Browse entries in the PDBbind-CN Database
HEADER IMMUNE SYSTEM 10-MAY-18 6DDR TITLE CRYSTAL STRUCTURE ANALYSIS OF THE EPITOPE OF AN ANTI-MICA ANTIBODY COMPND MOL_ID: 1; COMPND 2 MOLECULE: ANTI-MICA FAB FRAGMENT LIGHT CHAIN CLONE 13A9; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: ANTI-MICA FAB FRAGMENT HEAVY CHAIN CLONE 13A9; COMPND 7 CHAIN: B; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: MHC CLASS I POLYPEPTIDE-RELATED SEQUENCE A; COMPND 11 CHAIN: C; COMPND 12 SYNONYM: MHC CLASS I POLYPEPTIDE-RELATED SEQUENCE A,ISOFORM CRA_C, COMPND 13 MICA,STRESS INDUCIBLE CLASS I HOMOLOG,CDNA FLJ60820,HIGHLY SIMILAR TO COMPND 14 HOMO SAPIENS MHC CLASS I POLYPEPTIDE-RELATED SEQUENCE A (MICA),MRNA; COMPND 15 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 10090; SOURCE 4 STRAIN: BALB/C; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: 64B4; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PBR322; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 12 ORGANISM_TAXID: 10090; SOURCE 13 STRAIN: BALB/C; SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 16 EXPRESSION_SYSTEM_STRAIN: 64B4; SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PBR322; SOURCE 19 MOL_ID: 3; SOURCE 20 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 21 ORGANISM_COMMON: HUMAN; SOURCE 22 ORGANISM_TAXID: 9606; SOURCE 23 GENE: MICA, HCG_2001511; SOURCE 24 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 25 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 26 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 27 EXPRESSION_SYSTEM_PLASMID: PACGP67 KEYWDS FAB FRAGMENT-ANTIGEN COMPLEX, IMMUNOGLOBULIN DOMAIN, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR M.L.MATSUMOTO REVDAT 3 23-JAN-19 6DDR 1 JRNL REVDAT 2 05-DEC-18 6DDR 1 JRNL REVDAT 1 24-OCT-18 6DDR 0 JRNL AUTH T.N.LOMBANA,M.L.MATSUMOTO,A.M.BERKLEY,E.TOY,R.COOK,Y.GAN, JRNL AUTH 2 C.DU,P.SCHNIER,W.SANDOVAL,Z.YE,J.M.SCHARTNER,J.KIM,C.SPIESS JRNL TITL HIGH-RESOLUTION GLYCOSYLATION SITE-ENGINEERING METHOD JRNL TITL 2 IDENTIFIES MICA EPITOPE CRITICAL FOR SHEDDING INHIBITION JRNL TITL 3 ACTIVITY OF ANTI-MICA ANTIBODIES. JRNL REF MABS V. 11 75 2019 JRNL REFN ESSN 1942-0870 JRNL PMID 30307368 JRNL DOI 10.1080/19420862.2018.1532767 REMARK 2 REMARK 2 RESOLUTION. 1.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0155 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 95.0 REMARK 3 NUMBER OF REFLECTIONS : 40023 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) : 0.210 REMARK 3 R VALUE (WORKING SET) : 0.208 REMARK 3 FREE R VALUE : 0.247 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900 REMARK 3 FREE R VALUE TEST SET COUNT : 2050 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2295 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 75.76 REMARK 3 BIN R VALUE (WORKING SET) : 0.3140 REMARK 3 BIN FREE R VALUE SET COUNT : 124 REMARK 3 BIN FREE R VALUE : 0.3230 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3945 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 54 REMARK 3 SOLVENT ATOMS : 260 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.71 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -2.11000 REMARK 3 B22 (A**2) : 4.52000 REMARK 3 B33 (A**2) : -2.41000 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): 0.179 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.160 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.139 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.984 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.931 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4163 ; 0.006 ; 0.019 REMARK 3 BOND LENGTHS OTHERS (A): 3691 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5684 ; 1.117 ; 1.940 REMARK 3 BOND ANGLES OTHERS (DEGREES): 8523 ; 0.826 ; 3.000 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 543 ; 5.878 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 164 ;35.501 ;24.756 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 596 ;11.460 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;17.905 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 645 ; 0.065 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4802 ; 0.003 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): 952 ; 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 : A 1 A 214 REMARK 3 ORIGIN FOR THE GROUP (A): 6.3635 -10.8440 -23.6198 REMARK 3 T TENSOR REMARK 3 T11: 0.1513 T22: 0.0148 REMARK 3 T33: 0.1577 T12: 0.0219 REMARK 3 T13: -0.0330 T23: 0.0062 REMARK 3 L TENSOR REMARK 3 L11: 1.0216 L22: 0.2384 REMARK 3 L33: 1.3019 L12: 0.2206 REMARK 3 L13: -0.8056 L23: -0.2397 REMARK 3 S TENSOR REMARK 3 S11: -0.0429 S12: -0.1053 S13: 0.0189 REMARK 3 S21: -0.0065 S22: -0.0158 S23: -0.0440 REMARK 3 S31: 0.0506 S32: 0.0736 S33: 0.0587 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 : B 1 B 217 REMARK 3 ORIGIN FOR THE GROUP (A): -1.5337 2.7669 -30.5450 REMARK 3 T TENSOR REMARK 3 T11: 0.1308 T22: 0.0348 REMARK 3 T33: 0.2130 T12: 0.0260 REMARK 3 T13: -0.0375 T23: 0.0376 REMARK 3 L TENSOR REMARK 3 L11: 0.6670 L22: 0.2721 REMARK 3 L33: 2.4379 L12: 0.0580 REMARK 3 L13: -1.0289 L23: -0.1540 REMARK 3 S TENSOR REMARK 3 S11: 0.0647 S12: 0.1353 S13: 0.1581 REMARK 3 S21: 0.0387 S22: 0.0438 S23: -0.0346 REMARK 3 S31: -0.1744 S32: -0.2434 S33: -0.1085 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 : C 204 C 297 REMARK 3 ORIGIN FOR THE GROUP (A): 19.5164 -3.3481 -66.2825 REMARK 3 T TENSOR REMARK 3 T11: 0.1249 T22: 0.0339 REMARK 3 T33: 0.0753 T12: 0.0344 REMARK 3 T13: 0.0397 T23: 0.0126 REMARK 3 L TENSOR REMARK 3 L11: 2.0313 L22: 1.6191 REMARK 3 L33: 4.1013 L12: -0.0446 REMARK 3 L13: 1.0361 L23: -0.6579 REMARK 3 S TENSOR REMARK 3 S11: 0.1210 S12: 0.1943 S13: -0.1036 REMARK 3 S21: -0.2979 S22: -0.0640 S23: -0.1388 REMARK 3 S31: 0.3575 S32: 0.2620 S33: -0.0569 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 6DDR 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_1000234445. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 02-MAR-16 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ALS REMARK 200 BEAMLINE : 5.0.2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.00 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42120 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900 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 (%) : 95.0 REMARK 200 DATA REDUNDANCY : 5.200 REMARK 200 R MERGE (I) : 0.08500 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93 REMARK 200 COMPLETENESS FOR SHELL (%) : 74.6 REMARK 200 DATA REDUNDANCY IN SHELL : 4.00 REMARK 200 R MERGE FOR SHELL (I) : 0.48600 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHENIX REMARK 200 STARTING MODEL: 1A2Y, 4J8R, 1NZ8, 6DDM REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 48.44 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.01 M ZNSO4, 0.1 M MES, PH 6.5, 16% REMARK 280 PEG 550 MME, VAPOR DIFFUSION, HANGING DROP, 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 25.77450 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 86.18400 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.91650 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 86.18400 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.77450 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 30.91650 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 7660 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 22770 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -76.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C 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 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 A 3 CG CD OE1 NE2 REMARK 470 ARG A 24 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 42 CG CD CE NZ REMARK 470 GLN A 70 CG CD OE1 NE2 REMARK 470 LYS A 107 CG CD CE NZ REMARK 470 LYS A 126 CG CD CE NZ REMARK 470 LYS A 169 CG CD CE NZ REMARK 470 GLU A 213 CG CD OE1 OE2 REMARK 470 GLN B 5 CG CD OE1 NE2 REMARK 470 LYS B 23 CG CD CE NZ REMARK 470 GLU B 61 CG CD OE1 OE2 REMARK 470 LYS B 64 CG CD CE NZ REMARK 470 ARG B 68 CG CD NE CZ NH1 NH2 REMARK 470 ASN B 199 CG OD1 ND2 REMARK 470 LYS B 201 CG CD CE NZ REMARK 470 LYS B 206 CG CD CE NZ REMARK 470 LYS B 214 CG CD CE NZ REMARK 470 ASP B 217 CG OD1 OD2 REMARK 470 GLU C 215 CG CD OE1 OE2 REMARK 470 GLU C 218 CG CD OE1 OE2 REMARK 470 ARG C 233 CG CD NE CZ NH1 NH2 REMARK 470 GLN C 252 CG CD OE1 NE2 REMARK 470 ARG C 271 CG CD NE CZ NH1 NH2 REMARK 470 ARG C 274 CG CD NE CZ NH1 NH2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 SER A 31 19.07 59.12 REMARK 500 ALA A 51 -40.82 69.14 REMARK 500 SER A 77 70.42 47.69 REMARK 500 ASN A 138 64.74 61.43 REMARK 500 LEU B 96 -158.48 -94.89 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN C 304 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS C 248 NE2 REMARK 620 2 HOH C 404 O 113.9 REMARK 620 3 ASP A 185 OD1 24.1 124.7 REMARK 620 4 HIS A 189 NE2 22.9 122.6 2.2 REMARK 620 N 1 2 3 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 303 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 303 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 303 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 304 DBREF 6DDR A 1 214 PDB 6DDR 6DDR 1 214 DBREF 6DDR B 1 217 PDB 6DDR 6DDR 1 217 DBREF 6DDR C 204 297 UNP Q96QC4 Q96QC4_HUMAN 204 297 SEQRES 1 A 214 ASP ILE GLN MET THR GLN SER PRO ALA SER LEU SER ALA SEQRES 2 A 214 SER VAL GLY GLU THR VAL THR ILE THR CYS ARG ALA SER SEQRES 3 A 214 GLY ASN ILE HIS SER TYR LEU ALA TRP TYR GLN GLN LYS SEQRES 4 A 214 GLN GLY LYS SER PRO GLN LEU LEU VAL TYR TYR ALA GLU SEQRES 5 A 214 THR LEU ALA ASP GLY VAL PRO SER ARG PHE SER GLY ARG SEQRES 6 A 214 GLY SER GLY THR GLN TYR SER LEU LYS ILE ASN SER LEU SEQRES 7 A 214 GLN PRO GLU ASP PHE GLY SER TYR PHE CYS GLN GLN PHE SEQRES 8 A 214 TRP THR THR PRO TYR THR PHE GLY GLY GLY THR LYS VAL SEQRES 9 A 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 A 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 A 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 A 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 A 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 A 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 A 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 A 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 A 214 PHE ASN ARG GLY GLU CYS SEQRES 1 B 221 GLN VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL ARG SEQRES 2 B 221 PRO GLY THR SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 B 221 TYR ALA PHE THR ASN TYR LEU ILE GLU TRP VAL LYS GLN SEQRES 4 B 221 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY ALA ILE ASN SEQRES 5 B 221 PRO GLY SER GLY ALA THR ASN TYR ASN GLU LYS PHE LYS SEQRES 6 B 221 ASP LYS ALA ARG LEU THR ALA ASP LYS SER SER ASN THR SEQRES 7 B 221 ALA TYR LEU GLN PHE SER SER LEU THR SER ASP ASP SER SEQRES 8 B 221 ALA VAL TYR PHE CYS ALA ARG PHE LEU GLY ASN TYR PHE SEQRES 9 B 221 ASP ASN TRP GLY GLN GLY ALA THR LEU THR VAL SER SER SEQRES 10 B 221 ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SEQRES 11 B 221 SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY SEQRES 12 B 221 CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SEQRES 13 B 221 SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR SEQRES 14 B 221 PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SEQRES 15 B 221 SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR SEQRES 16 B 221 GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN SEQRES 17 B 221 THR LYS VAL ASP LYS LYS VAL GLU 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 CYS ARG GLY GLU GLU GLN ARG PHE THR SEQRES 7 C 94 CYS TYR MET GLU HIS SER GLY ASN HIS SER THR HIS PRO SEQRES 8 C 94 VAL PRO SER HET GOL A 301 6 HET GOL A 302 6 HET GOL A 303 6 HET GOL B 301 6 HET GOL B 302 6 HET SO4 B 303 5 HET GOL C 301 6 HET GOL C 302 6 HET GOL C 303 6 HET ZN C 304 1 HETNAM GOL GLYCEROL HETNAM SO4 SULFATE ION HETNAM ZN ZINC ION HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 4 GOL 8(C3 H8 O3) FORMUL 9 SO4 O4 S 2- FORMUL 13 ZN ZN 2+ FORMUL 14 HOH *260(H2 O) HELIX 1 AA1 GLN A 79 PHE A 83 5 5 HELIX 2 AA2 SER A 121 LYS A 126 1 6 HELIX 3 AA3 LYS A 183 GLU A 187 1 5 HELIX 4 AA4 ALA B 28 TYR B 32 5 5 HELIX 5 AA5 GLU B 61 LYS B 64 5 4 HELIX 6 AA6 THR B 83 SER B 87 5 5 HELIX 7 AA7 SER B 127 LYS B 129 5 3 HELIX 8 AA8 SER B 156 ALA B 158 5 3 HELIX 9 AA9 SER B 187 LEU B 189 5 3 HELIX 10 AB1 LYS B 201 ASN B 204 5 4 HELIX 11 AB2 SER C 247 ASP C 249 5 3 HELIX 12 AB3 GLU C 276 GLN C 278 5 3 SHEET 1 AA1 4 MET A 4 SER A 7 0 SHEET 2 AA1 4 VAL A 19 ALA A 25 -1 O ARG A 24 N THR A 5 SHEET 3 AA1 4 GLN A 70 ILE A 75 -1 O LEU A 73 N ILE A 21 SHEET 4 AA1 4 PHE A 62 SER A 67 -1 N SER A 63 O LYS A 74 SHEET 1 AA2 6 SER A 10 ALA A 13 0 SHEET 2 AA2 6 THR A 102 ILE A 106 1 O GLU A 105 N LEU A 11 SHEET 3 AA2 6 GLY A 84 GLN A 90 -1 N GLY A 84 O VAL A 104 SHEET 4 AA2 6 LEU A 33 GLN A 38 -1 N GLN A 38 O SER A 85 SHEET 5 AA2 6 GLN A 45 TYR A 49 -1 O LEU A 47 N TRP A 35 SHEET 6 AA2 6 THR A 53 LEU A 54 -1 O THR A 53 N TYR A 49 SHEET 1 AA3 4 SER A 10 ALA A 13 0 SHEET 2 AA3 4 THR A 102 ILE A 106 1 O GLU A 105 N LEU A 11 SHEET 3 AA3 4 GLY A 84 GLN A 90 -1 N GLY A 84 O VAL A 104 SHEET 4 AA3 4 THR A 97 PHE A 98 -1 O THR A 97 N GLN A 90 SHEET 1 AA4 4 SER A 114 PHE A 118 0 SHEET 2 AA4 4 THR A 129 PHE A 139 -1 O LEU A 135 N PHE A 116 SHEET 3 AA4 4 TYR A 173 SER A 182 -1 O TYR A 173 N PHE A 139 SHEET 4 AA4 4 SER A 159 VAL A 163 -1 N GLN A 160 O THR A 178 SHEET 1 AA5 4 ALA A 153 LEU A 154 0 SHEET 2 AA5 4 LYS A 145 VAL A 150 -1 N VAL A 150 O ALA A 153 SHEET 3 AA5 4 VAL A 191 THR A 197 -1 O GLU A 195 N GLN A 147 SHEET 4 AA5 4 VAL A 205 ASN A 210 -1 O VAL A 205 N VAL A 196 SHEET 1 AA6 4 GLN B 3 GLN B 6 0 SHEET 2 AA6 4 VAL B 18 SER B 25 -1 O LYS B 23 N GLN B 5 SHEET 3 AA6 4 THR B 77 PHE B 82 -1 O ALA B 78 N CYS B 22 SHEET 4 AA6 4 ALA B 67 ASP B 72 -1 N ASP B 72 O THR B 77 SHEET 1 AA7 6 GLU B 10 VAL B 12 0 SHEET 2 AA7 6 ALA B 107 VAL B 111 1 O THR B 108 N GLU B 10 SHEET 3 AA7 6 ALA B 88 PHE B 95 -1 N ALA B 88 O LEU B 109 SHEET 4 AA7 6 ILE B 34 ARG B 40 -1 N VAL B 37 O PHE B 91 SHEET 5 AA7 6 GLY B 44 ILE B 51 -1 O GLU B 46 N LYS B 38 SHEET 6 AA7 6 THR B 57 TYR B 59 -1 O ASN B 58 N ALA B 50 SHEET 1 AA8 4 GLU B 10 VAL B 12 0 SHEET 2 AA8 4 ALA B 107 VAL B 111 1 O THR B 108 N GLU B 10 SHEET 3 AA8 4 ALA B 88 PHE B 95 -1 N ALA B 88 O LEU B 109 SHEET 4 AA8 4 PHE B 100 ASP B 101 -1 O ASP B 101 N ARG B 94 SHEET 1 AA9 4 SER B 120 LEU B 124 0 SHEET 2 AA9 4 THR B 135 TYR B 145 -1 O GLY B 139 N LEU B 124 SHEET 3 AA9 4 TYR B 176 PRO B 185 -1 O VAL B 184 N ALA B 136 SHEET 4 AA9 4 VAL B 163 THR B 165 -1 N HIS B 164 O VAL B 181 SHEET 1 AB1 4 THR B 131 SER B 132 0 SHEET 2 AB1 4 THR B 135 TYR B 145 -1 O THR B 135 N SER B 132 SHEET 3 AB1 4 TYR B 176 PRO B 185 -1 O VAL B 184 N ALA B 136 SHEET 4 AB1 4 VAL B 169 LEU B 170 -1 N VAL B 169 O SER B 177 SHEET 1 AB2 3 THR B 151 TRP B 154 0 SHEET 2 AB2 3 ILE B 195 HIS B 200 -1 O ASN B 197 N SER B 153 SHEET 3 AB2 3 THR B 205 LYS B 210 -1 O VAL B 207 N VAL B 198 SHEET 1 AB3 4 MET C 208 ARG C 213 0 SHEET 2 AB3 4 ASN C 220 PHE C 230 -1 O ARG C 226 N ASN C 210 SHEET 3 AB3 4 TYR C 264 CYS C 273 -1 O ILE C 272 N ILE C 221 SHEET 4 AB3 4 GLN C 251 TRP C 253 -1 N GLN C 252 O ALA C 269 SHEET 1 AB4 4 MET C 208 ARG C 213 0 SHEET 2 AB4 4 ASN C 220 PHE C 230 -1 O ARG C 226 N ASN C 210 SHEET 3 AB4 4 TYR C 264 CYS C 273 -1 O ILE C 272 N ILE C 221 SHEET 4 AB4 4 LEU C 257 PRO C 258 -1 N LEU C 257 O GLN C 265 SHEET 1 AB5 4 VAL C 244 SER C 245 0 SHEET 2 AB5 4 ILE C 236 GLN C 241 -1 N GLN C 241 O VAL C 244 SHEET 3 AB5 4 PHE C 280 HIS C 286 -1 O TYR C 283 N THR C 238 SHEET 4 AB5 4 ASN C 289 PRO C 294 -1 O HIS C 293 N CYS C 282 SSBOND 1 CYS A 23 CYS A 88 1555 1555 2.03 SSBOND 2 CYS A 134 CYS A 194 1555 1555 2.02 SSBOND 3 CYS A 214 CYS B 216 1555 1555 2.04 SSBOND 4 CYS B 22 CYS B 92 1555 1555 2.05 SSBOND 5 CYS B 140 CYS B 196 1555 1555 2.03 SSBOND 6 CYS C 225 CYS C 282 1555 1555 2.03 LINK NE2 HIS C 248 ZN ZN C 304 1555 1555 2.55 LINK ZN ZN C 304 O HOH C 404 1555 1555 1.99 LINK OD1 ASP A 185 ZN ZN C 304 1555 3544 1.95 LINK NE2 HIS A 189 ZN ZN C 304 1555 3544 2.18 CISPEP 1 SER A 7 PRO A 8 0 -4.18 CISPEP 2 THR A 94 PRO A 95 0 0.27 CISPEP 3 TYR A 140 PRO A 141 0 1.97 CISPEP 4 PHE B 146 PRO B 147 0 -2.18 CISPEP 5 GLU B 148 PRO B 149 0 2.47 CISPEP 6 TYR C 231 PRO C 232 0 3.86 SITE 1 AC1 11 GLN A 160 SER A 162 SER A 176 SER A 177 SITE 2 AC1 11 THR A 178 HOH A 408 PHE B 166 PRO B 167 SITE 3 AC1 11 SER B 177 LEU B 178 SER B 179 SITE 1 AC2 6 GLN A 37 GLN A 45 PRO A 59 HOH A 410 SITE 2 AC2 6 HOH A 434 HOH A 482 SITE 1 AC3 6 VAL A 115 LYS A 190 LYS A 207 ARG A 211 SITE 2 AC3 6 HOH A 425 SER B 132 SITE 1 AC4 9 SER A 156 GLY A 157 THR B 30 ASN B 52 SITE 2 AC4 9 GLY B 53 SER B 54 HOH B 442 ARG C 240 SITE 3 AC4 9 SER C 245 SITE 1 AC5 7 GLY A 99 GLY A 100 GLY A 101 GLN B 39 SITE 2 AC5 7 GLY B 44 LEU B 45 HOH B 424 SITE 1 AC6 3 LEU B 189 ASP B 217 HOH B 439 SITE 1 AC7 7 LYS A 149 ASN A 152 LEU A 154 ARG C 233 SITE 2 AC7 7 ASN C 234 ILE C 235 VAL C 256 SITE 1 AC8 5 ASP C 249 THR C 250 GLN C 251 GLN C 252 SITE 2 AC8 5 ALA C 269 SITE 1 AC9 4 THR B 191 THR C 224 ARG C 226 TRP C 267 SITE 1 AD1 4 ASP A 185 HIS A 189 HIS C 248 HOH C 404 CRYST1 51.549 61.833 172.368 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 0.019399 0.000000 0.000000 0.00000 SCALE2 0.000000 0.016173 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005802 0.00000 ATOM 1 N ASP A 1 9.952 -16.450 -53.530 1.00 40.35 N ANISOU 1 N ASP A 1 5850 4600 4880 -673 286 -225 N ATOM 2 CA ASP A 1 9.905 -15.848 -52.166 1.00 39.20 C ANISOU 2 CA ASP A 1 5679 4392 4822 -575 226 -166 C ATOM 3 C ASP A 1 10.985 -16.462 -51.269 1.00 38.36 C ANISOU 3 C ASP A 1 5631 4136 4808 -497 281 -173 C ATOM 4 O ASP A 1 11.052 -17.684 -51.115 1.00 39.00 O ANISOU 4 O ASP A 1 5786 4145 4889 -530 366 -238 O ATOM 5 CB ASP A 1 8.519 -16.046 -51.534 1.00 39.58 C ANISOU 5 CB ASP A 1 5713 4485 4838 -619 195 -184 C ATOM 6 CG ASP A 1 8.153 -17.519 -51.353 1.00 40.16 C ANISOU 6 CG ASP A 1 5868 4506 4886 -698 282 -278 C ATOM 7 OD1 ASP A 1 8.612 -18.364 -52.151 1.00 40.91 O ANISOU 7 OD1 ASP A 1 6021 4577 4946 -759 367 -342 O ATOM 8 OD2 ASP A 1 7.417 -17.830 -50.400 1.00 40.48 O ANISOU 8 OD2 ASP A 1 5917 4521 4942 -700 272 -290 O ATOM 9 N ILE A 2 11.834 -15.620 -50.688 1.00 36.79 N ANISOU 9 N ILE A 2 5398 3894 4686 -397 238 -106 N ATOM 10 CA ILE A 2 12.801 -16.080 -49.699 1.00 35.70 C ANISOU 10 CA ILE A 2 5295 3640 4630 -316 276 -97 C ATOM 11 C ILE A 2 12.111 -16.052 -48.340 1.00 34.58 C ANISOU 11 C ILE A 2 5146 3468 4525 -284 237 -85 C ATOM 12 O ILE A 2 11.575 -15.018 -47.941 1.00 33.93 O ANISOU 12 O ILE A 2 5008 3434 4452 -264 156 -41 O ATOM 13 CB ILE A 2 14.064 -15.190 -49.658 1.00 35.34 C ANISOU 13 CB ILE A 2 5209 3578 4642 -235 248 -34 C ATOM 14 CG1 ILE A 2 14.733 -15.111 -51.040 1.00 35.74 C ANISOU 14 CG1 ILE A 2 5260 3667 4653 -265 282 -40 C ATOM 15 CG2 ILE A 2 15.046 -15.700 -48.607 1.00 35.09 C ANISOU 15 CG2 ILE A 2 5200 3450 4684 -152 286 -18 C ATOM 16 CD1 ILE A 2 15.439 -16.374 -51.491 1.00 36.30 C ANISOU 16 CD1 ILE A 2 5400 3675 4718 -278 391 -93 C ATOM 17 N GLN A 3 12.102 -17.192 -47.651 1.00 34.03 N ANISOU 17 N GLN A 3 5136 3318 4476 -280 302 -121 N ATOM 18 CA GLN A 3 11.650 -17.269 -46.265 1.00 33.15 C ANISOU 18 CA GLN A 3 5023 3167 4407 -238 275 -106 C ATOM 19 C GLN A 3 12.870 -17.080 -45.364 1.00 32.35 C ANISOU 19 C GLN A 3 4909 3001 4383 -133 274 -54 C ATOM 20 O GLN A 3 13.901 -17.728 -45.570 1.00 32.32 O ANISOU 20 O GLN A 3 4938 2943 4401 -98 345 -54 O ATOM 21 CB GLN A 3 10.984 -18.620 -45.984 1.00 33.65 C ANISOU 21 CB GLN A 3 5158 3179 4449 -291 351 -168 C ATOM 22 N MET A 4 12.755 -16.177 -44.390 1.00 31.31 N ANISOU 22 N MET A 4 4725 2884 4286 -84 197 -9 N ATOM 23 CA MET A 4 13.811 -15.941 -43.404 1.00 30.76 C ANISOU 23 CA MET A 4 4632 2776 4279 4 187 39 C ATOM 24 C MET A 4 13.394 -16.566 -42.080 1.00 30.17 C ANISOU 24 C MET A 4 4576 2658 4228 33 196 38 C ATOM 25 O MET A 4 12.354 -16.208 -41.524 1.00 29.82 O ANISOU 25 O MET A 4 4518 2640 4175 11 146 32 O ATOM 26 CB MET A 4 14.059 -14.440 -43.206 1.00 30.35 C ANISOU 26 CB MET A 4 4511 2772 4249 30 102 83 C ATOM 27 CG MET A 4 14.497 -13.683 -44.457 1.00 30.54 C ANISOU 27 CG MET A 4 4510 2839 4253 7 89 96 C ATOM 28 SD MET A 4 16.055 -14.225 -45.198 1.00 31.19 S ANISOU 28 SD MET A 4 4608 2895 4348 37 160 103 S ATOM 29 CE MET A 4 17.219 -13.901 -43.880 1.00 31.00 C ANISOU 29 CE MET A 4 4541 2850 4385 123 141 153 C ATOM 30 N THR A 5 14.210 -17.494 -41.587 1.00 30.04 N ANISOU 30 N THR A 5 4591 2581 4242 88 264 52 N ATOM 31 CA THR A 5 13.981 -18.152 -40.305 1.00 29.78 C ANISOU 31 CA THR A 5 4576 2507 4233 128 282 64 C ATOM 32 C THR A 5 14.931 -17.547 -39.267 1.00 29.26 C ANISOU 32 C THR A 5 4449 2461 4208 210 239 126 C ATOM 33 O THR A 5 16.142 -17.771 -39.328 1.00 29.48 O ANISOU 33 O THR A 5 4464 2480 4256 268 276 162 O ATOM 34 CB THR A 5 14.211 -19.669 -40.430 1.00 30.50 C ANISOU 34 CB THR A 5 4745 2515 4327 139 402 46 C ATOM 35 OG1 THR A 5 13.471 -20.161 -41.550 1.00 30.88 O ANISOU 35 OG1 THR A 5 4849 2556 4329 46 447 -21 O ATOM 36 CG2 THR A 5 13.767 -20.406 -39.162 1.00 30.59 C ANISOU 36 CG2 THR A 5 4782 2481 4357 171 427 59 C ATOM 37 N GLN A 6 14.372 -16.774 -38.334 1.00 28.57 N ANISOU 37 N GLN A 6 4321 2408 4126 211 162 136 N ATOM 38 CA GLN A 6 15.134 -16.129 -37.263 1.00 28.32 C ANISOU 38 CA GLN A 6 4229 2409 4122 269 116 183 C ATOM 39 C GLN A 6 14.952 -16.862 -35.940 1.00 28.58 C ANISOU 39 C GLN A 6 4270 2422 4166 312 134 204 C ATOM 40 O GLN A 6 13.816 -17.073 -35.510 1.00 28.52 O ANISOU 40 O GLN A 6 4288 2401 4147 281 123 177 O ATOM 41 CB GLN A 6 14.676 -14.681 -37.083 1.00 27.53 C ANISOU 41 CB GLN A 6 4081 2359 4022 238 26 178 C ATOM 42 CG GLN A 6 15.534 -13.888 -36.101 1.00 27.31 C ANISOU 42 CG GLN A 6 3990 2371 4015 276 -18 213 C ATOM 43 CD GLN A 6 15.273 -12.394 -36.143 1.00 26.66 C ANISOU 43 CD GLN A 6 3871 2322 3938 242 -86 204 C ATOM 44 OE1 GLN A 6 14.650 -11.885 -37.068 1.00 26.28 O ANISOU 44 OE1 GLN A 6 3834 2271 3879 202 -100 186 O ATOM 45 NE2 GLN A 6 15.741 -11.689 -35.127 1.00 26.59 N ANISOU 45 NE2 GLN A 6 3816 2346 3941 256 -124 218 N ATOM 46 N SER A 7 16.063 -17.204 -35.285 1.00 29.08 N ANISOU 46 N SER A 7 4305 2496 4247 385 160 257 N ATOM 47 CA SER A 7 16.033 -17.856 -33.975 1.00 29.57 C ANISOU 47 CA SER A 7 4365 2554 4317 437 176 292 C ATOM 48 C SER A 7 17.100 -17.283 -33.027 1.00 29.77 C ANISOU 48 C SER A 7 4307 2657 4347 492 135 348 C ATOM 49 O SER A 7 18.161 -16.855 -33.489 1.00 29.85 O ANISOU 49 O SER A 7 4275 2705 4360 509 131 371 O ATOM 50 CB SER A 7 16.248 -19.362 -34.129 1.00 30.26 C ANISOU 50 CB SER A 7 4516 2567 4413 482 288 311 C ATOM 51 OG SER A 7 17.466 -19.622 -34.798 1.00 30.85 O ANISOU 51 OG SER A 7 4582 2640 4499 529 340 345 O ATOM 52 N PRO A 8 16.844 -17.275 -31.713 1.00 29.95 N ANISOU 52 N PRO A 8 4302 2713 4364 513 105 370 N ATOM 53 CA PRO A 8 15.575 -17.696 -31.108 1.00 30.01 C ANISOU 53 CA PRO A 8 4353 2682 4366 490 105 343 C ATOM 54 C PRO A 8 14.549 -16.562 -31.130 1.00 29.52 C ANISOU 54 C PRO A 8 4282 2640 4296 416 26 287 C ATOM 55 O PRO A 8 14.923 -15.398 -31.304 1.00 29.37 O ANISOU 55 O PRO A 8 4216 2666 4278 394 -30 278 O ATOM 56 CB PRO A 8 15.978 -18.053 -29.672 1.00 30.30 C ANISOU 56 CB PRO A 8 4349 2766 4398 554 105 402 C ATOM 57 CG PRO A 8 17.151 -17.180 -29.385 1.00 30.36 C ANISOU 57 CG PRO A 8 4270 2868 4397 573 57 435 C ATOM 58 CD PRO A 8 17.874 -16.995 -30.694 1.00 30.39 C ANISOU 58 CD PRO A 8 4279 2856 4413 566 79 428 C ATOM 59 N ALA A 9 13.273 -16.904 -30.964 1.00 29.65 N ANISOU 59 N ALA A 9 4342 2619 4304 381 29 252 N ATOM 60 CA ALA A 9 12.190 -15.906 -30.924 1.00 29.44 C ANISOU 60 CA ALA A 9 4305 2612 4268 322 -37 208 C ATOM 61 C ALA A 9 12.285 -14.991 -29.703 1.00 29.60 C ANISOU 61 C ALA A 9 4268 2690 4288 333 -100 218 C ATOM 62 O ALA A 9 11.889 -13.829 -29.767 1.00 29.06 O ANISOU 62 O ALA A 9 4177 2644 4222 297 -153 192 O ATOM 63 CB ALA A 9 10.829 -16.586 -30.961 1.00 29.37 C ANISOU 63 CB ALA A 9 4349 2565 4245 283 -15 174 C ATOM 64 N SER A 10 12.780 -15.527 -28.588 1.00 30.40 N ANISOU 64 N SER A 10 4349 2817 4386 381 -87 258 N ATOM 65 CA SER A 10 13.077 -14.718 -27.407 1.00 30.82 C ANISOU 65 CA SER A 10 4341 2940 4429 386 -140 267 C ATOM 66 C SER A 10 14.346 -15.184 -26.717 1.00 31.54 C ANISOU 66 C SER A 10 4386 3088 4510 447 -122 329 C ATOM 67 O SER A 10 14.773 -16.338 -26.860 1.00 31.81 O ANISOU 67 O SER A 10 4442 3095 4548 501 -59 374 O ATOM 68 CB SER A 10 11.904 -14.713 -26.425 1.00 30.97 C ANISOU 68 CB SER A 10 4371 2960 4437 369 -163 245 C ATOM 69 OG SER A 10 11.527 -16.027 -26.080 1.00 31.62 O ANISOU 69 OG SER A 10 4493 3006 4514 400 -110 269 O ATOM 70 N LEU A 11 14.926 -14.265 -25.954 1.00 31.79 N ANISOU 70 N LEU A 11 4351 3202 4525 435 -172 331 N ATOM 71 CA LEU A 11 16.278 -14.403 -25.445 1.00 32.52 C ANISOU 71 CA LEU A 11 4377 3381 4598 479 -167 388 C ATOM 72 C LEU A 11 16.376 -13.657 -24.116 1.00 32.59 C ANISOU 72 C LEU A 11 4323 3486 4573 453 -220 380 C ATOM 73 O LEU A 11 16.017 -12.482 -24.046 1.00 32.27 O ANISOU 73 O LEU A 11 4276 3452 4533 387 -265 321 O ATOM 74 CB LEU A 11 17.242 -13.808 -26.480 1.00 32.92 C ANISOU 74 CB LEU A 11 4404 3443 4660 464 -170 386 C ATOM 75 CG LEU A 11 18.701 -14.251 -26.510 1.00 33.61 C ANISOU 75 CG LEU A 11 4434 3601 4735 521 -142 454 C ATOM 76 CD1 LEU A 11 19.338 -13.835 -27.827 1.00 33.57 C ANISOU 76 CD1 LEU A 11 4433 3573 4750 503 -132 442 C ATOM 77 CD2 LEU A 11 19.482 -13.677 -25.342 1.00 34.18 C ANISOU 77 CD2 LEU A 11 4413 3808 4765 513 -185 477 C ATOM 78 N SER A 12 16.842 -14.348 -23.073 1.00 32.98 N ANISOU 78 N SER A 12 4329 3611 4591 505 -209 441 N ATOM 79 CA SER A 12 17.052 -13.756 -21.748 1.00 33.11 C ANISOU 79 CA SER A 12 4277 3742 4562 479 -255 439 C ATOM 80 C SER A 12 18.543 -13.616 -21.491 1.00 33.22 C ANISOU 80 C SER A 12 4199 3885 4539 499 -263 491 C ATOM 81 O SER A 12 19.259 -14.618 -21.482 1.00 33.87 O ANISOU 81 O SER A 12 4256 4000 4614 581 -220 576 O ATOM 82 CB SER A 12 16.435 -14.638 -20.663 1.00 33.56 C ANISOU 82 CB SER A 12 4342 3813 4598 522 -240 476 C ATOM 83 OG SER A 12 15.074 -14.899 -20.940 1.00 33.57 O ANISOU 83 OG SER A 12 4426 3701 4630 506 -227 433 O ATOM 84 N ALA A 13 19.012 -12.386 -21.285 1.00 32.71 N ANISOU 84 N ALA A 13 4082 3894 4450 423 -310 443 N ATOM 85 CA ALA A 13 20.430 -12.143 -21.007 1.00 33.11 C ANISOU 85 CA ALA A 13 4034 4089 4456 422 -323 485 C ATOM 86 C ALA A 13 20.634 -11.018 -20.001 1.00 33.11 C ANISOU 86 C ALA A 13 3972 4205 4402 329 -375 430 C ATOM 87 O ALA A 13 19.740 -10.212 -19.765 1.00 32.34 O ANISOU 87 O ALA A 13 3919 4052 4317 260 -397 349 O ATOM 88 CB ALA A 13 21.177 -11.845 -22.296 1.00 33.05 C ANISOU 88 CB ALA A 13 4030 4048 4479 415 -307 483 C ATOM 89 N SER A 14 21.822 -10.994 -19.405 1.00 33.69 N ANISOU 89 N SER A 14 3941 4446 4413 329 -388 478 N ATOM 90 CA SER A 14 22.210 -9.986 -18.418 1.00 34.09 C ANISOU 90 CA SER A 14 3920 4636 4398 229 -432 427 C ATOM 91 C SER A 14 23.150 -8.987 -19.055 1.00 34.14 C ANISOU 91 C SER A 14 3890 4684 4399 151 -443 385 C ATOM 92 O SER A 14 23.750 -9.272 -20.092 1.00 34.20 O ANISOU 92 O SER A 14 3898 4657 4439 194 -420 425 O ATOM 93 CB SER A 14 22.918 -10.650 -17.235 1.00 34.92 C ANISOU 93 CB SER A 14 3918 4932 4419 273 -442 512 C ATOM 94 OG SER A 14 22.033 -11.488 -16.519 1.00 34.72 O ANISOU 94 OG SER A 14 3926 4874 4393 335 -431 547 O ATOM 95 N VAL A 15 23.289 -7.825 -18.420 1.00 34.34 N ANISOU 95 N VAL A 15 3884 4783 4382 31 -473 303 N ATOM 96 CA VAL A 15 24.274 -6.829 -18.837 1.00 34.80 C ANISOU 96 CA VAL A 15 3897 4905 4422 -62 -480 261 C ATOM 97 C VAL A 15 25.675 -7.440 -18.698 1.00 35.71 C ANISOU 97 C VAL A 15 3889 5205 4474 -18 -484 357 C ATOM 98 O VAL A 15 25.985 -8.073 -17.685 1.00 36.56 O ANISOU 98 O VAL A 15 3915 5463 4512 20 -497 421 O ATOM 99 CB VAL A 15 24.147 -5.510 -18.025 1.00 35.21 C ANISOU 99 CB VAL A 15 3941 5006 4432 -209 -499 149 C ATOM 100 CG1 VAL A 15 25.346 -4.588 -18.245 1.00 35.94 C ANISOU 100 CG1 VAL A 15 3966 5203 4484 -316 -503 112 C ATOM 101 CG2 VAL A 15 22.859 -4.787 -18.388 1.00 34.40 C ANISOU 101 CG2 VAL A 15 3960 4706 4402 -244 -483 61 C ATOM 102 N GLY A 16 26.496 -7.274 -19.733 1.00 35.63 N ANISOU 102 N GLY A 16 3863 5187 4488 -17 -469 374 N ATOM 103 CA GLY A 16 27.828 -7.880 -19.793 1.00 36.43 C ANISOU 103 CA GLY A 16 3851 5453 4539 39 -465 474 C ATOM 104 C GLY A 16 27.927 -9.187 -20.571 1.00 36.08 C ANISOU 104 C GLY A 16 3828 5336 4544 194 -422 582 C ATOM 105 O GLY A 16 29.021 -9.577 -20.969 1.00 36.62 O ANISOU 105 O GLY A 16 3821 5500 4593 245 -406 659 O ATOM 106 N GLU A 17 26.805 -9.872 -20.789 1.00 35.27 N ANISOU 106 N GLU A 17 3828 5069 4502 267 -398 587 N ATOM 107 CA GLU A 17 26.814 -11.141 -21.522 1.00 35.12 C ANISOU 107 CA GLU A 17 3848 4965 4533 405 -345 677 C ATOM 108 C GLU A 17 26.886 -10.937 -23.036 1.00 34.42 C ANISOU 108 C GLU A 17 3826 4739 4513 403 -317 649 C ATOM 109 O GLU A 17 26.577 -9.860 -23.552 1.00 33.80 O ANISOU 109 O GLU A 17 3793 4591 4461 305 -338 557 O ATOM 110 CB GLU A 17 25.592 -11.988 -21.159 1.00 34.83 C ANISOU 110 CB GLU A 17 3894 4811 4528 471 -324 689 C ATOM 111 CG GLU A 17 25.605 -12.471 -19.716 1.00 35.77 C ANISOU 111 CG GLU A 17 3944 5069 4580 503 -339 747 C ATOM 112 CD GLU A 17 24.497 -13.460 -19.407 1.00 35.58 C ANISOU 112 CD GLU A 17 4000 4930 4589 580 -307 774 C ATOM 113 OE1 GLU A 17 23.402 -13.332 -19.990 1.00 35.01 O ANISOU 113 OE1 GLU A 17 4039 4685 4579 555 -299 703 O ATOM 114 OE2 GLU A 17 24.712 -14.359 -18.567 1.00 36.58 O ANISOU 114 OE2 GLU A 17 4076 5146 4676 665 -288 870 O ATOM 115 N THR A 18 27.314 -11.985 -23.733 1.00 34.42 N ANISOU 115 N THR A 18 3832 4705 4540 514 -263 733 N ATOM 116 CA THR A 18 27.344 -12.002 -25.188 1.00 33.90 C ANISOU 116 CA THR A 18 3835 4510 4537 526 -227 715 C ATOM 117 C THR A 18 26.194 -12.860 -25.694 1.00 33.06 C ANISOU 117 C THR A 18 3848 4222 4490 586 -184 708 C ATOM 118 O THR A 18 25.989 -13.973 -25.207 1.00 33.55 O ANISOU 118 O THR A 18 3920 4276 4550 677 -145 775 O ATOM 119 CB THR A 18 28.677 -12.554 -25.714 1.00 34.63 C ANISOU 119 CB THR A 18 3854 4689 4616 602 -187 805 C ATOM 120 OG1 THR A 18 29.738 -11.704 -25.271 1.00 35.41 O ANISOU 120 OG1 THR A 18 3834 4969 4651 531 -230 805 O ATOM 121 CG2 THR A 18 28.685 -12.613 -27.246 1.00 34.21 C ANISOU 121 CG2 THR A 18 3875 4499 4624 613 -146 783 C ATOM 122 N VAL A 19 25.454 -12.336 -26.669 1.00 32.01 N ANISOU 122 N VAL A 19 3805 3952 4407 530 -187 630 N ATOM 123 CA VAL A 19 24.309 -13.037 -27.253 1.00 31.19 C ANISOU 123 CA VAL A 19 3813 3686 4352 564 -150 611 C ATOM 124 C VAL A 19 24.444 -13.087 -28.769 1.00 30.67 C ANISOU 124 C VAL A 19 3800 3525 4327 566 -113 595 C ATOM 125 O VAL A 19 25.059 -12.208 -29.375 1.00 30.37 O ANISOU 125 O VAL A 19 3732 3517 4288 513 -134 570 O ATOM 126 CB VAL A 19 22.959 -12.403 -26.841 1.00 30.67 C ANISOU 126 CB VAL A 19 3805 3551 4297 493 -192 530 C ATOM 127 CG1 VAL A 19 22.773 -12.508 -25.335 1.00 31.00 C ANISOU 127 CG1 VAL A 19 3800 3682 4296 497 -220 547 C ATOM 128 CG2 VAL A 19 22.837 -10.950 -27.293 1.00 30.31 C ANISOU 128 CG2 VAL A 19 3765 3489 4260 390 -236 451 C ATOM 129 N THR A 20 23.871 -14.131 -29.363 1.00 30.30 N ANISOU 129 N THR A 20 3834 3367 4313 622 -54 608 N ATOM 130 CA THR A 20 23.939 -14.360 -30.799 1.00 30.14 C ANISOU 130 CA THR A 20 3870 3257 4325 626 -9 593 C ATOM 131 C THR A 20 22.544 -14.662 -31.324 1.00 29.54 C ANISOU 131 C THR A 20 3899 3049 4276 598 6 535 C ATOM 132 O THR A 20 21.829 -15.473 -30.745 1.00 29.55 O ANISOU 132 O THR A 20 3940 3008 4280 631 31 545 O ATOM 133 CB THR A 20 24.880 -15.535 -31.117 1.00 30.87 C ANISOU 133 CB THR A 20 3949 3358 4422 729 74 674 C ATOM 134 OG1 THR A 20 26.172 -15.261 -30.568 1.00 31.55 O ANISOU 134 OG1 THR A 20 3922 3590 4473 758 56 737 O ATOM 135 CG2 THR A 20 25.007 -15.762 -32.629 1.00 30.79 C ANISOU 135 CG2 THR A 20 3998 3261 4440 727 126 653 C ATOM 136 N ILE A 21 22.167 -13.990 -32.409 1.00 29.13 N ANISOU 136 N ILE A 21 3886 2942 4240 536 -9 479 N ATOM 137 CA ILE A 21 20.885 -14.196 -33.077 1.00 28.68 C ANISOU 137 CA ILE A 21 3916 2781 4198 501 3 426 C ATOM 138 C ILE A 21 21.202 -14.649 -34.490 1.00 28.93 C ANISOU 138 C ILE A 21 3989 2760 4242 508 59 423 C ATOM 139 O ILE A 21 22.026 -14.027 -35.151 1.00 29.17 O ANISOU 139 O ILE A 21 3984 2825 4272 494 50 428 O ATOM 140 CB ILE A 21 20.076 -12.885 -33.158 1.00 28.08 C ANISOU 140 CB ILE A 21 3845 2700 4124 419 -66 367 C ATOM 141 CG1 ILE A 21 19.769 -12.354 -31.753 1.00 27.99 C ANISOU 141 CG1 ILE A 21 3795 2739 4100 404 -118 360 C ATOM 142 CG2 ILE A 21 18.794 -13.092 -33.968 1.00 27.73 C ANISOU 142 CG2 ILE A 21 3877 2571 4088 384 -55 322 C ATOM 143 CD1 ILE A 21 19.323 -10.907 -31.727 1.00 27.68 C ANISOU 143 CD1 ILE A 21 3748 2705 4066 330 -175 311 C ATOM 144 N THR A 22 20.544 -15.711 -34.954 1.00 28.88 N ANISOU 144 N THR A 22 4059 2671 4242 522 122 410 N ATOM 145 CA THR A 22 20.779 -16.244 -36.297 1.00 29.06 C ANISOU 145 CA THR A 22 4130 2640 4270 522 187 397 C ATOM 146 C THR A 22 19.569 -16.028 -37.215 1.00 28.47 C ANISOU 146 C THR A 22 4118 2512 4187 443 175 329 C ATOM 147 O THR A 22 18.427 -16.019 -36.754 1.00 27.97 O ANISOU 147 O THR A 22 4081 2428 4117 410 148 299 O ATOM 148 CB THR A 22 21.121 -17.747 -36.249 1.00 29.85 C ANISOU 148 CB THR A 22 4274 2687 4380 597 291 435 C ATOM 149 OG1 THR A 22 20.004 -18.479 -35.737 1.00 30.10 O ANISOU 149 OG1 THR A 22 4368 2657 4413 588 315 412 O ATOM 150 CG2 THR A 22 22.328 -17.994 -35.363 1.00 30.40 C ANISOU 150 CG2 THR A 22 4271 2826 4452 687 306 519 C ATOM 151 N CYS A 23 19.841 -15.835 -38.507 1.00 28.43 N ANISOU 151 N CYS A 23 4128 2498 4176 414 194 310 N ATOM 152 CA CYS A 23 18.813 -15.824 -39.554 1.00 28.14 C ANISOU 152 CA CYS A 23 4147 2425 4120 343 198 253 C ATOM 153 C CYS A 23 19.255 -16.754 -40.683 1.00 28.51 C ANISOU 153 C CYS A 23 4244 2429 4159 348 289 241 C ATOM 154 O CYS A 23 20.345 -16.588 -41.235 1.00 28.85 O ANISOU 154 O CYS A 23 4260 2493 4208 374 309 267 O ATOM 155 CB CYS A 23 18.547 -14.404 -40.088 1.00 27.63 C ANISOU 155 CB CYS A 23 4047 2405 4047 287 121 238 C ATOM 156 SG CYS A 23 17.291 -13.496 -39.141 1.00 27.40 S ANISOU 156 SG CYS A 23 4001 2392 4018 252 38 220 S ATOM 157 N ARG A 24 18.412 -17.736 -41.003 1.00 28.54 N ANISOU 157 N ARG A 24 4323 2372 4147 317 349 199 N ATOM 158 CA ARG A 24 18.663 -18.677 -42.091 1.00 29.02 C ANISOU 158 CA ARG A 24 4447 2383 4196 304 448 171 C ATOM 159 C ARG A 24 17.692 -18.405 -43.238 1.00 28.84 C ANISOU 159 C ARG A 24 4454 2374 4128 203 431 106 C ATOM 160 O ARG A 24 16.480 -18.440 -43.036 1.00 28.63 O ANISOU 160 O ARG A 24 4450 2350 4080 147 405 70 O ATOM 161 CB ARG A 24 18.499 -20.122 -41.600 1.00 29.59 C ANISOU 161 CB ARG A 24 4590 2371 4281 340 550 168 C ATOM 162 N ALA A 25 18.230 -18.129 -44.428 1.00 29.03 N ANISOU 162 N ALA A 25 4474 2421 4134 179 447 96 N ATOM 163 CA ALA A 25 17.427 -17.906 -45.640 1.00 28.99 C ANISOU 163 CA ALA A 25 4491 2448 4076 84 438 42 C ATOM 164 C ALA A 25 17.151 -19.222 -46.379 1.00 29.66 C ANISOU 164 C ALA A 25 4664 2476 4131 36 550 -20 C ATOM 165 O ALA A 25 17.984 -20.124 -46.382 1.00 30.05 O ANISOU 165 O ALA A 25 4755 2459 4205 87 647 -13 O ATOM 166 CB ALA A 25 18.138 -16.932 -46.563 1.00 28.90 C ANISOU 166 CB ALA A 25 4431 2494 4055 78 401 64 C ATOM 167 N SER A 26 15.982 -19.313 -47.012 1.00 29.82 N ANISOU 167 N SER A 26 4712 2526 4094 -64 543 -80 N ATOM 168 CA SER A 26 15.572 -20.516 -47.759 1.00 30.45 C ANISOU 168 CA SER A 26 4879 2561 4132 -139 650 -156 C ATOM 169 C SER A 26 16.326 -20.709 -49.080 1.00 30.96 C ANISOU 169 C SER A 26 4965 2630 4168 -164 715 -182 C ATOM 170 O SER A 26 16.359 -21.818 -49.620 1.00 31.82 O ANISOU 170 O SER A 26 5155 2677 4256 -204 832 -241 O ATOM 171 CB SER A 26 14.063 -20.489 -48.022 1.00 30.48 C ANISOU 171 CB SER A 26 4890 2621 4070 -251 614 -213 C ATOM 172 OG SER A 26 13.697 -19.340 -48.770 1.00 30.14 O ANISOU 172 OG SER A 26 4779 2690 3982 -294 522 -200 O ATOM 173 N GLY A 27 16.905 -19.627 -49.605 1.00 30.56 N ANISOU 173 N GLY A 27 4846 2651 4116 -145 646 -140 N ATOM 174 CA GLY A 27 17.807 -19.683 -50.759 1.00 30.92 C ANISOU 174 CA GLY A 27 4900 2706 4143 -150 700 -149 C ATOM 175 C GLY A 27 18.934 -18.679 -50.601 1.00 30.45 C ANISOU 175 C GLY A 27 4764 2677 4127 -67 641 -70 C ATOM 176 O GLY A 27 18.901 -17.840 -49.696 1.00 29.97 O ANISOU 176 O GLY A 27 4645 2641 4102 -22 553 -18 O ATOM 177 N ASN A 28 19.932 -18.765 -51.479 1.00 30.73 N ANISOU 177 N ASN A 28 4803 2714 4158 -52 695 -67 N ATOM 178 CA ASN A 28 21.089 -17.868 -51.439 1.00 30.33 C ANISOU 178 CA ASN A 28 4681 2699 4145 17 650 3 C ATOM 179 C ASN A 28 20.617 -16.424 -51.621 1.00 29.58 C ANISOU 179 C ASN A 28 4516 2692 4030 -19 529 31 C ATOM 180 O ASN A 28 19.954 -16.112 -52.611 1.00 29.71 O ANISOU 180 O ASN A 28 4535 2766 3988 -98 511 2 O ATOM 181 CB ASN A 28 22.095 -18.243 -52.537 1.00 31.02 C ANISOU 181 CB ASN A 28 4788 2782 4218 23 735 -7 C ATOM 182 CG ASN A 28 23.430 -17.511 -52.414 1.00 30.96 C ANISOU 182 CG ASN A 28 4708 2804 4251 101 707 66 C ATOM 183 OD1 ASN A 28 23.606 -16.597 -51.601 1.00 30.35 O ANISOU 183 OD1 ASN A 28 4563 2761 4206 137 619 120 O ATOM 184 ND2 ASN A 28 24.387 -17.917 -53.241 1.00 31.67 N ANISOU 184 ND2 ASN A 28 4812 2886 4336 121 788 63 N ATOM 185 N ILE A 29 20.945 -15.565 -50.657 1.00 28.79 N ANISOU 185 N ILE A 29 4356 2604 3978 37 455 90 N ATOM 186 CA ILE A 29 20.611 -14.135 -50.731 1.00 28.16 C ANISOU 186 CA ILE A 29 4215 2590 3894 14 354 123 C ATOM 187 C ILE A 29 21.843 -13.250 -50.941 1.00 28.13 C ANISOU 187 C ILE A 29 4155 2616 3918 51 333 175 C ATOM 188 O ILE A 29 21.734 -12.023 -50.895 1.00 27.57 O ANISOU 188 O ILE A 29 4038 2584 3855 40 260 209 O ATOM 189 CB ILE A 29 19.780 -13.656 -49.514 1.00 27.56 C ANISOU 189 CB ILE A 29 4119 2509 3844 25 282 138 C ATOM 190 CG1 ILE A 29 20.529 -13.848 -48.186 1.00 27.39 C ANISOU 190 CG1 ILE A 29 4078 2449 3880 103 284 170 C ATOM 191 CG2 ILE A 29 18.440 -14.373 -49.479 1.00 27.60 C ANISOU 191 CG2 ILE A 29 4172 2504 3811 -28 295 86 C ATOM 192 CD1 ILE A 29 19.823 -13.225 -47.000 1.00 26.87 C ANISOU 192 CD1 ILE A 29 3986 2386 3837 111 210 184 C ATOM 193 N HIS A 30 23.004 -13.869 -51.182 1.00 28.58 N ANISOU 193 N HIS A 30 4218 2653 3989 94 402 183 N ATOM 194 CA HIS A 30 24.212 -13.157 -51.617 1.00 28.77 C ANISOU 194 CA HIS A 30 4189 2715 4026 117 396 226 C ATOM 195 C HIS A 30 24.596 -11.993 -50.695 1.00 28.12 C ANISOU 195 C HIS A 30 4040 2660 3985 141 317 275 C ATOM 196 O HIS A 30 24.947 -10.898 -51.158 1.00 27.99 O ANISOU 196 O HIS A 30 3982 2684 3967 118 277 302 O ATOM 197 CB HIS A 30 24.036 -12.673 -53.061 1.00 29.22 C ANISOU 197 CB HIS A 30 4250 2818 4033 53 394 213 C ATOM 198 CG HIS A 30 23.671 -13.765 -54.018 1.00 29.96 C ANISOU 198 CG HIS A 30 4410 2898 4077 11 474 154 C ATOM 199 ND1 HIS A 30 24.605 -14.413 -54.795 1.00 30.73 N ANISOU 199 ND1 HIS A 30 4527 2986 4164 26 560 142 N ATOM 200 CD2 HIS A 30 22.479 -14.335 -54.309 1.00 30.18 C ANISOU 200 CD2 HIS A 30 4487 2922 4058 -51 488 99 C ATOM 201 CE1 HIS A 30 24.003 -15.330 -55.531 1.00 31.23 C ANISOU 201 CE1 HIS A 30 4657 3033 4178 -29 627 77 C ATOM 202 NE2 HIS A 30 22.711 -15.303 -55.256 1.00 30.94 N ANISOU 202 NE2 HIS A 30 4637 3003 4114 -81 583 48 N ATOM 203 N SER A 31 24.501 -12.248 -49.391 1.00 27.66 N ANISOU 203 N SER A 31 3973 2578 3959 183 301 285 N ATOM 204 CA SER A 31 24.838 -11.279 -48.339 1.00 27.16 C ANISOU 204 CA SER A 31 3849 2540 3929 199 234 320 C ATOM 205 C SER A 31 24.038 -9.969 -48.368 1.00 26.47 C ANISOU 205 C SER A 31 3748 2469 3841 146 158 321 C ATOM 206 O SER A 31 24.454 -8.995 -47.750 1.00 26.23 O ANISOU 206 O SER A 31 3672 2459 3836 145 114 345 O ATOM 207 CB SER A 31 26.350 -10.989 -48.334 1.00 27.56 C ANISOU 207 CB SER A 31 3840 2634 3997 233 248 362 C ATOM 208 OG SER A 31 27.094 -12.185 -48.191 1.00 28.19 O ANISOU 208 OG SER A 31 3928 2702 4083 299 323 374 O ATOM 209 N TYR A 32 22.885 -9.953 -49.044 1.00 26.08 N ANISOU 209 N TYR A 32 3737 2413 3760 103 149 296 N ATOM 210 CA TYR A 32 22.004 -8.784 -49.055 1.00 25.55 C ANISOU 210 CA TYR A 32 3658 2359 3692 67 87 307 C ATOM 211 C TYR A 32 21.056 -8.935 -47.885 1.00 25.06 C ANISOU 211 C TYR A 32 3607 2271 3644 77 55 291 C ATOM 212 O TYR A 32 19.884 -9.277 -48.050 1.00 24.89 O ANISOU 212 O TYR A 32 3616 2247 3595 53 50 268 O ATOM 213 CB TYR A 32 21.243 -8.658 -50.377 1.00 25.67 C ANISOU 213 CB TYR A 32 3693 2403 3657 20 91 300 C ATOM 214 CG TYR A 32 22.120 -8.222 -51.512 1.00 25.96 C ANISOU 214 CG TYR A 32 3713 2473 3680 6 112 323 C ATOM 215 CD1 TYR A 32 22.546 -6.899 -51.610 1.00 26.00 C ANISOU 215 CD1 TYR A 32 3680 2492 3708 1 80 366 C ATOM 216 CD2 TYR A 32 22.539 -9.123 -52.483 1.00 26.39 C ANISOU 216 CD2 TYR A 32 3791 2540 3697 -4 172 299 C ATOM 217 CE1 TYR A 32 23.362 -6.484 -52.649 1.00 26.35 C ANISOU 217 CE1 TYR A 32 3707 2566 3738 -13 101 390 C ATOM 218 CE2 TYR A 32 23.354 -8.721 -53.525 1.00 26.75 C ANISOU 218 CE2 TYR A 32 3818 2619 3727 -17 192 321 C ATOM 219 CZ TYR A 32 23.767 -7.400 -53.600 1.00 26.75 C ANISOU 219 CZ TYR A 32 3776 2638 3751 -21 154 369 C ATOM 220 OH TYR A 32 24.566 -6.986 -54.635 1.00 27.17 O ANISOU 220 OH TYR A 32 3810 2725 3787 -36 175 393 O ATOM 221 N LEU A 33 21.601 -8.694 -46.699 1.00 24.80 N ANISOU 221 N LEU A 33 3545 2228 3649 107 36 304 N ATOM 222 CA LEU A 33 20.886 -8.847 -45.450 1.00 24.41 C ANISOU 222 CA LEU A 33 3501 2158 3615 122 8 292 C ATOM 223 C LEU A 33 21.222 -7.676 -44.540 1.00 23.98 C ANISOU 223 C LEU A 33 3405 2113 3595 119 -37 309 C ATOM 224 O LEU A 33 22.381 -7.252 -44.468 1.00 24.10 O ANISOU 224 O LEU A 33 3382 2152 3623 123 -34 328 O ATOM 225 CB LEU A 33 21.264 -10.169 -44.781 1.00 24.76 C ANISOU 225 CB LEU A 33 3560 2184 3664 166 51 283 C ATOM 226 CG LEU A 33 20.475 -10.495 -43.503 1.00 24.66 C ANISOU 226 CG LEU A 33 3557 2150 3662 182 28 271 C ATOM 227 CD1 LEU A 33 19.956 -11.922 -43.524 1.00 24.96 C ANISOU 227 CD1 LEU A 33 3649 2151 3684 196 82 246 C ATOM 228 CD2 LEU A 33 21.300 -10.245 -42.247 1.00 24.77 C ANISOU 228 CD2 LEU A 33 3522 2186 3702 217 8 295 C ATOM 229 N ALA A 34 20.205 -7.145 -43.868 1.00 23.41 N ANISOU 229 N ALA A 34 3341 2024 3532 108 -75 300 N ATOM 230 CA ALA A 34 20.405 -6.095 -42.876 1.00 23.17 C ANISOU 230 CA ALA A 34 3281 1993 3531 99 -109 304 C ATOM 231 C ALA A 34 19.756 -6.482 -41.560 1.00 22.74 C ANISOU 231 C ALA A 34 3232 1927 3483 116 -128 285 C ATOM 232 O ALA A 34 18.762 -7.205 -41.544 1.00 22.51 O ANISOU 232 O ALA A 34 3234 1880 3438 124 -126 271 O ATOM 233 CB ALA A 34 19.852 -4.767 -43.367 1.00 23.13 C ANISOU 233 CB ALA A 34 3280 1972 3537 69 -127 317 C ATOM 234 N TRP A 35 20.342 -5.995 -40.468 1.00 22.58 N ANISOU 234 N TRP A 35 3178 1923 3480 113 -146 283 N ATOM 235 CA TRP A 35 19.809 -6.175 -39.124 1.00 22.30 C ANISOU 235 CA TRP A 35 3140 1884 3448 124 -168 265 C ATOM 236 C TRP A 35 19.317 -4.827 -38.595 1.00 22.33 C ANISOU 236 C TRP A 35 3143 1869 3473 88 -195 251 C ATOM 237 O TRP A 35 19.976 -3.799 -38.780 1.00 22.48 O ANISOU 237 O TRP A 35 3144 1891 3506 55 -193 253 O ATOM 238 CB TRP A 35 20.886 -6.723 -38.192 1.00 22.42 C ANISOU 238 CB TRP A 35 3112 1949 3457 147 -163 275 C ATOM 239 CG TRP A 35 21.296 -8.132 -38.484 1.00 22.42 C ANISOU 239 CG TRP A 35 3119 1957 3444 198 -124 295 C ATOM 240 CD1 TRP A 35 22.382 -8.538 -39.206 1.00 22.76 C ANISOU 240 CD1 TRP A 35 3142 2024 3481 218 -90 320 C ATOM 241 CD2 TRP A 35 20.630 -9.321 -38.057 1.00 22.24 C ANISOU 241 CD2 TRP A 35 3128 1909 3413 235 -105 292 C ATOM 242 NE1 TRP A 35 22.437 -9.911 -39.250 1.00 22.82 N ANISOU 242 NE1 TRP A 35 3172 2019 3481 271 -44 334 N ATOM 243 CE2 TRP A 35 21.371 -10.418 -38.557 1.00 22.58 C ANISOU 243 CE2 TRP A 35 3176 1955 3449 279 -52 316 C ATOM 244 CE3 TRP A 35 19.482 -9.571 -37.292 1.00 21.96 C ANISOU 244 CE3 TRP A 35 3120 1848 3376 236 -122 273 C ATOM 245 CZ2 TRP A 35 21.003 -11.743 -38.316 1.00 22.64 C ANISOU 245 CZ2 TRP A 35 3221 1929 3451 322 -8 320 C ATOM 246 CZ3 TRP A 35 19.115 -10.900 -37.050 1.00 22.03 C ANISOU 246 CZ3 TRP A 35 3161 1832 3376 274 -86 276 C ATOM 247 CH2 TRP A 35 19.876 -11.963 -37.564 1.00 22.34 C ANISOU 247 CH2 TRP A 35 3211 1865 3412 315 -26 300 C ATOM 248 N TYR A 36 18.163 -4.853 -37.936 1.00 22.19 N ANISOU 248 N TYR A 36 3147 1827 3457 94 -211 234 N ATOM 249 CA TYR A 36 17.545 -3.665 -37.366 1.00 22.40 C ANISOU 249 CA TYR A 36 3180 1825 3505 70 -226 219 C ATOM 250 C TYR A 36 17.203 -3.905 -35.904 1.00 22.71 C ANISOU 250 C TYR A 36 3213 1876 3542 74 -244 193 C ATOM 251 O TYR A 36 16.881 -5.032 -35.510 1.00 22.41 O ANISOU 251 O TYR A 36 3178 1851 3485 104 -247 193 O ATOM 252 CB TYR A 36 16.275 -3.305 -38.140 1.00 22.12 C ANISOU 252 CB TYR A 36 3178 1755 3473 77 -225 233 C ATOM 253 CG TYR A 36 16.538 -2.973 -39.586 1.00 22.12 C ANISOU 253 CG TYR A 36 3181 1753 3469 70 -208 263 C ATOM 254 CD1 TYR A 36 16.845 -1.670 -39.977 1.00 22.33 C ANISOU 254 CD1 TYR A 36 3208 1754 3522 49 -195 280 C ATOM 255 CD2 TYR A 36 16.514 -3.968 -40.564 1.00 21.96 C ANISOU 255 CD2 TYR A 36 3168 1756 3419 82 -199 274 C ATOM 256 CE1 TYR A 36 17.114 -1.367 -41.303 1.00 22.49 C ANISOU 256 CE1 TYR A 36 3230 1779 3537 44 -179 314 C ATOM 257 CE2 TYR A 36 16.773 -3.674 -41.894 1.00 22.12 C ANISOU 257 CE2 TYR A 36 3190 1786 3430 72 -183 302 C ATOM 258 CZ TYR A 36 17.068 -2.372 -42.261 1.00 22.39 C ANISOU 258 CZ TYR A 36 3218 1800 3488 57 -176 325 C ATOM 259 OH TYR A 36 17.329 -2.078 -43.579 1.00 22.48 O ANISOU 259 OH TYR A 36 3229 1825 3487 49 -160 359 O ATOM 260 N GLN A 37 17.292 -2.838 -35.113 1.00 23.37 N ANISOU 260 N GLN A 37 3289 1950 3642 40 -249 169 N ATOM 261 CA GLN A 37 16.844 -2.825 -33.728 1.00 23.79 C ANISOU 261 CA GLN A 37 3338 2012 3690 35 -264 139 C ATOM 262 C GLN A 37 15.507 -2.104 -33.656 1.00 24.38 C ANISOU 262 C GLN A 37 3449 2029 3786 38 -261 130 C ATOM 263 O GLN A 37 15.288 -1.118 -34.361 1.00 24.40 O ANISOU 263 O GLN A 37 3472 1987 3814 27 -242 141 O ATOM 264 CB GLN A 37 17.856 -2.078 -32.859 1.00 24.23 C ANISOU 264 CB GLN A 37 3359 2103 3742 -16 -264 111 C ATOM 265 CG GLN A 37 17.529 -2.035 -31.377 1.00 24.25 C ANISOU 265 CG GLN A 37 3352 2131 3731 -32 -278 75 C ATOM 266 CD GLN A 37 18.517 -1.187 -30.618 1.00 24.90 C ANISOU 266 CD GLN A 37 3400 2259 3802 -101 -274 39 C ATOM 267 OE1 GLN A 37 18.544 0.038 -30.771 1.00 25.20 O ANISOU 267 OE1 GLN A 37 3461 2249 3865 -152 -249 11 O ATOM 268 NE2 GLN A 37 19.340 -1.828 -29.795 1.00 25.12 N ANISOU 268 NE2 GLN A 37 3372 2383 3789 -106 -293 41 N ATOM 269 N GLN A 38 14.638 -2.577 -32.769 1.00 24.96 N ANISOU 269 N GLN A 38 3529 2105 3849 56 -275 114 N ATOM 270 CA GLN A 38 13.333 -1.971 -32.552 1.00 25.76 C ANISOU 270 CA GLN A 38 3659 2162 3967 65 -271 108 C ATOM 271 C GLN A 38 12.993 -2.027 -31.065 1.00 26.54 C ANISOU 271 C GLN A 38 3752 2274 4057 57 -282 70 C ATOM 272 O GLN A 38 13.020 -3.105 -30.472 1.00 26.36 O ANISOU 272 O GLN A 38 3714 2293 4007 74 -300 69 O ATOM 273 CB GLN A 38 12.282 -2.716 -33.381 1.00 25.56 C ANISOU 273 CB GLN A 38 3649 2135 3930 103 -277 137 C ATOM 274 CG GLN A 38 10.916 -2.055 -33.388 1.00 25.71 C ANISOU 274 CG GLN A 38 3686 2122 3962 120 -271 146 C ATOM 275 CD GLN A 38 10.043 -2.504 -34.552 1.00 25.64 C ANISOU 275 CD GLN A 38 3679 2128 3933 144 -274 184 C ATOM 276 OE1 GLN A 38 10.099 -3.658 -34.976 1.00 25.53 O ANISOU 276 OE1 GLN A 38 3663 2147 3889 144 -283 186 O ATOM 277 NE2 GLN A 38 9.230 -1.591 -35.075 1.00 25.85 N ANISOU 277 NE2 GLN A 38 3711 2136 3974 162 -260 216 N ATOM 278 N LYS A 39 12.700 -0.871 -30.468 1.00 27.86 N ANISOU 278 N LYS A 39 3934 2404 4247 32 -264 41 N ATOM 279 CA LYS A 39 12.273 -0.784 -29.065 1.00 28.93 C ANISOU 279 CA LYS A 39 4069 2551 4373 18 -268 0 C ATOM 280 C LYS A 39 10.793 -0.420 -28.970 1.00 29.58 C ANISOU 280 C LYS A 39 4181 2585 4474 51 -256 4 C ATOM 281 O LYS A 39 10.383 0.616 -29.500 1.00 30.23 O ANISOU 281 O LYS A 39 4288 2607 4589 56 -223 16 O ATOM 282 CB LYS A 39 13.092 0.265 -28.324 1.00 29.64 C ANISOU 282 CB LYS A 39 4154 2639 4468 -46 -247 -48 C ATOM 283 CG LYS A 39 14.560 -0.086 -28.206 1.00 29.91 C ANISOU 283 CG LYS A 39 4145 2746 4473 -84 -262 -53 C ATOM 284 CD LYS A 39 15.332 1.056 -27.581 1.00 30.80 C ANISOU 284 CD LYS A 39 4253 2863 4586 -166 -237 -107 C ATOM 285 CE LYS A 39 16.805 0.717 -27.511 1.00 31.03 C ANISOU 285 CE LYS A 39 4226 2986 4579 -205 -254 -106 C ATOM 286 NZ LYS A 39 17.534 1.712 -26.688 1.00 31.91 N ANISOU 286 NZ LYS A 39 4323 3128 4674 -301 -233 -170 N ATOM 287 N AGLN A 40 10.005 -1.274 -28.312 0.50 29.64 N ANISOU 287 N AGLN A 40 4182 2620 4458 76 -278 1 N ATOM 288 N BGLN A 40 10.016 -1.275 -28.298 0.50 29.71 N ANISOU 288 N BGLN A 40 4191 2630 4467 75 -278 1 N ATOM 289 CA AGLN A 40 8.573 -1.037 -28.072 0.50 29.83 C ANISOU 289 CA AGLN A 40 4225 2617 4493 107 -269 5 C ATOM 290 CA BGLN A 40 8.570 -1.088 -28.082 0.50 29.94 C ANISOU 290 CA BGLN A 40 4239 2633 4506 107 -270 6 C ATOM 291 C AGLN A 40 7.761 -0.790 -29.353 0.50 29.84 C ANISOU 291 C AGLN A 40 4237 2592 4510 145 -258 55 C ATOM 292 C BGLN A 40 7.776 -0.787 -29.355 0.50 29.92 C ANISOU 292 C BGLN A 40 4246 2601 4519 144 -258 55 C ATOM 293 O AGLN A 40 6.848 0.039 -29.361 0.50 30.11 O ANISOU 293 O AGLN A 40 4286 2589 4567 169 -232 67 O ATOM 294 O BGLN A 40 6.899 0.080 -29.360 0.50 30.19 O ANISOU 294 O BGLN A 40 4296 2596 4578 167 -230 66 O ATOM 295 CB AGLN A 40 8.393 0.139 -27.102 0.50 30.45 C ANISOU 295 CB AGLN A 40 4322 2655 4592 82 -237 -39 C ATOM 296 CB BGLN A 40 8.322 0.002 -27.038 0.50 30.62 C ANISOU 296 CB BGLN A 40 4341 2683 4610 85 -241 -39 C ATOM 297 CG AGLN A 40 9.219 0.013 -25.829 0.50 30.73 C ANISOU 297 CG AGLN A 40 4340 2734 4601 32 -247 -93 C ATOM 298 CG BGLN A 40 8.773 -0.397 -25.643 0.50 30.87 C ANISOU 298 CG BGLN A 40 4355 2764 4610 49 -258 -87 C ATOM 299 CD AGLN A 40 9.427 1.339 -25.120 0.50 31.42 C ANISOU 299 CD AGLN A 40 4451 2779 4709 -19 -203 -148 C ATOM 300 CD BGLN A 40 8.339 -1.805 -25.283 0.50 30.61 C ANISOU 300 CD BGLN A 40 4302 2786 4541 79 -296 -69 C ATOM 301 OE1AGLN A 40 9.631 2.371 -25.756 0.50 31.98 O ANISOU 301 OE1AGLN A 40 4548 2785 4817 -32 -161 -146 O ATOM 302 OE1BGLN A 40 7.452 -2.375 -25.921 0.50 30.50 O ANISOU 302 OE1BGLN A 40 4294 2766 4527 118 -303 -35 O ATOM 303 NE2AGLN A 40 9.389 1.313 -23.795 0.50 31.68 N ANISOU 303 NE2AGLN A 40 4476 2847 4715 -52 -206 -199 N ATOM 304 NE2BGLN A 40 8.965 -2.374 -24.257 0.50 30.75 N ANISOU 304 NE2BGLN A 40 4295 2865 4525 57 -315 -91 N ATOM 305 N GLY A 41 8.100 -1.509 -30.426 1.00 29.60 N ANISOU 305 N GLY A 41 4197 2588 4464 151 -273 88 N ATOM 306 CA GLY A 41 7.461 -1.317 -31.737 1.00 29.35 C ANISOU 306 CA GLY A 41 4166 2552 4434 178 -266 138 C ATOM 307 C GLY A 41 7.669 0.039 -32.408 1.00 29.34 C ANISOU 307 C GLY A 41 4178 2500 4470 184 -230 164 C ATOM 308 O GLY A 41 6.905 0.400 -33.307 1.00 29.71 O ANISOU 308 O GLY A 41 4222 2548 4520 217 -218 215 O ATOM 309 N LYS A 42 8.701 0.783 -31.994 1.00 28.87 N ANISOU 309 N LYS A 42 4130 2402 4436 149 -209 133 N ATOM 310 CA LYS A 42 8.984 2.110 -32.544 1.00 28.70 C ANISOU 310 CA LYS A 42 4130 2318 4455 146 -162 153 C ATOM 311 C LYS A 42 9.779 1.966 -33.842 1.00 28.08 C ANISOU 311 C LYS A 42 4042 2256 4370 139 -167 190 C ATOM 312 O LYS A 42 9.966 0.856 -34.337 1.00 28.00 O ANISOU 312 O LYS A 42 4011 2303 4325 141 -202 199 O ATOM 313 CB LYS A 42 9.744 2.963 -31.524 1.00 29.15 C ANISOU 313 CB LYS A 42 4208 2331 4537 94 -130 94 C ATOM 314 N SER A 43 10.233 3.085 -34.398 1.00 27.73 N ANISOU 314 N SER A 43 4017 2158 4362 130 -124 210 N ATOM 315 CA SER A 43 10.956 3.101 -35.675 1.00 27.16 C ANISOU 315 CA SER A 43 3937 2098 4285 125 -122 249 C ATOM 316 C SER A 43 12.161 2.143 -35.651 1.00 26.03 C ANISOU 316 C SER A 43 3769 2009 4112 85 -157 218 C ATOM 317 O SER A 43 13.016 2.270 -34.776 1.00 25.98 O ANISOU 317 O SER A 43 3760 2002 4110 40 -155 168 O ATOM 318 CB SER A 43 11.438 4.529 -35.965 1.00 27.97 C ANISOU 318 CB SER A 43 4069 2122 4435 108 -61 262 C ATOM 319 OG SER A 43 12.013 4.645 -37.251 1.00 28.48 O ANISOU 319 OG SER A 43 4127 2197 4496 108 -55 310 O ATOM 320 N PRO A 44 12.217 1.162 -36.580 1.00 24.92 N ANISOU 320 N PRO A 44 3609 1921 3937 101 -184 246 N ATOM 321 CA PRO A 44 13.425 0.337 -36.678 1.00 24.18 C ANISOU 321 CA PRO A 44 3496 1869 3822 74 -202 226 C ATOM 322 C PRO A 44 14.692 1.155 -36.976 1.00 24.09 C ANISOU 322 C PRO A 44 3482 1840 3833 34 -177 223 C ATOM 323 O PRO A 44 14.644 2.107 -37.759 1.00 24.16 O ANISOU 323 O PRO A 44 3507 1808 3865 34 -146 256 O ATOM 324 CB PRO A 44 13.113 -0.605 -37.841 1.00 24.13 C ANISOU 324 CB PRO A 44 3481 1904 3781 97 -216 261 C ATOM 325 CG PRO A 44 11.628 -0.712 -37.846 1.00 24.17 C ANISOU 325 CG PRO A 44 3493 1916 3776 129 -224 279 C ATOM 326 CD PRO A 44 11.150 0.662 -37.471 1.00 24.68 C ANISOU 326 CD PRO A 44 3573 1924 3881 140 -197 291 C ATOM 327 N GLN A 45 15.799 0.780 -36.340 1.00 23.61 N ANISOU 327 N GLN A 45 3398 1814 3760 0 -188 188 N ATOM 328 CA GLN A 45 17.084 1.470 -36.497 1.00 23.71 C ANISOU 328 CA GLN A 45 3398 1827 3784 -50 -168 178 C ATOM 329 C GLN A 45 18.097 0.516 -37.116 1.00 23.25 C ANISOU 329 C GLN A 45 3306 1832 3697 -46 -183 194 C ATOM 330 O GLN A 45 18.263 -0.603 -36.633 1.00 22.84 O ANISOU 330 O GLN A 45 3231 1829 3618 -26 -207 186 O ATOM 331 CB GLN A 45 17.584 1.952 -35.139 1.00 24.02 C ANISOU 331 CB GLN A 45 3427 1874 3825 -103 -164 122 C ATOM 332 CG GLN A 45 16.617 2.870 -34.408 1.00 24.25 C ANISOU 332 CG GLN A 45 3495 1837 3883 -110 -139 97 C ATOM 333 CD GLN A 45 16.258 4.096 -35.229 1.00 24.72 C ANISOU 333 CD GLN A 45 3596 1810 3985 -108 -88 126 C ATOM 334 OE1 GLN A 45 17.134 4.839 -35.666 1.00 25.21 O ANISOU 334 OE1 GLN A 45 3663 1851 4063 -153 -56 124 O ATOM 335 NE2 GLN A 45 14.972 4.298 -35.459 1.00 24.66 N ANISOU 335 NE2 GLN A 45 3616 1758 3996 -52 -77 158 N ATOM 336 N LEU A 46 18.758 0.960 -38.185 1.00 23.13 N ANISOU 336 N LEU A 46 3289 1810 3690 -61 -163 221 N ATOM 337 CA LEU A 46 19.725 0.130 -38.912 1.00 22.90 C ANISOU 337 CA LEU A 46 3229 1835 3635 -54 -168 240 C ATOM 338 C LEU A 46 20.976 -0.141 -38.069 1.00 23.00 C ANISOU 338 C LEU A 46 3196 1912 3632 -85 -176 214 C ATOM 339 O LEU A 46 21.585 0.789 -37.543 1.00 23.25 O ANISOU 339 O LEU A 46 3215 1944 3674 -142 -164 188 O ATOM 340 CB LEU A 46 20.114 0.799 -40.236 1.00 23.11 C ANISOU 340 CB LEU A 46 3265 1842 3673 -67 -142 275 C ATOM 341 CG LEU A 46 21.137 0.100 -41.135 1.00 23.12 C ANISOU 341 CG LEU A 46 3239 1896 3652 -62 -138 296 C ATOM 342 CD1 LEU A 46 20.587 -1.206 -41.685 1.00 22.70 C ANISOU 342 CD1 LEU A 46 3193 1864 3569 -13 -149 310 C ATOM 343 CD2 LEU A 46 21.560 1.023 -42.266 1.00 23.47 C ANISOU 343 CD2 LEU A 46 3291 1918 3710 -86 -109 327 C ATOM 344 N LEU A 47 21.340 -1.418 -37.949 1.00 22.75 N ANISOU 344 N LEU A 47 3137 1935 3573 -47 -190 224 N ATOM 345 CA LEU A 47 22.563 -1.838 -37.258 1.00 23.10 C ANISOU 345 CA LEU A 47 3124 2060 3594 -59 -196 219 C ATOM 346 C LEU A 47 23.661 -2.254 -38.232 1.00 23.34 C ANISOU 346 C LEU A 47 3124 2131 3612 -48 -179 252 C ATOM 347 O LEU A 47 24.796 -1.773 -38.148 1.00 23.87 O ANISOU 347 O LEU A 47 3147 2252 3672 -89 -173 251 O ATOM 348 CB LEU A 47 22.267 -3.013 -36.330 1.00 22.89 C ANISOU 348 CB LEU A 47 3084 2068 3545 -12 -214 220 C ATOM 349 CG LEU A 47 21.237 -2.768 -35.225 1.00 22.72 C ANISOU 349 CG LEU A 47 3084 2021 3529 -19 -233 188 C ATOM 350 CD1 LEU A 47 20.926 -4.078 -34.529 1.00 22.53 C ANISOU 350 CD1 LEU A 47 3051 2026 3482 36 -244 199 C ATOM 351 CD2 LEU A 47 21.728 -1.734 -34.228 1.00 23.20 C ANISOU 351 CD2 LEU A 47 3118 2111 3586 -87 -238 149 C ATOM 352 N VAL A 48 23.311 -3.172 -39.128 1.00 23.02 N ANISOU 352 N VAL A 48 3109 2072 3566 3 -167 277 N ATOM 353 CA VAL A 48 24.250 -3.813 -40.040 1.00 23.28 C ANISOU 353 CA VAL A 48 3120 2141 3586 27 -143 306 C ATOM 354 C VAL A 48 23.598 -3.961 -41.407 1.00 23.09 C ANISOU 354 C VAL A 48 3142 2067 3562 40 -126 319 C ATOM 355 O VAL A 48 22.421 -4.284 -41.487 1.00 22.63 O ANISOU 355 O VAL A 48 3125 1968 3503 57 -133 311 O ATOM 356 CB VAL A 48 24.635 -5.229 -39.531 1.00 23.29 C ANISOU 356 CB VAL A 48 3097 2187 3566 88 -133 324 C ATOM 357 CG1 VAL A 48 25.514 -5.971 -40.545 1.00 23.55 C ANISOU 357 CG1 VAL A 48 3118 2243 3588 122 -95 355 C ATOM 358 CG2 VAL A 48 25.322 -5.146 -38.172 1.00 23.62 C ANISOU 358 CG2 VAL A 48 3079 2302 3594 79 -152 322 C ATOM 359 N TYR A 49 24.368 -3.730 -42.468 1.00 23.43 N ANISOU 359 N TYR A 49 3175 2125 3603 28 -104 339 N ATOM 360 CA TYR A 49 23.927 -4.023 -43.836 1.00 23.54 C ANISOU 360 CA TYR A 49 3224 2115 3605 39 -84 353 C ATOM 361 C TYR A 49 25.015 -4.779 -44.598 1.00 23.81 C ANISOU 361 C TYR A 49 3236 2188 3622 60 -49 372 C ATOM 362 O TYR A 49 26.148 -4.883 -44.136 1.00 24.00 O ANISOU 362 O TYR A 49 3212 2262 3646 66 -42 382 O ATOM 363 CB TYR A 49 23.509 -2.744 -44.572 1.00 23.72 C ANISOU 363 CB TYR A 49 3266 2104 3642 0 -87 366 C ATOM 364 CG TYR A 49 24.581 -1.687 -44.681 1.00 24.31 C ANISOU 364 CG TYR A 49 3310 2193 3733 -44 -77 375 C ATOM 365 CD1 TYR A 49 24.844 -0.821 -43.623 1.00 24.56 C ANISOU 365 CD1 TYR A 49 3325 2220 3786 -83 -88 354 C ATOM 366 CD2 TYR A 49 25.321 -1.534 -45.852 1.00 24.70 C ANISOU 366 CD2 TYR A 49 3350 2263 3773 -55 -52 401 C ATOM 367 CE1 TYR A 49 25.822 0.162 -43.725 1.00 25.12 C ANISOU 367 CE1 TYR A 49 3372 2305 3869 -138 -72 356 C ATOM 368 CE2 TYR A 49 26.298 -0.553 -45.964 1.00 25.21 C ANISOU 368 CE2 TYR A 49 3387 2340 3851 -102 -39 409 C ATOM 369 CZ TYR A 49 26.545 0.290 -44.895 1.00 25.39 C ANISOU 369 CZ TYR A 49 3394 2356 3895 -147 -48 385 C ATOM 370 OH TYR A 49 27.510 1.262 -44.990 1.00 26.10 O ANISOU 370 OH TYR A 49 3461 2460 3996 -208 -30 385 O ATOM 371 N TYR A 50 24.643 -5.320 -45.756 1.00 23.97 N ANISOU 371 N TYR A 50 3290 2194 3622 71 -24 376 N ATOM 372 CA TYR A 50 25.491 -6.238 -46.528 1.00 24.42 C ANISOU 372 CA TYR A 50 3341 2277 3661 97 21 386 C ATOM 373 C TYR A 50 26.061 -7.350 -45.642 1.00 24.78 C ANISOU 373 C TYR A 50 3368 2342 3708 151 43 389 C ATOM 374 O TYR A 50 27.237 -7.713 -45.761 1.00 25.11 O ANISOU 374 O TYR A 50 3371 2425 3747 177 74 412 O ATOM 375 CB TYR A 50 26.628 -5.499 -47.257 1.00 24.78 C ANISOU 375 CB TYR A 50 3349 2359 3708 72 34 411 C ATOM 376 CG TYR A 50 26.202 -4.324 -48.113 1.00 24.79 C ANISOU 376 CG TYR A 50 3366 2342 3710 25 20 421 C ATOM 377 CD1 TYR A 50 24.966 -4.307 -48.765 1.00 24.52 C ANISOU 377 CD1 TYR A 50 3377 2280 3660 18 14 418 C ATOM 378 CD2 TYR A 50 27.056 -3.233 -48.297 1.00 25.11 C ANISOU 378 CD2 TYR A 50 3374 2401 3766 -13 20 440 C ATOM 379 CE1 TYR A 50 24.587 -3.239 -49.550 1.00 24.63 C ANISOU 379 CE1 TYR A 50 3400 2286 3674 -13 6 443 C ATOM 380 CE2 TYR A 50 26.680 -2.151 -49.086 1.00 25.20 C ANISOU 380 CE2 TYR A 50 3403 2388 3783 -49 18 460 C ATOM 381 CZ TYR A 50 25.446 -2.157 -49.710 1.00 24.98 C ANISOU 381 CZ TYR A 50 3418 2334 3740 -43 11 466 C ATOM 382 OH TYR A 50 25.063 -1.090 -50.491 1.00 25.12 O ANISOU 382 OH TYR A 50 3448 2336 3761 -67 14 500 O ATOM 383 N ALA A 51 25.221 -7.858 -44.738 1.00 24.80 N ANISOU 383 N ALA A 51 3393 2317 3714 170 28 372 N ATOM 384 CA ALA A 51 25.572 -8.922 -43.796 1.00 25.28 C ANISOU 384 CA ALA A 51 3440 2389 3776 227 50 382 C ATOM 385 C ALA A 51 26.576 -8.556 -42.685 1.00 25.83 C ANISOU 385 C ALA A 51 3437 2526 3853 239 28 407 C ATOM 386 O ALA A 51 26.403 -9.003 -41.552 1.00 25.83 O ANISOU 386 O ALA A 51 3423 2537 3853 269 18 412 O ATOM 387 CB ALA A 51 26.038 -10.171 -44.547 1.00 25.68 C ANISOU 387 CB ALA A 51 3515 2428 3815 274 122 392 C ATOM 388 N GLU A 52 27.625 -7.786 -43.004 1.00 26.62 N ANISOU 388 N GLU A 52 3484 2679 3952 212 24 424 N ATOM 389 CA GLU A 52 28.719 -7.502 -42.055 1.00 27.41 C ANISOU 389 CA GLU A 52 3503 2868 4046 214 8 448 C ATOM 390 C GLU A 52 29.163 -6.041 -41.911 1.00 27.56 C ANISOU 390 C GLU A 52 3482 2923 4067 133 -28 434 C ATOM 391 O GLU A 52 30.023 -5.757 -41.077 1.00 27.97 O ANISOU 391 O GLU A 52 3462 3060 4104 117 -43 446 O ATOM 392 CB GLU A 52 29.945 -8.340 -42.435 1.00 28.38 C ANISOU 392 CB GLU A 52 3580 3047 4155 274 60 494 C ATOM 393 CG GLU A 52 29.585 -9.715 -42.975 1.00 28.74 C ANISOU 393 CG GLU A 52 3683 3033 4202 344 121 502 C ATOM 394 CD GLU A 52 30.754 -10.658 -43.062 1.00 29.67 C ANISOU 394 CD GLU A 52 3757 3202 4313 423 182 556 C ATOM 395 OE1 GLU A 52 31.879 -10.226 -43.400 1.00 30.60 O ANISOU 395 OE1 GLU A 52 3811 3395 4422 416 188 583 O ATOM 396 OE2 GLU A 52 30.518 -11.848 -42.808 1.00 30.07 O ANISOU 396 OE2 GLU A 52 3842 3216 4369 494 232 572 O ATOM 397 N THR A 53 28.612 -5.119 -42.698 1.00 27.28 N ANISOU 397 N THR A 53 3490 2831 4046 80 -37 413 N ATOM 398 CA THR A 53 29.037 -3.723 -42.616 1.00 27.55 C ANISOU 398 CA THR A 53 3498 2882 4089 2 -56 399 C ATOM 399 C THR A 53 28.235 -3.030 -41.531 1.00 27.32 C ANISOU 399 C THR A 53 3486 2824 4072 -37 -91 364 C ATOM 400 O THR A 53 27.010 -2.934 -41.627 1.00 26.82 O ANISOU 400 O THR A 53 3482 2684 4023 -30 -100 348 O ATOM 401 CB THR A 53 28.850 -2.973 -43.943 1.00 27.50 C ANISOU 401 CB THR A 53 3531 2825 4095 -33 -41 402 