 -1211 -1104 C ATOM 1403 C ILE A 225 8.420 -12.364 35.209 1.00 65.04 C ANISOU 1403 C ILE A 225 5589 12761 6363 620 -1222 -1058 C ATOM 1404 O ILE A 225 9.486 -11.749 35.220 1.00 64.93 O ANISOU 1404 O ILE A 225 5628 12596 6444 623 -1274 -1084 O ATOM 1405 CB ILE A 225 6.118 -11.275 34.746 1.00 65.25 C ANISOU 1405 CB ILE A 225 5558 12957 6278 807 -1250 -1280 C ATOM 1406 CG1 ILE A 225 5.154 -10.801 33.635 1.00 65.95 C ANISOU 1406 CG1 ILE A 225 5676 12984 6398 888 -1257 -1331 C ATOM 1407 CG2 ILE A 225 6.551 -10.085 35.621 1.00 67.86 C ANISOU 1407 CG2 ILE A 225 5893 13284 6607 919 -1352 -1459 C ATOM 1408 CD1 ILE A 225 3.723 -10.613 34.075 1.00 76.32 C ANISOU 1408 CD1 ILE A 225 6868 14586 7546 998 -1262 -1462 C ATOM 1409 N ALA A 226 8.151 -13.404 36.036 1.00 61.40 N ANISOU 1409 N ALA A 226 5046 12508 5775 551 -1177 -969 N ATOM 1410 CA ALA A 226 9.050 -13.908 37.076 1.00 61.44 C ANISOU 1410 CA ALA A 226 5015 12595 5735 497 -1187 -895 C ATOM 1411 C ALA A 226 10.402 -14.375 36.470 1.00 65.89 C ANISOU 1411 C ALA A 226 5661 12928 6448 437 -1178 -769 C ATOM 1412 O ALA A 226 11.480 -14.040 36.994 1.00 65.42 O ANISOU 1412 O ALA A 226 5597 12844 6416 443 -1222 -784 O ATOM 1413 CB ALA A 226 8.380 -15.048 37.828 1.00 62.43 C ANISOU 1413 CB ALA A 226 5055 12961 5704 411 -1142 -776 C ATOM 1414 N LEU A 227 10.327 -15.108 35.340 1.00 61.27 N ANISOU 1414 N LEU A 227 5138 12193 5949 388 -1126 -664 N ATOM 1415 CA LEU A 227 11.484 -15.618 34.623 1.00 60.16 C ANISOU 1415 CA LEU A 227 5059 11864 5936 354 -1111 -563 C ATOM 1416 C LEU A 227 12.319 -14.472 34.064 1.00 65.14 C ANISOU 1416 C LEU A 227 5727 12351 6672 389 -1151 -644 C ATOM 1417 O LEU A 227 13.535 -14.459 34.288 1.00 66.04 O ANISOU 1417 O LEU A 227 5834 12426 6831 373 -1175 -612 O ATOM 1418 CB LEU A 227 11.033 -16.561 33.504 1.00 59.38 C ANISOU 1418 CB LEU A 227 5012 11662 5887 309 -1052 -475 C ATOM 1419 CG LEU A 227 11.375 -18.049 33.649 1.00 64.03 C ANISOU 1419 CG LEU A 227 5621 12226 6480 248 -1031 -324 C ATOM 1420 CD1 LEU A 227 11.491 -18.491 35.091 1.00 64.63 C ANISOU 1420 CD1 LEU A 227 5642 12466 6448 221 -1061 -257 C ATOM 1421 CD2 LEU A 227 10.374 -18.898 32.915 1.00 66.37 C ANISOU 1421 CD2 LEU A 227 5955 12490 6773 187 -990 -275 C ATOM 1422 N TYR A 228 11.671 -13.483 33.397 1.00 60.69 N ANISOU 1422 N TYR A 228 5199 11719 6141 431 -1171 -742 N ATOM 1423 CA TYR A 228 12.370 -12.319 32.835 1.00 60.25 C ANISOU 1423 CA TYR A 228 5196 11509 6189 441 -1226 -799 C ATOM 1424 C TYR A 228 13.019 -11.471 33.925 1.00 64.08 C ANISOU 1424 C TYR A 228 5658 12031 6658 457 -1309 -896 C ATOM 1425 O TYR A 228 14.130 -10.981 33.718 1.00 63.93 O ANISOU 1425 O TYR A 228 5663 11909 6720 408 -1348 -883 O ATOM 1426 CB TYR A 228 11.445 -11.435 31.981 1.00 61.25 C ANISOU 1426 CB TYR A 228 5377 11548 6348 493 -1250 -872 C ATOM 1427 CG TYR A 228 12.184 -10.293 31.319 1.00 62.24 C ANISOU 1427 CG TYR A 228 5574 11489 6586 474 -1320 -891 C ATOM 1428 CD1 TYR A 228 13.095 -10.527 30.296 1.00 63.36 C ANISOU 1428 CD1 TYR A 228 5739 11527 6808 391 -1288 -776 C ATOM 1429 CD2 TYR A 228 12.015 -8.981 31.755 1.00 63.68 C ANISOU 1429 CD2 TYR A 228 5799 11608 6789 533 -1428 -1025 C ATOM 1430 CE1 TYR A 228 13.791 -9.484 29.695 1.00 64.65 C ANISOU 1430 CE1 TYR A 228 5960 11545 7060 338 -1355 -766 C ATOM 1431 CE2 TYR A 228 12.711 -7.927 31.164 1.00 64.77 C ANISOU 1431 CE2 TYR A 228 6020 11550 7038 485 -1510 -1021 C ATOM 1432 CZ TYR A 228 13.588 -8.183 30.123 1.00 71.95 C ANISOU 1432 CZ TYR A 228 6945 12376 8018 373 -1470 -876 C ATOM 1433 OH TYR A 228 14.274 -7.159 29.517 1.00 76.20 O ANISOU 1433 OH TYR A 228 7556 12745 8651 293 -1552 -843 O ATOM 1434 N GLY A 229 12.319 -11.309 35.051 1.00 59.98 N ANISOU 1434 N GLY A 229 5085 11681 6025 516 -1336 -996 N ATOM 1435 CA GLY A 229 12.795 -10.554 36.201 1.00 60.40 C ANISOU 1435 CA GLY A 229 5106 11808 6037 543 -1418 -1119 C ATOM 1436 C GLY A 229 14.116 -11.075 36.722 1.00 63.49 C ANISOU 1436 C GLY A 229 5456 12233 6433 470 -1416 -1029 C ATOM 1437 O GLY A 229 15.066 -10.305 36.869 1.00 63.70 O ANISOU 1437 O GLY A 229 5498 12183 6520 439 -1485 -1083 O ATOM 1438 N ARG A 230 14.193 -12.401 36.951 1.00 58.49 N ANISOU 1438 N ARG A 230 4775 11705 5743 437 -1346 -883 N ATOM 1439 CA ARG A 230 15.382 -13.089 37.442 1.00 57.52 C ANISOU 1439 CA ARG A 230 4608 11631 5615 393 -1344 -778 C ATOM 1440 C ARG A 230 16.507 -13.014 36.411 1.00 62.82 C ANISOU 1440 C ARG A 230 5317 12131 6420 347 -1338 -714 C ATOM 1441 O ARG A 230 17.660 -12.788 36.797 1.00 64.37 O ANISOU 1441 O ARG A 230 5472 12356 6630 317 -1378 -711 O ATOM 1442 CB ARG A 230 15.064 -14.554 37.792 1.00 54.41 C ANISOU 1442 CB ARG A 230 4185 11345 5145 378 -1286 -624 C ATOM 1443 CG ARG A 230 14.283 -14.734 39.092 1.00 57.98 C ANISOU 1443 CG ARG A 230 4560 12043 5426 389 -1298 -648 C ATOM 1444 N ILE A 231 16.171 -13.168 35.103 1.00 57.96 N ANISOU 1444 N ILE A 231 4764 11372 5887 338 -1290 -669 N ATOM 1445 CA ILE A 231 17.134 -13.118 33.991 1.00 57.16 C ANISOU 1445 CA ILE A 231 4681 11148 5890 294 -1273 -607 C ATOM 1446 C ILE A 231 17.750 -11.706 33.898 1.00 61.68 C ANISOU 1446 C ILE A 231 5271 11645 6520 241 -1351 -690 C ATOM 1447 O ILE A 231 18.973 -11.588 33.843 1.00 63.19 O ANISOU 1447 O ILE A 231 5419 11848 6744 181 -1370 -652 O ATOM 1448 CB ILE A 231 16.482 -13.576 32.646 1.00 59.24 C ANISOU 1448 CB ILE A 231 4999 11307 6200 299 -1206 -555 C ATOM 1449 CG1 ILE A 231 16.190 -15.094 32.666 1.00 59.61 C ANISOU 1449 CG1 ILE A 231 5039 11395 6215 324 -1144 -459 C ATOM 1450 CG2 ILE A 231 17.376 -13.245 31.463 1.00 58.84 C ANISOU 1450 CG2 ILE A 231 4958 11165 6235 249 -1197 -516 C ATOM 1451 CD1 ILE A 231 15.243 -15.644 31.561 1.00 60.74 C ANISOU 1451 CD1 ILE A 231 5235 11463 6379 327 -1085 -435 C ATOM 1452 N TYR A 232 16.903 -10.655 33.890 1.00 57.36 N ANISOU 1452 N TYR A 232 4786 11025 5984 263 -1406 -803 N ATOM 1453 CA TYR A 232 17.279 -9.238 33.814 1.00 57.46 C ANISOU 1453 CA TYR A 232 4851 10915 6065 214 -1507 -890 C ATOM 1454 C TYR A 232 18.254 -8.869 34.932 1.00 61.80 C ANISOU 1454 C TYR A 232 5343 11550 6586 171 -1578 -951 C ATOM 1455 O TYR A 232 19.279 -8.242 34.660 1.00 63.03 O ANISOU 1455 O TYR A 232 5500 11642 6807 64 -1629 -931 O ATOM 1456 CB TYR A 232 16.016 -8.337 33.880 1.00 59.06 C ANISOU 1456 CB TYR A 232 5131 11039 6269 299 -1567 -1025 C ATOM 1457 CG TYR A 232 16.309 -6.856 33.776 1.00 61.53 C ANISOU 1457 CG TYR A 232 5533 11173 6673 260 -1698 -1120 C ATOM 1458 CD1 TYR A 232 16.612 -6.103 34.906 1.00 64.67 C ANISOU 1458 CD1 TYR A 232 5927 11593 7052 268 -1802 -1269 C ATOM 1459 CD2 TYR A 232 16.302 -6.212 32.545 1.00 62.51 C ANISOU 1459 CD2 TYR A 232 5750 11101 6899 206 -1728 -1056 C ATOM 1460 CE1 TYR A 232 16.939 -4.753 34.810 1.00 67.31 C ANISOU 1460 CE1 TYR A 232 6363 11725 7486 215 -1942 -1358 C ATOM 1461 CE2 TYR A 232 16.614 -4.859 32.436 1.00 65.33 C ANISOU 1461 CE2 TYR A 232 6211 11261 7352 147 -1868 -1117 C ATOM 1462 CZ TYR A 232 16.933 -4.131 33.572 1.00 77.22 C ANISOU 1462 CZ TYR A 232 7726 12758 8856 150 -1979 -1273 C ATOM 1463 OH TYR A 232 17.234 -2.792 33.468 1.00 83.86 O ANISOU 1463 OH TYR A 232 8689 13368 9805 83 -2137 -1340 O ATOM 1464 N VAL A 233 17.922 -9.249 36.182 1.00 57.70 N ANISOU 1464 N VAL A 233 4763 11200 5958 240 -1582 -1019 N ATOM 1465 CA VAL A 233 18.712 -8.987 37.388 1.00 57.88 C ANISOU 1465 CA VAL A 233 4717 11353 5922 217 -1647 -1090 C ATOM 1466 C VAL A 233 20.034 -9.780 37.314 1.00 65.14 C ANISOU 1466 C VAL A 233 5552 12354 6844 148 -1608 -949 C ATOM 1467 O VAL A 233 21.069 -9.251 37.742 1.00 67.56 O ANISOU 1467 O VAL A 233 5814 12698 7158 72 -1675 -985 O ATOM 1468 CB VAL A 233 17.899 -9.282 38.693 1.00 60.31 C ANISOU 1468 CB VAL A 233 4964 11867 6082 314 -1650 -1181 C ATOM 1469 CG1 VAL A 233 18.772 -9.193 39.938 1.00 60.62 C ANISOU 1469 CG1 VAL A 233 4912 12084 6038 289 -1707 -1232 C ATOM 1470 CG2 VAL A 233 16.717 -8.329 38.833 1.00 60.32 C ANISOU 1470 CG2 VAL A 233 5026 11822 6071 401 -1709 -1365 C ATOM 1471 N GLU A 234 20.012 -11.027 36.762 1.00 61.18 N ANISOU 1471 N GLU A 234 5028 11880 6336 180 -1510 -800 N ATOM 1472 CA GLU A 234 21.221 -11.853 36.641 1.00 61.38 C ANISOU 1472 CA GLU A 234 4973 11986 6364 158 -1478 -680 C ATOM 1473 C GLU A 234 22.229 -11.206 35.710 1.00 67.01 C ANISOU 1473 C GLU A 234 5676 12622 7163 55 -1497 -658 C ATOM 1474 O GLU A 234 23.373 -11.005 36.108 1.00 67.79 O ANISOU 1474 O GLU A 234 5689 12821 7246 -5 -1539 -656 O ATOM 1475 CB GLU A 234 20.912 -13.280 36.161 1.00 61.91 C ANISOU 1475 CB GLU A 234 5044 12055 6425 230 -1388 -550 C ATOM 1476 CG GLU A 234 21.242 -14.369 37.172 1.00 76.71 C ANISOU 1476 CG GLU A 234 6852 14082 8214 290 -1386 -470 C ATOM 1477 CD GLU A 234 22.605 -14.342 37.853 1.00102.02 C ANISOU 1477 CD GLU A 234 9950 17427 11385 277 -1436 -455 C ATOM 1478 OE1 GLU A 234 23.636 -14.466 37.153 1.00 91.82 O ANISOU 1478 OE1 GLU A 234 8612 16131 10146 264 -1424 -409 O ATOM 1479 OE2 GLU A 234 22.633 -14.255 39.102 1.00 96.05 O ANISOU 1479 OE2 GLU A 234 9144 16819 10533 285 -1485 -489 O ATOM 1480 N ALA A 235 21.792 -10.839 34.492 1.00 63.91 N ANISOU 1480 N ALA A 235 5360 12074 6848 23 -1470 -639 N ATOM 1481 CA ALA A 235 22.624 -10.190 33.480 1.00 64.28 C ANISOU 1481 CA ALA A 235 5401 12057 6964 -98 -1485 -595 C ATOM 1482 C ALA A 235 23.203 -8.837 33.966 1.00 69.92 C ANISOU 1482 C ALA A 235 6125 12734 7707 -227 -1603 -676 C ATOM 1483 O ALA A 235 24.362 -8.544 33.680 1.00 70.79 O ANISOU 1483 O ALA A 235 6161 12905 7830 -350 -1626 -625 O ATOM 1484 CB ALA A 235 21.814 -9.986 32.220 1.00 64.07 C ANISOU 1484 CB ALA A 235 5469 11879 6997 -100 -1449 -564 C ATOM 1485 N ARG A 236 22.403 -8.036 34.711 1.00 66.77 N ANISOU 1485 N ARG A 236 5810 12248 7313 -198 -1683 -811 N ATOM 1486 CA ARG A 236 22.774 -6.727 35.259 1.00 68.10 C ANISOU 1486 CA ARG A 236 6019 12339 7518 -302 -1817 -926 C ATOM 1487 C ARG A 236 23.958 -6.847 36.211 1.00 73.95 C ANISOU 1487 C ARG A 236 6633 13270 8196 -365 -1853 -943 C ATOM 1488 O ARG A 236 24.905 -6.061 36.111 1.00 75.41 O ANISOU 1488 O ARG A 236 6797 13434 8421 -529 -1929 -941 O ATOM 1489 CB ARG A 236 21.582 -6.097 35.996 1.00 68.92 C ANISOU 1489 CB ARG A 236 6217 12356 7612 -193 -1888 -1100 C ATOM 1490 CG ARG A 236 20.972 -4.866 35.325 1.00 79.35 C ANISOU 1490 CG ARG A 236 7695 13411 9044 -223 -1983 -1162 C ATOM 1491 CD ARG A 236 20.945 -3.651 36.255 1.00 92.51 C ANISOU 1491 CD ARG A 236 9431 14982 10735 -234 -2144 -1365 C ATOM 1492 NE ARG A 236 20.344 -3.919 37.572 1.00100.28 N ANISOU 1492 NE ARG A 236 10359 16140 11603 -80 -2146 -1528 N ATOM 1493 CZ ARG A 236 19.134 -3.512 37.955 1.00114.78 C ANISOU 1493 CZ ARG A 236 12259 17935 13415 79 -2189 -1691 C ATOM 1494 NH1 ARG A 236 18.368 -2.806 37.128 1.00104.82 N ANISOU 1494 NH1 ARG A 236 11135 16438 12252 122 -2242 -1717 N ATOM 1495 NH2 ARG A 236 18.681 -3.804 39.169 1.00 95.77 N ANISOU 1495 NH2 ARG A 236 9769 15747 10872 201 -2183 -1828 N ATOM 1496 N SER A 237 23.910 -7.834 37.126 1.00 70.35 N ANISOU 1496 N SER A 237 6087 13007 7634 -247 -1802 -946 N ATOM 1497 CA SER A 237 24.988 -8.083 38.087 1.00 71.22 C ANISOU 1497 CA SER A 237 6064 13331 7665 -279 -1833 -952 C ATOM 1498 C SER A 237 26.187 -8.772 37.409 1.00 74.26 C ANISOU 1498 C SER A 237 6331 13834 8051 -331 -1773 -801 C ATOM 1499 O SER A 237 27.317 -8.599 37.859 1.00 75.33 O ANISOU 1499 O SER A 237 6353 14122 8147 -415 -1820 -803 O ATOM 1500 CB SER A 237 24.487 -8.915 39.262 1.00 74.78 C ANISOU 1500 CB SER A 237 6463 13956 7996 -135 -1806 -979 C ATOM 1501 OG SER A 237 23.886 -10.118 38.815 1.00 84.84 O ANISOU 1501 OG SER A 237 7743 15238 9254 -24 -1698 -853 O ATOM 1502 N ARG A 238 25.944 -9.527 36.325 1.00 68.88 N ANISOU 1502 N ARG A 238 5666 13101 7404 -277 -1675 -685 N ATOM 1503 CA ARG A 238 26.992 -10.216 35.583 1.00 68.56 C ANISOU 1503 CA ARG A 238 5509 13184 7355 -291 -1615 -566 C ATOM 1504 C ARG A 238 27.808 -9.231 34.758 1.00 73.54 C ANISOU 1504 C ARG A 238 6111 13795 8036 -490 -1655 -541 C ATOM 1505 O ARG A 238 29.033 -9.386 34.695 1.00 74.42 O ANISOU 1505 O ARG A 238 6073 14099 8105 -555 -1656 -491 O ATOM 1506 CB ARG A 238 26.425 -11.340 34.717 1.00 67.36 C ANISOU 1506 CB ARG A 238 5390 12985 7220 -161 -1507 -479 C ATOM 1507 CG ARG A 238 26.421 -12.665 35.473 1.00 76.75 C ANISOU 1507 CG ARG A 238 6531 14287 8342 5 -1472 -438 C ATOM 1508 CD ARG A 238 25.798 -13.793 34.680 1.00 84.17 C ANISOU 1508 CD ARG A 238 7526 15145 9310 125 -1385 -367 C ATOM 1509 NE ARG A 238 26.790 -14.546 33.914 1.00 83.49 N ANISOU 1509 NE ARG A 238 7338 15159 9223 179 -1343 -301 N ATOM 1510 CZ ARG A 238 26.738 -15.857 33.700 1.00 93.31 C ANISOU 1510 CZ ARG A 238 8584 16402 10465 332 -1300 -246 C ATOM 1511 NH1 ARG A 238 25.755 -16.585 34.219 1.00 66.33 N ANISOU 1511 NH1 ARG A 238 5267 12888 7046 415 -1293 -223 N ATOM 1512 NH2 ARG A 238 27.675 -16.454 32.976 1.00 89.47 N ANISOU 1512 NH2 ARG A 238 7999 16020 9976 402 -1272 -218 N ATOM 1513 N ILE A 239 27.170 -8.188 34.181 1.00 69.78 N ANISOU 1513 N ILE A 239 5770 13101 7641 -592 -1701 -570 N ATOM 1514 CA ILE A 239 27.959 -7.186 33.452 1.00 71.00 C ANISOU 1514 CA ILE A 239 5910 13224 7842 -818 -1759 -521 C ATOM 1515 C ILE A 239 28.588 -6.188 34.468 1.00 75.75 C ANISOU 1515 C ILE A 239 6496 13841 8442 -965 -1894 -620 C ATOM 1516 O ILE A 239 29.673 -5.681 34.201 1.00 77.12 O ANISOU 1516 O ILE A 239 6581 14109 8612 -1163 -1940 -567 O ATOM 1517 CB ILE A 239 27.246 -6.472 32.266 1.00 73.76 C ANISOU 1517 CB ILE A 239 6403 13341 8280 -895 -1768 -470 C ATOM 1518 CG1 ILE A 239 26.085 -5.589 32.706 1.00 74.91 C ANISOU 1518 CG1 ILE A 239 6736 13229 8498 -860 -1860 -590 C ATOM 1519 CG2 ILE A 239 26.871 -7.431 31.137 1.00 71.70 C ANISOU 1519 CG2 ILE A 239 6124 13114 8004 -784 -1637 -372 C ATOM 1520 CD1 ILE A 239 26.255 -4.154 32.262 1.00 90.06 C ANISOU 1520 CD1 ILE A 239 8770 14938 10512 -1067 -1988 -576 C ATOM 1521 N ALA A1001 27.947 -5.957 35.640 1.00 63.94 N ANISOU 1521 N ALA A1001 5172 10255 8867 -452 -1231 -488 N ATOM 1522 CA ALA A1001 28.482 -5.085 36.702 1.00 64.40 C ANISOU 1522 CA ALA A1001 5125 10348 8996 -498 -1181 -646 C ATOM 1523 C ALA A1001 29.784 -5.667 37.296 1.00 68.70 C ANISOU 1523 C ALA A1001 5753 11021 9329 -556 -1133 -554 C ATOM 1524 O ALA A1001 30.658 -4.916 37.745 1.00 68.32 O ANISOU 1524 O ALA A1001 5652 10978 9327 -573 -1114 -612 O ATOM 1525 CB ALA A1001 27.452 -4.886 37.798 1.00 65.91 C ANISOU 1525 CB ALA A1001 5156 10667 9219 -576 -1121 -916 C ATOM 1526 N ASP A1002 29.895 -7.009 37.293 1.00 65.45 N ANISOU 1526 N ASP A1002 5452 10702 8713 -586 -1115 -413 N ATOM 1527 CA ASP A1002 31.072 -7.744 37.733 1.00 65.32 C ANISOU 1527 CA ASP A1002 5510 10787 8521 -621 -1086 -274 C ATOM 1528 C ASP A1002 32.096 -7.743 36.602 1.00 69.02 C ANISOU 1528 C ASP A1002 6090 11120 9016 -531 -1134 -109 C ATOM 1529 O ASP A1002 33.283 -7.548 36.857 1.00 69.53 O ANISOU 1529 O ASP A1002 6166 11222 9029 -533 -1125 -56 O ATOM 1530 CB ASP A1002 30.696 -9.173 38.160 1.00 67.74 C ANISOU 1530 CB ASP A1002 5863 11198 8677 -685 -1053 -174 C ATOM 1531 CG ASP A1002 29.974 -9.287 39.501 1.00 86.11 C ANISOU 1531 CG ASP A1002 8067 13746 10904 -813 -994 -294 C ATOM 1532 OD1 ASP A1002 29.689 -10.426 39.925 1.00 87.78 O ANISOU 1532 OD1 ASP A1002 8301 14045 11005 -884 -967 -174 O ATOM 1533 OD2 ASP A1002 29.681 -8.231 40.121 1.00 96.12 O ANISOU 1533 OD2 ASP A1002 9197 15103 12222 -853 -970 -516 O ATOM 1534 N LEU A1003 31.627 -7.889 35.348 1.00 64.83 N ANISOU 1534 N LEU A1003 5615 10467 8549 -463 -1185 -44 N ATOM 1535 CA LEU A1003 32.465 -7.852 34.150 1.00 63.95 C ANISOU 1535 CA LEU A1003 5580 10281 8439 -397 -1229 95 C ATOM 1536 C LEU A1003 33.164 -6.491 34.033 1.00 68.01 C ANISOU 1536 C LEU A1003 6044 10728 9070 -376 -1255 100 C ATOM 1537 O LEU A1003 34.342 -6.449 33.683 1.00 67.37 O ANISOU 1537 O LEU A1003 6008 10651 8937 -363 -1257 200 O ATOM 1538 CB LEU A1003 31.629 -8.161 32.877 1.00 63.88 C ANISOU 1538 CB LEU A1003 5593 10228 8450 -354 -1281 135 C ATOM 1539 CG LEU A1003 32.350 -8.041 31.522 1.00 68.20 C ANISOU 1539 CG LEU A1003 6182 10769 8964 -309 -1329 267 C ATOM 1540 CD1 LEU A1003 33.447 -9.083 31.368 1.00 67.96 C ANISOU 1540 CD1 LEU A1003 6228 10785 8808 -311 -1287 316 C ATOM 1541 CD2 LEU A1003 31.385 -8.125 30.379 1.00 70.13 C ANISOU 1541 CD2 LEU A1003 6396 11037 9212 -286 -1388 289 C ATOM 1542 N GLU A1004 32.442 -5.393 34.346 1.00 65.49 N ANISOU 1542 N GLU A1004 5612 10336 8936 -378 -1270 -20 N ATOM 1543 CA GLU A1004 32.955 -4.021 34.312 1.00 66.46 C ANISOU 1543 CA GLU A1004 5653 10340 9257 -366 -1290 -38 C ATOM 1544 C GLU A1004 34.114 -3.847 35.293 1.00 70.48 C ANISOU 1544 C GLU A1004 6144 10937 9700 -425 -1226 -114 C ATOM 1545 O GLU A1004 35.135 -3.280 34.922 1.00 70.91 O ANISOU 1545 O GLU A1004 6205 10932 9805 -419 -1237 -34 O ATOM 1546 CB GLU A1004 31.840 -3.018 34.631 1.00 69.42 C ANISOU 1546 CB GLU A1004 5878 10601 9898 -355 -1306 -203 C ATOM 1547 CG GLU A1004 31.026 -2.607 33.417 1.00 84.39 C ANISOU 1547 CG GLU A1004 7751 12362 11952 -277 -1403 -64 C ATOM 1548 CD GLU A1004 30.205 -1.345 33.604 1.00116.54 C ANISOU 1548 CD GLU A1004 11644 16248 16386 -241 -1437 -186 C ATOM 1549 OE1 GLU A1004 28.957 -1.440 33.552 1.00117.42 O ANISOU 1549 OE1 GLU A1004 11688 16357 16571 -211 -1464 -265 O ATOM 1550 OE2 GLU A1004 30.806 -0.260 33.783 1.00115.48 O ANISOU 1550 OE2 GLU A1004 11423 15960 16495 -243 -1436 -210 O ATOM 1551 N ASP A1005 33.968 -4.376 36.523 1.00 66.63 N ANISOU 1551 N ASP A1005 5619 10622 9076 -494 -1162 -251 N ATOM 1552 CA ASP A1005 34.973 -4.319 37.584 1.00 66.58 C ANISOU 1552 CA ASP A1005 5565 10779 8955 -566 -1106 -326 C ATOM 1553 C ASP A1005 36.223 -5.143 37.245 1.00 68.23 C ANISOU 1553 C ASP A1005 5893 11049 8982 -544 -1114 -121 C ATOM 1554 O ASP A1005 37.337 -4.667 37.498 1.00 67.87 O ANISOU 1554 O ASP A1005 5816 11046 8924 -566 -1098 -131 O ATOM 1555 CB ASP A1005 34.378 -4.798 38.917 1.00 69.25 C ANISOU 1555 CB ASP A1005 5813 11351 9148 -662 -1047 -478 C ATOM 1556 CG ASP A1005 33.453 -3.806 39.595 1.00 84.78 C ANISOU 1556 CG ASP A1005 7598 13326 11287 -712 -1011 -777 C ATOM 1557 OD1 ASP A1005 32.557 -4.250 40.341 1.00 87.54 O ANISOU 1557 OD1 ASP A1005 7878 13847 11536 -782 -973 -892 O ATOM 1558 OD2 ASP A1005 33.657 -2.578 39.418 1.00 91.63 O ANISOU 1558 OD2 ASP A1005 8375 14031 12411 -691 -1017 -905 O ATOM 1559 N ASN A1006 36.038 -6.374 36.696 1.00 62.76 N ANISOU 1559 N ASN A1006 5316 10357 8175 -504 -1132 35 N ATOM 1560 CA ASN A1006 37.138 -7.281 36.319 1.00 61.50 C ANISOU 1560 CA ASN A1006 5248 10231 7890 -469 -1138 203 C ATOM 1561 C ASN A1006 37.897 -6.725 35.126 1.00 63.95 C ANISOU 1561 C ASN A1006 5601 10432 8266 -416 -1172 283 C ATOM 1562 O ASN A1006 39.100 -6.936 35.028 1.00 61.98 O ANISOU 1562 O ASN A1006 5375 10232 7943 -404 -1165 358 O ATOM 1563 CB ASN A1006 36.635 -8.699 36.008 1.00 61.14 C ANISOU 1563 CB ASN A1006 5279 10173 7778 -445 -1140 300 C ATOM 1564 CG ASN A1006 35.830 -9.362 37.103 1.00 86.11 C ANISOU 1564 CG ASN A1006 8399 13445 10873 -514 -1108 274 C ATOM 1565 OD1 ASN A1006 36.122 -9.249 38.300 1.00 75.11 O ANISOU 1565 OD1 ASN A1006 6927 12226 9384 -585 -1080 253 O ATOM 1566 ND2 ASN A1006 34.794 -10.088 36.705 1.00 82.94 N ANISOU 1566 ND2 ASN A1006 8034 12976 10504 -510 -1110 280 N ATOM 1567 N TRP A1007 37.185 -6.026 34.214 1.00 61.55 N ANISOU 1567 N TRP A1007 5290 10001 8096 -389 -1213 286 N ATOM 1568 CA TRP A1007 37.769 -5.374 33.046 1.00 61.43 C ANISOU 1568 CA TRP A1007 5290 9911 8138 -363 -1253 401 C ATOM 1569 C TRP A1007 38.630 -4.193 33.504 1.00 66.82 C ANISOU 1569 C TRP A1007 5901 10559 8931 -401 -1237 362 C ATOM 1570 O TRP A1007 39.734 -4.014 32.995 1.00 65.37 O ANISOU 1570 O TRP A1007 5737 10393 8708 -406 -1239 459 O ATOM 1571 CB TRP A1007 36.673 -4.909 32.079 1.00 60.31 C ANISOU 1571 CB TRP A1007 5129 9673 8113 -334 -1315 453 C ATOM 1572 CG TRP A1007 37.183 -4.469 30.739 1.00 61.66 C ANISOU 1572 CG TRP A1007 5308 9835 8284 -323 -1366 631 C ATOM 1573 CD1 TRP A1007 37.261 -3.190 30.269 1.00 65.73 C ANISOU 1573 CD1 TRP A1007 5754 10241 8980 -333 -1413 738 C ATOM 1574 CD2 TRP A1007 37.677 -5.314 29.690 1.00 61.27 C ANISOU 1574 CD2 TRP A1007 5318 9913 8050 -315 -1372 726 C ATOM 1575 NE1 TRP A1007 37.776 -3.184 28.992 1.00 65.87 N ANISOU 1575 NE1 TRP A1007 5787 10342 8897 -343 -1454 932 N ATOM 1576 CE2 TRP A1007 38.044 -4.475 28.612 1.00 66.59 C ANISOU 1576 CE2 TRP A1007 5952 10600 8749 -335 -1425 900 C ATOM 1577 CE3 TRP A1007 37.851 -6.705 29.559 1.00 61.79 C ANISOU 1577 CE3 TRP A1007 5443 10080 7953 -300 -1335 672 C ATOM 1578 CZ2 TRP A1007 38.570 -4.979 27.414 1.00 66.43 C ANISOU 1578 CZ2 TRP A1007 5944 10752 8543 -353 -1436 997 C ATOM 1579 CZ3 TRP A1007 38.385 -7.203 28.379 1.00 63.87 C ANISOU 1579 CZ3 TRP A1007 5714 10469 8084 -304 -1341 729 C ATOM 1580 CH2 TRP A1007 38.735 -6.346 27.321 1.00 65.66 C ANISOU 1580 CH2 TRP A1007 5896 10768 8286 -336 -1388 879 C ATOM 1581 N GLU A1008 38.125 -3.402 34.475 1.00 65.92 N ANISOU 1581 N GLU A1008 5683 10403 8961 -440 -1213 191 N ATOM 1582 CA GLU A1008 38.832 -2.250 35.036 1.00 67.60 C ANISOU 1582 CA GLU A1008 5791 10571 9322 -492 -1184 84 C ATOM 1583 C GLU A1008 40.071 -2.697 35.819 1.00 70.74 C ANISOU 1583 C GLU A1008 6191 11160 9525 -536 -1134 50 C ATOM 1584 O GLU A1008 41.126 -2.079 35.674 1.00 69.92 O ANISOU 1584 O GLU A1008 6061 11041 9466 -563 -1124 72 O ATOM 1585 CB GLU A1008 37.895 -1.403 35.908 1.00 70.56 C ANISOU 1585 CB GLU A1008 6021 10878 9912 -528 -1159 -158 C ATOM 1586 CG GLU A1008 37.348 -0.174 35.188 1.00 89.81 C ANISOU 1586 CG GLU A1008 8378 13042 12703 -496 -1208 -131 C ATOM 1587 CD GLU A1008 36.556 -0.401 33.907 1.00122.49 C ANISOU 1587 CD GLU A1008 12589 17081 16870 -419 -1294 97 C ATOM 1588 OE1 GLU A1008 37.185 -0.452 32.825 1.00126.68 O ANISOU 1588 OE1 GLU A1008 13195 17600 17338 -403 -1340 340 O ATOM 1589 OE2 GLU A1008 35.307 -0.472 33.978 1.00118.14 O ANISOU 1589 OE2 GLU A1008 11998 16490 16401 -386 -1317 23 O ATOM 1590 N THR A1009 39.962 -3.810 36.575 1.00 66.99 N ANISOU 1590 N THR A1009 5743 10871 8840 -544 -1111 31 N ATOM 1591 CA THR A1009 41.063 -4.398 37.342 1.00 67.06 C ANISOU 1591 CA THR A1009 5739 11089 8651 -574 -1083 50 C ATOM 1592 C THR A1009 42.169 -4.862 36.363 1.00 71.10 C ANISOU 1592 C THR A1009 6343 11573 9096 -516 -1106 232 C ATOM 1593 O THR A1009 43.350 -4.685 36.662 1.00 71.43 O ANISOU 1593 O THR A1009 6345 11715 9079 -540 -1089 230 O ATOM 1594 CB THR A1009 40.528 -5.520 38.250 1.00 75.08 C ANISOU 1594 CB THR A1009 6755 12279 9493 -593 -1071 64 C ATOM 1595 OG1 THR A1009 39.522 -4.973 39.109 1.00 76.15 O ANISOU 1595 OG1 THR A1009 6780 12475 9679 -664 -1040 -136 O ATOM 1596 CG2 THR A1009 41.617 -6.174 39.099 1.00 72.99 C ANISOU 1596 CG2 THR A1009 6451 12251 9030 -621 -1060 137 C ATOM 1597 N LEU A1010 41.776 -5.399 35.190 1.00 67.10 N ANISOU 1597 N LEU A1010 5938 10958 8601 -450 -1140 357 N ATOM 1598 CA LEU A1010 42.648 -5.856 34.099 1.00 67.11 C ANISOU 1598 CA LEU A1010 6004 10956 8541 -405 -1156 488 C ATOM 1599 C LEU A1010 43.397 -4.668 33.478 1.00 71.43 C ANISOU 1599 C LEU A1010 6514 11449 9177 -440 -1160 516 C ATOM 1600 O LEU A1010 44.586 -4.791 33.185 