Browse entries in the PDBbind-CN Database
HEADER STRUCTURAL PROTEIN 28-APR-04 1T44 TITLE STRUCTURAL BASIS OF ACTIN SEQUESTRATION BY THYMOSIN-B4: IMPLICATIONS TITLE 2 FOR ARP2/3 ACTIVATION COMPND MOL_ID: 1; COMPND 2 MOLECULE: CHIMERA OF GELSOLIN DOMAIN 1 AND C-TERMINAL DOMAIN OF COMPND 3 THYMOSIN BETA-4; COMPND 4 CHAIN: G; COMPND 5 FRAGMENT: CHIMERA OF GELSOLIN DOMAIN 1 (RESIDUES 28-152) FROM HUMAN COMPND 6 AND C-TERMINAL DOMAIN OF THYMOSIN BETA-4 FROM MOUSE (RESIDUES 153- COMPND 7 171); COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 2; COMPND 10 MOLECULE: ACTIN, ALPHA; COMPND 11 CHAIN: A; COMPND 12 SYNONYM: ALPHA-ACTIN 1 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: HUMAN, HOUSE MOUSE; SOURCE 4 ORGANISM_TAXID: 9606, 10090; SOURCE 5 STRAIN: ,; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS; SOURCE 10 ORGANISM_COMMON: RABBIT; SOURCE 11 ORGANISM_TAXID: 9986; SOURCE 12 TISSUE: SKELETAL MUSCLE KEYWDS STRUCTURAL PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR E.IROBI,A.H.AGUDA,M.LARSSON,L.D.BURTNICK,R.C.ROBINSON REVDAT 4 23-AUG-17 1T44 1 SOURCE REVDAT 3 24-FEB-09 1T44 1 VERSN REVDAT 2 21-SEP-04 1T44 1 JRNL REVDAT 1 07-SEP-04 1T44 0 JRNL AUTH E.IROBI,A.H.AGUDA,M.LARSSON,C.GUERIN,H.L.YIN,L.D.BURTNICK, JRNL AUTH 2 L.BLANCHOIN,R.C.ROBINSON JRNL TITL STRUCTURAL BASIS OF ACTIN SEQUESTRATION BY THYMOSIN-BETA4: JRNL TITL 2 IMPLICATIONS FOR WH2 PROTEINS. JRNL REF EMBO J. V. 23 3599 2004 JRNL REFN ISSN 0261-4189 JRNL PMID 15329672 JRNL DOI 10.1038/SJ.EMBOJ.7600372 REMARK 2 REMARK 2 RESOLUTION. 2.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.1.24 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2 REMARK 3 NUMBER OF REFLECTIONS : 39223 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) : 0.147 REMARK 3 R VALUE (WORKING SET) : 0.144 REMARK 3 FREE R VALUE : 0.195 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 2079 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2890 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.1270 REMARK 3 BIN FREE R VALUE SET COUNT : 140 REMARK 3 BIN FREE R VALUE : 0.1960 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3959 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 34 REMARK 3 SOLVENT ATOMS : 427 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.98 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 1.14000 REMARK 3 B22 (A**2) : -0.42000 REMARK 3 B33 (A**2) : -0.66000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.35000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 0.134 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.085 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.957 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.937 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4082 ; 0.014 ; 0.021 REMARK 3 BOND LENGTHS OTHERS (A): 3627 ; 0.002 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5535 ; 1.434 ; 1.963 REMARK 3 BOND ANGLES OTHERS (DEGREES): 8473 ; 0.868 ; 3.000 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 499 ; 5.574 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 603 ; 0.094 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4512 ; 0.005 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 809 ; 0.004 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 784 ; 0.203 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 4127 ; 0.245 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): 2242 ; 0.086 ; 0.200 REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 304 ; 0.162 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 15 ; 0.078 ; 0.200 REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 3 ; 0.068 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): 42 ; 0.252 ; 0.200 REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 19 ; 0.106 ; 0.200 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): 2494 ; 0.969 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4025 ; 1.629 ; 2.000 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1588 ; 2.950 ; 3.000 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1510 ; 4.545 ; 4.500 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 : 7 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 4 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 6 A 32 REMARK 3 RESIDUE RANGE : A 71 A 136 REMARK 3 RESIDUE RANGE : A 337 A 375 REMARK 3 RESIDUE RANGE : A 700 A 700 REMARK 3 ORIGIN FOR THE GROUP (A): 13.2700 -8.4420 23.0340 REMARK 3 T TENSOR REMARK 3 T11: 0.0634 T22: 0.1292 REMARK 3 T33: 0.1194 T12: -0.0043 REMARK 3 T13: 0.0115 T23: -0.0121 REMARK 3 L TENSOR REMARK 3 L11: 0.5605 L22: 1.1180 REMARK 3 L33: 1.1494 L12: 0.1648 REMARK 3 L13: -0.2891 L23: 0.1821 REMARK 3 S TENSOR REMARK 3 S11: -0.0190 S12: -0.0111 S13: -0.0442 REMARK 3 S21: -0.0277 S22: 0.0356 S23: -0.1174 REMARK 3 S31: 0.0297 S32: 0.0954 S33: -0.0166 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 : A 33 A 70 REMARK 3 ORIGIN FOR THE GROUP (A): 18.5280 1.1990 3.7080 REMARK 3 T TENSOR REMARK 3 T11: 0.0516 T22: 0.1358 REMARK 3 T33: 0.0745 T12: -0.0136 REMARK 3 T13: 0.0600 T23: -0.0263 REMARK 3 L TENSOR REMARK 3 L11: 3.4305 L22: 8.0116 REMARK 3 L33: 2.9583 L12: 1.4418 REMARK 3 L13: -0.6866 L23: -1.3148 REMARK 3 S TENSOR REMARK 3 S11: 0.1536 S12: 0.1717 S13: 0.0814 REMARK 3 S21: -0.1824 S22: -0.0247 S23: -0.3562 REMARK 3 S31: 0.0883 S32: 0.2529 S33: -0.1289 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 2 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 137 A 180 REMARK 3 RESIDUE RANGE : A 274 A 336 REMARK 3 ORIGIN FOR THE GROUP (A): -10.5150 -0.4510 22.7710 REMARK 3 T TENSOR REMARK 3 T11: 0.0833 T22: 0.1425 REMARK 3 T33: 0.1016 T12: -0.0118 REMARK 3 T13: 0.0025 T23: 0.0092 REMARK 3 L TENSOR REMARK 3 L11: 0.8275 L22: 0.7237 REMARK 3 L33: 1.2282 L12: -0.0942 REMARK 3 L13: 0.0683 L23: -0.1121 REMARK 3 S TENSOR REMARK 3 S11: -0.0133 S12: 0.0317 S13: 0.0173 REMARK 3 S21: -0.0227 S22: 0.0288 S23: 0.0389 REMARK 3 S31: 0.0466 S32: -0.0964 S33: -0.0155 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 NUMBER OF COMPONENTS GROUP : 2 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 181 A 273 REMARK 3 RESIDUE RANGE : A 900 A 900 REMARK 3 ORIGIN FOR THE GROUP (A): -4.7810 13.5290 3.1250 REMARK 3 T TENSOR REMARK 3 T11: 0.1104 T22: 0.1341 REMARK 3 T33: 0.0662 T12: -0.0016 REMARK 3 T13: 0.0049 T23: 0.0351 REMARK 3 L TENSOR REMARK 3 L11: 0.9088 L22: 1.1919 REMARK 3 L33: 1.0628 L12: -0.1035 REMARK 3 L13: -0.3906 L23: -0.3899 REMARK 3 S TENSOR REMARK 3 S11: 0.0332 S12: 0.0584 S13: 0.0367 REMARK 3 S21: -0.1388 S22: -0.0017 S23: -0.0331 REMARK 3 S31: -0.0100 S32: -0.0762 S33: -0.0315 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 NUMBER OF COMPONENTS GROUP : 2 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : G 28 G 152 REMARK 3 RESIDUE RANGE : G 701 G 702 REMARK 3 ORIGIN FOR THE GROUP (A): -2.8120 -1.7860 47.4380 REMARK 3 T TENSOR REMARK 3 T11: 0.1344 T22: 0.1038 REMARK 3 T33: 0.0792 T12: 0.0056 REMARK 3 T13: 0.0027 T23: 0.0003 REMARK 3 L TENSOR REMARK 3 L11: 0.6797 L22: 1.5906 REMARK 3 L33: 0.9111 L12: 0.4544 REMARK 3 L13: -0.2006 L23: -0.0675 REMARK 3 S TENSOR REMARK 3 S11: 0.0099 S12: -0.0591 S13: -0.0098 REMARK 3 S21: 0.1737 S22: 0.0096 S23: 0.0193 REMARK 3 S31: 0.0130 S32: 0.0458 S33: -0.0195 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : G 153 G 171 REMARK 3 ORIGIN FOR THE GROUP (A): 15.5960 12.6590 3.6640 REMARK 3 T TENSOR REMARK 3 T11: 0.0940 T22: 0.0756 REMARK 3 T33: 0.1570 T12: 0.0203 REMARK 3 T13: 0.0962 T23: 0.0520 REMARK 3 L TENSOR REMARK 3 L11: 1.0654 L22: 0.9998 REMARK 3 L33: 32.7026 L12: 0.3132 REMARK 3 L13: -1.0000 L23: -4.8265 REMARK 3 S TENSOR REMARK 3 S11: 0.1943 S12: 0.1473 S13: 0.3959 REMARK 3 S21: 0.0083 S22: -0.0160 S23: -0.2443 REMARK 3 S31: -0.0383 S32: 0.3091 S33: -0.1783 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 901 A 1175 REMARK 3 ORIGIN FOR THE GROUP (A): -1.0040 1.3470 25.0510 REMARK 3 T TENSOR REMARK 3 T11: 0.1027 T22: 0.1280 REMARK 3 T33: 0.1012 T12: -0.0148 REMARK 3 T13: -0.0028 T23: 0.0088 REMARK 3 L TENSOR REMARK 3 L11: 0.0662 L22: 0.2688 REMARK 3 L33: 0.3065 L12: -0.0219 REMARK 3 L13: -0.1275 L23: -0.0315 REMARK 3 S TENSOR REMARK 3 S11: 0.0024 S12: 0.0201 S13: 0.0092 REMARK 3 S21: 0.0119 S22: 0.0066 S23: -0.0100 REMARK 3 S31: 0.0121 S32: -0.0104 S33: -0.0090 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : BABINET MODEL WITH MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.40 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 1T44 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAY-04. REMARK 100 THE DEPOSITION ID IS D_1000022287. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL 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 : ESRF REMARK 200 BEAMLINE : ID29 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0052 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : NULL REMARK 200 DETECTOR MANUFACTURER : NULL REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39223 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000 REMARK 200 RESOLUTION RANGE LOW (A) : 20.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : NULL REMARK 200 DATA REDUNDANCY : 3.300 REMARK 200 R MERGE (I) : 0.11400 REMARK 200 R SYM (I) : NULL REMARK 200
FOR THE DATA SET : 11.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.10 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : 3.30 REMARK 200 R MERGE FOR SHELL (I) : 0.19800 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200
FOR SHELL : 3.600 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: AMORE REMARK 200 STARTING MODEL: PDB ENTRY 1P8Z REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 51.30 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, SODIUM ACETATE, CALCIUM REMARK 280 CHLORIDE, PH 6.5, MICROBATCH, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 34.66750 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5310 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20980 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -59.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY G 25 REMARK 465 SER G 26 REMARK 465 HIS G 27 REMARK 465 ARG A 39 REMARK 465 HIS A 40 REMARK 465 GLN A 41 REMARK 465 GLY A 42 REMARK 465 VAL A 43 REMARK 465 MET A 44 REMARK 465 VAL A 45 REMARK 465 GLY A 46 REMARK 465 MET A 47 REMARK 465 GLY A 48 REMARK 465 GLN A 49 REMARK 465 LYS A 50 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O GLN G 171 O HOH G 749 2.17 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ASP A 51 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES REMARK 500 ARG A 147 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES REMARK 500 ARG A 147 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES REMARK 500 ASP A 222 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES REMARK 500 ARG A 256 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES REMARK 500 ARG A 256 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 LEU G 112 30.42 -86.37 REMARK 500 PHE G 125 27.13 -141.50 REMARK 500 LYS G 157 77.47 -101.83 REMARK 500 ALA A 181 -159.45 -151.97 REMARK 500 ASN A 296 55.73 -141.84 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 CA A 700 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HOH A 909 O REMARK 620 2 HOH A 970 O 100.3 REMARK 620 3 HOH A 911 O 82.4 78.7 REMARK 620 4 ATP A 900 O2B 171.1 86.8 94.0 REMARK 620 5 ATP A 900 O3G 91.2 152.1 77.7 80.1 REMARK 620 6 HOH A 918 O 96.2 70.2 148.1 91.2 134.1 REMARK 620 7 HOH A 915 O 82.9 136.0 144.4 95.6 70.3 65.8 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA G 701 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ALA G 116 O REMARK 620 2 HOH G 724 O 132.6 REMARK 620 3 GLY G 114 O 95.8 77.1 REMARK 620 4 HOH G 729 O 74.0 58.5 80.0 REMARK 620 5 GLU A 167 OE1 97.4 79.5 156.3 84.8 REMARK 620 6 ASP G 109 OD1 79.4 137.1 70.9 138.0 131.0 REMARK 620 7 ASP G 109 OD2 83.7 140.9 119.2 152.3 81.9 49.1 REMARK 620 8 HOH G 712 O 154.9 72.4 88.2 130.9 88.1 78.6 72.9 REMARK 620 N 1 2 3 4 5 6 7 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA G 702 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 VAL G 145 O REMARK 620 2 HOH G 704 O 74.8 REMARK 620 3 ASP G 66 OD2 88.5 100.6 REMARK 620 4 HOH G 730 O 92.7 89.3 170.0 REMARK 620 5 GLU G 97 OE2 84.7 158.1 86.2 84.1 REMARK 620 6 GLU G 97 OE1 134.4 144.4 100.1 72.1 51.8 REMARK 620 7 GLY G 65 O 149.9 80.1 79.8 103.5 121.7 75.4 REMARK 620 N 1 2 3 4 5 6 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 700 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA G 701 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA G 702 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 900 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1P8Z RELATED DB: PDB REMARK 900 A HYBRID OF THIS PROTEIN WITH THE C-TERMINAL HALF OF THYMOSIN B4 REMARK 999 REMARK 999 SEQUENCE REMARK 999 FUSION OF GELSOLIN DOMAIN 1 FROM HUMAN WITH REMARK 999 C-TERMINAL DOMAIN OF THYMOSIN B4 FROM MOUSE REMARK 999 (SEQUENCE:ETQEKNPLPSKETIEQEKQ) DBREF 1T44 G 28 152 UNP P06396 GELS_HUMAN 55 179 DBREF 1T44 G 153 171 UNP P20065 TYB4_MOUSE 28 46 DBREF 1T44 A 6 375 UNP P02568 ACTS_HUMAN 8 377 SEQADV 1T44 GLY G 25 UNP P06396 CLONING ARTIFACT SEQADV 1T44 SER G 26 UNP P06396 CLONING ARTIFACT SEQADV 1T44 HIS G 27 UNP P06396 CLONING ARTIFACT SEQRES 1 G 147 GLY SER HIS GLU HIS PRO GLU PHE LEU LYS ALA GLY LYS SEQRES 2 G 147 GLU PRO GLY LEU GLN ILE TRP ARG VAL GLU LYS PHE ASP SEQRES 3 G 147 LEU VAL PRO VAL PRO THR ASN LEU TYR GLY ASP PHE PHE SEQRES 4 G 147 THR GLY ASP ALA TYR VAL ILE LEU LYS THR VAL GLN LEU SEQRES 5 G 147 ARG ASN GLY ASN LEU GLN TYR ASP LEU HIS TYR TRP LEU SEQRES 6 G 147 GLY ASN GLU CYS SER GLN ASP GLU SER GLY ALA ALA ALA SEQRES 7 G 147 ILE PHE THR VAL GLN LEU ASP ASP TYR LEU ASN GLY ARG SEQRES 8 G 147 ALA VAL GLN HIS ARG GLU VAL GLN GLY PHE GLU SER ALA SEQRES 9 G 147 THR PHE LEU GLY TYR PHE LYS SER GLY LEU LYS TYR LYS SEQRES 10 G 147 LYS GLY GLY VAL ALA SER GLY PHE LYS HIS VAL GLU THR SEQRES 11 G 147 GLN GLU LYS ASN PRO LEU PRO SER LYS GLU THR ILE GLU SEQRES 12 G 147 GLN GLU LYS GLN SEQRES 1 A 370 THR ALA LEU VAL CYS ASP ASN GLY SER GLY LEU VAL LYS SEQRES 2 A 370 ALA GLY PHE ALA GLY ASP ASP ALA PRO ARG ALA VAL PHE SEQRES 3 A 370 PRO SER ILE VAL GLY ARG PRO ARG HIS GLN GLY VAL MET SEQRES 4 A 370 VAL GLY MET GLY GLN LYS ASP SER TYR VAL GLY ASP GLU SEQRES 5 A 370 ALA GLN SER LYS ARG GLY ILE LEU THR LEU LYS TYR PRO SEQRES 6 A 370 ILE GLU HIS GLY ILE ILE THR ASN TRP ASP ASP MET GLU SEQRES 7 A 370 LYS ILE TRP HIS HIS THR PHE TYR ASN GLU LEU ARG VAL SEQRES 8 A 370 ALA PRO GLU GLU HIS PRO THR LEU LEU THR GLU ALA PRO SEQRES 9 A 370 LEU ASN PRO LYS ALA ASN ARG GLU LYS MET THR GLN ILE SEQRES 10 A 370 MET PHE GLU THR PHE ASN VAL PRO ALA MET TYR VAL ALA SEQRES 11 A 370 ILE GLN ALA VAL LEU SER LEU TYR ALA SER GLY ARG THR SEQRES 12 A 370 THR GLY ILE VAL LEU ASP SER GLY ASP GLY VAL THR HIS SEQRES 13 A 370 ASN VAL PRO ILE TYR GLU GLY TYR ALA LEU PRO HIS ALA SEQRES 14 A 370 ILE MET ARG LEU ASP LEU ALA GLY ARG ASP LEU THR ASP SEQRES 15 A 370 TYR LEU MET LYS ILE LEU THR GLU ARG GLY TYR SER PHE SEQRES 16 A 370 VAL THR THR ALA GLU ARG GLU ILE VAL ARG ASP ILE LYS SEQRES 17 A 370 GLU LYS LEU CYS TYR VAL ALA LEU ASP PHE GLU ASN GLU SEQRES 18 A 370 MET ALA THR ALA ALA SER SER SER SER LEU GLU LYS SER SEQRES 19 A 370 TYR GLU LEU PRO ASP GLY GLN VAL ILE THR ILE GLY ASN SEQRES 20 A 370 GLU ARG PHE ARG CYS PRO GLU THR LEU PHE GLN PRO SER SEQRES 21 A 370 PHE ILE GLY MET GLU SER ALA GLY ILE HIS GLU THR THR SEQRES 22 A 370 TYR ASN SER ILE MET LYS CYS ASP ILE ASP ILE ARG LYS SEQRES 23 A 370 ASP LEU TYR ALA ASN ASN VAL MET SER GLY GLY THR THR SEQRES 24 A 370 MET TYR PRO GLY ILE ALA ASP ARG MET GLN LYS GLU ILE SEQRES 25 A 370 THR ALA LEU ALA PRO SER THR MET LYS ILE LYS ILE ILE SEQRES 26 A 370 ALA PRO PRO GLU ARG LYS TYR SER VAL TRP ILE GLY GLY SEQRES 27 A 370 SER ILE LEU ALA SER LEU SER THR PHE GLN GLN MET TRP SEQRES 28 A 370 ILE THR LYS GLN GLU TYR ASP GLU ALA GLY PRO SER ILE SEQRES 29 A 370 VAL HIS ARG LYS CYS PHE HET CA G 701 1 HET CA G 702 1 HET CA A 700 1 HET ATP A 900 31 HETNAM CA CALCIUM ION HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE FORMUL 3 CA 3(CA 2+) FORMUL 6 ATP C10 H16 N5 O13 P3 FORMUL 7 HOH *427(H2 O) HELIX 1 1 HIS G 29 ALA G 35 1 7 HELIX 2 2 PRO G 55 TYR G 59 5 5 HELIX 3 3 SER G 94 LEU G 112 1 19 HELIX 4 4 SER G 127 GLY G 132 1 6 HELIX 5 5 SER G 162 GLN G 171 1 10 HELIX 6 6 GLY A 55 LYS A 61 1 7 HELIX 7 7 ARG A 62 LEU A 65 5 4 HELIX 8 8 ASN A 78 ASN A 92 1 15 HELIX 9 9 ALA A 97 HIS A 101 5 5 HELIX 10 10 PRO A 112 THR A 126 1 15 HELIX 11 11 GLN A 137 SER A 145 1 9 HELIX 12 12 PRO A 172 ILE A 175 5 4 HELIX 13 13 ALA A 181 ARG A 196 1 16 HELIX 14 14 THR A 202 CYS A 217 1 16 HELIX 15 15 ASP A 222 SER A 233 1 12 HELIX 16 16 ASN A 252 THR A 260 1 9 HELIX 17 17 LEU A 261 PHE A 262 5 2 HELIX 18 18 GLN A 263 GLY A 268 5 6 HELIX 19 19 GLY A 273 LYS A 284 1 12 HELIX 20 20 ASP A 286 ALA A 295 1 10 HELIX 21 21 GLY A 301 MET A 305 5 5 HELIX 22 22 GLY A 308 ALA A 321 1 14 HELIX 23 23 GLU A 334 LYS A 336 5 3 HELIX 24 24 TYR A 337 LEU A 349 1 13 HELIX 25 25 SER A 350 GLN A 353 5 4 HELIX 26 26 LYS A 359 GLY A 366 1 8 HELIX 27 27 ILE A 369 CYS A 374 1 6 SHEET 1 A 5 ASP G 50 PRO G 53 0 SHEET 2 A 5 GLY G 40 GLU G 47 -1 N ARG G 45 O VAL G 52 SHEET 3 A 5 ALA G 67 GLN G 75 -1 O VAL G 69 N TRP G 44 SHEET 4 A 5 LEU G 81 LEU G 89 -1 O GLN G 82 N VAL G 74 SHEET 5 A 5 VAL G 117 VAL G 122 1 O GLU G 121 N TYR G 87 SHEET 1 B 2 ASP G 61 PHE G 63 0 SHEET 2 B 2 LYS G 139 LYS G 141 1 O LYS G 139 N PHE G 62 SHEET 1 C 7 GLN G 155 GLU G 156 0 SHEET 2 C 7 ALA A 29 PRO A 32 1 O VAL A 30 N GLN G 155 SHEET 3 C 7 LEU A 16 PHE A 21 -1 N VAL A 17 O PHE A 31 SHEET 4 C 7 LEU A 8 ASN A 12 -1 N ASP A 11 O LYS A 18 SHEET 5 C 7 THR A 103 GLU A 107 1 O LEU A 104 N LEU A 8 SHEET 6 C 7 ALA A 131 ILE A 136 1 O TYR A 133 N LEU A 105 SHEET 7 C 7 ILE A 357 THR A 358 -1 O ILE A 357 N MET A 132 SHEET 1 D 3 TYR A 53 VAL A 54 0 SHEET 2 D 3 VAL A 35 ARG A 37 -1 N GLY A 36 O TYR A 53 SHEET 3 D 3 THR A 66 LYS A 68 -1 O THR A 66 N ARG A 37 SHEET 1 E 2 ILE A 71 GLU A 72 0 SHEET 2 E 2 ILE A 75 ILE A 76 -1 O ILE A 75 N GLU A 72 SHEET 1 F 3 TYR A 169 ALA A 170 0 SHEET 2 F 3 THR A 160 TYR A 166 -1 N TYR A 166 O TYR A 169 SHEET 3 F 3 MET A 176 LEU A 178 -1 O LEU A 178 N THR A 160 SHEET 1 G 5 TYR A 169 ALA A 170 0 SHEET 2 G 5 THR A 160 TYR A 166 -1 N TYR A 166 O TYR A 169 SHEET 3 G 5 GLY A 150 SER A 155 -1 N GLY A 150 O ILE A 165 SHEET 4 G 5 ASN A 297 SER A 300 1 O SER A 300 N LEU A 153 SHEET 5 G 5 ILE A 329 ILE A 330 1 O ILE A 330 N ASN A 297 SHEET 1 H 2 LYS A 238 GLU A 241 0 SHEET 2 H 2 VAL A 247 ILE A 250 -1 O ILE A 248 N TYR A 240 LINK CA CA A 700 O HOH A 909 1555 1555 2.38 LINK CA CA A 700 O HOH A 970 1555 1555 2.38 LINK CA CA A 700 O HOH A 911 1555 1555 2.43 LINK CA CA A 700 O2B ATP A 900 1555 1555 2.30 LINK CA CA A 700 O3G ATP A 900 1555 1555 2.41 LINK CA CA A 700 O HOH A 918 1555 1555 2.36 LINK CA CA A 700 O HOH A 915 1555 1555 2.75 LINK CA CA G 701 O ALA G 116 1555 1555 2.31 LINK CA CA G 701 O HOH G 724 1555 1555 2.61 LINK CA CA G 701 O GLY G 114 1555 1555 2.43 LINK CA CA G 701 O HOH G 729 1555 1555 2.42 LINK CA CA G 701 OE1 GLU A 167 1555 1555 2.31 LINK CA CA G 701 OD1 ASP G 109 1555 1555 2.75 LINK CA CA G 701 OD2 ASP G 109 1555 1555 2.36 LINK CA CA G 701 O HOH G 712 1555 1555 2.40 LINK CA CA G 702 O VAL G 145 1555 1555 2.34 LINK CA CA G 702 O HOH G 704 1555 1555 2.32 LINK CA CA G 702 OD2 ASP G 66 1555 1555 2.34 LINK CA CA G 702 O HOH G 730 1555 1555 2.33 LINK CA CA G 702 OE2 GLU G 97 1555 1555 2.46 LINK CA CA G 702 OE1 GLU G 97 1555 1555 2.53 LINK CA CA G 702 O GLY G 65 1555 1555 2.33 SITE 1 AC1 6 ATP A 900 HOH A 909 HOH A 911 HOH A 915 SITE 2 AC1 6 HOH A 918 HOH A 970 SITE 1 AC2 7 GLU A 167 ASP G 109 GLY G 114 ALA G 116 SITE 2 AC2 7 HOH G 712 HOH G 724 HOH G 729 SITE 1 AC3 6 GLY G 65 ASP G 66 GLU G 97 VAL G 145 SITE 2 AC3 6 HOH G 704 HOH G 730 SITE 1 AC4 26 GLY A 13 SER A 14 GLY A 15 LEU A 16 SITE 2 AC4 26 LYS A 18 GLY A 156 ASP A 157 GLY A 158 SITE 3 AC4 26 VAL A 159 GLY A 182 ARG A 210 LYS A 213 SITE 4 AC4 26 GLU A 214 GLY A 301 GLY A 302 THR A 303 SITE 5 AC4 26 MET A 305 TYR A 306 CA A 700 HOH A 904 SITE 6 AC4 26 HOH A 911 HOH A 915 HOH A 949 HOH A 992 SITE 7 AC4 26 HOH A 999 HOH A1022 CRYST1 56.850 69.335 80.233 90.00 94.93 90.00 P 1 21 1 2 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.017590 0.000000 0.001517 0.00000 SCALE2 0.000000 0.014423 0.000000 0.00000 SCALE3 0.000000 0.000000 0.012510 0.00000 ATOM 1 N GLU G 28 8.638 -15.399 45.200 1.00 29.90 N ANISOU 1 N GLU G 28 3824 3791 3746 7 -104 -108 N ATOM 2 CA GLU G 28 9.932 -15.203 45.914 1.00 29.78 C ANISOU 2 CA GLU G 28 3779 3777 3756 -3 -12 -39 C ATOM 3 C GLU G 28 10.035 -13.826 46.588 1.00 28.00 C ANISOU 3 C GLU G 28 3566 3548 3525 18 -29 -40 C ATOM 4 O GLU G 28 10.720 -13.688 47.582 1.00 28.15 O ANISOU 4 O GLU G 28 3582 3594 3517 13 -43 -34 O ATOM 5 CB GLU G 28 11.135 -15.433 44.979 1.00 30.53 C ANISOU 5 CB GLU G 28 3884 3853 3860 11 -27 -54 C ATOM 6 CG GLU G 28 12.245 -16.237 45.649 1.00 33.63 C ANISOU 6 CG GLU G 28 4227 4253 4298 -119 12 -62 C ATOM 7 CD GLU G 28 13.554 -16.270 44.867 1.00 38.02 C ANISOU 7 CD GLU G 28 4957 4665 4820 -196 14 -214 C ATOM 8 OE1 GLU G 28 14.406 -15.360 45.074 1.00 40.30 O ANISOU 8 OE1 GLU G 28 5239 4933 5140 -460 -39 -201 O ATOM 9 OE2 GLU G 28 13.746 -17.218 44.063 1.00 39.37 O ANISOU 9 OE2 GLU G 28 5389 4456 5113 -180 -76 -455 O ATOM 10 N HIS G 29 9.364 -12.811 46.057 1.00 26.21 N ANISOU 10 N HIS G 29 3355 3326 3276 -19 23 -16 N ATOM 11 CA HIS G 29 9.335 -11.517 46.728 1.00 24.61 C ANISOU 11 CA HIS G 29 3143 3105 3101 21 -8 32 C ATOM 12 C HIS G 29 8.759 -11.658 48.154 1.00 23.40 C ANISOU 12 C HIS G 29 2976 2971 2944 19 -14 13 C ATOM 13 O HIS G 29 7.694 -12.232 48.320 1.00 22.00 O ANISOU 13 O HIS G 29 2731 2814 2811 40 -32 16 O ATOM 14 CB HIS G 29 8.504 -10.530 45.921 1.00 24.72 C ANISOU 14 CB HIS G 29 3157 3166 3068 0 3 41 C ATOM 15 CG HIS G 29 8.521 -9.146 46.472 1.00 23.27 C ANISOU 15 CG HIS G 29 3089 2786 2963 53 -76 148 C ATOM 16 ND1 HIS G 29 9.060 -8.076 45.790 1.00 24.88 N ANISOU 16 ND1 HIS G 29 3284 2971 3196 20 -143 67 N ATOM 17 CD2 HIS G 29 8.084 -8.661 47.654 1.00 21.31 C ANISOU 17 CD2 HIS G 29 2791 2555 2751 93 -62 183 C ATOM 18 CE1 HIS G 29 8.922 -6.984 46.526 1.00 23.68 C ANISOU 18 CE1 HIS G 29 3115 2885 2995 -26 -52 59 C ATOM 19 NE2 HIS G 29 8.346 -7.316 47.668 1.00 22.09 N ANISOU 19 NE2 HIS G 29 2898 2811 2684 18 -288 129 N ATOM 20 N PRO G 30 9.457 -11.141 49.172 1.00 22.54 N ANISOU 20 N PRO G 30 2856 2872 2834 3 -2 18 N ATOM 21 CA PRO G 30 9.028 -11.306 50.578 1.00 21.81 C ANISOU 21 CA PRO G 30 2755 2815 2718 -2 -2 3 C ATOM 22 C PRO G 30 7.572 -10.900 50.888 1.00 20.31 C ANISOU 22 C PRO G 30 2549 2630 2538 22 5 29 C ATOM 23 O PRO G 30 6.910 -11.580 51.665 1.00 20.05 O ANISOU 23 O PRO G 30 2528 2762 2328 79 -26 117 O ATOM 24 CB PRO G 30 10.014 -10.413 51.369 1.00 22.25 C ANISOU 24 CB PRO G 30 2792 2883 2778 -35 21 27 C ATOM 25 CG PRO G 30 11.201 -10.237 50.485 1.00 23.03 C ANISOU 25 CG PRO G 30 2864 2989 2895 16 8 -27 C ATOM 26 CD PRO G 30 10.718 -10.379 49.065 1.00 22.64 C ANISOU 26 CD PRO G 30 2829 2916 2855 12 -18 17 C ATOM 27 N GLU G 31 7.087 -9.815 50.296 1.00 18.73 N ANISOU 27 N GLU G 31 2380 2412 2323 7 39 14 N ATOM 28 CA GLU G 31 5.712 -9.376 50.516 1.00 17.17 C ANISOU 28 CA GLU G 31 2173 2226 2121 -1 -2 -8 C ATOM 29 C GLU G 31 4.649 -10.274 49.899 1.00 16.89 C ANISOU 29 C GLU G 31 2179 2125 2110 -18 54 6 C ATOM 30 O GLU G 31 3.545 -10.329 50.403 1.00 15.89 O ANISOU 30 O GLU G 31 1962 2102 1971 -155 85 -97 O ATOM 31 CB GLU G 31 5.512 -7.918 50.052 1.00 17.09 C ANISOU 31 CB GLU G 31 2127 2255 2111 -33 74 -21 C ATOM 32 CG GLU G 31 6.276 -6.889 50.886 1.00 17.07 C ANISOU 32 CG GLU G 31 2137 2268 2078 58 53 24 C ATOM 33 CD GLU G 31 6.007 -6.990 52.386 1.00 16.96 C ANISOU 33 CD GLU G 31 1946 2568 1930 153 83 -103 C ATOM 34 OE1 GLU G 31 4.823 -7.132 52.778 1.00 15.12 O ANISOU 34 OE1 GLU G 31 1531 2304 1907 157 -143 -79 O ATOM 35 OE2 GLU G 31 6.980 -6.920 53.177 1.00 16.49 O ANISOU 35 OE2 GLU G 31 1554 2792 1917 647 273 -119 O ATOM 36 N PHE G 32 4.958 -10.937 48.790 1.00 16.22 N ANISOU 36 N PHE G 32 2122 2012 2026 2 15 -27 N ATOM 37 CA PHE G 32 4.041 -11.930 48.233 1.00 16.71 C ANISOU 37 CA PHE G 32 2167 2096 2085 12 42 42 C ATOM 38 C PHE G 32 3.898 -13.094 49.208 1.00 16.85 C ANISOU 38 C PHE G 32 2204 2106 2092 15 4 35 C ATOM 39 O PHE G 32 2.800 -13.619 49.411 1.00 16.62 O ANISOU 39 O PHE G 32 2135 2091 2086 -62 -46 144 O ATOM 40 CB PHE G 32 4.527 -12.447 46.876 1.00 16.69 C ANISOU 40 CB PHE G 32 2235 2051 2055 -21 -32 5 C ATOM 41 CG PHE G 32 4.170 -11.560 45.726 1.00 17.39 C ANISOU 41 CG PHE G 32 2488 2169 1950 -46 -10 121 C ATOM 42 CD1 PHE G 32 4.227 -10.160 45.839 1.00 19.02 C ANISOU 42 CD1 PHE G 32 2828 2441 1958 -33 -46 142 C ATOM 43 CD2 PHE G 32 3.769 -12.112 44.528 1.00 18.96 C ANISOU 43 CD2 PHE G 32 2748 2209 2244 -202 -276 152 C ATOM 44 CE1 PHE G 32 3.889 -9.329 44.748 1.00 19.62 C ANISOU 44 CE1 PHE G 32 2788 2329 2337 39 -100 138 C ATOM 45 CE2 PHE G 32 3.438 -11.290 43.448 1.00 20.88 C ANISOU 45 CE2 PHE G 32 2891 2707 2333 -173 -365 118 C ATOM 46 CZ PHE G 32 3.492 -9.902 43.562 1.00 18.33 C ANISOU 46 CZ PHE G 32 2679 2189 2094 -81 -223 157 C ATOM 47 N LEU G 33 4.994 -13.476 49.838 1.00 17.00 N ANISOU 47 N LEU G 33 2145 2141 2170 47 34 -2 N ATOM 48 CA LEU G 33 4.949 -14.582 50.805 1.00 17.80 C ANISOU 48 CA LEU G 33 2269 2240 2253 42 -14 -33 C ATOM 49 C LEU G 33 4.035 -14.236 51.978 1.00 17.35 C ANISOU 49 C LEU G 33 2158 2165 2267 12 -4 3 C ATOM 50 O LEU G 33 3.451 -15.126 52.573 1.00 17.21 O ANISOU 50 O LEU G 33 2213 1873 2450 -4 -35 -72 O ATOM 51 CB LEU G 33 6.364 -14.924 51.302 1.00 18.71 C ANISOU 51 CB LEU G 33 2368 2344 2396 52 0 -64 C ATOM 52 CG LEU G 33 7.029 -16.169 50.700 1.00 22.73 C ANISOU 52 CG LEU G 33 2773 3010 2852 40 -39 -29 C ATOM 53 CD1 LEU G 33 7.154 -16.041 49.209 1.00 25.91 C ANISOU 53 CD1 LEU G 33 3219 3356 3268 40 56 -22 C ATOM 54 CD2 LEU G 33 8.392 -16.387 51.318 1.00 25.77 C ANISOU 54 CD2 LEU G 33 3121 3300 3369 83 -50 -110 C ATOM 55 N LYS G 34 3.916 -12.945 52.316 1.00 16.59 N ANISOU 55 N LYS G 34 2090 2067 2146 25 24 -21 N ATOM 56 CA LYS G 34 3.072 -12.524 53.444 1.00 16.84 C ANISOU 56 CA LYS G 34 2121 2120 2156 22 -25 -3 C ATOM 57 C LYS G 34 1.610 -12.254 53.048 1.00 15.49 C ANISOU 57 C LYS G 34 1937 1961 1985 8 -20 17 C ATOM 58 O LYS G 34 0.749 -12.197 53.913 1.00 15.41 O ANISOU 58 O LYS G 34 1986 1989 1879 33 -84 103 O ATOM 59 CB LYS G 34 3.646 -11.264 54.099 1.00 17.11 C ANISOU 59 CB LYS G 34 2136 2227 2138 22 -53 -18 C ATOM 60 CG LYS G 34 5.049 -11.463 54.671 1.00 19.94 C ANISOU 60 CG LYS G 34 2516 2597 2462 0 32 -84 C ATOM 61 CD LYS G 34 5.381 -10.446 55.748 1.00 23.27 C ANISOU 61 CD LYS G 34 2984 2974 2881 -50 -67 -4 C ATOM 62 CE LYS G 34 5.657 -9.093 55.194 1.00 24.44 C ANISOU 62 CE LYS G 34 3068 3278 2940 -93 -67 44 C ATOM 63 NZ LYS G 34 6.802 -8.422 55.880 1.00 24.68 N ANISOU 63 NZ LYS G 34 2881 3736 2759 -201 -357 -344 N ATOM 64 N ALA G 35 1.342 -12.059 51.759 1.00 14.37 N ANISOU 64 N ALA G 35 1849 1841 1769 4 4 22 N ATOM 65 CA ALA G 35 0.013 -11.635 51.305 1.00 13.72 C ANISOU 65 CA ALA G 35 1758 1749 1704 40 31 9 C ATOM 66 C ALA G 35 -1.031 -12.733 51.467 1.00 13.83 C ANISOU 66 C ALA G 35 1785 1742 1724 51 -2 41 C ATOM 67 O ALA G 35 -0.813 -13.873 51.053 1.00 13.92 O ANISOU 67 O ALA G 35 1740 1734 1814 106 105 103 O ATOM 68 CB ALA G 35 0.054 -11.164 49.840 1.00 13.71 C ANISOU 68 CB ALA G 35 1763 1676 1770 93 19 9 C ATOM 69 N GLY G 36 -2.162 -12.375 52.074 1.00 13.73 N ANISOU 69 N GLY G 36 1781 1728 1705 56 21 70 N ATOM 70 CA GLY G 36 -3.367 -13.181 52.026 1.00 14.35 C ANISOU 70 CA GLY G 36 1851 1757 1845 55 -17 46 C ATOM 71 C GLY G 36 -3.283 -14.464 52.823 1.00 15.50 C ANISOU 71 C GLY G 36 1984 1934 1968 38 -22 73 C ATOM 72 O GLY G 36 -3.916 -15.458 52.461 1.00 15.44 O ANISOU 72 O GLY G 36 2078 1829 1958 102 -182 165 O ATOM 73 N LYS G 37 -2.497 -14.454 53.892 1.00 16.73 N ANISOU 73 N LYS G 37 2164 2086 2103 11 -24 10 N ATOM 74 CA LYS G 37 -2.319 -15.650 54.725 1.00 18.52 C ANISOU 74 CA LYS G 37 2355 2338 2344 14 0 26 C ATOM 75 C LYS G 37 -3.373 -15.787 55.820 1.00 18.83 C ANISOU 75 C LYS G 37 2398 2370 2383 0 11 6 C ATOM 76 O LYS G 37 -3.668 -16.883 56.245 1.00 18.85 O ANISOU 76 O LYS G 37 2398 2372 2392 -16 93 87 O ATOM 77 CB LYS G 37 -0.915 -15.672 55.335 1.00 19.15 C ANISOU 77 CB LYS G 37 2441 2398 2435 1 18 14 C ATOM 78 CG LYS G 37 0.198 -15.911 54.296 1.00 22.30 C ANISOU 78 CG LYS G 37 2806 2762 2905 46 1 93 C ATOM 79 CD LYS G 37 1.062 -17.136 54.648 1.00 28.06 C ANISOU 79 CD LYS G 37 3491 3505 3662 30 62 -96 C ATOM 80 CE LYS G 37 0.567 -18.408 53.955 1.00 30.37 C ANISOU 80 CE LYS G 37 3754 3827 3957 31 40 -141 C ATOM 81 NZ LYS G 37 1.677 -19.382 53.670 1.00 33.48 N ANISOU 81 NZ LYS G 37 4166 4322 4233 180 66 -128 N ATOM 82 N GLU G 38 -3.925 -14.670 56.280 1.00 19.73 N ANISOU 82 N GLU G 38 2479 2530 2488 3 0 29 N ATOM 83 CA GLU G 38 -4.950 -14.674 57.327 1.00 20.20 C ANISOU 83 CA GLU G 38 2573 2580 2520 -18 -20 6 C ATOM 84 C GLU G 38 -5.973 -13.578 56.997 1.00 19.09 C ANISOU 84 C GLU G 38 2458 2409 2385 -16 -39 -26 C ATOM 85 O GLU G 38 -5.694 -12.696 56.201 1.00 18.62 O ANISOU 85 O GLU G 38 2439 2307 2329 -42 -73 -13 O ATOM 86 CB GLU G 38 -4.316 -14.450 58.717 1.00 20.88 C ANISOU 86 CB GLU G 38 2697 2642 2594 -42 -3 3 C ATOM 87 CG GLU G 38 -3.734 -13.054 58.932 1.00 25.10 C ANISOU 87 CG GLU G 38 3123 3442 2972 -80 10 36 C ATOM 88 CD GLU G 38 -3.389 -12.733 60.384 1.00 30.81 C ANISOU 88 CD GLU G 38 3578 4458 3669 -128 62 -52 C ATOM 89 OE1 GLU G 38 -2.182 -12.493 60.672 1.00 34.44 O ANISOU 89 OE1 GLU G 38 3684 5288 4113 -179 96 -33 O ATOM 90 OE2 GLU G 38 -4.326 -12.694 61.239 1.00 34.73 O ANISOU 90 OE2 GLU G 38 4135 5054 4003 -134 22 -127 O ATOM 91 N PRO G 39 -7.151 -13.626 57.593 1.00 18.24 N ANISOU 91 N PRO G 39 2330 2302 2297 -24 -34 -6 N ATOM 92 CA PRO G 39 -8.129 -12.547 57.391 1.00 17.51 C ANISOU 92 CA PRO G 39 2269 2202 2182 -28 -44 35 C ATOM 93 C PRO G 39 -7.602 -11.197 57.867 1.00 16.39 C ANISOU 93 C PRO G 39 2122 2042 2060 -41 -28 75 C ATOM 94 O PRO G 39 -6.921 -11.140 58.890 1.00 15.13 O ANISOU 94 O PRO G 39 2046 1893 1810 -109 -127 272 O ATOM 95 CB PRO G 39 -9.337 -12.979 58.238 1.00 17.67 C ANISOU 95 CB PRO G 39 2247 2196 2269 -38 -3 28 C ATOM 96 CG PRO G 39 -9.132 -14.439 58.514 1.00 18.74 C ANISOU 96 CG PRO G 39 2341 2321 2457 24 -27 5 C ATOM 97 CD PRO G 39 -7.645 -14.666 58.511 1.00 18.95 C ANISOU 97 CD PRO G 39 2415 2332 2453 -13 -58 14 C ATOM 98 N GLY G 40 -7.914 -10.133 57.128 1.00 15.35 N ANISOU 98 N GLY G 40 2014 1913 1904 -25 -50 68 N ATOM 99 CA GLY G 40 -7.555 -8.777 57.519 1.00 14.81 C ANISOU 99 CA GLY G 40 1899 1858 1870 -3 -53 73 C ATOM 100 C GLY G 40 -7.312 -7.866 56.322 1.00 13.77 C ANISOU 100 C GLY G 40 1789 1697 1746 -16 -30 104 C ATOM 101 O GLY G 40 -7.652 -8.200 55.205 1.00 12.82 O ANISOU 101 O GLY G 40 1696 1600 1573 31 -105 216 O ATOM 102 N LEU G 41 -6.693 -6.723 56.572 1.00 13.78 N ANISOU 102 N LEU G 41 1770 1727 1739 33 -33 71 N ATOM 103 CA LEU G 41 -6.384 -5.723 55.537 1.00 13.24 C ANISOU 103 CA LEU G 41 1730 1591 1708 25 -40 63 C ATOM 104 C LEU G 41 -4.863 -5.595 55.415 1.00 11.99 C ANISOU 104 C LEU G 41 1593 1399 1564 52 -9 63 C ATOM 105 O LEU G 41 -4.166 -5.494 56.415 1.00 11.66 O ANISOU 105 O LEU G 41 1420 1434 1575 72 22 41 O ATOM 106 CB LEU G 41 -6.960 -4.368 55.968 1.00 14.21 C ANISOU 106 CB LEU G 41 1814 1723 1859 95 -127 69 C ATOM 107 CG LEU G 41 -7.733 -3.419 55.023 1.00 16.77 C ANISOU 107 CG LEU G 41 2253 1972 2146 -3 -99 79 C ATOM 108 CD1 LEU G 41 -7.385 -1.952 55.261 1.00 17.34 C ANISOU 108 CD1 LEU G 41 2172 2152 2264 -211 -75 179 C ATOM 109 CD2 LEU G 41 -7.656 -3.773 53.577 1.00 15.33 C ANISOU 109 CD2 LEU G 41 2269 1757 1799 95 302 242 C ATOM 110 N GLN G 42 -4.350 -5.601 54.195 1.00 11.10 N ANISOU 110 N GLN G 42 1486 1276 1453 68 -66 67 N ATOM 111 CA GLN G 42 -2.939 -5.332 53.950 1.00 10.45 C ANISOU 111 CA GLN G 42 1368 1249 1353 -6 -75 49 C ATOM 112 C GLN G 42 -2.780 -4.217 52.943 1.00 9.96 C ANISOU 112 C GLN G 42 1325 1147 1309 21 -98 67 C ATOM 113 O GLN G 42 -3.412 -4.239 51.919 1.00 9.68 O ANISOU 113 O GLN G 42 1465 903 1307 95 -89 169 O ATOM 114 CB GLN G 42 -2.232 -6.588 53.460 1.00 10.33 C ANISOU 114 CB GLN G 42 1383 1238 1302 -54 -57 37 C ATOM 115 CG GLN G 42 -2.160 -7.691 54.525 1.00 10.56 C ANISOU 115 CG GLN G 42 1399 1258 1353 -53 -202 -3 C ATOM 116 CD GLN G 42 -1.651 -9.006 53.967 1.00 11.93 C ANISOU 116 CD GLN G 42 1575 1465 1490 30 -249 -75 C ATOM 117 OE1 GLN G 42 -2.320 -9.619 53.138 1.00 10.98 O ANISOU 117 OE1 GLN G 42 1631 1048 1493 -18 -581 -279 O ATOM 118 NE2 GLN G 42 -0.485 -9.452 54.432 1.00 11.43 N ANISOU 118 NE2 GLN G 42 1258 1591 1492 -82 -366 -46 N ATOM 119 N ILE G 43 -1.906 -3.257 53.232 1.00 10.42 N ANISOU 119 N ILE G 43 1400 1203 1355 46 -91 85 N ATOM 120 CA ILE G 43 -1.671 -2.120 52.338 1.00 10.18 C ANISOU 120 CA ILE G 43 1310 1286 1271 0 -60 39 C ATOM 121 C ILE G 43 -0.188 -1.940 52.067 1.00 10.10 C ANISOU 121 C ILE G 43 1332 1224 1280 19 -76 0 C ATOM 122 O ILE G 43 0.630 -1.921 52.989 1.00 10.29 O ANISOU 122 O ILE G 43 1250 1281 1376 -48 -170 -136 O ATOM 123 CB ILE G 43 -2.280 -0.829 52.909 1.00 9.99 C ANISOU 123 CB ILE G 43 1324 1205 1264 -45 -70 65 C ATOM 124 CG1 ILE G 43 -3.763 -1.047 53.228 1.00 11.08 C ANISOU 124 CG1 ILE G 43 1434 1430 1343 143 -78 15 C ATOM 125 CG2 ILE G 43 -2.123 0.310 51.907 1.00 10.92 C ANISOU 125 CG2 ILE G 43 1305 1496 1346 -74 -10 70 C ATOM 126 CD1 ILE G 43 -4.535 0.208 53.611 1.00 12.91 C ANISOU 126 CD1 ILE G 43 1821 1436 1648 28 -28 0 C ATOM 127 N TRP G 44 0.136 -1.831 50.782 1.00 9.65 N ANISOU 127 N TRP G 44 1288 1188 1189 32 -60 -4 N ATOM 128 CA TRP G 44 1.468 -1.538 50.300 1.00 9.30 C ANISOU 128 CA TRP G 44 1212 1140 1181 41 -46 0 C ATOM 129 C TRP G 44 1.427 -0.277 49.445 1.00 9.60 C ANISOU 129 C TRP G 44 1231 1208 1207 36 -47 -5 C ATOM 130 O TRP G 44 0.420 0.031 48.821 1.00 9.64 O ANISOU 130 O TRP G 44 1311 1124 1225 150 -25 179 O ATOM 131 CB TRP G 44 1.970 -2.681 49.422 1.00 9.70 C ANISOU 131 CB TRP G 44 1282 1219 1183 -28 -71 -28 C ATOM 132 CG TRP G 44 2.080 -4.012 50.082 1.00 8.70 C ANISOU 132 CG TRP G 44 1103 1038 1163 -13 -84 -19 C ATOM 133 CD1 TRP G 44 3.164 -4.504 50.744 1.00 9.21 C ANISOU 133 CD1 TRP G 44 1216 1091 1190 -91 159 24 C ATOM 134 CD2 TRP G 44 1.093 -5.054 50.100 1.00 10.47 C ANISOU 134 CD2 TRP G 44 1311 1394 1272 57 12 69 C ATOM 135 NE1 TRP G 44 2.913 -5.779 51.177 1.00 9.34 N ANISOU 135 NE1 TRP G 44 1075 1204 1269 27 11 58 N ATOM 136 CE2 TRP G 44 1.648 -6.143 50.797 1.00 11.08 C ANISOU 136 CE2 TRP G 44 1365 1412 1430 30 63 105 C ATOM 137 CE3 TRP G 44 -0.206 -5.174 49.604 1.00 11.53 C ANISOU 137 CE3 TRP G 44 1428 1453 1498 -15 160 52 C ATOM 138 CZ2 TRP G 44 0.954 -7.344 51.006 1.00 11.77 C ANISOU 138 CZ2 TRP G 44 1338 1596 1536 -95 -2 250 C ATOM 139 CZ3 TRP G 44 -0.899 -6.361 49.815 1.00 14.18 C ANISOU 139 CZ3 TRP G 44 1573 1782 2031 78 92 117 C ATOM 140 CH2 TRP G 44 -0.323 -7.422 50.535 1.00 12.31 C ANISOU 140 CH2 TRP G 44 1690 1592 1395 -81 -63 228 C ATOM 141 N ARG G 45 2.538 0.434 49.422 1.00 9.39 N ANISOU 141 N ARG G 45 1173 1172 1220 40 -32 32 N ATOM 142 CA ARG G 45 2.704 1.599 48.606 1.00 9.78 C ANISOU 142 CA ARG G 45 1204 1240 1269 -17 -23 -8 C ATOM 143 C ARG G 45 3.731 1.290 47.554 1.00 9.28 C ANISOU 143 C ARG G 45 1101 1153 1270 -41 -1 0 C ATOM 144 O ARG G 45 4.717 0.654 47.841 1.00 8.83 O ANISOU 144 O ARG G 45 945 1052 1355 -141 -114 110 O ATOM 145 CB ARG G 45 3.174 2.781 49.448 1.00 9.20 C ANISOU 145 CB ARG G 45 1085 1206 1203 -28 -29 -49 C ATOM 146 CG ARG G 45 3.292 4.032 48.639 1.00 10.37 C ANISOU 146 CG ARG G 45 1351 1284 1302 -86 -28 -63 C ATOM 147 CD ARG G 45 3.497 5.329 49.448 1.00 11.52 C ANISOU 147 CD ARG G 45 1645 1385 1346 -15 -118 118 C ATOM 148 NE ARG G 45 4.779 5.329 50.120 1.00 11.74 N ANISOU 148 NE ARG G 45 1562 1311 1588 -208 6 67 N ATOM 149 CZ ARG G 45 5.372 6.402 50.630 1.00 12.47 C ANISOU 149 CZ ARG G 45 1633 1415 1689 -47 77 50 C ATOM 150 NH1 ARG G 45 4.839 7.601 50.503 1.00 14.83 N ANISOU 150 NH1 ARG G 45 2070 1608 1957 -76 49 -4 N ATOM 151 NH2 ARG G 45 6.520 6.276 51.245 1.00 12.82 N ANISOU 151 NH2 ARG G 45 1818 1404 1648 -260 -205 41 N ATOM 152 N VAL G 46 3.487 1.723 46.325 1.00 9.94 N ANISOU 152 N VAL G 46 1165 1252 1360 -55 -57 -17 N ATOM 153 CA VAL G 46 4.498 1.629 45.273 1.00 10.58 C ANISOU 153 CA VAL G 46 1345 1333 1340 -33 42 -28 C ATOM 154 C VAL G 46 5.627 2.637 45.571 1.00 11.30 C ANISOU 154 C VAL G 46 1459 1397 1438 -11 63 -3 C ATOM 155 O VAL G 46 5.385 3.823 45.756 1.00 12.59 O ANISOU 155 O VAL G 46 1683 1460 1638 -41 143 18 O ATOM 156 CB VAL G 46 3.899 1.859 43.879 1.00 10.75 C ANISOU 156 CB VAL G 46 1311 1329 1442 -47 46 -15 C ATOM 157 CG1 VAL G 46 4.989 1.864 42.822 1.00 11.24 C ANISOU 157 CG1 VAL G 46 1510 1472 1288 -75 46 -42 C ATOM 158 CG2 VAL G 46 2.878 0.768 43.542 1.00 11.76 C ANISOU 158 CG2 VAL G 46 1507 1489 1471 -63 44 -38 C ATOM 159 N GLU G 47 6.854 2.164 45.674 1.00 11.62 N ANISOU 159 N GLU G 47 1487 1458 1467 -5 8 -29 N ATOM 160 CA GLU G 47 7.981 3.058 45.907 1.00 12.47 C ANISOU 160 CA GLU G 47 1578 1610 1548 -5 -1 15 C ATOM 161 C GLU G 47 9.135 2.646 45.002 1.00 12.42 C ANISOU 161 C GLU G 47 1585 1614 1520 -31 -10 -33 C ATOM 162 O GLU G 47 9.795 1.639 45.218 1.00 11.74 O ANISOU 162 O GLU G 47 1312 1714 1433 32 -91 -26 O ATOM 163 CB GLU G 47 8.404 3.093 47.397 1.00 12.67 C ANISOU 163 CB GLU G 47 1596 1657 1560 14 4 39 C ATOM 164 CG GLU G 47 7.249 3.294 48.386 1.00 13.22 C ANISOU 164 CG GLU G 47 1810 1691 1519 111 29 16 C ATOM 165 CD GLU G 47 7.674 3.356 49.848 1.00 15.42 C ANISOU 165 CD GLU G 47 1958 2147 1752 73 176 55 C ATOM 166 OE1 GLU G 47 6.765 3.329 50.712 1.00 14.85 O ANISOU 166 OE1 GLU G 47 1831 2429 1382 239 196 87 O ATOM 167 OE2 GLU G 47 8.894 3.448 50.152 1.00 16.66 O ANISOU 167 OE2 GLU G 47 2099 2418 1812 22 518 6 O ATOM 168 N LYS G 48 9.351 3.449 43.972 1.00 13.36 N ANISOU 168 N LYS G 48 1691 1759 1627 -50 -12 -29 N ATOM 169 CA LYS G 48 10.439 3.239 43.017 1.00 13.98 C ANISOU 169 CA LYS G 48 1755 1799 1755 27 19 -28 C ATOM 170 C LYS G 48 10.505 1.800 42.512 1.00 13.20 C ANISOU 170 C LYS G 48 1671 1701 1641 -14 30 -16 C ATOM 171 O LYS G 48 11.490 1.060 42.690 1.00 12.61 O ANISOU 171 O LYS G 48 1528 1773 1490 55 35 -110 O ATOM 172 CB LYS G 48 11.737 3.770 43.595 1.00 15.02 C ANISOU 172 CB LYS G 48 1901 1867 1937 12 18 -16 C ATOM 173 CG LYS G 48 11.649 5.300 43.690 1.00 17.66 C ANISOU 173 CG LYS G 48 2177 2226 2305 83 -7 -33 C ATOM 174 CD LYS G 48 12.870 5.975 44.213 1.00 22.03 C ANISOU 174 CD LYS G 48 2748 2682 2939 -9 -41 5 C ATOM 175 CE LYS G 48 12.592 7.447 44.486 1.00 24.32 C ANISOU 175 CE LYS G 48 2971 2962 3307 -92 -43 -90 C ATOM 176 NZ LYS G 48 13.872 8.202 44.479 1.00 26.41 N ANISOU 176 NZ LYS G 48 3164 3055 3815 -290 -79 -6 N ATOM 177 N PHE G 49 9.391 1.405 41.923 1.00 12.22 N ANISOU 177 N PHE G 49 1571 1653 1418 55 -53 22 N ATOM 178 CA PHE G 49 9.248 0.096 41.270 1.00 11.98 C ANISOU 178 CA PHE G 49 1602 1451 1498 12 0 54 C ATOM 179 C PHE G 49 9.261 -1.101 42.253 1.00 11.94 C ANISOU 179 C PHE G 49 1593 1487 1454 63 -15 98 C ATOM 180 O PHE G 49 9.479 -2.236 41.849 1.00 11.17 O ANISOU 180 O PHE G 49 1692 1252 1299 16 -51 177 O ATOM 181 CB PHE G 49 10.330 -0.113 40.214 1.00 11.30 C ANISOU 181 CB PHE G 49 1543 1411 1339 65 43 43 C ATOM 182 CG PHE G 49 10.299 0.889 39.106 1.00 11.78 C ANISOU 182 CG PHE G 49 1609 1487 1380 35 38 -83 C ATOM 183 CD1 PHE G 49 11.383 1.703 38.873 1.00 11.75 C ANISOU 183 CD1 PHE G 49 1788 1381 1292 -66 27 -87 C ATOM 184 CD2 PHE G 49 9.191 0.989 38.268 1.00 12.34 C ANISOU 184 CD2 PHE G 49 1655 1636 1397 145 160 204 C ATOM 185 CE1 PHE G 49 11.360 2.620 37.852 1.00 13.09 C ANISOU 185 CE1 PHE G 49 1831 1608 1534 -67 -136 27 C ATOM 186 CE2 PHE G 49 9.176 1.914 37.235 1.00 12.78 C ANISOU 186 CE2 PHE G 49 1762 1446 1647 -5 -134 50 C ATOM 187 CZ PHE G 49 10.268 2.706 37.027 1.00 13.27 C ANISOU 187 CZ PHE G 49 1769 1612 1658 124 -56 337 C ATOM 188 N ASP G 50 9.001 -0.834 43.521 1.00 12.15 N ANISOU 188 N ASP G 50 1606 1513 1495 68 -4 80 N ATOM 189 CA ASP G 50 8.869 -1.892 44.515 1.00 12.68 C ANISOU 189 CA ASP G 50 1651 1545 1619 26 37 10 C ATOM 190 C ASP G 50 7.551 -1.752 45.280 1.00 12.85 C ANISOU 190 C ASP G 50 1592 1601 1688 20 26 17 C ATOM 191 O ASP G 50 6.914 -0.702 45.241 1.00 12.48 O ANISOU 191 O ASP G 50 1527 1550 1665 39 65 73 O ATOM 192 CB ASP G 50 10.050 -1.831 45.467 1.00 12.37 C ANISOU 192 CB ASP G 50 1580 1480 1640 -13 2 5 C ATOM 193 CG ASP G 50 10.223 -3.094 46.290 1.00 13.26 C ANISOU 193 CG ASP G 50 1847 1555 1633 -144 -8 2 C ATOM 194 OD1 ASP G 50 9.687 -4.169 45.945 1.00 13.04 O ANISOU 194 OD1 ASP G 50 1915 1197 1840 -220 234 -173 O ATOM 195 OD2 ASP G 50 10.896 -3.101 47.314 1.00 16.29 O ANISOU 195 OD2 ASP G 50 2220 1762 2206 -278 -55 142 O ATOM 196 N LEU G 51 7.158 -2.826 45.954 1.00 13.17 N ANISOU 196 N LEU G 51 1696 1646 1659 85 13 39 N ATOM 197 CA LEU G 51 5.951 -2.874 46.773 1.00 14.14 C ANISOU 197 CA LEU G 51 1843 1736 1791 77 7 58 C ATOM 198 C LEU G 51 6.394 -2.859 48.223 1.00 13.70 C ANISOU 198 C LEU G 51 1822 1700 1681 67 10 37 C ATOM 199 O LEU G 51 6.969 -3.839 48.701 1.00 13.73 O ANISOU 199 O LEU G 51 1936 1696 1584 155 -10 133 O ATOM 200 CB LEU G 51 5.230 -4.178 46.528 1.00 14.78 C ANISOU 200 CB LEU G 51 1949 1840 1824 90 -80 -68 C ATOM 201 CG LEU G 51 3.795 -4.335 46.092 1.00 18.68 C ANISOU 201 CG LEU G 51 2403 2249 2444 65 92 -74 C ATOM 202 CD1 LEU G 51 3.242 -5.537 46.846 1.00 22.05 C ANISOU 202 CD1 LEU G 51 2848 2990 2537 84 115 181 C ATOM 203 CD2 LEU G 51 2.939 -3.106 46.210 1.00 21.58 C ANISOU 203 CD2 LEU G 51 2616 2889 2692 129 32 -56 C ATOM 204 N VAL G 52 6.123 -1.770 48.923 1.00 13.57 N ANISOU 204 N VAL G 52 1781 1696 1678 65 36 116 N ATOM 205 CA VAL G 52 6.627 -1.566 50.265 1.00 13.07 C ANISOU 205 CA VAL G 52 1681 1655 1630 20 6 48 C ATOM 206 C VAL G 52 5.460 -1.490 51.251 1.00 12.78 C ANISOU 206 C VAL G 52 1651 1631 1571 22 33 61 C ATOM 207 O VAL G 52 4.567 -0.700 51.053 1.00 11.17 O ANISOU 207 O VAL G 52 1510 1424 1309 119 48 139 O ATOM 208 CB VAL G 52 7.421 -0.247 50.335 1.00 13.10 C ANISOU 208 CB VAL G 52 1665 1648 1665 37 26 103 C ATOM 209 CG1 VAL G 52 7.936 -0.018 51.725 1.00 13.60 C ANISOU 209 CG1 VAL G 52 1700 1706 1758 5 81 -4 C ATOM 210 CG2 VAL G 52 8.567 -0.272 49.331 1.00 13.47 C ANISOU 210 CG2 VAL G 52 1650 1732 1735 -40 21 138 C ATOM 211 N PRO G 53 5.465 -2.269 52.328 1.00 13.45 N ANISOU 211 N PRO G 53 1730 1721 1656 44 38 25 N ATOM 212 CA PRO G 53 4.327 -2.213 53.256 1.00 13.84 C ANISOU 212 CA PRO G 53 1738 1789 1732 16 24 43 C ATOM 213 C PRO G 53 4.158 -0.830 53.913 1.00 14.12 C ANISOU 213 C PRO G 53 1770 1858 1737 21 22 27 C ATOM 214 O PRO G 53 5.133 -0.154 54.267 1.00 14.07 O ANISOU 214 O PRO G 53 1619 2012 1712 12 -120 16 O ATOM 215 CB PRO G 53 4.639 -3.299 54.293 1.00 14.14 C ANISOU 215 CB PRO G 53 1782 1804 1784 46 69 91 C ATOM 216 CG PRO G 53 6.080 -3.641 54.145 1.00 14.42 C ANISOU 216 CG PRO G 53 1798 1824 1855 27 60 135 C ATOM 217 CD PRO G 53 6.494 -3.241 52.760 1.00 13.61 C ANISOU 217 CD PRO G 53 1811 1771 1586 33 60 12 C ATOM 218 N VAL G 54 2.910 -0.385 54.003 1.00 13.97 N ANISOU 218 N VAL G 54 1711 1849 1745 -5 1 57 N ATOM 219 CA VAL G 54 2.577 0.809 54.765 1.00 14.26 C ANISOU 219 CA VAL G 54 1815 1823 1777 40 15 6 C ATOM 220 C VAL G 54 2.568 0.441 56.259 1.00 15.15 C ANISOU 220 C VAL G 54 1884 1944 1927 59 -5 8 C ATOM 221 O VAL G 54 2.034 -0.598 56.622 1.00 15.28 O ANISOU 221 O VAL G 54 1889 2003 1911 124 -25 52 O ATOM 222 CB VAL G 54 1.191 1.348 54.350 1.00 14.34 C ANISOU 222 CB VAL G 54 1864 1812 1771 18 -18 -47 C ATOM 223 CG1 VAL G 54 0.725 2.499 55.276 1.00 15.05 C ANISOU 223 CG1 VAL G 54 1939 1901 1878 67 64 10 C ATOM 224 CG2 VAL G 54 1.229 1.817 52.920 1.00 13.07 C ANISOU 224 CG2 VAL G 54 1777 1590 1598 16 19 86 C ATOM 225 N PRO G 55 3.153 1.264 57.128 1.00 16.09 N ANISOU 225 N PRO G 55 2031 2098 1982 34 5 -16 N ATOM 226 CA PRO G 55 3.039 1.027 58.571 1.00 17.17 C ANISOU 226 CA PRO G 55 2177 2214 2132 1 11 -46 C ATOM 227 C PRO G 55 1.578 0.954 58.990 1.00 17.43 C ANISOU 227 C PRO G 55 2233 2247 2141 14 20 -73 C ATOM 228 O PRO G 55 0.777 1.771 58.546 1.00 16.74 O ANISOU 228 O PRO G 55 2277 2155 1927 17 128 -142 O ATOM 229 CB PRO G 55 3.704 2.263 59.189 1.00 17.34 C ANISOU 229 CB PRO G 55 2204 2216 2165 13 27 -81 C ATOM 230 CG PRO G 55 4.580 2.786 58.166 1.00 17.34 C ANISOU 230 CG PRO G 55 2193 2210 2182 16 17 6 C ATOM 231 CD PRO G 55 3.984 2.439 56.836 1.00 16.33 C ANISOU 231 CD PRO G 55 2097 2070 2035 34 -44 -63 C ATOM 232 N THR G 56 1.247 -0.024 59.816 1.00 18.19 N ANISOU 232 N THR G 56 2340 2313 2256 16 19 -25 N ATOM 233 CA THR G 56 -0.126 -0.307 60.204 1.00 20.17 C ANISOU 233 CA THR G 56 2578 2517 2569 49 24 -13 C ATOM 234 C THR G 56 -0.866 0.904 60.806 1.00 20.52 C ANISOU 234 C THR G 56 2597 2572 2628 45 16 -24 C ATOM 235 O THR G 56 -2.067 1.086 60.576 1.00 21.03 O ANISOU 235 O THR G 56 2666 2588 2736 119 14 -89 O ATOM 236 CB THR G 56 -0.109 -1.512 61.172 1.00 20.57 C ANISOU 236 CB THR G 56 2568 2503 2743 -16 155 -17 C ATOM 237 OG1 THR G 56 0.155 -2.698 60.406 1.00 22.68 O ANISOU 237 OG1 THR G 56 2902 2673 3039 -71 146 74 O ATOM 238 CG2 THR G 56 -1.463 -1.773 61.754 1.00 23.65 C ANISOU 238 CG2 THR G 56 3037 2910 3038 64 85 -45 C ATOM 239 N ASN G 57 -0.149 1.743 61.547 1.00 21.02 N ANISOU 239 N ASN G 57 2667 2622 2695 89 -5 -11 N ATOM 240 CA ASN G 57 -0.773 2.900 62.184 1.00 21.57 C ANISOU 240 CA ASN G 57 2721 2715 2757 55 -25 -46 C ATOM 241 C ASN G 57 -1.118 4.039 61.193 1.00 20.56 C ANISOU 241 C ASN G 57 2616 2570 2626 100 -13 -14 C ATOM 242 O ASN G 57 -1.809 4.963 61.572 1.00 20.68 O ANISOU 242 O ASN G 57 2657 2581 2618 231 -69 -81 O ATOM 243 CB ASN G 57 0.076 3.406 63.358 1.00 22.86 C ANISOU 243 CB ASN G 57 2839 2854 2992 85 6 -60 C ATOM 244 CG ASN G 57 1.301 4.187 62.913 1.00 24.86 C ANISOU 244 CG ASN G 57 2921 3152 3370 25 97 -308 C ATOM 245 OD1 ASN G 57 2.097 3.711 62.114 1.00 29.15 O ANISOU 245 OD1 ASN G 57 3375 4107 3591 114 5 -691 O ATOM 246 ND2 ASN G 57 1.457 5.392 63.443 1.00 29.69 N ANISOU 246 ND2 ASN G 57 3211 3991 4080 -82 18 -641 N ATOM 247 N LEU G 58 -0.649 3.949 59.942 1.00 19.10 N ANISOU 247 N LEU G 58 2445 2421 2391 84 -22 -42 N ATOM 248 CA LEU G 58 -0.936 4.943 58.897 1.00 18.16 C ANISOU 248 CA LEU G 58 2330 2310 2259 43 28 -30 C ATOM 249 C LEU G 58 -1.959 4.447 57.870 1.00 16.86 C ANISOU 249 C LEU G 58 2161 2164 2080 86 56 -7 C ATOM 250 O LEU G 58 -2.163 5.091 56.838 1.00 16.56 O ANISOU 250 O LEU G 58 2176 2157 1958 55 175 -46 O ATOM 251 CB LEU G 58 0.362 5.342 58.177 1.00 18.84 C ANISOU 251 CB LEU G 58 2447 2362 2347 47 -38 -38 C ATOM 252 CG LEU G 58 1.431 6.102 58.990 1.00 21.80 C ANISOU 252 CG LEU G 58 2713 2752 2817 66 22 -41 C ATOM 253 CD1 LEU G 58 2.697 6.331 58.186 1.00 22.83 C ANISOU 253 CD1 LEU G 58 2931 2873 2868 38 44 94 C ATOM 254 CD2 LEU G 58 0.918 7.440 59.518 1.00 23.56 C ANISOU 254 CD2 LEU G 58 3030 2796 3123 2 -50 -180 C ATOM 255 N TYR G 59 -2.617 3.325 58.143 1.00 15.53 N ANISOU 255 N TYR G 59 2020 1990 1889 81 26 27 N ATOM 256 CA TYR G 59 -3.629 2.792 57.231 1.00 15.15 C ANISOU 256 CA TYR G 59 1957 1971 1827 38 35 5 C ATOM 257 C TYR G 59 -4.784 3.780 57.079 1.00 15.41 C ANISOU 257 C TYR G 59 1997 2005 1851 50 22 0 C ATOM 258 O TYR G 59 -5.307 4.282 58.050 1.00 14.84 O ANISOU 258 O TYR G 59 2021 2088 1530 138 108 -108 O ATOM 259 CB TYR G 59 -4.172 1.444 57.705 1.00 15.07 C ANISOU 259 CB TYR G 59 1894 1999 1830 68 -24 36 C ATOM 260 CG TYR G 59 -3.380 0.209 57.305 1.00 13.83 C ANISOU 260 CG TYR G 59 1796 1794 1665 -3 38 -54 C ATOM 261 CD1 TYR G 59 -2.047 0.283 56.896 1.00 13.97 C ANISOU 261 CD1 TYR G 59 1736 1706 1865 -62 -92 -45 C ATOM 262 CD2 TYR G 59 -3.964 -1.040 57.379 1.00 14.16 C ANISOU 262 CD2 TYR G 59 1680 1848 1848 25 -85 -40 C ATOM 263 CE1 TYR G 59 -1.332 -0.862 56.553 1.00 13.56 C ANISOU 263 CE1 TYR G 59 1698 1721 1734 22 18 -33 C ATOM 264 CE2 TYR G 59 -3.270 -2.183 57.030 1.00 14.32 C ANISOU 264 CE2 TYR G 59 1722 1760 1957 46 -2 83 C ATOM 265 CZ TYR G 59 -1.956 -2.098 56.612 1.00 14.57 C ANISOU 265 CZ TYR G 59 1777 1795 1964 162 -171 90 C ATOM 266 OH TYR G 59 -1.285 -3.264 56.266 1.00 14.16 O ANISOU 266 OH TYR G 59 1840 2033 1506 261 -518 -101 O ATOM 267 N GLY G 60 -5.179 4.062 55.847 1.00 15.79 N ANISOU 267 N GLY G 60 2021 2033 1943 41 -6 -20 N ATOM 268 CA GLY G 60 -6.233 5.031 55.603 1.00 16.08 C ANISOU 268 CA GLY G 60 2005 2059 2043 19 -20 5 C ATOM 269 C GLY G 60 -5.827 6.465 55.313 1.00 16.34 C ANISOU 269 C GLY G 60 2037 2080 2089 17 -37 37 C ATOM 270 O GLY G 60 -6.689 7.242 54.903 1.00 16.57 O ANISOU 270 O GLY G 60 1967 2069 2259 29 -107 126 O ATOM 271 N ASP G 61 -4.554 6.820 55.530 1.00 16.28 N ANISOU 271 N ASP G 61 2020 2140 2022 61 -29 50 N ATOM 272 CA ASP G 61 -4.017 8.139 55.184 1.00 16.61 C ANISOU 272 CA ASP G 61 2038 2241 2028 35 -2 1 C ATOM 273 C ASP G 61 -3.251 8.002 53.878 1.00 16.03 C ANISOU 273 C ASP G 61 1949 2207 1934 75 26 21 C ATOM 274 O ASP G 61 -2.080 7.610 53.915 1.00 16.48 O ANISOU 274 O ASP G 61 1910 2459 1890 236 -21 108 O ATOM 275 CB ASP G 61 -3.010 8.638 56.236 1.00 17.42 C ANISOU 275 CB ASP G 61 2120 2401 2098 59 70 10 C ATOM 276 CG ASP G 61 -3.640 8.950 57.578 1.00 20.61 C ANISOU 276 CG ASP G 61 2443 2996 2391 46 -29 -140 C ATOM 277 OD1 ASP G 61 -4.891 9.043 57.677 1.00 24.85 O ANISOU 277 OD1 ASP G 61 2696 4022 2722 161 73 -246 O ATOM 278 OD2 ASP G 61 -2.936 9.119 58.601 1.00 25.62 O ANISOU 278 OD2 ASP G 61 2804 3904 3025 34 -36 -278 O ATOM 279 N PHE G 62 -3.876 8.326 52.740 1.00 14.36 N ANISOU 279 N PHE G 62 1769 1911 1775 74 20 46 N ATOM 280 CA PHE G 62 -3.237 8.129 51.431 1.00 13.52 C ANISOU 280 CA PHE G 62 1729 1717 1689 20 0 36 C ATOM 281 C PHE G 62 -2.615 9.398 50.860 1.00 13.08 C ANISOU 281 C PHE G 62 1610 1704 1653 -8 23 18 C ATOM 282 O PHE G 62 -3.281 10.438 50.763 1.00 12.61 O ANISOU 282 O PHE G 62 1572 1662 1554 -34 -50 86 O ATOM 283 CB PHE G 62 -4.257 7.590 50.429 1.00 13.24 C ANISOU 283 CB PHE G 62 1747 1638 1644 -24 66 38 C ATOM 284 CG PHE G 62 -4.737 6.214 50.746 1.00 13.55 C ANISOU 284 CG PHE G 62 1823 1636 1687 -54 88 -28 C ATOM 285 CD1 PHE G 62 -5.875 6.016 51.520 1.00 12.27 C ANISOU 285 CD1 PHE G 62 1571 1347 1744 -152 114 82 C ATOM 286 CD2 PHE G 62 -4.055 5.120 50.280 1.00 13.17 C ANISOU 286 CD2 PHE G 62 1703 1420 1879 7 391 119 C ATOM 287 CE1 PHE G 62 -6.314 4.738 51.798 1.00 13.70 C ANISOU 287 CE1 PHE G 62 1727 1669 1807 22 74 102 C ATOM 288 CE2 PHE G 62 -4.500 3.834 50.558 1.00 14.87 C ANISOU 288 CE2 PHE G 62 1940 1656 2053 -31 253 -92 C ATOM 289 CZ PHE G 62 -5.625 3.649 51.311 1.00 12.71 C ANISOU 289 CZ PHE G 62 1688 1471 1670 -138 178 -1 C ATOM 290 N PHE G 63 -1.338 9.303 50.479 1.00 12.77 N ANISOU 290 N PHE G 63 1622 1658 1569 18 -38 -2 N ATOM 291 CA PHE G 63 -0.651 10.351 49.729 1.00 11.99 C ANISOU 291 CA PHE G 63 1513 1499 1541 -30 -12 -13 C ATOM 292 C PHE G 63 -1.217 10.465 48.314 1.00 11.26 C ANISOU 292 C PHE G 63 1446 1410 1423 -8 12 -34 C ATOM 293 O PHE G 63 -1.196 9.495 47.567 1.00 11.87 O ANISOU 293 O PHE G 63 1553 1499 1456 -9 -33 -3 O ATOM 294 CB PHE G 63 0.844 10.028 49.626 1.00 12.37 C ANISOU 294 CB PHE G 63 1628 1527 1542 -6 -8 -45 C ATOM 295 CG PHE G 63 1.652 10.436 50.839 1.00 14.00 C ANISOU 295 CG PHE G 63 1712 1788 1819 12 -53 19 C ATOM 296 CD1 PHE G 63 2.391 9.498 51.540 1.00 15.28 C ANISOU 296 CD1 PHE G 63 2060 1951 1794 -57 98 16 C ATOM 297 CD2 PHE G 63 1.717 11.769 51.241 1.00 14.84 C ANISOU 297 CD2 PHE G 63 1914 2054 1670 2 -60 -137 C ATOM 298 CE1 PHE G 63 3.168 9.868 52.623 1.00 15.80 C ANISOU 298 CE1 PHE G 63 2000 2143 1858 -101 23 -110 C ATOM 299 CE2 PHE G 63 2.476 12.140 52.338 1.00 16.60 C ANISOU 299 CE2 PHE G 63 2014 2193 2100 -38 2 1 C ATOM 300 CZ PHE G 63 3.204 11.193 53.023 1.00 16.00 C ANISOU 300 CZ PHE G 63 2141 2012 1924 -60 36 51 C ATOM 301 N THR G 64 -1.695 11.643 47.926 1.00 10.74 N ANISOU 301 N THR G 64 1407 1388 1284 -45 33 -28 N ATOM 302 CA THR G 64 -2.351 11.786 46.627 1.00 10.60 C ANISOU 302 CA THR G 64 1358 1322 1345 -9 -15 -70 C ATOM 303 C THR G 64 -1.333 11.815 45.489 1.00 10.39 C ANISOU 303 C THR G 64 1312 1346 1288 -38 13 -29 C ATOM 304 O THR G 64 -1.696 11.666 44.326 1.00 9.72 O ANISOU 304 O THR G 64 1294 1267 1130 11 70 20 O ATOM 305 CB THR G 64 -3.263 13.005 46.577 1.00 10.90 C ANISOU 305 CB THR G 64 1356 1419 1365 -40 15 -62 C ATOM 306 OG1 THR G 64 -2.543 14.200 46.909 1.00 9.57 O ANISOU 306 OG1 THR G 64 1253 924 1457 158 -120 -397 O ATOM 307 CG2 THR G 64 -4.338 12.904 47.639 1.00 12.31 C ANISOU 307 CG2 THR G 64 1587 1697 1393 -54 -98 -146 C ATOM 308 N GLY G 65 -0.055 11.947 45.835 1.00 10.68 N ANISOU 308 N GLY G 65 1361 1391 1306 -35 -6 -72 N ATOM 309 CA GLY G 65 1.019 11.834 44.862 1.00 10.45 C ANISOU 309 CA GLY G 65 1296 1381 1292 -35 1 -51 C ATOM 310 C GLY G 65 1.485 10.408 44.608 1.00 11.01 C ANISOU 310 C GLY G 65 1380 1484 1319 -44 -6 -47 C ATOM 311 O GLY G 65 2.438 10.200 43.840 1.00 10.93 O ANISOU 311 O GLY G 65 1315 1562 1275 28 -19 -159 O ATOM 312 N ASP G 66 0.830 9.430 45.244 1.00 11.32 N ANISOU 312 N ASP G 66 1430 1518 1350 -61 -18 -100 N ATOM 313 CA ASP G 66 1.230 8.029 45.163 1.00 11.03 C ANISOU 313 CA ASP G 66 1369 1448 1370 13 0 -21 C ATOM 314 C ASP G 66 0.140 7.040 44.746 1.00 10.55 C ANISOU 314 C ASP G 66 1366 1391 1250 29 -9 -39 C ATOM 315 O ASP G 66 -1.024 7.379 44.617 1.00 10.02 O ANISOU 315 O ASP G 66 1381 1280 1146 -2 -153 77 O ATOM 316 CB ASP G 66 1.823 7.601 46.509 1.00 11.03 C ANISOU 316 CB ASP G 66 1402 1510 1275 -56 64 -134 C ATOM 317 CG ASP G 66 3.181 8.244 46.774 1.00 12.99 C ANISOU 317 CG ASP G 66 1659 1838 1436 -60 49 -196 C ATOM 318 OD1 ASP G 66 3.518 8.423 47.968 1.00 13.35 O ANISOU 318 OD1 ASP G 66 1548 2304 1219 -30 -209 -316 O ATOM 319 OD2 ASP G 66 3.976 8.606 45.859 1.00 12.04 O ANISOU 319 OD2 ASP G 66 1923 1545 1103 -370 303 -285 O ATOM 320 N ALA G 67 0.564 5.800 44.546 1.00 10.36 N ANISOU 320 N ALA G 67 1359 1299 1279 15 3 -7 N ATOM 321 CA ALA G 67 -0.306 4.690 44.197 1.00 10.20 C ANISOU 321 CA ALA G 67 1308 1341 1225 38 -3 8 C ATOM 322 C ALA G 67 -0.040 3.573 45.189 1.00 9.41 C ANISOU 322 C ALA G 67 1221 1161 1195 79 11 30 C ATOM 323 O ALA G 67 1.101 3.385 45.618 1.00 9.71 O ANISOU 323 O ALA G 67 1213 1314 1161 25 14 154 O ATOM 324 CB ALA G 67 -0.011 4.221 42.780 1.00 10.74 C ANISOU 324 CB ALA G 67 1389 1385 1306 77 70 -51 C ATOM 325 N TYR G 68 -1.097 2.871 45.558 1.00 8.84 N ANISOU 325 N TYR G 68 1125 1076 1155 92 -9 19 N ATOM 326 CA TYR G 68 -1.089 1.845 46.596 1.00 9.31 C ANISOU 326 CA TYR G 68 1225 1146 1165 7 -7 -12 C ATOM 327 C TYR G 68 -1.818 0.578 46.115 1.00 9.47 C ANISOU 327 C TYR G 68 1260 1139 1198 -31 -66 37 C ATOM 328 O TYR G 68 -2.667 0.631 45.209 1.00 9.49 O ANISOU 328 O TYR G 68 1392 1054 1159 -97 -76 41 O ATOM 329 CB TYR G 68 -1.817 2.347 47.849 1.00 9.86 C ANISOU 329 CB TYR G 68 1318 1179 1248 -27 -18 10 C ATOM 330 CG TYR G 68 -1.202 3.548 48.586 1.00 9.18 C ANISOU 330 CG TYR G 68 1245 927 1316 -64 31 -40 C ATOM 331 CD1 TYR G 68 -1.264 4.832 48.052 1.00 9.07 C ANISOU 331 CD1 TYR G 68 1363 839 1242 -190 34 85 C ATOM 332 CD2 TYR G 68 -0.642 3.397 49.851 1.00 6.14 C ANISOU 332 CD2 TYR G 68 901 551 878 -169 -97 140 C ATOM 333 CE1 TYR G 68 -0.719 5.927 48.749 1.00 10.69 C ANISOU 333 CE1 TYR G 68 1471 997 1591 115 -122 -12 C ATOM 334 CE2 TYR G 68 -0.123 4.481 50.561 1.00 9.25 C ANISOU 334 CE2 TYR G 68 1267 991 1254 30 46 139 C ATOM 335 CZ TYR G 68 -0.159 5.747 50.010 1.00 9.60 C ANISOU 335 CZ TYR G 68 1401 901 1343 -2 -128 60 C ATOM 336 OH TYR G 68 0.363 6.831 50.711 1.00 9.51 O ANISOU 336 OH TYR G 68 990 893 1729 86 87 8 O ATOM 337 N VAL G 69 -1.494 -0.542 46.759 1.00 9.29 N ANISOU 337 N VAL G 69 1195 1173 1161 -20 -1 -20 N ATOM 338 CA VAL G 69 -2.135 -1.819 46.554 1.00 9.26 C ANISOU 338 CA VAL G 69 1229 1151 1136 -47 12 -12 C ATOM 339 C VAL G 69 -2.686 -2.300 47.893 1.00 9.14 C ANISOU 339 C VAL G 69 1241 1124 1106 -45 -25 29 C ATOM 340 O VAL G 69 -1.988 -2.258 48.916 1.00 9.14 O ANISOU 340 O VAL G 69 1171 1157 1142 -93 51 80 O ATOM 341 CB VAL G 69 -1.145 -2.853 45.976 1.00 9.76 C ANISOU 341 CB VAL G 69 1265 1155 1285 -58 1 39 C ATOM 342 CG1 VAL G 69 -1.807 -4.198 45.828 1.00 12.20 C ANISOU 342 CG1 VAL G 69 1792 1367 1474 -41 -82 0 C ATOM 343 CG2 VAL G 69 -0.649 -2.406 44.609 1.00 9.85 C ANISOU 343 CG2 VAL G 69 1370 1234 1139 -51 17 -82 C ATOM 344 N ILE G 70 -3.944 -2.713 47.880 1.00 8.37 N ANISOU 344 N ILE G 70 1099 1103 975 -72 -1 26 N ATOM 345 CA ILE G 70 -4.686 -3.094 49.080 1.00 9.53 C ANISOU 345 CA ILE G 70 1220 1218 1182 -34 -46 5 C ATOM 346 C ILE G 70 -5.279 -4.489 48.867 1.00 9.77 C ANISOU 346 C ILE G 70 1259 1275 1177 -78 -49 53 C ATOM 347 O ILE G 70 -5.927 -4.730 47.858 1.00 11.22 O ANISOU 347 O ILE G 70 1502 1448 1311 -193 -71 104 O ATOM 348 CB ILE G 70 -5.810 -2.050 49.350 1.00 8.94 C ANISOU 348 CB ILE G 70 1136 1188 1072 -12 -2 12 C ATOM 349 CG1 ILE G 70 -5.202 -0.666 49.571 1.00 9.23 C ANISOU 349 CG1 ILE G 70 1112 1326 1069 98 11 58 C ATOM 350 CG2 ILE G 70 -6.690 -2.463 50.562 1.00 9.74 C ANISOU 350 CG2 ILE G 70 1295 1142 1263 85 -60 -20 C ATOM 351 CD1 ILE G 70 -5.059 0.189 48.352 1.00 10.00 C ANISOU 351 CD1 ILE G 70 1151 1322 1326 74 146 107 C ATOM 352 N LEU G 71 -5.035 -5.407 49.797 1.00 9.86 N ANISOU 352 N LEU G 71 1229 1269 1245 -41 -13 29 N ATOM 353 CA LEU G 71 -5.627 -6.723 49.737 1.00 9.67 C ANISOU 353 CA LEU G 71 1223 1266 1185 -35 -46 32 C ATOM 354 C LEU G 71 -6.483 -6.890 50.966 1.00 9.62 C ANISOU 354 C LEU G 71 1204 1279 1169 -40 12 1 C ATOM 355 O LEU G 71 -5.974 -6.831 52.102 1.00 8.24 O ANISOU 355 O LEU G 71 1061 1131 937 -211 -85 271 O ATOM 356 CB LEU G 71 -4.551 -7.834 49.699 1.00 9.60 C ANISOU 356 CB LEU G 71 1164 1326 1157 45 -14 -16 C ATOM 357 CG LEU G 71 -5.055 -9.281 49.775 1.00 8.62 C ANISOU 357 CG LEU G 71 1104 1184 985 -30 -46 100 C ATOM 358 CD1 LEU G 71 -5.881 -9.698 48.572 1.00 10.12 C ANISOU 358 CD1 LEU G 71 1067 1481 1297 -114 39 110 C ATOM 359 CD2 LEU G 71 -3.917 -10.270 49.948 1.00 9.39 C ANISOU 359 CD2 LEU G 71 954 1325 1288 -46 86 -223 C ATOM 360 N LYS G 72 -7.782 -7.064 50.749 1.00 10.03 N ANISOU 360 N LYS G 72 1282 1374 1151 -50 -85 -44 N ATOM 361 CA LYS G 72 -8.697 -7.437 51.818 1.00 10.99 C ANISOU 361 CA LYS G 72 1383 1462 1328 -31 -6 -15 C ATOM 362 C LYS G 72 -8.946 -8.952 51.759 1.00 11.31 C ANISOU 362 C LYS G 72 1466 1495 1334 14 -36 -30 C ATOM 363 O LYS G 72 -9.403 -9.484 50.740 1.00 10.82 O ANISOU 363 O LYS G 72 1444 1535 1132 -30 -49 22 O ATOM 364 CB LYS G 72 -10.021 -6.645 51.721 1.00 11.06 C ANISOU 364 CB LYS G 72 1448 1494 1258 28 -28 -21 C ATOM 365 CG LYS G 72 -11.063 -7.006 52.825 1.00 13.57 C ANISOU 365 CG LYS G 72 1570 1760 1826 -70 2 -34 C ATOM 366 CD LYS G 72 -10.634 -6.475 54.209 1.00 15.83 C ANISOU 366 CD LYS G 72 2010 2129 1876 -45 105 -28 C ATOM 367 CE LYS G 72 -11.558 -6.880 55.373 1.00 18.53 C ANISOU 367 CE LYS G 72 2217 2220 2604 -74 47 -106 C ATOM 368 NZ LYS G 72 -12.975 -6.775 55.026 1.00 19.44 N ANISOU 368 NZ LYS G 72 2029 2546 2811 232 75 -21 N ATOM 369 N THR G 73 -8.624 -9.632 52.860 1.00 11.42 N ANISOU 369 N THR G 73 1509 1524 1302 -29 -13 -23 N ATOM 370 CA THR G 73 -8.787 -11.066 53.002 1.00 11.82 C ANISOU 370 CA THR G 73 1549 1549 1392 -6 10 -41 C ATOM 371 C THR G 73 -9.920 -11.359 53.998 1.00 12.45 C ANISOU 371 C THR G 73 1593 1599 1536 -36 26 -13 C ATOM 372 O THR G 73 -9.853 -10.947 55.165 1.00 11.29 O ANISOU 372 O THR G 73 1488 1383 1418 -94 38 -195 O ATOM 373 CB THR G 73 -7.481 -11.730 53.477 1.00 11.83 C ANISOU 373 CB THR G 73 1510 1527 1456 -23 -10 -7 C ATOM 374 OG1 THR G 73 -6.417 -11.490 52.546 1.00 10.74 O ANISOU 374 OG1 THR G 73 1445 1413 1221 15 3 -12 O ATOM 375 CG2 THR G 73 -7.626 -13.272 53.462 1.00 12.80 C ANISOU 375 CG2 THR G 73 1655 1686 1520 57 92 -44 C ATOM 376 N VAL G 74 -10.949 -12.067 53.532 1.00 13.29 N ANISOU 376 N VAL G 74 1742 1660 1645 -37 -23 -44 N ATOM 377 CA VAL G 74 -12.115 -12.417 54.346 1.00 14.47 C ANISOU 377 CA VAL G 74 1843 1836 1819 -27 1 -19 C ATOM 378 C VAL G 74 -12.183 -13.938 54.541 1.00 16.10 C ANISOU 378 C VAL G 74 2057 2053 2005 -20 -19 -6 C ATOM 379 O VAL G 74 -12.046 -14.709 53.587 1.00 15.19 O ANISOU 379 O VAL G 74 2064 1870 1838 -39 -162 -40 O ATOM 380 CB VAL G 74 -13.433 -11.922 53.669 1.00 14.69 C ANISOU 380 CB VAL G 74 1894 1867 1820 9 49 -6 C ATOM 381 CG1 VAL G 74 -14.689 -12.373 54.441 1.00 15.28 C ANISOU 381 CG1 VAL G 74 1924 1830 2050 -80 -21 40 C ATOM 382 CG2 VAL G 74 -13.429 -10.418 53.542 1.00 15.58 C ANISOU 382 CG2 VAL G 74 1834 2077 2008 -55 45 -103 C ATOM 383 N GLN G 75 -12.367 -14.350 55.793 1.00 17.62 N ANISOU 383 N GLN G 75 2295 2214 2186 -50 -31 37 N ATOM 384 CA GLN G 75 -12.599 -15.733 56.163 1.00 19.71 C ANISOU 384 CA GLN G 75 2539 2459 2489 -40 -13 26 C ATOM 385 C GLN G 75 -14.028 -16.131 55.849 1.00 19.97 C ANISOU 385 C GLN G 75 2568 2448 2568 -82 26 94 C ATOM 386 O GLN G 75 -14.941 -15.682 56.521 1.00 20.17 O ANISOU 386 O GLN G 75 2576 2330 2756 -170 104 50 O ATOM 387 CB GLN G 75 -12.391 -15.906 57.676 1.00 20.59 C ANISOU 387 CB GLN G 75 2663 2559 2598 -49 -29 101 C ATOM 388 CG GLN G 75 -12.587 -17.322 58.188 1.00 23.10 C ANISOU 388 CG GLN G 75 2852 2834 3090 11 -41 83 C ATOM 389 CD GLN G 75 -11.443 -18.225 57.808 1.00 25.82 C ANISOU 389 CD GLN G 75 3093 3307 3409 74 74 51 C ATOM 390 OE1 GLN G 75 -10.409 -18.245 58.489 1.00 28.56 O ANISOU 390 OE1 GLN G 75 3145 3713 3991 377 -131 452 O ATOM 391 NE2 GLN G 75 -11.619 -18.982 56.733 1.00 26.63 N ANISOU 391 NE2 GLN G 75 3359 3346 3410 32 257 245 N ATOM 392 N LEU G 76 -14.214 -16.984 54.849 1.00 20.38 N ANISOU 392 N LEU G 76 2685 2508 2550 -102 14 108 N ATOM 393 CA LEU G 76 -15.530 -17.530 54.547 1.00 21.57 C ANISOU 393 CA LEU G 76 2764 2712 2718 -76 11 92 C ATOM 394 C LEU G 76 -15.855 -18.646 55.555 1.00 22.40 C ANISOU 394 C LEU G 76 2859 2746 2905 -105 -25 108 C ATOM 395 O LEU G 76 -14.953 -19.242 56.148 1.00 21.27 O ANISOU 395 O LEU G 76 2674 2616 2788 -220 -120 285 O ATOM 396 CB LEU G 76 -15.579 -18.098 53.124 1.00 21.91 C ANISOU 396 CB LEU G 76 2819 2751 2756 -77 -33 72 C ATOM 397 CG LEU G 76 -16.007 -17.229 51.923 1.00 23.12 C ANISOU 397 CG LEU G 76 2959 2890 2936 -64 6 21 C ATOM 398 CD1 LEU G 76 -16.082 -15.746 52.201 1.00 24.55 C ANISOU 398 CD1 LEU G 76 3076 3138 3111 -103 -17 71 C ATOM 399 CD2 LEU G 76 -15.088 -17.525 50.745 1.00 23.39 C ANISOU 399 CD2 LEU G 76 2891 2991 3003 -82 6 132 C ATOM 400 N ARG G 77 -17.145 -18.917 55.733 1.00 23.25 N ANISOU 400 N ARG G 77 2915 2888 3029 -68 9 113 N ATOM 401 CA ARG G 77 -17.602 -20.005 56.616 1.00 24.76 C ANISOU 401 CA ARG G 77 3064 3115 3226 -29 3 44 C ATOM 402 C ARG G 77 -17.122 -21.402 56.179 1.00 24.30 C ANISOU 402 C ARG G 77 2998 3037 3197 -36 0 48 C ATOM 403 O ARG G 77 -16.916 -22.276 57.010 1.00 24.94 O ANISOU 403 O ARG G 77 2946 3099 3429 -51 2 128 O ATOM 404 CB ARG G 77 -19.120 -19.995 56.712 1.00 25.13 C ANISOU 404 CB ARG G 77 3092 3183 3270 -70 20 39 C ATOM 405 CG ARG G 77 -19.680 -18.831 57.468 1.00 27.51 C ANISOU 405 CG ARG G 77 3426 3415 3610 -20 11 5 C ATOM 406 CD ARG G 77 -21.190 -18.752 57.388 1.00 32.05 C ANISOU 406 CD ARG G 77 4036 3972 4166 20 -29 -48 C ATOM 407 NE ARG G 77 -21.695 -17.458 57.831 1.00 36.94 N ANISOU 407 NE ARG G 77 4487 4667 4882 77 -51 -95 N ATOM 408 CZ ARG G 77 -22.948 -17.014 57.654 1.00 41.14 C ANISOU 408 CZ ARG G 77 5095 5166 5370 97 -74 -105 C ATOM 409 NH1 ARG G 77 -23.873 -17.767 57.035 1.00 41.32 N ANISOU 409 NH1 ARG G 77 5140 5122 5436 47 -85 -137 N ATOM 410 NH2 ARG G 77 -23.279 -15.801 58.112 1.00 41.83 N ANISOU 410 NH2 ARG G 77 5216 5138 5539 114 -96 -104 N ATOM 411 N ASN G 78 -16.922 -21.598 54.886 1.00 24.26 N ANISOU 411 N ASN G 78 2979 3055 3182 10 -50 0 N ATOM 412 CA ASN G 78 -16.386 -22.865 54.369 1.00 24.06 C ANISOU 412 CA ASN G 78 3015 2986 3140 -12 -43 -30 C ATOM 413 C ASN G 78 -14.864 -23.084 54.621 1.00 23.38 C ANISOU 413 C ASN G 78 2926 2910 3046 -4 -47 -22 C ATOM 414 O ASN G 78 -14.285 -24.060 54.141 1.00 23.33 O ANISOU 414 O ASN G 78 2869 2912 3083 -57 -38 25 O ATOM 415 CB ASN G 78 -16.740 -23.014 52.870 1.00 23.95 C ANISOU 415 CB ASN G 78 3014 2943 3141 -12 -87 -32 C ATOM 416 CG ASN G 78 -15.929 -22.106 51.959 1.00 25.82 C ANISOU 416 CG ASN G 78 3306 3152 3351 170 -215 -250 C ATOM 417 OD1 ASN G 78 -16.027 -22.201 50.730 1.00 29.81 O ANISOU 417 OD1 ASN G 78 3797 3513 4016 266 -521 -658 O ATOM 418 ND2 ASN G 78 -15.131 -21.226 52.540 1.00 24.27 N ANISOU 418 ND2 ASN G 78 3116 2727 3379 188 -491 -693 N ATOM 419 N GLY G 79 -14.228 -22.164 55.355 1.00 22.88 N ANISOU 419 N GLY G 79 2850 2912 2929 0 -36 2 N ATOM 420 CA GLY G 79 -12.812 -22.244 55.684 1.00 21.81 C ANISOU 420 CA GLY G 79 2752 2771 2763 9 -34 20 C ATOM 421 C GLY G 79 -11.870 -21.577 54.687 1.00 21.21 C ANISOU 421 C GLY G 79 2710 2670 2677 -16 -58 33 C ATOM 422 O GLY G 79 -10.724 -21.273 55.044 1.00 20.54 O ANISOU 422 O GLY G 79 2665 2617 2522 48 -127 117 O ATOM 423 N ASN G 80 -12.332 -21.362 53.449 1.00 20.12 N ANISOU 423 N ASN G 80 2573 2542 2527 -32 -99 -2 N ATOM 424 CA ASN G 80 -11.550 -20.679 52.411 1.00 19.59 C ANISOU 424 CA ASN G 80 2547 2473 2423 3 -57 -12 C ATOM 425 C ASN G 80 -11.408 -19.193 52.667 1.00 17.65 C ANISOU 425 C ASN G 80 2279 2245 2183 -56 -84 1 C ATOM 426 O ASN G 80 -12.206 -18.588 53.367 1.00 16.15 O ANISOU 426 O ASN G 80 2061 2056 2016 -153 -42 58 O ATOM 427 CB ASN G 80 -12.172 -20.835 51.003 1.00 20.20 C ANISOU 427 CB ASN G 80 2660 2493 2520 1 -132 -62 C ATOM 428 CG ASN G 80 -12.253 -22.293 50.533 1.00 22.86 C ANISOU 428 CG ASN G 80 3299 2737 2649 165 -82 -77 C ATOM 429 OD1 ASN G 80 -12.323 -23.205 51.331 1.00 27.38 O ANISOU 429 OD1 ASN G 80 4243 3162 2997 244 -72 -72 O ATOM 430 ND2 ASN G 80 -12.289 -22.493 49.218 1.00 25.48 N ANISOU 430 ND2 ASN G 80 3718 3284 2678 255 229 -431 N ATOM 431 N LEU G 81 -10.395 -18.610 52.038 1.00 16.77 N ANISOU 431 N LEU G 81 2156 2176 2037 17 -50 -24 N ATOM 432 CA LEU G 81 -10.159 -17.178 52.094 1.00 15.78 C ANISOU 432 CA LEU G 81 2044 2009 1942 7 -25 -6 C ATOM 433 C LEU G 81 -10.668 -16.553 50.816 1.00 15.47 C ANISOU 433 C LEU G 81 2017 1973 1885 37 -19 -31 C ATOM 434 O LEU G 81 -10.464 -17.092 49.731 1.00 15.80 O ANISOU 434 O LEU G 81 2135 2075 1793 111 -62 -136 O ATOM 435 CB LEU G 81 -8.674 -16.879 52.277 1.00 15.94 C ANISOU 435 CB LEU G 81 2071 1977 2009 52 -16 28 C ATOM 436 CG LEU G 81 -8.048 -17.491 53.534 1.00 15.79 C ANISOU 436 CG LEU G 81 2009 2071 1916 -29 -45 -1 C ATOM 437 CD1 LEU G 81 -6.548 -17.161 53.599 1.00 16.24 C ANISOU 437 CD1 LEU G 81 2111 2054 2002 60 -4 60 C ATOM 438 CD2 LEU G 81 -8.777 -17.031 54.781 1.00 15.42 C ANISOU 438 CD2 LEU G 81 1927 1900 2031 -8 -21 41 C ATOM 439 N GLN G 82 -11.356 -15.429 50.967 1.00 14.17 N ANISOU 439 N GLN G 82 1841 1787 1754 50 -9 -77 N ATOM 440 CA GLN G 82 -11.818 -14.591 49.862 1.00 13.14 C ANISOU 440 CA GLN G 82 1680 1696 1617 8 4 -12 C ATOM 441 C GLN G 82 -10.905 -13.373 49.754 1.00 12.12 C ANISOU 441 C GLN G 82 1579 1560 1466 0 12 -15 C ATOM 442 O GLN G 82 -10.561 -12.779 50.762 1.00 10.74 O ANISOU 442 O GLN G 82 1519 1325 1233 4 146 6 O ATOM 443 CB GLN G 82 -13.256 -14.150 50.148 1.00 13.66 C ANISOU 443 CB GLN G 82 1739 1747 1701 65 -2 -11 C ATOM 444 CG GLN G 82 -13.767 -12.995 49.312 1.00 14.87 C ANISOU 444 CG GLN G 82 1887 1907 1855 42 74 17 C ATOM 445 CD GLN G 82 -15.085 -12.468 49.833 1.00 15.91 C ANISOU 445 CD GLN G 82 1892 2100 2050 14 186 80 C ATOM 446 OE1 GLN G 82 -16.111 -13.119 49.686 1.00 17.63 O ANISOU 446 OE1 GLN G 82 1712 2522 2461 -86 421 96 O ATOM 447 NE2 GLN G 82 -15.057 -11.294 50.452 1.00 17.12 N ANISOU 447 NE2 GLN G 82 2076 2382 2046 84 473 -43 N ATOM 448 N TYR G 83 -10.525 -13.008 48.527 1.00 11.43 N ANISOU 448 N TYR G 83 1495 1510 1337 -54 -20 -62 N ATOM 449 CA TYR G 83 -9.555 -11.958 48.266 1.00 10.94 C ANISOU 449 CA TYR G 83 1469 1395 1293 -37 6 -45 C ATOM 450 C TYR G 83 -10.110 -10.869 47.360 1.00 11.01 C ANISOU 450 C TYR G 83 1421 1424 1338 -71 -10 -47 C ATOM 451 O TYR G 83 -10.540 -11.146 46.243 1.00 11.12 O ANISOU 451 O TYR G 83 1589 1367 1266 -154 -37 -106 O ATOM 452 CB TYR G 83 -8.329 -12.546 47.570 1.00 11.20 C ANISOU 452 CB TYR G 83 1454 1375 1425 -50 -31 -45 C ATOM 453 CG TYR G 83 -7.558 -13.593 48.340 1.00 12.36 C ANISOU 453 CG TYR G 83 1632 1527 1535 93 18 -57 C ATOM 454 CD1 TYR G 83 -7.302 -14.859 47.781 1.00 13.02 C ANISOU 454 CD1 TYR G 83 1762 1446 1738 -83 10 159 C ATOM 455 CD2 TYR G 83 -7.035 -13.316 49.593 1.00 14.02 C ANISOU 455 CD2 TYR G 83 1889 1649 1789 282 -136 -2 C ATOM 456 CE1 TYR G 83 -6.559 -15.806 48.470 1.00 13.39 C ANISOU 456 CE1 TYR G 83 1633 1530 1923 79 17 0 C ATOM 457 CE2 TYR G 83 -6.307 -14.283 50.303 1.00 14.96 C ANISOU 457 CE2 TYR G 83 1850 1760 2072 92 115 -36 C ATOM 458 CZ TYR G 83 -6.057 -15.510 49.731 1.00 13.33 C ANISOU 458 CZ TYR G 83 1680 1494 1890 23 218 48 C ATOM 459 OH TYR G 83 -5.323 -16.451 50.438 1.00 12.46 O ANISOU 459 OH TYR G 83 1447 1231 2056 215 335 68 O ATOM 460 N ASP G 84 -10.056 -9.625 47.817 1.00 10.75 N ANISOU 460 N ASP G 84 1481 1347 1254 -11 -4 -67 N ATOM 461 CA ASP G 84 -10.304 -8.463 46.951 1.00 11.12 C ANISOU 461 CA ASP G 84 1464 1448 1312 -23 0 -7 C ATOM 462 C ASP G 84 -9.079 -7.562 46.906 1.00 11.11 C ANISOU 462 C ASP G 84 1435 1463 1323 -33 -4 -47 C ATOM 463 O ASP G 84 -8.582 -7.115 47.945 1.00 11.15 O ANISOU 463 O ASP G 84 1394 1445 1395 14 51 -58 O ATOM 464 CB ASP G 84 -11.529 -7.688 47.411 1.00 11.12 C ANISOU 464 CB ASP G 84 1555 1334 1335 -56 -11 21 C ATOM 465 CG ASP G 84 -12.825 -8.379 47.017 1.00 13.87 C ANISOU 465 CG ASP G 84 1930 1741 1599 -13 18 109 C ATOM 466 OD1 ASP G 84 -13.374 -8.062 45.928 1.00 14.62 O ANISOU 466 OD1 ASP G 84 2537 1832 1185 206 1 88 O ATOM 467 OD2 ASP G 84 -13.350 -9.282 47.727 1.00 16.73 O ANISOU 467 OD2 ASP G 84 2367 2001 1988 -341 195 364 O ATOM 468 N LEU G 85 -8.595 -7.311 45.692 1.00 11.33 N ANISOU 468 N LEU G 85 1368 1506 1431 -37 -20 -51 N ATOM 469 CA LEU G 85 -7.391 -6.540 45.456 1.00 12.07 C ANISOU 469 CA LEU G 85 1556 1539 1489 -39 18 -44 C ATOM 470 C LEU G 85 -7.808 -5.235 44.835 1.00 11.55 C ANISOU 470 C LEU G 85 1486 1450 1453 -12 -23 -30 C ATOM 471 O LEU G 85 -8.442 -5.243 43.794 1.00 12.52 O ANISOU 471 O LEU G 85 1707 1418 1632 -77 99 -75 O ATOM 472 CB LEU G 85 -6.455 -7.278 44.475 1.00 12.01 C ANISOU 472 CB LEU G 85 1501 1527 1534 -5 -14 -140 C ATOM 473 CG LEU G 85 -5.435 -8.237 45.020 1.00 13.21 C ANISOU 473 CG LEU G 85 1703 1697 1618 -54 4 -132 C ATOM 474 CD1 LEU G 85 -4.769 -9.038 43.853 1.00 12.70 C ANISOU 474 CD1 LEU G 85 1429 1868 1527 13 68 -200 C ATOM 475 CD2 LEU G 85 -4.379 -7.512 45.854 1.00 11.99 C ANISOU 475 CD2 LEU G 85 1260 1788 1504 -239 173 -189 C ATOM 476 N HIS G 86 -7.468 -4.125 45.488 1.00 11.28 N ANISOU 476 N HIS G 86 1484 1405 1394 -9 -37 -30 N ATOM 477 CA HIS G 86 -7.734 -2.780 44.992 1.00 10.52 C ANISOU 477 CA HIS G 86 1354 1352 1291 -1 -50 6 C ATOM 478 C HIS G 86 -6.420 -2.044 44.776 1.00 10.50 C ANISOU 478 C HIS G 86 1339 1394 1254 -16 -28 63 C ATOM 479 O HIS G 86 -5.531 -2.067 45.629 1.00 10.98 O ANISOU 479 O HIS G 86 1442 1451 1278 -25 -17 145 O ATOM 480 CB HIS G 86 -8.586 -2.004 45.998 1.00 10.00 C ANISOU 480 CB HIS G 86 1294 1238 1267 -20 -82 -47 C ATOM 481 CG HIS G 86 -9.821 -2.722 46.438 1.00 8.31 C ANISOU 481 CG HIS G 86 1076 1004 1076 -34 -76 -3 C ATOM 482 ND1 HIS G 86 -11.083 -2.335 46.046 1.00 7.61 N ANISOU 482 ND1 HIS G 86 1000 622 1269 -181 152 -50 N ATOM 483 CD2 HIS G 86 -9.989 -3.799 47.237 1.00 7.97 C ANISOU 483 CD2 HIS G 86 827 991 1207 149 -89 133 C ATOM 484 CE1 HIS G 86 -11.976 -3.147 46.586 1.00 8.31 C ANISOU 484 CE1 HIS G 86 1126 957 1073 22 65 -29 C ATOM 485 NE2 HIS G 86 -11.336 -4.049 47.307 1.00 8.60 N ANISOU 485 NE2 HIS G 86 1080 1029 1157 100 8 130 N ATOM 486 N TYR G 87 -6.267 -1.402 43.629 1.00 10.52 N ANISOU 486 N TYR G 87 1283 1344 1370 34 -49 46 N ATOM 487 CA TYR G 87 -5.123 -0.523 43.427 1.00 9.96 C ANISOU 487 CA TYR G 87 1251 1239 1291 27 -34 69 C ATOM 488 C TYR G 87 -5.673 0.889 43.361 1.00 9.88 C ANISOU 488 C TYR G 87 1206 1242 1306 29 -63 76 C ATOM 489 O TYR G 87 -6.580 1.164 42.581 1.00 9.98 O ANISOU 489 O TYR G 87 1216 1192 1384 -38 -238 172 O ATOM 490 CB TYR G 87 -4.272 -0.906 42.212 1.00 9.80 C ANISOU 490 CB TYR G 87 1174 1200 1348 76 -2 30 C ATOM 491 CG TYR G 87 -4.970 -1.085 40.894 1.00 10.02 C ANISOU 491 CG TYR G 87 1180 1207 1418 79 101 130 C ATOM 492 CD1 TYR G 87 -4.752 -0.200 39.855 1.00 12.17 C ANISOU 492 CD1 TYR G 87 1455 1344 1824 136 -15 130 C ATOM 493 CD2 TYR G 87 -5.787 -2.185 40.646 1.00 11.18 C ANISOU 493 CD2 TYR G 87 1320 1334 1594 242 15 119 C ATOM 494 CE1 TYR G 87 -5.331 -0.391 38.623 1.00 10.84 C ANISOU 494 CE1 TYR G 87 1163 1381 1573 233 -83 53 C ATOM 495 CE2 TYR G 87 -6.387 -2.376 39.421 1.00 10.51 C ANISOU 495 CE2 TYR G 87 1243 1404 1344 343 4 89 C ATOM 496 CZ TYR G 87 -6.176 -1.460 38.416 1.00 11.67 C ANISOU 496 CZ TYR G 87 1355 1513 1565 245 203 -37 C ATOM 497 OH TYR G 87 -6.781 -1.625 37.181 1.00 10.51 O ANISOU 497 OH TYR G 87 783 2102 1107 496 373 136 O ATOM 498 N TRP G 88 -5.155 1.741 44.241 1.00 8.98 N ANISOU 498 N TRP G 88 1108 1144 1160 60 -97 20 N ATOM 499 CA TRP G 88 -5.637 3.084 44.458 1.00 9.31 C ANISOU 499 CA TRP G 88 1159 1226 1151 7 -22 -10 C ATOM 500 C TRP G 88 -4.643 4.046 43.859 1.00 8.54 C ANISOU 500 C TRP G 88 1057 1154 1032 -2 23 -18 C ATOM 501 O TRP G 88 -3.446 3.952 44.122 1.00 9.02 O ANISOU 501 O TRP G 88 1184 1249 993 40 49 -65 O ATOM 502 CB TRP G 88 -5.796 3.345 45.952 1.00 9.43 C ANISOU 502 CB TRP G 88 1191 1199 1193 -50 48 -59 C ATOM 503 CG TRP G 88 -6.381 4.690 46.292 1.00 9.13 C ANISOU 503 CG TRP G 88 1075 1210 1182 4 62 -15 C ATOM 504 CD1 TRP G 88 -7.709 4.993 46.495 1.00 10.35 C ANISOU 504 CD1 TRP G 88 1468 1151 1311 -202 242 27 C ATOM 505 CD2 TRP G 88 -5.666 5.913 46.487 1.00 7.97 C ANISOU 505 CD2 TRP G 88 993 973 1060 -27 45 -261 C ATOM 506 NE1 TRP G 88 -7.851 6.320 46.814 1.00 11.20 N ANISOU 506 NE1 TRP G 88 1131 1608 1518 15 16 -280 N ATOM 507 CE2 TRP G 88 -6.619 6.916 46.804 1.00 10.52 C ANISOU 507 CE2 TRP G 88 1236 1385 1375 -206 218 -193 C ATOM 508 CE3 TRP G 88 -4.320 6.275 46.410 1.00 7.28 C ANISOU 508 CE3 TRP G 88 853 822 1090 -25 18 -94 C ATOM 509 CZ2 TRP G 88 -6.263 8.231 47.067 1.00 9.92 C ANISOU 509 CZ2 TRP G 88 1245 1123 1401 -95 243 -265 C ATOM 510 CZ3 TRP G 88 -3.966 7.594 46.691 1.00 8.17 C ANISOU 510 CZ3 TRP G 88 942 983 1177 46 -37 -111 C ATOM 511 CH2 TRP G 88 -4.930 8.549 47.006 1.00 8.99 C ANISOU 511 CH2 TRP G 88 1027 1173 1215 -93 68 -179 C ATOM 512 N LEU G 89 -5.149 4.949 43.036 1.00 8.72 N ANISOU 512 N LEU G 89 1031 1131 1148 68 42 -31 N ATOM 513 CA LEU G 89 -4.329 5.880 42.255 1.00 8.92 C ANISOU 513 CA LEU G 89 1071 1151 1167 0 -26 -24 C ATOM 514 C LEU G 89 -4.609 7.312 42.680 1.00 8.86 C ANISOU 514 C LEU G 89 1065 1091 1210 1 -24 -46 C ATOM 515 O LEU G 89 -5.701 7.834 42.496 1.00 8.92 O ANISOU 515 O LEU G 89 1258 929 1203 -57 -88 -138 O ATOM 516 CB LEU G 89 -4.621 5.720 40.774 1.00 9.72 C ANISOU 516 CB LEU G 89 1122 1246 1325 42 33 6 C ATOM 517 CG LEU G 89 -4.593 4.288 40.245 1.00 10.38 C ANISOU 517 CG LEU G 89 1229 1410 1303 64 -8 -61 C ATOM 518 CD1 LEU G 89 -4.896 4.323 38.785 1.00 13.56 C ANISOU 518 CD1 LEU G 89 1476 1821 1856 160 6 25 C ATOM 519 CD2 LEU G 89 -3.223 3.648 40.496 1.00 11.83 C ANISOU 519 CD2 LEU G 89 1536 1352 1605 104 -14 -59 C ATOM 520 N GLY G 90 -3.600 7.945 43.253 1.00 9.41 N ANISOU 520 N GLY G 90 1204 1148 1223 31 -10 -68 N ATOM 521 CA GLY G 90 -3.699 9.326 43.655 1.00 9.75 C ANISOU 521 CA GLY G 90 1231 1221 1253 5 3 5 C ATOM 522 C GLY G 90 -3.745 10.243 42.444 1.00 9.68 C ANISOU 522 C GLY G 90 1246 1234 1196 32 -1 24 C ATOM 523 O GLY G 90 -3.180 9.936 41.384 1.00 9.68 O ANISOU 523 O GLY G 90 1224 1264 1189 91 173 92 O ATOM 524 N ASN G 91 -4.435 11.364 42.603 1.00 9.12 N ANISOU 524 N ASN G 91 1173 1126 1166 20 3 2 N ATOM 525 CA ASN G 91 -4.551 12.347 41.526 1.00 9.04 C ANISOU 525 CA ASN G 91 1163 1161 1108 23 19 -4 C ATOM 526 C ASN G 91 -3.206 12.827 40.965 1.00 8.82 C ANISOU 526 C ASN G 91 1164 1094 1092 7 44 -43 C ATOM 527 O ASN G 91 -3.116 13.159 39.774 1.00 9.40 O ANISOU 527 O ASN G 91 1197 1307 1065 -34 143 -103 O ATOM 528 CB ASN G 91 -5.390 13.541 41.996 1.00 8.73 C ANISOU 528 CB ASN G 91 1216 1029 1070 6 45 -9 C ATOM 529 CG ASN G 91 -5.654 14.534 40.891 1.00 10.15 C ANISOU 529 CG ASN G 91 1231 1389 1235 143 -30 -76 C ATOM 530 OD1 ASN G 91 -6.279 14.179 39.905 1.00 10.37 O ANISOU 530 OD1 ASN G 91 1282 1480 1177 304 -130 -198 O ATOM 531 ND2 ASN G 91 -5.148 15.785 41.034 1.00 8.21 N ANISOU 531 ND2 ASN G 91 1078 829 1210 5 145 285 N ATOM 532 N GLU G 92 -2.167 12.893 41.788 1.00 8.66 N ANISOU 532 N GLU G 92 1115 1074 1099 51 50 -6 N ATOM 533 CA GLU G 92 -0.854 13.358 41.297 1.00 9.75 C ANISOU 533 CA GLU G 92 1217 1231 1256 38 28 -19 C ATOM 534 C GLU G 92 0.218 12.267 41.161 1.00 9.62 C ANISOU 534 C GLU G 92 1193 1192 1270 38 11 -15 C ATOM 535 O GLU G 92 1.414 12.591 40.970 1.00 9.25 O ANISOU 535 O GLU G 92 1054 1225 1234 6 109 0 O ATOM 536 CB GLU G 92 -0.310 14.529 42.165 1.00 9.42 C ANISOU 536 CB GLU G 92 1213 1126 1239 37 46 -23 C ATOM 537 CG GLU G 92 -1.277 15.705 42.307 1.00 12.02 C ANISOU 537 CG GLU G 92 1579 1570 1418 -13 143 14 C ATOM 538 CD GLU G 92 -2.237 15.595 43.497 1.00 14.37 C ANISOU 538 CD GLU G 92 1686 2043 1730 150 238 -44 C ATOM 539 OE1 GLU G 92 -3.400 16.014 43.359 1.00 18.31 O ANISOU 539 OE1 GLU G 92 2121 2736 2099 383 675 -162 O ATOM 540 OE2 GLU G 92 -1.845 15.096 44.568 1.00 16.22 O ANISOU 540 OE2 GLU G 92 2077 2323 1761 121 401 -44 O ATOM 541 N CYS G 93 -0.177 10.995 41.230 1.00 9.76 N ANISOU 541 N CYS G 93 1152 1272 1283 16 -42 -52 N ATOM 542 CA CYS G 93 0.808 9.901 41.118 1.00 10.04 C ANISOU 542 CA CYS G 93 1231 1299 1284 -26 -34 -70 C ATOM 543 C CYS G 93 1.387 9.829 39.696 1.00 9.90 C ANISOU 543 C CYS G 93 1201 1300 1258 -6 -39 -92 C ATOM 544 O CYS G 93 0.748 10.255 38.739 1.00 9.10 O ANISOU 544 O CYS G 93 1114 1106 1236 0 -126 -115 O ATOM 545 CB CYS G 93 0.240 8.557 41.593 1.00 10.18 C ANISOU 545 CB CYS G 93 1243 1382 1240 2 -137 9 C ATOM 546 SG CYS G 93 -0.833 7.678 40.438 1.00 11.07 S ANISOU 546 SG CYS G 93 1508 1507 1188 -6 100 -474 S ATOM 547 N SER G 94 2.645 9.391 39.589 1.00 9.91 N ANISOU 547 N SER G 94 1258 1230 1275 7 -5 -81 N ATOM 548 CA SER G 94 3.327 9.416 38.307 1.00 9.98 C ANISOU 548 CA SER G 94 1185 1255 1350 -16 45 -18 C ATOM 549 C SER G 94 2.988 8.152 37.562 1.00 9.72 C ANISOU 549 C SER G 94 1143 1250 1298 -21 29 -39 C ATOM 550 O SER G 94 2.509 7.152 38.148 1.00 9.22 O ANISOU 550 O SER G 94 1094 1016 1390 -121 16 -19 O ATOM 551 CB SER G 94 4.850 9.605 38.466 1.00 10.89 C ANISOU 551 CB SER G 94 1403 1386 1346 110 49 -49 C ATOM 552 OG SER G 94 5.369 8.795 39.487 1.00 12.20 O ANISOU 552 OG SER G 94 1494 1638 1501 188 294 167 O ATOM 553 N GLN G 95 3.228 8.189 36.271 1.00 9.18 N ANISOU 553 N GLN G 95 1088 1166 1232 -93 18 49 N ATOM 554 CA GLN G 95 2.911 7.065 35.394 1.00 9.36 C ANISOU 554 CA GLN G 95 1156 1151 1246 -12 41 -31 C ATOM 555 C GLN G 95 3.602 5.744 35.797 1.00 9.18 C ANISOU 555 C GLN G 95 1192 1122 1173 -26 16 76 C ATOM 556 O GLN G 95 3.056 4.676 35.612 1.00 9.03 O ANISOU 556 O GLN G 95 1193 1027 1209 -21 181 94 O ATOM 557 CB GLN G 95 3.233 7.415 33.930 1.00 9.19 C ANISOU 557 CB GLN G 95 1167 1161 1161 -28 62 25 C ATOM 558 CG GLN G 95 3.000 6.229 32.932 1.00 8.95 C ANISOU 558 CG GLN G 95 1072 1147 1179 -117 -100 -195 C ATOM 559 CD GLN G 95 3.055 6.621 31.446 1.00 9.41 C ANISOU 559 CD GLN G 95 1230 1144 1198 -130 -199 -216 C ATOM 560 OE1 GLN G 95 2.334 6.034 30.608 1.00 9.91 O ANISOU 560 OE1 GLN G 95 1042 1173 1550 -93 -701 -141 O ATOM 561 NE2 GLN G 95 3.937 7.544 31.108 1.00 6.41 N ANISOU 561 NE2 GLN G 95 801 601 1031 -173 108 -505 N ATOM 562 N ASP G 96 4.831 5.804 36.252 1.00 8.78 N ANISOU 562 N ASP G 96 1138 1052 1143 69 -40 32 N ATOM 563 CA ASP G 96 5.506 4.576 36.708 1.00 9.38 C ANISOU 563 CA ASP G 96 1242 1178 1144 7 -18 21 C ATOM 564 C ASP G 96 4.823 3.946 37.929 1.00 9.16 C ANISOU 564 C ASP G 96 1163 1105 1213 31 -64 16 C ATOM 565 O ASP G 96 4.843 2.716 38.128 1.00 9.82 O ANISOU 565 O ASP G 96 1250 1166 1313 23 -85 30 O ATOM 566 CB ASP G 96 6.963 4.892 37.014 1.00 9.40 C ANISOU 566 CB ASP G 96 1207 1207 1158 60 -71 9 C ATOM 567 CG ASP G 96 7.107 5.906 38.108 1.00 10.19 C ANISOU 567 CG ASP G 96 1465 1125 1280 98 -3 -21 C ATOM 568 OD1 ASP G 96 6.660 7.060 37.886 1.00 13.89 O ANISOU 568 OD1 ASP G 96 1949 1826 1500 -94 137 206 O ATOM 569 OD2 ASP G 96 7.631 5.633 39.214 1.00 10.46 O ANISOU 569 OD2 ASP G 96 1845 1267 862 58 -88 139 O ATOM 570 N GLU G 97 4.227 4.795 38.745 1.00 8.44 N ANISOU 570 N GLU G 97 1130 1022 1052 19 -103 -16 N ATOM 571 CA GLU G 97 3.561 4.372 39.952 1.00 8.50 C ANISOU 571 CA GLU G 97 1128 1008 1092 16 -29 -24 C ATOM 572 C GLU G 97 2.223 3.722 39.658 1.00 7.97 C ANISOU 572 C GLU G 97 1043 971 1012 66 -111 -76 C ATOM 573 O GLU G 97 1.926 2.649 40.174 1.00 7.08 O ANISOU 573 O GLU G 97 953 754 981 93 -136 -196 O ATOM 574 CB GLU G 97 3.422 5.560 40.928 1.00 8.59 C ANISOU 574 CB GLU G 97 1125 1020 1116 -8 -56 -16 C ATOM 575 CG GLU G 97 4.755 6.048 41.453 1.00 9.35 C ANISOU 575 CG GLU G 97 1197 1250 1103 -107 -65 -84 C ATOM 576 CD GLU G 97 4.666 7.301 42.333 1.00 10.79 C ANISOU 576 CD GLU G 97 1355 1437 1305 -22 -178 -212 C ATOM 577 OE1 GLU G 97 3.751 8.129 42.162 1.00 10.13 O ANISOU 577 OE1 GLU G 97 1397 1265 1186 -375 -82 -369 O ATOM 578 OE2 GLU G 97 5.553 7.487 43.206 1.00 12.26 O ANISOU 578 OE2 GLU G 97 1941 1844 871 -118 -162 -141 O ATOM 579 N SER G 98 1.409 4.345 38.820 1.00 9.44 N ANISOU 579 N SER G 98 1285 1054 1246 0 -63 -38 N ATOM 580 CA SER G 98 0.096 3.777 38.483 1.00 9.11 C ANISOU 580 CA SER G 98 1131 1127 1201 8 -60 -20 C ATOM 581 C SER G 98 0.276 2.514 37.626 1.00 8.72 C ANISOU 581 C SER G 98 1120 1085 1105 32 -54 -37 C ATOM 582 O SER G 98 -0.459 1.536 37.786 1.00 8.86 O ANISOU 582 O SER G 98 1269 1003 1092 -21 -17 -128 O ATOM 583 CB SER G 98 -0.821 4.807 37.769 1.00 9.40 C ANISOU 583 CB SER G 98 1232 1149 1190 33 37 -31 C ATOM 584 OG SER G 98 -0.159 5.511 36.740 1.00 10.03 O ANISOU 584 OG SER G 98 1096 1357 1356 11 7 43 O ATOM 585 N GLY G 99 1.237 2.526 36.717 1.00 8.49 N ANISOU 585 N GLY G 99 1083 1090 1051 39 -102 -32 N ATOM 586 CA GLY G 99 1.532 1.318 35.951 1.00 8.70 C ANISOU 586 CA GLY G 99 1095 1099 1110 28 -67 -20 C ATOM 587 C GLY G 99 2.006 0.174 36.838 1.00 8.72 C ANISOU 587 C GLY G 99 1108 1091 1113 -2 -29 -3 C ATOM 588 O GLY G 99 1.557 -0.972 36.712 1.00 8.36 O ANISOU 588 O GLY G 99 934 1074 1169 32 -103 -20 O ATOM 589 N ALA G 100 2.901 0.484 37.769 1.00 8.78 N ANISOU 589 N ALA G 100 1046 1138 1148 -27 1 80 N ATOM 590 CA ALA G 100 3.403 -0.541 38.672 1.00 8.73 C ANISOU 590 CA ALA G 100 1155 1033 1129 -43 17 59 C ATOM 591 C ALA G 100 2.282 -1.097 39.585 1.00 8.81 C ANISOU 591 C ALA G 100 1131 1008 1205 -60 98 78 C ATOM 592 O ALA G 100 2.265 -2.291 39.867 1.00 9.89 O ANISOU 592 O ALA G 100 1400 1060 1296 -213 153 41 O ATOM 593 CB ALA G 100 4.535 -0.006 39.507 1.00 9.00 C ANISOU 593 CB ALA G 100 1056 1087 1274 -124 44 190 C ATOM 594 N ALA G 101 1.388 -0.236 40.072 1.00 8.61 N ANISOU 594 N ALA G 101 1124 990 1157 -92 63 112 N ATOM 595 CA ALA G 101 0.264 -0.662 40.915 1.00 8.38 C ANISOU 595 CA ALA G 101 1077 1017 1087 -50 35 33 C ATOM 596 C ALA G 101 -0.629 -1.669 40.190 1.00 8.57 C ANISOU 596 C ALA G 101 1147 1010 1099 -97 12 45 C ATOM 597 O ALA G 101 -1.050 -2.687 40.768 1.00 9.20 O ANISOU 597 O ALA G 101 1203 1033 1256 -76 59 -20 O ATOM 598 CB ALA G 101 -0.561 0.546 41.371 1.00 8.28 C ANISOU 598 CB ALA G 101 1015 993 1137 -94 24 75 C ATOM 599 N ALA G 102 -0.890 -1.394 38.917 1.00 8.60 N ANISOU 599 N ALA G 102 1103 984 1177 -64 -2 23 N ATOM 600 CA ALA G 102 -1.694 -2.274 38.090 1.00 8.58 C ANISOU 600 CA ALA G 102 1093 1010 1153 -20 7 0 C ATOM 601 C ALA G 102 -1.000 -3.622 37.896 1.00 8.54 C ANISOU 601 C ALA G 102 1050 975 1218 -5 1 9 C ATOM 602 O ALA G 102 -1.625 -4.652 38.061 1.00 8.64 O ANISOU 602 O ALA G 102 1046 896 1338 -115 115 91 O ATOM 603 CB ALA G 102 -1.975 -1.644 36.752 1.00 8.84 C ANISOU 603 CB ALA G 102 1147 1003 1208 26 -47 22 C ATOM 604 N ILE G 103 0.282 -3.599 37.536 1.00 7.88 N ANISOU 604 N ILE G 103 966 937 1089 -37 12 -33 N ATOM 605 CA ILE G 103 1.029 -4.833 37.295 1.00 7.86 C ANISOU 605 CA ILE G 103 935 1004 1047 31 -19 21 C ATOM 606 C ILE G 103 1.182 -5.671 38.566 1.00 7.56 C ANISOU 606 C ILE G 103 899 951 1021 8 -2 42 C ATOM 607 O ILE G 103 1.026 -6.879 38.512 1.00 7.31 O ANISOU 607 O ILE G 103 878 923 977 38 -63 32 O ATOM 608 CB ILE G 103 2.409 -4.552 36.654 1.00 7.23 C ANISOU 608 CB ILE G 103 932 868 946 43 -32 25 C ATOM 609 CG1 ILE G 103 2.247 -3.913 35.284 1.00 7.99 C ANISOU 609 CG1 ILE G 103 1035 877 1123 10 -11 -102 C ATOM 610 CG2 ILE G 103 3.148 -5.838 36.494 1.00 9.11 C ANISOU 610 CG2 ILE G 103 1000 1327 1131 101 88 29 C ATOM 611 CD1 ILE G 103 3.479 -3.176 34.792 1.00 9.48 C ANISOU 611 CD1 ILE G 103 1038 1142 1420 248 115 51 C ATOM 612 N PHE G 104 1.510 -5.030 39.683 1.00 7.43 N ANISOU 612 N PHE G 104 897 936 990 15 21 28 N ATOM 613 CA PHE G 104 1.643 -5.710 40.973 1.00 8.10 C ANISOU 613 CA PHE G 104 1053 967 1054 0 -54 35 C ATOM 614 C PHE G 104 0.323 -6.385 41.332 1.00 8.02 C ANISOU 614 C PHE G 104 1051 940 1055 -33 -90 75 C ATOM 615 O PHE G 104 0.299 -7.464 41.900 1.00 8.32 O ANISOU 615 O PHE G 104 1307 890 965 -40 -281 242 O ATOM 616 CB PHE G 104 1.994 -4.726 42.107 1.00 8.56 C ANISOU 616 CB PHE G 104 1046 1050 1156 14 -3 42 C ATOM 617 CG PHE G 104 3.447 -4.311 42.173 1.00 9.90 C ANISOU 617 CG PHE G 104 1216 1193 1352 -116 -151 -127 C ATOM 618 CD1 PHE G 104 3.764 -3.007 42.508 1.00 12.37 C ANISOU 618 CD1 PHE G 104 1491 1521 1685 -129 -57 80 C ATOM 619 CD2 PHE G 104 4.483 -5.215 41.961 1.00 10.88 C ANISOU 619 CD2 PHE G 104 1168 1438 1527 -255 -130 -102 C ATOM 620 CE1 PHE G 104 5.085 -2.595 42.607 1.00 12.72 C ANISOU 620 CE1 PHE G 104 1560 1687 1583 -187 -130 102 C ATOM 621 CE2 PHE G 104 5.820 -4.811 42.054 1.00 11.73 C ANISOU 621 CE2 PHE G 104 1666 1671 1116 -175 -98 -131 C ATOM 622 CZ PHE G 104 6.114 -3.493 42.361 1.00 11.55 C ANISOU 622 CZ PHE G 104 1406 1486 1494 -113 -158 91 C ATOM 623 N THR G 105 -0.780 -5.743 41.003 1.00 7.90 N ANISOU 623 N THR G 105 1060 840 1100 -10 -46 91 N ATOM 624 CA THR G 105 -2.114 -6.295 41.255 1.00 8.46 C ANISOU 624 CA THR G 105 1028 1022 1164 -9 -36 -13 C ATOM 625 C THR G 105 -2.330 -7.601 40.450 1.00 8.54 C ANISOU 625 C THR G 105 1002 1084 1158 -25 -74 12 C ATOM 626 O THR G 105 -2.812 -8.587 40.975 1.00 9.70 O ANISOU 626 O THR G 105 1008 1302 1375 -65 -134 30 O ATOM 627 CB THR G 105 -3.149 -5.262 40.882 1.00 7.84 C ANISOU 627 CB THR G 105 931 931 1116 -37 -8 -4 C ATOM 628 OG1 THR G 105 -3.087 -4.151 41.795 1.00 9.44 O ANISOU 628 OG1 THR G 105 908 1355 1322 129 87 10 O ATOM 629 CG2 THR G 105 -4.565 -5.806 41.016 1.00 9.67 C ANISOU 629 CG2 THR G 105 1230 1111 1330 43 136 -22 C ATOM 630 N VAL G 106 -1.968 -7.600 39.179 1.00 8.75 N ANISOU 630 N VAL G 106 1019 1118 1187 29 -15 -38 N ATOM 631 CA VAL G 106 -2.066 -8.814 38.337 1.00 8.33 C ANISOU 631 CA VAL G 106 984 1018 1162 -3 -60 -41 C ATOM 632 C VAL G 106 -1.192 -9.951 38.923 1.00 8.45 C ANISOU 632 C VAL G 106 977 993 1240 -4 -50 -5 C ATOM 633 O VAL G 106 -1.616 -11.082 39.023 1.00 8.83 O ANISOU 633 O VAL G 106 842 1081 1432 123 -115 22 O ATOM 634 CB VAL G 106 -1.592 -8.495 36.895 1.00 7.61 C ANISOU 634 CB VAL G 106 970 879 1042 -38 -73 -59 C ATOM 635 CG1 VAL G 106 -1.507 -9.767 36.001 1.00 9.21 C ANISOU 635 CG1 VAL G 106 901 1244 1353 107 -14 -12 C ATOM 636 CG2 VAL G 106 -2.523 -7.486 36.273 1.00 8.53 C ANISOU 636 CG2 VAL G 106 1128 1035 1077 -87 -29 -5 C ATOM 637 N GLN G 107 0.035 -9.615 39.311 1.00 8.47 N ANISOU 637 N GLN G 107 969 1056 1192 8 -82 -44 N ATOM 638 CA GLN G 107 1.021 -10.589 39.793 1.00 8.31 C ANISOU 638 CA GLN G 107 1033 982 1141 -9 -40 -18 C ATOM 639 C GLN G 107 0.568 -11.188 41.128 1.00 8.74 C ANISOU 639 C GLN G 107 1142 1053 1123 34 19 -2 C ATOM 640 O GLN G 107 0.770 -12.373 41.380 1.00 8.67 O ANISOU 640 O GLN G 107 1099 1040 1154 38 28 44 O ATOM 641 CB GLN G 107 2.422 -9.949 39.916 1.00 7.97 C ANISOU 641 CB GLN G 107 888 1005 1134 61 40 -16 C ATOM 642 CG GLN G 107 3.018 -9.520 38.566 1.00 8.40 C ANISOU 642 CG GLN G 107 725 1177 1287 -91 11 -49 C ATOM 643 CD GLN G 107 4.393 -8.845 38.675 1.00 12.02 C ANISOU 643 CD GLN G 107 1188 1684 1694 -245 307 -98 C ATOM 644 OE1 GLN G 107 5.236 -8.976 37.754 1.00 14.45 O ANISOU 644 OE1 GLN G 107 1448 1857 2186 -161 192 -312 O ATOM 645 NE2 GLN G 107 4.606 -8.094 39.742 1.00 7.98 N ANISOU 645 NE2 GLN G 107 596 1232 1202 -502 384 -206 N ATOM 646 N LEU G 108 -0.061 -10.377 41.968 1.00 9.79 N ANISOU 646 N LEU G 108 1308 1175 1236 53 -42 69 N ATOM 647 CA LEU G 108 -0.554 -10.846 43.265 1.00 10.73 C ANISOU 647 CA LEU G 108 1390 1300 1387 73 3 7 C ATOM 648 C LEU G 108 -1.736 -11.782 43.053 1.00 9.03 C ANISOU 648 C LEU G 108 1208 1078 1145 46 -83 -13 C ATOM 649 O LEU G 108 -1.842 -12.812 43.682 1.00 8.79 O ANISOU 649 O LEU G 108 1156 1044 1137 46 -86 -24 O ATOM 650 CB LEU G 108 -0.978 -9.668 44.152 1.00 11.54 C ANISOU 650 CB LEU G 108 1625 1317 1441 125 -93 -36 C ATOM 651 CG LEU G 108 -0.427 -9.346 45.531 1.00 17.72 C ANISOU 651 CG LEU G 108 2295 2048 2387 224 -163 -19 C ATOM 652 CD1 LEU G 108 0.832 -10.124 45.937 1.00 20.30 C ANISOU 652 CD1 LEU G 108 2518 2647 2545 196 -63 -241 C ATOM 