Browse entries in the PDBbind-CN Database
HEADER IMMUNE SYSTEM 10-MAY-18 6DDM TITLE CRYSTAL STRUCTURE ANALYSIS OF THE EPITOPE OF AN ANTI-MICA ANTIBODY COMPND MOL_ID: 1; COMPND 2 MOLECULE: ANTI-MICA FAB FRAGMENT LIGHT CHAIN CLONE 1D5; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: MHC CLASS I POLYPEPTIDE-RELATED SEQUENCE A; COMPND 7 CHAIN: C; COMPND 8 SYNONYM: MHC CLASS I POLYPEPTIDE-RELATED SEQUENCE A,ISOFORM CRA_C, COMPND 9 MICA,STRESS INDUCIBLE CLASS I HOMOLOG,CDNA FLJ60820,HIGHLY SIMILAR TO COMPND 10 HOMO SAPIENS MHC CLASS I POLYPEPTIDE-RELATED SEQUENCE A (MICA),MRNA; COMPND 11 ENGINEERED: YES; COMPND 12 MOL_ID: 3; COMPND 13 MOLECULE: ANTI-MICA FAB FRAGMENT HEAVY CHAIN CLONE 1D5; COMPND 14 CHAIN: B; COMPND 15 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 10090; SOURCE 4 STRAIN: BALB/C; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: 64B4; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PBR322; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 12 ORGANISM_COMMON: HUMAN; SOURCE 13 ORGANISM_TAXID: 9606; SOURCE 14 GENE: MICA, HCG_2001511; SOURCE 15 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PACGP67; SOURCE 19 MOL_ID: 3; SOURCE 20 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 21 ORGANISM_TAXID: 10090; SOURCE 22 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 23 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 24 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 25 EXPRESSION_SYSTEM_PLASMID: PBR322 KEYWDS FAB FRAGMENT-ANTIGEN COMPLEX, IMMUNOGLOBULIN DOMAIN, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR M.L.MATSUMOTO REVDAT 3 23-JAN-19 6DDM 1 JRNL REVDAT 2 05-DEC-18 6DDM 1 JRNL REVDAT 1 24-OCT-18 6DDM 0 JRNL AUTH T.N.LOMBANA,M.L.MATSUMOTO,A.M.BERKLEY,E.TOY,R.COOK,Y.GAN, JRNL AUTH 2 C.DU,P.SCHNIER,W.SANDOVAL,Z.YE,J.M.SCHARTNER,J.KIM,C.SPIESS JRNL TITL HIGH-RESOLUTION GLYCOSYLATION SITE-ENGINEERING METHOD JRNL TITL 2 IDENTIFIES MICA EPITOPE CRITICAL FOR SHEDDING INHIBITION JRNL TITL 3 ACTIVITY OF ANTI-MICA ANTIBODIES. JRNL REF MABS V. 11 75 2019 JRNL REFN ESSN 1942-0870 JRNL PMID 30307368 JRNL DOI 10.1080/19420862.2018.1532767 REMARK 2 REMARK 2 RESOLUTION. 1.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0155 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 3 NUMBER OF REFLECTIONS : 120157 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) : 0.189 REMARK 3 R VALUE (WORKING SET) : 0.188 REMARK 3 FREE R VALUE : 0.205 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900 REMARK 3 FREE R VALUE TEST SET COUNT : 6152 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.30 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.33 REMARK 3 REFLECTION IN BIN (WORKING SET) : 8651 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.81 REMARK 3 BIN R VALUE (WORKING SET) : 0.2880 REMARK 3 BIN FREE R VALUE SET COUNT : 385 REMARK 3 BIN FREE R VALUE : 0.2940 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3880 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 618 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.98 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.05000 REMARK 3 B22 (A**2) : -1.75000 REMARK 3 B33 (A**2) : 1.72000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -0.79000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.054 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.054 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.054 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.755 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.964 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4331 ; 0.007 ; 0.019 REMARK 3 BOND LENGTHS OTHERS (A): 3840 ; 0.002 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5977 ; 1.302 ; 1.944 REMARK 3 BOND ANGLES OTHERS (DEGREES): 8929 ; 0.863 ; 3.002 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 596 ; 6.296 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 151 ;34.965 ;24.371 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 651 ;11.366 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 11 ;12.958 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 679 ; 0.076 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5113 ; 0.005 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): 966 ; 0.002 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 3 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 1 A 214 REMARK 3 ORIGIN FOR THE GROUP (A): 74.8516 -2.0633 19.2172 REMARK 3 T TENSOR REMARK 3 T11: 0.0388 T22: 0.0556 REMARK 3 T33: 0.0127 T12: -0.0041 REMARK 3 T13: -0.0108 T23: 0.0160 REMARK 3 L TENSOR REMARK 3 L11: 0.4624 L22: 0.5312 REMARK 3 L33: 0.4295 L12: 0.3802 REMARK 3 L13: 0.3457 L23: 0.3051 REMARK 3 S TENSOR REMARK 3 S11: 0.0383 S12: -0.0258 S13: 0.0219 REMARK 3 S21: -0.0461 S22: -0.0361 S23: 0.0411 REMARK 3 S31: 0.0558 S32: -0.0747 S33: -0.0022 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : C 204 C 297 REMARK 3 ORIGIN FOR THE GROUP (A): 114.2970 18.0556 36.3747 REMARK 3 T TENSOR REMARK 3 T11: 0.0350 T22: 0.0764 REMARK 3 T33: 0.0119 T12: 0.0176 REMARK 3 T13: -0.0009 T23: 0.0124 REMARK 3 L TENSOR REMARK 3 L11: 2.9720 L22: 1.3050 REMARK 3 L33: 1.1877 L12: 1.1927 REMARK 3 L13: -1.0505 L23: -0.4553 REMARK 3 S TENSOR REMARK 3 S11: 0.0202 S12: -0.1718 S13: -0.1006 REMARK 3 S21: 0.0283 S22: 0.0125 S23: -0.0063 REMARK 3 S31: -0.0277 S32: 0.1019 S33: -0.0327 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 2 B 216 REMARK 3 ORIGIN FOR THE GROUP (A): 91.8976 -9.1348 17.1848 REMARK 3 T TENSOR REMARK 3 T11: 0.0312 T22: 0.0351 REMARK 3 T33: 0.0383 T12: 0.0106 REMARK 3 T13: 0.0225 T23: 0.0223 REMARK 3 L TENSOR REMARK 3 L11: 0.6721 L22: 0.5471 REMARK 3 L33: 0.4550 L12: 0.3638 REMARK 3 L13: 0.3246 L23: 0.3132 REMARK 3 S TENSOR REMARK 3 S11: 0.0212 S12: 0.0947 S13: -0.0189 REMARK 3 S21: -0.0854 S22: 0.0218 S23: -0.0950 REMARK 3 S31: -0.0124 S32: 0.0205 S33: -0.0431 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: U VALUES : WITH TLS ADDED HYDROGENS REMARK 3 HAVE BEEN ADDED IN THE RIDING POSITIONS REMARK 4 REMARK 4 6DDM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-MAY-18. REMARK 100 THE DEPOSITION ID IS D_1000234424. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 14-OCT-15 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 4.6 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 22-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.00 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX300-HS REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 126363 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.300 REMARK 200 RESOLUTION RANGE LOW (A) : 35.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 200 DATA REDUNDANCY : 3.500 REMARK 200 R MERGE (I) : 0.05900 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.32 REMARK 200 COMPLETENESS FOR SHELL (%) : 96.4 REMARK 200 DATA REDUNDANCY IN SHELL : 2.90 REMARK 200 R MERGE FOR SHELL (I) : 0.56000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHENIX REMARK 200 STARTING MODEL: 1F3D, 4M1G, 1HYR, 1NZ8 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 46.17 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE, PH 4.6, 25% PEG REMARK 280 4000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 25.08850 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLU C 215 REMARK 465 ALA C 216 REMARK 465 SER C 217 REMARK 465 GLU C 218 REMARK 465 GLY C 219 REMARK 465 ASN C 220 REMARK 465 GLU B 1 REMARK 465 LYS B 129 REMARK 465 SER B 130 REMARK 465 THR B 131 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LYS A 45 CG CD CE NZ REMARK 470 LYS A 126 CG CD CE NZ REMARK 470 GLN A 147 CG CD OE1 NE2 REMARK 470 LYS A 169 CG CD CE NZ REMARK 470 ASN C 210 CG OD1 ND2 REMARK 470 ARG C 233 CG CD NE CZ NH1 NH2 REMARK 470 ARG C 274 CG CD NE CZ NH1 NH2 REMARK 470 GLN C 278 CG CD OE1 NE2 REMARK 470 GLN B 3 CG CD OE1 NE2 REMARK 470 MET B 58 CG SD CE REMARK 470 LYS B 64 CG CD CE NZ REMARK 470 GLU B 85 CG CD OE1 OE2 REMARK 470 GLN B 192 CG CD OE1 NE2 REMARK 470 LYS B 201 CG CD CE NZ REMARK 470 ASN B 204 CG OD1 ND2 REMARK 470 LYS B 206 CG CD CE NZ REMARK 470 LYS B 214 CG CD CE NZ 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 THR A 51 -43.53 72.86 REMARK 500 ALA A 84 170.86 179.77 REMARK 500 VAL B 55 66.15 65.96 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH C 412 DISTANCE = 6.68 ANGSTROMS REMARK 525 HOH B 545 DISTANCE = 6.30 ANGSTROMS DBREF 6DDM A 1 214 PDB 6DDM 6DDM 1 214 DBREF 6DDM C 204 297 UNP Q96QC4 Q96QC4_HUMAN 204 297 DBREF 6DDM B 1 216 PDB 6DDM 6DDM 1 216 SEQRES 1 A 215 GLU ILE ILE LEU THR GLN SER PRO THR THR MET ALA ALA SEQRES 2 A 215 SER PRO GLY GLU LYS ILE THR ILE THR CYS SER ALA SER SEQRES 3 A 215 SER SER ILE SER SER HIS TYR LEU HIS TRP TYR GLN GLN SEQRES 4 A 215 LYS SER GLY PHE SER PRO LYS LEU LEU ILE TYR ARG THR SEQRES 5 A 215 SER ASN LEU ALA SER GLY VAL PRO ALA ARG PHE SER GLY SEQRES 6 A 215 SER GLY SER GLY THR SER TYR SER LEU THR ILE GLY THR SEQRES 7 A 215 MET GLU ALA GLU ASP VAL ALA THR TYR TYR CYS GLN GLN SEQRES 8 A 215 GLY SER SER LEU PRO LEU THR PHE GLY ALA GLY THR LYS SEQRES 9 A 215 LEU GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 A 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 A 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 A 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 A 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 A 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 A 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 A 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 A 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 C 94 THR VAL PRO PRO MET VAL ASN VAL THR ARG SER GLU ALA SEQRES 2 C 94 SER GLU GLY ASN ILE THR VAL THR CYS ARG ALA SER SER SEQRES 3 C 94 PHE TYR PRO ARG ASN ILE ILE LEU THR TRP ARG GLN ASP SEQRES 4 C 94 GLY VAL SER LEU SER HIS ASP THR GLN GLN TRP GLY ASP SEQRES 5 C 94 VAL LEU PRO ASP GLY ASN GLY THR TYR GLN THR TRP VAL SEQRES 6 C 94 ALA THR ARG ILE CYS ARG GLY GLU GLU GLN ARG PHE THR SEQRES 7 C 94 CYS TYR MET GLU HIS SER GLY ASN HIS SER THR HIS PRO SEQRES 8 C 94 VAL PRO SER SEQRES 1 B 220 GLU ILE GLN LEU GLN GLN SER GLY PRO GLU LEU VAL LYS SEQRES 2 B 220 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 B 220 TYR ALA PHE THR SER GLN ASN ILE TYR TRP VAL LYS GLN SEQRES 4 B 220 SER HIS GLY LYS SER LEU GLU TRP ILE GLY TYR ILE GLU SEQRES 5 B 220 PRO TYR ASN VAL VAL PRO MET TYR ASN PRO LYS PHE LYS SEQRES 6 B 220 GLY LYS ALA THR LEU THR VAL ASP LYS SER SER SER SER SEQRES 7 B 220 ALA TYR ILE HIS LEU ASN SER LEU THR SER GLU ASP SER SEQRES 8 B 220 ALA ILE TYR TYR CYS ALA ARG SER GLY SER SER ASN PHE SEQRES 9 B 220 ASP TYR TRP GLY GLN GLY THR THR LEU THR VAL SER SER SEQRES 10 B 220 ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SEQRES 11 B 220 SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY SEQRES 12 B 220 CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SEQRES 13 B 220 SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR SEQRES 14 B 220 PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SEQRES 15 B 220 SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR SEQRES 16 B 220 GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN SEQRES 17 B 220 THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS FORMUL 4 HOH *618(H2 O) HELIX 1 AA1 SER A 29 HIS A 31 5 3 HELIX 2 AA2 GLU A 79 VAL A 83 5 5 HELIX 3 AA3 SER A 121 LYS A 126 1 6 HELIX 4 AA4 LYS A 183 LYS A 188 1 6 HELIX 5 AA5 SER C 247 GLN C 251 5 5 HELIX 6 AA6 GLU C 276 GLN C 278 5 3 HELIX 7 AA7 ALA B 28 GLN B 32 5 5 HELIX 8 AA8 PRO B 61 LYS B 64 5 4 HELIX 9 AA9 THR B 83 SER B 87 5 5 HELIX 10 AB1 SER B 156 ALA B 158 5 3 HELIX 11 AB2 SER B 187 LEU B 189 5 3 HELIX 12 AB3 LYS B 201 ASN B 204 5 4 SHEET 1 AA1 3 LEU A 4 SER A 7 0 SHEET 2 AA1 3 ILE A 19 ILE A 28 -1 O SER A 24 N THR A 5 SHEET 3 AA1 3 PHE A 62 ILE A 75 -1 O TYR A 71 N CYS A 23 SHEET 1 AA2 6 THR A 10 ALA A 13 0 SHEET 2 AA2 6 THR A 102 ILE A 106 1 O GLU A 105 N MET A 11 SHEET 3 AA2 6 ALA A 84 GLN A 90 -1 N ALA A 84 O LEU A 104 SHEET 4 AA2 6 LEU A 33 GLN A 38 -1 N GLN A 38 O THR A 85 SHEET 5 AA2 6 LYS A 45 TYR A 49 -1 O ILE A 48 N TRP A 35 SHEET 6 AA2 6 ASN A 53 LEU A 54 -1 O ASN A 53 N TYR A 49 SHEET 1 AA3 4 THR A 10 ALA A 13 0 SHEET 2 AA3 4 THR A 102 ILE A 106 1 O GLU A 105 N MET A 11 SHEET 3 AA3 4 ALA A 84 GLN A 90 -1 N ALA A 84 O LEU A 104 SHEET 4 AA3 4 THR A 97 PHE A 98 -1 O THR A 97 N GLN A 90 SHEET 1 AA4 4 SER A 114 PHE A 118 0 SHEET 2 AA4 4 THR A 129 PHE A 139 -1 O LEU A 135 N PHE A 116 SHEET 3 AA4 4 TYR A 173 SER A 182 -1 O LEU A 175 N LEU A 136 SHEET 4 AA4 4 SER A 159 VAL A 163 -1 N GLN A 160 O THR A 178 SHEET 1 AA5 4 ALA A 153 LEU A 154 0 SHEET 2 AA5 4 LYS A 145 VAL A 150 -1 N VAL A 150 O ALA A 153 SHEET 3 AA5 4 VAL A 191 THR A 197 -1 O GLU A 195 N GLN A 147 SHEET 4 AA5 4 VAL A 205 ASN A 210 -1 O VAL A 205 N VAL A 196 SHEET 1 AA6 4 MET C 208 ARG C 213 0 SHEET 2 AA6 4 THR C 222 PHE C 230 -1 O ARG C 226 N ASN C 210 SHEET 3 AA6 4 TYR C 264 ARG C 271 -1 O VAL C 268 N CYS C 225 SHEET 4 AA6 4 GLN C 252 TRP C 253 -1 N GLN C 252 O ALA C 269 SHEET 1 AA7 4 MET C 208 ARG C 213 0 SHEET 2 AA7 4 THR C 222 PHE C 230 -1 O ARG C 226 N ASN C 210 SHEET 3 AA7 4 TYR C 264 ARG C 271 -1 O VAL C 268 N CYS C 225 SHEET 4 AA7 4 LEU C 257 PRO C 258 -1 N LEU C 257 O GLN C 265 SHEET 1 AA8 4 VAL C 244 SER C 245 0 SHEET 2 AA8 4 ILE C 236 GLN C 241 -1 N GLN C 241 O VAL C 244 SHEET 3 AA8 4 PHE C 280 HIS C 286 -1 O TYR C 283 N THR C 238 SHEET 4 AA8 4 ASN C 289 PRO C 294 -1 O HIS C 293 N CYS C 282 SHEET 1 AA9 4 GLN B 3 GLN B 6 0 SHEET 2 AA9 4 VAL B 18 SER B 25 -1 O LYS B 23 N GLN B 5 SHEET 3 AA9 4 SER B 77 LEU B 82 -1 O LEU B 82 N VAL B 18 SHEET 4 AA9 4 ALA B 67 ASP B 72 -1 N THR B 70 O TYR B 79 SHEET 1 AB1 6 GLU B 10 VAL B 12 0 SHEET 2 AB1 6 THR B 107 VAL B 111 1 O THR B 110 N GLU B 10 SHEET 3 AB1 6 ALA B 88 ARG B 94 -1 N ALA B 88 O LEU B 109 SHEET 4 AB1 6 ILE B 34 GLN B 39 -1 N TYR B 35 O ALA B 93 SHEET 5 AB1 6 LEU B 45 GLU B 52 -1 O GLU B 46 N LYS B 38 SHEET 6 AB1 6 VAL B 56 TYR B 59 -1 O MET B 58 N TYR B 50 SHEET 1 AB2 4 GLU B 10 VAL B 12 0 SHEET 2 AB2 4 THR B 107 VAL B 111 1 O THR B 110 N GLU B 10 SHEET 3 AB2 4 ALA B 88 ARG B 94 -1 N ALA B 88 O LEU B 109 SHEET 4 AB2 4 TYR B 102 TRP B 103 -1 O TYR B 102 N ARG B 94 SHEET 1 AB3 4 SER B 120 LEU B 124 0 SHEET 2 AB3 4 THR B 135 TYR B 145 -1 O LEU B 141 N PHE B 122 SHEET 3 AB3 4 TYR B 176 PRO B 185 -1 O LEU B 178 N VAL B 142 SHEET 4 AB3 4 VAL B 163 THR B 165 -1 N HIS B 164 O VAL B 181 SHEET 1 AB4 4 SER B 120 LEU B 124 0 SHEET 2 AB4 4 THR B 135 TYR B 145 -1 O LEU B 141 N PHE B 122 SHEET 3 AB4 4 TYR B 176 PRO B 185 -1 O LEU B 178 N VAL B 142 SHEET 4 AB4 4 VAL B 169 LEU B 170 -1 N VAL B 169 O SER B 177 SHEET 1 AB5 3 THR B 151 TRP B 154 0 SHEET 2 AB5 3 ILE B 195 HIS B 200 -1 O ASN B 197 N SER B 153 SHEET 3 AB5 3 THR B 205 LYS B 210 -1 O VAL B 207 N VAL B 198 SSBOND 1 CYS A 23 CYS A 88 1555 1555 2.08 SSBOND 2 CYS A 134 CYS A 194 1555 1555 2.04 SSBOND 3 CYS A 214 CYS B 216 1555 1555 2.05 SSBOND 4 CYS C 225 CYS C 282 1555 1555 2.05 SSBOND 5 CYS B 22 CYS B 92 1555 1555 2.02 SSBOND 6 CYS B 140 CYS B 196 1555 1555 2.02 CISPEP 1 SER A 7 PRO A 8 0 -5.29 CISPEP 2 SER A 7 PRO A 8 0 -7.84 CISPEP 3 LEU A 94 PRO A 95 0 -0.65 CISPEP 4 TYR A 140 PRO A 141 0 1.93 CISPEP 5 TYR C 231 PRO C 232 0 2.40 CISPEP 6 PHE B 146 PRO B 147 0 -7.14 CISPEP 7 GLU B 148 PRO B 149 0 2.09 CRYST1 58.690 50.177 88.633 90.00 90.85 90.00 P 1 21 1 2 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 0.017039 0.000000 0.000252 0.00000 SCALE2 0.000000 0.019929 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011284 0.00000 ATOM 1 N GLU A 1 90.928 -0.064 46.215 1.00 28.86 N ANISOU 1 N GLU A 1 3958 3789 3220 -635 -385 363 N ATOM 2 CA GLU A 1 91.191 0.847 45.060 1.00 27.70 C ANISOU 2 CA GLU A 1 3749 3645 3130 -544 -331 330 C ATOM 3 C GLU A 1 90.156 1.975 44.993 1.00 26.67 C ANISOU 3 C GLU A 1 3578 3581 2977 -548 -249 292 C ATOM 4 O GLU A 1 89.080 1.874 45.589 1.00 27.21 O ANISOU 4 O GLU A 1 3656 3693 2989 -614 -228 285 O ATOM 5 CB GLU A 1 91.217 0.048 43.742 1.00 28.24 C ANISOU 5 CB GLU A 1 3810 3677 3243 -487 -348 333 C ATOM 6 CG GLU A 1 89.956 -0.747 43.408 1.00 28.98 C ANISOU 6 CG GLU A 1 3919 3789 3302 -522 -341 338 C ATOM 7 CD GLU A 1 90.037 -1.487 42.073 1.00 29.43 C ANISOU 7 CD GLU A 1 3967 3810 3404 -462 -356 338 C ATOM 8 OE1 GLU A 1 89.000 -1.608 41.387 1.00 30.69 O ANISOU 8 OE1 GLU A 1 4114 3995 3551 -461 -322 327 O ATOM 9 OE2 GLU A 1 91.134 -1.958 41.688 1.00 30.85 O ANISOU 9 OE2 GLU A 1 4152 3936 3634 -417 -403 346 O ATOM 10 N ILE A 2 90.485 3.058 44.285 1.00 24.49 N ANISOU 10 N ILE A 2 3252 3308 2743 -481 -205 264 N ATOM 11 CA ILE A 2 89.488 4.087 43.973 1.00 23.53 C ANISOU 11 CA ILE A 2 3088 3237 2615 -470 -135 225 C ATOM 12 C ILE A 2 88.513 3.506 42.950 1.00 22.32 C ANISOU 12 C ILE A 2 2925 3090 2465 -455 -122 221 C ATOM 13 O ILE A 2 88.916 3.101 41.853 1.00 22.64 O ANISOU 13 O ILE A 2 2961 3094 2545 -400 -136 230 O ATOM 14 CB ILE A 2 90.122 5.398 43.457 1.00 23.12 C ANISOU 14 CB ILE A 2 2993 3183 2610 -405 -101 201 C ATOM 15 CG1 ILE A 2 90.932 6.038 44.591 1.00 23.56 C ANISOU 15 CG1 ILE A 2 3056 3240 2656 -429 -110 202 C ATOM 16 CG2 ILE A 2 89.041 6.358 42.956 1.00 22.94 C ANISOU 16 CG2 ILE A 2 2927 3200 2589 -387 -41 163 C ATOM 17 CD1 ILE A 2 91.626 7.335 44.243 1.00 23.56 C ANISOU 17 CD1 ILE A 2 3019 3236 2698 -374 -80 181 C ATOM 18 N ILE A 3 87.235 3.440 43.328 1.00 21.53 N ANISOU 18 N ILE A 3 2823 3037 2320 -507 -95 204 N ATOM 19 CA ILE A 3 86.178 2.962 42.447 1.00 21.08 C ANISOU 19 CA ILE A 3 2755 2993 2264 -499 -79 197 C ATOM 20 C ILE A 3 85.562 4.170 41.750 1.00 19.73 C ANISOU 20 C ILE A 3 2528 2849 2119 -451 -23 155 C ATOM 21 O ILE A 3 85.227 5.161 42.406 1.00 19.52 O ANISOU 21 O ILE A 3 2476 2860 2082 -468 12 122 O ATOM 22 CB ILE A 3 85.095 2.173 43.230 1.00 22.02 C ANISOU 22 CB ILE A 3 2899 3149 2320 -587 -82 200 C ATOM 23 CG1 ILE A 3 85.728 0.959 43.926 1.00 22.79 C ANISOU 23 CG1 ILE A 3 3060 3211 2389 -638 -149 247 C ATOM 24 CG2 ILE A 3 83.944 1.765 42.315 1.00 22.12 C ANISOU 24 CG2 ILE A 3 2894 3178 2334 -578 -63 187 C ATOM 25 CD1 ILE A 3 86.318 -0.085 42.998 1.00 23.04 C ANISOU 25 CD1 ILE A 3 3115 3181 2459 -594 -201 279 C ATOM 26 N LEU A 4 85.443 4.083 40.424 1.00 18.78 N ANISOU 26 N LEU A 4 2392 2708 2036 -393 -19 155 N ATOM 27 CA LEU A 4 84.832 5.132 39.628 1.00 18.29 C ANISOU 27 CA LEU A 4 2284 2664 2003 -348 22 121 C ATOM 28 C LEU A 4 83.480 4.620 39.163 1.00 18.13 C ANISOU 28 C LEU A 4 2253 2668 1966 -365 34 108 C ATOM 29 O LEU A 4 83.402 3.583 38.511 1.00 18.22 O ANISOU 29 O LEU A 4 2287 2658 1977 -361 10 132 O ATOM 30 CB LEU A 4 85.714 5.468 38.430 1.00 17.64 C ANISOU 30 CB LEU A 4 2194 2540 1969 -275 17 131 C ATOM 31 CG LEU A 4 87.106 6.006 38.761 1.00 17.54 C ANISOU 31 CG LEU A 4 2186 2502 1978 -253 6 141 C ATOM 32 CD1 LEU A 4 87.867 6.246 37.466 1.00 17.20 C ANISOU 32 CD1 LEU A 4 2133 2424 1978 -190 5 148 C ATOM 33 CD2 LEU A 4 87.054 7.279 39.591 1.00 17.51 C ANISOU 33 CD2 LEU A 4 2158 2525 1971 -263 35 114 C ATOM 34 N THR A 5 82.421 5.349 39.512 1.00 18.51 N ANISOU 34 N THR A 5 2265 2763 2005 -383 71 66 N ATOM 35 CA THR A 5 81.059 4.964 39.174 1.00 18.65 C ANISOU 35 CA THR A 5 2265 2812 2010 -404 85 45 C ATOM 36 C THR A 5 80.525 5.916 38.116 1.00 18.30 C ANISOU 36 C THR A 5 2178 2766 2012 -342 106 15 C ATOM 37 O THR A 5 80.381 7.117 38.369 1.00 18.16 O ANISOU 37 O THR A 5 2123 2763 2014 -324 129 -22 O ATOM 38 CB THR A 5 80.157 5.004 40.415 1.00 19.25 C ANISOU 38 CB THR A 5 2328 2946 2039 -480 110 11 C ATOM 39 OG1 THR A 5 80.648 4.059 41.368 1.00 19.88 O ANISOU 39 OG1 THR A 5 2459 3025 2071 -545 84 46 O ATOM 40 CG2 THR A 5 78.707 4.678 40.062 1.00 19.56 C ANISOU 40 CG2 THR A 5 2340 3023 2069 -501 129 -19 C ATOM 41 N GLN A 6 80.232 5.368 36.944 1.00 18.45 N ANISOU 41 N GLN A 6 2201 2762 2046 -311 92 31 N ATOM 42 CA GLN A 6 79.762 6.167 35.819 1.00 18.76 C ANISOU 42 CA GLN A 6 2208 2792 2127 -254 101 11 C ATOM 43 C GLN A 6 78.252 6.099 35.704 1.00 19.97 C ANISOU 43 C GLN A 6 2328 2983 2276 -273 116 -26 C ATOM 44 O GLN A 6 77.663 5.019 35.845 1.00 20.43 O ANISOU 44 O GLN A 6 2402 3059 2303 -316 110 -17 O ATOM 45 CB GLN A 6 80.423 5.718 34.524 1.00 18.06 C ANISOU 45 CB GLN A 6 2145 2657 2059 -207 78 47 C ATOM 46 CG GLN A 6 81.890 6.106 34.466 1.00 17.52 C ANISOU 46 CG GLN A 6 2094 2554 2008 -178 70 70 C ATOM 47 CD GLN A 6 82.512 5.868 33.117 1.00 17.34 C ANISOU 47 CD GLN A 6 2087 2493 2008 -132 55 94 C ATOM 48 OE1 GLN A 6 83.391 5.019 32.969 1.00 17.37 O ANISOU 48 OE1 GLN A 6 2120 2473 2008 -131 36 121 O ATOM 49 NE2 GLN A 6 82.074 6.617 32.123 1.00 17.14 N ANISOU 49 NE2 GLN A 6 2043 2462 2007 -95 62 82 N ATOM 50 N ASER A 7 77.629 7.252 35.464 0.50 20.55 N ANISOU 50 N ASER A 7 2356 3069 2385 -242 132 -68 N ATOM 51 N BSER A 7 77.639 7.253 35.436 0.50 20.58 N ANISOU 51 N BSER A 7 2360 3070 2389 -241 131 -68 N ATOM 52 CA ASER A 7 76.184 7.336 35.277 0.50 21.31 C ANISOU 52 CA ASER A 7 2410 3198 2489 -250 143 -112 C ATOM 53 CA BSER A 7 76.193 7.368 35.283 0.50 21.37 C ANISOU 53 CA BSER A 7 2417 3205 2498 -250 143 -113 C ATOM 54 C ASER A 7 75.881 8.301 34.128 0.50 21.56 C ANISOU 54 C ASER A 7 2415 3201 2575 -184 131 -127 C ATOM 55 C BSER A 7 75.895 8.303 34.108 0.50 21.57 C ANISOU 55 C BSER A 7 2417 3202 2578 -183 131 -126 C ATOM 56 O ASER A 7 76.590 9.300 33.960 0.50 21.41 O ANISOU 56 O ASER A 7 2394 3155 2586 -145 127 -126 O ATOM 57 O BSER A 7 76.622 9.282 33.903 0.50 21.34 O ANISOU 57 O BSER A 7 2388 3145 2578 -143 126 -123 O ATOM 58 CB ASER A 7 75.486 7.774 36.566 0.50 21.86 C ANISOU 58 CB ASER A 7 2440 3324 2542 -299 175 -168 C ATOM 59 CB BSER A 7 75.561 7.910 36.561 0.50 21.96 C ANISOU 59 CB BSER A 7 2452 3334 2559 -293 175 -169 C ATOM 60 OG ASER A 7 76.020 8.982 37.073 0.50 22.16 O ANISOU 60 OG ASER A 7 2459 3358 2603 -277 186 -192 O ATOM 61 OG BSER A 7 74.148 7.793 36.518 0.50 22.75 O ANISOU 61 OG BSER A 7 2508 3474 2662 -313 189 -217 O ATOM 62 N PRO A 8 74.869 7.983 33.296 1.00 22.05 N ANISOU 62 N PRO A 8 2461 3266 2650 -173 121 -138 N ATOM 63 CA PRO A 8 74.066 6.743 33.290 1.00 22.58 C ANISOU 63 CA PRO A 8 2535 3359 2685 -217 122 -133 C ATOM 64 C PRO A 8 74.895 5.585 32.690 1.00 23.04 C ANISOU 64 C PRO A 8 2653 3383 2718 -217 100 -70 C ATOM 65 O PRO A 8 75.968 5.829 32.143 1.00 23.12 O ANISOU 65 O PRO A 8 2690 3351 2742 -179 87 -37 O ATOM 66 CB PRO A 8 72.881 7.107 32.400 1.00 22.72 C ANISOU 66 CB PRO A 8 2512 3379 2740 -186 112 -166 C ATOM 67 CG PRO A 8 73.445 8.087 31.437 1.00 22.55 C ANISOU 67 CG PRO A 8 2497 3309 2763 -121 90 -152 C ATOM 68 CD PRO A 8 74.476 8.877 32.186 1.00 22.21 C ANISOU 68 CD PRO A 8 2459 3258 2722 -115 102 -151 C ATOM 69 N ATHR A 9 74.406 4.356 32.840 0.50 23.42 N ANISOU 69 N ATHR A 9 2719 3448 2731 -263 97 -57 N ATOM 70 N BTHR A 9 74.409 4.349 32.789 0.50 23.31 N ANISOU 70 N BTHR A 9 2706 3433 2718 -262 96 -56 N ATOM 71 CA ATHR A 9 75.047 3.174 32.267 0.50 23.42 C ANISOU 71 CA ATHR A 9 2772 3415 2712 -265 71 -5 C ATOM 72 CA BTHR A 9 75.091 3.200 32.174 0.50 23.20 C ANISOU 72 CA BTHR A 9 2744 3383 2686 -260 70 -3 C ATOM 73 C ATHR A 9 74.936 3.220 30.754 0.50 23.26 C ANISOU 73 C ATHR A 9 2756 3361 2722 -211 53 8 C ATOM 74 C BTHR A 9 74.922 3.215 30.658 0.50 22.91 C ANISOU 74 C BTHR A 9 2712 3315 2680 -208 52 9 C ATOM 75 O ATHR A 9 75.858 2.847 30.023 0.50 22.78 O ANISOU 75 O ATHR A 9 2730 3260 2664 -183 35 45 O ATOM 76 O BTHR A 9 75.844 2.886 29.905 0.50 22.29 O ANISOU 76 O BTHR A 9 2669 3197 2606 -179 35 45 O ATOM 77 CB ATHR A 9 74.362 1.887 32.762 0.50 23.89 C ANISOU 77 CB ATHR A 9 2848 3500 2728 -330 68 2 C ATOM 78 CB BTHR A 9 74.560 1.867 32.727 0.50 23.76 C ANISOU 78 CB BTHR A 9 2838 3477 2712 -326 65 8 C ATOM 79 OG1ATHR A 9 74.251 1.920 34.188 0.50 24.43 O ANISOU 79 OG1ATHR A 9 2911 3610 2763 -391 87 -16 O ATOM 80 OG1BTHR A 9 73.128 1.869 32.696 0.50 24.30 O ANISOU 80 OG1BTHR A 9 2866 3587 2780 -349 79 -31 O ATOM 81 CG2ATHR A 9 75.150 0.658 32.345 0.50 23.74 C ANISOU 81 CG2ATHR A 9 2887 3442 2693 -333 36 54 C ATOM 82 CG2BTHR A 9 75.036 1.660 34.155 0.50 24.05 C ANISOU 82 CG2BTHR A 9 2892 3535 2711 -383 73 13 C ATOM 83 N ATHR A 10 73.784 3.689 30.294 0.50 23.54 N ANISOU 83 N ATHR A 10 2752 3413 2779 -198 56 -26 N ATOM 84 N BTHR A 10 73.727 3.591 30.218 0.50 23.04 N ANISOU 84 N BTHR A 10 2690 3350 2715 -199 54 -24 N ATOM 85 CA ATHR A 10 73.531 3.835 28.886 0.50 23.80 C ANISOU 85 CA ATHR A 10 2787 3417 2840 -152 35 -16 C ATOM 86 CA BTHR A 10 73.467 3.806 28.812 0.50 23.24 C ANISOU 86 CA BTHR A 10 2715 3345 2769 -152 34 -16 C ATOM 87 C ATHR A 10 72.544 4.974 28.699 0.50 24.18 C ANISOU 87 C ATHR A 10 2782 3479 2928 -128 37 -63 C ATOM 88 C BTHR A 10 72.570 5.024 28.682 0.50 23.81 C ANISOU 88 C BTHR A 10 2734 3430 2881 -126 36 -63 C ATOM 89 O ATHR A 10 71.731 5.254 29.581 0.50 24.79 O ANISOU 89 O ATHR A 10 2816 3597 3006 -155 56 -108 O ATOM 90 O BTHR A 10 71.831 5.367 29.605 0.50 24.38 O ANISOU 90 O BTHR A 10 2764 3543 2957 -152 56 -108 O ATOM 91 CB ATHR A 10 72.965 2.537 28.288 0.50 24.04 C ANISOU 91 CB ATHR A 10 2840 3447 2849 -173 20 2 C ATOM 92 CB BTHR A 10 72.772 2.599 28.153 0.50 23.23 C ANISOU 92 CB BTHR A 10 2731 3346 2750 -170 19 -2 C ATOM 93 OG1ATHR A 10 72.561 2.771 26.937 0.50 24.40 O ANISOU 93 OG1ATHR A 10 2883 3469 2920 -132 0 6 O ATOM 94 OG1BTHR A 10 71.405 2.539 28.577 0.50 23.83 O ANISOU 94 OG1BTHR A 10 2765 3465 2825 -201 29 -43 O ATOM 95 CG2ATHR A 10 71.779 2.044 29.105 0.50 24.51 C ANISOU 95 CG2ATHR A 10 2870 3556 2887 -228 34 -29 C ATOM 96 CG2BTHR A 10 73.487 1.297 28.511 0.50 23.04 C ANISOU 96 CG2BTHR A 10 2756 3312 2688 -204 12 36 C ATOM 97 N AMET A 11 72.623 5.650 27.564 0.50 24.28 N ANISOU 97 N AMET A 11 2797 3456 2973 -78 15 -55 N ATOM 98 N BMET A 11 72.642 5.693 27.544 0.50 24.20 N ANISOU 98 N BMET A 11 2787 3444 2963 -77 14 -55 N ATOM 99 CA AMET A 11 71.677 6.712 27.285 0.50 24.91 C ANISOU 99 CA AMET A 11 2829 3538 3096 -50 3 -97 C ATOM 100 CA BMET A 11 71.714 6.770 27.276 0.50 25.05 C ANISOU 100 CA BMET A 11 2847 3554 3116 -49 2 -97 C ATOM 101 C AMET A 11 71.610 6.976 25.794 0.50 24.70 C ANISOU 101 C AMET A 11 2822 3469 3092 -9 -33 -74 C ATOM 102 C BMET A 11 71.618 6.996 25.784 0.50 24.79 C ANISOU 102 C BMET A 11 2835 3481 3105 -8 -33 -74 C ATOM 103 O AMET A 11 72.618 6.871 25.093 0.50 23.81 O ANISOU 103 O AMET A 11 2756 3324 2968 7 -41 -31 O ATOM 104 O BMET A 11 72.616 6.878 25.070 0.50 23.90 O ANISOU 104 O BMET A 11 2767 3334 2979 7 -42 -30 O ATOM 105 CB AMET A 11 72.066 7.987 28.030 0.50 25.69 C ANISOU 105 CB AMET A 11 2902 3638 3222 -34 14 -125 C ATOM 106 CB BMET A 11 72.142 8.055 27.983 0.50 26.13 C ANISOU 106 CB BMET A 11 2960 3690 3280 -31 12 -123 C ATOM 107 CG AMET A 11 70.959 9.029 28.102 0.50 26.64 C ANISOU 107 CG AMET A 11 2961 3768 3392 -13 3 -185 C ATOM 108 CG BMET A 11 71.194 9.223 27.746 0.50 27.27 C ANISOU 108 CG BMET A 11 3053 3831 3479 2 -7 -173 C ATOM 109 SD AMET A 11 69.440 8.416 28.861 0.50 28.02 S ANISOU 109 SD AMET A 11 3078 4007 3562 -58 25 -246 S ATOM 110 SD BMET A 11 71.017 10.307 29.175 0.50 29.06 S ANISOU 110 SD BMET A 11 3223 4089 3730 -5 19 -238 S ATOM 111 CE AMET A 11 69.990 8.034 30.522 0.50 27.82 C ANISOU 111 CE AMET A 11 3054 4028 3486 -118 74 -256 C ATOM 112 CE BMET A 11 70.071 9.272 30.289 0.50 28.98 C ANISOU 112 CE BMET A 11 3178 4151 3682 -72 58 -278 C ATOM 113 N ALA A 12 70.405 7.298 25.327 1.00 24.94 N ANISOU 113 N ALA A 12 2817 3503 3155 5 -55 -106 N ATOM 114 CA ALA A 12 70.148 7.664 23.944 1.00 25.28 C ANISOU 114 CA ALA A 12 2876 3507 3223 40 -96 -89 C ATOM 115 C ALA A 12 69.921 9.172 23.950 1.00 25.39 C ANISOU 115 C ALA A 12 2857 3501 3290 77 -119 -121 C ATOM 116 O ALA A 12 69.120 9.678 24.745 1.00 27.49 O ANISOU 116 O ALA A 12 3065 3793 3587 76 -113 -177 O ATOM 117 CB ALA A 12 68.932 6.928 23.411 1.00 25.78 C ANISOU 117 CB ALA A 12 2922 3584 3287 30 -113 -102 C ATOM 118 N ALA A 13 70.640 9.882 23.088 1.00 24.04 N ANISOU 118 N ALA A 13 2722 3283 3129 105 -147 -87 N ATOM 119 CA ALA A 13 70.502 11.322 22.917 1.00 23.44 C ANISOU 119 CA ALA A 13 2627 3176 3105 141 -181 -107 C ATOM 120 C ALA A 13 69.965 11.621 21.522 1.00 23.02 C ANISOU 120 C ALA A 13 2593 3081 3073 164 -239 -89 C ATOM 121 O ALA A 13 70.322 10.941 20.567 1.00 22.44 O ANISOU 121 O ALA A 13 2569 2993 2964 155 -245 -43 O ATOM 122 CB ALA A 13 71.854 11.978 23.094 1.00 23.43 C ANISOU 122 CB ALA A 13 2659 3152 3092 147 -170 -79 C ATOM 123 N SER A 14 69.124 12.642 21.385 1.00 22.72 N ANISOU 123 N SER A 14 2518 3021 3095 194 -284 -127 N ATOM 124 CA SER A 14 68.689 13.079 20.060 1.00 23.01 C ANISOU 124 CA SER A 14 2580 3009 3154 215 -349 -105 C ATOM 125 C SER A 14 69.824 13.803 19.356 1.00 22.31 C ANISOU 125 C SER A 14 2553 2873 3051 221 -371 -53 C ATOM 126 O SER A 14 70.694 14.369 20.028 1.00 21.45 O ANISOU 126 O SER A 14 2446 2764 2941 222 -346 -52 O ATOM 127 CB SER A 14 67.473 14.004 20.141 1.00 24.08 C ANISOU 127 CB SER A 14 2655 3127 3366 248 -401 -164 C ATOM 128 OG SER A 14 66.337 13.299 20.592 1.00 25.17 O ANISOU 128 OG SER A 14 2737 3310 3517 239 -385 -213 O ATOM 129 N PRO A 15 69.836 13.791 18.006 1.00 22.27 N ANISOU 129 N PRO A 15 2598 2831 3032 220 -416 -9 N ATOM 130 CA PRO A 15 70.818 14.591 17.274 1.00 22.13 C ANISOU 130 CA PRO A 15 2639 2769 3000 219 -441 37 C ATOM 131 C PRO A 15 70.727 16.057 17.686 1.00 22.11 C ANISOU 131 C PRO A 15 2613 2730 3056 247 -482 12 C ATOM 132 O PRO A 15 69.626 16.596 17.779 1.00 22.07 O ANISOU 132 O PRO A 15 2564 2710 3113 274 -529 -31 O ATOM 133 CB PRO A 15 70.397 14.418 15.808 1.00 22.84 C ANISOU 133 CB PRO A 15 2775 2826 3076 212 -496 73 C ATOM 134 CG PRO A 15 69.680 13.122 15.788 1.00 22.81 C ANISOU 134 CG PRO A 15 2752 2861 3055 202 -472 60 C ATOM 135 CD PRO A 15 68.938 13.074 17.087 1.00 22.63 C ANISOU 135 CD PRO A 15 2653 2875 3072 216 -446 -2 C ATOM 136 N GLY A 16 71.871 16.668 17.983 1.00 21.49 N ANISOU 136 N GLY A 16 2560 2641 2963 241 -463 32 N ATOM 137 CA GLY A 16 71.917 18.065 18.404 1.00 21.67 C ANISOU 137 CA GLY A 16 2567 2628 3040 265 -500 11 C ATOM 138 C GLY A 16 71.681 18.317 19.880 1.00 21.72 C ANISOU 138 C GLY A 16 2503 2666 3083 282 -463 -52 C ATOM 139 O GLY A 16 71.717 19.467 20.324 1.00 22.50 O ANISOU 139 O GLY A 16 2582 2737 3229 304 -491 -78 O ATOM 140 N GLU A 17 71.421 17.261 20.644 1.00 21.00 N ANISOU 140 N GLU A 17 2376 2634 2969 268 -404 -78 N ATOM 141 CA GLU A 17 71.150 17.373 22.069 1.00 21.55 C ANISOU 141 CA GLU A 17 2382 2744 3063 273 -363 -139 C ATOM 142 C GLU A 17 72.457 17.556 22.841 1.00 20.28 C ANISOU 142 C GLU A 17 2240 2595 2871 257 -315 -121 C ATOM 143 O GLU A 17 73.478 16.945 22.507 1.00 19.37 O ANISOU 143 O GLU A 17 2175 2485 2701 234 -286 -69 O ATOM 144 CB GLU A 17 70.421 16.110 22.548 1.00 22.80 C ANISOU 144 CB GLU A 17 2504 2960 3199 252 -320 -166 C ATOM 145 CG GLU A 17 69.883 16.160 23.967 1.00 24.35 C ANISOU 145 CG GLU A 17 2629 3204 3417 248 -281 -237 C ATOM 146 CD GLU A 17 68.947 15.002 24.304 1.00 25.53 C ANISOU 146 CD GLU A 17 2743 3409 3550 223 -250 -267 C ATOM 147 OE1 GLU A 17 68.490 14.269 23.399 1.00 27.09 O ANISOU 147 OE1 GLU A 17 2961 3601 3733 219 -269 -241 O ATOM 148 OE2 GLU A 17 68.618 14.836 25.491 1.00 27.76 O ANISOU 148 OE2 GLU A 17 2976 3741 3832 205 -206 -319 O ATOM 149 N LYS A 18 72.418 18.404 23.864 1.00 19.84 N ANISOU 149 N LYS A 18 2141 2543 2853 272 -309 -169 N ATOM 150 CA LYS A 18 73.516 18.522 24.816 1.00 19.69 C ANISOU 150 CA LYS A 18 2129 2545 2808 256 -259 -164 C ATOM 151 C LYS A 18 73.384 17.369 25.809 1.00 19.50 C ANISOU 151 C LYS A 18 2078 2586 2746 225 -195 -185 C ATOM 152 O LYS A 18 72.345 17.236 26.464 1.00 20.87 O ANISOU 152 O LYS A 18 2194 2793 2943 225 -186 -244 O ATOM 153 CB LYS A 18 73.456 19.863 25.547 1.00 20.25 C ANISOU 153 CB LYS A 18 2164 2596 2935 281 -279 -211 C ATOM 154 CG LYS A 18 74.616 20.105 26.506 1.00 20.46 C ANISOU 154 CG LYS A 18 2199 2638 2936 265 -233 -204 C ATOM 155 CD LYS A 18 74.400 21.375 27.311 1.00 21.41 C ANISOU 155 CD LYS A 18 2277 2745 3115 289 -251 -262 C ATOM 156 CE LYS A 18 75.527 21.621 28.294 1.00 21.66 C ANISOU 156 CE LYS A 18 2316 2792 3120 272 -207 -257 C ATOM 157 NZ LYS A 18 75.240 22.785 29.171 1.00 22.69 N ANISOU 157 NZ LYS A 18 2400 2915 3307 294 -219 -322 N ATOM 158 N AILE A 19 74.415 16.540 25.922 0.50 18.62 N ANISOU 158 N AILE A 19 2006 2492 2577 197 -155 -140 N ATOM 159 N BILE A 19 74.423 16.542 25.909 0.50 18.86 N ANISOU 159 N BILE A 19 2037 2522 2607 198 -155 -139 N ATOM 160 CA AILE A 19 74.360 15.390 26.814 0.50 18.38 C ANISOU 160 CA AILE A 19 1961 2516 2506 164 -103 -151 C ATOM 161 CA BILE A 19 74.412 15.361 26.770 0.50 18.76 C ANISOU 161 CA BILE A 19 2012 2563 2552 163 -103 -147 C ATOM 162 C AILE A 19 75.568 15.392 27.738 0.50 17.99 C ANISOU 162 C AILE A 19 1927 2481 2428 145 -65 -137 C ATOM 163 C BILE A 19 75.569 15.465 27.752 0.50 18.23 C ANISOU 163 C BILE A 19 1956 2509 2460 146 -66 -138 C ATOM 164 O AILE A 19 76.702 15.601 27.297 0.50 17.50 O ANISOU 164 O AILE A 19 1908 2391 2350 148 -67 -92 O ATOM 165 O BILE A 19 76.680 15.817 27.359 0.50 17.72 O ANISOU 165 O BILE A 19 1932 2416 2386 152 -70 -97 O ATOM 166 CB AILE A 19 74.255 14.068 26.032 0.50 18.23 C ANISOU 166 CB AILE A 19 1974 2506 2447 146 -99 -112 C ATOM 167 CB BILE A 19 74.573 14.068 25.953 0.50 18.87 C ANISOU 167 CB BILE A 19 2067 2582 2521 145 -97 -100 C ATOM 168 CG1AILE A 19 74.309 12.878 26.992 0.50 18.17 C ANISOU 168 CG1AILE A 19 1959 2548 2396 107 -52 -118 C ATOM 169 CG1BILE A 19 76.037 13.839 25.612 0.50 18.81 C ANISOU 169 CG1BILE A 19 2114 2556 2477 137 -83 -45 C ATOM 170 CG2AILE A 19 75.354 13.972 24.988 0.50 17.76 C ANISOU 170 CG2AILE A 19 1975 2410 2361 149 -110 -50 C ATOM 171 CG2BILE A 19 73.759 14.133 24.674 0.50 19.15 C ANISOU 171 CG2BILE A 19 2110 2588 2577 165 -144 -91 C ATOM 172 CD1AILE A 19 73.488 11.695 26.541 0.50 18.31 C ANISOU 172 CD1AILE A 19 1978 2585 2394 89 -53 -113 C ATOM 173 CD1BILE A 19 76.845 13.257 26.749 0.50 18.72 C ANISOU 173 CD1BILE A 19 2103 2576 2432 110 -39 -43 C ATOM 174 N THR A 20 75.300 15.165 29.023 1.00 17.98 N ANISOU 174 N THR A 20 1890 2525 2418 121 -29 -177 N ATOM 175 CA THR A 20 76.316 15.157 30.070 1.00 17.99 C ANISOU 175 CA THR A 20 1901 2543 2393 99 5 -171 C ATOM 176 C THR A 20 76.298 13.797 30.748 1.00 17.93 C ANISOU 176 C THR A 20 1900 2579 2334 54 40 -163 C ATOM 177 O THR A 20 75.239 13.306 31.154 1.00 18.76 O ANISOU 177 O THR A 20 1972 2722 2435 33 51 -199 O ATOM 178 CB THR A 20 76.067 16.289 31.081 1.00 18.33 C ANISOU 178 CB THR A 20 1898 2596 2470 107 11 -229 C ATOM 179 OG1 THR A 20 76.203 17.552 30.417 1.00 18.61 O ANISOU 179 OG1 THR A 20 1936 2581 2553 148 -29 -229 O ATOM 180 CG2 THR A 20 77.058 16.242 32.241 1.00 18.20 C ANISOU 180 CG2 THR A 20 1893 2602 2423 78 47 -224 C ATOM 181 N ILE A 21 77.479 13.201 30.869 1.00 17.25 N ANISOU 181 N ILE A 21 1856 2487 2212 38 53 -117 N ATOM 182 CA ILE A 21 77.669 11.951 31.611 1.00 17.13 C ANISOU 182 CA ILE A 21 1855 2504 2148 -6 77 -104 C ATOM 183 C ILE A 21 78.603 12.242 32.783 1.00 16.86 C ANISOU 183 C ILE A 21 1826 2481 2099 -26 97 -105 C ATOM 184 O ILE A 21 79.438 13.155 32.713 1.00 16.60 O ANISOU 184 O ILE A 21 1800 2421 2086 -2 92 -97 O ATOM 185 CB ILE A 21 78.170 10.809 30.695 1.00 17.23 C ANISOU 185 CB ILE A 21 1913 2497 2135 -7 67 -51 C ATOM 186 CG1 ILE A 21 79.581 11.088 30.173 1.00 16.87 C ANISOU 186 CG1 ILE A 21 1903 2415 2090 14 60 -11 C ATOM 187 CG2 ILE A 21 77.198 10.598 29.537 1.00 17.40 C ANISOU 187 CG2 ILE A 21 1931 2510 2172 11 45 -52 C ATOM 188 CD1 ILE A 21 80.118 10.005 29.263 1.00 16.76 C ANISOU 188 CD1 ILE A 21 1928 2385 2055 14 52 30 C ATOM 189 N ATHR A 22 78.471 11.450 33.844 0.50 16.84 N ANISOU 189 N ATHR A 22 1823 2516 2060 -74 118 -113 N ATOM 190 N BTHR A 22 78.443 11.492 33.873 0.50 16.84 N ANISOU 190 N BTHR A 22 1820 2517 2060 -74 119 -115 N ATOM 191 CA ATHR A 22 79.125 11.724 35.116 0.50 17.08 C ANISOU 191 CA ATHR A 22 1854 2565 2072 -102 136 -123 C ATOM 192 CA BTHR A 22 79.168 11.770 35.110 0.50 17.05 C ANISOU 192 CA BTHR A 22 1850 2559 2069 -100 136 -122 C ATOM 193 C ATHR A 22 80.016 10.572 35.551 0.50 16.82 C ANISOU 193 C ATHR A 22 1865 2530 1995 -137 135 -78 C ATOM 194 C BTHR A 22 79.999 10.587 35.572 0.50 16.82 C ANISOU 194 C BTHR A 22 1864 2531 1995 -137 136 -79 C ATOM 195 O ATHR A 22 79.772 9.419 35.193 0.50 16.65 O ANISOU 195 O ATHR A 22 1865 2511 1952 -154 126 -54 O ATOM 196 O BTHR A 22 79.699 9.435 35.261 0.50 16.67 O ANISOU 196 O BTHR A 22 1865 2516 1953 -157 128 -57 O ATOM 197 CB ATHR A 22 78.083 11.964 36.207 0.50 17.59 C ANISOU 197 CB ATHR A 22 1875 2681 2129 -139 161 -183 C ATOM 198 CB BTHR A 22 78.227 12.192 36.250 0.50 17.55 C ANISOU 198 CB BTHR A 22 1868 2672 2129 -133 161 -185 C ATOM 199 OG1ATHR A 22 77.124 10.902 36.179 0.50 18.21 O ANISOU 199 OG1ATHR A 22 1949 2790 2180 -174 166 -189 O ATOM 200 OG1BTHR A 22 77.402 11.089 36.641 0.50 18.08 O ANISOU 200 OG1BTHR A 22 1933 2779 2157 -184 173 -193 O ATOM 201 CG2ATHR A 22 77.378 13.298 35.983 0.50 17.82 C ANISOU 201 CG2ATHR A 22 1854 2707 2211 -100 158 -237 C ATOM 202 CG2BTHR A 22 77.357 13.368 35.825 0.50 17.77 C ANISOU 202 CG2BTHR A 22 1847 2695 2210 -93 155 -236 C ATOM 203 N CYS A 23 81.053 10.908 36.311 1.00 16.80 N ANISOU 203 N CYS A 23 1876 2522 1985 -145 139 -68 N ATOM 204 CA CYS A 23 81.992 9.939 36.864 1.00 16.89 C ANISOU 204 CA CYS A 23 1928 2528 1962 -177 130 -29 C ATOM 205 C CYS A 23 82.196 10.328 38.322 1.00 17.16 C ANISOU 205 C CYS A 23 1955 2590 1973 -218 146 -51 C ATOM 206 O CYS A 23 82.682 11.427 38.628 1.00 17.42 O ANISOU 206 O CYS A 23 1974 2617 2028 -198 153 -67 O ATOM 207 CB CYS A 23 83.308 10.015 36.085 1.00 16.47 C ANISOU 207 CB CYS A 23 1900 2428 1929 -136 113 10 C ATOM 208 SG CYS A 23 84.655 8.973 36.690 1.00 17.45 S ANISOU 208 SG CYS A 23 2068 2534 2028 -161 93 53 S ATOM 209 N SER A 24 81.803 9.428 39.217 1.00 17.70 N ANISOU 209 N SER A 24 2037 2691 1997 -280 149 -51 N ATOM 210 CA SER A 24 81.888 9.666 40.648 1.00 18.49 C ANISOU 210 CA SER A 24 2136 2825 2064 -333 164 -72 C ATOM 211 C SER A 24 82.970 8.771 41.256 1.00 18.98 C ANISOU 211 C SER A 24 2249 2868 2093 -367 137 -23 C ATOM 212 O SER A 24 82.913 7.555 41.099 1.00 19.16 O ANISOU 212 O SER A 24 2305 2883 2092 -392 115 10 O ATOM 213 CB SER A 24 80.531 9.374 41.283 1.00 19.30 C ANISOU 213 CB SER A 24 2215 2986 2134 -390 189 -114 C ATOM 214 OG SER A 24 80.582 9.589 42.674 1.00 20.20 O ANISOU 214 OG SER A 24 2328 3137 2208 -450 207 -138 O ATOM 215 N ALA A 25 83.938 9.377 41.932 1.00 19.42 N ANISOU 215 N ALA A 25 2312 2913 2151 -366 135 -19 N ATOM 216 CA ALA A 25 85.056 8.651 42.549 1.00 19.83 C ANISOU 216 CA ALA A 25 2412 2943 2181 -394 102 25 C ATOM 217 C ALA A 25 84.755 8.354 44.013 1.00 20.96 C ANISOU 217 C ALA A 25 2572 3127 2266 -478 107 15 C ATOM 218 O ALA A 25 84.177 9.188 44.714 1.00 21.57 O ANISOU 218 O ALA A 25 2619 3247 2331 -502 141 -32 O ATOM 219 CB ALA A 25 86.334 9.464 42.439 1.00 19.76 C ANISOU 219 CB ALA A 25 2402 2899 2207 -348 94 36 C ATOM 220 N SER A 26 85.162 7.172 44.475 1.00 21.57 N ANISOU 220 N SER A 26 2698 3190 2307 -524 69 57 N ATOM 221 CA SER A 26 84.886 6.752 45.860 1.00 22.93 C ANISOU 221 CA SER A 26 2897 3399 2414 -616 66 56 C ATOM 222 C SER A 26 85.617 7.593 46.907 1.00 23.86 C ANISOU 222 C SER A 26 3018 3526 2522 -635 71 45 C ATOM 223 O SER A 26 85.197 7.648 48.059 1.00 24.62 O ANISOU 223 O SER A 26 3122 3667 2564 -711 86 25 O ATOM 224 CB SER A 26 85.198 5.266 46.045 1.00 22.95 C ANISOU 224 CB SER A 26 2960 3374 2385 -661 12 111 C ATOM 225 OG SER A 26 86.543 4.974 45.697 1.00 22.65 O ANISOU 225 OG SER A 26 2947 3274 2383 -615 -35 152 O ATOM 226 N SER A 27 86.706 8.248 46.513 1.00 24.12 N ANISOU 226 N SER A 27 3043 3518 2603 -571 60 56 N ATOM 227 CA SER A 27 87.333 9.283 47.340 1.00 24.76 C ANISOU 227 CA SER A 27 3115 3608 2686 -576 72 37 C ATOM 228 C SER A 27 87.928 10.386 46.459 1.00 23.77 C ANISOU 228 C SER A 27 2954 3453 2626 -489 85 25 C ATOM 229 O SER A 27 88.019 10.234 45.234 1.00 23.25 O ANISOU 229 O SER A 27 2878 3355 2600 -431 79 39 O ATOM 230 CB SER A 27 88.382 8.680 48.280 1.00 25.95 C ANISOU 230 CB SER A 27 3318 3736 2807 -621 24 79 C ATOM 231 OG SER A 27 89.385 7.989 47.561 1.00 26.71 O ANISOU 231 OG SER A 27 3438 3772 2940 -575 -24 126 O ATOM 232 N SER A 27A 88.300 11.498 47.083 1.00 23.75 N ANISOU 232 N SER A 27A 2934 3461 2630 -487 103 -2 N ATOM 233 CA SER A 27A 88.734 12.692 46.359 1.00 23.56 C ANISOU 233 CA SER A 27A 2875 3413 2663 -415 118 -19 C ATOM 234 C SER A 27A 90.040 12.470 45.601 1.00 23.21 C ANISOU 234 C SER A 27A 2848 3313 2657 -365 85 26 C ATOM 235 O SER A 27A 90.968 11.855 46.119 1.00 24.25 O ANISOU 235 O SER A 27A 3013 3424 2776 -386 50 59 O ATOM 236 CB SER A 27A 88.885 13.875 47.319 1.00 24.03 C ANISOU 236 CB SER A 27A 2916 3495 2719 -431 140 -58 C ATOM 237 OG SER A 27A 89.134 15.075 46.611 1.00 24.37 O ANISOU 237 OG SER A 27A 2925 3516 2816 -366 153 -77 O ATOM 238 N ILE A 28 90.084 12.958 44.363 1.00 22.01 N ANISOU 238 N ILE A 28 2673 3139 2552 -301 94 23 N ATOM 239 CA ILE A 28 91.296 12.920 43.538 1.00 21.58 C ANISOU 239 CA ILE A 28 2625 3038 2536 -253 72 55 C ATOM 240 C ILE A 28 91.553 14.306 42.953 1.00 20.82 C ANISOU 240 C ILE A 28 2499 2930 2480 -206 93 35 C ATOM 241 O ILE A 28 90.637 15.121 42.856 1.00 21.28 O ANISOU 241 O ILE A 28 2531 3007 2546 -198 118 0 O ATOM 242 CB ILE A 28 91.206 11.853 42.418 1.00 21.71 C ANISOU 242 CB ILE A 28 2653 3032 2562 -230 56 81 C ATOM 243 CG1 ILE A 28 90.056 12.145 41.433 1.00 21.82 C ANISOU 243 CG1 ILE A 28 2642 3059 2588 -204 81 60 C ATOM 244 CG2 ILE A 28 91.035 10.467 43.028 1.00 22.18 C ANISOU 244 CG2 ILE A 28 2747 3096 2584 -279 27 104 C ATOM 245 CD1 ILE A 28 89.965 11.164 40.281 1.00 21.68 C ANISOU 245 CD1 ILE A 28 2637 3021 2581 -181 67 84 C ATOM 246 N SER A 29 92.805 14.576 42.580 1.00 20.27 N ANISOU 246 N SER A 29 2434 2828 2439 -176 79 55 N ATOM 247 CA SER A 29 93.129 15.787 41.828 1.00 19.45 C ANISOU 247 CA SER A 29 2308 2708 2373 -134 94 45 C ATOM 248 C SER A 29 92.535 15.671 40.429 1.00 18.19 C ANISOU 248 C SER A 29 2141 2539 2231 -100 101 48 C ATOM 249 O SER A 29 92.614 14.620 39.794 1.00 17.68 O ANISOU 249 O SER A 29 2090 2464 2162 -95 89 70 O ATOM 250 CB SER A 29 94.640 15.987 41.692 1.00 19.76 C ANISOU 250 CB SER A 29 2354 2719 2436 -117 79 66 C ATOM 251 OG SER A 29 94.931 17.068 40.815 1.00 20.43 O ANISOU 251 OG SER A 29 2422 2787 2552 -81 92 60 O ATOM 252 N SER A 30 92.011 16.784 39.936 1.00 17.52 N ANISOU 252 N SER A 30 2037 2453 2169 -76 115 26 N ATOM 253 CA SER A 30 91.506 16.858 38.569 1.00 17.02 C ANISOU 253 CA SER A 30 1969 2374 2123 -44 117 31 C ATOM 254 C SER A 30 92.616 16.618 37.546 1.00 16.20 C ANISOU 254 C SER A 30 1879 2244 2034 -23 109 62 C ATOM 255 O SER A 30 92.341 16.301 36.395 1.00 15.39 O ANISOU 255 O SER A 30 1780 2131 1936 -5 108 73 O ATOM 256 CB SER A 30 90.868 18.222 38.322 1.00 17.40 C ANISOU 256 CB SER A 30 1996 2418 2197 -24 124 3 C ATOM 257 OG SER A 30 91.837 19.249 38.419 1.00 18.17 O ANISOU 257 OG SER A 30 2094 2496 2314 -14 121 6 O ATOM 258 N HIS A 31 93.874 16.766 37.962 1.00 15.93 N ANISOU 258 N HIS A 31 1849 2199 2006 -26 104 73 N ATOM 259 CA HIS A 31 94.995 16.527 37.065 1.00 15.79 C ANISOU 259 CA HIS A 31 1836 2160 2003 -10 100 94 C ATOM 260 C HIS A 31 95.243 15.042 36.785 1.00 15.09 C ANISOU 260 C HIS A 31 1759 2070 1905 -12 87 109 C ATOM 261 O HIS A 31 96.009 14.708 35.886 1.00 14.95 O ANISOU 261 O HIS A 31 1741 2039 1901 3 87 118 O ATOM 262 CB HIS A 31 96.258 17.195 37.615 1.00 16.63 C ANISOU 262 CB HIS A 31 1938 2257 2123 -13 98 95 C ATOM 263 CG HIS A 31 96.184 18.692 37.629 1.00 17.50 C ANISOU 263 CG HIS A 31 2040 2362 2248 -6 107 82 C ATOM 264 ND1 HIS A 31 97.226 19.493 37.224 1.00 18.23 N ANISOU 264 ND1 HIS A 31 2130 2438 2359 1 110 89 N ATOM 265 CD2 HIS A 31 95.185 19.532 37.986 1.00 18.52 C ANISOU 265 CD2 HIS A 31 2162 2498 2379 -6 112 61 C ATOM 266 CE1 HIS A 31 96.877 20.762 37.342 1.00 18.38 C ANISOU 266 CE1 HIS A 31 2145 2451 2389 4 112 76 C ATOM 267 NE2 HIS A 31 95.645 20.813 37.809 1.00 18.91 N ANISOU 267 NE2 HIS A 31 2207 2530 2449 3 112 57 N ATOM 268 N TYR A 32 94.598 14.160 37.547 1.00 14.91 N ANISOU 268 N TYR A 32 1745 2060 1860 -34 76 109 N ATOM 269 CA TYR A 32 94.786 12.728 37.388 1.00 14.97 C ANISOU 269 CA TYR A 32 1767 2061 1861 -38 56 124 C ATOM 270 C TYR A 32 93.467 12.018 37.055 1.00 14.58 C ANISOU 270 C TYR A 32 1725 2024 1791 -46 58 123 C ATOM 271 O TYR A 32 93.268 10.865 37.428 1.00 14.93 O ANISOU 271 O TYR A 32 1786 2069 1819 -66 37 133 O ATOM 272 CB TYR A 32 95.457 12.142 38.647 1.00 15.82 C ANISOU 272 CB TYR A 32 1887 2164 1959 -65 29 132 C ATOM 273 CG TYR A 32 96.725 12.873 39.082 1.00 16.44 C ANISOU 273 CG TYR A 32 1956 2231 2059 -59 25 131 C ATOM 274 CD1 TYR A 32 97.713 13.218 38.164 1.00 16.56 C ANISOU 274 CD1 TYR A 32 1956 2230 2104 -31 33 130 C ATOM 275 CD2 TYR A 32 96.944 13.190 40.421 1.00 17.04 C ANISOU 275 CD2 TYR A 32 2038 2314 2122 -88 14 129 C ATOM 276 CE1 TYR A 32 98.867 13.887 38.558 1.00 17.16 C ANISOU 276 CE1 TYR A 32 2022 2298 2200 -28 30 127 C ATOM 277 CE2 TYR A 32 98.099 13.855 40.826 1.00 17.44 C ANISOU 277 CE2 TYR A 32 2080 2354 2192 -84 9 128 C ATOM 278 CZ TYR A 32 99.053 14.202 39.892 1.00 17.42 C ANISOU 278 CZ TYR A 32 2061 2336 2223 -53 17 127 C ATOM 279 OH TYR A 32 100.210 14.860 40.279 1.00 18.41 O ANISOU 279 OH TYR A 32 2175 2451 2368 -50 13 124 O ATOM 280 N LEU A 33 92.584 12.710 36.330 1.00 14.11 N ANISOU 280 N LEU A 33 1654 1973 1735 -32 77 112 N ATOM 281 CA LEU A 33 91.314 12.167 35.867 1.00 13.58 C ANISOU 281 CA LEU A 33 1589 1917 1654 -35 80 108 C ATOM 282 C LEU A 33 91.230 12.414 34.369 1.00 12.99 C ANISOU 282 C LEU A 33 1512 1829 1595 -4 87 113 C ATOM 283 O LEU A 33 91.383 13.556 33.921 1.00 13.15 O ANISOU 283 O LEU A 33 1523 1841 1631 12 97 107 O ATOM 284 CB LEU A 33 90.139 12.832 36.594 1.00 13.85 C ANISOU 284 CB LEU A 33 1608 1977 1677 -52 93 83 C ATOM 285 CG LEU A 33 88.703 12.285 36.439 1.00 14.05 C ANISOU 285 CG LEU A 33 1629 2023 1685 -64 97 71 C ATOM 286 CD1 LEU A 33 88.057 12.651 35.104 1.00 14.04 C ANISOU 286 CD1 LEU A 33 1619 2013 1703 -32 100 67 C ATOM 287 CD2 LEU A 33 88.645 10.781 36.660 1.00 14.10 C ANISOU 287 CD2 LEU A 33 1657 2033 1666 -90 80 90 C ATOM 288 N HIS A 34 91.024 11.343 33.606 1.00 12.41 N ANISOU 288 N HIS A 34 1449 1750 1514 0 79 123 N ATOM 289 CA HIS A 34 91.055 11.395 32.145 1.00 12.19 C ANISOU 289 CA HIS A 34 1425 1711 1496 23 85 129 C ATOM 290 C HIS A 34 89.855 10.628 31.602 1.00 11.91 C ANISOU 290 C HIS A 34 1396 1684 1447 21 80 129 C ATOM 291 O HIS A 34 89.278 9.786 32.294 1.00 12.13 O ANISOU 291 O HIS A 34 1429 1723 1459 1 71 129 O ATOM 292 CB HIS A 34 92.365 10.767 31.635 1.00 12.20 C ANISOU 292 CB HIS A 34 1432 1696 1506 33 81 137 C ATOM 293 CG HIS A 34 93.580 11.185 32.410 1.00 12.34 C ANISOU 293 CG HIS A 34 1443 1709 1538 30 79 136 C ATOM 294 ND1 HIS A 34 94.125 12.441 32.311 1.00 12.51 N ANISOU 294 ND1 HIS A 34 1455 1728 1571 36 93 133 N ATOM 295 CD2 HIS A 34 94.343 10.518 33.310 1.00 12.44 C ANISOU 295 CD2 HIS A 34 1456 1714 1554 21 61 138 C ATOM 296 CE1 HIS A 34 95.173 12.536 33.109 1.00 12.44 C ANISOU 296 CE1 HIS A 34 1439 1714 1573 31 88 131 C ATOM 297 NE2 HIS A 34 95.330 11.378 33.724 1.00 12.64 N ANISOU 297 NE2 HIS A 34 1471 1736 1595 23 67 135 N ATOM 298 N TRP A 35 89.482 10.935 30.358 1.00 11.86 N ANISOU 298 N TRP A 35 1393 1671 1445 38 84 132 N ATOM 299 CA TRP A 35 88.392 10.234 29.667 1.00 12.05 C ANISOU 299 CA TRP A 35 1422 1699 1457 38 78 133 C ATOM 300 C TRP A 35 88.835 9.630 28.340 1.00 12.34 C ANISOU 300 C TRP A 35 1474 1723 1491 50 78 143 C ATOM 301 O TRP A 35 89.631 10.224 27.616 1.00 12.33 O ANISOU 301 O TRP A 35 1476 1712 1497 59 86 147 O ATOM 302 CB TRP A 35 87.254 11.186 29.373 1.00 12.24 C ANISOU 302 CB TRP A 35 1435 1728 1488 45 78 121 C ATOM 303 CG TRP A 35 86.535 11.756 30.549 1.00 12.32 C ANISOU 303 CG TRP A 35 1424 1755 1502 34 81 99 C ATOM 304 CD1 TRP A 35 86.892 12.851 31.287 1.00 12.45 C ANISOU 304 CD1 TRP A 35 1428 1772 1533 35 87 87 C ATOM 305 CD2 TRP A 35 85.300 11.289 31.103 1.00 12.49 C ANISOU 305 CD2 TRP A 35 1432 1799 1512 17 80 82 C ATOM 306 NE1 TRP A 35 85.960 13.097 32.255 1.00 12.74 N ANISOU 306 NE1 TRP A 35 1443 1831 1568 21 91 60 N ATOM 307 CE2 TRP A 35 84.970 12.154 32.169 1.00 12.62 C ANISOU 307 CE2 TRP A 35 1426 1833 1538 8 89 55 C ATOM 308 CE3 TRP A 35 84.437 10.232 30.798 1.00 12.46 C ANISOU 308 CE3 TRP A 35 1433 1807 1493 6 75 84 C ATOM 309 CZ2 TRP A 35 83.812 11.987 32.939 1.00 12.92 C ANISOU 309 CZ2 TRP A 35 1442 1901 1566 -14 95 26 C ATOM 310 CZ3 TRP A 35 83.282 10.076 31.554 1.00 12.70 C ANISOU 310 CZ3 TRP A 35 1445 1867 1515 -17 79 59 C ATOM 311 CH2 TRP A 35 82.984 10.947 32.617 1.00 12.97 C ANISOU 311 CH2 TRP A 35 1452 1920 1555 -28 91 29 C ATOM 312 N TYR A 36 88.261 8.471 28.016 1.00 12.39 N ANISOU 312 N TYR A 36 1490 1732 1485 45 68 146 N ATOM 313 CA TYR A 36 88.535 7.732 26.788 1.00 12.61 C ANISOU 313 CA TYR A 36 1531 1750 1509 54 67 151 C ATOM 314 C TYR A 36 87.233 7.434 26.065 1.00 12.91 C ANISOU 314 C TYR A 36 1577 1794 1536 54 60 152 C ATOM 315 O TYR A 36 86.191 7.263 26.690 1.00 13.60 O ANISOU 315 O TYR A 36 1658 1893 1618 43 53 148 O ATOM 316 CB TYR A 36 89.278 6.407 27.097 1.00 12.49 C ANISOU 316 CB TYR A 36 1523 1728 1496 52 56 150 C ATOM 317 CG TYR A 36 90.531 6.691 27.853 1.00 12.55 C ANISOU 317 CG TYR A 36 1520 1728 1518 53 57 147 C ATOM 318 CD1 TYR A 36 90.515 6.794 29.231 1.00 12.46 C ANISOU 318 CD1 TYR A 36 1506 1721 1508 39 48 149 C ATOM 319 CD2 TYR A 36 91.712 6.989 27.194 1.00 12.48 C ANISOU 319 CD2 TYR A 36 1506 1713 1522 65 70 139 C ATOM 320 CE1 TYR A 36 91.645 7.146 29.939 1.00 12.62 C ANISOU 320 CE1 TYR A 36 1517 1734 1542 39 47 147 C ATOM 321 CE2 TYR A 36 92.842 7.353 27.896 1.00 12.54 C ANISOU 321 CE2 TYR A 36 1501 1716 1547 67 72 134 C ATOM 322 CZ TYR A 36 92.808 7.421 29.273 1.00 12.38 C ANISOU 322 CZ TYR A 36 1479 1696 1529 55 57 140 C ATOM 323 OH TYR A 36 93.915 7.796 29.982 1.00 12.55 O ANISOU 323 OH TYR A 36 1489 1711 1567 56 55 136 O ATOM 324 N GLN A 37 87.312 7.365 24.741 1.00 13.32 N ANISOU 324 N GLN A 37 1641 1838 1581 61 63 156 N ATOM 325 CA GLN A 37 86.192 7.000 23.890 1.00 13.88 C ANISOU 325 CA GLN A 37 1721 1911 1640 61 53 159 C ATOM 326 C GLN A 37 86.548 5.721 23.153 1.00 14.45 C ANISOU 326 C GLN A 37 1809 1979 1703 61 51 158 C ATOM 327 O GLN A 37 87.626 5.638 22.576 1.00 14.39 O ANISOU 327 O GLN A 37 1806 1966 1697 66 63 153 O ATOM 328 CB GLN A 37 85.957 8.115 22.876 1.00 14.18 C ANISOU 328 CB GLN A 37 1768 1943 1678 66 53 165 C ATOM 329 CG GLN A 37 84.790 7.895 21.918 1.00 14.55 C ANISOU 329 CG GLN A 37 1825 1987 1714 66 37 169 C ATOM 330 CD GLN A 37 84.836 8.851 20.752 1.00 14.97 C ANISOU 330 CD GLN A 37 1897 2028 1761 65 31 180 C ATOM 331 OE1 GLN A 37 85.831 8.933 20.037 1.00 15.82 O ANISOU 331 OE1 GLN A 37 2021 2134 1857 58 45 185 O ATOM 332 NE2 GLN A 37 83.756 9.603 20.559 1.00 14.96 N ANISOU 332 NE2 GLN A 37 1893 2019 1770 70 8 183 N ATOM 333 N GLN A 38 85.649 4.742 23.168 1.00 15.07 N ANISOU 333 N GLN A 38 1893 2060 1773 55 37 159 N ATOM 334 CA GLN A 38 85.848 3.498 22.427 1.00 16.14 C ANISOU 334 CA GLN A 38 2044 2189 1901 57 31 156 C ATOM 335 C GLN A 38 84.660 3.264 21.513 1.00 16.97 C ANISOU 335 C GLN A 38 2160 2296 1991 54 21 160 C ATOM 336 O GLN A 38 83.554 2.978 21.983 1.00 17.02 O ANISOU 336 O GLN A 38 2162 2310 1995 44 9 162 O ATOM 337 CB GLN A 38 86.033 2.324 23.377 1.00 16.20 C ANISOU 337 CB GLN A 38 2052 2189 1913 49 14 154 C ATOM 338 CG GLN A 38 86.400 1.020 22.676 1.00 16.29 C ANISOU 338 CG GLN A 38 2078 2187 1925 55 2 146 C ATOM 339 CD GLN A 38 86.751 -0.101 23.643 1.00 16.42 C ANISOU 339 CD GLN A 38 2099 2187 1951 48 -24 146 C ATOM 340 OE1 GLN A 38 86.248 -0.161 24.755 1.00 16.03 O ANISOU 340 OE1 GLN A 38 2051 2143 1897 29 -37 158 O ATOM 341 NE2 GLN A 38 87.641 -0.989 23.218 1.00 16.89 N ANISOU 341 NE2 GLN A 38 2162 2228 2026 61 -35 131 N ATOM 342 N LYS A 39 84.904 3.422 20.216 1.00 19.24 N ANISOU 342 N LYS A 39 2462 2581 2269 57 28 159 N ATOM 343 CA LYS A 39 83.906 3.154 19.189 1.00 21.22 C ANISOU 343 CA LYS A 39 2728 2833 2504 53 17 164 C ATOM 344 C LYS A 39 83.935 1.662 18.919 1.00 22.93 C ANISOU 344 C LYS A 39 2955 3044 2714 52 9 155 C ATOM 345 O LYS A 39 84.995 1.030 18.989 1.00 23.25 O ANISOU 345 O LYS A 39 2995 3079 2762 57 16 143 O ATOM 346 CB LYS A 39 84.186 3.980 17.930 1.00 22.01 C ANISOU 346 CB LYS A 39 2843 2930 2588 50 25 168 C ATOM 347 CG LYS A 39 83.998 5.476 18.166 1.00 22.46 C ANISOU 347 CG LYS A 39 2895 2985 2655 51 22 179 C ATOM 348 CD LYS A 39 84.226 6.340 16.936 1.00 23.38 C ANISOU 348 CD LYS A 39 3034 3095 2753 40 22 190 C ATOM 349 CE LYS A 39 84.105 7.810 17.302 1.00 23.77 C ANISOU 349 CE LYS A 39 3079 3136 2818 43 12 200 C ATOM 350 NZ LYS A 39 84.063 8.726 16.128 1.00 24.46 N ANISOU 350 NZ LYS A 39 3195 3211 2887 27 -3 218 N ATOM 351 N SER A 40 82.766 1.086 18.644 1.00 25.09 N ANISOU 351 N SER A 40 3235 3319 2978 45 -8 160 N ATOM 352 CA SER A 40 82.632 -0.372 18.525 1.00 26.36 C ANISOU 352 CA SER A 40 3407 3473 3134 42 -22 154 C ATOM 353 C SER A 40 83.525 -0.931 17.413 1.00 26.56 C ANISOU 353 C SER A 40 3447 3490 3153 48 -12 138 C ATOM 354 O SER A 40 83.558 -0.394 16.306 1.00 27.70 O ANISOU 354 O SER A 40 3603 3641 3282 46 -1 137 O ATOM 355 CB SER A 40 81.172 -0.746 18.271 1.00 27.30 C ANISOU 355 CB SER A 40 3532 3597 3243 31 -40 162 C ATOM 356 OG SER A 40 80.703 -0.150 17.078 1.00 28.68 O ANISOU 356 OG SER A 40 3718 3775 3406 33 -41 165 O ATOM 357 N GLY A 41 84.271 -1.984 17.739 1.00 26.85 N ANISOU 357 N GLY A 41 3483 3514 3203 54 -19 123 N ATOM 358 CA GLY A 41 85.248 -2.587 16.821 1.00 26.79 C ANISOU 358 CA GLY A 41 3480 3501 3198 63 -9 96 C ATOM 359 C GLY A 41 86.633 -1.950 16.818 1.00 26.30 C ANISOU 359 C GLY A 41 3402 3444 3148 71 17 78 C ATOM 360 O GLY A 41 87.500 -2.350 16.035 1.00 27.55 O ANISOU 360 O GLY A 41 3556 3602 3307 76 32 48 O ATOM 361 N PHE A 42 86.860 -0.971 17.693 1.00 24.66 N ANISOU 361 N PHE A 42 3181 3241 2949 71 24 93 N ATOM 362 CA PHE A 42 88.125 -0.256 17.733 1.00 22.95 C ANISOU 362 CA PHE A 42 2948 3030 2743 76 49 79 C ATOM 363 C PHE A 42 88.699 -0.223 19.146 1.00 20.05 C ANISOU 363 C PHE A 42 2563 2652 2403 84 37 82 C ATOM 364 O PHE A 42 88.030 -0.569 20.133 1.00 19.46 O ANISOU 364 O PHE A 42 2491 2569 2333 81 13 99 O ATOM 365 CB PHE A 42 87.944 1.163 17.183 1.00 24.63 C ANISOU 365 CB PHE A 42 3167 3259 2934 63 69 94 C ATOM 366 CG PHE A 42 87.457 1.201 15.759 1.00 26.32 C ANISOU 366 CG PHE A 42 3403 3481 3117 49 76 94 C ATOM 367 CD1 PHE A 42 88.348 1.053 14.700 1.00 27.61 C ANISOU 367 CD1 PHE A 42 3569 3655 3265 40 101 67 C ATOM 368 CD2 PHE A 42 86.103 1.370 15.474 1.00 27.40 C ANISOU 368 CD2 PHE A 42 3556 3616 3237 43 57 118 C ATOM 369 CE1 PHE A 42 87.899 1.081 13.382 1.00 28.48 C ANISOU 369 CE1 PHE A 42 3704 3776 3340 20 107 68 C ATOM 370 CE2 PHE A 42 85.649 1.400 14.164 1.00 28.03 C ANISOU 370 CE2 PHE A 42 3661 3702 3288 27 57 120 C ATOM 371 CZ PHE A 42 86.549 1.257 13.116 1.00 28.57 C ANISOU 371 CZ PHE A 42 3738 3782 3336 14 82 97 C ATOM 372 N ASER A 43 89.959 0.184 19.241 0.50 19.19 N ANISOU 372 N ASER A 43 2435 2545 2310 91 55 63 N ATOM 373 N BSER A 43 89.959 0.190 19.233 0.50 18.74 N ANISOU 373 N BSER A 43 2378 2488 2253 91 56 63 N ATOM 374 CA ASER A 43 90.591 0.382 20.533 0.50 18.24 C ANISOU 374 CA ASER A 43 2300 2416 2216 97 45 67 C ATOM 375 CA BSER A 43 90.609 0.404 20.515 0.50 17.56 C ANISOU 375 CA BSER A 43 2213 2331 2130 97 46 67 C ATOM 376 C ASER A 43 90.060 1.673 21.159 0.50 17.13 C ANISOU 376 C ASER A 43 2159 2287 2064 87 53 95 C ATOM 377 C BSER A 43 90.074 1.688 21.153 0.50 16.76 C ANISOU 377 C BSER A 43 2112 2240 2017 87 54 94 C ATOM 378 O ASER A 43 89.537 2.537 20.446 0.50 16.88 O ANISOU 378 O ASER A 43 2135 2267 2010 79 69 105 O ATOM 379 O BSER A 43 89.556 2.558 20.445 0.50 16.52 O ANISOU 379 O BSER A 43 2089 2221 1965 79 70 105 O ATOM 380 CB ASER A 43 92.098 0.513 20.380 0.50 18.74 C ANISOU 380 CB ASER A 43 2339 2481 2302 108 63 35 C ATOM 381 CB BSER A 43 92.116 0.539 20.328 0.50 17.63 C ANISOU 381 CB BSER A 43 2198 2340 2160 107 64 35 C ATOM 382 OG ASER A 43 92.446 1.866 20.163 0.50 19.07 O ANISOU 382 OG ASER A 43 2374 2540 2330 97 93 42 O ATOM 383 OG BSER A 43 92.628 -0.529 19.552 0.50 17.30 O ANISOU 383 OG BSER A 43 2151 2292 2131 118 62 -2 O ATOM 384 N PRO A 44 90.214 1.822 22.486 1.00 15.98 N ANISOU 384 N PRO A 44 2004 2134 1933 86 40 105 N ATOM 385 CA PRO A 44 89.938 3.121 23.100 1.00 15.43 C ANISOU 385 CA PRO A 44 1929 2075 1857 79 51 121 C ATOM 386 C PRO A 44 90.891 4.189 22.583 1.00 15.02 C ANISOU 386 C PRO A 44 1867 2032 1809 81 78 113 C ATOM 387 O PRO A 44 91.979 3.866 22.094 1.00 15.13 O ANISOU 387 O PRO A 44 1871 2044 1833 87 90 91 O ATOM 388 CB PRO A 44 90.182 2.882 24.594 1.00 15.22 C ANISOU 388 CB PRO A 44 1896 2041 1846 75 31 127 C ATOM 389 CG PRO A 44 90.159 1.401 24.779 1.00 15.51 C ANISOU 389 CG PRO A 44 1943 2060 1889 75 1 123 C ATOM 390 CD PRO A 44 90.640 0.823 23.487 1.00 16.01 C ANISOU 390 CD PRO A 44 2007 2119 1958 90 9 101 C ATOM 391 N LYS A 45 90.452 5.437 22.675 1.00 14.54 N ANISOU 391 N LYS A 45 1808 1979 1739 74 88 128 N ATOM 392 CA LYS A 45 91.255 6.596 22.332 1.00 14.52 C ANISOU 392 CA LYS A 45 1800 1981 1737 70 109 127 C ATOM 393 C LYS A 45 91.126 7.624 23.432 1.00 13.87 C ANISOU 393 C LYS A 45 1708 1897 1664 69 106 138 C ATOM 394 O LYS A 45 90.053 7.789 24.010 1.00 13.32 O ANISOU 394 O LYS A 45 1640 1829 1593 68 92 148 O ATOM 395 CB LYS A 45 90.791 7.202 21.011 1.00 15.20 C ANISOU 395 CB LYS A 45 1904 2072 1798 59 118 135 C ATOM 396 N LEU A 46 92.221 8.313 23.730 1.00 13.43 N ANISOU 396 N LEU A 46 1640 1842 1620 68 119 133 N ATOM 397 CA LEU A 46 92.173 9.447 24.652 1.00 13.11 C ANISOU 397 CA LEU A 46 1592 1800 1588 65 118 142 C ATOM 398 C LEU A 46 91.282 10.552 24.099 1.00 12.87 C ANISOU 398 C LEU A 46 1575 1769 1548 61 115 155 C ATOM 399 O LEU A 46 91.421 10.953 22.950 1.00 13.18 O ANISOU 399 O LEU A 46 1629 1807 1573 52 122 160 O ATOM 400 CB LEU A 46 93.569 10.003 24.914 1.00 12.99 C ANISOU 400 CB LEU A 46 1563 1786 1586 63 132 134 C ATOM 401 CG LEU A 46 93.623 11.212 25.865 1.00 12.95 C ANISOU 401 CG LEU A 46 1551 1777 1591 60 131 141 C ATOM 402 CD1 LEU A 46 93.229 10.864 27.288 1.00 12.80 C ANISOU 402 CD1 LEU A 46 1525 1759 1582 63 115 141 C ATOM 403 CD2 LEU A 46 95.013 11.823 25.841 1.00 13.00 C ANISOU 403 CD2 LEU A 46 1546 1785 1608 54 147 134 C ATOM 404 N LEU A 47 90.355 11.004 24.939 1.00 12.94 N ANISOU 404 N LEU A 47 1577 1775 1563 64 102 158 N ATOM 405 CA LEU A 47 89.424 12.065 24.606 1.00 13.11 C ANISOU 405 CA LEU A 47 1605 1790 1586 65 90 165 C ATOM 406 C LEU A 47 89.718 13.353 25.378 1.00 12.86 C ANISOU 406 C LEU A 47 1562 1752 1571 66 89 163 C ATOM 407 O LEU A 47 89.775 14.433 24.788 1.00 12.51 O ANISOU 407 O LEU A 47 1530 1694 1530 63 83 172 O ATOM 408 CB LEU A 47 88.007 11.584 24.896 1.00 13.58 C ANISOU 408 CB LEU A 47 1659 1855 1646 70 75 160 C ATOM 409 CG LEU A 47 86.872 12.440 24.346 1.00 14.12 C ANISOU 409 CG LEU A 47 1731 1914 1720 76 55 162 C ATOM 410 CD1 LEU A 47 86.759 12.287 22.839 1.00 14.44 C ANISOU 410 CD1 LEU A 47 1798 1945 1744 71 48 177 C ATOM 411 CD2 LEU A 47 85.580 12.060 25.024 1.00 14.45 C ANISOU 411 CD2 LEU A 47 1754 1967 1769 79 45 147 C ATOM 412 N ILE A 48 89.872 13.240 26.695 1.00 12.29 N ANISOU 412 N ILE A 48 1472 1688 1509 67 92 153 N ATOM 413 CA ILE A 48 90.085 14.398 27.582 1.00 12.85 C ANISOU 413 CA ILE A 48 1531 1755 1597 68 92 146 C ATOM 414 C ILE A 48 91.148 14.032 28.593 1.00 12.61 C ANISOU 414 C ILE A 48 1491 1732 1570 62 103 142 C ATOM 415 O ILE A 48 91.060 12.974 29.219 1.00 12.60 O ANISOU 415 O ILE A 48 1485 1740 1561 57 101 138 O ATOM 416 CB ILE A 48 88.793 14.781 28.343 1.00 13.32 C ANISOU 416 CB ILE A 48 1575 1820 1667 72 80 129 C ATOM 417 CG1 ILE A 48 87.645 15.048 27.355 1.00 14.02 C ANISOU 417 CG1 ILE A 48 1670 1899 1759 81 62 130 C ATOM 418 CG2 ILE A 48 89.050 15.949 29.295 1.00 13.58 C ANISOU 418 CG2 ILE A 48 1593 1849 1718 73 81 116 C ATOM 419 CD1 ILE A 48 86.360 15.568 27.950 1.00 14.67 C ANISOU 419 CD1 ILE A 48 1729 1984 1859 89 49 105 C ATOM 420 N TYR A 49 92.144 14.904 28.761 1.00 12.42 N ANISOU 420 N TYR A 49 1464 1700 1556 59 110 144 N ATOM 421 CA TYR A 49 93.158 14.714 29.791 1.00 12.53 C ANISOU 421 CA TYR A 49 1467 1719 1576 54 115 139 C ATOM 422 C TYR A 49 93.084 15.820 30.822 1.00 12.60 C ANISOU 422 C TYR A 49 1465 1726 1597 52 113 130 C ATOM 423 O TYR A 49 92.718 16.957 30.514 1.00 12.62 O ANISOU 423 O TYR A 49 1469 1717 1608 56 108 129 O ATOM 424 CB TYR A 49 94.562 14.611 29.192 1.00 12.75 C ANISOU 424 CB TYR A 49 1495 1743 1607 51 127 142 C ATOM 425 CG TYR A 49 95.076 15.830 28.450 1.00 12.84 C ANISOU 425 CG TYR A 49 1512 1745 1620 45 136 148 C ATOM 426 CD1 TYR A 49 94.828 15.996 27.093 1.00 13.30 C ANISOU 426 CD1 TYR A 49 1588 1800 1664 39 139 158 C ATOM 427 CD2 TYR A 49 95.854 16.794 29.095 1.00 13.33 C ANISOU 427 CD2 TYR A 49 1567 1804 1696 39 139 147 C ATOM 428 CE1 TYR A 49 95.314 17.096 26.402 1.00 13.55 C ANISOU 428 CE1 TYR A 49 1633 1824 1692 24 143 167 C ATOM 429 CE2 TYR A 49 96.344 17.893 28.407 1.00 13.49 C ANISOU 429 CE2 TYR A 49 1597 1814 1715 27 144 155 C ATOM 430 CZ TYR A 49 96.072 18.039 27.059 1.00 13.77 C ANISOU 430 CZ TYR A 49 1653 1846 1734 17 145 166 C ATOM 431 OH TYR A 49 96.538 19.131 26.346 1.00 14.57 O ANISOU 431 OH TYR A 49 1771 1937 1828 -3 146 179 O ATOM 432 N ARG A 50 93.455 15.469 32.053 1.00 12.68 N ANISOU 432 N ARG A 50 1466 1744 1607 43 111 123 N ATOM 433 CA ARG A 50 93.380 16.327 33.227 1.00 12.94 C ANISOU 433 CA ARG A 50 1489 1781 1648 37 110 111 C ATOM 434 C ARG A 50 92.032 17.035 33.304 1.00 13.04 C ANISOU 434 C ARG A 50 1493 1797 1664 42 107 94 C ATOM 435 O ARG A 50 91.965 18.263 33.342 1.00 13.07 O ANISOU 435 O ARG A 50 1491 1789 1684 48 104 85 O ATOM 436 CB ARG A 50 94.527 17.344 33.249 1.00 13.24 C ANISOU 436 CB ARG A 50 1524 1807 1700 37 115 114 C ATOM 437 CG ARG A 50 95.926 16.751 33.217 1.00 13.54 C ANISOU 437 CG ARG A 50 1561 1843 1742 34 118 122 C ATOM 438 CD ARG A 50 96.951 17.762 33.711 1.00 13.90 C ANISOU 438 CD ARG A 50 1600 1881 1801 28 122 120 C ATOM 439 NE ARG A 50 97.051 18.925 32.825 1.00 14.28 N ANISOU 439 NE ARG A 50 1653 1917 1855 30 128 125 N ATOM 440 CZ ARG A 50 97.852 19.020 31.761 1.00 14.80 C ANISOU 440 CZ ARG A 50 1723 1979 1920 25 138 134 C ATOM 441 NH1 ARG A 50 97.846 20.134 31.034 1.00 15.62 N ANISOU 441 NH1 ARG A 50 1839 2070 2025 18 138 142 N ATOM 442 NH2 ARG A 50 98.637 18.013 31.382 1.00 15.11 N ANISOU 442 NH2 ARG A 50 1757 2027 1959 24 147 132 N ATOM 443 N THR A 51 90.970 16.230 33.268 1.00 12.78 N ANISOU 443 N THR A 51 1459 1777 1619 39 105 89 N ATOM 444 CA THR A 51 89.576 16.663 33.485 1.00 12.92 C ANISOU 444 CA THR A 51 1462 1805 1642 41 102 64 C ATOM 445 C THR A 51 88.920 17.467 32.371 1.00 12.94 C ANISOU 445 C THR A 51 1465 1788 1663 62 89 63 C ATOM 446 O THR A 51 87.761 17.204 32.067 1.00 12.81 O ANISOU 446 O THR A 51 1441 1779 1648 67 83 51 O ATOM 447 CB THR A 51 89.434 17.373 34.855 1.00 13.25 C ANISOU 447 CB THR A 51 1485 1861 1688 29 108 36 C ATOM 448 OG1 THR A 51 89.688 16.405 35.863 1.00 13.63 O ANISOU 448 OG1 THR A 51 1538 1931 1711 2 113 38 O ATOM 449 CG2 THR A 51 88.042 17.970 35.088 1.00 13.51 C ANISOU 449 CG2 THR A 51 1492 1905 1734 34 106 -2 C ATOM 450 N SER A 52 89.631 18.431 31.793 1.00 12.96 N ANISOU 450 N SER A 52 1478 1766 1680 72 83 75 N ATOM 451 CA SER A 52 89.020 19.433 30.928 1.00 13.27 C ANISOU 451 CA SER A 52 1521 1780 1740 87 61 74 C ATOM 452 C SER A 52 89.773 19.747 29.635 1.00 13.33 C ANISOU 452 C SER A 52 1558 1764 1743 86 54 106 C ATOM 453 O SER A 52 89.328 20.618 28.892 1.00 13.89 O ANISOU 453 O SER A 52 1640 1809 1828 93 29 111 O ATOM 454 CB SER A 52 88.829 20.719 31.742 1.00 13.75 C ANISOU 454 CB SER A 52 1564 1831 1829 94 52 47 C ATOM 455 OG SER A 52 90.047 21.123 32.330 1.00 14.04 O ANISOU 455 OG SER A 52 1605 1865 1864 84 63 54 O ATOM 456 N ASN A 53 90.871 19.058 29.332 1.00 12.98 N ANISOU 456 N ASN A 53 1526 1728 1679 73 73 126 N ATOM 457 CA ASN A 53 91.674 19.390 28.158 1.00 13.29 C ANISOU 457 CA ASN A 53 1589 1752 1708 63 73 150 C ATOM 458 C ASN A 53 91.419 18.394 27.042 1.00 13.01 C ANISOU 458 C ASN A 53 1569 1723 1651 60 76 162 C ATOM 459 O ASN A 53 91.649 17.188 27.206 1.00 12.84 O ANISOU 459 O ASN A 53 1541 1720 1617 60 92 159 O ATOM 460 CB ASN A 53 93.146 19.413 28.513 1.00 13.42 C ANISOU 460 CB ASN A 53 1603 1775 1721 51 93 154 C ATOM 461 CG ASN A 53 93.434 20.366 29.641 1.00 13.87 C ANISOU 461 CG ASN A 53 1647 1826 1798 52 90 142 C ATOM 462 OD1 ASN A 53 93.538 21.580 29.427 1.00 14.34 O ANISOU 462 OD1 ASN A 53 1715 1863 1870 49 76 147 O ATOM 463 ND2 ASN A 53 93.507 19.841 30.856 1.00 14.12 N ANISOU 463 ND2 ASN A 53 1659 1875 1831 54 99 126 N ATOM 464 N LEU A 54 90.965 18.894 25.898 1.00 13.16 N ANISOU 464 N LEU A 54 1612 1724 1665 56 57 177 N ATOM 465 CA LEU A 54 90.695 18.031 