1.00 71.37 O ANISOU 1600 O LEU A1010 6506 11519 9092 -442 -1147 565 O ATOM 1601 CB LEU A1010 41.768 -6.552 33.031 1.00 67.31 C ANISOU 1601 CB LEU A1010 6102 10912 8561 -355 -1185 553 C ATOM 1602 CG LEU A1010 42.392 -7.362 31.889 1.00 72.53 C ANISOU 1602 CG LEU A1010 6808 11615 9136 -314 -1189 629 C ATOM 1603 CD1 LEU A1010 41.353 -8.303 31.298 1.00 72.76 C ANISOU 1603 CD1 LEU A1010 6878 11613 9153 -281 -1200 617 C ATOM 1604 CD2 LEU A1010 42.855 -6.467 30.751 1.00 75.87 C ANISOU 1604 CD2 LEU A1010 7214 12046 9567 -342 -1209 705 C ATOM 1605 N ASN A1011 42.691 -3.537 33.251 1.00 68.17 N ANISOU 1605 N ASN A1011 6058 10892 8951 -469 -1179 496 N ATOM 1606 CA ASN A1011 43.251 -2.333 32.640 1.00 69.17 C ANISOU 1606 CA ASN A1011 6135 10920 9226 -514 -1190 565 C ATOM 1607 C ASN A1011 44.198 -1.621 33.577 1.00 75.62 C ANISOU 1607 C ASN A1011 6862 11769 10102 -581 -1140 435 C ATOM 1608 O ASN A1011 45.280 -1.214 33.145 1.00 76.66 O ANISOU 1608 O ASN A1011 6977 11921 10229 -619 -1129 505 O ATOM 1609 CB ASN A1011 42.154 -1.361 32.196 1.00 70.97 C ANISOU 1609 CB ASN A1011 6316 10948 9702 -515 -1236 606 C ATOM 1610 CG ASN A1011 41.182 -1.894 31.160 1.00 90.73 C ANISOU 1610 CG ASN A1011 8879 13447 12147 -462 -1296 742 C ATOM 1611 OD1 ASN A1011 41.469 -2.840 30.416 1.00 84.02 O ANISOU 1611 OD1 ASN A1011 8103 12736 11087 -439 -1302 827 O ATOM 1612 ND2 ASN A1011 39.999 -1.281 31.086 1.00 78.50 N ANISOU 1612 ND2 ASN A1011 7278 11750 10800 -442 -1339 741 N ATOM 1613 N ASP A1012 43.795 -1.457 34.853 1.00 72.29 N ANISOU 1613 N ASP A1012 6363 11384 9718 -610 -1105 229 N ATOM 1614 CA ASP A1012 44.586 -0.751 35.859 1.00 72.79 C ANISOU 1614 CA ASP A1012 6305 11525 9829 -693 -1051 46 C ATOM 1615 C ASP A1012 45.855 -1.516 36.203 1.00 74.50 C ANISOU 1615 C ASP A1012 6537 11978 9793 -695 -1032 81 C ATOM 1616 O ASP A1012 46.911 -0.890 36.234 1.00 75.25 O ANISOU 1616 O ASP A1012 6566 12102 9923 -753 -1005 43 O ATOM 1617 CB ASP A1012 43.752 -0.428 37.114 1.00 76.13 C ANISOU 1617 CB ASP A1012 6608 11995 10322 -740 -1014 -214 C ATOM 1618 CG ASP A1012 42.593 0.542 36.841 1.00 97.81 C ANISOU 1618 CG ASP A1012 9291 14476 13396 -736 -1029 -294 C ATOM 1619 OD1 ASP A1012 41.466 0.288 37.340 1.00100.66 O ANISOU 1619 OD1 ASP A1012 9630 14857 13761 -719 -1029 -401 O ATOM 1620 OD2 ASP A1012 42.809 1.547 36.116 1.00105.70 O ANISOU 1620 OD2 ASP A1012 10252 15245 14664 -748 -1044 -230 O ATOM 1621 N ASN A1013 45.784 -2.854 36.389 1.00 69.00 N ANISOU 1621 N ASN A1013 5915 11426 8877 -632 -1049 167 N ATOM 1622 CA ASN A1013 46.966 -3.682 36.699 1.00 68.41 C ANISOU 1622 CA ASN A1013 5838 11554 8601 -611 -1046 231 C ATOM 1623 C ASN A1013 47.945 -3.710 35.520 1.00 71.27 C ANISOU 1623 C ASN A1013 6250 11872 8956 -582 -1054 357 C ATOM 1624 O ASN A1013 49.153 -3.810 35.739 1.00 70.91 O ANISOU 1624 O ASN A1013 6154 11969 8820 -593 -1039 355 O ATOM 1625 CB ASN A1013 46.582 -5.105 37.113 1.00 68.92 C ANISOU 1625 CB ASN A1013 5954 11722 8512 -545 -1069 325 C ATOM 1626 CG ASN A1013 46.210 -5.224 38.574 1.00 87.98 C ANISOU 1626 CG ASN A1013 8269 14334 10827 -606 -1055 231 C ATOM 1627 OD1 ASN A1013 47.069 -5.347 39.447 1.00 91.19 O ANISOU 1627 OD1 ASN A1013 8578 14973 11096 -642 -1049 219 O ATOM 1628 ND2 ASN A1013 44.926 -5.164 38.882 1.00 71.46 N ANISOU 1628 ND2 ASN A1013 6177 12193 8784 -630 -1049 157 N ATOM 1629 N LEU A1014 47.421 -3.563 34.285 1.00 67.22 N ANISOU 1629 N LEU A1014 5816 11200 8526 -556 -1077 460 N ATOM 1630 CA LEU A1014 48.193 -3.495 33.040 1.00 67.10 C ANISOU 1630 CA LEU A1014 5829 11183 8485 -556 -1082 579 C ATOM 1631 C LEU A1014 49.002 -2.184 32.986 1.00 70.95 C ANISOU 1631 C LEU A1014 6233 11636 9088 -654 -1056 559 C ATOM 1632 O LEU A1014 50.096 -2.164 32.410 1.00 72.24 O ANISOU 1632 O LEU A1014 6378 11890 9178 -679 -1040 616 O ATOM 1633 CB LEU A1014 47.242 -3.615 31.825 1.00 67.08 C ANISOU 1633 CB LEU A1014 5897 11076 8514 -528 -1120 696 C ATOM 1634 CG LEU A1014 47.805 -3.604 30.385 1.00 72.02 C ANISOU 1634 CG LEU A1014 6533 11764 9066 -548 -1128 830 C ATOM 1635 CD1 LEU A1014 48.986 -4.564 30.208 1.00 71.11 C ANISOU 1635 CD1 LEU A1014 6409 11824 8784 -513 -1098 798 C ATOM 1636 CD2 LEU A1014 46.703 -3.932 29.392 1.00 75.50 C ANISOU 1636 CD2 LEU A1014 7023 12176 9488 -521 -1171 917 C ATOM 1637 N LYS A1015 48.470 -1.105 33.596 1.00 65.65 N ANISOU 1637 N LYS A1015 5493 10830 8621 -716 -1045 456 N ATOM 1638 CA LYS A1015 49.143 0.191 33.673 1.00 66.16 C ANISOU 1638 CA LYS A1015 5455 10811 8873 -820 -1011 403 C ATOM 1639 C LYS A1015 50.323 0.121 34.664 1.00 71.12 C ANISOU 1639 C LYS A1015 5993 11645 9383 -865 -962 244 C ATOM 1640 O LYS A1015 51.383 0.694 34.401 1.00 70.27 O ANISOU 1640 O LYS A1015 5828 11564 9308 -938 -933 252 O ATOM 1641 CB LYS A1015 48.163 1.301 34.093 1.00 68.51 C ANISOU 1641 CB LYS A1015 5672 10879 9481 -863 -1008 287 C ATOM 1642 CG LYS A1015 47.068 1.622 33.082 1.00 73.69 C ANISOU 1642 CG LYS A1015 6377 11315 10308 -826 -1068 470 C ATOM 1643 CD LYS A1015 46.467 3.009 33.322 1.00 85.29 C ANISOU 1643 CD LYS A1015 7720 12499 12188 -880 -1065 384 C ATOM 1644 CE LYS A1015 45.266 3.024 34.244 1.00100.55 C ANISOU 1644 CE LYS A1015 9601 14370 14234 -844 -1058 159 C ATOM 1645 NZ LYS A1015 44.007 2.678 33.528 1.00110.89 N ANISOU 1645 NZ LYS A1015 10988 15585 15560 -756 -1131 320 N ATOM 1646 N VAL A1016 50.114 -0.607 35.794 1.00 68.63 N ANISOU 1646 N VAL A1016 5656 11503 8917 -831 -958 119 N ATOM 1647 CA VAL A1016 51.032 -0.811 36.920 1.00 69.08 C ANISOU 1647 CA VAL A1016 5605 11823 8820 -870 -929 -19 C ATOM 1648 C VAL A1016 52.320 -1.498 36.443 1.00 74.39 C ANISOU 1648 C VAL A1016 6298 12646 9320 -829 -938 105 C ATOM 1649 O VAL A1016 53.401 -0.998 36.758 1.00 75.35 O ANISOU 1649 O VAL A1016 6314 12889 9426 -901 -904 16 O ATOM 1650 CB VAL A1016 50.348 -1.586 38.089 1.00 72.27 C ANISOU 1650 CB VAL A1016 5982 12406 9071 -843 -942 -92 C ATOM 1651 CG1 VAL A1016 51.329 -1.901 39.217 1.00 72.83 C ANISOU 1651 CG1 VAL A1016 5922 12814 8938 -885 -929 -178 C ATOM 1652 CG2 VAL A1016 49.149 -0.816 38.634 1.00 72.48 C ANISOU 1652 CG2 VAL A1016 5950 12321 9269 -900 -919 -275 C ATOM 1653 N ILE A1017 52.211 -2.604 35.670 1.00 70.91 N ANISOU 1653 N ILE A1017 5972 12198 8773 -719 -976 276 N ATOM 1654 CA ILE A1017 53.365 -3.341 35.121 1.00 71.10 C ANISOU 1654 CA ILE A1017 5998 12350 8668 -664 -981 364 C ATOM 1655 C ILE A1017 54.286 -2.368 34.347 1.00 76.79 C ANISOU 1655 C ILE A1017 6673 13051 9454 -757 -943 363 C ATOM 1656 O ILE A1017 55.499 -2.422 34.530 1.00 77.75 O ANISOU 1656 O ILE A1017 6711 13341 9489 -776 -924 325 O ATOM 1657 CB ILE A1017 52.938 -4.553 34.231 1.00 73.55 C ANISOU 1657 CB ILE A1017 6416 12603 8926 -548 -1013 493 C ATOM 1658 CG1 ILE A1017 51.998 -5.525 34.981 1.00 73.12 C ANISOU 1658 CG1 ILE A1017 6402 12539 8842 -470 -1046 516 C ATOM 1659 CG2 ILE A1017 54.168 -5.298 33.672 1.00 75.01 C ANISOU 1659 CG2 ILE A1017 6564 12920 9016 -490 -1008 527 C ATOM 1660 CD1 ILE A1017 51.159 -6.414 34.054 1.00 79.24 C ANISOU 1660 CD1 ILE A1017 7285 13182 9642 -389 -1066 596 C ATOM 1661 N GLU A1018 53.709 -1.464 33.526 1.00 73.82 N ANISOU 1661 N GLU A1018 6336 12476 9237 -822 -938 424 N ATOM 1662 CA GLU A1018 54.456 -0.471 32.752 1.00 74.76 C ANISOU 1662 CA GLU A1018 6407 12553 9447 -933 -906 479 C ATOM 1663 C GLU A1018 55.195 0.527 33.661 1.00 78.62 C ANISOU 1663 C GLU A1018 6760 13066 10045 -1047 -857 310 C ATOM 1664 O GLU A1018 56.371 0.818 33.414 1.00 79.34 O ANISOU 1664 O GLU A1018 6780 13266 10098 -1117 -822 303 O ATOM 1665 CB GLU A1018 53.518 0.293 31.791 1.00 76.93 C ANISOU 1665 CB GLU A1018 6732 12597 9901 -977 -930 633 C ATOM 1666 CG GLU A1018 54.249 0.938 30.617 1.00 91.85 C ANISOU 1666 CG GLU A1018 8591 14494 11814 -1081 -915 802 C ATOM 1667 CD GLU A1018 53.537 2.036 29.845 1.00118.81 C ANISOU 1667 CD GLU A1018 11996 17673 15472 -1164 -942 992 C ATOM 1668 OE1 GLU A1018 54.243 2.902 29.277 1.00110.52 O ANISOU 1668 OE1 GLU A1018 10878 16604 14511 -1290 -920 1120 O ATOM 1669 OE2 GLU A1018 52.285 2.022 29.782 1.00116.58 O ANISOU 1669 OE2 GLU A1018 11762 17229 15302 -1106 -989 1033 O ATOM 1670 N LYS A1019 54.511 1.047 34.699 1.00 74.79 N ANISOU 1670 N LYS A1019 6220 12503 9694 -1076 -847 143 N ATOM 1671 CA LYS A1019 55.071 2.056 35.606 1.00 76.28 C ANISOU 1671 CA LYS A1019 6249 12719 10016 -1200 -790 -83 C ATOM 1672 C LYS A1019 55.697 1.438 36.893 1.00 82.98 C ANISOU 1672 C LYS A1019 6999 13900 10631 -1188 -781 -261 C ATOM 1673 O LYS A1019 55.996 2.171 37.846 1.00 84.44 O ANISOU 1673 O LYS A1019 7026 14173 10885 -1295 -733 -505 O ATOM 1674 CB LYS A1019 54.001 3.112 35.958 1.00 78.38 C ANISOU 1674 CB LYS A1019 6460 12718 10603 -1261 -773 -213 C ATOM 1675 CG LYS A1019 53.518 3.904 34.742 1.00 82.56 C ANISOU 1675 CG LYS A1019 7041 12918 11410 -1290 -792 -2 C ATOM 1676 CD LYS A1019 52.777 5.170 35.109 1.00 90.98 C ANISOU 1676 CD LYS A1019 7992 13681 12894 -1366 -767 -152 C ATOM 1677 CE LYS A1019 52.176 5.822 33.887 1.00100.64 C ANISOU 1677 CE LYS A1019 9262 14583 14393 -1372 -813 135 C ATOM 1678 NZ LYS A1019 51.299 6.976 34.236 1.00108.04 N ANISOU 1678 NZ LYS A1019 10074 15172 15803 -1415 -801 2 N ATOM 1679 N ALA A1020 55.928 0.113 36.896 1.00 78.78 N ANISOU 1679 N ALA A1020 6533 13558 9841 -1065 -828 -136 N ATOM 1680 CA ALA A1020 56.504 -0.598 38.037 1.00 78.81 C ANISOU 1680 CA ALA A1020 6436 13887 9620 -1038 -844 -214 C ATOM 1681 C ALA A1020 57.939 -0.159 38.323 1.00 84.36 C ANISOU 1681 C ALA A1020 6990 14800 10264 -1122 -808 -324 C ATOM 1682 O ALA A1020 58.690 0.178 37.404 1.00 84.27 O ANISOU 1682 O ALA A1020 6993 14713 10312 -1153 -783 -264 O ATOM 1683 CB ALA A1020 56.460 -2.092 37.798 1.00 78.20 C ANISOU 1683 CB ALA A1020 6455 13889 9370 -878 -908 -13 C ATOM 1684 N ASP A1021 58.299 -0.167 39.623 1.00 81.80 N ANISOU 1684 N ASP A1021 6502 14779 9799 -1174 -804 -489 N ATOM 1685 CA ASP A1021 59.588 0.202 40.212 1.00 82.83 C ANISOU 1685 CA ASP A1021 6446 15194 9832 -1264 -776 -639 C ATOM 1686 C ASP A1021 60.372 -1.035 40.690 1.00 86.04 C ANISOU 1686 C ASP A1021 6795 15934 9962 -1150 -848 -497 C ATOM 1687 O ASP A1021 61.603 -1.010 40.707 1.00 87.37 O ANISOU 1687 O ASP A1021 6854 16294 10050 -1168 -843 -524 O ATOM 1688 CB ASP A1021 59.342 1.145 41.405 1.00 86.76 C ANISOU 1688 CB ASP A1021 6755 15840 10368 -1424 -720 -961 C ATOM 1689 CG ASP A1021 60.248 2.354 41.426 1.00107.63 C ANISOU 1689 CG ASP A1021 9242 18490 13162 -1590 -638 -1202 C ATOM 1690 OD1 ASP A1021 59.943 3.334 40.714 1.00109.20 O ANISOU 1690 OD1 ASP A1021 9483 18331 13677 -1665 -582 -1252 O ATOM 1691 OD2 ASP A1021 61.276 2.319 42.152 1.00119.73 O ANISOU 1691 OD2 ASP A1021 10594 20389 14507 -1650 -632 -1328 O ATOM 1692 N ASN A1022 59.658 -2.093 41.108 1.00 80.69 N ANISOU 1692 N ASN A1022 6174 15321 9164 -1038 -917 -338 N ATOM 1693 CA ASN A1022 60.217 -3.336 41.645 1.00 80.13 C ANISOU 1693 CA ASN A1022 6037 15524 8887 -918 -1002 -148 C ATOM 1694 C ASN A1022 59.821 -4.540 40.816 1.00 80.75 C ANISOU 1694 C ASN A1022 6285 15374 9024 -736 -1058 114 C ATOM 1695 O ASN A1022 58.811 -4.490 40.108 1.00 78.50 O ANISOU 1695 O ASN A1022 6167 14788 8873 -715 -1038 142 O ATOM 1696 CB ASN A1022 59.698 -3.569 43.078 1.00 82.27 C ANISOU 1696 CB ASN A1022 6177 16114 8967 -971 -1039 -169 C ATOM 1697 CG ASN A1022 59.827 -2.397 44.003 1.00111.35 C ANISOU 1697 CG ASN A1022 9668 20047 12594 -1170 -973 -495 C ATOM 1698 OD1 ASN A1022 60.851 -2.217 44.678 1.00116.63 O ANISOU 1698 OD1 ASN A1022 10132 21084 13098 -1240 -979 -592 O ATOM 1699 ND2 ASN A1022 58.780 -1.586 44.070 1.00 97.47 N ANISOU 1699 ND2 ASN A1022 7947 18105 10981 -1266 -908 -693 N ATOM 1700 N ALA A1023 60.555 -5.657 40.983 1.00 76.51 N ANISOU 1700 N ALA A1023 5682 14989 8400 -604 -1131 299 N ATOM 1701 CA ALA A1023 60.213 -6.932 40.358 1.00 75.10 C ANISOU 1701 CA ALA A1023 5617 14606 8312 -428 -1184 521 C ATOM 1702 C ALA A1023 58.929 -7.509 41.011 1.00 78.01 C ANISOU 1702 C ALA A1023 6047 14932 8659 -407 -1225 654 C ATOM 1703 O ALA A1023 58.066 -8.053 40.324 1.00 75.44 O ANISOU 1703 O ALA A1023 5875 14326 8463 -329 -1227 739 O ATOM 1704 CB ALA A1023 61.369 -7.903 40.506 1.00 77.05 C ANISOU 1704 CB ALA A1023 5729 15017 8529 -297 -1253 666 C ATOM 1705 N ALA A1024 58.797 -7.340 42.338 1.00 76.57 N ANISOU 1705 N ALA A1024 5728 15067 8300 -497 -1253 652 N ATOM 1706 CA ALA A1024 57.658 -7.822 43.116 1.00 77.14 C ANISOU 1706 CA ALA A1024 5818 15189 8305 -513 -1288 776 C ATOM 1707 C ALA A1024 56.378 -7.105 42.725 1.00 80.76 C ANISOU 1707 C ALA A1024 6424 15397 8865 -591 -1216 608 C ATOM 1708 O ALA A1024 55.297 -7.686 42.822 1.00 80.16 O ANISOU 1708 O ALA A1024 6437 15203 8819 -560 -1235 724 O ATOM 1709 CB ALA A1024 57.923 -7.636 44.598 1.00 80.01 C ANISOU 1709 CB ALA A1024 5958 16038 8406 -630 -1322 772 C ATOM 1710 N GLN A1025 56.504 -5.845 42.284 1.00 77.00 N ANISOU 1710 N GLN A1025 5960 14829 8467 -692 -1138 348 N ATOM 1711 CA GLN A1025 55.396 -5.003 41.842 1.00 75.60 C ANISOU 1711 CA GLN A1025 5894 14390 8441 -761 -1075 185 C ATOM 1712 C GLN A1025 54.830 -5.538 40.506 1.00 76.05 C ANISOU 1712 C GLN A1025 6159 14068 8667 -641 -1083 323 C ATOM 1713 O GLN A1025 53.605 -5.639 40.356 1.00 74.75 O ANISOU 1713 O GLN A1025 6097 13730 8575 -635 -1079 334 O ATOM 1714 CB GLN A1025 55.902 -3.564 41.698 1.00 78.05 C ANISOU 1714 CB GLN A1025 6126 14686 8842 -894 -999 -84 C ATOM 1715 CG GLN A1025 54.974 -2.503 42.258 1.00104.55 C ANISOU 1715 CG GLN A1025 9427 18008 12290 -1029 -939 -340 C ATOM 1716 CD GLN A1025 55.401 -1.130 41.795 1.00129.54 C ANISOU 1716 CD GLN A1025 12544 21010 15666 -1137 -865 -563 C ATOM 1717 OE1 GLN A1025 56.508 -0.650 42.097 1.00121.57 O ANISOU 1717 OE1 GLN A1025 11392 20190 14608 -1217 -836 -690 O ATOM 1718 NE2 GLN A1025 54.531 -0.476 41.029 1.00125.13 N ANISOU 1718 NE2 GLN A1025 12092 20088 15365 -1144 -835 -597 N ATOM 1719 N VAL A1026 55.743 -5.904 39.555 1.00 70.49 N ANISOU 1719 N VAL A1026 5494 13279 8011 -554 -1091 405 N ATOM 1720 CA VAL A1026 55.458 -6.482 38.234 1.00 68.34 C ANISOU 1720 CA VAL A1026 5371 12735 7860 -451 -1093 503 C ATOM 1721 C VAL A1026 54.749 -7.823 38.427 1.00 71.44 C ANISOU 1721 C VAL A1026 5819 13066 8261 -338 -1146 674 C ATOM 1722 O VAL A1026 53.661 -8.030 37.887 1.00 69.39 O ANISOU 1722 O VAL A1026 5682 12597 8087 -316 -1139 694 O ATOM 1723 CB VAL A1026 56.751 -6.659 37.376 1.00 72.77 C ANISOU 1723 CB VAL A1026 5899 13318 8432 -400 -1083 513 C ATOM 1724 CG1 VAL A1026 56.463 -7.365 36.056 1.00 71.84 C ANISOU 1724 CG1 VAL A1026 5896 12991 8409 -307 -1079 575 C ATOM 1725 CG2 VAL A1026 57.449 -5.333 37.116 1.00 73.20 C ANISOU 1725 CG2 VAL A1026 5898 13419 8497 -530 -1025 366 C ATOM 1726 N LYS A1027 55.385 -8.727 39.204 1.00 69.96 N ANISOU 1726 N LYS A1027 5523 13061 8000 -270 -1202 814 N ATOM 1727 CA LYS A1027 54.907 -10.076 39.501 1.00 70.34 C ANISOU 1727 CA LYS A1027 5581 13050 8093 -164 -1261 1025 C ATOM 1728 C LYS A1027 53.492 -10.065 40.127 1.00 73.54 C ANISOU 1728 C LYS A1027 6043 13434 8464 -232 -1261 1052 C ATOM 1729 O LYS A1027 52.650 -10.852 39.692 1.00 72.23 O ANISOU 1729 O LYS A1027 5977 13052 8415 -168 -1269 1140 O ATOM 1730 CB LYS A1027 55.909 -10.804 40.409 1.00 74.88 C ANISOU 1730 CB LYS A1027 5985 13873 8594 -105 -1334 1201 C ATOM 1731 CG LYS A1027 55.916 -12.321 40.232 1.00 96.70 C ANISOU 1731 CG LYS A1027 8738 16474 11531 55 -1396 1436 C ATOM 1732 CD LYS A1027 55.169 -13.059 41.359 1.00108.68 C ANISOU 1732 CD LYS A1027 10207 18082 13004 42 -1461 1690 C ATOM 1733 CE LYS A1027 55.423 -14.551 41.332 1.00115.72 C ANISOU 1733 CE LYS A1027 11040 18806 14121 201 -1533 1962 C ATOM 1734 NZ LYS A1027 54.895 -15.230 42.544 1.00121.13 N ANISOU 1734 NZ LYS A1027 11640 19639 14746 169 -1610 2280 N ATOM 1735 N ASP A1028 53.218 -9.145 41.083 1.00 70.69 N ANISOU 1735 N ASP A1028 5606 13297 7955 -371 -1241 935 N ATOM 1736 CA ASP A1028 51.922 -9.036 41.767 1.00 70.90 C ANISOU 1736 CA ASP A1028 5650 13362 7929 -455 -1230 916 C ATOM 1737 C ASP A1028 50.802 -8.568 40.820 1.00 71.91 C ANISOU 1737 C ASP A1028 5937 13176 8211 -461 -1182 785 C ATOM 1738 O ASP A1028 49.739 -9.191 40.784 1.00 70.57 O ANISOU 1738 O ASP A1028 5841 12887 8085 -440 -1191 865 O ATOM 1739 CB ASP A1028 52.015 -8.104 42.993 1.00 74.78 C ANISOU 1739 CB ASP A1028 5974 14212 8228 -614 -1208 753 C ATOM 1740 CG ASP A1028 50.693 -7.853 43.710 1.00 93.50 C ANISOU 1740 CG ASP A1028 8330 16656 10539 -721 -1180 661 C ATOM 1741 OD1 ASP A1028 50.360 -6.666 43.944 1.00 95.08 O ANISOU 1741 OD1 ASP A1028 8478 16893 10756 -836 -1116 371 O ATOM 1742 OD2 ASP A1028 49.976 -8.843 44.013 1.00101.71 O ANISOU 1742 OD2 ASP A1028 9401 17697 11547 -693 -1217 868 O ATOM 1743 N ALA A1029 51.041 -7.478 40.062 1.00 67.25 N ANISOU 1743 N ALA A1029 5383 12462 7707 -496 -1135 607 N ATOM 1744 CA ALA A1029 50.088 -6.915 39.105 1.00 65.33 C ANISOU 1744 CA ALA A1029 5263 11942 7616 -502 -1105 519 C ATOM 1745 C ALA A1029 49.727 -7.926 38.012 1.00 68.74 C ANISOU 1745 C ALA A1029 5826 12156 8135 -386 -1127 655 C ATOM 1746 O ALA A1029 48.617 -7.862 37.475 1.00 69.37 O ANISOU 1746 O ALA A1029 5997 12062 8298 -384 -1120 633 O ATOM 1747 CB ALA A1029 50.659 -5.660 38.482 1.00 66.03 C ANISOU 1747 CB ALA A1029 5339 11956 7795 -560 -1065 380 C ATOM 1748 N LEU A1030 50.650 -8.862 37.693 1.00 63.35 N ANISOU 1748 N LEU A1030 5132 11492 7448 -291 -1151 771 N ATOM 1749 CA LEU A1030 50.423 -9.927 36.719 1.00 61.34 C ANISOU 1749 CA LEU A1030 4958 11051 7299 -185 -1162 848 C ATOM 1750 C LEU A1030 49.472 -10.995 37.275 1.00 64.34 C ANISOU 1750 C LEU A1030 5360 11371 7717 -149 -1190 970 C ATOM 1751 O LEU A1030 48.547 -11.372 36.562 1.00 64.35 O ANISOU 1751 O LEU A1030 5450 11189 7809 -125 -1179 951 O ATOM 1752 CB LEU A1030 51.737 -10.571 36.262 1.00 61.54 C ANISOU 1752 CB LEU A1030 4923 11109 7352 -95 -1171 888 C ATOM 1753 CG LEU A1030 52.457 -9.898 35.091 1.00 64.61 C ANISOU 1753 CG LEU A1030 5323 11485 7742 -114 -1132 775 C ATOM 1754 CD1 LEU A1030 53.913 -10.363 35.010 1.00 65.60 C ANISOU 1754 CD1 LEU A1030 5338 11724 7861 -48 -1138 784 C ATOM 1755 CD2 LEU A1030 51.752 -10.161 33.780 1.00 62.78 C ANISOU 1755 CD2 LEU A1030 5182 11089 7582 -93 -1111 729 C ATOM 1756 N THR A1031 49.662 -11.458 38.533 1.00 61.02 N ANISOU 1756 N THR A1031 4845 11123 7217 -161 -1226 1105 N ATOM 1757 CA THR A1031 48.782 -12.473 39.149 1.00 61.57 C ANISOU 1757 CA THR A1031 4917 11155 7322 -151 -1254 1270 C ATOM 1758 C THR A1031 47.359 -11.909 39.357 1.00 65.35 C ANISOU 1758 C THR A1031 5459 11611 7760 -249 -1223 1167 C ATOM 1759 O THR A1031 46.383 -12.654 39.210 1.00 64.82 O ANISOU 1759 O THR A1031 5451 11399 7779 -234 -1224 1231 O ATOM 1760 CB THR A1031 49.334 -13.036 40.476 1.00 70.12 C ANISOU 1760 CB THR A1031 5856 12486 8299 -164 -1311 1490 C ATOM 1761 OG1 THR A1031 48.954 -12.191 41.558 1.00 71.75 O ANISOU 1761 OG1 THR A1031 5991 12978 8293 -306 -1299 1422 O ATOM 1762 CG2 THR A1031 50.855 -13.298 40.461 1.00 67.11 C ANISOU 1762 CG2 THR A1031 5372 12193 7933 -78 -1349 1569 C ATOM 1763 N LYS A1032 47.258 -10.594 39.701 1.00 61.24 N ANISOU 1763 N LYS A1032 4907 11225 7137 -349 -1193 990 N ATOM 1764 CA LYS A1032 45.989 -9.866 39.881 1.00 60.00 C ANISOU 1764 CA LYS A1032 4776 11043 6977 -437 -1160 843 C ATOM 1765 C LYS A1032 45.274 -9.748 38.534 1.00 62.73 C ANISOU 1765 C LYS A1032 5254 11103 7479 -384 -1146 774 C ATOM 1766 O LYS A1032 44.066 -9.932 38.460 1.00 61.28 O ANISOU 1766 O LYS A1032 5118 10827 7339 -400 -1140 752 O ATOM 1767 CB LYS A1032 46.214 -8.470 40.498 1.00 61.70 C ANISOU 1767 CB LYS A1032 4891 11432 7120 -546 -1126 635 C ATOM 1768 CG LYS A1032 46.682 -8.483 41.954 1.00 66.82 C ANISOU 1768 CG LYS A1032 5372 12451 7564 -638 -1133 651 C ATOM 1769 CD LYS A1032 46.061 -7.342 42.732 1.00 73.96 C ANISOU 1769 CD LYS A1032 6164 13516 8420 -777 -1081 383 C ATOM 1770 CE LYS A1032 46.962 -6.761 43.787 1.00 84.29 C ANISOU 1770 CE LYS A1032 7281 15190 9555 -884 -1066 263 C ATOM 1771 NZ LYS A1032 47.750 -5.619 43.254 1.00 94.51 N ANISOU 1771 NZ LYS A1032 8559 16375 10975 -892 -1032 70 N ATOM 1772 N MET A1033 46.039 -9.468 37.472 1.00 60.33 N ANISOU 1772 N MET A1033 4991 10695 7235 -330 -1144 749 N ATOM 1773 CA MET A1033 45.566 -9.371 36.098 1.00 60.11 C ANISOU 1773 CA MET A1033 5060 10471 7310 -290 -1138 710 C ATOM 1774 C MET A1033 45.064 -10.743 35.635 1.00 64.67 C ANISOU 1774 C MET A1033 5691 10931 7950 -218 -1148 789 C ATOM 1775 O MET A1033 43.989 -10.824 35.032 1.00 64.39 O ANISOU 1775 O MET A1033 5716 10779 7970 -219 -1145 745 O ATOM 1776 CB MET A1033 46.700 -8.872 35.201 1.00 62.89 C ANISOU 1776 CB MET A1033 5406 10825 7665 -274 -1130 689 C ATOM 1777 CG MET A1033 46.225 -8.082 34.033 1.00 66.93 C ANISOU 1777 CG MET A1033 5970 11223 8236 -295 -1127 647 C ATOM 1778 SD MET A1033 47.593 -7.537 32.977 1.00 72.09 S ANISOU 1778 SD MET A1033 6599 11930 8863 -306 -1113 658 S ATOM 1779 CE MET A1033 46.672 -7.282 31.461 1.00 68.53 C ANISOU 1779 CE MET A1033 6207 11385 8445 -319 -1129 688 C ATOM 1780 N ARG A1034 45.823 -11.824 35.980 1.00 61.23 N ANISOU 1780 N ARG A1034 5212 10521 7530 -157 -1162 902 N ATOM 1781 CA ARG A1034 45.522 -13.237 35.692 1.00 60.77 C ANISOU 1781 CA ARG A1034 5169 10319 7602 -86 -1167 977 C ATOM 1782 C ARG A1034 44.141 -13.591 36.281 1.00 62.72 C ANISOU 1782 C ARG A1034 5445 10521 7865 -138 -1167 1019 C ATOM 1783 O ARG A1034 43.266 -14.023 35.523 1.00 62.56 O ANISOU 1783 O ARG A1034 5480 10352 7936 -127 -1151 955 O ATOM 1784 CB ARG A1034 46.669 -14.142 36.240 1.00 62.41 C ANISOU 1784 CB ARG A1034 5286 10564 7864 -13 -1195 1125 C ATOM 1785 CG ARG A1034 46.477 -15.676 36.335 1.00 71.79 C ANISOU 1785 CG ARG A1034 6443 11579 9256 60 -1210 1259 C ATOM 1786 CD ARG A1034 46.191 -16.345 35.009 1.00 79.33 C ANISOU 1786 CD ARG A1034 7432 12319 10389 117 -1173 1108 C ATOM 1787 NE ARG A1034 46.832 -17.652 34.817 1.00 78.38 N ANISOU 1787 NE ARG A1034 7224 12032 10525 224 -1179 1160 N ATOM 1788 CZ ARG A1034 46.339 -18.823 35.221 1.00 82.66 C ANISOU 1788 CZ ARG A1034 7727 12389 11290 252 -1191 1300 C ATOM 1789 NH1 ARG A1034 46.964 -19.950 34.921 1.00 65.08 N ANISOU 1789 NH1 ARG A1034 5399 9965 9363 359 -1193 1315 N ATOM 1790 NH2 ARG A1034 45.232 -18.870 35.955 1.00 64.76 N ANISOU 1790 NH2 ARG A1034 5505 10129 8973 168 -1201 1428 N ATOM 1791 N ALA A1035 43.918 -13.293 37.589 1.00 58.00 N ANISOU 1791 N ALA A1035 4792 10092 7151 -214 -1179 1096 N ATOM 1792 CA ALA A1035 42.666 -13.541 38.325 1.00 57.32 C ANISOU 1792 CA ALA A1035 4704 10035 7039 -291 -1173 1135 C ATOM 1793 C ALA A1035 41.441 -12.776 37.750 1.00 60.19 C ANISOU 1793 C ALA A1035 5133 10320 7415 -334 -1147 950 C ATOM 1794 O ALA A1035 40.362 -13.365 37.649 1.00 59.60 O ANISOU 1794 O ALA A1035 5090 10155 7402 -353 -1137 957 O ATOM 1795 CB ALA A1035 42.845 -13.187 39.787 1.00 58.63 C ANISOU 1795 CB ALA A1035 4762 10488 7026 -385 -1184 1211 C ATOM 1796 N ALA A1036 41.615 -11.479 37.389 1.00 55.56 N ANISOU 1796 N ALA A1036 4551 9762 6796 -349 -1139 801 N ATOM 1797 CA ALA A1036 40.575 -10.608 36.833 1.00 54.29 C ANISOU 1797 CA ALA A1036 4424 9519 6683 -376 -1131 655 C ATOM 1798 C ALA A1036 40.127 -11.097 35.461 1.00 59.62 C ANISOU 1798 C ALA A1036 5180 