C ATOM 402 OG1 THR A 53 29.542 -3.672 -44.976 1.00 27.75 O ANISOU 402 OG1 THR A 53 3550 2882 4111 2 -5 430 O ATOM 403 CG2 THR A 53 29.401 -1.550 -43.845 1.00 27.93 C ANISOU 403 CG2 THR A 53 3562 2890 4161 -115 -46 391 C ATOM 404 N LEU A 54 28.937 -2.549 -40.511 1.00 27.76 N ANISOU 404 N LEU A 54 3484 2948 4114 -80 -107 351 N ATOM 405 CA LEU A 54 28.317 -1.868 -39.381 1.00 27.75 C ANISOU 405 CA LEU A 54 3495 2930 4120 -126 -133 311 C ATOM 406 C LEU A 54 27.912 -0.457 -39.811 1.00 27.93 C ANISOU 406 C LEU A 54 3564 2876 4174 -197 -124 283 C ATOM 407 O LEU A 54 28.701 0.247 -40.436 1.00 28.19 O ANISOU 407 O LEU A 54 3580 2922 4209 -246 -104 288 O ATOM 408 CB LEU A 54 29.297 -1.819 -38.203 1.00 28.41 C ANISOU 408 CB LEU A 54 3494 3130 4169 -160 -149 303 C ATOM 409 CG LEU A 54 28.741 -1.632 -36.795 1.00 28.46 C ANISOU 409 CG LEU A 54 3498 3150 4165 -185 -177 266 C ATOM 410 CD1 LEU A 54 27.823 -2.785 -36.409 1.00 27.93 C ANISOU 410 CD1 LEU A 54 3461 3053 4099 -98 -187 283 C ATOM 411 CD2 LEU A 54 29.890 -1.504 -35.805 1.00 29.20 C ANISOU 411 CD2 LEU A 54 3496 3387 4211 -233 -190 263 C ATOM 412 N ALA A 55 26.681 -0.061 -39.488 1.00 27.73 N ANISOU 412 N ALA A 55 3597 2769 4171 -198 -132 260 N ATOM 413 CA ALA A 55 26.146 1.246 -39.886 1.00 27.98 C ANISOU 413 CA ALA A 55 3680 2714 4237 -247 -111 245 C ATOM 414 C ALA A 55 26.747 2.373 -39.054 1.00 28.75 C ANISOU 414 C ALA A 55 3759 2826 4338 -342 -99 201 C ATOM 415 O ALA A 55 27.336 2.127 -37.999 1.00 28.83 O ANISOU 415 O ALA A 55 3717 2921 4318 -370 -118 175 O ATOM 416 CB ALA A 55 24.624 1.254 -39.774 1.00 27.49 C ANISOU 416 CB ALA A 55 3680 2569 4197 -208 -119 242 C ATOM 417 N AASP A 56 26.584 3.606 -39.532 0.50 29.23 N ANISOU 417 N AASP A 56 3866 2809 4433 -393 -63 193 N ATOM 418 N BASP A 56 26.592 3.605 -39.534 0.50 29.22 N ANISOU 418 N BASP A 56 3863 2807 4430 -393 -63 193 N ATOM 419 CA AASP A 56 27.148 4.784 -38.871 0.50 30.10 C ANISOU 419 CA AASP A 56 3973 2915 4549 -498 -34 142 C ATOM 420 CA BASP A 56 27.160 4.776 -38.867 0.50 30.06 C ANISOU 420 CA BASP A 56 3968 2912 4544 -499 -35 142 C ATOM 421 C AASP A 56 26.487 5.044 -37.518 0.50 30.14 C ANISOU 421 C AASP A 56 3997 2902 4555 -525 -41 88 C ATOM 422 C BASP A 56 26.492 5.036 -37.519 0.50 30.11 C ANISOU 422 C BASP A 56 3992 2899 4550 -524 -42 88 C ATOM 423 O AASP A 56 25.261 4.994 -37.400 0.50 29.89 O ANISOU 423 O AASP A 56 4016 2794 4547 -472 -44 93 O ATOM 424 O BASP A 56 25.265 4.979 -37.404 0.50 29.86 O ANISOU 424 O BASP A 56 4011 2790 4542 -471 -45 93 O ATOM 425 CB AASP A 56 26.998 6.016 -39.763 0.50 30.64 C ANISOU 425 CB AASP A 56 4101 2880 4662 -535 21 154 C ATOM 426 CB BASP A 56 27.025 6.016 -39.748 0.50 30.58 C ANISOU 426 CB BASP A 56 4092 2874 4653 -537 21 153 C ATOM 427 CG AASP A 56 27.836 5.929 -41.021 0.50 30.83 C ANISOU 427 CG AASP A 56 4102 2933 4680 -532 33 200 C ATOM 428 CG BASP A 56 27.376 7.289 -39.010 0.50 31.44 C ANISOU 428 CG BASP A 56 4221 2948 4776 -650 66 91 C ATOM 429 OD1AASP A 56 28.799 5.133 -41.041 0.50 30.93 O ANISOU 429 OD1AASP A 56 4044 3054 4653 -528 7 209 O ATOM 430 OD1BASP A 56 28.562 7.473 -38.661 0.50 32.00 O ANISOU 430 OD1BASP A 56 4237 3106 4816 -736 70 59 O ATOM 431 OD2AASP A 56 27.532 6.655 -41.991 0.50 31.09 O ANISOU 431 OD2AASP A 56 4184 2883 4746 -529 72 234 O ATOM 432 OD2BASP A 56 26.460 8.099 -38.767 0.50 31.66 O ANISOU 432 OD2BASP A 56 4320 2866 4845 -656 104 74 O ATOM 433 N GLY A 57 27.311 5.300 -36.502 1.00 30.65 N ANISOU 433 N GLY A 57 4012 3050 4585 -610 -45 37 N ATOM 434 CA GLY A 57 26.833 5.542 -35.140 1.00 30.72 C ANISOU 434 CA GLY A 57 4029 3061 4582 -649 -50 -23 C ATOM 435 C GLY A 57 26.589 4.301 -34.297 1.00 30.18 C ANISOU 435 C GLY A 57 3913 3079 4474 -584 -106 -13 C ATOM 436 O GLY A 57 26.342 4.426 -33.098 1.00 30.60 O ANISOU 436 O GLY A 57 3960 3162 4506 -622 -116 -62 O ATOM 437 N VAL A 58 26.678 3.108 -34.891 1.00 29.41 N ANISOU 437 N VAL A 58 3786 3023 4365 -490 -136 48 N ATOM 438 CA VAL A 58 26.344 1.867 -34.192 1.00 28.86 C ANISOU 438 CA VAL A 58 3685 3014 4266 -416 -177 68 C ATOM 439 C VAL A 58 27.578 1.428 -33.402 1.00 29.29 C ANISOU 439 C VAL A 58 3640 3228 4260 -448 -199 68 C ATOM 440 O VAL A 58 28.680 1.423 -33.956 1.00 29.71 O ANISOU 440 O VAL A 58 3643 3351 4297 -468 -191 92 O ATOM 441 CB VAL A 58 25.905 0.757 -35.173 1.00 28.17 C ANISOU 441 CB VAL A 58 3617 2895 4193 -307 -186 129 C ATOM 442 CG1 VAL A 58 25.627 -0.554 -34.438 1.00 27.88 C ANISOU 442 CG1 VAL A 58 3552 2912 4128 -234 -216 150 C ATOM 443 CG2 VAL A 58 24.668 1.200 -35.945 1.00 27.73 C ANISOU 443 CG2 VAL A 58 3645 2707 4184 -280 -169 133 C ATOM 444 N PRO A 59 27.408 1.077 -32.108 1.00 29.23 N ANISOU 444 N PRO A 59 3600 3290 4215 -453 -225 47 N ATOM 445 CA PRO A 59 28.553 0.636 -31.305 1.00 29.80 C ANISOU 445 CA PRO A 59 3565 3536 4220 -478 -247 59 C ATOM 446 C PRO A 59 29.246 -0.621 -31.842 1.00 29.63 C ANISOU 446 C PRO A 59 3487 3592 4182 -379 -256 142 C ATOM 447 O PRO A 59 28.578 -1.534 -32.341 1.00 28.84 O ANISOU 447 O PRO A 59 3428 3420 4109 -276 -255 184 O ATOM 448 CB PRO A 59 27.932 0.354 -29.935 1.00 29.81 C ANISOU 448 CB PRO A 59 3559 3576 4192 -476 -273 33 C ATOM 449 CG PRO A 59 26.739 1.243 -29.875 1.00 29.52 C ANISOU 449 CG PRO A 59 3620 3393 4203 -510 -253 -26 C ATOM 450 CD PRO A 59 26.201 1.252 -31.272 1.00 28.96 C ANISOU 450 CD PRO A 59 3619 3189 4195 -450 -231 7 C ATOM 451 N SER A 60 30.573 -0.658 -31.705 1.00 30.32 N ANISOU 451 N SER A 60 3476 3826 4219 -413 -260 164 N ATOM 452 CA SER A 60 31.405 -1.742 -32.246 1.00 30.41 C ANISOU 452 CA SER A 60 3424 3917 4213 -321 -256 246 C ATOM 453 C SER A 60 31.188 -3.101 -31.571 1.00 30.28 C ANISOU 453 C SER A 60 3376 3954 4173 -208 -269 306 C ATOM 454 O SER A 60 31.682 -4.111 -32.061 1.00 30.32 O ANISOU 454 O SER A 60 3351 3993 4177 -112 -252 378 O ATOM 455 CB SER A 60 32.892 -1.365 -32.173 1.00 31.35 C ANISOU 455 CB SER A 60 3434 4198 4278 -391 -255 258 C ATOM 456 OG SER A 60 33.283 -1.054 -30.844 1.00 32.01 O ANISOU 456 OG SER A 60 3442 4426 4296 -468 -281 228 O ATOM 457 N ARG A 61 30.481 -3.121 -30.442 1.00 30.24 N ANISOU 457 N ARG A 61 3381 3957 4152 -220 -293 277 N ATOM 458 CA ARG A 61 30.032 -4.377 -29.832 1.00 30.05 C ANISOU 458 CA ARG A 61 3350 3950 4117 -111 -299 331 C ATOM 459 C ARG A 61 29.050 -5.186 -30.707 1.00 29.25 C ANISOU 459 C ARG A 61 3346 3691 4076 -14 -276 354 C ATOM 460 O ARG A 61 28.946 -6.404 -30.544 1.00 29.13 O ANISOU 460 O ARG A 61 3326 3685 4057 88 -262 414 O ATOM 461 CB ARG A 61 29.439 -4.130 -28.438 1.00 30.17 C ANISOU 461 CB ARG A 61 3359 4007 4099 -156 -329 289 C ATOM 462 CG ARG A 61 28.178 -3.278 -28.381 1.00 29.60 C ANISOU 462 CG ARG A 61 3388 3789 4071 -214 -332 207 C ATOM 463 CD ARG A 61 27.537 -3.323 -27.001 1.00 29.72 C ANISOU 463 CD ARG A 61 3397 3843 4053 -231 -356 178 C ATOM 464 NE ARG A 61 26.340 -2.487 -26.964 1.00 29.21 N ANISOU 464 NE ARG A 61 3428 3639 4033 -280 -351 103 N ATOM 465 CZ ARG A 61 26.330 -1.159 -26.826 1.00 29.55 C ANISOU 465 CZ ARG A 61 3494 3653 4080 -395 -340 24 C ATOM 466 NH1 ARG A 61 27.458 -0.458 -26.701 1.00 30.33 N ANISOU 466 NH1 ARG A 61 3529 3857 4139 -492 -336 -1 N ATOM 467 NH2 ARG A 61 25.166 -0.517 -26.821 1.00 29.19 N ANISOU 467 NH2 ARG A 61 3539 3471 4080 -415 -326 -29 N ATOM 468 N PHE A 62 28.338 -4.510 -31.614 1.00 28.81 N ANISOU 468 N PHE A 62 3377 3497 4071 -49 -266 308 N ATOM 469 CA PHE A 62 27.481 -5.180 -32.600 1.00 28.25 C ANISOU 469 CA PHE A 62 3391 3296 4048 25 -243 325 C ATOM 470 C PHE A 62 28.329 -5.716 -33.747 1.00 28.71 C ANISOU 470 C PHE A 62 3432 3364 4112 73 -209 375 C ATOM 471 O PHE A 62 29.184 -5.002 -34.281 1.00 28.95 O ANISOU 471 O PHE A 62 3428 3434 4138 20 -205 370 O ATOM 472 CB PHE A 62 26.417 -4.228 -33.153 1.00 27.68 C ANISOU 472 CB PHE A 62 3406 3092 4019 -27 -244 268 C ATOM 473 CG PHE A 62 25.332 -3.896 -32.170 1.00 27.37 C ANISOU 473 CG PHE A 62 3403 3015 3984 -51 -266 224 C ATOM 474 CD1 PHE A 62 24.209 -4.705 -32.060 1.00 26.79 C ANISOU 474 CD1 PHE A 62 3381 2873 3924 13 -267 233 C ATOM 475 CD2 PHE A 62 25.427 -2.772 -31.356 1.00 27.78 C ANISOU 475 CD2 PHE A 62 3438 3096 4022 -142 -279 170 C ATOM 476 CE1 PHE A 62 23.202 -4.404 -31.155 1.00 26.59 C ANISOU 476 CE1 PHE A 62 3385 2816 3901 -7 -285 194 C ATOM 477 CE2 PHE A 62 24.421 -2.463 -30.446 1.00 27.60 C ANISOU 477 CE2 PHE A 62 3450 3034 4002 -163 -293 127 C ATOM 478 CZ PHE A 62 23.308 -3.281 -30.345 1.00 26.97 C ANISOU 478 CZ PHE A 62 3417 2893 3938 -91 -298 142 C ATOM 479 N SER A 63 28.074 -6.969 -34.124 1.00 28.80 N ANISOU 479 N SER A 63 3471 3336 4135 170 -180 419 N ATOM 480 CA SER A 63 28.853 -7.658 -35.145 1.00 29.32 C ANISOU 480 CA SER A 63 3525 3408 4205 228 -136 467 C ATOM 481 C SER A 63 27.948 -8.526 -36.011 1.00 29.05 C ANISOU 481 C SER A 63 3583 3252 4204 285 -100 468 C ATOM 482 O SER A 63 27.272 -9.422 -35.503 1.00 28.95 O ANISOU 482 O SER A 63 3603 3204 4194 339 -88 479 O ATOM 483 CB SER A 63 29.920 -8.528 -34.480 1.00 30.04 C ANISOU 483 CB SER A 63 3527 3627 4261 299 -119 539 C ATOM 484 OG SER A 63 30.702 -9.205 -35.445 1.00 30.47 O ANISOU 484 OG SER A 63 3571 3686 4322 362 -67 589 O ATOM 485 N GLY A 64 27.942 -8.254 -37.313 1.00 29.18 N ANISOU 485 N GLY A 64 3640 3209 4240 267 -80 455 N ATOM 486 CA GLY A 64 27.189 -9.048 -38.279 1.00 29.13 C ANISOU 486 CA GLY A 64 3713 3103 4252 305 -41 450 C ATOM 487 C GLY A 64 28.128 -9.968 -39.027 1.00 29.91 C ANISOU 487 C GLY A 64 3797 3221 4347 370 20 495 C ATOM 488 O GLY A 64 29.217 -9.553 -39.419 1.00 30.33 O ANISOU 488 O GLY A 64 3794 3340 4391 358 25 517 O ATOM 489 N ARG A 65 27.715 -11.216 -39.218 1.00 30.32 N ANISOU 489 N ARG A 65 3901 3214 4405 435 72 508 N ATOM 490 CA ARG A 65 28.491 -12.180 -39.991 1.00 31.29 C ANISOU 490 CA ARG A 65 4028 3333 4529 502 148 547 C ATOM 491 C ARG A 65 27.581 -13.049 -40.846 1.00 30.90 C ANISOU 491 C ARG A 65 4079 3172 4491 513 202 515 C ATOM 492 O ARG A 65 26.420 -13.276 -40.497 1.00 30.32 O ANISOU 492 O ARG A 65 4060 3039 4421 496 189 481 O ATOM 493 CB ARG A 65 29.341 -13.057 -39.058 1.00 32.60 C ANISOU 493 CB ARG A 65 4132 3568 4685 594 184 618 C ATOM 494 CG ARG A 65 30.513 -12.337 -38.386 1.00 33.65 C ANISOU 494 CG ARG A 65 4148 3843 4793 584 143 658 C ATOM 495 CD ARG A 65 31.635 -12.026 -39.373 1.00 34.64 C ANISOU 495 CD ARG A 65 4231 4017 4914 580 167 678 C ATOM 496 NE ARG A 65 32.501 -10.919 -38.953 1.00 35.50 N ANISOU 496 NE ARG A 65 4242 4250 4997 518 112 685 N ATOM 497 CZ ARG A 65 33.460 -10.984 -38.024 1.00 36.65 C ANISOU 497 CZ ARG A 65 4280 4535 5109 548 101 741 C ATOM 498 NH1 ARG A 65 33.706 -12.112 -37.351 1.00 37.46 N ANISOU 498 NH1 ARG A 65 4356 4675 5203 654 143 811 N ATOM 499 NH2 ARG A 65 34.179 -9.894 -37.750 1.00 37.11 N ANISOU 499 NH2 ARG A 65 4257 4704 5140 467 53 731 N ATOM 500 N GLY A 66 28.110 -13.513 -41.978 1.00 31.12 N ANISOU 500 N GLY A 66 4127 3178 4518 533 266 521 N ATOM 501 CA GLY A 66 27.428 -14.513 -42.792 1.00 31.08 C ANISOU 501 CA GLY A 66 4216 3078 4516 543 336 490 C ATOM 502 C GLY A 66 27.628 -14.401 -44.286 1.00 31.14 C ANISOU 502 C GLY A 66 4255 3065 4514 508 371 464 C ATOM 503 O GLY A 66 28.190 -13.429 -44.796 1.00 31.34 O ANISOU 503 O GLY A 66 4234 3142 4533 470 333 469 O ATOM 504 N SER A 67 27.159 -15.432 -44.977 1.00 31.23 N ANISOU 504 N SER A 67 4347 2999 4521 516 449 434 N ATOM 505 CA SER A 67 27.129 -15.480 -46.437 1.00 31.26 C ANISOU 505 CA SER A 67 4395 2978 4505 472 489 396 C ATOM 506 C SER A 67 26.207 -16.616 -46.863 1.00 31.25 C ANISOU 506 C SER A 67 4493 2888 4492 457 564 344 C ATOM 507 O SER A 67 25.804 -17.440 -46.035 1.00 31.24 O ANISOU 507 O SER A 67 4525 2838 4505 496 597 348 O ATOM 508 CB SER A 67 28.534 -15.697 -47.015 1.00 31.97 C ANISOU 508 CB SER A 67 4446 3102 4598 525 550 438 C ATOM 509 OG SER A 67 29.140 -16.851 -46.462 1.00 32.67 O ANISOU 509 OG SER A 67 4540 3168 4707 624 636 482 O ATOM 510 N GLY A 68 25.872 -16.651 -48.150 1.00 31.16 N ANISOU 510 N GLY A 68 4528 2859 4450 395 592 294 N ATOM 511 CA GLY A 68 24.988 -17.680 -48.686 1.00 31.31 C ANISOU 511 CA GLY A 68 4643 2805 4447 356 667 231 C ATOM 512 C GLY A 68 23.614 -17.638 -48.038 1.00 30.66 C ANISOU 512 C GLY A 68 4588 2704 4356 308 614 197 C ATOM 513 O GLY A 68 22.848 -16.700 -48.263 1.00 30.09 O ANISOU 513 O GLY A 68 4497 2676 4262 240 528 178 O ATOM 514 N THR A 69 23.329 -18.639 -47.207 1.00 30.65 N ANISOU 514 N THR A 69 4631 2639 4376 349 668 197 N ATOM 515 CA THR A 69 22.041 -18.767 -46.523 1.00 30.13 C ANISOU 515 CA THR A 69 4596 2550 4302 308 632 165 C ATOM 516 C THR A 69 22.111 -18.650 -44.992 1.00 29.66 C ANISOU 516 C THR A 69 4493 2497 4279 374 586 218 C ATOM 517 O THR A 69 21.073 -18.726 -44.338 1.00 29.30 O ANISOU 517 O THR A 69 4468 2434 4229 345 554 196 O ATOM 518 CB THR A 69 21.399 -20.131 -46.857 1.00 30.76 C ANISOU 518 CB THR A 69 4779 2542 4367 278 743 106 C ATOM 519 OG1 THR A 69 22.236 -21.189 -46.372 1.00 31.36 O ANISOU 519 OG1 THR A 69 4884 2549 4481 374 849 145 O ATOM 520 CG2 THR A 69 21.202 -20.282 -48.368 1.00 31.15 C ANISOU 520 CG2 THR A 69 4874 2595 4366 193 789 41 C ATOM 521 N GLN A 70 23.311 -18.477 -44.427 1.00 29.69 N ANISOU 521 N GLN A 70 4433 2535 4311 458 585 287 N ATOM 522 CA GLN A 70 23.512 -18.502 -42.970 1.00 29.42 C ANISOU 522 CA GLN A 70 4353 2520 4303 525 554 342 C ATOM 523 C GLN A 70 24.051 -17.161 -42.481 1.00 28.73 C ANISOU 523 C GLN A 70 4168 2529 4218 522 449 378 C ATOM 524 O GLN A 70 25.123 -16.731 -42.912 1.00 28.97 O ANISOU 524 O GLN A 70 4147 2611 4251 542 449 409 O ATOM 525 CB GLN A 70 24.488 -19.614 -42.587 1.00 30.35 C ANISOU 525 CB GLN A 70 4477 2608 4446 633 658 403 C ATOM 526 N TYR A 71 23.306 -16.507 -41.588 1.00 27.87 N ANISOU 526 N TYR A 71 4036 2444 4109 492 366 369 N ATOM 527 CA TYR A 71 23.663 -15.171 -41.086 1.00 27.36 C ANISOU 527 CA TYR A 71 3891 2459 4046 472 271 388 C ATOM 528 C TYR A 71 23.455 -15.078 -39.587 1.00 27.05 C ANISOU 528 C TYR A 71 3815 2449 4013 498 228 412 C ATOM 529 O TYR A 71 22.553 -15.713 -39.048 1.00 26.85 O ANISOU 529 O TYR A 71 3836 2376 3989 502 241 396 O ATOM 530 CB TYR A 71 22.839 -14.095 -41.803 1.00 26.72 C ANISOU 530 CB TYR A 71 3822 2379 3952 384 208 340 C ATOM 531 CG TYR A 71 23.071 -14.111 -43.287 1.00 26.91 C ANISOU 531 CG TYR A 71 3871 2391 3960 354 246 321 C ATOM 532 CD1 TYR A 71 24.137 -13.413 -43.851 1.00 27.09 C ANISOU 532 CD1 TYR A 71 3844 2463 3985 354 237 346 C ATOM 533 CD2 TYR A 71 22.262 -14.870 -44.128 1.00 26.99 C ANISOU 533 CD2 TYR A 71 3956 2349 3950 321 296 276 C ATOM 534 CE1 TYR A 71 24.378 -13.456 -45.214 1.00 27.35 C ANISOU 534 CE1 TYR A 71 3900 2490 4001 328 274 331 C ATOM 535 CE2 TYR A 71 22.494 -14.920 -45.494 1.00 27.29 C ANISOU 535 CE2 TYR A 71 4017 2386 3966 288 333 256 C ATOM 536 CZ TYR A 71 23.549 -14.211 -46.034 1.00 27.43 C ANISOU 536 CZ TYR A 71 3985 2451 3988 296 322 285 C ATOM 537 OH TYR A 71 23.776 -14.257 -47.390 1.00 27.78 O ANISOU 537 OH TYR A 71 4050 2499 4006 263 360 266 O ATOM 538 N SER A 72 24.288 -14.282 -38.920 1.00 27.07 N ANISOU 538 N SER A 72 3735 2535 4015 507 177 447 N ATOM 539 CA SER A 72 24.151 -14.060 -37.481 1.00 26.94 C ANISOU 539 CA SER A 72 3674 2566 3995 520 130 465 C ATOM 540 C SER A 72 24.468 -12.619 -37.074 1.00 26.76 C ANISOU 540 C SER A 72 3585 2618 3966 463 49 455 C ATOM 541 O SER A 72 25.255 -11.939 -37.734 1.00 26.76 O ANISOU 541 O SER A 72 3550 2655 3964 438 41 458 O ATOM 542 CB SER A 72 25.047 -15.029 -36.707 1.00 27.50 C ANISOU 542 CB SER A 72 3705 2679 4064 615 180 537 C ATOM 543 OG SER A 72 26.404 -14.854 -37.063 1.00 27.89 O ANISOU 543 OG SER A 72 3688 2801 4108 646 197 582 O ATOM 544 N LEU A 73 23.824 -12.172 -35.996 1.00 26.60 N ANISOU 544 N LEU A 73 3553 2613 3941 438 -2 437 N ATOM 545 CA LEU A 73 24.130 -10.901 -35.336 1.00 26.76 C ANISOU 545 CA LEU A 73 3513 2703 3952 383 -67 424 C ATOM 546 C LEU A 73 24.600 -11.222 -33.929 1.00 27.35 C ANISOU 546 C LEU A 73 3525 2863 4004 420 -79 461 C ATOM 547 O LEU A 73 23.880 -11.872 -33.166 1.00 27.04 O ANISOU 547 O LEU A 73 3511 2800 3963 450 -75 465 O ATOM 548 CB LEU A 73 22.894 -10.007 -35.275 1.00 26.13 C ANISOU 548 CB LEU A 73 3476 2569 3883 318 -112 366 C ATOM 549 CG LEU A 73 23.018 -8.651 -34.566 1.00 26.15 C ANISOU 549 CG LEU A 73 3437 2618 3881 253 -165 339 C ATOM 550 CD1 LEU A 73 23.990 -7.739 -35.303 1.00 26.37 C ANISOU 550 CD1 LEU A 73 3430 2678 3911 210 -166 340 C ATOM 551 CD2 LEU A 73 21.646 -8.006 -34.452 1.00 25.58 C ANISOU 551 CD2 LEU A 73 3416 2478 3824 212 -192 293 C ATOM 552 N LYS A 74 25.807 -10.777 -33.593 1.00 28.28 N ANISOU 552 N LYS A 74 3556 3088 4099 414 -93 491 N ATOM 553 CA LYS A 74 26.349 -10.968 -32.255 1.00 29.15 C ANISOU 553 CA LYS A 74 3589 3312 4175 439 -111 531 C ATOM 554 C LYS A 74 26.420 -9.627 -31.533 1.00 29.32 C ANISOU 554 C LYS A 74 3564 3401 4175 344 -173 484 C ATOM 555 O LYS A 74 26.824 -8.618 -32.122 1.00 29.36 O ANISOU 555 O LYS A 74 3558 3413 4184 275 -188 451 O ATOM 556 CB LYS A 74 27.724 -11.634 -32.314 1.00 30.23 C ANISOU 556 CB LYS A 74 3649 3546 4291 512 -72 611 C ATOM 557 CG LYS A 74 28.166 -12.213 -30.977 1.00 31.11 C ANISOU 557 CG LYS A 74 3685 3773 4363 569 -75 676 C ATOM 558 CD LYS A 74 29.179 -13.340 -31.121 1.00 32.14 C ANISOU 558 CD LYS A 74 3768 3959 4486 684 -9 776 C ATOM 559 CE LYS A 74 30.509 -12.855 -31.670 1.00 32.92 C ANISOU 559 CE LYS A 74 3783 4161 4565 671 -8 803 C ATOM 560 NZ LYS A 74 31.647 -13.644 -31.111 1.00 34.07 N ANISOU 560 NZ LYS A 74 3825 4445 4674 773 28 915 N ATOM 561 N ILE A 75 25.991 -9.626 -30.271 1.00 29.50 N ANISOU 561 N ILE A 75 3568 3468 4174 336 -203 477 N ATOM 562 CA ILE A 75 26.112 -8.472 -29.390 1.00 29.82 C ANISOU 562 CA ILE A 75 3561 3585 4184 244 -252 430 C ATOM 563 C ILE A 75 27.042 -8.884 -28.251 1.00 30.80 C ANISOU 563 C ILE A 75 3580 3875 4249 272 -262 487 C ATOM 564 O ILE A 75 26.640 -9.624 -27.353 1.00 30.76 O ANISOU 564 O ILE A 75 3569 3893 4226 324 -262 518 O ATOM 565 CB ILE A 75 24.748 -8.011 -28.820 1.00 29.25 C ANISOU 565 CB ILE A 75 3554 3434 4128 202 -278 367 C ATOM 566 CG1 ILE A 75 23.707 -7.863 -29.940 1.00 28.59 C ANISOU 566 CG1 ILE A 75 3568 3197 4096 198 -264 331 C ATOM 567 CG2 ILE A 75 24.922 -6.699 -28.054 1.00 29.55 C ANISOU 567 CG2 ILE A 75 3555 3534 4139 96 -315 306 C ATOM 568 CD1 ILE A 75 22.301 -7.560 -29.454 1.00 28.18 C ANISOU 568 CD1 ILE A 75 3577 3069 4061 174 -282 282 C ATOM 569 N ASN A 76 28.285 -8.415 -28.311 1.00 31.68 N ANISOU 569 N ASN A 76 3603 4108 4325 236 -270 504 N ATOM 570 CA ASN A 76 29.264 -8.640 -27.244 1.00 32.99 C ANISOU 570 CA ASN A 76 3649 4466 4421 247 -285 559 C ATOM 571 C ASN A 76 29.001 -7.621 -26.145 1.00 33.25 C ANISOU 571 C ASN A 76 3655 4568 4412 134 -334 487 C ATOM 572 O ASN A 76 28.644 -6.488 -26.446 1.00 33.21 O ANISOU 572 O ASN A 76 3697 4492 4428 32 -347 401 O ATOM 573 CB ASN A 76 30.688 -8.460 -27.773 1.00 33.81 C ANISOU 573 CB ASN A 76 3663 4686 4498 240 -274 601 C ATOM 574 CG ASN A 76 31.008 -9.393 -28.926 1.00 33.86 C ANISOU 574 CG ASN A 76 3698 4621 4546 347 -218 665 C ATOM 575 OD1 ASN A 76 30.998 -8.985 -30.088 1.00 33.87 O ANISOU 575 OD1 ASN A 76 3752 4528 4588 318 -203 631 O ATOM 576 ND2 ASN A 76 31.278 -10.650 -28.613 1.00 34.35 N ANISOU 576 ND2 ASN A 76 3730 4726 4598 470 -181 760 N ATOM 577 N ASER A 77 29.177 -8.026 -24.886 0.50 33.86 N ANISOU 577 N ASER A 77 3658 4779 4427 152 -353 525 N ATOM 578 N BSER A 77 29.155 -8.033 -24.886 0.50 33.82 N ANISOU 578 N BSER A 77 3655 4772 4423 153 -353 525 N ATOM 579 CA ASER A 77 29.002 -7.139 -23.726 0.50 34.22 C ANISOU 579 CA ASER A 77 3669 4913 4418 41 -395 457 C ATOM 580 CA BSER A 77 29.010 -7.139 -23.733 0.50 34.19 C ANISOU 580 CA BSER A 77 3665 4910 4415 41 -395 457 C ATOM 581 C ASER A 77 27.704 -6.340 -23.793 0.50 33.36 C ANISOU 581 C ASER A 77 3675 4640 4361 -28 -403 354 C ATOM 582 C BSER A 77 27.707 -6.340 -23.787 0.50 33.36 C ANISOU 582 C BSER A 77 3674 4640 4360 -28 -403 354 C ATOM 583 O ASER A 77 27.723 -5.125 -24.008 0.50 33.42 O ANISOU 583 O ASER A 77 3705 4617 4377 -141 -409 271 O ATOM 584 O BSER A 77 27.727 -5.122 -23.990 0.50 33.42 O ANISOU 584 O BSER A 77 3704 4619 4376 -141 -409 270 O ATOM 585 CB ASER A 77 30.190 -6.183 -23.598 0.50 35.14 C ANISOU 585 CB ASER A 77 3689 5187 4476 -71 -414 428 C ATOM 586 CB BSER A 77 30.206 -6.188 -23.656 0.50 35.10 C ANISOU 586 CB BSER A 77 3685 5178 4473 -70 -413 429 C ATOM 587 OG ASER A 77 31.380 -6.893 -23.311 0.50 36.11 O ANISOU 587 OG ASER A 77 3685 5500 4536 -10 -413 529 O ATOM 588 OG BSER A 77 30.198 -5.447 -22.450 0.50 35.68 O ANISOU 588 OG BSER A 77 3710 5367 4479 -181 -446 367 O ATOM 589 N LEU A 78 26.588 -7.043 -23.617 1.00 32.67 N ANISOU 589 N LEU A 78 3659 4446 4307 44 -395 365 N ATOM 590 CA LEU A 78 25.244 -6.461 -23.754 1.00 31.83 C ANISOU 590 CA LEU A 78 3662 4180 4254 4 -397 285 C ATOM 591 C LEU A 78 25.014 -5.316 -22.763 1.00 31.98 C ANISOU 591 C LEU A 78 3669 4245 4236 -116 -422 197 C ATOM 592 O LEU A 78 25.300 -5.464 -21.581 1.00 32.58 O ANISOU 592 O LEU A 78 3674 4460 4243 -135 -444 206 O ATOM 593 CB LEU A 78 24.192 -7.558 -23.547 1.00 31.36 C ANISOU 593 CB LEU A 78 3659 4036 4219 101 -386 322 C ATOM 594 CG LEU A 78 22.739 -7.301 -23.931 1.00 30.61 C ANISOU 594 CG LEU A 78 3675 3772 4184 93 -380 264 C ATOM 595 CD1 LEU A 78 22.575 -7.230 -25.439 1.00 30.09 C ANISOU 595 CD1 LEU A 78 3674 3581 4178 110 -355 261 C ATOM 596 CD2 LEU A 78 21.863 -8.407 -23.360 1.00 30.45 C ANISOU 596 CD2 LEU A 78 3685 3719 4164 171 -373 301 C ATOM 597 N GLN A 79 24.540 -4.176 -23.267 1.00 31.42 N ANISOU 597 N GLN A 79 3667 4062 4208 -196 -413 115 N ATOM 598 CA GLN A 79 24.317 -2.971 -22.462 1.00 31.62 C ANISOU 598 CA GLN A 79 3700 4104 4210 -317 -418 21 C ATOM 599 C GLN A 79 22.826 -2.741 -22.204 1.00 30.70 C ANISOU 599 C GLN A 79 3677 3850 4137 -309 -411 -27 C ATOM 600 O GLN A 79 21.994 -3.276 -22.940 1.00 29.77 O ANISOU 600 O GLN A 79 3625 3609 4076 -227 -402 3 O ATOM 601 CB GLN A 79 24.918 -1.757 -23.176 1.00 32.11 C ANISOU 601 CB GLN A 79 3773 4136 4291 -416 -397 -35 C ATOM 602 CG GLN A 79 26.429 -1.803 -23.313 1.00 33.06 C ANISOU 602 CG GLN A 79 3791 4412 4358 -449 -404 0 C ATOM 603 CD GLN A 79 27.126 -1.853 -21.970 1.00 34.14 C ANISOU 603 CD GLN A 79 3821 4755 4395 -509 -431 -5 C ATOM 604 OE1 GLN A 79 26.894 -1.006 -21.109 1.00 34.65 O ANISOU 604 OE1 GLN A 79 3892 4846 4427 -618 -431 -90 O ATOM 605 NE2 GLN A 79 27.967 -2.862 -21.775 1.00 34.70 N ANISOU 605 NE2 GLN A 79 3792 4976 4415 -435 -450 89 N ATOM 606 N PRO A 80 22.478 -1.941 -21.164 1.00 30.89 N ANISOU 606 N PRO A 80 3706 3900 4131 -397 -413 -104 N ATOM 607 CA PRO A 80 21.062 -1.681 -20.848 1.00 30.27 C ANISOU 607 CA PRO A 80 3711 3699 4091 -387 -402 -149 C ATOM 608 C PRO A 80 20.235 -1.158 -22.028 1.00 29.48 C ANISOU 608 C PRO A 80 3708 3415 4078 -364 -372 -163 C ATOM 609 O PRO A 80 19.069 -1.519 -22.164 1.00 28.84 O ANISOU 609 O PRO A 80 3684 3239 4035 -300 -370 -152 O ATOM 610 CB PRO A 80 21.137 -0.629 -19.732 1.00 31.10 C ANISOU 610 CB PRO A 80 3804 3862 4149 -511 -393 -242 C ATOM 611 CG PRO A 80 22.451 -0.869 -19.083 1.00 32.01 C ANISOU 611 CG PRO A 80 3806 4180 4175 -560 -419 -224 C ATOM 612 CD PRO A 80 23.373 -1.263 -20.201 1.00 31.95 C ANISOU 612 CD PRO A 80 3765 4188 4187 -515 -421 -156 C ATOM 613 N GLU A 81 20.851 -0.339 -22.880 1.00 29.62 N ANISOU 613 N GLU A 81 3737 3396 4122 -415 -348 -182 N ATOM 614 CA GLU A 81 20.196 0.184 -24.091 1.00 29.14 C ANISOU 614 CA GLU A 81 3757 3177 4138 -390 -318 -182 C ATOM 615 C GLU A 81 19.989 -0.835 -25.232 1.00 28.21 C ANISOU 615 C GLU A 81 3653 3013 4053 -284 -328 -103 C ATOM 616 O GLU A 81 19.336 -0.507 -26.222 1.00 27.81 O ANISOU 616 O GLU A 81 3663 2846 4057 -257 -308 -96 O ATOM 617 CB GLU A 81 20.935 1.431 -24.622 1.00 29.88 C ANISOU 617 CB GLU A 81 3862 3242 4248 -484 -282 -226 C ATOM 618 CG GLU A 81 22.346 1.212 -25.175 1.00 30.38 C ANISOU 618 CG GLU A 81 3857 3402 4283 -504 -292 -191 C ATOM 619 CD GLU A 81 23.460 1.491 -24.173 1.00 31.49 C ANISOU 619 CD GLU A 81 3914 3704 4347 -604 -303 -230 C ATOM 620 OE1 GLU A 81 23.251 1.294 -22.952 1.00 31.86 O ANISOU 620 OE1 GLU A 81 3930 3831 4343 -626 -322 -256 O ATOM 621 OE2 GLU A 81 24.560 1.893 -24.615 1.00 32.15 O ANISOU 621 OE2 GLU A 81 3955 3845 4413 -664 -294 -232 O ATOM 622 N ASP A 82 20.544 -2.045 -25.107 1.00 27.82 N ANISOU 622 N ASP A 82 3546 3054 3968 -225 -353 -43 N ATOM 623 CA ASP A 82 20.400 -3.095 -26.127 1.00 27.12 C ANISOU 623 CA ASP A 82 3474 2923 3906 -131 -352 24 C ATOM 624 C ASP A 82 19.171 -3.978 -25.932 1.00 26.42 C ANISOU 624 C ASP A 82 3429 2778 3831 -59 -357 43 C ATOM 625 O ASP A 82 18.803 -4.730 -26.839 1.00 25.90 O ANISOU 625 O ASP A 82 3395 2654 3790 4 -348 83 O ATOM 626 CB ASP A 82 21.653 -3.982 -26.166 1.00 27.37 C ANISOU 626 CB ASP A 82 3430 3070 3899 -95 -359 85 C ATOM 627 CG ASP A 82 22.925 -3.187 -26.415 1.00 28.05 C ANISOU 627 CG ASP A 82 3464 3229 3966 -168 -355 70 C ATOM 628 OD1 ASP A 82 22.851 -2.103 -27.034 1.00 27.96 O ANISOU 628 OD1 ASP A 82 3492 3142 3987 -229 -337 27 O ATOM 629 OD2 ASP A 82 24.009 -3.641 -25.983 1.00 28.50 O ANISOU 629 OD2 ASP A 82 3435 3421 3972 -164 -366 107 O ATOM 630 N PHE A 83 18.537 -3.905 -24.766 1.00 26.38 N ANISOU 630 N PHE A 83 3425 2794 3805 -74 -369 13 N ATOM 631 CA PHE A 83 17.310 -4.666 -24.534 1.00 25.90 C ANISOU 631 CA PHE A 83 3405 2680 3756 -16 -372 26 C ATOM 632 C PHE A 83 16.176 -4.073 -25.373 1.00 25.34 C ANISOU 632 C PHE A 83 3406 2484 3737 -13 -357 4 C ATOM 633 O PHE A 83 16.010 -2.853 -25.444 1.00 25.46 O ANISOU 633 O PHE A 83 3444 2456 3774 -66 -343 -41 O ATOM 634 CB PHE A 83 16.973 -4.732 -23.043 1.00 26.23 C ANISOU 634 CB PHE A 83 3423 2785 3757 -34 -389 2 C ATOM 635 CG PHE A 83 17.983 -5.512 -22.248 1.00 26.88 C ANISOU 635 CG PHE A 83 3428 3004 3781 -17 -404 45 C ATOM 636 CD1 PHE A 83 17.972 -6.902 -22.269 1.00 26.77 C ANISOU 636 CD1 PHE A 83 3404 3006 3759 70 -400 116 C ATOM 637 CD2 PHE A 83 18.973 -4.865 -21.517 1.00 27.71 C ANISOU 637 CD2 PHE A 83 3467 3225 3837 -89 -416 19 C ATOM 638 CE1 PHE A 83 18.910 -7.630 -21.559 1.00 27.40 C ANISOU 638 CE1 PHE A 83 3409 3214 3787 100 -407 172 C ATOM 639 CE2 PHE A 83 19.917 -5.587 -20.802 1.00 28.37 C ANISOU 639 CE2 PHE A 83 3466 3455 3858 -68 -431 71 C ATOM 640 CZ PHE A 83 19.886 -6.973 -20.823 1.00 28.21 C ANISOU 640 CZ PHE A 83 3434 3448 3834 35 -426 154 C ATOM 641 N GLY A 84 15.430 -4.960 -26.024 1.00 24.72 N ANISOU 641 N GLY A 84 3360 2355 3676 47 -353 38 N ATOM 642 CA GLY A 84 14.474 -4.600 -27.074 1.00 24.26 C ANISOU 642 CA GLY A 84 3356 2204 3657 59 -340 36 C ATOM 643 C GLY A 84 14.399 -5.732 -28.082 1.00 23.87 C ANISOU 643 C GLY A 84 3321 2136 3611 109 -332 80 C ATOM 644 O GLY A 84 14.792 -6.859 -27.779 1.00 23.97 O ANISOU 644 O GLY A 84 3317 2189 3602 144 -330 110 O ATOM 645 N SER A 85 13.912 -5.430 -29.281 1.00 23.51 N ANISOU 645 N SER A 85 3308 2033 3590 112 -321 87 N ATOM 646 CA SER A 85 13.745 -6.428 -30.335 1.00 23.20 C ANISOU 646 CA SER A 85 3290 1977 3549 145 -308 118 C ATOM 647 C SER A 85 14.706 -6.207 -31.498 1.00 23.05 C ANISOU 647 C SER A 85 3264 1957 3539 138 -295 137 C ATOM 648 O SER A 85 15.158 -5.086 -31.741 1.00 23.09 O ANISOU 648 O SER A 85 3259 1956 3560 106 -295 127 O ATOM 649 CB SER A 85 12.304 -6.434 -30.837 1.00 23.10 C ANISOU 649 CB SER A 85 3313 1920 3542 151 -308 114 C ATOM 650 OG SER A 85 11.466 -7.016 -29.857 1.00 23.46 O ANISOU 650 OG SER A 85 3366 1973 3574 164 -315 103 O ATOM 651 N TYR A 86 15.011 -7.294 -32.198 1.00 22.71 N ANISOU 651 N TYR A 86 3228 1916 3485 167 -275 162 N ATOM 652 CA TYR A 86 15.899 -7.274 -33.361 1.00 22.82 C ANISOU 652 CA TYR A 86 3237 1931 3503 166 -257 181 C ATOM 653 C TYR A 86 15.293 -8.103 -34.480 1.00 22.68 C ANISOU 653 C TYR A 86 3258 1883 3478 179 -234 189 C ATOM 654 O TYR A 86 14.667 -9.127 -34.211 1.00 22.63 O ANISOU 654 O TYR A 86 3275 1865 3458 197 -221 186 O ATOM 655 CB TYR A 86 17.282 -7.818 -32.988 1.00 23.03 C ANISOU 655 CB TYR A 86 3221 2010 3517 186 -246 205 C ATOM 656 CG TYR A 86 17.982 -6.956 -31.969 1.00 23.23 C ANISOU 656 CG TYR A 86 3200 2089 3539 157 -269 193 C ATOM 657 CD1 TYR A 86 17.798 -7.164 -30.602 1.00 23.26 C ANISOU 657 CD1 TYR A 86 3182 2130 3524 161 -285 185 C ATOM 658 CD2 TYR A 86 18.797 -5.898 -32.370 1.00 23.49 C ANISOU 658 CD2 TYR A 86 3208 2136 3579 114 -271 185 C ATOM 659 CE1 TYR A 86 18.419 -6.353 -29.662 1.00 23.60 C ANISOU 659 CE1 TYR A 86 3180 2234 3553 120 -305 165 C ATOM 660 CE2 TYR A 86 19.423 -5.081 -31.439 1.00 23.73 C ANISOU 660 CE2 TYR A 86 3197 2219 3600 69 -287 163 C ATOM 661 CZ TYR A 86 19.233 -5.312 -30.089 1.00 23.82 C ANISOU 661 CZ TYR A 86 3186 2276 3588 69 -304 151 C ATOM 662 OH TYR A 86 19.857 -4.502 -29.177 1.00 24.15 O ANISOU 662 OH TYR A 86 3185 2382 3610 12 -317 121 O ATOM 663 N PHE A 87 15.464 -7.656 -35.724 1.00 22.68 N ANISOU 663 N PHE A 87 3265 1871 3481 163 -225 197 N ATOM 664 CA PHE A 87 15.043 -8.446 -36.885 1.00 22.67 C ANISOU 664 CA PHE A 87 3296 1855 3462 163 -200 200 C ATOM 665 C PHE A 87 15.989 -8.306 -38.079 1.00 22.99 C ANISOU 665 C PHE A 87 3329 1904 3501 157 -179 217 C ATOM 666 O PHE A 87 16.629 -7.263 -38.260 1.00 23.01 O ANISOU 666 O PHE A 87 3308 1915 3520 143 -191 227 O ATOM 667 CB PHE A 87 13.592 -8.129 -37.286 1.00 22.40 C ANISOU 667 CB PHE A 87 3284 1812 3417 143 -214 190 C ATOM 668 CG PHE A 87 13.381 -6.743 -37.843 1.00 22.39 C ANISOU 668 CG PHE A 87 3269 1808 3429 127 -232 205 C ATOM 669 CD1 PHE A 87 13.581 -6.482 -39.195 1.00 22.55 C ANISOU 669 CD1 PHE A 87 3292 1839 3439 114 -220 224 C ATOM 670 CD2 PHE A 87 12.942 -5.706 -37.024 1.00 22.36 C ANISOU 670 CD2 PHE A 87 3257 1792 3449 126 -253 201 C ATOM 671 CE1 PHE A 87 13.370 -5.210 -39.718 1.00 22.66 C ANISOU 671 CE1 PHE A 87 3296 1848 3467 107 -228 248 C ATOM 672 CE2 PHE A 87 12.726 -4.433 -37.541 1.00 22.53 C ANISOU 672 CE2 PHE A 87 3274 1798 3489 119 -254 221 C ATOM 673 CZ PHE A 87 12.938 -4.185 -38.890 1.00 22.68 C ANISOU 673 CZ PHE A 87 3292 1825 3498 112 -242 249 C ATOM 674 N CYS A 88 16.069 -9.375 -38.873 1.00 23.24 N ANISOU 674 N CYS A 88 3388 1929 3513 164 -141 216 N ATOM 675 CA CYS A 88 16.808 -9.380 -40.132 1.00 23.59 C ANISOU 675 CA CYS A 88 3432 1980 3549 156 -114 227 C ATOM 676 C CYS A 88 15.850 -9.135 -41.293 1.00 23.23 C ANISOU 676 C CYS A 88 3409 1940 3479 120 -117 219 C ATOM 677 O CYS A 88 14.655 -9.399 -41.186 1.00 23.00 O ANISOU 677 O CYS A 88 3399 1910 3431 104 -126 203 O ATOM 678 CB CYS A 88 17.535 -10.713 -40.335 1.00 24.51 C ANISOU 678 CB CYS A 88 3567 2087 3657 185 -58 229 C ATOM 679 SG CYS A 88 16.467 -12.168 -40.440 1.00 25.28 S ANISOU 679 SG CYS A 88 3728 2149 3730 178 -13 197 S ATOM 680 N GLN A 89 16.386 -8.619 -42.395 1.00 23.01 N ANISOU 680 N GLN A 89 3371 1927 3444 105 -109 236 N ATOM 681 CA GLN A 89 15.621 -8.423 -43.625 1.00 22.89 C ANISOU 681 CA GLN A 89 3367 1935 3394 71 -109 238 C ATOM 682 C GLN A 89 16.524 -8.715 -44.810 1.00 22.98 C ANISOU 682 C GLN A 89 3382 1961 3388 62 -72 243 C ATOM 683 O GLN A 89 17.692 -8.339 -44.790 1.00 23.00 O ANISOU 683 O GLN A 89 3363 1960 3415 78 -66 261 O ATOM 684 CB GLN A 89 15.099 -6.984 -43.705 1.00 22.77 C ANISOU 684 CB GLN A 89 3329 1931 3393 65 -147 267 C ATOM 685 CG GLN A 89 14.151 -6.719 -44.869 1.00 22.98 C ANISOU 685 CG GLN A 89 3355 2000 3377 39 -152 285 C ATOM 686 CD GLN A 89 13.704 -5.272 -44.972 1.00 23.06 C ANISOU 686 CD GLN A 89 3342 2013 3406 49 -176 329 C ATOM 687 OE1 GLN A 89 14.008 -4.444 -44.111 1.00 23.08 O ANISOU 687 OE1 GLN A 89 3337 1976 3456 67 -187 337 O ATOM 688 NE2 GLN A 89 12.969 -4.961 -46.030 1.00 23.41 N ANISOU 688 NE2 GLN A 89 3375 2109 3410 36 -179 361 N ATOM 689 N GLN A 90 15.982 -9.379 -45.832 1.00 23.01 N ANISOU 689 N GLN A 90 3412 1988 3345 28 -46 224 N ATOM 690 CA GLN A 90 16.733 -9.681 -47.057 1.00 23.30 C ANISOU 690 CA GLN A 90 3455 2041 3355 12 -6 223 C ATOM 691 C GLN A 90 16.280 -8.775 -48.200 1.00 23.41 C ANISOU 691 C GLN A 90 3450 2109 3336 -21 -28 250 C ATOM 692 O GLN A 90 15.103 -8.419 -48.288 1.00 23.37 O ANISOU 692 O GLN A 90 3436 2137 3305 -40 -58 257 O ATOM 693 CB GLN A 90 16.641 -11.173 -47.435 1.00 23.59 C ANISOU 693 CB GLN A 90 3540 2063 3358 -7 56 177 C ATOM 694 CG GLN A 90 15.276 -11.683 -47.897 1.00 23.72 C ANISOU 694 CG GLN A 90 3584 2112 3318 -65 59 141 C ATOM 695 CD GLN A 90 14.968 -11.411 -49.365 1.00 24.05 C ANISOU 695 CD GLN A 90 3617 2223 3298 -120 63 141 C ATOM 696 OE1 GLN A 90 15.862 -11.162 -50.178 1.00 24.21 O ANISOU 696 OE1 GLN A 90 3629 2255 3316 -117 82 156 O ATOM 697 NE2 GLN A 90 13.686 -11.454 -49.706 1.00 24.15 N ANISOU 697 NE2 GLN A 90 3625 2294 3255 -171 43 127 N ATOM 698 N PHE A 91 17.232 -8.417 -49.062 1.00 23.63 N ANISOU 698 N PHE A 91 3465 2152 3362 -23 -11 270 N ATOM 699 CA PHE A 91 17.011 -7.509 -50.197 1.00 23.89 C ANISOU 699 CA PHE A 91 3476 2237 3365 -47 -26 308 C ATOM 700 C PHE A 91 17.485 -8.113 -51.518 1.00 24.42 C ANISOU 700 C PHE A 91 3555 2342 3382 -80 19 293 C ATOM 701 O PHE A 91 17.729 -7.390 -52.485 1.00 24.52 O ANISOU 701 O PHE A 91 3547 2396 3375 -93 15 329 O ATOM 702 CB PHE A 91 17.725 -6.187 -49.941 1.00 23.77 C ANISOU 702 CB PHE A 91 3429 2201 3401 -21 -48 356 C ATOM 703 CG PHE A 91 17.416 -5.594 -48.604 1.00 23.40 C ANISOU 703 CG PHE A 91 3374 2111 3404 5 -81 361 C ATOM 704 CD1 PHE A 91 16.315 -4.761 -48.431 1.00 23.34 C ANISOU 704 CD1 PHE A 91 3358 2111 3398 8 -112 389 C ATOM 705 CD2 PHE A 91 18.209 -5.888 -47.508 1.00 23.15 C ANISOU 705 CD2 PHE A 91 3341 2040 3413 28 -78 340 C ATOM 706 CE1 PHE A 91 16.022 -4.226 -47.186 1.00 23.05 C ANISOU 706 CE1 PHE A 91 3319 2031 3407 30 -134 387 C ATOM 707 CE2 PHE A 91 17.923 -5.351 -46.265 1.00 22.95 C ANISOU 707 CE2 PHE A 91 3309 1985 3428 43 -106 339 C ATOM 708 CZ PHE A 91 16.828 -4.517 -46.100 1.00 22.80 C ANISOU 708 CZ PHE A 91 3289 1961 3413 42 -133 358 C ATOM 709 N TRP A 92 17.583 -9.445 -51.556 1.00 24.72 N ANISOU 709 N TRP A 92 3632 2362 3398 -94 67 239 N ATOM 710 CA TRP A 92 18.042 -10.159 -52.738 1.00 25.35 C ANISOU 710 CA TRP A 92 3735 2468 3430 -129 124 211 C ATOM 711 C TRP A 92 16.930 -10.217 -53.790 1.00 25.82 C ANISOU 711 C TRP A 92 3795 2611 3406 -197 117 197 C ATOM 712 O TRP A 92 17.175 -9.932 -54.962 1.00 26.31 O ANISOU 712 O TRP A 92 3843 2731 3423 -227 128 212 O ATOM 713 CB TRP A 92 18.540 -11.563 -52.362 1.00 25.53 C ANISOU 713 CB TRP A 92 3807 2430 3465 -116 193 159 C ATOM 714 CG TRP A 92 18.746 -12.456 -53.536 1.00 26.18 C ANISOU 714 CG TRP A 92 3928 2530 3491 -163 265 113 C ATOM 715 CD1 TRP A 92 18.141 -13.654 -53.763 1.00 26.59 C ANISOU 715 CD1 TRP A 92 4035 2567 3499 -211 323 47 C ATOM 716 CD2 TRP A 92 19.592 -12.212 -54.663 1.00 26.63 C ANISOU 716 CD2 TRP A 92 3973 2620 3524 -174 292 126 C ATOM 717 NE1 TRP A 92 18.564 -14.180 -54.954 1.00 27.26 N ANISOU 717 NE1 TRP A 92 4149 2675 3536 -254 389 12 N ATOM 718 CE2 TRP A 92 19.453 -13.314 -55.533 1.00 27.26 C ANISOU 718 CE2 TRP A 92 4105 2707 3546 -229 369 61 C ATOM 719 CE3 TRP A 92 20.463 -11.173 -55.020 1.00 26.56 C ANISOU 719 CE3 TRP A 92 3917 2636 3538 -147 265 182 C ATOM 720 CZ2 TRP A 92 20.156 -13.413 -56.739 1.00 27.79 C ANISOU 720 CZ2 TRP A 92 4178 2808 3575 -255 416 52 C ATOM 721 CZ3 TRP A 92 21.159 -11.268 -56.224 1.00 27.05 C ANISOU 721 CZ3 TRP A 92 3982 2733 3564 -170 309 178 C ATOM 722 CH2 TRP A 92 20.997 -12.382 -57.069 1.00 27.69 C ANISOU 722 CH2 TRP A 92 4113 2823 3584 -222 383 113 C ATOM 723 N THR A 93 15.722 -10.595 -53.372 1.00 25.93 N ANISOU 723 N THR A 93 3818 2640 3393 -225 100 171 N ATOM 724 CA THR A 93 14.553 -10.600 -54.260 1.00 26.48 C ANISOU 724 CA THR A 93 3874 2813 3376 -294 86 164 C ATOM 725 C THR A 93 13.344 -9.967 -53.591 1.00 26.27 C ANISOU 725 C THR A 93 3813 2818 3350 -283 24 197 C ATOM 726 O THR A 93 13.186 -10.044 -52.370 1.00 25.67 O ANISOU 726 O THR A 93 3748 2676 3330 -244 9 191 O ATOM 727 CB THR A 93 14.142 -12.027 -54.684 1.00 27.06 C ANISOU 727 CB THR A 93 3999 2898 3384 -370 149 77 C ATOM 728 OG1 THR A 93 13.927 -12.839 -53.521 1.00 26.80 O ANISOU 728 OG1 THR A 93 4007 2781 3393 -352 169 37 O ATOM 729 CG2 THR A 93 15.203 -12.665 -55.582 1.00 27.55 C ANISOU 729 CG2 THR A 93 4097 2942 3428 -390 222 41 C ATOM 730 N THR A 94 12.496 -9.344 -54.409 1.00 26.74 N ANISOU 730 N THR A 94 3828 2988 3344 -314 -8 237 N ATOM 731 CA THR A 94 11.181 -8.899 -53.974 1.00 26.75 C ANISOU 731 CA THR A 94 3792 3044 3326 -312 -57 268 C ATOM 732 C THR A 94 10.201 -10.068 -54.157 1.00 27.18 C ANISOU 732 C THR A 94 3865 3161 3301 -396 -36 197 C ATOM 733 O THR A 94 10.366 -10.847 -55.095 1.00 27.86 O ANISOU 733 O THR A 94 3973 3291 3319 -468 8 145 O ATOM 734 CB THR A 94 10.695 -7.668 -54.754 1.00 27.08 C ANISOU 734 CB THR A 94 3770 3187 3334 -296 -96 360 C ATOM 735 OG1 THR A 94 10.777 -7.916 -56.160 1.00 27.80 O ANISOU 735 OG1 THR A 94 3847 3381 3335 -358 -75 355 O ATOM 736 CG2 THR A 94 11.547 -6.456 -54.402 1.00 26.76 C ANISOU 736 CG2 THR A 94 3719 3068 3381 -216 -110 427 C ATOM 737 N PRO A 95 9.196 -10.212 -53.286 1.00 27.02 N ANISOU 737 N PRO A 95 3838 3144 3285 -396 -62 188 N ATOM 738 CA PRO A 95 8.955 -9.315 -52.152 1.00 26.42 C ANISOU 738 CA PRO A 95 3739 3015 3285 -314 -108 243 C ATOM 739 C PRO A 95 10.009 -9.446 -51.053 1.00 25.76 C ANISOU 739 C PRO A 95 3699 2787 3301 -255 -92 224 C ATOM 740 O PRO A 95 10.452 -10.557 -50.754 1.00 25.70 O ANISOU 740 O PRO A 95 3743 2719 3303 -276 -47 158 O ATOM 741 CB PRO A 95 7.582 -9.765 -51.639 1.00 26.56 C ANISOU 741 CB PRO A 95 3743 3086 3261 -350 -126 219 C ATOM 742 CG PRO A 95 7.495 -11.202 -52.025 1.00 26.96 C ANISOU 742 CG PRO A 95 3843 3149 3252 -443 -73 126 C ATOM 743 CD PRO A 95 8.205 -11.305 -53.343 1.00 27.45 C ANISOU 743 CD PRO A 95 3909 3255 3264 -483 -41 118 C ATOM 744 N TYR A 96 10.430 -8.313 -50.488 1.00 25.20 N ANISOU 744 N TYR A 96 3606 2667 3300 -184 -122 282 N ATOM 745 CA TYR A 96 11.363 -8.325 -49.363 1.00 24.57 C ANISOU 745 CA TYR A 96 3553 2475 3306 -133 -115 268 C ATOM 746 C TYR A 96 10.693 -9.037 -48.201 1.00 24.31 C ANISOU 746 C TYR A 96 3542 2407 3287 -133 -119 227 C ATOM 747 O TYR A 96 9.494 -8.867 -47.971 1.00 24.47 O ANISOU 747 O TYR A 96 3542 2476 3282 -143 -146 237 O ATOM 748 CB TYR A 96 11.773 -6.914 -48.927 1.00 24.19 C ANISOU 748 CB TYR A 96 3478 2390 3323 -74 -144 330 C ATOM 749 CG TYR A 96 12.382 -6.073 -50.023 1.00 24.43 C ANISOU 749 CG TYR A 96 3487 2451 3345 -71 -139 381 C ATOM 750 CD1 TYR A 96 13.469 -6.533 -50.759 1.00 24.50 C ANISOU 750 CD1 TYR A 96 3512 2454 3343 -90 -105 361 C ATOM 751 CD2 TYR A 96 11.866 -4.819 -50.328 1.00 24.56 C ANISOU 751 CD2 TYR A 96 3467 2499 3365 -45 -162 454 C ATOM 752 CE1 TYR A 96 14.029 -5.763 -51.768 1.00 24.79 C ANISOU 752 CE1 TYR A 96 3528 2522 3371 -90 -100 409 C ATOM 753 CE2 TYR A 96 12.417 -4.042 -51.331 1.00 24.92 C ANISOU 753 CE2 TYR A 96 3495 2570 3403 -40 -152 507 C ATOM 754 CZ TYR A 96 13.497 -4.516 -52.048 1.00 24.97 C ANISOU 754 CZ TYR A 96 3515 2575 3396 -66 -124 482 C ATOM 755 OH TYR A 96 14.036 -3.745 -53.039 1.00 25.29 O ANISOU 755 OH TYR A 96 3538 2643 3428 -64 -114 536 O ATOM 756 N THR A 97 11.473 -9.839 -47.485 1.00 24.07 N ANISOU 756 N THR A 97 3551 2298 3296 -117 -88 188 N ATOM 757 CA THR A 97 10.959 -10.671 -46.408 1.00 23.90 C ANISOU 757 CA THR A 97 3557 2238 3287 -116 -80 149 C ATOM 758 C THR A 97 11.822 -10.496 -45.169 1.00 23.56 C ANISOU 758 C THR A 97 3518 2117 3318 -54 -85 159 C ATOM 759 O THR A 97 13.009 -10.163 -45.263 1.00 23.28 O ANISOU 759 O THR A 97 3475 2055 3316 -25 -76 178 O ATOM 760 CB THR A 97 10.911 -12.154 -46.814 1.00 24.26 C ANISOU 760 CB THR A 97 3654 2274 3290 -169 -18 86 C ATOM 761 OG1 THR A 97 12.178 -12.541 -47.355 1.00 24.42 O ANISOU 761 OG1 THR A 97 3699 2257 3324 -158 31 78 O ATOM 762 CG2 THR A 97 9.815 -12.405 -47.860 1.00 24.78 C ANISOU 762 CG2 THR A 97 3712 2436 3268 -250 -16 63 C ATOM 763 N PHE A 98 11.202 -10.735 -44.016 1.00 23.46 N ANISOU 763 N PHE A 98 3510 2080 3322 -40 -100 147 N ATOM 764 CA PHE A 98 11.777 -10.433 -42.712 1.00 23.27 C ANISOU 764 CA PHE A 98 3479 2004 3357 12 -116 159 C ATOM 765 C PHE A 98 11.844 -11.686 -41.864 1.00 23.49 C ANISOU 765 C PHE A 98 3543 1990 3393 22 -81 127 C ATOM 766 O PHE A 98 10.999 -12.576 -41.990 1.00 23.77 O ANISOU 766 O PHE A 98 3609 2029 3392 -16 -57 94 O ATOM 767 CB PHE A 98 10.896 -9.432 -41.966 1.00 22.97 C ANISOU 767 CB PHE A 98 3412 1979 3336 27 -166 180 C ATOM 768 CG PHE A 98 10.737 -8.109 -42.657 1.00 23.03 C ANISOU 768 CG PHE A 98 3386 2017 3345 30 -192 222 C ATOM 769 CD1 PHE A 98 9.828 -7.955 -43.696 1.00 23.40 C ANISOU 769 CD1 PHE A 98 3419 2130 3341 0 -198 238 C ATOM 770 CD2 PHE A 98 11.464 -7.003 -42.237 1.00 22.95 C ANISOU 770 CD2 PHE A 98 3359 1976 3385 61 -207 249 C ATOM 771 CE1 PHE A 98 9.664 -6.727 -44.321 1.00 23.64 C ANISOU 771 CE1 PHE A 98 3418 2190 3374 15 -216 291 C ATOM 772 CE2 PHE A 98 11.302 -5.771 -42.854 1.00 23.16 C ANISOU 772 CE2 PHE A 98 3363 2018 3418 67 -218 293 C ATOM 773 CZ PHE A 98 10.404 -5.634 -43.900 1.00 23.46 C ANISOU 773 CZ PHE A 98 3387 2117 3409 51 -222 320 C ATOM 774 N GLY A 99 12.832 -11.739 -40.975 1.00 23.65 N ANISOU 774 N GLY A 99 3557 1973 3455 70 -75 141 N ATOM 775 CA GLY A 99 12.839 -12.729 -39.904 1.00 23.88 C ANISOU 775 CA GLY A 99 3610 1965 3498 95 -49 129 C ATOM 776 C GLY A 99 11.712 -12.425 -38.934 1.00 23.84 C ANISOU 776 C GLY A 99 3596 1969 3493 90 -90 122 C ATOM 777 O GLY A 99 11.242 -11.280 -38.851 1.00 23.57 O ANISOU 777 O GLY A 99 3530 1961 3466 86 -139 136 O ATOM 778 N GLY A 100 11.287 -13.446 -38.192 1.00 24.09 N ANISOU 778 N GLY A 100 3659 1974 3521 94 -63 105 N ATOM 779 CA GLY A 100 10.195 -13.318 -37.223 1.00 24.15 C ANISOU 779 CA GLY A 100 3660 1989 3526 89 -95 96 C ATOM 780 C GLY A 100 10.513 -12.505 -35.979 1.00 24.15 C ANISOU 780 C GLY A 100 3623 1993 3561 130 -138 118 C ATOM 781 O GLY A 100 9.618 -12.208 -35.189 1.00 24.03 O ANISOU 781 O GLY A 100 3598 1987 3545 127 -168 112 O ATOM 782 N GLY A 101 11.787 -12.166 -35.791 1.00 24.50 N ANISOU 782 N GLY A 101 3644 2035 3630 164 -139 142 N ATOM 783 CA GLY A 101 12.221 -11.261 -34.735 1.00 24.65 C ANISOU 783 CA GLY A 101 3622 2070 3673 186 -178 155 C ATOM 784 C GLY A 101 12.759 -12.007 -33.532 1.00 25.06 C ANISOU 784 C GLY A 101 3668 2124 3730 225 -163 169 C ATOM 785 O GLY A 101 12.473 -13.192 -33.348 1.00 25.23 O ANISOU 785 O GLY A 101 3723 2121 3741 238 -124 168 O ATOM 786 N THR A 102 13.555 -11.306 -32.731 1.00 25.41 N ANISOU 786 N THR A 102 3668 2199 3786 240 -190 183 N ATOM 787 CA THR A 102 14.088 -11.830 -31.475 1.00 26.03 C ANISOU 787 CA THR A 102 3725 2305 3862 277 -186 204 C ATOM 788 C THR A 102 13.887 -10.760 -30.418 1.00 26.45 C ANISOU 788 C THR A 102 3742 2391 3916 257 -234 188 C ATOM 789 O THR A 102 14.411 -9.657 -30.560 1.00 26.47 O ANISOU 789 O THR A 102 3717 2413 3928 233 -257 180 O ATOM 790 CB THR A 102 15.592 -12.153 -31.584 1.00 26.29 C ANISOU 790 CB THR A 102 3725 2369 3896 313 -162 242 C ATOM 791 OG1 THR A 102 15.796 -13.158 -32.583 1.00 26.50 O ANISOU 791 OG1 THR A 102 3790 2355 3923 333 -105 254 O ATOM 792 CG2 THR A 102 16.161 -12.640 -30.249 1.00 26.57 C ANISOU 792 CG2 THR A 102 3722 2455 3919 356 -160 277 C ATOM 793 N LYS A 103 13.123 -11.085 -29.374 1.00 26.95 N ANISOU 793 N LYS A 103 3811 2458 3969 264 -243 180 N ATOM 794 CA LYS A 103 12.961 -10.198 -28.229 1.00 27.45 C ANISOU 794 CA LYS A 103 3844 2557 4029 245 -281 161 C ATOM 795 C LYS A 103 14.054 -10.506 -27.211 1.00 27.75 C ANISOU 795 C LYS A 103 3833 2663 4047 270 -282 190 C ATOM 796 O LYS A 103 14.155 -11.635 -26.730 1.00 27.77 O ANISOU 796 O LYS A 103 3838 2677 4037 313 -258 224 O ATOM 797 CB LYS A 103 11.576 -10.364 -27.602 1.00 27.94 C ANISOU 797 CB LYS A 103 3931 2598 4085 239 -289 140 C ATOM 798 CG LYS A 103 11.274 -9.344 -26.509 1.00 28.62 C ANISOU 798 CG LYS A 103 3994 2712 4169 216 -321 111 C ATOM 799 CD LYS A 103 9.777 -9.152 -26.308 1.00 28.85 C ANISOU 799 CD LYS A 103 4050 2711 4201 205 -329 86 C ATOM 800 CE LYS A 103 9.497 -8.198 -25.158 1.00 29.36 C ANISOU 800 CE LYS A 103 4096 2797 4263 184 -350 55 C ATOM 801 NZ LYS A 103 8.068 -7.770 -25.105 1.00 29.58 N ANISOU 801 NZ LYS A 103 4145 2794 4299 178 -353 34 N ATOM 802 N VAL A 104 14.875 -9.503 -26.905 1.00 27.82 N ANISOU 802 N VAL A 104 3798 2722 4052 240 -305 179 N ATOM 803 CA VAL A 104 15.974 -9.642 -25.960 1.00 28.46 C ANISOU 803 CA VAL A 104 3817 2896 4102 251 -313 205 C ATOM 804 C VAL A 104 15.537 -9.020 -24.637 1.00 28.91 C ANISOU 804 C VAL A 104 3853 2996 4137 216 -343 171 C ATOM 805 O VAL A 104 15.426 -7.792 -24.535 1.00 28.80 O ANISOU 805 O VAL A 104 3836 2977 4130 158 -360 122 O ATOM 806 CB VAL A 104 17.259 -8.964 -26.487 1.00 28.71 C ANISOU 806 CB VAL A 104 3805 2972 4133 227 -316 211 C ATOM 807 CG1 VAL A 104 18.388 -9.053 -25.460 1.00 29.26 C ANISOU 807 CG1 VAL A 104 3795 3163 4158 230 -328 240 C ATOM 808 CG2 VAL A 104 17.681 -9.592 -27.812 1.00 28.55 C ANISOU 808 CG2 VAL A 104 3807 2909 4133 263 -283 243 C ATOM 809 N GLU A 105 15.279 -9.871 -23.640 1.00 29.32 N ANISOU 809 N GLU A 105 3893 3084 4163 251 -341 197 N ATOM 810 CA GLU A 105 14.835 -9.421 -22.309 1.00 29.94 C ANISOU 810 CA GLU A 105 3951 3213 4213 220 -366 166 C ATOM 811 C GLU A 105 15.930 -9.596 -21.252 1.00 30.40 C ANISOU 811 C GLU A 105 3931 3403 4218 224 -379 199 C ATOM 812 O GLU A 105 16.900 -10.336 -21.449 1.00 30.57 O ANISOU 812 O GLU A 105 3914 3475 4225 272 -363 262 O ATOM 813 CB GLU A 105 13.543 -10.129 -21.866 1.00 30.18 C ANISOU 813 CB GLU A 105 4025 3196 4247 247 -359 166 C ATOM 814 CG GLU A 105 13.621 -11.649 -21.797 1.00 30.89 C ANISOU 814 CG GLU A 105 4124 3283 4329 317 -326 231 C ATOM 815 CD GLU A 105 13.094 -12.228 -20.493 1.00 31.64 C ANISOU 815 CD GLU A 105 4209 3419 4392 337 -329 248 C ATOM 816 OE1 GLU A 105 11.910 -12.020 -20.165 1.00 31.71 O ANISOU 816 OE1 GLU A 105 4252 3389 4408 313 -338 208 O ATOM 817 OE2 GLU A 105 13.874 -12.907 -19.795 1.00 32.83 O ANISOU 817 OE2 GLU A 105 4314 3649 4511 380 -319 308 O ATOM 818 N ILE A 106 15.749 -8.902 -20.130 1.00 30.46 N ANISOU 818 N ILE A 106 3911 3472 4192 172 -404 157 N ATOM 819 CA ILE A 106 16.716 -8.897 -19.035 1.00 31.16 C ANISOU 819 CA ILE A 106 3915 3710 4215 156 -422 179 C ATOM 820 C ILE A 106 16.537 -10.158 -18.193 1.00 31.27 C ANISOU 820 C ILE A 106 3910 3774 4197 229 -414 248 C ATOM 821 O ILE A 106 15.441 -10.427 -17.688 1.00 31.05 O ANISOU 821 O ILE A 106 3922 3700 4174 238 -412 232 O ATOM 822 CB ILE A 106 16.579 -7.641 -18.137 1.00 31.57 C ANISOU 822 CB ILE A 106 3949 3811 4235 60 -445 97 C ATOM 823 CG1 ILE A 106 16.712 -6.359 -18.968 1.00 31.53 C ANISOU 823 CG1 ILE A 106 3973 3737 4268 -10 -439 30 C ATOM 824 CG2 ILE A 106 17.633 -7.653 -17.025 1.00 32.47 C ANISOU 824 CG2 ILE A 106 3965 4104 4267 31 -466 117 C ATOM 825 CD1 ILE A 106 16.102 -5.142 -18.311 1.00 31.82 C ANISOU 825 CD1 ILE A 106 4036 3753 4301 -94 -439 -60 C ATOM 826 N LYS A 107 17.618 -10.925 -18.053 1.00 31.69 N ANISOU 826 N LYS A 107 3900 3924 4219 284 -404 330 N ATOM 827 CA LYS A 107 17.627 -12.126 -17.222 1.00 31.90 C ANISOU 827 CA LYS A 107 3899 4010 4211 362 -387 413 C ATOM 828 C LYS A 107 17.705 -11.717 -15.758 1.00 32.15 C ANISOU 828 C LYS A 107 3864 4184 4170 317 -422 399 C ATOM 829 O LYS A 107 18.374 -10.744 -15.410 1.00 32.72 O ANISOU 829 O LYS A 107 3876 4357 4198 239 -453 355 O ATOM 830 CB LYS A 107 18.817 -13.028 -17.566 1.00 32.52 C ANISOU 830 CB LYS A 107 3926 4152 4280 446 -356 516 C ATOM 831 N ARG A 108 16.999 -12.457 -14.911 1.00 31.80 N ANISOU 831 N ARG A 108 3831 4145 4108 359 -414 432 N ATOM 832 CA ARG A 108 17.101 -12.295 -13.464 1.00 32.16 C ANISOU 832 CA ARG A 108 3806 4340 4073 330 -443 436 C ATOM 833 C ARG A 108 16.702 -13.598 -12.779 1.00 32.15 C ANISOU 833 C ARG A 108 3808 4350 4056 422 -415 527 C ATOM 834 O ARG A 108 16.305 -14.557 -13.448 1.00 31.73 O ANISOU 834 O ARG A 108 3820 4177 4059 498 -369 574 O ATOM 835 CB ARG A 108 16.229 -11.130 -12.989 1.00 31.84 C ANISOU 835 CB ARG A 108 3798 4271 4028 226 -471 318 C ATOM 836 CG ARG A 108 14.737 -11.277 -13.283 1.00 31.06 C ANISOU 836 CG ARG A 108 3801 4010 3991 238 -455 277 C ATOM 837 CD ARG A 108 13.908 -10.572 -12.227 1.00 31.09 C ANISOU 837 CD ARG A 108 3810 4041 3963 170 -475 202 C ATOM 838 NE ARG A 108 14.017 -11.254 -10.933 1.00 31.70 N ANISOU 838 NE ARG A 108 3829 4248 3967 198 -483 259 N ATOM 839 CZ ARG A 108 13.933 -10.676 -9.732 1.00 32.08 C ANISOU 839 CZ ARG A 108 3835 4409 3947 132 -507 214 C ATOM 840 NH1 ARG A 108 13.733 -9.364 -9.593 1.00 32.05 N ANISOU 840 NH1 ARG A 108 3844 4395 3939 30 -519 102 N ATOM 841 NH2 ARG A 108 14.056 -11.429 -8.644 1.00 32.64 N ANISOU 841 NH2 ARG A 108 3850 4603 3950 170 -511 282 N ATOM 842 N THR A 109 16.801 -13.630 -11.454 1.00 32.44 N ANISOU 842 N THR A 109 3778 4533 4016 411 -437 550 N ATOM 843 CA THR A 109 16.401 -14.812 -10.694 1.00 32.57 C ANISOU 843 CA THR A 109 3794 4569 4012 497 -408 641 C ATOM 844 C THR A 109 14.882 -15.012 -10.749 1.00 31.45 C ANISOU 844 C THR A 109 3757 4270 3923 490 -392 588 C ATOM 845 O THR A 109 14.112 -14.053 -10.918 1.00 30.64 O ANISOU 845 O THR A 109 3700 4098 3845 407 -417 478 O ATOM 846 CB THR A 109 16.842 -14.723 -9.222 1.00 33.63 C ANISOU 846 CB THR A 109 3824 4914 4040 478 -440 677 C ATOM 847 OG1 THR A 109 16.326 -13.517 -8.641 1.00 33.71 O ANISOU 847 OG1 THR A 109 3835 4955 4018 356 -485 554 O ATOM 848 CG2 THR A 109 18.361 -14.738 -9.116 1.00 34.60 C ANISOU 848 CG2 THR A 109 3829 5218 4099 499 -452 754 C ATOM 849 N VAL A 110 14.469 -16.268 -10.608 1.00 31.13 N ANISOU 849 N VAL A 110 3752 4176 3901 579 -344 670 N ATOM 850 CA VAL A 110 13.054 -16.632 -10.585 1.00 30.25 C ANISOU 850 CA VAL A 110 3732 3933 3830 575 -323 633 C ATOM 851 C VAL A 110 12.399 -15.934 -9.387 1.00 29.92 C ANISOU 851 C VAL A 110 3664 3972 3734 506 -367 572 C ATOM 852 O VAL A 110 12.958 -15.925 -8.294 1.00 30.54 O ANISOU 852 O VAL A 110 3659 4212 3733 507 -388 615 O ATOM 853 CB VAL A 110 12.869 -18.173 -10.516 1.00 30.65 C ANISOU 853 CB VAL A 110 3819 3926 3899 680 -253 742 C ATOM 854 CG1 VAL A 110 11.417 -18.555 -10.236 1.00 30.29 C ANISOU 854 CG1 VAL A 110 3853 3779 3879 664 -234 706 C ATOM 855 CG2 VAL A 110 13.351 -18.820 -11.811 1.00 30.56 C ANISOU 855 CG2 VAL A 110 3854 3805 3951 737 -198 781 C ATOM 856 N ALA A 111 11.246 -15.314 -9.620 1.00 28.88 N ANISOU 856 N ALA A 111 3598 3735 3639 444 -379 473 N ATOM 857 CA ALA A 111 10.491 -14.621 -8.576 1.00 28.67 C ANISOU 857 CA ALA A 111 3562 3762 3571 379 -411 405 C ATOM 858 C ALA A 111 9.026 -15.004 -8.694 1.00 27.90 C ANISOU 858 C ALA A 111 3547 3536 3519 384 -388 376 C ATOM 859 O ALA A 111 8.411 -14.809 -9.744 1.00 27.13 O ANISOU 859 O ALA A 111 3515 3307 3487 371 -377 329 O ATOM 860 CB ALA A 111 10.657 -13.118 -8.712 1.00 28.58 C ANISOU 860 CB ALA A 111 3535 3768 3554 282 -449 296 C ATOM 861 N ALA A 112 8.471 -15.568 -7.625 1.00 28.07 N ANISOU 861 N ALA A 112 3561 3606 3501 402 -380 409 N ATOM 862 CA ALA A 112 7.060 -15.941 -7.602 1.00 27.58 C ANISOU 862 CA ALA A 112 3568 3441 3471 400 -358 383 C ATOM 863 C ALA A 112 6.198 -14.682 -7.555 1.00 27.10 C ANISOU 863 C ALA A 112 3526 3351 3420 320 -389 266 C ATOM 864 O ALA A 112 6.613 -13.677 -6.984 1.00 27.28 O ANISOU 864 O ALA A 112 3503 3461 3402 266 -422 214 O ATOM 865 CB ALA A 112 6.758 -16.822 -6.401 1.00 28.14 C ANISOU 865 CB ALA A 112 3620 3582 3492 438 -340 451 C ATOM 866 N PRO A 113 4.998 -14.731 -8.159 1.00 26.49 N ANISOU 866 N PRO A 113 3516 3153 3395 311 -373 226 N ATOM 867 CA PRO A 113 4.093 -13.595 -8.035 1.00 26.19 C ANISOU 867 CA PRO A 113 3494 3089 3367 251 -393 130 C ATOM 868 C PRO A 113 3.453 -13.515 -6.658 1.00 26.49 C ANISOU 868 C PRO A 113 3511 3202 3351 231 -399 112 C ATOM 869 O PRO A 113 3.219 -14.547 -6.030 1.00 26.66 O ANISOU 869 O PRO A 113 3531 3253 3347 268 -381 175 O ATOM 870 CB PRO A 113 3.011 -13.903 -9.071 1.00 25.57 C ANISOU 870 CB PRO A 113 3482 2883 3351 259 -370 115 C ATOM 871 CG PRO A 113 2.985 -15.390 -9.141 1.00 25.71 C ANISOU 871 CG PRO A 113 3522 2875 3371 311 -334 196 C ATOM 872 CD PRO A 113 4.412 -15.811 -8.974 1.00 26.20 C ANISOU 872 CD PRO A 113 3541 3005 3407 352 -331 266 C ATOM 873 N ASER A 114 3.198 -12.296 -6.188 0.50 26.59 N ANISOU 873 N ASER A 114 3512 3243 3348 172 -417 28 N ATOM 874 N BSER A 114 3.202 -12.290 -6.197 0.50 26.58 N ANISOU 874 N BSER A 114 3511 3241 3346 172 -417 27 N ATOM 875 CA ASER A 114 2.267 -12.074 -5.088 0.50 26.85 C ANISOU 875 CA ASER A 114 3542 3314 3344 147 -415 -10 C ATOM 876 CA BSER A 114 2.262 -12.040 -5.110 0.50 26.82 C ANISOU 876 CA BSER A 114 3539 3308 3341 146 -415 -12 C ATOM 877 C ASER A 114 0.891 -11.893 -5.725 0.50 26.30 C ANISOU 877 C ASER A 114 3531 3130 3334 148 -398 -49 C ATOM 878 C BSER A 114 0.890 -11.913 -5.758 0.50 26.27 C ANISOU 878 C BSER A 114 3527 3123 3331 150 -398 -47 C ATOM 879 O ASER A 114 0.734 -11.078 -6.636 0.50 25.98 O ANISOU 879 O ASER A 114 3515 3014 3343 133 -397 -95 O ATOM 880 O BSER A 114 0.733 -11.151 -6.715 0.50 25.92 O ANISOU 880 O BSER A 114 3509 3001 3338 137 -396 -90 O ATOM 881 CB ASER A 114 2.667 -10.847 -4.273 0.50 27.35 C ANISOU 881 CB ASER A 114 3571 3462 3360 79 -431 -88 C ATOM 882 CB BSER A 114 2.618 -10.754 -4.370 0.50 27.28 C ANISOU 882 CB BSER A 114 3566 3441 3357 77 -430 -95 C ATOM 883 OG ASER A 114 3.146 -9.816 -5.114 0.50 27.26 O ANISOU 883 OG ASER A 114 3571 3398 3387 45 -433 -143 O ATOM 884 OG BSER A 114 3.878 -10.866 -3.738 0.50 27.94 O ANISOU 884 OG BSER A 114 3585 3657 3373 63 -450 -63 O ATOM 885 N VAL A 115 -0.089 -12.662 -5.255 1.00 26.25 N ANISOU 885 N VAL A 115 3539 3117 3317 168 -383 -23 N ATOM 886 CA VAL A 115 -1.426 -12.725 -5.871 1.00 25.85 C ANISOU 886 CA VAL A 115 3533 2975 3313 171 -366 -44 C ATOM 887 C VAL A 115 -2.453 -11.955 -5.040 1.00 25.95 C ANISOU 887 C VAL A 115 3542 3009 3308 143 -362 -107 C ATOM 888 O VAL A 115 -2.533 -12.131 -3.829 1.00 26.26 O ANISOU 888 O VAL A 115 3557 3128 3291 133 -363 -105 O ATOM 889 CB VAL A 115 -1.873 -14.189 -6.071 1.00 25.76 C ANISOU 889 CB VAL A 115 3547 2932 3308 206 -342 26 C ATOM 890 CG1 VAL A 115 -3.176 -14.263 -6.861 1.00 25.36 C ANISOU 890 CG1 VAL A 115 3535 2802 3299 197 -326 3 C ATOM 891 CG2 VAL A 115 -0.775 -14.969 -6.787 1.00 25.82 C ANISOU 891 CG2 VAL A 115 3561 2919 3332 240 -333 90 C ATOM 892 N PHE A 116 -3.219 -11.093 -5.710 1.00 25.67 N ANISOU 892 N PHE A 116 3530 2906 3318 134 -354 -157 N ATOM 893 CA PHE A 116 -4.274 -10.305 -5.075 1.00 25.89 C ANISOU 893 CA PHE A 116 3558 2939 3339 117 -339 -214 C ATOM 894 C PHE A 116 -5.555 -10.451 -5.888 1.00 25.50 C ANISOU 894 C PHE A 116 3531 2824 3333 137 -325 -207 C ATOM 895 O PHE A 116 -5.494 -10.558 -7.112 1.00 25.12 O ANISOU 895 O PHE A 116 3499 2719 3327 150 -327 -187 O ATOM 896 CB PHE A 116 -3.876 -8.829 -5.004 1.00 26.27 C ANISOU 896 CB PHE A 116 3607 2977 3399 87 -332 -287 C ATOM 897 CG PHE A 116 -2.492 -8.591 -4.465 1.00 26.76 C ANISOU 897 CG PHE A 116 3642 3108 3418 53 -348 -300 C ATOM 898 CD1 PHE A 116 -2.269 -8.487 -3.102 1.00 27.53 C ANISOU 898 CD1 PHE A 116 3710 3304 3446 18 -350 -326 C ATOM 899 CD2 PHE A 116 -1.409 -8.460 -5.325 1.00 26.72 C ANISOU 899 CD2 PHE A 116 3636 3081 3437 52 -362 -285 C ATOM 900 CE1 PHE A 116 -0.993 -8.262 -2.600 1.00 28.02 C ANISOU 900 CE1 PHE A 116 3737 3453 3458 -22 -367 -337 C ATOM 901 CE2 PHE A 116 -0.132 -8.231 -4.833 1.00 27.18 C ANISOU 901 CE2 PHE A 116 3659 3218 3449 16 -377 -295 C ATOM 902 CZ PHE A 116 0.077 -8.133 -3.471 1.00 27.81 C ANISOU 902 CZ PHE A 116 3705 3408 3455 -23 -381 -320 C ATOM 903 N ILE A 117 -6.704 -10.442 -5.209 1.00 25.58 N ANISOU 903 N ILE A 117 3538 2856 3327 136 -309 -223 N ATOM 904 CA ILE A 117 -8.012 -10.557 -5.864 1.00 25.45 C ANISOU 904 CA ILE A 117 3528 2803 3338 151 -296 -215 C ATOM 905 C ILE A 117 -8.942 -9.427 -5.405 1.00 25.84 C ANISOU 905 C ILE A 117 3570 2854 3393 155 -272 -267 C ATOM 906 O ILE A 117 -8.935 -9.041 -4.235 1.00 26.08 O ANISOU 906 O ILE A 117 3593 2928 3390 140 -261 -303 O ATOM 907 CB ILE A 117 -8.655 -11.955 -5.652 1.00 25.37 C ANISOU 907 CB ILE A 117 3521 2816 3303 149 -292 -168 C ATOM 908 CG1 ILE A 117 -9.869 -12.139 -6.569 1.00 25.19 C ANISOU 908 CG1 ILE A 117 3500 2766 3305 150 -281 -158 C ATOM 909 CG2 ILE A 117 -9.047 -12.190 -4.197 1.00 25.77 C ANISOU 909 CG2 ILE A 117 3556 2933 3302 139 -284 -175 C ATOM 910 CD1 ILE A 117 -10.300 -13.582 -6.724 1.00 25.14 C ANISOU 910 CD1 ILE A 117 3507 2764 3282 133 -272 -115 C ATOM 911 N PHE A 118 -9.718 -8.902 -6.352 1.00 25.89 N ANISOU 911 N PHE A 118 3578 2818 3442 178 -259 -265 N ATOM 912 CA PHE A 118 -10.603 -7.763 -6.131 1.00 26.48 C ANISOU 912 CA PHE A 118 3646 2880 3534 199 -225 -302 C ATOM 913 C PHE A 118 -12.013 -8.113 -6.587 1.00 26.73 C ANISOU 913 C PHE A 118 3656 2929 3570 221 -217 -269 C ATOM 914 O PHE A 118 -12.218 -8.388 -7.767 1.00 26.35 O ANISOU 914 O PHE A 118 3603 2865 3545 230 -228 -232 O ATOM 915 CB PHE A 118 -10.124 -6.554 -6.928 1.00 26.49 C ANISOU 915 CB PHE A 118 3663 2816 3585 216 -208 -322 C ATOM 916 CG PHE A 118 -8.759 -6.077 -6.540 1.00 26.61 C ANISOU 916 CG PHE A 118 3695 2819 3594 184 -212 -362 C ATOM 917 CD1 PHE A 118 -8.590 -5.269 -5.422 1.00 27.13 C ANISOU 917 CD1 PHE A 118 3770 2899 3640 159 -183 -426 C ATOM 918 CD2 PHE A 118 -7.643 -6.429 -7.288 1.00 26.26 C ANISOU 918 CD2 PHE A 118 3659 2758 3562 172 -242 -338 C ATOM 919 CE1 PHE A 118 -7.333 -4.818 -5.056 1.00 27.36 C ANISOU 919 CE1 PHE A 118 3809 2934 3654 115 -186 -468 C ATOM 920 CE2 PHE A 118 -6.381 -5.982 -6.928 1.00 26.50 C ANISOU 920 CE2 PHE A 118 3696 2793 3580 138 -247 -373 C ATOM 921 CZ PHE A 118 -6.226 -5.173 -5.809 1.00 27.03 C ANISOU 921 CZ PHE A 118 3766 2883 3621 105 -220 -439 C ATOM 922 N PRO A 119 -12.990 -8.104 -5.659 1.00 27.58 N ANISOU 922 N PRO A 119 3747 3081 3652 224 -196 -282 N ATOM 923 CA PRO A 119 -14.386 -8.219 -6.075 1.00 28.03 C ANISOU 923 CA PRO A 119 3773 3166 3711 247 -183 -254 C ATOM 924 C PRO A 119 -14.823 -7.035 -6.944 1.00 28.55 C ANISOU 924 C PRO A 119 3828 3196 3825 297 -156 -248 C ATOM 925 O PRO A 119 -14.133 -6.016 -6.978 1.00 28.70 O ANISOU 925 O PRO A 119 3872 3158 3875 313 -135 -278 O ATOM 926 CB PRO A 119 -15.158 -8.205 -4.748 1.00 28.40 C ANISOU 926 CB PRO A 119 3805 3263 3721 245 -159 -279 C ATOM 927 CG PRO A 119 -14.166 -8.606 -3.713 1.00 28.35 C ANISOU 927 CG PRO A 119 3821 3271 3680 208 -173 -305 C ATOM 928 CD PRO A 119 -12.859 -8.065 -4.190 1.00 28.02 C ANISOU 928 CD PRO A 119 3805 3177 3665 204 -185 -321 C ATOM 929 N PRO A 120 -15.957 -7.167 -7.647 1.00 29.27 N ANISOU 929 N PRO A 120 3879 3325 3916 320 -152 -206 N ATOM 930 CA PRO A 120 -16.516 -5.997 -8.313 1.00 30.09 C ANISOU 930 CA PRO A 120 3964 3409 4060 383 -117 -187 C ATOM 931 C PRO A 120 -16.984 -4.992 -7.272 1.00 31.10 C ANISOU 931 C PRO A 120 4097 3524 4197 421 -61 -224 C ATOM 932 O PRO A 120 -17.506 -5.394 -6.230 1.00 31.10 O ANISOU 932 O PRO A 120 4086 3570 4160 404 -54 -245 O ATOM 933 CB PRO A 120 -17.707 -6.566 -9.088 1.00 30.12 C ANISOU 933 CB PRO A 120 3911 3492 4041 390 -129 -130 C ATOM 934 CG PRO A 120 -18.103 -7.776 -8.330 1.00 29.92 C ANISOU 934 CG PRO A 120 3878 3525 3965 334 -148 -139 C ATOM 935 CD PRO A 120 -16.829 -8.346 -7.783 1.00 29.39 C ANISOU 935 CD PRO A 120 3863 3411 3891 289 -171 -173 C ATOM 936 N SER A 121 -16.772 -3.708 -7.542 1.00 32.09 N ANISOU 936 N SER A 121 4242 3580 4372 470 -14 -234 N ATOM 937 CA SER A 121 -17.235 -2.648 -6.650 1.00 33.51 C ANISOU 937 CA SER A 121 4434 3730 4567 510 58 -272 C ATOM 938 C SER A 121 -18.759 -2.549 -6.683 1.00 34.85 C ANISOU 938 C SER A 121 4546 3964 4730 570 89 -224 C ATOM 939 O SER A 121 -19.397 -2.976 -7.646 1.00 34.65 O ANISOU 939 O SER A 121 4470 3997 4698 590 62 -156 O ATOM 940 CB SER A 121 -16.622 -1.299 -7.048 1.00 33.72 C ANISOU 940 CB SER A 121 4505 3653 4655 547 114 -291 C ATOM 941 OG SER A 121 -17.069 -0.884 -8.327 1.00 33.68 O ANISOU 941 OG SER A 121 4472 3638 4688 613 126 -217 O ATOM 942 N ASP A 122 -19.328 -1.971 -5.630 1.00 36.53 N ANISOU 942 N ASP A 122 4764 4174 4940 596 148 -260 N ATOM 943 CA ASP A 122 -20.765 -1.683 -5.588 1.00 38.03 C ANISOU 943 CA ASP A 122 4899 4422 5129 666 192 -214 C ATOM 944 C ASP A 122 -21.166 -0.688 -6.679 1.00 38.87 C ANISOU 944 C ASP A 122 4984 4494 5289 760 240 -148 C ATOM 945 O ASP A 122 -22.271 -0.776 -7.222 1.00 39.45 O ANISOU 945 O ASP A 122 4987 4650 5353 815 244 -73 O ATOM 946 CB ASP A 122 -21.171 -1.147 -4.212 1.00 39.09 C ANISOU 946 CB ASP A 122 5053 4545 5255 677 258 -274 C ATOM 947 CG ASP A 122 -20.986 -2.172 -3.105 1.00 39.29 C ANISOU 947 CG ASP A 122 5084 4628 5217 594 212 -323 C ATOM 948 OD1 ASP A 122 -21.194 -3.383 -3.358 1.00 39.18 O ANISOU 948 OD1 ASP A 122 5033 4692 5163 552 145 -287 O ATOM 949 OD2 ASP A 122 -20.629 -1.765 -1.977 1.00 40.00 O ANISOU 949 OD2 ASP A 122 5215 4687 5295 568 250 -398 O ATOM 950 N GLU A 123 -20.261 0.239 -6.997 1.00 39.29 N ANISOU 950 N GLU A 123 5097 4435 5396 776 278 -172 N ATOM 951 CA GLU A 123 -20.460 1.201 -8.085 1.00 40.10 C ANISOU 951 CA GLU A 123 5190 4491 5554 865 327 -103 C ATOM 952 C GLU A 123 -20.666 0.519 -9.433 1.00 39.32 C ANISOU 952 C GLU A 123 5030 4473 5438 869 257 -17 C ATOM 953 O GLU A 123 -21.569 0.894 -10.179 1.00 39.63 O ANISOU 953 O GLU A 123 