653 CD2 LEU G 108 -0.196 -7.806 45.625 1.00 20.30 C ANISOU 653 CD2 LEU G 108 2640 2406 2666 -70 -25 -45 C ATOM 654 N ASP G 109 -2.632 -11.401 42.166 1.00 8.80 N ANISOU 654 N ASP G 109 1180 1024 1140 59 1 29 N ATOM 655 CA ASP G 109 -3.794 -12.195 41.836 1.00 8.09 C ANISOU 655 CA ASP G 109 1030 1010 1030 -15 -40 42 C ATOM 656 C ASP G 109 -3.282 -13.547 41.290 1.00 8.37 C ANISOU 656 C ASP G 109 1051 1065 1062 -40 -18 27 C ATOM 657 O ASP G 109 -3.693 -14.600 41.774 1.00 8.26 O ANISOU 657 O ASP G 109 1059 1116 963 -101 166 180 O ATOM 658 CB ASP G 109 -4.659 -11.404 40.829 1.00 8.38 C ANISOU 658 CB ASP G 109 994 1090 1100 19 6 -3 C ATOM 659 CG ASP G 109 -6.035 -12.008 40.587 1.00 9.15 C ANISOU 659 CG ASP G 109 1058 1277 1140 76 -158 72 C ATOM 660 OD1 ASP G 109 -6.396 -13.077 41.145 1.00 9.96 O ANISOU 660 OD1 ASP G 109 1061 1241 1479 -290 27 28 O ATOM 661 OD2 ASP G 109 -6.850 -11.440 39.825 1.00 9.00 O ANISOU 661 OD2 ASP G 109 607 1790 1019 384 -492 -230 O ATOM 662 N ASP G 110 -2.341 -13.541 40.358 1.00 7.69 N ANISOU 662 N ASP G 110 980 1003 936 -124 0 66 N ATOM 663 CA ASP G 110 -1.779 -14.800 39.854 1.00 9.07 C ANISOU 663 CA ASP G 110 1167 1182 1097 -15 24 61 C ATOM 664 C ASP G 110 -1.142 -15.685 40.958 1.00 9.00 C ANISOU 664 C ASP G 110 1199 1160 1060 -6 34 21 C ATOM 665 O ASP G 110 -1.317 -16.888 40.972 1.00 8.94 O ANISOU 665 O ASP G 110 1308 1151 937 50 64 34 O ATOM 666 CB ASP G 110 -0.715 -14.582 38.777 1.00 9.47 C ANISOU 666 CB ASP G 110 1258 1226 1111 -55 16 143 C ATOM 667 CG ASP G 110 -1.234 -13.854 37.552 1.00 12.81 C ANISOU 667 CG ASP G 110 1578 1876 1413 -143 154 94 C ATOM 668 OD1 ASP G 110 -2.482 -13.760 37.329 1.00 14.61 O ANISOU 668 OD1 ASP G 110 1440 2541 1568 -373 225 56 O ATOM 669 OD2 ASP G 110 -0.418 -13.326 36.757 1.00 13.93 O ANISOU 669 OD2 ASP G 110 1856 2224 1211 -334 664 335 O ATOM 670 N TYR G 111 -0.389 -15.067 41.846 1.00 9.24 N ANISOU 670 N TYR G 111 1184 1139 1184 -11 22 -28 N ATOM 671 CA TYR G 111 0.204 -15.726 42.989 1.00 9.77 C ANISOU 671 CA TYR G 111 1256 1200 1255 -13 -3 0 C ATOM 672 C TYR G 111 -0.878 -16.359 43.906 1.00 9.39 C ANISOU 672 C TYR G 111 1130 1157 1277 12 23 26 C ATOM 673 O TYR G 111 -0.683 -17.434 44.472 1.00 9.22 O ANISOU 673 O TYR G 111 923 1149 1429 152 55 122 O ATOM 674 CB TYR G 111 1.079 -14.708 43.764 1.00 10.56 C ANISOU 674 CB TYR G 111 1355 1311 1345 -61 49 29 C ATOM 675 CG TYR G 111 1.608 -15.260 45.056 1.00 13.86 C ANISOU 675 CG TYR G 111 1750 1789 1725 -42 -117 -109 C ATOM 676 CD1 TYR G 111 2.772 -16.020 45.094 1.00 18.64 C ANISOU 676 CD1 TYR G 111 2391 2300 2389 -319 -306 -52 C ATOM 677 CD2 TYR G 111 0.913 -15.045 46.247 1.00 19.03 C ANISOU 677 CD2 TYR G 111 2505 2390 2332 -295 -254 125 C ATOM 678 CE1 TYR G 111 3.235 -16.552 46.299 1.00 20.17 C ANISOU 678 CE1 TYR G 111 2604 2611 2445 -371 -299 -9 C ATOM 679 CE2 TYR G 111 1.362 -15.571 47.441 1.00 21.15 C ANISOU 679 CE2 TYR G 111 2689 2671 2674 -248 -406 -35 C ATOM 680 CZ TYR G 111 2.518 -16.310 47.462 1.00 21.67 C ANISOU 680 CZ TYR G 111 2862 2652 2717 -293 -452 11 C ATOM 681 OH TYR G 111 2.940 -16.803 48.671 1.00 24.59 O ANISOU 681 OH TYR G 111 3410 2916 3014 -517 -795 194 O ATOM 682 N LEU G 112 -2.020 -15.698 44.033 1.00 9.01 N ANISOU 682 N LEU G 112 1161 1030 1229 41 26 52 N ATOM 683 CA LEU G 112 -3.189 -16.248 44.722 1.00 9.26 C ANISOU 683 CA LEU G 112 1189 1136 1192 71 56 -1 C ATOM 684 C LEU G 112 -4.088 -17.104 43.822 1.00 9.05 C ANISOU 684 C LEU G 112 1165 1113 1160 57 68 -26 C ATOM 685 O LEU G 112 -5.301 -17.205 44.044 1.00 8.76 O ANISOU 685 O LEU G 112 1200 1026 1100 95 138 20 O ATOM 686 CB LEU G 112 -3.996 -15.098 45.345 1.00 9.91 C ANISOU 686 CB LEU G 112 1306 1209 1250 23 75 7 C ATOM 687 CG LEU G 112 -3.182 -14.307 46.368 1.00 9.62 C ANISOU 687 CG LEU G 112 1224 1205 1226 -11 33 -5 C ATOM 688 CD1 LEU G 112 -3.945 -13.041 46.742 1.00 11.52 C ANISOU 688 CD1 LEU G 112 1268 1639 1467 -107 58 -215 C ATOM 689 CD2 LEU G 112 -2.815 -15.157 47.601 1.00 10.48 C ANISOU 689 CD2 LEU G 112 1207 1417 1355 -194 117 -128 C ATOM 690 N ASN G 113 -3.485 -17.757 42.828 1.00 9.04 N ANISOU 690 N ASN G 113 1166 1146 1123 46 45 36 N ATOM 691 CA ASN G 113 -4.177 -18.737 41.982 1.00 8.62 C ANISOU 691 CA ASN G 113 1115 1115 1043 12 33 -8 C ATOM 692 C ASN G 113 -5.361 -18.152 41.222 1.00 9.12 C ANISOU 692 C ASN G 113 1134 1210 1120 -48 73 -61 C ATOM 693 O ASN G 113 -6.307 -18.847 40.906 1.00 7.85 O ANISOU 693 O ASN G 113 960 1050 971 -227 154 9 O ATOM 694 CB ASN G 113 -4.584 -19.941 42.812 1.00 9.50 C ANISOU 694 CB ASN G 113 1172 1180 1258 -1 -28 -127 C ATOM 695 CG ASN G 113 -3.405 -20.556 43.546 1.00 10.57 C ANISOU 695 CG ASN G 113 1536 1319 1161 54 -43 35 C ATOM 696 OD1 ASN G 113 -3.314 -20.443 44.758 1.00 14.32 O ANISOU 696 OD1 ASN G 113 2482 1883 1076 113 368 102 O ATOM 697 ND2 ASN G 113 -2.476 -21.175 42.802 1.00 7.73 N ANISOU 697 ND2 ASN G 113 573 1086 1277 213 94 -144 N ATOM 698 N GLY G 114 -5.259 -16.862 40.911 1.00 9.44 N ANISOU 698 N GLY G 114 1173 1212 1202 -20 13 12 N ATOM 699 CA GLY G 114 -6.262 -16.119 40.186 1.00 10.22 C ANISOU 699 CA GLY G 114 1232 1340 1311 1 1 -5 C ATOM 700 C GLY G 114 -7.484 -15.773 41.006 1.00 10.80 C ANISOU 700 C GLY G 114 1367 1433 1302 60 31 -42 C ATOM 701 O GLY G 114 -8.430 -15.197 40.471 1.00 11.49 O ANISOU 701 O GLY G 114 1475 1482 1407 191 142 -79 O ATOM 702 N ARG G 115 -7.480 -16.094 42.292 1.00 11.33 N ANISOU 702 N ARG G 115 1446 1443 1416 27 48 19 N ATOM 703 CA ARG G 115 -8.721 -16.070 43.065 1.00 12.29 C ANISOU 703 CA ARG G 115 1543 1595 1530 39 36 19 C ATOM 704 C ARG G 115 -9.178 -14.689 43.513 1.00 10.95 C ANISOU 704 C ARG G 115 1413 1428 1319 38 34 -21 C ATOM 705 O ARG G 115 -10.319 -14.525 43.916 1.00 10.59 O ANISOU 705 O ARG G 115 1294 1556 1173 76 98 -135 O ATOM 706 CB ARG G 115 -8.653 -17.056 44.255 1.00 13.18 C ANISOU 706 CB ARG G 115 1633 1683 1691 16 47 64 C ATOM 707 CG ARG G 115 -8.843 -18.468 43.732 1.00 17.25 C ANISOU 707 CG ARG G 115 2152 2147 2255 48 135 78 C ATOM 708 CD ARG G 115 -8.551 -19.594 44.687 1.00 24.31 C ANISOU 708 CD ARG G 115 3158 3268 2808 104 62 47 C ATOM 709 NE ARG G 115 -8.999 -19.310 46.040 1.00 30.71 N ANISOU 709 NE ARG G 115 3887 4015 3766 33 -110 -62 N ATOM 710 CZ ARG G 115 -8.182 -19.014 47.062 1.00 35.46 C ANISOU 710 CZ ARG G 115 4472 4614 4384 -61 -71 -130 C ATOM 711 NH1 ARG G 115 -6.846 -18.943 46.891 1.00 36.50 N ANISOU 711 NH1 ARG G 115 4540 4667 4659 55 -148 -152 N ATOM 712 NH2 ARG G 115 -8.710 -18.789 48.260 1.00 36.21 N ANISOU 712 NH2 ARG G 115 4624 4712 4420 -58 4 -270 N ATOM 713 N ALA G 116 -8.314 -13.699 43.403 1.00 10.48 N ANISOU 713 N ALA G 116 1296 1414 1270 32 69 -39 N ATOM 714 CA ALA G 116 -8.685 -12.321 43.723 1.00 10.16 C ANISOU 714 CA ALA G 116 1313 1312 1234 35 64 -2 C ATOM 715 C ALA G 116 -9.551 -11.680 42.663 1.00 10.55 C ANISOU 715 C ALA G 116 1390 1302 1314 52 59 -15 C ATOM 716 O ALA G 116 -9.433 -11.981 41.470 1.00 10.66 O ANISOU 716 O ALA G 116 1491 1275 1282 236 24 23 O ATOM 717 CB ALA G 116 -7.448 -11.479 43.996 1.00 10.11 C ANISOU 717 CB ALA G 116 1346 1275 1219 33 122 15 C ATOM 718 N VAL G 117 -10.452 -10.816 43.114 1.00 10.54 N ANISOU 718 N VAL G 117 1339 1309 1356 15 54 -33 N ATOM 719 CA VAL G 117 -11.162 -9.877 42.248 1.00 11.02 C ANISOU 719 CA VAL G 117 1373 1404 1409 -46 9 -44 C ATOM 720 C VAL G 117 -10.438 -8.548 42.288 1.00 10.54 C ANISOU 720 C VAL G 117 1311 1338 1354 -53 29 -21 C ATOM 721 O VAL G 117 -10.145 -8.048 43.365 1.00 10.12 O ANISOU 721 O VAL G 117 1214 1091 1538 -164 118 -197 O ATOM 722 CB VAL G 117 -12.603 -9.672 42.746 1.00 11.34 C ANISOU 722 CB VAL G 117 1402 1433 1474 -16 29 -9 C ATOM 723 CG1 VAL G 117 -13.394 -8.736 41.816 1.00 12.46 C ANISOU 723 CG1 VAL G 117 1580 1524 1628 -101 16 -28 C ATOM 724 CG2 VAL G 117 -13.303 -11.053 42.872 1.00 13.44 C ANISOU 724 CG2 VAL G 117 1644 1665 1795 -81 56 -68 C ATOM 725 N GLN G 118 -10.174 -7.980 41.114 1.00 11.00 N ANISOU 725 N GLN G 118 1329 1402 1448 -79 8 -42 N ATOM 726 CA GLN G 118 -9.378 -6.759 40.953 1.00 10.51 C ANISOU 726 CA GLN G 118 1309 1300 1383 -32 8 -52 C ATOM 727 C GLN G 118 -10.300 -5.557 40.825 1.00 10.40 C ANISOU 727 C GLN G 118 1255 1402 1295 -24 14 -14 C ATOM 728 O GLN G 118 -11.328 -5.638 40.189 1.00 10.21 O ANISOU 728 O GLN G 118 1169 1497 1210 -3 78 -15 O ATOM 729 CB GLN G 118 -8.455 -6.857 39.730 1.00 9.47 C ANISOU 729 CB GLN G 118 1213 1192 1190 -78 24 -31 C ATOM 730 CG GLN G 118 -7.422 -8.036 39.818 1.00 9.25 C ANISOU 730 CG GLN G 118 1130 1336 1046 82 -51 9 C ATOM 731 CD GLN G 118 -6.487 -8.156 38.607 1.00 9.82 C ANISOU 731 CD GLN G 118 1034 1389 1306 165 -165 -24 C ATOM 732 OE1 GLN G 118 -5.883 -9.237 38.370 1.00 11.40 O ANISOU 732 OE1 GLN G 118 729 2130 1470 281 -333 25 O ATOM 733 NE2 GLN G 118 -6.347 -7.075 37.853 1.00 7.75 N ANISOU 733 NE2 GLN G 118 851 1207 885 489 -156 444 N ATOM 734 N HIS G 119 -9.918 -4.456 41.466 1.00 10.51 N ANISOU 734 N HIS G 119 1288 1327 1379 -24 58 -48 N ATOM 735 CA HIS G 119 -10.684 -3.224 41.468 1.00 11.14 C ANISOU 735 CA HIS G 119 1368 1429 1433 -6 -1 -31 C ATOM 736 C HIS G 119 -9.731 -2.048 41.272 1.00 10.34 C ANISOU 736 C HIS G 119 1264 1312 1351 0 34 -3 C ATOM 737 O HIS G 119 -8.773 -1.872 42.034 1.00 9.67 O ANISOU 737 O HIS G 119 1161 1221 1290 101 -19 -91 O ATOM 738 CB HIS G 119 -11.402 -3.014 42.820 1.00 11.45 C ANISOU 738 CB HIS G 119 1397 1483 1471 -43 55 -18 C ATOM 739 CG HIS G 119 -12.229 -4.175 43.274 1.00 14.24 C ANISOU 739 CG HIS G 119 1794 1662 1954 -56 -101 22 C ATOM 740 ND1 HIS G 119 -13.566 -4.304 42.959 1.00 17.86 N ANISOU 740 ND1 HIS G 119 2264 2012 2509 100 -176 375 N ATOM 741 CD2 HIS G 119 -11.919 -5.243 44.046 1.00 16.10 C ANISOU 741 CD2 HIS G 119 1944 2090 2082 -8 -274 102 C ATOM 742 CE1 HIS G 119 -14.037 -5.416 43.496 1.00 18.58 C ANISOU 742 CE1 HIS G 119 2378 2088 2592 -88 0 198 C ATOM 743 NE2 HIS G 119 -13.056 -6.003 44.166 1.00 17.28 N ANISOU 743 NE2 HIS G 119 2213 2108 2242 -43 -218 144 N ATOM 744 N ARG G 120 -10.001 -1.224 40.279 1.00 9.97 N ANISOU 744 N ARG G 120 1180 1350 1255 15 5 -57 N ATOM 745 CA ARG G 120 -9.282 0.032 40.129 1.00 9.71 C ANISOU 745 CA ARG G 120 1228 1240 1221 13 42 -4 C ATOM 746 C ARG G 120 -9.978 1.126 40.953 1.00 9.58 C ANISOU 746 C ARG G 120 1137 1299 1203 38 30 -7 C ATOM 747 O ARG G 120 -11.150 1.361 40.780 1.00 10.39 O ANISOU 747 O ARG G 120 1149 1514 1283 71 -27 -184 O ATOM 748 CB ARG G 120 -9.254 0.414 38.660 1.00 10.20 C ANISOU 748 CB ARG G 120 1315 1268 1293 67 46 -64 C ATOM 749 CG ARG G 120 -8.283 1.525 38.311 1.00 9.78 C ANISOU 749 CG ARG G 120 1202 1339 1172 -35 79 113 C ATOM 750 CD ARG G 120 -8.109 1.642 36.807 1.00 11.00 C ANISOU 750 CD ARG G 120 1488 1380 1311 -8 111 -168 C ATOM 751 NE ARG G 120 -7.205 2.716 36.441 1.00 12.71 N ANISOU 751 NE ARG G 120 1849 1649 1330 -68 132 -59 N ATOM 752 CZ ARG G 120 -7.575 3.954 36.143 1.00 14.23 C ANISOU 752 CZ ARG G 120 1948 1868 1589 -13 72 -66 C ATOM 753 NH1 ARG G 120 -8.835 4.309 36.167 1.00 13.97 N ANISOU 753 NH1 ARG G 120 1965 1772 1570 205 42 26 N ATOM 754 NH2 ARG G 120 -6.653 4.848 35.810 1.00 17.01 N ANISOU 754 NH2 ARG G 120 2617 2010 1836 -67 -4 -208 N ATOM 755 N GLU G 121 -9.264 1.760 41.867 1.00 9.43 N ANISOU 755 N GLU G 121 1056 1218 1309 -12 0 -3 N ATOM 756 CA GLU G 121 -9.811 2.816 42.703 1.00 10.21 C ANISOU 756 CA GLU G 121 1205 1279 1393 -7 -6 -5 C ATOM 757 C GLU G 121 -9.113 4.144 42.415 1.00 11.43 C ANISOU 757 C GLU G 121 1349 1385 1606 14 -53 22 C ATOM 758 O GLU G 121 -7.956 4.315 42.750 1.00 12.70 O ANISOU 758 O GLU G 121 1405 1434 1985 -52 -62 70 O ATOM 759 CB GLU G 121 -9.647 2.483 44.178 1.00 9.46 C ANISOU 759 CB GLU G 121 1123 1144 1325 37 -47 -16 C ATOM 760 CG GLU G 121 -10.215 1.136 44.627 1.00 10.61 C ANISOU 760 CG GLU G 121 1425 1325 1279 34 49 -121 C ATOM 761 CD GLU G 121 -11.726 1.002 44.513 1.00 11.53 C ANISOU 761 CD GLU G 121 1603 1315 1462 -71 8 -84 C ATOM 762 OE1 GLU G 121 -12.426 2.005 44.218 1.00 12.07 O ANISOU 762 OE1 GLU G 121 1833 1270 1484 -72 22 -51 O ATOM 763 OE2 GLU G 121 -12.223 -0.129 44.734 1.00 13.54 O ANISOU 763 OE2 GLU G 121 2096 1365 1682 -48 116 -35 O ATOM 764 N VAL G 122 -9.824 5.094 41.822 1.00 12.12 N ANISOU 764 N VAL G 122 1494 1480 1632 65 -55 23 N ATOM 765 CA VAL G 122 -9.284 6.437 41.584 1.00 12.01 C ANISOU 765 CA VAL G 122 1491 1489 1583 15 -24 33 C ATOM 766 C VAL G 122 -9.734 7.388 42.699 1.00 11.70 C ANISOU 766 C VAL G 122 1467 1400 1577 22 -35 51 C ATOM 767 O VAL G 122 -10.903 7.384 43.107 1.00 11.38 O ANISOU 767 O VAL G 122 1438 1320 1565 -6 -24 55 O ATOM 768 CB VAL G 122 -9.769 6.957 40.223 1.00 12.93 C ANISOU 768 CB VAL G 122 1670 1586 1657 -14 49 -10 C ATOM 769 CG1 VAL G 122 -9.330 8.404 39.980 1.00 13.85 C ANISOU 769 CG1 VAL G 122 1881 1659 1721 -48 -18 -42 C ATOM 770 CG2 VAL G 122 -9.304 6.015 39.079 1.00 14.55 C ANISOU 770 CG2 VAL G 122 1803 1811 1911 15 8 -73 C ATOM 771 N GLN G 123 -8.804 8.190 43.205 1.00 11.58 N ANISOU 771 N GLN G 123 1388 1434 1577 43 -19 84 N ATOM 772 CA GLN G 123 -9.098 9.260 44.164 1.00 11.88 C ANISOU 772 CA GLN G 123 1495 1514 1502 22 -15 49 C ATOM 773 C GLN G 123 -10.350 10.041 43.770 1.00 12.43 C ANISOU 773 C GLN G 123 1571 1546 1605 51 18 65 C ATOM 774 O GLN G 123 -10.480 10.457 42.642 1.00 11.83 O ANISOU 774 O GLN G 123 1607 1362 1525 62 22 244 O ATOM 775 CB GLN G 123 -7.922 10.227 44.254 1.00 11.90 C ANISOU 775 CB GLN G 123 1500 1516 1505 64 -15 52 C ATOM 776 CG GLN G 123 -8.049 11.275 45.362 1.00 12.21 C ANISOU 776 CG GLN G 123 1552 1520 1567 57 -30 -9 C ATOM 777 CD GLN G 123 -7.019 12.367 45.229 1.00 13.64 C ANISOU 777 CD GLN G 123 1670 1788 1724 171 -72 -102 C ATOM 778 OE1 GLN G 123 -5.876 12.079 44.943 1.00 14.44 O ANISOU 778 OE1 GLN G 123 1897 2002 1586 187 82 -351 O ATOM 779 NE2 GLN G 123 -7.428 13.626 45.420 1.00 14.98 N ANISOU 779 NE2 GLN G 123 2143 1876 1672 80 -43 -453 N ATOM 780 N GLY G 124 -11.296 10.179 44.691 1.00 13.70 N ANISOU 780 N GLY G 124 1732 1703 1767 52 0 33 N ATOM 781 CA GLY G 124 -12.536 10.907 44.421 1.00 13.94 C ANISOU 781 CA GLY G 124 1661 1779 1853 34 -37 32 C ATOM 782 C GLY G 124 -13.676 10.049 43.873 1.00 14.28 C ANISOU 782 C GLY G 124 1719 1809 1897 29 -21 38 C ATOM 783 O GLY G 124 -14.803 10.527 43.777 1.00 14.49 O ANISOU 783 O GLY G 124 1539 1802 2163 97 -102 102 O ATOM 784 N PHE G 125 -13.396 8.790 43.542 1.00 13.95 N ANISOU 784 N PHE G 125 1702 1756 1839 45 -5 77 N ATOM 785 CA PHE G 125 -14.354 7.903 42.878 1.00 14.40 C ANISOU 785 CA PHE G 125 1787 1812 1871 -15 24 59 C ATOM 786 C PHE G 125 -14.284 6.477 43.387 1.00 13.51 C ANISOU 786 C PHE G 125 1682 1703 1747 -58 81 28 C ATOM 787 O PHE G 125 -14.601 5.540 42.655 1.00 13.57 O ANISOU 787 O PHE G 125 1650 1718 1788 -340 143 104 O ATOM 788 CB PHE G 125 -14.096 7.872 41.369 1.00 15.07 C ANISOU 788 CB PHE G 125 1854 1879 1990 6 23 39 C ATOM 789 CG PHE G 125 -14.256 9.194 40.714 1.00 18.47 C ANISOU 789 CG PHE G 125 2239 2311 2465 16 -84 233 C ATOM 790 CD1 PHE G 125 -13.175 10.049 40.594 1.00 22.34 C ANISOU 790 CD1 PHE G 125 2768 2761 2959 -2 -157 246 C ATOM 791 CD2 PHE G 125 -15.493 9.598 40.239 1.00 22.51 C ANISOU 791 CD2 PHE G 125 2781 2823 2947 -11 -199 234 C ATOM 792 CE1 PHE G 125 -13.312 11.294 40.002 1.00 24.68 C ANISOU 792 CE1 PHE G 125 3038 3114 3224 -14 -123 309 C ATOM 793 CE2 PHE G 125 -15.646 10.849 39.648 1.00 23.62 C ANISOU 793 CE2 PHE G 125 2957 2901 3117 -133 -270 372 C ATOM 794 CZ PHE G 125 -14.550 11.697 39.527 1.00 24.79 C ANISOU 794 CZ PHE G 125 2969 3209 3239 6 -238 321 C ATOM 795 N GLU G 126 -13.859 6.303 44.627 1.00 12.67 N ANISOU 795 N GLU G 126 1624 1548 1643 -48 69 7 N ATOM 796 CA GLU G 126 -13.633 4.964 45.146 1.00 12.45 C ANISOU 796 CA GLU G 126 1529 1637 1561 38 50 -18 C ATOM 797 C GLU G 126 -14.960 4.250 45.370 1.00 12.01 C ANISOU 797 C GLU G 126 1475 1616 1470 -1 36 8 C ATOM 798 O GLU G 126 -15.962 4.883 45.665 1.00 12.74 O ANISOU 798 O GLU G 126 1368 1969 1503 -68 -3 -60 O ATOM 799 CB GLU G 126 -12.820 5.015 46.432 1.00 12.38 C ANISOU 799 CB GLU G 126 1561 1546 1594 42 63 -43 C ATOM 800 CG GLU G 126 -11.452 5.669 46.292 1.00 11.68 C ANISOU 800 CG GLU G 126 1494 1386 1556 197 76 -60 C ATOM 801 CD GLU G 126 -11.444 7.103 46.755 1.00 12.87 C ANISOU 801 CD GLU G 126 1542 1475 1872 52 100 -111 C ATOM 802 OE1 GLU G 126 -12.495 7.771 46.633 1.00 11.66 O ANISOU 802 OE1 GLU G 126 1358 885 2187 478 175 -101 O ATOM 803 OE2 GLU G 126 -10.404 7.556 47.249 1.00 12.80 O ANISOU 803 OE2 GLU G 126 1216 1699 1949 25 188 -551 O ATOM 804 N SER G 127 -14.939 2.937 45.262 1.00 12.14 N ANISOU 804 N SER G 127 1457 1687 1467 -40 66 -89 N ATOM 805 CA SER G 127 -16.110 2.102 45.510 1.00 12.72 C ANISOU 805 CA SER G 127 1586 1677 1569 -34 21 -45 C ATOM 806 C SER G 127 -16.516 2.129 46.989 1.00 12.61 C ANISOU 806 C SER G 127 1571 1681 1539 -42 40 1 C ATOM 807 O SER G 127 -15.680 2.330 47.873 1.00 11.06 O ANISOU 807 O SER G 127 1362 1434 1404 -183 -46 -68 O ATOM 808 CB SER G 127 -15.871 0.659 45.029 1.00 12.64 C ANISOU 808 CB SER G 127 1459 1684 1658 -32 57 -43 C ATOM 809 OG SER G 127 -14.989 -0.070 45.870 1.00 11.93 O ANISOU 809 OG SER G 127 1679 1530 1321 -87 148 -114 O ATOM 810 N ALA G 128 -17.810 1.967 47.233 1.00 13.29 N ANISOU 810 N ALA G 128 1639 1734 1675 -67 -55 -14 N ATOM 811 CA ALA G 128 -18.353 1.838 48.583 1.00 13.87 C ANISOU 811 CA ALA G 128 1741 1832 1694 -11 15 -38 C ATOM 812 C ALA G 128 -17.667 0.711 49.359 1.00 14.92 C ANISOU 812 C ALA G 128 1879 1991 1797 0 48 -67 C ATOM 813 O ALA G 128 -17.400 0.883 50.556 1.00 15.51 O ANISOU 813 O ALA G 128 2092 2131 1668 139 1 -173 O ATOM 814 CB ALA G 128 -19.897 1.595 48.545 1.00 14.88 C ANISOU 814 CB ALA G 128 1884 1932 1836 62 0 -92 C ATOM 815 N THR G 129 -17.347 -0.426 48.729 1.00 14.64 N ANISOU 815 N THR G 129 1928 1863 1770 -68 83 -75 N ATOM 816 CA THR G 129 -16.719 -1.482 49.526 1.00 15.48 C ANISOU 816 CA THR G 129 1974 1953 1952 -42 69 -77 C ATOM 817 C THR G 129 -15.310 -1.134 49.942 1.00 14.03 C ANISOU 817 C THR G 129 1809 1734 1786 -62 98 -41 C ATOM 818 O THR G 129 -14.928 -1.410 51.073 1.00 13.45 O ANISOU 818 O THR G 129 1735 1598 1774 -159 178 -146 O ATOM 819 CB THR G 129 -16.802 -2.965 48.971 1.00 16.59 C ANISOU 819 CB THR G 129 2071 2175 2058 33 83 -117 C ATOM 820 OG1 THR G 129 -15.510 -3.435 48.604 1.00 20.17 O ANISOU 820 OG1 THR G 129 2420 2825 2418 -26 420 -303 O ATOM 821 CG2 THR G 129 -17.647 -3.151 47.764 1.00 18.16 C ANISOU 821 CG2 THR G 129 2419 2356 2125 19 -45 -96 C ATOM 822 N PHE G 130 -14.554 -0.488 49.055 1.00 13.33 N ANISOU 822 N PHE G 130 1702 1673 1688 -49 92 -72 N ATOM 823 CA PHE G 130 -13.248 0.033 49.413 1.00 12.14 C ANISOU 823 CA PHE G 130 1528 1532 1552 -32 51 -12 C ATOM 824 C PHE G 130 -13.334 1.029 50.558 1.00 11.66 C ANISOU 824 C PHE G 130 1458 1486 1485 -29 70 -28 C ATOM 825 O PHE G 130 -12.580 0.930 51.522 1.00 12.38 O ANISOU 825 O PHE G 130 1594 1487 1620 9 160 50 O ATOM 826 CB PHE G 130 -12.559 0.696 48.200 1.00 11.91 C ANISOU 826 CB PHE G 130 1552 1466 1507 -31 56 -79 C ATOM 827 CG PHE G 130 -11.139 1.097 48.462 1.00 10.95 C ANISOU 827 CG PHE G 130 1370 1388 1402 -63 93 -108 C ATOM 828 CD1 PHE G 130 -10.141 0.142 48.552 1.00 10.52 C ANISOU 828 CD1 PHE G 130 1264 1306 1427 -157 91 -400 C ATOM 829 CD2 PHE G 130 -10.810 2.424 48.659 1.00 12.29 C ANISOU 829 CD2 PHE G 130 1389 1536 1742 -58 57 -33 C ATOM 830 CE1 PHE G 130 -8.833 0.509 48.796 1.00 13.18 C ANISOU 830 CE1 PHE G 130 1677 1638 1693 61 121 -443 C ATOM 831 CE2 PHE G 130 -9.486 2.809 48.911 1.00 13.08 C ANISOU 831 CE2 PHE G 130 1648 1664 1656 2 -40 -28 C ATOM 832 CZ PHE G 130 -8.502 1.857 48.963 1.00 12.47 C ANISOU 832 CZ PHE G 130 1442 1552 1743 -73 156 17 C ATOM 833 N LEU G 131 -14.231 2.003 50.449 1.00 11.34 N ANISOU 833 N LEU G 131 1427 1447 1435 -76 0 -42 N ATOM 834 CA LEU G 131 -14.388 3.016 51.503 1.00 11.44 C ANISOU 834 CA LEU G 131 1454 1450 1440 -52 -1 -57 C ATOM 835 C LEU G 131 -14.763 2.378 52.860 1.00 11.31 C ANISOU 835 C LEU G 131 1491 1396 1411 -84 17 -28 C ATOM 836 O LEU G 131 -14.320 2.823 53.919 1.00 10.72 O ANISOU 836 O LEU G 131 1533 1286 1252 -100 113 21 O ATOM 837 CB LEU G 131 -15.406 4.076 51.081 1.00 11.18 C ANISOU 837 CB LEU G 131 1482 1325 1440 -133 -89 -106 C ATOM 838 CG LEU G 131 -14.995 4.917 49.865 1.00 11.99 C ANISOU 838 CG LEU G 131 1494 1584 1476 -74 -3 -109 C ATOM 839 CD1 LEU G 131 -16.158 5.758 49.308 1.00 13.50 C ANISOU 839 CD1 LEU G 131 1591 1708 1829 -29 84 -100 C ATOM 840 CD2 LEU G 131 -13.827 5.834 50.204 1.00 13.28 C ANISOU 840 CD2 LEU G 131 1711 1783 1548 -144 66 32 C ATOM 841 N GLY G 132 -15.517 1.290 52.813 1.00 11.88 N ANISOU 841 N GLY G 132 1543 1520 1451 -54 15 -14 N ATOM 842 CA GLY G 132 -15.958 0.593 54.010 1.00 12.13 C ANISOU 842 CA GLY G 132 1605 1516 1487 -25 3 2 C ATOM 843 C GLY G 132 -14.851 -0.143 54.750 1.00 12.51 C ANISOU 843 C GLY G 132 1671 1570 1510 -52 2 -14 C ATOM 844 O GLY G 132 -15.086 -0.599 55.874 1.00 10.26 O ANISOU 844 O GLY G 132 1579 1400 917 -182 197 -36 O ATOM 845 N TYR G 133 -13.669 -0.286 54.131 1.00 12.39 N ANISOU 845 N TYR G 133 1670 1568 1470 -51 36 11 N ATOM 846 CA TYR G 133 -12.526 -0.913 54.798 1.00 13.61 C ANISOU 846 CA TYR G 133 1776 1716 1676 -26 32 -11 C ATOM 847 C TYR G 133 -11.929 -0.041 55.923 1.00 14.41 C ANISOU 847 C TYR G 133 1879 1854 1740 -2 35 37 C ATOM 848 O TYR G 133 -11.181 -0.539 56.780 1.00 14.30 O ANISOU 848 O TYR G 133 2014 1956 1464 12 25 218 O ATOM 849 CB TYR G 133 -11.403 -1.244 53.795 1.00 13.42 C ANISOU 849 CB TYR G 133 1798 1676 1622 -59 102 32 C ATOM 850 CG TYR G 133 -11.716 -2.276 52.696 1.00 12.07 C ANISOU 850 CG TYR G 133 1608 1489 1486 -128 56 4 C ATOM 851 CD1 TYR G 133 -12.781 -3.165 52.789 1.00 13.72 C ANISOU 851 CD1 TYR G 133 1788 1650 1772 -64 79 -124 C ATOM 852 CD2 TYR G 133 -10.901 -2.363 51.590 1.00 11.29 C ANISOU 852 CD2 TYR G 133 1443 1404 1442 -14 15 -127 C ATOM 853 CE1 TYR G 133 -13.049 -4.093 51.770 1.00 10.70 C ANISOU 853 CE1 TYR G 133 1691 1062 1312 -34 318 -124 C ATOM 854 CE2 TYR G 133 -11.146 -3.253 50.585 1.00 12.60 C ANISOU 854 CE2 TYR G 133 1764 1316 1706 -51 381 -79 C ATOM 855 CZ TYR G 133 -12.214 -4.140 50.671 1.00 12.48 C ANISOU 855 CZ TYR G 133 1651 1414 1674 -57 48 -46 C ATOM 856 OH TYR G 133 -12.407 -5.064 49.656 1.00 12.47 O ANISOU 856 OH TYR G 133 2149 819 1767 128 366 58 O ATOM 857 N PHE G 134 -12.246 1.252 55.904 1.00 14.79 N ANISOU 857 N PHE G 134 1904 1898 1817 10 56 24 N ATOM 858 CA PHE G 134 -11.608 2.239 56.768 1.00 15.37 