10023 7452 -315 -1139 644 C ATOM 1799 O ALA A1036 38.928 -11.088 35.180 1.00 59.26 O ANISOU 1799 O ALA A1036 5155 9913 7448 -332 -1139 584 O ATOM 1800 CB ALA A1036 41.077 -9.175 36.738 1.00 54.56 C ANISOU 1800 CB ALA A1036 4422 9589 6721 -402 -1128 546 C ATOM 1801 N ALA A1037 41.079 -11.545 34.615 1.00 56.97 N ANISOU 1801 N ALA A1037 4866 9644 7137 -250 -1142 680 N ATOM 1802 CA ALA A1037 40.787 -12.072 33.280 1.00 56.94 C ANISOU 1802 CA ALA A1037 4902 9543 7191 -209 -1140 632 C ATOM 1803 C ALA A1037 39.853 -13.299 33.353 1.00 61.53 C ANISOU 1803 C ALA A1037 5495 10026 7856 -205 -1126 632 C ATOM 1804 O ALA A1037 38.856 -13.346 32.638 1.00 59.97 O ANISOU 1804 O ALA A1037 5319 9784 7684 -219 -1126 550 O ATOM 1805 CB ALA A1037 42.083 -12.437 32.567 1.00 58.04 C ANISOU 1805 CB ALA A1037 5023 9699 7332 -154 -1132 637 C ATOM 1806 N LEU A1038 40.158 -14.263 34.248 1.00 60.54 N ANISOU 1806 N LEU A1038 5342 9875 7784 -195 -1119 743 N ATOM 1807 CA LEU A1038 39.363 -15.485 34.427 1.00 61.59 C ANISOU 1807 CA LEU A1038 5472 9887 8044 -204 -1102 781 C ATOM 1808 C LEU A1038 38.031 -15.178 35.115 1.00 65.32 C ANISOU 1808 C LEU A1038 5953 10405 8462 -290 -1098 775 C ATOM 1809 O LEU A1038 37.047 -15.899 34.890 1.00 65.92 O ANISOU 1809 O LEU A1038 6037 10382 8628 -316 -1080 742 O ATOM 1810 CB LEU A1038 40.142 -16.550 35.209 1.00 63.18 C ANISOU 1810 CB LEU A1038 5618 10041 8347 -171 -1109 964 C ATOM 1811 CG LEU A1038 41.452 -17.008 34.578 1.00 68.74 C ANISOU 1811 CG LEU A1038 6284 10680 9152 -74 -1110 952 C ATOM 1812 CD1 LEU A1038 42.462 -17.309 35.622 1.00 70.02 C ANISOU 1812 CD1 LEU A1038 6377 10904 9321 -44 -1143 1161 C ATOM 1813 CD2 LEU A1038 41.251 -18.202 33.672 1.00 72.27 C ANISOU 1813 CD2 LEU A1038 6706 10916 9836 -26 -1077 848 C ATOM 1814 N ASP A1039 37.993 -14.101 35.934 1.00 60.14 N ANISOU 1814 N ASP A1039 5275 9905 7670 -342 -1109 773 N ATOM 1815 CA ASP A1039 36.761 -13.646 36.583 1.00 59.50 C ANISOU 1815 CA ASP A1039 5172 9899 7536 -427 -1098 712 C ATOM 1816 C ASP A1039 35.860 -12.950 35.547 1.00 60.92 C ANISOU 1816 C ASP A1039 5384 10007 7754 -412 -1107 551 C ATOM 1817 O ASP A1039 34.647 -13.151 35.576 1.00 60.24 O ANISOU 1817 O ASP A1039 5293 9897 7699 -452 -1096 492 O ATOM 1818 CB ASP A1039 37.048 -12.726 37.784 1.00 61.45 C ANISOU 1818 CB ASP A1039 5345 10354 7648 -494 -1096 703 C ATOM 1819 CG ASP A1039 37.029 -13.426 39.132 1.00 75.75 C ANISOU 1819 CG ASP A1039 7082 12331 9366 -577 -1087 856 C ATOM 1820 OD1 ASP A1039 37.694 -12.930 40.065 1.00 78.22 O ANISOU 1820 OD1 ASP A1039 7314 12859 9545 -625 -1090 882 O ATOM 1821 OD2 ASP A1039 36.343 -14.468 39.255 1.00 82.45 O ANISOU 1821 OD2 ASP A1039 7939 13115 10274 -607 -1077 959 O ATOM 1822 N ALA A1040 36.460 -12.148 34.627 1.00 56.25 N ANISOU 1822 N ALA A1040 4813 9397 7163 -360 -1130 503 N ATOM 1823 CA ALA A1040 35.758 -11.464 33.532 1.00 55.50 C ANISOU 1823 CA ALA A1040 4729 9258 7101 -341 -1158 417 C ATOM 1824 C ALA A1040 35.137 -12.497 32.596 1.00 59.59 C ANISOU 1824 C ALA A1040 5270 9712 7658 -326 -1152 379 C ATOM 1825 O ALA A1040 33.987 -12.339 32.177 1.00 57.42 O ANISOU 1825 O ALA A1040 4982 9432 7404 -343 -1167 306 O ATOM 1826 CB ALA A1040 36.718 -10.562 32.769 1.00 55.61 C ANISOU 1826 CB ALA A1040 4745 9286 7097 -306 -1185 440 C ATOM 1827 N GLN A1041 35.893 -13.600 32.350 1.00 57.70 N ANISOU 1827 N GLN A1041 5044 9426 7453 -297 -1126 410 N ATOM 1828 CA GLN A1041 35.513 -14.751 31.529 1.00 58.16 C ANISOU 1828 CA GLN A1041 5096 9411 7593 -289 -1101 330 C ATOM 1829 C GLN A1041 34.261 -15.467 32.083 1.00 61.17 C ANISOU 1829 C GLN A1041 5469 9725 8048 -345 -1077 309 C ATOM 1830 O GLN A1041 33.484 -15.968 31.292 1.00 61.03 O ANISOU 1830 O GLN A1041 5433 9679 8076 -362 -1065 189 O ATOM 1831 CB GLN A1041 36.690 -15.743 31.425 1.00 60.15 C ANISOU 1831 CB GLN A1041 5332 9591 7933 -241 -1073 357 C ATOM 1832 CG GLN A1041 36.614 -16.680 30.214 1.00 73.64 C ANISOU 1832 CG GLN A1041 6998 11249 9732 -226 -1041 192 C ATOM 1833 CD GLN A1041 37.802 -17.610 30.118 1.00 91.86 C ANISOU 1833 CD GLN A1041 9259 13461 12183 -167 -1009 184 C ATOM 1834 OE1 GLN A1041 37.983 -18.529 30.925 1.00 83.21 O ANISOU 1834 OE1 GLN A1041 8145 12208 11264 -151 -993 284 O ATOM 1835 NE2 GLN A1041 38.622 -17.417 29.098 1.00 88.72 N ANISOU 1835 NE2 GLN A1041 8821 13164 11725 -139 -1001 72 N ATOM 1836 N LYS A1042 34.084 -15.552 33.413 1.00 58.10 N ANISOU 1836 N LYS A1042 5075 9343 7657 -390 -1066 418 N ATOM 1837 CA LYS A1042 32.906 -16.206 34.000 1.00 58.87 C ANISOU 1837 CA LYS A1042 5153 9405 7809 -467 -1038 419 C ATOM 1838 C LYS A1042 31.736 -15.216 34.123 1.00 64.50 C ANISOU 1838 C LYS A1042 5847 10219 8440 -510 -1054 314 C ATOM 1839 O LYS A1042 30.574 -15.627 34.033 1.00 65.25 O ANISOU 1839 O LYS A1042 5921 10294 8577 -561 -1036 238 O ATOM 1840 CB LYS A1042 33.221 -16.823 35.371 1.00 61.78 C ANISOU 1840 CB LYS A1042 5496 9788 8188 -519 -1021 612 C ATOM 1841 N ALA A1043 32.049 -13.916 34.320 1.00 60.93 N ANISOU 1841 N ALA A1043 5386 9859 7904 -488 -1087 299 N ATOM 1842 CA ALA A1043 31.079 -12.835 34.476 1.00 60.60 C ANISOU 1842 CA ALA A1043 5298 9882 7845 -509 -1107 191 C ATOM 1843 C ALA A1043 30.301 -12.581 33.195 1.00 65.40 C ANISOU 1843 C ALA A1043 5900 10456 8493 -470 -1146 101 C ATOM 1844 O ALA A1043 29.104 -12.340 33.277 1.00 66.42 O ANISOU 1844 O ALA A1043 5978 10609 8648 -499 -1153 9 O ATOM 1845 CB ALA A1043 31.782 -11.558 34.916 1.00 61.00 C ANISOU 1845 CB ALA A1043 5321 9992 7865 -491 -1127 189 C ATOM 1846 N THR A1044 30.969 -12.641 32.018 1.00 62.12 N ANISOU 1846 N THR A1044 5515 10022 8066 -414 -1174 125 N ATOM 1847 CA THR A1044 30.375 -12.384 30.698 1.00 61.98 C ANISOU 1847 CA THR A1044 5467 10044 8037 -388 -1222 70 C ATOM 1848 C THR A1044 29.129 -13.300 30.482 1.00 66.02 C ANISOU 1848 C THR A1044 5948 10558 8578 -435 -1199 -44 C ATOM 1849 O THR A1044 29.261 -14.532 30.441 1.00 66.31 O ANISOU 1849 O THR A1044 6003 10538 8653 -466 -1144 -82 O ATOM 1850 CB THR A1044 31.428 -12.450 29.550 1.00 67.89 C ANISOU 1850 CB THR A1044 6232 10842 8723 -351 -1240 110 C ATOM 1851 OG1 THR A1044 30.768 -12.376 28.288 1.00 70.44 O ANISOU 1851 OG1 THR A1044 6499 11273 8992 -353 -1285 62 O ATOM 1852 CG2 THR A1044 32.294 -13.691 29.577 1.00 64.49 C ANISOU 1852 CG2 THR A1044 5833 10359 8313 -352 -1178 88 C ATOM 1853 N PRO A1045 27.908 -12.694 30.422 1.00 61.90 N ANISOU 1853 N PRO A1045 5365 10081 8074 -443 -1238 -106 N ATOM 1854 CA PRO A1045 26.688 -13.509 30.265 1.00 61.99 C ANISOU 1854 CA PRO A1045 5334 10111 8109 -498 -1213 -228 C ATOM 1855 C PRO A1045 26.610 -14.228 28.903 1.00 67.48 C ANISOU 1855 C PRO A1045 6002 10876 8763 -503 -1220 -311 C ATOM 1856 O PRO A1045 27.305 -13.828 27.952 1.00 66.62 O ANISOU 1856 O PRO A1045 5885 10852 8576 -461 -1265 -265 O ATOM 1857 CB PRO A1045 25.546 -12.490 30.442 1.00 63.32 C ANISOU 1857 CB PRO A1045 5419 10328 8310 -487 -1266 -273 C ATOM 1858 CG PRO A1045 26.121 -11.190 30.089 1.00 67.65 C ANISOU 1858 CG PRO A1045 5953 10879 8872 -411 -1341 -170 C ATOM 1859 CD PRO A1045 27.579 -11.252 30.501 1.00 63.10 C ANISOU 1859 CD PRO A1045 5462 10251 8264 -401 -1305 -75 C ATOM 1860 N PRO A1046 25.781 -15.310 28.794 1.00 64.93 N ANISOU 1860 N PRO A1046 5645 10539 8487 -571 -1168 -450 N ATOM 1861 CA PRO A1046 25.669 -16.018 27.509 1.00 64.87 C ANISOU 1861 CA PRO A1046 5577 10628 8443 -594 -1162 -593 C ATOM 1862 C PRO A1046 25.078 -15.144 26.406 1.00 67.86 C ANISOU 1862 C PRO A1046 5864 11230 8689 -569 -1259 -604 C ATOM 1863 O PRO A1046 24.228 -14.284 26.653 1.00 67.62 O ANISOU 1863 O PRO A1046 5794 11238 8662 -545 -1322 -553 O ATOM 1864 CB PRO A1046 24.738 -17.200 27.827 1.00 67.55 C ANISOU 1864 CB PRO A1046 5882 10885 8899 -684 -1086 -744 C ATOM 1865 CG PRO A1046 24.705 -17.318 29.304 1.00 71.52 C ANISOU 1865 CG PRO A1046 6449 11233 9493 -711 -1041 -625 C ATOM 1866 CD PRO A1046 24.902 -15.928 29.814 1.00 66.57 C ANISOU 1866 CD PRO A1046 5846 10665 8781 -648 -1107 -494 C ATOM 1867 N LYS A1047 25.543 -15.379 25.182 1.00 64.36 N ANISOU 1867 N LYS A1047 5364 10952 8136 -578 -1271 -669 N ATOM 1868 CA LYS A1047 25.097 -14.690 23.986 1.00 65.03 C ANISOU 1868 CA LYS A1047 5335 11318 8054 -575 -1368 -646 C ATOM 1869 C LYS A1047 23.688 -15.171 23.596 1.00 71.47 C ANISOU 1869 C LYS A1047 6037 12264 8854 -636 -1373 -826 C ATOM 1870 O LYS A1047 23.210 -16.196 24.111 1.00 71.56 O ANISOU 1870 O LYS A1047 6058 12145 8986 -697 -1281 -1007 O ATOM 1871 CB LYS A1047 26.092 -14.950 22.843 1.00 68.26 C ANISOU 1871 CB LYS A1047 5697 11926 8314 -598 -1359 -691 C ATOM 1872 CG LYS A1047 27.494 -14.382 23.080 1.00 81.63 C ANISOU 1872 CG LYS A1047 7479 13543 9993 -543 -1366 -505 C ATOM 1873 CD LYS A1047 28.597 -15.196 22.382 1.00 93.76 C ANISOU 1873 CD LYS A1047 8987 15170 11469 -577 -1293 -648 C ATOM 1874 CE LYS A1047 28.738 -14.937 20.897 1.00107.66 C ANISOU 1874 CE LYS A1047 10603 17328 12974 -633 -1342 -677 C ATOM 1875 NZ LYS A1047 29.941 -15.614 20.339 1.00119.27 N ANISOU 1875 NZ LYS A1047 12034 18887 14397 -666 -1260 -839 N ATOM 1876 N LEU A1048 23.021 -14.425 22.692 1.00 68.73 N ANISOU 1876 N LEU A1048 5568 12179 8369 -625 -1487 -757 N ATOM 1877 CA LEU A1048 21.706 -14.803 22.208 1.00 69.68 C ANISOU 1877 CA LEU A1048 5551 12483 8441 -682 -1508 -924 C ATOM 1878 C LEU A1048 21.861 -16.018 21.303 1.00 79.13 C ANISOU 1878 C LEU A1048 6662 13860 9546 -786 -1427 -1207 C ATOM 1879 O LEU A1048 21.066 -16.960 21.380 1.00 80.86 O ANISOU 1879 O LEU A1048 6828 14050 9845 -863 -1352 -1456 O ATOM 1880 CB LEU A1048 21.029 -13.624 21.473 1.00 70.05 C ANISOU 1880 CB LEU A1048 5465 12784 8367 -633 -1669 -731 C ATOM 1881 CG LEU A1048 19.624 -13.861 20.865 1.00 74.26 C ANISOU 1881 CG LEU A1048 5822 13572 8822 -682 -1721 -873 C ATOM 1882 CD1 LEU A1048 18.620 -14.269 21.916 1.00 72.75 C ANISOU 1882 CD1 LEU A1048 5660 13160 8821 -694 -1658 -1025 C ATOM 1883 CD2 LEU A1048 19.144 -12.636 20.143 1.00 75.35 C ANISOU 1883 CD2 LEU A1048 5819 13948 8864 -617 -1899 -606 C ATOM 1884 N GLU A1049 22.909 -16.001 20.472 1.00 78.01 N ANISOU 1884 N GLU A1049 6490 13896 9253 -798 -1430 -1188 N ATOM 1885 CA GLU A1049 23.231 -17.055 19.517 1.00 80.74 C ANISOU 1885 CA GLU A1049 6719 14454 9505 -899 -1348 -1494 C ATOM 1886 C GLU A1049 23.794 -18.280 20.241 1.00 88.36 C ANISOU 1886 C GLU A1049 7776 15064 10732 -918 -1195 -1700 C ATOM 1887 O GLU A1049 24.720 -18.141 21.050 1.00 86.25 O ANISOU 1887 O GLU A1049 7660 14519 10592 -847 -1169 -1536 O ATOM 1888 CB GLU A1049 24.237 -16.544 18.464 1.00 82.69 C ANISOU 1888 CB GLU A1049 6892 15026 9499 -910 -1398 -1395 C ATOM 1889 CG GLU A1049 23.767 -15.350 17.645 1.00 89.02 C ANISOU 1889 CG GLU A1049 7578 16198 10048 -902 -1563 -1123 C ATOM 1890 CD GLU A1049 23.913 -13.979 18.281 1.00 93.59 C ANISOU 1890 CD GLU A1049 8272 16577 10710 -783 -1674 -709 C ATOM 1891 OE1 GLU A1049 24.818 -13.797 19.129 1.00 92.62 O ANISOU 1891 OE1 GLU A1049 8316 16133 10743 -719 -1625 -608 O ATOM 1892 OE2 GLU A1049 23.130 -13.076 17.910 1.00 74.17 O ANISOU 1892 OE2 GLU A1049 5716 14288 8179 -754 -1812 -490 O ATOM 1893 N ASP A1050 23.231 -19.476 19.953 1.00 89.80 N ANISOU 1893 N ASP A1050 7851 15252 11018 -1018 -1098 -2050 N ATOM 1894 CA ASP A1050 23.690 -20.738 20.539 1.00 91.29 C ANISOU 1894 CA ASP A1050 8086 15081 11518 -1045 -956 -2245 C ATOM 1895 C ASP A1050 24.307 -21.646 19.459 1.00100.61 C ANISOU 1895 C ASP A1050 9100 16434 12694 -1123 -867 -2611 C ATOM 1896 O ASP A1050 23.630 -22.026 18.491 1.00102.83 O ANISOU 1896 O ASP A1050 9187 17035 12850 -1229 -852 -2909 O ATOM 1897 CB ASP A1050 22.555 -21.463 21.289 1.00 93.62 C ANISOU 1897 CB ASP A1050 8389 15140 12044 -1104 -895 -2351 C ATOM 1898 CG ASP A1050 23.032 -22.480 22.318 1.00106.25 C ANISOU 1898 CG ASP A1050 10084 16280 14008 -1106 -781 -2358 C ATOM 1899 OD1 ASP A1050 23.913 -22.129 23.145 1.00106.33 O ANISOU 1899 OD1 ASP A1050 10242 16079 14078 -1017 -795 -2090 O ATOM 1900 OD2 ASP A1050 22.490 -23.606 22.333 1.00112.46 O ANISOU 1900 OD2 ASP A1050 10784 16915 15030 -1203 -682 -2610 O ATOM 1901 N LYS A1051 25.611 -21.956 19.622 1.00 98.26 N ANISOU 1901 N LYS A1051 8856 15954 12525 -1073 -808 -2606 N ATOM 1902 CA LYS A1051 26.386 -22.813 18.723 1.00101.07 C ANISOU 1902 CA LYS A1051 9046 16426 12928 -1131 -710 -2973 C ATOM 1903 C LYS A1051 26.731 -24.132 19.414 1.00107.53 C ANISOU 1903 C LYS A1051 9875 16759 14222 -1128 -577 -3158 C ATOM 1904 O LYS A1051 26.815 -24.169 20.644 1.00104.93 O ANISOU 1904 O LYS A1051 9719 16031 14118 -1056 -581 -2882 O ATOM 1905 CB LYS A1051 27.669 -22.097 18.264 1.00103.05 C ANISOU 1905 CB LYS A1051 9314 16883 12958 -1076 -753 -2829 C ATOM 1906 N SER A1052 26.915 -25.215 18.627 1.00109.23 N ANISOU 1906 N SER A1052 9880 17019 14604 -1214 -461 -3625 N ATOM 1907 CA SER A1052 27.288 -26.535 19.145 1.00111.91 C ANISOU 1907 CA SER A1052 10180 16871 15470 -1211 -332 -3829 C ATOM 1908 C SER A1052 28.732 -26.488 19.674 1.00120.50 C ANISOU 1908 C SER A1052 11370 17706 16709 -1082 -330 -3623 C ATOM 1909 O SER A1052 29.509 -25.669 19.166 1.00119.87 O ANISOU 1909 O SER A1052 11301 17937 16308 -1040 -387 -3533 O ATOM 1910 CB SER A1052 27.128 -27.604 18.068 1.00118.11 C ANISOU 1910 CB SER A1052 10674 17797 16406 -1339 -206 -4436 C ATOM 1911 OG SER A1052 27.736 -27.220 16.847 1.00127.50 O ANISOU 1911 OG SER A1052 11700 19499 17246 -1378 -211 -4669 O ATOM 1912 N PRO A1053 29.117 -27.298 20.705 1.00120.54 N ANISOU 1912 N PRO A1053 11446 17172 17184 -1020 -277 -3503 N ATOM 1913 CA PRO A1053 30.503 -27.223 21.226 1.00120.56 C ANISOU 1913 CA PRO A1053 11530 16962 17315 -889 -289 -3285 C ATOM 1914 C PRO A1053 31.577 -27.469 20.155 1.00129.01 C ANISOU 1914 C PRO A1053 12413 18238 18367 -882 -228 -3645 C ATOM 1915 O PRO A1053 32.632 -26.829 20.197 1.00127.19 O ANISOU 1915 O PRO A1053 12250 18112 17965 -795 -276 -3461 O ATOM 1916 CB PRO A1053 30.537 -28.311 22.305 1.00123.22 C ANISOU 1916 CB PRO A1053 11892 16718 18209 -858 -232 -3170 C ATOM 1917 CG PRO A1053 29.113 -28.499 22.704 1.00127.27 C ANISOU 1917 CG PRO A1053 12439 17158 18761 -959 -228 -3132 C ATOM 1918 CD PRO A1053 28.326 -28.305 21.445 1.00123.58 C ANISOU 1918 CD PRO A1053 11823 17131 18002 -1072 -210 -3527 C ATOM 1919 N ASP A1054 31.287 -28.365 19.184 1.00131.02 N ANISOU 1919 N ASP A1054 12414 18586 18781 -988 -118 -4185 N ATOM 1920 CA ASP A1054 32.164 -28.704 18.063 1.00134.43 C ANISOU 1920 CA ASP A1054 12606 19275 19195 -1017 -37 -4640 C ATOM 1921 C ASP A1054 31.988 -27.672 16.926 1.00140.32 C ANISOU 1921 C ASP A1054 13286 20734 19294 -1109 -97 -4717 C ATOM 1922 O ASP A1054 31.302 -27.944 15.932 1.00142.68 O ANISOU 1922 O ASP A1054 13372 21400 19440 -1253 -47 -5126 O ATOM 1923 CB ASP A1054 31.879 -30.140 17.568 1.00140.33 C ANISOU 1923 CB ASP A1054 13077 19809 20432 -1107 118 -5226 C ATOM 1924 CG ASP A1054 32.167 -31.223 18.587 1.00151.38 C ANISOU 1924 CG ASP A1054 14500 20484 22534 -1019 176 -5135 C ATOM 1925 OD1 ASP A1054 33.352 -31.599 18.735 1.00153.13 O ANISOU 1925 OD1 ASP A1054 14671 20463 23050 -907 205 -5145 O ATOM 1926 OD2 ASP A1054 31.206 -31.721 19.210 1.00156.62 O ANISOU 1926 OD2 ASP A1054 15211 20833 23465 -1068 191 -5048 O ATOM 1927 N SER A1055 32.579 -26.468 17.110 1.00135.35 N ANISOU 1927 N SER A1055 12830 20305 18292 -1034 -210 -4293 N ATOM 1928 CA SER A1055 32.557 -25.338 16.166 1.00135.46 C ANISOU 1928 CA SER A1055 12805 20953 17709 -1106 -292 -4219 C ATOM 1929 C SER A1055 33.668 -24.327 16.515 1.00138.43 C ANISOU 1929 C SER A1055 13345 21363 17888 -1001 -374 -3808 C ATOM 1930 O SER A1055 33.829 -24.023 17.703 1.00135.80 O ANISOU 1930 O SER A1055 13243 20632 17722 -881 -428 -3413 O ATOM 1931 CB SER A1055 31.189 -24.651 16.151 1.00138.28 C ANISOU 1931 CB SER A1055 13238 21523 17781 -1166 -392 -4012 C ATOM 1932 OG SER A1055 30.841 -24.104 17.413 1.00144.72 O ANISOU 1932 OG SER A1055 14326 21971 18691 -1059 -479 -3531 O ATOM 1933 N PRO A1056 34.443 -23.801 15.520 1.00136.74 N ANISOU 1933 N PRO A1056 13000 21641 17313 -1060 -379 -3899 N ATOM 1934 CA PRO A1056 35.541 -22.860 15.847 1.00134.92 C ANISOU 1934 CA PRO A1056 12913 21432 16919 -974 -446 -3524 C ATOM 1935 C PRO A1056 35.060 -21.534 16.458 1.00136.68 C ANISOU 1935 C PRO A1056 13379 21647 16908 -925 -595 -2962 C ATOM 1936 O PRO A1056 34.246 -20.826 15.856 1.00136.36 O ANISOU 1936 O PRO A1056 13306 21967 16537 -1007 -675 -2854 O ATOM 1937 CB PRO A1056 36.239 -22.631 14.497 1.00138.88 C ANISOU 1937 CB PRO A1056 13178 22543 17046 -1095 -413 -3777 C ATOM 1938 CG PRO A1056 35.781 -23.752 13.619 1.00146.51 C ANISOU 1938 CG PRO A1056 13856 23703 18107 -1218 -292 -4385 C ATOM 1939 CD PRO A1056 34.396 -24.078 14.070 1.00141.42 C ANISOU 1939 CD PRO A1056 13287 22817 17629 -1224 -315 -4363 C ATOM 1940 N GLU A1057 35.572 -21.210 17.667 1.00131.47 N ANISOU 1940 N GLU A1057 12937 20574 16440 -792 -633 -2617 N ATOM 1941 CA GLU A1057 35.215 -20.003 18.421 1.00128.88 C ANISOU 1941 CA GLU A1057 12826 20167 15975 -736 -755 -2132 C ATOM 1942 C GLU A1057 36.337 -18.937 18.344 1.00132.05 C ANISOU 1942 C GLU A1057 13286 20725 16160 -707 -809 -1860 C ATOM 1943 O GLU A1057 36.990 -18.614 19.346 1.00129.39 O ANISOU 1943 O GLU A1057 13102 20094 15966 -607 -827 -1621 O ATOM 1944 CB GLU A1057 34.871 -20.358 19.880 1.00128.51 C ANISOU 1944 CB GLU A1057 12958 19596 16274 -637 -756 -1957 C ATOM 1945 N MET A1058 36.537 -18.391 17.130 1.00130.61 N ANISOU 1945 N MET A1058 12964 21046 15617 -812 -834 -1895 N ATOM 1946 CA MET A1058 37.522 -17.347 16.832 1.00130.23 C ANISOU 1946 CA MET A1058 12931 21229 15322 -827 -884 -1642 C ATOM 1947 C MET A1058 36.859 -15.974 16.998 1.00131.80 C ANISOU 1947 C MET A1058 13245 21490 15342 -829 -1022 -1199 C ATOM 1948 O MET A1058 35.665 -15.832 16.704 1.00131.90 O ANISOU 1948 O MET A1058 13223 21622 15269 -870 -1079 -1173 O ATOM 1949 CB MET A1058 38.096 -17.539 15.404 1.00135.59 C ANISOU 1949 CB MET A1058 13358 22458 15704 -966 -830 -1918 C ATOM 1950 CG MET A1058 39.174 -16.524 14.987 1.00139.54 C ANISOU 1950 CG MET A1058 13842 23249 15930 -1013 -869 -1667 C ATOM 1951 SD MET A1058 40.670 -16.498 16.017 1.00142.00 S ANISOU 1951 SD MET A1058 14296 23161 16495 -880 -826 -1561 S ATOM 1952 CE MET A1058 41.682 -15.378 15.078 1.00139.93 C ANISOU 1952 CE MET A1058 13934 23404 15828 -1006 -858 -1350 C ATOM 1953 N LYS A1059 37.635 -14.974 17.500 1.00125.60 N ANISOU 1953 N LYS A1059 12581 20601 14539 -781 -1074 -865 N ATOM 1954 CA LYS A1059 37.221 -13.580 17.755 1.00123.53 C ANISOU 1954 CA LYS A1059 12418 20322 14196 -770 -1198 -441 C ATOM 1955 C LYS A1059 36.075 -13.514 18.800 1.00122.23 C ANISOU 1955 C LYS A1059 12390 19793 14259 -683 -1241 -349 C ATOM 1956 O LYS A1059 35.403 -12.482 18.934 1.00121.65 O ANISOU 1956 O LYS A1059 12359 19702 14162 -673 -1343 -69 O ATOM 1957 CB LYS A1059 36.839 -12.847 16.447 1.00128.59 C ANISOU 1957 CB LYS A1059 12899 21466 14491 -897 -1282 -291 C ATOM 1958 N ASP A1060 35.886 -14.621 19.550 1.00114.60 N ANISOU 1958 N ASP A1060 11476 18531 13534 -626 -1160 -582 N ATOM 1959 CA ASP A1060 34.908 -14.756 20.624 1.00111.15 C ANISOU 1959 CA ASP A1060 11155 17765 13311 -562 -1176 -534 C ATOM 1960 C ASP A1060 35.487 -14.073 21.857 1.00108.47 C ANISOU 1960 C ASP A1060 10971 17135 13110 -480 -1197 -292 C ATOM 1961 O ASP A1060 36.651 -14.309 22.183 1.00107.79 O ANISOU 1961 O ASP A1060 10911 16962 13081 -446 -1148 -307 O ATOM 1962 CB ASP A1060 34.604 -16.248 20.873 1.00113.42 C ANISOU 1962 CB ASP A1060 11413 17875 13808 -558 -1077 -850 C ATOM 1963 CG ASP A1060 33.631 -16.535 21.999 1.00122.20 C ANISOU 1963 CG ASP A1060 12626 18674 15131 -518 -1078 -808 C ATOM 1964 OD1 ASP A1060 32.538 -15.923 22.012 1.00123.07 O ANISOU 1964 OD1 ASP A1060 12745 18847 15169 -535 -1148 -706 O ATOM 1965 OD2 ASP A1060 33.939 -17.406 22.839 1.00127.09 O ANISOU 1965 OD2 ASP A1060 13294 19002 15992 -477 -1011 -876 O ATOM 1966 N PHE A1061 34.702 -13.194 22.508 1.00100.37 N ANISOU 1966 N PHE A1061 10018 15984 12133 -451 -1269 -93 N ATOM 1967 CA PHE A1061 35.118 -12.412 23.678 1.00 97.01 C ANISOU 1967 CA PHE A1061 9706 15326 11827 -392 -1289 100 C ATOM 1968 C PHE A1061 35.655 -13.291 24.824 1.00 97.42 C ANISOU 1968 C PHE A1061 9834 15131 12051 -344 -1212 18 C ATOM 1969 O PHE A1061 36.665 -12.937 25.428 1.00 95.20 O ANISOU 1969 O PHE A1061 9601 14770 11799 -312 -1203 117 O ATOM 1970 CB PHE A1061 33.961 -11.524 24.178 1.00 97.74 C ANISOU 1970 CB PHE A1061 9823 15327 11988 -376 -1362 232 C ATOM 1971 CG PHE A1061 34.267 -10.620 25.353 1.00 97.54 C ANISOU 1971 CG PHE A1061 9874 15096 12092 -333 -1377 373 C ATOM 1972 CD1 PHE A1061 35.409 -9.821 25.362 1.00100.30 C ANISOU 1972 CD1 PHE A1061 10236 15451 12421 -330 -1388 509 C ATOM 1973 CD2 PHE A1061 33.394 -10.534 26.429 1.00 98.33 C ANISOU 1973 CD2 PHE A1061 10008 15026 12325 -312 -1374 346 C ATOM 1974 CE1 PHE A1061 35.685 -8.982 26.444 1.00100.25 C ANISOU 1974 CE1 PHE A1061 10274 15273 12544 -305 -1393 591 C ATOM 1975 CE2 PHE A1061 33.666 -9.688 27.507 1.00100.49 C ANISOU 1975 CE2 PHE A1061 10318 15160 12706 -291 -1378 421 C ATOM 1976 CZ PHE A1061 34.807 -8.915 27.506 1.00 98.61 C ANISOU 1976 CZ PHE A1061 10087 14919 12461 -286 -1387 533 C ATOM 1977 N ARG A1062 34.995 -14.434 25.095 1.00 93.69 N ANISOU 1977 N ARG A1062 9354 14548 11694 -348 -1162 -144 N ATOM 1978 CA ARG A1062 35.373 -15.384 26.146 1.00 92.66 C ANISOU 1978 CA ARG A1062 9272 14184 11752 -311 -1100 -174 C ATOM 1979 C ARG A1062 36.705 -16.080 25.827 1.00 95.92 C ANISOU 1979 C ARG A1062 9640 14592 12212 -281 -1046 -261 C ATOM 1980 O ARG A1062 37.390 -16.514 26.752 1.00 95.30 O ANISOU 1980 O ARG A1062 9597 14341 12273 -233 -1022 -192 O ATOM 1981 CB ARG A1062 34.259 -16.423 26.359 1.00 93.07 C ANISOU 1981 CB ARG A1062 9303 14116 11941 -341 -1062 -307 C ATOM 1982 N HIS A1063 37.067 -16.183 24.527 1.00 92.81 N ANISOU 1982 N HIS A1063 9147 14418 11697 -315 -1031 -414 N ATOM 1983 CA HIS A1063 38.318 -16.793 24.056 1.00 93.17 C ANISOU 1983 CA HIS A1063 9114 14507 11781 -295 -973 -553 C ATOM 1984 C HIS A1063 39.503 -15.820 24.238 1.00 93.01 C ANISOU 1984 C HIS A1063 9133 14565 11643 -270 -1003 -371 C ATOM 1985 O HIS A1063 40.635 -16.260 24.444 1.00 92.33 O ANISOU 1985 O HIS A1063 9015 14422 11644 -223 -963 -416 O ATOM 1986 CB HIS A1063 38.193 -17.248 22.583 1.00 96.18 C ANISOU 1986 CB HIS A1063 9339 15160 12045 -368 -934 -831 C ATOM 1987 CG HIS A1063 39.505 -17.608 21.944 1.00101.10 C ANISOU 1987 CG HIS A1063 9851 15911 12651 -363 -875 -996 C ATOM 1988 ND1 HIS A1063 40.213 -18.739 22.328 1.00103.75 N ANISOU 1988 ND1 HIS A1063 10134 16012 13274 -294 -803 -1160 N ATOM 1989 CD2 HIS A1063 40.216 -16.947 21.000 1.00103.56 C ANISOU 1989 CD2 HIS A1063 10084 16558 12706 -421 -883 -1000 C ATOM 1990 CE1 HIS A1063 41.315 -18.738 21.594 1.00104.31 C ANISOU 1990 CE1 HIS A1063 10091 16285 13257 -305 -764 -1301 C ATOM 1991 NE2 HIS A1063 41.363 -17.680 20.781 1.00104.56 N ANISOU 1991 NE2 HIS A1063 10105 16680 12943 -391 -806 -1211 N ATOM 1992 N GLY A1064 39.218 -14.519 24.159 1.00 87.07 N ANISOU 1992 N GLY A1064 8431 13924 10727 -302 -1073 -173 N ATOM 1993 CA GLY A1064 40.189 -13.444 24.328 1.00 85.42 C ANISOU 1993 CA GLY A1064 8254 