24.751 1.00 13.31 C ANISOU 465 CA LEU A 54 1648 1749 1660 50 59 189 C ATOM 466 C LEU A 54 91.980 17.471 24.167 1.00 13.51 C ANISOU 466 C LEU A 54 1681 1788 1662 31 87 196 C ATOM 467 O LEU A 54 92.940 18.203 23.940 1.00 13.65 O ANISOU 467 O LEU A 54 1708 1802 1677 13 95 204 O ATOM 468 CB LEU A 54 89.942 18.802 23.668 1.00 13.66 C ANISOU 468 CB LEU A 54 1719 1767 1703 46 26 205 C ATOM 469 CG LEU A 54 88.557 19.322 24.055 1.00 13.94 C ANISOU 469 CG LEU A 54 1742 1786 1768 68 -9 191 C ATOM 470 CD1 LEU A 54 87.861 19.884 22.823 1.00 14.10 C ANISOU 470 CD1 LEU A 54 1793 1777 1786 63 -48 211 C ATOM 471 CD2 LEU A 54 87.716 18.252 24.739 1.00 14.04 C ANISOU 471 CD2 LEU A 54 1727 1823 1784 84 2 169 C ATOM 472 N ALA A 55 91.988 16.165 23.923 1.00 13.60 N ANISOU 472 N ALA A 55 1689 1818 1661 33 102 190 N ATOM 473 CA ALA A 55 93.130 15.528 23.281 1.00 14.40 C ANISOU 473 CA ALA A 55 1792 1933 1744 18 128 187 C ATOM 474 C ALA A 55 93.210 15.907 21.817 1.00 15.76 C ANISOU 474 C ALA A 55 1996 2103 1890 -8 129 201 C ATOM 475 O ALA A 55 92.272 16.481 21.254 1.00 15.70 O ANISOU 475 O ALA A 55 2010 2078 1876 -11 102 218 O ATOM 476 CB ALA A 55 93.037 14.022 23.423 1.00 14.32 C ANISOU 476 CB ALA A 55 1771 1939 1733 30 136 173 C ATOM 477 N SER A 56 94.344 15.592 21.195 1.00 17.26 N ANISOU 477 N SER A 56 2185 2311 2063 -29 157 193 N ATOM 478 CA SER A 56 94.524 15.862 19.769 1.00 19.09 C ANISOU 478 CA SER A 56 2447 2547 2259 -64 164 204 C ATOM 479 C SER A 56 93.447 15.158 18.932 1.00 19.03 C ANISOU 479 C SER A 56 2459 2537 2232 -61 150 210 C ATOM 480 O SER A 56 93.040 14.027 19.232 1.00 19.64 O ANISOU 480 O SER A 56 2521 2623 2320 -37 151 196 O ATOM 481 CB SER A 56 95.917 15.452 19.295 1.00 20.28 C ANISOU 481 CB SER A 56 2585 2725 2395 -88 205 182 C ATOM 482 OG SER A 56 96.157 15.996 18.016 1.00 22.48 O ANISOU 482 OG SER A 56 2897 3012 2634 -134 213 194 O ATOM 483 N GLY A 57 92.942 15.877 17.931 1.00 19.22 N ANISOU 483 N GLY A 57 2522 2548 2232 -87 129 234 N ATOM 484 CA GLY A 57 91.888 15.371 17.054 1.00 18.87 C ANISOU 484 CA GLY A 57 2501 2499 2168 -88 109 244 C ATOM 485 C GLY A 57 90.466 15.418 17.582 1.00 18.24 C ANISOU 485 C GLY A 57 2417 2396 2115 -54 70 251 C ATOM 486 O GLY A 57 89.542 15.056 16.858 1.00 20.20 O ANISOU 486 O GLY A 57 2684 2639 2351 -54 49 260 O ATOM 487 N VAL A 58 90.265 15.860 18.824 1.00 16.27 N ANISOU 487 N VAL A 58 2142 2137 1903 -27 60 245 N ATOM 488 CA VAL A 58 88.941 15.839 19.447 1.00 15.24 C ANISOU 488 CA VAL A 58 1998 1994 1800 4 30 241 C ATOM 489 C VAL A 58 88.230 17.158 19.131 1.00 14.91 C ANISOU 489 C VAL A 58 1976 1917 1771 2 -15 258 C ATOM 490 O VAL A 58 88.792 18.235 19.363 1.00 14.72 O ANISOU 490 O VAL A 58 1959 1879 1757 -8 -22 266 O ATOM 491 CB VAL A 58 89.049 15.636 20.968 1.00 14.71 C ANISOU 491 CB VAL A 58 1891 1936 1763 29 43 220 C ATOM 492 CG1 VAL A 58 87.681 15.730 21.652 1.00 14.64 C ANISOU 492 CG1 VAL A 58 1863 1919 1780 53 17 209 C ATOM 493 CG2 VAL A 58 89.710 14.286 21.257 1.00 14.56 C ANISOU 493 CG2 VAL A 58 1856 1943 1735 31 76 205 C ATOM 494 N PRO A 59 86.996 17.084 18.601 1.00 14.53 N ANISOU 494 N PRO A 59 1939 1855 1728 11 -51 264 N ATOM 495 CA PRO A 59 86.299 18.312 18.228 1.00 14.61 C ANISOU 495 CA PRO A 59 1970 1826 1756 11 -104 279 C ATOM 496 C PRO A 59 85.818 19.131 19.415 1.00 14.19 C ANISOU 496 C PRO A 59 1883 1756 1752 42 -124 258 C ATOM 497 O PRO A 59 85.602 18.605 20.508 1.00 13.66 O ANISOU 497 O PRO A 59 1776 1711 1704 65 -101 231 O ATOM 498 CB PRO A 59 85.125 17.814 17.374 1.00 15.10 C ANISOU 498 CB PRO A 59 2046 1879 1811 15 -136 285 C ATOM 499 CG PRO A 59 84.900 16.433 17.810 1.00 14.96 C ANISOU 499 CG PRO A 59 2000 1896 1789 30 -101 264 C ATOM 500 CD PRO A 59 86.227 15.886 18.240 1.00 14.49 C ANISOU 500 CD PRO A 59 1930 1864 1711 19 -48 257 C ATOM 501 N ALA A 60 85.621 20.422 19.162 1.00 13.96 N ANISOU 501 N ALA A 60 1874 1687 1742 39 -171 271 N ATOM 502 CA ALA A 60 85.322 21.410 20.204 1.00 13.97 C ANISOU 502 CA ALA A 60 1847 1667 1793 66 -192 249 C ATOM 503 C ALA A 60 83.980 21.211 20.925 1.00 13.92 C ANISOU 503 C ALA A 60 1797 1664 1830 104 -210 211 C ATOM 504 O ALA A 60 83.749 21.808 21.972 1.00 13.70 O ANISOU 504 O ALA A 60 1734 1631 1840 126 -214 180 O ATOM 505 CB ALA A 60 85.383 22.808 19.607 1.00 14.42 C ANISOU 505 CB ALA A 60 1941 1674 1863 52 -248 273 C ATOM 506 N ARG A 61 83.097 20.384 20.363 1.00 13.93 N ANISOU 506 N ARG A 61 1797 1674 1823 109 -219 210 N ATOM 507 CA ARG A 61 81.828 20.069 21.022 1.00 14.17 C ANISOU 507 CA ARG A 61 1781 1714 1889 140 -229 170 C ATOM 508 C ARG A 61 81.993 19.257 22.314 1.00 13.73 C ANISOU 508 C ARG A 61 1683 1704 1830 146 -174 140 C ATOM 509 O ARG A 61 81.049 19.187 23.108 1.00 13.97 O ANISOU 509 O ARG A 61 1670 1747 1891 166 -176 101 O ATOM 510 CB ARG A 61 80.859 19.364 20.067 1.00 14.54 C ANISOU 510 CB ARG A 61 1840 1759 1926 141 -253 178 C ATOM 511 CG ARG A 61 81.278 17.991 19.566 1.00 14.45 C ANISOU 511 CG ARG A 61 1845 1781 1863 119 -211 196 C ATOM 512 CD ARG A 61 80.175 17.387 18.710 1.00 14.85 C ANISOU 512 CD ARG A 61 1904 1829 1911 122 -241 199 C ATOM 513 NE ARG A 61 80.586 16.106 18.161 1.00 14.92 N ANISOU 513 NE ARG A 61 1931 1865 1871 102 -204 215 N ATOM 514 CZ ARG A 61 81.352 15.935 17.081 1.00 15.16 C ANISOU 514 CZ ARG A 61 2008 1892 1859 73 -198 248 C ATOM 515 NH1 ARG A 61 81.783 16.957 16.342 1.00 15.68 N ANISOU 515 NH1 ARG A 61 2114 1927 1916 54 -228 274 N ATOM 516 NH2 ARG A 61 81.672 14.702 16.722 1.00 15.24 N ANISOU 516 NH2 ARG A 61 2026 1930 1833 60 -163 251 N ATOM 517 N PHE A 62 83.155 18.630 22.517 1.00 13.55 N ANISOU 517 N PHE A 62 1671 1705 1771 127 -128 156 N ATOM 518 CA PHE A 62 83.441 17.952 23.772 1.00 13.22 C ANISOU 518 CA PHE A 62 1597 1701 1726 128 -85 133 C ATOM 519 C PHE A 62 83.991 18.924 24.809 1.00 13.48 C ANISOU 519 C PHE A 62 1613 1728 1782 133 -78 116 C ATOM 520 O PHE A 62 84.711 19.881 24.474 1.00 13.79 O ANISOU 520 O PHE A 62 1674 1741 1825 127 -92 134 O ATOM 521 CB PHE A 62 84.441 16.807 23.558 1.00 12.97 C ANISOU 521 CB PHE A 62 1583 1692 1653 108 -46 153 C ATOM 522 CG PHE A 62 83.868 15.641 22.797 1.00 12.93 C ANISOU 522 CG PHE A 62 1588 1699 1626 104 -45 161 C ATOM 523 CD1 PHE A 62 83.230 14.603 23.464 1.00 13.13 C ANISOU 523 CD1 PHE A 62 1590 1752 1649 107 -31 142 C ATOM 524 CD2 PHE A 62 83.946 15.592 21.402 1.00 13.31 C ANISOU 524 CD2 PHE A 62 1672 1731 1652 93 -61 187 C ATOM 525 CE1 PHE A 62 82.699 13.530 22.771 1.00 13.07 C ANISOU 525 CE1 PHE A 62 1592 1753 1622 102 -32 148 C ATOM 526 CE2 PHE A 62 83.409 14.520 20.701 1.00 13.43 C ANISOU 526 CE2 PHE A 62 1697 1757 1647 89 -61 192 C ATOM 527 CZ PHE A 62 82.784 13.489 21.389 1.00 13.39 C ANISOU 527 CZ PHE A 62 1667 1777 1644 96 -47 172 C ATOM 528 N SER A 63 83.663 18.651 26.067 1.00 13.30 N ANISOU 528 N SER A 63 1551 1732 1769 138 -57 83 N ATOM 529 CA SER A 63 84.237 19.369 27.202 1.00 13.61 C ANISOU 529 CA SER A 63 1572 1774 1824 139 -44 64 C ATOM 530 C SER A 63 84.153 18.495 28.432 1.00 13.52 C ANISOU 530 C SER A 63 1534 1805 1800 129 -8 41 C ATOM 531 O SER A 63 83.439 17.482 28.448 1.00 13.58 O ANISOU 531 O SER A 63 1531 1835 1792 123 0 33 O ATOM 532 CB SER A 63 83.533 20.715 27.435 1.00 13.95 C ANISOU 532 CB SER A 63 1596 1791 1915 160 -79 35 C ATOM 533 OG SER A 63 82.204 20.538 27.876 1.00 14.52 O ANISOU 533 OG SER A 63 1629 1879 2011 174 -87 -9 O ATOM 534 N GLY A 64 84.906 18.884 29.449 1.00 13.67 N ANISOU 534 N GLY A 64 1543 1832 1820 122 10 31 N ATOM 535 CA GLY A 64 84.906 18.174 30.710 1.00 13.94 C ANISOU 535 CA GLY A 64 1556 1902 1836 105 39 11 C ATOM 536 C GLY A 64 85.063 19.132 31.866 1.00 14.44 C ANISOU 536 C GLY A 64 1597 1970 1919 104 44 -20 C ATOM 537 O GLY A 64 85.653 20.206 31.720 1.00 14.41 O ANISOU 537 O GLY A 64 1600 1938 1935 115 31 -15 O ATOM 538 N ASER A 65 84.512 18.747 33.015 0.50 14.83 N ANISOU 538 N ASER A 65 1619 2055 1960 88 63 -54 N ATOM 539 N BSER A 65 84.516 18.762 33.020 0.50 14.87 N ANISOU 539 N BSER A 65 1624 2060 1966 88 63 -55 N ATOM 540 CA ASER A 65 84.561 19.561 34.219 0.50 15.40 C ANISOU 540 CA ASER A 65 1666 2139 2046 82 73 -92 C ATOM 541 CA BSER A 65 84.652 19.574 34.219 0.50 15.47 C ANISOU 541 CA BSER A 65 1677 2147 2054 82 74 -90 C ATOM 542 C ASER A 65 84.668 18.633 35.419 0.50 15.54 C ANISOU 542 C ASER A 65 1679 2200 2026 45 102 -101 C ATOM 543 C BSER A 65 84.538 18.695 35.443 0.50 15.66 C ANISOU 543 C BSER A 65 1690 2216 2043 46 102 -106 C ATOM 544 O ASER A 65 84.455 17.422 35.306 0.50 15.41 O ANISOU 544 O ASER A 65 1673 2201 1980 27 110 -84 O ATOM 545 O BSER A 65 83.972 17.602 35.389 0.50 15.71 O ANISOU 545 O BSER A 65 1698 2245 2025 29 110 -102 O ATOM 546 CB ASER A 65 83.302 20.429 34.328 0.50 16.00 C ANISOU 546 CB ASER A 65 1703 2215 2163 102 58 -146 C ATOM 547 CB BSER A 65 83.577 20.659 34.271 0.50 16.09 C ANISOU 547 CB BSER A 65 1719 2216 2176 105 55 -140 C ATOM 548 OG ASER A 65 83.422 21.409 35.340 0.50 16.55 O ANISOU 548 OG ASER A 65 1748 2288 2251 102 64 -186 O ATOM 549 OG BSER A 65 82.295 20.074 34.425 0.50 16.71 O ANISOU 549 OG BSER A 65 1768 2325 2254 99 61 -175 O ATOM 550 N GLY A 66 85.051 19.204 36.555 1.00 16.08 N ANISOU 550 N GLY A 66 1735 2281 2094 31 115 -125 N ATOM 551 CA GLY A 66 84.979 18.511 37.828 1.00 16.54 C ANISOU 551 CA GLY A 66 1787 2382 2116 -11 139 -141 C ATOM 552 C GLY A 66 86.137 18.765 38.744 1.00 16.87 C ANISOU 552 C GLY A 66 1843 2424 2144 -29 146 -130 C ATOM 553 O GLY A 66 87.150 19.360 38.367 1.00 16.94 O ANISOU 553 O GLY A 66 1867 2399 2168 -9 135 -105 O ATOM 554 N SER A 67 85.950 18.303 39.971 1.00 17.45 N ANISOU 554 N SER A 67 1911 2536 2183 -72 164 -150 N ATOM 555 CA SER A 67 86.978 18.341 40.994 1.00 17.98 C ANISOU 555 CA SER A 67 1994 2608 2228 -99 169 -140 C ATOM 556 C SER A 67 86.525 17.419 42.103 1.00 18.04 C ANISOU 556 C SER A 67 2006 2661 2187 -157 184 -152 C ATOM 557 O SER A 67 85.358 17.015 42.139 1.00 17.81 O ANISOU 557 O SER A 67 1958 2663 2146 -174 196 -180 O ATOM 558 CB SER A 67 87.193 19.759 41.535 1.00 18.64 C ANISOU 558 CB SER A 67 2058 2686 2340 -86 173 -176 C ATOM 559 OG SER A 67 86.030 20.277 42.133 1.00 19.89 O ANISOU 559 OG SER A 67 2177 2876 2506 -96 189 -240 O ATOM 560 N GLY A 68 87.447 17.106 43.010 1.00 18.03 N ANISOU 560 N GLY A 68 2030 2665 2157 -190 180 -131 N ATOM 561 CA GLY A 68 87.122 16.290 44.173 1.00 18.34 C ANISOU 561 CA GLY A 68 2081 2746 2143 -255 189 -139 C ATOM 562 C GLY A 68 86.732 14.888 43.768 1.00 18.29 C ANISOU 562 C GLY A 68 2097 2743 2110 -275 178 -107 C ATOM 563 O GLY A 68 87.550 14.161 43.203 1.00 17.59 O ANISOU 563 O GLY A 68 2039 2622 2024 -260 153 -58 O ATOM 564 N THR A 69 85.472 14.535 44.026 1.00 18.76 N ANISOU 564 N THR A 69 2138 2844 2146 -308 197 -141 N ATOM 565 CA THR A 69 84.923 13.227 43.687 1.00 19.01 C ANISOU 565 CA THR A 69 2189 2885 2150 -333 188 -116 C ATOM 566 C THR A 69 83.962 13.218 42.486 1.00 18.51 C ANISOU 566 C THR A 69 2100 2816 2117 -293 193 -130 C ATOM 567 O THR A 69 83.505 12.148 42.091 1.00 19.19 O ANISOU 567 O THR A 69 2201 2906 2184 -309 184 -109 O ATOM 568 CB THR A 69 84.137 12.660 44.888 1.00 20.02 C ANISOU 568 CB THR A 69 2320 3069 2219 -415 206 -142 C ATOM 569 OG1 THR A 69 83.016 13.506 45.154 1.00 21.00 O ANISOU 569 OG1 THR A 69 2392 3235 2353 -419 242 -213 O ATOM 570 CG2 THR A 69 85.020 12.583 46.118 1.00 20.46 C ANISOU 570 CG2 THR A 69 2408 3130 2236 -464 197 -126 C ATOM 571 N ASER A 70 83.676 14.387 41.909 0.50 18.13 N ANISOU 571 N ASER A 70 2016 2756 2117 -242 200 -162 N ATOM 572 N BSER A 70 83.651 14.391 41.927 0.50 18.25 N ANISOU 572 N BSER A 70 2030 2772 2132 -243 201 -163 N ATOM 573 CA ASER A 70 82.617 14.515 40.913 0.50 17.89 C ANISOU 573 CA ASER A 70 1957 2724 2117 -209 201 -184 C ATOM 574 CA BSER A 70 82.613 14.513 40.903 0.50 18.07 C ANISOU 574 CA BSER A 70 1980 2747 2140 -209 201 -184 C ATOM 575 C ASER A 70 83.129 15.120 39.615 0.50 17.17 C ANISOU 575 C ASER A 70 1870 2580 2073 -143 180 -158 C ATOM 576 C BSER A 70 83.166 15.105 39.622 0.50 17.26 C ANISOU 576 C BSER A 70 1882 2592 2084 -144 180 -157 C ATOM 577 O ASER A 70 83.534 16.282 39.591 0.50 17.47 O ANISOU 577 O ASER A 70 1894 2598 2144 -113 178 -173 O ATOM 578 O BSER A 70 83.656 16.234 39.620 0.50 17.56 O ANISOU 578 O BSER A 70 1911 2609 2154 -114 177 -168 O ATOM 579 CB ASER A 70 81.487 15.378 41.461 0.50 18.31 C ANISOU 579 CB ASER A 70 1956 2815 2185 -217 226 -259 C ATOM 580 CB BSER A 70 81.467 15.383 41.404 0.50 18.58 C ANISOU 580 CB BSER A 70 1990 2849 2221 -214 225 -259 C ATOM 581 OG ASER A 70 80.376 15.350 40.592 0.50 18.49 O ANISOU 581 OG ASER A 70 1950 2840 2236 -191 223 -282 O ATOM 582 OG BSER A 70 80.808 14.754 42.485 0.50 19.35 O ANISOU 582 OG BSER A 70 2080 3003 2270 -283 250 -288 O ATOM 583 N TYR A 71 83.073 14.327 38.544 1.00 16.70 N ANISOU 583 N TYR A 71 1830 2500 2015 -126 165 -122 N ATOM 584 CA TYR A 71 83.568 14.708 37.218 1.00 16.15 C ANISOU 584 CA TYR A 71 1772 2385 1980 -74 145 -93 C ATOM 585 C TYR A 71 82.483 14.475 36.172 1.00 16.12 C ANISOU 585 C TYR A 71 1755 2379 1991 -54 137 -100 C ATOM 586 O TYR A 71 81.613 13.618 36.341 1.00 16.57 O ANISOU 586 O TYR A 71 1805 2464 2026 -81 143 -111 O ATOM 587 CB TYR A 71 84.840 13.899 36.894 1.00 15.66 C ANISOU 587 CB TYR A 71 1751 2297 1901 -74 133 -38 C ATOM 588 CG TYR A 71 85.934 14.252 37.855 1.00 15.56 C ANISOU 588 CG TYR A 71 1748 2282 1880 -89 136 -32 C ATOM 589 CD1 TYR A 71 86.051 13.598 39.086 1.00 15.66 C ANISOU 589 CD1 TYR A 71 1772 2322 1856 -138 140 -33 C ATOM 590 CD2 TYR A 71 86.800 15.304 37.587 1.00 15.39 C ANISOU 590 CD2 TYR A 71 1725 2233 1887 -59 132 -27 C ATOM 591 CE1 TYR A 71 87.025 13.969 39.993 1.00 15.75 C ANISOU 591 CE1 TYR A 71 1793 2331 1861 -153 140 -28 C ATOM 592 CE2 TYR A 71 87.780 15.676 38.488 1.00 15.45 C ANISOU 592 CE2 TYR A 71 1740 2240 1890 -73 134 -24 C ATOM 593 CZ TYR A 71 87.886 15.007 39.687 1.00 15.75 C ANISOU 593 CZ TYR A 71 1789 2304 1893 -118 137 -25 C ATOM 594 OH TYR A 71 88.859 15.410 40.568 1.00 16.19 O ANISOU 594 OH TYR A 71 1851 2355 1944 -131 135 -21 O ATOM 595 N SER A 72 82.532 15.254 35.101 1.00 15.76 N ANISOU 595 N SER A 72 1708 2298 1983 -10 119 -94 N ATOM 596 CA SER A 72 81.584 15.106 34.020 1.00 15.67 C ANISOU 596 CA SER A 72 1689 2278 1988 11 104 -97 C ATOM 597 C SER A 72 82.227 15.345 32.667 1.00 14.99 C ANISOU 597 C SER A 72 1632 2147 1917 44 82 -56 C ATOM 598 O SER A 72 83.249 16.035 32.557 1.00 14.64 O ANISOU 598 O SER A 72 1602 2078 1882 57 78 -39 O ATOM 599 CB SER A 72 80.384 16.038 34.211 1.00 16.35 C ANISOU 599 CB SER A 72 1727 2374 2110 26 100 -155 C ATOM 600 OG SER A 72 80.746 17.394 34.090 1.00 17.34 O ANISOU 600 OG SER A 72 1845 2469 2275 57 85 -167 O ATOM 601 N LEU A 73 81.585 14.775 31.658 1.00 14.73 N ANISOU 601 N LEU A 73 1605 2107 1883 53 68 -44 N ATOM 602 CA LEU A 73 81.937 14.966 30.261 1.00 14.67 C ANISOU 602 CA LEU A 73 1626 2063 1886 78 47 -11 C ATOM 603 C LEU A 73 80.665 15.416 29.569 1.00 14.60 C ANISOU 603 C LEU A 73 1597 2045 1906 98 21 -33 C ATOM 604 O LEU A 73 79.599 14.836 29.789 1.00 14.36 O ANISOU 604 O LEU A 73 1544 2041 1873 89 25 -58 O ATOM 605 CB LEU A 73 82.452 13.652 29.671 1.00 14.78 C ANISOU 605 CB LEU A 73 1672 2078 1867 66 52 27 C ATOM 606 CG LEU A 73 82.744 13.590 28.160 1.00 15.12 C ANISOU 606 CG LEU A 73 1745 2092 1909 83 35 59 C ATOM 607 CD1 LEU A 73 83.680 12.430 27.857 1.00 15.43 C ANISOU 607 CD1 LEU A 73 1811 2132 1919 71 47 88 C ATOM 608 CD2 LEU A 73 81.488 13.476 27.307 1.00 15.72 C ANISOU 608 CD2 LEU A 73 1815 2164 1995 93 14 51 C ATOM 609 N THR A 74 80.776 16.449 28.741 1.00 14.52 N ANISOU 609 N THR A 74 1597 1997 1924 124 -7 -25 N ATOM 610 CA THR A 74 79.632 16.985 28.006 1.00 14.94 C ANISOU 610 CA THR A 74 1634 2031 2012 147 -43 -44 C ATOM 611 C THR A 74 79.904 17.022 26.508 1.00 14.78 C ANISOU 611 C THR A 74 1657 1975 1985 155 -73 1 C ATOM 612 O THR A 74 80.968 17.453 26.081 1.00 14.67 O ANISOU 612 O THR A 74 1676 1938 1962 153 -75 33 O ATOM 613 CB THR A 74 79.277 18.395 28.508 1.00 15.60 C ANISOU 613 CB THR A 74 1686 2097 2144 168 -64 -84 C ATOM 614 OG1 THR A 74 78.922 18.314 29.895 1.00 16.13 O ANISOU 614 OG1 THR A 74 1711 2205 2212 155 -33 -133 O ATOM 615 CG2 THR A 74 78.127 19.021 27.711 1.00 16.04 C ANISOU 615 CG2 THR A 74 1726 2124 2245 196 -113 -105 C ATOM 616 N ILE A 75 78.928 16.571 25.725 1.00 14.60 N ANISOU 616 N ILE A 75 1632 1949 1966 161 -94 0 N ATOM 617 CA ILE A 75 78.912 16.759 24.279 1.00 14.80 C ANISOU 617 CA ILE A 75 1696 1939 1990 168 -131 35 C ATOM 618 C ILE A 75 77.876 17.852 24.025 1.00 15.02 C ANISOU 618 C ILE A 75 1702 1935 2071 194 -183 7 C ATOM 619 O ILE A 75 76.701 17.686 24.342 1.00 14.86 O ANISOU 619 O ILE A 75 1639 1929 2076 205 -192 -34 O ATOM 620 CB ILE A 75 78.547 15.465 23.515 1.00 14.96 C ANISOU 620 CB ILE A 75 1733 1973 1977 156 -125 54 C ATOM 621 CG1 ILE A 75 79.383 14.292 24.022 1.00 14.90 C ANISOU 621 CG1 ILE A 75 1735 1997 1927 133 -78 68 C ATOM 622 CG2 ILE A 75 78.749 15.656 22.018 1.00 15.21 C ANISOU 622 CG2 ILE A 75 1812 1971 1996 155 -158 94 C ATOM 623 CD1 ILE A 75 79.100 12.979 23.334 1.00 14.85 C ANISOU 623 CD1 ILE A 75 1748 2004 1892 121 -73 85 C ATOM 624 N GLY A 76 78.312 18.983 23.479 1.00 15.27 N ANISOU 624 N GLY A 76 1759 1921 2120 204 -220 26 N ATOM 625 CA GLY A 76 77.438 20.145 23.337 1.00 15.82 C ANISOU 625 CA GLY A 76 1809 1953 2249 232 -278 -3 C ATOM 626 C GLY A 76 76.338 19.963 22.305 1.00 16.40 C ANISOU 626 C GLY A 76 1887 2006 2339 243 -327 0 C ATOM 627 O GLY A 76 75.284 20.591 22.392 1.00 17.13 O ANISOU 627 O GLY A 76 1943 2078 2488 270 -372 -41 O ATOM 628 N THR A 77 76.605 19.104 21.323 1.00 16.49 N ANISOU 628 N THR A 77 1942 2021 2303 221 -321 45 N ATOM 629 CA THR A 77 75.653 18.767 20.280 1.00 17.24 C ANISOU 629 CA THR A 77 2048 2099 2402 226 -364 54 C ATOM 630 C THR A 77 75.922 17.331 19.816 1.00 16.94 C ANISOU 630 C THR A 77 2035 2097 2306 200 -322 82 C ATOM 631 O THR A 77 76.934 17.066 19.176 1.00 16.73 O ANISOU 631 O THR A 77 2057 2068 2234 176 -305 125 O ATOM 632 CB THR A 77 75.728 19.778 19.113 1.00 18.01 C ANISOU 632 CB THR A 77 2195 2136 2512 226 -434 90 C ATOM 633 OG1 THR A 77 74.869 19.350 18.051 1.00 19.12 O ANISOU 633 OG1 THR A 77 2353 2262 2650 225 -476 104 O ATOM 634 CG2 THR A 77 77.135 19.949 18.553 1.00 17.84 C ANISOU 634 CG2 THR A 77 2235 2105 2440 194 -417 144 C ATOM 635 N MET A 78 75.043 16.398 20.177 1.00 16.93 N ANISOU 635 N MET A 78 1997 2130 2307 202 -304 53 N ATOM 636 CA MET A 78 75.264 14.985 19.870 1.00 16.98 C ANISOU 636 CA MET A 78 2022 2167 2261 179 -267 75 C ATOM 637 C MET A 78 75.275 14.761 18.358 1.00 17.18 C ANISOU 637 C MET A 78 2100 2167 2260 168 -299 117 C ATOM 638 O MET A 78 74.323 15.142 17.677 1.00 17.89 O ANISOU 638 O MET A 78 2190 2230 2376 180 -354 114 O ATOM 639 CB MET A 78 74.156 14.132 20.498 1.00 17.21 C ANISOU 639 CB MET A 78 2003 2234 2301 181 -251 35 C ATOM 640 CG MET A 78 74.313 12.628 20.300 1.00 17.15 C ANISOU 640 CG MET A 78 2013 2257 2244 156 -216 55 C ATOM 641 SD MET A 78 75.691 11.954 21.238 1.00 16.96 S ANISOU 641 SD MET A 78 2001 2263 2180 135 -154 68 S ATOM 642 CE MET A 78 75.716 10.281 20.587 1.00 16.89 C ANISOU 642 CE MET A 78 2021 2272 2125 113 -137 92 C ATOM 643 N AGLU A 79 76.330 14.127 17.854 0.50 17.04 N ANISOU 643 N AGLU A 79 2125 2159 2191 144 -268 153 N ATOM 644 N BGLU A 79 76.348 14.150 17.853 0.50 16.99 N ANISOU 644 N BGLU A 79 2120 2152 2185 144 -268 153 N ATOM 645 CA AGLU A 79 76.422 13.791 16.436 0.50 17.45 C ANISOU 645 CA AGLU A 79 2228 2194 2207 125 -289 189 C ATOM 646 CA BGLU A 79 76.468 13.797 16.435 0.50 17.36 C ANISOU 646 CA BGLU A 79 2218 2183 2195 125 -288 190 C ATOM 647 C AGLU A 79 76.451 12.287 16.254 0.50 17.10 C ANISOU 647 C AGLU A 79 2189 2184 2125 111 -252 192 C ATOM 648 C BGLU A 79 76.423 12.286 16.266 0.50 17.06 C ANISOU 648 C BGLU A 79 2182 2178 2120 111 -253 192 C ATOM 649 O AGLU A 79 76.819 11.552 17.172 0.50 16.48 O ANISOU 649 O AGLU A 79 2087 2136 2038 109 -207 177 O ATOM 650 O BGLU A 79 76.728 11.545 17.203 0.50 16.48 O ANISOU 650 O BGLU A 79 2084 2136 2040 110 -208 175 O ATOM 651 CB AGLU A 79 77.647 14.462 15.818 0.50 17.84 C ANISOU 651 CB AGLU A 79 2326 2224 2229 104 -287 225 C ATOM 652 CB BGLU A 79 77.770 14.347 15.849 0.50 17.63 C ANISOU 652 CB BGLU A 79 2301 2202 2197 102 -280 225 C ATOM 653 CG AGLU A 79 77.551 15.979 15.880 0.50 18.44 C ANISOU 653 CG AGLU A 79 2405 2259 2343 115 -335 226 C ATOM 654 CG BGLU A 79 77.905 15.863 15.931 0.50 18.15 C ANISOU 654 CG BGLU A 79 2373 2229 2295 110 -320 230 C ATOM 655 CD AGLU A 79 78.595 16.687 15.047 0.50 19.05 C ANISOU 655 CD AGLU A 79 2538 2311 2387 85 -346 267 C ATOM 656 CD BGLU A 79 76.745 16.605 15.297 0.50 18.96 C ANISOU 656 CD BGLU A 79 2481 2290 2434 124 -396 230 C ATOM 657 OE1AGLU A 79 79.394 16.005 14.375 0.50 19.53 O ANISOU 657 OE1AGLU A 79 2634 2392 2395 55 -312 289 O ATOM 658 OE1BGLU A 79 76.238 16.163 14.242 0.50 19.31 O ANISOU 658 OE1BGLU A 79 2555 2325 2457 111 -424 250 O ATOM 659 OE2AGLU A 79 78.602 17.936 15.070 0.50 19.84 O ANISOU 659 OE2AGLU A 79 2649 2374 2517 90 -389 273 O ATOM 660 OE2BGLU A 79 76.348 17.649 15.857 0.50 19.84 O ANISOU 660 OE2BGLU A 79 2566 2374 2597 148 -431 209 O ATOM 661 N ALA A 80 76.060 11.838 15.064 1.00 17.31 N ANISOU 661 N ALA A 80 2249 2201 2128 99 -276 212 N ATOM 662 CA ALA A 80 75.992 10.397 14.740 1.00 17.39 C ANISOU 662 CA ALA A 80 2266 2236 2104 85 -250 214 C ATOM 663 C ALA A 80 77.297 9.661 15.029 1.00 17.40 C ANISOU 663 C ALA A 80 2279 2261 2071 71 -194 220 C ATOM 664 O ALA A 80 77.278 8.541 15.544 1.00 17.10 O ANISOU 664 O ALA A 80 2225 2248 2024 70 -165 207 O ATOM 665 CB ALA A 80 75.608 10.216 13.278 1.00 17.79 C ANISOU 665 CB ALA A 80 2361 2269 2128 70 -285 239 C ATOM 666 N GLU A 81 78.427 10.312 14.750 1.00 17.78 N ANISOU 666 N GLU A 81 2353 2299 2103 59 -182 237 N ATOM 667 CA GLU A 81 79.740 9.704 14.993 1.00 18.11 C ANISOU 667 CA GLU A 81 2401 2362 2119 47 -132 237 C ATOM 668 C GLU A 81 80.166 9.614 16.465 1.00 16.98 C ANISOU 668 C GLU A 81 2219 2235 1998 61 -102 217 C ATOM 669 O GLU A 81 81.179 8.989 16.768 1.00 17.39 O ANISOU 669 O GLU A 81 2271 2301 2035 55 -66 214 O ATOM 670 CB GLU A 81 80.828 10.421 14.191 1.00 19.38 C ANISOU 670 CB GLU A 81 2598 2512 2252 24 -127 257 C ATOM 671 CG GLU A 81 81.171 11.841 14.652 1.00 20.64 C ANISOU 671 CG GLU A 81 2755 2652 2435 28 -140 264 C ATOM 672 CD GLU A 81 82.401 12.400 13.954 1.00 22.13 C ANISOU 672 CD GLU A 81 2979 2837 2591 -3 -125 283 C ATOM 673 OE1 GLU A 81 83.033 11.668 13.164 1.00 24.81 O ANISOU 673 OE1 GLU A 81 3341 3194 2890 -27 -99 286 O ATOM 674 OE2 GLU A 81 82.745 13.574 14.185 1.00 23.28 O ANISOU 674 OE2 GLU A 81 3130 2964 2751 -5 -140 292 O ATOM 675 N ASP A 82 79.403 10.224 17.373 1.00 16.12 N ANISOU 675 N ASP A 82 2076 2123 1925 79 -117 200 N ATOM 676 CA ASP A 82 79.697 10.183 18.805 1.00 15.27 C ANISOU 676 CA ASP A 82 1934 2033 1835 86 -91 181 C ATOM 677 C ASP A 82 79.169 8.945 19.539 1.00 14.99 C ANISOU 677 C ASP A 82 1876 2023 1795 83 -75 164 C ATOM 678 O ASP A 82 79.396 8.796 20.748 1.00 14.46 O ANISOU 678 O ASP A 82 1785 1973 1736 82 -54 150 O ATOM 679 CB ASP A 82 79.173 11.458 19.485 1.00 15.24 C ANISOU 679 CB ASP A 82 1903 2018 1871 102 -112 164 C ATOM 680 CG ASP A 82 79.791 12.731 18.916 1.00 15.30 C ANISOU 680 CG ASP A 82 1934 1995 1883 102 -131 183 C ATOM 681 OD1 ASP A 82 80.951 12.688 18.445 1.00 15.16 O ANISOU 681 OD1 ASP A 82 1946 1976 1837 86 -111 203 O ATOM 682 OD2 ASP A 82 79.123 13.787 18.933 1.00 15.29 O ANISOU 682 OD2 ASP A 82 1923 1971 1916 116 -169 174 O ATOM 683 N AVAL A 83 78.467 8.064 18.830 0.50 14.96 N ANISOU 683 N AVAL A 83 1884 2024 1779 78 -86 168 N ATOM 684 N BVAL A 83 78.467 8.060 18.829 0.50 14.94 N ANISOU 684 N BVAL A 83 1881 2021 1776 78 -86 168 N ATOM 685 CA AVAL A 83 78.029 6.808 19.413 0.50 14.94 C ANISOU 685 CA AVAL A 83 1867 2042 1766 69 -74 157 C ATOM 686 CA BVAL A 83 78.019 6.803 19.417 0.50 14.90 C ANISOU 686 CA BVAL A 83 1862 2037 1761 69 -74 157 C ATOM 687 C AVAL A 83 79.265 5.969 19.739 0.50 14.70 C ANISOU 687 C AVAL A 83 1852 2018 1717 60 -46 164 C ATOM 688 C BVAL A 83 79.255 5.958 19.736 0.50 14.68 C ANISOU 688 C BVAL A 83 1849 2016 1714 60 -46 164 C ATOM 689 O AVAL A 83 80.101 5.704 18.867 0.50 14.85 O ANISOU 689 O AVAL A 83 1898 2028 1718 58 -39 176 O ATOM 690 O BVAL A 83 80.082 5.682 18.860 0.50 14.86 O ANISOU 690 O BVAL A 83 1898 2028 1718 58 -39 176 O ATOM 691 CB AVAL A 83 77.083 6.054 18.472 0.50 15.16 C ANISOU 691 CB AVAL A 83 1908 2070 1784 64 -95 161 C ATOM 692 CB BVAL A 83 77.030 6.059 18.500 0.50 15.10 C ANISOU 692 CB BVAL A 83 1898 2062 1777 64 -95 160 C ATOM 693 CG1AVAL A 83 76.781 4.676 19.033 0.50 15.19 C ANISOU 693 CG1AVAL A 83 1905 2093 1774 49 -83 153 C ATOM 694 CG1BVAL A 83 75.850 6.962 18.184 0.50 15.40 C ANISOU 694 CG1BVAL A 83 1919 2090 1841 76 -130 150 C ATOM 695 CG2AVAL A 83 75.807 6.857 18.283 0.50 15.45 C ANISOU 695 CG2AVAL A 83 1923 2100 1848 75 -128 148 C ATOM 696 CG2BVAL A 83 77.709 5.579 17.224 0.50 15.19 C ANISOU 696 CG2BVAL A 83 1952 2061 1759 58 -95 180 C ATOM 697 N ALA A 84 79.379 5.604 21.010 1.00 14.40 N ANISOU 697 N ALA A 84 1794 1996 1684 53 -31 153 N ATOM 698 CA ALA A 84 80.597 4.998 21.561 1.00 14.22 C ANISOU 698 CA ALA A 84 1778 1972 1651 47 -12 158 C ATOM 699 C ALA A 84 80.359 4.726 23.023 1.00 14.25 C ANISOU 699 C ALA A 84 1761 1994 1659 33 -6 147 C ATOM 700 O ALA A 84 79.365 5.168 23.608 1.00 14.36 O ANISOU 700 O ALA A 84 1751 2024 1682 27 -9 131 O ATOM 701 CB ALA A 84 81.791 5.944 21.426 1.00 14.18 C ANISOU 701 CB ALA A 84 1779 1956 1652 57 0 163 C ATOM 702 N THR A 85 81.298 4.007 23.617 1.00 14.34 N ANISOU 702 N THR A 85 1783 2003 1663 25 1 152 N ATOM 703 CA THR A 85 81.365 3.887 25.058 1.00 14.41 C ANISOU 703 CA THR A 85 1778 2025 1671 6 6 146 C ATOM 704 C THR A 85 82.447 4.833 25.574 1.00 14.06 C ANISOU 704 C THR A 85 1727 1976 1640 16 19 145 C ATOM 705 O THR A 85 83.527 4.910 24.991 1.00 14.30 O ANISOU 705 O THR A 85 1770 1990 1674 31 23 153 O ATOM 706 CB THR A 85 81.649 2.442 25.468 1.00 15.06 C ANISOU 706 CB THR A 85 1880 2104 1739 -13 -6 155 C ATOM 707 OG1 THR A 85 80.599 1.615 24.961 1.00 16.31 O ANISOU 707 OG1 THR A 85 2045 2268 1886 -25 -18 156 O ATOM 708 CG2 THR A 85 81.709 2.317 26.971 1.00 15.15 C ANISOU 708 CG2 THR A 85 1885 2129 1743 -42 -5 153 C ATOM 709 N TYR A 86 82.121 5.548 26.647 1.00 13.91 N ANISOU 709 N TYR A 86 1686 1972 1626 6 26 132 N ATOM 710 CA TYR A 86 82.973 6.574 27.235 1.00 13.84 C ANISOU 710 CA TYR A 86 1668 1961 1630 14 37 129 C ATOM 711 C TYR A 86 83.392 6.117 28.612 1.00 13.85 C ANISOU 711 C TYR A 86 1668 1972 1621 -11 40 128 C ATOM 712 O TYR A 86 82.543 5.749 29.430 1.00 14.55 O ANISOU 712 O TYR A 86 1749 2083 1696 -39 39 118 O ATOM 713 CB TYR A 86 82.231 7.918 27.315 1.00 13.59 C ANISOU 713 CB TYR A 86 1611 1936 1617 24 40 110 C ATOM 714 CG TYR A 86 81.946 8.479 25.943 1.00 13.52 C ANISOU 714 CG TYR A 86 1609 1908 1618 47 29 116 C ATOM 715 CD1 TYR A 86 80.824 8.077 25.213 1.00 13.60 C ANISOU 715 CD1 TYR A 86 1619 1921 1626 48 15 113 C ATOM 716 CD2 TYR A 86 82.821 9.388 25.360 1.00 13.44 C ANISOU 716 CD2 TYR A 86 1609 1878 1618 63 30 127 C ATOM 717 CE1 TYR A 86 80.584 8.570 23.931 1.00 13.61 C ANISOU 717 CE1 TYR A 86 1633 1904 1635 65 -1 122 C ATOM 718 CE2 TYR A 86 82.598 9.889 24.086 1.00 13.43 C ANISOU 718 CE2 TYR A 86 1623 1859 1620 75 16 137 C ATOM 719 CZ TYR A 86 81.479 9.488 23.368 1.00 13.46 C ANISOU 719 CZ TYR A 86 1629 1864 1622 76 -2 135 C ATOM 720 OH TYR A 86 81.285 9.988 22.086 1.00 13.94 O ANISOU 720 OH TYR A 86 1710 1905 1683 84 -21 149 O ATOM 721 N TYR A 87 84.703 6.124 28.865 1.00 13.91 N ANISOU 721 N TYR A 87 1686 1965 1634 -5 40 138 N ATOM 722 CA TYR A 87 85.279 5.669 30.138 1.00 13.91 C ANISOU 722 CA TYR A 87 1692 1969 1626 -29 34 142 C ATOM 723 C TYR A 87 86.015 6.793 30.820 1.00 14.00 C ANISOU 723 C TYR A 87 1689 1981 1649 -24 46 135 C ATOM 724 O TYR A 87 86.795 7.495 30.180 1.00 13.98 O ANISOU 724 O TYR A 87 1685 1964 1664 1 54 137 O ATOM 725 CB TYR A 87 86.312 4.576 29.882 1.00 14.21 C ANISOU 725 CB TYR A 87 1751 1982 1666 -24 16 157 C ATOM 726 CG TYR A 87 85.767 3.299 29.320 1.00 14.63 C ANISOU 726 CG TYR A 87 1821 2028 1707 -31 -1 164 C ATOM 727 CD1 TYR A 87 85.226 2.338 30.167 1.00 15.18 C ANISOU 727 CD1 TYR A 87 1906 2105 1758 -67 -21 171 C ATOM 728 CD2 TYR A 87 85.813 3.028 27.959 1.00 15.12 C ANISOU 728 CD2 TYR A 87 1890 2079 1777 -7 0 164 C ATOM 729 CE1 TYR A 87 84.726 1.152 29.674 1.00 15.43 C ANISOU 729 CE1 TYR A 87 1956 2127 1779 -76 -40 179 C ATOM 730 CE2 TYR A 87 85.320 1.831 27.454 1.00 15.40 C ANISOU 730 CE2 TYR A 87 1942 2107 1803 -13 -18 169 C ATOM 731 CZ TYR A 87 84.780 0.903 28.322 1.00 15.59 C ANISOU 731 CZ TYR A 87 1979 2134 1811 -46 -39 177 C ATOM 732 OH TYR A 87 84.276 -0.287 27.843 1.00 16.71 O ANISOU 732 OH TYR A 87 2139 2267 1944 -54 -59 182 O ATOM 733 N CYS A 88 85.802 6.942 32.120 1.00 13.73 N ANISOU 733 N CYS A 88 1649 1965 1603 -53 49 127 N ATOM 734 CA CYS A 88 86.680 7.766 32.938 1.00 13.99 C ANISOU 734 CA CYS A 88 1675 1996 1644 -53 55 124 C ATOM 735 C CYS A 88 87.745 6.870 33.548 1.00 13.44 C ANISOU 735 C CYS A 88 1626 1910 1569 -67 34 142 C ATOM 736 O CYS A 88 87.580 5.648 33.626 1.00 13.09 O ANISOU 736 O CYS A 88 1603 1861 1511 -85 13 154 O ATOM 737 CB CYS A 88 85.914 8.550 33.995 1.00 14.75 C ANISOU 737 CB CYS A 88 1751 2122 1732 -76 70 99 C ATOM 738 SG CYS A 88 84.962 7.586 35.169 1.00 15.99 S ANISOU 738 SG CYS A 88 1915 2312 1850 -134 66 93 S ATOM 739 N GLN A 89 88.842 7.491 33.963 1.00 13.03 N ANISOU 739 N GLN A 89 1571 1849 1532 -58 35 143 N ATOM 740 CA GLN A 89 90.008 6.766 34.469 1.00 13.16 C ANISOU 740 CA GLN A 89 1603 1844 1553 -64 10 157 C ATOM 741 C GLN A 89 90.763 7.677 35.415 1.00 13.07 C ANISOU 741 C GLN A 89 1584 1836 1548 -70 15 153 C ATOM 742 O GLN A 89 91.004 8.840 35.088 1.00 12.96 O ANISOU 742 O GLN A 89 1551 1823 1550 -49 37 142 O ATOM 743 CB GLN A 89 90.901 6.354 33.297 1.00 13.20 C ANISOU 743 CB GLN A 89 1609 1823 1583 -29 4 161 C ATOM 744 CG GLN A 89 92.207 5.653 33.684 1.00 13.41 C ANISOU 744 CG GLN A 89 1644 1824 1628 -26 -25 167 C ATOM 745 CD GLN A 89 93.407 6.577 33.644 1.00 13.21 C ANISOU 745 CD GLN A 89 1600 1792 1627 -6 -13 159 C ATOM 746 OE1 GLN A 89 93.628 7.287 32.666 1.00 13.11 O ANISOU 746 OE1 GLN A 89 1572 1781 1626 17 14 150 O ATOM 747 NE2 GLN A 89 94.209 6.544 34.695 1.00 13.37 N ANISOU 747 NE2 GLN A 89 1623 1802 1655 -18 -34 163 N ATOM 748 N GLN A 90 91.150 7.147 36.572 1.00 13.24 N ANISOU 748 N GLN A 90 1621 1854 1556 -102 -10 162 N ATOM 749 CA GLN A 90 91.947 7.901 37.543 1.00 13.46 C ANISOU 749 CA GLN A 90 1644 1882 1587 -111 -10 160 C ATOM 750 C GLN A 90 93.382 7.375 37.639 1.00 13.65 C ANISOU 750 C GLN A 90 1676 1873 1635 -98 -42 172 C ATOM 751 O GLN A 90 93.622 6.152 37.600 1.00 13.41 O ANISOU 751 O GLN A 90 1666 1822 1608 -103 -78 186 O ATOM 752 CB GLN A 90 91.271 7.944 38.929 1.00 13.86 C ANISOU 752 CB GLN A 90 1705 1960 1601 -163 -12 156 C ATOM 753 CG GLN A 90 91.214 6.629 39.693 1.00 14.11 C ANISOU 753 CG GLN A 90 1772 1985 1605 -207 -51 178 C ATOM 754 CD GLN A 90 92.505 6.293 40.417 1.00 14.18 C ANISOU 754 CD GLN A 90 1800 1965 1625 -215 -92 195 C ATOM 755 OE1 GLN A 90 93.267 7.181 40.798 1.00 14.25 O ANISOU 755 OE1 GLN A 90 1794 1972 1647 -204 -83 188 O ATOM 756 NE2 GLN A 90 92.766 4.997 40.584 1.00 14.52 N ANISOU 756 NE2 GLN A 90 1873 1981 1663 -232 -140 218 N ATOM 757 N GLY A 91 94.321 8.310 37.774 1.00 14.02 N ANISOU 757 N GLY A 91 1708 1916 1705 -82 -32 165 N ATOM 758 CA GLY A 91 95.720 7.987 38.005 1.00 14.35 C ANISOU 758 CA GLY A 91 1749 1929 1773 -71 -61 171 C ATOM 759 C GLY A 91 96.281 8.584 39.270 1.00 14.86 C ANISOU 759 C GLY A 91 1817 1997 1832 -94 -72 173 C ATOM 760 O GLY A 91 97.490 8.713 39.413 1.00 15.04 O ANISOU 760 O GLY A 91 1831 2000 1883 -80 -88 172 O ATOM 761 N SER A 92 95.395 8.955 40.188 1.00 15.53 N ANISOU 761 N SER A 92 1912 2109 1881 -131 -61 171 N ATOM 762 CA SER A 92 95.787 9.534 41.469 1.00 16.58 C ANISOU 762 CA SER A 92 2051 2249 2001 -161 -69 171 C ATOM 763 C SER A 92 96.401 8.492 42.396 1.00 17.17 C ANISOU 763 C SER A 92 2156 2301 2066 -192 -125 193 C ATOM 764 O SER A 92 97.421 8.755 43.027 1.00 17.39 O ANISOU 764 O SER A 92 2184 2314 2108 -195 -147 197 O ATOM 765 CB SER A 92 94.566 10.170 42.138 1.00 17.18 C ANISOU 765 CB SER A 92 2126 2365 2039 -196 -38 155 C ATOM 766 OG SER A 92 94.880 10.615 43.444 1.00 18.53 O ANISOU 766 OG SER A 92 2305 2546 2188 -233 -46 153 O ATOM 767 N ASER A 93 95.779 7.325 42.500 0.50 17.50 N ANISOU 767 N ASER A 93 2225 2339 2085 -219 -152 209 N ATOM 768 N BSER A 93 95.762 7.320 42.449 0.50 17.37 N ANISOU 768 N BSER A 93 2208 2323 2069 -217 -151 208 N ATOM 769 CA ASER A 93 96.312 6.276 43.361 0.50 18.11 C ANISOU 769 CA ASER A 93 2339 2388 2153 -252 -215 234 C ATOM 770 CA BSER A 93 96.105 6.230 43.366 0.50 17.93 C ANISOU 770 CA BSER A 93 2318 2369 2124 -258 -212 234 C ATOM 771 C ASER A 93 96.379 4.958 42.628 0.50 18.15 C ANISOU 771 C ASER A 93 2358 2360 2179 -235 -254 247 C ATOM 772 C BSER A 93 96.375 4.948 42.586 0.50 18.03 C ANISOU 772 C BSER A 93 2341 2344 2164 -233 -253 247 C ATOM 773 O ASER A 93 95.591 4.677 41.723 0.50 18.12 O ANISOU 773 O ASER A 93 2347 2366 2173 -219 -230 241 O ATOM 774 O BSER A 93 95.715 4.687 41.576 0.50 17.97 O ANISOU 774 O BSER A 93 2324 2344 2161 -211 -229 239 O ATOM 775 CB ASER A 93 95.472 6.121 44.621 0.50 18.67 C ANISOU 775 CB ASER A 93 2443 2487 2163 -326 -223 244 C ATOM 776 CB BSER A 93 94.933 5.998 44.323 0.50 18.28 C ANISOU 776 CB BSER A 93 2392 2449 2106 -326 -209 241 C ATOM 777 OG ASER A 93 94.215 5.575 44.303 0.50 18.94 O ANISOU 777 OG ASER A 93 2486 2543 2166 -348 -206 244 O ATOM 778 OG BSER A 93 94.929 4.685 44.860 0.50 18.92 O ANISOU 778 OG BSER A 93 2518 2505 2165 -369 -270 271 O ATOM 779 N LEU A 94 97.351 4.157 43.040 1.00 18.36 N ANISOU 779 N LEU A 94 2405 2344 2229 -236 -318 263 N ATOM 780 CA LEU A 94 97.547 2.821 42.515 1.00 18.63 C ANISOU 780 CA LEU A 94 2454 2337 2287 -221 -370 273 C ATOM 781 C LEU A 94 96.659 1.861 43.318 1.00 18.92 C ANISOU 781 C LEU A 94 2543 2373 2272 -287 -410 303 C ATOM 782 O LEU A 94 96.561 2.016 44.542 1.00 19.64 O ANISOU 782 O LEU A 94 2663 2475 2322 -344 -428 320 O ATOM 783 CB LEU A 94 99.018 2.419 42.630 1.00 19.02 C ANISOU 783 CB LEU A 94 2498 2337 2392 -191 -428 272 C ATOM 784 CG LEU A 94 99.990 3.284 41.827 1.00 18.91 C ANISOU 784 CG LEU A 94 2431 2325 2429 -132 -391 240 C ATOM 785 CD1 LEU A 94 101.409 2.754 42.014 1.00 19.36 C ANISOU 785 CD1 LEU A 94 2479 2333 2545 -107 -455 234 C ATOM 786 CD2 LEU A 94 99.634 3.370 40.346 1.00 18.64 C ANISOU 786 CD2 LEU A 94 2366 2305 2412 -89 -339 217 C ATOM 787 N PRO A 95 96.015 0.888 42.677 1.00 18.29 N ANISOU 787 N PRO A 95 2478 2283 2190 -286 -423 309 N ATOM 788 CA PRO A 95 96.080 0.668 41.236 1.00 17.77 C ANISOU 788 CA PRO A 95 2380 2206 2166 -224 -401 288 C ATOM 789 C PRO A 95 95.274 1.685 40.441 1.00 16.90 C ANISOU 789 C PRO A 95 2235 2144 2042 -204 -318 266 C ATOM 790 O PRO A 95 94.250 2.181 40.900 1.00 16.73 O ANISOU 790 O PRO A 95 2219 2163 1974 -243 -283 267 O ATOM 791 CB PRO A 95 95.479 -0.727 41.062 1.00 18.24 C ANISOU 791 CB PRO A 95 2476 2240 2214 -246 -447 307 C ATOM 792 CG PRO A 95 94.548 -0.878 42.214 1.00 18.70 C ANISOU 792 CG PRO A 95 2577 2324 2205 -326 -457 334 C ATOM 793 CD PRO A 95 95.174 -0.126 43.349 1.00 18.54 C ANISOU 793 CD PRO A 95 2561 2310 2172 -352 -464 339 C ATOM 794 N LEU A 96 95.756 1.975 39.244 1.00 16.25 N ANISOU 794 N LEU A 96 2117 2056 2002 -146 -290 243 N ATOM 795 CA LEU A 96 95.025 2.799 38.290 1.00 15.92 C ANISOU 795 CA LEU A 96 2047 2050 1953 -123 -223 225 C ATOM 796 C LEU A 96 93.718 2.082 37.964 1.00 15.63 C ANISOU 796 C LEU A 96 2029 2026 1884 -145 -220 233 C ATOM 797 O LEU A 96 93.705 0.853 37.809 1.00 15.65 O ANISOU 797 O LEU A 96 2056 2000 1893 -150 -265 244 O ATOM 798 CB LEU A 96 95.856 2.990 37.018 1.00 15.94 C ANISOU 798 CB LEU A 96 2016 2039 2002 -65 -205 202 C ATOM 799 CG LEU A 96 97.289 3.512 37.201 1.00 16.38 C ANISOU 799 CG LEU A 96 2048 2078 2097 -41 -212 189 C ATOM 800 CD1 LEU A 96 98.020 3.491 35.877 1.00 16.46 C ANISOU 800 CD1 LEU A 96 2026 2079 2148 7 -193 162 C ATOM 801 CD2 LEU A 96 97.314 4.916 37.777 1.00 16.39 C ANISOU 801 CD2 LEU A 96 2037 2108 2083 -52 -175 187 C ATOM 802 N THR A 97 92.620 2.839 37.881 1.00 15.17 N ANISOU 802 N THR A 97 1960 2009 1795 -159 -172 225 N ATOM 803 CA THR A 97 91.305 2.249 37.658 1.00 15.26 C ANISOU 803 CA THR A 97 1986 2039 1775 -185 -165 230 C ATOM 804 C THR A 97 90.482 3.019 36.635 1.00 14.73 C ANISOU 804 C THR A 97 1889 1999 1709 -158 -113 210 C ATOM 805 O THR A 97 90.679 4.225 36.442 1.00 14.22 O ANISOU 805 O THR A 97 1797 1948 1657 -135 -77 195 O ATOM 806 CB THR A 97 90.490 2.155 38.965 1.00 15.62 C ANISOU 806 CB THR A 97 2054 2112 1770 -253 -171 241 C ATOM 807 OG1 THR A 97 90.434 3.436 39.596 1.00 15.78 O ANISOU 807 OG1 THR A 97 2053 2164 1780 -262 -134 224 O ATOM 808 CG2 THR A 97 91.090 1.112 39.922 1.00 16.18 C ANISOU 808 CG2 THR A 97 2168 2151 1830 -293 -237 269 C ATOM 809 N PHE A 98 89.560 2.292 36.005 1.00 14.65 N ANISOU 809 N PHE A 98 1886 1992 1686 -163 -114 213 N ATOM 810 CA PHE A 98 88.614 2.825 35.030 1.00 14.56 C ANISOU 810 CA PHE A 98 1854 2005 1675 -143 -75 197 C ATOM 811 C PHE A 98 87.211 2.662 35.583 1.00 14.89 C ANISOU 811 C PHE A 98 1899 2080 1677 -189 -65 194 C ATOM 812 O PHE A 98 86.928 1.722 36.335 1.00 15.63 O ANISOU 812 O PHE A 98 2021 2173 1743 -235 -93 210 O ATOM 813 CB PHE A 98 88.658 2.048 33.716 1.00 14.47 C ANISOU 813 CB PHE A 98 1846 1970 1681 -110 -84 198 C ATOM 814 CG PHE A 98 89.927 2.214 32.921 1.00 14.38 C ANISOU 814 CG PHE A 98 1823 1933 1707 -65 -84 191 C ATOM 815 CD1 PHE A 98 91.039 1.433 33.199 1.00 14.69 C ANISOU 815 CD1 PHE A 98 1874 1939 1769 -58 -123 196 C ATOM 816 CD2 PHE A 98 89.983 3.084 31.844 1.00 14.21 C ANISOU 816 CD2 PHE A 98 1780 1921 1700 -31 -49 177 C ATOM 817 CE1 PHE A 98 92.201 1.555 32.450 1.00 14.75 C ANISOU 817 CE1 PHE A 98 1864 1927 1814 -18 -119 181 C ATOM 818 CE2 PHE A 98 91.138 3.209 31.093 1.00 14.08 C ANISOU 818 CE2 PHE A 98 1752 1886 1713 2 -44 167 C ATOM 819 CZ PHE A 98 92.245 2.432 31.387 1.00 14.54 C ANISOU 819 CZ PHE A 98 1814 1916 1794 9 -77 165 C ATOM 820 N GLY A 99 86.319 3.561 35.183 1.00 14.89 N ANISOU 820 N GLY A 99 1871 2109 1676 -178 -27 173 N ATOM 821 CA GLY A 99 84.887 3.332 35.370 1.00 15.30 C ANISOU 821 CA GLY A 99 1918 2195 1700 -213 -15 162 C ATOM 822 C GLY A 99 84.414 2.236 34.432 1.00 15.55 C ANISOU 822 C GLY A 99 1965 2212 1730 -207 -32 174 C ATOM 823 O GLY A 99 85.140 1.824 33.512 1.00 15.32 O ANISOU 823 O GLY A 99 1945 2149 1725 -170 -48 185 O ATOM 824 N ALA A 100 83.180 1.788 34.644 1.00 16.07 N ANISOU 824 N ALA A 100 2032 2306 1769 -246 -28 167 N ATOM 825 CA ALA A 100 82.591 0.705 33.858 1.00 16.73 C ANISOU 825 CA ALA A 100 2132 2379 1847 -248 -46 178 C ATOM 826 C ALA A 100 82.113 1.119 32.463 1.00 16.81 C ANISOU 826 C ALA A 100 2119 2387 1880 -200 -28 165 C ATOM 827 O ALA A 100 81.768 0.257 31.653 1.00 17.56 O ANISOU 827 O ALA A 100 2228 2469 1975 -195 -43 174 O ATOM 828 CB ALA A 100 81.454 0.048 34.633 1.00 17.29 C ANISOU 828 CB ALA A 100 2211 2482 1875 -314 -48 177 C ATOM 829 N GLY A 101 82.083 2.424 32.186 1.00 16.54 N ANISOU 829 N GLY A 101 2054 2364 1867 -169 0 145 N ATOM 830 CA GLY A 101 81.723 2.925 30.873 1.00 16.83 C ANISOU 830 CA GLY A 101 2075 2394 1926 -127 10 137 C ATOM 831 C GLY A 101 80.276 3.370 30.806 1.00 17.29 C ANISOU 831 C GLY A 101 2104 2484 1981 -137 25 111 C ATOM 832 O GLY A 101 79.400 2.826 31.502 1.00 18.13 O ANISOU 832 O GLY A 101 2207 2618 2063 -181 26 102 O ATOM 833 N THR A 102 80.038 4.393 29.995 1.00 17.26 N ANISOU 833 N THR A 102 2079 2476 2004 -99 34 97 N ATOM 834 CA THR A 102 78.690 4.834 29.644 1.00 17.43 C ANISOU 834 CA THR A 102 2070 2517 2034 -97 39 71 C ATOM 835 C THR A 102 78.568 4.681 28.144 1.00 17.53 C ANISOU 835 C THR A 102 2096 2506 2060 -64 25 85 C ATOM 836 O THR A 102 79.368 5.251 27.398 1.00 16.57 O ANISOU 836 O THR A 102 1984 2359 1953 -31 23 97 O ATOM 837 CB THR A 102 78.471 6.307 30.019 1.00 17.84 C ANISOU 837 CB THR A 102 2086 2581 2111 -80 54 40 C ATOM 838 OG1 THR A 102 78.466 6.447 31.446 1.00 18.04 O ANISOU 838 OG1 THR A 102 2098 2635 2121 -116 70 21 O ATOM 839 CG2 THR A 102 77.156 6.826 29.458 1.00 18.10 C ANISOU 839 CG2 THR A 102 2085 2625 2166 -66 50 10 C ATOM 840 N LYS A 103 77.560 3.926 27.708 1.00 17.85 N ANISOU 840 N LYS A 103 2135 2556 2090 -77 16 82 N ATOM 841 CA LYS A 103 77.322 3.706 26.294 1.00 18.54 C ANISOU 841 CA LYS A 103 2237 2623 2186 -51 1 94 C ATOM 842 C LYS A 103 76.327 4.732 25.767 1.00 18.31 C ANISOU 842 C LYS A 103 2177 2599 2183 -30 -5 70 C ATOM 843 O LYS A 103 75.179 4.755 26.213 1.00 18.76 O ANISOU 843 O LYS A 103 2203 2683 2244 -47 -2 42 O ATOM 844 CB LYS A 103 76.773 2.302 26.082 1.00 19.80 C ANISOU 844 CB LYS A 103 2414 2787 2322 -76 -11 104 C ATOM 845 CG LYS A 103 76.647 1.922 24.628 1.00 21.00 C ANISOU 845 CG LYS A 103 2586 2917 2477 -53 -27 117 C ATOM 846 CD LYS A 103 76.299 0.453 24.512 1.00 22.20 C ANISOU 846 CD LYS A 103 2760 3069 2607 -79 -41 129 C ATOM 847 CE LYS A 103 76.335 -0.014 23.074 1.00 23.12 C ANISOU 847 CE LYS A 103 2900 3163 2723 -57 -56 141 C ATOM 848 NZ LYS A 103 75.862 -1.423 23.022 1.00 23.95 N ANISOU 848 NZ LYS A 103 3024 3268 2808 -84 -71 149 N ATOM 849 N ALEU A 104 76.774 5.594 24.860 0.50 17.79 N ANISOU 849 N ALEU A 104 2119 2506 2135 4 -14 79 N ATOM 850 N BLEU A 104 76.756 5.533 24.792 0.50 18.17 N ANISOU 850 N BLEU A 104 2168 2553 2182 4 -14 80 N ATOM 851 CA ALEU A 104 75.917 6.623 24.276 0.50 17.98 C ANISOU 851 CA ALEU A 104 2120 2524 2189 26 -30 61 C ATOM 852 CA BLEU A 104 75.896 6.520 24.127 0.50 18.59 C ANISOU 852 CA BLEU A 104 2200 2599 2264 27 -32 64 C ATOM 853 C ALEU A 104 75.503 6.218 22.879 0.50 18.26 C ANISOU 853 C ALEU A 104 2177 2541 2220 37 -54 78 C ATOM 854 C BLEU A 104 75.289 5.997 22.831 0.50 18.90 C ANISOU 854 C BLEU A 104 2258 2625 2299 34 -56 77 C ATOM 855 O ALEU A 104 76.343 5.928 22.019 0.50 17.99 O ANISOU 855 O ALEU A 104 2180 2485 2170 44 -56 106 O ATOM 856 O BLEU A 104 75.996 5.521 21.937 0.50 18.79 O ANISOU 856 O BLEU A 104 2281 2592 2267 38 -59 105 O ATOM 857 CB ALEU A 104 76.628 7.979 24.246 0.50 17.82 C ANISOU 857 CB ALEU A 104 2098 2483 2191 51 -32 61 C ATOM 858 CB BLEU A 104 76.682 7.795 23.820 0.50 18.73 C ANISOU 858 CB BLEU A 104 2224 2591 2302 53 -37 71 C ATOM 859 CG ALEU A 104 76.908 8.619 25.610 0.50 17.79 C ANISOU 859 CG ALEU A 104 2067 2496 2197 43 -12 38 C ATOM 860 CG BLEU A 104 76.810 8.812 24.949 0.50 18.92 C ANISOU 860 CG BLEU A 104 2218 2626 2347 56 -25 45 C ATOM 861 CD1ALEU A 104 77.435 10.035 25.430 0.50 17.76 C ANISOU 861 CD1ALEU A 104 2060 2467 2220 70 -21 36 C ATOM 862 CD1BLEU A 104 77.305 10.129 24.374 0.50 19.02 C ANISOU 862 CD1BLEU A 104 2237 2606 2384 83 -41 52 C ATOM 863 CD2ALEU A 104 75.681 8.624 26.504 0.50 17.99 C ANISOU 863 CD2ALEU A 104 2047 2556 2232 26 -5 -5 C ATOM 864 CD2BLEU A 104 75.478 9.001 25.659 0.50 19.34 C ANISOU 864 CD2BLEU A 104 2223 2708 2419 47 -25 0 C ATOM 865 N AGLU A 105 74.191 6.189 22.671 0.50 18.62 N ANISOU 865 N AGLU A 105 2198 2597 2280 37 -70 57 N ATOM 866 N BGLU A 105 73.967 6.110 22.751 0.50 19.12 N ANISOU 866 N BGLU A 105 2255 2665 2343 34 -71 52 N ATOM 867 CA AGLU A 105 73.613 5.939 21.368 0.50 19.11 C ANISOU 867 CA AGLU A 105 2277 2642 2342 47 -98 69 C ATOM 868 CA BGLU A 105 73.203 5.816 21.549 0.50 19.52 C ANISOU 868 CA BGLU A 105 2317 2704 2397 42 -99 59 C ATOM 869 C AGLU A 105 72.798 7.161 20.963 0.50 19.40 C ANISOU 869 C AGLU A 105 2288 2664 2419 71 -130 49 C ATOM 870 C BGLU A 105 72.702 7.148 20.996 0.50 19.60 C ANISOU 870 C BGLU A 105 2310 2691 2445 71 -130 46 C ATOM 871 O AGLU A 105 72.587 8.082 21.764 0.50 19.53 O ANISOU 871 O AGLU A 105 2268 2687 2465 81 -127 19 O ATOM 872 O BGLU A 105 72.628 8.144 21.732 0.50 19.65 O ANISOU 872 O BGLU A 105 2284 2700 2481 82 -128 20 O ATOM 873 CB AGLU A 105 72.770 4.660 21.402 0.50 19.46 C ANISOU 873 CB AGLU A 105 2318 2709 2368 22 -98 64 C ATOM 874 CB BGLU A 105 72.027 4.888 21.906 0.50 19.97 C ANISOU 874 CB BGLU A 105 2349 2790 2447 17 -97 38 C ATOM 875 CG AGLU A 105 73.627 3.404 21.361 0.50 19.55 C ANISOU 875 CG AGLU A 105 2368 2717 2342 4 -84 92 C ATOM 876 CG BGLU A 105 70.985 4.686 20.814 0.50 20.60 C ANISOU 876 CG BGLU A 105 2429 2862 2537 25 -130 37 C ATOM 877 CD AGLU A 105 72.848 2.124 21.589 0.50 20.01 C ANISOU 877 CD AGLU A 105 2425 2796 2381 -26 -85 88 C ATOM 878 CD BGLU A 105 69.866 3.736 21.207 0.50 21.20 C ANISOU 878 CD BGLU A 105 2480 2970 2605 -4 -126 15 C ATOM 879 OE1AGLU A 105 73.047 1.170 20.807 0.50 19.95 O ANISOU 879 OE1AGLU A 105 2451 2774 2354 -30 -94 109 O ATOM 880 OE1BGLU A 105 69.675 3.474 22.413 0.50 21.87 O ANISOU 880 OE1BGLU A 105 2539 3090 2683 -32 -99 -7 O ATOM 881 OE2AGLU A 105 72.042 2.067 22.544 0.50 20.85 O ANISOU 881 OE2AGLU A 105 2498 2934 2492 -50 -75 62 O ATOM 882 OE2BGLU A 105 69.173 3.247 20.292 0.50 21.66 O ANISOU 882 OE2BGLU A 105 2546 3021 2661 -3 -150 22 O ATOM 883 N ILE A 106 72.384 7.187 19.705 1.00 19.56 N ANISOU 883 N ILE A 106 2329 2661 2442 82 -163 64 N ATOM 884 CA ILE A 106 71.725 8.354 19.128 1.00 20.26 C ANISOU 884 CA ILE A 106 2405 2724 2570 107 -206 53 C ATOM 885 C ILE A 106 70.328 7.967 18.651 1.00 21.14 C ANISOU 885 C ILE A 106 2494 2840 2698 108 -236 34 C ATOM 886 O ILE A 106 70.122 6.889 18.091 1.00 20.90 O ANISOU 886 O ILE A 106 2485 2817 2638 93 -235 51 O ATOM 887 CB ILE A 106 72.603 9.021 18.038 1.00 20.28 C ANISOU 887 CB ILE A 106 2458 2687 2563 117 -228 92 C ATOM 888 CG1 ILE A 106 72.154 10.463 17.785 1.00 20.49 C ANISOU 888 CG1 ILE A 106 2471 2680 2634 141 -275 80 C ATOM 889 CG2 ILE A 106 72.607 8.227 16.738 1.00 20.21 C ANISOU 889 CG2 ILE A 106 2494 2666 2519 105 -243 123 C ATOM 890 CD1 ILE A 106 73.111 11.255 16.925 1.00 20.46 C ANISOU 890 CD1 ILE A 106 2518 2639 2618 141 -294 119 C ATOM 891 N LYS A 107 69.358 8.827 18.930 1.00 22.03 N ANISOU 891 N LYS A 107 2559 2951 2861 128 -264 -5 N ATOM 892 CA LYS A 107 68.036 8.668 18.349 1.00 23.56 C ANISOU 892 CA LYS A 107 2729 3142 3081 134 -303 -26 C ATOM 893 C LYS A 107 68.074 9.102 16.893 1.00 23.53 C ANISOU 893 C LYS A 107 2772 3091 3079 149 -357 11 C ATOM 894 O LYS A 107 68.932 9.880 16.453 1.00 24.52 O ANISOU 894 O LYS A 107 2935 3182 3199 157 -372 40 O ATOM 895 CB LYS A 107 66.988 9.461 19.120 1.00 25.10 C ANISOU 895 CB LYS A 107 2851 3350 3335 152 -317 -89 C ATOM 896 CG LYS A 107 66.802 9.007 20.554 1.00 25.95 C ANISOU 896 CG LYS A 107 2911 3512 3435 128 -262 -130 C ATOM 897 CD LYS A 107 65.461 9.472 21.112 1.00 27.47 C ANISOU 897 CD LYS A 107 3025 3729 3684 137 -275 -202 C ATOM 898 CE LYS A 107 65.261 9.048 22.554 1.00 28.27 C ANISOU 898 CE LYS A 107 3079 3891 3770 103 -217 -247 C ATOM 899 NZ LYS A 107 66.271 9.651 23.464 1.00 28.76 N ANISOU 899 NZ LYS A 107 3147 3956 3824 102 -185 -246 N ATOM 900 N ARG A 108 67.152 8.566 16.128 1.00 23.17 N ANISOU 900 N ARG A 108 2727 3042 3035 146 -389 11 N ATOM 901 CA ARG A 108 66.937 9.024 14.782 1.00 22.91 C ANISOU 901 CA ARG A 108 2732 2963 3008 157 -450 39 C ATOM 902 C ARG A 108 65.506 8.677 14.460 1.00 23.15 C ANISOU 902 C ARG A 108 2728 2999 3069 162 -487 11 C ATOM 903 O ARG A 108 64.823 8.036 15.273 1.00 23.54 O ANISOU 903 O ARG A 108 2725 3090 3127 154 -457 -28 O ATOM 904 CB ARG A 108 67.913 8.350 13.812 1.00 22.23 C ANISOU 904 CB ARG A 108 2720 2868 2859 134 -436 95 C ATOM 905 CG ARG A 108 67.873 6.824 13.829 1.00 21.70 C ANISOU 905 CG ARG A 108 2661 2835 2749 109 -397 100 C ATOM 906 CD ARG A 108 68.192 6.273 12.461 1.00 21.40 C ANISOU 906 CD ARG A 108 2686 2779 2667 93 -414 141 C ATOM 907 NE ARG A 108 67.141 6.591 11.496 1.00 21.53 N ANISOU 907 NE ARG A 108 2706 2768 2704 100 -479 142 N ATOM 908 CZ ARG A 108 67.297 6.655 10.173 1.00 21.65 C ANISOU 908 CZ ARG A 108 2780 2755 2692 88 -515 178 C ATOM 909 NH1 ARG A 108 66.252 6.962 9.406 1.00 22.28 N ANISOU 909 NH1 ARG A 108 2860 2810 2797 96 -581 178 N ATOM 910 NH2 ARG A 108 68.474 6.432 9.596 1.00 21.43 N ANISOU 910 NH2 ARG A 108 2807 2724 2610 67 -489 212 N ATOM 911 N THR A 109 65.059 9.084 13.284 1.00 23.41 N ANISOU 911 N THR A 109 2788 2990 3115 172 -553 31 N ATOM 912 CA THR A 109 63.711 8.767 12.850 1.00 23.62 C ANISOU 912 CA THR A 109 2785 3017 3173 179 -597 7 C ATOM 913 C THR A 109 63.561 7.253 12.758 1.00 22.57 C ANISOU 913 C THR A 109 2661 2922 2990 148 -556 16 C ATOM 914 O THR A 109 64.526 6.532 12.477 1.00 22.44 O ANISOU 914 O THR A 109 2698 2912 2914 125 -519 56 O ATOM 915 CB THR A 109 63.381 9.394 11.488 1.00 24.68 C ANISOU 915 CB THR A 109 2961 3094 3321 189 -681 37 C ATOM 916 OG1 THR A 109 64.362 8.995 10.525 1.00 25.45 O ANISOU 916 OG1 THR A 109 3142 3178 3349 162 -672 98 O ATOM 917 CG2 THR A 109 63.356 10.904 11.577 1.00 25.33 C ANISOU 917 CG2 THR A 109 3032 3132 3462 220 -736 24 C ATOM 918 N VAL A 110 62.352 6.778 13.025 1.00 21.58 N ANISOU 918 N VAL A 110 2483 2823 2894 147 -564 -25 N ATOM 919 CA VAL A 110 62.052 5.356 12.925 1.00 20.44 C ANISOU 919 CA VAL A 110 2346 2712 2708 117 -534 -18 C ATOM 920 C VAL A 110 62.330 4.914 11.489 1.00 19.47 C ANISOU 920 C VAL A 110 2296 2558 2544 107 -566 34 C ATOM 921 O VAL A 110 61.947 5.594 10.535 1.00 20.04 O ANISOU 921 O VAL A 110 2388 2589 2639 122 -632 47 O ATOM 922 CB VAL A 110 60.587 5.047 13.333 1.00 20.84 C ANISOU 922 CB VAL A 110 2324 2793 2801 116 -546 -74 C ATOM 923 CG1 VAL A 110 60.203 3.609 12.978 1.00 20.77 C ANISOU 923 CG1 VAL A 110 2333 2809 2750 83 -531 -60 C ATOM 924 CG2 VAL A 110 60.373 5.313 14.825 1.00 21.16 C ANISOU 924 CG2 VAL A 110 2293 2876 2869 114 -501 -130 C ATOM 925 N ALA A 111 63.030 3.787 11.352 1.00 18.13 N ANISOU 925 N ALA A 111 2169 2405 2313 79 -522 64 N ATOM 926 CA ALA A 111 63.350 3.199 10.057 1.00 17.47 C ANISOU 926 CA ALA A 111 2152 2301 2183 64 -541 106 C ATOM 927 C ALA A 111 62.992 1.723 10.114 1.00 16.82 C ANISOU 927 C ALA A 111 2071 2250 2071 38 -513 103 C ATOM 928 O ALA A 111 63.488 1.000 10.970 1.00 16.11 O ANISOU 928 O ALA A 111 1973 2188 1959 23 -460 98 O ATOM 929 CB ALA A 111 64.824 3.381 9.733 1.00 17.45 C ANISOU 929 CB ALA A 111 2209 2285 2138 57 -514 144 C ATOM 930 N ALA A 112 62.112 1.283 9.222 1.00 16.64 N ANISOU 930 N ALA A 112 2057 2218 2047 32 -555 107 N ATOM 931 CA ALA A 112 61.736 -0.118 9.139 1.00 16.54 C ANISOU 931 CA ALA A 112 2050 2229 2005 5 -536 106 C ATOM 932 C ALA A 112 62.890 -0.925 8.578 1.00 16.21 C ANISOU 932 C ALA A 112 2075 2182 1903 -12 -506 142 C ATOM 933 O ALA A 112 63.647 -0.422 7.746 1.00 16.66 O ANISOU 933 O ALA A 112 2180 2212 1938 -8 -519 169 O ATOM 934 CB ALA A 112 60.523 -0.282 8.236 1.00 16.87 C ANISOU 934 CB ALA A 112 2087 2259 2063 5 -594 101 C ATOM 935 N PRO A 113 63.034 -2.181 9.016 1.00 15.93 N ANISOU 935 N PRO A 113 2043 2170 1841 -34 -469 139 N ATOM 936 CA PRO A 113 64.041 -3.006 8.376 1.00 15.76 C ANISOU 936 CA PRO A 113 2080 2139 1769 -48 -449 165 C ATOM 937 C PRO A 113 63.674 -3.367 6.956 1.00 16.03 C ANISOU 937 C PRO A 113 2158 2155 1779 -57 -487 182 C ATOM 938 O PRO A 113 62.493 -3.503 6.636 1.00 16.53 O ANISOU 938 O PRO A 113 2201 2218 1860 -60 -524 173 O ATOM 939 CB PRO A 113 64.063 -4.272 9.234 1.00 15.63 C ANISOU 939 CB PRO A 113 2052 2147 1739 -69 -414 155 C ATOM 940 CG PRO A 113 62.725 -4.328 9.863 1.00 15.95 C ANISOU 940 CG PRO A 113 2038 2211 1812 -77 -428 128 C ATOM 941 CD PRO A 113 62.315 -2.906 10.077 1.00 15.98 C ANISOU 941 CD PRO A 113 2002 2211 1860 -51 -448 111 C ATOM 942 N SER A 114 64.696 -3.502 6.119 1.00 15.95 N ANISOU 942 N SER A 114 2202 2129 1728 -63 -476 203 N ATOM 943 CA SER A 114 64.579 -4.227 4.864 1.00 16.05 C ANISOU 943 CA SER A 114 2263 2132 1703 -81 -496 216 C ATOM 944 C SER A 114 64.899 -5.674 5.190 1.00 15.63 C ANISOU 944 C SER A 114 2217 2094 1629 -95 -462 207 C ATOM 945 O SER A 114 65.930 -5.949 5.809 1.00 15.20 O ANISOU 945 O SER A 114 2165 2045 1567 -92 -420 204 O ATOM 946 CB SER A 114 65.579 -3.693 3.849 1.00 16.51 C ANISOU 946 CB SER A 114 2375 2174 1725 -87 -495 237 C ATOM 947 OG SER A 114 65.228 -2.378 3.458 1.00 17.41 O ANISOU 947 OG SER A 114 2491 2267 1856 -80 -538 250 O ATOM 948 N VAL A 115 64.033 -6.602 4.795 1.00 15.51 N ANISOU 948 N VAL A 115 2205 2081 1607 -109 -483 203 N ATOM 949 CA VAL A 115 64.154 -8.002 5.201 1.00 15.49 C ANISOU 949 CA VAL A 115 2206 2087 1591 -124 -461 194 C ATOM 950 C VAL A 115 64.528 -8.875 4.003 1.00 15.65 C ANISOU 950 C VAL A 115 2281 2096 1571 -138 -466 199 C ATOM 951 O VAL A 115 63.934 -8.749 2.932 1.00 16.27 O ANISOU 951 O VAL A 115 2381 2165 1635 -146 -501 206 O ATOM 952 CB VAL A 115 62.845 -8.502 5.856 1.00 15.69 C ANISOU 952 CB VAL A 115 2191 2130 1642 -137 -478 181 C ATOM 953 CG1 VAL A 115 63.017 -9.920 6.388 1.00 15.61 C ANISOU 953 CG1 VAL A 115 2189 2126 1617 -157 -458 176 C ATOM 954 CG2 VAL A 115 62.423 -7.549 6.968 1.00 15.74 C ANISOU 954 CG2 VAL A 115 2140 2153 1688 -125 -471 168 C ATOM 955 N PHE A 116 65.513 -9.758 4.194 1.00 15.56 N ANISOU 955 N PHE A 116 2289 2082 1542 -140 -434 191 N ATOM 956 CA PHE A 116 66.022 -10.631 3.136 1.00 15.83 C ANISOU 956 CA PHE A 116 2369 2106 1539 -151 -432 185 C ATOM 957 C PHE A 116 66.197 -12.027 3.721 1.00 15.70 C ANISOU 957 C PHE A 116 2353 2086 1527 -158 -422 172 C ATOM 958 O PHE A 116 66.632 -12.155 4.860 1.00 15.46 O ANISOU 958 O PHE A 116 2300 2058 1515 -151 -402 169 O ATOM 959 CB PHE A 116 67.379 -10.149 2.618 1.00 16.01 C ANISOU 959 CB PHE A 116 2418 2125 1538 -145 -402 182 C ATOM 960 CG PHE A 116 67.411 -8.703 2.212 1.00 16.32 C ANISOU 960 CG PHE A 116 2462 2165 1575 -142 -411 199 C ATOM 961 CD1 PHE A 116 67.660 -7.694 3.143 1.00 16.40 C ANISOU 961 CD1 PHE A 116 2440 2179 1614 -125 -399 205 C ATOM 962 CD2 PHE A 116 67.216 -8.347 0.884 1.00 16.92 C ANISOU 962 CD2 PHE A 116 2576 2234 1617 -160 -435 209 C ATOM 963 CE1 PHE A 116 67.699 -6.358 2.753 1.00 16.67 C ANISOU 963 CE1 PHE A 116 2480 2207 1647 -123 -414 222 C ATOM 964 CE2 PHE A 116 67.262 -7.020 0.496 1.00 17.21 C ANISOU 964 CE2 PHE A 116 2623 2266 1650 -162 -452 229 C ATOM 965 CZ PHE A 116 67.499 -6.029 1.427 1.00 17.11 C ANISOU 965 CZ PHE A 116 2578 2253 1669 -142 -442 235 C ATOM 966 N ILE A 117 65.882 -13.060 2.945 1.00 15.85 N ANISOU 966 N ILE A 117 2400 2096 1525 -172 -439 165 N ATOM 967 CA ILE A 117 66.056 -14.446 3.372 1.00 15.73 C ANISOU 967 CA ILE A 117 2393 2070 1514 -179 -438 152 C ATOM 968 C ILE A 117 66.967 -15.168 2.381 1.00 15.86 C ANISOU 968 C ILE A 117 2449 2072 1505 -178 -429 131 C ATOM 969 O ILE A 117 66.894 -14.945 1.161 1.00 16.00 O ANISOU 969 O ILE A 117 2493 2092 1493 -185 -435 128 O ATOM 970 CB ILE A 117 64.703 -15.167 3.597 1.00 15.84 C ANISOU 970 CB ILE A 117 2396 2087 1536 -202 -471 158 C ATOM 971 CG1 ILE A 117 64.895 -16.508 4.333 1.00 15.91 C ANISOU 971 CG1 ILE A 117 2411 2082 1551 -214 -474 151 C ATOM 972 CG2 ILE A 117 63.930 -15.350 2.288 1.00 16.15 C ANISOU 972 CG2 ILE A 117 2461 2124 1553 -214 -501 159 C ATOM 973 CD1 ILE A 117 63.600 -17.166 4.772 1.00 16.05 C ANISOU 973 CD1 ILE A 117 2415 2107 1576 -243 -502 159 C ATOM 974 N PHE A 118 67.836 -16.017 2.921 1.00 15.91 N ANISOU 974 N PHE A 118 2458 2064 1522 -170 -416 113 N ATOM 975 CA PHE A 118 68.827 -16.751 2.160 1.00 16.16 C ANISOU 975 CA PHE A 118 2518 2082 1541 -163 -404 81 C ATOM 976 C PHE A 118 68.691 -18.248 2.453 1.00 16.44 C ANISOU 976 C PHE A 118 2564 2092 1589 -169 -428 68 C ATOM 977 O PHE A 118 68.791 -18.658 3.621 1.00 15.98 O ANISOU 977 O PHE A 118 2491 2022 1558 -167 -436 75 O ATOM 978 CB PHE A 118 70.235 -16.319 2.563 1.00 16.10 C ANISOU 978 CB PHE A 118 2499 2075 1544 -141 -368 65 C ATOM 979 CG PHE A 118 70.526 -14.880 2.285 1.00 16.07 C ANISOU 979 CG PHE A 118 2488 2092 1526 -138 -344 77 C ATOM 980 CD1 PHE A 118 70.845 -14.465 0.997 1.00 16.32 C ANISOU 980 CD1 PHE A 118 2544 2134 1520 -149 -331 65 C ATOM 981 CD2 PHE A 118 70.472 -13.932 3.293 1.00 15.90 C ANISOU 981 CD2 PHE A 118 2436 2079 1525 -129 -335 100 C ATOM 982 CE1 PHE A 118 71.130 -13.142 0.741 1.00 16.32 C ANISOU 982 CE1 PHE A 118 2544 2152 1506 -152 -314 80 C ATOM 983 CE2 PHE A 118 70.748 -12.604 3.034 1.00 15.88 C ANISOU 983 CE2 PHE A 118 2429 2092 1512 -127 -318 112 C ATOM 984 CZ PHE A 118 71.081 -12.206 1.757 1.00 16.16 C ANISOU 984 CZ PHE A 118 2494 2135 1511 -139 -310 104 C ATOM 985 N APRO A 119 68.522 -19.075 1.404 0.50 16.87 N ANISOU 985 N APRO A 119 2648 2136 1624 -178 -443 47 N ATOM 986 N BPRO A 119 68.440 -19.071 1.422 0.50 16.82 N ANISOU 986 N BPRO A 119 2642 2131 1619 -179 -445 49 N ATOM 987 CA APRO A 119 68.513 -20.509 1.631 0.50 17.28 C ANISOU 987 CA APRO A 119 2715 2159 1693 -181 -470 31 C ATOM 988 CA BPRO A 119 68.504 -20.518 1.619 0.50 17.25 C ANISOU 988 CA BPRO A 119 2711 2154 1688 -181 -470 31 C ATOM 989 C APRO A 119 69.929 -21.004 1.890 0.50 17.54 C ANISOU 989 C APRO A 119 2747 2170 1748 -156 -455 -5 C ATOM 990 C BPRO A 119 69.925 -20.999 1.894 0.50 17.51 C ANISOU 990 C BPRO A 119 2743 2166 1744 -156 -455 -5 C ATOM 991 O APRO A 119 70.885 -20.276 1.618 0.50 17.61 O ANISOU 991 O APRO A 119 2747 2193 1752 -139 -419 -23 O ATOM 992 O BPRO A 119 70.879 -20.262 1.636 0.50 17.58 O ANISOU 992 O BPRO A 119 2743 2189 1749 -139 -419 -23 O ATOM 993 CB APRO A 119 68.005 -21.064 0.302 0.50 17.58 C ANISOU 993 CB APRO A 119 2783 2194 1700 -196 -486 15 C ATOM 994 CB BPRO A 119 68.027 -21.081 0.276 0.50 17.52 C ANISOU 994 CB BPRO A 119 2777 2187 1694 -195 -485 13 C ATOM 995 CG APRO A 119 68.520 -20.102 -0.703 0.50 17.59 C ANISOU 995 CG APRO A 119 2792 2220 1671 -193 -454 3 C ATOM 996 CG BPRO A 119 67.192 -20.008 -0.315 0.50 17.41 C ANISOU 996 CG BPRO A 119 2761 2201 1652 -209 -484 40 C ATOM 997 CD APRO A 119 68.461 -18.755 -0.038 0.50 17.22 C ANISOU 997 CD APRO A 119 2719 2194 1631 -187 -437 35 C ATOM 998 CD BPRO A 119 67.813 -18.721 0.134 0.50 17.10 C ANISOU 998 CD BPRO A 119 2699 2181 1619 -195 -452 52 C ATOM 999 N PRO A 120 70.072 -22.236 2.407 1.00 17.99 N ANISOU 999 N PRO A 120 2814 2191 1831 -154 -486 -17 N ATOM 1000 CA PRO A 120 71.403 -22.810 2.513 1.00 18.63 C ANISOU 1000 CA PRO A 120 2894 2246 1941 -126 -481 -60 C ATOM 1001 C PRO A 120 72.006 -23.019 1.125 1.00 19.68 C ANISOU 1001 C PRO A 120 3040 2383 2054 -117 -460 -112 C ATOM 1002 O PRO A 120 71.275 -23.299 0.161 1.00 20.26 O ANISOU 1002 O PRO A 120 3136 2464 2098 -136 -470 -116 O ATOM 1003 CB PRO A 120 71.164 -24.147 3.213 1.00 18.72 C ANISOU 1003 CB PRO A 120 2920 2211 1980 -133 -533 -58 C ATOM 1004 CG PRO A 120 69.751 -24.481 2.943 1.00 18.86 C ANISOU 1004 CG PRO A 120 2956 2236 1975 -167 -559 -29 C ATOM 1005 CD PRO A 120 69.033 -23.167 2.882 1.00 18.30 C ANISOU 1005 CD PRO A 120 2866 2210 1877 -179 -531 5 C ATOM 1006 N SER A 121 73.320 -22.850 1.032 1.00 20.69 N ANISOU 1006 N SER A 121 3153 2512 2198 -91 -430 -155 N ATOM 1007 CA SER A 121 74.057 -23.088 -0.205 1.00 21.93 C ANISOU 1007 CA SER A 121 3315 2677 2338 -85 -404 -216 C ATOM 1008 C SER A 121 74.116 -24.587 -0.497 1.00 23.12 C ANISOU 1008 C SER A 121 3483 2787 2514 -77 -443 -259 C ATOM 1009 O SER A 121 74.089 -25.402 0.422 1.00 22.74 O ANISOU 1009 O SER A 121 3435 2696 2508 -66 -486 -251 O ATOM 1010 CB SER A 121 75.471 -22.510 -0.102 1.00 22.17 C ANISOU 1010 CB SER A 121 3317 2721 2384 -62 -361 -254 C ATOM 1011 OG SER A 121 76.272 -23.206 0.848 1.00 22.26 O ANISOU 1011 OG SER A 121 3310 2692 2454 -31 -384 -277 O ATOM 1012 N ASP A 122 74.180 -24.958 -1.778 1.00 24.94 N ANISOU 1012 N ASP A 122 3730 3029 2718 -85 -430 -306 N ATOM 1013 CA ASP A 122 74.397 -26.366 -2.139 1.00 26.54 C ANISOU 1013 CA ASP A 122 3945 3191 2948 -72 -463 -360 C ATOM 1014 C ASP A 122 75.723 -26.888 -1.586 1.00 27.00 C ANISOU 1014 C ASP A 122 3976 3217 3067 -32 -467 -415 C ATOM 1015 O ASP A 122 75.814 -28.052 -1.184 1.00 27.75 O ANISOU 1015 O ASP A 122 4076 3258 3208 -15 -519 -436 O ATOM 1016 CB ASP A 122 74.352 -26.575 -3.662 1.00 27.70 C ANISOU 1016 CB ASP A 122 4110 3363 3051 -89 -440 -409 C ATOM 1017 CG ASP A 122 72.943 -26.462 -4.240 1.00 28.25 C ANISOU 1017 CG ASP A 122 4213 3447 3072 -127 -457 -360 C ATOM 1018 OD1 ASP A 122 71.946 -26.528 -3.481 1.00 28.38 O ANISOU 1018 OD1 ASP A 122 4237 3448 3097 -137 -495 -299 O ATOM 1019 OD2 ASP A 122 72.831 -26.325 -5.479 1.00 29.37 O ANISOU 1019 OD2 ASP A 122 4375 3619 3166 -149 -434 -387 O ATOM 1020 N GLU A 123 76.733 -26.017 -1.546 1.00 27.52 N ANISOU 1020 N GLU A 123 4011 3313 3134 -18 -418 -438 N ATOM 1021 CA GLU A 123 78.040 -26.345 -0.954 1.00 28.08 C ANISOU 1021 CA GLU A 123 4048 3356 3265 21 -420 -490 C ATOM 1022 C GLU A 123 77.918 -26.804 0.502 1.00 27.17 C ANISOU 1022 C GLU A 123 3932 3188 3201 37 -478 -446 C ATOM 1023 O GLU A 123 78.496 -27.822 0.882 1.00 27.46 O ANISOU 1023 O GLU A 123 3965 3173 3297 65 -523 -486 O ATOM 1024 CB GLU A 123 79.012 -25.159 -1.022 1.00 29.05 C ANISOU 1024 CB GLU A 123 4138 3525 3375 27 -356 -507 C ATOM 1025 CG GLU A 123 79.378 -24.678 -2.420 1.00 30.39 C ANISOU 1025 CG GLU A 123 4307 3748 3493 5 -295 -558 C ATOM 1026 CD GLU A 123 78.661 -23.394 -2.810 1.00 30.85 C ANISOU 1026 CD GLU A 123 4384 3857 3481 -35 -261 -495 C ATOM 1027 OE1 GLU A 123 77.410 -23.415 -2.906 1.00 31.43 O ANISOU 1027 OE1 GLU A 123 4490 3926 3526 -58 -289 -439 O ATOM 1028 OE2 GLU A 123 79.350 -22.368 -3.024 1.00 31.63 O ANISOU 1028 OE2 GLU A 123 4466 3997 3557 -44 -209 -504 O ATOM 1029 N GLN A 124 77.164 -26.061 1.313 1.00 25.97 N ANISOU 1029 N GLN A 124 3788 3051 3030 16 -481 -366 N ATOM 1030 CA GLN A 124 76.977 -26.443 2.716 1.00 25.54 C ANISOU 1030 CA GLN A 124 3737 2953 3013 20 -533 -321 C ATOM 1031 C GLN A 124 76.164 -27.735 2.860 1.00 26.26 C ANISOU 1031 C GLN A 124 3863 2996 3118 6 -601 -308 C ATOM 1032 O GLN A 124 76.468 -28.563 3.717 1.00 26.49 O ANISOU 1032 O GLN A 124 3899 2970 3195 18 -657 -307 O ATOM 1033 CB GLN A 124 76.317 -25.324 3.524 1.00 24.22 C ANISOU 1033 CB GLN A 124 3566 2819 2817 -4 -515 -245 C ATOM 1034 CG GLN A 124 76.232 -25.656 5.016 1.00 23.54 C ANISOU 1034 CG GLN A 124 3484 2696 2765 -7 -562 -202 C ATOM 1035 CD GLN A 124 75.432 -24.678 5.852 1.00 22.66 C ANISOU 1035 CD GLN A 124 3368 2617 2625 -35 -547 -132 C ATOM 1036 OE1 GLN A 124 75.618 -24.607 7.071 1.00 22.47 O ANISOU 1036 OE1 GLN A 124 3339 2576 2622 -38 -567 -103 O ATOM 1037 NE2 GLN A 124 74.553 -23.930 5.224 1.00 21.66 N ANISOU 1037 NE2 GLN A 124 3243 2535 2453 -57 -515 -109 N ATOM 1038 N LEU A 125 75.139 -27.911 2.026 1.00 26.90 N ANISOU 1038 N LEU A 125 3969 3095 3158 -21 -600 -296 N ATOM 1039 CA LEU A 125 74.306 -29.116 2.114 1.00 27.95 C ANISOU 1039 CA LEU A 125 4136 3184 3300 -39 -663 -282 C ATOM 1040 C LEU A 125 75.099 -30.415 1.912 1.00 29.59 C ANISOU 1040 C LEU A 125 4349 3331 3562 -8 -708 -348 C ATOM 1041 O LEU A 125 74.779 -31.428 2.532 1.00 30.30 O ANISOU 1041 O LEU A 125 4465 3366 3682 -16 -776 -331 O ATOM 1042 CB LEU A 125 73.136 -29.042 1.136 1.00 27.66 C ANISOU 1042 CB LEU A 125 4121 3179 3210 -71 -651 -265 C ATOM 1043 CG LEU A 125 72.092 -27.972 1.452 1.00 27.07 C ANISOU 1043 CG LEU A 125 4044 3151 3092 -104 -627 -195 C ATOM 1044 CD1 LEU A 125 71.168 -27.802 0.257 1.00 27.17 C ANISOU 1044 CD1 LEU A 125 4073 3195 3055 -128 -613 -193 C ATOM 1045 CD2 LEU A 125 71.310 -28.308 2.714 1.00 26.82 C ANISOU 1045 CD2 LEU A 125 4022 3097 3073 -130 -672 -136 C ATOM 1046 N LYS A 126 76.146 -30.366 1.084 1.00 30.88 N ANISOU 1046 N LYS A 126 4489 3506 3740 24 -673 -426 N ATOM 1047 CA LYS A 126 77.052 -31.509 0.882 1.00 32.31 C ANISOU 1047 CA LYS A 126 4663 3630 3981 61 -713 -504 C ATOM 1048 C LYS A 126 77.619 -32.107 2.175 1.00 33.08 C ANISOU 1048 C LYS A 126 4760 3662 4147 83 -779 -494 C ATOM 1049 O LYS A 126 77.823 -33.322 2.241 1.00 34.23 O ANISOU 1049 O LYS A 126 4921 3742 4344 101 -846 -529 O ATOM 1050 CB LYS A 126 78.215 -31.113 -0.038 1.00 32.78 C ANISOU 1050 CB LYS A 126 4684 3724 4046 90 -651 -592 C ATOM 1051 N SER A 127 77.860 -31.269 3.190 1.00 33.09 N ANISOU 1051 N SER A 127 4745 3677 4149 81 -765 -446 N ATOM 1052 CA SER A 127 78.464 -31.704 4.459 1.00 33.35 C ANISOU 1052 CA SER A 127 4778 3651 4242 98 -826 -432 C ATOM 1053 C SER A 127 77.470 -31.948 5.616 1.00 32.68 C ANISOU 1053 C SER A 127 4733 3542 4143 55 -881 -340 C ATOM 1054 O SER A 127 77.889 -32.076 6.774 1.00 33.18 O ANISOU 1054 O SER A 127 4799 3566 4240 57 -925 -314 O ATOM 1055 CB SER A 127 79.529 -30.695 4.884 1.00 33.66 C ANISOU 1055 CB SER A 127 4773 3719 4296 125 -780 -446 C ATOM 1056 OG SER A 127 78.967 -29.411 5.063 1.00 33.75 O ANISOU 1056 OG SER A 127 4779 3795 4248 95 -719 -385 O ATOM 1057 N GLY A 128 76.173 -32.010 5.315 1.00 31.46 N ANISOU 1057 N GLY A 128 4607 3410 3937 11 -878 -295 N ATOM 1058 CA GLY A 128 75.170 -32.513 6.266 1.00 30.69 C ANISOU 1058 CA GLY A 128 4550 3285 3827 -37 -936 -222 C ATOM 1059 C GLY A 128 74.413 -31.527 7.142 1.00 29.24 C ANISOU 1059 C GLY A 128 4363 3149 3598 -79 -905 -145 C ATOM 1060 O GLY A 128 73.593 -31.951 7.965 1.00 29.27 O ANISOU 1060 O GLY A 128 4397 3136 3588 -125 -949 -89 O ATOM 1061 N THR A 129 74.655 -30.225 6.974 1.00 27.76 N ANISOU 1061 N THR A 129 4139 3023 3385 -67 -831 -145 