Browse entries in the PDBbind-CN Database
HEADER IMMUNE SYSTEM 10-MAY-18 6DDV TITLE CRYSTAL STRUCTURE ANALYSIS OF THE EPITOPE OF AN ANTI-MICA ANTIBODY COMPND MOL_ID: 1; COMPND 2 MOLECULE: ANTI-MICA FAB FRAGMENT HEAVY CHAIN CLONE 6E1; COMPND 3 CHAIN: B; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: MHC CLASS I CHAIN-RELATED PROTEIN A; COMPND 7 CHAIN: C; COMPND 8 ENGINEERED: YES; COMPND 9 MUTATION: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: ANTI-MICA FAB FRAGMENT LIGHT CHAIN CLONE 6E1; COMPND 12 CHAIN: A; COMPND 13 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; 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 STRAIN: BALB/C; SOURCE 23 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 24 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 25 EXPRESSION_SYSTEM_STRAIN: 64B4; SOURCE 26 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 27 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 6DDV 1 JRNL REVDAT 2 05-DEC-18 6DDV 1 JRNL REVDAT 1 24-OCT-18 6DDV 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. 2.05 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) : 2.05 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 75.9 REMARK 3 NUMBER OF REFLECTIONS : 24785 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) : 0.226 REMARK 3 R VALUE (WORKING SET) : 0.223 REMARK 3 FREE R VALUE : 0.275 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200 REMARK 3 FREE R VALUE TEST SET COUNT : 1353 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) : 2.05 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.10 REMARK 3 REFLECTION IN BIN (WORKING SET) : 476 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 19.96 REMARK 3 BIN R VALUE (WORKING SET) : 0.4220 REMARK 3 BIN FREE R VALUE SET COUNT : 24 REMARK 3 BIN FREE R VALUE : 0.2900 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4026 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 61 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.07 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 2.05000 REMARK 3 B22 (A**2) : -0.02000 REMARK 3 B33 (A**2) : -2.03000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.358 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.256 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.237 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 21.247 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.939 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.902 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4153 ; 0.006 ; 0.019 REMARK 3 BOND LENGTHS OTHERS (A): 3714 ; 0.002 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5667 ; 1.128 ; 1.935 REMARK 3 BOND ANGLES OTHERS (DEGREES): 8581 ; 0.836 ; 3.000 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 534 ; 6.362 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 163 ;33.443 ;24.233 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 624 ;13.314 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;11.608 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 636 ; 0.067 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4740 ; 0.004 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): 950 ; 0.001 ; 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 : B 2 B 214 REMARK 3 ORIGIN FOR THE GROUP (A): 2.3030 12.6573 47.8304 REMARK 3 T TENSOR REMARK 3 T11: 0.1517 T22: 0.0875 REMARK 3 T33: 0.0153 T12: -0.0138 REMARK 3 T13: 0.0102 T23: -0.0068 REMARK 3 L TENSOR REMARK 3 L11: 1.4274 L22: 0.3893 REMARK 3 L33: 1.9069 L12: -0.3779 REMARK 3 L13: 1.2423 L23: -0.2702 REMARK 3 S TENSOR REMARK 3 S11: -0.0721 S12: -0.0530 S13: 0.0602 REMARK 3 S21: -0.0200 S22: 0.0007 S23: -0.0703 REMARK 3 S31: -0.1685 S32: -0.0044 S33: 0.0715 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): -8.8537 13.4335 7.4635 REMARK 3 T TENSOR REMARK 3 T11: 0.2281 T22: 0.0885 REMARK 3 T33: 0.0081 T12: 0.0155 REMARK 3 T13: -0.0212 T23: 0.0002 REMARK 3 L TENSOR REMARK 3 L11: 2.2884 L22: 0.9834 REMARK 3 L33: 2.6518 L12: -0.6133 REMARK 3 L13: 0.0620 L23: 0.5605 REMARK 3 S TENSOR REMARK 3 S11: -0.1455 S12: 0.0436 S13: 0.0852 REMARK 3 S21: -0.0525 S22: 0.0448 S23: -0.0225 REMARK 3 S31: -0.2191 S32: -0.0550 S33: 0.1007 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 : A 1 A 212 REMARK 3 ORIGIN FOR THE GROUP (A): -0.8210 -4.8276 50.2054 REMARK 3 T TENSOR REMARK 3 T11: 0.1395 T22: 0.1230 REMARK 3 T33: 0.0072 T12: 0.0098 REMARK 3 T13: 0.0114 T23: -0.0108 REMARK 3 L TENSOR REMARK 3 L11: 1.0601 L22: 0.5041 REMARK 3 L33: 1.7841 L12: -0.0191 REMARK 3 L13: 0.9086 L23: -0.2478 REMARK 3 S TENSOR REMARK 3 S11: 0.1169 S12: -0.0463 S13: -0.0517 REMARK 3 S21: 0.0689 S22: -0.0632 S23: 0.0282 REMARK 3 S31: 0.2337 S32: 0.0374 S33: -0.0537 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 6DDV 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_1000234449. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-JUN-16 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRL REMARK 200 BEAMLINE : BL12-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97946 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26155 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050 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 (%) : 76.0 REMARK 200 DATA REDUNDANCY : 3.700 REMARK 200 R MERGE (I) : 0.09000 REMARK 200 R SYM (I) : NULL REMARK 200
FOR THE DATA SET : 8.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.09 REMARK 200 COMPLETENESS FOR SHELL (%) : 18.2 REMARK 200 DATA REDUNDANCY IN SHELL : 1.20 REMARK 200 R MERGE FOR SHELL (I) : 0.31600 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200
FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: REFMAC REMARK 200 STARTING MODEL: 4J8R, 1F3D, 1NZ8, 6DDM REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 46.38 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRI-SODIUM CITRATE, 15% REMARK 280 ISOPROPANOL, 15% PEG 4000, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 292K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 33.25250 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 44.86100 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.88800 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 44.86100 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.25250 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.88800 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 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: B, C, A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLN B 1 REMARK 465 SER B 215 REMARK 465 CYS B 216 REMARK 465 ASP B 217 REMARK 465 GLU A 213 REMARK 465 CYS A 214 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 GLN B 5 CG CD OE1 NE2 REMARK 470 LYS B 13 CG CD CE NZ REMARK 470 LYS B 23 CG CD CE NZ REMARK 470 ARG B 105 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 214 CG CD CE NZ REMARK 470 ARG C 213 CG CD NE CZ NH1 NH2 REMARK 470 ASP C 249 CG OD1 OD2 REMARK 470 GLN C 252 CG CD OE1 NE2 REMARK 470 ARG C 274 CG CD NE CZ NH1 NH2 REMARK 470 GLN C 278 CG CD OE1 NE2 REMARK 470 ASN C 289 CG OD1 ND2 REMARK 470 LYS A 45 CG CD CE NZ REMARK 470 ARG A 77 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 126 CG CD CE NZ REMARK 470 ASN A 152 CG OD1 ND2 REMARK 470 LYS A 169 CG CD CE NZ REMARK 470 LYS A 190 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 B 28 96.31 -68.01 REMARK 500 SER B 130 53.30 -116.46 REMARK 500 ASP B 144 63.23 62.15 REMARK 500 HIS C 286 117.78 -162.26 REMARK 500 LYS A 50 59.41 34.36 REMARK 500 VAL A 51 -56.10 76.26 REMARK 500 ASN A 138 71.73 58.76 REMARK 500 ASN A 152 15.22 58.49 REMARK 500 REMARK 500 REMARK: NULL DBREF 6DDV B 1 217 PDB 6DDV 6DDV 1 217 DBREF 6DDV C 204 297 UNP H9CTV0 H9CTV0_HUMAN 204 297 DBREF 6DDV A 1 214 PDB 6DDV 6DDV 1 214 SEQADV 6DDV SER C 273 UNP H9CTV0 CYS 273 ENGINEERED MUTATION SEQRES 1 B 226 GLN GLY GLN MET GLN GLN SER GLY ALA GLU LEU VAL LYS SEQRES 2 B 226 PRO GLY ALA SER VAL LYS LEU SER CYS LYS THR SER GLY SEQRES 3 B 226 PHE THR PHE SER ASP ASN TYR ILE SER TRP LEU LYS GLN SEQRES 4 B 226 LYS PRO GLY GLN SER LEU GLU TRP ILE ALA TRP ILE TYR SEQRES 5 B 226 ALA GLY THR GLY GLY SER SER TYR ASN GLN LYS PHE ARG SEQRES 6 B 226 ASP LYS ALA GLN LEU THR VAL ASP THR SER SER ARG THR SEQRES 7 B 226 ALA TYR MET GLN LEU SER SER LEU THR THR GLU ASP SER SEQRES 8 B 226 ALA ILE TYR TYR CYS ALA ARG HIS ASP TYR TYR GLY THR SEQRES 9 B 226 SER GLY ALA TRP PHE ALA TYR TRP GLY ARG GLY THR LEU SEQRES 10 B 226 VAL THR VAL SER ALA ALA SER THR LYS GLY PRO SER VAL SEQRES 11 B 226 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 B 226 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 B 226 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 B 226 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 B 226 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 B 226 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 B 226 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU SEQRES 18 B 226 PRO LYS SER CYS ASP 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 SER 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 A 219 ASP VAL LEU MET THR GLN THR PRO LEU SER LEU PRO VAL SEQRES 2 A 219 SER LEU GLY ASP GLN ALA SER ILE SER CYS ARG SER SER SEQRES 3 A 219 GLN HIS ILE VAL HIS SER ASN GLU ASN THR TYR LEU GLU SEQRES 4 A 219 TRP TYR LEU GLN LYS PRO GLY GLN SER PRO LYS LEU LEU SEQRES 5 A 219 ILE TYR LYS VAL SER ASN ARG PHE SER GLY VAL PRO ASP SEQRES 6 A 219 ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU SEQRES 7 A 219 LYS ILE SER ARG VAL GLU ALA GLU ASP LEU GLY VAL TYR SEQRES 8 A 219 TYR CYS PHE GLN GLY SER HIS VAL PRO TRP THR PHE GLY SEQRES 9 A 219 GLY GLY THR LYS LEU GLU ILE LYS ARG THR VAL ALA ALA SEQRES 10 A 219 PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU SEQRES 11 A 219 LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN SEQRES 12 A 219 PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP SEQRES 13 A 219 ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR SEQRES 14 A 219 GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER SEQRES 15 A 219 THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS SEQRES 16 A 219 VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER SEQRES 17 A 219 PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS FORMUL 4 HOH *61(H2 O) HELIX 1 AA1 THR B 28 SER B 30 5 3 HELIX 2 AA2 GLN B 61 ARG B 64 5 4 HELIX 3 AA3 THR B 83 SER B 87 5 5 HELIX 4 AA4 SER B 127 LYS B 129 5 3 HELIX 5 AA5 SER B 156 ALA B 158 5 3 HELIX 6 AA6 SER B 187 GLY B 190 5 4 HELIX 7 AA7 LYS B 201 ASN B 204 5 4 HELIX 8 AA8 SER C 247 GLN C 251 5 5 HELIX 9 AA9 GLU C 276 GLN C 278 5 3 HELIX 10 AB1 GLU A 79 LEU A 83 5 5 HELIX 11 AB2 SER A 121 SER A 127 1 7 HELIX 12 AB3 LYS A 183 LYS A 188 1 6 SHEET 1 AA1 4 GLN B 3 GLN B 6 0 SHEET 2 AA1 4 VAL B 18 SER B 25 -1 O LYS B 23 N GLN B 5 SHEET 3 AA1 4 THR B 77 LEU B 82 -1 O MET B 80 N LEU B 20 SHEET 4 AA1 4 ALA B 67 ASP B 72 -1 N ASP B 72 O THR B 77 SHEET 1 AA2 6 GLU B 10 VAL B 12 0 SHEET 2 AA2 6 THR B 107 VAL B 111 1 O THR B 110 N GLU B 10 SHEET 3 AA2 6 ALA B 88 ASP B 96 -1 N ALA B 88 O VAL B 109 SHEET 4 AA2 6 ASN B 32 GLN B 39 -1 N GLN B 39 O ILE B 89 SHEET 5 AA2 6 LEU B 45 TYR B 52 -1 O ILE B 51 N ILE B 34 SHEET 6 AA2 6 SER B 57 TYR B 59 -1 O SER B 58 N TRP B 50 SHEET 1 AA3 4 GLU B 10 VAL B 12 0 SHEET 2 AA3 4 THR B 107 VAL B 111 1 O THR B 110 N GLU B 10 SHEET 3 AA3 4 ALA B 88 ASP B 96 -1 N ALA B 88 O VAL B 109 SHEET 4 AA3 4 TYR B 102 TRP B 103 -1 O TYR B 102 N ARG B 94 SHEET 1 AA4 4 SER B 120 LEU B 124 0 SHEET 2 AA4 4 THR B 135 TYR B 145 -1 O LYS B 143 N SER B 120 SHEET 3 AA4 4 TYR B 176 PRO B 185 -1 O TYR B 176 N TYR B 145 SHEET 4 AA4 4 VAL B 163 THR B 165 -1 N HIS B 164 O VAL B 181 SHEET 1 AA5 4 THR B 131 SER B 132 0 SHEET 2 AA5 4 THR B 135 TYR B 145 -1 O THR B 135 N SER B 132 SHEET 3 AA5 4 TYR B 176 PRO B 185 -1 O TYR B 176 N TYR B 145 SHEET 4 AA5 4 VAL B 169 LEU B 170 -1 N VAL B 169 O SER B 177 SHEET 1 AA6 3 THR B 151 TRP B 154 0 SHEET 2 AA6 3 ILE B 195 HIS B 200 -1 O ASN B 197 N SER B 153 SHEET 3 AA6 3 THR B 205 LYS B 210 -1 O VAL B 207 N VAL B 198 SHEET 1 AA7 4 MET C 208 SER C 217 0 SHEET 2 AA7 4 ASN C 220 PHE C 230 -1 O THR C 222 N SER C 214 SHEET 3 AA7 4 TYR C 264 SER C 273 -1 O THR C 266 N ALA C 227 SHEET 4 AA7 4 GLN C 252 PRO C 258 -1 N GLY C 254 O TRP C 267 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 SER C 291 N MET C 284 SHEET 1 AA9 4 MET A 4 THR A 7 0 SHEET 2 AA9 4 ALA A 19 SER A 25 -1 O ARG A 24 N THR A 5 SHEET 3 AA9 4 ASP A 70 ILE A 75 -1 O ILE A 75 N ALA A 19 SHEET 4 AA9 4 PHE A 62 SER A 67 -1 N SER A 63 O LYS A 74 SHEET 1 AB1 6 SER A 10 VAL A 13 0 SHEET 2 AB1 6 THR A 102 ILE A 106 1 O LYS A 103 N LEU A 11 SHEET 3 AB1 6 GLY A 84 GLN A 90 -1 N GLY A 84 O LEU A 104 SHEET 4 AB1 6 LEU A 33 GLN A 38 -1 N GLN A 38 O VAL A 85 SHEET 5 AB1 6 LYS A 45 TYR A 49 -1 O LYS A 45 N LEU A 37 SHEET 6 AB1 6 ASN A 53 ARG A 54 -1 O ASN A 53 N TYR A 49 SHEET 1 AB2 4 SER A 10 VAL A 13 0 SHEET 2 AB2 4 THR A 102 ILE A 106 1 O LYS A 103 N LEU A 11 SHEET 3 AB2 4 GLY A 84 GLN A 90 -1 N GLY A 84 O LEU A 104 SHEET 4 AB2 4 THR A 97 PHE A 98 -1 O THR A 97 N GLN A 90 SHEET 1 AB3 4 SER A 114 PHE A 118 0 SHEET 2 AB3 4 THR A 129 PHE A 139 -1 O VAL A 133 N PHE A 118 SHEET 3 AB3 4 TYR A 173 SER A 182 -1 O LEU A 179 N VAL A 132 SHEET 4 AB3 4 SER A 159 VAL A 163 -1 N GLN A 160 O THR A 178 SHEET 1 AB4 4 ALA A 153 LEU A 154 0 SHEET 2 AB4 4 LYS A 145 VAL A 150 -1 N VAL A 150 O ALA A 153 SHEET 3 AB4 4 VAL A 191 THR A 197 -1 O GLU A 195 N GLN A 147 SHEET 4 AB4 4 VAL A 205 ASN A 210 -1 O LYS A 207 N CYS A 194 SSBOND 1 CYS B 22 CYS B 92 1555 1555 2.05 SSBOND 2 CYS B 140 CYS B 196 1555 1555 2.04 SSBOND 3 CYS C 225 CYS C 282 1555 1555 2.05 SSBOND 4 CYS A 23 CYS A 88 1555 1555 2.04 SSBOND 5 CYS A 134 CYS A 194 1555 1555 2.03 CISPEP 1 PHE B 146 PRO B 147 0 -6.38 CISPEP 2 GLU B 148 PRO B 149 0 2.48 CISPEP 3 TYR C 231 PRO C 232 0 0.50 CISPEP 4 THR A 7 PRO A 8 0 -4.05 CISPEP 5 VAL A 94 PRO A 95 0 -6.92 CISPEP 6 TYR A 140 PRO A 141 0 6.28 CRYST1 66.505 89.776 89.722 90.00 90.00 90.00 P 21 21 21 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.015036 0.000000 0.000000 0.00000 SCALE2 0.000000 0.011139 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011146 0.00000 ATOM 1 N GLY B 2 6.558 12.426 27.941 1.00 45.59 N ANISOU 1 N GLY B 2 6107 6954 4260 32 462 284 N ATOM 2 CA GLY B 2 6.818 13.780 28.506 1.00 45.80 C ANISOU 2 CA GLY B 2 6142 6923 4339 -125 446 411 C ATOM 3 C GLY B 2 6.963 13.797 30.019 1.00 45.42 C ANISOU 3 C GLY B 2 6123 6736 4399 -175 421 388 C ATOM 4 O GLY B 2 7.419 12.823 30.615 1.00 46.41 O ANISOU 4 O GLY B 2 6216 6878 4538 -109 434 313 O ATOM 5 N GLN B 3 6.587 14.918 30.633 1.00 44.67 N ANISOU 5 N GLN B 3 6091 6505 4377 -283 376 450 N ATOM 6 CA GLN B 3 6.595 15.076 32.092 1.00 43.35 C ANISOU 6 CA GLN B 3 5962 6200 4308 -326 343 426 C ATOM 7 C GLN B 3 5.315 15.770 32.534 1.00 41.69 C ANISOU 7 C GLN B 3 5864 5808 4169 -346 287 404 C ATOM 8 O GLN B 3 4.773 16.600 31.806 1.00 41.76 O ANISOU 8 O GLN B 3 5917 5792 4159 -379 261 457 O ATOM 9 CB GLN B 3 7.820 15.884 32.538 1.00 44.60 C ANISOU 9 CB GLN B 3 6063 6409 4472 -444 331 535 C ATOM 10 CG GLN B 3 9.056 15.037 32.821 1.00 45.44 C ANISOU 10 CG GLN B 3 6062 6658 4544 -411 377 521 C ATOM 11 CD GLN B 3 9.233 14.723 34.298 1.00 45.25 C ANISOU 11 CD GLN B 3 6059 6529 4605 -413 356 464 C ATOM 12 OE1 GLN B 3 8.877 13.641 34.768 1.00 44.90 O ANISOU 12 OE1 GLN B 3 6031 6444 4584 -316 368 356 O ATOM 13 NE2 GLN B 3 9.780 15.678 35.042 1.00 46.03 N ANISOU 13 NE2 GLN B 3 6159 6579 4750 -529 314 540 N ATOM 14 N MET B 4 4.829 15.402 33.716 1.00 39.89 N ANISOU 14 N MET B 4 5678 5467 4013 -318 268 327 N ATOM 15 CA MET B 4 3.646 16.015 34.314 1.00 38.83 C ANISOU 15 CA MET B 4 5635 5184 3937 -319 216 296 C ATOM 16 C MET B 4 3.935 16.238 35.795 1.00 38.19 C ANISOU 16 C MET B 4 5566 5023 3920 -350 185 280 C ATOM 17 O MET B 4 3.690 15.355 36.622 1.00 37.37 O ANISOU 17 O MET B 4 5454 4899 3845 -298 199 207 O ATOM 18 CB MET B 4 2.409 15.123 34.120 1.00 37.88 C ANISOU 18 CB MET B 4 5543 5033 3817 -225 226 204 C ATOM 19 CG MET B 4 1.990 14.934 32.668 1.00 38.10 C ANISOU 19 CG MET B 4 5569 5126 3781 -185 245 208 C ATOM 20 SD MET B 4 0.635 13.759 32.469 1.00 36.91 S ANISOU 20 SD MET B 4 5446 4940 3638 -86 243 102 S ATOM 21 CE MET B 4 -0.749 14.766 32.981 1.00 36.41 C ANISOU 21 CE MET B 4 5461 4755 3618 -100 191 98 C ATOM 22 N GLN B 5 4.474 17.418 36.111 1.00 38.54 N ANISOU 22 N GLN B 5 5633 5023 3986 -439 134 353 N ATOM 23 CA GLN B 5 4.918 17.761 37.469 1.00 38.05 C ANISOU 23 CA GLN B 5 5584 4894 3980 -474 94 343 C ATOM 24 C GLN B 5 3.773 18.364 38.274 1.00 37.64 C ANISOU 24 C GLN B 5 5624 4709 3969 -437 31 285 C ATOM 25 O GLN B 5 3.345 19.489 38.002 1.00 37.90 O ANISOU 25 O GLN B 5 5729 4662 4009 -464 -38 317 O ATOM 26 CB GLN B 5 6.088 18.746 37.421 1.00 38.74 C ANISOU 26 CB GLN B 5 5654 4996 4072 -593 51 452 C ATOM 27 N GLN B 6 3.272 17.608 39.252 1.00 36.76 N ANISOU 27 N GLN B 6 5507 4582 3879 -369 49 201 N ATOM 28 CA GLN B 6 2.241 18.102 40.163 1.00 36.66 C ANISOU 28 CA GLN B 6 5560 4481 3890 -318 -5 141 C ATOM 29 C GLN B 6 2.874 18.790 41.355 1.00 37.33 C ANISOU 29 C GLN B 6 5667 4508 4009 -352 -65 141 C ATOM 30 O GLN B 6 3.961 18.421 41.791 1.00 37.51 O ANISOU 30 O GLN B 6 5637 4571 4045 -396 -44 164 O ATOM 31 CB GLN B 6 1.340 16.966 40.638 1.00 35.47 C ANISOU 31 CB GLN B 6 5380 4362 3733 -237 39 68 C ATOM 32 CG GLN B 6 0.572 16.325 39.496 1.00 34.83 C ANISOU 32 CG GLN B 6 5289 4322 3623 -201 79 59 C ATOM 33 CD GLN B 6 -0.677 15.594 39.936 1.00 34.02 C ANISOU 33 CD GLN B 6 5179 4227 3518 -133 88 -1 C ATOM 34 OE1 GLN B 6 -0.860 14.426 39.606 1.00 33.28 O ANISOU 34 OE1 GLN B 6 5047 4177 3419 -114 126 -17 O ATOM 35 NE2 GLN B 6 -1.550 16.276 40.668 1.00 34.07 N ANISOU 35 NE2 GLN B 6 5223 4197 3526 -94 45 -33 N ATOM 36 N SER B 7 2.176 19.792 41.878 1.00 38.65 N ANISOU 36 N SER B 7 5915 4583 4188 -320 -148 107 N ATOM 37 CA SER B 7 2.640 20.552 43.037 1.00 39.60 C ANISOU 37 CA SER B 7 6076 4632 4338 -334 -228 90 C ATOM 38 C SER B 7 2.630 19.683 44.295 1.00 39.42 C ANISOU 38 C SER B 7 6002 4660 4316 -279 -188 26 C ATOM 39 O SER B 7 1.927 18.662 44.361 1.00 38.60 O ANISOU 39 O SER B 7 5853 4624 4191 -219 -119 -11 O ATOM 40 CB SER B 7 1.783 21.820 43.231 1.00 40.45 C ANISOU 40 CB SER B 7 6293 4628 4449 -284 -341 52 C ATOM 41 OG SER B 7 0.404 21.582 42.971 1.00 40.17 O ANISOU 41 OG SER B 7 6268 4615 4379 -183 -317 -6 O ATOM 42 N GLY B 8 3.423 20.094 45.283 1.00 40.47 N ANISOU 42 N GLY B 8 6146 4759 4473 -308 -240 22 N ATOM 43 CA GLY B 8 3.557 19.361 46.545 1.00 40.15 C ANISOU 43 CA GLY B 8 6059 4767 4431 -264 -211 -29 C ATOM 44 C GLY B 8 2.277 19.356 47.364 1.00 40.34 C ANISOU 44 C GLY B 8 6104 4801 4422 -149 -226 -112 C ATOM 45 O GLY B 8 1.365 20.156 47.117 1.00 41.20 O ANISOU 45 O GLY B 8 6279 4863 4514 -93 -282 -145 O ATOM 46 N ALA B 9 2.218 18.452 48.344 1.00 39.68 N ANISOU 46 N ALA B 9 5960 4792 4324 -110 -180 -143 N ATOM 47 CA ALA B 9 1.046 18.288 49.204 1.00 39.25 C ANISOU 47 CA ALA B 9 5897 4792 4223 -5 -181 -207 C ATOM 48 C ALA B 9 0.609 19.595 49.863 1.00 40.03 C ANISOU 48 C ALA B 9 6076 4834 4301 72 -287 -274 C ATOM 49 O ALA B 9 1.440 20.455 50.170 1.00 40.30 O ANISOU 49 O ALA B 9 6168 4782 4364 39 -368 -277 O ATOM 50 CB ALA B 9 1.325 17.250 50.275 1.00 39.25 C ANISOU 50 CB ALA B 9 5823 4876 4213 3 -133 -211 C ATOM 51 N GLU B 10 -0.701 19.724 50.075 1.00 40.13 N ANISOU 51 N GLU B 10 6091 4898 4258 179 -295 -328 N ATOM 52 CA GLU B 10 -1.309 20.939 50.623 1.00 40.72 C ANISOU 52 CA GLU B 10 6244 4932 4297 289 -402 -410 C ATOM 53 C GLU B 10 -2.026 20.642 51.941 1.00 40.21 C ANISOU 53 C GLU B 10 6125 4997 4157 407 -393 -476 C ATOM 54 O GLU B 10 -2.697 19.617 52.071 1.00 40.49 O ANISOU 54 O GLU B 10 6067 5164 4155 420 -305 -454 O ATOM 55 CB GLU B 10 -2.319 21.522 49.627 1.00 41.46 C ANISOU 55 CB GLU B 10 6388 4992 4374 336 -431 -423 C ATOM 56 CG GLU B 10 -1.742 21.927 48.271 1.00 41.84 C ANISOU 56 CG GLU B 10 6491 4925 4481 229 -447 -353 C ATOM 57 CD GLU B 10 -0.815 23.127 48.339 1.00 43.02 C ANISOU 57 CD GLU B 10 6743 4927 4678 180 -570 -346 C ATOM 58 OE1 GLU B 10 -1.020 23.999 49.203 1.00 43.68 O ANISOU 58 OE1 GLU B 10 6896 4959 4742 270 -679 -424 O ATOM 59 OE2 GLU B 10 0.123 23.205 47.514 1.00 43.76 O ANISOU 59 OE2 GLU B 10 6845 4960 4822 51 -565 -259 O ATOM 60 N LEU B 11 -1.852 21.534 52.914 1.00 39.89 N ANISOU 60 N LEU B 11 6142 4923 4091 488 -492 -552 N ATOM 61 CA LEU B 11 -2.705 21.601 54.094 1.00 39.70 C ANISOU 61 CA LEU B 11 6082 5031 3972 639 -510 -635 C ATOM 62 C LEU B 11 -3.589 22.820 53.903 1.00 39.92 C ANISOU 62 C LEU B 11 6199 5011 3956 774 -618 -724 C ATOM 63 O LEU B 11 -3.082 23.914 53.665 1.00 40.37 O ANISOU 63 O LEU B 11 6379 4902 4059 769 -739 -755 O ATOM 64 CB LEU B 11 -1.868 21.762 55.365 1.00 40.00 C ANISOU 64 CB LEU B 11 6127 5072 4001 659 -557 -674 C ATOM 65 CG LEU B 11 -2.618 21.996 56.686 1.00 40.85 C ANISOU 65 CG LEU B 11 6204 5322 3995 833 -594 -772 C ATOM 66 CD1 LEU B 11 -3.686 20.940 56.930 1.00 40.52 C ANISOU 66 CD1 LEU B 11 6027 5499 3872 874 -479 -737 C ATOM 67 CD2 LEU B 11 -1.640 22.057 57.851 1.00 41.16 C ANISOU 67 CD2 LEU B 11 6250 5355 4034 832 -636 -801 C ATOM 68 N VAL B 12 -4.901 22.639 53.999 1.00 39.62 N ANISOU 68 N VAL B 12 6102 5119 3831 891 -585 -760 N ATOM 69 CA VAL B 12 -5.843 23.746 53.822 1.00 40.64 C ANISOU 69 CA VAL B 12 6309 5225 3907 1044 -687 -854 C ATOM 70 C VAL B 12 -7.009 23.680 54.810 1.00 40.87 C ANISOU 70 C VAL B 12 6255 5475 3800 1230 -679 -935 C ATOM 71 O VAL B 12 -7.503 22.600 55.138 1.00 39.84 O ANISOU 71 O VAL B 12 5984 5535 3617 1213 -564 -881 O ATOM 72 CB VAL B 12 -6.374 23.819 52.372 1.00 40.57 C ANISOU 72 CB VAL B 12 6327 5151 3936 994 -667 -806 C ATOM 73 CG1 VAL B 12 -5.244 24.179 51.413 1.00 40.39 C ANISOU 73 CG1 VAL B 12 6398 4918 4029 837 -703 -736 C ATOM 74 CG2 VAL B 12 -7.036 22.513 51.952 1.00 39.73 C ANISOU 74 CG2 VAL B 12 6084 5203 3810 936 -521 -727 C ATOM 75 N LYS B 13 -7.443 24.853 55.264 1.00 41.76 N ANISOU 75 N LYS B 13 6455 5562 3850 1409 -812 -1062 N ATOM 76 CA LYS B 13 -8.457 24.955 56.305 1.00 42.76 C ANISOU 76 CA LYS B 13 6507 5914 3828 1616 -823 -1157 C ATOM 77 C LYS B 13 -9.849 24.601 55.760 1.00 42.73 C ANISOU 77 C LYS B 13 6405 6082 3749 1683 -752 -1141 C ATOM 78 O LYS B 13 -10.105 24.790 54.570 1.00 42.06 O ANISOU 78 O LYS B 13 6371 5887 3723 1627 -756 -1107 O ATOM 79 CB LYS B 13 -8.462 26.365 56.900 1.00 44.26 C ANISOU 79 CB LYS B 13 6834 6009 3972 1807 -1007 -1314 C ATOM 80 N PRO B 14 -10.747 24.073 56.623 1.00 43.49 N ANISOU 80 N PRO B 14 6352 6462 3709 1795 -688 -1155 N ATOM 81 CA PRO B 14 -12.139 23.843 56.221 1.00 44.11 C ANISOU 81 CA PRO B 14 6327 6733 3699 1876 -637 -1146 C ATOM 82 C PRO B 14 -12.848 25.122 55.759 1.00 45.63 C ANISOU 82 C PRO B 14 6630 6856 3852 2060 -764 -1271 C ATOM 83 O PRO B 14 -12.712 26.162 56.399 1.00 47.11 O ANISOU 83 O PRO B 14 6918 6989 3992 2229 -898 -1405 O ATOM 84 CB PRO B 14 -12.789 23.303 57.498 1.00 44.75 C ANISOU 84 CB PRO B 14 6240 7137 3625 1987 -578 -1155 C ATOM 85 CG PRO B 14 -11.676 22.668 58.248 1.00 43.99 C ANISOU 85 CG PRO B 14 6128 7010 3578 1866 -537 -1097 C ATOM 86 CD PRO B 14 -10.467 23.502 57.955 1.00 43.66 C ANISOU 86 CD PRO B 14 6274 6658 3658 1819 -643 -1151 C ATOM 87 N GLY B 15 -13.572 25.045 54.642 1.00 45.59 N ANISOU 87 N GLY B 15 6614 6840 3868 2029 -735 -1230 N ATOM 88 CA GLY B 15 -14.238 26.214 54.062 1.00 46.73 C ANISOU 88 CA GLY B 15 6870 6900 3985 2190 -858 -1335 C ATOM 89 C GLY B 15 -13.401 26.978 53.046 1.00 46.63 C ANISOU 89 C GLY B 15 7051 6548 4117 2089 -956 -1328 C ATOM 90 O GLY B 15 -13.956 27.666 52.187 1.00 47.44 O ANISOU 90 O GLY B 15 7235 6562 4228 2152 -1027 -1362 O ATOM 91 N ALA B 16 -12.074 26.855 53.133 1.00 46.07 N ANISOU 91 N ALA B 16 7049 6301 4156 1929 -960 -1275 N ATOM 92 CA ALA B 16 -11.152 27.506 52.203 1.00 45.86 C ANISOU 92 CA ALA B 16 7187 5974 4265 1801 -1046 -1239 C ATOM 93 C ALA B 16 -11.089 26.754 50.876 1.00 44.71 C ANISOU 93 C ALA B 16 7001 5783 4203 1609 -933 -1102 C ATOM 94 O ALA B 16 -11.718 25.703 50.706 1.00 43.77 O ANISOU 94 O ALA B 16 6738 5846 4048 1568 -798 -1039 O ATOM 95 CB ALA B 16 -9.759 27.600 52.822 1.00 45.65 C ANISOU 95 CB ALA B 16 7224 5808 4313 1699 -1087 -1225 C ATOM 96 N SER B 17 -10.326 27.314 49.940 1.00 44.79 N ANISOU 96 N SER B 17 7142 5555 4322 1491 -1000 -1055 N ATOM 97 CA SER B 17 -10.098 26.708 48.634 1.00 43.75 C ANISOU 97 CA SER B 17 6989 5366 4269 1312 -908 -930 C ATOM 98 C SER B 17 -8.603 26.515 48.394 1.00 43.13 C ANISOU 98 C SER B 17 6951 5135 4299 1113 -894 -838 C ATOM 99 O SER B 17 -7.766 27.019 49.144 1.00 43.52 O ANISOU 99 O SER B 17 7067 5094 4375 1110 -977 -870 O ATOM 100 CB SER B 17 -10.718 27.576 47.532 1.00 44.40 C ANISOU 100 CB SER B 17 7174 5337 4360 1361 -996 -944 C ATOM 101 OG SER B 17 -10.181 28.881 47.539 1.00 45.80 O ANISOU 101 OG SER B 17 7524 5297 4580 1394 -1173 -991 O ATOM 102 N VAL B 18 -8.284 25.760 47.349 1.00 42.21 N ANISOU 102 N VAL B 18 6790 5008 4241 955 -792 -726 N ATOM 103 CA VAL B 18 -6.901 25.502 46.949 1.00 41.61 C ANISOU 103 CA VAL B 18 6733 4820 4256 769 -765 -629 C ATOM 104 C VAL B 18 -6.853 25.331 45.435 1.00 41.18 C ANISOU 104 C VAL B 18 6690 4712 4246 658 -722 -537 C ATOM 105 O VAL B 18 -7.794 24.797 44.843 1.00 40.75 O ANISOU 105 O VAL B 18 6575 4754 4156 691 -652 -531 O ATOM 106 CB VAL B 18 -6.336 24.247 47.660 1.00 40.95 C ANISOU 106 CB VAL B 18 6526 4856 4175 696 -642 -591 C ATOM 107 CG1 VAL B 18 -7.064 22.973 47.223 1.00 40.05 C ANISOU 107 CG1 VAL B 18 6286 4896 4034 671 -505 -546 C ATOM 108 CG2 VAL B 18 -4.829 24.124 47.445 1.00 40.48 C ANISOU 108 CG2 VAL B 18 6488 4692 4200 532 -634 -510 C ATOM 109 N LYS B 19 -5.771 25.796 44.816 1.00 41.32 N ANISOU 109 N LYS B 19 6779 4585 4334 528 -768 -461 N ATOM 110 CA LYS B 19 -5.594 25.670 43.374 1.00 41.22 C ANISOU 110 CA LYS B 19 6773 4534 4354 419 -728 -365 C ATOM 111 C LYS B 19 -4.419 24.750 43.103 1.00 40.23 C ANISOU 111 C LYS B 19 6570 4444 4272 264 -625 -272 C ATOM 112 O LYS B 19 -3.268 25.115 43.345 1.00 40.76 O ANISOU 112 O LYS B 19 6668 4433 4384 173 -670 -228 O ATOM 113 CB LYS B 19 -5.384 27.034 42.717 1.00 42.70 C ANISOU 113 CB LYS B 19 7103 4546 4575 396 -876 -337 C ATOM 114 CG LYS B 19 -5.490 27.001 41.199 1.00 42.78 C ANISOU 114 CG LYS B 19 7120 4539 4595 315 -842 -246 C ATOM 115 CD LYS B 19 -5.587 28.404 40.628 1.00 44.27 C ANISOU 115 CD LYS B 19 7458 4560 4805 320 -1005 -227 C ATOM 116 CE LYS B 19 -5.378 28.404 39.126 1.00 44.56 C ANISOU 116 CE LYS B 19 7497 4580 4853 205 -973 -107 C ATOM 117 NZ LYS B 19 -5.392 29.790 38.582 1.00 46.30 N ANISOU 117 NZ LYS B 19 7867 4625 5100 190 -1145 -68 N ATOM 118 N LEU B 20 -4.729 23.548 42.616 1.00 39.02 N ANISOU 118 N LEU B 20 6315 4410 4100 242 -495 -245 N ATOM 119 CA LEU B 20 -3.724 22.537 42.289 1.00 38.13 C ANISOU 119 CA LEU B 20 6124 4348 4017 123 -396 -171 C ATOM 120 C LEU B 20 -3.233 22.758 40.860 1.00 37.82 C ANISOU 120 C LEU B 20 6109 4266 3995 27 -390 -81 C ATOM 121 O LEU B 20 -4.003 23.160 39.995 1.00 38.07 O ANISOU 121 O LEU B 20 6181 4277 4007 59 -414 -78 O ATOM 122 CB LEU B 20 -4.311 21.127 42.460 1.00 37.31 C ANISOU 122 CB LEU B 20 5912 4379 3886 152 -283 -191 C ATOM 123 CG LEU B 20 -4.865 20.824 43.863 1.00 37.28 C ANISOU 123 CG LEU B 20 5863 4450 3850 241 -280 -262 C ATOM 124 CD1 LEU B 20 -5.671 19.535 43.875 1.00 36.72 C ANISOU 124 CD1 LEU B 20 5692 4507 3751 259 -190 -262 C ATOM 125 CD2 LEU B 20 -3.740 20.767 44.889 1.00 37.21 C ANISOU 125 CD2 LEU B 20 5845 4423 3869 198 -288 -259 C ATOM 126 N SER B 21 -1.950 22.498 40.630 1.00 37.39 N ANISOU 126 N SER B 21 6021 4215 3969 -87 -358 -7 N ATOM 127 CA SER B 21 -1.324 22.716 39.335 1.00 37.69 C ANISOU 127 CA SER B 21 6064 4244 4011 -185 -350 92 C ATOM 128 C SER B 21 -0.715 21.421 38.799 1.00 36.98 C ANISOU 128 C SER B 21 5868 4274 3907 -232 -227 129 C ATOM 129 O SER B 21 -0.292 20.556 39.571 1.00 35.94 O ANISOU 129 O SER B 21 5673 4198 3785 -227 -173 101 O ATOM 130 CB SER B 21 -0.252 23.794 39.456 1.00 38.67 C ANISOU 130 CB SER B 21 6248 4273 4174 -285 -447 164 C ATOM 131 OG SER B 21 0.633 23.503 40.520 1.00 38.97 O ANISOU 131 OG SER B 21 6247 4323 4238 -317 -439 152 O ATOM 132 N CYS B 22 -0.694 21.304 37.470 1.00 37.29 N ANISOU 132 N CYS B 22 5895 4355 3920 -265 -193 187 N ATOM 133 CA CYS B 22 -0.087 20.173 36.756 1.00 36.82 C ANISOU 133 CA CYS B 22 5744 4411 3835 -294 -93 217 C ATOM 134 C CYS B 22 0.749 20.737 35.597 1.00 37.42 C ANISOU 134 C CYS B 22 5815 4515 3886 -386 -101 329 C ATOM 135 O CYS B 22 0.266 20.871 34.470 1.00 37.28 O ANISOU 135 O CYS B 22 5812 4521 3831 -377 -95 357 O ATOM 136 CB CYS B 22 -1.186 19.209 36.268 1.00 36.24 C ANISOU 136 CB CYS B 22 5645 4392 3733 -210 -37 156 C ATOM 137 SG CYS B 22 -0.626 17.731 35.380 1.00 35.81 S ANISOU 137 SG CYS B 22 5499 4465 3643 -210 62 163 S ATOM 138 N LYS B 23 1.994 21.103 35.905 1.00 38.06 N ANISOU 138 N LYS B 23 5872 4603 3985 -479 -121 399 N ATOM 139 CA LYS B 23 2.924 21.671 34.922 1.00 39.23 C ANISOU 139 CA LYS B 23 5997 4804 4106 -588 -132 529 C ATOM 140 C LYS B 23 3.501 20.545 34.078 1.00 39.24 C ANISOU 140 C LYS B 23 5887 4977 4045 -576 -22 546 C ATOM 141 O LYS B 23 3.981 19.555 34.632 1.00 38.69 O ANISOU 141 O LYS B 23 5750 4971 3978 -543 38 495 O ATOM 142 CB LYS B 23 4.058 22.433 35.615 1.00 39.97 C ANISOU 142 CB LYS B 23 6092 4854 4239 -699 -200 603 C ATOM 143 N THR B 24 3.452 20.700 32.750 1.00 39.73 N ANISOU 143 N THR B 24 5934 5115 4047 -594 -3 614 N ATOM 144 CA THR B 24 3.845 19.635 31.816 1.00 39.53 C ANISOU 144 CA THR B 24 5811 5261 3946 -551 94 612 C ATOM 145 C THR B 24 4.891 20.082 30.789 1.00 40.74 C ANISOU 145 C THR B 24 5894 5556 4030 -645 108 754 C ATOM 146 O THR B 24 5.115 21.279 30.581 1.00 41.63 O ANISOU 146 O THR B 24 6046 5620 4153 -754 35 869 O ATOM 147 CB THR B 24 2.625 19.064 31.047 1.00 39.01 C ANISOU 147 CB THR B 24 5775 5199 3848 -446 122 535 C ATOM 148 OG1 THR B 24 2.231 19.962 29.998 1.00 39.29 O ANISOU 148 OG1 THR B 24 5854 5229 3846 -482 84 614 O ATOM 149 CG2 THR B 24 1.441 18.829 31.981 1.00 38.05 C ANISOU 149 CG2 THR B 24 5722 4949 3789 -371 95 421 C ATOM 150 N SER B 25 5.518 19.093 30.153 1.00 40.75 N ANISOU 150 N SER B 25 5790 5739 3955 -596 193 745 N ATOM 151 CA SER B 25 6.473 19.320 29.067 1.00 41.95 C ANISOU 151 CA SER B 25 5847 6083 4010 -659 226 872 C ATOM 152 C SER B 25 6.684 18.041 28.257 1.00 41.80 C ANISOU 152 C SER B 25 5738 6251 3895 -536 316 804 C ATOM 153 O SER B 25 6.203 16.970 28.638 1.00 40.85 O ANISOU 153 O SER B 25 5634 6091 3798 -419 343 664 O ATOM 154 CB SER B 25 7.817 19.796 29.620 1.00 42.86 C ANISOU 154 CB SER B 25 5889 6258 4137 -782 209 980 C ATOM 155 OG SER B 25 8.423 18.787 30.409 1.00 42.73 O ANISOU 155 OG SER B 25 5808 6294 4133 -720 260 894 O ATOM 156 N GLY B 26 7.407 18.167 27.146 1.00 42.58 N ANISOU 156 N GLY B 26 5742 6555 3882 -562 354 906 N ATOM 157 CA GLY B 26 7.769 17.022 26.308 1.00 42.40 C ANISOU 157 CA GLY B 26 5623 6741 3746 -433 432 844 C ATOM 158 C GLY B 26 6.657 16.430 25.457 1.00 41.48 C ANISOU 158 C GLY B 26 5562 6608 3591 -306 442 743 C ATOM 159 O GLY B 26 6.762 15.280 25.032 1.00 41.18 O ANISOU 159 O GLY B 26 5479 6681 3488 -169 485 640 O ATOM 160 N PHE B 27 5.595 17.200 25.213 1.00 40.87 N ANISOU 160 N PHE B 27 5586 6389 3553 -344 393 766 N ATOM 161 CA PHE B 27 4.511 16.786 24.311 1.00 40.58 C ANISOU 161 CA PHE B 27 5599 6343 3475 -240 396 689 C ATOM 162 C PHE B 27 3.602 17.960 23.937 1.00 40.65 C ANISOU 162 C PHE B 27 5701 6232 3510 -313 337 764 C ATOM 163 O PHE B 27 3.534 18.957 24.659 1.00 40.48 O ANISOU 163 O PHE B 27 5740 6067 3572 -420 278 831 O ATOM 164 CB PHE B 27 3.671 15.646 24.912 1.00 39.21 C ANISOU 164 CB PHE B 27 5482 6048 3367 -120 392 513 C ATOM 165 CG PHE B 27 2.879 16.040 26.126 1.00 38.13 C ANISOU 165 CG PHE B 27 5441 5686 3362 -165 340 477 C ATOM 166 CD1 PHE B 27 1.595 16.567 25.998 1.00 37.68 C ANISOU 166 CD1 PHE B 27 5478 5496 3343 -163 294 460 C ATOM 167 CD2 PHE B 27 3.408 15.868 27.401 1.00 37.59 C ANISOU 167 CD2 PHE B 27 5362 5554 3368 -197 336 456 C ATOM 168 CE1 PHE B 27 0.864 16.931 27.118 1.00 36.88 C ANISOU 168 CE1 PHE B 27 5452 5216 3345 -186 246 421 C ATOM 169 CE2 PHE B 27 2.681 16.229 28.524 1.00 36.73 C ANISOU 169 CE2 PHE B 27 5332 5261 3364 -225 289 420 C ATOM 170 CZ PHE B 27 1.407 16.761 28.385 1.00 36.43 C ANISOU 170 CZ PHE B 27 5382 5106 3356 -215 245 401 C ATOM 171 N THR B 28 2.894 17.816 22.817 1.00 40.93 N ANISOU 171 N THR B 28 5756 6322 3475 -243 345 744 N ATOM 172 CA THR B 28 1.975 18.845 22.332 1.00 41.02 C ANISOU 172 CA THR B 28 5855 6230 3499 -291 287 807 C ATOM 173 C THR B 28 0.782 18.964 23.280 1.00 39.87 C ANISOU 173 C THR B 28 5824 5848 3476 -268 231 709 C ATOM 174 O THR B 28 -0.184 18.203 23.199 1.00 39.05 O ANISOU 174 O THR B 28 5755 5700 3384 -162 236 585 O ATOM 175 CB THR B 28 1.489 18.549 20.899 1.00 41.51 C ANISOU 175 CB THR B 28 5903 6421 3449 -207 311 798 C ATOM 176 OG1 THR B 28 2.616 18.250 20.070 1.00 42.59 O ANISOU 176 OG1 THR B 28 5916 6814 3454 -199 373 868 O ATOM 177 CG2 THR B 28 0.717 19.744 20.323 1.00 41.78 C ANISOU 177 CG2 THR B 28 6021 6370 3485 -273 248 893 C ATOM 178 N PHE B 29 0.887 19.929 24.185 1.00 39.97 N ANISOU 178 N PHE B 29 5891 5723 3574 -366 172 767 N ATOM 179 CA PHE B 29 -0.078 20.143 25.263 1.00 39.03 C ANISOU 179 CA PHE B 29 5867 5402 3562 -343 116 680 C ATOM 180 C PHE B 29 -1.511 20.396 24.777 1.00 38.79 C ANISOU 180 C PHE B 29 5919 5286 3533 -277 76 630 C ATOM 181 O PHE B 29 -2.463 19.897 25.382 1.00 37.36 O ANISOU 181 O PHE B 29 5774 5020 3403 -200 70 514 O ATOM 182 CB PHE B 29 0.413 21.309 26.126 1.00 39.62 C ANISOU 182 CB PHE B 29 5988 5361 3706 -459 43 767 C ATOM 183 CG PHE B 29 -0.511 21.683 27.241 1.00 38.98 C ANISOU 183 CG PHE B 29 6003 5090 3720 -425 -24 682 C ATOM 184 CD1 PHE B 29 -0.676 20.848 28.334 1.00 38.17 C ANISOU 184 CD1 PHE B 29 5883 4954 3668 -365 7 567 C ATOM 185 CD2 PHE B 29 -1.194 22.890 27.209 1.00 39.64 C ANISOU 185 CD2 PHE B 29 6192 5037 3833 -450 -123 720 C ATOM 186 CE1 PHE B 29 -1.519 21.207 29.375 1.00 37.81 C ANISOU 186 CE1 PHE B 29 5910 4764 3692 -327 -51 493 C ATOM 187 CE2 PHE B 29 -2.034 23.257 28.240 1.00 39.17 C ANISOU 187 CE2 PHE B 29 6213 4824 3844 -398 -188 633 C ATOM 188 CZ PHE B 29 -2.200 22.415 29.327 1.00 38.37 C ANISOU 188 CZ PHE B 29 6081 4715 3784 -336 -146 520 C ATOM 189 N SER B 30 -1.649 21.146 23.681 1.00 39.75 N ANISOU 189 N SER B 30 6063 5444 3595 -310 49 726 N ATOM 190 CA SER B 30 -2.965 21.513 23.128 1.00 39.87 C ANISOU 190 CA SER B 30 6159 5385 3606 -252 4 692 C ATOM 191 C SER B 30 -3.755 20.361 22.486 1.00 39.20 C ANISOU 191 C SER B 30 6046 5374 3475 -131 55 578 C ATOM 192 O SER B 30 -4.950 20.509 22.219 1.00 39.05 O ANISOU 192 O SER B 30 6086 5287 3463 -72 19 527 O ATOM 193 CB SER B 30 -2.801 22.631 22.096 1.00 41.38 C ANISOU 193 CB SER B 30 6381 5601 3741 -329 -45 841 C ATOM 194 OG SER B 30 -2.085 23.725 22.647 1.00 42.51 O ANISOU 194 OG SER B 30 6559 5659 3932 -454 -116 957 O ATOM 195 N ASP B 31 -3.093 19.232 22.233 1.00 38.98 N ANISOU 195 N ASP B 31 5931 5480 3397 -90 128 536 N ATOM 196 CA ASP B 31 -3.728 18.045 21.650 1.00 38.54 C ANISOU 196 CA ASP B 31 5855 5485 3302 25 159 421 C ATOM 197 C ASP B 31 -4.102 16.974 22.696 1.00 37.19 C ANISOU 197 C ASP B 31 5680 5241 3207 79 166 293 C ATOM 198 O ASP B 31 -4.181 15.791 22.363 1.00 36.94 O ANISOU 198 O ASP B 31 5616 5270 3148 158 189 205 O ATOM 199 CB ASP B 31 -2.781 17.439 20.602 1.00 39.46 C ANISOU 199 CB ASP B 31 5885 5804 3302 57 218 447 C ATOM 200 CG ASP B 31 -2.553 18.352 19.398 1.00 40.80 C ANISOU 200 CG ASP B 31 6048 6080 3376 13 214 578 C ATOM 201 OD1 ASP B 31 -3.311 19.325 19.193 1.00 41.06 O ANISOU 201 OD1 ASP B 31 6155 6015 3429 -25 158 631 O ATOM 202 OD2 ASP B 31 -1.609 18.074 18.630 1.00 41.83 O ANISOU 202 OD2 ASP B 31 6091 6403 3399 22 264 629 O ATOM 203 N ASN B 32 -4.368 17.393 23.938 1.00 36.34 N ANISOU 203 N ASN B 32 5610 5004 3193 39 136 282 N ATOM 204 CA ASN B 32 -4.557 16.475 25.074 1.00 35.32 C ANISOU 204 CA ASN B 32 5467 4819 3134 69 143 189 C ATOM 205 C ASN B 32 -5.761 16.850 25.937 1.00 34.40 C ANISOU 205 C ASN B 32 5405 4577 3088 80 95 145 C ATOM 206 O ASN B 32 -5.931 18.015 26.285 1.00 34.75 O ANISOU 206 O ASN B 32 5499 4548 3156 42 54 194 O ATOM 207 CB ASN B 32 -3.305 16.492 25.958 1.00 35.12 C ANISOU 207 CB ASN B 32 5401 4805 3139 9 168 225 C ATOM 208 CG ASN B 32 -2.222 15.566 25.454 1.00 35.53 C ANISOU 208 CG ASN B 32 5377 4994 3130 36 222 218 C ATOM 209 OD1 ASN B 32 -1.324 15.982 24.727 1.00 36.60 O ANISOU 209 OD1 ASN B 32 5470 5242 3195 2 247 302 O ATOM 210 ND2 ASN B 32 -2.302 14.303 25.836 1.00 35.03 N ANISOU 210 ND2 ASN B 32 5291 4929 3088 100 232 121 N ATOM 211 N TYR B 33 -6.582 15.862 26.291 1.00 33.68 N ANISOU 211 N TYR B 33 5303 4468 3026 133 92 56 N ATOM 212 CA TYR B 33 -7.601 16.045 27.325 1.00 33.26 C ANISOU 212 CA TYR B 33 5271 4333 3031 144 57 16 C ATOM 213 C TYR B 33 -6.937 15.828 28.682 1.00 32.87 C ANISOU 213 C TYR B 33 5198 4253 3038 110 71 9 C ATOM 214 O TYR B 33 -6.420 14.742 28.937 1.00 33.06 O ANISOU 214 O TYR B 33 5178 4309 3073 112 100 -21 O ATOM 215 CB TYR B 33 -8.737 15.028 27.207 1.00 32.66 C ANISOU 215 CB TYR B 33 5179 4266 2962 196 44 -58 C ATOM 216 CG TYR B 33 -9.596 15.077 25.970 1.00 32.83 C ANISOU 216 CG TYR B 33 5222 4317 2935 239 22 -70 C ATOM 217 CD1 TYR B 33 -9.270 14.331 24.840 1.00 33.09 C ANISOU 217 CD1 TYR B 33 5241 4415 2916 268 36 -87 C ATOM 218 CD2 TYR B 33 -10.782 15.799 25.959 1.00 32.87 C ANISOU 218 CD2 TYR B 33 5257 4290 2941 265 -18 -74 C ATOM 219 CE1 TYR B 33 -10.085 14.335 23.716 1.00 33.58 C ANISOU 219 CE1 TYR B 33 5322 4506 2930 312 11 -104 C ATOM 220 CE2 TYR B 33 -11.606 15.818 24.839 1.00 33.36 C ANISOU 220 CE2 TYR B 33 5337 4381 2958 307 -41 -87 C ATOM 221 CZ TYR B 33 -11.255 15.082 23.718 1.00 33.60 C ANISOU 221 CZ TYR B 33 5356 4472 2939 326 -26 -100 C ATOM 222 OH TYR B 33 -12.070 15.097 22.607 1.00 34.03 O ANISOU 222 OH TYR B 33 5428 4557 2946 371 -53 -116 O ATOM 223 N ILE B 34 -6.950 16.846 29.543 1.00 32.74 N ANISOU 223 N ILE B 34 5214 4173 3054 86 42 33 N ATOM 224 CA ILE B 34 -6.438 16.719 30.908 1.00 32.18 C ANISOU 224 CA ILE B 34 5123 4072 3031 61 48 21 C ATOM 225 C ILE B 34 -7.606 16.386 31.838 1.00 31.67 C ANISOU 225 C ILE B 34 5048 3992 2994 106 29 -39 C ATOM 226 O ILE B 34 -8.508 17.206 32.014 1.00 31.39 O ANISOU 226 O ILE B 34 5048 3926 2953 143 -13 -51 O ATOM 227 CB ILE B 34 -5.746 18.015 31.392 1.00 32.67 C ANISOU 227 CB ILE B 34 5229 4073 3110 13 13 76 C ATOM 228 CG1 ILE B 34 -4.594 18.414 30.457 1.00 33.37 C ANISOU 228 CG1 ILE B 34 5315 4198 3166 -51 27 162 C ATOM 229 CG2 ILE B 34 -5.247 17.859 32.826 1.00 32.46 C ANISOU 229 CG2 ILE B 34 5182 4020 3130 -4 15 55 C ATOM 230 CD1 ILE B 34 -3.493 17.381 30.307 1.00 33.26 C ANISOU 230 CD1 ILE B 34 5227 4274 3136 -71 91 168 C ATOM 231 N SER B 35 -7.588 15.179 32.410 1.00 31.32 N ANISOU 231 N SER B 35 4951 3976 2973 105 54 -72 N ATOM 232 CA SER B 35 -8.552 14.774 33.436 1.00 30.97 C ANISOU 232 CA SER B 35 4877 3941 2950 128 39 -108 C ATOM 233 C SER B 35 -7.946 14.937 34.823 1.00 30.73 C ANISOU 233 C SER B 35 4832 3895 2951 108 44 -106 C ATOM 234 O SER B 35 -6.728 14.855 34.986 1.00 30.27 O ANISOU 234 O SER B 35 4772 3823 2908 69 66 -84 O ATOM 235 CB SER B 35 -8.984 13.314 33.261 1.00 30.82 C ANISOU 235 CB SER B 35 4811 3957 2941 125 45 -131 C ATOM 236 OG SER B 35 -9.867 13.152 32.175 1.00 30.95 O ANISOU 236 OG SER B 35 4838 3991 2930 152 26 -145 O ATOM 237 N TRP B 36 -8.813 15.151 35.811 1.00 30.66 N ANISOU 237 N TRP B 36 4805 3903 2941 142 24 -129 N ATOM 238 CA TRP B 36 -8.430 15.142 37.219 1.00 30.67 C ANISOU 238 CA TRP B 36 4781 3910 2962 136 26 -135 C ATOM 239 C TRP B 36 -9.188 14.031 37.938 1.00 30.18 C ANISOU 239 C TRP B 36 4646 3917 2903 135 36 -142 C ATOM 240 O TRP B 36 -10.397 13.880 37.754 1.00 30.42 O ANISOU 240 O TRP B 36 4649 3999 2910 164 20 -150 O ATOM 241 CB TRP B 36 -8.696 16.504 37.862 1.00 31.34 C ANISOU 241 CB TRP B 36 4910 3968 3030 187 -18 -155 C ATOM 242 CG TRP B 36 -7.754 17.566 37.372 1.00 31.76 C ANISOU 242 CG TRP B 36 5036 3937 3093 160 -44 -129 C ATOM 243 CD1 TRP B 36 -7.860 18.286 36.216 1.00 32.20 C ANISOU 243 CD1 TRP B 36 5148 3952 3133 161 -70 -107 C ATOM 244 CD2 TRP B 36 -6.550 18.006 38.010 1.00 31.77 C ANISOU 244 CD2 TRP B 36 5060 3890 3123 117 -54 -110 C ATOM 245 NE1 TRP B 36 -6.800 19.154 36.098 1.00 32.53 N ANISOU 245 NE1 TRP B 36 5244 3924 3192 111 -99 -64 N ATOM 246 CE2 TRP B 36 -5.981 19.003 37.186 1.00 32.33 C ANISOU 246 CE2 TRP B 36 5198 3891 3195 83 -91 -67 C ATOM 247 CE3 TRP B 36 -5.898 17.659 39.201 1.00 31.63 C ANISOU 247 CE3 TRP B 36 5009 3882 3126 100 -41 -119 C ATOM 248 CZ2 TRP B 36 -4.790 19.660 37.517 1.00 32.70 C ANISOU 248 CZ2 TRP B 36 5277 3880 3269 22 -120 -29 C ATOM 249 CZ3 TRP B 36 -4.711 18.311 39.528 1.00 31.87 C ANISOU 249 CZ3 TRP B 36 5074 3853 3182 51 -66 -92 C ATOM 250 CH2 TRP B 36 -4.170 19.300 38.686 1.00 32.47 C ANISOU 250 CH2 TRP B 36 5214 3861 3263 9 -107 -46 C ATOM 251 N LEU B 37 -8.467 13.239 38.729 1.00 29.68 N ANISOU 251 N LEU B 37 4550 3859 2869 95 55 -129 N ATOM 252 CA LEU B 37 -9.057 12.124 39.467 1.00 29.71 C ANISOU 252 CA LEU B 37 4486 3922 2881 73 54 -115 C ATOM 253 C LEU B 37 -8.739 12.210 40.957 1.00 29.91 C ANISOU 253 C LEU B 37 4477 3980 2906 74 61 -110 C ATOM 254 O LEU B 37 -7.689 12.723 41.347 1.00 29.46 O ANISOU 254 O LEU B 37 4452 3880 2863 71 69 -117 O ATOM 255 CB LEU B 37 -8.570 10.796 38.904 1.00 29.70 C ANISOU 255 CB LEU B 37 4478 3891 2915 24 56 -101 C ATOM 256 CG LEU B 37 -8.675 10.691 37.375 1.00 29.72 C ANISOU 256 CG LEU B 37 4519 3864 2910 34 49 -116 C ATOM 257 CD1 LEU B 37 -7.349 11.027 36.704 1.00 29.42 C ANISOU 257 CD1 LEU B 37 4523 3783 2872 35 74 -122 C ATOM 258 CD2 LEU B 37 -9.136 9.308 36.975 1.00 29.98 C ANISOU 258 CD2 LEU B 37 4532 3896 2965 6 16 -113 C ATOM 259 N LYS B 38 -9.669 11.702 41.765 1.00 30.50 N ANISOU 259 N LYS B 38 4482 4145 2960 74 53 -91 N ATOM 260 CA LYS B 38 -9.610 11.758 43.226 1.00 31.05 C ANISOU 260 CA LYS B 38 4505 4282 3011 86 58 -82 C ATOM 261 C LYS B 38 -9.428 10.339 43.767 1.00 31.40 C ANISOU 261 C LYS B 38 4496 4349 3086 11 59 -28 C ATOM 262 O LYS B 38 -10.183 9.436 43.408 1.00 31.83 O ANISOU 262 O LYS B 38 4513 4432 3149 -32 39 9 O ATOM 263 CB LYS B 38 -10.914 12.367 43.773 1.00 31.53 C ANISOU 263 CB LYS B 38 4514 4464 3003 156 44 -95 C ATOM 264 CG LYS B 38 -11.043 12.362 45.289 1.00 31.82 C ANISOU 264 CG LYS B 38 4483 4611 2996 181 49 -84 C ATOM 265 CD LYS B 38 -12.300 13.069 45.773 1.00 32.56 C ANISOU 265 CD LYS B 38 4520 4849 3003 278 36 -109 C ATOM 266 CE LYS B 38 -12.338 13.142 47.296 1.00 33.04 C ANISOU 266 CE LYS B 38 4513 5037 3005 320 41 -106 C ATOM 267 NZ LYS B 38 -13.711 13.381 47.812 1.00 33.86 N ANISOU 267 NZ LYS B 38 4516 5340 3008 400 35 -105 N ATOM 268 N GLN B 39 -8.430 10.158 44.630 1.00 31.67 N ANISOU 268 N GLN B 39 4530 4362 3139 -7 71 -22 N ATOM 269 CA GLN B 39 -8.230 8.901 45.350 1.00 31.92 C ANISOU 269 CA GLN B 39 4516 4417 3197 -72 62 33 C ATOM 270 C GLN B 39 -7.955 9.169 46.832 1.00 32.62 C ANISOU 270 C GLN B 39 4563 4577 3254 -54 74 43 C ATOM 271 O GLN B 39 -6.950 9.795 47.187 1.00 31.95 O ANISOU 271 O GLN B 39 4517 4445 3177 -28 87 7 O ATOM 272 CB GLN B 39 -7.067 8.124 44.736 1.00 31.47 C ANISOU 272 CB GLN B 39 4508 4247 3202 -112 58 29 C ATOM 273 CG GLN B 39 -6.941 6.699 45.247 1.00 31.68 C ANISOU 273 CG GLN B 39 4505 4268 3265 -177 25 84 C ATOM 274 CD GLN B 39 -5.837 5.929 44.561 1.00 31.44 C ANISOU 274 CD GLN B 39 4528 4130 3286 -190 9 64 C ATOM 275 OE1 GLN B 39 -4.748 6.457 44.314 1.00 31.12 O ANISOU 275 OE1 GLN B 39 4525 4050 3250 -158 40 22 O ATOM 276 NE2 GLN B 39 -6.106 4.666 44.257 1.00 31.67 N ANISOU 276 NE2 GLN B 39 4562 4118 3352 -235 -49 93 N ATOM 277 N LYS B 40 -8.859 8.698 47.689 1.00 33.89 N ANISOU 277 N LYS B 40 4638 4863 3375 -70 66 98 N ATOM 278 CA LYS B 40 -8.609 8.642 49.131 1.00 34.94 C ANISOU 278 CA LYS B 40 4719 5082 3473 -64 74 123 C ATOM 279 C LYS B 40 -7.717 7.422 49.394 1.00 35.33 C ANISOU 279 C LYS B 40 4777 5061 3586 -147 60 175 C ATOM 280 O LYS B 40 -8.018 6.339 48.883 1.00 35.06 O ANISOU 280 O LYS B 40 4737 4993 3594 -220 27 228 O ATOM 281 CB LYS B 40 -9.921 8.507 49.899 1.00 35.75 C ANISOU 281 CB LYS B 40 4712 5373 3497 -57 71 179 C ATOM 282 CG LYS B 40 -10.875 9.672 49.692 1.00 36.17 C ANISOU 282 CG LYS B 40 4750 5514 3477 46 77 121 C ATOM 283 CD LYS B 40 -12.147 9.489 50.500 1.00 37.43 C ANISOU 283 CD LYS B 40 4781 5898 3544 60 78 181 C ATOM 284 CE LYS B 40 -12.929 10.785 50.614 1.00 37.94 C ANISOU 284 CE LYS B 40 4828 6072 3515 202 81 102 C ATOM 285 NZ LYS B 40 -14.147 10.621 51.453 1.00 39.04 N ANISOU 285 NZ LYS B 40 4820 6468 3543 232 87 160 N ATOM 286 N PRO B 41 -6.611 7.589 50.162 1.00 36.04 N ANISOU 286 N PRO B 41 4886 5122 3685 -134 73 156 N ATOM 287 CA PRO B 41 -5.690 6.468 50.437 1.00 36.13 C ANISOU 287 CA PRO B 41 4909 5064 3753 -198 55 197 C ATOM 288 C PRO B 41 -6.388 5.187 50.891 1.00 36.52 C ANISOU 288 C PRO B 41 4898 5170 3808 -280 15 299 C ATOM 289 O PRO B 41 -7.243 5.232 51.771 1.00 37.34 O ANISOU 289 O PRO B 41 4919 5420 3849 -287 18 355 O ATOM 290 CB PRO B 41 -4.794 7.019 51.550 1.00 36.20 C ANISOU 290 CB PRO B 41 4917 5098 3741 -160 75 172 C ATOM 291 CG PRO B 41 -4.728 8.484 51.265 1.00 36.04 C ANISOU 291 CG PRO B 41 4936 5068 3692 -82 95 89 C ATOM 292 CD PRO B 41 -6.091 8.854 50.727 1.00 36.36 C ANISOU 292 CD PRO B 41 4952 5175 3690 -55 93 88 C ATOM 293 N GLY B 42 -6.042 4.068 50.258 1.00 36.67 N ANISOU 293 N GLY B 42 4957 5078 3898 -340 -32 325 N ATOM 294 CA GLY B 42 -6.689 2.785 50.521 1.00 37.16 C ANISOU 294 CA GLY B 42 4981 5155 3981 -435 -98 430 C ATOM 295 C GLY B 42 -8.108 2.655 49.990 1.00 37.66 C ANISOU 295 C GLY B 42 5000 5286 4025 -475 -123 476 C ATOM 296 O GLY B 42 -8.843 1.763 50.414 1.00 39.17 O ANISOU 296 O GLY B 42 5133 5532 4217 -566 -178 585 O ATOM 297 N GLN B 43 -8.508 3.533 49.074 1.00 37.02 N ANISOU 297 N GLN B 43 4939 5203 3924 -414 -90 404 N ATOM 298 CA GLN B 43 -9.799 3.417 48.405 1.00 37.59 C ANISOU 298 CA GLN B 43 4974 5326 3981 -445 -116 437 C ATOM 299 C GLN B 43 -9.609 3.490 46.891 1.00 36.54 C ANISOU 299 C GLN B 43 4929 5060 3894 -417 -129 359 C ATOM 300 O GLN B 43 -8.499 3.718 46.402 1.00 35.25 O ANISOU 300 O GLN B 43 4843 4789 3762 -368 -109 284 O ATOM 301 CB GLN B 43 -10.761 4.508 48.886 1.00 38.50 C ANISOU 301 CB GLN B 43 5008 5620 4002 -385 -65 431 C ATOM 302 CG GLN B 43 -11.010 4.486 50.389 1.00 39.85 C ANISOU 302 CG GLN B 43 5079 5958 4105 -396 -49 504 C ATOM 303 CD GLN B 43 -12.219 5.312 50.815 1.00 41.23 C ANISOU 303 CD GLN B 43 5150 6343 4171 -335 -17 512 C ATOM 304 OE1 GLN B 43 -13.147 5.541 50.037 1.00 42.36 O ANISOU 304 OE1 GLN B 43 5274 6523 4298 -325 -24 504 O ATOM 305 NE2 GLN B 43 -12.216 5.755 52.068 1.00 41.97 N ANISOU 305 NE2 GLN B 43 5175 6588 4183 -284 16 523 N ATOM 306 N SER B 44 -10.704 3.286 46.160 1.00 36.43 N ANISOU 306 N SER B 44 4893 5071 3877 -447 -164 383 N ATOM 307 CA SER B 44 -10.711 3.381 44.701 1.00 35.68 C ANISOU 307 CA SER B 44 4872 4875 3811 -416 -179 313 C ATOM 308 C SER B 44 -10.661 4.845 44.243 1.00 34.64 C ANISOU 308 C SER B 44 4761 4771 3631 -314 -105 228 C ATOM 309 O SER B 44 -10.557 5.766 45.067 1.00 34.28 O ANISOU 309 O SER B 44 4684 4806 3536 -263 -53 214 O ATOM 310 CB SER B 44 -11.955 2.686 44.133 1.00 36.46 C ANISOU 310 CB SER B 44 4937 4996 3920 -487 -251 371 C ATOM 311 OG SER B 44 -11.785 2.401 42.760 1.00 36.42 O ANISOU 311 OG SER B 44 5016 4867 3957 -468 -289 308 O ATOM 312 N LEU B 45 -10.729 5.048 42.927 1.00 33.82 N ANISOU 312 N LEU B 45 4714 4596 3539 -283 -112 172 N ATOM 313 CA LEU B 45 -10.677 6.385 42.337 1.00 32.82 C ANISOU 313 CA LEU B 45 4621 4477 3374 -197 -59 102 C ATOM 314 C LEU B 45 -12.033 6.868 41.840 1.00 32.49 C ANISOU 314 C LEU B 45 4541 4514 3288 -177 -66 105 C ATOM 315 O LEU B 45 -12.949 6.073 41.614 1.00 32.22 O ANISOU 315 O LEU B 45 4466 4513 3264 -235 -116 154 O ATOM 316 CB LEU B 45 -9.680 6.423 41.176 1.00 32.33 C ANISOU 316 CB LEU B 45 4646 4296 3342 -167 -53 40 C ATOM 317 CG LEU B 45 -8.252 6.024 41.550 1.00 31.93 C ANISOU 317 CG LEU B 45 4628 4178 3326 -171 -42 28 C ATOM 318 CD1 LEU B 45 -7.943 4.623 41.040 1.00 32.28 C ANISOU 318 CD1 LEU B 45 4704 4142 3420 -205 -106 32 C ATOM 319 CD2 LEU B 45 -7.245 7.025 41.003 1.00 31.53 C ANISOU 319 CD2 LEU B 45 4627 4093 3260 -115 8 -26 C ATOM 320 N GLU B 46 -12.135 8.186 41.682 1.00 32.05 N ANISOU 320 N GLU B 46 4504 4487 3188 -95 -27 54 N ATOM 321 CA GLU B 46 -13.271 8.822 41.026 1.00 32.10 C ANISOU 321 CA GLU B 46 4493 4552 3151 -52 -33 37 C ATOM 322 C GLU B 46 -12.773 9.770 39.955 1.00 31.46 C ANISOU 322 C GLU B 46 4501 4383 3068 10 -16 -29 C ATOM 323 O GLU B 46 -11.704 10.356 40.099 1.00 31.17 O ANISOU 323 O GLU B 46 4518 4284 3042 34 10 -57 O ATOM 324 CB GLU B 46 -14.102 9.618 42.020 1.00 32.55 C ANISOU 324 CB GLU B 46 4477 4756 3136 6 -17 42 C ATOM 325 CG GLU B 46 -14.640 8.817 43.182 1.00 33.21 C ANISOU 325 CG GLU B 46 4452 4968 3199 -52 -27 121 C ATOM 326 CD GLU B 46 -15.592 9.639 44.016 1.00 33.97 C ANISOU 326 CD GLU B 46 4462 5245 3201 28 -11 118 C ATOM 327 OE1 GLU B 46 -16.756 9.812 43.596 1.00 34.70 O ANISOU 327 OE1 GLU B 46 4499 5435 3248 51 -26 126 O ATOM 328 OE2 GLU B 46 -15.177 10.123 45.084 1.00 34.21 O ANISOU 328 OE2 GLU B 46 4477 5327 3195 77 12 102 O ATOM 329 N TRP B 47 -13.554 9.916 38.887 1.00 31.41 N ANISOU 329 N TRP B 47 4508 4379 3048 28 -36 -43 N ATOM 330 CA TRP B 47 -13.271 10.903 37.850 1.00 31.13 C ANISOU 330 CA TRP B 47 4549 4280 2998 86 -25 -91 C ATOM 331 C TRP B 47 -14.015 12.191 38.197 1.00 31.31 C ANISOU 331 C TRP B 47 4563 4370 2965 169 -24 -117 C ATOM 332 O TRP B 47 -15.217 12.168 38.454 1.00 31.79 O ANISOU 332 O TRP B 47 4555 4538 2985 191 -40 -105 O ATOM 333 CB TRP B 47 -13.678 10.377 36.469 1.00 30.97 C ANISOU 333 CB TRP B 47 4554 4226 2988 71 -52 -99 C ATOM 334 CG TRP B 47 -13.686 11.414 35.405 1.00 30.64 C ANISOU 334 CG TRP B 47 4575 4149 2917 131 -46 -134 C ATOM 335 CD1 TRP B 47 -12.607 11.934 34.748 1.00 30.25 C ANISOU 335 CD1 TRP B 47 4596 4024 2872 143 -24 -150 C ATOM 336 CD2 TRP B 47 -14.838 12.064 34.869 1.00 30.83 C ANISOU 336 CD2 TRP B 47 4592 4223 2899 182 -66 -147 C ATOM 337 NE1 TRP B 47 -13.021 12.875 33.835 1.00 30.33 N ANISOU 337 NE1 TRP B 47 4650 4027 2848 192 -33 -165 N ATOM 338 CE2 TRP B 47 -14.387 12.973 33.887 1.00 30.65 C ANISOU 338 CE2 TRP B 47 4648 4136 2860 222 -60 -170 C ATOM 339 CE3 TRP B 47 -16.213 11.967 35.124 1.00 31.25 C ANISOU 339 CE3 TRP B 47 4573 4380 2921 196 -91 -135 C ATOM 340 CZ2 TRP B 47 -15.265 13.785 33.157 1.00 30.93 C ANISOU 340 CZ2 TRP B 47 4705 4192 2855 281 -83 -187 C ATOM 341 CZ3 TRP B 47 -17.091 12.775 34.395 1.00 31.63 C ANISOU 341 CZ3 TRP B 47 4635 4459 2926 262 -109 -160 C ATOM 342 CH2 TRP B 47 -16.609 13.676 33.426 1.00 31.41 C ANISOU 342 CH2 TRP B 47 4698 4348 2887 307 -107 -188 C ATOM 343 N ILE B 48 -13.288 13.304 38.207 1.00 31.25 N ANISOU 343 N ILE B 48 4623 4299 2950 217 -15 -149 N ATOM 344 CA ILE B 48 -13.842 14.607 38.569 1.00 31.89 C ANISOU 344 CA ILE B 48 4721 4415 2982 311 -35 -186 C ATOM 345 C ILE B 48 -14.341 15.312 37.306 1.00 32.35 C ANISOU 345 C ILE B 48 4837 4435 3021 354 -59 -207 C ATOM 346 O ILE B 48 -15.527 15.658 37.185 1.00 32.77 O ANISOU 346 O ILE B 48 4858 4564 3028 418 -83 -225 O ATOM 347 CB ILE B 48 -12.782 15.489 39.280 1.00 31.81 C ANISOU 347 CB ILE B 48 4769 4335 2981 334 -37 -208 C ATOM 348 CG1 ILE B 48 -12.228 14.773 40.524 1.00 31.60 C ANISOU 348 CG1 ILE B 48 4687 4348 2971 292 -12 -188 C ATOM 349 CG2 ILE B 48 -13.362 16.857 39.650 1.00 32.41 C ANISOU 349 CG2 ILE B 48 4880 4428 3006 446 -83 -260 C ATOM 350 CD1 ILE B 48 -10.929 15.348 41.049 1.00 31.46 C ANISOU 350 CD1 ILE B 48 4727 4246 2980 284 -12 -200 C ATOM 351 N ALA B 49 -13.418 15.516 36.369 1.00 32.19 N ANISOU 351 N ALA B 49 4892 4308 3030 321 -54 -200 N ATOM 352 CA ALA B 49 -13.672 16.313 35.176 1.00 32.29 C ANISOU 352 CA ALA B 49 4972 4274 3024 356 -79 -209 C ATOM 353 C ALA B 49 -12.512 16.169 34.199 1.00 32.31 C ANISOU 353 C ALA B 49 5027 4195 3053 296 -59 -181 C ATOM 354 O ALA B 49 -11.417 15.752 34.591 1.00 31.97 O ANISOU 354 O ALA B 49 4980 4125 3041 244 -31 -164 O ATOM 355 CB ALA B 49 -13.842 17.776 35.556 1.00 32.56 C ANISOU 355 CB ALA B 49 5064 4275 3030 437 -126 -239 C ATOM 356 N TRP B 50 -12.763 16.495 32.931 1.00 32.49 N ANISOU 356 N TRP B 50 5092 4198 3054 309 -72 -175 N ATOM 357 CA TRP B 50 -11.682 16.766 31.983 1.00 32.53 C ANISOU 357 CA TRP B 50 5151 4147 3062 269 -60 -141 C ATOM 358 C TRP B 50 -11.857 18.124 31.338 1.00 33.06 C ANISOU 358 C TRP B 50 5294 4164 3103 302 -105 -125 C ATOM 359 O TRP B 50 -12.947 18.690 31.331 1.00 33.62 O ANISOU 359 O TRP B 50 5379 4245 3150 369 -146 -152 O ATOM 360 CB TRP B 50 -11.501 15.672 30.911 1.00 32.09 C ANISOU 360 CB TRP B 50 5073 4119 3000 241 -33 -136 C ATOM 361 CG TRP B 50 -12.686 15.323 30.058 1.00 32.34 C ANISOU 361 CG TRP B 50 5094 4190 3005 276 -54 -158 C ATOM 362 CD1 TRP B 50 -13.437 14.196 30.155 1.00 32.28 C ANISOU 362 CD1 TRP B 50 5031 4225 3009 270 -62 -181 C ATOM 363 CD2 TRP B 50 -13.221 16.063 28.946 1.00 32.70 C ANISOU 363 CD2 TRP B 50 5185 4232 3009 314 -80 -152 C ATOM 364 NE1 TRP B 50 -14.422 14.189 29.199 1.00 32.56 N ANISOU 364 NE1 TRP B 50 5072 4288 3014 302 -91 -194 N ATOM 365 CE2 TRP B 50 -14.312 15.322 28.441 1.00 32.79 C ANISOU 365 CE2 TRP B 50 5161 4291 3007 336 -98 -181 C ATOM 366 CE3 TRP B 50 -12.898 17.283 28.341 1.00 33.11 C ANISOU 366 CE3 TRP B 50 5304 4242 3035 326 -99 -119 C ATOM 367 CZ2 TRP B 50 -15.086 15.762 27.363 1.00 33.13 C ANISOU 367 CZ2 TRP B 50 5232 4348 3009 378 -126 -185 C ATOM 368 CZ3 TRP B 50 -13.665 17.718 27.260 1.00 33.62 C ANISOU 368 CZ3 TRP B 50 5400 4316 3058 366 -128 -117 C ATOM 369 CH2 TRP B 50 -14.748 16.958 26.785 1.00 33.55 C ANISOU 369 CH2 TRP B 50 5353 4363 3034 397 -138 -155 C ATOM 370 N ILE B 51 -10.748 18.629 30.814 1.00 33.23 N ANISOU 370 N ILE B 51 5361 4138 3126 253 -102 -74 N ATOM 371 CA ILE B 51 -10.715 19.842 30.017 1.00 33.91 C ANISOU 371 CA ILE B 51 5525 4170 3190 257 -151 -33 C ATOM 372 C ILE B 51 -9.833 19.527 28.806 1.00 34.11 C ANISOU 372 C ILE B 51 5545 4226 3190 199 -112 27 C ATOM 373 O ILE B 51 -8.736 18.970 28.974 1.00 33.87 O ANISOU 373 O ILE B 51 5476 4221 3171 144 -67 50 O ATOM 374 CB ILE B 51 -10.184 21.061 30.834 1.00 34.29 C ANISOU 374 CB ILE B 51 5638 4125 3264 247 -212 -13 C ATOM 375 CG1 ILE B 51 -10.258 22.350 30.003 1.00 35.08 C ANISOU 375 CG1 ILE B 51 5832 4151 3346 247 -288 37 C ATOM 376 CG2 ILE B 51 -8.760 20.830 31.352 1.00 34.02 C ANISOU 376 CG2 ILE B 51 5582 4080 3262 162 -179 27 C ATOM 377 CD1 ILE B 51 -10.196 23.630 30.811 1.00 35.73 C ANISOU 377 CD1 ILE B 51 6001 4120 3454 270 -388 32 C ATOM 378 N TYR B 52 -10.323 19.822 27.598 1.00 34.33 N ANISOU 378 N TYR B 52 5601 4269 3174 220 -129 47 N ATOM 379 CA TYR B 52 -9.502 19.693 26.393 1.00 34.76 C ANISOU 379 CA TYR B 52 5649 4373 3184 175 -98 111 C ATOM 380 C TYR B 52 -8.667 20.952 26.282 1.00 35.49 C ANISOU 380 C TYR B 52 5798 4409 3277 109 -140 206 C ATOM 381 O TYR B 52 -9.217 22.044 26.195 1.00 35.82 O ANISOU 381 O TYR B 52 5915 4375 3321 126 -214 226 O ATOM 382 CB TYR B 52 -10.341 19.498 25.122 1.00 35.00 C ANISOU 382 CB TYR B 52 5686 4452 3161 222 -103 100 C ATOM 383 CG TYR B 52 -9.482 19.143 23.919 1.00 35.49 C ANISOU 383 CG TYR B 52 5723 4601 3162 193 -60 153 C ATOM 384 CD1 TYR B 52 -8.724 17.972 23.908 1.00 35.27 C ANISOU 384 CD1 TYR B 52 5629 4647 3125 187 -1 125 C ATOM 385 CD2 TYR B 52 -9.407 19.980 22.802 1.00 36.35 C ANISOU 385 CD2 TYR B 52 5870 4727 3213 178 -84 230 C ATOM 386 CE1 TYR B 52 -7.924 17.637 22.827 1.00 35.91 C ANISOU 386 CE1 TYR B 52 5678 4832 3134 183 36 163 C ATOM 387 CE2 TYR B 52 -8.610 19.650 21.712 1.00 36.89 C ANISOU 387 CE2 TYR B 52 5901 4907 3208 159 -41 282 C ATOM 388 CZ TYR B 52 -7.870 18.475 21.733 1.00 36.68 C ANISOU 388 CZ TYR B 52 5802 4968 3166 169 21 242 C ATOM 389 OH TYR B 52 -7.074 18.122 20.669 1.00 37.54 O ANISOU 389 OH TYR B 52 5865 5211 3187 172 64 282 O ATOM 390 N ALA B 52A -7.345 20.794 26.295 1.00 35.88 N ANISOU 390 N ALA B 52A 5811 4495 3324 34 -102 266 N ATOM 391 CA ALA B 52A -6.422 21.935 26.326 1.00 37.07 C ANISOU 391 CA ALA B 52A 6005 4596 3485 -54 -149 372 C ATOM 392 C ALA B 52A -6.503 22.824 25.089 1.00 38.46 C ANISOU 392 C ALA B 52A 6230 4774 3609 -85 -193 468 C ATOM 393 O ALA B 52A -6.335 24.037 25.192 1.00 39.85 O ANISOU 393 O ALA B 52A 6482 4853 3807 -138 -280 542 O ATOM 394 CB ALA B 52A -4.996 21.450 26.518 1.00 37.15 C ANISOU 394 CB ALA B 52A 5944 4680 3492 -129 -91 421 C ATOM 395 N GLY B 53 -6.750 22.221 23.928 1.00 38.85 N ANISOU 395 N GLY B 53 6241 4932 3590 -51 -144 467 N ATOM 396 CA GLY B 53 -6.885 22.957 22.672 1.00 39.75 C ANISOU 396 CA GLY B 53 6392 5070 3641 -72 -179 559 C ATOM 397 C GLY B 53 -8.006 23.985 22.640 1.00 40.18 C ANISOU 397 C GLY B 53 6551 4999 3717 -31 -278 552 C ATOM 398 O GLY B 53 -7.812 25.083 22.126 1.00 41.27 O ANISOU 398 O GLY B 53 6753 5086 3841 -90 -351 660 O ATOM 399 N THR B 54 -9.169 23.637 23.188 1.00 39.52 N ANISOU 399 N THR B 54 6480 4872 3663 69 -287 430 N ATOM 400 CA THR B 54 -10.344 24.522 23.175 1.00 40.16 C ANISOU 400 CA THR B 54 6650 4856 3754 138 -379 402 C ATOM 401 C THR B 54 -10.644 25.207 24.512 1.00 40.17 C ANISOU 401 C THR B 54 6710 4731 3823 170 -455 349 C ATOM 402 O THR B 54 -11.313 26.243 24.539 1.00 40.84 O ANISOU 402 O THR B 54 6888 4715 3915 217 -558 346 O ATOM 403 CB THR B 54 -11.617 23.757 22.745 1.00 39.81 C ANISOU 403 CB THR B 54 6573 4876 3679 242 -350 304 C ATOM 404 OG1 THR B 54 -11.877 22.679 23.656 1.00 39.07 O ANISOU 404 OG1 THR B 54 6408 4819 3619 279 -293 205 O ATOM 405 CG2 THR B 54 -11.466 23.197 21.342 1.00 40.09 C ANISOU 405 CG2 THR B 54 6568 5026 3639 232 -297 344 C ATOM 406 N GLY B 55 -10.175 24.626 25.615 1.00 39.63 N ANISOU 406 N GLY B 55 6590 4670 3797 157 -411 301 N ATOM 407 CA GLY B 55 -10.622 25.023 26.946 1.00 39.62 C ANISOU 407 CA GLY B 55 6624 4586 3844 217 -467 222 C ATOM 408 C GLY B 55 -12.004 24.499 27.322 1.00 39.38 C ANISOU 408 C GLY B 55 6558 4602 3801 339 -453 107 C ATOM 409 O GLY B 55 -12.518 24.851 28.385 1.00 39.79 O ANISOU 409 O GLY B 55 6629 4614 3874 411 -500 36 O ATOM 410 N GLY B 56 -12.600 23.650 26.479 1.00 39.01 N ANISOU 410 N GLY B 56 6454 4652 3715 364 -393 88 N ATOM 411 CA GLY B 56 -13.901 23.047 26.761 1.00 38.84 C ANISOU 411 CA GLY B 56 6382 4695 3680 458 -379 -5 C ATOM 412 C GLY B 56 -13.766 21.923 27.774 1.00 38.11 C ANISOU 412 C GLY B 56 6199 4665 3617 446 -311 -55 C ATOM 413 O GLY B 56 -12.725 21.270 27.839 