13774 10427 -300 -1103 9 C ATOM 1994 C GLY A1064 40.914 -13.521 25.651 1.00 87.06 C ANISOU 1994 C GLY A1064 8534 13769 10777 -231 -1089 96 C ATOM 1995 O GLY A1064 42.125 -13.294 25.709 1.00 87.02 O ANISOU 1995 O GLY A1064 8511 13811 10744 -216 -1075 131 O ATOM 1996 N PHE A1065 40.179 -13.904 26.708 1.00 81.41 N ANISOU 1996 N PHE A1065 7879 12853 10199 -201 -1092 128 N ATOM 1997 CA PHE A1065 40.733 -14.090 28.039 1.00 80.12 C ANISOU 1997 CA PHE A1065 7759 12539 10145 -153 -1085 227 C ATOM 1998 C PHE A1065 41.602 -15.343 28.093 1.00 84.73 C ANISOU 1998 C PHE A1065 8286 13038 10872 -94 -1037 143 C ATOM 1999 O PHE A1065 42.560 -15.347 28.853 1.00 84.39 O ANISOU 1999 O PHE A1065 8240 12955 10868 -50 -1040 240 O ATOM 2000 CB PHE A1065 39.625 -14.148 29.098 1.00 81.12 C ANISOU 2000 CB PHE A1065 7941 12539 10344 -164 -1100 293 C ATOM 2001 CG PHE A1065 38.795 -12.889 29.160 1.00 81.66 C ANISOU 2001 CG PHE A1065 8039 12659 10329 -206 -1146 354 C ATOM 2002 CD1 PHE A1065 39.346 -11.694 29.618 1.00 83.84 C ANISOU 2002 CD1 PHE A1065 8326 12969 10559 -216 -1172 453 C ATOM 2003 CD2 PHE A1065 37.464 -12.894 28.756 1.00 83.16 C ANISOU 2003 CD2 PHE A1065 8225 12851 10520 -236 -1164 298 C ATOM 2004 CE1 PHE A1065 38.588 -10.522 29.646 1.00 84.13 C ANISOU 2004 CE1 PHE A1065 8364 13008 10595 -246 -1215 494 C ATOM 2005 CE2 PHE A1065 36.702 -11.725 28.802 1.00 85.33 C ANISOU 2005 CE2 PHE A1065 8503 13151 10768 -258 -1215 356 C ATOM 2006 CZ PHE A1065 37.271 -10.548 29.244 1.00 83.19 C ANISOU 2006 CZ PHE A1065 8237 12879 10494 -259 -1239 453 C ATOM 2007 N ASP A1066 41.298 -16.385 27.280 1.00 82.29 N ANISOU 2007 N ASP A1066 7906 12703 10658 -93 -993 -52 N ATOM 2008 CA ASP A1066 42.090 -17.622 27.237 1.00 83.36 C ANISOU 2008 CA ASP A1066 7951 12714 11008 -29 -943 -172 C ATOM 2009 C ASP A1066 43.490 -17.356 26.685 1.00 87.32 C ANISOU 2009 C ASP A1066 8382 13363 11434 -3 -926 -230 C ATOM 2010 O ASP A1066 44.469 -17.818 27.281 1.00 87.08 O ANISOU 2010 O ASP A1066 8312 13227 11548 73 -920 -181 O ATOM 2011 CB ASP A1066 41.398 -18.721 26.412 1.00 86.71 C ANISOU 2011 CB ASP A1066 8286 13079 11580 -51 -887 -430 C ATOM 2012 CG ASP A1066 40.213 -19.387 27.085 1.00 98.74 C ANISOU 2012 CG ASP A1066 9849 14389 13278 -66 -885 -389 C ATOM 2013 OD1 ASP A1066 39.259 -19.769 26.366 1.00 99.99 O ANISOU 2013 OD1 ASP A1066 9965 14577 13448 -124 -856 -579 O ATOM 2014 OD2 ASP A1066 40.244 -19.548 28.328 1.00105.12 O ANISOU 2014 OD2 ASP A1066 10715 15028 14199 -33 -910 -168 O ATOM 2015 N ILE A1067 43.587 -16.591 25.572 1.00 83.73 N ANISOU 2015 N ILE A1067 7896 13172 10745 -73 -925 -311 N ATOM 2016 CA ILE A1067 44.874 -16.251 24.957 1.00 84.03 C ANISOU 2016 CA ILE A1067 7855 13404 10671 -79 -903 -369 C ATOM 2017 C ILE A1067 45.614 -15.236 25.863 1.00 84.79 C ANISOU 2017 C ILE A1067 8032 13493 10690 -62 -948 -123 C ATOM 2018 O ILE A1067 46.836 -15.342 26.033 1.00 85.22 O ANISOU 2018 O ILE A1067 8029 13572 10778 -18 -931 -133 O ATOM 2019 CB ILE A1067 44.718 -15.779 23.470 1.00 88.26 C ANISOU 2019 CB ILE A1067 8307 14272 10954 -187 -888 -502 C ATOM 2020 CG1 ILE A1067 45.861 -16.289 22.538 1.00 91.17 C ANISOU 2020 CG1 ILE A1067 8506 14843 11293 -199 -817 -752 C ATOM 2021 CG2 ILE A1067 44.366 -14.294 23.278 1.00 87.26 C ANISOU 2021 CG2 ILE A1067 8258 14310 10587 -268 -956 -264 C ATOM 2022 CD1 ILE A1067 47.391 -15.796 22.804 1.00101.63 C ANISOU 2022 CD1 ILE A1067 9806 16240 12569 -172 -811 -667 C ATOM 2023 N LEU A1068 44.854 -14.307 26.480 1.00 77.59 N ANISOU 2023 N LEU A1068 7232 12543 9705 -97 -1002 66 N ATOM 2024 CA LEU A1068 45.353 -13.274 27.382 1.00 75.29 C ANISOU 2024 CA LEU A1068 7001 12245 9362 -101 -1038 253 C ATOM 2025 C LEU A1068 45.963 -13.909 28.638 1.00 76.91 C ANISOU 2025 C LEU A1068 7202 12310 9710 -22 -1037 317 C ATOM 2026 O LEU A1068 47.051 -13.495 29.044 1.00 77.36 O ANISOU 2026 O LEU A1068 7231 12432 9730 -8 -1041 375 O ATOM 2027 CB LEU A1068 44.203 -12.320 27.739 1.00 74.43 C ANISOU 2027 CB LEU A1068 6975 12098 9207 -152 -1084 372 C ATOM 2028 CG LEU A1068 44.522 -10.941 28.306 1.00 78.70 C ANISOU 2028 CG LEU A1068 7547 12659 9696 -192 -1115 511 C ATOM 2029 CD1 LEU A1068 45.434 -10.139 27.386 1.00 79.31 C ANISOU 2029 CD1 LEU A1068 7576 12900 9657 -248 -1112 543 C ATOM 2030 CD2 LEU A1068 43.236 -10.165 28.543 1.00 81.23 C ANISOU 2030 CD2 LEU A1068 7915 12911 10037 -229 -1156 572 C ATOM 2031 N VAL A1069 45.306 -14.953 29.204 1.00 71.07 N ANISOU 2031 N VAL A1069 6471 11398 9135 23 -1035 318 N ATOM 2032 CA VAL A1069 45.785 -15.694 30.380 1.00 70.66 C ANISOU 2032 CA VAL A1069 6392 11223 9232 93 -1048 435 C ATOM 2033 C VAL A1069 47.095 -16.436 30.011 1.00 74.91 C ANISOU 2033 C VAL A1069 6816 11755 9892 176 -1024 354 C ATOM 2034 O VAL A1069 48.040 -16.455 30.811 1.00 74.13 O ANISOU 2034 O VAL A1069 6675 11672 9818 225 -1049 476 O ATOM 2035 CB VAL A1069 44.681 -16.631 30.955 1.00 74.54 C ANISOU 2035 CB VAL A1069 6906 11530 9886 100 -1050 483 C ATOM 2036 CG1 VAL A1069 45.258 -17.837 31.703 1.00 75.69 C ANISOU 2036 CG1 VAL A1069 6973 11515 10271 184 -1057 591 C ATOM 2037 CG2 VAL A1069 43.726 -15.848 31.854 1.00 73.13 C ANISOU 2037 CG2 VAL A1069 6811 11389 9587 29 -1081 609 C ATOM 2038 N GLY A1070 47.139 -16.972 28.787 1.00 72.12 N ANISOU 2038 N GLY A1070 6392 11412 9596 181 -974 129 N ATOM 2039 CA GLY A1070 48.291 -17.667 28.227 1.00 73.26 C ANISOU 2039 CA GLY A1070 6397 11567 9871 251 -935 -31 C ATOM 2040 C GLY A1070 49.503 -16.765 28.150 1.00 76.57 C ANISOU 2040 C GLY A1070 6790 12196 10107 237 -941 2 C ATOM 2041 O GLY A1070 50.621 -17.197 28.457 1.00 77.92 O ANISOU 2041 O GLY A1070 6860 12349 10396 320 -941 -1 O ATOM 2042 N GLN A1071 49.268 -15.487 27.787 1.00 70.36 N ANISOU 2042 N GLN A1071 6083 11594 9057 132 -951 52 N ATOM 2043 CA GLN A1071 50.287 -14.445 27.702 1.00 69.41 C ANISOU 2043 CA GLN A1071 5947 11665 8759 86 -954 104 C ATOM 2044 C GLN A1071 50.759 -14.031 29.106 1.00 73.53 C ANISOU 2044 C GLN A1071 6505 12140 9294 118 -1000 299 C ATOM 2045 O GLN A1071 51.966 -13.891 29.328 1.00 73.38 O ANISOU 2045 O GLN A1071 6410 12215 9258 144 -998 306 O ATOM 2046 CB GLN A1071 49.750 -13.233 26.938 1.00 69.73 C ANISOU 2046 CB GLN A1071 6051 11865 8579 -41 -959 141 C ATOM 2047 CG GLN A1071 49.664 -13.429 25.439 1.00 84.51 C ANISOU 2047 CG GLN A1071 7839 13928 10342 -104 -916 -35 C ATOM 2048 CD GLN A1071 48.920 -12.290 24.807 1.00106.00 C ANISOU 2048 CD GLN A1071 10619 16784 12872 -223 -946 84 C ATOM 2049 OE1 GLN A1071 47.691 -12.285 24.750 1.00103.96 O ANISOU 2049 OE1 GLN A1071 10423 16453 12624 -238 -975 117 O ATOM 2050 NE2 GLN A1071 49.643 -11.284 24.343 1.00 98.45 N ANISOU 2050 NE2 GLN A1071 9632 16015 11758 -312 -946 173 N ATOM 2051 N ILE A1072 49.808 -13.857 30.054 1.00 69.83 N ANISOU 2051 N ILE A1072 6128 11563 8841 105 -1039 437 N ATOM 2052 CA ILE A1072 50.099 -13.493 31.445 1.00 69.20 C ANISOU 2052 CA ILE A1072 6056 11498 8740 110 -1080 599 C ATOM 2053 C ILE A1072 50.977 -14.592 32.081 1.00 75.74 C ANISOU 2053 C ILE A1072 6779 12277 9723 223 -1099 661 C ATOM 2054 O ILE A1072 51.908 -14.262 32.824 1.00 76.40 O ANISOU 2054 O ILE A1072 6802 12477 9748 234 -1124 747 O ATOM 2055 CB ILE A1072 48.797 -13.222 32.266 1.00 71.06 C ANISOU 2055 CB ILE A1072 6380 11662 8958 62 -1106 694 C ATOM 2056 CG1 ILE A1072 48.038 -11.979 31.740 1.00 69.35 C ANISOU 2056 CG1 ILE A1072 6239 11483 8629 -36 -1100 651 C ATOM 2057 CG2 ILE A1072 49.109 -13.073 33.772 1.00 72.29 C ANISOU 2057 CG2 ILE A1072 6500 11894 9074 56 -1142 838 C ATOM 2058 CD1 ILE A1072 46.600 -11.814 32.270 1.00 67.90 C ANISOU 2058 CD1 ILE A1072 6124 11215 8460 -75 -1117 684 C ATOM 2059 N ASP A1073 50.704 -15.884 31.761 1.00 73.33 N ANISOU 2059 N ASP A1073 6429 11795 9637 305 -1088 614 N ATOM 2060 CA ASP A1073 51.482 -17.024 32.269 1.00 74.80 C ANISOU 2060 CA ASP A1073 6491 11873 10056 428 -1113 691 C ATOM 2061 C ASP A1073 52.890 -17.037 31.677 1.00 79.29 C ANISOU 2061 C ASP A1073 6936 12548 10644 485 -1091 560 C ATOM 2062 O ASP A1073 53.851 -17.306 32.406 1.00 78.83 O ANISOU 2062 O ASP A1073 6775 12521 10655 562 -1135 684 O ATOM 2063 CB ASP A1073 50.769 -18.353 31.988 1.00 77.75 C ANISOU 2063 CB ASP A1073 6834 11983 10726 490 -1097 644 C ATOM 2064 CG ASP A1073 49.626 -18.643 32.942 1.00 87.02 C ANISOU 2064 CG ASP A1073 8085 13042 11937 454 -1133 848 C ATOM 2065 OD1 ASP A1073 49.783 -18.382 34.160 1.00 87.43 O ANISOU 2065 OD1 ASP A1073 8137 13187 11896 439 -1191 1092 O ATOM 2066 OD2 ASP A1073 48.591 -19.170 32.481 1.00 92.51 O ANISOU 2066 OD2 ASP A1073 8821 13583 12745 430 -1100 755 O ATOM 2067 N ASP A1074 53.006 -16.712 30.361 1.00 76.43 N ANISOU 2067 N ASP A1074 6565 12278 10196 436 -1026 318 N ATOM 2068 CA ASP A1074 54.271 -16.623 29.623 1.00 77.17 C ANISOU 2068 CA ASP A1074 6532 12525 10262 456 -987 150 C ATOM 2069 C ASP A1074 55.163 -15.504 30.213 1.00 82.05 C ANISOU 2069 C ASP A1074 7158 13350 10668 406 -1014 271 C ATOM 2070 O ASP A1074 56.374 -15.700 30.340 1.00 82.95 O ANISOU 2070 O ASP A1074 7142 13544 10834 473 -1018 247 O ATOM 2071 CB ASP A1074 54.013 -16.397 28.122 1.00 78.47 C ANISOU 2071 CB ASP A1074 6687 12819 10308 368 -912 -103 C ATOM 2072 N ALA A1075 54.552 -14.361 30.617 1.00 77.85 N ANISOU 2072 N ALA A1075 6758 12892 9931 292 -1031 386 N ATOM 2073 CA ALA A1075 55.242 -13.213 31.225 1.00 77.03 C ANISOU 2073 CA ALA A1075 6656 12961 9651 220 -1047 470 C ATOM 2074 C ALA A1075 55.708 -13.528 32.655 1.00 82.52 C ANISOU 2074 C ALA A1075 7288 13671 10394 288 -1110 639 C ATOM 2075 O ALA A1075 56.818 -13.138 33.012 1.00 83.46 O ANISOU 2075 O ALA A1075 7314 13953 10443 287 -1119 647 O ATOM 2076 CB ALA A1075 54.337 -11.992 31.224 1.00 76.04 C ANISOU 2076 CB ALA A1075 6661 12856 9375 87 -1043 514 C ATOM 2077 N LEU A1076 54.876 -14.238 33.462 1.00 79.34 N ANISOU 2077 N LEU A1076 6919 13131 10097 335 -1155 784 N ATOM 2078 CA LEU A1076 55.204 -14.642 34.839 1.00 80.21 C ANISOU 2078 CA LEU A1076 6949 13297 10231 386 -1227 997 C ATOM 2079 C LEU A1076 56.368 -15.637 34.866 1.00 87.26 C ANISOU 2079 C LEU A1076 7673 14167 11314 531 -1259 1037 C ATOM 2080 O LEU A1076 57.127 -15.642 35.832 1.00 89.02 O ANISOU 2080 O LEU A1076 7787 14544 11493 561 -1321 1194 O ATOM 2081 CB LEU A1076 53.991 -15.255 35.557 1.00 80.26 C ANISOU 2081 CB LEU A1076 7017 13169 10312 386 -1262 1162 C ATOM 2082 CG LEU A1076 52.922 -14.290 36.092 1.00 83.58 C ANISOU 2082 CG LEU A1076 7549 13669 10539 249 -1254 1175 C ATOM 2083 CD1 LEU A1076 51.561 -14.961 36.139 1.00 83.32 C ANISOU 2083 CD1 LEU A1076 7599 13449 10610 245 -1255 1235 C ATOM 2084 CD2 LEU A1076 53.272 -13.784 37.476 1.00 87.13 C ANISOU 2084 CD2 LEU A1076 7919 14371 10816 189 -1301 1310 C ATOM 2085 N LYS A1077 56.508 -16.474 33.810 1.00 84.76 N ANISOU 2085 N LYS A1077 7310 13678 11215 618 -1219 877 N ATOM 2086 CA LYS A1077 57.590 -17.457 33.636 1.00 86.45 C ANISOU 2086 CA LYS A1077 7339 13826 11684 770 -1236 847 C ATOM 2087 C LYS A1077 58.941 -16.721 33.587 1.00 89.80 C ANISOU 2087 C LYS A1077 7662 14512 11943 755 -1229 770 C ATOM 2088 O LYS A1077 59.853 -17.098 34.319 1.00 90.87 O ANISOU 2088 O LYS A1077 7649 14716 12160 849 -1296 911 O ATOM 2089 CB LYS A1077 57.357 -18.300 32.363 1.00 89.64 C ANISOU 2089 CB LYS A1077 7704 14025 12329 827 -1164 587 C ATOM 2090 CG LYS A1077 58.417 -19.366 32.079 1.00106.40 C ANISOU 2090 CG LYS A1077 9604 16034 14788 992 -1168 488 C ATOM 2091 CD LYS A1077 59.037 -19.179 30.686 1.00114.73 C ANISOU 2091 CD LYS A1077 10579 17205 15809 966 -1066 105 C ATOM 2092 CE LYS A1077 60.025 -20.260 30.300 1.00121.34 C ANISOU 2092 CE LYS A1077 11166 17924 17014 1129 -1053 -72 C ATOM 2093 NZ LYS A1077 59.352 -21.541 29.944 1.00128.06 N ANISOU 2093 NZ LYS A1077 11945 18422 18291 1225 -1034 -173 N ATOM 2094 N LEU A1078 59.033 -15.639 32.776 1.00 84.59 N ANISOU 2094 N LEU A1078 7077 14011 11051 626 -1156 580 N ATOM 2095 CA LEU A1078 60.218 -14.780 32.641 1.00 84.45 C ANISOU 2095 CA LEU A1078 6979 14248 10859 571 -1134 495 C ATOM 2096 C LEU A1078 60.514 -14.070 33.956 1.00 89.38 C ANISOU 2096 C LEU A1078 7594 15050 11316 519 -1196 681 C ATOM 2097 O LEU A1078 61.680 -13.895 34.305 1.00 89.99 O ANISOU 2097 O LEU A1078 7531 15313 11348 543 -1216 681 O ATOM 2098 CB LEU A1078 60.038 -13.728 31.527 1.00 83.06 C ANISOU 2098 CB LEU A1078 6897 14183 10481 413 -1047 317 C ATOM 2099 CG LEU A1078 59.460 -14.166 30.168 1.00 87.26 C ANISOU 2099 CG LEU A1078 7456 14627 11072 401 -980 127 C ATOM 2100 CD1 LEU A1078 59.193 -12.959 29.287 1.00 85.53 C ANISOU 2100 CD1 LEU A1078 7330 14557 10609 221 -923 65 C ATOM 2101 CD2 LEU A1078 60.386 -15.148 29.448 1.00 91.95 C ANISOU 2101 CD2 LEU A1078 7857 15235 11846 510 -941 -86 C ATOM 2102 N ALA A1079 59.454 -13.651 34.682 1.00 85.52 N ANISOU 2102 N ALA A1079 7233 14533 10727 439 -1220 812 N ATOM 2103 CA ALA A1079 59.572 -12.993 35.984 1.00 85.27 C ANISOU 2103 CA ALA A1079 7172 14705 10522 367 -1270 948 C ATOM 2104 C ALA A1079 60.145 -13.969 37.014 1.00 91.78 C ANISOU 2104 C ALA A1079 7834 15596 11441 494 -1368 1171 C ATOM 2105 O ALA A1079 61.000 -13.580 37.811 1.00 92.60 O ANISOU 2105 O ALA A1079 7811 15963 11408 470 -1409 1230 O ATOM 2106 CB ALA A1079 58.219 -12.471 36.434 1.00 84.44 C ANISOU 2106 CB ALA A1079 7214 14547 10323 259 -1264 995 C ATOM 2107 N ASN A1080 59.714 -15.250 36.955 1.00 89.49 N ANISOU 2107 N ASN A1080 7529 15067 11406 626 -1407 1301 N ATOM 2108 CA ASN A1080 60.199 -16.313 37.843 1.00 91.89 C ANISOU 2108 CA ASN A1080 7663 15374 11875 762 -1513 1575 C ATOM 2109 C ASN A1080 61.612 -16.788 37.422 1.00 96.75 C ANISOU 2109 C ASN A1080 8088 16014 12659 901 -1530 1503 C ATOM 2110 O ASN A1080 62.343 -17.340 38.242 1.00 98.03 O ANISOU 2110 O ASN A1080 8068 16278 12902 1002 -1629 1730 O ATOM 2111 CB ASN A1080 59.207 -17.480 37.884 1.00 93.78 C ANISOU 2111 CB ASN A1080 7944 15302 12386 842 -1543 1743 C ATOM 2112 CG ASN A1080 57.917 -17.152 38.608 1.00118.33 C ANISOU 2112 CG ASN A1080 11190 18445 15326 713 -1550 1876 C ATOM 2113 OD1 ASN A1080 57.911 -16.699 39.764 1.00113.49 O ANISOU 2113 OD1 ASN A1080 10532 18114 14475 625 -1602 2046 O ATOM 2114 ND2 ASN A1080 56.789 -17.406 37.955 1.00108.32 N ANISOU 2114 ND2 ASN A1080 10067 16918 14173 693 -1495 1784 N ATOM 2115 N GLU A1081 61.980 -16.560 36.151 1.00 92.50 N ANISOU 2115 N GLU A1081 7572 15412 12161 899 -1435 1193 N ATOM 2116 CA GLU A1081 63.288 -16.862 35.570 1.00 93.87 C ANISOU 2116 CA GLU A1081 7563 15637 12465 1003 -1421 1036 C ATOM 2117 C GLU A1081 64.294 -15.787 36.045 1.00 97.44 C ANISOU 2117 C GLU A1081 7943 16454 12625 909 -1426 1007 C ATOM 2118 O GLU A1081 65.460 -16.100 36.306 1.00 99.39 O ANISOU 2118 O GLU A1081 7986 16832 12946 1009 -1474 1029 O ATOM 2119 CB GLU A1081 63.162 -16.905 34.027 1.00 94.73 C ANISOU 2119 CB GLU A1081 7723 15613 12658 985 -1302 697 C ATOM 2120 CG GLU A1081 64.457 -17.016 33.230 1.00108.35 C ANISOU 2120 CG GLU A1081 9263 17449 14456 1045 -1254 450 C ATOM 2121 CD GLU A1081 64.317 -16.739 31.742 1.00122.23 C ANISOU 2121 CD GLU A1081 11069 19221 16152 953 -1127 112 C ATOM 2122 OE1 GLU A1081 64.917 -15.748 31.261 1.00106.52 O ANISOU 2122 OE1 GLU A1081 9080 17485 13907 823 -1065 -25 O ATOM 2123 OE2 GLU A1081 63.617 -17.519 31.054 1.00110.42 O ANISOU 2123 OE2 GLU A1081 9592 17502 14860 1000 -1087 -13 O ATOM 2124 N GLY A1082 63.808 -14.551 36.179 1.00 91.42 N ANISOU 2124 N GLY A1082 7330 15839 11567 719 -1378 952 N ATOM 2125 CA GLY A1082 64.582 -13.390 36.605 1.00 90.79 C ANISOU 2125 CA GLY A1082 7196 16076 11223 591 -1363 885 C ATOM 2126 C GLY A1082 64.659 -12.280 35.570 1.00 93.26 C ANISOU 2126 C GLY A1082 7610 16424 11399 435 -1247 632 C ATOM 2127 O GLY A1082 65.261 -11.235 35.837 1.00 93.47 O ANISOU 2127 O GLY A1082 7598 16675 11240 305 -1220 557 O ATOM 2128 N LYS A1083 64.055 -12.498 34.375 1.00 87.75 N ANISOU 2128 N LYS A1083 7025 15521 10795 434 -1179 508 N ATOM 2129 CA LYS A1083 64.031 -11.546 33.259 1.00 85.50 C ANISOU 2129 CA LYS A1083 6827 15275 10386 282 -1078 325 C ATOM 2130 C LYS A1083 62.763 -10.659 33.344 1.00 85.12 C ANISOU 2130 C LYS A1083 6978 15131 10233 142 -1059 379 C ATOM 2131 O LYS A1083 61.820 -10.815 32.566 1.00 83.75 O ANISOU 2131 O LYS A1083 6926 14791 10103 128 -1029 353 O ATOM 2132 CB LYS A1083 64.137 -12.292 31.914 1.00 88.39 C ANISOU 2132 CB LYS A1083 7157 15548 10877 346 -1019 153 C ATOM 2133 N VAL A1084 62.774 -9.726 34.317 1.00 80.10 N ANISOU 2133 N VAL A1084 6346 14618 9470 37 -1076 432 N ATOM 2134 CA VAL A1084 61.717 -8.759 34.665 1.00 77.79 C ANISOU 2134 CA VAL A1084 6191 14257 9110 -96 -1062 455 C ATOM 2135 C VAL A1084 61.533 -7.704 33.558 1.00 80.41 C ANISOU 2135 C VAL A1084 6610 14533 9412 -241 -983 362 C ATOM 2136 O VAL A1084 60.396 -7.296 33.295 1.00 78.88 O ANISOU 2136 O VAL A1084 6549 14179 9242 -299 -972 393 O ATOM 2137 CB VAL A1084 62.012 -8.072 36.028 1.00 81.74 C ANISOU 2137 CB VAL A1084 6605 14955 9498 -176 -1090 470 C ATOM 2138 CG1 VAL A1084 60.796 -7.312 36.543 1.00 80.54 C ANISOU 2138 CG1 VAL A1084 6562 14715 9323 -285 -1080 468 C ATOM 2139 CG2 VAL A1084 62.493 -9.081 37.068 1.00 82.89 C ANISOU 2139 CG2 VAL A1084 6612 15249 9634 -47 -1179 605 C ATOM 2140 N LYS A1085 62.644 -7.243 32.936 1.00 77.37 N ANISOU 2140 N LYS A1085 6132 14291 8975 -307 -932 270 N ATOM 2141 CA LYS A1085 62.598 -6.259 31.855 1.00 77.23 C ANISOU 2141 CA LYS A1085 6166 14255 8923 -462 -863 236 C ATOM 2142 C LYS A1085 61.801 -6.844 30.684 1.00 82.29 C ANISOU 2142 C LYS A1085 6899 14779 9587 -423 -851 254 C ATOM 2143 O LYS A1085 60.966 -6.153 30.087 1.00 81.44 O ANISOU 2143 O LYS A1085 6896 14574 9475 -526 -833 315 O ATOM 2144 CB LYS A1085 64.012 -5.859 31.426 1.00 80.81 C ANISOU 2144 CB LYS A1085 6476 14921 9305 -537 -811 144 C ATOM 2145 N GLU A1086 62.015 -8.155 30.427 1.00 79.59 N ANISOU 2145 N GLU A1086 6501 14442 9296 -270 -865 198 N ATOM 2146 CA GLU A1086 61.327 -8.951 29.412 1.00 79.00 C ANISOU 2146 CA GLU A1086 6472 14283 9260 -219 -850 154 C ATOM 2147 C GLU A1086 59.859 -9.153 29.793 1.00 80.50 C ANISOU 2147 C GLU A1086 6813 14253 9518 -184 -894 255 C ATOM 2148 O GLU A1086 59.000 -9.110 28.915 1.00 79.60 O ANISOU 2148 O GLU A1086 6781 14082 9382 -233 -876 255 O ATOM 2149 CB GLU A1086 62.023 -10.307 29.227 1.00 81.61 C ANISOU 2149 CB GLU A1086 6665 14643 9702 -57 -850 27 C ATOM 2150 CG GLU A1086 63.290 -10.227 28.403 1.00 96.29 C ANISOU 2150 CG GLU A1086 8361 16738 11487 -101 -786 -131 C ATOM 2151 CD GLU A1086 64.003 -11.553 28.233 1.00132.65 C ANISOU 2151 CD GLU A1086 12793 21352 16256 71 -783 -295 C ATOM 2152 OE1 GLU A1086 63.415 -12.468 27.609 1.00132.29 O ANISOU 2152 OE1 GLU A1086 12741 21193 16329 145 -767 -402 O ATOM 2153 OE2 GLU A1086 65.158 -11.672 28.705 1.00132.83 O ANISOU 2153 OE2 GLU A1086 12666 21493 16311 130 -795 -334 O ATOM 2154 N ALA A1087 59.577 -9.371 31.097 1.00 76.30 N ANISOU 2154 N ALA A1087 6301 13638 9050 -111 -952 343 N ATOM 2155 CA ALA A1087 58.226 -9.545 31.638 1.00 74.97 C ANISOU 2155 CA ALA A1087 6256 13293 8936 -89 -991 437 C ATOM 2156 C ALA A1087 57.433 -8.242 31.505 1.00 78.39 C ANISOU 2156 C ALA A1087 6795 13678 9311 -235 -975 471 C ATOM 2157 O ALA A1087 56.247 -8.285 31.206 1.00 77.27 O ANISOU 2157 O ALA A1087 6757 13398 9203 -241 -984 506 O ATOM 2158 CB ALA A1087 58.293 -9.985 33.093 1.00 75.82 C ANISOU 2158 CB ALA A1087 6319 13413 9077 -14 -1053 535 C ATOM 2159 N GLN A1088 58.101 -7.088 31.686 1.00 76.11 N ANISOU 2159 N GLN A1088 6461 13489 8966 -353 -950 456 N ATOM 2160 CA GLN A1088 57.517 -5.753 31.526 1.00 75.85 C ANISOU 2160 CA GLN A1088 6492 13377 8952 -495 -932 489 C ATOM 2161 C GLN A1088 57.208 -5.477 30.054 1.00 82.25 C ANISOU 2161 C GLN A1088 7346 14168 9738 -561 -907 534 C ATOM 2162 O GLN A1088 56.204 -4.833 29.753 1.00 81.73 O ANISOU 2162 O GLN A1088 7359 13971 9725 -621 -919 613 O ATOM 2163 CB GLN A1088 58.484 -4.682 32.053 1.00 77.67 C ANISOU 2163 CB GLN A1088 6626 13712 9171 -609 -902 439 C ATOM 2164 CG GLN A1088 58.374 -4.380 33.535 1.00 77.38 C ANISOU 2164 CG GLN A1088 6545 13703 9152 -618 -923 386 C ATOM 2165 CD GLN A1088 58.985 -3.037 33.855 1.00 91.85 C ANISOU 2165 CD GLN A1088 8291 15583 11025 -772 -878 299 C ATOM 2166 OE1 GLN A1088 60.112 -2.720 33.452 1.00 87.81 O ANISOU 2166 OE1 GLN A1088 7696 15190 10476 -832 -842 268 O ATOM 2167 NE2 GLN A1088 58.263 -2.220 34.609 1.00 83.27 N ANISOU 2167 NE2 GLN A1088 7202 14403 10034 -846 -873 232 N ATOM 2168 N ALA A1089 58.093 -5.950 29.138 1.00 81.35 N ANISOU 2168 N ALA A1089 7155 14216 9537 -556 -873 483 N ATOM 2169 CA ALA A1089 57.980 -5.803 27.680 1.00 82.14 C ANISOU 2169 CA ALA A1089 7252 14409 9550 -638 -843 514 C ATOM 2170 C ALA A1089 56.825 -6.627 27.119 1.00 86.83 C ANISOU 2170 C ALA A1089 7918 14926 10149 -567 -866 509 C ATOM 2171 O ALA A1089 56.348 -6.342 26.018 1.00 88.02 O ANISOU 2171 O ALA A1089 8079 15146 10218 -653 -860 572 O ATOM 2172 CB ALA A1089 59.275 -6.223 27.015 1.00 84.13 C ANISOU 2172 CB ALA A1089 7369 14900 9698 -648 -792 401 C ATOM 2173 N ALA A1090 56.379 -7.649 27.875 1.00 82.27 N ANISOU 2173 N ALA A1090 7373 14222 9662 -422 -895 449 N ATOM 2174 CA ALA A1090 55.267 -8.517 27.506 1.00 81.44 C ANISOU 2174 CA ALA A1090 7329 14016 9599 -352 -913 421 C ATOM 2175 C ALA A1090 53.928 -7.779 27.631 1.00 84.27 C ANISOU 2175 C ALA A1090 7805 14227 9987 -405 -951 546 C ATOM 2176 O ALA A1090 52.924 -8.245 27.085 1.00 84.26 O ANISOU 2176 O ALA A1090 7850 14177 9990 -384 -964 535 O ATOM 2177 CB ALA A1090 55.271 -9.763 28.374 1.00 81.97 C ANISOU 2177 CB ALA A1090 7381 13969 9795 -196 -933 359 C ATOM 2178 N ALA A1091 53.923 -6.612 28.315 1.00 80.07 N ANISOU 2178 N ALA A1091 7299 13629 9495 -478 -965 638 N ATOM 2179 CA ALA A1091 52.743 -5.765 28.494 1.00 79.51 C ANISOU 2179 CA ALA A1091 7307 13400 9505 -527 -1000 736 C ATOM 2180 C ALA A1091 52.333 -5.089 27.183 1.00 84.81 C ANISOU 2180 C ALA A1091 7978 14120 10127 -628 -1009 858 C ATOM 2181 O ALA A1091 51.172 -4.716 27.046 1.00 84.22 O ANISOU 2181 O ALA A1091 7958 13923 10119 -638 -1049 941 O ATOM 2182 CB ALA A1091 52.999 -4.717 29.566 1.00 80.26 C ANISOU 2182 CB ALA A1091 7382 13417 9695 -584 -999 743 C ATOM 2183 N GLU A1092 53.274 -4.939 26.220 1.00 83.44 N ANISOU 2183 N GLU A1092 7725 14150 9827 -708 -975 881 N ATOM 2184 CA GLU A1092 53.019 -4.348 24.899 1.00 84.84 C ANISOU 2184 CA GLU A1092 7870 14461 9906 -828 -987 1037 C ATOM 2185 C GLU A1092 52.122 -5.275 24.076 1.00 89.71 C ANISOU 2185 C GLU A1092 8497 15172 10417 -786 -1004 988 C ATOM 2186 O GLU A1092 51.308 -4.799 23.280 1.00 90.40 O ANISOU 2186 O GLU A1092 8584 15301 10461 -855 -1047 1146 O ATOM 2187 CB GLU A1092 54.333 -4.073 24.159 1.00 87.82 C ANISOU 2187 CB GLU A1092 8136 15093 10139 -938 -935 1050 C ATOM 2188 CG GLU A1092 55.159 -2.945 24.762 1.00101.96 C ANISOU 2188 CG GLU A1092 9898 16802 12040 -1025 -918 1130 C ATOM 2189 CD GLU A1092 56.668 -3.056 24.605 1.00130.95 C ANISOU 2189 CD GLU A1092 13463 20693 15598 -1080 -853 1037 C ATOM 2190 OE1 GLU A1092 57.386 -2.751 25.586 1.00131.90 O ANISOU 2190 OE1 GLU A1092 13565 20735 15816 -1068 -833 962 O ATOM 2191 OE2 GLU A1092 57.137 -3.438 23.507 1.00123.71 O ANISOU 2191 OE2 GLU A1092 12461 20056 14485 -1144 -820 1021 O