C ANISOU 858 CA PHE G 134 1950 1933 1956 45 49 -19 C ATOM 859 C PHE G 134 -12.655 2.788 57.715 1.00 16.67 C ANISOU 859 C PHE G 134 2150 2120 2062 31 53 -23 C ATOM 860 O PHE G 134 -13.442 3.677 57.363 1.00 16.03 O ANISOU 860 O PHE G 134 2175 1922 1992 120 109 -81 O ATOM 861 CB PHE G 134 -10.936 3.329 55.900 1.00 14.91 C ANISOU 861 CB PHE G 134 1925 1898 1841 7 61 25 C ATOM 862 CG PHE G 134 -9.968 2.759 54.892 1.00 12.91 C ANISOU 862 CG PHE G 134 1636 1550 1719 110 52 25 C ATOM 863 CD1 PHE G 134 -10.378 2.479 53.607 1.00 11.40 C ANISOU 863 CD1 PHE G 134 1397 1448 1484 146 87 -99 C ATOM 864 CD2 PHE G 134 -8.664 2.456 55.254 1.00 12.69 C ANISOU 864 CD2 PHE G 134 1520 1723 1576 -100 89 -90 C ATOM 865 CE1 PHE G 134 -9.499 1.910 52.684 1.00 12.98 C ANISOU 865 CE1 PHE G 134 1492 1748 1690 -51 71 83 C ATOM 866 CE2 PHE G 134 -7.776 1.886 54.339 1.00 11.99 C ANISOU 866 CE2 PHE G 134 1333 1558 1663 57 82 0 C ATOM 867 CZ PHE G 134 -8.197 1.599 53.061 1.00 11.22 C ANISOU 867 CZ PHE G 134 1146 1644 1473 123 75 12 C ATOM 868 N LYS G 135 -12.665 2.221 58.912 1.00 18.29 N ANISOU 868 N LYS G 135 2355 2285 2310 84 27 10 N ATOM 869 CA LYS G 135 -13.757 2.410 59.862 1.00 20.15 C ANISOU 869 CA LYS G 135 2569 2548 2537 23 7 22 C ATOM 870 C LYS G 135 -13.975 3.845 60.283 1.00 19.83 C ANISOU 870 C LYS G 135 2559 2494 2480 31 18 0 C ATOM 871 O LYS G 135 -15.110 4.247 60.496 1.00 19.77 O ANISOU 871 O LYS G 135 2511 2564 2436 32 77 17 O ATOM 872 CB LYS G 135 -13.547 1.536 61.101 1.00 20.82 C ANISOU 872 CB LYS G 135 2648 2606 2654 7 11 33 C ATOM 873 CG LYS G 135 -13.640 0.026 60.821 1.00 25.27 C ANISOU 873 CG LYS G 135 3161 3186 3252 66 -47 -15 C ATOM 874 CD LYS G 135 -14.632 -0.385 59.691 1.00 29.00 C ANISOU 874 CD LYS G 135 3596 3749 3672 43 -68 -13 C ATOM 875 CE LYS G 135 -16.069 0.079 59.950 1.00 31.35 C ANISOU 875 CE LYS G 135 3855 4029 4028 -82 -61 37 C ATOM 876 NZ LYS G 135 -16.949 -1.071 60.277 1.00 33.85 N ANISOU 876 NZ LYS G 135 4099 4343 4416 -274 -262 96 N ATOM 877 N SER G 136 -12.902 4.617 60.388 1.00 19.75 N ANISOU 877 N SER G 136 2556 2506 2440 7 4 18 N ATOM 878 CA SER G 136 -13.033 6.028 60.751 1.00 20.26 C ANISOU 878 CA SER G 136 2624 2561 2510 6 11 -5 C ATOM 879 C SER G 136 -12.897 6.969 59.531 1.00 19.46 C ANISOU 879 C SER G 136 2538 2393 2461 -6 14 -10 C ATOM 880 O SER G 136 -12.748 8.173 59.689 1.00 19.14 O ANISOU 880 O SER G 136 2678 2202 2390 48 59 -135 O ATOM 881 CB SER G 136 -12.032 6.375 61.853 1.00 20.49 C ANISOU 881 CB SER G 136 2561 2624 2598 -32 25 -62 C ATOM 882 OG SER G 136 -10.724 6.372 61.347 1.00 23.97 O ANISOU 882 OG SER G 136 2934 3202 2970 110 9 -10 O ATOM 883 N GLY G 137 -12.975 6.400 58.327 1.00 18.03 N ANISOU 883 N GLY G 137 2365 2224 2258 45 55 -32 N ATOM 884 CA GLY G 137 -13.043 7.144 57.085 1.00 17.70 C ANISOU 884 CA GLY G 137 2282 2211 2229 13 37 17 C ATOM 885 C GLY G 137 -11.652 7.367 56.519 1.00 17.61 C ANISOU 885 C GLY G 137 2261 2212 2217 -11 3 62 C ATOM 886 O GLY G 137 -10.763 7.829 57.232 1.00 17.32 O ANISOU 886 O GLY G 137 2238 2249 2093 -54 -39 146 O ATOM 887 N LEU G 138 -11.454 7.070 55.237 1.00 17.14 N ANISOU 887 N LEU G 138 2188 2108 2214 21 12 -2 N ATOM 888 CA LEU G 138 -10.148 7.317 54.640 1.00 17.71 C ANISOU 888 CA LEU G 138 2295 2174 2257 42 -1 13 C ATOM 889 C LEU G 138 -9.923 8.828 54.451 1.00 17.74 C ANISOU 889 C LEU G 138 2275 2222 2241 39 9 63 C ATOM 890 O LEU G 138 -10.881 9.612 54.388 1.00 16.67 O ANISOU 890 O LEU G 138 2169 1897 2266 178 67 40 O ATOM 891 CB LEU G 138 -9.915 6.461 53.380 1.00 18.18 C ANISOU 891 CB LEU G 138 2350 2259 2296 -8 0 12 C ATOM 892 CG LEU G 138 -10.436 6.842 52.012 1.00 19.52 C ANISOU 892 CG LEU G 138 2524 2393 2496 29 -26 2 C ATOM 893 CD1 LEU G 138 -9.851 8.160 51.572 1.00 21.60 C ANISOU 893 CD1 LEU G 138 2676 2717 2812 2 39 -47 C ATOM 894 CD2 LEU G 138 -10.109 5.746 50.959 1.00 20.01 C ANISOU 894 CD2 LEU G 138 2543 2504 2553 100 57 -94 C ATOM 895 N LYS G 139 -8.655 9.225 54.449 1.00 17.65 N ANISOU 895 N LYS G 139 2193 2277 2234 57 40 77 N ATOM 896 CA LYS G 139 -8.277 10.615 54.289 1.00 18.24 C ANISOU 896 CA LYS G 139 2284 2353 2292 43 26 25 C ATOM 897 C LYS G 139 -7.122 10.784 53.283 1.00 17.07 C ANISOU 897 C LYS G 139 2123 2222 2138 61 37 55 C ATOM 898 O LYS G 139 -6.322 9.873 53.054 1.00 16.60 O ANISOU 898 O LYS G 139 2025 2275 2004 170 141 171 O ATOM 899 CB LYS G 139 -7.970 11.266 55.650 1.00 19.89 C ANISOU 899 CB LYS G 139 2388 2609 2559 27 -26 85 C ATOM 900 CG LYS G 139 -6.665 10.837 56.317 1.00 24.27 C ANISOU 900 CG LYS G 139 3026 3081 3113 -52 14 100 C ATOM 901 CD LYS G 139 -5.512 11.880 56.118 1.00 29.29 C ANISOU 901 CD LYS G 139 3787 3615 3726 -88 -26 40 C ATOM 902 CE LYS G 139 -5.611 13.071 57.063 1.00 30.95 C ANISOU 902 CE LYS G 139 4060 3742 3957 -54 -44 -8 C ATOM 903 NZ LYS G 139 -5.320 14.389 56.375 1.00 32.09 N ANISOU 903 NZ LYS G 139 4175 3674 4343 -268 -14 94 N ATOM 904 N TYR G 140 -7.102 11.942 52.644 1.00 15.43 N ANISOU 904 N TYR G 140 1950 1983 1928 53 37 28 N ATOM 905 CA TYR G 140 -6.112 12.278 51.639 1.00 14.59 C ANISOU 905 CA TYR G 140 1841 1876 1824 29 0 -27 C ATOM 906 C TYR G 140 -5.118 13.262 52.243 1.00 14.42 C ANISOU 906 C TYR G 140 1871 1847 1758 47 -23 -28 C ATOM 907 O TYR G 140 -5.502 14.118 53.018 1.00 14.61 O ANISOU 907 O TYR G 140 1880 1985 1685 17 -88 -207 O ATOM 908 CB TYR G 140 -6.793 12.954 50.454 1.00 14.59 C ANISOU 908 CB TYR G 140 1867 1940 1733 -15 52 -80 C ATOM 909 CG TYR G 140 -7.894 12.157 49.763 1.00 13.44 C ANISOU 909 CG TYR G 140 1678 1813 1615 -102 86 -91 C ATOM 910 CD1 TYR G 140 -8.953 12.807 49.141 1.00 11.44 C ANISOU 910 CD1 TYR G 140 1094 1670 1580 -65 167 -250 C ATOM 911 CD2 TYR G 140 -7.830 10.767 49.654 1.00 13.86 C ANISOU 911 CD2 TYR G 140 1755 1801 1707 -45 51 24 C ATOM 912 CE1 TYR G 140 -9.949 12.081 48.470 1.00 14.14 C ANISOU 912 CE1 TYR G 140 1609 2014 1748 265 27 -253 C ATOM 913 CE2 TYR G 140 -8.836 10.034 48.981 1.00 13.17 C ANISOU 913 CE2 TYR G 140 1514 1851 1637 97 -64 -227 C ATOM 914 CZ TYR G 140 -9.890 10.704 48.403 1.00 14.06 C ANISOU 914 CZ TYR G 140 1579 2043 1720 -2 39 -314 C ATOM 915 OH TYR G 140 -10.885 10.002 47.734 1.00 14.36 O ANISOU 915 OH TYR G 140 1438 2412 1606 306 151 -852 O ATOM 916 N LYS G 141 -3.851 13.130 51.879 1.00 14.00 N ANISOU 916 N LYS G 141 1840 1793 1684 16 -57 2 N ATOM 917 CA LYS G 141 -2.840 14.126 52.172 1.00 14.54 C ANISOU 917 CA LYS G 141 1908 1830 1787 19 -25 18 C ATOM 918 C LYS G 141 -1.995 14.369 50.934 1.00 14.49 C ANISOU 918 C LYS G 141 1933 1810 1763 1 -40 48 C ATOM 919 O LYS G 141 -1.754 13.446 50.158 1.00 13.96 O ANISOU 919 O LYS G 141 2010 1662 1630 -45 -8 135 O ATOM 920 CB LYS G 141 -1.954 13.693 53.346 1.00 15.10 C ANISOU 920 CB LYS G 141 1967 1860 1907 10 -73 48 C ATOM 921 CG LYS G 141 -1.299 12.320 53.209 1.00 16.58 C ANISOU 921 CG LYS G 141 2091 2150 2055 99 -24 47 C ATOM 922 CD LYS G 141 -0.647 11.886 54.561 1.00 18.32 C ANISOU 922 CD LYS G 141 2218 2377 2365 8 -61 127 C ATOM 923 CE LYS G 141 -0.046 10.457 54.473 1.00 18.17 C ANISOU 923 CE LYS G 141 2257 2340 2304 -5 -46 97 C ATOM 924 NZ LYS G 141 0.839 10.078 55.636 1.00 17.48 N ANISOU 924 NZ LYS G 141 2119 2352 2168 -148 -103 211 N ATOM 925 N LYS G 142 -1.548 15.610 50.747 1.00 14.62 N ANISOU 925 N LYS G 142 1945 1819 1789 13 -54 21 N ATOM 926 CA LYS G 142 -0.697 15.956 49.607 1.00 14.73 C ANISOU 926 CA LYS G 142 1926 1812 1856 16 -47 28 C ATOM 927 C LYS G 142 0.709 15.408 49.786 1.00 14.76 C ANISOU 927 C LYS G 142 1984 1772 1852 21 -35 11 C ATOM 928 O LYS G 142 1.197 15.253 50.911 1.00 14.60 O ANISOU 928 O LYS G 142 2055 1624 1868 127 -186 19 O ATOM 929 CB LYS G 142 -0.634 17.477 49.426 1.00 15.61 C ANISOU 929 CB LYS G 142 2010 1990 1930 18 -22 -21 C ATOM 930 CG LYS G 142 -2.002 18.141 49.166 1.00 16.76 C ANISOU 930 CG LYS G 142 2135 2054 2177 107 -116 34 C ATOM 931 CD LYS G 142 -2.598 17.770 47.784 1.00 19.81 C ANISOU 931 CD LYS G 142 2418 2598 2509 93 -150 -83 C ATOM 932 CE LYS G 142 -3.941 18.512 47.566 1.00 21.22 C ANISOU 932 CE LYS G 142 2698 2721 2641 1 -207 -72 C ATOM 933 NZ LYS G 142 -4.770 18.022 46.402 1.00 23.07 N ANISOU 933 NZ LYS G 142 2901 3131 2732 -115 -216 103 N ATOM 934 N GLY G 143 1.349 15.099 48.669 1.00 14.84 N ANISOU 934 N GLY G 143 1932 1824 1881 37 -43 3 N ATOM 935 CA GLY G 143 2.756 14.733 48.645 1.00 15.22 C ANISOU 935 CA GLY G 143 1961 1940 1883 13 -55 -12 C ATOM 936 C GLY G 143 2.960 13.285 48.249 1.00 15.02 C ANISOU 936 C GLY G 143 1936 1920 1849 7 -32 26 C ATOM 937 O GLY G 143 2.054 12.645 47.729 1.00 14.22 O ANISOU 937 O GLY G 143 1811 1952 1638 -23 -59 70 O ATOM 938 N GLY G 144 4.160 12.775 48.502 1.00 15.20 N ANISOU 938 N GLY G 144 1876 1976 1923 0 -19 -26 N ATOM 939 CA GLY G 144 4.458 11.373 48.310 1.00 15.27 C ANISOU 939 CA GLY G 144 1891 1960 1948 -24 -1 -2 C ATOM 940 C GLY G 144 5.911 11.118 47.949 1.00 15.59 C ANISOU 940 C GLY G 144 1882 1988 2053 -30 1 -19 C ATOM 941 O GLY G 144 6.770 12.009 48.011 1.00 15.13 O ANISOU 941 O GLY G 144 1736 1909 2101 -154 -7 -74 O ATOM 942 N VAL G 145 6.175 9.873 47.583 1.00 14.89 N ANISOU 942 N VAL G 145 1845 1900 1911 -68 -3 -99 N ATOM 943 CA VAL G 145 7.507 9.442 47.176 1.00 15.20 C ANISOU 943 CA VAL G 145 1875 1975 1924 -74 -18 -60 C ATOM 944 C VAL G 145 7.752 9.840 45.713 1.00 14.70 C ANISOU 944 C VAL G 145 1801 1944 1839 -72 30 -101 C ATOM 945 O VAL G 145 6.808 9.933 44.905 1.00 14.69 O ANISOU 945 O VAL G 145 1759 2096 1724 -103 63 -52 O ATOM 946 CB VAL G 145 7.706 7.931 47.450 1.00 15.58 C ANISOU 946 CB VAL G 145 1902 2013 2004 -30 24 -60 C ATOM 947 CG1 VAL G 145 6.659 7.085 46.716 1.00 15.88 C ANISOU 947 CG1 VAL G 145 2029 1974 2029 -114 8 -86 C ATOM 948 CG2 VAL G 145 9.113 7.475 47.081 1.00 18.00 C ANISOU 948 CG2 VAL G 145 2164 2309 2365 -68 -55 -4 C ATOM 949 N ALA G 146 9.012 10.127 45.389 1.00 14.33 N ANISOU 949 N ALA G 146 1752 1917 1773 -78 -14 -114 N ATOM 950 CA ALA G 146 9.392 10.581 44.054 1.00 13.49 C ANISOU 950 CA ALA G 146 1691 1746 1687 -76 6 -55 C ATOM 951 C ALA G 146 9.276 9.432 43.048 1.00 13.11 C ANISOU 951 C ALA G 146 1658 1722 1602 -28 55 -66 C ATOM 952 O ALA G 146 9.402 8.256 43.400 1.00 11.76 O ANISOU 952 O ALA G 146 1587 1521 1360 32 95 -78 O ATOM 953 CB ALA G 146 10.814 11.109 44.050 1.00 14.51 C ANISOU 953 CB ALA G 146 1855 1845 1810 -72 3 -56 C ATOM 954 N SER G 147 9.032 9.807 41.799 1.00 11.94 N ANISOU 954 N SER G 147 1542 1594 1400 -37 14 -16 N ATOM 955 CA SER G 147 9.010 8.864 40.693 1.00 12.09 C ANISOU 955 CA SER G 147 1538 1578 1479 -48 -3 6 C ATOM 956 C SER G 147 10.305 8.047 40.607 1.00 11.71 C ANISOU 956 C SER G 147 1483 1538 1426 -25 22 -51 C ATOM 957 O SER G 147 11.407 8.559 40.858 1.00 11.51 O ANISOU 957 O SER G 147 1327 1685 1358 -64 -33 -145 O ATOM 958 CB SER G 147 8.760 9.616 39.364 1.00 11.64 C ANISOU 958 CB SER G 147 1519 1573 1331 -24 -15 26 C ATOM 959 OG SER G 147 8.808 8.718 38.260 1.00 11.94 O ANISOU 959 OG SER G 147 1824 1290 1421 11 -217 283 O ATOM 960 N GLY G 148 10.162 6.784 40.221 1.00 11.69 N ANISOU 960 N GLY G 148 1449 1510 1480 -78 42 35 N ATOM 961 CA GLY G 148 11.292 5.926 39.882 1.00 11.32 C ANISOU 961 CA GLY G 148 1434 1436 1430 0 -4 -2 C ATOM 962 C GLY G 148 11.872 6.096 38.485 1.00 11.18 C ANISOU 962 C GLY G 148 1430 1454 1365 19 -28 8 C ATOM 963 O GLY G 148 12.953 5.561 38.192 1.00 10.68 O ANISOU 963 O GLY G 148 1244 1522 1292 176 -109 55 O ATOM 964 N PHE G 149 11.156 6.794 37.601 1.00 11.27 N ANISOU 964 N PHE G 149 1430 1380 1471 10 -3 -34 N ATOM 965 CA PHE G 149 11.658 7.027 36.236 1.00 11.01 C ANISOU 965 CA PHE G 149 1398 1402 1381 -24 41 -26 C ATOM 966 C PHE G 149 12.895 7.932 36.215 1.00 12.03 C ANISOU 966 C PHE G 149 1546 1494 1530 -39 8 -38 C ATOM 967 O PHE G 149 12.981 8.909 36.951 1.00 11.63 O ANISOU 967 O PHE G 149 1451 1413 1553 -97 13 -174 O ATOM 968 CB PHE G 149 10.625 7.718 35.347 1.00 10.90 C ANISOU 968 CB PHE G 149 1316 1426 1398 9 66 -21 C ATOM 969 CG PHE G 149 9.619 6.801 34.679 1.00 10.59 C ANISOU 969 CG PHE G 149 1375 1372 1275 29 27 1 C ATOM 970 CD1 PHE G 149 8.344 7.288 34.408 1.00 9.49 C ANISOU 970 CD1 PHE G 149 921 1470 1211 59 164 -10 C ATOM 971 CD2 PHE G 149 9.929 5.509 34.270 1.00 10.81 C ANISOU 971 CD2 PHE G 149 1172 1508 1426 -40 -119 -97 C ATOM 972 CE1 PHE G 149 7.398 6.513 33.772 1.00 9.36 C ANISOU 972 CE1 PHE G 149 845 1447 1264 -70 185 15 C ATOM 973 CE2 PHE G 149 8.955 4.700 33.633 1.00 11.36 C ANISOU 973 CE2 PHE G 149 1369 1546 1401 -72 139 -59 C ATOM 974 CZ PHE G 149 7.691 5.213 33.382 1.00 8.08 C ANISOU 974 CZ PHE G 149 877 1055 1139 -6 42 0 C ATOM 975 N LYS G 150 13.824 7.607 35.328 1.00 12.22 N ANISOU 975 N LYS G 150 1546 1498 1599 -12 53 -14 N ATOM 976 CA LYS G 150 14.853 8.536 34.900 1.00 13.92 C ANISOU 976 CA LYS G 150 1766 1746 1776 -15 -29 -10 C ATOM 977 C LYS G 150 14.312 9.298 33.674 1.00 14.03 C ANISOU 977 C LYS G 150 1812 1777 1741 -29 29 24 C ATOM 978 O LYS G 150 13.694 8.713 32.777 1.00 13.19 O ANISOU 978 O LYS G 150 1719 1639 1651 -53 -46 140 O ATOM 979 CB LYS G 150 16.134 7.778 34.580 1.00 14.32 C ANISOU 979 CB LYS G 150 1786 1807 1847 -49 54 -23 C ATOM 980 CG LYS G 150 17.299 8.663 34.137 1.00 18.86 C ANISOU 980 CG LYS G 150 2299 2354 2512 88 -75 -43 C ATOM 981 CD LYS G 150 18.674 8.025 34.482 1.00 24.33 C ANISOU 981 CD LYS G 150 2997 3060 3186 128 -32 -67 C ATOM 982 CE LYS G 150 19.236 7.181 33.320 1.00 26.82 C ANISOU 982 CE LYS G 150 3321 3289 3580 164 -77 -93 C ATOM 983 NZ LYS G 150 20.211 6.117 33.787 1.00 27.69 N ANISOU 983 NZ LYS G 150 3222 3266 4033 236 -218 -123 N ATOM 984 N HIS G 151 14.501 10.604 33.662 1.00 14.69 N ANISOU 984 N HIS G 151 1896 1834 1849 -44 -15 27 N ATOM 985 CA HIS G 151 14.018 11.430 32.569 1.00 16.43 C ANISOU 985 CA HIS G 151 2131 2067 2042 -42 -50 0 C ATOM 986 C HIS G 151 15.045 11.434 31.430 1.00 16.55 C ANISOU 986 C HIS G 151 2099 2096 2090 -37 -27 33 C ATOM 987 O HIS G 151 16.224 11.656 31.645 1.00 15.74 O ANISOU 987 O HIS G 151 1990 2065 1925 -156 -109 24 O ATOM 988 CB HIS G 151 13.731 12.861 33.039 1.00 17.56 C ANISOU 988 CB HIS G 151 2278 2162 2229 7 -115 60 C ATOM 989 CG HIS G 151 13.202 13.746 31.956 1.00 20.85 C ANISOU 989 CG HIS G 151 2864 2537 2520 -135 -241 161 C ATOM 990 ND1 HIS G 151 12.132 13.383 31.164 1.00 24.45 N ANISOU 990 ND1 HIS G 151 3297 3064 2928 -237 -343 366 N ATOM 991 CD2 HIS G 151 13.598 14.967 31.521 1.00 23.64 C ANISOU 991 CD2 HIS G 151 3171 2710 3099 -275 -294 300 C ATOM 992 CE1 HIS G 151 11.892 14.347 30.290 1.00 26.45 C ANISOU 992 CE1 HIS G 151 3603 3149 3298 -91 -452 300 C ATOM 993 NE2 HIS G 151 12.773 15.313 30.477 1.00 23.17 N ANISOU 993 NE2 HIS G 151 3232 2491 3079 -483 -453 391 N ATOM 994 N VAL G 152 14.563 11.155 30.225 1.00 16.91 N ANISOU 994 N VAL G 152 2150 2166 2107 -20 -9 22 N ATOM 995 CA VAL G 152 15.387 11.071 29.038 1.00 18.26 C ANISOU 995 CA VAL G 152 2342 2296 2298 10 16 20 C ATOM 996 C VAL G 152 14.805 11.905 27.899 1.00 19.08 C ANISOU 996 C VAL G 152 2440 2407 2400 21 40 58 C ATOM 997 O VAL G 152 13.594 12.132 27.802 1.00 19.45 O ANISOU 997 O VAL G 152 2553 2375 2462 62 75 159 O ATOM 998 CB VAL G 152 15.559 9.594 28.531 1.00 18.30 C ANISOU 998 CB VAL G 152 2322 2318 2311 -16 37 44 C ATOM 999 CG1 VAL G 152 16.348 8.790 29.509 1.00 18.58 C ANISOU 999 CG1 VAL G 152 2478 2233 2347 59 76 32 C ATOM 1000 CG2 VAL G 152 14.252 8.943 28.272 1.00 18.47 C ANISOU 1000 CG2 VAL G 152 2536 2316 2166 37 -25 -58 C ATOM 1001 N GLU G 153 15.691 12.326 27.016 1.00 20.13 N ANISOU 1001 N GLU G 153 2595 2535 2515 -4 54 34 N ATOM 1002 CA GLU G 153 15.310 13.071 25.826 1.00 20.98 C ANISOU 1002 CA GLU G 153 2670 2644 2655 12 43 23 C ATOM 1003 C GLU G 153 15.475 12.152 24.598 1.00 21.20 C ANISOU 1003 C GLU G 153 2697 2719 2636 3 36 69 C ATOM 1004 O GLU G 153 16.578 11.886 24.129 1.00 20.60 O ANISOU 1004 O GLU G 153 2550 2702 2576 4 183 3 O ATOM 1005 CB GLU G 153 16.163 14.330 25.749 1.00 21.68 C ANISOU 1005 CB GLU G 153 2752 2799 2687 10 48 72 C ATOM 1006 CG GLU G 153 16.210 15.054 27.084 1.00 24.07 C ANISOU 1006 CG GLU G 153 3009 3004 3130 10 52 73 C ATOM 1007 CD GLU G 153 16.005 16.532 26.956 1.00 28.80 C ANISOU 1007 CD GLU G 153 3475 3841 3624 382 190 173 C ATOM 1008 OE1 GLU G 153 16.482 17.102 25.943 1.00 32.23 O ANISOU 1008 OE1 GLU G 153 3767 4365 4112 632 405 274 O ATOM 1009 OE2 GLU G 153 15.382 17.117 27.875 1.00 31.07 O ANISOU 1009 OE2 GLU G 153 3694 4496 3613 376 135 56 O ATOM 1010 N THR G 154 14.347 11.639 24.127 1.00 21.19 N ANISOU 1010 N THR G 154 2698 2677 2676 -19 55 75 N ATOM 1011 CA THR G 154 14.311 10.709 23.014 1.00 21.96 C ANISOU 1011 CA THR G 154 2745 2751 2847 31 49 87 C ATOM 1012 C THR G 154 14.880 11.354 21.769 1.00 22.83 C ANISOU 1012 C THR G 154 2868 2868 2938 24 98 82 C ATOM 1013 O THR G 154 14.497 12.464 21.437 1.00 22.71 O ANISOU 1013 O THR G 154 2855 2732 3041 108 179 238 O ATOM 1014 CB THR G 154 12.864 10.334 22.749 1.00 21.80 C ANISOU 1014 CB THR G 154 2739 2718 2823 -17 69 76 C ATOM 1015 OG1 THR G 154 12.322 9.730 23.925 1.00 22.18 O ANISOU 1015 OG1 THR G 154 2658 2609 3158 -41 123 162 O ATOM 1016 CG2 THR G 154 12.738 9.289 21.642 1.00 21.74 C ANISOU 1016 CG2 THR G 154 2688 2670 2902 -23 67 53 C ATOM 1017 N GLN G 155 15.776 10.647 21.079 1.00 24.00 N ANISOU 1017 N GLN G 155 2967 3030 3120 14 14 44 N ATOM 1018 CA GLN G 155 16.233 11.060 19.755 1.00 24.74 C ANISOU 1018 CA GLN G 155 3093 3171 3135 0 48 27 C ATOM 1019 C GLN G 155 15.442 10.308 18.678 1.00 24.90 C ANISOU 1019 C GLN G 155 3106 3204 3149 0 50 12 C ATOM 1020 O GLN G 155 15.599 9.104 18.532 1.00 22.73 O ANISOU 1020 O GLN G 155 2908 2909 2820 54 12 78 O ATOM 1021 CB GLN G 155 17.729 10.750 19.561 1.00 25.77 C ANISOU 1021 CB GLN G 155 3200 3266 3324 -21 -27 36 C ATOM 1022 CG GLN G 155 18.642 11.170 20.684 1.00 28.84 C ANISOU 1022 CG GLN G 155 3588 3607 3761 -38 26 54 C ATOM 1023 CD GLN G 155 19.804 10.183 20.895 1.00 34.36 C ANISOU 1023 CD GLN G 155 4153 4060 4840 -202 113 223 C ATOM 1024 OE1 GLN G 155 19.604 9.054 21.389 1.00 38.45 O ANISOU 1024 OE1 GLN G 155 4622 4338 5649 -499 128 332 O ATOM 1025 NE2 GLN G 155 21.009 10.598 20.512 1.00 35.21 N ANISOU 1025 NE2 GLN G 155 3918 4072 5386 -604 120 321 N ATOM 1026 N GLU G 156 14.593 11.019 17.938 1.00 25.71 N ANISOU 1026 N GLU G 156 3289 3239 3241 41 22 3 N ATOM 1027 CA GLU G 156 13.927 10.456 16.768 1.00 27.52 C ANISOU 1027 CA GLU G 156 3482 3453 3521 28 -11 -25 C ATOM 1028 C GLU G 156 14.839 10.672 15.543 1.00 28.12 C ANISOU 1028 C GLU G 156 3656 3491 3536 28 -42 -25 C ATOM 1029 O GLU G 156 15.045 11.790 15.073 1.00 28.31 O ANISOU 1029 O GLU G 156 3799 3379 3577 26 -89 -43 O ATOM 1030 CB GLU G 156 12.515 11.051 16.581 1.00 28.59 C ANISOU 1030 CB GLU G 156 3678 3543 3639 41 -62 -37 C ATOM 1031 CG GLU G 156 11.650 10.299 15.564 1.00 30.99 C ANISOU 1031 CG GLU G 156 3793 3834 4146 29 -50 -120 C ATOM 1032 CD GLU G 156 10.136 10.356 15.810 1.00 35.99 C ANISOU 1032 CD GLU G 156 4450 4310 4911 23 -6 -239 C ATOM 1033 OE1 GLU G 156 9.645 11.288 16.507 1.00 37.88 O ANISOU 1033 OE1 GLU G 156 4600 4633 5159 188 198 -397 O ATOM 1034 OE2 GLU G 156 9.422 9.458 15.269 1.00 38.34 O ANISOU 1034 OE2 GLU G 156 4546 4381 5637 -95 -219 -230 O ATOM 1035 N LYS G 157 15.451 9.585 15.085 1.00 28.92 N ANISOU 1035 N LYS G 157 3736 3623 3627 -21 -24 -19 N ATOM 1036 CA LYS G 157 16.314 9.596 13.893 1.00 29.44 C ANISOU 1036 CA LYS G 157 3751 3717 3714 -3 -51 -31 C ATOM 1037 C LYS G 157 15.588 9.029 12.663 1.00 29.21 C ANISOU 1037 C LYS G 157 3740 3699 3659 11 -84 -25 C ATOM 1038 O LYS G 157 15.815 7.884 12.249 1.00 28.62 O ANISOU 1038 O LYS G 157 3729 3565 3578 -88 -175 -2 O ATOM 1039 CB LYS G 157 17.597 8.826 14.182 1.00 29.55 C ANISOU 1039 CB LYS G 157 3729 3714 3783 14 -94 -15 C ATOM 1040 CG LYS G 157 18.299 9.309 15.446 1.00 31.29 C ANISOU 1040 CG LYS G 157 4043 3907 3938 54 -38 -82 C ATOM 1041 CD LYS G 157 19.650 8.622 15.664 1.00 33.24 C ANISOU 1041 CD LYS G 157 4212 4194 4222 11 -121 -50 C ATOM 1042 CE LYS G 157 19.923 8.397 17.148 1.00 34.14 C ANISOU 1042 CE LYS G 157 4408 4310 4252 -5 -16 -52 C ATOM 1043 NZ LYS G 157 20.101 9.689 17.848 1.00 34.89 N ANISOU 1043 NZ LYS G 157 4426 4369 4461 -54 10 -16 N ATOM 1044 N ASN G 158 14.720 9.861 12.086 1.00 29.31 N ANISOU 1044 N ASN G 158 3706 3759 3669 -3 -80 -31 N ATOM 1045 CA ASN G 158 14.001 9.528 10.860 1.00 29.03 C ANISOU 1045 CA ASN G 158 3662 3712 3656 21 -49 -23 C ATOM 1046 C ASN G 158 13.904 10.785 9.956 1.00 28.78 C ANISOU 1046 C ASN G 158 3629 3706 3599 39 -40 -4 C ATOM 1047 O ASN G 158 12.863 11.447 9.891 1.00 29.37 O ANISOU 1047 O ASN G 158 3603 3920 3633 149 -67 27 O ATOM 1048 CB ASN G 158 12.622 8.924 11.214 1.00 28.79 C ANISOU 1048 CB ASN G 158 3590 3706 3640 28 -39 -111 C ATOM 1049 CG ASN G 158 11.946 8.239 10.016 1.00 29.48 C ANISOU 1049 CG ASN G 158 3561 3826 3813 7 -14 -201 C ATOM 1050 OD1 ASN G 158 12.593 7.923 9.004 1.00 26.95 O ANISOU 1050 OD1 ASN G 158 3076 3762 3398 171 148 -620 O ATOM 1051 ND2 ASN G 158 10.638 8.025 10.124 1.00 26.71 N ANISOU 1051 ND2 ASN G 158 2885 3643 3618 -309 240 -271 N ATOM 1052 N PRO G 159 15.005 11.123 9.281 1.00 27.50 N ANISOU 1052 N PRO G 159 3492 3540 3417 16 -10 -3 N ATOM 1053 CA PRO G 159 15.083 12.365 8.495 1.00 26.86 C ANISOU 1053 CA PRO G 159 3430 3427 3349 25 -31 -2 C ATOM 1054 C PRO G 159 14.270 12.293 7.210 1.00 25.92 C ANISOU 1054 C PRO G 159 3339 3331 3178 21 -38 6 C ATOM 1055 O PRO G 159 14.198 11.223 6.592 1.00 24.98 O ANISOU 1055 O PRO G 159 3400 3211 2880 121 -121 -3 O ATOM 1056 CB PRO G 159 16.571 12.468 8.148 1.00 27.13 C ANISOU 1056 CB PRO G 159 3472 3459 3376 65 -31 14 C ATOM 1057 CG PRO G 159 16.997 11.034 8.056 1.00 27.88 C ANISOU 1057 CG PRO G 159 3562 3552 3479 -10 -12 3 C ATOM 1058 CD PRO G 159 16.244 10.338 9.179 1.00 27.74 C ANISOU 1058 CD PRO G 159 3527 3552 3458 -7 -44 25 C ATOM 1059 N LEU G 160 13.672 13.421 6.839 1.00 24.77 N ANISOU 1059 N LEU G 160 3166 3177 3067 19 -24 13 N ATOM 1060 CA LEU G 160 12.917 13.551 5.599 1.00 24.86 C ANISOU 1060 CA LEU G 160 3120 3184 3140 -18 -36 -16 C ATOM 1061 C LEU G 160 13.878 13.782 4.454 1.00 24.29 C ANISOU 1061 C LEU G 160 3034 3158 3035 -46 -30 4 C ATOM 1062 O LEU G 160 14.900 14.429 4.648 1.00 24.62 O ANISOU 1062 O LEU G 160 3032 3348 2973 -123 -89 8 O ATOM 1063 CB LEU G 160 11.957 14.753 5.681 1.00 24.71 C ANISOU 1063 CB LEU G 160 3118 3117 3154 12 -35 24 C ATOM 1064 CG LEU G 160 10.959 14.783 6.841 1.00 25.44 C ANISOU 1064 CG LEU G 160 3194 3186 3282 21 -43 0 C ATOM 