1.00 37.61 O ANISOU 413 O GLY B 56 6099 4618 3572 370 -253 -24 O ATOM 414 N SER B 57 -14.828 21.684 28.544 1.00 37.85 N ANISOU 414 N SER B 57 6122 4678 3581 523 -320 -128 N ATOM 415 CA SER B 57 -14.775 20.756 29.672 1.00 37.32 C ANISOU 415 CA SER B 57 5972 4668 3539 511 -271 -164 C ATOM 416 C SER B 57 -16.038 19.916 29.843 1.00 37.22 C ANISOU 416 C SER B 57 5873 4763 3505 559 -254 -212 C ATOM 417 O SER B 57 -17.123 20.287 29.393 1.00 37.79 O ANISOU 417 O SER B 57 5949 4868 3541 630 -292 -236 O ATOM 418 CB SER B 57 -14.525 21.526 30.970 1.00 37.56 C ANISOU 418 CB SER B 57 6033 4651 3589 544 -311 -189 C ATOM 419 OG SER B 57 -15.633 22.351 31.281 1.00 38.15 O ANISOU 419 OG SER B 57 6133 4733 3630 660 -380 -243 O ATOM 420 N SER B 58 -15.857 18.768 30.491 1.00 36.66 N ANISOU 420 N SER B 58 5722 4748 3460 511 -203 -217 N ATOM 421 CA SER B 58 -16.946 17.937 30.989 1.00 36.32 C ANISOU 421 CA SER B 58 5584 4812 3405 532 -195 -244 C ATOM 422 C SER B 58 -16.706 17.715 32.481 1.00 35.95 C ANISOU 422 C SER B 58 5486 4799 3375 526 -177 -253 C ATOM 423 O SER B 58 -15.576 17.413 32.896 1.00 35.46 O ANISOU 423 O SER B 58 5435 4687 3351 464 -147 -233 O ATOM 424 CB SER B 58 -16.974 16.593 30.274 1.00 36.02 C ANISOU 424 CB SER B 58 5499 4804 3383 464 -166 -229 C ATOM 425 OG SER B 58 -17.959 15.754 30.845 1.00 36.27 O ANISOU 425 OG SER B 58 5436 4933 3412 459 -170 -236 O ATOM 426 N TYR B 59 -17.773 17.855 33.269 1.00 35.76 N ANISOU 426 N TYR B 59 5397 4876 3314 595 -196 -282 N ATOM 427 CA TYR B 59 -17.718 17.723 34.718 1.00 35.28 C ANISOU 427 CA TYR B 59 5277 4879 3249 608 -182 -292 C ATOM 428 C TYR B 59 -18.600 16.580 35.187 1.00 35.22 C ANISOU 428 C TYR B 59 5141 5014 3227 574 -161 -269 C ATOM 429 O TYR B 59 -19.766 16.488 34.794 1.00 35.69 O ANISOU 429 O TYR B 59 5146 5166 3247 609 -181 -272 O ATOM 430 CB TYR B 59 -18.194 19.018 35.381 1.00 35.71 C ANISOU 430 CB TYR B 59 5362 4955 3253 738 -233 -346 C ATOM 431 CG TYR B 59 -17.154 20.105 35.395 1.00 35.45 C ANISOU 431 CG TYR B 59 5452 4772 3246 752 -271 -359 C ATOM 432 CD1 TYR B 59 -16.213 20.178 36.418 1.00 35.05 C ANISOU 432 CD1 TYR B 59 5413 4683 3221 727 -262 -361 C ATOM 433 CD2 TYR B 59 -17.107 21.062 34.391 1.00 35.64 C ANISOU 433 CD2 TYR B 59 5581 4693 3269 782 -324 -361 C ATOM 434 CE1 TYR B 59 -15.248 21.169 36.435 1.00 35.09 C ANISOU 434 CE1 TYR B 59 5529 4548 3254 726 -310 -364 C ATOM 435 CE2 TYR B 59 -16.150 22.063 34.404 1.00 35.90 C ANISOU 435 CE2 TYR B 59 5726 4584 3329 775 -374 -355 C ATOM 436 CZ TYR B 59 -15.226 22.112 35.431 1.00 35.64 C ANISOU 436 CZ TYR B 59 5702 4514 3326 744 -369 -357 C ATOM 437 OH TYR B 59 -14.276 23.103 35.443 1.00 35.94 O ANISOU 437 OH TYR B 59 5850 4410 3397 724 -431 -342 O ATOM 438 N ASN B 60 -18.038 15.716 36.031 1.00 34.69 N ANISOU 438 N ASN B 60 5025 4965 3191 500 -128 -238 N ATOM 439 CA ASN B 60 -18.838 14.826 36.861 1.00 34.82 C ANISOU 439 CA ASN B 60 4913 5130 3186 470 -119 -203 C ATOM 440 C ASN B 60 -19.727 15.732 37.704 1.00 35.67 C ANISOU 440 C ASN B 60 4968 5372 3212 594 -136 -241 C ATOM 441 O ASN B 60 -19.227 16.648 38.360 1.00 35.76 O ANISOU 441 O ASN B 60 5031 5349 3206 669 -145 -285 O ATOM 442 CB ASN B 60 -17.945 13.971 37.763 1.00 34.13 C ANISOU 442 CB ASN B 60 4800 5026 3143 384 -89 -165 C ATOM 443 CG ASN B 60 -18.708 12.893 38.500 1.00 34.27 C ANISOU 443 CG ASN B 60 4689 5187 3147 321 -89 -103 C ATOM 444 OD1 ASN B 60 -19.922 12.973 38.681 1.00 34.86 O ANISOU 444 OD1 ASN B 60 4672 5412 3162 358 -104 -91 O ATOM 445 ND2 ASN B 60 -17.991 11.877 38.940 1.00 33.95 N ANISOU 445 ND2 ASN B 60 4635 5105 3159 222 -77 -57 N ATOM 446 N GLN B 61 -21.033 15.476 37.675 1.00 36.62 N ANISOU 446 N GLN B 61 4984 5650 3278 619 -150 -225 N ATOM 447 CA GLN B 61 -22.017 16.345 38.328 1.00 37.67 C ANISOU 447 CA GLN B 61 5056 5943 3315 761 -170 -269 C ATOM 448 C GLN B 61 -21.885 16.356 39.851 1.00 38.11 C ANISOU 448 C GLN B 61 5036 6119 3324 797 -150 -268 C ATOM 449 O GLN B 61 -22.214 17.347 40.503 1.00 38.48 O ANISOU 449 O GLN B 61 5081 6244 3295 945 -173 -335 O ATOM 450 CB GLN B 61 -23.436 15.945 37.932 1.00 38.74 C ANISOU 450 CB GLN B 61 5075 6248 3398 767 -185 -239 C ATOM 451 CG GLN B 61 -24.481 16.967 38.364 1.00 40.22 C ANISOU 451 CG GLN B 61 5206 6601 3474 943 -212 -300 C ATOM 452 CD GLN B 61 -25.740 16.935 37.528 1.00 41.16 C ANISOU 452 CD GLN B 61 5259 6829 3549 974 -239 -294 C ATOM 453 OE1 GLN B 61 -26.848 16.926 38.065 1.00 42.58 O ANISOU 453 OE1 GLN B 61 5296 7245 3637 1039 -243 -283 O ATOM 454 NE2 GLN B 61 -25.581 16.931 36.210 1.00 40.68 N ANISOU 454 NE2 GLN B 61 5295 6615 3547 931 -258 -298 N ATOM 455 N LYS B 62 -21.400 15.248 40.401 1.00 37.87 N ANISOU 455 N LYS B 62 4950 6101 3336 669 -116 -196 N ATOM 456 CA LYS B 62 -21.013 15.156 41.805 1.00 38.02 C ANISOU 456 CA LYS B 62 4914 6205 3325 681 -93 -185 C ATOM 457 C LYS B 62 -20.008 16.244 42.223 1.00 37.64 C ANISOU 457 C LYS B 62 4988 6029 3285 772 -105 -268 C ATOM 458 O LYS B 62 -20.076 16.745 43.345 1.00 37.67 O ANISOU 458 O LYS B 62 4955 6138 3221 869 -109 -305 O ATOM 459 CB LYS B 62 -20.446 13.757 42.082 1.00 37.71 C ANISOU 459 CB LYS B 62 4834 6140 3356 511 -66 -91 C ATOM 460 CG LYS B 62 -20.010 13.509 43.512 1.00 38.10 C ANISOU 460 CG LYS B 62 4822 6278 3377 503 -41 -63 C ATOM 461 CD LYS B 62 -19.504 12.092 43.694 1.00 37.88 C ANISOU 461 CD LYS B 62 4762 6209 3423 333 -30 35 C ATOM 462 CE LYS B 62 -18.821 11.942 45.042 1.00 37.68 C ANISOU 462 CE LYS B 62 4705 6231 3381 328 -6 55 C ATOM 463 NZ LYS B 62 -18.568 10.516 45.367 1.00 37.76 N ANISOU 463 NZ LYS B 62 4661 6240 3446 168 -8 165 N ATOM 464 N PHE B 63 -19.091 16.603 41.326 1.00 37.21 N ANISOU 464 N PHE B 63 5073 5757 3307 739 -117 -292 N ATOM 465 CA PHE B 63 -18.090 17.650 41.590 1.00 37.60 C ANISOU 465 CA PHE B 63 5245 5664 3376 800 -143 -355 C ATOM 466 C PHE B 63 -18.390 18.973 40.868 1.00 38.34 C ANISOU 466 C PHE B 63 5444 5676 3449 917 -207 -426 C ATOM 467 O PHE B 63 -17.492 19.804 40.705 1.00 38.04 O ANISOU 467 O PHE B 63 5530 5473 3449 931 -244 -458 O ATOM 468 CB PHE B 63 -16.697 17.149 41.190 1.00 36.57 C ANISOU 468 CB PHE B 63 5192 5359 3344 670 -117 -316 C ATOM 469 CG PHE B 63 -16.271 15.897 41.903 1.00 36.28 C ANISOU 469 CG PHE B 63 5075 5372 3336 562 -70 -252 C ATOM 470 CD1 PHE B 63 -16.679 14.646 41.447 1.00 36.29 C ANISOU 470 CD1 PHE B 63 5007 5417 3364 459 -49 -184 C ATOM 471 CD2 PHE B 63 -15.447 15.961 43.018 1.00 36.06 C ANISOU 471 CD2 PHE B 63 5049 5337 3313 562 -60 -259 C ATOM 472 CE1 PHE B 63 -16.282 13.485 42.096 1.00 35.97 C ANISOU 472 CE1 PHE B 63 4906 5405 3357 358 -24 -121 C ATOM 473 CE2 PHE B 63 -15.046 14.806 43.670 1.00 35.90 C ANISOU 473 CE2 PHE B 63 4961 5358 3320 464 -23 -196 C ATOM 474 CZ PHE B 63 -15.462 13.566 43.208 1.00 35.86 C ANISOU 474 CZ PHE B 63 4894 5389 3344 361 -8 -125 C ATOM 475 N ARG B 64 -19.651 19.181 40.476 1.00 39.58 N ANISOU 475 N ARG B 64 5548 5949 3542 999 -227 -445 N ATOM 476 CA ARG B 64 -20.074 20.369 39.725 1.00 40.66 C ANISOU 476 CA ARG B 64 5781 6015 3655 1115 -296 -509 C ATOM 477 C ARG B 64 -19.674 21.655 40.440 1.00 41.39 C ANISOU 477 C ARG B 64 5972 6035 3721 1248 -369 -594 C ATOM 478 O ARG B 64 -18.947 22.478 39.894 1.00 41.01 O ANISOU 478 O ARG B 64 6067 5792 3723 1245 -424 -611 O ATOM 479 CB ARG B 64 -21.597 20.350 39.523 1.00 41.89 C ANISOU 479 CB ARG B 64 5833 6359 3725 1207 -307 -524 C ATOM 480 CG ARG B 64 -22.181 21.567 38.816 1.00 42.78 C ANISOU 480 CG ARG B 64 6036 6418 3800 1349 -386 -595 C ATOM 481 CD ARG B 64 -23.686 21.432 38.668 1.00 43.99 C ANISOU 481 CD ARG B 64 6065 6785 3864 1438 -390 -606 C ATOM 482 NE ARG B 64 -24.377 21.796 39.906 1.00 45.38 N ANISOU 482 NE ARG B 64 6143 7170 3929 1594 -406 -664 N ATOM 483 CZ ARG B 64 -25.700 21.774 40.082 1.00 46.71 C ANISOU 483 CZ ARG B 64 6176 7580 3992 1700 -410 -680 C ATOM 484 NH1 ARG B 64 -26.213 22.145 41.257 1.00 47.88 N ANISOU 484 NH1 ARG B 64 6234 7931 4027 1855 -423 -738 N ATOM 485 NH2 ARG B 64 -26.521 21.386 39.102 1.00 46.93 N ANISOU 485 NH2 ARG B 64 6150 7662 4018 1659 -402 -640 N ATOM 486 N ASP B 65 -20.144 21.805 41.672 1.00 42.55 N ANISOU 486 N ASP B 65 6038 6343 3785 1360 -377 -642 N ATOM 487 CA ASP B 65 -19.866 23.002 42.464 1.00 43.72 C ANISOU 487 CA ASP B 65 6277 6439 3897 1511 -462 -740 C ATOM 488 C ASP B 65 -18.506 22.926 43.181 1.00 43.36 C ANISOU 488 C ASP B 65 6288 6273 3914 1429 -454 -727 C ATOM 489 O ASP B 65 -17.997 23.949 43.632 1.00 44.06 O ANISOU 489 O ASP B 65 6490 6250 4003 1517 -541 -799 O ATOM 490 CB ASP B 65 -21.006 23.247 43.461 1.00 45.10 C ANISOU 490 CB ASP B 65 6336 6866 3935 1697 -480 -811 C ATOM 491 CG ASP B 65 -22.381 23.310 42.784 1.00 45.97 C ANISOU 491 CG ASP B 65 6373 7120 3975 1783 -488 -822 C ATOM 492 OD1 ASP B 65 -22.469 23.738 41.612 1.00 45.81 O ANISOU 492 OD1 ASP B 65 6450 6957 3999 1771 -528 -823 O ATOM 493 OD2 ASP B 65 -23.379 22.927 43.426 1.00 47.00 O ANISOU 493 OD2 ASP B 65 6340 7520 3999 1859 -455 -823 O ATOM 494 N LYS B 66 -17.917 21.730 43.264 1.00 42.32 N ANISOU 494 N LYS B 66 6086 6157 3837 1262 -362 -638 N ATOM 495 CA LYS B 66 -16.638 21.519 43.955 1.00 41.99 C ANISOU 495 CA LYS B 66 6080 6023 3852 1179 -345 -618 C ATOM 496 C LYS B 66 -15.421 21.981 43.145 1.00 41.55 C ANISOU 496 C LYS B 66 6171 5721 3897 1082 -377 -597 C ATOM 497 O LYS B 66 -14.651 22.827 43.602 1.00 42.03 O ANISOU 497 O LYS B 66 6330 5661 3978 1115 -445 -639 O ATOM 498 CB LYS B 66 -16.481 20.031 44.315 1.00 41.37 C ANISOU 498 CB LYS B 66 5873 6052 3793 1042 -245 -528 C ATOM 499 CG LYS B 66 -15.263 19.664 45.160 1.00 40.88 C ANISOU 499 CG LYS B 66 5823 5933 3777 964 -221 -506 C ATOM 500 CD LYS B 66 -15.163 20.435 46.473 1.00 41.97 C ANISOU 500 CD LYS B 66 5970 6127 3850 1096 -270 -586 C ATOM 501 CE LYS B 66 -16.389 20.268 47.365 1.00 42.66 C ANISOU 501 CE LYS B 66 5919 6479 3813 1218 -257 -610 C ATOM 502 NZ LYS B 66 -16.198 20.931 48.682 1.00 43.75 N ANISOU 502 NZ LYS B 66 6062 6684 3878 1353 -303 -692 N ATOM 503 N ALA B 67 -15.253 21.409 41.953 1.00 40.92 N ANISOU 503 N ALA B 67 6098 5576 3874 963 -333 -527 N ATOM 504 CA ALA B 67 -14.043 21.593 41.149 1.00 40.28 C ANISOU 504 CA ALA B 67 6119 5307 3878 849 -340 -481 C ATOM 505 C ALA B 67 -14.263 22.564 39.988 1.00 40.62 C ANISOU 505 C ALA B 67 6270 5234 3930 880 -409 -489 C ATOM 506 O ALA B 67 -15.362 22.639 39.436 1.00 40.52 O ANISOU 506 O ALA B 67 6233 5290 3873 949 -418 -507 O ATOM 507 CB ALA B 67 -13.562 20.250 40.623 1.00 39.17 C ANISOU 507 CB ALA B 67 5913 5182 3788 701 -247 -401 C ATOM 508 N GLN B 68 -13.207 23.302 39.640 1.00 40.41 N ANISOU 508 N GLN B 68 6359 5039 3958 824 -462 -466 N ATOM 509 CA GLN B 68 -13.191 24.163 38.464 1.00 41.05 C ANISOU 509 CA GLN B 68 6547 4995 4056 817 -528 -443 C ATOM 510 C GLN B 68 -11.857 24.011 37.735 1.00 40.00 C ANISOU 510 C GLN B 68 6455 4754 3991 659 -501 -351 C ATOM 511 O GLN B 68 -10.812 24.399 38.262 1.00 39.46 O ANISOU 511 O GLN B 68 6432 4599 3960 607 -535 -335 O ATOM 512 CB GLN B 68 -13.407 25.622 38.856 1.00 43.23 C ANISOU 512 CB GLN B 68 6942 5170 4314 939 -669 -512 C ATOM 513 CG GLN B 68 -13.753 26.521 37.675 1.00 44.53 C ANISOU 513 CG GLN B 68 7212 5226 4481 961 -752 -494 C ATOM 514 CD GLN B 68 -13.505 27.989 37.951 1.00 46.64 C ANISOU 514 CD GLN B 68 7634 5325 4763 1032 -917 -534 C ATOM 515 OE1 GLN B 68 -13.511 28.434 39.105 1.00 47.96 O ANISOU 515 OE1 GLN B 68 7825 5487 4911 1131 -983 -616 O ATOM 516 NE2 GLN B 68 -13.292 28.760 36.885 1.00 47.72 N ANISOU 516 NE2 GLN B 68 7882 5321 4930 983 -996 -475 N ATOM 517 N LEU B 69 -11.906 23.444 36.527 1.00 39.31 N ANISOU 517 N LEU B 69 6343 4686 3909 588 -444 -293 N ATOM 518 CA LEU B 69 -10.712 23.198 35.720 1.00 38.87 C ANISOU 518 CA LEU B 69 6302 4571 3895 452 -407 -205 C ATOM 519 C LEU B 69 -10.414 24.391 34.829 1.00 39.58 C ANISOU 519 C LEU B 69 6507 4537 3995 428 -496 -156 C ATOM 520 O LEU B 69 -11.323 24.968 34.241 1.00 40.01 O ANISOU 520 O LEU B 69 6609 4573 4019 501 -550 -175 O ATOM 521 CB LEU B 69 -10.879 21.958 34.834 1.00 37.83 C ANISOU 521 CB LEU B 69 6088 4532 3755 400 -308 -173 C ATOM 522 CG LEU B 69 -11.188 20.600 35.469 1.00 36.93 C ANISOU 522 CG LEU B 69 5862 4532 3638 397 -228 -199 C ATOM 523 CD1 LEU B 69 -10.841 19.493 34.484 1.00 36.19 C ANISOU 523 CD1 LEU B 69 5723 4476 3553 322 -157 -156 C ATOM 524 CD2 LEU B 69 -10.458 20.387 36.784 1.00 36.67 C ANISOU 524 CD2 LEU B 69 5802 4502 3630 377 -215 -211 C ATOM 525 N THR B 70 -9.138 24.755 34.747 1.00 39.80 N ANISOU 525 N THR B 70 6575 4485 4062 320 -516 -84 N ATOM 526 CA THR B 70 -8.664 25.737 33.775 1.00 41.03 C ANISOU 526 CA THR B 70 6824 4537 4230 254 -592 1 C ATOM 527 C THR B 70 -7.339 25.264 33.222 1.00 41.13 C ANISOU 527 C THR B 70 6790 4578 4259 109 -525 105 C ATOM 528 O THR B 70 -6.718 24.344 33.756 1.00 40.28 O ANISOU 528 O THR B 70 6600 4541 4165 71 -441 97 O ATOM 529 CB THR B 70 -8.483 27.147 34.379 1.00 41.88 C ANISOU 529 CB THR B 70 7058 4489 4366 279 -747 -9 C ATOM 530 OG1 THR B 70 -7.521 27.101 35.438 1.00 41.80 O ANISOU 530 OG1 THR B 70 7037 4452 4395 228 -753 -12 O ATOM 531 CG2 THR B 70 -9.804 27.685 34.906 1.00 42.23 C ANISOU 531 CG2 THR B 70 7150 4517 4378 451 -825 -124 C ATOM 532 N VAL B 71 -6.927 25.898 32.134 1.00 42.48 N ANISOU 532 N VAL B 71 7011 4706 4424 32 -565 205 N ATOM 533 CA VAL B 71 -5.718 25.532 31.419 1.00 43.25 C ANISOU 533 CA VAL B 71 7053 4862 4516 -99 -502 316 C ATOM 534 C VAL B 71 -5.015 26.808 30.967 1.00 45.12 C ANISOU 534 C VAL B 71 7379 4992 4771 -202 -616 436 C ATOM 535 O VAL B 71 -5.665 27.733 30.488 1.00 45.90 O ANISOU 535 O VAL B 71 7575 5000 4865 -172 -715 452 O ATOM 536 CB VAL B 71 -6.062 24.646 30.202 1.00 42.91 C ANISOU 536 CB VAL B 71 6942 4945 4418 -88 -404 330 C ATOM 537 CG1 VAL B 71 -4.864 24.489 29.284 1.00 43.75 C ANISOU 537 CG1 VAL B 71 6999 5128 4497 -205 -357 451 C ATOM 538 CG2 VAL B 71 -6.559 23.278 30.649 1.00 41.85 C ANISOU 538 CG2 VAL B 71 6717 4908 4276 -17 -304 231 C ATOM 539 N ASP B 72 -3.694 26.849 31.141 1.00 46.42 N ANISOU 539 N ASP B 72 7510 5169 4958 -326 -608 524 N ATOM 540 CA ASP B 72 -2.852 27.917 30.614 1.00 48.46 C ANISOU 540 CA ASP B 72 7826 5356 5230 -463 -707 672 C ATOM 541 C ASP B 72 -1.972 27.317 29.518 1.00 49.26 C ANISOU 541 C ASP B 72 7819 5622 5275 -564 -601 791 C ATOM 542 O ASP B 72 -1.015 26.591 29.801 1.00 49.27 O ANISOU 542 O ASP B 72 7719 5728 5272 -616 -516 809 O ATOM 543 CB ASP B 72 -2.005 28.535 31.730 1.00 49.10 C ANISOU 543 CB ASP B 72 7949 5329 5377 -532 -799 689 C ATOM 544 CG ASP B 72 -1.319 29.833 31.309 1.00 50.81 C ANISOU 544 CG ASP B 72 8256 5428 5623 -676 -948 842 C ATOM 545 OD1 ASP B 72 -0.833 29.937 30.163 1.00 51.81 O ANISOU 545 OD1 ASP B 72 8343 5632 5709 -784 -925 986 O ATOM 546 OD2 ASP B 72 -1.258 30.762 32.141 1.00 51.74 O ANISOU 546 OD2 ASP B 72 8483 5374 5801 -682 -1098 823 O ATOM 547 N THR B 73 -2.321 27.624 28.270 1.00 50.75 N ANISOU 547 N THR B 73 8027 5843 5414 -579 -610 866 N ATOM 548 CA THR B 73 -1.602 27.142 27.090 1.00 51.84 C ANISOU 548 CA THR B 73 8063 6158 5477 -655 -518 979 C ATOM 549 C THR B 73 -0.139 27.592 27.054 1.00 53.06 C ANISOU 549 C THR B 73 8171 6356 5634 -826 -543 1140 C ATOM 550 O THR B 73 0.740 26.805 26.698 1.00 53.08 O ANISOU 550 O THR B 73 8045 6540 5582 -866 -433 1184 O ATOM 551 CB THR B 73 -2.299 27.624 25.797 1.00 53.22 C ANISOU 551 CB THR B 73 8285 6341 5595 -644 -550 1042 C ATOM 552 OG1 THR B 73 -3.681 27.242 25.827 1.00 52.89 O ANISOU 552 OG1 THR B 73 8281 6264 5550 -489 -534 897 O ATOM 553 CG2 THR B 73 -1.635 27.037 24.550 1.00 53.77 C ANISOU 553 CG2 THR B 73 8240 6624 5567 -696 -446 1143 C ATOM 554 N SER B 74 0.113 28.845 27.431 1.00 54.40 N ANISOU 554 N SER B 74 8444 6361 5864 -922 -696 1224 N ATOM 555 CA SER B 74 1.457 29.437 27.383 1.00 55.96 C ANISOU 555 CA SER B 74 8608 6584 6072 -1109 -750 1400 C ATOM 556 C SER B 74 2.471 28.658 28.219 1.00 55.55 C ANISOU 556 C SER B 74 8443 6631 6034 -1137 -664 1371 C ATOM 557 O SER B 74 3.531 28.266 27.723 1.00 56.01 O ANISOU 557 O SER B 74 8372 6874 6035 -1231 -585 1481 O ATOM 558 CB SER B 74 1.412 30.888 27.867 1.00 57.38 C ANISOU 558 CB SER B 74 8945 6522 6335 -1190 -960 1463 C ATOM 559 OG SER B 74 0.348 31.589 27.253 1.00 58.01 O ANISOU 559 OG SER B 74 9146 6485 6410 -1132 -1052 1460 O ATOM 560 N SER B 75 2.118 28.427 29.481 1.00 54.52 N ANISOU 560 N SER B 75 8355 6389 5970 -1047 -678 1220 N ATOM 561 CA SER B 75 2.965 27.691 30.422 1.00 53.82 C ANISOU 561 CA SER B 75 8176 6371 5903 -1057 -607 1173 C ATOM 562 C SER B 75 2.846 26.157 30.312 1.00 52.48 C ANISOU 562 C SER B 75 7885 6377 5679 -943 -432 1065 C ATOM 563 O SER B 75 3.580 25.438 30.997 1.00 51.33 O ANISOU 563 O SER B 75 7656 6305 5542 -945 -366 1030 O ATOM 564 CB SER B 75 2.632 28.131 31.849 1.00 53.46 C ANISOU 564 CB SER B 75 8232 6136 5945 -1006 -708 1061 C ATOM 565 OG SER B 75 1.249 27.979 32.110 1.00 52.42 O ANISOU 565 OG SER B 75 8173 5926 5819 -842 -710 910 O ATOM 566 N ARG B 76 1.928 25.668 29.468 1.00 52.21 N ANISOU 566 N ARG B 76 7848 6399 5590 -844 -370 1012 N ATOM 567 CA ARG B 76 1.689 24.228 29.257 1.00 51.03 C ANISOU 567 CA ARG B 76 7604 6392 5392 -731 -229 907 C ATOM 568 C ARG B 76 1.255 23.561 30.563 1.00 48.69 C ANISOU 568 C ARG B 76 7318 6028 5153 -636 -208 755 C ATOM 569 O ARG B 76 1.652 22.432 30.860 1.00 47.74 O ANISOU 569 O ARG B 76 7110 6009 5020 -595 -116 697 O ATOM 570 CB ARG B 76 2.929 23.523 28.670 1.00 52.43 C ANISOU 570 CB ARG B 76 7640 6781 5498 -786 -132 986 C ATOM 571 CG ARG B 76 3.617 24.257 27.520 1.00 54.67 C ANISOU 571 CG ARG B 76 7889 7167 5716 -909 -154 1169 C ATOM 572 CD ARG B 76 4.923 23.579 27.118 1.00 55.83 C ANISOU 572 CD ARG B 76 7879 7549 5785 -954 -59 1241 C ATOM 573 NE ARG B 76 4.746 22.556 26.085 1.00 56.46 N ANISOU 573 NE ARG B 76 7877 7812 5761 -846 49 1193 N ATOM 574 CZ ARG B 76 5.704 21.733 25.649 1.00 57.34 C ANISOU 574 CZ ARG B 76 7850 8151 5784 -826 143 1212 C ATOM 575 NH1 ARG B 76 5.420 20.852 24.694 1.00 57.58 N ANISOU 575 NH1 ARG B 76 7829 8328 5720 -708 220 1150 N ATOM 576 NH2 ARG B 76 6.942 21.771 26.155 1.00 57.74 N ANISOU 576 NH2 ARG B 76 7813 8289 5836 -912 153 1285 N ATOM 577 N THR B 77 0.421 24.273 31.321 1.00 47.56 N ANISOU 577 N THR B 77 7284 5720 5068 -594 -302 693 N ATOM 578 CA THR B 77 0.084 23.914 32.695 1.00 45.90 C ANISOU 578 CA THR B 77 7086 5443 4909 -520 -305 571 C ATOM 579 C THR B 77 -1.430 23.876 32.876 1.00 44.47 C ANISOU 579 C THR B 77 6967 5200 4730 -390 -324 457 C ATOM 580 O THR B 77 -2.131 24.801 32.442 1.00 45.32 O ANISOU 580 O THR B 77 7164 5220 4836 -372 -409 473 O ATOM 581 CB THR B 77 0.691 24.938 33.675 1.00 46.71 C ANISOU 581 CB THR B 77 7255 5419 5074 -592 -419 604 C ATOM 582 OG1 THR B 77 2.114 24.966 33.507 1.00 47.32 O ANISOU 582 OG1 THR B 77 7261 5569 5148 -725 -403 721 O ATOM 583 CG2 THR B 77 0.359 24.586 35.133 1.00 46.16 C ANISOU 583 CG2 THR B 77 7194 5298 5045 -506 -422 477 C ATOM 584 N ALA B 78 -1.918 22.807 33.512 1.00 42.10 N ANISOU 584 N ALA B 78 6613 4951 4430 -303 -250 351 N ATOM 585 CA ALA B 78 -3.332 22.651 33.856 1.00 40.86 C ANISOU 585 CA ALA B 78 6488 4766 4270 -184 -261 246 C ATOM 586 C ALA B 78 -3.543 22.973 35.333 1.00 40.30 C ANISOU 586 C ALA B 78 6450 4625 4238 -135 -315 172 C ATOM 587 O ALA B 78 -2.645 22.772 36.156 1.00 39.47 O ANISOU 587 O ALA B 78 6313 4522 4160 -180 -304 178 O ATOM 588 CB ALA B 78 -3.801 21.235 33.553 1.00 39.73 C ANISOU 588 CB ALA B 78 6260 4735 4099 -130 -157 192 C ATOM 589 N TYR B 79 -4.738 23.467 35.655 1.00 40.04 N ANISOU 589 N TYR B 79 6474 4542 4197 -33 -374 99 N ATOM 590 CA TYR B 79 -5.093 23.861 37.016 1.00 39.51 C ANISOU 590 CA TYR B 79 6440 4427 4146 42 -434 17 C ATOM 591 C TYR B 79 -6.444 23.275 37.409 1.00 38.80 C ANISOU 591 C TYR B 79 6308 4414 4020 166 -398 -77 C ATOM 592 O TYR B 79 -7.353 23.216 36.586 1.00 38.36 O ANISOU 592 O TYR B 79 6255 4387 3935 210 -388 -85 O ATOM 593 CB TYR B 79 -5.153 25.384 37.124 1.00 40.51 C ANISOU 593 CB TYR B 79 6695 4407 4291 57 -584 22 C ATOM 594 CG TYR B 79 -3.829 26.073 36.877 1.00 41.15 C ANISOU 594 CG TYR B 79 6819 4404 4413 -82 -645 128 C ATOM 595 CD1 TYR B 79 -2.809 26.011 37.825 1.00 41.07 C ANISOU 595 CD1 TYR B 79 6787 4378 4438 -140 -653 136 C ATOM 596 CD2 TYR B 79 -3.594 26.797 35.703 1.00 41.85 C ANISOU 596 CD2 TYR B 79 6963 4436 4501 -162 -700 232 C ATOM 597 CE1 TYR B 79 -1.593 26.638 37.615 1.00 41.75 C ANISOU 597 CE1 TYR B 79 6902 4400 4561 -279 -714 243 C ATOM 598 CE2 TYR B 79 -2.379 27.427 35.483 1.00 42.63 C ANISOU 598 CE2 TYR B 79 7089 4475 4633 -306 -760 350 C ATOM 599 CZ TYR B 79 -1.383 27.342 36.446 1.00 42.73 C ANISOU 599 CZ TYR B 79 7074 4478 4683 -367 -768 355 C ATOM 600 OH TYR B 79 -0.169 27.947 36.254 1.00 43.88 O ANISOU 600 OH TYR B 79 7233 4577 4861 -520 -832 480 O ATOM 601 N MET B 80 -6.559 22.819 38.657 1.00 38.45 N ANISOU 601 N MET B 80 6217 4417 3976 214 -377 -140 N ATOM 602 CA MET B 80 -7.858 22.521 39.255 1.00 38.42 C ANISOU 602 CA MET B 80 6173 4495 3929 334 -367 -222 C ATOM 603 C MET B 80 -8.006 23.342 40.530 1.00 39.59 C ANISOU 603 C MET B 80 6367 4608 4066 425 -453 -294 C ATOM 604 O MET B 80 -7.178 23.251 41.438 1.00 39.52 O ANISOU 604 O MET B 80 6348 4587 4080 392 -454 -297 O ATOM 605 CB MET B 80 -8.043 21.027 39.559 1.00 37.00 C ANISOU 605 CB MET B 80 5875 4443 3741 317 -258 -223 C ATOM 606 CG MET B 80 -9.403 20.727 40.197 1.00 36.96 C ANISOU 606 CG MET B 80 5812 4546 3684 425 -251 -287 C ATOM 607 SD MET B 80 -9.910 19.003 40.313 1.00 35.71 S ANISOU 607 SD MET B 80 5523 4529 3518 390 -150 -267 S ATOM 608 CE MET B 80 -8.650 18.355 41.407 1.00 35.32 C ANISOU 608 CE MET B 80 5436 4478 3505 320 -113 -248 C ATOM 609 N GLN B 81 -9.067 24.141 40.578 1.00 41.00 N ANISOU 609 N GLN B 81 6597 4777 4204 549 -530 -359 N ATOM 610 CA GLN B 81 -9.454 24.861 41.773 1.00 42.13 C ANISOU 610 CA GLN B 81 6776 4917 4314 678 -615 -452 C ATOM 611 C GLN B 81 -10.560 24.084 42.469 1.00 41.92 C ANISOU 611 C GLN B 81 6634 5076 4219 779 -548 -509 C ATOM 612 O GLN B 81 -11.617 23.851 41.884 1.00 41.69 O ANISOU 612 O GLN B 81 6564 5126 4149 830 -522 -517 O ATOM 613 CB GLN B 81 -9.949 26.249 41.403 1.00 44.10 C ANISOU 613 CB GLN B 81 7157 5048 4553 771 -757 -495 C ATOM 614 CG GLN B 81 -10.173 27.157 42.595 1.00 45.74 C ANISOU 614 CG GLN B 81 7430 5221 4728 915 -878 -603 C ATOM 615 CD GLN B 81 -10.222 28.608 42.181 1.00 47.87 C ANISOU 615 CD GLN B 81 7866 5308 5017 969 -1051 -628 C ATOM 616 OE1 GLN B 81 -11.232 29.089 41.659 1.00 49.18 O ANISOU 616 OE1 GLN B 81 8069 5475 5141 1078 -1102 -669 O ATOM 617 NE2 GLN B 81 -9.122 29.315 42.397 1.00 49.04 N ANISOU 617 NE2 GLN B 81 8115 5291 5228 888 -1152 -597 N ATOM 618 N LEU B 82 -10.293 23.667 43.707 1.00 42.10 N ANISOU 618 N LEU B 82 6597 5174 4225 799 -521 -539 N ATOM 619 CA LEU B 82 -11.291 23.057 44.596 1.00 42.24 C ANISOU 619 CA LEU B 82 6499 5385 4165 898 -473 -585 C ATOM 620 C LEU B 82 -11.674 24.085 45.660 1.00 43.15 C ANISOU 620 C LEU B 82 6663 5517 4217 1069 -577 -694 C ATOM 621 O LEU B 82 -10.794 24.736 46.229 1.00 43.17 O ANISOU 621 O LEU B 82 6748 5405 4250 1068 -651 -722 O ATOM 622 CB LEU B 82 -10.712 21.817 45.281 1.00 41.47 C ANISOU 622 CB LEU B 82 6297 5376 4084 804 -374 -535 C ATOM 623 CG LEU B 82 -10.252 20.670 44.386 1.00 40.53 C ANISOU 623 CG LEU B 82 6129 5246 4023 652 -280 -442 C ATOM 624 CD1 LEU B 82 -9.362 19.719 45.169 1.00 40.12 C ANISOU 624 CD1 LEU B 82 6015 5227 4001 567 -219 -403 C ATOM 625 CD2 LEU B 82 -11.448 19.935 43.801 1.00 40.64 C ANISOU 625 CD2 LEU B 82 6060 5380 4001 664 -229 -422 C ATOM 626 N SER B 82A -12.972 24.201 45.947 1.00 43.51 N ANISOU 626 N SER B 82A 6649 5714 4168 1219 -586 -758 N ATOM 627 CA SER B 82A -13.491 25.225 46.866 1.00 44.58 C ANISOU 627 CA SER B 82A 6829 5887 4223 1420 -695 -880 C ATOM 628 C SER B 82A -14.470 24.662 47.900 1.00 44.78 C ANISOU 628 C SER B 82A 6700 6184 4129 1539 -638 -920 C ATOM 629 O SER B 82A -15.026 23.576 47.712 1.00 43.90 O ANISOU 629 O SER B 82A 6452 6230 3998 1471 -527 -848 O ATOM 630 CB SER B 82A -14.149 26.351 46.065 1.00 45.30 C ANISOU 630 CB SER B 82A 7033 5879 4300 1531 -808 -938 C ATOM 631 OG SER B 82A -14.967 25.828 45.034 1.00 44.85 O ANISOU 631 OG SER B 82A 6911 5895 4234 1496 -738 -885 O ATOM 632 N SER B 82B -14.656 25.420 48.988 1.00 45.77 N ANISOU 632 N SER B 82B 6850 6366 4174 1716 -723 -1032 N ATOM 633 CA SER B 82B -15.537 25.056 50.113 1.00 46.26 C ANISOU 633 CA SER B 82B 6764 6712 4100 1857 -683 -1078 C ATOM 634 C SER B 82B -15.153 23.701 50.714 1.00 44.78 C ANISOU 634 C SER B 82B 6434 6659 3922 1712 -551 -975 C ATOM 635 O SER B 82B -15.998 22.825 50.914 1.00 44.19 O ANISOU 635 O SER B 82B 6198 6815 3777 1704 -462 -921 O ATOM 636 CB SER B 82B -17.010 25.063 49.681 1.00 47.04 C ANISOU 636 CB SER B 82B 6774 6995 4104 1975 -668 -1099 C ATOM 637 OG SER B 82B -17.366 26.307 49.111 1.00 48.44 O ANISOU 637 OG SER B 82B 7091 7041 4275 2116 -799 -1195 O ATOM 638 N LEU B 82C -13.863 23.551 50.999 1.00 43.72 N ANISOU 638 N LEU B 82C 6361 6376 3873 1593 -549 -944 N ATOM 639 CA LEU B 82C -13.299 22.253 51.354 1.00 42.64 C ANISOU 639 CA LEU B 82C 6121 6307 3775 1430 -435 -837 C ATOM 640 C LEU B 82C -13.781 21.740 52.716 1.00 42.91 C ANISOU 640 C LEU B 82C 6010 6603 3690 1513 -392 -845 C ATOM 641 O LEU B 82C -13.847 22.496 53.686 1.00 44.11 O ANISOU 641 O LEU B 82C 6184 6819 3759 1677 -463 -948 O ATOM 642 CB LEU B 82C -11.761 22.274 51.272 1.00 42.13 C ANISOU 642 CB LEU B 82C 6157 6020 3828 1291 -450 -804 C ATOM 643 CG LEU B 82C -11.187 21.852 49.916 1.00 41.40 C ANISOU 643 CG LEU B 82C 6112 5764 3854 1114 -408 -712 C ATOM 644 CD1 LEU B 82C -11.717 22.715 48.785 1.00 42.21 C ANISOU 644 CD1 LEU B 82C 6307 5762 3969 1162 -473 -743 C ATOM 645 CD2 LEU B 82C -9.671 21.888 49.929 1.00 41.06 C ANISOU 645 CD2 LEU B 82C 6148 5545 3910 989 -421 -679 C ATOM 646 N THR B 83 -14.145 20.460 52.747 1.00 42.12 N ANISOU 646 N THR B 83 5765 6658 3581 1399 -284 -732 N ATOM 647 CA THR B 83 -14.510 19.740 53.963 1.00 42.59 C ANISOU 647 CA THR B 83 5670 6972 3540 1424 -229 -694 C ATOM 648 C THR B 83 -13.484 18.627 54.158 1.00 41.50 C ANISOU 648 C THR B 83 5510 6763 3494 1230 -163 -586 C ATOM 649 O THR B 83 -12.623 18.427 53.303 1.00 39.89 O ANISOU 649 O THR B 83 5398 6341 3418 1096 -156 -549 O ATOM 650 CB THR B 83 -15.925 19.127 53.851 1.00 43.02 C ANISOU 650 CB THR B 83 5560 7286 3500 1444 -174 -632 C ATOM 651 OG1 THR B 83 -15.936 18.098 52.855 1.00 42.28 O ANISOU 651 OG1 THR B 83 5438 7121 3504 1251 -113 -512 O ATOM 652 CG2 THR B 83 -16.946 20.185 53.474 1.00 43.91 C ANISOU 652 CG2 THR B 83 5695 7459 3528 1634 -238 -738 C ATOM 653 N THR B 84 -13.589 17.894 55.264 1.00 42.23 N ANISOU 653 N THR B 84 5477 7053 3515 1219 -116 -531 N ATOM 654 CA THR B 84 -12.683 16.766 55.536 1.00 41.58 C ANISOU 654 CA THR B 84 5368 6920 3512 1045 -61 -425 C ATOM 655 C THR B 84 -12.819 15.651 54.507 1.00 40.92 C ANISOU 655 C THR B 84 5252 6776 3518 867 -8 -307 C ATOM 656 O THR B 84 -11.847 14.942 54.238 1.00 39.90 O ANISOU 656 O THR B 84 5166 6499 3496 726 14 -248 O ATOM 657 CB THR B 84 -12.913 16.136 56.924 1.00 42.41 C ANISOU 657 CB THR B 84 5331 7271 3511 1064 -24 -372 C ATOM 658 OG1 THR B 84 -14.258 15.648 57.012 1.00 43.34 O ANISOU 658 OG1 THR B 84 5292 7647 3526 1082 12 -303 O ATOM 659 CG2 THR B 84 -12.642 17.144 58.036 1.00 43.20 C ANISOU 659 CG2 THR B 84 5465 7431 3518 1243 -81 -495 C ATOM 660 N GLU B 85 -14.014 15.502 53.932 1.00 41.59 N ANISOU 660 N GLU B 85 5265 6978 3560 882 5 -277 N ATOM 661 CA GLU B 85 -14.254 14.493 52.893 1.00 41.37 C ANISOU 661 CA GLU B 85 5214 6891 3614 725 37 -176 C ATOM 662 C GLU B 85 -13.552 14.802 51.556 1.00 39.56 C ANISOU 662 C GLU B 85 5131 6394 3506 670 19 -211 C ATOM 663 O GLU B 85 -13.414 13.915 50.718 1.00 38.74 O ANISOU 663 O GLU B 85 5032 6203 3484 537 40 -139 O ATOM 664 CB GLU B 85 -15.758 14.283 52.678 1.00 43.20 C ANISOU 664 CB GLU B 85 5319 7336 3759 756 48 -133 C ATOM 665 CG GLU B 85 -16.512 13.897 53.952 1.00 45.24 C ANISOU 665 CG GLU B 85 5405 7900 3882 796 71 -74 C ATOM 666 CD GLU B 85 -17.240 12.567 53.838 1.00 46.35 C ANISOU 666 CD GLU B 85 5409 8177 4026 639 101 87 C ATOM 667 OE1 GLU B 85 -16.559 11.543 53.587 1.00 46.08 O ANISOU 667 OE1 GLU B 85 5406 8002 4102 470 108 174 O ATOM 668 OE2 GLU B 85 -18.484 12.546 54.013 1.00 48.23 O ANISOU 668 OE2 GLU B 85 5506 8665 4153 686 108 127 O ATOM 669 N ASP B 86 -13.112 16.050 51.370 1.00 38.82 N ANISOU 669 N ASP B 86 5156 6175 3420 772 -30 -319 N ATOM 670 CA ASP B 86 -12.252 16.439 50.243 1.00 37.46 C ANISOU 670 CA ASP B 86 5121 5757 3355 714 -51 -341 C ATOM 671 C ASP B 86 -10.755 16.172 50.477 1.00 36.29 C ANISOU 671 C ASP B 86 5035 5461 3291 621 -43 -324 C ATOM 672 O ASP B 86 -9.935 16.476 49.604 1.00 35.79 O ANISOU 672 O ASP B 86 5072 5218 3310 566 -57 -331 O ATOM 673 CB ASP B 86 -12.468 17.920 49.890 1.00 37.86 C ANISOU 673 CB ASP B 86 5275 5731 3380 849 -124 -448 C ATOM 674 CG ASP B 86 -13.915 18.235 49.540 1.00 38.52 C ANISOU 674 CG ASP B 86 5303 5952 3381 953 -137 -473 C ATOM 675 OD1 ASP B 86 -14.552 17.433 48.825 1.00 38.32 O ANISOU 675 OD1 ASP B 86 5211 5980 3370 875 -94 -403 O ATOM 676 OD2 ASP B 86 -14.420 19.283 49.981 1.00 38.90 O ANISOU 676 OD2 ASP B 86 5375 6057 3349 1119 -198 -568 O ATOM 677 N SER B 87 -10.392 15.614 51.633 1.00 35.93 N ANISOU 677 N SER B 87 4926 5504 3221 603 -21 -295 N ATOM 678 CA SER B 87 -9.021 15.152 51.865 1.00 35.12 C ANISOU 678 CA SER B 87 4863 5283 3197 507 -7 -266 C ATOM 679 C SER B 87 -8.761 13.899 51.036 1.00 34.36 C ANISOU 679 C SER B 87 4748 5128 3180 365 36 -178 C ATOM 680 O SER B 87 -9.434 12.886 51.228 1.00 34.95 O ANISOU 680 O SER B 87 4729 5315 3234 315 62 -105 O ATOM 681 CB SER B 87 -8.780 14.838 53.343 1.00 35.35 C ANISOU 681 CB SER B 87 4824 5435 3171 531 2 -255 C ATOM 682 OG SER B 87 -8.940 15.992 54.144 1.00 36.12 O ANISOU 682 OG SER B 87 4948 5586 3191 677 -50 -352 O ATOM 683 N ALA B 88 -7.796 13.975 50.120 1.00 33.49 N ANISOU 683 N ALA B 88 4723 4846 3154 303 34 -182 N ATOM 684 CA ALA B 88 -7.487 12.870 49.201 1.00 32.51 C ANISOU 684 CA ALA B 88 4597 4656 3100 194 63 -120 C ATOM 685 C ALA B 88 -6.226 13.159 48.378 1.00 31.67 C ANISOU 685 C ALA B 88 4578 4391 3065 150 61 -136 C ATOM 686 O ALA B 88 -5.693 14.269 48.421 1.00 31.19 O ANISOU 686 O ALA B 88 4582 4264 3005 189 32 -183 O ATOM 687 CB ALA B 88 -8.668 12.619 48.268 1.00 32.59 C ANISOU 687 CB ALA B 88 4581 4705 3095 192 65 -102 C ATOM 688 N ILE B 89 -5.752 12.141 47.655 1.00 31.53 N ANISOU 688 N ILE B 89 4558 4319 3101 71 83 -94 N ATOM 689 CA ILE B 89 -4.762 12.320 46.578 1.00 31.39 C ANISOU 689 CA ILE B 89 4604 4188 3133 36 88 -101 C ATOM 690 C ILE B 89 -5.505 12.718 45.300 1.00 31.27 C ANISOU 690 C ILE B 89 4622 4149 3110 53 81 -112 C ATOM 691 O ILE B 89 -6.504 12.087 44.929 1.00 31.05 O ANISOU 691 O ILE B 89 4558 4168 3069 49 84 -95 O ATOM 692 CB ILE B 89 -3.951 11.034 46.270 1.00 31.35 C ANISOU 692 CB ILE B 89 4584 4149 3176 -30 107 -66 C ATOM 693 CG1 ILE B 89 -3.209 10.523 47.514 1.00 31.34 C ANISOU 693 CG1 ILE B 89 4551 4171 3185 -49 110 -48 C ATOM 694 CG2 ILE B 89 -2.952 11.287 45.138 1.00 31.14 C ANISOU 694 CG2 ILE B 89 4608 4045 3180 -50 117 -74 C ATOM 695 CD1 ILE B 89 -2.684 9.106 47.376 1.00 31.11 C ANISOU 695 CD1 ILE B 89 4504 4119 3198 -98 112 -14 C ATOM 696 N TYR B 90 -4.999 13.757 44.636 1.00 31.13 N ANISOU 696 N TYR B 90 4671 4058 3100 63 67 -133 N ATOM 697 CA TYR B 90 -5.579 14.277 43.402 1.00 31.28 C ANISOU 697 CA TYR B 90 4730 4047 3109 80 56 -140 C ATOM 698 C TYR B 90 -4.566 14.150 42.269 1.00 31.25 C ANISOU 698 C TYR B 90 4757 3980 3135 27 73 -116 C ATOM 699 O TYR B 90 -3.466 14.695 42.357 1.00 31.54 O ANISOU 699 O TYR B 90 4822 3973 3190 -2 67 -106 O ATOM 700 CB TYR B 90 -6.021 15.732 43.592 1.00 31.38 C ANISOU 700 CB TYR B 90 4795 4036 3091 146 6 -179 C ATOM 701 CG TYR B 90 -7.253 15.866 44.470 1.00 31.58 C ANISOU 701 CG TYR B 90 4779 4158 3062 227 -10 -211 C ATOM 702 CD1 TYR B 90 -7.137 15.999 45.855 1.00 31.61 C ANISOU 702 CD1 TYR B 90 4755 4215 3042 265 -21 -234 C ATOM 703 CD2 TYR B 90 -8.541 15.848 43.915 1.00 31.38 C ANISOU 703 CD2 TYR B 90 4732 4191 3001 270 -14 -219 C ATOM 704 CE1 TYR B 90 -8.265 16.119 46.665 1.00 32.11 C ANISOU 704 CE1 TYR B 90 4763 4401 3037 349 -33 -262 C ATOM 705 CE2 TYR B 90 -9.674 15.966 44.714 1.00 31.88 C ANISOU 705 CE2 TYR B 90 4737 4375 3001 349 -26 -244 C ATOM 706 CZ TYR B 90 -9.535 16.101 46.089 1.00 32.35 C ANISOU 706 CZ TYR B 90 4763 4501 3027 391 -33 -264 C ATOM 707 OH TYR B 90 -10.653 16.215 46.891 1.00 32.60 O ANISOU 707 OH TYR B 90 4722 4685 2978 480 -41 -287 O ATOM 708 N TYR B 91 -4.940 13.414 41.222 1.00 31.24 N ANISOU 708 N TYR B 91 4746 3988 3135 15 90 -106 N ATOM 709 CA TYR B 91 -4.073 13.164 40.069 1.00 31.31 C ANISOU 709 CA TYR B 91 4773 3970 3155 -16 110 -89 C ATOM 710 C TYR B 91 -4.515 13.956 38.859 1.00 31.59 C ANISOU 710 C TYR B 91 4851 3986 3164 -1 98 -85 C ATOM 711 O TYR B 91 -5.713 14.118 38.637 1.00 31.74 O ANISOU 711 O TYR B 91 4877 4020 3165 36 80 -102 O ATOM 712 CB TYR B 91 -4.134 11.693 39.667 1.00 31.15 C ANISOU 712 CB TYR B 91 4719 3971 3146 -26 124 -90 C ATOM 713 CG TYR B 91 -3.625 10.716 40.699 1.00 30.90 C ANISOU 713 CG TYR B 91 4649 3949 3143 -46 128 -85 C ATOM 714 CD1 TYR B 91 -2.253 10.491 40.859 1.00 30.84 C ANISOU 714 CD1 TYR B 91 4636 3932 3151 -65 145 -79 C ATOM 715 CD2 TYR B 91 -4.512 9.977 41.482 1.00 30.88 C ANISOU 715 CD2 TYR B 91 4610 3975 3147 -51 110 -77 C ATOM 716 CE1 TYR B 91 -1.779 9.579 41.790 1.00 30.82 C ANISOU 716 CE1 TYR B 91 4602 3934 3173 -78 142 -74 C ATOM 717 CE2 TYR B 91 -4.049 9.064 42.420 1.00 31.08 C ANISOU 717 CE2 TYR B 91 4605 4006 3198 -76 105 -61 C ATOM 718 CZ TYR B 91 -2.681 8.869 42.573 1.00 31.09 C ANISOU 718 CZ TYR B 91 4612 3984 3219 -85 120 -64 C ATOM 719 OH TYR B 91 -2.214 7.964 43.495 1.00 31.55 O ANISOU 719 OH TYR B 91 4644 4043 3301 -104 110 -49 O ATOM 720 N CYS B 92 -3.544 14.417 38.067 1.00 31.89 N ANISOU 720 N CYS B 92 4913 4006 3199 -31 106 -56 N ATOM 721 CA CYS B 92 -3.790 14.863 36.695 1.00 32.22 C ANISOU 721 CA CYS B 92 4985 4045 3210 -27 103 -38 C ATOM 722 C CYS B 92 -3.310 13.751 35.759 1.00 31.69 C ANISOU 722 C CYS B 92 4886 4027 3129 -28 138 -39 C ATOM 723 O CYS B 92 -2.259 13.125 35.987 1.00 31.05 O ANISOU 723 O CYS B 92 4771 3970 3057 -46 163 -33 O ATOM 724 CB CYS B 92 -3.092 16.192 36.372 1.00 33.34 C ANISOU 724 CB CYS B 92 5172 4149 3345 -64 77 10 C ATOM 725 SG CYS B 92 -1.290 16.153 36.508 1.00 34.71 S ANISOU 725 SG CYS B 92 5311 4347 3529 -136 102 63 S ATOM 726 N ALA B 93 -4.106 13.493 34.725 1.00 30.95 N ANISOU 726 N ALA B 93 4803 3948 3009 3 134 -53 N ATOM 727 CA ALA B 93 -3.798 12.471 33.741 1.00 30.58 C ANISOU 727 CA ALA B 93 4736 3944 2938 23 152 -69 C ATOM 728 C ALA B 93 -4.218 12.965 32.365 1.00 30.37 C ANISOU 728 C ALA B 93 4736 3939 2862 43 148 -57 C ATOM 729 O ALA B 93 -5.183 13.728 32.244 1.00 30.25 O ANISOU 729 O ALA B 93 4755 3896 2844 52 123 -53 O ATOM 730 CB ALA B 93 -4.507 11.172 34.088 1.00 30.30 C ANISOU 730 CB ALA B 93 4682 3900 2929 45 133 -114 C ATOM 731 N ARG B 94 -3.491 12.540 31.335 1.00 30.11 N ANISOU 731 N ARG B 94 4687 3969 2785 61 171 -53 N ATOM 732 CA ARG B 94 -3.740 13.031 29.983 1.00 30.35 C ANISOU 732 CA ARG B 94 4736 4040 2757 79 172 -32 C ATOM 733 C ARG B 94 -4.179 11.928 29.021 1.00 30.08 C ANISOU 733 C ARG B 94 4698 4044 2689 144 162 -91 C ATOM 734 O ARG B 94 -3.747 10.776 29.131 1.00 29.90 O ANISOU 734 O ARG B 94 4652 4037 2672 177 160 -139 O ATOM 735 CB ARG B 94 -2.528 13.801 29.443 1.00 30.92 C ANISOU 735 CB ARG B 94 4789 4178 2782 40 201 42 C ATOM 736 CG ARG B 94 -1.304 12.970 29.106 1.00 31.28 C ANISOU 736 CG ARG B 94 4774 4324 2786 63 239 35 C ATOM 737 CD ARG B 94 -0.121 13.883 28.827 1.00 31.98 C ANISOU 737 CD ARG B 94 4828 4491 2834 0 265 132 C ATOM 738 NE ARG B 94 1.103 13.136 28.510 1.00 32.60 N ANISOU 738 NE ARG B 94 4832 4698 2858 31 306 128 N ATOM 739 CZ ARG B 94 1.589 12.891 27.289 1.00 33.34 C ANISOU 739 CZ ARG B 94 4880 4936 2854 79 334 141 C ATOM 740 NH1 ARG B 94 0.983 13.335 26.193 1.00 33.94 N ANISOU 740 NH1 ARG B 94 4979 5043 2874 92 328 166 N ATOM 741 NH2 ARG B 94 2.714 12.192 27.161 1.00 33.81 N ANISOU 741 NH2 ARG B 94 4864 5121 2861 123 367 126 N ATOM 742 N HIS B 95 -5.076 12.310 28.114 1.00 29.91 N ANISOU 742 N HIS B 95 4705 4025 2633 167 144 -92 N ATOM 743 CA HIS B 95 -5.507 11.494 26.989 1.00 30.10 C ANISOU 743 CA HIS B 95 4734 4090 2613 231 126 -143 C ATOM 744 C HIS B 95 -4.746 12.006 25.775 1.00 30.64 C ANISOU 744 C HIS B 95 4790 4259 2592 248 158 -100 C ATOM 745 O HIS B 95 -5.049 13.075 25.252 1.00 30.72 O ANISOU 745 O HIS B 95 4824 4277 2573 224 159 -43 O ATOM 746 CB HIS B 95 -7.021 11.633 26.780 1.00 29.91 C ANISOU 746 CB HIS B 95 4743 4018 2605 243 84 -165 C ATOM 747 CG HIS B 95 -7.534 11.020 25.515 1.00 30.22 C ANISOU 747 CG HIS B 95 4795 4095 2593 304 57 -211 C ATOM 748 ND1 HIS B 95 -8.845 11.149 25.114 1.00 30.19 N ANISOU 748 ND1 HIS B 95 4814 4067 2589 318 17 -228 N ATOM 749 CD2 HIS B 95 -6.914 10.307 24.545 1.00 30.82 C ANISOU 749 CD2 HIS B 95 4862 4241 2608 364 58 -249 C ATOM 750 CE1 HIS B 95 -9.015 10.531 23.960 1.00 30.70 C ANISOU 750 CE1 HIS B 95 4890 4173 2603 376 -7 -273 C ATOM 751 NE2 HIS B 95 -7.857 10.017 23.592 1.00 31.16 N ANISOU 751 NE2 HIS B 95 4931 4290 2620 411 16 -290 N ATOM 752 N ASP B 96 -3.756 11.224 25.351 1.00 31.02 N ANISOU 752 N ASP B 96 4800 4394 2592 295 179 -127 N ATOM 753 CA ASP B 96 -2.982 11.480 24.138 1.00 31.96 C ANISOU 753 CA ASP B 96 4886 4653 2605 328 213 -92 C ATOM 754 C ASP B 96 -3.864 11.182 22.914 1.00 32.28 C ANISOU 754 C ASP B 96 4955 4723 2588 400 183 -140 C ATOM 755 O ASP B 96 -3.805 10.103 22.329 1.00 32.38 O ANISOU 755 O ASP B 96 4962 4779 2559 492 160 -225 O ATOM 756 CB ASP B 96 -1.709 10.618 24.178 1.00 32.39 C ANISOU 756 CB ASP B 96 4882 4805 2621 379 239 -125 C ATOM 757 CG ASP B 96 -0.707 10.965 23.093 1.00 33.51 C ANISOU 757 CG ASP B 96 4961 5131 2638 407 286 -71 C ATOM 758 OD1 ASP B 96 -0.870 11.984 22.383 1.00 33.79 O ANISOU 758 OD1 ASP B 96 4998 5217 2624 363 301 15 O ATOM 759 OD2 ASP B 96 0.270 10.198 22.968 1.00 33.97 O ANISOU 759 OD2 ASP B 96 4965 5298 2645 476 304 -111 O ATOM 760 N TYR B 97 -4.687 12.169 22.561 1.00 32.38 N ANISOU 760 N TYR B 97 5003 4701 2598 363 173 -88 N ATOM 761 CA TYR B 97 -5.752 12.031 21.550 1.00 32.97 C ANISOU 761 CA TYR B 97 5113 4780 2634 418 136 -128 C ATOM 762 C TYR B 97 -5.248 11.645 20.152 1.00 34.04 C ANISOU 762 C TYR B 97 5222 5065 2646 503 150 -148 C ATOM 763 O TYR B 97 -5.940 10.932 19.424 1.00 33.98 O ANISOU 763 O TYR B 97 5238 5063 2610 581 108 -228 O ATOM 764 CB TYR B 97 -6.592 13.326 21.481 1.00 32.89 C ANISOU 764 CB TYR B 97 5145 4713 2639 363 123 -58 C ATOM 765 CG TYR B 97 -7.762 13.282 20.512 1.00 33.15 C ANISOU 765 CG TYR B 97 5213 4746 2636 416 84 -94 C ATOM 766 CD1 TYR B 97 -8.679 12.231 20.542 1.00 32.91 C ANISOU 766 CD1 TYR B 97 5196 4668 2639 465 36 -192 C ATOM 767 CD2 TYR B 97 -7.953 14.294 19.564 1.00 33.74 C ANISOU 767 CD2 TYR B 97 5308 4869 2644 409 85 -22 C ATOM 768 CE1 TYR B 97 -9.747 12.181 19.655 1.00 33.09 C ANISOU 768 CE1 TYR B 97 5247 4694 2630 510 -6 -224 C ATOM 769 CE2 TYR B 97 -9.019 14.254 18.675 1.00 33.86 C ANISOU 769 CE2 TYR B 97 5353 4888 2623 461 48 -57 C ATOM 770 CZ TYR B 97 -9.913 13.195 18.726 1.00 33.63 C ANISOU 770 CZ TYR B 97 5334 4816 2629 513 4 -161 C ATOM 771 OH TYR B 97 -10.974 13.143 17.854 1.00 33.74 O ANISOU 771 OH TYR B 97 5374 4836 2609 561 -40 -196 O ATOM 772 N TYR B 98 -4.049 12.108 19.802 1.00 34.97 N ANISOU 772 N TYR B 98 5285 5315 2689 488 205 -72 N ATOM 773 CA TYR B 98 -3.420 11.781 18.522 1.00 36.41 C ANISOU 773 CA TYR B 98 5420 5682 2733 576 228 -81 C ATOM 774 C TYR B 98 -2.491 10.571 18.584 1.00 36.87 C ANISOU 774 C TYR B 98 5431 5825 2753 672 235 -171 C ATOM 775 O TYR B 98 -2.404 9.826 17.609 1.00 37.89 O ANISOU 775 O TYR B 98 5549 6063 2786 795 219 -250 O ATOM 776 CB TYR B 98 -2.714 13.011 17.941 1.00 37.31 C ANISOU 776 CB TYR B 98 5488 5924 2763 505 278 68 C ATOM 777 CG TYR B 98 -3.729 14.022 17.467 1.00 37.64 C ANISOU 777 CG TYR B 98 5590 5901 2810 456 250 132 C ATOM 778 CD1 TYR B 98 -4.287 14.943 18.349 1.00 37.12 C ANISOU 778 CD1 TYR B 98 5580 5673 2851 356 223 187 C ATOM 779 CD2 TYR B 98 -4.191 14.011 16.151 1.00 38.63 C ANISOU 779 CD2 TYR B 98 5722 6124 2834 526 240 123 C ATOM 780 CE1 TYR B 98 -5.243 15.854 17.931 1.00 37.17 C ANISOU 780 CE1 TYR B 98 5647 5615 2863 328 186 235 C ATOM 781 CE2 TYR B 98 -5.150 14.917 15.722 1.00 38.69 C ANISOU 781 CE2 TYR B 98 5787 6067 2847 488 208 178 C ATOM 782 CZ TYR B 98 -5.673 15.831 16.616 1.00 37.95 C ANISOU 782 CZ TYR B 98 5749 5808 2861 391 179 233 C ATOM 783 OH TYR B 98 -6.621 16.724 16.188 1.00 38.29 O ANISOU 783 OH TYR B 98 5854 5787 2908 369 138 279 O ATOM 784 N GLY B 99 -1.825 10.362 19.718 1.00 36.26 N ANISOU 784 N GLY B 99 5332 5698 2748 628 250 -167 N ATOM 785 CA GLY B 99 -0.862 9.263 19.867 1.00 36.64 C ANISOU 785 CA GLY B 99 5335 5823 2763 721 252 -248 C ATOM 786 C GLY B 99 -1.490 7.914 20.185 1.00 36.24 C ANISOU 786 C GLY B 99 5346 5645 2779 804 172 -391 C ATOM 787 O GLY B 99 -1.087 6.895 19.625 1.00 37.09 O ANISOU 787 O GLY B 99 5446 5828 2819 938 138 -494 O ATOM 788 N THR B 100 -2.444 7.910 21.116 1.00 35.17 N ANISOU 788 N THR B 100 5270 5322 2773 725 132 -396 N ATOM 789 CA THR B 100 -3.234 6.720 21.458 1.00 34.82 C ANISOU 789 CA THR B 100 5286 5140 2805 767 41 -504 C ATOM 790 C THR B 100 -4.684 7.145 21.691 1.00 33.86 C ANISOU 790 C THR B 100 5215 4890 2760 689 7 -479 C ATOM 791 O THR B 100 -5.098 7.398 22.826 1.00 32.71 O ANISOU 791 O THR B 100 5078 4637 2713 597 7 -441 O ATOM 792 CB THR B 100 -2.675 6.008 22.710 1.00 34.64 C ANISOU 792 CB THR B 100 5259 5037 2866 747 24 -529 C ATOM 793 OG1 THR B 100 -1.278 5.752 22.533 1.00 35.50 O ANISOU 793 OG1 THR B 100 5309 5282 2897 820 64 -542 O ATOM 794 CG2 THR B 100 -3.399 4.688 22.951 1.00 34.73 C ANISOU 794 CG2 THR B 100 5335 4914 2949 790 -87 -630 C ATOM 795 N SER B 100A -5.443 7.238 20.601 1.00 34.02 N ANISOU 795 N SER B 100A 5261 4939 2724 734 -21 -504 N ATOM 796 CA SER B 100A -6.803 7.770 20.651 1.00 33.63 C ANISOU 796 CA SER B 100A 5248 4802 2727 671 -47 -476 C ATOM 797 C SER B 100A -7.739 6.800 21.371 1.00 33.26 C ANISOU 797 C SER B 100A 5238 4616 2784 649 -133 -534 C ATOM 798 O SER B 100A -7.581 5.586 21.268 1.00 34.06 O ANISOU 798 O SER B 100A 5361 4685 2894 711 -204 -620 O ATOM 799 CB SER B 100A -7.327 8.091 19.246 1.00 34.16 C ANISOU 799 CB SER B 100A 5331 4948 2701 731 -58 -486 C ATOM 800 OG SER B 100A -8.328 9.089 19.302 1.00 33.79 O ANISOU 800 OG SER B 100A 5303 4853 2684 662 -52 -422 O ATOM 801 N GLY B 100B -8.722 7.352 22.079 1.00 32.61 N ANISOU 801 N GLY B 100B 5161 4458 2774 562 -136 -484 N ATOM 802 CA GLY B 100B -9.583 6.600 22.999 1.00 32.19 C ANISOU 802 CA GLY B 100B 5119 4294 2819 509 -204 -503 C ATOM 803 C GLY B 100B -8.979 5.948 24.234 1.00 31.73 C ANISOU 803 C GLY B 100B 5046 4177 2832 470 -210 -501 C ATOM 804 O GLY B 100B -9.565 5.000 24.766 1.00 31.73 O ANISOU 804 O GLY B 100B 5060 4096 2902 440 -289 -525 O ATOM 805 N ALA B 100C -7.820 6.431 24.684 1.00 31.29 N ANISOU 805 N ALA B 100C 4962 4166 2761 464 -136 -466 N ATOM 806 CA ALA B 100C -7.203 5.991 25.943 1.00 30.92 C ANISOU 806 CA ALA B 100C 4897 4071 2779 423 -131 -454 C ATOM 807 C ALA B 100C -7.124 7.202 26.874 1.00 30.19 C ANISOU 807 C ALA B 100C 4775 3983 2711 346 -58 -371 C ATOM 808 O ALA B 100C -6.266 8.068 26.694 1.00 30.24 O ANISOU 808 O ALA B 100C 4763 4052 2673 346 8 -330 O ATOM 809 CB ALA B 100C -5.818 5.425 25.687 1.00 31.34 C ANISOU 809 CB ALA B 100C 4941 4178 2788 495 -117 -496 C ATOM 810 N TRP B 100D -8.010 7.246 27.871 1.00 29.65 N ANISOU 810 N TRP B 100D 4700 3856 2710 281 -79 -343 N ATOM 811 CA TRP B 100D -8.269 8.472 28.643 1.00 28.94 C ANISOU 811 CA TRP B 100D 4593 3769 2634 230 -30 -282 C ATOM 812 C TRP B 100D -7.173 8.929 29.613 1.00 28.12 C ANISOU 812 C TRP B 100D 4468 3668 2547 198 21 -246 C ATOM 813 O TRP B 100D -6.901 10.129 29.697 1.00 27.24 O ANISOU 813 O TRP B 100D 4359 3574 2418 180 62 -201 O ATOM 814 CB TRP B 100D -9.633 8.388 29.360 1.00 29.06 C ANISOU 814 CB TRP B 100D 4593 3752 2694 189 -69 -268 C ATOM 815 CG TRP B 100D -10.741 8.669 28.414 1.00 29.55 C ANISOU 815 CG TRP B 100D 4670 3831 2725 212 -98 -280 C ATOM 816 CD1 TRP B 100D -11.583 7.763 27.835 1.00 30.17 C ANISOU 816 CD1 TRP B 100D 4756 3896 2811 220 -167 -313 C ATOM 817 CD2 TRP B 100D -11.093 9.948 27.881 1.00 29.66 C ANISOU 817 CD2 TRP B 100D 4699 3876 2695 232 -69 -256 C ATOM 818 NE1 TRP B 100D -12.453 8.406 26.982 1.00 30.55 N ANISOU 818 NE1 TRP B 100D 4814 3974 2818 246 -174 -315 N ATOM 819 CE2 TRP B 100D -12.174 9.748 26.992 1.00 30.13 C ANISOU 819 CE2 TRP B 100D 4768 3947 2732 257 -114 -280 C ATOM 820 CE3 TRP B 100D -10.606 11.250 28.079 1.00 29.51 C ANISOU 820 CE3 TRP B 100D 4692 3864 2655 228 -22 -215 C ATOM 821 CZ2 TRP B 100D -12.778 10.801 26.300 1.00 30.27 C ANISOU 821 CZ2 TRP B 100D 4805 3991 2705 286 -107 -265 C ATOM 822 CZ3 TRP B 100D -11.202 12.297 27.394 1.00 29.77 C ANISOU 822 CZ3 TRP B 100D 4753 3911 2649 252 -26 -198 C ATOM 823 CH2 TRP B 100D -12.276 12.067 26.508 1.00 30.14 C ANISOU 823 CH2 TRP B 100D 4807 3976 2670 285 -64 -224 C ATOM 824 N PHE B 100E -6.566 7.989 30.342 1.00 27.92 N ANISOU 824 N PHE B 100E 4429 3618 2561 190 8 -263 N ATOM 825 CA PHE B 100E -5.546 8.313 31.353 1.00 27.64 C ANISOU 825 CA PHE B 100E 4370 3586 2547 159 50 -232 C ATOM 826 C PHE B 100E -4.239 7.587 31.012 1.00 28.06 C ANISOU 826 C PHE B 100E 4413 3672 2577 202 59 -262 C ATOM 827 O PHE B 100E -3.730 6.765 31.776 1.00 27.89 O ANISOU 827 O PHE B 100E 4381 3622 2593 199 41 -278 O ATOM 828 CB PHE B 100E -6.039 7.980 32.777 1.00 27.23 C ANISOU 828 CB PHE B 100E 4299 3489 2558 110 30 -215 C ATOM 829 CG PHE B 100E -7.504 8.275 33.013 1.00 27.00 C ANISOU 829 CG PHE B 100E 4266 3454 2541 88 4 -201 C ATOM 830 CD1 PHE B 100E -8.020 9.552 32.812 1.00 26.94 C ANISOU 830 CD1 PHE B 100E 4266 3466 2503 95 28 -181 C ATOM 831 CD2 PHE B 100E -8.367 7.276 33.457 1.00 27.01 C ANISOU 831 CD2 PHE B 100E 4250 3433 2580 60 -52 -201 C ATOM 832 CE1 PHE B 100E -9.370 9.817 33.038 1.00 26.94 C ANISOU 832 CE1 PHE B 100E 4253 3479 2504 91 3 -174 C ATOM 833 CE2 PHE B 100E -9.711 7.532 33.676 1.00 27.22 C ANISOU 833 CE2 PHE B 100E 4253 3483 2607 39 -73 -180 C ATOM 834 CZ PHE B 100E -10.216 8.807 33.466 1.00 27.02 C ANISOU 834 CZ PHE B 100E 4230 3493 2544 64 -42 -172 C ATOM 835 N ALA B 101 -3.698 7.921 29.847 1.00 28.73 N ANISOU 835 N ALA B 101 4497 3829 2590 247 86 -267 N ATOM 836 CA ALA B 101 -2.517 7.243 29.305 1.00 29.52 C ANISOU 836 CA ALA B 101 4577 3997 2642 314 94 -304 C ATOM 837 C ALA B 101 -1.224 7.599 30.045 1.00 29.67 C ANISOU 837 C ALA B 101 4551 4060 2663 285 145 -264 C ATOM 838 O ALA B 101 -0.328 6.771 30.146 1.00 29.89 O ANISOU 838 O ALA B 101 4558 4120 2680 336 138 -302 O ATOM 839 CB ALA B 101 -2.376 7.543 27.816 1.00 30.15 C ANISOU 839 CB ALA B 101 4654 4175 2628 374 112 -312 C ATOM 840 N TYR B 102 -1.123 8.838 30.523 1.00 29.90 N ANISOU 840 N TYR B 102 4568 4088 2703 210 186 -190 N ATOM 841 CA TYR B 102 0.029 9.298 31.317 1.00 30.26 C ANISOU 841 CA TYR B 102 4575 4164 2759 165 223 -143 C ATOM 842 C TYR B 102 -0.459 10.125 32.505 1.00 29.81 C ANISOU 842 C TYR B 102 4537 4023 2768 88 219 -102 C ATOM 843 O TYR B 102 -1.384 10.932 32.374 1.00 29.86 O ANISOU 843 O TYR B 102 4577 3990 2779 65 207 -81 O ATOM 844 CB TYR B 102 0.995 10.132 30.461 1.00 30.89 C ANISOU 844 CB TYR B 102 4613 4361 2761 153 270 -81 C ATOM 845 CG TYR B 102 1.380 9.458 29.169 1.00 31.67 C ANISOU 845 CG TYR B 102 4686 4576 2771 245 278 -121 C ATOM 846 CD1 TYR B 102 2.437 8.548 29.125 1.00 32.19 C ANISOU 846 CD1 TYR B 102 4704 4728 2801 316 286 -165 C ATOM 847 CD2 TYR B 102 0.673 9.710 27.992 1.00 31.91 C ANISOU 847 CD2 TYR B 102 4740 4637 2748 275 271 -124 C ATOM 848 CE1 TYR B 102 2.788 7.917 27.942 1.00 33.08 C ANISOU 848 CE1 TYR B 102 4791 4960 2818 425 286 -216 C ATOM 849 CE2 TYR B 102 1.013 9.082 26.804 1.00 32.80 C ANISOU 849 CE2 TYR B 102 4828 4867 2766 374 274 -169 C ATOM 850 CZ TYR B 102 2.072 8.187 26.785 1.00 33.43 C ANISOU 850 CZ TYR B 102 4859 5037 2805 454 281 -219 C ATOM 851 OH TYR B 102 2.413 7.552 25.613 1.00 34.58 O ANISOU 851 OH TYR B 102 4980 5314 2845 575 277 -278 O ATOM 852 N TRP B 103 0.199 9.937 33.643 1.00 29.81 N ANISOU 852 N TRP B 103 4514 4004 2808 61 224 -97 N ATOM 853 CA TRP B 103 -0.251 10.468 34.927 1.00 29.46 C ANISOU 853 CA TRP B 103 4484 3887 2820 10 212 -78 C ATOM 854 C TRP B 103 0.817 11.357 35.563 1.00 29.79 C ANISOU 854 C TRP B 103 4505 3944 2868 -44 232 -27 C ATOM 855 O TRP B 103 2.016 11.189 35.315 1.00 29.85 O ANISOU 855 O TRP B 103 4471 4022 2850 -45 257 -9 O ATOM 856 CB TRP B 103 -0.558 9.304 35.876 1.00 29.12 C ANISOU 856 CB TRP B 103 4437 3801 2826 24 186 -117 C ATOM 857 CG TRP B 103 -1.761 8.472 35.493 1.00 29.29 C ANISOU 857 CG TRP B 103 4481 3788 2857 52 145 -154 C ATOM 858 CD1 TRP B 103 -1.897 7.673 34.390 1.00 29.69 C ANISOU 858 CD1 TRP B 103 4546 3853 2882 104 122 -195 C ATOM 859 CD2 TRP B 103 -2.986 8.340 36.234 1.00 29.05 C ANISOU 859 CD2 TRP B 103 4459 3716 2864 28 114 -150 C ATOM 860 NE1 TRP B 103 -3.137 7.068 34.391 1.00 29.76 N ANISOU 860 NE1 TRP B 103 4576 3814 2918 102 72 -214 N ATOM 861 CE2 TRP B 103 -3.821 7.454 35.513 1.00 29.29 C ANISOU 861 CE2 TRP B 103 4506 3729 2895 52 70 -180 C ATOM 862 CE3 TRP B 103 -3.461 8.889 37.432 1.00 28.62 C ANISOU 862 CE3 TRP B 103 4391 3649 2832 -6 116 -125 C ATOM 863 CZ2 TRP B 103 -5.107 7.105 35.955 1.00 29.34 C ANISOU 863 CZ2 TRP B 103 4508 3713 2928 25 30 -171 C ATOM 864 CZ3 TRP B 103 -4.743 8.533 37.875 1.00 28.56 C ANISOU 864 CZ3 TRP B 103 4375 3637 2840 -18 84 -121 C ATOM 865 CH2 TRP B 103 -5.548 7.653 37.136 1.00 28.82 C ANISOU 865 CH2 TRP B 103 4416 3659 2877 -10 43 -136 C ATOM 866 N GLY B 104 0.365 12.309 36.377 1.00 29.77 N ANISOU 866 N GLY B 104 4532 3883 2897 -83 213 -6 N ATOM 867 CA GLY B 104 1.231 12.988 37.338 1.00 30.16 C ANISOU 867 CA GLY B 104 4571 3918 2970 -133 209 28 C ATOM 868 C GLY B 104 1.439 12.130 38.584 1.00 29.88 C ANISOU 868 C GLY B 104 4510 3869 2972 -123 209 -5 C ATOM 869 O GLY B 104 0.801 11.085 38.744 1.00 29.58 O ANISOU 869 O GLY B 104 4468 3823 2947 -86 204 -44 O ATOM 870 N ARG B 105 2.324 12.575 39.473 1.00 30.08 N ANISOU 870 N ARG B 105 4521 3891 3018 -162 206 18 N ATOM 871 CA ARG B 105 2.656 11.819 40.689 1.00 29.84 C ANISOU 871 CA ARG B 105 4463 3855 3018 -155 206 -5 C ATOM 872 C ARG B 105 1.603 11.933 41.811 1.00 29.65 C ANISOU 872 C ARG B 105 4462 3786 3017 -143 179 -28 C ATOM 873 O ARG B 105 1.648 11.168 42.766 1.00 29.39 O ANISOU 873 O ARG B 105 4406 3756 3003 -135 177 -42 O ATOM 874 CB ARG B 105 4.036 12.235 41.209 1.00 29.98 C ANISOU 874 CB ARG B 105 4449 3898 3043 -199 210 28 C ATOM 875 N GLY B 106 0.672 12.882 41.692 1.00 30.06 N ANISOU 875 N GLY B 106 4555 3807 3060 -136 156 -30 N ATOM 876 CA GLY B 106 -0.407 13.092 42.670 1.00 29.93 C ANISOU 876 CA GLY B 106 4550 3778 3045 -106 131 -56 C ATOM 877 C GLY B 106 -0.089 14.163 43.714 1.00 30.35 C ANISOU 877 C GLY B 106 4626 3804 3103 -110 96 -62 C ATOM 878 O GLY B 106 1.053 14.272 44.165 1.00 30.50 O ANISOU 878 O GLY B 106 4633 3816 3139 -146 95 -46 O ATOM 879 N THR B 107 -1.093 14.965 44.080 1.00 30.53 N ANISOU 879 N THR B 107 4682 3813 3107 -66 59 -89 N ATOM 880 CA THR B 107 -0.972 15.959 45.147 1.00 31.03 C ANISOU 880 CA THR B 107 4776 3846 3166 -43 8 -115 C ATOM 881 C THR B 107 -1.895 15.564 46.290 1.00 31.20 C ANISOU 881 C THR B 107 4761 3935 3159 19 9 -150 C ATOM 882 O THR B 107 -3.120 15.563 46.125 1.00 31.64 O ANISOU 882 O THR B 107 4809 4030 3181 71 7 -169 O ATOM 883 CB THR B 107 -1.351 17.379 44.674 1.00 31.69 C ANISOU 883 CB THR B 107 4939 3861 3241 -21 -57 -126 C ATOM 884 OG1 THR B 107 -0.478 17.787 43.614 1.00 32.04 O ANISOU 884 OG1 THR B 107 5010 3858 3306 -94 -61 -73 O ATOM 885 CG2 THR B 107 -1.235 18.391 45.830 1.00 32.17 C ANISOU 885 CG2 THR B 107 5045 3880 3298 18 -132 -168 C ATOM 886 N LEU B 108 -1.306 15.240 47.442 1.00 31.16 N ANISOU 886 N LEU B 108 4726 3956 3159 15 11 -154 N ATOM 887 CA LEU B 108 -2.066 14.915 48.653 1.00 31.26 C ANISOU 887 CA LEU B 108 4693 4054 3131 71 11 -177 C ATOM 888 C LEU B 108 -2.633 16.183 49.293 1.00 31.77 C ANISOU 888 C LEU B 108 4800 4118 3152 157 -52 -237 C ATOM 889 O LEU B 108 -1.879 17.054 49.726 1.00 32.15 O ANISOU 889 O LEU B 108 4901 4102 3213 161 -104 -263 O ATOM 890 CB LEU B 108 -1.185 14.176 49.662 1.00 31.04 C ANISOU 890 CB LEU B 108 4622 4055 3118 39 29 -159 C ATOM 891 CG LEU B 108 -1.899 13.626 50.908 1.00 31.41 C ANISOU 891 CG LEU B 108 4606 4212 3118 82 37 -160 C ATOM 892 CD1 LEU B 108 -2.894 12.528 50.535 1.00 31.22 C ANISOU 892 CD1 LEU B 108 4524 4254 3082 64 70 -117 C ATOM 893 CD2 LEU B 108 -0.879 13.119 51.921 1.00 31.16 C ANISOU 893 CD2 LEU B 108 4547 4192 3101 54 43 -145 C ATOM 894 N VAL B 109 -3.960 16.280 49.342 1.00 32.07 N ANISOU 894 N VAL B 109 4817 4231 3136 231 -55 -261 N ATOM 895 CA VAL B 109 -4.646 17.409 49.976 1.00 32.65 C ANISOU 895 CA VAL B 109 4925 4329 3152 345 -120 -333 C ATOM 896 C VAL B 109 -5.220 16.952 51.317 1.00 32.87 C ANISOU 896 C VAL B 109 4870 4510 3110 411 -104 -348 C ATOM 897 O VAL B 109 -6.005 16.002 51.370 1.00 32.75 O ANISOU 897 O VAL B 109 4767 4610 3065 399 -52 -305 O ATOM 898 CB VAL B 109 -5.771 17.949 49.073 1.00 32.77 C ANISOU 898 CB VAL B 109 4967 4344 3139 402 -141 -355 C ATOM 899 CG1 VAL B 109 -6.527 19.091 49.753 1.00 33.63 C ANISOU 899 CG1 VAL B 109 5112 4487 3178 546 -218 -442 C ATOM 900 CG2 VAL B 109 -5.186 18.402 47.744 1.00 32.61 C ANISOU 900 CG2 VAL B 109 5025 4185 3180 333 -157 -328 C ATOM 901 N THR B 110 -4.810 17.624 52.391 1.00 33.36 N ANISOU 901 N THR B 110 4958 4575 3144 475 -155 -403 N ATOM 902 CA THR B 110 -5.325 17.358 53.734 1.00 33.74 C ANISOU 902 CA THR B 110 4928 4786 3107 555 -148 -424 C ATOM 903 C THR B 110 -6.161 18.559 54.163 1.00 34.68 C ANISOU 903 C THR B 110 5082 4952 3142 718 -223 -525 C ATOM 904 O THR B 110 -5.639 19.668 54.281 1.00 35.21 O ANISOU 904 O THR B 110 5252 4900 3224 768 -312 -595 O ATOM 905 CB THR B 110 -4.178 17.121 54.743 1.00 33.59 C ANISOU 905 CB THR B 110 4903 4752 3106 521 -151 -420 C ATOM 906 OG1 THR B 110 -3.336 16.046 54.286 1.00 32.62 O ANISOU 906 OG1 THR B 110 4755 4577 3061 384 -92 -336 O ATOM 907 CG2 THR B 110 -4.733 16.782 56.124 1.00 34.09 C ANISOU 907 CG2 THR B 110 4877 5006 3071 603 -138 -431 C ATOM 908 N VAL B 111 -7.459 18.336 54.372 1.00 35.28 N ANISOU 908 N VAL B 111 5073 5203 3127 801 -198 -529 N ATOM 909 CA VAL B 111 -8.367 19.382 54.851 1.00 36.25 C ANISOU 909 CA VAL B 111 5212 5414 3149 984 -268 -633 C ATOM 910 C VAL B 111 -8.544 19.272 56.363 1.00 36.97 C ANISOU 910 C VAL B 111 5222 5692 3133 1085 -268 -666 C ATOM 911 O VAL B 111 -9.215 18.358 56.845 1.00 37.26 O ANISOU 911 O VAL B 111 5123 5933 3101 1075 -197 -601 O ATOM 912 CB VAL B 111 -9.742 19.306 54.162 1.00 36.63 C ANISOU 912 CB VAL B 111 5204 5571 3143 1035 -244 -624 C ATOM 913 CG1 VAL B 111 -10.649 20.434 54.656 1.00 37.96 C ANISOU 913 CG1 VAL B 111 5389 5836 3197 1248 -324 -744 C ATOM 914 CG2 VAL B 111 -9.562 19.345 52.650 1.00 35.83 C ANISOU 914 CG2 VAL B 111 5178 5295 3142 934 -239 -586 C ATOM 915 N SER B 112 -7.944 20.215 57.089 1.00 37.31 N ANISOU 915 N SER B 112 5350 5667 3159 1178 -357 -764 N ATOM 916 CA SER B 112 -7.916 20.202 58.553 1.00 38.10 C ANISOU 916 CA SER B 112 5390 5929 3159 1281 -369 -808 C ATOM 917 C SER B 112 -7.588 21.597 59.125 1.00 38.95 C ANISOU 917 C SER B 112 5622 5944 3234 1438 -509 -956 C ATOM 918 O SER B 112 -6.848 22.374 58.511 1.00 38.60 O ANISOU 918 O SER B 112 5719 5660 3289 1395 -592 -990 O ATOM 919 CB SER B 112 -6.885 19.174 59.043 1.00 37.36 C ANISOU 919 CB SER B 112 5249 5824 3122 1134 -304 -716 C ATOM 920 OG SER B 112 -6.824 19.125 60.460 1.00 38.02 O ANISOU 920 OG SER B 112 5271 6068 3105 1226 -314 -751 O ATOM 921 N ALA B 113 -8.152 21.897 60.297 1.00 39.95 N ANISOU 921 N ALA B 113 5693 6269 3219 1618 -541 -1040 N ATOM 922 CA ALA B 113 -7.885 23.155 61.006 1.00 41.06 C ANISOU 922 CA ALA B 113 5948 6340 3312 1792 -687 -1196 C ATOM 923 C ALA B 113 -6.556 23.149 61.776 1.00 40.87 C ANISOU 923 C ALA B 113 5976 6211 3342 1727 -725 -1202 C ATOM 924 O ALA B 113 -6.076 24.211 62.177 1.00 41.73 O ANISOU 924 O ALA B 113 6212 6189 3454 1825 -867 -1320 O ATOM 925 CB ALA B 113 -9.036 23.483 61.950 1.00 42.44 C ANISOU 925 CB ALA B 113 6037 6792 3295 2036 -711 -1296 C ATOM 926 N ALA B 114 -5.970 21.966 61.979 1.00 39.87 N ANISOU 926 N ALA B 114 5755 6135 3258 1565 -611 -1078 N ATOM 927 CA ALA B 114 -4.722 21.812 62.740 1.00 39.58 C ANISOU 927 CA ALA B 114 5746 6027 3267 1497 -632 -1072 C ATOM 928 C ALA B 114 -3.513 22.424 62.030 1.00 39.23 C ANISOU 928 C ALA B 114 5850 5681 3375 1376 -713 -1075 C ATOM 929 O ALA B 114 -3.431 22.417 60.803 1.00 37.91 O ANISOU 929 O ALA B 114 5725 5373 3305 1262 -694 -1015 O ATOM 930 CB ALA B 114 -4.462 20.340 63.025 1.00 38.53 C ANISOU 930 CB ALA B 114 5476 6018 3144 1354 -494 -931 C ATOM 931 N SER B 115 -2.574 22.935 62.824 1.00 40.30 N ANISOU 931 N SER B 115 6055 5733 3526 1397 -806 -1137 N ATOM 932 CA SER B 115 -1.362 23.568 62.305 1.00 40.59 C ANISOU 932 CA SER B 115 6221 5503 3697 1277 -898 -1132 C ATOM 933 C SER B 115 -0.383 22.546 61.748 1.00 39.32 C ANISOU 933 C SER B 115 6007 5285 3649 1054 -788 -989 C ATOM 934 O SER B 115 -0.362 21.390 62.174 1.00 38.64 O ANISOU 934 O SER B 115 5800 5346 3534 1007 -670 -915 O ATOM 935 CB SER B 115 -0.658 24.358 63.406 1.00 41.90 C ANISOU 935 CB SER B 115 6468 5612 3841 1364 -1037 -1240 C ATOM 936 OG SER B 115 -1.544 25.269 64.029 1.00 44.09 O ANISOU 936 OG SER B 115 6795 5957 3999 1599 -1150 -1390 O ATOM 937 N THR B 116 0.429 22.985 60.791 1.00 39.28 N ANISOU 937 N THR B 116 6090 5069 3764 922 -835 -947 N ATOM 938 CA THR B 116 1.593 22.215 60.350 1.00 38.51 C ANISOU 938 CA THR B 116 5955 4909 3768 729 -761 -832 C ATOM 939 C THR B 116 2.574 21.986 61.507 1.00 38.69 C ANISOU 939 C THR B 116 5954 4959 3786 715 -781 -844 C ATOM 940 O THR B 116 2.688 22.822 62.405 1.00 39.65 O ANISOU 940 O THR B 116 6141 5058 3867 822 -902 -946 O ATOM 941 CB THR B 116 2.337 22.897 59.174 1.00 38.63 C ANISOU 941 CB THR B 116 6066 4714 3898 598 -825 -786 C ATOM 942 OG1 THR B 116 3.397 22.046 58.722 1.00 37.99 O ANISOU 942 OG1 THR B 116 5924 4617 3895 430 -737 -674 O ATOM 943 CG2 THR B 116 2.930 24.257 59.572 1.00 40.09 C ANISOU 943 CG2 THR B 116 6385 4735 4112 628 -1011 -864 C ATOM 944 N LYS B 117 3.262 20.845 61.484 1.00 37.86 N ANISOU 944 N LYS B 117 5759 4904 3720 595 -672 -746 N ATOM 945 CA LYS B 117 4.279 20.527 62.492 1.00 37.97 C ANISOU 945 CA LYS B 117 5745 4944 3739 566 -683 -743 C ATOM 946 C LYS B 117 5.319 