ATOM 2192 N GLN A1093 52.264 -6.601 24.292 1.00 85.75 N ANISOU 2192 N GLN A1093 7988 14696 9898 -672 -973 770 N ATOM 2193 CA GLN A1093 51.470 -7.652 23.651 1.00 85.54 C ANISOU 2193 CA GLN A1093 7953 14731 9817 -624 -972 648 C ATOM 2194 C GLN A1093 50.092 -7.722 24.297 1.00 88.59 C ANISOU 2194 C GLN A1093 8450 14874 10337 -556 -1024 695 C ATOM 2195 O GLN A1093 49.086 -7.873 23.594 1.00 88.25 O ANISOU 2195 O GLN A1093 8411 14880 10239 -580 -1052 717 O ATOM 2196 CB GLN A1093 52.181 -9.008 23.756 1.00 87.03 C ANISOU 2196 CB GLN A1093 8072 14964 10032 -522 -916 394 C ATOM 2197 CG GLN A1093 53.392 -9.133 22.838 1.00107.28 C ANISOU 2197 CG GLN A1093 10490 17830 12444 -594 -854 281 C ATOM 2198 CD GLN A1093 54.633 -9.549 23.585 1.00124.80 C ANISOU 2198 CD GLN A1093 12652 20008 14758 -508 -820 168 C ATOM 2199 OE1 GLN A1093 54.748 -10.680 24.071 1.00118.19 O ANISOU 2199 OE1 GLN A1093 11787 19049 14072 -371 -808 7 O ATOM 2200 NE2 GLN A1093 55.602 -8.647 23.670 1.00118.40 N ANISOU 2200 NE2 GLN A1093 11807 19302 13878 -592 -807 263 N ATOM 2201 N LEU A1094 50.057 -7.605 25.648 1.00 83.99 N ANISOU 2201 N LEU A1094 7937 14066 9910 -484 -1037 704 N ATOM 2202 CA LEU A1094 48.848 -7.614 26.486 1.00 82.27 C ANISOU 2202 CA LEU A1094 7809 13631 9819 -430 -1077 732 C ATOM 2203 C LEU A1094 47.954 -6.425 26.139 1.00 84.71 C ANISOU 2203 C LEU A1094 8142 13882 10160 -507 -1127 897 C ATOM 2204 O LEU A1094 46.738 -6.573 26.065 1.00 83.99 O ANISOU 2204 O LEU A1094 8091 13710 10110 -483 -1163 909 O ATOM 2205 CB LEU A1094 49.253 -7.560 27.971 1.00 81.56 C ANISOU 2205 CB LEU A1094 7741 13414 9834 -379 -1072 712 C ATOM 2206 CG LEU A1094 49.337 -8.868 28.773 1.00 86.07 C ANISOU 2206 CG LEU A1094 8315 13927 10459 -269 -1062 618 C ATOM 2207 CD1 LEU A1094 50.224 -9.893 28.107 1.00 87.28 C ANISOU 2207 CD1 LEU A1094 8393 14186 10583 -218 -1025 508 C ATOM 2208 CD2 LEU A1094 49.911 -8.608 30.151 1.00 87.93 C ANISOU 2208 CD2 LEU A1094 8536 14138 10735 -253 -1066 640 C ATOM 2209 N LYS A1095 48.578 -5.257 25.896 1.00 80.83 N ANISOU 2209 N LYS A1095 7610 13426 9675 -600 -1132 1032 N ATOM 2210 CA LYS A1095 47.928 -4.012 25.514 1.00 80.96 C ANISOU 2210 CA LYS A1095 7617 13360 9784 -677 -1186 1233 C ATOM 2211 C LYS A1095 47.181 -4.170 24.193 1.00 85.30 C ANISOU 2211 C LYS A1095 8135 14074 10200 -717 -1229 1345 C ATOM 2212 O LYS A1095 46.034 -3.747 24.109 1.00 86.05 O ANISOU 2212 O LYS A1095 8244 14057 10392 -709 -1291 1451 O ATOM 2213 CB LYS A1095 48.966 -2.879 25.403 1.00 84.59 C ANISOU 2213 CB LYS A1095 8015 13834 10290 -783 -1170 1360 C ATOM 2214 CG LYS A1095 48.998 -1.925 26.590 1.00 97.70 C ANISOU 2214 CG LYS A1095 9678 15247 12196 -789 -1166 1337 C ATOM 2215 CD LYS A1095 48.115 -0.702 26.338 1.00110.54 C ANISOU 2215 CD LYS A1095 11276 16675 14050 -840 -1226 1528 C ATOM 2216 CE LYS A1095 48.001 0.187 27.549 1.00122.87 C ANISOU 2216 CE LYS A1095 12812 17978 15894 -841 -1211 1424 C ATOM 2217 NZ LYS A1095 47.038 1.295 27.324 1.00131.67 N ANISOU 2217 NZ LYS A1095 13878 18851 17301 -866 -1272 1580 N ATOM 2218 N THR A1096 47.809 -4.811 23.184 1.00 81.60 N ANISOU 2218 N THR A1096 7602 13896 9505 -763 -1195 1298 N ATOM 2219 CA THR A1096 47.220 -5.014 21.852 1.00 82.35 C ANISOU 2219 CA THR A1096 7627 14252 9409 -829 -1228 1374 C ATOM 2220 C THR A1096 46.098 -6.073 21.889 1.00 83.58 C ANISOU 2220 C THR A1096 7820 14376 9559 -741 -1237 1199 C ATOM 2221 O THR A1096 45.073 -5.886 21.221 1.00 83.73 O ANISOU 2221 O THR A1096 7810 14480 9524 -773 -1298 1308 O ATOM 2222 CB THR A1096 48.290 -5.361 20.798 1.00 92.81 C ANISOU 2222 CB THR A1096 8837 15949 10478 -927 -1173 1320 C ATOM 2223 OG1 THR A1096 49.005 -6.531 21.201 1.00 95.43 O ANISOU 2223 OG1 THR A1096 9167 16289 10802 -842 -1094 1016 O ATOM 2224 CG2 THR A1096 49.262 -4.211 20.541 1.00 91.29 C ANISOU 2224 CG2 THR A1096 8588 15832 10266 -1053 -1172 1548 C ATOM 2225 N THR A1097 46.284 -7.165 22.675 1.00 77.15 N ANISOU 2225 N THR A1097 7056 13440 8818 -636 -1180 951 N ATOM 2226 CA THR A1097 45.284 -8.229 22.832 1.00 75.63 C ANISOU 2226 CA THR A1097 6896 13172 8669 -558 -1177 780 C ATOM 2227 C THR A1097 44.019 -7.624 23.445 1.00 76.85 C ANISOU 2227 C THR A1097 7126 13106 8968 -527 -1243 902 C ATOM 2228 O THR A1097 42.938 -7.801 22.880 1.00 76.30 O ANISOU 2228 O THR A1097 7037 13100 8855 -537 -1282 906 O ATOM 2229 CB THR A1097 45.833 -9.399 23.654 1.00 82.84 C ANISOU 2229 CB THR A1097 7834 13954 9686 -457 -1113 563 C ATOM 2230 OG1 THR A1097 47.110 -9.771 23.140 1.00 85.26 O ANISOU 2230 OG1 THR A1097 8051 14445 9899 -478 -1055 456 O ATOM 2231 CG2 THR A1097 44.900 -10.609 23.651 1.00 80.11 C ANISOU 2231 CG2 THR A1097 7495 13539 9405 -398 -1096 383 C ATOM 2232 N ARG A1098 44.173 -6.853 24.549 1.00 71.74 N ANISOU 2232 N ARG A1098 6538 12233 8488 -500 -1254 981 N ATOM 2233 CA ARG A1098 43.077 -6.144 25.211 1.00 71.30 C ANISOU 2233 CA ARG A1098 6523 11966 8601 -477 -1306 1060 C ATOM 2234 C ARG A1098 42.392 -5.200 24.219 1.00 77.78 C ANISOU 2234 C ARG A1098 7284 12854 9414 -539 -1386 1277 C ATOM 2235 O ARG A1098 41.160 -5.176 24.141 1.00 76.65 O ANISOU 2235 O ARG A1098 7140 12651 9331 -512 -1437 1299 O ATOM 2236 CB ARG A1098 43.584 -5.358 26.435 1.00 69.96 C ANISOU 2236 CB ARG A1098 6377 11606 8597 -468 -1291 1067 C ATOM 2237 CG ARG A1098 42.461 -4.773 27.296 1.00 78.88 C ANISOU 2237 CG ARG A1098 7524 12526 9919 -439 -1323 1058 C ATOM 2238 CD ARG A1098 42.298 -3.274 27.113 1.00 88.70 C ANISOU 2238 CD ARG A1098 8709 13648 11345 -489 -1373 1221 C ATOM 2239 NE ARG A1098 43.163 -2.516 28.019 1.00 97.69 N ANISOU 2239 NE ARG A1098 9823 14679 12616 -519 -1333 1175 N ATOM 2240 CZ ARG A1098 44.210 -1.791 27.637 1.00112.65 C ANISOU 2240 CZ ARG A1098 11672 16599 14530 -590 -1324 1288 C ATOM 2241 NH1 ARG A1098 44.535 -1.703 26.352 1.00 97.63 N ANISOU 2241 NH1 ARG A1098 9742 14847 12504 -645 -1354 1480 N ATOM 2242 NH2 ARG A1098 44.934 -1.136 28.536 1.00101.48 N ANISOU 2242 NH2 ARG A1098 10222 15089 13247 -624 -1281 1203 N ATOM 2243 N ASN A1099 43.208 -4.451 23.444 1.00 76.73 N ANISOU 2243 N ASN A1099 7086 12863 9205 -628 -1399 1456 N ATOM 2244 CA ASN A1099 42.735 -3.490 22.450 1.00 78.41 C ANISOU 2244 CA ASN A1099 7217 13166 9410 -703 -1486 1742 C ATOM 2245 C ASN A1099 41.902 -4.150 21.348 1.00 82.84 C ANISOU 2245 C ASN A1099 7719 14003 9754 -726 -1526 1747 C ATOM 2246 O ASN A1099 41.024 -3.495 20.781 1.00 84.15 O ANISOU 2246 O ASN A1099 7821 14201 9953 -750 -1621 1970 O ATOM 2247 CB ASN A1099 43.900 -2.700 21.849 1.00 78.71 C ANISOU 2247 CB ASN A1099 7187 13334 9387 -816 -1481 1945 C ATOM 2248 CG ASN A1099 44.394 -1.562 22.721 1.00 97.86 C ANISOU 2248 CG ASN A1099 9624 15463 12096 -825 -1476 2032 C ATOM 2249 OD1 ASN A1099 43.756 -1.145 23.699 1.00 88.03 O ANISOU 2249 OD1 ASN A1099 8416 13919 11113 -755 -1489 1967 O ATOM 2250 ND2 ASN A1099 45.561 -1.036 22.390 1.00 94.04 N ANISOU 2250 ND2 ASN A1099 9090 15073 11567 -924 -1448 2152 N ATOM 2251 N ALA A1100 42.147 -5.441 21.076 1.00 78.32 N ANISOU 2251 N ALA A1100 7147 13622 8989 -715 -1457 1490 N ATOM 2252 CA ALA A1100 41.423 -6.190 20.051 1.00 79.12 C ANISOU 2252 CA ALA A1100 7168 14016 8878 -751 -1474 1410 C ATOM 2253 C ALA A1100 40.067 -6.724 20.566 1.00 81.62 C ANISOU 2253 C ALA A1100 7536 14160 9315 -664 -1496 1279 C ATOM 2254 O ALA A1100 39.237 -7.152 19.756 1.00 82.61 O ANISOU 2254 O ALA A1100 7585 14508 9297 -697 -1528 1237 O ATOM 2255 CB ALA A1100 42.283 -7.339 19.545 1.00 80.13 C ANISOU 2255 CB ALA A1100 7243 14395 8808 -782 -1377 1137 C ATOM 2256 N TYR A1101 39.826 -6.666 21.892 1.00 75.45 N ANISOU 2256 N TYR A1101 6866 13024 8779 -570 -1479 1212 N ATOM 2257 CA TYR A1101 38.582 -7.177 22.459 1.00 73.94 C ANISOU 2257 CA TYR A1101 6717 12679 8697 -503 -1490 1085 C ATOM 2258 C TYR A1101 37.690 -6.093 23.088 1.00 75.31 C ANISOU 2258 C TYR A1101 6904 12616 9095 -463 -1565 1240 C ATOM 2259 O TYR A1101 36.636 -6.433 23.629 1.00 74.22 O ANISOU 2259 O TYR A1101 6791 12358 9052 -414 -1571 1130 O ATOM 2260 CB TYR A1101 38.878 -8.304 23.458 1.00 74.11 C ANISOU 2260 CB TYR A1101 6823 12540 8795 -438 -1398 833 C ATOM 2261 CG TYR A1101 39.206 -9.596 22.748 1.00 77.31 C ANISOU 2261 CG TYR A1101 7180 13135 9059 -457 -1333 616 C ATOM 2262 CD1 TYR A1101 38.196 -10.432 22.277 1.00 80.17 C ANISOU 2262 CD1 TYR A1101 7500 13579 9383 -465 -1329 459 C ATOM 2263 CD2 TYR A1101 40.525 -9.945 22.469 1.00 78.64 C ANISOU 2263 CD2 TYR A1101 7318 13415 9147 -476 -1272 543 C ATOM 2264 CE1 TYR A1101 38.491 -11.592 21.559 1.00 82.84 C ANISOU 2264 CE1 TYR A1101 7759 14088 9628 -494 -1260 211 C ATOM 2265 CE2 TYR A1101 40.833 -11.103 21.756 1.00 80.73 C ANISOU 2265 CE2 TYR A1101 7501 13852 9322 -494 -1206 299 C ATOM 2266 CZ TYR A1101 39.812 -11.922 21.295 1.00 89.29 C ANISOU 2266 CZ TYR A1101 8535 15001 10391 -506 -1197 123 C ATOM 2267 OH TYR A1101 40.111 -13.076 20.605 1.00 90.01 O ANISOU 2267 OH TYR A1101 8518 15242 10439 -530 -1119 -171 O ATOM 2268 N ILE A1102 38.054 -4.800 22.938 1.00 71.45 N ANISOU 2268 N ILE A1102 6375 12064 8709 -493 -1620 1488 N ATOM 2269 CA ILE A1102 37.280 -3.660 23.457 1.00 71.04 C ANISOU 2269 CA ILE A1102 6295 11759 8938 -455 -1692 1625 C ATOM 2270 C ILE A1102 35.868 -3.671 22.843 1.00 76.37 C ANISOU 2270 C ILE A1102 6897 12512 9607 -435 -1781 1695 C ATOM 2271 O ILE A1102 34.883 -3.571 23.577 1.00 74.91 O ANISOU 2271 O ILE A1102 6719 12135 9610 -370 -1796 1599 O ATOM 2272 CB ILE A1102 37.990 -2.290 23.209 1.00 74.97 C ANISOU 2272 CB ILE A1102 6731 12171 9584 -506 -1738 1903 C ATOM 2273 CG1 ILE A1102 39.423 -2.264 23.776 1.00 73.96 C ANISOU 2273 CG1 ILE A1102 6659 11999 9445 -538 -1648 1820 C ATOM 2274 CG2 ILE A1102 37.151 -1.115 23.754 1.00 76.45 C ANISOU 2274 CG2 ILE A1102 6857 12047 10144 -457 -1808 2009 C ATOM 2275 CD1 ILE A1102 40.241 -1.047 23.385 1.00 80.99 C ANISOU 2275 CD1 ILE A1102 7479 12858 10436 -618 -1679 2090 C ATOM 2276 N GLN A1103 35.791 -3.804 21.500 1.00 75.74 N ANISOU 2276 N GLN A1103 6729 12759 9290 -501 -1838 1850 N ATOM 2277 CA GLN A1103 34.555 -3.829 20.705 1.00 77.32 C ANISOU 2277 CA GLN A1103 6826 13135 9418 -501 -1936 1948 C ATOM 2278 C GLN A1103 33.668 -5.019 21.120 1.00 79.10 C ANISOU 2278 C GLN A1103 7100 13360 9594 -455 -1881 1622 C ATOM 2279 O GLN A1103 32.463 -4.830 21.277 1.00 79.40 O ANISOU 2279 O GLN A1103 7095 13319 9756 -406 -1944 1626 O ATOM 2280 CB GLN A1103 34.838 -3.817 19.179 1.00 81.12 C ANISOU 2280 CB GLN A1103 7179 14061 9582 -614 -1995 2161 C ATOM 2281 CG GLN A1103 35.892 -4.825 18.675 1.00102.96 C ANISOU 2281 CG GLN A1103 9962 17120 12039 -694 -1887 1955 C ATOM 2282 CD GLN A1103 37.328 -4.338 18.790 1.00121.81 C ANISOU 2282 CD GLN A1103 12381 19468 14432 -742 -1840 2062 C ATOM 2283 OE1 GLN A1103 37.940 -4.357 19.865 1.00113.52 O ANISOU 2283 OE1 GLN A1103 11449 18121 13563 -684 -1763 1924 O ATOM 2284 NE2 GLN A1103 37.919 -3.948 17.669 1.00116.28 N ANISOU 2284 NE2 GLN A1103 11562 19113 13506 -864 -1880 2303 N ATOM 2285 N LYS A1104 34.269 -6.204 21.374 1.00 73.29 N ANISOU 2285 N LYS A1104 6445 12677 8725 -468 -1765 1345 N ATOM 2286 CA LYS A1104 33.545 -7.394 21.843 1.00 71.51 C ANISOU 2286 CA LYS A1104 6266 12406 8498 -437 -1700 1048 C ATOM 2287 C LYS A1104 33.081 -7.210 23.312 1.00 72.83 C ANISOU 2287 C LYS A1104 6522 12222 8928 -361 -1673 965 C ATOM 2288 O LYS A1104 32.030 -7.733 23.682 1.00 72.64 O ANISOU 2288 O LYS A1104 6498 12143 8958 -338 -1666 824 O ATOM 2289 CB LYS A1104 34.398 -8.664 21.687 1.00 73.41 C ANISOU 2289 CB LYS A1104 6542 12758 8594 -469 -1588 807 C ATOM 2290 CG LYS A1104 34.448 -9.200 20.255 1.00 84.52 C ANISOU 2290 CG LYS A1104 7820 14567 9726 -557 -1592 744 C ATOM 2291 N TYR A1105 33.853 -6.446 24.131 1.00 67.26 N ANISOU 2291 N TYR A1105 5870 11314 8372 -339 -1654 1039 N ATOM 2292 CA TYR A1105 33.527 -6.121 25.530 1.00 64.54 C ANISOU 2292 CA TYR A1105 5572 10699 8250 -291 -1624 947 C ATOM 2293 C TYR A1105 32.314 -5.199 25.564 1.00 68.23 C ANISOU 2293 C TYR A1105 5951 11063 8909 -255 -1712 1029 C ATOM 2294 O TYR A1105 31.333 -5.504 26.243 1.00 67.15 O ANISOU 2294 O TYR A1105 5813 10846 8856 -228 -1696 874 O ATOM 2295 CB TYR A1105 34.740 -5.480 26.259 1.00 63.96 C ANISOU 2295 CB TYR A1105 5539 10495 8269 -295 -1583 987 C ATOM 2296 CG TYR A1105 34.404 -4.600 27.452 1.00 64.48 C ANISOU 2296 CG TYR A1105 5583 10328 8587 -268 -1579 933 C ATOM 2297 CD1 TYR A1105 34.627 -3.226 27.416 1.00 66.95 C ANISOU 2297 CD1 TYR A1105 5822 10502 9113 -269 -1629 1076 C ATOM 2298 CD2 TYR A1105 33.907 -5.147 28.635 1.00 64.16 C ANISOU 2298 CD2 TYR A1105 5575 10220 8584 -257 -1518 728 C ATOM 2299 CE1 TYR A1105 34.328 -2.412 28.509 1.00 66.27 C ANISOU 2299 CE1 TYR A1105 5682 10206 9291 -252 -1612 960 C ATOM 2300 CE2 TYR A1105 33.611 -4.343 29.738 1.00 64.96 C ANISOU 2300 CE2 TYR A1105 5622 10168 8891 -252 -1502 627 C ATOM 2301 CZ TYR A1105 33.826 -2.975 29.670 1.00 71.60 C ANISOU 2301 CZ TYR A1105 6378 10864 9961 -246 -1545 716 C ATOM 2302 OH TYR A1105 33.543 -2.173 30.751 1.00 73.21 O ANISOU 2302 OH TYR A1105 6497 10919 10400 -248 -1517 555 O ATOM 2303 N LEU A1106 32.382 -4.083 24.808 1.00 65.62 N ANISOU 2303 N LEU A1106 5531 10740 8661 -258 -1808 1287 N ATOM 2304 CA LEU A1106 31.323 -3.081 24.715 1.00 66.32 C ANISOU 2304 CA LEU A1106 5503 10704 8993 -210 -1912 1417 C ATOM 2305 C LEU A1106 30.035 -3.700 24.181 1.00 68.80 C ANISOU 2305 C LEU A1106 5759 11178 9202 -194 -1963 1364 C ATOM 2306 O LEU A1106 28.952 -3.255 24.559 1.00 68.74 O ANISOU 2306 O LEU A1106 5673 11037 9406 -137 -2012 1331 O ATOM 2307 CB LEU A1106 31.770 -1.889 23.851 1.00 68.33 C ANISOU 2307 CB LEU A1106 5660 10951 9353 -227 -2014 1772 C ATOM 2308 CG LEU A1106 32.869 -0.988 24.467 1.00 72.58 C ANISOU 2308 CG LEU A1106 6217 11257 10102 -243 -1974 1824 C ATOM 2309 CD1 LEU A1106 33.501 -0.104 23.420 1.00 74.89 C ANISOU 2309 CD1 LEU A1106 6427 11611 10416 -296 -2059 2201 C ATOM 2310 CD2 LEU A1106 32.332 -0.126 25.607 1.00 74.43 C ANISOU 2310 CD2 LEU A1106 6392 11149 10739 -181 -1966 1690 C ATOM 2311 N ALA A 306 30.161 -4.776 23.374 1.00 71.25 N ANISOU 2311 N ALA A 306 5701 13591 7779 -1972 -1563 551 N ATOM 2312 CA ALA A 306 29.038 -5.535 22.826 1.00 68.52 C ANISOU 2312 CA ALA A 306 5438 13153 7443 -1727 -1471 507 C ATOM 2313 C ALA A 306 28.335 -6.330 23.927 1.00 71.49 C ANISOU 2313 C ALA A 306 5888 13402 7872 -1448 -1444 326 C ATOM 2314 O ALA A 306 27.102 -6.319 23.976 1.00 70.77 O ANISOU 2314 O ALA A 306 5968 13068 7853 -1317 -1453 272 O ATOM 2315 CB ALA A 306 29.515 -6.473 21.726 1.00 68.88 C ANISOU 2315 CB ALA A 306 5286 13535 7350 -1665 -1332 558 C ATOM 2316 N ALA A 307 29.115 -7.008 24.809 1.00 67.79 N ANISOU 2316 N ALA A 307 5281 13119 7358 -1364 -1417 243 N ATOM 2317 CA ALA A 307 28.609 -7.832 25.922 1.00 66.29 C ANISOU 2317 CA ALA A 307 5135 12858 7195 -1121 -1396 99 C ATOM 2318 C ALA A 307 27.723 -7.031 26.895 1.00 70.66 C ANISOU 2318 C ALA A 307 5883 13114 7850 -1121 -1504 15 C ATOM 2319 O ALA A 307 26.674 -7.534 27.329 1.00 68.01 O ANISOU 2319 O ALA A 307 5649 12647 7545 -927 -1478 -74 O ATOM 2320 CB ALA A 307 29.769 -8.465 26.682 1.00 67.57 C ANISOU 2320 CB ALA A 307 5108 13282 7283 -1075 -1377 58 C ATOM 2321 N ARG A 308 28.147 -5.776 27.201 1.00 69.70 N ANISOU 2321 N ARG A 308 5811 12896 7777 -1346 -1631 38 N ATOM 2322 CA ARG A 308 27.502 -4.804 28.096 1.00 69.50 C ANISOU 2322 CA ARG A 308 5964 12594 7848 -1371 -1764 -61 C ATOM 2323 C ARG A 308 26.089 -4.428 27.660 1.00 74.10 C ANISOU 2323 C ARG A 308 6746 12900 8508 -1275 -1786 -79 C ATOM 2324 O ARG A 308 25.309 -3.950 28.487 1.00 73.89 O ANISOU 2324 O ARG A 308 6855 12675 8544 -1191 -1869 -208 O ATOM 2325 CB ARG A 308 28.334 -3.522 28.165 1.00 68.65 C ANISOU 2325 CB ARG A 308 5873 12428 7781 -1667 -1905 -7 C ATOM 2326 CG ARG A 308 29.690 -3.687 28.802 1.00 71.44 C ANISOU 2326 CG ARG A 308 6035 13048 8061 -1781 -1914 -16 C ATOM 2327 CD ARG A 308 30.362 -2.346 28.977 1.00 83.01 C ANISOU 2327 CD ARG A 308 7548 14412 9581 -2091 -2076 18 C ATOM 2328 NE ARG A 308 29.791 -1.588 30.092 1.00 93.19 N ANISOU 2328 NE ARG A 308 9011 15430 10965 -2057 -2215 -151 N ATOM 2329 CZ ARG A 308 29.129 -0.443 29.963 1.00110.12 C ANISOU 2329 CZ ARG A 308 11381 17225 13235 -2144 -2358 -169 C ATOM 2330 NH1 ARG A 308 28.958 0.103 28.765 1.00 99.61 N ANISOU 2330 NH1 ARG A 308 10137 15760 11951 -2289 -2384 0 N ATOM 2331 NH2 ARG A 308 28.646 0.174 31.033 1.00 98.43 N ANISOU 2331 NH2 ARG A 308 10038 15533 11826 -2077 -2484 -359 N ATOM 2332 N GLU A 309 25.774 -4.614 26.362 1.00 71.54 N ANISOU 2332 N GLU A 309 6427 12588 8168 -1282 -1717 40 N ATOM 2333 CA GLU A 309 24.480 -4.292 25.746 1.00 71.36 C ANISOU 2333 CA GLU A 309 6571 12341 8203 -1197 -1733 47 C ATOM 2334 C GLU A 309 23.405 -5.360 26.021 1.00 73.93 C ANISOU 2334 C GLU A 309 6911 12676 8503 -926 -1632 -60 C ATOM 2335 O GLU A 309 22.235 -5.129 25.692 1.00 73.31 O ANISOU 2335 O GLU A 309 6960 12431 8464 -831 -1648 -83 O ATOM 2336 CB GLU A 309 24.638 -4.102 24.227 1.00 73.61 C ANISOU 2336 CB GLU A 309 6833 12677 8458 -1329 -1700 229 C ATOM 2337 CG GLU A 309 25.472 -2.894 23.830 1.00 90.78 C ANISOU 2337 CG GLU A 309 9032 14795 10665 -1631 -1822 371 C ATOM 2338 CD GLU A 309 25.330 -2.477 22.379 1.00126.76 C ANISOU 2338 CD GLU A 309 13611 19355 15198 -1767 -1819 567 C ATOM 2339 OE1 GLU A 309 25.495 -3.342 21.487 1.00129.93 O ANISOU 2339 OE1 GLU A 309 13864 20015 15488 -1726 -1681 631 O ATOM 2340 OE2 GLU A 309 25.060 -1.278 22.133 1.00127.59 O ANISOU 2340 OE2 GLU A 309 13884 19203 15391 -1911 -1964 654 O ATOM 2341 N ARG A 310 23.803 -6.518 26.616 1.00 69.70 N ANISOU 2341 N ARG A 310 6246 12336 7901 -809 -1539 -116 N ATOM 2342 CA ARG A 310 22.959 -7.678 26.979 1.00 67.77 C ANISOU 2342 CA ARG A 310 6002 12121 7625 -585 -1449 -197 C ATOM 2343 C ARG A 310 21.838 -7.922 25.934 1.00 68.31 C ANISOU 2343 C ARG A 310 6147 12109 7699 -505 -1393 -165 C ATOM 2344 O ARG A 310 20.653 -7.756 26.234 1.00 66.69 O ANISOU 2344 O ARG A 310 6052 11765 7522 -403 -1418 -238 O ATOM 2345 CB ARG A 310 22.353 -7.541 28.399 1.00 68.65 C ANISOU 2345 CB ARG A 310 6182 12146 7754 -484 -1510 -337 C ATOM 2346 CG ARG A 310 23.313 -7.043 29.474 1.00 82.37 C ANISOU 2346 CG ARG A 310 7867 13940 9489 -575 -1593 -388 C ATOM 2347 CD ARG A 310 22.534 -6.530 30.661 1.00 98.69 C ANISOU 2347 CD ARG A 310 10022 15902 11572 -490 -1676 -540 C ATOM 2348 NE ARG A 310 23.017 -5.226 31.117 1.00114.46 N ANISOU 2348 NE ARG A 310 12076 17787 13626 -632 -1820 -599 N ATOM 2349 CZ ARG A 310 22.230 -4.227 31.504 1.00133.08 C ANISOU 2349 CZ ARG A 310 14579 19939 16048 -605 -1936 -713 C ATOM 2350 NH1 ARG A 310 20.908 -4.363 31.480 1.00120.64 N ANISOU 2350 NH1 ARG A 310 13085 18279 14473 -437 -1914 -777 N ATOM 2351 NH2 ARG A 310 22.758 -3.079 31.910 1.00121.65 N ANISOU 2351 NH2 ARG A 310 13192 18370 14661 -742 -2082 -774 N ATOM 2352 N LYS A 311 22.242 -8.299 24.706 1.00 62.98 N ANISOU 2352 N LYS A 311 5397 11552 6982 -553 -1319 -63 N ATOM 2353 CA LYS A 311 21.367 -8.602 23.578 1.00 60.73 C ANISOU 2353 CA LYS A 311 5154 11241 6681 -495 -1259 -25 C ATOM 2354 C LYS A 311 20.360 -9.726 23.918 1.00 60.79 C ANISOU 2354 C LYS A 311 5185 11240 6673 -300 -1186 -120 C ATOM 2355 O LYS A 311 19.210 -9.622 23.501 1.00 61.92 O ANISOU 2355 O LYS A 311 5415 11285 6827 -241 -1184 -136 O ATOM 2356 CB LYS A 311 22.209 -8.993 22.343 1.00 63.93 C ANISOU 2356 CB LYS A 311 5430 11848 7014 -573 -1184 78 C ATOM 2357 CG LYS A 311 21.410 -9.029 21.031 1.00 86.07 C ANISOU 2357 CG LYS A 311 8274 14640 9790 -559 -1142 135 C ATOM 2358 CD LYS A 311 21.973 -10.009 20.003 1.00 96.87 C ANISOU 2358 CD LYS A 311 9495 16251 11059 -530 -1031 159 C ATOM 2359 CE LYS A 311 22.907 -9.356 19.013 1.00106.33 C ANISOU 2359 CE LYS A 311 10588 17623 12189 -720 -1036 298 C ATOM 2360 NZ LYS A 311 23.348 -10.307 17.961 1.00112.97 N ANISOU 2360 NZ LYS A 311 11276 18733 12916 -664 -927 292 N ATOM 2361 N ALA A 312 20.771 -10.775 24.666 1.00 53.13 N ANISOU 2361 N ALA A 312 4139 10373 5674 -210 -1137 -172 N ATOM 2362 CA ALA A 312 19.899 -11.907 25.009 1.00 51.37 C ANISOU 2362 CA ALA A 312 3942 10139 5437 -58 -1080 -235 C ATOM 2363 C ALA A 312 18.696 -11.486 25.888 1.00 56.22 C ANISOU 2363 C ALA A 312 4660 10628 6072 -5 -1130 -308 C ATOM 2364 O ALA A 312 17.546 -11.861 25.572 1.00 55.54 O ANISOU 2364 O ALA A 312 4626 10500 5975 65 -1097 -333 O ATOM 2365 CB ALA A 312 20.689 -13.018 25.686 1.00 51.64 C ANISOU 2365 CB ALA A 312 3889 10287 5445 16 -1046 -252 C ATOM 2366 N THR A 313 18.941 -10.682 26.943 1.00 52.44 N ANISOU 2366 N THR A 313 4200 10110 5614 -39 -1214 -353 N ATOM 2367 CA THR A 313 17.845 -10.221 27.799 1.00 52.96 C ANISOU 2367 CA THR A 313 4344 10096 5682 28 -1267 -447 C ATOM 2368 C THR A 313 17.027 -9.149 27.071 1.00 58.15 C ANISOU 2368 C THR A 313 5101 10612 6382 15 -1324 -454 C ATOM 2369 O THR A 313 15.791 -9.165 27.170 1.00 57.42 O ANISOU 2369 O THR A 313 5057 10489 6271 111 -1323 -516 O ATOM 2370 CB THR A 313 18.322 -9.748 29.174 1.00 63.19 C ANISOU 2370 CB THR A 313 5624 11413 6973 17 -1343 -521 C ATOM 2371 OG1 THR A 313 18.967 -8.484 29.058 1.00 71.51 O ANISOU 2371 OG1 THR A 313 6712 12377 8084 -99 -1438 -519 O ATOM 2372 CG2 THR A 313 19.231 -10.739 29.836 1.00 59.52 C ANISOU 2372 CG2 THR A 313 5057 11094 6463 32 -1300 -494 C ATOM 2373 N LYS A 314 17.715 -8.248 26.315 1.00 55.53 N ANISOU 2373 N LYS A 314 4793 10208 6098 -109 -1377 -378 N ATOM 2374 CA LYS A 314 17.067 -7.189 25.534 1.00 56.22 C ANISOU 2374 CA LYS A 314 4987 10140 6233 -132 -1450 -352 C ATOM 2375 C LYS A 314 16.047 -7.789 24.573 1.00 61.10 C ANISOU 2375 C LYS A 314 5612 10789 6813 -50 -1372 -324 C ATOM 2376 O LYS A 314 14.896 -7.349 24.569 1.00 60.40 O ANISOU 2376 O LYS A 314 5600 10617 6734 42 -1414 -382 O ATOM 2377 CB LYS A 314 18.080 -6.327 24.765 1.00 58.88 C ANISOU 2377 CB LYS A 314 5336 10423 6613 -315 -1510 -227 C ATOM 2378 N THR A 315 16.438 -8.846 23.838 1.00 58.88 N ANISOU 2378 N THR A 315 5244 10644 6484 -66 -1261 -259 N ATOM 2379 CA THR A 315 15.555 -9.490 22.858 1.00 59.47 C ANISOU 2379 CA THR A 315 5317 10763 6517 -5 -1187 -241 C ATOM 2380 C THR A 315 14.452 -10.321 23.541 1.00 63.99 C ANISOU 2380 C THR A 315 5893 11366 7055 122 -1144 -341 C ATOM 2381 O THR A 315 13.332 -10.354 23.019 1.00 63.83 O ANISOU 2381 O THR A 315 5903 11339 7009 180 -1131 -359 O ATOM 2382 CB THR A 315 16.346 -10.276 21.823 1.00 68.96 C ANISOU 2382 CB THR A 315 6427 12100 7674 -58 -1098 -164 C ATOM 2383 OG1 THR A 315 17.109 -11.275 22.488 1.00 74.59 O ANISOU 2383 OG1 THR A 315 7061 12908 8372 -28 -1045 -200 O ATOM 2384 CG2 THR A 315 17.276 -9.373 21.019 1.00 66.77 C ANISOU 2384 CG2 THR A 315 6130 11835 7403 -206 -1139 -45 C ATOM 2385 N LEU A 316 14.728 -10.910 24.725 1.00 60.71 N ANISOU 2385 N LEU A 316 5443 10997 6629 155 -1134 -397 N ATOM 2386 CA LEU A 316 13.710 -11.639 25.487 1.00 60.56 C ANISOU 2386 CA LEU A 316 5421 11026 6564 243 -1105 -469 C ATOM 2387 C LEU A 316 12.647 -10.649 26.005 1.00 65.66 C ANISOU 2387 C LEU A 316 6122 11623 7204 309 -1180 -555 C ATOM 2388 O LEU A 316 11.467 -11.007 26.109 1.00 65.33 O ANISOU 2388 O LEU A 316 6075 11639 7108 377 -1156 -603 O ATOM 2389 CB LEU A 316 14.328 -12.441 26.640 