5008 4563 5486 951 283 70 O ATOM 954 CB GLU A 123 -19.275 2.166 -8.180 1.00 40.86 C ANISOU 954 CB GLU A 123 5371 4448 5707 857 373 -154 C ATOM 955 CG GLU A 123 -19.192 3.146 -7.022 1.00 42.31 C ANISOU 955 CG GLU A 123 5619 4542 5916 865 471 -236 C ATOM 956 CD GLU A 123 -17.792 3.684 -6.810 1.00 42.81 C ANISOU 956 CD GLU A 123 5767 4496 6004 798 489 -320 C ATOM 957 OE1 GLU A 123 -17.267 4.360 -7.725 1.00 43.52 O ANISOU 957 OE1 GLU A 123 5885 4506 6145 826 516 -292 O ATOM 958 OE2 GLU A 123 -17.220 3.433 -5.725 1.00 43.18 O ANISOU 958 OE2 GLU A 123 5849 4545 6014 713 477 -412 O ATOM 959 N GLN A 124 -19.832 -0.478 -9.737 1.00 38.12 N ANISOU 959 N GLN A 124 4890 4337 5256 780 173 -40 N ATOM 960 CA GLN A 124 -19.944 -1.211 -11.004 1.00 37.65 C ANISOU 960 CA GLN A 124 4781 4352 5174 765 108 27 C ATOM 961 C GLN A 124 -21.233 -2.021 -11.096 1.00 37.91 C ANISOU 961 C GLN A 124 4728 4527 5149 763 80 77 C ATOM 962 O GLN A 124 -21.862 -2.052 -12.154 1.00 38.04 O ANISOU 962 O GLN A 124 4679 4622 5152 796 68 155 O ATOM 963 CB GLN A 124 -18.744 -2.133 -11.243 1.00 36.48 C ANISOU 963 CB GLN A 124 4672 4181 5008 671 36 -13 C ATOM 964 CG GLN A 124 -18.716 -2.705 -12.657 1.00 35.99 C ANISOU 964 CG GLN A 124 4572 4173 4930 655 -16 48 C ATOM 965 CD GLN A 124 -17.619 -3.721 -12.899 1.00 35.04 C ANISOU 965 CD GLN A 124 4490 4033 4791 567 -79 13 C ATOM 966 OE1 GLN A 124 -17.040 -4.281 -11.968 1.00 34.26 O ANISOU 966 OE1 GLN A 124 4430 3910 4678 512 -95 -46 O ATOM 967 NE2 GLN A 124 -17.345 -3.982 -14.169 1.00 34.83 N ANISOU 967 NE2 GLN A 124 4447 4024 4762 556 -111 54 N ATOM 968 N LEU A 125 -21.624 -2.665 -9.998 1.00 38.16 N ANISOU 968 N LEU A 125 4758 4600 5143 719 72 34 N ATOM 969 CA LEU A 125 -22.824 -3.515 -9.979 1.00 38.68 C ANISOU 969 CA LEU A 125 4746 4802 5149 700 47 71 C ATOM 970 C LEU A 125 -24.122 -2.766 -10.343 1.00 39.98 C ANISOU 970 C LEU A 125 4828 5045 5316 799 96 151 C ATOM 971 O LEU A 125 -25.075 -3.384 -10.815 1.00 40.49 O ANISOU 971 O LEU A 125 4810 5244 5328 786 68 203 O ATOM 972 CB LEU A 125 -22.964 -4.222 -8.625 1.00 38.46 C ANISOU 972 CB LEU A 125 4737 4791 5085 642 40 10 C ATOM 973 CG LEU A 125 -21.858 -5.228 -8.267 1.00 37.59 C ANISOU 973 CG LEU A 125 4688 4639 4957 545 -14 -48 C ATOM 974 CD1 LEU A 125 -22.021 -5.699 -6.830 1.00 37.65 C ANISOU 974 CD1 LEU A 125 4713 4662 4931 507 -7 -99 C ATOM 975 CD2 LEU A 125 -21.825 -6.417 -9.219 1.00 37.15 C ANISOU 975 CD2 LEU A 125 4609 4643 4864 477 -74 -18 C ATOM 976 N LYS A 126 -24.146 -1.448 -10.139 1.00 40.99 N ANISOU 976 N LYS A 126 4979 5093 5502 897 175 161 N ATOM 977 CA LYS A 126 -25.222 -0.588 -10.652 1.00 41.98 C ANISOU 977 CA LYS A 126 5031 5278 5642 1014 234 254 C ATOM 978 C LYS A 126 -25.331 -0.585 -12.187 1.00 42.25 C ANISOU 978 C LYS A 126 5005 5382 5668 1040 202 347 C ATOM 979 O LYS A 126 -26.426 -0.429 -12.721 1.00 43.44 O ANISOU 979 O LYS A 126 5058 5657 5791 1104 216 438 O ATOM 980 CB LYS A 126 -25.038 0.846 -10.151 1.00 42.64 C ANISOU 980 CB LYS A 126 5172 5228 5799 1112 340 241 C ATOM 981 N SER A 127 -24.206 -0.748 -12.886 1.00 41.56 N ANISOU 981 N SER A 127 4970 5224 5598 990 160 326 N ATOM 982 CA SER A 127 -24.187 -0.818 -14.359 1.00 41.54 C ANISOU 982 CA SER A 127 4916 5287 5580 1000 125 404 C ATOM 983 C SER A 127 -24.701 -2.147 -14.945 1.00 40.88 C ANISOU 983 C SER A 127 4759 5362 5411 906 43 421 C ATOM 984 O SER A 127 -24.950 -2.224 -16.153 1.00 41.27 O ANISOU 984 O SER A 127 4745 5505 5432 913 17 493 O ATOM 985 CB SER A 127 -22.772 -0.537 -14.901 1.00 41.21 C ANISOU 985 CB SER A 127 4957 5115 5587 975 112 371 C ATOM 986 OG SER A 127 -21.924 -1.680 -14.829 1.00 40.60 O ANISOU 986 OG SER A 127 4923 5023 5479 853 38 299 O ATOM 987 N GLY A 128 -24.821 -3.188 -14.116 1.00 39.72 N ANISOU 987 N GLY A 128 4625 5244 5223 814 8 355 N ATOM 988 CA GLY A 128 -25.337 -4.489 -14.556 1.00 39.00 C ANISOU 988 CA GLY A 128 4477 5290 5051 712 -55 359 C ATOM 989 C GLY A 128 -24.284 -5.480 -15.026 1.00 37.76 C ANISOU 989 C GLY A 128 4381 5086 4881 602 -113 305 C ATOM 990 O GLY A 128 -24.628 -6.592 -15.437 1.00 37.52 O ANISOU 990 O GLY A 128 4317 5152 4787 507 -155 300 O ATOM 991 N THR A 129 -23.009 -5.088 -14.961 1.00 36.67 N ANISOU 991 N THR A 129 4332 4799 4802 610 -109 265 N ATOM 992 CA THR A 129 -21.881 -5.974 -15.248 1.00 35.40 C ANISOU 992 CA THR A 129 4237 4576 4638 518 -155 212 C ATOM 993 C THR A 129 -21.038 -6.094 -13.975 1.00 34.23 C ANISOU 993 C THR A 129 4174 4312 4521 496 -146 134 C ATOM 994 O THR A 129 -21.037 -5.194 -13.133 1.00 34.55 O ANISOU 994 O THR A 129 4236 4292 4599 559 -102 118 O ATOM 995 CB THR A 129 -21.047 -5.435 -16.433 1.00 35.42 C ANISOU 995 CB THR A 129 4257 4527 4673 543 -163 242 C ATOM 996 OG1 THR A 129 -21.867 -5.399 -17.606 1.00 36.28 O ANISOU 996 OG1 THR A 129 4277 4766 4739 557 -174 318 O ATOM 997 CG2 THR A 129 -19.825 -6.314 -16.730 1.00 34.73 C ANISOU 997 CG2 THR A 129 4238 4370 4586 456 -204 189 C ATOM 998 N ALA A 130 -20.359 -7.229 -13.826 1.00 32.81 N ANISOU 998 N ALA A 130 4039 4107 4319 406 -183 88 N ATOM 999 CA ALA A 130 -19.447 -7.461 -12.716 1.00 31.68 C ANISOU 999 CA ALA A 130 3970 3872 4195 381 -182 25 C ATOM 1000 C ALA A 130 -18.089 -7.844 -13.276 1.00 30.52 C ANISOU 1000 C ALA A 130 3880 3648 4067 341 -210 5 C ATOM 1001 O ALA A 130 -17.994 -8.756 -14.098 1.00 30.30 O ANISOU 1001 O ALA A 130 3849 3651 4012 283 -238 16 O ATOM 1002 CB ALA A 130 -19.984 -8.563 -11.819 1.00 31.63 C ANISOU 1002 CB ALA A 130 3959 3917 4140 319 -190 0 C ATOM 1003 N SER A 131 -17.049 -7.136 -12.842 1.00 29.73 N ANISOU 1003 N SER A 131 3833 3452 4012 368 -198 -27 N ATOM 1004 CA SER A 131 -15.669 -7.446 -13.202 1.00 28.85 C ANISOU 1004 CA SER A 131 3774 3270 3918 335 -222 -48 C ATOM 1005 C SER A 131 -14.926 -7.864 -11.943 1.00 28.32 C ANISOU 1005 C SER A 131 3752 3165 3845 304 -225 -97 C ATOM 1006 O SER A 131 -14.893 -7.119 -10.963 1.00 28.44 O ANISOU 1006 O SER A 131 3778 3156 3872 330 -198 -128 O ATOM 1007 CB SER A 131 -14.989 -6.235 -13.831 1.00 28.89 C ANISOU 1007 CB SER A 131 3795 3205 3975 385 -205 -39 C ATOM 1008 OG SER A 131 -15.658 -5.844 -15.017 1.00 29.10 O ANISOU 1008 OG SER A 131 3775 3277 4004 421 -201 19 O ATOM 1009 N VAL A 132 -14.363 -9.070 -11.970 1.00 27.59 N ANISOU 1009 N VAL A 132 3684 3072 3729 248 -251 -101 N ATOM 1010 CA VAL A 132 -13.518 -9.580 -10.896 1.00 27.21 C ANISOU 1010 CA VAL A 132 3672 2998 3669 223 -256 -131 C ATOM 1011 C VAL A 132 -12.089 -9.540 -11.423 1.00 26.68 C ANISOU 1011 C VAL A 132 3639 2870 3626 218 -272 -135 C ATOM 1012 O VAL A 132 -11.823 -10.039 -12.514 1.00 26.23 O ANISOU 1012 O VAL A 132 3589 2803 3575 201 -285 -112 O ATOM 1013 CB VAL A 132 -13.902 -11.022 -10.500 1.00 27.19 C ANISOU 1013 CB VAL A 132 3674 3035 3624 174 -262 -122 C ATOM 1014 CG1 VAL A 132 -13.290 -11.381 -9.153 1.00 27.20 C ANISOU 1014 CG1 VAL A 132 3698 3029 3606 165 -260 -142 C ATOM 1015 CG2 VAL A 132 -15.417 -11.186 -10.452 1.00 27.62 C ANISOU 1015 CG2 VAL A 132 3684 3160 3650 168 -250 -109 C ATOM 1016 N VAL A 133 -11.180 -8.937 -10.661 1.00 26.61 N ANISOU 1016 N VAL A 133 3651 2830 3629 226 -268 -167 N ATOM 1017 CA VAL A 133 -9.805 -8.721 -11.118 1.00 26.50 C ANISOU 1017 CA VAL A 133 3663 2769 3638 222 -281 -172 C ATOM 1018 C VAL A 133 -8.841 -9.537 -10.266 1.00 26.42 C ANISOU 1018 C VAL A 133 3668 2770 3599 195 -295 -177 C ATOM 1019 O VAL A 133 -8.961 -9.553 -9.042 1.00 26.46 O ANISOU 1019 O VAL A 133 3668 2809 3575 189 -289 -198 O ATOM 1020 CB VAL A 133 -9.412 -7.225 -11.063 1.00 26.71 C ANISOU 1020 CB VAL A 133 3696 2753 3700 246 -260 -204 C ATOM 1021 CG1 VAL A 133 -7.985 -7.017 -11.566 1.00 26.56 C ANISOU 1021 CG1 VAL A 133 3700 2693 3701 233 -274 -209 C ATOM 1022 CG2 VAL A 133 -10.398 -6.391 -11.870 1.00 26.96 C ANISOU 1022 CG2 VAL A 133 3710 2773 3762 288 -237 -183 C ATOM 1023 N CYS A 134 -7.906 -10.221 -10.926 1.00 26.35 N ANISOU 1023 N CYS A 134 3675 2740 3595 185 -310 -153 N ATOM 1024 CA CYS A 134 -6.816 -10.936 -10.261 1.00 26.53 C ANISOU 1024 CA CYS A 134 3708 2777 3595 174 -320 -142 C ATOM 1025 C CYS A 134 -5.492 -10.314 -10.696 1.00 26.09 C ANISOU 1025 C CYS A 134 3657 2694 3560 176 -331 -151 C ATOM 1026 O CYS A 134 -5.235 -10.178 -11.894 1.00 25.68 O ANISOU 1026 O CYS A 134 3615 2603 3540 182 -334 -138 O ATOM 1027 CB CYS A 134 -6.834 -12.423 -10.612 1.00 26.97 C ANISOU 1027 CB CYS A 134 3781 2829 3637 164 -315 -99 C ATOM 1028 SG CYS A 134 -5.658 -13.393 -9.639 1.00 28.03 S ANISOU 1028 SG CYS A 134 3922 2989 3739 169 -314 -65 S ATOM 1029 N LEU A 135 -4.669 -9.937 -9.717 1.00 25.99 N ANISOU 1029 N LEU A 135 3635 2714 3525 167 -336 -173 N ATOM 1030 CA LEU A 135 -3.365 -9.322 -9.952 1.00 25.85 C ANISOU 1030 CA LEU A 135 3615 2689 3518 157 -346 -186 C ATOM 1031 C LEU A 135 -2.262 -10.301 -9.561 1.00 25.78 C ANISOU 1031 C LEU A 135 3594 2725 3476 158 -360 -146 C ATOM 1032 O LEU A 135 -2.249 -10.789 -8.440 1.00 25.96 O ANISOU 1032 O LEU A 135 3600 2809 3454 154 -361 -136 O ATOM 1033 CB LEU A 135 -3.236 -8.039 -9.124 1.00 26.25 C ANISOU 1033 CB LEU A 135 3658 2755 3560 134 -335 -249 C ATOM 1034 CG LEU A 135 -1.876 -7.336 -9.078 1.00 26.47 C ANISOU 1034 CG LEU A 135 3680 2795 3585 105 -341 -276 C ATOM 1035 CD1 LEU A 135 -1.442 -6.930 -10.475 1.00 26.16 C ANISOU 1035 CD1 LEU A 135 3656 2687 3597 116 -340 -264 C ATOM 1036 CD2 LEU A 135 -1.927 -6.129 -8.153 1.00 27.02 C ANISOU 1036 CD2 LEU A 135 3750 2878 3640 67 -317 -350 C ATOM 1037 N LEU A 136 -1.351 -10.577 -10.489 1.00 25.56 N ANISOU 1037 N LEU A 136 3572 2671 3470 167 -367 -117 N ATOM 1038 CA LEU A 136 -0.133 -11.345 -10.220 1.00 25.83 C ANISOU 1038 CA LEU A 136 3589 2748 3477 178 -374 -72 C ATOM 1039 C LEU A 136 1.001 -10.345 -10.294 1.00 26.22 C ANISOU 1039 C LEU A 136 3617 2820 3527 155 -388 -102 C ATOM 1040 O LEU A 136 1.321 -9.865 -11.379 1.00 25.93 O ANISOU 1040 O LEU A 136 3594 2729 3530 154 -388 -110 O ATOM 1041 CB LEU A 136 0.081 -12.440 -11.268 1.00 25.49 C ANISOU 1041 CB LEU A 136 3571 2657 3459 205 -362 -18 C ATOM 1042 CG LEU A 136 -0.748 -13.720 -11.180 1.00 25.47 C ANISOU 1042 CG LEU A 136 3593 2635 3448 219 -337 20 C ATOM 1043 CD1 LEU A 136 -2.242 -13.441 -11.217 1.00 25.32 C ANISOU 1043 CD1 LEU A 136 3587 2596 3437 200 -333 -15 C ATOM 1044 CD2 LEU A 136 -0.340 -14.645 -12.317 1.00 25.34 C ANISOU 1044 CD2 LEU A 136 3607 2561 3458 236 -314 60 C ATOM 1045 N ASN A 137 1.601 -10.021 -9.151 1.00 26.99 N ANISOU 1045 N ASN A 137 3679 3002 3575 131 -399 -120 N ATOM 1046 CA ASN A 137 2.521 -8.891 -9.075 1.00 27.61 C ANISOU 1046 CA ASN A 137 3738 3109 3646 87 -406 -169 C ATOM 1047 C ASN A 137 3.996 -9.296 -8.953 1.00 27.99 C ANISOU 1047 C ASN A 137 3741 3237 3657 87 -424 -127 C ATOM 1048 O ASN A 137 4.362 -10.093 -8.088 1.00 28.13 O ANISOU 1048 O ASN A 137 3722 3345 3621 103 -432 -80 O ATOM 1049 CB ASN A 137 2.120 -7.973 -7.912 1.00 28.34 C ANISOU 1049 CB ASN A 137 3821 3245 3702 39 -399 -240 C ATOM 1050 CG ASN A 137 2.423 -6.508 -8.188 1.00 28.87 C ANISOU 1050 CG ASN A 137 3902 3274 3793 -11 -382 -316 C ATOM 1051 OD1 ASN A 137 2.318 -6.044 -9.323 1.00 28.98 O ANISOU 1051 OD1 ASN A 137 3947 3198 3868 3 -371 -319 O ATOM 1052 ND2 ASN A 137 2.785 -5.769 -7.151 1.00 29.80 N ANISOU 1052 ND2 ASN A 137 4001 3461 3863 -72 -375 -378 N ATOM 1053 N ASN A 138 4.819 -8.738 -9.844 1.00 28.10 N ANISOU 1053 N ASN A 138 3755 3223 3700 73 -427 -137 N ATOM 1054 CA ASN A 138 6.283 -8.759 -9.747 1.00 28.65 C ANISOU 1054 CA ASN A 138 3774 3380 3734 58 -443 -113 C ATOM 1055 C ASN A 138 6.869 -10.172 -9.770 1.00 28.47 C ANISOU 1055 C ASN A 138 3724 3402 3690 122 -446 -14 C ATOM 1056 O ASN A 138 7.482 -10.626 -8.804 1.00 28.74 O ANISOU 1056 O ASN A 138 3704 3555 3661 128 -456 25 O ATOM 1057 CB ASN A 138 6.755 -7.977 -8.513 1.00 29.77 C ANISOU 1057 CB ASN A 138 3871 3634 3807 -11 -452 -169 C ATOM 1058 CG ASN A 138 6.225 -6.546 -8.485 1.00 30.31 C ANISOU 1058 CG ASN A 138 3975 3641 3899 -76 -432 -271 C ATOM 1059 OD1 ASN A 138 6.209 -5.854 -9.503 1.00 30.48 O ANISOU 1059 OD1 ASN A 138 4034 3567 3981 -82 -416 -297 O ATOM 1060 ND2 ASN A 138 5.796 -6.094 -7.310 1.00 31.14 N ANISOU 1060 ND2 ASN A 138 4073 3801 3958 -121 -424 -327 N ATOM 1061 N PHE A 139 6.687 -10.845 -10.902 1.00 27.82 N ANISOU 1061 N PHE A 139 3681 3227 3662 170 -430 27 N ATOM 1062 CA PHE A 139 7.147 -12.224 -11.069 1.00 27.95 C ANISOU 1062 CA PHE A 139 3692 3256 3674 237 -414 120 C ATOM 1063 C PHE A 139 8.098 -12.360 -12.252 1.00 27.97 C ANISOU 1063 C PHE A 139 3694 3224 3709 259 -407 150 C ATOM 1064 O PHE A 139 8.147 -11.499 -13.132 1.00 27.49 O ANISOU 1064 O PHE A 139 3653 3107 3686 227 -413 102 O ATOM 1065 CB PHE A 139 5.958 -13.189 -11.202 1.00 27.39 C ANISOU 1065 CB PHE A 139 3673 3105 3627 272 -387 144 C ATOM 1066 CG PHE A 139 5.078 -12.928 -12.396 1.00 26.67 C ANISOU 1066 CG PHE A 139 3641 2897 3596 260 -377 104 C ATOM 1067 CD1 PHE A 139 4.029 -12.013 -12.326 1.00 26.33 C ANISOU 1067 CD1 PHE A 139 3616 2821 3567 222 -387 37 C ATOM 1068 CD2 PHE A 139 5.289 -13.607 -13.587 1.00 26.32 C ANISOU 1068 CD2 PHE A 139 3630 2782 3591 289 -354 138 C ATOM 1069 CE1 PHE A 139 3.219 -11.773 -13.425 1.00 25.82 C ANISOU 1069 CE1 PHE A 139 3593 2669 3550 217 -378 13 C ATOM 1070 CE2 PHE A 139 4.482 -13.374 -14.689 1.00 25.89 C ANISOU 1070 CE2 PHE A 139 3619 2639 3579 272 -347 104 C ATOM 1071 CZ PHE A 139 3.445 -12.454 -14.610 1.00 25.65 C ANISOU 1071 CZ PHE A 139 3598 2590 3558 238 -362 46 C ATOM 1072 N TYR A 140 8.861 -13.448 -12.243 1.00 28.56 N ANISOU 1072 N TYR A 140 3747 3334 3769 319 -388 237 N ATOM 1073 CA TYR A 140 9.781 -13.775 -13.328 1.00 28.77 C ANISOU 1073 CA TYR A 140 3775 3330 3826 352 -371 277 C ATOM 1074 C TYR A 140 10.054 -15.293 -13.316 1.00 29.35 C ANISOU 1074 C TYR A 140 3858 3394 3899 436 -324 376 C ATOM 1075 O TYR A 140 10.258 -15.840 -12.238 1.00 29.64 O ANISOU 1075 O TYR A 140 3855 3517 3888 469 -319 432 O ATOM 1076 CB TYR A 140 11.091 -12.999 -13.166 1.00 29.15 C ANISOU 1076 CB TYR A 140 3752 3484 3839 324 -399 273 C ATOM 1077 CG TYR A 140 12.008 -13.186 -14.342 1.00 29.17 C ANISOU 1077 CG TYR A 140 3754 3454 3874 352 -383 306 C ATOM 1078 CD1 TYR A 140 12.913 -14.247 -14.379 1.00 29.67 C ANISOU 1078 CD1 TYR A 140 3786 3561 3924 428 -354 404 C ATOM 1079 CD2 TYR A 140 11.940 -12.335 -15.450 1.00 28.78 C ANISOU 1079 CD2 TYR A 140 3739 3325 3872 311 -390 247 C ATOM 1080 CE1 TYR A 140 13.741 -14.445 -15.469 1.00 29.76 C ANISOU 1080 CE1 TYR A 140 3800 3540 3967 458 -333 434 C ATOM 1081 CE2 TYR A 140 12.767 -12.528 -16.548 1.00 28.79 C ANISOU 1081 CE2 TYR A 140 3740 3296 3901 336 -373 277 C ATOM 1082 CZ TYR A 140 13.664 -13.585 -16.549 1.00 29.28 C ANISOU 1082 CZ TYR A 140 3772 3404 3949 408 -345 367 C ATOM 1083 OH TYR A 140 14.490 -13.795 -17.622 1.00 29.47 O ANISOU 1083 OH TYR A 140 3796 3400 4000 436 -323 397 O ATOM 1084 N PRO A 141 10.080 -15.980 -14.466 1.00 29.68 N ANISOU 1084 N PRO A 141 3952 3335 3990 471 -283 401 N ATOM 1085 CA PRO A 141 9.907 -15.416 -15.812 1.00 29.55 C ANISOU 1085 CA PRO A 141 3978 3228 4024 437 -286 345 C ATOM 1086 C PRO A 141 8.449 -15.081 -16.167 1.00 29.55 C ANISOU 1086 C PRO A 141 4035 3141 4051 391 -292 276 C ATOM 1087 O PRO A 141 7.554 -15.225 -15.334 1.00 29.30 O ANISOU 1087 O PRO A 141 4012 3118 4001 381 -295 264 O ATOM 1088 CB PRO A 141 10.467 -16.522 -16.723 1.00 29.64 C ANISOU 1088 CB PRO A 141 4021 3178 4064 497 -228 407 C ATOM 1089 CG PRO A 141 10.260 -17.783 -15.957 1.00 30.02 C ANISOU 1089 CG PRO A 141 4082 3227 4096 555 -181 478 C ATOM 1090 CD PRO A 141 10.400 -17.420 -14.506 1.00 30.34 C ANISOU 1090 CD PRO A 141 4055 3393 4080 552 -220 494 C ATOM 1091 N ARG A 142 8.241 -14.628 -17.400 1.00 29.89 N ANISOU 1091 N ARG A 142 4111 3112 4133 365 -293 237 N ATOM 1092 CA ARG A 142 6.940 -14.157 -17.884 1.00 30.23 C ANISOU 1092 CA ARG A 142 4196 3091 4199 323 -301 178 C ATOM 1093 C ARG A 142 5.830 -15.215 -17.885 1.00 30.21 C ANISOU 1093 C ARG A 142 4243 3036 4199 330 -267 187 C ATOM 1094 O ARG A 142 4.661 -14.872 -17.754 1.00 29.89 O ANISOU 1094 O ARG A 142 4217 2981 4159 298 -279 147 O ATOM 1095 CB ARG A 142 7.103 -13.592 -19.303 1.00 30.58 C ANISOU 1095 CB ARG A 142 4259 3083 4278 304 -304 152 C ATOM 1096 CG ARG A 142 5.941 -12.753 -19.811 1.00 30.87 C ANISOU 1096 CG ARG A 142 4317 3080 4333 264 -321 99 C ATOM 1097 CD ARG A 142 6.362 -12.008 -21.073 1.00 31.34 C ANISOU 1097 CD ARG A 142 4379 3108 4419 249 -328 84 C ATOM 1098 NE ARG A 142 5.330 -11.107 -21.578 1.00 31.67 N ANISOU 1098 NE ARG A 142 4434 3121 4478 222 -341 47 N ATOM 1099 CZ ARG A 142 4.263 -11.473 -22.290 1.00 32.06 C ANISOU 1099 CZ ARG A 142 4510 3140 4531 212 -330 43 C ATOM 1100 NH1 ARG A 142 4.038 -12.751 -22.602 1.00 32.46 N ANISOU 1100 NH1 ARG A 142 4590 3172 4571 216 -301 61 N ATOM 1101 NH2 ARG A 142 3.399 -10.544 -22.695 1.00 32.15 N ANISOU 1101 NH2 ARG A 142 4520 3143 4554 198 -343 21 N ATOM 1102 N GLU A 143 6.200 -16.486 -18.017 1.00 30.75 N ANISOU 1102 N GLU A 143 4337 3077 4269 370 -216 241 N ATOM 1103 CA GLU A 143 5.236 -17.569 -18.210 1.00 31.13 C ANISOU 1103 CA GLU A 143 4443 3060 4323 365 -168 245 C ATOM 1104 C GLU A 143 4.469 -17.840 -16.917 1.00 31.11 C ANISOU 1104 C GLU A 143 4434 3092 4293 365 -171 251 C ATOM 1105 O GLU A 143 5.065 -18.203 -15.903 1.00 31.40 O ANISOU 1105 O GLU A 143 4441 3182 4306 407 -165 303 O ATOM 1106 CB GLU A 143 5.931 -18.856 -18.687 1.00 32.05 C ANISOU 1106 CB GLU A 143 4599 3125 4453 410 -96 301 C ATOM 1107 CG GLU A 143 6.432 -18.816 -20.134 1.00 32.32 C ANISOU 1107 CG GLU A 143 4658 3108 4515 401 -78 286 C ATOM 1108 CD GLU A 143 7.595 -17.854 -20.363 1.00 32.62 C ANISOU 1108 CD GLU A 143 4639 3199 4556 416 -121 292 C ATOM 1109 OE1 GLU A 143 8.498 -17.764 -19.497 1.00 32.93 O ANISOU 1109 OE1 GLU A 143 4627 3309 4577 457 -134 338 O ATOM 1110 OE2 GLU A 143 7.605 -17.177 -21.415 1.00 32.87 O ANISOU 1110 OE2 GLU A 143 4675 3209 4604 382 -140 253 O ATOM 1111 N ALA A 144 3.154 -17.641 -16.969 1.00 30.67 N ANISOU 1111 N ALA A 144 4400 3017 4238 320 -182 204 N ATOM 1112 CA ALA A 144 2.264 -17.839 -15.826 1.00 30.67 C ANISOU 1112 CA ALA A 144 4395 3046 4212 312 -185 202 C ATOM 1113 C ALA A 144 0.870 -18.242 -16.309 1.00 30.42 C ANISOU 1113 C ALA A 144 4407 2967 4184 265 -164 166 C ATOM 1114 O ALA A 144 0.452 -17.857 -17.405 1.00 30.27 O ANISOU 1114 O ALA A 144 4400 2921 4181 230 -172 128 O ATOM 1115 CB ALA A 144 2.188 -16.566 -14.998 1.00 30.58 C ANISOU 1115 CB ALA A 144 4331 3106 4182 299 -244 168 C ATOM 1116 N LYS A 145 0.164 -19.016 -15.490 1.00 30.47 N ANISOU 1116 N LYS A 145 4431 2974 4172 262 -136 181 N ATOM 1117 CA LYS A 145 -1.185 -19.488 -15.805 1.00 30.36 C ANISOU 1117 CA LYS A 145 4452 2930 4152 209 -112 149 C ATOM 1118 C LYS A 145 -2.155 -18.969 -14.749 1.00 29.61 C ANISOU 1118 C LYS A 145 4325 2892 4032 195 -146 128 C ATOM 1119 O LYS A 145 -1.937 -19.182 -13.556 1.00 29.45 O ANISOU 1119 O LYS A 145 4290 2908 3993 225 -144 160 O ATOM 1120 CB LYS A 145 -1.210 -21.017 -15.823 1.00 31.44 C ANISOU 1120 CB LYS A 145 4651 3004 4291 211 -31 185 C ATOM 1121 CG LYS A 145 -2.444 -21.638 -16.462 1.00 32.13 C ANISOU 1121 CG LYS A 145 4784 3053 4372 138 7 144 C ATOM 1122 CD LYS A 145 -2.508 -23.133 -16.169 1.00 33.13 C ANISOU 1122 CD LYS A 145 4977 3113 4499 137 98 178 C ATOM 1123 CE LYS A 145 -3.380 -23.878 -17.170 1.00 33.73 C ANISOU 1123 CE LYS A 145 5111 3134 4570 51 154 131 C ATOM 1124 NZ LYS A 145 -4.793 -23.409 -17.158 1.00 33.88 N ANISOU 1124 NZ LYS A 145 5101 3212 4559 -20 113 78 N ATOM 1125 N VAL A 146 -3.200 -18.271 -15.192 1.00 28.56 N ANISOU 1125 N VAL A 146 4179 2775 3898 153 -174 79 N ATOM 1126 CA VAL A 146 -4.309 -17.870 -14.332 1.00 28.16 C ANISOU 1126 CA VAL A 146 4102 2772 3825 136 -194 57 C ATOM 1127 C VAL A 146 -5.504 -18.754 -14.670 1.00 27.87 C ANISOU 1127 C VAL A 146 4096 2719 3774 83 -157 45 C ATOM 1128 O VAL A 146 -5.871 -18.890 -15.838 1.00 27.75 O ANISOU 1128 O VAL A 146 4096 2684 3763 43 -147 24 O ATOM 1129 CB VAL A 146 -4.684 -16.386 -14.536 1.00 27.94 C ANISOU 1129 CB VAL A 146 4031 2779 3806 134 -244 18 C ATOM 1130 CG1 VAL A 146 -5.944 -16.025 -13.752 1.00 28.01 C ANISOU 1130 CG1 VAL A 146 4016 2834 3793 119 -255 -4 C ATOM 1131 CG2 VAL A 146 -3.519 -15.490 -14.129 1.00 27.88 C ANISOU 1131 CG2 VAL A 146 3997 2787 3808 170 -274 20 C ATOM 1132 N GLN A 147 -6.102 -19.348 -13.644 1.00 27.59 N ANISOU 1132 N GLN A 147 4067 2701 3716 77 -137 57 N ATOM 1133 CA GLN A 147 -7.296 -20.165 -13.799 1.00 27.61 C ANISOU 1133 CA GLN A 147 4094 2698 3699 17 -99 42 C ATOM 1134 C GLN A 147 -8.360 -19.621 -12.857 1.00 27.16 C ANISOU 1134 C GLN A 147 3995 2708 3616 10 -127 25 C ATOM 1135 O GLN A 147 -8.174 -19.634 -11.643 1.00 27.11 O ANISOU 1135 O GLN A 147 3978 2724 3598 42 -131 46 O ATOM 1136 CB GLN A 147 -6.973 -21.633 -13.482 1.00 28.19 C ANISOU 1136 CB GLN A 147 4229 2712 3771 15 -26 80 C ATOM 1137 CG GLN A 147 -8.148 -22.600 -13.573 1.00 28.80 C ANISOU 1137 CG GLN A 147 4343 2774 3826 -59 26 61 C ATOM 1138 CD GLN A 147 -8.764 -22.652 -14.964 1.00 29.02 C ANISOU 1138 CD GLN A 147 4381 2797 3848 -134 34 13 C ATOM 1139 OE1 GLN A 147 -8.193 -23.242 -15.884 1.00 29.39 O ANISOU 1139 OE1 GLN A 147 4475 2780 3909 -152 77 10 O ATOM 1140 NE2 GLN A 147 -9.937 -22.037 -15.123 1.00 28.91 N ANISOU 1140 NE2 GLN A 147 4319 2858 3808 -179 -4 -23 N ATOM 1141 N TRP A 148 -9.461 -19.128 -13.422 1.00 26.76 N ANISOU 1141 N TRP A 148 3916 2697 3554 -31 -146 -10 N ATOM 1142 CA TRP A 148 -10.595 -18.647 -12.629 1.00 26.61 C ANISOU 1142 CA TRP A 148 3855 2743 3511 -38 -165 -24 C ATOM 1143 C TRP A 148 -11.508 -19.808 -12.232 1.00 26.99 C ANISOU 1143 C TRP A 148 3928 2798 3529 -93 -119 -22 C ATOM 1144 O TRP A 148 -11.704 -20.747 -13.013 1.00 26.87 O ANISOU 1144 O TRP A 148 3953 2750 3508 -151 -78 -29 O ATOM 1145 CB TRP A 148 -11.401 -17.609 -13.405 1.00 26.35 C ANISOU 1145 CB TRP A 148 3773 2760 3477 -47 -199 -50 C ATOM 1146 CG TRP A 148 -10.744 -16.273 -13.487 1.00 25.94 C ANISOU 1146 CG TRP A 148 3694 2708 3455 10 -238 -54 C ATOM 1147 CD1 TRP A 148 -10.014 -15.782 -14.526 1.00 25.67 C ANISOU 1147 CD1 TRP A 148 3663 2644 3447 23 -252 -53 C ATOM 1148 CD2 TRP A 148 -10.767 -15.247 -12.489 1.00 25.80 C ANISOU 1148 CD2 TRP A 148 3645 2715 3442 54 -259 -63 C ATOM 1149 NE1 TRP A 148 -9.580 -14.509 -14.241 1.00 25.48 N ANISOU 1149 NE1 TRP A 148 3613 2621 3446 72 -279 -60 N ATOM 1150 CE2 TRP A 148 -10.029 -14.155 -12.996 1.00 25.57 C ANISOU 1150 CE2 TRP A 148 3606 2664 3444 89 -281 -70 C ATOM 1151 CE3 TRP A 148 -11.346 -15.141 -11.218 1.00 25.98 C ANISOU 1151 CE3 TRP A 148 3651 2777 3443 62 -256 -70 C ATOM 1152 CZ2 TRP A 148 -9.848 -12.967 -12.272 1.00 25.57 C ANISOU 1152 CZ2 TRP A 148 3586 2673 3457 127 -295 -88 C ATOM 1153 CZ3 TRP A 148 -11.169 -13.958 -10.497 1.00 25.94 C ANISOU 1153 CZ3 TRP A 148 3623 2787 3448 102 -272 -89 C ATOM 1154 CH2 TRP A 148 -10.424 -12.887 -11.030 1.00 25.73 C ANISOU 1154 CH2 TRP A 148 3592 2730 3454 131 -288 -101 C ATOM 1155 N LYS A 149 -12.057 -19.729 -11.020 1.00 27.11 N ANISOU 1155 N LYS A 149 3923 2855 3524 -82 -123 -17 N ATOM 1156 CA LYS A 149 -13.057 -20.681 -10.539 1.00 27.69 C ANISOU 1156 CA LYS A 149 4011 2945 3566 -136 -82 -17 C ATOM 1157 C LYS A 149 -14.218 -19.942 -9.889 1.00 27.77 C ANISOU 1157 C LYS A 149 3962 3040 3551 -137 -110 -35 C ATOM 1158 O LYS A 149 -14.006 -18.995 -9.128 1.00 27.41 O ANISOU 1158 O LYS A 149 3883 3023 3510 -82 -143 -36 O ATOM 1159 CB LYS A 149 -12.450 -21.657 -9.535 1.00 28.07 C ANISOU 1159 CB LYS A 149 4104 2950 3611 -114 -39 25 C ATOM 1160 CG LYS A 149 -11.278 -22.451 -10.076 1.00 28.15 C ANISOU 1160 CG LYS A 149 4174 2874 3649 -99 1 55 C ATOM 1161 CD LYS A 149 -10.758 -23.437 -9.048 1.00 28.59 C ANISOU 1161 CD LYS A 149 4269 2894 3699 -67 52 111 C ATOM 1162 CE LYS A 149 -9.479 -24.090 -9.541 1.00 28.73 C ANISOU 1162 CE LYS A 149 4338 2832 3748 -29 93 152 C ATOM 1163 NZ LYS A 149 -8.979 -25.118 -8.594 1.00 29.36 N ANISOU 1163 NZ LYS A 149 4455 2877 3824 12 154 222 N ATOM 1164 N VAL A 150 -15.436 -20.379 -10.202 1.00 28.21 N ANISOU 1164 N VAL A 150 4003 3138 3576 -205 -91 -52 N ATOM 1165 CA VAL A 150 -16.657 -19.857 -9.590 1.00 28.60 C ANISOU 1165 CA VAL A 150 3995 3276 3597 -211 -107 -64 C ATOM 1166 C VAL A 150 -17.409 -21.036 -8.976 1.00 29.31 C ANISOU 1166 C VAL A 150 4109 3375 3653 -275 -58 -60 C ATOM 1167 O VAL A 150 -17.810 -21.953 -9.696 1.00 29.53 O ANISOU 1167 O VAL A 150 4165 3391 3663 -356 -20 -71 O ATOM 1168 CB VAL A 150 -17.539 -19.125 -10.620 1.00 28.58 C ANISOU 1168 CB VAL A 150 3933 3344 3583 -232 -133 -82 C ATOM 1169 CG1 VAL A 150 -18.805 -18.586 -9.962 1.00 28.88 C ANISOU 1169 CG1 VAL A 150 3904 3476 3591 -227 -143 -86 C ATOM 1170 CG2 VAL A 150 -16.746 -17.998 -11.271 1.00 28.14 C ANISOU 1170 CG2 VAL A 150 3862 3266 3565 -168 -171 -80 C ATOM 1171 N ASP A 151 -17.584 -21.006 -7.652 1.00 29.90 N ANISOU 1171 N ASP A 151 4175 3471 3714 -245 -55 -46 N ATOM 1172 CA ASP A 151 -18.083 -22.155 -6.870 1.00 30.79 C ANISOU 1172 CA ASP A 151 4321 3580 3799 -294 -4 -31 C ATOM 1173 C ASP A 151 -17.333 -23.444 -7.233 1.00 31.36 C ANISOU 1173 C ASP A 151 4477 3554 3886 -325 56 -10 C ATOM 1174 O ASP A 151 -17.943 -24.481 -7.497 1.00 31.99 O ANISOU 1174 O ASP A 151 4593 3616 3947 -408 112 -18 O ATOM 1175 CB ASP A 151 -19.606 -22.320 -7.042 1.00 31.21 C ANISOU 1175 CB ASP A 151 4331 3716 3810 -370 7 -56 C ATOM 1176 CG ASP A 151 -20.405 -21.146 -6.470 1.00 31.24 C ANISOU 1176 CG ASP A 151 4254 3816 3799 -326 -36 -66 C ATOM 1177 OD1 ASP A 151 -19.887 -20.396 -5.614 1.00 30.97 O ANISOU 1177 OD1 ASP A 151 4208 3779 3780 -250 -60 -58 O ATOM 1178 OD2 ASP A 151 -21.576 -20.976 -6.868 1.00 31.64 O ANISOU 1178 OD2 ASP A 151 4250 3951 3820 -371 -40 -81 O ATOM 1179 N ASN A 152 -16.003 -23.342 -7.277 1.00 31.53 N ANISOU 1179 N ASN A 152 4528 3512 3941 -261 48 16 N ATOM 1180 CA ASN A 152 -15.096 -24.446 -7.649 1.00 32.28 C ANISOU 1180 CA ASN A 152 4702 3505 4059 -266 108 46 C ATOM 1181 C ASN A 152 -15.261 -25.045 -9.066 1.00 32.40 C ANISOU 1181 C ASN A 152 4757 3471 4080 -344 146 13 C ATOM 1182 O ASN A 152 -14.713 -26.111 -9.349 1.00 32.98 O ANISOU 1182 O ASN A 152 4907 3453 4171 -362 216 32 O ATOM 1183 CB ASN A 152 -15.126 -25.545 -6.569 1.00 33.28 C ANISOU 1183 CB ASN A 152 4874 3599 4171 -267 173 92 C ATOM 1184 CG ASN A 152 -14.465 -25.099 -5.284 1.00 33.58 C ANISOU 1184 CG ASN A 152 4884 3672 4204 -178 142 138 C ATOM 1185 OD1 ASN A 152 -13.241 -24.965 -5.224 1.00 33.95 O ANISOU 1185 OD1 ASN A 152 4939 3689 4271 -110 131 173 O ATOM 1186 ND2 ASN A 152 -15.266 -24.852 -4.252 1.00 33.98 N ANISOU 1186 ND2 ASN A 152 4895 3795 4220 -182 127 135 N ATOM 1187 N ALA A 153 -15.979 -24.354 -9.954 1.00 32.04 N ANISOU 1187 N ALA A 153 4662 3491 4021 -387 104 -32 N ATOM 1188 CA ALA A 153 -16.102 -24.763 -11.353 1.00 32.07 C ANISOU 1188 CA ALA A 153 4692 3472 4022 -464 130 -67 C ATOM 1189 C ALA A 153 -15.108 -23.940 -12.158 1.00 31.18 C ANISOU 1189 C ALA A 153 4566 3338 3943 -404 83 -66 C ATOM 1190 O ALA A 153 -15.131 -22.708 -12.090 1.00 30.66 O ANISOU 1190 O ALA A 153 4435 3333 3883 -348 15 -67 O ATOM 1191 CB ALA A 153 -17.518 -24.527 -11.859 1.00 32.35 C ANISOU 1191 CB ALA A 153 4669 3613 4010 -549 112 -109 C ATOM 1192 N LEU A 154 -14.234 -24.618 -12.903 1.00 31.01 N ANISOU 1192 N LEU A 154 4610 3228 3945 -414 128 -63 N ATOM 1193 CA LEU A 154 -13.240 -23.935 -13.741 1.00 30.33 C ANISOU 1193 CA LEU A 154 4516 3118 3890 -364 91 -62 C ATOM 1194 C LEU A 154 -13.927 -23.150 -14.849 1.00 29.95 C ANISOU 1194 C LEU A 154 4410 3149 3820 -408 44 -100 C ATOM 1195 O LEU A 154 -14.820 -23.663 -15.521 1.00 30.18 O ANISOU 1195 O LEU A 154 4441 3215 3811 -506 71 -136 O ATOM 1196 CB LEU A 154 -12.231 -24.917 -14.355 1.00 30.63 C ANISOU 1196 CB LEU A 154 4638 3044 3955 -370 160 -51 C ATOM 1197 CG LEU A 154 -10.999 -25.219 -13.502 1.00 30.65 C ANISOU 1197 CG LEU A 154 4676 2976 3993 -275 182 9 C ATOM 1198 CD1 LEU A 154 -11.401 -25.881 -12.190 1.00 31.14 C ANISOU 1198 CD1 LEU A 154 4755 3035 4041 -268 221 43 C ATOM 1199 CD2 LEU A 154 -10.019 -26.090 -14.279 1.00 30.93 C ANISOU 1199 CD2 LEU A 154 4789 2906 4058 -274 253 22 C ATOM 1200 N GLN A 155 -13.504 -21.903 -15.017 1.00 29.30 N ANISOU 1200 N GLN A 155 4276 3098 3758 -337 -23 -91 N ATOM 1201 CA GLN A 155 -14.044 -21.026 -16.043 1.00 29.24 C ANISOU 1201 CA GLN A 155 4208 3166 3735 -355 -68 -111 C ATOM 1202 C GLN A 155 -13.200 -21.116 -17.305 1.00 29.17 C ANISOU 1202 C GLN A 155 4230 3111 3742 -366 -60 -119 C ATOM 1203 O GLN A 155 -12.004 -21.416 -17.247 1.00 28.96 O ANISOU 1203 O GLN A 155 4256 2996 3753 -324 -40 -103 O ATOM 1204 CB GLN A 155 -14.066 -19.579 -15.542 1.00 28.76 C ANISOU 1204 CB GLN A 155 4082 3154 3692 -269 -131 -94 C ATOM 1205 CG GLN A 155 -14.869 -19.371 -14.267 1.00 28.85 C ANISOU 1205 CG GLN A 155 4060 3214 3687 -251 -138 -89 C ATOM 1206 CD GLN A 155 -16.335 -19.726 -14.447 1.00 29.35 C ANISOU 1206 CD GLN A 155 4085 3366 3699 -328 -126 -105 C ATOM 1207 OE1 GLN A 155 -17.049 -19.080 -15.211 1.00 29.38 O ANISOU 1207 OE1 GLN A 155 4028 3453 3683 -341 -153 -109 O ATOM 1208 NE2 GLN A 155 -16.783 -20.764 -13.756 1.00 29.72 N ANISOU 1208 NE2 GLN A 155 4165 3404 3724 -381 -82 -110 N ATOM 1209 N SER A 156 -13.833 -20.854 -18.441 1.00 29.34 N ANISOU 1209 N SER A 156 4214 3202 3732 -422 -76 -141 N ATOM 1210 CA SER A 156 -13.131 -20.780 -19.717 1.00 29.36 C ANISOU 1210 CA SER A 156 4233 3179 3742 -435 -76 -150 C ATOM 1211 C SER A 156 -13.891 -19.885 -20.683 1.00 29.37 C ANISOU 1211 C SER A 156 4155 3295 3710 -453 -123 -152 C ATOM 1212 O SER A 156 -15.112 -19.986 -20.797 1.00 30.00 O ANISOU 1212 O SER A 156 4187 3475 3737 -516 -126 -164 O ATOM 1213 CB SER A 156 -12.965 -22.177 -20.315 1.00 29.92 C ANISOU 1213 CB SER A 156 4382 3189 3796 -528 0 -183 C ATOM 1214 OG SER A 156 -12.082 -22.141 -21.422 1.00 30.04 O ANISOU 1214 OG SER A 156 4424 3163 3826 -528 6 -190 O ATOM 1215 N GLY A 157 -13.164 -19.000 -21.362 1.00 28.87 N ANISOU 1215 N GLY A 157 4073 3222 3674 -396 -158 -134 N ATOM 1216 CA GLY A 157 -13.744 -18.131 -22.383 1.00 28.85 C ANISOU 1216 CA GLY A 157 3997 3322 3641 -401 -198 -123 C ATOM 1217 C GLY A 157 -14.422 -16.858 -21.897 1.00 28.62 C ANISOU 1217 C GLY A 157 3889 3367 3619 -325 -244 -87 C ATOM 1218 O GLY A 157 -15.002 -16.144 -22.710 1.00 29.10 O ANISOU 1218 O GLY A 157 3882 3522 3653 -321 -270 -64 O ATOM 1219 N ASN A 158 -14.346 -16.561 -20.595 1.00 28.04 N ANISOU 1219 N ASN A 158 3822 3253 3579 -264 -248 -78 N ATOM 1220 CA ASN A 158 -14.972 -15.353 -20.019 1.00 27.81 C ANISOU 1220 CA ASN A 158 3728 3278 3561 -189 -277 -49 C ATOM 1221 C ASN A 158 -13.981 -14.478 -19.234 1.00 27.24 C ANISOU 1221 C ASN A 158 3680 3119 3552 -95 -290 -40 C ATOM 1222 O ASN A 158 -14.383 -13.708 -18.353 1.00 27.14 O ANISOU 1222 O ASN A 158 3638 3121 3553 -40 -297 -31 O ATOM 1223 CB ASN A 158 -16.183 -15.733 -19.149 1.00 28.12 C ANISOU 1223 CB ASN A 158 3736 3386 3563 -220 -267 -55 C ATOM 1224 CG ASN A 158 -15.828 -16.677 -18.013 1.00 27.98 C ANISOU 1224 CG ASN A 158 3782 3292 3555 -239 -237 -78 C ATOM 1225 OD1 ASN A 158 -14.715 -17.197 -17.938 1.00 27.68 O ANISOU 1225 OD1 ASN A 158 3811 3158 3548 -235 -221 -86 O ATOM 1226 ND2 ASN A 158 -16.785 -16.914 -17.130 1.00 28.29 N ANISOU 1226 ND2 ASN A 158 3797 3383 3568 -256 -228 -81 N ATOM 1227 N SER A 159 -12.692 -14.600 -19.560 1.00 26.83 N ANISOU 1227 N SER A 159 3679 2983 3534 -83 -288 -45 N ATOM 1228 CA SER A 159 -11.649 -13.767 -18.972 1.00 26.46 C ANISOU 1228 CA SER A 159 3650 2865 3538 -9 -300 -40 C ATOM 1229 C SER A 159 -10.681 -13.254 -20.033 1.00 26.41 C ANISOU 1229 C SER A 159 3654 2821 3560 11 -311 -30 C ATOM 1230 O SER A 159 -10.554 -13.832 -21.115 1.00 26.26 O ANISOU 1230 O SER A 159 3646 2809 3522 -36 -305 -32 O ATOM 1231 CB SER A 159 -10.883 -14.531 -17.889 1.00 26.23 C ANISOU 1231 CB SER A 159 3673 2773 3521 -9 -284 -53 C ATOM 1232 OG SER A 159 -10.145 -15.605 -18.435 1.00 26.09 O ANISOU 1232 OG SER A 159 3705 2706 3502 -48 -260 -57 O ATOM 1233 N GLN A 160 -10.015 -12.154 -19.704 1.00 26.43 N ANISOU 1233 N GLN A 160 3654 2784 3604 74 -324 -24 N ATOM 1234 CA GLN A 160 -8.973 -11.567 -20.539 1.00 26.65 C ANISOU 1234 CA GLN A 160 3694 2767 3664 97 -332 -15 C ATOM 1235 C GLN A 160 -7.857 -11.086 -19.630 1.00 26.66 C ANISOU 1235 C GLN A 160 3721 2705 3702 135 -334 -28 C ATOM 1236 O GLN A 160 -8.117 -10.665 -18.497 1.00 26.59 O ANISOU 1236 O GLN A 160 3705 2699 3698 158 -332 -40 O ATOM 1237 CB GLN A 160 -9.517 -10.383 -21.344 1.00 27.01 C ANISOU 1237 CB GLN A 160 3694 2851 3718 133 -341 14 C ATOM 1238 CG GLN A 160 -10.533 -10.761 -22.411 1.00 27.47 C ANISOU 1238 CG GLN A 160 3711 2996 3728 94 -344 35 C ATOM 1239 CD GLN A 160 -10.916 -9.583 -23.285 1.00 27.90 C ANISOU 1239 CD GLN A 160 3717 3093 3791 141 -350 79 C ATOM 1240 OE1 GLN A 160 -10.611 -9.554 -24.478 1.00 28.23 O ANISOU 1240 OE1 GLN A 160 3752 3151 3823 127 -357 98 O ATOM 1241 NE2 GLN A 160 -11.570 -8.599 -22.693 1.00 28.11 N ANISOU 1241 NE2 GLN A 160 3711 3134 3836 202 -342 100 N ATOM 1242 N GLU A 161 -6.623 -11.151 -20.123 1.00 26.76 N ANISOU 1242 N GLU A 161 3761 2670 3736 137 -337 -27 N ATOM 1243 CA GLU A 161 -5.472 -10.700 -19.351 1.00 27.01 C ANISOU 1243 CA GLU A 161 3809 2659 3794 163 -340 -38 C ATOM 1244 C GLU A 161 -4.525 -9.835 -20.158 1.00 26.98 C ANISOU 1244 C GLU A 161 3808 2621 3823 181 -347 -32 C ATOM 1245 O GLU A 161 -4.609 -9.768 -21.388 1.00 26.83 O ANISOU 1245 O GLU A 161 3784 2604 3806 174 -348 -15 O ATOM 1246 CB GLU A 161 -4.712 -11.896 -18.767 1.00 27.18 C ANISOU 1246 CB GLU A 161 3861 2664 3803 147 -331 -38 C ATOM 1247 CG GLU A 161 -4.108 -12.842 -19.794 1.00 27.45 C ANISOU 1247 CG GLU A 161 3923 2672 3835 125 -317 -24 C ATOM 1248 CD GLU A 161 -3.371 -14.011 -19.159 1.00 27.91 C ANISOU 1248 CD GLU A 161 4013 2707 3885 126 -295 -13 C ATOM 1249 OE1 GLU A 161 -2.341 -14.435 -19.725 1.00 28.36 O ANISOU 1249 OE1 GLU A 161 4090 2730 3954 132 -282 1 O ATOM 1250 OE2 GLU A 161 -3.807 -14.509 -18.095 1.00 28.31 O ANISOU 1250 OE2 GLU A 161 4066 2774 3918 125 -286 -12 O ATOM 1251 N ASER A 162 -3.617 -9.185 -19.433 0.50 27.02 N ANISOU 1251 N ASER A 162 3818 2600 3848 197 -349 -48 N ATOM 1252 N BSER A 162 -3.630 -9.153 -19.457 0.50 26.89 N ANISOU 1252 N BSER A 162 3802 2584 3832 197 -349 -48 N ATOM 1253 CA ASER A 162 -2.601 -8.316 -20.002 0.50 27.19 C ANISOU 1253 CA ASER A 162 3844 2586 3900 207 -351 -49 C ATOM 1254 CA BSER A 162 -2.535 -8.448 -20.098 0.50 26.94 C ANISOU 1254 CA BSER A 162 3814 2555 3868 205 -352 -47 C ATOM 1255 C ASER A 162 -1.375 -8.370 -19.100 0.50 27.32 C ANISOU 1255 C ASER A 162 3868 2598 3916 201 -355 -67 C ATOM 1256 C BSER A 162 -1.379 -8.354 -19.123 0.50 27.20 C ANISOU 1256 C BSER A 162 3852 2582 3901 201 -355 -66 C ATOM 1257 O ASER A 162 -1.516 -8.560 -17.892 0.50 27.31 O ANISOU 1257 O ASER A 162 3861 2621 3895 197 -356 -83 O ATOM 1258 O BSER A 162 -1.570 -8.415 -17.908 0.50 27.25 O ANISOU 1258 O BSER A 162 3852 2611 3889 198 -355 -85 O ATOM 1259 CB ASER A 162 -3.129 -6.887 -20.076 0.50 27.40 C ANISOU 1259 CB ASER A 162 3858 2597 3954 232 -338 -54 C ATOM 1260 CB BSER A 162 -2.969 -7.063 -20.580 0.50 26.99 C ANISOU 1260 CB BSER A 162 3808 2544 3902 229 -342 -44 C ATOM 1261 OG ASER A 162 -2.500 -6.177 -21.119 0.50 27.57 O ANISOU 1261 OG ASER A 162 3885 2586 4004 240 -334 -40 O ATOM 1262 OG BSER A 162 -3.274 -6.212 -19.498 0.50 26.97 O ANISOU 1262 OG BSER A 162 3803 2534 3909 242 -328 -71 O ATOM 1263 N VAL A 163 -0.184 -8.216 -19.682 1.00 27.44 N ANISOU 1263 N VAL A 163 3887 2592 3946 197 -359 -60 N ATOM 1264 CA VAL A 163 1.069 -8.237 -18.929 1.00 28.04 C ANISOU 1264 CA VAL A 163 3958 2683 4014 189 -365 -71 C ATOM 1265 C VAL A 163 1.823 -6.940 -19.214 1.00 28.89 C ANISOU 1265 C VAL A 163 4063 2767 4148 179 -362 -92 C ATOM 1266 O VAL A 163 1.848 -6.468 -20.357 1.00 28.83 O ANISOU 1266 O VAL A 163 4063 2724 4168 185 -356 -79 O ATOM 1267 CB VAL A 163 1.942 -9.451 -19.332 1.00 27.96 C ANISOU 1267 CB VAL A 163 3953 2678 3991 194 -366 -37 C ATOM 1268 CG1 VAL A 163 3.072 -9.667 -18.335 1.00 28.31 C ANISOU 1268 CG1 VAL A 163 3977 2764 4014 194 -372 -33 C ATOM 1269 CG2 VAL A 163 1.096 -10.715 -19.430 1.00 27.96 C ANISOU 1269 CG2 VAL A 163 3971 2679 3974 196 -354 -17 C ATOM 1270 N THR A 164 2.424 -6.366 -18.173 1.00 29.90 N ANISOU 1270 N THR A 164 4180 2917 4265 158 -362 -125 N ATOM 1271 CA THR A 164 3.309 -5.218 -18.331 1.00 30.82 C ANISOU 1271 CA THR A 164 4296 3014 4401 133 -352 -153 C ATOM 1272 C THR A 164 4.612 -5.652 -18.993 1.00 31.47 C ANISOU 1272 C THR A 164 4366 3110 4480 127 -365 -127 C ATOM 1273 O THR A 164 4.944 -6.840 -19.034 1.00 31.16 O ANISOU 1273 O THR A 164 4318 3102 4421 145 -377 -91 O ATOM 1274 CB THR A 164 3.645 -4.560 -16.977 1.00 31.35 C ANISOU 1274 CB THR A 164 4352 3116 4443 95 -345 -205 C ATOM 1275 OG1 THR A 164 4.087 -5.558 -16.049 1.00 31.68 O ANISOU 1275 OG1 THR A 164 4365 3234 4436 90 -368 -193 O ATOM 1276 CG2 THR A 164 2.435 -3.853 -16.406 1.00 31.53 C ANISOU 1276 CG2 THR A 164 4393 3110 4477 100 -319 -239 C ATOM 1277 N GLU A 165 5.348 -4.682 -19.522 1.00 32.59 N ANISOU 1277 N GLU A 165 4511 3225 4646 105 -354 -143 N ATOM 1278 CA GLU A 165 6.725 -4.929 -19.957 1.00 33.42 C ANISOU 1278 CA GLU A 165 4597 3358 4745 92 -365 -126 C ATOM 1279 C GLU A 165 7.604 -5.014 -18.715 1.00 33.73 C ANISOU 1279 C GLU A 165 4600 3478 4738 59 -377 -147 C ATOM 1280 O GLU A 165 7.161 -4.668 -17.614 1.00 33.80 O ANISOU 1280 O GLU A 165 4606 3511 4726 37 -373 -185 O ATOM 1281 CB GLU A 165 7.210 -3.826 -20.909 1.00 34.27 C ANISOU 1281 CB GLU A 165 4718 3413 4889 72 -347 -137 C ATOM 1282 CG GLU A 165 6.460 -3.784 -22.237 1.00 34.57 C ANISOU 1282 CG GLU A 165 4781 3391 4962 108 -337 -103 C ATOM 1283 CD GLU A 165 6.630 -5.058 -23.053 1.00 34.89 C ANISOU 1283 CD GLU A 165 4817 3448 4992 135 -354 -57 C ATOM 1284 OE1 GLU A 165 7.787 -5.424 -23.361 1.00 35.96 O ANISOU 1284 OE1 GLU A 165 4937 3606 5119 129 -359 -42 O ATOM 1285 OE2 GLU A 165 5.610 -5.706 -23.383 1.00 35.33 O ANISOU 1285 OE2 GLU A 165 4884 3495 5043 160 -355 -37 O ATOM 1286 N GLN A 166 8.837 -5.488 -18.885 1.00 34.04 N ANISOU 1286 N GLN A 166 4607 3569 4758 56 -389 -119 N ATOM 1287 CA GLN A 166 9.764 -5.630 -17.758 1.00 34.75 C ANISOU 1287 CA GLN A 166 4646 3763 4794 27 -404 -126 C ATOM 1288 C GLN A 166 9.943 -4.321 -17.006 1.00 35.88 C ANISOU 1288 C GLN A 166 4785 3925 4924 -47 -393 -199 C ATOM 1289 O GLN A 166 10.136 -3.271 -17.619 1.00 36.42 O ANISOU 1289 O GLN A 166 4876 3935 5026 -82 -372 -234 O ATOM 1290 CB GLN A 166 11.131 -6.137 -18.211 1.00 34.59 C ANISOU 1290 CB GLN A 166 4586 3799 4758 36 -413 -81 C ATOM 1291 CG GLN A 166 11.180 -7.628 -18.433 1.00 34.05 C ANISOU 1291 CG GLN A 166 4512 3743 4683 106 -414 -8 C ATOM 1292 CD GLN A 166 12.595 -8.145 -18.513 1.00 34.10 C ANISOU 1292 CD GLN A 166 4465 3830 4662 122 -418 42 C ATOM 1293 OE1 GLN A 166 13.350 -7.760 -19.400 1.00 33.49 O ANISOU 1293 OE1 GLN A 166 4382 3740 4604 110 -414 44 O ATOM 1294 NE2 GLN A 166 12.964 -9.024 -17.586 1.00 34.34 N ANISOU 1294 NE2 GLN A 166 4452 3950 4646 154 -423 89 N ATOM 1295 N ASP A 167 9.862 -4.401 -15.681 1.00 36.97 N ANISOU 1295 N ASP A 167 4896 4140 5011 -73 -402 -224 N ATOM 1296 CA ASP A 167 9.966 -3.235 -14.815 1.00 38.17 C ANISOU 1296 CA ASP A 167 5047 4317 5140 -154 -384 -305 C ATOM 1297 C ASP A 167 11.394 -2.696 -14.843 1.00 39.11 C ANISOU 1297 C ASP A 167 5124 4508 5229 -222 -387 -326 C ATOM 1298 O ASP A 167 12.354 -3.469 -14.943 1.00 39.01 O ANISOU 1298 O ASP A 167 5057 4582 5183 -203 -414 -271 O ATOM 1299 CB ASP A 167 9.572 -3.612 -13.387 1.00 38.92 C ANISOU 1299 CB ASP A 167 5116 4497 5176 -165 -396 -321 C ATOM 1300 CG ASP A 167 9.458 -2.411 -12.470 1.00 39.96 C ANISOU 1300 CG ASP A 167 5258 4641 5283 -252 -368 -416 C ATOM 1301 OD1 ASP A 167 8.515 -1.611 -12.653 1.00 40.40 O ANISOU 1301 OD1 ASP A 167 5374 4590 5388 -254 -330 -461 O ATOM 1302 OD2 ASP A 167 10.307 -2.275 -11.563 1.00 40.65 O ANISOU 1302 OD2 ASP A 167 5294 4852 5300 -319 -380 -445 O ATOM 1303 N SER A 168 11.518 -1.372 -14.765 1.00 39.73 N ANISOU 1303 N SER A 168 5229 4547 5319 -301 -352 -405 N ATOM 1304 CA SER A 168 12.823 -0.701 -14.798 1.00 40.33 C ANISOU 1304 CA SER A 168 5270 4687 5367 -386 -347 -440 C ATOM 1305 C SER A 168 13.641 -0.932 -13.520 1.00 40.82 C ANISOU 1305 C SER A 168 5255 4924 5331 -450 -373 -459 C ATOM 1306 O SER A 168 14.868 -0.987 -13.579 1.00 41.62 O ANISOU 1306 O SER A 168 5294 5130 5390 -490 -391 -445 O ATOM 1307 CB SER A 168 12.650 0.804 -15.055 1.00 40.83 C ANISOU 1307 CB SER A 168 5395 4644 5473 -458 -288 -524 C ATOM 1308 OG SER A 168 11.733 1.384 -14.139 1.00 41.17 O ANISOU 1308 OG SER A 168 5477 4652 5512 -488 -254 -591 O ATOM 1309 N LYS A 169 12.965 -1.067 -12.379 1.00 40.56 N ANISOU 1309 N LYS A 169 5219 4934 5258 -460 -375 -488 N ATOM 1310 CA LYS A 169 13.637 -1.323 -11.101 1.00 40.86 C ANISOU 1310 CA LYS A 169 5178 5154 5193 -519 -401 -501 C ATOM 1311 C LYS A 169 14.137 -2.767 -10.980 1.00 40.10 C ANISOU 1311 C LYS A 169 5008 5174 5054 -435 -450 -389 C ATOM 1312 O LYS A 169 15.348 -2.995 -10.887 1.00 40.54 O ANISOU 1312 O LYS A 169 4986 5365 5054 -460 -473 -356 O ATOM 1313 CB LYS A 169 12.709 -0.999 -9.925 1.00 41.27 C ANISOU 1313 CB LYS A 169 5254 5213 5215 -555 -383 -567 C ATOM 1314 N ASP A 170 13.209 -3.730 -11.000 1.00 38.50 N ANISOU 1314 N ASP A 170 4831 4918 4880 -336 -459 -328 N ATOM 1315 CA ASP A 170 13.518 -5.131 -10.646 1.00 37.73 C ANISOU 1315 CA ASP A 170 4673 4922 4739 -255 -490 -224 C ATOM 1316 C ASP A 170 13.419 -6.176 -11.777 1.00 36.05 C ANISOU 1316 C ASP A 170 4486 4621 4589 -144 -490 -131 C ATOM 1317 O ASP A 170 13.564 -7.368 -11.513 1.00 35.79 O ANISOU 1317 O ASP A 170 4420 4648 4532 -69 -500 -44 O ATOM 1318 CB ASP A 170 12.680 -5.565 -9.422 1.00 38.12 C ANISOU 1318 CB ASP A 170 4718 5021 4743 -243 -496 -225 C ATOM 1319 CG ASP A 170 11.172 -5.653 -9.706 1.00 37.61 C ANISOU 1319 CG ASP A 170 4739 4802 4749 -195 -476 -241 C ATOM 1320 OD1 ASP A 170 10.733 -5.460 -10.861 1.00 36.82 O ANISOU 1320 OD1 ASP A 170 4699 4561 4728 -163 -459 -242 O ATOM 1321 OD2 ASP A 170 10.419 -5.923 -8.743 1.00 38.03 O ANISOU 1321 OD2 ASP A 170 4793 4886 4769 -190 -477 -249 O ATOM 1322 N SER A 171 13.165 -5.734 -13.012 1.00 34.47 N ANISOU 1322 N SER A 171 4347 4284 4467 -136 -472 -150 N ATOM 1323 CA SER A 171 13.111 -6.617 -14.196 1.00 33.02 C ANISOU 1323 CA SER A 171 4190 4017 4339 -48 -466 -77 C ATOM 1324 C SER A 171 12.037 -7.715 -14.150 1.00 31.60 C ANISOU 1324 C SER A 171 4049 3778 4181 31 -460 -29 C ATOM 1325 O SER A 171 12.174 -8.746 -14.808 1.00 31.21 O ANISOU 1325 O SER A 171 4008 3699 4153 102 -451 42 O ATOM 1326 CB SER A 171 14.489 -7.235 -14.466 1.00 33.45 C ANISOU 1326 CB SER A 171 4178 4170 4363 -20 -476 -5 C ATOM 1327 OG SER A 171 15.494 -6.241 -14.448 1.00 34.30 O ANISOU 1327 OG SER A 171 4242 4347 4442 -104 -483 -52 O ATOM 1328 N THR A 172 10.967 -7.485 -13.393 1.00 30.77 N ANISOU 1328 N THR A 172 3971 3652 4069 15 -458 -71 N ATOM 1329 CA THR A 172 9.871 -8.445 -13.279 1.00 29.73 C ANISOU 1329 CA THR A 172 3875 3469 3953 75 -450 -35 C ATOM 1330 C THR A 172 8.689 -8.040 -14.149 1.00 28.75 C ANISOU 1330 C THR A 172 3821 3209 3895 81 -433 -70 C ATOM 1331 O THR A 172 8.634 -6.926 -14.680 1.00 28.55 O ANISOU 1331 O THR A 172 3818 3128 3901 41 -426 -123 O ATOM 1332 CB THR A 172 9.378 -8.574 -11.828 1.00 29.92 C ANISOU 1332 CB THR A 172 3876 3572 3921 60 -458 -49 C ATOM 1333 OG1 THR A 172 8.895 -7.307 -11.367 1.00 29.84 O ANISOU 1333 OG1 THR A 172 3883 3546 3909 -12 -453 -142 O ATOM 1334 CG2 THR A 172 10.493 -9.068 -10.923 1.00 30.60 C ANISOU 1334 CG2 THR A 172 3882 3814 3932 62 -475 1 C ATOM 1335 N TYR A 173 7.758 -8.977 -14.282 1.00 27.86 N ANISOU 1335 N TYR A 173 3740 3048 3798 130 -424 -35 N ATOM 1336 CA TYR A 173 6.493 -8.766 -14.961 1.00 27.19 C ANISOU 1336 CA TYR A 173 3709 2863 3760 138 -412 -59 C ATOM 1337 C TYR A 173 5.384 -8.703 -13.928 1.00 26.85 C ANISOU 1337 C TYR A 173 3674 2832 3698 130 -410 -87 C ATOM 1338 O TYR A 173 5.527 -9.204 -12.812 1.00 27.01 O ANISOU 1338 O TYR A 173 3664 2929 3669 132 -417 -72 O ATOM 1339 CB TYR A 173 6.223 -9.918 -15.928 1.00 26.96 C ANISOU 1339 CB TYR A 173 3708 2778 3756 186 -398 -5 C ATOM 1340 CG TYR A 173 7.283 -10.047 -16.986 1.00 27.10 C ANISOU 1340 CG TYR A 173 3722 2782 3794 198 -394 24 C ATOM 1341 CD1 TYR A 173 7.229 -9.275 -18.149 1.00 27.00 C ANISOU 1341 CD1 TYR A 173 3732 2706 3822 182 -391 0 C ATOM 1342 CD2 TYR A 173 8.358 -10.914 -16.820 1.00 27.49 C ANISOU 1342 CD2 TYR A 173 3741 2884 3819 230 -389 81 C ATOM 1343 CE1 TYR A 173 8.208 -9.376 -19.124 1.00 27.10 C ANISOU 1343 CE1 TYR A 173 3739 2707 3850 191 -387 25 C ATOM 1344 CE2 TYR A 173 9.342 -11.025 -17.789 1.00 27.68 C ANISOU 1344 CE2 TYR A 173 3759 2898 3862 244 -381 108 C ATOM 1345 CZ TYR A 173 9.258 -10.257 -18.939 1.00 27.49 C ANISOU 1345 CZ TYR A 173 3760 2809 3877 221 -381 76 C ATOM 1346 OH TYR A 173 10.232 -10.354 -19.894 1.00 27.88 O ANISOU 1346 OH TYR A 173 3802 2850 3941 233 -373 101 O ATOM 1347 N SER A 174 4.288 -8.062 -14.306 1.00 26.29 N ANISOU 1347 N SER A 174 3636 2691 3660 124 -399 -123 N ATOM 1348 CA SER A 174 3.040 -8.151 -13.566 1.00 26.04 C ANISOU 1348 CA SER A 174 3617 2659 3619 128 -392 -141 C ATOM 1349 C SER A 174 1.930 -8.470 -14.556 1.00 25.41 C ANISOU 1349 C SER A 174 3569 2509 3575 155 -382 -123 C ATOM 1350 O SER A 174 2.034 -8.146 -15.741 1.00 25.00 O ANISOU 1350 O SER A 174 3532 2406 3560 161 -378 -117 O ATOM 1351 CB SER A 174 2.759 -6.854 -12.810 1.00 26.49 C ANISOU 1351 CB SER A 174 3673 2721 3670 88 -381 -209 C ATOM 1352 OG SER A 174 3.629 -6.728 -11.697 1.00 27.03 O ANISOU 1352 OG SER A 174 3706 2878 3686 51 -391 -230 O ATOM 1353 N LEU A 175 0.869 -9.098 -14.058 1.00 25.13 N ANISOU 1353 N LEU A 175 3540 2482 3525 167 -377 -115 N ATOM 1354 CA LEU A 175 -0.237 -9.551 -14.891 1.00 24.79 C ANISOU 1354 CA LEU A 175 3520 2397 3503 182 -368 -97 C ATOM 1355 C LEU A 175 -1.566 -9.222 -14.221 1.00 24.81 C ANISOU 1355 C LEU A 175 3520 2409 3498 181 -360 -122 C ATOM 1356 O LEU A 175 -1.730 -9.417 -13.013 1.00 24.96 O ANISOU 1356 O LEU A 175 3529 2471 3485 175 -360 -133 O ATOM 1357 CB LEU A 175 -0.111 -11.060 -15.159 1.00 24.66 C ANISOU 1357 CB LEU A 175 3515 2381 3473 195 -361 -50 C ATOM 1358 CG LEU A 175 -1.153 -11.741 -16.057 1.00 24.54 C ANISOU 1358 CG LEU A 175 3524 2333 3467 193 -347 -37 C ATOM 1359 CD1 LEU A 175 -0.545 -12.961 -16.742 1.00 24.56 C ANISOU 1359 CD1 LEU A 175 3550 2311 3471 198 -328 1 C ATOM 1360 CD2 LEU A 175 -2.423 -12.132 -15.301 1.00 24.68 C ANISOU 1360 CD2 LEU A 175 3541 2374 3463 186 -339 -43 C ATOM 1361 N SER A 176 -2.504 -8.731 -15.025 1.00 24.66 N ANISOU 1361 N SER A 176 3508 2358 3505 190 -351 -125 N ATOM 1362 CA SER A 176 -3.856 -8.419 -14.592 1.00 24.92 C ANISOU 1362 CA SER A 176 3534 2402 3533 197 -340 -138 C ATOM 1363 C SER A 176 -4.809 -9.274 -15.405 1.00 24.78 C ANISOU 1363 C SER A 176 3516 2389 3510 199 -339 -107 C ATOM 1364 O SER A 176 -4.730 -9.280 -16.631 1.00 24.74 O ANISOU 1364 O SER A 176 3515 2364 3522 200 -342 -88 O ATOM 1365 CB SER A 176 -4.143 -6.939 -14.845 1.00 25.20 C ANISOU 1365 CB SER A 176 3569 2404 3602 212 -321 -163 C ATOM 1366 OG SER A 176 -5.434 -6.569 -14.396 1.00 25.42 O ANISOU 1366 OG SER A 176 3587 2445 3628 229 -303 -171 O ATOM 1367 N SER A 177 -5.681 -10.019 -14.731 1.00 24.91 N ANISOU 1367 N SER A 177 3527 2439 3497 191 -335 -104 N ATOM 1368 CA SER A 177 -6.726 -10.796 -15.399 1.00 24.82 C ANISOU 1368 CA SER A 177 3513 2445 3471 176 -330 -83 C ATOM 1369 C SER A 177 -8.085 -10.317 -14.920 1.00 25.06 C ANISOU 1369 C SER A 177 3517 2514 3492 186 -322 -92 C ATOM 1370 O SER A 177 -8.270 -10.102 -13.724 1.00 25.31 O ANISOU 1370 O SER A 177 3544 2561 3511 192 -316 -112 O ATOM 1371 CB SER A 177 -6.572 -12.287 -15.107 1.00 24.83 C ANISOU 1371 CB SER A 177 3537 2452 3446 151 -321 -67 C ATOM 1372 OG SER A 177 -7.522 -13.035 -15.849 1.00 24.93 O ANISOU 1372 OG SER A 177 3552 2479 3443 121 -310 -57 O ATOM 1373 N THR A 178 -9.025 -10.152 -15.851 1.00 25.14 N ANISOU 1373 N THR A 178 3505 2547 3501 187 -320 -74 N ATOM 1374 CA THR A 178 -10.391 -9.730 -15.535 1.00 25.37 C ANISOU 1374 CA THR A 178 3499 2625 3518 202 -310 -71 C ATOM 1375 C THR A 178 -11.385 -10.806 -15.946 1.00 25.43 C ANISOU 1375 C THR A 178 3489 2689 3485 160 -310 -56 C ATOM 1376 O THR A 178 -11.463 -11.153 -17.119 1.00 25.24 O ANISOU 1376 O THR A 178 3459 2680 3452 136 -316 -39 O ATOM 1377 CB THR A 178 -10.760 -8.422 -16.258 1.00 25.69 C ANISOU 1377 CB THR A 178 3513 2662 3588 248 -301 -54 C ATOM 1378 OG1 THR A 178 -9.832 -7.397 -15.893 1.00 25.79 O ANISOU 1378 OG1 THR A 178 3549 2612 3638 276 -290 -76 O ATOM 1379 CG2 THR A 178 -12.177 -7.972 -15.889 1.00 26.12 C ANISOU 1379 CG2 THR A 178 3524 2772 3629 276 -283 -41 C ATOM 1380 N LEU A 179 -12.126 -11.329 -14.969 1.00 25.59 N ANISOU 1380 N LEU A 179 3502 2745 3477 144 -301 -65 N ATOM 1381 CA LEU A 179 -13.263 -12.215 -15.213 1.00 25.80 C ANISOU 1381 CA LEU A 179 3505 2836 3461 98 -295 -56 C ATOM 1382 C LEU A 179 -14.509 -11.348 -15.310 1.00 26.30 C ANISOU 1382 C LEU A 179 3509 2969 3517 129 -292 -39 C ATOM 1383 O LEU A 179 -14.799 -10.571 -14.396 1.00 26.28 O ANISOU 1383 O LEU A 179 3492 2965 3526 174 -282 -46 O ATOM 1384 CB LEU A 179 -13.425 -13.216 -14.065 1.00 25.85 C ANISOU 1384 CB LEU A 179 3534 2845 3442 66 -282 -69 C ATOM 1385 CG LEU A 179 -14.575 -14.230 -14.123 1.00 26.17 C ANISOU 1385 CG LEU A 179 3559 2947 3436 5 -267 -67 C ATOM 1386 CD1 LEU A 179 -14.287 -15.301 -15.164 1.00 26.17 C ANISOU 1386 CD1 LEU A 179 3592 2929 3422 -59 -256 -67 C ATOM 1387 CD2 LEU A 179 -14.813 -14.866 -12.760 1.00 26.24 C ANISOU 1387 CD2 LEU A 179 3584 2959 3426 -7 -251 -75 C ATOM 1388 N THR A 180 -15.241 -11.486 -16.411 1.00 26.73 N ANISOU 1388 N THR A 180 3523 3088 3545 106 -298 -14 N ATOM 1389 CA THR A 180 -16.443 -10.699 -16.647 1.00 27.38 C ANISOU 1389 CA THR A 180 3535 3256 3614 143 -293 18 C ATOM 1390 C THR A 180 -17.675 -11.593 -16.656 1.00 27.82 C ANISOU 1390 C THR A 180 3548 3415 3607 80 -291 22 C ATOM 1391 O THR A 180 -17.704 -12.627 -17.324 1.00 27.88 O ANISOU 1391 O THR A 180 3565 3448 3578 0 -295 12 O ATOM 1392 CB THR A 180 -16.339 -9.932 -17.974 1.00 27.64 C ANISOU 1392 CB THR A 180 3538 3307 3659 175 -302 56 C ATOM 1393 OG1 THR A 180 -15.146 -9.142 -17.957 1.00 27.41 O ANISOU 1393 OG1 THR A 180 3553 3174 3686 223 -299 48 O ATOM 1394 CG2 THR A 180 -17.545 -9.019 -18.183 1.00 28.32 C ANISOU 1394 CG2 THR A 180 3545 3482 3734 234 -290 106 C ATOM 1395 N LEU A 181 -18.679 -11.187 -15.888 1.00 28.23 N ANISOU 1395 N LEU A 181 3554 3524 3647 112 -279 32 N ATOM 1396 CA LEU A 181 -19.993 -11.824 -15.907 1.00 28.82 C ANISOU 1396 CA LEU A 181 3571 3719 3661 60 -276 43 C ATOM 1397 C LEU A 181 -21.061 -10.782 -15.617 1.00 29.17 C ANISOU 1397 C LEU A 181 3540 3841 3703 137 -263 82 C ATOM 1398 O LEU A 181 -20.751 -9.649 -15.239 1.00 29.12 O ANISOU 1398 O LEU A 181 3541 3776 3748 226 -247 92 O ATOM 1399 CB LEU A 181 -20.069 -12.990 -14.907 1.00 28.88 C ANISOU 1399 CB LEU A 181 3620 3709 3645 -8 -264 3 C ATOM 1400 CG LEU A 181 -19.880 -12.763 -13.403 1.00 28.86 C ANISOU 1400 CG LEU A 181 3647 3651 3667 34 -250 -18 C ATOM 1401 CD1 LEU A 181 -20.240 -14.037 -12.645 1.00 29.04 C ANISOU 1401 CD1 LEU A 181 3693 3689 3651 -42 -236 -40 C ATOM 1402 CD2 LEU A 181 -18.462 -12.322 -13.056 1.00 28.43 C ANISOU 1402 CD2 LEU A 181 3658 3479 3667 78 -255 -36 C ATOM 1403 N SER A 182 -22.316 -11.160 -15.820 1.00 29.64 N ANISOU 1403 N SER A 182 3525 4035 3703 99 -262 105 N ATOM 1404 CA SER A 182 -23.435 -10.271 -15.531 1.00 30.21 C ANISOU 1404 CA SER A 182 3515 4196 3766 175 -245 151 C ATOM 1405 C SER A 182 -23.575 -10.093 -14.023 1.00 30.13 C ANISOU 1405 C SER A 182 3532 4137 3780 210 -220 121 C ATOM 1406 O SER A 182 -23.155 -10.957 -13.244 1.00 29.54 O ANISOU 1406 O SER A 182 3517 4008 3700 150 -222 72 O ATOM 1407 CB SER A 182 -24.734 -10.830 -16.118 1.00 30.94 C ANISOU 1407 CB SER A 182 3513 4466 3778 114 -253 183 C ATOM 1408 OG SER A 182 -25.096 -12.048 -15.494 1.00 30.81 O ANISOU 1408 OG SER A 182 3515 4474 3718 11 -252 137 O ATOM 1409 N LYS A 183 -24.153 -8.964 -13.622 1.00 30.64 N ANISOU 1409 N LYS A 183 3553 4220 3867 310 -190 155 N ATOM 1410 CA LYS A 183 -24.492 -8.713 -12.219 1.00 30.83 C ANISOU 1410 CA LYS A 183 3590 4220 3903 344 -159 129 C ATOM 1411 C LYS A 183 -25.430 -9.807 -11.714 1.00 30.91 C ANISOU 1411 C LYS A 183 3564 4332 3848 263 -166 116 C ATOM 1412 O LYS A 183 -25.232 -10.352 -10.627 1.00 30.49 O ANISOU 1412 O LYS A 183 3558 4234 3792 227 -160 71 O ATOM 1413 CB LYS A 183 -25.170 -7.351 -12.071 1.00 31.75 C ANISOU 1413 CB LYS A 183 3654 4359 4049 464 -114 176 C ATOM 1414 CG LYS A 183 -25.476 -6.947 -10.636 1.00 32.16 C ANISOU 1414 CG LYS A 183 3724 4376 4117 506 -73 143 C ATOM 1415 CD LYS A 183 -26.794 -6.206 -10.545 1.00 33.32 C ANISOU 1415 CD LYS A 183 3783 4625 4254 591 -30 203 C ATOM 1416 CE LYS A 183 -27.063 -5.718 -9.134 1.00 33.76 C ANISOU 1416 CE LYS A 183 3862 4637 4328 636 21 165 C ATOM 1417 NZ LYS A 183 -28.181 -4.734 -9.128 1.00 34.95 N ANISOU 1417 NZ LYS A 183 3936 4856 4487 748 80 230 N ATOM 1418 N ALA A 184 -26.449 -10.103 -12.520 1.00 31.42 N ANISOU 1418 N ALA A 184 3540 4541 3856 232 -176 161 N ATOM 1419 CA ALA A 184 -27.434 -11.140 -12.221 1.00 31.73 C ANISOU 1419 CA ALA A 184 3535 4695 3825 141 -180 152 C ATOM 1420 C ALA A 184 -26.777 -12.480 -11.895 1.00 31.16 C ANISOU 1420 C ALA A 184 3547 4553 3739 26 -192 90 C ATOM 1421 O ALA A 184 -27.099 -13.099 -10.879 1.00 31.29 O ANISOU 1421 O ALA A 184 3581 4571 3736 -14 -178 62 O ATOM 1422 CB ALA A 184 -28.396 -11.295 -13.389 1.00 32.37 C ANISOU 1422 CB ALA A 184 3512 4947 3841 105 -196 204 C ATOM 1423 N ASP A 185 -25.848 -12.913 -12.744 1.00 30.67 N ANISOU 1423 N ASP A 185 3538 4427 3689 -20 -212 74 N ATOM 1424 CA ASP A 185 -25.134 -14.169 -12.514 1.00 30.29 C ANISOU 1424 CA ASP A 185 3575 4298 3635 -116 -212 24 C ATOM 1425 C ASP A 185 -24.133 -14.073 -11.358 1.00 29.79 C ANISOU 1425 C ASP A 185 3597 4098 3625 -72 -203 -6 C ATOM 1426 O ASP A 185 -23.994 -15.026 -10.591 1.00 29.45 O ANISOU 1426 O ASP A 185 3602 4020 3568 -129 -189 -34 O ATOM 1427 CB ASP A 185 -24.422 -14.652 -13.779 1.00 29.99 C ANISOU 1427 CB ASP A 185 3570 4231 3594 -174 -228 17 C ATOM 1428 CG ASP A 185 -23.964 -16.100 -13.665 1.00 29.79 C ANISOU 1428 CG ASP A 185 3624 4144 3551 -284 -212 -28 C ATOM 1429 OD1 ASP A 185 -24.804 -16.962 -13.326 1.00 30.20 O ANISOU 1429 OD1 ASP A 185 3660 4262 3553 -368 -193 -43 O ATOM 1430 OD2 ASP A 185 -22.772 -16.378 -13.903 1.00 29.09 O ANISOU 1430 OD2 ASP A 185 3613 3940 3501 -285 -213 -46 O ATOM 1431 N TYR A 186 -23.452 -12.933 -11.227 1.00 29.68 N ANISOU 1431 N TYR A 186 3599 4013 3667 24 -206 0 N ATOM 1432 CA TYR A 186 -22.526 -12.713 -10.111 1.00 29.55 C ANISOU 1432 CA TYR A 186 3649 3889 3689 62 -198 -31 C ATOM 1433 C TYR A 186 -23.197 -12.946 -8.749 1.00 30.27 C ANISOU 1433 C TYR A 186 3731 4013 3756 58 -177 -45 C ATOM 1434 O TYR A 186 -22.608 -13.551 -7.851 1.00 29.88 O ANISOU 1434 O TYR A 186 3738 3909 3707 33 -172 -71 O ATOM 1435 CB TYR A 186 -21.905 -11.306 -10.162 1.00 29.29 C ANISOU 1435 CB TYR A 186 3624 3792 3713 158 -194 -26 C ATOM 1436 CG TYR A 186 -21.055 -10.974 -8.948 1.00 28.89 C ANISOU 1436 CG TYR A 186 3630 3655 3691 188 -183 -65 C ATOM 1437 CD1 TYR A 186 -19.798 -11.558 -8.771 1.00 28.35 C ANISOU 1437 CD1 TYR A 186 3630 3507 3635 155 -198 -88 C ATOM 1438 CD2 TYR A 186 -21.514 -10.092 -7.964 1.00 29.17 C ANISOU 1438 CD2 TYR A 186 3650 3698 3737 245 -154 -77 C ATOM 1439 CE1 TYR A 186 -19.019 -11.267 -7.659 1.00 28.16 C ANISOU 1439 CE1 TYR A 186 3646 3428 3624 174 -192 -120 C ATOM 1440 CE2 TYR A 186 -20.741 -9.791 -6.848 1.00 29.02 C ANISOU 1440 CE2 TYR A 186 3679 3614 3731 258 -143 -119 C ATOM 1441 CZ TYR A 186 -19.495 -10.380 -6.697 1.00 28.54 C ANISOU 1441 CZ TYR A 186 3676 3491 3675 220 -165 -139 C ATOM 1442 OH TYR A 186 -18.728 -10.092 -5.590 1.00 28.41 O ANISOU 1442 OH TYR A 186 3698 3435 3662 226 -157 -178 O ATOM 1443 N GLU A 187 -24.441 -12.489 -8.621 1.00 31.46 N ANISOU 1443 N GLU A 187 3807 4264 3883 85 -162 -23 N ATOM 1444 CA GLU A 187 -25.195 -12.599 -7.371 1.00 32.36 C ANISOU 1444 CA GLU A 187 3902 4422 3972 87 -139 -34 C ATOM 1445 C GLU A 187 -25.842 -13.973 -7.141 1.00 32.65 C ANISOU 1445 C GLU A 187 3933 4522 3952 -15 -136 -40 C ATOM 1446 O GLU A 187 -26.455 -14.188 -6.098 1.00 32.90 O ANISOU 1446 O GLU A 187 3952 4591 3958 -23 -117 -48 O ATOM 1447 CB GLU A 187 -26.224 -11.457 -7.288 1.00 33.32 C ANISOU 1447 CB GLU A 187 3946 4619 4096 171 -115 -4 C ATOM 1448 CG GLU A 187 -25.536 -10.090 -7.273 1.00 33.60 C ANISOU 1448 CG GLU A 187 4006 4566 4194 271 -99 -7 C ATOM 1449 CD GLU A 187 -26.470 -8.910 -7.072 1.00 34.71 C ANISOU 1449 CD GLU A 187 4084 4756 4348 368 -57 23 C ATOM 1450 OE1 GLU A 187 -27.692 -9.036 -7.307 1.00 35.40 O ANISOU 1450 OE1 GLU A 187 4087 4967 4395 371 -50 65 O ATOM 1451 OE2 GLU A 187 -25.954 -7.835 -6.679 1.00 35.28 O ANISOU 1451 OE2 GLU A 187 4193 4742 4471 443 -25 5 O ATOM 1452 N LYS A 188 -25.686 -14.894 -8.097 1.00 32.73 N ANISOU 1452 N LYS A 188 3958 4538 3941 -98 -149 -39 N ATOM 1453 CA LYS A 188 -26.119 -16.293 -7.958 1.00 33.14 C ANISOU 1453 CA LYS A 188 4026 4621 3944 -210 -135 -52 C ATOM 1454 C LYS A 188 -25.026 -17.246 -7.449 1.00 32.60 C ANISOU 1454 C LYS A 188 4059 4434 3894 -247 -123 -74 C ATOM 1455 O LYS A 188 -25.332 -18.376 -7.065 1.00 33.08 O ANISOU 1455 O LYS A 188 4147 4500 3922 -328 -97 -83 O ATOM 1456 CB LYS A 188 -26.627 -16.825 -9.300 1.00 33.80 C ANISOU 1456 CB LYS A 188 4072 4783 3988 -293 -142 -45 C ATOM 1457 CG LYS A 188 -27.986 -16.298 -9.720 1.00 34.85 C ANISOU 1457 CG LYS A 188 4089 5077 4074 -287 -147 -13 C ATOM 1458 CD LYS A 188 -28.309 -16.759 -11.136 1.00 35.46 C ANISOU 1458 CD LYS A 188 4128 5239 4107 -373 -159 -8 C ATOM 1459 CE LYS A 188 -29.769 -17.128 -11.322 1.00 36.53 C ANISOU 1459 CE LYS A 188 4165 5554 4162 -449 -152 5 C ATOM 1460 NZ LYS A 188 -29.942 -17.879 -12.599 1.00 37.10 N ANISOU 1460 NZ LYS A 188 4220 5699 4178 -571 -158 -9 N ATOM 1461 N HIS A 189 -23.766 -16.815 -7.474 1.00 31.72 N ANISOU 1461 N HIS A 189 4001 4220 3832 -191 -138 -79 N ATOM 1462 CA HIS A 189 -22.646 -17.643 -7.012 1.00 31.08 C ANISOU 1462 CA HIS A 189 4005 4035 3768 -210 -126 -87 C ATOM 1463 C HIS A 189 -21.967 -16.987 -5.819 1.00 30.69 C ANISOU 1463 C HIS A 189 3976 3943 3742 -135 -132 -92 C ATOM 1464 O HIS A 189 -22.138 -15.786 -5.591 1.00 30.63 O ANISOU 1464 O HIS A 189 3930 3958 3752 -67 -143 -98 O ATOM 1465 CB HIS A 189 -21.665 -17.873 -8.158 1.00 30.62 C ANISOU 1465 CB HIS A 189 3990 3906 3737 -224 -137 -87 C ATOM 1466 CG HIS A 189 -22.256 -18.632 -9.301 1.00 30.92 C ANISOU 1466 CG HIS A 189 4018 3988 3743 -315 -126 -91 C ATOM 1467 ND1 HIS A 189 -22.427 -19.999 -9.274 1.00 31.23 N ANISOU 1467 ND1 HIS A 189 4104 4008 3755 -410 -86 -102 N ATOM 1468 CD2 HIS A 189 -22.738 -18.217 -10.496 1.00 31.04 C ANISOU 1468 CD2 HIS A 189 3980 4070 3744 -332 -144 -88 C ATOM 1469 CE1 HIS A 189 -22.980 -20.395 -10.405 1.00 31.60 C ANISOU 1469 CE1 HIS A 189 4129 4108 3769 -491 -79 -114 C ATOM 1470 NE2 HIS A 189 -23.179 -19.333 -11.163 1.00 31.53 N ANISOU 1470 NE2 HIS A 189 4055 4161 3764 -445 -119 -104 N ATOM 1471 N LYS A 190 -21.209 -17.782 -5.063 1.00 30.47 N ANISOU 1471 N LYS A 190 4007 3858 3713 -148 -117 -88 N ATOM 1472 CA LYS A 190 -20.615 -17.349 -3.789 1.00 30.51 C ANISOU 1472 CA LYS A 190 4025 3845 3721 -95 -120 -92 C ATOM 1473 C LYS A 190 -19.093 -17.217 -3.845 1.00 29.80 C ANISOU 1473 C LYS A 190 3982 3678 3663 -60 -136 -88 C ATOM 1474 O LYS A 190 -18.555 -16.159 -3.514 1.00 29.37 O ANISOU 1474 O LYS A 190 3917 3615 3626 -7 -154 -106 O ATOM 1475 CB LYS A 190 -21.008 -18.333 -2.676 1.00 31.29 C ANISOU 1475 CB LYS A 190 4140 3968 3781 -132 -90 -78 C ATOM 1476 CG LYS A 190 -20.673 -17.904 -1.246 1.00 31.74 C ANISOU 1476 CG LYS A 190 4196 4042 3823 -87 -91 -83 C ATOM 1477 CD LYS A 190 -21.385 -16.615 -0.841 1.00 32.30 C ANISOU 1477 CD LYS A 190 4212 4170 3892 -44 -99 -114 C ATOM 1478 CE LYS A 190 -21.802 -16.593 0.630 1.00 33.04 C ANISOU 1478 CE LYS A 190 4291 4317 3945 -38 -81 -122 C ATOM 1479 NZ LYS A 190 -20.674 -16.435 1.589 1.00 33.21 N ANISOU 1479 NZ LYS A 190 4342 4319 3957 -12 -89 -127 N ATOM 1480 N VAL A 191 -18.410 -18.288 -4.258 1.00 29.45 N ANISOU 1480 N VAL A 191 3988 3576 3624 -92 -122 -65 N ATOM 1481 CA VAL A 191 -16.949 -18.378 -4.153 1.00 28.96 C ANISOU 1481 CA VAL A 191 3968 3452 3584 -58 -130 -50 C ATOM 1482 C VAL A 191 -16.289 -18.025 -5.481 1.00 28.38 C ANISOU 1482 C VAL A 191 3905 3328 3549 -50 -149 -56 C ATOM 1483 O VAL A 191 -16.528 -18.687 -6.492 1.00 28.49 O ANISOU 1483 O VAL A 191 3937 3319 3568 -95 -134 -51 O ATOM 1484 CB VAL A 191 -16.490 -19.790 -3.727 1.00 29.31 C ANISOU 1484 CB VAL A 191 4064 3457 3614 -82 -92 -8 C ATOM 1485 CG1 VAL A 191 -14.997 -19.793 -3.388 1.00 29.17 C ANISOU 1485 CG1 VAL A 191 4072 3401 3610 -32 -102 19 C ATOM 1486 CG2 VAL A 191 -17.321 -20.287 -2.548 1.00 29.80 C ANISOU 1486 CG2 VAL A 191 4117 3571 3635 -102 -67 3 C ATOM 1487 N TYR A 192 -15.450 -16.994 -5.457 1.00 27.65 N ANISOU 1487 N TYR A 192 3804 3222 3482 1 -178 -69 N ATOM 1488 CA TYR A 192 -14.725 -16.523 -6.630 1.00 27.13 C ANISOU 1488 CA TYR A 192 3746 3109 3453 16 -197 -74 C ATOM 1489 C TYR A 192 -13.246 -16.662 -6.356 1.00 27.01 C ANISOU 1489 C TYR A 192 3761 3051 3450 43 -204 -57 C ATOM 1490 O TYR A 192 -12.747 -16.102 -5.386 1.00 26.93 O ANISOU 1490 O TYR A 192 3740 3064 3429 72 -215 -66 O ATOM 1491 CB TYR A 192 -15.093 -15.071 -6.914 1.00 26.78 C ANISOU 1491 CB TYR A 192 3660 3086 3428 51 -217 -102 C ATOM 1492 CG TYR A 192 -16.512 -14.950 -7.389 1.00 26.86 C ANISOU 1492 CG TYR A 192 3630 3150 3425 32 -210 -104 C ATOM 1493 CD1 TYR A 192 -17.570 -14.857 -6.478 1.00 27.11 C ANISOU 1493 CD1 TYR A 192 3629 3243 3427 30 -197 -111 C ATOM 1494 CD2 TYR A 192 -16.813 -14.979 -8.750 1.00 26.65 C ANISOU 1494 CD2 TYR A 192 3591 3126 3408 12 -216 -96 C ATOM 1495 CE1 TYR A 192 -18.885 -14.772 -6.915 1.00 27.33 C ANISOU 1495 CE1 TYR A 192 3610 3337 3438 14 -190 -106 C ATOM 1496 CE2 TYR A 192 -18.124 -14.895 -9.196 1.00 26.93 C ANISOU 1496 CE2 TYR A 192 3576 3235 3421 -9 -212 -91 C ATOM 1497 CZ TYR A 192 -19.155 -14.792 -8.280 1.00 27.24 C ANISOU 1497 CZ TYR A 192 3579 3337 3432 -6 -198 -94 C ATOM 1498 OH TYR A 192 -20.449 -14.704 -8.729 1.00 27.36 O ANISOU 1498 OH TYR A 192 3535 3440 3421 -25 -194 -83 O ATOM 1499 N ALA A 193 -12.552 -17.419 -7.203 1.00 27.05 N ANISOU 1499 N ALA A 193 3804 3001 3473 31 -193 -34 N ATOM 1500 CA ALA A 193 -11.163 -17.795 -6.946 1.00 27.17 C ANISOU 1500 CA ALA A 193 3845 2982 3494 60 -191 -4 C ATOM 1501 C ALA A 193 -10.287 -17.632 -8.181 1.00 27.13 C ANISOU 1501 C ALA A 193 3857 2924 3526 69 -200 -2 C ATOM 1502 O ALA A 193 -10.732 -17.851 -9.308 1.00 26.90 O ANISOU 1502 O ALA A 193 3840 2870 3511 38 -192 -12 O ATOM 1503 CB ALA A 193 -11.094 -19.224 -6.437 1.00 27.42 C ANISOU 1503 CB ALA A 193 3915 2996 3507 48 -147 42 C ATOM 1504 N CYS A 194 -9.040 -17.240 -7.933 1.00 27.43 N ANISOU 1504 N CYS A 194 3892 2957 3573 106 -218 9 N ATOM 1505 CA CYS A 194 -8.016 -17.089 -8.946 1.00 27.60 C ANISOU 1505 CA CYS A 194 3928 2933 3626 120 -226 15 C ATOM 1506 C CYS A 194 -6.885 -18.051 -8.591 1.00 27.52 C ANISOU 1506 C CYS A 194 3941 2904 3609 146 -203 70 C ATOM 1507 O CYS A 194 -6.172 -17.822 -7.614 1.00 27.52 O ANISOU 1507 O CYS A 194 3917 2951 3588 175 -217 87 O ATOM 1508 CB CYS A 194 -7.513 -15.644 -8.927 1.00 28.00 C ANISOU 1508 CB CYS A 194 3946 3003 3691 140 -265 -19 C ATOM 1509 SG CYS A 194 -6.150 -15.309 -10.052 1.00 29.16 S ANISOU 1509 SG CYS A 194 4103 3104 3874 157 -278 -12 S ATOM 1510 N GLU A 195 -6.751 -19.139 -9.352 1.00 27.39 N ANISOU 1510 N GLU A 195 3970 2828 3608 136 -162 98 N ATOM 1511 CA GLU A 195 -5.659 -20.101 -9.156 1.00 27.60 C ANISOU 1511 CA GLU A 195 4023 2825 3637 174 -125 160 C ATOM 1512 C GLU A 195 -4.489 -19.793 -10.092 1.00 27.13 C ANISOU 1512 C GLU A 195 3966 2734 3607 198 -137 166 C ATOM 1513 O GLU A 195 -4.642 -19.836 -11.316 1.00 26.82 O ANISOU 1513 O GLU A 195 3952 2643 3594 172 -127 142 O ATOM 1514 CB GLU A 195 -6.126 -21.540 -9.368 1.00 28.12 C ANISOU 1514 CB GLU A 195 4149 2829 3706 151 -54 190 C ATOM 1515 CG GLU A 195 -5.038 -22.559 -9.044 1.00 28.80 C ANISOU 1515 CG GLU A 195 4265 2881 3796 206 -2 268 C ATOM 1516 CD GLU A 195 -5.519 -23.995 -9.067 1.00 29.55 C ANISOU 1516 CD GLU A 195 4429 2905 3895 186 85 300 C ATOM 1517 OE1 GLU A 195 -6.337 -24.351 -9.939 1.00 29.79 O ANISOU 1517 OE1 GLU A 195 4500 2884 3937 119 114 255 O ATOM 1518 OE2 GLU A 195 -5.056 -24.775 -8.212 1.00 30.50 O ANISOU 1518 OE2 GLU A 195 4562 3022 4003 235 129 373 O ATOM 1519 N VAL A 196 -3.326 -19.514 -9.503 1.00 26.96 N ANISOU 1519 N VAL A 196 3913 2754 3575 245 -155 200 N ATOM 1520 CA VAL A 196 -2.137 -19.094 -10.237 1.00 26.61 C ANISOU 1520 CA VAL A 196 3858 2698 3553 269 -172 207 C ATOM 1521 C VAL A 196 -1.080 -20.197 -10.214 1.00 26.87 C ANISOU 1521 C VAL A 196 3912 2708 3589 320 -123 286 C ATOM 1522 O VAL A 196 -0.742 -20.699 -9.147 1.00 27.15 O ANISOU 1522 O VAL A 196 3930 2791 3594 358 -108 343 O ATOM 1523 CB VAL A 196 -1.549 -17.796 -9.636 1.00 26.50 C ANISOU 1523 CB VAL A 196 3785 2762 3521 274 -230 180 C ATOM 1524 CG1 VAL A 196 -0.225 -17.424 -10.300 1.00 26.40 C ANISOU 1524 CG1 VAL A 196 3757 2748 3526 296 -244 192 C ATOM 1525 CG2 VAL A 196 -2.555 -16.655 -9.767 1.00 26.20 C ANISOU 1525 CG2 VAL A 196 3735 2729 3490 234 -263 106 C ATOM 1526 N THR A 197 -0.574 -20.556 -11.397 1.00 26.69 N ANISOU 1526 N THR A 197 3923 2615 3601 326 -95 292 N ATOM 1527 CA THR A 197 0.544 -21.496 -11.542 1.00 27.14 C ANISOU 1527 CA THR A 197 4000 2644 3670 385 -43 368 C ATOM 1528 C THR A 197 1.766 -20.751 -12.076 1.00 26.83 C ANISOU 1528 C THR A 197 3921 2633 3641 409 -79 370 C ATOM 1529 O THR A 197 1.668 -20.003 -13.054 1.00 26.25 O ANISOU 1529 O THR A 197 3850 2533 3590 373 -109 313 O ATOM 1530 CB THR A 197 0.195 -22.648 -12.506 1.00 27.37 C ANISOU 1530 CB THR A 197 4110 2560 3731 369 37 373 C ATOM 1531 OG1 THR A 197 -1.018 -23.274 -12.078 1.00 27.63 O ANISOU 1531 OG1 THR A 197 4180 2568 3752 329 71 360 O ATOM 1532 CG2 THR A 197 1.313 -23.695 -12.556 1.00 28.04 C ANISOU 1532 CG2 THR A 197 4222 2603 3831 442 110 460 C ATOM 1533 N HIS A 198 2.908 -20.960 -11.427 1.00 27.19 N ANISOU 1533 N HIS A 198 3927 2739 3666 471 -75 441 N ATOM 1534 CA HIS A 198 4.156 -20.295 -11.801 1.00 27.21 C ANISOU 1534 CA HIS A 198 3881 2787 3669 493 -108 450 C ATOM 1535 C HIS A 198 5.334 -21.074 -11.218 1.00 28.04 C ANISOU 1535 C HIS A 198 3955 2945 3754 576 -72 557 C ATOM 1536 O HIS A 198 5.233 -21.610 -10.111 1.00 28.48 O ANISOU 1536 O HIS A 198 3993 3054 3774 608 -55 614 O ATOM 1537 CB HIS A 198 4.148 -18.842 -11.305 1.00 26.83 C ANISOU 1537 CB HIS A 198 3773 2828 3595 450 -188 388 C ATOM 1538 CG HIS A 198 5.307 -18.036 -11.793 1.00 26.68 C ANISOU 1538 CG HIS A 198 3709 2848 3579 452 -221 380 C ATOM 1539 ND1 HIS A 198 6.467 -17.899 -11.069 1.00 27.13 N ANISOU 1539 ND1 HIS A 198 3698 3015 3594 483 -239 430 N ATOM 1540 CD2 HIS A 198 5.492 -17.339 -12.938 1.00 26.21 C ANISOU 1540 CD2 HIS A 198 3662 2741 3555 423 -238 331 C ATOM 1541 CE1 HIS A 198 7.319 -17.150 -11.744 1.00 27.03 C ANISOU 1541 CE1 HIS A 198 3659 3018 3594 469 -265 407 C ATOM 1542 NE2 HIS A 198 6.752 -16.797 -12.883 1.00 26.37 N ANISOU 1542 NE2 HIS A 198 3627 2835 3559 435 -264 349 N ATOM 1543 N GLN A 199 6.438 -21.151 -11.962 1.00 28.34 N ANISOU 1543 N GLN A 199 3983 2975 3811 613 -57 590 N ATOM 1544 CA GLN A 199 7.570 -22.018 -11.578 1.00 29.35 C ANISOU 1544 CA GLN A 199 4082 3145 3924 706 -8 706 C ATOM 1545 C GLN A 199 8.262 -21.621 -10.266 1.00 29.70 C ANISOU 1545 C GLN A 199 4027 3356 3901 733 -54 758 C ATOM 1546 O GLN A 199 8.810 -22.467 -9.568 1.00 30.54 O ANISOU 1546 O GLN A 199 4108 3515 3982 812 -11 867 O ATOM 1547 CB GLN A 199 8.589 -22.133 -12.719 1.00 29.73 C ANISOU 1547 CB GLN A 199 4136 3151 4007 739 20 727 C ATOM 1548 CG GLN A 199 9.363 -20.868 -13.054 1.00 29.70 C ANISOU 1548 CG GLN A 199 4066 3227 3991 705 -56 682 C ATOM 1549 CD GLN A 199 10.071 -20.982 -14.392 1.00 29.89 C ANISOU 1549 CD GLN A 199 4115 3181 4059 722 -25 682 C ATOM 1550 OE1 GLN A 199 9.461 -20.807 -15.451 1.00 29.76 O ANISOU 1550 OE1 GLN A 199 4161 3065 4083 672 -19 611 O ATOM 1551 NE2 GLN A 199 11.360 -21.283 -14.353 1.00 30.64 N ANISOU 1551 NE2 GLN A 199 4160 3341 4142 794 -4 767 N ATOM 1552 N GLY A 200 8.255 -20.331 -9.958 1.00 29.19 N ANISOU 1552 N GLY A 200 3908 3376 3806 667 -136 683 N ATOM 1553 CA GLY A 200 8.646 -19.823 -8.642 1.00 29.65 C ANISOU 1553 CA GLY A 200 3878 3598 3789 661 -186 703 C ATOM 1554 C GLY A 200 7.823 -20.247 -7.428 1.00 29.89 C ANISOU 1554 C GLY A 200 3909 3669 3780 664 -178 725 C ATOM 1555 O GLY A 200 8.310 -20.146 -6.301 1.00 30.43 O ANISOU 1555 O GLY A 200 3900 3885 3778 679 -203 772 O ATOM 1556 N LEU A 201 6.586 -20.699 -7.636 1.00 29.41 N ANISOU 1556 N LEU A 201 3928 3490 3757 644 -146 691 N ATOM 1557 CA LEU A 201 5.729 -21.159 -6.534 1.00 29.84 C ANISOU 1557 CA LEU A 201 3989 3572 3777 645 -133 712 C ATOM 1558 C LEU A 201 5.986 -22.625 -6.213 1.00 30.82 C ANISOU 1558 C LEU A 201 4136 3673 3903 736 -51 839 C ATOM 1559 O LEU A 201 6.173 -23.428 -7.121 1.00 30.86 O ANISOU 1559 O LEU A 201 4201 3562 3961 776 16 874 O ATOM 1560 CB LEU A 201 4.253 -20.977 -6.888 1.00 29.08 C ANISOU 1560 CB LEU A 201 3962 3370 3717 579 -133 620 C ATOM 1561 CG LEU A 201 3.773 -19.538 -7.040 1.00 28.30 C ANISOU 1561 CG LEU A 201 3845 3290 3617 497 -203 503 C ATOM 1562 CD1 LEU A 201 2.423 -19.499 -7.738 1.00 27.67 C ANISOU 1562 CD1 LEU A 201 3834 3095 3583 449 -191 431 C ATOM 1563 CD2 LEU A 201 3.705 -18.861 -5.678 1.00 28.65 C ANISOU 1563 CD2 LEU A 201 3825 3468 3592 470 -248 484 C ATOM 1564 N SER A 202 5.982 -22.969 -4.926 1.00 31.90 N ANISOU 1564 N SER A 202 4227 3915 3979 768 -49 908 N ATOM 1565 CA SER A 202 6.152 -24.366 -4.498 1.00 33.10 C ANISOU 1565 CA SER A 202 4402 4044 4131 862 38 1040 C ATOM 1566 C SER A 202 4.962 -25.236 -4.929 1.00 33.10 C ANISOU 1566 C SER A 202 4516 3874 4188 844 112 1018 C ATOM 1567 O SER A 202 5.139 -26.397 -5.287 1.00 33.81 O ANISOU 1567 O SER A 202 4666 3865 4317 909 208 1098 O ATOM 1568 CB SER A 202 6.389 -24.463 -2.988 1.00 33.94 C ANISOU 1568 CB SER A 202 4426 4319 4150 896 19 1120 C ATOM 1569 OG SER A 202 5.410 -23.736 -2.277 1.00 33.72 O ANISOU 1569 OG SER A 202 4388 4337 4086 812 -38 1029 O ATOM 1570 N SER A 203 3.759 -24.665 -4.893 1.00 32.65 N ANISOU 1570 N SER A 203 4485 3785 4133 754 72 910 N ATOM 1571 CA SER A 203 2.577 -25.272 -5.521 1.00 32.51 C ANISOU 1571 CA SER A 203 4568 3615 4168 711 128 861 C ATOM 1572 C SER A 203 1.629 -24.161 -5.985 1.00 31.66 C ANISOU 1572 C SER A 203 4465 3492 4071 610 57 723 C ATOM 1573 O SER A 203 1.769 -23.018 -5.538 1.00 31.31 O ANISOU 1573 O SER A 203 4354 3551 3991 580 -23 674 O ATOM 1574 CB SER A 203 1.878 -26.226 -4.547 1.00 33.17 C ANISOU 1574 CB SER A 203 4681 3691 4231 732 186 924 C ATOM 1575 OG SER A 203 1.457 -25.557 -3.372 1.00 33.34 O ANISOU 1575 OG SER A 203 4638 3840 4188 702 120 903 O ATOM 1576 N PRO A 204 0.672 -24.478 -6.887 1.00 31.40 N ANISOU 1576 N PRO A 204 4510 3336 4085 556 92 663 N ATOM 1577 CA PRO A 204 -0.260 -23.439 -7.351 1.00 30.56 C ANISOU 1577 CA PRO A 204 4400 3224 3985 472 30 546 C ATOM 1578 C PRO A 204 -0.979 -22.738 -6.195 1.00 30.46 C ANISOU 1578 C PRO A 204 4340 3308 3925 441 -24 512 C ATOM 1579 O PRO A 204 -1.435 -23.407 -5.268 1.00 30.85 O ANISOU 1579 O PRO A 204 4397 3379 3948 454 8 556 O ATOM 1580 CB PRO A 204 -1.252 -24.220 -8.220 1.00 30.51 C ANISOU 1580 CB PRO A 204 4480 3096 4019 424 92 513 C ATOM 1581 CG PRO A 204 -0.475 -25.394 -8.707 1.00 31.03 C ANISOU 1581 CG PRO A 204 4600 3077 4115 479 181 588 C ATOM 1582 CD PRO A 204 0.431 -25.765 -7.572 1.00 31.72 C ANISOU 1582 CD PRO A 204 4643 3241 4169 567 195 696 C ATOM 1583 N AVAL A 205 -1.059 -21.409 -6.266 0.50 29.98 N ANISOU 1583 N AVAL A 205 4235 3300 3856 402 -97 434 N ATOM 1584 N BVAL A 205 -1.051 -21.409 -6.245 0.50 29.95 N ANISOU 1584 N BVAL A 205 4230 3297 3851 402 -98 435 N ATOM 1585 CA AVAL A 205 -1.651 -20.577 -5.219 0.50 29.97 C ANISOU 1585 CA AVAL A 205 4188 3388 3811 371 -146 390 C ATOM 1586 CA BVAL A 205 -1.657 -20.618 -5.174 0.50 29.93 C ANISOU 1586 CA BVAL A 205 4184 3385 3805 372 -144 393 C ATOM 1587 C AVAL A 205 -3.044 -20.124 -5.635 0.50 29.54 C ANISOU 1587 C AVAL A 205 4160 3286 3777 310 -156 307 C ATOM 1588 C BVAL A 205 -3.027 -20.110 -5.613 0.50 29.51 C ANISOU 1588 C BVAL A 205 4155 3285 3773 310 -157 307 C ATOM 1589 O AVAL A 205 -3.229 -19.671 -6.767 0.50 28.99 O ANISOU 1589 O AVAL A 205 4110 3157 3748 284 -167 258 O ATOM 1590 O BVAL A 205 -3.180 -19.613 -6.733 0.50 28.96 O ANISOU 1590 O BVAL A 205 4103 3158 3743 285 -170 257 O ATOM 1591 CB AVAL A 205 -0.789 -19.326 -4.966 0.50 29.93 C ANISOU 1591 CB AVAL A 205 4119 3472 3782 364 -208 355 C ATOM 1592 CB BVAL A 205 -0.760 -19.427 -4.778 0.50 29.91 C ANISOU 1592 CB BVAL A 205 4112 3481 3771 369 -206 365 C ATOM 1593 CG1AVAL A 205 -1.583 -18.261 -4.223 0.50 29.80 C ANISOU 1593 CG1AVAL A 205 4074 3514 3736 315 -249 277 C ATOM 1594 CG1BVAL A 205 -0.654 -18.429 -5.919 0.50 29.24 C ANISOU 1594 CG1BVAL A 205 4033 3346 3729 337 -237 291 C ATOM 1595 CG2AVAL A 205 0.467 -19.697 -4.196 0.50 30.57 C ANISOU 1595 CG2AVAL A 205 4149 3650 3817 418 -207 439 C ATOM 1596 CG2BVAL A 205 -1.293 -18.755 -3.520 0.50 30.09 C ANISOU 1596 CG2BVAL A 205 4092 3600 3739 339 -238 327 C ATOM 1597 N THR A 206 -4.012 -20.248 -4.725 1.00 29.73 N ANISOU 1597 N THR A 206 4180 3345 3771 290 -151 298 N ATOM 1598 CA THR A 206 -5.389 -19.796 -4.966 1.00 29.62 C ANISOU 1598 CA THR A 206 4178 3309 3768 237 -161 227 C ATOM 1599 C THR A 206 -5.700 -18.614 -4.058 1.00 29.85 C ANISOU 1599 C THR A 206 4157 3423 3764 221 -207 174 C ATOM 1600 O THR A 206 -5.504 -18.696 -2.847 1.00 30.39 O ANISOU 1600 O THR A 206 4195 3569 3783 234 -211 200 O ATOM 1601 CB THR A 206 -6.402 -20.921 -4.695 1.00 30.01 C ANISOU 1601 CB THR A 206 4266 3325 3810 219 -109 253 C ATOM 1602 OG1 THR A 206 -6.128 -22.021 -5.569 1.00 30.13 O ANISOU 1602 OG1 THR A 206 4340 3250 3859 225 -52 293 O ATOM 1603 CG2 THR A 206 -7.841 -20.446 -4.929 1.00 29.69 C ANISOU 1603 CG2 THR A 206 4225 3282 3773 164 -121 185 C ATOM 1604 N LYS A 207 -6.167 -17.520 -4.657 1.00 29.70 N ANISOU 1604 N LYS A 207 4130 3387 3769 195 -236 103 N ATOM 1605 CA LYS A 207 -6.685 -16.367 -3.921 1.00 30.09 C ANISOU 1605 CA LYS A 207 4144 3492 3796 176 -262 42 C ATOM 1606 C LYS A 207 -8.170 -16.252 -4.210 1.00 29.67 C ANISOU 1606 C LYS A 207 4102 3415 3758 151 -251 7 C ATOM 1607 O LYS A 207 -8.563 -16.165 -5.374 1.00 29.14 O ANISOU 1607 O LYS A 207 4051 3292 3729 140 -249 -8 O ATOM 1608 CB LYS A 207 -5.961 -15.085 -4.337 1.00 30.23 C ANISOU 1608 CB LYS A 207 4143 3510 3833 173 -293 -6 C ATOM 1609 CG LYS A 207 -4.737 -14.796 -3.491 1.00 31.08 C ANISOU 1609 CG LYS A 207 4216 3695 3899 179 -312 4 C ATOM 1610 CD LYS A 207 -5.135 -14.174 -2.157 1.00 31.87 C ANISOU 1610 CD LYS A 207 4286 3877 3946 156 -318 -38 C ATOM 1611 CE LYS A 207 -4.192 -14.589 -1.047 1.00 32.85 C ANISOU 1611 CE LYS A 207 4372 4107 4003 163 -327 6 C ATOM 1612 NZ LYS A 207 -2.793 -14.150 -1.293 1.00 33.22 N ANISOU 1612 NZ LYS A 207 4392 4187 4042 162 -350 9 N ATOM 1613 N SER A 208 -8.990 -16.253 -3.159 1.00 29.74 N ANISOU 1613 N SER A 208 4094 3475 3730 140 -244 -4 N ATOM 1614 CA SER A 208 -10.438 -16.253 -3.327 1.00 29.64 C ANISOU 1614 CA SER A 208 4083 3456 3723 117 -230 -28 C ATOM 1615 C SER A 208 -11.153 -15.374 -2.317 1.00 29.77 C ANISOU 1615 C SER A 208 4068 3532 3711 113 -235 -74 C ATOM 1616 O SER A 208 -10.594 -15.022 -1.280 1.00 30.08 O ANISOU 1616 O SER A 208 4090 3626 3715 118 -243 -83 O ATOM 1617 CB SER A 208 -10.976 -17.682 -3.234 1.00 29.99 C ANISOU 1617 CB SER A 208 4155 3486 3754 101 -194 20 C ATOM 1618 OG SER A 208 -10.826 -18.193 -1.930 1.00 30.71 O ANISOU 1618 OG SER A 208 4238 3631 3799 110 -182 53 O ATOM 1619 N PHE A 209 -12.389 -15.015 -2.652 1.00 29.48 N ANISOU 1619 N PHE A 209 4021 3491 3687 102 -226 -102 N ATOM 1620 CA PHE A 209 -13.294 -14.333 -1.733 1.00 29.70 C ANISOU 1620 CA PHE A 209 4022 3572 3691 101 -218 -139 C ATOM 1621 C PHE A 209 -14.694 -14.916 -1.872 1.00 29.94 C ANISOU 1621 C PHE A 209 4045 3618 3714 82 -198 -128 C ATOM 1622 O PHE A 209 -15.048 -15.470 -2.916 1.00 29.60 O ANISOU 1622 O PHE A 209 4012 3543 3692 65 -193 -108 O ATOM 1623 CB PHE A 209 -13.317 -12.820 -1.998 1.00 29.41 C ANISOU 1623 CB PHE A 209 3971 3519 3683 120 -222 -195 C ATOM 1624 CG PHE A 209 -13.931 -12.439 -3.319 1.00 28.94 C ANISOU 1624 CG PHE A 209 3909 3418 3670 131 -221 -194 C ATOM 1625 CD1 PHE A 209 -15.300 -12.195 -3.427 1.00 28.99 C ANISOU 1625 CD1 PHE A 209 3889 3451 3677 137 -203 -200 C ATOM 1626 CD2 PHE A 209 -13.141 -12.323 -4.459 1.00 28.46 C ANISOU 1626 CD2 PHE A 209 3864 3302 3646 138 -236 -184 C ATOM 1627 CE1 PHE A 209 -15.868 -11.854 -4.649 1.00 28.89 C ANISOU 1627 CE1 PHE A 209 3861 3420 3696 149 -203 -189 C ATOM 1628 CE2 PHE A 209 -13.701 -11.975 -5.680 1.00 28.27 C ANISOU 1628 CE2 PHE A 209 3832 3254 3657 148 -236 -178 C ATOM 1629 CZ PHE A 209 -15.067 -11.740 -5.777 1.00 28.48 C ANISOU 1629 CZ PHE A 209 3826 3315 3679 154 -221 -178 C ATOM 1630 N ASN A 210 -15.474 -14.778 -0.806 1.00 30.58 N ANISOU 1630 N ASN A 210 4104 3756 3759 78 -183 -143 N ATOM 1631 CA ASN A 210 -16.894 -15.096 -0.815 1.00 31.09 C ANISOU 1631 CA ASN A 210 4148 3853 3812 60 -164 -140 C ATOM 1632 C ASN A 210 -17.667 -13.801 -1.026 1.00 31.40 C ANISOU 1632 C ASN A 210 4153 3907 3871 87 -159 -180 C ATOM 1633 O ASN A 210 -17.381 -12.798 -0.366 1.00 31.27 O ANISOU 1633 O ASN A 210 4131 3896 3853 112 -155 -219 O ATOM 1634 CB ASN A 210 -17.300 -15.742 0.510 1.00 31.63 C ANISOU 1634 CB ASN A 210 4212 3979 3828 43 -146 -127 C ATOM 1635 CG ASN A 210 -16.599 -17.066 0.751 1.00 31.81 C ANISOU 1635 CG ASN A 210 4269 3985 3833 26 -138 -72 C ATOM 1636 OD1 ASN A 210 -16.521 -17.911 -0.140 1.00 31.84 O ANISOU 1636 OD1 ASN A 210 4301 3939 3858 6 -128 -42 O ATOM 1637 ND2 ASN A 210 -16.084 -17.251 1.957 1.00 32.25 N ANISOU 1637 ND2 ASN A 210 4322 4083 3846 35 -136 -57 N ATOM 1638 N ARG A 211 -18.625 -13.814 -1.954 1.00 31.86 N ANISOU 1638 N ARG A 211 4188 3972 3945 82 -155 -170 N ATOM 1639 CA ARG A 211 -19.479 -12.649 -2.203 1.00 32.54 C ANISOU 1639 CA ARG A 211 4234 4079 4049 121 -142 -190 C ATOM 1640 C ARG A 211 -20.240 -12.310 -0.921 1.00 33.50 C ANISOU 1640 C ARG A 211 4333 4257 4138 132 -116 -213 C ATOM 1641 O ARG A 211 -20.815 -13.200 -0.286 1.00 33.56 O ANISOU 1641 O ARG A 211 4333 4312 4105 98 -108 -198 O ATOM 1642 CB ARG A 211 -20.463 -12.924 -3.349 1.00 32.61 C ANISOU 1642 CB ARG A 211 4208 4118 4063 108 -143 -161 C ATOM 1643 CG ARG A 211 -21.434 -11.783 -3.656 1.00 32.99 C ANISOU 1643 CG ARG A 211 4204 4203 4127 160 -125 -162 C ATOM 1644 CD ARG A 211 -22.435 -12.138 -4.750 1.00 33.34 C ANISOU 1644 CD ARG A 211 4199 4308 4160 140 -129 -126 C ATOM 1645 NE ARG A 211 -23.013 -13.477 -4.587 1.00 33.54 N ANISOU 1645 NE ARG A 211 4220 4385 4139 64 -130 -114 N ATOM 1646 CZ ARG A 211 -23.918 -13.831 -3.669 1.00 34.20 C ANISOU 1646 CZ ARG A 211 4277 4533 4183 45 -110 -116 C ATOM 1647 NH1 ARG A 211 -24.400 -12.956 -2.789 1.00 34.70 N ANISOU 1647 NH1 ARG A 211 4314 4624 4246 100 -88 -130 N ATOM 1648 NH2 ARG A 211 -24.352 -15.091 -3.626 1.00 34.45 N ANISOU 1648 NH2 ARG A 211 4314 4598 4176 -32 -105 -105 N ATOM 1649 N GLY A 212 -20.213 -11.033 -0.541 1.00 34.31 N ANISOU 1649 N GLY A 212 4430 4347 4259 177 -95 -251 N ATOM 1650 CA GLY A 212 -20.835 -10.564 0.696 1.00 35.38 C ANISOU 1650 CA GLY A 212 4550 4528 4366 189 -62 -284 C ATOM 1651 C GLY A 212 -19.935 -10.588 1.923 1.00 36.11 C ANISOU 1651 C GLY A 212 4671 4624 4423 167 -63 -319 C ATOM 1652 O GLY A 212 -20.323 -10.061 2.967 1.00 36.57 O ANISOU 1652 O GLY A 212 4722 4718 4456 174 -32 -357 O ATOM 1653 N GLU A 213 -18.747 -11.192 1.813 0.99 36.64 N ANISOU 1653 N GLU A 213 4768 4667 4485 141 -96 -305 N ATOM 1654 CA GLU A 213 -17.798 -11.268 2.924 0.99 37.82 C ANISOU 1654 CA GLU A 213 4935 4842 4593 118 -103 -327 C ATOM 1655 C GLU A 213 -16.943 -10.006 2.968 0.99 39.16 C ANISOU 1655 C GLU A 213 5121 4974 4782 128 -95 -385 C ATOM 1656 O GLU A 213 -16.636 -9.410 1.931 0.99 39.05 O ANISOU 1656 O GLU A 213 5119 4895 4822 150 -97 -389 O ATOM 1657 CB GLU A 213 -16.898 -12.499 2.794 1.00 37.46 C ANISOU 1657 CB GLU A 213 4909 4795 4531 94 -134 -273 C ATOM 1658 N CYS A 214 -16.547 -9.614 4.174 1.00 40.87 N ANISOU 1658 N CYS A 214 5341 5237 4952 106 -82 -432 N ATOM 1659 CA CYS A 214 -15.812 -8.377 4.376 1.00 42.51 C ANISOU 1659 CA CYS A 214 5567 5416 5169 98 -62 -503 C ATOM 1660 C CYS A 214 -14.374 -8.482 3.870 1.00 42.07 C ANISOU 1660 C CYS A 214 5526 5336 5121 79 -99 -493 C ATOM 1661 O CYS A 214 -13.625 -9.361 4.291 1.00 42.22 O ANISOU 1661 O CYS A 214 5537 5410 5096 55 -133 -456 O ATOM 1662 CB CYS A 214 -15.817 -7.999 5.855 1.00 44.44 C ANISOU 1662 CB CYS A 214 5806 5732 5347 64 -35 -562 C ATOM 1663 SG CYS A 214 -15.067 -6.392 6.163 1.00 47.18 S ANISOU 1663 SG CYS A 214 6184 6042 5702 36 9 -669 S TER 1664 CYS A 214 ATOM 1665 N AGLN B 1 19.795 14.613 -40.439 0.50 40.51 N ANISOU 1665 N AGLN B 1 5446 3794 6151 -1277 374 -16 N ATOM 1666 N BGLN B 1 20.294 15.862 -42.238 0.50 41.83 N ANISOU 1666 N BGLN B 1 5751 3823 6320 -1353 532 21 N ATOM 1667 CA AGLN B 1 19.068 15.545 -41.351 0.50 40.80 C ANISOU 1667 CA AGLN B 1 5655 3637 6210 -1223 486 44 C ATOM 1668 CA BGLN B 1 19.131 15.508 -41.377 0.50 40.89 C ANISOU 1668 CA BGLN B 1 5658 3657 6220 -1227 482 42 C ATOM 1669 C AGLN B 1 17.942 14.882 -42.140 0.50 39.56 C ANISOU 1669 C AGLN B 1 5490 3447 6095 -1006 441 148 C ATOM 1670 C BGLN B 1 18.006 14.914 -42.218 0.50 39.64 C ANISOU 1670 C BGLN B 1 5501 3457 6104 -1011 446 149 C ATOM 1671 O AGLN B 1 16.894 15.500 -42.351 0.50 39.77 O ANISOU 1671 O AGLN B 1 5650 3329 6131 -911 509 203 O ATOM 1672 O BGLN B 1 17.032 15.600 -42.532 0.50 39.88 O ANISOU 1672 O BGLN B 1 5671 3339 6144 -924 522 204 O ATOM 1673 CB AGLN B 1 20.021 16.191 -42.350 0.50 41.83 C ANISOU 1673 CB AGLN B 1 5814 3756 6323 -1340 568 34 C ATOM 1674 CB BGLN B 1 18.619 16.746 -40.645 0.50 41.88 C ANISOU 1674 CB BGLN B 1 5975 3610 6328 -1295 597 8 C ATOM 1675 CG AGLN B 1 19.262 16.842 -43.492 0.50 41.88 C ANISOU 1675 CG AGLN B 1 5966 3594 6352 -1234 663 121 C ATOM 1676 CG BGLN B 1 17.639 17.572 -41.457 0.50 42.13 C ANISOU 1676 CG BGLN B 1 6186 3444 6378 -1179 708 91 C ATOM 1677 CD AGLN B 1 18.161 17.755 -42.979 0.50 42.32 C ANISOU 1677 CD AGLN B 1 6212 3460 6407 -1178 756 142 C ATOM 1678 CD BGLN B 1 18.171 17.939 -42.830 0.50 42.73 C ANISOU 1678 CD BGLN B 1 6290 3491 6454 -1200 774 131 C ATOM 1679 OE1AGLN B 1 17.555 17.490 -41.937 0.50 41.66 O ANISOU 1679 OE1AGLN B 1 6121 3381 6326 -1136 708 123 O ATOM 1680 OE1BGLN B 1 19.038 17.256 -43.382 0.50 42.40 O ANISOU 1680 OE1BGLN B 1 6102 3593 6415 -1240 706 121 O ATOM 1681 NE2AGLN B 1 17.898 18.835 -43.705 0.50 43.22 N ANISOU 1681 NE2AGLN B 1 6504 3405 6512 -1168 896 185 N ATOM 1682 NE2BGLN B 1 17.650 19.023 -43.392 0.50 43.58 N ANISOU 1682 NE2BGLN B 1 6591 3412 6554 -1161 914 180 N ATOM 1683 N VAL B 2 18.159 13.645 -42.589 1.00 38.50 N ANISOU 1683 N VAL B 2 5203 3451 5973 -928 337 177 N ATOM 1684 CA VAL B 2 17.149 12.917 -43.370 1.00 37.27 C ANISOU 1684 CA VAL B 2 5029 3288 5845 -748 293 265 C ATOM 1685 C VAL B 2 16.014 12.488 -42.444 1.00 36.45 C ANISOU 1685 C VAL B 2 4933 3168 5749 -649 241 275 C ATOM 1686 O VAL B 2 16.256 11.963 -41.359 1.00 36.19 O ANISOU 1686 O VAL B 2 4833 3209 5709 -685 178 222 O ATOM 1687 CB VAL B 2 17.748 11.686 -44.092 1.00 36.62 C ANISOU 1687 CB VAL B 2 4800 3349 5767 -707 210 283 C ATOM 1688 CG1 VAL B 2 16.660 10.874 -44.793 1.00 35.62 C ANISOU 1688 CG1 VAL B 2 4658 3222 5654 -545 164 359 C ATOM 1689 CG2 VAL B 2 18.812 12.127 -45.091 1.00 37.33 C ANISOU 1689 CG2 VAL B 2 4881 3457 5847 -795 265 279 C ATOM 1690 N GLN B 3 14.780 12.714 -42.881 1.00 36.19 N ANISOU 1690 N GLN B 3 4975 3051 5723 -522 269 348 N ATOM 1691 CA GLN B 3 13.614 12.452 -42.049 1.00 35.73 C ANISOU 1691 CA GLN B 3 4934 2975 5666 -430 235 363 C ATOM 1692 C GLN B 3 12.402 12.102 -42.894 1.00 34.79 C ANISOU 1692 C GLN B 3 4814 2860 5545 -274 222 454 C ATOM 1693 O GLN B 3 12.069 12.820 -43.843 1.00 35.04 O ANISOU 1693 O GLN B 3 4920 2827 5567 -221 296 517 O ATOM 1694 CB GLN B 3 13.310 13.676 -41.187 1.00 37.14 C ANISOU 1694 CB GLN B 3 5254 3023 5836 -474 326 336 C ATOM 1695 CG GLN B 3 12.236 13.444 -40.134 1.00 37.17 C ANISOU 1695 CG GLN B 3 5271 3014 5838 -396 292 340 C ATOM 1696 CD GLN B 3 12.292 14.469 -39.013 1.00 38.48 C ANISOU 1696 CD GLN B 3 5558 3073 5991 -482 369 282 C ATOM 1697 OE1 GLN B 3 13.289 14.562 -38.294 1.00 39.27 O ANISOU 1697 OE1 GLN B 3 5635 3205 6080 -631 361 195 O ATOM 1698 NE2 GLN B 3 11.219 15.238 -38.855 1.00 39.12 N ANISOU 1698 NE2 GLN B 3 5765 3036 6062 -387 448 330 N ATOM 1699 N LEU B 4 11.766 10.982 -42.549 1.00 33.34 N ANISOU 1699 N LEU B 4 4545 2761 5360 -205 131 460 N ATOM 1700 CA LEU B 4 10.475 10.604 -43.097 1.00 32.65 C ANISOU 1700 CA LEU B 4 4447 2703 5255 -75 113 534 C ATOM 1701 C LEU B 4 9.444 10.735 -41.979 1.00 32.27 C ANISOU 1701 C LEU B 4 4433 2629 5200 -22 107 533 C ATOM 1702 O LEU B 4 9.443 9.942 -41.037 1.00 31.59 O ANISOU 1702 O LEU B 4 4291 2592 5120 -45 38 485 O ATOM 1703 CB LEU B 4 10.517 9.173 -43.640 1.00 31.78 C ANISOU 1703 CB LEU B 4 4222 2713 5138 -54 25 537 C ATOM 1704 CG LEU B 4 11.546 8.843 -44.730 1.00 31.86 C ANISOU 1704 CG LEU B 4 4188 2765 5154 -97 23 537 C ATOM 1705 CD1 LEU B 4 11.199 7.516 -45.399 1.00 31.19 C ANISOU 1705 CD1 LEU B 4 4024 2777 5048 -50 -41 556 C ATOM 1706 CD2 LEU B 4 11.664 9.943 -45.769 1.00 32.66 C ANISOU 1706 CD2 LEU B 4 4361 2800 5250 -89 109 586 C ATOM 1707 N GLN B 5 8.597 11.760 -42.076 1.00 32.62 N ANISOU 1707 N GLN B 5 4574 2593 5227 55 187 590 N ATOM 1708 CA GLN B 5 7.593 12.060 -41.059 1.00 32.67 C ANISOU 1708 CA GLN B 5 4627 2565 5222 117 201 598 C ATOM 1709 C GLN B 5 6.236 11.586 -41.551 1.00 32.29 C ANISOU 1709 C GLN B 5 4525 2608 5136 252 171 677 C ATOM 1710 O GLN B 5 5.714 12.105 -42.536 1.00 32.97 O ANISOU 1710 O GLN B 5 4638 2698 5192 343 225 759 O ATOM 1711 CB GLN B 5 7.545 13.562 -40.770 1.00 33.79 C ANISOU 1711 CB GLN B 5 4927 2554 5358 123 328 611 C ATOM 1712 N GLN B 6 5.677 10.592 -40.872 1.00 31.51 N ANISOU 1712 N GLN B 6 4348 2595 5032 261 88 653 N ATOM 1713 CA GLN B 6 4.368 10.046 -41.228 1.00 31.44 C ANISOU 1713 CA GLN B 6 4273 2697 4975 363 54 714 C ATOM 1714 C GLN B 6 3.228 10.797 -40.556 1.00 32.38 C ANISOU 1714 C GLN B 6 4448 2789 5067 465 105 761 C ATOM 1715 O GLN B 6 3.432 11.515 -39.572 1.00 32.64 O ANISOU 1715 O GLN B 6 4570 2710 5123 445 153 728 O ATOM 1716 CB GLN B 6 4.288 8.567 -40.856 1.00 30.21 C ANISOU 1716 CB GLN B 6 4016 2644 4818 313 -48 664 C ATOM 1717 CG GLN B 6 5.229 7.699 -41.663 1.00 29.52 C ANISOU 1717 CG GLN B 6 3873 2601 4743 242 -91 635 C ATOM 1718 CD GLN B 6 5.174 6.245 -41.251 1.00 28.57 C ANISOU 1718 CD GLN B 6 3683 2559 4615 200 -171 586 C ATOM 1719 OE1 GLN B 6 6.169 5.685 -40.790 1.00 27.91 O ANISOU 1719 OE1 GLN B 6 3588 2455 4561 132 -201 527 O ATOM 1720 NE2 GLN B 6 4.011 5.622 -41.412 1.00 28.35 N ANISOU 1720 NE2 GLN B 6 3610 2626 4536 239 -198 613 N ATOM 1721 N SER B 7 2.027 10.611 -41.100 1.00 32.98 N ANISOU 1721 N SER B 7 4466 2981 5083 573 98 838 N ATOM 1722 CA SER B 7 0.800 11.107 -40.481 1.00 34.08 C ANISOU 1722 CA SER B 7 4627 3140 5183 688 135 891 C ATOM 1723 C SER B 7 0.505 10.357 -39.179 1.00 33.93 C ANISOU 1723 C SER B 7 4570 3143 5177 637 69 823 C ATOM 1724 O SER B 7 1.078 9.293 -38.910 1.00 33.32 O ANISOU 1724 O SER B 7 4436 3097 5128 531 -11 748 O ATOM 1725 CB SER B 7 -0.383 10.991 -41.454 1.00 34.56 C ANISOU 1725 CB SER B 7 4606 3366 5161 810 134 992 C ATOM 1726 OG SER B 7 -0.317 9.792 -42.210 1.00 33.86 O ANISOU 1726 OG SER B 7 4401 3414 5051 740 48 969 O ATOM 1727 N GLY B 8 -0.396 10.923 -38.378 1.00 34.91 N ANISOU 1727 N GLY B 8 4734 3250 5278 725 111 854 N ATOM 1728 CA GLY B 8 -0.716 10.389 -37.053 1.00 34.70 C ANISOU 1728 CA GLY B 8 4690 3230 5263 687 64 794 C ATOM 1729 C GLY B 8 -1.574 9.137 -37.073 1.00 34.47 C ANISOU 1729 C GLY B 8 4532 3375 5190 680 -23 793 C ATOM 1730 O GLY B 8 -1.791 8.532 -38.129 1.00 34.43 O ANISOU 1730 O GLY B 8 4443 3491 5146 677 -58 822 O ATOM 1731 N ALA B 9 -2.062 8.758 -35.890 1.00 34.47 N ANISOU 1731 N ALA B 9 4522 3384 5189 668 -52 755 N ATOM 1732 CA ALA B 9 -2.910 7.573 -35.717 1.00 34.27 C ANISOU 1732 CA ALA B 9 4390 3511 5118 644 -124 742 C ATOM 1733 C ALA B 9 -4.237 7.716 -36.460 1.00 35.14 C ANISOU 1733 C ALA B 9 4421 3790 5139 752 -107 836 C ATOM 1734 O ALA B 9 -4.765 8.822 -36.593 1.00 36.10 O ANISOU 1734 O ALA B 9 4581 3900 5233 882 -32 916 O ATOM 1735 CB ALA B 9 -3.161 7.307 -34.240 1.00 33.91 C ANISOU 1735 CB ALA B 9 4366 3428 5090 618 -144 688 C ATOM 1736 N GLU B 10 -4.753 6.589 -36.945 1.00 35.10 N ANISOU 1736 N GLU B 10 4308 3947 5079 695 -169 825 N ATOM 1737 CA GLU B 10 -5.981 6.546 -37.738 1.00 35.96 C ANISOU 1737 CA GLU B 10 4313 4266 5085 768 -166 905 C ATOM 1738 C GLU B 10 -6.977 5.618 -37.065 1.00 35.71 C ANISOU 1738 C GLU B 10 4198 4374 4995 720 -213 874 C ATOM 1739 O GLU B 10 -6.638 4.477 -36.734 1.00 34.79 O ANISOU 1739 O GLU B 10 4075 4246 4896 587 -266 789 O ATOM 1740 CB GLU B 10 -5.700 6.015 -39.145 1.00 36.24 C ANISOU 1740 CB GLU B 10 4288 4397 5085 714 -192 914 C ATOM 1741 CG GLU B 10 -4.703 6.828 -39.959 1.00 36.48 C ANISOU 1741 CG GLU B 10 4391 4306 5165 749 -148 944 C ATOM 1742 CD GLU B 10 -5.244 8.158 -40.446 1.00 37.89 C ANISOU 1742 CD GLU B 10 4591 4505 5302 919 -67 1059 C ATOM 1743 OE1 GLU B 10 -6.476 8.385 -40.404 1.00 38.96 O ANISOU 1743 OE1 GLU B 10 4657 4795 5352 1025 -50 1132 O ATOM 1744 OE2 GLU B 10 -4.421 8.980 -40.896 1.00 38.20 O ANISOU 1744 OE2 GLU B 10 4720 4408 5388 951 -12 1081 O ATOM 1745 N LEU B 11 -8.196 6.120 -36.871 1.00 36.36 N ANISOU 1745 N LEU B 11 4224 4588 5002 834 -183 948 N ATOM 1746 CA LEU B 11 -9.331 5.325 -36.411 1.00 36.43 C ANISOU 1746 CA LEU B 11 4131 4779 4931 795 -220 935 C ATOM 1747 C LEU B 11 -10.384 5.382 -37.508 1.00 37.06 C ANISOU 1747 C LEU B 11 4075 5123 4882 857 -216 1022 C ATOM 1748 O LEU B 11 -10.964 6.436 -37.750 1.00 37.96 O ANISOU 1748 O LEU B 11 4171 5300 4951 1028 -159 1128 O ATOM 1749 CB LEU B 11 -9.886 5.892 -35.108 1.00 36.99 C ANISOU 1749 CB LEU B 11 4240 4799 5015 881 -188 948 C ATOM 1750 CG LEU B 11 -8.855 6.055 -33.992 1.00 36.36 C ANISOU 1750 CG LEU B 11 4296 4468 5053 835 -183 871 C ATOM 1751 CD1 LEU B 11 -9.438 6.903 -32.881 1.00 36.99 C ANISOU 1751 CD1 LEU B 11 4424 4494 5135 948 -131 903 C ATOM 1752 CD2 LEU B 11 -8.385 4.704 -33.473 1.00 35.47 C ANISOU 1752 CD2 LEU B 11 4181 4325 4970 667 -252 763 C ATOM 1753 N VAL B 12 -10.621 4.247 -38.162 1.00 36.68 N ANISOU 1753 N VAL B 12 3936 5232 4767 720 -269 979 N ATOM 1754 CA VAL B 12 -11.397 4.182 -39.403 1.00 37.48 C ANISOU 1754 CA VAL B 12 3905 5596 4741 741 -274 1046 C ATOM 1755 C VAL B 12 -12.362 2.998 -39.404 1.00 37.64 C ANISOU 1755 C VAL B 12 3801 5853 4646 598 -320 998 C ATOM 1756 O VAL B 12 -12.094 1.971 -38.780 1.00 36.72 O ANISOU 1756 O VAL B 12 3729 5659 4563 442 -351 893 O ATOM 1757 CB VAL B 12 -10.467 4.087 -40.638 1.00 37.32 C ANISOU 1757 CB VAL B 12 3912 5523 4744 694 -280 1041 C ATOM 1758 CG1 VAL B 12 -9.764 5.415 -40.879 1.00 37.46 C ANISOU 1758 CG1 VAL B 12 4026 5370 4836 850 -220 1113 C ATOM 1759 CG2 VAL B 12 -9.437 2.973 -40.482 1.00 36.22 C ANISOU 1759 CG2 VAL B 12 3850 5229 4682 510 -320 918 C ATOM 1760 N ARG B 13 -13.471 3.145 -40.124 1.00 38.75 N ANISOU 1760 N ARG B 13 3791 6291 4642 649 -318 1075 N ATOM 1761 CA ARG B 13 -14.533 2.134 -40.144 1.00 39.44 C ANISOU 1761 CA ARG B 13 3743 6648 4594 509 -353 1035 C ATOM 1762 C ARG B 13 -14.262 1.020 -41.161 1.00 39.04 C ANISOU 1762 C ARG B 13 3665 6683 4486 305 -387 959 C ATOM 1763 O ARG B 13 -13.609 1.264 -42.177 1.00 38.86 O ANISOU 1763 O ARG B 13 3664 6621 4480 327 -383 983 O ATOM 1764 CB ARG B 13 -15.885 2.789 -40.442 1.00 41.34 C ANISOU 1764 CB ARG B 13 3812 7209 4685 653 -335 1154 C ATOM 1765 CG ARG B 13 -16.326 3.780 -39.378 1.00 41.90 C ANISOU 1765 CG ARG B 13 3909 7219 4791 850 -291 1228 C ATOM 1766 CD ARG B 13 -17.678 4.398 -39.701 1.00 43.90 C ANISOU 1766 CD ARG B 13 3986 7811 4883 1012 -266 1358 C ATOM 1767 NE ARG B 13 -18.772 3.425 -39.641 1.00 44.98 N ANISOU 1767 NE ARG B 13 3955 8263 4873 861 -308 1316 N ATOM 1768 CZ ARG B 13 -19.311 2.924 -38.524 1.00 44.98 C ANISOU 1768 CZ ARG B 13 3941 8281 4867 784 -318 1257 C ATOM 1769 NH1 ARG B 13 -18.873 3.282 -37.316 1.00 44.13 N ANISOU 1769 NH1 ARG B 13 3977 7895 4895 848 -294 1233 N ATOM 1770 NH2 ARG B 13 -20.310 2.046 -38.614 1.00 46.07 N ANISOU 1770 NH2 ARG B 13 3921 8727 4855 629 -351 1219 N ATOM 1771 N PRO B 14 -14.762 -0.207 -40.891 1.00 38.87 N ANISOU 1771 N PRO B 14 3606 6771 4391 102 -412 863 N ATOM 1772 CA PRO B 14 -14.627 -1.282 -41.881 1.00 38.99 C ANISOU 1772 CA PRO B 14 3603 6883 4328 -102 -429 788 C ATOM 1773 C PRO B 14 -15.442 -1.008 -43.146 1.00 40.20 C ANISOU 1773 C PRO B 14 3582 7375 4317 -80 -436 865 C ATOM 1774 O PRO B 14 -16.521 -0.427 -43.065 1.00 41.34 O ANISOU 1774 O PRO B 14 3581 7769 4356 30 -434 952 O ATOM 1775 CB PRO B 14 -15.149 -2.525 -41.142 1.00 39.09 C ANISOU 1775 CB PRO B 14 3624 6942 4287 -310 -435 678 C ATOM 1776 CG PRO B 14 -15.996 -2.001 -40.041 1.00 39.43 C ANISOU 1776 CG PRO B 14 3607 7054 4319 -202 -431 724 C ATOM 1777 CD PRO B 14 -15.393 -0.687 -39.647 1.00 38.82 C ANISOU 1777 CD PRO B 14 3598 6778 4375 40 -415 812 C ATOM 1778 N GLY B 15 -14.907 -1.402 -44.298 1.00 40.03 N ANISOU 1778 N GLY B 15 3575 7366 4269 -173 -442 838 N ATOM 1779 CA GLY B 15 -15.522 -1.117 -45.592 1.00 41.36 C ANISOU 1779 CA GLY B 15 3587 7844 4285 -150 -449 911 C ATOM 1780 C GLY B 15 -15.122 0.210 -46.228 1.00 41.38 C ANISOU 1780 C GLY B 15 3585 7804 4333 95 -431 1043 C ATOM 1781 O GLY B 15 -15.344 0.396 -47.423 1.00 42.54 O ANISOU 1781 O GLY B 15 3633 8157 4373 113 -435 1100 O ATOM 1782 N THR B 16 -14.542 1.129 -45.450 1.00 40.35 N ANISOU 1782 N THR B 16 3566 7412 4352 276 -405 1092 N ATOM 1783 CA THR B 16 -14.135 2.445 -45.950 1.00 40.37 C ANISOU 1783 CA THR B 16 3596 7338 4404 507 -368 1214 C ATOM 1784 C THR B 16 -12.682 2.418 -46.426 1.00 39.15 C ANISOU 1784 C THR B 16 3594 6897 4384 469 -362 1168 C ATOM 1785 O THR B 16 -11.991 1.405 -46.274 1.00 38.17 O ANISOU 1785 O THR B 16 3554 6628 4320 284 -384 1048 O ATOM 1786 CB THR B 16 -14.291 3.539 -44.869 1.00 40.22 C ANISOU 1786 CB THR B 16 3632 7186 4464 719 -326 1291 C ATOM 1787 OG1 THR B 16 -13.360 3.310 -43.803 1.00 38.71 O ANISOU 1787 OG1 THR B 16 3607 6661 4440 657 -326 1197 O ATOM 1788 CG2 THR B 16 -15.712 3.555 -44.318 1.00 41.36 C ANISOU 1788 CG2 THR B 16 3627 7610 4479 767 -329 1337 C ATOM 1789 N SER B 17 -12.255 3.534 -47.017 1.00 39.31 N ANISOU 1789 N SER B 17 3648 6847 4441 649 -323 1270 N ATOM 1790 CA ASER B 17 -10.884 3.718 -47.479 0.39 38.37 C ANISOU 1790 CA ASER B 17 3666 6467 4447 638 -308 1244 C ATOM 1791 CA BSER B 17 -10.881 3.718 -47.479 0.61 38.39 C ANISOU 1791 CA BSER B 17 3669 6468 4450 638 -308 1244 C ATOM 1792 C SER B 17 -10.180 4.784 -46.645 1.00 37.75 C ANISOU 1792 C SER B 17 3729 6099 4515 788 -259 1278 C ATOM 1793 O SER B 17 -10.824 5.681 -46.102 1.00 38.35 O ANISOU 1793 O SER B 17 3793 6207 4573 956 -219 1364 O ATOM 1794 CB ASER B 17 -10.879 4.119 -48.953 0.39 39.23 C ANISOU 1794 CB ASER B 17 3710 6724 4470 700 -295 1326 C ATOM 1795 CB BSER B 17 -10.857 4.110 -48.959 0.61 39.24 C ANISOU 1795 CB BSER B 17 3714 6722 4473 698 -295 1324 C ATOM 1796 OG ASER B 17 -11.477 3.110 -49.750 0.39 39.87 O ANISOU 1796 OG ASER B 17 3665 7075 4407 539 -339 1283 O ATOM 1797 OG BSER B 17 -11.531 5.335 -49.186 0.61 40.46 O ANISOU 1797 OG BSER B 17 3811 7000 4563 933 -247 1474 O ATOM 1798 N VAL B 18 -8.857 4.671 -46.546 1.00 36.53 N ANISOU 1798 N VAL B 18 3712 5672 4497 721 -256 1209 N ATOM 1799 CA VAL B 18 -8.031 5.654 -45.838 1.00 36.06 C ANISOU 1799 CA VAL B 18 3794 5336 4572 826 -207 1225 C ATOM 1800 C VAL B 18 -6.689 5.806 -46.549 1.00 35.34 C ANISOU 1800 C VAL B 18 3798 5063 4568 789 -192 1201 C ATOM 1801 O VAL B 18 -6.164 4.838 -47.098 1.00 34.98 O ANISOU 1801 O VAL B 18 3742 5025 4523 644 -233 1128 O ATOM 1802 CB VAL B 18 -7.819 5.264 -44.355 1.00 35.24 C ANISOU 1802 CB VAL B 18 3759 5073 4557 758 -225 1136 C ATOM 1803 CG1 VAL B 18 -6.934 4.026 -44.216 1.00 34.16 C ANISOU 1803 CG1 VAL B 18 3668 4829 4482 565 -274 1010 C ATOM 1804 CG2 VAL B 18 -7.243 6.431 -43.559 1.00 35.10 C ANISOU 1804 CG2 VAL B 18 3871 4820 4645 877 -165 1164 C ATOM 1805 N LYS B 19 -6.151 7.022 -46.530 1.00 35.38 N ANISOU 1805 N LYS B 19 3902 4904 4639 919 -126 1263 N ATOM 1806 CA LYS B 19 -4.861 7.333 -47.135 1.00 34.96 C ANISOU 1806 CA LYS B 19 3943 4671 4668 891 -101 1247 C ATOM 1807 C LYS B 19 -3.941 7.904 -46.061 1.00 34.07 C ANISOU 1807 C LYS B 19 3970 4290 4685 890 -66 1199 C ATOM 1808 O LYS B 19 -4.236 8.954 -45.488 1.00 34.78 O ANISOU 1808 O LYS B 19 4125 4304 4788 1015 -1 1257 O ATOM 1809 CB LYS B 19 -5.043 8.336 -48.277 1.00 36.29 C ANISOU 1809 CB LYS B 19 4107 4905 4776 1038 -39 1369 C ATOM 1810 CG LYS B 19 -3.771 8.645 -49.056 1.00 36.24 C ANISOU 1810 CG LYS B 19 4188 4739 4841 1004 -10 1357 C ATOM 1811 CD LYS B 19 -4.052 9.495 -50.290 1.00 37.53 C ANISOU 1811 CD LYS B 19 4337 4997 4926 1144 50 1481 C ATOM 1812 CE LYS B 19 -4.567 8.662 -51.455 1.00 38.04 C ANISOU 1812 CE LYS B 19 4260 5318 4874 1091 -7 1495 C ATOM 1813 NZ LYS B 19 -4.694 9.466 -52.702 1.00 39.29 N ANISOU 1813 NZ LYS B 19 4407 5563 4958 1224 49 1615 N ATOM 1814 N VAL B 20 -2.843 7.198 -45.787 1.00 32.57 N ANISOU 1814 N VAL B 20 3827 3969 4582 748 -104 1096 N ATOM 1815 CA VAL B 20 -1.813 7.655 -44.840 1.00 31.76 C ANISOU 1815 CA VAL B 20 3840 3634 4592 719 -79 1040 C ATOM 1816 C VAL B 20 -0.604 8.188 -45.610 1.00 31.36 C ANISOU 1816 C VAL B 20 3862 3458 4596 702 -40 1043 C ATOM 1817 O VAL B 20 -0.334 7.740 -46.721 1.00 31.34 O ANISOU 1817 O VAL B 20 3815 3528 4566 664 -59 1050 O ATOM 1818 CB VAL B 20 -1.397 6.542 -43.848 1.00 30.86 C ANISOU 1818 CB VAL B 20 3724 3474 4529 588 -144 929 C ATOM 1819 CG1 VAL B 20 -2.628 5.926 -43.195 1.00 31.00 C ANISOU 1819 CG1 VAL B 20 3668 3629 4483 590 -181 924 C ATOM 1820 CG2 VAL B 20 -0.542 5.464 -44.512 1.00 30.34 C ANISOU 1820 CG2 VAL B 20 3637 3414 4479 466 -189 865 C ATOM 1821 N SER B 21 0.112 9.142 -45.017 1.00 31.02 N ANISOU 1821 N SER B 21 3931 3230 4624 719 20 1034 N ATOM 1822 CA SER B 21 1.175 9.870 -45.718 1.00 30.95 C ANISOU 1822 CA SER B 21 4001 3100 4658 708 77 1045 C ATOM 1823 C SER B 21 2.567 9.643 -45.128 1.00 29.91 C ANISOU 1823 C SER B 21 3920 2827 4616 576 60 944 C ATOM 1824 O SER B 21 2.712 9.192 -43.989 1.00 29.26 O ANISOU 1824 O SER B 21 3837 2710 4569 516 20 874 O ATOM 1825 CB SER B 21 0.862 11.366 -45.731 1.00 32.06 C ANISOU 1825 CB SER B 21 4248 3148 4785 840 190 1131 C ATOM 1826 OG SER B 21 0.779 11.882 -44.417 1.00 32.23 O ANISOU 1826 OG SER B 21 4350 3053 4843 848 223 1100 O ATOM 1827 N CYS B 22 3.577 9.960 -45.935 1.00 29.63 N ANISOU 1827 N CYS B 22 3921 2729 4609 535 91 943 N ATOM 1828 CA CYS B 22 4.978 9.927 -45.530 1.00 29.00 C ANISOU 1828 CA CYS B 22 3882 2536 4601 417 89 860 C ATOM 1829 C CYS B 22 5.687 11.116 -46.182 1.00 29.63 C ANISOU 1829 C CYS B 22 4058 2505 4697 423 184 894 C ATOM 1830 O CYS B 22 5.938 11.104 -47.389 1.00 29.81 O ANISOU 1830 O CYS B 22 4062 2565 4700 435 196 933 O ATOM 1831 CB CYS B 22 5.610 8.598 -45.953 1.00 28.13 C ANISOU 1831 CB CYS B 22 3684 2504 4499 328 8 805 C ATOM 1832 SG CYS B 22 7.373 8.426 -45.598 1.00 27.85 S ANISOU 1832 SG CYS B 22 3666 2382 4534 200 0 717 S ATOM 1833 N LYS B 23 5.971 12.149 -45.387 1.00 30.00 N ANISOU 1833 N LYS B 23 4217 2412 4772 411 258 877 N ATOM 1834 CA LYS B 23 6.598 13.379 -45.880 1.00 30.76 C ANISOU 1834 CA LYS B 23 4434 2377 4876 405 371 903 C ATOM 1835 C LYS B 23 8.112 13.290 -45.725 1.00 30.42 C ANISOU 1835 C LYS B 23 4398 2278 4884 244 362 811 C ATOM 1836 O LYS B 23 8.608 13.133 -44.607 1.00 30.16 O ANISOU 1836 O LYS B 23 4365 2213 4882 151 335 729 O ATOM 1837 CB LYS B 23 6.078 14.595 -45.113 1.00 31.72 C ANISOU 1837 CB LYS B 23 4697 2368 4988 470 477 930 C ATOM 1838 N ALA B 24 8.830 13.403 -46.844 1.00 30.37 N ANISOU 1838 N ALA B 24 4390 2272 4879 213 387 829 N ATOM 1839 CA ALA B 24 10.294 13.288 -46.877 1.00 30.14 C ANISOU 1839 CA ALA B 24 4346 2221 4887 64 380 751 C ATOM 1840 C ALA B 24 10.964 14.661 -46.839 1.00 31.06 C ANISOU 1840 C ALA B 24 4608 2186 5009 -4 507 739 C ATOM 1841 O ALA B 24 10.488 15.600 -47.467 1.00 31.98 O ANISOU 1841 O ALA B 24 4832 2221 5098 81 608 816 O ATOM 1842 CB ALA B 24 10.726 12.544 -48.129 1.00 29.71 C ANISOU 1842 CB ALA B 24 4202 2261 4825 61 336 772 C ATOM 1843 N SER B 25 12.074 14.762 -46.113 1.00 31.00 N ANISOU 1843 N SER B 25 4604 2149 5026 -158 507 644 N ATOM 1844 CA SER B 25 12.869 15.991 -46.067 1.00 32.06 C ANISOU 1844 CA SER B 25 4873 2150 5158 -269 629 612 C ATOM 1845 C SER B 25 14.348 15.693 -45.825 1.00 31.93 C ANISOU 1845 C SER B 25 4783 2192 5156 -451 594 514 C ATOM 1846 O SER B 25 14.712 14.602 -45.369 1.00 31.03 O ANISOU 1846 O SER B 25 4527 2206 5056 -482 480 468 O ATOM 1847 CB SER B 25 12.336 16.938 -44.988 1.00 32.82 C ANISOU 1847 CB SER B 25 5113 2114 5243 -269 714 595 C ATOM 1848 OG SER B 25 12.482 16.378 -43.698 1.00 32.34 O ANISOU 1848 OG SER B 25 4984 2107 5197 -340 634 513 O ATOM 1849 N GLY B 26 15.188 16.671 -46.151 1.00 32.85 N ANISOU 1849 N GLY B 26 4999 2221 5263 -569 701 488 N ATOM 1850 CA GLY B 26 16.637 16.561 -45.987 1.00 33.11 C ANISOU 1850 CA GLY B 26 4962 2323 5295 -755 686 397 C ATOM 1851 C GLY B 26 17.389 15.897 -47.129 1.00 32.65 C ANISOU 1851 C GLY B 26 4788 2375 5243 -762 640 417 C ATOM 1852 O GLY B 26 18.572 15.584 -46.983 1.00 32.83 O ANISOU 1852 O GLY B 26 4715 2498 5260 -894 607 349 O ATOM 1853 N TYR B 27 16.717 15.683 -48.261 1.00 32.18 N ANISOU 1853 N TYR B 27 4730 2309 5186 -619 639 510 N ATOM 1854 CA TYR B 27 17.340 15.092 -49.452 1.00 31.89 C ANISOU 1854 CA TYR B 27 4601 2364 5152 -615 606 536 C ATOM 1855 C TYR B 27 16.448 15.297 -50.677 1.00 31.84 C ANISOU 1855 C TYR B 27 4651 2313 5133 -466 646 643 C ATOM 1856 O TYR B 27 15.309 15.746 -50.551 1.00 32.00 O ANISOU 1856 O TYR B 27 4758 2260 5141 -351 683 703 O ATOM 1857 CB TYR B 27 17.614 13.586 -49.252 1.00 30.77 C ANISOU 1857 CB TYR B 27 4279 2389 5023 -593 467 509 C ATOM 1858 CG TYR B 27 16.372 12.721 -49.261 1.00 29.77 C ANISOU 1858 CG TYR B 27 4111 2301 4898 -438 390 563 C ATOM 1859 CD1 TYR B 27 15.583 12.582 -48.120 1.00 29.41 C ANISOU 1859 CD1 TYR B 27 4077 2241 4857 -400 354 546 C ATOM 1860 CD2 TYR B 27 15.983 12.042 -50.415 1.00 29.22 C ANISOU 1860 CD2 TYR B 27 3992 2292 4820 -342 356 625 C ATOM 1861 CE1 TYR B 27 14.444 11.792 -48.129 1.00 28.54 C ANISOU 1861 CE1 TYR B 27 3925 2177 4740 -275 289 590 C ATOM 1862 CE2 TYR B 27 14.847 11.250 -50.436 1.00 28.45 C ANISOU 1862 CE2 TYR B 27 3854 2244 4710 -226 292 665 C ATOM 1863 CZ TYR B 27 14.080 11.129 -49.291 1.00 28.13 C ANISOU 1863 CZ TYR B 27 3823 2192 4674 -195 258 648 C ATOM 1864 OH TYR B 27 12.956 10.347 -49.313 1.00 27.45 O ANISOU 1864 OH TYR B 27 3694 2167 4569 -95 198 683 O ATOM 1865 N ALA B 28 16.970 14.953 -51.852 1.00 31.72 N ANISOU 1865 N ALA B 28 4579 2358 5114 -464 638 672 N ATOM 1866 CA ALA B 28 16.218 15.072 -53.106 1.00 31.75 C ANISOU 1866 CA ALA B 28 4619 2350 5096 -329 668 774 C ATOM 1867 C ALA B 28 15.201 13.933 -53.208 1.00 30.59 C ANISOU 1867 C ALA B 28 4368 2314 4940 -200 559 813 C ATOM 1868 O ALA B 28 15.564 12.792 -53.500 1.00 29.75 O ANISOU 1868 O ALA B 28 4140 2325 4840 -211 470 790 O ATOM 1869 CB ALA B 28 17.162 15.063 -54.302 1.00 32.11 C ANISOU 1869 CB ALA B 28 4638 2426 5136 -383 696 783 C ATOM 1870 N PHE B 29 13.931 14.275 -52.978 1.00 30.61 N ANISOU 1870 N PHE B 29 4428 2282 4920 -79 577 873 N ATOM 1871 CA PHE B 29 12.821 13.319 -52.863 1.00 29.73 C ANISOU 1871 CA PHE B 29 4228 2277 4790 28 484 903 C ATOM 1872 C PHE B 29 12.696 12.348 -54.039 1.00 29.17 C ANISOU 1872 C PHE B 29 4057 2333 4692 72 421 938 C ATOM 1873 O PHE B 29 12.480 11.153 -53.832 1.00 28.12 O ANISOU 1873 O PHE B 29 3824 2303 4557 71 326 907 O ATOM 1874 CB PHE B 29 11.506 14.089 -52.674 1.00 30.25 C ANISOU 1874 CB PHE B 29 4380 2293 4821 162 540 982 C ATOM 1875 CG PHE B 29 10.291 13.214 -52.509 1.00 29.60 C ANISOU 1875 CG PHE B 29 4205 2334 4706 262 452 1013 C ATOM 1876 CD1 PHE B 29 10.248 12.232 -51.520 1.00 28.72 C ANISOU 1876 CD1 PHE B 29 4012 2281 4620 212 356 940 C ATOM 1877 CD2 PHE B 29 9.179 13.382 -53.331 1.00 30.02 C ANISOU 1877 CD2 PHE B 29 4253 2458 4696 404 471 1116 C ATOM 1878 CE1 PHE B 29 9.123 11.434 -51.358 1.00 28.21 C ANISOU 1878 CE1 PHE B 29 3871 2328 4520 287 285 963 C ATOM 1879 CE2 PHE B 29 8.049 12.592 -53.169 1.00 29.54 C ANISOU 1879 CE2 PHE B 29 4100 2532 4594 477 393 1139 C ATOM 1880 CZ PHE B 29 8.022 11.615 -52.185 1.00 28.64 C ANISOU 1880 CZ PHE B 29 3913 2461 4508 410 302 1058 C ATOM 1881 N THR B 30 12.867 12.861 -55.257 1.00 29.76 N ANISOU 1881 N THR B 30 4170 2394 4741 102 484 999 N ATOM 1882 CA THR B 30 12.701 12.056 -56.476 1.00 29.47 C ANISOU 1882 CA THR B 30 4052 2477 4668 143 438 1037 C ATOM 1883 C THR B 30 13.848 11.069 -56.769 1.00 28.86 C ANISOU 1883 C THR B 30 3889 2458 4618 42 382 969 C ATOM 1884 O THR B 30 13.710 10.226 -57.658 1.00 28.51 O ANISOU 1884 O THR B 30 3779 2512 4541 65 339 986 O ATOM 1885 CB THR B 30 12.492 12.949 -57.724 1.00 30.43 C ANISOU 1885 CB THR B 30 4244 2573 4745 220 527 1133 C ATOM 1886 OG1 THR B 30 13.613 13.821 -57.890 1.00 31.20 O ANISOU 1886 OG1 THR B 30 4428 2552 4875 134 616 1113 O ATOM 1887 CG2 THR B 30 11.223 13.781 -57.592 1.00 31.13 C ANISOU 1887 CG2 THR B 30 4404 2636 4787 361 583 1224 C ATOM 1888 N ASN B 31 14.966 11.175 -56.044 1.00 28.81 N ANISOU 1888 N ASN B 31 3885 2402 4660 -68 389 894 N ATOM 1889 CA ASN B 31 16.134 10.324 -56.285 1.00 28.41 C ANISOU 1889 CA ASN B 31 3751 2416 4628 -148 348 838 C ATOM 1890 C ASN B 31 16.057 8.948 -55.635 1.00 27.41 C ANISOU 1890 C ASN B 31 3533 2376 4507 -147 252 788 C ATOM 1891 O ASN B 31 16.763 8.042 -56.071 1.00 27.12 O ANISOU 1891 O ASN B 31 3430 2406 4467 -170 220 764 O ATOM 1892 CB ASN B 31 17.424 11.024 -55.835 1.00 29.08 C ANISOU 1892 CB ASN B 31 3860 2445 4746 -270 400 782 C ATOM 1893 CG ASN B 31 17.822 12.175 -56.750 1.00 30.13 C ANISOU 1893 CG ASN B 31 4081 2498 4868 -297 506 823 C ATOM 1894 OD1 ASN B 31 17.117 12.507 -57.705 1.00 30.51 O ANISOU 1894 OD1 ASN B 31 4177 2528 4885 -208 543 901 O ATOM 1895 ND2 ASN B 31 18.961 12.789 -56.458 1.00 30.76 N ANISOU 1895 ND2 ASN B 31 4182 2540 4966 -424 559 770 N ATOM 1896 N TYR B 32 15.215 8.790 -54.612 1.00 26.93 N ANISOU 1896 N TYR B 32 3477 2308 4449 -114 214 776 N ATOM 1897 CA TYR B 32 15.160 7.557 -53.827 1.00 26.15 C ANISOU 1897 CA TYR B 32 3309 2272 4354 -117 134 726 C ATOM 1898 C TYR B 32 13.769 6.926 -53.846 1.00 25.69 C ANISOU 1898 C TYR B 32 3241 2263 4258 -42 91 755 C ATOM 1899 O TYR B 32 12.751 7.628 -53.788 1.00 25.81 O ANISOU 1899 O TYR B 32 3298 2255 4254 15 113 801 O ATOM 1900 CB TYR B 32 15.564 7.841 -52.378 1.00 26.11 C ANISOU 1900 CB TYR B 32 3308 2229 4384 -171 125 668 C ATOM 1901 CG TYR B 32 17.005 8.276 -52.207 1.00 26.61 C ANISOU 1901 CG TYR B 32 3355 2286 4470 -270 156 624 C ATOM 1902 CD1 TYR B 32 17.392 9.598 -52.445 1.00 27.47 C ANISOU 1902 CD1 TYR B 32 3536 2315 4586 -328 239 632 C ATOM 1903 CD2 TYR B 32 17.981 7.372 -51.793 1.00 26.40 C ANISOU 1903 CD2 TYR B 32 3242 2341 4448 -307 111 575 C ATOM 1904 CE1 TYR B 32 18.713 10.002 -52.285 1.00 28.07 C ANISOU 1904 CE1 TYR B 32 3591 2403 4672 -442 271 584 C ATOM 1905 CE2 TYR B 32 19.300 7.764 -51.628 1.00 27.01 C ANISOU 1905 CE2 TYR B 32 3283 2448 4532 -400 138 536 C ATOM 1906 CZ TYR B 32 19.661 9.077 -51.870 1.00 27.85 C ANISOU 1906 CZ TYR B 32 3454 2485 4644 -479 214 535 C ATOM 1907 OH TYR B 32 20.968 9.461 -51.705 1.00 28.58 O ANISOU 1907 OH TYR B 32 3504 2624 4732 -594 243 489 O ATOM 1908 N LEU B 33 13.738 5.598 -53.899 1.00 25.13 N ANISOU 1908 N LEU B 33 3118 2261 4168 -42 37 727 N ATOM 1909 CA LEU B 33 12.486 4.853 -53.814 1.00 24.77 C ANISOU 1909 CA LEU B 33 3060 2274 4079 -1 -4 736 C ATOM 1910 C LEU B 33 11.975 4.899 -52.376 1.00 24.52 C ANISOU 1910 C LEU B 33 3035 2213 4068 5 -33 707 C ATOM 1911 O LEU B 33 12.772 4.833 -51.433 1.00 24.17 O ANISOU 1911 O LEU B 33 2985 2133 4065 -33 -43 659 O ATOM 1912 CB LEU B 33 12.680 3.395 -54.249 1.00 24.40 C ANISOU 1912 CB LEU B 33 2980 2289 4001 -20 -35 705 C ATOM 1913 CG LEU B 33 13.300 3.138 -55.625 1.00 24.60 C ANISOU 1913 CG LEU B 33 2999 2345 4004 -33 -8 722 C ATOM 1914 CD1 LEU B 33 13.460 1.644 -55.845 1.00 24.35 C ANISOU 1914 CD1 LEU B 33 2959 2356 3938 -51 -26 683 C ATOM 1915 CD2 LEU B 33 12.472 3.760 -56.738 1.00 25.03 C ANISOU 1915 CD2 LEU B 33 3061 2441 4008 1 15 786 C ATOM 1916 N ILE B 34 10.656 5.040 -52.224 1.00 24.66 N ANISOU 1916 N ILE B 34 3059 2262 4050 54 -44 740 N ATOM 1917 CA ILE B 34 9.994 4.983 -50.916 1.00 24.54 C ANISOU 1917 CA ILE B 34 3048 2231 4045 66 -73 717 C ATOM 1918 C ILE B 34 9.367 3.598 -50.743 1.00 24.21 C ANISOU 1918 C ILE B 34 2971 2265 3962 54 -124 686 C ATOM 1919 O ILE B 34 8.732 3.080 -51.658 1.00 24.32 O ANISOU 1919 O ILE B 34 2964 2360 3915 58 -130 708 O ATOM 1920 CB ILE B 34 8.918 6.084 -50.761 1.00 24.99 C ANISOU 1920 CB ILE B 34 3137 2275 4083 136 -42 776 C ATOM 1921 CG1 ILE B 34 9.560 7.481 -50.768 1.00 25.59 C ANISOU 1921 CG1 ILE B 34 3281 2244 4198 140 29 798 C ATOM 1922 CG2 ILE B 34 8.091 5.881 -49.489 1.00 24.73 C ANISOU 1922 CG2 ILE B 34 3102 2246 4050 153 -74 754 C ATOM 1923 CD1 ILE B 34 10.340 7.849 -49.519 1.00 25.57 C ANISOU 1923 CD1 ILE B 34 3311 2152 4252 80 35 737 C ATOM 1924 N GLU B 35 9.541 3.041 -49.547 1.00 24.01 N ANISOU 1924 N GLU B 35 2946 2213 3963 33 -154 634 N ATOM 1925 CA GLU B 35 9.132 1.684 -49.189 1.00 23.77 C ANISOU 1925 CA GLU B 35 2906 2226 3899 12 -190 595 C ATOM 1926 C GLU B 35 8.027 1.751 -48.143 1.00 23.79 C ANISOU 1926 C GLU B 35 2909 2240 3891 30 -214 591 C ATOM 1927 O GLU B 35 8.022 2.667 -47.323 1.00 23.85 O ANISOU 1927 O GLU B 35 2931 2195 3937 53 -208 597 O ATOM 1928 CB GLU B 35 10.321 0.956 -48.572 1.00 23.52 C ANISOU 1928 CB GLU B 35 2878 2156 3904 -12 -198 545 C ATOM 1929 CG GLU B 35 11.569 0.934 -49.440 1.00 23.70 C ANISOU 1929 CG GLU B 35 2892 2173 3942 -25 -172 548 C ATOM 1930 CD GLU B 35 11.436 0.043 -50.659 1.00 23.75 C ANISOU 1930 CD GLU B 35 2904 2224 3895 -36 -158 554 C ATOM 1931 OE1 GLU B 35 10.579 -0.869 -50.665 1.00 23.66 O ANISOU 1931 OE1 GLU B 35 2910 2247 3833 -49 -168 539 O ATOM 1932 OE2 GLU B 35 12.209 0.251 -51.610 1.00 23.92 O ANISOU 1932 OE2 GLU B 35 2918 2248 3922 -40 -131 571 O ATOM 1933 N TRP B 36 7.113 0.779 -48.160 1.00 23.84 N ANISOU 1933 N TRP B 36 2906 2314 3838 11 -234 576 N ATOM 1934 CA TRP B 36 6.037 0.687 -47.166 1.00 23.83 C ANISOU 1934 CA TRP B 36 2899 2337 3818 21 -257 568 C ATOM 1935 C TRP B 36 5.997 -0.704 -46.546 1.00 23.76 C ANISOU 1935 C TRP B 36 2912 2328 3788 -27 -274 510 C ATOM 1936 O TRP B 36 6.105 -1.709 -47.248 1.00 23.60 O ANISOU 1936 O TRP B 36 2908 2336 3724 -72 -263 488 O ATOM 1937 CB TRP B 36 4.686 1.008 -47.793 1.00 24.23 C ANISOU 1937 CB TRP B 36 2911 2499 3795 43 -257 617 C ATOM 1938 CG TRP B 36 4.511 2.440 -48.153 1.00 24.60 C ANISOU 1938 CG TRP B 36 2952 2539 3855 118 -229 686 C ATOM 1939 CD1 TRP B 36 4.734 3.012 -49.370 1.00 25.04 C ANISOU 1939 CD1 TRP B 36 3001 2619 3894 144 -200 737 C ATOM 1940 CD2 TRP B 36 4.062 3.490 -47.291 1.00 24.70 C ANISOU 1940 CD2 TRP B 36 2982 2510 3894 184 -215 716 C ATOM 1941 NE1 TRP B 36 4.451 4.355 -49.321 1.00 25.43 N ANISOU 1941 NE1 TRP B 36 3068 2638 3955 227 -163 800 N ATOM 1942 CE2 TRP B 36 4.034 4.675 -48.058 1.00 25.31 C ANISOU 1942 CE2 TRP B 36 3071 2578 3966 253 -168 788 C ATOM 1943 CE3 TRP B 36 3.676 3.544 -45.947 1.00 24.47 C ANISOU 1943 CE3 TRP B 36 2967 2443 3888 194 -229 691 C ATOM 1944 CZ2 TRP B 36 3.637 5.908 -47.522 1.00 25.75 C ANISOU 1944 CZ2 TRP B 36 3167 2579 4037 335 -126 836 C ATOM 1945 CZ3 TRP B 36 3.285 4.766 -45.412 1.00 24.88 C ANISOU 1945 CZ3 TRP B 36 3049 2448 3958 269 -195 734 C ATOM 1946 CH2 TRP B 36 3.267 5.934 -46.203 1.00 25.52 C ANISOU 1946 CH2 TRP B 36 3154 2511 4031 340 -139 806 C ATOM 1947 N VAL B 37 5.830 -0.736 -45.223 1.00 23.93 N ANISOU 1947 N VAL B 37 2946 2310 3836 -16 -293 485 N ATOM 1948 CA VAL B 37 5.932 -1.956 -44.420 1.00 24.05 C ANISOU 1948 CA VAL B 37 2997 2302 3840 -46 -301 434 C ATOM 1949 C VAL B 37 4.804 -1.989 -43.379 1.00 24.43 C ANISOU 1949 C VAL B 37 3041 2373 3868 -47 -321 424 C ATOM 1950 O VAL B 37 4.500 -0.976 -42.752 1.00 24.37 O ANISOU 1950 O VAL B 37 3015 2352 3892 -5 -332 446 O ATOM 1951 CB VAL B 37 7.306 -2.020 -43.711 1.00 23.75 C ANISOU 1951 CB VAL B 37 2976 2186 3863 -24 -301 412 C ATOM 1952 CG1 VAL B 37 7.410 -3.239 -42.795 1.00 23.63 C ANISOU 1952 CG1 VAL B 37 3004 2144 3831 -29 -301 371 C ATOM 1953 CG2 VAL B 37 8.429 -2.006 -44.741 1.00 23.85 C ANISOU 1953 CG2 VAL B 37 2983 2190 3890 -23 -278 423 C ATOM 1954 N LYS B 38 4.208 -3.164 -43.210 1.00 25.07 N ANISOU 1954 N LYS B 38 3150 2483 3893 -97 -317 390 N ATOM 1955 CA LYS B 38 3.139 -3.408 -42.241 1.00 25.76 C ANISOU 1955 CA LYS B 38 3237 2599 3950 -112 -331 373 C ATOM 1956 C LYS B 38 3.697 -4.237 -41.080 1.00 26.19 C ANISOU 1956 C LYS B 38 3352 2572 4029 -111 -329 330 C ATOM 1957 O LYS B 38 4.467 -5.169 -41.306 1.00 26.00 O ANISOU 1957 O LYS B 38 3380 2501 3996 -125 -302 307 O ATOM 1958 CB LYS B 38 2.002 -4.165 -42.934 1.00 26.18 C ANISOU 1958 CB LYS B 38 3282 2761 3905 -191 -320 361 C ATOM 1959 CG LYS B 38 0.837 -4.595 -42.053 1.00 26.27 C ANISOU 1959 CG LYS B 38 3290 2823 3867 -229 -328 337 C ATOM 1960 CD LYS B 38 -0.215 -5.290 -42.902 1.00 26.86 C ANISOU 1960 CD LYS B 38 3344 3031 3829 -330 -313 321 C ATOM 1961 CE LYS B 38 -1.419 -5.717 -42.080 1.00 27.16 C ANISOU 1961 CE LYS B 38 3370 3142 3807 -384 -318 295 C ATOM 1962 NZ LYS B 38 -2.444 -6.402 -42.917 1.00 27.85 N ANISOU 1962 NZ LYS B 38 3427 3385 3769 -507 -301 271 N ATOM 1963 N GLN B 39 3.308 -3.889 -39.852 1.00 26.98 N ANISOU 1963 N GLN B 39 3446 2654 4152 -85 -350 325 N ATOM 1964 CA GLN B 39 3.697 -4.638 -38.656 1.00 27.88 C ANISOU 1964 CA GLN B 39 3611 2703 4278 -77 -349 291 C ATOM 1965 C GLN B 39 2.502 -4.869 -37.735 1.00 28.96 C ANISOU 1965 C GLN B 39 3753 2869 4380 -100 -359 274 C ATOM 1966 O GLN B 39 1.838 -3.915 -37.324 1.00 28.68 O ANISOU 1966 O GLN B 39 3671 2866 4360 -74 -381 296 O ATOM 1967 CB GLN B 39 4.788 -3.901 -37.867 1.00 27.69 C ANISOU 1967 CB GLN B 39 3573 2622 4326 -17 -369 296 C ATOM 1968 CG GLN B 39 5.344 -4.715 -36.699 1.00 27.62 C ANISOU 1968 CG GLN B 39 3608 2565 4319 6 -368 269 C ATOM 1969 CD GLN B 39 6.622 -4.143 -36.108 1.00 27.66 C ANISOU 1969 CD GLN B 39 3585 2547 4376 52 -385 271 C ATOM 1970 OE1 GLN B 39 6.767 -2.933 -35.949 1.00 27.55 O ANISOU 1970 OE1 GLN B 39 3529 2535 4402 56 -404 280 O ATOM 1971 NE2 GLN B 39 7.553 -5.022 -35.764 1.00 27.93 N ANISOU 1971 NE2 GLN B 39 3647 2566 4399 87 -370 264 N ATOM 1972 N ARG B 40 2.258 -6.136 -37.402 1.00 30.70 N ANISOU 1972 N ARG B 40 4041 3071 4552 -145 -332 238 N ATOM 1973 CA ARG B 40 1.324 -6.513 -36.340 1.00 32.17 C ANISOU 1973 CA ARG B 40 4247 3269 4708 -170 -334 216 C ATOM 1974 C ARG B 40 2.046 -7.352 -35.284 1.00 33.19 C ANISOU 1974 C ARG B 40 4455 3305 4849 -139 -316 192 C ATOM 1975 O ARG B 40 3.073 -7.970 -35.587 1.00 33.78 O ANISOU 1975 O ARG B 40 4580 3325 4929 -114 -287 190 O ATOM 1976 CB ARG B 40 0.152 -7.296 -36.914 1.00 32.99 C ANISOU 1976 CB ARG B 40 4364 3451 4718 -273 -307 192 C ATOM 1977 CG ARG B 40 -0.777 -6.448 -37.760 1.00 33.61 C ANISOU 1977 CG ARG B 40 4346 3660 4766 -291 -329 223 C ATOM 1978 CD ARG B 40 -1.833 -7.297 -38.439 1.00 34.60 C ANISOU 1978 CD ARG B 40 4472 3894 4781 -413 -301 194 C ATOM 1979 NE ARG B 40 -1.273 -8.133 -39.503 1.00 35.24 N ANISOU 1979 NE ARG B 40 4615 3949 4825 -476 -259 169 N ATOM 1980 CZ ARG B 40 -1.963 -9.018 -40.222 1.00 36.06 C ANISOU 1980 CZ ARG B 40 4746 4129 4825 -606 -220 129 C ATOM 1981 NH1 ARG B 40 -3.261 -9.216 -39.999 1.00 36.72 N ANISOU 1981 NH1 ARG B 40 4788 4338 4825 -694 -222 109 N ATOM 1982 NH2 ARG B 40 -1.349 -9.715 -41.175 1.00 36.49 N ANISOU 1982 NH2 ARG B 40 4870 4142 4851 -655 -175 107 N ATOM 1983 N PRO B 41 1.519 -7.379 -34.041 1.00 34.24 N ANISOU 1983 N PRO B 41 4598 3428 4982 -129 -329 179 N ATOM 1984 CA PRO B 41 2.155 -8.205 -33.002 1.00 34.70 C ANISOU 1984 CA PRO B 41 4733 3409 5041 -90 -308 164 C ATOM 1985 C PRO B 41 2.138 -9.712 -33.289 1.00 35.69 C ANISOU 1985 C PRO B 41 4975 3487 5098 -136 -236 138 C ATOM 1986 O PRO B 41 3.105 -10.411 -32.967 1.00 36.12 O ANISOU 1986 O PRO B 41 5099 3471 5153 -74 -202 143 O ATOM 1987 CB PRO B 41 1.330 -7.893 -31.746 1.00 34.64 C ANISOU 1987 CB PRO B 41 4711 3414 5035 -88 -334 154 C ATOM 1988 CG PRO B 41 0.680 -6.577 -32.019 1.00 34.38 C ANISOU 1988 CG PRO B 41 4583 3450 5030 -87 -375 176 C ATOM 1989 CD PRO B 41 0.404 -6.579 -33.490 1.00 34.39 C ANISOU 1989 CD PRO B 41 4557 3509 5001 -136 -361 187 C ATOM 1990 N GLY B 42 1.057 -10.197 -33.895 1.00 36.35 N ANISOU 1990 N GLY B 42 5082 3615 5115 -242 -207 112 N ATOM 1991 CA GLY B 42 0.871 -11.627 -34.130 1.00 37.20 C ANISOU 1991 CA GLY B 42 5322 3669 5144 -314 -123 76 C ATOM 1992 C GLY B 42 1.724 -12.211 -35.240 1.00 37.75 C ANISOU 1992 C GLY B 42 5454 3692 5196 -313 -70 78 C ATOM 1993 O GLY B 42 2.398 -13.224 -35.036 1.00 38.38 O ANISOU 1993 O GLY B 42 5659 3673 5251 -276 0 73 O ATOM 1994 N GLN B 43 1.719 -11.563 -36.404 1.00 37.69 N ANISOU 1994 N GLN B 43 5366 3755 5199 -340 -99 90 N ATOM 1995 CA GLN B 43 2.273 -12.157 -37.631 1.00 37.99 C ANISOU 1995 CA GLN B 43 5465 3766 5203 -370 -43 83 C ATOM 1996 C GLN B 43 3.390 -11.331 -38.300 1.00 36.80 C ANISOU 1996 C GLN B 43 5237 3623 5124 -280 -81 126 C ATOM 1997 O GLN B 43 3.537 -11.349 -39.527 1.00 37.57 O ANISOU 1997 O GLN B 43 5329 3747 5200 -320 -63 126 O ATOM 1998 CB GLN B 43 1.140 -12.500 -38.619 1.00 39.16 C ANISOU 1998 CB GLN B 43 5618 4000 5261 -525 -16 44 C ATOM 1999 CG GLN B 43 0.120 -11.396 -38.859 1.00 39.35 C ANISOU 1999 CG GLN B 43 5490 4174 5286 -563 -92 60 C ATOM 2000 CD GLN B 43 -1.103 -11.505 -37.958 1.00 39.76 C ANISOU 2000 CD GLN B 43 5528 4286 5295 -626 -102 36 C ATOM 2001 OE1 GLN B 43 -1.939 -12.389 -38.140 1.00 41.43 O ANISOU 2001 OE1 GLN B 43 5800 4534 5409 -762 -50 -14 O ATOM 2002 NE2 GLN B 43 -1.218 -10.602 -36.992 1.00 39.17 N ANISOU 2002 NE2 GLN B 43 5374 4223 5285 -539 -163 68 N ATOM 2003 N GLY B 44 4.184 -10.633 -37.486 1.00 34.82 N ANISOU 2003 N GLY B 44 4929 3352 4949 -170 -129 159 N ATOM 2004 CA GLY B 44 5.465 -10.080 -37.927 1.00 33.57 C ANISOU 2004 CA GLY B 44 4721 3187 4848 -87 -147 193 C ATOM 2005 C GLY B 44 5.413 -8.968 -38.966 1.00 32.29 C ANISOU 2005 C GLY B 44 4457 3094 4718 -109 -190 214 C ATOM 2006 O GLY B 44 4.355 -8.371 -39.210 1.00 32.34 O ANISOU 2006 O GLY B 44 4407 3168 4711 -166 -220 212 O ATOM 2007 N LEU B 45 6.572 -8.703 -39.573 1.00 30.94 N ANISOU 2007 N LEU B 45 4261 2912 4581 -55 -187 238 N ATOM 2008 CA LEU B 45 6.745 -7.614 -40.544 1.00 29.73 C ANISOU 2008 CA LEU B 45 4022 2810 4463 -62 -219 263 C ATOM 2009 C LEU B 45 6.478 -8.108 -41.961 1.00 29.15 C ANISOU 2009 C LEU B 45 3979 2759 4336 -126 -180 256 C ATOM 2010 O LEU B 45 6.927 -9.193 -42.334 1.00 28.98 O ANISOU 2010 O LEU B 45 4047 2691 4274 -131 -119 241 O ATOM 2011 CB LEU B 45 8.163 -7.036 -40.465 1.00 29.65 C ANISOU 2011 CB LEU B 45 3964 2788 4513 13 -234 288 C ATOM 2012 CG LEU B 45 8.486 -6.151 -39.254 1.00 29.46 C ANISOU 2012 CG LEU B 45 3882 2768 4543 56 -282 293 C ATOM 2013 CD1 LEU B 45 9.981 -6.098 -38.971 1.00 29.68 C ANISOU 2013 CD1 LEU B 45 3879 2800 4597 121 -282 306 C ATOM 2014 CD2 LEU B 45 7.946 -4.745 -39.468 1.00 29.20 C ANISOU 2014 CD2 LEU B 45 3781 2766 4547 29 -320 307 C ATOM 2015 N GLU B 46 5.764 -7.298 -42.745 1.00 28.25 N ANISOU 2015 N GLU B 46 3799 2721 4216 -169 -207 271 N ATOM 2016 CA GLU B 46 5.455 -7.616 -44.138 1.00 28.18 C ANISOU 2016 CA GLU B 46 3800 2760 4148 -236 -178 267 C ATOM 2017 C GLU B 46 5.713 -6.404 -45.023 1.00 27.24 C ANISOU 2017 C GLU B 46 3593 2691 4066 -208 -209 311 C ATOM 2018 O GLU B 46 5.239 -5.307 -44.727 1.00 26.75 O ANISOU 2018 O GLU B 46 3462 2668 4034 -181 -249 340 O ATOM 2019 CB GLU B 46 3.984 -8.008 -44.303 1.00 28.96 C ANISOU 2019 CB GLU B 46 3902 2941 4161 -336 -174 241 C ATOM 2020 CG GLU B 46 3.470 -9.092 -43.372 1.00 29.55 C ANISOU 2020 CG GLU B 46 4063 2973 4190 -384 -141 194 C ATOM 2021 CD GLU B 46 2.003 -9.399 -43.628 1.00 30.30 C ANISOU 2021 CD GLU B 46 4143 3178 4190 -505 -137 165 C ATOM 2022 OE1 GLU B 46 1.182 -9.252 -42.696 1.00 30.56 O ANISOU 2022 OE1 GLU B 46 4151 3245 4217 -515 -162 158 O ATOM 2023 OE2 GLU B 46 1.670 -9.772 -44.773 1.00 31.26 O ANISOU 2023 OE2 GLU B 46 4273 3367 4237 -593 -109 148 O ATOM 2024 N TRP B 47 6.430 -6.615 -46.121 1.00 26.58 N ANISOU 2024 N TRP B 47 3526 2601 3974 -212 -179 318 N ATOM 2025 CA TRP B 47 6.646 -5.569 -47.116 1.00 26.13 C ANISOU 2025 CA TRP B 47 3399 2590 3939 -194 -196 359 C ATOM 2026 C TRP B 47 5.400 -5.414 -47.992 1.00 26.04 C ANISOU 2026 C TRP B 47 3350 2692 3850 -258 -202 369 C ATOM 2027 O TRP B 47 4.906 -6.392 -48.548 1.00 26.30 O ANISOU 2027 O TRP B 47 3427 2764 3801 -341 -171 334 O ATOM 2028 CB TRP B 47 7.854 -5.921 -47.976 1.00 26.14 C ANISOU 2028 CB TRP B 47 3430 2551 3951 -177 -159 363 C ATOM 2029 CG TRP B 47 8.197 -4.905 -49.010 1.00 26.15 C ANISOU 2029 CG TRP B 47 3371 2589 3975 -160 -168 405 C ATOM 2030 CD1 TRP B 47 8.685 -3.646 -48.800 1.00 25.90 C ANISOU 2030 CD1 TRP B 47 3282 2545 4013 -109 -193 440 C ATOM 2031 CD2 TRP B 47 8.106 -5.072 -50.425 1.00 26.48 C ANISOU 2031 CD2 TRP B 47 3415 2682 3965 -201 -143 413 C ATOM 2032 NE1 TRP B 47 8.900 -3.017 -50.002 1.00 26.10 N ANISOU 2032 NE1 TRP B 47 3278 2603 4034 -109 -182 475 N ATOM 2033 CE2 TRP B 47 8.555 -3.870 -51.017 1.00 26.40 C ANISOU 2033 