19.561 61.938 1.00 36.65 C ANISOU 946 C LYS B 117 5518 4748 3659 400 -594 -629 C ATOM 947 O LYS B 117 4.971 18.508 61.405 1.00 35.77 O ANISOU 947 O LYS B 117 5331 4707 3551 353 -479 -554 O ATOM 948 CB LYS B 117 3.643 19.926 63.749 1.00 38.41 C ANISOU 948 CB LYS B 117 5715 5202 3677 686 -637 -775 C ATOM 949 CG LYS B 117 4.595 19.895 64.933 1.00 39.11 C ANISOU 949 CG LYS B 117 5796 5312 3752 694 -682 -803 C ATOM 950 CD LYS B 117 4.113 19.014 66.072 1.00 39.38 C ANISOU 950 CD LYS B 117 5722 5564 3676 773 -610 -792 C ATOM 951 CE LYS B 117 5.271 18.709 67.013 1.00 39.57 C ANISOU 951 CE LYS B 117 5728 5594 3713 735 -629 -784 C ATOM 952 NZ LYS B 117 4.827 18.059 68.271 1.00 40.01 N ANISOU 952 NZ LYS B 117 5691 5865 3647 829 -585 -784 N ATOM 953 N GLY B 118 6.593 19.925 62.089 1.00 36.78 N ANISOU 953 N GLY B 118 5569 4666 3740 317 -658 -620 N ATOM 954 CA GLY B 118 7.710 19.102 61.635 1.00 35.80 C ANISOU 954 CA GLY B 118 5386 4528 3689 176 -587 -523 C ATOM 955 C GLY B 118 7.965 17.937 62.569 1.00 35.27 C ANISOU 955 C GLY B 118 5226 4592 3584 189 -510 -497 C ATOM 956 O GLY B 118 7.697 18.042 63.765 1.00 35.63 O ANISOU 956 O GLY B 118 5265 4716 3558 288 -544 -557 O ATOM 957 N PRO B 119 8.495 16.818 62.034 1.00 34.52 N ANISOU 957 N PRO B 119 5060 4522 3532 97 -414 -408 N ATOM 958 CA PRO B 119 8.690 15.608 62.834 1.00 34.16 C ANISOU 958 CA PRO B 119 4932 4589 3457 105 -347 -372 C ATOM 959 C PRO B 119 9.918 15.670 63.738 1.00 34.61 C ANISOU 959 C PRO B 119 4980 4643 3529 82 -394 -382 C ATOM 960 O PRO B 119 10.898 16.334 63.397 1.00 34.88 O ANISOU 960 O PRO B 119 5047 4582 3623 12 -453 -382 O ATOM 961 CB PRO B 119 8.914 14.535 61.769 1.00 33.34 C ANISOU 961 CB PRO B 119 4780 4480 3406 21 -256 -287 C ATOM 962 CG PRO B 119 9.602 15.264 60.670 1.00 33.18 C ANISOU 962 CG PRO B 119 4803 4350 3455 -59 -286 -274 C ATOM 963 CD PRO B 119 8.995 16.637 60.657 1.00 33.87 C ANISOU 963 CD PRO B 119 4974 4369 3525 -12 -374 -340 C ATOM 964 N SER B 120 9.851 14.978 64.875 1.00 34.85 N ANISOU 964 N SER B 120 4958 4782 3501 135 -372 -382 N ATOM 965 CA SER B 120 11.034 14.658 65.668 1.00 35.23 C ANISOU 965 CA SER B 120 4976 4846 3564 105 -392 -372 C ATOM 966 C SER B 120 11.537 13.300 65.187 1.00 34.60 C ANISOU 966 C SER B 120 4829 4791 3527 34 -304 -283 C ATOM 967 O SER B 120 10.733 12.396 64.935 1.00 34.28 O ANISOU 967 O SER B 120 4754 4804 3466 45 -236 -238 O ATOM 968 CB SER B 120 10.701 14.601 67.158 1.00 35.81 C ANISOU 968 CB SER B 120 5030 5032 3544 206 -418 -416 C ATOM 969 OG SER B 120 10.195 15.841 67.618 1.00 36.73 O ANISOU 969 OG SER B 120 5214 5132 3610 298 -510 -515 O ATOM 970 N VAL B 121 12.857 13.167 65.069 1.00 34.68 N ANISOU 970 N VAL B 121 4819 4764 3593 -35 -317 -259 N ATOM 971 CA VAL B 121 13.491 11.992 64.467 1.00 34.51 C ANISOU 971 CA VAL B 121 4742 4755 3614 -89 -250 -190 C ATOM 972 C VAL B 121 14.439 11.323 65.461 1.00 35.12 C ANISOU 972 C VAL B 121 4773 4887 3685 -85 -259 -175 C ATOM 973 O VAL B 121 15.477 11.888 65.808 1.00 35.83 O ANISOU 973 O VAL B 121 4860 4958 3795 -114 -312 -195 O ATOM 974 CB VAL B 121 14.286 12.367 63.197 1.00 34.36 C ANISOU 974 CB VAL B 121 4724 4667 3662 -172 -248 -166 C ATOM 975 CG1 VAL B 121 14.917 11.124 62.567 1.00 33.98 C ANISOU 975 CG1 VAL B 121 4618 4650 3645 -199 -184 -111 C ATOM 976 CG2 VAL B 121 13.385 13.093 62.202 1.00 34.25 C ANISOU 976 CG2 VAL B 121 4764 4595 3657 -179 -247 -177 C ATOM 977 N PHE B 122 14.092 10.110 65.894 1.00 35.06 N ANISOU 977 N PHE B 122 4727 4943 3650 -56 -214 -133 N ATOM 978 CA PHE B 122 14.896 9.368 66.870 1.00 35.36 C ANISOU 978 CA PHE B 122 4724 5034 3676 -45 -224 -112 C ATOM 979 C PHE B 122 15.551 8.142 66.223 1.00 34.90 C ANISOU 979 C PHE B 122 4629 4964 3666 -75 -186 -57 C ATOM 980 O PHE B 122 14.968 7.534 65.320 1.00 34.19 O ANISOU 980 O PHE B 122 4547 4850 3596 -85 -145 -27 O ATOM 981 CB PHE B 122 14.029 8.935 68.052 1.00 35.63 C ANISOU 981 CB PHE B 122 4746 5160 3633 15 -223 -99 C ATOM 982 CG PHE B 122 13.220 10.054 68.649 1.00 36.22 C ANISOU 982 CG PHE B 122 4852 5269 3640 75 -259 -163 C ATOM 983 CD1 PHE B 122 13.840 11.056 69.393 1.00 36.88 C ANISOU 983 CD1 PHE B 122 4959 5346 3707 103 -332 -234 C ATOM 984 CD2 PHE B 122 11.838 10.115 68.463 1.00 36.13 C ANISOU 984 CD2 PHE B 122 4847 5300 3581 112 -232 -159 C ATOM 985 CE1 PHE B 122 13.099 12.093 69.939 1.00 37.42 C ANISOU 985 CE1 PHE B 122 5068 5441 3709 179 -382 -309 C ATOM 986 CE2 PHE B 122 11.091 11.149 69.008 1.00 36.61 C ANISOU 986 CE2 PHE B 122 4935 5406 3570 191 -271 -230 C ATOM 987 CZ PHE B 122 11.722 12.138 69.746 1.00 37.36 C ANISOU 987 CZ PHE B 122 5064 5485 3646 231 -350 -311 C ATOM 988 N PRO B 123 16.766 7.778 66.682 1.00 34.97 N ANISOU 988 N PRO B 123 4602 4994 3690 -81 -206 -51 N ATOM 989 CA PRO B 123 17.416 6.579 66.152 1.00 34.80 C ANISOU 989 CA PRO B 123 4549 4969 3704 -84 -182 -12 C ATOM 990 C PRO B 123 16.790 5.289 66.674 1.00 34.42 C ANISOU 990 C PRO B 123 4502 4940 3635 -52 -175 39 C ATOM 991 O PRO B 123 16.357 5.240 67.821 1.00 35.02 O ANISOU 991 O PRO B 123 4577 5068 3662 -30 -193 54 O ATOM 992 CB PRO B 123 18.862 6.713 66.653 1.00 35.23 C ANISOU 992 CB PRO B 123 4560 5055 3769 -91 -216 -25 C ATOM 993 CG PRO B 123 18.757 7.523 67.897 1.00 35.50 C ANISOU 993 CG PRO B 123 4609 5118 3763 -78 -261 -57 C ATOM 994 CD PRO B 123 17.629 8.486 67.651 1.00 35.45 C ANISOU 994 CD PRO B 123 4652 5079 3736 -79 -261 -87 C ATOM 995 N LEU B 124 16.727 4.274 65.815 1.00 34.03 N ANISOU 995 N LEU B 124 4458 4853 3620 -49 -159 69 N ATOM 996 CA LEU B 124 16.434 2.895 66.203 1.00 34.15 C ANISOU 996 CA LEU B 124 4479 4861 3634 -30 -178 127 C ATOM 997 C LEU B 124 17.774 2.175 66.085 1.00 34.78 C ANISOU 997 C LEU B 124 4535 4934 3744 0 -202 119 C ATOM 998 O LEU B 124 18.165 1.759 65.005 1.00 34.60 O ANISOU 998 O LEU B 124 4513 4876 3756 17 -195 102 O ATOM 999 CB LEU B 124 15.377 2.287 65.278 1.00 33.82 C ANISOU 999 CB LEU B 124 4471 4766 3612 -43 -164 158 C ATOM 1000 CG LEU B 124 13.978 2.915 65.350 1.00 33.52 C ANISOU 1000 CG LEU B 124 4448 4751 3539 -66 -140 171 C ATOM 1001 CD1 LEU B 124 13.116 2.502 64.165 1.00 33.21 C ANISOU 1001 CD1 LEU B 124 4437 4652 3528 -84 -125 187 C ATOM 1002 CD2 LEU B 124 13.295 2.543 66.657 1.00 34.01 C ANISOU 1002 CD2 LEU B 124 4493 4885 3544 -67 -159 232 C ATOM 1003 N ALA B 125 18.499 2.076 67.196 1.00 35.87 N ANISOU 1003 N ALA B 125 4648 5120 3862 17 -233 124 N ATOM 1004 CA ALA B 125 19.914 1.690 67.166 1.00 36.79 C ANISOU 1004 CA ALA B 125 4728 5254 3999 51 -255 102 C ATOM 1005 C ALA B 125 20.112 0.195 66.891 1.00 37.75 C ANISOU 1005 C ALA B 125 4869 5330 4145 100 -292 130 C ATOM 1006 O ALA B 125 19.334 -0.623 67.375 1.00 37.65 O ANISOU 1006 O ALA B 125 4896 5283 4128 97 -323 188 O ATOM 1007 CB ALA B 125 20.591 2.069 68.476 1.00 37.19 C ANISOU 1007 CB ALA B 125 4746 5367 4017 56 -283 97 C ATOM 1008 N PRO B 126 21.157 -0.165 66.111 1.00 39.03 N ANISOU 1008 N PRO B 126 5004 5497 4329 148 -297 92 N ATOM 1009 CA PRO B 126 21.500 -1.582 65.981 1.00 40.24 C ANISOU 1009 CA PRO B 126 5184 5605 4502 219 -355 102 C ATOM 1010 C PRO B 126 22.163 -2.127 67.251 1.00 41.71 C ANISOU 1010 C PRO B 126 5358 5818 4674 249 -409 128 C ATOM 1011 O PRO B 126 22.816 -1.382 67.978 1.00 41.86 O ANISOU 1011 O PRO B 126 5325 5911 4668 233 -395 114 O ATOM 1012 CB PRO B 126 22.462 -1.612 64.787 1.00 40.31 C ANISOU 1012 CB PRO B 126 5150 5647 4518 279 -339 39 C ATOM 1013 CG PRO B 126 23.048 -0.250 64.724 1.00 39.93 C ANISOU 1013 CG PRO B 126 5031 5688 4453 227 -284 16 C ATOM 1014 CD PRO B 126 22.013 0.690 65.266 1.00 39.17 C ANISOU 1014 CD PRO B 126 4965 5569 4350 142 -258 42 C ATOM 1015 N SER B 127 21.975 -3.415 67.513 1.00 43.51 N ANISOU 1015 N SER B 127 5639 5976 4918 288 -480 169 N ATOM 1016 CA SER B 127 22.526 -4.076 68.705 1.00 45.15 C ANISOU 1016 CA SER B 127 5846 6196 5112 318 -544 206 C ATOM 1017 C SER B 127 22.490 -5.590 68.508 1.00 46.61 C ANISOU 1017 C SER B 127 6103 6277 5331 378 -641 235 C ATOM 1018 O SER B 127 22.094 -6.062 67.441 1.00 46.82 O ANISOU 1018 O SER B 127 6175 6226 5389 401 -659 213 O ATOM 1019 CB SER B 127 21.719 -3.680 69.951 1.00 45.18 C ANISOU 1019 CB SER B 127 5852 6236 5078 244 -534 277 C ATOM 1020 OG SER B 127 20.347 -4.016 69.803 1.00 45.26 O ANISOU 1020 OG SER B 127 5914 6190 5094 188 -540 344 O ATOM 1021 N SER B 128 22.901 -6.346 69.524 1.00 48.42 N ANISOU 1021 N SER B 128 6347 6496 5554 405 -716 280 N ATOM 1022 CA SER B 128 22.676 -7.799 69.545 1.00 50.13 C ANISOU 1022 CA SER B 128 6652 6590 5807 442 -834 332 C ATOM 1023 C SER B 128 21.176 -8.155 69.491 1.00 50.65 C ANISOU 1023 C SER B 128 6782 6572 5890 345 -858 426 C ATOM 1024 O SER B 128 20.802 -9.180 68.914 1.00 51.21 O ANISOU 1024 O SER B 128 6935 6515 6007 364 -949 447 O ATOM 1025 CB SER B 128 23.325 -8.426 70.781 1.00 51.05 C ANISOU 1025 CB SER B 128 6772 6718 5908 472 -910 381 C ATOM 1026 OG SER B 128 22.847 -7.819 71.969 1.00 51.19 O ANISOU 1026 OG SER B 128 6753 6818 5878 384 -869 455 O ATOM 1027 N LYS B 129 20.335 -7.292 70.067 1.00 50.96 N ANISOU 1027 N LYS B 129 6783 6689 5891 249 -783 479 N ATOM 1028 CA LYS B 129 18.873 -7.479 70.076 1.00 51.51 C ANISOU 1028 CA LYS B 129 6887 6723 5962 151 -790 576 C ATOM 1029 C LYS B 129 18.219 -7.217 68.713 1.00 51.37 C ANISOU 1029 C LYS B 129 6891 6650 5976 139 -751 527 C ATOM 1030 O LYS B 129 17.101 -7.686 68.460 1.00 51.22 O ANISOU 1030 O LYS B 129 6917 6569 5977 72 -787 601 O ATOM 1031 CB LYS B 129 18.212 -6.580 71.134 1.00 51.32 C ANISOU 1031 CB LYS B 129 6801 6830 5866 77 -718 634 C ATOM 1032 CG LYS B 129 18.789 -6.681 72.545 1.00 52.06 C ANISOU 1032 CG LYS B 129 6864 7005 5912 87 -745 681 C ATOM 1033 CD LYS B 129 18.946 -8.120 73.019 1.00 53.24 C ANISOU 1033 CD LYS B 129 7073 7066 6090 90 -872 778 C ATOM 1034 CE LYS B 129 19.139 -8.202 74.524 1.00 53.66 C ANISOU 1034 CE LYS B 129 7091 7218 6079 73 -893 861 C ATOM 1035 NZ LYS B 129 19.053 -9.607 75.005 1.00 54.91 N ANISOU 1035 NZ LYS B 129 7315 7286 6264 50 -1027 986 N ATOM 1036 N SER B 130 18.898 -6.450 67.858 1.00 51.21 N ANISOU 1036 N SER B 130 6835 6664 5958 196 -681 411 N ATOM 1037 CA SER B 130 18.500 -6.291 66.461 1.00 51.43 C ANISOU 1037 CA SER B 130 6886 6642 6015 206 -653 354 C ATOM 1038 C SER B 130 19.574 -6.845 65.508 1.00 52.33 C ANISOU 1038 C SER B 130 7015 6712 6155 324 -693 259 C ATOM 1039 O SER B 130 20.030 -6.144 64.599 1.00 52.42 O ANISOU 1039 O SER B 130 6983 6778 6157 361 -624 175 O ATOM 1040 CB SER B 130 18.206 -4.819 66.158 1.00 50.53 C ANISOU 1040 CB SER B 130 6711 6618 5869 163 -533 311 C ATOM 1041 OG SER B 130 19.381 -4.041 66.262 1.00 50.45 O ANISOU 1041 OG SER B 130 6637 6694 5838 205 -485 241 O ATOM 1042 N THR B 131 19.964 -8.103 65.729 1.00 53.60 N ANISOU 1042 N THR B 131 7236 6785 6344 386 -812 275 N ATOM 1043 CA THR B 131 20.909 -8.818 64.855 1.00 54.33 C ANISOU 1043 CA THR B 131 7355 6834 6453 525 -875 180 C ATOM 1044 C THR B 131 20.451 -10.273 64.681 1.00 55.29 C ANISOU 1044 C THR B 131 7597 6783 6626 555 -1032 216 C ATOM 1045 O THR B 131 20.330 -11.011 65.659 1.00 56.30 O ANISOU 1045 O THR B 131 7771 6849 6771 523 -1125 304 O ATOM 1046 CB THR B 131 22.364 -8.759 65.397 1.00 54.94 C ANISOU 1046 CB THR B 131 7368 7004 6501 616 -874 129 C ATOM 1047 OG1 THR B 131 22.856 -7.413 65.310 1.00 53.94 O ANISOU 1047 OG1 THR B 131 7135 7026 6335 589 -745 86 O ATOM 1048 CG2 THR B 131 23.311 -9.675 64.601 1.00 55.79 C ANISOU 1048 CG2 THR B 131 7504 7077 6615 782 -959 33 C ATOM 1049 N SER B 132 20.199 -10.654 63.428 1.00 55.11 N ANISOU 1049 N SER B 132 7627 6685 6628 614 -1068 149 N ATOM 1050 CA SER B 132 19.803 -12.010 63.046 1.00 55.90 C ANISOU 1050 CA SER B 132 7854 6602 6782 656 -1236 161 C ATOM 1051 C SER B 132 20.825 -12.549 62.040 1.00 56.05 C ANISOU 1051 C SER B 132 7896 6608 6793 851 -1296 15 C ATOM 1052 O SER B 132 20.941 -12.037 60.922 1.00 55.23 O ANISOU 1052 O SER B 132 7752 6571 6661 908 -1221 -78 O ATOM 1053 CB SER B 132 18.400 -11.997 62.429 1.00 55.63 C ANISOU 1053 CB SER B 132 7870 6488 6780 550 -1241 212 C ATOM 1054 OG SER B 132 17.946 -13.311 62.154 1.00 56.74 O ANISOU 1054 OG SER B 132 8140 6436 6981 568 -1423 239 O ATOM 1055 N GLY B 133 21.577 -13.569 62.451 1.00 56.84 N ANISOU 1055 N GLY B 133 8054 6635 6907 960 -1432 -5 N ATOM 1056 CA GLY B 133 22.626 -14.156 61.618 1.00 57.21 C ANISOU 1056 CA GLY B 133 8119 6686 6932 1173 -1503 -151 C ATOM 1057 C GLY B 133 23.801 -13.207 61.465 1.00 56.10 C ANISOU 1057 C GLY B 133 7829 6771 6716 1251 -1357 -234 C ATOM 1058 O GLY B 133 24.365 -12.737 62.461 1.00 56.21 O ANISOU 1058 O GLY B 133 7766 6884 6709 1209 -1298 -190 O ATOM 1059 N GLY B 134 24.164 -12.926 60.216 1.00 54.90 N ANISOU 1059 N GLY B 134 7632 6708 6521 1360 -1305 -348 N ATOM 1060 CA GLY B 134 25.212 -11.964 59.902 1.00 53.64 C ANISOU 1060 CA GLY B 134 7317 6780 6285 1414 -1165 -413 C ATOM 1061 C GLY B 134 24.724 -10.553 59.625 1.00 51.32 C ANISOU 1061 C GLY B 134 6929 6598 5972 1264 -991 -370 C ATOM 1062 O GLY B 134 25.543 -9.665 59.393 1.00 51.05 O ANISOU 1062 O GLY B 134 6765 6752 5880 1278 -879 -401 O ATOM 1063 N THR B 135 23.406 -10.333 59.652 1.00 49.55 N ANISOU 1063 N THR B 135 6768 6265 5794 1119 -977 -294 N ATOM 1064 CA THR B 135 22.822 -9.031 59.320 1.00 47.72 C ANISOU 1064 CA THR B 135 6466 6118 5547 988 -830 -260 C ATOM 1065 C THR B 135 22.206 -8.347 60.540 1.00 46.08 C ANISOU 1065 C THR B 135 6243 5903 5361 818 -776 -148 C ATOM 1066 O THR B 135 21.670 -9.007 61.428 1.00 46.35 O ANISOU 1066 O THR B 135 6350 5828 5434 767 -858 -72 O ATOM 1067 CB THR B 135 21.740 -9.159 58.225 1.00 47.39 C ANISOU 1067 CB THR B 135 6494 5986 5526 969 -842 -275 C ATOM 1068 OG1 THR B 135 20.687 -10.007 58.685 1.00 47.56 O ANISOU 1068 OG1 THR B 135 6636 5822 5613 903 -953 -204 O ATOM 1069 CG2 THR B 135 22.331 -9.740 56.932 1.00 48.38 C ANISOU 1069 CG2 THR B 135 6629 6139 5614 1151 -889 -400 C ATOM 1070 N ALA B 136 22.296 -7.019 60.560 1.00 44.18 N ANISOU 1070 N ALA B 136 5908 5788 5090 735 -646 -136 N ATOM 1071 CA ALA B 136 21.697 -6.186 61.595 1.00 42.42 C ANISOU 1071 CA ALA B 136 5665 5580 4873 592 -588 -52 C ATOM 1072 C ALA B 136 20.647 -5.270 60.969 1.00 40.88 C ANISOU 1072 C ALA B 136 5468 5384 4679 495 -506 -34 C ATOM 1073 O ALA B 136 20.767 -4.887 59.801 1.00 40.28 O ANISOU 1073 O ALA B 136 5366 5351 4587 528 -459 -90 O ATOM 1074 CB ALA B 136 22.773 -5.357 62.280 1.00 42.22 C ANISOU 1074 CB ALA B 136 5537 5691 4812 584 -528 -59 C ATOM 1075 N ALA B 137 19.620 -4.930 61.747 1.00 39.55 N ANISOU 1075 N ALA B 137 5323 5180 4522 383 -491 44 N ATOM 1076 CA ALA B 137 18.632 -3.926 61.358 1.00 38.18 C ANISOU 1076 CA ALA B 137 5142 5023 4344 294 -413 61 C ATOM 1077 C ALA B 137 18.854 -2.657 62.177 1.00 37.39 C ANISOU 1077 C ALA B 137 4975 5018 4213 228 -340 76 C ATOM 1078 O ALA B 137 19.162 -2.721 63.367 1.00 37.31 O ANISOU 1078 O ALA B 137 4951 5035 4192 216 -361 110 O ATOM 1079 CB ALA B 137 17.223 -4.452 61.569 1.00 38.08 C ANISOU 1079 CB ALA B 137 5198 4915 4355 226 -456 134 C ATOM 1080 N LEU B 138 18.712 -1.511 61.521 1.00 36.55 N ANISOU 1080 N LEU B 138 4835 4960 4092 190 -265 49 N ATOM 1081 CA LEU B 138 18.770 -0.199 62.170 1.00 35.95 C ANISOU 1081 CA LEU B 138 4715 4951 3993 124 -213 56 C ATOM 1082 C LEU B 138 17.770 0.700 61.474 1.00 35.26 C ANISOU 1082 C LEU B 138 4645 4849 3904 69 -163 54 C ATOM 1083 O LEU B 138 17.252 0.341 60.414 1.00 35.09 O ANISOU 1083 O LEU B 138 4653 4782 3896 83 -159 43 O ATOM 1084 CB LEU B 138 20.182 0.393 62.096 1.00 36.29 C ANISOU 1084 CB LEU B 138 4683 5083 4022 144 -193 17 C ATOM 1085 CG LEU B 138 20.883 0.469 60.725 1.00 36.52 C ANISOU 1085 CG LEU B 138 4670 5159 4045 185 -165 -26 C ATOM 1086 CD1 LEU B 138 20.634 1.800 60.032 1.00 36.05 C ANISOU 1086 CD1 LEU B 138 4588 5130 3979 112 -107 -27 C ATOM 1087 CD2 LEU B 138 22.379 0.253 60.888 1.00 37.22 C ANISOU 1087 CD2 LEU B 138 4683 5342 4116 242 -179 -51 C ATOM 1088 N GLY B 139 17.493 1.864 62.048 1.00 34.93 N ANISOU 1088 N GLY B 139 4588 4840 3843 14 -134 58 N ATOM 1089 CA GLY B 139 16.452 2.714 61.483 1.00 34.60 C ANISOU 1089 CA GLY B 139 4571 4780 3797 -29 -98 56 C ATOM 1090 C GLY B 139 16.234 4.060 62.128 1.00 34.47 C ANISOU 1090 C GLY B 139 4547 4793 3756 -71 -85 45 C ATOM 1091 O GLY B 139 17.061 4.530 62.917 1.00 34.73 O ANISOU 1091 O GLY B 139 4550 4866 3779 -75 -102 33 O ATOM 1092 N CYS B 140 15.106 4.674 61.773 1.00 34.09 N ANISOU 1092 N CYS B 140 4531 4723 3699 -94 -65 44 N ATOM 1093 CA CYS B 140 14.705 5.965 62.311 1.00 34.20 C ANISOU 1093 CA CYS B 140 4556 4754 3687 -115 -67 22 C ATOM 1094 C CYS B 140 13.210 5.979 62.605 1.00 34.06 C ANISOU 1094 C CYS B 140 4564 4740 3635 -108 -60 39 C ATOM 1095 O CYS B 140 12.408 5.549 61.777 1.00 33.44 O ANISOU 1095 O CYS B 140 4505 4632 3569 -113 -41 57 O ATOM 1096 CB CYS B 140 15.055 7.086 61.331 1.00 34.42 C ANISOU 1096 CB CYS B 140 4587 4759 3733 -150 -56 -7 C ATOM 1097 SG CYS B 140 16.766 7.641 61.471 1.00 35.40 S ANISOU 1097 SG CYS B 140 4661 4916 3873 -180 -80 -18 S ATOM 1098 N LEU B 141 12.859 6.468 63.793 1.00 34.16 N ANISOU 1098 N LEU B 141 4574 4804 3600 -90 -79 32 N ATOM 1099 CA LEU B 141 11.477 6.721 64.165 1.00 34.17 C ANISOU 1099 CA LEU B 141 4585 4848 3551 -72 -72 41 C ATOM 1100 C LEU B 141 11.173 8.189 63.903 1.00 34.06 C ANISOU 1100 C LEU B 141 4602 4816 3522 -60 -82 -23 C ATOM 1101 O LEU B 141 11.700 9.064 64.589 1.00 34.43 O ANISOU 1101 O LEU B 141 4658 4873 3551 -42 -119 -69 O ATOM 1102 CB LEU B 141 11.259 6.390 65.643 1.00 34.90 C ANISOU 1102 CB LEU B 141 4648 5032 3581 -42 -91 69 C ATOM 1103 CG LEU B 141 9.869 6.646 66.236 1.00 35.19 C ANISOU 1103 CG LEU B 141 4670 5161 3538 -10 -84 83 C ATOM 1104 CD1 LEU B 141 8.774 5.929 65.452 1.00 35.07 C ANISOU 1104 CD1 LEU B 141 4651 5138 3534 -42 -57 143 C ATOM 1105 CD2 LEU B 141 9.858 6.227 67.697 1.00 35.66 C ANISOU 1105 CD2 LEU B 141 4688 5333 3529 17 -102 122 C ATOM 1106 N VAL B 142 10.334 8.445 62.903 1.00 33.60 N ANISOU 1106 N VAL B 142 4568 4724 3473 -68 -59 -26 N ATOM 1107 CA VAL B 142 9.906 9.795 62.540 1.00 33.67 C ANISOU 1107 CA VAL B 142 4618 4703 3471 -53 -77 -83 C ATOM 1108 C VAL B 142 8.545 10.037 63.187 1.00 34.05 C ANISOU 1108 C VAL B 142 4664 4831 3444 7 -79 -93 C ATOM 1109 O VAL B 142 7.534 9.486 62.737 1.00 33.71 O ANISOU 1109 O VAL B 142 4606 4814 3389 4 -46 -55 O ATOM 1110 CB VAL B 142 9.811 9.955 61.007 1.00 33.27 C ANISOU 1110 CB VAL B 142 4593 4578 3470 -92 -53 -78 C ATOM 1111 CG1 VAL B 142 9.442 11.385 60.621 1.00 33.42 C ANISOU 1111 CG1 VAL B 142 4664 4552 3483 -82 -86 -129 C ATOM 1112 CG2 VAL B 142 11.132 9.555 60.355 1.00 33.18 C ANISOU 1112 CG2 VAL B 142 4564 4530 3514 -139 -43 -60 C ATOM 1113 N LYS B 143 8.527 10.879 64.224 1.00 34.67 N ANISOU 1113 N LYS B 143 4752 4955 3468 65 -123 -148 N ATOM 1114 CA LYS B 143 7.385 10.983 65.133 1.00 35.09 C ANISOU 1114 CA LYS B 143 4779 5131 3423 143 -125 -158 C ATOM 1115 C LYS B 143 6.785 12.392 65.203 1.00 35.04 C ANISOU 1115 C LYS B 143 4822 5121 3370 224 -175 -250 C ATOM 1116 O LYS B 143 7.499 13.387 65.095 1.00 35.41 O ANISOU 1116 O LYS B 143 4930 5073 3452 224 -236 -313 O ATOM 1117 CB LYS B 143 7.820 10.525 66.534 1.00 36.08 C ANISOU 1117 CB LYS B 143 4860 5353 3496 171 -139 -141 C ATOM 1118 CG LYS B 143 6.682 10.024 67.414 1.00 36.98 C ANISOU 1118 CG LYS B 143 4910 5634 3505 223 -116 -98 C ATOM 1119 CD LYS B 143 7.195 9.369 68.684 1.00 37.75 C ANISOU 1119 CD LYS B 143 4959 5827 3558 231 -124 -57 C ATOM 1120 CE LYS B 143 6.045 8.887 69.558 1.00 38.70 C ANISOU 1120 CE LYS B 143 5001 6140 3561 274 -101 6 C ATOM 1121 NZ LYS B 143 5.287 9.997 70.192 1.00 39.69 N ANISOU 1121 NZ LYS B 143 5121 6385 3574 398 -126 -82 N ATOM 1122 N ASP B 144 5.466 12.447 65.382 1.00 34.82 N ANISOU 1122 N ASP B 144 4769 5199 3264 291 -158 -254 N ATOM 1123 CA ASP B 144 4.727 13.671 65.726 1.00 35.34 C ANISOU 1123 CA ASP B 144 4870 5304 3254 406 -213 -350 C ATOM 1124 C ASP B 144 4.809 14.787 64.676 1.00 34.97 C ANISOU 1124 C ASP B 144 4915 5102 3267 401 -262 -413 C ATOM 1125 O ASP B 144 5.323 15.874 64.951 1.00 35.36 O ANISOU 1125 O ASP B 144 5036 5074 3324 440 -350 -495 O ATOM 1126 CB ASP B 144 5.154 14.206 67.113 1.00 36.16 C ANISOU 1126 CB ASP B 144 4978 5476 3286 495 -276 -419 C ATOM 1127 CG ASP B 144 4.891 13.216 68.250 1.00 36.34 C ANISOU 1127 CG ASP B 144 4904 5682 3222 517 -232 -355 C ATOM 1128 OD1 ASP B 144 3.914 12.432 68.188 1.00 36.17 O ANISOU 1128 OD1 ASP B 144 4808 5780 3153 508 -170 -277 O ATOM 1129 OD2 ASP B 144 5.673 13.235 69.220 1.00 36.30 O ANISOU 1129 OD2 ASP B 144 4895 5704 3195 538 -266 -376 O ATOM 1130 N TYR B 145 4.283 14.514 63.483 1.00 34.18 N ANISOU 1130 N TYR B 145 4817 4957 3211 349 -216 -370 N ATOM 1131 CA TYR B 145 4.220 15.516 62.410 1.00 33.86 C ANISOU 1131 CA TYR B 145 4859 4784 3221 341 -258 -414 C ATOM 1132 C TYR B 145 2.814 15.634 61.818 1.00 33.62 C ANISOU 1132 C TYR B 145 4821 4806 3145 395 -234 -420 C ATOM 1133 O TYR B 145 1.972 14.747 61.996 1.00 33.20 O ANISOU 1133 O TYR B 145 4689 4882 3042 404 -170 -366 O ATOM 1134 CB TYR B 145 5.245 15.208 61.318 1.00 33.22 C ANISOU 1134 CB TYR B 145 4797 4575 3249 212 -235 -357 C ATOM 1135 CG TYR B 145 5.026 13.895 60.596 1.00 32.65 C ANISOU 1135 CG TYR B 145 4666 4533 3206 144 -144 -270 C ATOM 1136 CD1 TYR B 145 5.579 12.708 61.078 1.00 32.30 C ANISOU 1136 CD1 TYR B 145 4562 4538 3173 102 -103 -211 C ATOM 1137 CD2 TYR B 145 4.268 13.842 59.417 1.00 32.37 C ANISOU 1137 CD2 TYR B 145 4643 4467 3189 127 -113 -250 C ATOM 1138 CE1 TYR B 145 5.378 11.504 60.416 1.00 32.06 C ANISOU 1138 CE1 TYR B 145 4493 4514 3173 47 -44 -139 C ATOM 1139 CE2 TYR B 145 4.062 12.645 58.746 1.00 31.76 C ANISOU 1139 CE2 TYR B 145 4522 4406 3140 70 -48 -180 C ATOM 1140 CZ TYR B 145 4.616 11.476 59.246 1.00 31.76 C ANISOU 1140 CZ TYR B 145 4471 4443 3153 31 -19 -126 C ATOM 1141 OH TYR B 145 4.412 10.285 58.577 1.00 31.34 O ANISOU 1141 OH TYR B 145 4389 4386 3132 -18 22 -63 O ATOM 1142 N PHE B 146 2.564 16.748 61.136 1.00 33.60 N ANISOU 1142 N PHE B 146 4901 4704 3160 427 -294 -479 N ATOM 1143 CA PHE B 146 1.286 16.961 60.454 1.00 33.69 C ANISOU 1143 CA PHE B 146 4914 4752 3136 481 -278 -490 C ATOM 1144 C PHE B 146 1.460 17.987 59.334 1.00 33.89 C ANISOU 1144 C PHE B 146 5040 4609 3226 456 -339 -520 C ATOM 1145 O PHE B 146 2.195 18.947 59.534 1.00 34.58 O ANISOU 1145 O PHE B 146 5209 4587 3343 460 -432 -572 O ATOM 1146 CB PHE B 146 0.224 17.442 61.451 1.00 34.33 C ANISOU 1146 CB PHE B 146 4970 4983 3091 641 -312 -566 C ATOM 1147 CG PHE B 146 -1.178 17.398 60.913 1.00 34.06 C ANISOU 1147 CG PHE B 146 4900 5041 3001 699 -278 -562 C ATOM 1148 CD1 PHE B 146 -1.894 16.203 60.901 1.00 33.68 C ANISOU 1148 CD1 PHE B 146 4740 5137 2919 658 -186 -470 C ATOM 1149 CD2 PHE B 146 -1.788 18.546 60.423 1.00 34.58 C ANISOU 1149 CD2 PHE B 146 5043 5047 3047 792 -350 -646 C ATOM 1150 CE1 PHE B 146 -3.190 16.154 60.406 1.00 33.81 C ANISOU 1150 CE1 PHE B 146 4713 5249 2883 703 -158 -460 C ATOM 1151 CE2 PHE B 146 -3.087 18.505 59.925 1.00 34.74 C ANISOU 1151 CE2 PHE B 146 5024 5164 3013 852 -319 -644 C ATOM 1152 CZ PHE B 146 -3.786 17.307 59.913 1.00 34.35 C ANISOU 1152 CZ PHE B 146 4852 5270 2929 804 -220 -549 C ATOM 1153 N PRO B 147 0.843 17.798 58.155 1.00 33.77 N ANISOU 1153 N PRO B 147 5025 4569 3236 420 -296 -482 N ATOM 1154 CA PRO B 147 0.086 16.596 57.762 1.00 33.27 C ANISOU 1154 CA PRO B 147 4874 4609 3158 387 -197 -410 C ATOM 1155 C PRO B 147 1.015 15.581 57.102 1.00 32.59 C ANISOU 1155 C PRO B 147 4763 4464 3155 253 -136 -325 C ATOM 1156 O PRO B 147 2.216 15.695 57.248 1.00 32.25 O ANISOU 1156 O PRO B 147 4744 4349 3162 199 -157 -321 O ATOM 1157 CB PRO B 147 -0.933 17.156 56.767 1.00 33.44 C ANISOU 1157 CB PRO B 147 4931 4606 3168 427 -208 -432 C ATOM 1158 CG PRO B 147 -0.206 18.280 56.116 1.00 33.63 C ANISOU 1158 CG PRO B 147 5065 4458 3255 400 -286 -465 C ATOM 1159 CD PRO B 147 0.645 18.899 57.194 1.00 34.05 C ANISOU 1159 CD PRO B 147 5157 4477 3304 430 -363 -518 C ATOM 1160 N GLU B 148 0.471 14.582 56.411 1.00 32.70 N ANISOU 1160 N GLU B 148 4727 4516 3181 207 -69 -263 N ATOM 1161 CA GLU B 148 1.273 13.786 55.474 1.00 32.57 C ANISOU 1161 CA GLU B 148 4707 4424 3242 103 -28 -203 C ATOM 1162 C GLU B 148 1.605 14.673 54.254 1.00 32.76 C ANISOU 1162 C GLU B 148 4804 4331 3313 74 -54 -219 C ATOM 1163 O GLU B 148 0.877 15.640 54.001 1.00 33.38 O ANISOU 1163 O GLU B 148 4930 4389 3366 130 -94 -262 O ATOM 1164 CB GLU B 148 0.520 12.523 55.044 1.00 32.58 C ANISOU 1164 CB GLU B 148 4651 4485 3243 71 27 -142 C ATOM 1165 CG GLU B 148 0.470 11.421 56.098 1.00 32.86 C ANISOU 1165 CG GLU B 148 4615 4617 3253 59 47 -93 C ATOM 1166 CD GLU B 148 1.450 10.291 55.827 1.00 32.99 C ANISOU 1166 CD GLU B 148 4621 4580 3334 -17 67 -42 C ATOM 1167 OE1 GLU B 148 0.972 9.181 55.503 1.00 33.56 O ANISOU 1167 OE1 GLU B 148 4662 4669 3419 -56 84 14 O ATOM 1168 OE2 GLU B 148 2.688 10.503 55.919 1.00 32.75 O ANISOU 1168 OE2 GLU B 148 4614 4490 3340 -37 58 -59 O ATOM 1169 N PRO B 149 2.676 14.389 53.497 1.00 32.47 N ANISOU 1169 N PRO B 149 4774 4227 3336 -7 -35 -182 N ATOM 1170 CA PRO B 149 3.570 13.253 53.685 1.00 32.10 C ANISOU 1170 CA PRO B 149 4677 4201 3319 -58 5 -139 C ATOM 1171 C PRO B 149 4.938 13.656 54.220 1.00 32.23 C ANISOU 1171 C PRO B 149 4700 4184 3362 -92 -26 -143 C ATOM 1172 O PRO B 149 5.243 14.845 54.349 1.00 32.37 O ANISOU 1172 O PRO B 149 4768 4147 3383 -90 -85 -173 O ATOM 1173 CB PRO B 149 3.735 12.736 52.257 1.00 31.73 C ANISOU 1173 CB PRO B 149 4630 4119 3308 -106 43 -104 C ATOM 1174 CG PRO B 149 3.772 13.996 51.449 1.00 32.08 C ANISOU 1174 CG PRO B 149 4733 4097 3360 -117 9 -118 C ATOM 1175 CD PRO B 149 2.831 14.959 52.144 1.00 32.56 C ANISOU 1175 CD PRO B 149 4831 4159 3380 -47 -42 -169 C ATOM 1176 N VAL B 150 5.744 12.637 54.499 1.00 32.02 N ANISOU 1176 N VAL B 150 4626 4186 3355 -122 6 -112 N ATOM 1177 CA VAL B 150 7.159 12.788 54.813 1.00 32.22 C ANISOU 1177 CA VAL B 150 4640 4193 3409 -164 -12 -104 C ATOM 1178 C VAL B 150 7.941 11.831 53.910 1.00 31.94 C ANISOU 1178 C VAL B 150 4566 4165 3404 -205 34 -64 C ATOM 1179 O VAL B 150 7.443 10.758 53.563 1.00 31.78 O ANISOU 1179 O VAL B 150 4527 4166 3383 -189 69 -49 O ATOM 1180 CB VAL B 150 7.433 12.510 56.312 1.00 32.42 C ANISOU 1180 CB VAL B 150 4639 4267 3412 -135 -30 -118 C ATOM 1181 CG1 VAL B 150 7.273 11.032 56.665 1.00 32.12 C ANISOU 1181 CG1 VAL B 150 4550 4287 3368 -127 13 -83 C ATOM 1182 CG2 VAL B 150 8.818 12.995 56.701 1.00 32.84 C ANISOU 1182 CG2 VAL B 150 4689 4296 3492 -175 -67 -120 C ATOM 1183 N THR B 151 9.149 12.219 53.515 1.00 32.10 N ANISOU 1183 N THR B 151 4573 4174 3448 -254 26 -46 N ATOM 1184 CA THR B 151 9.994 11.344 52.697 1.00 32.17 C ANISOU 1184 CA THR B 151 4535 4218 3470 -272 67 -17 C ATOM 1185 C THR B 151 11.295 11.067 53.424 1.00 32.27 C ANISOU 1185 C THR B 151 4500 4269 3493 -289 57 -8 C ATOM 1186 O THR B 151 11.874 11.970 54.033 1.00 32.56 O ANISOU 1186 O THR B 151 4542 4293 3536 -324 15 -8 O ATOM 1187 CB THR B 151 10.288 11.937 51.306 1.00 32.48 C ANISOU 1187 CB THR B 151 4577 4253 3512 -314 78 10 C ATOM 1188 OG1 THR B 151 11.016 13.156 51.446 1.00 33.42 O ANISOU 1188 OG1 THR B 151 4705 4352 3642 -377 32 32 O ATOM 1189 CG2 THR B 151 8.997 12.201 50.550 1.00 32.36 C ANISOU 1189 CG2 THR B 151 4610 4201 3486 -294 85 0 C ATOM 1190 N VAL B 152 11.734 9.811 53.359 1.00 32.05 N ANISOU 1190 N VAL B 152 4431 4280 3466 -259 86 -3 N ATOM 1191 CA VAL B 152 12.935 9.355 54.045 1.00 32.33 C ANISOU 1191 CA VAL B 152 4417 4361 3508 -258 79 2 C ATOM 1192 C VAL B 152 13.874 8.726 53.029 1.00 32.51 C ANISOU 1192 C VAL B 152 4386 4442 3524 -247 108 14 C ATOM 1193 O VAL B 152 13.462 7.880 52.242 1.00 32.08 O ANISOU 1193 O VAL B 152 4339 4388 3464 -202 130 3 O ATOM 1194 CB VAL B 152 12.614 8.306 55.137 1.00 32.17 C ANISOU 1194 CB VAL B 152 4397 4340 3486 -212 70 -8 C ATOM 1195 CG1 VAL B 152 13.887 7.883 55.871 1.00 32.57 C ANISOU 1195 CG1 VAL B 152 4400 4435 3542 -206 56 -4 C ATOM 1196 CG2 VAL B 152 11.564 8.837 56.108 1.00 32.03 C ANISOU 1196 CG2 VAL B 152 4417 4299 3452 -206 48 -19 C ATOM 1197 N SER B 153 15.129 9.155 53.055 1.00 33.30 N ANISOU 1197 N SER B 153 4431 4602 3622 -284 103 36 N ATOM 1198 CA SER B 153 16.202 8.509 52.316 1.00 34.00 C ANISOU 1198 CA SER B 153 4445 4785 3689 -257 129 45 C ATOM 1199 C SER B 153 17.275 8.111 53.315 1.00 34.41 C ANISOU 1199 C SER B 153 4445 4884 3743 -244 110 42 C ATOM 1200 O SER B 153 17.214 8.492 54.486 1.00 34.47 O ANISOU 1200 O SER B 153 4475 4850 3770 -270 76 39 O ATOM 1201 CB SER B 153 16.779 9.457 51.267 1.00 34.58 C ANISOU 1201 CB SER B 153 4475 4923 3742 -322 144 92 C ATOM 1202 OG SER B 153 17.606 10.438 51.867 1.00 35.21 O ANISOU 1202 OG SER B 153 4522 5021 3834 -407 108 131 O ATOM 1203 N TRP B 154 18.258 7.354 52.841 1.00 35.13 N ANISOU 1203 N TRP B 154 4466 5072 3808 -194 128 38 N ATOM 1204 CA TRP B 154 19.371 6.904 53.667 1.00 35.62 C ANISOU 1204 CA TRP B 154 4469 5197 3868 -170 110 34 C ATOM 1205 C TRP B 154 20.692 7.223 52.972 1.00 36.93 C ANISOU 1205 C TRP B 154 4524 5511 3995 -190 130 68 C ATOM 1206 O TRP B 154 20.866 6.910 51.788 1.00 37.15 O ANISOU 1206 O TRP B 154 4512 5621 3982 -147 164 67 O ATOM 1207 CB TRP B 154 19.239 5.406 53.947 1.00 35.20 C ANISOU 1207 CB TRP B 154 4438 5120 3815 -61 98 -11 C ATOM 1208 CG TRP B 154 18.238 5.107 55.005 1.00 34.32 C ANISOU 1208 CG TRP B 154 4406 4897 3738 -62 69 -19 C ATOM 1209 CD1 TRP B 154 16.904 4.873 54.835 1.00 33.52 C ANISOU 1209 CD1 TRP B 154 4378 4707 3650 -58 68 -24 C ATOM 1210 CD2 TRP B 154 18.485 5.024 56.413 1.00 34.07 C ANISOU 1210 CD2 TRP B 154 4376 4849 3719 -71 36 -15 C ATOM 1211 NE1 TRP B 154 16.306 4.645 56.049 1.00 33.10 N ANISOU 1211 NE1 TRP B 154 4365 4599 3614 -66 40 -17 N ATOM 1212 CE2 TRP B 154 17.254 4.731 57.035 1.00 33.58 C ANISOU 1212 CE2 TRP B 154 4385 4701 3672 -70 20 -12 C ATOM 1213 CE3 TRP B 154 19.631 5.162 57.208 1.00 34.41 C ANISOU 1213 CE3 TRP B 154 4361 4954 3758 -78 18 -9 C ATOM 1214 CZ2 TRP B 154 17.132 4.579 58.422 1.00 33.55 C ANISOU 1214 CZ2 TRP B 154 4395 4681 3672 -74 -10 -2 C ATOM 1215 CZ3 TRP B 154 19.511 5.015 58.585 1.00 34.47 C ANISOU 1215 CZ3 TRP B 154 4392 4928 3776 -80 -16 -7 C ATOM 1216 CH2 TRP B 154 18.268 4.725 59.179 1.00 33.93 C ANISOU 1216 CH2 TRP B 154 4394 4782 3715 -75 -28 -3 C ATOM 1217 N ASN B 155 21.606 7.844 53.723 1.00 37.98 N ANISOU 1217 N ASN B 155 4603 5690 4136 -256 104 101 N ATOM 1218 CA ASN B 155 22.889 8.364 53.211 1.00 39.30 C ANISOU 1218 CA ASN B 155 4651 6013 4268 -310 114 157 C ATOM 1219 C ASN B 155 22.726 9.190 51.924 1.00 39.89 C ANISOU 1219 C ASN B 155 4703 6135 4318 -381 140 214 C ATOM 1220 O ASN B 155 23.418 8.974 50.922 1.00 40.84 O ANISOU 1220 O ASN B 155 4727 6414 4379 -357 178 242 O ATOM 1221 CB ASN B 155 23.905 7.223 53.061 1.00 39.88 C ANISOU 1221 CB ASN B 155 4631 6226 4294 -198 133 128 C ATOM 1222 CG ASN B 155 24.224 6.557 54.387 1.00 40.02 C ANISOU 1222 CG ASN B 155 4665 6204 4338 -147 96 88 C ATOM 1223 OD1 ASN B 155 23.812 7.035 55.449 1.00 39.78 O ANISOU 1223 OD1 ASN B 155 4698 6065 4353 -206 59 91 O ATOM 1224 ND2 ASN B 155 24.958 5.452 54.339 1.00 40.57 N ANISOU 1224 ND2 ASN B 155 4677 6365 4371 -29 99 49 N ATOM 1225 N SER B 156 21.781 10.129 51.986 1.00 39.60 N ANISOU 1225 N SER B 156 4759 5967 4321 -460 115 231 N ATOM 1226 CA SER B 156 21.458 11.054 50.895 1.00 39.87 C ANISOU 1226 CA SER B 156 4797 6008 4343 -541 123 291 C ATOM 1227 C SER B 156 21.094 10.349 49.579 1.00 39.93 C ANISOU 1227 C SER B 156 4787 6085 4298 -457 185 273 C ATOM 1228 O SER B 156 21.409 10.846 48.492 1.00 41.10 O ANISOU 1228 O SER B 156 4876 6337 4404 -506 208 338 O ATOM 1229 CB SER B 156 22.611 12.044 50.694 1.00 40.85 C ANISOU 1229 CB SER B 156 4824 6242 4454 -672 95 392 C ATOM 1230 OG SER B 156 22.997 12.624 51.931 1.00 40.66 O ANISOU 1230 OG SER B 156 4819 6151 4480 -742 25 398 O ATOM 1231 N GLY B 157 20.423 9.199 49.689 1.00 38.97 N ANISOU 1231 N GLY B 157 4721 5906 4180 -334 203 191 N ATOM 1232 CA GLY B 157 20.048 8.380 48.529 1.00 38.61 C ANISOU 1232 CA GLY B 157 4673 5909 4087 -234 245 154 C ATOM 1233 C GLY B 157 21.059 7.331 48.092 1.00 39.05 C ANISOU 1233 C GLY B 157 4632 6125 4079 -119 268 122 C ATOM 1234 O GLY B 157 20.749 6.508 47.234 1.00 39.20 O ANISOU 1234 O GLY B 157 4662 6173 4060 -11 287 71 O ATOM 1235 N ALA B 158 22.262 7.351 48.668 1.00 39.54 N ANISOU 1235 N ALA B 158 4601 6295 4127 -133 260 146 N ATOM 1236 CA ALA B 158 23.292 6.346 48.373 1.00 40.27 C ANISOU 1236 CA ALA B 158 4595 6554 4153 -6 276 107 C ATOM 1237 C ALA B 158 22.922 4.943 48.877 1.00 39.93 C ANISOU 1237 C ALA B 158 4628 6412 4132 140 244 5 C ATOM 1238 O ALA B 158 23.360 3.948 48.292 1.00 40.63 O ANISOU 1238 O ALA B 158 4678 6596 4162 284 245 -55 O ATOM 1239 CB ALA B 158 24.633 6.775 48.953 1.00 41.16 C ANISOU 1239 CB ALA B 158 4586 6804 4248 -66 269 164 C ATOM 1240 N LEU B 159 22.140 4.871 49.961 1.00 38.90 N ANISOU 1240 N LEU B 159 4603 6098 4079 105 207 -10 N ATOM 1241 CA LEU B 159 21.617 3.604 50.479 1.00 38.31 C ANISOU 1241 CA LEU B 159 4614 5907 4036 212 165 -83 C ATOM 1242 C LEU B 159 20.121 3.494 50.191 1.00 37.24 C ANISOU 1242 C LEU B 159 4595 5616 3939 199 157 -99 C ATOM 1243 O LEU B 159 19.320 4.262 50.717 1.00 36.41 O ANISOU 1243 O LEU B 159 4545 5411 3878 99 157 -64 O ATOM 1244 CB LEU B 159 21.880 3.480 51.984 1.00 38.18 C ANISOU 1244 CB LEU B 159 4613 5826 4066 184 126 -77 C ATOM 1245 CG LEU B 159 21.622 2.106 52.621 1.00 38.13 C ANISOU 1245 CG LEU B 159 4677 5724 4086 290 70 -133 C ATOM 1246 CD1 LEU B 159 22.531 1.029 52.041 1.00 38.98 C ANISOU 1246 CD1 LEU B 159 4734 5935 4141 443 50 -193 C ATOM 1247 CD2 LEU B 159 21.799 2.190 54.131 1.00 38.17 C ANISOU 1247 CD2 LEU B 159 4695 5675 4131 241 39 -111 C ATOM 1248 N THR B 160 19.776 2.578 49.290 1.00 37.41 N ANISOU 1248 N THR B 160 4649 5631 3935 308 145 -155 N ATOM 1249 CA THR B 160 18.391 2.154 49.036 1.00 36.57 C ANISOU 1249 CA THR B 160 4653 5376 3866 315 120 -178 C ATOM 1250 C THR B 160 18.175 0.651 49.265 1.00 36.84 C ANISOU 1250 C THR B 160 4756 5321 3920 430 45 -241 C ATOM 1251 O THR B 160 17.040 0.210 49.478 1.00 36.25 O ANISOU 1251 O THR B 160 4775 5104 3894 411 5 -242 O ATOM 1252 CB THR B 160 17.982 2.470 47.581 1.00 36.73 C ANISOU 1252 CB THR B 160 4669 5446 3841 331 156 -186 C ATOM 1253 OG1 THR B 160 18.731 1.647 46.672 1.00 37.45 O ANISOU 1253 OG1 THR B 160 4712 5654 3863 472 148 -247 O ATOM 1254 CG2 THR B 160 18.221 3.945 47.262 1.00 36.55 C ANISOU 1254 CG2 THR B 160 4584 5507 3798 212 215 -112 C ATOM 1255 N SER B 161 19.257 -0.129 49.211 1.00 37.81 N ANISOU 1255 N SER B 161 4832 5529 4007 546 17 -289 N ATOM 1256 CA SER B 161 19.179 -1.581 49.285 1.00 38.35 C ANISOU 1256 CA SER B 161 4972 5510 4090 673 -75 -356 C ATOM 1257 C SER B 161 18.900 -2.021 50.723 1.00 37.72 C ANISOU 1257 C SER B 161 4951 5302 4080 624 -131 -323 C ATOM 1258 O SER B 161 19.615 -1.624 51.648 1.00 37.50 O ANISOU 1258 O SER B 161 4867 5327 4055 583 -110 -290 O ATOM 1259 CB SER B 161 20.480 -2.205 48.772 1.00 39.50 C ANISOU 1259 CB SER B 161 5042 5803 4162 831 -91 -425 C ATOM 1260 OG SER B 161 20.305 -3.582 48.525 1.00 40.36 O ANISOU 1260 OG SER B 161 5238 5818 4279 975 -196 -508 O ATOM 1261 N GLY B 162 17.848 -2.821 50.893 1.00 37.47 N ANISOU 1261 N GLY B 162 5027 5109 4100 622 -204 -325 N ATOM 1262 CA GLY B 162 17.424 -3.318 52.202 1.00 37.36 C ANISOU 1262 CA GLY B 162 5070 4977 4146 567 -263 -278 C ATOM 1263 C GLY B 162 16.457 -2.423 52.961 1.00 36.33 C ANISOU 1263 C GLY B 162 4949 4806 4048 417 -216 -198 C ATOM 1264 O GLY B 162 16.064 -2.757 54.083 1.00 36.48 O ANISOU 1264 O GLY B 162 5002 4756 4104 366 -256 -148 O ATOM 1265 N VAL B 163 16.054 -1.307 52.353 1.00 35.54 N ANISOU 1265 N VAL B 163 4819 4756 3929 353 -136 -184 N ATOM 1266 CA VAL B 163 15.273 -0.271 53.037 1.00 34.62 C ANISOU 1266 CA VAL B 163 4701 4624 3829 232 -90 -124 C ATOM 1267 C VAL B 163 13.767 -0.567 52.988 1.00 34.01 C ANISOU 1267 C VAL B 163 4697 4443 3782 185 -118 -95 C ATOM 1268 O VAL B 163 13.250 -1.011 51.972 1.00 34.27 O ANISOU 1268 O VAL B 163 4769 4435 3817 220 -140 -123 O ATOM 1269 CB VAL B 163 15.551 1.133 52.433 1.00 34.27 C ANISOU 1269 CB VAL B 163 4598 4671 3751 182 -8 -119 C ATOM 1270 CG1 VAL B 163 14.689 2.206 53.099 1.00 33.60 C ANISOU 1270 CG1 VAL B 163 4527 4557 3681 78 22 -73 C ATOM 1271 CG2 VAL B 163 17.030 1.490 52.556 1.00 34.55 C ANISOU 1271 CG2 VAL B 163 4546 4825 3755 204 17 -127 C ATOM 1272 N HIS B 164 13.083 -0.333 54.104 1.00 33.60 N ANISOU 1272 N HIS B 164 4655 4362 3747 109 -121 -38 N ATOM 1273 CA HIS B 164 11.621 -0.343 54.158 1.00 33.27 C ANISOU 1273 CA HIS B 164 4656 4264 3721 48 -132 4 C ATOM 1274 C HIS B 164 11.175 0.850 54.984 1.00 32.89 C ANISOU 1274 C HIS B 164 4577 4266 3653 -22 -78 38 C ATOM 1275 O HIS B 164 11.577 0.986 56.151 1.00 32.79 O ANISOU 1275 O HIS B 164 4539 4285 3634 -37 -81 62 O ATOM 1276 CB HIS B 164 11.094 -1.620 54.806 1.00 33.78 C ANISOU 1276 CB HIS B 164 4767 4248 3819 39 -221 51 C ATOM 1277 CG HIS B 164 11.357 -2.858 54.011 1.00 34.80 C ANISOU 1277 CG HIS B 164 4951 4298 3974 113 -305 11 C ATOM 1278 ND1 HIS B 164 12.385 -3.728 54.308 1.00 35.57 N ANISOU 1278 ND1 HIS B 164 5059 4375 4081 188 -367 -15 N ATOM 1279 CD2 HIS B 164 10.724 -3.377 52.933 1.00 35.02 C ANISOU 1279 CD2 HIS B 164 5031 4259 4017 136 -348 -16 C ATOM 1280 CE1 HIS B 164 12.374 -4.728 53.446 1.00 36.23 C ANISOU 1280 CE1 HIS B 164 5204 4379 4183 261 -450 -61 C ATOM 1281 NE2 HIS B 164 11.377 -4.539 52.601 1.00 35.94 N ANISOU 1281 NE2 HIS B 164 5194 4311 4150 229 -441 -63 N ATOM 1282 N THR B 165 10.362 1.714 54.378 1.00 32.27 N ANISOU 1282 N THR B 165 4503 4195 3563 -53 -37 35 N ATOM 1283 CA THR B 165 9.756 2.841 55.076 1.00 31.90 C ANISOU 1283 CA THR B 165 4441 4187 3493 -101 -1 55 C ATOM 1284 C THR B 165 8.263 2.566 55.191 1.00 31.72 C ANISOU 1284 C THR B 165 4439 4145 3467 -133 -17 96 C ATOM 1285 O THR B 165 7.570 2.458 54.188 1.00 31.81 O ANISOU 1285 O THR B 165 4476 4125 3487 -134 -16 88 O ATOM 1286 CB THR B 165 10.035 4.159 54.346 1.00 31.68 C ANISOU 1286 CB THR B 165 4401 4185 3449 -110 47 21 C ATOM 1287 OG1 THR B 165 11.434 4.450 54.444 1.00 32.03 O ANISOU 1287 OG1 THR B 165 4409 4268 3491 -98 56 3 O ATOM 1288 CG2 THR B 165 9.239 5.315 54.950 1.00 31.47 C ANISOU 1288 CG2 THR B 165 4379 4178 3399 -141 62 28 C ATOM 1289 N PHE B 166 7.782 2.468 56.424 1.00 31.68 N ANISOU 1289 N PHE B 166 4416 4176 3444 -159 -31 144 N ATOM 1290 CA PHE B 166 6.434 1.973 56.698 1.00 31.69 C ANISOU 1290 CA PHE B 166 4417 4187 3435 -197 -55 206 C ATOM 1291 C PHE B 166 5.374 3.044 56.484 1.00 31.39 C ANISOU 1291 C PHE B 166 4369 4199 3360 -205 -14 195 C ATOM 1292 O PHE B 166 5.665 4.234 56.617 1.00 30.82 O ANISOU 1292 O PHE B 166 4289 4157 3262 -183 22 149 O ATOM 1293 CB PHE B 166 6.352 1.441 58.129 1.00 31.84 C ANISOU 1293 CB PHE B 166 4408 4256 3435 -220 -84 273 C ATOM 1294 CG PHE B 166 7.091 0.159 58.323 1.00 32.10 C ANISOU 1294 CG PHE B 166 4463 4225 3508 -218 -147 301 C ATOM 1295 CD1 PHE B 166 8.465 0.153 58.540 1.00 32.02 C ANISOU 1295 CD1 PHE B 166 4451 4204 3510 -174 -147 257 C ATOM 1296 CD2 PHE B 166 6.418 -1.052 58.248 1.00 32.46 C ANISOU 1296 CD2 PHE B 166 4534 4218 3584 -260 -219 372 C ATOM 1297 CE1 PHE B 166 9.150 -1.038 58.698 1.00 32.54 C ANISOU 1297 CE1 PHE B 166 4542 4210 3610 -156 -214 274 C ATOM 1298 CE2 PHE B 166 7.095 -2.242 58.409 1.00 32.94 C ANISOU 1298 CE2 PHE B 166 4630 4200 3686 -251 -298 394 C ATOM 1299 CZ PHE B 166 8.462 -2.241 58.632 1.00 33.10 C ANISOU 1299 CZ PHE B 166 4651 4213 3713 -190 -294 340 C ATOM 1300 N PRO B 167 4.142 2.623 56.136 1.00 31.69 N ANISOU 1300 N PRO B 167 4408 4239 3396 -236 -30 238 N ATOM 1301 CA PRO B 167 3.001 3.535 56.151 1.00 31.67 C ANISOU 1301 CA PRO B 167 4382 4307 3346 -235 2 237 C ATOM 1302 C PRO B 167 2.873 4.224 57.500 1.00 32.34 C ANISOU 1302 C PRO B 167 4422 4499 3367 -216 19 246 C ATOM 1303 O PRO B 167 3.029 3.571 58.541 1.00 32.84 O ANISOU 1303 O PRO B 167 4455 4607 3416 -235 -3 302 O ATOM 1304 CB PRO B 167 1.806 2.609 55.936 1.00 31.95 C ANISOU 1304 CB PRO B 167 4405 4349 3386 -286 -35 312 C ATOM 1305 CG PRO B 167 2.349 1.464 55.165 1.00 32.14 C ANISOU 1305 CG PRO B 167 4478 4256 3477 -301 -87 314 C ATOM 1306 CD PRO B 167 3.793 1.313 55.553 1.00 32.07 C ANISOU 1306 CD PRO B 167 4483 4214 3487 -267 -89 280 C ATOM 1307 N ALA B 168 2.620 5.529 57.483 1.00 32.45 N ANISOU 1307 N ALA B 168 4437 4550 3341 -173 48 188 N ATOM 1308 CA ALA B 168 2.478 6.292 58.720 1.00 33.40 C ANISOU 1308 CA ALA B 168 4524 4773 3393 -131 54 174 C ATOM 1309 C ALA B 168 1.169 5.924 59.396 1.00 34.25 C ANISOU 1309 C ALA B 168 4567 5013 3433 -137 52 242 C ATOM 1310 O ALA B 168 0.190 5.629 58.723 1.00 34.68 O ANISOU 1310 O ALA B 168 4611 5077 3489 -163 53 276 O ATOM 1311 CB ALA B 168 2.525 7.785 58.434 1.00 33.49 C ANISOU 1311 CB ALA B 168 4570 4769 3384 -75 63 86 C ATOM 1312 N VAL B 169 1.161 5.925 60.722 1.00 35.20 N ANISOU 1312 N VAL B 169 4638 5246 3489 -115 48 269 N ATOM 1313 CA VAL B 169 -0.070 5.719 61.475 1.00 36.29 C ANISOU 1313 CA VAL B 169 4694 5554 3539 -113 52 339 C ATOM 1314 C VAL B 169 -0.474 7.020 62.157 1.00 36.85 C ANISOU 1314 C VAL B 169 4743 5745 3512 -6 65 262 C ATOM 1315 O VAL B 169 0.361 7.714 62.757 1.00 36.69 O ANISOU 1315 O VAL B 169 4752 5709 3479 50 55 191 O ATOM 1316 CB VAL B 169 0.066 4.597 62.521 1.00 36.89 C ANISOU 1316 CB VAL B 169 4716 5704 3596 -169 31 450 C ATOM 1317 CG1 VAL B 169 -1.243 4.429 63.285 1.00 37.99 C ANISOU 1317 CG1 VAL B 169 4752 6053 3630 -174 37 539 C ATOM 1318 CG2 VAL B 169 0.447 3.287 61.841 1.00 36.68 C ANISOU 1318 CG2 VAL B 169 4727 5540 3669 -263 -6 518 C ATOM 1319 N LEU B 170 -1.763 7.336 62.049 1.00 37.45 N ANISOU 1319 N LEU B 170 4769 5941 3518 26 77 273 N ATOM 1320 CA LEU B 170 -2.346 8.453 62.763 1.00 38.28 C ANISOU 1320 CA LEU B 170 4842 6192 3511 148 80 201 C ATOM 1321 C LEU B 170 -2.469 8.055 64.227 1.00 39.59 C ANISOU 1321 C LEU B 170 4917 6547 3577 168 81 263 C ATOM 1322 O LEU B 170 -3.209 7.127 64.562 1.00 40.22 O ANISOU 1322 O LEU B 170 4906 6759 3615 103 91 388 O ATOM 1323 CB LEU B 170 -3.720 8.806 62.186 1.00 38.35 C ANISOU 1323 CB LEU B 170 4811 6293 3467 183 92 200 C ATOM 1324 CG LEU B 170 -4.424 10.030 62.779 1.00 39.01 C ANISOU 1324 CG LEU B 170 4869 6528 3427 337 85 107 C ATOM 1325 CD1 LEU B 170 -3.549 11.275 62.673 1.00 38.65 C ANISOU 1325 CD1 LEU B 170 4936 6338 3413 422 47 -36 C ATOM 1326 CD2 LEU B 170 -5.764 10.243 62.095 1.00 39.21 C ANISOU 1326 CD2 LEU B 170 4850 6641 3408 364 97 114 C ATOM 1327 N GLN B 171 -1.713 8.738 65.086 1.00 40.29 N ANISOU 1327 N GLN B 171 5032 6648 3629 249 63 184 N ATOM 1328 CA GLN B 171 -1.812 8.554 66.538 1.00 41.40 C ANISOU 1328 CA GLN B 171 5088 6987 3654 295 63 223 C ATOM 1329 C GLN B 171 -3.076 9.234 67.072 1.00 42.12 C ANISOU 1329 C GLN B 171 5096 7316 3593 417 72 194 C ATOM 1330 O GLN B 171 -3.677 10.071 66.385 1.00 41.84 O ANISOU 1330 O GLN B 171 5091 7260 3547 488 67 111 O ATOM 1331 CB GLN B 171 -0.562 9.101 67.238 1.00 41.74 C ANISOU 1331 CB GLN B 171 5192 6958 3710 349 32 135 C ATOM 1332 CG GLN B 171 0.697 8.295 66.932 1.00 41.55 C ANISOU 1332 CG GLN B 171 5221 6753 3812 238 26 178 C ATOM 1333 CD GLN B 171 1.991 9.009 67.300 1.00 41.91 C ANISOU 1333 CD GLN B 171 5339 6693 3892 282 -9 78 C ATOM 1334 OE1 GLN B 171 2.823 8.472 68.042 1.00 42.19 O ANISOU 1334 OE1 GLN B 171 5362 6732 3935 254 -19 112 O ATOM 1335 NE2 GLN B 171 2.178 10.216 66.768 1.00 41.98 N ANISOU 1335 NE2 GLN B 171 5425 6603 3925 343 -36 -41 N ATOM 1336 N SER B 172 -3.479 8.871 68.293 1.00 42.90 N ANISOU 1336 N SER B 172 5084 7653 3564 448 83 264 N ATOM 1337 CA SER B 172 -4.659 9.475 68.934 1.00 43.72 C ANISOU 1337 CA SER B 172 5085 8032 3494 583 93 239 C ATOM 1338 C SER B 172 -4.474 10.979 69.194 1.00 43.54 C ANISOU 1338 C SER B 172 5135 7995 3412 774 51 43 C ATOM 1339 O SER B 172 -5.454 11.719 69.277 1.00 44.26 O ANISOU 1339 O SER B 172 5183 8246 3389 910 46 -24 O ATOM 1340 CB SER B 172 -5.015 8.745 70.233 1.00 45.01 C ANISOU 1340 CB SER B 172 5106 8471 3523 574 113 365 C ATOM 1341 OG SER B 172 -4.048 8.976 71.242 1.00 45.46 O ANISOU 1341 OG SER B 172 5193 8530 3549 635 90 309 O ATOM 1342 N SER B 173 -3.215 11.411 69.315 1.00 42.44 N ANISOU 1342 N SER B 173 5108 7664 3352 784 10 -46 N ATOM 1343 CA SER B 173 -2.847 12.831 69.385 1.00 42.19 C ANISOU 1343 CA SER B 173 5181 7543 3307 933 -57 -230 C ATOM 1344 C SER B 173 -3.328 13.686 68.206 1.00 41.56 C ANISOU 1344 C SER B 173 5181 7332 3278 973 -81 -316 C ATOM 1345 O SER B 173 -3.537 14.881 68.378 1.00 42.30 O ANISOU 1345 O SER B 173 5332 7430 3312 1130 -145 -458 O ATOM 1346 CB SER B 173 -1.322 12.976 69.490 1.00 41.30 C ANISOU 1346 CB SER B 173 5174 7213 3305 882 -99 -277 C ATOM 1347 OG SER B 173 -0.673 12.476 68.331 1.00 39.90 O ANISOU 1347 OG SER B 173 5061 6805 3294 727 -79 -223 O ATOM 1348 N GLY B 174 -3.479 13.080 67.026 1.00 40.33 N ANISOU 1348 N GLY B 174 5037 7053 3232 837 -41 -234 N ATOM 1349 CA GLY B 174 -3.786 13.803 65.783 1.00 39.71 C ANISOU 1349 CA GLY B 174 5044 6822 3222 849 -62 -302 C ATOM 1350 C GLY B 174 -2.565 14.057 64.903 1.00 38.54 C ANISOU 1350 C GLY B 174 5026 6382 3234 757 -90 -335 C ATOM 1351 O GLY B 174 -2.669 14.734 63.878 1.00 38.00 O ANISOU 1351 O GLY B 174 5039 6174 3226 762 -116 -389 O ATOM 1352 N LEU B 175 -1.413 13.517 65.308 1.00 38.21 N ANISOU 1352 N LEU B 175 4998 6265 3253 675 -87 -297 N ATOM 1353 CA LEU B 175 -0.149 13.663 64.589 1.00 37.40 C ANISOU 1353 CA LEU B 175 4996 5926 3290 583 -110 -314 C ATOM 1354 C LEU B 175 0.288 12.299 64.068 1.00 36.71 C ANISOU 1354 C LEU B 175 4874 5784 3291 432 -51 -191 C ATOM 1355 O LEU B 175 -0.016 11.269 64.677 1.00 37.35 O ANISOU 1355 O LEU B 175 4868 5992 3330 395 -15 -98 O ATOM 1356 CB LEU B 175 0.927 14.217 65.523 1.00 37.62 C ANISOU 1356 CB LEU B 175 5068 5913 3312 626 -169 -384 C ATOM 1357 CG LEU B 175 0.589 15.516 66.256 1.00 38.69 C ANISOU 1357 CG LEU B 175 5246 6103 3351 793 -252 -518 C ATOM 1358 CD1 LEU B 175 1.621 15.800 67.340 1.00 39.14 C ANISOU 1358 CD1 LEU B 175 5329 6149 3395 826 -309 -570 C ATOM 1359 CD2 LEU B 175 0.490 16.678 65.284 1.00 38.48 C ANISOU 1359 CD2 LEU B 175 5331 5912 3379 825 -318 -605 C ATOM 1360 N TYR B 176 1.009 12.298 62.950 1.00 35.77 N ANISOU 1360 N TYR B 176 4823 5479 3287 348 -50 -190 N ATOM 1361 CA TYR B 176 1.481 11.062 62.343 1.00 34.88 C ANISOU 1361 CA TYR B 176 4693 5300 3259 226 -9 -96 C ATOM 1362 C TYR B 176 2.810 10.618 62.938 1.00 34.57 C ANISOU 1362 C TYR B 176 4659 5213 3262 183 -19 -80 C ATOM 1363 O TYR B 176 3.527 11.392 63.587 1.00 34.07 O ANISOU 1363 O TYR B 176 4628 5131 3186 229 -60 -147 O ATOM 1364 CB TYR B 176 1.590 11.201 60.818 1.00 34.45 C ANISOU 1364 CB TYR B 176 4698 5099 3294 171 1 -103 C ATOM 1365 CG TYR B 176 0.237 11.310 60.162 1.00 34.65 C ANISOU 1365 CG TYR B 176 4706 5176 3284 195 17 -95 C ATOM 1366 CD1 TYR B 176 -0.507 10.168 59.858 1.00 34.60 C ANISOU 1366 CD1 TYR B 176 4640 5228 3280 136 52 -4 C ATOM 1367 CD2 TYR B 176 -0.325 12.556 59.886 1.00 34.98 C ANISOU 1367 CD2 TYR B 176 4791 5208 3289 280 -14 -178 C ATOM 1368 CE1 TYR B 176 -1.766 10.266 59.280 1.00 34.78 C ANISOU 1368 CE1 TYR B 176 4638 5310 3268 154 64 7 C ATOM 1369 CE2 TYR B 176 -1.580 12.661 59.308 1.00 35.21 C ANISOU 1369 CE2 TYR B 176 4799 5297 3281 311 0 -173 C ATOM 1370 CZ TYR B 176 -2.294 11.517 59.008 1.00 35.12 C ANISOU 1370 CZ TYR B 176 4719 5356 3271 246 44 -80 C ATOM 1371 OH TYR B 176 -3.535 11.631 58.439 1.00 35.90 O ANISOU 1371 OH TYR B 176 4788 5520 3331 272 54 -73 O ATOM 1372 N SER B 177 3.099 9.342 62.716 1.00 34.25 N ANISOU 1372 N SER B 177 4589 5152 3271 99 9 8 N ATOM 1373 CA SER B 177 4.353 8.729 63.111 1.00 34.25 C ANISOU 1373 CA SER B 177 4592 5102 3319 56 0 31 C ATOM 1374 C SER B 177 4.656 7.550 62.183 1.00 33.68 C ANISOU 1374 C SER B 177 4525 4943 3329 -27 18 96 C ATOM 1375 O SER B 177 3.749 6.802 61.802 1.00 33.33 O ANISOU 1375 O SER B 177 4456 4925 3283 -60 30 159 O ATOM 1376 CB SER B 177 4.274 8.251 64.562 1.00 34.93 C ANISOU 1376 CB SER B 177 4617 5324 3330 80 -7 74 C ATOM 1377 OG SER B 177 5.515 7.706 64.980 1.00 35.15 O ANISOU 1377 OG SER B 177 4650 5302 3403 46 -20 91 O ATOM 1378 N LEU B 178 5.925 7.407 61.809 1.00 33.65 N ANISOU 1378 N LEU B 178 4552 4841 3393 -55 10 78 N ATOM 1379 CA LEU B 178 6.372 6.266 61.012 1.00 33.63 C ANISOU 1379 CA LEU B 178 4557 4761 3459 -107 15 123 C ATOM 1380 C LEU B 178 7.792 5.870 61.360 1.00 33.60 C ANISOU 1380 C LEU B 178 4554 4722 3492 -114 -1 118 C ATOM 1381 O LEU B 178 8.545 6.640 61.957 1.00 33.79 O ANISOU 1381 O LEU B 178 4577 4759 3502 -93 -12 74 O ATOM 1382 CB LEU B 178 6.248 6.539 59.500 1.00 33.51 C ANISOU 1382 CB LEU B 178 4581 4663 3490 -122 32 94 C ATOM 1383 CG LEU B 178 7.168 7.509 58.730 1.00 33.54 C ANISOU 1383 CG LEU B 178 4618 4600 3528 -120 36 33 C ATOM 1384 CD1 LEU B 178 8.625 7.058 58.633 1.00 33.60 C ANISOU 1384 CD1 LEU B 178 4617 4572 3577 -136 31 32 C ATOM 1385 CD2 LEU B 178 6.591 7.707 57.329 1.00 33.36 C ANISOU 1385 CD2 LEU B 178 4623 4527 3525 -132 55 23 C ATOM 1386 N SER B 179 8.134 4.652 60.962 1.00 33.78 N ANISOU 1386 N SER B 179 4579 4698 3560 -140 -12 160 N ATOM 1387 CA SER B 179 9.468 4.104 61.107 1.00 33.81 C ANISOU 1387 CA SER B 179 4580 4666 3599 -136 -30 155 C ATOM 1388 C SER B 179 10.028 3.806 59.722 1.00 33.02 C ANISOU 1388 C SER B 179 4504 4490 3552 -135 -23 127 C ATOM 1389 O SER B 179 9.286 3.418 58.821 1.00 32.77 O ANISOU 1389 O SER B 179 4495 4421 3536 -144 -21 137 O ATOM 1390 CB SER B 179 9.408 2.817 61.920 1.00 34.70 C ANISOU 1390 CB SER B 179 4680 4794 3711 -148 -67 227 C ATOM 1391 OG SER B 179 8.479 1.914 61.338 1.00 35.72 O ANISOU 1391 OG SER B 179 4825 4886 3860 -179 -87 281 O ATOM 1392 N SER B 180 11.333 4.013 59.567 1.00 32.60 N ANISOU 1392 N SER B 180 4438 4430 3516 -120 -21 91 N ATOM 1393 CA SER B 180 12.071 3.641 58.367 1.00 32.25 C ANISOU 1393 CA SER B 180 4398 4350 3504 -103 -15 65 C ATOM 1394 C SER B 180 13.274 2.832 58.817 1.00 32.47 C ANISOU 1394 C SER B 180 4404 4389 3546 -71 -44 65 C ATOM 1395 O SER B 180 14.073 3.315 59.617 1.00 32.27 O ANISOU 1395 O SER B 180 4347 4405 3507 -74 -45 57 O ATOM 1396 CB SER B 180 12.523 4.888 57.602 1.00 32.15 C ANISOU 1396 CB SER B 180 4375 4351 3489 -119 18 28 C ATOM 1397 OG SER B 180 13.237 4.552 56.418 1.00 31.90 O ANISOU 1397 OG SER B 180 4331 4318 3471 -98 31 9 O ATOM 1398 N VAL B 181 13.393 1.608 58.305 1.00 32.58 N ANISOU 1398 N VAL B 181 4438 4359 3583 -35 -77 68 N ATOM 1399 CA VAL B 181 14.470 0.689 58.686 1.00 33.04 C ANISOU 1399 CA VAL B 181 4484 4419 3652 14 -118 63 C ATOM 1400 C VAL B 181 15.294 0.229 57.474 1.00 33.42 C ANISOU 1400 C VAL B 181 4525 4467 3707 81 -122 11 C ATOM 1401 O VAL B 181 14.879 0.397 56.318 1.00 32.89 O ANISOU 1401 O VAL B 181 4472 4385 3639 87 -100 -12 O ATOM 1402 CB VAL B 181 13.930 -0.542 59.454 1.00 33.44 C ANISOU 1402 CB VAL B 181 4572 4415 3718 13 -186 118 C ATOM 1403 CG1 VAL B 181 13.139 -0.098 60.681 1.00 33.28 C ANISOU 1403 CG1 VAL B 181 4540 4434 3671 -45 -177 175 C ATOM 1404 CG2 VAL B 181 13.079 -1.440 58.556 1.00 33.56 C ANISOU 1404 CG2 VAL B 181 4644 4346 3762 18 -229 128 C ATOM 1405 N VAL B 182 16.464 -0.339 57.760 1.00 33.72 N ANISOU 1405 N VAL B 182 4536 4534 3743 140 -151 -9 N ATOM 1406 CA VAL B 182 17.355 -0.889 56.733 1.00 34.36 C ANISOU 1406 CA VAL B 182 4598 4642 3814 231 -162 -65 C ATOM 1407 C VAL B 182 18.187 -2.019 57.326 1.00 35.00 C ANISOU 1407 C VAL B 182 4685 4711 3902 311 -233 -78 C ATOM 1408 O VAL B 182 18.701 -1.895 58.442 1.00 35.16 O ANISOU 1408 O VAL B 182 4678 4762 3921 292 -240 -53 O ATOM 1409 CB VAL B 182 18.274 0.195 56.107 1.00 34.42 C ANISOU 1409 CB VAL B 182 4524 4767 3786 224 -93 -89 C ATOM 1410 CG1 VAL B 182 19.204 0.820 57.137 1.00 34.65 C ANISOU 1410 CG1 VAL B 182 4491 4867 3807 190 -82 -71 C ATOM 1411 CG2 VAL B 182 19.076 -0.367 54.942 1.00 35.20 C ANISOU 1411 CG2 VAL B 182 4591 4929 3856 328 -97 -145 C ATOM 1412 N THR B 183 18.293 -3.121 56.586 1.00 35.38 N ANISOU 1412 N THR B 183 4776 4710 3957 407 -296 -121 N ATOM 1413 CA THR B 183 19.098 -4.268 56.992 1.00 36.20 C ANISOU 1413 CA THR B 183 4898 4790 4067 506 -382 -147 C ATOM 1414 C THR B 183 20.470 -4.153 56.344 1.00 36.81 C ANISOU 1414 C THR B 183 4893 4998 4095 611 -354 -217 C ATOM 1415 O THR B 183 20.570 -3.859 55.155 1.00 36.69 O ANISOU 1415 O THR B 183 4849 5047 4047 651 -314 -262 O ATOM 1416 CB THR B 183 18.438 -5.588 56.573 1.00 36.77 C ANISOU 1416 CB THR B 183 5075 4720 4175 563 -493 -160 C ATOM 1417 OG1 THR B 183 17.905 -5.455 55.250 1.00 36.94 O ANISOU 1417 OG1 THR B 183 5117 4733 4187 585 -472 -204 O ATOM 1418 CG2 THR B 183 17.316 -5.940 57.530 1.00 36.47 C ANISOU 1418 CG2 THR B 183 5103 4572 4183 457 -543 -67 C ATOM 1419 N VAL B 184 21.519 -4.371 57.135 1.00 37.34 N ANISOU 1419 N VAL B 184 4915 5124 4150 656 -376 -222 N ATOM 1420 CA VAL B 184 22.904 -4.211 56.678 1.00 38.29 C ANISOU 1420 CA VAL B 184 4932 5402 4213 749 -347 -277 C ATOM 1421 C VAL B 184 23.766 -5.338 57.251 1.00 39.33 C ANISOU 1421 C VAL B 184 5076 5524 4343 874 -440 -313 C ATOM 1422 O VAL B 184 23.340 -6.017 58.183 1.00 39.22 O ANISOU 1422 O VAL B 184 5142 5384 4375 855 -516 -277 O ATOM 1423 CB VAL B 184 23.485 -2.826 57.085 1.00 37.93 C ANISOU 1423 CB VAL B 184 4779 5487 4146 645 -254 -235 C ATOM 1424 CG1 VAL B 184 22.539 -1.705 56.672 1.00 37.12 C ANISOU 1424 CG1 VAL B 184 4685 5365 4054 519 -183 -195 C ATOM 1425 CG2 VAL B 184 23.773 -2.744 58.583 1.00 37.75 C ANISOU 1425 CG2 VAL B 184 4751 5447 4145 592 -278 -191 C ATOM 1426 N PRO B 185 24.981 -5.538 56.706 1.00 40.57 N ANISOU 1426 N PRO B 185 5150 5825 4441 1005 -438 -380 N ATOM 1427 CA PRO B 185 25.871 -6.530 57.312 1.00 41.75 C ANISOU 1427 CA PRO B 185 5304 5976 4582 1132 -528 -419 C ATOM 1428 C PRO B 185 26.289 -6.118 58.717 1.00 41.72 C ANISOU 1428 C PRO B 185 5261 5993 4598 1044 -515 -355 C ATOM 1429 O PRO B 185 26.593 -4.946 58.942 1.00 41.16 O ANISOU 1429 O PRO B 185 5096 6032 4509 939 -424 -314 O ATOM 1430 CB PRO B 185 27.091 -6.540 56.381 1.00 42.78 C ANISOU 1430 CB PRO B 185 5317 6310 4625 1280 -501 -499 C ATOM 1431 CG PRO B 185 26.629 -5.909 55.119 1.00 42.44 C ANISOU 1431 CG PRO B 185 5246 6328 4550 1252 -424 -510 C ATOM 1432 CD PRO B 185 25.593 -4.914 55.520 1.00 40.98 C ANISOU 1432 CD PRO B 185 5093 6056 4421 1048 -359 -419 C ATOM 1433 N SER B 186 26.306 -7.077 59.641 1.00 42.31 N ANISOU 1433 N SER B 186 5412 5958 4707 1088 -616 -344 N ATOM 1434 CA SER B 186 26.731 -6.832 61.019 1.00 42.41 C ANISOU 1434 CA SER B 186 5393 5990 4730 1024 -618 -288 C ATOM 1435 C SER B 186 28.150 -6.267 61.104 1.00 42.91 C ANISOU 1435 C SER B 186 5311 6255 4737 1067 -567 -317 C ATOM 1436 O SER B 186 28.415 -5.367 61.906 1.00 42.27 O ANISOU 1436 O SER B 186 5166 6239 4656 958 -514 -266 O ATOM 1437 CB SER B 186 26.634 -8.118 61.841 1.00 43.26 C ANISOU 1437 CB SER B 186 5605 5956 4876 1089 -751 -275 C ATOM 1438 OG SER B 186 25.280 -8.520 61.952 1.00 43.20 O ANISOU 1438 OG SER B 186 5717 5774 4923 1007 -797 -217 O ATOM 1439 N SER B 187 29.042 -6.785 60.260 1.00 43.98 N ANISOU 1439 N SER B 187 5392 6498 4820 1228 -588 -399 N ATOM 1440 CA SER B 187 30.427 -6.310 60.185 1.00 44.73 C ANISOU 1440 CA SER B 187 5330 6818 4848 1279 -541 -424 C ATOM 1441 C SER B 187 30.591 -4.870 59.665 1.00 44.49 C ANISOU 1441 C SER B 187 5178 6939 4787 1148 -418 -382 C ATOM 1442 O SER B 187 31.647 -4.271 59.866 1.00 45.15 O ANISOU 1442 O SER B 187 5126 7199 4829 1129 -379 -367 O ATOM 1443 CB SER B 187 31.265 -7.265 59.330 1.00 45.99 C ANISOU 1443 CB SER B 187 5456 7075 4943 1504 -597 -527 C ATOM 1444 OG SER B 187 30.712 -7.406 58.038 1.00 45.67 O ANISOU 1444 OG SER B 187 5448 7024 4881 1558 -584 -575 O ATOM 1445 N SER B 188 29.571 -4.327 58.996 1.00 43.99 N ANISOU 1445 N SER B 188 5162 6807 4746 1054 -367 -358 N ATOM 1446 CA SER B 188 29.587 -2.927 58.544 1.00 43.93 C ANISOU 1446 CA SER B 188 5063 6907 4720 913 -267 -306 C ATOM 1447 C SER B 188 29.354 -1.900 59.661 1.00 43.39 C ANISOU 1447 C SER B 188 4996 6794 4698 739 -243 -231 C ATOM 1448 O SER B 188 29.688 -0.726 59.486 1.00 43.39 O ANISOU 1448 O SER B 188 4908 6894 4683 627 -185 -187 O ATOM 1449 CB SER B 188 28.559 -2.699 57.422 1.00 43.26 C ANISOU 1449 CB SER B 188 5034 6762 4640 883 -229 -310 C ATOM 1450 OG SER B 188 27.228 -2.642 57.913 1.00 42.10 O ANISOU 1450 OG SER B 188 5017 6415 4563 787 -244 -275 O ATOM 1451 N LEU B 189 28.785 -2.331 60.791 1.00 43.31 N ANISOU 1451 N LEU B 189 5084 6635 4737 718 -296 -214 N ATOM 1452 CA LEU B 189 28.406 -1.408 61.881 1.00 42.93 C ANISOU 1452 CA LEU B 189 5051 6537 4723 572 -281 -154 C ATOM 1453 C LEU B 189 29.578 -0.648 62.506 1.00 43.76 C ANISOU 1453 C LEU B 189 5042 6780 4807 524 -271 -135 C ATOM 1454 O LEU B 189 29.384 0.430 63.057 1.00 43.33 O ANISOU 1454 O LEU B 189 4980 6714 4769 396 -252 -95 O ATOM 1455 CB LEU B 189 27.637 -2.143 62.987 1.00 42.50 C ANISOU 1455 CB LEU B 189 5109 6330 4707 576 -342 -135 C ATOM 1456 CG LEU B 189 26.251 -2.696 62.636 1.00 42.05 C ANISOU 1456 CG LEU B 189 5173 6120 4683 570 -359 -125 C ATOM 1457 CD1 LEU B 189 25.726 -3.537 63.792 1.00 42.06 C ANISOU 1457 CD1 LEU B 189 5261 6008 4713 574 -432 -87 C ATOM 1458 CD2 LEU B 189 25.267 -1.586 62.294 1.00 41.04 C ANISOU 1458 CD2 LEU B 189 5062 5963 4568 447 -294 -95 C ATOM 1459 N GLY B 190 30.779 -1.212 62.425 1.00 45.42 N ANISOU 1459 N GLY B 190 5163 7119 4976 631 -293 -167 N ATOM 1460 CA GLY B 190 31.979 -0.546 62.904 1.00 46.71 C ANISOU 1460 CA GLY B 190 5199 7436 5114 587 -287 -145 C ATOM 1461 C GLY B 190 32.365 0.692 62.116 1.00 47.46 C ANISOU 1461 C GLY B 190 5186 7660 5186 474 -227 -104 C ATOM 1462 O GLY B 190 32.494 1.767 62.694 1.00 47.57 O ANISOU 1462 O GLY B 190 5174 7680 5222 337 -226 -57 O ATOM 1463 N THR B 191 32.542 0.545 60.802 1.00 48.75 N ANISOU 1463 N THR B 191 5291 7927 5304 532 -186 -120 N ATOM 1464 CA THR B 191 33.123 1.607 59.965 1.00 49.82 C ANISOU 1464 CA THR B 191 5297 8231 5402 434 -133 -67 C ATOM 1465 C THR B 191 32.080 2.458 59.223 1.00 49.55 C ANISOU 1465 C THR B 191 5324 8107 5394 318 -90 -30 C ATOM 1466 O THR B 191 32.126 3.692 59.284 1.00 50.03 O ANISOU 1466 O THR B 191 5353 8182 5475 158 -81 37 O ATOM 1467 CB THR B 191 34.138 1.032 58.953 1.00 51.17 C ANISOU 1467 CB THR B 191 5328 8631 5481 570 -110 -96 C ATOM 1468 OG1 THR B 191 33.469 0.203 57.997 1.00 51.15 O ANISOU 1468 OG1 THR B 191 5398 8578 5458 699 -99 -158 O ATOM 1469 CG2 THR B 191 35.206 0.215 59.671 1.00 52.09 C ANISOU 1469 CG2 THR B 191 5378 8846 5566 696 -158 -137 C ATOM 1470 N GLN B 192 31.150 1.799 58.536 1.00 49.13 N ANISOU 1470 N GLN B 192 5367 7957 5345 399 -77 -74 N ATOM 1471 CA GLN B 192 30.145 2.482 57.707 1.00 48.49 C ANISOU 1471 CA GLN B 192 5343 7802 5281 312 -36 -47 C ATOM 1472 C GLN B 192 29.171 3.276 