N ATOM 1062 CA THR A 129 73.962 -29.191 7.759 1.00 26.19 C ANISOU 1062 CA THR A 129 3931 2873 3147 -101 -798 -81 C ATOM 1063 C THR A 129 73.393 -28.123 6.831 1.00 24.42 C ANISOU 1063 C THR A 129 3686 2718 2875 -105 -728 -80 C ATOM 1064 O THR A 129 73.907 -27.902 5.736 1.00 24.84 O ANISOU 1064 O THR A 129 3726 2787 2926 -76 -693 -129 O ATOM 1065 CB THR A 129 74.910 -28.544 8.785 1.00 26.40 C ANISOU 1065 CB THR A 129 3935 2899 3199 -84 -789 -72 C ATOM 1066 OG1 THR A 129 75.500 -29.575 9.584 1.00 27.31 O ANISOU 1066 OG1 THR A 129 4072 2942 3361 -79 -863 -75 O ATOM 1067 CG2 THR A 129 74.180 -27.556 9.692 1.00 26.14 C ANISOU 1067 CG2 THR A 129 3892 2911 3127 -122 -760 -10 C ATOM 1068 N ALA A 130 72.299 -27.501 7.268 1.00 22.61 N ANISOU 1068 N ALA A 130 3455 2527 2608 -144 -712 -25 N ATOM 1069 CA ALA A 130 71.635 -26.434 6.536 1.00 21.15 C ANISOU 1069 CA ALA A 130 3252 2402 2381 -151 -658 -16 C ATOM 1070 C ALA A 130 71.486 -25.220 7.448 1.00 19.81 C ANISOU 1070 C ALA A 130 3056 2273 2200 -161 -624 23 C ATOM 1071 O ALA A 130 70.902 -25.328 8.513 1.00 20.00 O ANISOU 1071 O ALA A 130 3084 2295 2221 -195 -646 63 O ATOM 1072 CB ALA A 130 70.267 -26.907 6.080 1.00 21.15 C ANISOU 1072 CB ALA A 130 3273 2411 2352 -188 -678 5 C ATOM 1073 N SER A 131 71.998 -24.069 7.015 1.00 18.44 N ANISOU 1073 N SER A 131 2855 2134 2016 -137 -571 10 N ATOM 1074 CA SER A 131 71.829 -22.807 7.713 1.00 17.54 C ANISOU 1074 CA SER A 131 2714 2060 1891 -143 -536 41 C ATOM 1075 C SER A 131 70.953 -21.918 6.839 1.00 16.89 C ANISOU 1075 C SER A 131 2622 2021 1773 -152 -505 51 C ATOM 1076 O SER A 131 71.272 -21.712 5.678 1.00 17.14 O ANISOU 1076 O SER A 131 2659 2063 1793 -135 -484 23 O ATOM 1077 CB SER A 131 73.179 -22.114 7.932 1.00 17.28 C ANISOU 1077 CB SER A 131 2658 2028 1878 -108 -505 19 C ATOM 1078 OG SER A 131 74.068 -22.901 8.708 1.00 17.58 O ANISOU 1078 OG SER A 131 2704 2022 1954 -95 -539 7 O ATOM 1079 N VAL A 132 69.848 -21.427 7.391 1.00 16.31 N ANISOU 1079 N VAL A 132 2537 1976 1686 -181 -505 88 N ATOM 1080 CA VAL A 132 68.953 -20.504 6.700 1.00 16.05 C ANISOU 1080 CA VAL A 132 2491 1981 1627 -188 -485 99 C ATOM 1081 C VAL A 132 69.140 -19.156 7.381 1.00 15.61 C ANISOU 1081 C VAL A 132 2402 1954 1574 -180 -452 114 C ATOM 1082 O VAL A 132 69.074 -19.074 8.607 1.00 15.09 O ANISOU 1082 O VAL A 132 2322 1891 1521 -193 -454 132 O ATOM 1083 CB VAL A 132 67.471 -20.939 6.806 1.00 16.36 C ANISOU 1083 CB VAL A 132 2534 2030 1654 -227 -512 121 C ATOM 1084 CG1 VAL A 132 66.629 -20.203 5.777 1.00 16.48 C ANISOU 1084 CG1 VAL A 132 2541 2073 1647 -228 -503 123 C ATOM 1085 CG2 VAL A 132 67.332 -22.442 6.644 1.00 16.85 C ANISOU 1085 CG2 VAL A 132 2629 2055 1719 -243 -554 113 C ATOM 1086 N VAL A 133 69.393 -18.107 6.616 1.00 15.29 N ANISOU 1086 N VAL A 133 2354 1935 1523 -161 -423 108 N ATOM 1087 CA VAL A 133 69.723 -16.811 7.193 1.00 15.19 C ANISOU 1087 CA VAL A 133 2311 1943 1515 -149 -393 119 C ATOM 1088 C VAL A 133 68.688 -15.763 6.828 1.00 15.02 C ANISOU 1088 C VAL A 133 2274 1951 1482 -157 -389 136 C ATOM 1089 O VAL A 133 68.313 -15.637 5.656 1.00 14.89 O ANISOU 1089 O VAL A 133 2273 1938 1446 -158 -396 131 O ATOM 1090 CB VAL A 133 71.135 -16.351 6.773 1.00 15.36 C ANISOU 1090 CB VAL A 133 2335 1961 1540 -120 -363 96 C ATOM 1091 CG1 VAL A 133 71.442 -14.953 7.289 1.00 15.27 C ANISOU 1091 CG1 VAL A 133 2297 1972 1533 -110 -334 109 C ATOM 1092 CG2 VAL A 133 72.172 -17.342 7.282 1.00 15.53 C ANISOU 1092 CG2 VAL A 133 2365 1952 1585 -108 -372 75 C ATOM 1093 N ACYS A 134 68.233 -15.015 7.832 0.50 15.04 N ANISOU 1093 N ACYS A 134 2244 1972 1497 -163 -383 152 N ATOM 1094 N BCYS A 134 68.211 -15.038 7.834 0.50 14.81 N ANISOU 1094 N BCYS A 134 2215 1944 1468 -164 -383 152 N ATOM 1095 CA ACYS A 134 67.281 -13.923 7.672 0.50 15.22 C ANISOU 1095 CA ACYS A 134 2242 2020 1520 -166 -383 162 C ATOM 1096 CA BCYS A 134 67.332 -13.907 7.638 0.50 14.83 C ANISOU 1096 CA BCYS A 134 2194 1971 1471 -165 -382 162 C ATOM 1097 C ACYS A 134 67.970 -12.628 8.112 0.50 14.74 C ANISOU 1097 C ACYS A 134 2160 1970 1471 -145 -355 165 C ATOM 1098 C BCYS A 134 68.074 -12.661 8.065 0.50 14.53 C ANISOU 1098 C BCYS A 134 2136 1942 1443 -144 -354 164 C ATOM 1099 O ACYS A 134 68.450 -12.537 9.249 0.50 14.39 O ANISOU 1099 O ACYS A 134 2099 1928 1440 -144 -341 167 O ATOM 1100 O BCYS A 134 68.696 -12.635 9.136 0.50 14.19 O ANISOU 1100 O BCYS A 134 2080 1899 1413 -141 -339 165 O ATOM 1101 CB ACYS A 134 66.034 -14.195 8.521 0.50 15.79 C ANISOU 1101 CB ACYS A 134 2288 2109 1601 -194 -399 170 C ATOM 1102 CB BCYS A 134 66.074 -14.057 8.470 0.50 15.09 C ANISOU 1102 CB BCYS A 134 2199 2022 1514 -191 -398 170 C ATOM 1103 SG ACYS A 134 64.724 -12.953 8.404 0.50 16.61 S ANISOU 1103 SG ACYS A 134 2351 2242 1718 -195 -407 172 S ATOM 1104 SG BCYS A 134 64.787 -12.866 8.049 0.50 15.58 S ANISOU 1104 SG BCYS A 134 2227 2108 1584 -190 -409 172 S ATOM 1105 N LEU A 135 68.031 -11.643 7.215 1.00 14.50 N ANISOU 1105 N LEU A 135 2134 1944 1432 -132 -352 167 N ATOM 1106 CA LEU A 135 68.713 -10.376 7.453 1.00 14.34 C ANISOU 1106 CA LEU A 135 2099 1930 1419 -113 -329 171 C ATOM 1107 C LEU A 135 67.688 -9.275 7.605 1.00 14.41 C ANISOU 1107 C LEU A 135 2078 1952 1444 -112 -344 180 C ATOM 1108 O LEU A 135 66.815 -9.128 6.752 1.00 14.51 O ANISOU 1108 O LEU A 135 2098 1964 1450 -118 -372 184 O ATOM 1109 CB LEU A 135 69.639 -10.050 6.282 1.00 14.39 C ANISOU 1109 CB LEU A 135 2137 1928 1402 -105 -317 166 C ATOM 1110 CG LEU A 135 70.237 -8.638 6.227 1.00 14.40 C ANISOU 1110 CG LEU A 135 2132 1935 1404 -92 -300 173 C ATOM 1111 CD1 LEU A 135 71.175 -8.368 7.393 1.00 14.27 C ANISOU 1111 CD1 LEU A 135 2093 1921 1408 -79 -271 169 C ATOM 1112 CD2 LEU A 135 70.940 -8.449 4.892 1.00 14.73 C ANISOU 1112 CD2 LEU A 135 2212 1974 1412 -98 -292 168 C ATOM 1113 N LEU A 136 67.784 -8.524 8.701 1.00 14.49 N ANISOU 1113 N LEU A 136 2054 1974 1477 -105 -329 180 N ATOM 1114 CA LEU A 136 67.010 -7.306 8.909 1.00 14.69 C ANISOU 1114 CA LEU A 136 2046 2011 1525 -97 -341 180 C ATOM 1115 C LEU A 136 68.003 -6.164 8.788 1.00 14.78 C ANISOU 1115 C LEU A 136 2064 2014 1538 -77 -325 186 C ATOM 1116 O LEU A 136 68.895 -6.041 9.636 1.00 14.53 O ANISOU 1116 O LEU A 136 2023 1985 1511 -71 -296 184 O ATOM 1117 CB LEU A 136 66.371 -7.284 10.303 1.00 14.90 C ANISOU 1117 CB LEU A 136 2026 2058 1576 -107 -333 169 C ATOM 1118 CG LEU A 136 65.170 -8.178 10.589 1.00 15.28 C ANISOU 1118 CG LEU A 136 2057 2122 1626 -133 -349 161 C ATOM 1119 CD1 LEU A 136 65.468 -9.645 10.332 1.00 15.46 C ANISOU 1119 CD1 LEU A 136 2118 2133 1624 -152 -352 167 C ATOM 1120 CD2 LEU A 136 64.703 -7.957 12.020 1.00 15.42 C ANISOU 1120 CD2 LEU A 136 2028 2169 1664 -149 -333 146 C ATOM 1121 N ASN A 137 67.877 -5.344 7.750 1.00 15.24 N ANISOU 1121 N ASN A 137 2140 2061 1589 -71 -345 196 N ATOM 1122 CA ASN A 137 68.922 -4.373 7.442 1.00 15.55 C ANISOU 1122 CA ASN A 137 2196 2092 1620 -61 -331 205 C ATOM 1123 C ASN A 137 68.489 -2.945 7.729 1.00 15.49 C ANISOU 1123 C ASN A 137 2162 2080 1642 -47 -350 209 C ATOM 1124 O ASN A 137 67.405 -2.524 7.323 1.00 15.25 O ANISOU 1124 O ASN A 137 2123 2044 1628 -45 -391 210 O ATOM 1125 CB ASN A 137 69.359 -4.479 5.983 1.00 16.55 C ANISOU 1125 CB ASN A 137 2374 2208 1708 -73 -339 214 C ATOM 1126 CG ASN A 137 70.788 -4.015 5.782 1.00 17.24 C ANISOU 1126 CG ASN A 137 2481 2293 1775 -73 -305 215 C ATOM 1127 OD1 ASN A 137 71.675 -4.430 6.531 1.00 18.43 O ANISOU 1127 OD1 ASN A 137 2621 2450 1932 -65 -271 203 O ATOM 1128 ND2 ASN A 137 71.018 -3.157 4.816 1.00 18.32 N ANISOU 1128 ND2 ASN A 137 2650 2422 1890 -83 -318 230 N ATOM 1129 N ASN A 138 69.362 -2.214 8.425 1.00 15.25 N ANISOU 1129 N ASN A 138 2120 2051 1622 -35 -324 209 N ATOM 1130 CA ASN A 138 69.286 -0.747 8.558 1.00 15.63 C ANISOU 1130 CA ASN A 138 2154 2089 1695 -21 -341 214 C ATOM 1131 C ASN A 138 67.974 -0.244 9.162 1.00 15.68 C ANISOU 1131 C ASN A 138 2112 2099 1745 -9 -371 198 C ATOM 1132 O ASN A 138 67.238 0.549 8.541 1.00 16.22 O ANISOU 1132 O ASN A 138 2180 2150 1832 -2 -417 203 O ATOM 1133 CB ASN A 138 69.559 -0.060 7.212 1.00 16.30 C ANISOU 1133 CB ASN A 138 2286 2152 1754 -30 -367 236 C ATOM 1134 CG ASN A 138 70.969 -0.287 6.704 1.00 16.56 C ANISOU 1134 CG ASN A 138 2358 2187 1746 -44 -331 243 C ATOM 1135 OD1 ASN A 138 71.774 -0.953 7.348 1.00 16.63 O ANISOU 1135 OD1 ASN A 138 2358 2210 1751 -41 -289 231 O ATOM 1136 ND2 ASN A 138 71.272 0.271 5.530 1.00 17.50 N ANISOU 1136 ND2 ASN A 138 2522 2293 1833 -62 -348 262 N ATOM 1137 N PHE A 139 67.710 -0.684 10.383 1.00 15.20 N ANISOU 1137 N PHE A 139 2010 2062 1703 -10 -346 178 N ATOM 1138 CA PHE A 139 66.485 -0.322 11.102 1.00 15.55 C ANISOU 1138 CA PHE A 139 1999 2120 1790 -3 -364 152 C ATOM 1139 C PHE A 139 66.748 0.472 12.369 1.00 15.74 C ANISOU 1139 C PHE A 139 1981 2157 1842 8 -340 133 C ATOM 1140 O PHE A 139 67.856 0.460 12.909 1.00 15.16 O ANISOU 1140 O PHE A 139 1921 2087 1754 7 -305 141 O ATOM 1141 CB PHE A 139 65.621 -1.557 11.390 1.00 15.41 C ANISOU 1141 CB PHE A 139 1965 2126 1766 -25 -361 138 C ATOM 1142 CG PHE A 139 66.280 -2.596 12.261 1.00 14.94 C ANISOU 1142 CG PHE A 139 1911 2084 1683 -44 -319 139 C ATOM 1143 CD1 PHE A 139 67.038 -3.620 11.703 1.00 14.77 C ANISOU 1143 CD1 PHE A 139 1936 2051 1625 -54 -308 157 C ATOM 1144 CD2 PHE A 139 66.118 -2.569 13.634 1.00 14.99 C ANISOU 1144 CD2 PHE A 139 1876 2117 1705 -54 -294 118 C ATOM 1145 CE1 PHE A 139 67.640 -4.578 12.509 1.00 14.51 C ANISOU 1145 CE1 PHE A 139 1909 2028 1577 -70 -280 157 C ATOM 1146 CE2 PHE A 139 66.713 -3.518 14.444 1.00 14.90 C ANISOU 1146 CE2 PHE A 139 1875 2117 1671 -76 -264 123 C ATOM 1147 CZ PHE A 139 67.471 -4.530 13.878 1.00 14.49 C ANISOU 1147 CZ PHE A 139 1870 2047 1587 -82 -261 143 C ATOM 1148 N TYR A 140 65.715 1.171 12.830 1.00 16.27 N ANISOU 1148 N TYR A 140 1997 2232 1952 19 -361 104 N ATOM 1149 CA TYR A 140 65.771 1.906 14.092 1.00 16.96 C ANISOU 1149 CA TYR A 140 2037 2336 2069 27 -339 76 C ATOM 1150 C TYR A 140 64.345 2.046 14.615 1.00 17.61 C ANISOU 1150 C TYR A 140 2055 2443 2193 27 -355 31 C ATOM 1151 O TYR A 140 63.478 2.397 13.816 1.00 17.38 O ANISOU 1151 O TYR A 140 2017 2396 2190 41 -402 25 O ATOM 1152 CB TYR A 140 66.403 3.307 13.917 1.00 17.45 C ANISOU 1152 CB TYR A 140 2107 2369 2153 54 -354 84 C ATOM 1153 CG TYR A 140 66.564 3.952 15.269 1.00 17.91 C ANISOU 1153 CG TYR A 140 2119 2447 2237 61 -325 54 C ATOM 1154 CD1 TYR A 140 65.516 4.683 15.844 1.00 18.68 C ANISOU 1154 CD1 TYR A 140 2155 2557 2387 74 -343 8 C ATOM 1155 CD2 TYR A 140 67.714 3.744 16.026 1.00 18.03 C ANISOU 1155 CD2 TYR A 140 2149 2474 2227 51 -280 65 C ATOM 1156 CE1 TYR A 140 65.633 5.209 17.119 1.00 19.16 C ANISOU 1156 CE1 TYR A 140 2171 2640 2468 76 -313 -25 C ATOM 1157 CE2 TYR A 140 67.837 4.271 17.302 1.00 18.40 C ANISOU 1157 CE2 TYR A 140 2156 2542 2295 52 -253 37 C ATOM 1158 CZ TYR A 140 66.796 5.007 17.837 1.00 18.97 C ANISOU 1158 CZ TYR A 140 2168 2626 2413 63 -268 -8 C ATOM 1159 OH TYR A 140 66.943 5.512 19.113 1.00 20.33 O ANISOU 1159 OH TYR A 140 2301 2824 2601 60 -237 -40 O ATOM 1160 N PRO A 141 64.070 1.828 15.911 1.00 18.75 N ANISOU 1160 N PRO A 141 2153 2626 2344 9 -318 -1 N ATOM 1161 CA PRO A 141 65.031 1.485 16.972 1.00 19.10 C ANISOU 1161 CA PRO A 141 2206 2690 2361 -9 -269 5 C ATOM 1162 C PRO A 141 65.477 0.020 16.957 1.00 19.56 C ANISOU 1162 C PRO A 141 2305 2756 2369 -41 -247 33 C ATOM 1163 O PRO A 141 65.102 -0.720 16.061 1.00 19.03 O ANISOU 1163 O PRO A 141 2263 2679 2288 -48 -268 48 O ATOM 1164 CB PRO A 141 64.257 1.822 18.246 1.00 19.55 C ANISOU 1164 CB PRO A 141 2194 2788 2445 -23 -248 -47 C ATOM 1165 CG PRO A 141 62.841 1.595 17.884 1.00 19.90 C ANISOU 1165 CG PRO A 141 2200 2847 2514 -28 -275 -77 C ATOM 1166 CD PRO A 141 62.721 2.050 16.456 1.00 19.70 C ANISOU 1166 CD PRO A 141 2204 2776 2506 6 -328 -54 C ATOM 1167 N ARG A 142 66.290 -0.380 17.934 1.00 20.53 N ANISOU 1167 N ARG A 142 2437 2893 2469 -61 -211 39 N ATOM 1168 CA ARG A 142 66.916 -1.713 17.958 1.00 21.90 C ANISOU 1168 CA ARG A 142 2654 3065 2601 -87 -198 67 C ATOM 1169 C ARG A 142 65.922 -2.856 18.152 1.00 22.01 C ANISOU 1169 C ARG A 142 2660 3103 2601 -125 -202 58 C ATOM 1170 O ARG A 142 66.171 -3.970 17.689 1.00 21.31 O ANISOU 1170 O ARG A 142 2611 3001 2484 -140 -209 82 O ATOM 1171 CB ARG A 142 67.991 -1.783 19.063 1.00 23.01 C ANISOU 1171 CB ARG A 142 2804 3212 2727 -99 -166 74 C ATOM 1172 CG ARG A 142 68.902 -3.017 19.028 1.00 24.27 C ANISOU 1172 CG ARG A 142 3013 3356 2853 -115 -161 104 C ATOM 1173 CD ARG A 142 70.000 -2.929 20.090 1.00 25.72 C ANISOU 1173 CD ARG A 142 3204 3540 3029 -122 -138 111 C ATOM 1174 NE ARG A 142 70.893 -4.098 20.109 1.00 26.99 N ANISOU 1174 NE ARG A 142 3409 3682 3166 -134 -141 135 N ATOM 1175 CZ ARG A 142 70.636 -5.271 20.702 1.00 28.57 C ANISOU 1175 CZ ARG A 142 3623 3889 3345 -174 -148 141 C ATOM 1176 NH1 ARG A 142 71.541 -6.248 20.652 1.00 29.57 N ANISOU 1176 NH1 ARG A 142 3789 3988 3458 -178 -159 161 N ATOM 1177 NH2 ARG A 142 69.490 -5.493 21.347 1.00 29.50 N ANISOU 1177 NH2 ARG A 142 3714 4041 3456 -213 -145 125 N ATOM 1178 N GLU A 143 64.803 -2.572 18.816 1.00 22.80 N ANISOU 1178 N GLU A 143 2705 3238 2719 -143 -197 20 N ATOM 1179 CA GLU A 143 63.851 -3.611 19.222 1.00 24.00 C ANISOU 1179 CA GLU A 143 2843 3423 2854 -191 -194 7 C ATOM 1180 C GLU A 143 63.153 -4.191 18.005 1.00 23.92 C ANISOU 1180 C GLU A 143 2847 3396 2844 -185 -227 17 C ATOM 1181 O GLU A 143 62.546 -3.464 17.215 1.00 24.09 O ANISOU 1181 O GLU A 143 2848 3407 2897 -154 -254 3 O ATOM 1182 CB GLU A 143 62.806 -3.070 20.198 1.00 25.54 C ANISOU 1182 CB GLU A 143 2968 3666 3071 -213 -177 -45 C ATOM 1183 CG GLU A 143 63.354 -2.747 21.585 1.00 26.67 C ANISOU 1183 CG GLU A 143 3095 3835 3202 -236 -139 -58 C ATOM 1184 CD GLU A 143 64.335 -1.583 21.597 1.00 27.59 C ANISOU 1184 CD GLU A 143 3216 3926 3341 -190 -135 -52 C ATOM 1185 OE1 GLU A 143 64.114 -0.597 20.852 1.00 28.99 O ANISOU 1185 OE1 GLU A 143 3375 4082 3558 -144 -158 -64 O ATOM 1186 OE2 GLU A 143 65.338 -1.657 22.336 1.00 29.03 O ANISOU 1186 OE2 GLU A 143 3422 4106 3501 -201 -114 -34 O ATOM 1187 N ALA A 144 63.266 -5.503 17.860 1.00 23.74 N ANISOU 1187 N ALA A 144 2865 3370 2787 -216 -231 41 N ATOM 1188 CA ALA A 144 62.630 -6.225 16.774 1.00 23.94 C ANISOU 1188 CA ALA A 144 2909 3381 2806 -218 -261 51 C ATOM 1189 C ALA A 144 62.306 -7.636 17.237 1.00 24.27 C ANISOU 1189 C ALA A 144 2969 3438 2815 -271 -258 59 C ATOM 1190 O ALA A 144 62.963 -8.169 18.135 1.00 25.00 O ANISOU 1190 O ALA A 144 3082 3535 2883 -300 -240 72 O ATOM 1191 CB ALA A 144 63.554 -6.259 15.570 1.00 23.69 C ANISOU 1191 CB ALA A 144 2932 3304 2766 -181 -278 83 C ATOM 1192 N LYS A 145 61.275 -8.223 16.644 1.00 24.22 N ANISOU 1192 N LYS A 145 2955 3438 2807 -288 -280 52 N ATOM 1193 CA LYS A 145 60.933 -9.627 16.873 1.00 23.94 C ANISOU 1193 CA LYS A 145 2945 3412 2741 -340 -285 64 C ATOM 1194 C LYS A 145 61.117 -10.353 15.542 1.00 22.64 C ANISOU 1194 C LYS A 145 2829 3206 2565 -321 -316 90 C ATOM 1195 O LYS A 145 60.616 -9.899 14.512 1.00 22.02 O ANISOU 1195 O LYS A 145 2742 3118 2506 -291 -338 84 O ATOM 1196 CB LYS A 145 59.497 -9.753 17.366 1.00 25.66 C ANISOU 1196 CB LYS A 145 3108 3677 2963 -384 -281 29 C ATOM 1197 CG LYS A 145 59.073 -11.146 17.816 1.00 26.97 C ANISOU 1197 CG LYS A 145 3297 3858 3093 -451 -284 40 C ATOM 1198 CD LYS A 145 57.558 -11.298 17.852 1.00 28.41 C ANISOU 1198 CD LYS A 145 3427 4085 3284 -488 -287 4 C ATOM 1199 CE LYS A 145 56.907 -10.375 18.872 1.00 29.56 C ANISOU 1199 CE LYS A 145 3497 4285 3450 -506 -254 -47 C ATOM 1200 NZ LYS A 145 55.450 -10.653 18.987 1.00 30.82 N ANISOU 1200 NZ LYS A 145 3602 4493 3616 -551 -254 -87 N ATOM 1201 N VAL A 146 61.861 -11.455 15.571 1.00 21.44 N ANISOU 1201 N VAL A 146 2732 3031 2385 -338 -322 118 N ATOM 1202 CA VAL A 146 62.050 -12.316 14.409 1.00 21.00 C ANISOU 1202 CA VAL A 146 2723 2938 2316 -326 -349 137 C ATOM 1203 C VAL A 146 61.574 -13.712 14.771 1.00 20.12 C ANISOU 1203 C VAL A 146 2634 2830 2181 -380 -364 145 C ATOM 1204 O VAL A 146 62.072 -14.297 15.728 1.00 19.83 O ANISOU 1204 O VAL A 146 2616 2792 2127 -412 -357 157 O ATOM 1205 CB VAL A 146 63.526 -12.380 13.986 1.00 21.64 C ANISOU 1205 CB VAL A 146 2851 2981 2392 -291 -346 156 C ATOM 1206 CG1 VAL A 146 63.679 -13.181 12.701 1.00 22.14 C ANISOU 1206 CG1 VAL A 146 2958 3012 2444 -278 -372 166 C ATOM 1207 CG2 VAL A 146 64.072 -10.981 13.803 1.00 21.91 C ANISOU 1207 CG2 VAL A 146 2865 3013 2445 -247 -330 150 C ATOM 1208 N GLN A 147 60.609 -14.225 14.014 1.00 19.02 N ANISOU 1208 N GLN A 147 2494 2693 2039 -393 -387 141 N ATOM 1209 CA GLN A 147 60.047 -15.564 14.227 1.00 18.96 C ANISOU 1209 CA GLN A 147 2508 2687 2008 -447 -406 150 C ATOM 1210 C GLN A 147 60.255 -16.403 12.976 1.00 18.44 C ANISOU 1210 C GLN A 147 2491 2580 1934 -429 -437 164 C ATOM 1211 O GLN A 147 59.930 -15.965 11.868 1.00 18.34 O ANISOU 1211 O GLN A 147 2474 2562 1933 -397 -449 157 O ATOM 1212 CB GLN A 147 58.551 -15.481 14.540 1.00 19.34 C ANISOU 1212 CB GLN A 147 2505 2783 2061 -489 -405 125 C ATOM 1213 N TRP A 148 60.793 -17.606 13.146 1.00 18.05 N ANISOU 1213 N TRP A 148 2491 2501 1866 -452 -455 182 N ATOM 1214 CA TRP A 148 60.963 -18.561 12.049 1.00 18.01 C ANISOU 1214 CA TRP A 148 2532 2457 1853 -441 -486 190 C ATOM 1215 C TRP A 148 59.779 -19.517 12.003 1.00 18.39 C ANISOU 1215 C TRP A 148 2583 2516 1888 -492 -511 191 C ATOM 1216 O TRP A 148 59.280 -19.968 13.041 1.00 18.26 O ANISOU 1216 O TRP A 148 2558 2521 1858 -549 -510 196 O ATOM 1217 CB TRP A 148 62.243 -19.386 12.218 1.00 17.97 C ANISOU 1217 CB TRP A 148 2578 2406 1843 -432 -497 204 C ATOM 1218 CG TRP A 148 63.500 -18.667 11.884 1.00 17.63 C ANISOU 1218 CG TRP A 148 2540 2344 1813 -376 -478 199 C ATOM 1219 CD1 TRP A 148 64.333 -18.036 12.755 1.00 17.49 C ANISOU 1219 CD1 TRP A 148 2511 2331 1803 -364 -455 202 C ATOM 1220 CD2 TRP A 148 64.090 -18.517 10.584 1.00 17.50 C ANISOU 1220 CD2 TRP A 148 2544 2305 1800 -330 -479 190 C ATOM 1221 NE1 TRP A 148 65.406 -17.505 12.083 1.00 17.16 N ANISOU 1221 NE1 TRP A 148 2479 2270 1772 -313 -441 194 N ATOM 1222 CE2 TRP A 148 65.274 -17.774 10.747 1.00 17.22 C ANISOU 1222 CE2 TRP A 148 2505 2263 1775 -294 -454 186 C ATOM 1223 CE3 TRP A 148 63.731 -18.936 9.296 1.00 17.55 C ANISOU 1223 CE3 TRP A 148 2571 2299 1798 -321 -498 183 C ATOM 1224 CZ2 TRP A 148 66.111 -17.453 9.680 1.00 17.27 C ANISOU 1224 CZ2 TRP A 148 2528 2253 1782 -252 -445 174 C ATOM 1225 CZ3 TRP A 148 64.559 -18.605 8.238 1.00 17.65 C ANISOU 1225 CZ3 TRP A 148 2602 2295 1810 -280 -489 171 C ATOM 1226 CH2 TRP A 148 65.729 -17.866 8.435 1.00 17.35 C ANISOU 1226 CH2 TRP A 148 2558 2253 1780 -248 -461 167 C ATOM 1227 N LYS A 149 59.330 -19.816 10.787 1.00 18.65 N ANISOU 1227 N LYS A 149 2630 2536 1920 -478 -533 187 N ATOM 1228 CA LYS A 149 58.334 -20.849 10.566 1.00 19.49 C ANISOU 1228 CA LYS A 149 2748 2645 2014 -523 -562 190 C ATOM 1229 C LYS A 149 58.813 -21.779 9.464 1.00 19.15 C ANISOU 1229 C LYS A 149 2760 2554 1964 -504 -592 195 C ATOM 1230 O LYS A 149 59.346 -21.331 8.451 1.00 19.08 O ANISOU 1230 O LYS A 149 2762 2527 1960 -455 -589 188 O ATOM 1231 CB LYS A 149 56.991 -20.240 10.177 1.00 20.33 C ANISOU 1231 CB LYS A 149 2803 2789 2130 -531 -562 172 C ATOM 1232 CG LYS A 149 56.407 -19.309 11.225 1.00 21.31 C ANISOU 1232 CG LYS A 149 2864 2965 2268 -550 -532 154 C ATOM 1233 CD LYS A 149 55.232 -18.544 10.657 1.00 22.32 C ANISOU 1233 CD LYS A 149 2938 3123 2418 -539 -538 129 C ATOM 1234 CE LYS A 149 54.782 -17.458 11.612 1.00 23.09 C ANISOU 1234 CE LYS A 149 2967 3269 2538 -545 -507 103 C ATOM 1235 NZ LYS A 149 53.692 -16.654 11.004 1.00 23.83 N ANISOU 1235 NZ LYS A 149 3006 3385 2665 -525 -520 73 N ATOM 1236 N VAL A 150 58.614 -23.076 9.679 1.00 18.94 N ANISOU 1236 N VAL A 150 2768 2506 1923 -546 -622 206 N ATOM 1237 CA VAL A 150 58.957 -24.105 8.712 1.00 19.09 C ANISOU 1237 CA VAL A 150 2838 2478 1936 -534 -655 207 C ATOM 1238 C VAL A 150 57.680 -24.899 8.469 1.00 19.52 C ANISOU 1238 C VAL A 150 2895 2544 1979 -583 -684 209 C ATOM 1239 O VAL A 150 57.107 -25.444 9.419 1.00 19.49 O ANISOU 1239 O VAL A 150 2888 2554 1964 -643 -692 221 O ATOM 1240 CB VAL A 150 60.078 -25.023 9.234 1.00 19.04 C ANISOU 1240 CB VAL A 150 2879 2424 1931 -535 -674 216 C ATOM 1241 CG1 VAL A 150 60.391 -26.107 8.212 1.00 19.31 C ANISOU 1241 CG1 VAL A 150 2962 2411 1966 -521 -710 208 C ATOM 1242 CG2 VAL A 150 61.325 -24.208 9.548 1.00 18.68 C ANISOU 1242 CG2 VAL A 150 2825 2372 1900 -489 -644 212 C ATOM 1243 N ASP A 151 57.217 -24.922 7.216 1.00 20.03 N ANISOU 1243 N ASP A 151 2964 2603 2042 -564 -698 199 N ATOM 1244 CA ASP A 151 55.912 -25.517 6.855 1.00 20.90 C ANISOU 1244 CA ASP A 151 3070 2728 2144 -606 -724 198 C ATOM 1245 C ASP A 151 54.785 -24.968 7.747 1.00 21.44 C ANISOU 1245 C ASP A 151 3079 2852 2215 -649 -707 195 C ATOM 1246 O ASP A 151 53.896 -25.708 8.187 1.00 21.60 O ANISOU 1246 O ASP A 151 3096 2888 2223 -710 -723 199 O ATOM 1247 CB ASP A 151 55.981 -27.055 6.893 1.00 21.39 C ANISOU 1247 CB ASP A 151 3186 2750 2193 -643 -764 209 C ATOM 1248 CG ASP A 151 56.808 -27.645 5.753 1.00 21.62 C ANISOU 1248 CG ASP A 151 3265 2728 2223 -601 -785 200 C ATOM 1249 OD1 ASP A 151 57.134 -26.942 4.781 1.00 21.87 O ANISOU 1249 OD1 ASP A 151 3292 2761 2257 -553 -770 185 O ATOM 1250 OD2 ASP A 151 57.124 -28.850 5.808 1.00 22.69 O ANISOU 1250 OD2 ASP A 151 3447 2820 2355 -619 -819 204 O ATOM 1251 N ASN A 152 54.859 -23.660 8.014 1.00 21.68 N ANISOU 1251 N ASN A 152 3062 2914 2262 -619 -674 184 N ATOM 1252 CA ASN A 152 53.903 -22.926 8.849 1.00 22.78 C ANISOU 1252 CA ASN A 152 3135 3110 2412 -649 -652 169 C ATOM 1253 C ASN A 152 53.914 -23.287 10.348 1.00 23.00 C ANISOU 1253 C ASN A 152 3155 3159 2424 -708 -634 176 C ATOM 1254 O ASN A 152 53.018 -22.869 11.086 1.00 24.60 O ANISOU 1254 O ASN A 152 3303 3415 2630 -747 -614 158 O ATOM 1255 CB ASN A 152 52.478 -23.051 8.259 1.00 23.78 C ANISOU 1255 CB ASN A 152 3230 3262 2544 -674 -673 153 C ATOM 1256 CG ASN A 152 51.608 -21.826 8.508 1.00 24.74 C ANISOU 1256 CG ASN A 152 3272 3434 2694 -666 -654 124 C ATOM 1257 OD1 ASN A 152 50.377 -21.937 8.547 1.00 26.79 O ANISOU 1257 OD1 ASN A 152 3489 3728 2961 -702 -663 105 O ATOM 1258 ND2 ASN A 152 52.225 -20.660 8.644 1.00 24.95 N ANISOU 1258 ND2 ASN A 152 3277 3463 2739 -617 -630 118 N ATOM 1259 N ALA A 153 54.929 -24.024 10.811 1.00 22.38 N ANISOU 1259 N ALA A 153 3130 3043 2330 -716 -642 199 N ATOM 1260 CA ALA A 153 55.074 -24.365 12.232 1.00 21.97 C ANISOU 1260 CA ALA A 153 3082 3006 2259 -775 -632 212 C ATOM 1261 C ALA A 153 56.097 -23.429 12.862 1.00 21.20 C ANISOU 1261 C ALA A 153 2972 2909 2172 -737 -599 211 C ATOM 1262 O ALA A 153 57.222 -23.323 12.373 1.00 20.01 O ANISOU 1262 O ALA A 153 2853 2716 2033 -680 -604 218 O ATOM 1263 CB ALA A 153 55.525 -25.807 12.382 1.00 22.31 C ANISOU 1263 CB ALA A 153 3196 2998 2282 -811 -673 239 C ATOM 1264 N LEU A 154 55.716 -22.764 13.953 1.00 21.28 N ANISOU 1264 N LEU A 154 2935 2970 2178 -771 -566 200 N ATOM 1265 CA LEU A 154 56.623 -21.851 14.652 1.00 21.07 C ANISOU 1265 CA LEU A 154 2896 2950 2161 -741 -534 199 C ATOM 1266 C LEU A 154 57.810 -22.627 15.219 1.00 20.59 C ANISOU 1266 C LEU A 154 2897 2841 2085 -750 -554 229 C ATOM 1267 O LEU A 154 57.639 -23.662 15.862 1.00 20.83 O ANISOU 1267 O LEU A 154 2963 2862 2090 -816 -578 249 O ATOM 1268 CB LEU A 154 55.891 -21.124 15.787 1.00 21.78 C ANISOU 1268 CB LEU A 154 2924 3106 2246 -787 -496 176 C ATOM 1269 CG LEU A 154 56.626 -20.020 16.551 1.00 22.05 C ANISOU 1269 CG LEU A 154 2931 3156 2291 -759 -459 168 C ATOM 1270 CD1 LEU A 154 56.963 -18.844 15.653 1.00 21.89 C ANISOU 1270 CD1 LEU A 154 2884 3127 2308 -673 -448 152 C ATOM 1271 CD2 LEU A 154 55.789 -19.562 17.740 1.00 22.70 C ANISOU 1271 CD2 LEU A 154 2957 3307 2361 -821 -424 141 C ATOM 1272 N GLN A 155 59.009 -22.128 14.951 1.00 19.76 N ANISOU 1272 N GLN A 155 2806 2704 1999 -686 -547 232 N ATOM 1273 CA GLN A 155 60.241 -22.746 15.428 1.00 19.80 C ANISOU 1273 CA GLN A 155 2863 2660 2001 -682 -567 255 C ATOM 1274 C GLN A 155 60.645 -22.151 16.766 1.00 20.01 C ANISOU 1274 C GLN A 155 2872 2711 2018 -706 -541 260 C ATOM 1275 O GLN A 155 60.385 -20.977 17.044 1.00 19.86 O ANISOU 1275 O GLN A 155 2800 2738 2008 -691 -499 240 O ATOM 1276 CB GLN A 155 61.359 -22.561 14.408 1.00 19.20 C ANISOU 1276 CB GLN A 155 2807 2537 1948 -602 -572 249 C ATOM 1277 CG GLN A 155 61.021 -23.086 13.025 1.00 19.12 C ANISOU 1277 CG GLN A 155 2815 2505 1943 -578 -595 241 C ATOM 1278 CD GLN A 155 60.791 -24.580 13.023 1.00 19.41 C ANISOU 1278 CD GLN A 155 2902 2506 1967 -622 -644 256 C ATOM 1279 OE1 GLN A 155 59.656 -25.050 12.879 1.00 20.08 O ANISOU 1279 OE1 GLN A 155 2982 2610 2037 -667 -657 257 O ATOM 1280 NE2 GLN A 155 61.860 -25.336 13.186 1.00 19.22 N ANISOU 1280 NE2 GLN A 155 2924 2427 1950 -610 -674 266 N ATOM 1281 N SER A 156 61.299 -22.968 17.584 1.00 20.53 N ANISOU 1281 N SER A 156 2986 2744 2070 -742 -570 285 N ATOM 1282 CA SER A 156 61.813 -22.525 18.871 1.00 20.96 C ANISOU 1282 CA SER A 156 3035 2815 2113 -768 -552 295 C ATOM 1283 C SER A 156 63.093 -23.275 19.181 1.00 20.92 C ANISOU 1283 C SER A 156 3090 2743 2114 -757 -595 320 C ATOM 1284 O SER A 156 63.156 -24.493 19.019 1.00 21.02 O ANISOU 1284 O SER A 156 3155 2710 2123 -781 -647 338 O ATOM 1285 CB SER A 156 60.783 -22.790 19.962 1.00 21.78 C ANISOU 1285 CB SER A 156 3129 2969 2178 -866 -545 300 C ATOM 1286 OG SER A 156 61.194 -22.217 21.179 1.00 22.67 O ANISOU 1286 OG SER A 156 3231 3106 2276 -893 -521 304 O ATOM 1287 N GLY A 157 64.112 -22.529 19.594 1.00 20.73 N ANISOU 1287 N GLY A 157 3057 2713 2106 -717 -576 318 N ATOM 1288 CA GLY A 157 65.347 -23.105 20.092 1.00 21.25 C ANISOU 1288 CA GLY A 157 3172 2722 2182 -709 -615 338 C ATOM 1289 C GLY A 157 66.437 -23.386 19.078 1.00 21.05 C ANISOU 1289 C GLY A 157 3167 2636 2196 -630 -638 327 C ATOM 1290 O GLY A 157 67.566 -23.646 19.476 1.00 21.93 O ANISOU 1290 O GLY A 157 3305 2703 2325 -610 -665 335 O ATOM 1291 N ASN A 158 66.127 -23.257 17.786 1.00 20.35 N ANISOU 1291 N ASN A 158 3062 2550 2121 -584 -625 305 N ATOM 1292 CA ASN A 158 67.020 -23.690 16.687 1.00 19.95 C ANISOU 1292 CA ASN A 158 3032 2447 2101 -519 -646 288 C ATOM 1293 C ASN A 158 67.542 -22.512 15.852 1.00 19.82 C ANISOU 1293 C ASN A 158 2978 2450 2104 -448 -597 261 C ATOM 1294 O ASN A 158 68.039 -22.701 14.731 1.00 19.16 O ANISOU 1294 O ASN A 158 2902 2340 2039 -400 -601 240 O ATOM 1295 CB ASN A 158 66.397 -24.812 15.808 1.00 19.99 C ANISOU 1295 CB ASN A 158 3068 2425 2103 -532 -684 286 C ATOM 1296 CG ASN A 158 65.069 -24.439 15.143 1.00 19.67 C ANISOU 1296 CG ASN A 158 2996 2434 2044 -548 -657 278 C ATOM 1297 OD1 ASN A 158 64.545 -25.220 14.332 1.00 20.25 O ANISOU 1297 OD1 ASN A 158 3090 2490 2115 -554 -683 274 O ATOM 1298 ND2 ASN A 158 64.500 -23.308 15.503 1.00 18.92 N ANISOU 1298 ND2 ASN A 158 2854 2397 1939 -555 -610 274 N ATOM 1299 N SER A 159 67.449 -21.307 16.411 1.00 19.85 N ANISOU 1299 N SER A 159 2941 2499 2103 -447 -552 261 N ATOM 1300 CA SER A 159 68.031 -20.117 15.788 1.00 20.18 C ANISOU 1300 CA SER A 159 2950 2556 2161 -386 -510 240 C ATOM 1301 C SER A 159 68.953 -19.377 16.750 1.00 20.53 C ANISOU 1301 C SER A 159 2981 2604 2215 -374 -490 244 C ATOM 1302 O SER A 159 68.832 -19.517 17.970 1.00 20.81 O ANISOU 1302 O SER A 159 3021 2648 2237 -420 -499 263 O ATOM 1303 CB SER A 159 66.938 -19.193 15.248 1.00 20.51 C ANISOU 1303 CB SER A 159 2952 2648 2194 -385 -476 231 C ATOM 1304 OG SER A 159 66.014 -18.815 16.246 1.00 21.23 O ANISOU 1304 OG SER A 159 3015 2783 2269 -434 -462 238 O ATOM 1305 N GLN A 160 69.894 -18.623 16.182 1.00 20.58 N ANISOU 1305 N GLN A 160 2974 2605 2241 -317 -465 227 N ATOM 1306 CA GLN A 160 70.743 -17.688 16.943 1.00 20.87 C ANISOU 1306 CA GLN A 160 2991 2652 2289 -299 -439 227 C ATOM 1307 C GLN A 160 70.729 -16.338 16.216 1.00 20.67 C ANISOU 1307 C GLN A 160 2928 2658 2268 -259 -394 212 C ATOM 1308 O GLN A 160 70.733 -16.309 14.975 1.00 19.99 O ANISOU 1308 O GLN A 160 2846 2566 2185 -230 -390 197 O ATOM 1309 CB GLN A 160 72.180 -18.229 17.102 1.00 21.68 C ANISOU 1309 CB GLN A 160 3117 2705 2416 -271 -464 222 C ATOM 1310 CG GLN A 160 72.302 -19.452 18.030 1.00 22.60 C ANISOU 1310 CG GLN A 160 3272 2783 2531 -312 -518 243 C ATOM 1311 CD GLN A 160 73.745 -19.833 18.385 1.00 23.42 C ANISOU 1311 CD GLN A 160 3394 2837 2668 -283 -547 236 C ATOM 1312 OE1 GLN A 160 74.239 -19.516 19.480 1.00 25.24 O ANISOU 1312 OE1 GLN A 160 3623 3068 2900 -297 -550 251 O ATOM 1313 NE2 GLN A 160 74.425 -20.521 17.473 1.00 23.90 N ANISOU 1313 NE2 GLN A 160 3469 2857 2756 -242 -570 211 N ATOM 1314 N GLU A 161 70.662 -15.246 16.988 1.00 20.82 N ANISOU 1314 N GLU A 161 2916 2710 2286 -263 -364 214 N ATOM 1315 CA GLU A 161 70.607 -13.859 16.495 1.00 20.86 C ANISOU 1315 CA GLU A 161 2887 2743 2298 -230 -327 203 C ATOM 1316 C GLU A 161 71.915 -13.126 16.818 1.00 19.68 C ANISOU 1316 C GLU A 161 2730 2584 2164 -197 -306 199 C ATOM 1317 O GLU A 161 72.576 -13.410 17.834 1.00 19.52 O ANISOU 1317 O GLU A 161 2719 2551 2148 -210 -315 207 O ATOM 1318 CB GLU A 161 69.446 -13.060 17.140 1.00 22.00 C ANISOU 1318 CB GLU A 161 2992 2933 2435 -258 -308 202 C ATOM 1319 CG GLU A 161 68.071 -13.198 16.485 1.00 23.49 C ANISOU 1319 CG GLU A 161 3168 3141 2615 -275 -316 196 C ATOM 1320 CD GLU A 161 67.015 -12.303 17.115 1.00 24.29 C ANISOU 1320 CD GLU A 161 3222 3290 2719 -296 -296 184 C ATOM 1321 OE1 GLU A 161 67.368 -11.357 17.869 1.00 26.58 O ANISOU 1321 OE1 GLU A 161 3486 3596 3017 -288 -272 178 O ATOM 1322 OE2 GLU A 161 65.811 -12.546 16.869 1.00 26.56 O ANISOU 1322 OE2 GLU A 161 3494 3598 3001 -320 -305 176 O ATOM 1323 N SER A 162 72.254 -12.160 15.971 1.00 18.28 N ANISOU 1323 N SER A 162 2539 2413 1993 -160 -282 187 N ATOM 1324 CA SER A 162 73.413 -11.300 16.152 1.00 17.72 C ANISOU 1324 CA SER A 162 2458 2339 1937 -130 -259 182 C ATOM 1325 C SER A 162 73.034 -9.920 15.629 1.00 16.86 C ANISOU 1325 C SER A 162 2324 2255 1828 -112 -234 178 C ATOM 1326 O SER A 162 72.369 -9.819 14.604 1.00 15.88 O ANISOU 1326 O SER A 162 2203 2136 1696 -108 -238 175 O ATOM 1327 CB SER A 162 74.574 -11.875 15.341 1.00 18.54 C ANISOU 1327 CB SER A 162 2584 2410 2048 -101 -264 168 C ATOM 1328 OG SER A 162 75.741 -11.138 15.493 1.00 19.58 O ANISOU 1328 OG SER A 162 2706 2541 2195 -75 -241 160 O ATOM 1329 N VAL A 163 73.427 -8.867 16.340 1.00 16.35 N ANISOU 1329 N VAL A 163 2236 2204 1773 -104 -212 179 N ATOM 1330 CA VAL A 163 73.055 -7.489 15.982 1.00 16.39 C ANISOU 1330 CA VAL A 163 2216 2228 1783 -88 -195 175 C ATOM 1331 C VAL A 163 74.299 -6.630 15.922 1.00 16.27 C ANISOU 1331 C VAL A 163 2200 2205 1777 -61 -174 173 C ATOM 1332 O VAL A 163 75.182 -6.753 16.773 1.00 16.29 O ANISOU 1332 O VAL A 163 2201 2201 1787 -61 -166 174 O ATOM 1333 CB VAL A 163 72.063 -6.892 17.002 1.00 16.54 C ANISOU 1333 CB VAL A 163 2200 2277 1809 -109 -190 173 C ATOM 1334 CG1 VAL A 163 71.455 -5.583 16.507 1.00 16.62 C ANISOU 1334 CG1 VAL A 163 2184 2299 1830 -90 -185 165 C ATOM 1335 CG2 VAL A 163 70.964 -7.887 17.318 1.00 17.09 C ANISOU 1335 CG2 VAL A 163 2270 2358 1867 -145 -208 173 C ATOM 1336 N THR A 164 74.385 -5.764 14.926 1.00 16.47 N ANISOU 1336 N THR A 164 2227 2231 1800 -43 -166 172 N ATOM 1337 CA THR A 164 75.497 -4.824 14.857 1.00 17.06 C ANISOU 1337 CA THR A 164 2300 2302 1881 -24 -145 170 C ATOM 1338 C THR A 164 75.305 -3.701 15.861 1.00 17.82 C ANISOU 1338 C THR A 164 2365 2413 1993 -22 -135 172 C ATOM 1339 O THR A 164 74.210 -3.462 16.380 1.00 17.88 O ANISOU 1339 O THR A 164 2350 2436 2008 -33 -143 170 O ATOM 1340 CB THR A 164 75.644 -4.216 13.466 1.00 17.05 C ANISOU 1340 CB THR A 164 2314 2296 1866 -14 -143 171 C ATOM 1341 OG1 THR A 164 74.393 -3.624 13.081 1.00 16.95 O ANISOU 1341 OG1 THR A 164 2295 2291 1855 -18 -162 178 O ATOM 1342 CG2 THR A 164 76.067 -5.276 12.462 1.00 17.44 C ANISOU 1342 CG2 THR A 164 2393 2334 1898 -16 -145 162 C ATOM 1343 N GLU A 165 76.394 -3.013 16.143 1.00 18.64 N ANISOU 1343 N GLU A 165 2466 2513 2105 -9 -116 172 N ATOM 1344 CA GLU A 165 76.316 -1.786 16.906 1.00 19.62 C ANISOU 1344 CA GLU A 165 2563 2647 2244 -4 -106 172 C ATOM 1345 C GLU A 165 75.811 -0.682 15.986 1.00 18.96 C ANISOU 1345 C GLU A 165 2479 2562 2163 7 -115 175 C ATOM 1346 O GLU A 165 75.856 -0.788 14.751 1.00 18.90 O ANISOU 1346 O GLU A 165 2496 2545 2140 8 -123 181 O ATOM 1347 CB GLU A 165 77.670 -1.458 17.541 1.00 21.23 C ANISOU 1347 CB GLU A 165 2765 2846 2455 5 -85 171 C ATOM 1348 CG GLU A 165 78.121 -2.479 18.587 1.00 22.99 C ANISOU 1348 CG GLU A 165 2989 3066 2680 -7 -87 170 C ATOM 1349 CD GLU A 165 77.143 -2.626 19.736 1.00 24.37 C ANISOU 1349 CD GLU A 165 3145 3259 2855 -31 -94 170 C ATOM 1350 OE1 GLU A 165 76.853 -1.614 20.408 1.00 26.92 O ANISOU 1350 OE1 GLU A 165 3443 3598 3188 -31 -83 164 O ATOM 1351 OE2 GLU A 165 76.630 -3.749 19.972 1.00 27.10 O ANISOU 1351 OE2 GLU A 165 3502 3605 3191 -52 -110 172 O ATOM 1352 N GLN A 166 75.295 0.372 16.601 1.00 18.54 N ANISOU 1352 N GLN A 166 2398 2518 2130 12 -117 170 N ATOM 1353 CA GLN A 166 74.667 1.448 15.862 1.00 18.55 C ANISOU 1353 CA GLN A 166 2395 2511 2141 23 -137 173 C ATOM 1354 C GLN A 166 75.634 2.056 14.845 1.00 18.52 C ANISOU 1354 C GLN A 166 2424 2490 2124 29 -134 187 C ATOM 1355 O GLN A 166 76.787 2.350 15.172 1.00 18.48 O ANISOU 1355 O GLN A 166 2422 2483 2116 32 -111 189 O ATOM 1356 CB GLN A 166 74.146 2.515 16.824 1.00 18.62 C ANISOU 1356 CB GLN A 166 2365 2529 2181 31 -139 158 C ATOM 1357 CG GLN A 166 73.241 3.524 16.161 1.00 18.87 C ANISOU 1357 CG GLN A 166 2388 2549 2234 43 -172 155 C ATOM 1358 CD GLN A 166 72.548 4.416 17.165 1.00 18.80 C ANISOU 1358 CD GLN A 166 2332 2551 2262 53 -177 129 C ATOM 1359 OE1 GLN A 166 73.111 4.745 18.214 1.00 18.71 O ANISOU 1359 OE1 GLN A 166 2302 2550 2257 53 -152 119 O ATOM 1360 NE2 GLN A 166 71.344 4.839 16.842 1.00 18.72 N ANISOU 1360 NE2 GLN A 166 2299 2537 2278 61 -210 113 N ATOM 1361 N ASP A 167 75.182 2.217 13.608 1.00 18.75 N ANISOU 1361 N ASP A 167 2476 2507 2140 26 -158 197 N ATOM 1362 CA ASP A 167 76.051 2.681 12.529 1.00 19.02 C ANISOU 1362 CA ASP A 167 2547 2530 2150 19 -155 211 C ATOM 1363 C ASP A 167 76.461 4.141 12.761 1.00 18.85 C ANISOU 1363 C ASP A 167 2521 2498 2145 26 -158 219 C ATOM 1364 O ASP A 167 75.618 4.979 13.094 1.00 18.32 O ANISOU 1364 O ASP A 167 2433 2423 2106 38 -186 217 O ATOM 1365 CB ASP A 167 75.349 2.537 11.183 1.00 19.89 C ANISOU 1365 CB ASP A 167 2688 2630 2239 8 -186 223 C ATOM 1366 CG ASP A 167 76.247 2.885 10.012 1.00 20.80 C ANISOU 1366 CG ASP A 167 2847 2739 2320 -10 -179 236 C ATOM 1367 OD1 ASP A 167 77.000 2.005 9.557 1.00 22.66 O ANISOU 1367 OD1 ASP A 167 3100 2984 2528 -22 -152 228 O ATOM 1368 OD2 ASP A 167 76.203 4.029 9.534 1.00 21.12 O ANISOU 1368 OD2 ASP A 167 2903 2764 2359 -16 -202 252 O ATOM 1369 N ASER A 168 77.748 4.431 12.571 0.50 18.76 N ANISOU 1369 N ASER A 168 2527 2486 2116 19 -132 224 N ATOM 1370 N BSER A 168 77.747 4.429 12.567 0.50 18.85 N ANISOU 1370 N BSER A 168 2539 2498 2128 19 -132 224 N ATOM 1371 CA ASER A 168 78.303 5.759 12.852 0.50 18.94 C ANISOU 1371 CA ASER A 168 2547 2498 2151 22 -132 232 C ATOM 1372 CA BSER A 168 78.308 5.755 12.846 0.50 19.08 C ANISOU 1372 CA BSER A 168 2565 2516 2168 22 -132 232 C ATOM 1373 C ASER A 168 77.827 6.849 11.888 0.50 19.39 C ANISOU 1373 C ASER A 168 2632 2533 2204 13 -173 252 C ATOM 1374 C BSER A 168 77.863 6.847 11.872 0.50 19.46 C ANISOU 1374 C BSER A 168 2641 2542 2212 13 -172 252 C ATOM 1375 O ASER A 168 77.947 8.039 12.203 0.50 19.65 O ANISOU 1375 O ASER A 168 2659 2550 2257 19 -187 258 O ATOM 1376 O BSER A 168 78.044 8.035 12.163 0.50 19.71 O ANISOU 1376 O BSER A 168 2669 2558 2261 18 -185 259 O ATOM 1377 CB ASER A 168 79.830 5.704 12.812 0.50 18.88 C ANISOU 1377 CB ASER A 168 2551 2499 2124 12 -93 230 C ATOM 1378 CB BSER A 168 79.837 5.681 12.858 0.50 19.10 C ANISOU 1378 CB BSER A 168 2577 2527 2152 12 -92 229 C ATOM 1379 OG ASER A 168 80.278 5.621 11.473 0.50 19.29 O ANISOU 1379 OG ASER A 168 2643 2551 2137 -13 -90 239 O ATOM 1380 OG BSER A 168 80.286 4.854 13.911 0.50 19.26 O ANISOU 1380 OG BSER A 168 2571 2561 2186 24 -65 212 O ATOM 1381 N LYS A 169 77.311 6.453 10.721 1.00 19.73 N ANISOU 1381 N LYS A 169 2706 2570 2221 -2 -196 263 N ATOM 1382 CA LYS A 169 76.831 7.395 9.700 1.00 20.06 C ANISOU 1382 CA LYS A 169 2783 2586 2255 -17 -244 287 C ATOM 1383 C LYS A 169 75.305 7.553 9.704 1.00 20.06 C ANISOU 1383 C LYS A 169 2764 2569 2288 1 -297 284 C ATOM 1384 O LYS A 169 74.806 8.673 9.840 1.00 21.16 O ANISOU 1384 O LYS A 169 2897 2683 2460 13 -339 289 O ATOM 1385 CB LYS A 169 77.304 6.960 8.309 1.00 20.67 C ANISOU 1385 CB LYS A 169 2911 2667 2276 -53 -239 301 C ATOM 1386 N ASP A 170 74.569 6.447 9.542 1.00 19.37 N ANISOU 1386 N ASP A 170 2669 2495 2196 3 -298 274 N ATOM 1387 CA ASP A 170 73.096 6.504 9.445 1.00 19.06 C ANISOU 1387 CA ASP A 170 2611 2442 2187 17 -348 267 C ATOM 1388 C ASP A 170 72.337 6.148 10.727 1.00 18.13 C ANISOU 1388 C ASP A 170 2433 2344 2113 42 -337 236 C ATOM 1389 O ASP A 170 71.109 6.198 10.746 1.00 18.07 O ANISOU 1389 O ASP A 170 2400 2331 2135 53 -373 223 O ATOM 1390 CB ASP A 170 72.565 5.716 8.222 1.00 19.64 C ANISOU 1390 CB ASP A 170 2720 2514 2227 -3 -370 279 C ATOM 1391 CG ASP A 170 72.679 4.209 8.365 1.00 19.78 C ANISOU 1391 CG ASP A 170 2732 2560 2223 -8 -330 265 C ATOM 1392 OD1 ASP A 170 72.828 3.706 9.485 1.00 18.89 O ANISOU 1392 OD1 ASP A 170 2581 2466 2129 6 -296 245 O ATOM 1393 OD2 ASP A 170 72.585 3.519 7.325 1.00 20.80 O ANISOU 1393 OD2 ASP A 170 2896 2690 2316 -28 -337 274 O ATOM 1394 N SER A 171 73.055 5.767 11.784 1.00 16.94 N ANISOU 1394 N SER A 171 2259 2216 1963 46 -287 222 N ATOM 1395 CA SER A 171 72.470 5.531 13.106 1.00 16.53 C ANISOU 1395 CA SER A 171 2153 2184 1944 59 -272 193 C ATOM 1396 C SER A 171 71.472 4.365 13.188 1.00 16.33 C ANISOU 1396 C SER A 171 2110 2178 1917 53 -275 179 C ATOM 1397 O SER A 171 70.629 4.323 14.089 1.00 16.64 O ANISOU 1397 O SER A 171 2103 2234 1985 58 -275 152 O ATOM 1398 CB SER A 171 71.842 6.826 13.646 1.00 16.84 C ANISOU 1398 CB SER A 171 2156 2211 2032 80 -302 176 C ATOM 1399 OG SER A 171 72.787 7.893 13.564 1.00 17.00 O ANISOU 1399 OG SER A 171 2196 2210 2052 84 -302 192 O ATOM 1400 N THR A 172 71.597 3.414 12.265 1.00 15.96 N ANISOU 1400 N THR A 172 2100 2131 1835 37 -274 194 N ATOM 1401 CA THR A 172 70.736 2.227 12.242 1.00 15.82 C ANISOU 1401 CA THR A 172 2072 2128 1810 27 -278 184 C ATOM 1402 C THR A 172 71.447 1.000 12.790 1.00 15.47 C ANISOU 1402 C THR A 172 2034 2101 1742 15 -238 182 C ATOM 1403 O THR A 172 72.668 0.998 12.988 1.00 15.41 O ANISOU 1403 O THR A 172 2042 2092 1721 15 -209 188 O ATOM 1404 CB THR A 172 70.238 1.881 10.817 1.00 16.12 C ANISOU 1404 CB THR A 172 2147 2151 1826 18 -312 200 C ATOM 1405 OG1 THR A 172 71.345 1.519 9.980 1.00 16.07 O ANISOU 1405 OG1 THR A 172 2189 2138 1778 4 -293 218 O ATOM 1406 CG2 THR A 172 69.481 3.050 10.194 1.00 16.54 C ANISOU 1406 CG2 THR A 172 2200 2180 1905 29 -365 205 C ATOM 1407 N TYR A 173 70.652 -0.037 13.025 1.00 15.43 N ANISOU 1407 N TYR A 173 2017 2110 1735 3 -241 172 N ATOM 1408 CA TYR A 173 71.120 -1.365 13.398 1.00 15.19 C ANISOU 1408 CA TYR A 173 1999 2089 1683 -13 -218 172 C ATOM 1409 C TYR A 173 70.810 -2.320 12.266 1.00 14.87 C ANISOU 1409 C TYR A 173 1991 2040 1618 -23 -235 180 C ATOM 1410 O TYR A 173 69.931 -2.066 11.444 1.00 14.98 O ANISOU 1410 O TYR A 173 2009 2049 1635 -22 -265 182 O ATOM 1411 CB TYR A 173 70.395 -1.861 14.642 1.00 15.78 C ANISOU 1411 CB TYR A 173 2037 2187 1771 -27 -210 156 C ATOM 1412 CG TYR A 173 70.555 -0.951 15.827 1.00 16.21 C ANISOU 1412 CG TYR A 173 2057 2256 1848 -22 -193 143 C ATOM 1413 CD1 TYR A 173 71.639 -1.079 16.682 1.00 16.47 C ANISOU 1413 CD1 TYR A 173 2094 2290 1874 -25 -165 146 C ATOM 1414 CD2 TYR A 173 69.625 0.056 16.082 1.00 17.01 C ANISOU 1414 CD2 TYR A 173 2117 2365 1980 -12 -207 123 C ATOM 1415 CE1 TYR A 173 71.793 -0.231 17.766 1.00 16.96 C ANISOU 1415 CE1 TYR A 173 2125 2365 1954 -22 -149 133 C ATOM 1416 CE2 TYR A 173 69.770 0.904 17.169 1.00 17.47 C ANISOU 1416 CE2 TYR A 173 2142 2437 2061 -7 -190 105 C ATOM 1417 CZ TYR A 173 70.852 0.748 18.006 1.00 17.32 C ANISOU 1417 CZ TYR A 173 2131 2421 2028 -14 -160 112 C ATOM 1418 OH TYR A 173 71.003 1.594 19.079 1.00 18.90 O ANISOU 1418 OH TYR A 173 2299 2635 2247 -11 -143 94 O ATOM 1419 N SER A 174 71.549 -3.419 12.226 1.00 14.25 N ANISOU 1419 N SER A 174 1936 1959 1519 -31 -218 181 N ATOM 1420 CA SER A 174 71.197 -4.556 11.390 1.00 14.26 C ANISOU 1420 CA SER A 174 1963 1954 1499 -43 -233 182 C ATOM 1421 C SER A 174 71.274 -5.815 12.231 1.00 14.05 C ANISOU 1421 C SER A 174 1934 1931 1471 -57 -226 177 C ATOM 1422 O SER A 174 71.960 -5.854 13.246 1.00 13.76 O ANISOU 1422 O SER A 174 1888 1898 1444 -57 -208 175 O ATOM 1423 CB SER A 174 72.097 -4.625 10.159 1.00 14.18 C ANISOU 1423 CB SER A 174 1994 1931 1464 -40 -227 186 C ATOM 1424 OG SER A 174 71.890 -3.493 9.318 1.00 14.41 O ANISOU 1424 OG SER A 174 2032 1954 1488 -37 -242 197 O ATOM 1425 N LEU A 175 70.539 -6.843 11.821 1.00 14.17 N ANISOU 1425 N LEU A 175 1962 1946 1476 -73 -245 176 N ATOM 1426 CA LEU A 175 70.398 -8.055 12.612 1.00 14.53 C ANISOU 1426 CA LEU A 175 2009 1992 1520 -93 -248 174 C ATOM 1427 C LEU A 175 70.391 -9.254 11.677 1.00 14.63 C ANISOU 1427 C LEU A 175 2056 1987 1514 -100 -265 173 C ATOM 1428 O LEU A 175 69.731 -9.222 10.621 1.00 14.69 O ANISOU 1428 O LEU A 175 2074 1994 1512 -100 -281 173 O ATOM 1429 CB LEU A 175 69.099 -8.011 13.435 1.00 15.04 C ANISOU 1429 CB LEU A 175 2039 2080 1594 -116 -257 170 C ATOM 1430 CG LEU A 175 68.731 -9.208 14.329 1.00 15.56 C ANISOU 1430 CG LEU A 175 2108 2153 1653 -151 -264 171 C ATOM 1431 CD1 LEU A 175 67.879 -8.730 15.498 1.00 16.04 C ANISOU 1431 CD1 LEU A 175 2126 2246 1723 -174 -255 162 C ATOM 1432 CD2 LEU A 175 67.987 -10.324 13.596 1.00 16.11 C ANISOU 1432 CD2 LEU A 175 2198 2214 1708 -169 -290 173 C ATOM 1433 N ASER A 176 71.150 -10.283 12.043 0.50 14.58 N ANISOU 1433 N ASER A 176 2068 1965 1507 -104 -265 170 N ATOM 1434 N BSER A 176 71.090 -10.317 12.073 0.50 14.95 N ANISOU 1434 N BSER A 176 2114 2012 1553 -105 -266 170 N ATOM 1435 CA ASER A 176 71.051 -11.578 11.392 0.50 14.85 C ANISOU 1435 CA ASER A 176 2132 1981 1530 -113 -286 164 C ATOM 1436 CA BSER A 176 71.153 -11.573 11.315 0.50 15.42 C ANISOU 1436 CA BSER A 176 2206 2052 1602 -110 -284 163 C ATOM 1437 C ASER A 176 70.366 -12.549 12.328 0.50 15.25 C ANISOU 1437 C ASER A 176 2181 2031 1582 -144 -306 172 C ATOM 1438 C BSER A 176 70.636 -12.711 12.203 0.50 15.67 C ANISOU 1438 C BSER A 176 2241 2077 1634 -139 -307 170 C ATOM 1439 O ASER A 176 70.464 -12.458 13.559 0.50 14.90 O ANISOU 1439 O ASER A 176 2122 1994 1545 -158 -301 179 O ATOM 1440 O BSER A 176 71.179 -12.903 13.298 0.50 15.56 O ANISOU 1440 O BSER A 176 2224 2058 1631 -146 -304 174 O ATOM 1441 CB ASER A 176 72.420 -12.109 11.018 0.50 14.83 C ANISOU 1441 CB ASER A 176 2152 1955 1529 -94 -278 149 C ATOM 1442 CB BSER A 176 72.609 -11.804 10.881 0.50 15.68 C ANISOU 1442 CB BSER A 176 2258 2065 1636 -88 -271 148 C ATOM 1443 OG ASER A 176 73.132 -12.468 12.184 0.50 14.36 O ANISOU 1443 OG ASER A 176 2088 1884 1486 -94 -278 151 O ATOM 1444 OG BSER A 176 72.818 -13.042 10.225 0.50 16.18 O ANISOU 1444 OG BSER A 176 2349 2106 1694 -89 -288 134 O ATOM 1445 N SER A 177 69.615 -13.455 11.739 1.00 15.91 N ANISOU 1445 N SER A 177 2282 2108 1654 -160 -330 172 N ATOM 1446 CA SER A 177 69.032 -14.587 12.480 1.00 16.39 C ANISOU 1446 CA SER A 177 2353 2163 1712 -196 -355 180 C ATOM 1447 C SER A 177 69.326 -15.826 11.649 1.00 16.74 C ANISOU 1447 C SER A 177 2434 2174 1751 -193 -380 172 C ATOM 1448 O SER A 177 69.008 -15.849 10.454 1.00 16.67 O ANISOU 1448 O SER A 177 2437 2165 1732 -183 -384 163 O ATOM 1449 CB SER A 177 67.537 -14.407 12.704 1.00 17.00 C ANISOU 1449 CB SER A 177 2406 2272 1784 -227 -361 184 C ATOM 1450 OG SER A 177 66.960 -15.518 13.404 1.00 17.77 O ANISOU 1450 OG SER A 177 2515 2367 1872 -271 -384 193 O ATOM 1451 N THR A 178 69.949 -16.829 12.243 1.00 16.59 N ANISOU 1451 N THR A 178 2437 2126 1740 -202 -400 173 N ATOM 1452 CA THR A 178 70.350 -18.029 11.522 1.00 16.80 C ANISOU 1452 CA THR A 178 2498 2115 1769 -194 -428 159 C ATOM 1453 C THR A 178 69.627 -19.224 12.105 1.00 16.73 C ANISOU 1453 C THR A 178 2511 2091 1756 -236 -468 174 C ATOM 1454 O THR A 178 69.801 -19.525 13.282 1.00 16.42 O ANISOU 1454 O THR A 178 2475 2042 1721 -260 -482 189 O ATOM 1455 CB THR A 178 71.865 -18.257 11.603 1.00 17.30 C ANISOU 1455 CB THR A 178 2571 2148 1855 -162 -426 140 C ATOM 1456 OG1 THR A 178 72.535 -17.086 11.118 1.00 17.72 O ANISOU 1456 OG1 THR A 178 2604 2221 1909 -130 -386 127 O ATOM 1457 CG2 THR A 178 72.289 -19.483 10.799 1.00 17.86 C ANISOU 1457 CG2 THR A 178 2671 2179 1934 -150 -455 115 C ATOM 1458 N LEU A 179 68.830 -19.891 11.272 1.00 16.71 N ANISOU 1458 N LEU A 179 2524 2083 1741 -249 -488 170 N ATOM 1459 CA LEU A 179 68.114 -21.116 11.619 1.00 17.26 C ANISOU 1459 CA LEU A 179 2619 2135 1804 -291 -530 183 C ATOM 1460 C LEU A 179 68.986 -22.288 11.198 1.00 18.01 C ANISOU 1460 C LEU A 179 2751 2175 1916 -273 -564 166 C ATOM 1461 O LEU A 179 69.403 -22.370 10.046 1.00 17.80 O ANISOU 1461 O LEU A 179 2731 2138 1893 -239 -558 139 O ATOM 1462 CB LEU A 179 66.783 -21.174 10.860 1.00 17.21 C ANISOU 1462 CB LEU A 179 2608 2152 1779 -312 -533 185 C ATOM 1463 CG LEU A 179 65.879 -22.388 11.080 1.00 17.58 C ANISOU 1463 CG LEU A 179 2680 2186 1815 -361 -574 198 C ATOM 1464 CD1 LEU A 179 65.244 -22.334 12.453 1.00 17.75 C ANISOU 1464 CD1 LEU A 179 2687 2233 1826 -414 -575 222 C ATOM 1465 CD2 LEU A 179 64.803 -22.486 10.012 1.00 17.75 C ANISOU 1465 CD2 LEU A 179 2698 2223 1822 -368 -580 192 C ATOM 1466 N THR A 180 69.263 -23.200 12.128 1.00 18.87 N ANISOU 1466 N THR A 180 2884 2249 2035 -297 -604 179 N ATOM 1467 CA THR A 180 70.117 -24.355 11.845 1.00 20.15 C ANISOU 1467 CA THR A 180 3081 2353 2224 -278 -648 160 C ATOM 1468 C THR A 180 69.349 -25.677 11.964 1.00 20.82 C ANISOU 1468 C THR A 180 3204 2407 2302 -322 -704 175 C ATOM 1469 O THR A 180 68.735 -25.947 12.995 1.00 21.41 O ANISOU 1469 O THR A 180 3288 2485 2360 -375 -725 209 O ATOM 1470 CB THR A 180 71.322 -24.390 12.801 1.00 20.77 C ANISOU 1470 CB THR A 180 3162 2400 2330 -262 -663 160 C ATOM 1471 OG1 THR A 180 72.039 -23.154 12.699 1.00 21.01 O ANISOU 1471 OG1 THR A 180 3157 2460 2366 -224 -610 146 O ATOM 1472 CG2 THR A 180 72.256 -25.567 12.475 1.00 21.43 C ANISOU 1472 CG2 THR A 180 3275 2418 2451 -235 -713 131 C ATOM 1473 N ALEU A 181 69.438 -26.487 10.909 0.50 21.32 N ANISOU 1473 N ALEU A 181 3288 2439 2375 -302 -727 148 N ATOM 1474 N BLEU A 181 69.368 -26.485 10.913 0.50 21.46 N ANISOU 1474 N BLEU A 181 3306 2458 2391 -304 -727 149 N ATOM 1475 CA ALEU A 181 68.760 -27.778 10.796 0.50 21.93 C ANISOU 1475 CA ALEU A 181 3403 2480 2447 -338 -782 157 C ATOM 1476 CA BLEU A 181 68.845 -27.845 10.992 0.50 22.19 C ANISOU 1476 CA BLEU A 181 3439 2508 2483 -341 -788 160 C ATOM 1477 C ALEU A 181 69.738 -28.772 10.180 0.50 22.52 C ANISOU 1477 C ALEU A 181 3503 2493 2560 -298 -822 118 C ATOM 1478 C BLEU A 181 69.714 -28.777 10.180 0.50 22.66 C ANISOU 1478 C BLEU A 181 3521 2511 2577 -299 -822 118 C ATOM 1479 O ALEU A 181 70.687 -28.369 9.515 0.50 22.19 O ANISOU 1479 O ALEU A 181 3443 2451 2538 -245 -794 77 O ATOM 1480 O BLEU A 181 70.557 -28.346 9.399 0.50 22.33 O ANISOU 1480 O BLEU A 181 3461 2473 2552 -246 -791 78 O ATOM 1481 CB ALEU A 181 67.535 -27.652 9.885 0.50 22.01 C ANISOU 1481 CB ALEU A 181 3407 2528 2428 -356 -764 158 C ATOM 1482 CB BLEU A 181 67.371 -27.940 10.564 0.50 22.47 C ANISOU 1482 CB BLEU A 181 3475 2579 2485 -383 -784 177 C ATOM 1483 CG ALEU A 181 66.454 -26.647 10.291 0.50 21.85 C ANISOU 1483 CG ALEU A 181 3352 2571 2377 -389 -725 185 C ATOM 1484 CG BLEU A 181 66.722 -26.880 9.676 0.50 22.30 C ANISOU 1484 CG BLEU A 181 3419 2614 2442 -368 -730 167 C ATOM 1485 CD1ALEU A 181 65.423 -26.537 9.176 0.50 21.89 C ANISOU 1485 CD1ALEU A 181 3350 2604 2362 -393 -714 177 C ATOM 1486 CD1BLEU A 181 67.697 -26.271 8.682 0.50 22.19 C ANISOU 1486 CD1BLEU A 181 3390 2601 2440 -306 -695 130 C ATOM 1487 CD2ALEU A 181 65.802 -27.056 11.602 0.50 22.15 C ANISOU 1487 CD2ALEU A 181 3401 2614 2401 -455 -751 222 C ATOM 1488 CD2BLEU A 181 65.518 -27.481 8.957 0.50 22.48 C ANISOU 1488 CD2BLEU A 181 3455 2643 2444 -399 -749 171 C ATOM 1489 N SER A 182 69.516 -30.069 10.400 1.00 23.34 N ANISOU 1489 N SER A 182 3649 2544 2675 -325 -889 126 N ATOM 1490 CA SER A 182 70.244 -31.095 9.663 1.00 24.53 C ANISOU 1490 CA SER A 182 3823 2635 2864 -288 -932 81 C ATOM 1491 C SER A 182 69.800 -31.064 8.207 1.00 25.45 C ANISOU 1491 C SER A 182 3932 2774 2963 -269 -902 48 C ATOM 1492 O SER A 182 68.688 -30.616 7.906 1.00 25.03 O ANISOU 1492 O SER A 182 3870 2769 2870 -300 -874 71 O ATOM 1493 CB SER A 182 69.974 -32.476 10.256 1.00 25.13 C ANISOU 1493 CB SER A 182 3949 2646 2953 -328 -1018 103 C ATOM 1494 OG SER A 182 68.597 -32.809 10.183 1.00 25.49 O ANISOU 1494 OG SER A 182 4012 2713 2959 -387 -1027 136 O ATOM 1495 N LYS A 183 70.673 -31.514 7.307 1.00 26.75 N ANISOU 1495 N LYS A 183 4097 2907 3158 -221 -909 -10 N ATOM 1496 CA LYS A 183 70.320 -31.647 5.897 1.00 27.69 C ANISOU 1496 CA LYS A 183 4218 3043 3261 -208 -887 -46 C ATOM 1497 C LYS A 183 69.071 -32.519 5.760 1.00 28.08 C ANISOU 1497 C LYS A 183 4301 3079 3288 -256 -931 -18 C ATOM 1498 O LYS A 183 68.164 -32.177 5.011 1.00 27.60 O ANISOU 1498 O LYS A 183 4236 3060 3191 -273 -903 -12 O ATOM 1499 CB LYS A 183 71.471 -32.253 5.087 1.00 28.87 C ANISOU 1499 CB LYS A 183 4367 3153 3451 -155 -898 -119 C ATOM 1500 CG LYS A 183 71.243 -32.255 3.580 1.00 29.58 C ANISOU 1500 CG LYS A 183 4455 3268 3517 -143 -866 -163 C ATOM 1501 CD LYS A 183 71.991 -33.370 2.870 1.00 30.78 C ANISOU 1501 CD LYS A 183 4619 3367 3710 -109 -901 -233 C ATOM 1502 CE LYS A 183 71.680 -33.359 1.383 1.00 31.38 C ANISOU 1502 CE LYS A 183 4697 3473 3753 -106 -867 -275 C ATOM 1503 NZ LYS A 183 72.496 -34.339 0.619 1.00 32.24 N ANISOU 1503 NZ LYS A 183 4809 3538 3901 -70 -891 -357 N ATOM 1504 N ALA A 184 69.031 -33.621 6.512 1.00 28.82 N ANISOU 1504 N ALA A 184 4431 3114 3406 -280 -1002 -1 N ATOM 1505 CA ALA A 184 67.884 -34.532 6.514 1.00 29.21 C ANISOU 1505 CA ALA A 184 4516 3145 3436 -334 -1050 28 C ATOM 1506 C ALA A 184 66.583 -33.806 6.859 1.00 28.85 C ANISOU 1506 C ALA A 184 4457 3165 3340 -387 -1016 80 C ATOM 1507 O ALA A 184 65.592 -33.967 6.154 1.00 29.38 O ANISOU 1507 O ALA A 184 4529 3254 3380 -410 -1012 83 O ATOM 1508 CB ALA A 184 68.116 -35.689 7.476 1.00 29.95 C ANISOU 1508 CB ALA A 184 4654 3166 3561 -359 -1135 48 C ATOM 1509 N ASP A 185 66.599 -33.004 7.927 1.00 28.14 N ANISOU 1509 N ASP A 185 4346 3107 3241 -405 -991 115 N ATOM 1510 CA ASP A 185 65.413 -32.226 8.324 1.00 27.69 C ANISOU 1510 CA ASP A 185 4265 3114 3141 -453 -955 155 C ATOM 1511 C ASP A 185 65.068 -31.135 7.298 1.00 26.25 C ANISOU 1511 C ASP A 185 4045 2991 2939 -424 -891 136 C ATOM 1512 O ASP A 185 63.890 -30.918 6.983 1.00 26.30 O ANISOU 1512 O ASP A 185 4041 3036 2917 -456 -879 151 O ATOM 1513 CB ASP A 185 65.585 -31.607 9.718 1.00 28.24 C ANISOU 1513 CB ASP A 185 4321 3204 3206 -478 -942 190 C ATOM 1514 CG ASP A 185 65.481 -32.634 10.847 1.00 29.57 C ANISOU 1514 CG ASP A 185 4532 3327 3376 -536 -1008 225 C ATOM 1515 OD1 ASP A 185 65.198 -33.822 10.576 1.00 31.35 O ANISOU 1515 OD1 ASP A 185 4799 3504 3607 -558 -1067 225 O ATOM 1516 OD2 ASP A 185 65.676 -32.241 12.016 1.00 30.36 O ANISOU 1516 OD2 ASP A 185 4627 3438 3469 -562 -1004 253 O ATOM 1517 N TYR A 186 66.091 -30.469 6.764 1.00 24.86 N ANISOU 1517 N TYR A 186 3849 2819 2778 -366 -854 103 N ATOM 1518 CA TYR A 186 65.893 -29.443 5.748 1.00 23.89 C ANISOU 1518 CA TYR A 186 3698 2745 2635 -341 -800 86 C ATOM 1519 C TYR A 186 65.206 -29.996 4.484 1.00 24.51 C ANISOU 1519 C TYR A 186 3795 2822 2696 -346 -813 67 C ATOM 1520 O TYR A 186 64.293 -29.373 3.939 1.00 23.67 O ANISOU 1520 O TYR A 186 3673 2758 2562 -360 -791 78 O ATOM 1521 CB TYR A 186 67.223 -28.779 5.387 1.00 22.97 C ANISOU 1521 CB TYR A 186 3563 2629 2535 -285 -762 50 C ATOM 1522 CG TYR A 186 67.099 -27.759 4.279 1.00 22.10 C ANISOU 1522 CG TYR A 186 3432 2565 2400 -265 -712 34 C ATOM 1523 CD1 TYR A 186 66.477 -26.531 4.503 1.00 21.45 C ANISOU 1523 CD1 TYR A 186 3320 2533 2296 -276 -676 63 C ATOM 1524 CD2 TYR A 186 67.594 -28.023 3.002 1.00 22.02 C ANISOU 1524 CD2 TYR A 186 3435 2546 2386 -238 -704 -11 C ATOM 1525 CE1 TYR A 186 66.351 -25.597 3.485 1.00 21.22 C ANISOU 1525 CE1 TYR A 186 3278 2539 2244 -261 -641 53 C ATOM 1526 CE2 TYR A 186 67.475 -27.092 1.980 1.00 21.65 C ANISOU 1526 CE2 TYR A 186 3376 2540 2309 -229 -662 -22 C ATOM 1527 CZ TYR A 186 66.856 -25.881 2.227 1.00 21.21 C ANISOU 1527 CZ TYR A 186 3296 2529 2235 -240 -634 13 C ATOM 1528 OH TYR A 186 66.736 -24.960 1.208 1.00 20.96 O ANISOU 1528 OH TYR A 186 3259 2531 2174 -233 -603 7 O ATOM 1529 N GLU A 187 65.639 -31.171 4.033 1.00 25.55 N ANISOU 1529 N GLU A 187 3960 2902 2847 -335 -854 38 N ATOM 1530 CA GLU A 187 65.062 -31.803 2.839 1.00 26.75 C ANISOU 1530 CA GLU A 187 4134 3047 2984 -341 -871 16 C ATOM 1531 C GLU A 187 63.645 -32.373 3.058 1.00 26.75 C ANISOU 1531 C GLU A 187 4150 3051 2964 -398 -906 53 C ATOM 1532 O GLU A 187 62.939 -32.657 2.088 1.00 27.07 O ANISOU 1532 O GLU A 187 4202 3099 2986 -409 -913 43 O ATOM 1533 CB GLU A 187 65.997 -32.900 2.300 1.00 28.20 C ANISOU 1533 CB GLU A 187 4345 3172 3199 -310 -904 -36 C ATOM 1534 CG GLU A 187 67.389 -32.439 1.858 1.00 29.05 C ANISOU 1534 CG GLU A 187 4433 3278 3326 -254 -867 -87 C ATOM 1535 CD GLU A 187 67.394 -31.416 0.731 1.00 29.70 C ANISOU 1535 CD GLU A 187 4496 3415 3373 -239 -807 -107 C ATOM 1536 OE1 GLU A 187 66.456 -31.405 -0.094 1.00 30.79 O ANISOU 1536 OE1 GLU A 187 4646 3576 3478 -261 -805 -100 O ATOM 1537 OE2 GLU A 187 68.358 -30.614 0.669 1.00 30.47 O ANISOU 1537 OE2 GLU A 187 4569 3532 3476 -207 -763 -129 O ATOM 1538 N LYS A 188 63.239 -32.533 4.318 1.00 26.55 N ANISOU 1538 N LYS A 188 4125 3023 2940 -439 -927 94 N ATOM 1539 CA LYS A 188 61.887 -32.992 4.681 1.00 26.96 C ANISOU 1539 CA LYS A 188 4186 3088 2971 -503 -954 129 C ATOM 1540 C LYS A 188 60.815 -31.897 4.737 1.00 25.97 C ANISOU 1540 C LYS A 188 4018 3032 2818 -526 -912 151 C ATOM 1541 O LYS A 188 59.638 -32.210 4.928 1.00 26.66 O ANISOU 1541 O LYS A 188 4105 3138 2888 -578 -930 173 O ATOM 1542 CB LYS A 188 61.927 -33.703 6.038 1.00 27.94 C ANISOU 1542 CB LYS A 188 4332 3179 3104 -547 -997 162 C ATOM 1543 CG LYS A 188 62.568 -35.077 5.983 1.00 29.20 C ANISOU 1543 CG LYS A 188 4543 3260 3292 -541 -1063 146 C ATOM 1544 CD LYS A 188 62.877 -35.596 7.371 1.00 29.77 C ANISOU 1544 CD LYS A 188 4640 3296 3376 -579 -1107 180 C ATOM 1545 CE LYS A 188 63.502 -36.980 7.309 1.00 30.79 C ANISOU 1545 CE LYS A 188 4820 3337 3540 -571 -1184 164 C ATOM 1546 NZ LYS A 188 63.750 -37.533 8.665 1.00 31.43 N ANISOU 1546 NZ LYS A 188 4935 3378 3630 -616 -1239 203 N ATOM 1547 N HIS A 189 61.205 -30.630 4.598 1.00 24.52 N ANISOU 1547 N HIS A 189 3798 2886 2633 -489 -861 144 N ATOM 1548 CA HIS A 189 60.252 -29.513 4.647 1.00 23.82 C ANISOU 1548 CA HIS A 189 3666 2858 2527 -503 -826 160 C ATOM 1549 C HIS A 189 60.403 -28.627 3.429 1.00 22.64 C ANISOU 1549 C HIS A 189 3502 2730 2370 -460 -795 138 C ATOM 1550 O HIS A 189 61.401 -28.699 2.715 1.00 22.49 O ANISOU 1550 O HIS A 189 3501 2688 2355 -420 -787 111 O ATOM 1551 CB HIS A 189 60.418 -28.715 5.946 1.00 24.06 C ANISOU 1551 CB HIS A 189 3663 2916 2563 -514 -799 180 C ATOM 1552 CG HIS A 189 60.237 -29.546 7.177 1.00 24.99 C ANISOU 1552 CG HIS A 189 3799 3016 2680 -567 -830 205 C ATOM 1553 ND1 HIS A 189 61.301 -30.080 7.872 1.00 25.71 N ANISOU 1553 ND1 HIS A 189 3918 3062 2787 -559 -851 209 N ATOM 1554 CD2 HIS A 189 59.122 -29.969 7.818 1.00 25.77 C ANISOU 1554 CD2 HIS A 189 3894 3134 2762 -633 -847 228 C ATOM 1555 CE1 HIS A 189 60.849 -30.779 8.898 1.00 26.04 C ANISOU 1555 CE1 HIS A 189 3978 3095 2820 -621 -883 237 C ATOM 1556 NE2 HIS A 189 59.530 -30.727 8.887 1.00 26.37 N ANISOU 1556 NE2 HIS A 189 4002 3179 2840 -669 -878 248 N ATOM 1557 N LYS A 190 59.390 -27.802 3.186 1.00 21.78 N ANISOU 1557 N LYS A 190 3361 2666 2249 -472 -780 148 N ATOM 1558 CA LYS A 190 59.298 -27.011 1.968 1.00 21.30 C ANISOU 1558 CA LYS A 190 3294 2623 2175 -444 -764 135 C ATOM 1559 C LYS A 190 59.382 -25.498 2.206 1.00 20.12 C ANISOU 1559 C LYS A 190 3103 2511 2030 -421 -726 142 C ATOM 1560 O LYS A 190 60.210 -24.828 1.595 1.00 19.71 O ANISOU 1560 O LYS A 190 3056 2459 1974 -385 -702 129 O ATOM 1561 CB LYS A 190 58.004 -27.366 1.221 1.00 22.09 C ANISOU 1561 CB LYS A 190 3398 2735 2261 -473 -793 138 C ATOM 1562 CG LYS A 190 57.751 -26.555 -0.036 1.00 22.61 C ANISOU 1562 CG LYS A 190 3461 2818 2311 -452 -786 129 C ATOM 1563 CD LYS A 190 56.582 -27.148 -0.815 1.00 23.46 C ANISOU 1563 CD LYS A 190 3582 2927 2406 -481 -823 130 C ATOM 1564 CE LYS A 190 55.674 -26.083 -1.381 1.00 24.16 C ANISOU 1564 CE LYS A 190 3640 3049 2491 -479 -825 137 C ATOM 1565 NZ LYS A 190 54.459 -26.713 -1.954 1.00 24.77 N ANISOU 1565 NZ LYS A 190 3723 3128 2560 -512 -865 139 N ATOM 1566 N VAL A 191 58.498 -24.970 3.053 1.00 19.36 N ANISOU 1566 N VAL A 191 2966 2448 1941 -446 -721 159 N ATOM 1567 CA VAL A 191 58.340 -23.522 3.216 1.00 18.73 C ANISOU 1567 CA VAL A 191 2843 2404 1870 -427 -693 162 C ATOM 1568 C VAL A 191 59.164 -23.019 4.403 1.00 18.03 C ANISOU 1568 C VAL A 191 2735 2321 1795 -416 -662 168 C ATOM 1569 O VAL A 191 58.920 -23.410 5.546 1.00 18.13 O ANISOU 1569 O VAL A 191 2735 2340 1812 -449 -663 178 O ATOM 1570 CB VAL A 191 56.860 -23.120 3.410 1.00 18.86 C ANISOU 1570 CB VAL A 191 2816 2458 1893 -456 -705 167 C ATOM 1571 CG1 VAL A 191 56.715 -21.602 3.405 1.00 18.70 C ANISOU 1571 CG1 VAL A 191 2752 2465 1887 -428 -684 166 C ATOM 1572 CG2 VAL A 191 55.979 -23.759 2.331 1.00 19.25 C ANISOU 1572 CG2 VAL A 191 2886 2500 1930 -472 -741 164 C ATOM 1573 N TYR A 192 60.131 -22.155 4.108 1.00 17.29 N ANISOU 1573 N TYR A 192 2640 2225 1703 -375 -635 161 N ATOM 1574 CA TYR A 192 61.012 -21.557 5.109 1.00 16.91 C ANISOU 1574 CA TYR A 192 2574 2181 1668 -359 -605 165 C ATOM 1575 C TYR A 192 60.709 -20.073 5.142 1.00 16.74 C ANISOU 1575 C TYR A 192 2512 2192 1656 -342 -583 167 C ATOM 1576 O TYR A 192 60.840 -19.392 4.125 1.00 16.74 O ANISOU 1576 O TYR A 192 2519 2193 1649 -317 -581 163 O ATOM 1577 CB TYR A 192 62.467 -21.842 4.743 1.00 16.77 C ANISOU 1577 CB TYR A 192 2590 2132 1651 -327 -594 151 C ATOM 1578 CG TYR A 192 62.777 -23.298 4.941 1.00 17.06 C ANISOU 1578 CG TYR A 192 2662 2131 1689 -342 -622 146 C ATOM 1579 CD1 TYR A 192 63.220 -23.760 6.173 1.00 17.10 C ANISOU 1579 CD1 TYR A 192 2669 2122 1708 -356 -627 156 C ATOM 1580 CD2 TYR A 192 62.553 -24.229 3.930 1.00 17.42 C ANISOU 1580 CD2 TYR A 192 2741 2154 1724 -347 -649 132 C ATOM 1581 CE1 TYR A 192 63.469 -25.100 6.384 1.00 17.44 C ANISOU 1581 CE1 TYR A 192 2746 2123 1756 -372 -664 154 C ATOM 1582 CE2 TYR A 192 62.802 -25.574 4.128 1.00 17.78 C ANISOU 1582 CE2 TYR A 192 2819 2160 1776 -361 -682 127 C ATOM 1583 CZ TYR A 192 63.255 -26.002 5.360 1.00 17.83 C ANISOU 1583 CZ TYR A 192 2828 2149 1799 -373 -691 138 C ATOM 1584 OH TYR A 192 63.505 -27.331 5.566 1.00 18.62 O ANISOU 1584 OH TYR A 192 2963 2201 1908 -387 -733 135 O ATOM 1585 N ALA A 193 60.282 -19.586 6.304 1.00 16.75 N ANISOU 1585 N ALA A 193 2472 2220 1671 -358 -570 173 N ATOM 1586 CA ALA A 193 59.771 -18.221 6.431 1.00 16.96 C ANISOU 1586 CA ALA A 193 2453 2278 1713 -344 -556 170 C ATOM 1587 C ALA A 193 60.336 -17.519 7.655 1.00 16.99 C ANISOU 1587 C ALA A 193 2428 2297 1731 -338 -525 171 C ATOM 1588 O ALA A 193 60.422 -18.107 8.728 1.00 17.11 O ANISOU 1588 O ALA A 193 2440 2316 1744 -367 -519 175 O ATOM 1589 CB ALA A 193 58.247 -18.248 6.519 1.00 17.19 C ANISOU 1589 CB ALA A 193 2446 2336 1751 -375 -576 165 C ATOM 1590 N ACYS A 194 60.781 -16.276 7.503 0.50 17.03 N ANISOU 1590 N ACYS A 194 2416 2308 1747 -303 -506 168 N ATOM 1591 N BCYS A 194 60.637 -16.238 7.469 0.50 16.63 N ANISOU 1591 N BCYS A 194 2361 2259 1697 -305 -509 168 N ATOM 1592 CA ACYS A 194 61.099 -15.461 8.671 0.50 17.13 C ANISOU 1592 CA ACYS A 194 2393 2341 1776 -299 -478 166 C ATOM 1593 CA BCYS A 194 61.139 -15.351 8.494 0.50 16.41 C ANISOU 1593 CA BCYS A 194 2303 2246 1684 -293 -479 166 C ATOM 1594 C ACYS A 194 60.173 -14.254 8.689 0.50 17.13 C ANISOU 1594 C ACYS A 194 2341 2367 1799 -290 -479 155 C ATOM 1595 C BCYS A 194 60.121 -14.225 8.648 0.50 16.73 C ANISOU 1595 C BCYS A 194 2289 2317 1749 -289 -481 154 C ATOM 1596 O ACYS A 194 60.026 -13.543 7.694 0.50 17.13 O ANISOU 1596 O ACYS A 194 2344 2359 1805 -264 -495 154 O ATOM 1597 O BCYS A 194 59.867 -13.514 7.679 0.50 16.72 O ANISOU 1597 O BCYS A 194 2288 2310 1755 -265 -498 153 O ATOM 1598 CB ACYS A 194 62.583 -15.090 8.746 0.50 17.10 C ANISOU 1598 CB ACYS A 194 2410 2316 1770 -267 -454 171 C ATOM 1599 CB BCYS A 194 62.474 -14.792 8.018 0.50 15.93 C ANISOU 1599 CB BCYS A 194 2268 2165 1620 -255 -461 170 C ATOM 1600 SG ACYS A 194 63.161 -13.922 7.514 0.50 17.37 S ANISOU 1600 SG ACYS A 194 2456 2340 1803 -224 -450 171 S ATOM 1601 SG BCYS A 194 63.221 -13.592 9.125 0.50 15.42 S ANISOU 1601 SG BCYS A 194 2170 2114 1574 -235 -426 169 S ATOM 1602 N GLU A 195 59.523 -14.074 9.832 1.00 17.14 N ANISOU 1602 N GLU A 195 2297 2402 1814 -316 -467 143 N ATOM 1603 CA GLU A 195 58.503 -13.058 10.051 1.00 17.83 C ANISOU 1603 CA GLU A 195 2324 2520 1932 -312 -469 120 C ATOM 1604 C GLU A 195 59.077 -12.020 11.004 1.00 17.27 C ANISOU 1604 C GLU A 195 2222 2462 1877 -295 -438 112 C ATOM 1605 O GLU A 195 59.554 -12.362 12.091 1.00 16.86 O ANISOU 1605 O GLU A 195 2171 2422 1814 -318 -412 114 O ATOM 1606 CB GLU A 195 57.255 -13.692 10.655 1.00 19.21 C ANISOU 1606 CB GLU A 195 2462 2728 2108 -361 -474 103 C ATOM 1607 CG GLU A 195 56.157 -12.715 11.034 1.00 20.50 C ANISOU 1607 CG GLU A 195 2552 2929 2308 -360 -473 68 C ATOM 1608 CD GLU A 195 55.292 -13.275 12.146 1.00 21.90 C ANISOU 1608 CD GLU A 195 2689 3153 2481 -419 -456 46 C ATOM 1609 OE1 GLU A 195 54.274 -13.893 11.806 1.00 23.99 O ANISOU 1609 OE1 GLU A 195 2940 3430 2744 -447 -477 36 O ATOM 1610 OE2 GLU A 195 55.667 -13.142 13.339 1.00 23.50 O ANISOU 1610 OE2 GLU A 195 2876 3378 2676 -441 -422 39 O ATOM 1611 N VAL A 196 58.976 -10.758 10.611 1.00 16.94 N ANISOU 1611 N VAL A 196 2155 2418 1862 -258 -445 102 N ATOM 1612 CA VAL A 196 59.631 -9.662 11.300 1.00 16.87 C ANISOU 1612 CA VAL A 196 2124 2415 1871 -234 -420 96 C ATOM 1613 C VAL A 196 58.599 -8.661 11.801 1.00 17.30 C ANISOU 1613 C VAL A 196 2108 2499 1967 -229 -423 60 C ATOM 1614 O VAL A 196 57.769 -8.188 11.023 1.00 17.64 O ANISOU 1614 O VAL A 196 2131 2537 2035 -213 -458 48 O ATOM 1615 CB VAL A 196 60.653 -8.968 10.369 1.00 16.50 C ANISOU 1615 CB VAL A 196 2117 2333 1821 -192 -426 116 C ATOM 1616 CG1 VAL A 196 61.220 -7.714 11.030 1.00 16.35 C ANISOU 1616 CG1 VAL A 196 2071 2317 1823 -167 -405 109 C ATOM 1617 CG2 VAL A 196 61.779 -9.938 10.012 1.00 16.23 C ANISOU 1617 CG2 VAL A 196 2143 2274 1750 -196 -415 140 C ATOM 1618 N THR A 197 58.686 -8.335 13.094 1.00 17.86 N ANISOU 1618 N THR A 197 2140 2599 2045 -244 -389 40 N ATOM 1619 CA THR A 197 57.852 -7.305 13.719 1.00 18.60 C ANISOU 1619 CA THR A 197 2161 2725 2182 -238 -385 -3 C ATOM 1620 C THR A 197 58.745 -6.172 14.187 1.00 18.24 C ANISOU 1620 C THR A 197 2109 2670 2152 -205 -366 -4 C ATOM 1621 O THR A 197 59.744 -6.400 14.859 1.00 18.21 O ANISOU 1621 O THR A 197 2131 2665 2123 -215 -335 13 O ATOM 1622 CB THR A 197 57.069 -7.868 14.921 1.00 19.25 C ANISOU 1622 CB THR A 197 2197 2859 2257 -293 -357 -35 C ATOM 1623 OG1 THR A 197 56.353 -9.041 14.509 1.00 20.01 O ANISOU 1623 OG1 THR A 197 2309 2962 2333 -330 -374 -28 O ATOM 1624 CG2 THR A 197 56.068 -6.835 15.466 1.00 19.96 C ANISOU 1624 CG2 THR A 197 2202 2986 2397 -287 -354 -92 C ATOM 1625 N HIS A 198 58.370 -4.951 13.834 1.00 18.25 N ANISOU 1625 N HIS A 198 2075 2661 2197 -166 -390 -25 N ATOM 1626 CA HIS A 198 59.156 -3.770 14.166 1.00 18.24 C ANISOU 1626 CA HIS A 198 2068 2647 2216 -132 -379 -27 C ATOM 1627 C HIS A 198 58.245 -2.554 14.070 1.00 19.19 C ANISOU 1627 C HIS A 198 2126 2768 2396 -102 -410 -69 C ATOM 1628 O HIS A 198 57.334 -2.519 13.250 1.00 19.28 O ANISOU 1628 O HIS A 198 2124 2769 2431 -92 -454 -78 O ATOM 1629 CB HIS A 198 60.352 -3.660 13.212 1.00 17.59 C ANISOU 1629 CB HIS A 198 2055 2518 2109 -106 -390 21 C ATOM 1630 CG HIS A 198 61.208 -2.459 13.453 1.00 17.17 C ANISOU 1630 CG HIS A 198 2002 2449 2073 -74 -382 24 C ATOM 1631 ND1 HIS A 198 62.251 -2.434 14.352 1.00 17.10 N ANISOU 1631 ND1 HIS A 198 2003 2447 2046 -80 -340 32 N ATOM 1632 CD2 HIS A 198 61.152 -1.227 12.903 1.00 17.17 C ANISOU 1632 CD2 HIS A 198 1995 2422 2108 -38 -415 20 C ATOM 1633 CE1 HIS A 198 62.796 -1.229 14.339 1.00 16.61 C ANISOU 1633 CE1 HIS A 198 1937 2366 2006 -48 -344 32 C ATOM 