1065 CD1 LEU G 160 10.182 16.117 6.890 1.00 25.53 C ANISOU 1065 CD1 LEU G 160 3136 3163 3399 15 6 -13 C ATOM 1066 CD2 LEU G 160 10.001 13.598 6.738 1.00 25.22 C ANISOU 1066 CD2 LEU G 160 3056 3171 3355 23 -54 58 C ATOM 1067 N PRO G 161 13.551 13.313 3.253 1.00 23.99 N ANISOU 1067 N PRO G 161 2987 3056 3070 -47 -16 -31 N ATOM 1068 CA PRO G 161 14.443 13.481 2.102 1.00 23.76 C ANISOU 1068 CA PRO G 161 2982 3025 3020 -15 -9 -40 C ATOM 1069 C PRO G 161 14.580 14.923 1.590 1.00 23.77 C ANISOU 1069 C PRO G 161 2946 3028 3057 -43 -13 -71 C ATOM 1070 O PRO G 161 13.613 15.707 1.554 1.00 24.04 O ANISOU 1070 O PRO G 161 2900 3042 3189 -59 -22 -147 O ATOM 1071 CB PRO G 161 13.782 12.621 1.031 1.00 23.91 C ANISOU 1071 CB PRO G 161 2974 3024 3087 -17 -5 -22 C ATOM 1072 CG PRO G 161 12.356 12.628 1.388 1.00 24.10 C ANISOU 1072 CG PRO G 161 3019 3080 3055 8 25 -61 C ATOM 1073 CD PRO G 161 12.316 12.607 2.878 1.00 24.09 C ANISOU 1073 CD PRO G 161 3017 3100 3034 -16 -4 -13 C ATOM 1074 N SER G 162 15.796 15.247 1.162 1.00 23.32 N ANISOU 1074 N SER G 162 2859 3035 2965 -6 5 -69 N ATOM 1075 CA SER G 162 16.124 16.541 0.569 1.00 22.78 C ANISOU 1075 CA SER G 162 2802 2904 2947 -25 15 5 C ATOM 1076 C SER G 162 15.720 16.562 -0.902 1.00 23.36 C ANISOU 1076 C SER G 162 2842 3012 3020 -13 51 31 C ATOM 1077 O SER G 162 15.462 15.507 -1.488 1.00 22.71 O ANISOU 1077 O SER G 162 2757 2955 2915 -52 123 153 O ATOM 1078 CB SER G 162 17.635 16.772 0.669 1.00 22.69 C ANISOU 1078 CB SER G 162 2773 2923 2925 4 7 -15 C ATOM 1079 OG SER G 162 18.344 15.840 -0.152 1.00 21.10 O ANISOU 1079 OG SER G 162 2297 2772 2949 -184 -150 50 O ATOM 1080 N LYS G 163 15.699 17.760 -1.498 1.00 24.39 N ANISOU 1080 N LYS G 163 2986 3111 3170 14 30 36 N ATOM 1081 CA LYS G 163 15.549 17.931 -2.951 1.00 25.53 C ANISOU 1081 CA LYS G 163 3180 3249 3272 19 10 12 C ATOM 1082 C LYS G 163 16.427 16.943 -3.688 1.00 25.55 C ANISOU 1082 C LYS G 163 3214 3176 3317 67 -24 19 C ATOM 1083 O LYS G 163 16.002 16.278 -4.628 1.00 25.59 O ANISOU 1083 O LYS G 163 3187 3163 3372 206 -75 7 O ATOM 1084 CB LYS G 163 16.052 19.315 -3.416 1.00 25.91 C ANISOU 1084 CB LYS G 163 3259 3213 3372 69 -6 5 C ATOM 1085 CG LYS G 163 15.390 20.507 -2.835 1.00 29.01 C ANISOU 1085 CG LYS G 163 3591 3691 3738 -6 -27 -14 C ATOM 1086 CD LYS G 163 16.226 21.810 -3.033 1.00 31.65 C ANISOU 1086 CD LYS G 163 3982 3948 4093 8 -69 -75 C ATOM 1087 CE LYS G 163 16.461 22.548 -1.688 1.00 33.53 C ANISOU 1087 CE LYS G 163 4155 4195 4387 -13 -95 -83 C ATOM 1088 NZ LYS G 163 16.415 24.043 -1.808 1.00 33.37 N ANISOU 1088 NZ LYS G 163 4204 3906 4570 21 -172 -193 N ATOM 1089 N GLU G 164 17.677 16.894 -3.243 1.00 26.05 N ANISOU 1089 N GLU G 164 3287 3263 3344 29 2 17 N ATOM 1090 CA GLU G 164 18.760 16.190 -3.927 1.00 26.43 C ANISOU 1090 CA GLU G 164 3363 3325 3352 0 24 0 C ATOM 1091 C GLU G 164 18.572 14.680 -3.859 1.00 26.76 C ANISOU 1091 C GLU G 164 3425 3355 3386 7 8 6 C ATOM 1092 O GLU G 164 18.864 13.960 -4.816 1.00 26.67 O ANISOU 1092 O GLU G 164 3542 3286 3302 -38 72 2 O ATOM 1093 CB GLU G 164 20.109 16.591 -3.304 1.00 26.44 C ANISOU 1093 CB GLU G 164 3338 3336 3371 -5 28 -5 C ATOM 1094 CG GLU G 164 20.511 18.044 -3.591 1.00 26.97 C ANISOU 1094 CG GLU G 164 3324 3447 3476 -43 80 -23 C ATOM 1095 CD GLU G 164 19.930 19.090 -2.630 1.00 26.87 C ANISOU 1095 CD GLU G 164 3200 3437 3570 47 164 -79 C ATOM 1096 OE1 GLU G 164 19.514 18.747 -1.492 1.00 27.78 O ANISOU 1096 OE1 GLU G 164 3262 3606 3687 63 213 -211 O ATOM 1097 OE2 GLU G 164 19.901 20.280 -3.020 1.00 27.14 O ANISOU 1097 OE2 GLU G 164 3027 3590 3694 32 307 -110 O ATOM 1098 N THR G 165 18.082 14.212 -2.718 1.00 26.64 N ANISOU 1098 N THR G 165 3404 3369 3347 -11 32 35 N ATOM 1099 CA THR G 165 17.815 12.806 -2.530 1.00 27.39 C ANISOU 1099 CA THR G 165 3516 3440 3448 13 -36 12 C ATOM 1100 C THR G 165 16.664 12.356 -3.434 1.00 28.19 C ANISOU 1100 C THR G 165 3658 3542 3509 42 -47 -5 C ATOM 1101 O THR G 165 16.709 11.265 -4.009 1.00 28.96 O ANISOU 1101 O THR G 165 3814 3591 3598 70 -131 -15 O ATOM 1102 CB THR G 165 17.490 12.529 -1.031 1.00 27.50 C ANISOU 1102 CB THR G 165 3582 3408 3458 0 -25 5 C ATOM 1103 OG1 THR G 165 18.704 12.568 -0.265 1.00 25.14 O ANISOU 1103 OG1 THR G 165 3101 3120 3329 213 -194 132 O ATOM 1104 CG2 THR G 165 16.958 11.122 -0.817 1.00 27.76 C ANISOU 1104 CG2 THR G 165 3566 3490 3492 -47 -45 42 C ATOM 1105 N ILE G 166 15.651 13.206 -3.567 1.00 28.49 N ANISOU 1105 N ILE G 166 3644 3637 3542 47 10 -28 N ATOM 1106 CA ILE G 166 14.485 12.920 -4.385 1.00 28.79 C ANISOU 1106 CA ILE G 166 3663 3678 3596 1 30 -20 C ATOM 1107 C ILE G 166 14.910 12.861 -5.860 1.00 29.95 C ANISOU 1107 C ILE G 166 3790 3849 3740 -11 57 -7 C ATOM 1108 O ILE G 166 14.507 11.948 -6.575 1.00 28.74 O ANISOU 1108 O ILE G 166 3643 3791 3485 -47 155 -17 O ATOM 1109 CB ILE G 166 13.377 14.001 -4.122 1.00 28.57 C ANISOU 1109 CB ILE G 166 3619 3660 3576 -35 39 -20 C ATOM 1110 CG1 ILE G 166 12.734 13.769 -2.749 1.00 28.33 C ANISOU 1110 CG1 ILE G 166 3564 3640 3557 -54 -14 -80 C ATOM 1111 CG2 ILE G 166 12.320 14.005 -5.217 1.00 28.46 C ANISOU 1111 CG2 ILE G 166 3609 3605 3598 -12 50 24 C ATOM 1112 CD1 ILE G 166 11.927 14.982 -2.216 1.00 27.05 C ANISOU 1112 CD1 ILE G 166 3388 3473 3416 19 31 -36 C ATOM 1113 N GLU G 167 15.752 13.808 -6.284 1.00 31.69 N ANISOU 1113 N GLU G 167 4036 4027 3977 -25 25 -22 N ATOM 1114 CA GLU G 167 16.325 13.831 -7.646 1.00 33.03 C ANISOU 1114 CA GLU G 167 4190 4175 4184 -20 41 -8 C ATOM 1115 C GLU G 167 17.160 12.567 -7.941 1.00 33.18 C ANISOU 1115 C GLU G 167 4202 4206 4199 -20 32 14 C ATOM 1116 O GLU G 167 17.148 12.048 -9.063 1.00 32.94 O ANISOU 1116 O GLU G 167 4195 4161 4156 -27 -10 8 O ATOM 1117 CB GLU G 167 17.225 15.053 -7.835 1.00 33.83 C ANISOU 1117 CB GLU G 167 4331 4206 4314 5 0 -14 C ATOM 1118 CG GLU G 167 16.528 16.413 -7.823 1.00 37.51 C ANISOU 1118 CG GLU G 167 4750 4679 4819 -43 99 -106 C ATOM 1119 CD GLU G 167 17.511 17.585 -7.631 1.00 41.19 C ANISOU 1119 CD GLU G 167 5296 5042 5310 -37 213 -242 C ATOM 1120 OE1 GLU G 167 18.643 17.541 -8.205 1.00 43.03 O ANISOU 1120 OE1 GLU G 167 5485 5366 5495 -77 544 -299 O ATOM 1121 OE2 GLU G 167 17.156 18.554 -6.905 1.00 42.85 O ANISOU 1121 OE2 GLU G 167 5739 5060 5479 42 308 -441 O ATOM 1122 N GLN G 168 17.887 12.082 -6.936 1.00 33.47 N ANISOU 1122 N GLN G 168 4233 4271 4212 -12 17 17 N ATOM 1123 CA GLN G 168 18.694 10.866 -7.079 1.00 33.83 C ANISOU 1123 CA GLN G 168 4283 4311 4259 -9 11 12 C ATOM 1124 C GLN G 168 17.811 9.654 -7.387 1.00 34.60 C ANISOU 1124 C GLN G 168 4387 4411 4347 -9 18 12 C ATOM 1125 O GLN G 168 18.149 8.852 -8.265 1.00 34.26 O ANISOU 1125 O GLN G 168 4348 4446 4222 -9 115 8 O ATOM 1126 CB GLN G 168 19.521 10.586 -5.812 1.00 33.78 C ANISOU 1126 CB GLN G 168 4257 4309 4268 -5 15 0 C ATOM 1127 CG GLN G 168 20.923 11.207 -5.795 1.00 33.20 C ANISOU 1127 CG GLN G 168 4187 4252 4175 -75 -35 29 C ATOM 1128 CD GLN G 168 21.674 10.918 -4.498 1.00 32.31 C ANISOU 1128 CD GLN G 168 4063 4095 4115 -155 -55 35 C ATOM 1129 OE1 GLN G 168 21.068 10.839 -3.429 1.00 30.10 O ANISOU 1129 OE1 GLN G 168 3710 4081 3643 -275 -17 103 O ATOM 1130 NE2 GLN G 168 22.987 10.765 -4.591 1.00 29.87 N ANISOU 1130 NE2 GLN G 168 3406 3942 4000 -205 -78 124 N ATOM 1131 N GLU G 169 16.689 9.514 -6.671 1.00 35.32 N ANISOU 1131 N GLU G 169 4478 4504 4436 20 8 -6 N ATOM 1132 CA GLU G 169 15.806 8.360 -6.876 1.00 36.36 C ANISOU 1132 CA GLU G 169 4603 4637 4574 4 13 14 C ATOM 1133 C GLU G 169 15.105 8.414 -8.244 1.00 36.67 C ANISOU 1133 C GLU G 169 4651 4679 4600 6 1 19 C ATOM 1134 O GLU G 169 14.872 7.375 -8.853 1.00 36.14 O ANISOU 1134 O GLU G 169 4641 4598 4491 33 8 37 O ATOM 1135 CB GLU G 169 14.785 8.202 -5.737 1.00 36.88 C ANISOU 1135 CB GLU G 169 4664 4695 4652 18 -5 -9 C ATOM 1136 CG GLU G 169 15.219 7.199 -4.655 1.00 38.79 C ANISOU 1136 CG GLU G 169 4883 4944 4911 -16 77 3 C ATOM 1137 CD GLU G 169 14.792 7.600 -3.237 1.00 42.93 C ANISOU 1137 CD GLU G 169 5263 5231 5818 -9 90 -137 C ATOM 1138 OE1 GLU G 169 14.784 8.830 -2.976 1.00 45.76 O ANISOU 1138 OE1 GLU G 169 5494 5405 6485 57 4 -69 O ATOM 1139 OE2 GLU G 169 14.491 6.701 -2.377 1.00 41.50 O ANISOU 1139 OE2 GLU G 169 5020 5058 5689 -274 474 -119 O ATOM 1140 N LYS G 170 14.791 9.618 -8.727 1.00 37.32 N ANISOU 1140 N LYS G 170 4750 4750 4678 18 8 9 N ATOM 1141 CA LYS G 170 14.165 9.788 -10.053 1.00 38.17 C ANISOU 1141 CA LYS G 170 4831 4846 4823 12 -2 -2 C ATOM 1142 C LYS G 170 15.010 9.162 -11.180 1.00 38.92 C ANISOU 1142 C LYS G 170 4922 4954 4908 17 -4 -6 C ATOM 1143 O LYS G 170 14.481 8.477 -12.062 1.00 39.09 O ANISOU 1143 O LYS G 170 4940 4962 4947 42 -28 -40 O ATOM 1144 CB LYS G 170 13.920 11.277 -10.361 1.00 38.03 C ANISOU 1144 CB LYS G 170 4813 4828 4805 17 0 14 C ATOM 1145 CG LYS G 170 12.844 11.911 -9.512 1.00 37.94 C ANISOU 1145 CG LYS G 170 4819 4793 4801 20 0 11 C ATOM 1146 CD LYS G 170 12.380 13.266 -10.043 1.00 38.42 C ANISOU 1146 CD LYS G 170 4882 4846 4868 -3 8 12 C ATOM 1147 CE LYS G 170 11.174 13.772 -9.231 1.00 38.69 C ANISOU 1147 CE LYS G 170 4958 4826 4916 4 7 24 C ATOM 1148 NZ LYS G 170 10.970 15.249 -9.292 1.00 39.11 N ANISOU 1148 NZ LYS G 170 5112 4837 4910 0 -2 -52 N ATOM 1149 N GLN G 171 16.321 9.376 -11.118 1.00 39.71 N ANISOU 1149 N GLN G 171 5012 5046 5026 1 12 2 N ATOM 1150 CA GLN G 171 17.240 8.954 -12.178 1.00 40.34 C ANISOU 1150 CA GLN G 171 5090 5116 5121 -6 20 16 C ATOM 1151 C GLN G 171 17.583 7.470 -12.116 1.00 40.28 C ANISOU 1151 C GLN G 171 5071 5085 5145 19 10 39 C ATOM 1152 O GLN G 171 17.057 6.742 -11.273 1.00 40.20 O ANISOU 1152 O GLN G 171 5067 5084 5121 46 11 57 O ATOM 1153 CB GLN G 171 18.513 9.783 -12.090 1.00 40.72 C ANISOU 1153 CB GLN G 171 5128 5173 5171 -13 20 9 C ATOM 1154 CG GLN G 171 18.265 11.270 -12.292 1.00 42.26 C ANISOU 1154 CG GLN G 171 5328 5359 5369 -74 22 38 C ATOM 1155 CD GLN G 171 19.409 12.124 -11.782 1.00 44.74 C ANISOU 1155 CD GLN G 171 5713 5708 5579 -122 3 133 C ATOM 1156 OE1 GLN G 171 19.706 12.117 -10.580 1.00 45.47 O ANISOU 1156 OE1 GLN G 171 5870 5858 5547 -149 -35 399 O ATOM 1157 NE2 GLN G 171 20.055 12.865 -12.691 1.00 45.78 N ANISOU 1157 NE2 GLN G 171 5822 5922 5648 -230 174 276 N TER 1158 GLN G 171 ATOM 1159 N THR A 6 21.740 -3.185 33.568 1.00 18.95 N ANISOU 1159 N THR A 6 2023 2718 2459 -87 -331 -117 N ATOM 1160 CA THR A 6 20.328 -2.704 33.527 1.00 19.22 C ANISOU 1160 CA THR A 6 2390 2504 2406 -17 -127 -50 C ATOM 1161 C THR A 6 19.648 -3.252 32.276 1.00 17.32 C ANISOU 1161 C THR A 6 2023 2319 2237 -54 -122 -42 C ATOM 1162 O THR A 6 20.274 -3.423 31.213 1.00 16.76 O ANISOU 1162 O THR A 6 1774 2280 2314 -141 -121 -202 O ATOM 1163 CB THR A 6 20.187 -1.125 33.668 1.00 20.44 C ANISOU 1163 CB THR A 6 2508 2707 2548 -22 -187 23 C ATOM 1164 OG1 THR A 6 19.422 -0.547 32.584 1.00 24.35 O ANISOU 1164 OG1 THR A 6 3616 3082 2554 -85 -408 88 O ATOM 1165 CG2 THR A 6 21.520 -0.371 33.647 1.00 20.53 C ANISOU 1165 CG2 THR A 6 2443 2711 2644 36 -49 119 C ATOM 1166 N ALA A 7 18.357 -3.521 32.399 1.00 15.62 N ANISOU 1166 N ALA A 7 1964 1972 1998 -39 35 25 N ATOM 1167 CA ALA A 7 17.631 -4.196 31.351 1.00 13.81 C ANISOU 1167 CA ALA A 7 1652 1797 1796 -15 -7 45 C ATOM 1168 C ALA A 7 17.375 -3.251 30.190 1.00 13.27 C ANISOU 1168 C ALA A 7 1593 1703 1744 -44 56 32 C ATOM 1169 O ALA A 7 17.304 -2.030 30.374 1.00 12.71 O ANISOU 1169 O ALA A 7 1490 1670 1669 -99 92 47 O ATOM 1170 CB ALA A 7 16.336 -4.748 31.894 1.00 14.47 C ANISOU 1170 CB ALA A 7 1842 1827 1828 -1 22 101 C ATOM 1171 N LEU A 8 17.269 -3.836 28.995 1.00 12.73 N ANISOU 1171 N LEU A 8 1561 1601 1674 -39 -31 57 N ATOM 1172 CA LEU A 8 16.904 -3.135 27.775 1.00 12.57 C ANISOU 1172 CA LEU A 8 1590 1549 1637 -20 -37 72 C ATOM 1173 C LEU A 8 15.450 -3.425 27.410 1.00 11.87 C ANISOU 1173 C LEU A 8 1464 1479 1565 -28 -52 63 C ATOM 1174 O LEU A 8 14.929 -4.505 27.703 1.00 11.94 O ANISOU 1174 O LEU A 8 1280 1633 1624 -92 -122 162 O ATOM 1175 CB LEU A 8 17.785 -3.571 26.604 1.00 11.99 C ANISOU 1175 CB LEU A 8 1522 1458 1574 18 -1 17 C ATOM 1176 CG LEU A 8 19.288 -3.619 26.853 1.00 14.46 C ANISOU 1176 CG LEU A 8 2009 1712 1773 10 -31 57 C ATOM 1177 CD1 LEU A 8 20.012 -4.096 25.608 1.00 16.03 C ANISOU 1177 CD1 LEU A 8 2203 2016 1870 89 35 89 C ATOM 1178 CD2 LEU A 8 19.849 -2.265 27.335 1.00 15.35 C ANISOU 1178 CD2 LEU A 8 2062 1942 1825 -47 -132 141 C ATOM 1179 N VAL A 9 14.827 -2.455 26.741 1.00 11.22 N ANISOU 1179 N VAL A 9 1414 1385 1464 14 -28 25 N ATOM 1180 CA VAL A 9 13.491 -2.590 26.204 1.00 10.63 C ANISOU 1180 CA VAL A 9 1355 1306 1377 21 4 2 C ATOM 1181 C VAL A 9 13.513 -2.208 24.740 1.00 11.00 C ANISOU 1181 C VAL A 9 1443 1369 1367 50 6 -18 C ATOM 1182 O VAL A 9 13.893 -1.092 24.404 1.00 9.87 O ANISOU 1182 O VAL A 9 1531 1190 1028 210 -37 -98 O ATOM 1183 CB VAL A 9 12.494 -1.694 26.960 1.00 10.52 C ANISOU 1183 CB VAL A 9 1391 1217 1387 23 -5 -37 C ATOM 1184 CG1 VAL A 9 11.084 -1.821 26.382 1.00 10.36 C ANISOU 1184 CG1 VAL A 9 1212 1234 1491 37 28 36 C ATOM 1185 CG2 VAL A 9 12.469 -2.068 28.413 1.00 10.18 C ANISOU 1185 CG2 VAL A 9 1352 1236 1280 148 -3 3 C ATOM 1186 N CYS A 10 13.127 -3.153 23.879 1.00 11.98 N ANISOU 1186 N CYS A 10 1551 1456 1542 66 23 10 N ATOM 1187 CA CYS A 10 13.063 -2.952 22.445 1.00 13.55 C ANISOU 1187 CA CYS A 10 1779 1692 1676 113 8 -8 C ATOM 1188 C CYS A 10 11.668 -3.298 21.934 1.00 13.26 C ANISOU 1188 C CYS A 10 1851 1549 1638 42 -61 9 C ATOM 1189 O CYS A 10 11.230 -4.446 22.008 1.00 13.81 O ANISOU 1189 O CYS A 10 2087 1548 1610 263 -165 103 O ATOM 1190 CB CYS A 10 14.124 -3.800 21.746 1.00 15.25 C ANISOU 1190 CB CYS A 10 2153 1911 1729 65 0 32 C ATOM 1191 SG CYS A 10 14.220 -3.476 19.983 1.00 23.21 S ANISOU 1191 SG CYS A 10 3133 3138 2546 271 212 -230 S ATOM 1192 N ASP A 11 10.952 -2.275 21.459 1.00 12.86 N ANISOU 1192 N ASP A 11 1738 1528 1619 11 -58 17 N ATOM 1193 CA ASP A 11 9.617 -2.419 20.889 1.00 12.59 C ANISOU 1193 CA ASP A 11 1653 1514 1615 -1 52 6 C ATOM 1194 C ASP A 11 9.710 -2.320 19.364 1.00 12.69 C ANISOU 1194 C ASP A 11 1705 1509 1606 -26 47 9 C ATOM 1195 O ASP A 11 9.818 -1.238 18.804 1.00 12.77 O ANISOU 1195 O ASP A 11 1752 1506 1591 -31 188 -29 O ATOM 1196 CB ASP A 11 8.696 -1.332 21.464 1.00 12.42 C ANISOU 1196 CB ASP A 11 1682 1360 1678 -31 59 58 C ATOM 1197 CG ASP A 11 7.315 -1.353 20.848 1.00 12.95 C ANISOU 1197 CG ASP A 11 1695 1550 1675 61 140 -72 C ATOM 1198 OD1 ASP A 11 6.657 -0.282 20.793 1.00 13.37 O ANISOU 1198 OD1 ASP A 11 1848 1932 1301 403 249 -344 O ATOM 1199 OD2 ASP A 11 6.815 -2.402 20.367 1.00 14.17 O ANISOU 1199 OD2 ASP A 11 1515 1953 1913 55 369 -425 O ATOM 1200 N ASN A 12 9.657 -3.458 18.687 1.00 13.45 N ANISOU 1200 N ASN A 12 1773 1680 1656 -37 83 45 N ATOM 1201 CA ASN A 12 9.865 -3.505 17.247 1.00 14.17 C ANISOU 1201 CA ASN A 12 1834 1792 1758 -16 8 -5 C ATOM 1202 C ASN A 12 8.554 -3.424 16.492 1.00 13.64 C ANISOU 1202 C ASN A 12 1727 1738 1716 -15 33 22 C ATOM 1203 O ASN A 12 7.719 -4.304 16.633 1.00 15.41 O ANISOU 1203 O ASN A 12 1916 2030 1910 -10 73 98 O ATOM 1204 CB ASN A 12 10.529 -4.824 16.883 1.00 15.18 C ANISOU 1204 CB ASN A 12 1928 1958 1882 37 -12 -3 C ATOM 1205 CG ASN A 12 11.962 -4.908 17.355 1.00 17.01 C ANISOU 1205 CG ASN A 12 2210 2233 2020 -125 -42 62 C ATOM 1206 OD1 ASN A 12 12.286 -5.672 18.266 1.00 17.93 O ANISOU 1206 OD1 ASN A 12 2766 2179 1867 105 54 424 O ATOM 1207 ND2 ASN A 12 12.837 -4.123 16.725 1.00 22.06 N ANISOU 1207 ND2 ASN A 12 2746 2913 2723 -146 -236 187 N ATOM 1208 N GLY A 13 8.393 -2.408 15.653 1.00 12.63 N ANISOU 1208 N GLY A 13 1612 1604 1582 -21 39 -1 N ATOM 1209 CA GLY A 13 7.200 -2.278 14.833 1.00 12.01 C ANISOU 1209 CA GLY A 13 1487 1547 1527 30 82 69 C ATOM 1210 C GLY A 13 7.431 -2.340 13.335 1.00 11.75 C ANISOU 1210 C GLY A 13 1442 1503 1517 43 44 -4 C ATOM 1211 O GLY A 13 8.578 -2.385 12.878 1.00 11.54 O ANISOU 1211 O GLY A 13 1369 1589 1423 66 233 78 O ATOM 1212 N SER A 14 6.326 -2.295 12.583 1.00 11.33 N ANISOU 1212 N SER A 14 1420 1426 1457 -1 27 -21 N ATOM 1213 CA SER A 14 6.329 -2.378 11.128 1.00 10.81 C ANISOU 1213 CA SER A 14 1291 1398 1418 -32 33 56 C ATOM 1214 C SER A 14 7.122 -1.232 10.511 1.00 10.61 C ANISOU 1214 C SER A 14 1291 1321 1417 -53 23 38 C ATOM 1215 O SER A 14 7.833 -1.425 9.519 1.00 9.69 O ANISOU 1215 O SER A 14 1207 1161 1312 -127 88 136 O ATOM 1216 CB SER A 14 4.891 -2.344 10.559 1.00 11.24 C ANISOU 1216 CB SER A 14 1380 1454 1435 -73 2 0 C ATOM 1217 OG SER A 14 4.102 -3.415 11.066 1.00 9.05 O ANISOU 1217 OG SER A 14 964 1103 1369 -300 -56 283 O ATOM 1218 N GLY A 15 6.987 -0.065 11.125 1.00 10.35 N ANISOU 1218 N GLY A 15 1211 1376 1345 2 20 11 N ATOM 1219 CA GLY A 15 7.539 1.177 10.641 1.00 10.50 C ANISOU 1219 CA GLY A 15 1271 1376 1341 -39 36 -11 C ATOM 1220 C GLY A 15 8.752 1.677 11.412 1.00 11.19 C ANISOU 1220 C GLY A 15 1333 1503 1414 -64 -4 17 C ATOM 1221 O GLY A 15 9.715 2.135 10.790 1.00 10.71 O ANISOU 1221 O GLY A 15 1087 1449 1534 -194 37 -7 O ATOM 1222 N LEU A 16 8.683 1.579 12.746 1.00 11.21 N ANISOU 1222 N LEU A 16 1375 1473 1408 -61 -25 -5 N ATOM 1223 CA LEU A 16 9.650 2.163 13.663 1.00 11.51 C ANISOU 1223 CA LEU A 16 1445 1470 1458 -3 -42 18 C ATOM 1224 C LEU A 16 10.040 1.199 14.790 1.00 11.17 C ANISOU 1224 C LEU A 16 1391 1436 1414 6 -58 75 C ATOM 1225 O LEU A 16 9.184 0.502 15.370 1.00 11.09 O ANISOU 1225 O LEU A 16 1410 1308 1493 6 -207 102 O ATOM 1226 CB LEU A 16 9.061 3.419 14.311 1.00 11.31 C ANISOU 1226 CB LEU A 16 1500 1471 1324 -21 -47 13 C ATOM 1227 CG LEU A 16 8.740 4.640 13.443 1.00 12.63 C ANISOU 1227 CG LEU A 16 1650 1516 1631 -1 -54 -88 C ATOM 1228 CD1 LEU A 16 8.008 5.676 14.259 1.00 13.38 C ANISOU 1228 CD1 LEU A 16 1673 1838 1572 56 130 63 C ATOM 1229 CD2 LEU A 16 9.982 5.230 12.815 1.00 12.21 C ANISOU 1229 CD2 LEU A 16 1631 1341 1665 74 68 -11 C ATOM 1230 N VAL A 17 11.336 1.216 15.110 1.00 10.70 N ANISOU 1230 N VAL A 17 1328 1367 1369 38 -2 40 N ATOM 1231 CA VAL A 17 11.899 0.606 16.315 1.00 10.50 C ANISOU 1231 CA VAL A 17 1328 1279 1381 31 -27 3 C ATOM 1232 C VAL A 17 11.958 1.660 17.398 1.00 10.25 C ANISOU 1232 C VAL A 17 1288 1279 1326 40 -14 13 C ATOM 1233 O VAL A 17 12.448 2.774 17.153 1.00 11.27 O ANISOU 1233 O VAL A 17 1445 1347 1488 102 -19 -36 O ATOM 1234 CB VAL A 17 13.342 0.123 16.044 1.00 10.18 C ANISOU 1234 CB VAL A 17 1267 1279 1321 21 -32 -15 C ATOM 1235 CG1 VAL A 17 13.940 -0.540 17.249 1.00 10.75 C ANISOU 1235 CG1 VAL A 17 1417 1339 1326 -64 -21 -93 C ATOM 1236 CG2 VAL A 17 13.367 -0.856 14.875 1.00 11.26 C ANISOU 1236 CG2 VAL A 17 1419 1336 1523 151 -187 -41 C ATOM 1237 N LYS A 18 11.459 1.328 18.582 1.00 10.04 N ANISOU 1237 N LYS A 18 1293 1198 1324 32 3 9 N ATOM 1238 CA LYS A 18 11.567 2.180 19.779 1.00 10.06 C ANISOU 1238 CA LYS A 18 1288 1253 1279 -7 -15 13 C ATOM 1239 C LYS A 18 12.448 1.395 20.759 1.00 10.25 C ANISOU 1239 C LYS A 18 1301 1308 1284 2 -2 21 C ATOM 1240 O LYS A 18 12.093 0.299 21.168 1.00 10.04 O ANISOU 1240 O LYS A 18 1345 1282 1186 34 85 8 O ATOM 1241 CB LYS A 18 10.173 2.431 20.398 1.00 9.78 C ANISOU 1241 CB LYS A 18 1334 1200 1180 48 -50 -55 C ATOM 1242 CG LYS A 18 9.262 3.444 19.656 1.00 10.94 C ANISOU 1242 CG LYS A 18 1468 1297 1390 -5 -41 -148 C ATOM 1243 CD LYS A 18 8.726 2.966 18.274 1.00 11.03 C ANISOU 1243 CD LYS A 18 1339 1475 1375 -75 4 -39 C ATOM 1244 CE LYS A 18 7.655 1.902 18.399 1.00 11.11 C ANISOU 1244 CE LYS A 18 1346 1577 1295 -124 11 -161 C ATOM 1245 NZ LYS A 18 7.024 1.555 17.081 1.00 9.54 N ANISOU 1245 NZ LYS A 18 1181 1702 742 -109 -60 -273 N ATOM 1246 N ALA A 19 13.617 1.923 21.095 1.00 10.16 N ANISOU 1246 N ALA A 19 1324 1327 1207 26 -25 4 N ATOM 1247 CA ALA A 19 14.560 1.179 21.928 1.00 10.67 C ANISOU 1247 CA ALA A 19 1346 1398 1310 41 50 -36 C ATOM 1248 C ALA A 19 15.111 2.051 23.069 1.00 10.16 C ANISOU 1248 C ALA A 19 1352 1314 1192 47 32 -55 C ATOM 1249 O ALA A 19 15.261 3.251 22.937 1.00 9.27 O ANISOU 1249 O ALA A 19 1333 1215 974 154 148 -91 O ATOM 1250 CB ALA A 19 15.701 0.631 21.065 1.00 11.38 C ANISOU 1250 CB ALA A 19 1504 1470 1348 68 25 -91 C ATOM 1251 N GLY A 20 15.421 1.414 24.185 1.00 10.86 N ANISOU 1251 N GLY A 20 1435 1348 1342 32 25 -44 N ATOM 1252 CA GLY A 20 15.869 2.107 25.367 1.00 10.41 C ANISOU 1252 CA GLY A 20 1347 1321 1285 -30 6 -55 C ATOM 1253 C GLY A 20 16.216 1.195 26.522 1.00 10.63 C ANISOU 1253 C GLY A 20 1349 1352 1338 0 23 -39 C ATOM 1254 O GLY A 20 16.339 -0.024 26.357 1.00 10.61 O ANISOU 1254 O GLY A 20 1304 1475 1251 20 -34 -171 O ATOM 1255 N PHE A 21 16.330 1.810 27.702 1.00 10.83 N ANISOU 1255 N PHE A 21 1333 1421 1360 -38 23 -24 N ATOM 1256 CA PHE A 21 16.668 1.148 28.965 1.00 10.31 C ANISOU 1256 CA PHE A 21 1220 1364 1334 -4 44 36 C ATOM 1257 C PHE A 21 15.486 1.139 29.934 1.00 10.61 C ANISOU 1257 C PHE A 21 1329 1371 1330 14 36 -15 C ATOM 1258 O PHE A 21 14.785 2.165 30.106 1.00 10.20 O ANISOU 1258 O PHE A 21 1176 1419 1277 -5 150 45 O ATOM 1259 CB PHE A 21 17.812 1.902 29.607 1.00 11.01 C ANISOU 1259 CB PHE A 21 1386 1419 1376 97 66 18 C ATOM 1260 CG PHE A 21 19.078 1.836 28.807 1.00 12.43 C ANISOU 1260 CG PHE A 21 1426 1660 1633 -13 197 198 C ATOM 1261 CD1 PHE A 21 19.963 0.787 28.985 1.00 14.20 C ANISOU 1261 CD1 PHE A 21 1692 1754 1947 90 255 129 C ATOM 1262 CD2 PHE A 21 19.357 2.784 27.833 1.00 14.70 C ANISOU 1262 CD2 PHE A 21 1932 1882 1771 0 189 75 C ATOM 1263 CE1 PHE A 21 21.153 0.710 28.238 1.00 14.80 C ANISOU 1263 CE1 PHE A 21 1886 1823 1913 228 371 10 C ATOM 1264 CE2 PHE A 21 20.546 2.703 27.076 1.00 14.79 C ANISOU 1264 CE2 PHE A 21 1704 2073 1842 200 150 91 C ATOM 1265 CZ PHE A 21 21.429 1.662 27.282 1.00 14.56 C ANISOU 1265 CZ PHE A 21 1938 1736 1856 129 285 0 C ATOM 1266 N ALA A 22 15.264 -0.012 30.558 1.00 9.81 N ANISOU 1266 N ALA A 22 1184 1249 1294 -14 71 10 N ATOM 1267 CA ALA A 22 14.221 -0.178 31.547 1.00 10.84 C ANISOU 1267 CA ALA A 22 1408 1343 1368 3 37 -5 C ATOM 1268 C ALA A 22 14.466 0.847 32.648 1.00 10.67 C ANISOU 1268 C ALA A 22 1335 1316 1401 -37 -6 -39 C ATOM 1269 O ALA A 22 15.601 1.028 33.074 1.00 11.57 O ANISOU 1269 O ALA A 22 1252 1567 1576 -37 5 30 O ATOM 1270 CB ALA A 22 14.268 -1.612 32.139 1.00 10.92 C ANISOU 1270 CB ALA A 22 1416 1311 1420 -48 114 -32 C ATOM 1271 N GLY A 23 13.408 1.495 33.109 1.00 9.50 N ANISOU 1271 N GLY A 23 1155 1195 1260 -11 27 -2 N ATOM 1272 CA GLY A 23 13.511 2.541 34.116 1.00 9.20 C ANISOU 1272 CA GLY A 23 1238 1127 1127 -9 33 -27 C