58.578 1.00 47.33 C ANISOU 1472 C GLN B 192 5304 7474 5205 179 -53 -16 C ATOM 1473 O GLN B 192 28.500 2.698 59.433 1.00 47.25 O ANISOU 1473 O GLN B 192 5398 7323 5233 214 -87 -44 O ATOM 1474 CB GLN B 192 29.380 1.449 56.857 1.00 48.46 C ANISOU 1474 CB GLN B 192 5420 7729 5264 444 -32 -111 C ATOM 1475 CG GLN B 192 28.269 1.986 55.959 1.00 47.79 C ANISOU 1475 CG GLN B 192 5401 7564 5194 377 7 -93 C ATOM 1476 CD GLN B 192 28.763 2.922 54.871 1.00 48.23 C ANISOU 1476 CD GLN B 192 5342 7787 5197 306 63 -40 C ATOM 1477 OE1 GLN B 192 28.292 4.050 54.750 1.00 47.64 O ANISOU 1477 OE1 GLN B 192 5284 7666 5151 160 83 21 O ATOM 1478 NE2 GLN B 192 29.707 2.452 54.064 1.00 49.55 N ANISOU 1478 NE2 GLN B 192 5390 8157 5281 415 84 -61 N ATOM 1479 N THR B 193 29.104 4.593 58.372 1.00 46.77 N ANISOU 1479 N THR B 193 5208 7415 5147 31 -37 45 N ATOM 1480 CA THR B 193 28.111 5.426 59.061 1.00 45.46 C ANISOU 1480 CA THR B 193 5150 7084 5039 -77 -59 61 C ATOM 1481 C THR B 193 26.778 5.351 58.313 1.00 43.90 C ANISOU 1481 C THR B 193 5053 6772 4856 -66 -29 46 C ATOM 1482 O THR B 193 26.754 5.248 57.081 1.00 44.16 O ANISOU 1482 O THR B 193 5053 6870 4857 -40 12 50 O ATOM 1483 CB THR B 193 28.553 6.901 59.184 1.00 45.95 C ANISOU 1483 CB THR B 193 5164 7180 5117 -237 -81 127 C ATOM 1484 OG1 THR B 193 28.619 7.497 57.885 1.00 46.77 O ANISOU 1484 OG1 THR B 193 5213 7361 5195 -297 -43 176 O ATOM 1485 CG2 THR B 193 29.918 7.018 59.874 1.00 46.98 C ANISOU 1485 CG2 THR B 193 5182 7435 5233 -261 -116 150 C ATOM 1486 N TYR B 194 25.681 5.391 59.066 1.00 42.22 N ANISOU 1486 N TYR B 194 4955 6405 4683 -81 -50 30 N ATOM 1487 CA TYR B 194 24.327 5.361 58.510 1.00 40.90 C ANISOU 1487 CA TYR B 194 4883 6126 4531 -79 -28 19 C ATOM 1488 C TYR B 194 23.567 6.580 59.001 1.00 39.64 C ANISOU 1488 C TYR B 194 4786 5874 4400 -184 -45 38 C ATOM 1489 O TYR B 194 23.535 6.844 60.205 1.00 39.20 O ANISOU 1489 O TYR B 194 4758 5777 4359 -205 -85 32 O ATOM 1490 CB TYR B 194 23.604 4.081 58.932 1.00 40.82 C ANISOU 1490 CB TYR B 194 4950 6028 4531 18 -44 -18 C ATOM 1491 CG TYR B 194 24.249 2.831 58.384 1.00 41.76 C ANISOU 1491 CG TYR B 194 5033 6211 4625 141 -48 -52 C ATOM 1492 CD1 TYR B 194 23.999 2.413 57.073 1.00 42.05 C ANISOU 1492 CD1 TYR B 194 5072 6267 4640 200 -22 -75 C ATOM 1493 CD2 TYR B 194 25.128 2.073 59.161 1.00 42.19 C ANISOU 1493 CD2 TYR B 194 5052 6308 4671 211 -86 -69 C ATOM 1494 CE1 TYR B 194 24.601 1.274 56.558 1.00 42.77 C ANISOU 1494 CE1 TYR B 194 5135 6418 4699 334 -40 -122 C ATOM 1495 CE2 TYR B 194 25.730 0.930 58.654 1.00 42.96 C ANISOU 1495 CE2 TYR B 194 5123 6460 4740 343 -104 -112 C ATOM 1496 CZ TYR B 194 25.465 0.534 57.354 1.00 43.21 C ANISOU 1496 CZ TYR B 194 5161 6509 4748 410 -84 -143 C ATOM 1497 OH TYR B 194 26.054 -0.598 56.847 1.00 43.97 O ANISOU 1497 OH TYR B 194 5238 6659 4809 562 -116 -201 O ATOM 1498 N ILE B 195 22.979 7.327 58.065 1.00 38.65 N ANISOU 1498 N ILE B 195 4684 5722 4278 -240 -23 58 N ATOM 1499 CA ILE B 195 22.223 8.545 58.373 1.00 38.19 C ANISOU 1499 CA ILE B 195 4694 5572 4244 -326 -50 69 C ATOM 1500 C ILE B 195 20.888 8.526 57.620 1.00 37.44 C ANISOU 1500 C ILE B 195 4675 5397 4153 -310 -20 57 C ATOM 1501 O ILE B 195 20.880 8.395 56.393 1.00 37.74 O ANISOU 1501 O ILE B 195 4689 5474 4175 -304 18 71 O ATOM 1502 CB ILE B 195 23.021 9.819 57.984 1.00 38.62 C ANISOU 1502 CB ILE B 195 4695 5675 4305 -442 -78 121 C ATOM 1503 CG1 ILE B 195 24.402 9.811 58.668 1.00 39.27 C ANISOU 1503 CG1 ILE B 195 4686 5853 4382 -466 -110 140 C ATOM 1504 CG2 ILE B 195 22.220 11.082 58.316 1.00 38.32 C ANISOU 1504 CG2 ILE B 195 4747 5518 4295 -517 -130 122 C ATOM 1505 CD1 ILE B 195 25.243 11.050 58.449 1.00 40.21 C ANISOU 1505 CD1 ILE B 195 4748 6019 4512 -600 -157 206 C ATOM 1506 N CYS B 196 19.772 8.644 58.343 1.00 36.63 N ANISOU 1506 N CYS B 196 4657 5200 4062 -298 -38 32 N ATOM 1507 CA CYS B 196 18.469 8.839 57.702 1.00 36.29 C ANISOU 1507 CA CYS B 196 4681 5086 4020 -294 -17 25 C ATOM 1508 C CYS B 196 18.273 10.329 57.441 1.00 36.45 C ANISOU 1508 C CYS B 196 4733 5065 4052 -376 -48 40 C ATOM 1509 O CYS B 196 18.629 11.154 58.280 1.00 36.86 O ANISOU 1509 O CYS B 196 4794 5097 4114 -418 -104 36 O ATOM 1510 CB CYS B 196 17.316 8.264 58.540 1.00 35.79 C ANISOU 1510 CB CYS B 196 4679 4966 3953 -242 -22 1 C ATOM 1511 SG CYS B 196 16.928 9.130 60.080 1.00 36.03 S ANISOU 1511 SG CYS B 196 4751 4966 3974 -254 -76 -21 S ATOM 1512 N ASN B 197 17.735 10.657 56.267 1.00 36.58 N ANISOU 1512 N ASN B 197 4769 5063 4067 -396 -22 55 N ATOM 1513 CA ASN B 197 17.440 12.038 55.882 1.00 36.90 C ANISOU 1513 CA ASN B 197 4852 5047 4120 -471 -61 75 C ATOM 1514 C ASN B 197 15.932 12.174 55.772 1.00 36.14 C ANISOU 1514 C ASN B 197 4840 4872 4021 -431 -55 41 C ATOM 1515 O ASN B 197 15.319 11.562 54.905 1.00 35.79 O ANISOU 1515 O ASN B 197 4799 4833 3965 -396 -5 42 O ATOM 1516 CB ASN B 197 18.094 12.395 54.536 1.00 37.48 C ANISOU 1516 CB ASN B 197 4871 5182 4187 -535 -39 134 C ATOM 1517 CG ASN B 197 19.474 11.798 54.380 1.00 38.08 C ANISOU 1517 CG ASN B 197 4837 5388 4245 -539 -14 165 C ATOM 1518 OD1 ASN B 197 19.665 10.854 53.621 1.00 38.34 O ANISOU 1518 OD1 ASN B 197 4820 5499 4249 -478 43 162 O ATOM 1519 ND2 ASN B 197 20.439 12.334 55.109 1.00 38.75 N ANISOU 1519 ND2 ASN B 197 4882 5499 4344 -602 -65 189 N ATOM 1520 N VAL B 198 15.343 12.969 56.658 1.00 36.41 N ANISOU 1520 N VAL B 198 4938 4840 4057 -427 -112 8 N ATOM 1521 CA VAL B 198 13.899 13.178 56.701 1.00 36.05 C ANISOU 1521 CA VAL B 198 4961 4739 3996 -378 -113 -28 C ATOM 1522 C VAL B 198 13.592 14.547 56.110 1.00 36.48 C ANISOU 1522 C VAL B 198 5076 4720 4063 -426 -167 -23 C ATOM 1523 O VAL B 198 14.246 15.530 56.450 1.00 37.44 O ANISOU 1523 O VAL B 198 5217 4803 4205 -482 -244 -17 O ATOM 1524 CB VAL B 198 13.366 13.100 58.152 1.00 36.13 C ANISOU 1524 CB VAL B 198 4996 4749 3982 -314 -143 -76 C ATOM 1525 CG1 VAL B 198 11.844 13.221 58.177 1.00 35.87 C ANISOU 1525 CG1 VAL B 198 5014 4697 3919 -254 -135 -108 C ATOM 1526 CG2 VAL B 198 13.818 11.797 58.810 1.00 35.84 C ANISOU 1526 CG2 VAL B 198 4903 4780 3937 -281 -105 -66 C ATOM 1527 N ASN B 199 12.602 14.602 55.225 1.00 36.37 N ANISOU 1527 N ASN B 199 5097 4680 4042 -407 -139 -24 N ATOM 1528 CA ASN B 199 12.172 15.850 54.607 1.00 36.81 C ANISOU 1528 CA ASN B 199 5220 4658 4108 -443 -195 -18 C ATOM 1529 C ASN B 199 10.656 15.954 54.749 1.00 35.99 C ANISOU 1529 C ASN B 199 5176 4522 3977 -359 -195 -72 C ATOM 1530 O ASN B 199 9.930 15.045 54.344 1.00 35.29 O ANISOU 1530 O ASN B 199 5065 4474 3870 -317 -125 -72 O ATOM 1531 CB ASN B 199 12.592 15.871 53.130 1.00 37.43 C ANISOU 1531 CB ASN B 199 5267 4758 4196 -511 -158 49 C ATOM 1532 CG ASN B 199 12.391 17.229 52.469 1.00 38.49 C ANISOU 1532 CG ASN B 199 5468 4808 4347 -574 -231 78 C ATOM 1533 OD1 ASN B 199 12.351 18.267 53.130 1.00 39.83 O ANISOU 1533 OD1 ASN B 199 5706 4894 4535 -588 -331 54 O ATOM 1534 ND2 ASN B 199 12.276 17.225 51.150 1.00 38.78 N ANISOU 1534 ND2 ASN B 199 5492 4866 4378 -607 -192 128 N ATOM 1535 N HIS B 200 10.198 17.053 55.346 1.00 36.23 N ANISOU 1535 N HIS B 200 5280 4484 4000 -332 -283 -119 N ATOM 1536 CA HIS B 200 8.776 17.324 55.562 1.00 36.08 C ANISOU 1536 CA HIS B 200 5314 4452 3943 -238 -295 -178 C ATOM 1537 C HIS B 200 8.442 18.686 54.955 1.00 36.57 C ANISOU 1537 C HIS B 200 5466 4408 4020 -253 -384 -189 C ATOM 1538 O HIS B 200 8.586 19.725 55.608 1.00 36.93 O ANISOU 1538 O HIS B 200 5579 4380 4071 -239 -495 -232 O ATOM 1539 CB HIS B 200 8.457 17.283 57.063 1.00 36.37 C ANISOU 1539 CB HIS B 200 5353 4529 3937 -150 -327 -244 C ATOM 1540 CG HIS B 200 6.999 17.410 57.378 1.00 36.31 C ANISOU 1540 CG HIS B 200 5370 4555 3870 -41 -327 -301 C ATOM 1541 ND1 HIS B 200 6.046 16.595 56.807 1.00 35.78 N ANISOU 1541 ND1 HIS B 200 5266 4549 3782 -18 -245 -278 N ATOM 1542 CD2 HIS B 200 6.332 18.237 58.216 1.00 36.74 C ANISOU 1542 CD2 HIS B 200 5476 4607 3875 58 -404 -381 C ATOM 1543 CE1 HIS B 200 4.855 16.929 57.267 1.00 35.79 C ANISOU 1543 CE1 HIS B 200 5285 4593 3722 82 -265 -332 C ATOM 1544 NE2 HIS B 200 4.999 17.920 58.127 1.00 36.65 N ANISOU 1544 NE2 HIS B 200 5446 4670 3807 139 -359 -399 N ATOM 1545 N LYS B 201 8.005 18.664 53.695 1.00 36.57 N ANISOU 1545 N LYS B 201 5472 4395 4028 -280 -346 -150 N ATOM 1546 CA LYS B 201 7.774 19.886 52.913 1.00 37.40 C ANISOU 1546 CA LYS B 201 5661 4396 4153 -313 -428 -138 C ATOM 1547 C LYS B 201 6.673 20.794 53.460 1.00 37.57 C ANISOU 1547 C LYS B 201 5775 4356 4144 -206 -517 -226 C ATOM 1548 O LYS B 201 6.811 22.009 53.371 1.00 38.44 O ANISOU 1548 O LYS B 201 5975 4350 4279 -227 -640 -235 O ATOM 1549 CB LYS B 201 7.480 19.562 51.439 1.00 37.52 C ANISOU 1549 CB LYS B 201 5656 4429 4171 -353 -358 -78 C ATOM 1550 CG LYS B 201 8.665 18.991 50.678 1.00 37.96 C ANISOU 1550 CG LYS B 201 5633 4542 4248 -455 -297 9 C ATOM 1551 CD LYS B 201 8.255 18.492 49.299 1.00 37.96 C ANISOU 1551 CD LYS B 201 5606 4583 4233 -464 -219 49 C ATOM 1552 CE LYS B 201 9.438 17.883 48.558 1.00 38.37 C ANISOU 1552 CE LYS B 201 5570 4722 4288 -540 -158 125 C ATOM 1553 NZ LYS B 201 9.002 16.898 47.533 1.00 38.16 N ANISOU 1553 NZ LYS B 201 5501 4765 4233 -504 -65 131 N ATOM 1554 N PRO B 202 5.583 20.220 54.021 1.00 36.86 N ANISOU 1554 N PRO B 202 5660 4347 3998 -89 -467 -287 N ATOM 1555 CA PRO B 202 4.531 21.076 54.581 1.00 37.47 C ANISOU 1555 CA PRO B 202 5811 4396 4028 35 -551 -379 C ATOM 1556 C PRO B 202 4.962 22.004 55.729 1.00 38.43 C ANISOU 1556 C PRO B 202 6000 4456 4145 81 -681 -450 C ATOM 1557 O PRO B 202 4.330 23.036 55.924 1.00 39.59 O ANISOU 1557 O PRO B 202 6240 4533 4270 171 -791 -525 O ATOM 1558 CB PRO B 202 3.485 20.068 55.069 1.00 36.92 C ANISOU 1558 CB PRO B 202 5665 4471 3891 130 -455 -407 C ATOM 1559 CG PRO B 202 3.674 18.887 54.186 1.00 35.93 C ANISOU 1559 CG PRO B 202 5463 4396 3794 47 -337 -324 C ATOM 1560 CD PRO B 202 5.159 18.807 53.997 1.00 35.87 C ANISOU 1560 CD PRO B 202 5441 4342 3845 -68 -340 -266 C ATOM 1561 N SER B 203 6.009 21.641 56.471 1.00 38.48 N ANISOU 1561 N SER B 203 5964 4485 4171 30 -676 -433 N ATOM 1562 CA SER B 203 6.558 22.493 57.532 1.00 39.49 C ANISOU 1562 CA SER B 203 6156 4548 4301 60 -808 -498 C ATOM 1563 C SER B 203 7.922 23.105 57.193 1.00 40.18 C ANISOU 1563 C SER B 203 6277 4518 4470 -89 -892 -431 C ATOM 1564 O SER B 203 8.508 23.779 58.046 1.00 40.93 O ANISOU 1564 O SER B 203 6426 4549 4578 -85 -1011 -476 O ATOM 1565 CB SER B 203 6.677 21.701 58.837 1.00 39.23 C ANISOU 1565 CB SER B 203 6050 4641 4215 127 -758 -536 C ATOM 1566 OG SER B 203 7.854 20.911 58.860 1.00 38.71 O ANISOU 1566 OG SER B 203 5907 4607 4193 13 -694 -459 O ATOM 1567 N ASN B 204 8.425 22.859 55.976 1.00 39.82 N ANISOU 1567 N ASN B 204 6196 4461 4474 -220 -832 -324 N ATOM 1568 CA ASN B 204 9.721 23.377 55.512 1.00 40.56 C ANISOU 1568 CA ASN B 204 6295 4479 4637 -380 -898 -234 C ATOM 1569 C ASN B 204 10.880 22.876 56.390 1.00 40.51 C ANISOU 1569 C ASN B 204 6218 4533 4643 -428 -884 -219 C ATOM 1570 O ASN B 204 11.785 23.637 56.724 1.00 41.22 O ANISOU 1570 O ASN B 204 6345 4542 4776 -509 -1004 -200 O ATOM 1571 CB ASN B 204 9.679 24.920 55.440 1.00 42.10 C ANISOU 1571 CB ASN B 204 6631 4497 4868 -401 -1090 -254 C ATOM 1572 CG ASN B 204 10.889 25.526 54.745 1.00 43.07 C ANISOU 1572 CG ASN B 204 6758 4544 5064 -592 -1166 -130 C ATOM 1573 OD1 ASN B 204 11.433 26.531 55.198 1.00 44.39 O ANISOU 1573 OD1 ASN B 204 7009 4585 5273 -644 -1334 -135 O ATOM 1574 ND2 ASN B 204 11.302 24.936 53.641 1.00 42.54 N ANISOU 1574 ND2 ASN B 204 6600 4558 5006 -695 -1051 -17 N ATOM 1575 N THR B 205 10.841 21.585 56.727 1.00 39.64 N ANISOU 1575 N THR B 205 6006 4558 4497 -383 -747 -223 N ATOM 1576 CA THR B 205 11.773 20.962 57.673 1.00 40.15 C ANISOU 1576 CA THR B 205 6001 4694 4562 -398 -724 -223 C ATOM 1577 C THR B 205 12.614 19.866 57.010 1.00 39.79 C ANISOU 1577 C THR B 205 5839 4748 4532 -481 -602 -132 C ATOM 1578 O THR B 205 12.079 19.032 56.274 1.00 39.07 O ANISOU 1578 O THR B 205 5704 4718 4422 -457 -492 -109 O ATOM 1579 CB THR B 205 11.013 20.321 58.865 1.00 39.80 C ANISOU 1579 CB THR B 205 5939 4732 4450 -255 -684 -311 C ATOM 1580 OG1 THR B 205 10.224 21.312 59.528 1.00 40.59 O ANISOU 1580 OG1 THR B 205 6138 4767 4517 -149 -797 -409 O ATOM 1581 CG2 THR B 205 11.981 19.710 59.886 1.00 39.96 C ANISOU 1581 CG2 THR B 205 5894 4821 4468 -267 -670 -309 C ATOM 1582 N LYS B 206 13.921 19.885 57.284 1.00 40.40 N ANISOU 1582 N LYS B 206 5867 4842 4640 -571 -630 -85 N ATOM 1583 CA LYS B 206 14.836 18.787 56.965 1.00 40.35 C ANISOU 1583 CA LYS B 206 5743 4953 4636 -618 -526 -21 C ATOM 1584 C LYS B 206 15.603 18.398 58.217 1.00 40.88 C ANISOU 1584 C LYS B 206 5769 5067 4698 -600 -543 -50 C ATOM 1585 O LYS B 206 16.247 19.250 58.831 1.00 41.48 O ANISOU 1585 O LYS B 206 5877 5085 4799 -650 -655 -56 O ATOM 1586 CB LYS B 206 15.854 19.190 55.897 1.00 40.97 C ANISOU 1586 CB LYS B 206 5775 5044 4748 -759 -538 85 C ATOM 1587 CG LYS B 206 15.425 18.933 54.461 1.00 40.96 C ANISOU 1587 CG LYS B 206 5753 5074 4736 -777 -459 139 C ATOM 1588 CD LYS B 206 14.982 20.200 53.744 1.00 41.94 C ANISOU 1588 CD LYS B 206 5967 5085 4883 -838 -550 171 C ATOM 1589 CE LYS B 206 15.339 20.168 52.267 1.00 42.21 C ANISOU 1589 CE LYS B 206 5943 5182 4913 -927 -496 276 C ATOM 1590 NZ LYS B 206 15.399 21.545 51.716 1.00 43.43 N ANISOU 1590 NZ LYS B 206 6171 5228 5101 -1037 -618 344 N ATOM 1591 N VAL B 207 15.545 17.115 58.577 1.00 40.93 N ANISOU 1591 N VAL B 207 5708 5170 4675 -533 -443 -63 N ATOM 1592 CA VAL B 207 16.282 16.573 59.722 1.00 41.33 C ANISOU 1592 CA VAL B 207 5710 5278 4715 -511 -447 -82 C ATOM 1593 C VAL B 207 17.136 15.395 59.248 1.00 41.15 C ANISOU 1593 C VAL B 207 5580 5359 4694 -534 -354 -26 C ATOM 1594 O VAL B 207 16.637 14.504 58.561 1.00 40.16 O ANISOU 1594 O VAL B 207 5432 5273 4555 -495 -266 -15 O ATOM 1595 CB VAL B 207 15.328 16.104 60.848 1.00 41.21 C ANISOU 1595 CB VAL B 207 5723 5285 4651 -388 -433 -156 C ATOM 1596 CG1 VAL B 207 16.105 15.802 62.129 1.00 41.62 C ANISOU 1596 CG1 VAL B 207 5740 5384 4691 -369 -463 -178 C ATOM 1597 CG2 VAL B 207 14.249 17.149 61.114 1.00 41.49 C ANISOU 1597 CG2 VAL B 207 5857 5241 4665 -330 -509 -223 C ATOM 1598 N ASP B 208 18.422 15.421 59.604 1.00 42.39 N ANISOU 1598 N ASP B 208 5677 5561 4868 -593 -384 4 N ATOM 1599 CA ASP B 208 19.352 14.317 59.367 1.00 42.76 C ANISOU 1599 CA ASP B 208 5619 5720 4907 -592 -311 43 C ATOM 1600 C ASP B 208 19.774 13.734 60.709 1.00 43.05 C ANISOU 1600 C ASP B 208 5633 5794 4931 -538 -325 6 C ATOM 1601 O ASP B 208 20.337 14.452 61.531 1.00 44.08 O ANISOU 1601 O ASP B 208 5774 5902 5073 -575 -408 -7 O ATOM 1602 CB ASP B 208 20.599 14.812 58.630 1.00 43.64 C ANISOU 1602 CB ASP B 208 5655 5886 5038 -707 -332 121 C ATOM 1603 CG ASP B 208 20.312 15.237 57.197 1.00 43.90 C ANISOU 1603 CG ASP B 208 5691 5914 5074 -763 -306 176 C ATOM 1604 OD1 ASP B 208 19.601 14.509 56.475 1.00 42.62 O ANISOU 1604 OD1 ASP B 208 5532 5771 4891 -698 -225 164 O ATOM 1605 OD2 ASP B 208 20.824 16.301 56.785 1.00 45.54 O ANISOU 1605 OD2 ASP B 208 5897 6100 5306 -879 -375 238 O ATOM 1606 N LYS B 209 19.513 12.443 60.924 1.00 43.02 N ANISOU 1606 N LYS B 209 5601 5841 4903 -455 -254 -8 N ATOM 1607 CA LYS B 209 19.874 11.753 62.176 1.00 43.15 C ANISOU 1607 CA LYS B 209 5595 5897 4902 -401 -264 -33 C ATOM 1608 C LYS B 209 20.861 10.612 61.918 1.00 43.08 C ANISOU 1608 C LYS B 209 5498 5979 4892 -382 -216 -4 C ATOM 1609 O LYS B 209 20.535 9.659 61.211 1.00 42.72 O ANISOU 1609 O LYS B 209 5440 5952 4839 -335 -156 5 O ATOM 1610 CB LYS B 209 18.610 11.204 62.852 1.00 42.89 C ANISOU 1610 CB LYS B 209 5615 5844 4837 -315 -243 -69 C ATOM 1611 CG LYS B 209 18.806 10.535 64.216 1.00 43.34 C ANISOU 1611 CG LYS B 209 5656 5946 4866 -258 -257 -85 C ATOM 1612 CD LYS B 209 19.509 11.404 65.256 1.00 44.19 C ANISOU 1612 CD LYS B 209 5767 6054 4970 -278 -339 -115 C ATOM 1613 CE LYS B 209 18.840 12.761 65.434 1.00 44.88 C ANISOU 1613 CE LYS B 209 5933 6070 5051 -287 -408 -161 C ATOM 1614 NZ LYS B 209 19.300 13.484 66.651 1.00 45.89 N ANISOU 1614 NZ LYS B 209 6081 6192 5163 -276 -502 -208 N ATOM 1615 N LYS B 210 22.061 10.717 62.489 1.00 43.68 N ANISOU 1615 N LYS B 210 5515 6110 4973 -410 -254 7 N ATOM 1616 CA LYS B 210 23.036 9.621 62.464 1.00 44.20 C ANISOU 1616 CA LYS B 210 5496 6271 5028 -370 -221 22 C ATOM 1617 C LYS B 210 22.582 8.526 63.430 1.00 43.61 C ANISOU 1617 C LYS B 210 5449 6187 4935 -277 -212 -6 C ATOM 1618 O LYS B 210 22.089 8.826 64.518 1.00 43.02 O ANISOU 1618 O LYS B 210 5422 6076 4848 -264 -249 -30 O ATOM 1619 CB LYS B 210 24.425 10.128 62.855 1.00 45.49 C ANISOU 1619 CB LYS B 210 5581 6503 5198 -432 -270 45 C ATOM 1620 CG LYS B 210 25.541 9.111 62.657 1.00 46.38 C ANISOU 1620 CG LYS B 210 5591 6737 5293 -387 -238 61 C ATOM 1621 CD LYS B 210 26.905 9.676 63.026 1.00 47.64 C ANISOU 1621 CD LYS B 210 5661 6983 5456 -458 -288 91 C ATOM 1622 CE LYS B 210 26.990 10.025 64.506 1.00 48.36 C ANISOU 1622 CE LYS B 210 5791 7027 5555 -462 -361 59 C ATOM 1623 NZ LYS B 210 28.395 10.101 64.997 1.00 49.71 N ANISOU 1623 NZ LYS B 210 5864 7301 5724 -497 -404 81 N ATOM 1624 N VAL B 211 22.751 7.265 63.027 1.00 43.70 N ANISOU 1624 N VAL B 211 5430 6235 4939 -210 -171 0 N ATOM 1625 CA VAL B 211 22.233 6.112 63.778 1.00 43.51 C ANISOU 1625 CA VAL B 211 5441 6188 4903 -133 -172 -7 C ATOM 1626 C VAL B 211 23.378 5.158 64.101 1.00 44.02 C ANISOU 1626 C VAL B 211 5444 6321 4961 -78 -185 -6 C ATOM 1627 O VAL B 211 23.795 4.372 63.252 1.00 43.80 O ANISOU 1627 O VAL B 211 5383 6327 4933 -29 -164 -7 O ATOM 1628 CB VAL B 211 21.120 5.370 62.995 1.00 42.88 C ANISOU 1628 CB VAL B 211 5412 6054 4827 -96 -135 -3 C ATOM 1629 CG1 VAL B 211 20.516 4.254 63.843 1.00 42.70 C ANISOU 1629 CG1 VAL B 211 5427 6001 4795 -42 -152 10 C ATOM 1630 CG2 VAL B 211 20.036 6.345 62.548 1.00 42.59 C ANISOU 1630 CG2 VAL B 211 5427 5962 4793 -144 -120 -6 C ATOM 1631 N GLU B 212 23.876 5.239 65.337 1.00 44.82 N ANISOU 1631 N GLU B 212 5531 6447 5053 -76 -226 -9 N ATOM 1632 CA GLU B 212 25.013 4.426 65.795 1.00 45.81 C ANISOU 1632 CA GLU B 212 5597 6640 5170 -22 -249 -10 C ATOM 1633 C GLU B 212 24.544 3.252 66.662 1.00 45.27 C ANISOU 1633 C GLU B 212 5575 6534 5090 48 -271 -1 C ATOM 1634 O GLU B 212 23.450 3.309 67.232 1.00 44.83 O ANISOU 1634 O GLU B 212 5582 6425 5025 37 -274 12 O ATOM 1635 CB GLU B 212 26.009 5.296 66.573 1.00 46.75 C ANISOU 1635 CB GLU B 212 5661 6818 5284 -72 -290 -13 C ATOM 1636 CG GLU B 212 26.656 6.390 65.732 1.00 47.63 C ANISOU 1636 CG GLU B 212 5714 6975 5409 -159 -286 -1 C ATOM 1637 CD GLU B 212 27.972 6.893 66.304 1.00 49.18 C ANISOU 1637 CD GLU B 212 5827 7255 5603 -204 -334 8 C ATOM 1638 OE1 GLU B 212 28.061 7.103 67.536 1.00 50.09 O ANISOU 1638 OE1 GLU B 212 5965 7354 5713 -203 -386 -9 O ATOM 1639 OE2 GLU B 212 28.925 7.090 65.520 1.00 50.13 O ANISOU 1639 OE2 GLU B 212 5854 7473 5722 -240 -323 35 O ATOM 1640 N PRO B 213 25.358 2.177 66.752 1.00 45.49 N ANISOU 1640 N PRO B 213 5570 6598 5116 123 -293 -2 N ATOM 1641 CA PRO B 213 24.992 1.050 67.628 1.00 45.48 C ANISOU 1641 CA PRO B 213 5618 6554 5109 179 -332 21 C ATOM 1642 C PRO B 213 25.044 1.391 69.127 1.00 45.65 C ANISOU 1642 C PRO B 213 5641 6600 5105 159 -365 35 C ATOM 1643 O PRO B 213 25.859 2.221 69.543 1.00 45.44 O ANISOU 1643 O PRO B 213 5562 6635 5069 129 -376 14 O ATOM 1644 CB PRO B 213 26.014 -0.045 67.269 1.00 45.91 C ANISOU 1644 CB PRO B 213 5637 6642 5166 273 -360 4 C ATOM 1645 CG PRO B 213 27.120 0.646 66.558 1.00 46.37 C ANISOU 1645 CG PRO B 213 5599 6803 5216 262 -333 -25 C ATOM 1646 CD PRO B 213 26.556 1.888 65.940 1.00 45.76 C ANISOU 1646 CD PRO B 213 5524 6716 5147 166 -286 -21 C ATOM 1647 N LYS B 214 24.169 0.749 69.906 1.00 45.78 N ANISOU 1647 N LYS B 214 5713 6575 5105 172 -386 76 N ATOM 1648 CA LYS B 214 24.011 1.007 71.341 1.00 46.16 C ANISOU 1648 CA LYS B 214 5765 6659 5112 162 -414 95 C ATOM 1649 C LYS B 214 24.668 -0.105 72.144 1.00 46.91 C ANISOU 1649 C LYS B 214 5854 6772 5199 220 -467 126 C ATOM 1650 O LYS B 214 24.296 -1.268 72.005 1.00 47.25 O ANISOU 1650 O LYS B 214 5938 6759 5256 252 -494 169 O ATOM 1651 CB LYS B 214 22.524 1.087 71.701 1.00 45.44 C ANISOU 1651 CB LYS B 214 5728 6544 4994 134 -399 135 C TER 1652 LYS B 214 ATOM 1653 N THR C 204 -26.894 22.790 13.453 1.00 55.33 N ANISOU 1653 N THR C 204 7604 8153 5265 2390 -889 -968 N ATOM 1654 CA THR C 204 -25.839 22.120 12.634 1.00 53.78 C ANISOU 1654 CA THR C 204 7493 7788 5151 2160 -848 -844 C ATOM 1655 C THR C 204 -24.632 23.034 12.427 1.00 53.55 C ANISOU 1655 C THR C 204 7705 7450 5190 2160 -919 -792 C ATOM 1656 O THR C 204 -24.793 24.213 12.112 1.00 55.02 O ANISOU 1656 O THR C 204 8018 7517 5371 2334 -1026 -818 O ATOM 1657 CB THR C 204 -26.390 21.699 11.260 1.00 53.68 C ANISOU 1657 CB THR C 204 7414 7856 5127 2121 -862 -809 C ATOM 1658 OG1 THR C 204 -27.529 20.854 11.448 1.00 54.10 O ANISOU 1658 OG1 THR C 204 7229 8201 5128 2100 -797 -872 O ATOM 1659 CG2 THR C 204 -25.335 20.955 10.445 1.00 52.20 C ANISOU 1659 CG2 THR C 204 7300 7522 5011 1895 -815 -698 C ATOM 1660 N VAL C 205 -23.435 22.473 12.607 1.00 52.30 N ANISOU 1660 N VAL C 205 7608 7166 5098 1965 -857 -720 N ATOM 1661 CA VAL C 205 -22.170 23.206 12.485 1.00 51.75 C ANISOU 1661 CA VAL C 205 7740 6821 5102 1918 -905 -673 C ATOM 1662 C VAL C 205 -21.205 22.393 11.615 1.00 50.50 C ANISOU 1662 C VAL C 205 7610 6577 5000 1697 -846 -557 C ATOM 1663 O VAL C 205 -20.930 21.232 11.928 1.00 49.69 O ANISOU 1663 O VAL C 205 7407 6566 4907 1552 -751 -532 O ATOM 1664 CB VAL C 205 -21.506 23.447 13.861 1.00 51.48 C ANISOU 1664 CB VAL C 205 7741 6737 5082 1921 -896 -733 C ATOM 1665 CG1 VAL C 205 -20.322 24.401 13.724 1.00 51.55 C ANISOU 1665 CG1 VAL C 205 7952 6465 5172 1886 -964 -712 C ATOM 1666 CG2 VAL C 205 -22.518 23.980 14.869 1.00 52.69 C ANISOU 1666 CG2 VAL C 205 7822 7038 5158 2133 -929 -863 C ATOM 1667 N PRO C 206 -20.680 22.995 10.530 1.00 50.49 N ANISOU 1667 N PRO C 206 7749 6401 5033 1676 -900 -483 N ATOM 1668 CA PRO C 206 -19.741 22.274 9.673 1.00 49.15 C ANISOU 1668 CA PRO C 206 7602 6167 4905 1479 -844 -382 C ATOM 1669 C PRO C 206 -18.331 22.255 10.279 1.00 48.20 C ANISOU 1669 C PRO C 206 7557 5901 4854 1345 -813 -358 C ATOM 1670 O PRO C 206 -17.963 23.197 10.987 1.00 49.06 O ANISOU 1670 O PRO C 206 7764 5886 4992 1407 -867 -403 O ATOM 1671 CB PRO C 206 -19.762 23.093 8.385 1.00 50.07 C ANISOU 1671 CB PRO C 206 7845 6167 5012 1533 -915 -311 C ATOM 1672 CG PRO C 206 -19.995 24.488 8.853 1.00 51.59 C ANISOU 1672 CG PRO C 206 8167 6225 5211 1708 -1010 -357 C ATOM 1673 CD PRO C 206 -20.867 24.386 10.076 1.00 51.98 C ANISOU 1673 CD PRO C 206 8095 6434 5222 1834 -1010 -483 C ATOM 1674 N PRO C 207 -17.547 21.192 10.010 1.00 46.63 N ANISOU 1674 N PRO C 207 7311 5722 4683 1169 -732 -300 N ATOM 1675 CA PRO C 207 -16.204 21.089 10.597 1.00 45.72 C ANISOU 1675 CA PRO C 207 7242 5504 4623 1052 -704 -285 C ATOM 1676 C PRO C 207 -15.156 21.980 9.947 1.00 45.94 C ANISOU 1676 C PRO C 207 7419 5331 4706 984 -745 -228 C ATOM 1677 O PRO C 207 -15.290 22.336 8.778 1.00 46.14 O ANISOU 1677 O PRO C 207 7507 5303 4722 984 -768 -160 O ATOM 1678 CB PRO C 207 -15.821 19.620 10.368 1.00 44.49 C ANISOU 1678 CB PRO C 207 6986 5445 4474 910 -607 -241 C ATOM 1679 CG PRO C 207 -16.667 19.167 9.241 1.00 44.74 C ANISOU 1679 CG PRO C 207 6964 5565 4471 914 -597 -215 C ATOM 1680 CD PRO C 207 -17.928 19.972 9.275 1.00 45.76 C ANISOU 1680 CD PRO C 207 7086 5750 4551 1085 -666 -267 C ATOM 1681 N AMET C 208 -14.130 22.341 10.714 0.50 46.22 N ANISOU 1681 N AMET C 208 7503 5268 4792 926 -754 -256 N ATOM 1682 N BMET C 208 -14.131 22.329 10.721 0.50 46.02 N ANISOU 1682 N BMET C 208 7476 5244 4766 926 -753 -257 N ATOM 1683 CA AMET C 208 -12.942 23.010 10.182 0.50 46.74 C ANISOU 1683 CA AMET C 208 7682 5157 4921 810 -771 -202 C ATOM 1684 CA BMET C 208 -12.932 22.987 10.208 0.50 46.42 C ANISOU 1684 CA BMET C 208 7638 5119 4880 808 -770 -204 C ATOM 1685 C AMET C 208 -11.878 21.955 9.884 0.50 45.60 C ANISOU 1685 C AMET C 208 7466 5068 4792 643 -690 -149 C ATOM 1686 C BMET C 208 -11.901 21.914 9.887 0.50 45.38 C ANISOU 1686 C BMET C 208 7434 5045 4762 644 -688 -149 C ATOM 1687 O AMET C 208 -11.254 21.418 10.805 0.50 45.36 O ANISOU 1687 O AMET C 208 7371 5091 4773 601 -661 -195 O ATOM 1688 O BMET C 208 -11.320 21.318 10.801 0.50 45.06 O ANISOU 1688 O BMET C 208 7324 5067 4730 605 -656 -194 O ATOM 1689 CB AMET C 208 -12.404 24.037 11.180 0.50 47.74 C ANISOU 1689 CB AMET C 208 7889 5150 5100 831 -834 -286 C ATOM 1690 CB BMET C 208 -12.348 23.933 11.253 0.50 47.09 C ANISOU 1690 CB BMET C 208 7795 5081 5017 823 -828 -289 C ATOM 1691 CG AMET C 208 -13.007 25.426 11.031 0.50 49.44 C ANISOU 1691 CG AMET C 208 8247 5205 5334 956 -927 -310 C ATOM 1692 CG BMET C 208 -13.319 24.974 11.774 0.50 48.28 C ANISOU 1692 CG BMET C 208 8017 5173 5155 1007 -914 -372 C ATOM 1693 SD AMET C 208 -12.483 26.271 9.523 0.50 50.47 S ANISOU 1693 SD AMET C 208 8541 5124 5510 862 -943 -168 S ATOM 1694 SD BMET C 208 -12.504 26.049 12.963 0.50 49.17 S ANISOU 1694 SD BMET C 208 8216 5129 5336 1006 -987 -497 S ATOM 1695 CE AMET C 208 -13.504 25.477 8.283 0.50 49.67 C ANISOU 1695 CE AMET C 208 8371 5187 5313 925 -905 -73 C ATOM 1696 CE BMET C 208 -11.824 24.844 14.097 0.50 47.95 C ANISOU 1696 CE BMET C 208 7901 5170 5148 935 -920 -551 C ATOM 1697 N VAL C 209 -11.682 21.661 8.599 1.00 45.09 N ANISOU 1697 N VAL C 209 7413 5002 4717 567 -656 -57 N ATOM 1698 CA VAL C 209 -10.716 20.649 8.159 1.00 44.13 C ANISOU 1698 CA VAL C 209 7223 4940 4603 427 -580 -13 C ATOM 1699 C VAL C 209 -9.315 21.265 8.029 1.00 44.58 C ANISOU 1699 C VAL C 209 7342 4880 4716 297 -580 17 C ATOM 1700 O VAL C 209 -9.157 22.371 7.514 1.00 45.74 O ANISOU 1700 O VAL C 209 7603 4887 4887 276 -620 62 O ATOM 1701 CB VAL C 209 -11.153 19.978 6.841 1.00 43.75 C ANISOU 1701 CB VAL C 209 7144 4973 4505 409 -542 52 C ATOM 1702 CG1 VAL C 209 -10.142 18.911 6.419 1.00 43.02 C ANISOU 1702 CG1 VAL C 209 6983 4944 4420 282 -466 80 C ATOM 1703 CG2 VAL C 209 -12.548 19.372 6.995 1.00 43.39 C ANISOU 1703 CG2 VAL C 209 7018 5054 4413 518 -543 7 C ATOM 1704 N ASN C 210 -8.310 20.528 8.499 1.00 43.80 N ANISOU 1704 N ASN C 210 7164 4843 4637 210 -534 -6 N ATOM 1705 CA ASN C 210 -6.937 21.016 8.577 1.00 44.07 C ANISOU 1705 CA ASN C 210 7216 4805 4724 82 -533 -5 C ATOM 1706 C ASN C 210 -5.982 19.826 8.427 1.00 42.46 C ANISOU 1706 C ASN C 210 6900 4724 4508 -2 -460 6 C ATOM 1707 O ASN C 210 -6.025 18.899 9.239 1.00 42.34 O ANISOU 1707 O ASN C 210 6804 4808 4476 50 -440 -43 O ATOM 1708 CB ASN C 210 -6.751 21.717 9.928 1.00 45.42 C ANISOU 1708 CB ASN C 210 7406 4917 4934 119 -595 -107 C ATOM 1709 CG ASN C 210 -5.416 22.429 10.057 1.00 47.14 C ANISOU 1709 CG ASN C 210 7645 5047 5219 -22 -610 -128 C ATOM 1710 OD1 ASN C 210 -5.343 23.659 9.978 1.00 49.19 O ANISOU 1710 OD1 ASN C 210 8014 5141 5534 -56 -662 -133 O ATOM 1711 ND2 ASN C 210 -4.354 21.662 10.291 1.00 47.01 N ANISOU 1711 ND2 ASN C 210 7519 5139 5202 -102 -567 -147 N ATOM 1712 N VAL C 211 -5.138 19.844 7.392 1.00 41.32 N ANISOU 1712 N VAL C 211 6756 4577 4368 -121 -419 73 N ATOM 1713 CA VAL C 211 -4.166 18.770 7.150 1.00 39.87 C ANISOU 1713 CA VAL C 211 6466 4513 4169 -188 -352 75 C ATOM 1714 C VAL C 211 -2.768 19.182 7.634 1.00 39.92 C ANISOU 1714 C VAL C 211 6431 4515 4222 -297 -355 37 C ATOM 1715 O VAL C 211 -2.319 20.287 7.351 1.00 40.80 O ANISOU 1715 O VAL C 211 6605 4522 4375 -396 -375 62 O ATOM 1716 CB VAL C 211 -4.128 18.371 5.658 1.00 39.75 C ANISOU 1716 CB VAL C 211 6449 4548 4109 -237 -296 157 C ATOM 1717 CG1 VAL C 211 -3.067 17.308 5.389 1.00 39.39 C ANISOU 1717 CG1 VAL C 211 6293 4626 4046 -293 -231 144 C ATOM 1718 CG2 VAL C 211 -5.493 17.865 5.219 1.00 39.12 C ANISOU 1718 CG2 VAL C 211 6383 4498 3980 -131 -300 169 C ATOM 1719 N THR C 212 -2.090 18.280 8.349 1.00 39.04 N ANISOU 1719 N THR C 212 6215 4516 4103 -280 -336 -21 N ATOM 1720 CA THR C 212 -0.744 18.534 8.890 1.00 39.57 C ANISOU 1720 CA THR C 212 6210 4623 4203 -368 -345 -78 C ATOM 1721 C THR C 212 0.230 17.424 8.516 1.00 38.69 C ANISOU 1721 C THR C 212 5980 4661 4060 -393 -282 -76 C ATOM 1722 O THR C 212 -0.164 16.271 8.377 1.00 37.83 O ANISOU 1722 O THR C 212 5843 4620 3911 -303 -246 -62 O ATOM 1723 CB THR C 212 -0.760 18.641 10.424 1.00 39.98 C ANISOU 1723 CB THR C 212 6240 4688 4264 -286 -407 -180 C ATOM 1724 OG1 THR C 212 -1.195 17.397 10.992 1.00 39.49 O ANISOU 1724 OG1 THR C 212 6128 4726 4150 -156 -384 -188 O ATOM 1725 CG2 THR C 212 -1.692 19.758 10.876 1.00 40.65 C ANISOU 1725 CG2 THR C 212 6437 4632 4377 -243 -475 -206 C ATOM 1726 N ARG C 213 1.501 17.791 8.372 1.00 39.11 N ANISOU 1726 N ARG C 213 5962 4763 4136 -515 -270 -97 N ATOM 1727 CA ARG C 213 2.559 16.879 7.967 1.00 38.88 C ANISOU 1727 CA ARG C 213 5808 4891 4075 -539 -213 -106 C ATOM 1728 C ARG C 213 3.483 16.639 9.147 1.00 39.14 C ANISOU 1728 C ARG C 213 5732 5028 4112 -508 -250 -207 C ATOM 1729 O ARG C 213 3.939 17.591 9.776 1.00 40.55 O ANISOU 1729 O ARG C 213 5900 5173 4335 -585 -302 -268 O ATOM 1730 CB ARG C 213 3.352 17.476 6.806 1.00 40.11 C ANISOU 1730 CB ARG C 213 5939 5064 4236 -707 -161 -50 C ATOM 1731 N SER C 214 3.765 15.373 9.440 1.00 38.24 N ANISOU 1731 N SER C 214 5542 5036 3952 -390 -228 -230 N ATOM 1732 CA SER C 214 4.587 15.001 10.590 1.00 38.34 C ANISOU 1732 CA SER C 214 5452 5167 3947 -319 -268 -319 C ATOM 1733 C SER C 214 5.449 13.767 10.310 1.00 38.32 C ANISOU 1733 C SER C 214 5339 5323 3897 -248 -222 -329 C ATOM 1734 O SER C 214 5.322 13.126 9.260 1.00 37.70 O ANISOU 1734 O SER C 214 5269 5254 3802 -246 -159 -276 O ATOM 1735 CB SER C 214 3.680 14.726 11.784 1.00 37.51 C ANISOU 1735 CB SER C 214 5412 5019 3822 -171 -315 -335 C ATOM 1736 OG SER C 214 2.782 13.674 11.487 1.00 36.33 O ANISOU 1736 OG SER C 214 5320 4838 3645 -66 -269 -267 O ATOM 1737 N GLU C 215 6.328 13.455 11.263 1.00 38.68 N ANISOU 1737 N GLU C 215 5280 5501 3917 -176 -261 -408 N ATOM 1738 CA GLU C 215 7.131 12.229 11.244 1.00 38.91 C ANISOU 1738 CA GLU C 215 5209 5681 3894 -58 -234 -429 C ATOM 1739 C GLU C 215 7.929 12.089 9.942 1.00 39.17 C ANISOU 1739 C GLU C 215 5155 5805 3923 -153 -167 -421 C ATOM 1740 O GLU C 215 7.912 11.038 9.299 1.00 38.71 O ANISOU 1740 O GLU C 215 5095 5778 3833 -66 -116 -394 O ATOM 1741 CB GLU C 215 6.234 10.994 11.473 1.00 37.90 C ANISOU 1741 CB GLU C 215 5175 5487 3737 117 -212 -369 C ATOM 1742 CG GLU C 215 5.327 11.071 12.698 1.00 37.34 C ANISOU 1742 CG GLU C 215 5192 5339 3656 210 -259 -358 C ATOM 1743 CD GLU C 215 4.598 9.765 12.981 1.00 36.61 C ANISOU 1743 CD GLU C 215 5176 5197 3537 367 -224 -293 C ATOM 1744 OE1 GLU C 215 3.931 9.246 12.060 1.00 35.77 O ANISOU 1744 OE1 GLU C 215 5134 5002 3455 347 -168 -238 O ATOM 1745 OE2 GLU C 215 4.677 9.261 14.127 1.00 36.30 O ANISOU 1745 OE2 GLU C 215 5137 5206 3450 507 -253 -295 O ATOM 1746 N ALA C 216 8.619 13.163 9.563 1.00 40.16 N ANISOU 1746 N ALA C 216 5209 5972 4079 -337 -165 -448 N ATOM 1747 CA ALA C 216 9.373 13.208 8.302 1.00 40.91 C ANISOU 1747 CA ALA C 216 5215 6169 4161 -456 -91 -430 C ATOM 1748 C ALA C 216 10.697 12.439 8.383 1.00 41.87 C ANISOU 1748 C ALA C 216 5149 6530 4231 -383 -79 -512 C ATOM 1749 O ALA C 216 11.603 12.853 9.103 1.00 42.92 O ANISOU 1749 O ALA C 216 5153 6786 4368 -420 -125 -600 O ATOM 1750 CB ALA C 216 9.642 14.653 7.907 1.00 41.86 C ANISOU 1750 CB ALA C 216 5330 6238 4336 -694 -84 -414 C ATOM 1751 N SER C 217 10.801 11.325 7.653 1.00 41.73 N ANISOU 1751 N SER C 217 5111 6582 4163 -269 -24 -497 N ATOM 1752 CA SER C 217 12.088 10.629 7.468 1.00 43.14 C ANISOU 1752 CA SER C 217 5105 7001 4286 -198 -2 -575 C ATOM 1753 C SER C 217 12.074 9.683 6.269 1.00 43.09 C ANISOU 1753 C SER C 217 5100 7040 4232 -126 75 -552 C ATOM 1754 O SER C 217 11.014 9.179 5.880 1.00 41.79 O ANISOU 1754 O SER C 217 5087 6717 4075 -63 93 -491 O ATOM 1755 CB SER C 217 12.501 9.850 8.726 1.00 43.42 C ANISOU 1755 CB SER C 217 5087 7119 4291 12 -73 -648 C ATOM 1756 OG SER C 217 11.999 8.524 8.715 1.00 42.63 O ANISOU 1756 OG SER C 217 5079 6956 4163 225 -61 -618 O ATOM 1757 N GLU C 218 13.266 9.444 5.713 1.00 44.60 N ANISOU 1757 N GLU C 218 5111 7464 4372 -134 118 -615 N ATOM 1758 CA GLU C 218 13.478 8.554 4.559 1.00 44.98 C ANISOU 1758 CA GLU C 218 5124 7606 4358 -54 191 -624 C ATOM 1759 C GLU C 218 12.561 8.885 3.373 1.00 44.32 C ANISOU 1759 C GLU C 218 5169 7397 4275 -171 253 -530 C ATOM 1760 O GLU C 218 11.960 7.993 2.766 1.00 43.55 O ANISOU 1760 O GLU C 218 5158 7236 4153 -55 277 -523 O ATOM 1761 CB GLU C 218 13.321 7.078 4.970 1.00 44.67 C ANISOU 1761 CB GLU C 218 5136 7538 4298 222 162 -666 C ATOM 1762 CG GLU C 218 14.182 6.640 6.147 1.00 45.61 C ANISOU 1762 CG GLU C 218 5146 7786 4400 382 94 -747 C ATOM 1763 CD GLU C 218 15.669 6.848 5.909 1.00 47.64 C ANISOU 1763 CD GLU C 218 5150 8349 4600 348 113 -843 C ATOM 1764 OE1 GLU C 218 16.214 6.256 4.955 1.00 48.69 O ANISOU 1764 OE1 GLU C 218 5195 8629 4677 405 174 -886 O ATOM 1765 OE2 GLU C 218 16.295 7.604 6.681 1.00 48.52 O ANISOU 1765 OE2 GLU C 218 5144 8568 4722 264 66 -888 O ATOM 1766 N GLY C 219 12.446 10.179 3.069 1.00 44.54 N ANISOU 1766 N GLY C 219 5211 7382 4330 -398 274 -462 N ATOM 1767 CA GLY C 219 11.607 10.660 1.972 1.00 44.03 C ANISOU 1767 CA GLY C 219 5268 7208 4253 -511 326 -360 C ATOM 1768 C GLY C 219 10.101 10.489 2.141 1.00 42.33 C ANISOU 1768 C GLY C 219 5261 6747 4077 -440 285 -301 C ATOM 1769 O GLY C 219 9.353 10.770 1.198 1.00 42.21 O ANISOU 1769 O GLY C 219 5342 6657 4038 -502 320 -226 O ATOM 1770 N ASN C 220 9.654 10.047 3.324 1.00 41.02 N ANISOU 1770 N ASN C 220 5156 6470 3960 -313 213 -333 N ATOM 1771 CA ASN C 220 8.241 9.786 3.611 1.00 39.45 C ANISOU 1771 CA ASN C 220 5131 6059 3797 -240 179 -287 C ATOM 1772 C ASN C 220 7.745 10.788 4.655 1.00 38.76 C ANISOU 1772 C ASN C 220 5116 5838 3774 -307 114 -258 C ATOM 1773 O ASN C 220 8.541 11.374 5.391 1.00 39.36 O ANISOU 1773 O ASN C 220 5104 5981 3869 -362 82 -299 O ATOM 1774 CB ASN C 220 8.047 8.358 4.152 1.00 38.92 C ANISOU 1774 CB ASN C 220 5089 5968 3730 -29 159 -339 C ATOM 1775 CG ASN C 220 8.257 7.274 3.099 1.00 39.57 C ANISOU 1775 CG ASN C 220 5143 6130 3761 61 213 -381 C ATOM 1776 OD1 ASN C 220 8.915 6.267 3.358 1.00 40.30 O ANISOU 1776 OD1 ASN C 220 5173 6302 3836 211 211 -450 O ATOM 1777 ND2 ASN C 220 7.682 7.458 1.924 1.00 39.50 N ANISOU 1777 ND2 ASN C 220 5184 6101 3723 -13 255 -345 N ATOM 1778 N ILE C 221 6.429 10.980 4.705 1.00 37.67 N ANISOU 1778 N ILE C 221 5127 5524 3664 -298 93 -201 N ATOM 1779 CA ILE C 221 5.782 11.811 5.730 1.00 37.33 C ANISOU 1779 CA ILE C 221 5164 5346 3674 -323 28 -184 C ATOM 1780 C ILE C 221 4.459 11.197 6.162 1.00 35.93 C ANISOU 1780 C ILE C 221 5106 5036 3511 -204 6 -162 C ATOM 1781 O ILE C 221 3.839 10.451 5.408 1.00 35.95 O ANISOU 1781 O ILE C 221 5153 5012 3494 -157 41 -143 O ATOM 1782 CB ILE C 221 5.517 13.260 5.246 1.00 37.94 C ANISOU 1782 CB ILE C 221 5301 5336 3777 -495 26 -122 C ATOM 1783 CG1 ILE C 221 4.702 13.281 3.946 1.00 37.96 C ANISOU 1783 CG1 ILE C 221 5390 5288 3747 -523 71 -43 C ATOM 1784 CG2 ILE C 221 6.827 14.008 5.043 1.00 39.50 C ANISOU 1784 CG2 ILE C 221 5381 5649 3980 -646 48 -142 C ATOM 1785 CD1 ILE C 221 4.177 14.656 3.580 1.00 38.42 C ANISOU 1785 CD1 ILE C 221 5550 5221 3829 -648 57 37 C ATOM 1786 N THR C 222 4.040 11.520 7.379 1.00 35.37 N ANISOU 1786 N THR C 222 5077 4894 3468 -162 -51 -173 N ATOM 1787 CA THR C 222 2.724 11.153 7.878 1.00 34.26 C ANISOU 1787 CA THR C 222 5041 4635 3340 -74 -68 -145 C ATOM 1788 C THR C 222 1.840 12.361 7.687 1.00 33.96 C ANISOU 1788 C THR C 222 5092 4486 3327 -160 -95 -105 C ATOM 1789 O THR C 222 2.223 13.473 8.042 1.00 34.71 O ANISOU 1789 O THR C 222 5181 4561 3445 -241 -133 -120 O ATOM 1790 CB THR C 222 2.770 10.792 9.369 1.00 34.22 C ANISOU 1790 CB THR C 222 5029 4642 3333 40 -110 -176 C ATOM 1791 OG1 THR C 222 3.618 9.657 9.544 1.00 34.45 O ANISOU 1791 OG1 THR C 222 4987 4768 3334 142 -90 -204 O ATOM 1792 CG2 THR C 222 1.362 10.478 9.922 1.00 33.33 C ANISOU 1792 CG2 THR C 222 5016 4420 3227 114 -116 -138 C ATOM 1793 N VAL C 223 0.654 12.138 7.138 1.00 33.15 N ANISOU 1793 N VAL C 223 5068 4307 3221 -137 -81 -64 N ATOM 1794 CA VAL C 223 -0.278 13.222 6.863 1.00 33.06 C ANISOU 1794 CA VAL C 223 5144 4195 3223 -188 -110 -24 C ATOM 1795 C VAL C 223 -1.539 12.968 7.667 1.00 32.16 C ANISOU 1795 C VAL C 223 5087 4017 3117 -92 -136 -27 C ATOM 1796 O VAL C 223 -2.138 11.902 7.557 1.00 31.26 O ANISOU 1796 O VAL C 223 4973 3910 2993 -29 -105 -25 O ATOM 1797 CB VAL C 223 -0.583 13.391 5.349 1.00 33.32 C ANISOU 1797 CB VAL C 223 5207 4226 3226 -251 -74 29 C ATOM 1798 CG1 VAL C 223 0.583 14.092 4.656 1.00 34.43 C ANISOU 1798 CG1 VAL C 223 5305 4420 3357 -374 -49 52 C ATOM 1799 CG2 VAL C 223 -0.903 12.064 4.662 1.00 32.88 C ANISOU 1799 CG2 VAL C 223 5128 4224 3139 -190 -29 16 C ATOM 1800 N THR C 224 -1.917 13.944 8.488 1.00 32.37 N ANISOU 1800 N THR C 224 5157 3982 3162 -86 -191 -40 N ATOM 1801 CA THR C 224 -3.075 13.824 9.360 1.00 32.07 C ANISOU 1801 CA THR C 224 5158 3908 3120 8 -214 -49 C ATOM 1802 C THR C 224 -4.115 14.836 8.932 1.00 32.46 C ANISOU 1802 C THR C 224 5285 3873 3174 -1 -248 -27 C ATOM 1803 O THR C 224 -3.818 16.024 8.821 1.00 33.04 O ANISOU 1803 O THR C 224 5402 3883 3269 -57 -289 -27 O ATOM 1804 CB THR C 224 -2.690 14.079 10.822 1.00 32.28 C ANISOU 1804 CB THR C 224 5163 3958 3145 62 -256 -101 C ATOM 1805 OG1 THR C 224 -1.583 13.243 11.173 1.00 32.37 O ANISOU 1805 OG1 THR C 224 5098 4058 3142 81 -234 -120 O ATOM 1806 CG2 THR C 224 -3.868 13.790 11.761 1.00 31.99 C ANISOU 1806 CG2 THR C 224 5153 3918 3085 168 -263 -103 C ATOM 1807 N CYS C 225 -5.329 14.354 8.693 1.00 32.31 N ANISOU 1807 N CYS C 225 5284 3855 3139 54 -234 -11 N ATOM 1808 CA CYS C 225 -6.465 15.207 8.373 1.00 32.90 C ANISOU 1808 CA CYS C 225 5420 3874 3205 82 -273 1 C ATOM 1809 C CYS C 225 -7.324 15.345 9.626 1.00 32.93 C ANISOU 1809 C CYS C 225 5426 3882 3203 178 -302 -39 C ATOM 1810 O CYS C 225 -7.993 14.393 10.027 1.00 32.42 O ANISOU 1810 O CYS C 225 5320 3874 3122 226 -265 -43 O ATOM 1811 CB CYS C 225 -7.271 14.581 7.236 1.00 33.24 C ANISOU 1811 CB CYS C 225 5456 3950 3222 83 -242 28 C ATOM 1812 SG CYS C 225 -8.723 15.510 6.695 1.00 34.01 S ANISOU 1812 SG CYS C 225 5614 4017 3293 143 -294 42 S ATOM 1813 N ARG C 226 -7.284 16.520 10.249 1.00 33.33 N ANISOU 1813 N ARG C 226 5526 3874 3266 202 -364 -72 N ATOM 1814 CA ARG C 226 -8.098 16.813 11.425 1.00 33.63 C ANISOU 1814 CA ARG C 226 5566 3929 3284 306 -398 -123 C ATOM 1815 C ARG C 226 -9.423 17.433 11.008 1.00 33.99 C ANISOU 1815 C ARG C 226 5655 3947 3314 374 -430 -122 C ATOM 1816 O ARG C 226 -9.445 18.297 10.136 1.00 34.78 O ANISOU 1816 O ARG C 226 5824 3961 3429 349 -466 -95 O ATOM 1817 CB ARG C 226 -7.378 17.800 12.333 1.00 34.43 C ANISOU 1817 CB ARG C 226 5696 3981 3404 311 -459 -187 C ATOM 1818 CG ARG C 226 -5.991 17.372 12.763 1.00 34.44 C ANISOU 1818 CG ARG C 226 5644 4026 3416 251 -444 -205 C ATOM 1819 CD ARG C 226 -5.404 18.387 13.723 1.00 35.45 C ANISOU 1819 CD ARG C 226 5789 4119 3561 256 -516 -293 C ATOM 1820 NE ARG C 226 -4.196 17.873 14.364 1.00 35.82 N ANISOU 1820 NE ARG C 226 5759 4253 3597 231 -509 -328 N ATOM 1821 CZ ARG C 226 -3.678 18.306 15.518 1.00 36.42 C ANISOU 1821 CZ ARG C 226 5811 4368 3659 267 -565 -423 C ATOM 1822 NH1 ARG C 226 -2.573 17.734 15.990 1.00 36.56 N ANISOU 1822 NH1 ARG C 226 5745 4490 3656 255 -559 -449 N ATOM 1823 NH2 ARG C 226 -4.245 19.291 16.213 1.00 37.22 N ANISOU 1823 NH2 ARG C 226 5965 4418 3760 329 -633 -502 N ATOM 1824 N ALA C 227 -10.515 16.990 11.629 1.00 33.89 N ANISOU 1824 N ALA C 227 5597 4016 3265 462 -416 -145 N ATOM 1825 CA ALA C 227 -11.832 17.618 11.478 1.00 34.51 C ANISOU 1825 CA ALA C 227 5693 4103 3317 556 -455 -167 C ATOM 1826 C ALA C 227 -12.352 17.950 12.873 1.00 35.26 C ANISOU 1826 C ALA C 227 5768 4251 3379 666 -479 -237 C ATOM 1827 O ALA C 227 -12.463 17.062 13.720 1.00 34.67 O ANISOU 1827 O ALA C 227 5622 4278 3275 680 -425 -239 O ATOM 1828 CB ALA C 227 -12.790 16.686 10.761 1.00 34.04 C ANISOU 1828 CB ALA C 227 5566 4132 3235 550 -406 -140 C ATOM 1829 N SER C 228 -12.673 19.220 13.103 1.00 36.69 N ANISOU 1829 N SER C 228 6017 4362 3560 751 -558 -291 N ATOM 1830 CA SER C 228 -12.994 19.717 14.440 1.00 37.79 C ANISOU 1830 CA SER C 228 6148 4546 3664 865 -595 -380 C ATOM 1831 C SER C 228 -14.158 20.704 14.448 1.00 39.06 C ANISOU 1831 C SER C 228 6345 4698 3800 1009 -660 -438 C ATOM 1832 O SER C 228 -14.540 21.235 13.411 1.00 39.50 O ANISOU 1832 O SER C 228 6459 4675 3875 1020 -695 -406 O ATOM 1833 CB SER C 228 -11.755 20.384 15.041 1.00 38.25 C ANISOU 1833 CB SER C 228 6264 4510 3760 827 -643 -430 C ATOM 1834 OG SER C 228 -11.484 21.617 14.404 1.00 39.20 O ANISOU 1834 OG SER C 228 6499 4457 3939 808 -716 -442 O ATOM 1835 N SER C 229 -14.704 20.933 15.642 1.00 40.14 N ANISOU 1835 N SER C 229 6443 4927 3882 1132 -677 -525 N ATOM 1836 CA SER C 229 -15.753 21.930 15.889 1.00 41.52 C ANISOU 1836 CA SER C 229 6645 5108 4023 1301 -747 -609 C ATOM 1837 C SER C 229 -17.035 21.680 15.098 1.00 41.33 C ANISOU 1837 C SER C 229 6561 5177 3965 1360 -730 -578 C ATOM 1838 O SER C 229 -17.654 22.626 14.612 1.00 42.42 O ANISOU 1838 O SER C 229 6764 5250 4103 1471 -804 -608 O ATOM 1839 CB SER C 229 -15.230 23.351 15.609 1.00 42.92 C ANISOU 1839 CB SER C 229 6978 5064 4267 1326 -850 -653 C ATOM 1840 OG SER C 229 -13.980 23.577 16.240 1.00 43.28 O ANISOU 1840 OG SER C 229 7063 5026 4354 1244 -869 -693 O ATOM 1841 N PHE C 230 -17.444 20.414 14.993 1.00 40.26 N ANISOU 1841 N PHE C 230 6303 5193 3800 1290 -636 -524 N ATOM 1842 CA PHE C 230 -18.648 20.060 14.233 1.00 40.17 C ANISOU 1842 CA PHE C 230 6209 5296 3759 1323 -617 -509 C ATOM 1843 C PHE C 230 -19.779 19.469 15.071 1.00 40.66 C ANISOU 1843 C PHE C 230 6120 5584 3745 1391 -558 -553 C ATOM 1844 O PHE C 230 -19.575 18.993 16.183 1.00 40.15 O ANISOU 1844 O PHE C 230 6007 5601 3648 1381 -502 -561 O ATOM 1845 CB PHE C 230 -18.319 19.156 13.033 1.00 38.92 C ANISOU 1845 CB PHE C 230 6035 5112 3641 1168 -567 -417 C ATOM 1846 CG PHE C 230 -17.743 17.810 13.389 1.00 37.67 C ANISOU 1846 CG PHE C 230 5812 5002 3500 1029 -466 -364 C ATOM 1847 CD1 PHE C 230 -18.580 16.717 13.580 1.00 37.51 C ANISOU 1847 CD1 PHE C 230 5662 5138 3453 992 -382 -355 C ATOM 1848 CD2 PHE C 230 -16.364 17.617 13.471 1.00 36.66 C ANISOU 1848 CD2 PHE C 230 5752 4760 3418 931 -453 -322 C ATOM 1849 CE1 PHE C 230 -18.060 15.467 13.882 1.00 36.72 C ANISOU 1849 CE1 PHE C 230 5525 5052 3376 870 -289 -297 C ATOM 1850 CE2 PHE C 230 -15.839 16.367 13.776 1.00 35.76 C ANISOU 1850 CE2 PHE C 230 5588 4684 3316 828 -366 -272 C ATOM 1851 CZ PHE C 230 -16.687 15.293 13.985 1.00 35.96 C ANISOU 1851 CZ PHE C 230 5508 4838 3319 801 -284 -254 C ATOM 1852 N TYR C 231 -20.977 19.531 14.501 1.00 41.52 N ANISOU 1852 N TYR C 231 6150 5805 3820 1463 -571 -579 N ATOM 1853 CA TYR C 231 -22.186 19.000 15.105 1.00 42.36 C ANISOU 1853 CA TYR C 231 6090 6150 3857 1515 -510 -623 C ATOM 1854 C TYR C 231 -23.185 18.776 13.961 1.00 42.83 C ANISOU 1854 C TYR C 231 6061 6302 3908 1515 -520 -627 C ATOM 1855 O TYR C 231 -23.270 19.632 13.081 1.00 43.08 O ANISOU 1855 O TYR C 231 6177 6244 3947 1602 -615 -638 O ATOM 1856 CB TYR C 231 -22.751 19.992 16.131 1.00 43.69 C ANISOU 1856 CB TYR C 231 6251 6398 3953 1719 -564 -731 C ATOM 1857 CG TYR C 231 -23.993 19.478 16.821 1.00 44.75 C ANISOU 1857 CG TYR C 231 6195 6807 4000 1774 -492 -777 C ATOM 1858 CD1 TYR C 231 -25.253 19.620 16.236 1.00 45.74 C ANISOU 1858 CD1 TYR C 231 6205 7087 4087 1861 -513 -829 C ATOM 1859 CD2 TYR C 231 -23.906 18.808 18.040 1.00 45.01 C ANISOU 1859 CD2 TYR C 231 6154 6965 3982 1735 -395 -762 C ATOM 1860 CE1 TYR C 231 -26.390 19.127 16.852 1.00 46.97 C ANISOU 1860 CE1 TYR C 231 6166 7517 4164 1892 -437 -874 C ATOM 1861 CE2 TYR C 231 -25.041 18.313 18.665 1.00 46.21 C ANISOU 1861 CE2 TYR C 231 6126 7381 4050 1766 -312 -790 C ATOM 1862 CZ TYR C 231 -26.276 18.474 18.065 1.00 47.19 C ANISOU 1862 CZ TYR C 231 6126 7657 4147 1836 -331 -850 C ATOM 1863 OH TYR C 231 -27.401 17.988 18.676 1.00 48.90 O ANISOU 1863 OH TYR C 231 6144 8154 4280 1852 -242 -882 O ATOM 1864 N PRO C 232 -23.939 17.670 13.936 1.00 43.44 N ANISOU 1864 N PRO C 232 5978 6558 3971 1421 -429 -619 N ATOM 1865 CA PRO C 232 -23.928 16.591 14.936 1.00 43.61 C ANISOU 1865 CA PRO C 232 5907 6682 3983 1311 -305 -583 C ATOM 1866 C PRO C 232 -22.698 15.666 14.849 1.00 42.99 C ANISOU 1866 C PRO C 232 5909 6450 3977 1131 -242 -483 C ATOM 1867 O PRO C 232 -21.759 15.945 14.108 1.00 42.36 O ANISOU 1867 O PRO C 232 5953 6192 3951 1094 -295 -450 O ATOM 1868 CB PRO C 232 -25.234 15.835 14.636 1.00 44.29 C ANISOU 1868 CB PRO C 232 5798 6984 4044 1259 -242 -612 C ATOM 1869 CG PRO C 232 -25.513 16.103 13.198 1.00 44.22 C ANISOU 1869 CG PRO C 232 5800 6940 4060 1269 -322 -636 C ATOM 1870 CD PRO C 232 -24.990 17.478 12.916 1.00 44.04 C ANISOU 1870 CD PRO C 232 5942 6761 4030 1429 -447 -652 C ATOM 1871 N ARG C 233 -22.712 14.593 15.633 1.00 43.76 N ANISOU 1871 N ARG C 233 5936 6623 4069 1030 -127 -431 N ATOM 1872 CA ARG C 233 -21.593 13.648 15.748 1.00 43.23 C ANISOU 1872 CA ARG C 233 5940 6427 4058 890 -62 -337 C ATOM 1873 C ARG C 233 -21.221 12.875 14.461 1.00 41.79 C ANISOU 1873 C ARG C 233 5782 6135 3963 742 -51 -298 C ATOM 1874 O ARG C 233 -20.049 12.515 14.279 1.00 40.61 O ANISOU 1874 O ARG C 233 5730 5838 3862 673 -44 -241 O ATOM 1875 CB ARG C 233 -21.922 12.650 16.866 1.00 44.95 C ANISOU 1875 CB ARG C 233 6074 6765 4239 831 64 -280 C ATOM 1876 CG ARG C 233 -20.816 11.674 17.244 1.00 45.30 C ANISOU 1876 CG ARG C 233 6197 6692 4323 726 134 -175 C ATOM 1877 CD ARG C 233 -21.149 10.915 18.527 1.00 47.03 C ANISOU 1877 CD ARG C 233 6355 7035 4479 710 251 -106 C ATOM 1878 NE ARG C 233 -22.584 10.603 18.632 1.00 48.86 N ANISOU 1878 NE ARG C 233 6431 7454 4680 675 323 -127 N ATOM 1879 CZ ARG C 233 -23.462 11.156 19.479 1.00 50.53 C ANISOU 1879 CZ ARG C 233 6544 7869 4788 787 338 -176 C ATOM 1880 NH1 ARG C 233 -23.099 12.072 20.385 1.00 50.87 N ANISOU 1880 NH1 ARG C 233 6634 7953 4741 954 282 -216 N ATOM 1881 NH2 ARG C 233 -24.738 10.765 19.436 1.00 51.86 N ANISOU 1881 NH2 ARG C 233 6551 8214 4938 729 410 -196 N ATOM 1882 N ASN C 234 -22.197 12.628 13.582 1.00 41.38 N ANISOU 1882 N ASN C 234 5632 6168 3921 704 -52 -340 N ATOM 1883 CA ASN C 234 -22.002 11.717 12.436 1.00 40.39 C ANISOU 1883 CA ASN C 234 5504 5974 3868 557 -28 -323 C ATOM 1884 C ASN C 234 -21.134 12.358 11.345 1.00 38.50 C ANISOU 1884 C ASN C 234 5385 5592 3651 583 -121 -321 C ATOM 1885 O ASN C 234 -21.426 13.460 10.882 1.00 38.42 O ANISOU 1885 O ASN C 234 5401 5595 3601 701 -214 -362 O ATOM 1886 CB ASN C 234 -23.343 11.288 11.824 1.00 41.83 C ANISOU 1886 CB ASN C 234 5530 6315 4047 508 -11 -390 C ATOM 1887 CG ASN C 234 -24.346 10.822 12.863 1.00 43.32 C ANISOU 1887 CG ASN C 234 5577 6678 4204 484 82 -397 C ATOM 1888 OD1 ASN C 234 -24.760 11.594 13.730 1.00 44.30 O ANISOU 1888 OD1 ASN C 234 5670 6910 4252 618 66 -420 O ATOM 1889 ND2 ASN C 234 -24.763 9.566 12.766 1.00 44.15 N ANISOU 1889 ND2 ASN C 234 5595 6814 4366 310 181 -381 N ATOM 1890 N ILE C 235 -20.078 11.660 10.936 1.00 36.91 N ANISOU 1890 N ILE C 235 5258 5258 3508 477 -91 -268 N ATOM 1891 CA ILE C 235 -19.121 12.190 9.959 1.00 35.69 C ANISOU 1891 CA ILE C 235 5213 4979 3368 483 -158 -253 C ATOM 1892 C ILE C 235 -18.389 11.071 9.212 1.00 34.76 C ANISOU 1892 C ILE C 235 5115 4782 3310 350 -110 -226 C ATOM 1893 O ILE C 235 -18.172 9.991 9.752 1.00 34.26 O ANISOU 1893 O ILE C 235 5035 4696 3289 267 -27 -197 O ATOM 1894 CB ILE C 235 -18.099 13.140 10.645 1.00 35.10 C ANISOU 1894 CB ILE C 235 5251 4803 3283 558 -202 -222 C ATOM 1895 CG1 ILE C 235 -17.326 13.969 9.613 1.00 34.60 C ANISOU 1895 CG1 ILE C 235 5290 4629 3226 570 -276 -206 C ATOM 1896 CG2 ILE C 235 -17.140 12.375 11.556 1.00 34.61 C ANISOU 1896 CG2 ILE C 235 5217 4684 3249 499 -134 -170 C ATOM 1897 CD1 ILE C 235 -16.560 15.129 10.210 1.00 34.52 C ANISOU 1897 CD1 ILE C 235 5382 4523 3212 642 -334 -198 C ATOM 1898 N ILE C 236 -18.034 11.341 7.958 1.00 34.50 N ANISOU 1898 N ILE C 236 5124 4710 3274 340 -161 -235 N ATOM 1899 CA ILE C 236 -17.142 10.479 7.185 1.00 33.79 C ANISOU 1899 CA ILE C 236 5069 4544 3227 241 -128 -220 C ATOM 1900 C ILE C 236 -15.848 11.252 6.992 1.00 32.78 C ANISOU 1900 C ILE C 236 5051 4315 3091 269 -167 -170 C ATOM 1901 O ILE C 236 -15.879 12.428 6.623 1.00 32.80 O ANISOU 1901 O ILE C 236 5102 4309 3052 341 -237 -162 O ATOM 1902 CB ILE C 236 -17.709 10.147 5.787 1.00 34.42 C ANISOU 1902 CB ILE C 236 5097 4688 3292 203 -152 -279 C ATOM 1903 CG1 ILE C 236 -19.110 9.510 5.878 1.00 35.52 C ANISOU 1903 CG1 ILE C 236 5105 4951 3440 166 -126 -350 C ATOM 1904 CG2 ILE C 236 -16.735 9.267 5.003 1.00 34.01 C ANISOU 1904 CG2 ILE C 236 5083 4563 3277 116 -120 -278 C ATOM 1905 CD1 ILE C 236 -19.141 8.119 6.482 1.00 35.82 C ANISOU 1905 CD1 ILE C 236 5102 4952 3557 43 -26 -350 C ATOM 1906 N LEU C 237 -14.722 10.592 7.236 1.00 31.65 N ANISOU 1906 N LEU C 237 4945 4093 2986 212 -121 -136 N ATOM 1907 CA LEU C 237 -13.420 11.177 6.978 1.00 31.17 C ANISOU 1907 CA LEU C 237 4963 3957 2922 213 -147 -98 C ATOM 1908 C LEU C 237 -12.479 10.081 6.498 1.00 30.81 C ANISOU 1908 C LEU C 237 4920 3876 2911 140 -95 -94 C ATOM 1909 O LEU C 237 -12.313 9.075 7.178 1.00 31.02 O ANISOU 1909 O LEU C 237 4929 3879 2976 116 -38 -89 O ATOM 1910 CB LEU C 237 -12.877 11.845 8.241 1.00 31.07 C ANISOU 1910 CB LEU C 237 4990 3905 2910 263 -162 -73 C ATOM 1911 CG LEU C 237 -11.760 12.872 8.040 1.00 31.08 C ANISOU 1911 CG LEU C 237 5065 3836 2908 264 -208 -48 C ATOM 1912 CD1 LEU C 237 -12.263 14.106 7.299 1.00 31.67 C ANISOU 1912 CD1 LEU C 237 5187 3894 2951 306 -277 -44 C ATOM 1913 CD2 LEU C 237 -11.164 13.261 9.385 1.00 30.99 C ANISOU 1913 CD2 LEU C 237 5073 3799 2904 302 -219 -49 C ATOM 1914 N THR C 238 -11.885 10.263 5.321 1.00 30.62 N ANISOU 1914 N THR C 238 4919 3849 2866 113 -113 -93 N ATOM 1915 CA THR C 238 -10.948 9.275 4.779 1.00 30.43 C ANISOU 1915 CA THR C 238 4893 3807 2864 61 -68 -104 C ATOM 1916 C THR C 238 -9.971 9.887 3.783 1.00 30.39 C ANISOU 1916 C THR C 238 4919 3810 2817 44 -88 -81 C ATOM 1917 O THR C 238 -10.333 10.764 2.995 1.00 30.69 O ANISOU 1917 O THR C 238 4979 3879 2804 56 -130 -65 O ATOM 1918 CB THR C 238 -11.682 8.081 4.119 1.00 30.64 C ANISOU 1918 CB THR C 238 4869 3861 2912 19 -36 -170 C ATOM 1919 OG1 THR C 238 -10.735 7.060 3.784 1.00 30.55 O ANISOU 1919 OG1 THR C 238 4865 3813 2931 -12 7 -190 O ATOM 1920 CG2 THR C 238 -12.435 8.497 2.861 1.00 31.15 C ANISOU 1920 CG2 THR C 238 4909 4007 2919 21 -81 -210 C ATOM 1921 N TRP C 239 -8.717 9.459 3.882 1.00 30.16 N ANISOU 1921 N TRP C 239 4893 3760 2805 23 -55 -72 N ATOM 1922 CA TRP C 239 -7.731 9.652 2.829 1.00 30.46 C ANISOU 1922 CA TRP C 239 4935 3834 2803 -9 -48 -62 C ATOM 1923 C TRP C 239 -8.108 8.889 1.567 1.00 30.59 C ANISOU 1923 C TRP C 239 4924 3912 2787 -23 -33 -118 C ATOM 1924 O TRP C 239 -8.668 7.793 1.631 1.00 30.73 O ANISOU 1924 O TRP C 239 4913 3918 2843 -24 -11 -180 O ATOM 1925 CB TRP C 239 -6.328 9.252 3.306 1.00 30.44 C ANISOU 1925 CB TRP C 239 4918 3823 2825 -17 -15 -58 C ATOM 1926 CG TRP C 239 -5.791 10.262 4.245 1.00 30.61 C ANISOU 1926 CG TRP C 239 4960 3812 2858 -17 -43 -15 C ATOM 1927 CD1 TRP C 239 -5.682 10.162 5.600 1.00 30.46 C ANISOU 1927 CD1 TRP C 239 4940 3759 2874 22 -48 -15 C ATOM 1928 CD2 TRP C 239 -5.341 11.572 3.900 1.00 31.24 C ANISOU 1928 CD2 TRP C 239 5070 3888 2913 -59 -73 30 C ATOM 1929 NE1 TRP C 239 -5.172 11.328 6.120 1.00 30.72 N ANISOU 1929 NE1 TRP C 239 4992 3774 2905 7 -87 7 N ATOM 1930 CE2 TRP C 239 -4.953 12.210 5.096 1.00 31.15 C ANISOU 1930 CE2 TRP C 239 5070 3832 2934 -51 -101 36 C ATOM 1931 CE3 TRP C 239 -5.224 12.270 2.689 1.00 31.83 C ANISOU 1931 CE3 TRP C 239 5169 3989 2937 -105 -76 70 C ATOM 1932 CZ2 TRP C 239 -4.448 13.511 5.118 1.00 31.73 C ANISOU 1932 CZ2 TRP C 239 5179 3867 3009 -101 -134 68 C ATOM 1933 CZ3 TRP C 239 -4.729 13.564 2.712 1.00 32.41 C ANISOU 1933 CZ3 TRP C 239 5286 4019 3009 -155 -100 126 C ATOM 1934 CH2 TRP C 239 -4.347 14.171 3.920 1.00 32.25 C ANISOU 1934 CH2 TRP C 239 5278 3934 3040 -159 -130 118 C ATOM 1935 N ARG C 240 -7.795 9.498 0.428 1.00 30.80 N ANISOU 1935 N ARG C 240 4960 4001 2740 -38 -45 -95 N ATOM 1936 CA ARG C 240 -8.049 8.923 -0.883 1.00 31.16 C ANISOU 1936 CA ARG C 240 4978 4134 2728 -41 -38 -152 C ATOM 1937 C ARG C 240 -6.807 9.098 -1.731 1.00 31.79 C ANISOU 1937 C ARG C 240 5053 4282 2745 -65 -8 -126 C ATOM 1938 O ARG C 240 -6.146 10.137 -1.651 1.00 31.84 O ANISOU 1938 O ARG C 240 5090 4279 2728 -92 -9 -39 O ATOM 1939 CB ARG C 240 -9.228 9.628 -1.556 1.00 31.21 C ANISOU 1939 CB ARG C 240 4996 4194 2669 -14 -91 -142 C ATOM 1940 CG ARG C 240 -10.558 9.359 -0.882 1.00 30.81 C ANISOU 1940 CG ARG C 240 4920 4119 2668 9 -117 -189 C ATOM 1941 CD ARG C 240 -11.710 10.047 -1.587 1.00 31.28 C ANISOU 1941 CD ARG C 240 4975 4258 2652 56 -177 -191 C ATOM 1942 NE ARG C 240 -12.992 9.468 -1.188 1.00 31.30 N ANISOU 1942 NE ARG C 240 4912 4284 2695 63 -192 -272 N ATOM 1943 CZ ARG C 240 -14.182 9.844 -1.656 1.00 31.92 C ANISOU 1943 CZ ARG C 240 4954 4456 2718 111 -247 -305 C ATOM 1944 NH1 ARG C 240 -14.290 10.825 -2.548 1.00 32.66 N ANISOU 1944 NH1 ARG C 240 5088 4616 2707 176 -299 -253 N ATOM 1945 NH2 ARG C 240 -15.281 9.237 -1.220 1.00 32.23 N ANISOU 1945 NH2 ARG C 240 4914 4529 2804 97 -249 -387 N ATOM 1946 N GLN C 241 -6.483 8.074 -2.518 1.00 32.27 N ANISOU 1946 N GLN C 241 5072 4410 2780 -60 23 -208 N ATOM 1947 CA GLN C 241 -5.433 8.162 -3.523 1.00 33.01 C ANISOU 1947 CA GLN C 241 5142 4611 2787 -73 57 -198 C ATOM 1948 C GLN C 241 -6.109 8.113 -4.888 1.00 33.70 C ANISOU 1948 C GLN C 241 5220 4816 2768 -54 39 -238 C ATOM 1949 O GLN C 241 -6.780 7.138 -5.203 1.00 33.89 O ANISOU 1949 O GLN C 241 5215 4856 2805 -30 27 -354 O ATOM 1950 CB GLN C 241 -4.440 7.014 -3.370 1.00 33.37 C ANISOU 1950 CB GLN C 241 5142 4665 2871 -56 104 -277 C ATOM 1951 CG GLN C 241 -3.255 7.113 -4.321 1.00 34.53 C ANISOU 1951 CG GLN C 241 5245 4950 2924 -64 148 -272 C ATOM 1952 CD GLN C 241 -2.204 6.054 -4.071 1.00 34.93 C ANISOU 1952 CD GLN C 241 5244 5015 3011 -23 188 -353 C ATOM 1953 OE1 GLN C 241 -2.522 4.890 -3.845 1.00 35.23 O ANISOU 1953 OE1 GLN C 241 5287 4987 3113 27 185 -451 O ATOM 1954 NE2 GLN C 241 -0.940 6.453 -4.123 1.00 35.59 N ANISOU 1954 NE2 GLN C 241 5279 5186 3057 -44 226 -311 N ATOM 1955 N ASP C 242 -5.943 9.169 -5.683 1.00 34.31 N ANISOU 1955 N ASP C 242 5325 4973 2739 -65 35 -143 N ATOM 1956 CA ASP C 242 -6.601 9.295 -6.994 1.00 35.31 C ANISOU 1956 CA ASP C 242 5449 5232 2735 -30 10 -159 C ATOM 1957 C ASP C 242 -8.127 9.154 -6.893 1.00 35.40 C ANISOU 1957 C ASP C 242 5461 5223 2766 13 -57 -220 C ATOM 1958 O ASP C 242 -8.751 8.483 -7.724 1.00 35.86 O ANISOU 1958 O ASP C 242 5475 5385 2766 46 -80 -330 O ATOM 1959 CB ASP C 242 -6.029 8.271 -7.989 1.00 35.96 C ANISOU 1959 CB ASP C 242 5467 5451 2744 -11 48 -271 C ATOM 1960 CG ASP C 242 -4.519 8.317 -8.071 1.00 36.15 C ANISOU 1960 CG ASP C 242 5464 5524 2746 -46 119 -228 C ATOM 1961 OD1 ASP C 242 -3.954 9.408 -7.909 1.00 36.06 O ANISOU 1961 OD1 ASP C 242 5486 5498 2715 -98 140 -88 O ATOM 1962 OD2 ASP C 242 -3.893 7.269 -8.313 1.00 36.65 O ANISOU 1962 OD2 ASP C 242 5470 5644 2812 -21 154 -341 O ATOM 1963 N GLY C 243 -8.705 9.777 -5.859 1.00 34.71 N ANISOU 1963 N GLY C 243 5413 5017 2759 14 -90 -162 N ATOM 1964 CA GLY C 243 -10.143 9.724 -5.589 1.00 34.85 C ANISOU 1964 CA GLY C 243 5414 5025 2801 53 -148 -216 C ATOM 1965 C GLY C 243 -10.690 8.406 -5.048 1.00 34.83 C ANISOU 1965 C GLY C 243 5348 4984 2901 30 -139 -353 C ATOM 1966 O GLY C 243 -11.904 8.257 -4.905 1.00 35.08 O ANISOU 1966 O GLY C 243 5343 5034 2952 46 -180 -413 O ATOM 1967 N VAL C 244 -9.803 7.464 -4.726 1.00 34.87 N ANISOU 1967 N VAL C 244 5339 4934 2975 -6 -84 -401 N ATOM 1968 CA VAL C 244 -10.177 6.117 -4.297 1.00 35.07 C ANISOU 1968 CA VAL C 244 5326 4897 3103 -32 -64 -522 C ATOM 1969 C VAL C 244 -9.808 5.976 -2.823 1.00 34.54 C ANISOU 1969 C VAL C 244 5287 4685 3153 -50 -31 -464 C ATOM 1970 O VAL C 244 -8.639 6.162 -2.454 1.00 33.97 O ANISOU 1970 O VAL C 244 5241 4577 3088 -46 0 -403 O ATOM 1971 CB VAL C 244 -9.439 5.044 -5.129 1.00 35.66 C ANISOU 1971 CB VAL C 244 5375 5015 3159 -32 -32 -630 C ATOM 1972 CG1 VAL C 244 -9.761 3.638 -4.621 1.00 35.82 C ANISOU 1972 CG1 VAL C 244 5380 4925 3305 -64 -9 -747 C ATOM 1973 CG2 VAL C 244 -9.789 5.202 -6.604 1.00 36.60 C ANISOU 1973 CG2 VAL C 244 5461 5305 3139 -4 -67 -692 C ATOM 1974 N SER C 245 -10.795 5.635 -1.995 1.00 34.56 N ANISOU 1974 N SER C 245 5274 4622 3235 -70 -36 -488 N ATOM 1975 CA SER C 245 -10.607 5.560 -0.541 1.00 34.06 C ANISOU 1975 CA SER C 245 5239 4442 3262 -75 -6 -424 C ATOM 1976 C SER C 245 -9.578 4.507 -0.170 1.00 34.46 C ANISOU 1976 C SER C 245 5309 4409 3376 -78 47 -444 C ATOM 1977 O SER C 245 -9.620 3.390 -0.694 1.00 35.34 O ANISOU 1977 O SER C 245 5407 4501 3520 -95 67 -543 O ATOM 1978 CB SER C 245 -11.932 5.251 0.153 1.00 34.03 C ANISOU 1978 CB SER C 245 5201 4411 3318 -103 -9 -452 C ATOM 1979 OG SER C 245 -12.859 6.296 -0.066 1.00 34.24 O ANISOU 1979 OG SER C 245 5205 4524 3282 -74 -64 -432 O ATOM 1980 N LEU C 246 -8.644 4.880 0.707 1.00 34.42 N ANISOU 1980 N LEU C 246 5335 4356 3385 -51 63 -361 N ATOM 1981 CA LEU C 246 -7.640 3.941 1.221 1.00 35.04 C ANISOU 1981 CA LEU C 246 5432 4364 3518 -26 107 -369 C ATOM 1982 C LEU C 246 -8.265 2.826 2.064 1.00 35.81 C ANISOU 1982 C LEU C 246 5550 4343 3712 -38 141 -388 C ATOM 1983 O LEU C 246 -9.342 2.980 2.644 1.00 35.06 O ANISOU 1983 O LEU C 246 5448 4229 3646 -71 139 -366 O ATOM 1984 CB LEU C 246 -6.541 4.654 2.031 1.00 34.45 C ANISOU 1984 CB LEU C 246 5370 4290 3429 9 107 -283 C ATOM 1985 CG LEU C 246 -5.321 5.126 1.231 1.00 34.92 C ANISOU 1985 CG LEU C 246 5407 4442 3420 15 108 -281 C ATOM 1986 CD1 LEU C 246 -5.729 6.148 0.180 1.00 35.24 C ANISOU 1986 CD1 LEU C 246 5440 4569 3379 -22 78 -263 C ATOM 1987 CD2 LEU C 246 -4.250 5.703 2.148 1.00 34.61 C ANISOU 1987 CD2 LEU C 246 5363 4403 3383 34 108 -216 C ATOM 1988 N SER C 247 -7.568 1.695 2.092 1.00 37.53 N ANISOU 1988 N SER C 247 5794 4488 3979 -9 176 -427 N ATOM 1989 CA SER C 247 -7.877 0.574 2.977 1.00 38.87 C ANISOU 1989 CA SER C 247 6010 4515 4246 -12 220 -418 C ATOM 1990 C SER C 247 -7.945 1.012 4.446 1.00 38.97 C ANISOU 1990 C SER C 247 6044 4497 4267 11 232 -298 C ATOM 1991 O SER C 247 -7.284 1.969 4.856 1.00 38.21 O ANISOU 1991 O SER C 247 5936 4468 4113 55 206 -239 O ATOM 1992 CB SER C 247 -6.802 -0.509 2.805 1.00 39.81 C ANISOU 1992 CB SER C 247 6169 4560 4398 56 246 -462 C ATOM 1993 OG SER