1634 NE2 HIS A 198 62.140 -0.477 13.477 1.00 17.35 N ANISOU 1634 NE2 HIS A 198 2021 2438 2132 -23 -390 26 N ATOM 1635 N GLN A 199 58.481 -1.553 14.904 1.00 20.19 N ANISOU 1635 N GLN A 199 2215 2905 2552 -85 -392 -96 N ATOM 1636 CA GLN A 199 57.535 -0.429 14.977 1.00 21.60 C ANISOU 1636 CA GLN A 199 2324 3087 2797 -56 -422 -147 C ATOM 1637 C GLN A 199 57.452 0.434 13.701 1.00 21.47 C ANISOU 1637 C GLN A 199 2330 3016 2814 -10 -488 -130 C ATOM 1638 O GLN A 199 56.475 1.118 13.487 1.00 22.30 O ANISOU 1638 O GLN A 199 2383 3114 2975 13 -531 -169 O ATOM 1639 CB GLN A 199 57.764 0.410 16.232 1.00 23.18 C ANISOU 1639 CB GLN A 199 2474 3312 3021 -52 -386 -187 C ATOM 1640 CG GLN A 199 59.074 1.140 16.314 1.00 24.02 C ANISOU 1640 CG GLN A 199 2622 3387 3117 -26 -376 -155 C ATOM 1641 CD GLN A 199 59.422 1.462 17.753 1.00 25.20 C ANISOU 1641 CD GLN A 199 2734 3574 3266 -42 -324 -187 C ATOM 1642 OE1 GLN A 199 59.876 0.593 18.518 1.00 26.30 O ANISOU 1642 OE1 GLN A 199 2891 3743 3358 -84 -278 -173 O ATOM 1643 NE2 GLN A 199 59.187 2.704 18.144 1.00 26.54 N ANISOU 1643 NE2 GLN A 199 2852 3741 3489 -11 -334 -230 N ATOM 1644 N GLY A 200 58.487 0.395 12.873 1.00 20.54 N ANISOU 1644 N GLY A 200 2288 2858 2660 0 -498 -73 N ATOM 1645 CA GLY A 200 58.448 0.935 11.506 1.00 20.62 C ANISOU 1645 CA GLY A 200 2337 2816 2680 27 -561 -44 C ATOM 1646 C GLY A 200 57.572 0.235 10.475 1.00 20.75 C ANISOU 1646 C GLY A 200 2368 2824 2691 17 -604 -35 C ATOM 1647 O GLY A 200 57.340 0.789 9.391 1.00 20.92 O ANISOU 1647 O GLY A 200 2416 2805 2729 37 -665 -18 O ATOM 1648 N LEU A 201 57.103 -0.975 10.781 1.00 20.52 N ANISOU 1648 N LEU A 201 2328 2832 2638 -18 -576 -44 N ATOM 1649 CA LEU A 201 56.214 -1.738 9.902 1.00 21.00 C ANISOU 1649 CA LEU A 201 2398 2889 2693 -32 -613 -40 C ATOM 1650 C LEU A 201 54.791 -1.691 10.443 1.00 22.09 C ANISOU 1650 C LEU A 201 2450 3062 2884 -37 -625 -100 C ATOM 1651 O LEU A 201 54.569 -1.942 11.628 1.00 22.45 O ANISOU 1651 O LEU A 201 2444 3153 2932 -60 -577 -137 O ATOM 1652 CB LEU A 201 56.667 -3.194 9.837 1.00 20.29 C ANISOU 1652 CB LEU A 201 2356 2814 2539 -70 -576 -10 C ATOM 1653 CG LEU A 201 58.090 -3.450 9.348 1.00 19.66 C ANISOU 1653 CG LEU A 201 2355 2707 2407 -69 -556 40 C ATOM 1654 CD1 LEU A 201 58.507 -4.879 9.661 1.00 19.30 C ANISOU 1654 CD1 LEU A 201 2340 2680 2312 -105 -515 56 C ATOM 1655 CD2 LEU A 201 58.189 -3.145 7.865 1.00 19.83 C ANISOU 1655 CD2 LEU A 201 2431 2686 2418 -54 -607 72 C ATOM 1656 N SER A 202 53.826 -1.395 9.578 1.00 23.11 N ANISOU 1656 N SER A 202 2561 3168 3050 -20 -691 -112 N ATOM 1657 CA SER A 202 52.434 -1.292 10.023 1.00 24.27 C ANISOU 1657 CA SER A 202 2618 3347 3255 -21 -707 -178 C ATOM 1658 C SER A 202 51.871 -2.655 10.425 1.00 24.57 C ANISOU 1658 C SER A 202 2642 3435 3260 -72 -669 -190 C ATOM 1659 O SER A 202 50.978 -2.727 11.274 1.00 25.62 O ANISOU 1659 O SER A 202 2695 3615 3424 -91 -648 -249 O ATOM 1660 CB SER A 202 51.559 -0.623 8.962 1.00 25.20 C ANISOU 1660 CB SER A 202 2723 3423 3428 13 -796 -187 C ATOM 1661 OG SER A 202 51.522 -1.379 7.778 1.00 25.84 O ANISOU 1661 OG SER A 202 2869 3479 3469 -2 -829 -140 O ATOM 1662 N SER A 203 52.380 -3.721 9.809 1.00 24.23 N ANISOU 1662 N SER A 203 2672 3379 3154 -98 -660 -137 N ATOM 1663 CA SER A 203 52.122 -5.095 10.260 1.00 24.13 C ANISOU 1663 CA SER A 203 2662 3408 3099 -151 -620 -137 C ATOM 1664 C SER A 203 53.357 -5.960 9.999 1.00 23.32 C ANISOU 1664 C SER A 203 2648 3286 2926 -167 -592 -77 C ATOM 1665 O SER A 203 54.249 -5.544 9.252 1.00 23.02 O ANISOU 1665 O SER A 203 2667 3205 2873 -139 -608 -38 O ATOM 1666 CB SER A 203 50.887 -5.680 9.564 1.00 24.89 C ANISOU 1666 CB SER A 203 2737 3509 3210 -166 -663 -152 C ATOM 1667 OG SER A 203 51.070 -5.812 8.162 1.00 25.27 O ANISOU 1667 OG SER A 203 2851 3508 3241 -148 -715 -107 O ATOM 1668 N PRO A 204 53.420 -7.163 10.600 1.00 22.70 N ANISOU 1668 N PRO A 204 2582 3237 2806 -215 -552 -71 N ATOM 1669 CA PRO A 204 54.652 -7.935 10.417 1.00 21.88 C ANISOU 1669 CA PRO A 204 2557 3111 2645 -225 -529 -21 C ATOM 1670 C PRO A 204 54.929 -8.313 8.958 1.00 21.25 C ANISOU 1670 C PRO A 204 2545 2988 2542 -211 -568 18 C ATOM 1671 O PRO A 204 53.995 -8.543 8.183 1.00 21.91 O ANISOU 1671 O PRO A 204 2621 3066 2637 -214 -609 12 O ATOM 1672 CB PRO A 204 54.427 -9.177 11.283 1.00 22.12 C ANISOU 1672 CB PRO A 204 2584 3177 2642 -283 -495 -25 C ATOM 1673 CG PRO A 204 53.424 -8.748 12.299 1.00 22.66 C ANISOU 1673 CG PRO A 204 2568 3297 2746 -303 -478 -80 C ATOM 1674 CD PRO A 204 52.513 -7.810 11.570 1.00 23.06 C ANISOU 1674 CD PRO A 204 2571 3337 2852 -265 -524 -110 C ATOM 1675 N VAL A 205 56.206 -8.340 8.588 1.00 20.33 N ANISOU 1675 N VAL A 205 2490 2841 2392 -196 -555 54 N ATOM 1676 CA VAL A 205 56.632 -8.668 7.228 1.00 20.04 C ANISOU 1676 CA VAL A 205 2520 2768 2326 -186 -583 87 C ATOM 1677 C VAL A 205 57.174 -10.092 7.245 1.00 19.38 C ANISOU 1677 C VAL A 205 2484 2684 2197 -216 -560 106 C ATOM 1678 O VAL A 205 57.992 -10.437 8.111 1.00 18.86 O ANISOU 1678 O VAL A 205 2426 2625 2115 -226 -520 111 O ATOM 1679 CB VAL A 205 57.733 -7.706 6.728 1.00 20.02 C ANISOU 1679 CB VAL A 205 2554 2735 2317 -153 -583 110 C ATOM 1680 CG1 VAL A 205 58.378 -8.205 5.434 1.00 20.10 C ANISOU 1680 CG1 VAL A 205 2639 2716 2284 -155 -598 141 C ATOM 1681 CG2 VAL A 205 57.178 -6.301 6.527 1.00 20.35 C ANISOU 1681 CG2 VAL A 205 2560 2767 2406 -123 -621 96 C ATOM 1682 N THR A 206 56.719 -10.914 6.303 1.00 19.32 N ANISOU 1682 N THR A 206 2507 2664 2169 -230 -589 116 N ATOM 1683 CA THR A 206 57.238 -12.263 6.143 1.00 19.14 C ANISOU 1683 CA THR A 206 2534 2631 2106 -254 -576 131 C ATOM 1684 C THR A 206 57.979 -12.389 4.814 1.00 18.68 C ANISOU 1684 C THR A 206 2541 2540 2019 -239 -591 153 C ATOM 1685 O THR A 206 57.450 -12.018 3.768 1.00 19.08 O ANISOU 1685 O THR A 206 2602 2578 2070 -231 -629 157 O ATOM 1686 CB THR A 206 56.117 -13.322 6.234 1.00 19.61 C ANISOU 1686 CB THR A 206 2579 2708 2163 -293 -593 121 C ATOM 1687 OG1 THR A 206 55.488 -13.232 7.517 1.00 20.29 O ANISOU 1687 OG1 THR A 206 2606 2832 2271 -317 -572 98 O ATOM 1688 CG2 THR A 206 56.682 -14.743 6.058 1.00 19.81 C ANISOU 1688 CG2 THR A 206 2660 2716 2150 -316 -587 138 C ATOM 1689 N LYS A 207 59.209 -12.892 4.866 1.00 18.15 N ANISOU 1689 N LYS A 207 2515 2459 1924 -236 -563 163 N ATOM 1690 CA LYS A 207 59.958 -13.294 3.683 1.00 18.06 C ANISOU 1690 CA LYS A 207 2562 2422 1878 -230 -568 174 C ATOM 1691 C LYS A 207 60.134 -14.798 3.737 1.00 17.92 C ANISOU 1691 C LYS A 207 2573 2395 1840 -253 -564 172 C ATOM 1692 O LYS A 207 60.458 -15.354 4.786 1.00 17.28 O ANISOU 1692 O LYS A 207 2483 2320 1765 -264 -543 169 O ATOM 1693 CB LYS A 207 61.316 -12.602 3.606 1.00 18.23 C ANISOU 1693 CB LYS A 207 2604 2432 1889 -207 -539 180 C ATOM 1694 CG LYS A 207 61.238 -11.091 3.471 1.00 18.60 C ANISOU 1694 CG LYS A 207 2633 2481 1955 -186 -548 186 C ATOM 1695 CD LYS A 207 60.654 -10.640 2.136 1.00 19.50 C ANISOU 1695 CD LYS A 207 2771 2582 2058 -187 -592 195 C ATOM 1696 CE LYS A 207 60.444 -9.132 2.119 1.00 20.08 C ANISOU 1696 CE LYS A 207 2822 2650 2157 -167 -613 201 C ATOM 1697 NZ LYS A 207 59.828 -8.671 0.849 1.00 21.20 N ANISOU 1697 NZ LYS A 207 2991 2773 2290 -171 -667 214 N ATOM 1698 N SER A 208 59.906 -15.460 2.609 1.00 18.02 N ANISOU 1698 N SER A 208 2624 2394 1830 -262 -589 173 N ATOM 1699 CA SER A 208 59.956 -16.903 2.577 1.00 18.35 C ANISOU 1699 CA SER A 208 2692 2423 1855 -283 -594 168 C ATOM 1700 C SER A 208 60.488 -17.426 1.266 1.00 18.23 C ANISOU 1700 C SER A 208 2731 2387 1808 -280 -602 164 C ATOM 1701 O SER A 208 60.504 -16.710 0.249 1.00 18.36 O ANISOU 1701 O SER A 208 2765 2402 1809 -272 -612 167 O ATOM 1702 CB SER A 208 58.564 -17.466 2.822 1.00 19.02 C ANISOU 1702 CB SER A 208 2754 2523 1951 -313 -622 167 C ATOM 1703 OG SER A 208 57.745 -17.190 1.718 1.00 20.17 O ANISOU 1703 OG SER A 208 2906 2667 2092 -314 -656 168 O ATOM 1704 N PHE A 209 60.904 -18.683 1.286 1.00 18.08 N ANISOU 1704 N PHE A 209 2740 2351 1779 -290 -601 154 N ATOM 1705 CA PHE A 209 61.158 -19.428 0.055 1.00 18.40 C ANISOU 1705 CA PHE A 209 2827 2373 1790 -294 -614 142 C ATOM 1706 C PHE A 209 60.658 -20.859 0.201 1.00 18.90 C ANISOU 1706 C PHE A 209 2905 2421 1854 -318 -638 136 C ATOM 1707 O PHE A 209 60.471 -21.372 1.316 1.00 18.67 O ANISOU 1707 O PHE A 209 2859 2392 1845 -332 -639 142 O ATOM 1708 CB PHE A 209 62.643 -19.413 -0.315 1.00 18.22 C ANISOU 1708 CB PHE A 209 2831 2338 1754 -273 -583 124 C ATOM 1709 CG PHE A 209 63.522 -20.169 0.649 1.00 18.01 C ANISOU 1709 CG PHE A 209 2802 2295 1746 -264 -566 112 C ATOM 1710 CD1 PHE A 209 64.085 -19.529 1.751 1.00 17.75 C ANISOU 1710 CD1 PHE A 209 2740 2269 1734 -250 -541 120 C ATOM 1711 CD2 PHE A 209 63.799 -21.517 0.448 1.00 18.19 C ANISOU 1711 CD2 PHE A 209 2852 2291 1767 -271 -581 93 C ATOM 1712 CE1 PHE A 209 64.893 -20.227 2.636 1.00 17.73 C ANISOU 1712 CE1 PHE A 209 2739 2249 1751 -244 -533 112 C ATOM 1713 CE2 PHE A 209 64.606 -22.218 1.329 1.00 18.20 C ANISOU 1713 CE2 PHE A 209 2855 2271 1791 -262 -576 83 C ATOM 1714 CZ PHE A 209 65.161 -21.569 2.424 1.00 17.88 C ANISOU 1714 CZ PHE A 209 2787 2238 1770 -249 -553 94 C ATOM 1715 N ASN A 210 60.417 -21.493 -0.945 1.00 19.63 N ANISOU 1715 N ASN A 210 3033 2502 1923 -328 -660 126 N ATOM 1716 CA ASN A 210 60.110 -22.911 -1.002 1.00 20.48 C ANISOU 1716 CA ASN A 210 3164 2589 2029 -348 -685 117 C ATOM 1717 C ASN A 210 61.345 -23.667 -1.468 1.00 20.73 C ANISOU 1717 C ASN A 210 3233 2593 2051 -333 -673 88 C ATOM 1718 O ASN A 210 61.860 -23.404 -2.556 1.00 20.63 O ANISOU 1718 O ASN A 210 3244 2582 2013 -323 -661 71 O ATOM 1719 CB ASN A 210 58.986 -23.165 -2.004 1.00 21.21 C ANISOU 1719 CB ASN A 210 3271 2685 2104 -370 -721 120 C ATOM 1720 CG ASN A 210 57.645 -22.569 -1.593 1.00 21.74 C ANISOU 1720 CG ASN A 210 3296 2777 2187 -387 -741 140 C ATOM 1721 OD1 ASN A 210 56.706 -22.580 -2.398 1.00 23.77 O ANISOU 1721 OD1 ASN A 210 3558 3038 2434 -401 -772 143 O ATOM 1722 ND2 ASN A 210 57.530 -22.066 -0.373 1.00 21.57 N ANISOU 1722 ND2 ASN A 210 3231 2772 2192 -386 -724 150 N ATOM 1723 N ARG A 211 61.824 -24.603 -0.651 1.00 21.21 N ANISOU 1723 N ARG A 211 3297 2629 2131 -333 -677 81 N ATOM 1724 CA ARG A 211 62.961 -25.432 -1.028 1.00 21.97 C ANISOU 1724 CA ARG A 211 3423 2694 2229 -315 -673 46 C ATOM 1725 C ARG A 211 62.663 -26.169 -2.338 1.00 22.84 C ANISOU 1725 C ARG A 211 3569 2794 2315 -325 -693 23 C ATOM 1726 O ARG A 211 61.583 -26.730 -2.500 1.00 23.08 O ANISOU 1726 O ARG A 211 3609 2822 2340 -352 -727 36 O ATOM 1727 CB ARG A 211 63.275 -26.448 0.073 1.00 22.18 C ANISOU 1727 CB ARG A 211 3452 2688 2285 -319 -693 46 C ATOM 1728 CG ARG A 211 64.503 -27.316 -0.212 1.00 22.66 C ANISOU 1728 CG ARG A 211 3538 2712 2361 -294 -695 4 C ATOM 1729 CD ARG A 211 64.605 -28.544 0.691 1.00 23.07 C ANISOU 1729 CD ARG A 211 3604 2719 2442 -305 -736 6 C ATOM 1730 NE ARG A 211 63.324 -29.239 0.842 1.00 23.49 N ANISOU 1730 NE ARG A 211 3671 2768 2487 -347 -776 33 N ATOM 1731 CZ ARG A 211 62.691 -29.917 -0.117 1.00 24.19 C ANISOU 1731 CZ ARG A 211 3784 2848 2560 -362 -800 20 C ATOM 1732 NH1 ARG A 211 63.206 -30.046 -1.339 1.00 24.67 N ANISOU 1732 NH1 ARG A 211 3863 2904 2608 -340 -790 -20 N ATOM 1733 NH2 ARG A 211 61.513 -30.472 0.154 1.00 24.54 N ANISOU 1733 NH2 ARG A 211 3835 2890 2597 -404 -835 47 N ATOM 1734 N GLY A 212 63.620 -26.145 -3.260 1.00 23.64 N ANISOU 1734 N GLY A 212 3690 2892 2400 -307 -671 -15 N ATOM 1735 CA GLY A 212 63.511 -26.878 -4.523 1.00 24.71 C ANISOU 1735 CA GLY A 212 3862 3019 2510 -317 -685 -46 C ATOM 1736 C GLY A 212 62.779 -26.149 -5.638 1.00 25.60 C ANISOU 1736 C GLY A 212 3988 3161 2580 -336 -687 -33 C ATOM 1737 O GLY A 212 62.574 -26.725 -6.710 1.00 25.74 O ANISOU 1737 O GLY A 212 4037 3173 2571 -351 -701 -56 O ATOM 1738 N GLU A 213 62.390 -24.894 -5.406 1.00 26.34 N ANISOU 1738 N GLU A 213 4058 3281 2669 -338 -676 2 N ATOM 1739 CA GLU A 213 61.639 -24.106 -6.396 1.00 27.79 C ANISOU 1739 CA GLU A 213 4255 3487 2818 -356 -689 20 C ATOM 1740 C GLU A 213 62.464 -22.949 -6.925 1.00 29.87 C ANISOU 1740 C GLU A 213 4523 3771 3054 -349 -653 17 C ATOM 1741 O GLU A 213 63.298 -22.399 -6.207 1.00 30.60 O ANISOU 1741 O GLU A 213 4593 3868 3165 -327 -621 16 O ATOM 1742 CB GLU A 213 60.348 -23.558 -5.790 1.00 27.05 C ANISOU 1742 CB GLU A 213 4130 3405 2744 -367 -717 62 C ATOM 1743 CG GLU A 213 59.341 -24.641 -5.432 1.00 26.78 C ANISOU 1743 CG GLU A 213 4093 3357 2726 -387 -755 68 C ATOM 1744 CD GLU A 213 57.975 -24.107 -5.029 1.00 26.45 C ANISOU 1744 CD GLU A 213 4017 3333 2701 -402 -783 100 C ATOM 1745 OE1 GLU A 213 57.178 -24.916 -4.519 1.00 26.59 O ANISOU 1745 OE1 GLU A 213 4024 3345 2734 -423 -807 106 O ATOM 1746 OE2 GLU A 213 57.704 -22.897 -5.204 1.00 26.52 O ANISOU 1746 OE2 GLU A 213 4008 3360 2708 -396 -782 117 O ATOM 1747 N CYS A 214 62.209 -22.577 -8.178 1.00 32.91 N ANISOU 1747 N CYS A 214 4942 4168 3395 -371 -663 16 N ATOM 1748 CA CYS A 214 62.831 -21.395 -8.780 1.00 35.17 C ANISOU 1748 CA CYS A 214 5240 4476 3648 -376 -638 21 C ATOM 1749 C CYS A 214 62.135 -20.126 -8.281 1.00 35.92 C ANISOU 1749 C CYS A 214 5309 4579 3760 -371 -656 68 C ATOM 1750 O CYS A 214 60.957 -20.131 -7.905 1.00 36.69 O ANISOU 1750 O CYS A 214 5386 4672 3882 -374 -695 94 O ATOM 1751 CB CYS A 214 62.793 -21.487 -10.307 1.00 37.25 C ANISOU 1751 CB CYS A 214 5555 4748 3851 -409 -646 5 C ATOM 1752 SG CYS A 214 63.508 -23.034 -10.929 1.00 39.78 S ANISOU 1752 SG CYS A 214 5901 5057 4155 -414 -627 -61 S ATOM 1753 OXT CYS A 214 62.739 -19.057 -8.218 1.00 36.65 O ANISOU 1753 OXT CYS A 214 5397 4684 3845 -365 -633 78 O TER 1754 CYS A 214 ATOM 1755 N ATHR C 204 128.046 21.687 21.906 0.50 16.99 N ANISOU 1755 N ATHR C 204 2062 2777 1615 -433 545 -492 N ATOM 1756 N BTHR C 204 127.816 21.256 21.718 0.50 16.92 N ANISOU 1756 N BTHR C 204 2060 2766 1604 -439 560 -516 N ATOM 1757 CA ATHR C 204 126.987 21.202 22.832 0.50 16.29 C ANISOU 1757 CA ATHR C 204 1985 2638 1568 -359 477 -451 C ATOM 1758 CA BTHR C 204 126.899 21.004 22.853 0.50 16.15 C ANISOU 1758 CA BTHR C 204 1965 2613 1556 -354 480 -458 C ATOM 1759 C ATHR C 204 127.610 20.520 24.065 0.50 16.15 C ANISOU 1759 C ATHR C 204 1892 2563 1682 -261 477 -451 C ATOM 1760 C BTHR C 204 127.685 20.613 24.093 0.50 16.04 C ANISOU 1760 C BTHR C 204 1875 2551 1667 -261 475 -448 C ATOM 1761 O ATHR C 204 128.585 19.775 23.942 0.50 16.77 O ANISOU 1761 O ATHR C 204 1904 2622 1844 -243 554 -506 O ATOM 1762 O BTHR C 204 128.849 20.200 24.007 0.50 16.54 O ANISOU 1762 O BTHR C 204 1871 2610 1804 -250 543 -492 O ATOM 1763 CB ATHR C 204 126.018 20.255 22.082 0.50 16.60 C ANISOU 1763 CB ATHR C 204 2062 2687 1559 -403 501 -501 C ATOM 1764 CB BTHR C 204 125.896 19.873 22.540 0.50 16.25 C ANISOU 1764 CB BTHR C 204 2003 2608 1561 -362 494 -501 C ATOM 1765 OG1ATHR C 204 125.384 20.970 21.011 0.50 16.94 O ANISOU 1765 OG1ATHR C 204 2159 2817 1460 -504 477 -467 O ATOM 1766 OG1BTHR C 204 126.607 18.676 22.200 0.50 16.95 O ANISOU 1766 OG1BTHR C 204 2049 2660 1732 -363 604 -609 O ATOM 1767 CG2ATHR C 204 124.943 19.696 22.989 0.50 15.96 C ANISOU 1767 CG2ATHR C 204 1987 2552 1525 -333 439 -462 C ATOM 1768 CG2BTHR C 204 124.967 20.265 21.393 0.50 16.65 C ANISOU 1768 CG2BTHR C 204 2118 2743 1467 -468 473 -488 C ATOM 1769 N VAL C 205 127.054 20.798 25.245 1.00 15.46 N ANISOU 1769 N VAL C 205 1805 2455 1615 -202 395 -380 N ATOM 1770 CA VAL C 205 127.555 20.263 26.519 1.00 15.81 C ANISOU 1770 CA VAL C 205 1772 2479 1756 -122 372 -347 C ATOM 1771 C VAL C 205 126.351 19.624 27.193 1.00 15.83 C ANISOU 1771 C VAL C 205 1798 2442 1773 -73 325 -310 C ATOM 1772 O VAL C 205 125.344 20.297 27.410 1.00 14.80 O ANISOU 1772 O VAL C 205 1728 2317 1578 -85 269 -276 O ATOM 1773 CB VAL C 205 128.176 21.344 27.416 1.00 15.69 C ANISOU 1773 CB VAL C 205 1729 2507 1725 -128 321 -305 C ATOM 1774 CG1 VAL C 205 128.879 20.698 28.608 1.00 16.07 C ANISOU 1774 CG1 VAL C 205 1675 2575 1855 -67 296 -261 C ATOM 1775 CG2 VAL C 205 129.170 22.187 26.644 1.00 16.09 C ANISOU 1775 CG2 VAL C 205 1773 2593 1747 -193 365 -340 C ATOM 1776 N PRO C 206 126.430 18.318 27.494 1.00 17.13 N ANISOU 1776 N PRO C 206 1911 2559 2038 -17 359 -312 N ATOM 1777 CA PRO C 206 125.274 17.614 28.038 1.00 17.24 C ANISOU 1777 CA PRO C 206 1948 2531 2072 22 326 -279 C ATOM 1778 C PRO C 206 125.036 17.983 29.494 1.00 16.95 C ANISOU 1778 C PRO C 206 1889 2525 2028 66 242 -190 C ATOM 1779 O PRO C 206 126.000 18.199 30.239 1.00 17.66 O ANISOU 1779 O PRO C 206 1909 2660 2143 85 221 -149 O ATOM 1780 CB PRO C 206 125.687 16.146 27.932 1.00 18.19 C ANISOU 1780 CB PRO C 206 2003 2576 2331 68 409 -303 C ATOM 1781 CG PRO C 206 127.165 16.184 28.122 1.00 18.77 C ANISOU 1781 CG PRO C 206 1981 2667 2483 96 442 -285 C ATOM 1782 CD PRO C 206 127.621 17.441 27.433 1.00 18.35 C ANISOU 1782 CD PRO C 206 1969 2685 2318 21 436 -330 C ATOM 1783 N PRO C 207 123.762 18.063 29.911 1.00 16.74 N ANISOU 1783 N PRO C 207 1915 2487 1958 72 194 -162 N ATOM 1784 CA PRO C 207 123.511 18.364 31.312 1.00 16.78 C ANISOU 1784 CA PRO C 207 1900 2528 1946 99 130 -94 C ATOM 1785 C PRO C 207 123.916 17.247 32.251 1.00 17.78 C ANISOU 1785 C PRO C 207 1941 2654 2159 160 123 -21 C ATOM 1786 O PRO C 207 123.798 16.071 31.908 1.00 18.19 O ANISOU 1786 O PRO C 207 1970 2635 2307 198 170 -19 O ATOM 1787 CB PRO C 207 121.995 18.581 31.379 1.00 16.22 C ANISOU 1787 CB PRO C 207 1901 2435 1828 93 102 -87 C ATOM 1788 CG PRO C 207 121.449 17.979 30.154 1.00 16.48 C ANISOU 1788 CG PRO C 207 1969 2422 1871 73 141 -133 C ATOM 1789 CD PRO C 207 122.523 17.936 29.128 1.00 16.61 C ANISOU 1789 CD PRO C 207 1970 2443 1899 41 199 -192 C ATOM 1790 N MET C 208 124.396 17.641 33.424 1.00 18.56 N ANISOU 1790 N MET C 208 1989 2837 2227 159 70 40 N ATOM 1791 CA MET C 208 124.510 16.752 34.573 1.00 20.15 C ANISOU 1791 CA MET C 208 2108 3071 2477 207 36 150 C ATOM 1792 C MET C 208 123.183 16.826 35.312 1.00 19.50 C ANISOU 1792 C MET C 208 2084 2995 2331 201 -1 170 C ATOM 1793 O MET C 208 122.780 17.904 35.743 1.00 19.21 O ANISOU 1793 O MET C 208 2097 3010 2191 149 -28 134 O ATOM 1794 CB MET C 208 125.625 17.229 35.490 1.00 22.15 C ANISOU 1794 CB MET C 208 2274 3454 2690 180 -14 209 C ATOM 1795 CG MET C 208 126.994 17.181 34.845 1.00 23.98 C ANISOU 1795 CG MET C 208 2428 3690 2992 187 22 200 C ATOM 1796 SD MET C 208 128.221 17.884 35.946 1.00 28.07 S ANISOU 1796 SD MET C 208 2838 4391 3437 128 -51 266 S ATOM 1797 CE MET C 208 129.711 17.605 34.997 1.00 28.12 C ANISOU 1797 CE MET C 208 2745 4373 3568 157 9 261 C ATOM 1798 N VAL C 209 122.506 15.688 35.450 1.00 19.51 N ANISOU 1798 N VAL C 209 2075 2931 2408 250 13 222 N ATOM 1799 CA VAL C 209 121.181 15.634 36.070 1.00 19.33 C ANISOU 1799 CA VAL C 209 2103 2905 2337 247 -12 242 C ATOM 1800 C VAL C 209 121.287 14.968 37.425 1.00 19.98 C ANISOU 1800 C VAL C 209 2108 3057 2428 270 -54 373 C ATOM 1801 O VAL C 209 121.830 13.874 37.525 1.00 21.77 O ANISOU 1801 O VAL C 209 2252 3249 2771 325 -38 465 O ATOM 1802 CB VAL C 209 120.183 14.861 35.192 1.00 19.45 C ANISOU 1802 CB VAL C 209 2168 2803 2418 266 34 201 C ATOM 1803 CG1 VAL C 209 118.791 14.842 35.807 1.00 19.34 C ANISOU 1803 CG1 VAL C 209 2197 2790 2361 261 10 223 C ATOM 1804 CG2 VAL C 209 120.131 15.485 33.825 1.00 19.11 C ANISOU 1804 CG2 VAL C 209 2188 2725 2346 227 66 92 C ATOM 1805 N ASN C 210 120.776 15.646 38.452 1.00 19.50 N ANISOU 1805 N ASN C 210 2069 3093 2248 223 -97 384 N ATOM 1806 CA ASN C 210 120.785 15.141 39.821 1.00 20.19 C ANISOU 1806 CA ASN C 210 2087 3285 2298 218 -144 512 C ATOM 1807 C ASN C 210 119.425 15.366 40.435 1.00 19.41 C ANISOU 1807 C ASN C 210 2054 3196 2124 190 -144 491 C ATOM 1808 O ASN C 210 118.872 16.470 40.346 1.00 19.00 O ANISOU 1808 O ASN C 210 2077 3149 1992 141 -128 380 O ATOM 1809 CB ASN C 210 121.837 15.865 40.663 1.00 20.91 C ANISOU 1809 CB ASN C 210 2115 3548 2281 151 -196 540 C ATOM 1810 N VAL C 211 118.893 14.317 41.052 1.00 19.65 N ANISOU 1810 N VAL C 211 2050 3221 2197 223 -152 603 N ATOM 1811 CA VAL C 211 117.617 14.375 41.737 1.00 19.35 C ANISOU 1811 CA VAL C 211 2059 3201 2094 196 -147 600 C ATOM 1812 C VAL C 211 117.858 14.295 43.241 1.00 20.37 C ANISOU 1812 C VAL C 211 2124 3507 2110 142 -196 712 C ATOM 1813 O VAL C 211 118.644 13.461 43.719 1.00 21.37 O ANISOU 1813 O VAL C 211 2150 3694 2276 167 -235 868 O ATOM 1814 CB VAL C 211 116.701 13.220 41.301 1.00 19.24 C ANISOU 1814 CB VAL C 211 2056 3051 2203 257 -114 640 C ATOM 1815 CG1 VAL C 211 115.382 13.258 42.067 1.00 19.32 C ANISOU 1815 CG1 VAL C 211 2103 3088 2148 228 -108 647 C ATOM 1816 CG2 VAL C 211 116.484 13.250 39.792 1.00 18.82 C ANISOU 1816 CG2 VAL C 211 2059 2855 2235 284 -69 527 C ATOM 1817 N THR C 212 117.182 15.159 43.985 1.00 20.67 N ANISOU 1817 N THR C 212 2210 3631 2010 63 -187 639 N ATOM 1818 CA THR C 212 117.285 15.173 45.442 1.00 22.37 C ANISOU 1818 CA THR C 212 2375 4043 2080 -21 -224 721 C ATOM 1819 C THR C 212 115.906 15.098 46.094 1.00 22.63 C ANISOU 1819 C THR C 212 2456 4080 2062 -48 -187 707 C ATOM 1820 O THR C 212 114.946 15.673 45.588 1.00 21.65 O ANISOU 1820 O THR C 212 2413 3846 1967 -38 -128 578 O ATOM 1821 CB THR C 212 118.025 16.422 45.949 1.00 23.24 C ANISOU 1821 CB THR C 212 2487 4307 2036 -136 -235 622 C ATOM 1822 OG1 THR C 212 117.365 17.605 45.495 1.00 23.39 O ANISOU 1822 OG1 THR C 212 2607 4238 2043 -166 -162 430 O ATOM 1823 CG2 THR C 212 119.470 16.432 45.470 1.00 23.61 C ANISOU 1823 CG2 THR C 212 2466 4384 2123 -120 -280 660 C ATOM 1824 N ARG C 213 115.828 14.382 47.220 1.00 24.29 N ANISOU 1824 N ARG C 213 2604 4425 2201 -83 -222 855 N ATOM 1825 CA ARG C 213 114.604 14.231 48.011 1.00 25.06 C ANISOU 1825 CA ARG C 213 2732 4558 2232 -123 -186 860 C ATOM 1826 C ARG C 213 114.823 15.023 49.292 1.00 26.73 C ANISOU 1826 C ARG C 213 2931 5007 2217 -274 -192 822 C ATOM 1827 O ARG C 213 115.849 14.842 49.955 1.00 28.27 O ANISOU 1827 O ARG C 213 3042 5386 2314 -334 -264 938 O ATOM 1828 CB ARG C 213 114.357 12.742 48.330 1.00 25.78 C ANISOU 1828 CB ARG C 213 2757 4628 2410 -62 -214 1072 C ATOM 1829 CG ARG C 213 113.141 12.421 49.209 1.00 26.53 C ANISOU 1829 CG ARG C 213 2870 4772 2438 -105 -181 1109 C ATOM 1830 CD ARG C 213 113.149 10.960 49.669 1.00 27.72 C ANISOU 1830 CD ARG C 213 2937 4929 2669 -59 -216 1354 C ATOM 1831 NE ARG C 213 112.133 10.651 50.683 1.00 28.76 N ANISOU 1831 NE ARG C 213 3071 5150 2706 -121 -191 1416 N ATOM 1832 CZ ARG C 213 112.199 10.974 51.985 1.00 30.27 C ANISOU 1832 CZ ARG C 213 3232 5591 2680 -249 -213 1467 C ATOM 1833 NH1 ARG C 213 113.236 11.653 52.479 1.00 31.13 N ANISOU 1833 NH1 ARG C 213 3302 5896 2630 -340 -266 1458 N ATOM 1834 NH2 ARG C 213 111.210 10.618 52.814 1.00 31.21 N ANISOU 1834 NH2 ARG C 213 3357 5777 2726 -302 -178 1522 N ATOM 1835 N SER C 214 113.883 15.907 49.627 1.00 27.20 N ANISOU 1835 N SER C 214 3065 5069 2199 -344 -109 660 N ATOM 1836 CA SER C 214 113.899 16.633 50.905 1.00 29.11 C ANISOU 1836 CA SER C 214 3307 5534 2221 -511 -83 590 C ATOM 1837 C SER C 214 112.552 16.524 51.598 1.00 29.70 C ANISOU 1837 C SER C 214 3416 5620 2249 -549 -7 561 C ATOM 1838 O SER C 214 111.532 16.941 51.057 1.00 28.60 O ANISOU 1838 O SER C 214 3343 5308 2214 -496 80 438 O ATOM 1839 CB SER C 214 114.273 18.103 50.698 1.00 29.48 C ANISOU 1839 CB SER C 214 3408 5576 2216 -591 -20 367 C ATOM 1840 OG SER C 214 113.605 18.665 49.583 1.00 29.02 O ANISOU 1840 OG SER C 214 3425 5276 2326 -495 53 239 O ATOM 1841 N ILE C 221 107.156 15.922 51.228 1.00 24.87 N ANISOU 1841 N ILE C 221 2933 4555 1963 -380 290 429 N ATOM 1842 CA ILE C 221 108.400 15.655 50.520 1.00 24.04 C ANISOU 1842 CA ILE C 221 2810 4427 1899 -326 189 498 C ATOM 1843 C ILE C 221 108.470 16.510 49.255 1.00 22.43 C ANISOU 1843 C ILE C 221 2649 4048 1826 -253 213 368 C ATOM 1844 O ILE C 221 107.527 16.507 48.468 1.00 21.94 O ANISOU 1844 O ILE C 221 2607 3829 1901 -176 247 338 O ATOM 1845 CB ILE C 221 108.484 14.164 50.096 1.00 24.11 C ANISOU 1845 CB ILE C 221 2774 4367 2020 -229 109 696 C ATOM 1846 CG1 ILE C 221 108.330 13.240 51.314 1.00 25.67 C ANISOU 1846 CG1 ILE C 221 2918 4722 2114 -291 87 863 C ATOM 1847 CG2 ILE C 221 109.774 13.861 49.339 1.00 23.78 C ANISOU 1847 CG2 ILE C 221 2704 4287 2045 -169 26 760 C ATOM 1848 CD1 ILE C 221 109.316 13.495 52.430 1.00 27.23 C ANISOU 1848 CD1 ILE C 221 3072 5172 2101 -414 43 916 C ATOM 1849 N THR C 222 109.578 17.228 49.068 1.00 21.94 N ANISOU 1849 N THR C 222 2593 4025 1716 -286 189 305 N ATOM 1850 CA THR C 222 109.864 17.947 47.825 1.00 20.68 C ANISOU 1850 CA THR C 222 2468 3714 1676 -220 196 216 C ATOM 1851 C THR C 222 110.941 17.167 47.099 1.00 19.72 C ANISOU 1851 C THR C 222 2315 3573 1607 -155 94 327 C ATOM 1852 O THR C 222 111.968 16.822 47.692 1.00 20.51 O ANISOU 1852 O THR C 222 2367 3812 1613 -200 34 407 O ATOM 1853 CB THR C 222 110.356 19.387 48.081 1.00 21.40 C ANISOU 1853 CB THR C 222 2590 3845 1697 -309 263 50 C ATOM 1854 OG1 THR C 222 109.351 20.107 48.810 1.00 22.67 O ANISOU 1854 OG1 THR C 222 2775 4010 1827 -375 385 -68 O ATOM 1855 CG2 THR C 222 110.677 20.119 46.756 1.00 20.49 C ANISOU 1855 CG2 THR C 222 2504 3569 1712 -238 268 -15 C ATOM 1856 N VAL C 223 110.700 16.867 45.825 1.00 18.11 N ANISOU 1856 N VAL C 223 2125 3205 1550 -55 80 336 N ATOM 1857 CA VAL C 223 111.714 16.247 44.979 1.00 17.57 C ANISOU 1857 CA VAL C 223 2033 3093 1552 4 13 404 C ATOM 1858 C VAL C 223 112.133 17.302 43.965 1.00 16.74 C ANISOU 1858 C VAL C 223 1967 2909 1486 16 30 290 C ATOM 1859 O VAL C 223 111.279 17.974 43.365 1.00 16.15 O ANISOU 1859 O VAL C 223 1931 2736 1469 35 79 213 O ATOM 1860 CB VAL C 223 111.250 14.912 44.335 1.00 17.31 C ANISOU 1860 CB VAL C 223 1982 2950 1645 85 -8 503 C ATOM 1861 CG1 VAL C 223 111.109 13.837 45.418 1.00 18.32 C ANISOU 1861 CG1 VAL C 223 2059 3162 1741 71 -28 646 C ATOM 1862 CG2 VAL C 223 109.952 15.056 43.550 1.00 16.71 C ANISOU 1862 CG2 VAL C 223 1946 2751 1653 119 33 440 C ATOM 1863 N THR C 224 113.443 17.472 43.803 1.00 16.68 N ANISOU 1863 N THR C 224 1937 2951 1451 1 -8 294 N ATOM 1864 CA THR C 224 114.009 18.508 42.940 1.00 16.44 C ANISOU 1864 CA THR C 224 1938 2865 1444 -2 9 195 C ATOM 1865 C THR C 224 114.926 17.851 41.927 1.00 16.15 C ANISOU 1865 C THR C 224 1876 2776 1484 56 -38 247 C ATOM 1866 O THR C 224 115.785 17.040 42.290 1.00 16.56 O ANISOU 1866 O THR C 224 1867 2895 1530 64 -84 341 O ATOM 1867 CB THR C 224 114.810 19.546 43.749 1.00 17.23 C ANISOU 1867 CB THR C 224 2034 3084 1426 -104 25 117 C ATOM 1868 OG1 THR C 224 113.984 20.065 44.802 1.00 17.81 O ANISOU 1868 OG1 THR C 224 2129 3217 1422 -176 88 53 O ATOM 1869 CG2 THR C 224 115.288 20.693 42.855 1.00 16.95 C ANISOU 1869 CG2 THR C 224 2037 2970 1434 -110 59 13 C ATOM 1870 N ACYS C 225 114.751 18.193 40.657 0.50 15.15 N ANISOU 1870 N ACYS C 225 1787 2535 1434 94 -20 193 N ATOM 1871 N BCYS C 225 114.712 18.201 40.659 0.50 16.02 N ANISOU 1871 N BCYS C 225 1898 2644 1545 94 -19 192 N ATOM 1872 CA ACYS C 225 115.594 17.672 39.594 0.50 14.90 C ANISOU 1872 CA ACYS C 225 1739 2452 1469 135 -42 212 C ATOM 1873 CA BCYS C 225 115.546 17.776 39.546 0.50 16.29 C ANISOU 1873 CA BCYS C 225 1920 2624 1644 133 -39 204 C ATOM 1874 C ACYS C 225 116.400 18.827 39.019 0.50 14.83 C ANISOU 1874 C ACYS C 225 1752 2445 1440 103 -30 133 C ATOM 1875 C BCYS C 225 116.406 18.932 39.136 0.50 15.71 C ANISOU 1875 C BCYS C 225 1863 2564 1542 96 -29 129 C ATOM 1876 O ACYS C 225 115.828 19.754 38.444 0.50 14.39 O ANISOU 1876 O ACYS C 225 1742 2328 1398 95 3 72 O ATOM 1877 O BCYS C 225 115.871 19.974 38.765 0.50 15.30 O ANISOU 1877 O BCYS C 225 1857 2464 1492 80 8 62 O ATOM 1878 CB ACYS C 225 114.727 17.032 38.526 0.50 14.24 C ANISOU 1878 CB ACYS C 225 1679 2259 1471 180 -31 214 C ATOM 1879 CB BCYS C 225 114.694 17.467 38.339 0.50 16.76 C ANISOU 1879 CB BCYS C 225 2013 2573 1782 171 -24 187 C ATOM 1880 SG ACYS C 225 115.586 16.527 37.016 0.50 14.08 S ANISOU 1880 SG ACYS C 225 1656 2170 1525 204 -27 191 S ATOM 1881 SG BCYS C 225 115.415 16.199 37.301 0.50 18.17 S ANISOU 1881 SG BCYS C 225 2165 2691 2050 211 -29 215 S ATOM 1882 N ARG C 226 117.722 18.757 39.182 1.00 15.62 N ANISOU 1882 N ARG C 226 1805 2611 1517 86 -55 151 N ATOM 1883 CA ARG C 226 118.644 19.823 38.789 1.00 15.74 C ANISOU 1883 CA ARG C 226 1829 2644 1506 43 -44 80 C ATOM 1884 C ARG C 226 119.367 19.392 37.542 1.00 15.01 C ANISOU 1884 C ARG C 226 1724 2491 1486 84 -45 86 C ATOM 1885 O ARG C 226 119.873 18.272 37.483 1.00 15.48 O ANISOU 1885 O ARG C 226 1729 2552 1599 126 -61 153 O ATOM 1886 CB ARG C 226 119.653 20.095 39.914 1.00 17.28 C ANISOU 1886 CB ARG C 226 1969 2985 1611 -25 -71 91 C ATOM 1887 CG ARG C 226 119.009 20.698 41.152 1.00 18.62 C ANISOU 1887 CG ARG C 226 2158 3233 1682 -100 -52 50 C ATOM 1888 CD ARG C 226 120.042 21.076 42.199 1.00 20.38 C ANISOU 1888 CD ARG C 226 2326 3631 1786 -202 -80 43 C ATOM 1889 NE ARG C 226 119.411 21.739 43.339 1.00 21.96 N ANISOU 1889 NE ARG C 226 2554 3912 1878 -299 -39 -31 N ATOM 1890 CZ ARG C 226 118.731 21.131 44.315 1.00 23.18 C ANISOU 1890 CZ ARG C 226 2693 4147 1967 -316 -51 27 C ATOM 1891 NH1 ARG C 226 118.579 19.805 44.342 1.00 23.58 N ANISOU 1891 NH1 ARG C 226 2696 4201 2061 -236 -108 177 N ATOM 1892 NH2 ARG C 226 118.195 21.859 45.297 1.00 24.50 N ANISOU 1892 NH2 ARG C 226 2891 4389 2031 -422 8 -71 N ATOM 1893 N ALA C 227 119.424 20.284 36.558 1.00 14.00 N ANISOU 1893 N ALA C 227 1643 2309 1369 67 -16 20 N ATOM 1894 CA ALA C 227 120.239 20.075 35.356 1.00 13.58 C ANISOU 1894 CA ALA C 227 1581 2221 1360 81 -6 6 C ATOM 1895 C ALA C 227 121.296 21.165 35.342 1.00 13.47 C ANISOU 1895 C ALA C 227 1559 2250 1308 26 4 -41 C ATOM 1896 O ALA C 227 120.958 22.349 35.379 1.00 13.21 O ANISOU 1896 O ALA C 227 1571 2199 1249 -15 29 -90 O ATOM 1897 CB ALA C 227 119.379 20.151 34.107 1.00 13.12 C ANISOU 1897 CB ALA C 227 1577 2081 1327 91 16 -16 C ATOM 1898 N ASER C 228 122.558 20.758 35.296 0.50 13.87 N ANISOU 1898 N ASER C 228 1545 2350 1374 26 -6 -24 N ATOM 1899 N BSER C 228 122.570 20.785 35.286 0.50 13.77 N ANISOU 1899 N BSER C 228 1533 2337 1360 25 -6 -25 N ATOM 1900 CA ASER C 228 123.671 21.680 35.425 0.50 14.32 C ANISOU 1900 CA ASER C 228 1577 2470 1394 -35 -3 -63 C ATOM 1901 CA BSER C 228 123.657 21.766 35.343 0.50 14.13 C ANISOU 1901 CA BSER C 228 1559 2440 1370 -38 1 -69 C ATOM 1902 C ASER C 228 124.651 21.532 34.281 0.50 14.24 C ANISOU 1902 C ASER C 228 1542 2434 1432 -26 23 -78 C ATOM 1903 C BSER C 228 124.714 21.595 34.261 0.50 14.21 C ANISOU 1903 C BSER C 228 1539 2433 1428 -30 24 -81 C ATOM 1904 O ASER C 228 124.707 20.491 33.629 0.50 14.32 O ANISOU 1904 O ASER C 228 1532 2400 1509 28 38 -53 O ATOM 1905 O BSER C 228 124.794 20.560 33.601 0.50 14.33 O ANISOU 1905 O BSER C 228 1532 2404 1509 24 39 -57 O ATOM 1906 CB ASER C 228 124.385 21.432 36.754 0.50 15.24 C ANISOU 1906 CB ASER C 228 1611 2719 1462 -66 -49 -16 C ATOM 1907 CB BSER C 228 124.320 21.740 36.722 0.50 14.88 C ANISOU 1907 CB BSER C 228 1582 2668 1405 -81 -42 -37 C ATOM 1908 OG ASER C 228 123.465 21.455 37.831 0.50 15.58 O ANISOU 1908 OG ASER C 228 1675 2799 1445 -86 -66 -4 O ATOM 1909 OG BSER C 228 124.795 20.443 37.038 0.50 15.27 O ANISOU 1909 OG BSER C 228 1541 2759 1501 -25 -78 65 O ATOM 1910 N ASER C 229 125.393 22.604 34.034 0.50 14.33 N ANISOU 1910 N ASER C 229 1560 2469 1416 -88 42 -130 N ATOM 1911 N BSER C 229 125.518 22.642 34.106 0.50 14.50 N ANISOU 1911 N BSER C 229 1574 2501 1434 -93 40 -130 N ATOM 1912 CA ASER C 229 126.547 22.580 33.145 0.50 14.57 C ANISOU 1912 CA ASER C 229 1551 2505 1481 -96 69 -146 C ATOM 1913 CA BSER C 229 126.569 22.729 33.095 0.50 14.77 C ANISOU 1913 CA BSER C 229 1582 2528 1501 -104 72 -153 C ATOM 1914 C ASER C 229 126.239 22.267 31.684 0.50 14.06 C ANISOU 1914 C ASER C 229 1534 2357 1452 -71 114 -167 C ATOM 1915 C BSER C 229 126.164 22.162 31.738 0.50 14.17 C ANISOU 1915 C BSER C 229 1547 2369 1469 -65 111 -162 C ATOM 1916 O ASER C 229 127.090 21.689 30.992 0.50 14.42 O ANISOU 1916 O ASER C 229 1532 2402 1544 -59 148 -175 O ATOM 1917 O BSER C 229 126.827 21.265 31.190 0.50 14.58 O ANISOU 1917 O BSER C 229 1547 2414 1579 -34 139 -158 O ATOM 1918 CB ASER C 229 127.584 21.587 33.670 0.50 15.33 C ANISOU 1918 CB ASER C 229 1530 2674 1623 -63 44 -84 C ATOM 1919 CB BSER C 229 127.878 22.102 33.587 0.50 15.73 C ANISOU 1919 CB BSER C 229 1584 2739 1653 -96 50 -109 C ATOM 1920 OG ASER C 229 128.115 22.022 34.913 0.50 16.06 O ANISOU 1920 OG ASER C 229 1562 2887 1652 -119 -5 -61 O ATOM 1921 OG BSER C 229 127.668 20.816 34.131 0.50 16.26 O ANISOU 1921 OG BSER C 229 1593 2814 1771 -25 23 -27 O ATOM 1922 N PHE C 230 125.073 22.704 31.195 1.00 13.39 N ANISOU 1922 N PHE C 230 1532 2213 1343 -76 120 -175 N ATOM 1923 CA PHE C 230 124.634 22.368 29.829 1.00 13.02 C ANISOU 1923 CA PHE C 230 1526 2120 1299 -75 151 -187 C ATOM 1924 C PHE C 230 124.689 23.551 28.879 1.00 12.90 C ANISOU 1924 C PHE C 230 1558 2096 1247 -133 176 -197 C ATOM 1925 O PHE C 230 124.677 24.710 29.285 1.00 12.81 O ANISOU 1925 O PHE C 230 1565 2074 1227 -162 176 -194 O ATOM 1926 CB PHE C 230 123.253 21.706 29.812 1.00 12.47 C ANISOU 1926 CB PHE C 230 1493 2012 1232 -40 132 -161 C ATOM 1927 CG PHE C 230 122.127 22.562 30.347 1.00 12.00 C ANISOU 1927 CG PHE C 230 1478 1932 1151 -41 106 -132 C ATOM 1928 CD1 PHE C 230 121.427 23.422 29.513 1.00 11.99 C ANISOU 1928 CD1 PHE C 230 1523 1902 1130 -68 113 -110 C ATOM 1929 CD2 PHE C 230 121.750 22.493 31.687 1.00 11.84 C ANISOU 1929 CD2 PHE C 230 1444 1921 1135 -17 81 -118 C ATOM 1930 CE1 PHE C 230 120.392 24.205 30.001 1.00 11.81 C ANISOU 1930 CE1 PHE C 230 1524 1840 1122 -58 106 -75 C ATOM 1931 CE2 PHE C 230 120.710 23.266 32.175 1.00 11.70 C ANISOU 1931 CE2 PHE C 230 1462 1872 1112 -20 80 -106 C ATOM 1932 CZ PHE C 230 120.026 24.121 31.334 1.00 11.70 C ANISOU 1932 CZ PHE C 230 1501 1822 1123 -33 97 -85 C ATOM 1933 N TYR C 231 124.787 23.229 27.589 1.00 13.05 N ANISOU 1933 N TYR C 231 1593 2119 1248 -158 208 -213 N ATOM 1934 CA TYR C 231 124.818 24.232 26.526 1.00 13.51 C ANISOU 1934 CA TYR C 231 1689 2185 1261 -221 230 -197 C ATOM 1935 C TYR C 231 124.315 23.548 25.255 1.00 13.65 C ANISOU 1935 C TYR C 231 1730 2229 1226 -254 246 -204 C ATOM 1936 O TYR C 231 124.745 22.438 24.974 1.00 13.73 O ANISOU 1936 O TYR C 231 1715 2249 1251 -250 282 -266 O ATOM 1937 CB TYR C 231 126.237 24.773 26.284 1.00 14.19 C ANISOU 1937 CB TYR C 231 1744 2299 1350 -264 271 -232 C ATOM 1938 CG TYR C 231 126.268 25.856 25.230 1.00 14.97 C ANISOU 1938 CG TYR C 231 1880 2402 1405 -332 296 -198 C ATOM 1939 CD1 TYR C 231 126.403 25.534 23.887 1.00 15.67 C ANISOU 1939 CD1 TYR C 231 1982 2540 1434 -384 329 -205 C ATOM 1940 CD2 TYR C 231 126.111 27.200 25.570 1.00 15.30 C ANISOU 1940 CD2 TYR C 231 1944 2401 1470 -351 295 -155 C ATOM 1941 CE1 TYR C 231 126.399 26.519 22.916 1.00 16.48 C ANISOU 1941 CE1 TYR C 231 2112 2665 1485 -453 345 -147 C ATOM 1942 CE2 TYR C 231 126.100 28.192 24.601 1.00 16.23 C ANISOU 1942 CE2 TYR C 231 2087 2511 1568 -407 321 -94 C ATOM 1943 CZ TYR C 231 126.249 27.842 23.274 1.00 16.71 C ANISOU 1943 CZ TYR C 231 2156 2640 1554 -458 338 -78 C ATOM 1944 OH TYR C 231 126.234 28.806 22.282 1.00 18.51 O ANISOU 1944 OH TYR C 231 2403 2881 1749 -522 357 7 O ATOM 1945 N PRO C 232 123.431 24.175 24.474 1.00 13.79 N ANISOU 1945 N PRO C 232 1787 2263 1188 -294 225 -139 N ATOM 1946 CA PRO C 232 122.893 25.530 24.676 1.00 13.91 C ANISOU 1946 CA PRO C 232 1822 2243 1220 -293 202 -50 C ATOM 1947 C PRO C 232 121.781 25.563 25.727 1.00 13.72 C ANISOU 1947 C PRO C 232 1801 2162 1248 -228 164 -15 C ATOM 1948 O PRO C 232 121.474 24.538 26.335 1.00 12.94 O ANISOU 1948 O PRO C 232 1693 2062 1161 -187 146 -53 O ATOM 1949 CB PRO C 232 122.353 25.890 23.283 1.00 14.63 C ANISOU 1949 CB PRO C 232 1932 2394 1234 -361 193 29 C ATOM 1950 CG PRO C 232 122.009 24.575 22.674 1.00 14.68 C ANISOU 1950 CG PRO C 232 1939 2464 1172 -390 190 -27 C ATOM 1951 CD PRO C 232 123.061 23.624 23.160 1.00 14.35 C ANISOU 1951 CD PRO C 232 1876 2401 1175 -363 238 -148 C ATOM 1952 N ARG C 233 121.206 26.745 25.932 1.00 14.48 N ANISOU 1952 N ARG C 233 1908 2204 1388 -221 164 59 N ATOM 1953 CA ARG C 233 120.275 26.976 27.045 1.00 14.59 C ANISOU 1953 CA ARG C 233 1922 2153 1469 -165 154 75 C ATOM 1954 C ARG C 233 118.925 26.276 26.921 1.00 14.81 C ANISOU 1954 C ARG C 233 1946 2194 1487 -133 109 128 C ATOM 1955 O ARG C 233 118.247 26.081 27.921 1.00 14.49 O ANISOU 1955 O ARG C 233 1902 2116 1489 -85 103 117 O ATOM 1956 CB ARG C 233 120.063 28.478 27.240 1.00 15.43 C ANISOU 1956 CB ARG C 233 2033 2172 1657 -168 197 130 C ATOM 1957 N ASN C 234 118.558 25.856 25.719 1.00 15.53 N ANISOU 1957 N ASN C 234 2035 2354 1510 -173 81 176 N ATOM 1958 CA ASN C 234 117.254 25.285 25.453 1.00 16.02 C ANISOU 1958 CA ASN C 234 2085 2448 1553 -165 34 233 C ATOM 1959 C ASN C 234 117.217 23.899 26.086 1.00 15.06 C ANISOU 1959 C ASN C 234 1967 2332 1423 -141 28 137 C ATOM 1960 O ASN C 234 118.075 23.077 25.793 1.00 15.07 O ANISOU 1960 O ASN C 234 1974 2364 1389 -167 51 53 O ATOM 1961 CB ASN C 234 117.005 25.124 23.939 1.00 17.56 C ANISOU 1961 CB ASN C 234 2273 2752 1645 -249 4 295 C ATOM 1962 CG ASN C 234 117.282 26.387 23.134 1.00 19.24 C ANISOU 1962 CG ASN C 234 2478 2979 1852 -288 12 406 C ATOM 1963 OD1 ASN C 234 116.371 26.920 22.488 1.00 21.28 O ANISOU 1963 OD1 ASN C 234 2704 3278 2103 -306 -29 555 O ATOM 1964 ND2 ASN C 234 118.548 26.830 23.102 1.00 19.48 N ANISOU 1964 ND2 ASN C 234 2527 2986 1886 -307 61 349 N ATOM 1965 N ILE C 235 116.241 23.637 26.946 1.00 14.57 N ANISOU 1965 N ILE C 235 1895 2233 1409 -88 10 156 N ATOM 1966 CA ILE C 235 116.132 22.345 27.621 1.00 14.30 C ANISOU 1966 CA ILE C 235 1859 2194 1382 -62 7 88 C ATOM 1967 C ILE C 235 114.685 22.086 28.015 1.00 14.55 C ANISOU 1967 C ILE C 235 1874 2214 1439 -34 -24 142 C ATOM 1968 O ILE C 235 113.933 23.036 28.248 1.00 14.85 O ANISOU 1968 O ILE C 235 1899 2222 1523 -8 -29 218 O ATOM 1969 CB ILE C 235 117.053 22.302 28.879 1.00 13.77 C ANISOU 1969 CB ILE C 235 1789 2088 1356 -19 33 30 C ATOM 1970 CG1 ILE C 235 117.203 20.881 29.437 1.00 13.62 C ANISOU 1970 CG1 ILE C 235 1754 2068 1352 7 33 -16 C ATOM 1971 CG2 ILE C 235 116.592 23.296 29.947 1.00 13.80 C ANISOU 1971 CG2 ILE C 235 1793 2044 1408 15 43 56 C ATOM 1972 CD1 ILE C 235 118.362 20.745 30.405 1.00 13.58 C ANISOU 1972 CD1 ILE C 235 1726 2063 1371 33 48 -48 C ATOM 1973 N AILE C 236 114.307 20.809 28.050 0.50 14.75 N ANISOU 1973 N AILE C 236 1897 2255 1454 -40 -33 102 N ATOM 1974 N BILE C 236 114.311 20.812 28.065 0.50 14.71 N ANISOU 1974 N BILE C 236 1891 2248 1448 -39 -33 102 N ATOM 1975 CA AILE C 236 113.025 20.357 28.587 0.50 15.02 C ANISOU 1975 CA AILE C 236 1913 2277 1518 -14 -56 138 C ATOM 1976 CA BILE C 236 113.023 20.384 28.590 0.50 14.97 C ANISOU 1976 CA BILE C 236 1907 2271 1512 -14 -56 139 C ATOM 1977 C AILE C 236 113.309 19.561 29.850 0.50 14.68 C ANISOU 1977 C AILE C 236 1870 2188 1519 36 -35 91 C ATOM 1978 C BILE C 236 113.291 19.557 29.839 0.50 14.65 C ANISOU 1978 C BILE C 236 1867 2185 1515 35 -35 91 C ATOM 1979 O AILE C 236 114.140 18.651 29.838 0.50 14.56 O ANISOU 1979 O AILE C 236 1857 2166 1508 31 -12 32 O ATOM 1980 O BILE C 236 114.096 18.625 29.808 0.50 14.54 O ANISOU 1980 O BILE C 236 1855 2164 1505 30 -13 32 O ATOM 1981 CB AILE C 236 112.267 19.455 27.599 0.50 15.77 C ANISOU 1981 CB AILE C 236 1997 2433 1561 -82 -82 135 C ATOM 1982 CB BILE C 236 112.233 19.548 27.571 0.50 15.69 C ANISOU 1982 CB BILE C 236 1986 2425 1550 -82 -84 142 C ATOM 1983 CG1AILE C 236 111.406 20.297 26.662 0.50 16.63 C ANISOU 1983 CG1AILE C 236 2078 2612 1629 -125 -129 240 C ATOM 1984 CG1BILE C 236 112.173 20.281 26.230 0.50 16.43 C ANISOU 1984 CG1BILE C 236 2072 2602 1570 -154 -112 200 C ATOM 1985 CG2AILE C 236 111.378 18.465 28.342 0.50 15.55 C ANISOU 1985 CG2AILE C 236 1956 2377 1576 -58 -85 124 C ATOM 1986 CG2BILE C 236 110.835 19.268 28.095 0.50 15.76 C ANISOU 1986 CG2BILE C 236 1965 2427 1595 -59 -111 195 C ATOM 1987 CD1AILE C 236 112.183 21.257 25.796 0.50 17.14 C ANISOU 1987 CD1AILE C 236 2151 2714 1649 -161 -127 275 C ATOM 1988 CD1BILE C 236 111.051 19.833 25.322 0.50 17.29 C ANISOU 1988 CD1BILE C 236 2149 2808 1611 -235 -160 243 C ATOM 1989 N LEU C 237 112.623 19.914 30.938 1.00 14.66 N ANISOU 1989 N LEU C 237 1858 2156 1556 82 -35 124 N ATOM 1990 CA LEU C 237 112.735 19.200 32.203 1.00 15.00 C ANISOU 1990 CA LEU C 237 1895 2181 1625 118 -23 105 C ATOM 1991 C LEU C 237 111.316 19.120 32.737 1.00 14.89 C ANISOU 1991 C LEU C 237 1865 2156 1638 137 -30 149 C ATOM 1992 O LEU C 237 110.570 20.102 32.659 1.00 16.15 O ANISOU 1992 O LEU C 237 2013 2304 1819 145 -26 190 O ATOM 1993 CB LEU C 237 113.636 19.971 33.178 1.00 15.62 C ANISOU 1993 CB LEU C 237 1977 2260 1698 134 -2 83 C ATOM 1994 CG LEU C 237 114.473 19.272 34.251 1.00 16.28 C ANISOU 1994 CG LEU C 237 2043 2367 1774 148 0 70 C ATOM 1995 CD1 LEU C 237 115.424 18.233 33.681 1.00 16.72 C ANISOU 1995 CD1 LEU C 237 2082 2422 1848 150 0 57 C ATOM 1996 CD2 LEU C 237 115.266 20.353 34.967 1.00 16.24 C ANISOU 1996 CD2 LEU C 237 2041 2391 1740 129 16 41 C ATOM 1997 N THR C 238 110.931 17.965 33.262 1.00 14.24 N ANISOU 1997 N THR C 238 1771 2067 1571 146 -31 149 N ATOM 1998 CA THR C 238 109.625 17.853 33.901 1.00 14.01 C ANISOU 1998 CA THR C 238 1722 2031 1569 162 -30 188 C ATOM 1999 C THR C 238 109.566 16.629 34.785 1.00 13.56 C ANISOU 1999 C THR C 238 1658 1966 1530 175 -22 192 C ATOM 2000 O THR C 238 110.174 15.600 34.508 1.00 13.85 O ANISOU 2000 O THR C 238 1694 1985 1582 167 -18 175 O ATOM 2001 CB THR C 238 108.454 17.797 32.880 1.00 14.37 C ANISOU 2001 CB THR C 238 1746 2093 1622 132 -58 225 C ATOM 2002 OG1 THR C 238 107.202 17.844 33.580 1.00 14.55 O ANISOU 2002 OG1 THR C 238 1736 2107 1683 155 -51 269 O ATOM 2003 CG2 THR C 238 108.491 16.529 32.013 1.00 14.74 C ANISOU 2003 CG2 THR C 238 1795 2153 1651 79 -71 189 C ATOM 2004 N TRP C 239 108.774 16.742 35.837 1.00 13.04 N ANISOU 2004 N TRP C 239 1577 1903 1473 193 -7 221 N ATOM 2005 CA TRP C 239 108.403 15.601 36.637 1.00 12.80 C ANISOU 2005 CA TRP C 239 1532 1869 1463 199 0 251 C ATOM 2006 C TRP C 239 107.278 14.841 35.951 1.00 12.74 C ANISOU 2006 C TRP C 239 1508 1839 1493 177 -9 263 C ATOM 2007 O TRP C 239 106.472 15.412 35.197 1.00 12.81 O ANISOU 2007 O TRP C 239 1505 1861 1504 160 -25 268 O ATOM 2008 CB TRP C 239 107.984 16.021 38.051 1.00 12.78 C ANISOU 2008 CB TRP C 239 1521 1899 1437 209 27 271 C ATOM 2009 CG TRP C 239 109.192 16.337 38.854 1.00 12.88 C ANISOU 2009 CG TRP C 239 1540 1959 1394 205 30 260 C ATOM 2010 CD1 TRP C 239 109.748 17.567 39.100 1.00 12.91 C ANISOU 2010 CD1 TRP C 239 1560 1990 1356 189 48 211 C ATOM 2011 CD2 TRP C 239 110.057 15.377 39.451 1.00 13.14 C ANISOU 2011 CD2 TRP C 239 1554 2024 1417 209 13 308 C ATOM 2012 NE1 TRP C 239 110.900 17.421 39.836 1.00 13.05 N ANISOU 2012 NE1 TRP C 239 1568 2073 1315 171 35 217 N ATOM 2013 CE2 TRP C 239 111.120 16.085 40.055 1.00 13.30 C ANISOU 2013 CE2 TRP C 239 1573 2114 1369 189 8 290 C ATOM 2014 CE3 TRP C 239 110.038 13.978 39.533 1.00 13.42 C ANISOU 2014 CE3 TRP C 239 1563 2029 1507 226 7 373 C ATOM 2015 CZ2 TRP C 239 112.156 15.434 40.747 1.00 13.88 C ANISOU 2015 CZ2 TRP C 239 1607 2250 1416 187 -18 354 C ATOM 2016 CZ3 TRP C 239 111.057 13.337 40.205 1.00 13.95 C ANISOU 2016 CZ3 TRP C 239 1594 2132 1572 237 -7 442 C ATOM 2017 CH2 TRP C 239 112.106 14.065 40.811 1.00 14.15 C ANISOU 2017 CH2 TRP C 239 1607 2251 1519 219 -27 442 C ATOM 2018 N ARG C 240 107.275 13.537 36.213 1.00 12.86 N ANISOU 2018 N ARG C 240 1516 1825 1547 172 4 276 N ATOM 2019 CA ARG C 240 106.238 12.619 35.756 1.00 13.13 C ANISOU 2019 CA ARG C 240 1533 1834 1623 135 8 277 C ATOM 2020 C ARG C 240 105.786 11.755 36.920 1.00 13.25 C ANISOU 2020 C ARG C 240 1529 1828 1679 151 33 333 C ATOM 2021 O ARG C 240 106.596 11.402 37.778 1.00 13.44 O ANISOU 2021 O ARG C 240 1551 1847 1709 182 46 372 O ATOM 2022 CB ARG C 240 106.783 11.715 34.654 1.00 13.62 C ANISOU 2022 CB ARG C 240 1607 1855 1715 91 22 217 C ATOM 2023 CG ARG C 240 107.126 12.436 33.370 1.00 13.59 C ANISOU 2023 CG ARG C 240 1619 1891 1654 52 -1 164 C ATOM 2024 CD ARG C 240 107.802 11.516 32.375 1.00 14.08 C ANISOU 2024 CD ARG C 240 1696 1914 1738 -2 37 81 C ATOM 2025 NE ARG C 240 107.921 12.132 31.048 1.00 14.24 N ANISOU 2025 NE ARG C 240 1730 2002 1681 -69 13 32 N ATOM 2026 CZ ARG C 240 108.406 11.527 29.966 1.00 15.07 C ANISOU 2026 CZ ARG C 240 1850 2102 1773 -145 52 -63 C ATOM 2027 NH1 ARG C 240 108.855 10.275 30.028 1.00 15.81 N ANISOU 2027 NH1 ARG C 240 1948 2102 1958 -156 130 -127 N ATOM 2028 NH2 ARG C 240 108.441 12.178 28.803 1.00 15.31 N ANISOU 2028 NH2 ARG C 240 1889 2223 1706 -218 22 -91 N ATOM 2029 N GLN C 241 104.498 11.425 36.946 1.00 13.20 N ANISOU 2029 N GLN C 241 1499 1822 1695 124 37 349 N ATOM 2030 CA GLN C 241 103.939 10.446 37.879 1.00 13.56 C ANISOU 2030 CA GLN C 241 1524 1841 1788 124 67 404 C ATOM 2031 C GLN C 241 103.467 9.266 37.035 1.00 13.76 C ANISOU 2031 C GLN C 241 1541 1805 1882 66 85 369 C ATOM 2032 O GLN C 241 102.619 9.438 36.169 1.00 13.69 O ANISOU 2032 O GLN C 241 1517 1824 1858 13 64 331 O ATOM 2033 CB GLN C 241 102.769 11.039 38.677 1.00 13.91 C ANISOU 2033 CB GLN C 241 1542 1934 1809 130 73 441 C ATOM 2034 CG GLN C 241 102.153 10.028 39.643 1.00 14.73 C ANISOU 2034 CG GLN C 241 1625 2021 1953 121 107 504 C ATOM 2035 CD GLN C 241 100.981 10.560 40.451 1.00 15.29 C ANISOU 2035 CD GLN C 241 1665 2142 2004 120 129 531 C ATOM 2036 OE1 GLN C 241 101.029 10.579 41.681 1.00 16.24 O ANISOU 2036 OE1 GLN C 241 1783 2300 2086 129 159 576 O ATOM 2037 NE2 GLN C 241 99.918 10.958 39.780 1.00 15.60 N ANISOU 2037 NE2 GLN C 241 1671 2191 2067 101 119 511 N ATOM 2038 N ASP C 242 104.035 8.082 37.256 1.00 13.87 N ANISOU 2038 N ASP C 242 1556 1737 1977 69 129 385 N ATOM 2039 CA ASP C 242 103.762 6.892 36.439 1.00 14.51 C ANISOU 2039 CA ASP C 242 1634 1733 2145 3 176 325 C ATOM 2040 C ASP C 242 103.992 7.161 34.945 1.00 14.34 C ANISOU 2040 C ASP C 242 1635 1732 2083 -62 165 207 C ATOM 2041 O ASP C 242 103.301 6.606 34.089 1.00 14.80 O ANISOU 2041 O ASP C 242 1687 1784 2153 -157 182 133 O ATOM 2042 CB ASP C 242 102.329 6.371 36.673 1.00 15.10 C ANISOU 2042 CB ASP C 242 1681 1809 2249 -49 186 344 C ATOM 2043 CG ASP C 242 101.989 6.207 38.137 1.00 15.30 C ANISOU 2043 CG ASP C 242 1684 1838 2290 2 198 461 C ATOM 2044 OD1 ASP C 242 102.778 5.584 38.894 1.00 15.66 O ANISOU 2044 OD1 ASP C 242 1727 1829 2395 48 230 536 O ATOM 2045 OD2 ASP C 242 100.904 6.668 38.537 1.00 15.58 O ANISOU 2045 OD2 ASP C 242 1696 1939 2284 -9 179 487 O ATOM 2046 N GLY C 243 104.974 8.013 34.637 1.00 13.72 N ANISOU 2046 N GLY C 243 1577 1689 1945 -26 138 190 N ATOM 2047 CA GLY C 243 105.261 8.370 33.248 1.00 13.81 C ANISOU 2047 CA GLY C 243 1609 1741 1898 -92 126 92 C ATOM 2048 C GLY C 243 104.457 9.525 32.676 1.00 13.56 C ANISOU 2048 C GLY C 243 1565 1828 1759 -125 51 105 C ATOM 2049 O GLY C 243 104.768 9.996 31.585 1.00 13.75 O ANISOU 2049 O GLY C 243 1600 1908 1714 -176 29 53 O ATOM 2050 N VAL C 244 103.428 9.964 33.397 1.00 13.48 N ANISOU 2050 N VAL C 244 1522 1855 1744 -96 20 182 N ATOM 2051 CA VAL C 244 102.530 11.025 32.938 1.00 13.63 C ANISOU 2051 CA VAL C 244 1506 1971 1702 -113 -42 223 C ATOM 2052 C VAL C 244 103.129 12.374 33.332 1.00 13.39 C ANISOU 2052 C VAL C 244 1487 1958 1642 -31 -60 266 C ATOM 2053 O VAL C 244 103.356 12.634 34.512 1.00 13.01 O ANISOU 2053 O VAL C 244 1448 1879 1617 40 -36 299 O ATOM 2054 CB VAL C 244 101.120 10.878 33.566 1.00 13.73 C ANISOU 2054 CB VAL C 244 1465 2002 1750 -116 -47 284 C ATOM 2055 CG1 VAL C 244 100.173 11.947 33.043 1.00 13.89 C ANISOU 2055 CG1 VAL C 244 1425 2116 1737 -126 -105 347 C ATOM 2056 CG2 VAL C 244 100.531 9.492 33.314 1.00 14.45 C ANISOU 2056 CG2 VAL C 244 1544 2063 1882 -204 -18 237 C ATOM 2057 N SER C 245 103.397 13.224 32.348 1.00 14.01 N ANISOU 2057 N SER C 245 1566 2092 1665 -53 -97 264 N ATOM 2058 CA SER C 245 104.036 14.509 32.619 1.00 14.12 C ANISOU 2058 CA SER C 245 1594 2106 1666 15 -102 294 C ATOM 2059 C SER C 245 103.091 15.398 33.427 1.00 14.28 C ANISOU 2059 C SER C 245 1571 2127 1729 71 -97 368 C ATOM 2060 O SER C 245 101.923 15.525 33.093 1.00 15.26 O ANISOU 2060 O SER C 245 1635 2291 1872 50 -122 424 O ATOM 2061 CB SER C 245 104.480 15.170 31.315 1.00 14.74 C ANISOU 2061 CB SER C 245 1676 2241 1682 -30 -139 290 C ATOM 2062 OG SER C 245 105.502 14.381 30.702 1.00 15.72 O ANISOU 2062 OG SER C 245 1844 2353 1775 -78 -117 200 O ATOM 2063 N LEU C 246 103.586 15.934 34.548 1.00 13.96 N ANISOU 2063 N LEU C 246 1554 2046 1704 134 -54 362 N ATOM 2064 CA LEU C 246 102.794 16.851 35.369 1.00 14.34 C ANISOU 2064 CA LEU C 246 1567 2082 1800 181 -18 403 C ATOM 2065 C LEU C 246 102.554 18.160 34.632 1.00 14.87 C ANISOU 2065 C LEU C 246 1598 2152 1899 199 -28 454 C ATOM 2066 O LEU C 246 103.383 18.597 33.834 1.00 14.70 O ANISOU 2066 O LEU C 246 1602 2139 1844 186 -53 447 O ATOM 2067 CB LEU C 246 103.454 17.147 36.720 1.00 14.19 C ANISOU 2067 CB LEU C 246 1585 2039 1768 214 38 364 C ATOM 2068 CG LEU C 246 103.129 16.149 37.827 1.00 14.25 C ANISOU 2068 CG LEU C 246 1592 2053 1768 209 63 366 C ATOM 2069 CD1 LEU C 246 103.735 14.771 37.585 1.00 14.10 C ANISOU 2069 CD1 LEU C 246 1596 2028 1732 183 34 360 C ATOM 2070 CD2 LEU C 246 103.599 16.704 39.160 1.00 14.33 C ANISOU 2070 CD2 LEU C 246 1625 2078 1743 221 119 336 C ATOM 2071 N SER C 247 101.427 18.792 34.939 1.00 15.71 N ANISOU 2071 N SER C 247 1638 2244 2085 232 1 515 N ATOM 2072 CA SER C 247 101.166 20.147 34.448 1.00 16.61 C ANISOU 2072 CA SER C 247 1703 2333 2274 269 14 586 C ATOM 2073 C SER C 247 102.255 21.105 34.930 1.00 16.62 C ANISOU 2073 C SER C 247 1763 2272 2281 297 76 524 C ATOM 2074 O SER C 247 102.907 20.853 35.951 1.00 15.81 O ANISOU 2074 O SER C 247 1718 2155 2133 294 119 433 O ATOM 2075 CB SER C 247 99.821 20.649 34.950 1.00 17.60 C ANISOU 2075 CB SER C 247 1740 2429 2519 313 66 655 C ATOM 2076 OG SER C 247 99.842 20.769 36.365 1.00 17.59 O ANISOU 2076 OG SER C 247 1769 2373 2541 339 165 573 O ATOM 2077 N AHIS C 248 102.451 22.204 34.206 0.50 17.21 N ANISOU 2077 N AHIS C 248 1814 2317 2407 316 79 582 N ATOM 2078 N BHIS C 248 102.436 22.201 34.200 0.50 17.26 N ANISOU 2078 N BHIS C 248 1820 2324 2415 316 78 583 N ATOM 2079 CA AHIS C 248 103.430 23.221 34.607 0.50 17.36 C ANISOU 2079 CA AHIS C 248 1882 2266 2448 333 148 520 C ATOM 2080 CA BHIS C 248 103.386 23.244 34.586 0.50 17.47 C ANISOU 2080 CA BHIS C 248 1893 2279 2467 335 148 524 C ATOM 2081 C AHIS C 248 103.069 23.842 35.968 0.50 17.94 C ANISOU 2081 C AHIS C 248 1952 2262 2602 364 271 453 C ATOM 2082 C BHIS C 248 103.062 23.820 35.968 0.50 17.97 C ANISOU 2082 C BHIS C 248 1956 2267 2605 363 270 453 C ATOM 2083 O AHIS C 248 103.955 24.117 36.777 0.50 17.76 O ANISOU 2083 O AHIS C 248 1992 2221 2535 342 327 343 O ATOM 2084 O BHIS C 248 103.956 24.043 36.783 0.50 17.76 O ANISOU 2084 O BHIS C 248 1993 2226 2529 340 323 342 O ATOM 2085 CB AHIS C 248 103.549 24.304 33.524 0.50 18.10 C ANISOU 2085 CB AHIS C 248 1939 2331 2609 349 136 619 C ATOM 2086 CB BHIS C 248 103.380 24.367 33.547 0.50 18.36 C ANISOU 2086 CB BHIS C 248 1960 2357 2659 355 142 631 C ATOM 2087 CG AHIS C 248 104.787 25.144 33.632 0.50 18.06 C ANISOU 2087 CG AHIS C 248 1994 2269 2598 342 186 550 C ATOM 2088 CG BHIS C 248 104.518 25.324 33.693 0.50 18.46 C ANISOU 2088 CG BHIS C 248 2027 2302 2685 355 202 568 C ATOM 2089 ND1AHIS C 248 105.961 24.832 32.979 0.50 17.51 N ANISOU 2089 ND1AHIS C 248 1983 2254 2418 297 128 515 N ATOM 2090 ND1BHIS C 248 104.458 26.436 34.504 0.50 19.17 N ANISOU 2090 ND1BHIS C 248 2111 2276 2897 387 328 524 N ATOM 2091 CD2AHIS C 248 105.024 26.297 34.300 0.50 18.62 C ANISOU 2091 CD2AHIS C 248 2073 2232 2770 366 300 502 C ATOM 2092 CD2BHIS C 248 105.752 25.330 33.137 0.50 18.05 C ANISOU 2092 CD2BHIS C 248 2034 2280 2544 316 164 530 C ATOM 2093 CE1AHIS C 248 106.871 25.752 33.250 0.50 17.59 C ANISOU 2093 CE1AHIS C 248 2030 2199 2453 295 191 458 C ATOM 2094 CE1BHIS C 248 105.606 27.086 34.440 0.50 19.10 C ANISOU 2094 CE1BHIS C 248 2158 2232 2870 363 359 463 C ATOM 2095 NE2AHIS C 248 106.329 26.649 34.055 0.50 18.42 N ANISOU 2095 NE2AHIS C 248 2110 2205 2685 331 298 443 N ATOM 2096 NE2BHIS C 248 106.410 26.433 33.620 0.50 18.52 N ANISOU 2096 NE2BHIS C 248 2121 2248 2667 324 256 472 N ATOM 2097 N ASP C 249 101.774 24.015 36.233 1.00 18.83 N ANISOU 2097 N ASP C 249 1988 2344 2825 401 315 512 N ATOM 2098 CA ASP C 249 101.304 24.684 37.460 1.00 19.85 C ANISOU 2098 CA ASP C 249 2103 2393 3047 423 457 440 C ATOM 2099 C ASP C 249 101.271 23.845 38.740 1.00 19.24 C ANISOU 2099 C ASP C 249 2070 2369 2872 384 490 335 C ATOM 2100 O ASP C 249 100.848 24.348 39.776 1.00 20.39 O ANISOU 2100 O ASP C 249 2205 2468 3073 384 615 263 O ATOM 2101 CB ASP C 249 99.950 25.402 37.218 1.00 21.73 C ANISOU 2101 CB ASP C 249 2221 2555 3479 489 518 554 C ATOM 2102 CG ASP C 249 98.780 24.447 36.969 1.00 22.24 C ANISOU 2102 CG ASP C 249 2211 2697 3542 495 445 649 C ATOM 2103 OD1 ASP C 249 98.932 23.222 37.126 1.00 21.98 O ANISOU 2103 OD1 ASP C 249 2225 2756 3369 446 369 608 O ATOM 2104 OD2 ASP C 249 97.681 24.939 36.606 1.00 24.35 O ANISOU 2104 OD2 ASP C 249 2360 2927 3964 547 468 773 O ATOM 2105 N THR C 250 101.676 22.571 38.673 1.00 17.61 N ANISOU 2105 N THR C 250 1905 2257 2530 348 390 332 N ATOM 2106 CA THR C 250 101.864 21.743 39.874 1.00 17.09 C ANISOU 2106 CA THR C 250 1881 2251 2360 306 409 259 C ATOM 2107 C THR C 250 103.347 21.428 40.115 1.00 15.98 C ANISOU 2107 C THR C 250 1818 2164 2091 263 368 196 C ATOM 2108 O THR C 250 103.677 20.516 40.872 1.00 15.47 O ANISOU 2108 O THR C 250 1778 2169 1929 229 347 179 O ATOM 2109 CB THR C 250 101.045 20.432 39.801 1.00 17.02 C ANISOU 2109 CB THR C 250 1842 2294 2329 301 346 323 C ATOM 2110 OG1 THR C 250 101.403 19.684 38.632 1.00 16.65 O ANISOU 2110 OG1 THR C 250 1804 2278 2246 292 234 375 O ATOM 2111 CG2 THR C 250 99.549 20.741 39.781 1.00 18.09 C ANISOU 2111 CG2 THR C 250 1888 2395 2590 336 396 383 C ATOM 2112 N GLN C 251 104.225 22.185 39.456 1.00 15.43 N ANISOU 2112 N GLN C 251 1772 2062 2029 265 357 180 N ATOM 2113 CA GLN C 251 105.664 22.116 39.670 1.00 14.95 C ANISOU 2113 CA GLN C 251 1769 2047 1865 225 331 119 C ATOM 2114 C GLN C 251 106.193 23.521 39.931 1.00 15.51 C ANISOU 2114 C GLN C 251 1858 2065 1971 205 420 39 C ATOM 2115 O GLN C 251 105.541 24.511 39.599 1.00 16.10 O ANISOU 2115 O GLN C 251 1901 2044 2173 238 490 52 O ATOM 2116 CB GLN C 251 106.357 21.492 38.452 1.00 14.14 C ANISOU 2116 CB GLN C 251 1678 1962 1731 234 227 170 C ATOM 2117 CG GLN C 251 105.707 20.189 38.001 1.00 13.77 C ANISOU 2117 CG GLN C 251 1610 1944 1680 242 159 235 C ATOM 2118 CD GLN C 251 106.351 19.617 36.770 1.00 13.31 C ANISOU 2118 CD GLN C 251 1564 1899 1594 233 84 257 C ATOM 2119 OE1 GLN C 251 105.765 19.605 35.669 1.00 13.82 O ANISOU 2119 OE1 GLN C 251 1602 1961 1689 232 46 308 O ATOM 2120 NE2 GLN C 251 107.558 19.194 36.919 1.00 12.74 N ANISOU 2120 NE2 GLN C 251 1525 1852 1463 217 66 221 N ATOM 2121 N GLN C 252 107.385 23.588 40.524 1.00 15.74 N ANISOU 2121 N GLN C 252 1930 2155 1897 148 420 -38 N ATOM 2122 CA GLN C 252 108.073 24.841 40.804 1.00 16.61 C ANISOU 2122 CA GLN C 252 2064 2226 2021 103 504 -136 C ATOM 2123 C GLN C 252 109.297 24.866 39.918 1.00 15.90 C ANISOU 2123 C GLN C 252 1996 2150 1896 99 428 -118 C ATOM 2124 O GLN C 252 109.978 23.853 39.786 1.00 15.56 O ANISOU 2124 O GLN C 252 1959 2190 1763 95 335 -82 O ATOM 2125 CB GLN C 252 108.470 24.920 42.279 1.00 17.78 C ANISOU 2125 CB GLN C 252 2234 2466 2055 10 567 -249 C ATOM 2126 CG GLN C 252 107.287 24.835 43.234 1.00 19.10 C ANISOU 2126 CG GLN C 252 2382 2638 2238 -1 654 -279 C ATOM 2127 CD GLN C 252 106.881 23.406 43.587 1.00 19.23 C ANISOU 2127 CD GLN C 252 2382 2752 2173 12 569 -192 C ATOM 2128 OE1 GLN C 252 107.716 22.580 43.984 1.00 20.03 O ANISOU 2128 OE1 GLN C 252 2494 2972 2144 -26 488 -164 O ATOM 2129 NE2 GLN C 252 105.599 23.107 43.441 1.00 19.80 N ANISOU 2129 NE2 GLN C 252 2419 2771 2334 67 589 -136 N ATOM 2130 N TRP C 253 109.559 26.013 39.303 1.00 16.22 N ANISOU 2130 N TRP C 253 2041 2099 2023 103 479 -135 N ATOM 2131 CA TRP C 253 110.487 26.101 38.177 1.00 15.68 C ANISOU 2131 CA TRP C 253 1984 2026 1946 111 412 -94 C ATOM 2132 C TRP C 253 111.611 27.070 38.440 1.00 16.20 C ANISOU 2132 C TRP C 253 2079 2080 1996 46 468 -190 C ATOM 2133 O TRP C 253 111.371 28.218 38.815 1.00 17.39 O ANISOU 2133 O TRP C 253 2233 2140 2235 23 587 -258 O ATOM 2134 CB TRP C 253 109.745 26.561 36.920 1.00 15.70 C ANISOU 2134 CB TRP C 253 1956 1939 2071 174 403 16 C ATOM 2135 CG TRP C 253 108.712 25.606 36.538 1.00 15.28 C ANISOU 2135 CG TRP C 253 1868 1916 2022 218 337 108 C ATOM 2136 CD1 TRP C 253 107.418 25.599 36.948 1.00 15.64 C ANISOU 2136 CD1 TRP C 253 1872 1927 2144 253 379 140 C ATOM 2137 CD2 TRP C 253 108.880 24.471 35.692 1.00 14.46 C ANISOU 2137 CD2 TRP C 253 1765 1885 1844 222 227 167 C ATOM 2138 NE1 TRP C 253 106.757 24.522 36.401 1.00 15.28 N ANISOU 2138 NE1 TRP C 253 1799 1937 2069 274 291 223 N ATOM 2139 CE2 TRP C 253 107.635 23.812 35.628 1.00 14.56 C ANISOU 2139 CE2 TRP C 253 1737 1908 1886 250 202 232 C ATOM 2140 CE3 TRP C 253 109.962 23.944 34.983 1.00 14.03 C ANISOU 2140 CE3 TRP C 253 1737 1884 1710 197 161 161 C ATOM 2141 CZ2 TRP C 253 107.436 22.660 34.857 1.00 14.14 C ANISOU 2141 CZ2 TRP C 253 1676 1917 1781 243 114 281 C ATOM 2142 CZ3 TRP C 253 109.772 22.799 34.233 1.00 13.58 C ANISOU 2142 CZ3 TRP C 253 1672 1878 1609 196 86 204 C ATOM 2143 CH2 TRP C 253 108.516 22.165 34.178 1.00 13.75 C ANISOU 2143 CH2 TRP C 253 1659 1909 1656 214 64 258 C ATOM 2144 N GLY C 254 112.837 26.609 38.218 1.00 15.70 N ANISOU 2144 N GLY C 254 2030 2101 1835 15 395 -198 N ATOM 2145 CA GLY C 254 113.968 27.499 38.201 1.00 16.22 C ANISOU 2145 CA GLY C 254 2115 2160 1889 -48 432 -273 C ATOM 2146 C GLY C 254 114.064 28.212 36.878 1.00 16.47 C ANISOU 2146 C GLY C 254 2147 2093 2019 -13 438 -209 C ATOM 2147 O GLY C 254 113.556 27.742 35.854 1.00 16.20 O ANISOU 2147 O GLY C 254 2097 2046 2013 49 375 -99 O ATOM 2148 N AASP C 255 114.715 29.368 36.891 0.50 17.23 N ANISOU 2148 N AASP C 255 2258 2128 2161 -65 516 -276 N ATOM 2149 N BASP C 255 114.739 29.350 36.898 0.50 17.26 N ANISOU 2149 N BASP C 255 2262 2134 2161 -66 514 -277 N ATOM 2150 CA AASP C 255 115.126 30.022 35.662 0.50 17.42 C ANISOU 2150 CA AASP C 255 2282 2081 2255 -49 514 -210 C ATOM 2151 CA BASP C 255 115.146 30.030 35.692 0.50 17.48 C ANISOU 2151 CA BASP C 255 2291 2090 2261 -52 515 -213 C ATOM 2152 C AASP C 255 116.262 29.209 35.048 0.50 16.68 C ANISOU 2152 C AASP C 255 2193 2100 2046 -65 410 -189 C ATOM 2153 C BASP C 255 116.279 29.223 35.058 0.50 16.72 C ANISOU 2153 C BASP C 255 2198 2105 2051 -66 411 -191 C ATOM 2154 O AASP C 255 116.803 28.300 35.684 0.50 16.14 O ANISOU 2154 O AASP C 255 2120 2144 1869 -87 355 -231 O ATOM 2155 O BASP C 255 116.834 28.322 35.693 0.50 16.21 O ANISOU 2155 O BASP C 255 2128 2152 1877 -89 357 -233 O ATOM 2156 CB AASP C 255 115.592 31.452 35.946 0.50 18.72 C ANISOU 2156 CB AASP C 255 2462 2141 2509 -112 640 -299 C ATOM 2157 CB BASP C 255 115.612 31.434 36.065 0.50 18.83 C ANISOU 2157 CB BASP C 255 2477 2161 2515 -118 643 -311 C ATOM 2158 CG AASP C 255 114.454 32.376 36.352 0.50 19.92 C ANISOU 2158 CG AASP C 255 2601 2140 2828 -86 774 -311 C ATOM 2159 CG BASP C 255 115.498 32.413 34.925 0.50 19.58 C ANISOU 2159 CG BASP C 255 2561 2124 2755 -84 686 -212 C ATOM 2160 OD1AASP C 255 113.281 32.051 36.078 0.50 20.14 O ANISOU 2160 OD1AASP C 255 2597 2134 2923 -4 756 -207 O ATOM 2161 OD1BASP C 255 115.289 31.971 33.777 0.50 19.40 O ANISOU 2161 OD1BASP C 255 2521 2127 2724 -28 597 -72 O ATOM 2162 OD2AASP C 255 114.743 33.442 36.931 0.50 21.28 O ANISOU 2162 OD2AASP C 255 2788 2220 3076 -154 908 -429 O ATOM 2163 OD2BASP C 255 115.623 33.624 35.185 0.50 20.97 O ANISOU 2163 OD2BASP C 255 2743 2172 3050 -124 815 -276 O ATOM 2164 N VAL C 256 116.589 29.515 33.798 1.00 16.67 N ANISOU 2164 N VAL C 256 2190 2067 2075 -52 388 -114 N ATOM 2165 CA VAL C 256 117.742 28.918 33.114 1.00 16.54 C ANISOU 2165 CA VAL C 256 2175 2140 1970 -75 319 -110 C ATOM 2166 C VAL C 256 118.826 29.989 33.161 1.00 17.36 C ANISOU 2166 C VAL C 256 2289 2213 2094 -144 382 -176 C ATOM 2167 O VAL C 256 118.732 30.997 32.456 1.00 18.57 O ANISOU 2167 O VAL C 256 2448 2271 2337 -147 434 -128 O ATOM 2168 CB VAL C 256 117.396 28.521 31.669 1.00 16.44 C ANISOU 2168 CB VAL C 256 2154 2136 1954 -39 262 6 C ATOM 2169 CG1 VAL C 256 118.614 27.939 30.954 1.00 16.36 C ANISOU 2169 CG1 VAL C 256 2146 2209 1862 -71 219 -12 C ATOM 2170 CG2 VAL C 256 116.243 27.531 31.670 1.00 16.21 C ANISOU 2170 CG2 VAL C 256 2112 2134 1912 13 210 59 C ATOM 2171 N LEU C 257 119.833 29.777 34.007 1.00 17.36 N ANISOU 2171 N LEU C 257 2283 2297 2014 -204 375 -274 N ATOM 2172 CA LEU C 257 120.811 30.814 34.331 1.00 18.26 C ANISOU 2172 CA LEU C 257 2402 2395 2140 -294 443 -365 C ATOM 2173 C LEU C 257 122.212 30.420 33.879 1.00 18.02 C ANISOU 2173 C LEU C 257 2348 2463 2035 -329 389 -372 C ATOM 2174 O LEU C 257 122.591 29.261 34.015 1.00 17.04 O ANISOU 2174 O LEU C 257 2193 2447 1834 -305 311 -353 O ATOM 2175 CB LEU C 257 120.835 31.070 35.835 1.00 19.19 C ANISOU 2175 CB LEU C 257 2520 2554 2217 -368 492 -489 C ATOM 2176 CG LEU C 257 119.572 31.688 36.431 1.00 20.00 C ANISOU 2176 CG LEU C 257 2644 2544 2409 -355 587 -523 C ATOM 2177 CD1 LEU C 257 119.685 31.803 37.944 1.00 20.93 C ANISOU 2177 CD1 LEU C 257 2763 2742 2447 -454 636 -664 C ATOM 2178 CD2 LEU C 257 119.271 33.044 35.808 1.00 21.01 C ANISOU 2178 CD2 LEU C 257 2789 2491 2704 -354 701 -512 C ATOM 2179 N PRO C 258 122.992 31.393 33.365 1.00 18.74 N ANISOU 2179 N PRO C 258 2446 2509 2167 -387 441 -395 N ATOM 2180 CA PRO C 258 124.394 31.107 33.052 1.00 19.01 C ANISOU 2180 CA PRO C 258 2446 2641 2135 -432 403 -415 C ATOM 2181 C PRO C 258 125.208 30.883 34.329 1.00 19.69 C ANISOU 2181 C PRO C 258 2491 2853 2137 -509 384 -509 C ATOM 2182 O PRO C 258 124.892 31.465 35.371 1.00 20.60 O ANISOU 2182 O PRO C 258 2619 2960 2246 -572 435 -595 O ATOM 2183 CB PRO C 258 124.852 32.373 32.330 1.00 19.70 C ANISOU 2183 CB PRO C 258 2553 2634 2299 -486 481 -419 C ATOM 2184 CG PRO C 258 124.000 33.455 32.879 1.00 20.48 C ANISOU 2184 CG PRO C 258 2686 2598 2499 -506 580 -459 C ATOM 2185 CD PRO C 258 122.675 32.824 33.192 1.00 19.82 C ANISOU 2185 CD PRO C 258 2610 2496 2423 -420 551 -411 C ATOM 2186 N ASP C 259 126.254 30.067 34.236 1.00 19.71 N ANISOU 2186 N ASP C 259 2435 2977 2075 -511 316 -490 N ATOM 2187 CA ASP C 259 127.048 29.666 35.404 1.00 20.61 C ANISOU 2187 CA ASP C 259 2483 3247 2101 -577 271 -533 C ATOM 2188 C ASP C 259 128.473 30.224 35.453 1.00 22.05 C ANISOU 2188 C ASP C 259 2613 3511 2255 -681 280 -588 C ATOM 2189 O ASP C 259 129.263 29.809 36.306 1.00 23.06 O ANISOU 2189 O ASP C 259 2661 3797 2303 -738 225 -596 O ATOM 2190 CB ASP C 259 127.087 28.142 35.519 1.00 19.90 C ANISOU 2190 CB ASP C 259 2336 3246 1977 -491 181 -442 C ATOM 2191 CG ASP C 259 127.727 27.468 34.308 1.00 19.21 C ANISOU 2191 CG ASP C 259 2219 3146 1933 -426 162 -380 C ATOM 2192 OD1 ASP C 259 128.527 28.100 33.586 1.00 19.52 O ANISOU 2192 OD1 ASP C 259 2254 3168 1993 -468 197 -406 O ATOM 2193 OD2 ASP C 259 127.421 26.291 34.107 1.00 18.84 O ANISOU 2193 OD2 ASP C 259 2151 3104 1902 -340 122 -312 O ATOM 2194 N GLY C 260 128.818 31.136 34.548 1.00 22.65 N ANISOU 2194 N GLY C 260 2720 3490 2394 -710 345 -610 N ATOM 2195 CA GLY C 260 130.176 31.702 34.521 1.00 23.81 C ANISOU 2195 CA GLY C 260 2816 3708 2524 -816 361 -665 C ATOM 2196 C GLY C 260 131.251 30.844 33.857 1.00 23.93 C ANISOU 2196 C GLY C 260 2749 3813 2528 -775 303 -596 C ATOM 2197 O GLY C 260 132.385 31.305 33.706 1.00 25.01 O ANISOU 2197 O GLY C 260 2836 4005 2661 -856 320 -631 O ATOM 2198 N ASN C 261 130.907 29.611 33.459 1.00 23.23 N ANISOU 2198 N ASN C 261 2645 3733 2449 -656 250 -507 N ATOM 2199 CA ASN C 261 131.818 28.717 32.736 1.00 23.35 C ANISOU 2199 CA ASN C 261 2584 3803 2486 -605 224 -450 C ATOM 2200 C ASN C 261 131.322 28.465 31.320 1.00 22.05 C ANISOU 2200 C ASN C 261 2481 3528 2369 -531 260 -413 C ATOM 2201 O ASN C 261 131.750 27.502 30.683 1.00 22.41 O ANISOU 2201 O ASN C 261 2480 3595 2439 -473 255 -376 O ATOM 2202 CB ASN C 261 131.958 27.380 33.478 1.00 24.31 C ANISOU 2202 CB ASN C 261 2616 4027 2592 -540 148 -381 C ATOM 2203 CG ASN C 261 132.551 27.538 34.863 1.00 26.14 C ANISOU 2203 CG ASN C 261 2766 4416 2751 -629 95 -393 C ATOM 2204 OD1 ASN C 261 132.111 26.892 35.820 1.00 27.84 O ANISOU 2204 OD1 ASN C 261 2951 4703 2923 -608 38 -346 O ATOM 2205 ND2 ASN C 261 133.536 28.417 34.986 1.00 27.49 N ANISOU 2205 ND2 ASN C 261 2896 4654 2896 -744 114 -454 N ATOM 2206 N GLY C 262 130.442 29.340 30.825 1.00 20.88 N ANISOU 2206 N GLY C 262 2427 3267 2237 -542 305 -419 N ATOM 2207 CA GLY C 262 129.891 29.231 29.478 1.00 19.84 C ANISOU 2207 CA GLY C 262 2351 3061 2126 -496 