CE2 TRP B 47 3346 2687 3999 -160 -155 461 C ATOM 2034 CE3 TRP B 47 7.689 -6.123 -51.254 1.00 26.91 C ANISOU 2034 CE3 TRP B 47 3523 2770 3932 -277 -104 381 C ATOM 2035 CZ2 TRP B 47 8.604 -3.690 -52.401 1.00 26.73 C ANISOU 2035 CZ2 TRP B 47 3373 2779 4004 -180 -137 485 C ATOM 2036 CZ3 TRP B 47 7.729 -5.941 -52.632 1.00 27.28 C ANISOU 2036 CZ3 TRP B 47 3551 2874 3939 -305 -88 400 C ATOM 2037 CH2 TRP B 47 8.182 -4.728 -53.191 1.00 27.16 C ANISOU 2037 CH2 TRP B 47 3469 2877 3973 -250 -108 454 C ATOM 2038 N ILE B 48 4.906 -4.184 -48.111 1.00 25.56 N ANISOU 2038 N ILE B 48 3212 2691 3808 -219 -235 417 N ATOM 2039 CA ILE B 48 3.734 -3.892 -48.936 1.00 25.73 C ANISOU 2039 CA ILE B 48 3176 2852 3749 -254 -243 443 C ATOM 2040 C ILE B 48 4.179 -3.617 -50.369 1.00 25.74 C ANISOU 2040 C ILE B 48 3159 2890 3730 -255 -226 473 C ATOM 2041 O ILE B 48 3.718 -4.272 -51.311 1.00 25.99 O ANISOU 2041 O ILE B 48 3193 3011 3673 -332 -209 456 O ATOM 2042 CB ILE B 48 2.931 -2.700 -48.373 1.00 25.70 C ANISOU 2042 CB ILE B 48 3105 2899 3761 -186 -274 494 C ATOM 2043 CG1 ILE B 48 2.322 -3.075 -47.015 1.00 25.52 C ANISOU 2043 CG1 ILE B 48 3096 2859 3741 -198 -291 461 C ATOM 2044 CG2 ILE B 48 1.823 -2.273 -49.336 1.00 26.37 C ANISOU 2044 CG2 ILE B 48 3113 3152 3755 -192 -280 541 C ATOM 2045 CD1 ILE B 48 1.991 -1.883 -46.143 1.00 25.35 C ANISOU 2045 CD1 ILE B 48 3039 2822 3771 -111 -311 503 C ATOM 2046 N GLY B 49 5.074 -2.645 -50.524 1.00 25.25 N ANISOU 2046 N GLY B 49 3085 2764 3746 -180 -225 513 N ATOM 2047 CA GLY B 49 5.577 -2.277 -51.837 1.00 25.36 C ANISOU 2047 CA GLY B 49 3085 2803 3750 -172 -206 547 C ATOM 2048 C GLY B 49 6.511 -1.081 -51.837 1.00 25.04 C ANISOU 2048 C GLY B 49 3034 2684 3795 -97 -200 589 C ATOM 2049 O GLY B 49 6.768 -0.472 -50.790 1.00 24.53 O ANISOU 2049 O GLY B 49 2974 2548 3797 -56 -210 591 O ATOM 2050 N ALA B 50 7.014 -0.753 -53.028 1.00 25.18 N ANISOU 2050 N ALA B 50 3045 2718 3805 -91 -177 620 N ATOM 2051 CA ALA B 50 7.873 0.414 -53.239 1.00 25.14 C ANISOU 2051 CA ALA B 50 3038 2648 3868 -37 -159 661 C ATOM 2052 C ALA B 50 7.302 1.292 -54.337 1.00 25.62 C ANISOU 2052 C ALA B 50 3068 2786 3882 1 -142 732 C ATOM 2053 O ALA B 50 6.569 0.814 -55.206 1.00 26.05 O ANISOU 2053 O ALA B 50 3094 2955 3848 -27 -146 742 O ATOM 2054 CB ALA B 50 9.287 -0.013 -53.606 1.00 24.99 C ANISOU 2054 CB ALA B 50 3043 2561 3889 -58 -136 634 C ATOM 2055 N ILE B 51 7.656 2.571 -54.295 1.00 25.73 N ANISOU 2055 N ILE B 51 3093 2739 3946 60 -117 780 N ATOM 2056 CA ILE B 51 7.295 3.524 -55.345 1.00 26.41 C ANISOU 2056 CA ILE B 51 3166 2875 3992 117 -85 859 C ATOM 2057 C ILE B 51 8.503 4.394 -55.676 1.00 26.48 C ANISOU 2057 C ILE B 51 3216 2776 4068 129 -39 876 C ATOM 2058 O ILE B 51 9.277 4.749 -54.787 1.00 26.08 O ANISOU 2058 O ILE B 51 3197 2618 4092 114 -31 843 O ATOM 2059 CB ILE B 51 6.083 4.410 -54.945 1.00 26.88 C ANISOU 2059 CB ILE B 51 3211 2985 4018 202 -80 922 C ATOM 2060 CG1 ILE B 51 5.642 5.295 -56.124 1.00 27.73 C ANISOU 2060 CG1 ILE B 51 3305 3167 4065 281 -40 1017 C ATOM 2061 CG2 ILE B 51 6.388 5.269 -53.719 1.00 26.70 C ANISOU 2061 CG2 ILE B 51 3239 2830 4076 235 -61 917 C ATOM 2062 CD1 ILE B 51 4.299 5.962 -55.923 1.00 28.39 C ANISOU 2062 CD1 ILE B 51 3356 3347 4082 382 -33 1093 C ATOM 2063 N ASN B 52 8.660 4.707 -56.959 1.00 26.93 N ANISOU 2063 N ASN B 52 3270 2874 4090 145 -9 923 N ATOM 2064 CA ASN B 52 9.601 5.726 -57.411 1.00 27.33 C ANISOU 2064 CA ASN B 52 3364 2833 4187 162 47 955 C ATOM 2065 C ASN B 52 8.842 7.056 -57.430 1.00 28.03 C ANISOU 2065 C ASN B 52 3486 2908 4256 259 95 1039 C ATOM 2066 O ASN B 52 7.985 7.253 -58.294 1.00 28.60 O ANISOU 2066 O ASN B 52 3532 3087 4249 323 104 1110 O ATOM 2067 CB ASN B 52 10.133 5.384 -58.812 1.00 27.50 C ANISOU 2067 CB ASN B 52 3372 2901 4174 138 63 968 C ATOM 2068 CG ASN B 52 11.134 6.405 -59.332 1.00 27.93 C ANISOU 2068 CG ASN B 52 3473 2866 4273 145 127 999 C ATOM 2069 OD1 ASN B 52 11.419 7.416 -58.686 1.00 28.18 O ANISOU 2069 OD1 ASN B 52 3555 2797 4355 160 166 1009 O ATOM 2070 ND2 ASN B 52 11.679 6.136 -60.508 1.00 28.06 N ANISOU 2070 ND2 ASN B 52 3480 2917 4265 123 144 1009 N ATOM 2071 N PRO B 52A 9.157 7.982 -56.498 1.00 28.17 N ANISOU 2071 N PRO B 52A 3566 2801 4335 272 132 1036 N ATOM 2072 CA PRO B 52A 8.439 9.270 -56.505 1.00 28.97 C ANISOU 2072 CA PRO B 52A 3725 2870 4413 377 198 1121 C ATOM 2073 C PRO B 52A 8.673 10.156 -57.740 1.00 29.86 C ANISOU 2073 C PRO B 52A 3885 2966 4496 432 274 1201 C ATOM 2074 O PRO B 52A 7.878 11.064 -57.983 1.00 30.70 O ANISOU 2074 O PRO B 52A 4031 3080 4554 548 331 1293 O ATOM 2075 CB PRO B 52A 8.959 9.982 -55.245 1.00 28.94 C ANISOU 2075 CB PRO B 52A 3798 2715 4484 347 232 1080 C ATOM 2076 CG PRO B 52A 9.707 8.957 -54.466 1.00 28.01 C ANISOU 2076 CG PRO B 52A 3634 2591 4418 240 165 978 C ATOM 2077 CD PRO B 52A 10.201 7.961 -55.461 1.00 27.71 C ANISOU 2077 CD PRO B 52A 3535 2633 4360 195 129 959 C ATOM 2078 N GLY B 53 9.751 9.914 -58.488 1.00 29.82 N ANISOU 2078 N GLY B 53 3878 2938 4515 359 282 1173 N ATOM 2079 CA GLY B 53 10.014 10.632 -59.735 1.00 30.65 C ANISOU 2079 CA GLY B 53 4023 3035 4588 402 351 1245 C ATOM 2080 C GLY B 53 9.025 10.341 -60.855 1.00 31.06 C ANISOU 2080 C GLY B 53 4012 3251 4537 484 333 1322 C ATOM 2081 O GLY B 53 8.628 11.253 -61.586 1.00 32.05 O ANISOU 2081 O GLY B 53 4180 3386 4611 587 401 1420 O ATOM 2082 N SER B 54 8.638 9.073 -60.991 1.00 30.49 N ANISOU 2082 N SER B 54 3845 3313 4425 436 248 1278 N ATOM 2083 CA SER B 54 7.730 8.614 -62.051 1.00 30.88 C ANISOU 2083 CA SER B 54 3819 3550 4363 478 221 1330 C ATOM 2084 C SER B 54 6.375 8.087 -61.562 1.00 30.90 C ANISOU 2084 C SER B 54 3745 3702 4293 508 163 1337 C ATOM 2085 O SER B 54 5.457 7.922 -62.368 1.00 31.42 O ANISOU 2085 O SER B 54 3741 3950 4247 554 148 1394 O ATOM 2086 CB SER B 54 8.418 7.508 -62.853 1.00 30.48 C ANISOU 2086 CB SER B 54 3729 3550 4304 372 184 1268 C ATOM 2087 OG SER B 54 8.559 6.333 -62.070 1.00 29.62 O ANISOU 2087 OG SER B 54 3590 3439 4224 278 122 1169 O ATOM 2088 N GLY B 55 6.256 7.793 -60.266 1.00 30.27 N ANISOU 2088 N GLY B 55 3670 3562 4267 475 130 1276 N ATOM 2089 CA GLY B 55 5.064 7.151 -59.719 1.00 30.22 C ANISOU 2089 CA GLY B 55 3591 3693 4198 478 73 1265 C ATOM 2090 C GLY B 55 4.963 5.648 -59.953 1.00 29.78 C ANISOU 2090 C GLY B 55 3472 3745 4100 355 6 1182 C ATOM 2091 O GLY B 55 3.969 5.036 -59.557 1.00 29.82 O ANISOU 2091 O GLY B 55 3417 3873 4041 334 -37 1164 O ATOM 2092 N ALA B 56 5.979 5.037 -60.567 1.00 29.48 N ANISOU 2092 N ALA B 56 3454 3656 4089 271 7 1130 N ATOM 2093 CA ALA B 56 5.933 3.609 -60.892 1.00 29.29 C ANISOU 2093 CA ALA B 56 3397 3715 4016 156 -34 1053 C ATOM 2094 C ALA B 56 6.127 2.756 -59.637 1.00 28.58 C ANISOU 2094 C ALA B 56 3331 3544 3985 87 -67 963 C ATOM 2095 O ALA B 56 6.979 3.057 -58.800 1.00 28.01 O ANISOU 2095 O ALA B 56 3307 3320 4017 95 -56 937 O ATOM 2096 CB ALA B 56 6.973 3.256 -61.940 1.00 29.25 C ANISOU 2096 CB ALA B 56 3419 3675 4020 105 -11 1033 C ATOM 2097 N THR B 57 5.352 1.677 -59.539 1.00 28.71 N ANISOU 2097 N THR B 57 3314 3670 3926 12 -101 914 N ATOM 2098 CA THR B 57 5.212 0.908 -58.305 1.00 28.27 C ANISOU 2098 CA THR B 57 3278 3561 3903 -40 -128 841 C ATOM 2099 C THR B 57 5.696 -0.541 -58.436 1.00 28.21 C ANISOU 2099 C THR B 57 3313 3526 3879 -153 -126 752 C ATOM 2100 O THR B 57 5.651 -1.128 -59.519 1.00 28.51 O ANISOU 2100 O THR B 57 3348 3644 3839 -215 -113 738 O ATOM 2101 CB THR B 57 3.740 0.880 -57.866 1.00 28.62 C ANISOU 2101 CB THR B 57 3259 3752 3865 -33 -158 859 C ATOM 2102 OG1 THR B 57 2.930 0.411 -58.951 1.00 29.39 O ANISOU 2102 OG1 THR B 57 3295 4044 3827 -87 -166 869 O ATOM 2103 CG2 THR B 57 3.274 2.266 -57.464 1.00 28.88 C ANISOU 2103 CG2 THR B 57 3269 3784 3921 99 -148 947 C ATOM 2104 N ASN B 58 6.163 -1.091 -57.315 1.00 27.80 N ANISOU 2104 N ASN B 58 3309 3359 3896 -174 -132 694 N ATOM 2105 CA ASN B 58 6.554 -2.493 -57.196 1.00 27.84 C ANISOU 2105 CA ASN B 58 3375 3319 3884 -260 -118 613 C ATOM 2106 C ASN B 58 5.819 -3.069 -55.984 1.00 27.87 C ANISOU 2106 C ASN B 58 3391 3321 3879 -292 -139 570 C ATOM 2107 O ASN B 58 6.221 -2.827 -54.848 1.00 27.29 O ANISOU 2107 O ASN B 58 3334 3147 3889 -245 -151 563 O ATOM 2108 CB ASN B 58 8.074 -2.606 -57.015 1.00 27.41 C ANISOU 2108 CB ASN B 58 3373 3118 3924 -231 -92 595 C ATOM 2109 CG ASN B 58 8.584 -4.038 -57.120 1.00 27.37 C ANISOU 2109 CG ASN B 58 3445 3064 3891 -294 -56 529 C ATOM 2110 OD1 ASN B 58 7.862 -4.948 -57.523 1.00 27.88 O ANISOU 2110 OD1 ASN B 58 3538 3193 3861 -379 -41 489 O ATOM 2111 ND2 ASN B 58 9.843 -4.236 -56.769 1.00 27.06 N ANISOU 2111 ND2 ASN B 58 3441 2916 3923 -254 -34 516 N ATOM 2112 N TYR B 59 4.738 -3.811 -56.235 1.00 28.66 N ANISOU 2112 N TYR B 59 3478 3542 3869 -381 -143 539 N ATOM 2113 CA TYR B 59 3.875 -4.334 -55.169 1.00 28.93 C ANISOU 2113 CA TYR B 59 3517 3598 3876 -424 -160 499 C ATOM 2114 C TYR B 59 4.242 -5.753 -54.762 1.00 29.18 C ANISOU 2114 C TYR B 59 3654 3537 3895 -509 -122 415 C ATOM 2115 O TYR B 59 4.624 -6.565 -55.601 1.00 29.37 O ANISOU 2115 O TYR B 59 3740 3550 3870 -577 -78 379 O ATOM 2116 CB TYR B 59 2.407 -4.350 -55.609 1.00 29.72 C ANISOU 2116 CB TYR B 59 3538 3907 3848 -486 -180 510 C ATOM 2117 CG TYR B 59 1.759 -2.989 -55.690 1.00 29.99 C ANISOU 2117 CG TYR B 59 3468 4046 3879 -379 -212 602 C ATOM 2118 CD1 TYR B 59 1.350 -2.320 -54.536 1.00 29.68 C ANISOU 2118 CD1 TYR B 59 3403 3979 3894 -299 -236 631 C ATOM 2119 CD2 TYR B 59 1.535 -2.374 -56.921 1.00 30.65 C ANISOU 2119 CD2 TYR B 59 3488 4258 3900 -348 -211 665 C ATOM 2120 CE1 TYR B 59 0.743 -1.074 -54.605 1.00 30.03 C ANISOU 2120 CE1 TYR B 59 3372 4109 3930 -186 -249 721 C ATOM 2121 CE2 TYR B 59 0.931 -1.128 -57.003 1.00 30.99 C ANISOU 2121 CE2 TYR B 59 3450 4393 3931 -229 -225 761 C ATOM 2122 CZ TYR B 59 0.537 -0.482 -55.846 1.00 30.74 C ANISOU 2122 CZ TYR B 59 3405 4321 3954 -145 -240 789 C ATOM 2123 OH TYR B 59 -0.060 0.755 -55.930 1.00 31.19 O ANISOU 2123 OH TYR B 59 3400 4458 3993 -12 -238 890 O ATOM 2124 N ASN B 60 4.107 -6.038 -53.468 1.00 29.23 N ANISOU 2124 N ASN B 60 3691 3472 3941 -498 -132 388 N ATOM 2125 CA ASN B 60 3.964 -7.408 -52.986 1.00 29.80 C ANISOU 2125 CA ASN B 60 3863 3492 3967 -589 -91 313 C ATOM 2126 C ASN B 60 2.605 -7.880 -53.500 1.00 31.15 C ANISOU 2126 C ASN B 60 4006 3831 4001 -722 -88 281 C ATOM 2127 O ASN B 60 1.599 -7.200 -53.292 1.00 31.15 O ANISOU 2127 O ASN B 60 3904 3964 3969 -712 -135 314 O ATOM 2128 CB ASN B 60 4.010 -7.443 -51.450 1.00 29.14 C ANISOU 2128 CB ASN B 60 3803 3316 3953 -538 -108 302 C ATOM 2129 CG ASN B 60 3.951 -8.857 -50.870 1.00 29.37 C ANISOU 2129 CG ASN B 60 3954 3266 3937 -614 -53 231 C ATOM 2130 OD1 ASN B 60 3.498 -9.804 -51.517 1.00 29.95 O ANISOU 2130 OD1 ASN B 60 4093 3379 3909 -735 -3 180 O ATOM 2131 ND2 ASN B 60 4.410 -8.995 -49.627 1.00 28.81 N ANISOU 2131 ND2 ASN B 60 3923 3085 3937 -546 -55 226 N ATOM 2132 N GLU B 61 2.585 -9.036 -54.167 1.00 32.56 N ANISOU 2132 N GLU B 61 4275 4009 4088 -846 -28 216 N ATOM 2133 CA GLU B 61 1.351 -9.620 -54.724 1.00 34.23 C ANISOU 2133 CA GLU B 61 4467 4391 4147 -1010 -15 169 C ATOM 2134 C GLU B 61 0.204 -9.731 -53.710 1.00 35.07 C ANISOU 2134 C GLU B 61 4535 4579 4213 -1061 -40 148 C ATOM 2135 O GLU B 61 -0.963 -9.598 -54.079 1.00 35.83 O ANISOU 2135 O GLU B 61 4534 4884 4197 -1148 -65 147 O ATOM 2136 CB GLU B 61 1.636 -11.005 -55.325 1.00 34.94 C ANISOU 2136 CB GLU B 61 4708 4414 4153 -1148 77 85 C ATOM 2137 N LYS B 62 0.543 -9.965 -52.443 1.00 35.33 N ANISOU 2137 N LYS B 62 4634 4461 4329 -1005 -34 135 N ATOM 2138 CA LYS B 62 -0.446 -10.026 -51.358 1.00 36.13 C ANISOU 2138 CA LYS B 62 4704 4617 4407 -1038 -58 118 C ATOM 2139 C LYS B 62 -1.221 -8.717 -51.133 1.00 36.36 C ANISOU 2139 C LYS B 62 4566 4798 4452 -948 -138 194 C ATOM 2140 O LYS B 62 -2.349 -8.761 -50.647 1.00 37.04 O ANISOU 2140 O LYS B 62 4592 5013 4469 -1007 -157 183 O ATOM 2141 CB LYS B 62 0.219 -10.440 -50.038 1.00 35.80 C ANISOU 2141 CB LYS B 62 4766 4374 4461 -969 -37 100 C ATOM 2142 CG LYS B 62 0.791 -11.849 -50.035 1.00 36.47 C ANISOU 2142 CG LYS B 62 5034 4309 4512 -1047 59 29 C ATOM 2143 CD LYS B 62 1.419 -12.186 -48.689 1.00 36.16 C ANISOU 2143 CD LYS B 62 5084 4095 4561 -954 76 27 C ATOM 2144 CE LYS B 62 2.015 -13.588 -48.696 1.00 36.89 C ANISOU 2144 CE LYS B 62 5373 4030 4612 -1004 188 -30 C ATOM 2145 NZ LYS B 62 2.304 -14.075 -47.318 1.00 36.72 N ANISOU 2145 NZ LYS B 62 5441 3872 4638 -936 214 -37 N ATOM 2146 N PHE B 63 -0.620 -7.572 -51.465 1.00 36.13 N ANISOU 2146 N PHE B 63 4471 4749 4507 -807 -174 272 N ATOM 2147 CA PHE B 63 -1.263 -6.261 -51.291 1.00 36.56 C ANISOU 2147 CA PHE B 63 4392 4921 4578 -698 -230 354 C ATOM 2148 C PHE B 63 -1.733 -5.605 -52.600 1.00 37.83 C ANISOU 2148 C PHE B 63 4446 5271 4656 -688 -246 413 C ATOM 2149 O PHE B 63 -2.124 -4.434 -52.590 1.00 38.20 O ANISOU 2149 O PHE B 63 4398 5400 4719 -569 -278 497 O ATOM 2150 CB PHE B 63 -0.314 -5.320 -50.536 1.00 35.54 C ANISOU 2150 CB PHE B 63 4279 4623 4601 -540 -249 403 C ATOM 2151 CG PHE B 63 -0.070 -5.731 -49.112 1.00 34.93 C ANISOU 2151 CG PHE B 63 4271 4407 4593 -528 -247 363 C ATOM 2152 CD1 PHE B 63 0.975 -6.595 -48.788 1.00 34.57 C ANISOU 2152 CD1 PHE B 63 4342 4196 4599 -546 -211 313 C ATOM 2153 CD2 PHE B 63 -0.889 -5.260 -48.088 1.00 34.81 C ANISOU 2153 CD2 PHE B 63 4205 4436 4585 -489 -277 382 C ATOM 2154 CE1 PHE B 63 1.199 -6.979 -47.474 1.00 34.09 C ANISOU 2154 CE1 PHE B 63 4341 4020 4591 -524 -208 284 C ATOM 2155 CE2 PHE B 63 -0.669 -5.642 -46.772 1.00 34.24 C ANISOU 2155 CE2 PHE B 63 4197 4242 4572 -478 -276 346 C ATOM 2156 CZ PHE B 63 0.373 -6.503 -46.465 1.00 33.90 C ANISOU 2156 CZ PHE B 63 4265 4039 4575 -496 -243 298 C ATOM 2157 N LYS B 64 -1.735 -6.356 -53.705 1.00 38.94 N ANISOU 2157 N LYS B 64 4609 5486 4701 -810 -216 371 N ATOM 2158 CA LYS B 64 -2.069 -5.801 -55.025 1.00 40.05 C ANISOU 2158 CA LYS B 64 4652 5809 4756 -802 -228 425 C ATOM 2159 C LYS B 64 -3.519 -5.317 -55.133 1.00 41.24 C ANISOU 2159 C LYS B 64 4651 6236 4784 -805 -266 473 C ATOM 2160 O LYS B 64 -3.781 -4.314 -55.796 1.00 42.01 O ANISOU 2160 O LYS B 64 4647 6462 4855 -698 -287 565 O ATOM 2161 CB LYS B 64 -1.779 -6.820 -56.133 1.00 40.77 C ANISOU 2161 CB LYS B 64 4809 5922 4759 -951 -184 358 C ATOM 2162 N ASP B 65 -4.447 -6.032 -54.496 1.00 41.81 N ANISOU 2162 N ASP B 65 4707 6403 4775 -923 -267 414 N ATOM 2163 CA ASP B 65 -5.860 -5.623 -54.442 1.00 42.83 C ANISOU 2163 CA ASP B 65 4679 6812 4781 -925 -302 458 C ATOM 2164 C ASP B 65 -6.170 -4.654 -53.299 1.00 41.85 C ANISOU 2164 C ASP B 65 4507 6650 4743 -757 -332 530 C ATOM 2165 O ASP B 65 -7.106 -3.861 -53.399 1.00 42.95 O ANISOU 2165 O ASP B 65 4508 7001 4809 -670 -358 612 O ATOM 2166 CB ASP B 65 -6.774 -6.852 -54.313 1.00 44.13 C ANISOU 2166 CB ASP B 65 4844 7121 4801 -1152 -283 356 C ATOM 2167 CG ASP B 65 -6.726 -7.761 -55.535 1.00 45.42 C ANISOU 2167 CG ASP B 65 5042 7376 4839 -1340 -247 285 C ATOM 2168 OD1 ASP B 65 -6.314 -7.310 -56.628 1.00 45.91 O ANISOU 2168 OD1 ASP B 65 5071 7483 4888 -1288 -251 333 O ATOM 2169 OD2 ASP B 65 -7.121 -8.938 -55.402 1.00 46.53 O ANISOU 2169 OD2 ASP B 65 5250 7542 4886 -1548 -206 177 O ATOM 2170 N LYS B 66 -5.390 -4.730 -52.224 1.00 39.99 N ANISOU 2170 N LYS B 66 4386 6156 4653 -708 -323 501 N ATOM 2171 CA LYS B 66 -5.633 -3.968 -50.994 1.00 38.94 C ANISOU 2171 CA LYS B 66 4232 5960 4603 -577 -343 547 C ATOM 2172 C LYS B 66 -5.017 -2.560 -51.008 1.00 37.75 C ANISOU 2172 C LYS B 66 4075 5706 4563 -372 -349 646 C ATOM 2173 O LYS B 66 -5.653 -1.610 -50.552 1.00 37.78 O ANISOU 2173 O LYS B 66 4009 5780 4567 -245 -360 722 O ATOM 2174 CB LYS B 66 -5.102 -4.772 -49.790 1.00 38.24 C ANISOU 2174 CB LYS B 66 4271 5654 4604 -634 -328 463 C ATOM 2175 CG LYS B 66 -5.151 -4.092 -48.421 1.00 37.89 C ANISOU 2175 CG LYS B 66 4232 5505 4659 -511 -346 494 C ATOM 2176 CD LYS B 66 -6.549 -3.668 -47.993 1.00 38.68 C ANISOU 2176 CD LYS B 66 4209 5816 4671 -483 -368 537 C ATOM 2177 CE LYS B 66 -7.431 -4.862 -47.664 1.00 39.24 C ANISOU 2177 CE LYS B 66 4272 6006 4631 -665 -362 453 C ATOM 2178 NZ LYS B 66 -8.732 -4.431 -47.089 1.00 39.91 N ANISOU 2178 NZ LYS B 66 4233 6292 4639 -629 -384 495 N ATOM 2179 N ALA B 67 -3.786 -2.438 -51.514 1.00 36.30 N ANISOU 2179 N ALA B 67 3972 5353 4467 -345 -331 644 N ATOM 2180 CA ALA B 67 -2.988 -1.214 -51.373 1.00 35.10 C ANISOU 2180 CA ALA B 67 3850 5052 4435 -183 -323 715 C ATOM 2181 C ALA B 67 -2.801 -0.467 -52.691 1.00 34.99 C ANISOU 2181 C ALA B 67 3793 5115 4387 -113 -310 792 C ATOM 2182 O ALA B 67 -2.691 -1.083 -53.751 1.00 35.26 O ANISOU 2182 O ALA B 67 3817 5231 4350 -205 -306 766 O ATOM 2183 CB ALA B 67 -1.627 -1.547 -50.778 1.00 34.06 C ANISOU 2183 CB ALA B 67 3840 4664 4437 -196 -311 657 C ATOM 2184 N ARG B 68 -2.756 0.862 -52.597 1.00 34.40 N ANISOU 2184 N ARG B 68 3707 5004 4361 49 -296 885 N ATOM 2185 CA ARG B 68 -2.441 1.742 -53.720 1.00 34.35 C ANISOU 2185 CA ARG B 68 3685 5026 4342 142 -270 968 C ATOM 2186 C ARG B 68 -1.380 2.764 -53.291 1.00 33.30 C ANISOU 2186 C ARG B 68 3647 4656 4349 248 -236 999 C ATOM 2187 O ARG B 68 -1.614 3.548 -52.368 1.00 33.29 O ANISOU 2187 O ARG B 68 3667 4587 4396 344 -222 1034 O ATOM 2188 CB ARG B 68 -3.699 2.465 -54.196 1.00 35.52 C ANISOU 2188 CB ARG B 68 3716 5416 4366 249 -268 1074 C ATOM 2189 N LEU B 69 -0.224 2.743 -53.957 1.00 32.35 N ANISOU 2189 N LEU B 69 3587 4418 4288 221 -218 981 N ATOM 2190 CA LEU B 69 0.883 3.663 -53.664 1.00 31.53 C ANISOU 2190 CA LEU B 69 3571 4105 4305 289 -180 999 C ATOM 2191 C LEU B 69 0.926 4.818 -54.658 1.00 32.01 C ANISOU 2191 C LEU B 69 3631 4189 4342 403 -133 1101 C ATOM 2192 O LEU B 69 0.925 4.601 -55.870 1.00 32.11 O ANISOU 2192 O LEU B 69 3606 4308 4286 383 -131 1125 O ATOM 2193 CB LEU B 69 2.223 2.923 -53.698 1.00 30.67 C ANISOU 2193 CB LEU B 69 3527 3852 4276 190 -185 915 C ATOM 2194 CG LEU B 69 2.397 1.761 -52.717 1.00 29.91 C ANISOU 2194 CG LEU B 69 3455 3700 4210 92 -217 818 C ATOM 2195 CD1 LEU B 69 3.811 1.206 -52.803 1.00 29.31 C ANISOU 2195 CD1 LEU B 69 3442 3486 4208 34 -208 759 C ATOM 2196 CD2 LEU B 69 2.070 2.177 -51.291 1.00 29.62 C ANISOU 2196 CD2 LEU B 69 3435 3596 4225 137 -226 813 C ATOM 2197 N THR B 70 0.961 6.040 -54.131 1.00 32.01 N ANISOU 2197 N THR B 70 3685 4085 4392 520 -86 1162 N ATOM 2198 CA THR B 70 1.089 7.250 -54.940 1.00 32.86 C ANISOU 2198 CA THR B 70 3827 4172 4487 640 -19 1263 C ATOM 2199 C THR B 70 2.120 8.182 -54.315 1.00 32.62 C ANISOU 2199 C THR B 70 3920 3901 4574 663 39 1253 C ATOM 2200 O THR B 70 2.570 7.962 -53.186 1.00 31.94 O ANISOU 2200 O THR B 70 3874 3693 4568 602 22 1178 O ATOM 2201 CB THR B 70 -0.256 7.994 -55.077 1.00 33.81 C ANISOU 2201 CB THR B 70 3891 4451 4503 793 8 1377 C ATOM 2202 OG1 THR B 70 -0.753 8.340 -53.781 1.00 33.54 O ANISOU 2202 OG1 THR B 70 3882 4359 4501 844 16 1375 O ATOM 2203 CG2 THR B 70 -1.277 7.124 -55.786 1.00 34.29 C ANISOU 2203 CG2 THR B 70 3813 4788 4427 756 -48 1387 C ATOM 2204 N ALA B 71 2.502 9.207 -55.068 1.00 33.42 N ANISOU 2204 N ALA B 71 4081 3940 4677 742 112 1327 N ATOM 2205 CA ALA B 71 3.468 10.194 -54.604 1.00 33.62 C ANISOU 2205 CA ALA B 71 4234 3744 4797 749 185 1319 C ATOM 2206 C ALA B 71 3.174 11.558 -55.211 1.00 35.00 C ANISOU 2206 C ALA B 71 4483 3884 4931 899 289 1440 C ATOM 2207 O ALA B 71 2.839 11.656 -56.390 1.00 35.54 O ANISOU 2207 O ALA B 71 4510 4072 4921 965 303 1517 O ATOM 2208 CB ALA B 71 4.882 9.753 -54.951 1.00 32.92 C ANISOU 2208 CB ALA B 71 4169 3559 4780 620 172 1241 C ATOM 2209 N ASP B 72 3.281 12.594 -54.382 1.00 35.72 N ANISOU 2209 N ASP B 72 4692 3811 5068 954 368 1456 N ATOM 2210 CA ASP B 72 3.151 13.982 -54.811 1.00 37.20 C ANISOU 2210 CA ASP B 72 4997 3910 5228 1094 495 1564 C ATOM 2211 C ASP B 72 4.519 14.637 -54.641 1.00 37.40 C ANISOU 2211 C ASP B 72 5160 3705 5346 997 567 1508 C ATOM 2212 O ASP B 72 4.908 15.004 -53.530 1.00 37.36 O ANISOU 2212 O ASP B 72 5240 3551 5405 940 596 1446 O ATOM 2213 CB ASP B 72 2.083 14.703 -53.975 1.00 37.95 C ANISOU 2213 CB ASP B 72 5137 3997 5286 1241 550 1632 C ATOM 2214 CG ASP B 72 1.869 16.156 -54.398 1.00 39.55 C ANISOU 2214 CG ASP B 72 5482 4097 5446 1412 702 1757 C ATOM 2215 OD1 ASP B 72 2.463 16.599 -55.403 1.00 40.09 O ANISOU 2215 OD1 ASP B 72 5608 4117 5508 1421 762 1798 O ATOM 2216 OD2 ASP B 72 1.093 16.859 -53.718 1.00 40.53 O ANISOU 2216 OD2 ASP B 72 5673 4186 5542 1545 771 1818 O ATOM 2217 N LYS B 73 5.249 14.773 -55.746 1.00 37.89 N ANISOU 2217 N LYS B 73 5241 3752 5406 967 596 1525 N ATOM 2218 CA LYS B 73 6.608 15.320 -55.694 1.00 38.16 C ANISOU 2218 CA LYS B 73 5388 3595 5517 852 661 1466 C ATOM 2219 C LYS B 73 6.663 16.827 -55.434 1.00 39.46 C ANISOU 2219 C LYS B 73 5743 3568 5684 926 818 1522 C ATOM 2220 O LYS B 73 7.688 17.321 -54.968 1.00 39.69 O ANISOU 2220 O LYS B 73 5876 3428 5776 804 875 1450 O ATOM 2221 CB LYS B 73 7.429 14.927 -56.930 1.00 38.19 C ANISOU 2221 CB LYS B 73 5348 3644 5520 784 643 1459 C ATOM 2222 CG LYS B 73 6.971 15.474 -58.274 1.00 39.30 C ANISOU 2222 CG LYS B 73 5506 3850 5577 919 708 1585 C ATOM 2223 CD LYS B 73 7.504 14.576 -59.384 1.00 38.86 C ANISOU 2223 CD LYS B 73 5348 3910 5509 842 638 1560 C ATOM 2224 CE LYS B 73 7.364 15.201 -60.758 1.00 40.02 C ANISOU 2224 CE LYS B 73 5528 4095 5583 948 712 1673 C ATOM 2225 NZ LYS B 73 8.080 14.385 -61.778 1.00 39.59 N ANISOU 2225 NZ LYS B 73 5393 4122 5528 851 655 1634 N ATOM 2226 N SER B 74 5.563 17.539 -55.689 1.00 40.46 N ANISOU 2226 N SER B 74 5917 3726 5732 1121 892 1648 N ATOM 2227 CA SER B 74 5.468 18.965 -55.352 1.00 41.80 C ANISOU 2227 CA SER B 74 6290 3700 5891 1215 1059 1710 C ATOM 2228 C SER B 74 5.453 19.232 -53.838 1.00 41.46 C ANISOU 2228 C SER B 74 6325 3526 5900 1160 1079 1635 C ATOM 2229 O SER B 74 5.837 20.317 -53.407 1.00 42.57 O ANISOU 2229 O SER B 74 6658 3457 6059 1148 1217 1631 O ATOM 2230 CB SER B 74 4.234 19.608 -56.008 1.00 43.19 C ANISOU 2230 CB SER B 74 6490 3964 5958 1470 1138 1879 C ATOM 2231 OG SER B 74 3.032 19.276 -55.327 1.00 43.18 O ANISOU 2231 OG SER B 74 6400 4096 5913 1580 1083 1913 O ATOM 2232 N SER B 75 4.999 18.260 -53.045 1.00 40.19 N ANISOU 2232 N SER B 75 6029 3486 5757 1122 950 1574 N ATOM 2233 CA SER B 75 4.978 18.378 -51.579 1.00 39.69 C ANISOU 2233 CA SER B 75 6020 3321 5742 1062 952 1496 C ATOM 2234 C SER B 75 5.895 17.367 -50.857 1.00 38.09 C ANISOU 2234 C SER B 75 5722 3131 5619 850 829 1346 C ATOM 2235 O SER B 75 5.808 17.223 -49.637 1.00 37.65 O ANISOU 2235 O SER B 75 5673 3036 5596 798 800 1278 O ATOM 2236 CB SER B 75 3.541 18.221 -51.084 1.00 39.84 C ANISOU 2236 CB SER B 75 5975 3460 5701 1224 924 1566 C ATOM 2237 OG SER B 75 3.101 16.881 -51.234 1.00 38.74 O ANISOU 2237 OG SER B 75 5630 3542 5547 1193 767 1538 O ATOM 2238 N ASN B 76 6.770 16.684 -51.600 1.00 37.16 N ANISOU 2238 N ASN B 76 5521 3073 5527 739 763 1300 N ATOM 2239 CA ASN B 76 7.678 15.663 -51.045 1.00 35.79 C ANISOU 2239 CA ASN B 76 5250 2932 5418 563 652 1173 C ATOM 2240 C ASN B 76 6.975 14.593 -50.191 1.00 34.51 C ANISOU 2240 C ASN B 76 4966 2890 5257 566 532 1132 C ATOM 2241 O ASN B 76 7.500 14.158 -49.163 1.00 33.80 O ANISOU 2241 O ASN B 76 4856 2770 5217 455 481 1036 O ATOM 2242 CB ASN B 76 8.818 16.333 -50.255 1.00 36.24 C ANISOU 2242 CB ASN B 76 5419 2819 5531 415 717 1082 C ATOM 2243 CG ASN B 76 9.893 16.912 -51.148 1.00 36.93 C ANISOU 2243 CG ASN B 76 5576 2828 5628 337 795 1080 C ATOM 2244 OD1 ASN B 76 9.662 17.219 -52.314 1.00 37.49 O ANISOU 2244 OD1 ASN B 76 5668 2916 5659 428 843 1168 O ATOM 2245 ND2 ASN B 76 11.089 17.056 -50.598 1.00 37.17 N ANISOU 2245 ND2 ASN B 76 5636 2784 5702 162 807 978 N ATOM 2246 N THR B 77 5.795 14.165 -50.634 1.00 34.22 N ANISOU 2246 N THR B 77 4845 3000 5157 689 491 1207 N ATOM 2247 CA THR B 77 4.951 13.274 -49.845 1.00 33.41 C ANISOU 2247 CA THR B 77 4643 3011 5041 702 397 1180 C ATOM 2248 C THR B 77 4.572 12.031 -50.642 1.00 32.66 C ANISOU 2248 C THR B 77 4399 3108 4901 691 296 1184 C ATOM 2249 O THR B 77 4.143 12.125 -51.795 1.00 33.14 O ANISOU 2249 O THR B 77 4426 3267 4898 768 312 1264 O ATOM 2250 CB THR B 77 3.684 14.001 -49.357 1.00 34.21 C ANISOU 2250 CB THR B 77 4789 3118 5090 858 455 1263 C ATOM 2251 OG1 THR B 77 4.057 15.235 -48.737 1.00 35.04 O ANISOU 2251 OG1 THR B 77 5062 3024 5228 868 573 1263 O ATOM 2252 CG2 THR B 77 2.909 13.151 -48.346 1.00 33.52 C ANISOU 2252 CG2 THR B 77 4611 3127 4997 849 366 1221 C ATOM 2253 N ALA B 78 4.766 10.871 -50.017 1.00 31.56 N ANISOU 2253 N ALA B 78 4182 3018 4791 590 201 1095 N ATOM 2254 CA ALA B 78 4.309 9.587 -50.542 1.00 30.99 C ANISOU 2254 CA ALA B 78 3988 3115 4672 560 112 1081 C ATOM 2255 C ALA B 78 3.061 9.177 -49.776 1.00 30.89 C ANISOU 2255 C ALA B 78 3919 3205 4614 606 70 1088 C ATOM 2256 O ALA B 78 2.911 9.537 -48.608 1.00 30.83 O ANISOU 2256 O ALA B 78 3958 3116 4642 618 83 1065 O ATOM 2257 CB ALA B 78 5.396 8.540 -50.379 1.00 30.09 C ANISOU 2257 CB ALA B 78 3844 2976 4612 423 52 981 C ATOM 2258 N TYR B 79 2.174 8.428 -50.429 1.00 31.04 N ANISOU 2258 N TYR B 79 3836 3408 4549 622 23 1116 N ATOM 2259 CA TYR B 79 0.913 7.997 -49.819 1.00 31.23 C ANISOU 2259 CA TYR B 79 3791 3563 4513 655 -16 1125 C ATOM 2260 C TYR B 79 0.673 6.497 -49.984 1.00 30.82 C ANISOU 2260 C TYR B 79 3649 3641 4420 542 -97 1058 C ATOM 2261 O TYR B 79 1.032 5.906 -51.005 1.00 30.58 O ANISOU 2261 O TYR B 79 3587 3672 4362 482 -115 1046 O ATOM 2262 CB TYR B 79 -0.266 8.747 -50.432 1.00 32.36 C ANISOU 2262 CB TYR B 79 3894 3846 4555 806 26 1246 C ATOM 2263 CG TYR B 79 -0.228 10.251 -50.278 1.00 33.14 C ANISOU 2263 CG TYR B 79 4101 3815 4674 944 128 1328 C ATOM 2264 CD1 TYR B 79 -0.723 10.869 -49.128 1.00 33.38 C ANISOU 2264 CD1 TYR B 79 4188 3774 4723 1016 165 1341 C ATOM 2265 CD2 TYR B 79 0.275 11.060 -51.295 1.00 33.80 C ANISOU 2265 CD2 TYR B 79 4245 3844 4753 1002 198 1394 C ATOM 2266 CE1 TYR B 79 -0.704 12.253 -48.991 1.00 34.29 C ANISOU 2266 CE1 TYR B 79 4427 3754 4849 1142 278 1415 C ATOM 2267 CE2 TYR B 79 0.297 12.443 -51.169 1.00 34.74 C ANISOU 2267 CE2 TYR B 79 4489 3829 4883 1127 311 1470 C ATOM 2268 CZ TYR B 79 -0.192 13.034 -50.017 1.00 35.03 C ANISOU 2268 CZ TYR B 79 4591 3785 4935 1196 354 1479 C ATOM 2269 OH TYR B 79 -0.167 14.404 -49.891 1.00 36.26 O ANISOU 2269 OH TYR B 79 4894 3788 5094 1317 483 1552 O ATOM 2270 N LEU B 80 0.065 5.897 -48.962 1.00 30.79 N ANISOU 2270 N LEU B 80 3617 3672 4409 509 -137 1013 N ATOM 2271 CA LEU B 80 -0.419 4.518 -49.013 1.00 30.85 C ANISOU 2271 CA LEU B 80 3553 3811 4359 404 -198 954 C ATOM 2272 C LEU B 80 -1.927 4.545 -48.770 1.00 31.84 C ANISOU 2272 C LEU B 80 3594 4119 4386 459 -210 1001 C ATOM 2273 O LEU B 80 -2.369 4.943 -47.690 1.00 31.56 O ANISOU 2273 O LEU B 80 3575 4044 4374 512 -203 1007 O ATOM 2274 CB LEU B 80 0.292 3.668 -47.955 1.00 29.90 C ANISOU 2274 CB LEU B 80 3480 3566 4316 305 -230 852 C ATOM 2275 CG LEU B 80 -0.313 2.312 -47.558 1.00 29.67 C ANISOU 2275 CG LEU B 80 3412 3629 4234 204 -275 785 C ATOM 2276 CD1 LEU B 80 -0.496 1.399 -48.759 1.00 30.01 C ANISOU 2276 CD1 LEU B 80 3410 3802 4191 119 -287 770 C ATOM 2277 CD2 LEU B 80 0.553 1.644 -46.502 1.00 28.85 C ANISOU 2277 CD2 LEU B 80 3373 3377 4212 139 -291 701 C ATOM 2278 N GLN B 81 -2.706 4.140 -49.774 1.00 33.16 N ANISOU 2278 N GLN B 81 3667 4498 4436 443 -226 1033 N ATOM 2279 CA GLN B 81 -4.168 4.086 -49.661 1.00 34.62 C ANISOU 2279 CA GLN B 81 3744 4906 4503 483 -241 1079 C ATOM 2280 C GLN B 81 -4.653 2.644 -49.554 1.00 34.94 C ANISOU 2280 C GLN B 81 3728 5071 4476 317 -292 990 C ATOM 2281 O GLN B 81 -4.219 1.783 -50.316 1.00 34.66 O ANISOU 2281 O GLN B 81 3696 5056 4416 197 -306 935 O ATOM 2282 CB GLN B 81 -4.842 4.764 -50.857 1.00 35.90 C ANISOU 2282 CB GLN B 81 3823 5263 4554 591 -217 1192 C ATOM 2283 CG GLN B 81 -6.347 4.956 -50.680 1.00 37.09 C ANISOU 2283 CG GLN B 81 3851 5663 4577 672 -223 1262 C ATOM 2284 CD GLN B 81 -7.006 5.715 -51.820 1.00 38.63 C ANISOU 2284 CD GLN B 81 3958 6067 4652 811 -193 1391 C ATOM 2285 OE1 GLN B 81 -7.876 6.558 -51.597 1.00 39.83 O ANISOU 2285 OE1 GLN B 81 4064 6327 4744 979 -159 1495 O ATOM 2286 NE2 GLN B 81 -6.606 5.411 -53.047 1.00 38.94 N ANISOU 2286 NE2 GLN B 81 3974 6171 4649 752 -202 1389 N ATOM 2287 N PHE B 82 -5.555 2.398 -48.606 1.00 35.84 N ANISOU 2287 N PHE B 82 3800 5262 4555 309 -309 975 N ATOM 2288 CA PHE B 82 -6.221 1.106 -48.463 1.00 36.69 C ANISOU 2288 CA PHE B 82 3854 5509 4578 150 -345 896 C ATOM 2289 C PHE B 82 -7.652 1.211 -48.960 1.00 38.49 C ANISOU 2289 C PHE B 82 3931 6051 4644 174 -355 959 C ATOM 2290 O PHE B 82 -8.306 2.226 -48.743 1.00 39.04 O ANISOU 2290 O PHE B 82 3947 6201 4687 335 -337 1057 O ATOM 2291 CB PHE B 82 -6.233 0.667 -47.002 1.00 36.17 C ANISOU 2291 CB PHE B 82 3844 5320 4577 108 -356 828 C ATOM 2292 CG PHE B 82 -4.868 0.492 -46.418 1.00 35.21 C ANISOU 2292 CG PHE B 82 3854 4925 4599 84 -350 766 C ATOM 2293 CD1 PHE B 82 -4.206 -0.726 -46.520 1.00 34.82 C ANISOU 2293 CD1 PHE B 82 3866 4800 4564 -58 -358 674 C ATOM 2294 CD2 PHE B 82 -4.236 1.550 -45.776 1.00 34.89 C ANISOU 2294 CD2 PHE B 82 3878 4710 4667 203 -329 802 C ATOM 2295 CE1 PHE B 82 -2.938 -0.888 -45.981 1.00 34.00 C ANISOU 2295 CE1 PHE B 82 3867 4472 4579 -63 -351 627 C ATOM 2296 CE2 PHE B 82 -2.971 1.395 -45.234 1.00 34.08 C ANISOU 2296 CE2 PHE B 82 3877 4389 4681 173 -327 745 C ATOM 2297 CZ PHE B 82 -2.322 0.176 -45.338 1.00 33.65 C ANISOU 2297 CZ PHE B 82 3865 4283 4638 48 -341 662 C ATOM 2298 N SER B 82A -8.125 0.164 -49.631 1.00 39.70 N ANISOU 2298 N SER B 82A 4019 6389 4679 13 -376 904 N ATOM 2299 CA SER B 82A -9.530 0.046 -50.021 1.00 41.57 C ANISOU 2299 CA SER B 82A 4094 6964 4739 -9 -392 943 C ATOM 2300 C SER B 82A -10.173 -1.079 -49.219 1.00 41.86 C ANISOU 2300 C SER B 82A 4116 7066 4722 -181 -410 844 C ATOM 2301 O SER B 82A -9.477 -1.991 -48.757 1.00 41.26 O ANISOU 2301 O SER B 82A 4160 6796 4720 -313 -407 738 O ATOM 2302 CB SER B 82A -9.647 -0.245 -51.516 1.00 42.72 C ANISOU 2302 CB SER B 82A 4163 7307 4761 -81 -398 955 C ATOM 2303 OG SER B 82A -9.058 -1.495 -51.837 1.00 42.62 O ANISOU 2303 OG SER B 82A 4230 7212 4750 -292 -399 833 O ATOM 2304 N SER B 82B -11.493 -0.999 -49.046 1.00 43.06 N ANISOU 2304 N SER B 82B 4124 7496 4740 -173 -423 882 N ATOM 2305 CA SER B 82B -12.280 -2.058 -48.402 1.00 43.43 C ANISOU 2305 CA SER B 82B 4137 7659 4704 -354 -436 791 C ATOM 2306 C SER B 82B -11.666 -2.532 -47.074 1.00 41.86 C ANISOU 2306 C SER B 82B 4090 7167 4649 -396 -427 708 C ATOM 2307 O SER B 82B -11.364 -3.717 -46.908 1.00 41.44 O ANISOU 2307 O SER B 82B 4125 7025 4595 -585 -419 594 O ATOM 2308 CB SER B 82B -12.453 -3.237 -49.373 1.00 44.35 C ANISOU 2308 CB SER B 82B 4229 7933 4689 -594 -437 701 C ATOM 2309 OG SER B 82B -13.262 -4.259 -48.808 1.00 45.24 O ANISOU 2309 OG SER B 82B 4316 8168 4705 -788 -437 609 O ATOM 2310 N LEU B 82C -11.482 -1.595 -46.146 1.00 40.99 N ANISOU 2310 N LEU B 82C 4015 6909 4651 -217 -423 767 N ATOM 2311 CA LEU B 82C -10.795 -1.872 -44.877 1.00 39.61 C ANISOU 2311 CA LEU B 82C 3979 6453 4616 -229 -417 702 C ATOM 2312 C LEU B 82C -11.474 -2.974 -44.060 1.00 39.86 C ANISOU 2312 C LEU B 82C 4012 6545 4589 -394 -421 611 C ATOM 2313 O LEU B 82C -12.699 -3.002 -43.956 1.00 40.74 O ANISOU 2313 O LEU B 82C 3994 6909 4575 -419 -429 632 O ATOM 2314 CB LEU B 82C -10.686 -0.603 -44.021 1.00 39.09 C ANISOU 2314 CB LEU B 82C 3936 6264 4653 -17 -407 784 C ATOM 2315 CG LEU B 82C -9.612 0.420 -44.404 1.00 38.44 C ANISOU 2315 CG LEU B 82C 3932 5988 4684 128 -386 843 C ATOM 2316 CD1 LEU B 82C -9.884 1.741 -43.699 1.00 38.51 C ANISOU 2316 CD1 LEU B 82C 3943 5948 4741 331 -360 935 C ATOM 2317 CD2 LEU B 82C -8.217 -0.101 -44.080 1.00 37.13 C ANISOU 2317 CD2 LEU B 82C 3914 5540 4652 52 -386 757 C ATOM 2318 N THR B 83 -10.668 -3.880 -43.505 1.00 39.04 N ANISOU 2318 N THR B 83 4053 6215 4567 -503 -409 514 N ATOM 2319 CA THR B 83 -11.143 -4.915 -42.578 1.00 39.21 C ANISOU 2319 CA THR B 83 4115 6230 4553 -648 -399 427 C ATOM 2320 C THR B 83 -10.284 -4.892 -41.317 1.00 37.95 C ANISOU 2320 C THR B 83 4092 5782 4547 -581 -394 400 C ATOM 2321 O THR B 83 -9.314 -4.135 -41.231 1.00 37.12 O ANISOU 2321 O THR B 83 4042 5498 4564 -447 -398 440 O ATOM 2322 CB THR B 83 -11.081 -6.326 -43.204 1.00 39.79 C ANISOU 2322 CB THR B 83 4251 6330 4539 -880 -370 323 C ATOM 2323 OG1 THR B 83 -9.724 -6.792 -43.232 1.00 39.15 O ANISOU 2323 OG1 THR B 83 4333 5972 4569 -889 -347 276 O ATOM 2324 CG2 THR B 83 -11.651 -6.327 -44.619 1.00 41.02 C ANISOU 2324 CG2 THR B 83 4286 6750 4549 -953 -376 343 C ATOM 2325 N SER B 84 -10.635 -5.736 -40.350 1.00 37.86 N ANISOU 2325 N SER B 84 4133 5734 4519 -683 -380 330 N ATOM 2326 CA SER B 84 -9.842 -5.893 -39.125 1.00 36.91 C ANISOU 2326 CA SER B 84 4141 5357 4525 -637 -374 298 C ATOM 2327 C SER B 84 -8.423 -6.442 -39.375 1.00 35.99 C ANISOU 2327 C SER B 84 4167 5011 4496 -658 -354 254 C ATOM 2328 O SER B 84 -7.524 -6.203 -38.574 1.00 35.33 O ANISOU 2328 O SER B 84 4166 4729 4531 -568 -357 256 O ATOM 2329 CB SER B 84 -10.577 -6.798 -38.134 1.00 37.17 C ANISOU 2329 CB SER B 84 4205 5416 4502 -756 -355 232 C ATOM 2330 OG SER B 84 -10.771 -8.083 -38.693 1.00 37.99 O ANISOU 2330 OG SER B 84 4360 5568 4505 -958 -316 150 O ATOM 2331 N ASP B 85 -8.231 -7.169 -40.477 1.00 36.34 N ANISOU 2331 N ASP B 85 4236 5096 4475 -774 -330 217 N ATOM 2332 CA ASP B 85 -6.899 -7.628 -40.904 1.00 35.68 C ANISOU 2332 CA ASP B 85 4275 4820 4462 -777 -305 189 C ATOM 2333 C ASP B 85 -5.939 -6.470 -41.231 1.00 34.32 C ANISOU 2333 C ASP B 85 4082 4558 4402 -613 -333 259 C ATOM 2334 O ASP B 85 -4.723 -6.636 -41.150 1.00 33.65 O ANISOU 2334 O ASP B 85 4090 4290 4405 -575 -321 246 O ATOM 2335 CB ASP B 85 -7.022 -8.554 -42.122 1.00 36.95 C ANISOU 2335 CB ASP B 85 4460 5067 4514 -937 -267 138 C ATOM 2336 CG ASP B 85 -5.739 -9.315 -42.415 1.00 37.19 C ANISOU 2336 CG ASP B 85 4642 4890 4600 -957 -222 96 C ATOM 2337 OD1 ASP B 85 -5.296 -10.087 -41.538 1.00 37.61 O ANISOU 2337 OD1 ASP B 85 4821 4781 4689 -974 -186 51 O ATOM 2338 OD2 ASP B 85 -5.175 -9.150 -43.521 1.00 37.72 O ANISOU 2338 OD2 ASP B 85 4701 4962 4667 -947 -219 114 O ATOM 2339 N ASP B 86 -6.487 -5.312 -41.598 1.00 33.76 N ANISOU 2339 N ASP B 86 3891 4619 4318 -516 -363 336 N ATOM 2340 CA ASP B 86 -5.686 -4.112 -41.876 1.00 32.67 C ANISOU 2340 CA ASP B 86 3742 4394 4275 -366 -377 405 C ATOM 2341 C ASP B 86 -5.232 -3.341 -40.634 1.00 31.26 C ANISOU 2341 C ASP B 86 3603 4064 4211 -246 -387 425 C ATOM 2342 O ASP B 86 -4.365 -2.472 -40.744 1.00 30.59 O ANISOU 2342 O ASP B 86 3540 3870 4212 -149 -388 463 O ATOM 2343 CB ASP B 86 -6.451 -3.166 -42.806 1.00 33.46 C ANISOU 2343 CB ASP B 86 3718 4690 4307 -297 -388 488 C ATOM 2344 CG ASP B 86 -6.788 -3.805 -44.139 1.00 34.31 C ANISOU 2344 CG ASP B 86 3778 4961 4299 -412 -380 471 C ATOM 2345 OD1 ASP B 86 -5.903 -4.456 -44.738 1.00 34.06 O ANISOU 2345 OD1 ASP B 86 3826 4828 4288 -482 -363 426 O ATOM 2346 OD2 ASP B 86 -7.942 -3.656 -44.591 1.00 35.28 O ANISOU 2346 OD2 ASP B 86 3781 5325 4300 -432 -390 505 O ATOM 2347 N SER B 87 -5.811 -3.636 -39.468 1.00 30.47 N ANISOU 2347 N SER B 87 3513 3961 4105 -264 -392 398 N ATOM 2348 CA SER B 87 -5.376 -3.004 -38.220 1.00 29.39 C ANISOU 2348 CA SER B 87 3420 3680 4066 -168 -400 406 C ATOM 2349 C SER B 87 -3.924 -3.386 -37.913 1.00 28.11 C ANISOU 2349 C SER B 87 3362 3322 3997 -171 -395 365 C ATOM 2350 O SER B 87 -3.615 -4.556 -37.673 1.00 27.92 O ANISOU 2350 O SER B 87 3407 3242 3960 -254 -381 306 O ATOM 2351 CB SER B 87 -6.284 -3.381 -37.043 1.00 29.57 C ANISOU 2351 CB SER B 87 3437 3743 4056 -197 -403 380 C ATOM 2352 OG SER B 87 -7.581 -2.833 -37.209 1.00 30.38 O ANISOU 2352 OG SER B 87 3429 4038 4077 -165 -408 431 O ATOM 2353 N ALA B 88 -3.042 -2.392 -37.949 1.00 27.08 N ANISOU 2353 N ALA B 88 3244 3095 3951 -79 -399 400 N ATOM 2354 CA ALA B 88 -1.601 -2.620 -37.843 1.00 26.19 C ANISOU 2354 CA ALA B 88 3202 2834 3915 -76 -396 371 C ATOM 2355 C ALA B 88 -0.880 -1.301 -37.631 1.00 25.57 C ANISOU 2355 C ALA B 88 3126 2673 3918 16 -398 407 C ATOM 2356 O ALA B 88 -1.509 -0.245 -37.585 1.00 25.84 O ANISOU 2356 O ALA B 88 3125 2745 3949 82 -391 456 O ATOM 2357 CB ALA B 88 -1.081 -3.295 -39.110 1.00 26.19 C ANISOU 2357 CB ALA B 88 3216 2850 3887 -134 -381 360 C ATOM 2358 N VAL B 89 0.438 -1.379 -37.483 1.00 24.78 N ANISOU 2358 N VAL B 89 3071 2464 3881 18 -398 384 N ATOM 2359 CA VAL B 89 1.311 -0.217 -37.560 1.00 24.41 C ANISOU 2359 CA VAL B 89 3030 2344 3899 70 -390 408 C ATOM 2360 C VAL B 89 1.943 -0.246 -38.946 1.00 24.21 C ANISOU 2360 C VAL B 89 2995 2333 3872 57 -377 426 C ATOM 2361 O VAL B 89 2.425 -1.297 -39.384 1.00 24.06 O ANISOU 2361 O VAL B 89 2992 2315 3836 9 -377 397 O ATOM 2362 CB VAL B 89 2.415 -0.255 -36.482 1.00 24.06 C ANISOU 2362 CB VAL B 89 3026 2201 3915 70 -400 368 C ATOM 2363 CG1 VAL B 89 3.325 0.966 -36.600 1.00 24.17 C ANISOU 2363 CG1 VAL B 89 3047 2152 3984 96 -385 383 C ATOM 2364 CG2 VAL B 89 1.797 -0.342 -35.092 1.00 23.97 C ANISOU 2364 CG2 VAL B 89 3029 2179 3901 79 -414 346 C ATOM 2365 N TYR B 90 1.937 0.900 -39.624 1.00 24.07 N ANISOU 2365 N TYR B 90 2960 2319 3866 103 -357 476 N ATOM 2366 CA TYR B 90 2.494 1.020 -40.968 1.00 24.02 C ANISOU 2366 CA TYR B 90 2942 2328 3856 97 -341 501 C ATOM 2367 C TYR B 90 3.689 1.964 -40.957 1.00 23.84 C ANISOU 2367 C TYR B 90 2950 2207 3903 116 -321 505 C ATOM 2368 O TYR B 90 3.620 3.050 -40.389 1.00 24.03 O ANISOU 2368 O TYR B 90 2997 2177 3956 156 -301 522 O ATOM 2369 CB TYR B 90 1.420 1.483 -41.955 1.00 24.43 C ANISOU 2369 CB TYR B 90 2947 2492 3844 132 -327 562 C ATOM 2370 CG TYR B 90 0.353 0.435 -42.152 1.00 24.53 C ANISOU 2370 CG TYR B 90 2918 2630 3771 80 -346 548 C ATOM 2371 CD1 TYR B 90 0.548 -0.626 -43.036 1.00 24.57 C ANISOU 2371 CD1 TYR B 90 2922 2682 3733 2 -348 519 C ATOM 2372 CD2 TYR B 90 -0.839 0.475 -41.423 1.00 24.75 C ANISOU 2372 CD2 TYR B 90 2915 2732 3756 97 -355 557 C ATOM 2373 CE1 TYR B 90 -0.418 -1.612 -43.201 1.00 24.85 C ANISOU 2373 CE1 TYR B 90 2933 2832 3679 -73 -355 493 C ATOM 2374 CE2 TYR B 90 -1.813 -0.506 -41.585 1.00 24.97 C ANISOU 2374 CE2 TYR B 90 2903 2889 3696 27 -368 535 C ATOM 2375 CZ TYR B 90 -1.599 -1.545 -42.475 1.00 25.10 C ANISOU 2375 CZ TYR B 90 2925 2947 3665 -67 -366 500 C ATOM 2376 OH TYR B 90 -2.556 -2.519 -42.649 1.00 25.56 O ANISOU 2376 OH TYR B 90 2954 3132 3624 -162 -369 468 O ATOM 2377 N PHE B 91 4.787 1.520 -41.564 1.00 23.49 N ANISOU 2377 N PHE B 91 2909 2139 3878 82 -320 486 N ATOM 2378 CA PHE B 91 6.014 2.304 -41.654 1.00 23.45 C ANISOU 2378 CA PHE B 91 2920 2062 3926 78 -300 483 C ATOM 2379 C PHE B 91 6.312 2.628 -43.104 1.00 23.72 C ANISOU 2379 C PHE B 91 2944 2116 3950 82 -274 522 C ATOM 2380 O PHE B 91 6.052 1.812 -43.989 1.00 23.69 O ANISOU 2380 O PHE B 91 2920 2177 3904 67 -281 528 O ATOM 2381 CB PHE B 91 7.201 1.515 -41.108 1.00 23.06 C ANISOU 2381 CB PHE B 91 2872 1986 3903 43 -319 433 C ATOM 2382 CG PHE B 91 7.174 1.312 -39.623 1.00 22.80 C ANISOU 2382 CG PHE B 91 2850 1929 3883 41 -343 395 C ATOM 2383 CD1 PHE B 91 7.550 2.339 -38.762 1.00 22.88 C ANISOU 2383 CD1 PHE B 91 2874 1889 3929 36 -335 382 C ATOM 2384 CD2 PHE B 91 6.808 0.087 -39.083 1.00 22.46 C ANISOU 2384 CD2 PHE B 91 2812 1909 3811 38 -365 370 C ATOM 2385 CE1 PHE B 91 7.544 2.153 -37.391 1.00 22.74 C ANISOU 2385 CE1 PHE B 91 2864 1858 3917 32 -357 346 C ATOM 2386 CE2 PHE B 91 6.802 -0.107 -37.710 1.00 22.30 C ANISOU 2386 CE2 PHE B 91 2805 1869 3800 43 -385 340 C ATOM 2387 CZ PHE B 91 7.169 0.925 -36.861 1.00 22.43 C ANISOU 2387 CZ PHE B 91 2822 1849 3851 41 -386 328 C ATOM 2388 N CYS B 92 6.865 3.814 -43.340 1.00 24.07 N ANISOU 2388 N CYS B 92 3012 2103 4029 94 -237 544 N ATOM 2389 CA CYS B 92 7.554 4.092 -44.586 1.00 24.32 C ANISOU 2389 CA CYS B 92 3041 2136 4064 85 -209 569 C ATOM 2390 C CYS B 92 9.058 4.030 -44.321 1.00 24.02 C ANISOU 2390 C CYS B 92 3003 2054 4071 32 -209 525 C ATOM 2391 O CYS B 92 9.513 4.175 -43.184 1.00 23.78 O ANISOU 2391 O CYS B 92 2980 1988 4067 7 -219 484 O ATOM 2392 CB CYS B 92 7.133 5.431 -45.198 1.00 25.21 C ANISOU 2392 CB CYS B 92 3186 2222 4170 135 -155 633 C ATOM 2393 SG CYS B 92 7.480 6.910 -44.223 1.00 26.09 S ANISOU 2393 SG CYS B 92 3375 2209 4327 137 -100 626 S ATOM 2394 N ALA B 93 9.813 3.773 -45.379 1.00 23.84 N ANISOU 2394 N ALA B 93 2962 2050 4045 14 -197 533 N ATOM 2395 CA ALA B 93 11.264 3.739 -45.310 1.00 23.84 C ANISOU 2395 CA ALA B 93 2945 2036 4075 -32 -192 500 C ATOM 2396 C ALA B 93 11.853 4.155 -46.653 1.00 24.01 C ANISOU 2396 C ALA B 93 2965 2060 4096 -42 -154 531 C ATOM 2397 O ALA B 93 11.130 4.335 -47.637 1.00 24.06 O ANISOU 2397 O ALA B 93 2983 2083 4076 -10 -137 577 O ATOM 2398 CB ALA B 93 11.747 2.349 -44.903 1.00 23.50 C ANISOU 2398 CB ALA B 93 2871 2036 4021 -34 -228 464 C ATOM 2399 N ARG B 94 13.170 4.309 -46.674 1.00 24.16 N ANISOU 2399 N ARG B 94 2963 2077 4138 -88 -141 506 N ATOM 2400 CA ARG B 94 13.897 4.793 -47.834 1.00 24.49 C ANISOU 2400 CA ARG B 94 3004 2117 4183 -111 -100 528 C ATOM 2401 C ARG B 94 14.797 3.679 -48.350 1.00 24.09 C ANISOU 2401 C ARG B 94 2903 2130 4121 -113 -116 515 C ATOM 2402 O ARG B 94 15.470 3.018 -47.559 1.00 23.91 O ANISOU 2402 O ARG B 94 2843 2142 4101 -119 -142 479 O ATOM 2403 CB ARG B 94 14.722 5.974 -47.375 1.00 25.32 C ANISOU 2403 CB ARG B 94 3128 2177 4317 -177 -61 506 C ATOM 2404 CG ARG B 94 15.345 6.852 -48.438 1.00 26.17 C ANISOU 2404 CG ARG B 94 3259 2256 4429 -213 0 530 C ATOM 2405 CD ARG B 94 16.418 7.636 -47.713 1.00 26.96 C ANISOU 2405 CD ARG B 94 3360 2339 4545 -312 29 480 C ATOM 2406 NE ARG B 94 17.023 8.704 -48.470 1.00 27.99 N ANISOU 2406 NE ARG B 94 3535 2422 4679 -373 103 491 N ATOM 2407 CZ ARG B 94 18.176 9.286 -48.150 1.00 28.68 C ANISOU 2407 CZ ARG B 94 3609 2521 4768 -485 136 443 C ATOM 2408 NH1 ARG B 94 18.879 8.905 -47.078 1.00 28.75 N ANISOU 2408 NH1 ARG B 94 3546 2606 4770 -543 94 384 N ATOM 2409 NH2 ARG B 94 18.638 10.258 -48.917 1.00 29.64 N ANISOU 2409 NH2 ARG B 94 3785 2589 4887 -545 214 455 N ATOM 2410 N PHE B 95 14.797 3.460 -49.664 1.00 23.86 N ANISOU 2410 N PHE B 95 2875 2119 4073 -99 -96 547 N ATOM 2411 CA PHE B 95 15.675 2.464 -50.282 1.00 23.76 C ANISOU 2411 CA PHE B 95 2828 2155 4044 -94 -96 539 C ATOM 2412 C PHE B 95 17.050 3.081 -50.530 1.00 24.23 C ANISOU 2412 C PHE B 95 2852 2230 4125 -139 -66 532 C ATOM 2413 O PHE B 95 17.182 4.032 -51.306 1.00 24.57 O ANISOU 2413 O PHE B 95 2914 2245 4176 -168 -26 556 O ATOM 2414 CB PHE B 95 15.073 1.953 -51.596 1.00 23.65 C ANISOU 2414 CB PHE B 95 2834 2160 3992 -71 -83 571 C ATOM 2415 CG PHE B 95 15.819 0.790 -52.204 1.00 23.65 C ANISOU 2415 CG PHE B 95 2821 2198 3968 -59 -74 561 C ATOM 2416 CD1 PHE B 95 15.870 -0.439 -51.556 1.00 23.47 C ANISOU 2416 CD1 PHE B 95 2805 2186 3925 -33 -89 533 C ATOM 2417 CD2 PHE B 95 16.469 0.922 -53.430 1.00 23.98 C ANISOU 2417 CD2 PHE B 95 2853 2256 4001 -68 -39 583 C ATOM 2418 CE1 PHE B 95 16.561 -1.514 -52.111 1.00 23.63 C ANISOU 2418 CE1 PHE B 95 2833 2229 3917 -7 -63 529 C ATOM 2419 CE2 PHE B 95 17.155 -0.148 -53.993 1.00 24.12 C ANISOU 2419 CE2 PHE B 95 2868 2303 3993 -48 -20 576 C ATOM 2420 CZ PHE B 95 17.201 -1.370 -53.331 1.00 23.93 C ANISOU 2420 CZ PHE B 95 2861 2285 3948 -14 -29 550 C ATOM 2421 N LEU B 96 18.061 2.538 -49.856 1.00 24.27 N ANISOU 2421 N LEU B 96 2803 2289 4130 -145 -81 501 N ATOM 2422 CA LEU B 96 19.458 2.899 -50.095 1.00 24.90 C ANISOU 2422 CA LEU B 96 2824 2422 4213 -190 -56 491 C ATOM 2423 C LEU B 96 20.019 1.865 -51.087 1.00 24.80 C ANISOU 2423 C LEU B 96 2789 2459 4174 -140 -42 512 C ATOM 2424 O LEU B 96 19.247 1.262 -51.836 1.00 24.48 O ANISOU 2424 O LEU B 96 2796 2388 4117 -100 -38 533 O ATOM 2425 CB LEU B 96 20.227 2.983 -48.759 1.00 25.30 C ANISOU 2425 CB LEU B 96 2815 2533 4264 -222 -80 451 C ATOM 2426 CG LEU B 96 20.125 4.303 -47.973 1.00 25.76 C ANISOU 2426 CG LEU B 96 2895 2550 4343 -310 -70 421 C ATOM 2427 CD1 LEU B 96 20.809 5.451 -48.702 1.00 26.55 C ANISOU 2427 CD1 LEU B 96 3002 2636 4450 -400 -13 420 C ATOM 2428 CD2 LEU B 96 18.687 4.677 -47.664 1.00 25.31 C ANISOU 2428 CD2 LEU B 96 2923 2391 4303 -286 -76 432 C ATOM 2429 N GLY B 97 21.335 1.684 -51.149 1.00 25.19 N ANISOU 2429 N GLY B 97 2766 2592 4212 -147 -28 505 N ATOM 2430 CA GLY B 97 21.919 0.650 -51.993 1.00 25.25 C ANISOU 2430 CA GLY B 97 2757 2646 4190 -84 -6 527 C ATOM 2431 C GLY B 97 21.649 -0.745 -51.467 1.00 24.86 C ANISOU 2431 C GLY B 97 2731 2602 4111 6 -20 526 C ATOM 2432 O GLY B 97 22.508 -1.333 -50.824 1.00 25.24 O ANISOU 2432 O GLY B 97 2723 2729 4137 55 -21 525 O ATOM 2433 N ASN B 98 20.455 -1.266 -51.747 1.00 24.18 N ANISOU 2433 N ASN B 98 2729 2442 4017 27 -23 530 N ATOM 2434 CA ASN B 98 20.065 -2.644 -51.385 1.00 23.94 C ANISOU 2434 CA ASN B 98 2752 2394 3951 98 -19 526 C ATOM 2435 C ASN B 98 19.948 -2.893 -49.871 1.00 23.79 C ANISOU 2435 C ASN B 98 2719 2386 3934 125 -54 507 C ATOM 2436 O ASN B 98 20.367 -3.932 -49.358 1.00 23.96 O ANISOU 2436 O ASN B 98 2749 2432 3923 203 -39 511 O ATOM 2437 CB ASN B 98 20.994 -3.673 -52.047 1.00 24.43 C ANISOU 2437 CB ASN B 98 2817 2492 3973 168 32 544 C ATOM 2438 CG ASN B 98 21.056 -3.507 -53.551 1.00 24.57 C ANISOU 2438 CG ASN B 98 2856 2497 3984 140 68 561 C ATOM 2439 OD1 ASN B 98 20.025 -3.512 -54.223 1.00 24.23 O ANISOU 2439 OD1 ASN B 98 2877 2400 3931 103 69 558 O ATOM 2440 ND2 ASN B 98 22.261 -3.357 -54.086 1.00 25.13 N ANISOU 2440 ND2 ASN B 98 2864 2632 4051 157 97 579 N ATOM 2441 N TYR B 99 19.388 -1.906 -49.177 1.00 23.49 N ANISOU 2441 N TYR B 99 2667 2327 3931 67 -92 490 N ATOM 2442 CA TYR B 99 18.921 -2.046 -47.799 1.00 23.26 C ANISOU 2442 CA TYR B 99 2644 2290 3905 80 -128 468 C ATOM 2443 C TYR B 99 18.010 -0.854 -47.489 1.00 22.97 C ANISOU 2443 C TYR B 99 2622 2202 3905 11 -155 456 C ATOM 2444 O TYR B 99 18.008 0.126 -48.239 1.00 22.98 O ANISOU 2444 O TYR B 99 2620 2184 3926 -39 -139 467 O ATOM 2445 CB TYR B 99 20.082 -2.123 -46.802 1.00 23.75 C ANISOU 2445 CB TYR B 99 2623 2445 3956 108 -141 461 C ATOM 2446 CG TYR B 99 20.984 -0.916 -46.786 1.00 24.23 C ANISOU 2446 CG TYR B 99 2600 2571 4036 31 -145 450 C ATOM 2447 CD1 TYR B 99 22.068 -0.817 -47.660 1.00 24.79 C ANISOU 2447 CD1 TYR B 99 2615 2711 4095 25 -114 467 C ATOM 2448 CD2 TYR B 99 20.760 0.134 -45.892 1.00 24.23 C ANISOU 2448 CD2 TYR B 99 2584 2562 4060 -46 -173 419 C ATOM 2449 CE1 TYR B 99 22.899 0.295 -47.647 1.00 25.37 C ANISOU 2449 CE1 TYR B 99 2614 2848 4177 -66 -110 450 C ATOM 2450 CE2 TYR B 99 21.588 1.247 -45.870 1.00 24.87 C ANISOU 2450 CE2 TYR B 99 2605 2696 4148 -140 -163 399 C ATOM 2451 CZ TYR B 99 22.655 1.322 -46.747 1.00 25.45 C ANISOU 2451 CZ TYR B 99 2619 2843 4207 -155 -132 413 C ATOM 2452 OH TYR B 99 23.472 2.424 -46.721 1.00 26.28 O ANISOU 2452 OH TYR B 99 2668 3004 4311 -267 -116 387 O ATOM 2453 N PHE B 100 17.236 -0.944 -46.408 1.00 22.70 N ANISOU 2453 N PHE B 100 2611 2140 3873 17 -185 439 N ATOM 2454 CA PHE B 100 16.338 0.144 -45.999 1.00 22.53 C ANISOU 2454 CA PHE B 100 2611 2070 3881 -31 -202 431 C ATOM 2455 C PHE B 100 17.018 0.977 -44.922 1.00 22.92 C ANISOU 2455 C PHE B 100 2615 2145 3949 -74 -216 403 C ATOM 2456 O PHE B 100 17.733 0.451 -44.068 1.00 23.12 O ANISOU 2456 O PHE B 100 2593 2233 3957 -52 -234 387 O ATOM 2457 CB PHE B 100 15.014 -0.383 -45.412 1.00 22.08 C ANISOU 2457 CB PHE B 100 2606 1974 3811 -7 -224 425 C ATOM 2458 CG PHE B 100 14.034 -0.951 -46.417 1.00 21.86 C ANISOU 2458 CG PHE B 100 2625 1928 3753 2 -211 444 C ATOM 2459 CD1 PHE B 100 14.395 -1.304 -47.722 1.00 22.07 C ANISOU 2459 CD1 PHE B 100 2656 1969 3759 3 -180 462 C ATOM 2460 CD2 PHE B 100 12.723 -1.189 -46.011 1.00 21.59 C ANISOU 2460 CD2 PHE B 100 2626 1876 3700 3 -228 439 C ATOM 2461 CE1 PHE B 100 13.463 -1.861 -48.589 1.00 21.97 C ANISOU 2461 CE1 PHE B 100 2685 1957 3706 -4 -168 472 C ATOM 2462 CE2 PHE B 100 11.791 -1.734 -46.876 1.00 21.54 C ANISOU 2462 CE2 PHE B 100 2652 1882 3650 -7 -217 450 C ATOM 2463 CZ PHE B 100 12.160 -2.076 -48.164 1.00 21.76 C ANISOU 2463 CZ PHE B 100 2686 1927 3654 -15 -188 464 C ATOM 2464 N ASP B 101 16.765 2.277 -44.951 1.00 23.19 N ANISOU 2464 N ASP B 101 2669 2134 4010 -134 -202 400 N ATOM 2465 CA ASP B 101 17.208 3.174 -43.890 1.00 23.66 C ANISOU 2465 CA ASP B 101 2708 2201 4080 -198 -205 363 C ATOM 2466 C ASP B 101 16.164 4.272 -43.734 1.00 23.64 C ANISOU 2466 C ASP B 101 2781 2101 4099 -223 -185 368 C ATOM 2467 O ASP B 101 15.224 4.348 -44.526 1.00 23.25 O ANISOU 2467 O ASP B 101 2780 2003 4053 -184 -170 406 O ATOM 2468 CB ASP B 101 18.582 3.761 -44.246 1.00 24.44 C ANISOU 2468 CB ASP B 101 2750 2361 4174 -270 -178 349 C ATOM 2469 CG ASP B 101 19.415 4.128 -43.027 1.00 25.02 C ANISOU 2469 CG ASP B 101 2765 2510 4232 -338 -194 301 C ATOM 2470 OD1 ASP B 101 18.887 4.163 -41.893 1.00 24.86 O ANISOU 2470 OD1 ASP B 101 2763 2472 4210 -337 -220 277 O ATOM 2471 OD2 ASP B 101 20.621 4.390 -43.210 1.00 25.85 O ANISOU 2471 OD2 ASP B 101 2799 2706 4317 -399 -179 285 O ATOM 2472 N ASN B 102 16.318 5.094 -42.698 1.00 24.21 N ANISOU 2472 N ASN B 102 2865 2156 4178 -284 -180 330 N ATOM 2473 CA ASN B 102 15.492 6.289 -42.493 1.00 24.60 C ANISOU 2473 CA ASN B 102 3001 2103 4243 -308 -139 334 C ATOM 2474 C ASN B 102 14.007 5.941 -42.355 1.00 24.22 C ANISOU 2474 C ASN B 102 2996 2011 4196 -223 -159 366 C ATOM 2475 O ASN B 102 13.145 6.575 -42.974 1.00 24.35 O ANISOU 2475 O ASN B 102 3072 1967 4214 -188 -122 409 O ATOM 2476 CB ASN B 102 15.710 7.291 -43.634 1.00 25.08 C ANISOU 2476 CB ASN B 102 3109 2107 4313 -343 -72 361 C ATOM 2477 CG ASN B 102 17.175 7.513 -43.938 1.00 25.75 C ANISOU 2477 CG ASN B 102 3140 2252 4390 -433 -52 331 C ATOM 2478 OD1 ASN B 102 17.677 7.065 -44.962 1.00 25.68 O ANISOU 2478 OD1 ASN B 102 3090 2288 4378 -415 -50 356 O ATOM 2479 ND2 ASN B 102 17.875 8.185 -43.035 1.00 26.43 N ANISOU 2479 ND2 ASN B 102 3222 2353 4467 -538 -35 274 N ATOM 2480 N TRP B 103 13.718 4.934 -41.530 1.00 23.97 N ANISOU 2480 N TRP B 103 2933 2022 4153 -186 -212 349 N ATOM 2481 CA TRP B 103 12.346 4.488 -41.301 1.00 23.66 C ANISOU 2481 CA TRP B 103 2923 1962 4105 -120 -233 371 C ATOM 2482 C TRP B 103 11.565 5.621 -40.651 1.00 24.29 C ANISOU 2482 C TRP B 103 3067 1968 4195 -124 -204 373 C ATOM 2483 O TRP B 103 12.094 6.328 -39.786 1.00 24.69 O ANISOU 2483 O TRP B 103 3135 1991 4255 -183 -188 332 O ATOM 2484 CB TRP B 103 12.295 3.265 -40.376 1.00 23.15 C ANISOU 2484 CB TRP B 103 2827 1946 4025 -93 -285 345 C ATOM 2485 CG TRP B 103 12.845 1.978 -40.949 1.00 22.89 C ANISOU 2485 CG TRP B 103 2756 1970 3972 -64 -300 352 C ATOM 2486 CD1 TRP B 103 14.150 1.693 -41.222 1.00 23.20 C ANISOU 2486 CD1 TRP B 103 2746 2062 4006 -77 -297 344 C ATOM 2487 CD2 TRP B 103 12.101 0.792 -41.270 1.00 22.38 C ANISOU 2487 CD2 TRP B 103 2709 1916 3880 -18 -312 366 C ATOM 2488 NE1 TRP B 103 14.266 0.408 -41.701 1.00 23.00 N ANISOU 2488 NE1 TRP B 103 2717 2068 3956 -25 -300 357 N ATOM 2489 CE2 TRP B 103 13.024 -0.166 -41.747 1.00 22.48 C ANISOU 2489 CE2 TRP B 103 2699 1969 3875 2 -306 367 C ATOM 2490 CE3 TRP B 103 10.743 0.449 -41.211 1.00 22.03 C ANISOU 2490 CE3 TRP B 103 2699 1857 3815 2 -320 376 C ATOM 2491 CZ2 TRP B 103 12.635 -1.450 -42.162 1.00 22.22 C ANISOU 2491 CZ2 TRP B 103 2698 1940 3806 36 -299 373 C ATOM 2492 CZ3 TRP B 103 10.353 -0.831 -41.623 1.00 21.84 C ANISOU 2492 CZ3 TRP B 103 2693 1853 3752 19 -320 377 C ATOM 2493 CH2 TRP B 103 11.301 -1.762 -42.095 1.00 21.94 C ANISOU 2493 CH2 TRP B 103 2703 1883 3749 33 -305 374 C ATOM 2494 N GLY B 104 10.316 5.801 -41.072 1.00 24.69 N ANISOU 2494 N GLY B 104 3151 1995 4233 -61 -190 419 N ATOM 2495 CA GLY B 104 9.413 6.742 -40.414 1.00 25.41 C ANISOU 2495 CA GLY B 104 3305 2022 4325 -35 -157 432 C ATOM 2496 C GLY B 104 9.064 6.283 -39.008 1.00 25.53 C ANISOU 2496 C GLY B 104 3313 2047 4339 -36 -199 391 C ATOM 2497 O GLY B 104 9.343 5.135 -38.630 1.00 24.93 O ANISOU 2497 O GLY B 104 3185 2030 4257 -43 -253 364 O ATOM 2498 N GLN B 105 8.464 7.183 -38.231 1.00 26.39 N ANISOU 2498 N GLN B 105 3484 2091 4450 -25 -165 391 N ATOM 2499 CA GLN B 105 8.074 6.877 -36.845 1.00 26.61 C ANISOU 2499 CA GLN B 105 3513 2122 4476 -26 -198 353 C ATOM 2500 C GLN B 105 6.945 5.845 -36.732 1.00 26.28 C ANISOU 2500 C GLN B 105 3434 2140 4410 39 -244 375 C ATOM 2501 O GLN B 105 6.728 5.289 -35.659 1.00 26.06 O ANISOU 2501 O GLN B 105 3396 2129 4378 35 -281 343 O ATOM 2502 CB GLN B 105 7.727 8.158 -36.060 1.00 27.45 C ANISOU 2502 CB GLN B 105 3709 2134 4586 -32 -137 344 C ATOM 2503 CG GLN B 105 6.311 8.719 -36.218 1.00 27.82 C ANISOU 2503 CG GLN B 105 3807 2148 4615 69 -94 408 C ATOM 2504 CD GLN B 105 6.096 9.535 -37.485 1.00 28.58 C ANISOU 2504 CD GLN B 105 3947 2210 4703 121 -25 476 C ATOM 2505 OE1 GLN B 105 6.874 9.465 -38.444 1.00 28.75 O ANISOU 2505 OE1 GLN B 105 3947 2245 4733 85 -22 481 O ATOM 2506 NE2 GLN B 105 5.027 10.324 -37.492 1.00 29.13 N ANISOU 2506 NE2 GLN B 105 4079 2240 4750 216 35 535 N ATOM 2507 N GLY B 106 6.226 5.606 -37.830 1.00 26.56 N ANISOU 2507 N GLY B 106 3451 2218 4424 89 -239 429 N ATOM 2508 CA GLY B 106 5.117 4.661 -37.858 1.00 26.56 C ANISOU 2508 CA GLY B 106 3414 2292 4386 128 -275 447 C ATOM 2509 C GLY B 106 3.784 5.363 -37.659 1.00 27.17 C ANISOU 2509 C GLY B 106 3512 2375 4437 199 -247 493 C ATOM 2510 O GLY B 106 3.714 6.405 -37.012 1.00 27.50 O ANISOU 2510 O GLY B 106 3611 2342 4495 219 -205 496 O ATOM 2511 N ALA B 107 2.735 4.787 -38.236 1.00 27.66 N ANISOU 2511 N ALA B 107 3527 2534 4449 234 -263 530 N ATOM 2512 CA ALA B 107 1.361 5.268 -38.071 1.00 28.44 C ANISOU 2512 CA ALA B 107 3619 2683 4505 311 -243 581 C ATOM 2513 C ALA B 107 0.475 4.078 -37.741 1.00 28.47 C ANISOU 2513 C ALA B 107 3566 2791 4462 288 -291 562 C ATOM 2514 O ALA B 107 0.464 3.097 -38.487 1.00 28.29 O ANISOU 2514 O ALA B 107 3502 2842 4406 242 -318 552 O ATOM 2515 CB ALA B 107 0.878 5.937 -39.342 1.00 28.99 C ANISOU 2515 CB ALA B 107 3674 2806 4536 380 -202 661 C ATOM 2516 N THR B 108 -0.250 4.157 -36.626 1.00 28.96 N ANISOU 2516 N THR B 108 3636 2853 4515 313 -295 553 N ATOM 2517 CA THR B 108 -1.148 3.078 -36.218 1.00 29.32 C ANISOU 2517 CA THR B 108 3634 2994 4510 282 -332 533 C ATOM 2518 C THR B 108 -2.490 3.243 -36.926 1.00 30.04 C ANISOU 2518 C THR B 108 3658 3233 4521 335 -320 598 C ATOM 2519 O THR B 108 -3.048 4.346 -36.979 1.00 30.78 O ANISOU 2519 O THR B 108 3755 3338 4602 434 -279 662 O ATOM 2520 CB THR B 108 -1.337 3.027 -34.687 1.00 29.32 C ANISOU 2520 CB THR B 108 3666 2942 4532 281 -343 493 C ATOM 2521 OG1 THR B 108 -0.069 2.777 -34.064 1.00 29.04 O ANISOU 2521 OG1 THR B 108 3676 2804 4555 229 -359 435 O ATOM 2522 CG2 THR B 108 -2.299 1.904 -34.288 1.00 29.33 C ANISOU 2522 CG2 THR B 108 3626 3042 4476 241 -373 471 C ATOM 2523 N LEU B 109 -2.978 2.141 -37.490 1.00 30.06 N ANISOU 2523 N LEU B 109 3604 3356 4461 269 -349 582 N ATOM 2524 CA LEU B 109 -4.279 2.085 -38.139 1.00 30.90 C ANISOU 2524 CA LEU B 109 3624 3648 4470 292 -347 633 C ATOM 2525 C LEU B 109 -5.140 1.109 -37.341 1.00 30.75 C ANISOU 2525 C LEU B 109 3574 3709 4399 225 -372 589 C ATOM 2526 O LEU B 109 -4.775 -0.060 -37.188 1.00 30.18 O ANISOU 2526 O LEU B 109 3531 3611 4327 118 -392 521 O ATOM 2527 CB LEU B 109 -4.114 1.624 -39.589 1.00 31.38 C ANISOU 2527 CB LEU B 109 3644 3797 4483 243 -352 644 C ATOM 2528 CG LEU B 109 -5.291 1.823 -40.550 1.00 32.60 C ANISOU 2528 CG LEU B 109 3695 4165 4526 279 -346 713 C ATOM 2529 CD1 LEU B 109 -4.800 2.147 -41.958 1.00 32.94 C ANISOU 2529 CD1 LEU B 109 3725 4233 4556 297 -332 754 C ATOM 2530 CD2 LEU B 109 -6.206 0.606 -40.573 1.00 33.04 C ANISOU 2530 CD2 LEU B 109 3685 4384 4483 164 -373 669 C ATOM 2531 N THR B 110 -6.255 1.602 -36.804 1.00 31.12 N ANISOU 2531 N THR B 110 3575 3848 4401 293 -362 630 N ATOM 2532 CA THR B 110 -7.201 0.780 -36.053 1.00 31.18 C ANISOU 2532 CA THR B 110 3544 3953 4350 230 -380 595 C ATOM 2533 C THR B 110 -8.543 0.793 -36.773 1.00 31.98 C ANISOU 2533 C THR B 110 3523 4302 4327 244 -378 650 C ATOM 2534 O THR B 110 -9.157 1.848 -36.921 1.00 32.53 O ANISOU 2534 O THR B 110 3544 4449 4368 376 -353 735 O ATOM 2535 CB THR B 110 -7.370 1.296 -34.613 1.00 31.10 C ANISOU 2535 CB THR B 110 3579 3851 4388 293 -371 590 C ATOM 2536 OG1 THR B 110 -6.083 1.400 -33.988 1.00 30.48 O ANISOU 2536 OG1 THR B 110 3601 3568 4413 283 -374 543 O ATOM 2537 CG2 THR B 110 -8.251 0.358 -33.788 1.00 31.20 C ANISOU 2537 CG2 THR B 110 3562 3950 4344 217 -389 546 C ATOM 2538 N VAL B 111 -8.970 -0.384 -37.234 1.00 32.17 N ANISOU 2538 N VAL B 111 3501 4453 4268 106 -397 602 N ATOM 2539 CA VAL B 111 -10.239 -0.560 -37.924 1.00 33.30 C ANISOU 2539 CA VAL B 111 3512 4868 4272 79 -400 639 C ATOM 2540 C VAL B 111 -11.291 -0.975 -36.899 1.00 33.70 C ANISOU 2540 C VAL B 111 3519 5019 4265 39 -404 615 C ATOM 2541 O VAL B 111 -11.128 -1.986 -36.216 1.00 33.19 O ANISOU 2541 O VAL B 111 3519 4878 4215 -84 -411 530 O ATOM 2542 CB VAL B 111 -10.129 -1.606 -39.057 1.00 33.56 C ANISOU 2542 CB VAL B 111 3525 4995 4232 -76 -409 590 C ATOM 2543 CG1 VAL B 111 -11.486 -1.842 -39.717 1.00 34.89 C ANISOU 2543 CG1 VAL B 111 3543 5478 4237 -130 -415 618 C ATOM 2544 CG2 VAL B 111 -9.092 -1.153 -40.083 1.00 33.36 C ANISOU 2544 CG2 VAL B 111 3537 4874 4263 -29 -404 618 C ATOM 2545 N SER B 112 -12.356 -0.184 -36.794 1.00 34.65 N ANISOU 2545 N SER B 112 3536 5313 4317 153 -394 696 N ATOM 2546 CA SER B 112 -13.423 -0.429 -35.819 1.00 35.15 C ANISOU 2546 CA SER B 112 3543 5493 4321 136 -394 686 C ATOM 2547 C SER B 112 -14.699 0.337 -36.164 1.00 36.51 C ANISOU 2547 C SER B 112 3559 5939 4374 257 -381 790 C ATOM 2548 O SER B 112 -14.645 1.431 -36.730 1.00 36.54 O ANISOU 2548 O SER B 112 3540 5961 4382 424 -358 887 O ATOM 2549 CB SER B 112 -12.959 -0.028 -34.415 1.00 34.41 C ANISOU 2549 CB SER B 112 3559 5171 4343 209 -384 667 C ATOM 2550 OG SER B 112 -14.015 -0.122 -33.471 1.00 34.80 O ANISOU 2550 OG SER B 112 3553 5333 4337 215 -380 670 O ATOM 2551 N SER B 113 -15.837 -0.251 -35.793 1.00 37.45 N ANISOU 2551 N SER B 113 3575 6273 4380 176 -389 771 N ATOM 2552 CA SER B 113 -17.146 0.393 -35.924 1.00 39.11 C ANISOU 2552 CA SER B 113 3621 6776 4463 294 -376 870 C ATOM 2553 C SER B 113 -17.533 1.225 -34.697 1.00 39.29 C ANISOU 2553 C SER B 113 3668 6728 4532 459 -347 921 C ATOM 2554 O SER B 113 -18.577 1.871 -34.710 1.00 40.50 O ANISOU 2554 O SER B 113 3696 7105 4586 594 -325 1016 O ATOM 2555 CB SER B 113 -18.226 -0.660 -36.179 1.00 40.12 C ANISOU 2555 CB SER B 113 3608 7209 4427 108 -396 823 C ATOM 2556 OG SER B 113 -17.981 -1.355 -37.387 1.00 40.52 O ANISOU 2556 OG SER B 113 3631 7353 4413 -42 -414 782 O ATOM 2557 N ALA B 114 -16.701 1.218 -33.652 1.00 38.32 N ANISOU 2557 N ALA B 114 3703 6308 4550 454 -342 861 N ATOM 2558 CA ALA B 114 -17.031 1.869 -32.382 1.00 38.55 C ANISOU 2558 CA ALA B 114 3772 6253 4622 578 -314 888 C ATOM 2559 C ALA B 114 -17.012 3.395 -32.464 1.00 39.38 C ANISOU 2559 C ALA B 114 3903 6304 4758 826 -259 1006 C ATOM 2560 O ALA B 114 -16.243 3.977 -33.234 1.00 39.08 O ANISOU 2560 O ALA B 114 3921 6156 4770 891 -243 1041 O ATOM 2561 CB ALA B 114 -16.078 1.401 -31.290 1.00 37.16 C ANISOU 2561 CB ALA B 114 3757 5785 4578 491 -326 788 C ATOM 2562 N SER B 115 -17.870 4.024 -31.663 1.00 40.71 N ANISOU 2562 N SER B 115 4037 6543 4890 963 -221 1066 N ATOM 2563 CA SER B 115 -17.884 5.477 -31.491 1.00 41.80 C ANISOU 2563 CA SER B 115 4236 6589 5057 1206 -146 1173 C ATOM 2564 C SER B 115 -17.045 5.866 -30.281 1.00 41.04 C ANISOU 2564 C SER B 115 4325 6167 5102 1219 -122 1115 C ATOM 2565 O SER B 115 -16.744 5.031 -29.423 1.00 40.22 O ANISOU 2565 O SER B 115 4267 5966 5050 1071 -164 1011 O ATOM 2566 CB SER B 115 -19.312 5.988 -31.294 1.00 43.42 C ANISOU 2566 CB SER B 115 4305 7061 5132 1367 -105 1280 C ATOM 2567 OG SER B 115 -20.106 5.749 -32.439 1.00 44.91 O ANISOU 2567 OG SER B 115 4306 7583 5173 1371 -124 1345 O ATOM 2568 N THR B 116 -16.694 7.147 -30.214 1.00 41.62 N ANISOU 2568 N THR B 116 4507 6080 5225 1397 -47 1185 N ATOM 2569 CA THR B 116 -15.904 7.685 -29.111 1.00 41.10 C ANISOU 2569 CA THR B 116 4621 5716 5280 1413 -11 1135 C ATOM 2570 C THR B 116 -16.713 7.652 -27.812 1.00 41.44 C ANISOU 2570 C THR B 116 4655 5791 5299 1447 5 1125 C ATOM 2571 O THR B 116 -17.829 8.165 -27.758 1.00 42.67 O ANISOU 2571 O THR B 116 4730 6123 5361 1601 54 1221 O ATOM 2572 CB THR B 116 -15.427 9.120 -29.420 1.00 41.71 C ANISOU 2572 CB THR B 116 4828 5624 5396 1589 86 1214 C ATOM 2573 OG1 THR B 116 -14.583 9.093 -30.579 1.00 41.38 O ANISOU 2573 OG1 THR B 116 4801 5537 5385 1540 68 1212 O ATOM 2574 CG2 THR B 116 -14.647 9.719 -28.248 1.00 41.28 C ANISOU 2574 CG2 THR B 116 4961 5273 5449 1586 132 1154 C ATOM 2575 N LYS B 117 -16.142 7.032 -26.779 1.00 40.49 N ANISOU 2575 N LYS B 117 4614 5513 5258 1308 -35 1014 N ATOM 2576 CA LYS B 117 -16.806 6.872 -25.486 1.00 40.73 C ANISOU 2576 CA LYS B 117 4644 5559 5274 1313 -28 989 C ATOM 2577 C LYS B 117 -15.794 6.996 -24.354 1.00 39.84 C ANISOU 2577 C LYS B 117 4698 5162 5277 1252 -26 900 C ATOM 2578 O LYS B 117 -14.714 6.402 -24.418 1.00 38.79 O ANISOU 2578 O LYS B 117 4622 4898 5219 1110 -78 815 O ATOM 2579 CB LYS B 117 -17.492 