C 247 -6.835 -1.468 3.843 1.00 41.00 O ANISOU 1993 OG SER C 247 6387 4559 4632 80 289 -413 O ATOM 1994 N HIS C 248 -8.737 0.294 5.233 1.00 40.53 N ANISOU 1994 N HIS C 248 6270 4595 4533 -23 273 -268 N ATOM 1995 CA HIS C 248 -8.798 0.519 6.685 1.00 41.00 C ANISOU 1995 CA HIS C 248 6355 4632 4590 12 295 -154 C ATOM 1996 C HIS C 248 -7.443 0.217 7.361 1.00 40.35 C ANISOU 1996 C HIS C 248 6320 4517 4494 121 302 -99 C ATOM 1997 O HIS C 248 -7.036 0.926 8.276 1.00 39.67 O ANISOU 1997 O HIS C 248 6228 4487 4357 178 285 -29 O ATOM 1998 CB HIS C 248 -9.924 -0.314 7.326 1.00 42.82 C ANISOU 1998 CB HIS C 248 6606 4771 4894 -59 355 -124 C ATOM 1999 CG HIS C 248 -10.573 0.356 8.497 1.00 43.88 C ANISOU 1999 CG HIS C 248 6720 4962 4991 -56 367 -33 C ATOM 2000 ND1 HIS C 248 -10.068 0.276 9.779 1.00 44.56 N ANISOU 2000 ND1 HIS C 248 6853 5026 5053 22 393 74 N ATOM 2001 CD2 HIS C 248 -11.681 1.132 8.576 1.00 44.26 C ANISOU 2001 CD2 HIS C 248 6701 5105 5010 -105 352 -41 C ATOM 2002 CE1 HIS C 248 -10.840 0.970 10.597 1.00 44.75 C ANISOU 2002 CE1 HIS C 248 6840 5130 5033 16 398 123 C ATOM 2003 NE2 HIS C 248 -11.826 1.500 9.893 1.00 44.59 N ANISOU 2003 NE2 HIS C 248 6750 5180 5014 -58 373 53 N ATOM 2004 N ASP C 249 -6.748 -0.813 6.876 1.00 40.64 N ANISOU 2004 N ASP C 249 6396 4474 4571 161 320 -146 N ATOM 2005 CA ASP C 249 -5.446 -1.233 7.411 1.00 40.55 C ANISOU 2005 CA ASP C 249 6421 4440 4545 286 323 -110 C ATOM 2006 C ASP C 249 -4.254 -0.363 6.983 1.00 39.53 C ANISOU 2006 C ASP C 249 6228 4455 4338 341 275 -141 C ATOM 2007 O ASP C 249 -3.125 -0.633 7.401 1.00 40.09 O ANISOU 2007 O ASP C 249 6304 4543 4386 449 270 -125 O ATOM 2008 CB ASP C 249 -5.160 -2.688 7.008 1.00 41.87 C ANISOU 2008 CB ASP C 249 6659 4461 4788 324 357 -160 C ATOM 2009 N THR C 250 -4.482 0.646 6.142 1.00 38.23 N ANISOU 2009 N THR C 250 6001 4396 4129 269 242 -183 N ATOM 2010 CA THR C 250 -3.434 1.605 5.771 1.00 37.48 C ANISOU 2010 CA THR C 250 5844 4434 3962 289 207 -195 C ATOM 2011 C THR C 250 -3.657 2.984 6.398 1.00 36.25 C ANISOU 2011 C THR C 250 5663 4344 3765 254 171 -135 C ATOM 2012 O THR C 250 -2.908 3.915 6.102 1.00 36.03 O ANISOU 2012 O THR C 250 5589 4411 3689 240 143 -138 O ATOM 2013 CB THR C 250 -3.312 1.738 4.234 1.00 37.62 C ANISOU 2013 CB THR C 250 5822 4524 3949 243 201 -279 C ATOM 2014 OG1 THR C 250 -4.586 2.075 3.668 1.00 37.35 O ANISOU 2014 OG1 THR C 250 5789 4483 3918 156 191 -297 O ATOM 2015 CG2 THR C 250 -2.827 0.435 3.632 1.00 38.63 C ANISOU 2015 CG2 THR C 250 5967 4604 4107 303 227 -362 C ATOM 2016 N GLN C 251 -4.662 3.109 7.269 1.00 35.60 N ANISOU 2016 N GLN C 251 5612 4213 3703 238 175 -83 N ATOM 2017 CA GLN C 251 -4.949 4.370 7.962 1.00 34.82 C ANISOU 2017 CA GLN C 251 5497 4165 3567 224 138 -41 C ATOM 2018 C GLN C 251 -5.186 4.132 9.451 1.00 34.86 C ANISOU 2018 C GLN C 251 5530 4141 3572 283 152 23 C ATOM 2019 O GLN C 251 -5.614 3.048 9.843 1.00 35.14 O ANISOU 2019 O GLN C 251 5606 4098 3645 301 200 53 O ATOM 2020 CB GLN C 251 -6.194 5.043 7.391 1.00 34.41 C ANISOU 2020 CB GLN C 251 5438 4123 3512 150 121 -55 C ATOM 2021 CG GLN C 251 -6.300 5.103 5.879 1.00 34.38 C ANISOU 2021 CG GLN C 251 5415 4151 3497 97 114 -112 C ATOM 2022 CD GLN C 251 -7.607 5.740 5.455 1.00 34.23 C ANISOU 2022 CD GLN C 251 5388 4154 3464 50 89 -122 C ATOM 2023 OE1 GLN C 251 -8.533 5.072 4.992 1.00 34.82 O ANISOU 2023 OE1 GLN C 251 5452 4213 3565 16 106 -165 O ATOM 2024 NE2 GLN C 251 -7.710 7.025 5.673 1.00 33.70 N ANISOU 2024 NE2 GLN C 251 5324 4122 3360 54 45 -89 N ATOM 2025 N GLN C 252 -4.914 5.164 10.255 1.00 34.37 N ANISOU 2025 N GLN C 252 5451 4142 3467 310 110 44 N ATOM 2026 CA GLN C 252 -5.210 5.184 11.694 1.00 34.41 C ANISOU 2026 CA GLN C 252 5474 4156 3445 373 114 98 C ATOM 2027 C GLN C 252 -6.246 6.283 11.981 1.00 34.01 C ANISOU 2027 C GLN C 252 5413 4137 3374 339 85 94 C ATOM 2028 O GLN C 252 -6.100 7.415 11.499 1.00 33.68 O ANISOU 2028 O GLN C 252 5354 4124 3320 305 33 56 O ATOM 2029 CB GLN C 252 -3.931 5.443 12.489 1.00 34.51 C ANISOU 2029 CB GLN C 252 5465 4235 3411 457 78 99 C ATOM 2030 N TRP C 253 -7.280 5.952 12.760 1.00 33.90 N ANISOU 2030 N TRP C 253 5412 4115 3353 353 121 136 N ATOM 2031 CA TRP C 253 -8.387 6.880 13.035 1.00 33.61 C ANISOU 2031 CA TRP C 253 5357 4123 3293 340 99 123 C ATOM 2032 C TRP C 253 -8.382 7.397 14.477 1.00 33.49 C ANISOU 2032 C TRP C 253 5340 4175 3212 425 82 144 C ATOM 2033 O TRP C 253 -8.137 6.646 15.413 1.00 33.99 O ANISOU 2033 O TRP C 253 5419 4250 3247 483 122 203 O ATOM 2034 CB TRP C 253 -9.736 6.208 12.753 1.00 34.13 C ANISOU 2034 CB TRP C 253 5410 4167 3391 281 156 135 C ATOM 2035 CG TRP C 253 -10.225 6.341 11.335 1.00 34.19 C ANISOU 2035 CG TRP C 253 5397 4158 3436 203 139 77 C ATOM 2036 CD1 TRP C 253 -11.013 7.340 10.827 1.00 34.19 C ANISOU 2036 CD1 TRP C 253 5369 4206 3417 189 92 36 C ATOM 2037 CD2 TRP C 253 -9.981 5.438 10.253 1.00 34.42 C ANISOU 2037 CD2 TRP C 253 5433 4129 3517 146 165 50 C ATOM 2038 NE1 TRP C 253 -11.270 7.115 9.494 1.00 34.03 N ANISOU 2038 NE1 TRP C 253 5335 4174 3422 128 87 -8 N ATOM 2039 CE2 TRP C 253 -10.652 5.953 9.116 1.00 34.37 C ANISOU 2039 CE2 TRP C 253 5395 4155 3509 96 131 -8 C ATOM 2040 CE3 TRP C 253 -9.259 4.246 10.131 1.00 34.91 C ANISOU 2040 CE3 TRP C 253 5528 4115 3619 148 208 62 C ATOM 2041 CZ2 TRP C 253 -10.618 5.317 7.874 1.00 34.81 C ANISOU 2041 CZ2 TRP C 253 5444 4187 3595 41 139 -61 C ATOM 2042 CZ3 TRP C 253 -9.231 3.606 8.898 1.00 35.36 C ANISOU 2042 CZ3 TRP C 253 5584 4132 3719 93 217 2 C ATOM 2043 CH2 TRP C 253 -9.903 4.146 7.783 1.00 35.32 C ANISOU 2043 CH2 TRP C 253 5538 4176 3704 37 183 -62 C ATOM 2044 N GLY C 254 -8.656 8.689 14.637 1.00 32.81 N ANISOU 2044 N GLY C 254 5239 4131 3095 440 19 95 N ATOM 2045 CA GLY C 254 -9.005 9.263 15.928 1.00 32.71 C ANISOU 2045 CA GLY C 254 5218 4195 3015 522 0 91 C ATOM 2046 C GLY C 254 -10.470 9.014 16.206 1.00 32.77 C ANISOU 2046 C GLY C 254 5202 4243 3008 518 52 115 C ATOM 2047 O GLY C 254 -11.290 9.041 15.284 1.00 32.62 O ANISOU 2047 O GLY C 254 5165 4201 3030 455 60 95 O ATOM 2048 N ASP C 255 -10.800 8.788 17.473 1.00 33.00 N ANISOU 2048 N ASP C 255 5220 4351 2968 589 87 155 N ATOM 2049 CA ASP C 255 -12.182 8.562 17.881 1.00 33.47 C ANISOU 2049 CA ASP C 255 5238 4480 3000 585 148 180 C ATOM 2050 C ASP C 255 -12.992 9.841 17.729 1.00 33.16 C ANISOU 2050 C ASP C 255 5164 4497 2939 617 83 92 C ATOM 2051 O ASP C 255 -12.465 10.940 17.911 1.00 32.87 O ANISOU 2051 O ASP C 255 5150 4461 2880 678 -3 24 O ATOM 2052 CB ASP C 255 -12.253 8.089 19.337 1.00 34.57 C ANISOU 2052 CB ASP C 255 5375 4712 3048 664 205 253 C ATOM 2053 CG ASP C 255 -11.577 6.749 19.558 1.00 35.01 C ANISOU 2053 CG ASP C 255 5481 4703 3120 651 275 361 C ATOM 2054 OD1 ASP C 255 -10.799 6.311 18.682 1.00 34.58 O ANISOU 2054 OD1 ASP C 255 5460 4538 3141 605 261 356 O ATOM 2055 OD2 ASP C 255 -11.821 6.136 20.619 1.00 36.05 O ANISOU 2055 OD2 ASP C 255 5621 4896 3181 699 346 453 O ATOM 2056 N VAL C 256 -14.274 9.690 17.403 1.00 33.38 N ANISOU 2056 N VAL C 256 5136 4572 2976 578 123 87 N ATOM 2057 CA VAL C 256 -15.177 10.832 17.255 1.00 33.67 C ANISOU 2057 CA VAL C 256 5134 4675 2985 633 63 3 C ATOM 2058 C VAL C 256 -15.657 11.240 18.649 1.00 34.62 C ANISOU 2058 C VAL C 256 5219 4933 3003 744 74 -10 C ATOM 2059 O VAL C 256 -16.631 10.683 19.160 1.00 35.73 O ANISOU 2059 O VAL C 256 5288 5184 3103 736 157 26 O ATOM 2060 CB VAL C 256 -16.369 10.514 16.322 1.00 33.89 C ANISOU 2060 CB VAL C 256 5094 4729 3052 559 93 -13 C ATOM 2061 CG1 VAL C 256 -17.248 11.746 16.139 1.00 34.32 C ANISOU 2061 CG1 VAL C 256 5113 4857 3071 647 19 -101 C ATOM 2062 CG2 VAL C 256 -15.870 10.007 14.973 1.00 33.00 C ANISOU 2062 CG2 VAL C 256 5016 4499 3026 456 86 -6 C ATOM 2063 N LEU C 257 -14.964 12.213 19.247 1.00 34.59 N ANISOU 2063 N LEU C 257 5258 4929 2956 842 -7 -70 N ATOM 2064 CA LEU C 257 -15.176 12.618 20.650 1.00 35.71 C ANISOU 2064 CA LEU C 257 5374 5207 2985 966 -8 -99 C ATOM 2065 C LEU C 257 -15.523 14.113 20.794 1.00 36.14 C ANISOU 2065 C LEU C 257 5436 5284 3010 1078 -113 -230 C ATOM 2066 O LEU C 257 -15.183 14.910 19.922 1.00 35.31 O ANISOU 2066 O LEU C 257 5387 5054 2977 1059 -197 -285 O ATOM 2067 CB LEU C 257 -13.921 12.298 21.469 1.00 35.60 C ANISOU 2067 CB LEU C 257 5407 5188 2932 999 -13 -64 C ATOM 2068 CG LEU C 257 -13.594 10.808 21.606 1.00 35.58 C ANISOU 2068 CG LEU C 257 5412 5171 2937 933 92 73 C ATOM 2069 CD1 LEU C 257 -12.216 10.617 22.217 1.00 35.69 C ANISOU 2069 CD1 LEU C 257 5473 5172 2915 984 61 93 C ATOM 2070 CD2 LEU C 257 -14.651 10.077 22.423 1.00 36.71 C ANISOU 2070 CD2 LEU C 257 5498 5448 3003 945 205 156 C ATOM 2071 N PRO C 258 -16.197 14.495 21.903 1.00 37.57 N ANISOU 2071 N PRO C 258 5568 5624 3084 1200 -106 -279 N ATOM 2072 CA PRO C 258 -16.572 15.902 22.117 1.00 38.42 C ANISOU 2072 CA PRO C 258 5688 5749 3162 1329 -209 -419 C ATOM 2073 C PRO C 258 -15.408 16.879 22.401 1.00 38.82 C ANISOU 2073 C PRO C 258 5829 5693 3229 1377 -322 -511 C ATOM 2074 O PRO C 258 -14.360 16.489 22.932 1.00 38.07 O ANISOU 2074 O PRO C 258 5756 5594 3116 1355 -318 -484 O ATOM 2075 CB PRO C 258 -17.521 15.834 23.322 1.00 39.52 C ANISOU 2075 CB PRO C 258 5737 6115 3165 1447 -153 -441 C ATOM 2076 CG PRO C 258 -17.146 14.587 24.032 1.00 39.50 C ANISOU 2076 CG PRO C 258 5711 6191 3107 1393 -43 -312 C ATOM 2077 CD PRO C 258 -16.754 13.623 22.957 1.00 38.46 C ANISOU 2077 CD PRO C 258 5609 5912 3094 1226 5 -203 C ATOM 2078 N ASP C 259 -15.632 18.135 22.008 1.00 39.71 N ANISOU 2078 N ASP C 259 5992 5716 3380 1440 -424 -622 N ATOM 2079 CA ASP C 259 -14.729 19.263 22.253 1.00 40.52 C ANISOU 2079 CA ASP C 259 6183 5701 3512 1480 -540 -735 C ATOM 2080 C ASP C 259 -14.730 19.680 23.712 1.00 41.47 C ANISOU 2080 C ASP C 259 6278 5963 3516 1625 -572 -845 C ATOM 2081 O ASP C 259 -13.691 20.065 24.257 1.00 41.73 O ANISOU 2081 O ASP C 259 6350 5958 3547 1630 -635 -915 O ATOM 2082 CB ASP C 259 -15.187 20.499 21.452 1.00 41.60 C ANISOU 2082 CB ASP C 259 6395 5693 3720 1524 -634 -815 C ATOM 2083 CG ASP C 259 -14.615 20.551 20.074 1.00 41.46 C ANISOU 2083 CG ASP C 259 6449 5483 3822 1384 -650 -742 C ATOM 2084 OD1 ASP C 259 -13.391 20.764 19.963 1.00 42.81 O ANISOU 2084 OD1 ASP C 259 6678 5535 4052 1295 -686 -747 O ATOM 2085 OD2 ASP C 259 -15.381 20.415 19.101 1.00 41.33 O ANISOU 2085 OD2 ASP C 259 6422 5448 3833 1365 -629 -687 O ATOM 2086 N GLY C 260 -15.916 19.639 24.317 1.00 41.89 N ANISOU 2086 N GLY C 260 6255 6195 3467 1746 -531 -870 N ATOM 2087 CA GLY C 260 -16.197 20.352 25.552 1.00 43.40 C ANISOU 2087 CA GLY C 260 6425 6524 3541 1922 -579 -1012 C ATOM 2088 C GLY C 260 -16.899 21.688 25.335 1.00 44.21 C ANISOU 2088 C GLY C 260 6573 6556 3669 2051 -682 -1162 C ATOM 2089 O GLY C 260 -17.108 22.427 26.297 1.00 45.58 O ANISOU 2089 O GLY C 260 6743 6820 3756 2211 -741 -1311 O ATOM 2090 N ASN C 261 -17.249 21.999 24.082 1.00 43.49 N ANISOU 2090 N ASN C 261 6530 6305 3689 1996 -707 -1127 N ATOM 2091 CA ASN C 261 -18.043 23.178 23.724 1.00 44.59 C ANISOU 2091 CA ASN C 261 6720 6369 3853 2132 -798 -1242 C ATOM 2092 C ASN C 261 -19.350 22.798 22.996 1.00 44.17 C ANISOU 2092 C ASN C 261 6580 6417 3784 2156 -739 -1176 C ATOM 2093 O ASN C 261 -19.988 23.660 22.387 1.00 44.82 O ANISOU 2093 O ASN C 261 6710 6418 3902 2256 -814 -1237 O ATOM 2094 CB ASN C 261 -17.217 24.131 22.845 1.00 44.68 C ANISOU 2094 CB ASN C 261 6892 6077 4009 2065 -905 -1270 C ATOM 2095 CG ASN C 261 -15.959 24.631 23.531 1.00 45.32 C ANISOU 2095 CG ASN C 261 7046 6058 4117 2032 -975 -1363 C ATOM 2096 OD1 ASN C 261 -14.868 24.545 22.975 1.00 44.96 O ANISOU 2096 OD1 ASN C 261 7060 5853 4168 1869 -985 -1304 O ATOM 2097 ND2 ASN C 261 -16.105 25.161 24.741 1.00 46.89 N ANISOU 2097 ND2 ASN C 261 7227 6367 4224 2188 -1025 -1521 N ATOM 2098 N GLY C 262 -19.752 21.524 23.079 1.00 43.01 N ANISOU 2098 N GLY C 262 6309 6448 3586 2069 -610 -1057 N ATOM 2099 CA GLY C 262 -20.993 21.036 22.464 1.00 42.77 C ANISOU 2099 CA GLY C 262 6167 6546 3539 2067 -545 -1006 C ATOM 2100 C GLY C 262 -20.817 20.464 21.066 1.00 41.24 C ANISOU 2100 C GLY C 262 5997 6215 3455 1897 -521 -886 C ATOM 2101 O GLY C 262 -21.760 19.901 20.503 1.00 41.22 O ANISOU 2101 O GLY C 262 5891 6324 3446 1864 -463 -842 O ATOM 2102 N THR C 263 -19.610 20.602 20.517 1.00 39.83 N ANISOU 2102 N THR C 263 5943 5815 3374 1788 -565 -845 N ATOM 2103 CA THR C 263 -19.265 20.142 19.185 1.00 38.38 C ANISOU 2103 CA THR C 263 5798 5498 3288 1634 -551 -741 C ATOM 2104 C THR C 263 -18.259 18.997 19.316 1.00 37.02 C ANISOU 2104 C THR C 263 5619 5305 3142 1469 -468 -636 C ATOM 2105 O THR C 263 -17.822 18.682 20.428 1.00 37.28 O ANISOU 2105 O THR C 263 5631 5418 3116 1488 -435 -642 O ATOM 2106 CB THR C 263 -18.661 21.300 18.377 1.00 38.44 C ANISOU 2106 CB THR C 263 5958 5266 3381 1647 -666 -773 C ATOM 2107 OG1 THR C 263 -17.558 21.861 19.098 1.00 38.82 O ANISOU 2107 OG1 THR C 263 6095 5207 3449 1646 -718 -829 O ATOM 2108 CG2 THR C 263 -19.699 22.379 18.150 1.00 39.60 C ANISOU 2108 CG2 THR C 263 6127 5416 3505 1828 -750 -864 C ATOM 2109 N TYR C 264 -17.900 18.385 18.187 1.00 35.73 N ANISOU 2109 N TYR C 264 5475 5046 3057 1326 -440 -545 N ATOM 2110 CA TYR C 264 -17.083 17.160 18.157 1.00 34.67 C ANISOU 2110 CA TYR C 264 5327 4896 2950 1179 -355 -444 C ATOM 2111 C TYR C 264 -15.863 17.304 17.267 1.00 33.48 C ANISOU 2111 C TYR C 264 5273 4560 2888 1074 -395 -408 C ATOM 2112 O TYR C 264 -15.749 18.258 16.494 1.00 33.50 O ANISOU 2112 O TYR C 264 5353 4441 2936 1088 -474 -438 O ATOM 2113 CB TYR C 264 -17.921 15.969 17.682 1.00 34.50 C ANISOU 2113 CB TYR C 264 5205 4971 2931 1093 -256 -371 C ATOM 2114 CG TYR C 264 -19.135 15.721 18.543 1.00 35.65 C ANISOU 2114 CG TYR C 264 5232 5322 2989 1168 -195 -394 C ATOM 2115 CD1 TYR C 264 -20.352 16.348 18.261 1.00 36.55 C ANISOU 2115 CD1 TYR C 264 5281 5534 3072 1264 -231 -468 C ATOM 2116 CD2 TYR C 264 -19.070 14.884 19.660 1.00 36.04 C ANISOU 2116 CD2 TYR C 264 5232 5484 2977 1153 -101 -340 C ATOM 2117 CE1 TYR C 264 -21.470 16.139 19.055 1.00 37.59 C ANISOU 2117 CE1 TYR C 264 5283 5882 3116 1331 -170 -497 C ATOM 2118 CE2 TYR C 264 -20.188 14.670 20.461 1.00 37.17 C ANISOU 2118 CE2 TYR C 264 5259 5834 3030 1212 -33 -351 C ATOM 2119 CZ TYR C 264 -21.385 15.298 20.147 1.00 37.91 C ANISOU 2119 CZ TYR C 264 5273 6035 3097 1296 -65 -435 C ATOM 2120 OH TYR C 264 -22.502 15.096 20.920 1.00 39.51 O ANISOU 2120 OH TYR C 264 5339 6467 3205 1352 8 -454 O ATOM 2121 N GLN C 265 -14.950 16.347 17.403 1.00 32.62 N ANISOU 2121 N GLN C 265 5161 4436 2797 976 -337 -339 N ATOM 2122 CA GLN C 265 -13.718 16.315 16.622 1.00 31.98 C ANISOU 2122 CA GLN C 265 5146 4215 2789 872 -358 -304 C ATOM 2123 C GLN C 265 -13.306 14.877 16.310 1.00 31.22 C ANISOU 2123 C GLN C 265 5013 4133 2715 766 -267 -213 C ATOM 2124 O GLN C 265 -13.577 13.959 17.095 1.00 31.18 O ANISOU 2124 O GLN C 265 4957 4223 2669 777 -193 -172 O ATOM 2125 CB GLN C 265 -12.590 17.039 17.363 1.00 32.56 C ANISOU 2125 CB GLN C 265 5273 4236 2861 897 -421 -360 C ATOM 2126 CG GLN C 265 -12.159 16.382 18.672 1.00 33.06 C ANISOU 2126 CG GLN C 265 5292 4413 2857 938 -382 -356 C ATOM 2127 CD GLN C 265 -11.216 17.236 19.496 1.00 33.97 C ANISOU 2127 CD GLN C 265 5442 4509 2956 985 -463 -448 C ATOM 2128 OE1 GLN C 265 -10.786 18.307 19.069 1.00 34.67 O ANISOU 2128 OE1 GLN C 265 5594 4474 3103 961 -544 -513 O ATOM 2129 NE2 GLN C 265 -10.884 16.757 20.689 1.00 34.55 N ANISOU 2129 NE2 GLN C 265 5475 4705 2947 1048 -441 -454 N ATOM 2130 N THR C 266 -12.653 14.697 15.160 1.00 30.33 N ANISOU 2130 N THR C 266 4934 3922 2666 669 -270 -179 N ATOM 2131 CA THR C 266 -12.042 13.418 14.790 1.00 29.54 C ANISOU 2131 CA THR C 266 4817 3810 2596 580 -199 -111 C ATOM 2132 C THR C 266 -10.810 13.651 13.917 1.00 28.95 C ANISOU 2132 C THR C 266 4788 3639 2571 506 -230 -104 C ATOM 2133 O THR C 266 -10.483 14.788 13.603 1.00 28.92 O ANISOU 2133 O THR C 266 4834 3573 2583 507 -299 -139 O ATOM 2134 CB THR C 266 -13.060 12.485 14.095 1.00 29.47 C ANISOU 2134 CB THR C 266 4758 3835 2604 528 -134 -78 C ATOM 2135 OG1 THR C 266 -12.524 11.158 14.017 1.00 29.04 O ANISOU 2135 OG1 THR C 266 4696 3760 2580 460 -60 -21 O ATOM 2136 CG2 THR C 266 -13.432 12.986 12.693 1.00 29.36 C ANISOU 2136 CG2 THR C 266 4758 3778 2619 493 -176 -98 C ATOM 2137 N TRP C 267 -10.112 12.578 13.553 1.00 28.80 N ANISOU 2137 N TRP C 267 4757 3609 2577 444 -176 -59 N ATOM 2138 CA TRP C 267 -8.990 12.680 12.615 1.00 28.57 C ANISOU 2138 CA TRP C 267 4750 3519 2586 371 -192 -53 C ATOM 2139 C TRP C 267 -8.700 11.364 11.904 1.00 28.64 C ANISOU 2139 C TRP C 267 4737 3523 2620 316 -125 -16 C ATOM 2140 O TRP C 267 -9.220 10.308 12.283 1.00 28.91 O ANISOU 2140 O TRP C 267 4750 3579 2654 327 -66 11 O ATOM 2141 CB TRP C 267 -7.727 13.225 13.310 1.00 28.73 C ANISOU 2141 CB TRP C 267 4779 3534 2601 381 -234 -82 C ATOM 2142 CG TRP C 267 -7.233 12.415 14.481 1.00 28.92 C ANISOU 2142 CG TRP C 267 4773 3625 2590 440 -205 -71 C ATOM 2143 CD1 TRP C 267 -7.557 12.593 15.799 1.00 29.36 C ANISOU 2143 CD1 TRP C 267 4820 3745 2590 530 -218 -90 C ATOM 2144 CD2 TRP C 267 -6.316 11.310 14.441 1.00 28.94 C ANISOU 2144 CD2 TRP C 267 4753 3644 2598 431 -160 -35 C ATOM 2145 NE1 TRP C 267 -6.907 11.667 16.576 1.00 29.56 N ANISOU 2145 NE1 TRP C 267 4824 3828 2581 576 -184 -56 N ATOM 2146 CE2 TRP C 267 -6.136 10.868 15.772 1.00 29.24 C ANISOU 2146 CE2 TRP C 267 4778 3752 2581 522 -150 -22 C ATOM 2147 CE3 TRP C 267 -5.635 10.644 13.409 1.00 28.60 C ANISOU 2147 CE3 TRP C 267 4702 3573 2593 371 -129 -16 C ATOM 2148 CZ2 TRP C 267 -5.306 9.787 16.100 1.00 29.41 C ANISOU 2148 CZ2 TRP C 267 4787 3801 2588 561 -114 19 C ATOM 2149 CZ3 TRP C 267 -4.802 9.567 13.738 1.00 28.77 C ANISOU 2149 CZ3 TRP C 267 4705 3622 2605 410 -94 9 C ATOM 2150 CH2 TRP C 267 -4.649 9.154 15.075 1.00 29.20 C ANISOU 2150 CH2 TRP C 267 4755 3731 2608 508 -89 31 C ATOM 2151 N VAL C 268 -7.887 11.445 10.856 1.00 28.69 N ANISOU 2151 N VAL C 268 4753 3498 2649 253 -132 -15 N ATOM 2152 CA VAL C 268 -7.445 10.262 10.110 1.00 28.72 C ANISOU 2152 CA VAL C 268 4739 3499 2675 213 -78 0 C ATOM 2153 C VAL C 268 -6.082 10.527 9.455 1.00 28.68 C ANISOU 2153 C VAL C 268 4729 3496 2675 168 -91 -7 C ATOM 2154 O VAL C 268 -5.877 11.576 8.854 1.00 28.90 O ANISOU 2154 O VAL C 268 4774 3508 2697 124 -128 -10 O ATOM 2155 CB VAL C 268 -8.507 9.815 9.073 1.00 28.81 C ANISOU 2155 CB VAL C 268 4743 3507 2697 175 -55 -7 C ATOM 2156 CG1 VAL C 268 -8.659 10.829 7.946 1.00 28.93 C ANISOU 2156 CG1 VAL C 268 4777 3520 2695 143 -100 -15 C ATOM 2157 CG2 VAL C 268 -8.181 8.431 8.529 1.00 28.99 C ANISOU 2157 CG2 VAL C 268 4751 3515 2749 146 2 -11 C ATOM 2158 N ALA C 269 -5.159 9.573 9.588 1.00 28.83 N ANISOU 2158 N ALA C 269 4722 3533 2700 183 -56 -6 N ATOM 2159 CA ALA C 269 -3.769 9.744 9.153 1.00 28.99 C ANISOU 2159 CA ALA C 269 4710 3590 2716 152 -62 -22 C ATOM 2160 C ALA C 269 -3.251 8.534 8.387 1.00 28.97 C ANISOU 2160 C ALA C 269 4684 3603 2721 156 -12 -31 C ATOM 2161 O ALA C 269 -3.760 7.426 8.551 1.00 28.88 O ANISOU 2161 O ALA C 269 4689 3556 2727 196 25 -25 O ATOM 2162 CB ALA C 269 -2.875 10.018 10.355 1.00 29.43 C ANISOU 2162 CB ALA C 269 4739 3686 2758 198 -92 -37 C ATOM 2163 N THR C 270 -2.230 8.769 7.558 1.00 29.23 N ANISOU 2163 N THR C 270 4677 3688 2739 111 -9 -49 N ATOM 2164 CA THR C 270 -1.646 7.743 6.675 1.00 29.29 C ANISOU 2164 CA THR C 270 4655 3732 2743 122 34 -76 C ATOM 2165 C THR C 270 -0.219 8.159 6.246 1.00 29.64 C ANISOU 2165 C THR C 270 4628 3875 2759 88 35 -97 C ATOM 2166 O THR C 270 0.112 9.344 6.294 1.00 29.75 O ANISOU 2166 O THR C 270 4628 3909 2765 16 7 -82 O ATOM 2167 CB THR C 270 -2.577 7.481 5.454 1.00 29.25 C ANISOU 2167 CB THR C 270 4676 3702 2734 81 54 -86 C ATOM 2168 OG1 THR C 270 -2.277 6.211 4.862 1.00 29.70 O ANISOU 2168 OG1 THR C 270 4718 3766 2798 118 94 -132 O ATOM 2169 CG2 THR C 270 -2.473 8.590 4.398 1.00 29.32 C ANISOU 2169 CG2 THR C 270 4679 3757 2703 -1 40 -69 C ATOM 2170 N ARG C 271 0.618 7.187 5.867 1.00 30.00 N ANISOU 2170 N ARG C 271 4625 3980 2793 139 68 -135 N ATOM 2171 CA ARG C 271 2.007 7.447 5.425 1.00 30.74 C ANISOU 2171 CA ARG C 271 4625 4202 2852 112 78 -165 C ATOM 2172 C ARG C 271 2.061 7.560 3.914 1.00 30.99 C ANISOU 2172 C ARG C 271 4638 4291 2846 43 115 -172 C ATOM 2173 O ARG C 271 1.532 6.695 3.222 1.00 30.81 O ANISOU 2173 O ARG C 271 4645 4242 2819 81 140 -199 O ATOM 2174 CB ARG C 271 2.967 6.305 5.813 1.00 31.34 C ANISOU 2174 CB ARG C 271 4646 4340 2921 234 92 -212 C ATOM 2175 CG ARG C 271 3.403 6.243 7.263 1.00 31.65 C ANISOU 2175 CG ARG C 271 4669 4389 2966 319 54 -209 C ATOM 2176 CD ARG C 271 4.326 7.390 7.652 1.00 31.99 C ANISOU 2176 CD ARG C 271 4623 4541 2991 247 19 -227 C ATOM 2177 NE ARG C 271 5.746 7.194 7.364 1.00 32.76 N ANISOU 2177 NE ARG C 271 4592 4802 3053 267 31 -284 N ATOM 2178 CZ ARG C 271 6.688 8.113 7.598 1.00 33.43 C ANISOU 2178 CZ ARG C 271 4571 5004 3125 185 7 -316 C ATOM 2179 NH1 ARG C 271 6.377 9.307 8.108 1.00 33.37 N ANISOU 2179 NH1 ARG C 271 4590 4945 3145 79 -33 -298 N ATOM 2180 NH2 ARG C 271 7.957 7.846 7.329 1.00 34.50 N ANISOU 2180 NH2 ARG C 271 4570 5313 3225 209 22 -376 N ATOM 2181 N ILE C 272 2.717 8.602 3.407 1.00 31.49 N ANISOU 2181 N ILE C 272 4652 4434 2878 -63 122 -150 N ATOM 2182 CA ILE C 272 2.928 8.764 1.964 1.00 32.44 C ANISOU 2182 CA ILE C 272 4746 4641 2939 -128 166 -142 C ATOM 2183 C ILE C 272 4.384 9.112 1.679 1.00 33.66 C ANISOU 2183 C ILE C 272 4779 4954 3055 -186 199 -157 C ATOM 2184 O ILE C 272 5.151 9.380 2.604 1.00 33.76 O ANISOU 2184 O ILE C 272 4732 5000 3096 -191 177 -176 O ATOM 2185 CB ILE C 272 1.966 9.812 1.336 1.00 32.20 C ANISOU 2185 CB ILE C 272 4798 4542 2893 -219 155 -67 C ATOM 2186 CG1 ILE C 272 2.222 11.225 1.875 1.00 32.51 C ANISOU 2186 CG1 ILE C 272 4854 4538 2961 -323 126 -8 C ATOM 2187 CG2 ILE C 272 0.521 9.411 1.600 1.00 31.37 C ANISOU 2187 CG2 ILE C 272 4785 4315 2821 -157 123 -69 C ATOM 2188 CD1 ILE C 272 1.437 12.303 1.154 1.00 32.68 C ANISOU 2188 CD1 ILE C 272 4965 4490 2960 -400 117 76 C ATOM 2189 N SER C 273 4.750 9.083 0.396 1.00 34.78 N ANISOU 2189 N SER C 273 4877 5212 3125 -229 253 -155 N ATOM 2190 CA SER C 273 6.085 9.489 -0.059 1.00 36.30 C ANISOU 2190 CA SER C 273 4942 5583 3268 -309 302 -159 C ATOM 2191 C SER C 273 6.091 10.946 -0.507 1.00 36.99 C ANISOU 2191 C SER C 273 5055 5657 3343 -486 318 -57 C ATOM 2192 O SER C 273 5.109 11.434 -1.073 1.00 36.59 O ANISOU 2192 O SER C 273 5114 5512 3276 -520 312 16 O ATOM 2193 CB SER C 273 6.567 8.589 -1.199 1.00 37.29 C ANISOU 2193 CB SER C 273 4992 5867 3307 -245 361 -219 C ATOM 2194 OG SER C 273 6.834 7.274 -0.735 1.00 37.33 O ANISOU 2194 OG SER C 273 4967 5885 3333 -80 347 -320 O ATOM 2195 N ARG C 274 7.201 11.633 -0.231 1.00 38.18 N ANISOU 2195 N ARG C 274 5104 5899 3504 -596 337 -52 N ATOM 2196 CA ARG C 274 7.416 12.996 -0.710 1.00 39.34 C ANISOU 2196 CA ARG C 274 5269 6034 3646 -787 367 49 C ATOM 2197 C ARG C 274 7.541 12.930 -2.235 1.00 40.41 C ANISOU 2197 C ARG C 274 5384 6301 3667 -827 451 105 C ATOM 2198 O ARG C 274 8.220 12.051 -2.768 1.00 40.92 O ANISOU 2198 O ARG C 274 5334 6554 3663 -760 500 36 O ATOM 2199 CB ARG C 274 8.670 13.613 -0.071 1.00 40.46 C ANISOU 2199 CB ARG C 274 5281 6263 3830 -909 374 19 C ATOM 2200 N GLY C 275 6.863 13.846 -2.922 1.00 40.85 N ANISOU 2200 N GLY C 275 5557 6266 3698 -917 463 227 N ATOM 2201 CA GLY C 275 6.670 13.770 -4.369 1.00 41.83 C ANISOU 2201 CA GLY C 275 5698 6500 3696 -923 529 292 C ATOM 2202 C GLY C 275 5.303 13.257 -4.802 1.00 40.92 C ANISOU 2202 C GLY C 275 5703 6300 3546 -790 485 288 C ATOM 2203 O GLY C 275 4.938 13.430 -5.961 1.00 41.85 O ANISOU 2203 O GLY C 275 5863 6484 3555 -797 522 357 O ATOM 2204 N GLU C 276 4.547 12.631 -3.896 1.00 39.54 N ANISOU 2204 N GLU C 276 5576 5996 3452 -673 410 208 N ATOM 2205 CA GLU C 276 3.213 12.098 -4.212 1.00 38.91 C ANISOU 2205 CA GLU C 276 5592 5840 3354 -560 367 186 C ATOM 2206 C GLU C 276 2.050 12.847 -3.539 1.00 37.96 C ANISOU 2206 C GLU C 276 5603 5514 3306 -559 293 242 C ATOM 2207 O GLU C 276 0.919 12.356 -3.537 1.00 36.74 O ANISOU 2207 O GLU C 276 5508 5297 3157 -465 249 206 O ATOM 2208 CB GLU C 276 3.151 10.614 -3.841 1.00 38.51 C ANISOU 2208 CB GLU C 276 5490 5812 3331 -420 351 45 C ATOM 2209 CG GLU C 276 3.966 9.712 -4.758 1.00 39.87 C ANISOU 2209 CG GLU C 276 5554 6182 3411 -371 414 -33 C ATOM 2210 CD GLU C 276 3.182 8.498 -5.241 1.00 39.91 C ANISOU 2210 CD GLU C 276 5586 6184 3394 -242 395 -139 C ATOM 2211 OE1 GLU C 276 2.417 7.904 -4.433 1.00 39.57 O ANISOU 2211 OE1 GLU C 276 5600 5991 3444 -173 342 -190 O ATOM 2212 OE2 GLU C 276 3.316 8.145 -6.431 1.00 40.31 O ANISOU 2212 OE2 GLU C 276 5600 6384 3333 -217 435 -174 O ATOM 2213 N GLU C 277 2.311 14.049 -3.026 1.00 38.40 N ANISOU 2213 N GLU C 277 5701 5474 3414 -666 280 324 N ATOM 2214 CA GLU C 277 1.316 14.796 -2.245 1.00 37.63 C ANISOU 2214 CA GLU C 277 5722 5184 3393 -650 205 359 C ATOM 2215 C GLU C 277 0.053 15.103 -3.053 1.00 37.64 C ANISOU 2215 C GLU C 277 5832 5138 3330 -596 177 423 C ATOM 2216 O GLU C 277 -1.058 14.883 -2.560 1.00 36.66 O ANISOU 2216 O GLU C 277 5761 4927 3242 -502 117 384 O ATOM 2217 CB GLU C 277 1.907 16.100 -1.691 1.00 38.61 C ANISOU 2217 CB GLU C 277 5879 5209 3583 -783 196 425 C ATOM 2218 CG GLU C 277 2.920 15.906 -0.564 1.00 38.51 C ANISOU 2218 CG GLU C 277 5762 5220 3648 -818 190 339 C ATOM 2219 CD GLU C 277 4.353 15.736 -1.037 1.00 39.71 C ANISOU 2219 CD GLU C 277 5775 5552 3762 -916 267 329 C ATOM 2220 OE1 GLU C 277 4.580 15.451 -2.230 1.00 40.39 O ANISOU 2220 OE1 GLU C 277 5827 5770 3750 -931 335 369 O ATOM 2221 OE2 GLU C 277 5.269 15.885 -0.207 1.00 40.39 O ANISOU 2221 OE2 GLU C 277 5772 5667 3907 -975 260 272 O ATOM 2222 N GLN C 278 0.235 15.575 -4.294 1.00 38.50 N ANISOU 2222 N GLN C 278 5965 5328 3336 -649 225 520 N ATOM 2223 CA GLN C 278 -0.881 15.891 -5.202 1.00 38.80 C ANISOU 2223 CA GLN C 278 6099 5357 3285 -584 198 588 C ATOM 2224 C GLN C 278 -1.797 14.694 -5.466 1.00 37.83 C ANISOU 2224 C GLN C 278 5942 5307 3126 -451 168 473 C ATOM 2225 O GLN C 278 -2.972 14.858 -5.785 1.00 37.58 O ANISOU 2225 O GLN C 278 5978 5244 3057 -373 115 487 O ATOM 2226 CB GLN C 278 -0.352 16.429 -6.536 1.00 40.51 C ANISOU 2226 CB GLN C 278 6330 5691 3372 -657 269 712 C ATOM 2227 N ARG C 279 -1.244 13.496 -5.320 1.00 37.62 N ANISOU 2227 N ARG C 279 5808 5372 3113 -425 199 355 N ATOM 2228 CA ARG C 279 -1.974 12.244 -5.514 1.00 37.17 C ANISOU 2228 CA ARG C 279 5714 5363 3044 -319 177 230 C ATOM 2229 C ARG C 279 -2.992 11.902 -4.395 1.00 35.68 C ANISOU 2229 C ARG C 279 5557 5035 2965 -258 113 167 C ATOM 2230 O ARG C 279 -3.889 11.087 -4.615 1.00 34.99 O ANISOU 2230 O ARG C 279 5460 4964 2871 -189 88 82 O ATOM 2231 CB ARG C 279 -0.954 11.100 -5.687 1.00 37.75 C ANISOU 2231 CB ARG C 279 5677 5559 3106 -306 234 127 C ATOM 2232 CG ARG C 279 -1.353 10.061 -6.706 1.00 38.39 C ANISOU 2232 CG ARG C 279 5723 5761 3103 -228 241 25 C ATOM 2233 CD ARG C 279 -0.249 9.064 -7.009 1.00 39.04 C ANISOU 2233 CD ARG C 279 5703 5971 3159 -202 299 -74 C ATOM 2234 NE ARG C 279 -0.847 7.822 -7.501 1.00 39.25 N ANISOU 2234 NE ARG C 279 5713 6032 3169 -110 281 -219 N ATOM 2235 CZ ARG C 279 -0.231 6.644 -7.594 1.00 39.70 C ANISOU 2235 CZ ARG C 279 5705 6144 3237 -46 307 -350 C ATOM 2236 NH1 ARG C 279 1.047 6.497 -7.245 1.00 40.15 N ANISOU 2236 NH1 ARG C 279 5691 6256 3308 -49 354 -355 N ATOM 2237 NH2 ARG C 279 -0.910 5.593 -8.055 1.00 39.85 N ANISOU 2237 NH2 ARG C 279 5727 6162 3254 26 283 -487 N ATOM 2238 N PHE C 280 -2.853 12.520 -3.216 1.00 35.06 N ANISOU 2238 N PHE C 280 5510 4830 2982 -288 88 202 N ATOM 2239 CA PHE C 280 -3.684 12.196 -2.046 1.00 33.97 C ANISOU 2239 CA PHE C 280 5389 4580 2937 -232 40 147 C ATOM 2240 C PHE C 280 -4.604 13.342 -1.622 1.00 34.06 C ANISOU 2240 C PHE C 280 5490 4483 2970 -219 -20 213 C ATOM 2241 O PHE C 280 -4.229 14.514 -1.681 1.00 34.62 O ANISOU 2241 O PHE C 280 5619 4501 3034 -273 -27 304 O ATOM 2242 CB PHE C 280 -2.802 11.812 -0.857 1.00 33.14 C ANISOU 2242 CB PHE C 280 5237 4437 2916 -243 54 108 C ATOM 2243 CG PHE C 280 -2.161 10.455 -0.977 1.00 32.73 C ANISOU 2243 CG PHE C 280 5106 4464 2865 -207 97 20 C ATOM 2244 CD1 PHE C 280 -0.906 10.315 -1.556 1.00 33.17 C ANISOU 2244 CD1 PHE C 280 5094 4634 2875 -243 148 15 C ATOM 2245 CD2 PHE C 280 -2.797 9.324 -0.479 1.00 31.88 C ANISOU 2245 CD2 PHE C 280 4993 4311 2808 -137 89 -57 C ATOM 2246 CE1 PHE C 280 -0.300 9.074 -1.647 1.00 33.29 C ANISOU 2246 CE1 PHE C 280 5041 4718 2891 -186 181 -75 C ATOM 2247 CE2 PHE C 280 -2.197 8.077 -0.566 1.00 32.03 C ANISOU 2247 CE2 PHE C 280 4961 4372 2838 -92 124 -137 C ATOM 2248 CZ PHE C 280 -0.944 7.952 -1.146 1.00 32.73 C ANISOU 2248 CZ PHE C 280 4985 4574 2877 -105 166 -151 C ATOM 2249 N THR C 281 -5.805 12.986 -1.173 1.00 33.85 N ANISOU 2249 N THR C 281 5472 4418 2971 -147 -62 163 N ATOM 2250 CA THR C 281 -6.786 13.958 -0.680 1.00 34.28 C ANISOU 2250 CA THR C 281 5598 4384 3043 -104 -123 201 C ATOM 2251 C THR C 281 -7.561 13.393 0.512 1.00 34.00 C ANISOU 2251 C THR C 281 5534 4305 3080 -50 -145 130 C ATOM 2252 O THR C 281 -7.787 12.183 0.594 1.00 33.60 O ANISOU 2252 O THR C 281 5422 4296 3048 -38 -118 57 O ATOM 2253 CB THR C 281 -7.814 14.333 -1.762 1.00 34.89 C ANISOU 2253 CB THR C 281 5712 4514 3031 -49 -159 230 C ATOM 2254 OG1 THR C 281 -8.606 13.186 -2.097 1.00 34.62 O ANISOU 2254 OG1 THR C 281 5606 4567 2979 -7 -159 133 O ATOM 2255 CG2 THR C 281 -7.140 14.861 -3.024 1.00 35.96 C ANISOU 2255 CG2 THR C 281 5881 4710 3071 -93 -131 319 C ATOM 2256 N CYS C 282 -7.971 14.278 1.421 1.00 34.43 N ANISOU 2256 N CYS C 282 5637 4271 3172 -19 -190 151 N ATOM 2257 CA CYS C 282 -8.828 13.910 2.538 1.00 34.27 C ANISOU 2257 CA CYS C 282 5592 4230 3199 40 -208 96 C ATOM 2258 C CYS C 282 -10.269 14.247 2.185 1.00 34.95 C ANISOU 2258 C CYS C 282 5688 4345 3245 115 -256 85 C ATOM 2259 O CYS C 282 -10.604 15.419 2.007 1.00 35.72 O ANISOU 2259 O CYS C 282 5858 4398 3318 158 -307 133 O ATOM 2260 CB CYS C 282 -8.422 14.668 3.798 1.00 34.31 C ANISOU 2260 CB CYS C 282 5631 4149 3255 46 -233 104 C ATOM 2261 SG CYS C 282 -9.505 14.341 5.205 1.00 34.20 S ANISOU 2261 SG CYS C 282 5586 4135 3273 130 -250 47 S ATOM 2262 N TYR C 283 -11.113 13.222 2.085 1.00 35.21 N ANISOU 2262 N TYR C 283 5650 4451 3277 132 -240 19 N ATOM 2263 CA TYR C 283 -12.538 13.410 1.826 1.00 35.88 C ANISOU 2263 CA TYR C 283 5709 4597 3325 203 -285 -13 C ATOM 2264 C TYR C 283 -13.297 13.476 3.148 1.00 35.93 C ANISOU 2264 C TYR C 283 5689 4587 3375 251 -295 -45 C ATOM 2265 O TYR C 283 -13.193 12.565 3.966 1.00 35.50 O ANISOU 2265 O TYR C 283 5586 4528 3372 215 -246 -76 O ATOM 2266 CB TYR C 283 -13.093 12.280 0.951 1.00 36.09 C ANISOU 2266 CB TYR C 283 5656 4728 3327 178 -264 -85 C ATOM 2267 CG TYR C 283 -14.597 12.341 0.749 1.00 36.50 C ANISOU 2267 CG TYR C 283 5651 4874 3345 242 -310 -141 C ATOM 2268 CD1 TYR C 283 -15.157 13.191 -0.199 1.00 37.22 C ANISOU 2268 CD1 TYR C 283 5768 5030 3345 319 -375 -118 C ATOM 2269 CD2 TYR C 283 -15.458 11.552 1.514 1.00 36.44 C ANISOU 2269 CD2 TYR C 283 5557 4901 3389 227 -286 -212 C ATOM 2270 CE1 TYR C 283 -16.531 13.258 -0.381 1.00 37.90 C ANISOU 2270 CE1 TYR C 283 5784 5227 3390 394 -425 -180 C ATOM 2271 CE2 TYR C 283 -16.835 11.611 1.338 1.00 37.19 C ANISOU 2271 CE2 TYR C 283 5573 5107 3451 277 -326 -274 C ATOM 2272 CZ TYR C 283 -17.366 12.464 0.386 1.00 37.88 C ANISOU 2272 CZ TYR C 283 5675 5272 3444 367 -400 -266 C ATOM 2273 OH TYR C 283 -18.728 12.529 0.206 1.00 38.83 O ANISOU 2273 OH TYR C 283 5702 5528 3523 433 -447 -338 O ATOM 2274 N MET C 284 -14.059 14.554 3.333 1.00 36.56 N ANISOU 2274 N MET C 284 5804 4661 3426 342 -358 -34 N ATOM 2275 CA MET C 284 -14.892 14.755 4.511 1.00 36.95 C ANISOU 2275 CA MET C 284 5819 4724 3494 411 -373 -73 C ATOM 2276 C MET C 284 -16.340 14.900 4.059 1.00 37.54 C ANISOU 2276 C MET C 284 5834 4914 3517 495 -416 -120 C ATOM 2277 O MET C 284 -16.629 15.699 3.164 1.00 38.39 O ANISOU 2277 O MET C 284 5990 5031 3566 563 -477 -94 O ATOM 2278 CB MET C 284 -14.440 16.015 5.258 1.00 37.63 C ANISOU 2278 CB MET C 284 6001 4701 3594 466 -418 -39 C ATOM 2279 CG MET C 284 -15.169 16.299 6.566 1.00 38.17 C ANISOU 2279 CG MET C 284 6040 4792 3672 551 -434 -89 C ATOM 2280 SD MET C 284 -16.772 17.127 6.399 1.00 40.50 S ANISOU 2280 SD MET C 284 6313 5168 3906 710 -510 -132 S ATOM 2281 CE MET C 284 -16.291 18.695 5.669 1.00 40.86 C ANISOU 2281 CE MET C 284 6526 5063 3935 773 -594 -65 C ATOM 2282 N GLU C 285 -17.240 14.133 4.673 1.00 37.24 N ANISOU 2282 N GLU C 285 5686 4968 3494 491 -385 -184 N ATOM 2283 CA GLU C 285 -18.686 14.276 4.449 1.00 37.98 C ANISOU 2283 CA GLU C 285 5690 5200 3540 573 -425 -247 C ATOM 2284 C GLU C 285 -19.383 14.397 5.794 1.00 38.38 C ANISOU 2284 C GLU C 285 5683 5297 3604 628 -410 -281 C ATOM 2285 O GLU C 285 -19.042 13.681 6.741 1.00 37.89 O ANISOU 2285 O GLU C 285 5596 5211 3591 557 -339 -275 O ATOM 2286 CB GLU C 285 -19.244 13.087 3.666 1.00 37.93 C ANISOU 2286 CB GLU C 285 5571 5307 3534 488 -392 -312 C ATOM 2287 CG GLU C 285 -20.740 13.152 3.376 1.00 38.85 C ANISOU 2287 CG GLU C 285 5564 5597 3598 558 -435 -395 C ATOM 2288 CD GLU C 285 -21.240 11.989 2.538 1.00 38.96 C ANISOU 2288 CD GLU C 285 5463 5720 3619 458 -410 -479 C ATOM 2289 OE1 GLU C 285 -20.458 11.403 1.762 1.00 38.54 O ANISOU 2289 OE1 GLU C 285 5451 5613 3579 375 -389 -472 O ATOM 2290 OE2 GLU C 285 -22.435 11.659 2.651 1.00 39.67 O ANISOU 2290 OE2 GLU C 285 5414 5960 3700 459 -412 -564 O ATOM 2291 N HIS C 286 -20.372 15.289 5.856 1.00 39.23 N ANISOU 2291 N HIS C 286 5767 5482 3656 768 -478 -317 N ATOM 2292 CA HIS C 286 -21.022 15.649 7.111 1.00 39.53 C ANISOU 2292 CA HIS C 286 5757 5577 3686 855 -476 -355 C ATOM 2293 C HIS C 286 -22.372 16.333 6.848 1.00 40.59 C ANISOU 2293 C HIS C 286 5816 5857 3748 1011 -548 -421 C ATOM 2294 O HIS C 286 -22.420 17.395 6.229 1.00 40.56 O ANISOU 2294 O HIS C 286 5905 5805 3702 1135 -637 -403 O ATOM 2295 CB HIS C 286 -20.090 16.566 7.916 1.00 39.33 C ANISOU 2295 CB HIS C 286 5866 5396 3680 906 -501 -313 C ATOM 2296 CG HIS C 286 -20.741 17.212 9.099 1.00 40.27 C ANISOU 2296 CG HIS C 286 5958 5571 3771 1036 -522 -366 C ATOM 2297 ND1 HIS C 286 -20.999 16.535 10.272 1.00 40.34 N ANISOU 2297 ND1 HIS C 286 5874 5671 3782 1005 -448 -391 N ATOM 2298 CD2 HIS C 286 -21.185 18.477 9.288 1.00 41.25 C ANISOU 2298 CD2 HIS C 286 6139 5676 3857 1208 -610 -401 C ATOM 2299 CE1 HIS C 286 -21.579 17.353 11.130 1.00 41.03 C ANISOU 2299 CE1 HIS C 286 5950 5814 3824 1152 -487 -446 C ATOM 2300 NE2 HIS C 286 -21.700 18.538 10.559 1.00 41.86 N ANISOU 2300 NE2 HIS C 286 6147 5847 3910 1281 -589 -461 N ATOM 2301 N SER C 287 -23.447 15.699 7.321 1.00 41.27 N ANISOU 2301 N SER C 287 5737 6124 3821 1001 -506 -492 N ATOM 2302 CA SER C 287 -24.829 16.195 7.214 1.00 43.01 C ANISOU 2302 CA SER C 287 5839 6534 3968 1147 -563 -576 C ATOM 2303 C SER C 287 -25.186 16.815 5.853 1.00 43.59 C ANISOU 2303 C SER C 287 5942 6640 3979 1253 -666 -585 C ATOM 2304 O SER C 287 -25.494 18.006 5.756 1.00 44.36 O ANISOU 2304 O SER C 287 6111 6722 4022 1446 -759 -586 O ATOM 2305 CB SER C 287 -25.141 17.164 8.365 1.00 43.94 C ANISOU 2305 CB SER C 287 5978 6663 4053 1312 -594 -602 C ATOM 2306 OG SER C 287 -24.364 18.349 8.284 1.00 44.22 O ANISOU 2306 OG SER C 287 6207 6505 4091 1419 -673 -554 O ATOM 2307 N GLY C 288 -25.124 15.988 4.812 1.00 43.44 N ANISOU 2307 N GLY C 288 5876 6662 3966 1135 -649 -591 N ATOM 2308 CA GLY C 288 -25.445 16.400 3.444 1.00 44.35 C ANISOU 2308 CA GLY C 288 6006 6839 4005 1224 -739 -598 C ATOM 2309 C GLY C 288 -24.250 16.898 2.649 1.00 43.49 C ANISOU 2309 C GLY C 288 6094 6538 3894 1215 -767 -487 C ATOM 2310 O GLY C 288 -23.976 16.395 1.557 1.00 43.55 O ANISOU 2310 O GLY C 288 6099 6570 3878 1142 -768 -479 O ATOM 2311 N ASN C 289 -23.549 17.893 3.198 1.00 42.93 N ANISOU 2311 N ASN C 289 6185 6284 3843 1285 -789 -410 N ATOM 2312 CA ASN C 289 -22.420 18.537 2.527 1.00 42.20 C ANISOU 2312 CA ASN C 289 6281 6002 3750 1273 -813 -295 C ATOM 2313 C ASN C 289 -21.181 17.650 2.570 1.00 40.37 C ANISOU 2313 C ASN C 289 6078 5667 3594 1068 -721 -252 C ATOM 2314 O ASN C 289 -21.026 16.842 3.487 1.00 39.89 O ANISOU 2314 O ASN C 289 5946 5611 3600 966 -647 -288 O ATOM 2315 CB ASN C 289 -22.122 19.898 3.171 1.00 42.45 C ANISOU 2315 CB ASN C 289 6470 5862 3796 1401 -868 -244 C ATOM 2316 N HIS C 290 -20.318 17.791 1.562 1.00 39.76 N ANISOU 2316 N HIS C 290 6103 5508 3495 1018 -725 -170 N ATOM 2317 CA HIS C 290 -19.022 17.103 1.534 1.00 38.43 C ANISOU 2317 CA HIS C 290 5972 5241 3387 848 -646 -126 C ATOM 2318 C HIS C 290 -17.942 17.957 0.880 1.00 38.62 C ANISOU 2318 C HIS C 290 6159 5121 3395 837 -661 -7 C ATOM 2319 O HIS C 290 -18.244 18.911 0.170 1.00 39.76 O ANISOU 2319 O HIS C 290 6389 5250 3468 949 -729 51 O ATOM 2320 CB HIS C 290 -19.124 15.729 0.844 1.00 37.90 C ANISOU 2320 CB HIS C 290 5786 5297 3316 735 -595 -188 C ATOM 2321 CG HIS C 290 -19.580 15.782 -0.582 1.00 38.68 C ANISOU 2321 CG HIS C 290 5867 5517 3312 789 -647 -196 C ATOM 2322 ND1 HIS C 290 -18.703 15.845 -1.644 1.00 38.62 N ANISOU 2322 ND1 HIS C 290 5940 5478 3255 748 -639 -125 N ATOM 2323 CD2 HIS C 290 -20.823 15.755 -1.124 1.00 39.67 C ANISOU 2323 CD2 HIS C 290 5891 5820 3361 884 -707 -272 C ATOM 2324 CE1 HIS C 290 -19.386 15.873 -2.776 1.00 39.53 C ANISOU 2324 CE1 HIS C 290 6016 5742 3262 824 -695 -151 C ATOM 2325 NE2 HIS C 290 -20.673 15.818 -2.488 1.00 40.03 N ANISOU 2325 NE2 HIS C 290 5966 5934 3308 908 -741 -245 N ATOM 2326 N SER C 291 -16.686 17.611 1.144 1.00 37.93 N ANISOU 2326 N SER C 291 6111 4930 3370 703 -597 32 N ATOM 2327 CA SER C 291 -15.542 18.338 0.589 1.00 38.29 C ANISOU 2327 CA SER C 291 6291 4849 3411 655 -592 143 C ATOM 2328 C SER C 291 -14.295 17.468 0.519 1.00 37.47 C ANISOU 2328 C SER C 291 6160 4727 3350 498 -509 153 C ATOM 2329 O SER C 291 -14.205 16.429 1.176 1.00 36.35 O ANISOU 2329 O SER C 291 5927 4624 3262 437 -460 83 O ATOM 2330 CB SER C 291 -15.247 19.580 1.426 1.00 38.94 C ANISOU 2330 CB SER C 291 6493 4760 3543 702 -632 186 C ATOM 2331 OG SER C 291 -14.917 19.229 2.761 1.00 38.18 O ANISOU 2331 OG SER C 291 6352 4624 3529 655 -599 124 O ATOM 2332 N THR C 292 -13.336 17.921 -0.280 1.00 38.13 N ANISOU 2332 N THR C 292 6328 4756 3405 439 -493 247 N ATOM 2333 CA THR C 292 -12.078 17.213 -0.501 1.00 38.07 C ANISOU 2333 CA THR C 292 6292 4752 3421 305 -417 260 C ATOM 2334 C THR C 292 -10.931 18.187 -0.234 1.00 38.66 C ANISOU 2334 C THR C 292 6469 4682 3538 235 -406 348 C ATOM 2335 O THR C 292 -10.977 19.332 -0.682 1.00 40.12 O ANISOU 2335 O THR C 292 6768 4784 3691 268 -443 440 O ATOM 2336 CB THR C 292 -12.020 16.649 -1.937 1.00 38.61 C ANISOU 2336 CB THR C 292 6327 4951 3392 287 -394 271 C ATOM 2337 OG1 THR C 292 -13.238 15.948 -2.219 1.00 38.94 O ANISOU 2337 OG1 THR C 292 6279 5122 3395 357 -424 178 O ATOM 2338 CG2 THR C 292 -10.866 15.692 -2.108 1.00 38.00 C ANISOU 2338 CG2 THR C 292 6193 4907 3337 172 -316 249 C ATOM 2339 N HIS C 293 -9.918 17.743 0.511 1.00 38.12 N ANISOU 2339 N HIS C 293 6361 4580 3542 140 -357 320 N ATOM 2340 CA HIS C 293 -8.872 18.647 1.000 1.00 38.70 C ANISOU 2340 CA HIS C 293 6507 4523 3674 64 -354 372 C ATOM 2341 C HIS C 293 -7.476 18.178 0.619 1.00 38.57 C ANISOU 2341 C HIS C 293 6443 4549 3661 -67 -281 395 C ATOM 2342 O HIS C 293 -7.127 17.025 0.858 1.00 37.37 O ANISOU 2342 O HIS C 293 6192 4484 3523 -88 -238 327 O ATOM 2343 CB HIS C 293 -8.994 18.811 2.511 1.00 38.36 C ANISOU 2343 CB HIS C 293 6455 4408 3713 96 -384 299 C ATOM 2344 CG HIS C 293 -10.319 19.354 2.930 1.00 38.69 C ANISOU 2344 CG HIS C 293 6535 4422 3746 232 -453 270 C ATOM 2345 ND1 HIS C 293 -10.562 20.704 3.049 1.00 39.85 N ANISOU 2345 ND1 HIS C 293 6803 4432 3905 287 -517 309 N ATOM 2346 CD2 HIS C 293 -11.493 18.733 3.191 1.00 38.38 C ANISOU 2346 CD2 HIS C 293 6423 4479 3682 327 -468 202 C ATOM 2347 CE1 HIS C 293 -11.824 20.891 3.393 1.00 40.19 C ANISOU 2347 CE1 HIS C 293 6843 4501 3925 430 -572 260 C ATOM 2348 NE2 HIS C 293 -12.409 19.711 3.490 1.00 39.32 N ANISOU 2348 NE2 HIS C 293 6607 4543 3791 448 -540 196 N ATOM 2349 N PRO C 294 -6.673 19.075 0.023 1.00 39.97 N ANISOU 2349 N PRO C 294 6694 4666 3827 -153 -263 494 N ATOM 2350 CA PRO C 294 -5.350 18.682 -0.440 1.00 40.74 C ANISOU 2350 CA PRO C 294 6731 4835 3915 -278 -188 517 C ATOM 2351 C PRO C 294 -4.320 18.561 0.680 1.00 40.81 C ANISOU 2351 C PRO C 294 6680 4813 4014 -355 -172 455 C ATOM 2352 O PRO C 294 -4.541 19.050 1.787 1.00 40.66 O ANISOU 2352 O PRO C 294 6693 4691 4066 -328 -223 412 O ATOM 2353 CB PRO C 294 -4.968 19.823 -1.393 1.00 42.33 C ANISOU 2353 CB PRO C 294 7037 4974 4072 -350 -173 658 C ATOM 2354 CG PRO C 294 -5.665 21.014 -0.842 1.00 42.70 C ANISOU 2354 CG PRO C 294 7216 4840 4170 -294 -249 690 C ATOM 2355 CD PRO C 294 -6.957 20.494 -0.277 1.00 41.52 C ANISOU 2355 CD PRO C 294 7036 4723 4019 -139 -308 594 C ATOM 2356 N VAL C 295 -3.209 17.903 0.361 1.00 41.60 N ANISOU 2356 N VAL C 295 6686 5021 4099 -438 -106 443 N ATOM 2357 CA VAL C 295 -2.041 17.820 1.230 1.00 42.35 C ANISOU 2357 CA VAL C 295 6707 5122 4261 -517 -88 391 C ATOM 2358 C VAL C 295 -1.143 19.029 0.945 1.00 44.81 C ANISOU 2358 C VAL C 295 7064 5363 4597 -665 -70 472 C ATOM 2359 O VAL C 295 -0.749 19.231 -0.202 1.00 46.02 O ANISOU 2359 O VAL C 295 7227 5573 4687 -738 -14 562 O ATOM 2360 CB VAL C 295 -1.242 16.522 0.958 1.00 41.74 C ANISOU 2360 CB VAL C 295 6499 5210 4151 -522 -25 335 C ATOM 2361 CG1 VAL C 295 0.041 16.470 1.789 1.00 41.93 C ANISOU 2361 CG1 VAL C 295 6433 5269 4229 -592 -11 281 C ATOM 2362 CG2 VAL C 295 -2.114 15.299 1.214 1.00 40.38 C ANISOU 2362 CG2 VAL C 295 6296 5079 3970 -395 -37 260 C ATOM 2363 N PRO C 296 -0.821 19.841 1.976 1.00 46.62 N ANISOU 2363 N PRO C 296 7325 5473 4918 -714 -114 438 N ATOM 2364 CA PRO C 296 0.218 20.873 1.791 1.00 48.80 C ANISOU 2364 CA PRO C 296 7621 5685 5238 -890 -89 494 C ATOM 2365 C PRO C 296 1.594 20.279 1.468 1.00 49.97 C ANISOU 2365 C PRO C 296 7616 6007 5363 -1003 -9 475 C ATOM 2366 O PRO C 296 1.911 19.171 1.915 1.00 49.09 O ANISOU 2366 O PRO C 296 7383 6031 5238 -935 -1 380 O ATOM 2367 CB PRO C 296 0.251 21.597 3.147 1.00 48.82 C ANISOU 2367 CB PRO C 296 7657 5548 5344 -898 -165 409 C ATOM 2368 CG PRO C 296 -1.094 21.360 3.740 1.00 47.66 C ANISOU 2368 CG PRO C 296 7568 5350 5189 -715 -232 362 C ATOM 2369 CD PRO C 296 -1.509 19.988 3.274 1.00 46.17 C ANISOU 2369 CD PRO C 296 7299 5324 4921 -616 -192 352 C ATOM 2370 N SER C 297 2.391 21.015 0.695 1.00 52.72 N ANISOU 2370 N SER C 297 7973 6353 5704 -1170 50 570 N ATOM 2371 CA SER C 297 3.738 20.583 0.303 1.00 54.08 C ANISOU 2371 CA SER C 297 7988 6712 5847 -1291 134 557 C ATOM 2372 C SER C 297 4.762 21.638 0.701 1.00 56.11 C ANISOU 2372 C SER C 297 8224 6899 6195 -1496 144 561 C ATOM 2373 O SER C 297 5.208 21.677 1.850 1.00 56.53 O ANISOU 2373 O SER C 297 8209 6941 6329 -1511 93 440 O ATOM 2374 CB SER C 297 3.796 20.315 -1.205 1.00 54.86 C ANISOU 2374 CB SER C 297 8082 6937 5825 -1312 222 671 C ATOM 2375 OG SER C 297 3.388 21.457 -1.935 1.00 56.42 O ANISOU 2375 OG SER C 297 8437 6990 6008 -1387 233 826 O ATOM 2376 OXT SER C 297 5.167 22.475 -0.103 1.00 58.10 O ANISOU 2376 OXT SER C 297 8526 7107 6442 -1657 204 683 O TER 2377 SER C 297 ATOM 2378 N ASP A 1 -26.203 5.842 37.322 1.00 39.19 N ANISOU 2378 N ASP A 1 4093 6129 4667 252 69 -191 N ATOM 2379 CA ASP A 1 -24.750 5.680 37.011 1.00 38.07 C ANISOU 2379 CA ASP A 1 4089 5841 4535 222 57 -186 C ATOM 2380 C ASP A 1 -24.409 4.239 36.677 1.00 37.17 C ANISOU 2380 C ASP A 1 4028 5707 4390 94 52 -136 C ATOM 2381 O ASP A 1 -25.128 3.315 37.051 1.00 37.66 O ANISOU 2381 O ASP A 1 4035 5856 4419 15 65 -107 O ATOM 2382 CB ASP A 1 -23.881 6.125 38.194 1.00 37.94 C ANISOU 2382 CB ASP A 1 4120 5790 4508 271 99 -232 C ATOM 2383 CG ASP A 1 -24.110 7.579 38.597 1.00 38.99 C ANISOU 2383 CG ASP A 1 4225 5920 4669 407 92 -292 C ATOM 2384 OD1 ASP A 1 -25.006 8.248 38.030 1.00 39.61 O ANISOU 2384 OD1 ASP A 1 4240 6033 4775 473 57 -300 O ATOM 2385 OD2 ASP A 1 -23.383 8.051 39.502 1.00 39.40 O ANISOU 2385 OD2 ASP A 1 4325 5931 4714 452 114 -335 O ATOM 2386 N VAL A 2 -23.298 4.058 35.975 1.00 36.23 N ANISOU 2386 N VAL A 2 4014 5473 4278 76 27 -127 N ATOM 2387 CA VAL A 2 -22.781 2.728 35.678 1.00 35.67 C ANISOU 2387 CA VAL A 2 4016 5363 4176 -21 15 -96 C ATOM 2388 C VAL A 2 -21.968 2.250 36.877 1.00 35.27 C ANISOU 2388 C VAL A 2 4012 5294 4095 -42 60 -109 C ATOM 2389 O VAL A 2 -20.905 2.810 37.178 1.00 34.51 O ANISOU 2389 O VAL A 2 3971 5134 4007 9 77 -134 O ATOM 2390 CB VAL A 2 -21.898 2.725 34.414 1.00 34.95 C ANISOU 2390 CB VAL A 2 4012 5177 4091 -17 -27 -86 C ATOM 2391 CG1 VAL A 2 -21.312 1.333 34.160 1.00 34.58 C ANISOU 2391 CG1 VAL A 2 4048 5086 4004 -95 -44 -69 C ATOM 2392 CG2 VAL A 2 -22.705 3.207 33.214 1.00 35.47 C ANISOU 2392 CG2 VAL A 2 4035 5262 4181 1 -76 -68 C ATOM 2393 N LEU A 3 -22.472 1.222 37.556 1.00 35.42 N ANISOU 2393 N LEU A 3 4006 5371 4079 -125 74 -84 N ATOM 2394 CA LEU A 3 -21.749 0.600 38.661 1.00 35.10 C ANISOU 2394 CA LEU A 3 4016 5315 4006 -159 107 -86 C ATOM 2395 C LEU A 3 -20.819 -0.466 38.109 1.00 34.21 C ANISOU 2395 C LEU A 3 4019 5102 3877 -212 70 -68 C ATOM 2396 O LEU A 3 -21.187 -1.188 37.184 1.00 34.09 O ANISOU 2396 O LEU A 3 4026 5068 3858 -266 18 -43 O ATOM 2397 CB LEU A 3 -22.722 0.007 39.682 1.00 36.09 C ANISOU 2397 CB LEU A 3 4062 5557 4094 -229 134 -58 C ATOM 2398 CG LEU A 3 -23.719 1.012 40.274 1.00 37.12 C ANISOU 2398 CG LEU A 3 4064 5814 4226 -162 175 -83 C ATOM 2399 CD1 LEU A 3 -24.708 0.324 41.205 1.00 38.03 C ANISOU 2399 CD1 LEU A 3 4085 6073 4290 -244 202 -43 C ATOM 2400 CD2 LEU A 3 -22.993 2.142 40.991 1.00 36.76 C ANISOU 2400 CD2 LEU A 3 4036 5740 4192 -50 215 -145 C ATOM 2401 N MET A 4 -19.619 -0.549 38.685 1.00 33.39 N ANISOU 2401 N MET A 4 3987 4938 3761 -190 91 -87 N ATOM 2402 CA MET A 4 -18.535 -1.399 38.188 1.00 32.96 C ANISOU 2402 CA MET A 4 4042 4791 3690 -206 59 -84 C ATOM 2403 C MET A 4 -18.038 -2.326 39.309 1.00 32.70 C ANISOU 2403 C MET A 4 4060 4741 3623 -254 71 -73 C ATOM 2404 O MET A 4 -17.354 -1.876 40.227 1.00 32.39 O ANISOU 2404 O MET A 4 4026 4703 3580 -217 113 -92 O ATOM 2405 CB MET A 4 -17.386 -0.514 37.679 1.00 32.53 C ANISOU 2405 CB MET A 4 4024 4683 3652 -121 67 -111 C ATOM 2406 CG MET A 4 -17.749 0.411 36.521 1.00 32.89 C ANISOU 2406 CG MET A 4 4033 4734 3729 -77 46 -113 C ATOM 2407 SD MET A 4 -17.904 -0.430 34.928 1.00 33.56 S ANISOU 2407 SD MET A 4 4165 4790 3797 -109 -18 -95 S ATOM 2408 CE MET A 4 -16.190 -0.502 34.427 1.00 32.65 C ANISOU 2408 CE MET A 4 4138 4614 3655 -58 -20 -110 C ATOM 2409 N THR A 5 -18.390 -3.611 39.236 1.00 32.74 N ANISOU 2409 N THR A 5 4109 4727 3603 -341 24 -40 N ATOM 2410 CA THR A 5 -18.030 -4.602 40.262 1.00 32.48 C ANISOU 2410 CA THR A 5 4132 4672 3538 -402 19 -18 C ATOM 2411 C THR A 5 -16.936 -5.545 39.768 1.00 31.97 C ANISOU 2411 C THR A 5 4196 4495 3457 -389 -34 -29 C ATOM 2412 O THR A 5 -17.099 -6.178 38.730 1.00 32.24 O ANISOU 2412 O THR A 5 4281 4480 3489 -407 -96 -27 O ATOM 2413 CB THR A 5 -19.252 -5.452 40.652 1.00 33.22 C ANISOU 2413 CB THR A 5 4189 4823 3611 -523 -10 39 C ATOM 2414 OG1 THR A 5 -20.269 -4.599 41.175 1.00 33.46 O ANISOU 2414 OG1 THR A 5 4087 4982 3645 -522 44 46 O ATOM 2415 CG2 THR A 5 -18.889 -6.505 41.699 1.00 33.64 C ANISOU 2415 CG2 THR A 5 4308 4847 3627 -598 -28 74 C ATOM 2416 N GLN A 6 -15.848 -5.650 40.531 1.00 31.42 N ANISOU 2416 N GLN A 6 4176 4390 3373 -355 -12 -43 N ATOM 2417 CA GLN A 6 -14.727 -6.539 40.210 1.00 31.25 C ANISOU 2417 CA GLN A 6 4271 4272 3330 -325 -59 -59 C ATOM 2418 C GLN A 6 -14.709 -7.828 41.039 1.00 32.24 C ANISOU 2418 C GLN A 6 4473 4350 3427 -402 -107 -25 C ATOM 2419 O GLN A 6 -15.147 -7.845 42.194 1.00 32.57 O ANISOU 2419 O GLN A 6 4475 4443 3459 -466 -78 10 O ATOM 2420 CB GLN A 6 -13.402 -5.805 40.397 1.00 30.03 C ANISOU 2420 CB GLN A 6 4122 4110 3176 -228 -14 -94 C ATOM 2421 CG GLN A 6 -13.198 -4.690 39.391 1.00 29.35 C ANISOU 2421 CG GLN A 6 3989 4050 3114 -157 10 -119 C ATOM 2422 CD GLN A 6 -11.862 -3.984 39.521 1.00 28.69 C ANISOU 2422 CD GLN A 6 3908 3965 3027 -79 44 -141 C ATOM 2423 OE1 GLN A 6 -11.800 -2.756 39.458 1.00 28.14 O ANISOU 2423 OE1 GLN A 6 3778 3931 2982 -46 80 -147 O ATOM 2424 NE2 GLN A 6 -10.786 -4.746 39.685 1.00 28.54 N ANISOU 2424 NE2 GLN A 6 3961 3904 2978 -49 24 -151 N ATOM 2425 N THR A 7 -14.180 -8.890 40.434 1.00 32.92 N ANISOU 2425 N THR A 7 4673 4338 3496 -391 -184 -36 N ATOM 2426 CA THR A 7 -14.005 -10.185 41.084 1.00 34.09 C ANISOU 2426 CA THR A 7 4922 4410 3619 -453 -252 -7 C ATOM 2427 C THR A 7 -12.662 -10.794 40.671 1.00 34.51 C ANISOU 2427 C THR A 7 5089 4370 3653 -353 -297 -54 C ATOM 2428 O THR A 7 -12.406 -10.896 39.476 1.00 35.39 O ANISOU 2428 O THR A 7 5238 4449 3760 -287 -330 -96 O ATOM 2429 CB THR A 7 -15.116 -11.169 40.667 1.00 34.94 C ANISOU 2429 CB THR A 7 5073 4480 3722 -567 -342 36 C ATOM 2430 OG1 THR A 7 -16.386 -10.652 41.074 1.00 35.36 O ANISOU 2430 OG1 THR A 7 5007 4642 3786 -660 -301 85 O ATOM 2431 CG2 THR A 7 -14.913 -12.548 41.296 1.00 35.66 C ANISOU 2431 CG2 THR A 7 5288 4471 3788 -638 -434 72 C ATOM 2432 N PRO A 8 -11.806 -11.214 41.607 1.00 35.14 N ANISOU 2432 N PRO A 8 5223 4415 3716 -335 -300 -50 N ATOM 2433 CA PRO A 8 -11.986 -11.077 43.049 1.00 35.35 C ANISOU 2433 CA PRO A 8 5208 4486 3737 -405 -259 -2 C ATOM 2434 C PRO A 8 -11.480 -9.722 43.544 1.00 34.66 C ANISOU 2434 C PRO A 8 5020 4489 3662 -340 -153 -25 C ATOM 2435 O PRO A 8 -10.979 -8.922 42.753 1.00 33.90 O ANISOU 2435 O PRO A 8 4888 4414 3579 -251 -118 -69 O ATOM 2436 CB PRO A 8 -11.102 -12.195 43.590 1.00 36.07 C ANISOU 2436 CB PRO A 8 5424 4479 3804 -391 -329 3 C ATOM 2437 CG PRO A 8 -9.947 -12.212 42.640 1.00 35.69 C ANISOU 2437 CG PRO A 8 5426 4386 3749 -249 -344 -67 C ATOM 2438 CD PRO A 8 -10.515 -11.855 41.287 1.00 35.45 C ANISOU 2438 CD PRO A 8 5365 4374 3732 -229 -347 -96 C ATOM 2439 N LEU A 9 -11.611 -9.479 44.846 1.00 34.81 N ANISOU 2439 N LEU A 9 4997 4560 3669 -389 -109 6 N ATOM 2440 CA LEU A 9 -11.085 -8.264 45.464 1.00 34.11 C ANISOU 2440 CA LEU A 9 4832 4542 3586 -331 -23 -18 C ATOM 2441 C LEU A 9 -9.605 -8.463 45.798 1.00 33.44 C ANISOU 2441 C LEU A 9 4809 4410 3487 -255 -31 -40 C ATOM 2442 O LEU A 9 -8.807 -7.539 45.671 1.00 32.34 O ANISOU 2442 O LEU A 9 4632 4300 3358 -177 14 -74 O ATOM 2443 CB LEU A 9 -11.899 -7.887 46.706 1.00 34.86 C ANISOU 2443 CB LEU A 9 4853 4728 3666 -407 27 17 C ATOM 2444 CG LEU A 9 -13.440 -7.904 46.590 1.00 35.89 C ANISOU 2444 CG LEU A 9 4912 4927 3796 -497 30 53 C ATOM 2445 CD1 LEU A 9 -14.056 -7.074 47.708 1.00 36.28 C ANISOU 2445 CD1 LEU A 9 4858 5100 3826 -519 107 60 C ATOM 2446 CD2 LEU A 9 -13.963 -7.411 45.245 1.00 35.89 C ANISOU 2446 CD2 LEU A 9 4874 4930 3833 -462 26 26 C ATOM 2447 N SER A 10 -9.248 -9.674 46.220 1.00 33.90 N ANISOU 2447 N SER A 10 4965 4396 3521 -282 -97 -16 N ATOM 2448 CA SER A 10 -7.849 -10.077 46.350 1.00 33.91 C ANISOU 2448 CA SER A 10 5035 4344 3507 -197 -124 -39 C ATOM 2449 C SER A 10 -7.597 -11.351 45.542 1.00 34.09 C ANISOU 2449 C SER A 10 5174 4260 3518 -168 -223 -52 C ATOM 2450 O SER A 10 -8.439 -12.249 45.489 1.00 34.23 O ANISOU 2450 O SER A 10 5252 4222 3533 -252 -291 -18 O ATOM 2451 CB SER A 10 -7.461 -10.283 47.817 1.00 34.28 C ANISOU 2451 CB SER A 10 5097 4399 3528 -235 -115 -6 C ATOM 2452 OG SER A 10 -8.334 -11.202 48.447 1.00 35.44 O ANISOU 2452 OG SER A 10 5288 4520 3657 -351 -164 54 O ATOM 2453 N LEU A 11 -6.414 -11.412 44.941 1.00 33.82 N ANISOU 2453 N LEU A 11 5172 4204 3474 -47 -236 -100 N ATOM 2454 CA LEU A 11 -6.074 -12.414 43.951 1.00 34.74 C ANISOU 2454 CA LEU A 11 5389 4236 3575 22 -322 -136 C ATOM 2455 C LEU A 11 -4.662 -12.936 44.225 1.00 35.34 C ANISOU 2455 C LEU A 11 5526 4280 3623 132 -354 -163 C ATOM 2456 O LEU A 11 -3.680 -12.377 43.721 1.00 34.70 O ANISOU 2456 O LEU A 11 5397 4260 3530 241 -314 -203 O ATOM 2457 CB LEU A 11 -6.171 -11.779 42.557 1.00 34.27 C ANISOU 2457 CB LEU A 11 5278 4222 3522 83 -294 -179 C ATOM 2458 CG LEU A 11 -5.862 -12.613 41.311 1.00 34.77 C ANISOU 2458 CG LEU A 11 5429 4223 3559 172 -371 -232 C ATOM 2459 CD1 LEU A 11 -6.652 -13.912 41.274 1.00 35.68 C ANISOU 2459 CD1 LEU A 11 5668 4217 3672 102 -483 -217 C ATOM 2460 CD2 LEU A 11 -6.166 -11.778 40.080 1.00 34.39 C ANISOU 2460 CD2 LEU A 11 5306 4244 3515 201 -327 -258 C ATOM 2461 N PRO A 12 -4.550 -13.984 45.066 1.00 36.82 N ANISOU 2461 N PRO A 12 5813 4380 3797 99 -429 -135 N ATOM 2462 CA PRO A 12 -3.264 -14.670 45.212 1.00 37.61 C ANISOU 2462 CA PRO A 12 5987 4433 3869 217 -482 -166 C ATOM 2463 C PRO A 12 -2.969 -15.538 43.992 1.00 38.66 C ANISOU 2463 C PRO A 12 6217 4492 3981 327 -569 -230 C ATOM 2464 O PRO A 12 -3.831 -16.312 43.575 1.00 39.07 O ANISOU 2464 O PRO A 12 6357 4450 4038 269 -651 -224 O ATOM 2465 CB PRO A 12 -3.447 -15.539 46.472 1.00 38.44 C ANISOU 2465 CB PRO A 12 6178 4458 3970 129 -548 -106 C ATOM 2466 CG PRO A 12 -4.730 -15.108 47.100 1.00 38.02 C ANISOU 2466 CG PRO A 12 6065 4445 3934 -35 -504 -40 C ATOM 2467 CD PRO A 12 -5.557 -14.492 46.016 1.00 37.46 C ANISOU 2467 CD PRO A 12 5928 4419 3884 -51 -463 -64 C ATOM 2468 N VAL A 13 -1.774 -15.393 43.424 1.00 39.32 N ANISOU 2468 N VAL A 13 6280 4626 4036 482 -553 -289 N ATOM 2469 CA VAL A 13 -1.345 -16.187 42.264 1.00 40.82 C ANISOU 2469 CA VAL A 13 6554 4766 4189 618 -630 -364 C ATOM 2470 C VAL A 13 0.139 -16.506 42.353 1.00 41.71 C ANISOU 2470 C VAL A 13 6679 4908 4260 784 -647 -409 C ATOM 2471 O VAL A 13 0.941 -15.660 42.764 1.00 40.97 O ANISOU 2471 O VAL A 13 6474 4931 4161 814 -561 -395 O ATOM 2472 CB VAL A 13 -1.619 -15.478 40.909 1.00 40.76 C ANISOU 2472 CB VAL A 13 6471 4843 4173 654 -577 -403 C ATOM 2473 CG1 VAL A 13 -3.109 -15.470 40.592 1.00 41.02 C ANISOU 2473 CG1 VAL A 13 6520 4827 4240 516 -594 -373 C ATOM 2474 CG2 VAL A 13 -1.049 -14.058 40.880 1.00 39.83 C ANISOU 2474 CG2 VAL A 13 6190 4886 4056 672 -450 -390 C ATOM 2475 N SER A 14 0.496 -17.727 41.967 1.00 43.63 N ANISOU 2475 N SER A 14 7061 5045 4472 893 -764 -464 N ATOM 2476 CA SER A 14 1.884 -18.180 42.002 1.00 44.88 C ANISOU 2476 CA SER A 14 7240 5229 4585 1073 -795 -517 C ATOM 2477 C SER A 14 2.620 -17.612 40.794 1.00 45.05 C ANISOU 2477 C SER A 14 7164 5399 4556 1219 -731 -583 C ATOM 2478 O SER A 14 2.002 -17.355 39.756 1.00 44.52 O ANISOU 2478 O SER A 14 7081 5354 4482 1206 -714 -609 O ATOM 2479 CB SER A 14 1.940 -19.714 41.997 1.00 46.51 C ANISOU 2479 CB SER A 14 7642 5255 4773 1148 -957 -558 C ATOM 2480 OG SER A 14 1.112 -20.261 43.021 1.00 46.91 O ANISOU 2480 OG SER A 14 7788 5168 4868 986 -1026 -482 O ATOM 2481 N LEU A 15 3.931 -17.404 40.937 1.00 45.56 N ANISOU 2481 N LEU A 15 7155 5576 4580 1351 -695 -604 N ATOM 2482 CA LEU A 15 4.769 -16.918 39.828 1.00 45.68 C ANISOU 2482 CA LEU A 15 7065 5758 4532 1496 -636 -660 C ATOM 2483 C LEU A 15 4.664 -17.854 38.629 1.00 46.34 C ANISOU 2483 C LEU A 15 7258 5786 4562 1632 -724 -756 C ATOM 2484 O LEU A 15 4.740 -19.070 38.784 1.00 47.41 O ANISOU 2484 O LEU A 15 7549 5777 4686 1713 -847 -804 O ATOM 2485 CB LEU A 15 6.237 -16.796 40.251 1.00 46.27 C ANISOU 2485 CB LEU A 15 7058 5957 4564 1624 -608 -666 C ATOM 2486 CG LEU A 15 6.562 -15.647 41.213 1.00 45.42 C ANISOU 2486 CG LEU A 15 6814 5951 4492 1510 -509 -580 C ATOM 2487 CD1 LEU A 15 7.892 -15.883 41.922 1.00 46.12 C ANISOU 2487 CD1 LEU A 15 6868 6106 4549 1621 -521 -580 C ATOM 2488 CD2 LEU A 15 6.568 -14.313 40.481 1.00 44.64 C ANISOU 2488 CD2 LEU A 15 6557 6018 4386 1463 -396 -553 C ATOM 2489 N GLY A 16 4.460 -17.274 37.448 1.00 45.98 N ANISOU 2489 N GLY A 16 7139 5847 4485 1652 -668 -784 N ATOM 2490 CA GLY A 16 4.305 -18.037 36.209 1.00 46.88 C ANISOU 2490 CA GLY A 16 7347 5926 4539 1778 -742 -880 C ATOM 2491 C GLY A 16 2.917 -18.592 35.927 1.00 46.67 C ANISOU 2491 C GLY A 16 7458 5721 4555 1665 -826 -883 C ATOM 2492 O GLY A 16 2.714 -19.200 34.882 1.00 47.56 O ANISOU 2492 O GLY A 16 7656 5796 4618 1758 -895 -964 O ATOM 2493 N ASP A 17 1.964 -18.377 36.835 1.00 45.76 N ANISOU 2493 N ASP A 17 7357 5508 4522 1465 -822 -796 N ATOM 2494 CA ASP A 17 0.601 -18.901 36.699 1.00 46.05 C ANISOU 2494 CA ASP A 17 7510 5385 4601 1332 -903 -780 C ATOM 2495 C ASP A 17 -0.271 -17.898 35.935 1.00 45.04 C ANISOU 2495 C ASP A 17 7277 5345 4490 1227 -818 -752 C ATOM 2496 O ASP A 17 0.127 -16.743 35.748 1.00 44.03 O ANISOU 2496 O ASP A 17 6990 5383 4355 1229 -697 -727 O ATOM 2497 CB ASP A 17 0.017 -19.156 38.097 1.00 46.09 C ANISOU 2497 CB ASP A 17 7566 5269 4676 1168 -936 -692 C ATOM 2498 CG ASP A 17 -1.061 -20.228 38.115 1.00 47.23 C ANISOU 2498 CG ASP A 17 7882 5215 4846 1070 -1076 -684 C ATOM 2499 OD1 ASP A 17 -1.619 -20.579 37.049 1.00 48.40 O ANISOU 2499 OD1 ASP A 17 8098 5318 4975 1089 -1134 -735 O ATOM 2500 OD2 ASP A 17 -1.354 -20.721 39.224 1.00 47.66 O ANISOU 2500 OD2 ASP A 17 8007 5162 4939 965 -1131 -620 O ATOM 2501 N GLN A 18 -1.448 -18.337 35.486 1.00 45.30 N ANISOU 2501 N GLN A 18 7400 5267 4545 1133 -890 -752 N ATOM 2502 CA GLN A 18 -2.403 -17.433 34.838 1.00 44.60 C ANISOU 2502 CA GLN A 18 7217 5248 4479 1022 -821 -717 C ATOM 2503 C GLN A 18 -3.342 -16.807 35.868 1.00 43.02 C ANISOU 2503 C GLN A 18 6952 5034 4360 820 -768 -613 C ATOM 2504 O GLN A 18 -4.033 -17.522 36.587 1.00 43.60 O ANISOU 2504 O GLN A 18 7120 4976 4469 712 -846 -574 O ATOM 2505 CB GLN A 18 -3.232 -18.142 33.758 1.00 46.06 C ANISOU 2505 CB GLN A 18 7517 5341 4643 1021 -923 -769 C ATOM 2506 CG GLN A 18 -3.831 -17.162 32.750 1.00 46.11 C ANISOU 2506 CG GLN A 18 7412 5462 4645 976 -845 -759 C ATOM 2507 CD GLN A 18 -5.128 -17.628 32.115 1.00 47.02 C ANISOU 2507 CD GLN A 18 7613 5474 4776 876 -933 -761 C ATOM 2508 OE1 GLN A 18 -6.137 -17.818 32.795 1.00 47.50 O ANISOU 2508 OE1 GLN A 18 7704 5443 4899 711 -969 -692 O ATOM 2509 NE2 GLN A 18 -5.116 -17.781 30.796 1.00 47.96 N ANISOU 2509 NE2 GLN A 18 7764 5625 4834 970 -965 -834 N ATOM 2510 N ALA A 19 -3.351 -15.475 35.927 1.00 41.24 N ANISOU 2510 N ALA A 19 6567 4947 4156 772 -641 -569 N ATOM 2511 CA ALA A 19 -4.316 -14.706 36.719 1.00 39.60 C ANISOU 2511 CA ALA A 19 6280 4752 4016 600 -581 -484 C ATOM 2512 C ALA A 19 -5.343 -14.080 35.787 1.00 38.69 C ANISOU 2512 C ALA A 19 6107 4678 3914 532 -554 -474 C ATOM 2513 O ALA A 19 -5.001 -13.666 34.678 1.00 38.73 O ANISOU 2513 O ALA A 19 6070 4765 3882 617 -527 -515 O ATOM 2514 CB ALA A 19 -3.602 -13.617 37.499 1.00 38.65 C ANISOU 2514 CB ALA A 19 6031 4744 3910 600 -470 -445 C ATOM 2515 N SER A 20 -6.595 -14.006 36.234 1.00 37.79 N ANISOU 2515 N SER A 20 5986 4521 3851 379 -563 -416 N ATOM 2516 CA SER A 20 -7.633 -13.291 35.490 1.00 36.81 C ANISOU 2516 CA SER A 20 5790 4448 3750 306 -531 -397 C ATOM 2517 C SER A 20 -8.595 -12.567 