330 -369 C ATOM 2208 C GLY C 262 128.717 28.280 29.326 1.00 18.44 C ANISOU 2208 C GLY C 262 2205 2856 1944 -408 294 -320 C ATOM 2209 O GLY C 262 128.264 28.048 28.206 1.00 18.36 O ANISOU 2209 O GLY C 262 2231 2816 1929 -386 306 -281 O ATOM 2210 N THR C 263 128.211 27.735 30.432 1.00 17.33 N ANISOU 2210 N THR C 263 2051 2740 1795 -372 251 -322 N ATOM 2211 CA THR C 263 127.110 26.779 30.395 1.00 16.19 C ANISOU 2211 CA THR C 263 1930 2570 1652 -294 218 -280 C ATOM 2212 C THR C 263 125.964 27.297 31.254 1.00 15.74 C ANISOU 2212 C THR C 263 1917 2466 1597 -289 214 -280 C ATOM 2213 O THR C 263 126.025 28.424 31.739 1.00 16.05 O ANISOU 2213 O THR C 263 1975 2477 1647 -348 251 -322 O ATOM 2214 CB THR C 263 127.583 25.358 30.775 1.00 16.05 C ANISOU 2214 CB THR C 263 1840 2617 1642 -241 182 -264 C ATOM 2215 OG1 THR C 263 128.392 25.386 31.955 1.00 16.53 O ANISOU 2215 OG1 THR C 263 1828 2766 1687 -271 153 -273 O ATOM 2216 CG2 THR C 263 128.415 24.753 29.651 1.00 16.28 C ANISOU 2216 CG2 THR C 263 1834 2655 1695 -233 217 -270 C ATOM 2217 N TYR C 264 124.902 26.509 31.376 1.00 15.13 N ANISOU 2217 N TYR C 264 1857 2369 1522 -225 184 -242 N ATOM 2218 CA TYR C 264 123.682 26.922 32.051 1.00 15.20 C ANISOU 2218 CA TYR C 264 1904 2326 1544 -211 189 -236 C ATOM 2219 C TYR C 264 123.247 25.882 33.064 1.00 14.51 C ANISOU 2219 C TYR C 264 1792 2289 1434 -171 145 -226 C ATOM 2220 O TYR C 264 123.665 24.724 33.012 1.00 13.76 O ANISOU 2220 O TYR C 264 1653 2242 1331 -135 109 -199 O ATOM 2221 CB TYR C 264 122.573 27.097 31.017 1.00 15.61 C ANISOU 2221 CB TYR C 264 2001 2302 1630 -176 198 -173 C ATOM 2222 CG TYR C 264 122.805 28.255 30.083 1.00 16.80 C ANISOU 2222 CG TYR C 264 2175 2399 1811 -216 242 -150 C ATOM 2223 CD1 TYR C 264 122.333 29.520 30.403 1.00 17.76 C ANISOU 2223 CD1 TYR C 264 2319 2430 2001 -236 299 -148 C ATOM 2224 CD2 TYR C 264 123.471 28.088 28.868 1.00 17.61 C ANISOU 2224 CD2 TYR C 264 2272 2534 1884 -238 241 -127 C ATOM 2225 CE1 TYR C 264 122.530 30.600 29.563 1.00 19.00 C ANISOU 2225 CE1 TYR C 264 2489 2523 2208 -269 346 -103 C ATOM 2226 CE2 TYR C 264 123.671 29.170 28.018 1.00 18.63 C ANISOU 2226 CE2 TYR C 264 2419 2622 2037 -281 281 -85 C ATOM 2227 CZ TYR C 264 123.188 30.418 28.374 1.00 19.35 C ANISOU 2227 CZ TYR C 264 2528 2615 2208 -291 330 -62 C ATOM 2228 OH TYR C 264 123.363 31.511 27.562 1.00 21.43 O ANISOU 2228 OH TYR C 264 2802 2822 2520 -329 377 1 O ATOM 2229 N GLN C 265 122.376 26.312 33.974 1.00 14.50 N ANISOU 2229 N GLN C 265 1814 2265 1432 -179 161 -243 N ATOM 2230 CA GLN C 265 121.749 25.423 34.920 1.00 14.56 C ANISOU 2230 CA GLN C 265 1804 2315 1412 -146 126 -222 C ATOM 2231 C GLN C 265 120.306 25.827 35.182 1.00 13.79 C ANISOU 2231 C GLN C 265 1749 2141 1348 -124 158 -219 C ATOM 2232 O GLN C 265 119.913 26.992 35.042 1.00 14.06 O ANISOU 2232 O GLN C 265 1816 2096 1431 -148 220 -248 O ATOM 2233 CB GLN C 265 122.524 25.405 36.237 1.00 15.94 C ANISOU 2233 CB GLN C 265 1932 2606 1517 -208 108 -258 C ATOM 2234 CG GLN C 265 122.711 26.759 36.877 1.00 17.53 C ANISOU 2234 CG GLN C 265 2156 2809 1697 -306 169 -355 C ATOM 2235 CD GLN C 265 123.578 26.669 38.114 1.00 18.96 C ANISOU 2235 CD GLN C 265 2280 3148 1777 -395 140 -390 C ATOM 2236 OE1 GLN C 265 123.138 26.975 39.227 1.00 21.15 O ANISOU 2236 OE1 GLN C 265 2565 3477 1993 -460 164 -446 O ATOM 2237 NE2 GLN C 265 124.806 26.211 37.931 1.00 19.68 N ANISOU 2237 NE2 GLN C 265 2301 3329 1846 -404 88 -353 N ATOM 2238 N THR C 266 119.518 24.836 35.564 1.00 12.96 N ANISOU 2238 N THR C 266 1636 2054 1235 -76 124 -176 N ATOM 2239 CA THR C 266 118.131 25.053 35.941 1.00 12.75 C ANISOU 2239 CA THR C 266 1634 1970 1240 -52 152 -168 C ATOM 2240 C THR C 266 117.663 23.904 36.817 1.00 12.36 C ANISOU 2240 C THR C 266 1562 1982 1152 -27 113 -135 C ATOM 2241 O THR C 266 118.442 22.989 37.137 1.00 12.36 O ANISOU 2241 O THR C 266 1523 2062 1112 -25 66 -107 O ATOM 2242 CB THR C 266 117.238 25.202 34.680 1.00 12.42 C ANISOU 2242 CB THR C 266 1612 1840 1266 -4 154 -107 C ATOM 2243 OG1 THR C 266 115.951 25.723 35.040 1.00 12.66 O ANISOU 2243 OG1 THR C 266 1652 1805 1354 17 197 -95 O ATOM 2244 CG2 THR C 266 117.097 23.877 33.932 1.00 11.99 C ANISOU 2244 CG2 THR C 266 1545 1812 1197 37 95 -53 C ATOM 2245 N TRP C 267 116.399 23.963 37.217 1.00 12.22 N ANISOU 2245 N TRP C 267 1559 1924 1160 -6 140 -127 N ATOM 2246 CA TRP C 267 115.821 22.933 38.058 1.00 12.36 C ANISOU 2246 CA TRP C 267 1557 1993 1145 13 112 -90 C ATOM 2247 C TRP C 267 114.306 22.951 37.972 1.00 12.26 C ANISOU 2247 C TRP C 267 1559 1910 1191 52 139 -66 C ATOM 2248 O TRP C 267 113.712 23.929 37.519 1.00 12.31 O ANISOU 2248 O TRP C 267 1580 1834 1263 60 189 -79 O ATOM 2249 CB TRP C 267 116.269 23.113 39.524 1.00 13.04 C ANISOU 2249 CB TRP C 267 1627 2187 1141 -59 126 -136 C ATOM 2250 CG TRP C 267 115.956 24.467 40.111 1.00 13.71 C ANISOU 2250 CG TRP C 267 1740 2244 1224 -125 217 -240 C ATOM 2251 CD1 TRP C 267 116.771 25.559 40.117 1.00 14.25 C ANISOU 2251 CD1 TRP C 267 1821 2309 1285 -195 264 -326 C ATOM 2252 CD2 TRP C 267 114.738 24.873 40.747 1.00 14.09 C ANISOU 2252 CD2 TRP C 267 1805 2248 1300 -132 292 -279 C ATOM 2253 NE1 TRP C 267 116.146 26.621 40.724 1.00 14.95 N ANISOU 2253 NE1 TRP C 267 1937 2343 1402 -247 372 -425 N ATOM 2254 CE2 TRP C 267 114.894 26.228 41.122 1.00 14.99 C ANISOU 2254 CE2 TRP C 267 1943 2322 1432 -206 395 -398 C ATOM 2255 CE3 TRP C 267 113.530 24.228 41.037 1.00 14.02 C ANISOU 2255 CE3 TRP C 267 1791 2223 1313 -85 294 -231 C ATOM 2256 CZ2 TRP C 267 113.884 26.945 41.767 1.00 15.74 C ANISOU 2256 CZ2 TRP C 267 2052 2351 1577 -230 510 -475 C ATOM 2257 CZ3 TRP C 267 112.530 24.945 41.682 1.00 14.79 C ANISOU 2257 CZ3 TRP C 267 1899 2271 1449 -107 396 -297 C ATOM 2258 CH2 TRP C 267 112.715 26.291 42.029 1.00 15.65 C ANISOU 2258 CH2 TRP C 267 2029 2330 1587 -176 508 -420 C ATOM 2259 N VAL C 268 113.692 21.854 38.409 1.00 12.15 N ANISOU 2259 N VAL C 268 1528 1926 1164 79 109 -16 N ATOM 2260 CA VAL C 268 112.249 21.771 38.558 1.00 12.36 C ANISOU 2260 CA VAL C 268 1554 1907 1236 107 135 8 C ATOM 2261 C VAL C 268 111.946 20.907 39.777 1.00 12.72 C ANISOU 2261 C VAL C 268 1581 2026 1226 94 128 29 C ATOM 2262 O VAL C 268 112.614 19.899 40.017 1.00 12.63 O ANISOU 2262 O VAL C 268 1549 2075 1176 97 76 77 O ATOM 2263 CB VAL C 268 111.548 21.252 37.268 1.00 11.96 C ANISOU 2263 CB VAL C 268 1498 1799 1247 154 98 69 C ATOM 2264 CG1 VAL C 268 111.977 19.839 36.902 1.00 11.74 C ANISOU 2264 CG1 VAL C 268 1459 1799 1203 167 43 106 C ATOM 2265 CG2 VAL C 268 110.032 21.321 37.418 1.00 12.10 C ANISOU 2265 CG2 VAL C 268 1499 1777 1320 179 125 101 C ATOM 2266 N ALA C 269 110.940 21.315 40.540 1.00 13.43 N ANISOU 2266 N ALA C 269 1672 2107 1322 81 187 3 N ATOM 2267 CA ALA C 269 110.576 20.615 41.768 1.00 14.18 C ANISOU 2267 CA ALA C 269 1752 2286 1351 54 191 23 C ATOM 2268 C ALA C 269 109.094 20.330 41.809 1.00 14.42 C ANISOU 2268 C ALA C 269 1771 2264 1443 89 222 53 C ATOM 2269 O ALA C 269 108.310 21.004 41.149 1.00 14.44 O ANISOU 2269 O ALA C 269 1772 2176 1537 122 260 42 O ATOM 2270 CB ALA C 269 110.980 21.433 42.979 1.00 15.10 C ANISOU 2270 CB ALA C 269 1876 2488 1373 -36 251 -66 C ATOM 2271 N THR C 270 108.710 19.324 42.577 1.00 15.04 N ANISOU 2271 N THR C 270 1831 2404 1480 81 205 108 N ATOM 2272 CA THR C 270 107.302 19.092 42.855 1.00 15.56 C ANISOU 2272 CA THR C 270 1881 2439 1592 98 246 127 C ATOM 2273 C THR C 270 107.175 18.462 44.234 1.00 16.74 C ANISOU 2273 C THR C 270 2018 2698 1644 46 260 153 C ATOM 2274 O THR C 270 108.139 17.884 44.757 1.00 16.65 O ANISOU 2274 O THR C 270 1998 2782 1547 15 209 200 O ATOM 2275 CB THR C 270 106.626 18.255 41.735 1.00 15.02 C ANISOU 2275 CB THR C 270 1796 2297 1615 157 194 200 C ATOM 2276 OG1 THR C 270 105.202 18.370 41.840 1.00 15.37 O ANISOU 2276 OG1 THR C 270 1814 2303 1721 172 241 210 O ATOM 2277 CG2 THR C 270 107.042 16.798 41.783 1.00 14.85 C ANISOU 2277 CG2 THR C 270 1765 2305 1575 163 133 277 C ATOM 2278 N ARG C 271 105.997 18.630 44.828 1.00 18.16 N ANISOU 2278 N ARG C 271 2187 2872 1841 34 332 133 N ATOM 2279 CA ARG C 271 105.736 18.166 46.190 1.00 20.01 C ANISOU 2279 CA ARG C 271 2410 3223 1970 -31 363 150 C ATOM 2280 C ARG C 271 104.921 16.888 46.143 1.00 19.72 C ANISOU 2280 C ARG C 271 2344 3169 1978 6 328 262 C ATOM 2281 O ARG C 271 103.899 16.838 45.472 1.00 19.39 O ANISOU 2281 O ARG C 271 2288 3031 2047 56 344 268 O ATOM 2282 CB ARG C 271 105.005 19.241 46.987 1.00 22.08 C ANISOU 2282 CB ARG C 271 2678 3494 2217 -87 494 31 C ATOM 2283 CG ARG C 271 105.916 20.387 47.393 1.00 23.91 C ANISOU 2283 CG ARG C 271 2939 3773 2374 -164 547 -94 C ATOM 2284 CD ARG C 271 105.230 21.367 48.329 1.00 26.33 C ANISOU 2284 CD ARG C 271 3252 4090 2661 -242 705 -236 C ATOM 2285 NE ARG C 271 104.488 22.397 47.601 1.00 27.47 N ANISOU 2285 NE ARG C 271 3391 4056 2991 -176 801 -303 N ATOM 2286 CZ ARG C 271 105.023 23.469 47.009 1.00 28.23 C ANISOU 2286 CZ ARG C 271 3505 4058 3163 -166 840 -378 C ATOM 2287 NH1 ARG C 271 106.339 23.687 47.017 1.00 28.99 N ANISOU 2287 NH1 ARG C 271 3632 4223 3159 -224 789 -414 N ATOM 2288 NH2 ARG C 271 104.228 24.338 46.384 1.00 29.04 N ANISOU 2288 NH2 ARG C 271 3585 3994 3456 -97 931 -402 N ATOM 2289 N ILE C 272 105.383 15.854 46.851 1.00 20.13 N ANISOU 2289 N ILE C 272 2380 3316 1952 -22 279 361 N ATOM 2290 CA ILE C 272 104.732 14.546 46.849 1.00 20.31 C ANISOU 2290 CA ILE C 272 2375 3312 2029 7 252 477 C ATOM 2291 C ILE C 272 104.541 14.038 48.275 1.00 21.66 C ANISOU 2291 C ILE C 272 2525 3621 2086 -64 274 548 C ATOM 2292 O ILE C 272 105.097 14.593 49.223 1.00 22.41 O ANISOU 2292 O ILE C 272 2623 3855 2037 -144 293 515 O ATOM 2293 CB ILE C 272 105.510 13.520 45.989 1.00 19.93 C ANISOU 2293 CB ILE C 272 2317 3198 2057 63 170 566 C ATOM 2294 CG1 ILE C 272 106.861 13.147 46.611 1.00 20.62 C ANISOU 2294 CG1 ILE C 272 2383 3390 2063 39 118 648 C ATOM 2295 CG2 ILE C 272 105.689 14.061 44.568 1.00 18.96 C ANISOU 2295 CG2 ILE C 272 2218 2966 2022 112 152 488 C ATOM 2296 CD1 ILE C 272 107.663 12.166 45.783 1.00 20.51 C ANISOU 2296 CD1 ILE C 272 2347 3291 2154 101 63 729 C ATOM 2297 N CYS C 273 103.746 12.981 48.401 1.00 22.31 N ANISOU 2297 N CYS C 273 2581 3673 2224 -47 274 645 N ATOM 2298 CA CYS C 273 103.498 12.339 49.692 1.00 23.95 C ANISOU 2298 CA CYS C 273 2761 4008 2329 -113 291 745 C ATOM 2299 C CYS C 273 104.507 11.233 49.955 1.00 23.98 C ANISOU 2299 C CYS C 273 2729 4062 2321 -104 210 919 C ATOM 2300 O CYS C 273 104.978 10.590 49.021 1.00 23.04 O ANISOU 2300 O CYS C 273 2602 3822 2329 -30 162 968 O ATOM 2301 CB CYS C 273 102.100 11.741 49.714 1.00 24.86 C ANISOU 2301 CB CYS C 273 2860 4059 2528 -101 340 775 C ATOM 2302 SG CYS C 273 100.783 12.970 49.653 1.00 26.80 S ANISOU 2302 SG CYS C 273 3115 4264 2804 -110 452 609 S ATOM 2303 N ARG C 274 104.805 11.000 51.235 1.00 24.95 N ANISOU 2303 N ARG C 274 2821 4365 2293 -186 203 1019 N ATOM 2304 CA ARG C 274 105.655 9.883 51.665 1.00 25.60 C ANISOU 2304 CA ARG C 274 2843 4512 2372 -179 128 1235 C ATOM 2305 C ARG C 274 105.135 8.564 51.092 1.00 25.18 C ANISOU 2305 C ARG C 274 2767 4286 2514 -98 129 1352 C ATOM 2306 O ARG C 274 103.931 8.312 51.108 1.00 25.16 O ANISOU 2306 O ARG C 274 2777 4223 2559 -103 185 1327 O ATOM 2307 CB ARG C 274 105.702 9.795 53.200 1.00 27.37 C ANISOU 2307 CB ARG C 274 3029 4978 2392 -298 128 1343 C ATOM 2308 N GLY C 275 106.046 7.754 50.556 1.00 25.17 N ANISOU 2308 N GLY C 275 2729 4199 2637 -28 77 1467 N ATOM 2309 CA GLY C 275 105.707 6.476 49.939 1.00 25.16 C ANISOU 2309 CA GLY C 275 2706 4012 2844 41 95 1560 C ATOM 2310 C GLY C 275 105.408 6.541 48.453 1.00 23.87 C ANISOU 2310 C GLY C 275 2590 3649 2832 101 119 1403 C ATOM 2311 O GLY C 275 105.282 5.504 47.814 1.00 24.34 O ANISOU 2311 O GLY C 275 2633 3548 3067 145 143 1448 O ATOM 2312 N GLU C 276 105.282 7.746 47.898 1.00 22.67 N ANISOU 2312 N GLU C 276 2490 3508 2614 93 120 1220 N ATOM 2313 CA GLU C 276 104.955 7.906 46.482 1.00 21.53 C ANISOU 2313 CA GLU C 276 2385 3213 2584 133 133 1083 C ATOM 2314 C GLU C 276 106.180 8.036 45.597 1.00 20.31 C ANISOU 2314 C GLU C 276 2236 3004 2479 177 99 1046 C ATOM 2315 O GLU C 276 106.032 8.101 44.380 1.00 18.95 O ANISOU 2315 O GLU C 276 2092 2720 2388 199 108 941 O ATOM 2316 CB GLU C 276 104.061 9.135 46.286 1.00 21.71 C ANISOU 2316 CB GLU C 276 2448 3266 2536 107 158 931 C ATOM 2317 CG GLU C 276 102.767 9.053 47.066 1.00 23.00 C ANISOU 2317 CG GLU C 276 2600 3472 2668 66 209 948 C ATOM 2318 CD GLU C 276 101.915 7.895 46.605 1.00 23.90 C ANISOU 2318 CD GLU C 276 2694 3469 2919 76 229 997 C ATOM 2319 OE1 GLU C 276 101.437 7.962 45.459 1.00 24.41 O ANISOU 2319 OE1 GLU C 276 2770 3435 3068 91 229 907 O ATOM 2320 OE2 GLU C 276 101.742 6.921 47.370 1.00 26.17 O ANISOU 2320 OE2 GLU C 276 2950 3768 3226 58 245 1128 O ATOM 2321 N GLU C 277 107.372 8.041 46.188 1.00 20.37 N ANISOU 2321 N GLU C 277 2206 3100 2433 182 60 1139 N ATOM 2322 CA GLU C 277 108.611 8.332 45.463 1.00 19.76 C ANISOU 2322 CA GLU C 277 2126 2996 2386 219 30 1100 C ATOM 2323 C GLU C 277 108.833 7.464 44.239 1.00 19.00 C ANISOU 2323 C GLU C 277 2028 2716 2474 272 58 1077 C ATOM 2324 O GLU C 277 109.250 7.970 43.207 1.00 17.85 O ANISOU 2324 O GLU C 277 1915 2521 2347 285 57 957 O ATOM 2325 CB GLU C 277 109.837 8.204 46.374 1.00 21.12 C ANISOU 2325 CB GLU C 277 2231 3299 2496 214 -20 1247 C ATOM 2326 CG GLU C 277 109.947 9.274 47.453 1.00 21.71 C ANISOU 2326 CG GLU C 277 2312 3585 2354 132 -49 1226 C ATOM 2327 CD GLU C 277 109.359 8.848 48.783 1.00 23.12 C ANISOU 2327 CD GLU C 277 2456 3893 2436 74 -47 1357 C ATOM 2328 OE1 GLU C 277 108.397 8.044 48.806 1.00 23.42 O ANISOU 2328 OE1 GLU C 277 2495 3842 2561 91 -8 1409 O ATOM 2329 OE2 GLU C 277 109.877 9.301 49.824 1.00 24.75 O ANISOU 2329 OE2 GLU C 277 2631 4304 2470 -3 -83 1411 O ATOM 2330 N GLN C 278 108.542 6.168 44.351 1.00 19.39 N ANISOU 2330 N GLN C 278 2040 2664 2662 293 96 1185 N ATOM 2331 CA GLN C 278 108.751 5.230 43.241 1.00 19.44 C ANISOU 2331 CA GLN C 278 2042 2482 2861 328 152 1147 C ATOM 2332 C GLN C 278 107.902 5.534 42.000 1.00 18.28 C ANISOU 2332 C GLN C 278 1963 2258 2725 293 179 956 C ATOM 2333 O GLN C 278 108.228 5.065 40.909 1.00 18.59 O ANISOU 2333 O GLN C 278 2011 2177 2877 297 222 873 O ATOM 2334 CB GLN C 278 108.528 3.785 43.695 1.00 20.76 C ANISOU 2334 CB GLN C 278 2153 2541 3194 348 206 1301 C ATOM 2335 N ARG C 279 106.830 6.311 42.155 1.00 17.33 N ANISOU 2335 N ARG C 279 1880 2215 2491 252 158 891 N ATOM 2336 CA ARG C 279 106.003 6.705 41.021 1.00 16.49 C ANISOU 2336 CA ARG C 279 1816 2070 2380 215 165 743 C ATOM 2337 C ARG C 279 106.552 7.905 40.260 1.00 15.57 C ANISOU 2337 C ARG C 279 1735 2003 2179 217 128 637 C ATOM 2338 O ARG C 279 106.112 8.168 39.139 1.00 14.98 O ANISOU 2338 O ARG C 279 1686 1901 2107 186 128 533 O ATOM 2339 CB ARG C 279 104.585 7.015 41.495 1.00 16.34 C ANISOU 2339 CB ARG C 279 1801 2104 2303 179 165 740 C ATOM 2340 CG ARG C 279 103.908 5.834 42.169 1.00 17.18 C ANISOU 2340 CG ARG C 279 1875 2159 2492 165 207 840 C ATOM 2341 CD ARG C 279 102.579 6.235 42.765 1.00 17.11 C ANISOU 2341 CD ARG C 279 1862 2222 2417 130 211 842 C ATOM 2342 NE ARG C 279 101.595 6.552 41.723 1.00 16.65 N ANISOU 2342 NE ARG C 279 1813 2140 2372 93 209 729 N ATOM 2343 CZ ARG C 279 100.415 7.117 41.951 1.00 16.75 C ANISOU 2343 CZ ARG C 279 1810 2211 2342 70 211 712 C ATOM 2344 NH1 ARG C 279 100.038 7.462 43.182 1.00 17.06 N ANISOU 2344 NH1 ARG C 279 1836 2330 2317 75 230 772 N ATOM 2345 NH2 ARG C 279 99.602 7.345 40.927 1.00 16.49 N ANISOU 2345 NH2 ARG C 279 1767 2168 2329 35 197 635 N ATOM 2346 N PHE C 280 107.513 8.631 40.840 1.00 15.51 N ANISOU 2346 N PHE C 280 1722 2078 2092 243 96 669 N ATOM 2347 CA PHE C 280 107.968 9.899 40.267 1.00 14.93 C ANISOU 2347 CA PHE C 280 1681 2056 1937 240 67 575 C ATOM 2348 C PHE C 280 109.315 9.793 39.577 1.00 15.04 C ANISOU 2348 C PHE C 280 1690 2033 1990 263 64 552 C ATOM 2349 O PHE C 280 110.243 9.186 40.105 1.00 15.78 O ANISOU 2349 O PHE C 280 1741 2124 2130 295 67 640 O ATOM 2350 CB PHE C 280 107.972 10.996 41.335 1.00 14.79 C ANISOU 2350 CB PHE C 280 1667 2158 1794 230 47 588 C ATOM 2351 CG PHE C 280 106.611 11.548 41.595 1.00 14.58 C ANISOU 2351 CG PHE C 280 1653 2155 1733 206 65 555 C ATOM 2352 CD1 PHE C 280 105.722 10.868 42.405 1.00 15.16 C ANISOU 2352 CD1 PHE C 280 1704 2237 1817 192 88 622 C ATOM 2353 CD2 PHE C 280 106.171 12.704 40.956 1.00 14.09 C ANISOU 2353 CD2 PHE C 280 1615 2093 1647 201 67 468 C ATOM 2354 CE1 PHE C 280 104.436 11.344 42.614 1.00 15.23 C ANISOU 2354 CE1 PHE C 280 1713 2263 1812 173 116 591 C ATOM 2355 CE2 PHE C 280 104.888 13.184 41.168 1.00 14.21 C ANISOU 2355 CE2 PHE C 280 1622 2115 1662 190 94 452 C ATOM 2356 CZ PHE C 280 104.018 12.500 41.998 1.00 14.82 C ANISOU 2356 CZ PHE C 280 1675 2207 1749 176 120 507 C ATOM 2357 N THR C 281 109.402 10.378 38.386 1.00 14.72 N ANISOU 2357 N THR C 281 1684 1973 1936 246 62 445 N ATOM 2358 CA THR C 281 110.649 10.427 37.633 1.00 15.08 C ANISOU 2358 CA THR C 281 1729 1993 2007 258 68 403 C ATOM 2359 C THR C 281 110.823 11.811 37.015 1.00 14.81 C ANISOU 2359 C THR C 281 1732 2016 1879 239 39 325 C ATOM 2360 O THR C 281 109.834 12.510 36.763 1.00 14.25 O ANISOU 2360 O THR C 281 1685 1970 1761 215 25 294 O ATOM 2361 CB THR C 281 110.673 9.398 36.493 1.00 15.46 C ANISOU 2361 CB THR C 281 1781 1932 2163 238 123 340 C ATOM 2362 OG1 THR C 281 109.530 9.610 35.652 1.00 15.18 O ANISOU 2362 OG1 THR C 281 1778 1900 2089 178 118 262 O ATOM 2363 CG2 THR C 281 110.652 7.966 37.019 1.00 16.38 C ANISOU 2363 CG2 THR C 281 1854 1953 2416 262 176 418 C ATOM 2364 N ACYS C 282 112.069 12.215 36.791 0.50 14.62 N ANISOU 2364 N ACYS C 282 1703 2011 1841 251 34 308 N ATOM 2365 N BCYS C 282 112.096 12.158 36.789 0.50 15.83 N ANISOU 2365 N BCYS C 282 1854 2161 1999 252 35 309 N ATOM 2366 CA ACYS C 282 112.371 13.477 36.126 0.50 14.23 C ANISOU 2366 CA ACYS C 282 1686 2001 1719 231 16 240 C ATOM 2367 CA BCYS C 282 112.556 13.343 36.068 0.50 16.27 C ANISOU 2367 CA BCYS C 282 1940 2253 1988 233 19 240 C ATOM 2368 C ACYS C 282 112.849 13.175 34.709 0.50 14.54 C ANISOU 2368 C ACYS C 282 1739 1993 1792 207 41 168 C ATOM 2369 C BCYS C 282 112.773 13.004 34.638 0.50 15.72 C ANISOU 2369 C BCYS C 282 1887 2133 1952 205 46 166 C ATOM 2370 O ACYS C 282 113.842 12.463 34.528 0.50 14.78 O ANISOU 2370 O ACYS C 282 1743 1984 1890 224 74 165 O ATOM 2371 O BCYS C 282 113.586 12.125 34.365 0.50 16.00 O ANISOU 2371 O BCYS C 282 1899 2116 2066 218 86 157 O ATOM 2372 CB ACYS C 282 113.427 14.274 36.899 0.50 14.01 C ANISOU 2372 CB ACYS C 282 1644 2045 1636 241 -4 260 C ATOM 2373 CB BCYS C 282 113.971 13.696 36.496 0.50 17.84 C ANISOU 2373 CB BCYS C 282 2113 2496 2170 252 9 260 C ATOM 2374 SG ACYS C 282 114.001 15.732 35.987 0.50 13.54 S ANISOU 2374 SG ACYS C 282 1620 2007 1518 213 -9 179 S ATOM 2375 SG BCYS C 282 114.152 14.734 37.915 0.50 20.17 S ANISOU 2375 SG BCYS C 282 2398 2902 2362 240 -24 296 S ATOM 2376 N TYR C 283 112.142 13.729 33.725 1.00 14.64 N ANISOU 2376 N TYR C 283 1784 2020 1761 163 31 118 N ATOM 2377 CA TYR C 283 112.456 13.571 32.308 1.00 15.12 C ANISOU 2377 CA TYR C 283 1861 2070 1814 111 53 42 C ATOM 2378 C TYR C 283 113.156 14.815 31.801 1.00 15.01 C ANISOU 2378 C TYR C 283 1864 2105 1732 101 33 25 C ATOM 2379 O TYR C 283 112.774 15.932 32.157 1.00 14.60 O ANISOU 2379 O TYR C 283 1821 2088 1638 113 1 61 O ATOM 2380 CB TYR C 283 111.186 13.324 31.512 1.00 15.25 C ANISOU 2380 CB TYR C 283 1888 2101 1806 48 43 18 C ATOM 2381 CG TYR C 283 111.414 13.204 30.025 1.00 15.83 C ANISOU 2381 CG TYR C 283 1978 2200 1835 -36 63 -65 C ATOM 2382 CD1 TYR C 283 111.980 12.057 29.474 1.00 16.43 C ANISOU 2382 CD1 TYR C 283 2056 2219 1969 -75 137 -153 C ATOM 2383 CD2 TYR C 283 111.078 14.249 29.168 1.00 15.87 C ANISOU 2383 CD2 TYR C 283 1994 2291 1746 -84 17 -52 C ATOM 2384 CE1 TYR C 283 112.183 11.946 28.113 1.00 17.29 C ANISOU 2384 CE1 TYR C 283 2183 2367 2018 -175 170 -250 C ATOM 2385 CE2 TYR C 283 111.267 14.145 27.800 1.00 16.73 C ANISOU 2385 CE2 TYR C 283 2116 2455 1786 -182 30 -120 C ATOM 2386 CZ TYR C 283 111.833 12.994 27.274 1.00 17.29 C ANISOU 2386 CZ TYR C 283 2196 2481 1892 -234 109 -232 C ATOM 2387 OH TYR C 283 112.048 12.856 25.928 1.00 18.52 O ANISOU 2387 OH TYR C 283 2368 2704 1966 -352 140 -323 O ATOM 2388 N AMET C 284 114.187 14.602 30.972 0.50 14.88 N ANISOU 2388 N AMET C 284 1851 2081 1722 77 69 -34 N ATOM 2389 N BMET C 284 114.147 14.620 30.941 0.50 16.15 N ANISOU 2389 N BMET C 284 2013 2243 1880 75 68 -35 N ATOM 2390 CA AMET C 284 115.059 15.654 30.438 0.50 14.52 C ANISOU 2390 CA AMET C 284 1818 2076 1622 62 62 -53 C ATOM 2391 CA BMET C 284 114.891 15.727 30.394 0.50 16.57 C ANISOU 2391 CA BMET C 284 2081 2341 1875 58 57 -50 C ATOM 2392 C AMET C 284 115.200 15.463 28.928 0.50 15.29 C ANISOU 2392 C AMET C 284 1935 2197 1679 -18 92 -127 C ATOM 2393 C BMET C 284 115.192 15.480 28.938 0.50 16.49 C ANISOU 2393 C BMET C 284 2086 2348 1829 -17 91 -126 C ATOM 2394 O AMET C 284 115.352 14.331 28.477 0.50 15.99 O ANISOU 2394 O AMET C 284 2018 2245 1813 -47 150 -194 O ATOM 2395 O BMET C 284 115.472 14.349 28.547 0.50 17.07 O ANISOU 2395 O BMET C 284 2152 2379 1955 -40 152 -192 O ATOM 2396 CB AMET C 284 116.438 15.548 31.107 0.50 14.12 C ANISOU 2396 CB AMET C 284 1735 2012 1618 109 83 -47 C ATOM 2397 CB BMET C 284 116.186 15.879 31.151 0.50 17.76 C ANISOU 2397 CB BMET C 284 2205 2485 2057 106 69 -38 C ATOM 2398 CG AMET C 284 117.429 16.649 30.741 0.50 13.68 C ANISOU 2398 CG AMET C 284 1686 1998 1514 93 80 -66 C ATOM 2399 CG BMET C 284 116.894 17.176 30.844 0.50 18.62 C ANISOU 2399 CG BMET C 284 2328 2638 2110 88 57 -47 C ATOM 2400 SD AMET C 284 118.244 16.423 29.149 0.50 13.75 S ANISOU 2400 SD AMET C 284 1705 2009 1510 31 138 -153 S ATOM 2401 SD BMET C 284 118.462 17.084 31.683 0.50 21.02 S ANISOU 2401 SD BMET C 284 2581 2951 2453 127 70 -37 S ATOM 2402 CE AMET C 284 119.197 14.946 29.488 0.50 14.59 C ANISOU 2402 CE AMET C 284 1752 2043 1750 78 210 -177 C ATOM 2403 CE BMET C 284 119.073 15.686 30.730 0.50 21.34 C ANISOU 2403 CE BMET C 284 2596 2934 2577 122 141 -93 C ATOM 2404 N GLU C 285 115.116 16.545 28.149 1.00 15.77 N ANISOU 2404 N GLU C 285 2015 2321 1655 -62 63 -114 N ATOM 2405 CA GLU C 285 115.514 16.525 26.732 1.00 16.39 C ANISOU 2405 CA GLU C 285 2109 2451 1666 -152 92 -177 C ATOM 2406 C GLU C 285 116.431 17.681 26.518 1.00 15.32 C ANISOU 2406 C GLU C 285 1980 2344 1496 -147 86 -156 C ATOM 2407 O GLU C 285 116.123 18.793 26.927 1.00 14.39 O ANISOU 2407 O GLU C 285 1864 2235 1368 -116 42 -78 O ATOM 2408 CB GLU C 285 114.375 16.747 25.734 1.00 17.81 C ANISOU 2408 CB GLU C 285 2298 2719 1752 -241 50 -153 C ATOM 2409 CG GLU C 285 113.266 15.745 25.760 1.00 18.89 C ANISOU 2409 CG GLU C 285 2425 2851 1900 -275 46 -173 C ATOM 2410 CD GLU C 285 112.372 15.787 24.527 1.00 20.36 C ANISOU 2410 CD GLU C 285 2608 3160 1969 -402 10 -170 C ATOM 2411 OE1 GLU C 285 111.429 14.984 24.479 1.00 21.50 O ANISOU 2411 OE1 GLU C 285 2740 3317 2114 -450 5 -194 O ATOM 2412 OE2 GLU C 285 112.592 16.611 23.603 1.00 22.48 O ANISOU 2412 OE2 GLU C 285 2878 3525 2139 -464 -16 -135 O ATOM 2413 N HIS C 286 117.516 17.431 25.797 1.00 15.02 N ANISOU 2413 N HIS C 286 1944 2317 1447 -187 144 -231 N ATOM 2414 CA HIS C 286 118.463 18.472 25.478 1.00 14.86 C ANISOU 2414 CA HIS C 286 1927 2327 1392 -197 148 -218 C ATOM 2415 C HIS C 286 119.229 18.078 24.239 1.00 15.93 C ANISOU 2415 C HIS C 286 2069 2504 1479 -284 217 -310 C ATOM 2416 O HIS C 286 119.799 16.998 24.197 1.00 16.30 O ANISOU 2416 O HIS C 286 2099 2503 1591 -281 292 -401 O ATOM 2417 CB HIS C 286 119.436 18.673 26.642 1.00 13.84 C ANISOU 2417 CB HIS C 286 1770 2145 1343 -114 156 -207 C ATOM 2418 CG HIS C 286 120.406 19.785 26.410 1.00 13.42 C ANISOU 2418 CG HIS C 286 1718 2120 1262 -130 162 -198 C ATOM 2419 ND1 HIS C 286 121.679 19.572 25.923 1.00 13.67 N ANISOU 2419 ND1 HIS C 286 1728 2160 1306 -152 221 -260 N ATOM 2420 CD2 HIS C 286 120.274 21.125 26.548 1.00 12.98 C ANISOU 2420 CD2 HIS C 286 1677 2075 1178 -134 129 -137 C ATOM 2421 CE1 HIS C 286 122.285 20.733 25.772 1.00 13.63 C ANISOU 2421 CE1 HIS C 286 1728 2181 1268 -174 215 -236 C ATOM 2422 NE2 HIS C 286 121.461 21.693 26.150 1.00 13.11 N ANISOU 2422 NE2 HIS C 286 1687 2111 1184 -163 163 -163 N ATOM 2423 N SER C 287 119.226 18.950 23.226 1.00 16.91 N ANISOU 2423 N SER C 287 2212 2715 1496 -363 201 -282 N ATOM 2424 CA SER C 287 120.033 18.763 22.013 1.00 18.21 C ANISOU 2424 CA SER C 287 2385 2943 1589 -462 272 -369 C ATOM 2425 C SER C 287 119.879 17.386 21.366 1.00 19.65 C ANISOU 2425 C SER C 287 2573 3131 1763 -540 350 -504 C ATOM 2426 O SER C 287 120.854 16.743 20.976 1.00 20.48 O ANISOU 2426 O SER C 287 2668 3208 1907 -567 456 -621 O ATOM 2427 CB SER C 287 121.500 19.062 22.315 1.00 18.24 C ANISOU 2427 CB SER C 287 2368 2903 1659 -417 325 -401 C ATOM 2428 OG SER C 287 121.656 20.402 22.744 1.00 17.86 O ANISOU 2428 OG SER C 287 2321 2858 1606 -379 268 -299 O ATOM 2429 N GLY C 288 118.635 16.942 21.267 1.00 20.20 N ANISOU 2429 N GLY C 288 2652 3231 1792 -580 308 -491 N ATOM 2430 CA GLY C 288 118.319 15.668 20.639 1.00 21.85 C ANISOU 2430 CA GLY C 288 2869 3447 1986 -677 386 -629 C ATOM 2431 C GLY C 288 118.535 14.428 21.493 1.00 22.24 C ANISOU 2431 C GLY C 288 2899 3341 2211 -594 463 -706 C ATOM 2432 O GLY C 288 118.311 13.318 21.007 1.00 24.03 O ANISOU 2432 O GLY C 288 3131 3543 2456 -675 552 -836 O ATOM 2433 N ASN C 289 118.949 14.596 22.752 1.00 21.71 N ANISOU 2433 N ASN C 289 2804 3175 2272 -446 435 -624 N ATOM 2434 CA ASN C 289 119.169 13.485 23.667 1.00 22.13 C ANISOU 2434 CA ASN C 289 2821 3089 2497 -355 494 -647 C ATOM 2435 C ASN C 289 118.112 13.585 24.745 1.00 20.97 C ANISOU 2435 C ASN C 289 2672 2922 2373 -282 397 -533 C ATOM 2436 O ASN C 289 117.500 14.644 24.923 1.00 20.18 O ANISOU 2436 O ASN C 289 2589 2894 2185 -275 296 -438 O ATOM 2437 CB ASN C 289 120.567 13.555 24.293 1.00 22.98 C ANISOU 2437 CB ASN C 289 2879 3129 2723 -255 534 -625 C ATOM 2438 CG ASN C 289 121.687 13.486 23.261 1.00 24.81 C ANISOU 2438 CG ASN C 289 3103 3376 2948 -321 643 -738 C ATOM 2439 OD1 ASN C 289 121.615 12.736 22.286 1.00 26.70 O ANISOU 2439 OD1 ASN C 289 3360 3611 3175 -423 748 -876 O ATOM 2440 ND2 ASN C 289 122.737 14.270 23.481 1.00 25.17 N ANISOU 2440 ND2 ASN C 289 3120 3443 3002 -274 629 -692 N ATOM 2441 N HIS C 290 117.884 12.486 25.457 1.00 20.64 N ANISOU 2441 N HIS C 290 2606 2775 2463 -229 437 -540 N ATOM 2442 CA HIS C 290 116.924 12.475 26.558 1.00 19.62 C ANISOU 2442 CA HIS C 290 2471 2625 2360 -161 359 -435 C ATOM 2443 C HIS C 290 117.318 11.456 27.606 1.00 19.53 C ANISOU 2443 C HIS C 290 2410 2492 2520 -65 407 -400 C ATOM 2444 O HIS C 290 118.092 10.537 27.337 1.00 20.61 O ANISOU 2444 O HIS C 290 2516 2539 2778 -60 517 -468 O ATOM 2445 CB HIS C 290 115.507 12.180 26.048 1.00 19.96 C ANISOU 2445 CB HIS C 290 2541 2711 2331 -250 333 -461 C ATOM 2446 CG HIS C 290 115.361 10.807 25.479 1.00 21.19 C ANISOU 2446 CG HIS C 290 2697 2797 2556 -326 443 -589 C ATOM 2447 ND1 HIS C 290 115.037 9.717 26.254 1.00 21.64 N ANISOU 2447 ND1 HIS C 290 2730 2733 2758 -275 489 -580 N ATOM 2448 CD2 HIS C 290 115.553 10.338 24.225 1.00 22.44 C ANISOU 2448 CD2 HIS C 290 2876 2982 2667 -457 532 -739 C ATOM 2449 CE1 HIS C 290 115.006 8.639 25.497 1.00 22.66 C ANISOU 2449 CE1 HIS C 290 2866 2799 2943 -368 608 -724 C ATOM 2450 NE2 HIS C 290 115.322 8.984 24.262 1.00 23.47 N ANISOU 2450 NE2 HIS C 290 2996 2995 2925 -485 640 -833 N ATOM 2451 N SER C 291 116.754 11.613 28.791 1.00 18.70 N ANISOU 2451 N SER C 291 2291 2384 2430 7 334 -286 N ATOM 2452 CA SER C 291 116.993 10.689 29.888 1.00 18.83 C ANISOU 2452 CA SER C 291 2254 2309 2591 93 361 -213 C ATOM 2453 C SER C 291 115.855 10.774 30.882 1.00 17.81 C ANISOU 2453 C SER C 291 2132 2202 2435 121 287 -120 C ATOM 2454 O SER C 291 115.112 11.758 30.917 1.00 16.86 O ANISOU 2454 O SER C 291 2046 2163 2195 98 211 -99 O ATOM 2455 CB SER C 291 118.324 10.989 30.586 1.00 19.22 C ANISOU 2455 CB SER C 291 2245 2366 2693 173 353 -139 C ATOM 2456 OG SER C 291 118.309 12.263 31.197 1.00 18.94 O ANISOU 2456 OG SER C 291 2225 2435 2538 186 255 -75 O ATOM 2457 N THR C 292 115.751 9.729 31.689 1.00 17.89 N ANISOU 2457 N THR C 292 2099 2127 2569 172 320 -56 N ATOM 2458 CA THR C 292 114.764 9.639 32.743 1.00 17.59 C ANISOU 2458 CA THR C 292 2059 2105 2519 199 265 39 C ATOM 2459 C THR C 292 115.488 9.230 34.023 1.00 18.07 C ANISOU 2459 C THR C 292 2050 2150 2666 286 257 175 C ATOM 2460 O THR C 292 116.295 8.302 34.002 1.00 18.77 O ANISOU 2460 O THR C 292 2082 2146 2903 326 328 200 O ATOM 2461 CB THR C 292 113.663 8.634 32.372 1.00 18.04 C ANISOU 2461 CB THR C 292 2132 2088 2634 148 314 -10 C ATOM 2462 OG1 THR C 292 112.965 9.117 31.216 1.00 17.90 O ANISOU 2462 OG1 THR C 292 2167 2130 2505 51 300 -116 O ATOM 2463 CG2 THR C 292 112.682 8.456 33.506 1.00 17.98 C ANISOU 2463 CG2 THR C 292 2114 2091 2627 178 269 96 C ATOM 2464 N AHIS C 293 115.175 9.916 35.123 0.50 17.56 N ANISOU 2464 N AHIS C 293 1982 2179 2511 307 176 267 N ATOM 2465 N BHIS C 293 115.203 9.927 35.123 0.50 17.52 N ANISOU 2465 N BHIS C 293 1976 2175 2505 308 176 267 N ATOM 2466 CA AHIS C 293 115.848 9.731 36.408 0.50 18.18 C ANISOU 2466 CA AHIS C 293 1990 2301 2616 364 145 409 C ATOM 2467 CA BHIS C 293 115.858 9.666 36.403 0.50 18.15 C ANISOU 2467 CA BHIS C 293 1985 2292 2621 366 148 411 C ATOM 2468 C AHIS C 293 114.830 9.470 37.508 0.50 17.97 C ANISOU 2468 C AHIS C 293 1960 2305 2561 367 112 502 C ATOM 2469 C BHIS C 293 114.840 9.458 37.501 0.50 17.94 C ANISOU 2469 C BHIS C 293 1956 2300 2559 367 113 503 C ATOM 2470 O AHIS C 293 113.850 10.208 37.609 0.50 16.94 O ANISOU 2470 O AHIS C 293 1884 2229 2322 330 79 459 O ATOM 2471 O BHIS C 293 113.875 10.217 37.593 0.50 16.89 O ANISOU 2471 O BHIS C 293 1879 2223 2317 330 79 458 O ATOM 2472 CB AHIS C 293 116.631 10.990 36.777 0.50 18.17 C ANISOU 2472 CB AHIS C 293 1986 2426 2493 357 82 414 C ATOM 2473 CB BHIS C 293 116.769 10.821 36.800 0.50 18.20 C ANISOU 2473 CB BHIS C 293 1978 2420 2519 365 88 426 C ATOM 2474 CG AHIS C 293 118.041 10.995 36.280 0.50 19.03 C ANISOU 2474 CG AHIS C 293 2047 2524 2659 378 107 401 C ATOM 2475 CG BHIS C 293 118.047 10.862 36.032 0.50 18.88 C ANISOU 2475 CG BHIS C 293 2032 2481 2661 377 124 383 C ATOM 2476 ND1AHIS C 293 119.126 10.861 37.119 0.50 19.94 N ANISOU 2476 ND1AHIS C 293 2071 2701 2805 415 80 520 N ATOM 2477 ND1BHIS C 293 118.157 11.494 34.816 0.50 18.55 N ANISOU 2477 ND1BHIS C 293 2047 2427 2573 335 147 250 N ATOM 2478 CD2AHIS C 293 118.545 11.107 35.029 0.50 19.11 C ANISOU 2478 CD2AHIS C 293 2080 2482 2698 359 160 289 C ATOM 2479 CD2BHIS C 293 119.266 10.335 36.297 0.50 19.88 C ANISOU 2479 CD2BHIS C 293 2065 2596 2891 427 143 465 C ATOM 2480 CE1AHIS C 293 120.236 10.900 36.406 0.50 20.37 C ANISOU 2480 CE1AHIS C 293 2089 2730 2920 429 117 480 C ATOM 2481 CE1BHIS C 293 119.391 11.366 34.367 0.50 18.99 C ANISOU 2481 CE1BHIS C 293 2055 2464 2695 353 186 235 C ATOM 2482 NE2AHIS C 293 119.910 11.056 35.135 0.50 19.97 N ANISOU 2482 NE2AHIS C 293 2113 2608 2867 393 171 333 N ATOM 2483 NE2BHIS C 293 120.085 10.662 35.244 0.50 20.06 N ANISOU 2483 NE2BHIS C 293 2096 2595 2933 414 186 364 N ATOM 2484 N PRO C 294 115.065 8.447 38.356 1.00 18.69 N ANISOU 2484 N PRO C 294 1981 2365 2757 412 127 643 N ATOM 2485 CA PRO C 294 114.180 8.212 39.481 1.00 18.87 C ANISOU 2485 CA PRO C 294 1994 2436 2738 407 96 746 C ATOM 2486 C PRO C 294 114.532 9.115 40.653 1.00 18.67 C ANISOU 2486 C PRO C 294 1947 2587 2558 390 18 822 C ATOM 2487 O PRO C 294 115.556 9.807 40.634 1.00 18.72 O ANISOU 2487 O PRO C 294 1934 2669 2510 388 -13 809 O ATOM 2488 CB PRO C 294 114.463 6.758 39.835 1.00 20.26 C ANISOU 2488 CB PRO C 294 2092 2506 3101 459 149 884 C ATOM 2489 CG PRO C 294 115.906 6.613 39.542 1.00 20.82 C ANISOU 2489 CG PRO C 294 2093 2554 3264 507 167 919 C ATOM 2490 CD PRO C 294 116.156 7.452 38.325 1.00 19.90 C ANISOU 2490 CD PRO C 294 2045 2431 3084 472 179 730 C ATOM 2491 N VAL C 295 113.673 9.096 41.660 1.00 18.78 N ANISOU 2491 N VAL C 295 1965 2671 2499 366 -4 890 N ATOM 2492 CA VAL C 295 113.970 9.698 42.948 1.00 19.17 C ANISOU 2492 CA VAL C 295 1983 2901 2401 329 -63 974 C ATOM 2493 C VAL C 295 114.900 8.700 43.645 1.00 20.76 C ANISOU 2493 C VAL C 295 2072 3131 2686 370 -83 1178 C ATOM 2494 O VAL C 295 114.545 7.527 43.777 1.00 21.57 O ANISOU 2494 O VAL C 295 2136 3137 2924 409 -48 1288 O ATOM 2495 CB VAL C 295 112.697 9.903 43.790 1.00 19.00 C ANISOU 2495 CB VAL C 295 1996 2943 2279 282 -62 977 C ATOM 2496 CG1 VAL C 295 113.035 10.490 45.156 1.00 19.59 C ANISOU 2496 CG1 VAL C 295 2038 3224 2182 218 -110 1048 C ATOM 2497 CG2 VAL C 295 111.710 10.808 43.057 1.00 17.86 C ANISOU 2497 CG2 VAL C 295 1939 2751 2094 257 -36 804 C ATOM 2498 N PRO C 296 116.102 9.144 44.068 1.00 21.53 N ANISOU 2498 N PRO C 296 2105 3358 2717 359 -136 1239 N ATOM 2499 CA PRO C 296 116.967 8.227 44.815 1.00 23.31 C ANISOU 2499 CA PRO C 296 2199 3638 3021 397 -168 1473 C ATOM 2500 C PRO C 296 116.332 7.739 46.102 1.00 24.36 C ANISOU 2500 C PRO C 296 2292 3881 3081 362 -199 1641 C ATOM 2501 O PRO C 296 115.494 8.425 46.699 1.00 24.03 O ANISOU 2501 O PRO C 296 2317 3949 2863 283 -213 1569 O ATOM 2502 CB PRO C 296 118.202 9.076 45.130 1.00 23.80 C ANISOU 2502 CB PRO C 296 2205 3873 2965 358 -236 1486 C ATOM 2503 CG PRO C 296 118.221 10.103 44.067 1.00 22.46 C ANISOU 2503 CG PRO C 296 2134 3640 2758 340 -207 1251 C ATOM 2504 CD PRO C 296 116.780 10.424 43.812 1.00 21.17 C ANISOU 2504 CD PRO C 296 2089 3406 2549 313 -167 1114 C ATOM 2505 N SER C 297 116.731 6.543 46.509 1.00 25.84 N ANISOU 2505 N SER C 297 2367 4031 3420 423 -197 1872 N ATOM 2506 CA SER C 297 116.202 5.932 47.721 1.00 27.09 C ANISOU 2506 CA SER C 297 2472 4294 3527 393 -226 2075 C ATOM 2507 C SER C 297 117.356 5.420 48.566 1.00 29.15 C ANISOU 2507 C SER C 297 2566 4699 3810 411 -298 2360 C ATOM 2508 O SER C 297 117.158 4.643 49.494 1.00 30.72 O ANISOU 2508 O SER C 297 2682 4966 4022 408 -321 2598 O ATOM 2509 CB SER C 297 115.221 4.814 47.367 1.00 27.08 C ANISOU 2509 CB SER C 297 2497 4073 3721 449 -139 2102 C ATOM 2510 OG SER C 297 115.877 3.732 46.729 1.00 28.09 O ANISOU 2510 OG SER C 297 2544 3998 4130 553 -76 2201 O ATOM 2511 OXT SER C 297 118.511 5.793 48.354 1.00 29.69 O ANISOU 2511 OXT SER C 297 2570 4832 3880 423 -338 2372 O TER 2512 SER C 297 ATOM 2513 N ILE B 2 102.473 8.669 15.824 1.00 24.69 N ANISOU 2513 N ILE B 2 3175 2916 3291 -281 468 506 N ATOM 2514 CA ILE B 2 102.768 7.622 16.858 1.00 24.05 C ANISOU 2514 CA ILE B 2 3038 2855 3245 -239 476 450 C ATOM 2515 C ILE B 2 101.917 6.374 16.595 1.00 23.04 C ANISOU 2515 C ILE B 2 2910 2756 3090 -202 468 434 C ATOM 2516 O ILE B 2 100.712 6.477 16.400 1.00 23.59 O ANISOU 2516 O ILE B 2 3012 2809 3143 -179 433 458 O ATOM 2517 CB ILE B 2 102.603 8.188 18.300 1.00 24.12 C ANISOU 2517 CB ILE B 2 3030 2823 3313 -207 442 439 C ATOM 2518 CG1 ILE B 2 103.737 9.192 18.568 1.00 25.05 C ANISOU 2518 CG1 ILE B 2 3136 2922 3461 -247 460 443 C ATOM 2519 CG2 ILE B 2 102.610 7.079 19.351 1.00 23.62 C ANISOU 2519 CG2 ILE B 2 2922 2778 3274 -164 437 393 C ATOM 2520 CD1 ILE B 2 103.467 10.206 19.658 1.00 25.28 C ANISOU 2520 CD1 ILE B 2 3166 2900 3538 -230 422 447 C ATOM 2521 N GLN B 3 102.571 5.212 16.568 1.00 22.03 N ANISOU 2521 N GLN B 3 2742 2666 2961 -196 499 391 N ATOM 2522 CA GLN B 3 101.931 3.928 16.268 1.00 21.18 C ANISOU 2522 CA GLN B 3 2631 2587 2831 -166 495 370 C ATOM 2523 C GLN B 3 102.426 2.875 17.249 1.00 20.16 C ANISOU 2523 C GLN B 3 2450 2466 2742 -134 493 321 C ATOM 2524 O GLN B 3 103.625 2.793 17.513 1.00 19.76 O ANISOU 2524 O GLN B 3 2361 2425 2721 -148 519 292 O ATOM 2525 CB GLN B 3 102.283 3.471 14.854 1.00 21.76 C ANISOU 2525 CB GLN B 3 2714 2703 2851 -201 535 366 C ATOM 2526 N LEU B 4 101.493 2.089 17.783 1.00 19.17 N ANISOU 2526 N LEU B 4 2326 2338 2621 -92 460 313 N ATOM 2527 CA LEU B 4 101.799 0.926 18.613 1.00 18.92 C ANISOU 2527 CA LEU B 4 2256 2313 2621 -64 449 273 C ATOM 2528 C LEU B 4 101.191 -0.280 17.899 1.00 18.74 C ANISOU 2528 C LEU B 4 2239 2314 2567 -48 448 260 C ATOM 2529 O LEU B 4 99.964 -0.378 17.779 1.00 18.80 O ANISOU 2529 O LEU B 4 2277 2318 2549 -31 423 281 O ATOM 2530 CB LEU B 4 101.188 1.096 20.000 1.00 18.56 C ANISOU 2530 CB LEU B 4 2208 2241 2604 -38 407 278 C ATOM 2531 CG LEU B 4 101.658 2.307 20.800 1.00 18.85 C ANISOU 2531 CG LEU B 4 2239 2251 2671 -50 403 287 C ATOM 2532 CD1 LEU B 4 100.827 2.442 22.065 1.00 18.72 C ANISOU 2532 CD1 LEU B 4 2225 2218 2672 -26 363 288 C ATOM 2533 CD2 LEU B 4 103.134 2.219 21.138 1.00 19.16 C ANISOU 2533 CD2 LEU B 4 2238 2296 2748 -66 424 259 C ATOM 2534 N AGLN B 5 102.054 -1.172 17.409 0.50 18.87 N ANISOU 2534 N AGLN B 5 2224 2355 2589 -53 475 221 N ATOM 2535 N BGLN B 5 102.043 -1.175 17.398 0.50 18.87 N ANISOU 2535 N BGLN B 5 2224 2355 2589 -53 475 221 N ATOM 2536 CA AGLN B 5 101.635 -2.321 16.610 0.50 18.99 C ANISOU 2536 CA AGLN B 5 2242 2394 2578 -41 479 200 C ATOM 2537 CA BGLN B 5 101.585 -2.310 16.597 0.50 18.96 C ANISOU 2537 CA BGLN B 5 2240 2390 2573 -41 478 202 C ATOM 2538 C AGLN B 5 101.836 -3.595 17.409 0.50 18.31 C ANISOU 2538 C AGLN B 5 2122 2300 2534 -8 451 163 C ATOM 2539 C BGLN B 5 101.827 -3.605 17.360 0.50 18.31 C ANISOU 2539 C BGLN B 5 2123 2301 2533 -9 452 163 C ATOM 2540 O AGLN B 5 102.967 -3.941 17.738 0.50 18.59 O ANISOU 2540 O AGLN B 5 2116 2336 2613 -8 460 126 O ATOM 2541 O BGLN B 5 102.970 -3.972 17.617 0.50 18.62 O ANISOU 2541 O BGLN B 5 2120 2342 2614 -9 463 125 O ATOM 2542 CB AGLN B 5 102.456 -2.403 15.326 0.50 19.94 C ANISOU 2542 CB AGLN B 5 2352 2551 2673 -75 531 176 C ATOM 2543 CB BGLN B 5 102.299 -2.340 15.244 0.50 19.89 C ANISOU 2543 CB BGLN B 5 2353 2545 2659 -75 529 182 C ATOM 2544 CG AGLN B 5 102.079 -3.590 14.455 0.50 20.54 C ANISOU 2544 CG AGLN B 5 2428 2654 2721 -64 537 147 C ATOM 2545 CG BGLN B 5 101.579 -3.190 14.207 0.50 20.49 C ANISOU 2545 CG BGLN B 5 2448 2648 2690 -71 534 174 C ATOM 2546 CD AGLN B 5 100.645 -3.503 13.964 0.50 20.83 C ANISOU 2546 CD AGLN B 5 2517 2691 2708 -58 514 188 C ATOM 2547 CD BGLN B 5 102.260 -3.185 12.851 0.50 21.44 C ANISOU 2547 CD BGLN B 5 2565 2813 2770 -113 588 151 C ATOM 2548 OE1AGLN B 5 100.032 -2.433 13.994 0.50 21.48 O ANISOU 2548 OE1AGLN B 5 2635 2757 2768 -69 502 237 O ATOM 2549 OE1BGLN B 5 102.651 -2.135 12.337 0.50 22.44 O ANISOU 2549 OE1BGLN B 5 2708 2949 2869 -156 617 177 O ATOM 2550 NE2AGLN B 5 100.103 -4.628 13.508 0.50 21.09 N ANISOU 2550 NE2AGLN B 5 2550 2738 2724 -40 506 165 N ATOM 2551 NE2BGLN B 5 102.393 -4.366 12.258 0.50 21.90 N ANISOU 2551 NE2BGLN B 5 2600 2897 2822 -103 602 102 N ATOM 2552 N GLN B 6 100.742 -4.285 17.727 1.00 17.60 N ANISOU 2552 N GLN B 6 2051 2202 2434 17 415 172 N ATOM 2553 CA GLN B 6 100.815 -5.515 18.510 1.00 17.03 C ANISOU 2553 CA GLN B 6 1955 2117 2398 43 380 146 C ATOM 2554 C GLN B 6 100.888 -6.751 17.648 1.00 17.17 C ANISOU 2554 C GLN B 6 1961 2151 2411 53 387 109 C ATOM 2555 O GLN B 6 100.482 -6.739 16.483 1.00 17.45 O ANISOU 2555 O GLN B 6 2017 2212 2402 42 414 110 O ATOM 2556 CB GLN B 6 99.611 -5.629 19.428 1.00 16.20 C ANISOU 2556 CB GLN B 6 1875 1995 2285 58 336 174 C ATOM 2557 CG GLN B 6 99.472 -4.430 20.331 1.00 15.77 C ANISOU 2557 CG GLN B 6 1829 1926 2237 50 327 202 C ATOM 2558 CD GLN B 6 98.308 -4.564 21.274 1.00 15.14 C ANISOU 2558 CD GLN B 6 1767 1837 2148 61 288 220 C ATOM 2559 OE1 GLN B 6 98.023 -5.645 21.820 1.00 15.62 O ANISOU 2559 OE1 GLN B 6 1824 1895 2217 70 258 210 O ATOM 2560 NE2 GLN B 6 97.626 -3.466 21.487 1.00 14.61 N ANISOU 2560 NE2 GLN B 6 1719 1766 2066 56 288 244 N ATOM 2561 N SER B 7 101.366 -7.829 18.264 1.00 17.29 N ANISOU 2561 N SER B 7 1946 2149 2473 74 358 76 N ATOM 2562 CA SER B 7 101.363 -9.148 17.641 1.00 17.44 C ANISOU 2562 CA SER B 7 1953 2174 2501 90 351 36 C ATOM 2563 C SER B 7 99.941 -9.666 17.495 1.00 17.23 C ANISOU 2563 C SER B 7 1966 2147 2435 99 325 61 C ATOM 2564 O SER B 7 98.981 -9.128 18.089 1.00 16.90 O ANISOU 2564 O SER B 7 1954 2098 2369 96 305 105 O ATOM 2565 CB SER B 7 102.249 -10.132 18.420 1.00 17.69 C ANISOU 2565 CB SER B 7 1943 2176 2602 111 314 -2 C ATOM 2566 OG SER B 7 102.017 -10.042 19.815 1.00 17.21 O ANISOU 2566 OG SER B 7 1892 2085 2562 116 265 30 O ATOM 2567 N GLY B 8 99.817 -10.709 16.682 1.00 17.62 N ANISOU 2567 N GLY B 8 2010 2207 2480 108 327 27 N ATOM 2568 CA GLY B 8 98.526 -11.208 16.264 1.00 17.49 C ANISOU 2568 CA GLY B 8 2028 2197 2422 113 311 44 C ATOM 2569 C GLY B 8 97.778 -12.013 17.312 1.00 17.41 C ANISOU 2569 C GLY B 8 2029 2157 2430 127 252 61 C ATOM 2570 O GLY B 8 98.281 -12.223 18.428 1.00 17.16 O ANISOU 2570 O GLY B 8 1982 2097 2443 133 219 62 O ATOM 2571 N PRO B 9 96.567 -12.474 16.960 1.00 17.44 N ANISOU 2571 N PRO B 9 2062 2168 2398 129 238 75 N ATOM 2572 CA PRO B 9 95.753 -13.250 17.898 1.00 17.25 C ANISOU 2572 CA PRO B 9 2052 2120 2382 134 185 93 C ATOM 2573 C PRO B 9 96.416 -14.583 18.238 1.00 17.53 C ANISOU 2573 C PRO B 9 2065 2124 2472 148 147 58 C ATOM 2574 O PRO B 9 97.174 -15.129 17.423 1.00 18.25 O ANISOU 2574 O PRO B 9 2131 2217 2587 160 163 11 O ATOM 2575 CB PRO B 9 94.439 -13.450 17.135 1.00 17.28 C ANISOU 2575 CB PRO B 9 2086 2146 2334 131 187 105 C ATOM 2576 CG PRO B 9 94.823 -13.374 15.698 1.00 17.61 C ANISOU 2576 CG PRO B 9 2123 2214 2355 131 230 77 C ATOM 2577 CD PRO B 9 95.912 -12.346 15.642 1.00 17.73 C ANISOU 2577 CD PRO B 9 2120 2237 2381 123 268 74 C ATOM 2578 N AGLU B 10 96.089 -15.096 19.420 0.50 17.28 N ANISOU 2578 N AGLU B 10 2043 2063 2459 143 94 81 N ATOM 2579 N BGLU B 10 96.176 -15.083 19.446 0.50 17.47 N ANISOU 2579 N BGLU B 10 2065 2087 2486 144 94 79 N ATOM 2580 CA AGLU B 10 96.718 -16.292 19.958 0.50 17.56 C ANISOU 2580 CA AGLU B 10 2063 2058 2553 154 43 58 C ATOM 2581 CA BGLU B 10 96.769 -16.352 19.872 0.50 17.88 C ANISOU 2581 CA BGLU B 10 2101 2098 2596 156 44 54 C ATOM 2582 C AGLU B 10 95.696 -17.216 20.608 0.50 17.07 C ANISOU 2582 C AGLU B 10 2030 1975 2480 142 -12 85 C ATOM 2583 C BGLU B 10 95.799 -17.225 20.655 0.50 17.27 C ANISOU 2583 C BGLU B 10 2053 1998 2510 142 -14 83 C ATOM 2584 O AGLU B 10 94.780 -16.752 21.291 0.50 16.70 O ANISOU 2584 O AGLU B 10 2009 1943 2395 120 -18 126 O ATOM 2585 O BGLU B 10 95.061 -16.743 21.510 0.50 16.94 O ANISOU 2585 O BGLU B 10 2034 1966 2436 120 -24 125 O ATOM 2586 CB AGLU B 10 97.786 -15.884 20.973 0.50 18.08 C ANISOU 2586 CB AGLU B 10 2105 2101 2662 153 26 62 C ATOM 2587 CB BGLU B 10 98.040 -16.122 20.701 0.50 18.70 C ANISOU 2587 CB BGLU B 10 2175 2177 2754 160 27 45 C ATOM 2588 CG AGLU B 10 99.113 -15.505 20.326 0.50 18.66 C ANISOU 2588 CG AGLU B 10 2137 2182 2771 168 65 17 C ATOM 2589 CG BGLU B 10 99.322 -16.650 20.056 0.50 19.80 C ANISOU 2589 CG BGLU B 10 2269 2302 2951 184 35 -16 C ATOM 2590 CD AGLU B 10 99.887 -16.732 19.881 0.50 19.78 C ANISOU 2590 CD AGLU B 10 2246 2296 2973 193 41 -39 C ATOM 2591 CD BGLU B 10 100.222 -15.565 19.475 0.50 20.21 C ANISOU 2591 CD BGLU B 10 2292 2386 3002 183 99 -38 C ATOM 2592 OE1AGLU B 10 99.878 -17.058 18.669 0.50 20.37 O ANISOU 2592 OE1AGLU B 10 2310 2391 3038 202 75 -80 O ATOM 2593 OE1BGLU B 10 100.786 -14.771 20.255 0.50 20.35 O ANISOU 2593 OE1BGLU B 10 2300 2399 3034 175 99 -20 O ATOM 2594 OE2AGLU B 10 100.470 -17.393 20.756 0.50 20.71 O ANISOU 2594 OE2AGLU B 10 2351 2370 3149 201 -18 -45 O ATOM 2595 OE2BGLU B 10 100.415 -15.525 18.240 0.50 20.87 O ANISOU 2595 OE2BGLU B 10 2361 2499 3069 187 148 -75 O ATOM 2596 N LEU B 11 95.837 -18.515 20.337 1.00 17.02 N ANISOU 2596 N LEU B 11 2019 1939 2510 154 -50 57 N ATOM 2597 CA LEU B 11 95.133 -19.575 21.064 1.00 16.67 C ANISOU 2597 CA LEU B 11 2000 1862 2470 139 -114 80 C ATOM 2598 C LEU B 11 96.206 -20.278 21.869 1.00 16.82 C ANISOU 2598 C LEU B 11 2003 1828 2561 147 -174 70 C ATOM 2599 O LEU B 11 97.201 -20.736 21.300 1.00 17.07 O ANISOU 2599 O LEU B 11 1999 1837 2648 177 -175 19 O ATOM 2600 CB LEU B 11 94.515 -20.569 20.085 1.00 16.65 C ANISOU 2600 CB LEU B 11 2006 1857 2462 148 -120 54 C ATOM 2601 CG LEU B 11 93.901 -21.842 20.678 1.00 16.74 C ANISOU 2601 CG LEU B 11 2043 1828 2489 132 -190 71 C ATOM 2602 CD1 LEU B 11 92.786 -21.538 21.669 1.00 16.44 C ANISOU 2602 CD1 LEU B 11 2040 1806 2398 91 -206 129 C ATOM 2603 CD2 LEU B 11 93.412 -22.730 19.548 1.00 17.03 C ANISOU 2603 CD2 LEU B 11 2082 1864 2524 146 -188 36 C ATOM 2604 N VAL B 12 96.006 -20.355 23.178 1.00 16.33 N ANISOU 2604 N VAL B 12 1962 1745 2496 119 -223 114 N ATOM 2605 CA VAL B 12 96.960 -21.001 24.076 1.00 17.03 C ANISOU 2605 CA VAL B 12 2042 1780 2650 121 -292 114 C ATOM 2606 C VAL B 12 96.227 -21.965 25.001 1.00 16.92 C ANISOU 2606 C VAL B 12 2070 1733 2627 86 -367 158 C ATOM 2607 O VAL B 12 95.102 -21.700 25.433 1.00 16.86 O ANISOU 2607 O VAL B 12 2094 1755 2554 48 -358 198 O ATOM 2608 CB VAL B 12 97.751 -19.945 24.872 1.00 17.17 C ANISOU 2608 CB VAL B 12 2043 1806 2673 116 -280 128 C ATOM 2609 CG1 VAL B 12 98.807 -20.601 25.751 1.00 17.94 C ANISOU 2609 CG1 VAL B 12 2129 1847 2842 121 -356 126 C ATOM 2610 CG2 VAL B 12 98.397 -18.941 23.915 1.00 17.35 C ANISOU 2610 CG2 VAL B 12 2030 1866 2698 142 -202 90 C ATOM 2611 N LYS B 13 96.873 -23.085 25.307 1.00 17.27 N ANISOU 2611 N LYS B 13 2110 1712 2738 96 -444 147 N ATOM 2612 CA LYS B 13 96.260 -24.103 26.141 1.00 17.59 C ANISOU 2612 CA LYS B 13 2194 1713 2775 57 -524 191 C ATOM 2613 C LYS B 13 96.274 -23.671 27.611 1.00 17.58 C ANISOU 2613 C LYS B 13 2219 1714 2747 11 -559 247 C ATOM 2614 O LYS B 13 97.198 -22.982 28.046 1.00 17.63 O ANISOU 2614 O LYS B 13 2201 1720 2776 22 -554 242 O ATOM 2615 CB LYS B 13 96.929 -25.464 25.927 1.00 18.41 C ANISOU 2615 CB LYS B 13 2289 1741 2967 84 -602 161 C ATOM 2616 CG LYS B 13 96.533 -26.062 24.580 1.00 18.71 C ANISOU 2616 CG LYS B 13 2313 1782 3013 114 -572 111 C ATOM 2617 CD LYS B 13 97.108 -27.429 24.308 1.00 19.37 C ANISOU 2617 CD LYS B 13 2385 1789 3186 143 -649 73 C ATOM 2618 CE LYS B 13 96.779 -27.864 22.891 1.00 19.41 C ANISOU 2618 CE LYS B 13 2372 1809 3196 175 -606 14 C ATOM 2619 NZ LYS B 13 95.325 -28.090 22.674 1.00 18.99 N ANISOU 2619 NZ LYS B 13 2362 1784 3070 139 -592 47 N ATOM 2620 N PRO B 14 95.236 -24.055 28.376 1.00 17.73 N ANISOU 2620 N PRO B 14 2286 1739 2713 -46 -593 299 N ATOM 2621 CA PRO B 14 95.194 -23.804 29.813 1.00 17.98 C ANISOU 2621 CA PRO B 14 2346 1773 2711 -100 -633 352 C ATOM 2622 C PRO B 14 96.446 -24.303 30.520 1.00 18.45 C ANISOU 2622 C PRO B 14 2400 1766 2842 -92 -717 358 C ATOM 2623 O PRO B 14 96.920 -25.410 30.240 1.00 18.72 O ANISOU 2623 O PRO B 14 2433 1733 2946 -68 -784 343 O ATOM 2624 CB PRO B 14 93.962 -24.585 30.285 1.00 18.40 C ANISOU 2624 CB PRO B 14 2450 1829 2712 -162 -671 396 C ATOM 2625 CG PRO B 14 93.124 -24.756 29.094 1.00 18.27 C ANISOU 2625 CG PRO B 14 2426 1837 2678 -140 -620 367 C ATOM 2626 CD PRO B 14 94.027 -24.750 27.904 1.00 17.95 C ANISOU 2626 CD PRO B 14 2340 1775 2704 -67 -593 307 C ATOM 2627 N GLY B 15 96.985 -23.465 31.406 1.00 18.52 N ANISOU 2627 N GLY B 15 2404 1792 2839 -108 -715 376 N ATOM 2628 CA GLY B 15 98.174 -23.787 32.173 1.00 19.25 C ANISOU 2628 CA GLY B 15 2491 1827 2995 -102 -795 385 C ATOM 2629 C GLY B 15 99.484 -23.377 31.518 1.00 19.37 C ANISOU 2629 C GLY B 15 2446 1827 3089 -34 -770 326 C ATOM 2630 O GLY B 15 100.515 -23.377 32.177 1.00 20.38 O ANISOU 2630 O GLY B 15 2560 1918 3267 -27 -825 328 O ATOM 2631 N ALA B 16 99.448 -23.016 30.233 1.00 18.81 N ANISOU 2631 N ALA B 16 2337 1785 3025 12 -690 273 N ATOM 2632 CA ALA B 16 100.645 -22.622 29.490 1.00 18.87 C ANISOU 2632 CA ALA B 16 2283 1786 3099 71 -656 211 C ATOM 2633 C ALA B 16 100.826 -21.107 29.637 1.00 18.33 C ANISOU 2633 C ALA B 16 2197 1778 2988 66 -577 212 C ATOM 2634 O ALA B 16 100.100 -20.469 30.412 1.00 18.01 O ANISOU 2634 O ALA B 16 2191 1776 2878 20 -562 257 O ATOM 2635 CB ALA B 16 100.519 -23.038 28.030 1.00 19.08 C ANISOU 2635 CB ALA B 16 2284 1817 3149 114 -611 154 C ATOM 2636 N ASER B 17 101.802 -20.554 28.918 0.50 18.26 N ANISOU 2636 N ASER B 17 2135 1779 3024 109 -529 158 N ATOM 2637 N BSER B 17 101.789 -20.546 28.911 0.50 18.48 N ANISOU 2637 N BSER B 17 2164 1808 3052 109 -528 159 N ATOM 2638 CA ASER B 17 102.108 -19.122 28.949 0.50 17.95 C ANISOU 2638 CA ASER B 17 2075 1790 2956 107 -456 154 C ATOM 2639 CA BSER B 17 102.068 -19.113 28.953 0.50 18.32 C ANISOU 2639 CA BSER B 17 2123 1837 2999 106 -455 156 C ATOM 2640 C ASER B 17 102.049 -18.540 27.546 0.50 17.81 C ANISOU 2640 C ASER B 17 2028 1814 2924 136 -363 110 C ATOM 2641 C BSER B 17 102.077 -18.540 27.548 0.50 18.03 C ANISOU 2641 C BSER B 17 2056 1842 2954 137 -363 109 C ATOM 2642 O ASER B 17 101.984 -19.276 26.563 0.50 17.98 O ANISOU 2642 O ASER B 17 2037 1825 2969 162 -356 73 O ATOM 2643 O BSER B 17 102.081 -19.280 26.566 0.50 18.22 O ANISOU 2643 O BSER B 17 2064 1853 3005 164 -358 71 O ATOM 2644 CB ASER B 17 103.497 -18.866 29.539 0.50 18.30 C ANISOU 2644 CB ASER B 17 2082 1807 3065 122 -490 136 C ATOM 2645 CB BSER B 17 103.400 -18.834 29.653 0.50 18.89 C ANISOU 2645 CB BSER B 17 2162 1883 3133 117 -492 144 C ATOM 2646 OG ASER B 17 103.605 -19.344 30.869 0.50 18.36 O ANISOU 2646 OG ASER B 17 2119 1775 3082 91 -581 181 O ATOM 2647 OG BSER B 17 104.492 -19.368 28.926 0.50 19.68 O ANISOU 2647 OG BSER B 17 2209 1950 3319 165 -503 81 O ATOM 2648 N VAL B 18 102.068 -17.212 27.469 1.00 17.60 N ANISOU 2648 N VAL B 18 1994 1835 2860 128 -294 114 N ATOM 2649 CA VAL B 18 102.099 -16.499 26.187 1.00 17.75 C ANISOU 2649 CA VAL B 18 1989 1895 2861 148 -207 79 C ATOM 2650 C VAL B 18 102.849 -15.182 26.350 1.00 17.76 C ANISOU 2650 C VAL B 18 1964 1921 2863 145 -160 74 C ATOM 2651 O VAL B 18 102.840 -14.597 27.428 1.00 17.13 O ANISOU 2651 O VAL B 18 1898 1842 2767 121 -178 108 O ATOM 2652 CB VAL B 18 100.664 -16.252 25.643 1.00 17.61 C ANISOU 2652 CB VAL B 18 2009 1916 2766 132 -164 104 C ATOM 2653 CG1 VAL B 18 99.922 -15.202 26.457 1.00 17.26 C ANISOU 2653 CG1 VAL B 18 1993 1902 2662 99 -146 150 C ATOM 2654 CG2 VAL B 18 100.684 -15.898 24.157 1.00 17.65 C ANISOU 2654 CG2 VAL B 18 1994 1953 2757 152 -92 67 C ATOM 2655 N LYS B 19 103.481 -14.732 25.269 1.00 18.14 N ANISOU 2655 N LYS B 19 1975 1991 2925 164 -98 30 N ATOM 2656 CA LYS B 19 104.163 -13.437 25.238 1.00 18.27 C ANISOU 2656 CA LYS B 19 1968 2033 2939 157 -46 24 C ATOM 2657 C LYS B 19 103.616 -12.625 24.079 1.00 17.72 C ANISOU 2657 C LYS B 19 1909 2010 2815 151 34 23 C ATOM 2658 O LYS B 19 103.670 -13.070 22.940 1.00 18.32 O ANISOU 2658 O LYS B 19 1971 2098 2892 165 63 -13 O ATOM 2659 CB LYS B 19 105.666 -13.631 25.093 1.00 19.54 C ANISOU 2659 CB LYS B 19 2071 2177 3177 178 -51 -30 C ATOM 2660 CG LYS B 19 106.508 -12.395 25.384 1.00 20.21 C ANISOU 2660 CG LYS B 19 2130 2280 3271 166 -15 -33 C ATOM 2661 CD LYS B 19 107.987 -12.753 25.286 1.00 21.52 C ANISOU 2661 CD LYS B 19 2231 2426 3520 188 -28 -92 C ATOM 2662 CE LYS B 19 108.897 -11.742 25.957 1.00 22.34 C ANISOU 2662 CE LYS B 19 2309 2534 3646 175 -19 -91 C ATOM 2663 NZ LYS B 19 110.279 -12.294 26.027 1.00 23.24 N ANISOU 2663 NZ LYS B 19 2357 2622 3851 200 -50 -151 N ATOM 2664 N VAL B 20 103.069 -11.450 24.388 1.00 16.79 N ANISOU 2664 N VAL B 20 1816 1916 2648 129 64 61 N ATOM 2665 CA VAL B 20 102.468 -10.555 23.394 1.00 16.45 C ANISOU 2665 CA VAL B 20 1789 1910 2551 121 128 70 C ATOM 2666 C VAL B 20 103.412 -9.367 23.235 1.00 16.70 C ANISOU 2666 C VAL B 20 1795 1955 2594 111 173 60 C ATOM 2667 O VAL B 20 103.951 -8.882 24.227 1.00 16.31 O ANISOU 2667 O VAL B 20 1735 1892 2569 103 154 69 O ATOM 2668 CB VAL B 20 101.079 -10.070 23.863 1.00 16.05 C ANISOU 2668 CB VAL B 20 1785 1871 2443 105 122 117 C ATOM 2669 CG1 VAL B 20 100.497 -9.038 22.899 1.00 15.82 C ANISOU 2669 CG1 VAL B 20 1772 1873 2366 98 179 130 C ATOM 2670 CG2 VAL B 20 100.123 -11.247 24.036 1.00 16.15 C ANISOU 2670 CG2 VAL B 20 1822 1873 2441 108 79 128 C ATOM 2671 N SER B 21 103.637 -8.931 21.994 1.00 17.16 N ANISOU 2671 N SER B 21 1845 2042 2634 106 232 41 N ATOM 2672 CA SER B 21 104.566 -7.838 21.710 1.00 17.74 C ANISOU 2672 CA SER B 21 1895 2130 2716 89 278 31 C ATOM 2673 C SER B 21 103.837 -6.573 21.276 1.00 17.51 C ANISOU 2673 C SER B 21 1903 2121 2630 67 317 71 C ATOM 2674 O SER B 21 102.693 -6.623 20.813 1.00 17.14 O ANISOU 2674 O SER B 21 1892 2084 2536 68 318 95 O ATOM 2675 CB SER B 21 105.572 -8.249 20.630 1.00 18.43 C ANISOU 2675 CB SER B 21 1939 2236 2828 92 317 -26 C ATOM 2676 OG SER B 21 104.958 -8.441 19.376 1.00 19.03 O ANISOU 2676 OG SER B 21 2035 2341 2856 86 353 -31 O ATOM 2677 N ACYS B 22 104.523 -5.447 21.443 0.50 18.00 N ANISOU 2677 N ACYS B 22 1953 2185 2700 48 343 76 N ATOM 2678 N BCYS B 22 104.521 -5.438 21.433 0.50 17.35 N ANISOU 2678 N BCYS B 22 1871 2103 2618 48 343 77 N ATOM 2679 CA ACYS B 22 104.013 -4.142 21.072 0.50 18.34 C ANISOU 2679 CA ACYS B 22 2029 2239 2702 26 373 113 C ATOM 2680 CA BCYS B 22 103.993 -4.113 21.104 0.50 17.29 C ANISOU 2680 CA BCYS B 22 1897 2105 2568 26 372 115 C ATOM 2681 C ACYS B 22 105.171 -3.320 20.539 0.50 18.64 C ANISOU 2681 C ACYS B 22 2041 2290 2752 -1 420 97 C ATOM 2682 C BCYS B 22 105.135 -3.261 20.552 0.50 18.03 C ANISOU 2682 C BCYS B 22 1966 2212 2673 -2 420 100 C ATOM 2683 O ACYS B 22 106.038 -2.915 21.308 0.50 18.75 O ANISOU 2683 O ACYS B 22 2027 2291 2807 -6 414 88 O ATOM 2684 O BCYS B 22 105.956 -2.767 21.323 0.50 18.25 O ANISOU 2684 O BCYS B 22 1968 2226 2739 -8 415 93 O ATOM 2685 CB ACYS B 22 103.439 -3.453 22.297 0.50 18.37 C ANISOU 2685 CB ACYS B 22 2052 2221 2706 26 341 147 C ATOM 2686 CB BCYS B 22 103.419 -3.470 22.373 0.50 16.47 C ANISOU 2686 CB BCYS B 22 1812 1980 2467 27 338 147 C ATOM 2687 SG ACYS B 22 103.000 -1.732 22.011 0.50 19.10 S ANISOU 2687 SG ACYS B 22 2177 2314 2768 3 368 185 S ATOM 2688 SG BCYS B 22 102.846 -1.756 22.247 0.50 16.19 S ANISOU 2688 SG BCYS B 22 1810 1941 2400 6 359 188 S ATOM 2689 N LYS B 23 105.193 -3.104 19.226 1.00 18.93 N ANISOU 2689 N LYS B 23 2087 2354 2751 -22 466 94 N ATOM 2690 CA LYS B 23 106.248 -2.312 18.574 1.00 19.92 C ANISOU 2690 CA LYS B 23 2191 2499 2877 -59 517 81 C ATOM 2691 C LYS B 23 105.830 -0.848 18.504 1.00 19.51 C ANISOU 2691 C LYS B 23 2180 2438 2793 -87 528 133 C ATOM 2692 O LYS B 23 104.798 -0.529 17.906 1.00 19.66 O ANISOU 2692 O LYS B 23 2246 2459 2763 -92 526 170 O ATOM 2693 CB LYS B 23 106.514 -2.836 17.167 1.00 21.20 C ANISOU 2693 CB LYS B 23 2344 2702 3008 -76 563 49 C ATOM 2694 CG LYS B 23 107.706 -2.179 16.476 1.00 22.61 C ANISOU 2694 CG LYS B 23 2494 2910 3186 -122 621 25 C ATOM 2695 CD LYS B 23 108.042 -2.856 15.153 1.00 24.01 C ANISOU 2695 CD LYS B 23 2653 3135 3334 -141 668 -21 C ATOM 2696 CE LYS B 23 107.136 -2.376 14.027 1.00 24.84 C ANISOU 2696 CE LYS B 23 2818 3264 3358 -172 690 22 C ATOM 2697 NZ LYS B 23 107.603 -1.084 13.442 1.00 26.07 N ANISOU 2697 NZ LYS B 23 2992 3437 3478 -234 733 52 N ATOM 2698 N ALA B 24 106.641 0.021 19.108 1.00 19.59 N ANISOU 2698 N ALA B 24 2173 2435 2836 -105 534 135 N ATOM 2699 CA ALA B 24 106.341 1.447 19.224 1.00 19.53 C ANISOU 2699 CA ALA B 24 2200 2408 2812 -130 535 182 C ATOM 2700 C ALA B 24 107.157 2.249 18.226 1.00 20.18 C ANISOU 2700 C ALA B 24 2281 2511 2874 -183 587 185 C ATOM 2701 O ALA B 24 108.372 2.102 18.170 1.00 20.57 O ANISOU 2701 O ALA B 24 2284 2580 2953 -201 617 145 O ATOM 2702 CB ALA B 24 106.647 1.925 20.631 1.00 19.53 C ANISOU 2702 CB ALA B 24 2184 2378 2860 -118 504 182 C ATOM 2703 N SER B 25 106.483 3.091 17.444 1.00 20.30 N ANISOU 2703 N SER B 25 2348 2524 2841 -210 595 232 N ATOM 2704 CA SER B 25 107.155 3.952 16.473 1.00 21.24 C ANISOU 2704 CA SER B 25 2479 2662 2931 -271 640 247 C ATOM 2705 C SER B 25 106.587 5.366 16.509 1.00 21.06 C ANISOU 2705 C SER B 25 2508 2600 2895 -293 619 308 C ATOM 2706 O SER B 25 105.510 5.599 17.053 1.00 20.40 O ANISOU 2706 O SER B 25 2454 2482 2815 -258 573 335 O ATOM 2707 CB SER B 25 107.052 3.355 15.062 1.00 21.96 C ANISOU 2707 CB SER B 25 2582 2799 2964 -296 677 237 C ATOM 2708 OG SER B 25 105.714 3.221 14.637 1.00 22.44 O ANISOU 2708 OG SER B 25 2693 2851 2981 -277 648 274 O ATOM 2709 N GLY B 26 107.335 6.302 15.929 1.00 21.72 N ANISOU 2709 N GLY B 26 2600 2688 2964 -352 652 326 N ATOM 2710 CA GLY B 26 106.926 7.707 15.859 1.00 22.02 C ANISOU 2710 CA GLY B 26 2689 2685 2993 -381 629 385 C ATOM 2711 C GLY B 26 107.469 8.600 16.965 1.00 22.04 C ANISOU 2711 C GLY B 26 2674 2648 3053 -381 614 385 C ATOM 2712 O GLY B 26 107.184 9.793 16.982 1.00 22.83 O ANISOU 2712 O GLY B 26 2813 2706 3155 -403 591 430 O ATOM 2713 N TYR B 27 108.236 8.027 17.894 1.00 21.55 N ANISOU 2713 N TYR B 27 2553 2595 3040 -357 620 334 N ATOM 2714 CA TYR B 27 108.871 8.777 18.976 1.00 21.35 C ANISOU 2714 CA TYR B 27 2504 2538 3070 -359 607 326 C ATOM 2715 C TYR B 27 110.034 7.926 19.485 1.00 21.18 C ANISOU 2715 C TYR B 27 2413 2547 3088 -350 630 265 C ATOM 2716 O TYR B 27 110.140 6.747 19.126 1.00 21.22 O ANISOU 2716 O TYR B 27 2392 2588 3084 -332 645 230 O ATOM 2717 CB TYR B 27 107.857 9.058 20.097 1.00 20.81 C ANISOU 2717 CB TYR B 27 2454 2426 3029 -308 550 340 C ATOM 2718 CG TYR B 27 107.444 7.804 20.840 1.00 20.27 C ANISOU 2718 CG TYR B 27 2358 2371 2973 -252 528 305 C ATOM 2719 CD1 TYR B 27 106.528 6.908 20.287 1.00 20.21 C ANISOU 2719 CD1 TYR B 27 2369 2382 2928 -226 521 309 C ATOM 2720 CD2 TYR B 27 107.998 7.496 22.076 1.00 19.89 C ANISOU 2720 CD2 TYR B 27 2267 2318 2972 -230 511 270 C ATOM 2721 CE1 TYR B 27 106.163 5.749 20.957 1.00 19.69 C ANISOU 2721 CE1 TYR B 27 2281 2327 2873 -181 498 280 C ATOM 2722 CE2 TYR B 27 107.647 6.340 22.753 1.00 19.59 C ANISOU 2722 CE2 TYR B 27 2209 2290 2944 -186 486 244 C ATOM 2723 CZ TYR B 27 106.736 5.466 22.186 1.00 19.48 C ANISOU 2723 CZ TYR B 27 2215 2292 2893 -163 480 250 C ATOM 2724 OH TYR B 27 106.390 4.322 22.863 1.00 19.20 O ANISOU 2724 OH TYR B 27 2163 2265 2867 -125 452 227 O ATOM 2725 N ALA B 28 110.884 8.504 20.330 1.00 21.10 N ANISOU 2725 N ALA B 28 2372 2520 3127 -361 628 250 N ATOM 2726 CA ALA B 28 112.045 7.801 20.871 1.00 21.30 C ANISOU 2726 CA ALA B 28 2327 2567 3197 -353 642 191 C ATOM 2727 C ALA B 28 111.576 6.771 21.892 1.00 20.80 C ANISOU 2727 C ALA B 28 2246 2496 3161 -289 596 168 C ATOM 2728 O ALA B 28 110.980 7.123 22.915 1.00 19.85 O ANISOU 2728 O ALA B 28 2143 2342 3057 -263 553 184 O ATOM 2729 CB ALA B 28 113.025 8.778 21.505 1.00 21.59 C ANISOU 2729 CB ALA B 28 2339 2586 3278 -385 647 185 C ATOM 2730 N PHE B 29 111.831 5.498 21.597 1.00 20.89 N ANISOU 2730 N PHE B 29 2224 2539 3176 -267 605 128 N ATOM 2731 CA PHE B 29 111.274 4.385 22.366 1.00 20.64 C ANISOU 2731 CA PHE B 29 2184 2499 3159 -212 559 113 C ATOM 2732 C PHE B 29 111.447 4.534 23.880 1.00 19.64 C ANISOU 2732 C PHE B 29 2040 2342 3078 -189 512 107 C ATOM 2733 O PHE B 29 110.503 4.341 24.640 1.00 19.14 O ANISOU 2733 O PHE B 29 2004 2260 3007 -159 470 125 O ATOM 2734 CB PHE B 29 111.912 3.072 21.897 1.00 21.45 C ANISOU 2734 CB PHE B 29 2239 2633 3278 -197 574 60 C ATOM 2735 CG PHE B 29 111.428 1.862 22.643 1.00 21.68 C ANISOU 2735 CG PHE B 29 2260 2650 3326 -145 523 45 C ATOM 2736 CD1 PHE B 29 110.129 1.410 22.475 1.00 21.78 C ANISOU 2736 CD1 PHE B 29 2319 2659 3299 -121 502 74 C ATOM 2737 CD2 PHE B 29 112.261 1.188 23.530 1.00 22.34 C ANISOU 2737 CD2 PHE B 29 2294 2725 3470 -122 492 5 C ATOM 2738 CE1 PHE B 29 109.667 0.298 23.167 1.00 21.70 C ANISOU 2738 CE1 PHE B 29 2305 2637 3302 -80 454 64 C ATOM 2739 CE2 PHE B 29 111.806 0.071 24.218 1.00 22.28 C ANISOU 2739 CE2 PHE B 29 2285 2702 3477 -81 438 -1 C ATOM 2740 CZ PHE B 29 110.510 -0.374 24.035 1.00 22.08 C ANISOU 2740 CZ PHE B 29 2308 2674 3408 -62 421 29 C ATOM 2741 N THR B 30 112.639 4.922 24.318 1.00 19.50 N ANISOU 2741 N THR B 30 1980 2324 3106 -209 521 80 N ATOM 2742 CA THR B 30 112.922 4.996 25.753 1.00 18.90 C ANISOU 2742 CA THR B 30 1884 2223 3072 -191 475 70 C ATOM 2743 C THR B 30 112.442 6.283 26.443 1.00 18.51 C ANISOU 2743 C THR B 30 1871 2144 3019 -204 459 105 C ATOM 2744 O THR B 30 112.704 6.462 27.630 1.00 18.80 O ANISOU 2744 O THR B 30 1892 2164 3086 -196 424 95 O ATOM 2745 CB THR B 30 114.419 4.768 26.050 1.00 19.52 C ANISOU 2745 CB THR B 30 1895 2312 3209 -200 481 22 C ATOM 2746 OG1 THR B 30 115.205 5.718 25.338 1.00 20.23 O ANISOU 2746 OG1 THR B 30 1972 2414 3300 -249 534 18 O ATOM 2747 CG2 THR B 30 114.847 3.370 25.645 1.00 19.70 C ANISOU 2747 CG2 THR B 30 1877 2357 3252 -175 480 -22 C ATOM 2748 N SER B 31 111.734 7.155 25.727 1.00 17.75 N ANISOU 2748 N SER B 31 1821 2039 2885 -224 480 143 N ATOM 2749 CA SER B 31 111.308 8.449 26.278 1.00 17.60 C ANISOU 2749 CA SER B 31 1832 1986 2869 -236 464 170 C ATOM 2750 C SER B 31 109.937 8.452 26.960 1.00 16.81 C ANISOU 2750 C SER B 31 1769 1867 2750 -202 423 188 C ATOM 2751 O SER B 31 109.558 9.479 27.524 1.00 16.68 O ANISOU 2751 O SER B 31 1772 1823 2743 -207 406 201 O ATOM 2752 CB SER B 31 111.331 9.526 25.187 1.00 17.99 C ANISOU 2752 CB SER B 31 1913 2026 2897 -280 499 203 C ATOM 2753 OG SER B 31 110.307 9.354 24.223 1.00 17.91 O ANISOU 2753 OG SER B 31 1947 2021 2838 -274 505 234 O ATOM 2754 N GLN B 32 109.177 7.354 26.869 1.00 16.39 N ANISOU 2754 N GLN B 32 1725 1831 2672 -171 408 187 N ATOM 2755 CA GLN B 32 107.820 7.289 27.428 1.00 15.95 C ANISOU 2755 CA GLN B 32 1701 1766 2593 -143 374 201 C ATOM 2756 C GLN B 32 107.531 5.899 27.968 1.00 15.60 C ANISOU 2756 C GLN B 32 1644 1740 2542 -114 347 184 C ATOM 2757 O GLN B 32 108.066 4.905 27.467 1.00 15.93 O ANISOU 2757 O GLN B 32 1665 1802 2587 -109 358 170 O ATOM 2758 CB GLN B 32 106.769 7.638 26.363 1.00 15.80 C ANISOU 2758 CB GLN B 32 1726 1741 2535 -142 386 234 C ATOM 2759 CG GLN B 32 106.985 8.967 25.639 1.00 16.11 C ANISOU 2759 CG GLN B 32 1787 1757 2577 -175 406 260 C ATOM 2760 CD GLN B 32 106.629 10.202 26.452 1.00 16.21 C ANISOU 2760 CD GLN B 32 1813 1731 2614 -177 381 265 C ATOM 2761 OE1 GLN B 32 105.997 10.140 27.512 1.00 15.68 O ANISOU 2761 OE1 GLN B 32 1743 1659 2555 -152 350 249 O ATOM 2762 NE2 GLN B 32 107.037 11.347 25.944 1.00 16.66 N ANISOU 2762 NE2 GLN B 32 1886 1762 2683 -210 394 287 N ATOM 2763 N ASN B 33 106.661 5.825 28.974 1.00 15.27 N ANISOU 2763 N ASN B 33 1616 1695 2491 -98 312 184 N ATOM 2764 CA ASN B 33 106.263 4.532 29.539 1.00 15.14 C ANISOU 2764 CA ASN B 33 1596 1695 2462 -78 282 175 C ATOM 2765 C ASN B 33 105.319 3.783 28.608 1.00 15.10 C ANISOU 2765 C ASN B 33 1614 1703 2420 -61 289 190 C ATOM 2766 O ASN B 33 104.480 4.383 27.929 1.00 15.22 O ANISOU 2766 O ASN B 33 1658 1713 2411 -60 303 209 O ATOM 2767 CB ASN B 33 105.578 4.705 30.894 1.00 14.94 C ANISOU 2767 CB ASN B 33 1579 1668 2429 -76 246 170 C ATOM 2768 CG ASN B 33 106.547 5.070 31.996 1.00 15.22 C ANISOU 2768 CG ASN B 33 1589 1697 2498 -91 228 151 C ATOM 2769 OD1 ASN B 33 107.690 5.444 31.736 1.00 15.87 O ANISOU 2769 OD1 ASN B 33 1647 1771 2614 -104 244 143 O ATOM 2770 ND2 ASN B 33 106.092 4.973 33.235 1.00 15.06 N ANISOU 2770 ND2 ASN B 33 1574 1684 2466 -95 194 143 N ATOM 2771 N ILE B 34 105.458 2.464 28.604 1.00 14.98 N ANISOU 2771 N ILE B 34 1588 1701 2404 -47 274 179 N ATOM 2772 CA ILE B 34 104.487 1.577 27.962 1.00 14.95 C ANISOU 2772 CA ILE B 34 1606 1710 2366 -30 271 189 C ATOM 2773 C ILE B 34 103.593 0.962 29.026 1.00 14.49 C ANISOU 2773 C ILE B 34 1560 1657 2290 -23 230 191 C ATOM 2774 O ILE B 34 104.060 0.489 30.060 1.00 14.64 O ANISOU 2774 O ILE B 34 1564 1673 2326 -27 197 181 O ATOM 2775 CB ILE B 34 105.168 0.486 27.111 1.00 15.56 C ANISOU 2775 CB ILE B 34 1661 1796 2453 -22 283 173 C ATOM 2776 CG1 ILE B 34 105.904 1.125 25.924 1.00 16.08 C ANISOU 2776 CG1 ILE B 34 1718 1868 2524 -38 332 170 C ATOM 2777 CG2 ILE B 34 104.146 -0.535 26.609 1.00 15.53 C ANISOU 2777 CG2 ILE B 34 1680 1805 2416 -4 273 181 C ATOM 2778 CD1 ILE B 34 105.015 1.679 24.823 1.00 16.32 C ANISOU 2778 CD1 ILE B 34 1786 1905 2511 -44 359 196 C ATOM 2779 N TYR B 35 102.298 0.936 28.724 1.00 13.77 N ANISOU 2779 N TYR B 35 1497 1574 2162 -15 230 205 N ATOM 2780 CA TYR B 35 101.257 0.427 29.591 1.00 13.49 C ANISOU 2780 CA TYR B 35 1475 1550 2100 -14 199 207 C ATOM 2781 C TYR B 35 100.590 -0.789 28.948 1.00 13.29 C ANISOU 2781 C TYR B 35 1463 1536 2050 -1 192 213 C ATOM 2782 O TYR B 35 100.583 -0.919 27.721 1.00 13.64 O ANISOU 2782 O TYR B 35 1512 1581 2088 10 217 218 O ATOM 2783 CB TYR B 35 100.196 1.500 29.773 1.00 13.02 C ANISOU 2783 CB TYR B 35 1432 1492 2023 -15 206 210 C ATOM 2784 CG TYR B 35 100.461 2.488 30.877 1.00 12.92 C ANISOU 2784 CG TYR B 35 1409 1472 2027 -29 198 196 C ATOM 2785 CD1 TYR B 35 101.483 3.441 30.793 1.00 12.96 C ANISOU 2785 CD1 TYR B 35 1401 1457 2066 -37 214 193 C ATOM 2786 CD2 TYR B 35 99.654 2.498 32.005 1.00 12.77 C ANISOU 2786 CD2 TYR B 35 1393 1470 1988 -39 177 183 C ATOM 2787 CE1 TYR B 35 101.692 4.357 31.821 1.00 12.98 C ANISOU 2787 CE1 TYR B 35 1394 1453 2086 -50 206 177 C ATOM 2788 CE2 TYR B 35 99.852 3.407 33.015 1.00 12.95 C ANISOU 2788 CE2 TYR B 35 1405 1490 2024 -54 172 164 C ATOM 2789 CZ TYR B 35 100.861 4.330 32.930 