5.505 -25.415 1.00 40.64 C ANISOU 2579 CB LYS B 117 4496 5754 5191 1158 -101 937 C ATOM 2580 CG LYS B 117 -18.365 5.304 -24.187 1.00 41.01 C ANISOU 2580 CG LYS B 117 4516 5864 5201 1167 -91 923 C ATOM 2581 CD LYS B 117 -19.184 4.031 -24.302 1.00 41.37 C ANISOU 2581 CD LYS B 117 4416 6150 5151 1014 -147 883 C ATOM 2582 CE LYS B 117 -20.114 3.852 -23.110 1.00 41.94 C ANISOU 2582 CE LYS B 117 4453 6302 5178 1024 -133 875 C ATOM 2583 NZ LYS B 117 -19.391 3.431 -21.877 1.00 40.96 N ANISOU 2583 NZ LYS B 117 4470 5939 5154 929 -150 775 N ATOM 2584 N GLY B 118 -16.154 7.758 -23.321 1.00 40.38 N ANISOU 2584 N GLY B 118 4841 5150 5352 1360 37 920 N ATOM 2585 CA GLY B 118 -15.316 7.913 -22.134 1.00 39.73 C ANISOU 2585 CA GLY B 118 4908 4827 5361 1300 43 835 C ATOM 2586 C GLY B 118 -15.442 6.727 -21.192 1.00 39.01 C ANISOU 2586 C GLY B 118 4780 4768 5274 1156 -28 746 C ATOM 2587 O GLY B 118 -16.474 6.053 -21.185 1.00 39.41 O ANISOU 2587 O GLY B 118 4705 5023 5244 1139 -53 764 O ATOM 2588 N PRO B 119 -14.398 6.466 -20.382 1.00 38.10 N ANISOU 2588 N PRO B 119 4774 4462 5242 1050 -57 652 N ATOM 2589 CA PRO B 119 -14.426 5.317 -19.480 1.00 37.47 C ANISOU 2589 CA PRO B 119 4675 4396 5164 921 -119 572 C ATOM 2590 C PRO B 119 -15.284 5.531 -18.239 1.00 37.93 C ANISOU 2590 C PRO B 119 4746 4475 5191 979 -85 576 C ATOM 2591 O PRO B 119 -15.467 6.665 -17.792 1.00 38.91 O ANISOU 2591 O PRO B 119 4944 4520 5320 1105 -11 615 O ATOM 2592 CB PRO B 119 -12.962 5.170 -19.061 1.00 36.59 C ANISOU 2592 CB PRO B 119 4678 4082 5144 824 -150 488 C ATOM 2593 CG PRO B 119 -12.419 6.552 -19.127 1.00 37.08 C ANISOU 2593 CG PRO B 119 4845 3997 5247 916 -81 515 C ATOM 2594 CD PRO B 119 -13.130 7.214 -20.273 1.00 37.84 C ANISOU 2594 CD PRO B 119 4882 4202 5293 1041 -31 617 C ATOM 2595 N SER B 120 -15.807 4.433 -17.705 1.00 37.63 N ANISOU 2595 N SER B 120 4644 4537 5116 885 -130 535 N ATOM 2596 CA SER B 120 -16.310 4.391 -16.340 1.00 37.69 C ANISOU 2596 CA SER B 120 4683 4524 5112 896 -114 509 C ATOM 2597 C SER B 120 -15.145 3.938 -15.470 1.00 36.60 C ANISOU 2597 C SER B 120 4655 4201 5049 788 -154 414 C ATOM 2598 O SER B 120 -14.387 3.046 -15.867 1.00 36.14 O ANISOU 2598 O SER B 120 4595 4118 5017 674 -209 366 O ATOM 2599 CB SER B 120 -17.483 3.420 -16.229 1.00 38.18 C ANISOU 2599 CB SER B 120 4621 4799 5087 840 -137 513 C ATOM 2600 OG SER B 120 -18.556 3.832 -17.063 1.00 39.37 O ANISOU 2600 OG SER B 120 4647 5159 5151 939 -104 605 O ATOM 2601 N VAL B 121 -14.981 4.565 -14.305 1.00 36.38 N ANISOU 2601 N VAL B 121 4724 4050 5049 830 -120 390 N ATOM 2602 CA VAL B 121 -13.866 4.257 -13.404 1.00 35.47 C ANISOU 2602 CA VAL B 121 4706 3779 4992 740 -155 306 C ATOM 2603 C VAL B 121 -14.409 3.689 -12.094 1.00 35.38 C ANISOU 2603 C VAL B 121 4702 3788 4953 710 -163 269 C ATOM 2604 O VAL B 121 -15.181 4.346 -11.394 1.00 35.93 O ANISOU 2604 O VAL B 121 4789 3868 4994 796 -111 295 O ATOM 2605 CB VAL B 121 -12.983 5.492 -13.127 1.00 35.67 C ANISOU 2605 CB VAL B 121 4853 3631 5070 784 -109 292 C ATOM 2606 CG1 VAL B 121 -11.793 5.117 -12.241 1.00 35.05 C ANISOU 2606 CG1 VAL B 121 4850 3433 5035 678 -153 203 C ATOM 2607 CG2 VAL B 121 -12.500 6.100 -14.437 1.00 35.75 C ANISOU 2607 CG2 VAL B 121 4863 3618 5103 817 -90 332 C ATOM 2608 N PHE B 122 -13.992 2.466 -11.778 1.00 34.62 N ANISOU 2608 N PHE B 122 4600 3693 4860 595 -222 213 N ATOM 2609 CA PHE B 122 -14.438 1.756 -10.583 1.00 34.53 C ANISOU 2609 CA PHE B 122 4601 3699 4820 554 -232 177 C ATOM 2610 C PHE B 122 -13.242 1.462 -9.682 1.00 33.88 C ANISOU 2610 C PHE B 122 4610 3481 4780 494 -266 109 C ATOM 2611 O PHE B 122 -12.175 1.099 -10.179 1.00 33.27 O ANISOU 2611 O PHE B 122 4550 3351 4738 442 -303 86 O ATOM 2612 CB PHE B 122 -15.131 0.456 -10.982 1.00 34.40 C ANISOU 2612 CB PHE B 122 4503 3820 4748 470 -257 176 C ATOM 2613 CG PHE B 122 -16.273 0.660 -11.934 1.00 35.01 C ANISOU 2613 CG PHE B 122 4467 4071 4766 511 -232 240 C ATOM 2614 CD1 PHE B 122 -17.380 1.416 -11.552 1.00 35.78 C ANISOU 2614 CD1 PHE B 122 4520 4258 4818 615 -183 291 C ATOM 2615 CD2 PHE B 122 -16.238 0.123 -13.218 1.00 34.95 C ANISOU 2615 CD2 PHE B 122 4391 4150 4738 453 -253 254 C ATOM 2616 CE1 PHE B 122 -18.433 1.624 -12.429 1.00 36.48 C ANISOU 2616 CE1 PHE B 122 4486 4537 4836 667 -160 360 C ATOM 2617 CE2 PHE B 122 -17.291 0.326 -14.098 1.00 35.64 C ANISOU 2617 CE2 PHE B 122 4359 4426 4756 490 -233 315 C ATOM 2618 CZ PHE B 122 -18.392 1.075 -13.701 1.00 36.44 C ANISOU 2618 CZ PHE B 122 4404 4634 4806 600 -188 371 C ATOM 2619 N PRO B 123 -13.411 1.620 -8.357 1.00 34.10 N ANISOU 2619 N PRO B 123 4693 3466 4799 507 -252 81 N ATOM 2620 CA PRO B 123 -12.303 1.365 -7.444 1.00 33.77 C ANISOU 2620 CA PRO B 123 4726 3323 4782 456 -285 21 C ATOM 2621 C PRO B 123 -12.064 -0.127 -7.237 1.00 33.39 C ANISOU 2621 C PRO B 123 4668 3303 4714 377 -329 -5 C ATOM 2622 O PRO B 123 -13.020 -0.901 -7.177 1.00 33.67 O ANISOU 2622 O PRO B 123 4666 3421 4705 354 -320 6 O ATOM 2623 CB PRO B 123 -12.776 2.009 -6.145 1.00 34.25 C ANISOU 2623 CB PRO B 123 4840 3348 4824 499 -247 5 C ATOM 2624 CG PRO B 123 -14.256 1.868 -6.185 1.00 34.71 C ANISOU 2624 CG PRO B 123 4835 3518 4833 544 -213 51 C ATOM 2625 CD PRO B 123 -14.638 2.003 -7.631 1.00 34.77 C ANISOU 2625 CD PRO B 123 4764 3609 4839 571 -205 106 C ATOM 2626 N LEU B 124 -10.793 -0.508 -7.153 1.00 33.09 N ANISOU 2626 N LEU B 124 4668 3203 4702 337 -367 -38 N ATOM 2627 CA LEU B 124 -10.383 -1.848 -6.752 1.00 32.93 C ANISOU 2627 CA LEU B 124 4669 3185 4659 286 -396 -60 C ATOM 2628 C LEU B 124 -9.899 -1.701 -5.318 1.00 33.14 C ANISOU 2628 C LEU B 124 4753 3164 4674 295 -406 -96 C ATOM 2629 O LEU B 124 -8.743 -1.352 -5.070 1.00 32.71 O ANISOU 2629 O LEU B 124 4723 3067 4639 291 -432 -121 O ATOM 2630 CB LEU B 124 -9.287 -2.386 -7.675 1.00 32.61 C ANISOU 2630 CB LEU B 124 4624 3124 4642 257 -426 -60 C ATOM 2631 CG LEU B 124 -9.689 -2.534 -9.147 1.00 32.63 C ANISOU 2631 CG LEU B 124 4572 3176 4651 240 -417 -28 C ATOM 2632 CD1 LEU B 124 -8.476 -2.759 -10.035 1.00 32.38 C ANISOU 2632 CD1 LEU B 124 4540 3111 4651 225 -443 -28 C ATOM 2633 CD2 LEU B 124 -10.696 -3.662 -9.322 1.00 32.71 C ANISOU 2633 CD2 LEU B 124 4566 3254 4608 190 -397 -20 C ATOM 2634 N ALA B 125 -10.813 -1.937 -4.379 1.00 33.67 N ANISOU 2634 N ALA B 125 4836 3254 4704 302 -384 -100 N ATOM 2635 CA ALA B 125 -10.593 -1.616 -2.973 1.00 34.35 C ANISOU 2635 CA ALA B 125 4973 3304 4772 316 -386 -132 C ATOM 2636 C ALA B 125 -9.675 -2.630 -2.294 1.00 34.64 C ANISOU 2636 C ALA B 125 5048 3330 4785 294 -419 -152 C ATOM 2637 O ALA B 125 -9.736 -3.824 -2.608 1.00 34.37 O ANISOU 2637 O ALA B 125 5018 3312 4729 273 -419 -137 O ATOM 2638 CB ALA B 125 -11.923 -1.544 -2.237 1.00 34.62 C ANISOU 2638 CB ALA B 125 5010 3374 4772 336 -347 -125 C ATOM 2639 N PRO B 126 -8.830 -2.163 -1.352 1.00 35.51 N ANISOU 2639 N PRO B 126 5190 3417 4886 299 -441 -185 N ATOM 2640 CA PRO B 126 -8.003 -3.096 -0.594 1.00 35.96 C ANISOU 2640 CA PRO B 126 5274 3486 4903 300 -470 -194 C ATOM 2641 C PRO B 126 -8.835 -3.885 0.414 1.00 36.91 C ANISOU 2641 C PRO B 126 5434 3615 4974 308 -447 -190 C ATOM 2642 O PRO B 126 -9.797 -3.353 0.971 1.00 37.19 O ANISOU 2642 O PRO B 126 5477 3650 5003 312 -419 -199 O ATOM 2643 CB PRO B 126 -7.013 -2.182 0.124 1.00 36.17 C ANISOU 2643 CB PRO B 126 5308 3513 4923 292 -496 -234 C ATOM 2644 CG PRO B 126 -7.753 -0.906 0.308 1.00 36.29 C ANISOU 2644 CG PRO B 126 5339 3493 4958 288 -460 -254 C ATOM 2645 CD PRO B 126 -8.644 -0.771 -0.893 1.00 35.98 C ANISOU 2645 CD PRO B 126 5268 3443 4958 304 -429 -216 C ATOM 2646 N SER B 127 -8.473 -5.145 0.623 1.00 37.86 N ANISOU 2646 N SER B 127 5587 3742 5058 316 -449 -173 N ATOM 2647 CA SER B 127 -9.128 -5.997 1.622 1.00 38.83 C ANISOU 2647 CA SER B 127 5763 3864 5125 323 -421 -169 C ATOM 2648 C SER B 127 -8.140 -7.057 2.107 1.00 39.74 C ANISOU 2648 C SER B 127 5926 3981 5193 361 -430 -151 C ATOM 2649 O SER B 127 -6.977 -7.052 1.694 1.00 39.66 O ANISOU 2649 O SER B 127 5893 3986 5190 385 -463 -142 O ATOM 2650 CB SER B 127 -10.384 -6.647 1.023 1.00 38.79 C ANISOU 2650 CB SER B 127 5763 3861 5116 282 -373 -152 C ATOM 2651 OG SER B 127 -10.058 -7.666 0.090 1.00 38.70 O ANISOU 2651 OG SER B 127 5771 3833 5099 263 -358 -131 O ATOM 2652 N SER B 128 -8.601 -7.962 2.970 1.00 40.80 N ANISOU 2652 N SER B 128 6126 4104 5271 374 -396 -140 N ATOM 2653 CA SER B 128 -7.784 -9.097 3.420 1.00 41.76 C ANISOU 2653 CA SER B 128 6310 4221 5334 430 -385 -108 C ATOM 2654 C SER B 128 -7.330 -10.021 2.270 1.00 41.99 C ANISOU 2654 C SER B 128 6368 4218 5370 437 -359 -75 C ATOM 2655 O SER B 128 -6.283 -10.663 2.374 1.00 42.42 O ANISOU 2655 O SER B 128 6451 4279 5387 508 -361 -42 O ATOM 2656 CB SER B 128 -8.542 -9.919 4.469 1.00 42.41 C ANISOU 2656 CB SER B 128 6477 4281 5356 437 -335 -100 C ATOM 2657 OG SER B 128 -9.665 -10.568 3.894 1.00 42.53 O ANISOU 2657 OG SER B 128 6532 4256 5372 371 -274 -98 O ATOM 2658 N LYS B 129 -8.123 -10.087 1.195 1.00 41.99 N ANISOU 2658 N LYS B 129 6357 4191 5406 369 -331 -81 N ATOM 2659 CA LYS B 129 -7.800 -10.902 0.011 1.00 42.02 C ANISOU 2659 CA LYS B 129 6392 4159 5416 356 -300 -59 C ATOM 2660 C LYS B 129 -6.952 -10.160 -1.036 1.00 41.41 C ANISOU 2660 C LYS B 129 6232 4107 5397 365 -351 -58 C ATOM 2661 O LYS B 129 -6.591 -10.740 -2.066 1.00 40.71 O ANISOU 2661 O LYS B 129 6160 3991 5315 359 -330 -40 O ATOM 2662 CB LYS B 129 -9.085 -11.457 -0.623 1.00 42.45 C ANISOU 2662 CB LYS B 129 6478 4190 5461 261 -239 -70 C ATOM 2663 CG LYS B 129 -10.030 -12.171 0.349 1.00 43.21 C ANISOU 2663 CG LYS B 129 6656 4266 5496 230 -180 -76 C ATOM 2664 CD LYS B 129 -9.348 -13.279 1.148 1.00 44.11 C ANISOU 2664 CD LYS B 129 6892 4322 5545 302 -135 -45 C ATOM 2665 CE LYS B 129 -10.297 -13.953 2.132 1.00 44.73 C ANISOU 2665 CE LYS B 129 7059 4373 5561 267 -70 -51 C ATOM 2666 NZ LYS B 129 -11.418 -14.673 1.470 1.00 45.14 N ANISOU 2666 NZ LYS B 129 7164 4401 5587 140 7 -72 N ATOM 2667 N SER B 130 -6.642 -8.889 -0.773 1.00 40.99 N ANISOU 2667 N SER B 130 6098 4097 5381 372 -410 -81 N ATOM 2668 CA SER B 130 -5.606 -8.165 -1.507 1.00 40.87 C ANISOU 2668 CA SER B 130 6013 4107 5408 384 -458 -83 C ATOM 2669 C SER B 130 -4.485 -7.671 -0.572 1.00 41.30 C ANISOU 2669 C SER B 130 6037 4218 5436 432 -507 -92 C ATOM 2670 O SER B 130 -3.957 -6.574 -0.769 1.00 40.88 O ANISOU 2670 O SER B 130 5920 4197 5416 409 -547 -118 O ATOM 2671 CB SER B 130 -6.218 -6.991 -2.282 1.00 40.55 C ANISOU 2671 CB SER B 130 5907 4068 5431 331 -471 -106 C ATOM 2672 OG SER B 130 -6.573 -5.925 -1.419 1.00 40.40 O ANISOU 2672 OG SER B 130 5869 4063 5419 325 -486 -136 O ATOM 2673 N THR B 131 -4.122 -8.483 0.427 1.00 41.78 N ANISOU 2673 N THR B 131 6148 4300 5429 492 -497 -70 N ATOM 2674 CA THR B 131 -2.946 -8.212 1.266 1.00 42.50 C ANISOU 2674 CA THR B 131 6199 4478 5472 542 -543 -69 C ATOM 2675 C THR B 131 -1.907 -9.315 1.093 1.00 42.89 C ANISOU 2675 C THR B 131 6268 4560 5467 636 -531 -12 C ATOM 2676 O THR B 131 -2.255 -10.488 0.923 1.00 43.23 O ANISOU 2676 O THR B 131 6402 4538 5485 676 -470 28 O ATOM 2677 CB THR B 131 -3.282 -8.087 2.772 1.00 43.08 C ANISOU 2677 CB THR B 131 6298 4581 5490 554 -548 -87 C ATOM 2678 OG1 THR B 131 -3.906 -9.289 3.240 1.00 43.83 O ANISOU 2678 OG1 THR B 131 6487 4626 5539 597 -491 -51 O ATOM 2679 CG2 THR B 131 -4.184 -6.879 3.046 1.00 42.80 C ANISOU 2679 CG2 THR B 131 6243 4520 5498 476 -555 -142 C ATOM 2680 N SER B 132 -0.636 -8.920 1.131 1.00 42.91 N ANISOU 2680 N SER B 132 6191 4666 5446 668 -582 -7 N ATOM 2681 CA SER B 132 0.498 -9.842 1.071 1.00 43.29 C ANISOU 2681 CA SER B 132 6238 4781 5429 780 -574 55 C ATOM 2682 C SER B 132 1.545 -9.354 2.070 1.00 43.62 C ANISOU 2682 C SER B 132 6192 4986 5397 814 -634 50 C ATOM 2683 O SER B 132 2.237 -8.366 1.818 1.00 43.38 O ANISOU 2683 O SER B 132 6060 5040 5382 753 -689 12 O ATOM 2684 CB SER B 132 1.076 -9.894 -0.347 1.00 43.02 C ANISOU 2684 CB SER B 132 6169 4734 5442 778 -573 72 C ATOM 2685 OG SER B 132 2.226 -10.718 -0.405 1.00 43.78 O ANISOU 2685 OG SER B 132 6256 4906 5470 899 -562 137 O ATOM 2686 N GLY B 133 1.635 -10.039 3.210 1.00 43.87 N ANISOU 2686 N GLY B 133 6263 5067 5340 901 -619 87 N ATOM 2687 CA GLY B 133 2.464 -9.594 4.325 1.00 44.19 C ANISOU 2687 CA GLY B 133 6220 5280 5292 924 -676 78 C ATOM 2688 C GLY B 133 1.939 -8.282 4.885 1.00 43.56 C ANISOU 2688 C GLY B 133 6104 5202 5245 788 -717 -12 C ATOM 2689 O GLY B 133 0.752 -8.169 5.206 1.00 43.05 O ANISOU 2689 O GLY B 133 6115 5023 5220 742 -687 -40 O ATOM 2690 N GLY B 134 2.819 -7.286 4.977 1.00 43.30 N ANISOU 2690 N GLY B 134 5963 5300 5190 720 -777 -58 N ATOM 2691 CA GLY B 134 2.429 -5.931 5.369 1.00 42.78 C ANISOU 2691 CA GLY B 134 5879 5222 5154 579 -801 -150 C ATOM 2692 C GLY B 134 1.996 -5.037 4.215 1.00 41.43 C ANISOU 2692 C GLY B 134 5712 4934 5096 478 -790 -196 C ATOM 2693 O GLY B 134 1.726 -3.855 4.429 1.00 41.38 O ANISOU 2693 O GLY B 134 5705 4904 5115 368 -796 -269 O ATOM 2694 N THR B 135 1.924 -5.595 3.002 1.00 40.43 N ANISOU 2694 N THR B 135 5600 4731 5031 518 -767 -152 N ATOM 2695 CA THR B 135 1.570 -4.858 1.787 1.00 39.33 C ANISOU 2695 CA THR B 135 5458 4492 4992 440 -755 -181 C ATOM 2696 C THR B 135 0.104 -5.082 1.420 1.00 37.90 C ANISOU 2696 C THR B 135 5363 4155 4881 437 -705 -174 C ATOM 2697 O THR B 135 -0.413 -6.191 1.549 1.00 37.66 O ANISOU 2697 O THR B 135 5393 4081 4834 505 -672 -128 O ATOM 2698 CB THR B 135 2.452 -5.316 0.606 1.00 39.37 C ANISOU 2698 CB THR B 135 5415 4531 5014 480 -762 -138 C ATOM 2699 OG1 THR B 135 3.830 -5.112 0.937 1.00 40.55 O ANISOU 2699 OG1 THR B 135 5466 4854 5087 484 -809 -142 O ATOM 2700 CG2 THR B 135 2.129 -4.562 -0.667 1.00 38.77 C ANISOU 2700 CG2 THR B 135 5335 4361 5035 405 -750 -164 C ATOM 2701 N ALA B 136 -0.549 -4.017 0.960 1.00 36.77 N ANISOU 2701 N ALA B 136 5227 3937 4806 356 -693 -219 N ATOM 2702 CA ALA B 136 -1.915 -4.077 0.444 1.00 35.58 C ANISOU 2702 CA ALA B 136 5130 3670 4717 349 -649 -210 C ATOM 2703 C ALA B 136 -1.915 -3.570 -0.992 1.00 34.66 C ANISOU 2703 C ALA B 136 4986 3508 4675 315 -641 -208 C ATOM 2704 O ALA B 136 -1.281 -2.557 -1.292 1.00 34.49 O ANISOU 2704 O ALA B 136 4928 3505 4672 263 -658 -242 O ATOM 2705 CB ALA B 136 -2.841 -3.227 1.300 1.00 35.60 C ANISOU 2705 CB ALA B 136 5169 3635 4722 309 -630 -253 C ATOM 2706 N ALA B 137 -2.621 -4.280 -1.870 1.00 33.65 N ANISOU 2706 N ALA B 137 4881 3324 4581 335 -612 -171 N ATOM 2707 CA ALA B 137 -2.812 -3.854 -3.252 1.00 32.86 C ANISOU 2707 CA ALA B 137 4756 3184 4546 306 -601 -164 C ATOM 2708 C ALA B 137 -4.172 -3.176 -3.393 1.00 32.36 C ANISOU 2708 C ALA B 137 4711 3067 4518 281 -567 -174 C ATOM 2709 O ALA B 137 -5.165 -3.625 -2.817 1.00 32.24 O ANISOU 2709 O ALA B 137 4730 3038 4481 292 -542 -168 O ATOM 2710 CB ALA B 137 -2.711 -5.042 -4.197 1.00 32.54 C ANISOU 2710 CB ALA B 137 4725 3132 4508 336 -586 -120 C ATOM 2711 N LEU B 138 -4.196 -2.086 -4.148 1.00 32.03 N ANISOU 2711 N LEU B 138 4646 3000 4524 254 -560 -186 N ATOM 2712 CA LEU B 138 -5.435 -1.394 -4.507 1.00 32.11 C ANISOU 2712 CA LEU B 138 4664 2972 4564 254 -520 -179 C ATOM 2713 C LEU B 138 -5.287 -0.844 -5.920 1.00 31.64 C ANISOU 2713 C LEU B 138 4571 2896 4553 245 -512 -161 C ATOM 2714 O LEU B 138 -4.191 -0.855 -6.474 1.00 31.27 O ANISOU 2714 O LEU B 138 4502 2859 4521 229 -538 -164 O ATOM 2715 CB LEU B 138 -5.740 -0.278 -3.505 1.00 32.67 C ANISOU 2715 CB LEU B 138 4771 3017 4625 247 -499 -215 C ATOM 2716 CG LEU B 138 -4.684 0.826 -3.332 1.00 33.24 C ANISOU 2716 CG LEU B 138 4852 3074 4701 204 -506 -259 C ATOM 2717 CD1 LEU B 138 -5.030 2.072 -4.140 1.00 33.55 C ANISOU 2717 CD1 LEU B 138 4911 3051 4784 200 -458 -257 C ATOM 2718 CD2 LEU B 138 -4.530 1.194 -1.865 1.00 33.90 C ANISOU 2718 CD2 LEU B 138 4977 3167 4737 181 -507 -307 C ATOM 2719 N GLY B 139 -6.381 -0.372 -6.509 1.00 31.80 N ANISOU 2719 N GLY B 139 4584 2904 4593 263 -475 -136 N ATOM 2720 CA GLY B 139 -6.334 0.068 -7.898 1.00 31.70 C ANISOU 2720 CA GLY B 139 4539 2885 4620 265 -465 -110 C ATOM 2721 C GLY B 139 -7.592 0.695 -8.459 1.00 32.00 C ANISOU 2721 C GLY B 139 4561 2932 4665 303 -420 -74 C ATOM 2722 O GLY B 139 -8.516 1.041 -7.719 1.00 32.35 O ANISOU 2722 O GLY B 139 4623 2980 4688 333 -389 -72 O ATOM 2723 N CYS B 140 -7.613 0.836 -9.783 1.00 31.99 N ANISOU 2723 N CYS B 140 4521 2946 4687 309 -414 -41 N ATOM 2724 CA CYS B 140 -8.765 1.364 -10.507 1.00 32.41 C ANISOU 2724 CA CYS B 140 4541 3039 4736 357 -373 6 C ATOM 2725 C CYS B 140 -8.972 0.599 -11.798 1.00 31.66 C ANISOU 2725 C CYS B 140 4383 3011 4636 337 -388 39 C ATOM 2726 O CYS B 140 -8.023 0.400 -12.555 1.00 31.09 O ANISOU 2726 O CYS B 140 4305 2916 4590 308 -412 34 O ATOM 2727 CB CYS B 140 -8.562 2.844 -10.829 1.00 33.60 C ANISOU 2727 CB CYS B 140 4727 3126 4915 401 -329 18 C ATOM 2728 SG CYS B 140 -8.816 3.912 -9.404 1.00 35.48 S ANISOU 2728 SG CYS B 140 5051 3290 5140 432 -279 -12 S ATOM 2729 N LEU B 141 -10.214 0.179 -12.033 1.00 31.46 N ANISOU 2729 N LEU B 141 4307 3078 4568 345 -371 69 N ATOM 2730 CA LEU B 141 -10.619 -0.441 -13.286 1.00 31.15 C ANISOU 2730 CA LEU B 141 4202 3125 4507 315 -376 98 C ATOM 2731 C LEU B 141 -11.204 0.639 -14.195 1.00 31.27 C ANISOU 2731 C LEU B 141 4169 3191 4522 387 -343 154 C ATOM 2732 O LEU B 141 -12.251 1.210 -13.888 1.00 31.39 O ANISOU 2732 O LEU B 141 4157 3265 4504 451 -307 187 O ATOM 2733 CB LEU B 141 -11.660 -1.531 -13.026 1.00 31.32 C ANISOU 2733 CB LEU B 141 4193 3243 4466 264 -371 94 C ATOM 2734 CG LEU B 141 -12.174 -2.308 -14.240 1.00 31.47 C ANISOU 2734 CG LEU B 141 4147 3369 4442 202 -370 110 C ATOM 2735 CD1 LEU B 141 -11.050 -3.125 -14.860 1.00 31.07 C ANISOU 2735 CD1 LEU B 141 4136 3253 4416 142 -394 85 C ATOM 2736 CD2 LEU B 141 -13.336 -3.201 -13.834 1.00 31.85 C ANISOU 2736 CD2 LEU B 141 4167 3521 4415 137 -352 100 C ATOM 2737 N VAL B 142 -10.516 0.906 -15.303 1.00 30.81 N ANISOU 2737 N VAL B 142 4100 3112 4495 387 -351 169 N ATOM 2738 CA VAL B 142 -10.949 1.877 -16.300 1.00 31.25 C ANISOU 2738 CA VAL B 142 4115 3211 4546 461 -317 230 C ATOM 2739 C VAL B 142 -11.639 1.121 -17.442 1.00 31.33 C ANISOU 2739 C VAL B 142 4031 3369 4505 426 -329 260 C ATOM 2740 O VAL B 142 -10.970 0.575 -18.323 1.00 30.85 O ANISOU 2740 O VAL B 142 3961 3302 4459 368 -355 249 O ATOM 2741 CB VAL B 142 -9.747 2.688 -16.822 1.00 31.13 C ANISOU 2741 CB VAL B 142 4153 3084 4591 475 -312 226 C ATOM 2742 CG1 VAL B 142 -10.216 3.793 -17.757 1.00 31.74 C ANISOU 2742 CG1 VAL B 142 4210 3189 4661 569 -261 295 C ATOM 2743 CG2 VAL B 142 -8.960 3.274 -15.651 1.00 31.07 C ANISOU 2743 CG2 VAL B 142 4238 2948 4621 470 -304 177 C ATOM 2744 N LYS B 143 -12.973 1.110 -17.423 1.00 31.88 N ANISOU 2744 N LYS B 143 4026 3580 4507 457 -307 298 N ATOM 2745 CA LYS B 143 -13.762 0.199 -18.254 1.00 32.12 C ANISOU 2745 CA LYS B 143 3960 3779 4464 388 -319 311 C ATOM 2746 C LYS B 143 -14.606 0.884 -19.333 1.00 32.69 C ANISOU 2746 C LYS B 143 3929 4008 4482 467 -294 390 C ATOM 2747 O LYS B 143 -15.148 1.976 -19.120 1.00 33.06 O ANISOU 2747 O LYS B 143 3964 4077 4519 597 -252 448 O ATOM 2748 CB LYS B 143 -14.674 -0.641 -17.361 1.00 32.61 C ANISOU 2748 CB LYS B 143 4000 3924 4467 326 -318 282 C ATOM 2749 CG LYS B 143 -15.224 -1.871 -18.058 1.00 33.11 C ANISOU 2749 CG LYS B 143 3999 4128 4455 197 -329 262 C ATOM 2750 CD LYS B 143 -15.899 -2.822 -17.096 1.00 33.42 C ANISOU 2750 CD LYS B 143 4048 4210 4442 109 -321 219 C ATOM 2751 CE LYS B 143 -16.543 -3.970 -17.852 1.00 34.08 C ANISOU 2751 CE LYS B 143 4073 4443 4433 -38 -316 194 C ATOM 2752 NZ LYS B 143 -17.745 -3.573 -18.635 1.00 35.25 N ANISOU 2752 NZ LYS B 143 4070 4834 4489 -20 -305 249 N ATOM 2753 N ASP B 144 -14.713 0.203 -20.477 1.00 32.54 N ANISOU 2753 N ASP B 144 3842 4102 4420 390 -314 393 N ATOM 2754 CA ASP B 144 -15.618 0.553 -21.583 1.00 33.27 C ANISOU 2754 CA ASP B 144 3810 4398 4433 438 -299 464 C ATOM 2755 C ASP B 144 -15.370 1.935 -22.177 1.00 33.36 C ANISOU 2755 C ASP B 144 3830 4369 4476 594 -266 541 C ATOM 2756 O ASP B 144 -16.230 2.815 -22.118 1.00 34.18 O ANISOU 2756 O ASP B 144 3883 4569 4533 728 -222 616 O ATOM 2757 CB ASP B 144 -17.091 0.387 -21.166 1.00 34.19 C ANISOU 2757 CB ASP B 144 3821 4725 4447 446 -281 492 C ATOM 2758 CG ASP B 144 -17.457 -1.054 -20.843 1.00 34.28 C ANISOU 2758 CG ASP B 144 3816 4807 4403 267 -303 418 C ATOM 2759 OD1 ASP B 144 -16.800 -1.990 -21.344 1.00 34.06 O ANISOU 2759 OD1 ASP B 144 3831 4724 4388 138 -326 361 O ATOM 2760 OD2 ASP B 144 -18.417 -1.256 -20.078 1.00 34.95 O ANISOU 2760 OD2 ASP B 144 3855 4998 4428 256 -288 416 O ATOM 2761 N TYR B 145 -14.185 2.108 -22.753 1.00 32.62 N ANISOU 2761 N TYR B 145 3805 4132 4455 578 -278 524 N ATOM 2762 CA TYR B 145 -13.838 3.336 -23.456 1.00 32.88 C ANISOU 2762 CA TYR B 145 3862 4114 4517 704 -240 590 C ATOM 2763 C TYR B 145 -13.379 3.048 -24.873 1.00 32.84 C ANISOU 2763 C TYR B 145 3815 4158 4505 657 -263 602 C ATOM 2764 O TYR B 145 -13.004 1.920 -25.210 1.00 32.02 O ANISOU 2764 O TYR B 145 3700 4069 4399 519 -308 543 O ATOM 2765 CB TYR B 145 -12.759 4.121 -22.701 1.00 32.42 C ANISOU 2765 CB TYR B 145 3946 3815 4557 741 -218 560 C ATOM 2766 CG TYR B 145 -11.398 3.453 -22.637 1.00 31.42 C ANISOU 2766 CG TYR B 145 3889 3545 4505 619 -265 478 C ATOM 2767 CD1 TYR B 145 -11.082 2.565 -21.606 1.00 30.83 C ANISOU 2767 CD1 TYR B 145 3852 3412 4449 527 -301 404 C ATOM 2768 CD2 TYR B 145 -10.418 3.721 -23.596 1.00 31.12 C ANISOU 2768 CD2 TYR B 145 3878 3436 4510 608 -269 482 C ATOM 2769 CE1 TYR B 145 -9.836 1.958 -21.539 1.00 30.09 C ANISOU 2769 CE1 TYR B 145 3815 3206 4411 439 -338 342 C ATOM 2770 CE2 TYR B 145 -9.170 3.118 -23.537 1.00 30.36 C ANISOU 2770 CE2 TYR B 145 3834 3229 4473 510 -309 415 C ATOM 2771 CZ TYR B 145 -8.884 2.236 -22.507 1.00 29.90 C ANISOU 2771 CZ TYR B 145 3807 3126 4427 433 -343 348 C ATOM 2772 OH TYR B 145 -7.651 1.635 -22.443 1.00 29.24 O ANISOU 2772 OH TYR B 145 3768 2950 4389 358 -377 294 O ATOM 2773 N PHE B 146 -13.421 4.093 -25.692 1.00 33.65 N ANISOU 2773 N PHE B 146 3907 4278 4600 780 -222 682 N ATOM 2774 CA PHE B 146 -12.902 4.067 -27.051 1.00 33.92 C ANISOU 2774 CA PHE B 146 3916 4339 4635 760 -234 703 C ATOM 2775 C PHE B 146 -12.647 5.517 -27.485 1.00 34.86 C ANISOU 2775 C PHE B 146 4092 4375 4780 919 -168 783 C ATOM 2776 O PHE B 146 -13.469 6.385 -27.181 1.00 35.82 O ANISOU 2776 O PHE B 146 4206 4546 4859 1064 -109 856 O ATOM 2777 CB PHE B 146 -13.912 3.407 -27.993 1.00 34.48 C ANISOU 2777 CB PHE B 146 3835 4675 4590 722 -256 738 C ATOM 2778 CG PHE B 146 -13.401 3.215 -29.392 1.00 34.39 C ANISOU 2778 CG PHE B 146 3793 4704 4570 680 -274 749 C ATOM 2779 CD1 PHE B 146 -12.694 2.066 -29.735 1.00 33.68 C ANISOU 2779 CD1 PHE B 146 3724 4572 4502 515 -320 667 C ATOM 2780 CD2 PHE B 146 -13.618 4.182 -30.369 1.00 35.16 C ANISOU 2780 CD2 PHE B 146 3851 4877 4633 814 -236 847 C ATOM 2781 CE1 PHE B 146 -12.214 1.886 -31.026 1.00 33.66 C ANISOU 2781 CE1 PHE B 146 3699 4602 4490 476 -333 676 C ATOM 2782 CE2 PHE B 146 -13.140 4.007 -31.661 1.00 35.10 C ANISOU 2782 CE2 PHE B 146 3815 4906 4614 775 -252 858 C ATOM 2783 CZ PHE B 146 -12.441 2.857 -31.991 1.00 34.37 C ANISOU 2783 CZ PHE B 146 3740 4774 4547 601 -302 770 C ATOM 2784 N PRO B 147 -11.545 5.816 -28.173 1.00 35.13 N ANISOU 2784 N PRO B 147 4192 4280 4876 900 -165 772 N ATOM 2785 CA PRO B 147 -10.467 4.898 -28.553 1.00 34.67 C ANISOU 2785 CA PRO B 147 4154 4150 4870 751 -224 694 C ATOM 2786 C PRO B 147 -9.358 4.865 -27.500 1.00 34.39 C ANISOU 2786 C PRO B 147 4235 3905 4928 688 -235 612 C ATOM 2787 O PRO B 147 -9.489 5.487 -26.446 1.00 34.63 O ANISOU 2787 O PRO B 147 4329 3850 4980 741 -201 608 O ATOM 2788 CB PRO B 147 -9.938 5.542 -29.839 1.00 34.84 C ANISOU 2788 CB PRO B 147 4183 4154 4901 801 -198 747 C ATOM 2789 CG PRO B 147 -10.137 7.002 -29.594 1.00 35.49 C ANISOU 2789 CG PRO B 147 4338 4156 4992 960 -114 818 C ATOM 2790 CD PRO B 147 -11.459 7.091 -28.903 1.00 36.12 C ANISOU 2790 CD PRO B 147 4358 4365 5000 1043 -94 860 C ATOM 2791 N GLU B 148 -8.275 4.150 -27.796 1.00 34.33 N ANISOU 2791 N GLU B 148 4251 3825 4967 579 -278 552 N ATOM 2792 CA GLU B 148 -7.029 4.284 -27.036 1.00 34.49 C ANISOU 2792 CA GLU B 148 4369 3666 5069 531 -285 487 C ATOM 2793 C GLU B 148 -6.428 5.685 -27.302 1.00 35.02 C ANISOU 2793 C GLU B 148 4514 3615 5178 603 -225 519 C ATOM 2794 O GLU B 148 -6.688 6.252 -28.365 1.00 35.51 O ANISOU 2794 O GLU B 148 4554 3722 5216 671 -191 586 O ATOM 2795 CB GLU B 148 -6.025 3.202 -27.449 1.00 34.30 C ANISOU 2795 CB GLU B 148 4342 3620 5072 419 -337 431 C ATOM 2796 CG GLU B 148 -6.370 1.797 -26.972 1.00 34.40 C ANISOU 2796 CG GLU B 148 4325 3694 5051 335 -379 383 C ATOM 2797 CD GLU B 148 -5.611 1.395 -25.718 1.00 34.47 C ANISOU 2797 CD GLU B 148 4398 3595 5102 293 -400 319 C ATOM 2798 OE1 GLU B 148 -4.793 0.452 -25.803 1.00 34.30 O ANISOU 2798 OE1 GLU B 148 4394 3543 5094 225 -427 278 O ATOM 2799 OE2 GLU B 148 -5.816 2.025 -24.652 1.00 35.10 O ANISOU 2799 OE2 GLU B 148 4515 3626 5196 333 -384 313 O ATOM 2800 N PRO B 149 -5.631 6.250 -26.386 1.00 35.10 N ANISOU 2800 N PRO B 149 4619 3477 5241 583 -206 473 N ATOM 2801 CA PRO B 149 -5.213 5.633 -25.128 1.00 34.55 C ANISOU 2801 CA PRO B 149 4575 3359 5195 508 -246 396 C ATOM 2802 C PRO B 149 -5.822 6.323 -23.905 1.00 35.03 C ANISOU 2802 C PRO B 149 4692 3372 5246 562 -204 394 C ATOM 2803 O PRO B 149 -6.445 7.379 -24.025 1.00 35.68 O ANISOU 2803 O PRO B 149 4811 3435 5309 663 -133 451 O ATOM 2804 CB PRO B 149 -3.705 5.866 -25.146 1.00 34.35 C ANISOU 2804 CB PRO B 149 4605 3223 5225 436 -253 345 C ATOM 2805 CG PRO B 149 -3.554 7.192 -25.834 1.00 35.11 C ANISOU 2805 CG PRO B 149 4760 3249 5332 494 -179 390 C ATOM 2806 CD PRO B 149 -4.773 7.409 -26.703 1.00 35.57 C ANISOU 2806 CD PRO B 149 4767 3407 5341 601 -148 479 C ATOM 2807 N VAL B 150 -5.630 5.705 -22.745 1.00 34.70 N ANISOU 2807 N VAL B 150 4663 3310 5213 503 -242 332 N ATOM 2808 CA VAL B 150 -5.947 6.297 -21.446 1.00 35.13 C ANISOU 2808 CA VAL B 150 4783 3300 5264 530 -208 311 C ATOM 2809 C VAL B 150 -4.631 6.433 -20.672 1.00 34.73 C ANISOU 2809 C VAL B 150 4800 3143 5255 442 -224 234 C ATOM 2810 O VAL B 150 -3.756 5.574 -20.779 1.00 34.09 O ANISOU 2810 O VAL B 150 4683 3079 5190 365 -284 194 O ATOM 2811 CB VAL B 150 -6.962 5.411 -20.676 1.00 35.21 C ANISOU 2811 CB VAL B 150 4740 3404 5234 534 -240 307 C ATOM 2812 CG1 VAL B 150 -6.994 5.733 -19.186 1.00 35.51 C ANISOU 2812 CG1 VAL B 150 4846 3371 5276 532 -225 263 C ATOM 2813 CG2 VAL B 150 -8.353 5.561 -21.273 1.00 35.73 C ANISOU 2813 CG2 VAL B 150 4738 3594 5244 627 -210 385 C ATOM 2814 N THR B 151 -4.492 7.522 -19.915 1.00 35.14 N ANISOU 2814 N THR B 151 4948 3093 5313 454 -163 214 N ATOM 2815 CA THR B 151 -3.397 7.680 -18.957 1.00 35.04 C ANISOU 2815 CA THR B 151 4991 3006 5318 359 -176 133 C ATOM 2816 C THR B 151 -3.952 7.534 -17.548 1.00 35.10 C ANISOU 2816 C THR B 151 5023 3012 5302 365 -179 102 C ATOM 2817 O THR B 151 -5.091 7.926 -17.280 1.00 35.42 O ANISOU 2817 O THR B 151 5084 3054 5318 452 -132 142 O ATOM 2818 CB THR B 151 -2.706 9.052 -19.080 1.00 35.94 C ANISOU 2818 CB THR B 151 5213 2997 5444 333 -95 114 C ATOM 2819 OG1 THR B 151 -3.622 10.098 -18.724 1.00 36.67 O ANISOU 2819 OG1 THR B 151 5399 3018 5516 421 1 148 O ATOM 2820 CG2 THR B 151 -2.199 9.273 -20.498 1.00 35.97 C ANISOU 2820 CG2 THR B 151 5199 2997 5469 333 -83 150 C ATOM 2821 N VAL B 152 -3.147 6.959 -16.658 1.00 34.70 N ANISOU 2821 N VAL B 152 4964 2969 5251 281 -234 35 N ATOM 2822 CA VAL B 152 -3.491 6.853 -15.244 1.00 34.79 C ANISOU 2822 CA VAL B 152 5006 2974 5238 273 -239 -3 C ATOM 2823 C VAL B 152 -2.296 7.315 -14.415 1.00 35.24 C ANISOU 2823 C VAL B 152 5116 2982 5291 173 -240 -82 C ATOM 2824 O VAL B 152 -1.157 6.966 -14.721 1.00 35.46 O ANISOU 2824 O VAL B 152 5104 3041 5327 102 -285 -110 O ATOM 2825 CB VAL B 152 -3.875 5.407 -14.844 1.00 34.13 C ANISOU 2825 CB VAL B 152 4844 2985 5137 276 -312 -1 C ATOM 2826 CG1 VAL B 152 -4.315 5.350 -13.383 1.00 34.24 C ANISOU 2826 CG1 VAL B 152 4895 2993 5124 277 -310 -35 C ATOM 2827 CG2 VAL B 152 -4.967 4.863 -15.761 1.00 33.86 C ANISOU 2827 CG2 VAL B 152 4747 3024 5094 341 -313 65 C ATOM 2828 N SER B 153 -2.564 8.121 -13.391 1.00 35.82 N ANISOU 2828 N SER B 153 5277 2989 5343 166 -186 -115 N ATOM 2829 CA SER B 153 -1.573 8.474 -12.374 1.00 36.29 C ANISOU 2829 CA SER B 153 5382 3028 5379 56 -191 -200 C ATOM 2830 C SER B 153 -2.211 8.295 -11.002 1.00 36.40 C ANISOU 2830 C SER B 153 5422 3048 5359 72 -194 -225 C ATOM 2831 O SER B 153 -3.420 8.061 -10.904 1.00 36.26 O ANISOU 2831 O SER B 153 5400 3037 5342 168 -179 -176 O ATOM 2832 CB SER B 153 -1.081 9.912 -12.561 1.00 37.43 C ANISOU 2832 CB SER B 153 5643 3059 5521 -4 -96 -233 C ATOM 2833 OG SER B 153 -2.105 10.856 -12.289 1.00 38.07 O ANISOU 2833 OG SER B 153 5835 3036 5592 72 5 -209 O ATOM 2834 N TRP B 154 -1.396 8.409 -9.955 1.00 36.73 N ANISOU 2834 N TRP B 154 5486 3103 5367 -26 -212 -301 N ATOM 2835 CA TRP B 154 -1.851 8.223 -8.577 1.00 36.93 C ANISOU 2835 CA TRP B 154 5537 3141 5355 -24 -220 -332 C ATOM 2836 C TRP B 154 -1.439 9.406 -7.702 1.00 38.34 C ANISOU 2836 C TRP B 154 5831 3243 5495 -117 -150 -410 C ATOM 2837 O TRP B 154 -0.279 9.824 -7.730 1.00 38.81 O ANISOU 2837 O TRP B 154 5898 3313 5534 -237 -151 -469 O ATOM 2838 CB TRP B 154 -1.296 6.910 -8.020 1.00 36.21 C ANISOU 2838 CB TRP B 154 5345 3173 5241 -45 -322 -346 C ATOM 2839 CG TRP B 154 -1.999 5.727 -8.584 1.00 35.00 C ANISOU 2839 CG TRP B 154 5115 3072 5110 46 -367 -277 C ATOM 2840 CD1 TRP B 154 -1.684 5.046 -9.725 1.00 34.47 C ANISOU 2840 CD1 TRP B 154 4978 3047 5073 64 -403 -237 C ATOM 2841 CD2 TRP B 154 -3.164 5.103 -8.049 1.00 34.47 C ANISOU 2841 CD2 TRP B 154 5042 3021 5033 118 -371 -246 C ATOM 2842 NE1 TRP B 154 -2.581 4.023 -9.928 1.00 33.71 N ANISOU 2842 NE1 TRP B 154 4840 2989 4980 134 -426 -187 N ATOM 2843 CE2 TRP B 154 -3.500 4.036 -8.912 1.00 33.80 C ANISOU 2843 CE2 TRP B 154 4886 2989 4966 165 -408 -192 C ATOM 2844 CE3 TRP B 154 -3.956 5.336 -6.918 1.00 34.73 C ANISOU 2844 CE3 TRP B 154 5127 3032 5038 141 -342 -262 C ATOM 2845 CZ2 TRP B 154 -4.596 3.204 -8.678 1.00 33.36 C ANISOU 2845 CZ2 TRP B 154 4809 2969 4898 219 -415 -158 C ATOM 2846 CZ3 TRP B 154 -5.047 4.509 -6.684 1.00 34.28 C ANISOU 2846 CZ3 TRP B 154 5040 3012 4972 208 -354 -222 C ATOM 2847 CH2 TRP B 154 -5.355 3.453 -7.560 1.00 33.67 C ANISOU 2847 CH2 TRP B 154 4890 2992 4909 240 -389 -173 C ATOM 2848 N ASN B 155 -2.402 9.924 -6.932 1.00 39.15 N ANISOU 2848 N ASN B 155 6021 3274 5579 -68 -85 -411 N ATOM 2849 CA ASN B 155 -2.237 11.122 -6.092 1.00 40.65 C ANISOU 2849 CA ASN B 155 6353 3364 5727 -147 7 -482 C ATOM 2850 C ASN B 155 -1.588 12.296 -6.847 1.00 41.70 C ANISOU 2850 C ASN B 155 6586 3392 5866 -223 96 -509 C ATOM 2851 O ASN B 155 -0.668 12.950 -6.343 1.00 42.84 O ANISOU 2851 O ASN B 155 6798 3515 5967 -373 128 -599 O ATOM 2852 CB ASN B 155 -1.474 10.772 -4.803 1.00 40.96 C ANISOU 2852 CB ASN B 155 6367 3489 5708 -263 -53 -567 C ATOM 2853 CG ASN B 155 -2.226 9.782 -3.921 1.00 40.44 C ANISOU 2853 CG ASN B 155 6241 3496 5629 -184 -114 -542 C ATOM 2854 OD1 ASN B 155 -3.405 9.491 -4.145 1.00 39.93 O ANISOU 2854 OD1 ASN B 155 6170 3408 5593 -57 -99 -472 O ATOM 2855 ND2 ASN B 155 -1.545 9.264 -2.905 1.00 40.56 N ANISOU 2855 ND2 ASN B 155 6209 3611 5591 -262 -181 -598 N ATOM 2856 N SER B 156 -2.090 12.537 -8.060 1.00 41.57 N ANISOU 2856 N SER B 156 6578 3322 5896 -122 139 -430 N ATOM 2857 CA SER B 156 -1.625 13.613 -8.952 1.00 42.43 C ANISOU 2857 CA SER B 156 6788 3320 6015 -163 235 -434 C ATOM 2858 C SER B 156 -0.126 13.561 -9.288 1.00 42.65 C ANISOU 2858 C SER B 156 6766 3403 6034 -328 187 -501 C ATOM 2859 O SER B 156 0.501 14.602 -9.495 1.00 43.71 O ANISOU 2859 O SER B 156 7016 3443 6150 -434 278 -552 O ATOM 2860 CB SER B 156 -1.995 14.981 -8.365 1.00 43.73 C ANISOU 2860 CB SER B 156 7159 3315 6142 -177 390 -470 C ATOM 2861 OG SER B 156 -3.351 14.999 -7.962 1.00 43.81 O ANISOU 2861 OG SER B 156 7203 3292 6150 -19 433 -407 O ATOM 2862 N GLY B 157 0.432 12.352 -9.353 1.00 41.71 N ANISOU 2862 N GLY B 157 6482 3441 5925 -345 54 -497 N ATOM 2863 CA GLY B 157 1.860 12.153 -9.622 1.00 41.88 C ANISOU 2863 CA GLY B 157 6427 3555 5930 -484 -4 -551 C ATOM 2864 C GLY B 157 2.760 11.963 -8.407 1.00 42.30 C ANISOU 2864 C GLY B 157 6443 3717 5914 -623 -56 -644 C ATOM 2865 O GLY B 157 3.916 11.571 -8.566 1.00 42.59 O ANISOU 2865 O GLY B 157 6377 3879 5926 -716 -123 -676 O ATOM 2866 N ALA B 158 2.248 12.237 -7.204 1.00 42.51 N ANISOU 2866 N ALA B 158 6544 3710 5899 -634 -25 -684 N ATOM 2867 CA ALA B 158 3.018 12.065 -5.960 1.00 42.97 C ANISOU 2867 CA ALA B 158 6565 3885 5878 -763 -74 -771 C ATOM 2868 C ALA B 158 3.303 10.594 -5.601 1.00 41.98 C ANISOU 2868 C ALA B 158 6266 3943 5741 -705 -213 -739 C ATOM 2869 O ALA B 158 4.264 10.307 -4.882 1.00 42.25 O ANISOU 2869 O ALA B 158 6224 4125 5705 -807 -273 -796 O ATOM 2870 CB ALA B 158 2.307 12.753 -4.803 1.00 43.70 C ANISOU 2870 CB ALA B 158 6794 3881 5928 -781 3 -819 C ATOM 2871 N LEU B 159 2.466 9.678 -6.087 1.00 40.68 N ANISOU 2871 N LEU B 159 6045 3777 5637 -544 -255 -647 N ATOM 2872 CA LEU B 159 2.649 8.246 -5.871 1.00 39.82 C ANISOU 2872 CA LEU B 159 5799 3811 5520 -474 -365 -607 C ATOM 2873 C LEU B 159 2.985 7.576 -7.201 1.00 39.06 C ANISOU 2873 C LEU B 159 5615 3752 5476 -417 -406 -543 C ATOM 2874 O LEU B 159 2.135 7.500 -8.085 1.00 38.55 O ANISOU 2874 O LEU B 159 5570 3603 5472 -322 -380 -479 O ATOM 2875 CB LEU B 159 1.372 7.650 -5.269 1.00 39.25 C ANISOU 2875 CB LEU B 159 5745 3705 5461 -353 -371 -562 C ATOM 2876 CG LEU B 159 1.325 6.145 -4.982 1.00 38.43 C ANISOU 2876 CG LEU B 159 5538 3716 5349 -269 -461 -515 C ATOM 2877 CD1 LEU B 159 2.518 5.687 -4.151 1.00 38.94 C ANISOU 2877 CD1 LEU B 159 5525 3935 5337 -338 -527 -558 C ATOM 2878 CD2 LEU B 159 0.020 5.806 -4.276 1.00 38.04 C ANISOU 2878 CD2 LEU B 159 5531 3619 5303 -180 -445 -487 C ATOM 2879 N THR B 160 4.234 7.125 -7.349 1.00 39.25 N ANISOU 2879 N THR B 160 5537 3910 5466 -476 -468 -559 N ATOM 2880 CA THR B 160 4.688 6.415 -8.561 1.00 38.57 C ANISOU 2880 CA THR B 160 5364 3870 5420 -424 -508 -502 C ATOM 2881 C THR B 160 5.310 5.026 -8.317 1.00 38.14 C ANISOU 2881 C THR B 160 5190 3972 5331 -364 -596 -468 C ATOM 2882 O THR B 160 5.148 4.134 -9.152 1.00 37.42 O ANISOU 2882 O THR B 160 5056 3882 5279 -271 -620 -401 O ATOM 2883 CB THR B 160 5.693 7.266 -9.368 1.00 39.26 C ANISOU 2883 CB THR B 160 5448 3961 5507 -537 -478 -538 C ATOM 2884 OG1 THR B 160 6.831 7.573 -8.555 1.00 40.64 O ANISOU 2884 OG1 THR B 160 5580 4264 5597 -672 -499 -615 O ATOM 2885 CG2 THR B 160 5.044 8.558 -9.845 1.00 39.56 C ANISOU 2885 CG2 THR B 160 5623 3823 5586 -568 -374 -552 C ATOM 2886 N SER B 161 6.026 4.838 -7.208 1.00 38.69 N ANISOU 2886 N SER B 161 5210 4172 5318 -414 -636 -509 N ATOM 2887 CA SER B 161 6.674 3.551 -6.932 1.00 38.68 C ANISOU 2887 CA SER B 161 5101 4326 5269 -338 -708 -467 C ATOM 2888 C SER B 161 5.631 2.464 -6.669 1.00 37.61 C ANISOU 2888 C SER B 161 4994 4139 5159 -200 -719 -405 C ATOM 2889 O SER B 161 4.645 2.694 -5.963 1.00 37.37 O ANISOU 2889 O SER B 161 5036 4027 5134 -190 -693 -418 O ATOM 2890 CB SER B 161 7.648 3.656 -5.754 1.00 39.86 C ANISOU 2890 CB SER B 161 5184 4650 5310 -417 -746 -522 C ATOM 2891 OG SER B 161 6.960 3.842 -4.531 1.00 40.40 O ANISOU 2891 OG SER B 161 5316 4689 5346 -426 -736 -555 O ATOM 2892 N GLY B 162 5.848 1.294 -7.264 1.00 36.99 N ANISOU 2892 N GLY B 162 4864 4102 5089 -100 -747 -338 N ATOM 2893 CA GLY B 162 4.912 0.174 -7.156 1.00 36.26 C ANISOU 2893 CA GLY B 162 4808 3956 5014 15 -745 -280 C ATOM 2894 C GLY B 162 3.679 0.253 -8.047 1.00 35.35 C ANISOU 2894 C GLY B 162 4757 3693 4979 43 -703 -253 C ATOM 2895 O GLY B 162 2.843 -0.645 -8.000 1.00 34.78 O ANISOU 2895 O GLY B 162 4717 3581 4916 115 -696 -213 O ATOM 2896 N VAL B 163 3.564 1.306 -8.862 1.00 35.19 N ANISOU 2896 N VAL B 163 4758 3602 5009 -17 -672 -273 N ATOM 2897 CA VAL B 163 2.427 1.477 -9.762 1.00 34.50 C ANISOU 2897 CA VAL B 163 4718 3402 4987 16 -632 -241 C ATOM 2898 C VAL B 163 2.618 0.588 -10.989 1.00 33.87 C ANISOU 2898 C VAL B 163 4600 3334 4935 65 -643 -188 C ATOM 2899 O VAL B 163 3.689 0.591 -11.599 1.00 34.29 O ANISOU 2899 O VAL B 163 4603 3439 4987 43 -660 -187 O ATOM 2900 CB VAL B 163 2.260 2.951 -10.211 1.00 34.85 C ANISOU 2900 CB VAL B 163 4809 3365 5066 -48 -581 -271 C ATOM 2901 CG1 VAL B 163 1.164 3.089 -11.268 1.00 34.39 C ANISOU 2901 CG1 VAL B 163 4780 3221 5064 5 -542 -223 C ATOM 2902 CG2 VAL B 163 1.951 3.841 -9.011 1.00 35.39 C ANISOU 2902 CG2 VAL B 163 4941 3400 5105 -96 -552 -325 C ATOM 2903 N HIS B 164 1.577 -0.168 -11.333 1.00 33.13 N ANISOU 2903 N HIS B 164 4531 3198 4860 122 -629 -148 N ATOM 2904 CA HIS B 164 1.533 -0.947 -12.567 1.00 32.52 C ANISOU 2904 CA HIS B 164 4437 3115 4806 154 -625 -104 C ATOM 2905 C HIS B 164 0.233 -0.646 -13.314 1.00 31.81 C ANISOU 2905 C HIS B 164 4371 2962 4752 161 -590 -82 C ATOM 2906 O HIS B 164 -0.856 -0.988 -12.846 1.00 31.52 O ANISOU 2906 O HIS B 164 4363 2912 4703 182 -576 -74 O ATOM 2907 CB HIS B 164 1.637 -2.444 -12.265 1.00 32.69 C ANISOU 2907 CB HIS B 164 4464 3169 4787 210 -636 -75 C ATOM 2908 CG HIS B 164 2.942 -2.848 -11.652 1.00 33.44 C ANISOU 2908 CG HIS B 164 4522 3349 4834 233 -667 -78 C ATOM 2909 ND1 HIS B 164 4.129 -2.840 -12.353 1.00 33.81 N ANISOU 2909 ND1 HIS B 164 4513 3453 4880 232 -683 -69 N ATOM 2910 CD2 HIS B 164 3.246 -3.279 -10.405 1.00 33.93 C ANISOU 2910 CD2 HIS B 164 4585 3468 4838 264 -685 -84 C ATOM 2911 CE1 HIS B 164 5.107 -3.245 -11.562 1.00 34.43 C ANISOU 2911 CE1 HIS B 164 4552 3631 4897 265 -709 -66 C ATOM 2912 NE2 HIS B 164 4.598 -3.520 -10.376 1.00 34.57 N ANISOU 2912 NE2 HIS B 164 4606 3652 4879 287 -711 -74 N ATOM 2913 N THR B 165 0.358 0.019 -14.460 1.00 31.39 N ANISOU 2913 N THR B 165 4302 2886 4737 144 -575 -70 N ATOM 2914 CA THR B 165 -0.770 0.301 -15.346 1.00 30.92 C ANISOU 2914 CA THR B 165 4250 2797 4702 162 -543 -38 C ATOM 2915 C THR B 165 -0.645 -0.615 -16.553 1.00 30.15 C ANISOU 2915 C THR B 165 4123 2723 4608 168 -549 -5 C ATOM 2916 O THR B 165 0.326 -0.532 -17.305 1.00 30.25 O ANISOU 2916 O THR B 165 4113 2743 4640 155 -558 -3 O ATOM 2917 CB THR B 165 -0.781 1.777 -15.769 1.00 31.34 C ANISOU 2917 CB THR B 165 4321 2803 4786 149 -508 -41 C ATOM 2918 OG1 THR B 165 -0.938 2.587 -14.597 1.00 31.87 O ANISOU 2918 OG1 THR B 165 4434 2836 4841 136 -489 -76 O ATOM 2919 CG2 THR B 165 -1.929 2.069 -16.736 1.00 31.27 C ANISOU 2919 CG2 THR B 165 4306 2785 4789 189 -473 7 C ATOM 2920 N PHE B 166 -1.628 -1.494 -16.720 1.00 29.37 N ANISOU 2920 N PHE B 166 4030 2640 4488 180 -539 15 N ATOM 2921 CA PHE B 166 -1.539 -2.592 -17.679 1.00 28.87 C ANISOU 2921 CA PHE B 166 3960 2596 4412 172 -537 35 C ATOM 2922 C PHE B 166 -1.999 -2.169 -19.074 1.00 28.34 C ANISOU 2922 C PHE B 166 3861 2543 4363 162 -521 62 C ATOM 2923 O PHE B 166 -2.783 -1.230 -19.200 1.00 28.35 O ANISOU 2923 O PHE B 166 3848 2549 4373 176 -504 76 O ATOM 2924 CB PHE B 166 -2.366 -3.780 -17.184 1.00 28.77 C ANISOU 2924 CB PHE B 166 3983 2595 4353 166 -522 34 C ATOM 2925 CG PHE B 166 -1.833 -4.387 -15.924 1.00 28.90 C ANISOU 2925 CG PHE B 166 4038 2599 4344 188 -533 17 C ATOM 2926 CD1 PHE B 166 -2.185 -3.872 -14.675 1.00 29.04 C ANISOU 2926 CD1 PHE B 166 4066 2614 4354 198 -541 -2 C ATOM 2927 CD2 PHE B 166 -0.949 -5.455 -15.980 1.00 28.98 C ANISOU 2927 CD2 PHE B 166 4077 2605 4330 209 -530 24 C ATOM 2928 CE1 PHE B 166 -1.675 -4.422 -13.509 1.00 29.10 C ANISOU 2928 CE1 PHE B 166 4104 2624 4330 223 -552 -15 C ATOM 2929 CE2 PHE B 166 -0.441 -6.007 -14.818 1.00 29.15 C ANISOU 2929 CE2 PHE B 166 4130 2628 4316 249 -535 20 C ATOM 2930 CZ PHE B 166 -0.801 -5.494 -13.583 1.00 29.28 C ANISOU 2930 CZ PHE B 166 4148 2651 4324 252 -550 0 C ATOM 2931 N PRO B 167 -1.514 -2.862 -20.126 1.00 27.88 N ANISOU 2931 N PRO B 167 3795 2495 4303 148 -519 75 N ATOM 2932 CA PRO B 167 -2.061 -2.616 -21.468 1.00 27.66 C ANISOU 2932 CA PRO B 167 3734 2497 4278 134 -504 102 C ATOM 2933 C PRO B 167 -3.549 -2.959 -21.535 1.00 27.44 C ANISOU 2933 C PRO B 167 3694 2526 4206 115 -486 113 C ATOM 2934 O PRO B 167 -3.999 -3.911 -20.881 1.00 27.30 O ANISOU 2934 O PRO B 167 3708 2514 4149 91 -478 95 O ATOM 2935 CB PRO B 167 -1.253 -3.551 -22.386 1.00 27.59 C ANISOU 2935 CB PRO B 167 3733 2485 4263 115 -502 105 C ATOM 2936 CG PRO B 167 -0.129 -4.076 -21.573 1.00 27.67 C ANISOU 2936 CG PRO B 167 3773 2466 4273 137 -516 88 C ATOM 2937 CD PRO B 167 -0.461 -3.895 -20.127 1.00 27.87 C ANISOU 2937 CD PRO B 167 3817 2483 4288 153 -526 69 C ATOM 2938 N ALA B 168 -4.293 -2.180 -22.313 1.00 27.05 N ANISOU 2938 N ALA B 168 3597 2525 4155 129 -474 145 N ATOM 2939 CA ALA B 168 -5.735 -2.371 -22.447 1.00 27.07 C ANISOU 2939 CA ALA B 168 3563 2620 4103 115 -457 162 C ATOM 2940 C ALA B 168 -6.051 -3.651 -23.211 1.00 26.79 C ANISOU 2940 C ALA B 168 3525 2641 4014 36 -448 151 C ATOM 2941 O ALA B 168 -5.278 -4.080 -24.068 1.00 26.56 O ANISOU 2941 O ALA B 168 3510 2587 3995 12 -449 147 O ATOM 2942 CB ALA B 168 -6.363 -1.177 -23.152 1.00 27.32 C ANISOU 2942 CB ALA B 168 3538 2706 4135 170 -442 211 C ATOM 2943 N VAL B 169 -7.194 -4.246 -22.891 1.00 26.73 N ANISOU 2943 N VAL B 169 3504 2708 3943 -10 -433 142 N ATOM 2944 CA VAL B 169 -7.715 -5.384 -23.640 1.00 26.95 C ANISOU 2944 CA VAL B 169 3532 2807 3901 -109 -411 124 C ATOM 2945 C VAL B 169 -8.947 -4.914 -24.402 1.00 27.34 C ANISOU 2945 C VAL B 169 3479 3017 3892 -123 -407 157 C ATOM 2946 O VAL B 169 -9.716 -4.094 -23.896 1.00 27.40 O ANISOU 2946 O VAL B 169 3434 3085 3894 -63 -409 187 O ATOM 2947 CB VAL B 169 -8.040 -6.603 -22.742 1.00 27.14 C ANISOU 2947 CB VAL B 169 3629 2804 3878 -179 -386 81 C ATOM 2948 CG1 VAL B 169 -6.760 -7.163 -22.133 1.00 26.79 C ANISOU 2948 CG1 VAL B 169 3683 2619 3877 -149 -384 60 C ATOM 2949 CG2 VAL B 169 -9.059 -6.277 -21.649 1.00 27.36 C ANISOU 2949 CG2 VAL B 169 3629 2883 3883 -163 -386 82 C ATOM 2950 N LEU B 170 -9.114 -5.417 -25.622 1.00 27.62 N ANISOU 2950 N LEU B 170 3485 3131 3878 -196 -396 156 N ATOM 2951 CA LEU B 170 -10.279 -5.097 -26.443 1.00 28.21 C ANISOU 2951 CA LEU B 170 3448 3395 3875 -219 -393 189 C ATOM 2952 C LEU B 170 -11.370 -6.113 -26.147 1.00 28.67 C ANISOU 2952 C LEU B 170 3494 3565 3833 -343 -368 150 C ATOM 2953 O LEU B 170 -11.181 -7.304 -26.365 1.00 28.70 O ANISOU 2953 O LEU B 170 3571 3535 3798 -463 -341 97 O ATOM 2954 CB LEU B 170 -9.916 -5.112 -27.931 1.00 28.35 C ANISOU 2954 CB LEU B 170 3435 3459 3879 -246 -394 205 C ATOM 2955 CG LEU B 170 -11.007 -4.706 -28.933 1.00 29.17 C ANISOU 2955 CG LEU B 170 3408 3780 3894 -256 -394 249 C ATOM 2956 CD1 LEU B 170 -11.561 -3.324 -28.622 1.00 29.35 C ANISOU 2956 CD1 LEU B 170 3353 3865 3933 -109 -401 322 C ATOM 2957 CD2 LEU B 170 -10.454 -4.756 -30.351 1.00 29.26 C ANISOU 2957 CD2 LEU B 170 3407 3812 3900 -282 -396 260 C ATOM 2958 N GLN B 171 -12.501 -5.635 -25.635 1.00 29.18 N ANISOU 2958 N GLN B 171 3476 3760 3852 -315 -369 176 N ATOM 2959 CA GLN B 171 -13.636 -6.495 -25.293 1.00 29.85 C ANISOU 2959 CA GLN B 171 3533 3977 3832 -439 -345 139 C ATOM 2960 C GLN B 171 -14.481 -6.759 -26.537 1.00 30.51 C ANISOU 2960 C GLN B 171 3507 4284 3801 -540 -337 145 C ATOM 2961 O GLN B 171 -14.365 -6.043 -27.533 1.00 30.51 O ANISOU 2961 O GLN B 171 3432 4355 3804 -474 -355 196 O ATOM 2962 CB GLN B 171 -14.486 -5.845 -24.196 1.00 30.22 C ANISOU 2962 CB GLN B 171 3526 4085 3873 -360 -348 167 C ATOM 2963 CG GLN B 171 -13.739 -5.625 -22.882 1.00 29.63 C ANISOU 2963 CG GLN B 171 3556 3807 3894 -279 -354 154 C ATOM 2964 CD GLN B 171 -14.371 -4.563 -21.998 1.00 29.90 C ANISOU 2964 CD GLN B 171 3539 3880 3944 -156 -357 199 C ATOM 2965 OE1 GLN B 171 -14.678 -4.812 -20.832 1.00 29.98 O ANISOU 2965 OE1 GLN B 171 3587 3854 3951 -163 -348 174 O ATOM 2966 NE2 GLN B 171 -14.559 -3.369 -22.545 1.00 30.20 N ANISOU 2966 NE2 GLN B 171 3499 3983 3992 -35 -363 267 N ATOM 2967 N SER B 172 -15.335 -7.780 -26.475 1.00 31.16 N ANISOU 2967 N SER B 172 3581 4485 3774 -706 -306 92 N ATOM 2968 CA SER B 172 -16.209 -8.140 -27.606 1.00 32.10 C ANISOU 2968 CA SER B 172 3590 4848 3760 -837 -295 84 C ATOM 2969 C SER B 172 -17.203 -7.030 -27.983 1.00 32.59 C ANISOU 2969 C SER B 172 3458 5161 3762 -732 -323 168 C ATOM 2970 O SER B 172 -17.662 -6.977 -29.118 1.00 33.42 O ANISOU 2970 O SER B 172 3454 5469 3777 -781 -329 189 O ATOM 2971 CB SER B 172 -16.964 -9.446 -27.327 1.00 32.92 C ANISOU 2971 CB SER B 172 3732 5029 3748 -1056 -246 1 C ATOM 2972 OG SER B 172 -17.794 -9.324 -26.187 1.00 33.30 O ANISOU 2972 OG SER B 172 3741 5140 3771 -1040 -242 5 O ATOM 2973 N SER B 173 -17.512 -6.141 -27.038 1.00 32.23 N ANISOU 2973 N SER B 173 3378 5104 3763 -580 -335 221 N ATOM 2974 CA SER B 173 -18.283 -4.922 -27.324 1.00 32.80 C ANISOU 2974 CA SER B 173 3294 5371 3796 -424 -349 320 C ATOM 2975 C SER B 173 -17.635 -3.965 -28.335 1.00 32.54 C ANISOU 2975 C SER B 173 3239 5308 3817 -286 -365 390 C ATOM 2976 O SER B 173 -18.329 -3.128 -28.918 1.00 33.25 O ANISOU 2976 O SER B 173 3193 5598 3842 -178 -366 475 O ATOM 2977 CB SER B 173 -18.528 -4.144 -26.031 1.00 32.48 C ANISOU 2977 CB SER B 173 3266 5260 3814 -275 -344 357 C ATOM 2978 OG SER B 173 -17.307 -3.669 -25.492 1.00 31.27 O ANISOU 2978 OG SER B 173 3253 4820 3810 -171 -351 354 O ATOM 2979 N GLY B 174 -16.317 -4.073 -28.519 1.00 31.52 N ANISOU 2979 N GLY B 174 3241 4936 3799 -282 -373 360 N ATOM 2980 CA GLY B 174 -15.542 -3.118 -29.309 1.00 31.23 C ANISOU 2980 CA GLY B 174 3210 4824 3832 -150 -383 421 C ATOM 2981 C GLY B 174 -14.904 -2.030 -28.460 1.00 30.55 C ANISOU 2981 C GLY B 174 3201 4539 3868 23 -379 459 C ATOM 2982 O GLY B 174 -14.219 -1.161 -28.994 1.00 30.54 O ANISOU 2982 O GLY B 174 3223 4452 3930 131 -377 506 O ATOM 2983 N LEU B 175 -15.115 -2.076 -27.144 1.00 30.26 N ANISOU 2983 N LEU B 175 3211 4428 3859 38 -372 434 N ATOM 2984 CA LEU B 175 -14.588 -1.074 -26.219 1.00 29.90 C ANISOU 2984 CA LEU B 175 3243 4203 3915 181 -362 459 C ATOM 2985 C LEU B 175 -13.410 -1.643 -25.435 1.00 29.01 C ANISOU 2985 C LEU B 175 3271 3853 3899 121 -376 384 C ATOM 2986 O LEU B 175 -13.324 -2.853 -25.212 1.00 28.75 O ANISOU 2986 O LEU B 175 3278 3804 3843 -13 -383 317 O ATOM 2987 CB LEU B 175 -15.682 -0.634 -25.246 1.00 30.46 C ANISOU 2987 CB LEU B 175 3262 4371 3941 256 -342 492 C ATOM 2988 CG LEU B 175 -16.981 -0.141 -25.882 1.00 31.76 C ANISOU 2988 CG LEU B 175 3268 4811 3988 329 -324 575 C ATOM 2989 CD1 LEU B 175 -18.063 0.048 -24.829 1.00 32.38 C ANISOU 2989 CD1 LEU B 175 3296 4994 4015 380 -302 596 C ATOM 2990 CD2 LEU B 175 -16.734 1.149 -26.654 1.00 32.14 C ANISOU 2990 CD2 LEU B 175 3303 4846 4060 502 -300 668 C ATOM 2991 N TYR B 176 -12.516 -0.757 -25.008 1.00 28.72 N ANISOU 2991 N TYR B 176 3312 3640 3959 221 -373 396 N ATOM 2992 CA TYR B 176 -11.330 -1.147 -24.247 1.00 28.08 C ANISOU 2992 CA TYR B 176 3348 3359 3962 183 -388 334 C ATOM 2993 C TYR B 176 -11.591 -1.142 -22.745 1.00 28.11 C ANISOU 2993 C TYR B 176 3397 3303 3980 201 -383 308 C ATOM 2994 O TYR B 176 -12.518 -0.490 -22.259 1.00 28.51 O ANISOU 2994 O TYR B 176 3405 3428 4000 275 -362 346 O ATOM 2995 CB TYR B 176 -10.152 -0.224 -24.576 1.00 27.73 C ANISOU 2995 CB TYR B 176 3359 3173 4005 256 -388 351 C ATOM 2996 CG TYR B 176 -9.693 -0.340 -26.009 1.00 27.77 C ANISOU 2996 CG TYR B 176 3335 3211 4005 229 -395 368 C ATOM 2997 CD1 TYR B 176 -8.768 -1.312 -26.391 1.00 27.26 C ANISOU 2997 CD1 TYR B 176 3316 3080 3963 137 -414 319 C ATOM 2998 CD2 TYR B 176 -10.195 0.514 -26.992 1.00 28.39 C ANISOU 2998 CD2 TYR B 176 3344 3391 4051 307 -375 440 C ATOM 2999 CE1 TYR B 176 -8.353 -1.428 -27.709 1.00 27.28 C ANISOU 2999 CE1 TYR B 176 3295 3112 3959 112 -417 333 C ATOM 3000 CE2 TYR B 176 -9.785 0.407 -28.312 1.00 28.41 C ANISOU 3000 CE2 TYR B 176 3320 3428 4046 282 -381 456 C ATOM 3001 CZ TYR B 176 -8.867 -0.565 -28.667 1.00 27.88 C ANISOU 3001 CZ TYR B 176 3299 3291 4005 179 -404 399 C ATOM 3002 OH TYR B 176 -8.463 -0.669 -29.977 1.00 27.93 O ANISOU 3002 OH TYR B 176 3281 3331 4001 154 -407 415 O ATOM 3003 N SER B 177 -10.762 -1.894 -22.027 1.00 27.78 N ANISOU 3003 N SER B 177 3441 3134 3978 141 -399 248 N ATOM 3004 CA SER B 177 -10.762 -1.912 -20.568 1.00 27.79 C ANISOU 3004 CA SER B 177 3500 3059 4001 157 -398 219 C ATOM 3005 C SER B 177 -9.331 -2.105 -20.079 1.00 27.34 C ANISOU 3005 C SER B 177 3534 2841 4014 149 -418 178 C ATOM 3006 O SER B 177 -8.610 -2.955 -20.604 1.00 27.00 O ANISOU 3006 O SER B 177 3519 2764 3976 89 -428 154 O ATOM 3007 CB SER B 177 -11.655 -3.043 -20.047 1.00 28.06 C ANISOU 3007 CB SER B 177 3524 3174 3963 68 -390 187 C ATOM 3008 OG SER B 177 -11.617 -3.131 -18.631 1.00 28.04 O ANISOU 3008 OG SER B 177 3582 3094 3979 83 -389 159 O ATOM 3009 N LEU B 178 -8.915 -1.304 -19.099 1.00 27.54 N ANISOU 3009 N LEU B 178 3603 2776 4084 209 -418 171 N ATOM 3010 CA LEU B 178 -7.624 -1.507 -18.438 1.00 27.32 C ANISOU 3010 CA LEU B 178 3645 2630 4105 197 -439 131 C ATOM 3011 C LEU B 178 -7.715 -1.301 -16.940 1.00 27.24 C ANISOU 3011 C LEU B 178 3679 2573 4097 219 -438 106 C ATOM 3012 O LEU B 178 -8.680 -0.730 -16.437 1.00 27.71 O ANISOU 3012 O LEU B 178 3723 2668 4137 259 -416 122 O ATOM 3013 CB LEU B 178 -6.524 -0.631 -19.058 1.00 27.42 C ANISOU 3013 CB LEU B 178 3668 2576 4173 226 -445 139 C ATOM 3014 CG LEU B 178 -6.361 0.870 -18.781 1.00 27.89 C ANISOU 3014 CG LEU B 178 3750 2579 4269 288 -421 152 C ATOM 3015 CD1 LEU B 178 -5.907 1.190 -17.360 1.00 27.97 C ANISOU 3015 CD1 LEU B 178 3818 2515 4293 288 -424 111 C ATOM 3016 CD2 LEU B 178 -5.354 1.434 -19.777 1.00 27.88 C ANISOU 3016 CD2 LEU B 178 3752 2534 4308 286 -420 162 C ATOM 3017 N SER B 179 -6.695 -1.788 -16.241 1.00 26.83 N ANISOU 3017 N SER B 179 3678 2453 4063 200 -461 69 N ATOM 3018 CA SER B 179 -6.582 -1.631 -14.800 1.00 26.79 C ANISOU 3018 CA SER B 179 3716 2406 4057 215 -465 41 C ATOM 3019 C SER B 179 -5.269 -0.945 -14.465 1.00 26.62 C ANISOU 3019 C SER B 179 3721 2319 4075 224 -483 18 C ATOM 3020 O SER B 179 -4.277 -1.110 -15.175 1.00 26.40 O ANISOU 3020 O SER B 179 3683 2279 4068 209 -500 17 O ATOM 3021 CB SER B 179 -6.648 -2.992 -14.111 1.00 26.70 C ANISOU 3021 CB SER B 179 3738 2400 4006 181 -471 20 C ATOM 3022 OG SER B 179 -5.552 -3.799 -14.495 1.00 26.65 O ANISOU 3022 OG SER B 179 3755 2365 4006 164 -486 12 O ATOM 3023 N SER B 180 -5.282 -0.162 -13.390 1.00 26.89 N ANISOU 3023 N SER B 180 3785 2319 4111 241 -476 -4 N ATOM 3024 CA SER B 180 -4.071 0.419 -12.817 1.00 27.09 C ANISOU 3024 CA SER B 180 3838 2302 4155 225 -491 -40 C ATOM 3025 C SER B 180 -4.041 0.041 -11.347 1.00 27.32 C ANISOU 3025 C SER B 180 3896 2332 4151 221 -506 -72 C ATOM 3026 O SER B 180 -5.031 0.240 -10.646 1.00 27.34 O ANISOU 3026 O SER B 180 3920 2333 4137 241 -483 -72 O ATOM 3027 CB SER B 180 -4.062 1.940 -12.974 1.00 27.50 C ANISOU 3027 CB SER B 180 3914 2301 4232 234 -454 -43 C ATOM 3028 OG SER B 180 -2.822 2.477 -12.549 1.00 27.75 O ANISOU 3028 OG SER B 180 3968 2303 4271 188 -465 -87 O ATOM 3029 N VAL B 181 -2.917 -0.512 -10.892 1.00 27.51 N ANISOU 3029 N VAL B 181 3920 2372 4160 204 -541 -94 N ATOM 3030 CA VAL B 181 -2.771 -0.950 -9.502 1.00 27.84 C ANISOU 3030 CA VAL B 181 3986 2431 4162 208 -557 -119 C ATOM 3031 C VAL B 181 -1.544 -0.329 -8.847 1.00 28.40 C ANISOU 3031 C VAL B 181 4051 2520 4219 177 -581 -159 C ATOM 3032 O VAL B 181 -0.628 0.134 -9.526 1.00 28.30 O ANISOU 3032 O VAL B 181 4011 2515 4225 148 -590 -167 O ATOM 3033 CB VAL B 181 -2.708 -2.496 -9.378 1.00 27.71 C ANISOU 3033 CB VAL B 181 3975 2442 4110 231 -569 -98 C ATOM 3034 CG1 VAL B 181 -3.933 -3.128 -10.027 1.00 27.48 C ANISOU 3034 CG1 VAL B 181 3954 2406 4080 231 -539 -70 C ATOM 3035 CG2 VAL B 181 -1.423 -3.068 -9.973 1.00 27.71 C ANISOU 3035 CG2 VAL B 181 3951 2470 4108 239 -592 -86 C ATOM 3036 N VAL B 182 -1.558 -0.320 -7.518 1.00 28.91 N ANISOU 3036 N VAL B 182 4139 2601 4243 174 -589 -188 N ATOM 3037 CA VAL B 182 -0.418 0.120 -6.716 1.00 29.70 C ANISOU 3037 CA VAL B 182 4226 2751 4307 133 -616 -231 C ATOM 3038 C VAL B 182 -0.391 -0.665 -5.407 1.00 30.13 C ANISOU 3038 C VAL B 182 4289 2858 4301 162 -639 -236 C ATOM 3039 O VAL B 182 -1.441 -0.945 -4.819 1.00 29.99 O ANISOU 3039 O VAL B 182 4312 2806 4276 189 -619 -228 O ATOM 3040 CB VAL B 182 -0.446 1.645 -6.436 1.00 30.18 C ANISOU 3040 CB VAL B 182 4325 2765 4379 70 -584 -281 C ATOM 3041 CG1 VAL B 182 -1.683 2.053 -5.636 1.00 30.27 C ANISOU 3041 CG1 VAL B 182 4399 2718 4386 90 -545 -289 C ATOM 3042 CG2 VAL B 182 0.833 2.092 -5.731 1.00 30.91 C ANISOU 3042 CG2 VAL B 182 4394 2929 4421 -3 -611 -336 C ATOM 3043 N THR B 183 0.815 -1.025 -4.975 1.00 30.91 N ANISOU 3043 N THR B 183 4344 3050 4349 160 -678 -243 N ATOM 3044 CA THR B 183 1.032 -1.718 -3.712 1.00 31.58 C ANISOU 3044 CA THR B 183 4431 3206 4364 197 -700 -243 C ATOM 3045 C THR B 183 1.553 -0.711 -2.694 1.00 32.61 C ANISOU 3045 C THR B 183 4550 3392 4447 123 -715 -307 C ATOM 3046 O THR B 183 2.512 0.006 -2.973 1.00 32.99 O ANISOU 3046 O THR B 183 4554 3494 4486 54 -729 -340 O ATOM 3047 CB THR B 183 2.055 -2.848 -3.879 1.00 31.77 C ANISOU 3047 CB THR B 183 4407 3322 4343 263 -728 -197 C ATOM 3048 OG1 THR B 183 3.205 -2.348 -4.570 1.00 32.15 O ANISOU 3048 OG1 THR B 183 4385 3437 4394 223 -751 -209 O ATOM 3049 CG2 THR B 183 1.445 -4.009 -4.665 1.00 31.14 C ANISOU 3049 CG2 THR B 183 4368 3174 4291 332 -698 -140 C ATOM 3050 N VAL B 184 0.909 -0.664 -1.527 1.00 33.23 N ANISOU 3050 N VAL B 184 4673 3459 4492 126 -706 -327 N ATOM 3051 CA VAL B 184 1.273 0.251 -0.437 1.00 34.23 C ANISOU 3051 CA VAL B 184 4807 3635 4565 48 -712 -394 C ATOM 3052 C VAL B 184 1.231 -0.491 0.905 1.00 34.87 C ANISOU 3052 C VAL B 184 4890 3793 4568 95 -735 -387 C ATOM 3053 O VAL B 184 0.701 -1.600 0.974 1.00 34.48 O ANISOU 3053 O VAL B 184 4860 3722 4518 187 -731 -331 O ATOM 3054 CB VAL B 184 0.336 1.487 -0.391 1.00 34.28 C ANISOU 3054 CB VAL B 184 4892 3517 4614 -10 -656 -438 C ATOM 3055 CG1 VAL B 184 0.352 2.218 -1.728 1.00 34.01 C ANISOU 3055 CG1 VAL B 184 4865 3407 4652 -41 -625 -436 C ATOM 3056 CG2 VAL B 184 -1.092 1.098 -0.005 1.00 33.87 C ANISOU 3056 CG2 VAL B 184 4900 3385 4585 58 -624 -410 C ATOM 3057 N PRO B 185 1.793 0.110 1.975 1.00 36.00 N ANISOU 3057 N PRO B 185 5018 4024 4635 26 -753 -445 N ATOM 3058 CA PRO B 185 1.677 -0.521 3.296 1.00 36.59 C ANISOU 3058 CA PRO B 185 5100 4172 4632 73 -771 -438 C ATOM 3059 C PRO B 185 0.233 -0.594 3.810 1.00 36.38 C ANISOU 3059 C PRO B 185 5165 4020 4637 107 -729 -433 C ATOM 3060 O PRO B 185 -0.494 0.400 3.745 1.00 36.15 O ANISOU 3060 O PRO B 185 5195 3889 4653 51 -686 -474 O ATOM 3061 CB PRO B 185 2.522 0.390 4.198 1.00 37.61 C ANISOU 3061 CB PRO B 185 5197 4419 4675 -40 -793 -516 C ATOM 3062 CG PRO B 185 3.476 1.062 3.276 1.00 37.84 C ANISOU 3062 CG PRO B 185 5169 4490 4719 -126 -802 -545 C ATOM 3063 CD PRO B 185 2.720 1.259 2.000 1.00 36.82 C ANISOU 3063 CD PRO B 185 5092 4191 4708 -103 -759 -518 C ATOM 3064 N SER B 186 -0.162 -1.762 4.320 1.00 36.57 N ANISOU 3064 N SER B 186 5205 4059 4632 203 -732 -380 N ATOM 3065 CA SER B 186 -1.490 -1.960 4.921 1.00 36.59 C ANISOU 3065 CA SER B 186 5285 3969 4650 233 -693 -374 C ATOM 3066 C SER B 186 -1.806 -0.954 6.036 1.00 37.40 C ANISOU 3066 C SER B 186 5427 4068 4717 164 -679 -442 C ATOM 3067 O SER B 186 -2.952 -0.520 6.172 1.00 36.96 O ANISOU 3067 O SER B 186 5434 3908 4699 159 -633 -455 O ATOM 3068 CB SER B 186 -1.618 -3.379 5.480 1.00 36.62 C ANISOU 3068 CB SER B 186 5305 4007 4602 332 -696 -313 C ATOM 3069 OG SER B 186 -1.509 -4.339 4.448 1.00 36.31 O ANISOU 3069 OG SER B 186 5259 3941 4595 394 -688 -252 O ATOM 3070 N SER B 187 -0.786 -0.597 6.818 1.00 38.65 N ANISOU 3070 N SER B 187 5545 4350 4792 111 -716 -486 N ATOM 3071 CA SER B 187 -0.924 0.367 7.916 1.00 39.81 C ANISOU 3071 CA SER B 187 5734 4505 4887 27 -701 -562 C ATOM 3072 C SER B 187 -1.151 1.823 7.477 1.00 40.56 C ANISOU 3072 C SER B 187 5883 4497 5032 -78 -651 -629 C ATOM 3073 O SER B 187 -1.559 2.644 8.297 1.00 41.12 O ANISOU 3073 O SER B 187 6022 4526 5074 -137 -613 -689 O ATOM 3074 CB SER B 187 0.307 0.308 8.824 1.00 40.76 C ANISOU 3074 CB SER B 187 5784 4816 4888 -15 -756 -592 C ATOM 3075 OG SER B 187 1.487 0.630 8.110 1.00 40.87 O ANISOU 3075 OG SER B 187 5717 4923 4889 -76 -787 -608 O ATOM 3076 N SER B 188 -0.864 2.144 6.213 1.00 40.88 N ANISOU 3076 N SER B 188 5901 4491 5138 -96 -643 -618 N ATOM 3077 CA SER B 188 -1.132 3.477 5.655 1.00 41.58 C ANISOU 3077 CA SER B 188 6057 4462 5278 -175 -581 -667 C ATOM 3078 C SER B 188 -2.594 3.699 5.236 1.00 41.51 C ANISOU 3078 C SER B 188 6125 4298 5349 -104 -515 -632 C ATOM 3079 O SER B 188 -2.989 4.838 4.987 1.00 42.00 O ANISOU 3079 O SER B 188 6264 4253 5441 -144 -446 -665 O ATOM 3080 CB SER B 188 -0.219 3.744 4.450 1.00 41.54 C ANISOU 3080 CB SER B 188 5999 4477 5307 -221 -595 -666 C ATOM 3081 OG SER B 188 -0.639 3.018 3.304 1.00 40.62 O ANISOU 3081 OG SER B 188 5853 4311 5270 -125 -601 -588 O ATOM 3082 N LEU B 189 -3.388 2.628 5.158 1.00 41.27 N ANISOU 3082 N LEU B 189 6075 4261 5344 0 -528 -564 N ATOM 3083 CA LEU B 189 -4.757 2.709 4.624 1.00 41.04 C ANISOU 3083 CA LEU B 189 6087 4125 5380 67 -474 -522 C ATOM 3084 C LEU B 189 -5.721 3.541 5.484 1.00 41.92 C ANISOU 3084 C LEU B 189 6287 4163 5478 67 -408 -554 C ATOM 3085 O LEU B 189 -6.672 4.119 4.960 1.00 42.03 O ANISOU 3085 O LEU B 189 6341 4089 5538 108 -345 -531 O ATOM 3086 CB LEU B 189 -5.330 1.304 4.405 1.00 40.19 C ANISOU 3086 CB LEU B 189 5939 4045 5285 151 -500 -452 C ATOM 3087 CG LEU B 189 -4.594 0.422 3.387 1.00 39.69 C ANISOU 3087 CG LEU B 189 5808 4027 5244 171 -544 -409 C ATOM 3088 CD1 LEU B 189 -5.126 -1.003 3.440 1.00 39.17 C ANISOU 3088 CD1 LEU B 189 5735 3980 5168 239 -553 -353 C ATOM 3089 CD2 LEU B 189 -4.705 0.992 1.978 1.00 39.32 C ANISOU 3089 CD2 LEU B 189 5748 3921 5269 163 -521 -393 C ATOM 3090 N GLY B 190 -5.473 3.598 6.791 1.00 43.05 N ANISOU 3090 N GLY B 190 6458 4351 5549 29 -418 -601 N ATOM 3091 CA GLY B 190 -6.251 4.441 7.700 1.00 43.90 C ANISOU 3091 CA GLY B 190 6660 4389 5632 19 -350 -641 C ATOM 3092 C GLY B 190 -5.942 5.930 7.613 1.00 45.07 C ANISOU 3092 C GLY B 190 6895 4453 5777 -64 -281 -707 C ATOM 3093 O GLY B 190 -6.819 6.757 7.876 1.00 45.55 O ANISOU 3093 O GLY B 190 7051 4412 5845 -39 -196 -718 O ATOM 3094 N THR B 191 -4.703 6.270 7.250 1.00 45.56 N ANISOU 3094 N THR B 191 6931 4558 5822 -161 -310 -751 N ATOM 3095 CA THR B 191 -4.225 7.661 7.233 1.00 46.62 C ANISOU 3095 CA THR B 191 7160 4618 5936 -274 -239 -828 C ATOM 3096 C THR B 191 -4.088 8.263 5.829 1.00 46.20 C ANISOU 3096 C THR B 191 7122 4481 5953 -274 -198 -806 C ATOM 3097 O THR B 191 -4.494 9.407 5.604 1.00 47.11 O ANISOU 3097 O THR B 191 7356 4461 6084 -287 -94 -827 O ATOM 3098 CB THR B 191 -2.857 7.775 7.937 1.00 47.69 C ANISOU 3098 CB THR B 191 7261 4879 5979 -420 -289 -911 C ATOM 3099 OG1 THR B 191 -1.896 6.944 7.274 1.00 47.62 O ANISOU 3099 OG1 THR B 191 7121 4998 5976 -420 -380 -878 O ATOM 3100 CG2 THR B 191 -2.967 7.349 9.395 1.00 48.24 C ANISOU 3100 CG2 THR B 191 7329 5034 5965 -427 -319 -940 C ATOM 3101 N GLN B 192 -3.508 7.502 4.901 1.00 45.00 N ANISOU 3101 N GLN B 192 6859 4403 5838 -254 -270 -760 N ATOM 3102 CA GLN B 192 -3.171 8.007 3.567 1.00 44.44 C ANISOU 3102 CA GLN B 192 6788 4274 5824 -268 -244 -743 C ATOM 3103 C GLN B 192 -4.328 7.835 2.582 1.00 43.12 C ANISOU 3103 C GLN B 192 6620 4026 5738 -132 -209 -654 C ATOM 3104 O GLN B 192 -4.878 6.739 2.448 1.00 42.13 O ANISOU 3104 O GLN B 192 6417 3956 5634 -42 -261 -591 O ATOM 3105 CB GLN B 192 -1.922 7.289 3.038 1.00 44.36 C ANISOU 3105 CB GLN B 192 6655 4395 5806 -315 -336 -739 C ATOM 3106 CG GLN B 192 -1.384 7.795 1.701 1.00 44.55 C ANISOU 3106 CG GLN B 192 6671 4375 5880 -348 -315 -730 C ATOM 3107 CD GLN B 192 -1.098 9.287 1.687 1.00 45.92 C ANISOU 3107 CD GLN B 192 6969 4444 6036 -464 -218 -804 C ATOM 3108 OE1 GLN B 192 -1.497 9.999 0.767 1.00 46.08 O ANISOU 3108 OE1 GLN B 192 7059 4339 6110 -434 -143 -779 O ATOM 3109 NE2 GLN B 192 -0.409 9.766 2.715 1.00 47.24 N ANISOU 3109 NE2 GLN B 192 7170 4661 6116 -599 -212 -897 N ATOM 3110 N THR B 193 -4.677 8.919 1.888 1.00 42.81 N ANISOU 3110 N THR B 193 6670 3864 5733 -121 -116 -648 N ATOM 3111 CA THR B 193 -5.697 8.890 0.836 1.00 41.81 C ANISOU 3111 CA THR B 193 6532 3683 5670 7 -80 -560 C ATOM 3112 C THR B 193 -5.068 8.459 -0.487 1.00 40.69 C ANISOU 3112 C THR B 193 6302 3583 5576 3 -131 -523 C ATOM 3113 O THR B 193 -3.962 8.885 -0.820 1.00 41.03 O ANISOU 3113 O THR B 193 6351 3625 5612 -97 -137 -568 O ATOM 3114 CB THR B 193 -6.355 10.273 0.648 1.00 42.61 C ANISOU 3114 CB THR B 193 6776 3636 5777 45 56 -557 C ATOM 3115 OG1 THR B 193 -6.867 10.734 1.903 1.00 43.33 O ANISOU 3115 OG1 THR B 193 6964 3680 5819 43 114 -599 O ATOM 3116 CG2 THR B 193 -7.493 10.213 -0.375 1.00 42.05 C ANISOU 3116 CG2 THR B 193 6675 3545 5756 197 91 -455 C ATOM 3117 N TYR B 194 -5.786 7.615 -1.230 1.00 39.28 N ANISOU 3117 N TYR B 194 6041 3446 5438 103 -165 -443 N ATOM 3118 CA TYR B 194 -5.325 7.088 -2.513 1.00 38.30 C