1.00 60.78 C ANISOU 2389 CB LEU A 316 5399 11125 6572 250 -1088 -482 C ATOM 2390 CG LEU A 316 13.396 -13.439 27.332 1.00 65.17 C ANISOU 2390 CG LEU A 316 5941 11754 7066 303 -1048 -510 C ATOM 2391 CD1 LEU A 316 13.218 -14.706 26.517 1.00 64.78 C ANISOU 2391 CD1 LEU A 316 5883 11719 7010 299 -971 -460 C ATOM 2392 CD2 LEU A 316 13.903 -13.779 28.700 1.00 68.70 C ANISOU 2392 CD2 LEU A 316 6351 12268 7485 311 -1070 -521 C ATOM 2393 N GLY A 317 13.071 -9.410 26.257 1.00 62.75 N ANISOU 2393 N GLY A 317 5804 11151 6889 288 -1279 -579 N ATOM 2394 CA GLY A 317 12.186 -8.318 26.650 1.00 63.06 C ANISOU 2394 CA GLY A 317 5909 11111 6940 374 -1377 -679 C ATOM 2395 C GLY A 317 11.236 -7.937 25.530 1.00 65.86 C ANISOU 2395 C GLY A 317 6313 11414 7298 421 -1388 -652 C ATOM 2396 O GLY A 317 10.045 -7.748 25.776 1.00 65.72 O ANISOU 2396 O GLY A 317 6300 11434 7237 540 -1409 -743 O ATOM 2397 N ILE A 318 11.750 -7.869 24.278 1.00 62.46 N ANISOU 2397 N ILE A 318 5900 10931 6900 330 -1370 -525 N ATOM 2398 CA ILE A 318 10.974 -7.534 23.068 1.00 62.55 C ANISOU 2398 CA ILE A 318 5951 10911 6905 357 -1379 -469 C ATOM 2399 C ILE A 318 9.937 -8.645 22.802 1.00 66.25 C ANISOU 2399 C ILE A 318 6352 11535 7286 426 -1277 -504 C ATOM 2400 O ILE A 318 8.800 -8.328 22.485 1.00 66.23 O ANISOU 2400 O ILE A 318 6367 11544 7252 520 -1305 -545 O ATOM 2401 CB ILE A 318 11.887 -7.253 21.835 1.00 65.76 C ANISOU 2401 CB ILE A 318 6368 11278 7339 221 -1376 -311 C ATOM 2402 CG1 ILE A 318 12.902 -6.130 22.144 1.00 66.91 C ANISOU 2402 CG1 ILE A 318 6579 11275 7570 115 -1488 -263 C ATOM 2403 CG2 ILE A 318 11.057 -6.875 20.604 1.00 66.43 C ANISOU 2403 CG2 ILE A 318 6491 11346 7403 252 -1394 -243 C ATOM 2404 CD1 ILE A 318 14.159 -6.212 21.393 1.00 72.31 C ANISOU 2404 CD1 ILE A 318 7214 12009 8252 -56 -1453 -118 C ATOM 2405 N ILE A 319 10.314 -9.927 22.994 1.00 62.49 N ANISOU 2405 N ILE A 319 5802 11169 6772 381 -1173 -494 N ATOM 2406 CA ILE A 319 9.424 -11.087 22.868 1.00 61.10 C ANISOU 2406 CA ILE A 319 5573 11120 6524 412 -1087 -525 C ATOM 2407 C ILE A 319 8.346 -10.999 23.966 1.00 66.58 C ANISOU 2407 C ILE A 319 6249 11882 7165 503 -1115 -633 C ATOM 2408 O ILE A 319 7.166 -11.099 23.641 1.00 66.75 O ANISOU 2408 O ILE A 319 6250 11987 7127 558 -1103 -671 O ATOM 2409 CB ILE A 319 10.229 -12.419 22.923 1.00 62.94 C ANISOU 2409 CB ILE A 319 5756 11407 6751 347 -1001 -489 C ATOM 2410 CG1 ILE A 319 10.926 -12.692 21.581 1.00 62.72 C ANISOU 2410 CG1 ILE A 319 5714 11384 6733 288 -956 -413 C ATOM 2411 CG2 ILE A 319 9.353 -13.614 23.358 1.00 62.99 C ANISOU 2411 CG2 ILE A 319 5728 11509 6696 362 -944 -530 C ATOM 2412 CD1 ILE A 319 12.080 -13.608 21.663 1.00 66.68 C ANISOU 2412 CD1 ILE A 319 6172 11915 7249 251 -904 -390 C ATOM 2413 N LEU A 320 8.749 -10.784 25.244 1.00 64.51 N ANISOU 2413 N LEU A 320 5982 11617 6911 517 -1152 -687 N ATOM 2414 CA LEU A 320 7.826 -10.637 26.379 1.00 65.61 C ANISOU 2414 CA LEU A 320 6084 11866 6978 605 -1181 -800 C ATOM 2415 C LEU A 320 6.831 -9.517 26.063 1.00 68.97 C ANISOU 2415 C LEU A 320 6542 12267 7396 728 -1261 -882 C ATOM 2416 O LEU A 320 5.617 -9.752 26.104 1.00 69.39 O ANISOU 2416 O LEU A 320 6538 12468 7360 798 -1242 -941 O ATOM 2417 CB LEU A 320 8.597 -10.373 27.700 1.00 66.80 C ANISOU 2417 CB LEU A 320 6227 12014 7138 603 -1224 -850 C ATOM 2418 CG LEU A 320 7.806 -9.839 28.917 1.00 73.76 C ANISOU 2418 CG LEU A 320 7069 13016 7941 712 -1280 -995 C ATOM 2419 CD1 LEU A 320 7.980 -10.742 30.129 1.00 74.47 C ANISOU 2419 CD1 LEU A 320 7079 13269 7948 670 -1233 -992 C ATOM 2420 CD2 LEU A 320 8.242 -8.418 29.279 1.00 78.01 C ANISOU 2420 CD2 LEU A 320 7678 13412 8549 781 -1406 -1094 C ATOM 2421 N GLY A 321 7.357 -8.355 25.669 1.00 64.38 N ANISOU 2421 N GLY A 321 6052 11502 6908 744 -1355 -870 N ATOM 2422 CA GLY A 321 6.555 -7.202 25.280 1.00 65.24 C ANISOU 2422 CA GLY A 321 6221 11530 7036 872 -1460 -931 C ATOM 2423 C GLY A 321 5.575 -7.518 24.163 1.00 68.16 C ANISOU 2423 C GLY A 321 6565 11979 7354 906 -1417 -885 C ATOM 2424 O GLY A 321 4.383 -7.239 24.295 1.00 68.53 O ANISOU 2424 O GLY A 321 6580 12122 7336 1046 -1453 -983 O ATOM 2425 N ALA A 322 6.074 -8.152 23.074 1.00 63.23 N ANISOU 2425 N ALA A 322 5938 11344 6743 783 -1340 -749 N ATOM 2426 CA ALA A 322 5.292 -8.554 21.904 1.00 62.60 C ANISOU 2426 CA ALA A 322 5827 11352 6607 789 -1292 -699 C ATOM 2427 C ALA A 322 4.199 -9.559 22.266 1.00 66.97 C ANISOU 2427 C ALA A 322 6274 12125 7046 817 -1214 -775 C ATOM 2428 O ALA A 322 3.129 -9.521 21.667 1.00 66.35 O ANISOU 2428 O ALA A 322 6159 12149 6902 884 -1217 -798 O ATOM 2429 CB ALA A 322 6.197 -9.148 20.840 1.00 62.30 C ANISOU 2429 CB ALA A 322 5790 11289 6592 648 -1220 -567 C ATOM 2430 N PHE A 323 4.467 -10.446 23.244 1.00 63.06 N ANISOU 2430 N PHE A 323 5728 11709 6522 754 -1152 -802 N ATOM 2431 CA PHE A 323 3.532 -11.472 23.685 1.00 62.69 C ANISOU 2431 CA PHE A 323 5585 11869 6367 734 -1083 -845 C ATOM 2432 C PHE A 323 2.363 -10.847 24.459 1.00 69.06 C ANISOU 2432 C PHE A 323 6328 12829 7083 874 -1138 -973 C ATOM 2433 O PHE A 323 1.202 -11.183 24.190 1.00 68.75 O ANISOU 2433 O PHE A 323 6206 12975 6942 898 -1110 -1006 O ATOM 2434 CB PHE A 323 4.270 -12.519 24.533 1.00 63.85 C ANISOU 2434 CB PHE A 323 5713 12030 6517 624 -1024 -809 C ATOM 2435 CG PHE A 323 3.381 -13.418 25.352 1.00 65.40 C ANISOU 2435 CG PHE A 323 5820 12430 6601 585 -979 -839 C ATOM 2436 CD1 PHE A 323 3.273 -13.249 26.728 1.00 68.42 C ANISOU 2436 CD1 PHE A 323 6153 12919 6924 618 -1004 -898 C ATOM 2437 CD2 PHE A 323 2.619 -14.410 24.744 1.00 67.23 C ANISOU 2437 CD2 PHE A 323 6009 12764 6773 500 -919 -807 C ATOM 2438 CE1 PHE A 323 2.426 -14.059 27.481 1.00 69.55 C ANISOU 2438 CE1 PHE A 323 6199 13285 6941 559 -964 -902 C ATOM 2439 CE2 PHE A 323 1.764 -15.217 25.501 1.00 70.39 C ANISOU 2439 CE2 PHE A 323 6323 13360 7061 429 -886 -814 C ATOM 2440 CZ PHE A 323 1.670 -15.034 26.864 1.00 68.62 C ANISOU 2440 CZ PHE A 323 6045 13258 6770 455 -907 -851 C ATOM 2441 N ILE A 324 2.665 -9.942 25.410 1.00 67.30 N ANISOU 2441 N ILE A 324 6132 12551 6888 969 -1217 -1057 N ATOM 2442 CA ILE A 324 1.634 -9.272 26.202 1.00 69.02 C ANISOU 2442 CA ILE A 324 6283 12928 7015 1135 -1280 -1212 C ATOM 2443 C ILE A 324 0.749 -8.422 25.280 1.00 75.28 C ANISOU 2443 C ILE A 324 7094 13705 7805 1284 -1350 -1252 C ATOM 2444 O ILE A 324 -0.464 -8.626 25.268 1.00 76.50 O ANISOU 2444 O ILE A 324 7136 14095 7834 1359 -1333 -1321 O ATOM 2445 CB ILE A 324 2.213 -8.422 27.373 1.00 73.13 C ANISOU 2445 CB ILE A 324 6841 13371 7574 1220 -1368 -1319 C ATOM 2446 CG1 ILE A 324 3.195 -9.215 28.306 1.00 73.01 C ANISOU 2446 CG1 ILE A 324 6809 13372 7560 1079 -1309 -1268 C ATOM 2447 CG2 ILE A 324 1.099 -7.700 28.153 1.00 75.39 C ANISOU 2447 CG2 ILE A 324 7047 13843 7753 1427 -1441 -1514 C ATOM 2448 CD1 ILE A 324 2.643 -10.490 29.072 1.00 79.68 C ANISOU 2448 CD1 ILE A 324 7521 14495 8261 986 -1210 -1244 C ATOM 2449 N VAL A 325 1.352 -7.520 24.477 1.00 71.74 N ANISOU 2449 N VAL A 325 6777 12998 7483 1311 -1430 -1192 N ATOM 2450 CA VAL A 325 0.621 -6.609 23.594 1.00 73.07 C ANISOU 2450 CA VAL A 325 6989 13111 7665 1460 -1521 -1205 C ATOM 2451 C VAL A 325 -0.244 -7.378 22.545 1.00 75.47 C ANISOU 2451 C VAL A 325 7205 13595 7874 1418 -1439 -1140 C ATOM 2452 O VAL A 325 -1.218 -6.815 22.054 1.00 76.55 O ANISOU 2452 O VAL A 325 7317 13806 7962 1572 -1501 -1187 O ATOM 2453 CB VAL A 325 1.573 -5.565 22.941 1.00 78.44 C ANISOU 2453 CB VAL A 325 7840 13462 8503 1447 -1628 -1110 C ATOM 2454 CG1 VAL A 325 2.367 -6.154 21.775 1.00 77.67 C ANISOU 2454 CG1 VAL A 325 7774 13291 8445 1256 -1549 -917 C ATOM 2455 CG2 VAL A 325 0.816 -4.314 22.504 1.00 80.25 C ANISOU 2455 CG2 VAL A 325 8143 13586 8762 1659 -1782 -1165 C ATOM 2456 N CYS A 326 0.069 -8.659 22.263 1.00 69.51 N ANISOU 2456 N CYS A 326 6401 12919 7089 1226 -1310 -1049 N ATOM 2457 CA CYS A 326 -0.674 -9.458 21.285 1.00 68.34 C ANISOU 2457 CA CYS A 326 6177 12933 6857 1161 -1236 -1001 C ATOM 2458 C CYS A 326 -1.808 -10.260 21.924 1.00 71.08 C ANISOU 2458 C CYS A 326 6370 13583 7052 1154 -1177 -1090 C ATOM 2459 O CYS A 326 -2.883 -10.325 21.342 1.00 72.31 O ANISOU 2459 O CYS A 326 6441 13921 7112 1206 -1175 -1119 O ATOM 2460 CB CYS A 326 0.262 -10.382 20.509 1.00 67.23 C ANISOU 2460 CB CYS A 326 6075 12703 6768 966 -1146 -875 C ATOM 2461 SG CYS A 326 1.236 -9.560 19.219 1.00 70.96 S ANISOU 2461 SG CYS A 326 6670 12943 7349 947 -1196 -740 S ATOM 2462 N TRP A 327 -1.561 -10.917 23.066 1.00 65.84 N ANISOU 2462 N TRP A 327 5663 12994 6360 1070 -1128 -1115 N ATOM 2463 CA TRP A 327 -2.532 -11.811 23.698 1.00 65.40 C ANISOU 2463 CA TRP A 327 5459 13236 6153 1002 -1065 -1160 C ATOM 2464 C TRP A 327 -3.289 -11.243 24.912 1.00 69.24 C ANISOU 2464 C TRP A 327 5836 13946 6525 1149 -1111 -1302 C ATOM 2465 O TRP A 327 -4.371 -11.756 25.206 1.00 69.97 O ANISOU 2465 O TRP A 327 5775 14351 6460 1126 -1075 -1347 O ATOM 2466 CB TRP A 327 -1.834 -13.099 24.138 1.00 63.49 C ANISOU 2466 CB TRP A 327 5233 12958 5932 787 -982 -1068 C ATOM 2467 CG TRP A 327 -1.427 -14.017 23.031 1.00 63.60 C ANISOU 2467 CG TRP A 327 5304 12856 6005 634 -923 -964 C ATOM 2468 CD1 TRP A 327 -0.159 -14.377 22.691 1.00 65.34 C ANISOU 2468 CD1 TRP A 327 5634 12843 6350 554 -901 -881 C ATOM 2469 CD2 TRP A 327 -2.302 -14.780 22.191 1.00 63.93 C ANISOU 2469 CD2 TRP A 327 5281 13041 5969 542 -879 -951 C ATOM 2470 NE1 TRP A 327 -0.187 -15.291 21.662 1.00 64.53 N ANISOU 2470 NE1 TRP A 327 5543 12723 6253 438 -849 -831 N ATOM 2471 CE2 TRP A 327 -1.492 -15.561 21.341 1.00 66.88 C ANISOU 2471 CE2 TRP A 327 5741 13238 6432 419 -837 -873 C ATOM 2472 CE3 TRP A 327 -3.701 -14.869 22.065 1.00 66.36 C ANISOU 2472 CE3 TRP A 327 5454 13630 6131 553 -875 -1010 C ATOM 2473 CZ2 TRP A 327 -2.030 -16.413 20.371 1.00 66.59 C ANISOU 2473 CZ2 TRP A 327 5676 13273 6352 308 -797 -862 C ATOM 2474 CZ3 TRP A 327 -4.231 -15.700 21.095 1.00 68.00 C ANISOU 2474 CZ3 TRP A 327 5628 13913 6294 426 -834 -983 C ATOM 2475 CH2 TRP A 327 -3.401 -16.448 20.250 1.00 67.76 C ANISOU 2475 CH2 TRP A 327 5702 13681 6364 306 -798 -915 C ATOM 2476 N LEU A 328 -2.733 -10.251 25.648 1.00 65.30 N ANISOU 2476 N LEU A 328 5401 13318 6091 1286 -1190 -1381 N ATOM 2477 CA LEU A 328 -3.437 -9.684 26.804 1.00 66.51 C ANISOU 2477 CA LEU A 328 5443 13701 6125 1450 -1240 -1548 C ATOM 2478 C LEU A 328 -4.816 -9.130 26.391 1.00 74.01 C ANISOU 2478 C LEU A 328 6280 14882 6959 1642 -1288 -1665 C ATOM 2479 O LEU A 328 -5.774 -9.459 27.096 1.00 75.50 O ANISOU 2479 O LEU A 328 6286 15435 6965 1665 -1257 -1753 O ATOM 2480 CB LEU A 328 -2.624 -8.613 27.554 1.00 66.62 C ANISOU 2480 CB LEU A 328 5561 13511 6240 1586 -1340 -1641 C ATOM 2481 CG LEU A 328 -3.234 -8.056 28.855 1.00 72.30 C ANISOU 2481 CG LEU A 328 6163 14477 6830 1764 -1395 -1844 C ATOM 2482 CD1 LEU A 328 -3.169 -9.071 29.989 1.00 72.24 C ANISOU 2482 CD1 LEU A 328 6028 14730 6688 1602 -1301 -1817 C ATOM 2483 CD2 LEU A 328 -2.546 -6.772 29.272 1.00 74.08 C ANISOU 2483 CD2 LEU A 328 6522 14443 7181 1934 -1529 -1964 C ATOM 2484 N PRO A 329 -4.996 -8.370 25.265 1.00 70.30 N ANISOU 2484 N PRO A 329 5893 14251 6567 1772 -1361 -1655 N ATOM 2485 CA PRO A 329 -6.353 -7.897 24.936 1.00 71.39 C ANISOU 2485 CA PRO A 329 5904 14643 6578 1973 -1411 -1769 C ATOM 2486 C PRO A 329 -7.329 -9.055 24.729 1.00 75.04 C ANISOU 2486 C PRO A 329 6179 15469 6865 1817 -1300 -1731 C ATOM 2487 O PRO A 329 -8.406 -9.023 25.326 1.00 76.33 O ANISOU 2487 O PRO A 329 6152 16003 6848 1920 -1301 -1859 O ATOM 2488 CB PRO A 329 -6.151 -7.075 23.660 1.00 73.31 C ANISOU 2488 CB PRO A 329 6297 14605 6954 2080 -1501 -1703 C ATOM 2489 CG PRO A 329 -4.702 -6.683 23.682 1.00 76.87 C ANISOU 2489 CG PRO A 329 6952 14655 7600 2001 -1536 -1613 C ATOM 2490 CD PRO A 329 -4.009 -7.858 24.285 1.00 70.74 C ANISOU 2490 CD PRO A 329 6144 13921 6811 1749 -1409 -1537 C ATOM 2491 N PHE A 330 -6.928 -10.112 23.980 1.00 69.98 N ANISOU 2491 N PHE A 330 5583 14740 6269 1560 -1206 -1566 N ATOM 2492 CA PHE A 330 -7.794 -11.264 23.722 1.00 70.14 C ANISOU 2492 CA PHE A 330 5450 15058 6142 1375 -1112 -1522 C ATOM 2493 C PHE A 330 -8.275 -11.933 25.015 1.00 74.54 C ANISOU 2493 C PHE A 330 5844 15939 6538 1271 -1057 -1565 C ATOM 2494 O PHE A 330 -9.480 -12.083 25.202 1.00 74.87 O ANISOU 2494 O PHE A 330 5687 16369 6391 1295 -1044 -1638 O ATOM 2495 CB PHE A 330 -7.124 -12.311 22.809 1.00 70.71 C ANISOU 2495 CB PHE A 330 5625 14933 6310 1119 -1036 -1360 C ATOM 2496 CG PHE A 330 -8.007 -13.524 22.573 1.00 72.98 C ANISOU 2496 CG PHE A 330 5774 15497 6459 907 -956 -1323 C ATOM 2497 CD1 PHE A 330 -9.021 -13.494 21.622 1.00 76.49 C ANISOU 2497 CD1 PHE A 330 6118 16140 6806 942 -964 -1352 C ATOM 2498 CD2 PHE A 330 -7.844 -14.683 23.327 1.00 75.43 C ANISOU 2498 CD2 PHE A 330 6054 15874 6731 667 -887 -1257 C ATOM 2499 CE1 PHE A 330 -9.857 -14.600 21.433 1.00 78.17 C ANISOU 2499 CE1 PHE A 330 6197 16617 6886 725 -900 -1326 C ATOM 2500 CE2 PHE A 330 -8.687 -15.785 23.140 1.00 78.71 C ANISOU 2500 CE2 PHE A 330 6353 16530 7023 447 -832 -1217 C ATOM 2501 CZ PHE A 330 -9.677 -15.739 22.186 1.00 77.46 C ANISOU 2501 CZ PHE A 330 6093 16567 6771 469 -837 -1257 C ATOM 2502 N PHE A 331 -7.343 -12.353 25.884 1.00 71.25 N ANISOU 2502 N PHE A 331 5498 15390 6182 1147 -1025 -1509 N ATOM 2503 CA PHE A 331 -7.687 -13.060 27.117 1.00 71.83 C ANISOU 2503 CA PHE A 331 5429 15761 6102 1014 -973 -1510 C ATOM 2504 C PHE A 331 -8.383 -12.166 28.157 1.00 80.73 C ANISOU 2504 C PHE A 331 6400 17197 7076 1247 -1027 -1697 C ATOM 2505 O PHE A 331 -9.095 -12.698 29.012 1.00 81.78 O ANISOU 2505 O PHE A 331 6346 17716 7012 1154 -983 -1715 O ATOM 2506 CB PHE A 331 -6.461 -13.770 27.698 1.00 71.18 C ANISOU 2506 CB PHE A 331 5473 15442 6130 826 -934 -1382 C ATOM 2507 CG PHE A 331 -6.129 -14.998 26.879 1.00 70.11 C ANISOU 2507 CG PHE A 331 5422 15144 6072 569 -870 -1217 C ATOM 2508 CD1 PHE A 331 -6.858 -16.173 27.029 1.00 72.67 C ANISOU 2508 CD1 PHE A 331 5638 15703 6269 332 -813 -1137 C ATOM 2509 CD2 PHE A 331 -5.132 -14.963 25.917 1.00 69.20 C ANISOU 2509 CD2 PHE A 331 5489 14654 6149 563 -876 -1151 C ATOM 2510 CE1 PHE A 331 -6.565 -17.298 26.263 1.00 71.92 C ANISOU 2510 CE1 PHE A 331 5638 15430 6259 108 -773 -1011 C ATOM 2511 CE2 PHE A 331 -4.823 -16.099 25.171 1.00 70.37 C ANISOU 2511 CE2 PHE A 331 5710 14664 6363 353 -825 -1033 C ATOM 2512 CZ PHE A 331 -5.547 -17.254 25.341 1.00 68.87 C ANISOU 2512 CZ PHE A 331 5432 14672 6064 135 -780 -972 C ATOM 2513 N ILE A 332 -8.254 -10.828 28.045 1.00 80.00 N ANISOU 2513 N ILE A 332 6377 16959 7061 1546 -1130 -1840 N ATOM 2514 CA ILE A 332 -8.967 -9.907 28.934 1.00 82.94 C ANISOU 2514 CA ILE A 332 6606 17616 7293 1815 -1201 -2060 C ATOM 2515 C ILE A 332 -10.436 -9.886 28.495 1.00 90.09 C ANISOU 2515 C ILE A 332 7301 18920 8009 1912 -1199 -2143 C ATOM 2516 O ILE A 332 -11.317 -10.062 29.335 1.00 92.13 O ANISOU 2516 O ILE A 332 7326 19642 8039 1935 -1173 -2243 O ATOM 2517 CB ILE A 332 -8.311 -8.488 28.984 1.00 86.30 C ANISOU 2517 CB ILE A 332 7202 17705 7883 2100 -1335 -2192 C ATOM 2518 CG1 ILE A 332 -7.098 -8.441 29.963 1.00 85.57 C ANISOU 2518 CG1 ILE A 332 7219 17412 7883 2031 -1340 -2183 C ATOM 2519 CG2 ILE A 332 -9.325 -7.340 29.238 1.00 89.31 C ANISOU 2519 CG2 ILE A 332 7466 18311 8155 2467 -1448 -2443 C ATOM 2520 CD1 ILE A 332 -7.348 -8.831 31.456 1.00 93.40 C ANISOU 2520 CD1 ILE A 332 8027 18788 8674 1991 -1296 -2266 C ATOM 2521 N ILE A 333 -10.684 -9.728 27.181 1.00 87.05 N ANISOU 2521 N ILE A 333 6983 18389 7703 1950 -1222 -2090 N ATOM 2522 CA ILE A 333 -12.025 -9.695 26.583 1.00 88.96 C ANISOU 2522 CA ILE A 333 7035 18987 7780 2043 -1227 -2156 C ATOM 2523 C ILE A 333 -12.691 -11.069 26.751 1.00 93.62 C ANISOU 2523 C ILE A 333 7435 19952 8186 1720 -1104 -2052 C ATOM 2524 O ILE A 333 -13.875 -11.131 27.052 1.00 94.36 O ANISOU 2524 O ILE A 333 7276 20528 8050 1770 -1093 -2150 O ATOM 2525 CB ILE A 333 -11.955 -9.215 25.095 1.00 91.70 C ANISOU 2525 CB ILE A 333 7524 19047 8269 2141 -1287 -2096 C ATOM 2526 CG1 ILE A 333 -11.419 -7.755 24.980 1.00 93.02 C ANISOU 2526 CG1 ILE A 333 7876 18863 8606 2464 -1435 -2193 C ATOM 2527 CG2 ILE A 333 -13.278 -9.373 24.340 1.00 93.49 C ANISOU 2527 CG2 ILE A 333 7556 19640 8326 2185 -1280 -2129 C ATOM 2528 CD1 ILE A 333 -12.080 -6.611 25.920 1.00104.46 C ANISOU 2528 CD1 ILE A 333 9217 20517 9955 2840 -1553 -2458 C ATOM 2529 N SER A 334 -11.910 -12.150 26.634 1.00 90.29 N ANISOU 2529 N SER A 334 7132 19314 7862 1393 -1023 -1862 N ATOM 2530 CA SER A 334 -12.357 -13.533 26.778 1.00 90.95 C ANISOU 2530 CA SER A 334 7094 19645 7816 1044 -925 -1733 C ATOM 2531 C SER A 334 -12.943 -13.796 28.164 1.00 97.46 C ANISOU 2531 C SER A 334 7697 20923 8411 987 -893 -1784 C ATOM 2532 O SER A 334 -13.830 -14.634 28.284 1.00 99.26 O ANISOU 2532 O SER A 334 7736 21526 8452 766 -836 -1727 O ATOM 2533 CB SER A 334 -11.198 -14.488 26.511 1.00 93.57 C ANISOU 2533 CB SER A 334 7641 19575 8335 769 -874 -1542 C ATOM 2534 OG SER A 334 -11.626 -15.833 26.399 1.00104.29 O ANISOU 2534 OG SER A 334 8931 21086 9610 431 -804 -1410 O ATOM 2535 N LEU A 335 -12.475 -13.071 29.196 1.00 94.59 N ANISOU 2535 N LEU A 335 7343 20548 8048 1176 -934 -1894 N ATOM 2536 CA LEU A 335 -12.966 -13.207 30.572 1.00 96.40 C ANISOU 2536 CA LEU A 335 7352 21235 8042 1155 -910 -1962 C ATOM 2537 C LEU A 335 -14.106 -12.246 30.894 1.00103.95 C ANISOU 2537 C LEU A 335 8065 22645 8788 1478 -964 -2210 C ATOM 2538 O LEU A 335 -14.966 -12.599 31.697 1.00105.47 O ANISOU 2538 O LEU A 335 7986 23379 8709 1406 -922 -2251 O ATOM 2539 CB LEU A 335 -11.837 -12.982 31.587 1.00 95.69 C ANISOU 2539 CB LEU A 335 7387 20929 8042 1184 -926 -1963 C ATOM 2540 CG LEU A 335 -11.054 -14.201 32.056 1.00 99.06 C ANISOU 2540 CG LEU A 335 7907 21213 8519 828 -856 -1730 C ATOM 2541 CD1 LEU A 335 -10.002 -13.789 33.036 1.00 98.58 C ANISOU 2541 CD1 LEU A 335 7952 20967 8537 915 -887 -1764 C ATOM 2542 CD2 LEU A 335 -11.953 -15.227 32.729 1.00103.65 C ANISOU 2542 CD2 LEU A 335 8252 22293 8838 548 -786 -1627 C ATOM 2543 N VAL A 336 -14.101 -11.033 30.312 1.00102.70 N ANISOU 2543 N VAL A 336 7998 22277 8745 1837 -1065 -2373 N ATOM 2544 CA VAL A 336 -15.142 -10.026 30.561 1.00106.49 C ANISOU 2544 CA VAL A 336 8270 23140 9050 2206 -1142 -2634 C ATOM 2545 C VAL A 336 -16.379 -10.261 29.664 1.00115.01 C ANISOU 2545 C VAL A 336 9159 24558 9981 2199 -1124 -2636 C ATOM 2546 O VAL A 336 -17.436 -9.715 29.961 1.00116.56 O ANISOU 2546 O VAL A 336 9105 25222 9960 2444 -1163 -2834 O ATOM 2547 CB VAL A 336 -14.637 -8.555 30.452 1.00110.52 C ANISOU 2547 CB VAL A 336 8967 23280 9745 2619 -1287 -2824 C ATOM 2548 CG1 VAL A 336 -13.448 -8.300 31.376 1.00109.34 C ANISOU 2548 CG1 VAL A 336 8982 22840 9722 2618 -1310 -2843 C ATOM 2549 CG2 VAL A 336 -14.312 -8.154 29.015 1.00108.88 C ANISOU 2549 CG2 VAL A 336 8991 22605 9775 2684 -1346 -2734 C ATOM 2550 N MET A 337 -16.234 -11.049 28.572 1.00114.16 N ANISOU 2550 N MET A 337 9162 24230 9984 1935 -1072 -2433 N ATOM 2551 CA MET A 337 -17.296 -11.385 27.613 1.00117.00 C ANISOU 2551 CA MET A 337 9364 24869 10222 1877 -1053 -2410 C ATOM 2552 C MET A 337 -18.445 -12.154 28.318 1.00126.49 C ANISOU 2552 C MET A 337 10213 26753 11092 1679 -975 -2420 C ATOM 2553 O MET A 337 -19.589 -11.720 28.143 1.00128.55 O ANISOU 2553 O MET A 337 10229 27460 11154 1880 -1007 -2570 O ATOM 2554 CB MET A 337 -16.722 -12.146 26.390 1.00117.46 C ANISOU 2554 CB MET A 337 9636 24517 10476 1604 -1012 -2195 C ATOM 2555 CG MET A 337 -17.561 -13.295 25.866 1.00122.28 C ANISOU 2555 CG MET A 337 10083 25441 10936 1269 -932 -2079 C ATOM 2556 SD MET A 337 -16.608 -14.835 25.898 1.00124.96 S ANISOU 2556 SD MET A 337 10611 25455 11413 765 -838 -1816 S ATOM 2557 CE MET A 337 -17.905 -16.001 25.482 1.00123.51 C ANISOU 2557 CE MET A 337 10181 25745 11000 414 -777 -1738 C ATOM 2558 N PRO A 338 -18.211 -13.218 29.149 1.00125.11 N ANISOU 2558 N PRO A 338 9992 26708 10836 1311 -885 -2269 N ATOM 2559 CA PRO A 338 -19.350 -13.866 29.829 1.00128.24 C ANISOU 2559 CA PRO A 338 10037 27791 10896 1116 -822 -2267 C ATOM 2560 C PRO A 338 -20.132 -12.881 30.720 1.00136.05 C ANISOU 2560 C PRO A 338 10748 29305 11639 1484 -867 -2537 C ATOM 2561 O PRO A 338 -21.360 -12.822 30.607 1.00138.92 O ANISOU 2561 O PRO A 338 10805 30232 11747 1545 -862 -2638 O ATOM 2562 CB PRO A 338 -18.686 -14.982 30.650 1.00129.31 C ANISOU 2562 CB PRO A 338 10245 27847 11041 707 -747 -2047 C ATOM 2563 CG PRO A 338 -17.385 -15.247 29.952 1.00130.27 C ANISOU 2563 CG PRO A 338 10745 27242 11509 610 -755 -1899 C ATOM 2564 CD PRO A 338 -16.942 -13.895 29.498 1.00124.61 C ANISOU 2564 CD PRO A 338 10179 26199 10967 1050 -844 -2080 C ATOM 2565 N ILE A 339 -19.411 -12.066 31.543 1.00131.96 N ANISOU 2565 N ILE A 339 10336 28599 11203 1750 -921 -2673 N ATOM 2566 CA ILE A 339 -19.953 -11.036 32.452 1.00144.77 C ANISOU 2566 CA ILE A 339 11743 30633 12630 2150 -983 -2968 C ATOM 2567 C ILE A 339 -20.718 -9.973 31.641 1.00175.90 C ANISOU 2567 C ILE A 339 15622 34645 16569 2584 -1088 -3191 C ATOM 2568 O ILE A 339 -21.944 -10.011 31.568 1.00141.70 O ANISOU 2568 O ILE A 339 10970 30901 11969 2652 -1077 -3292 O ATOM 2569 CB ILE A 339 -18.814 -10.382 33.301 1.00146.51 C ANISOU 2569 CB ILE A 339 12171 30486 13010 2325 -1036 -3056 C ATOM 2570 CG1 ILE A 339 -17.997 -11.433 34.087 1.00145.19 C ANISOU 2570 CG1 ILE A 339 12078 30234 12854 1910 -942 -2820 C ATOM 2571 CG2 ILE A 339 -19.360 -9.288 34.232 1.00150.06 C ANISOU 2571 CG2 ILE A 339 12410 31342 13265 2763 -1117 -3399 C ATOM 2572 CD1 ILE A 339 -16.537 -11.057 34.320 1.00148.62 C ANISOU 2572 CD1 ILE A 339 12845 30047 13578 1965 -987 -2791 C ATOM 2573 N TRP A 345 -20.425 -2.900 26.611 1.00144.16 N ANISOU 2573 N TRP A 345 12718 28371 13685 5010 -2047 -3860 N ATOM 2574 CA TRP A 345 -19.239 -3.189 25.804 1.00140.75 C ANISOU 2574 CA TRP A 345 12623 27316 13539 4713 -2016 -3577 C ATOM 2575 C TRP A 345 -19.550 -3.134 24.294 1.00143.57 C ANISOU 2575 C TRP A 345 13052 27532 13967 4723 -2056 -3419 C ATOM 2576 O TRP A 345 -20.710 -3.266 23.891 1.00144.97 O ANISOU 2576 O TRP A 345 12976 28171 13937 4831 -2054 -3480 O ATOM 2577 CB TRP A 345 -18.639 -4.555 26.182 1.00136.87 C ANISOU 2577 CB TRP A 345 12107 26878 13018 4192 -1816 -3374 C ATOM 2578 N PHE A 346 -18.494 -2.951 23.469 1.00137.30 N ANISOU 2578 N PHE A 346 12591 26128 13451 4601 -2092 -3213 N ATOM 2579 CA PHE A 346 -18.536 -2.831 22.002 1.00136.17 C ANISOU 2579 CA PHE A 346 12566 25769 13403 4592 -2138 -3034 C ATOM 2580 C PHE A 346 -18.973 -4.145 21.287 1.00134.74 C ANISOU 2580 C PHE A 346 12213 25903 13078 4213 -1968 -2862 C ATOM 2581 O PHE A 346 -19.304 -5.137 21.950 1.00134.04 O ANISOU 2581 O PHE A 346 11920 26189 12821 3952 -1822 -2873 O ATOM 2582 CB PHE A 346 -17.164 -2.359 21.471 1.00136.61 C ANISOU 2582 CB PHE A 346 13007 25123 13775 4517 -2208 -2856 C ATOM 2583 CG PHE A 346 -16.902 -0.877 21.627 1.00140.58 C ANISOU 2583 CG PHE A 346 13719 25248 14447 4923 -2434 -2982 C ATOM 2584 CD1 PHE A 346 -16.259 -0.382 22.757 1.00144.08 C ANISOU 2584 CD1 PHE A 346 14271 25486 14985 5015 -2489 -3129 