1.00 12.99 C ANISOU 2789 CZ TYR B 35 1398 1472 2066 -58 184 161 C ATOM 2790 OH TYR B 35 101.034 5.238 33.946 1.00 13.36 O ANISOU 2790 OH TYR B 35 1435 1516 2127 -72 177 139 O ATOM 2791 N TRP B 36 99.986 -1.642 29.772 1.00 13.54 N ANISOU 2791 N TRP B 36 1503 1578 2063 -6 158 214 N ATOM 2792 CA TRP B 36 99.179 -2.755 29.289 1.00 13.39 C ANISOU 2792 CA TRP B 36 1500 1570 2019 2 147 221 C ATOM 2793 C TRP B 36 97.830 -2.774 29.988 1.00 13.42 C ANISOU 2793 C TRP B 36 1521 1594 1985 -9 132 224 C ATOM 2794 O TRP B 36 97.756 -2.532 31.191 1.00 13.10 O ANISOU 2794 O TRP B 36 1478 1561 1938 -30 114 219 O ATOM 2795 CB TRP B 36 99.891 -4.089 29.501 1.00 13.71 C ANISOU 2795 CB TRP B 36 1531 1600 2078 3 115 217 C ATOM 2796 CG TRP B 36 101.103 -4.254 28.617 1.00 13.96 C ANISOU 2796 CG TRP B 36 1539 1618 2148 18 133 203 C ATOM 2797 CD1 TRP B 36 102.397 -3.919 28.915 1.00 14.44 C ANISOU 2797 CD1 TRP B 36 1571 1666 2251 15 133 189 C ATOM 2798 CD2 TRP B 36 101.123 -4.794 27.291 1.00 14.30 C ANISOU 2798 CD2 TRP B 36 1580 1663 2189 35 156 195 C ATOM 2799 NE1 TRP B 36 103.216 -4.212 27.853 1.00 14.82 N ANISOU 2799 NE1 TRP B 36 1597 1710 2324 29 158 171 N ATOM 2800 CE2 TRP B 36 102.468 -4.757 26.845 1.00 14.51 C ANISOU 2800 CE2 TRP B 36 1574 1681 2257 40 173 173 C ATOM 2801 CE3 TRP B 36 100.141 -5.307 26.431 1.00 14.40 C ANISOU 2801 CE3 TRP B 36 1614 1688 2170 45 165 202 C ATOM 2802 CZ2 TRP B 36 102.856 -5.229 25.572 1.00 14.81 C ANISOU 2802 CZ2 TRP B 36 1600 1726 2302 52 202 154 C ATOM 2803 CZ3 TRP B 36 100.520 -5.769 25.177 1.00 14.80 C ANISOU 2803 CZ3 TRP B 36 1655 1742 2225 57 190 186 C ATOM 2804 CH2 TRP B 36 101.869 -5.718 24.755 1.00 14.89 C ANISOU 2804 CH2 TRP B 36 1634 1748 2276 60 210 161 C ATOM 2805 N VAL B 37 96.791 -3.077 29.204 1.00 13.38 N ANISOU 2805 N VAL B 37 1531 1600 1953 2 141 230 N ATOM 2806 CA VAL B 37 95.392 -3.063 29.621 1.00 13.62 C ANISOU 2806 CA VAL B 37 1574 1654 1949 -7 134 228 C ATOM 2807 C VAL B 37 94.709 -4.348 29.154 1.00 13.59 C ANISOU 2807 C VAL B 37 1583 1660 1921 -5 120 236 C ATOM 2808 O VAL B 37 94.952 -4.814 28.054 1.00 13.74 O ANISOU 2808 O VAL B 37 1605 1668 1946 14 130 240 O ATOM 2809 CB VAL B 37 94.662 -1.833 29.036 1.00 13.76 C ANISOU 2809 CB VAL B 37 1593 1673 1964 8 159 223 C ATOM 2810 CG1 VAL B 37 93.165 -1.861 29.354 1.00 14.00 C ANISOU 2810 CG1 VAL B 37 1628 1728 1963 4 153 212 C ATOM 2811 CG2 VAL B 37 95.300 -0.559 29.571 1.00 13.97 C ANISOU 2811 CG2 VAL B 37 1607 1684 2016 4 169 214 C ATOM 2812 N LYS B 38 93.840 -4.889 29.999 1.00 14.02 N ANISOU 2812 N LYS B 38 1645 1736 1946 -28 98 234 N ATOM 2813 CA LYS B 38 93.009 -6.041 29.664 1.00 14.38 C ANISOU 2813 CA LYS B 38 1705 1792 1966 -32 83 241 C ATOM 2814 C LYS B 38 91.566 -5.599 29.470 1.00 14.66 C ANISOU 2814 C LYS B 38 1743 1856 1973 -31 97 231 C ATOM 2815 O LYS B 38 91.062 -4.802 30.259 1.00 14.84 O ANISOU 2815 O LYS B 38 1756 1898 1987 -45 103 215 O ATOM 2816 CB LYS B 38 93.049 -7.038 30.805 1.00 14.50 C ANISOU 2816 CB LYS B 38 1730 1814 1967 -68 43 250 C ATOM 2817 CG LYS B 38 92.232 -8.296 30.579 1.00 14.78 C ANISOU 2817 CG LYS B 38 1782 1856 1976 -80 22 259 C ATOM 2818 CD LYS B 38 92.391 -9.231 31.755 1.00 15.20 C ANISOU 2818 CD LYS B 38 1850 1910 2017 -123 -24 274 C ATOM 2819 CE LYS B 38 91.510 -10.454 31.623 1.00 15.64 C ANISOU 2819 CE LYS B 38 1925 1972 2044 -143 -48 286 C ATOM 2820 NZ LYS B 38 91.625 -11.264 32.865 1.00 15.99 N ANISOU 2820 NZ LYS B 38 1989 2017 2070 -195 -97 307 N ATOM 2821 N GLN B 39 90.924 -6.105 28.416 1.00 15.06 N ANISOU 2821 N GLN B 39 1802 1908 2012 -14 102 236 N ATOM 2822 CA GLN B 39 89.482 -5.926 28.238 1.00 15.94 C ANISOU 2822 CA GLN B 39 1913 2046 2096 -14 108 224 C ATOM 2823 C GLN B 39 88.845 -7.277 27.917 1.00 16.75 C ANISOU 2823 C GLN B 39 2029 2159 2175 -24 90 232 C ATOM 2824 O GLN B 39 88.989 -7.800 26.816 1.00 16.60 O ANISOU 2824 O GLN B 39 2020 2126 2161 -3 92 241 O ATOM 2825 CB GLN B 39 89.169 -4.916 27.143 1.00 16.02 C ANISOU 2825 CB GLN B 39 1921 2048 2117 20 130 222 C ATOM 2826 CG GLN B 39 87.696 -4.554 27.066 1.00 16.27 C ANISOU 2826 CG GLN B 39 1946 2104 2132 23 130 204 C ATOM 2827 CD GLN B 39 87.457 -3.336 26.219 1.00 16.16 C ANISOU 2827 CD GLN B 39 1930 2074 2136 55 141 203 C ATOM 2828 OE1 GLN B 39 88.014 -3.211 25.133 1.00 16.89 O ANISOU 2828 OE1 GLN B 39 2038 2145 2236 73 149 223 O ATOM 2829 NE2 GLN B 39 86.613 -2.431 26.705 1.00 16.77 N ANISOU 2829 NE2 GLN B 39 1989 2162 2221 58 140 177 N ATOM 2830 N SER B 40 88.113 -7.815 28.882 1.00 19.01 N ANISOU 2830 N SER B 40 2317 2472 2434 -61 74 227 N ATOM 2831 CA SER B 40 87.354 -9.041 28.660 1.00 20.72 C ANISOU 2831 CA SER B 40 2547 2700 2627 -77 56 234 C ATOM 2832 C SER B 40 86.151 -8.718 27.786 1.00 22.14 C ANISOU 2832 C SER B 40 2720 2899 2794 -57 72 220 C ATOM 2833 O SER B 40 85.701 -7.568 27.741 1.00 22.18 O ANISOU 2833 O SER B 40 2709 2915 2805 -41 91 201 O ATOM 2834 CB SER B 40 86.917 -9.645 29.984 1.00 21.34 C ANISOU 2834 CB SER B 40 2631 2805 2674 -132 34 235 C ATOM 2835 OG SER B 40 88.039 -10.095 30.715 1.00 22.26 O ANISOU 2835 OG SER B 40 2759 2898 2803 -151 8 254 O ATOM 2836 N HIS B 41 85.645 -9.721 27.068 1.00 24.00 N ANISOU 2836 N HIS B 41 2968 3135 3016 -55 61 226 N ATOM 2837 CA HIS B 41 84.569 -9.484 26.107 1.00 25.23 C ANISOU 2837 CA HIS B 41 3119 3306 3162 -33 72 215 C ATOM 2838 C HIS B 41 83.349 -8.886 26.800 1.00 25.41 C ANISOU 2838 C HIS B 41 3119 3368 3168 -51 78 188 C ATOM 2839 O HIS B 41 82.872 -9.431 27.789 1.00 25.93 O ANISOU 2839 O HIS B 41 3181 3461 3208 -95 70 181 O ATOM 2840 CB HIS B 41 84.175 -10.769 25.380 1.00 26.31 C ANISOU 2840 CB HIS B 41 3272 3440 3285 -36 56 223 C ATOM 2841 CG HIS B 41 83.166 -10.549 24.296 1.00 27.62 C ANISOU 2841 CG HIS B 41 3435 3620 3441 -12 63 213 C ATOM 2842 ND1 HIS B 41 83.475 -9.928 23.105 1.00 28.67 N ANISOU 2842 ND1 HIS B 41 3572 3735 3585 27 76 218 N ATOM 2843 CD2 HIS B 41 81.847 -10.846 24.235 1.00 28.63 C ANISOU 2843 CD2 HIS B 41 3554 3778 3547 -24 57 199 C ATOM 2844 CE1 HIS B 41 82.392 -9.862 22.351 1.00 28.95 C ANISOU 2844 CE1 HIS B 41 3605 3787 3607 40 73 210 C ATOM 2845 NE2 HIS B 41 81.391 -10.413 23.013 1.00 29.29 N ANISOU 2845 NE2 HIS B 41 3638 3859 3633 12 62 195 N ATOM 2846 N GLY B 42 82.882 -7.749 26.283 1.00 25.46 N ANISOU 2846 N GLY B 42 3109 3376 3188 -19 92 171 N ATOM 2847 CA GLY B 42 81.723 -7.046 26.831 1.00 25.53 C ANISOU 2847 CA GLY B 42 3088 3419 3192 -26 98 135 C ATOM 2848 C GLY B 42 81.952 -6.323 28.149 1.00 25.80 C ANISOU 2848 C GLY B 42 3103 3470 3231 -49 108 112 C ATOM 2849 O GLY B 42 80.989 -5.867 28.777 1.00 27.11 O ANISOU 2849 O GLY B 42 3239 3671 3390 -64 115 72 O ATOM 2850 N LYS B 43 83.213 -6.187 28.560 1.00 24.60 N ANISOU 2850 N LYS B 43 2964 3292 3090 -54 109 132 N ATOM 2851 CA LYS B 43 83.550 -5.692 29.891 1.00 24.07 C ANISOU 2851 CA LYS B 43 2883 3241 3021 -84 115 114 C ATOM 2852 C LYS B 43 84.395 -4.421 29.808 1.00 22.70 C ANISOU 2852 C LYS B 43 2704 3036 2885 -52 125 112 C ATOM 2853 O LYS B 43 84.730 -3.935 28.723 1.00 22.80 O ANISOU 2853 O LYS B 43 2724 3014 2923 -11 127 128 O ATOM 2854 CB LYS B 43 84.294 -6.780 30.686 1.00 24.93 C ANISOU 2854 CB LYS B 43 3015 3351 3107 -128 98 141 C ATOM 2855 CG LYS B 43 83.549 -8.101 30.830 1.00 25.95 C ANISOU 2855 CG LYS B 43 3156 3504 3198 -167 82 149 C ATOM 2856 CD LYS B 43 82.173 -7.928 31.458 1.00 27.14 C ANISOU 2856 CD LYS B 43 3281 3712 3319 -201 95 109 C ATOM 2857 CE LYS B 43 81.475 -9.259 31.677 1.00 27.86 C ANISOU 2857 CE LYS B 43 3387 3830 3370 -250 79 121 C ATOM 2858 NZ LYS B 43 80.061 -9.053 32.111 1.00 28.78 N ANISOU 2858 NZ LYS B 43 3470 4006 3459 -280 97 75 N ATOM 2859 N SER B 44 84.718 -3.890 30.975 1.00 21.98 N ANISOU 2859 N SER B 44 2599 2959 2794 -77 130 92 N ATOM 2860 CA SER B 44 85.466 -2.656 31.079 1.00 21.28 C ANISOU 2860 CA SER B 44 2501 2842 2741 -54 139 85 C ATOM 2861 C SER B 44 86.961 -2.911 30.925 1.00 20.34 C ANISOU 2861 C SER B 44 2405 2687 2637 -51 134 123 C ATOM 2862 O SER B 44 87.419 -4.035 30.721 1.00 20.43 O ANISOU 2862 O SER B 44 2436 2691 2634 -62 121 152 O ATOM 2863 CB SER B 44 85.183 -1.970 32.423 1.00 21.79 C ANISOU 2863 CB SER B 44 2539 2940 2800 -84 148 40 C ATOM 2864 OG SER B 44 85.725 -0.653 32.442 1.00 21.79 O ANISOU 2864 OG SER B 44 2527 2911 2842 -57 154 26 O ATOM 2865 N LEU B 45 87.696 -1.822 31.028 1.00 19.25 N ANISOU 2865 N LEU B 45 2260 2524 2531 -35 142 118 N ATOM 2866 CA LEU B 45 89.137 -1.800 30.896 1.00 18.41 C ANISOU 2866 CA LEU B 45 2166 2384 2446 -30 141 146 C ATOM 2867 C LEU B 45 89.794 -1.997 32.260 1.00 17.96 C ANISOU 2867 C LEU B 45 2106 2340 2379 -68 131 140 C ATOM 2868 O LEU B 45 89.354 -1.443 33.264 1.00 18.12 O ANISOU 2868 O LEU B 45 2108 2386 2389 -90 135 108 O ATOM 2869 CB LEU B 45 89.539 -0.461 30.293 1.00 18.51 C ANISOU 2869 CB LEU B 45 2173 2362 2497 2 153 144 C ATOM 2870 CG LEU B 45 88.972 -0.185 28.895 1.00 18.74 C ANISOU 2870 CG LEU B 45 2212 2374 2534 37 157 156 C ATOM 2871 CD1 LEU B 45 89.088 1.290 28.547 1.00 18.89 C ANISOU 2871 CD1 LEU B 45 2226 2362 2590 60 161 150 C ATOM 2872 CD2 LEU B 45 89.683 -1.038 27.847 1.00 18.63 C ANISOU 2872 CD2 LEU B 45 2221 2345 2514 45 159 192 C ATOM 2873 N GLU B 46 90.849 -2.804 32.292 1.00 17.50 N ANISOU 2873 N GLU B 46 2061 2263 2324 -77 116 168 N ATOM 2874 CA GLU B 46 91.573 -3.097 33.524 1.00 17.72 C ANISOU 2874 CA GLU B 46 2091 2298 2344 -114 97 170 C ATOM 2875 C GLU B 46 93.066 -2.839 33.326 1.00 16.29 C ANISOU 2875 C GLU B 46 1909 2079 2203 -98 94 186 C ATOM 2876 O GLU B 46 93.660 -3.361 32.385 1.00 16.18 O ANISOU 2876 O GLU B 46 1901 2038 2207 -75 93 206 O ATOM 2877 CB GLU B 46 91.361 -4.557 33.897 1.00 19.19 C ANISOU 2877 CB GLU B 46 2296 2498 2498 -146 68 191 C ATOM 2878 CG GLU B 46 91.878 -4.919 35.261 1.00 21.08 C ANISOU 2878 CG GLU B 46 2542 2750 2718 -194 40 196 C ATOM 2879 CD GLU B 46 91.396 -6.281 35.745 1.00 22.91 C ANISOU 2879 CD GLU B 46 2796 2999 2908 -237 7 217 C ATOM 2880 OE1 GLU B 46 90.945 -7.109 34.918 1.00 24.60 O ANISOU 2880 OE1 GLU B 46 3022 3205 3121 -224 2 231 O ATOM 2881 OE2 GLU B 46 91.455 -6.511 36.972 1.00 25.41 O ANISOU 2881 OE2 GLU B 46 3122 3339 3194 -290 -16 219 O ATOM 2882 N TRP B 47 93.659 -2.015 34.185 1.00 15.11 N ANISOU 2882 N TRP B 47 1746 1928 2065 -111 95 172 N ATOM 2883 CA TRP B 47 95.105 -1.748 34.110 1.00 14.54 C ANISOU 2883 CA TRP B 47 1669 1823 2032 -100 92 182 C ATOM 2884 C TRP B 47 95.916 -2.935 34.635 1.00 14.51 C ANISOU 2884 C TRP B 47 1675 1812 2028 -121 54 203 C ATOM 2885 O TRP B 47 95.680 -3.394 35.748 1.00 15.03 O ANISOU 2885 O TRP B 47 1749 1900 2063 -160 27 204 O ATOM 2886 CB TRP B 47 95.449 -0.491 34.906 1.00 14.30 C ANISOU 2886 CB TRP B 47 1622 1793 2016 -110 101 159 C ATOM 2887 CG TRP B 47 96.925 -0.222 35.024 1.00 14.10 C ANISOU 2887 CG TRP B 47 1588 1739 2029 -107 95 166 C ATOM 2888 CD1 TRP B 47 97.796 0.068 34.019 1.00 13.95 C ANISOU 2888 CD1 TRP B 47 1564 1689 2049 -79 111 177 C ATOM 2889 CD2 TRP B 47 97.702 -0.263 36.229 1.00 14.26 C ANISOU 2889 CD2 TRP B 47 1604 1764 2050 -137 70 162 C ATOM 2890 NE1 TRP B 47 99.062 0.235 34.521 1.00 14.11 N ANISOU 2890 NE1 TRP B 47 1571 1692 2098 -88 100 176 N ATOM 2891 CE2 TRP B 47 99.033 0.031 35.877 1.00 14.11 C ANISOU 2891 CE2 TRP B 47 1572 1712 2077 -121 71 168 C ATOM 2892 CE3 TRP B 47 97.399 -0.515 37.572 1.00 14.45 C ANISOU 2892 CE3 TRP B 47 1633 1819 2037 -180 45 153 C ATOM 2893 CZ2 TRP B 47 100.067 0.084 36.823 1.00 14.55 C ANISOU 2893 CZ2 TRP B 47 1618 1761 2148 -142 46 166 C ATOM 2894 CZ3 TRP B 47 98.421 -0.470 38.507 1.00 14.76 C ANISOU 2894 CZ3 TRP B 47 1668 1853 2087 -204 19 154 C ATOM 2895 CH2 TRP B 47 99.741 -0.160 38.128 1.00 14.61 C ANISOU 2895 CH2 TRP B 47 1634 1797 2119 -182 17 160 C ATOM 2896 N ILE B 48 96.870 -3.409 33.830 1.00 14.06 N ANISOU 2896 N ILE B 48 1615 1723 2004 -97 50 217 N ATOM 2897 CA ILE B 48 97.737 -4.531 34.212 1.00 14.26 C ANISOU 2897 CA ILE B 48 1644 1731 2043 -108 7 233 C ATOM 2898 C ILE B 48 99.037 -4.026 34.835 1.00 14.46 C ANISOU 2898 C ILE B 48 1652 1738 2104 -112 -5 227 C ATOM 2899 O ILE B 48 99.439 -4.491 35.912 1.00 14.71 O ANISOU 2899 O ILE B 48 1689 1770 2130 -141 -48 235 O ATOM 2900 CB ILE B 48 98.070 -5.434 33.005 1.00 14.38 C ANISOU 2900 CB ILE B 48 1659 1722 2082 -77 7 241 C ATOM 2901 CG1 ILE B 48 96.793 -6.056 32.418 1.00 14.41 C ANISOU 2901 CG1 ILE B 48 1681 1743 2051 -75 13 247 C ATOM 2902 CG2 ILE B 48 99.066 -6.520 33.420 1.00 14.73 C ANISOU 2902 CG2 ILE B 48 1702 1741 2156 -82 -44 250 C ATOM 2903 CD1 ILE B 48 96.975 -6.686 31.051 1.00 14.64 C ANISOU 2903 CD1 ILE B 48 1709 1755 2099 -42 24 248 C ATOM 2904 N GLY B 49 99.716 -3.124 34.132 1.00 14.29 N ANISOU 2904 N GLY B 49 1611 1701 2118 -87 29 216 N ATOM 2905 CA GLY B 49 100.992 -2.618 34.591 1.00 14.40 C ANISOU 2905 CA GLY B 49 1604 1698 2170 -90 22 208 C ATOM 2906 C GLY B 49 101.560 -1.621 33.606 1.00 14.28 C ANISOU 2906 C GLY B 49 1571 1669 2188 -66 67 198 C ATOM 2907 O GLY B 49 100.977 -1.373 32.536 1.00 14.02 O ANISOU 2907 O GLY B 49 1544 1637 2144 -48 100 201 O ATOM 2908 N TYR B 50 102.689 -1.024 33.968 1.00 14.35 N ANISOU 2908 N TYR B 50 1557 1663 2232 -71 66 188 N ATOM 2909 CA TYR B 50 103.461 -0.209 33.035 1.00 14.41 C ANISOU 2909 CA TYR B 50 1546 1655 2273 -56 106 180 C ATOM 2910 C TYR B 50 104.939 -0.455 33.226 1.00 14.81 C ANISOU 2910 C TYR B 50 1566 1690 2372 -56 90 168 C ATOM 2911 O TYR B 50 105.350 -1.001 34.240 1.00 15.07 O ANISOU 2911 O TYR B 50 1593 1719 2412 -68 44 167 O ATOM 2912 CB TYR B 50 103.130 1.282 33.172 1.00 14.41 C ANISOU 2912 CB TYR B 50 1549 1656 2269 -63 134 174 C ATOM 2913 CG TYR B 50 103.516 1.957 34.487 1.00 14.47 C ANISOU 2913 CG TYR B 50 1547 1664 2286 -86 115 160 C ATOM 2914 CD1 TYR B 50 104.845 2.277 34.773 1.00 14.78 C ANISOU 2914 CD1 TYR B 50 1561 1688 2366 -93 110 151 C ATOM 2915 CD2 TYR B 50 102.545 2.327 35.425 1.00 14.51 C ANISOU 2915 CD2 TYR B 50 1566 1689 2259 -102 104 152 C ATOM 2916 CE1 TYR B 50 105.200 2.910 35.960 1.00 14.72 C ANISOU 2916 CE1 TYR B 50 1546 1683 2366 -115 91 137 C ATOM 2917 CE2 TYR B 50 102.889 2.970 36.608 1.00 14.69 C ANISOU 2917 CE2 TYR B 50 1579 1716 2285 -125 89 134 C ATOM 2918 CZ TYR B 50 104.223 3.252 36.874 1.00 14.78 C ANISOU 2918 CZ TYR B 50 1569 1710 2336 -131 81 129 C ATOM 2919 OH TYR B 50 104.585 3.901 38.024 1.00 15.28 O ANISOU 2919 OH TYR B 50 1624 1778 2404 -156 65 110 O ATOM 2920 N ILE B 51 105.731 -0.055 32.241 1.00 14.94 N ANISOU 2920 N ILE B 51 1561 1697 2418 -46 126 159 N ATOM 2921 CA ILE B 51 107.178 -0.169 32.327 1.00 15.47 C ANISOU 2921 CA ILE B 51 1590 1752 2537 -47 118 139 C ATOM 2922 C ILE B 51 107.821 1.119 31.837 1.00 15.69 C ANISOU 2922 C ILE B 51 1602 1776 2585 -57 164 131 C ATOM 2923 O ILE B 51 107.432 1.680 30.812 1.00 15.30 O ANISOU 2923 O ILE B 51 1565 1730 2518 -56 207 140 O ATOM 2924 CB ILE B 51 107.696 -1.427 31.592 1.00 15.61 C ANISOU 2924 CB ILE B 51 1587 1764 2579 -26 109 126 C ATOM 2925 CG1 ILE B 51 109.205 -1.629 31.843 1.00 16.14 C ANISOU 2925 CG1 ILE B 51 1608 1818 2708 -24 92 98 C ATOM 2926 CG2 ILE B 51 107.363 -1.391 30.100 1.00 15.83 C ANISOU 2926 CG2 ILE B 51 1621 1803 2591 -15 161 125 C ATOM 2927 CD1 ILE B 51 109.666 -3.050 31.581 1.00 16.46 C ANISOU 2927 CD1 ILE B 51 1627 1846 2783 -2 57 80 C ATOM 2928 N GLU B 52 108.786 1.592 32.623 1.00 16.20 N ANISOU 2928 N GLU B 52 1641 1831 2684 -70 149 117 N ATOM 2929 CA GLU B 52 109.614 2.736 32.280 1.00 16.54 C ANISOU 2929 CA GLU B 52 1663 1867 2754 -85 186 106 C ATOM 2930 C GLU B 52 110.817 2.166 31.513 1.00 16.83 C ANISOU 2930 C GLU B 52 1656 1905 2832 -79 202 82 C ATOM 2931 O GLU B 52 111.678 1.537 32.115 1.00 17.47 O ANISOU 2931 O GLU B 52 1705 1980 2953 -74 165 61 O ATOM 2932 CB GLU B 52 110.016 3.459 33.568 1.00 16.75 C ANISOU 2932 CB GLU B 52 1682 1887 2797 -103 160 99 C ATOM 2933 CG GLU B 52 110.649 4.822 33.395 1.00 17.05 C ANISOU 2933 CG GLU B 52 1705 1914 2858 -123 194 92 C ATOM 2934 CD GLU B 52 111.949 4.758 32.639 1.00 17.44 C ANISOU 2934 CD GLU B 52 1714 1963 2950 -128 220 72 C ATOM 2935 OE1 GLU B 52 112.987 4.428 33.260 1.00 18.35 O ANISOU 2935 OE1 GLU B 52 1791 2076 3107 -130 193 49 O ATOM 2936 OE2 GLU B 52 111.925 4.990 31.409 1.00 17.76 O ANISOU 2936 OE2 GLU B 52 1758 2009 2982 -132 267 78 O ATOM 2937 N PRO B 52A 110.865 2.350 30.180 1.00 17.15 N ANISOU 2937 N PRO B 52A 1695 1955 2864 -81 253 81 N ATOM 2938 CA PRO B 52A 111.856 1.634 29.356 1.00 17.59 C ANISOU 2938 CA PRO B 52A 1709 2022 2954 -75 272 48 C ATOM 2939 C PRO B 52A 113.304 2.103 29.455 1.00 18.26 C ANISOU 2939 C PRO B 52A 1741 2106 3091 -93 286 16 C ATOM 2940 O PRO B 52A 114.200 1.341 29.100 1.00 18.95 O ANISOU 2940 O PRO B 52A 1781 2200 3218 -83 287 -22 O ATOM 2941 CB PRO B 52A 111.368 1.894 27.933 1.00 17.69 C ANISOU 2941 CB PRO B 52A 1742 2051 2929 -83 328 60 C ATOM 2942 CG PRO B 52A 110.737 3.232 28.035 1.00 17.66 C ANISOU 2942 CG PRO B 52A 1776 2038 2896 -104 344 93 C ATOM 2943 CD PRO B 52A 110.009 3.209 29.341 1.00 16.94 C ANISOU 2943 CD PRO B 52A 1707 1933 2798 -91 294 107 C ATOM 2944 N TYR B 53 113.537 3.342 29.884 1.00 18.32 N ANISOU 2944 N TYR B 53 1753 2105 3102 -118 298 26 N ATOM 2945 CA TYR B 53 114.900 3.882 29.946 1.00 19.00 C ANISOU 2945 CA TYR B 53 1789 2192 3237 -140 315 -4 C ATOM 2946 C TYR B 53 115.754 3.130 30.964 1.00 19.45 C ANISOU 2946 C TYR B 53 1803 2240 3348 -123 260 -34 C ATOM 2947 O TYR B 53 116.827 2.617 30.619 1.00 19.99 O ANISOU 2947 O TYR B 53 1815 2316 3463 -119 265 -76 O ATOM 2948 CB TYR B 53 114.869 5.380 30.258 1.00 18.91 C ANISOU 2948 CB TYR B 53 1798 2169 3219 -172 333 16 C ATOM 2949 CG TYR B 53 116.211 6.062 30.146 1.00 19.51 C ANISOU 2949 CG TYR B 53 1827 2248 3339 -203 360 -11 C ATOM 2950 CD1 TYR B 53 116.701 6.483 28.907 1.00 20.06 C ANISOU 2950 CD1 TYR B 53 1883 2335 3404 -233 422 -18 C ATOM 2951 CD2 TYR B 53 116.987 6.302 31.282 1.00 19.80 C ANISOU 2951 CD2 TYR B 53 1832 2272 3419 -206 324 -31 C ATOM 2952 CE1 TYR B 53 117.931 7.121 28.805 1.00 20.76 C ANISOU 2952 CE1 TYR B 53 1926 2430 3531 -268 450 -44 C ATOM 2953 CE2 TYR B 53 118.221 6.934 31.186 1.00 20.33 C ANISOU 2953 CE2 TYR B 53 1853 2343 3530 -236 349 -58 C ATOM 2954 CZ TYR B 53 118.682 7.340 29.951 1.00 20.84 C ANISOU 2954 CZ TYR B 53 1903 2427 3590 -268 413 -66 C ATOM 2955 OH TYR B 53 119.906 7.962 29.874 1.00 21.70 O ANISOU 2955 OH TYR B 53 1963 2542 3739 -303 440 -95 O ATOM 2956 N ASN B 54 115.276 3.057 32.204 1.00 19.48 N ANISOU 2956 N ASN B 54 1832 2229 3343 -116 204 -16 N ATOM 2957 CA ASN B 54 115.941 2.286 33.262 1.00 20.17 C ANISOU 2957 CA ASN B 54 1889 2303 3472 -102 137 -35 C ATOM 2958 C ASN B 54 115.371 0.889 33.453 1.00 20.22 C ANISOU 2958 C ASN B 54 1911 2303 3470 -73 87 -27 C ATOM 2959 O ASN B 54 115.923 0.110 34.232 1.00 20.89 O ANISOU 2959 O ASN B 54 1973 2372 3591 -61 24 -40 O ATOM 2960 CB ASN B 54 115.892 3.051 34.585 1.00 20.32 C ANISOU 2960 CB ASN B 54 1924 2312 3486 -121 102 -22 C ATOM 2961 CG ASN B 54 116.590 4.391 34.498 1.00 20.91 C ANISOU 2961 CG ASN B 54 1978 2386 3580 -150 143 -33 C ATOM 2962 OD1 ASN B 54 115.986 5.444 34.747 1.00 21.97 O ANISOU 2962 OD1 ASN B 54 2146 2516 3684 -168 160 -13 O ATOM 2963 ND2 ASN B 54 117.854 4.368 34.102 1.00 21.59 N ANISOU 2963 ND2 ASN B 54 2007 2475 3720 -155 158 -69 N ATOM 2964 N VAL B 55 114.277 0.581 32.749 1.00 19.84 N ANISOU 2964 N VAL B 55 1902 2263 3373 -64 111 -5 N ATOM 2965 CA VAL B 55 113.648 -0.739 32.755 1.00 19.91 C ANISOU 2965 CA VAL B 55 1929 2266 3369 -39 70 4 C ATOM 2966 C VAL B 55 113.071 -1.055 34.141 1.00 19.90 C ANISOU 2966 C VAL B 55 1962 2254 3346 -45 2 31 C ATOM 2967 O VAL B 55 113.512 -1.968 34.839 1.00 20.85 O ANISOU 2967 O VAL B 55 2069 2357 3496 -36 -64 26 O ATOM 2968 CB VAL B 55 114.590 -1.854 32.230 1.00 20.29 C ANISOU 2968 CB VAL B 55 1925 2306 3476 -13 53 -38 C ATOM 2969 CG1 VAL B 55 113.784 -3.121 31.953 1.00 20.17 C ANISOU 2969 CG1 VAL B 55 1935 2284 3443 11 23 -27 C ATOM 2970 CG2 VAL B 55 115.295 -1.409 30.953 1.00 20.45 C ANISOU 2970 CG2 VAL B 55 1905 2347 3516 -19 127 -73 C ATOM 2971 N VAL B 56 112.057 -0.286 34.519 1.00 19.49 N ANISOU 2971 N VAL B 56 1954 2213 3239 -63 18 60 N ATOM 2972 CA VAL B 56 111.445 -0.371 35.843 1.00 19.45 C ANISOU 2972 CA VAL B 56 1981 2208 3200 -79 -34 82 C ATOM 2973 C VAL B 56 109.934 -0.551 35.674 1.00 19.33 C ANISOU 2973 C VAL B 56 2015 2208 3122 -80 -21 109 C ATOM 2974 O VAL B 56 109.236 0.393 35.290 1.00 18.94 O ANISOU 2974 O VAL B 56 1983 2170 3042 -86 26 115 O ATOM 2975 CB VAL B 56 111.735 0.895 36.671 1.00 19.69 C ANISOU 2975 CB VAL B 56 2009 2242 3231 -105 -27 78 C ATOM 2976 CG1 VAL B 56 111.121 0.784 38.063 1.00 19.62 C ANISOU 2976 CG1 VAL B 56 2032 2241 3181 -129 -78 95 C ATOM 2977 CG2 VAL B 56 113.242 1.128 36.747 1.00 20.16 C ANISOU 2977 CG2 VAL B 56 2017 2289 3355 -106 -35 49 C ATOM 2978 N PRO B 57 109.424 -1.762 35.949 1.00 19.46 N ANISOU 2978 N PRO B 57 2052 2222 3122 -75 -67 124 N ATOM 2979 CA PRO B 57 107.994 -2.009 35.828 1.00 19.24 C ANISOU 2979 CA PRO B 57 2067 2210 3035 -79 -58 147 C ATOM 2980 C PRO B 57 107.228 -1.723 37.112 1.00 19.19 C ANISOU 2980 C PRO B 57 2091 2221 2979 -112 -85 162 C ATOM 2981 O PRO B 57 107.806 -1.737 38.199 1.00 19.76 O ANISOU 2981 O PRO B 57 2158 2289 3060 -133 -130 162 O ATOM 2982 CB PRO B 57 107.935 -3.496 35.506 1.00 19.49 C ANISOU 2982 CB PRO B 57 2101 2228 3076 -62 -97 153 C ATOM 2983 CG PRO B 57 109.101 -4.073 36.231 1.00 19.89 C ANISOU 2983 CG PRO B 57 2127 2254 3178 -62 -159 144 C ATOM 2984 CD PRO B 57 110.158 -3.003 36.260 1.00 19.98 C ANISOU 2984 CD PRO B 57 2100 2264 3227 -64 -132 120 C ATOM 2985 N MET B 58 105.932 -1.459 36.963 1.00 18.53 N ANISOU 2985 N MET B 58 2036 2159 2844 -118 -57 172 N ATOM 2986 CA MET B 58 104.982 -1.391 38.069 1.00 18.60 C ANISOU 2986 CA MET B 58 2075 2194 2800 -151 -78 180 C ATOM 2987 C MET B 58 103.773 -2.231 37.686 1.00 18.08 C ANISOU 2987 C MET B 58 2036 2141 2691 -149 -78 197 C ATOM 2988 O MET B 58 103.301 -2.147 36.548 1.00 17.75 O ANISOU 2988 O MET B 58 1995 2100 2651 -123 -38 196 O ATOM 2989 CB MET B 58 104.540 0.052 38.323 1.00 18.68 C ANISOU 2989 CB MET B 58 2083 2221 2794 -161 -37 162 C ATOM 2990 N TYR B 59 103.265 -3.020 38.630 1.00 18.20 N ANISOU 2990 N TYR B 59 2077 2172 2667 -182 -124 213 N ATOM 2991 CA TYR B 59 102.157 -3.947 38.399 1.00 18.00 C ANISOU 2991 CA TYR B 59 2079 2160 2601 -189 -132 231 C ATOM 2992 C TYR B 59 100.951 -3.668 39.278 1.00 18.46 C ANISOU 2992 C TYR B 59 2159 2261 2593 -230 -127 229 C ATOM 2993 O TYR B 59 101.095 -3.311 40.445 1.00 18.96 O ANISOU 2993 O TYR B 59 2227 2343 2635 -268 -147 224 O ATOM 2994 CB TYR B 59 102.614 -5.383 38.701 1.00 17.94 C ANISOU 2994 CB TYR B 59 2084 2128 2605 -197 -200 255 C ATOM 2995 CG TYR B 59 103.734 -5.861 37.825 1.00 17.81 C ANISOU 2995 CG TYR B 59 2041 2071 2657 -155 -210 248 C ATOM 2996 CD1 TYR B 59 103.472 -6.434 36.587 1.00 17.64 C ANISOU 2996 CD1 TYR B 59 2015 2037 2650 -121 -187 245 C ATOM 2997 CD2 TYR B 59 105.063 -5.720 38.221 1.00 18.13 C ANISOU 2997 CD2 TYR B 59 2054 2086 2748 -150 -240 239 C ATOM 2998 CE1 TYR B 59 104.500 -6.861 35.768 1.00 17.75 C ANISOU 2998 CE1 TYR B 59 1999 2020 2726 -85 -191 229 C ATOM 2999 CE2 TYR B 59 106.098 -6.155 37.417 1.00 18.21 C ANISOU 2999 CE2 TYR B 59 2031 2063 2825 -112 -246 223 C ATOM 3000 CZ TYR B 59 105.811 -6.724 36.186 1.00 18.02 C ANISOU 3000 CZ TYR B 59 2002 2031 2812 -80 -219 216 C ATOM 3001 OH TYR B 59 106.808 -7.158 35.353 1.00 18.53 O ANISOU 3001 OH TYR B 59 2030 2070 2942 -44 -219 190 O ATOM 3002 N ASN B 60 99.765 -3.864 38.715 1.00 18.68 N ANISOU 3002 N ASN B 60 2200 2308 2590 -225 -100 229 N ATOM 3003 CA ASN B 60 98.535 -3.974 39.491 1.00 19.27 C ANISOU 3003 CA ASN B 60 2294 2426 2599 -268 -101 227 C ATOM 3004 C ASN B 60 98.665 -5.264 40.314 1.00 20.50 C ANISOU 3004 C ASN B 60 2478 2581 2728 -311 -166 259 C ATOM 3005 O ASN B 60 98.921 -6.320 39.740 1.00 20.31 O ANISOU 3005 O ASN B 60 2464 2527 2726 -294 -195 282 O ATOM 3006 CB ASN B 60 97.344 -4.059 38.523 1.00 18.66 C ANISOU 3006 CB ASN B 60 2221 2363 2506 -247 -63 222 C ATOM 3007 CG ASN B 60 95.986 -4.080 39.215 1.00 18.81 C ANISOU 3007 CG ASN B 60 2252 2434 2462 -289 -55 209 C ATOM 3008 OD1 ASN B 60 95.854 -4.466 40.375 1.00 19.29 O ANISOU 3008 OD1 ASN B 60 2328 2521 2480 -344 -85 215 O ATOM 3009 ND2 ASN B 60 94.960 -3.699 38.475 1.00 18.42 N ANISOU 3009 ND2 ASN B 60 2194 2399 2405 -267 -15 191 N ATOM 3010 N PRO B 61 98.491 -5.192 41.651 1.00 21.86 N ANISOU 3010 N PRO B 61 2665 2787 2853 -370 -191 260 N ATOM 3011 CA PRO B 61 98.540 -6.403 42.479 1.00 23.23 C ANISOU 3011 CA PRO B 61 2874 2961 2993 -421 -258 297 C ATOM 3012 C PRO B 61 97.601 -7.530 42.027 1.00 23.90 C ANISOU 3012 C PRO B 61 2984 3048 3050 -431 -270 320 C ATOM 3013 O PRO B 61 97.911 -8.697 42.262 1.00 25.03 O ANISOU 3013 O PRO B 61 3153 3164 3194 -452 -333 358 O ATOM 3014 CB PRO B 61 98.143 -5.895 43.867 1.00 23.49 C ANISOU 3014 CB PRO B 61 2917 3046 2961 -489 -261 284 C ATOM 3015 CG PRO B 61 98.554 -4.472 43.876 1.00 23.27 C ANISOU 3015 CG PRO B 61 2856 3024 2962 -462 -216 243 C ATOM 3016 CD PRO B 61 98.352 -3.978 42.473 1.00 22.52 C ANISOU 3016 CD PRO B 61 2735 2907 2914 -394 -162 226 C ATOM 3017 N LYS B 62 96.492 -7.200 41.360 1.00 24.81 N ANISOU 3017 N LYS B 62 3090 3191 3146 -416 -214 299 N ATOM 3018 CA LYS B 62 95.657 -8.213 40.684 1.00 25.89 C ANISOU 3018 CA LYS B 62 3244 3325 3268 -414 -219 317 C ATOM 3019 C LYS B 62 96.440 -9.086 39.674 1.00 25.69 C ANISOU 3019 C LYS B 62 3220 3239 3304 -364 -248 338 C ATOM 3020 O LYS B 62 96.068 -10.233 39.446 1.00 27.23 O ANISOU 3020 O LYS B 62 3437 3419 3489 -375 -282 363 O ATOM 3021 CB LYS B 62 94.466 -7.552 39.974 1.00 26.98 C ANISOU 3021 CB LYS B 62 3364 3497 3389 -392 -153 284 C ATOM 3022 CG LYS B 62 93.396 -6.993 40.899 1.00 28.37 C ANISOU 3022 CG LYS B 62 3539 3740 3502 -446 -126 256 C ATOM 3023 CD LYS B 62 92.305 -6.253 40.131 1.00 29.19 C ANISOU 3023 CD LYS B 62 3616 3868 3605 -414 -66 218 C ATOM 3024 CE LYS B 62 91.279 -5.628 41.072 1.00 30.29 C ANISOU 3024 CE LYS B 62 3744 4076 3691 -463 -38 176 C ATOM 3025 NZ LYS B 62 90.430 -4.579 40.429 1.00 31.13 N ANISOU 3025 NZ LYS B 62 3816 4199 3815 -422 16 128 N ATOM 3026 N PHE B 63 97.512 -8.546 39.087 1.00 25.57 N ANISOU 3026 N PHE B 63 3176 3189 3351 -312 -236 324 N ATOM 3027 CA PHE B 63 98.335 -9.252 38.093 1.00 25.45 C ANISOU 3027 CA PHE B 63 3151 3122 3397 -263 -255 331 C ATOM 3028 C PHE B 63 99.786 -9.581 38.509 1.00 26.39 C ANISOU 3028 C PHE B 63 3261 3197 3570 -255 -310 340 C ATOM 3029 O PHE B 63 100.560 -10.074 37.680 1.00 26.48 O ANISOU 3029 O PHE B 63 3254 3168 3641 -211 -322 333 O ATOM 3030 CB PHE B 63 98.343 -8.446 36.795 1.00 24.75 C ANISOU 3030 CB PHE B 63 3034 3031 3340 -207 -188 303 C ATOM 3031 CG PHE B 63 96.996 -8.329 36.153 1.00 23.60 C ANISOU 3031 CG PHE B 63 2895 2915 3156 -203 -145 296 C ATOM 3032 CD1 PHE B 63 96.533 -9.312 35.284 1.00 23.54 C ANISOU 3032 CD1 PHE B 63 2899 2895 3150 -187 -152 305 C ATOM 3033 CD2 PHE B 63 96.186 -7.235 36.412 1.00 23.40 C ANISOU 3033 CD2 PHE B 63 2863 2930 3097 -214 -101 276 C ATOM 3034 CE1 PHE B 63 95.288 -9.194 34.680 1.00 22.95 C ANISOU 3034 CE1 PHE B 63 2829 2849 3042 -183 -115 298 C ATOM 3035 CE2 PHE B 63 94.947 -7.110 35.813 1.00 22.96 C ANISOU 3035 CE2 PHE B 63 2810 2901 3014 -208 -67 266 C ATOM 3036 CZ PHE B 63 94.491 -8.096 34.947 1.00 22.96 C ANISOU 3036 CZ PHE B 63 2822 2890 3013 -193 -74 279 C ATOM 3037 N LYS B 64 100.162 -9.315 39.763 1.00 27.19 N ANISOU 3037 N LYS B 64 3372 3309 3652 -298 -345 349 N ATOM 3038 CA LYS B 64 101.460 -9.762 40.300 1.00 28.17 C ANISOU 3038 CA LYS B 64 3491 3391 3823 -297 -413 362 C ATOM 3039 C LYS B 64 101.558 -11.286 40.237 1.00 28.51 C ANISOU 3039 C LYS B 64 3558 3391 3885 -301 -488 393 C ATOM 3040 O LYS B 64 100.662 -11.991 40.693 1.00 29.49 O ANISOU 3040 O LYS B 64 3722 3529 3955 -348 -516 422 O ATOM 3041 CB LYS B 64 101.649 -9.304 41.752 1.00 28.83 C ANISOU 3041 CB LYS B 64 3589 3499 3866 -354 -444 372 C ATOM 3042 N GLY B 65 102.632 -11.787 39.636 1.00 28.61 N ANISOU 3042 N GLY B 65 3544 3350 3976 -253 -519 383 N ATOM 3043 CA GLY B 65 102.809 -13.227 39.457 1.00 28.50 C ANISOU 3043 CA GLY B 65 3547 3286 3996 -247 -593 403 C ATOM 3044 C GLY B 65 102.053 -13.840 38.286 1.00 27.58 C ANISOU 3044 C GLY B 65 3433 3165 3882 -218 -561 395 C ATOM 3045 O GLY B 65 102.227 -15.025 38.015 1.00 29.02 O ANISOU 3045 O GLY B 65 3624 3301 4102 -206 -619 405 O ATOM 3046 N LYS B 66 101.194 -13.059 37.622 1.00 25.14 N ANISOU 3046 N LYS B 66 3117 2902 3534 -208 -475 376 N ATOM 3047 CA LYS B 66 100.538 -13.442 36.370 1.00 23.48 C ANISOU 3047 CA LYS B 66 2902 2691 3326 -175 -434 362 C ATOM 3048 C LYS B 66 101.292 -12.818 35.195 1.00 21.85 C ANISOU 3048 C LYS B 66 2649 2478 3174 -115 -377 320 C ATOM 3049 O LYS B 66 101.649 -13.518 34.247 1.00 21.70 O ANISOU 3049 O LYS B 66 2613 2430 3202 -76 -382 301 O ATOM 3050 CB LYS B 66 99.071 -12.966 36.385 1.00 23.48 C ANISOU 3050 CB LYS B 66 2925 2748 3249 -206 -381 369 C ATOM 3051 CG LYS B 66 98.287 -13.096 35.083 1.00 23.64 C ANISOU 3051 CG LYS B 66 2940 2779 3265 -173 -330 352 C ATOM 3052 CD LYS B 66 98.150 -14.532 34.612 1.00 23.74 C ANISOU 3052 CD LYS B 66 2969 2754 3299 -165 -378 363 C ATOM 3053 CE LYS B 66 97.244 -15.338 35.524 1.00 23.88 C ANISOU 3053 CE LYS B 66 3031 2779 3263 -227 -428 402 C ATOM 3054 NZ LYS B 66 96.945 -16.682 34.961 1.00 23.81 N ANISOU 3054 NZ LYS B 66 3040 2733 3273 -220 -470 412 N ATOM 3055 N ALA B 67 101.512 -11.504 35.262 1.00 19.91 N ANISOU 3055 N ALA B 67 2383 2262 2919 -112 -322 304 N ATOM 3056 CA ALA B 67 102.093 -10.732 34.167 1.00 18.95 C ANISOU 3056 CA ALA B 67 2223 2143 2835 -67 -259 269 C ATOM 3057 C ALA B 67 103.533 -10.328 34.459 1.00 18.49 C ANISOU 3057 C ALA B 67 2129 2063 2834 -53 -274 251 C ATOM 3058 O ALA B 67 103.854 -9.961 35.593 1.00 18.82 O ANISOU 3058 O ALA B 67 2176 2106 2868 -82 -305 264 O ATOM 3059 CB ALA B 67 101.257 -9.493 33.922 1.00 18.45 C ANISOU 3059 CB ALA B 67 2163 2123 2723 -73 -188 265 C ATOM 3060 N THR B 68 104.388 -10.396 33.435 1.00 17.88 N ANISOU 3060 N THR B 68 2013 1968 2813 -12 -250 217 N ATOM 3061 CA THR B 68 105.764 -9.888 33.499 1.00 18.19 C ANISOU 3061 CA THR B 68 2008 1992 2910 4 -248 189 C ATOM 3062 C THR B 68 106.006 -8.977 32.303 1.00 17.65 C ANISOU 3062 C THR B 68 1910 1946 2848 26 -164 159 C ATOM 3063 O THR B 68 105.789 -9.387 31.167 1.00 17.45 O ANISOU 3063 O THR B 68 1880 1925 2828 48 -134 143 O ATOM 3064 CB THR B 68 106.793 -11.034 33.468 1.00 19.00 C ANISOU 3064 CB THR B 68 2082 2048 3087 28 -313 169 C ATOM 3065 OG1 THR B 68 106.479 -11.991 34.480 1.00 19.96 O ANISOU 3065 OG1 THR B 68 2240 2144 3200 4 -399 204 O ATOM 3066 CG2 THR B 68 108.217 -10.503 33.698 1.00 19.38 C ANISOU 3066 CG2 THR B 68 2082 2084 3198 41 -318 139 C ATOM 3067 N LEU B 69 106.469 -7.754 32.559 1.00 17.58 N ANISOU 3067 N LEU B 69 1886 1953 2841 16 -130 154 N ATOM 3068 CA LEU B 69 106.715 -6.769 31.506 1.00 17.50 C ANISOU 3068 CA LEU B 69 1855 1963 2833 27 -53 132 C ATOM 3069 C LEU B 69 108.196 -6.636 31.212 1.00 17.69 C ANISOU 3069 C LEU B 69 1825 1973 2922 42 -46 94 C ATOM 3070 O LEU B 69 108.999 -6.533 32.134 1.00 18.45 O ANISOU 3070 O LEU B 69 1903 2054 3053 34 -86 90 O ATOM 3071 CB LEU B 69 106.169 -5.404 31.907 1.00 17.44 C ANISOU 3071 CB LEU B 69 1866 1978 2782 4 -17 150 C ATOM 3072 CG LEU B 69 104.699 -5.313 32.294 1.00 17.58 C ANISOU 3072 CG LEU B 69 1928 2014 2736 -13 -18 179 C ATOM 3073 CD1 LEU B 69 104.299 -3.851 32.420 1.00 17.57 C ANISOU 3073 CD1 LEU B 69 1935 2033 2710 -26 26 183 C ATOM 3074 CD2 LEU B 69 103.795 -6.030 31.298 1.00 17.48 C ANISOU 3074 CD2 LEU B 69 1934 2010 2699 2 -2 184 C ATOM 3075 N THR B 70 108.536 -6.626 29.928 1.00 17.60 N ANISOU 3075 N THR B 70 1788 1972 2926 58 6 65 N ATOM 3076 CA THR B 70 109.911 -6.422 29.471 1.00 18.30 C ANISOU 3076 CA THR B 70 1820 2059 3074 68 28 20 C ATOM 3077 C THR B 70 109.937 -5.508 28.241 1.00 18.51 C ANISOU 3077 C THR B 70 1839 2117 3077 59 113 8 C ATOM 3078 O THR B 70 108.884 -5.174 27.670 1.00 17.74 O ANISOU 3078 O THR B 70 1781 2038 2923 52 147 34 O ATOM 3079 CB THR B 70 110.575 -7.768 29.123 1.00 18.74 C ANISOU 3079 CB THR B 70 1839 2092 3190 97 -10 -20 C ATOM 3080 OG1 THR B 70 109.774 -8.460 28.159 1.00 18.69 O ANISOU 3080 OG1 THR B 70 1852 2095 3155 110 9 -23 O ATOM 3081 CG2 THR B 70 110.722 -8.642 30.366 1.00 18.89 C ANISOU 3081 CG2 THR B 70 1864 2072 3240 103 -105 -6 C ATOM 3082 N VAL B 71 111.137 -5.073 27.865 1.00 19.28 N ANISOU 3082 N VAL B 71 1887 2221 3217 55 144 -30 N ATOM 3083 CA VAL B 71 111.342 -4.265 26.660 1.00 20.18 C ANISOU 3083 CA VAL B 71 1990 2366 3310 38 223 -43 C ATOM 3084 C VAL B 71 112.561 -4.776 25.883 1.00 21.21 C ANISOU 3084 C VAL B 71 2056 2507 3495 47 247 -107 C ATOM 3085 O VAL B 71 113.411 -5.489 26.442 1.00 22.08 O ANISOU 3085 O VAL B 71 2123 2597 3672 67 200 -142 O ATOM 3086 CB VAL B 71 111.517 -2.756 26.978 1.00 20.02 C ANISOU 3086 CB VAL B 71 1980 2353 3274 7 255 -20 C ATOM 3087 CG1 VAL B 71 110.267 -2.177 27.628 1.00 19.64 C ANISOU 3087 CG1 VAL B 71 1990 2298 3174 -1 239 33 C ATOM 3088 CG2 VAL B 71 112.744 -2.499 27.849 1.00 20.50 C ANISOU 3088 CG2 VAL B 71 1995 2400 3395 3 230 -45 C ATOM 3089 N ASP B 72 112.628 -4.435 24.595 1.00 22.31 N ANISOU 3089 N ASP B 72 2190 2681 3608 30 318 -124 N ATOM 3090 CA ASP B 72 113.815 -4.727 23.764 1.00 23.81 C ANISOU 3090 CA ASP B 72 2313 2894 3841 28 357 -193 C ATOM 3091 C ASP B 72 114.090 -3.587 22.770 1.00 24.53 C ANISOU 3091 C ASP B 72 2404 3025 3892 -18 440 -192 C ATOM 3092 O ASP B 72 113.241 -3.272 21.930 1.00 23.56 O ANISOU 3092 O ASP B 72 2327 2923 3703 -35 478 -162 O ATOM 3093 CB ASP B 72 113.633 -6.032 22.998 1.00 24.55 C ANISOU 3093 CB ASP B 72 2391 2992 3945 56 352 -234 C ATOM 3094 CG ASP B 72 114.881 -6.437 22.239 1.00 25.88 C ANISOU 3094 CG ASP B 72 2482 3185 4167 57 388 -318 C ATOM 3095 OD1 ASP B 72 115.827 -6.924 22.885 1.00 27.59 O ANISOU 3095 OD1 ASP B 72 2642 3377 4462 80 344 -361 O ATOM 3096 OD2 ASP B 72 114.922 -6.260 21.002 1.00 26.69 O ANISOU 3096 OD2 ASP B 72 2577 3332 4233 33 458 -343 O ATOM 3097 N LYS B 73 115.294 -3.017 22.840 1.00 26.04 N ANISOU 3097 N LYS B 73 2543 3228 4124 -39 466 -227 N ATOM 3098 CA LYS B 73 115.646 -1.825 22.047 1.00 27.20 C ANISOU 3098 CA LYS B 73 2691 3409 4234 -93 540 -220 C ATOM 3099 C LYS B 73 115.840 -2.112 20.549 1.00 27.50 C ANISOU 3099 C LYS B 73 2711 3496 4241 -116 609 -261 C ATOM 3100 O LYS B 73 115.425 -1.300 19.717 1.00 27.40 O ANISOU 3100 O LYS B 73 2740 3510 4163 -159 659 -226 O ATOM 3101 CB LYS B 73 116.883 -1.113 22.623 1.00 28.84 C ANISOU 3101 CB LYS B 73 2848 3615 4494 -114 547 -246 C ATOM 3102 CG LYS B 73 116.582 -0.116 23.737 1.00 29.26 C ANISOU 3102 CG LYS B 73 2939 3635 4542 -122 513 -189 C ATOM 3103 CD LYS B 73 116.413 -0.778 25.093 1.00 29.60 C ANISOU 3103 CD LYS B 73 2983 3638 4626 -79 430 -182 C ATOM 3104 CE LYS B 73 115.811 0.180 26.105 1.00 29.80 C ANISOU 3104 CE LYS B 73 3057 3637 4628 -89 401 -124 C ATOM 3105 NZ LYS B 73 115.792 -0.357 27.491 1.00 29.95 N ANISOU 3105 NZ LYS B 73 3075 3624 4682 -60 323 -118 N ATOM 3106 N SER B 74 116.425 -3.258 20.200 1.00 27.54 N ANISOU 3106 N SER B 74 2658 3514 4292 -90 606 -333 N ATOM 3107 CA SER B 74 116.641 -3.603 18.781 1.00 27.94 C ANISOU 3107 CA SER B 74 2685 3618 4314 -113 674 -384 C ATOM 3108 C SER B 74 115.333 -3.758 17.985 1.00 26.89 C ANISOU 3108 C SER B 74 2623 3496 4098 -117 687 -338 C ATOM 3109 O SER B 74 115.308 -3.501 16.777 1.00 26.82 O ANISOU 3109 O SER B 74 2622 3536 4033 -159 752 -349 O ATOM 3110 CB SER B 74 117.503 -4.867 18.637 1.00 28.89 C ANISOU 3110 CB SER B 74 2723 3745 4511 -77 662 -481 C ATOM 3111 OG SER B 74 116.786 -6.030 19.012 1.00 29.29 O ANISOU 3111 OG SER B 74 2792 3757 4581 -21 595 -477 O ATOM 3112 N SER B 75 114.260 -4.178 18.663 1.00 25.56 N ANISOU 3112 N SER B 75 2504 3285 3921 -77 624 -289 N ATOM 3113 CA SER B 75 112.937 -4.281 18.050 1.00 24.70 C ANISOU 3113 CA SER B 75 2463 3182 3739 -78 627 -242 C ATOM 3114 C SER B 75 111.978 -3.106 18.342 1.00 23.46 C ANISOU 3114 C SER B 75 2381 3010 3525 -99 621 -154 C ATOM 3115 O SER B 75 110.849 -3.114 17.842 1.00 23.24 O ANISOU 3115 O SER B 75 2407 2984 3437 -99 621 -114 O ATOM 3116 CB SER B 75 112.277 -5.589 18.486 1.00 24.99 C ANISOU 3116 CB SER B 75 2508 3188 3801 -23 564 -250 C ATOM 3117 OG SER B 75 112.090 -5.619 19.883 1.00 25.26 O ANISOU 3117 OG SER B 75 2553 3173 3872 5 496 -217 O ATOM 3118 N ASER B 76 112.430 -2.127 19.131 0.50 22.98 N ANISOU 3118 N ASER B 76 2316 2930 3485 -115 615 -131 N ATOM 3119 N BSER B 76 112.438 -2.113 19.113 0.50 22.93 N ANISOU 3119 N BSER B 76 2309 2924 3478 -116 616 -131 N ATOM 3120 CA ASER B 76 111.613 -0.986 19.550 0.50 22.26 C ANISOU 3120 CA ASER B 76 2285 2816 3355 -131 602 -58 C ATOM 3121 CA BSER B 76 111.618 -0.980 19.568 0.50 22.15 C ANISOU 3121 CA BSER B 76 2272 2802 3342 -131 602 -57 C ATOM 3122 C ASER B 76 110.281 -1.449 20.132 0.50 21.11 C ANISOU 3122 C ASER B 76 2189 2642 3191 -92 548 -18 C ATOM 3123 C BSER B 76 110.283 -1.452 20.130 0.50 21.05 C ANISOU 3123 C BSER B 76 2181 2635 3184 -92 548 -18 C ATOM 3124 O ASER B 76 109.232 -0.888 19.817 0.50 20.46 O ANISOU 3124 O ASER B 76 2162 2557 3055 -102 549 32 O ATOM 3125 O BSER B 76 109.233 -0.899 19.801 0.50 20.42 O ANISOU 3125 O BSER B 76 2156 2552 3049 -102 550 32 O ATOM 3126 CB ASER B 76 111.364 -0.048 18.370 0.50 22.74 C ANISOU 3126 CB ASER B 76 2384 2906 3349 -183 658 -26 C ATOM 3127 CB BSER B 76 111.384 0.018 18.430 0.50 22.56 C ANISOU 3127 CB BSER B 76 2362 2881 3328 -183 657 -25 C ATOM 3128 OG ASER B 76 110.839 1.183 18.813 0.50 22.71 O ANISOU 3128 OG ASER B 76 2428 2874 3326 -200 645 35 O ATOM 3129 OG BSER B 76 112.616 0.491 17.909 0.50 23.27 O ANISOU 3129 OG BSER B 76 2409 3002 3430 -229 711 -60 O ATOM 3130 N SER B 77 110.342 -2.486 20.965 1.00 20.55 N ANISOU 3130 N SER B 77 2094 2550 3165 -52 497 -41 N ATOM 3131 CA SER B 77 109.147 -3.193 21.410 1.00 19.65 C ANISOU 3131 CA SER B 77 2018 2415 3032 -20 448 -13 C ATOM 3132 C SER B 77 109.101 -3.454 22.902 1.00 18.78 C ANISOU 3132 C SER B 77 1906 2270 2961 3 384 -2 C ATOM 3133 O SER B 77 110.119 -3.642 23.556 1.00 18.91 O ANISOU 3133 O SER B 77 1878 2274 3034 9 364 -32 O ATOM 3134 CB SER B 77 109.004 -4.519 20.658 1.00 20.00 C ANISOU 3134 CB SER B 77 2048 2472 3077 3 447 -51 C ATOM 3135 OG SER B 77 108.870 -4.323 19.246 1.00 20.55 O ANISOU 3135 OG SER B 77 2129 2581 3098 -22 506 -59 O ATOM 3136 N ALA B 78 107.873 -3.461 23.420 1.00 17.84 N ANISOU 3136 N ALA B 78 1834 2137 2807 13 351 40 N ATOM 3137 CA ALA B 78 107.563 -3.875 24.782 1.00 17.30 C ANISOU 3137 CA ALA B 78 1774 2042 2758 29 289 55 C ATOM 3138 C ALA B 78 106.829 -5.213 24.713 1.00 16.95 C ANISOU 3138 C ALA B 78 1743 1991 2705 53 253 53 C ATOM 3139 O ALA B 78 106.190 -5.520 23.707 1.00 16.83 O ANISOU 3139 O ALA B 78 1746 1993 2655 56 278 54 O ATOM 3140 CB ALA B 78 106.680 -2.837 25.454 1.00 16.98 C ANISOU 3140 CB ALA B 78 1773 1996 2682 16 283 99 C ATOM 3141 N TYR B 79 106.923 -5.993 25.787 1.00 17.07 N ANISOU 3141 N TYR B 79 1753 1981 2751 66 191 52 N ATOM 3142 CA TYR B 79 106.346 -7.342 25.828 1.00 17.04 C ANISOU 3142 CA TYR B 79 1762 1965 2748 85 148 51 C ATOM 3143 C TYR B 79 105.601 -7.576 27.120 1.00 16.53 C ANISOU 3143 C TYR B 79 1730 1883 2667 78 90 87 C ATOM 3144 O TYR B 79 106.023 -7.111 28.175 1.00 16.17 O ANISOU 3144 O TYR B 79 1679 1827 2637 66 65 97 O ATOM 3145 CB TYR B 79 107.437 -8.417 25.707 1.00 17.88 C ANISOU 3145 CB TYR B 79 1820 2051 2921 107 120 2 C ATOM 3146 CG TYR B 79 108.268 -8.279 24.463 1.00 18.61 C ANISOU 3146 CG TYR B 79 1872 2168 3033 110 179 -47 C ATOM 3147 CD1 TYR B 79 109.376 -7.433 24.437 1.00 19.42 C ANISOU 3147 CD1 TYR B 79 1934 2280 3163 96 212 -70 C ATOM 3148 CD2 TYR B 79 107.914 -8.942 23.289 1.00 19.15 C ANISOU 3148 CD2 TYR B 79 1941 2253 3084 120 206 -71 C ATOM 3149 CE1 TYR B 79 110.131 -7.278 23.282 1.00 20.11 C ANISOU 3149 CE1 TYR B 79 1983 2397 3261 90 273 -116 C ATOM 3150 CE2 TYR B 79 108.661 -8.791 22.130 1.00 19.82 C ANISOU 3150 CE2 TYR B 79 1987 2366 3176 115 266 -119 C ATOM 3151 CZ TYR B 79 109.765 -7.953 22.132 1.00 20.37 C ANISOU 3151 CZ TYR B 79 2017 2449 3272 97 300 -141 C ATOM 3152 OH TYR B 79 110.513 -7.794 20.983 1.00 21.33 O ANISOU 3152 OH TYR B 79 2101 2608 3397 83 364 -191 O ATOM 3153 N ILE B 80 104.508 -8.325 27.042 1.00 15.96 N ANISOU 3153 N ILE B 80 1692 1811 2562 81 69 106 N ATOM 3154 CA ILE B 80 103.832 -8.812 28.249 1.00 15.84 C ANISOU 3154 CA ILE B 80 1706 1782 2531 69 11 137 C ATOM 3155 C ILE B 80 103.820 -10.336 28.201 1.00 16.04 C ANISOU 3155 C ILE B 80 1732 1782 2581 83 -42 127 C ATOM 3156 O ILE B 80 103.383 -10.927 27.215 1.00 15.70 O ANISOU 3156 O ILE B 80 1692 1743 2528 98 -25 115 O ATOM 3157 CB ILE B 80 102.409 -8.235 28.462 1.00 15.68 C ANISOU 3157 CB ILE B 80 1727 1787 2444 50 27 171 C ATOM 3158 CG1 ILE B 80 101.833 -8.755 29.780 1.00 15.70 C ANISOU 3158 CG1 ILE B 80 1755 1781 2428 28 -31 197 C ATOM 3159 CG2 ILE B 80 101.476 -8.520 27.296 1.00 15.45 C ANISOU 3159 CG2 ILE B 80 1716 1774 2381 61 58 171 C ATOM 3160 CD1 ILE B 80 100.549 -8.073 30.193 1.00 15.50 C ANISOU 3160 CD1 ILE B 80 1760 1785 2344 6 -14 220 C ATOM 3161 N HIS B 81 104.344 -10.955 29.255 1.00 16.50 N ANISOU 3161 N HIS B 81 1785 1808 2674 78 -110 133 N ATOM 3162 CA HIS B 81 104.331 -12.399 29.406 1.00 17.22 C ANISOU 3162 CA HIS B 81 1883 1865 2796 88 -176 131 C ATOM 3163 C HIS B 81 103.260 -12.733 30.434 1.00 17.34 C ANISOU 3163 C HIS B 81 1948 1880 2761 54 -221 179 C ATOM 3164 O HIS B 81 103.264 -12.174 31.526 1.00 17.21 O ANISOU 3164 O HIS B 81 1944 1870 2725 26 -240 204 O ATOM 3165 CB HIS B 81 105.711 -12.892 29.854 1.00 18.15 C ANISOU 3165 CB HIS B 81 1960 1942 2992 105 -229 104 C ATOM 3166 CG HIS B 81 105.812 -14.378 30.017 1.00 19.13 C ANISOU 3166 CG HIS B 81 2089 2020 3161 118 -308 100 C ATOM 3167 ND1 HIS B 81 105.508 -15.015 31.199 1.00 19.69 N ANISOU 3167 ND1 HIS B 81 2196 2061 3225 93 -390 142 N ATOM 3168 CD2 HIS B 81 106.194 -15.349 29.155 1.00 19.82 C ANISOU 3168 CD2 HIS B 81 2148 2082 3300 153 -321 57 C ATOM 3169 CE1 HIS B 81 105.699 -16.314 31.061 1.00 20.13 C ANISOU 3169 CE1 HIS B 81 2249 2070 3330 111 -455 130 C ATOM 3170 NE2 HIS B 81 106.127 -16.542 29.833 1.00 20.35 N ANISOU 3170 NE2 HIS B 81 2235 2098 3398 151 -414 75 N ATOM 3171 N LEU B 82 102.331 -13.617 30.067 1.00 17.51 N ANISOU 3171 N LEU B 82 1996 1898 2758 53 -236 190 N ATOM 3172 CA LEU B 82 101.265 -14.060 30.967 1.00 18.15 C ANISOU 3172 CA LEU B 82 2125 1983 2790 14 -278 234 C ATOM 3173 C LEU B 82 101.462 -15.535 31.231 1.00 18.85 C ANISOU 3173 C LEU B 82 2225 2022 2917 15 -360 240 C ATOM 3174 O LEU B 82 101.574 -16.293 30.284 1.00 19.08 O ANISOU 3174 O LEU B 82 2240 2031 2979 46 -360 213 O ATOM 3175 CB LEU B 82 99.907 -13.841 30.320 1.00 18.09 C ANISOU 3175 CB LEU B 82 2141 2013 2720 7 -228 242 C ATOM 3176 CG LEU B 82 99.535 -12.389 30.038 1.00 18.13 C ANISOU 3176 CG LEU B 82 2140 2061 2687 6 -155 239 C ATOM 3177 CD1 LEU B 82 98.312 -12.313 29.134 1.00 18.28 C ANISOU 3177 CD1 LEU B 82 2176 2110 2661 10 -112 241 C ATOM 3178 CD2 LEU B 82 99.289 -11.633 31.338 1.00 18.18 C ANISOU 3178 CD2 LEU B 82 2161 2087 2661 -31 -165 263 C ATOM 3179 N ASN B 82A 101.515 -15.940 32.500 1.00 19.58 N ANISOU 3179 N ASN B 82A 2343 2094 3004 -21 -431 276 N ATOM 3180 CA ASN B 82A 101.709 -17.365 32.846 1.00 20.79 C ANISOU 3180 CA ASN B 82A 2514 2191 3196 -25 -524 290 C ATOM 3181 C ASN B 82A 100.460 -18.021 33.438 1.00 20.61 C ANISOU 3181 C ASN B 82A 2547 2175 3111 -76 -559 337 C ATOM 3182 O ASN B 82A 99.465 -17.355 33.711 1.00 19.94 O ANISOU 3182 O ASN B 82A 2484 2142 2952 -111 -514 357 O ATOM 3183 CB ASN B 82A 102.919 -17.549 33.776 1.00 22.25 C ANISOU 3183 CB ASN B 82A 2685 2333 3438 -26 -598 295 C ATOM 3184 CG ASN B 82A 102.726 -16.903 35.131 1.00 23.05 C ANISOU 3184 CG ASN B 82A 2816 2459 3485 -81 -617 337 C ATOM 3185 OD1 ASN B 82A 103.280 -15.838 35.406 1.00 24.63 O ANISOU 3185 OD1 ASN B 82A 2991 2682 3684 -78 -581 324 O ATOM 3186 ND2 ASN B 82A 101.928 -17.533 35.980 1.00 24.07 N ANISOU 3186 ND2 ASN B 82A 2997 2585 3563 -135 -671 385 N ATOM 3187 N SER B 82B 100.523 -19.344 33.602 1.00 21.11 N ANISOU 3187 N SER B 82B 2630 2183 3207 -82 -642 353 N ATOM 3188 CA SER B 82B 99.477 -20.126 34.276 1.00 21.68 C ANISOU 3188 CA SER B 82B 2759 2253 3225 -140 -692 403 C ATOM 3189 C SER B 82B 98.085 -19.798 33.749 1.00 20.46 C ANISOU 3189 C SER B 82B 2620 2156 2997 -157 -619 405 C ATOM 3190 O SER B 82B 97.169 -19.497 34.512 1.00 20.62 O ANISOU 3190 O SER B 82B 2673 2219 2944 -214 -609 437 O ATOM 3191 CB SER B 82B 99.539 -19.897 35.789 1.00 22.60 C ANISOU 3191 CB SER B 82B 2909 2377 3302 -202 -742 450 C ATOM 3192 OG SER B 82B 100.839 -20.144 36.284 1.00 24.15 O ANISOU 3192 OG SER B 82B 3089 2520 3568 -185 -813 449 O ATOM 3193 N LEU B 82C 97.935 -19.851 32.431 1.00 19.83 N ANISOU 3193 N LEU B 82C 2515 2080 2938 -109 -568 366 N ATOM 3194 CA LEU B 82C 96.743 -19.304 31.776 1.00 19.27 C ANISOU 3194 CA LEU B 82C 2449 2067 2806 -113 -490 359 C ATOM 3195 C LEU B 82C 95.460 -20.091 32.079 1.00 19.40 C ANISOU 3195 C LEU B 82C 2510 2092 2768 -163 -517 393 C ATOM 3196 O LEU B 82C 95.467 -21.328 32.123 1.00 19.44 O ANISOU 3196 O LEU B 82C 2537 2049 2801 -173 -586 407 O ATOM 3197 CB LEU B 82C 96.959 -19.196 30.263 1.00 19.02 C ANISOU 3197 CB LEU B 82C 2383 2037 2808 -54 -434 310 C ATOM 3198 CG LEU B 82C 97.969 -18.122 29.812 1.00 18.86 C ANISOU 3198 CG LEU B 82C 2317 2029 2818 -14 -380 276 C ATOM 3199 CD1 LEU B 82C 98.362 -18.324 28.354 1.00 18.97 C ANISOU 3199 CD1 LEU B 82C 2299 2038 2871 38 -341 226 C ATOM 3200 CD2 LEU B 82C 97.418 -16.720 30.048 1.00 18.46 C ANISOU 3200 CD2 LEU B 82C 2269 2037 2709 -32 -314 286 C ATOM 3201 N THR B 83 94.369 -19.362 32.295 1.00 19.58 N ANISOU 3201 N THR B 83 2544 2177 2719 -196 -464 403 N ATOM 3202 CA THR B 83 93.040 -19.947 32.490 1.00 20.16 C ANISOU 3202 CA THR B 83 2652 2275 2736 -246 -473 427 C ATOM 3203 C THR B 83 92.040 -19.248 31.574 1.00 19.88 C ANISOU 3203 C THR B 83 2600 2292 2663 -226 -392 400 C ATOM 3204 O THR B 83 92.364 -18.221 30.950 1.00 19.05 O ANISOU 3204 O THR B 83 2463 2206 2569 -183 -333 372 O ATOM 3205 CB THR B 83 92.548 -19.795 33.946 1.00 20.87 C ANISOU 3205 CB THR B 83 2772 2395 2763 -324 -498 465 C ATOM 3206 OG1 THR B 83 92.170 -18.432 34.187 1.00 21.53 O ANISOU 3206 OG1 THR B 83 2835 2541 2803 -328 -428 449 O ATOM 3207 CG2 THR B 83 93.615 -20.220 34.953 1.00 21.48 C ANISOU 3207 CG2 THR B 83 2866 2425 2871 -345 -577 494 C ATOM 3208 N SER B 84 90.811 -19.755 31.532 1.00 20.27 N ANISOU 3208 N SER B 84 2670 2364 2666 -262 -392 412 N ATOM 3209 CA SER B 84 89.756 -19.150 30.705 1.00 20.64 C ANISOU 3209 CA SER B 84 2703 2462 2679 -246 -324 388 C ATOM 3210 C SER B 84 89.472 -17.690 31.077 1.00 20.38 C ANISOU 3210 C SER B 84 2650 2483 2612 -249 -266 376 C ATOM 3211 O SER B 84 89.101 -16.901 30.210 1.00 20.57 O ANISOU 3211 O SER B 84 2652 2533 2632 -212 -210 350 O ATOM 3212 CB SER B 84 88.470 -19.970 30.790 1.00 21.29 C ANISOU 3212 CB SER B 84 2811 2563 2717 -293 -340 403 C ATOM 3213 OG SER B 84 88.028 -20.060 32.125 1.00 22.65 O ANISOU 3213 OG SER B 84 3006 2759 2840 -367 -365 433 O ATOM 3214 N GLU B 85 89.663 -17.346 32.349 1.00 20.30 N ANISOU 3214 N GLU B 85 2647 2487 2577 -294 -283 393 N ATOM 3215 CA GLU B 85 89.556 -15.961 32.826 1.00 20.15 C ANISOU 3215 CA GLU B 85 2607 2513 2535 -297 -234 377 C ATOM 3216 C GLU B 85 90.564 -15.014 32.176 1.00 19.21 C ANISOU 3216 C GLU B 85 2459 2377 2463 -235 -200 355 C ATOM 3217 O GLU B 85 90.356 -13.799 32.175 1.00 19.37 O ANISOU 3217 O GLU B 85 2459 2429 2471 -223 -152 335 O ATOM 3218 CB GLU B 85 89.777 -15.905 34.333 1.00 20.52 C ANISOU 3218 CB GLU B 85 2672 2574 2552 -359 -267 399 C ATOM 3219 N ASP B 86 91.676 -15.552 31.673 1.00 18.75 N ANISOU 3219 N ASP B 86 2397 2267 2460 -199 -228 355 N ATOM 3220 CA ASP B 86 92.655 -14.734 30.959 1.00 17.76 C ANISOU 3220 CA ASP B 86 2242 2128 2378 -145 -193 332 C ATOM 3221 C ASP B 86 92.271 -14.472 29.504 1.00 17.06 C ANISOU 3221 C ASP B 86 2139 2048 2293 -100 -144 309 C ATOM 3222 O ASP B 86 92.915 -13.641 28.872 1.00 16.34 O ANISOU 3222 O ASP B 86 2027 1956 2226 -65 -107 291 O ATOM 3223 CB ASP B 86 94.047 -15.370 31.026 1.00 18.11 C ANISOU 3223 CB ASP B 86 2280 2118 2482 -126 -239 333 C ATOM 3224 CG ASP B 86 94.552 -15.527 32.449 1.00 18.56 C ANISOU 3224 CG ASP B 86 2351 2163 2537 -168 -292 359 C ATOM 3225 OD1 ASP B 86 94.486 -14.551 33.225 1.00 19.08 O ANISOU 3225 OD1 ASP B 86 2414 2261 2575 -191 -271 361 O ATOM 3226 OD2 ASP B 86 95.047 -16.622 32.809 1.00 19.12 O ANISOU 3226 OD2 ASP B 86 2438 2190 2637 -179 -361 376 O ATOM 3227 N SER B 87 91.243 -15.143 28.964 1.00 16.41 N ANISOU 3227 N SER B 87 2071 1977 2187 -106 -145 310 N ATOM 3228 CA SER B 87 90.802 -14.870 27.603 1.00 16.21 C ANISOU 3228 CA SER B 87 2036 1964 2159 -69 -102 290 C ATOM 3229 C SER B 87 90.232 -13.462 27.559 1.00 15.66 C ANISOU 3229 C SER B 87 1954 1934 2063 -64 -53 282 C ATOM 3230 O SER B 87 89.299 -13.140 28.304 1.00 16.22 O ANISOU 3230 O SER B 87 2029 2037 2097 -96 -50 286 O ATOM 3231 CB SER B 87 89.747 -15.866 27.112 1.00 16.27 C ANISOU 3231 CB SER B 87 2061 1978 2144 -80 -117 292 C ATOM 3232 OG SER B 87 90.228 -17.200 27.214 1.00 16.75 O ANISOU 3232 OG SER B 87 2135 1996 2234 -87 -170 299 O ATOM 3233 N ALA B 88 90.781 -12.641 26.673 1.00 15.21 N ANISOU 3233 N ALA B 88 1881 1873 2024 -26 -16 268 N ATOM 3234 CA ALA B 88 90.466 -11.215 26.632 1.00 15.10 C ANISOU 3234 CA ALA B 88 1856 1883 1998 -18 23 262 C ATOM 3235 C ALA B 88 91.186 -10.582 25.457 1.00 14.99 C ANISOU 3235 C ALA B 88 1833 1859 2006 19 56 253 C ATOM 3236 O ALA B 88 92.020 -11.220 24.807 1.00 15.01 O ANISOU 3236 O ALA B 88 1831 1839 2033 35 53 246 O ATOM 3237 CB ALA B 88 90.909 -10.550 27.932 1.00 15.24 C ANISOU 3237 CB ALA B 88 1866 1904 2019 -41 16 266 C ATOM 3238 N ILE B 89 90.859 -9.320 25.191 1.00 14.82 N ANISOU 3238 N ILE B 89 1806 1852 1975 29 87 251 N ATOM 3239 CA ILE B 89 91.682 -8.498 24.326 1.00 15.07 C ANISOU 3239 CA ILE B 89 1830 1872 2024 52 118 248 C ATOM 3240 C ILE B 89 92.660 -7.736 25.224 1.00 14.90 C ANISOU 3240 C ILE B 89 1795 1839 2029 44 120 248 C ATOM 3241 O ILE B 89 92.253 -7.134 26.222 1.00 15.32 O ANISOU 3241 O ILE B 89 1844 1902 2074 28 114 249 O ATOM 3242 CB ILE B 89 90.844 -7.540 23.445 1.00 15.66 C ANISOU 3242 CB ILE B 89 1912 1961 2078 66 141 251 C ATOM 3243 CG1 ILE B 89 90.014 -8.373 22.444 1.00 16.19 C ANISOU 3243 CG1 ILE B 89 1992 2039 2120 74 137 250 C ATOM 3244 CG2 ILE B 89 91.777 -6.572 22.724 1.00 15.84 C ANISOU 3244 CG2 ILE B 89 1931 1971 2116 77 170 255 C ATOM 3245 CD1 ILE B 89 89.135 -7.608 21.479 1.00 16.66 C ANISOU 3245 CD1 ILE B 89 2061 2110 2157 88 150 256 C ATOM 3246 N TYR B 90 93.941 -7.778 24.854 1.00 14.48 N ANISOU 3246 N TYR B 90 1729 1766 2005 54 130 242 N ATOM 3247 CA TYR B 90 95.007 -7.080 25.576 1.00 14.46 C ANISOU 3247 CA TYR B 90 1710 1751 2032 48 133 240 C ATOM 3248 C TYR B 90 95.503 -5.933 24.725 1.00 14.52 C ANISOU 3248 C TYR B 90 1713 1757 2047 58 172 240 C ATOM 3249 O TYR B 90 95.775 -6.117 23.541 1.00 14.99 O ANISOU 3249 O TYR B 90 1773 1818 2104 69 194 235 O ATOM 3250 CB TYR B 90 96.150 -8.038 25.916 1.00 14.43 C ANISOU 3250 CB TYR B 90 1692 1725 2064 48 108 231 C ATOM 3251 CG TYR B 90 95.734 -9.037 26.965 1.00 14.32 C ANISOU 3251 CG TYR B 90 1689 1708 2044 29 60 239 C ATOM 3252 CD1 TYR B 90 95.038 -10.183 26.613 1.00 14.38 C ANISOU 3252 CD1 TYR B 90 1711 1715 2036 28 39 242 C ATOM 3253 CD2 TYR B 90 95.987 -8.813 28.317 1.00 14.19 C ANISOU 3253 CD2 TYR B 90 1671 1689 2031 5 34 247 C ATOM 3254 CE1 TYR B 90 94.618 -11.086 27.572 1.00 14.40 C ANISOU 3254 CE1 TYR B 90 1729 1713 2029 3 -7 255 C ATOM 3255 CE2 TYR B 90 95.571 -9.707 29.292 1.00 14.50 C ANISOU 3255 CE2 TYR B 90 1726 1728 2056 -23 -12 260 C ATOM 3256 CZ TYR B 90 94.887 -10.853 28.913 1.00 14.46 C ANISOU 3256 CZ TYR B 90 1738 1720 2037 -25 -33 266 C ATOM 3257 OH TYR B 90 94.468 -11.732 29.884 1.00 14.96 O ANISOU 3257 OH TYR B 90 1820 1781 2082 -60 -80 284 O ATOM 3258 N TYR B 91 95.583 -4.743 25.326 1.00 14.42 N ANISOU 3258 N TYR B 91 1696 1742 2041 51 180 244 N ATOM 3259 CA TYR B 91 96.059 -3.544 24.642 1.00 14.72 C ANISOU 3259 CA TYR B 91 1732 1772 2087 55 212 248 C ATOM 3260 C TYR B 91 97.350 -3.063 25.261 1.00 14.70 C ANISOU 3260 C TYR B 91 1709 1756 2121 46 217 241 C ATOM 3261 O TYR B 91 97.490 -3.052 26.478 1.00 14.17 O ANISOU 3261 O TYR B 91 1633 1686 2065 36 194 237 O ATOM 3262 CB TYR B 91 95.071 -2.385 24.783 1.00 14.87 C ANISOU 3262 CB TYR B 91 1763 1794 2093 56 214 257 C ATOM 3263 CG TYR B 91 93.746 -2.584 24.103 1.00 14.99 C ANISOU 3263 CG TYR B 91 1797 1823 2078 66 209 263 C ATOM 3264 CD1 TYR B 91 93.617 -2.418 22.730 1.00 15.48 C ANISOU 3264 CD1 TYR B 91 1874 1884 2123 75 226 276 C ATOM 3265 CD2 TYR B 91 92.624 -2.927 24.835 1.00 15.45 C ANISOU 3265 CD2 TYR B 91 1854 1896 2119 64 188 255 C ATOM 3266 CE1 TYR B 91 92.401 -2.599 22.105 1.00 15.62 C ANISOU 3266 CE1 TYR B 91 1909 1914 2114 85 217 281 C ATOM 3267 CE2 TYR B 91 91.396 -3.101 24.216 1.00 15.55 C ANISOU 3267 CE2 TYR B 91 1879 1922 2107 74 183 258 C ATOM 3268 CZ TYR B 91 91.301 -2.947 22.853 1.00 15.87 C ANISOU 3268 CZ TYR B 91 1936 1959 2136 87 195 271 C ATOM 3269 OH TYR B 91 90.079 -3.129 22.248 1.00 16.87 O ANISOU 3269 OH TYR B 91 2073 2098 2238 97 184 273 O ATOM 3270 N ACYS B 92 98.286 -2.688 24.394 0.50 15.21 N ANISOU 3270 N ACYS B 92 1765 1815 2199 45 246 239 N ATOM 3271 N BCYS B 92 98.315 -2.690 24.435 0.50 14.27 N ANISOU 3271 N BCYS B 92 1645 1695 2081 45 245 238 N ATOM 3272 CA ACYS B 92 99.443 -1.874 24.705 0.50 15.87 C ANISOU 3272 CA ACYS B 92 1830 1887 2314 34 260 233 C ATOM 3273 CA BCYS B 92 99.391 -1.855 24.907 0.50 14.33 C ANISOU 3273 CA BCYS B 92 1634 1690 2120 34 256 233 C ATOM 3274 C ACYS B 92 99.019 -0.410 24.589 0.50 15.26 C ANISOU 3274 C ACYS B 92 1768 1801 2230 27 274 250 C ATOM 3275 C BCYS B 92 99.012 -0.419 24.626 0.50 14.41 C ANISOU 3275 C BCYS B 92 1659 1693 2122 28 273 250 C ATOM 3276 O ACYS B 92 98.092 -0.079 23.826 0.50 15.14 O ANISOU 3276 O ACYS B 92 1777 1789 2188 33 279 266 O ATOM 3277 O BCYS B 92 98.131 -0.118 23.798 0.50 14.41 O ANISOU 3277 O BCYS B 92 1683 1697 2095 33 280 265 O ATOM 3278 CB ACYS B 92 100.554 -2.205 23.699 0.50 17.01 C ANISOU 3278 CB ACYS B 92 1957 2035 2472 31 290 219 C ATOM 3279 CB BCYS B 92 100.726 -2.204 24.268 0.50 14.32 C ANISOU 3279 CB BCYS B 92 1608 1688 2144 31 278 216 C ATOM 3280 SG ACYS B 92 102.060 -1.209 23.724 0.50 19.04 S ANISOU 3280 SG ACYS B 92 2187 2283 2766 12 318 209 S ATOM 3281 SG BCYS B 92 100.833 -1.867 22.507 0.50 13.98 S ANISOU 3281 SG BCYS B 92 1578 1660 2075 23 325 221 S ATOM 3282 N ALA B 93 99.672 0.464 25.352 1.00 14.67 N ANISOU 3282 N ALA B 93 1680 1712 2182 16 274 247 N ATOM 3283 CA ALA B 93 99.388 1.887 25.289 1.00 14.60 C ANISOU 3283 CA ALA B 93 1683 1687 2176 10 282 260 C ATOM 3284 C ALA B 93 100.621 2.637 25.751 1.00 14.56 C ANISOU 3284 C ALA B 93 1658 1667 2206 -7 293 252 C ATOM 3285 O ALA B 93 101.551 2.031 26.287 1.00 14.62 O ANISOU 3285 O ALA B 93 1641 1679 2236 -11 289 235 O ATOM 3286 CB ALA B 93 98.180 2.214 26.161 1.00 14.49 C ANISOU 3286 CB ALA B 93 1679 1674 2155 19 257 256 C ATOM 3287 N ARG B 94 100.629 3.946 25.526 1.00 14.73 N ANISOU 3287 N ARG B 94 1691 1668 2237 -17 303 265 N ATOM 3288 CA ARG B 94 101.758 4.794 25.877 1.00 15.00 C ANISOU 3288 CA ARG B 94 1708 1685 2304 -37 315 260 C ATOM 3289 C ARG B 94 101.229 6.009 26.621 1.00 14.76 C ANISOU 3289 C ARG B 94 1687 1632 2291 -37 297 260 C ATOM 3290 O ARG B 94 100.275 6.633 26.169 1.00 14.71 O ANISOU 3290 O ARG B 94 1704 1611 2273 -28 290 275 O ATOM 3291 CB ARG B 94 102.476 5.231 24.610 1.00 15.86 C ANISOU 3291 CB ARG B 94 1826 1792 2409 -59 349 277 C ATOM 3292 CG ARG B 94 103.909 5.674 24.812 1.00 16.50 C ANISOU 3292 CG ARG B 94 1879 1868 2524 -84 369 265 C ATOM 3293 CD ARG B 94 104.214 6.804 23.864 1.00 17.17 C ANISOU 3293 CD ARG B 94 1985 1937 2603 -115 394 292 C ATOM 3294 NE ARG B 94 103.751 8.063 24.421 1.00 17.29 N ANISOU 3294 NE ARG B 94 2017 1916 2637 -116 372 305 N ATOM 3295 CZ ARG B 94 104.019 9.258 23.907 1.00 17.95 C ANISOU 3295 CZ ARG B 94 2121 1972 2728 -144 380 329 C ATOM 3296 NH1 ARG B 94 104.703 9.386 22.767 1.00 18.58 N ANISOU 3296 NH1 ARG B 94 2210 2062 2789 -180 414 348 N ATOM 3297 NH2 ARG B 94 103.590 10.336 24.538 1.00 18.15 N ANISOU 3297 NH2 ARG B 94 2157 1959 2779 -140 354 333 N ATOM 3298 N SER B 95 101.835 6.339 27.755 1.00 14.27 N ANISOU 3298 N SER B 95 1602 1563 2257 -45 288 240 N ATOM 3299 CA SER B 95 101.434 7.518 28.522 1.00 14.14 C ANISOU 3299 CA SER B 95 1588 1523 2260 -46 272 231 C ATOM 3300 C SER B 95 102.005 8.814 27.922 1.00 14.10 C ANISOU 3300 C SER B 95 1593 1484 2280 -64 286 248 C ATOM 3301 O SER B 95 102.841 8.803 27.015 1.00 14.34 O ANISOU 3301 O SER B 95 1626 1514 2310 -83 312 266 O ATOM 3302 CB SER B 95 101.870 7.376 29.986 1.00 14.02 C ANISOU 3302 CB SER B 95 1548 1518 2262 -52 256 202 C ATOM 3303 OG SER B 95 103.195 6.889 30.071 1.00 14.12 O ANISOU 3303 OG SER B 95 1538 1537 2291 -66 265 198 O ATOM 3304 N GLY B 96 101.539 9.940 28.446 1.00 14.04 N ANISOU 3304 N GLY B 96 1591 1447 2295 -61 269 240 N ATOM 3305 CA GLY B 96 101.979 11.261 28.020 1.00 14.35 C ANISOU 3305 CA GLY B 96 1644 1446 2364 -80 272 257 C ATOM 3306 C GLY B 96 101.304 12.290 28.903 1.00 14.43 C ANISOU 3306 C GLY B 96 1651 1426 2404 -68 244 232 C ATOM 3307 O GLY B 96 101.723 12.505 30.029 1.00 14.46 O ANISOU 3307 O GLY B 96 1631 1433 2429 -74 239 201 O ATOM 3308 N SER B 97 100.274 12.949 28.386 1.00 14.48 N ANISOU 3308 N SER B 97 1682 1405 2416 -51 224 244 N ATOM 3309 CA SER B 97 99.451 13.854 29.191 1.00 14.72 C ANISOU 3309 CA SER B 97 1705 1409 2480 -32 194 210 C ATOM 3310 C SER B 97 98.470 13.100 30.091 1.00 14.18 C ANISOU 3310 C SER B 97 1615 1381 2391 -9 186 168 C ATOM 3311 O SER B 97 98.014 13.642 31.103 1.00 13.90 O ANISOU 3311 O SER B 97 1560 1342 2378 0 170 123 O ATOM 3312 CB SER B 97 98.694 14.815 28.284 1.00 15.43 C ANISOU 3312 CB SER B 97 1825 1447 2588 -21 168 235 C ATOM 3313 OG SER B 97 99.614 15.641 27.590 1.00 16.43 O ANISOU 3313 OG SER B 97 1974 1534 2734 -52 173 273 O ATOM 3314 N SER B 98 98.134 11.879 29.685 1.00 13.57 N ANISOU 3314 N SER B 98 1543 1343 2271 -2 196 182 N ATOM 3315 CA SER B 98 97.321 10.947 30.468 1.00 13.32 C ANISOU 3315 CA SER B 98 1493 1356 2210 10 192 151 C ATOM 3316 C SER B 98 98.107 9.662 30.660 1.00 12.98 C ANISOU 3316 C SER B 98 1443 1352 2136 -6 208 161 C ATOM 3317 O SER B 98 99.195 9.493 30.115 1.00 12.93 O ANISOU 3317 O SER B 98 1441 1339 2134 -21 225 186 O ATOM 3318 CB SER B 98 96.019 10.621 29.729 1.00 13.16 C ANISOU 3318 CB SER B 98 1487 1343 2170 35 180 158 C ATOM 3319 OG SER B 98 96.220 9.692 28.667 1.00 13.18 O ANISOU 3319 OG SER B 98 1510 1360 2139 33 194 198 O ATOM 3320 N ASN B 99 97.524 8.709 31.380 1.00 12.86 N ANISOU 3320 N ASN B 99 1417 1378 2092 -4 202 140 N ATOM 3321 CA ASN B 99 98.147 7.395 31.514 1.00 12.83 C ANISOU 3321 CA ASN B 99 1410 1404 2061 -16 208 152 C ATOM 3322 C ASN B 99 98.108 6.595 30.207 1.00 12.76 C ANISOU 3322 C ASN B 99 1418 1397 2031 -6 219 186 C ATOM 3323 O ASN B 99 98.911 5.690 30.037 1.00 12.71 O ANISOU 3323 O ASN B 99 1408 1403 2017 -14 226 197 O ATOM 3324 CB ASN B 99 97.497 6.579 32.634 1.00 12.81 C ANISOU 3324 CB ASN B 99 1397 1442 2028 -25 193 126 C ATOM 3325 CG ASN B 99 97.704 7.198 34.007 1.00 13.01 C ANISOU 3325 CG ASN B 99 1404 1475 2066 -43 184 90 C ATOM 3326 OD1 ASN B 99 98.715 6.906 34.700 1.00 14.07 O ANISOU 3326 OD1 ASN B 99 1529 1615 2203 -64 178 90 O ATOM 3327 ND2 ASN B 99 96.812 8.072 34.396 1.00 12.76 N ANISOU 3327 ND2 ASN B 99 1364 1441 2043 -36 181 56 N ATOM 3328 N PHE B 100 97.183 6.924 29.291 1.00 12.73 N ANISOU 3328 N PHE B 100 1433 1383 2020 12 218 199 N ATOM 3329 CA PHE B 100 96.989 6.145 28.059 1.00 12.70 C ANISOU 3329 CA PHE B 100 1448 1387 1990 20 227 227 C ATOM 3330 C PHE B 100 96.742 7.061 26.856 1.00 13.06 C ANISOU 3330 C PHE B 100 1518 1401 2042 26 230 254 C ATOM 3331 O PHE B 100 95.648 7.068 26.285 1.00 12.76 O ANISOU 3331 O PHE B 100 1495 1362 1991 43 217 261 O ATOM 3332 CB PHE B 100 95.832 5.145 28.216 1.00 12.41 C ANISOU 3332 CB PHE B 100 1413 1382 1921 32 215 217 C ATOM 3333 CG PHE B 100 95.892 4.326 29.477 1.00 12.36 C ANISOU 3333 CG PHE B 100 1389 1406 1903 19 205 194 C ATOM 3334 CD1 PHE B 100 95.277 4.771 30.643 1.00 12.63 C ANISOU 3334 CD1 PHE B 100 1408 1452 1939 13 194 162 C ATOM 3335 CD2 PHE B 100 96.519 3.093 29.496 1.00 12.33 C ANISOU 3335 CD2 PHE B 100 1383 1417 1884 10 205 204 C ATOM 3336 CE1 PHE B 100 95.328 4.019 31.805 1.00 12.74 C ANISOU 3336 CE1 PHE B 100 1411 1496 1933 -8 183 145 C ATOM 3337 CE2 PHE B 100 96.569 2.342 30.655 1.00 12.36 C ANISOU 3337 CE2 PHE B 100 1377 1444 1877 -6 187 190 C ATOM 3338 CZ PHE B 100 95.965 2.796 31.805 1.00 12.46 C ANISOU 3338 CZ PHE B 100 1381 1472 1883 -19 177 163 C ATOM 3339 N ASP B 101 97.766 7.820 26.456 1.00 13.40 N ANISOU 3339 N ASP B 101 1567 1418 2107 8 243 271 N ATOM 3340 CA ASP B 101 97.630 8.762 25.326 1.00 13.95 C ANISOU 3340 CA ASP B 101 1666 1454 2181 3 241 304 C ATOM 3341 C ASP B 101 97.403 8.086 23.974 1.00 14.31 C ANISOU 3341 C ASP B 101 1736 1515 2186 2 252 335 C ATOM 3342 O ASP B 101 96.697 8.626 23.124 1.00 14.46 O ANISOU 3342 O ASP B 101 1783 1513 2197 7 236 360 O ATOM 3343 CB ASP B 101 98.881 9.649 25.192 1.00 14.37 C ANISOU 3343 CB ASP B 101 1720 1481 2260 -26 257 318 C ATOM 3344 CG ASP B 101 98.893 10.823 26.146 1.00 14.63 C ANISOU 3344 CG ASP B 101 1742 1480 2337 -25 238 298 C ATOM 3345 OD1 ASP B 101 98.212 10.796 27.190 1.00 14.81 O ANISOU 3345 OD1 ASP B 101 1747 1510 2371 -6 220 262 O ATOM 3346 OD2 ASP B 101 99.593 11.804 25.843 1.00 15.25 O ANISOU 3346 OD2 ASP B 101 1831 1523 2439 -48 241 316 O ATOM 3347 N TYR B 102 98.063 6.950 23.768 1.00 14.45 N ANISOU 3347 N TYR B 102 1741 1566 2182 -6 277 331 N ATOM 3348 CA TYR B 102 98.053 6.218 22.497 1.00 15.08 C ANISOU 3348 CA TYR B 102 1840 1667 2224 -12 294 351 C ATOM 3349 C TYR B 102 97.830 4.753 22.798 1.00 14.74 C ANISOU 3349 C TYR B 102 1779 1659 2162 4 295 329 C ATOM 3350 O TYR B 102 98.350 4.243 23.790 1.00 14.57 O ANISOU 3350 O TYR B 102 1731 1647 2159 5 294 305 O ATOM 3351 CB TYR B 102 99.381 6.408 21.765 1.00 15.72 C ANISOU 3351 CB TYR B 102 1921 1750 2303 -47 329 364 C ATOM 3352 CG TYR B 102 99.690 7.858 21.489 1.00 16.67 C ANISOU 3352 CG TYR B 102 2061 1832 2440 -71 326 390 C ATOM 3353 CD1 TYR B 102 99.118 8.515 20.403 1.00 17.36 C ANISOU 3353 CD1 TYR B 102 2190 1900 2505 -82 315 429 C ATOM 3354 CD2 TYR B 102 100.526 8.589 22.333 1.00 17.06 C ANISOU 3354 CD2 TYR B 102 2090 1861 2529 -84 330 378 C ATOM 3355 CE1 TYR B 102 99.372 9.854 20.156 1.00 18.23 C ANISOU 3355 CE1 TYR B 102 2323 1969 2633 -107 305 458 C ATOM 3356 CE2 TYR B 102 100.790 9.927 22.095 1.00 17.71 C ANISOU 3356 CE2 TYR B 102 2193 1904 2631 -108 323 402 C ATOM 3357 CZ TYR B 102 100.210 10.556 21.009 1.00 18.25 C ANISOU 3357 CZ TYR B 102 2305 1950 2678 -120 310 444 C ATOM 3358 OH TYR B 102 100.465 11.885 20.756 1.00 19.89 O ANISOU 3358 OH TYR B 102 2537 2112 2907 -148 296 473 O ATOM 3359 N TRP B 103 97.071 4.081 21.938 1.00 14.61 N ANISOU 3359 N TRP B 103 1781 1659 2111 14 293 339 N ATOM 3360 CA TRP B 103 96.707 2.683 22.135 1.00 14.33 C ANISOU 3360 CA TRP B 103 1734 1653 2059 28 289 321 C ATOM 3361 C TRP B 103 97.061 1.864 20.920 1.00 14.70 C ANISOU 3361 C TRP B 103 1789 1720 2077 21 311 327 C ATOM 3362 O TRP B 103 96.915 2.330 19.787 1.00 15.32 O ANISOU 3362 O TRP B 103 1894 1797 2130 9 322 351 O ATOM 3363 CB TRP B 103 95.202 2.560 22.368 1.00 14.08 C ANISOU 3363 CB TRP B 103 1712 1625 2014 50 260 319 C ATOM 3364 CG TRP B 103 94.724 3.208 23.625 1.00 13.81 C ANISOU 3364 CG TRP B 103 1664 1580 2005 58 239 301 C ATOM 3365 CD1 TRP B 103 94.675 4.549 23.900 1.00 13.98 C ANISOU 3365 CD1 TRP B 103 1687 1571 2053 58 230 303 C ATOM 3366 CD2 TRP B 103 94.206 2.541 24.776 1.00 13.52 C ANISOU 3366 CD2 TRP B 103 1607 1562 1966 63 225 274 C ATOM 3367 NE1 TRP B 103 94.148 4.753 25.158 1.00 13.68 N ANISOU 3367 NE1 TRP B 103 1629 1538 2032 65 214 273 N ATOM 3368 CE2 TRP B 103 93.864 3.535 25.720 1.00 13.47 C ANISOU 3368 CE2 TRP B 103 1590 1544 1984 65 212 256 C ATOM 3369 CE3 TRP B 103 94.007 1.198 25.109 1.00 13.26 C ANISOU 3369 CE3 TRP B 103 1568 1557 1914 62 219 264 C ATOM 3370 CZ2 TRP B 103 93.318 3.222 26.970 1.00 13.26 C ANISOU 3370 CZ2 TRP B 103 1544 1539 1955 62 199 227 C ATOM 3371 CZ3 TRP B 103 93.467 0.890 26.356 1.00 13.08 C ANISOU 3371 CZ3 TRP B 103 1531 1551 1889 57 202 242 C ATOM 3372 CH2 TRP B 103 93.140 1.891 27.269 1.00 13.23 C ANISOU 3372 CH2 TRP B 103 1538 1565 1925 55 195 223 C ATOM 3373 N GLY B 104 97.491 0.623 21.148 1.00 14.89 N ANISOU 3373 N GLY B 104 1792 1763 2102 26 316 304 N ATOM 3374 CA GLY B 104 97.673 -0.322 20.048 1.00 15.24 C ANISOU 3374 CA GLY B 104 1840 1830 2120 23 335 298 C ATOM 3375 C GLY B 104 96.340 -0.874 19.585 1.00 15.27 C ANISOU 3375 C GLY B 104 1866 1845 2091 40 316 306 C ATOM 3376 O GLY B 104 95.287 -0.512 20.111 1.00 15.41 O