ANISOU 3118 CA TYR B 194 5832 3362 5357 110 -212 -401 C ATOM 3119 C TYR B 194 -6.368 7.365 -3.586 1.00 38.24 C ANISOU 3119 C TYR B 194 5823 3314 5391 213 -160 -325 C ATOM 3120 O TYR B 194 -7.508 6.895 -3.491 1.00 38.01 O ANISOU 3120 O TYR B 194 5764 3319 5360 298 -155 -276 O ATOM 3121 CB TYR B 194 -5.039 5.589 -2.407 1.00 37.10 C ANISOU 3121 CB TYR B 194 5574 3323 5198 115 -311 -383 C ATOM 3122 CG TYR B 194 -3.878 5.286 -1.486 1.00 37.08 C ANISOU 3122 CG TYR B 194 5555 3389 5145 30 -366 -444 C ATOM 3123 CD1 TYR B 194 -2.570 5.612 -1.854 1.00 37.17 C ANISOU 3123 CD1 TYR B 194 5544 3431 5149 -58 -389 -482 C ATOM 3124 CD2 TYR B 194 -4.082 4.692 -0.237 1.00 36.93 C ANISOU 3124 CD2 TYR B 194 5534 3420 5076 36 -394 -461 C ATOM 3125 CE1 TYR B 194 -1.499 5.350 -1.008 1.00 37.46 C ANISOU 3125 CE1 TYR B 194 5544 3565 5122 -133 -442 -534 C ATOM 3126 CE2 TYR B 194 -3.015 4.425 0.613 1.00 37.23 C ANISOU 3126 CE2 TYR B 194 5547 3545 5055 -32 -446 -510 C ATOM 3127 CZ TYR B 194 -1.726 4.754 0.222 1.00 37.51 C ANISOU 3127 CZ TYR B 194 5547 3628 5076 -115 -471 -545 C ATOM 3128 OH TYR B 194 -0.669 4.497 1.060 1.00 37.78 O ANISOU 3128 OH TYR B 194 5536 3782 5036 -180 -524 -589 O ATOM 3129 N ILE B 195 -5.969 8.145 -4.589 1.00 38.48 N ANISOU 3129 N ILE B 195 5884 3286 5451 203 -117 -315 N ATOM 3130 CA ILE B 195 -6.852 8.577 -5.662 1.00 38.66 C ANISOU 3130 CA ILE B 195 5910 3276 5502 307 -58 -239 C ATOM 3131 C ILE B 195 -6.154 8.304 -6.986 1.00 38.32 C ANISOU 3131 C ILE B 195 5802 3260 5497 284 -97 -215 C ATOM 3132 O ILE B 195 -5.016 8.731 -7.178 1.00 38.60 O ANISOU 3132 O ILE B 195 5866 3262 5539 193 -99 -262 O ATOM 3133 CB ILE B 195 -7.167 10.091 -5.560 1.00 39.80 C ANISOU 3133 CB ILE B 195 6198 3288 5635 340 70 -243 C ATOM 3134 CG1 ILE B 195 -7.861 10.416 -4.227 1.00 40.41 C ANISOU 3134 CG1 ILE B 195 6354 3330 5672 366 120 -269 C ATOM 3135 CG2 ILE B 195 -8.030 10.548 -6.738 1.00 39.99 C ANISOU 3135 CG2 ILE B 195 6220 3294 5680 469 135 -150 C ATOM 3136 CD1 ILE B 195 -7.902 11.893 -3.878 1.00 41.67 C ANISOU 3136 CD1 ILE B 195 6687 3338 5807 367 255 -298 C ATOM 3137 N CYS B 196 -6.830 7.583 -7.884 1.00 37.69 N ANISOU 3137 N CYS B 196 5632 3252 5436 356 -127 -145 N ATOM 3138 CA CYS B 196 -6.353 7.417 -9.259 1.00 37.50 C ANISOU 3138 CA CYS B 196 5554 3248 5445 351 -150 -112 C ATOM 3139 C CYS B 196 -6.914 8.536 -10.130 1.00 38.14 C ANISOU 3139 C CYS B 196 5689 3265 5537 434 -57 -56 C ATOM 3140 O CYS B 196 -8.084 8.896 -10.010 1.00 38.39 O ANISOU 3140 O CYS B 196 5738 3300 5549 537 1 -5 O ATOM 3141 CB CYS B 196 -6.736 6.047 -9.835 1.00 36.76 C ANISOU 3141 CB CYS B 196 5344 3266 5356 371 -223 -71 C ATOM 3142 SG CYS B 196 -8.493 5.771 -10.160 1.00 36.92 S ANISOU 3142 SG CYS B 196 5310 3366 5353 482 -194 8 S ATOM 3143 N ASN B 197 -6.067 9.072 -11.003 1.00 38.49 N ANISOU 3143 N ASN B 197 5758 3259 5606 395 -39 -61 N ATOM 3144 CA ASN B 197 -6.428 10.178 -11.879 1.00 39.25 C ANISOU 3144 CA ASN B 197 5923 3281 5709 473 59 -6 C ATOM 3145 C ASN B 197 -6.405 9.636 -13.303 1.00 38.93 C ANISOU 3145 C ASN B 197 5783 3317 5693 501 16 52 C ATOM 3146 O ASN B 197 -5.338 9.335 -13.841 1.00 38.39 O ANISOU 3146 O ASN B 197 5683 3254 5650 416 -33 22 O ATOM 3147 CB ASN B 197 -5.447 11.349 -11.708 1.00 40.06 C ANISOU 3147 CB ASN B 197 6160 3246 5813 390 133 -66 C ATOM 3148 CG ASN B 197 -5.017 11.547 -10.262 1.00 40.27 C ANISOU 3148 CG ASN B 197 6258 3230 5811 294 137 -157 C ATOM 3149 OD1 ASN B 197 -3.865 11.299 -9.909 1.00 40.13 O ANISOU 3149 OD1 ASN B 197 6224 3234 5791 161 83 -231 O ATOM 3150 ND2 ASN B 197 -5.947 11.973 -9.417 1.00 40.78 N ANISOU 3150 ND2 ASN B 197 6396 3252 5847 365 202 -148 N ATOM 3151 N VAL B 198 -7.590 9.486 -13.893 1.00 39.29 N ANISOU 3151 N VAL B 198 5769 3437 5722 619 32 136 N ATOM 3152 CA VAL B 198 -7.742 8.895 -15.218 1.00 39.26 C ANISOU 3152 CA VAL B 198 5660 3529 5726 645 -9 192 C ATOM 3153 C VAL B 198 -8.052 9.994 -16.225 1.00 40.34 C ANISOU 3153 C VAL B 198 5846 3622 5858 746 82 266 C ATOM 3154 O VAL B 198 -9.033 10.716 -16.062 1.00 41.22 O ANISOU 3154 O VAL B 198 6000 3725 5935 869 165 324 O ATOM 3155 CB VAL B 198 -8.874 7.845 -15.233 1.00 38.84 C ANISOU 3155 CB VAL B 198 5491 3628 5640 688 -59 233 C ATOM 3156 CG1 VAL B 198 -9.024 7.226 -16.622 1.00 38.52 C ANISOU 3156 CG1 VAL B 198 5346 3695 5596 695 -98 283 C ATOM 3157 CG2 VAL B 198 -8.611 6.774 -14.180 1.00 38.29 C ANISOU 3157 CG2 VAL B 198 5394 3585 5568 598 -134 166 C ATOM 3158 N ASN B 199 -7.209 10.116 -17.250 1.00 40.77 N ANISOU 3158 N ASN B 199 5898 3651 5942 704 74 268 N ATOM 3159 CA ASN B 199 -7.412 11.069 -18.341 1.00 42.01 C ANISOU 3159 CA ASN B 199 6099 3771 6094 799 158 342 C ATOM 3160 C ASN B 199 -7.623 10.310 -19.650 1.00 41.97 C ANISOU 3160 C ASN B 199 5961 3900 6084 820 98 398 C ATOM 3161 O ASN B 199 -6.777 9.502 -20.045 1.00 41.44 O ANISOU 3161 O ASN B 199 5836 3862 6047 714 17 355 O ATOM 3162 CB ASN B 199 -6.207 12.003 -18.468 1.00 42.49 C ANISOU 3162 CB ASN B 199 6287 3674 6184 722 217 294 C ATOM 3163 N HIS B 200 -8.764 10.556 -20.296 1.00 43.13 N ANISOU 3163 N HIS B 200 6060 4143 6186 958 139 495 N ATOM 3164 CA HIS B 200 -9.057 10.038 -21.634 1.00 43.36 C ANISOU 3164 CA HIS B 200 5971 4308 6194 986 100 556 C ATOM 3165 C HIS B 200 -9.337 11.229 -22.555 1.00 45.09 C ANISOU 3165 C HIS B 200 6248 4494 6391 1124 204 650 C ATOM 3166 O HIS B 200 -10.480 11.679 -22.682 1.00 46.02 O ANISOU 3166 O HIS B 200 6343 4695 6449 1277 264 740 O ATOM 3167 CB HIS B 200 -10.237 9.060 -21.593 1.00 42.89 C ANISOU 3167 CB HIS B 200 5770 4447 6080 1012 44 588 C ATOM 3168 CG HIS B 200 -10.566 8.455 -22.922 1.00 42.59 C ANISOU 3168 CG HIS B 200 5607 4569 6007 1016 2 639 C ATOM 3169 ND1 HIS B 200 -11.792 8.618 -23.528 1.00 43.29 N ANISOU 3169 ND1 HIS B 200 5602 4828 6017 1137 31 735 N ATOM 3170 CD2 HIS B 200 -9.826 7.704 -23.771 1.00 41.82 C ANISOU 3170 CD2 HIS B 200 5461 4495 5934 915 -63 609 C ATOM 3171 CE1 HIS B 200 -11.797 7.989 -24.689 1.00 42.99 C ANISOU 3171 CE1 HIS B 200 5463 4917 5954 1097 -17 755 C ATOM 3172 NE2 HIS B 200 -10.615 7.425 -24.860 1.00 42.09 N ANISOU 3172 NE2 HIS B 200 5382 4706 5905 963 -72 679 N ATOM 3173 N LYS B 201 -8.270 11.732 -23.178 1.00 46.01 N ANISOU 3173 N LYS B 201 6440 4492 6549 1074 230 631 N ATOM 3174 CA LYS B 201 -8.313 12.941 -24.015 1.00 47.70 C ANISOU 3174 CA LYS B 201 6746 4630 6747 1192 344 711 C ATOM 3175 C LYS B 201 -9.287 12.884 -25.202 1.00 48.81 C ANISOU 3175 C LYS B 201 6776 4944 6825 1334 352 830 C ATOM 3176 O LYS B 201 -9.958 13.880 -25.474 1.00 50.20 O ANISOU 3176 O LYS B 201 7014 5105 6954 1504 464 927 O ATOM 3177 CB LYS B 201 -6.909 13.292 -24.527 1.00 47.38 C ANISOU 3177 CB LYS B 201 6789 4452 6761 1079 355 658 C ATOM 3178 N PRO B 202 -9.370 11.732 -25.910 1.00 48.57 N ANISOU 3178 N PRO B 202 6586 5083 6785 1267 243 826 N ATOM 3179 CA PRO B 202 -10.300 11.609 -27.044 1.00 49.20 C ANISOU 3179 CA PRO B 202 6542 5359 6791 1380 243 932 C ATOM 3180 C PRO B 202 -11.763 11.956 -26.748 1.00 50.35 C ANISOU 3180 C PRO B 202 6636 5646 6850 1552 296 1026 C ATOM 3181 O PRO B 202 -12.412 12.580 -27.583 1.00 51.71 O ANISOU 3181 O PRO B 202 6780 5911 6956 1712 361 1140 O ATOM 3182 CB PRO B 202 -10.168 10.138 -27.432 1.00 48.17 C ANISOU 3182 CB PRO B 202 6267 5374 6662 1236 114 877 C ATOM 3183 CG PRO B 202 -8.754 9.819 -27.112 1.00 47.19 C ANISOU 3183 CG PRO B 202 6217 5086 6626 1079 71 770 C ATOM 3184 CD PRO B 202 -8.473 10.560 -25.835 1.00 47.32 C ANISOU 3184 CD PRO B 202 6370 4933 6679 1083 128 726 C ATOM 3185 N SER B 203 -12.262 11.562 -25.576 1.00 50.36 N ANISOU 3185 N SER B 203 6620 5669 6845 1526 272 983 N ATOM 3186 CA SER B 203 -13.641 11.860 -25.163 1.00 51.32 C ANISOU 3186 CA SER B 203 6686 5929 6882 1685 323 1067 C ATOM 3187 C SER B 203 -13.779 13.056 -24.201 1.00 52.31 C ANISOU 3187 C SER B 203 6982 5878 7015 1807 447 1088 C ATOM 3188 O SER B 203 -14.869 13.289 -23.677 1.00 53.00 O ANISOU 3188 O SER B 203 7036 6064 7037 1938 493 1150 O ATOM 3189 CB SER B 203 -14.254 10.626 -24.503 1.00 50.58 C ANISOU 3189 CB SER B 203 6459 5995 6763 1582 225 1012 C ATOM 3190 OG SER B 203 -13.730 10.441 -23.198 1.00 49.62 O ANISOU 3190 OG SER B 203 6433 5714 6706 1481 208 911 O ATOM 3191 N ASN B 204 -12.689 13.791 -23.964 1.00 52.52 N ANISOU 3191 N ASN B 204 7191 5653 7113 1756 506 1035 N ATOM 3192 CA ASN B 204 -12.667 14.929 -23.034 1.00 53.77 C ANISOU 3192 CA ASN B 204 7541 5611 7278 1837 635 1034 C ATOM 3193 C ASN B 204 -13.122 14.545 -21.610 1.00 53.72 C ANISOU 3193 C ASN B 204 7530 5611 7271 1799 609 974 C ATOM 3194 O ASN B 204 -13.915 15.256 -20.979 1.00 54.75 O ANISOU 3194 O ASN B 204 7731 5717 7355 1946 709 1029 O ATOM 3195 CB ASN B 204 -13.504 16.090 -23.605 1.00 55.62 C ANISOU 3195 CB ASN B 204 7838 5859 7437 2090 783 1182 C ATOM 3196 CG ASN B 204 -13.123 17.437 -23.015 1.00 56.78 C ANISOU 3196 CG ASN B 204 8243 5733 7599 2156 947 1179 C ATOM 3197 OD1 ASN B 204 -11.969 17.855 -23.090 1.00 56.78 O ANISOU 3197 OD1 ASN B 204 8383 5530 7659 2035 978 1106 O ATOM 3198 ND2 ASN B 204 -14.098 18.126 -22.433 1.00 58.03 N ANISOU 3198 ND2 ASN B 204 8466 5889 7694 2344 1062 1257 N ATOM 3199 N THR B 205 -12.593 13.422 -21.115 1.00 52.42 N ANISOU 3199 N THR B 205 7291 5473 7154 1608 480 865 N ATOM 3200 CA THR B 205 -12.957 12.863 -19.806 1.00 51.91 C ANISOU 3200 CA THR B 205 7205 5429 7089 1551 437 802 C ATOM 3201 C THR B 205 -11.769 12.914 -18.841 1.00 51.12 C ANISOU 3201 C THR B 205 7234 5131 7060 1391 422 677 C ATOM 3202 O THR B 205 -10.648 12.549 -19.205 1.00 50.51 O ANISOU 3202 O THR B 205 7159 4998 7035 1252 361 611 O ATOM 3203 CB THR B 205 -13.433 11.399 -19.948 1.00 51.20 C ANISOU 3203 CB THR B 205 6919 5558 6978 1466 305 784 C ATOM 3204 OG1 THR B 205 -14.597 11.352 -20.781 1.00 52.10 O ANISOU 3204 OG1 THR B 205 6899 5890 7008 1600 318 895 O ATOM 3205 CG2 THR B 205 -13.768 10.775 -18.587 1.00 50.88 C ANISOU 3205 CG2 THR B 205 6865 5531 6937 1400 263 717 C ATOM 3206 N LYS B 206 -12.030 13.372 -17.616 1.00 51.26 N ANISOU 3206 N LYS B 206 7352 5058 7069 1414 480 647 N ATOM 3207 CA LYS B 206 -11.057 13.342 -16.527 1.00 50.63 C ANISOU 3207 CA LYS B 206 7372 4829 7035 1259 459 525 C ATOM 3208 C LYS B 206 -11.769 12.892 -15.255 1.00 50.34 C ANISOU 3208 C LYS B 206 7308 4844 6974 1262 435 497 C ATOM 3209 O LYS B 206 -12.683 13.574 -14.789 1.00 51.46 O ANISOU 3209 O LYS B 206 7507 4973 7071 1401 530 552 O ATOM 3210 CB LYS B 206 -10.428 14.719 -16.318 1.00 51.71 C ANISOU 3210 CB LYS B 206 7722 4743 7182 1267 593 505 C ATOM 3211 N VAL B 207 -11.355 11.748 -14.708 1.00 48.73 N ANISOU 3211 N VAL B 207 7021 4698 6794 1121 315 417 N ATOM 3212 CA VAL B 207 -11.986 11.157 -13.520 1.00 48.24 C ANISOU 3212 CA VAL B 207 6924 4695 6709 1108 281 387 C ATOM 3213 C VAL B 207 -10.962 11.026 -12.393 1.00 47.43 C ANISOU 3213 C VAL B 207 6905 4477 6640 962 247 272 C ATOM 3214 O VAL B 207 -9.831 10.598 -12.627 1.00 46.76 O ANISOU 3214 O VAL B 207 6807 4366 6594 836 180 212 O ATOM 3215 CB VAL B 207 -12.583 9.762 -13.828 1.00 47.47 C ANISOU 3215 CB VAL B 207 6648 4797 6594 1077 174 403 C ATOM 3216 CG1 VAL B 207 -13.432 9.263 -12.660 1.00 47.44 C ANISOU 3216 CG1 VAL B 207 6611 4860 6553 1086 159 387 C ATOM 3217 CG2 VAL B 207 -13.403 9.801 -15.114 1.00 48.02 C ANISOU 3217 CG2 VAL B 207 6612 5010 6623 1187 190 507 C ATOM 3218 N ASP B 208 -11.373 11.395 -11.179 1.00 47.47 N ANISOU 3218 N ASP B 208 6987 4428 6621 985 296 245 N ATOM 3219 CA ASP B 208 -10.558 11.240 -9.978 1.00 47.17 C ANISOU 3219 CA ASP B 208 7016 4311 6596 854 263 139 C ATOM 3220 C ASP B 208 -11.319 10.385 -8.970 1.00 46.80 C ANISOU 3220 C ASP B 208 6900 4359 6521 858 212 128 C ATOM 3221 O ASP B 208 -12.222 10.881 -8.287 1.00 47.63 O ANISOU 3221 O ASP B 208 7055 4452 6591 951 284 154 O ATOM 3222 CB ASP B 208 -10.224 12.607 -9.376 1.00 48.29 C ANISOU 3222 CB ASP B 208 7348 4274 6727 855 386 103 C ATOM 3223 CG ASP B 208 -9.294 13.428 -10.257 1.00 48.75 C ANISOU 3223 CG ASP B 208 7493 4220 6809 813 441 94 C ATOM 3224 OD1 ASP B 208 -8.305 12.874 -10.778 1.00 47.95 O ANISOU 3224 OD1 ASP B 208 7326 4150 6741 699 355 56 O ATOM 3225 OD2 ASP B 208 -9.547 14.639 -10.422 1.00 50.34 O ANISOU 3225 OD2 ASP B 208 7839 4297 6992 897 579 128 O ATOM 3226 N LYS B 209 -10.952 9.106 -8.882 1.00 45.38 N ANISOU 3226 N LYS B 209 6616 4272 6356 763 97 92 N ATOM 3227 CA LYS B 209 -11.670 8.139 -8.048 1.00 45.12 C ANISOU 3227 CA LYS B 209 6514 4336 6294 758 46 85 C ATOM 3228 C LYS B 209 -10.865 7.798 -6.798 1.00 44.77 C ANISOU 3228 C LYS B 209 6520 4240 6252 650 3 -6 C ATOM 3229 O LYS B 209 -9.783 7.214 -6.894 1.00 43.95 O ANISOU 3229 O LYS B 209 6393 4136 6171 549 -68 -54 O ATOM 3230 CB LYS B 209 -11.954 6.864 -8.854 1.00 44.42 C ANISOU 3230 CB LYS B 209 6283 4389 6204 733 -36 115 C ATOM 3231 CG LYS B 209 -12.916 5.868 -8.207 1.00 44.40 C ANISOU 3231 CG LYS B 209 6208 4501 6162 733 -70 121 C ATOM 3232 CD LYS B 209 -14.321 6.412 -7.962 1.00 45.33 C ANISOU 3232 CD LYS B 209 6309 4684 6231 855 3 183 C ATOM 3233 CE LYS B 209 -14.939 7.038 -9.207 1.00 46.06 C ANISOU 3233 CE LYS B 209 6352 4843 6307 965 53 272 C ATOM 3234 NZ LYS B 209 -16.414 7.207 -9.088 1.00 47.05 N ANISOU 3234 NZ LYS B 209 6409 5101 6366 1084 104 345 N ATOM 3235 N LYS B 210 -11.399 8.165 -5.633 1.00 45.26 N ANISOU 3235 N LYS B 210 6646 4269 6283 678 48 -26 N ATOM 3236 CA LYS B 210 -10.811 7.785 -4.350 1.00 45.28 C ANISOU 3236 CA LYS B 210 6685 4248 6273 586 7 -105 C ATOM 3237 C LYS B 210 -11.018 6.288 -4.137 1.00 44.55 C ANISOU 3237 C LYS B 210 6485 4270 6170 553 -85 -104 C ATOM 3238 O LYS B 210 -12.125 5.778 -4.326 1.00 44.64 O ANISOU 3238 O LYS B 210 6428 4370 6163 613 -83 -52 O ATOM 3239 CB LYS B 210 -11.445 8.571 -3.193 1.00 46.33 C ANISOU 3239 CB LYS B 210 6918 4316 6369 633 88 -122 C ATOM 3240 CG LYS B 210 -10.784 8.339 -1.836 1.00 46.48 C ANISOU 3240 CG LYS B 210 6986 4310 6365 534 52 -209 C ATOM 3241 CD LYS B 210 -11.451 9.139 -0.726 1.00 47.45 C ANISOU 3241 CD LYS B 210 7215 4365 6448 579 140 -227 C ATOM 3242 CE LYS B 210 -10.838 8.801 0.627 1.00 47.60 C ANISOU 3242 CE LYS B 210 7267 4384 6435 478 96 -311 C ATOM 3243 NZ LYS B 210 -11.589 9.382 1.772 1.00 48.41 N ANISOU 3243 NZ LYS B 210 7463 4437 6495 521 173 -328 N ATOM 3244 N VAL B 211 -9.944 5.602 -3.753 1.00 43.89 N ANISOU 3244 N VAL B 211 6392 4192 6092 457 -158 -159 N ATOM 3245 CA VAL B 211 -9.960 4.170 -3.506 1.00 43.31 C ANISOU 3245 CA VAL B 211 6247 4204 6005 424 -232 -160 C ATOM 3246 C VAL B 211 -9.630 3.965 -2.033 1.00 43.77 C ANISOU 3246 C VAL B 211 6352 4250 6028 383 -250 -216 C ATOM 3247 O VAL B 211 -8.542 4.325 -1.584 1.00 43.77 O ANISOU 3247 O VAL B 211 6392 4215 6023 321 -267 -270 O ATOM 3248 CB VAL B 211 -8.927 3.437 -4.390 1.00 42.64 C ANISOU 3248 CB VAL B 211 6110 4146 5947 370 -296 -162 C ATOM 3249 CG1 VAL B 211 -9.080 1.923 -4.259 1.00 41.97 C ANISOU 3249 CG1 VAL B 211 5971 4133 5841 351 -349 -152 C ATOM 3250 CG2 VAL B 211 -9.065 3.874 -5.845 1.00 42.36 C ANISOU 3250 CG2 VAL B 211 6041 4108 5945 402 -273 -115 C ATOM 3251 N GLU B 212 -10.574 3.391 -1.289 1.00 44.34 N ANISOU 3251 N GLU B 212 6413 4365 6068 412 -245 -204 N ATOM 3252 CA GLU B 212 -10.439 3.215 0.157 1.00 45.10 C ANISOU 3252 CA GLU B 212 6556 4455 6125 386 -255 -250 C ATOM 3253 C GLU B 212 -10.956 1.838 0.589 1.00 45.01 C ANISOU 3253 C GLU B 212 6503 4516 6085 386 -291 -233 C ATOM 3254 O GLU B 212 -11.654 1.174 -0.187 1.00 44.19 O ANISOU 3254 O GLU B 212 6340 4463 5986 403 -292 -189 O ATOM 3255 CB GLU B 212 -11.180 4.342 0.891 1.00 46.20 C ANISOU 3255 CB GLU B 212 6770 4539 6246 431 -177 -261 C ATOM 3256 CG GLU B 212 -12.695 4.363 0.700 1.00 46.54 C ANISOU 3256 CG GLU B 212 6782 4623 6277 521 -126 -200 C ATOM 3257 CD GLU B 212 -13.321 5.707 1.052 1.00 47.66 C ANISOU 3257 CD GLU B 212 7005 4695 6407 593 -29 -194 C ATOM 3258 OE1 GLU B 212 -12.779 6.424 1.921 1.00 48.45 O ANISOU 3258 OE1 GLU B 212 7204 4713 6493 558 0 -252 O ATOM 3259 OE2 GLU B 212 -14.363 6.050 0.459 1.00 48.08 O ANISOU 3259 OE2 GLU B 212 7027 4783 6457 687 25 -129 O ATOM 3260 N PRO B 213 -10.612 1.398 1.821 1.00 45.57 N ANISOU 3260 N PRO B 213 6606 4593 6116 359 -315 -270 N ATOM 3261 CA PRO B 213 -11.111 0.101 2.310 1.00 45.78 C ANISOU 3261 CA PRO B 213 6614 4671 6108 360 -334 -254 C ATOM 3262 C PRO B 213 -12.636 0.022 2.415 1.00 46.36 C ANISOU 3262 C PRO B 213 6671 4777 6165 398 -285 -222 C ATOM 3263 O PRO B 213 -13.303 1.057 2.509 1.00 46.77 O ANISOU 3263 O PRO B 213 6738 4811 6221 442 -235 -216 O ATOM 3264 CB PRO B 213 -10.483 -0.018 3.706 1.00 45.96 C ANISOU 3264 CB PRO B 213 6686 4692 6086 340 -356 -298 C ATOM 3265 CG PRO B 213 -9.284 0.857 3.662 1.00 46.22 C ANISOU 3265 CG PRO B 213 6735 4698 6128 302 -374 -339 C ATOM 3266 CD PRO B 213 -9.664 2.005 2.777 1.00 46.17 C ANISOU 3266 CD PRO B 213 6736 4637 6167 318 -325 -330 C ATOM 3267 N LYS B 214 -13.167 -1.200 2.400 1.00 46.56 N ANISOU 3267 N LYS B 214 6671 4854 6164 380 -293 -201 N ATOM 3268 CA LYS B 214 -14.607 -1.432 2.556 1.00 47.24 C ANISOU 3268 CA LYS B 214 6730 5000 6220 396 -250 -175 C ATOM 3269 C LYS B 214 -15.079 -0.971 3.938 1.00 48.11 C ANISOU 3269 C LYS B 214 6888 5094 6296 425 -220 -197 C ATOM 3270 O LYS B 214 -14.331 -1.065 4.917 1.00 48.53 O ANISOU 3270 O LYS B 214 6998 5107 6332 410 -243 -234 O ATOM 3271 CB LYS B 214 -14.947 -2.913 2.352 1.00 46.90 C ANISOU 3271 CB LYS B 214 6670 5005 6145 343 -257 -162 C ATOM 3272 N SER B 215 -16.319 -0.484 4.004 1.00 48.63 N ANISOU 3272 N SER B 215 6926 5206 6345 470 -168 -171 N ATOM 3273 CA SER B 215 -16.893 0.092 5.233 1.00 49.11 C ANISOU 3273 CA SER B 215 7034 5252 6373 510 -126 -187 C ATOM 3274 C SER B 215 -16.868 -0.860 6.439 1.00 48.91 C ANISOU 3274 C SER B 215 7049 5231 6303 470 -143 -214 C ATOM 3275 O SER B 215 -16.742 -0.419 7.584 1.00 49.11 O ANISOU 3275 O SER B 215 7136 5216 6306 485 -131 -246 O ATOM 3276 CB SER B 215 -18.332 0.559 4.970 1.00 49.92 C ANISOU 3276 CB SER B 215 7079 5434 6454 575 -64 -140 C ATOM 3277 OG SER B 215 -18.861 1.250 6.087 1.00 50.87 O ANISOU 3277 OG SER B 215 7252 5532 6546 629 -14 -151 O ATOM 3278 N CYS B 216 -16.988 -2.157 6.169 1.00 48.16 N ANISOU 3278 N CYS B 216 6929 5180 6189 417 -163 -202 N ATOM 3279 CA CYS B 216 -16.905 -3.196 7.197 1.00 47.92 C ANISOU 3279 CA CYS B 216 6950 5146 6113 382 -170 -219 C ATOM 3280 C CYS B 216 -15.507 -3.401 7.811 1.00 48.17 C ANISOU 3280 C CYS B 216 7043 5116 6142 376 -217 -249 C ATOM 3281 O CYS B 216 -15.397 -3.912 8.931 1.00 48.79 O ANISOU 3281 O CYS B 216 7175 5189 6176 374 -218 -264 O ATOM 3282 CB CYS B 216 -17.369 -4.519 6.597 1.00 47.27 C ANISOU 3282 CB CYS B 216 6843 5111 6005 321 -161 -198 C ATOM 3283 SG CYS B 216 -16.326 -5.089 5.232 1.00 46.11 S ANISOU 3283 SG CYS B 216 6684 4938 5898 286 -201 -188 S ATOM 3284 N ASP B 217 -14.453 -3.043 7.074 1.00 47.86 N ANISOU 3284 N ASP B 217 6992 5049 6145 375 -256 -255 N ATOM 3285 CA ASP B 217 -13.072 -3.300 7.501 1.00 47.84 C ANISOU 3285 CA ASP B 217 7023 5023 6130 368 -305 -276 C ATOM 3286 C ASP B 217 -12.669 -2.444 8.697 1.00 48.33 C ANISOU 3286 C ASP B 217 7127 5071 6165 377 -310 -319 C ATOM 3287 O ASP B 217 -12.839 -1.228 8.682 1.00 48.62 O ANISOU 3287 O ASP B 217 7169 5079 6223 383 -288 -342 O ATOM 3288 CB ASP B 217 -12.102 -3.049 6.344 1.00 47.43 C ANISOU 3288 CB ASP B 217 6935 4959 6126 358 -340 -272 C TER 3289 ASP B 217 ATOM 3290 N THR C 204 -0.470 -6.169 -72.460 1.00 50.64 N ANISOU 3290 N THR C 204 6382 7158 5702 -1466 -1330 748 N ATOM 3291 CA THR C 204 0.821 -5.884 -71.760 1.00 48.34 C ANISOU 3291 CA THR C 204 6195 6682 5491 -1279 -1143 668 C ATOM 3292 C THR C 204 1.450 -7.162 -71.200 1.00 48.27 C ANISOU 3292 C THR C 204 6382 6456 5503 -1426 -1166 629 C ATOM 3293 O THR C 204 0.785 -7.932 -70.500 1.00 49.49 O ANISOU 3293 O THR C 204 6459 6678 5667 -1647 -1248 715 O ATOM 3294 CB THR C 204 0.635 -4.857 -70.615 1.00 47.61 C ANISOU 3294 CB THR C 204 5842 6767 5480 -1122 -995 726 C ATOM 3295 OG1 THR C 204 0.207 -3.603 -71.162 1.00 47.90 O ANISOU 3295 OG1 THR C 204 5747 6950 5502 -935 -972 747 O ATOM 3296 CG2 THR C 204 1.934 -4.637 -69.833 1.00 45.62 C ANISOU 3296 CG2 THR C 204 5696 6334 5305 -972 -830 651 C ATOM 3297 N VAL C 205 2.729 -7.370 -71.512 1.00 46.66 N ANISOU 3297 N VAL C 205 6424 6003 5302 -1300 -1096 510 N ATOM 3298 CA VAL C 205 3.508 -8.485 -70.986 1.00 46.44 C ANISOU 3298 CA VAL C 205 6602 5744 5300 -1367 -1104 460 C ATOM 3299 C VAL C 205 4.650 -7.894 -70.154 1.00 44.28 C ANISOU 3299 C VAL C 205 6301 5412 5113 -1153 -910 423 C ATOM 3300 O VAL C 205 5.423 -7.087 -70.674 1.00 42.75 O ANISOU 3300 O VAL C 205 6138 5188 4916 -950 -803 357 O ATOM 3301 CB VAL C 205 4.086 -9.364 -72.116 1.00 47.41 C ANISOU 3301 CB VAL C 205 7054 5627 5333 -1380 -1200 338 C ATOM 3302 CG1 VAL C 205 4.734 -10.621 -71.543 1.00 47.84 C ANISOU 3302 CG1 VAL C 205 7332 5432 5412 -1450 -1241 296 C ATOM 3303 CG2 VAL C 205 2.997 -9.737 -73.119 1.00 49.54 C ANISOU 3303 CG2 VAL C 205 7360 5964 5498 -1574 -1398 360 C ATOM 3304 N PRO C 206 4.765 -8.293 -68.866 1.00 43.99 N ANISOU 3304 N PRO C 206 6206 5366 5143 -1213 -874 475 N ATOM 3305 CA PRO C 206 5.831 -7.747 -68.023 1.00 42.26 C ANISOU 3305 CA PRO C 206 5956 5103 4998 -1028 -709 443 C ATOM 3306 C PRO C 206 7.206 -8.321 -68.396 1.00 41.75 C ANISOU 3306 C PRO C 206 6141 4791 4931 -912 -677 332 C ATOM 3307 O PRO C 206 7.275 -9.472 -68.833 1.00 43.08 O ANISOU 3307 O PRO C 206 6524 4789 5055 -1006 -793 293 O ATOM 3308 CB PRO C 206 5.421 -8.183 -66.614 1.00 42.58 C ANISOU 3308 CB PRO C 206 5879 5219 5081 -1159 -712 541 C ATOM 3309 CG PRO C 206 4.667 -9.448 -66.824 1.00 44.64 C ANISOU 3309 CG PRO C 206 6244 5422 5295 -1423 -890 597 C ATOM 3310 CD PRO C 206 3.965 -9.303 -68.145 1.00 45.64 C ANISOU 3310 CD PRO C 206 6389 5601 5350 -1473 -993 575 C ATOM 3311 N PRO C 207 8.291 -7.530 -68.237 1.00 40.19 N ANISOU 3311 N PRO C 207 5917 4577 4776 -706 -528 282 N ATOM 3312 CA PRO C 207 9.626 -8.054 -68.553 1.00 40.02 C ANISOU 3312 CA PRO C 207 6088 4371 4746 -577 -484 187 C ATOM 3313 C PRO C 207 10.165 -9.070 -67.551 1.00 40.44 C ANISOU 3313 C PRO C 207 6232 4288 4846 -606 -506 195 C ATOM 3314 O PRO C 207 9.883 -8.973 -66.355 1.00 40.07 O ANISOU 3314 O PRO C 207 6054 4316 4856 -675 -489 276 O ATOM 3315 CB PRO C 207 10.521 -6.803 -68.543 1.00 38.52 C ANISOU 3315 CB PRO C 207 5790 4253 4593 -390 -325 166 C ATOM 3316 CG PRO C 207 9.604 -5.639 -68.513 1.00 38.11 C ANISOU 3316 CG PRO C 207 5552 4377 4553 -409 -307 230 C ATOM 3317 CD PRO C 207 8.350 -6.106 -67.857 1.00 38.83 C ANISOU 3317 CD PRO C 207 5549 4554 4650 -582 -404 308 C ATOM 3318 N MET C 208 10.927 -10.036 -68.061 1.00 41.74 N ANISOU 3318 N MET C 208 6629 4258 4974 -539 -547 110 N ATOM 3319 CA MET C 208 11.785 -10.883 -67.240 1.00 42.32 C ANISOU 3319 CA MET C 208 6810 4181 5091 -483 -549 102 C ATOM 3320 C MET C 208 13.116 -10.143 -67.138 1.00 40.26 C ANISOU 3320 C MET C 208 6465 3969 4864 -253 -387 55 C ATOM 3321 O MET C 208 13.744 -9.867 -68.160 1.00 39.99 O ANISOU 3321 O MET C 208 6484 3937 4775 -110 -325 -28 O ATOM 3322 CB MET C 208 12.000 -12.249 -67.898 1.00 45.24 C ANISOU 3322 CB MET C 208 7486 4305 5396 -480 -677 19 C ATOM 3323 CG MET C 208 10.729 -13.031 -68.215 1.00 47.94 C ANISOU 3323 CG MET C 208 7951 4575 5689 -737 -866 57 C ATOM 3324 SD MET C 208 9.756 -13.562 -66.788 1.00 50.11 S ANISOU 3324 SD MET C 208 8137 4876 6027 -1021 -969 231 S ATOM 3325 CE MET C 208 10.920 -14.606 -65.923 1.00 50.66 C ANISOU 3325 CE MET C 208 8410 4697 6144 -905 -986 219 C ATOM 3326 N VAL C 209 13.540 -9.813 -65.919 1.00 38.67 N ANISOU 3326 N VAL C 209 6128 3825 4739 -231 -322 114 N ATOM 3327 CA VAL C 209 14.780 -9.059 -65.708 1.00 37.43 C ANISOU 3327 CA VAL C 209 5867 3735 4619 -52 -184 88 C ATOM 3328 C VAL C 209 15.838 -9.951 -65.075 1.00 37.92 C ANISOU 3328 C VAL C 209 6020 3679 4709 58 -192 73 C ATOM 3329 O VAL C 209 15.550 -10.662 -64.113 1.00 37.98 O ANISOU 3329 O VAL C 209 6070 3615 4748 -34 -271 135 O ATOM 3330 CB VAL C 209 14.557 -7.818 -64.820 1.00 35.93 C ANISOU 3330 CB VAL C 209 5450 3714 4487 -91 -106 155 C ATOM 3331 CG1 VAL C 209 15.842 -6.991 -64.719 1.00 34.97 C ANISOU 3331 CG1 VAL C 209 5235 3656 4398 58 15 131 C ATOM 3332 CG2 VAL C 209 13.407 -6.975 -65.365 1.00 35.69 C ANISOU 3332 CG2 VAL C 209 5333 3796 4431 -177 -113 178 C ATOM 3333 N ASN C 210 17.059 -9.894 -65.608 1.00 38.17 N ANISOU 3333 N ASN C 210 6070 3711 4724 257 -109 4 N ATOM 3334 CA ASN C 210 18.150 -10.765 -65.161 1.00 39.37 C ANISOU 3334 CA ASN C 210 6302 3763 4892 412 -117 -20 C ATOM 3335 C ASN C 210 19.467 -9.987 -65.139 1.00 38.61 C ANISOU 3335 C ASN C 210 6037 3817 4815 580 22 -31 C ATOM 3336 O ASN C 210 19.784 -9.284 -66.102 1.00 38.51 O ANISOU 3336 O ASN C 210 5965 3910 4756 643 114 -70 O ATOM 3337 CB ASN C 210 18.256 -11.976 -66.100 1.00 41.77 C ANISOU 3337 CB ASN C 210 6874 3877 5119 514 -196 -118 C ATOM 3338 CG ASN C 210 18.927 -13.176 -65.451 1.00 43.75 C ANISOU 3338 CG ASN C 210 7279 3953 5393 633 -272 -123 C ATOM 3339 OD1 ASN C 210 18.531 -13.617 -64.370 1.00 44.24 O ANISOU 3339 OD1 ASN C 210 7361 3939 5510 506 -361 -33 O ATOM 3340 ND2 ASN C 210 19.933 -13.732 -66.126 1.00 45.54 N ANISOU 3340 ND2 ASN C 210 7620 4119 5566 889 -239 -226 N ATOM 3341 N VAL C 211 20.214 -10.111 -64.040 1.00 37.87 N ANISOU 3341 N VAL C 211 5862 3745 4782 633 28 18 N ATOM 3342 CA VAL C 211 21.516 -9.458 -63.883 1.00 37.46 C ANISOU 3342 CA VAL C 211 5632 3848 4752 768 138 24 C ATOM 3343 C VAL C 211 22.625 -10.506 -63.940 1.00 39.27 C ANISOU 3343 C VAL C 211 5941 4016 4964 1001 129 -19 C ATOM 3344 O VAL C 211 22.557 -11.524 -63.251 1.00 39.66 O ANISOU 3344 O VAL C 211 6122 3912 5035 1025 25 -1 O ATOM 3345 CB VAL C 211 21.609 -8.679 -62.552 1.00 36.09 C ANISOU 3345 CB VAL C 211 5281 3780 4652 661 147 111 C ATOM 3346 CG1 VAL C 211 22.984 -8.036 -62.384 1.00 36.20 C ANISOU 3346 CG1 VAL C 211 5111 3956 4687 769 236 126 C ATOM 3347 CG2 VAL C 211 20.522 -7.612 -62.487 1.00 34.60 C ANISOU 3347 CG2 VAL C 211 5020 3652 4473 476 160 139 C ATOM 3348 N THR C 212 23.641 -10.239 -64.761 1.00 40.42 N ANISOU 3348 N THR C 212 6004 4291 5063 1177 238 -67 N ATOM 3349 CA THR C 212 24.838 -11.077 -64.858 1.00 42.95 C ANISOU 3349 CA THR C 212 6345 4615 5356 1448 257 -110 C ATOM 3350 C THR C 212 26.088 -10.222 -64.690 1.00 43.63 C ANISOU 3350 C THR C 212 6148 4969 5461 1526 378 -60 C ATOM 3351 O THR C 212 26.043 -9.001 -64.843 1.00 42.41 O ANISOU 3351 O THR C 212 5827 4969 5317 1380 454 -14 O ATOM 3352 CB THR C 212 24.908 -11.813 -66.211 1.00 44.53 C ANISOU 3352 CB THR C 212 6740 4737 5444 1633 276 -235 C ATOM 3353 OG1 THR C 212 24.717 -10.877 -67.277 1.00 43.96 O ANISOU 3353 OG1 THR C 212 6588 4811 5303 1568 382 -256 O ATOM 3354 CG2 THR C 212 23.840 -12.893 -66.291 1.00 44.98 C ANISOU 3354 CG2 THR C 212 7109 4499 5482 1567 121 -286 C ATOM 3355 N ARG C 213 27.200 -10.880 -64.377 1.00 46.34 N ANISOU 3355 N ARG C 213 6441 5361 5805 1755 383 -63 N ATOM 3356 CA ARG C 213 28.476 -10.206 -64.142 1.00 47.80 C ANISOU 3356 CA ARG C 213 6333 5823 6005 1831 480 -2 C ATOM 3357 C ARG C 213 29.607 -10.919 -64.875 1.00 51.51 C ANISOU 3357 C ARG C 213 6773 6404 6395 2167 556 -66 C ATOM 3358 O ARG C 213 29.638 -12.150 -64.928 1.00 53.12 O ANISOU 3358 O ARG C 213 7185 6427 6571 2383 485 -139 O ATOM 3359 CB ARG C 213 28.777 -10.123 -62.642 1.00 47.14 C ANISOU 3359 CB ARG C 213 6135 5759 6016 1754 398 95 C ATOM 3360 CG ARG C 213 28.786 -11.456 -61.903 1.00 48.11 C ANISOU 3360 CG ARG C 213 6436 5682 6162 1900 269 91 C ATOM 3361 CD ARG C 213 29.031 -11.250 -60.416 1.00 47.47 C ANISOU 3361 CD ARG C 213 6233 5647 6156 1795 189 199 C ATOM 3362 NE ARG C 213 30.420 -10.884 -60.120 1.00 48.43 N ANISOU 3362 NE ARG C 213 6079 6034 6289 1921 241 253 N ATOM 3363 CZ ARG C 213 30.846 -10.279 -59.007 1.00 47.98 C ANISOU 3363 CZ ARG C 213 5836 6113 6281 1797 201 347 C ATOM 3364 NH1 ARG C 213 30.007 -9.932 -58.030 1.00 46.44 N ANISOU 3364 NH1 ARG C 213 5703 5820 6123 1560 120 392 N ATOM 3365 NH2 ARG C 213 32.142 -10.007 -58.867 1.00 49.54 N ANISOU 3365 NH2 ARG C 213 5774 6569 6481 1911 241 397 N ATOM 3366 N SER C 214 30.523 -10.133 -65.440 1.00 53.71 N ANISOU 3366 N SER C 214 6798 6982 6628 2210 698 -34 N ATOM 3367 CA SER C 214 31.695 -10.655 -66.145 1.00 57.59 C ANISOU 3367 CA SER C 214 7189 7666 7025 2539 802 -82 C ATOM 3368 C SER C 214 32.820 -10.954 -65.159 1.00 60.17 C ANISOU 3368 C SER C 214 7312 8140 7411 2693 773 -9 C ATOM 3369 O SER C 214 32.705 -10.660 -63.965 1.00 59.59 O ANISOU 3369 O SER C 214 7171 8026 7443 2517 676 81 O ATOM 3370 CB SER C 214 32.183 -9.641 -67.184 1.00 58.10 C ANISOU 3370 CB SER C 214 7042 8033 7001 2488 972 -52 C ATOM 3371 OG SER C 214 32.791 -8.522 -66.558 1.00 57.42 O ANISOU 3371 OG SER C 214 6650 8183 6985 2288 1004 90 O ATOM 3372 N GLU C 215 33.909 -11.528 -65.670 1.00 64.10 N ANISOU 3372 N GLU C 215 7701 8826 7827 3034 859 -49 N ATOM 3373 CA GLU C 215 35.116 -11.764 -64.874 1.00 66.89 C ANISOU 3373 CA GLU C 215 7805 9389 8221 3216 846 29 C ATOM 3374 C GLU C 215 35.841 -10.444 -64.593 1.00 67.46 C ANISOU 3374 C GLU C 215 7485 9821 8326 2987 923 175 C ATOM 3375 O GLU C 215 35.670 -9.462 -65.326 1.00 66.88 O ANISOU 3375 O GLU C 215 7322 9881 8209 2785 1028 201 O ATOM 3376 CB GLU C 215 36.057 -12.736 -65.591 1.00 70.24 C ANISOU 3376 CB GLU C 215 8214 9941 8534 3680 926 -63 C ATOM 3377 N ALA C 216 36.646 -10.436 -63.531 1.00 69.09 N ANISOU 3377 N ALA C 216 7474 10174 8604 3010 856 276 N ATOM 3378 CA ALA C 216 37.392 -9.243 -63.115 1.00 69.71 C ANISOU 3378 CA ALA C 216 7188 10580 8719 2772 892 421 C ATOM 3379 C ALA C 216 38.541 -8.948 -64.083 1.00 72.96 C ANISOU 3379 C ALA C 216 7282 11414 9024 2925 1069 459 C ATOM 3380 O ALA C 216 39.512 -9.707 -64.149 1.00 76.11 O ANISOU 3380 O ALA C 216 7530 12013 9375 3274 1106 452 O ATOM 3381 CB ALA C 216 37.924 -9.415 -61.698 1.00 70.12 C ANISOU 3381 CB ALA C 216 7110 10671 8861 2763 750 513 C ATOM 3382 N SER C 217 38.419 -7.847 -64.827 1.00 72.92 N ANISOU 3382 N SER C 217 7176 11553 8976 2669 1177 508 N ATOM 3383 CA SER C 217 39.399 -7.473 -65.853 1.00 75.83 C ANISOU 3383 CA SER C 217 7250 12339 9223 2761 1361 562 C ATOM 3384 C SER C 217 40.688 -6.934 -65.216 1.00 78.06 C ANISOU 3384 C SER C 217 7095 13026 9537 2686 1361 729 C ATOM 3385 O SER C 217 41.728 -7.597 -65.271 1.00 81.61 O ANISOU 3385 O SER C 217 7317 13760 9932 3012 1417 742 O ATOM 3386 CB SER C 217 38.787 -6.463 -66.842 1.00 74.70 C ANISOU 3386 CB SER C 217 7170 12194 9019 2484 1458 580 C ATOM 3387 OG SER C 217 39.722 -6.067 -67.832 1.00 77.35 O ANISOU 3387 OG SER C 217 7217 12951 9221 2542 1641 654 O ATOM 3388 N GLU C 218 40.610 -5.745 -64.615 1.00 76.59 N ANISOU 3388 N GLU C 218 6800 12865 9434 2265 1289 853 N ATOM 3389 CA GLU C 218 41.734 -5.141 -63.889 1.00 78.11 C ANISOU 3389 CA GLU C 218 6605 13405 9668 2113 1247 1019 C ATOM 3390 C GLU C 218 41.223 -4.630 -62.544 1.00 75.52 C ANISOU 3390 C GLU C 218 6388 12830 9475 1808 1046 1052 C ATOM 3391 O GLU C 218 41.379 -3.454 -62.204 1.00 75.34 O ANISOU 3391 O GLU C 218 6239 12894 9494 1432 997 1164 O ATOM 3392 CB GLU C 218 42.353 -4.005 -64.708 1.00 79.66 C ANISOU 3392 CB GLU C 218 6517 13961 9790 1861 1377 1160 C ATOM 3393 N GLY C 219 40.611 -5.539 -61.786 1.00 73.56 N ANISOU 3393 N GLY C 219 6394 12269 9286 1974 928 953 N ATOM 3394 CA GLY C 219 39.892 -5.192 -60.562 1.00 70.64 C ANISOU 3394 CA GLY C 219 6199 11622 9019 1722 752 955 C ATOM 3395 C GLY C 219 38.568 -4.476 -60.804 1.00 67.15 C ANISOU 3395 C GLY C 219 6051 10863 8601 1451 745 894 C ATOM 3396 O GLY C 219 38.051 -3.814 -59.898 1.00 65.34 O ANISOU 3396 O GLY C 219 5913 10476 8439 1183 625 912 O ATOM 3397 N ASN C 220 38.016 -4.618 -62.014 1.00 65.84 N ANISOU 3397 N ASN C 220 6034 10614 8369 1539 869 818 N ATOM 3398 CA ASN C 220 36.767 -3.961 -62.413 1.00 62.54 C ANISOU 3398 CA ASN C 220 5875 9926 7961 1316 872 765 C ATOM 3399 C ASN C 220 35.834 -4.980 -63.061 1.00 60.21 C ANISOU 3399 C ASN C 220 5881 9372 7625 1545 903 624 C ATOM 3400 O ASN C 220 36.226 -5.681 -63.999 1.00 61.74 O ANISOU 3400 O ASN C 220 6056 9673 7728 1814 1012 573 O ATOM 3401 CB ASN C 220 37.039 -2.811 -63.395 1.00 63.92 C ANISOU 3401 CB ASN C 220 5913 10294 8081 1107 985 847 C ATOM 3402 CG ASN C 220 37.317 -1.490 -62.695 1.00 64.35 C ANISOU 3402 CG ASN C 220 5835 10416 8199 736 900 965 C ATOM 3403 OD1 ASN C 220 38.087 -1.428 -61.735 1.00 65.98 O ANISOU 3403 OD1 ASN C 220 5853 10766 8450 684 811 1035 O ATOM 3404 ND2 ASN C 220 36.692 -0.420 -63.181 1.00 63.49 N ANISOU 3404 ND2 ASN C 220 5840 10196 8089 477 914 989 N ATOM 3405 N ILE C 221 34.604 -5.046 -62.554 1.00 56.05 N ANISOU 3405 N ILE C 221 5627 8516 7154 1432 804 561 N ATOM 3406 CA ILE C 221 33.579 -5.964 -63.042 1.00 53.91 C ANISOU 3406 CA ILE C 221 5659 7971 6854 1579 797 440 C ATOM 3407 C ILE C 221 32.644 -5.198 -63.976 1.00 51.10 C ANISOU 3407 C ILE C 221 5433 7520 6462 1403 855 412 C ATOM 3408 O ILE C 221 32.368 -4.019 -63.747 1.00 49.57 O ANISOU 3408 O ILE C 221 5193 7333 6308 1133 838 475 O ATOM 3409 CB ILE C 221 32.743 -6.547 -61.872 1.00 52.81 C ANISOU 3409 CB ILE C 221 5723 7553 6790 1543 645 410 C ATOM 3410 CG1 ILE C 221 33.643 -7.030 -60.718 1.00 54.19 C ANISOU 3410 CG1 ILE C 221 5755 7827 7009 1646 559 471 C ATOM 3411 CG2 ILE C 221 31.826 -7.666 -62.361 1.00 52.62 C ANISOU 3411 CG2 ILE C 221 5999 7261 6732 1699 620 300 C ATOM 3412 CD1 ILE C 221 34.751 -7.977 -61.128 1.00 56.92 C ANISOU 3412 CD1 ILE C 221 5982 8340 7305 1992 610 461 C ATOM 3413 N THR C 222 32.169 -5.868 -65.025 1.00 49.85 N ANISOU 3413 N THR C 222 5452 7266 6223 1565 912 317 N ATOM 3414 CA THR C 222 31.096 -5.342 -65.872 1.00 47.59 C ANISOU 3414 CA THR C 222 5335 6849 5898 1421 938 280 C ATOM 3415 C THR C 222 29.805 -6.065 -65.501 1.00 45.12 C ANISOU 3415 C THR C 222 5306 6215 5622 1412 822 197 C ATOM 3416 O THR C 222 29.737 -7.291 -65.596 1.00 45.53 O ANISOU 3416 O THR C 222 5509 6145 5645 1621 787 115 O ATOM 3417 CB THR C 222 31.392 -5.552 -67.372 1.00 48.99 C ANISOU 3417 CB THR C 222 5522 7159 5935 1582 1073 233 C ATOM 3418 OG1 THR C 222 32.604 -4.875 -67.719 1.00 50.46 O ANISOU 3418 OG1 THR C 222 5415 7683 6074 1571 1190 334 O ATOM 3419 CG2 THR C 222 30.252 -5.016 -68.243 1.00 47.66 C ANISOU 3419 CG2 THR C 222 5534 6856 5720 1430 1081 204 C ATOM 3420 N VAL C 223 28.797 -5.303 -65.073 1.00 42.32 N ANISOU 3420 N VAL C 223 5022 5730 5326 1170 759 222 N ATOM 3421 CA VAL C 223 27.474 -5.857 -64.754 1.00 40.52 C ANISOU 3421 CA VAL C 223 5028 5242 5125 1119 657 164 C ATOM 3422 C VAL C 223 26.505 -5.508 -65.877 1.00 39.61 C ANISOU 3422 C VAL C 223 5045 5057 4949 1046 685 124 C ATOM 3423 O VAL C 223 26.485 -4.373 -66.351 1.00 38.91 O ANISOU 3423 O VAL C 223 4872 5065 4846 918 743 173 O ATOM 3424 CB VAL C 223 26.917 -5.401 -63.374 1.00 39.03 C ANISOU 3424 CB VAL C 223 4826 4972 5031 935 559 214 C ATOM 3425 CG1 VAL C 223 27.722 -6.031 -62.245 1.00 39.73 C ANISOU 3425 CG1 VAL C 223 4837 5095 5165 1025 502 246 C ATOM 3426 CG2 VAL C 223 26.878 -3.882 -63.216 1.00 37.99 C ANISOU 3426 CG2 VAL C 223 4574 4931 4931 729 585 276 C ATOM 3427 N THR C 224 25.727 -6.500 -66.306 1.00 39.55 N ANISOU 3427 N THR C 224 5253 4876 4899 1122 631 41 N ATOM 3428 CA THR C 224 24.768 -6.352 -67.395 1.00 39.03 C ANISOU 3428 CA THR C 224 5328 4740 4760 1065 635 -4 C ATOM 3429 C THR C 224 23.385 -6.724 -66.882 1.00 37.81 C ANISOU 3429 C THR C 224 5331 4384 4650 933 509 -18 C ATOM 3430 O THR C 224 23.188 -7.830 -66.372 1.00 37.97 O ANISOU 3430 O THR C 224 5478 4260 4688 989 422 -50 O ATOM 3431 CB THR C 224 25.130 -7.270 -68.576 1.00 40.89 C ANISOU 3431 CB THR C 224 5690 4974 4870 1278 681 -102 C ATOM 3432 OG1 THR C 224 26.453 -6.963 -69.031 1.00 42.32 O ANISOU 3432 OG1 THR C 224 5692 5393 4996 1415 814 -79 O ATOM 3433 CG2 THR C 224 24.145 -7.098 -69.733 1.00 40.93 C ANISOU 3433 CG2 THR C 224 5845 4922 4784 1207 672 -148 C ATOM 3434 N CYS C 225 22.441 -5.794 -67.015 1.00 36.31 N ANISOU 3434 N CYS C 225 5128 4193 4474 761 497 17 N ATOM 3435 CA CYS C 225 21.051 -6.017 -66.641 1.00 35.45 C ANISOU 3435 CA CYS C 225 5126 3951 4392 629 391 17 C ATOM 3436 C CYS C 225 20.227 -6.181 -67.908 1.00 35.81 C ANISOU 3436 C CYS C 225 5309 3950 4347 613 369 -32 C ATOM 3437 O CYS C 225 20.146 -5.254 -68.709 1.00 35.71 O ANISOU 3437 O CYS C 225 5248 4028 4292 582 427 -13 O ATOM 3438 CB CYS C 225 20.531 -4.838 -65.827 1.00 34.02 C ANISOU 3438 CB CYS C 225 4822 3820 4283 477 386 86 C ATOM 3439 SG CYS C 225 18.843 -5.054 -65.243 1.00 33.46 S ANISOU 3439 SG CYS C 225 4821 3656 4235 328 276 102 S ATOM 3440 N ARG C 226 19.623 -7.355 -68.083 1.00 36.48 N ANISOU 3440 N ARG C 226 5576 3887 4397 621 272 -88 N ATOM 3441 CA ARG C 226 18.859 -7.676 -69.287 1.00 37.15 C ANISOU 3441 CA ARG C 226 5818 3917 4382 601 225 -147 C ATOM 3442 C ARG C 226 17.367 -7.741 -68.980 1.00 36.19 C ANISOU 3442 C ARG C 226 5737 3726 4287 407 104 -109 C ATOM 3443 O ARG C 226 16.962 -8.406 -68.029 1.00 35.95 O ANISOU 3443 O ARG C 226 5740 3604 4314 330 20 -82 O ATOM 3444 CB ARG C 226 19.311 -9.023 -69.850 1.00 39.44 C ANISOU 3444 CB ARG C 226 6317 4079 4590 756 186 -253 C ATOM 3445 CG ARG C 226 20.754 -9.058 -70.325 1.00 40.85 C ANISOU 3445 CG ARG C 226 6447 4362 4711 986 315 -301 C ATOM 3446 CD ARG C 226 21.087 -10.404 -70.950 1.00 43.30 C ANISOU 3446 CD ARG C 226 6997 4532 4922 1176 269 -429 C ATOM 3447 NE ARG C 226 22.416 -10.413 -71.566 1.00 45.13 N ANISOU 3447 NE ARG C 226 7166 4913 5069 1427 410 -482 N ATOM 3448 CZ ARG C 226 22.727 -9.873 -72.748 1.00 46.30 C ANISOU 3448 CZ ARG C 226 7278 5225 5088 1494 522 -512 C ATOM 3449 NH1 ARG C 226 21.811 -9.248 -73.495 1.00 45.95 N ANISOU 3449 NH1 ARG C 226 7269 5202 4987 1334 501 -495 N ATOM 3450 NH2 ARG C 226 23.979 -9.951 -73.194 1.00 48.01 N ANISOU 3450 NH2 ARG C 226 7409 5609 5222 1728 659 -549 N ATOM 3451 N ALA C 227 16.565 -7.039 -69.782 1.00 35.51 N ANISOU 3451 N ALA C 227 5635 3705 4153 327 96 -96 N ATOM 3452 CA ALA C 227 15.105 -7.159 -69.762 1.00 35.18 C ANISOU 3452 CA ALA C 227 5623 3635 4110 158 -23 -64 C ATOM 3453 C ALA C 227 14.677 -7.889 -71.034 1.00 36.38 C ANISOU 3453 C ALA C 227 5972 3713 4139 154 -106 -140 C ATOM 3454 O ALA C 227 15.158 -7.557 -72.117 1.00 36.51 O ANISOU 3454 O ALA C 227 6027 3782 4061 255 -40 -187 O ATOM 3455 CB ALA C 227 14.459 -5.785 -69.690 1.00 34.03 C ANISOU 3455 CB ALA C 227 5307 3625 3997 89 11 12 C ATOM 3456 N SER C 228 13.790 -8.880 -70.904 1.00 37.03 N ANISOU 3456 N SER C 228 6184 3677 4209 24 -255 -148 N ATOM 3457 CA SER C 228 13.358 -9.694 -72.053 1.00 38.70 C ANISOU 3457 CA SER C 228 6620 3788 4296 -3 -366 -233 C ATOM 3458 C SER C 228 11.889 -10.106 -71.980 1.00 39.26 C ANISOU 3458 C SER C 228 6721 3832 4362 -244 -538 -181 C ATOM 3459 O SER C 228 11.285 -10.104 -70.905 1.00 38.70 O ANISOU 3459 O SER C 228 6527 3792 4384 -381 -576 -84 O ATOM 3460 CB SER C 228 14.238 -10.940 -72.177 1.00 40.16 C ANISOU 3460 CB SER C 228 7040 3783 4437 135 -392 -343 C ATOM 3461 OG SER C 228 14.190 -11.715 -70.990 1.00 40.49 O ANISOU 3461 OG SER C 228 7115 3695 4573 67 -465 -299 O ATOM 3462 N SER C 229 11.337 -10.451 -73.146 1.00 40.51 N ANISOU 3462 N SER C 229 7036 3958 4400 -298 -642 -241 N ATOM 3463 CA SER C 229 9.961 -10.949 -73.293 1.00 41.42 C ANISOU 3463 CA SER C 229 7197 4055 4485 -545 -831 -197 C ATOM 3464 C SER C 229 8.892 -9.958 -72.806 1.00 39.96 C ANISOU 3464 C SER C 229 6726 4091 4368 -680 -829 -58 C ATOM 3465 O SER C 229 7.937 -10.352 -72.130 1.00 40.41 O ANISOU 3465 O SER C 229 6713 4172 4468 -884 -938 30 O ATOM 3466 CB SER C 229 9.802 -12.307 -72.587 1.00 42.84 C ANISOU 3466 CB SER C 229 7555 4023 4699 -675 -971 -198 C ATOM 3467 OG SER C 229 10.829 -13.205 -72.970 1.00 44.15 O ANISOU 3467 OG SER C 229 7995 3973 4807 -503 -972 -334 O ATOM 3468 N PHE C 230 9.048 -8.682 -73.167 1.00 38.32 N ANISOU 3468 N PHE C 230 6356 4045 4159 -563 -708 -34 N ATOM 3469 CA PHE C 230 8.094 -7.636 -72.760 1.00 37.18 C ANISOU 3469 CA PHE C 230 5952 4102 4071 -630 -698 83 C ATOM 3470 C PHE C 230 7.398 -6.952 -73.937 1.00 37.61 C ANISOU 3470 C PHE C 230 5976 4281 4032 -637 -749 99 C ATOM 3471 O PHE C 230 7.915 -6.927 -75.053 1.00 38.07 O ANISOU 3471 O PHE C 230 6182 4297 3984 -546 -735 24 O ATOM 3472 CB PHE C 230 8.753 -6.592 -71.841 1.00 35.25 C ANISOU 3472 CB PHE C 230 5528 3932 3934 -495 -529 125 C ATOM 3473 CG PHE C 230 9.896 -5.837 -72.465 1.00 34.38 C ANISOU 3473 CG PHE C 230 5450 3815 3798 -307 -394 76 C ATOM 3474 CD1 PHE C 230 9.665 -4.673 -73.188 1.00 34.06 C ANISOU 3474 CD1 PHE C 230 5330 3889 3721 -251 -358 114 C ATOM 3475 CD2 PHE C 230 11.208 -6.270 -72.298 1.00 34.09 C ANISOU 3475 CD2 PHE C 230 5509 3672 3770 -190 -304 7 C ATOM 3476 CE1 PHE C 230 10.714 -3.968 -73.757 1.00 33.64 C ANISOU 3476 CE1 PHE C 230 5304 3841 3637 -113 -236 94 C ATOM 3477 CE2 PHE C 230 12.265 -5.567 -72.860 1.00 33.70 C ANISOU 3477 CE2 PHE C 230 5456 3659 3689 -39 -175 -18 C ATOM 3478 CZ PHE C 230 12.018 -4.416 -73.593 1.00 33.46 C ANISOU 3478 CZ PHE C 230 5356 3740 3619 -17 -140 30 C ATOM 3479 N TYR C 231 6.210 -6.422 -73.657 1.00 37.56 N ANISOU 3479 N TYR C 231 5771 4445 4056 -736 -810 202 N ATOM 3480 CA TYR C 231 5.430 -5.625 -74.599 1.00 38.20 C ANISOU 3480 CA TYR C 231 5773 4675 4065 -729 -866 247 C ATOM 3481 C TYR C 231 4.559 -4.672 -73.766 1.00 37.49 C ANISOU 3481 C TYR C 231 5399 4782 4064 -720 -839 362 C ATOM 3482 O TYR C 231 3.986 -5.117 -72.774 1.00 37.66 O ANISOU 3482 O TYR C 231 5303 4861 4146 -838 -872 415 O ATOM 3483 CB TYR C 231 4.544 -6.528 -75.469 1.00 40.43 C ANISOU 3483 CB TYR C 231 6171 4958 4234 -915 -1067 234 C ATOM 3484 CG TYR C 231 3.708 -5.773 -76.482 1.00 41.44 C ANISOU 3484 CG TYR C 231 6219 5254 4275 -912 -1147 287 C ATOM 3485 CD1 TYR C 231 2.443 -5.281 -76.149 1.00 42.12 C ANISOU 3485 CD1 TYR C 231 6050 5558 4396 -991 -1223 408 C ATOM 3486 CD2 TYR C 231 4.189 -5.531 -77.770 1.00 42.05 C ANISOU 3486 CD2 TYR C 231 6463 5292 4222 -815 -1143 223 C ATOM 3487 CE1 TYR C 231 1.682 -4.576 -77.071 1.00 43.19 C ANISOU 3487 CE1 TYR C 231 6105 5853 4452 -966 -1306 466 C ATOM 3488 CE2 TYR C 231 3.435 -4.829 -78.699 1.00 43.08 C ANISOU 3488 CE2 TYR C 231 6527 5576 4264 -809 -1226 284 C ATOM 3489 CZ TYR C 231 2.185 -4.353 -78.344 1.00 43.69 C ANISOU 3489 CZ TYR C 231 6356 5854 4390 -880 -1314 406 C ATOM 3490 OH TYR C 231 1.438 -3.657 -79.263 1.00 45.23 O ANISOU 3490 OH TYR C 231 6481 6206 4498 -855 -1408 474 O ATOM 3491 N PRO C 232 4.424 -3.392 -74.136 1.00 36.85 N ANISOU 3491 N PRO C 232 5213 4806 3983 -578 -785 404 N ATOM 3492 CA PRO C 232 4.982 -2.785 -75.351 1.00 36.76 C ANISOU 3492 CA PRO C 232 5326 4756 3885 -463 -755 374 C ATOM 3493 C PRO C 232 6.478 -2.452 -75.266 1.00 35.29 C ANISOU 3493 C PRO C 232 5245 4437 3727 -324 -591 315 C ATOM 3494 O PRO C 232 7.116 -2.714 -74.247 1.00 34.07 O ANISOU 3494 O PRO C 232 5071 4210 3663 -309 -507 289 O ATOM 3495 CB PRO C 232 4.139 -1.512 -75.510 1.00 37.13 C ANISOU 3495 CB PRO C 232 5197 4967 3944 -375 -774 473 C ATOM 3496 CG PRO C 232 3.711 -1.165 -74.132 1.00 36.45 C ANISOU 3496 CG PRO C 232 4907 4964 3980 -352 -722 519 C ATOM 3497 CD PRO C 232 3.502 -2.479 -73.435 1.00 36.74 C ANISOU 3497 CD PRO C 232 4944 4980 4034 -532 -774 499 C ATOM 3498 N ARG C 233 7.010 -1.888 -76.352 1.00 35.41 N ANISOU 3498 N ARG C 233 5359 4442 3651 -235 -553 308 N ATOM 3499 CA ARG C 233 8.445 -1.595 -76.493 1.00 34.60 C ANISOU 3499 CA ARG C 233 5347 4256 3545 -124 -403 267 C ATOM 3500 C ARG C 233 8.995 -0.567 -75.494 1.00 33.01 C ANISOU 3500 C ARG C 233 5021 4046 3477 -40 -281 316 C ATOM 3501 O ARG C 233 10.171 -0.636 -75.141 1.00 32.32 O ANISOU 3501 O ARG C 233 4967 3891 3424 8 -168 279 O ATOM 3502 CB ARG C 233 8.752 -1.129 -77.928 1.00 35.43 C ANISOU 3502 CB ARG C 233 5565 4395 3501 -69 -394 277 C ATOM 3503 N ASN C 234 8.158 0.374 -75.047 1.00 32.78 N ANISOU 3503 N ASN C 234 4853 4089 3514 -16 -311 393 N ATOM 3504 CA ASN C 234 8.590 1.414 -74.097 1.00 31.80 C ANISOU 3504 CA ASN C 234 4641 3938 3505 67 -217 426 C ATOM 3505 C ASN C 234 9.035 0.835 -72.754 1.00 30.81 C ANISOU 3505 C ASN C 234 4461 3767 3477 40 -160 378 C ATOM 3506 O ASN C 234 8.246 0.201 -72.053 1.00 30.77 O ANISOU 3506 O ASN C 234 4376 3813 3503 -26 -217 374 O ATOM 3507 CB ASN C 234 7.478 2.446 -73.846 1.00 32.35 C ANISOU 3507 CB ASN C 234 4588 4090 3613 131 -275 500 C ATOM 3508 CG ASN C 234 7.330 3.451 -74.977 1.00 33.29 C ANISOU 3508 CG ASN C 234 4768 4218 3662 200 -309 572 C ATOM 3509 OD1 ASN C 234 8.183 3.560 -75.857 1.00 33.56 O ANISOU 3509 OD1 ASN C 234 4928 4201 3624 194 -266 578 O ATOM 3510 ND2 ASN C 234 6.232 4.193 -74.956 1.00 34.14 N ANISOU 3510 ND2 ASN C 234 4781 4407 3784 275 -388 635 N ATOM 3511 N ILE C 235 10.300 1.070 -72.410 1.00 30.02 N ANISOU 3511 N ILE C 235 4397 3591 3417 80 -51 355 N ATOM 3512 CA ILE C 235 10.883 0.582 -71.162 1.00 29.23 C ANISOU 3512 CA ILE C 235 4256 3449 3402 65 2 316 C ATOM 3513 C ILE C 235 11.989 1.529 -70.701 1.00 28.77 C ANISOU 3513 C ILE C 235 4182 3344 3404 121 102 329 C ATOM 3514 O ILE C 235 12.652 2.168 -71.525 1.00 28.84 O ANISOU 3514 O ILE C 235 4246 3339 3372 146 145 359 O ATOM 3515 CB ILE C 235 11.428 -0.862 -71.327 1.00 29.28 C ANISOU 3515 CB ILE C 235 4357 3399 3367 22 -3 249 C ATOM 3516 CG1 ILE C 235 11.706 -1.509 -69.966 1.00 28.68 C ANISOU 3516 CG1 ILE C 235 4234 3289 3376 -6 14 227 C ATOM 3517 CG2 ILE C 235 12.677 -0.902 -72.203 1.00 29.54 C ANISOU 3517 CG2 ILE C 235 4489 3400 3336 83 78 218 C ATOM 3518 CD1 ILE C 235 12.046 -2.982 -70.056 1.00 29.18 C ANISOU 3518 CD1 ILE C 235 4413 3270 3404 -42 -22 169 C ATOM 3519 N ILE C 236 12.155 1.631 -69.385 1.00 28.45 N ANISOU 3519 N ILE C 236 4069 3292 3450 122 129 315 N ATOM 3520 CA ILE C 236 13.304 2.296 -68.778 1.00 28.38 C ANISOU 3520 CA ILE C 236 4049 3235 3498 142 205 316 C ATOM 3521 C ILE C 236 14.097 1.202 -68.084 1.00 28.20 C ANISOU 3521 C ILE C 236 4017 3198 3499 119 237 271 C ATOM 3522 O ILE C 236 13.521 0.347 -67.413 1.00 28.32 O ANISOU 3522 O ILE C 236 4009 3225 3528 88 196 250 O ATOM 3523 CB ILE C 236 12.877 3.388 -67.777 1.00 28.32 C ANISOU 3523 CB ILE C 236 3985 3219 3558 177 196 327 C ATOM 3524 CG1 ILE C 236 12.243 4.565 -68.523 1.00 29.18 C ANISOU 3524 CG1 ILE C 236 4128 3313 3645 232 159 377 C ATOM 3525 CG2 ILE C 236 14.065 3.872 -66.945 1.00 28.11 C ANISOU 3525 CG2 ILE C 236 3953 3138 3588 165 251 317 C ATOM 3526 CD1 ILE C 236 11.373 5.449 -67.655 1.00 29.50 C ANISOU 3526 CD1 ILE C 236 4123 3358 3728 313 126 369 C ATOM 3527 N LEU C 237 15.412 1.226 -68.272 1.00 28.52 N ANISOU 3527 N LEU C 237 4073 3225 3540 133 306 270 N ATOM 3528 CA LEU C 237 16.314 0.257 -67.664 1.00 28.79 C ANISOU 3528 CA LEU C 237 4094 3251 3594 144 337 234 C ATOM 3529 C LEU C 237 17.624 0.970 -67.360 1.00 29.11 C ANISOU 3529 C LEU C 237 4077 3313 3671 147 407 261 C ATOM 3530 O LEU C 237 18.310 1.412 -68.279 1.00 29.62 O ANISOU 3530 O LEU C 237 4149 3414 3690 153 460 293 O ATOM 3531 CB LEU C 237 16.536 -0.925 -68.614 1.00 29.53 C ANISOU 3531 CB LEU C 237 4276 3335 3608 182 336 191 C ATOM 3532 CG LEU C 237 17.128 -2.203 -68.010 1.00 29.86 C ANISOU 3532 CG LEU C 237 4344 3336 3666 218 332 145 C ATOM 3533 CD1 LEU C 237 16.165 -2.842 -67.018 1.00 29.43 C ANISOU 3533 CD1 LEU C 237 4292 3236 3655 151 247 145 C ATOM 3534 CD2 LEU C 237 17.495 -3.186 -69.116 1.00 30.91 C ANISOU 3534 CD2 LEU C 237 4596 3446 3704 294 338 87 C ATOM 3535 N THR C 238 17.958 1.110 -66.078 1.00 28.92 N ANISOU 3535 N THR C 238 3990 3281 3716 127 402 256 N ATOM 3536 CA THR C 238 19.124 1.911 -65.685 1.00 29.53 C ANISOU 3536 CA THR C 238 4006 3384 3831 96 443 289 C ATOM 3537 C THR C 238 19.725 1.473 -64.353 1.00 28.98 C ANISOU 3537 C THR C 238 3872 3327 3812 91 432 270 C ATOM 3538 O THR C 238 19.014 1.006 -63.465 1.00 28.92 O ANISOU 3538 O THR C 238 3870 3295 3821 93 388 242 O ATOM 3539 CB THR C 238 18.773 3.419 -65.637 1.00 30.21 C ANISOU 3539 CB THR C 238 4113 3424 3941 45 420 325 C ATOM 3540 OG1 THR C 238 19.957 4.187 -65.389 1.00 31.67 O ANISOU 3540 OG1 THR C 238 4255 3623 4154 -23 444 367 O ATOM 3541 CG2 THR C 238 17.758 3.722 -64.556 1.00 29.95 C ANISOU 3541 CG2 THR C 238 4086 3348 3944 56 364 287 C ATOM 3542 N TRP C 239 21.042 1.635 -64.230 1.00 28.88 N ANISOU 3542 N TRP C 239 3785 3374 3813 77 471 299 N ATOM 3543 CA TRP C 239 21.772 1.262 -63.018 1.00 28.60 C ANISOU 3543 CA TRP C 239 3676 3371 3819 73 452 293 C ATOM 3544 C TRP C 239 21.717 2.365 -61.966 1.00 28.19 C ANISOU 3544 C TRP C 239 3613 3290 3809 -15 406 296 C ATOM 3545 O TRP C 239 21.846 3.547 -62.290 1.00 28.25 O ANISOU 3545 O TRP C 239 3639 3272 3824 -85 404 325 O ATOM 3546 CB TRP C 239 23.236 0.921 -63.337 1.00 29.44 C ANISOU 3546 CB TRP C 239 3682 3588 3915 106 507 327 C ATOM 3547 CG TRP C 239 23.397 -0.448 -63.902 1.00 29.83 C ANISOU 3547 CG TRP C 239 3758 3655 3923 240 536 294 C ATOM 3548 CD1 TRP C 239 23.577 -0.786 -65.211 1.00 30.47 C ANISOU 3548 CD1 TRP C 239 3869 3776 3934 316 598 286 C ATOM 3549 CD2 TRP C 239 23.373 -1.673 -63.167 1.00 29.78 C ANISOU 3549 CD2 TRP C 239 3777 3608 3929 320 492 260 C ATOM 3550 NE1 TRP C 239 23.673 -2.150 -65.337 1.00 31.04 N ANISOU 3550 NE1 TRP C 239 3997 3820 3975 452 593 232 N ATOM 3551 CE2 TRP C 239 23.550 -2.720 -64.096 1.00 30.57 C ANISOU 3551 CE2 TRP C 239 3941 3701 3973 452 523 223 C ATOM 3552 CE3 TRP C 239 23.220 -1.988 -61.810 1.00 29.29 C ANISOU 3552 CE3 TRP C 239 3708 3512 3911 294 425 261 C ATOM 3553 CZ2 TRP C 239 23.577 -4.064 -63.713 1.00 30.92 C ANISOU 3553 CZ2 TRP C 239 4059 3673 4015 558 477 187 C ATOM 3554 CZ3 TRP C 239 23.250 -3.325 -61.426 1.00 29.74 C ANISOU 3554 CZ3 TRP C 239 3819 3518 3963 385 385 244 C ATOM 3555 CH2 TRP C 239 23.429 -4.346 -62.377 1.00 30.48 C ANISOU 3555 CH2 TRP C 239 3993 3575 4013 516 405 208 C ATOM 3556 N ARG C 240 21.528 1.950 -60.712 1.00 27.66 N ANISOU 3556 N ARG C 240 3532 3219 3757 -11 362 267 N ATOM 3557 CA ARG C 240 21.599 2.829 -59.549 1.00 27.75 C ANISOU 3557 CA ARG C 240 3542 3216 3788 -77 313 250 C ATOM 3558 C ARG C 240 22.786 2.435 -58.685 1.00 28.16 C ANISOU 3558 C ARG C 240 3502 3343 3853 -101 291 269 C ATOM 3559 O ARG C 240 23.158 1.262 -58.637 1.00 28.12 O ANISOU 3559 O ARG C 240 3454 3385 3844 -33 301 283 O ATOM 3560 CB ARG C 240 20.322 2.731 -58.713 1.00 27.30 C ANISOU 3560 CB ARG C 240 3536 3128 3710 -49 282 201 C ATOM 3561 CG ARG C 240 19.072 3.217 -59.423 1.00 27.06 C ANISOU 3561 CG ARG C 240 3570 3049 3664 -14 290 185 C ATOM 3562 CD ARG C 240 17.862 3.232 -58.505 1.00 27.00 C ANISOU 3562 CD ARG C 240 3574 3060 3624 20 269 144 C ATOM 3563 NE ARG C 240 16.733 3.918 -59.145 1.00 27.21 N ANISOU 3563 NE ARG C 240 3641 3060 3637 71 270 132 N ATOM 3564 CZ ARG C 240 16.056 4.969 -58.663 1.00 27.63 C ANISOU 3564 CZ ARG C 240 3734 3091 3674 122 252 86 C ATOM 3565 NH1 ARG C 240 16.333 5.518 -57.478 1.00 27.92 N ANISOU 3565 NH1 ARG C 240 3792 3122 3695 121 230 34 N ATOM 3566 NH2 ARG C 240 15.057 5.473 -59.385 1.00 27.85 N ANISOU 3566 NH2 ARG C 240 3786 3104 3691 191 249 88 N ATOM 3567 N GLN C 241 23.375 3.422 -58.016 1.00 28.79 N ANISOU 3567 N GLN C 241 3566 3426 3947 -196 246 272 N ATOM 3568 CA GLN C 241 24.413 3.198 -57.009 1.00 29.57 C ANISOU 3568 CA GLN C 241 3576 3608 4051 -237 199 289 C ATOM 3569 C GLN C 241 23.985 3.899 -55.726 1.00 29.44 C ANISOU 3569 C GLN C 241 3630 3544 4011 -292 125 231 C ATOM 3570 O GLN C 241 23.613 5.076 -55.759 1.00 29.70 O ANISOU 3570 O GLN C 241 3755 3486 4042 -348 99 195 O ATOM 3571 CB GLN C 241 25.766 3.738 -57.475 1.00 30.96 C ANISOU 3571 CB GLN C 241 3645 3870 4251 -331 201 358 C ATOM 3572 CG GLN C 241 26.913 3.425 -56.517 1.00 32.24 C ANISOU 3572 CG GLN C 241 3680 4153 4416 -368 145 390 C ATOM 3573 CD GLN C 241 28.255 3.952 -56.990 1.00 33.86 C ANISOU 3573 CD GLN C 241 3738 4487 4639 -478 147 476 C ATOM 3574 OE1 GLN C 241 28.363 4.567 -58.047 1.00 34.50 O ANISOU 3574 OE1 GLN C 241 3820 4564 4725 -538 197 519 O ATOM 3575 NE2 GLN C 241 29.290 3.706 -56.199 1.00 35.24 N ANISOU 3575 NE2 GLN C 241 3776 4797 4816 -515 89 515 N ATOM 3576 N ASP C 242 24.040 3.173 -54.610 1.00 29.17 N ANISOU 3576 N ASP C 242 3569 3566 3948 -264 88 220 N ATOM 3577 CA ASP C 242 23.566 3.660 -53.307 1.00 29.31 C ANISOU 3577 CA ASP C 242 3657 3567 3911 -293 27 156 C ATOM 3578 C ASP C 242 22.103 4.139 -53.358 1.00 28.61 C ANISOU 3578 C ASP C 242 3679 3402 3789 -235 57 88 C ATOM 3579 O ASP C 242 21.736 5.104 -52.691 1.00 28.97 O ANISOU 3579 O ASP C 242 3812 3402 3794 -250 18 15 O ATOM 3580 CB ASP C 242 24.492 4.767 -52.773 1.00 30.58 C ANISOU 3580 CB ASP C 242 3824 3723 4072 -421 -55 141 C ATOM 3581 CG ASP C 242 25.957 4.367 -52.799 1.00 31.53 C ANISOU 3581 CG ASP C 242 3794 3961 4225 -484 -85 224 C ATOM 3582 OD1 ASP C 242 26.290 3.255 -52.337 1.00 31.36 O ANISOU 3582 OD1 ASP C 242 3689 4034 4191 -417 -89 261 O ATOM 3583 OD2 ASP C 242 26.782 5.165 -53.289 1.00 32.63 O ANISOU 3583 OD2 ASP C 242 3893 4107 4399 -601 -109 262 O ATOM 3584 N GLY C 243 21.284 3.454 -54.158 1.00 27.82 N ANISOU 3584 N GLY C 243 3576 3294 3700 -161 119 109 N ATOM 3585 CA GLY C 243 19.873 3.801 -54.341 1.00 27.67 C ANISOU 3585 CA GLY C 243 3621 3241 3651 -98 149 64 C ATOM 3586 C GLY C 243 19.530 4.905 -55.338 1.00 27.80 C ANISOU 3586 C GLY C 243 3705 3159 3697 -86 161 45 C ATOM 3587 O GLY C 243 18.348 5.195 -55.531 1.00 27.67 O ANISOU 3587 O GLY C 243 3729 3129 3657 -11 180 13 O ATOM 3588 N VAL C 244 20.538 5.506 -55.980 1.00 28.30 N ANISOU 3588 N VAL C 244 3774 3170 3808 -162 146 79 N ATOM 3589 CA VAL C 244 20.342 6.660 -56.874 1.00 28.92 C ANISOU 3589 CA VAL C 244 3940 3137 3910 -176 139 80 C ATOM 3590 C VAL C 244 20.846 6.343 -58.281 1.00 28.87 C ANISOU 3590 C VAL C 244 3885 3147 3938 -203 188 164 C ATOM 3591 O VAL C 244 21.923 5.763 -58.441 1.00 28.88 O ANISOU 3591 O VAL C 244 3791 3228 3956 -254 206 216 O ATOM 3592 CB VAL C 244 21.081 7.918 -56.352 1.00 30.21 C ANISOU 3592 CB VAL C 244 4188 3209 4081 -279 60 56 C ATOM 3593 CG1 VAL C 244 20.766 9.139 -57.215 1.00 31.08 C ANISOU 3593 CG1 VAL C 244 4429 3169 4212 -291 35 65 C ATOM 3594 CG2 VAL C 244 20.719 8.185 -54.896 1.00 30.69 C ANISOU 3594 CG2 VAL C 244 4309 3267 4084 -245 9 -43 C ATOM 3595 N SER C 245 20.070 6.744 -59.290 1.00 28.99 N ANISOU 3595 N SER C 245 3963 3101 3952 -157 208 176 N ATOM 3596 CA SER C 245 20.421 6.540 -60.701 1.00 29.16 C ANISOU 3596 CA SER C 245 3959 3143 3979 -175 257 251 C ATOM 3597 C SER C 245 21.799 7.100 -61.046 1.00 30.34 C ANISOU 3597 C SER C 245 4074 3307 4148 -306 255 323 C ATOM 3598 O SER C 245 22.157 8.200 -60.622 1.00 31.06 O ANISOU 3598 O SER C 245 4231 3313 4257 -402 191 327 O ATOM 3599 CB SER C 245 19.376 7.195 -61.612 1.00 29.34 C ANISOU 3599 CB SER C 245 4076 3083 3987 -120 253 259 C ATOM 3600 OG SER C 245 18.109 6.579 -61.468 1.00 28.78 O ANISOU 3600 OG SER C 245 3998 3046 3893 -11 259 213 O ATOM 3601 N LEU C 246 22.571 6.325 -61.799 1.00 30.74 N ANISOU 3601 N LEU C 246 4021 3472 4187 -309 320 381 N ATOM 3602 CA LEU C 246 23.854 6.790 -62.315 1.00 32.20 C ANISOU 3602 CA LEU C 246 4131 3728 4374 -432 338 472 C ATOM 3603 C LEU C 246 23.634 7.647 -63.546 1.00 33.22 C ANISOU 3603 C LEU C 246 4342 3799 4480 -482 354 543 C ATOM 3604 O LEU C 246 22.571 7.600 -64.164 1.00 32.57 O ANISOU 3604 O LEU C 246 4349 3652 4376 -391 364 519 O ATOM 3605 CB LEU C 246 24.746 5.607 -62.684 1.00 32.35 C ANISOU 3605 CB LEU C 246 3998 3922 4372 -375 416 502 C ATOM 3606 CG LEU C 246 25.211 4.728 -61.526 1.00 32.19 C ANISOU 3606 CG LEU C 246 3887 3971 4373 -328 392 462 C ATOM 3607 CD1 LEU C 246 25.933 3.495 -62.054 1.00 32.61 C ANISOU 3607 CD1 LEU C 246 3822 4171 4399 -214 467 481 C ATOM 3608 CD2 LEU C 246 26.107 5.516 -60.578 1.00 33.13 C ANISOU 3608 CD2 LEU C 246 3949 4116 4523 -475 319 491 C ATOM 3609 N SER C 247 24.652 8.427 -63.898 1.00 35.16 N ANISOU 3609 N SER C 247 4550 4080 4727 -642 349 643 N ATOM 3610 CA SER C 247 24.668 9.159 -65.162 1.00 36.41 C ANISOU 3610 CA SER C 247 4769 4217 4847 -715 373 746 C ATOM 3611 C SER C 247 24.656 8.166 -66.327 1.00 36.31 C ANISOU 3611 C SER C 247 4680 4353 4762 -601 487 765 C ATOM 3612 O SER C 247 25.280 7.103 -66.245 1.00 35.92 O ANISOU 3612 O SER C 247 4491 4461 4694 -527 554 743 O ATOM 3613 CB SER C 247 25.913 10.048 -65.246 1.00 38.45 C ANISOU 3613 CB SER C 247 4970 4528 5112 -943 348 873 C ATOM 3614 OG SER C 247 26.015 10.688 -66.510 1.00 40.18 O ANISOU 3614 OG SER C 247 5236 4753 5279 -1032 379 998 O ATOM 3615 N HIS C 248 23.943 8.513 -67.399 1.00 36.83 N ANISOU 3615 N HIS C 248 4854 4362 4779 -574 499 801 N ATOM 3616 CA HIS C 248 23.949 7.706 -68.639 1.00 37.15 C ANISOU 3616 CA HIS C 248 4853 4539 4723 -482 599 820 C ATOM 3617 C HIS C 248 25.337 7.581 -69.286 1.00 38.67 C ANISOU 3617 C HIS C 248 4891 4953 4851 -558 698 924 C ATOM 3618 O HIS C 248 25.604 6.596 -69.978 1.00 38.92 O ANISOU 3618 O HIS C 248 4850 5138 4801 -437 794 900 O ATOM 3619 CB HIS C 248 22.930 8.225 -69.675 1.00 37.43 C ANISOU 3619 CB HIS C 248 5038 4479 4705 -455 577 854 C ATOM 3620 CG HIS C 248 23.127 9.656 -70.068 1.00 38.90 C ANISOU 3620 CG HIS C 248 5315 4573 4891 -616 527 984 C ATOM 3621 ND1 HIS C 248 22.369 10.676 -69.537 1.00 39.12 N ANISOU 3621 ND1 HIS C 248 5497 4380 4986 -638 411 973 N ATOM 3622 CD2 HIS C 248 23.985 10.239 -70.938 1.00 40.77 C ANISOU 3622 CD2 HIS C 248 5523 4904 5061 -762 571 1134 C ATOM 3623 CE1 HIS C 248 22.753 11.826 -70.058 1.00 40.84 C ANISOU 3623 CE1 HIS C 248 5804 4526 5189 -794 371 1109 C ATOM 3624 NE2 HIS C 248 23.731 11.589 -70.911 1.00 41.91 N ANISOU 3624 NE2 HIS C 248 5823 4857 5243 -889 467 1219 N ATOM 3625 N ASP C 249 26.209 8.564 -69.052 1.00 39.96 N ANISOU 3625 N ASP C 249 5004 5138 5042 -756 670 1036 N ATOM 3626 CA ASP C 249 27.593 8.514 -69.545 1.00 41.89 C ANISOU 3626 CA ASP C 249 5054 5637 5224 -854 763 1155 C ATOM 3627 C ASP C 249 28.472 7.444 -68.876 1.00 41.71 C ANISOU 3627 C ASP C 249 4827 5803 5218 -755 818 1098 C ATOM 3628 O ASP C 249 29.529 7.109 -69.410 1.00 43.21 O ANISOU 3628 O ASP C 249 4829 6254 5336 -756 922 1175 O ATOM 3629 CB ASP C 249 28.265 9.890 -69.422 1.00 43.89 C ANISOU 3629 CB ASP C 249 5311 5859 5507 -1136 695 1309 C ATOM 3630 CG ASP C 249 27.697 10.916 -70.399 1.00 45.02 C ANISOU 3630 CG ASP C 249 5635 5867 5602 -1238 663 1416 C ATOM 3631 OD1 ASP C 249 27.341 10.545 -71.540 1.00 45.14 O ANISOU 3631 OD1 ASP C 249 5675 5965 5513 -1136 748 1435 O ATOM 3632 OD2 ASP C 249 27.623 12.106 -70.027 1.00 46.30 O ANISOU 3632 OD2 ASP C 249 5933 5836 5825 -1421 542 1482 O ATOM 3633 N THR C 250 28.047 6.923 -67.722 1.00 40.05 N ANISOU 3633 N THR C 250 4647 5478 5092 -663 748 974 N ATOM 3634 CA THR C 250 28.716 5.784 -67.078 1.00 40.06 C ANISOU 3634 CA THR C 250 4490 5623 5106 -532 784 913 C ATOM 3635 C THR C 250 28.097 4.424 -67.453 1.00 39.16 C ANISOU 3635 C THR C 250 4431 5501 4948 -280 839 795 C ATOM 3636 O THR C 250 28.455 3.406 -66.856 1.00 39.22 O ANISOU 3636 O THR C 250 4360 5567 4973 -145 846 731 O ATOM 3637 CB THR C 250 28.713 5.930 -65.537 1.00 39.19 C ANISOU 3637 CB THR C 250 4382 5409 5099 -588 668 861 C ATOM 3638 OG1 THR C 250 27.379 5.798 -65.037 1.00 37.31 O ANISOU 3638 OG1 THR C 250 4330 4948 4899 -506 602 748 O ATOM 3639 CG2 THR C 250 29.279 7.282 -65.117 1.00 40.46 C ANISOU 3639 CG2 THR C 250 4531 5542 5300 -851 584 960 C ATOM 3640 N GLN C 251 27.184 4.401 -68.432 1.00 38.91 N ANISOU 3640 N GLN C 251 4544 5386 4854 -224 863 770 N ATOM 3641 CA GLN C 251 26.476 3.176 -68.828 1.00 38.10 C ANISOU 3641 CA GLN C 251 4531 5240 4704 -21 887 655 C ATOM 3642 C GLN C 251 26.407 3.017 -70.349 1.00 39.33 C ANISOU 3642 C GLN C 251 4732 5488 4724 43 977 674 C ATOM 3643 O GLN C 251 26.598 3.982 -71.092 1.00 39.93 O ANISOU 3643 O GLN C 251 4802 5621 4748 -82 1009 784 O ATOM 3644 CB GLN C 251 25.051 3.180 -68.273 1.00 36.31 C ANISOU 3644 CB GLN C 251 4471 4787 4539 -15 785 576 C ATOM 3645 CG GLN C 251 24.937 3.465 -66.785 1.00 35.47 C ANISOU 3645 CG GLN C 251 4349 4586 4542 -80 696 552 C ATOM 3646 CD GLN C 251 23.498 3.553 -66.332 1.00 34.14 C ANISOU 3646 CD GLN C 251 4321 4241 4411 -65 615 485 C ATOM 3647 OE1 GLN C 251 22.778 2.552 -66.320 1.00 33.35 O ANISOU 3647 OE1 GLN C 251 4277 4100 4297 38 603 413 O ATOM 3648 NE2 GLN C 251 23.066 4.752 -65.955 1.00 33.92 N ANISOU 3648 NE2 GLN C 251 4352 4109 4425 -169 554 510 N ATOM 3649 N GLN C 252 26.128 1.788 -70.789 1.00 39.48 N ANISOU 3649 N GLN C 252 4814 5510 4676 232 1008 569 N ATOM 3650 CA GLN C 252 25.898 1.468 -72.202 1.00 40.75 C ANISOU 3650 CA GLN C 252 5059 5736 4688 320 1077 550 C ATOM 3651 C GLN C 252 24.585 0.695 -72.344 1.00 39.99 C ANISOU 3651 C GLN C 252 5159 5453 4583 404 995 432 C ATOM 3652 O GLN C 252 24.311 -0.207 -71.554 1.00 39.01 O ANISOU 3652 O GLN C 252 5072 5227 4523 484 937 343 O ATOM 3653 CB GLN C 252 27.052 0.638 -72.764 1.00 42.52 C ANISOU 3653 CB GLN C 252 5169 6187 4802 488 1204 528 C ATOM 3654 N TRP C 253 23.793 1.057 -73.355 1.00 40.68 N ANISOU 3654 N TRP C 253 5367 5507 4584 372 982 446 N ATOM 3655 CA TRP C 253 22.466 0.485 -73.600 1.00 40.32 C ANISOU 3655 CA TRP C 253 5493 5308 4520 410 888 357 C ATOM 3656 C TRP C 253 22.424 -0.214 -74.947 1.00 41.43 C ANISOU 3656 C TRP C 253 5740 5519 4482 523 934 296 C ATOM 3657 O TRP C 