C ATOM 2585 CD2 PHE A 346 -17.296 0.023 20.642 1.00144.86 C ANISOU 2585 CD2 PHE A 346 14359 25628 15054 5209 -2604 -2952 C ATOM 2586 CE1 PHE A 346 -16.023 0.989 22.904 1.00147.18 C ANISOU 2586 CE1 PHE A 346 14875 25500 15546 5382 -2717 -3259 C ATOM 2587 CE2 PHE A 346 -17.058 1.394 20.790 1.00149.93 C ANISOU 2587 CE2 PHE A 346 15220 25879 15869 5578 -2836 -3060 C ATOM 2588 CZ PHE A 346 -16.422 1.867 21.919 1.00148.29 C ANISOU 2588 CZ PHE A 346 15127 25451 15765 5659 -2894 -3220 C ATOM 2589 N HIS A 347 -18.984 -4.132 19.931 1.00127.08 N ANISOU 2589 N HIS A 347 11332 24781 12172 4181 -1998 -2702 N ATOM 2590 CA HIS A 347 -19.424 -5.270 19.126 1.00124.28 C ANISOU 2590 CA HIS A 347 10830 24701 11690 3858 -1865 -2563 C ATOM 2591 C HIS A 347 -18.325 -6.339 18.909 1.00119.50 C ANISOU 2591 C HIS A 347 10383 23809 11213 3392 -1718 -2355 C ATOM 2592 O HIS A 347 -17.216 -6.221 19.422 1.00116.74 O ANISOU 2592 O HIS A 347 10228 23098 11031 3308 -1704 -2317 O ATOM 2593 CB HIS A 347 -20.054 -4.824 17.778 1.00126.54 C ANISOU 2593 CB HIS A 347 11107 25022 11951 4030 -1959 -2500 C ATOM 2594 CG HIS A 347 -19.222 -3.933 16.898 1.00129.61 C ANISOU 2594 CG HIS A 347 11815 24846 12584 4162 -2088 -2359 C ATOM 2595 ND1 HIS A 347 -19.734 -3.431 15.708 1.00132.64 N ANISOU 2595 ND1 HIS A 347 12208 25242 12949 4339 -2192 -2284 N ATOM 2596 CD2 HIS A 347 -17.953 -3.482 17.048 1.00130.00 C ANISOU 2596 CD2 HIS A 347 12166 24346 12882 4125 -2130 -2271 C ATOM 2597 CE1 HIS A 347 -18.768 -2.697 15.180 1.00131.48 C ANISOU 2597 CE1 HIS A 347 12370 24552 13036 4392 -2294 -2141 C ATOM 2598 NE2 HIS A 347 -17.677 -2.698 15.949 1.00130.29 N ANISOU 2598 NE2 HIS A 347 12400 24051 13052 4262 -2261 -2131 N ATOM 2599 N LEU A 348 -18.698 -7.412 18.181 1.00112.37 N ANISOU 2599 N LEU A 348 9376 23107 10214 3100 -1614 -2241 N ATOM 2600 CA LEU A 348 -17.947 -8.622 17.829 1.00107.97 C ANISOU 2600 CA LEU A 348 8916 22376 9733 2663 -1477 -2070 C ATOM 2601 C LEU A 348 -16.714 -8.360 16.939 1.00105.18 C ANISOU 2601 C LEU A 348 8870 21466 9625 2610 -1506 -1904 C ATOM 2602 O LEU A 348 -15.922 -9.282 16.728 1.00102.15 O ANISOU 2602 O LEU A 348 8593 20890 9329 2288 -1404 -1782 O ATOM 2603 CB LEU A 348 -18.910 -9.588 17.101 1.00108.64 C ANISOU 2603 CB LEU A 348 8784 22869 9626 2436 -1399 -2039 C ATOM 2604 CG LEU A 348 -19.617 -10.677 17.926 1.00114.03 C ANISOU 2604 CG LEU A 348 9219 23999 10107 2166 -1286 -2089 C ATOM 2605 CD1 LEU A 348 -20.525 -10.101 18.998 1.00116.94 C ANISOU 2605 CD1 LEU A 348 9349 24794 10289 2425 -1328 -2277 C ATOM 2606 CD2 LEU A 348 -20.436 -11.579 17.033 1.00116.10 C ANISOU 2606 CD2 LEU A 348 9310 24588 10215 1919 -1228 -2044 C ATOM 2607 N ALA A 349 -16.558 -7.125 16.418 1.00 99.59 N ANISOU 2607 N ALA A 349 8303 20512 9024 2921 -1650 -1897 N ATOM 2608 CA ALA A 349 -15.427 -6.711 15.587 1.00 96.77 C ANISOU 2608 CA ALA A 349 8225 19661 8882 2885 -1695 -1729 C ATOM 2609 C ALA A 349 -14.143 -6.628 16.407 1.00 97.64 C ANISOU 2609 C ALA A 349 8535 19386 9180 2788 -1674 -1700 C ATOM 2610 O ALA A 349 -13.063 -6.922 15.889 1.00 95.71 O ANISOU 2610 O ALA A 349 8467 18820 9078 2586 -1630 -1546 O ATOM 2611 CB ALA A 349 -15.716 -5.369 14.940 1.00 99.22 C ANISOU 2611 CB ALA A 349 8623 19834 9242 3243 -1876 -1723 C ATOM 2612 N ILE A 350 -14.268 -6.245 17.690 1.00 93.67 N ANISOU 2612 N ILE A 350 7985 18945 8660 2933 -1703 -1855 N ATOM 2613 CA ILE A 350 -13.145 -6.117 18.603 1.00 92.08 C ANISOU 2613 CA ILE A 350 7948 18425 8613 2860 -1692 -1850 C ATOM 2614 C ILE A 350 -12.668 -7.528 19.015 1.00 93.27 C ANISOU 2614 C ILE A 350 8053 18646 8738 2478 -1519 -1777 C ATOM 2615 O ILE A 350 -11.500 -7.674 19.383 1.00 90.76 O ANISOU 2615 O ILE A 350 7901 18011 8571 2335 -1486 -1701 O ATOM 2616 CB ILE A 350 -13.456 -5.174 19.811 1.00 97.09 C ANISOU 2616 CB ILE A 350 8553 19104 9234 3163 -1797 -2058 C ATOM 2617 CG1 ILE A 350 -13.641 -5.915 21.160 1.00 97.52 C ANISOU 2617 CG1 ILE A 350 8457 19423 9175 3025 -1688 -2162 C ATOM 2618 CG2 ILE A 350 -14.604 -4.196 19.505 1.00 99.50 C ANISOU 2618 CG2 ILE A 350 8740 19637 9429 3547 -1936 -2203 C ATOM 2619 CD1 ILE A 350 -13.061 -5.190 22.373 1.00105.44 C ANISOU 2619 CD1 ILE A 350 9519 20307 10234 3236 -1775 -2326 C ATOM 2620 N PHE A 351 -13.554 -8.560 18.935 1.00 89.68 N ANISOU 2620 N PHE A 351 7382 18594 8097 2308 -1419 -1794 N ATOM 2621 CA PHE A 351 -13.157 -9.938 19.247 1.00 87.77 C ANISOU 2621 CA PHE A 351 7121 18385 7842 1940 -1278 -1710 C ATOM 2622 C PHE A 351 -12.369 -10.487 18.074 1.00 89.17 C ANISOU 2622 C PHE A 351 7455 18282 8144 1737 -1234 -1549 C ATOM 2623 O PHE A 351 -11.299 -11.074 18.275 1.00 86.99 O ANISOU 2623 O PHE A 351 7315 17744 7993 1538 -1172 -1461 O ATOM 2624 CB PHE A 351 -14.348 -10.848 19.596 1.00 90.79 C ANISOU 2624 CB PHE A 351 7236 19268 7993 1791 -1200 -1768 C ATOM 2625 CG PHE A 351 -14.209 -11.587 20.912 1.00 92.57 C ANISOU 2625 CG PHE A 351 7389 19625 8158 1608 -1124 -1785 C ATOM 2626 CD1 PHE A 351 -13.037 -12.278 21.226 1.00 94.26 C ANISOU 2626 CD1 PHE A 351 7772 19524 8518 1372 -1061 -1669 C ATOM 2627 CD2 PHE A 351 -15.247 -11.595 21.837 1.00 96.48 C ANISOU 2627 CD2 PHE A 351 7635 20587 8436 1674 -1118 -1911 C ATOM 2628 CE1 PHE A 351 -12.902 -12.941 22.453 1.00 95.09 C ANISOU 2628 CE1 PHE A 351 7816 19751 8563 1208 -1002 -1664 C ATOM 2629 CE2 PHE A 351 -15.115 -12.268 23.058 1.00 99.52 C ANISOU 2629 CE2 PHE A 351 7947 21120 8748 1491 -1050 -1904 C ATOM 2630 CZ PHE A 351 -13.939 -12.926 23.362 1.00 95.94 C ANISOU 2630 CZ PHE A 351 7680 20322 8450 1260 -996 -1773 C ATOM 2631 N ASP A 352 -12.863 -10.219 16.841 1.00 85.06 N ANISOU 2631 N ASP A 352 6913 17819 7586 1817 -1276 -1515 N ATOM 2632 CA ASP A 352 -12.213 -10.594 15.587 1.00 83.33 C ANISOU 2632 CA ASP A 352 6819 17386 7455 1667 -1248 -1378 C ATOM 2633 C ASP A 352 -10.826 -9.941 15.481 1.00 85.02 C ANISOU 2633 C ASP A 352 7276 17146 7880 1707 -1290 -1282 C ATOM 2634 O ASP A 352 -9.877 -10.601 15.053 1.00 83.89 O ANISOU 2634 O ASP A 352 7241 16803 7829 1496 -1221 -1184 O ATOM 2635 CB ASP A 352 -13.084 -10.189 14.382 1.00 86.82 C ANISOU 2635 CB ASP A 352 7178 18015 7794 1797 -1307 -1369 C ATOM 2636 CG ASP A 352 -14.242 -11.131 14.059 1.00100.49 C ANISOU 2636 CG ASP A 352 8684 20171 9326 1647 -1242 -1424 C ATOM 2637 OD1 ASP A 352 -13.993 -12.350 13.897 1.00101.38 O ANISOU 2637 OD1 ASP A 352 8795 20289 9436 1342 -1140 -1386 O ATOM 2638 OD2 ASP A 352 -15.381 -10.635 13.869 1.00105.69 O ANISOU 2638 OD2 ASP A 352 9174 21149 9835 1838 -1303 -1502 O ATOM 2639 N PHE A 353 -10.701 -8.662 15.905 1.00 80.31 N ANISOU 2639 N PHE A 353 6762 16395 7357 1975 -1410 -1319 N ATOM 2640 CA PHE A 353 -9.441 -7.921 15.848 1.00 78.26 C ANISOU 2640 CA PHE A 353 6728 15714 7292 2007 -1471 -1226 C ATOM 2641 C PHE A 353 -8.418 -8.484 16.824 1.00 78.21 C ANISOU 2641 C PHE A 353 6794 15542 7381 1834 -1395 -1224 C ATOM 2642 O PHE A 353 -7.258 -8.668 16.455 1.00 76.29 O ANISOU 2642 O PHE A 353 6691 15032 7263 1689 -1364 -1107 O ATOM 2643 CB PHE A 353 -9.662 -6.420 16.105 1.00 81.89 C ANISOU 2643 CB PHE A 353 7266 16040 7810 2333 -1641 -1282 C ATOM 2644 CG PHE A 353 -8.381 -5.622 16.188 1.00 83.27 C ANISOU 2644 CG PHE A 353 7674 15778 8186 2342 -1718 -1190 C ATOM 2645 CD1 PHE A 353 -7.513 -5.551 15.103 1.00 86.00 C ANISOU 2645 CD1 PHE A 353 8156 15894 8625 2210 -1719 -1001 C ATOM 2646 CD2 PHE A 353 -8.040 -4.947 17.352 1.00 85.95 C ANISOU 2646 CD2 PHE A 353 8086 15961 8610 2471 -1791 -1298 C ATOM 2647 CE1 PHE A 353 -6.306 -4.849 15.197 1.00 86.85 C ANISOU 2647 CE1 PHE A 353 8463 15628 8907 2181 -1788 -904 C ATOM 2648 CE2 PHE A 353 -6.841 -4.233 17.441 1.00 88.84 C ANISOU 2648 CE2 PHE A 353 8664 15929 9161 2449 -1868 -1213 C ATOM 2649 CZ PHE A 353 -5.980 -4.191 16.363 1.00 86.38 C ANISOU 2649 CZ PHE A 353 8481 15398 8941 2294 -1864 -1009 C ATOM 2650 N PHE A 354 -8.851 -8.770 18.056 1.00 73.59 N ANISOU 2650 N PHE A 354 6096 15146 6718 1847 -1364 -1348 N ATOM 2651 CA PHE A 354 -7.994 -9.295 19.106 1.00 70.85 C ANISOU 2651 CA PHE A 354 5799 14685 6438 1699 -1300 -1349 C ATOM 2652 C PHE A 354 -7.599 -10.761 18.864 1.00 73.94 C ANISOU 2652 C PHE A 354 6175 15098 6820 1388 -1167 -1258 C ATOM 2653 O PHE A 354 -6.510 -11.136 19.285 1.00 73.79 O ANISOU 2653 O PHE A 354 6263 14862 6912 1261 -1128 -1199 O ATOM 2654 CB PHE A 354 -8.629 -9.093 20.481 1.00 73.15 C ANISOU 2654 CB PHE A 354 5962 15204 6626 1819 -1317 -1505 C ATOM 2655 CG PHE A 354 -8.653 -7.648 20.947 1.00 76.37 C ANISOU 2655 CG PHE A 354 6436 15491 7090 2130 -1462 -1620 C ATOM 2656 CD1 PHE A 354 -7.799 -6.698 20.385 1.00 79.59 C ANISOU 2656 CD1 PHE A 354 7051 15513 7675 2221 -1563 -1546 C ATOM 2657 CD2 PHE A 354 -9.477 -7.250 21.993 1.00 80.32 C ANISOU 2657 CD2 PHE A 354 6792 16261 7465 2322 -1503 -1804 C ATOM 2658 CE1 PHE A 354 -7.807 -5.369 20.830 1.00 81.92 C ANISOU 2658 CE1 PHE A 354 7432 15653 8040 2499 -1718 -1655 C ATOM 2659 CE2 PHE A 354 -9.474 -5.923 22.447 1.00 84.40 C ANISOU 2659 CE2 PHE A 354 7382 16641 8043 2627 -1653 -1939 C ATOM 2660 CZ PHE A 354 -8.650 -4.990 21.851 1.00 82.41 C ANISOU 2660 CZ PHE A 354 7361 15964 7988 2714 -1766 -1864 C ATOM 2661 N THR A 355 -8.418 -11.572 18.155 1.00 70.41 N ANISOU 2661 N THR A 355 5609 14887 6255 1270 -1110 -1248 N ATOM 2662 CA THR A 355 -8.013 -12.953 17.825 1.00 68.21 C ANISOU 2662 CA THR A 355 5348 14578 5991 983 -1007 -1173 C ATOM 2663 C THR A 355 -6.848 -12.897 16.844 1.00 70.47 C ANISOU 2663 C THR A 355 5799 14555 6420 935 -1004 -1068 C ATOM 2664 O THR A 355 -5.855 -13.609 17.013 1.00 68.61 O ANISOU 2664 O THR A 355 5654 14137 6279 780 -949 -1014 O ATOM 2665 CB THR A 355 -9.161 -13.778 17.203 1.00 67.45 C ANISOU 2665 CB THR A 355 5097 14790 5740 858 -963 -1199 C ATOM 2666 OG1 THR A 355 -9.612 -13.095 16.045 1.00 73.68 O ANISOU 2666 OG1 THR A 355 5865 15638 6491 1000 -1017 -1196 O ATOM 2667 CG2 THR A 355 -10.309 -14.050 18.156 1.00 57.15 C ANISOU 2667 CG2 THR A 355 3600 13845 4268 835 -948 -1284 C ATOM 2668 N TRP A 356 -6.978 -12.026 15.816 1.00 67.55 N ANISOU 2668 N TRP A 356 5461 14149 6057 1076 -1069 -1034 N ATOM 2669 CA TRP A 356 -5.968 -11.852 14.780 1.00 66.89 C ANISOU 2669 CA TRP A 356 5506 13836 6073 1033 -1071 -923 C ATOM 2670 C TRP A 356 -4.683 -11.207 15.358 1.00 71.21 C ANISOU 2670 C TRP A 356 6204 14076 6778 1067 -1106 -868 C ATOM 2671 O TRP A 356 -3.584 -11.507 14.878 1.00 70.00 O ANISOU 2671 O TRP A 356 6138 13751 6708 950 -1068 -784 O ATOM 2672 CB TRP A 356 -6.537 -11.091 13.573 1.00 66.38 C ANISOU 2672 CB TRP A 356 5422 13848 5950 1163 -1140 -880 C ATOM 2673 CG TRP A 356 -7.135 -12.029 12.560 1.00 67.35 C ANISOU 2673 CG TRP A 356 5443 14190 5956 1032 -1077 -887 C ATOM 2674 CD1 TRP A 356 -8.434 -12.446 12.492 1.00 71.09 C ANISOU 2674 CD1 TRP A 356 5756 14978 6278 1031 -1066 -972 C ATOM 2675 CD2 TRP A 356 -6.423 -12.772 11.558 1.00 66.45 C ANISOU 2675 CD2 TRP A 356 5372 14015 5860 867 -1014 -829 C ATOM 2676 NE1 TRP A 356 -8.582 -13.378 11.489 1.00 70.09 N ANISOU 2676 NE1 TRP A 356 5581 14967 6083 866 -1007 -968 N ATOM 2677 CE2 TRP A 356 -7.366 -13.590 10.892 1.00 70.66 C ANISOU 2677 CE2 TRP A 356 5779 14813 6257 776 -975 -890 C ATOM 2678 CE3 TRP A 356 -5.076 -12.826 11.155 1.00 66.64 C ANISOU 2678 CE3 TRP A 356 5516 13812 5992 791 -989 -742 C ATOM 2679 CZ2 TRP A 356 -7.006 -14.445 9.841 1.00 69.72 C ANISOU 2679 CZ2 TRP A 356 5663 14716 6113 623 -918 -882 C ATOM 2680 CZ3 TRP A 356 -4.726 -13.662 10.102 1.00 67.83 C ANISOU 2680 CZ3 TRP A 356 5655 14012 6106 654 -927 -732 C ATOM 2681 CH2 TRP A 356 -5.681 -14.462 9.462 1.00 69.02 C ANISOU 2681 CH2 TRP A 356 5691 14407 6127 576 -895 -809 C ATOM 2682 N LEU A 357 -4.823 -10.408 16.439 1.00 68.43 N ANISOU 2682 N LEU A 357 5865 13682 6453 1217 -1175 -933 N ATOM 2683 CA LEU A 357 -3.714 -9.790 17.167 1.00 67.42 C ANISOU 2683 CA LEU A 357 5865 13287 6463 1245 -1218 -908 C ATOM 2684 C LEU A 357 -2.841 -10.888 17.808 1.00 69.56 C ANISOU 2684 C LEU A 357 6151 13501 6779 1049 -1118 -892 C ATOM 2685 O LEU A 357 -1.616 -10.787 17.776 1.00 69.94 O ANISOU 2685 O LEU A 357 6303 13331 6938 980 -1113 -816 O ATOM 2686 CB LEU A 357 -4.266 -8.829 18.225 1.00 68.58 C ANISOU 2686 CB LEU A 357 5997 13462 6600 1455 -1314 -1027 C ATOM 2687 CG LEU A 357 -3.369 -7.685 18.684 1.00 73.96 C ANISOU 2687 CG LEU A 357 6829 13847 7425 1554 -1419 -1016 C ATOM 2688 CD1 LEU A 357 -3.136 -6.679 17.562 1.00 75.33 C ANISOU 2688 CD1 LEU A 357 7121 13830 7672 1637 -1526 -906 C ATOM 2689 CD2 LEU A 357 -3.998 -6.966 19.878 1.00 77.68 C ANISOU 2689 CD2 LEU A 357 7260 14391 7864 1757 -1501 -1184 C ATOM 2690 N GLY A 358 -3.481 -11.943 18.318 1.00 63.68 N ANISOU 2690 N GLY A 358 5296 12959 5939 952 -1045 -951 N ATOM 2691 CA GLY A 358 -2.813 -13.111 18.875 1.00 61.54 C ANISOU 2691 CA GLY A 358 5039 12645 5699 766 -962 -925 C ATOM 2692 C GLY A 358 -2.182 -13.935 17.768 1.00 64.07 C ANISOU 2692 C GLY A 358 5407 12876 6061 623 -903 -852 C ATOM 2693 O GLY A 358 -1.067 -14.450 17.921 1.00 61.88 O ANISOU 2693 O GLY A 358 5203 12436 5873 529 -867 -806 O ATOM 2694 N TYR A 359 -2.886 -14.034 16.617 1.00 61.71 N ANISOU 2694 N TYR A 359 5057 12701 5688 622 -899 -853 N ATOM 2695 CA TYR A 359 -2.393 -14.749 15.440 1.00 60.87 C ANISOU 2695 CA TYR A 359 4981 12551 5597 508 -850 -811 C ATOM 2696 C TYR A 359 -1.112 -14.095 14.914 1.00 65.56 C ANISOU 2696 C TYR A 359 5677 12940 6292 542 -870 -724 C ATOM 2697 O TYR A 359 -0.152 -14.798 14.610 1.00 64.94 O ANISOU 2697 O TYR A 359 5640 12769 6265 443 -820 -698 O ATOM 2698 CB TYR A 359 -3.448 -14.785 14.333 1.00 62.23 C ANISOU 2698 CB TYR A 359 5065 12928 5650 518 -854 -835 C ATOM 2699 CG TYR A 359 -4.693 -15.609 14.594 1.00 63.50 C ANISOU 2699 CG TYR A 359 5107 13329 5693 433 -827 -914 C ATOM 2700 CD1 TYR A 359 -5.867 -15.368 13.889 1.00 66.31 C ANISOU 2700 CD1 TYR A 359 5352 13923 5920 486 -850 -951 C ATOM 2701 CD2 TYR A 359 -4.668 -16.699 15.461 1.00 63.48 C ANISOU 2701 CD2 TYR A 359 5098 13320 5700 278 -781 -938 C ATOM 2702 CE1 TYR A 359 -7.006 -16.142 14.088 1.00 67.63 C ANISOU 2702 CE1 TYR A 359 5391 14339 5965 380 -826 -1019 C ATOM 2703 CE2 TYR A 359 -5.797 -17.494 15.656 1.00 65.00 C ANISOU 2703 CE2 TYR A 359 5180 13738 5778 156 -761 -989 C ATOM 2704 CZ TYR A 359 -6.968 -17.205 14.970 1.00 71.93 C ANISOU 2704 CZ TYR A 359 5934 14872 6522 202 -781 -1035 C ATOM 2705 OH TYR A 359 -8.105 -17.956 15.144 1.00 69.90 O ANISOU 2705 OH TYR A 359 5549 14871 6138 64 -764 -1083 O ATOM 2706 N LEU A 360 -1.086 -12.749 14.863 1.00 63.31 N ANISOU 2706 N LEU A 360 5432 12587 6035 681 -952 -681 N ATOM 2707 CA LEU A 360 0.040 -11.924 14.408 1.00 63.69 C ANISOU 2707 CA LEU A 360 5576 12451 6171 697 -992 -576 C ATOM 2708 C LEU A 360 1.332 -12.221 15.196 1.00 67.21 C ANISOU 2708 C LEU A 360 6084 12729 6723 620 -962 -557 C ATOM 2709 O LEU A 360 2.428 -12.074 14.652 1.00 67.21 O ANISOU 2709 O LEU A 360 6131 12632 6775 564 -954 -474 O ATOM 2710 CB LEU A 360 -0.347 -10.443 14.563 1.00 65.09 C ANISOU 2710 CB LEU A 360 5802 12558 6373 862 -1113 -548 C ATOM 2711 CG LEU A 360 0.486 -9.397 13.825 1.00 70.65 C ANISOU 2711 CG LEU A 360 6605 13091 7146 869 -1185 -408 C ATOM 2712 CD1 LEU A 360 0.190 -9.404 12.335 1.00 71.54 C ANISOU 2712 CD1 LEU A 360 6683 13324 7174 843 -1178 -320 C ATOM 2713 CD2 LEU A 360 0.201 -8.015 14.373 1.00 74.78 C ANISOU 2713 CD2 LEU A 360 7211 13468 7733 1028 -1324 -406 C ATOM 2714 N ASN A 361 1.201 -12.669 16.459 1.00 62.58 N ANISOU 2714 N ASN A 361 5483 12144 6151 611 -943 -630 N ATOM 2715 CA ASN A 361 2.335 -13.013 17.316 1.00 60.99 C ANISOU 2715 CA ASN A 361 5328 11810 6036 548 -919 -617 C ATOM 2716 C ASN A 361 3.140 -14.200 16.750 1.00 63.39 C ANISOU 2716 C ASN A 361 5631 12098 6356 427 -838 -595 C ATOM 2717 O ASN A 361 4.315 -14.359 17.085 1.00 62.87 O ANISOU 2717 O ASN A 361 5604 11921 6364 389 -825 -563 O ATOM 2718 CB ASN A 361 1.855 -13.316 18.736 1.00 58.53 C ANISOU 2718 CB ASN A 361 4983 11551 5704 563 -918 -693 C ATOM 2719 CG ASN A 361 2.977 -13.391 19.735 1.00 59.19 C ANISOU 2719 CG ASN A 361 5114 11505 5870 531 -918 -676 C ATOM 2720 OD1 ASN A 361 3.288 -14.463 20.264 1.00 47.48 O ANISOU 2720 OD1 ASN A 361 3619 10029 4390 444 -865 -676 O ATOM 2721 ND2 ASN A 361 3.646 -12.266 19.968 1.00 44.74 N ANISOU 2721 ND2 ASN A 361 3344 9544 4110 595 -987 -654 N ATOM 2722 N SER A 362 2.513 -15.006 15.882 1.00 59.45 N ANISOU 2722 N SER A 362 5085 11717 5786 377 -794 -626 N ATOM 2723 CA SER A 362 3.143 -16.150 15.226 1.00 59.04 C ANISOU 2723 CA SER A 362 5035 11656 5743 287 -732 -641 C ATOM 2724 C SER A 362 4.053 -15.673 14.077 1.00 61.47 C ANISOU 2724 C SER A 362 5349 11952 6055 294 -727 -578 C ATOM 2725 O SER A 362 4.882 -16.441 13.585 1.00 60.21 O ANISOU 2725 O SER A 362 5185 11784 5907 249 -682 -596 O ATOM 2726 CB SER A 362 2.080 -17.127 14.721 1.00 63.91 C ANISOU 2726 CB SER A 362 5601 12406 6277 226 -702 -714 C ATOM 2727 OG SER A 362 1.325 -17.652 15.803 1.00 75.42 O ANISOU 2727 OG SER A 362 7044 13891 7723 179 -702 -752 O ATOM 2728 N LEU A 363 3.900 -14.403 13.670 1.00 58.52 N ANISOU 2728 N LEU A 363 4985 11584 5668 353 -783 -502 N ATOM 2729 CA LEU A 363 4.678 -13.765 12.614 1.00 59.36 C ANISOU 2729 CA LEU A 363 5093 11699 5760 338 -793 -403 C ATOM 2730 C LEU A 363 5.738 -12.844 13.222 1.00 65.45 C ANISOU 2730 C LEU A 363 5923 12321 6623 336 -841 -316 C ATOM 2731 O LEU A 363 6.865 -12.809 12.724 1.00 66.40 O ANISOU 2731 O LEU A 363 6033 12444 6753 275 -820 -251 O ATOM 2732 CB LEU A 363 3.749 -12.984 11.649 1.00 60.17 C ANISOU 2732 CB LEU A 363 5175 11906 5779 388 -842 -352 C ATOM 2733 CG LEU A 363 4.414 -12.007 10.670 1.00 65.82 C ANISOU 2733 CG LEU A 363 5907 12626 6477 370 -883 -203 C ATOM 2734 CD1 LEU A 363 5.165 -12.732 9.564 1.00 66.50 C ANISOU 2734 CD1 LEU A 363 5926 12853 6489 287 -807 -195 C ATOM 2735 CD2 LEU A 363 3.419 -11.030 10.111 1.00 68.69 C ANISOU 2735 CD2 LEU A 363 6280 13033 6785 451 -966 -137 C ATOM 2736 N ILE A 364 5.380 -12.099 14.287 1.00 62.41 N ANISOU 2736 N ILE A 364 5591 11828 6295 400 -909 -324 N ATOM 2737 CA ILE A 364 6.272 -11.152 14.967 1.00 62.62 C ANISOU 2737 CA ILE A 364 5684 11696 6414 396 -975 -261 C ATOM 2738 C ILE A 364 7.493 -11.898 15.548 1.00 66.09 C ANISOU 2738 C ILE A 364 6108 12099 6903 324 -917 -277 C ATOM 2739 O ILE A 364 8.626 -11.506 15.260 1.00 66.55 O ANISOU 2739 O ILE A 364 6173 12122 6993 258 -927 -192 O ATOM 2740 CB ILE A 364 5.503 -10.321 16.039 1.00 65.88 C ANISOU 2740 CB ILE A 364 6146 12021 6864 504 -1062 -318 C ATOM 2741 CG1 ILE A 364 4.414 -9.445 15.371 1.00 67.22 C ANISOU 2741 CG1 ILE A 364 6332 12218 6990 604 -1140 -295 C ATOM 2742 CG2 ILE A 364 6.451 -9.440 16.841 1.00 66.67 C ANISOU 2742 CG2 ILE A 364 6319 11947 7065 491 -1135 -284 C ATOM 2743 CD1 ILE A 364 3.362 -8.871 16.317 1.00 73.16 C ANISOU 2743 CD1 ILE A 364 7100 12952 7745 751 -1216 -398 C ATOM 2744 N ASN A 365 7.254 -12.985 16.314 1.00 60.86 N ANISOU 2744 N ASN A 365 5420 11463 6240 331 -863 -374 N ATOM 2745 CA ASN A 365 8.282 -13.819 16.956 1.00 58.98 C ANISOU 2745 CA ASN A 365 5173 11190 6048 290 -819 -394 C ATOM 2746 C ASN A 365 9.389 -14.266 15.971 1.00 60.95 C ANISOU 2746 C ASN A 365 5379 11496 6283 237 -769 -356 C ATOM 2747 O ASN A 365 10.537 -13.915 16.249 1.00 59.58 O ANISOU 2747 O ASN A 365 5202 11285 6152 205 -782 -304 O ATOM 2748 CB ASN A 365 7.650 -15.019 17.635 1.00 57.17 C ANISOU 2748 CB ASN A 365 4931 10987 5805 294 -779 -480 C ATOM 2749 CG ASN A 365 7.668 -14.900 19.111 1.00 78.96 C ANISOU 2749 CG ASN A 365 7712 13689 8602 314 -810 -500 C ATOM 2750 OD1 ASN A 365 6.833 -14.224 19.722 1.00 69.45 O ANISOU 2750 OD1 ASN A 365 6513 12498 7378 363 -855 -528 O ATOM 2751 ND2 ASN A 365 8.662 -15.525 19.710 1.00 79.68 N ANISOU 2751 ND2 ASN A 365 7805 13732 8739 289 -791 -492 N ATOM 2752 N PRO A 366 9.109 -14.929 14.799 1.00 57.29 N ANISOU 2752 N PRO A 366 4871 11146 5749 228 -718 -384 N ATOM 2753 CA PRO A 366 10.212 -15.289 13.885 1.00 56.79 C ANISOU 2753 CA PRO A 366 4747 11177 5653 196 -673 -367 C ATOM 2754 C PRO A 366 10.903 -14.089 13.250 1.00 61.91 C ANISOU 2754 C PRO A 366 5376 11870 6279 140 -705 -234 C ATOM 2755 O PRO A 366 12.071 -14.216 12.914 1.00 62.26 O ANISOU 2755 O PRO A 366 5357 11995 6305 102 -676 -204 O ATOM 2756 CB PRO A 366 9.549 -16.154 12.821 1.00 58.63 C ANISOU 2756 CB PRO A 366 4942 11530 5806 206 -626 -447 C ATOM 2757 CG PRO A 366 8.124 -15.817 12.874 1.00 63.30 C ANISOU 2757 CG PRO A 366 5565 12116 6371 221 -657 -454 C ATOM 2758 CD PRO A 366 7.824 -15.458 14.297 1.00 58.59 C ANISOU 2758 CD PRO A 366 5026 11386 5851 244 -699 -452 C ATOM 2759 N ILE A 367 10.243 -12.921 13.129 1.00 60.21 N ANISOU 2759 N ILE A 367 5210 11602 6063 134 -774 -148 N ATOM 2760 CA ILE A 367 10.964 -11.774 12.558 1.00 61.64 C ANISOU 2760 CA ILE A 367 5392 11795 6235 54 -824 7 C ATOM 2761 C ILE A 367 11.873 -11.148 13.635 1.00 65.07 C ANISOU 2761 C ILE A 367 5868 12089 6766 11 -876 49 C ATOM 2762 O ILE A 367 12.927 -10.639 13.273 1.00 65.63 O ANISOU 2762 O ILE A 367 5903 12206 6826 -91 -889 156 O ATOM 2763 CB ILE A 367 10.105 -10.711 11.800 1.00 66.07 C ANISOU 2763 CB ILE A 367 5999 12346 6757 55 -898 114 C ATOM 2764 CG1 ILE A 367 9.531 -9.611 12.708 1.00 67.35 C ANISOU 2764 CG1 ILE A 367 6278 12299 7014 107 -1012 137 C ATOM 2765 CG2 ILE A 367 9.053 -11.345 10.861 1.00 66.42 C ANISOU 2765 CG2 ILE A 367 5995 12543 6698 106 -852 56 C ATOM 2766 CD1 ILE A 367 9.098 -8.391 11.952 1.00 82.54 C ANISOU 2766 CD1 ILE A 367 8263 14175 8922 98 -1113 282 C ATOM 2767 N ILE A 368 11.494 -11.222 14.938 1.00 60.96 N ANISOU 2767 N ILE A 368 5407 11431 6325 76 -905 -38 N ATOM 2768 CA ILE A 368 12.300 -10.688 16.050 1.00 61.33 C ANISOU 2768 CA ILE A 368 5489 11358 6456 44 -957 -25 C ATOM 2769 C ILE A 368 13.600 -11.507 16.170 1.00 65.77 C ANISOU 2769 C ILE A 368 5963 12017 7010 -1 -889 -39 C ATOM 2770 O ILE A 368 14.660 -10.917 16.343 1.00 65.97 O ANISOU 2770 O ILE A 368 5970 12037 7060 -88 -922 35 O ATOM 2771 CB ILE A 368 11.518 -10.621 17.411 1.00 63.71 C ANISOU 2771 CB ILE A 368 5854 11538 6815 136 -999 -130 C ATOM 2772 CG1 ILE A 368 10.319 -9.626 17.335 1.00 65.02 C ANISOU 2772 CG1 ILE A 368 6099 11617 6989 205 -1087 -128 C ATOM 2773 CG2 ILE A 368 12.445 -10.280 18.600 1.00 62.42 C ANISOU 2773 CG2 ILE A 368 5706 11289 6722 104 -1041 -141 C ATOM 2774 CD1 ILE A 368 9.412 -9.541 18.623 1.00 69.28 C ANISOU 2774 CD1 ILE A 368 6671 12100 7551 316 -1124 -253 C ATOM 2775 N TYR A 369 13.516 -12.846 16.059 1.00 62.56 N ANISOU 2775 N TYR A 369 5503 11697 6568 60 -805 -135 N ATOM 2776 CA TYR A 369 14.672 -13.730 16.154 1.00 63.06 C ANISOU 2776 CA TYR A 369 5486 11851 6625 63 -750 -169 C ATOM 2777 C TYR A 369 15.604 -13.571 14.989 1.00 69.58 C ANISOU 2777 C TYR A 369 6210 12854 7373 -7 -718 -99 C ATOM 2778 O TYR A 369 16.813 -13.593 15.192 1.00 71.79 O ANISOU 2778 O TYR A 369 6417 13211 7651 -45 -711 -74 O ATOM 2779 CB TYR A 369 14.255 -15.201 16.238 1.00 64.48 C ANISOU 2779 CB TYR A 369 5658 12044 6797 154 -692 -292 C ATOM 2780 CG TYR A 369 14.001 -15.698 17.642 1.00 67.53 C ANISOU 2780 CG TYR A 369 6100 12308 7250 202 -712 -345 C ATOM 2781 CD1 TYR A 369 12.720 -16.069 18.051 1.00 69.31 C ANISOU 2781 CD1 