ANISOU 3376 O GLY B 104 1893 1854 2107 53 290 314 O ATOM 3377 N GLN B 105 96.385 -1.762 18.593 1.00 15.71 N ANISOU 3377 N GLN B 105 1926 1921 2120 38 330 298 N ATOM 3378 CA GLN B 105 95.162 -2.259 17.959 1.00 15.75 C ANISOU 3378 CA GLN B 105 1954 1939 2090 50 314 306 C ATOM 3379 C GLN B 105 94.491 -3.398 18.728 1.00 15.55 C ANISOU 3379 C GLN B 105 1918 1919 2071 69 287 288 C ATOM 3380 O GLN B 105 93.411 -3.831 18.363 1.00 15.88 O ANISOU 3380 O GLN B 105 1974 1971 2087 79 271 292 O ATOM 3381 CB GLN B 105 95.427 -2.657 16.495 1.00 16.37 C ANISOU 3381 CB GLN B 105 2047 2041 2132 36 341 305 C ATOM 3382 CG GLN B 105 95.947 -4.072 16.245 1.00 16.69 C ANISOU 3382 CG GLN B 105 2066 2101 2176 41 353 268 C ATOM 3383 CD GLN B 105 97.427 -4.258 16.489 1.00 17.17 C ANISOU 3383 CD GLN B 105 2091 2162 2271 32 379 239 C ATOM 3384 OE1 GLN B 105 98.095 -3.438 17.138 1.00 17.38 O ANISOU 3384 OE1 GLN B 105 2106 2173 2326 23 384 245 O ATOM 3385 NE2 GLN B 105 97.963 -5.354 15.967 1.00 17.75 N ANISOU 3385 NE2 GLN B 105 2145 2252 2348 34 393 202 N ATOM 3386 N GLY B 106 95.166 -3.905 19.753 1.00 15.32 N ANISOU 3386 N GLY B 106 1863 1883 2075 71 280 269 N ATOM 3387 CA GLY B 106 94.661 -5.001 20.576 1.00 15.28 C ANISOU 3387 CA GLY B 106 1851 1880 2076 80 250 257 C ATOM 3388 C GLY B 106 95.140 -6.346 20.073 1.00 15.39 C ANISOU 3388 C GLY B 106 1854 1899 2093 84 251 235 C ATOM 3389 O GLY B 106 95.430 -6.509 18.881 1.00 15.97 O ANISOU 3389 O GLY B 106 1933 1986 2151 83 276 227 O ATOM 3390 N THR B 107 95.234 -7.298 20.997 1.00 15.41 N ANISOU 3390 N THR B 107 1846 1893 2117 87 221 223 N ATOM 3391 CA THR B 107 95.569 -8.698 20.706 1.00 15.60 C ANISOU 3391 CA THR B 107 1861 1913 2155 95 208 200 C ATOM 3392 C THR B 107 94.522 -9.573 21.384 1.00 15.68 C ANISOU 3392 C THR B 107 1884 1920 2153 93 168 208 C ATOM 3393 O THR B 107 94.364 -9.499 22.604 1.00 15.52 O ANISOU 3393 O THR B 107 1863 1893 2141 82 142 219 O ATOM 3394 CB THR B 107 96.961 -9.058 21.271 1.00 15.85 C ANISOU 3394 CB THR B 107 1862 1925 2236 96 200 179 C ATOM 3395 OG1 THR B 107 97.968 -8.286 20.605 1.00 15.96 O ANISOU 3395 OG1 THR B 107 1859 1945 2260 93 241 167 O ATOM 3396 CG2 THR B 107 97.274 -10.553 21.102 1.00 16.06 C ANISOU 3396 CG2 THR B 107 1876 1938 2288 108 174 151 C ATOM 3397 N THR B 108 93.834 -10.400 20.600 1.00 15.77 N ANISOU 3397 N THR B 108 1908 1941 2144 99 163 202 N ATOM 3398 CA THR B 108 92.830 -11.328 21.122 1.00 15.83 C ANISOU 3398 CA THR B 108 1929 1948 2139 93 127 208 C ATOM 3399 C THR B 108 93.528 -12.619 21.593 1.00 15.64 C ANISOU 3399 C THR B 108 1894 1896 2152 93 91 193 C ATOM 3400 O THR B 108 94.121 -13.331 20.788 1.00 16.14 O ANISOU 3400 O THR B 108 1947 1951 2235 108 95 166 O ATOM 3401 CB THR B 108 91.773 -11.662 20.044 1.00 16.29 C ANISOU 3401 CB THR B 108 2004 2025 2160 99 134 207 C ATOM 3402 OG1 THR B 108 91.161 -10.452 19.585 1.00 17.01 O ANISOU 3402 OG1 THR B 108 2106 2135 2222 100 158 222 O ATOM 3403 CG2 THR B 108 90.693 -12.587 20.604 1.00 16.49 C ANISOU 3403 CG2 THR B 108 2042 2052 2172 87 98 213 C ATOM 3404 N LEU B 109 93.459 -12.887 22.895 1.00 15.13 N ANISOU 3404 N LEU B 109 1832 1818 2097 76 53 208 N ATOM 3405 CA LEU B 109 93.957 -14.133 23.487 1.00 15.26 C ANISOU 3405 CA LEU B 109 1847 1802 2148 72 4 203 C ATOM 3406 C LEU B 109 92.786 -15.010 23.865 1.00 14.82 C ANISOU 3406 C LEU B 109 1816 1748 2066 50 -31 219 C ATOM 3407 O LEU B 109 91.897 -14.581 24.618 1.00 14.76 O ANISOU 3407 O LEU B 109 1821 1762 2023 25 -34 240 O ATOM 3408 CB LEU B 109 94.764 -13.841 24.754 1.00 15.53 C ANISOU 3408 CB LEU B 109 1872 1819 2210 58 -21 214 C ATOM 3409 CG LEU B 109 95.290 -15.048 25.555 1.00 16.25 C ANISOU 3409 CG LEU B 109 1966 1871 2339 49 -85 216 C ATOM 3410 CD1 LEU B 109 96.287 -15.855 24.735 1.00 16.73 C ANISOU 3410 CD1 LEU B 109 2003 1901 2454 80 -94 180 C ATOM 3411 CD2 LEU B 109 95.901 -14.608 26.884 1.00 16.45 C ANISOU 3411 CD2 LEU B 109 1987 1885 2377 29 -112 234 C ATOM 3412 N THR B 110 92.800 -16.240 23.351 1.00 14.69 N ANISOU 3412 N THR B 110 1804 1711 2068 59 -57 204 N ATOM 3413 CA THR B 110 91.834 -17.267 23.743 1.00 14.57 C ANISOU 3413 CA THR B 110 1813 1689 2035 34 -99 220 C ATOM 3414 C THR B 110 92.585 -18.381 24.465 1.00 14.60 C ANISOU 3414 C THR B 110 1819 1643 2085 27 -163 223 C ATOM 3415 O THR B 110 93.546 -18.930 23.923 1.00 14.78 O ANISOU 3415 O THR B 110 1823 1635 2159 56 -174 194 O ATOM 3416 CB THR B 110 91.097 -17.825 22.510 1.00 14.83 C ANISOU 3416 CB THR B 110 1852 1732 2050 48 -85 202 C ATOM 3417 OG1 THR B 110 90.441 -16.740 21.850 1.00 14.91 O ANISOU 3417 OG1 THR B 110 1862 1785 2020 56 -34 203 O ATOM 3418 CG2 THR B 110 90.058 -18.885 22.901 1.00 15.02 C ANISOU 3418 CG2 THR B 110 1900 1750 2055 19 -128 219 C ATOM 3419 N VAL B 111 92.160 -18.686 25.688 1.00 14.35 N ANISOU 3419 N VAL B 111 1810 1606 2038 -14 -206 256 N ATOM 3420 CA VAL B 111 92.734 -19.794 26.458 1.00 14.94 C ANISOU 3420 CA VAL B 111 1896 1629 2152 -30 -279 269 C ATOM 3421 C VAL B 111 91.739 -20.941 26.401 1.00 15.00 C ANISOU 3421 C VAL B 111 1933 1627 2141 -56 -317 283 C ATOM 3422 O VAL B 111 90.626 -20.827 26.927 1.00 15.65 O ANISOU 3422 O VAL B 111 2037 1742 2168 -99 -313 309 O ATOM 3423 CB VAL B 111 93.034 -19.408 27.921 1.00 15.07 C ANISOU 3423 CB VAL B 111 1922 1644 2159 -68 -309 302 C ATOM 3424 CG1 VAL B 111 93.672 -20.567 28.681 1.00 15.69 C ANISOU 3424 CG1 VAL B 111 2017 1663 2280 -85 -396 320 C ATOM 3425 CG2 VAL B 111 93.943 -18.182 27.971 1.00 15.08 C ANISOU 3425 CG2 VAL B 111 1895 1660 2176 -44 -268 288 C ATOM 3426 N SER B 112 92.127 -22.018 25.727 1.00 14.97 N ANISOU 3426 N SER B 112 1926 1579 2185 -31 -350 260 N ATOM 3427 CA SER B 112 91.249 -23.165 25.506 1.00 14.84 C ANISOU 3427 CA SER B 112 1935 1545 2159 -51 -386 268 C ATOM 3428 C SER B 112 92.063 -24.362 25.057 1.00 15.13 C ANISOU 3428 C SER B 112 1964 1516 2269 -22 -441 240 C ATOM 3429 O SER B 112 93.121 -24.190 24.452 1.00 15.18 O ANISOU 3429 O SER B 112 1935 1507 2325 25 -424 198 O ATOM 3430 CB SER B 112 90.232 -22.852 24.417 1.00 14.72 C ANISOU 3430 CB SER B 112 1917 1577 2100 -40 -328 249 C ATOM 3431 OG SER B 112 89.463 -24.006 24.106 1.00 15.14 O ANISOU 3431 OG SER B 112 1991 1611 2149 -56 -363 250 O ATOM 3432 N SER B 113 91.566 -25.560 25.358 1.00 15.34 N ANISOU 3432 N SER B 113 2022 1504 2304 -51 -506 259 N ATOM 3433 CA SER B 113 92.198 -26.794 24.908 1.00 15.73 C ANISOU 3433 CA SER B 113 2065 1483 2428 -22 -565 230 C ATOM 3434 C SER B 113 91.714 -27.251 23.526 1.00 15.92 C ANISOU 3434 C SER B 113 2079 1518 2454 8 -533 184 C ATOM 3435 O SER B 113 92.281 -28.181 22.962 1.00 16.35 O ANISOU 3435 O SER B 113 2119 1520 2574 40 -570 143 O ATOM 3436 CB SER B 113 91.985 -27.917 25.931 1.00 16.10 C ANISOU 3436 CB SER B 113 2155 1473 2491 -70 -663 276 C ATOM 3437 OG SER B 113 90.653 -28.396 25.933 1.00 16.01 O ANISOU 3437 OG SER B 113 2179 1481 2425 -117 -667 303 O ATOM 3438 N ALA B 114 90.666 -26.625 22.996 1.00 15.71 N ANISOU 3438 N ALA B 114 2057 1555 2358 -3 -469 187 N ATOM 3439 CA ALA B 114 90.166 -26.988 21.672 1.00 16.05 C ANISOU 3439 CA ALA B 114 2091 1613 2394 22 -437 145 C ATOM 3440 C ALA B 114 91.172 -26.605 20.600 1.00 16.50 C ANISOU 3440 C ALA B 114 2106 1677 2486 79 -390 85 C ATOM 3441 O ALA B 114 91.919 -25.633 20.747 1.00 16.35 O ANISOU 3441 O ALA B 114 2065 1679 2470 94 -354 82 O ATOM 3442 CB ALA B 114 88.823 -26.338 21.393 1.00 15.66 C ANISOU 3442 CB ALA B 114 2055 1630 2264 -2 -384 165 C ATOM 3443 N SER B 115 91.175 -27.367 19.517 1.00 17.23 N ANISOU 3443 N SER B 115 2186 1756 2603 105 -389 35 N ATOM 3444 CA SER B 115 92.104 -27.134 18.418 1.00 18.11 C ANISOU 3444 CA SER B 115 2257 1880 2746 152 -343 -31 C ATOM 3445 C SER B 115 91.637 -26.025 17.494 1.00 18.03 C ANISOU 3445 C SER B 115 2240 1944 2665 156 -257 -37 C ATOM 3446 O SER B 115 90.429 -25.814 17.321 1.00 17.57 O ANISOU 3446 O SER B 115 2209 1923 2546 132 -240 -9 O ATOM 3447 CB SER B 115 92.283 -28.419 17.611 1.00 18.99 C ANISOU 3447 CB SER B 115 2356 1948 2910 176 -377 -89 C ATOM 3448 OG SER B 115 92.920 -29.397 18.406 1.00 20.46 O ANISOU 3448 OG SER B 115 2543 2056 3175 180 -463 -89 O ATOM 3449 N ATHR B 116 92.599 -25.341 16.884 0.50 18.18 N ANISOU 3449 N ATHR B 116 2226 1987 2697 183 -206 -76 N ATOM 3450 N BTHR B 116 92.592 -25.314 16.892 0.50 18.19 N ANISOU 3450 N BTHR B 116 2227 1989 2697 182 -205 -75 N ATOM 3451 CA ATHR B 116 92.313 -24.348 15.867 0.50 18.26 C ANISOU 3451 CA ATHR B 116 2231 2063 2646 186 -129 -86 C ATOM 3452 CA BTHR B 116 92.266 -24.323 15.873 0.50 18.29 C ANISOU 3452 CA BTHR B 116 2235 2067 2646 184 -129 -84 C ATOM 3453 C ATHR B 116 91.612 -25.003 14.681 0.50 18.57 C ANISOU 3453 C ATHR B 116 2277 2119 2659 190 -118 -120 C ATOM 3454 C BTHR B 116 91.586 -25.009 14.704 0.50 18.58 C ANISOU 3454 C BTHR B 116 2280 2120 2661 189 -119 -119 C ATOM 3455 O ATHR B 116 91.963 -26.120 14.289 0.50 18.90 O ANISOU 3455 O ATHR B 116 2305 2125 2751 207 -148 -170 O ATOM 3456 O BTHR B 116 91.929 -26.138 14.341 0.50 18.92 O ANISOU 3456 O BTHR B 116 2309 2126 2753 206 -151 -167 O ATOM 3457 CB ATHR B 116 93.607 -23.683 15.363 0.50 18.69 C ANISOU 3457 CB ATHR B 116 2245 2134 2722 208 -81 -128 C ATOM 3458 CB BTHR B 116 93.501 -23.604 15.293 0.50 18.74 C ANISOU 3458 CB BTHR B 116 2254 2147 2721 206 -76 -125 C ATOM 3459 OG1ATHR B 116 94.462 -23.370 16.469 0.50 18.94 O ANISOU 3459 OG1ATHR B 116 2263 2136 2797 210 -105 -109 O ATOM 3460 OG1BTHR B 116 94.421 -24.575 14.798 0.50 19.53 O ANISOU 3460 OG1BTHR B 116 2320 2214 2887 234 -93 -195 O ATOM 3461 CG2ATHR B 116 93.282 -22.418 14.603 0.50 18.42 C ANISOU 3461 CG2ATHR B 116 2218 2165 2618 199 -9 -115 C ATOM 3462 CG2BTHR B 116 94.180 -22.742 16.314 0.50 18.58 C ANISOU 3462 CG2BTHR B 116 2225 2120 2716 202 -76 -93 C ATOM 3463 N LYS B 117 90.613 -24.311 14.131 1.00 18.38 N ANISOU 3463 N LYS B 117 2274 2147 2562 175 -78 -96 N ATOM 3464 CA LYS B 117 89.907 -24.767 12.949 1.00 19.05 C ANISOU 3464 CA LYS B 117 2368 2258 2613 176 -62 -126 C ATOM 3465 C LYS B 117 89.578 -23.540 12.116 1.00 18.59 C ANISOU 3465 C LYS B 117 2316 2262 2485 171 1 -114 C ATOM 3466 O LYS B 117 88.984 -22.586 12.626 1.00 17.94 O ANISOU 3466 O LYS B 117 2250 2201 2365 156 11 -62 O ATOM 3467 CB LYS B 117 88.631 -25.487 13.358 1.00 19.66 C ANISOU 3467 CB LYS B 117 2476 2319 2675 155 -109 -95 C ATOM 3468 CG LYS B 117 87.877 -26.125 12.209 1.00 20.74 C ANISOU 3468 CG LYS B 117 2622 2476 2784 156 -103 -127 C ATOM 3469 CD LYS B 117 86.712 -26.930 12.747 1.00 21.55 C ANISOU 3469 CD LYS B 117 2751 2556 2880 131 -154 -98 C ATOM 3470 CE LYS B 117 85.993 -27.688 11.652 1.00 22.69 C ANISOU 3470 CE LYS B 117 2903 2713 3004 131 -156 -134 C ATOM 3471 NZ LYS B 117 85.323 -26.768 10.706 1.00 23.29 N ANISOU 3471 NZ LYS B 117 2986 2854 3008 129 -105 -129 N ATOM 3472 N GLY B 118 89.983 -23.556 10.850 1.00 19.07 N ANISOU 3472 N GLY B 118 2363 2354 2529 180 41 -164 N ATOM 3473 CA GLY B 118 89.631 -22.487 9.919 1.00 18.94 C ANISOU 3473 CA GLY B 118 2360 2397 2441 169 95 -151 C ATOM 3474 C GLY B 118 88.173 -22.573 9.481 1.00 18.84 C ANISOU 3474 C GLY B 118 2379 2407 2374 156 83 -126 C ATOM 3475 O GLY B 118 87.564 -23.637 9.548 1.00 18.86 O ANISOU 3475 O GLY B 118 2388 2386 2391 156 44 -139 O ATOM 3476 N PRO B 119 87.606 -21.445 9.028 1.00 18.82 N ANISOU 3476 N PRO B 119 2395 2447 2310 144 112 -91 N ATOM 3477 CA PRO B 119 86.196 -21.422 8.658 1.00 18.73 C ANISOU 3477 CA PRO B 119 2410 2457 2250 134 96 -66 C ATOM 3478 C PRO B 119 85.904 -22.088 7.317 1.00 19.10 C ANISOU 3478 C PRO B 119 2464 2529 2264 132 105 -109 C ATOM 3479 O PRO B 119 86.765 -22.127 6.432 1.00 19.40 O ANISOU 3479 O PRO B 119 2491 2588 2294 133 141 -153 O ATOM 3480 CB PRO B 119 85.899 -19.928 8.543 1.00 18.60 C ANISOU 3480 CB PRO B 119 2408 2471 2187 126 121 -20 C ATOM 3481 CG PRO B 119 87.194 -19.336 8.118 1.00 18.79 C ANISOU 3481 CG PRO B 119 2419 2507 2214 126 165 -38 C ATOM 3482 CD PRO B 119 88.233 -20.120 8.868 1.00 18.84 C ANISOU 3482 CD PRO B 119 2395 2474 2289 139 155 -71 C ATOM 3483 N SER B 120 84.682 -22.590 7.197 1.00 19.21 N ANISOU 3483 N SER B 120 2496 2547 2258 125 74 -100 N ATOM 3484 CA SER B 120 84.061 -22.879 5.913 1.00 19.73 C ANISOU 3484 CA SER B 120 2576 2648 2274 118 81 -124 C ATOM 3485 C SER B 120 83.315 -21.610 5.506 1.00 19.23 C ANISOU 3485 C SER B 120 2535 2623 2149 108 93 -76 C ATOM 3486 O SER B 120 82.668 -20.977 6.336 1.00 19.65 O ANISOU 3486 O SER B 120 2593 2668 2205 108 76 -29 O ATOM 3487 CB SER B 120 83.105 -24.059 6.047 1.00 20.14 C ANISOU 3487 CB SER B 120 2633 2679 2339 116 37 -137 C ATOM 3488 OG SER B 120 83.814 -25.220 6.444 1.00 21.48 O ANISOU 3488 OG SER B 120 2785 2804 2573 126 17 -178 O ATOM 3489 N VAL B 121 83.426 -21.221 4.241 1.00 19.27 N ANISOU 3489 N VAL B 121 2554 2669 2099 98 122 -89 N ATOM 3490 CA VAL B 121 82.811 -19.983 3.761 1.00 18.90 C ANISOU 3490 CA VAL B 121 2533 2654 1995 87 126 -42 C ATOM 3491 C VAL B 121 81.777 -20.341 2.702 1.00 19.25 C ANISOU 3491 C VAL B 121 2599 2728 1987 77 108 -51 C ATOM 3492 O VAL B 121 82.114 -20.904 1.648 1.00 20.16 O ANISOU 3492 O VAL B 121 2719 2870 2073 66 127 -95 O ATOM 3493 CB VAL B 121 83.862 -18.997 3.207 1.00 19.01 C ANISOU 3493 CB VAL B 121 2551 2691 1981 74 171 -36 C ATOM 3494 CG1 VAL B 121 83.208 -17.690 2.788 1.00 18.90 C ANISOU 3494 CG1 VAL B 121 2569 2699 1915 62 165 20 C ATOM 3495 CG2 VAL B 121 84.941 -18.738 4.248 1.00 18.84 C ANISOU 3495 CG2 VAL B 121 2504 2639 2015 85 188 -34 C ATOM 3496 N PHE B 122 80.520 -20.019 2.989 1.00 18.68 N ANISOU 3496 N PHE B 122 2537 2655 1905 80 72 -13 N ATOM 3497 CA PHE B 122 79.398 -20.355 2.118 1.00 18.86 C ANISOU 3497 CA PHE B 122 2578 2704 1885 72 45 -18 C ATOM 3498 C PHE B 122 78.737 -19.083 1.610 1.00 18.83 C ANISOU 3498 C PHE B 122 2599 2723 1833 67 33 30 C ATOM 3499 O PHE B 122 78.613 -18.112 2.360 1.00 18.59 O ANISOU 3499 O PHE B 122 2564 2676 1821 76 25 72 O ATOM 3500 CB PHE B 122 78.359 -21.167 2.878 1.00 18.58 C ANISOU 3500 CB PHE B 122 2530 2647 1884 79 6 -21 C ATOM 3501 CG PHE B 122 78.888 -22.444 3.455 1.00 18.75 C ANISOU 3501 CG PHE B 122 2531 2636 1957 83 4 -61 C ATOM 3502 CD1 PHE B 122 79.424 -23.429 2.632 1.00 19.17 C ANISOU 3502 CD1 PHE B 122 2584 2693 2006 80 16 -117 C ATOM 3503 CD2 PHE B 122 78.843 -22.670 4.828 1.00 18.30 C ANISOU 3503 CD2 PHE B 122 2457 2542 1953 87 -13 -45 C ATOM 3504 CE1 PHE B 122 79.905 -24.616 3.168 1.00 19.35 C ANISOU 3504 CE1 PHE B 122 2588 2677 2086 86 5 -155 C ATOM 3505 CE2 PHE B 122 79.324 -23.853 5.371 1.00 18.47 C ANISOU 3505 CE2 PHE B 122 2466 2527 2024 87 -24 -76 C ATOM 3506 CZ PHE B 122 79.858 -24.826 4.538 1.00 18.89 C ANISOU 3506 CZ PHE B 122 2518 2578 2082 89 -18 -131 C ATOM 3507 N PRO B 123 78.281 -19.083 0.346 1.00 19.35 N ANISOU 3507 N PRO B 123 2691 2824 1838 52 24 25 N ATOM 3508 CA PRO B 123 77.617 -17.896 -0.174 1.00 19.32 C ANISOU 3508 CA PRO B 123 2713 2835 1790 46 1 75 C ATOM 3509 C PRO B 123 76.207 -17.705 0.383 1.00 19.15 C ANISOU 3509 C PRO B 123 2683 2802 1792 64 -51 99 C ATOM 3510 O PRO B 123 75.495 -18.684 0.644 1.00 19.22 O ANISOU 3510 O PRO B 123 2675 2807 1820 69 -70 72 O ATOM 3511 CB PRO B 123 77.554 -18.160 -1.682 1.00 20.02 C ANISOU 3511 CB PRO B 123 2833 2967 1806 20 3 57 C ATOM 3512 CG PRO B 123 77.512 -19.642 -1.796 1.00 20.18 C ANISOU 3512 CG PRO B 123 2835 2990 1841 22 8 -4 C ATOM 3513 CD PRO B 123 78.313 -20.177 -0.644 1.00 19.77 C ANISOU 3513 CD PRO B 123 2750 2902 1861 39 31 -27 C ATOM 3514 N LEU B 124 75.839 -16.441 0.577 1.00 19.02 N ANISOU 3514 N LEU B 124 2675 2777 1775 71 -72 146 N ATOM 3515 CA LEU B 124 74.472 -16.036 0.850 1.00 19.20 C ANISOU 3515 CA LEU B 124 2688 2794 1811 87 -123 166 C ATOM 3516 C LEU B 124 74.052 -15.381 -0.453 1.00 20.17 C ANISOU 3516 C LEU B 124 2850 2939 1873 75 -153 193 C ATOM 3517 O LEU B 124 74.314 -14.200 -0.694 1.00 19.84 O ANISOU 3517 O LEU B 124 2831 2890 1816 72 -161 236 O ATOM 3518 CB LEU B 124 74.396 -15.074 2.035 1.00 18.57 C ANISOU 3518 CB LEU B 124 2587 2686 1784 107 -129 193 C ATOM 3519 CG LEU B 124 74.774 -15.686 3.396 1.00 17.96 C ANISOU 3519 CG LEU B 124 2474 2589 1762 113 -104 171 C ATOM 3520 CD1 LEU B 124 75.064 -14.617 4.442 1.00 17.76 C ANISOU 3520 CD1 LEU B 124 2433 2538 1776 127 -98 197 C ATOM 3521 CD2 LEU B 124 73.676 -16.623 3.883 1.00 17.91 C ANISOU 3521 CD2 LEU B 124 2442 2587 1777 115 -129 145 C ATOM 3522 N ALA B 125 73.448 -16.191 -1.315 1.00 21.24 N ANISOU 3522 N ALA B 125 2996 3101 1972 64 -172 169 N ATOM 3523 CA ALA B 125 73.242 -15.835 -2.712 1.00 22.54 C ANISOU 3523 CA ALA B 125 3204 3295 2064 42 -194 188 C ATOM 3524 C ALA B 125 72.075 -14.879 -2.859 1.00 23.18 C ANISOU 3524 C ALA B 125 3294 3367 2147 57 -261 229 C ATOM 3525 O ALA B 125 70.999 -15.148 -2.318 1.00 22.85 O ANISOU 3525 O ALA B 125 3220 3316 2145 80 -296 215 O ATOM 3526 CB ALA B 125 72.990 -17.093 -3.526 1.00 22.86 C ANISOU 3526 CB ALA B 125 3251 3368 2069 26 -192 142 C ATOM 3527 N PRO B 126 72.267 -13.769 -3.611 1.00 24.39 N ANISOU 3527 N PRO B 126 3488 3520 2257 42 -283 278 N ATOM 3528 CA PRO B 126 71.134 -12.893 -3.871 1.00 25.24 C ANISOU 3528 CA PRO B 126 3607 3615 2370 58 -358 315 C ATOM 3529 C PRO B 126 70.141 -13.559 -4.828 1.00 26.38 C ANISOU 3529 C PRO B 126 3762 3788 2471 49 -402 299 C ATOM 3530 O PRO B 126 70.523 -14.362 -5.679 1.00 26.28 O ANISOU 3530 O PRO B 126 3773 3812 2400 19 -376 275 O ATOM 3531 CB PRO B 126 71.780 -11.660 -4.499 1.00 25.67 C ANISOU 3531 CB PRO B 126 3711 3661 2383 35 -368 373 C ATOM 3532 CG PRO B 126 72.985 -12.193 -5.203 1.00 25.76 C ANISOU 3532 CG PRO B 126 3751 3707 2330 -8 -304 358 C ATOM 3533 CD PRO B 126 73.460 -13.362 -4.380 1.00 24.98 C ANISOU 3533 CD PRO B 126 3605 3612 2273 5 -245 298 C ATOM 3534 N SER B 127 68.872 -13.257 -4.628 1.00 27.42 N ANISOU 3534 N SER B 127 3873 3907 2638 78 -466 304 N ATOM 3535 CA SER B 127 67.794 -13.801 -5.435 1.00 28.71 C ANISOU 3535 CA SER B 127 4041 4095 2772 74 -518 289 C ATOM 3536 C SER B 127 66.615 -12.864 -5.232 1.00 29.66 C ANISOU 3536 C SER B 127 4144 4187 2936 108 -598 314 C ATOM 3537 O SER B 127 66.756 -11.846 -4.542 1.00 29.92 O ANISOU 3537 O SER B 127 4165 4185 3018 130 -607 340 O ATOM 3538 CB SER B 127 67.467 -15.232 -4.986 1.00 28.46 C ANISOU 3538 CB SER B 127 3970 4082 2764 78 -488 227 C ATOM 3539 OG SER B 127 66.898 -15.246 -3.683 1.00 28.13 O ANISOU 3539 OG SER B 127 3870 4016 2802 109 -489 208 O ATOM 3540 N ASER B 128 65.474 -13.212 -5.822 0.50 29.85 N ANISOU 3540 N ASER B 128 4163 4229 2950 112 -656 301 N ATOM 3541 N BSER B 128 65.464 -13.186 -5.818 0.50 30.43 N ANISOU 3541 N BSER B 128 4236 4301 3023 113 -657 302 N ATOM 3542 CA ASER B 128 64.233 -12.457 -5.669 0.50 30.05 C ANISOU 3542 CA ASER B 128 4163 4231 3025 147 -738 312 C ATOM 3543 CA BSER B 128 64.269 -12.349 -5.679 0.50 31.02 C ANISOU 3543 CA BSER B 128 4288 4352 3148 148 -741 317 C ATOM 3544 C ASER B 128 63.769 -12.381 -4.216 0.50 29.56 C ANISOU 3544 C ASER B 128 4028 4148 3056 185 -725 278 C ATOM 3545 C BSER B 128 63.723 -12.364 -4.253 0.50 30.63 C ANISOU 3545 C BSER B 128 4164 4283 3191 186 -729 278 C ATOM 3546 O ASER B 128 63.275 -11.347 -3.771 0.50 29.55 O ANISOU 3546 O ASER B 128 4004 4114 3110 217 -772 292 O ATOM 3547 O BSER B 128 63.927 -11.417 -3.494 0.50 30.60 O ANISOU 3547 O BSER B 128 4143 4246 3239 209 -731 295 O ATOM 3548 CB ASER B 128 63.136 -13.104 -6.512 0.50 30.42 C ANISOU 3548 CB ASER B 128 4209 4306 3042 143 -794 291 C ATOM 3549 CB BSER B 128 63.180 -12.805 -6.646 0.50 31.71 C ANISOU 3549 CB BSER B 128 4383 4464 3202 143 -805 306 C ATOM 3550 OG ASER B 128 63.032 -14.489 -6.228 0.50 29.83 O ANISOU 3550 OG ASER B 128 4103 4262 2968 132 -745 234 O ATOM 3551 OG BSER B 128 62.044 -11.960 -6.558 0.50 32.41 O ANISOU 3551 OG BSER B 128 4445 4525 3342 179 -892 317 O ATOM 3552 N SER B 132 64.690 -6.098 -2.298 1.00 30.27 N ANISOU 3552 N SER B 132 4126 4017 3359 293 -860 438 N ATOM 3553 CA SER B 132 63.829 -5.218 -1.512 1.00 30.48 C ANISOU 3553 CA SER B 132 4096 4004 3480 344 -915 415 C ATOM 3554 C SER B 132 63.970 -3.770 -1.979 1.00 30.24 C ANISOU 3554 C SER B 132 4109 3914 3467 355 -991 476 C ATOM 3555 O SER B 132 64.960 -3.107 -1.668 1.00 30.34 O ANISOU 3555 O SER B 132 4147 3898 3481 344 -959 508 O ATOM 3556 CB SER B 132 64.168 -5.317 -0.016 1.00 30.44 C ANISOU 3556 CB SER B 132 4031 4000 3535 360 -843 368 C ATOM 3557 OG SER B 132 63.374 -4.425 0.761 1.00 31.76 O ANISOU 3557 OG SER B 132 4140 4133 3795 407 -892 338 O ATOM 3558 N GLY B 133 62.985 -3.282 -2.728 1.00 30.13 N ANISOU 3558 N GLY B 133 4105 3877 3467 375 -1094 493 N ATOM 3559 CA GLY B 133 62.972 -1.885 -3.149 1.00 30.06 C ANISOU 3559 CA GLY B 133 4134 3801 3484 388 -1183 551 C ATOM 3560 C GLY B 133 64.062 -1.496 -4.131 1.00 29.74 C ANISOU 3560 C GLY B 133 4194 3752 3356 333 -1181 636 C ATOM 3561 O GLY B 133 64.568 -0.376 -4.079 1.00 30.39 O ANISOU 3561 O GLY B 133 4308 3779 3460 333 -1211 683 O ATOM 3562 N GLY B 134 64.432 -2.415 -5.019 1.00 28.78 N ANISOU 3562 N GLY B 134 4119 3684 3133 283 -1143 651 N ATOM 3563 CA GLY B 134 65.526 -2.179 -5.970 1.00 28.54 C ANISOU 3563 CA GLY B 134 4179 3660 3006 219 -1125 722 C ATOM 3564 C GLY B 134 66.922 -2.414 -5.411 1.00 27.37 C ANISOU 3564 C GLY B 134 4035 3531 2832 189 -1011 718 C ATOM 3565 O GLY B 134 67.915 -2.154 -6.090 1.00 27.55 O ANISOU 3565 O GLY B 134 4126 3561 2781 134 -986 770 O ATOM 3566 N THR B 135 66.994 -2.903 -4.175 1.00 25.84 N ANISOU 3566 N THR B 135 3770 3347 2699 221 -943 654 N ATOM 3567 CA THR B 135 68.249 -3.236 -3.514 1.00 24.71 C ANISOU 3567 CA THR B 135 3622 3222 2544 199 -837 641 C ATOM 3568 C THR B 135 68.327 -4.748 -3.340 1.00 23.58 C ANISOU 3568 C THR B 135 3448 3141 2372 188 -761 583 C ATOM 3569 O THR B 135 67.347 -5.384 -2.940 1.00 23.46 O ANISOU 3569 O THR B 135 3379 3140 2394 219 -774 533 O ATOM 3570 CB THR B 135 68.327 -2.560 -2.131 1.00 24.45 C ANISOU 3570 CB THR B 135 3534 3148 2609 242 -822 616 C ATOM 3571 OG1 THR B 135 68.250 -1.140 -2.292 1.00 25.61 O ANISOU 3571 OG1 THR B 135 3709 3231 2792 254 -899 668 O ATOM 3572 CG2 THR B 135 69.617 -2.911 -1.412 1.00 23.87 C ANISOU 3572 CG2 THR B 135 3453 3092 2526 220 -718 602 C ATOM 3573 N ALA B 136 69.497 -5.309 -3.636 1.00 22.68 N ANISOU 3573 N ALA B 136 3365 3061 2192 143 -683 588 N ATOM 3574 CA ALA B 136 69.779 -6.720 -3.407 1.00 21.63 C ANISOU 3574 CA ALA B 136 3204 2977 2037 133 -607 533 C ATOM 3575 C ALA B 136 70.713 -6.846 -2.217 1.00 20.43 C ANISOU 3575 C ALA B 136 3017 2818 1929 140 -529 507 C ATOM 3576 O ALA B 136 71.632 -6.051 -2.074 1.00 20.24 O ANISOU 3576 O ALA B 136 3016 2771 1905 126 -508 540 O ATOM 3577 CB ALA B 136 70.423 -7.330 -4.635 1.00 22.03 C ANISOU 3577 CB ALA B 136 3310 3073 1987 78 -578 546 C ATOM 3578 N ALA B 137 70.465 -7.849 -1.375 1.00 19.43 N ANISOU 3578 N ALA B 137 2837 2710 1838 158 -490 450 N ATOM 3579 CA ALA B 137 71.407 -8.245 -0.322 1.00 18.51 C ANISOU 3579 CA ALA B 137 2690 2594 1750 158 -413 423 C ATOM 3580 C ALA B 137 72.096 -9.548 -0.707 1.00 18.23 C ANISOU 3580 C ALA B 137 2663 2598 1664 128 -353 393 C ATOM 3581 O ALA B 137 71.474 -10.453 -1.258 1.00 18.37 O ANISOU 3581 O ALA B 137 2680 2645 1654 122 -365 368 O ATOM 3582 CB ALA B 137 70.686 -8.414 1.005 1.00 18.07 C ANISOU 3582 CB ALA B 137 2569 2527 1772 195 -415 382 C ATOM 3583 N LEU B 138 73.384 -9.629 -0.395 1.00 17.94 N ANISOU 3583 N LEU B 138 2631 2562 1622 110 -289 391 N ATOM 3584 CA LEU B 138 74.183 -10.834 -0.588 1.00 17.83 C ANISOU 3584 CA LEU B 138 2617 2580 1579 87 -229 354 C ATOM 3585 C LEU B 138 75.216 -10.890 0.523 1.00 17.23 C ANISOU 3585 C LEU B 138 2513 2488 1547 92 -173 340 C ATOM 3586 O LEU B 138 75.410 -9.919 1.252 1.00 17.07 O ANISOU 3586 O LEU B 138 2483 2436 1567 107 -178 363 O ATOM 3587 CB LEU B 138 74.849 -10.831 -1.980 1.00 18.55 C ANISOU 3587 CB LEU B 138 2761 2702 1586 44 -214 372 C ATOM 3588 CG LEU B 138 75.797 -9.663 -2.300 1.00 19.14 C ANISOU 3588 CG LEU B 138 2873 2765 1635 18 -201 420 C ATOM 3589 CD1 LEU B 138 77.257 -10.072 -2.199 1.00 19.24 C ANISOU 3589 CD1 LEU B 138 2881 2794 1634 -8 -123 396 C ATOM 3590 CD2 LEU B 138 75.544 -9.094 -3.688 1.00 20.13 C ANISOU 3590 CD2 LEU B 138 3058 2907 1683 -18 -243 464 C ATOM 3591 N GLY B 139 75.879 -12.025 0.664 1.00 16.96 N ANISOU 3591 N GLY B 139 2464 2471 1510 82 -125 299 N ATOM 3592 CA GLY B 139 76.822 -12.171 1.761 1.00 16.66 C ANISOU 3592 CA GLY B 139 2397 2414 1518 89 -79 283 C ATOM 3593 C GLY B 139 77.620 -13.447 1.747 1.00 16.77 C ANISOU 3593 C GLY B 139 2400 2444 1529 77 -33 237 C ATOM 3594 O GLY B 139 77.582 -14.212 0.778 1.00 17.01 O ANISOU 3594 O GLY B 139 2446 2503 1516 61 -29 213 O ATOM 3595 N CYS B 140 78.330 -13.660 2.851 1.00 16.71 N ANISOU 3595 N CYS B 140 2362 2415 1571 87 -4 222 N ATOM 3596 CA CYS B 140 79.083 -14.883 3.088 1.00 16.97 C ANISOU 3596 CA CYS B 140 2377 2450 1622 83 30 177 C ATOM 3597 C CYS B 140 78.817 -15.317 4.510 1.00 16.20 C ANISOU 3597 C CYS B 140 2245 2325 1585 101 21 167 C ATOM 3598 O CYS B 140 78.855 -14.504 5.424 1.00 15.57 O ANISOU 3598 O CYS B 140 2153 2226 1537 111 18 191 O ATOM 3599 CB CYS B 140 80.576 -14.661 2.877 1.00 17.78 C ANISOU 3599 CB CYS B 140 2484 2556 1718 68 79 170 C ATOM 3600 SG CYS B 140 81.024 -14.630 1.140 1.00 19.64 S ANISOU 3600 SG CYS B 140 2755 2835 1871 33 101 162 S ATOM 3601 N LEU B 141 78.534 -16.601 4.663 1.00 16.28 N ANISOU 3601 N LEU B 141 2242 2336 1608 100 14 132 N ATOM 3602 CA LEU B 141 78.392 -17.228 5.966 1.00 16.06 C ANISOU 3602 CA LEU B 141 2186 2284 1632 106 7 121 C ATOM 3603 C LEU B 141 79.742 -17.857 6.272 1.00 16.13 C ANISOU 3603 C LEU B 141 2186 2275 1669 104 37 97 C ATOM 3604 O LEU B 141 80.210 -18.727 5.545 1.00 16.34 O ANISOU 3604 O LEU B 141 2216 2308 1684 99 49 61 O ATOM 3605 CB LEU B 141 77.270 -18.266 5.923 1.00 16.40 C ANISOU 3605 CB LEU B 141 2223 2333 1674 102 -24 101 C ATOM 3606 CG LEU B 141 77.060 -19.125 7.167 1.00 16.40 C ANISOU 3606 CG LEU B 141 2201 2311 1718 97 -36 89 C ATOM 3607 CD1 LEU B 141 76.620 -18.292 8.353 1.00 16.36 C ANISOU 3607 CD1 LEU B 141 2178 2300 1738 99 -44 115 C ATOM 3608 CD2 LEU B 141 76.029 -20.200 6.850 1.00 16.61 C ANISOU 3608 CD2 LEU B 141 2227 2347 1736 87 -64 67 C ATOM 3609 N VAL B 142 80.363 -17.383 7.353 1.00 15.64 N ANISOU 3609 N VAL B 142 2109 2190 1644 109 48 112 N ATOM 3610 CA VAL B 142 81.697 -17.786 7.769 1.00 15.90 C ANISOU 3610 CA VAL B 142 2128 2202 1710 110 72 92 C ATOM 3611 C VAL B 142 81.533 -18.718 8.963 1.00 15.88 C ANISOU 3611 C VAL B 142 2109 2171 1753 108 49 84 C ATOM 3612 O VAL B 142 81.362 -18.267 10.089 1.00 15.35 O ANISOU 3612 O VAL B 142 2032 2091 1708 107 40 107 O ATOM 3613 CB VAL B 142 82.544 -16.546 8.121 1.00 15.91 C ANISOU 3613 CB VAL B 142 2128 2199 1720 112 98 118 C ATOM 3614 CG1 VAL B 142 83.939 -16.964 8.559 1.00 16.09 C ANISOU 3614 CG1 VAL B 142 2133 2201 1781 114 121 94 C ATOM 3615 CG2 VAL B 142 82.617 -15.609 6.913 1.00 16.32 C ANISOU 3615 CG2 VAL B 142 2203 2277 1720 105 115 134 C ATOM 3616 N LYS B 143 81.563 -20.019 8.700 1.00 16.65 N ANISOU 3616 N LYS B 143 2205 2259 1863 106 36 50 N ATOM 3617 CA LYS B 143 81.040 -21.003 9.645 1.00 17.26 C ANISOU 3617 CA LYS B 143 2275 2311 1971 96 1 47 C ATOM 3618 C LYS B 143 82.103 -21.934 10.222 1.00 16.98 C ANISOU 3618 C LYS B 143 2229 2236 1988 98 -6 25 C ATOM 3619 O LYS B 143 83.035 -22.337 9.534 1.00 17.03 O ANISOU 3619 O LYS B 143 2230 2236 2005 109 10 -11 O ATOM 3620 CB LYS B 143 79.945 -21.823 8.960 1.00 18.64 C ANISOU 3620 CB LYS B 143 2460 2501 2123 88 -22 30 C ATOM 3621 CG LYS B 143 79.176 -22.730 9.903 1.00 19.54 C ANISOU 3621 CG LYS B 143 2570 2594 2260 69 -59 35 C ATOM 3622 CD LYS B 143 77.706 -22.825 9.564 1.00 20.29 C ANISOU 3622 CD LYS B 143 2669 2717 2323 58 -78 39 C ATOM 3623 CE LYS B 143 77.101 -24.102 10.093 1.00 20.95 C ANISOU 3623 CE LYS B 143 2753 2781 2426 33 -113 29 C ATOM 3624 NZ LYS B 143 77.013 -24.139 11.566 1.00 21.05 N ANISOU 3624 NZ LYS B 143 2759 2777 2464 10 -128 55 N ATOM 3625 N ASP B 144 81.929 -22.267 11.502 1.00 16.31 N ANISOU 3625 N ASP B 144 2140 2125 1933 85 -34 45 N ATOM 3626 CA ASP B 144 82.649 -23.354 12.165 1.00 16.58 C ANISOU 3626 CA ASP B 144 2169 2112 2018 81 -62 30 C ATOM 3627 C ASP B 144 84.153 -23.145 12.273 1.00 16.43 C ANISOU 3627 C ASP B 144 2135 2072 2036 100 -44 14 C ATOM 3628 O ASP B 144 84.943 -23.998 11.858 1.00 17.02 O ANISOU 3628 O ASP B 144 2201 2121 2146 113 -51 -26 O ATOM 3629 CB ASP B 144 82.314 -24.702 11.493 1.00 17.16 C ANISOU 3629 CB ASP B 144 2249 2170 2100 79 -88 -6 C ATOM 3630 CG ASP B 144 80.863 -25.113 11.679 1.00 17.46 C ANISOU 3630 CG ASP B 144 2300 2221 2114 53 -115 11 C ATOM 3631 OD1 ASP B 144 80.146 -24.533 12.527 1.00 17.86 O ANISOU 3631 OD1 ASP B 144 2351 2287 2148 34 -119 47 O ATOM 3632 OD2 ASP B 144 80.432 -26.053 10.967 1.00 18.71 O ANISOU 3632 OD2 ASP B 144 2464 2374 2269 51 -133 -17 O ATOM 3633 N TYR B 145 84.534 -22.025 12.885 1.00 15.72 N ANISOU 3633 N TYR B 145 2039 1990 1944 101 -23 43 N ATOM 3634 CA TYR B 145 85.942 -21.720 13.102 1.00 15.69 C ANISOU 3634 CA TYR B 145 2018 1968 1975 115 -6 31 C ATOM 3635 C TYR B 145 86.246 -21.548 14.579 1.00 15.35 C ANISOU 3635 C TYR B 145 1971 1897 1962 104 -29 62 C ATOM 3636 O TYR B 145 85.353 -21.298 15.385 1.00 14.96 O ANISOU 3636 O TYR B 145 1932 1857 1894 82 -45 96 O ATOM 3637 CB TYR B 145 86.364 -20.479 12.314 1.00 15.66 C ANISOU 3637 CB TYR B 145 2010 2000 1939 125 45 32 C ATOM 3638 CG TYR B 145 85.731 -19.182 12.754 1.00 15.40 C ANISOU 3638 CG TYR B 145 1987 1991 1876 117 57 76 C ATOM 3639 CD1 TYR B 145 84.525 -18.755 12.199 1.00 15.39 C ANISOU 3639 CD1 TYR B 145 2001 2020 1828 112 58 92 C ATOM 3640 CD2 TYR B 145 86.331 -18.378 13.717 1.00 15.13 C ANISOU 3640 CD2 TYR B 145 1942 1945 1861 116 64 99 C ATOM 3641 CE1 TYR B 145 83.936 -17.567 12.586 1.00 15.18 C ANISOU 3641 CE1 TYR B 145 1977 2009 1782 110 64 126 C ATOM 3642 CE2 TYR B 145 85.754 -17.183 14.119 1.00 14.91 C ANISOU 3642 CE2 TYR B 145 1919 1935 1810 111 73 133 C ATOM 3643 CZ TYR B 145 84.547 -16.784 13.562 1.00 14.87 C ANISOU 3643 CZ TYR B 145 1928 1958 1766 109 72 145 C ATOM 3644 OH TYR B 145 83.945 -15.606 13.921 1.00 15.07 O ANISOU 3644 OH TYR B 145 1953 1996 1775 109 76 171 O ATOM 3645 N PHE B 146 87.526 -21.679 14.918 1.00 15.43 N ANISOU 3645 N PHE B 146 1964 1879 2020 116 -32 46 N ATOM 3646 CA PHE B 146 87.980 -21.496 16.294 1.00 15.54 C ANISOU 3646 CA PHE B 146 1975 1867 2064 105 -56 75 C ATOM 3647 C PHE B 146 89.462 -21.152 16.281 1.00 15.81 C ANISOU 3647 C PHE B 146 1984 1885 2138 126 -38 52 C ATOM 3648 O PHE B 146 90.186 -21.771 15.506 1.00 16.00 O ANISOU 3648 O PHE B 146 1991 1897 2192 145 -33 6 O ATOM 3649 CB PHE B 146 87.765 -22.771 17.118 1.00 15.73 C ANISOU 3649 CB PHE B 146 2011 1846 2120 87 -118 82 C ATOM 3650 CG PHE B 146 87.982 -22.559 18.585 1.00 15.57 C ANISOU 3650 CG PHE B 146 1996 1807 2114 64 -147 120 C ATOM 3651 CD1 PHE B 146 86.990 -21.976 19.364 1.00 15.48 C ANISOU 3651 CD1 PHE B 146 1997 1824 2059 32 -144 158 C ATOM 3652 CD2 PHE B 146 89.192 -22.892 19.192 1.00 15.81 C ANISOU 3652 CD2 PHE B 146 2014 1794 2201 73 -176 113 C ATOM 3653 CE1 PHE B 146 87.197 -21.738 20.718 1.00 15.43 C ANISOU 3653 CE1 PHE B 146 1997 1808 2060 6 -167 190 C ATOM 3654 CE2 PHE B 146 89.404 -22.643 20.544 1.00 15.84 C ANISOU 3654 CE2 PHE B 146 2024 1783 2211 48 -204 150 C ATOM 3655 CZ PHE B 146 88.402 -22.072 21.307 1.00 15.71 C ANISOU 3655 CZ PHE B 146 2025 1800 2145 12 -198 189 C ATOM 3656 N PRO B 147 89.940 -20.198 17.091 1.00 16.05 N ANISOU 3656 N PRO B 147 2008 1918 2173 121 -26 78 N ATOM 3657 CA PRO B 147 89.182 -19.287 17.945 1.00 15.93 C ANISOU 3657 CA PRO B 147 2006 1924 2124 100 -23 122 C ATOM 3658 C PRO B 147 88.791 -18.027 17.172 1.00 16.15 C ANISOU 3658 C PRO B 147 2035 1994 2107 106 27 129 C ATOM 3659 O PRO B 147 89.046 -17.948 15.985 1.00 16.34 O ANISOU 3659 O PRO B 147 2055 2033 2119 121 57 105 O ATOM 3660 CB PRO B 147 90.234 -18.901 18.996 1.00 15.90 C ANISOU 3660 CB PRO B 147 1988 1897 2157 98 -33 133 C ATOM 3661 CG PRO B 147 91.479 -18.819 18.195 1.00 16.12 C ANISOU 3661 CG PRO B 147 1990 1917 2216 125 -6 94 C ATOM 3662 CD PRO B 147 91.391 -19.943 17.196 1.00 16.42 C ANISOU 3662 CD PRO B 147 2027 1947 2265 138 -14 56 C ATOM 3663 N GLU B 148 88.212 -17.049 17.848 1.00 16.67 N ANISOU 3663 N GLU B 148 2106 2078 2150 94 34 160 N ATOM 3664 CA GLU B 148 88.137 -15.682 17.303 1.00 17.33 C ANISOU 3664 CA GLU B 148 2189 2189 2206 102 75 170 C ATOM 3665 C GLU B 148 89.548 -15.127 17.182 1.00 17.73 C ANISOU 3665 C GLU B 148 2223 2229 2283 113 101 159 C ATOM 3666 O GLU B 148 90.422 -15.585 17.913 1.00 18.07 O ANISOU 3666 O GLU B 148 2252 2245 2367 113 83 151 O ATOM 3667 CB GLU B 148 87.331 -14.792 18.238 1.00 17.95 C ANISOU 3667 CB GLU B 148 2270 2281 2269 89 70 197 C ATOM 3668 CG GLU B 148 85.846 -15.078 18.207 1.00 18.70 C ANISOU 3668 CG GLU B 148 2376 2397 2333 78 54 203 C ATOM 3669 CD GLU B 148 85.115 -14.211 17.193 1.00 19.83 C ANISOU 3669 CD GLU B 148 2526 2566 2445 91 74 206 C ATOM 3670 OE1 GLU B 148 84.242 -13.441 17.641 1.00 21.28 O ANISOU 3670 OE1 GLU B 148 2705 2765 2615 87 72 217 O ATOM 3671 OE2 GLU B 148 85.410 -14.285 15.969 1.00 20.54 O ANISOU 3671 OE2 GLU B 148 2623 2660 2522 104 90 196 O ATOM 3672 N PRO B 149 89.804 -14.156 16.300 1.00 17.76 N ANISOU 3672 N PRO B 149 2229 2254 2267 119 139 160 N ATOM 3673 CA PRO B 149 88.840 -13.501 15.422 1.00 17.79 C ANISOU 3673 CA PRO B 149 2251 2284 2224 119 153 174 C ATOM 3674 C PRO B 149 88.989 -13.935 13.962 1.00 18.17 C ANISOU 3674 C PRO B 149 2306 2350 2247 123 173 150 C ATOM 3675 O PRO B 149 89.921 -14.660 13.627 1.00 18.62 O ANISOU 3675 O PRO B 149 2348 2400 2326 127 183 117 O ATOM 3676 CB PRO B 149 89.261 -12.042 15.547 1.00 17.77 C ANISOU 3676 CB PRO B 149 2248 2285 2219 117 177 195 C ATOM 3677 CG PRO B 149 90.752 -12.117 15.647 1.00 17.95 C ANISOU 3677 CG PRO B 149 2250 2294 2275 118 197 176 C ATOM 3678 CD PRO B 149 91.090 -13.432 16.301 1.00 17.95 C ANISOU 3678 CD PRO B 149 2235 2272 2312 122 167 154 C ATOM 3679 N VAL B 150 88.080 -13.462 13.115 1.00 18.54 N ANISOU 3679 N VAL B 150 2374 2421 2250 120 178 165 N ATOM 3680 CA VAL B 150 88.219 -13.528 11.659 1.00 19.36 C ANISOU 3680 CA VAL B 150 2490 2550 2317 116 202 150 C ATOM 3681 C VAL B 150 88.042 -12.112 11.133 1.00 19.74 C ANISOU 3681 C VAL B 150 2558 2612 2331 108 218 184 C ATOM 3682 O VAL B 150 87.371 -11.299 11.768 1.00 20.46 O ANISOU 3682 O VAL B 150 2654 2695 2426 112 200 214 O ATOM 3683 CB VAL B 150 87.172 -14.431 10.966 1.00 19.53 C ANISOU 3683 CB VAL B 150 2525 2585 2310 118 182 137 C ATOM 3684 CG1 VAL B 150 87.389 -15.894 11.308 1.00 20.01 C ANISOU 3684 CG1 VAL B 150 2570 2626 2405 123 163 102 C ATOM 3685 CG2 VAL B 150 85.736 -14.004 11.288 1.00 19.24 C ANISOU 3685 CG2 VAL B 150 2503 2554 2256 119 153 168 C ATOM 3686 N THR B 151 88.638 -11.825 9.984 1.00 20.32 N ANISOU 3686 N THR B 151 2641 2707 2373 94 249 177 N ATOM 3687 CA THR B 151 88.335 -10.592 9.261 1.00 20.79 C ANISOU 3687 CA THR B 151 2730 2780 2391 80 256 214 C ATOM 3688 C THR B 151 87.655 -10.924 7.935 1.00 20.62 C ANISOU 3688 C THR B 151 2735 2788 2313 69 252 211 C ATOM 3689 O THR B 151 87.944 -11.951 7.316 1.00 20.89 O ANISOU 3689 O THR B 151 2762 2841 2336 65 267 171 O ATOM 3690 CB THR B 151 89.598 -9.751 9.005 1.00 21.56 C ANISOU 3690 CB THR B 151 2825 2882 2487 59 295 219 C ATOM 3691 OG1 THR B 151 90.498 -10.472 8.166 1.00 22.76 O ANISOU 3691 OG1 THR B 151 2966 3059 2624 44 331 176 O ATOM 3692 CG2 THR B 151 90.292 -9.413 10.312 1.00 21.75 C ANISOU 3692 CG2 THR B 151 2822 2877 2567 69 296 220 C ATOM 3693 N VAL B 152 86.743 -10.053 7.511 1.00 20.26 N ANISOU 3693 N VAL B 152 2717 2745 2234 66 229 251 N ATOM 3694 CA VAL B 152 86.074 -10.182 6.223 1.00 20.42 C ANISOU 3694 CA VAL B 152 2768 2793 2196 52 219 256 C ATOM 3695 C VAL B 152 86.154 -8.846 5.492 1.00 20.73 C ANISOU 3695 C VAL B 152 2843 2836 2196 28 219 302 C ATOM 3696 O VAL B 152 85.831 -7.798 6.059 1.00 20.93 O ANISOU 3696 O VAL B 152 2875 2835 2244 37 196 339 O ATOM 3697 CB VAL B 152 84.590 -10.598 6.381 1.00 20.26 C ANISOU 3697 CB VAL B 152 2752 2769 2177 73 173 261 C ATOM 3698 CG1 VAL B 152 83.964 -10.873 5.021 1.00 20.56 C ANISOU 3698 CG1 VAL B 152 2820 2838 2155 58 162 261 C ATOM 3699 CG2 VAL B 152 84.461 -11.816 7.298 1.00 20.08 C ANISOU 3699 CG2 VAL B 152 2697 2736 2196 91 167 224 C ATOM 3700 N SER B 153 86.618 -8.888 4.246 1.00 20.82 N ANISOU 3700 N SER B 153 2879 2882 2150 -7 245 299 N ATOM 3701 CA SER B 153 86.503 -7.747 3.335 1.00 21.16 C ANISOU 3701 CA SER B 153 2967 2933 2141 -39 235 348 C ATOM 3702 C SER B 153 85.739 -8.193 2.108 1.00 21.16 C ANISOU 3702 C SER B 153 2999 2966 2077 -55 217 349 C ATOM 3703 O SER B 153 85.475 -9.382 1.922 1.00 20.78 O ANISOU 3703 O SER B 153 2934 2937 2024 -44 222 304 O ATOM 3704 CB SER B 153 87.878 -7.182 2.947 1.00 21.70 C ANISOU 3704 CB SER B 153 3041 3017 2189 -80 286 351 C ATOM 3705 OG SER B 153 88.664 -8.137 2.265 1.00 22.61 O ANISOU 3705 OG SER B 153 3141 3175 2275 -103 334 298 O ATOM 3706 N TRP B 154 85.366 -7.223 1.282 1.00 21.42 N ANISOU 3706 N TRP B 154 3079 3001 2060 -82 190 400 N ATOM 3707 CA TRP B 154 84.642 -7.479 0.053 1.00 21.82 C ANISOU 3707 CA TRP B 154 3167 3083 2041 -104 167 410 C ATOM 3708 C TRP B 154 85.420 -6.874 -1.099 1.00 23.09 C ANISOU 3708 C TRP B 154 3370 3278 2127 -168 195 435 C ATOM 3709 O TRP B 154 85.864 -5.731 -1.003 1.00 23.60 O ANISOU 3709 O TRP B 154 3455 3321 2191 -190 192 481 O ATOM 3710 CB TRP B 154 83.233 -6.891 0.139 1.00 21.40 C ANISOU 3710 CB TRP B 154 3133 2998 1998 -77 92 453 C ATOM 3711 CG TRP B 154 82.345 -7.743 0.986 1.00 20.36 C ANISOU 3711 CG TRP B 154 2962 2854 1921 -27 69 418 C ATOM 3712 CD1 TRP B 154 82.125 -7.623 2.326 1.00 19.75 C ANISOU 3712 CD1 TRP B 154 2847 2741 1917 12 59 411 C ATOM 3713 CD2 TRP B 154 81.592 -8.875 0.551 1.00 20.18 C ANISOU 3713 CD2 TRP B 154 2934 2857 1878 -18 57 384 C ATOM 3714 NE1 TRP B 154 81.270 -8.617 2.756 1.00 19.28 N ANISOU 3714 NE1 TRP B 154 2759 2684 1881 41 42 376 N ATOM 3715 CE2 TRP B 154 80.922 -9.393 1.683 1.00 19.49 C ANISOU 3715 CE2 TRP B 154 2805 2746 1854 25 39 360 C ATOM 3716 CE3 TRP B 154 81.405 -9.497 -0.690 1.00 20.46 C ANISOU 3716 CE3 TRP B 154 2995 2934 1844 -46 59 370 C ATOM 3717 CZ2 TRP B 154 80.079 -10.499 1.608 1.00 19.46 C ANISOU 3717 CZ2 TRP B 154 2786 2757 1850 40 22 326 C ATOM 3718 CZ3 TRP B 154 80.582 -10.602 -0.765 1.00 20.40 C ANISOU 3718 CZ3 TRP B 154 2972 2940 1840 -26 42 333 C ATOM 3719 CH2 TRP B 154 79.921 -11.093 0.383 1.00 19.69 C ANISOU 3719 CH2 TRP B 154 2841 2823 1817 16 23 313 C ATOM 3720 N ASN B 155 85.604 -7.669 -2.150 1.00 23.98 N ANISOU 3720 N ASN B 155 3494 3444 2174 -201 223 401 N ATOM 3721 CA ASN B 155 86.353 -7.267 -3.344 1.00 25.42 C ANISOU 3721 CA ASN B 155 3715 3673 2271 -273 258 414 C ATOM 3722 C ASN B 155 87.723 -6.677 -3.008 1.00 26.13 C ANISOU 3722 C ASN B 155 3789 3763 2375 -302 314 413 C ATOM 3723 O ASN B 155 88.121 -5.638 -3.546 1.00 26.49 O ANISOU 3723 O ASN B 155 3877 3815 2373 -355 316 464 O ATOM 3724 CB ASN B 155 85.504 -6.317 -4.190 1.00 26.14 C ANISOU 3724 CB ASN B 155 3873 3758 2301 -303 196 489 C ATOM 3725 CG ASN B 155 84.281 -6.998 -4.771 1.00 26.30 C ANISOU 3725 CG ASN B 155 3909 3793 2292 -286 149 482 C ATOM 3726 OD1 ASN B 155 84.166 -8.230 -4.751 1.00 26.35 O ANISOU 3726 OD1 ASN B 155 3880 3823 2307 -264 171 418 O ATOM 3727 ND2 ASN B 155 83.361 -6.203 -5.299 1.00 26.75 N ANISOU 3727 ND2 ASN B 155 4017 3831 2317 -296 78 547 N ATOM 3728 N SER B 156 88.431 -7.362 -2.111 1.00 26.31 N ANISOU 3728 N SER B 156 3753 3779 2465 -269 355 355 N ATOM 3729 CA SER B 156 89.779 -6.990 -1.661 1.00 26.83 C ANISOU 3729 CA SER B 156 3791 3846 2558 -288 410 339 C ATOM 3730 C SER B 156 89.862 -5.566 -1.099 1.00 26.97 C ANISOU 3730 C SER B 156 3831 3817 2600 -294 384 408 C ATOM 3731 O SER B 156 90.877 -4.879 -1.265 1.00 28.02 O ANISOU 3731 O SER B 156 3970 3962 2716 -340 423 420 O ATOM 3732 CB SER B 156 90.790 -7.201 -2.795 1.00 27.65 C ANISOU 3732 CB SER B 156 3899 4018 2587 -357 476 302 C ATOM 3733 OG SER B 156 90.678 -8.512 -3.325 1.00 28.15 O ANISOU 3733 OG SER B 156 3941 4123 2632 -350 497 231 O ATOM 3734 N GLY B 157 88.792 -5.134 -0.426 1.00 26.66 N ANISOU 3734 N GLY B 157 3801 3725 2603 -247 319 450 N ATOM 3735 CA GLY B 157 88.716 -3.804 0.171 1.00 26.69 C ANISOU 3735 CA GLY B 157 3823 3676 2641 -243 284 510 C ATOM 3736 C GLY B 157 88.063 -2.718 -0.675 1.00 27.28 C ANISOU 3736 C GLY B 157 3966 3738 2663 -278 231 586 C ATOM 3737 O GLY B 157 87.816 -1.622 -0.162 1.00 27.86 O ANISOU 3737 O GLY B 157 4053 3758 2773 -266 189 635 O ATOM 3738 N ALA B 158 87.783 -3.002 -1.952 1.00 27.76 N ANISOU 3738 N ALA B 158 4066 3843 2638 -321 227 594 N ATOM 3739 CA ALA B 158 87.169 -2.026 -2.864 1.00 28.34 C ANISOU 3739 CA ALA B 158 4211 3905 2653 -361 169 670 C ATOM 3740 C ALA B 158 85.672 -1.793 -2.607 1.00 27.96 C ANISOU 3740 C ALA B 158 4174 3808 2640 -306 79 701 C ATOM 3741 O ALA B 158 85.127 -0.778 -3.046 1.00 29.04 O ANISOU 3741 O ALA B 158 4363 3912 2758 -323 15 769 O ATOM 3742 CB ALA B 158 87.389 -2.442 -4.311 1.00 29.04 C ANISOU 3742 CB ALA B 158 4339 4062 2632 -430 195 667 C ATOM 3743 N LEU B 159 85.010 -2.733 -1.923 1.00 26.76 N ANISOU 3743 N LEU B 159 3975 3653 2540 -243 73 651 N ATOM 3744 CA LEU B 159 83.596 -2.599 -1.570 1.00 26.24 C ANISOU 3744 CA LEU B 159 3906 3547 2515 -189 -4 667 C ATOM 3745 C LEU B 159 83.470 -2.465 -0.061 1.00 25.46 C ANISOU 3745 C LEU B 159 3754 3403 2516 -128 -7 645 C ATOM 3746 O LEU B 159 83.701 -3.427 0.676 1.00 24.58 O ANISOU 3746 O LEU B 159 3593 3306 2441 -100 34 588 O ATOM 3747 CB LEU B 159 82.799 -3.799 -2.082 1.00 25.99 C ANISOU 3747 CB LEU B 159 3867 3555 2454 -174 -12 628 C ATOM 3748 CG LEU B 159 81.306 -3.866 -1.727 1.00 25.76 C ANISOU 3748 CG LEU B 159 3826 3494 2467 -118 -85 631 C ATOM 3749 CD1 LEU B 159 80.569 -2.577 -2.064 1.00 26.30 C ANISOU 3749 CD1 LEU B 159 3938 3518 2537 -119 -168 700 C ATOM 3750 CD2 LEU B 159 80.670 -5.044 -2.442 1.00 25.79 C ANISOU 3750 CD2 LEU B 159 3829 3543 2426 -119 -88 596 C ATOM 3751 N THR B 160 83.138 -1.259 0.389 1.00 25.52 N ANISOU 3751 N THR B 160 3774 3355 2567 -112 -58 689 N ATOM 3752 CA THR B 160 82.945 -0.961 1.811 1.00 25.17 C ANISOU 3752 CA THR B 160 3681 3267 2614 -59 -66 670 C ATOM 3753 C THR B 160 81.554 -0.407 2.143 1.00 25.02 C ANISOU 3753 C THR B 160 3658 3205 2643 -11 -148 685 C ATOM 3754 O THR B 160 81.035 -0.680 3.230 1.00 24.55 O ANISOU 3754 O THR B 160 3547 3131 2648 37 -152 646 O ATOM 3755 CB THR B 160 84.013 0.027 2.323 1.00 25.36 C ANISOU 3755 CB THR B 160 3709 3262 2666 -79 -41 693 C ATOM 3756 OG1 THR B 160 83.932 1.252 1.586 1.00 26.54 O ANISOU 3756 OG1 THR B 160 3915 3379 2789 -112 -91 761 O ATOM 3757 CG2 THR B 160 85.405 -0.569 2.165 1.00 25.34 C ANISOU 3757 CG2 THR B 160 3695 3303 2630 -119 43 665 C ATOM 3758 N SER B 161 80.970 0.380 1.236 1.00 25.50 N ANISOU 3758 N SER B 161 3770 3244 2675 -28 -214 739 N ATOM 3759 CA SER B 161 79.637 0.940 1.433 1.00 25.36 C ANISOU 3759 CA SER B 161 3747 3183 2707 18 -299 750 C ATOM 3760 C SER B 161 78.597 -0.177 1.534 1.00 24.39 C ANISOU 3760 C SER B 161 3588 3092 2589 55 -309 701 C ATOM 3761 O SER B 161 78.563 -1.073 0.695 1.00 24.44 O ANISOU 3761 O SER B 161 3611 3145 2531 30 -290 693 O ATOM 3762 CB SER B 161 79.277 1.887 0.282 1.00 26.67 C ANISOU 3762 CB SER B 161 3981 3321 2832 -12 -374 821 C ATOM 3763 OG SER B 161 78.027 2.511 0.510 1.00 27.66 O ANISOU 3763 OG SER B 161 4097 3397 3018 37 -463 828 O ATOM 3764 N GLY B 162 77.777 -0.117 2.581 1.00 23.30 N ANISOU 3764 N GLY B 162 3397 2929 2527 109 -334 666 N ATOM 3765 CA GLY B 162 76.683 -1.069 2.782 1.00 22.69 C ANISOU 3765 CA GLY B 162 3280 2877 2463 143 -348 620 C ATOM 3766 C GLY B 162 77.064 -2.421 3.355 1.00 21.52 C ANISOU 3766 C GLY B 162 3094 2775 2309 143 -276 565 C ATOM 3767 O GLY B 162 76.224 -3.321 3.390 1.00 21.30 O ANISOU 3767 O GLY B 162 3040 2772 2280 160 -284 530 O ATOM 3768 N VAL B 163 78.310 -2.572 3.812 1.00 20.33 N ANISOU 3768 N VAL B 163 2937 2632 2156 123 -210 558 N ATOM 3769 CA VAL B 163 78.779 -3.841 4.375 1.00 19.53 C ANISOU 3769 CA VAL B 163 2801 2565 2054 122 -148 509 C ATOM 3770 C VAL B 163 78.442 -3.875 5.852 1.00 18.80 C ANISOU 3770 C VAL B 163 2654 2456 2032 157 -144 473 C ATOM 3771 O VAL B 163 78.696 -2.909 6.569 1.00 18.93 O ANISOU 3771 O VAL B 163 2659 2439 2092 169 -149 484 O ATOM 3772 CB VAL B 163 80.303 -4.031 4.190 1.00 19.39 C ANISOU 3772 CB VAL B 163 2798 2564 2006 85 -82 512 C ATOM 3773 CG1 VAL B 163 80.795 -5.284 4.922 1.00 18.86 C ANISOU 3773 CG1 VAL B 163 2691 2521 1955 91 -29 460 C ATOM 3774 CG2 VAL B 163 80.652 -4.100 2.716 1.00 19.99 C ANISOU 3774 CG2 VAL B 163 2926 2669 2003 40 -77 539 C ATOM 3775 N HIS B 164 77.890 -5.000 6.308 1.00 18.09 N ANISOU 3775 N HIS B 164 2530 2392 1951 170 -133 431 N ATOM 3776 CA HIS B 164 77.707 -5.268 7.730 1.00 17.50 C ANISOU 3776 CA HIS B 164 2405 2314 1930 191 -118 394 C ATOM 3777 C HIS B 164 78.273 -6.643 8.032 1.00 17.01 C ANISOU 3777 C HIS B 164 2329 2280 1853 176 -70 363 C ATOM 3778 O HIS B 164 77.805 -7.639 7.490 1.00 16.96 O ANISOU 3778 O HIS B 164 2326 2299 1819 171 -74 346 O ATOM 3779 CB HIS B 164 76.232 -5.254 8.125 1.00 17.73 C ANISOU 3779 CB HIS B 164 2402 2344 1991 219 -163 370 C ATOM 3780 CG HIS B 164 75.581 -3.918 7.991 1.00 18.40 C ANISOU 3780 CG HIS B 164 2490 2395 2107 242 -219 390 C ATOM 3781 ND1 HIS B 164 75.984 -2.810 8.704 1.00 18.62 N ANISOU 3781 ND1 HIS B 164 2509 2388 2179 252 -221 398 N ATOM 3782 CD2 HIS B 164 74.545 -3.514 7.221 1.00 18.95 C ANISOU 3782 CD2 HIS B 164 2571 2456 2174 257 -280 402 C ATOM 3783 CE1 HIS B 164 75.216 -1.784 8.388 1.00 19.08 C ANISOU 3783 CE1 HIS B 164 2571 2414 2265 275 -282 413 C ATOM 3784 NE2 HIS B 164 74.339 -2.182 7.483 1.00 19.31 N ANISOU 3784 NE2 HIS B 164 2613 2458 2267 279 -321 417 N ATOM 3785 N THR B 165 79.284 -6.690 8.896 1.00 16.63 N ANISOU 3785 N THR B 165 2266 2224 1829 170 -30 354 N ATOM 3786 CA THR B 165 79.851 -7.950 9.360 1.00 16.42 C ANISOU 3786 CA THR B 165 2222 2214 1802 160 6 324 C ATOM 3787 C THR B 165 79.412 -8.109 10.791 1.00 16.11 C ANISOU 3787 C THR B 165 2144 2170 1808 171 3 301 C ATOM 3788 O THR B 165 79.703 -7.263 11.628 1.00 16.89 O ANISOU 3788 O THR B 165 2229 2249 1939 177 7 306 O ATOM 3789 CB THR B 165 81.375 -7.947 9.214 1.00 16.60 C ANISOU 3789 CB THR B 165 2256 2232 1817 141 50 330 C ATOM 3790 OG1 THR B 165 81.683 -7.828 7.822 1.00 17.36 O ANISOU 3790 OG1 THR B 165 2390 2344 1864 123 55 348 O ATOM 3791 CG2 THR B 165 81.995 -9.234 9.773 1.00 16.41 C ANISOU 3791 CG2 THR B 165 2212 2218 1806 136 79 296 C ATOM 3792 N PHE B 166 78.660 -9.170 11.053 1.00 15.84 N ANISOU 3792 N PHE B 166 2093 2155 1772 169 -6 275 N ATOM 3793 CA PHE B 166 78.008 -9.354 12.340 1.00 15.47 C ANISOU 3793 CA PHE B 166 2010 2111 1756 171 -12 252 C ATOM 3794 C PHE B 166 78.951 -9.921 13.392 1.00 15.36 C ANISOU 3794 C PHE B 166 1985 2092 1761 156 17 243 C ATOM 3795 O PHE B 166 79.915 -10.612 13.048 1.00 15.68 O ANISOU 3795 O PHE B 166 2040 2129 1791 147 37 244 O ATOM 3796 CB PHE B 166 76.781 -10.259 12.190 1.00 15.55 C ANISOU 3796 CB PHE B 166 2008 2146 1755 169 -35 230 C ATOM 3797 CG PHE B 166 75.658 -9.602 11.447 1.00 15.75 C ANISOU 3797 CG PHE B 166 2034 2176 1774 187 -72 234 C ATOM 3798 CD1 PHE B 166 74.738 -8.819 12.131 1.00 15.90 C ANISOU 3798 CD1 PHE B 166 2021 2195 1826 202 -95 219 C ATOM 3799 CD2 PHE B 166 75.544 -9.701 10.063 1.00 16.36 C ANISOU 3799 CD2 PHE B 166 2143 2257 1814 189 -88 250 C ATOM 3800 CE1 PHE B 166 73.727 -8.185 11.463 1.00 16.28 C ANISOU 3800 CE1 PHE B 166 2066 2243 1878 223 -137 220 C ATOM 3801 CE2 PHE B 166 74.522 -9.055 9.396 1.00 16.75 C ANISOU 3801 CE2 PHE B 166 2196 2308 1861 206 -132 257 C ATOM 3802 CZ PHE B 166 73.616 -8.296 10.100 1.00 16.68 C ANISOU 3802 CZ PHE B 166 2151 2293 1892 225 -158 242 C ATOM 3803 N PRO B 167 78.674 -9.629 14.678 1.00 15.46 N ANISOU 3803 N PRO B 167 1969 2104 1801 153 16 230 N ATOM 3804 CA PRO B 167 79.438 -10.306 15.726 1.00 15.55 C ANISOU 3804 CA PRO B 167 1971 2112 1825 133 34 223 C ATOM 3805 C PRO B 167 79.278 -11.820 15.610 1.00 15.92 C ANISOU 3805 C PRO B 167 2023 2169 1857 116 30 211 C ATOM 3806 O PRO B 167 78.191 -12.295 15.294 1.00 16.22 O ANISOU 3806 O PRO B 167 2056 2225 1880 113 11 200 O ATOM 3807 CB PRO B 167 78.780 -9.819 17.017 1.00 15.63 C ANISOU 3807 CB PRO B 167 1950 2132 1855 127 29 207 C ATOM 3808 CG PRO B 167 78.096 -8.555 16.672 1.00 15.95 C ANISOU 3808 CG PRO B 167 1982 2170 1908 151 14 206 C ATOM 3809 CD PRO B 167 77.700 -8.673 15.233 1.00 15.81 C ANISOU 3809 CD PRO B 167 1988 2154 1867 165 -3 219 C ATOM 3810 N ALA B 168 80.348 -12.559 15.870 1.00 16.32 N ANISOU 3810 N ALA B 168 2081 2204 1915 105 42 212 N ATOM 3811 CA ALA B 168 80.290 -14.012 15.825 1.00 16.80 C ANISOU 3811 CA ALA B 168 2147 2264 1970 90 31 201 C ATOM 3812 C ALA B 168 79.471 -14.537 16.987 1.00 17.06 C ANISOU 3812 C ALA B 168 2166 2311 2008 63 15 193 C ATOM 3813 O ALA B 168 79.403 -13.902 18.049 1.00 17.74 O ANISOU 3813 O ALA B 168 2235 2401 2104 52 19 195 O ATOM 3814 CB ALA B 168 81.688 -14.595 15.868 1.00 16.92 C ANISOU 3814 CB ALA B 168 2170 2255 2004 88 43 200 C ATOM 3815 N AVAL B 169 78.855 -15.697 16.776 0.50 17.31 N ANISOU 3815 N AVAL B 169 2202 2348 2027 47 -3 184 N ATOM 3816 N BVAL B 169 78.841 -15.690 16.777 0.50 17.20 N ANISOU 3816 N BVAL B 169 2188 2335 2013 47 -3 184 N ATOM 3817 CA AVAL B 169 78.145 -16.417 17.823 0.50 17.39 C ANISOU 3817 CA AVAL B 169 2202 2370 2035 10 -20 179 C ATOM 3818 CA BVAL B 169 78.139 -16.408 17.833 0.50 17.20 C ANISOU 3818 CA BVAL B 169 2178 2346 2011 10 -20 179 C ATOM 3819 C AVAL B 169 78.872 -17.726 18.081 0.50 17.29 C ANISOU 3819 C AVAL B 169 2207 2328 2034 -10 -36 183 C ATOM 3820 C BVAL B 169 78.857 -17.727 18.082 0.50 17.18 C ANISOU 3820 C BVAL B 169 2193 2315 2020 -10 -36 183 C ATOM 3821 O AVAL B 169 79.314 -18.384 17.141 0.50 16.99 O ANISOU 3821 O AVAL B 169 2183 2273 2000 6 -40 176 O ATOM 3822 O BVAL B 169 79.282 -18.391 17.137 0.50 16.91 O ANISOU 3822 O BVAL B 169 2173 2264 1990 6 -40 176 O ATOM 3823 CB AVAL B 169 76.692 -16.725 17.422 0.50 17.80 C ANISOU 3823 CB AVAL B 169 2245 2452 2066 1 -34 164 C ATOM 3824 CB BVAL B 169 76.668 -16.684 17.465 0.50 17.46 C ANISOU 3824 CB BVAL B 169 2201 2409 2023 0 -33 164 C ATOM 3825 CG1AVAL B 169 76.629 -17.871 16.424 0.50 18.08 C ANISOU 3825 CG1AVAL B 169 2300 2477 2092 2 -48 158 C ATOM 3826 CG1BVAL B 169 75.859 -15.393 17.509 0.50 17.42 C ANISOU 3826 CG1BVAL B 169 2171 2430 2017 17 -26 155 C ATOM 3827 CG2AVAL B 169 75.871 -17.054 18.656 0.50 17.97 C ANISOU 3827 CG2AVAL B 169 2249 2497 2081 -43 -42 157 C ATOM 3828 CG2BVAL B 169 76.556 -17.333 16.095 0.50 17.65 C ANISOU 3828 CG2BVAL B 169 2243 2428 2035 18 -42 158 C ATOM 3829 N LEU B 170 79.008 -18.080 19.357 1.00 17.17 N ANISOU 3829 N LEU B 170 2191 2309 2026 -45 -48 193 N ATOM 3830 CA LEU B 170 79.559 -19.375 19.759 1.00 17.30 C ANISOU 3830 CA LEU B 170 2224 2291 2056 -69 -76 200 C ATOM 3831 C LEU B 170 78.430 -20.389 19.665 1.00 17.28 C ANISOU 3831 C LEU B 170 2228 2302 2036 -101 -99 195 C ATOM 3832 O LEU B 170 77.388 -20.243 20.321 1.00 18.41 O ANISOU 3832 O LEU B 170 2360 2481 2157 -135 -99 193 O ATOM 3833 CB LEU B 170 80.099 -19.311 21.184 1.00 17.54 C ANISOU 3833 CB LEU B 170 2256 2313 2096 -101 -86 219 C ATOM 3834 CG LEU B 170 80.745 -20.601 21.689 1.00 17.95 C ANISOU 3834 CG LEU B 170 2330 2323 2169 -127 -126 233 C ATOM 3835 CD1 LEU B 170 81.911 -21.060 20.827 1.00 18.13 C ANISOU 3835 CD1 LEU B 170 2359 2301 2229 -87 -133 222 C ATOM 3836 CD2 LEU B 170 81.205 -20.401 23.122 1.00 18.24 C ANISOU 3836 CD2 LEU B 170 2369 2354 2206 -163 -138 254 C ATOM 3837 N GLN B 171 78.617 -21.400 18.821 1.00 16.59 N ANISOU 3837 N GLN B 171 2156 2189 1959 -91 -117 186 N ATOM 3838 CA GLN B 171 77.600 -22.427 18.606 1.00 16.55 C ANISOU 3838 CA GLN B 171 2158 2191 1939 -119 -141 179 C ATOM 3839 C GLN B 171 77.759 -23.546 19.634 1.00 16.37 C ANISOU 3839 C GLN B 171 2154 2139 1928 -169 -180 198 C ATOM 3840 O GLN B 171 78.806 -23.675 20.277 1.00 16.14 O ANISOU 3840 O GLN B 171 2134 2074 1923 -171 -194 213 O ATOM 3841 CB GLN B 171 77.722 -23.002 17.191 1.00 16.86 C ANISOU 3841 CB GLN B 171 2205 2215 1984 -86 -145 157 C ATOM 3842 CG GLN B 171 77.633 -21.965 16.072 1.00 17.18 C ANISOU 3842 CG GLN B 171 2237 2283 2009 -43 -112 144 C ATOM 3843 CD GLN B 171 78.099 -22.486 14.731 1.00 17.66 C ANISOU 3843 CD GLN B 171 2308 2328 2073 -14 -110 121 C ATOM 3844 OE1 GLN B 171 77.309 -22.603 13.783 1.00 18.64 O ANISOU 3844 OE1 GLN B 171 2433 2474 2173 -7 -111 107 O ATOM 3845 NE2 GLN B 171 79.394 -22.780 14.620 1.00 17.50 N ANISOU 3845 NE2 GLN B 171 2292 2274 2082 3 -108 114 N ATOM 3846 N ASER B 172 76.733 -24.378 19.769 0.50 16.54 N ANISOU 3846 N ASER B 172 2182 2172 1932 -210 -202 198 N ATOM 3847 N BSER B 172 76.721 -24.372 19.763 0.50 16.42 N ANISOU 3847 N BSER B 172 2166 2157 1916 -210 -202 198 N ATOM 3848 CA ASER B 172 76.796 -25.527 20.676 0.50 16.69 C ANISOU 3848 CA ASER B 172 2225 2159 1958 -266 -247 221 C ATOM 3849 CA BSER B 172 76.759 -25.547 20.646 0.50 16.50 C ANISOU 3849 CA BSER B 172 2201 2136 1934 -266 -247 220 C ATOM 3850 C ASER B 172 77.864 -26.570 20.291 0.50 16.53 C ANISOU 3850 C ASER B 172 2227 2069 1984 -246 -286 221 C ATOM 3851 C BSER B 172 77.890 -26.532 20.304 0.50 16.40 C ANISOU 3851 C BSER B 172 2210 2053 1967 -245 -285 221 C ATOM 3852 O ASER B 172 78.233 -27.415 21.109 0.50 16.65 O ANISOU 3852 O ASER B 172 2265 2043 2016 -284 -331 245 O ATOM 3853 O BSER B 172 78.335 -27.291 21.167 0.50 16.51 O ANISOU 3853 O BSER B 172 2247 2027 2000 -281 -328 246 O ATOM 3854 CB ASER B 172 75.415 -26.169 20.784 0.50 17.17 C ANISOU 3854 CB ASER B 172 2287 2249 1988 -318 -260 218 C ATOM 3855 CB BSER B 172 75.409 -26.277 20.628 0.50 16.84 C ANISOU 3855 CB BSER B 172 2247 2204 1949 -314 -262 216 C ATOM 3856 OG ASER B 172 74.517 -25.249 21.387 0.50 17.50 O ANISOU 3856 OG ASER B 172 2302 2354 1994 -343 -227 214 O ATOM 3857 OG BSER B 172 75.150 -26.856 19.366 0.50 17.06 O ANISOU 3857 OG BSER B 172 2277 2219 1987 -284 -269 192 O ATOM 3858 N SER B 173 78.363 -26.497 19.058 1.00 15.98 N ANISOU 3858 N SER B 173 2151 1988 1935 -188 -270 192 N ATOM 3859 CA SER B 173 79.528 -27.278 18.628 1.00 15.77 C ANISOU 3859 CA SER B 173 2134 1900 1958 -158 -298 178 C ATOM 3860 C SER B 173 80.859 -26.800 19.208 1.00 15.21 C ANISOU 3860 C SER B 173 2058 1802 1919 -138 -296 188 C ATOM 3861 O SER B 173 81.882 -27.443 18.971 1.00 15.40 O ANISOU 3861 O SER B 173 2085 1774 1992 -114 -322 172 O ATOM 3862 CB SER B 173 79.639 -27.213 17.111 1.00 15.72 C ANISOU 3862 CB SER B 173 2116 1902 1954 -108 -271 137 C ATOM 3863 OG SER B 173 79.767 -25.861 16.707 1.00 15.44 O ANISOU 3863 OG SER B 173 2063 1909 1896 -76 -219 133 O ATOM 3864 N GLY B 174 80.875 -25.661 19.900 1.00 14.57 N ANISOU 3864 N GLY B 174 1966 1755 1814 -144 -266 207 N ATOM 3865 CA GLY B 174 82.113 -25.111 20.432 1.00 14.33 C ANISOU 3865 CA GLY B 174 1928 1703 1812 -125 -262 215 C ATOM 3866 C GLY B 174 82.867 -24.283 19.407 1.00 14.03 C ANISOU 3866 C GLY B 174 1870 1675 1785 -68 -217 186 C ATOM 3867 O GLY B 174 83.992 -23.857 19.672 1.00 14.25 O ANISOU 3867 O GLY B 174 1888 1684 1842 -47 -210 186 O ATOM 3868 N LEU B 175 82.244 -24.035 18.248 1.00 13.78 N ANISOU 3868 N LEU B 175 1832 1675 1729 -46 -186 164 N ATOM 3869 CA LEU B 175 82.865 -23.303 17.155 1.00 13.83 C ANISOU 3869 CA LEU B 175 1825 1696 1736 0 -145 139 C ATOM 3870 C LEU B 175 82.072 -22.037 16.889 1.00 13.71 C ANISOU 3870 C LEU B 175 1802 1732 1676 4 -106 149 C ATOM 3871 O LEU B 175 80.873 -21.984 17.169 1.00 13.57 O ANISOU 3871 O LEU B 175 1786 1741 1629 -20 -111 159 O ATOM 3872 CB LEU B 175 82.884 -24.155 15.889 1.00 13.96 C ANISOU 3872 CB LEU B 175 1843 1701 1760 20 -148 102 C ATOM 3873 CG LEU B 175 83.572 -25.522 15.998 1.00 14.41 C ANISOU 3873 CG LEU B 175 1904 1701 1868 21 -194 82 C ATOM 3874 CD1 LEU B 175 83.335 -26.330 14.729 1.00 14.68 C ANISOU 3874 CD1 LEU B 175 1941 1734 1904 37 -195 40 C ATOM 3875 CD2 LEU B 175 85.063 -25.359 16.262 1.00 14.54 C ANISOU 3875 CD2 LEU B 175 1906 1686 1934 45 -192 71 C ATOM 3876 N TYR B 176 82.755 -21.021 16.372 1.00 13.85 N ANISOU 3876 N TYR B 176 1810 1761 1692 34 -69 144 N ATOM 3877 CA TYR B 176 82.123 -19.745 16.020 1.00 14.21 C ANISOU 3877 CA TYR B 176 1850 1847 1703 43 -38 153 C ATOM 3878 C TYR B 176 81.556 -19.731 14.607 1.00 14.41 C ANISOU 3878 C TYR B 176 1881 1895 1699 59 -26 136 C ATOM 3879 O TYR B 176 82.002 -20.484 13.736 1.00 14.36 O ANISOU 3879 O TYR B 176 1880 1877 1698 70 -26 111 O ATOM 3880 CB TYR B 176 83.128 -18.602 16.162 1.00 14.69 C ANISOU 3880 CB TYR B 176 1901 1905 1774 61 -9 161 C ATOM 3881 CG TYR B 176 83.495 -18.345 17.589 1.00 15.16 C ANISOU 3881 CG TYR B 176 1954 1952 1854 43 -19 180 C ATOM 3882 CD1 TYR B 176 82.707 -17.524 18.385 1.00 15.60 C ANISOU 3882 CD1 TYR B 176 2003 2031 1891 27 -15 196 C ATOM 3883 CD2 TYR B 176 84.607 -18.947 18.163 1.00 15.90 C ANISOU 3883 CD2 TYR B 176 2047 2009 1986 40 -36 178 C ATOM 3884 CE1 TYR B 176 83.011 -17.299 19.716 1.00 16.23 C ANISOU 3884 CE1 TYR B 176 2078 2105 1983 5 -23 211 C ATOM 3885 CE2 TYR B 176 84.930 -18.717 19.499 1.00 16.25 C ANISOU 3885 CE2 TYR B 176 2087 2042 2043 20 -50 198 C ATOM 3886 CZ TYR B 176 84.121 -17.893 20.263 1.00 16.58 C ANISOU 3886 CZ TYR B 176 2125 2113 2059 0 -41 215 C ATOM 3887 OH TYR B 176 84.409 -17.669 21.590 1.00 18.29 O ANISOU 3887 OH TYR B 176 2340 2325 2283 -26 -53 231 O ATOM 3888 N ASER B 177 80.578 -18.850 14.397 0.50 14.28 N ANISOU 3888 N ASER B 177 1862 1910 1652 61 -18 147 N ATOM 3889 N BSER B 177 80.562 -18.869 14.402 0.50 14.37 N ANISOU 3889 N BSER B 177 1874 1922 1664 60 -18 147 N ATOM 3890 CA ASER B 177 79.991 -18.600 13.084 0.50 14.58 C ANISOU 3890 CA ASER B 177 1909 1973 1658 75 -10 139 C ATOM 3891 CA BSER B 177 80.037 -18.566 13.077 0.50 14.74 C ANISOU 3891 CA BSER B 177 1929 1993 1678 76 -9 139 C ATOM 3892 C ASER B 177 79.529 -17.149 13.003 0.50 14.67 C ANISOU 3892 C ASER B 177 1916 2007 1653 87 2 158 C ATOM 3893 C BSER B 177 79.614 -17.114 13.028 0.50 14.74 C ANISOU 3893 C BSER B 177 1924 2013 1662 87 4 158 C ATOM 3894 O ASER B 177 78.979 -16.612 13.972 0.50 14.61 O ANISOU 3894 O ASER B 177 1893 2004 1652 78 -4 168 O ATOM 3895 O BSER B 177 79.197 -16.540 14.038 0.50 14.64 O ANISOU 3895 O BSER B 177 1899 2006 1660 79 -1 170 O ATOM 3896 CB ASER B 177 78.808 -19.538 12.828 0.50 14.81 C ANISOU 3896 CB ASER B 177 1941 2014 1672 61 -37 127 C ATOM 3897 CB BSER B 177 78.852 -19.461 12.725 0.50 15.06 C ANISOU 3897 CB BSER B 177 1974 2047 1702 63 -34 126 C ATOM 3898 OG ASER B 177 78.281 -19.354 11.531 0.50 15.10 O ANISOU 3898 OG ASER B 177 1987 2073 1676 74 -34 117 O ATOM 3899 OG BSER B 177 79.274 -20.803 12.632 0.50 15.60 O ANISOU 3899 OG BSER B 177 2049 2091 1789 55 -50 107 O ATOM 3900 N LEU B 178 79.743 -16.523 11.849 1.00 14.95 N ANISOU 3900 N LEU B 178 1964 2052 1664 103 17 160 N ATOM 3901 CA LEU B 178 79.206 -15.191 11.603 1.00 15.15 C ANISOU 3901 CA LEU B 178 1990 2091 1675 115 17 180 C ATOM 3902 C LEU B 178 78.854 -15.060 10.153 1.00 15.21 C ANISOU 3902 C LEU B 178 2018 2116 1644 121 13 180 C ATOM 3903 O LEU B 178 79.296 -15.854 9.315 1.00 15.46 O ANISOU 3903 O LEU B 178 2063 2152 1659 117 22 163 O ATOM 3904 CB LEU B 178 80.174 -14.082 12.026 1.00 15.80 C ANISOU 3904 CB LEU B 178 2070 2159 1773 122 39 198 C ATOM 3905 CG LEU B 178 81.505 -13.829 11.302 1.00 16.25 C ANISOU 3905 CG LEU B 178 2140 2208 1824 124 68 200 C ATOM 3906 CD1 LEU B 178 81.356 -13.209 9.911 1.00 16.66 C ANISOU 3906 CD1 LEU B 178 2217 2278 1836 127 72 212 C ATOM 3907 CD2 LEU B 178 82.376 -12.920 12.159 1.00 16.33 C ANISOU 3907 CD2 LEU B 178 2140 2201 1862 126 85 215 C ATOM 3908 N ASER B 179 78.075 -14.026 9.867 0.50 15.10 N ANISOU 3908 N ASER B 179 2007 2112 1618 131 -3 198 N ATOM 3909 N BSER B 179 78.029 -14.062 9.856 0.50 14.95 N ANISOU 3909 N BSER B 179 1988 2094 1599 131 -4 197 N ATOM 3910 CA ASER B 179 77.748 -13.647 8.509 0.50 15.31 C ANISOU 3910 CA ASER B 179 2059 2154 1606 136 -13 208 C ATOM 3911 CA BSER B 179 77.731 -13.688 8.480 0.50 15.06 C ANISOU 3911 CA BSER B 179 2027 2123 1573 136 -13 207 C ATOM 3912 C ASER B 179 78.289 -12.258 8.245 0.50 15.14 C ANISOU 3912 C ASER B 179 2052 2122 1580 142 -6 239 C ATOM 3913 C BSER B 179 78.234 -12.271 8.229 0.50 15.00 C ANISOU 3913 C BSER B 179 2033 2104 1561 142 -7 239 C ATOM 3914 O ASER B 179 78.384 -11.425 9.154 0.50 15.06 O ANISOU 3914 O ASER B 179 2026 2095 1601 150 -5 251 O ATOM 3915 O BSER B 179 78.267 -11.440 9.140 0.50 14.91 O ANISOU 3915 O BSER B 179 2006 2077 1581 151 -8 250 O ATOM 3916 CB ASER B 179 76.246 -13.619 8.321 0.50 15.56 C ANISOU 3916 CB ASER B 179 2082 2201 1630 142 -52 205 C ATOM 3917 CB BSER B 179 76.229 -13.792 8.185 0.50 15.17 C ANISOU 3917 CB BSER B 179 2035 2153 1575 141 -52 202 C ATOM 3918 OG ASER B 179 75.689 -12.669 9.203 0.50 15.63 O ANISOU 3918 OG ASER B 179 2068 2202 1669 154 -66 213 O ATOM 3919 OG BSER B 179 75.817 -15.145 7.996 0.50 15.01 O ANISOU 3919 OG BSER B 179 2012 2145 1547 129 -58 175 O ATOM 3920 N SER B 180 78.653 -12.023 6.990 1.00 15.23 N ANISOU 3920 N SER B 180 2094 2144 1549 134 0 251 N ATOM 3921 CA SER B 180 78.976 -10.691 6.506 1.00 15.36 C ANISOU 3921 CA SER B 180 2133 2151 1551 132 -3 288 C ATOM 3922 C SER B 180 78.099 -10.477 5.289 1.00 15.69 C ANISOU 3922 C SER B 180 2204 2209 1549 129 -38 304 C ATOM 3923 O SER B 180 78.048 -11.335 4.402 1.00 15.71 O ANISOU 3923 O SER B 180 2221 2237 1512 116 -34 287 O ATOM 3924 CB SER B 180 80.444 -10.595 6.115 1.00 15.47 C ANISOU 3924 CB SER B 180 2162 2167 1549 113 42 291 C ATOM 3925 OG SER B 180 80.744 -9.289 5.638 1.00 15.98 O ANISOU 3925 OG SER B 180 2254 2223 1597 104 37 331 O ATOM 3926 N VAL B 181 77.399 -9.345 5.263 1.00 15.76 N ANISOU 3926 N VAL B 181 2218 2202 1567 143 -78 333 N ATOM 3927 CA VAL B 181 76.467 -9.035 4.183 1.00 16.26 C ANISOU 3927 CA VAL B 181 2309 2275 1596 143 -126 353 C ATOM 3928 C VAL B 181 76.782 -7.685 3.585 1.00 16.89 C ANISOU 3928 C VAL B 181 2425 2334 1658 134 -146 402 C ATOM 3929 O VAL B 181 77.501 -6.878 4.175 1.00 16.72 O ANISOU 3929 O VAL B 181 2401 2288 1665 135 -129 418 O ATOM 3930 CB VAL B 181 74.985 -9.072 4.648 1.00 16.25 C ANISOU 3930 CB VAL B 181 2277 2271 1628 170 -174 337 C ATOM 3931 CG1 VAL B 181 74.653 -10.420 5.261 1.00 15.95 C ANISOU 3931 CG1 VAL B 181 2206 2252 1603 170 -155 292 C ATOM 3932 CG2 VAL B 181 74.666 -7.943 5.620 1.00 16.25 C ANISOU 3932 CG2 VAL B 181 2251 2239 1684 195 -195 345 C ATOM 3933 N VAL B 182 76.258 -7.464 2.389 1.00 17.63 N ANISOU 3933 N VAL B 182 2557 2438 1705 122 -185 427 N ATOM 3934 CA VAL B 182 76.345 -6.179 1.728 1.00 18.42 C ANISOU 3934 CA VAL B 182 2698 2514 1785 111 -221 481 C ATOM 3935 C VAL B 182 75.079 -5.991 0.902 1.00 18.95 C ANISOU 3935 C VAL B 182 2784 2582 1833 120 -294 498 C ATOM 3936 O VAL B 182 74.558 -6.957 0.328 1.00 18.82 O ANISOU 3936 O VAL B 182 2769 2599 1783 114 -298 475 O ATOM 3937 CB VAL B 182 77.624 -6.071 0.849 1.00 18.97 C ANISOU 3937 CB VAL B 182 2812 2603 1792 62 -178 505 C ATOM 3938 CG1 VAL B 182 77.646 -7.129 -0.246 1.00 19.25 C ANISOU 3938 CG1 VAL B 182 2869 2688 1757 33 -160 485 C ATOM 3939 CG2 VAL B 182 77.768 -4.671 0.257 1.00 19.61 C ANISOU 3939 CG2 VAL B 182 2941 2655 1854 42 -217 568 C ATOM 3940 N THR B 183 74.578 -4.760 0.883 1.00 19.50 N ANISOU 3940 N THR B 183 2866 2611 1931 135 -355 536 N ATOM 3941 CA THR B 183 73.476 -4.379 -0.004 1.00 20.31 C ANISOU 3941 CA THR B 183 2994 2706 2016 142 -435 561 C ATOM 3942 C THR B 183 74.017 -3.566 -1.169 1.00 21.07 C ANISOU 3942 C THR B 183 3162 2793 2050 100 -461 627 C ATOM 3943 O THR B 183 74.914 -2.728 -1.002 1.00 21.08 O ANISOU 3943 O THR B 183 3184 2768 2055 82 -443 659 O ATOM 3944 CB THR B 183 72.377 -3.586 0.725 1.00 20.66 C ANISOU 3944 CB THR B 183 3000 2707 2142 193 -501 554 C ATOM 3945 OG1 THR B 183 72.947 -2.448 1.384 1.00 20.92 O ANISOU 3945 OG1 THR B 183 3032 2695 2221 202 -502 576 O ATOM 3946 CG2 THR B 183 71.655 -4.467 1.715 1.00 20.43 C ANISOU 3946 CG2 THR B 183 2903 2699 2161 225 -481 489 C ATOM 3947 N VAL B 184 73.473 -3.844 -2.349 1.00 21.66 N ANISOU 3947 N VAL B 184 3276 2892 2063 78 -501 645 N ATOM 3948 CA VAL B 184 73.911 -3.226 -3.596 1.00 22.78 C ANISOU 3948 CA VAL B 184 3493 3036 2128 26 -527 708 C ATOM 3949 C VAL B 184 72.680 -2.989 -4.469 1.00 23.72 C ANISOU 3949 C VAL B 184 3640 3146 2228 33 -624 735 C ATOM 3950 O VAL B 184 71.630 -3.583 -4.232 1.00 23.30 O ANISOU 3950 O VAL B 184 3545 3100 2208 72 -653 695 O ATOM 3951 CB VAL B 184 74.941 -4.116 -4.337 1.00 22.74 C ANISOU 3951 CB VAL B 184 3514 3092 2033 -31 -449 694 C ATOM 3952 CG1 VAL B 184 76.169 -4.353 -3.467 1.00 22.23 C ANISOU 3952 CG1 VAL B 184 3418 3034 1995 -35 -359 664 C ATOM 3953 CG2 VAL B 184 74.325 -5.447 -4.787 1.00 22.61 C ANISOU 3953 CG2 VAL B 184 3482 3125 1983 -28 -440 646 C ATOM 3954 N PRO B 185 72.792 -2.118 -5.488 1.00 25.17 N ANISOU 3954 N PRO B 185 3895 3313 2357 -8 -680 806 N ATOM 3955 CA PRO B 185 71.667 -1.996 -6.408 1.00 26.22 C ANISOU 3955 CA PRO B 185 4058 3441 2464 -6 -776 833 