253 22.914 0.326 -75.937 1.00 42.53 O ANISOU 3657 O TRP C 253 5854 5806 4501 510 1021 367 O ATOM 3658 CB TRP C 253 21.403 1.589 -73.638 1.00 40.12 C ANISOU 3658 CB TRP C 253 5526 5179 4539 278 804 426 C ATOM 3659 CG TRP C 253 20.837 1.968 -72.326 1.00 39.46 C ANISOU 3659 CG TRP C 253 5417 4966 4608 210 718 424 C ATOM 3660 CD1 TRP C 253 19.752 1.412 -71.707 1.00 38.63 C ANISOU 3660 CD1 TRP C 253 5371 4747 4560 227 625 353 C ATOM 3661 CD2 TRP C 253 21.299 3.014 -71.469 1.00 39.56 C ANISOU 3661 CD2 TRP C 253 5344 4962 4722 108 713 498 C ATOM 3662 NE1 TRP C 253 19.516 2.043 -70.510 1.00 37.90 N ANISOU 3662 NE1 TRP C 253 5226 4587 4588 164 578 373 N ATOM 3663 CE2 TRP C 253 20.450 3.031 -70.337 1.00 38.47 C ANISOU 3663 CE2 TRP C 253 5226 4701 4691 95 624 451 C ATOM 3664 CE3 TRP C 253 22.354 3.933 -71.541 1.00 40.60 C ANISOU 3664 CE3 TRP C 253 5390 5179 4858 13 768 602 C ATOM 3665 CZ2 TRP C 253 20.623 3.935 -69.281 1.00 38.16 C ANISOU 3665 CZ2 TRP C 253 5142 4606 4750 15 589 484 C ATOM 3666 CZ3 TRP C 253 22.526 4.836 -70.491 1.00 40.42 C ANISOU 3666 CZ3 TRP C 253 5330 5081 4947 -95 716 642 C ATOM 3667 CH2 TRP C 253 21.663 4.826 -69.375 1.00 39.08 C ANISOU 3667 CH2 TRP C 253 5202 4774 4873 -80 627 572 C ATOM 3668 N GLY C 254 21.813 -1.396 -74.987 1.00 40.97 N ANISOU 3668 N GLY C 254 5816 5353 4397 620 868 170 N ATOM 3669 CA GLY C 254 21.433 -2.021 -76.250 1.00 42.35 C ANISOU 3669 CA GLY C 254 6149 5542 4398 703 865 93 C ATOM 3670 C GLY C 254 20.161 -1.384 -76.777 1.00 41.72 C ANISOU 3670 C GLY C 254 6160 5396 4296 581 767 137 C ATOM 3671 O GLY C 254 19.462 -0.681 -76.044 1.00 40.35 O ANISOU 3671 O GLY C 254 5941 5138 4253 465 692 200 O ATOM 3672 N ASP C 255 19.859 -1.620 -78.050 1.00 43.17 N ANISOU 3672 N ASP C 255 6473 5629 4303 622 766 101 N ATOM 3673 CA ASP C 255 18.560 -1.233 -78.611 1.00 43.31 C ANISOU 3673 CA ASP C 255 6588 5585 4282 526 647 129 C ATOM 3674 C ASP C 255 17.461 -2.148 -78.076 1.00 42.68 C ANISOU 3674 C ASP C 255 6604 5343 4270 498 496 36 C ATOM 3675 O ASP C 255 17.734 -3.245 -77.584 1.00 42.81 O ANISOU 3675 O ASP C 255 6672 5280 4314 569 482 -67 O ATOM 3676 CB ASP C 255 18.573 -1.291 -80.147 1.00 45.41 C ANISOU 3676 CB ASP C 255 6973 5964 4316 573 678 114 C ATOM 3677 CG ASP C 255 19.320 -0.128 -80.781 1.00 46.43 C ANISOU 3677 CG ASP C 255 7010 6263 4367 536 799 259 C ATOM 3678 OD1 ASP C 255 20.018 0.623 -80.063 1.00 46.18 O ANISOU 3678 OD1 ASP C 255 6824 6265 4457 481 868 358 O ATOM 3679 OD2 ASP C 255 19.204 0.036 -82.014 1.00 47.96 O ANISOU 3679 OD2 ASP C 255 7295 6561 4368 547 816 282 O ATOM 3680 N VAL C 256 16.220 -1.680 -78.165 1.00 42.22 N ANISOU 3680 N VAL C 256 6563 5241 4237 393 377 85 N ATOM 3681 CA VAL C 256 15.059 -2.508 -77.863 1.00 42.21 C ANISOU 3681 CA VAL C 256 6640 5129 4268 332 224 21 C ATOM 3682 C VAL C 256 14.711 -3.251 -79.152 1.00 44.35 C ANISOU 3682 C VAL C 256 7099 5408 4343 356 158 -65 C ATOM 3683 O VAL C 256 14.147 -2.663 -80.077 1.00 44.79 O ANISOU 3683 O VAL C 256 7188 5537 4295 317 115 -12 O ATOM 3684 CB VAL C 256 13.869 -1.665 -77.354 1.00 41.12 C ANISOU 3684 CB VAL C 256 6403 4983 4238 223 128 117 C ATOM 3685 CG1 VAL C 256 12.667 -2.552 -77.045 1.00 41.13 C ANISOU 3685 CG1 VAL C 256 6450 4916 4262 137 -27 70 C ATOM 3686 CG2 VAL C 256 14.282 -0.863 -76.125 1.00 39.56 C ANISOU 3686 CG2 VAL C 256 6049 4774 4209 217 196 184 C ATOM 3687 N LEU C 257 15.076 -4.533 -79.210 1.00 45.62 N ANISOU 3687 N LEU C 257 7402 5486 4446 429 142 -200 N ATOM 3688 CA LEU C 257 14.913 -5.350 -80.414 1.00 48.22 C ANISOU 3688 CA LEU C 257 7952 5801 4569 476 82 -315 C ATOM 3689 C LEU C 257 13.827 -6.415 -80.233 1.00 49.41 C ANISOU 3689 C LEU C 257 8251 5792 4731 364 -118 -393 C ATOM 3690 O LEU C 257 13.582 -6.855 -79.110 1.00 48.36 O ANISOU 3690 O LEU C 257 8072 5550 4754 300 -172 -385 O ATOM 3691 CB LEU C 257 16.236 -6.035 -80.760 1.00 49.58 C ANISOU 3691 CB LEU C 257 8211 5994 4633 676 214 -429 C ATOM 3692 CG LEU C 257 17.401 -5.122 -81.158 1.00 49.71 C ANISOU 3692 CG LEU C 257 8085 6212 4588 777 416 -353 C ATOM 3693 CD1 LEU C 257 18.692 -5.922 -81.246 1.00 51.04 C ANISOU 3693 CD1 LEU C 257 8294 6421 4677 994 546 -465 C ATOM 3694 CD2 LEU C 257 17.117 -4.416 -82.476 1.00 50.82 C ANISOU 3694 CD2 LEU C 257 8272 6496 4540 746 429 -299 C ATOM 3695 N PRO C 258 13.172 -6.837 -81.338 1.00 52.06 N ANISOU 3695 N PRO C 258 8770 6121 4891 322 -237 -460 N ATOM 3696 CA PRO C 258 12.241 -7.972 -81.241 1.00 53.66 C ANISOU 3696 CA PRO C 258 9143 6161 5084 195 -443 -541 C ATOM 3697 C PRO C 258 12.933 -9.292 -80.885 1.00 55.44 C ANISOU 3697 C PRO C 258 9564 6195 5306 298 -452 -688 C ATOM 3698 O PRO C 258 14.126 -9.457 -81.156 1.00 56.44 O ANISOU 3698 O PRO C 258 9743 6344 5359 512 -304 -768 O ATOM 3699 CB PRO C 258 11.637 -8.064 -82.651 1.00 55.48 C ANISOU 3699 CB PRO C 258 9544 6444 5092 154 -554 -593 C ATOM 3700 CG PRO C 258 11.861 -6.729 -83.265 1.00 54.78 C ANISOU 3700 CG PRO C 258 9307 6561 4946 206 -432 -479 C ATOM 3701 CD PRO C 258 13.138 -6.217 -82.676 1.00 53.33 C ANISOU 3701 CD PRO C 258 8979 6429 4855 353 -211 -442 C ATOM 3702 N ASP C 259 12.180 -10.211 -80.281 1.00 56.45 N ANISOU 3702 N ASP C 259 9793 6146 5509 147 -628 -711 N ATOM 3703 CA ASP C 259 12.657 -11.584 -80.024 1.00 58.50 C ANISOU 3703 CA ASP C 259 10304 6171 5751 225 -690 -851 C ATOM 3704 C ASP C 259 11.936 -12.642 -80.884 1.00 61.39 C ANISOU 3704 C ASP C 259 10998 6371 5955 123 -910 -980 C ATOM 3705 O ASP C 259 12.131 -13.841 -80.680 1.00 63.26 O ANISOU 3705 O ASP C 259 11492 6366 6179 152 -1012 -1095 O ATOM 3706 CB ASP C 259 12.576 -11.931 -78.523 1.00 57.44 C ANISOU 3706 CB ASP C 259 10070 5923 5833 136 -719 -772 C ATOM 3707 CG ASP C 259 11.181 -11.749 -77.933 1.00 56.93 C ANISOU 3707 CG ASP C 259 9874 5883 5873 -158 -870 -639 C ATOM 3708 OD1 ASP C 259 10.173 -11.956 -78.646 1.00 58.14 O ANISOU 3708 OD1 ASP C 259 10123 6038 5930 -326 -1036 -647 O ATOM 3709 OD2 ASP C 259 11.096 -11.395 -76.738 1.00 55.41 O ANISOU 3709 OD2 ASP C 259 9471 5730 5850 -218 -823 -523 O ATOM 3710 N GLY C 260 11.122 -12.193 -81.844 1.00 62.18 N ANISOU 3710 N GLY C 260 11106 6592 5929 5 -996 -960 N ATOM 3711 CA GLY C 260 10.397 -13.087 -82.750 1.00 64.71 C ANISOU 3711 CA GLY C 260 11732 6781 6074 -115 -1220 -1079 C ATOM 3712 C GLY C 260 9.167 -13.777 -82.173 1.00 65.25 C ANISOU 3712 C GLY C 260 11847 6709 6235 -432 -1473 -1020 C ATOM 3713 O GLY C 260 8.734 -14.800 -82.713 1.00 68.14 O ANISOU 3713 O GLY C 260 12526 6887 6478 -542 -1682 -1139 O ATOM 3714 N ASN C 261 8.608 -13.230 -81.089 1.00 62.72 N ANISOU 3714 N ASN C 261 11226 6486 6119 -585 -1459 -839 N ATOM 3715 CA ASN C 261 7.391 -13.766 -80.452 1.00 62.83 C ANISOU 3715 CA ASN C 261 11211 6436 6224 -908 -1677 -742 C ATOM 3716 C ASN C 261 6.367 -12.663 -80.098 1.00 60.43 C ANISOU 3716 C ASN C 261 10532 6411 6018 -1067 -1674 -544 C ATOM 3717 O ASN C 261 5.511 -12.858 -79.229 1.00 60.35 O ANISOU 3717 O ASN C 261 10378 6425 6127 -1293 -1776 -421 O ATOM 3718 CB ASN C 261 7.774 -14.571 -79.196 1.00 62.94 C ANISOU 3718 CB ASN C 261 11277 6246 6393 -929 -1678 -728 C ATOM 3719 CG ASN C 261 8.391 -15.924 -79.527 1.00 65.76 C ANISOU 3719 CG ASN C 261 12059 6276 6650 -841 -1780 -915 C ATOM 3720 OD1 ASN C 261 7.730 -16.958 -79.422 1.00 67.93 O ANISOU 3720 OD1 ASN C 261 12558 6340 6911 -1071 -2014 -931 O ATOM 3721 ND2 ASN C 261 9.659 -15.923 -79.927 1.00 65.96 N ANISOU 3721 ND2 ASN C 261 12200 6261 6602 -507 -1610 -1053 N ATOM 3722 N GLY C 262 6.436 -11.522 -80.789 1.00 58.38 N ANISOU 3722 N GLY C 262 10121 6364 5697 -943 -1563 -509 N ATOM 3723 CA GLY C 262 5.589 -10.363 -80.487 1.00 56.20 C ANISOU 3723 CA GLY C 262 9502 6342 5510 -1021 -1541 -332 C ATOM 3724 C GLY C 262 6.005 -9.547 -79.268 1.00 52.90 C ANISOU 3724 C GLY C 262 8809 6003 5286 -917 -1349 -228 C ATOM 3725 O GLY C 262 5.249 -8.683 -78.814 1.00 52.01 O ANISOU 3725 O GLY C 262 8423 6077 5263 -974 -1340 -89 O ATOM 3726 N THR C 263 7.208 -9.803 -78.751 1.00 50.87 N ANISOU 3726 N THR C 263 8630 5614 5086 -751 -1200 -298 N ATOM 3727 CA THR C 263 7.729 -9.135 -77.558 1.00 47.83 C ANISOU 3727 CA THR C 263 8021 5280 4872 -658 -1029 -217 C ATOM 3728 C THR C 263 9.129 -8.587 -77.850 1.00 46.24 C ANISOU 3728 C THR C 263 7842 5082 4646 -402 -822 -277 C ATOM 3729 O THR C 263 9.671 -8.808 -78.937 1.00 46.99 O ANISOU 3729 O THR C 263 8120 5147 4585 -293 -804 -381 O ATOM 3730 CB THR C 263 7.758 -10.098 -76.349 1.00 47.59 C ANISOU 3730 CB THR C 263 8025 5099 4958 -756 -1076 -208 C ATOM 3731 OG1 THR C 263 8.390 -11.328 -76.720 1.00 49.03 O ANISOU 3731 OG1 THR C 263 8526 5046 5060 -713 -1139 -350 O ATOM 3732 CG2 THR C 263 6.349 -10.394 -75.872 1.00 48.37 C ANISOU 3732 CG2 THR C 263 8013 5266 5100 -1032 -1249 -98 C ATOM 3733 N TYR C 264 9.695 -7.860 -76.886 1.00 43.89 N ANISOU 3733 N TYR C 264 7350 4838 4489 -316 -670 -208 N ATOM 3734 CA TYR C 264 10.979 -7.176 -77.058 1.00 42.80 C ANISOU 3734 CA TYR C 264 7175 4744 4344 -112 -476 -228 C ATOM 3735 C TYR C 264 11.999 -7.544 -75.984 1.00 41.64 C ANISOU 3735 C TYR C 264 7002 4510 4309 -19 -373 -250 C ATOM 3736 O TYR C 264 11.669 -8.176 -74.976 1.00 41.09 O ANISOU 3736 O TYR C 264 6921 4351 4339 -111 -442 -231 O ATOM 3737 CB TYR C 264 10.761 -5.661 -77.066 1.00 41.62 C ANISOU 3737 CB TYR C 264 6811 4763 4241 -96 -395 -108 C ATOM 3738 CG TYR C 264 9.899 -5.192 -78.212 1.00 42.66 C ANISOU 3738 CG TYR C 264 6966 4994 4249 -149 -486 -75 C ATOM 3739 CD1 TYR C 264 8.514 -5.110 -78.080 1.00 43.10 C ANISOU 3739 CD1 TYR C 264 6930 5113 4331 -299 -636 -3 C ATOM 3740 CD2 TYR C 264 10.467 -4.846 -79.437 1.00 43.62 C ANISOU 3740 CD2 TYR C 264 7189 5171 4215 -50 -425 -105 C ATOM 3741 CE1 TYR C 264 7.718 -4.685 -79.135 1.00 44.28 C ANISOU 3741 CE1 TYR C 264 7092 5369 4365 -340 -734 35 C ATOM 3742 CE2 TYR C 264 9.679 -4.419 -80.498 1.00 44.80 C ANISOU 3742 CE2 TYR C 264 7369 5416 4238 -98 -520 -66 C ATOM 3743 CZ TYR C 264 8.307 -4.341 -80.342 1.00 45.08 C ANISOU 3743 CZ TYR C 264 7314 5502 4311 -240 -681 3 C ATOM 3744 OH TYR C 264 7.526 -3.922 -81.388 1.00 46.49 O ANISOU 3744 OH TYR C 264 7512 5788 4362 -281 -788 50 O ATOM 3745 N GLN C 265 13.243 -7.137 -76.225 1.00 41.12 N ANISOU 3745 N GLN C 265 6916 4492 4218 157 -212 -278 N ATOM 3746 CA GLN C 265 14.345 -7.361 -75.291 1.00 40.38 C ANISOU 3746 CA GLN C 265 6768 4354 4219 268 -105 -290 C ATOM 3747 C GLN C 265 15.400 -6.261 -75.399 1.00 39.10 C ANISOU 3747 C GLN C 265 6452 4339 4067 385 74 -240 C ATOM 3748 O GLN C 265 15.627 -5.714 -76.481 1.00 39.83 O ANISOU 3748 O GLN C 265 6561 4534 4038 435 133 -239 O ATOM 3749 CB GLN C 265 14.991 -8.719 -75.555 1.00 42.35 C ANISOU 3749 CB GLN C 265 7245 4455 4392 388 -134 -426 C ATOM 3750 CG GLN C 265 15.296 -8.986 -77.025 1.00 44.65 C ANISOU 3750 CG GLN C 265 7716 4769 4481 504 -117 -535 C ATOM 3751 CD GLN C 265 16.572 -9.773 -77.230 1.00 46.45 C ANISOU 3751 CD GLN C 265 8067 4948 4635 745 -27 -656 C ATOM 3752 OE1 GLN C 265 16.552 -10.880 -77.766 1.00 48.82 O ANISOU 3752 OE1 GLN C 265 8629 5098 4822 818 -116 -793 O ATOM 3753 NE2 GLN C 265 17.693 -9.201 -76.803 1.00 45.93 N ANISOU 3753 NE2 GLN C 265 7814 5011 4627 875 143 -608 N ATOM 3754 N THR C 266 16.043 -5.952 -74.276 1.00 37.30 N ANISOU 3754 N THR C 266 6078 4124 3972 410 150 -191 N ATOM 3755 CA THR C 266 17.107 -4.943 -74.231 1.00 36.43 C ANISOU 3755 CA THR C 266 5814 4145 3884 486 303 -132 C ATOM 3756 C THR C 266 18.034 -5.175 -73.031 1.00 35.39 C ANISOU 3756 C THR C 266 5582 3995 3867 544 360 -125 C ATOM 3757 O THR C 266 17.822 -6.103 -72.244 1.00 35.34 O ANISOU 3757 O THR C 266 5638 3870 3922 535 282 -160 O ATOM 3758 CB THR C 266 16.523 -3.508 -74.196 1.00 35.51 C ANISOU 3758 CB THR C 266 5565 4111 3817 379 310 -18 C ATOM 3759 OG1 THR C 266 17.576 -2.552 -74.380 1.00 35.45 O ANISOU 3759 OG1 THR C 266 5450 4217 3805 424 442 45 O ATOM 3760 CG2 THR C 266 15.796 -3.225 -72.873 1.00 34.35 C ANISOU 3760 CG2 THR C 266 5314 3917 3821 279 247 34 C ATOM 3761 N TRP C 267 19.059 -4.335 -72.903 1.00 34.63 N ANISOU 3761 N TRP C 267 5338 4024 3797 589 483 -67 N ATOM 3762 CA TRP C 267 20.014 -4.444 -71.802 1.00 33.94 C ANISOU 3762 CA TRP C 267 5133 3952 3809 639 533 -49 C ATOM 3763 C TRP C 267 20.693 -3.118 -71.482 1.00 33.21 C ANISOU 3763 C TRP C 267 4855 3987 3774 584 621 53 C ATOM 3764 O TRP C 267 20.702 -2.208 -72.305 1.00 33.22 O ANISOU 3764 O TRP C 267 4831 4074 3715 541 669 108 O ATOM 3765 CB TRP C 267 21.076 -5.507 -72.117 1.00 35.37 C ANISOU 3765 CB TRP C 267 5373 4147 3918 833 588 -133 C ATOM 3766 CG TRP C 267 21.868 -5.248 -73.377 1.00 36.76 C ANISOU 3766 CG TRP C 267 5535 4485 3948 945 710 -148 C ATOM 3767 CD1 TRP C 267 21.605 -5.738 -74.623 1.00 38.13 C ANISOU 3767 CD1 TRP C 267 5873 4654 3960 1023 709 -231 C ATOM 3768 CD2 TRP C 267 23.052 -4.445 -73.503 1.00 37.28 C ANISOU 3768 CD2 TRP C 267 5407 4758 3998 980 851 -70 C ATOM 3769 NE1 TRP C 267 22.547 -5.287 -75.520 1.00 39.45 N ANISOU 3769 NE1 TRP C 267 5957 5029 4003 1118 854 -210 N ATOM 3770 CE2 TRP C 267 23.445 -4.490 -74.860 1.00 38.97 C ANISOU 3770 CE2 TRP C 267 5667 5106 4033 1083 943 -102 C ATOM 3771 CE3 TRP C 267 23.813 -3.681 -72.603 1.00 36.62 C ANISOU 3771 CE3 TRP C 267 5116 4771 4026 916 899 29 C ATOM 3772 CZ2 TRP C 267 24.571 -3.805 -75.340 1.00 40.15 C ANISOU 3772 CZ2 TRP C 267 5642 5502 4111 1118 1094 -22 C ATOM 3773 CZ3 TRP C 267 24.934 -2.998 -73.081 1.00 37.83 C ANISOU 3773 CZ3 TRP C 267 5102 5151 4119 934 1032 106 C ATOM 3774 CH2 TRP C 267 25.299 -3.066 -74.439 1.00 39.60 C ANISOU 3774 CH2 TRP C 267 5357 5523 4164 1031 1133 88 C ATOM 3775 N VAL C 268 21.253 -3.033 -70.276 1.00 32.62 N ANISOU 3775 N VAL C 268 4667 3916 3809 572 627 83 N ATOM 3776 CA VAL C 268 22.093 -1.905 -69.857 1.00 32.41 C ANISOU 3776 CA VAL C 268 4474 4002 3837 512 695 172 C ATOM 3777 C VAL C 268 23.262 -2.412 -69.008 1.00 33.02 C ANISOU 3777 C VAL C 268 4441 4140 3964 593 728 169 C ATOM 3778 O VAL C 268 23.081 -3.263 -68.132 1.00 32.69 O ANISOU 3778 O VAL C 268 4439 4004 3977 632 662 128 O ATOM 3779 CB VAL C 268 21.297 -0.810 -69.095 1.00 31.01 C ANISOU 3779 CB VAL C 268 4265 3763 3754 362 633 229 C ATOM 3780 CG1 VAL C 268 20.710 -1.331 -67.785 1.00 30.09 C ANISOU 3780 CG1 VAL C 268 4158 3548 3726 339 550 198 C ATOM 3781 CG2 VAL C 268 22.173 0.413 -68.838 1.00 31.14 C ANISOU 3781 CG2 VAL C 268 4155 3866 3810 280 684 317 C ATOM 3782 N ALA C 269 24.451 -1.875 -69.269 1.00 34.18 N ANISOU 3782 N ALA C 269 4442 4458 4087 607 824 229 N ATOM 3783 CA ALA C 269 25.667 -2.290 -68.576 1.00 35.25 C ANISOU 3783 CA ALA C 269 4435 4701 4258 694 859 241 C ATOM 3784 C ALA C 269 26.398 -1.113 -67.952 1.00 35.50 C ANISOU 3784 C ALA C 269 4286 4845 4356 545 875 348 C ATOM 3785 O ALA C 269 26.289 0.015 -68.424 1.00 35.41 O ANISOU 3785 O ALA C 269 4257 4867 4332 404 897 420 O ATOM 3786 CB ALA C 269 26.593 -3.024 -69.532 1.00 37.10 C ANISOU 3786 CB ALA C 269 4638 5085 4375 891 962 204 C ATOM 3787 N THR C 270 27.143 -1.395 -66.886 1.00 36.22 N ANISOU 3787 N THR C 270 4261 4984 4515 570 850 362 N ATOM 3788 CA THR C 270 28.040 -0.419 -66.263 1.00 36.96 C ANISOU 3788 CA THR C 270 4173 5208 4662 429 853 460 C ATOM 3789 C THR C 270 29.238 -1.137 -65.628 1.00 38.65 C ANISOU 3789 C THR C 270 4220 5573 4892 552 865 472 C ATOM 3790 O THR C 270 29.152 -2.323 -65.294 1.00 38.87 O ANISOU 3790 O THR C 270 4313 5532 4923 727 836 400 O ATOM 3791 CB THR C 270 27.289 0.468 -65.236 1.00 35.47 C ANISOU 3791 CB THR C 270 4045 4867 4565 247 748 473 C ATOM 3792 OG1 THR C 270 28.106 1.586 -64.865 1.00 35.94 O ANISOU 3792 OG1 THR C 270 3970 5028 4659 77 740 566 O ATOM 3793 CG2 THR C 270 26.886 -0.319 -63.986 1.00 34.47 C ANISOU 3793 CG2 THR C 270 3968 4629 4499 301 661 413 C ATOM 3794 N ARG C 271 30.351 -0.415 -65.495 1.00 40.34 N ANISOU 3794 N ARG C 271 4221 5994 5113 454 899 573 N ATOM 3795 CA ARG C 271 31.582 -0.947 -64.906 1.00 42.33 C ANISOU 3795 CA ARG C 271 4266 6440 5377 558 907 608 C ATOM 3796 C ARG C 271 31.638 -0.571 -63.429 1.00 42.28 C ANISOU 3796 C ARG C 271 4223 6371 5470 417 781 634 C ATOM 3797 O ARG C 271 31.315 0.564 -63.067 1.00 41.83 O ANISOU 3797 O ARG C 271 4197 6242 5455 186 724 673 O ATOM 3798 CB ARG C 271 32.809 -0.392 -65.633 1.00 44.34 C ANISOU 3798 CB ARG C 271 4273 7008 5567 515 1015 720 C ATOM 3799 N ILE C 272 32.042 -1.520 -62.581 1.00 43.11 N ANISOU 3799 N ILE C 272 4282 6495 5604 567 729 609 N ATOM 3800 CA ILE C 272 32.116 -1.301 -61.129 1.00 42.96 C ANISOU 3800 CA ILE C 272 4235 6431 5657 455 604 630 C ATOM 3801 C ILE C 272 33.409 -1.875 -60.544 1.00 44.89 C ANISOU 3801 C ILE C 272 4255 6895 5907 574 584 685 C ATOM 3802 O ILE C 272 33.868 -2.938 -60.965 1.00 45.85 O ANISOU 3802 O ILE C 272 4334 7096 5991 833 638 661 O ATOM 3803 CB ILE C 272 30.874 -1.877 -60.397 1.00 41.54 C ANISOU 3803 CB ILE C 272 4289 5986 5508 485 519 545 C ATOM 3804 CG1 ILE C 272 30.751 -3.398 -60.588 1.00 42.12 C ANISOU 3804 CG1 ILE C 272 4457 5989 5556 746 527 485 C ATOM 3805 CG2 ILE C 272 29.605 -1.189 -60.893 1.00 40.01 C ANISOU 3805 CG2 ILE C 272 4277 5614 5310 360 530 503 C ATOM 3806 CD1 ILE C 272 29.463 -3.982 -60.037 1.00 40.90 C ANISOU 3806 CD1 ILE C 272 4534 5585 5421 739 449 424 C ATOM 3807 N CYS C 273 33.988 -1.162 -59.580 1.00 45.41 N ANISOU 3807 N CYS C 273 4186 7057 6013 393 496 755 N ATOM 3808 CA CYS C 273 35.231 -1.588 -58.936 1.00 47.67 C ANISOU 3808 CA CYS C 273 4230 7577 6304 478 454 825 C ATOM 3809 C CYS C 273 34.981 -2.815 -58.066 1.00 46.72 C ANISOU 3809 C CYS C 273 4217 7335 6201 685 374 773 C ATOM 3810 O CYS C 273 33.932 -2.921 -57.428 1.00 44.79 O ANISOU 3810 O CYS C 273 4194 6847 5978 628 302 714 O ATOM 3811 CB CYS C 273 35.812 -0.461 -58.076 1.00 48.87 C ANISOU 3811 CB CYS C 273 4242 7838 6488 192 352 908 C ATOM 3812 SG CYS C 273 35.999 1.115 -58.944 1.00 50.76 S ANISOU 3812 SG CYS C 273 4416 8154 6715 -119 404 988 S ATOM 3813 N ARG C 274 35.945 -3.735 -58.051 1.00 48.09 N ANISOU 3813 N ARG C 274 4229 7685 6357 929 386 804 N ATOM 3814 CA ARG C 274 35.862 -4.945 -57.225 1.00 47.87 C ANISOU 3814 CA ARG C 274 4299 7545 6344 1139 294 778 C ATOM 3815 C ARG C 274 35.699 -4.571 -55.750 1.00 46.68 C ANISOU 3815 C ARG C 274 4172 7338 6228 950 141 814 C ATOM 3816 O ARG C 274 36.335 -3.630 -55.267 1.00 47.29 O ANISOU 3816 O ARG C 274 4067 7587 6314 745 92 882 O ATOM 3817 CB ARG C 274 37.105 -5.820 -57.416 1.00 50.51 C ANISOU 3817 CB ARG C 274 4419 8120 6653 1440 322 821 C ATOM 3818 N GLY C 275 34.822 -5.295 -55.056 1.00 44.97 N ANISOU 3818 N GLY C 275 4187 6881 6017 1002 64 769 N ATOM 3819 CA GLY C 275 34.477 -4.993 -53.664 1.00 43.86 C ANISOU 3819 CA GLY C 275 4109 6672 5882 831 -69 791 C ATOM 3820 C GLY C 275 33.375 -3.967 -53.410 1.00 41.47 C ANISOU 3820 C GLY C 275 3962 6216 5578 568 -76 738 C ATOM 3821 O GLY C 275 33.039 -3.719 -52.250 1.00 41.30 O ANISOU 3821 O GLY C 275 4005 6146 5540 444 -177 741 O ATOM 3822 N AGLU C 276 32.819 -3.385 -54.476 0.50 40.17 N ANISOU 3822 N AGLU C 276 3859 5984 5419 503 28 689 N ATOM 3823 N BGLU C 276 32.818 -3.376 -54.469 0.50 40.21 N ANISOU 3823 N BGLU C 276 3865 5990 5425 501 27 689 N ATOM 3824 CA AGLU C 276 31.749 -2.388 -54.378 0.50 38.18 C ANISOU 3824 CA AGLU C 276 3756 5586 5166 296 28 635 C ATOM 3825 CA BGLU C 276 31.730 -2.399 -54.348 0.50 38.24 C ANISOU 3825 CA BGLU C 276 3767 5590 5173 296 26 635 C ATOM 3826 C AGLU C 276 30.447 -2.845 -55.042 0.50 36.41 C ANISOU 3826 C AGLU C 276 3745 5154 4936 360 90 565 C ATOM 3827 C BGLU C 276 30.445 -2.847 -55.043 0.50 36.46 C ANISOU 3827 C BGLU C 276 3752 5160 4942 360 90 565 C ATOM 3828 O AGLU C 276 29.557 -2.023 -55.268 0.50 35.13 O ANISOU 3828 O AGLU C 276 3686 4891 4772 229 114 521 O ATOM 3829 O BGLU C 276 29.565 -2.021 -55.290 0.50 35.19 O ANISOU 3829 O BGLU C 276 3692 4900 4780 230 115 521 O ATOM 3830 CB AGLU C 276 32.206 -1.081 -55.029 0.50 38.57 C ANISOU 3830 CB AGLU C 276 3692 5736 5225 121 73 658 C ATOM 3831 CB BGLU C 276 32.170 -1.058 -54.931 0.50 38.67 C ANISOU 3831 CB BGLU C 276 3713 5742 5238 112 64 657 C ATOM 3832 CG AGLU C 276 33.538 -0.562 -54.510 0.50 40.41 C ANISOU 3832 CG AGLU C 276 3692 6198 5463 15 6 743 C ATOM 3833 CG BGLU C 276 33.278 -0.381 -54.145 0.50 40.24 C ANISOU 3833 CG BGLU C 276 3725 6125 5439 -36 -28 726 C ATOM 3834 CD AGLU C 276 33.483 -0.176 -53.046 0.50 40.44 C ANISOU 3834 CD AGLU C 276 3737 6175 5453 -125 -137 736 C ATOM 3835 CD BGLU C 276 33.550 1.025 -54.631 0.50 40.77 C ANISOU 3835 CD BGLU C 276 3739 6235 5516 -272 -17 753 C ATOM 3836 OE1AGLU C 276 32.391 0.190 -52.566 0.50 39.02 O ANISOU 3836 OE1AGLU C 276 3760 5807 5257 -202 -164 662 O ATOM 3837 OE1BGLU C 276 32.809 1.502 -55.516 0.50 39.82 O ANISOU 3837 OE1BGLU C 276 3741 5988 5398 -308 62 717 O ATOM 3838 OE2AGLU C 276 34.533 -0.234 -52.373 0.50 42.20 O ANISOU 3838 OE2AGLU C 276 3781 6583 5671 -150 -223 805 O ATOM 3839 OE2BGLU C 276 34.506 1.653 -54.129 0.50 42.49 O ANISOU 3839 OE2BGLU C 276 3799 6610 5735 -432 -99 820 O ATOM 3840 N GLU C 277 30.323 -4.144 -55.326 1.00 36.41 N ANISOU 3840 N GLU C 277 3820 5085 4929 560 101 555 N ATOM 3841 CA GLU C 277 29.194 -4.676 -56.111 1.00 35.24 C ANISOU 3841 CA GLU C 277 3866 4754 4770 615 149 494 C ATOM 3842 C GLU C 277 27.836 -4.564 -55.415 1.00 33.35 C ANISOU 3842 C GLU C 277 3791 4360 4520 487 100 468 C ATOM 3843 O GLU C 277 26.821 -4.354 -56.076 1.00 32.21 O ANISOU 3843 O GLU C 277 3756 4113 4368 440 144 423 O ATOM 3844 CB GLU C 277 29.425 -6.146 -56.494 1.00 36.44 C ANISOU 3844 CB GLU C 277 4093 4841 4912 853 144 486 C ATOM 3845 CG GLU C 277 30.600 -6.389 -57.431 1.00 38.18 C ANISOU 3845 CG GLU C 277 4168 5219 5120 1039 223 490 C ATOM 3846 CD GLU C 277 31.874 -6.777 -56.705 1.00 40.13 C ANISOU 3846 CD GLU C 277 4235 5635 5377 1164 170 558 C ATOM 3847 OE1 GLU C 277 32.179 -6.160 -55.661 1.00 40.03 O ANISOU 3847 OE1 GLU C 277 4115 5713 5382 1016 98 614 O ATOM 3848 OE2 GLU C 277 32.572 -7.698 -57.178 1.00 42.17 O ANISOU 3848 OE2 GLU C 277 4464 5940 5617 1421 193 551 O ATOM 3849 N GLN C 278 27.822 -4.694 -54.090 1.00 33.11 N ANISOU 3849 N GLN C 278 3764 4339 4477 435 11 502 N ATOM 3850 CA GLN C 278 26.568 -4.649 -53.325 1.00 31.89 C ANISOU 3850 CA GLN C 278 3742 4085 4291 326 -26 488 C ATOM 3851 C GLN C 278 25.902 -3.272 -53.248 1.00 30.73 C ANISOU 3851 C GLN C 278 3597 3945 4132 171 4 438 C ATOM 3852 O GLN C 278 24.749 -3.172 -52.835 1.00 29.61 O ANISOU 3852 O GLN C 278 3551 3743 3956 108 -1 415 O ATOM 3853 CB GLN C 278 26.772 -5.219 -51.925 1.00 32.45 C ANISOU 3853 CB GLN C 278 3820 4182 4327 323 -126 546 C ATOM 3854 CG GLN C 278 27.109 -6.695 -51.956 1.00 33.53 C ANISOU 3854 CG GLN C 278 4020 4248 4471 484 -174 598 C ATOM 3855 CD GLN C 278 27.141 -7.308 -50.579 1.00 34.33 C ANISOU 3855 CD GLN C 278 4161 4355 4529 468 -281 675 C ATOM 3856 OE1 GLN C 278 28.166 -7.285 -49.906 1.00 35.16 O ANISOU 3856 OE1 GLN C 278 4154 4578 4629 510 -343 721 O ATOM 3857 NE2 GLN C 278 26.015 -7.870 -50.157 1.00 34.14 N ANISOU 3857 NE2 GLN C 278 4288 4220 4464 398 -309 701 N ATOM 3858 N ARG C 279 26.618 -2.226 -53.653 1.00 30.86 N ANISOU 3858 N ARG C 279 3512 4040 4172 115 31 428 N ATOM 3859 CA ARG C 279 26.055 -0.878 -53.740 1.00 30.23 C ANISOU 3859 CA ARG C 279 3467 3931 4088 -13 50 378 C ATOM 3860 C ARG C 279 25.173 -0.633 -54.976 1.00 29.05 C ANISOU 3860 C ARG C 279 3396 3692 3952 2 128 343 C ATOM 3861 O ARG C 279 24.475 0.379 -55.027 1.00 28.63 O ANISOU 3861 O ARG C 279 3399 3587 3890 -74 136 303 O ATOM 3862 CB ARG C 279 27.185 0.156 -53.682 1.00 31.35 C ANISOU 3862 CB ARG C 279 3492 4170 4249 -113 24 399 C ATOM 3863 CG ARG C 279 27.965 0.119 -52.374 1.00 32.56 C ANISOU 3863 CG ARG C 279 3573 4421 4377 -159 -76 427 C ATOM 3864 CD ARG C 279 29.257 0.908 -52.461 1.00 34.10 C ANISOU 3864 CD ARG C 279 3618 4743 4596 -265 -111 471 C ATOM 3865 NE ARG C 279 29.018 2.334 -52.663 1.00 34.42 N ANISOU 3865 NE ARG C 279 3723 4714 4639 -427 -121 432 N ATOM 3866 CZ ARG C 279 29.973 3.248 -52.845 1.00 35.78 C ANISOU 3866 CZ ARG C 279 3801 4963 4831 -578 -161 475 C ATOM 3867 NH1 ARG C 279 31.261 2.906 -52.847 1.00 37.10 N ANISOU 3867 NH1 ARG C 279 3762 5321 5013 -587 -184 563 N ATOM 3868 NH2 ARG C 279 29.637 4.521 -53.023 1.00 35.91 N ANISOU 3868 NH2 ARG C 279 3928 4867 4850 -723 -185 438 N ATOM 3869 N PHE C 280 25.186 -1.550 -55.949 1.00 28.82 N ANISOU 3869 N PHE C 280 3380 3638 3933 110 175 355 N ATOM 3870 CA PHE C 280 24.516 -1.344 -57.237 1.00 28.32 C ANISOU 3870 CA PHE C 280 3380 3511 3869 125 242 327 C ATOM 3871 C PHE C 280 23.210 -2.127 -57.388 1.00 27.90 C ANISOU 3871 C PHE C 280 3452 3354 3794 154 234 303 C ATOM 3872 O PHE C 280 23.100 -3.282 -56.954 1.00 27.70 O ANISOU 3872 O PHE C 280 3474 3293 3759 207 194 319 O ATOM 3873 CB PHE C 280 25.472 -1.675 -58.389 1.00 29.05 C ANISOU 3873 CB PHE C 280 3403 3669 3965 216 305 347 C ATOM 3874 CG PHE C 280 26.629 -0.724 -58.492 1.00 29.87 C ANISOU 3874 CG PHE C 280 3363 3903 4084 145 324 391 C ATOM 3875 CD1 PHE C 280 27.717 -0.853 -57.645 1.00 30.87 C ANISOU 3875 CD1 PHE C 280 3359 4146 4224 143 279 433 C ATOM 3876 CD2 PHE C 280 26.622 0.318 -59.414 1.00 29.92 C ANISOU 3876 CD2 PHE C 280 3361 3920 4087 61 375 404 C ATOM 3877 CE1 PHE C 280 28.790 0.026 -57.718 1.00 31.96 C ANISOU 3877 CE1 PHE C 280 3347 4423 4374 43 282 488 C ATOM 3878 CE2 PHE C 280 27.693 1.200 -59.495 1.00 31.01 C ANISOU 3878 CE2 PHE C 280 3368 4179 4235 -45 381 466 C ATOM 3879 CZ PHE C 280 28.776 1.056 -58.644 1.00 32.00 C ANISOU 3879 CZ PHE C 280 3350 4434 4376 -63 334 508 C ATOM 3880 N THR C 281 22.236 -1.476 -58.021 1.00 27.48 N ANISOU 3880 N THR C 281 3453 3255 3731 111 262 274 N ATOM 3881 CA THR C 281 20.903 -2.028 -58.242 1.00 27.25 C ANISOU 3881 CA THR C 281 3516 3159 3678 108 250 260 C ATOM 3882 C THR C 281 20.455 -1.670 -59.656 1.00 27.41 C ANISOU 3882 C THR C 281 3576 3148 3689 121 293 241 C ATOM 3883 O THR C 281 20.492 -0.497 -60.026 1.00 26.86 O ANISOU 3883 O THR C 281 3484 3094 3628 87 321 237 O ATOM 3884 CB THR C 281 19.877 -1.412 -57.261 1.00 26.71 C ANISOU 3884 CB THR C 281 3451 3108 3588 38 226 249 C ATOM 3885 OG1 THR C 281 20.392 -1.437 -55.923 1.00 26.78 O ANISOU 3885 OG1 THR C 281 3422 3167 3588 15 189 262 O ATOM 3886 CG2 THR C 281 18.540 -2.155 -57.322 1.00 26.41 C ANISOU 3886 CG2 THR C 281 3467 3048 3518 16 206 261 C ATOM 3887 N CYS C 282 20.035 -2.665 -60.439 1.00 28.37 N ANISOU 3887 N CYS C 282 3776 3215 3787 163 286 232 N ATOM 3888 CA CYS C 282 19.380 -2.391 -61.721 1.00 28.86 C ANISOU 3888 CA CYS C 282 3891 3254 3822 164 309 213 C ATOM 3889 C CYS C 282 17.939 -1.973 -61.455 1.00 28.37 C ANISOU 3889 C CYS C 282 3840 3190 3749 93 276 216 C ATOM 3890 O CYS C 282 17.229 -2.654 -60.719 1.00 28.15 O ANISOU 3890 O CYS C 282 3826 3157 3713 52 229 231 O ATOM 3891 CB CYS C 282 19.397 -3.612 -62.641 1.00 30.36 C ANISOU 3891 CB CYS C 282 4181 3382 3973 230 296 189 C ATOM 3892 SG CYS C 282 18.505 -3.347 -64.198 1.00 31.67 S ANISOU 3892 SG CYS C 282 4424 3528 4079 218 304 165 S ATOM 3893 N TYR C 283 17.524 -0.853 -62.046 1.00 28.21 N ANISOU 3893 N TYR C 283 3807 3185 3725 84 299 213 N ATOM 3894 CA TYR C 283 16.146 -0.366 -61.950 1.00 28.16 C ANISOU 3894 CA TYR C 283 3795 3200 3703 56 272 214 C ATOM 3895 C TYR C 283 15.466 -0.550 -63.300 1.00 28.30 C ANISOU 3895 C TYR C 283 3867 3204 3684 60 257 217 C ATOM 3896 O TYR C 283 15.982 -0.073 -64.311 1.00 28.84 O ANISOU 3896 O TYR C 283 3964 3256 3738 90 290 218 O ATOM 3897 CB TYR C 283 16.129 1.114 -61.561 1.00 28.10 C ANISOU 3897 CB TYR C 283 3757 3204 3716 67 289 206 C ATOM 3898 CG TYR C 283 14.743 1.716 -61.505 1.00 28.54 C ANISOU 3898 CG TYR C 283 3797 3296 3750 87 267 201 C ATOM 3899 CD1 TYR C 283 13.945 1.576 -60.366 1.00 28.61 C ANISOU 3899 CD1 TYR C 283 3751 3380 3740 86 254 193 C ATOM 3900 CD2 TYR C 283 14.221 2.425 -62.593 1.00 28.95 C ANISOU 3900 CD2 TYR C 283 3880 3329 3790 121 261 213 C ATOM 3901 CE1 TYR C 283 12.672 2.125 -60.309 1.00 29.26 C ANISOU 3901 CE1 TYR C 283 3790 3536 3793 132 244 190 C ATOM 3902 CE2 TYR C 283 12.949 2.980 -62.545 1.00 29.58 C ANISOU 3902 CE2 TYR C 283 3929 3459 3849 169 236 212 C ATOM 3903 CZ TYR C 283 12.176 2.828 -61.402 1.00 29.74 C ANISOU 3903 CZ TYR C 283 3875 3572 3853 183 232 198 C ATOM 3904 OH TYR C 283 10.918 3.371 -61.351 1.00 30.27 O ANISOU 3904 OH TYR C 283 3883 3729 3891 256 217 199 O ATOM 3905 N MET C 284 14.317 -1.229 -63.307 1.00 28.24 N ANISOU 3905 N MET C 284 3865 3217 3648 16 204 228 N ATOM 3906 CA MET C 284 13.505 -1.427 -64.510 1.00 28.60 C ANISOU 3906 CA MET C 284 3956 3263 3646 1 165 232 C ATOM 3907 C MET C 284 12.149 -0.778 -64.298 1.00 28.72 C ANISOU 3907 C MET C 284 3890 3371 3652 -15 134 259 C ATOM 3908 O MET C 284 11.546 -0.961 -63.248 1.00 28.78 O ANISOU 3908 O MET C 284 3822 3448 3665 -50 122 278 O ATOM 3909 CB MET C 284 13.308 -2.923 -64.784 1.00 29.28 C ANISOU 3909 CB MET C 284 4129 3296 3700 -57 102 226 C ATOM 3910 CG MET C 284 12.605 -3.250 -66.099 1.00 30.00 C ANISOU 3910 CG MET C 284 4296 3377 3728 -87 44 218 C ATOM 3911 SD MET C 284 10.806 -3.064 -66.083 1.00 30.73 S ANISOU 3911 SD MET C 284 4293 3587 3794 -184 -39 273 S ATOM 3912 CE MET C 284 10.325 -4.430 -65.023 1.00 31.19 C ANISOU 3912 CE MET C 284 4355 3636 3859 -326 -111 311 C ATOM 3913 N GLU C 285 11.670 -0.035 -65.295 1.00 28.85 N ANISOU 3913 N GLU C 285 3914 3404 3643 22 123 269 N ATOM 3914 CA GLU C 285 10.316 0.518 -65.279 1.00 29.42 C ANISOU 3914 CA GLU C 285 3899 3581 3697 36 83 298 C ATOM 3915 C GLU C 285 9.626 0.244 -66.618 1.00 29.95 C ANISOU 3915 C GLU C 285 4003 3670 3707 7 17 320 C ATOM 3916 O GLU C 285 10.202 0.476 -67.683 1.00 30.10 O ANISOU 3916 O GLU C 285 4115 3623 3699 35 27 312 O ATOM 3917 CB GLU C 285 10.333 2.021 -64.964 1.00 29.46 C ANISOU 3917 CB GLU C 285 3875 3586 3731 146 121 292 C ATOM 3918 CG GLU C 285 8.952 2.649 -64.826 1.00 30.53 C ANISOU 3918 CG GLU C 285 3910 3845 3846 214 87 314 C ATOM 3919 CD GLU C 285 8.980 4.146 -64.544 1.00 31.00 C ANISOU 3919 CD GLU C 285 3986 3863 3929 352 109 294 C ATOM 3920 OE1 GLU C 285 8.079 4.846 -65.047 1.00 31.72 O ANISOU 3920 OE1 GLU C 285 4047 4004 4000 447 71 318 O ATOM 3921 OE2 GLU C 285 9.875 4.625 -63.810 1.00 30.81 O ANISOU 3921 OE2 GLU C 285 4013 3752 3942 369 152 254 O ATOM 3922 N HIS C 286 8.386 -0.238 -66.541 1.00 30.53 N ANISOU 3922 N HIS C 286 3993 3856 3750 -60 -54 357 N ATOM 3923 CA HIS C 286 7.622 -0.659 -67.712 1.00 31.18 C ANISOU 3923 CA HIS C 286 4102 3976 3768 -121 -145 381 C ATOM 3924 C HIS C 286 6.126 -0.612 -67.407 1.00 32.04 C ANISOU 3924 C HIS C 286 4043 4274 3857 -162 -211 443 C ATOM 3925 O HIS C 286 5.666 -1.272 -66.470 1.00 31.96 O ANISOU 3925 O HIS C 286 3943 4347 3853 -256 -223 472 O ATOM 3926 CB HIS C 286 8.032 -2.083 -68.107 1.00 31.49 C ANISOU 3926 CB HIS C 286 4276 3916 3775 -239 -196 352 C ATOM 3927 CG HIS C 286 7.341 -2.599 -69.330 1.00 32.69 C ANISOU 3927 CG HIS C 286 4492 4084 3844 -318 -305 359 C ATOM 3928 ND1 HIS C 286 6.132 -3.258 -69.277 1.00 34.06 N ANISOU 3928 ND1 HIS C 286 4594 4360 3986 -463 -419 410 N ATOM 3929 CD2 HIS C 286 7.690 -2.558 -70.637 1.00 33.07 C ANISOU 3929 CD2 HIS C 286 4671 4072 3823 -284 -325 324 C ATOM 3930 CE1 HIS C 286 5.764 -3.599 -70.499 1.00 34.96 C ANISOU 3930 CE1 HIS C 286 4801 4463 4019 -520 -517 400 C ATOM 3931 NE2 HIS C 286 6.693 -3.187 -71.344 1.00 34.49 N ANISOU 3931 NE2 HIS C 286 4871 4305 3929 -403 -458 343 N ATOM 3932 N SER C 287 5.389 0.181 -68.189 1.00 32.60 N ANISOU 3932 N SER C 287 4061 4430 3897 -89 -253 474 N ATOM 3933 CA SER C 287 3.923 0.314 -68.081 1.00 33.91 C ANISOU 3933 CA SER C 287 4037 4816 4032 -101 -322 542 C ATOM 3934 C SER C 287 3.434 0.723 -66.683 1.00 33.86 C ANISOU 3934 C SER C 287 3853 4956 4056 -33 -256 558 C ATOM 3935 O SER C 287 2.399 0.250 -66.214 1.00 34.65 O ANISOU 3935 O SER C 287 3779 5260 4125 -118 -295 619 O ATOM 3936 CB SER C 287 3.228 -0.982 -68.540 1.00 35.11 C ANISOU 3936 CB SER C 287 4179 5033 4128 -316 -443 583 C ATOM 3937 OG SER C 287 3.617 -1.329 -69.861 1.00 35.42 O ANISOU 3937 OG SER C 287 4396 4948 4115 -359 -508 552 O ATOM 3938 N GLY C 288 4.189 1.604 -66.026 1.00 32.90 N ANISOU 3938 N GLY C 288 3777 4741 3982 113 -158 503 N ATOM 3939 CA GLY C 288 3.857 2.068 -64.678 1.00 33.06 C ANISOU 3939 CA GLY C 288 3666 4882 4012 205 -88 493 C ATOM 3940 C GLY C 288 4.246 1.136 -63.539 1.00 32.53 C ANISOU 3940 C GLY C 288 3585 4824 3950 77 -45 490 C ATOM 3941 O GLY C 288 3.947 1.429 -62.382 1.00 32.78 O ANISOU 3941 O GLY C 288 3506 4981 3967 140 15 483 O ATOM 3942 N ASN C 289 4.905 0.021 -63.858 1.00 31.88 N ANISOU 3942 N ASN C 289 3625 4610 3878 -87 -80 493 N ATOM 3943 CA ASN C 289 5.448 -0.897 -62.860 1.00 31.52 C ANISOU 3943 CA ASN C 289 3610 4525 3843 -201 -55 496 C ATOM 3944 C ASN C 289 6.953 -0.709 -62.800 1.00 29.96 C ANISOU 3944 C ASN C 289 3576 4111 3696 -140 0 424 C ATOM 3945 O ASN C 289 7.563 -0.311 -63.789 1.00 29.98 O ANISOU 3945 O ASN C 289 3687 3989 3716 -83 -1 388 O ATOM 3946 CB ASN C 289 5.149 -2.343 -63.246 1.00 32.25 C ANISOU 3946 CB ASN C 289 3747 4599 3910 -418 -152 552 C ATOM 3947 CG ASN C 289 3.697 -2.564 -63.592 1.00 34.01 C ANISOU 3947 CG ASN C 289 3808 5035 4078 -518 -234 637 C ATOM 3948 OD1 ASN C 289 2.809 -2.315 -62.781 1.00 35.13 O ANISOU 3948 OD1 ASN C 289 3748 5410 4189 -513 -205 694 O ATOM 3949 ND2 ASN C 289 3.448 -3.031 -64.805 1.00 34.85 N ANISOU 3949 ND2 ASN C 289 3995 5084 4161 -608 -337 645 N ATOM 3950 N HIS C 290 7.555 -1.000 -61.651 1.00 29.21 N ANISOU 3950 N HIS C 290 3488 3996 3616 -160 46 413 N ATOM 3951 CA HIS C 290 9.009 -1.060 -61.550 1.00 27.89 C ANISOU 3951 CA HIS C 290 3453 3651 3494 -132 83 361 C ATOM 3952 C HIS C 290 9.463 -2.314 -60.811 1.00 27.87 C ANISOU 3952 C HIS C 290 3494 3603 3491 -245 62 390 C ATOM 3953 O HIS C 290 8.673 -2.957 -60.118 1.00 28.74 O ANISOU 3953 O HIS C 290 3529 3826 3564 -350 33 454 O ATOM 3954 CB HIS C 290 9.602 0.241 -60.949 1.00 27.35 C ANISOU 3954 CB HIS C 290 3378 3562 3451 4 153 305 C ATOM 3955 CG HIS C 290 9.811 0.217 -59.463 1.00 27.21 C ANISOU 3955 CG HIS C 290 3314 3604 3421 3 190 296 C ATOM 3956 ND1 HIS C 290 8.986 0.885 -58.586 1.00 27.85 N ANISOU 3956 ND1 HIS C 290 3288 3838 3456 75 223 287 N ATOM 3957 CD2 HIS C 290 10.782 -0.349 -58.705 1.00 26.71 C ANISOU 3957 CD2 HIS C 290 3299 3478 3372 -43 200 292 C ATOM 3958 CE1 HIS C 290 9.419 0.708 -57.351 1.00 27.80 C ANISOU 3958 CE1 HIS C 290 3274 3862 3426 58 252 276 C ATOM 3959 NE2 HIS C 290 10.505 -0.041 -57.396 1.00 27.07 N ANISOU 3959 NE2 HIS C 290 3273 3637 3374 -20 232 285 N ATOM 3960 N SER C 291 10.732 -2.662 -61.004 1.00 26.97 N ANISOU 3960 N SER C 291 3500 3335 3413 -222 72 353 N ATOM 3961 CA SER C 291 11.388 -3.724 -60.244 1.00 27.03 C ANISOU 3961 CA SER C 291 3569 3275 3428 -283 52 375 C ATOM 3962 C SER C 291 12.870 -3.391 -60.069 1.00 26.24 C ANISOU 3962 C SER C 291 3518 3082 3371 -186 103 325 C ATOM 3963 O SER C 291 13.452 -2.671 -60.887 1.00 25.92 O ANISOU 3963 O SER C 291 3501 2998 3351 -107 140 282 O ATOM 3964 CB SER C 291 11.211 -5.084 -60.932 1.00 27.62 C ANISOU 3964 CB SER C 291 3761 3246 3486 -384 -36 401 C ATOM 3965 OG SER C 291 11.911 -5.135 -62.163 1.00 27.51 O ANISOU 3965 OG SER C 291 3861 3112 3481 -310 -35 339 O ATOM 3966 N THR C 292 13.459 -3.913 -58.994 1.00 26.26 N ANISOU 3966 N THR C 292 3527 3072 3379 -203 98 347 N ATOM 3967 CA THR C 292 14.862 -3.666 -58.651 1.00 25.70 C ANISOU 3967 CA THR C 292 3472 2949 3345 -125 132 315 C ATOM 3968 C THR C 292 15.611 -4.988 -58.511 1.00 26.27 C ANISOU 3968 C THR C 292 3635 2920 3426 -127 85 340 C ATOM 3969 O THR C 292 15.044 -5.988 -58.066 1.00 26.59 O ANISOU 3969 O THR C 292 3723 2938 3443 -213 22 396 O ATOM 3970 CB THR C 292 14.996 -2.847 -57.351 1.00 25.44 C ANISOU 3970 CB THR C 292 3356 3007 3301 -115 163 310 C ATOM 3971 OG1 THR C 292 14.061 -3.320 -56.374 1.00 25.88 O ANISOU 3971 OG1 THR C 292 3370 3158 3304 -193 141 364 O ATOM 3972 CG2 THR C 292 14.737 -1.367 -57.627 1.00 25.18 C ANISOU 3972 CG2 THR C 292 3279 3015 3274 -59 209 259 C ATOM 3973 N HIS C 293 16.883 -4.984 -58.907 1.00 26.44 N ANISOU 3973 N HIS C 293 3682 2886 3479 -29 111 305 N ATOM 3974 CA HIS C 293 17.683 -6.208 -59.014 1.00 27.46 C ANISOU 3974 CA HIS C 293 3908 2910 3615 29 69 312 C ATOM 3975 C HIS C 293 19.148 -5.939 -58.652 1.00 27.60 C ANISOU 3975 C HIS C 293 3863 2960 3664 132 106 302 C ATOM 3976 O HIS C 293 19.855 -5.247 -59.388 1.00 27.33 O ANISOU 3976 O HIS C 293 3777 2964 3642 198 169 266 O ATOM 3977 CB HIS C 293 17.575 -6.780 -60.428 1.00 28.15 C ANISOU 3977 CB HIS C 293 4111 2902 3683 72 56 267 C ATOM 3978 CG HIS C 293 16.164 -6.921 -60.899 1.00 28.33 C ANISOU 3978 CG HIS C 293 4176 2916 3673 -46 9 280 C ATOM 3979 ND1 HIS C 293 15.396 -8.029 -60.622 1.00 29.39 N ANISOU 3979 ND1 HIS C 293 4408 2974 3785 -155 -89 326 N ATOM 3980 CD2 HIS C 293 15.361 -6.064 -61.571 1.00 28.04 C ANISOU 3980 CD2 HIS C 293 4084 2952 3619 -82 35 266 C ATOM 3981 CE1 HIS C 293 14.188 -7.862 -61.129 1.00 29.55 C ANISOU 3981 CE1 HIS C 293 4413 3039 3775 -264 -119 340 C ATOM 3982 NE2 HIS C 293 14.140 -6.676 -61.707 1.00 28.80 N ANISOU 3982 NE2 HIS C 293 4223 3036 3682 -206 -44 301 N ATOM 3983 N PRO C 294 19.603 -6.473 -57.506 1.00 28.07 N ANISOU 3983 N PRO C 294 3916 3021 3728 135 62 348 N ATOM 3984 CA PRO C 294 20.993 -6.261 -57.101 1.00 28.50 C ANISOU 3984 CA PRO C 294 3889 3131 3809 227 80 349 C ATOM 3985 C PRO C 294 21.991 -7.133 -57.871 1.00 29.82 C ANISOU 3985 C PRO C 294 4107 3238 3986 384 80 330 C ATOM 3986 O PRO C 294 21.598 -8.016 -58.639 1.00 30.03 O ANISOU 3986 O PRO C 294 4272 3144 3994 425 52 305 O ATOM 3987 CB PRO C 294 20.984 -6.614 -55.615 1.00 28.77 C ANISOU 3987 CB PRO C 294 3913 3192 3828 175 17 413 C ATOM 3988 CG PRO C 294 19.838 -7.536 -55.434 1.00 29.19 C ANISOU 3988 CG PRO C 294 4082 3161 3849 88 -43 457 C ATOM 3989 CD PRO C 294 18.839 -7.242 -56.506 1.00 28.54 C ANISOU 3989 CD PRO C 294 4029 3056 3761 37 -11 416 C ATOM 3990 N VAL C 295 23.275 -6.866 -57.649 1.00 30.90 N ANISOU 3990 N VAL C 295 4129 3468 4143 475 106 338 N ATOM 3991 CA VAL C 295 24.362 -7.570 -58.327 1.00 32.46 C ANISOU 3991 CA VAL C 295 4329 3664 4341 664 124 318 C ATOM 3992 C VAL C 295 24.597 -8.923 -57.641 1.00 34.29 C ANISOU 3992 C VAL C 295 4670 3785 4573 761 27 354 C ATOM 3993 O VAL C 295 24.846 -8.956 -56.435 1.00 33.99 O ANISOU 3993 O VAL C 295 4580 3788 4546 722 -29 418 O ATOM 3994 CB VAL C 295 25.669 -6.742 -58.300 1.00 32.85 C ANISOU 3994 CB VAL C 295 4173 3899 4408 711 185 334 C ATOM 3995 CG1 VAL C 295 26.821 -7.506 -58.949 1.00 34.43 C ANISOU 3995 CG1 VAL C 295 4341 4147 4596 936 216 319 C ATOM 3996 CG2 VAL C 295 25.459 -5.395 -58.987 1.00 31.94 C ANISOU 3996 CG2 VAL C 295 3981 3865 4292 598 265 315 C ATOM 3997 N PRO C 296 24.544 -10.038 -58.403 1.00 36.10 N ANISOU 3997 N PRO C 296 5070 3865 4782 892 -2 313 N ATOM 3998 CA PRO C 296 24.735 -11.377 -57.825 1.00 38.33 C ANISOU 3998 CA PRO C 296 5505 3994 5065 994 -114 350 C ATOM 3999 C PRO C 296 26.173 -11.679 -57.366 1.00 40.36 C ANISOU 3999 C PRO C 296 5653 4344 5339 1203 -122 378 C ATOM 4000 O PRO C 296 27.039 -10.802 -57.405 1.00 39.98 O ANISOU 4000 O PRO C 296 5382 4506 5303 1236 -42 380 O ATOM 4001 CB PRO C 296 24.322 -12.313 -58.976 1.00 39.20 C ANISOU 4001 CB PRO C 296 5844 3911 5140 1086 -140 271 C ATOM 4002 CG PRO C 296 24.596 -11.533 -60.205 1.00 38.66 C ANISOU 4002 CG PRO C 296 5678 3967 5045 1145 -14 189 C ATOM 4003 CD PRO C 296 24.281 -10.112 -59.854 1.00 36.55 C ANISOU 4003 CD PRO C 296 5214 3873 4803 953 54 227 C ATOM 4004 N SER C 297 26.389 -12.932 -56.960 1.00 43.08 N ANISOU 4004 N SER C 297 6160 4525 5682 1334 -231 409 N ATOM 4005 CA SER C 297 27.655 -13.457 -56.427 1.00 45.45 C ANISOU 4005 CA SER C 297 6388 4883 5996 1562 -272 450 C ATOM 4006 C SER C 297 28.020 -12.818 -55.092 1.00 45.28 C ANISOU 4006 C SER C 297 6177 5032 5994 1444 -303 551 C ATOM 4007 O SER C 297 27.918 -13.471 -54.055 1.00 46.05 O ANISOU 4007 O SER C 297 6367 5041 6090 1423 -419 639 O ATOM 4008 CB SER C 297 28.800 -13.327 -57.437 1.00 46.53 C ANISOU 4008 CB SER C 297 6391 5171 6120 1819 -166 374 C ATOM 4009 OG SER C 297 29.972 -13.954 -56.957 1.00 48.89 O ANISOU 4009 OG SER C 297 6620 5530 6427 2070 -215 416 O ATOM 4010 OXT SER C 297 28.412 -11.653 -55.017 1.00 44.86 O ANISOU 4010 OXT SER C 297 5896 5199 5950 1359 -222 550 O TER 4011 SER C 297 HETATM 4012 C1 GOL A 301 -7.221 -7.248 -18.013 1.00 38.63 C HETATM 4013 O1 GOL A 301 -7.285 -7.323 -16.584 1.00 38.26 O HETATM 4014 C2 GOL A 301 -7.051 -5.799 -18.470 1.00 39.01 C HETATM 4015 O2 GOL A 301 -8.227 -5.039 -18.174 1.00 39.32 O HETATM 4016 C3 GOL A 301 -5.868 -5.155 -17.762 1.00 39.13 C HETATM 4017 O3 GOL A 301 -5.386 -4.053 -18.535 1.00 39.70 O HETATM 4018 C1 GOL A 302 21.065 2.201 -33.154 1.00 43.43 C HETATM 4019 O1 GOL A 302 20.154 3.289 -33.343 1.00 44.42 O HETATM 4020 C2 GOL A 302 21.517 2.165 -31.701 1.00 42.77 C HETATM 4021 O2 GOL A 302 20.377 2.032 -30.847 1.00 43.26 O HETATM 4022 C3 GOL A 302 22.458 0.987 -31.483 1.00 42.27 C HETATM 4023 O3 GOL A 302 23.054 1.087 -30.185 1.00 41.29 O HETATM 4024 C1 GOL A 303 -25.586 -15.849 -0.139 1.00 59.19 C HETATM 4025 O1 GOL A 303 -25.988 -15.703 -1.505 1.00 58.53 O HETATM 4026 C2 GOL A 303 -25.447 -17.339 0.186 1.00 59.29 C HETATM 4027 O2 GOL A 303 -24.382 -17.878 -0.606 1.00 59.97 O HETATM 4028 C3 GOL A 303 -25.191 -17.627 1.674 1.00 59.06 C HETATM 4029 O3 GOL A 303 -25.166 -16.450 2.493 1.00 58.76 O HETATM 4030 C1 GOL B 301 13.165 9.722 -61.902 1.00 55.68 C HETATM 4031 O1 GOL B 301 11.968 8.955 -62.083 1.00 55.60 O HETATM 4032 C2 GOL B 301 14.124 8.972 -60.982 1.00 55.32 C HETATM 4033 O2 GOL B 301 14.407 7.677 -61.532 1.00 54.38 O HETATM 4034 C3 GOL B 301 15.412 9.776 -60.792 1.00 55.18 C HETATM 4035 O3 GOL B 301 16.377 9.459 -61.803 1.00 55.17 O HETATM 4036 C1 GOL B 302 9.778 -8.950 -36.908 1.00 52.39 C HETATM 4037 O1 GOL B 302 8.975 -9.197 -38.071 1.00 52.37 O HETATM 4038 C2 GOL B 302 9.084 -7.988 -35.945 1.00 52.44 C HETATM 4039 O2 GOL B 302 7.661 -8.137 -36.013 1.00 52.16 O HETATM 4040 C3 GOL B 302 9.540 -8.242 -34.511 1.00 52.70 C HETATM 4041 O3 GOL B 302 10.949 -8.014 -34.396 1.00 53.36 O HETATM 4042 S SO4 B 303 -7.991 -3.642 5.496 1.00 64.10 S HETATM 4043 O1 SO4 B 303 -7.064 -3.958 4.383 1.00 64.64 O HETATM 4044 O2 SO4 B 303 -9.372 -3.564 4.974 1.00 64.96 O HETATM 4045 O3 SO4 B 303 -7.907 -4.706 6.521 1.00 63.93 O HETATM 4046 O4 SO4 B 303 -7.623 -2.340 6.099 1.00 64.83 O HETATM 4047 C1 GOL C 301 11.934 3.711 -78.016 1.00 50.80 C HETATM 4048 O1 GOL C 301 10.851 4.058 -78.887 1.00 51.21 O HETATM 4049 C2 GOL C 301 11.428 2.806 -76.898 1.00 50.75 C HETATM 4050 O2 GOL C 301 10.791 1.646 -77.452 1.00 50.70 O HETATM 4051 C3 GOL C 301 12.584 2.383 -75.998 1.00 50.48 C HETATM 4052 O3 GOL C 301 12.086 1.639 -74.881 1.00 49.51 O HETATM 4053 C1 GOL C 302 29.634 0.807 -69.694 1.00 59.86 C HETATM 4054 O1 GOL C 302 29.670 -0.487 -70.310 1.00 60.05 O HETATM 4055 C2 GOL C 302 30.515 1.783 -70.467 1.00 60.12 C HETATM 4056 O2 GOL C 302 30.166 1.770 -71.857 1.00 61.55 O HETATM 4057 C3 GOL C 302 30.334 3.190 -69.909 1.00 60.20 C HETATM 4058 O3 GOL C 302 31.319 4.066 -70.469 1.00 60.16 O HETATM 4059 C1 GOL C 303 26.827 -8.509 -73.992 1.00 62.96 C HETATM 4060 O1 GOL C 303 25.839 -8.694 -75.014 1.00 62.89 O HETATM 4061 C2 GOL C 303 26.817 -7.055 -73.539 1.00 62.93 C HETATM 4062 O2 GOL C 303 25.515 -6.719 -73.049 1.00 63.02 O HETATM 4063 C3 GOL C 303 27.853 -6.847 -72.441 1.00 63.23 C HETATM 4064 O3 GOL C 303 28.073 -5.446 -72.246 1.00 63.55 O HETATM 4065 ZN ZN C 304 24.423 12.100 -73.313 1.00 33.63 ZN HETATM 4066 O HOH A 401 26.766 -14.139 -17.192 1.00 51.61 O HETATM 4067 O HOH A 402 26.210 10.466 -39.504 1.00 37.59 O HETATM 4068 O HOH A 403 -6.445 -14.689 -17.545 1.00 26.75 O HETATM 4069 O HOH A 404 -14.902 -6.592 -17.474 1.00 32.71 O HETATM 4070 O HOH A 405 8.448 -8.647 -57.102 1.00 40.87 O HETATM 4071 O HOH A 406 -13.024 -10.338 -19.066 1.00 30.13 O HETATM 4072 O HOH A 407 29.816 -6.217 -45.570 1.00 30.62 O HETATM 4073 O HOH A 408 -10.766 -5.636 -17.844 1.00 39.34 O HETATM 4074 O HOH A 409 16.889 -1.053 -23.733 1.00 35.88 O HETATM 4075 O HOH A 410 21.500 -0.324 -28.434 1.00 24.44 O HETATM 4076 O HOH A 411 25.106 1.540 -50.693 1.00 39.95 O HETATM 4077 O HOH A 412 3.128 -5.472 -22.520 1.00 31.26 O HETATM 4078 O HOH A 413 -4.090 -23.675 -5.270 1.00 31.86 O HETATM 4079 O HOH A 414 -13.252 -5.570 -9.582 1.00 32.37 O HETATM 4080 O HOH A 415 21.352 -17.812 -31.889 1.00 39.52 O HETATM 4081 O HOH A 416 -12.067 -24.672 -22.225 1.00 30.54 O HETATM 4082 O HOH A 417 11.499 -12.748 -51.842 1.00 31.26 O HETATM 4083 O HOH A 418 14.394 -19.906 -44.035 1.00 33.57 O HETATM 4084 O HOH A 419 6.350 -20.174 -14.636 1.00 30.81 O HETATM 4085 O HOH A 420 7.281 -9.401 -46.569 1.00 25.12 O HETATM 4086 O HOH A 421 6.393 -4.767 -14.950 1.00 28.35 O HETATM 4087 O HOH A 422 -0.146 -15.755 -18.948 1.00 35.28 O HETATM 4088 O HOH A 423 15.671 -4.837 -54.857 1.00 25.55 O HETATM 4089 O HOH A 424 20.693 -9.403 -15.431 1.00 36.78 O HETATM 4090 O HOH A 425 -23.611 -14.744 3.855 1.00 45.11 O HETATM 4091 O HOH A 426 -11.881 -8.077 -20.083 1.00 29.82 O HETATM 4092 O HOH A 427 -8.087 -23.549 -6.575 1.00 39.05 O HETATM 4093 O HOH A 428 -29.287 -12.319 -9.526 1.00 31.78 O HETATM 4094 O HOH A 429 6.953 -12.313 -35.535 1.00 37.73 O HETATM 4095 O HOH A 430 33.801 -7.252 -24.426 1.00 31.04 O HETATM 4096 O HOH A 431 -19.780 -8.204 -3.988 1.00 36.27 O HETATM 4097 O HOH A 432 11.825 -15.290 -34.914 1.00 29.34 O HETATM 4098 O HOH A 433 -15.726 -2.823 -10.112 1.00 32.37 O HETATM 4099 O HOH A 434 23.857 3.396 -29.032 1.00 36.67 O HETATM 4100 O HOH A 435 12.990 -6.727 -24.033 1.00 33.86 O HETATM 4101 O HOH A 436 9.079 -20.246 -18.580 1.00 39.32 O HETATM 4102 O HOH A 437 9.444 -6.351 -21.428 1.00 43.85 O HETATM 4103 O HOH A 438 14.882 -16.430 -18.123 1.00 50.45 O HETATM 4104 O HOH A 439 -18.037 1.055 -4.712 1.00 46.13 O HETATM 4105 O HOH A 440 -7.453 -17.122 -17.157 1.00 30.71 O HETATM 4106 O HOH A 441 12.923 -15.016 -54.804 1.00 37.53 O HETATM 4107 O HOH A 442 19.478 4.621 -37.032 1.00 48.23 O HETATM 4108 O HOH A 443 10.065 -12.296 -31.086 1.00 40.57 O HETATM 4109 O HOH A 444 10.529 -14.512 -43.847 1.00 28.24 O HETATM 4110 O HOH A 445 10.513 -14.209 -19.337 1.00 30.31 O HETATM 4111 O HOH A 446 -20.293 -22.187 -10.798 1.00 39.20 O HETATM 4112 O HOH A 447 8.669 5.216 -33.729 1.00 41.61 O HETATM 4113 O HOH A 448 29.769 -6.262 -38.409 1.00 34.55 O HETATM 4114 O HOH A 449 -11.038 -16.483 -21.547 1.00 29.82 O HETATM 4115 O HOH A 450 17.989 -22.854 -46.455 1.00 49.26 O HETATM 4116 O HOH A 451 -23.005 -9.547 2.931 1.00 41.44 O HETATM 4117 O HOH A 452 17.705 -19.171 -37.579 1.00 36.34 O HETATM 4118 O HOH A 453 -3.326 -21.885 -12.556 1.00 33.15 O HETATM 4119 O HOH A 454 12.300 -6.318 -57.779 1.00 28.34 O HETATM 4120 O HOH A 455 27.035 -14.281 -49.951 1.00 31.25 O HETATM 4121 O HOH A 456 17.800 -4.741 -53.173 1.00 25.08 O HETATM 4122 O HOH A 457 24.594 -10.904 -40.771 1.00 27.98 O HETATM 4123 O HOH A 458 30.512 -3.003 -23.645 1.00 42.51 O HETATM 4124 O HOH A 459 -3.158 -17.163 -17.874 1.00 32.14 O HETATM 4125 O HOH A 460 17.851 -10.872 -57.454 1.00 26.64 O HETATM 4126 O HOH A 461 15.675 4.123 -39.319 1.00 23.12 O HETATM 4127 O HOH A 462 16.469 -18.111 -10.164 1.00 35.11 O HETATM 4128 O HOH A 463 29.213 -11.535 -46.551 1.00 48.07 O HETATM 4129 O HOH A 464 27.899 -14.244 -22.263 1.00 33.05 O HETATM 4130 O HOH A 465 13.429 1.534 -32.146 1.00 24.51 O HETATM 4131 O HOH A 466 5.501 -8.286 -21.323 1.00 33.16 O HETATM 4132 O HOH A 467 11.462 -7.809 -7.011 1.00 55.71 O HETATM 4133 O HOH A 468 -13.121 -17.810 -0.436 1.00 33.28 O HETATM 4134 O HOH A 469 11.301 -2.752 -26.334 1.00 44.02 O HETATM 4135 O HOH A 470 11.685 -16.175 -38.704 1.00 29.56 O HETATM 4136 O HOH A 471 -14.738 -27.312 -13.378 1.00 29.70 O HETATM 4137 O HOH A 472 16.135 1.271 -31.457 1.00 39.18 O HETATM 4138 O HOH A 473 9.744 -3.779 -30.281 1.00 38.53 O HETATM 4139 O HOH A 474 27.367 2.349 -26.719 1.00 49.16 O HETATM 4140 O HOH A 475 4.430 -2.000 -19.426 1.00 32.69 O HETATM 4141 O HOH A 476 12.336 -19.200 -34.321 1.00 51.91 O HETATM 4142 O HOH A 477 21.569 -7.070 -16.274 1.00 31.42 O HETATM 4143 O HOH A 478 -11.936 -17.839 -17.865 1.00 25.90 O HETATM 4144 O HOH A 479 17.669 -7.564 -13.155 1.00 51.54 O HETATM 4145 O HOH A 480 -10.002 -19.123 -16.228 1.00 29.24 O HETATM 4146 O HOH A 481 17.830 -11.403 -9.857 1.00 43.35 O HETATM 4147 O HOH A 482 20.142 2.174 -27.990 1.00 41.11 O HETATM 4148 O HOH A 483 26.369 -16.317 -27.891 1.00 47.97 O HETATM 4149 O HOH A 484 -10.270 -19.053 -21.310 1.00 47.87 O HETATM 4150 O HOH A 485 -14.441 -20.963 -6.730 1.00 29.99 O HETATM 4151 O HOH A 486 31.246 -5.159 -36.323 1.00 36.74 O HETATM 4152 O HOH A 487 -14.186 -13.433 1.430 1.00 33.36 O HETATM 4153 O HOH A 488 12.838 -10.176 -57.177 1.00 36.83 O HETATM 4154 O HOH A 489 31.841 1.147 -29.595 1.00 41.60 O HETATM 4155 O HOH A 490 12.793 -19.748 -30.545 1.00 40.74 O HETATM 4156 O HOH A 491 10.893 -5.025 -27.805 1.00 47.60 O HETATM 4157 O HOH A 492 31.850 -2.629 -40.403 1.00 25.90 O HETATM 4158 O HOH A 493 -19.238 -15.364 -17.475 1.00 31.65 O HETATM 4159 O HOH A 494 22.976 -16.264 -27.568 1.00 39.22 O HETATM 4160 O HOH A 495 15.589 -7.481 -55.246 1.00 27.37 O HETATM 4161 O HOH A 496 -3.432 -21.338 -2.062 1.00 31.05 O HETATM 4162 O HOH A 497 -7.768 -14.666 -19.883 1.00 32.60 O HETATM 4163 O HOH A 498 -12.538 -22.101 -5.125 1.00 38.11 O HETATM 4164 O HOH A 499 -6.504 -12.247 -22.872 1.00 30.17 O HETATM 4165 O HOH A 500 8.271 -11.097 -44.278 1.00 29.82 O HETATM 4166 O HOH A 501 -18.284 -9.290 -1.977 1.00 45.14 O HETATM 4167 O HOH A 502 30.132 -1.262 -25.686 1.00 34.67 O HETATM 4168 O HOH A 503 -0.292 -8.435 -22.645 1.00 29.86 O HETATM 4169 O HOH A 504 19.842 -19.701 -32.980 1.00 35.20 O HETATM 4170 O HOH A 505 2.757 -23.102 -9.314 1.00 29.33 O HETATM 4171 O HOH A 506 6.464 -5.955 -12.493 1.00 26.75 O HETATM 4172 O HOH A 507 -19.283 -2.286 -16.131 1.00 36.04 O HETATM 4173 O HOH A 508 -7.723 -16.127 -0.430 1.00 34.46 O HETATM 4174 O HOH A 509 -16.148 -8.092 -0.800 1.00 53.49 O HETATM 4175 O HOH A 510 26.322 -16.921 -39.346 1.00 47.44 O HETATM 4176 O HOH A 511 -27.132 -8.329 -14.947 1.00 30.89 O HETATM 4177 O HOH A 512 -16.907 -20.639 -18.032 1.00 40.28 O HETATM 4178 O HOH A 513 8.439 -13.054 -40.250 1.00 38.73 O HETATM 4179 O HOH A 514 26.961 -16.661 -51.943 1.00 49.44 O HETATM 4180 O HOH A 515 -22.224 -13.972 -17.326 1.00 35.90 O HETATM 4181 O HOH A 516 12.613 -18.672 -28.064 1.00 42.22 O HETATM 4182 O HOH A 517 26.259 -16.716 -17.048 1.00 53.15 O HETATM 4183 O HOH A 518 25.148 3.986 -42.371 1.00 39.50 O HETATM 4184 O HOH A 519 -3.051 -18.021 -0.864 1.00 57.21 O HETATM 4185 O HOH A 520 -11.330 -21.250 -2.893 1.00 40.55 O HETATM 4186 O HOH A 521 -14.181 -11.743 -21.098 1.00 35.84 O HETATM 4187 O HOH A 522 8.057 -0.251 -15.792 1.00 53.16 O HETATM 4188 O HOH A 523 27.965 1.825 -48.584 1.00 45.20 O HETATM 4189 O HOH A 524 4.396 -22.081 -14.863 1.00 43.79 O HETATM 4190 O HOH A 525 20.177 -13.981 -13.071 1.00 38.61 O HETATM 4191 O HOH A 526 -1.080 -10.995 -22.917 1.00 45.63 O HETATM 4192 O HOH A 527 17.187 -13.247 -58.658 1.00 42.56 O HETATM 4193 O HOH B 401 12.624 -1.501 -53.522 1.00 24.20 O HETATM 4194 O HOH B 402 -18.679 3.394 -28.729 1.00 38.57 O HETATM 4195 O HOH B 403 20.716 11.839 -49.247 1.00 44.52 O HETATM 4196 O HOH B 404 17.624 8.058 -58.558 1.00 25.24 O HETATM 4197 O HOH B 405 -13.158 -1.554 -31.397 1.00 27.65 O HETATM 4198 O HOH B 406 -4.591 -11.695 0.518 1.00 49.47 O HETATM 4199 O HOH B 407 -9.037 -4.612 -35.868 1.00 37.12 O HETATM 4200 O HOH B 408 14.257 16.809 -41.750 1.00 48.36 O HETATM 4201 O HOH B 409 1.607 7.216 -42.571 1.00 30.92 O HETATM 4202 O HOH B 410 -6.633 -2.552 -30.471 1.00 34.76 O HETATM 4203 O HOH B 411 5.207 -1.324 -34.494 1.00 27.29 O HETATM 4204 O HOH B 412 -17.981 -3.844 -22.868 1.00 32.62 O HETATM 4205 O HOH B 413 -5.916 -7.096 -45.170 1.00 40.81 O HETATM 4206 O HOH B 414 1.985 8.341 -36.345 1.00 33.26 O HETATM 4207 O HOH B 415 1.614 -8.101 -40.310 1.00 42.96 O HETATM 4208 O HOH B 416 16.354 4.363 -53.839 1.00 21.84 O HETATM 4209 O HOH B 417 -21.825 2.062 -36.395 1.00 38.80 O HETATM 4210 O HOH B 418 -11.936 20.476 -22.485 1.00 42.86 O HETATM 4211 O HOH B 419 1.674 -2.251 6.588 1.00 34.64 O HETATM 4212 O HOH B 420 12.319 9.416 -51.783 1.00 21.83 O HETATM 4213 O HOH B 421 -3.050 -0.136 -23.835 1.00 30.50 O HETATM 4214 O HOH B 422 -6.056 10.002 -23.542 1.00 39.97 O HETATM 4215 O HOH B 423 -1.714 7.969 -40.766 1.00 41.33 O HETATM 4216 O HOH B 424 5.612 -7.911 -34.267 1.00 48.60 O HETATM 4217 O HOH B 425 22.877 4.142 -44.718 1.00 35.70 O HETATM 4218 O HOH B 426 14.522 6.408 -38.594 1.00 36.08 O HETATM 4219 O HOH B 427 -3.673 -8.560 -45.697 1.00 47.37 O HETATM 4220 O HOH B 428 1.921 3.093 7.057 1.00 47.64 O HETATM 4221 O HOH B 429 -2.000 6.233 -52.445 1.00 31.50 O HETATM 4222 O HOH B 430 3.644 5.576 -51.671 1.00 22.00 O HETATM 4223 O HOH B 431 -4.328 -7.441 -51.966 1.00 44.72 O HETATM 4224 O HOH B 432 4.884 -10.327 -54.836 1.00 32.98 O HETATM 4225 O HOH B 433 -3.180 -4.329 -44.582 1.00 26.87 O HETATM 4226 O HOH B 434 -5.209 3.937 -34.482 1.00 35.10 O HETATM 4227 O HOH B 435 -20.567 2.561 -32.981 1.00 32.20 O HETATM 4228 O HOH B 436 -1.094 15.621 -52.662 1.00 51.53 O HETATM 4229 O HOH B 437 -0.610 1.547 -58.481 1.00 43.93 O HETATM 4230 O HOH B 438 -1.746 0.868 -20.604 1.00 37.42 O HETATM 4231 O HOH B 439 -11.519 -3.224 3.199 1.00 37.73 O HETATM 4232 O HOH B 440 -4.296 6.493 -54.020 1.00 38.89 O HETATM 4233 O HOH B 441 10.149 15.007 -43.326 1.00 35.35 O HETATM 4234 O HOH B 442 14.709 5.865 -63.554 1.00 37.53 O HETATM 4235 O HOH B 443 0.650 5.029 -15.402 1.00 42.43 O HETATM 4236 O HOH B 444 -14.897 -9.428 -24.334 1.00 31.96 O HETATM 4237 O HOH B 445 1.739 6.178 -58.444 1.00 36.97 O HETATM 4238 O HOH B 446 3.618 -12.070 -45.987 1.00 39.75 O HETATM 4239 O HOH B 447 18.366 3.556 -39.261 1.00 34.56 O HETATM 4240 O HOH B 448 14.016 7.492 -57.705 1.00 25.50 O HETATM 4241 O HOH B 449 -15.805 -2.769 -34.680 1.00 33.40 O HETATM 4242 O HOH B 450 16.294 9.288 -40.708 1.00 34.43 O HETATM 4243 O HOH B 451 -7.802 9.192 -46.140 1.00 44.47 O HETATM 4244 O HOH B 452 -18.342 9.422 -23.049 1.00 44.46 O HETATM 4245 O HOH B 453 1.148 -12.648 3.976 1.00 40.87 O HETATM 4246 O HOH B 454 20.767 14.152 -47.866 1.00 37.06 O HETATM 4247 O HOH B 455 -4.943 -7.001 -37.803 1.00 31.27 O HETATM 4248 O HOH B 456 11.545 -2.195 -55.916 1.00 27.97 O HETATM 4249 O HOH B 457 -5.023 13.182 -6.634 1.00 47.81 O HETATM 4250 O HOH B 458 -9.616 -6.874 -2.563 1.00 30.93 O HETATM 4251 O HOH B 459 -1.405 -8.651 -44.252 1.00 27.78 O HETATM 4252 O HOH B 460 4.173 -12.546 -51.591 1.00 43.38 O HETATM 4253 O HOH B 461 1.835 8.800 -57.785 1.00 29.27 O HETATM 4254 O HOH B 462 1.359 8.402 -10.659 1.00 39.74 O HETATM 4255 O HOH B 463 -10.545 -1.213 -31.854 1.00 29.79 O HETATM 4256 O HOH B 464 22.255 4.985 -40.944 1.00 39.40 O HETATM 4257 O HOH B 465 -16.674 6.738 -13.522 1.00 43.05 O HETATM 4258 O HOH B 466 -3.970 11.485 2.957 1.00 42.89 O HETATM 4259 O HOH B 467 6.747 -8.413 -55.042 1.00 32.42 O HETATM 4260 O HOH B 468 0.090 6.575 -35.110 1.00 32.83 O HETATM 4261 O HOH B 469 -16.997 -6.255 -31.823 1.00 46.39 O HETATM 4262 O HOH B 470 11.488 7.496 -37.213 1.00 36.24 O HETATM 4263 O HOH B 471 -11.169 -7.756 4.296 1.00 44.33 O HETATM 4264 O HOH B 472 13.388 15.741 -55.726 1.00 36.77 O HETATM 4265 O HOH B 473 -7.049 -7.296 -26.482 1.00 34.54 O HETATM 4266 O HOH B 474 21.834 -5.421 -47.313 1.00 23.63 O HETATM 4267 O HOH B 475 -7.905 2.194 -30.308 1.00 34.63 O HETATM 4268 O HOH B 476 -20.415 -1.198 -28.178 1.00 32.72 O HETATM 4269 O HOH B 477 13.221 9.042 -40.883 1.00 35.49 O HETATM 4270 O HOH B 478 5.407 -10.990 -47.692 1.00 34.26 O HETATM 4271 O HOH B 479 -14.371 5.236 -48.189 1.00 44.48 O HETATM 4272 O HOH B 480 -13.667 1.119 -49.856 1.00 52.61 O HETATM 4273 O HOH B 481 23.656 3.374 -49.535 1.00 33.62 O HETATM 4274 O HOH B 482 4.120 -4.118 -59.152 1.00 30.83 O HETATM 4275 O HOH B 483 -12.348 -9.483 -0.591 1.00 39.09 O HETATM 4276 O HOH B 484 -9.507 -16.990 1.413 1.00 49.99 O HETATM 4277 O HOH B 485 -13.071 2.511 -2.737 1.00 51.24 O HETATM 4278 O HOH B 486 20.827 8.438 -43.626 1.00 40.35 O HETATM 4279 O HOH B 487 3.112 -0.404 -15.699 1.00 48.71 O HETATM 4280 O HOH B 488 6.084 8.907 -65.231 1.00 54.55 O HETATM 4281 O HOH B 489 10.487 -9.411 -31.663 1.00 44.51 O HETATM 4282 O HOH B 490 -13.592 6.244 -36.072 1.00 44.90 O HETATM 4283 O HOH B 491 3.328 10.129 -34.814 1.00 43.88 O HETATM 4284 O HOH B 492 -11.618 12.162 -5.402 1.00 66.43 O HETATM 4285 O HOH B 493 6.193 16.037 -63.800 1.00 55.38 O HETATM 4286 O HOH B 494 20.004 6.685 -40.113 1.00 49.85 O HETATM 4287 O HOH B 495 14.280 19.564 -47.422 1.00 49.61 O HETATM 4288 O HOH B 496 -10.795 -1.741 11.254 1.00 46.33 O HETATM 4289 O HOH B 497 20.180 13.683 -52.296 1.00 31.92 O HETATM 4290 O HOH B 498 4.168 3.776 -33.747 1.00 45.04 O HETATM 4291 O HOH B 499 -8.776 -3.719 10.120 1.00 48.30 O HETATM 4292 O HOH B 500 -13.894 -3.883 -32.562 1.00 36.34 O HETATM 4293 O HOH B 501 2.995 10.184 -60.072 1.00 48.71 O HETATM 4294 O HOH B 502 5.000 -5.655 -32.610 1.00 48.55 O HETATM 4295 O HOH B 503 -12.133 -5.456 -33.802 1.00 47.94 O HETATM 4296 O HOH C 401 27.387 13.832 -72.034 1.00 53.35 O HETATM 4297 O HOH C 402 6.434 -4.337 -60.544 1.00 29.12 O HETATM 4298 O HOH C 403 16.410 4.537 -61.863 1.00 32.67 O HETATM 4299 O HOH C 404 26.169 11.296 -73.838 1.00 38.35 O HETATM 4300 O HOH C 405 26.723 7.537 -54.553 1.00 43.56 O HETATM 4301 O HOH C 406 22.690 7.369 -51.595 1.00 33.06 O HETATM 4302 O HOH C 407 2.675 -2.010 -60.110 1.00 33.94 O HETATM 4303 O HOH C 408 24.571 3.053 -75.015 1.00 40.68 O HETATM 4304 O HOH C 409 19.422 -9.526 -59.243 1.00 26.36 O HETATM 4305 O HOH C 410 21.783 0.885 -55.614 1.00 21.45 O HETATM 4306 O HOH C 411 21.013 2.435 -81.842 1.00 47.65 O HETATM 4307 O HOH C 412 16.088 -10.799 -69.258 1.00 41.00 O HETATM 4308 O HOH C 413 15.659 0.599 -79.589 1.00 37.26 O HETATM 4309 O HOH C 414 24.722 7.195 -57.120 1.00 40.26 O HETATM 4310 O HOH C 415 22.332 11.263 -66.837 1.00 46.14 O HETATM 4311 O HOH C 416 1.681 -0.264 -71.536 1.00 42.44 O HETATM 4312 O HOH C 417 8.261 -7.551 -64.612 1.00 36.81 O HETATM 4313 O HOH C 418 5.040 -4.414 -66.986 1.00 37.60 O HETATM 4314 O HOH C 419 21.241 -3.464 -79.736 1.00 42.92 O HETATM 4315 O HOH C 420 5.919 1.257 -76.599 1.00 32.47 O HETATM 4316 O HOH C 421 32.196 0.942 -58.571 1.00 46.95 O HETATM 4317 O HOH C 422 16.724 2.449 -71.355 1.00 51.65 O HETATM 4318 O HOH C 423 30.296 -9.160 -55.197 1.00 40.81 O HETATM 4319 O HOH C 424 30.069 -4.323 -52.138 1.00 35.10 O HETATM 4320 O HOH C 425 5.225 -1.077 -78.636 1.00 48.09 O HETATM 4321 O HOH C 426 6.406 3.337 -67.171 1.00 39.53 O HETATM 4322 O HOH C 427 29.421 -8.928 -47.648 1.00 49.27 O HETATM 4323 O HOH C 428 32.674 6.678 -53.677 1.00 57.53 O HETATM 4324 O HOH C 429 6.827 -9.733 -63.787 1.00 52.60 O HETATM 4325 O HOH C 430 24.079 6.338 -49.172 1.00 40.49 O CONECT 156 679 CONECT 679 156 CONECT 1028 1509 CONECT 1509 1028 CONECT 1663 3283 CONECT 1832 2393 CONECT 2393 1832 CONECT 2728 3142 CONECT 3142 2728 CONECT 3283 1663 CONECT 3439 3892 CONECT 3624 4065 CONECT 3892 3439 CONECT 4012 4013 4014 CONECT 4013 4012 CONECT 4014 4012 4015 4016 CONECT 4015 4014 CONECT 4016 4014 4017 CONECT 4017 4016 CONECT 4018 4019 4020 CONECT 4019 4018 CONECT 4020 4018 4021 4022 CONECT 4021 4020 CONECT 4022 4020 4023 CONECT 4023 4022 CONECT 4024 4025 4026 CONECT 4025 4024 CONECT 4026 4024 4027 4028 CONECT 4027 4026 CONECT 4028 4026 4029 CONECT 4029 4028 CONECT 4030 4031 4032 CONECT 4031 4030 CONECT 4032 4030 4033 4034 CONECT 4033 4032 CONECT 4034 4032 4035 CONECT 4035 4034 CONECT 4036 4037 4038 CONECT 4037 4036 CONECT 4038 4036 4039 4040 CONECT 4039 4038 CONECT 4040 4038 4041 CONECT 4041 4040 CONECT 4042 4043 4044 4045 4046 CONECT 4043 4042 CONECT 4044 4042 CONECT 4045 4042 CONECT 4046 4042 CONECT 4047 4048 4049 CONECT 4048 4047 CONECT 4049 4047 4050 4051 CONECT 4050 4049 CONECT 4051 4049 4052 CONECT 4052 4051 CONECT 4053 4054 4055 CONECT 4054 4053 CONECT 4055 4053 4056 4057 CONECT 4056 4055 CONECT 4057 4055 4058 CONECT 4058 4057 CONECT 4059 4060 4061 CONECT 4060 4059 CONECT 4061 4059 4062 4063 CONECT 4062 4061 CONECT 4063 4061 4064 CONECT 4064 4063 CONECT 4065 3624 4299 CONECT 4299 4065 MASTER 399 0 10 12 59 0 19 6 4259 3 68 42 END
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Related entries of code: 6ddr
Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code
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Protein Sequence Similarity
No similar entries are found!
Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
6ddm
RCSB PDB
PDBbind
MICA*008
6ddv
RCSB PDB
PDBbind
MICA*008
Entry Information
PDB ID
6ddr
Complex Type
Protein-Protein
PDBbind Subset
general set
Protein Name
Anti-MICA Fab 13A9
Ligand Name
MICA*008
EC.Number
E.C.-.-.-.-
Resolution
1.9(Å)
Affinity (Kd/Ki/IC50)
Kd=0.94nM
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
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