TYR A 369 6386 12467 7480 233 -718 -396 C ATOM 2782 CD2 TYR A 369 15.044 -15.822 18.559 1.00 68.80 C ANISOU 2782 CD2 TYR A 369 6236 12451 7453 208 -726 -338 C ATOM 2783 CE1 TYR A 369 12.480 -16.540 19.342 1.00 69.76 C ANISOU 2783 CE1 TYR A 369 6480 12449 7577 259 -735 -427 C ATOM 2784 CE2 TYR A 369 14.814 -16.277 19.858 1.00 69.57 C ANISOU 2784 CE2 TYR A 369 6377 12460 7595 247 -748 -371 C ATOM 2785 CZ TYR A 369 13.530 -16.640 20.242 1.00 78.77 C ANISOU 2785 CZ TYR A 369 7604 13566 8758 267 -751 -410 C ATOM 2786 OH TYR A 369 13.298 -17.109 21.513 1.00 82.69 O ANISOU 2786 OH TYR A 369 8132 14011 9278 287 -772 -425 O ATOM 2787 N THR A 370 15.075 -13.439 13.769 1.00 65.54 N ANISOU 2787 N THR A 370 5678 12443 6782 -25 -698 -67 N ATOM 2788 CA THR A 370 15.947 -13.344 12.600 1.00 66.58 C ANISOU 2788 CA THR A 370 5690 12799 6808 -96 -660 1 C ATOM 2789 C THR A 370 16.569 -11.939 12.482 1.00 70.74 C ANISOU 2789 C THR A 370 6218 13326 7334 -251 -728 185 C ATOM 2790 O THR A 370 17.531 -11.775 11.745 1.00 72.13 O ANISOU 2790 O THR A 370 6277 13710 7421 -343 -701 265 O ATOM 2791 CB THR A 370 15.240 -13.804 11.298 1.00 72.68 C ANISOU 2791 CB THR A 370 6421 13721 7472 -65 -612 -36 C ATOM 2792 OG1 THR A 370 14.313 -12.817 10.865 1.00 74.67 O ANISOU 2792 OG1 THR A 370 6746 13913 7712 -111 -668 72 O ATOM 2793 CG2 THR A 370 14.542 -15.154 11.448 1.00 66.61 C ANISOU 2793 CG2 THR A 370 5673 12918 6718 61 -565 -219 C ATOM 2794 N MET A 371 16.048 -10.945 13.202 1.00 66.30 N ANISOU 2794 N MET A 371 5783 12542 6865 -282 -821 248 N ATOM 2795 CA MET A 371 16.626 -9.606 13.144 1.00 67.93 C ANISOU 2795 CA MET A 371 6019 12697 7093 -440 -909 421 C ATOM 2796 C MET A 371 17.675 -9.431 14.245 1.00 72.73 C ANISOU 2796 C MET A 371 6612 13251 7772 -494 -937 409 C ATOM 2797 O MET A 371 18.633 -8.671 14.075 1.00 74.44 O ANISOU 2797 O MET A 371 6786 13525 7974 -658 -979 539 O ATOM 2798 CB MET A 371 15.536 -8.533 13.259 1.00 70.78 C ANISOU 2798 CB MET A 371 6537 12832 7523 -432 -1020 485 C ATOM 2799 CG MET A 371 14.783 -8.317 11.971 1.00 75.94 C ANISOU 2799 CG MET A 371 7191 13574 8087 -435 -1020 572 C ATOM 2800 SD MET A 371 13.962 -6.711 11.879 1.00 82.32 S ANISOU 2800 SD MET A 371 8176 14133 8971 -465 -1188 720 S ATOM 2801 CE MET A 371 12.419 -7.090 12.628 1.00 77.64 C ANISOU 2801 CE MET A 371 7662 13407 8430 -241 -1192 530 C ATOM 2802 N SER A 372 17.497 -10.171 15.360 1.00 66.87 N ANISOU 2802 N SER A 372 5894 12419 7096 -369 -915 259 N ATOM 2803 CA SER A 372 18.309 -10.132 16.566 1.00 65.68 C ANISOU 2803 CA SER A 372 5735 12212 7011 -384 -943 221 C ATOM 2804 C SER A 372 19.408 -11.198 16.599 1.00 70.30 C ANISOU 2804 C SER A 372 6171 12999 7541 -350 -859 162 C ATOM 2805 O SER A 372 20.558 -10.855 16.876 1.00 71.62 O ANISOU 2805 O SER A 372 6260 13252 7701 -448 -879 214 O ATOM 2806 CB SER A 372 17.410 -10.295 17.776 1.00 66.14 C ANISOU 2806 CB SER A 372 5899 12079 7151 -263 -974 105 C ATOM 2807 OG SER A 372 16.358 -9.348 17.722 1.00 71.85 O ANISOU 2807 OG SER A 372 6747 12635 7917 -260 -1057 135 O ATOM 2808 N ASN A 373 19.063 -12.480 16.365 1.00 65.36 N ANISOU 2808 N ASN A 373 5511 12442 6883 -206 -778 46 N ATOM 2809 CA ASN A 373 20.042 -13.570 16.357 1.00 65.36 C ANISOU 2809 CA ASN A 373 5383 12613 6839 -130 -713 -32 C ATOM 2810 C ASN A 373 20.847 -13.488 15.050 1.00 72.49 C ANISOU 2810 C ASN A 373 6135 13791 7617 -204 -666 29 C ATOM 2811 O ASN A 373 20.256 -13.518 13.969 1.00 73.13 O ANISOU 2811 O ASN A 373 6212 13943 7630 -209 -636 43 O ATOM 2812 CB ASN A 373 19.329 -14.919 16.527 1.00 62.65 C ANISOU 2812 CB ASN A 373 5081 12206 6516 39 -668 -173 C ATOM 2813 CG ASN A 373 20.234 -16.113 16.629 1.00 80.38 C ANISOU 2813 CG ASN A 373 7231 14569 8742 157 -626 -270 C ATOM 2814 OD1 ASN A 373 20.898 -16.500 15.668 1.00 75.63 O ANISOU 2814 OD1 ASN A 373 6506 14178 8051 184 -578 -301 O ATOM 2815 ND2 ASN A 373 20.212 -16.777 17.769 1.00 69.78 N ANISOU 2815 ND2 ASN A 373 5943 13096 7473 247 -649 -328 N ATOM 2816 N GLU A 374 22.183 -13.342 15.147 1.00 71.17 N ANISOU 2816 N GLU A 374 5830 13809 7403 -271 -662 68 N ATOM 2817 CA GLU A 374 23.056 -13.192 13.976 1.00 73.12 C ANISOU 2817 CA GLU A 374 5900 14375 7505 -362 -617 137 C ATOM 2818 C GLU A 374 23.160 -14.457 13.116 1.00 76.99 C ANISOU 2818 C GLU A 374 6278 15078 7897 -195 -529 -7 C ATOM 2819 O GLU A 374 23.458 -14.338 11.920 1.00 77.37 O ANISOU 2819 O GLU A 374 6202 15390 7806 -255 -486 35 O ATOM 2820 CB GLU A 374 24.454 -12.702 14.359 1.00 76.03 C ANISOU 2820 CB GLU A 374 6130 14920 7837 -488 -638 213 C ATOM 2821 CG GLU A 374 24.791 -11.377 13.692 1.00 91.86 C ANISOU 2821 CG GLU A 374 8103 17019 9780 -754 -683 423 C ATOM 2822 CD GLU A 374 24.295 -10.157 14.448 1.00127.78 C ANISOU 2822 CD GLU A 374 12840 21247 14463 -892 -798 530 C ATOM 2823 OE1 GLU A 374 23.084 -9.849 14.363 1.00123.50 O ANISOU 2823 OE1 GLU A 374 12467 20468 13990 -855 -833 538 O ATOM 2824 OE2 GLU A 374 25.117 -9.522 15.148 1.00133.16 O ANISOU 2824 OE2 GLU A 374 13497 21919 15180 -1027 -859 590 O ATOM 2825 N ASP A 375 22.899 -15.648 13.696 1.00 72.59 N ANISOU 2825 N ASP A 375 5770 14405 7408 8 -512 -176 N ATOM 2826 CA ASP A 375 22.911 -16.897 12.933 1.00 72.85 C ANISOU 2826 CA ASP A 375 5731 14576 7373 186 -451 -341 C ATOM 2827 C ASP A 375 21.726 -16.901 11.977 1.00 74.39 C ANISOU 2827 C ASP A 375 6000 14731 7533 174 -430 -353 C ATOM 2828 O ASP A 375 21.907 -17.203 10.794 1.00 75.64 O ANISOU 2828 O ASP A 375 6039 15142 7558 198 -379 -403 O ATOM 2829 CB ASP A 375 22.884 -18.137 13.845 1.00 74.58 C ANISOU 2829 CB ASP A 375 6020 14621 7695 388 -465 -495 C ATOM 2830 CG ASP A 375 24.002 -18.219 14.859 1.00 91.67 C ANISOU 2830 CG ASP A 375 8115 16823 9894 427 -493 -490 C ATOM 2831 OD1 ASP A 375 25.126 -17.769 14.543 1.00 95.39 O ANISOU 2831 OD1 ASP A 375 8406 17573 10265 366 -475 -443 O ATOM 2832 OD2 ASP A 375 23.764 -18.765 15.960 1.00 99.55 O ANISOU 2832 OD2 ASP A 375 9225 17596 11005 518 -533 -530 O ATOM 2833 N PHE A 376 20.526 -16.517 12.482 1.00 66.59 N ANISOU 2833 N PHE A 376 5193 13462 6647 135 -472 -308 N ATOM 2834 CA PHE A 376 19.307 -16.423 11.686 1.00 64.67 C ANISOU 2834 CA PHE A 376 5023 13174 6374 118 -463 -308 C ATOM 2835 C PHE A 376 19.353 -15.226 10.733 1.00 68.18 C ANISOU 2835 C PHE A 376 5414 13774 6719 -49 -471 -134 C ATOM 2836 O PHE A 376 18.808 -15.319 9.634 1.00 69.10 O ANISOU 2836 O PHE A 376 5505 14010 6741 -52 -443 -141 O ATOM 2837 CB PHE A 376 18.072 -16.346 12.588 1.00 64.53 C ANISOU 2837 CB PHE A 376 5188 12849 6482 136 -510 -314 C ATOM 2838 CG PHE A 376 17.706 -17.687 13.173 1.00 65.10 C ANISOU 2838 CG PHE A 376 5323 12785 6625 281 -501 -473 C ATOM 2839 CD1 PHE A 376 17.097 -18.667 12.387 1.00 67.67 C ANISOU 2839 CD1 PHE A 376 5657 13143 6912 362 -469 -604 C ATOM 2840 CD2 PHE A 376 17.974 -17.978 14.507 1.00 65.72 C ANISOU 2840 CD2 PHE A 376 5461 12704 6807 324 -535 -486 C ATOM 2841 CE1 PHE A 376 16.790 -19.922 12.922 1.00 67.88 C ANISOU 2841 CE1 PHE A 376 5760 13016 7014 474 -479 -737 C ATOM 2842 CE2 PHE A 376 17.652 -19.227 15.045 1.00 67.63 C ANISOU 2842 CE2 PHE A 376 5772 12811 7114 440 -540 -603 C ATOM 2843 CZ PHE A 376 17.062 -20.187 14.251 1.00 66.20 C ANISOU 2843 CZ PHE A 376 5612 12634 6906 507 -517 -723 C ATOM 2844 N LYS A 377 20.008 -14.115 11.143 1.00 63.45 N ANISOU 2844 N LYS A 377 4800 13170 6138 -199 -518 27 N ATOM 2845 CA LYS A 377 20.170 -12.897 10.338 1.00 63.83 C ANISOU 2845 CA LYS A 377 4813 13336 6104 -391 -549 230 C ATOM 2846 C LYS A 377 20.991 -13.188 9.072 1.00 70.18 C ANISOU 2846 C LYS A 377 5407 14542 6715 -426 -477 241 C ATOM 2847 O LYS A 377 20.526 -12.872 7.976 1.00 70.82 O ANISOU 2847 O LYS A 377 5463 14759 6688 -490 -467 322 O ATOM 2848 CB LYS A 377 20.834 -11.785 11.174 1.00 65.70 C ANISOU 2848 CB LYS A 377 5087 13459 6418 -550 -628 378 C ATOM 2849 CG LYS A 377 20.698 -10.376 10.606 1.00 68.47 C ANISOU 2849 CG LYS A 377 5482 13792 6740 -761 -704 611 C ATOM 2850 CD LYS A 377 21.500 -9.379 11.453 1.00 67.06 C ANISOU 2850 CD LYS A 377 5339 13495 6645 -928 -793 731 C ATOM 2851 CE LYS A 377 21.270 -7.925 11.108 1.00 73.96 C ANISOU 2851 CE LYS A 377 6319 14243 7541 -1135 -906 961 C ATOM 2852 NZ LYS A 377 19.869 -7.481 11.384 1.00 84.08 N ANISOU 2852 NZ LYS A 377 7816 15188 8944 -1045 -986 946 N ATOM 2853 N GLN A 378 22.190 -13.817 9.228 1.00 67.40 N ANISOU 2853 N GLN A 378 4895 14405 6310 -370 -430 151 N ATOM 2854 CA GLN A 378 23.104 -14.175 8.136 1.00 69.19 C ANISOU 2854 CA GLN A 378 4886 15067 6336 -375 -357 125 C ATOM 2855 C GLN A 378 22.471 -15.220 7.202 1.00 72.75 C ANISOU 2855 C GLN A 378 5305 15635 6701 -202 -295 -61 C ATOM 2856 O GLN A 378 22.727 -15.183 5.989 1.00 73.86 O ANISOU 2856 O GLN A 378 5289 16124 6652 -247 -247 -38 O ATOM 2857 CB GLN A 378 24.459 -14.669 8.676 1.00 71.39 C ANISOU 2857 CB GLN A 378 5005 15529 6591 -311 -332 40 C ATOM 2858 N ALA A 379 21.614 -16.118 7.758 1.00 67.04 N ANISOU 2858 N ALA A 379 4732 14630 6110 -24 -302 -236 N ATOM 2859 CA ALA A 379 20.881 -17.141 6.996 1.00 66.12 C ANISOU 2859 CA ALA A 379 4623 14556 5943 128 -263 -428 C ATOM 2860 C ALA A 379 19.889 -16.484 6.059 1.00 69.74 C ANISOU 2860 C ALA A 379 5122 15055 6323 18 -267 -315 C ATOM 2861 O ALA A 379 19.750 -16.927 4.916 1.00 70.48 O ANISOU 2861 O ALA A 379 5113 15400 6266 64 -220 -406 O ATOM 2862 CB ALA A 379 20.158 -18.090 7.933 1.00 64.88 C ANISOU 2862 CB ALA A 379 4640 14052 5961 284 -290 -588 C ATOM 2863 N PHE A 380 19.227 -15.405 6.539 1.00 65.34 N ANISOU 2863 N PHE A 380 4707 14261 5859 -118 -331 -123 N ATOM 2864 CA PHE A 380 18.259 -14.634 5.773 1.00 65.67 C ANISOU 2864 CA PHE A 380 4806 14303 5845 -217 -358 15 C ATOM 2865 C PHE A 380 18.963 -13.896 4.644 1.00 72.39 C ANISOU 2865 C PHE A 380 5492 15513 6501 -376 -340 192 C ATOM 2866 O PHE A 380 18.529 -14.004 3.501 1.00 73.47 O ANISOU 2866 O PHE A 380 5559 15868 6488 -377 -310 188 O ATOM 2867 CB PHE A 380 17.473 -13.666 6.669 1.00 66.25 C ANISOU 2867 CB PHE A 380 5074 14021 6077 -287 -447 154 C ATOM 2868 CG PHE A 380 16.280 -13.063 5.969 1.00 68.28 C ANISOU 2868 CG PHE A 380 5407 14241 6293 -326 -485 253 C ATOM 2869 CD1 PHE A 380 15.093 -13.778 5.840 1.00 71.21 C ANISOU 2869 CD1 PHE A 380 5843 14533 6679 -204 -470 104 C ATOM 2870 CD2 PHE A 380 16.352 -11.796 5.405 1.00 71.90 C ANISOU 2870 CD2 PHE A 380 5869 14759 6692 -492 -544 503 C ATOM 2871 CE1 PHE A 380 13.993 -13.226 5.174 1.00 72.43 C ANISOU 2871 CE1 PHE A 380 6049 14690 6782 -229 -507 191 C ATOM 2872 CE2 PHE A 380 15.256 -11.248 4.734 1.00 75.33 C ANISOU 2872 CE2 PHE A 380 6372 15168 7084 -507 -590 601 C ATOM 2873 CZ PHE A 380 14.079 -11.962 4.631 1.00 72.57 C ANISOU 2873 CZ PHE A 380 6070 14762 6742 -367 -568 438 C ATOM 2874 N HIS A 381 20.061 -13.183 4.957 1.00 70.34 N ANISOU 2874 N HIS A 381 5158 15338 6229 -520 -360 347 N ATOM 2875 CA HIS A 381 20.890 -12.441 3.998 1.00 72.95 C ANISOU 2875 CA HIS A 381 5316 16032 6368 -714 -349 548 C ATOM 2876 C HIS A 381 21.368 -13.373 2.879 1.00 78.67 C ANISOU 2876 C HIS A 381 5811 17210 6870 -619 -248 390 C ATOM 2877 O HIS A 381 21.363 -12.972 1.712 1.00 80.43 O ANISOU 2877 O HIS A 381 5917 17746 6898 -731 -229 516 O ATOM 2878 CB HIS A 381 22.084 -11.781 4.711 1.00 74.76 C ANISOU 2878 CB HIS A 381 5491 16278 6635 -870 -383 685 C ATOM 2879 CG HIS A 381 21.723 -10.623 5.599 1.00 77.70 C ANISOU 2879 CG HIS A 381 6073 16260 7191 -1008 -498 868 C ATOM 2880 ND1 HIS A 381 22.699 -9.805 6.138 1.00 80.47 N ANISOU 2880 ND1 HIS A 381 6396 16605 7576 -1198 -553 1025 N ATOM 2881 CD2 HIS A 381 20.508 -10.183 6.015 1.00 78.66 C ANISOU 2881 CD2 HIS A 381 6420 16007 7460 -970 -574 897 C ATOM 2882 CE1 HIS A 381 22.056 -8.899 6.857 1.00 79.43 C ANISOU 2882 CE1 HIS A 381 6487 16075 7619 -1264 -664 1133 C ATOM 2883 NE2 HIS A 381 20.736 -9.089 6.820 1.00 78.60 N ANISOU 2883 NE2 HIS A 381 6535 15745 7585 -1120 -679 1057 N ATOM 2884 N LYS A 382 21.704 -14.637 3.228 1.00 74.18 N ANISOU 2884 N LYS A 382 5189 16665 6333 -397 -193 106 N ATOM 2885 CA LYS A 382 22.088 -15.671 2.264 1.00 74.91 C ANISOU 2885 CA LYS A 382 5084 17139 6239 -245 -110 -115 C ATOM 2886 C LYS A 382 20.884 -16.004 1.355 1.00 76.63 C ANISOU 2886 C LYS A 382 5357 17369 6390 -184 -99 -196 C ATOM 2887 O LYS A 382 21.026 -15.963 0.135 1.00 78.06 O ANISOU 2887 O LYS A 382 5369 17949 6343 -226 -54 -180 O ATOM 2888 CB LYS A 382 22.598 -16.936 2.989 1.00 77.13 C ANISOU 2888 CB LYS A 382 5355 17332 6619 1 -88 -402 C ATOM 2889 CG LYS A 382 23.896 -17.516 2.426 1.00 97.47 C ANISOU 2889 CG LYS A 382 7654 20371 9007 97 -23 -541 C ATOM 2890 CD LYS A 382 23.680 -18.479 1.249 1.00113.41 C ANISOU 2890 CD LYS A 382 9547 22692 10850 267 33 -787 C ATOM 2891 CE LYS A 382 23.715 -19.933 1.662 1.00125.96 C ANISOU 2891 CE LYS A 382 11187 24127 12546 573 28 -1133 C ATOM 2892 NZ LYS A 382 23.733 -20.845 0.485 1.00135.13 N ANISOU 2892 NZ LYS A 382 12197 25629 13518 745 74 -1400 N ATOM 2893 N LEU A 383 19.693 -16.263 1.962 1.00 69.59 N ANISOU 2893 N LEU A 383 4691 16065 5684 -104 -142 -268 N ATOM 2894 CA LEU A 383 18.438 -16.608 1.290 1.00 67.91 C ANISOU 2894 CA LEU A 383 4552 15814 5439 -47 -142 -356 C ATOM 2895 C LEU A 383 18.055 -15.583 0.222 1.00 75.29 C ANISOU 2895 C LEU A 383 5430 16972 6204 -220 -154 -119 C ATOM 2896 O LEU A 383 17.748 -15.992 -0.901 1.00 78.41 O ANISOU 2896 O LEU A 383 5717 17656 6419 -181 -114 -212 O ATOM 2897 CB LEU A 383 17.302 -16.770 2.316 1.00 64.89 C ANISOU 2897 CB LEU A 383 4413 14955 5287 10 -198 -400 C ATOM 2898 CG LEU A 383 15.875 -16.987 1.785 1.00 67.87 C ANISOU 2898 CG LEU A 383 4881 15258 5649 40 -213 -460 C ATOM 2899 CD1 LEU A 383 15.766 -18.277 0.979 1.00 69.40 C ANISOU 2899 CD1 LEU A 383 4987 15645 5738 186 -163 -748 C ATOM 2900 CD2 LEU A 383 14.854 -16.955 2.916 1.00 62.88 C ANISOU 2900 CD2 LEU A 383 4464 14197 5231 64 -271 -458 C ATOM 2901 N ILE A 384 18.094 -14.273 0.543 1.00 70.63 N ANISOU 2901 N ILE A 384 4915 16255 5666 -409 -218 183 N ATOM 2902 CA ILE A 384 17.746 -13.213 -0.424 1.00 71.14 C ANISOU 2902 CA ILE A 384 4952 16492 5585 -584 -254 451 C ATOM 2903 C ILE A 384 18.979 -12.711 -1.237 1.00 76.30 C ANISOU 2903 C ILE A 384 5376 17601 6014 -756 -219 626 C ATOM 2904 O ILE A 384 18.843 -11.755 -2.002 1.00 76.32 O ANISOU 2904 O ILE A 384 5351 17759 5888 -936 -259 895 O ATOM 2905 CB ILE A 384 17.014 -12.027 0.254 1.00 72.94 C ANISOU 2905 CB ILE A 384 5403 16321 5989 -689 -367 688 C ATOM 2906 CG1 ILE A 384 17.726 -11.581 1.548 1.00 72.49 C ANISOU 2906 CG1 ILE A 384 5433 15992 6119 -748 -412 753 C ATOM 2907 CG2 ILE A 384 15.537 -12.337 0.477 1.00 71.02 C ANISOU 2907 CG2 ILE A 384 5325 15802 5857 -551 -398 566 C ATOM 2908 CD1 ILE A 384 17.775 -10.157 1.730 1.00 80.50 C ANISOU 2908 CD1 ILE A 384 6554 16837 7194 -944 -520 1059 C ATOM 2909 N ARG A 385 20.157 -13.372 -1.087 1.00 74.16 N ANISOU 2909 N ARG A 385 4934 17560 5683 -700 -150 478 N ATOM 2910 CA ARG A 385 21.445 -13.075 -1.759 1.00 76.38 C ANISOU 2910 CA ARG A 385 4954 18333 5735 -844 -103 597 C ATOM 2911 C ARG A 385 21.868 -11.603 -1.539 1.00 81.23 C ANISOU 2911 C ARG A 385 5613 18877 6373 -1147 -185 987 C ATOM 2912 O ARG A 385 22.229 -10.898 -2.491 1.00 82.79 O ANISOU 2912 O ARG A 385 5670 19429 6358 -1358 -187 1231 O ATOM 2913 CB ARG A 385 21.421 -13.446 -3.261 1.00 76.99 C ANISOU 2913 CB ARG A 385 4811 18937 5506 -829 -33 541 C ATOM 2914 N PHE A 386 21.821 -11.162 -0.258 1.00 76.64 N ANISOU 2914 N PHE A 386 5232 17835 6052 -1171 -260 1040 N ATOM 2915 CA PHE A 386 22.202 -9.820 0.205 1.00 77.86 C ANISOU 2915 CA PHE A 386 5480 17814 6291 -1437 -361 1361 C ATOM 2916 C PHE A 386 23.492 -9.882 1.058 1.00 83.62 C ANISOU 2916 C PHE A 386 6109 18595 7067 -1492 -346 1332 C ATOM 2917 O PHE A 386 23.589 -10.710 1.964 1.00 82.12 O ANISOU 2917 O PHE A 386 5961 18222 7020 -1290 -318 1086 O ATOM 2918 CB PHE A 386 21.043 -9.181 0.998 1.00 77.55 C ANISOU 2918 CB PHE A 386 5754 17206 6507 -1413 -475 1431 C ATOM 2919 CG PHE A 386 21.345 -7.898 1.741 1.00 80.00 C ANISOU 2919 CG PHE A 386 6210 17222 6963 -1636 -602 1694 C ATOM 2920 CD1 PHE A 386 21.349 -6.675 1.080 1.00 85.59 C ANISOU 2920 CD1 PHE A 386 6951 17974 7595 -1895 -696 2037 C ATOM 2921 CD2 PHE A 386 21.587 -7.908 3.111 1.00 80.98 C ANISOU 2921 CD2 PHE A 386 6453 17012 7304 -1588 -640 1598 C ATOM 2922 CE1 PHE A 386 21.625 -5.487 1.769 1.00 87.22 C ANISOU 2922 CE1 PHE A 386 7315 17872 7952 -2105 -835 2269 C ATOM 2923 CE2 PHE A 386 21.860 -6.719 3.800 1.00 84.44 C ANISOU 2923 CE2 PHE A 386 7032 17174 7879 -1792 -768 1815 C ATOM 2924 CZ PHE A 386 21.879 -5.517 3.122 1.00 84.81 C ANISOU 2924 CZ PHE A 386 7121 17242 7862 -2050 -869 2143 C ATOM 2925 N LYS A 387 24.470 -9.001 0.777 1.00 82.62 N ANISOU 2925 N LYS A 387 5849 18724 6817 -1777 -374 1596 N ATOM 2926 CA LYS A 387 25.720 -8.974 1.540 1.00111.03 C ANISOU 2926 CA LYS A 387 9331 22418 10439 -1861 -366 1589 C ATOM 2927 C LYS A 387 25.810 -7.723 2.425 1.00122.46 C ANISOU 2927 C LYS A 387 10975 23476 12077 -2104 -505 1840 C ATOM 2928 O LYS A 387 25.793 -6.597 1.929 1.00 83.60 O ANISOU 2928 O LYS A 387 6105 18547 7110 -2380 -593 2155 O ATOM 2929 CB LYS A 387 26.938 -9.078 0.604 1.00116.71 C ANISOU 2929 CB LYS A 387 9697 23798 10848 -1999 -282 1656 C ATOM 2930 CG LYS A 387 27.369 -10.514 0.305 1.00131.82 C ANISOU 2930 CG LYS A 387 11383 26077 12624 -1699 -150 1300 C ATOM 2931 CD LYS A 387 28.175 -11.136 1.455 1.00140.34 C ANISOU 2931 CD LYS A 387 12422 27071 13831 -1547 -132 1094 C ATOM 2932 CE LYS A 387 28.582 -12.562 1.180 1.00150.36 C ANISOU 2932 CE LYS A 387 13488 28660 14981 -1223 -25 736 C ATOM 2933 NZ LYS A 387 29.355 -13.141 2.311 1.00157.11 N ANISOU 2933 NZ LYS A 387 14311 29422 15961 -1066 -23 558 N TER 2934 LYS A 387 HETATM 2935 C1 ERM A2001 -5.279 -20.621 23.228 1.00 71.20 C HETATM 2936 N1 ERM A2001 -5.767 -21.035 24.418 1.00 71.70 N HETATM 2937 O1 ERM A2001 -11.837 -16.865 19.965 1.00 71.53 O HETATM 2938 C10 ERM A2001 -9.680 -19.785 23.970 1.00 71.51 C HETATM 2939 C11 ERM A2001 -9.403 -20.411 25.209 1.00 71.68 C HETATM 2940 C12 ERM A2001 -8.079 -20.896 25.478 1.00 72.23 C HETATM 2941 C13 ERM A2001 -7.124 -20.726 24.524 1.00 72.39 C HETATM 2942 C14 ERM A2001 -7.402 -20.099 23.301 1.00 72.46 C HETATM 2943 C15 ERM A2001 -6.868 -16.917 19.089 1.00 66.56 C HETATM 2944 C16 ERM A2001 -11.589 -17.893 19.367 1.00 71.09 C HETATM 2945 C17 ERM A2001 -13.795 -17.992 18.167 1.00 64.24 C HETATM 2946 C18 ERM A2001 -14.741 -17.931 19.335 1.00 62.14 C HETATM 2947 C19 ERM A2001 -16.000 -16.150 20.437 1.00 65.68 C HETATM 2948 N2 ERM A2001 -7.721 -18.066 19.493 1.00 69.38 N HETATM 2949 C2 ERM A2001 -6.252 -20.018 22.492 1.00 71.13 C HETATM 2950 O2 ERM A2001 -13.762 -16.643 17.689 1.00 63.54 O HETATM 2951 C20 ERM A2001 -16.859 -15.036 19.817 1.00 68.65 C HETATM 2952 C21 ERM A2001 -17.252 -13.431 17.946 1.00 68.68 C HETATM 2953 C22 ERM A2001 -16.233 -12.666 17.129 1.00 68.63 C HETATM 2954 C23 ERM A2001 -14.980 -13.587 17.041 1.00 68.78 C HETATM 2955 C24 ERM A2001 -15.457 -14.858 17.768 1.00 67.79 C HETATM 2956 C25 ERM A2001 -14.427 -15.697 18.524 1.00 64.22 C HETATM 2957 C26 ERM A2001 -14.268 -18.981 17.116 1.00 62.81 C HETATM 2958 C27 ERM A2001 -15.364 -15.628 21.701 1.00 64.22 C HETATM 2959 C28 ERM A2001 -14.753 -16.660 22.630 1.00 61.94 C HETATM 2960 C29 ERM A2001 -13.409 -16.496 23.034 1.00 60.35 C HETATM 2961 C3 ERM A2001 -6.319 -19.424 21.114 1.00 71.27 C HETATM 2962 N3 ERM A2001 -12.463 -18.493 18.524 1.00 69.30 N HETATM 2963 O3 ERM A2001 -15.147 -18.879 19.977 1.00 60.81 O HETATM 2964 C30 ERM A2001 -12.800 -17.423 23.900 1.00 57.75 C HETATM 2965 C31 ERM A2001 -13.557 -18.487 24.409 1.00 57.84 C HETATM 2966 C32 ERM A2001 -14.910 -18.620 24.044 1.00 59.88 C HETATM 2967 C33 ERM A2001 -15.516 -17.727 23.143 1.00 60.10 C HETATM 2968 C4 ERM A2001 -7.553 -18.459 20.955 1.00 71.91 C HETATM 2969 N4 ERM A2001 -15.047 -16.631 19.463 1.00 63.61 N HETATM 2970 O4 ERM A2001 -17.845 -14.600 20.436 1.00 71.56 O HETATM 2971 C5 ERM A2001 -9.099 -17.646 19.053 1.00 71.08 C HETATM 2972 N5 ERM A2001 -16.541 -14.490 18.652 1.00 68.46 N HETATM 2973 O5 ERM A2001 -13.496 -14.900 19.173 1.00 63.18 O HETATM 2974 C6 ERM A2001 -10.197 -18.572 19.543 1.00 72.13 C HETATM 2975 C7 ERM A2001 -9.984 -19.123 20.930 1.00 73.25 C HETATM 2976 C8 ERM A2001 -8.843 -18.992 21.600 1.00 73.13 C HETATM 2977 C9 ERM A2001 -8.695 -19.603 22.985 1.00 72.79 C HETATM 2978 C1 OLB A2002 10.586 -5.804 15.946 1.00101.28 C HETATM 2979 C2 OLB A2002 9.411 -6.554 15.326 1.00 99.34 C HETATM 2980 C3 OLB A2002 8.353 -5.771 14.553 1.00 97.13 C HETATM 2981 C4 OLB A2002 7.041 -6.462 14.185 1.00 95.25 C HETATM 2982 C5 OLB A2002 6.349 -6.014 12.901 1.00 93.61 C HETATM 2983 O19 OLB A2002 10.348 -4.842 16.677 1.00102.55 O HETATM 2984 O20 OLB A2002 11.857 -6.419 15.959 1.00100.52 O HETATM 2985 C21 OLB A2002 13.057 -5.675 16.022 1.00 99.23 C HETATM 2986 C22 OLB A2002 14.212 -6.263 16.781 1.00 97.82 C HETATM 2987 O23 OLB A2002 14.469 -7.540 16.330 1.00 99.09 O HETATM 2988 C24 OLB A2002 15.438 -5.402 16.629 1.00 95.43 C HETATM 2989 O25 OLB A2002 16.663 -5.911 17.036 1.00 93.77 O HETATM 2990 C6 OLB A2002 5.498 -7.016 12.136 1.00 91.37 C HETATM 2991 C7 OLB A2002 4.310 -6.502 11.349 1.00 88.93 C HETATM 2992 O HOH A2004 21.837 -18.985 27.620 1.00 48.85 O HETATM 2993 O HOH A2005 17.109 -4.409 9.226 1.00 73.78 O HETATM 2994 O HOH A2006 -23.879 -21.900 6.501 1.00 60.81 O HETATM 2995 O HOH A2007 -18.349 -27.050 18.738 1.00 63.95 O HETATM 2996 O HOH A2008 17.518 -27.427 35.725 1.00 67.89 O HETATM 2997 O HOH A2009 18.249 -7.713 9.172 1.00 62.91 O HETATM 2998 O HOH A2010 -16.607 -19.419 6.202 1.00 72.30 O HETATM 2999 O HOH A2011 18.658 -18.117 19.891 1.00 56.03 O HETATM 3000 O HOH A2012 25.026 -24.459 38.981 1.00 51.12 O CONECT 645 1198 CONECT 1198 645 CONECT 2935 2936 2949 CONECT 2936 2935 2941 CONECT 2937 2944 CONECT 2938 2939 2977 CONECT 2939 2938 2940 CONECT 2940 2939 2941 CONECT 2941 2936 2940 2942 CONECT 2942 2941 2949 2977 CONECT 2943 2948 CONECT 2944 2937 2962 2974 CONECT 2945 2946 2950 2957 2962 CONECT 2946 2945 2963 2969 CONECT 2947 2951 2958 2969 CONECT 2948 2943 2968 2971 CONECT 2949 2935 2942 2961 CONECT 2950 2945 2956 CONECT 2951 2947 2970 2972 CONECT 2952 2953 2972 CONECT 2953 2952 2954 CONECT 2954 2953 2955 CONECT 2955 2954 2956 2972 CONECT 2956 2950 2955 2969 2973 CONECT 2957 2945 CONECT 2958 2947 2959 CONECT 2959 2958 2960 2967 CONECT 2960 2959 2964 CONECT 2961 2949 2968 CONECT 2962 2944 2945 CONECT 2963 2946 CONECT 2964 2960 2965 CONECT 2965 2964 2966 CONECT 2966 2965 2967 CONECT 2967 2959 2966 CONECT 2968 2948 2961 2976 CONECT 2969 2946 2947 2956 CONECT 2970 2951 CONECT 2971 2948 2974 CONECT 2972 2951 2952 2955 CONECT 2973 2956 CONECT 2974 2944 2971 2975 CONECT 2975 2974 2976 CONECT 2976 2968 2975 2977 CONECT 2977 2938 2942 2976 CONECT 2978 2979 2983 2984 CONECT 2979 2978 2980 CONECT 2980 2979 2981 CONECT 2981 2980 2982 CONECT 2982 2981 2990 CONECT 2983 2978 CONECT 2984 2978 2985 CONECT 2985 2984 2986 CONECT 2986 2985 2987 2988 CONECT 2987 2986 CONECT 2988 2986 2989 CONECT 2989 2988 CONECT 2990 2982 2991 CONECT 2991 2990 MASTER 350 0 2 18 0 0 5 6 2999 1 59 31 END