36.430 1.00 35.50 C ANISOU 2517 C SER A 20 5533 4314 3641 162 -473 -321 C ATOM 2518 O SER A 20 -8.959 -13.099 37.478 1.00 35.40 O ANISOU 2518 O SER A 20 5559 4243 3647 77 -502 -279 O ATOM 2519 CB SER A 20 -8.384 -14.234 34.535 1.00 37.79 C ANISOU 2519 CB SER A 20 6022 4482 3854 289 -641 -429 C ATOM 2520 OG SER A 20 -9.140 -15.204 35.224 1.00 38.62 O ANISOU 2520 OG SER A 20 6223 4468 3983 177 -732 -391 O ATOM 2521 N ILE A 21 -8.989 -11.354 36.036 1.00 34.36 N ANISOU 2521 N ILE A 21 5269 4268 3519 143 -393 -304 N ATOM 2522 CA ILE A 21 -9.842 -10.478 36.842 1.00 33.73 C ANISOU 2522 CA ILE A 21 5088 4239 3488 38 -328 -246 C ATOM 2523 C ILE A 21 -11.104 -10.136 36.074 1.00 33.43 C ANISOU 2523 C ILE A 21 5005 4226 3472 -30 -337 -229 C ATOM 2524 O ILE A 21 -11.027 -9.689 34.932 1.00 33.54 O ANISOU 2524 O ILE A 21 4994 4278 3473 25 -330 -256 O ATOM 2525 CB ILE A 21 -9.139 -9.146 37.180 1.00 33.11 C ANISOU 2525 CB ILE A 21 4901 4256 3423 85 -227 -241 C ATOM 2526 CG1 ILE A 21 -7.795 -9.398 37.879 1.00 33.11 C ANISOU 2526 CG1 ILE A 21 4933 4248 3398 157 -216 -256 C ATOM 2527 CG2 ILE A 21 -10.057 -8.259 38.029 1.00 32.78 C ANISOU 2527 CG2 ILE A 21 4766 4262 3427 -7 -169 -195 C ATOM 2528 CD1 ILE A 21 -6.925 -8.166 38.005 1.00 32.46 C ANISOU 2528 CD1 ILE A 21 4757 4256 3320 209 -135 -252 C ATOM 2529 N SER A 22 -12.256 -10.316 36.712 1.00 33.40 N ANISOU 2529 N SER A 22 4980 4214 3496 -151 -350 -180 N ATOM 2530 CA SER A 22 -13.549 -9.980 36.102 1.00 33.55 C ANISOU 2530 CA SER A 22 4941 4270 3538 -224 -359 -156 C ATOM 2531 C SER A 22 -13.959 -8.543 36.461 1.00 32.67 C ANISOU 2531 C SER A 22 4688 4264 3462 -231 -262 -134 C ATOM 2532 O SER A 22 -13.645 -8.065 37.552 1.00 32.55 O ANISOU 2532 O SER A 22 4630 4281 3458 -232 -202 -120 O ATOM 2533 CB SER A 22 -14.620 -10.980 36.545 1.00 34.43 C ANISOU 2533 CB SER A 22 5097 4332 3653 -356 -434 -108 C ATOM 2534 OG SER A 22 -15.922 -10.465 36.337 1.00 34.85 O ANISOU 2534 OG SER A 22 5053 4456 3731 -439 -419 -69 O ATOM 2535 N CYS A 23 -14.630 -7.862 35.530 1.00 32.16 N ANISOU 2535 N CYS A 23 4561 4246 3413 -229 -253 -134 N ATOM 2536 CA CYS A 23 -15.233 -6.547 35.774 1.00 31.56 C ANISOU 2536 CA CYS A 23 4359 4256 3374 -236 -183 -115 C ATOM 2537 C CYS A 23 -16.631 -6.516 35.170 1.00 32.05 C ANISOU 2537 C CYS A 23 4371 4352 3453 -305 -215 -89 C ATOM 2538 O CYS A 23 -16.794 -6.625 33.950 1.00 32.03 O ANISOU 2538 O CYS A 23 4393 4336 3442 -287 -258 -104 O ATOM 2539 CB CYS A 23 -14.382 -5.418 35.192 1.00 30.91 C ANISOU 2539 CB CYS A 23 4240 4207 3297 -139 -135 -140 C ATOM 2540 SG CYS A 23 -15.141 -3.774 35.320 1.00 30.70 S ANISOU 2540 SG CYS A 23 4083 4262 3320 -135 -74 -123 S ATOM 2541 N ARG A 24 -17.629 -6.369 36.037 1.00 32.36 N ANISOU 2541 N ARG A 24 4336 4448 3511 -381 -193 -50 N ATOM 2542 CA ARG A 24 -19.026 -6.434 35.648 1.00 33.02 C ANISOU 2542 CA ARG A 24 4357 4582 3607 -459 -224 -16 C ATOM 2543 C ARG A 24 -19.655 -5.050 35.776 1.00 32.96 C ANISOU 2543 C ARG A 24 4218 4674 3634 -422 -158 -14 C ATOM 2544 O ARG A 24 -19.605 -4.446 36.853 1.00 32.90 O ANISOU 2544 O ARG A 24 4152 4716 3634 -405 -94 -14 O ATOM 2545 CB ARG A 24 -19.752 -7.436 36.544 1.00 33.82 C ANISOU 2545 CB ARG A 24 4466 4690 3693 -582 -259 36 C ATOM 2546 CG ARG A 24 -21.120 -7.863 36.046 1.00 34.72 C ANISOU 2546 CG ARG A 24 4538 4845 3809 -687 -318 82 C ATOM 2547 CD ARG A 24 -21.007 -8.887 34.931 1.00 35.31 C ANISOU 2547 CD ARG A 24 4735 4815 3867 -712 -424 70 C ATOM 2548 NE ARG A 24 -22.296 -9.066 34.269 1.00 36.11 N ANISOU 2548 NE ARG A 24 4784 4961 3974 -801 -480 109 N ATOM 2549 CZ ARG A 24 -23.270 -9.880 34.685 1.00 37.21 C ANISOU 2549 CZ ARG A 24 4910 5124 4103 -945 -539 177 C ATOM 2550 NH1 ARG A 24 -23.125 -10.630 35.779 1.00 37.49 N ANISOU 2550 NH1 ARG A 24 4987 5137 4121 -1023 -551 217 N ATOM 2551 NH2 ARG A 24 -24.411 -9.946 33.998 1.00 38.02 N ANISOU 2551 NH2 ARG A 24 4956 5279 4212 -1022 -590 213 N ATOM 2552 N SER A 25 -20.234 -4.549 34.685 1.00 33.21 N ANISOU 2552 N SER A 25 4207 4729 3681 -404 -179 -16 N ATOM 2553 CA SER A 25 -20.951 -3.269 34.706 1.00 33.48 C ANISOU 2553 CA SER A 25 4122 4849 3750 -364 -135 -15 C ATOM 2554 C SER A 25 -22.447 -3.506 34.935 1.00 34.50 C ANISOU 2554 C SER A 25 4157 5068 3882 -449 -151 28 C ATOM 2555 O SER A 25 -22.949 -4.590 34.658 1.00 35.14 O ANISOU 2555 O SER A 25 4274 5134 3944 -545 -214 60 O ATOM 2556 CB SER A 25 -20.704 -2.468 33.420 1.00 33.25 C ANISOU 2556 CB SER A 25 4095 4803 3737 -291 -149 -34 C ATOM 2557 OG SER A 25 -21.152 -3.151 32.260 1.00 33.54 O ANISOU 2557 OG SER A 25 4167 4818 3758 -333 -220 -23 O ATOM 2558 N SER A 26 -23.137 -2.494 35.461 1.00 34.93 N ANISOU 2558 N SER A 26 4093 5220 3958 -412 -100 27 N ATOM 2559 CA SER A 26 -24.579 -2.581 35.769 1.00 36.01 C ANISOU 2559 CA SER A 26 4113 5478 4092 -479 -103 68 C ATOM 2560 C SER A 26 -25.474 -2.372 34.541 1.00 36.95 C ANISOU 2560 C SER A 26 4184 5627 4230 -486 -155 83 C ATOM 2561 O SER A 26 -26.672 -2.658 34.581 1.00 37.47 O ANISOU 2561 O SER A 26 4158 5791 4288 -559 -176 126 O ATOM 2562 CB SER A 26 -24.956 -1.573 36.857 1.00 35.88 C ANISOU 2562 CB SER A 26 3984 5567 4081 -414 -27 49 C ATOM 2563 OG SER A 26 -24.534 -0.267 36.515 1.00 35.31 O ANISOU 2563 OG SER A 26 3904 5467 4045 -288 -3 1 O ATOM 2564 N GLN A 27 -24.887 -1.858 33.464 1.00 37.18 N ANISOU 2564 N GLN A 27 4266 5581 4278 -414 -177 54 N ATOM 2565 CA GLN A 27 -25.577 -1.686 32.189 1.00 37.79 C ANISOU 2565 CA GLN A 27 4318 5672 4369 -418 -234 68 C ATOM 2566 C GLN A 27 -24.535 -1.666 31.073 1.00 37.45 C ANISOU 2566 C GLN A 27 4386 5522 4319 -370 -265 41 C ATOM 2567 O GLN A 27 -23.332 -1.699 31.345 1.00 36.96 O ANISOU 2567 O GLN A 27 4405 5392 4247 -328 -237 13 O ATOM 2568 CB GLN A 27 -26.378 -0.382 32.200 1.00 38.20 C ANISOU 2568 CB GLN A 27 4244 5815 4457 -340 -206 62 C ATOM 2569 CG GLN A 27 -25.521 0.869 32.329 1.00 37.76 C ANISOU 2569 CG GLN A 27 4205 5714 4429 -217 -163 18 C ATOM 2570 CD GLN A 27 -26.335 2.129 32.488 1.00 38.43 C ANISOU 2570 CD GLN A 27 4176 5875 4549 -131 -146 6 C ATOM 2571 OE1 GLN A 27 -26.693 2.517 33.601 1.00 39.18 O ANISOU 2571 OE1 GLN A 27 4199 6044 4644 -97 -96 -11 O ATOM 2572 NE2 GLN A 27 -26.614 2.792 31.376 1.00 38.80 N ANISOU 2572 NE2 GLN A 27 4211 5908 4622 -87 -191 11 N ATOM 2573 N HIS A 27A -24.996 -1.595 29.828 1.00 38.00 N ANISOU 2573 N HIS A 27A 4454 5593 4392 -374 -322 51 N ATOM 2574 CA HIS A 27A -24.096 -1.563 28.677 1.00 37.81 C ANISOU 2574 CA HIS A 27A 4523 5494 4348 -329 -352 30 C ATOM 2575 C HIS A 27A -23.223 -0.312 28.714 1.00 36.73 C ANISOU 2575 C HIS A 27A 4381 5342 4234 -225 -302 9 C ATOM 2576 O HIS A 27A -23.637 0.727 29.228 1.00 36.95 O ANISOU 2576 O HIS A 27A 4324 5413 4300 -179 -267 11 O ATOM 2577 CB HIS A 27A -24.878 -1.628 27.359 1.00 38.86 C ANISOU 2577 CB HIS A 27A 4643 5647 4476 -355 -424 48 C ATOM 2578 CG HIS A 27A -25.564 -2.939 27.131 1.00 40.27 C ANISOU 2578 CG HIS A 27A 4855 5818 4626 -465 -495 68 C ATOM 2579 ND1 HIS A 27A -24.892 -4.142 27.163 1.00 40.86 N ANISOU 2579 ND1 HIS A 27A 5053 5811 4660 -506 -529 49 N ATOM 2580 CD2 HIS A 27A -26.859 -3.239 26.870 1.00 41.58 C ANISOU 2580 CD2 HIS A 27A 4953 6048 4799 -546 -547 108 C ATOM 2581 CE1 HIS A 27A -25.742 -5.128 26.937 1.00 41.79 C ANISOU 2581 CE1 HIS A 27A 5188 5928 4763 -613 -606 77 C ATOM 2582 NE2 HIS A 27A -26.943 -4.607 26.753 1.00 42.36 N ANISOU 2582 NE2 HIS A 27A 5139 6093 4862 -646 -617 116 N ATOM 2583 N ILE A 27B -22.007 -0.431 28.190 1.00 35.85 N ANISOU 2583 N ILE A 27B 4360 5170 4092 -189 -302 -11 N ATOM 2584 CA ILE A 27B -21.065 0.685 28.154 1.00 34.96 C ANISOU 2584 CA ILE A 27B 4249 5041 3992 -110 -265 -18 C ATOM 2585 C ILE A 27B -20.536 0.936 26.740 1.00 34.76 C ANISOU 2585 C ILE A 27B 4265 5006 3936 -81 -301 -10 C ATOM 2586 O ILE A 27B -19.345 1.197 26.547 1.00 34.24 O ANISOU 2586 O ILE A 27B 4245 4921 3846 -40 -281 -16 O ATOM 2587 CB ILE A 27B -19.926 0.502 29.190 1.00 34.27 C ANISOU 2587 CB ILE A 27B 4209 4919 3895 -90 -213 -40 C ATOM 2588 CG1 ILE A 27B -19.174 -0.819 28.992 1.00 34.10 C ANISOU 2588 CG1 ILE A 27B 4285 4854 3819 -114 -232 -59 C ATOM 2589 CG2 ILE A 27B -20.501 0.557 30.595 1.00 34.33 C ANISOU 2589 CG2 ILE A 27B 4159 4953 3931 -109 -172 -43 C ATOM 2590 CD1 ILE A 27B -17.802 -0.825 29.632 1.00 33.51 C ANISOU 2590 CD1 ILE A 27B 4259 4748 3726 -72 -189 -79 C ATOM 2591 N VAL A 27C -21.437 0.871 25.755 1.00 35.21 N ANISOU 2591 N VAL A 27C 4300 5090 3990 -105 -356 8 N ATOM 2592 CA VAL A 27C -21.109 1.261 24.380 1.00 35.05 C ANISOU 2592 CA VAL A 27C 4304 5076 3938 -78 -393 23 C ATOM 2593 C VAL A 27C -21.433 2.743 24.226 1.00 34.68 C ANISOU 2593 C VAL A 27C 4187 5049 3942 -37 -392 55 C ATOM 2594 O VAL A 27C -22.593 3.136 24.269 1.00 34.93 O ANISOU 2594 O VAL A 27C 4147 5109 4015 -44 -414 70 O ATOM 2595 CB VAL A 27C -21.867 0.434 23.312 1.00 35.73 C ANISOU 2595 CB VAL A 27C 4412 5176 3987 -125 -463 24 C ATOM 2596 CG1 VAL A 27C -21.436 0.857 21.912 1.00 36.01 C ANISOU 2596 CG1 VAL A 27C 4474 5231 3977 -93 -495 39 C ATOM 2597 CG2 VAL A 27C -21.628 -1.060 23.504 1.00 35.90 C ANISOU 2597 CG2 VAL A 27C 4518 5159 3963 -167 -482 -11 C ATOM 2598 N HIS A 27D -20.387 3.550 24.058 1.00 34.32 N ANISOU 2598 N HIS A 27D 4163 4988 3889 5 -373 69 N ATOM 2599 CA HIS A 27D -20.492 5.003 23.818 1.00 34.48 C ANISOU 2599 CA HIS A 27D 4143 5006 3953 42 -390 107 C ATOM 2600 C HIS A 27D -21.327 5.233 22.541 1.00 35.00 C ANISOU 2600 C HIS A 27D 4185 5103 4012 32 -455 140 C ATOM 2601 O HIS A 27D -21.382 4.357 21.678 1.00 35.17 O ANISOU 2601 O HIS A 27D 4240 5147 3976 1 -482 135 O ATOM 2602 CB HIS A 27D -19.058 5.557 23.693 1.00 34.24 C ANISOU 2602 CB HIS A 27D 4155 4960 3896 62 -370 127 C ATOM 2603 CG HIS A 27D -18.938 7.046 23.782 1.00 34.46 C ANISOU 2603 CG HIS A 27D 4160 4959 3975 92 -389 166 C ATOM 2604 ND1 HIS A 27D -19.165 7.872 22.709 1.00 34.94 N ANISOU 2604 ND1 HIS A 27D 4211 5027 4037 94 -447 219 N ATOM 2605 CD2 HIS A 27D -18.535 7.852 24.791 1.00 34.57 C ANISOU 2605 CD2 HIS A 27D 4171 4929 4035 118 -369 161 C ATOM 2606 CE1 HIS A 27D -18.946 9.126 23.054 1.00 35.25 C ANISOU 2606 CE1 HIS A 27D 4246 5021 4127 118 -468 247 C ATOM 2607 NE2 HIS A 27D -18.561 9.143 24.316 1.00 35.18 N ANISOU 2607 NE2 HIS A 27D 4243 4979 4145 135 -421 209 N ATOM 2608 N SER A 27E -21.990 6.378 22.411 1.00 35.31 N ANISOU 2608 N SER A 27E 4172 5139 4105 63 -488 169 N ATOM 2609 CA SER A 27E -22.862 6.610 21.238 1.00 36.19 C ANISOU 2609 CA SER A 27E 4256 5281 4213 54 -556 204 C ATOM 2610 C SER A 27E -22.111 6.646 19.880 1.00 36.24 C ANISOU 2610 C SER A 27E 4315 5304 4150 38 -589 243 C ATOM 2611 O SER A 27E -22.711 6.396 18.834 1.00 36.75 O ANISOU 2611 O SER A 27E 4374 5403 4184 17 -640 261 O ATOM 2612 CB SER A 27E -23.731 7.855 21.431 1.00 36.83 C ANISOU 2612 CB SER A 27E 4272 5352 4369 104 -591 224 C ATOM 2613 OG SER A 27E -22.942 8.987 21.721 1.00 37.12 O ANISOU 2613 OG SER A 27E 4334 5335 4435 144 -591 245 O ATOM 2614 N ASN A 28 -20.812 6.953 19.912 1.00 35.54 N ANISOU 2614 N ASN A 28 4270 5202 4030 46 -559 258 N ATOM 2615 CA ASN A 28 -19.887 6.731 18.787 1.00 35.56 C ANISOU 2615 CA ASN A 28 4318 5249 3943 30 -569 286 C ATOM 2616 C ASN A 28 -19.508 5.258 18.491 1.00 35.72 C ANISOU 2616 C ASN A 28 4388 5302 3880 16 -548 234 C ATOM 2617 O ASN A 28 -18.670 5.008 17.622 1.00 35.56 O ANISOU 2617 O ASN A 28 4404 5334 3775 19 -549 245 O ATOM 2618 CB ASN A 28 -18.613 7.600 18.946 1.00 35.06 C ANISOU 2618 CB ASN A 28 4272 5179 3871 37 -548 329 C ATOM 2619 CG ASN A 28 -17.615 7.053 19.969 1.00 34.17 C ANISOU 2619 CG ASN A 28 4185 5054 3746 45 -478 287 C ATOM 2620 OD1 ASN A 28 -17.795 5.987 20.548 1.00 33.75 O ANISOU 2620 OD1 ASN A 28 4145 4992 3686 48 -445 225 O ATOM 2621 ND2 ASN A 28 -16.549 7.802 20.190 1.00 33.95 N ANISOU 2621 ND2 ASN A 28 4163 5022 3713 43 -463 327 N ATOM 2622 N GLU A 29 -20.093 4.311 19.235 1.00 35.90 N ANISOU 2622 N GLU A 29 4415 5300 3927 4 -533 179 N ATOM 2623 CA GLU A 29 -19.969 2.854 19.019 1.00 36.20 C ANISOU 2623 CA GLU A 29 4512 5345 3899 -11 -536 126 C ATOM 2624 C GLU A 29 -18.656 2.214 19.492 1.00 35.50 C ANISOU 2624 C GLU A 29 4479 5249 3760 15 -484 88 C ATOM 2625 O GLU A 29 -18.414 1.038 19.217 1.00 35.49 O ANISOU 2625 O GLU A 29 4541 5247 3696 18 -496 39 O ATOM 2626 CB GLU A 29 -20.269 2.458 17.564 1.00 37.51 C ANISOU 2626 CB GLU A 29 4706 5555 3992 -23 -597 131 C ATOM 2627 CG GLU A 29 -21.574 3.031 17.022 1.00 38.53 C ANISOU 2627 CG GLU A 29 4778 5696 4165 -48 -656 171 C ATOM 2628 CD GLU A 29 -22.054 2.333 15.769 1.00 39.67 C ANISOU 2628 CD GLU A 29 4957 5876 4239 -72 -723 162 C ATOM 2629 OE1 GLU A 29 -21.259 1.595 15.151 1.00 40.71 O ANISOU 2629 OE1 GLU A 29 5160 6030 4278 -55 -724 128 O ATOM 2630 OE2 GLU A 29 -23.233 2.524 15.397 1.00 40.55 O ANISOU 2630 OE2 GLU A 29 5024 5997 4385 -102 -777 186 O ATOM 2631 N ASN A 30 -17.820 2.974 20.201 1.00 34.89 N ANISOU 2631 N ASN A 30 4383 5164 3710 37 -435 108 N ATOM 2632 CA ASN A 30 -16.694 2.406 20.949 1.00 34.34 C ANISOU 2632 CA ASN A 30 4352 5084 3611 60 -383 72 C ATOM 2633 C ASN A 30 -17.120 2.080 22.374 1.00 33.32 C ANISOU 2633 C ASN A 30 4215 4895 3551 45 -354 42 C ATOM 2634 O ASN A 30 -18.039 2.695 22.916 1.00 33.06 O ANISOU 2634 O ASN A 30 4128 4842 3591 28 -358 58 O ATOM 2635 CB ASN A 30 -15.525 3.380 20.995 1.00 34.35 C ANISOU 2635 CB ASN A 30 4334 5115 3601 80 -350 116 C ATOM 2636 CG ASN A 30 -14.946 3.639 19.635 1.00 35.11 C ANISOU 2636 CG ASN A 30 4434 5294 3613 89 -371 155 C ATOM 2637 OD1 ASN A 30 -14.508 2.716 18.958 1.00 35.51 O ANISOU 2637 OD1 ASN A 30 4524 5393 3573 115 -373 119 O ATOM 2638 ND2 ASN A 30 -14.942 4.899 19.221 1.00 35.69 N ANISOU 2638 ND2 ASN A 30 4467 5384 3709 70 -392 229 N ATOM 2639 N THR A 31 -16.429 1.110 22.962 1.00 32.57 N ANISOU 2639 N THR A 31 4171 4781 3424 57 -327 -2 N ATOM 2640 CA THR A 31 -16.649 0.693 24.332 1.00 32.15 C ANISOU 2640 CA THR A 31 4118 4680 3419 39 -298 -27 C ATOM 2641 C THR A 31 -15.390 1.059 25.102 1.00 31.60 C ANISOU 2641 C THR A 31 4053 4607 3346 72 -243 -27 C ATOM 2642 O THR A 31 -14.384 0.351 25.040 1.00 31.27 O ANISOU 2642 O THR A 31 4061 4574 3245 102 -230 -54 O ATOM 2643 CB THR A 31 -16.936 -0.821 24.413 1.00 32.49 C ANISOU 2643 CB THR A 31 4227 4688 3428 15 -328 -73 C ATOM 2644 OG1 THR A 31 -18.063 -1.134 23.583 1.00 32.96 O ANISOU 2644 OG1 THR A 31 4284 4755 3485 -24 -389 -67 O ATOM 2645 CG2 THR A 31 -17.220 -1.270 25.861 1.00 32.32 C ANISOU 2645 CG2 THR A 31 4203 4624 3452 -19 -302 -85 C ATOM 2646 N TYR A 32 -15.459 2.163 25.844 1.00 31.51 N ANISOU 2646 N TYR A 32 3991 4584 3397 71 -217 -1 N ATOM 2647 CA TYR A 32 -14.304 2.698 26.572 1.00 31.02 C ANISOU 2647 CA TYR A 32 3929 4519 3338 93 -175 8 C ATOM 2648 C TYR A 32 -14.084 2.010 27.925 1.00 30.83 C ANISOU 2648 C TYR A 32 3926 4458 3328 89 -138 -30 C ATOM 2649 O TYR A 32 -13.993 2.666 28.966 1.00 30.94 O ANISOU 2649 O TYR A 32 3916 4451 3388 90 -110 -26 O ATOM 2650 CB TYR A 32 -14.437 4.220 26.726 1.00 30.88 C ANISOU 2650 CB TYR A 32 3863 4491 3378 94 -181 51 C ATOM 2651 CG TYR A 32 -14.372 4.948 25.406 1.00 31.25 C ANISOU 2651 CG TYR A 32 3897 4574 3402 92 -220 102 C ATOM 2652 CD1 TYR A 32 -13.147 5.263 24.821 1.00 31.28 C ANISOU 2652 CD1 TYR A 32 3909 4625 3350 95 -216 141 C ATOM 2653 CD2 TYR A 32 -15.537 5.308 24.729 1.00 31.80 C ANISOU 2653 CD2 TYR A 32 3940 4643 3500 83 -265 119 C ATOM 2654 CE1 TYR A 32 -13.084 5.923 23.606 1.00 31.87 C ANISOU 2654 CE1 TYR A 32 3969 4744 3395 83 -254 198 C ATOM 2655 CE2 TYR A 32 -15.486 5.972 23.508 1.00 32.30 C ANISOU 2655 CE2 TYR A 32 3994 4740 3539 77 -307 172 C ATOM 2656 CZ TYR A 32 -14.256 6.275 22.948 1.00 32.36 C ANISOU 2656 CZ TYR A 32 4015 4794 3489 74 -301 214 C ATOM 2657 OH TYR A 32 -14.192 6.925 21.739 1.00 33.01 O ANISOU 2657 OH TYR A 32 4085 4920 3537 58 -344 276 O ATOM 2658 N LEU A 33 -13.983 0.684 27.905 1.00 30.92 N ANISOU 2658 N LEU A 33 3992 4460 3297 87 -146 -66 N ATOM 2659 CA LEU A 33 -13.532 -0.059 29.069 1.00 30.69 C ANISOU 2659 CA LEU A 33 3996 4397 3266 86 -119 -94 C ATOM 2660 C LEU A 33 -12.002 -0.046 29.090 1.00 30.41 C ANISOU 2660 C LEU A 33 3984 4386 3186 133 -93 -97 C ATOM 2661 O LEU A 33 -11.359 -0.428 28.107 1.00 30.64 O ANISOU 2661 O LEU A 33 4038 4452 3150 169 -108 -104 O ATOM 2662 CB LEU A 33 -14.027 -1.500 29.053 1.00 31.00 C ANISOU 2662 CB LEU A 33 4095 4402 3280 61 -155 -126 C ATOM 2663 CG LEU A 33 -13.782 -2.172 30.411 1.00 30.86 C ANISOU 2663 CG LEU A 33 4107 4344 3273 45 -133 -143 C ATOM 2664 CD1 LEU A 33 -15.049 -2.189 31.251 1.00 30.95 C ANISOU 2664 CD1 LEU A 33 4079 4346 3334 -21 -132 -129 C ATOM 2665 CD2 LEU A 33 -13.226 -3.568 30.222 1.00 31.42 C ANISOU 2665 CD2 LEU A 33 4273 4376 3289 63 -169 -179 C ATOM 2666 N GLU A 34 -11.442 0.380 30.218 1.00 29.89 N ANISOU 2666 N GLU A 34 3904 4307 3147 134 -55 -92 N ATOM 2667 CA GLU A 34 -10.002 0.483 30.399 1.00 30.14 C ANISOU 2667 CA GLU A 34 3942 4368 3141 170 -29 -87 C ATOM 2668 C GLU A 34 -9.581 -0.249 31.676 1.00 30.07 C ANISOU 2668 C GLU A 34 3968 4322 3135 174 -8 -115 C ATOM 2669 O GLU A 34 -10.356 -0.314 32.631 1.00 29.74 O ANISOU 2669 O GLU A 34 3923 4239 3138 138 0 -123 O ATOM 2670 CB GLU A 34 -9.601 1.960 30.472 1.00 30.18 C ANISOU 2670 CB GLU A 34 3894 4395 3177 161 -16 -40 C ATOM 2671 CG GLU A 34 -10.133 2.791 29.308 1.00 30.33 C ANISOU 2671 CG GLU A 34 3881 4440 3203 148 -47 -1 C ATOM 2672 CD GLU A 34 -9.697 4.244 29.338 1.00 30.35 C ANISOU 2672 CD GLU A 34 3847 4449 3237 131 -52 53 C ATOM 2673 OE1 GLU A 34 -9.314 4.757 30.410 1.00 29.81 O ANISOU 2673 OE1 GLU A 34 3775 4349 3204 124 -36 54 O ATOM 2674 OE2 GLU A 34 -9.750 4.888 28.264 1.00 30.88 O ANISOU 2674 OE2 GLU A 34 3893 4550 3289 121 -82 98 O ATOM 2675 N TRP A 35 -8.367 -0.804 31.668 1.00 30.24 N ANISOU 2675 N TRP A 35 4017 4369 3103 219 1 -128 N ATOM 2676 CA TRP A 35 -7.768 -1.471 32.825 1.00 30.22 C ANISOU 2676 CA TRP A 35 4049 4337 3097 230 16 -150 C ATOM 2677 C TRP A 35 -6.497 -0.721 33.225 1.00 30.17 C ANISOU 2677 C TRP A 35 4005 4378 3079 251 48 -124 C ATOM 2678 O TRP A 35 -5.668 -0.404 32.364 1.00 30.57 O ANISOU 2678 O TRP A 35 4028 4502 3084 283 50 -104 O ATOM 2679 CB TRP A 35 -7.407 -2.926 32.502 1.00 30.76 C ANISOU 2679 CB TRP A 35 4192 4388 3108 278 -15 -194 C ATOM 2680 CG TRP A 35 -8.588 -3.825 32.321 1.00 31.23 C ANISOU 2680 CG TRP A 35 4305 4384 3178 243 -60 -216 C ATOM 2681 CD1 TRP A 35 -9.213 -4.127 31.148 1.00 31.70 C ANISOU 2681 CD1 TRP A 35 4383 4446 3215 245 -100 -229 C ATOM 2682 CD2 TRP A 35 -9.291 -4.538 33.346 1.00 31.44 C ANISOU 2682 CD2 TRP A 35 4370 4339 3235 189 -76 -222 C ATOM 2683 NE1 TRP A 35 -10.260 -4.988 31.374 1.00 31.97 N ANISOU 2683 NE1 TRP A 35 4468 4411 3269 192 -144 -241 N ATOM 2684 CE2 TRP A 35 -10.333 -5.255 32.716 1.00 31.85 C ANISOU 2684 CE2 TRP A 35 4462 4353 3285 153 -130 -232 C ATOM 2685 CE3 TRP A 35 -9.144 -4.640 34.738 1.00 31.37 C ANISOU 2685 CE3 TRP A 35 4365 4302 3251 160 -53 -213 C ATOM 2686 CZ2 TRP A 35 -11.225 -6.068 33.428 1.00 32.12 C ANISOU 2686 CZ2 TRP A 35 4537 4327 3342 81 -164 -226 C ATOM 2687 CZ3 TRP A 35 -10.031 -5.450 35.447 1.00 31.63 C ANISOU 2687 CZ3 TRP A 35 4437 4278 3301 94 -81 -209 C ATOM 2688 CH2 TRP A 35 -11.059 -6.153 34.786 1.00 32.09 C ANISOU 2688 CH2 TRP A 35 4530 4303 3358 51 -137 -212 C ATOM 2689 N TYR A 36 -6.351 -0.463 34.526 1.00 29.51 N ANISOU 2689 N TYR A 36 3918 4263 3032 227 70 -122 N ATOM 2690 CA TYR A 36 -5.184 0.206 35.094 1.00 29.50 C ANISOU 2690 CA TYR A 36 3887 4297 3025 234 92 -97 C ATOM 2691 C TYR A 36 -4.555 -0.663 36.181 1.00 29.67 C ANISOU 2691 C TYR A 36 3947 4296 3030 254 101 -121 C ATOM 2692 O TYR A 36 -5.266 -1.394 36.874 1.00 29.64 O ANISOU 2692 O TYR A 36 3985 4233 3044 235 95 -146 O ATOM 2693 CB TYR A 36 -5.594 1.560 35.690 1.00 29.19 C ANISOU 2693 CB TYR A 36 3810 4234 3047 187 99 -70 C ATOM 2694 CG TYR A 36 -6.028 2.529 34.634 1.00 29.20 C ANISOU 2694 CG TYR A 36 3776 4254 3065 171 80 -37 C ATOM 2695 CD1 TYR A 36 -5.100 3.349 34.014 1.00 29.19 C ANISOU 2695 CD1 TYR A 36 3739 4309 3041 165 72 13 C ATOM 2696 CD2 TYR A 36 -7.365 2.600 34.214 1.00 29.07 C ANISOU 2696 CD2 TYR A 36 3758 4206 3081 156 65 -48 C ATOM 2697 CE1 TYR A 36 -5.477 4.227 33.014 1.00 29.36 C ANISOU 2697 CE1 TYR A 36 3734 4347 3074 144 46 54 C ATOM 2698 CE2 TYR A 36 -7.755 3.479 33.207 1.00 29.13 C ANISOU 2698 CE2 TYR A 36 3736 4228 3102 145 41 -14 C ATOM 2699 CZ TYR A 36 -6.798 4.290 32.611 1.00 29.29 C ANISOU 2699 CZ TYR A 36 3731 4297 3101 138 30 38 C ATOM 2700 OH TYR A 36 -7.133 5.169 31.610 1.00 29.43 O ANISOU 2700 OH TYR A 36 3725 4329 3129 119 -2 82 O ATOM 2701 N LEU A 37 -3.232 -0.570 36.325 1.00 29.80 N ANISOU 2701 N LEU A 37 3945 4368 3011 286 111 -107 N ATOM 2702 CA LEU A 37 -2.502 -1.203 37.430 1.00 29.87 C ANISOU 2702 CA LEU A 37 3981 4362 3006 305 117 -122 C ATOM 2703 C LEU A 37 -1.845 -0.126 38.285 1.00 29.65 C ANISOU 2703 C LEU A 37 3910 4353 3002 270 135 -87 C ATOM 2704 O LEU A 37 -1.025 0.636 37.779 1.00 29.76 O ANISOU 2704 O LEU A 37 3873 4437 2997 270 136 -49 O ATOM 2705 CB LEU A 37 -1.424 -2.162 36.899 1.00 30.37 C ANISOU 2705 CB LEU A 37 4059 4481 2998 389 106 -141 C ATOM 2706 CG LEU A 37 -0.400 -2.715 37.907 1.00 30.46 C ANISOU 2706 CG LEU A 37 4088 4498 2988 424 108 -149 C ATOM 2707 CD1 LEU A 37 -1.086 -3.361 39.105 1.00 30.30 C ANISOU 2707 CD1 LEU A 37 4133 4378 3004 388 97 -169 C ATOM 2708 CD2 LEU A 37 0.545 -3.693 37.220 1.00 31.06 C ANISOU 2708 CD2 LEU A 37 4177 4634 2989 528 91 -178 C ATOM 2709 N GLN A 38 -2.205 -0.072 39.570 1.00 29.75 N ANISOU 2709 N GLN A 38 3945 4308 3049 236 143 -99 N ATOM 2710 CA GLN A 38 -1.524 0.783 40.548 1.00 29.61 C ANISOU 2710 CA GLN A 38 3905 4298 3047 208 151 -78 C ATOM 2711 C GLN A 38 -0.519 -0.049 41.357 1.00 29.96 C ANISOU 2711 C GLN A 38 3971 4357 3055 239 151 -85 C ATOM 2712 O GLN A 38 -0.903 -0.823 42.235 1.00 29.94 O ANISOU 2712 O GLN A 38 4016 4305 3055 236 152 -110 O ATOM 2713 CB GLN A 38 -2.543 1.469 41.466 1.00 29.16 C ANISOU 2713 CB GLN A 38 3857 4181 3042 161 158 -92 C ATOM 2714 CG GLN A 38 -1.936 2.540 42.364 1.00 29.14 C ANISOU 2714 CG GLN A 38 3838 4176 3057 132 154 -76 C ATOM 2715 CD GLN A 38 -2.966 3.447 43.025 1.00 28.73 C ANISOU 2715 CD GLN A 38 3790 4074 3051 105 155 -98 C ATOM 2716 OE1 GLN A 38 -4.084 3.034 43.318 1.00 28.63 O ANISOU 2716 OE1 GLN A 38 3790 4038 3050 105 170 -128 O ATOM 2717 NE2 GLN A 38 -2.583 4.690 43.265 1.00 28.59 N ANISOU 2717 NE2 GLN A 38 3763 4044 3058 84 131 -82 N ATOM 2718 N LYS A 39 0.766 0.097 41.034 1.00 30.84 N ANISOU 2718 N LYS A 39 4043 4546 3128 267 148 -58 N ATOM 2719 CA LYS A 39 1.844 -0.523 41.818 1.00 31.29 C ANISOU 2719 CA LYS A 39 4107 4629 3151 301 145 -59 C ATOM 2720 C LYS A 39 1.995 0.249 43.126 1.00 31.26 C ANISOU 2720 C LYS A 39 4102 4596 3178 243 147 -46 C ATOM 2721 O LYS A 39 1.684 1.443 43.165 1.00 30.94 O ANISOU 2721 O LYS A 39 4039 4542 3174 189 145 -26 O ATOM 2722 CB LYS A 39 3.179 -0.473 41.073 1.00 32.03 C ANISOU 2722 CB LYS A 39 4140 4842 3190 347 143 -28 C ATOM 2723 CG LYS A 39 3.302 -1.372 39.852 1.00 32.76 C ANISOU 2723 CG LYS A 39 4234 4985 3230 431 140 -52 C ATOM 2724 CD LYS A 39 4.582 -1.021 39.097 1.00 33.75 C ANISOU 2724 CD LYS A 39 4270 5259 3293 466 147 -11 C ATOM 2725 CE LYS A 39 5.244 -2.216 38.427 1.00 34.89 C ANISOU 2725 CE LYS A 39 4418 5478 3361 589 142 -50 C ATOM 2726 NZ LYS A 39 4.480 -2.715 37.252 1.00 35.24 N ANISOU 2726 NZ LYS A 39 4497 5509 3385 632 136 -89 N ATOM 2727 N PRO A 40 2.487 -0.417 44.197 1.00 31.51 N ANISOU 2727 N PRO A 40 4164 4614 3194 257 143 -57 N ATOM 2728 CA PRO A 40 2.614 0.265 45.495 1.00 31.31 C ANISOU 2728 CA PRO A 40 4143 4562 3189 205 142 -50 C ATOM 2729 C PRO A 40 3.540 1.486 45.442 1.00 31.31 C ANISOU 2729 C PRO A 40 4087 4617 3192 168 129 -6 C ATOM 2730 O PRO A 40 4.650 1.399 44.919 1.00 31.51 O ANISOU 2730 O PRO A 40 4063 4728 3180 194 121 28 O ATOM 2731 CB PRO A 40 3.169 -0.824 46.431 1.00 31.40 C ANISOU 2731 CB PRO A 40 4195 4568 3169 237 134 -62 C ATOM 2732 CG PRO A 40 3.589 -1.954 45.564 1.00 31.84 C ANISOU 2732 CG PRO A 40 4258 4652 3186 316 123 -72 C ATOM 2733 CD PRO A 40 2.818 -1.851 44.290 1.00 31.77 C ANISOU 2733 CD PRO A 40 4241 4642 3189 323 131 -81 C ATOM 2734 N GLY A 41 3.049 2.616 45.952 1.00 31.15 N ANISOU 2734 N GLY A 41 4073 4549 3212 110 120 -6 N ATOM 2735 CA GLY A 41 3.795 3.871 45.964 1.00 31.48 C ANISOU 2735 CA GLY A 41 4080 4617 3264 58 89 39 C ATOM 2736 C GLY A 41 3.879 4.573 44.622 1.00 31.83 C ANISOU 2736 C GLY A 41 4077 4702 3315 40 75 83 C ATOM 2737 O GLY A 41 4.760 5.413 44.417 1.00 32.76 O ANISOU 2737 O GLY A 41 4154 4867 3427 -8 43 141 O ATOM 2738 N GLN A 42 2.967 4.239 43.709 1.00 31.30 N ANISOU 2738 N GLN A 42 4016 4619 3257 69 94 64 N ATOM 2739 CA GLN A 42 2.912 4.856 42.385 1.00 31.20 C ANISOU 2739 CA GLN A 42 3964 4645 3246 52 81 106 C ATOM 2740 C GLN A 42 1.482 5.192 42.019 1.00 30.45 C ANISOU 2740 C GLN A 42 3899 4471 3198 49 83 75 C ATOM 2741 O GLN A 42 0.530 4.705 42.632 1.00 30.22 O ANISOU 2741 O GLN A 42 3912 4381 3189 70 103 20 O ATOM 2742 CB GLN A 42 3.463 3.911 41.325 1.00 31.72 C ANISOU 2742 CB GLN A 42 3989 4809 3253 110 102 119 C ATOM 2743 CG GLN A 42 4.941 3.592 41.456 1.00 32.51 C ANISOU 2743 CG GLN A 42 4037 5018 3296 128 101 155 C ATOM 2744 CD GLN A 42 5.435 2.718 40.316 1.00 33.23 C ANISOU 2744 CD GLN A 42 4085 5219 3320 204 121 157 C ATOM 2745 OE1 GLN A 42 5.046 2.911 39.162 1.00 34.19 O ANISOU 2745 OE1 GLN A 42 4187 5373 3432 206 124 171 O ATOM 2746 NE2 GLN A 42 6.296 1.754 40.626 1.00 33.70 N ANISOU 2746 NE2 GLN A 42 4133 5342 3331 274 130 140 N ATOM 2747 N SER A 43 1.345 6.022 40.997 1.00 30.33 N ANISOU 2747 N SER A 43 3859 4470 3196 21 59 117 N ATOM 2748 CA SER A 43 0.042 6.330 40.431 1.00 30.09 C ANISOU 2748 CA SER A 43 3847 4381 3205 25 55 95 C ATOM 2749 C SER A 43 -0.384 5.187 39.498 1.00 29.54 C ANISOU 2749 C SER A 43 3771 4351 3103 76 87 74 C ATOM 2750 O SER A 43 0.466 4.411 39.049 1.00 29.33 O ANISOU 2750 O SER A 43 3720 4404 3019 109 102 87 O ATOM 2751 CB SER A 43 0.102 7.659 39.681 1.00 30.59 C ANISOU 2751 CB SER A 43 3892 4438 3293 -28 5 155 C ATOM 2752 OG SER A 43 1.036 7.591 38.625 1.00 31.36 O ANISOU 2752 OG SER A 43 3935 4642 3340 -43 2 222 O ATOM 2753 N PRO A 44 -1.695 5.074 39.202 1.00 29.19 N ANISOU 2753 N PRO A 44 3748 4254 3090 89 92 39 N ATOM 2754 CA PRO A 44 -2.161 4.059 38.250 1.00 29.11 C ANISOU 2754 CA PRO A 44 3739 4271 3050 128 108 21 C ATOM 2755 C PRO A 44 -1.477 4.160 36.887 1.00 29.37 C ANISOU 2755 C PRO A 44 3731 4391 3036 135 98 68 C ATOM 2756 O PRO A 44 -1.176 5.270 36.443 1.00 30.17 O ANISOU 2756 O PRO A 44 3801 4514 3148 92 72 124 O ATOM 2757 CB PRO A 44 -3.658 4.368 38.110 1.00 29.07 C ANISOU 2757 CB PRO A 44 3749 4202 3095 119 102 -5 C ATOM 2758 CG PRO A 44 -4.033 5.047 39.374 1.00 28.88 C ANISOU 2758 CG PRO A 44 3740 4118 3115 100 100 -27 C ATOM 2759 CD PRO A 44 -2.821 5.835 39.781 1.00 29.18 C ANISOU 2759 CD PRO A 44 3769 4170 3148 73 80 10 C ATOM 2760 N LYS A 45 -1.229 3.013 36.254 1.00 29.13 N ANISOU 2760 N LYS A 45 3704 4414 2950 190 114 46 N ATOM 2761 CA LYS A 45 -0.643 2.936 34.908 1.00 29.42 C ANISOU 2761 CA LYS A 45 3700 4555 2924 215 111 79 C ATOM 2762 C LYS A 45 -1.604 2.196 33.969 1.00 29.42 C ANISOU 2762 C LYS A 45 3730 4539 2910 250 107 40 C ATOM 2763 O LYS A 45 -2.200 1.185 34.347 1.00 29.30 O ANISOU 2763 O LYS A 45 3768 4464 2902 280 110 -17 O ATOM 2764 CB LYS A 45 0.704 2.211 34.943 1.00 29.49 C ANISOU 2764 CB LYS A 45 3683 4662 2860 269 127 80 C ATOM 2765 N LEU A 46 -1.752 2.715 32.752 1.00 29.76 N ANISOU 2765 N LEU A 46 3740 4636 2931 238 94 77 N ATOM 2766 CA LEU A 46 -2.634 2.121 31.738 1.00 29.55 C ANISOU 2766 CA LEU A 46 3739 4604 2886 267 84 46 C ATOM 2767 C LEU A 46 -2.035 0.843 31.153 1.00 29.73 C ANISOU 2767 C LEU A 46 3779 4694 2823 352 91 2 C ATOM 2768 O LEU A 46 -0.872 0.825 30.739 1.00 30.03 O ANISOU 2768 O LEU A 46 3772 4850 2790 389 104 25 O ATOM 2769 CB LEU A 46 -2.899 3.121 30.612 1.00 29.74 C ANISOU 2769 CB LEU A 46 3721 4672 2906 227 63 106 C ATOM 2770 CG LEU A 46 -3.799 2.699 29.445 1.00 29.85 C ANISOU 2770 CG LEU A 46 3754 4692 2898 247 46 85 C ATOM 2771 CD1 LEU A 46 -5.185 2.274 29.915 1.00 29.41 C ANISOU 2771 CD1 LEU A 46 3748 4520 2907 238 34 33 C ATOM 2772 CD2 LEU A 46 -3.899 3.840 28.439 1.00 30.12 C ANISOU 2772 CD2 LEU A 46 3742 4775 2927 199 22 159 C ATOM 2773 N LEU A 47 -2.843 -0.215 31.139 1.00 29.49 N ANISOU 2773 N LEU A 47 3815 4592 2797 384 76 -62 N ATOM 2774 CA LEU A 47 -2.504 -1.485 30.508 1.00 29.94 C ANISOU 2774 CA LEU A 47 3915 4684 2777 472 63 -118 C ATOM 2775 C LEU A 47 -3.298 -1.680 29.221 1.00 30.49 C ANISOU 2775 C LEU A 47 4002 4764 2818 482 37 -134 C ATOM 2776 O LEU A 47 -2.724 -1.960 28.166 1.00 31.05 O ANISOU 2776 O LEU A 47 4058 4937 2802 545 34 -144 O ATOM 2777 CB LEU A 47 -2.816 -2.640 31.456 1.00 29.76 C ANISOU 2777 CB LEU A 47 3975 4556 2778 494 46 -177 C ATOM 2778 CG LEU A 47 -2.157 -2.609 32.837 1.00 29.44 C ANISOU 2778 CG LEU A 47 3931 4490 2766 484 66 -169 C ATOM 2779 CD1 LEU A 47 -2.663 -3.785 33.660 1.00 29.32 C ANISOU 2779 CD1 LEU A 47 4005 4365 2772 491 38 -218 C ATOM 2780 CD2 LEU A 47 -0.634 -2.617 32.742 1.00 29.62 C ANISOU 2780 CD2 LEU A 47 3906 4628 2721 551 85 -157 C ATOM 2781 N ILE A 48 -4.622 -1.547 29.329 1.00 30.32 N ANISOU 2781 N ILE A 48 4008 4648 2864 421 16 -136 N ATOM 2782 CA ILE A 48 -5.545 -1.857 28.244 1.00 30.65 C ANISOU 2782 CA ILE A 48 4077 4680 2888 421 -18 -155 C ATOM 2783 C ILE A 48 -6.589 -0.749 28.087 1.00 30.44 C ANISOU 2783 C ILE A 48 4009 4625 2931 341 -23 -106 C ATOM 2784 O ILE A 48 -7.117 -0.235 29.082 1.00 29.66 O ANISOU 2784 O ILE A 48 3899 4460 2910 289 -13 -91 O ATOM 2785 CB ILE A 48 -6.219 -3.233 28.484 1.00 31.07 C ANISOU 2785 CB ILE A 48 4224 4637 2944 440 -59 -223 C ATOM 2786 CG1 ILE A 48 -5.131 -4.314 28.510 1.00 31.79 C ANISOU 2786 CG1 ILE A 48 4366 4753 2961 538 -68 -277 C ATOM 2787 CG2 ILE A 48 -7.285 -3.521 27.423 1.00 31.52 C ANISOU 2787 CG2 ILE A 48 4311 4674 2990 424 -104 -239 C ATOM 2788 CD1 ILE A 48 -5.620 -5.728 28.612 1.00 32.50 C ANISOU 2788 CD1 ILE A 48 4565 4742 3040 566 -127 -343 C ATOM 2789 N TYR A 49 -6.873 -0.392 26.831 1.00 30.73 N ANISOU 2789 N TYR A 49 4025 4718 2933 340 -42 -85 N ATOM 2790 CA TYR A 49 -7.923 0.579 26.493 1.00 30.71 C ANISOU 2790 CA TYR A 49 3990 4689 2989 277 -59 -41 C ATOM 2791 C TYR A 49 -8.862 0.005 25.439 1.00 30.89 C ANISOU 2791 C TYR A 49 4045 4707 2986 282 -101 -68 C ATOM 2792 O TYR A 49 -8.546 -0.985 24.765 1.00 30.99 O ANISOU 2792 O TYR A 49 4103 4751 2921 337 -118 -114 O ATOM 2793 CB TYR A 49 -7.333 1.919 26.033 1.00 30.96 C ANISOU 2793 CB TYR A 49 3956 4794 3015 250 -51 37 C ATOM 2794 CG TYR A 49 -6.553 1.856 24.745 1.00 31.82 C ANISOU 2794 CG TYR A 49 4040 5029 3020 285 -52 59 C ATOM 2795 CD1 TYR A 49 -5.232 1.407 24.726 1.00 32.19 C ANISOU 2795 CD1 TYR A 49 4073 5171 2986 341 -23 50 C ATOM 2796 CD2 TYR A 49 -7.133 2.256 23.537 1.00 32.44 C ANISOU 2796 CD2 TYR A 49 4105 5148 3074 267 -83 90 C ATOM 2797 CE1 TYR A 49 -4.515 1.344 23.537 1.00 33.04 C ANISOU 2797 CE1 TYR A 49 4147 5422 2984 380 -19 68 C ATOM 2798 CE2 TYR A 49 -6.421 2.198 22.344 1.00 33.33 C ANISOU 2798 CE2 TYR A 49 4191 5395 3078 298 -82 112 C ATOM 2799 CZ TYR A 49 -5.114 1.745 22.352 1.00 33.51 C ANISOU 2799 CZ TYR A 49 4195 5523 3016 357 -47 101 C ATOM 2800 OH TYR A 49 -4.414 1.690 21.171 1.00 35.14 O ANISOU 2800 OH TYR A 49 4363 5887 3103 395 -41 121 O ATOM 2801 N LYS A 50 -10.023 0.644 25.323 1.00 30.72 N ANISOU 2801 N LYS A 50 4001 4643 3028 229 -123 -41 N ATOM 2802 CA LYS A 50 -11.138 0.163 24.503 1.00 30.79 C ANISOU 2802 CA LYS A 50 4035 4633 3030 215 -170 -61 C ATOM 2803 C LYS A 50 -11.243 -1.369 24.483 1.00 30.89 C ANISOU 2803 C LYS A 50 4128 4609 3001 244 -197 -131 C ATOM 2804 O LYS A 50 -11.122 -2.005 23.430 1.00 31.11 O ANISOU 2804 O LYS A 50 4195 4672 2952 283 -229 -162 O ATOM 2805 CB LYS A 50 -11.062 0.752 23.087 1.00 31.35 C ANISOU 2805 CB LYS A 50 4078 4786 3048 221 -191 -21 C ATOM 2806 CG LYS A 50 -11.370 2.240 23.036 1.00 31.19 C ANISOU 2806 CG LYS A 50 3994 4769 3086 175 -193 53 C ATOM 2807 CD LYS A 50 -11.402 2.769 21.608 1.00 31.87 C ANISOU 2807 CD LYS A 50 4058 4933 3117 170 -224 101 C ATOM 2808 CE LYS A 50 -10.001 2.986 21.054 1.00 32.05 C ANISOU 2808 CE LYS A 50 4058 5069 3049 195 -199 136 C ATOM 2809 NZ LYS A 50 -10.037 3.513 19.667 1.00 32.67 N ANISOU 2809 NZ LYS A 50 4112 5238 3065 182 -229 191 N ATOM 2810 N VAL A 51 -11.417 -1.935 25.681 1.00 30.36 N ANISOU 2810 N VAL A 51 4090 4468 2978 226 -188 -156 N ATOM 2811 CA VAL A 51 -11.697 -3.362 25.912 1.00 30.41 C ANISOU 2811 CA VAL A 51 4181 4407 2965 231 -229 -212 C ATOM 2812 C VAL A 51 -10.489 -4.293 25.764 1.00 30.97 C ANISOU 2812 C VAL A 51 4317 4492 2956 316 -233 -264 C ATOM 2813 O VAL A 51 -10.189 -5.046 26.690 1.00 31.22 O ANISOU 2813 O VAL A 51 4399 4466 2998 325 -236 -291 O ATOM 2814 CB VAL A 51 -12.873 -3.901 25.051 1.00 30.63 C ANISOU 2814 CB VAL A 51 4243 4408 2986 195 -295 -226 C ATOM 2815 CG1 VAL A 51 -13.219 -5.329 25.459 1.00 30.95 C ANISOU 2815 CG1 VAL A 51 4380 4361 3019 178 -351 -272 C ATOM 2816 CG2 VAL A 51 -14.092 -2.987 25.158 1.00 30.33 C ANISOU 2816 CG2 VAL A 51 4131 4371 3024 122 -294 -176 C ATOM 2817 N SER A 52 -9.824 -4.267 24.611 1.00 31.65 N ANISOU 2817 N SER A 52 4403 4663 2959 383 -237 -278 N ATOM 2818 CA SER A 52 -8.808 -5.274 24.265 1.00 32.48 C ANISOU 2818 CA SER A 52 4575 4795 2973 485 -253 -343 C ATOM 2819 C SER A 52 -7.477 -4.740 23.702 1.00 33.11 C ANISOU 2819 C SER A 52 4593 5015 2971 563 -204 -330 C ATOM 2820 O SER A 52 -6.600 -5.537 23.358 1.00 33.39 O ANISOU 2820 O SER A 52 4671 5096 2921 666 -214 -388 O ATOM 2821 CB SER A 52 -9.425 -6.257 23.263 1.00 33.09 C ANISOU 2821 CB SER A 52 4739 4837 2996 510 -331 -402 C ATOM 2822 OG SER A 52 -9.984 -5.563 22.162 1.00 33.01 O ANISOU 2822 OG SER A 52 4683 4892 2968 482 -338 -370 O ATOM 2823 N ASN A 53 -7.305 -3.418 23.639 1.00 33.55 N ANISOU 2823 N ASN A 53 4551 5142 3053 516 -158 -252 N ATOM 2824 CA ASN A 53 -6.107 -2.825 23.034 1.00 34.53 C ANISOU 2824 CA ASN A 53 4606 5417 3097 564 -117 -219 C ATOM 2825 C ASN A 53 -5.023 -2.619 24.071 1.00 34.86 C ANISOU 2825 C ASN A 53 4610 5482 3151 581 -70 -201 C ATOM 2826 O ASN A 53 -5.176 -1.820 24.991 1.00 34.40 O ANISOU 2826 O ASN A 53 4515 5375 3179 508 -48 -150 O ATOM 2827 CB ASN A 53 -6.425 -1.495 22.369 1.00 34.50 C ANISOU 2827 CB ASN A 53 4524 5476 3109 494 -107 -133 C ATOM 2828 CG ASN A 53 -7.394 -1.649 21.232 1.00 34.81 C ANISOU 2828 CG ASN A 53 4590 5513 3122 483 -154 -145 C ATOM 2829 OD1 ASN A 53 -7.013 -2.045 20.134 1.00 35.53 O ANISOU 2829 OD1 ASN A 53 4691 5703 3107 546 -166 -171 O ATOM 2830 ND2 ASN A 53 -8.659 -1.351 21.488 1.00 34.52 N ANISOU 2830 ND2 ASN A 53 4563 5376 3178 408 -182 -128 N ATOM 2831 N ARG A 54 -3.930 -3.347 23.896 1.00 36.12 N ANISOU 2831 N ARG A 54 4781 5722 3220 684 -60 -247 N ATOM 2832 CA ARG A 54 -2.763 -3.266 24.758 1.00 36.63 C ANISOU 2832 CA ARG A 54 4805 5833 3278 715 -19 -233 C ATOM 2833 C ARG A 54 -2.010 -1.951 24.497 1.00 36.70 C ANISOU 2833 C ARG A 54 4697 5979 3267 668 24 -137 C ATOM 2834 O ARG A 54 -1.668 -1.649 23.360 1.00 37.48 O ANISOU 2834 O ARG A 54 4746 6214 3280 689 31 -110 O ATOM 2835 CB ARG A 54 -1.883 -4.481 24.466 1.00 37.87 C ANISOU 2835 CB ARG A 54 5007 6049 3333 856 -31 -318 C ATOM 2836 CG ARG A 54 -0.692 -4.689 25.371 1.00 38.62 C ANISOU 2836 CG ARG A 54 5074 6186 3414 911 -1 -322 C ATOM 2837 CD ARG A 54 -0.187 -6.134 25.334 1.00 40.13 C ANISOU 2837 CD ARG A 54 5350 6362 3534 1056 -37 -427 C ATOM 2838 NE ARG A 54 -0.200 -6.746 23.994 1.00 41.75 N ANISOU 2838 NE ARG A 54 5589 6642 3630 1157 -67 -492 N ATOM 2839 CZ ARG A 54 -1.130 -7.588 23.523 1.00 42.67 C ANISOU 2839 CZ ARG A 54 5821 6646 3747 1176 -134 -563 C ATOM 2840 NH1 ARG A 54 -2.184 -7.966 24.262 1.00 42.03 N ANISOU 2840 NH1 ARG A 54 5829 6373 3769 1092 -180 -571 N ATOM 2841 NH2 ARG A 54 -1.012 -8.056 22.277 1.00 43.82 N ANISOU 2841 NH2 ARG A 54 5990 6879 3779 1276 -160 -624 N ATOM 2842 N PHE A 55 -1.787 -1.169 25.552 1.00 36.18 N ANISOU 2842 N PHE A 55 4593 5874 3279 596 48 -81 N ATOM 2843 CA PHE A 55 -1.079 0.118 25.474 1.00 36.45 C ANISOU 2843 CA PHE A 55 4529 6012 3309 531 73 20 C ATOM 2844 C PHE A 55 0.428 -0.087 25.231 1.00 37.32 C ANISOU 2844 C PHE A 55 4570 6299 3311 603 105 32 C ATOM 2845 O PHE A 55 0.980 -1.113 25.618 1.00 37.08 O ANISOU 2845 O PHE A 55 4570 6275 3242 699 112 -38 O ATOM 2846 CB PHE A 55 -1.325 0.893 26.778 1.00 35.86 C ANISOU 2846 CB PHE A 55 4453 5823 3350 444 76 58 C ATOM 2847 CG PHE A 55 -0.734 2.274 26.804 1.00 36.10 C ANISOU 2847 CG PHE A 55 4404 5919 3393 360 82 162 C ATOM 2848 CD1 PHE A 55 -1.197 3.254 25.941 1.00 36.54 C ANISOU 2848 CD1 PHE A 55 4430 5999 3455 293 59 232 C ATOM 2849 CD2 PHE A 55 0.271 2.602 27.709 1.00 36.15 C ANISOU 2849 CD2 PHE A 55 4372 5957 3407 342 100 195 C ATOM 2850 CE1 PHE A 55 -0.661 4.533 25.964 1.00 36.75 C ANISOU 2850 CE1 PHE A 55 4396 6071 3497 206 47 335 C ATOM 2851 CE2 PHE A 55 0.810 3.881 27.741 1.00 36.44 C ANISOU 2851 CE2 PHE A 55 4344 6043 3458 252 90 297 C ATOM 2852 CZ PHE A 55 0.343 4.848 26.866 1.00 36.74 C ANISOU 2852 CZ PHE A 55 4361 6097 3504 181 60 368 C ATOM 2853 N SER A 56 1.081 0.887 24.589 1.00 38.27 N ANISOU 2853 N SER A 56 4594 6566 3379 554 120 126 N ATOM 2854 CA SER A 56 2.527 0.809 24.276 1.00 39.49 C ANISOU 2854 CA SER A 56 4656 6927 3419 610 154 156 C ATOM 2855 C SER A 56 3.378 0.522 25.511 1.00 39.36 C ANISOU 2855 C SER A 56 4630 6897 3429 636 172 141 C ATOM 2856 O SER A 56 3.144 1.102 26.573 1.00 39.25 O ANISOU 2856 O SER A 56 4633 6760 3519 551 164 172 O ATOM 2857 CB SER A 56 3.042 2.087 23.588 1.00 40.28 C ANISOU 2857 CB SER A 56 4650 7178 3479 511 159 288 C ATOM 2858 OG SER A 56 3.268 1.864 22.202 1.00 41.26 O ANISOU 2858 OG SER A 56 4728 7476 3472 566 168 292 O ATOM 2859 N GLY A 57 4.338 -0.392 25.369 1.00 39.76 N ANISOU 2859 N GLY A 57 4655 7073 3379 763 193 87 N ATOM 2860 CA GLY A 57 5.169 -0.829 26.489 1.00 39.80 C ANISOU 2860 CA GLY A 57 4653 7070 3398 809 206 63 C ATOM 2861 C GLY A 57 4.621 -2.002 27.291 1.00 39.17 C ANISOU 2861 C GLY A 57 4699 6811 3374 883 181 -47 C ATOM 2862 O GLY A 57 5.383 -2.673 27.974 1.00 39.70 O ANISOU 2862 O GLY A 57 4769 6893 3420 963 186 -87 O ATOM 2863 N VAL A 58 3.315 -2.262 27.205 1.00 38.52 N ANISOU 2863 N VAL A 58 4715 6563 3357 854 151 -91 N ATOM 2864 CA VAL A 58 2.663 -3.290 28.015 1.00 38.27 C ANISOU 2864 CA VAL A 58 4803 6351 3387 891 119 -176 C ATOM 2865 C VAL A 58 2.969 -4.671 27.417 1.00 39.21 C ANISOU 2865 C VAL A 58 4984 6502 3412 1050 93 -280 C ATOM 2866 O VAL A 58 2.729 -4.875 26.232 1.00 39.22 O ANISOU 2866 O VAL A 58 4991 6568 3341 1098 83 -308 O ATOM 2867 CB VAL A 58 1.126 -3.085 28.078 1.00 37.42 C ANISOU 2867 CB VAL A 58 4768 6075 3375 797 91 -179 C ATOM 2868 CG1 VAL A 58 0.455 -4.200 28.873 1.00 37.03 C ANISOU 2868 CG1 VAL A 58 4836 5856 3377 822 53 -255 C ATOM 2869 CG2 VAL A 58 0.780 -1.724 28.677 1.00 36.74 C ANISOU 2869 CG2 VAL A 58 4631 5948 3379 660 108 -91 C ATOM 2870 N PRO A 59 3.504 -5.617 28.228 1.00 39.89 N ANISOU 2870 N PRO A 59 5123 6540 3495 1136 76 -339 N ATOM 2871 CA PRO A 59 3.804 -6.957 27.695 1.00 41.02 C ANISOU 2871 CA PRO A 59 5341 6694 3550 1302 36 -446 C ATOM 2872 C PRO A 59 2.576 -7.718 27.193 1.00 41.17 C ANISOU 2872 C PRO A 59 5491 6563 3589 1306 -26 -515 C ATOM 2873 O PRO A 59 1.483 -7.553 27.738 1.00 40.41 O ANISOU 2873 O PRO A 59 5450 6308 3595 1188 -45 -493 O ATOM 2874 CB PRO A 59 4.420 -7.684 28.894 1.00 41.14 C ANISOU 2874 CB PRO A 59 5400 6639 3590 1360 18 -479 C ATOM 2875 CG PRO A 59 4.976 -6.606 29.751 1.00 40.35 C ANISOU 2875 CG PRO A 59 5195 6597 3540 1259 70 -382 C ATOM 2876 CD PRO A 59 4.026 -5.457 29.602 1.00 39.41 C ANISOU 2876 CD PRO A 59 5046 6434 3495 1100 89 -308 C ATOM 2877 N ASP A 60 2.771 -8.551 26.171 1.00 42.49 N ANISOU 2877 N ASP A 60 5704 6787 3652 1443 -59 -600 N ATOM 2878 CA ASP A 60 1.670 -9.322 25.563 1.00 42.86 C ANISOU 2878 CA ASP A 60 5880 6701 3704 1452 -131 -670 C ATOM 2879 C ASP A 60 1.028 -10.377 26.478 1.00 42.60 C ANISOU 2879 C ASP A 60 5998 6441 3748 1441 -208 -723 C ATOM 2880 O ASP A 60 -0.044 -10.897 26.156 1.00 42.59 O ANISOU 2880 O ASP A 60 6101 6306 3774 1402 -273 -758 O ATOM 2881 CB ASP A 60 2.098 -9.960 24.229 1.00 44.50 C ANISOU 2881 CB ASP A 60 6107 7031 3770 1613 -155 -757 C ATOM 2882 CG ASP A 60 3.161 -11.046 24.388 1.00 45.77 C ANISOU 2882 CG ASP A 60 6314 7229 3848 1807 -186 -853 C ATOM 2883 OD1 ASP A 60 3.654 -11.283 25.517 1.00 45.27 O ANISOU 2883 OD1 ASP A 60 6259 7107 3835 1815 -187 -844 O ATOM 2884 OD2 ASP A 60 3.502 -11.665 23.356 1.00 47.42 O ANISOU 2884 OD2 ASP A 60 6551 7530 3935 1961 -213 -942 O ATOM 2885 N ARG A 61 1.679 -10.702 27.597 1.00 42.27 N ANISOU 2885 N ARG A 61 5967 6359 3737 1468 -208 -722 N ATOM 2886 CA ARG A 61 1.051 -11.541 28.622 1.00 41.89 C ANISOU 2886 CA ARG A 61 6049 6099 3770 1423 -276 -743 C ATOM 2887 C ARG A 61 -0.238 -10.920 29.185 1.00 40.33 C ANISOU 2887 C ARG A 61 5850 5785 3687 1231 -267 -670 C ATOM 2888 O ARG A 61 -1.127 -11.645 29.629 1.00 40.29 O ANISOU 2888 O ARG A 61 5959 5614 3736 1173 -335 -687 O ATOM 2889 CB ARG A 61 2.038 -11.922 29.738 1.00 42.24 C ANISOU 2889 CB ARG A 61 6094 6134 3821 1485 -275 -746 C ATOM 2890 CG ARG A 61 2.656 -10.769 30.511 1.00 41.91 C ANISOU 2890 CG ARG A 61 5911 6196 3816 1408 -185 -654 C ATOM 2891 CD ARG A 61 3.114 -11.218 31.898 1.00 42.11 C ANISOU 2891 CD ARG A 61 5976 6137 3888 1410 -204 -647 C ATOM 2892 NE ARG A 61 3.576 -10.101 32.722 1.00 41.22 N ANISOU 2892 NE ARG A 61 5742 6100 3819 1318 -129 -559 N ATOM 2893 CZ ARG A 61 4.766 -9.507 32.614 1.00 41.92 C ANISOU 2893 CZ ARG A 61 5708 6368 3853 1371 -74 -529 C ATOM 2894 NH1 ARG A 61 5.667 -9.904 31.710 1.00 43.29 N ANISOU 2894 NH1 ARG A 61 5844 6686 3917 1526 -74 -579 N ATOM 2895 NH2 ARG A 61 5.064 -8.493 33.416 1.00 41.42 N ANISOU 2895 NH2 ARG A 61 5553 6345 3838 1268 -21 -447 N ATOM 2896 N PHE A 62 -0.334 -9.590 29.139 1.00 38.94 N ANISOU 2896 N PHE A 62 5549 5703 3542 1135 -188 -588 N ATOM 2897 CA PHE A 62 -1.567 -8.871 29.469 1.00 37.64 C ANISOU 2897 CA PHE A 62 5369 5459 3474 974 -176 -527 C ATOM 2898 C PHE A 62 -2.549 -8.871 28.304 1.00 37.59 C ANISOU 2898 C PHE A 62 5389 5441 3452 948 -207 -542 C ATOM 2899 O PHE A 62 -2.191 -8.504 27.187 1.00 38.23 O ANISOU 2899 O PHE A 62 5417 5648 3460 1003 -187 -548 O ATOM 2900 CB PHE A 62 -1.253 -7.434 29.865 1.00 36.82 C ANISOU 2900 CB PHE A 62 5134 5448 3409 894 -95 -440 C ATOM 2901 CG PHE A 62 -0.537 -7.320 31.177 1.00 36.56 C ANISOU 2901 CG PHE A 62 5078 5402 3411 884 -68 -414 C ATOM 2902 CD1 PHE A 62 -1.254 -7.295 32.369 1.00 35.85 C ANISOU 2902 CD1 PHE A 62 5023 5189 3408 785 -74 -389 C ATOM 2903 CD2 PHE A 62 0.851 -7.245 31.226 1.00 36.85 C ANISOU 2903 CD2 PHE A 62 5054 5563 3386 972 -39 -412 C ATOM 2904 CE1 PHE A 62 -0.599 -7.189 33.585 1.00 35.76 C ANISOU 2904 CE1 PHE A 62 4995 5170 3423 775 -52 -366 C ATOM 2905 CE2 PHE A 62 1.510 -7.138 32.439 1.00 36.54 C ANISOU 2905 CE2 PHE A 62 4993 5513 3377 959 -20 -387 C ATOM 2906 CZ PHE A 62 0.785 -7.111 33.620 1.00 35.99 C ANISOU 2906 CZ PHE A 62 4968 5310 3395 860 -28 -365 C ATOM 2907 N SER A 63 -3.792 -9.253 28.586 1.00 36.79 N ANISOU 2907 N SER A 63 5362 5201 3417 857 -257 -542 N ATOM 2908 CA SER A 63 -4.820 -9.427 27.560 1.00 36.72 C ANISOU 2908 CA SER A 63 5393 5161 3397 826 -304 -560 C ATOM 2909 C SER A 63 -6.198 -9.045 28.105 1.00 35.51 C ANISOU 2909 C SER A 63 5232 4916 3343 674 -310 -505 C ATOM 2910 O SER A 63 -6.563 -9.460 29.200 1.00 35.27 O ANISOU 2910 O SER A 63 5243 4786 3370 613 -329 -492 O ATOM 2911 CB SER A 63 -4.826 -10.887 27.093 1.00 37.93 C ANISOU 2911 CB SER A 63 5690 5230 3493 917 -402 -652 C ATOM 2912 OG SER A 63 -6.009 -11.202 26.379 1.00 38.36 O ANISOU 2912 OG SER A 63 5805 5213 3555 857 -467 -666 O ATOM 2913 N GLY A 64 -6.954 -8.272 27.326 1.00 34.64 N ANISOU 2913 N GLY A 64 5065 4850 3245 617 -296 -472 N ATOM 2914 CA GLY A 64 -8.284 -7.801 27.715 1.00 33.76 C ANISOU 2914 CA GLY A 64 4926 4680 3220 487 -298 -421 C ATOM 2915 C GLY A 64 -9.347 -8.268 26.737 1.00 33.90 C ANISOU 2915 C GLY A 64 4997 4659 3225 455 -368 -442 C ATOM 2916 O GLY A 64 -9.090 -8.366 25.539 1.00 34.63 O ANISOU 2916 O GLY A 64 5103 4809 3245 523 -388 -477 O ATOM 2917 N SER A 65 -10.543 -8.551 27.243 1.00 33.35 N ANISOU 2917 N SER A 65 4951 4503 3219 349 -406 -419 N ATOM 2918 CA SER A 65 -11.652 -9.004 26.405 1.00 33.55 C ANISOU 2918 CA SER A 65 5021 4487 3239 299 -481 -429 C ATOM 2919 C SER A 65 -13.002 -8.765 27.069 1.00 33.19 C ANISOU 2919 C SER A 65 4933 4401 3276 164 -488 -371 C ATOM 2920 O SER A 65 -13.072 -8.273 28.196 1.00 32.34 O ANISOU 2920 O SER A 65 4766 4298 3225 117 -433 -329 O ATOM 2921 CB SER A 65 -11.501 -10.494 26.100 1.00 34.33 C ANISOU 2921 CB SER A 65 5270 4491 3284 345 -583 -500 C ATOM 2922 OG SER A 65 -11.899 -11.278 27.204 1.00 34.25 O ANISOU 2922 OG SER A 65 5322 4370 3320 272 -627 -485 O ATOM 2923 N GLY A 66 -14.061 -9.117 26.343 1.00 33.76 N ANISOU 2923 N GLY A 66 5033 4447 3348 105 -557 -370 N ATOM 2924 CA GLY A 66 -15.421 -9.133 26.863 1.00 34.05 C ANISOU 2924 CA GLY A 66 5035 4455 3449 -25 -581 -317 C ATOM 2925 C GLY A 66 -16.355 -8.172 26.162 1.00 34.06 C ANISOU 2925 C GLY A 66 4938 4528 3477 -67 -565 -279 C ATOM 2926 O GLY A 66 -15.926 -7.329 25.383 1.00 33.85 O ANISOU 2926 O GLY A 66 4862 4572 3427 -3 -526 -282 O ATOM 2927 N SER A 67 -17.643 -8.306 26.458 1.00 34.70 N ANISOU 2927 N SER A 67 4986 4596 3603 -178 -600 -236 N ATOM 2928 CA SER A 67 -18.681 -7.481 25.844 1.00 34.93 C ANISOU 2928 CA SER A 67 4920 4692 3661 -220 -597 -198 C ATOM 2929 C SER A 67 -19.969 -7.501 26.662 1.00 35.35 C ANISOU 2929 C SER A 67 4903 4758 3772 -338 -606 -141 C ATOM 2930 O SER A 67 -20.123 -8.315 27.570 1.00 35.60 O ANISOU 2930 O SER A 67 4974 4740 3812 -403 -629 -129 O ATOM 2931 CB SER A 67 -18.962 -7.962 24.420 1.00 35.69 C ANISOU 2931 CB SER A 67 5080 4776 3704 -211 -681 -228 C ATOM 2932 OG SER A 67 -19.282 -9.341 24.408 1.00 36.67 O ANISOU 2932 OG SER A 67 5321 4807 3804 -266 -783 -250 O ATOM 2933 N GLY A 68 -20.889 -6.600 26.323 1.00 35.68 N ANISOU 2933 N GLY A 68 4836 4874 3848 -363 -589 -104 N ATOM 2934 CA GLY A 68 -22.133 -6.425 27.065 1.00 36.22 C ANISOU 2934 CA GLY A 68 4805 4990 3965 -458 -583 -50 C ATOM 2935 C GLY A 68 -21.863 -5.782 28.418 1.00 35.97 C ANISOU 2935 C GLY A 68 4703 4994 3970 -440 -491 -35 C ATOM 2936 O GLY A 68 -21.555 -4.586 28.502 1.00 35.67 O ANISOU 2936 O GLY A 68 4595 5001 3957 -367 -423 -38 O ATOM 2937 N THR A 69 -21.968 -6.582 29.475 1.00 36.33 N ANISOU 2937 N THR A 69 4774 5013 4016 -509 -498 -18 N ATOM 2938 CA THR A 69 -21.661 -6.133 30.832 1.00 35.81 C ANISOU 2938 CA THR A 69 4656 4979 3973 -496 -416 -8 C ATOM 2939 C THR A 69 -20.525 -6.938 31.467 1.00 35.77 C ANISOU 2939 C THR A 69 4760 4891 3940 -478 -417 -33 C ATOM 2940 O THR A 69 -20.262 -6.773 32.652 1.00 35.66 O ANISOU 2940 O THR A 69 4718 4893 3936 -481 -362 -23 O ATOM 2941 CB THR A 69 -22.903 -6.217 31.748 1.00 36.27 C ANISOU 2941 CB THR A 69 4614 5115 4051 -597 -408 47 C ATOM 2942 OG1 THR A 69 -23.230 -7.587 32.009 1.00 36.96 O ANISOU 2942 OG1 THR A 69 4777 5153 4114 -712 -485 78 O ATOM 2943 CG2 THR A 69 -24.105 -5.510 31.124 1.00 36.68 C ANISOU 2943 CG2 THR A 69 4551 5258 4127 -612 -416 72 C ATOM 2944 N ASP A 70 -19.833 -7.764 30.679 1.00 36.13 N ANISOU 2944 N ASP A 70 4928 4852 3946 -448 -480 -71 N ATOM 2945 CA ASP A 70 -18.930 -8.792 31.200 1.00 36.52 C ANISOU 2945 CA ASP A 70 5098 4813 3967 -438 -510 -94 C ATOM 2946 C ASP A 70 -17.543 -8.681 30.557 1.00 35.96 C ANISOU 2946 C ASP A 70 5093 4711 3860 -308 -495 -156 C ATOM 2947 O ASP A 70 -17.374 -9.030 29.393 1.00 36.82 O ANISOU 2947 O ASP A 70 5265 4793 3931 -267 -550 -192 O ATOM 2948 CB ASP A 70 -19.549 -10.172 30.929 1.00 37.80 C ANISOU 2948 CB ASP A 70 5360 4893 4107 -535 -630 -81 C ATOM 2949 CG ASP A 70 -18.986 -11.266 31.821 1.00 38.56 C ANISOU 2949 CG ASP A 70 5567 4898 4187 -564 -672 -81 C ATOM 2950 OD1 ASP A 70 -18.117 -10.994 32.675 1.00 38.43 O ANISOU 2950 OD1 ASP A 70 5543 4885 4173 -508 -605 -90 O ATOM 2951 OD2 ASP A 70 -19.433 -12.423 31.673 1.00 40.10 O ANISOU 2951 OD2 ASP A 70 5861 5008 4365 -648 -784 -66 O ATOM 2952 N PHE A 71 -16.560 -8.201 31.317 1.00 35.08 N ANISOU 2952 N PHE A 71 4963 4613 3752 -244 -422 -166 N ATOM 2953 CA PHE A 71 -15.220 -7.905 30.789 1.00 34.51 C ANISOU 2953 CA PHE A 71 4921 4547 3645 -124 -392 -212 C ATOM 2954 C PHE A 71 -14.137 -8.537 31.648 1.00 34.30 C ANISOU 2954 C PHE A 71 4964 4470 3598 -82 -386 -233 C ATOM 2955 O PHE A 71 -14.298 -8.647 32.852 1.00 33.94 O ANISOU 2955 O PHE A 71 4905 4412 3579 -137 -365 -204 O ATOM 2956 CB PHE A 71 -15.002 -6.392 30.698 1.00 33.82 C ANISOU 2956 CB PHE A 71 4722 4544 3584 -80 -308 -196 C ATOM 2957 CG PHE A 71 -16.091 -5.671 29.952 1.00 33.75 C ANISOU 2957 CG PHE A 71 4638 4585 3601 -115 -315 -170 C ATOM 2958 CD1 PHE A 71 -16.022 -5.515 28.570 1.00 34.01 C ANISOU 2958 CD1 PHE A 71 4684 4638 3601 -74 -345 -186 C ATOM 2959 CD2 PHE A 71 -17.205 -5.177 30.626 1.00 33.65 C ANISOU 2959 CD2 PHE A 71 4539 4607 3639 -185 -293 -131 C ATOM 2960 CE1 PHE A 71 -17.042 -4.865 27.875 1.00 34.07 C ANISOU 2960 CE1 PHE A 71 4624 4689 3633 -107 -359 -159 C ATOM 2961 CE2 PHE A 71 -18.223 -4.526 29.940 1.00 33.90 C ANISOU 2961 CE2 PHE A 71 4498 4688 3695 -208 -305 -109 C ATOM 2962 CZ PHE A 71 -18.144 -4.370 28.562 1.00 34.01 C ANISOU 2962 CZ PHE A 71 4530 4710 3683 -172 -340 -121 C ATOM 2963 N THR A 72 -13.034 -8.940 31.018 1.00 34.61 N ANISOU 2963 N THR A 72 5074 4491 3584 19 -405 -285 N ATOM 2964 CA THR A 72 -11.985 -9.711 31.691 1.00 34.92 C ANISOU 2964 CA THR A 72 5193 4477 3597 74 -418 -313 C ATOM 2965 C THR A 72 -10.583 -9.266 31.283 1.00 35.00 C ANISOU 2965 C THR A 72 5186 4549 3564 202 -370 -349 C ATOM 2966 O THR A 72 -10.308 -9.110 30.096 1.00 35.03 O ANISOU 2966 O THR A 72 5189 4598 3522 268 -378 -379 O ATOM 2967 CB THR A 72 -12.117 -11.213 31.362 1.00 35.68 C ANISOU 2967 CB THR A 72 5436 4464 3659 72 -534 -350 C ATOM 2968 OG1 THR A 72 -13.451 -11.642 31.638 1.00 35.87 O ANISOU 2968 OG1 THR A 72 5471 4441 3718 -64 -589 -305 O ATOM 2969 CG2 THR A 72 -11.135 -12.055 32.187 1.00 35.96 C ANISOU 2969 CG2 THR A 72 5558 4430 3673 124 -560 -374 C ATOM 2970 N LEU A 73 -9.716 -9.067 32.278 1.00 35.19 N ANISOU 2970 N LEU A 73 5191 4584 3595 230 -321 -341 N ATOM 2971 CA LEU A 73 -8.273 -8.906 32.075 1.00 35.66 C ANISOU 2971 CA LEU A 73 5243 4700 3606 347 -288 -371 C ATOM 2972 C LEU A 73 -7.587 -10.218 32.452 1.00 37.00 C ANISOU 2972 C LEU A 73 5529 4791 3739 409 -350 -416 C ATOM 2973 O LEU A 73 -7.871 -10.772 33.509 1.00 37.34 O ANISOU 2973 O LEU A 73 5617 4756 3813 348 -376 -396 O ATOM 2974 CB LEU A 73 -7.722 -7.765 32.945 1.00 34.83 C ANISOU 2974 CB LEU A 73 5039 4661 3535 336 -200 -330 C ATOM 2975 CG LEU A 73 -6.193 -7.578 33.035 1.00 34.70 C ANISOU 2975 CG LEU A 73 5001 4710 3475 434 -164 -345 C ATOM 2976 CD1 LEU A 73 -5.635 -7.021 31.735 1.00 34.84 C ANISOU 2976 CD1 LEU A 73 4968 4831 3438 504 -144 -354 C ATOM 2977 CD2 LEU A 73 -5.809 -6.682 34.203 1.00 33.89 C ANISOU 2977 CD2 LEU A 73 4827 4636 3414 396 -101 -302 C ATOM 2978 N LYS A 74 -6.679 -10.699 31.604 1.00 38.39 N ANISOU 2978 N LYS A 74 5750 4993 3843 535 -377 -476 N ATOM 2979 CA LYS A 74 -5.914 -11.918 31.876 1.00 39.79 C ANISOU 2979 CA LYS A 74 6040 5099 3979 625 -443 -530 C ATOM 2980 C LYS A 74 -4.423 -11.652 31.797 1.00 40.20 C ANISOU 2980 C LYS A 74 6044 5255 3975 758 -393 -557 C ATOM 2981 O LYS A 74 -3.963 -10.908 30.931 1.00 39.73 O ANISOU 2981 O LYS A 74 5900 5320 3874 811 -341 -560 O ATOM 2982 CB LYS A 74 -6.288 -13.022 30.889 1.00 41.16 C ANISOU 2982 CB LYS A 74 6340 5193 4106 672 -550 -596 C ATOM 2983 CG LYS A 74 -7.753 -13.394 30.975 1.00 41.72 C ANISOU 2983 CG LYS A 74 6462 5162 4228 529 -615 -563 C ATOM 2984 CD LYS A 74 -8.111 -14.633 30.177 1.00 43.19 C ANISOU 2984 CD LYS A 74 6799 5238 4372 562 -745 -626 C ATOM 2985 CE LYS A 74 -9.531 -15.080 30.496 1.00 43.75 C ANISOU 2985 CE LYS A 74 6919 5204 4498 396 -817 -575 C ATOM 2986 NZ LYS A 74 -10.323 -15.311 29.257 1.00 44.64 N ANISOU 2986 NZ LYS A 74 7075 5299 4586 379 -885 -605 N ATOM 2987 N ILE A 75 -3.681 -12.272 32.711 1.00 41.16 N ANISOU 2987 N ILE A 75 6215 5331 4094 804 -413 -569 N ATOM 2988 CA ILE A 75 -2.224 -12.225 32.721 1.00 42.22 C ANISOU 2988 CA ILE A 75 6310 5562 4171 939 -380 -597 C ATOM 2989 C ILE A 75 -1.773 -13.674 32.611 1.00 43.90 C ANISOU 2989 C ILE A 75 6665 5681 4332 1060 -482 -676 C ATOM 2990 O ILE A 75 -2.057 -14.472 33.502 1.00 44.76 O ANISOU 2990 O ILE A 75 6873 5655 4478 1017 -548 -670 O ATOM 2991 CB ILE A 75 -1.670 -11.575 34.010 1.00 41.73 C ANISOU 2991 CB ILE A 75 6172 5533 4152 892 -314 -538 C ATOM 2992 CG1 ILE A 75 -2.442 -10.292 34.350 1.00 40.68 C ANISOU 2992 CG1 ILE A 75 5937 5435 4086 753 -241 -464 C ATOM 2993 CG2 ILE A 75 -0.189 -11.251 33.844 1.00 41.95 C ANISOU 2993 CG2 ILE A 75 6121 5700 4117 1016 -267 -552 C ATOM 2994 CD1 ILE A 75 -2.190 -9.775 35.746 1.00 40.35 C ANISOU 2994 CD1 ILE A 75 5848 5389 4092 687 -195 -413 C ATOM 2995 N SER A 76 -1.090 -14.008 31.517 1.00 45.04 N ANISOU 2995 N SER A 76 6823 5900 4388 1212 -501 -750 N ATOM 2996 CA SER A 76 -0.794 -15.408 31.164 1.00 46.44 C ANISOU 2996 CA SER A 76 7155 5982 4510 1347 -616 -846 C ATOM 2997 C SER A 76 0.351 -16.036 31.968 1.00 47.30 C ANISOU 2997 C SER A 76 7299 6077 4595 1464 -640 -874 C ATOM 2998 O SER A 76 0.294 -17.228 32.292 1.00 48.39 O ANISOU 2998 O SER A 76 7591 6060 4733 1511 -754 -921 O ATOM 2999 CB SER A 76 -0.514 -15.535 29.663 1.00 47.05 C ANISOU 2999 CB SER A 76 7233 6155 4487 1482 -628 -925 C ATOM 3000 OG SER A 76 0.637 -14.799 29.292 1.00 46.83 O ANISOU 3000 OG SER A 76 7065 6336 4393 1584 -533 -924 O ATOM 3001 N ARG A 77 1.383 -15.242 32.265 1.00 46.98 N ANISOU 3001 N ARG A 77 7120 6195 4535 1510 -544 -843 N ATOM 3002 CA ARG A 77 2.524 -15.680 33.079 1.00 47.55 C ANISOU 3002 CA ARG A 77 7198 6281 4587 1615 -555 -858 C ATOM 3003 C ARG A 77 2.897 -14.569 34.066 1.00 46.89 C ANISOU 3003 C ARG A 77 6974 6286 4555 1513 -452 -763 C ATOM 3004 O ARG A 77 3.641 -13.650 33.721 1.00 47.06 O ANISOU 3004 O ARG A 77 6852 6489 4539 1543 -365 -737 O ATOM 3005 CB ARG A 77 3.715 -16.021 32.183 1.00 48.24 C ANISOU 3005 CB ARG A 77 7258 6511 4559 1837 -557 -944 C ATOM 3006 N VAL A 78 2.386 -14.669 35.294 1.00 46.29 N ANISOU 3006 N VAL A 78 6945 6086 4559 1388 -470 -708 N ATOM 3007 CA VAL A 78 2.493 -13.589 36.286 1.00 45.01 C ANISOU 3007 CA VAL A 78 6667 5982 4452 1269 -382 -621 C ATOM 3008 C VAL A 78 3.921 -13.453 36.835 1.00 45.22 C ANISOU 3008 C VAL A 78 6622 6118 4443 1367 -350 -616 C ATOM 3009 O VAL A 78 4.412 -14.359 37.511 1.00 46.23 O ANISOU 3009 O VAL A 78 6831 6170 4562 1438 -414 -641 O ATOM 3010 CB VAL A 78 1.502 -13.799 37.461 1.00 44.34 C ANISOU 3010 CB VAL A 78 6653 5745 4450 1113 -412 -568 C ATOM 3011 CG1 VAL A 78 1.701 -12.753 38.559 1.00 43.54 C ANISOU 3011 CG1 VAL A 78 6445 5704 4395 1013 -329 -492 C ATOM 3012 CG2 VAL A 78 0.058 -13.768 36.965 1.00 43.97 C ANISOU 3012 CG2 VAL A 78 6646 5620 4441 997 -432 -557 C ATOM 3013 N AGLU A 79 4.569 -12.329 36.529 0.50 44.75 N ANISOU 3013 N AGLU A 79 6410 6234 4360 1367 -259 -579 N ATOM 3014 N BGLU A 79 4.568 -12.327 36.536 0.50 44.70 N ANISOU 3014 N BGLU A 79 6403 6227 4354 1366 -259 -579 N ATOM 3015 CA AGLU A 79 5.889 -11.997 37.068 0.50 44.95 C ANISOU 3015 CA AGLU A 79 6340 6385 4354 1430 -221 -556 C ATOM 3016 CA BGLU A 79 5.889 -12.007 37.072 0.50 44.87 C ANISOU 3016 CA BGLU A 79 6330 6373 4344 1430 -222 -556 C ATOM 3017 C AGLU A 79 5.716 -11.199 38.354 0.50 44.00 C ANISOU 3017 C AGLU A 79 6175 6233 4309 1280 -179 -475 C ATOM 3018 C BGLU A 79 5.717 -11.197 38.352 0.50 43.95 C ANISOU 3018 C BGLU A 79 6168 6227 4303 1281 -179 -475 C ATOM 3019 O AGLU A 79 4.613 -10.731 38.647 0.50 43.20 O ANISOU 3019 O AGLU A 79 6091 6048 4274 1140 -164 -439 O ATOM 3020 O BGLU A 79 4.617 -10.719 38.638 0.50 43.14 O ANISOU 3020 O BGLU A 79 6083 6043 4267 1140 -163 -439 O ATOM 3021 CB AGLU A 79 6.698 -11.196 36.043 0.50 45.13 C ANISOU 3021 CB AGLU A 79 6219 6624 4306 1493 -154 -547 C ATOM 3022 CB BGLU A 79 6.700 -11.222 36.041 0.50 45.01 C ANISOU 3022 CB BGLU A 79 6206 6607 4290 1496 -155 -548 C ATOM 3023 CG AGLU A 79 7.159 -12.018 34.847 0.50 46.28 C ANISOU 3023 CG AGLU A 79 6391 6841 4351 1677 -190 -636 C ATOM 3024 CG BGLU A 79 6.823 -11.925 34.697 0.50 45.91 C ANISOU 3024 CG BGLU A 79 6354 6773 4315 1646 -188 -633 C ATOM 3025 CD AGLU A 79 8.041 -11.231 33.895 0.50 46.62 C ANISOU 3025 CD AGLU A 79 6276 7130 4308 1736 -118 -615 C ATOM 3026 CD BGLU A 79 7.263 -13.372 34.825 0.50 46.91 C ANISOU 3026 CD BGLU A 79 6605 6819 4400 1813 -280 -723 C ATOM 3027 OE1AGLU A 79 8.948 -11.837 33.287 0.50 47.85 O ANISOU 3027 OE1AGLU A 79 6410 7406 4364 1915 -133 -679 O ATOM 3028 OE1BGLU A 79 7.632 -13.788 35.942 0.50 46.70 O ANISOU 3028 OE1BGLU A 79 6620 6718 4406 1818 -312 -712 O ATOM 3029 OE2AGLU A 79 7.832 -10.008 33.754 0.50 45.68 O ANISOU 3029 OE2AGLU A 79 6052 7086 4217 1604 -52 -535 O ATOM 3030 OE2BGLU A 79 7.240 -14.095 33.806 0.50 47.93 O ANISOU 3030 OE2BGLU A 79 6797 6955 4460 1944 -327 -809 O ATOM 3031 N ALA A 80 6.802 -11.046 39.112 1.00 43.97 N ANISOU 3031 N ALA A 80 6112 6305 4291 1318 -163 -450 N ATOM 3032 CA ALA A 80 6.762 -10.371 40.429 1.00 43.29 C ANISOU 3032 CA ALA A 80 5993 6188 4266 1191 -133 -383 C ATOM 3033 C ALA A 80 6.384 -8.894 40.356 1.00 42.18 C ANISOU 3033 C ALA A 80 5749 6113 4165 1057 -59 -319 C ATOM 3034 O ALA A 80 5.713 -8.372 41.248 1.00 40.60 O ANISOU 3034 O ALA A 80 5561 5838 4028 932 -43 -280 O ATOM 3035 CB ALA A 80 8.093 -10.526 41.155 1.00 43.83 C ANISOU 3035 CB ALA A 80 6016 6336 4301 1268 -138 -371 C ATOM 3036 N GLU A 81 6.783 -8.246 39.264 1.00 42.47 N ANISOU 3036 N GLU A 81 5690 6289 4158 1089 -20 -311 N ATOM 3037 CA GLU A 81 6.492 -6.829 39.043 1.00 41.56 C ANISOU 3037 CA GLU A 81 5482 6235 4075 970 36 -248 C ATOM 3038 C GLU A 81 5.012 -6.560 38.701 1.00 39.81 C ANISOU 3038 C GLU A 81 5311 5906 3909 877 37 -251 C ATOM 3039 O GLU A 81 4.602 -5.403 38.655 1.00 39.23 O ANISOU 3039 O GLU A 81 5180 5851 3874 776 72 -203 O ATOM 3040 CB GLU A 81 7.419 -6.244 37.965 1.00 42.62 C ANISOU 3040 CB GLU A 81 5494 6562 4137 1024 70 -225 C ATOM 3041 CG GLU A 81 8.880 -6.107 38.398 1.00 44.13 C ANISOU 3041 CG GLU A 81 5594 6894 4281 1077 81 -194 C ATOM 3042 CD GLU A 81 9.675 -7.418 38.398 1.00 46.18 C ANISOU 3042 CD GLU A 81 5890 7182 4474 1248 43 -260 C ATOM 3043 OE1 GLU A 81 9.311 -8.373 37.660 1.00 46.72 O ANISOU 3043 OE1 GLU A 81 6037 7206 4507 1352 10 -334 O ATOM 3044 OE2 GLU A 81 10.680 -7.497 39.148 1.00 46.95 O ANISOU 3044 OE2 GLU A 81 5942 7343 4553 1284 39 -240 O ATOM 3045 N ASP A 82 4.217 -7.613 38.479 1.00 38.97 N ANISOU 