C ATOM 3956 C PRO B 185 71.408 -3.324 -7.114 1.00 26.63 C ANISOU 3956 C PRO B 185 4110 3562 2446 -27 -746 794 C ATOM 3957 O PRO B 185 72.363 -3.981 -7.536 1.00 26.38 O ANISOU 3957 O PRO B 185 4098 3582 2344 -76 -667 780 O ATOM 3958 CB PRO B 185 72.145 -0.936 -7.408 1.00 27.01 C ANISOU 3958 CB PRO B 185 4245 3519 2499 -65 -824 920 C ATOM 3959 CG PRO B 185 73.196 -0.169 -6.687 1.00 26.68 C ANISOU 3959 CG PRO B 185 4201 3444 2492 -73 -778 938 C ATOM 3960 CD PRO B 185 73.874 -1.169 -5.804 1.00 25.69 C ANISOU 3960 CD PRO B 185 4014 3359 2387 -58 -666 865 C ATOM 3961 N ASER B 186 70.143 -3.721 -7.238 0.50 27.11 N ANISOU 3961 N ASER B 186 4145 3624 2530 10 -807 770 N ATOM 3962 N BSER B 186 70.139 -3.715 -7.230 0.50 27.17 N ANISOU 3962 N BSER B 186 4153 3632 2540 10 -807 770 N ATOM 3963 CA ASER B 186 69.798 -4.975 -7.917 0.50 27.57 C ANISOU 3963 CA ASER B 186 4203 3744 2527 -9 -787 731 C ATOM 3964 CA BSER B 186 69.762 -4.948 -7.929 0.50 27.69 C ANISOU 3964 CA BSER B 186 4219 3758 2544 -8 -790 732 C ATOM 3965 C ASER B 186 70.300 -5.018 -9.369 0.50 28.83 C ANISOU 3965 C ASER B 186 4444 3945 2564 -84 -789 775 C ATOM 3966 C BSER B 186 70.321 -5.007 -9.354 0.50 28.88 C ANISOU 3966 C BSER B 186 4450 3951 2571 -84 -788 775 C ATOM 3967 O ASER B 186 70.663 -6.086 -9.864 0.50 28.96 O ANISOU 3967 O ASER B 186 4464 4023 2516 -116 -728 736 O ATOM 3968 O BSER B 186 70.745 -6.069 -9.812 0.50 28.95 O ANISOU 3968 O BSER B 186 4462 4022 2517 -117 -723 736 O ATOM 3969 CB ASER B 186 68.289 -5.228 -7.859 0.50 27.68 C ANISOU 3969 CB ASER B 186 4179 3748 2589 41 -865 705 C ATOM 3970 CB BSER B 186 68.241 -5.095 -7.960 0.50 27.96 C ANISOU 3970 CB BSER B 186 4222 3780 2623 39 -877 714 C ATOM 3971 OG ASER B 186 67.564 -4.188 -8.488 0.50 28.38 O ANISOU 3971 OG ASER B 186 4307 3794 2681 45 -977 764 O ATOM 3972 OG BSER B 186 67.721 -5.221 -6.650 0.50 27.34 O ANISOU 3972 OG BSER B 186 4062 3677 2648 101 -865 661 O ATOM 3973 N SER B 187 70.333 -3.861 -10.033 1.00 30.09 N ANISOU 3973 N SER B 187 4669 4073 2693 -114 -859 853 N ATOM 3974 CA SER B 187 70.910 -3.748 -11.384 1.00 31.64 C ANISOU 3974 CA SER B 187 4949 4309 2764 -199 -860 903 C ATOM 3975 C SER B 187 72.414 -4.089 -11.492 1.00 32.11 C ANISOU 3975 C SER B 187 5024 4417 2759 -258 -744 889 C ATOM 3976 O SER B 187 72.879 -4.432 -12.577 1.00 33.14 O ANISOU 3976 O SER B 187 5206 4607 2780 -329 -718 898 O ATOM 3977 CB SER B 187 70.654 -2.348 -11.960 1.00 32.67 C ANISOU 3977 CB SER B 187 5148 4383 2881 -222 -966 998 C ATOM 3978 OG SER B 187 71.226 -1.343 -11.146 1.00 32.82 O ANISOU 3978 OG SER B 187 5160 4343 2966 -206 -960 1027 O ATOM 3979 N ASER B 188 73.146 -4.002 -10.383 0.50 31.70 N ANISOU 3979 N ASER B 188 4924 4344 2775 -230 -676 861 N ATOM 3980 N BSER B 188 73.148 -3.987 -10.381 0.50 31.74 N ANISOU 3980 N BSER B 188 4930 4349 2781 -230 -677 862 N ATOM 3981 CA ASER B 188 74.573 -4.330 -10.361 0.50 31.73 C ANISOU 3981 CA ASER B 188 4930 4390 2735 -278 -567 839 C ATOM 3982 CA BSER B 188 74.575 -4.329 -10.339 0.50 31.77 C ANISOU 3982 CA BSER B 188 4934 4395 2743 -277 -566 838 C ATOM 3983 C ASER B 188 74.869 -5.834 -10.317 0.50 31.56 C ANISOU 3983 C ASER B 188 4865 4432 2696 -275 -481 752 C ATOM 3984 C BSER B 188 74.861 -5.835 -10.343 0.50 31.61 C ANISOU 3984 C BSER B 188 4872 4439 2700 -276 -482 753 C ATOM 3985 O ASER B 188 76.019 -6.234 -10.517 0.50 31.72 O ANISOU 3985 O ASER B 188 4887 4496 2669 -319 -394 725 O ATOM 3986 O BSER B 188 75.996 -6.236 -10.611 0.50 31.82 O ANISOU 3986 O BSER B 188 4904 4512 2675 -323 -397 727 O ATOM 3987 CB ASER B 188 75.239 -3.664 -9.160 0.50 31.19 C ANISOU 3987 CB ASER B 188 4826 4272 2752 -247 -533 842 C ATOM 3988 CB BSER B 188 75.247 -3.713 -9.105 0.50 31.24 C ANISOU 3988 CB BSER B 188 4828 4279 2762 -244 -529 838 C ATOM 3989 OG ASER B 188 74.962 -4.387 -7.978 0.50 30.27 O ANISOU 3989 OG ASER B 188 4630 4146 2725 -179 -499 774 O ATOM 3990 OG BSER B 188 75.132 -2.301 -9.086 0.50 31.82 O ANISOU 3990 OG BSER B 188 4942 4290 2859 -248 -601 913 O ATOM 3991 N LEU B 189 73.858 -6.661 -10.038 1.00 31.34 N ANISOU 3991 N LEU B 189 4794 4406 2710 -224 -506 706 N ATOM 3992 CA LEU B 189 74.043 -8.125 -9.972 1.00 31.16 C ANISOU 3992 CA LEU B 189 4729 4434 2678 -219 -436 624 C ATOM 3993 C LEU B 189 74.471 -8.733 -11.309 1.00 32.21 C ANISOU 3993 C LEU B 189 4907 4638 2693 -288 -405 610 C ATOM 3994 O LEU B 189 75.274 -9.661 -11.337 1.00 31.89 O ANISOU 3994 O LEU B 189 4843 4641 2633 -306 -321 548 O ATOM 3995 CB LEU B 189 72.778 -8.829 -9.460 1.00 30.49 C ANISOU 3995 CB LEU B 189 4594 4335 2657 -157 -479 583 C ATOM 3996 CG LEU B 189 72.312 -8.523 -8.031 1.00 29.75 C ANISOU 3996 CG LEU B 189 4440 4185 2680 -89 -494 573 C ATOM 3997 CD1 LEU B 189 71.117 -9.398 -7.677 1.00 29.37 C ANISOU 3997 CD1 LEU B 189 4343 4140 2677 -44 -524 525 C ATOM 3998 CD2 LEU B 189 73.434 -8.730 -7.027 1.00 29.20 C ANISOU 3998 CD2 LEU B 189 4333 4109 2654 -80 -407 542 C ATOM 3999 N GLY B 190 73.946 -8.196 -12.409 1.00 33.75 N ANISOU 3999 N GLY B 190 5167 4844 2812 -329 -474 666 N ATOM 4000 CA GLY B 190 74.345 -8.631 -13.745 1.00 35.14 C ANISOU 4000 CA GLY B 190 5394 5093 2864 -406 -449 659 C ATOM 4001 C GLY B 190 75.748 -8.216 -14.169 1.00 36.15 C ANISOU 4001 C GLY B 190 5557 5256 2922 -480 -376 674 C ATOM 4002 O GLY B 190 76.391 -8.933 -14.940 1.00 37.38 O ANISOU 4002 O GLY B 190 5723 5483 2996 -535 -312 629 O ATOM 4003 N THR B 191 76.220 -7.066 -13.678 1.00 36.27 N ANISOU 4003 N THR B 191 5587 5224 2970 -483 -386 733 N ATOM 4004 CA THR B 191 77.472 -6.449 -14.145 1.00 36.92 C ANISOU 4004 CA THR B 191 5711 5335 2981 -562 -331 764 C ATOM 4005 C THR B 191 78.692 -6.644 -13.234 1.00 36.01 C ANISOU 4005 C THR B 191 5541 5220 2922 -549 -230 715 C ATOM 4006 O THR B 191 79.805 -6.811 -13.737 1.00 36.77 O ANISOU 4006 O THR B 191 5648 5373 2950 -614 -151 691 O ATOM 4007 CB THR B 191 77.285 -4.930 -14.372 1.00 37.73 C ANISOU 4007 CB THR B 191 5881 5385 3071 -590 -414 872 C ATOM 4008 OG1 THR B 191 76.986 -4.284 -13.129 1.00 37.58 O ANISOU 4008 OG1 THR B 191 5821 5281 3175 -514 -449 890 O ATOM 4009 CG2 THR B 191 76.158 -4.669 -15.359 1.00 38.71 C ANISOU 4009 CG2 THR B 191 6065 5507 3135 -611 -521 927 C ATOM 4010 N GLN B 192 78.489 -6.601 -11.913 1.00 34.44 N ANISOU 4010 N GLN B 192 5283 4960 2841 -469 -235 699 N ATOM 4011 CA GLN B 192 79.593 -6.609 -10.943 1.00 33.44 C ANISOU 4011 CA GLN B 192 5108 4822 2776 -453 -155 665 C ATOM 4012 C GLN B 192 79.798 -7.991 -10.333 1.00 32.38 C ANISOU 4012 C GLN B 192 4902 4709 2692 -408 -91 568 C ATOM 4013 O GLN B 192 78.827 -8.719 -10.115 1.00 32.55 O ANISOU 4013 O GLN B 192 4897 4722 2749 -359 -125 538 O ATOM 4014 CB GLN B 192 79.314 -5.605 -9.822 1.00 32.87 C ANISOU 4014 CB GLN B 192 5019 4667 2803 -399 -202 712 C ATOM 4015 N THR B 193 81.056 -8.343 -10.063 1.00 31.56 N ANISOU 4015 N THR B 193 4767 4632 2594 -427 -1 520 N ATOM 4016 CA THR B 193 81.384 -9.555 -9.306 1.00 30.28 C ANISOU 4016 CA THR B 193 4533 4475 2497 -380 55 433 C ATOM 4017 C THR B 193 81.577 -9.187 -7.840 1.00 28.54 C ANISOU 4017 C THR B 193 4267 4192 2386 -321 57 439 C ATOM 4018 O THR B 193 82.122 -8.124 -7.520 1.00 28.00 O ANISOU 4018 O THR B 193 4213 4096 2329 -336 60 487 O ATOM 4019 CB THR B 193 82.661 -10.252 -9.815 1.00 31.17 C ANISOU 4019 CB THR B 193 4628 4652 2563 -427 149 364 C ATOM 4020 OG1 THR B 193 83.780 -9.365 -9.701 1.00 32.37 O ANISOU 4020 OG1 THR B 193 4789 4805 2705 -468 192 391 O ATOM 4021 CG2 THR B 193 82.496 -10.680 -11.258 1.00 31.98 C ANISOU 4021 CG2 THR B 193 4773 4826 2553 -489 154 347 C ATOM 4022 N TYR B 194 81.123 -10.077 -6.962 1.00 26.86 N ANISOU 4022 N TYR B 194 4001 3956 2249 -259 55 391 N ATOM 4023 CA TYR B 194 81.201 -9.879 -5.526 1.00 25.62 C ANISOU 4023 CA TYR B 194 3799 3744 2192 -205 55 390 C ATOM 4024 C TYR B 194 81.917 -11.063 -4.918 1.00 24.53 C ANISOU 4024 C TYR B 194 3604 3616 2099 -183 115 312 C ATOM 4025 O TYR B 194 81.481 -12.199 -5.086 1.00 24.43 O ANISOU 4025 O TYR B 194 3573 3621 2088 -168 115 262 O ATOM 4026 CB TYR B 194 79.799 -9.737 -4.944 1.00 25.12 C ANISOU 4026 CB TYR B 194 3726 3638 2180 -152 -20 414 C ATOM 4027 CG TYR B 194 79.109 -8.504 -5.453 1.00 25.59 C ANISOU 4027 CG TYR B 194 3836 3676 2210 -166 -90 490 C ATOM 4028 CD1 TYR B 194 79.436 -7.243 -4.954 1.00 25.47 C ANISOU 4028 CD1 TYR B 194 3832 3617 2226 -165 -105 542 C ATOM 4029 CD2 TYR B 194 78.160 -8.585 -6.469 1.00 26.09 C ANISOU 4029 CD2 TYR B 194 3938 3760 2216 -181 -145 509 C ATOM 4030 CE1 TYR B 194 78.819 -6.100 -5.436 1.00 26.04 C ANISOU 4030 CE1 TYR B 194 3953 3662 2278 -177 -177 613 C ATOM 4031 CE2 TYR B 194 77.536 -7.448 -6.955 1.00 26.67 C ANISOU 4031 CE2 TYR B 194 4060 3808 2267 -193 -219 581 C ATOM 4032 CZ TYR B 194 77.871 -6.211 -6.440 1.00 26.58 C ANISOU 4032 CZ TYR B 194 4060 3748 2292 -190 -236 633 C ATOM 4033 OH TYR B 194 77.246 -5.090 -6.934 1.00 27.43 O ANISOU 4033 OH TYR B 194 4217 3823 2383 -201 -318 704 O ATOM 4034 N ILE B 195 83.030 -10.778 -4.250 1.00 24.07 N ANISOU 4034 N ILE B 195 3522 3546 2080 -184 163 304 N ATOM 4035 CA ILE B 195 83.867 -11.788 -3.604 1.00 23.55 C ANISOU 4035 CA ILE B 195 3402 3482 2066 -164 216 233 C ATOM 4036 C ILE B 195 84.120 -11.360 -2.167 1.00 22.62 C ANISOU 4036 C ILE B 195 3251 3310 2035 -124 213 249 C ATOM 4037 O ILE B 195 84.573 -10.245 -1.920 1.00 22.38 O ANISOU 4037 O ILE B 195 3233 3262 2008 -137 217 293 O ATOM 4038 CB ILE B 195 85.225 -11.937 -4.338 1.00 24.23 C ANISOU 4038 CB ILE B 195 3485 3617 2105 -214 289 193 C ATOM 4039 CG1 ILE B 195 85.007 -12.416 -5.780 1.00 25.10 C ANISOU 4039 CG1 ILE B 195 3627 3788 2122 -260 297 169 C ATOM 4040 CG2 ILE B 195 86.157 -12.884 -3.578 1.00 23.94 C ANISOU 4040 CG2 ILE B 195 3387 3572 2137 -187 336 120 C ATOM 4041 CD1 ILE B 195 86.212 -12.229 -6.680 1.00 25.89 C ANISOU 4041 CD1 ILE B 195 3736 3947 2154 -326 364 143 C ATOM 4042 N CYS B 196 83.824 -12.240 -1.216 1.00 21.74 N ANISOU 4042 N CYS B 196 3098 3173 1991 -79 205 213 N ATOM 4043 CA CYS B 196 84.216 -11.990 0.168 1.00 21.19 C ANISOU 4043 CA CYS B 196 2993 3059 1998 -47 209 217 C ATOM 4044 C CYS B 196 85.596 -12.590 0.394 1.00 21.28 C ANISOU 4044 C CYS B 196 2969 3080 2035 -54 268 164 C ATOM 4045 O CYS B 196 85.872 -13.690 -0.082 1.00 22.25 O ANISOU 4045 O CYS B 196 3077 3228 2150 -58 290 106 O ATOM 4046 CB CYS B 196 83.193 -12.553 1.158 1.00 20.55 C ANISOU 4046 CB CYS B 196 2888 2947 1974 -3 168 212 C ATOM 4047 SG CYS B 196 83.025 -14.343 1.183 1.00 20.24 S ANISOU 4047 SG CYS B 196 2820 2917 1955 12 173 142 S ATOM 4048 N ASN B 197 86.444 -11.864 1.116 1.00 21.12 N ANISOU 4048 N ASN B 197 2935 3038 2050 -54 289 180 N ATOM 4049 CA ASN B 197 87.805 -12.295 1.433 1.00 21.36 C ANISOU 4049 CA ASN B 197 2928 3074 2115 -58 340 132 C ATOM 4050 C ASN B 197 87.867 -12.516 2.939 1.00 20.74 C ANISOU 4050 C ASN B 197 2813 2946 2121 -16 323 129 C ATOM 4051 O ASN B 197 87.755 -11.567 3.725 1.00 20.59 O ANISOU 4051 O ASN B 197 2798 2899 2128 -7 306 174 O ATOM 4052 CB ASN B 197 88.837 -11.239 1.018 1.00 21.94 C ANISOU 4052 CB ASN B 197 3013 3165 2157 -99 381 152 C ATOM 4053 CG ASN B 197 88.469 -10.527 -0.271 1.00 22.78 C ANISOU 4053 CG ASN B 197 3174 3309 2175 -147 378 191 C ATOM 4054 OD1 ASN B 197 88.105 -9.351 -0.256 1.00 22.94 O ANISOU 4054 OD1 ASN B 197 3228 3310 2178 -158 350 258 O ATOM 4055 ND2 ASN B 197 88.556 -11.235 -1.386 1.00 23.30 N ANISOU 4055 ND2 ASN B 197 3248 3424 2183 -175 402 150 N ATOM 4056 N VAL B 198 88.018 -13.774 3.334 1.00 20.75 N ANISOU 4056 N VAL B 198 2782 2939 2165 7 322 76 N ATOM 4057 CA VAL B 198 87.955 -14.169 4.739 1.00 20.53 C ANISOU 4057 CA VAL B 198 2725 2865 2209 41 298 74 C ATOM 4058 C VAL B 198 89.358 -14.557 5.186 1.00 21.11 C ANISOU 4058 C VAL B 198 2760 2930 2332 44 331 31 C ATOM 4059 O VAL B 198 89.994 -15.381 4.541 1.00 21.97 O ANISOU 4059 O VAL B 198 2851 3059 2439 39 356 -27 O ATOM 4060 CB VAL B 198 86.969 -15.341 4.925 1.00 20.20 C ANISOU 4060 CB VAL B 198 2680 2814 2183 62 260 54 C ATOM 4061 CG1 VAL B 198 86.933 -15.798 6.378 1.00 19.64 C ANISOU 4061 CG1 VAL B 198 2583 2699 2180 87 233 55 C ATOM 4062 CG2 VAL B 198 85.580 -14.930 4.451 1.00 20.17 C ANISOU 4062 CG2 VAL B 198 2709 2822 2133 58 226 93 C ATOM 4063 N ASN B 199 89.849 -13.942 6.261 1.00 21.29 N ANISOU 4063 N ASN B 199 2768 2923 2399 54 329 54 N ATOM 4064 CA ASN B 199 91.155 -14.290 6.830 1.00 22.06 C ANISOU 4064 CA ASN B 199 2825 3006 2552 61 351 15 C ATOM 4065 C ASN B 199 90.971 -14.729 8.273 1.00 20.97 C ANISOU 4065 C ASN B 199 2669 2822 2478 89 312 23 C ATOM 4066 O ASN B 199 90.326 -14.045 9.062 1.00 20.69 O ANISOU 4066 O ASN B 199 2647 2768 2446 94 288 71 O ATOM 4067 CB ASN B 199 92.130 -13.103 6.770 1.00 23.44 C ANISOU 4067 CB ASN B 199 2996 3191 2718 38 390 32 C ATOM 4068 CG ASN B 199 93.527 -13.455 7.283 1.00 24.86 C ANISOU 4068 CG ASN B 199 3129 3359 2957 45 414 -14 C ATOM 4069 OD1 ASN B 199 94.003 -14.583 7.119 1.00 27.01 O ANISOU 4069 OD1 ASN B 199 3371 3632 3260 57 418 -75 O ATOM 4070 ND2 ASN B 199 94.185 -12.489 7.919 1.00 25.84 N ANISOU 4070 ND2 ASN B 199 3245 3471 3102 38 426 11 N ATOM 4071 N HIS B 200 91.535 -15.885 8.598 1.00 20.58 N ANISOU 4071 N HIS B 200 2589 2752 2478 105 303 -26 N ATOM 4072 CA HIS B 200 91.536 -16.410 9.958 1.00 19.73 C ANISOU 4072 CA HIS B 200 2466 2599 2432 125 262 -19 C ATOM 4073 C HIS B 200 92.986 -16.713 10.309 1.00 20.21 C ANISOU 4073 C HIS B 200 2486 2642 2550 133 276 -62 C ATOM 4074 O HIS B 200 93.528 -17.757 9.922 1.00 20.61 O ANISOU 4074 O HIS B 200 2512 2687 2631 144 275 -120 O ATOM 4075 CB HIS B 200 90.658 -17.656 10.022 1.00 19.53 C ANISOU 4075 CB HIS B 200 2448 2558 2416 136 221 -34 C ATOM 4076 CG HIS B 200 90.610 -18.305 11.371 1.00 19.00 C ANISOU 4076 CG HIS B 200 2371 2445 2404 147 174 -24 C ATOM 4077 ND1 HIS B 200 90.103 -17.690 12.494 1.00 18.89 N ANISOU 4077 ND1 HIS B 200 2367 2417 2392 142 153 26 N ATOM 4078 CD2 HIS B 200 90.976 -19.547 11.759 1.00 18.81 C ANISOU 4078 CD2 HIS B 200 2330 2385 2433 159 141 -58 C ATOM 4079 CE1 HIS B 200 90.174 -18.528 13.514 1.00 18.11 C ANISOU 4079 CE1 HIS B 200 2261 2280 2338 146 111 25 C ATOM 4080 NE2 HIS B 200 90.706 -19.657 13.095 1.00 18.97 N ANISOU 4080 NE2 HIS B 200 2354 2371 2481 157 99 -23 N ATOM 4081 N LYS B 201 93.618 -15.776 11.013 1.00 20.37 N ANISOU 4081 N LYS B 201 2497 2654 2588 129 287 -36 N ATOM 4082 CA LYS B 201 95.052 -15.850 11.307 1.00 20.75 C ANISOU 4082 CA LYS B 201 2504 2690 2689 135 304 -75 C ATOM 4083 C LYS B 201 95.461 -17.083 12.118 1.00 21.24 C ANISOU 4083 C LYS B 201 2539 2707 2824 160 258 -108 C ATOM 4084 O LYS B 201 96.454 -17.712 11.777 1.00 21.58 O ANISOU 4084 O LYS B 201 2545 2746 2909 170 269 -169 O ATOM 4085 CB LYS B 201 95.536 -14.570 12.004 1.00 20.52 C ANISOU 4085 CB LYS B 201 2473 2657 2664 125 319 -36 C ATOM 4086 N PRO B 202 94.691 -17.461 13.164 1.00 21.29 N ANISOU 4086 N PRO B 202 2564 2679 2846 166 205 -71 N ATOM 4087 CA PRO B 202 95.110 -18.615 13.988 1.00 21.71 C ANISOU 4087 CA PRO B 202 2598 2683 2969 184 152 -94 C ATOM 4088 C PRO B 202 95.287 -19.948 13.254 1.00 22.49 C ANISOU 4088 C PRO B 202 2679 2769 3096 200 138 -156 C ATOM 4089 O PRO B 202 96.097 -20.774 13.687 1.00 22.68 O ANISOU 4089 O PRO B 202 2674 2752 3191 219 104 -193 O ATOM 4090 CB PRO B 202 94.004 -18.708 15.040 1.00 21.43 C ANISOU 4090 CB PRO B 202 2594 2626 2920 174 105 -37 C ATOM 4091 CG PRO B 202 93.502 -17.312 15.163 1.00 20.93 C ANISOU 4091 CG PRO B 202 2552 2594 2807 158 136 10 C ATOM 4092 CD PRO B 202 93.533 -16.775 13.759 1.00 21.09 C ANISOU 4092 CD PRO B 202 2575 2658 2782 154 189 -8 C ATOM 4093 N SER B 203 94.547 -20.158 12.166 1.00 22.54 N ANISOU 4093 N SER B 203 2703 2808 3053 194 159 -169 N ATOM 4094 CA SER B 203 94.702 -21.358 11.330 1.00 23.24 C ANISOU 4094 CA SER B 203 2774 2891 3164 208 153 -236 C ATOM 4095 C SER B 203 95.478 -21.084 10.031 1.00 24.29 C ANISOU 4095 C SER B 203 2881 3074 3276 203 218 -297 C ATOM 4096 O SER B 203 95.658 -21.997 9.224 1.00 25.08 O ANISOU 4096 O SER B 203 2961 3177 3390 213 222 -363 O ATOM 4097 CB SER B 203 93.326 -21.925 10.977 1.00 23.05 C ANISOU 4097 CB SER B 203 2787 2872 3100 201 129 -217 C ATOM 4098 OG SER B 203 92.654 -21.057 10.076 1.00 22.57 O ANISOU 4098 OG SER B 203 2751 2866 2958 181 174 -195 O ATOM 4099 N ASN B 204 95.928 -19.841 9.832 1.00 24.64 N ANISOU 4099 N ASN B 204 2923 3154 3284 184 269 -276 N ATOM 4100 CA ASN B 204 96.578 -19.402 8.589 1.00 25.92 C ANISOU 4100 CA ASN B 204 3068 3373 3408 165 337 -322 C ATOM 4101 C ASN B 204 95.709 -19.682 7.350 1.00 26.66 C ANISOU 4101 C ASN B 204 3190 3508 3433 150 356 -334 C ATOM 4102 O ASN B 204 96.211 -20.121 6.313 1.00 27.93 O ANISOU 4102 O ASN B 204 3326 3703 3583 143 392 -404 O ATOM 4103 CB ASN B 204 97.965 -20.037 8.445 1.00 26.61 C ANISOU 4103 CB ASN B 204 3093 3453 3564 182 351 -409 C ATOM 4104 N THR B 205 94.405 -19.430 7.486 1.00 26.75 N ANISOU 4104 N THR B 205 3248 3518 3397 143 329 -270 N ATOM 4105 CA THR B 205 93.410 -19.683 6.439 1.00 27.23 C ANISOU 4105 CA THR B 205 3340 3612 3393 130 335 -272 C ATOM 4106 C THR B 205 93.063 -18.370 5.747 1.00 26.85 C ANISOU 4106 C THR B 205 3326 3612 3262 97 373 -224 C ATOM 4107 O THR B 205 92.760 -17.381 6.420 1.00 26.53 O ANISOU 4107 O THR B 205 3306 3561 3213 93 364 -158 O ATOM 4108 CB THR B 205 92.100 -20.262 7.033 1.00 27.34 C ANISOU 4108 CB THR B 205 3384 3593 3412 143 275 -232 C ATOM 4109 OG1 THR B 205 92.366 -21.493 7.716 1.00 28.37 O ANISOU 4109 OG1 THR B 205 3490 3672 3618 168 231 -268 O ATOM 4110 CG2 THR B 205 91.056 -20.521 5.940 1.00 28.12 C ANISOU 4110 CG2 THR B 205 3513 3726 3444 130 278 -236 C ATOM 4111 N LYS B 206 93.110 -18.369 4.416 1.00 26.91 N ANISOU 4111 N LYS B 206 3342 3672 3210 72 413 -256 N ATOM 4112 CA LYS B 206 92.611 -17.264 3.592 1.00 26.93 C ANISOU 4112 CA LYS B 206 3387 3720 3126 35 438 -207 C ATOM 4113 C LYS B 206 91.688 -17.846 2.521 1.00 27.15 C ANISOU 4113 C LYS B 206 3441 3779 3095 24 430 -223 C ATOM 4114 O LYS B 206 92.123 -18.662 1.711 1.00 27.69 O ANISOU 4114 O LYS B 206 3488 3874 3157 18 455 -296 O ATOM 4115 CB LYS B 206 93.768 -16.505 2.939 1.00 27.45 C ANISOU 4115 CB LYS B 206 3438 3829 3162 -1 500 -228 C ATOM 4116 N VAL B 207 90.417 -17.444 2.537 1.00 26.53 N ANISOU 4116 N VAL B 207 3406 3696 2979 24 395 -161 N ATOM 4117 CA VAL B 207 89.415 -17.928 1.582 1.00 26.84 C ANISOU 4117 CA VAL B 207 3474 3763 2962 14 380 -168 C ATOM 4118 C VAL B 207 88.798 -16.740 0.849 1.00 27.01 C ANISOU 4118 C VAL B 207 3543 3817 2901 -19 383 -106 C ATOM 4119 O VAL B 207 88.331 -15.789 1.482 1.00 26.79 O ANISOU 4119 O VAL B 207 3534 3766 2878 -14 359 -39 O ATOM 4120 CB VAL B 207 88.283 -18.718 2.284 1.00 26.61 C ANISOU 4120 CB VAL B 207 3449 3693 2968 45 321 -154 C ATOM 4121 CG1 VAL B 207 87.252 -19.215 1.267 1.00 27.02 C ANISOU 4121 CG1 VAL B 207 3528 3774 2964 34 305 -164 C ATOM 4122 CG2 VAL B 207 88.846 -19.890 3.075 1.00 26.72 C ANISOU 4122 CG2 VAL B 207 3422 3664 3065 75 306 -206 C ATOM 4123 N ASP B 208 88.817 -16.797 -0.480 1.00 28.00 N ANISOU 4123 N ASP B 208 3688 3997 2954 -55 410 -130 N ATOM 4124 CA ASP B 208 88.050 -15.889 -1.320 1.00 28.33 C ANISOU 4124 CA ASP B 208 3782 4068 2912 -87 398 -71 C ATOM 4125 C ASP B 208 86.886 -16.696 -1.867 1.00 28.30 C ANISOU 4125 C ASP B 208 3797 4075 2882 -79 361 -84 C ATOM 4126 O ASP B 208 87.098 -17.763 -2.462 1.00 29.30 O ANISOU 4126 O ASP B 208 3906 4225 3003 -82 379 -154 O ATOM 4127 CB ASP B 208 88.898 -15.356 -2.476 1.00 29.44 C ANISOU 4127 CB ASP B 208 3937 4268 2979 -144 453 -86 C ATOM 4128 CG ASP B 208 90.101 -14.561 -2.010 1.00 29.74 C ANISOU 4128 CG ASP B 208 3956 4303 3043 -159 494 -78 C ATOM 4129 OD1 ASP B 208 89.990 -13.773 -1.044 1.00 29.45 O ANISOU 4129 OD1 ASP B 208 3922 4221 3046 -139 470 -21 O ATOM 4130 OD2 ASP B 208 91.171 -14.713 -2.636 1.00 30.97 O ANISOU 4130 OD2 ASP B 208 4090 4502 3176 -192 552 -133 O ATOM 4131 N LYS B 209 85.664 -16.204 -1.665 1.00 27.40 N ANISOU 4131 N LYS B 209 3714 3942 2756 -68 310 -21 N ATOM 4132 CA LYS B 209 84.465 -16.877 -2.159 1.00 27.47 C ANISOU 4132 CA LYS B 209 3739 3959 2738 -61 270 -28 C ATOM 4133 C LYS B 209 83.649 -15.931 -3.033 1.00 27.24 C ANISOU 4133 C LYS B 209 3762 3955 2632 -90 243 31 C ATOM 4134 O LYS B 209 83.181 -14.893 -2.562 1.00 25.88 O ANISOU 4134 O LYS B 209 3608 3758 2468 -82 212 97 O ATOM 4135 CB LYS B 209 83.614 -17.376 -0.982 1.00 27.32 C ANISOU 4135 CB LYS B 209 3701 3890 2789 -17 223 -17 C ATOM 4136 CG LYS B 209 82.393 -18.216 -1.360 1.00 28.09 C ANISOU 4136 CG LYS B 209 3808 3993 2872 -9 183 -31 C ATOM 4137 CD LYS B 209 82.706 -19.468 -2.179 1.00 29.18 C ANISOU 4137 CD LYS B 209 3935 4157 2994 -19 203 -107 C ATOM 4138 CE LYS B 209 83.694 -20.397 -1.483 1.00 29.61 C ANISOU 4138 CE LYS B 209 3945 4183 3122 2 226 -165 C ATOM 4139 NZ LYS B 209 83.915 -21.667 -2.233 1.00 30.64 N ANISOU 4139 NZ LYS B 209 4060 4332 3249 -2 239 -246 N ATOM 4140 N LYS B 210 83.482 -16.294 -4.307 1.00 27.72 N ANISOU 4140 N LYS B 210 3847 4066 2619 -123 251 7 N ATOM 4141 CA LYS B 210 82.611 -15.545 -5.209 1.00 28.43 C ANISOU 4141 CA LYS B 210 3990 4179 2632 -151 215 62 C ATOM 4142 C LYS B 210 81.159 -15.850 -4.869 1.00 27.81 C ANISOU 4142 C LYS B 210 3914 4074 2579 -116 149 81 C ATOM 4143 O LYS B 210 80.789 -17.015 -4.716 1.00 27.89 O ANISOU 4143 O LYS B 210 3900 4080 2618 -94 142 31 O ATOM 4144 CB LYS B 210 82.893 -15.909 -6.669 1.00 29.66 C ANISOU 4144 CB LYS B 210 4171 4401 2696 -203 244 25 C ATOM 4145 CG LYS B 210 82.175 -15.019 -7.675 1.00 30.64 C ANISOU 4145 CG LYS B 210 4357 4552 2732 -243 206 89 C ATOM 4146 CD LYS B 210 82.602 -15.329 -9.103 1.00 31.95 C ANISOU 4146 CD LYS B 210 4551 4792 2798 -306 243 51 C ATOM 4147 CE LYS B 210 82.127 -14.271 -10.088 1.00 33.07 C ANISOU 4147 CE LYS B 210 4761 4960 2844 -358 207 126 C ATOM 4148 NZ LYS B 210 80.652 -14.284 -10.312 1.00 33.40 N ANISOU 4148 NZ LYS B 210 4830 4985 2875 -337 126 164 N ATOM 4149 N VAL B 211 80.350 -14.799 -4.743 1.00 27.52 N ANISOU 4149 N VAL B 211 3904 4016 2535 -110 99 152 N ATOM 4150 CA VAL B 211 78.936 -14.929 -4.415 1.00 27.28 C ANISOU 4150 CA VAL B 211 3872 3962 2529 -78 35 171 C ATOM 4151 C VAL B 211 78.137 -14.569 -5.666 1.00 28.54 C ANISOU 4151 C VAL B 211 4081 4154 2610 -107 -7 201 C ATOM 4152 O VAL B 211 78.098 -13.409 -6.070 1.00 28.62 O ANISOU 4152 O VAL B 211 4129 4163 2583 -128 -30 261 O ATOM 4153 CB VAL B 211 78.554 -14.023 -3.222 1.00 26.30 C ANISOU 4153 CB VAL B 211 3733 3788 2471 -43 5 218 C ATOM 4154 CG1 VAL B 211 77.085 -14.205 -2.850 1.00 25.90 C ANISOU 4154 CG1 VAL B 211 3671 3720 2450 -11 -56 227 C ATOM 4155 CG2 VAL B 211 79.452 -14.313 -2.021 1.00 25.73 C ANISOU 4155 CG2 VAL B 211 3619 3689 2470 -22 47 192 C ATOM 4156 N GLU B 212 77.525 -15.582 -6.273 1.00 29.69 N ANISOU 4156 N GLU B 212 4225 4326 2729 -109 -20 160 N ATOM 4157 CA GLU B 212 76.778 -15.435 -7.520 1.00 31.43 C ANISOU 4157 CA GLU B 212 4492 4582 2869 -139 -60 180 C ATOM 4158 C GLU B 212 75.278 -15.464 -7.244 1.00 31.24 C ANISOU 4158 C GLU B 212 4461 4534 2875 -105 -133 200 C ATOM 4159 O GLU B 212 74.837 -16.155 -6.318 1.00 30.29 O ANISOU 4159 O GLU B 212 4297 4388 2825 -67 -138 170 O ATOM 4160 CB GLU B 212 77.135 -16.573 -8.477 1.00 32.73 C ANISOU 4160 CB GLU B 212 4659 4799 2980 -170 -23 112 C ATOM 4161 CG GLU B 212 78.629 -16.754 -8.673 1.00 33.83 C ANISOU 4161 CG GLU B 212 4788 4965 3101 -200 56 71 C ATOM 4162 CD GLU B 212 78.967 -17.595 -9.886 1.00 35.28 C ANISOU 4162 CD GLU B 212 4984 5211 3211 -242 90 8 C ATOM 4163 OE1 GLU B 212 78.546 -18.772 -9.939 1.00 36.47 O ANISOU 4163 OE1 GLU B 212 5110 5364 3381 -223 85 -51 O ATOM 4164 OE2 GLU B 212 79.655 -17.075 -10.787 1.00 36.95 O ANISOU 4164 OE2 GLU B 212 5228 5469 3341 -298 123 16 O ATOM 4165 N PRO B 213 74.479 -14.736 -8.050 1.00 32.29 N ANISOU 4165 N PRO B 213 4636 4677 2957 -121 -193 249 N ATOM 4166 CA PRO B 213 73.022 -14.844 -7.906 1.00 32.55 C ANISOU 4166 CA PRO B 213 4658 4693 3018 -89 -264 258 C ATOM 4167 C PRO B 213 72.487 -16.244 -8.203 1.00 33.33 C ANISOU 4167 C PRO B 213 4737 4818 3111 -86 -263 195 C ATOM 4168 O PRO B 213 73.118 -17.001 -8.945 1.00 33.49 O ANISOU 4168 O PRO B 213 4768 4877 3079 -118 -220 152 O ATOM 4169 CB PRO B 213 72.478 -13.838 -8.934 1.00 33.20 C ANISOU 4169 CB PRO B 213 4796 4784 3034 -115 -328 320 C ATOM 4170 CG PRO B 213 73.619 -12.940 -9.263 1.00 33.40 C ANISOU 4170 CG PRO B 213 4859 4815 3016 -154 -294 360 C ATOM 4171 CD PRO B 213 74.858 -13.762 -9.093 1.00 33.05 C ANISOU 4171 CD PRO B 213 4791 4796 2969 -170 -203 301 C ATOM 4172 N LYS B 214 71.341 -16.579 -7.611 1.00 33.84 N ANISOU 4172 N LYS B 214 4769 4860 3229 -50 -308 186 N ATOM 4173 CA LYS B 214 70.643 -17.828 -7.910 1.00 35.06 C ANISOU 4173 CA LYS B 214 4906 5035 3380 -49 -319 133 C ATOM 4174 C LYS B 214 70.156 -17.790 -9.361 1.00 36.94 C ANISOU 4174 C LYS B 214 5191 5315 3529 -83 -358 143 C ATOM 4175 O LYS B 214 69.540 -16.812 -9.781 1.00 37.75 O ANISOU 4175 O LYS B 214 5322 5413 3607 -85 -417 198 O ATOM 4176 CB LYS B 214 69.458 -18.019 -6.962 1.00 34.66 C ANISOU 4176 CB LYS B 214 4811 4955 3402 -10 -362 129 C ATOM 4177 N SER B 215 70.444 -18.845 -10.121 1.00 38.33 N ANISOU 4177 N SER B 215 5376 5531 3659 -110 -328 89 N ATOM 4178 CA SER B 215 70.196 -18.850 -11.566 1.00 40.04 C ANISOU 4178 CA SER B 215 5641 5796 3777 -152 -353 92 C ATOM 4179 C SER B 215 68.715 -19.062 -11.899 1.00 41.22 C ANISOU 4179 C SER B 215 5789 5948 3925 -139 -431 96 C ATOM 4180 O SER B 215 68.136 -18.291 -12.671 1.00 42.04 O ANISOU 4180 O SER B 215 5933 6063 3976 -155 -492 145 O ATOM 4181 CB SER B 215 71.059 -19.908 -12.258 1.00 40.40 C ANISOU 4181 CB SER B 215 5691 5886 3774 -186 -290 22 C ATOM 4182 OG SER B 215 71.222 -19.594 -13.628 1.00 41.05 O ANISOU 4182 OG SER B 215 5828 6022 3747 -240 -296 35 O ATOM 4183 N CYS B 216 68.109 -20.096 -11.316 1.00 41.84 N ANISOU 4183 N CYS B 216 5823 6014 4062 -112 -434 47 N ATOM 4184 CA CYS B 216 66.676 -20.361 -11.508 1.00 42.68 C ANISOU 4184 CA CYS B 216 5918 6122 4178 -98 -505 44 C ATOM 4185 C CYS B 216 65.854 -19.431 -10.614 1.00 43.03 C ANISOU 4185 C CYS B 216 5935 6124 4291 -58 -556 90 C ATOM 4186 O CYS B 216 65.428 -18.354 -11.041 1.00 43.78 O ANISOU 4186 O CYS B 216 6057 6214 4361 -58 -613 145 O ATOM 4187 CB CYS B 216 66.330 -21.831 -11.210 1.00 42.64 C ANISOU 4187 CB CYS B 216 5873 6118 4210 -91 -488 -27 C ATOM 4188 SG CYS B 216 64.985 -22.479 -12.237 1.00 43.61 S ANISOU 4188 SG CYS B 216 6005 6275 4288 -104 -556 -52 S TER 4189 CYS B 216 HETATM 4190 O HOH A 301 76.987 -28.833 6.380 1.00 34.37 O HETATM 4191 O HOH A 302 79.974 13.686 38.795 1.00 35.31 O HETATM 4192 O HOH A 303 73.390 3.194 24.599 1.00 42.50 O HETATM 4193 O HOH A 304 71.340 -21.459 14.488 1.00 20.20 O HETATM 4194 O HOH A 305 76.883 -5.981 18.702 1.00 31.31 O HETATM 4195 O HOH A 306 101.139 15.105 42.702 1.00 23.55 O HETATM 4196 O HOH A 307 67.643 -30.585 12.548 1.00 31.12 O HETATM 4197 O HOH A 308 75.074 -22.295 3.234 1.00 19.05 O HETATM 4198 O HOH A 309 80.767 6.180 16.132 1.00 23.03 O HETATM 4199 O HOH A 310 82.535 -1.446 29.794 1.00 36.44 O HETATM 4200 O HOH A 311 78.222 9.024 38.522 1.00 28.56 O HETATM 4201 O HOH A 312 63.689 -9.510 0.419 1.00 26.69 O HETATM 4202 O HOH A 313 88.275 5.155 47.687 1.00 32.19 O HETATM 4203 O HOH A 314 86.547 10.377 17.939 1.00 38.62 O HETATM 4204 O HOH A 315 66.324 12.670 23.164 1.00 43.52 O HETATM 4205 O HOH A 316 87.296 6.844 19.324 1.00 25.94 O HETATM 4206 O HOH A 317 93.096 4.353 19.504 1.00 24.95 O HETATM 4207 O HOH A 318 74.281 -22.635 11.341 1.00 21.92 O HETATM 4208 O HOH A 319 97.691 21.048 27.780 1.00 23.80 O HETATM 4209 O HOH A 320 90.235 17.732 43.156 1.00 25.61 O HETATM 4210 O HOH A 321 77.100 -0.398 10.699 1.00 29.17 O HETATM 4211 O HOH A 322 74.503 11.224 35.788 1.00 35.08 O HETATM 4212 O HOH A 323 63.387 -29.261 -6.905 1.00 31.51 O HETATM 4213 O HOH A 324 73.250 11.602 30.636 1.00 37.86 O HETATM 4214 O HOH A 325 91.364 12.164 18.304 1.00 39.42 O HETATM 4215 O HOH A 326 91.627 9.872 47.789 1.00 43.93 O HETATM 4216 O HOH A 327 70.344 -24.636 -1.963 1.00 26.69 O HETATM 4217 O HOH A 328 74.891 -15.992 10.469 1.00 24.47 O HETATM 4218 O HOH A 329 75.086 6.973 14.801 1.00 17.37 O HETATM 4219 O HOH A 330 82.230 13.693 47.710 1.00 36.46 O HETATM 4220 O HOH A 331 91.520 22.868 30.925 1.00 19.57 O HETATM 4221 O HOH A 332 95.905 22.643 28.750 1.00 28.53 O HETATM 4222 O HOH A 333 80.717 20.438 25.646 1.00 15.73 O HETATM 4223 O HOH A 334 74.017 1.294 7.780 1.00 29.09 O HETATM 4224 O HOH A 335 73.562 15.624 15.147 1.00 35.41 O HETATM 4225 O HOH A 336 65.368 -14.945 15.735 1.00 47.52 O HETATM 4226 O HOH A 337 93.450 11.456 21.256 1.00 29.97 O HETATM 4227 O HOH A 338 94.182 9.307 45.694 1.00 37.02 O HETATM 4228 O HOH A 339 86.719 21.189 28.520 1.00 14.88 O HETATM 4229 O HOH A 340 67.116 1.562 19.830 1.00 27.87 O HETATM 4230 O HOH A 341 70.723 3.663 24.893 1.00 39.09 O HETATM 4231 O HOH A 342 78.248 1.903 17.398 1.00 34.63 O HETATM 4232 O HOH A 343 82.462 5.162 43.043 1.00 23.02 O HETATM 4233 O HOH A 344 74.522 13.212 33.760 1.00 38.36 O HETATM 4234 O HOH A 345 82.035 20.650 30.573 1.00 24.47 O HETATM 4235 O HOH A 346 89.802 21.238 35.022 1.00 30.72 O HETATM 4236 O HOH A 347 75.290 0.581 19.413 1.00 31.72 O HETATM 4237 O HOH A 348 74.388 -30.099 -2.232 1.00 36.88 O HETATM 4238 O HOH A 349 72.512 9.466 11.378 1.00 33.48 O HETATM 4239 O HOH A 350 66.922 12.973 26.490 1.00 43.84 O HETATM 4240 O HOH A 351 62.723 -20.202 22.153 1.00 42.03 O HETATM 4241 O HOH A 352 63.424 -11.967 18.016 1.00 35.44 O HETATM 4242 O HOH A 353 74.892 -1.142 12.109 1.00 18.18 O HETATM 4243 O HOH A 354 66.704 -20.253 19.483 1.00 31.07 O HETATM 4244 O AHOH A 355 72.343 -14.924 13.286 0.50 12.10 O HETATM 4245 O BHOH A 355 73.492 -15.025 12.594 0.50 30.14 O HETATM 4246 O HOH A 356 56.392 -21.926 -7.373 1.00 24.05 O HETATM 4247 O HOH A 357 76.568 3.774 6.855 1.00 38.82 O HETATM 4248 O HOH A 358 70.180 -28.574 -3.209 1.00 38.13 O HETATM 4249 O HOH A 359 81.115 16.051 44.852 1.00 37.05 O HETATM 4250 O HOH A 360 86.274 21.674 25.786 1.00 21.33 O HETATM 4251 O HOH A 361 78.712 2.148 34.041 1.00 32.08 O HETATM 4252 O HOH A 362 64.384 12.066 19.161 1.00 45.57 O HETATM 4253 O HOH A 363 52.852 -12.291 10.134 1.00 47.53 O HETATM 4254 O HOH A 364 94.022 22.719 38.866 1.00 47.05 O HETATM 4255 O HOH A 365 81.092 18.343 31.566 1.00 21.87 O HETATM 4256 O HOH A 366 81.831 20.521 37.358 1.00 38.12 O HETATM 4257 O HOH A 367 78.626 10.437 11.029 1.00 25.57 O HETATM 4258 O HOH A 368 87.003 1.643 47.330 1.00 39.05 O HETATM 4259 O HOH A 369 63.640 -33.170 -0.492 1.00 39.69 O HETATM 4260 O HOH A 370 61.475 0.043 21.051 1.00 39.10 O HETATM 4261 O HOH A 371 57.654 -19.368 0.085 1.00 31.14 O HETATM 4262 O HOH A 372 67.218 16.305 16.534 1.00 41.80 O HETATM 4263 O HOH A 373 80.843 17.400 12.534 1.00 43.64 O HETATM 4264 O HOH A 374 61.472 -9.450 -1.184 1.00 47.64 O HETATM 4265 O HOH A 375 54.475 -15.497 8.660 1.00 36.89 O HETATM 4266 O HOH A 376 77.259 0.507 29.935 1.00 40.05 O HETATM 4267 O HOH A 377 99.836 17.344 39.210 1.00 18.80 O HETATM 4268 O HOH A 378 85.461 23.534 23.216 1.00 22.24 O HETATM 4269 O HOH A 379 91.834 15.460 46.418 1.00 38.55 O HETATM 4270 O HOH A 380 49.644 -3.289 7.227 1.00 43.99 O HETATM 4271 O HOH A 381 60.184 7.649 10.138 1.00 45.97 O HETATM 4272 O HOH A 382 54.235 -9.886 16.022 1.00 31.81 O HETATM 4273 O HOH A 383 73.782 -20.296 14.822 1.00 35.49 O HETATM 4274 O HOH A 384 63.881 -17.105 16.382 1.00 67.47 O HETATM 4275 O HOH A 385 53.581 -11.279 7.735 1.00 29.74 O HETATM 4276 O HOH A 386 92.872 19.814 35.409 1.00 30.40 O HETATM 4277 O HOH A 387 96.945 22.517 32.048 1.00 41.72 O HETATM 4278 O HOH A 388 57.817 -23.670 18.599 1.00 31.40 O HETATM 4279 O HOH A 389 71.009 14.383 26.758 1.00 38.93 O HETATM 4280 O HOH A 390 80.516 3.041 18.252 1.00 23.40 O HETATM 4281 O HOH A 391 86.476 8.387 14.861 1.00 45.78 O HETATM 4282 O HOH A 392 83.571 -0.658 25.124 1.00 30.54 O HETATM 4283 O HOH A 393 60.398 -1.753 17.121 1.00 19.73 O HETATM 4284 O HOH A 394 80.929 7.200 43.990 1.00 27.27 O HETATM 4285 O HOH A 395 94.562 20.281 24.725 1.00 16.47 O HETATM 4286 O HOH A 396 80.186 1.431 40.698 1.00 48.95 O HETATM 4287 O HOH A 397 94.955 13.331 43.888 1.00 24.32 O HETATM 4288 O HOH A 398 72.252 -19.608 4.194 1.00 18.39 O HETATM 4289 O HOH A 399 83.279 11.232 18.204 1.00 18.68 O HETATM 4290 O HOH A 400 72.985 22.126 30.617 1.00 33.37 O HETATM 4291 O HOH A 401 75.939 11.176 9.573 1.00 37.93 O HETATM 4292 O HOH A 402 57.673 -27.995 10.310 1.00 24.44 O HETATM 4293 O HOH A 403 53.417 -27.954 9.720 1.00 31.86 O HETATM 4294 O HOH A 404 81.971 22.285 24.030 1.00 16.95 O HETATM 4295 O HOH A 405 85.971 22.546 33.159 1.00 35.01 O HETATM 4296 O HOH A 406 79.959 8.499 32.546 1.00 20.50 O HETATM 4297 O HOH A 407 86.220 1.658 39.008 1.00 21.96 O HETATM 4298 O HOH A 408 64.743 -26.731 19.375 1.00 25.60 O HETATM 4299 O HOH A 409 63.946 -20.652 16.173 1.00 21.60 O HETATM 4300 O HOH A 410 60.250 -5.942 0.672 1.00 36.74 O HETATM 4301 O HOH A 411 97.617 17.728 40.909 1.00 24.98 O HETATM 4302 O HOH A 412 58.949 -20.423 -5.192 1.00 32.75 O HETATM 4303 O HOH A 413 92.273 -1.217 36.650 1.00 15.99 O HETATM 4304 O HOH A 414 98.705 11.215 43.065 1.00 22.52 O HETATM 4305 O HOH A 415 82.447 9.647 46.835 1.00 33.72 O HETATM 4306 O HOH A 416 80.684 12.114 43.834 1.00 29.78 O HETATM 4307 O HOH A 417 57.761 -11.435 14.284 1.00 22.05 O HETATM 4308 O HOH A 418 73.928 0.250 4.687 1.00 28.67 O HETATM 4309 O HOH A 419 56.704 -30.059 3.329 1.00 27.17 O HETATM 4310 O HOH A 420 62.664 7.727 17.015 1.00 42.80 O HETATM 4311 O HOH A 421 87.796 11.673 49.824 1.00 36.40 O HETATM 4312 O HOH A 422 68.246 18.437 19.364 1.00 26.72 O HETATM 4313 O HOH A 423 79.369 12.706 41.242 1.00 38.97 O HETATM 4314 O HOH A 424 75.188 22.876 24.001 1.00 32.61 O HETATM 4315 O HOH A 425 59.100 -19.620 19.126 1.00 31.33 O HETATM 4316 O HOH A 426 97.440 18.572 23.757 1.00 32.34 O HETATM 4317 O HOH A 427 87.562 4.147 19.283 1.00 20.47 O HETATM 4318 O HOH A 428 58.832 -21.684 -8.864 1.00 30.87 O HETATM 4319 O HOH A 429 73.636 -3.335 19.119 1.00 26.98 O HETATM 4320 O HOH A 430 73.088 -17.275 20.709 1.00 33.69 O HETATM 4321 O HOH A 431 91.392 0.685 16.874 1.00 32.68 O HETATM 4322 O HOH A 432 73.961 -23.041 -3.814 1.00 40.65 O HETATM 4323 O HOH A 433 75.659 4.174 37.626 1.00 38.76 O HETATM 4324 O HOH A 434 73.489 4.258 4.767 1.00 41.93 O HETATM 4325 O HOH A 435 86.012 15.551 33.628 1.00 15.02 O HETATM 4326 O HOH A 436 67.990 -25.720 -1.192 1.00 23.98 O HETATM 4327 O HOH A 437 83.810 20.973 40.552 1.00 44.75 O HETATM 4328 O HOH A 438 79.755 2.315 12.817 1.00 36.38 O HETATM 4329 O HOH A 439 67.110 2.661 6.684 1.00 38.31 O HETATM 4330 O HOH A 440 98.744 15.061 35.295 1.00 15.62 O HETATM 4331 O HOH A 441 70.902 -15.767 19.750 1.00 30.13 O HETATM 4332 O HOH A 442 74.480 -12.447 19.680 1.00 34.77 O HETATM 4333 O HOH A 443 82.203 0.513 22.237 1.00 38.08 O HETATM 4334 O HOH A 444 56.627 -21.713 6.989 1.00 19.02 O HETATM 4335 O HOH A 445 62.173 -27.600 11.522 1.00 39.22 O HETATM 4336 O HOH A 446 67.178 -6.460 18.578 1.00 39.23 O HETATM 4337 O HOH A 447 93.176 2.968 43.412 1.00 19.48 O HETATM 4338 O HOH A 448 82.268 18.681 40.411 1.00 32.20 O HETATM 4339 O HOH A 449 72.738 -18.974 -0.099 1.00 32.70 O HETATM 4340 O HOH A 450 72.825 -0.882 10.330 1.00 16.93 O HETATM 4341 O HOH A 451 68.811 -2.019 3.433 1.00 28.25 O HETATM 4342 O HOH A 452 74.782 13.717 13.353 1.00 27.38 O HETATM 4343 O HOH A 453 65.872 -9.000 18.416 1.00 33.22 O HETATM 4344 O HOH A 454 83.160 6.378 49.593 1.00 36.14 O HETATM 4345 O HOH A 455 80.615 -1.065 25.935 1.00 36.02 O HETATM 4346 O HOH A 456 81.296 2.708 36.577 1.00 24.57 O HETATM 4347 O HOH A 457 88.869 21.085 19.237 1.00 16.68 O HETATM 4348 O HOH A 458 98.640 4.913 45.477 1.00 28.40 O HETATM 4349 O HOH A 459 80.805 19.637 16.044 1.00 25.46 O HETATM 4350 O HOH A 460 53.242 -23.454 15.231 1.00 34.68 O HETATM 4351 O HOH A 461 83.607 16.817 14.130 1.00 31.85 O HETATM 4352 O HOH A 462 66.850 11.037 12.168 1.00 32.67 O HETATM 4353 O HOH A 463 66.827 -2.361 1.066 1.00 39.09 O HETATM 4354 O HOH A 464 65.952 -24.539 -2.728 1.00 30.73 O HETATM 4355 O HOH A 465 68.077 6.585 26.868 1.00 44.88 O HETATM 4356 O HOH A 466 85.477 -0.672 35.631 1.00 28.08 O HETATM 4357 O HOH A 467 69.773 -25.677 15.678 1.00 30.28 O HETATM 4358 O HOH A 468 71.357 -34.768 7.807 1.00 38.33 O HETATM 4359 O HOH A 469 89.611 -0.552 36.569 1.00 20.83 O HETATM 4360 O HOH A 470 65.516 -36.007 4.092 1.00 41.15 O HETATM 4361 O HOH A 471 95.040 20.961 33.312 1.00 29.19 O HETATM 4362 O HOH A 472 73.610 18.510 29.515 1.00 31.87 O HETATM 4363 O HOH A 473 87.812 17.393 47.768 1.00 34.68 O HETATM 4364 O HOH A 474 84.400 21.759 38.059 1.00 50.86 O HETATM 4365 O HOH A 475 82.886 7.275 13.893 1.00 31.36 O HETATM 4366 O HOH A 476 72.389 9.672 35.147 1.00 38.82 O HETATM 4367 O HOH A 477 81.245 17.943 36.915 1.00 32.65 O HETATM 4368 O HOH A 478 72.512 15.057 29.911 1.00 29.31 O HETATM 4369 O HOH A 479 65.827 -29.727 -2.621 1.00 31.98 O HETATM 4370 O HOH A 480 59.389 -27.928 12.362 1.00 30.48 O HETATM 4371 O HOH A 481 54.751 -9.927 4.360 1.00 24.24 O HETATM 4372 O HOH A 482 91.700 19.242 41.514 1.00 34.57 O HETATM 4373 O HOH A 483 69.168 -10.285 19.930 1.00 37.66 O HETATM 4374 O HOH A 484 60.092 -33.278 1.691 1.00 30.14 O HETATM 4375 O HOH A 485 60.277 8.709 13.818 1.00 27.44 O HETATM 4376 O HOH A 486 65.678 -27.924 14.658 1.00 42.43 O HETATM 4377 O HOH A 487 53.154 -12.066 14.465 1.00 41.78 O HETATM 4378 O HOH A 488 92.097 -2.766 45.893 1.00 39.40 O HETATM 4379 O HOH A 489 61.792 -18.731 15.701 1.00 25.01 O HETATM 4380 O HOH A 490 74.318 -9.432 19.122 1.00 25.39 O HETATM 4381 O HOH A 491 71.042 10.188 14.310 1.00 33.93 O HETATM 4382 O HOH A 492 68.431 -34.764 12.429 1.00 45.90 O HETATM 4383 O HOH A 493 55.761 -30.842 7.565 1.00 42.07 O HETATM 4384 O HOH A 494 59.091 -13.717 0.319 1.00 25.54 O HETATM 4385 O HOH A 495 69.747 3.872 6.417 1.00 45.50 O HETATM 4386 O HOH A 496 83.797 16.646 45.356 1.00 30.00 O HETATM 4387 O HOH A 497 78.411 12.523 12.706 1.00 20.43 O HETATM 4388 O HOH A 498 59.861 -31.089 -2.290 1.00 41.30 O HETATM 4389 O HOH A 499 79.678 3.299 9.063 1.00 43.15 O HETATM 4390 O HOH A 500 63.930 -19.518 19.650 1.00 31.98 O HETATM 4391 O HOH A 501 82.521 24.236 35.888 1.00 49.59 O HETATM 4392 O HOH A 502 61.051 -25.856 16.733 1.00 30.99 O HETATM 4393 O HOH A 503 77.784 -26.521 7.955 1.00 25.62 O HETATM 4394 O HOH A 504 79.006 -3.773 14.822 1.00 26.25 O HETATM 4395 O HOH A 505 69.934 -18.464 20.582 1.00 41.92 O HETATM 4396 O HOH A 506 55.489 -4.863 12.742 1.00 25.26 O HETATM 4397 O HOH A 507 84.744 19.209 44.662 1.00 37.31 O HETATM 4398 O HOH A 508 67.995 -28.536 -1.511 1.00 31.27 O HETATM 4399 O HOH A 509 61.092 -20.039 -3.538 1.00 28.22 O HETATM 4400 O HOH A 510 85.876 21.192 16.223 1.00 15.82 O HETATM 4401 O HOH A 511 83.689 0.515 38.738 1.00 33.70 O HETATM 4402 O HOH A 512 58.186 -15.575 -1.461 1.00 40.28 O HETATM 4403 O HOH A 513 68.942 2.144 4.588 1.00 42.95 O HETATM 4404 O HOH A 514 93.323 4.891 47.552 1.00 48.20 O HETATM 4405 O HOH A 515 94.828 14.303 15.701 1.00 41.78 O HETATM 4406 O HOH A 516 58.788 -30.846 1.746 1.00 24.48 O HETATM 4407 O HOH A 517 69.011 6.477 6.463 1.00 42.81 O HETATM 4408 O HOH A 518 86.949 21.680 35.787 1.00 36.26 O HETATM 4409 O HOH A 519 78.908 21.561 30.837 1.00 46.79 O HETATM 4410 O HOH A 520 83.681 4.515 13.779 1.00 40.92 O HETATM 4411 O HOH A 521 70.806 -23.086 16.720 1.00 25.29 O HETATM 4412 O HOH A 522 71.173 -13.340 20.979 1.00 42.08 O HETATM 4413 O HOH A 523 73.047 -30.047 11.959 1.00 49.05 O HETATM 4414 O HOH A 524 69.903 9.489 10.312 1.00 39.43 O HETATM 4415 O HOH A 525 55.234 -18.183 3.868 1.00 36.22 O HETATM 4416 O HOH A 526 78.282 6.985 43.253 1.00 40.86 O HETATM 4417 O HOH A 527 85.774 23.283 29.918 1.00 34.71 O HETATM 4418 O HOH A 528 72.928 25.142 27.802 1.00 48.87 O HETATM 4419 O HOH A 529 54.855 -19.748 6.337 1.00 32.03 O HETATM 4420 O HOH A 530 62.076 4.907 18.406 1.00 41.64 O HETATM 4421 O HOH A 531 79.609 21.342 14.043 1.00 37.10 O HETATM 4422 O HOH A 532 94.297 0.660 16.432 1.00 36.55 O HETATM 4423 O HOH A 533 98.502 -1.174 44.715 1.00 35.03 O HETATM 4424 O HOH A 534 83.282 23.090 31.230 1.00 35.35 O HETATM 4425 O HOH A 535 92.318 17.732 45.006 1.00 47.52 O HETATM 4426 O HOH A 536 89.576 24.334 29.750 1.00 24.24 O HETATM 4427 O HOH A 537 63.614 -36.426 2.203 1.00 39.79 O HETATM 4428 O HOH A 538 92.325 24.051 33.334 1.00 34.73 O HETATM 4429 O HOH A 539 89.160 10.642 18.640 1.00 52.83 O HETATM 4430 O HOH A 540 98.702 16.959 43.346 1.00 39.36 O HETATM 4431 O HOH A 541 76.410 -8.193 20.326 1.00 42.82 O HETATM 4432 O HOH A 542 78.757 22.194 26.539 1.00 32.49 O HETATM 4433 O HOH A 543 82.121 3.486 45.154 1.00 30.83 O HETATM 4434 O HOH A 544 67.859 -35.612 2.748 1.00 46.72 O HETATM 4435 O HOH A 545 72.344 12.537 13.079 1.00 34.87 O HETATM 4436 O HOH A 546 80.988 7.260 46.841 1.00 40.54 O HETATM 4437 O HOH A 547 85.396 12.786 17.792 1.00 32.93 O HETATM 4438 O HOH A 548 82.879 24.221 25.705 1.00 29.57 O HETATM 4439 O HOH A 549 53.128 -11.957 3.519 1.00 43.60 O HETATM 4440 O HOH A 550 82.735 11.300 48.904 1.00 48.11 O HETATM 4441 O HOH A 551 83.593 -1.708 37.223 1.00 39.98 O HETATM 4442 O HOH A 552 57.298 2.629 22.107 1.00 36.52 O HETATM 4443 O HOH A 553 52.164 -7.995 15.627 1.00 36.87 O HETATM 4444 O HOH A 554 53.897 -19.454 1.863 1.00 39.28 O HETATM 4445 O HOH A 555 55.460 -29.509 10.473 1.00 34.50 O HETATM 4446 O HOH A 556 88.069 4.353 16.583 1.00 36.59 O HETATM 4447 O HOH A 557 84.340 24.518 27.955 1.00 42.20 O HETATM 4448 O HOH A 558 99.763 22.442 27.171 1.00 33.45 O HETATM 4449 O HOH A 559 84.955 19.730 14.139 1.00 37.18 O HETATM 4450 O HOH A 560 86.823 10.137 51.857 1.00 38.14 O HETATM 4451 O HOH A 561 50.126 -9.124 14.192 1.00 43.80 O HETATM 4452 O HOH C 301 109.025 8.832 52.191 1.00 28.49 O HETATM 4453 O HOH C 302 123.952 31.189 25.059 1.00 38.19 O HETATM 4454 O HOH C 303 121.057 5.255 48.645 1.00 29.57 O HETATM 4455 O HOH C 304 116.344 12.923 33.542 1.00 23.22 O HETATM 4456 O HOH C 305 118.878 17.768 42.687 1.00 30.25 O HETATM 4457 O HOH C 306 99.214 8.228 37.226 1.00 15.86 O HETATM 4458 O HOH C 307 127.570 20.630 37.103 1.00 42.07 O HETATM 4459 O HOH C 308 108.804 8.018 33.650 1.00 17.96 O HETATM 4460 O HOH C 309 101.511 10.389 44.365 1.00 26.99 O HETATM 4461 O HOH C 310 116.260 9.637 48.951 1.00 40.70 O HETATM 4462 O HOH C 311 114.344 18.527 47.021 1.00 22.62 O HETATM 4463 O HOH C 312 111.432 7.233 41.485 1.00 18.08 O HETATM 4464 O HOH C 313 116.630 35.311 37.215 1.00 37.19 O HETATM 4465 O HOH C 314 109.339 14.135 23.047 1.00 34.70 O HETATM 4466 O HOH C 315 102.265 6.125 49.875 1.00 39.15 O HETATM 4467 O HOH C 316 107.293 4.271 38.524 1.00 33.01 O HETATM 4468 O HOH C 317 107.368 14.895 28.837 1.00 28.10 O HETATM 4469 O HOH C 318 114.150 30.582 31.769 1.00 47.09 O HETATM 4470 O HOH C 319 103.117 16.954 42.885 1.00 19.69 O HETATM 4471 O HOH C 320 104.848 27.124 39.740 1.00 31.89 O HETATM 4472 O HOH C 321 118.208 9.730 40.078 1.00 25.31 O HETATM 4473 O HOH C 322 121.692 21.748 20.391 1.00 19.89 O HETATM 4474 O HOH C 323 115.628 5.049 43.974 1.00 32.65 O HETATM 4475 O HOH C 324 125.970 24.830 35.883 1.00 18.69 O HETATM 4476 O HOH C 325 97.334 27.462 35.652 1.00 37.40 O HETATM 4477 O HOH C 326 122.848 18.866 38.394 1.00 20.54 O HETATM 4478 O HOH C 327 112.004 28.519 33.759 1.00 39.93 O HETATM 4479 O HOH C 328 105.095 11.962 29.518 1.00 14.75 O HETATM 4480 O HOH C 329 101.607 9.238 52.193 1.00 36.55 O HETATM 4481 O HOH C 330 118.276 21.606 23.504 1.00 24.75 O HETATM 4482 O HOH C 331 109.877 23.513 45.375 1.00 34.55 O HETATM 4483 O HOH C 332 122.733 23.067 39.916 1.00 35.96 O HETATM 4484 O HOH C 333 130.723 24.026 32.410 1.00 27.55 O HETATM 4485 O HOH C 334 108.694 22.648 48.028 1.00 38.55 O HETATM 4486 O HOH C 335 123.019 14.262 29.998 1.00 25.57 O HETATM 4487 O HOH C 336 118.326 28.249 37.994 1.00 24.21 O HETATM 4488 O HOH C 337 119.295 8.420 48.473 1.00 34.94 O HETATM 4489 O HOH C 338 122.106 11.576 39.012 1.00 30.81 O HETATM 4490 O HOH C 339 125.115 16.597 23.211 1.00 40.05 O HETATM 4491 O HOH C 340 114.109 8.821 28.725 1.00 24.52 O HETATM 4492 O HOH C 341 113.523 22.730 45.395 1.00 32.85 O HETATM 4493 O HOH C 342 128.142 18.920 31.869 1.00 25.66 O HETATM 4494 O HOH C 343 113.576 24.362 34.582 1.00 29.85 O HETATM 4495 O HOH C 344 107.147 8.434 36.574 1.00 13.34 O HETATM 4496 O HOH C 345 111.290 30.210 36.725 1.00 39.52 O HETATM 4497 O HOH C 346 98.507 24.282 41.290 1.00 40.62 O HETATM 4498 O HOH C 347 112.942 7.371 47.094 1.00 33.53 O HETATM 4499 O HOH C 348 126.847 30.665 30.292 1.00 32.01 O HETATM 4500 O HOH C 349 112.067 6.276 44.147 1.00 20.91 O HETATM 4501 O HOH C 350 115.471 26.475 28.174 1.00 27.60 O HETATM 4502 O HOH C 351 118.262 13.439 48.277 1.00 32.65 O HETATM 4503 O HOH C 352 125.627 31.430 23.105 1.00 37.81 O HETATM 4504 O HOH C 353 105.384 19.055 31.758 1.00 33.09 O HETATM 4505 O HOH C 354 123.071 17.142 25.390 1.00 20.04 O HETATM 4506 O HOH C 355 99.479 17.419 36.504 1.00 16.33 O HETATM 4507 O HOH C 356 110.947 4.965 40.034 1.00 24.38 O HETATM 4508 O HOH C 357 96.785 23.215 34.481 1.00 45.64 O HETATM 4509 O HOH C 358 104.048 4.395 45.441 1.00 30.36 O HETATM 4510 O HOH C 359 108.678 21.152 30.732 1.00 29.51 O HETATM 4511 O HOH C 360 102.169 12.425 46.034 1.00 27.18 O HETATM 4512 O HOH C 361 120.084 11.687 40.775 1.00 23.78 O HETATM 4513 O HOH C 362 120.378 23.947 39.075 1.00 28.80 O HETATM 4514 O HOH C 363 124.142 27.232 41.939 1.00 35.38 O HETATM 4515 O HOH C 364 107.971 4.693 46.790 1.00 27.51 O HETATM 4516 O HOH C 365 99.948 24.210 33.977 1.00 25.12 O HETATM 4517 O HOH C 366 107.655 28.227 39.610 1.00 23.20 O HETATM 4518 O HOH C 367 99.599 10.934 36.860 1.00 16.46 O HETATM 4519 O HOH C 368 128.661 31.982 31.735 1.00 33.02 O HETATM 4520 O HOH C 369 104.067 20.600 43.792 1.00 19.85 O HETATM 4521 O HOH C 370 122.374 29.062 24.535 1.00 18.82 O HETATM 4522 O HOH C 371 123.261 13.210 34.018 1.00 29.64 O HETATM 4523 O HOH C 372 121.213 12.587 31.684 1.00 22.71 O HETATM 4524 O HOH C 373 103.830 25.428 42.927 1.00 42.47 O HETATM 4525 O HOH C 374 111.181 22.498 30.700 1.00 26.02 O HETATM 4526 O HOH C 375 100.898 13.318 36.047 1.00 16.93 O HETATM 4527 O HOH C 376 105.922 22.200 31.586 1.00 37.18 O HETATM 4528 O HOH C 377 103.998 14.102 28.143 1.00 33.16 O HETATM 4529 O HOH C 378 116.069 18.331 21.936 1.00 36.59 O HETATM 4530 O HOH C 379 120.144 26.908 39.376 1.00 25.79 O HETATM 4531 O HOH C 380 112.714 12.071 23.111 1.00 35.73 O HETATM 4532 O HOH C 381 118.984 10.119 23.968 1.00 30.07 O HETATM 4533 O HOH C 382 100.621 22.486 31.803 1.00 28.46 O HETATM 4534 O HOH C 383 125.354 23.845 39.741 1.00 45.49 O HETATM 4535 O HOH C 384 108.927 16.167 25.746 1.00 37.72 O HETATM 4536 O HOH C 385 123.127 10.734 35.108 1.00 39.42 O HETATM 4537 O HOH C 386 118.619 5.006 44.665 1.00 31.57 O HETATM 4538 O HOH C 387 99.153 9.962 45.873 1.00 44.57 O HETATM 4539 O HOH C 388 121.132 11.107 27.314 1.00 45.56 O HETATM 4540 O HOH C 389 102.168 17.587 30.800 1.00 33.72 O HETATM 4541 O HOH C 390 119.052 8.091 25.634 1.00 39.71 O HETATM 4542 O HOH C 391 110.907 23.699 27.744 1.00 40.37 O HETATM 4543 O HOH C 392 113.534 25.651 29.965 1.00 34.56 O HETATM 4544 O HOH C 393 130.459 24.171 35.131 1.00 42.20 O HETATM 4545 O HOH C 394 116.503 24.456 20.462 1.00 33.30 O HETATM 4546 O HOH C 395 113.928 24.833 22.234 1.00 48.13 O HETATM 4547 O HOH C 396 108.206 29.110 35.093 1.00 44.13 O HETATM 4548 O HOH C 397 98.192 7.482 46.268 1.00 38.27 O HETATM 4549 O HOH C 398 115.163 13.196 22.340 1.00 45.67 O HETATM 4550 O HOH C 399 115.299 21.011 24.154 1.00 32.34 O HETATM 4551 O HOH C 400 104.411 26.275 29.899 1.00 28.75 O HETATM 4552 O HOH C 401 121.921 30.279 40.683 1.00 37.79 O HETATM 4553 O HOH C 402 121.426 5.032 45.863 1.00 40.32 O HETATM 4554 O HOH C 403 100.863 18.881 43.086 1.00 38.05 O HETATM 4555 O HOH C 404 115.296 24.634 44.430 1.00 46.73 O HETATM 4556 O HOH C 405 118.869 23.164 21.198 1.00 28.79 O HETATM 4557 O HOH C 406 112.755 3.674 43.755 1.00 32.49 O HETATM 4558 O HOH C 407 119.707 7.562 39.846 1.00 37.13 O HETATM 4559 O HOH C 408 107.411 19.455 29.177 1.00 35.01 O HETATM 4560 O HOH C 409 108.453 17.126 28.231 1.00 30.93 O HETATM 4561 O HOH C 410 109.933 28.441 43.660 1.00 45.75 O HETATM 4562 O HOH C 411 114.684 2.983 40.275 1.00 38.22 O HETATM 4563 O HOH C 412 107.583 20.153 26.253 1.00 41.99 O HETATM 4564 O HOH B 301 85.170 -25.008 9.021 1.00 30.94 O HETATM 4565 O HOH B 302 88.144 -4.826 23.154 1.00 28.60 O HETATM 4566 O HOH B 303 76.766 -14.254 14.367 1.00 24.97 O HETATM 4567 O HOH B 304 91.449 -31.285 19.457 1.00 20.38 O HETATM 4568 O HOH B 305 107.907 3.841 24.937 1.00 18.41 O HETATM 4569 O HOH B 306 86.564 -18.490 22.823 1.00 27.88 O HETATM 4570 O HOH B 307 104.010 -21.846 31.529 1.00 35.09 O HETATM 4571 O HOH B 308 113.309 3.022 17.984 1.00 40.54 O HETATM 4572 O HOH B 309 100.366 -12.051 20.209 1.00 18.82 O HETATM 4573 O HOH B 310 99.001 5.703 18.242 1.00 31.55 O HETATM 4574 O HOH B 311 70.126 -0.028 -3.766 1.00 38.08 O HETATM 4575 O HOH B 312 79.608 -26.632 23.377 1.00 21.20 O HETATM 4576 O HOH B 313 111.491 -10.046 26.694 1.00 26.17 O HETATM 4577 O HOH B 314 78.789 -26.114 14.163 1.00 23.38 O HETATM 4578 O HOH B 315 116.564 -2.891 27.446 1.00 38.47 O HETATM 4579 O HOH B 316 96.195 -15.876 7.868 1.00 45.01 O HETATM 4580 O HOH B 317 109.160 -7.686 36.463 1.00 22.26 O HETATM 4581 O HOH B 318 77.065 -1.186 -1.493 1.00 26.43 O HETATM 4582 O HOH B 319 111.434 7.148 29.944 1.00 20.32 O HETATM 4583 O HOH B 320 83.874 -6.407 7.323 1.00 31.69 O HETATM 4584 O HOH B 321 68.347 -14.996 -1.467 1.00 28.54 O HETATM 4585 O HOH B 322 85.289 -8.753 -7.598 1.00 39.12 O HETATM 4586 O HOH B 323 107.131 -19.047 28.805 1.00 37.71 O HETATM 4587 O HOH B 324 94.472 7.872 21.871 1.00 14.86 O HETATM 4588 O AHOH B 325 101.446 -0.841 41.380 0.50 21.19 O HETATM 4589 O BHOH B 325 99.035 -0.897 41.839 0.50 17.45 O HETATM 4590 O HOH B 326 113.334 5.015 35.838 1.00 28.15 O HETATM 4591 O HOH B 327 74.108 -1.058 -11.216 1.00 34.37 O HETATM 4592 O HOH B 328 117.701 1.252 28.451 1.00 46.70 O HETATM 4593 O HOH B 329 87.695 -6.630 31.316 1.00 23.14 O HETATM 4594 O HOH B 330 101.018 13.001 23.916 1.00 32.98 O HETATM 4595 O HOH B 331 99.236 15.500 32.598 1.00 14.14 O HETATM 4596 O HOH B 332 92.251 -8.358 18.317 1.00 35.80 O HETATM 4597 O HOH B 333 105.377 8.419 29.479 1.00 13.56 O HETATM 4598 O HOH B 334 94.660 2.507 18.337 1.00 29.79 O HETATM 4599 O HOH B 335 103.012 -16.523 20.796 1.00 39.75 O HETATM 4600 O HOH B 336 102.149 -21.445 33.186 1.00 30.92 O HETATM 4601 O HOH B 337 87.788 -2.076 35.358 1.00 32.25 O HETATM 4602 O HOH B 338 87.985 -18.686 27.170 1.00 32.51 O HETATM 4603 O AHOH B 339 75.582 -13.677 11.696 0.50 13.71 O HETATM 4604 O BHOH B 339 75.483 -13.411 12.181 0.50 25.74 O HETATM 4605 O HOH B 340 108.921 7.677 30.874 1.00 19.62 O HETATM 4606 O HOH B 341 107.846 -10.063 29.144 1.00 19.25 O HETATM 4607 O HOH B 342 93.672 -31.660 17.150 1.00 34.28 O HETATM 4608 O HOH B 343 68.466 -14.476 -8.969 1.00 42.20 O HETATM 4609 O HOH B 344 97.697 -17.375 16.020 1.00 35.45 O HETATM 4610 O HOH B 345 88.891 -0.617 2.103 1.00 45.51 O HETATM 4611 O HOH B 346 109.424 -8.399 18.584 1.00 33.06 O HETATM 4612 O HOH B 347 94.417 -11.903 32.583 1.00 18.22 O HETATM 4613 O HOH B 348 91.968 -9.024 37.832 1.00 40.01 O HETATM 4614 O AHOH B 349 86.877 -23.222 23.956 0.50 14.92 O HETATM 4615 O BHOH B 349 87.197 -23.161 25.562 0.50 24.03 O HETATM 4616 O HOH B 350 88.142 -12.918 30.742 1.00 31.93 O HETATM 4617 O HOH B 351 83.299 -11.361 29.640 1.00 46.01 O HETATM 4618 O HOH B 352 114.454 1.212 20.002 1.00 34.06 O HETATM 4619 O HOH B 353 94.168 -25.439 22.244 1.00 15.34 O HETATM 4620 O HOH B 354 79.446 -12.256 -8.119 1.00 31.89 O HETATM 4621 O HOH B 355 90.018 -3.515 19.563 1.00 31.79 O HETATM 4622 O HOH B 356 85.923 2.554 0.278 1.00 38.69 O HETATM 4623 O HOH B 357 84.850 -24.083 22.239 1.00 20.81 O HETATM 4624 O HOH B 358 117.905 5.427 25.398 1.00 32.68 O HETATM 4625 O HOH B 359 78.066 -2.863 10.449 1.00 26.65 O HETATM 4626 O HOH B 360 99.226 -14.452 15.775 1.00 34.30 O HETATM 4627 O HOH B 361 81.459 -22.821 -0.164 1.00 36.58 O HETATM 4628 O HOH B 362 108.694 11.417 23.487 1.00 20.79 O HETATM 4629 O HOH B 363 91.423 -9.767 35.247 1.00 24.73 O HETATM 4630 O HOH B 364 82.907 -29.363 17.337 1.00 18.50 O HETATM 4631 O HOH B 365 104.845 0.606 15.427 1.00 26.31 O HETATM 4632 O HOH B 366 87.740 -5.856 6.210 1.00 44.64 O HETATM 4633 O HOH B 367 85.980 1.729 -3.703 1.00 34.00 O HETATM 4634 O HOH B 368 82.874 -11.442 16.384 1.00 27.62 O HETATM 4635 O HOH B 369 91.502 -2.110 17.444 1.00 26.41 O HETATM 4636 O HOH B 370 102.200 -19.813 23.890 1.00 31.32 O HETATM 4637 O HOH B 371 76.844 -10.360 -9.201 1.00 28.94 O HETATM 4638 O HOH B 372 78.297 -2.706 -6.111 1.00 35.46 O HETATM 4639 O HOH B 373 79.794 -6.301 14.184 1.00 33.75 O HETATM 4640 O HOH B 374 77.902 -27.089 10.912 1.00 30.81 O HETATM 4641 O HOH B 375 92.018 -3.089 38.775 1.00 27.06 O HETATM 4642 O HOH B 376 92.202 -15.776 19.992 1.00 18.33 O HETATM 4643 O HOH B 377 96.429 -8.448 17.230 1.00 16.73 O HETATM 4644 O HOH B 378 93.228 -14.583 35.654 1.00 29.82 O HETATM 4645 O HOH B 379 97.059 10.449 35.729 1.00 14.35 O HETATM 4646 O HOH B 380 105.286 10.938 15.372 1.00 35.27 O HETATM 4647 O HOH B 381 80.816 -12.005 19.438 1.00 39.26 O HETATM 4648 O HOH B 382 72.977 -0.137 -0.094 1.00 33.93 O HETATM 4649 O HOH B 383 73.661 -2.431 4.033 1.00 21.62 O HETATM 4650 O HOH B 384 102.257 -22.477 35.992 1.00 32.80 O HETATM 4651 O HOH B 385 75.958 -26.127 13.139 1.00 34.34 O HETATM 4652 O HOH B 386 95.261 -23.292 34.037 1.00 33.17 O HETATM 4653 O HOH B 387 88.600 -10.042 -4.278 1.00 27.31 O HETATM 4654 O HOH B 388 85.559 -4.557 2.363 1.00 24.68 O HETATM 4655 O HOH B 389 99.899 -16.806 37.695 1.00 35.98 O HETATM 4656 O HOH B 390 64.913 -4.920 -8.304 1.00 43.18 O HETATM 4657 O HOH B 391 88.220 -9.219 13.366 1.00 35.59 O HETATM 4658 O HOH B 392 89.305 -26.272 27.077 1.00 18.77 O HETATM 4659 O HOH B 393 85.989 -11.946 14.615 1.00 25.05 O HETATM 4660 O HOH B 394 90.503 -28.494 14.586 1.00 45.20 O HETATM 4661 O HOH B 395 94.243 -27.689 14.296 1.00 28.84 O HETATM 4662 O HOH B 396 63.628 -4.921 -5.879 1.00 35.97 O HETATM 4663 O HOH B 397 93.104 -17.318 36.545 1.00 37.15 O HETATM 4664 O HOH B 398 92.271 -13.808 12.431 1.00 24.86 O HETATM 4665 O HOH B 399 91.641 -5.858 19.037 1.00 29.27 O HETATM 4666 O HOH B 400 106.300 11.549 22.082 1.00 26.23 O HETATM 4667 O HOH B 401 110.289 3.976 18.886 1.00 30.98 O HETATM 4668 O HOH B 402 98.176 -0.269 15.654 1.00 31.54 O HETATM 4669 O HOH B 403 76.001 -11.671 -6.631 1.00 33.44 O HETATM 4670 O HOH B 404 75.525 -20.696 12.826 1.00 21.39 O HETATM 4671 O HOH B 405 100.182 17.983 28.979 1.00 35.94 O HETATM 4672 O HOH B 406 106.076 -4.358 28.591 1.00 16.26 O HETATM 4673 O HOH B 407 107.628 -6.256 17.672 1.00 33.73 O HETATM 4674 O AHOH B 408 82.557 -16.501 23.318 0.50 21.67 O HETATM 4675 O BHOH B 408 82.397 -17.270 25.192 0.50 33.47 O HETATM 4676 O HOH B 409 82.155 -28.185 10.451 1.00 43.52 O HETATM 4677 O HOH B 410 98.664 2.883 17.682 1.00 25.59 O HETATM 4678 O HOH B 411 102.022 -11.510 15.159 1.00 32.84 O HETATM 4679 O HOH B 412 92.988 -30.489 21.548 1.00 18.54 O HETATM 4680 O HOH B 413 88.455 -10.628 18.877 1.00 33.76 O HETATM 4681 O HOH B 414 99.618 -20.076 20.043 1.00 41.10 O HETATM 4682 O HOH B 415 95.174 -28.508 19.820 1.00 30.59 O HETATM 4683 O HOH B 416 76.169 -26.206 16.834 1.00 24.27 O HETATM 4684 O HOH B 417 96.145 11.188 22.109 1.00 26.03 O HETATM 4685 O HOH B 418 104.554 -13.909 33.602 1.00 18.86 O HETATM 4686 O HOH B 419 105.709 -11.146 19.101 1.00 31.83 O HETATM 4687 O HOH B 420 80.453 -25.883 8.151 1.00 25.74 O HETATM 4688 O HOH B 421 83.445 -4.011 26.201 1.00 31.27 O HETATM 4689 O HOH B 422 80.511 -4.243 9.621 1.00 33.42 O HETATM 4690 O HOH B 423 87.858 -17.124 20.750 1.00 18.70 O HETATM 4691 O HOH B 424 82.805 -1.602 5.246 1.00 32.98 O HETATM 4692 O HOH B 425 81.250 -2.306 7.669 1.00 38.36 O HETATM 4693 O HOH B 426 82.502 -9.684 13.790 1.00 30.09 O HETATM 4694 O HOH B 427 104.619 -6.310 17.516 1.00 25.60 O HETATM 4695 O HOH B 428 75.666 -18.241 11.797 1.00 26.88 O HETATM 4696 O HOH B 429 87.637 -26.395 8.808 1.00 46.57 O HETATM 4697 O HOH B 430 65.936 -14.951 -8.050 1.00 45.10 O HETATM 4698 O HOH B 431 83.788 -3.418 -5.860 1.00 29.85 O HETATM 4699 O HOH B 432 101.914 14.894 26.039 1.00 39.40 O HETATM 4700 O HOH B 433 78.615 -9.909 -13.400 1.00 49.98 O HETATM 4701 O HOH B 434 89.881 -10.477 5.335 1.00 27.63 O HETATM 4702 O HOH B 435 87.641 -22.919 32.045 1.00 49.76 O HETATM 4703 O HOH B 436 84.584 -6.006 24.732 1.00 34.69 O HETATM 4704 O HOH B 437 103.871 -22.160 27.697 1.00 22.57 O HETATM 4705 O HOH B 438 77.620 -0.248 6.229 1.00 34.80 O HETATM 4706 O HOH B 439 77.332 -12.533 19.530 1.00 27.33 O HETATM 4707 O HOH B 440 102.022 -5.104 42.518 1.00 37.66 O HETATM 4708 O HOH B 441 82.023 0.820 -1.423 1.00 29.27 O HETATM 4709 O HOH B 442 104.341 12.877 23.370 1.00 34.20 O HETATM 4710 O HOH B 443 95.377 -25.719 17.895 1.00 20.97 O HETATM 4711 O HOH B 444 86.773 -17.949 33.661 1.00 47.70 O HETATM 4712 O HOH B 445 107.748 5.900 35.425 1.00 16.96 O HETATM 4713 O HOH B 446 95.922 -18.150 37.241 1.00 28.71 O HETATM 4714 O HOH B 447 83.052 -0.945 -5.063 1.00 46.60 O HETATM 4715 O HOH B 448 94.220 -20.599 2.933 1.00 33.45 O HETATM 4716 O HOH B 449 86.440 -16.816 29.059 1.00 40.11 O HETATM 4717 O HOH B 450 104.326 -16.515 23.136 1.00 25.61 O HETATM 4718 O HOH B 451 88.432 -27.856 16.781 1.00 23.08 O HETATM 4719 O HOH B 452 74.366 -23.505 18.293 1.00 24.56 O HETATM 4720 O AHOH B 453 77.944 -16.320 21.416 0.50 19.48 O HETATM 4721 O BHOH B 453 80.620 -14.955 22.046 0.50 33.61 O HETATM 4722 O HOH B 454 86.939 -12.321 26.796 1.00 26.67 O HETATM 4723 O HOH B 455 118.015 -5.043 21.874 1.00 34.94 O HETATM 4724 O HOH B 456 90.664 -22.542 32.393 1.00 28.77 O HETATM 4725 O HOH B 457 99.456 -8.158 14.142 1.00 40.70 O HETATM 4726 O HOH B 458 99.478 -23.791 24.181 1.00 22.26 O HETATM 4727 O HOH B 459 91.262 -25.959 9.770 1.00 32.37 O HETATM 4728 O HOH B 460 68.775 -1.565 -8.974 1.00 40.18 O HETATM 4729 O HOH B 461 85.314 -22.596 2.465 1.00 34.15 O HETATM 4730 O HOH B 462 105.029 -9.634 38.263 1.00 35.09 O HETATM 4731 O HOH B 463 94.270 -10.172 17.702 1.00 18.35 O HETATM 4732 O HOH B 464 77.907 -13.235 -10.138 1.00 48.11 O HETATM 4733 O HOH B 465 110.036 -13.963 28.450 1.00 41.49 O HETATM 4734 O HOH B 466 110.846 11.373 21.025 1.00 29.30 O HETATM 4735 O HOH B 467 95.387 5.824 20.248 1.00 18.60 O HETATM 4736 O HOH B 468 74.941 -19.672 3.381 1.00 20.15 O HETATM 4737 O HOH B 469 77.435 -18.253 -4.991 1.00 34.13 O HETATM 4738 O HOH B 470 72.946 -28.518 18.285 1.00 35.76 O HETATM 4739 O HOH B 471 61.785 -5.516 3.015 1.00 22.87 O HETATM 4740 O HOH B 472 85.835 -8.122 9.571 1.00 29.04 O HETATM 4741 O HOH B 473 104.779 -3.197 41.178 1.00 22.76 O HETATM 4742 O HOH B 474 87.239 -7.315 24.466 1.00 26.29 O HETATM 4743 O HOH B 475 84.612 -18.833 -5.380 1.00 35.23 O HETATM 4744 O HOH B 476 110.023 5.367 15.039 1.00 31.57 O HETATM 4745 O HOH B 477 96.275 -7.459 14.693 1.00 32.84 O HETATM 4746 O HOH B 478 83.368 -6.967 -11.430 1.00 42.67 O HETATM 4747 O HOH B 479 89.014 -14.328 23.877 1.00 31.54 O HETATM 4748 O HOH B 480 94.499 -4.374 43.037 1.00 40.11 O HETATM 4749 O HOH B 481 106.092 14.119 26.547 1.00 27.60 O HETATM 4750 O HOH B 482 117.085 -3.972 25.038 1.00 28.86 O HETATM 4751 O HOH B 483 114.956 5.297 22.379 1.00 26.20 O HETATM 4752 O HOH B 484 97.349 -19.354 17.870 1.00 27.30 O HETATM 4753 O HOH B 485 113.339 -5.918 29.745 1.00 21.90 O HETATM 4754 O HOH B 486 113.971 5.154 19.462 1.00 31.36 O HETATM 4755 O HOH B 487 70.597 -0.510 1.420 1.00 47.58 O HETATM 4756 O HOH B 488 108.801 3.131 36.571 1.00 26.49 O HETATM 4757 O HOH B 489 92.058 -9.727 -0.871 1.00 43.03 O HETATM 4758 O HOH B 490 88.910 -21.171 34.851 1.00 49.17 O HETATM 4759 O HOH B 491 89.924 -19.397 -1.689 1.00 31.69 O HETATM 4760 O HOH B 492 91.553 -12.433 35.719 1.00 37.32 O HETATM 4761 O HOH B 493 79.841 -23.926 23.180 1.00 26.88 O HETATM 4762 O HOH B 494 97.185 -21.912 17.067 1.00 62.27 O HETATM 4763 O HOH B 495 108.397 -14.182 32.134 1.00 34.23 O HETATM 4764 O HOH B 496 106.314 -11.938 21.636 1.00 34.92 O HETATM 4765 O HOH B 497 76.001 -16.085 12.929 1.00 36.17 O HETATM 4766 O HOH B 498 86.676 -9.714 23.101 1.00 41.62 O HETATM 4767 O HOH B 499 95.920 -31.040 21.379 1.00 37.16 O HETATM 4768 O HOH B 500 88.190 -9.542 33.957 1.00 48.95 O HETATM 4769 O HOH B 501 72.636 -0.191 -2.782 1.00 39.26 O HETATM 4770 O HOH B 502 74.791 -24.353 15.134 1.00 33.10 O HETATM 4771 O HOH B 503 88.815 -12.097 34.669 1.00 49.60 O HETATM 4772 O HOH B 504 100.403 -20.205 17.450 1.00 59.85 O HETATM 4773 O HOH B 505 117.814 4.121 37.571 1.00 36.70 O HETATM 4774 O HOH B 506 115.102 3.908 37.754 1.00 29.59 O HETATM 4775 O HOH B 507 91.977 -22.136 2.058 1.00 40.02 O HETATM 4776 O HOH B 508 81.317 -11.126 34.650 1.00 54.12 O HETATM 4777 O HOH B 509 82.597 -27.217 3.738 1.00 42.18 O HETATM 4778 O HOH B 510 115.735 -4.781 29.093 1.00 27.10 O HETATM 4779 O HOH B 511 94.646 -6.699 44.454 1.00 36.44 O HETATM 4780 O HOH B 512 96.199 -27.556 16.096 1.00 36.54 O HETATM 4781 O HOH B 513 87.989 -11.855 24.353 1.00 31.22 O HETATM 4782 O HOH B 514 118.784 3.534 27.569 1.00 39.22 O HETATM 4783 O HOH B 515 98.608 -15.087 39.422 1.00 40.84 O HETATM 4784 O HOH B 516 86.814 -25.759 26.125 1.00 32.88 O HETATM 4785 O HOH B 517 110.624 8.870 15.103 1.00 43.27 O HETATM 4786 O HOH B 518 87.603 -8.536 -6.316 1.00 39.58 O HETATM 4787 O HOH B 519 107.775 -16.610 26.412 1.00 36.89 O HETATM 4788 O HOH B 520 96.249 -25.111 20.477 1.00 24.43 O HETATM 4789 O HOH B 521 84.240 -4.427 5.005 1.00 39.86 O HETATM 4790 O HOH B 522 87.166 -16.842 24.855 1.00 34.34 O HETATM 4791 O HOH B 523 102.543 -25.809 29.789 1.00 39.65 O HETATM 4792 O HOH B 524 90.031 -20.185 37.122 1.00 48.84 O HETATM 4793 O HOH B 525 77.446 -26.366 25.007 1.00 34.33 O HETATM 4794 O HOH B 526 104.116 -13.143 18.214 1.00 34.35 O HETATM 4795 O HOH B 527 108.379 -10.898 18.518 1.00 41.62 O HETATM 4796 O HOH B 528 86.867 -20.569 24.474 1.00 31.32 O HETATM 4797 O HOH B 529 71.302 -24.769 24.268 1.00 30.83 O HETATM 4798 O HOH B 530 109.241 -12.191 30.353 1.00 26.19 O HETATM 4799 O HOH B 531 106.952 -15.879 22.241 1.00 35.12 O HETATM 4800 O HOH B 532 111.055 4.599 37.221 1.00 29.78 O HETATM 4801 O HOH B 533 96.551 6.705 17.979 1.00 31.67 O HETATM 4802 O HOH B 534 91.060 -9.167 13.606 1.00 35.82 O HETATM 4803 O HOH B 535 113.636 -6.720 32.433 1.00 38.81 O HETATM 4804 O HOH B 536 104.564 -6.089 41.878 1.00 38.63 O HETATM 4805 O HOH B 537 98.940 -25.050 21.552 1.00 35.12 O HETATM 4806 O HOH B 538 82.634 -23.763 24.130 1.00 26.01 O HETATM 4807 O HOH B 539 77.906 -0.827 -4.068 1.00 33.55 O HETATM 4808 O HOH B 540 99.099 -13.958 13.145 1.00 37.89 O HETATM 4809 O HOH B 541 103.684 13.156 17.001 1.00 45.07 O HETATM 4810 O HOH B 542 100.878 -25.970 25.465 1.00 30.44 O HETATM 4811 O HOH B 543 80.238 0.532 -3.815 1.00 37.43 O HETATM 4812 O HOH B 544 111.478 -11.829 31.980 1.00 32.19 O HETATM 4813 O AHOH B 545 82.757 -21.815 26.034 0.50 25.12 O HETATM 4814 O BHOH B 545 83.900 -19.866 25.900 0.50 28.33 O CONECT 208 738 CONECT 738 208 CONECT 1103 1600 CONECT 1104 1601 CONECT 1600 1103 CONECT 1601 1104 CONECT 1752 4188 CONECT 1880 2374 CONECT 1881 2375 CONECT 2374 1880 CONECT 2375 1881 CONECT 2687 3280 CONECT 2688 3281 CONECT 3280 2687 CONECT 3281 2688 CONECT 3600 4047 CONECT 4047 3600 CONECT 4188 1752 MASTER 354 0 0 12 58 0 0 6 4498 3 18 42 END
Display Options:
Goto PDB code:
3D presentation of molecule is powered by
3Dmol
, which supports all modern browsers and mobile devices via WebGL.
Hold mouse button:
left to rotate,middle to shift,right to zoom
Related entries of code: 6ddm
Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code
Check Database
Protein Sequence Similarity
No similar entries are found!
Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
6ddr
RCSB PDB
PDBbind
MICA*008
6ddv
RCSB PDB
PDBbind
MICA*008
Entry Information
PDB ID
6ddm
Complex Type
Protein-Protein
PDBbind Subset
general set
Protein Name
Anti-MICA Fab 1D5
Ligand Name
MICA*008
EC.Number
E.C.-.-.-.-
Resolution
1.3(Å)
Affinity (Kd/Ki/IC50)
Kd=0.42nM
Release Year
2018
Protein/NA Sequence
Check fasta file
Primary Reference
(2018) MAbs Vol. : pp. 1-19
Links to External Databases
RCSB PDB
The mother database
PDBsum
Enhanced annotations on PDB entries
Pubchem
Comprehensive collection of chemical and biological data
UniProtKB AC
UniProt accession number (AC):
Q96QC4
Entrez Gene ID
NCBI Entrez Gene ID:
100507436
ASD
Information of known allosteric effects of PDB entries
This site has been visited
times since Nov 2007.
Copyright ©2007-2024 涓婃捣鐩堣禌鎬濅俊鎭鎶鏈夐檺鍏徃 缃戠珯澶囨鍙凤細
娌狪CP澶2021015625鍙-3
娌叕缃戝畨澶囷細
姝ｅ湪鐢宠涓
Technical Support锛堟妧鏈敮鎸侊級:
yingsaisi@foxmail.com
times since Nov 2007. 
娌叕缃戝畨澶囷細姝ｅ湪鐢宠涓