3045 N ASP A 82 5314 5687 3807 909 -9 -305 N ATOM 3046 CA ASP A 82 2.776 -7.471 38.241 1.00 37.69 C ANISOU 3046 CA ASP A 82 5199 5425 3696 818 -15 -305 C ATOM 3047 C ASP A 82 1.949 -7.141 39.486 1.00 36.15 C ANISOU 3047 C ASP A 82 5029 5130 3575 695 -7 -272 C ATOM 3048 O ASP A 82 0.783 -6.767 39.341 1.00 35.62 O ANISOU 3048 O ASP A 82 4970 5012 3552 613 1 -261 O ATOM 3049 CB ASP A 82 2.193 -8.743 37.600 1.00 38.35 C ANISOU 3049 CB ASP A 82 5395 5420 3757 881 -79 -368 C ATOM 3050 CG ASP A 82 2.807 -9.067 36.242 1.00 39.19 C ANISOU 3050 CG ASP A 82 5483 5625 3781 1009 -88 -415 C ATOM 3051 OD1 ASP A 82 3.611 -8.269 35.717 1.00 39.23 O ANISOU 3051 OD1 ASP A 82 5377 5782 3745 1038 -39 -388 O ATOM 3052 OD2 ASP A 82 2.478 -10.136 35.697 1.00 39.79 O ANISOU 3052 OD2 ASP A 82 5660 5630 3829 1080 -151 -477 O ATOM 3053 N LEU A 83 2.510 -7.288 40.692 1.00 34.93 N ANISOU 3053 N LEU A 83 4885 4958 3430 687 -9 -257 N ATOM 3054 CA LEU A 83 1.739 -7.045 41.926 1.00 33.69 C ANISOU 3054 CA LEU A 83 4752 4720 3328 579 -1 -229 C ATOM 3055 C LEU A 83 1.292 -5.592 42.035 1.00 32.18 C ANISOU 3055 C LEU A 83 4481 4566 3179 489 51 -192 C ATOM 3056 O LEU A 83 1.935 -4.695 41.496 1.00 32.34 O ANISOU 3056 O LEU A 83 4423 4678 3188 500 79 -171 O ATOM 3057 CB LEU A 83 2.509 -7.483 43.188 1.00 33.84 C ANISOU 3057 CB LEU A 83 4798 4722 3339 592 -18 -219 C ATOM 3058 CG LEU A 83 3.769 -6.725 43.645 1.00 33.90 C ANISOU 3058 CG LEU A 83 4722 4830 3330 611 12 -191 C ATOM 3059 CD1 LEU A 83 3.449 -5.476 44.467 1.00 33.14 C ANISOU 3059 CD1 LEU A 83 4575 4741 3278 502 53 -152 C ATOM 3060 CD2 LEU A 83 4.676 -7.657 44.445 1.00 34.48 C ANISOU 3060 CD2 LEU A 83 4840 4889 3373 677 -27 -199 C ATOM 3061 N GLY A 84 0.187 -5.385 42.738 1.00 31.04 N ANISOU 3061 N GLY A 84 4360 4355 3080 401 59 -183 N ATOM 3062 CA GLY A 84 -0.446 -4.074 42.868 1.00 30.19 C ANISOU 3062 CA GLY A 84 4192 4263 3014 327 99 -161 C ATOM 3063 C GLY A 84 -1.953 -4.214 42.776 1.00 29.66 C ANISOU 3063 C GLY A 84 4152 4139 2981 269 96 -169 C ATOM 3064 O GLY A 84 -2.480 -5.337 42.763 1.00 30.04 O ANISOU 3064 O GLY A 84 4265 4129 3018 267 62 -182 O ATOM 3065 N VAL A 85 -2.643 -3.076 42.704 1.00 28.94 N ANISOU 3065 N VAL A 85 4008 4063 2926 222 125 -158 N ATOM 3066 CA VAL A 85 -4.107 -3.043 42.582 1.00 28.71 C ANISOU 3066 CA VAL A 85 3981 4001 2928 170 127 -162 C ATOM 3067 C VAL A 85 -4.530 -2.779 41.130 1.00 28.30 C ANISOU 3067 C VAL A 85 3907 3966 2882 188 118 -165 C ATOM 3068 O VAL A 85 -4.065 -1.824 40.508 1.00 28.13 O ANISOU 3068 O VAL A 85 3836 3988 2864 205 130 -152 O ATOM 3069 CB VAL A 85 -4.739 -1.977 43.501 1.00 28.44 C ANISOU 3069 CB VAL A 85 3905 3973 2927 121 160 -157 C ATOM 3070 CG1 VAL A 85 -6.264 -2.073 43.456 1.00 28.55 C ANISOU 3070 CG1 VAL A 85 3910 3974 2963 75 163 -161 C ATOM 3071 CG2 VAL A 85 -4.231 -2.142 44.929 1.00 28.57 C ANISOU 3071 CG2 VAL A 85 3941 3986 2929 106 169 -155 C ATOM 3072 N TYR A 86 -5.417 -3.631 40.615 1.00 28.25 N ANISOU 3072 N TYR A 86 3939 3924 2873 174 91 -177 N ATOM 3073 CA TYR A 86 -5.947 -3.517 39.253 1.00 28.09 C ANISOU 3073 CA TYR A 86 3906 3915 2853 186 76 -181 C ATOM 3074 C TYR A 86 -7.353 -2.909 39.272 1.00 27.89 C ANISOU 3074 C TYR A 86 3841 3884 2871 126 87 -172 C ATOM 3075 O TYR A 86 -8.216 -3.381 40.011 1.00 27.81 O ANISOU 3075 O TYR A 86 3845 3849 2873 74 83 -169 O ATOM 3076 CB TYR A 86 -5.980 -4.893 38.582 1.00 28.61 C ANISOU 3076 CB TYR A 86 4047 3942 2883 216 25 -206 C ATOM 3077 CG TYR A 86 -4.609 -5.442 38.247 1.00 28.74 C ANISOU 3077 CG TYR A 86 4093 3979 2847 305 10 -226 C ATOM 3078 CD1 TYR A 86 -3.837 -6.092 39.213 1.00 28.78 C ANISOU 3078 CD1 TYR A 86 4140 3960 2835 328 0 -231 C ATOM 3079 CD2 TYR A 86 -4.079 -5.303 36.964 1.00 28.84 C ANISOU 3079 CD2 TYR A 86 4087 4050 2821 371 5 -240 C ATOM 3080 CE1 TYR A 86 -2.575 -6.591 38.909 1.00 29.13 C ANISOU 3080 CE1 TYR A 86 4203 4036 2829 424 -16 -253 C ATOM 3081 CE2 TYR A 86 -2.819 -5.796 36.652 1.00 29.29 C ANISOU 3081 CE2 TYR A 86 4156 4151 2820 465 -4 -261 C ATOM 3082 CZ TYR A 86 -2.070 -6.441 37.624 1.00 29.35 C ANISOU 3082 CZ TYR A 86 4203 4134 2816 495 -15 -270 C ATOM 3083 OH TYR A 86 -0.827 -6.926 37.305 1.00 29.71 O ANISOU 3083 OH TYR A 86 4252 4235 2800 601 -26 -295 O ATOM 3084 N TYR A 87 -7.568 -1.866 38.464 1.00 27.77 N ANISOU 3084 N TYR A 87 3773 3901 2876 133 97 -162 N ATOM 3085 CA TYR A 87 -8.873 -1.190 38.352 1.00 27.91 C ANISOU 3085 CA TYR A 87 3747 3923 2936 94 102 -156 C ATOM 3086 C TYR A 87 -9.399 -1.246 36.930 1.00 28.08 C ANISOU 3086 C TYR A 87 3762 3952 2953 101 74 -153 C ATOM 3087 O TYR A 87 -8.672 -0.908 35.999 1.00 27.59 O ANISOU 3087 O TYR A 87 3694 3918 2870 139 68 -146 O ATOM 3088 CB TYR A 87 -8.767 0.294 38.736 1.00 27.65 C ANISOU 3088 CB TYR A 87 3660 3907 2937 98 127 -147 C ATOM 3089 CG TYR A 87 -8.382 0.559 40.167 1.00 27.50 C ANISOU 3089 CG TYR A 87 3643 3883 2924 90 153 -154 C ATOM 3090 CD1 TYR A 87 -9.343 0.570 41.178 1.00 27.69 C ANISOU 3090 CD1 TYR A 87 3650 3908 2961 61 172 -167 C ATOM 3091 CD2 TYR A 87 -7.050 0.817 40.516 1.00 27.37 C ANISOU 3091 CD2 TYR A 87 3636 3872 2890 111 158 -146 C ATOM 3092 CE1 TYR A 87 -8.987 0.818 42.499 1.00 27.66 C ANISOU 3092 CE1 TYR A 87 3651 3907 2953 56 195 -177 C ATOM 3093 CE2 TYR A 87 -6.687 1.069 41.830 1.00 27.27 C ANISOU 3093 CE2 TYR A 87 3629 3854 2878 102 176 -154 C ATOM 3094 CZ TYR A 87 -7.657 1.065 42.814 1.00 27.39 C ANISOU 3094 CZ TYR A 87 3636 3865 2905 76 195 -172 C ATOM 3095 OH TYR A 87 -7.298 1.317 44.108 1.00 27.75 O ANISOU 3095 OH TYR A 87 3688 3912 2942 70 212 -183 O ATOM 3096 N CYS A 88 -10.656 -1.658 36.767 1.00 28.51 N ANISOU 3096 N CYS A 88 3814 3995 3022 61 56 -154 N ATOM 3097 CA CYS A 88 -11.370 -1.440 35.512 1.00 28.92 C ANISOU 3097 CA CYS A 88 3846 4061 3081 59 30 -148 C ATOM 3098 C CYS A 88 -12.062 -0.073 35.577 1.00 29.06 C ANISOU 3098 C CYS A 88 3791 4103 3147 54 48 -134 C ATOM 3099 O CYS A 88 -12.401 0.413 36.664 1.00 29.23 O ANISOU 3099 O CYS A 88 3782 4130 3196 43 76 -138 O ATOM 3100 CB CYS A 88 -12.367 -2.560 35.213 1.00 29.31 C ANISOU 3100 CB CYS A 88 3928 4086 3120 14 -12 -153 C ATOM 3101 SG CYS A 88 -13.761 -2.670 36.343 1.00 29.21 S ANISOU 3101 SG CYS A 88 3872 4086 3141 -64 0 -136 S ATOM 3102 N PHE A 89 -12.233 0.547 34.413 1.00 29.08 N ANISOU 3102 N PHE A 89 3771 4124 3156 70 28 -121 N ATOM 3103 CA PHE A 89 -12.788 1.898 34.299 1.00 29.26 C ANISOU 3103 CA PHE A 89 3736 4157 3224 78 29 -106 C ATOM 3104 C PHE A 89 -13.667 1.957 33.058 1.00 29.50 C ANISOU 3104 C PHE A 89 3747 4204 3259 71 -7 -92 C ATOM 3105 O PHE A 89 -13.320 1.372 32.039 1.00 29.60 O ANISOU 3105 O PHE A 89 3791 4224 3231 76 -31 -89 O ATOM 3106 CB PHE A 89 -11.648 2.926 34.195 1.00 28.95 C ANISOU 3106 CB PHE A 89 3694 4119 3187 105 34 -86 C ATOM 3107 CG PHE A 89 -12.091 4.293 33.739 1.00 29.24 C ANISOU 3107 CG PHE A 89 3693 4152 3267 115 11 -63 C ATOM 3108 CD1 PHE A 89 -12.540 5.237 34.658 1.00 29.42 C ANISOU 3108 CD1 PHE A 89 3692 4151 3337 127 16 -77 C ATOM 3109 CD2 PHE A 89 -12.068 4.637 32.385 1.00 29.35 C ANISOU 3109 CD2 PHE A 89 3699 4184 3268 116 -22 -30 C ATOM 3110 CE1 PHE A 89 -12.952 6.501 34.239 1.00 29.64 C ANISOU 3110 CE1 PHE A 89 3697 4158 3405 146 -20 -60 C ATOM 3111 CE2 PHE A 89 -12.478 5.893 31.964 1.00 29.64 C ANISOU 3111 CE2 PHE A 89 3710 4207 3346 122 -55 -3 C ATOM 3112 CZ PHE A 89 -12.916 6.829 32.890 1.00 29.72 C ANISOU 3112 CZ PHE A 89 3704 4179 3410 139 -58 -18 C ATOM 3113 N GLN A 90 -14.786 2.671 33.136 1.00 29.69 N ANISOU 3113 N GLN A 90 3716 4237 3327 68 -14 -89 N ATOM 3114 CA GLN A 90 -15.606 2.929 31.951 1.00 30.14 C ANISOU 3114 CA GLN A 90 3747 4311 3393 65 -53 -71 C ATOM 3115 C GLN A 90 -15.610 4.424 31.663 1.00 30.16 C ANISOU 3115 C GLN A 90 3717 4307 3436 99 -69 -50 C ATOM 3116 O GLN A 90 -15.936 5.233 32.539 1.00 30.33 O ANISOU 3116 O GLN A 90 3709 4317 3498 122 -57 -64 O ATOM 3117 CB GLN A 90 -17.029 2.356 32.101 1.00 30.65 C ANISOU 3117 CB GLN A 90 3774 4401 3471 29 -64 -77 C ATOM 3118 CG GLN A 90 -17.954 3.045 33.107 1.00 31.00 C ANISOU 3118 CG GLN A 90 3748 4472 3558 41 -41 -88 C ATOM 3119 CD GLN A 90 -18.732 4.225 32.536 1.00 31.39 C ANISOU 3119 CD GLN A 90 3740 4536 3649 81 -69 -78 C ATOM 3120 OE1 GLN A 90 -18.696 4.493 31.336 1.00 31.65 O ANISOU 3120 OE1 GLN A 90 3784 4561 3681 86 -109 -55 O ATOM 3121 NE2 GLN A 90 -19.429 4.946 33.406 1.00 31.61 N ANISOU 3121 NE2 GLN A 90 3710 4590 3709 117 -51 -99 N ATOM 3122 N GLY A 91 -15.221 4.783 30.442 1.00 29.95 N ANISOU 3122 N GLY A 91 3702 4286 3392 103 -101 -17 N ATOM 3123 CA GLY A 91 -15.317 6.159 29.955 1.00 30.13 C ANISOU 3123 CA GLY A 91 3702 4296 3451 123 -136 16 C ATOM 3124 C GLY A 91 -16.405 6.340 28.910 1.00 30.56 C ANISOU 3124 C GLY A 91 3725 4368 3518 122 -180 34 C ATOM 3125 O GLY A 91 -16.287 7.214 28.057 1.00 30.98 O ANISOU 3125 O GLY A 91 3776 4415 3578 128 -222 76 O ATOM 3126 N SER A 92 -17.467 5.534 28.981 1.00 30.60 N ANISOU 3126 N SER A 92 3705 4398 3524 106 -178 11 N ATOM 3127 CA SER A 92 -18.505 5.511 27.948 1.00 31.08 C ANISOU 3127 CA SER A 92 3736 4485 3589 97 -224 29 C ATOM 3128 C SER A 92 -19.721 6.372 28.297 1.00 31.41 C ANISOU 3128 C SER A 92 3709 4535 3691 129 -242 25 C ATOM 3129 O SER A 92 -20.223 7.095 27.437 1.00 31.67 O ANISOU 3129 O SER A 92 3720 4570 3744 147 -291 53 O ATOM 3130 CB SER A 92 -18.943 4.072 27.665 1.00 31.33 C ANISOU 3130 CB SER A 92 3783 4542 3579 51 -227 12 C ATOM 3131 OG SER A 92 -17.854 3.296 27.181 1.00 31.28 O ANISOU 3131 OG SER A 92 3845 4529 3512 43 -222 8 O ATOM 3132 N HIS A 93 -20.189 6.285 29.544 1.00 31.19 N ANISOU 3132 N HIS A 93 3645 4519 3685 142 -204 -10 N ATOM 3133 CA HIS A 93 -21.355 7.038 30.011 1.00 31.61 C ANISOU 3133 CA HIS A 93 3623 4601 3786 189 -214 -26 C ATOM 3134 C HIS A 93 -21.010 7.882 31.237 1.00 31.46 C ANISOU 3134 C HIS A 93 3605 4554 3796 247 -186 -61 C ATOM 3135 O HIS A 93 -20.437 7.377 32.204 1.00 31.42 O ANISOU 3135 O HIS A 93 3622 4546 3769 229 -136 -84 O ATOM 3136 CB HIS A 93 -22.495 6.085 30.363 1.00 32.02 C ANISOU 3136 CB HIS A 93 3611 4729 3825 150 -197 -37 C ATOM 3137 CG HIS A 93 -22.954 5.237 29.218 1.00 32.44 C ANISOU 3137 CG HIS A 93 3667 4805 3852 90 -237 -7 C ATOM 3138 ND1 HIS A 93 -23.599 5.755 28.115 1.00 32.80 N ANISOU 3138 ND1 HIS A 93 3684 4865 3914 105 -293 20 N ATOM 3139 CD2 HIS A 93 -22.883 3.899 29.017 1.00 32.53 C ANISOU 3139 CD2 HIS A 93 3716 4825 3821 15 -238 -1 C ATOM 3140 CE1 HIS A 93 -23.897 4.775 27.281 1.00 32.98 C ANISOU 3140 CE1 HIS A 93 3722 4907 3902 41 -323 38 C ATOM 3141 NE2 HIS A 93 -23.475 3.638 27.804 1.00 32.74 N ANISOU 3141 NE2 HIS A 93 3736 4869 3836 -14 -294 24 N ATOM 3142 N VAL A 94 -21.382 9.160 31.191 1.00 31.71 N ANISOU 3142 N VAL A 94 3618 4559 3873 318 -225 -67 N ATOM 3143 CA VAL A 94 -21.137 10.118 32.277 1.00 31.76 C ANISOU 3143 CA VAL A 94 3634 4526 3908 387 -218 -109 C ATOM 3144 C VAL A 94 -22.134 9.850 33.439 1.00 31.83 C ANISOU 3144 C VAL A 94 3563 4617 3912 425 -170 -162 C ATOM 3145 O VAL A 94 -23.291 9.527 33.174 1.00 32.22 O ANISOU 3145 O VAL A 94 3533 4747 3960 427 -172 -159 O ATOM 3146 CB VAL A 94 -21.254 11.574 31.738 1.00 32.49 C ANISOU 3146 CB VAL A 94 3744 4549 4051 456 -296 -97 C ATOM 3147 CG1 VAL A 94 -21.157 12.627 32.840 1.00 33.23 C ANISOU 3147 CG1 VAL A 94 3857 4592 4177 541 -307 -151 C ATOM 3148 CG2 VAL A 94 -20.173 11.835 30.698 1.00 32.15 C ANISOU 3148 CG2 VAL A 94 3774 4442 4001 403 -339 -33 C ATOM 3149 N PRO A 95 -21.719 9.955 34.708 1.00 31.21 N ANISOU 3149 N PRO A 95 3499 4535 3824 450 -126 -206 N ATOM 3150 CA PRO A 95 -20.333 10.171 35.131 1.00 30.39 C ANISOU 3150 CA PRO A 95 3482 4349 3714 434 -119 -207 C ATOM 3151 C PRO A 95 -19.486 8.922 34.950 1.00 29.43 C ANISOU 3151 C PRO A 95 3400 4234 3549 339 -82 -174 C ATOM 3152 O PRO A 95 -19.973 7.814 35.143 1.00 29.35 O ANISOU 3152 O PRO A 95 3355 4290 3508 292 -45 -173 O ATOM 3153 CB PRO A 95 -20.475 10.506 36.619 1.00 30.65 C ANISOU 3153 CB PRO A 95 3498 4405 3740 494 -81 -272 C ATOM 3154 CG PRO A 95 -21.735 9.826 37.038 1.00 31.12 C ANISOU 3154 CG PRO A 95 3458 4590 3776 497 -38 -291 C ATOM 3155 CD PRO A 95 -22.645 9.986 35.857 1.00 31.69 C ANISOU 3155 CD PRO A 95 3481 4685 3874 506 -85 -260 C ATOM 3156 N TRP A 96 -18.232 9.111 34.559 1.00 28.89 N ANISOU 3156 N TRP A 96 3403 4099 3476 312 -99 -145 N ATOM 3157 CA TRP A 96 -17.302 8.000 34.405 1.00 28.28 C ANISOU 3157 CA TRP A 96 3366 4026 3352 244 -68 -122 C ATOM 3158 C TRP A 96 -16.988 7.390 35.763 1.00 28.04 C ANISOU 3158 C TRP A 96 3343 4014 3298 234 -11 -157 C ATOM 3159 O TRP A 96 -16.910 8.104 36.752 1.00 28.41 O ANISOU 3159 O TRP A 96 3390 4045 3360 276 -2 -192 O ATOM 3160 CB TRP A 96 -16.020 8.459 33.721 1.00 28.02 C ANISOU 3160 CB TRP A 96 3391 3942 3314 227 -97 -81 C ATOM 3161 CG TRP A 96 -16.211 8.943 32.307 1.00 28.40 C ANISOU 3161 CG TRP A 96 3437 3982 3372 223 -153 -34 C ATOM 3162 CD1 TRP A 96 -17.306 8.748 31.494 1.00 28.76 C ANISOU 3162 CD1 TRP A 96 3441 4061 3424 226 -176 -26 C ATOM 3163 CD2 TRP A 96 -15.259 9.657 31.523 1.00 28.41 C ANISOU 3163 CD2 TRP A 96 3475 3950 3369 206 -194 19 C ATOM 3164 NE1 TRP A 96 -17.093 9.323 30.266 1.00 28.93 N ANISOU 3164 NE1 TRP A 96 3478 4067 3448 217 -229 26 N ATOM 3165 CE2 TRP A 96 -15.845 9.887 30.253 1.00 28.77 C ANISOU 3165 CE2 TRP A 96 3504 4009 3419 202 -241 58 C ATOM 3166 CE3 TRP A 96 -13.967 10.143 31.773 1.00 28.25 C ANISOU 3166 CE3 TRP A 96 3495 3897 3339 186 -201 46 C ATOM 3167 CZ2 TRP A 96 -15.178 10.572 29.235 1.00 28.94 C ANISOU 3167 CZ2 TRP A 96 3549 4015 3430 177 -291 124 C ATOM 3168 CZ3 TRP A 96 -13.302 10.821 30.761 1.00 28.57 C ANISOU 3168 CZ3 TRP A 96 3555 3929 3372 156 -251 115 C ATOM 3169 CH2 TRP A 96 -13.912 11.030 29.506 1.00 28.90 C ANISOU 3169 CH2 TRP A 96 3581 3988 3414 151 -295 155 C ATOM 3170 N THR A 97 -16.816 6.070 35.800 1.00 27.68 N ANISOU 3170 N THR A 97 3309 3996 3212 178 18 -148 N ATOM 3171 CA THR A 97 -16.779 5.322 37.059 1.00 27.61 C ANISOU 3171 CA THR A 97 3300 4015 3176 157 66 -172 C ATOM 3172 C THR A 97 -15.738 4.217 37.035 1.00 27.18 C ANISOU 3172 C THR A 97 3307 3940 3081 110 79 -157 C ATOM 3173 O THR A 97 -15.557 3.533 36.016 1.00 27.25 O ANISOU 3173 O THR A 97 3341 3941 3071 83 56 -134 O ATOM 3174 CB THR A 97 -18.142 4.666 37.368 1.00 27.92 C ANISOU 3174 CB THR A 97 3272 4130 3205 131 82 -177 C ATOM 3175 OG1 THR A 97 -18.574 3.898 36.241 1.00 27.55 O ANISOU 3175 OG1 THR A 97 3226 4092 3150 84 51 -145 O ATOM 3176 CG2 THR A 97 -19.196 5.710 37.698 1.00 28.66 C ANISOU 3176 CG2 THR A 97 3292 4269 3330 196 81 -205 C ATOM 3177 N PHE A 98 -15.071 4.046 38.171 1.00 26.88 N ANISOU 3177 N PHE A 98 3294 3894 3026 108 111 -174 N ATOM 3178 CA PHE A 98 -14.089 2.989 38.352 1.00 26.61 C ANISOU 3178 CA PHE A 98 3316 3841 2953 75 121 -164 C ATOM 3179 C PHE A 98 -14.703 1.802 39.083 1.00 27.01 C ANISOU 3179 C PHE A 98 3365 3922 2977 25 139 -165 C ATOM 3180 O PHE A 98 -15.651 1.956 39.865 1.00 27.53 O ANISOU 3180 O PHE A 98 3377 4037 3046 17 161 -175 O ATOM 3181 CB PHE A 98 -12.904 3.509 39.167 1.00 26.14 C ANISOU 3181 CB PHE A 98 3288 3755 2890 97 137 -174 C ATOM 3182 CG PHE A 98 -12.042 4.483 38.423 1.00 25.87 C ANISOU 3182 CG PHE A 98 3267 3690 2872 122 110 -156 C ATOM 3183 CD1 PHE A 98 -12.358 5.840 38.394 1.00 25.95 C ANISOU 3183 CD1 PHE A 98 3255 3680 2923 154 88 -161 C ATOM 3184 CD2 PHE A 98 -10.901 4.041 37.755 1.00 25.49 C ANISOU 3184 CD2 PHE A 98 3253 3638 2793 115 102 -130 C ATOM 3185 CE1 PHE A 98 -11.550 6.735 37.710 1.00 25.90 C ANISOU 3185 CE1 PHE A 98 3267 3643 2930 160 52 -130 C ATOM 3186 CE2 PHE A 98 -10.093 4.927 37.070 1.00 25.34 C ANISOU 3186 CE2 PHE A 98 3237 3611 2781 124 77 -99 C ATOM 3187 CZ PHE A 98 -10.416 6.273 37.049 1.00 25.63 C ANISOU 3187 CZ PHE A 98 3256 3621 2861 137 49 -93 C ATOM 3188 N GLY A 99 -14.139 0.622 38.844 1.00 26.98 N ANISOU 3188 N GLY A 99 3419 3892 2941 -7 124 -152 N ATOM 3189 CA GLY A 99 -14.379 -0.529 39.712 1.00 27.49 C ANISOU 3189 CA GLY A 99 3506 3963 2976 -62 130 -145 C ATOM 3190 C GLY A 99 -13.732 -0.342 41.080 1.00 27.51 C ANISOU 3190 C GLY A 99 3518 3970 2965 -54 167 -157 C ATOM 3191 O GLY A 99 -12.940 0.580 41.286 1.00 27.28 O ANISOU 3191 O GLY A 99 3490 3926 2948 -6 182 -173 O ATOM 3192 N GLY A 100 -14.064 -1.224 42.013 1.00 28.17 N ANISOU 3192 N GLY A 100 3610 4071 3020 -109 175 -143 N ATOM 3193 CA GLY A 100 -13.547 -1.148 43.380 1.00 28.52 C ANISOU 3193 CA GLY A 100 3663 4129 3043 -109 209 -152 C ATOM 3194 C GLY A 100 -12.080 -1.512 43.594 1.00 28.51 C ANISOU 3194 C GLY A 100 3735 4070 3025 -87 200 -154 C ATOM 3195 O GLY A 100 -11.522 -1.200 44.653 1.00 28.67 O ANISOU 3195 O GLY A 100 3761 4100 3032 -76 226 -164 O ATOM 3196 N GLY A 101 -11.466 -2.190 42.624 1.00 28.55 N ANISOU 3196 N GLY A 101 3796 4026 3025 -76 162 -147 N ATOM 3197 CA GLY A 101 -10.057 -2.585 42.701 1.00 28.70 C ANISOU 3197 CA GLY A 101 3876 4006 3023 -41 151 -152 C ATOM 3198 C GLY A 101 -9.868 -4.065 42.995 1.00 29.55 C ANISOU 3198 C GLY A 101 4058 4071 3098 -73 114 -137 C ATOM 3199 O GLY A 101 -10.662 -4.663 43.714 1.00 30.20 O ANISOU 3199 O GLY A 101 4143 4160 3169 -140 108 -116 O ATOM 3200 N THR A 102 -8.819 -4.657 42.427 1.00 30.22 N ANISOU 3200 N THR A 102 4203 4117 3164 -25 82 -148 N ATOM 3201 CA THR A 102 -8.462 -6.058 42.675 1.00 31.11 C ANISOU 3201 CA THR A 102 4404 4171 3245 -35 32 -142 C ATOM 3202 C THR A 102 -6.983 -6.122 43.024 1.00 31.88 C ANISOU 3202 C THR A 102 4531 4262 3321 33 35 -154 C ATOM 3203 O THR A 102 -6.132 -5.796 42.194 1.00 32.15 O ANISOU 3203 O THR A 102 4554 4314 3346 105 37 -173 O ATOM 3204 CB THR A 102 -8.745 -6.949 41.452 1.00 31.28 C ANISOU 3204 CB THR A 102 4484 4146 3257 -24 -30 -153 C ATOM 3205 OG1 THR A 102 -10.157 -7.026 41.236 1.00 31.34 O ANISOU 3205 OG1 THR A 102 4465 4160 3282 -102 -42 -132 O ATOM 3206 CG2 THR A 102 -8.197 -8.372 41.651 1.00 31.83 C ANISOU 3206 CG2 THR A 102 4663 4137 3294 -13 -98 -157 C ATOM 3207 N LYS A 103 -6.684 -6.562 44.243 1.00 32.98 N ANISOU 3207 N LYS A 103 4700 4386 3445 7 33 -139 N ATOM 3208 CA LYS A 103 -5.319 -6.564 44.758 1.00 33.64 C ANISOU 3208 CA LYS A 103 4801 4473 3509 64 37 -146 C ATOM 3209 C LYS A 103 -4.633 -7.873 44.397 1.00 34.34 C ANISOU 3209 C LYS A 103 4981 4500 3567 116 -29 -157 C ATOM 3210 O LYS A 103 -4.998 -8.933 44.907 1.00 34.71 O ANISOU 3210 O LYS A 103 5102 4485 3603 73 -79 -140 O ATOM 3211 CB LYS A 103 -5.340 -6.360 46.275 1.00 33.93 C ANISOU 3211 CB LYS A 103 4827 4526 3540 14 64 -124 C ATOM 3212 CG LYS A 103 -4.049 -5.819 46.867 1.00 34.14 C ANISOU 3212 CG LYS A 103 4836 4580 3554 62 85 -130 C ATOM 3213 CD LYS A 103 -4.283 -5.313 48.293 1.00 34.70 C ANISOU 3213 CD LYS A 103 4884 4681 3621 9 120 -117 C ATOM 3214 CE LYS A 103 -3.210 -4.339 48.741 1.00 34.89 C ANISOU 3214 CE LYS A 103 4871 4741 3644 45 145 -126 C ATOM 3215 NZ LYS A 103 -1.851 -4.949 48.648 1.00 35.56 N ANISOU 3215 NZ LYS A 103 4991 4816 3706 104 113 -122 N ATOM 3216 N LEU A 104 -3.648 -7.801 43.508 1.00 34.73 N ANISOU 3216 N LEU A 104 5027 4571 3598 210 -35 -185 N ATOM 3217 CA LEU A 104 -2.884 -8.986 43.122 1.00 35.72 C ANISOU 3217 CA LEU A 104 5236 4649 3687 290 -98 -211 C ATOM 3218 C LEU A 104 -1.733 -9.175 44.101 1.00 35.70 C ANISOU 3218 C LEU A 104 5245 4656 3665 331 -100 -204 C ATOM 3219 O LEU A 104 -0.914 -8.273 44.258 1.00 35.47 O ANISOU 3219 O LEU A 104 5142 4703 3632 360 -52 -199 O ATOM 3220 CB LEU A 104 -2.349 -8.837 41.694 1.00 35.85 C ANISOU 3220 CB LEU A 104 5231 4711 3680 385 -100 -247 C ATOM 3221 CG LEU A 104 -1.706 -10.082 41.058 1.00 36.87 C ANISOU 3221 CG LEU A 104 5450 4796 3762 490 -172 -292 C ATOM 3222 CD1 LEU A 104 -2.037 -10.168 39.570 1.00 37.28 C ANISOU 3222 CD1 LEU A 104 5508 4862 3794 536 -190 -328 C ATOM 3223 CD2 LEU A 104 -0.193 -10.134 41.253 1.00 37.23 C ANISOU 3223 CD2 LEU A 104 5476 4901 3769 598 -165 -307 C ATOM 3224 N GLU A 105 -1.671 -10.333 44.759 1.00 36.56 N ANISOU 3224 N GLU A 105 5448 4684 3758 326 -163 -198 N ATOM 3225 CA GLU A 105 -0.486 -10.697 45.546 1.00 37.14 C ANISOU 3225 CA GLU A 105 5544 4759 3807 385 -181 -196 C ATOM 3226 C GLU A 105 0.206 -11.931 44.971 1.00 37.39 C ANISOU 3226 C GLU A 105 5671 4733 3804 499 -264 -235 C ATOM 3227 O GLU A 105 -0.447 -12.871 44.517 1.00 37.35 O ANISOU 3227 O GLU A 105 5760 4635 3797 491 -334 -250 O ATOM 3228 CB GLU A 105 -0.801 -10.874 47.050 1.00 37.71 C ANISOU 3228 CB GLU A 105 5643 4800 3887 291 -184 -150 C ATOM 3229 CG GLU A 105 -1.622 -12.099 47.445 1.00 39.17 C ANISOU 3229 CG GLU A 105 5937 4876 4069 222 -262 -124 C ATOM 3230 CD GLU A 105 -1.571 -12.411 48.937 1.00 39.93 C ANISOU 3230 CD GLU A 105 6064 4954 4155 152 -274 -74 C ATOM 3231 OE1 GLU A 105 -0.478 -12.323 49.538 1.00 40.49 O ANISOU 3231 OE1 GLU A 105 6126 5049 4208 210 -270 -76 O ATOM 3232 OE2 GLU A 105 -2.624 -12.773 49.510 1.00 40.64 O ANISOU 3232 OE2 GLU A 105 6182 5011 4247 35 -292 -29 O ATOM 3233 N ILE A 106 1.537 -11.907 45.004 1.00 37.42 N ANISOU 3233 N ILE A 106 5648 4793 3776 607 -260 -254 N ATOM 3234 CA ILE A 106 2.355 -13.045 44.604 1.00 38.42 C ANISOU 3234 CA ILE A 106 5858 4878 3862 742 -339 -299 C ATOM 3235 C ILE A 106 2.310 -14.092 45.719 1.00 39.07 C ANISOU 3235 C ILE A 106 6053 4844 3947 712 -418 -275 C ATOM 3236 O ILE A 106 2.702 -13.810 46.852 1.00 38.79 O ANISOU 3236 O ILE A 106 5989 4832 3916 671 -395 -235 O ATOM 3237 CB ILE A 106 3.828 -12.639 44.344 1.00 38.44 C ANISOU 3237 CB ILE A 106 5776 5006 3824 869 -306 -321 C ATOM 3238 CG1 ILE A 106 3.923 -11.504 43.301 1.00 38.00 C ANISOU 3238 CG1 ILE A 106 5598 5078 3760 879 -228 -326 C ATOM 3239 CG2 ILE A 106 4.657 -13.855 43.926 1.00 39.54 C ANISOU 3239 CG2 ILE A 106 5999 5111 3914 1032 -390 -378 C ATOM 3240 CD1 ILE A 106 3.235 -11.777 41.977 1.00 38.10 C ANISOU 3240 CD1 ILE A 106 5644 5070 3763 908 -247 -368 C ATOM 3241 N LYS A 107 1.817 -15.284 45.391 1.00 39.93 N ANISOU 3241 N LYS A 107 6294 4826 4052 725 -518 -296 N ATOM 3242 CA LYS A 107 1.801 -16.415 46.316 1.00 40.93 C ANISOU 3242 CA LYS A 107 6549 4826 4178 701 -617 -269 C ATOM 3243 C LYS A 107 3.124 -17.174 46.199 1.00 40.99 C ANISOU 3243 C LYS A 107 6611 4818 4144 880 -684 -320 C ATOM 3244 O LYS A 107 3.317 -17.963 45.279 1.00 42.20 O ANISOU 3244 O LYS A 107 6847 4915 4271 999 -760 -385 O ATOM 3245 CB LYS A 107 0.606 -17.333 46.028 1.00 42.25 C ANISOU 3245 CB LYS A 107 6840 4852 4360 616 -709 -258 C ATOM 3246 CG LYS A 107 0.287 -18.315 47.147 1.00 43.63 C ANISOU 3246 CG LYS A 107 7136 4899 4541 526 -805 -198 C ATOM 3247 CD LYS A 107 -0.205 -19.646 46.593 1.00 45.52 C ANISOU 3247 CD LYS A 107 7546 4971 4777 534 -953 -218 C ATOM 3248 CE LYS A 107 -0.714 -20.574 47.688 1.00 46.82 C ANISOU 3248 CE LYS A 107 7830 5007 4950 404 -1055 -136 C ATOM 3249 NZ LYS A 107 -2.122 -20.257 48.064 1.00 46.85 N ANISOU 3249 NZ LYS A 107 7794 5028 4978 193 -1021 -55 N ATOM 3250 N ARG A 108 4.028 -16.913 47.139 1.00 40.12 N ANISOU 3250 N ARG A 108 6453 4766 4025 904 -659 -293 N ATOM 3251 CA ARG A 108 5.367 -17.519 47.165 1.00 40.34 C ANISOU 3251 CA ARG A 108 6508 4807 4013 1077 -713 -335 C ATOM 3252 C ARG A 108 5.509 -18.460 48.377 1.00 40.46 C ANISOU 3252 C ARG A 108 6640 4700 4032 1049 -810 -292 C ATOM 3253 O ARG A 108 4.591 -18.568 49.196 1.00 40.37 O ANISOU 3253 O ARG A 108 6676 4613 4049 887 -824 -225 O ATOM 3254 CB ARG A 108 6.441 -16.421 47.141 1.00 39.73 C ANISOU 3254 CB ARG A 108 6266 4916 3915 1139 -610 -337 C ATOM 3255 CG ARG A 108 6.505 -15.523 48.373 1.00 39.08 C ANISOU 3255 CG ARG A 108 6101 4894 3856 1015 -540 -265 C ATOM 3256 CD ARG A 108 7.605 -15.939 49.334 1.00 39.83 C ANISOU 3256 CD ARG A 108 6209 4997 3929 1083 -583 -249 C ATOM 3257 NE ARG A 108 8.857 -15.196 49.197 1.00 39.69 N ANISOU 3257 NE ARG A 108 6055 5144 3880 1174 -523 -258 N ATOM 3258 CZ ARG A 108 10.041 -15.613 49.654 1.00 40.03 C ANISOU 3258 CZ ARG A 108 6092 5227 3892 1286 -565 -262 C ATOM 3259 NH1 ARG A 108 10.174 -16.788 50.267 1.00 40.74 N ANISOU 3259 NH1 ARG A 108 6312 5192 3976 1335 -672 -263 N ATOM 3260 NH2 ARG A 108 11.116 -14.849 49.480 1.00 40.05 N ANISOU 3260 NH2 ARG A 108 5953 5399 3865 1350 -506 -260 N ATOM 3261 N THR A 109 6.643 -19.150 48.480 1.00 40.60 N ANISOU 3261 N THR A 109 6703 4708 4017 1209 -879 -328 N ATOM 3262 CA THR A 109 6.850 -20.129 49.550 1.00 41.08 C ANISOU 3262 CA THR A 109 6888 4641 4078 1201 -989 -290 C ATOM 3263 C THR A 109 6.914 -19.426 50.907 1.00 39.80 C ANISOU 3263 C THR A 109 6650 4543 3930 1068 -923 -206 C ATOM 3264 O THR A 109 7.223 -18.242 50.974 1.00 38.60 O ANISOU 3264 O THR A 109 6346 4542 3778 1043 -804 -196 O ATOM 3265 CB THR A 109 8.114 -20.993 49.324 1.00 42.44 C ANISOU 3265 CB THR A 109 7119 4796 4209 1426 -1082 -356 C ATOM 3266 OG1 THR A 109 9.271 -20.158 49.190 1.00 42.14 O ANISOU 3266 OG1 THR A 109 6917 4953 4141 1533 -988 -378 O ATOM 3267 CG2 THR A 109 7.962 -21.852 48.068 1.00 43.36 C ANISOU 3267 CG2 THR A 109 7346 4824 4306 1562 -1172 -447 C ATOM 3268 N VAL A 110 6.585 -20.143 51.979 1.00 39.71 N ANISOU 3268 N VAL A 110 6749 4414 3927 976 -1004 -142 N ATOM 3269 CA VAL A 110 6.524 -19.535 53.309 1.00 38.77 C ANISOU 3269 CA VAL A 110 6568 4352 3811 840 -946 -61 C ATOM 3270 C VAL A 110 7.910 -19.036 53.709 1.00 38.39 C ANISOU 3270 C VAL A 110 6421 4427 3739 951 -906 -74 C ATOM 3271 O VAL A 110 8.897 -19.761 53.583 1.00 39.30 O ANISOU 3271 O VAL A 110 6585 4517 3831 1111 -986 -110 O ATOM 3272 CB VAL A 110 5.960 -20.503 54.380 1.00 39.52 C ANISOU 3272 CB VAL A 110 6805 4303 3907 722 -1053 18 C ATOM 3273 CG1 VAL A 110 6.151 -19.950 55.786 1.00 39.12 C ANISOU 3273 CG1 VAL A 110 6693 4328 3844 618 -1001 91 C ATOM 3274 CG2 VAL A 110 4.482 -20.762 54.129 1.00 39.56 C ANISOU 3274 CG2 VAL A 110 6872 4224 3934 566 -1072 53 C ATOM 3275 N ALA A 111 7.963 -17.786 54.165 1.00 37.06 N ANISOU 3275 N ALA A 111 6114 4394 3575 868 -787 -46 N ATOM 3276 CA ALA A 111 9.189 -17.165 54.644 1.00 36.87 C ANISOU 3276 CA ALA A 111 5984 4496 3529 935 -745 -44 C ATOM 3277 C ALA A 111 8.958 -16.665 56.068 1.00 36.52 C ANISOU 3277 C ALA A 111 5919 4474 3483 786 -712 29 C ATOM 3278 O ALA A 111 8.090 -15.825 56.295 1.00 35.76 O ANISOU 3278 O ALA A 111 5771 4415 3403 650 -631 52 O ATOM 3279 CB ALA A 111 9.575 -16.017 53.735 1.00 35.95 C ANISOU 3279 CB ALA A 111 5716 4531 3412 980 -640 -84 C ATOM 3280 N ALA A 112 9.722 -17.193 57.024 1.00 37.08 N ANISOU 3280 N ALA A 112 6033 4524 3531 818 -778 62 N ATOM 3281 CA ALA A 112 9.644 -16.743 58.418 1.00 36.80 C ANISOU 3281 CA ALA A 112 5978 4523 3482 690 -751 128 C ATOM 3282 C ALA A 112 10.271 -15.345 58.554 1.00 35.92 C ANISOU 3282 C ALA A 112 5711 4572 3366 682 -647 119 C ATOM 3283 O ALA A 112 11.261 -15.049 57.884 1.00 36.20 O ANISOU 3283 O ALA A 112 5665 4694 3396 804 -632 80 O ATOM 3284 CB ALA A 112 10.346 -17.731 59.333 1.00 37.79 C ANISOU 3284 CB ALA A 112 6197 4581 3582 736 -861 167 C ATOM 3285 N PRO A 113 9.687 -14.471 59.395 1.00 35.06 N ANISOU 3285 N PRO A 113 5559 4509 3255 538 -578 154 N ATOM 3286 CA PRO A 113 10.319 -13.160 59.578 1.00 34.31 C ANISOU 3286 CA PRO A 113 5334 4546 3156 527 -500 145 C ATOM 3287 C PRO A 113 11.634 -13.238 60.344 1.00 34.52 C ANISOU 3287 C PRO A 113 5335 4629 3152 586 -542 167 C ATOM 3288 O PRO A 113 11.823 -14.153 61.136 1.00 35.15 O ANISOU 3288 O PRO A 113 5502 4643 3210 592 -620 202 O ATOM 3289 CB PRO A 113 9.280 -12.379 60.394 1.00 33.75 C ANISOU 3289 CB PRO A 113 5251 4489 3083 369 -436 170 C ATOM 3290 CG PRO A 113 8.484 -13.423 61.093 1.00 34.44 C ANISOU 3290 CG PRO A 113 5456 4476 3154 298 -494 215 C ATOM 3291 CD PRO A 113 8.409 -14.563 60.124 1.00 34.99 C ANISOU 3291 CD PRO A 113 5608 4444 3243 384 -567 197 C ATOM 3292 N SER A 114 12.539 -12.303 60.070 1.00 34.13 N ANISOU 3292 N SER A 114 5166 4701 3101 627 -498 152 N ATOM 3293 CA SER A 114 13.619 -11.983 60.995 1.00 34.47 C ANISOU 3293 CA SER A 114 5161 4822 3115 632 -518 183 C ATOM 3294 C SER A 114 13.044 -10.959 61.972 1.00 33.93 C ANISOU 3294 C SER A 114 5074 4777 3040 481 -464 204 C ATOM 3295 O SER A 114 12.525 -9.915 61.548 1.00 33.13 O ANISOU 3295 O SER A 114 4914 4713 2961 422 -392 181 O ATOM 3296 CB SER A 114 14.828 -11.399 60.265 1.00 34.54 C ANISOU 3296 CB SER A 114 5042 4962 3119 726 -500 166 C ATOM 3297 OG SER A 114 15.351 -12.329 59.337 1.00 35.39 O ANISOU 3297 OG SER A 114 5161 5066 3221 883 -546 136 O ATOM 3298 N VAL A 115 13.109 -11.264 63.268 1.00 34.24 N ANISOU 3298 N VAL A 115 5168 4795 3046 425 -502 244 N ATOM 3299 CA VAL A 115 12.509 -10.402 64.286 1.00 33.88 C ANISOU 3299 CA VAL A 115 5118 4773 2981 292 -457 257 C ATOM 3300 C VAL A 115 13.589 -9.613 65.014 1.00 34.20 C ANISOU 3300 C VAL A 115 5091 4908 2996 282 -464 270 C ATOM 3301 O VAL A 115 14.582 -10.182 65.466 1.00 35.23 O ANISOU 3301 O VAL A 115 5227 5056 3102 340 -529 299 O ATOM 3302 CB VAL A 115 11.659 -11.191 65.296 1.00 33.96 C ANISOU 3302 CB VAL A 115 5235 4709 2958 211 -487 297 C ATOM 3303 CG1 VAL A 115 10.881 -10.232 66.191 1.00 33.59 C ANISOU 3303 CG1 VAL A 115 5173 4707 2883 87 -424 296 C ATOM 3304 CG2 VAL A 115 10.704 -12.129 64.568 1.00 33.88 C ANISOU 3304 CG2 VAL A 115 5299 4600 2972 219 -503 296 C ATOM 3305 N PHE A 116 13.371 -8.303 65.119 1.00 33.94 N ANISOU 3305 N PHE A 116 4998 4929 2969 209 -405 249 N ATOM 3306 CA PHE A 116 14.280 -7.384 65.798 1.00 34.29 C ANISOU 3306 CA PHE A 116 4982 5055 2991 177 -415 258 C ATOM 3307 C PHE A 116 13.505 -6.497 66.779 1.00 34.13 C ANISOU 3307 C PHE A 116 4987 5035 2945 63 -379 243 C ATOM 3308 O PHE A 116 12.334 -6.176 66.544 1.00 33.38 O ANISOU 3308 O PHE A 116 4913 4907 2864 19 -324 212 O ATOM 3309 CB PHE A 116 14.984 -6.495 64.777 1.00 34.18 C ANISOU 3309 CB PHE A 116 4861 5115 3011 210 -394 244 C ATOM 3310 CG PHE A 116 15.556 -7.238 63.603 1.00 34.57 C ANISOU 3310 CG PHE A 116 4873 5183 3081 331 -410 244 C ATOM 3311 CD1 PHE A 116 16.761 -7.926 63.714 1.00 35.42 C ANISOU 3311 CD1 PHE A 116 4952 5343 3165 422 -471 272 C ATOM 3312 CD2 PHE A 116 14.902 -7.232 62.377 1.00 34.16 C ANISOU 3312 CD2 PHE A 116 4809 5105 3065 361 -366 212 C ATOM 3313 CE1 PHE A 116 17.299 -8.600 62.636 1.00 35.79 C ANISOU 3313 CE1 PHE A 116 4961 5419 3219 552 -486 261 C ATOM 3314 CE2 PHE A 116 15.434 -7.907 61.289 1.00 34.66 C ANISOU 3314 CE2 PHE A 116 4840 5195 3136 482 -382 204 C ATOM 3315 CZ PHE A 116 16.636 -8.590 61.418 1.00 35.53 C ANISOU 3315 CZ PHE A 116 4921 5361 3217 582 -440 225 C ATOM 3316 N ILE A 117 14.166 -6.094 67.864 1.00 34.48 N ANISOU 3316 N ILE A 117 5029 5126 2947 22 -412 260 N ATOM 3317 CA ILE A 117 13.590 -5.157 68.832 1.00 34.52 C ANISOU 3317 CA ILE A 117 5056 5145 2917 -71 -386 234 C ATOM 3318 C ILE A 117 14.528 -3.964 69.035 1.00 34.85 C ANISOU 3318 C ILE A 117 5037 5246 2957 -98 -409 225 C ATOM 3319 O ILE A 117 15.753 -4.116 69.029 1.00 35.25 O ANISOU 3319 O ILE A 117 5042 5346 3006 -64 -462 262 O ATOM 3320 CB ILE A 117 13.224 -5.844 70.178 1.00 34.92 C ANISOU 3320 CB ILE A 117 5186 5184 2897 -117 -409 262 C ATOM 3321 CG1 ILE A 117 12.480 -4.868 71.103 1.00 34.78 C ANISOU 3321 CG1 ILE A 117 5189 5194 2833 -200 -371 221 C ATOM 3322 CG2 ILE A 117 14.448 -6.420 70.885 1.00 35.53 C ANISOU 3322 CG2 ILE A 117 5270 5290 2941 -91 -487 313 C ATOM 3323 CD1 ILE A 117 11.570 -5.551 72.092 1.00 35.08 C ANISOU 3323 CD1 ILE A 117 5298 5228 2802 -251 -359 242 C ATOM 3324 N PHE A 118 13.933 -2.782 69.189 1.00 34.93 N ANISOU 3324 N PHE A 118 5048 5254 2969 -157 -376 177 N ATOM 3325 CA PHE A 118 14.668 -1.541 69.396 1.00 35.54 C ANISOU 3325 CA PHE A 118 5087 5369 3048 -200 -408 165 C ATOM 3326 C PHE A 118 14.201 -0.876 70.687 1.00 36.61 C ANISOU 3326 C PHE A 118 5284 5502 3124 -265 -413 125 C ATOM 3327 O PHE A 118 12.998 -0.625 70.848 1.00 36.62 O ANISOU 3327 O PHE A 118 5326 5475 3114 -280 -361 75 O ATOM 3328 CB PHE A 118 14.443 -0.591 68.223 1.00 34.89 C ANISOU 3328 CB PHE A 118 4955 5274 3030 -202 -380 138 C ATOM 3329 CG PHE A 118 14.939 -1.127 66.914 1.00 34.51 C ANISOU 3329 CG PHE A 118 4837 5245 3028 -137 -373 173 C ATOM 3330 CD1 PHE A 118 16.273 -0.988 66.564 1.00 34.76 C ANISOU 3330 CD1 PHE A 118 4789 5350 3066 -122 -420 220 C ATOM 3331 CD2 PHE A 118 14.082 -1.789 66.043 1.00 33.74 C ANISOU 3331 CD2 PHE A 118 4751 5106 2962 -88 -322 159 C ATOM 3332 CE1 PHE A 118 16.750 -1.486 65.365 1.00 34.56 C ANISOU 3332 CE1 PHE A 118 4694 5367 3072 -50 -410 247 C ATOM 3333 CE2 PHE A 118 14.554 -2.292 64.842 1.00 33.73 C ANISOU 3333 CE2 PHE A 118 4692 5130 2995 -18 -318 182 C ATOM 3334 CZ PHE A 118 15.890 -2.140 64.502 1.00 33.99 C ANISOU 3334 CZ PHE A 118 4642 5246 3028 7 -360 224 C ATOM 3335 N PRO A 119 15.141 -0.583 71.614 1.00 37.72 N ANISOU 3335 N PRO A 119 5428 5683 3221 -299 -477 144 N ATOM 3336 CA PRO A 119 14.754 0.201 72.784 1.00 38.39 C ANISOU 3336 CA PRO A 119 5573 5770 3245 -356 -488 93 C ATOM 3337 C PRO A 119 14.575 1.672 72.394 1.00 38.48 C ANISOU 3337 C PRO A 119 5577 5752 3290 -387 -494 35 C ATOM 3338 O PRO A 119 15.058 2.077 71.343 1.00 37.96 O ANISOU 3338 O PRO A 119 5452 5680 3291 -383 -506 56 O ATOM 3339 CB PRO A 119 15.944 0.025 73.728 1.00 39.10 C ANISOU 3339 CB PRO A 119 5663 5909 3285 -381 -566 138 C ATOM 3340 CG PRO A 119 17.111 -0.138 72.821 1.00 39.10 C ANISOU 3340 CG PRO A 119 5576 5939 3340 -352 -604 197 C ATOM 3341 CD PRO A 119 16.599 -0.818 71.575 1.00 38.27 C ANISOU 3341 CD PRO A 119 5441 5807 3295 -286 -545 205 C ATOM 3342 N PRO A 120 13.876 2.463 73.224 1.00 39.38 N ANISOU 3342 N PRO A 120 5754 5851 3356 -416 -490 -37 N ATOM 3343 CA PRO A 120 13.766 3.896 72.943 1.00 39.72 C ANISOU 3343 CA PRO A 120 5810 5850 3431 -441 -517 -96 C ATOM 3344 C PRO A 120 15.121 4.583 73.101 1.00 40.89 C ANISOU 3344 C PRO A 120 5938 6010 3588 -496 -616 -61 C ATOM 3345 O PRO A 120 15.930 4.161 73.923 1.00 41.33 O ANISOU 3345 O PRO A 120 5997 6114 3594 -518 -663 -22 O ATOM 3346 CB PRO A 120 12.784 4.388 74.006 1.00 39.99 C ANISOU 3346 CB PRO A 120 5924 5881 3391 -441 -498 -186 C ATOM 3347 CG PRO A 120 12.937 3.426 75.133 1.00 40.42 C ANISOU 3347 CG PRO A 120 6004 5997 3359 -448 -496 -154 C ATOM 3348 CD PRO A 120 13.287 2.102 74.529 1.00 39.85 C ANISOU 3348 CD PRO A 120 5880 5941 3321 -425 -473 -65 C ATOM 3349 N SER A 121 15.365 5.620 72.306 1.00 41.72 N ANISOU 3349 N SER A 121 6022 6076 3755 -526 -653 -67 N ATOM 3350 CA SER A 121 16.621 6.372 72.371 1.00 43.04 C ANISOU 3350 CA SER A 121 6165 6256 3933 -598 -756 -24 C ATOM 3351 C SER A 121 16.650 7.243 73.611 1.00 44.76 C ANISOU 3351 C SER A 121 6475 6443 4088 -644 -828 -88 C ATOM 3352 O SER A 121 15.605 7.536 74.187 1.00 44.67 O ANISOU 3352 O SER A 121 6543 6393 4037 -613 -796 -179 O ATOM 3353 CB SER A 121 16.776 7.265 71.140 1.00 42.75 C ANISOU 3353 CB SER A 121 6085 6180 3976 -629 -780 -4 C ATOM 3354 OG SER A 121 15.833 8.323 71.162 1.00 42.81 O ANISOU 3354 OG SER A 121 6172 6095 3996 -632 -788 -93 O ATOM 3355 N ASP A 122 17.850 7.668 74.001 1.00 46.80 N ANISOU 3355 N ASP A 122 6721 6728 4335 -717 -929 -41 N ATOM 3356 CA ASP A 122 18.016 8.636 75.090 1.00 48.92 C ANISOU 3356 CA ASP A 122 7082 6957 4548 -772 -1022 -101 C ATOM 3357 C ASP A 122 17.383 9.982 74.726 1.00 49.47 C ANISOU 3357 C ASP A 122 7222 6917 4656 -789 -1060 -179 C ATOM 3358 O ASP A 122 16.761 10.623 75.575 1.00 49.82 O ANISOU 3358 O ASP A 122 7372 6909 4647 -773 -1086 -282 O ATOM 3359 CB ASP A 122 19.500 8.851 75.425 1.00 50.40 C ANISOU 3359 CB ASP A 122 7230 7194 4726 -860 -1134 -20 C ATOM 3360 CG ASP A 122 20.173 7.600 75.979 1.00 50.88 C ANISOU 3360 CG ASP A 122 7236 7358 4739 -838 -1116 48 C ATOM 3361 OD1 ASP A 122 19.627 6.975 76.919 1.00 51.07 O ANISOU 3361 OD1 ASP A 122 7317 7395 4691 -794 -1074 5 O ATOM 3362 OD2 ASP A 122 21.265 7.254 75.476 1.00 51.50 O ANISOU 3362 OD2 ASP A 122 7211 7510 4847 -863 -1148 147 O ATOM 3363 N GLU A 123 17.537 10.392 73.465 1.00 49.76 N ANISOU 3363 N GLU A 123 7201 6925 4779 -813 -1067 -131 N ATOM 3364 CA GLU A 123 16.999 11.670 72.986 1.00 50.55 C ANISOU 3364 CA GLU A 123 7368 6913 4927 -832 -1117 -190 C ATOM 3365 C GLU A 123 15.487 11.772 73.219 1.00 49.97 C ANISOU 3365 C GLU A 123 7371 6782 4831 -735 -1040 -313 C ATOM 3366 O GLU A 123 14.994 12.824 73.636 1.00 50.63 O ANISOU 3366 O GLU A 123 7560 6777 4901 -728 -1101 -409 O ATOM 3367 CB GLU A 123 17.334 11.902 71.499 1.00 51.04 C ANISOU 3367 CB GLU A 123 7342 6971 5081 -870 -1120 -105 C ATOM 3368 CG GLU A 123 17.243 13.370 71.070 1.00 52.59 C ANISOU 3368 CG GLU A 123 7607 7049 5327 -934 -1224 -129 C ATOM 3369 CD GLU A 123 17.470 13.611 69.577 1.00 52.98 C ANISOU 3369 CD GLU A 123 7569 7100 5459 -975 -1222 -40 C ATOM 3370 OE1 GLU A 123 17.241 12.691 68.757 1.00 52.72 O ANISOU 3370 OE1 GLU A 123 7442 7138 5450 -916 -1112 0 O ATOM 3371 OE2 GLU A 123 17.864 14.744 69.215 1.00 54.11 O ANISOU 3371 OE2 GLU A 123 7746 7172 5643 -1070 -1338 -10 O ATOM 3372 N GLN A 124 14.766 10.678 72.971 1.00 48.74 N ANISOU 3372 N GLN A 124 7166 6684 4669 -657 -913 -311 N ATOM 3373 CA GLN A 124 13.311 10.653 73.159 1.00 48.34 C ANISOU 3373 CA GLN A 124 7165 6609 4592 -567 -829 -413 C ATOM 3374 C GLN A 124 12.915 10.652 74.634 1.00 48.90 C ANISOU 3374 C GLN A 124 7318 6708 4554 -538 -831 -500 C ATOM 3375 O GLN A 124 11.979 11.352 75.021 1.00 49.81 O ANISOU 3375 O GLN A 124 7508 6781 4637 -483 -828 -612 O ATOM 3376 CB GLN A 124 12.683 9.443 72.469 1.00 47.11 C ANISOU 3376 CB GLN A 124 6931 6511 4459 -510 -703 -373 C ATOM 3377 CG GLN A 124 11.160 9.532 72.349 1.00 46.94 C ANISOU 3377 CG GLN A 124 6939 6468 4430 -429 -620 -462 C ATOM 3378 CD GLN A 124 10.492 8.240 71.904 1.00 45.94 C ANISOU 3378 CD GLN A 124 6746 6402 4306 -384 -504 -423 C ATOM 3379 OE1 GLN A 124 9.267 8.168 71.829 1.00 46.02 O ANISOU 3379 OE1 GLN A 124 6764 6416 4304 -327 -432 -482 O ATOM 3380 NE2 GLN A 124 11.285 7.218 71.605 1.00 45.44 N ANISOU 3380 NE2 GLN A 124 6620 6387 4258 -407 -492 -326 N ATOM 3381 N LEU A 125 13.613 9.865 75.448 1.00 48.65 N ANISOU 3381 N LEU A 125 7269 6753 4460 -566 -837 -450 N ATOM 3382 CA LEU A 125 13.263 9.743 76.867 1.00 49.21 C ANISOU 3382 CA LEU A 125 7411 6871 4416 -542 -832 -521 C ATOM 3383 C LEU A 125 13.372 11.059 77.635 1.00 49.96 C ANISOU 3383 C LEU A 125 7615 6900 4468 -558 -941 -619 C ATOM 3384 O LEU A 125 12.621 11.271 78.580 1.00 50.71 O ANISOU 3384 O LEU A 125 7780 7016 4470 -503 -922 -722 O ATOM 3385 CB LEU A 125 14.091 8.651 77.556 1.00 49.21 C ANISOU 3385 CB LEU A 125 7375 6962 4362 -577 -832 -436 C ATOM 3386 CG LEU A 125 13.964 7.215 77.029 1.00 48.43 C ANISOU 3386 CG LEU A 125 7190 6924 4285 -551 -737 -347 C ATOM 3387 CD1 LEU A 125 14.482 6.215 78.051 1.00 48.78 C ANISOU 3387 CD1 LEU A 125 7234 7050 4248 -569 -741 -294 C ATOM 3388 CD2 LEU A 125 12.539 6.857 76.624 1.00 48.13 C ANISOU 3388 CD2 LEU A 125 7145 6890 4251 -483 -624 -393 C ATOM 3389 N LYS A 126 14.273 11.948 77.214 1.00 49.81 N ANISOU 3389 N LYS A 126 7612 6803 4511 -632 -1058 -589 N ATOM 3390 CA LYS A 126 14.369 13.287 77.809 1.00 50.43 C ANISOU 3390 CA LYS A 126 7810 6789 4562 -651 -1182 -684 C ATOM 3391 C LYS A 126 13.057 14.075 77.660 1.00 50.14 C ANISOU 3391 C LYS A 126 7847 6678 4526 -555 -1157 -817 C ATOM 3392 O LYS A 126 12.675 14.803 78.575 1.00 51.49 O ANISOU 3392 O LYS A 126 8127 6815 4620 -512 -1211 -938 O ATOM 3393 CB LYS A 126 15.541 14.074 77.207 1.00 50.59 C ANISOU 3393 CB LYS A 126 7825 6734 4661 -766 -1318 -606 C ATOM 3394 N SER A 127 12.364 13.901 76.532 1.00 48.43 N ANISOU 3394 N SER A 127 7570 6444 4388 -513 -1076 -798 N ATOM 3395 CA SER A 127 11.084 14.583 76.269 1.00 48.22 C ANISOU 3395 CA SER A 127 7596 6356 4369 -412 -1046 -915 C ATOM 3396 C SER A 127 9.850 13.960 76.951 1.00 47.80 C ANISOU 3396 C SER A 127 7536 6406 4221 -302 -919 -999 C ATOM 3397 O SER A 127 8.741 14.488 76.808 1.00 48.05 O ANISOU 3397 O SER A 127 7600 6410 4247 -206 -888 -1102 O ATOM 3398 CB SER A 127 10.835 14.680 74.758 1.00 47.22 C ANISOU 3398 CB SER A 127 7405 6174 4363 -416 -1017 -856 C ATOM 3399 OG SER A 127 10.609 13.401 74.189 1.00 45.92 O ANISOU 3399 OG SER A 127 7123 6106 4218 -404 -886 -773 O ATOM 3400 N GLY A 128 10.029 12.841 77.658 1.00 47.09 N ANISOU 3400 N GLY A 128 7398 6438 4056 -318 -850 -950 N ATOM 3401 CA GLY A 128 8.991 12.285 78.537 1.00 46.99 C ANISOU 3401 CA GLY A 128 7385 6541 3928 -237 -747 -1019 C ATOM 3402 C GLY A 128 8.202 11.099 78.006 1.00 45.61 C ANISOU 3402 C GLY A 128 7108 6456 3766 -211 -605 -956 C ATOM 3403 O GLY A 128 7.289 10.620 78.680 1.00 45.55 O ANISOU 3403 O GLY A 128 7088 6556 3662 -157 -519 -1000 O ATOM 3404 N THR A 129 8.552 10.618 76.813 1.00 44.35 N ANISOU 3404 N THR A 129 6873 6260 3717 -253 -584 -852 N ATOM 3405 CA THR A 129 7.877 9.477 76.184 1.00 43.24 C ANISOU 3405 CA THR A 129 6644 6185 3601 -236 -466 -787 C ATOM 3406 C THR A 129 8.906 8.410 75.809 1.00 42.31 C ANISOU 3406 C THR A 129 6464 6086 3526 -308 -467 -649 C ATOM 3407 O THR A 129 10.072 8.725 75.544 1.00 42.35 O ANISOU 3407 O THR A 129 6470 6041 3581 -365 -552 -598 O ATOM 3408 CB THR A 129 7.092 9.929 74.935 1.00 42.61 C ANISOU 3408 CB THR A 129 6535 6040 3616 -189 -433 -811 C ATOM 3409 OG1 THR A 129 6.149 10.940 75.304 1.00 43.55 O ANISOU 3409 OG1 THR A 129 6712 6141 3693 -106 -440 -945 O ATOM 3410 CG2 THR A 129 6.334 8.781 74.302 1.00 41.95 C ANISOU 3410 CG2 THR A 129 6366 6020 3552 -174 -318 -750 C ATOM 3411 N ALA A 130 8.461 7.152 75.817 1.00 41.45 N ANISOU 3411 N ALA A 130 6302 6054 3391 -303 -379 -590 N ATOM 3412 CA ALA A 130 9.268 6.003 75.411 1.00 40.57 C ANISOU 3412 CA ALA A 130 6137 5960 3319 -346 -374 -469 C ATOM 3413 C ALA A 130 8.515 5.194 74.355 1.00 39.62 C ANISOU 3413 C ALA A 130 5955 5841 3259 -320 -290 -426 C ATOM 3414 O ALA A 130 7.414 4.709 74.616 1.00 39.72 O ANISOU 3414 O ALA A 130 5961 5909 3222 -295 -214 -446 O ATOM 3415 CB ALA A 130 9.575 5.131 76.615 1.00 41.11 C ANISOU 3415 CB ALA A 130 6223 6110 3286 -374 -374 -430 C ATOM 3416 N SER A 131 9.114 5.074 73.168 1.00 38.68 N ANISOU 3416 N SER A 131 5788 5670 3238 -330 -307 -365 N ATOM 3417 CA SER A 131 8.617 4.232 72.087 1.00 37.60 C ANISOU 3417 CA SER A 131 5597 5529 3162 -308 -242 -317 C ATOM 3418 C SER A 131 9.548 3.035 71.965 1.00 37.30 C ANISOU 3418 C SER A 131 5529 5512 3133 -326 -259 -217 C ATOM 3419 O SER A 131 10.745 3.203 71.730 1.00 37.27 O ANISOU 3419 O SER A 131 5504 5497 3161 -346 -321 -174 O ATOM 3420 CB SER A 131 8.604 4.999 70.766 1.00 37.03 C ANISOU 3420 CB SER A 131 5494 5387 3188 -293 -252 -327 C ATOM 3421 OG SER A 131 7.663 6.053 70.795 1.00 37.42 O ANISOU 3421 OG SER A 131 5575 5406 3235 -263 -241 -420 O ATOM 3422 N VAL A 132 9.005 1.835 72.149 1.00 37.16 N ANISOU 3422 N VAL A 132 5509 5527 3082 -320 -210 -178 N ATOM 3423 CA VAL A 132 9.750 0.592 71.929 1.00 37.15 C ANISOU 3423 CA VAL A 132 5490 5531 3096 -320 -229 -89 C ATOM 3424 C VAL A 132 9.233 0.021 70.613 1.00 36.51 C ANISOU 3424 C VAL A 132 5372 5415 3087 -286 -185 -67 C ATOM 3425 O VAL A 132 8.029 -0.186 70.471 1.00 36.26 O ANISOU 3425 O VAL A 132 5346 5384 3048 -282 -126 -90 O ATOM 3426 CB VAL A 132 9.531 -0.432 73.071 1.00 37.51 C ANISOU 3426 CB VAL A 132 5575 5625 3052 -344 -224 -52 C ATOM 3427 CG1 VAL A 132 10.574 -1.541 73.008 1.00 37.48 C ANISOU 3427 CG1 VAL A 132 5566 5614 3060 -337 -274 34 C ATOM 3428 CG2 VAL A 132 9.562 0.260 74.428 1.00 38.36 C ANISOU 3428 CG2 VAL A 132 5726 5781 3069 -374 -245 -99 C ATOM 3429 N VAL A 133 10.135 -0.221 69.661 1.00 36.43 N ANISOU 3429 N VAL A 133 5319 5383 3140 -262 -214 -23 N ATOM 3430 CA VAL A 133 9.764 -0.665 68.313 1.00 36.21 C ANISOU 3430 CA VAL A 133 5256 5321 3179 -223 -180 -9 C ATOM 3431 C VAL A 133 10.218 -2.102 68.085 1.00 36.64 C ANISOU 3431 C VAL A 133 5314 5372 3236 -190 -199 56 C ATOM 3432 O VAL A 133 11.374 -2.437 68.354 1.00 36.90 O ANISOU 3432 O VAL A 133 5337 5427 3257 -177 -252 96 O ATOM 3433 CB VAL A 133 10.387 0.246 67.228 1.00 35.77 C ANISOU 3433 CB VAL A 133 5145 5253 3192 -210 -198 -15 C ATOM 3434 CG1 VAL A 133 10.144 -0.316 65.826 1.00 35.25 C ANISOU 3434 CG1 VAL A 133 5042 5166 3186 -164 -167 5 C ATOM 3435 CG2 VAL A 133 9.831 1.664 67.339 1.00 35.70 C ANISOU 3435 CG2 VAL A 133 5148 5224 3192 -237 -192 -81 C ATOM 3436 N CYS A 134 9.302 -2.934 67.582 1.00 37.05 N ANISOU 3436 N CYS A 134 5383 5393 3301 -176 -162 64 N ATOM 3437 CA CYS A 134 9.621 -4.301 67.135 1.00 37.76 C ANISOU 3437 CA CYS A 134 5490 5455 3404 -133 -189 116 C ATOM 3438 C CYS A 134 9.428 -4.449 65.627 1.00 36.52 C ANISOU 3438 C CYS A 134 5298 5265 3314 -81 -168 107 C ATOM 3439 O CYS A 134 8.378 -4.070 65.101 1.00 35.80 O ANISOU 3439 O CYS A 134 5200 5156 3248 -97 -119 74 O ATOM 3440 CB CYS A 134 8.743 -5.328 67.851 1.00 39.07 C ANISOU 3440 CB CYS A 134 5721 5603 3522 -171 -185 145 C ATOM 3441 SG CYS A 134 9.122 -7.039 67.400 1.00 40.32 S ANISOU 3441 SG CYS A 134 5927 5698 3694 -120 -244 208 S ATOM 3442 N LEU A 135 10.430 -5.025 64.956 1.00 36.30 N ANISOU 3442 N LEU A 135 5246 5237 3309 -14 -208 134 N ATOM 3443 CA LEU A 135 10.440 -5.196 63.492 1.00 35.80 C ANISOU 3443 CA LEU A 135 5145 5159 3298 49 -194 125 C ATOM 3444 C LEU A 135 10.334 -6.673 63.095 1.00 35.65 C ANISOU 3444 C LEU A 135 5178 5086 3280 107 -225 147 C ATOM 3445 O LEU A 135 11.075 -7.510 63.611 1.00 35.99 O ANISOU 3445 O LEU A 135 5253 5125 3296 144 -282 180 O ATOM 3446 CB LEU A 135 11.724 -4.596 62.904 1.00 35.94 C ANISOU 3446 CB LEU A 135 5081 5241 3334 91 -215 133 C ATOM 3447 CG LEU A 135 11.994 -4.721 61.398 1.00 35.85 C ANISOU 3447 CG LEU A 135 5015 5246 3361 163 -203 129 C ATOM 3448 CD1 LEU A 135 10.894 -4.060 60.582 1.00 35.27 C ANISOU 3448 CD1 LEU A 135 4933 5141 3327 132 -148 94 C ATOM 3449 CD2 LEU A 135 13.348 -4.117 61.056 1.00 36.10 C ANISOU 3449 CD2 LEU A 135 4954 5372 3392 188 -227 153 C ATOM 3450 N LEU A 136 9.397 -6.972 62.190 1.00 34.84 N ANISOU 3450 N LEU A 136 5092 4937 3210 116 -196 128 N ATOM 3451 CA LEU A 136 9.278 -8.280 61.541 1.00 34.78 C ANISOU 3451 CA LEU A 136 5137 4866 3211 179 -235 139 C ATOM 3452 C LEU A 136 9.578 -8.040 60.070 1.00 34.08 C ANISOU 3452 C LEU A 136 4990 4798 3161 255 -217 110 C ATOM 3453 O LEU A 136 8.814 -7.352 59.397 1.00 33.37 O ANISOU 3453 O LEU A 136 4869 4710 3101 225 -166 84 O ATOM 3454 CB LEU A 136 7.865 -8.849 61.691 1.00 34.63 C ANISOU 3454 CB LEU A 136 5187 4780 3191 112 -223 146 C ATOM 3455 CG LEU A 136 7.389 -9.335 63.064 1.00 35.03 C ANISOU 3455 CG LEU A 136 5304 4816 3192 29 -243 187 C ATOM 3456 CD1 LEU A 136 7.365 -8.214 64.096 1.00 34.81 C ANISOU 3456 CD1 LEU A 136 5235 4861 3131 -37 -200 177 C ATOM 3457 CD2 LEU A 136 6.011 -9.964 62.918 1.00 35.15 C ANISOU 3457 CD2 LEU A 136 5370 4777 3208 -35 -235 203 C ATOM 3458 N ASN A 137 10.681 -8.598 59.576 1.00 34.30 N ANISOU 3458 N ASN A 137 5000 4851 3184 359 -261 114 N ATOM 3459 CA ASN A 137 11.199 -8.238 58.260 1.00 34.17 C ANISOU 3459 CA ASN A 137 4905 4893 3187 435 -241 91 C ATOM 3460 C ASN A 137 11.200 -9.409 57.278 1.00 34.56 C ANISOU 3460 C ASN A 137 4999 4896 3238 544 -277 69 C ATOM 3461 O ASN A 137 11.662 -10.497 57.610 1.00 35.23 O ANISOU 3461 O ASN A 137 5145 4939 3301 613 -343 77 O ATOM 3462 CB ASN A 137 12.617 -7.677 58.404 1.00 34.55 C ANISOU 3462 CB ASN A 137 4861 5051 3215 471 -253 110 C ATOM 3463 CG ASN A 137 12.971 -6.671 57.318 1.00 34.35 C ANISOU 3463 CG ASN A 137 4730 5116 3207 480 -212 104 C ATOM 3464 OD1 ASN A 137 12.148 -5.837 56.923 1.00 33.87 O ANISOU 3464 OD1 ASN A 137 4656 5038 3175 412 -165 90 O ATOM 3465 ND2 ASN A 137 14.213 -6.724 56.851 1.00 34.83 N ANISOU 3465 ND2 ASN A 137 4709 5282 3244 562 -232 119 N ATOM 3466 N ASN A 138 10.665 -9.168 56.079 1.00 34.33 N ANISOU 3466 N ASN A 138 4944 4867 3232 562 -241 39 N ATOM 3467 CA ASN A 138 10.739 -10.099 54.944 1.00 34.85 C ANISOU 3467 CA ASN A 138 5040 4907 3295 677 -272 6 C ATOM 3468 C ASN A 138 10.124 -11.477 55.220 1.00 35.08 C ANISOU 3468 C ASN A 138 5206 4802 3322 694 -341 2 C ATOM 3469 O ASN A 138 10.836 -12.475 55.344 1.00 35.66 O ANISOU 3469 O ASN A 138 5330 4846 3371 794 -413 -1 O ATOM 3470 CB ASN A 138 12.192 -10.230 54.453 1.00 35.78 C ANISOU 3470 CB ASN A 138 5082 5134 3380 808 -294 -1 C ATOM 3471 CG ASN A 138 12.790 -8.899 54.011 1.00 35.77 C ANISOU 3471 CG ASN A 138 4942 5271 3378 780 -235 15 C ATOM 3472 OD1 ASN A 138 12.079 -7.908 53.836 1.00 35.54 O ANISOU 3472 OD1 ASN A 138 4885 5241 3379 681 -183 20 O ATOM 3473 ND2 ASN A 138 14.105 -8.873 53.830 1.00 36.36 N ANISOU 3473 ND2 ASN A 138 4930 5468 3417 867 -250 27 N ATOM 3474 N PHE A 139 8.795 -11.505 55.298 1.00 34.72 N ANISOU 3474 N PHE A 139 5216 4676 3299 593 -324 7 N ATOM 3475 CA PHE A 139 8.032 -12.725 55.560 1.00 35.36 C ANISOU 3475 CA PHE A 139 5427 4628 3381 571 -391 18 C ATOM 3476 C PHE A 139 6.835 -12.879 54.620 1.00 35.58 C ANISOU 3476 C PHE A 139 5487 4596 3434 536 -379 -4 C ATOM 3477 O PHE A 139 6.351 -11.901 54.049 1.00 34.68 O ANISOU 3477 O PHE A 139 5297 4539 3343 496 -305 -20 O ATOM 3478 CB PHE A 139 7.559 -12.752 57.025 1.00 35.29 C ANISOU 3478 CB PHE A 139 5461 4589 3360 448 -397 72 C ATOM 3479 CG PHE A 139 6.616 -11.639 57.392 1.00 34.15 C ANISOU 3479 CG PHE A 139 5257 4491 3227 322 -312 81 C ATOM 3480 CD1 PHE A 139 5.253 -11.789 57.208 1.00 33.93 C ANISOU 3480 CD1 PHE A 139 5264 4413 3213 237 -297 87 C ATOM 3481 CD2 PHE A 139 7.090 -10.449 57.937 1.00 33.63 C ANISOU 3481 CD2 PHE A 139 5104 4519 3155 293 -256 81 C ATOM 3482 CE1 PHE A 139 4.370 -10.773 57.546 1.00 33.42 C ANISOU 3482 CE1 PHE A 139 5140 4401 3155 139 -220 88 C ATOM 3483 CE2 PHE A 139 6.214 -9.426 58.282 1.00 32.96 C ANISOU 3483 CE2 PHE A 139 4976 4470 3078 195 -187 78 C ATOM 3484 CZ PHE A 139 4.851 -9.587 58.086 1.00 32.84 C ANISOU 3484 CZ PHE A 139 4988 4413 3075 126 -166 79 C ATOM 3485 N TYR A 140 6.378 -14.122 54.471 1.00 37.02 N ANISOU 3485 N TYR A 140 5790 4660 3616 550 -462 -2 N ATOM 3486 CA TYR A 140 5.169 -14.452 53.716 1.00 37.86 C ANISOU 3486 CA TYR A 140 5946 4694 3745 499 -470 -13 C ATOM 3487 C TYR A 140 4.550 -15.704 54.341 1.00 39.37 C ANISOU 3487 C TYR A 140 6278 4751 3930 435 -569 30 C ATOM 3488 O TYR A 140 5.296 -16.638 54.633 1.00 40.02 O ANISOU 3488 O TYR A 140 6444 4768 3995 514 -659 33 O ATOM 3489 CB TYR A 140 5.488 -14.721 52.233 1.00 38.33 C ANISOU 3489 CB TYR A 140 6006 4751 3806 630 -489 -78 C ATOM 3490 CG TYR A 140 4.228 -14.811 51.389 1.00 38.31 C ANISOU 3490 CG TYR A 140 6034 4695 3828 569 -484 -91 C ATOM 3491 CD1 TYR A 140 3.613 -13.653 50.901 1.00 37.29 C ANISOU 3491 CD1 TYR A 140 5803 4647 3721 508 -389 -97 C ATOM 3492 CD2 TYR A 140 3.604 -16.047 51.139 1.00 39.09 C ANISOU 3492 CD2 TYR A 140 6269 4656 3928 560 -585 -91 C ATOM 3493 CE1 TYR A 140 2.436 -13.721 50.169 1.00 37.16 C ANISOU 3493 CE1 TYR A 140 5806 4586 3725 448 -387 -104 C ATOM 3494 CE2 TYR A 140 2.427 -16.123 50.403 1.00 38.92 C ANISOU 3494 CE2 TYR A 140 6271 4590 3928 491 -587 -96 C ATOM 3495 CZ TYR A 140 1.848 -14.958 49.921 1.00 38.08 C ANISOU 3495 CZ TYR A 140 6051 4577 3842 437 -484 -103 C ATOM 3496 OH TYR A 140 0.684 -15.011 49.194 1.00 38.29 O ANISOU 3496 OH TYR A 140 6093 4568 3888 371 -486 -106 O ATOM 3497 N PRO A 141 3.224 -15.776 54.530 1.00 40.57 N ANISOU 3497 N PRO A 141 6458 4863 4094 296 -562 68 N ATOM 3498 CA PRO A 141 2.225 -14.794 54.073 1.00 40.45 C ANISOU 3498 CA PRO A 141 6354 4915 4102 216 -468 59 C ATOM 3499 C PRO A 141 2.095 -13.552 54.959 1.00 40.97 C ANISOU 3499 C PRO A 141 6313 5093 4162 139 -368 79 C ATOM 3500 O PRO A 141 2.848 -13.390 55.906 1.00 41.65 O ANISOU 3500 O PRO A 141 6386 5213 4225 146 -365 98 O ATOM 3501 CB PRO A 141 0.930 -15.612 54.083 1.00 40.85 C ANISOU 3501 CB PRO A 141 6490 4873 4157 101 -525 102 C ATOM 3502 CG PRO A 141 1.127 -16.584 55.196 1.00 41.60 C ANISOU 3502 CG PRO A 141 6686 4894 4225 54 -612 164 C ATOM 3503 CD PRO A 141 2.592 -16.929 55.200 1.00 41.62 C ANISOU 3503 CD PRO A 141 6719 4879 4217 205 -660 129 C ATOM 3504 N ARG A 142 1.158 -12.671 54.621 1.00 42.09 N ANISOU 3504 N ARG A 142 6379 5289 4323 74 -292 70 N ATOM 3505 CA ARG A 142 0.917 -11.433 55.377 1.00 42.56 C ANISOU 3505 CA ARG A 142 6344 5448 4377 12 -202 75 C ATOM 3506 C ARG A 142 0.558 -11.678 56.857 1.00 43.24 C ANISOU 3506 C ARG A 142 6458 5548 4425 -89 -208 132 C ATOM 3507 O ARG A 142 0.959 -10.900 57.723 1.00 42.74 O ANISOU 3507 O ARG A 142 6344 5555 4341 -100 -163 131 O ATOM 3508 CB ARG A 142 -0.199 -10.621 54.703 1.00 42.82 C ANISOU 3508 CB ARG A 142 6309 5522 4438 -34 -137 55 C ATOM 3509 CG ARG A 142 -0.334 -9.179 55.169 1.00 43.20 C ANISOU 3509 CG ARG A 142 6260 5666 4489 -58 -50 37 C ATOM 3510 CD ARG A 142 -1.701 -8.622 54.788 1.00 44.36 C ANISOU 3510 CD ARG A 142 6356 5844 4654 -119 -1 29 C ATOM 3511 NE ARG A 142 -1.891 -7.244 55.252 1.00 44.91 N ANISOU 3511 NE ARG A 142 6344 5994 4725 -131 71 3 N ATOM 3512 CZ ARG A 142 -1.522 -6.141 54.595 1.00 45.18 C ANISOU 3512 CZ ARG A 142 6320 6056 4791 -77 105 -37 C ATOM 3513 NH1 ARG A 142 -0.916 -6.197 53.405 1.00 45.45 N ANISOU 3513 NH1 ARG A 142 6352 6065 4853 -9 86 -54 N ATOM 3514 NH2 ARG A 142 -1.754 -4.951 55.145 1.00 45.44 N ANISOU 3514 NH2 ARG A 142 6299 6145 4823 -92 153 -61 N ATOM 3515 N GLU A 143 -0.182 -12.754 57.138 1.00 44.23 N ANISOU 3515 N GLU A 143 6664 5607 4535 -167 -269 183 N ATOM 3516 CA GLU A 143 -0.685 -13.025 58.496 1.00 45.14 C ANISOU 3516 CA GLU A 143 6799 5750 4604 -282 -274 250 C ATOM 3517 C GLU A 143 0.433 -13.242 59.525 1.00 44.79 C ANISOU 3517 C GLU A 143 6789 5705 4525 -252 -307 271 C ATOM 3518 O GLU A 143 1.319 -14.079 59.335 1.00 44.43 O ANISOU 3518 O GLU A 143 6821 5577 4485 -177 -389 273 O ATOM 3519 CB GLU A 143 -1.637 -14.235 58.524 1.00 46.87 C ANISOU 3519 CB GLU A 143 7105 5892 4811 -384 -351 317 C ATOM 3520 CG GLU A 143 -3.070 -13.934 58.095 1.00 47.60 C ANISOU 3520 CG GLU A 143 7141 6031 4912 -475 -305 327 C ATOM 3521 CD GLU A 143 -3.247 -13.742 56.594 1.00 47.83 C ANISOU 3521 CD GLU A 143 7155 6022 4996 -405 -300 267 C ATOM 3522 OE1 GLU A 143 -2.329 -14.086 55.809 1.00 47.85 O ANISOU 3522 OE1 GLU A 143 7208 5949 5023 -290 -348 223 O ATOM 3523 OE2 GLU A 143 -4.325 -13.244 56.198 1.00 48.46 O ANISOU 3523 OE2 GLU A 143 7168 6159 5088 -460 -248 263 O ATOM 3524 N ALA A 144 0.362 -12.477 60.612 1.00 44.34 N ANISOU 3524 N ALA A 144 6675 5744 4430 -305 -246 282 N ATOM 3525 CA ALA A 144 1.301 -12.578 61.724 1.00 44.75 C ANISOU 3525 CA ALA A 144 6750 5812 4440 -295 -272 307 C ATOM 3526 C ALA A 144 0.707 -11.919 62.973 1.00 44.93 C ANISOU 3526 C ALA A 144 6723 5943 4405 -391 -208 330 C ATOM 3527 O ALA A 144 -0.109 -11.005 62.860 1.00 44.65 O ANISOU 3527 O ALA A 144 6609 5984 4371 -420 -128 297 O ATOM 3528 CB ALA A 144 2.625 -11.924 61.353 1.00 44.09 C ANISOU 3528 CB ALA A 144 6625 5746 4382 -173 -259 250 C ATOM 3529 N LYS A 145 1.110 -12.396 64.149 1.00 45.60 N ANISOU 3529 N LYS A 145 6855 6036 4435 -434 -249 384 N ATOM 3530 CA LYS A 145 0.682 -11.826 65.428 1.00 46.36 C ANISOU 3530 CA LYS A 145 6909 6246 4460 -515 -194 404 C ATOM 3531 C LYS A 145 1.901 -11.289 66.180 1.00 45.98 C ANISOU 3531 C LYS A 145 6851 6229 4388 -459 -196 381 C ATOM 3532 O LYS A 145 2.874 -12.016 66.388 1.00 46.25 O ANISOU 3532 O LYS A 145 6950 6201 4422 -420 -273 411 O ATOM 3533 CB LYS A 145 -0.025 -12.891 66.277 1.00 48.22 C ANISOU 3533 CB LYS A 145 7207 6481 4634 -640 -244 504 C ATOM 3534 CG LYS A 145 -0.617 -12.379 67.592 1.00 49.21 C ANISOU 3534 CG LYS A 145 7282 6748 4667 -731 -182 530 C ATOM 3535 CD LYS A 145 -0.820 -13.499 68.608 1.00 50.98 C ANISOU 3535 CD LYS A 145 7581 6969 4819 -845 -252 643 C ATOM 3536 CE LYS A 145 -2.128 -14.245 68.394 1.00 52.14 C ANISOU 3536 CE LYS A 145 7738 7122 4951 -969 -269 720 C ATOM 3537 NZ LYS A 145 -3.261 -13.562 69.082 1.00 52.68 N ANISOU 3537 NZ LYS A 145 7703 7370 4941 -1054 -171 727 N ATOM 3538 N VAL A 146 1.832 -10.021 66.585 1.00 45.24 N ANISOU 3538 N VAL A 146 6682 6232 4275 -452 -118 325 N ATOM 3539 CA VAL A 146 2.850 -9.384 67.422 1.00 44.67 C ANISOU 3539 CA VAL A 146 6597 6204 4171 -420 -118 304 C ATOM 3540 C VAL A 146 2.238 -9.117 68.798 1.00 44.76 C ANISOU 3540 C VAL A 146 6600 6320 4089 -506 -83 324 C ATOM 3541 O VAL A 146 1.279 -8.356 68.911 1.00 44.43 O ANISOU 3541 O VAL A 146 6500 6358 4023 -533 -10 286 O ATOM 3542 CB VAL A 146 3.340 -8.054 66.800 1.00 43.92 C ANISOU 3542 CB VAL A 146 6433 6131 4125 -344 -72 219 C ATOM 3543 CG1 VAL A 146 4.368 -7.368 67.703 1.00 44.20 C ANISOU 3543 CG1 VAL A 146 6458 6210 4125 -326 -83 201 C ATOM 3544 CG2 VAL A 146 3.911 -8.300 65.409 1.00 43.23 C ANISOU 3544 CG2 VAL A 146 6343 5965 4117 -262 -100 203 C ATOM 3545 N GLN A 147 2.787 -9.754 69.831 1.00 44.92 N ANISOU 3545 N GLN A 147 6674 6344 4049 -541 -136 384 N ATOM 3546 CA GLN A 147 2.382 -9.503 71.214 1.00 45.20 C ANISOU 3546 CA GLN A 147 6702 6492 3981 -616 -107 404 C ATOM 3547 C GLN A 147 3.511 -8.843 71.990 1.00 44.47 C ANISOU 3547 C GLN A 147 6609 6429 3859 -575 -122 371 C ATOM 3548 O GLN A 147 4.647 -9.312 71.954 1.00 44.26 O ANISOU 3548 O GLN A 147 6624 6336 3858 -532 -192 396 O ATOM 3549 CB GLN A 147 1.992 -10.804 71.904 1.00 46.54 C ANISOU 3549 CB GLN A 147 6938 6655 4090 -716 -163 515 C ATOM 3550 CG GLN A 147 0.624 -11.323 71.499 1.00 47.15 C ANISOU 3550 CG GLN A 147 7004 6748 4164 -798 -141 559 C ATOM 3551 CD GLN A 147 0.119 -12.406 72.431 1.00 48.46 C ANISOU 3551 CD GLN A 147 7223 6945 4245 -927 -189 679 C ATOM 3552 OE1 GLN A 147 0.873 -13.295 72.840 1.00 49.28 O ANISOU 3552 OE1 GLN A 147 7413 6972 4338 -940 -282 747 O ATOM 3553 NE2 GLN A 147 -1.162 -12.336 72.775 1.00 49.00 N ANISOU 3553 NE2 GLN A 147 7237 7133 4247 -1023 -131 711 N ATOM 3554 N TRP A 148 3.183 -7.759 72.688 1.00 44.06 N ANISOU 3554 N TRP A 148 6512 6480 3750 -583 -60 312 N ATOM 3555 CA TRP A 148 4.125 -7.074 73.574 1.00 43.81 C ANISOU 3555 CA TRP A 148 6485 6487 3674 -560 -77 280 C ATOM 3556 C TRP A 148 3.976 -7.591 74.997 1.00 44.81 C ANISOU 3556 C TRP A 148 6649 6695 3683 -639 -94 341 C ATOM 3557 O TRP A 148 2.863 -7.857 75.458 1.00 45.19 O ANISOU 3557 O TRP A 148 6684 6825 3660 -709 -52 371 O ATOM 3558 CB TRP A 148 3.901 -5.559 73.545 1.00 43.29 C ANISOU 3558 CB TRP A 148 6364 6474 3609 -518 -17 172 C ATOM 3559 CG TRP A 148 4.531 -4.899 72.363 1.00 42.28 C ANISOU 3559 CG TRP A 148 6209 6266 3588 -443 -25 120 C ATOM 3560 CD1 TRP A 148 3.905 -4.450 71.235 1.00 41.35 C ANISOU 3560 CD1 TRP A 148 6050 6119 3542 -409 17 77 C ATOM 3561 CD2 TRP A 148 5.924 -4.623 72.187 1.00 41.74 C ANISOU 3561 CD2 TRP A 148 6147 6151 3563 -398 -82 115 C ATOM 3562 NE1 TRP A 148 4.820 -3.908 70.372 1.00 40.73 N ANISOU 3562 NE1 TRP A 148 5954 5978 3544 -351 -9 48 N ATOM 3563 CE2 TRP A 148 6.069 -4.002 70.930 1.00 41.07 C ANISOU 3563 CE2 TRP A 148 6020 6014 3569 -344 -69 72 C ATOM 3564 CE3 TRP A 148 7.065 -4.844 72.972 1.00 41.97 C ANISOU 3564 CE3 TRP A 148 6206 6185 3557 -401 -145 148 C ATOM 3565 CZ2 TRP A 148 7.316 -3.590 70.437 1.00 40.61 C ANISOU 3565 CZ2 TRP A 148 5943 5922 3565 -300 -114 65 C ATOM 3566 CZ3 TRP A 148 8.302 -4.437 72.486 1.00 41.51 C ANISOU 3566 CZ3 TRP A 148 6127 6091 3555 -352 -190 138 C ATOM 3567 CH2 TRP A 148 8.417 -3.817 71.227 1.00 40.96 C ANISOU 3567 CH2 TRP A 148 6010 5982 3574 -305 -173 99 C ATOM 3568 N LYS A 149 5.107 -7.733 75.682 1.00 45.29 N ANISOU 3568 N LYS A 149 6748 6743 3718 -629 -156 364 N ATOM 3569 CA LYS A 149 5.134 -8.135 77.086 1.00 46.37 C ANISOU 3569 CA LYS A 149 6923 6959 3737 -700 -180 421 C ATOM 3570 C LYS A 149 6.121 -7.275 77.861 1.00 46.16 C ANISOU 3570 C LYS A 149 6897 6969 3671 -667 -201 369 C ATOM 3571 O LYS A 149 7.233 -7.012 77.388 1.00 45.32 O ANISOU 3571 O LYS A 149 6790 6793 3637 -604 -247 347 O ATOM 3572 CB LYS A 149 5.498 -9.615 77.216 1.00 47.37 C ANISOU 3572 CB LYS A 149 7121 7013 3864 -741 -267 539 C ATOM 3573 CG LYS A 149 4.359 -10.544 76.837 1.00 47.93 C ANISOU 3573 CG LYS A 149 7207 7068 3935 -813 -258 609 C ATOM 3574 CD LYS A 149 4.799 -11.993 76.760 1.00 48.76 C ANISOU 3574 CD LYS A 149 7400 7062 4063 -840 -366 717 C ATOM 3575 CE LYS A 149 3.647 -12.867 76.290 1.00 49.35 C ANISOU 3575 CE LYS A 149 7495 7108 4146 -920 -369 786 C ATOM 3576 NZ LYS A 149 3.917 -14.313 76.501 1.00 50.55 N ANISOU 3576 NZ LYS A 149 7753 7160 4294 -973 -488 904 N ATOM 3577 N VAL A 150 5.693 -6.831 79.041 1.00 46.75 N ANISOU 3577 N VAL A 150 6970 7164 3628 -712 -168 351 N ATOM 3578 CA VAL A 150 6.522 -6.035 79.939 1.00 47.05 C ANISOU 3578 CA VAL A 150 7021 7247 3609 -693 -194 301 C ATOM 3579 C VAL A 150 6.547 -6.763 81.285 1.00 48.21 C ANISOU 3579 C VAL A 150 7214 7476 3629 -771 -227 383 C ATOM 3580 O VAL A 150 5.557 -6.748 82.021 1.00 48.80 O ANISOU 3580 O VAL A 150 7277 7672 3595 -826 -172 387 O ATOM 3581 CB VAL A 150 5.989 -4.592 80.082 1.00 46.90 C ANISOU 3581 CB VAL A 150 6963 7297 3559 -655 -128 176 C ATOM 3582 CG1 VAL A 150 6.949 -3.750 80.908 1.00 47.27 C ANISOU 3582 CG1 VAL A 150 7036 7366 3560 -636 -174 121 C ATOM 3583 CG2 VAL A 150 5.786 -3.956 78.715 1.00 45.79 C ANISOU 3583 CG2 VAL A 150 6780 7077 3542 -591 -96 111 C ATOM 3584 N ASP A 151 7.679 -7.404 81.583 1.00 48.59 N ANISOU 3584 N ASP A 151 7308 7466 3687 -773 -317 449 N ATOM 3585 CA ASP A 151 7.829 -8.308 82.738 1.00 49.61 C ANISOU 3585 CA ASP A 151 7492 7646 3711 -849 -370 550 C ATOM 3586 C ASP A 151 6.807 -9.450 82.712 1.00 49.97 C ANISOU 3586 C ASP A 151 7558 7703 3726 -932 -360 652 C ATOM 3587 O ASP A 151 6.030 -9.630 83.653 1.00 51.42 O ANISOU 3587 O ASP A 151 7742 8009 3784 -1016 -328 694 O ATOM 3588 CB ASP A 151 7.761 -7.537 84.063 1.00 50.54 C ANISOU 3588 CB ASP A 151 7612 7903 3690 -878 -347 504 C ATOM 3589 CG ASP A 151 8.863 -6.514 84.202 1.00 50.32 C ANISOU 3589 CG ASP A 151 7581 7853 3686 -815 -383 420 C ATOM 3590 OD1 ASP A 151 10.001 -6.789 83.769 1.00 50.08 O ANISOU 3590 OD1 ASP A 151 7562 7726 3739 -778 -458 450 O ATOM 3591 OD2 ASP A 151 8.594 -5.439 84.768 1.00 50.65 O ANISOU 3591 OD2 ASP A 151 7609 7978 3656 -803 -342 325 O ATOM 3592 N ASN A 152 6.807 -10.193 81.604 1.00 48.97 N ANISOU 3592 N ASN A 152 7444 7451 3711 -910 -390 692 N ATOM 3593 CA ASN A 152 5.903 -11.330 81.379 1.00 49.22 C ANISOU 3593 CA ASN A 152 7504 7459 3737 -990 -401 792 C ATOM 3594 C ASN A 152 4.391 -11.017 81.438 1.00 49.23 C ANISOU 3594 C ASN A 152 7447 7581 3676 -1056 -300 778 C ATOM 3595 O ASN A 152 3.581 -11.944 81.512 1.00 49.94 O ANISOU 3595 O ASN A 152 7558 7686 3732 -1153 -312 879 O ATOM 3596 CB ASN A 152 6.237 -12.468 82.354 1.00 50.36 C ANISOU 3596 CB ASN A 152 7731 7600 3805 -1072 -495 924 C ATOM 3597 N ALA A 153 4.016 -9.735 81.373 1.00 48.46 N ANISOU 3597 N ALA A 153 7279 7569 3566 -1003 -208 658 N ATOM 3598 CA ALA A 153 2.617 -9.302 81.443 1.00 48.58 C ANISOU 3598 CA ALA A 153 7224 7718 3517 -1041 -107 627 C ATOM 3599 C ALA A 153 2.175 -8.801 80.066 1.00 47.42 C ANISOU 3599 C ALA A 153 7028 7499 3492 -971 -59 550 C ATOM 3600 O ALA A 153 2.714 -7.810 79.563 1.00 46.42 O ANISOU 3600 O ALA A 153 6881 7324 3434 -874 -44 444 O ATOM 3601 CB ALA A 153 2.457 -8.205 82.480 1.00 49.05 C ANISOU 3601 CB ALA A 153 7247 7934 3456 -1021 -46 539 C ATOM 3602 N LEU A 154 1.204 -9.493 79.467 1.00 47.35 N ANISOU 3602 N LEU A 154 7001 7483 3506 -1030 -41 611 N ATOM 3603 CA LEU A 154 0.705 -9.178 78.122 1.00 46.39 C ANISOU 3603 CA LEU A 154 6836 7293 3497 -975 -2 555 C ATOM 3604 C LEU A 154 0.153 -7.754 78.061 1.00 45.78 C ANISOU 3604 C LEU A 154 6677 7312 3403 -904 94 423 C ATOM 3605 O LEU A 154 -0.614 -7.356 78.936 1.00 47.09 O ANISOU 3605 O LEU A 154 6798 7643 3449 -934 155 405 O ATOM 3606 CB LEU A 154 -0.390 -10.179 77.718 1.00 47.08 C ANISOU 3606 CB LEU A 154 6916 7387 3584 -1074 -2 653 C ATOM 3607 CG LEU A 154 -1.070 -10.015 76.350 1.00 46.58 C ANISOU 3607 CG LEU A 154 6808 7263 3625 -1037 34 611 C ATOM 3608 CD1 LEU A 154 -0.057 -10.076 75.211 1.00 45.57 C ANISOU 3608 CD1 LEU A 154 6725 6950 3638 -942 -23 573 C ATOM 3609 CD2 LEU A 154 -2.157 -11.067 76.167 1.00 47.37 C ANISOU 3609 CD2 LEU A 154 6907 7387 3704 -1160 21 724 C ATOM 3610 N GLN A 155 0.547 -6.997 77.037 1.00 44.04 N ANISOU 3610 N GLN A 155 6442 6995 3297 -806 101 333 N ATOM 3611 CA GLN A 155 0.115 -5.609 76.883 1.00 43.33 C ANISOU 3611 CA GLN A 155 6292 6965 3207 -728 173 205 C ATOM 3612 C GLN A 155 -1.119 -5.491 76.009 1.00 42.90 C ANISOU 3612 C GLN A 155 6170 6938 3190 -724 236 186 C ATOM 3613 O GLN A 155 -1.457 -6.404 75.250 1.00 42.58 O ANISOU 3613 O GLN A 155 6136 6835 3208 -771 217 261 O ATOM 3614 CB GLN A 155 1.238 -4.754 76.296 1.00 42.40 C ANISOU 3614 CB GLN A 155 6193 6731 3185 -635 137 124 C ATOM 3615 CG GLN A 155 2.498 -4.718 77.141 1.00 42.71 C ANISOU 3615 CG GLN A 155 6287 6751 3189 -633 72 134 C ATOM 3616 CD GLN A 155 2.266 -4.131 78.520 1.00 43.73 C ANISOU 3616 CD GLN A 155 6417 7020 3180 -647 99 91 C ATOM 3617 OE1 GLN A 155 2.253 -4.853 79.518 1.00 44.59 O ANISOU 3617 OE1 GLN A 155 6551 7202 3188 -717 82 166 O ATOM 3618 NE2 GLN A 155 2.064 -2.821 78.580 1.00 43.56 N ANISOU 3618 NE2 GLN A 155 6371 7031 3147 -578 134 -30 N ATOM 3619 N SER A 156 -1.782 -4.344 76.122 1.00 42.75 N ANISOU 3619 N SER A 156 6094 7012 3139 -663 305 81 N ATOM 3620 CA SER A 156 -3.031 -4.092 75.414 1.00 42.33 C ANISOU 3620 CA SER A 156 5965 7013 3106 -650 371 52 C ATOM 3621 C SER A 156 -3.328 -2.598 75.324 1.00 41.93 C ANISOU 3621 C SER A 156 5874 7000 3058 -538 418 -91 C ATOM 3622 O SER A 156 -3.159 -1.869 76.299 1.00 42.76 O ANISOU 3622 O SER A 156 5987 7184 3074 -499 429 -161 O ATOM 3623 CB SER A 156 -4.181 -4.801 76.132 1.00 43.31 C ANISOU 3623 CB SER A 156 6037 7307 3110 -746 417 131 C ATOM 3624 OG SER A 156 -5.308 -4.889 75.291 1.00 43.12 O ANISOU 3624 OG SER A 156 5942 7317 3123 -757 462 139 O ATOM 3625 N GLY A 157 -3.760 -2.153 74.150 1.00 41.03 N ANISOU 3625 N GLY A 157 5723 6821 3043 -485 437 -136 N ATOM 3626 CA GLY A 157 -4.188 -0.774 73.944 1.00 41.20 C ANISOU 3626 CA GLY A 157 5710 6869 3076 -378 474 -267 C ATOM 3627 C GLY A 157 -3.108 0.293 73.874 1.00 40.86 C ANISOU 3627 C GLY A 157 5725 6713 3086 -300 423 -356 C ATOM 3628 O GLY A 157 -3.437 1.474 73.805 1.00 41.25 O ANISOU 3628 O GLY A 157 5762 6773 3139 -211 438 -467 O ATOM 3629 N ASN A 158 -1.833 -0.105 73.860 1.00 40.47 N ANISOU 3629 N ASN A 158 5740 6556 3082 -331 355 -306 N ATOM 3630 CA ASN A 158 -0.706 0.839 73.901 1.00 40.44 C ANISOU 3630 CA ASN A 158 5788 6459 3118 -280 297 -372 C ATOM 3631 C ASN A 158 0.330 0.588 72.796 1.00 39.52 C ANISOU 3631 C ASN A 158 5694 6191 3130 -285 240 -324 C ATOM 3632 O ASN A 158 1.505 0.947 72.943 1.00 39.40 O ANISOU 3632 O ASN A 158 5721 6110 3139 -279 179 -332 O ATOM 3633 CB ASN A 158 -0.040 0.810 75.284 1.00 41.40 C ANISOU 3633 CB ASN A 158 5958 6639 3134 -306 266 -371 C ATOM 3634 CG ASN A 158 0.496 -0.566 75.663 1.00 41.58 C ANISOU 3634 CG ASN A 158 6005 6663 3132 -394 238 -246 C ATOM 3635 OD1 ASN A 158 0.215 -1.575 75.009 1.00 41.07 O ANISOU 3635 OD1 ASN A 158 5924 6569 3113 -439 244 -161 O ATOM 3636 ND2 ASN A 158 1.257 -0.610 76.748 1.00 42.23 N ANISOU 3636 ND2 ASN A 158 6133 6776 3137 -417 198 -236 N ATOM 3637 N SER A 159 -0.114 -0.019 71.693 1.00 38.90 N ANISOU 3637 N SER A 159 5584 6070 3128 -297 259 -277 N ATOM 3638 CA SER A 159 0.737 -0.247 70.529 1.00 37.82 C ANISOU 3638 CA SER A 159 5456 5808 3104 -288 214 -240 C ATOM 3639 C SER A 159 -0.018 0.006 69.231 1.00 37.36 C ANISOU 3639 C SER A 159 5355 5711 3129 -256 246 -261 C ATOM 3640 O SER A 159 -1.246 -0.027 69.201 1.00 37.61 O ANISOU 3640 O SER A 159 5346 5811 3133 -257 300 -276 O ATOM 3641 CB SER A 159 1.328 -1.662 70.546 1.00 37.43 C ANISOU 3641 CB SER A 159 5436 5729 3057 -342 179 -135 C ATOM 3642 OG SER A 159 0.326 -2.649 70.375 1.00 37.40 O ANISOU 3642 OG SER A 159 5416 5760 3036 -389 211 -77 O ATOM 3643 N GLN A 160 0.736 0.287 68.171 1.00 36.94 N ANISOU 3643 N GLN A 160 5305 5560 3172 -228 209 -259 N ATOM 3644 CA GLN A 160 0.185 0.470 66.824 1.00 36.47 C ANISOU 3644 CA GLN A 160 5208 5452 3195 -199 229 -269 C ATOM 3645 C GLN A 160 1.067 -0.258 65.817 1.00 36.19 C ANISOU 3645 C GLN A 160 5181 5338 3233 -203 190 -206 C ATOM 3646 O GLN A 160 2.282 -0.323 65.988 1.00 36.03 O ANISOU 3646 O GLN A 160 5184 5288 3219 -202 142 -183 O ATOM 3647 CB GLN A 160 0.078 1.959 66.462 1.00 36.22 C ANISOU 3647 CB GLN A 160 5167 5393 3203 -144 224 -354 C ATOM 3648 CG GLN A 160 -1.058 2.690 67.175 1.00 37.03 C ANISOU 3648 CG GLN A 160 5253 5574 3242 -111 268 -433 C ATOM 3649 CD GLN A 160 -1.293 4.097 66.644 1.00 37.02 C ANISOU 3649 CD GLN A 160 5250 5525 3291 -45 252 -517 C ATOM 3650 OE1 GLN A 160 -2.414 4.457 66.284 1.00 36.95 O ANISOU 3650 OE1 GLN A 160 5203 5547 3288 -5 292 -560 O ATOM 3651 NE2 GLN A 160 -0.230 4.895 66.578 1.00 37.09 N ANISOU 3651 NE2 GLN A 160 5301 5456 3337 -38 187 -536 N ATOM 3652 N GLU A 161 0.434 -0.806 64.782 1.00 36.57 N ANISOU 3652 N GLU A 161 5206 5361 3328 -202 210 -182 N ATOM 3653 CA GLU A 161 1.114 -1.557 63.727 1.00 36.40 C ANISOU 3653 CA GLU A 161 5191 5272 3367 -190 178 -133 C ATOM 3654 C GLU A 161 1.043 -0.860 62.378 1.00 36.03 C ANISOU 3654 C GLU A 161 5109 5182 3398 -149 183 -161 C ATOM 3655 O GLU A 161 0.123 -0.081 62.106 1.00 35.84 O ANISOU 3655 O GLU A 161 5056 5172 3389 -137 216 -207 O ATOM 3656 CB GLU A 161 0.500 -2.948 63.568 1.00 36.83 C ANISOU 3656 CB GLU A 161 5263 5321 3408 -227 180 -74 C ATOM 3657 CG GLU A 161 1.109 -4.003 64.468 1.00 37.67 C ANISOU 3657 CG GLU A 161 5422 5428 3463 -262 140 -15 C ATOM 3658 CD GLU A 161 0.453 -5.358 64.301 1.00 38.12 C ANISOU 3658 CD GLU A 161 5510 5463 3510 -308 125 48 C ATOM 3659 OE1 GLU A 161 -0.139 -5.620 63.230 1.00 38.02 O ANISOU 3659 OE1 GLU A 161 5485 5415 3546 -301 132 49 O ATOM 3660 OE2 GLU A 161 0.532 -6.166 65.247 1.00 39.04 O ANISOU 3660 OE2 GLU A 161 5669 5595 3568 -359 98 101 O ATOM 3661 N SER A 162 2.023 -1.184 61.538 1.00 35.95 N ANISOU 3661 N SER A 162 5099 5127 3432 -125 148 -131 N ATOM 3662 CA SER A 162 2.048 -0.787 60.142 1.00 35.67 C ANISOU 3662 CA SER A 162 5031 5060 3463 -91 149 -139 C ATOM 3663 C SER A 162 2.654 -1.920 59.330 1.00 35.57 C ANISOU 3663 C SER A 162 5027 5018 3468 -66 122 -94 C ATOM 3664 O SER A 162 3.709 -2.444 59.699 1.00 35.63 O ANISOU 3664 O SER A 162 5053 5028 3456 -54 86 -64 O ATOM 3665 CB SER A 162 2.895 0.473 59.976 1.00 35.94 C ANISOU 3665 CB SER A 162 5044 5088 3523 -78 124 -161 C ATOM 3666 OG SER A 162 2.851 0.930 58.644 1.00 35.95 O ANISOU 3666 OG SER A 162 5011 5066 3582 -55 125 -162 O ATOM 3667 N VAL A 163 1.988 -2.304 58.240 1.00 35.61 N ANISOU 3667 N VAL A 163 5023 5000 3509 -52 136 -93 N ATOM 3668 CA VAL A 163 2.518 -3.306 57.311 1.00 35.44 C ANISOU 3668 CA VAL A 163 5015 4947 3503 -12 107 -65 C ATOM 3669 C VAL A 163 2.778 -2.628 55.977 1.00 35.14 C ANISOU 3669 C VAL A 163 4929 4911 3511 27 113 -78 C ATOM 3670 O VAL A 163 1.932 -1.874 55.490 1.00 34.87 O ANISOU 3670 O VAL A 163 4868 4875 3505 15 141 -103 O ATOM 3671 CB VAL A 163 1.549 -4.486 57.072 1.00 35.72 C ANISOU 3671 CB VAL A 163 5092 4948 3535 -31 103 -47 C ATOM 3672 CG1 VAL A 163 2.309 -5.682 56.516 1.00 36.02 C ANISOU 3672 CG1 VAL A 163 5172 4943 3572 20 52 -23 C ATOM 3673 CG2 VAL A 163 0.841 -4.889 58.355 1.00 36.41 C ANISOU 3673 CG2 VAL A 163 5209 5050 3573 -97 112 -29 C ATOM 3674 N THR A 164 3.946 -2.904 55.392 1.00 35.05 N ANISOU 3674 N THR A 164 4903 4913 3502 78 84 -60 N ATOM 3675 CA THR A 164 4.256 -2.487 54.024 1.00 34.76 C ANISOU 3675 CA THR A 164 4818 4894 3495 116 87 -62 C ATOM 3676 C THR A 164 3.415 -3.276 53.025 1.00 34.54 C ANISOU 3676 C THR A 164 4812 4832 3482 140 93 -71 C ATOM 3677 O THR A 164 2.854 -4.327 53.346 1.00 34.53 O ANISOU 3677 O THR A 164 4866 4787 3466 132 80 -68 O ATOM 3678 CB THR A 164 5.742 -2.723 53.659 1.00 34.85 C ANISOU 3678 CB THR A 164 4797 4956 3489 172 57 -37 C ATOM 3679 OG1 THR A 164 6.138 -4.027 54.097 1.00 35.74 O ANISOU 3679 OG1 THR A 164 4959 5050 3571 213 26 -28 O ATOM 3680 CG2 THR A 164 6.643 -1.683 54.295 1.00 34.92 C ANISOU 3680 CG2 THR A 164 4765 5011 3492 139 45 -21 C ATOM 3681 N GLU A 165 3.341 -2.748 51.811 1.00 34.60 N ANISOU 3681 N GLU A 165 4776 4855 3514 161 105 -78 N ATOM 3682 CA GLU A 165 2.799 -3.480 50.674 1.00 35.03 C ANISOU 3682 CA GLU A 165 4846 4886 3577 196 102 -87 C ATOM 3683 C GLU A 165 3.817 -4.543 50.275 1.00 35.19 C ANISOU 3683 C GLU A 165 4886 4919 3567 276 65 -82 C ATOM 3684 O GLU A 165 4.981 -4.483 50.692 1.00 34.88 O ANISOU 3684 O GLU A 165 4823 4925 3505 305 51 -67 O ATOM 3685 CB GLU A 165 2.519 -2.531 49.501 1.00 35.13 C ANISOU 3685 CB GLU A 165 4804 4924 3619 197 122 -92 C ATOM 3686 CG GLU A 165 1.483 -1.448 49.797 1.00 35.38 C ANISOU 3686 CG GLU A 165 4820 4938 3684 137 149 -105 C ATOM 3687 CD GLU A 165 0.152 -2.020 50.254 1.00 35.81 C ANISOU 3687 CD GLU A 165 4913 4952 3742 103 162 -121 C ATOM 3688 OE1 GLU A 165 -0.412 -2.862 49.525 1.00 35.89 O ANISOU 3688 OE1 GLU A 165 4946 4937 3754 115 153 -123 O ATOM 3689 OE2 GLU A 165 -0.321 -1.646 51.351 1.00 36.65 O ANISOU 3689 OE2 GLU A 165 5025 5057 3842 63 178 -130 O ATOM 3690 N GLN A 166 3.380 -5.518 49.479 1.00 35.20 N ANISOU 3690 N GLN A 166 4931 4881 3564 316 45 -98 N ATOM 3691 CA GLN A 166 4.257 -6.619 49.075 1.00 35.64 C ANISOU 3691 CA GLN A 166 5019 4937 3586 412 1 -107 C ATOM 3692 C GLN A 166 5.411 -6.074 48.234 1.00 36.41 C ANISOU 3692 C GLN A 166 5034 5138 3663 481 13 -105 C ATOM 3693 O GLN A 166 5.191 -5.230 47.364 1.00 36.79 O ANISOU 3693 O GLN A 166 5025 5230 3726 465 43 -103 O ATOM 3694 CB GLN A 166 3.485 -7.695 48.307 1.00 35.30 C ANISOU 3694 CB GLN A 166 5049 4820 3542 441 -34 -132 C ATOM 3695 CG GLN A 166 4.233 -9.014 48.195 1.00 35.66 C ANISOU 3695 CG GLN A 166 5164 4833 3552 541 -99 -150 C ATOM 3696 CD GLN A 166 3.398 -10.127 47.593 1.00 35.67 C ANISOU 3696 CD GLN A 166 5262 4736 3555 555 -152 -174 C ATOM 3697 OE1 GLN A 166 2.454 -9.878 46.850 1.00 35.16 O ANISOU 3697 OE1 GLN A 166 5191 4657 3511 516 -134 -184 O ATOM 3698 NE2 GLN A 166 3.753 -11.365 47.898 1.00 36.28 N ANISOU 3698 NE2 GLN A 166 5434 4740 3610 612 -227 -184 N ATOM 3699 N ASP A 167 6.631 -6.523 48.525 1.00 37.48 N ANISOU 3699 N ASP A 167 5157 5320 3762 552 -14 -99 N ATOM 3700 CA ASP A 167 7.821 -6.088 47.794 1.00 38.23 C ANISOU 3700 CA ASP A 167 5159 5541 3825 618 -4 -88 C ATOM 3701 C ASP A 167 7.977 -6.963 46.561 1.00 38.83 C ANISOU 3701 C ASP A 167 5249 5638 3866 734 -23 -126 C ATOM 3702 O ASP A 167 8.019 -8.183 46.670 1.00 39.12 O ANISOU 3702 O ASP A 167 5367 5612 3884 810 -71 -158 O ATOM 3703 CB ASP A 167 9.066 -6.195 48.683 1.00 39.57 C ANISOU 3703 CB ASP A 167 5299 5769 3966 649 -25 -64 C ATOM 3704 CG ASP A 167 10.344 -5.725 47.989 1.00 40.75 C ANISOU 3704 CG ASP A 167 5333 6074 4075 708 -15 -41 C ATOM 3705 OD1 ASP A 167 10.280 -4.872 47.078 1.00 41.85 O ANISOU 3705 OD1 ASP A 167 5403 6282 4217 679 17 -24 O ATOM 3706 OD2 ASP A 167 11.430 -6.217 48.358 1.00 42.34 O ANISOU 3706 OD2 ASP A 167 5510 6338 4237 782 -42 -34 O ATOM 3707 N SER A 168 8.063 -6.335 45.390 1.00 39.00 N ANISOU 3707 N SER A 168 5197 5745 3875 748 8 -123 N ATOM 3708 CA SER A 168 8.267 -7.062 44.131 1.00 39.51 C ANISOU 3708 CA SER A 168 5265 5854 3893 866 -6 -164 C ATOM 3709 C SER A 168 9.618 -7.781 44.074 1.00 40.09 C ANISOU 3709 C SER A 168 5308 6022 3901 1004 -33 -180 C ATOM 3710 O SER A 168 9.725 -8.820 43.427 1.00 41.30 O ANISOU 3710 O SER A 168 5513 6164 4015 1127 -69 -235 O ATOM 3711 CB SER A 168 8.138 -6.113 42.940 1.00 39.59 C ANISOU 3711 CB SER A 168 5189 5957 3895 841 36 -146 C ATOM 3712 OG SER A 168 9.076 -5.054 43.036 1.00 40.13 O ANISOU 3712 OG SER A 168 5144 6155 3950 802 63 -88 O ATOM 3713 N LYS A 169 10.633 -7.228 44.747 1.00 39.62 N ANISOU 3713 N LYS A 169 5167 6057 3830 987 -22 -135 N ATOM 3714 CA LYS A 169 11.982 -7.823 44.793 1.00 39.90 C ANISOU 3714 CA LYS A 169 5153 6205 3802 1117 -46 -142 C ATOM 3715 C LYS A 169 11.998 -9.269 45.283 1.00 39.81 C ANISOU 3715 C LYS A 169 5261 6083 3780 1223 -113 -196 C ATOM 3716 O LYS A 169 12.695 -10.089 44.699 1.00 41.43 O ANISOU 3716 O LYS A 169 5464 6351 3927 1381 -143 -241 O ATOM 3717 CB LYS A 169 12.929 -6.984 45.663 1.00 39.87 C ANISOU 3717 CB LYS A 169 5054 6297 3798 1052 -33 -76 C ATOM 3718 N ASP A 170 11.247 -9.575 46.346 1.00 38.29 N ANISOU 3718 N ASP A 170 5174 5734 3641 1141 -140 -190 N ATOM 3719 CA ASP A 170 11.192 -10.946 46.897 1.00 37.94 C ANISOU 3719 CA ASP A 170 5258 5566 3591 1218 -217 -226 C ATOM 3720 C ASP A 170 9.799 -11.479 47.317 1.00 37.04 C ANISOU 3720 C ASP A 170 5282 5264 3527 1126 -249 -233 C ATOM 3721 O ASP A 170 9.720 -12.547 47.930 1.00 37.53 O ANISOU 3721 O ASP A 170 5457 5212 3589 1159 -321 -245 O ATOM 3722 CB ASP A 170 12.187 -11.067 48.067 1.00 38.22 C ANISOU 3722 CB ASP A 170 5273 5635 3614 1236 -243 -194 C ATOM 3723 CG ASP A 170 11.861 -10.136 49.243 1.00 37.39 C ANISOU 3723 CG ASP A 170 5147 5505 3553 1069 -210 -134 C ATOM 3724 OD1 ASP A 170 10.803 -9.463 49.243 1.00 36.20 O ANISOU 3724 OD1 ASP A 170 5010 5300 3446 946 -170 -121 O ATOM 3725 OD2 ASP A 170 12.679 -10.081 50.185 1.00 37.51 O ANISOU 3725 OD2 ASP A 170 5136 5560 3557 1069 -227 -103 O ATOM 3726 N SER A 171 8.727 -10.754 46.978 1.00 35.66 N ANISOU 3726 N SER A 171 5096 5062 3392 1012 -201 -221 N ATOM 3727 CA SER A 171 7.333 -11.126 47.292 1.00 34.86 C ANISOU 3727 CA SER A 171 5099 4814 3334 912 -222 -220 C ATOM 3728 C SER A 171 7.025 -11.253 48.790 1.00 34.27 C ANISOU 3728 C SER A 171 5076 4662 3282 812 -238 -178 C ATOM 3729 O SER A 171 6.148 -12.028 49.179 1.00 34.30 O ANISOU 3729 O SER A 171 5185 4545 3303 760 -284 -173 O ATOM 3730 CB SER A 171 6.928 -12.402 46.540 1.00 35.68 C ANISOU 3730 CB SER A 171 5317 4817 3421 997 -295 -272 C ATOM 3731 OG SER A 171 7.001 -12.223 45.139 1.00 36.11 O ANISOU 3731 OG SER A 171 5327 4942 3450 1074 -274 -314 O ATOM 3732 N THR A 172 7.718 -10.470 49.618 1.00 33.57 N ANISOU 3732 N THR A 172 4912 4650 3192 776 -204 -142 N ATOM 3733 CA THR A 172 7.553 -10.519 51.081 1.00 33.40 C ANISOU 3733 CA THR A 172 4931 4578 3180 689 -216 -104 C ATOM 3734 C THR A 172 6.874 -9.267 51.635 1.00 32.64 C ANISOU 3734 C THR A 172 4780 4509 3115 556 -149 -77 C ATOM 3735 O THR A 172 6.666 -8.289 50.917 1.00 32.15 O ANISOU 3735 O THR A 172 4643 4502 3069 534 -97 -83 O ATOM 3736 CB THR A 172 8.912 -10.698 51.798 1.00 33.79 C ANISOU 3736 CB THR A 172 4955 4686 3198 756 -245 -88 C ATOM 3737 OG1 THR A 172 9.770 -9.578 51.535 1.00 33.43 O ANISOU 3737 OG1 THR A 172 4781 4778 3144 765 -194 -75 O ATOM 3738 CG2 THR A 172 9.592 -11.972 51.356 1.00 34.61 C ANISOU 3738 CG2 THR A 172 5121 4760 3269 906 -321 -121 C ATOM 3739 N TYR A 173 6.520 -9.325 52.916 1.00 32.87 N ANISOU 3739 N TYR A 173 4849 4495 3144 473 -156 -48 N ATOM 3740 CA TYR A 173 6.028 -8.172 53.672 1.00 32.46 C ANISOU 3740 CA TYR A 173 4750 4475 3107 365 -100 -30 C ATOM 3741 C TYR A 173 6.953 -7.908 54.847 1.00 32.91 C ANISOU 3741 C TYR A 173 4790 4573 3140 354 -111 -5 C ATOM 3742 O TYR A 173 7.720 -8.782 55.270 1.00 33.86 O ANISOU 3742 O TYR A 173 4950 4680 3235 410 -165 7 O ATOM 3743 CB TYR A 173 4.629 -8.433 54.229 1.00 32.36 C ANISOU 3743 CB TYR A 173 4795 4394 3104 268 -93 -20 C ATOM 3744 CG TYR A 173 3.581 -8.740 53.193 1.00 32.26 C ANISOU 3744 CG TYR A 173 4805 4337 3116 261 -90 -38 C ATOM 3745 CD1 TYR A 173 3.361 -10.048 52.764 1.00 32.75 C ANISOU 3745 CD1 TYR A 173 4955 4317 3172 296 -154 -41 C ATOM 3746 CD2 TYR A 173 2.795 -7.727 52.648 1.00 31.88 C ANISOU 3746 CD2 TYR A 173 4697 4321 3097 219 -32 -53 C ATOM 3747 CE1 TYR A 173 2.392 -10.338 51.816 1.00 32.76 C ANISOU 3747 CE1 TYR A 173 4980 4275 3192 282 -159 -57 C ATOM 3748 CE2 TYR A 173 1.820 -8.005 51.697 1.00 31.84 C ANISOU 3748 CE2 TYR A 173 4707 4278 3112 209 -32 -67 C ATOM 3749 CZ TYR A 173 1.622 -9.314 51.289 1.00 32.38 C ANISOU 3749 CZ TYR A 173 4861 4271 3172 237 -95 -68 C ATOM 3750 OH TYR A 173 0.663 -9.599 50.344 1.00 32.56 O ANISOU 3750 OH TYR A 173 4903 4255 3212 222 -103 -82 O ATOM 3751 N SER A 174 6.871 -6.692 55.369 1.00 32.53 N ANISOU 3751 N SER A 174 4687 4572 3100 285 -68 0 N ATOM 3752 CA SER A 174 7.513 -6.337 56.625 1.00 32.75 C ANISOU 3752 CA SER A 174 4709 4632 3105 250 -78 22 C ATOM 3753 C SER A 174 6.507 -5.591 57.500 1.00 32.66 C ANISOU 3753 C SER A 174 4706 4608 3094 150 -40 16 C ATOM 3754 O SER A 174 5.587 -4.941 56.993 1.00 32.28 O ANISOU 3754 O SER A 174 4638 4555 3074 119 1 -6 O ATOM 3755 CB SER A 174 8.774 -5.514 56.376 1.00 32.66 C ANISOU 3755 CB SER A 174 4611 4708 3089 282 -78 30 C ATOM 3756 OG SER A 174 9.767 -6.314 55.754 1.00 33.10 O ANISOU 3756 OG SER A 174 4653 4797 3128 385 -114 36 O ATOM 3757 N LEU A 175 6.684 -5.710 58.815 1.00 33.19 N ANISOU 3757 N LEU A 175 4805 4679 3127 110 -56 34 N ATOM 3758 CA LEU A 175 5.731 -5.195 59.797 1.00 33.20 C ANISOU 3758 CA LEU A 175 4822 4683 3110 28 -23 26 C ATOM 3759 C LEU A 175 6.492 -4.508 60.932 1.00 33.67 C ANISOU 3759 C LEU A 175 4869 4787 3137 1 -34 29 C ATOM 3760 O LEU A 175 7.506 -5.026 61.402 1.00 33.66 O ANISOU 3760 O LEU A 175 4882 4797 3112 27 -79 58 O ATOM 3761 CB LEU A 175 4.863 -6.346 60.325 1.00 33.40 C ANISOU 3761 CB LEU A 175 4918 4665 3109 -11 -37 52 C ATOM 3762 CG LEU A 175 3.642 -6.023 61.210 1.00 33.48 C ANISOU 3762 CG LEU A 175 4935 4698 3088 -95 4 48 C ATOM 3763 CD1 LEU A 175 2.627 -7.160 61.181 1.00 33.68 C ANISOU 3763 CD1 LEU A 175 5012 4683 3101 -140 -8 83 C ATOM 3764 CD2 LEU A 175 4.034 -5.700 62.648 1.00 33.85 C ANISOU 3764 CD2 LEU A 175 4993 4790 3080 -133 0 57 C ATOM 3765 N SER A 176 6.009 -3.337 61.349 1.00 34.14 N ANISOU 3765 N SER A 176 4906 4870 3195 -43 -1 -3 N ATOM 3766 CA SER A 176 6.557 -2.625 62.509 1.00 35.06 C ANISOU 3766 CA SER A 176 5025 5022 3275 -75 -15 -9 C ATOM 3767 C SER A 176 5.483 -2.478 63.585 1.00 35.54 C ANISOU 3767 C SER A 176 5118 5097 3289 -127 16 -31 C ATOM 3768 O SER A 176 4.344 -2.117 63.281 1.00 35.34 O ANISOU 3768 O SER A 176 5082 5069 3276 -139 60 -63 O ATOM 3769 CB SER A 176 7.082 -1.248 62.107 1.00 35.14 C ANISOU 3769 CB SER A 176 4987 5048 3316 -76 -20 -34 C ATOM 3770 OG SER A 176 6.012 -0.381 61.777 1.00 35.85 O ANISOU 3770 OG SER A 176 5069 5122 3431 -90 19 -80 O ATOM 3771 N SER A 177 5.850 -2.768 64.832 1.00 35.96 N ANISOU 3771 N SER A 177 5205 5176 3282 -155 -7 -13 N ATOM 3772 CA SER A 177 4.952 -2.623 65.969 1.00 36.58 C ANISOU 3772 CA SER A 177 5308 5294 3297 -203 23 -31 C ATOM 3773 C SER A 177 5.605 -1.678 66.974 1.00 36.75 C ANISOU 3773 C SER A 177 5335 5349 3278 -216 2 -61 C ATOM 3774 O SER A 177 6.723 -1.935 67.432 1.00 37.06 O ANISOU 3774 O SER A 177 5388 5394 3301 -216 -48 -29 O ATOM 3775 CB SER A 177 4.669 -3.984 66.609 1.00 37.15 C ANISOU 3775 CB SER A 177 5426 5369 3319 -238 9 28 C ATOM 3776 OG SER A 177 3.743 -3.858 67.679 1.00 38.25 O ANISOU 3776 OG SER A 177 5577 5571 3386 -291 45 18 O ATOM 3777 N THR A 178 4.913 -0.584 67.298 1.00 36.36 N ANISOU 3777 N THR A 178 5278 5323 3213 -221 33 -126 N ATOM 3778 CA THR A 178 5.424 0.409 68.238 1.00 36.59 C ANISOU 3778 CA THR A 178 5326 5375 3202 -230 5 -169 C ATOM 3779 C THR A 178 4.640 0.351 69.542 1.00 36.99 C ANISOU 3779 C THR A 178 5404 5494 3156 -255 34 -195 C ATOM 3780 O THR A 178 3.435 0.557 69.544 1.00 36.88 O ANISOU 3780 O THR A 178 5376 5515 3123 -248 88 -234 O ATOM 3781 CB THR A 178 5.334 1.828 67.657 1.00 36.28 C ANISOU 3781 CB THR A 178 5270 5302 3212 -207 -1 -234 C ATOM 3782 OG1 THR A 178 6.069 1.875 66.433 1.00 35.99 O ANISOU 3782 OG1 THR A 178 5200 5220 3255 -194 -27 -199 O ATOM 3783 CG2 THR A 178 5.916 2.857 68.618 1.00 36.75 C ANISOU 3783 CG2 THR A 178 5364 5368 3231 -219 -49 -280 C ATOM 3784 N LEU A 179 5.343 0.060 70.635 1.00 37.33 N ANISOU 3784 N LEU A 179 5480 5569 3133 -282 -2 -171 N ATOM 3785 CA LEU A 179 4.804 0.159 71.989 1.00 37.74 C ANISOU 3785 CA LEU A 179 5559 5701 3078 -306 18 -199 C ATOM 3786 C LEU A 179 5.139 1.554 72.513 1.00 37.68 C ANISOU 3786 C LEU A 179 5572 5694 3050 -285 -12 -284 C ATOM 3787 O LEU A 179 6.310 1.923 72.555 1.00 37.72 O ANISOU 3787 O LEU A 179 5593 5660 3080 -293 -77 -274 O ATOM 3788 CB LEU A 179 5.444 -0.906 72.876 1.00 38.32 C ANISOU 3788 CB LEU A 179 5666 5803 3091 -349 -17 -123 C ATOM 3789 CG LEU A 179 4.906 -1.115 74.291 1.00 39.27 C ANISOU 3789 CG LEU A 179 5812 6022 3086 -388 3 -124 C ATOM 3790 CD1 LEU A 179 3.512 -1.734 74.261 1.00 39.49 C ANISOU 3790 CD1 LEU A 179 5816 6111 3077 -413 71 -104 C ATOM 3791 CD2 LEU A 179 5.872 -1.992 75.075 1.00 39.74 C ANISOU 3791 CD2 LEU A 179 5910 6087 3100 -426 -56 -47 C ATOM 3792 N THR A 180 4.123 2.324 72.893 1.00 37.72 N ANISOU 3792 N THR A 180 5579 5743 3009 -258 29 -367 N ATOM 3793 CA THR A 180 4.318 3.697 73.365 1.00 38.17 C ANISOU 3793 CA THR A 180 5671 5786 3046 -226 -8 -463 C ATOM 3794 C THR A 180 3.923 3.816 74.834 1.00 39.28 C ANISOU 3794 C THR A 180 5844 6027 3053 -225 6 -512 C ATOM 3795 O THR A 180 2.758 3.624 75.174 1.00 39.75 O ANISOU 3795 O THR A 180 5879 6178 3047 -207 75 -538 O ATOM 3796 CB THR A 180 3.500 4.697 72.531 1.00 37.82 C ANISOU 3796 CB THR A 180 5611 5701 3060 -168 13 -541 C ATOM 3797 OG1 THR A 180 3.887 4.589 71.158 1.00 36.61 O ANISOU 3797 OG1 THR A 180 5426 5463 3022 -173 -1 -491 O ATOM 3798 CG2 THR A 180 3.725 6.139 73.021 1.00 38.52 C ANISOU 3798 CG2 THR A 180 5755 5752 3130 -131 -46 -644 C ATOM 3799 N LEU A 181 4.907 4.124 75.682 1.00 39.76 N ANISOU 3799 N LEU A 181 5954 6083 3070 -247 -61 -519 N ATOM 3800 CA LEU A 181 4.714 4.330 77.117 1.00 40.93 C ANISOU 3800 CA LEU A 181 6143 6326 3084 -245 -61 -571 C ATOM 3801 C LEU A 181 5.252 5.701 77.522 1.00 41.40 C ANISOU 3801 C LEU A 181 6265 6332 3133 -214 -138 -670 C ATOM 3802 O LEU A 181 6.052 6.304 76.796 1.00 40.98 O ANISOU 3802 O LEU A 181 6224 6169 3177 -223 -205 -666 O ATOM 3803 CB LEU A 181 5.466 3.264 77.913 1.00 41.33 C ANISOU 3803 CB LEU A 181 6207 6422 3074 -312 -84 -477 C ATOM 3804 CG LEU A 181 5.184 1.788 77.627 1.00 41.11 C ANISOU 3804 CG LEU A 181 6141 6424 3055 -356 -41 -362 C ATOM 3805 CD1 LEU A 181 6.127 0.914 78.447 1.00 41.56 C ANISOU 3805 CD1 LEU A 181 6228 6503 3059 -413 -92 -276 C ATOM 3806 CD2 LEU A 181 3.734 1.434 77.923 1.00 41.60 C ANISOU 3806 CD2 LEU A 181 6169 6596 3040 -353 48 -374 C ATOM 3807 N SER A 182 4.830 6.179 78.691 1.00 42.22 N ANISOU 3807 N SER A 182 6410 6517 3115 -183 -134 -756 N ATOM 3808 CA SER A 182 5.454 7.350 79.320 1.00 42.82 C ANISOU 3808 CA SER A 182 6567 6544 3161 -163 -225 -848 C ATOM 3809 C SER A 182 6.825 6.960 79.872 1.00 42.62 C ANISOU 3809 C SER A 182 6570 6502 3122 -241 -302 -772 C ATOM 3810 O SER A 182 7.092 5.776 80.090 1.00 42.11 O ANISOU 3810 O SER A 182 6472 6494 3034 -293 -274 -669 O ATOM 3811 CB SER A 182 4.577 7.880 80.444 1.00 44.17 C ANISOU 3811 CB SER A 182 6772 6821 3188 -94 -195 -968 C ATOM 3812 OG SER A 182 4.377 6.880 81.426 1.00 44.77 O ANISOU 3812 OG SER A 182 6826 7041 3143 -132 -142 -913 O ATOM 3813 N LYS A 183 7.688 7.952 80.089 1.00 43.08 N ANISOU 3813 N LYS A 183 6693 6480 3195 -251 -408 -820 N ATOM 3814 CA LYS A 183 9.034 7.708 80.634 1.00 43.30 C ANISOU 3814 CA LYS A 183 6745 6497 3209 -326 -492 -753 C ATOM 3815 C LYS A 183 8.963 7.030 82.010 1.00 44.15 C ANISOU 3815 C LYS A 183 6873 6730 3170 -342 -471 -743 C ATOM 3816 O LYS A 183 9.744 6.115 82.298 1.00 43.92 O ANISOU 3816 O LYS A 183 6826 6731 3131 -403 -489 -639 O ATOM 3817 CB LYS A 183 9.856 9.009 80.712 1.00 43.94 C ANISOU 3817 CB LYS A 183 6900 6477 3320 -342 -618 -814 C ATOM 3818 CG LYS A 183 11.129 8.894 81.545 1.00 44.64 C ANISOU 3818 CG LYS A 183 7021 6578 3364 -415 -712 -765 C ATOM 3819 CD LYS A 183 11.987 10.151 81.513 1.00 45.41 C ANISOU 3819 CD LYS A 183 7185 6567 3501 -451 -849 -808 C ATOM 3820 CE LYS A 183 12.766 10.299 82.812 1.00 46.78 C ANISOU 3820 CE LYS A 183 7426 6778 3571 -495 -936 -824 C ATOM 3821 NZ LYS A 183 13.744 11.419 82.792 1.00 47.78 N ANISOU 3821 NZ LYS A 183 7616 6799 3739 -555 -1086 -844 N ATOM 3822 N ALA A 184 8.032 7.488 82.849 1.00 45.06 N ANISOU 3822 N ALA A 184 7027 6924 3169 -283 -434 -853 N ATOM 3823 CA ALA A 184 7.794 6.884 84.159 1.00 45.91 C ANISOU 3823 CA ALA A 184 7149 7174 3121 -295 -402 -848 C ATOM 3824 C ALA A 184 7.466 5.394 84.047 1.00 45.32 C ANISOU 3824 C ALA A 184 7001 7182 3036 -342 -319 -719 C ATOM 3825 O ALA A 184 8.191 4.567 84.592 1.00 45.42 O ANISOU 3825 O ALA A 184 7018 7227 3012 -407 -348 -624 O ATOM 3826 CB ALA A 184 6.685 7.620 84.889 1.00 47.14 C ANISOU 3826 CB ALA A 184 7337 7421 3154 -206 -359 -992 C ATOM 3827 N ASP A 185 6.398 5.062 83.320 1.00 44.88 N ANISOU 3827 N ASP A 185 6885 7151 3017 -311 -226 -712 N ATOM 3828 CA ASP A 185 6.007 3.659 83.091 1.00 44.44 C ANISOU 3828 CA ASP A 185 6767 7154 2963 -361 -158 -587 C ATOM 3829 C ASP A 185 7.140 2.829 82.501 1.00 43.82 C ANISOU 3829 C ASP A 185 6679 6984 2987 -422 -212 -462 C ATOM 3830 O ASP A 185 7.350 1.689 82.915 1.00 43.99 O ANISOU 3830 O ASP A 185 6694 7052 2968 -478 -210 -358 O ATOM 3831 CB ASP A 185 4.780 3.562 82.174 1.00 43.74 C ANISOU 3831 CB ASP A 185 6615 7078 2925 -321 -67 -601 C ATOM 3832 CG ASP A 185 3.485 3.948 82.870 1.00 44.76 C ANISOU 3832 CG ASP A 185 6727 7354 2925 -266 10 -692 C ATOM 3833 OD1 ASP A 185 3.501 4.262 84.079 1.00 46.21 O ANISOU 3833 OD1 ASP A 185 6949 7636 2971 -254 -2 -749 O ATOM 3834 OD2 ASP A 185 2.434 3.942 82.199 1.00 44.33 O ANISOU 3834 OD2 ASP A 185 6615 7328 2902 -229 83 -710 O ATOM 3835 N TYR A 186 7.874 3.407 81.553 1.00 43.43 N ANISOU 3835 N TYR A 186 6628 6809 3065 -409 -266 -472 N ATOM 3836 CA TYR A 186 9.008 2.723 80.946 1.00 42.98 C ANISOU 3836 CA TYR A 186 6550 6680 3101 -450 -319 -364 C ATOM 3837 C TYR A 186 10.095 2.387 81.976 1.00 44.06 C ANISOU 3837 C TYR A 186 6725 6848 3170 -499 -395 -314 C ATOM 3838 O TYR A 186 10.583 1.256 82.028 1.00 44.03 O ANISOU 3838 O TYR A 186 6705 6854 3170 -533 -409 -207 O ATOM 3839 CB TYR A 186 9.611 3.533 79.789 1.00 42.16 C ANISOU 3839 CB TYR A 186 6430 6462 3129 -432 -365 -385 C ATOM 3840 CG TYR A 186 10.813 2.839 79.187 1.00 41.51 C ANISOU 3840 CG TYR A 186 6312 6332 3127 -463 -416 -277 C ATOM 3841 CD1 TYR A 186 10.672 1.607 78.550 1.00 40.93 C ANISOU 3841 CD1 TYR A 186 6196 6258 3098 -462 -374 -189 C ATOM 3842 CD2 TYR A 186 12.095 3.385 79.288 1.00 41.65 C ANISOU 3842 CD2 TYR A 186 6338 6315 3171 -492 -511 -264 C ATOM 3843 CE1 TYR A 186 11.765 0.942 78.020 1.00 40.59 C ANISOU 3843 CE1 TYR A 186 6121 6182 3120 -470 -423 -101 C ATOM 3844 CE2 TYR A 186 13.194 2.731 78.750 1.00 41.26 C ANISOU 3844 CE2 TYR A 186 6243 6249 3186 -510 -554 -167 C ATOM 3845 CZ TYR A 186 13.021 1.509 78.121 1.00 40.82 C ANISOU 3845 CZ TYR A 186 6146 6195 3170 -489 -507 -91 C ATOM 3846 OH TYR A 186 14.092 0.843 77.580 1.00 40.81 O ANISOU 3846 OH TYR A 186 6098 6183 3225 -485 -551 -5 O ATOM 3847 N GLU A 187 10.464 3.365 82.796 1.00 45.40 N ANISOU 3847 N GLU A 187 6948 7029 3275 -498 -453 -393 N ATOM 3848 CA GLU A 187 11.518 3.157 83.803 1.00 46.55 C ANISOU 3848 CA GLU A 187 7131 7206 3352 -547 -534 -352 C ATOM 3849 C GLU A 187 11.095 2.317 85.024 1.00 47.53 C ANISOU 3849 C GLU A 187 7277 7451 3332 -573 -502 -317 C ATOM 3850 O GLU A 187 11.955 1.892 85.787 1.00 48.17 O ANISOU 3850 O GLU A 187 7383 7561 3361 -617 -566 -258 O ATOM 3851 CB GLU A 187 12.142 4.499 84.220 1.00 47.34 C ANISOU 3851 CB GLU A 187 7287 7264 3436 -547 -624 -444 C ATOM 3852 CG GLU A 187 13.129 5.002 83.171 1.00 46.72 C ANISOU 3852 CG GLU A 187 7180 7077 3495 -565 -695 -414 C ATOM 3853 CD GLU A 187 13.470 6.475 83.277 1.00 47.36 C ANISOU 3853 CD GLU A 187 7320 7090 3585 -568 -782 -511 C ATOM 3854 OE1 GLU A 187 13.272 7.090 84.346 1.00 48.38 O ANISOU 3854 OE1 GLU A 187 7525 7251 3607 -560 -815 -600 O ATOM 3855 OE2 GLU A 187 13.958 7.017 82.264 1.00 47.20 O ANISOU 3855 OE2 GLU A 187 7271 6982 3679 -582 -823 -495 O ATOM 3856 N LYS A 188 9.793 2.061 85.185 1.00 47.98 N ANISOU 3856 N LYS A 188 7320 7587 3323 -552 -407 -343 N ATOM 3857 CA LYS A 188 9.273 1.174 86.244 1.00 49.03 C ANISOU 3857 CA LYS A 188 7462 7851 3317 -591 -368 -290 C ATOM 3858 C LYS A 188 9.357 -0.344 85.962 1.00 48.52 C ANISOU 3858 C LYS A 188 7369 7783 3285 -644 -357 -139 C ATOM 3859 O LYS A 188 9.022 -1.141 86.845 1.00 49.40 O ANISOU 3859 O LYS A 188 7492 7994 3283 -693 -341 -75 O ATOM 3860 CB LYS A 188 7.810 1.532 86.561 1.00 49.99 C ANISOU 3860 CB LYS A 188 7567 8085 3342 -552 -270 -374 C ATOM 3861 CG LYS A 188 7.638 2.827 87.334 1.00 51.23 C ANISOU 3861 CG LYS A 188 7774 8289 3403 -496 -287 -524 C ATOM 3862 CD LYS A 188 6.194 3.306 87.296 1.00 51.93 C ANISOU 3862 CD LYS A 188 7830 8470 3431 -426 -189 -622 C ATOM 3863 CE LYS A 188 6.074 4.687 87.915 1.00 53.25 C ANISOU 3863 CE LYS A 188 8058 8655 3520 -345 -220 -790 C ATOM 3864 NZ LYS A 188 4.663 5.071 88.199 1.00 54.33 N ANISOU 3864 NZ LYS A 188 8162 8931 3552 -264 -124 -890 N ATOM 3865 N HIS A 189 9.770 -0.749 84.757 1.00 47.20 N ANISOU 3865 N HIS A 189 7167 7503 3262 -634 -371 -84 N ATOM 3866 CA HIS A 189 9.862 -2.173 84.396 1.00 46.72 C ANISOU 3866 CA HIS A 189 7093 7417 3242 -668 -374 47 C ATOM 3867 C HIS A 189 11.211 -2.509 83.761 1.00 46.10 C ANISOU 3867 C HIS A 189 7007 7236 3273 -656 -457 108 C ATOM 3868 O HIS A 189 11.873 -1.634 83.202 1.00 45.72 O ANISOU 3868 O HIS A 189 6942 7129 3302 -623 -489 54 O ATOM 3869 CB HIS A 189 8.740 -2.542 83.434 1.00 45.99 C ANISOU 3869 CB HIS A 189 6958 7307 3208 -655 -293 55 C ATOM 3870 CG HIS A 189 7.366 -2.251 83.954 1.00 46.64 C ANISOU 3870 CG HIS A 189 7027 7510 3186 -661 -205 1 C ATOM 3871 ND1 HIS A 189 6.682 -1.098 83.634 1.00 46.49 N ANISOU 3871 ND1 HIS A 189 6984 7504 3175 -602 -153 -121 N ATOM 3872 CD2 HIS A 189 6.541 -2.966 84.756 1.00 47.41 C ANISOU 3872 CD2 HIS A 189 7124 7726 3162 -718 -163 57 C ATOM 3873 CE1 HIS A 189 5.497 -1.114 84.217 1.00 47.23 C ANISOU 3873 CE1 HIS A 189 7058 7731 3157 -610 -77 -146 C ATOM 3874 NE2 HIS A 189 5.388 -2.236 84.905 1.00 47.84 N ANISOU 3874 NE2 HIS A 189 7144 7881 3151 -687 -80 -35 N ATOM 3875 N LYS A 190 11.599 -3.783 83.840 1.00 46.33 N ANISOU 3875 N LYS A 190 7048 7248 3306 -682 -495 222 N ATOM 3876 CA LYS A 190 12.916 -4.252 83.374 1.00 46.23 C ANISOU 3876 CA LYS A 190 7026 7161 3378 -658 -578 285 C ATOM 3877 C LYS A 190 12.857 -4.908 81.989 1.00 45.35 C ANISOU 3877 C LYS A 190 6878 6960 3391 -613 -563 323 C ATOM 3878 O LYS A 190 13.521 -4.453 81.054 1.00 44.26 O ANISOU 3878 O LYS A 190 6696 6768 3352 -564 -580 298 O ATOM 3879 CB LYS A 190 13.516 -5.241 84.382 1.00 46.93 C ANISOU 3879 CB LYS A 190 7160 7282 3390 -697 -650 383 C ATOM 3880 N VAL A 191 12.050 -5.966 81.873 1.00 45.77 N ANISOU 3880 N VAL A 191 6953 7003 3433 -634 -535 385 N ATOM 3881 CA VAL A 191 12.041 -6.840 80.690 1.00 45.54 C ANISOU 3881 CA VAL A 191 6911 6883 3508 -593 -541 433 C ATOM 3882 C VAL A 191 10.968 -6.397 79.702 1.00 45.04 C ANISOU 3882 C VAL A 191 6811 6800 3503 -577 -453 373 C ATOM 3883 O VAL A 191 9.779 -6.422 80.023 1.00 45.31 O ANISOU 3883 O VAL A 191 6853 6886 3478 -623 -391 364 O ATOM 3884 CB VAL A 191 11.784 -8.332 81.047 1.00 46.13 C ANISOU 3884 CB VAL A 191 7046 6935 3548 -631 -581 543 C ATOM 3885 CG1 VAL A 191 12.160 -9.238 79.874 1.00 45.63 C ANISOU 3885 CG1 VAL A 191 6983 6760 3594 -566 -622 586 C ATOM 3886 CG2 VAL A 191 12.548 -8.738 82.297 1.00 47.17 C ANISOU 3886 CG2 VAL A 191 7223 7108 3591 -667 -660 606 C ATOM 3887 N TYR A 192 11.402 -6.007 78.504 1.00 44.66 N ANISOU 3887 N TYR A 192 6718 6689 3564 -513 -451 337 N ATOM 3888 CA TYR A 192 10.510 -5.650 77.404 1.00 44.02 C ANISOU 3888 CA TYR A 192 6600 6576 3551 -490 -380 288 C ATOM 3889 C TYR A 192 10.697 -6.643 76.278 1.00 43.70 C ANISOU 3889 C TYR A 192 6555 6450 3598 -444 -402 338 C ATOM 3890 O TYR A 192 11.810 -6.789 75.778 1.00 43.84 O ANISOU 3890 O TYR A 192 6553 6433 3671 -387 -455 354 O ATOM 3891 CB TYR A 192 10.829 -4.245 76.918 1.00 43.65 C ANISOU 3891 CB TYR A 192 6505 6527 3551 -457 -362 200 C ATOM 3892 CG TYR A 192 10.408 -3.222 77.921 1.00 44.37 C ANISOU 3892 CG TYR A 192 6612 6689 3557 -490 -338 131 C ATOM 3893 CD1 TYR A 192 11.260 -2.845 78.960 1.00 44.99 C ANISOU 3893 CD1 TYR A 192 6716 6807 3571 -512 -396 127 C ATOM 3894 CD2 TYR A 192 9.134 -2.663 77.867 1.00 44.32 C ANISOU 3894 CD2 TYR A 192 6597 6714 3527 -494 -261 65 C ATOM 3895 CE1 TYR A 192 10.862 -1.913 79.901 1.00 45.57 C ANISOU 3895 CE1 TYR A 192 6814 6943 3557 -533 -381 53 C ATOM 3896 CE2 TYR A 192 8.727 -1.732 78.803 1.00 44.94 C ANISOU 3896 CE2 TYR A 192 6694 6864 3519 -505 -241 -10 C ATOM 3897 CZ TYR A 192 9.592 -1.365 79.814 1.00 45.54 C ANISOU 3897 CZ TYR A 192 6803 6970 3528 -524 -302 -19 C ATOM 3898 OH TYR A 192 9.177 -0.447 80.733 1.00 46.52 O ANISOU 3898 OH TYR A 192 6954 7162 3560 -526 -288 -104 O ATOM 3899 N ALA A 193 9.607 -7.300 75.875 1.00 43.50 N ANISOU 3899 N ALA A 193 6546 6401 3581 -466 -363 361 N ATOM 3900 CA ALA A 193 9.660 -8.418 74.934 1.00 43.25 C ANISOU 3900 CA ALA A 193 6535 6281 3617 -429 -397 412 C ATOM 3901 C ALA A 193 8.629 -8.289 73.816 1.00 42.66 C ANISOU 3901 C ALA A 193 6432 6175 3603 -420 -333 376 C ATOM 3902 O ALA A 193 7.477 -7.913 74.056 1.00 42.31 O ANISOU 3902 O ALA A 193 6376 6181 3521 -474 -267 353 O ATOM 3903 CB ALA A 193 9.447 -9.728 75.678 1.00 44.12 C ANISOU 3903 CB ALA A 193 6722 6373 3669 -483 -453 506 C ATOM 3904 N CYS A 194 9.067 -8.618 72.601 1.00 42.34 N ANISOU 3904 N CYS A 194 6377 6061 3650 -347 -354 372 N ATOM 3905 CA CYS A 194 8.208 -8.725 71.427 1.00 42.01 C ANISOU 3905 CA CYS A 194 6319 5974 3670 -331 -311 350 C ATOM 3906 C CYS A 194 8.064 -10.205 71.083 1.00 42.04 C ANISOU 3906 C CYS A 194 6392 5893 3690 -326 -372 418 C ATOM 3907 O CYS A 194 9.062 -10.867 70.804 1.00 41.88 O ANISOU 3907 O CYS A 194 6397 5819 3697 -256 -445 441 O ATOM 3908 CB CYS A 194 8.848 -7.972 70.256 1.00 41.68 C ANISOU 3908 CB CYS A 194 6213 5917 3709 -249 -296 293 C ATOM 3909 SG CYS A 194 7.984 -8.130 68.679 1.00 41.98 S ANISOU 3909 SG CYS A 194 6230 5896 3826 -215 -254 265 S ATOM 3910 N GLU A 195 6.834 -10.717 71.108 1.00 42.28 N ANISOU 3910 N GLU A 195 6452 5912 3700 -399 -351 448 N ATOM 3911 CA GLU A 195 6.559 -12.124 70.794 1.00 43.11 C ANISOU 3911 CA GLU A 195 6639 5923 3820 -413 -422 517 C ATOM 3912 C GLU A 195 5.844 -12.257 69.450 1.00 42.16 C ANISOU 3912 C GLU A 195 6505 5743 3769 -388 -397 487 C ATOM 3913 O GLU A 195 4.759 -11.695 69.263 1.00 42.29 O ANISOU 3913 O GLU A 195 6476 5810 3783 -441 -321 462 O ATOM 3914 CB GLU A 195 5.722 -12.769 71.901 1.00 44.52 C ANISOU 3914 CB GLU A 195 6869 6132 3914 -539 -438 599 C ATOM 3915 CG GLU A 195 5.526 -14.270 71.720 1.00 45.78 C ANISOU 3915 CG GLU A 195 7132 6179 4083 -570 -537 685 C ATOM 3916 CD GLU A 195 4.781 -14.921 72.868 1.00 47.36 C ANISOU 3916 CD GLU A 195 7384 6419 4193 -711 -563 786 C ATOM 3917 OE1 GLU A 195 5.006 -14.526 74.033 1.00 48.15 O ANISOU 3917 OE1 GLU A 195 7468 6615 4213 -754 -545 802 O ATOM 3918 OE2 GLU A 195 3.980 -15.845 72.605 1.00 48.04 O ANISOU 3918 OE2 GLU A 195 7527 6442 4282 -786 -608 853 O ATOM 3919 N VAL A 196 6.439 -13.026 68.535 1.00 41.56 N ANISOU 3919 N VAL A 196 6471 5568 3751 -302 -464 488 N ATOM 3920 CA VAL A 196 5.954 -13.137 67.156 1.00 40.59 C ANISOU 3920 CA VAL A 196 6338 5388 3696 -258 -448 450 C ATOM 3921 C VAL A 196 5.460 -14.548 66.829 1.00 40.80 C ANISOU 3921 C VAL A 196 6471 5299 3733 -283 -535 507 C ATOM 3922 O VAL A 196 6.174 -15.526 67.047 1.00 41.17 O ANISOU 3922 O VAL A 196 6602 5267 3776 -240 -636 547 O ATOM 3923 CB VAL A 196 7.050 -12.746 66.149 1.00 40.06 C ANISOU 3923 CB VAL A 196 6224 5312 3686 -121 -450 387 C ATOM 3924 CG1 VAL A 196 6.536 -12.855 64.713 1.00 39.65 C ANISOU 3924 CG1 VAL A 196 6161 5209 3694 -75 -433 347 C ATOM 3925 CG2 VAL A 196 7.546 -11.334 66.439 1.00 39.66 C ANISOU 3925 CG2 VAL A 196 6076 5365 3629 -112 -379 340 C ATOM 3926 N THR A 197 4.244 -14.628 66.288 1.00 40.37 N ANISOU 3926 N THR A 197 6414 5231 3694 -350 -504 511 N ATOM 3927 CA THR A 197 3.661 -15.882 65.798 1.00 40.89 C ANISOU 3927 CA THR A 197 6580 5179 3778 -383 -590 560 C ATOM 3928 C THR A 197 3.474 -15.800 64.277 1.00 40.07 C ANISOU 3928 C THR A 197 6458 5023 3744 -303 -577 493 C ATOM 3929 O THR A 197 2.905 -14.830 63.773 1.00 39.36 O ANISOU 3929 O THR A 197 6276 5005 3673 -312 -480 444 O ATOM 3930 CB THR A 197 2.304 -16.166 66.474 1.00 41.39 C ANISOU 3930 CB THR A 197 6657 5280 3791 -553 -577 638 C ATOM 3931 OG1 THR A 197 2.448 -16.071 67.898 1.00 41.81 O ANISOU 3931 OG1 THR A 197 6708 5410 3766 -627 -572 693 O ATOM 3932 CG2 THR A 197 1.784 -17.556 66.107 1.00 42.25 C ANISOU 3932 CG2 THR A 197 6887 5253 3914 -609 -693 707 C ATOM 3933 N HIS A 198 3.956 -16.815 63.559 1.00 40.16 N ANISOU 3933 N HIS A 198 6562 4910 3789 -218 -678 489 N ATOM 3934 CA HIS A 198 3.891 -16.847 62.097 1.00 39.62 C ANISOU 3934 CA HIS A 198 6488 4791 3776 -127 -677 422 C ATOM 3935 C HIS A 198 4.101 -18.277 61.560 1.00 40.61 C ANISOU 3935 C HIS A 198 6755 4756 3919 -68 -817 436 C ATOM 3936 O HIS A 198 4.871 -19.061 62.131 1.00 40.91 O ANISOU 3936 O HIS A 198 6877 4728 3939 -24 -913 468 O ATOM 3937 CB HIS A 198 4.923 -15.872 61.504 1.00 38.78 C ANISOU 3937 CB HIS A 198 6279 4761 3693 7 -610 341 C ATOM 3938 CG HIS A 198 4.960 -15.855 60.007 1.00 38.45 C ANISOU 3938 CG HIS A 198 6223 4689 3698 108 -605 274 C ATOM 3939 ND1 HIS A 198 4.043 -15.167 59.241 1.00 37.80 N ANISOU 3939 ND1 HIS A 198 6076 4643 3641 66 -528 243 N ATOM 3940 CD2 HIS A 198 5.817 -16.435 59.136 1.00 38.70 C ANISOU 3940 CD2 HIS A 198 6292 4667 3747 256 -667 229 C ATOM 3941 CE1 HIS A 198 4.326 -15.338 57.963 1.00 37.51 C ANISOU 3941 CE1 HIS A 198 6042 4573 3635 174 -544 187 C ATOM 3942 NE2 HIS A 198 5.398 -16.103 57.871 1.00 38.22 N ANISOU 3942 NE2 HIS A 198 6192 4613 3718 294 -626 174 N ATOM 3943 N GLN A 199 3.418 -18.582 60.452 1.00 40.47 N ANISOU 3943 N GLN A 199 6767 4674 3937 -61 -834 407 N ATOM 3944 CA GLN A 199 3.381 -19.925 59.840 1.00 41.58 C ANISOU 3944 CA GLN A 199 7056 4648 4095 -18 -975 413 C ATOM 3945 C GLN A 199 4.762 -20.568 59.660 1.00 42.29 C ANISOU 3945 C GLN A 199 7213 4669 4186 162 -1067 371 C ATOM 3946 O GLN A 199 4.955 -21.741 59.970 1.00 43.70 O ANISOU 3946 O GLN A 199 7534 4713 4357 174 -1206 411 O ATOM 3947 CB GLN A 199 2.666 -19.858 58.480 1.00 41.15 C ANISOU 3947 CB GLN A 199 6992 4564 4078 1 -957 358 C ATOM 3948 CG GLN A 199 2.271 -21.214 57.896 1.00 42.44 C ANISOU 3948 CG GLN A 199 7320 4549 4257 1 -1107 371 C ATOM 3949 CD GLN A 199 1.629 -21.123 56.518 1.00 42.05 C ANISOU 3949 CD GLN A 199 7261 4476 4240 29 -1092 310 C ATOM 3950 OE1 GLN A 199 1.723 -22.057 55.715 1.00 42.84 O ANISOU 3950 OE1 GLN A 199 7483 4441 4355 108 -1207 274 O ATOM 3951 NE2 GLN A 199 0.972 -20.004 56.236 1.00 40.97 N ANISOU 3951 NE2 GLN A 199 6987 4466 4113 -31 -958 294 N ATOM 3952 N GLY A 200 5.704 -19.792 59.138 1.00 41.65 N ANISOU 3952 N GLY A 200 7027 4685 4114 302 -994 294 N ATOM 3953 CA GLY A 200 7.092 -20.219 58.968 1.00 42.27 C ANISOU 3953 CA GLY A 200 7129 4746 4185 487 -1059 250 C ATOM 3954 C GLY A 200 7.915 -20.500 60.212 1.00 42.79 C ANISOU 3954 C GLY A 200 7222 4816 4219 492 -1110 303 C ATOM 3955 O GLY A 200 8.994 -21.074 60.100 1.00 43.48 O ANISOU 3955 O GLY A 200 7350 4870 4300 648 -1189 274 O ATOM 3956 N LEU A 201 7.429 -20.083 61.384 1.00 42.86 N ANISOU 3956 N LEU A 201 7204 4878 4204 333 -1065 378 N ATOM 3957 CA LEU A 201 8.080 -20.370 62.673 1.00 43.52 C ANISOU 3957 CA LEU A 201 7321 4965 4250 312 -1118 441 C ATOM 3958 C LEU A 201 7.471 -21.614 63.337 1.00 45.10 C ANISOU 3958 C LEU A 201 7684 5019 4434 207 -1250 532 C ATOM 3959 O LEU A 201 6.253 -21.676 63.534 1.00 45.22 O ANISOU 3959 O LEU A 201 7723 5018 4442 43 -1235 588 O ATOM 3960 CB LEU A 201 7.931 -19.172 63.610 1.00 42.44 C ANISOU 3960 CB LEU A 201 7063 4979 4083 199 -996 468 C ATOM 3961 CG LEU A 201 8.543 -17.865 63.107 1.00 41.36 C ANISOU 3961 CG LEU A 201 6771 4982 3961 276 -877 394 C ATOM 3962 CD1 LEU A 201 8.010 -16.678 63.896 1.00 40.66 C ANISOU 3962 CD1 LEU A 201 6586 5015 3849 145 -764 412 C ATOM 3963 CD2 LEU A 201 10.066 -17.925 63.149 1.00 41.64 C ANISOU 3963 CD2 LEU A 201 6777 5055 3989 430 -917 367 C ATOM 3964 N SER A 202 8.316 -22.591 63.681 1.00 46.63 N ANISOU 3964 N SER A 202 7987 5112 4617 300 -1384 552 N ATOM 3965 CA SER A 202 7.874 -23.812 64.381 1.00 48.30 C ANISOU 3965 CA SER A 202 8368 5172 4812 202 -1533 650 C ATOM 3966 C SER A 202 7.038 -23.454 65.610 1.00 48.30 C ANISOU 3966 C SER A 202 8338 5249 4765 -20 -1478 755 C ATOM 3967 O SER A 202 5.899 -23.890 65.747 1.00 49.30 O ANISOU 3967 O SER A 202 8528 5322 4883 -180 -1510 827 O ATOM 3968 CB SER A 202 9.074 -24.669 64.815 1.00 49.56 C ANISOU 3968 CB SER A 202 8624 5246 4961 340 -1670 659 C ATOM 3969 OG SER A 202 10.011 -24.832 63.767 1.00 49.87 O ANISOU 3969 OG SER A 202 8656 5264 5028 571 -1699 550 O ATOM 3970 N SER A 203 7.621 -22.639 66.482 1.00 47.62 N ANISOU 3970 N SER A 203 8148 5301 4642 -26 -1396 762 N ATOM 3971 CA SER A 203 6.936 -22.088 67.648 1.00 47.34 C ANISOU 3971 CA SER A 203 8059 5378 4550 -211 -1321 841 C ATOM 3972 C SER A 203 7.212 -20.585 67.682 1.00 45.70 C ANISOU 3972 C SER A 203 7677 5351 4337 -183 -1157 770 C ATOM 3973 O SER A 203 8.158 -20.126 67.030 1.00 45.05 O ANISOU 3973 O SER A 203 7529 5299 4287 -28 -1128 685 O ATOM 3974 CB SER A 203 7.442 -22.757 68.926 1.00 48.54 C ANISOU 3974 CB SER A 203 8296 5496 4649 -256 -1423 936 C ATOM 3975 OG SER A 203 8.857 -22.710 68.990 1.00 48.73 O ANISOU 3975 OG SER A 203 8304 5528 4682 -87 -1456 888 O ATOM 3976 N PRO A 204 6.396 -19.810 68.428 1.00 45.02 N ANISOU 3976 N PRO A 204 7514 5387 4205 -330 -1055 803 N ATOM 3977 CA PRO A 204 6.609 -18.361 68.446 1.00 43.92 C ANISOU 3977 CA PRO A 204 7225 5400 4061 -303 -913 731 C ATOM 3978 C PRO A 204 8.018 -17.942 68.883 1.00 44.02 C ANISOU 3978 C PRO A 204 7196 5466 4065 -195 -919 701 C ATOM 3979 O PRO A 204 8.663 -18.648 69.665 1.00 44.46 O ANISOU 3979 O PRO A 204 7325 5479 4088 -186 -1013 758 O ATOM 3980 CB PRO A 204 5.558 -17.858 69.441 1.00 43.80 C ANISOU 3980 CB PRO A 204 7168 5496 3980 -474 -837 784 C ATOM 3981 CG PRO A 204 4.490 -18.886 69.417 1.00 44.64 C ANISOU 3981 CG PRO A 204 7367 5520 4076 -594 -905 869 C ATOM 3982 CD PRO A 204 5.175 -20.193 69.160 1.00 45.65 C ANISOU 3982 CD PRO A 204 7635 5477 4233 -523 -1064 903 C ATOM 3983 N VAL A 205 8.480 -16.813 68.347 1.00 43.45 N ANISOU 3983 N VAL A 205 7007 5483 4020 -119 -825 617 N ATOM 3984 CA VAL A 205 9.814 -16.281 68.628 1.00 43.70 C ANISOU 3984 CA VAL A 205 6977 5582 4046 -22 -824 586 C ATOM 3985 C VAL A 205 9.677 -15.032 69.499 1.00 43.33 C ANISOU 3985 C VAL A 205 6841 5668 3955 -107 -728 576 C ATOM 3986 O VAL A 205 8.799 -14.200 69.269 1.00 42.59 O ANISOU 3986 O VAL A 205 6688 5629 3866 -169 -633 542 O ATOM 3987 CB VAL A 205 10.582 -15.961 67.318 1.00 43.22 C ANISOU 3987 CB VAL A 205 6850 5527 4045 131 -806 506 C ATOM 3988 CG1 VAL A 205 11.888 -15.217 67.599 1.00 43.07 C ANISOU 3988 CG1 VAL A 205 6740 5609 4016 206 -791 481 C ATOM 3989 CG2 VAL A 205 10.867 -17.247 66.550 1.00 43.97 C ANISOU 3989 CG2 VAL A 205 7042 5494 4171 241 -915 505 C ATOM 3990 N THR A 206 10.552 -14.924 70.496 1.00 44.14 N ANISOU 3990 N THR A 206 6940 5818 4013 -103 -761 603 N ATOM 3991 CA THR A 206 10.603 -13.779 71.391 1.00 44.14 C ANISOU 3991 CA THR A 206 6870 5937 3965 -169 -691 588 C ATOM 3992 C THR A 206 11.953 -13.094 71.267 1.00 44.39 C ANISOU 3992 C THR A 206 6826 6027 4014 -74 -694 547 C ATOM 3993 O THR A 206 12.997 -13.731 71.414 1.00 44.70 O ANISOU 3993 O THR A 206 6889 6042 4052 4 -778 574 O ATOM 3994 CB THR A 206 10.391 -14.196 72.859 1.00 44.84 C ANISOU 3994 CB THR A 206 7021 6050 3968 -274 -730 665 C ATOM 3995 OG1 THR A 206 9.062 -14.704 73.016 1.00 45.07 O ANISOU 3995 OG1 THR A 206 7101 6053 3969 -384 -716 712 O ATOM 3996 CG2 THR A 206 10.591 -13.010 73.811 1.00 44.46 C ANISOU 3996 CG2 THR A 206 6907 6125 3861 -323 -668 638 C ATOM 3997 N LYS A 207 11.913 -11.795 70.984 1.00 44.46 N ANISOU 3997 N LYS A 207 6742 6113 4038 -83 -610 486 N ATOM 3998 CA LYS A 207 13.068 -10.922 71.126 1.00 44.90 C ANISOU 3998 CA LYS A 207 6719 6245 4094 -40 -609 459 C ATOM 3999 C LYS A 207 12.768 -9.961 72.271 1.00 44.94 C ANISOU 3999 C LYS A 207 6711 6326 4038 -140 -568 450 C ATOM 4000 O LYS A 207 11.646 -9.462 72.386 1.00 44.50 O ANISOU 4000 O LYS A 207 6656 6286 3967 -211 -499 423 O ATOM 4001 CB LYS A 207 13.356 -10.171 69.820 1.00 44.67 C ANISOU 4001 CB LYS A 207 6601 6238 4132 29 -562 400 C ATOM 4002 CG LYS A 207 14.315 -10.892 68.877 1.00 45.52 C ANISOU 4002 CG LYS A 207 6691 6324 4280 161 -617 402 C ATOM 4003 CD LYS A 207 15.706 -11.055 69.492 1.00 46.82 C ANISOU 4003 CD LYS A 207 6830 6542 4417 215 -687 434 C ATOM 4004 CE LYS A 207 16.806 -11.135 68.443 1.00 47.43 C ANISOU 4004 CE LYS A 207 6828 6664 4531 348 -709 416 C ATOM 4005 NZ LYS A 207 16.679 -12.331 67.565 1.00 48.09 N ANISOU 4005 NZ LYS A 207 6966 6664 4641 457 -750 409 N ATOM 4006 N SER A 208 13.764 -9.726 73.124 1.00 45.58 N ANISOU 4006 N SER A 208 6780 6459 4079 -139 -614 468 N ATOM 4007 CA SER A 208 13.586 -8.898 74.319 1.00 45.97 C ANISOU 4007 CA SER A 208 6830 6579 4057 -227 -591 457 C ATOM 4008 C SER A 208 14.881 -8.244 74.782 1.00 46.47 C ANISOU 4008 C SER A 208 6846 6704 4106 -208 -635 453 C ATOM 4009 O SER A 208 15.959 -8.538 74.261 1.00 46.27 O ANISOU 4009 O SER A 208 6782 6679 4120 -129 -686 472 O ATOM 4010 CB SER A 208 13.004 -9.737 75.462 1.00 46.66 C ANISOU 4010 CB SER A 208 7003 6661 4065 -300 -619 519 C ATOM 4011 OG SER A 208 13.932 -10.705 75.915 1.00 47.16 O ANISOU 4011 OG SER A 208 7110 6698 4111 -264 -716 586 O ATOM 4012 N PHE A 209 14.750 -7.351 75.761 1.00 47.06 N ANISOU 4012 N PHE A 209 6923 6838 4120 -281 -618 428 N ATOM 4013 CA PHE A 209 15.900 -6.710 76.400 1.00 47.83 C ANISOU 4013 CA PHE A 209 6989 6995 4191 -287 -670 429 C ATOM 4014 C PHE A 209 15.573 -6.274 77.823 1.00 48.88 C ANISOU 4014 C PHE A 209 7170 7178 4224 -371 -671 420 C ATOM 4015 O PHE A 209 14.403 -6.199 78.205 1.00 48.54 O ANISOU 4015 O PHE A 209 7165 7142 4135 -421 -614 397 O ATOM 4016 CB PHE A 209 16.373 -5.507 75.572 1.00 47.11 C ANISOU 4016 CB PHE A 209 6816 6925 4160 -269 -649 376 C ATOM 4017 CG PHE A 209 15.400 -4.360 75.545 1.00 46.67 C ANISOU 4017 CG PHE A 209 6762 6870 4100 -321 -581 301 C ATOM 4018 CD1 PHE A 209 14.346 -4.340 74.634 1.00 46.10 C ANISOU 4018 CD1 PHE A 209 6686 6756 4076 -306 -510 267 C ATOM 4019 CD2 PHE A 209 15.540 -3.291 76.424 1.00 46.97 C ANISOU 4019 CD2 PHE A 209 6811 6949 4087 -377 -595 260 C ATOM 4020 CE1 PHE A 209 13.447 -3.278 74.604 1.00 45.84 C ANISOU 4020 CE1 PHE A 209 6653 6726 4040 -340 -451 196 C ATOM 4021 CE2 PHE A 209 14.642 -2.233 76.403 1.00 46.86 C ANISOU 4021 CE2 PHE A 209 6807 6929 4067 -407 -541 181 C ATOM 4022 CZ PHE A 209 13.595 -2.222 75.489 1.00 46.18 C ANISOU 4022 CZ PHE A 209 6711 6805 4031 -385 -468 150 C ATOM 4023 N ASN A 210 16.624 -5.990 78.591 1.00 50.41 N ANISOU 4023 N ASN A 210 7356 7420 4379 -383 -738 437 N ATOM 4024 CA ASN A 210 16.506 -5.396 79.922 1.00 51.76 C ANISOU 4024 CA ASN A 210 7567 7648 4451 -456 -748 417 C ATOM 4025 C ASN A 210 16.900 -3.932 79.833 1.00 51.87 C ANISOU 4025 C ASN A 210 7539 7688 4480 -474 -749 346 C ATOM 4026 O ASN A 210 17.960 -3.617 79.287 1.00 51.62 O ANISOU 4026 O ASN A 210 7446 7661 4505 -447 -795 359 O ATOM 4027 CB ASN A 210 17.430 -6.096 80.921 1.00 53.24 C ANISOU 4027 CB ASN A 210 7784 7866 4577 -465 -838 490 C ATOM 4028 CG ASN A 210 17.218 -7.599 80.974 1.00 54.06 C ANISOU 4028 CG ASN A 210 7939 7927 4674 -443 -865 572 C ATOM 4029 OD1 ASN A 210 18.158 -8.352 81.220 1.00 55.07 O ANISOU 4029 OD1 ASN A 210 8074 8050 4800 -407 -948 637 O ATOM 4030 ND2 ASN A 210 15.985 -8.043 80.743 1.00 54.07 N ANISOU 4030 ND2 ASN A 210 7978 7895 4672 -466 -804 572 N ATOM 4031 N ARG A 211 16.062 -3.045 80.373 1.00 52.38 N ANISOU 4031 N ARG A 211 7638 7773 4492 -519 -704 273 N ATOM 4032 CA ARG A 211 16.373 -1.611 80.399 1.00 52.76 C ANISOU 4032 CA ARG A 211 7670 7828 4547 -541 -722 199 C ATOM 4033 C ARG A 211 17.714 -1.384 81.112 1.00 53.69 C ANISOU 4033 C ARG A 211 7782 7985 4633 -569 -821 232 C ATOM 4034 O ARG A 211 17.845 -1.676 82.301 1.00 54.85 O ANISOU 4034 O ARG A 211 7978 8176 4685 -602 -856 251 O ATOM 4035 CB ARG A 211 15.258 -0.813 81.089 1.00 52.92 C ANISOU 4035 CB ARG A 211 7744 7870 4493 -570 -671 109 C ATOM 4036 CG ARG A 211 15.349 0.681 80.834 1.00 52.96 C ANISOU 4036 CG ARG A 211 7746 7849 4527 -577 -687 21 C ATOM 4037 CD ARG A 211 14.326 1.479 81.620 1.00 53.70 C ANISOU 4037 CD ARG A 211 7901 7969 4535 -585 -650 -81 C ATOM 4038 NE ARG A 211 14.793 1.734 82.981 1.00 55.41 N ANISOU 4038 NE ARG A 211 8173 8241 4642 -623 -712 -96 N ATOM 4039 CZ ARG A 211 14.509 0.999 84.058 1.00 56.23 C ANISOU 4039 CZ ARG A 211 8313 8419 4633 -643 -700 -67 C ATOM 4040 NH1 ARG A 211 13.721 -0.074 83.988 1.00 56.60 N ANISOU 4040 NH1 ARG A 211 8350 8494 4661 -637 -632 -14 N ATOM 4041 NH2 ARG A 211 15.014 1.352 85.236 1.00 57.26 N ANISOU 4041 NH2 ARG A 211 8493 8598 4665 -677 -764 -87 N ATOM 4042 N GLY A 212 18.708 -0.898 80.370 1.00 53.80 N ANISOU 4042 N GLY A 212 7728 7991 4721 -559 -868 248 N ATOM 4043 CA GLY A 212 20.058 -0.696 80.905 1.00 54.82 C ANISOU 4043 CA GLY A 212 7831 8167 4830 -589 -967 291 C ATOM 4044 C GLY A 212 20.820 -1.995 81.096 1.00 55.36 C ANISOU 4044 C GLY A 212 7877 8267 4889 -548 -1010 385 C ATOM 4045 O GLY A 212 21.470 -2.490 80.172 1.00 55.55 O ANISOU 4045 O GLY A 212 7827 8295 4984 -491 -1021 434 O TER 4046 GLY A 212 HETATM 4047 O HOH B 301 -15.664 12.382 46.281 1.00 32.82 O HETATM 4048 O HOH B 302 -13.784 25.228 42.363 1.00 38.99 O HETATM 4049 O HOH B 303 -17.871 9.703 41.236 1.00 20.06 O HETATM 4050 O HOH B 304 -4.051 8.626 25.426 1.00 26.73 O HETATM 4051 O HOH B 305 -10.772 3.084 26.172 1.00 22.33 O HETATM 4052 O HOH B 306 -13.322 16.196 46.617 1.00 22.10 O HETATM 4053 O HOH B 307 -5.689 21.225 19.740 1.00 38.02 O HETATM 4054 O HOH B 308 4.765 9.710 54.413 1.00 39.31 O HETATM 4055 O HOH B 309 3.076 12.787 30.301 1.00 21.42 O HETATM 4056 O HOH B 310 3.864 14.911 39.270 1.00 21.48 O HETATM 4057 O HOH B 311 -1.669 18.877 41.405 1.00 31.26 O HETATM 4058 O HOH B 312 -11.398 7.799 46.646 1.00 29.40 O HETATM 4059 O HOH B 313 3.460 19.709 27.272 1.00 36.38 O HETATM 4060 O HOH B 314 -2.194 14.046 56.291 1.00 23.38 O HETATM 4061 O HOH B 315 -20.890 19.347 43.400 1.00 26.83 O HETATM 4062 O HOH B 316 -7.293 21.460 34.490 1.00 28.23 O HETATM 4063 O HOH B 317 -7.671 12.747 30.414 1.00 34.59 O HETATM 4064 O HOH B 318 9.374 15.341 50.938 1.00 39.42 O HETATM 4065 O HOH B 319 -28.413 17.053 40.399 1.00 40.49 O HETATM 4066 O HOH B 320 -15.433 6.086 40.222 1.00 22.75 O HETATM 4067 O HOH B 321 1.590 15.103 47.646 1.00 23.41 O HETATM 4068 O HOH B 322 -15.574 30.430 38.163 1.00 46.57 O HETATM 4069 O HOH B 323 -0.147 25.697 59.559 1.00 38.37 O HETATM 4070 O HOH B 324 -4.039 6.547 17.854 1.00 26.37 O HETATM 4071 O HOH B 325 -10.845 20.859 62.553 1.00 40.41 O HETATM 4072 O HOH B 326 -7.225 8.231 73.100 1.00 49.99 O HETATM 4073 O HOH C 301 0.625 14.537 10.335 1.00 31.14 O HETATM 4074 O HOH C 302 -18.289 18.950 23.094 1.00 32.26 O HETATM 4075 O HOH C 303 -16.091 16.181 -2.407 1.00 35.44 O HETATM 4076 O HOH C 304 -1.134 0.953 8.651 1.00 54.93 O HETATM 4077 O HOH C 305 2.850 7.633 -1.195 1.00 25.31 O HETATM 4078 O HOH C 306 -14.880 21.817 4.057 1.00 47.31 O HETATM 4079 O HOH C 307 -0.493 18.394 -3.061 1.00 32.64 O HETATM 4080 O HOH C 308 6.386 14.596 14.136 1.00 36.00 O HETATM 4081 O HOH A 301 5.375 5.883 69.677 1.00 48.23 O HETATM 4082 O HOH A 302 13.684 6.954 70.704 1.00 25.75 O HETATM 4083 O HOH A 303 -0.037 3.133 82.391 1.00 38.46 O HETATM 4084 O HOH A 304 2.305 2.923 69.906 1.00 34.28 O HETATM 4085 O HOH A 305 -15.899 8.531 39.167 1.00 24.49 O HETATM 4086 O HOH A 306 -13.220 -4.307 44.326 1.00 36.21 O HETATM 4087 O HOH A 307 8.895 -12.462 38.279 1.00 40.19 O HETATM 4088 O HOH A 308 11.860 -7.082 50.841 1.00 48.60 O HETATM 4089 O HOH A 309 -15.226 8.387 25.889 1.00 23.93 O HETATM 4090 O HOH A 310 -0.477 -0.736 44.910 1.00 30.84 O HETATM 4091 O HOH A 311 -15.907 -11.316 29.616 1.00 45.70 O HETATM 4092 O HOH A 312 5.231 -17.894 73.900 1.00 43.56 O HETATM 4093 O HOH A 313 2.623 4.886 79.640 1.00 29.57 O HETATM 4094 O HOH A 314 -24.192 1.537 26.215 1.00 35.70 O HETATM 4095 O HOH A 315 12.544 2.562 69.762 1.00 25.76 O HETATM 4096 O HOH A 316 19.950 6.920 72.399 1.00 42.61 O HETATM 4097 O HOH A 317 0.849 -5.332 48.302 1.00 28.34 O HETATM 4098 O HOH A 318 -11.674 -5.959 28.974 1.00 29.94 O HETATM 4099 O HOH A 319 4.763 -4.290 41.314 1.00 29.97 O HETATM 4100 O HOH A 320 9.204 -6.873 53.001 1.00 29.42 O HETATM 4101 O HOH A 321 -9.434 0.408 45.833 1.00 31.22 O HETATM 4102 O HOH A 322 2.372 -13.341 69.342 1.00 30.43 O HETATM 4103 O HOH A 323 -0.102 -3.930 73.195 1.00 34.90 O HETATM 4104 O HOH A 324 11.773 -19.265 56.226 1.00 32.31 O HETATM 4105 O HOH A 325 -0.410 -0.494 57.716 1.00 32.47 O HETATM 4106 O HOH A 326 -22.492 10.241 28.465 1.00 33.29 O HETATM 4107 O HOH A 327 -16.928 0.118 16.344 1.00 32.65 O CONECT 137 725 CONECT 725 137 CONECT 1097 1511 CONECT 1511 1097 CONECT 1812 2261 CONECT 2261 1812 CONECT 2540 3101 CONECT 3101 2540 CONECT 3441 3909 CONECT 3909 3441 MASTER 350 0 0 12 55 0 0 6 4087 3 10 43 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: 6ddv
Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code
Check Database
Protein Sequence Similarity
1a4k
RCSB PDB
PDBbind
217aa, >1A4K_1|Chains... at 90%
1fl6
RCSB PDB
PDBbind
217aa, >1FL6_1|Chains... at 93%
4yhm
RCSB PDB
PDBbind
219aa, >4YHM_2|Chain... *
5tkj
RCSB PDB
PDBbind
219aa, >5TKJ_2|Chains... at 92%
6cdm
RCSB PDB
PDBbind
219aa, >6CDM_2|Chains... at 92%
6cdo
RCSB PDB
PDBbind
219aa, >6CDO_2|Chain... at 92%
6cdp
RCSB PDB
PDBbind
219aa, >6CDP_2|Chain... at 90%
6pyd
RCSB PDB
PDBbind
219aa, >6PYD_2|Chains... at 92%
Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
6ddm
RCSB PDB
PDBbind
MICA*008
6ddr
RCSB PDB
PDBbind
MICA*008
Entry Information
PDB ID
6ddv
Complex Type
Protein-Protein
PDBbind Subset
general set
Protein Name
Anti-MICA Fab 6E1
Ligand Name
MICA*008
EC.Number
E.C.-.-.-.-
Resolution
2.05(Å)
Affinity (Kd/Ki/IC50)
Kd=5.78nM
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