ATOM 1273 C GLY A 23 13.480 3.981 33.609 1.00 9.17 C ANISOU 1273 C GLY A 23 1246 1091 1145 13 53 -42 C ATOM 1274 O GLY A 23 13.283 4.899 34.398 1.00 8.35 O ANISOU 1274 O GLY A 23 1323 870 977 59 210 -77 O ATOM 1275 N ASP A 24 13.721 4.179 32.317 1.00 9.01 N ANISOU 1275 N ASP A 24 1274 1040 1109 48 80 -69 N ATOM 1276 CA ASP A 24 13.650 5.483 31.680 1.00 9.99 C ANISOU 1276 CA ASP A 24 1247 1299 1246 -64 37 -33 C ATOM 1277 C ASP A 24 12.185 5.770 31.342 1.00 10.07 C ANISOU 1277 C ASP A 24 1235 1323 1268 -57 30 -38 C ATOM 1278 O ASP A 24 11.410 4.830 31.136 1.00 10.27 O ANISOU 1278 O ASP A 24 1139 1205 1556 -279 32 -53 O ATOM 1279 CB ASP A 24 14.483 5.501 30.383 1.00 10.12 C ANISOU 1279 CB ASP A 24 1266 1358 1218 -10 60 -41 C ATOM 1280 CG ASP A 24 15.990 5.507 30.621 1.00 11.43 C ANISOU 1280 CG ASP A 24 1363 1767 1210 -114 166 -45 C ATOM 1281 OD1 ASP A 24 16.451 5.576 31.792 1.00 13.87 O ANISOU 1281 OD1 ASP A 24 1187 2458 1625 -382 443 -136 O ATOM 1282 OD2 ASP A 24 16.802 5.431 29.667 1.00 11.08 O ANISOU 1282 OD2 ASP A 24 1581 1814 812 -62 334 -21 O ATOM 1283 N ASP A 25 11.809 7.044 31.267 1.00 10.01 N ANISOU 1283 N ASP A 25 1245 1336 1219 -90 -3 9 N ATOM 1284 CA ASP A 25 10.415 7.418 30.994 1.00 10.82 C ANISOU 1284 CA ASP A 25 1328 1450 1333 11 38 -2 C ATOM 1285 C ASP A 25 10.060 7.419 29.516 1.00 10.82 C ANISOU 1285 C ASP A 25 1293 1457 1360 20 -28 60 C ATOM 1286 O ASP A 25 8.902 7.601 29.155 1.00 11.05 O ANISOU 1286 O ASP A 25 1168 1574 1453 98 50 108 O ATOM 1287 CB ASP A 25 10.046 8.759 31.633 1.00 10.97 C ANISOU 1287 CB ASP A 25 1437 1347 1381 -55 6 -16 C ATOM 1288 CG ASP A 25 10.825 9.952 31.086 1.00 12.95 C ANISOU 1288 CG ASP A 25 1703 1817 1400 42 34 -33 C ATOM 1289 OD1 ASP A 25 11.686 9.795 30.200 1.00 14.01 O ANISOU 1289 OD1 ASP A 25 2077 2027 1216 197 36 -298 O ATOM 1290 OD2 ASP A 25 10.622 11.123 31.525 1.00 13.52 O ANISOU 1290 OD2 ASP A 25 2273 1446 1418 -146 -92 40 O ATOM 1291 N ALA A 26 11.065 7.210 28.675 1.00 10.23 N ANISOU 1291 N ALA A 26 1232 1340 1315 55 11 77 N ATOM 1292 CA ALA A 26 10.903 7.121 27.227 1.00 10.48 C ANISOU 1292 CA ALA A 26 1349 1290 1343 -10 -52 37 C ATOM 1293 C ALA A 26 12.082 6.390 26.565 1.00 10.57 C ANISOU 1293 C ALA A 26 1346 1366 1301 -45 -25 58 C ATOM 1294 O ALA A 26 13.148 6.252 27.160 1.00 10.39 O ANISOU 1294 O ALA A 26 1488 1228 1231 85 -7 141 O ATOM 1295 CB ALA A 26 10.771 8.526 26.637 1.00 11.58 C ANISOU 1295 CB ALA A 26 1458 1516 1426 -19 -52 43 C ATOM 1296 N PRO A 27 11.893 5.919 25.333 1.00 10.69 N ANISOU 1296 N PRO A 27 1380 1371 1309 -29 -9 32 N ATOM 1297 CA PRO A 27 12.990 5.322 24.582 1.00 11.02 C ANISOU 1297 CA PRO A 27 1422 1414 1350 -26 -32 23 C ATOM 1298 C PRO A 27 14.125 6.317 24.297 1.00 11.08 C ANISOU 1298 C PRO A 27 1463 1394 1352 -42 -40 -5 C ATOM 1299 O PRO A 27 13.888 7.523 24.142 1.00 12.04 O ANISOU 1299 O PRO A 27 1515 1626 1432 -72 27 -53 O ATOM 1300 CB PRO A 27 12.317 4.828 23.285 1.00 10.82 C ANISOU 1300 CB PRO A 27 1409 1365 1333 -18 -44 16 C ATOM 1301 CG PRO A 27 11.036 5.576 23.192 1.00 10.99 C ANISOU 1301 CG PRO A 27 1412 1456 1307 -120 -20 19 C ATOM 1302 CD PRO A 27 10.625 5.904 24.577 1.00 10.80 C ANISOU 1302 CD PRO A 27 1394 1403 1307 -80 0 15 C ATOM 1303 N ARG A 28 15.350 5.821 24.272 1.00 11.13 N ANISOU 1303 N ARG A 28 1436 1443 1348 -44 -15 -64 N ATOM 1304 CA ARG A 28 16.493 6.646 23.880 1.00 12.70 C ANISOU 1304 CA ARG A 28 1618 1603 1603 -10 -10 21 C ATOM 1305 C ARG A 28 16.485 6.928 22.387 1.00 12.28 C ANISOU 1305 C ARG A 28 1540 1593 1530 -29 -47 41 C ATOM 1306 O ARG A 28 16.932 7.984 21.968 1.00 12.38 O ANISOU 1306 O ARG A 28 1413 1736 1553 -116 -138 145 O ATOM 1307 CB ARG A 28 17.832 5.968 24.188 1.00 13.50 C ANISOU 1307 CB ARG A 28 1691 1737 1701 -60 -72 26 C ATOM 1308 CG ARG A 28 18.100 5.706 25.635 1.00 16.93 C ANISOU 1308 CG ARG A 28 2233 2167 2033 -40 16 59 C ATOM 1309 CD ARG A 28 18.211 6.941 26.493 1.00 19.95 C ANISOU 1309 CD ARG A 28 2666 2468 2445 13 27 -46 C ATOM 1310 NE ARG A 28 18.531 6.548 27.862 1.00 22.01 N ANISOU 1310 NE ARG A 28 2549 2925 2887 118 -148 93 N ATOM 1311 CZ ARG A 28 19.763 6.343 28.337 1.00 25.61 C ANISOU 1311 CZ ARG A 28 3062 3485 3182 -8 -89 31 C ATOM 1312 NH1 ARG A 28 20.847 6.533 27.568 1.00 25.51 N ANISOU 1312 NH1 ARG A 28 3003 3639 3051 75 0 36 N ATOM 1313 NH2 ARG A 28 19.911 5.949 29.603 1.00 25.20 N ANISOU 1313 NH2 ARG A 28 2772 3682 3120 -7 -213 49 N ATOM 1314 N ALA A 29 15.996 5.981 21.588 1.00 12.03 N ANISOU 1314 N ALA A 29 1476 1613 1482 -1 -20 30 N ATOM 1315 CA ALA A 29 16.130 6.082 20.145 1.00 12.36 C ANISOU 1315 CA ALA A 29 1511 1618 1567 -12 -28 17 C ATOM 1316 C ALA A 29 14.909 5.500 19.443 1.00 11.97 C ANISOU 1316 C ALA A 29 1465 1548 1535 -56 -59 44 C ATOM 1317 O ALA A 29 14.364 4.460 19.847 1.00 11.92 O ANISOU 1317 O ALA A 29 1545 1474 1508 -167 -127 134 O ATOM 1318 CB ALA A 29 17.402 5.355 19.685 1.00 12.78 C ANISOU 1318 CB ALA A 29 1534 1707 1615 24 -8 11 C ATOM 1319 N VAL A 30 14.465 6.213 18.420 1.00 10.87 N ANISOU 1319 N VAL A 30 1339 1400 1391 -89 19 103 N ATOM 1320 CA VAL A 30 13.363 5.793 17.592 1.00 10.59 C ANISOU 1320 CA VAL A 30 1332 1318 1370 -3 -28 27 C ATOM 1321 C VAL A 30 13.881 5.930 16.182 1.00 10.22 C ANISOU 1321 C VAL A 30 1284 1290 1307 -14 -9 42 C ATOM 1322 O VAL A 30 14.373 6.989 15.804 1.00 9.00 O ANISOU 1322 O VAL A 30 965 1235 1220 17 -88 79 O ATOM 1323 CB VAL A 30 12.133 6.689 17.840 1.00 11.17 C ANISOU 1323 CB VAL A 30 1405 1442 1398 -17 -26 101 C ATOM 1324 CG1 VAL A 30 10.979 6.296 16.936 1.00 11.89 C ANISOU 1324 CG1 VAL A 30 1534 1329 1652 -60 -132 -19 C ATOM 1325 CG2 VAL A 30 11.714 6.624 19.304 1.00 12.28 C ANISOU 1325 CG2 VAL A 30 1406 1596 1662 97 0 -116 C ATOM 1326 N PHE A 31 13.812 4.860 15.405 1.00 10.33 N ANISOU 1326 N PHE A 31 1293 1294 1338 22 21 42 N ATOM 1327 CA PHE A 31 14.364 4.878 14.047 1.00 11.18 C ANISOU 1327 CA PHE A 31 1433 1438 1375 2 4 -2 C ATOM 1328 C PHE A 31 13.629 3.889 13.154 1.00 11.22 C ANISOU 1328 C PHE A 31 1464 1401 1399 -37 15 -11 C ATOM 1329 O PHE A 31 13.065 2.933 13.654 1.00 10.99 O ANISOU 1329 O PHE A 31 1405 1532 1236 -52 128 -136 O ATOM 1330 CB PHE A 31 15.871 4.577 14.064 1.00 11.41 C ANISOU 1330 CB PHE A 31 1434 1463 1435 -31 24 3 C ATOM 1331 CG PHE A 31 16.223 3.221 14.612 1.00 12.94 C ANISOU 1331 CG PHE A 31 1532 1755 1630 47 27 -28 C ATOM 1332 CD1 PHE A 31 16.326 2.118 13.772 1.00 16.19 C ANISOU 1332 CD1 PHE A 31 1874 1997 2281 138 117 145 C ATOM 1333 CD2 PHE A 31 16.428 3.044 15.966 1.00 15.67 C ANISOU 1333 CD2 PHE A 31 1783 2060 2110 171 46 99 C ATOM 1334 CE1 PHE A 31 16.649 0.872 14.281 1.00 16.93 C ANISOU 1334 CE1 PHE A 31 2004 2200 2225 68 32 228 C ATOM 1335 CE2 PHE A 31 16.743 1.796 16.477 1.00 15.85 C ANISOU 1335 CE2 PHE A 31 1879 1955 2188 -13 85 160 C ATOM 1336 CZ PHE A 31 16.852 0.720 15.638 1.00 16.58 C ANISOU 1336 CZ PHE A 31 1979 2163 2155 131 73 59 C ATOM 1337 N PRO A 32 13.642 4.105 11.840 1.00 11.33 N ANISOU 1337 N PRO A 32 1501 1429 1373 -15 31 -18 N ATOM 1338 CA PRO A 32 12.833 3.285 10.936 1.00 11.64 C ANISOU 1338 CA PRO A 32 1522 1479 1421 -59 18 -2 C ATOM 1339 C PRO A 32 13.329 1.845 10.831 1.00 12.59 C ANISOU 1339 C PRO A 32 1620 1625 1538 -38 -24 -27 C ATOM 1340 O PRO A 32 14.536 1.610 10.749 1.00 11.88 O ANISOU 1340 O PRO A 32 1558 1487 1466 -196 -17 -84 O ATOM 1341 CB PRO A 32 12.938 4.018 9.593 1.00 12.17 C ANISOU 1341 CB PRO A 32 1528 1574 1520 -16 3 -3 C ATOM 1342 CG PRO A 32 14.191 4.812 9.673 1.00 11.53 C ANISOU 1342 CG PRO A 32 1559 1414 1406 -46 -5 9 C ATOM 1343 CD PRO A 32 14.364 5.169 11.125 1.00 11.50 C ANISOU 1343 CD PRO A 32 1480 1473 1414 -52 29 -32 C ATOM 1344 N SER A 33 12.384 0.901 10.820 1.00 13.34 N ANISOU 1344 N SER A 33 1704 1680 1682 -41 20 43 N ATOM 1345 CA SER A 33 12.687 -0.514 10.743 1.00 15.43 C ANISOU 1345 CA SER A 33 1969 1951 1939 11 -27 -9 C ATOM 1346 C SER A 33 12.961 -0.953 9.296 1.00 15.82 C ANISOU 1346 C SER A 33 2041 1968 2000 12 -28 -20 C ATOM 1347 O SER A 33 12.146 -1.645 8.663 1.00 16.58 O ANISOU 1347 O SER A 33 2308 1990 2000 192 -12 -92 O ATOM 1348 CB SER A 33 11.555 -1.330 11.389 1.00 15.72 C ANISOU 1348 CB SER A 33 2029 1893 2049 -36 -116 35 C ATOM 1349 OG SER A 33 11.940 -2.722 11.480 1.00 19.75 O ANISOU 1349 OG SER A 33 2554 2313 2636 373 -75 -274 O ATOM 1350 N ILE A 34 14.114 -0.527 8.784 1.00 16.95 N ANISOU 1350 N ILE A 34 2224 2111 2106 50 3 -48 N ATOM 1351 CA ILE A 34 14.483 -0.722 7.379 1.00 17.39 C ANISOU 1351 CA ILE A 34 2267 2172 2168 -14 0 23 C ATOM 1352 C ILE A 34 15.927 -1.153 7.247 1.00 17.36 C ANISOU 1352 C ILE A 34 2260 2173 2160 -52 4 20 C ATOM 1353 O ILE A 34 16.779 -0.789 8.049 1.00 17.63 O ANISOU 1353 O ILE A 34 2478 2195 2023 -103 40 -40 O ATOM 1354 CB ILE A 34 14.274 0.581 6.549 1.00 17.76 C ANISOU 1354 CB ILE A 34 2249 2224 2273 0 -43 -16 C ATOM 1355 CG1 ILE A 34 15.024 1.771 7.188 1.00 18.90 C ANISOU 1355 CG1 ILE A 34 2458 2324 2396 20 44 31 C ATOM 1356 CG2 ILE A 34 12.809 0.897 6.410 1.00 18.00 C ANISOU 1356 CG2 ILE A 34 2273 2286 2277 -65 -38 73 C ATOM 1357 CD1 ILE A 34 15.294 2.868 6.238 1.00 22.66 C ANISOU 1357 CD1 ILE A 34 2776 2934 2900 65 -71 0 C ATOM 1358 N VAL A 35 16.191 -1.932 6.210 1.00 17.89 N ANISOU 1358 N VAL A 35 2279 2249 2270 -76 -26 -24 N ATOM 1359 CA VAL A 35 17.538 -2.258 5.779 1.00 18.56 C ANISOU 1359 CA VAL A 35 2349 2364 2337 -69 -52 13 C ATOM 1360 C VAL A 35 17.626 -1.827 4.320 1.00 19.17 C ANISOU 1360 C VAL A 35 2443 2416 2424 -45 -50 56 C ATOM 1361 O VAL A 35 16.749 -2.143 3.511 1.00 18.78 O ANISOU 1361 O VAL A 35 2362 2336 2438 -68 -171 57 O ATOM 1362 CB VAL A 35 17.857 -3.773 5.933 1.00 18.00 C ANISOU 1362 CB VAL A 35 2257 2282 2299 -52 -10 1 C ATOM 1363 CG1 VAL A 35 19.227 -4.127 5.347 1.00 18.80 C ANISOU 1363 CG1 VAL A 35 2397 2350 2395 -155 -138 79 C ATOM 1364 CG2 VAL A 35 17.780 -4.178 7.387 1.00 18.40 C ANISOU 1364 CG2 VAL A 35 2314 2300 2376 -28 -186 116 C ATOM 1365 N GLY A 36 18.683 -1.094 3.990 1.00 19.78 N ANISOU 1365 N GLY A 36 2477 2506 2532 -4 -26 54 N ATOM 1366 CA GLY A 36 18.872 -0.598 2.637 1.00 20.54 C ANISOU 1366 CA GLY A 36 2590 2639 2574 19 15 7 C ATOM 1367 C GLY A 36 20.173 -1.087 2.046 1.00 20.92 C ANISOU 1367 C GLY A 36 2620 2681 2646 34 0 -19 C ATOM 1368 O GLY A 36 21.169 -1.174 2.742 1.00 21.40 O ANISOU 1368 O GLY A 36 2609 2804 2716 123 69 10 O ATOM 1369 N ARG A 37 20.149 -1.403 0.758 1.00 21.38 N ANISOU 1369 N ARG A 37 2717 2753 2650 18 34 28 N ATOM 1370 CA ARG A 37 21.306 -1.923 0.039 1.00 21.37 C ANISOU 1370 CA ARG A 37 2680 2710 2727 -4 5 20 C ATOM 1371 C ARG A 37 21.477 -1.113 -1.270 1.00 21.74 C ANISOU 1371 C ARG A 37 2749 2778 2733 -9 24 26 C ATOM 1372 O ARG A 37 20.496 -0.605 -1.817 1.00 20.54 O ANISOU 1372 O ARG A 37 2638 2521 2644 -46 15 128 O ATOM 1373 CB ARG A 37 21.107 -3.410 -0.284 1.00 21.64 C ANISOU 1373 CB ARG A 37 2705 2761 2754 5 -23 13 C ATOM 1374 CG ARG A 37 20.964 -4.351 0.926 1.00 20.81 C ANISOU 1374 CG ARG A 37 2627 2632 2646 -32 -37 -23 C ATOM 1375 CD ARG A 37 20.548 -5.770 0.546 1.00 21.94 C ANISOU 1375 CD ARG A 37 2692 2859 2785 -3 -151 119 C ATOM 1376 NE ARG A 37 20.729 -6.719 1.639 1.00 21.42 N ANISOU 1376 NE ARG A 37 2494 2813 2829 -162 -6 104 N ATOM 1377 CZ ARG A 37 19.845 -6.965 2.609 1.00 21.83 C ANISOU 1377 CZ ARG A 37 2687 2786 2819 -39 -30 -37 C ATOM 1378 NH1 ARG A 37 18.669 -6.343 2.648 1.00 21.37 N ANISOU 1378 NH1 ARG A 37 2569 2867 2682 -268 -83 -116 N ATOM 1379 NH2 ARG A 37 20.146 -7.854 3.548 1.00 20.85 N ANISOU 1379 NH2 ARG A 37 2564 2773 2582 -177 59 40 N ATOM 1380 N PRO A 38 22.712 -1.003 -1.762 1.00 22.65 N ANISOU 1380 N PRO A 38 2860 2885 2859 0 14 6 N ATOM 1381 CA PRO A 38 23.040 -0.227 -2.980 1.00 23.10 C ANISOU 1381 CA PRO A 38 2916 2934 2925 13 6 -13 C ATOM 1382 C PRO A 38 22.071 -0.358 -4.159 1.00 23.35 C ANISOU 1382 C PRO A 38 2919 2994 2957 8 0 -100 C ATOM 1383 O PRO A 38 21.854 -1.498 -4.582 1.00 23.42 O ANISOU 1383 O PRO A 38 2983 2952 2962 176 39 -265 O ATOM 1384 CB PRO A 38 24.403 -0.799 -3.390 1.00 23.25 C ANISOU 1384 CB PRO A 38 2944 2981 2909 1 25 -12 C ATOM 1385 CG PRO A 38 25.020 -1.307 -2.118 1.00 23.16 C ANISOU 1385 CG PRO A 38 2893 2980 2926 15 -5 19 C ATOM 1386 CD PRO A 38 23.909 -1.648 -1.184 1.00 22.67 C ANISOU 1386 CD PRO A 38 2838 2934 2840 15 -19 28 C ATOM 1387 N ASP A 51 28.120 -2.970 2.504 1.00 28.60 N ANISOU 1387 N ASP A 51 3638 3675 3554 60 15 -83 N ATOM 1388 CA ASP A 51 27.123 -3.605 1.624 1.00 28.95 C ANISOU 1388 CA ASP A 51 3693 3678 3628 21 6 -32 C ATOM 1389 C ASP A 51 25.650 -3.380 2.022 1.00 27.98 C ANISOU 1389 C ASP A 51 3598 3523 3508 0 -27 -21 C ATOM 1390 O ASP A 51 24.746 -3.601 1.203 1.00 28.15 O ANISOU 1390 O ASP A 51 3746 3491 3459 8 -6 -45 O ATOM 1391 CB ASP A 51 27.422 -5.109 1.427 1.00 29.77 C ANISOU 1391 CB ASP A 51 3795 3784 3732 -9 -38 -2 C ATOM 1392 CG ASP A 51 27.401 -5.922 2.737 1.00 32.06 C ANISOU 1392 CG ASP A 51 4051 4186 3944 53 -90 -18 C ATOM 1393 OD1 ASP A 51 28.365 -6.695 2.965 1.00 35.72 O ANISOU 1393 OD1 ASP A 51 4571 4654 4348 -20 -362 -46 O ATOM 1394 OD2 ASP A 51 26.459 -5.903 3.567 1.00 36.70 O ANISOU 1394 OD2 ASP A 51 4745 4857 4342 83 -216 16 O ATOM 1395 N SER A 52 25.402 -2.974 3.269 1.00 26.37 N ANISOU 1395 N SER A 52 3381 3308 3329 -2 5 -53 N ATOM 1396 CA SER A 52 24.062 -2.557 3.690 1.00 25.59 C ANISOU 1396 CA SER A 52 3311 3192 3218 -25 -11 -35 C ATOM 1397 C SER A 52 24.088 -1.501 4.799 1.00 24.34 C ANISOU 1397 C SER A 52 3152 3016 3078 -2 15 -52 C ATOM 1398 O SER A 52 25.090 -1.311 5.480 1.00 23.63 O ANISOU 1398 O SER A 52 3030 2954 2992 35 56 -142 O ATOM 1399 CB SER A 52 23.210 -3.753 4.146 1.00 25.50 C ANISOU 1399 CB SER A 52 3316 3161 3211 -54 -7 -54 C ATOM 1400 OG SER A 52 23.671 -4.279 5.372 1.00 25.81 O ANISOU 1400 OG SER A 52 3491 3071 3242 -179 -64 2 O ATOM 1401 N TYR A 53 22.952 -0.842 4.962 1.00 23.22 N ANISOU 1401 N TYR A 53 2988 2879 2952 -2 22 1 N ATOM 1402 CA TYR A 53 22.772 0.204 5.955 1.00 22.75 C ANISOU 1402 CA TYR A 53 2889 2853 2899 10 4 16 C ATOM 1403 C TYR A 53 21.443 -0.041 6.666 1.00 22.00 C ANISOU 1403 C TYR A 53 2820 2695 2843 17 -15 50 C ATOM 1404 O TYR A 53 20.510 -0.596 6.092 1.00 21.41 O ANISOU 1404 O TYR A 53 2684 2589 2860 -35 -58 44 O ATOM 1405 CB TYR A 53 22.752 1.586 5.295 1.00 23.15 C ANISOU 1405 CB TYR A 53 2969 2894 2932 -15 26 28 C ATOM 1406 CG TYR A 53 24.033 1.983 4.586 1.00 24.49 C ANISOU 1406 CG TYR A 53 2930 3204 3170 66 55 35 C ATOM 1407 CD1 TYR A 53 24.291 1.550 3.284 1.00 27.15 C ANISOU 1407 CD1 TYR A 53 3218 3557 3540 -18 73 97 C ATOM 1408 CD2 TYR A 53 24.970 2.809 5.201 1.00 26.98 C ANISOU 1408 CD2 TYR A 53 3258 3500 3490 -56 175 30 C ATOM 1409 CE1 TYR A 53 25.475 1.915 2.609 1.00 29.24 C ANISOU 1409 CE1 TYR A 53 3554 3808 3748 23 91 -20 C ATOM 1410 CE2 TYR A 53 26.167 3.171 4.535 1.00 29.60 C ANISOU 1410 CE2 TYR A 53 3632 3857 3757 -149 13 13 C ATOM 1411 CZ TYR A 53 26.406 2.720 3.239 1.00 29.28 C ANISOU 1411 CZ TYR A 53 3436 3895 3792 -133 148 -57 C ATOM 1412 OH TYR A 53 27.563 3.074 2.558 1.00 32.52 O ANISOU 1412 OH TYR A 53 3761 4489 4105 -67 -70 -37 O ATOM 1413 N VAL A 54 21.353 0.385 7.913 1.00 20.68 N ANISOU 1413 N VAL A 54 2692 2536 2627 32 29 5 N ATOM 1414 CA VAL A 54 20.173 0.105 8.708 1.00 20.94 C ANISOU 1414 CA VAL A 54 2639 2625 2690 14 -19 -2 C ATOM 1415 C VAL A 54 19.634 1.390 9.327 1.00 20.56 C ANISOU 1415 C VAL A 54 2594 2596 2618 53 49 -21 C ATOM 1416 O VAL A 54 20.398 2.288 9.700 1.00 19.32 O ANISOU 1416 O VAL A 54 2339 2396 2604 126 80 -151 O ATOM 1417 CB VAL A 54 20.501 -0.893 9.837 1.00 20.87 C ANISOU 1417 CB VAL A 54 2648 2616 2663 13 19 10 C ATOM 1418 CG1 VAL A 54 19.255 -1.335 10.541 1.00 22.15 C ANISOU 1418 CG1 VAL A 54 2842 2830 2743 -32 -132 100 C ATOM 1419 CG2 VAL A 54 21.285 -2.099 9.283 1.00 22.72 C ANISOU 1419 CG2 VAL A 54 2940 2821 2872 -52 -16 76 C ATOM 1420 N GLY A 55 18.316 1.475 9.424 1.00 20.73 N ANISOU 1420 N GLY A 55 2615 2648 2611 50 34 -13 N ATOM 1421 CA GLY A 55 17.699 2.488 10.257 1.00 21.66 C ANISOU 1421 CA GLY A 55 2715 2755 2760 -3 59 54 C ATOM 1422 C GLY A 55 17.849 3.877 9.694 1.00 22.47 C ANISOU 1422 C GLY A 55 2741 2898 2899 -31 67 21 C ATOM 1423 O GLY A 55 17.659 4.094 8.498 1.00 20.96 O ANISOU 1423 O GLY A 55 2541 2777 2646 -140 70 155 O ATOM 1424 N ASP A 56 18.196 4.802 10.581 1.00 23.63 N ANISOU 1424 N ASP A 56 2921 3070 2983 -23 90 -1 N ATOM 1425 CA ASP A 56 18.397 6.207 10.247 1.00 25.22 C ANISOU 1425 CA ASP A 56 3158 3236 3187 -20 67 20 C ATOM 1426 C ASP A 56 19.398 6.464 9.109 1.00 25.44 C ANISOU 1426 C ASP A 56 3229 3261 3176 -19 87 -19 C ATOM 1427 O ASP A 56 19.198 7.375 8.308 1.00 24.93 O ANISOU 1427 O ASP A 56 3193 3234 3044 -116 240 17 O ATOM 1428 CB ASP A 56 18.827 7.007 11.493 1.00 25.90 C ANISOU 1428 CB ASP A 56 3265 3346 3227 43 29 10 C ATOM 1429 CG ASP A 56 19.899 6.288 12.347 1.00 29.15 C ANISOU 1429 CG ASP A 56 3528 3815 3731 23 -12 68 C ATOM 1430 OD1 ASP A 56 19.644 5.129 12.811 1.00 30.70 O ANISOU 1430 OD1 ASP A 56 3762 4008 3895 436 53 -108 O ATOM 1431 OD2 ASP A 56 21.005 6.827 12.623 1.00 33.17 O ANISOU 1431 OD2 ASP A 56 3849 4408 4344 -276 -194 146 O ATOM 1432 N GLU A 57 20.462 5.680 9.037 1.00 25.95 N ANISOU 1432 N GLU A 57 3270 3306 3283 -24 33 -6 N ATOM 1433 CA GLU A 57 21.426 5.857 7.944 1.00 26.71 C ANISOU 1433 CA GLU A 57 3357 3416 3375 -30 47 7 C ATOM 1434 C GLU A 57 20.925 5.305 6.618 1.00 26.31 C ANISOU 1434 C GLU A 57 3325 3346 3324 -35 49 22 C ATOM 1435 O GLU A 57 21.278 5.836 5.570 1.00 26.51 O ANISOU 1435 O GLU A 57 3366 3359 3346 -145 155 70 O ATOM 1436 CB GLU A 57 22.820 5.311 8.261 1.00 27.83 C ANISOU 1436 CB GLU A 57 3553 3512 3508 15 1 20 C ATOM 1437 CG GLU A 57 22.899 4.100 9.175 1.00 30.59 C ANISOU 1437 CG GLU A 57 3718 4015 3888 -35 112 -32 C ATOM 1438 CD GLU A 57 24.246 4.006 9.871 1.00 33.95 C ANISOU 1438 CD GLU A 57 3993 4598 4305 -44 -27 -270 C ATOM 1439 OE1 GLU A 57 24.296 4.242 11.110 1.00 35.37 O ANISOU 1439 OE1 GLU A 57 4322 4823 4295 -66 166 -249 O ATOM 1440 OE2 GLU A 57 25.249 3.705 9.166 1.00 35.97 O ANISOU 1440 OE2 GLU A 57 3903 5101 4661 21 30 -678 O ATOM 1441 N ALA A 58 20.103 4.255 6.644 1.00 25.54 N ANISOU 1441 N ALA A 58 3248 3238 3216 -17 38 34 N ATOM 1442 CA ALA A 58 19.439 3.793 5.415 1.00 25.28 C ANISOU 1442 CA ALA A 58 3183 3194 3226 20 37 0 C ATOM 1443 C ALA A 58 18.478 4.866 4.915 1.00 25.13 C ANISOU 1443 C ALA A 58 3149 3197 3203 22 20 -4 C ATOM 1444 O ALA A 58 18.379 5.119 3.714 1.00 24.16 O ANISOU 1444 O ALA A 58 3007 3102 3070 102 133 -17 O ATOM 1445 CB ALA A 58 18.693 2.502 5.652 1.00 25.38 C ANISOU 1445 CB ALA A 58 3192 3197 3253 3 24 -25 C ATOM 1446 N GLN A 59 17.784 5.506 5.856 1.00 24.68 N ANISOU 1446 N GLN A 59 3112 3149 3114 31 53 -22 N ATOM 1447 CA GLN A 59 16.819 6.544 5.522 1.00 25.07 C ANISOU 1447 CA GLN A 59 3171 3186 3166 -6 -13 -1 C ATOM 1448 C GLN A 59 17.543 7.738 4.906 1.00 25.24 C ANISOU 1448 C GLN A 59 3193 3181 3215 11 -74 -25 C ATOM 1449 O GLN A 59 17.194 8.201 3.831 1.00 24.52 O ANISOU 1449 O GLN A 59 3198 3091 3026 -16 -242 -17 O ATOM 1450 CB GLN A 59 16.035 6.955 6.778 1.00 25.35 C ANISOU 1450 CB GLN A 59 3229 3195 3207 32 -57 -36 C ATOM 1451 CG GLN A 59 14.876 7.913 6.542 1.00 26.85 C ANISOU 1451 CG GLN A 59 3428 3584 3189 -4 -44 5 C ATOM 1452 CD GLN A 59 13.771 7.303 5.702 1.00 28.20 C ANISOU 1452 CD GLN A 59 3774 3866 3074 -107 -18 125 C ATOM 1453 OE1 GLN A 59 13.775 7.461 4.492 1.00 29.66 O ANISOU 1453 OE1 GLN A 59 4264 4282 2723 -156 -20 -78 O ATOM 1454 NE2 GLN A 59 12.820 6.632 6.337 1.00 26.70 N ANISOU 1454 NE2 GLN A 59 3792 3728 2626 -277 90 543 N ATOM 1455 N SER A 60 18.598 8.203 5.560 1.00 25.25 N ANISOU 1455 N SER A 60 3196 3192 3206 1 -55 -28 N ATOM 1456 CA SER A 60 19.283 9.395 5.082 1.00 25.52 C ANISOU 1456 CA SER A 60 3179 3264 3252 -22 -36 0 C ATOM 1457 C SER A 60 20.054 9.161 3.751 1.00 24.76 C ANISOU 1457 C SER A 60 3120 3151 3137 -25 -20 -1 C ATOM 1458 O SER A 60 20.186 10.075 2.959 1.00 24.87 O ANISOU 1458 O SER A 60 3042 3284 3121 -39 -14 23 O ATOM 1459 CB SER A 60 20.187 9.964 6.178 1.00 25.91 C ANISOU 1459 CB SER A 60 3223 3326 3294 -21 -43 0 C ATOM 1460 OG SER A 60 21.535 9.694 5.880 1.00 27.65 O ANISOU 1460 OG SER A 60 3178 3707 3621 66 -111 -21 O ATOM 1461 N LYS A 61 20.513 7.937 3.500 1.00 24.36 N ANISOU 1461 N LYS A 61 3054 3116 3084 -17 -42 25 N ATOM 1462 CA LYS A 61 21.210 7.591 2.255 1.00 23.92 C ANISOU 1462 CA LYS A 61 3032 3016 3041 -7 -16 -11 C ATOM 1463 C LYS A 61 20.280 6.946 1.214 1.00 23.48 C ANISOU 1463 C LYS A 61 2995 2918 3005 5 3 29 C ATOM 1464 O LYS A 61 20.743 6.336 0.241 1.00 22.49 O ANISOU 1464 O LYS A 61 2923 2774 2845 17 33 33 O ATOM 1465 CB LYS A 61 22.398 6.670 2.555 1.00 24.49 C ANISOU 1465 CB LYS A 61 3117 3098 3090 -38 -17 -16 C ATOM 1466 CG LYS A 61 23.587 7.400 3.191 1.00 26.12 C ANISOU 1466 CG LYS A 61 3247 3377 3298 42 -50 -44 C ATOM 1467 CD LYS A 61 24.733 6.454 3.550 1.00 28.77 C ANISOU 1467 CD LYS A 61 3690 3606 3636 -2 -99 -53 C ATOM 1468 CE LYS A 61 25.713 7.101 4.558 1.00 30.01 C ANISOU 1468 CE LYS A 61 3799 3773 3830 8 -109 26 C ATOM 1469 NZ LYS A 61 26.364 8.338 4.052 1.00 31.11 N ANISOU 1469 NZ LYS A 61 4072 3793 3954 -29 -179 30 N ATOM 1470 N ARG A 62 18.972 7.121 1.363 1.00 23.02 N ANISOU 1470 N ARG A 62 2953 2855 2937 -53 14 26 N ATOM 1471 CA ARG A 62 18.033 6.385 0.506 1.00 23.49 C ANISOU 1471 CA ARG A 62 2983 2961 2982 7 10 11 C ATOM 1472 C ARG A 62 18.101 6.752 -0.963 1.00 23.46 C ANISOU 1472 C ARG A 62 2983 2958 2972 -30 23 0 C ATOM 1473 O ARG A 62 17.595 6.004 -1.797 1.00 23.79 O ANISOU 1473 O ARG A 62 3006 2935 3096 -113 43 -62 O ATOM 1474 CB ARG A 62 16.592 6.471 1.014 1.00 23.20 C ANISOU 1474 CB ARG A 62 2920 2949 2944 -2 9 36 C ATOM 1475 CG ARG A 62 15.908 7.800 0.834 1.00 22.66 C ANISOU 1475 CG ARG A 62 2882 2910 2816 -4 3 -7 C ATOM 1476 CD ARG A 62 14.517 7.792 1.380 1.00 21.52 C ANISOU 1476 CD ARG A 62 2702 2736 2739 95 125 -55 C ATOM 1477 NE ARG A 62 13.659 6.840 0.687 1.00 21.29 N ANISOU 1477 NE ARG A 62 2592 2820 2676 206 190 55 N ATOM 1478 CZ ARG A 62 12.623 6.199 1.228 1.00 23.05 C ANISOU 1478 CZ ARG A 62 2932 2926 2898 67 28 5 C ATOM 1479 NH1 ARG A 62 12.284 6.375 2.499 1.00 22.80 N ANISOU 1479 NH1 ARG A 62 2726 3136 2797 3 201 -69 N ATOM 1480 NH2 ARG A 62 11.913 5.360 0.488 1.00 23.42 N ANISOU 1480 NH2 ARG A 62 3045 2959 2894 105 -48 -39 N ATOM 1481 N GLY A 63 18.722 7.892 -1.280 1.00 23.57 N ANISOU 1481 N GLY A 63 2982 2975 2999 7 8 -48 N ATOM 1482 CA GLY A 63 18.980 8.273 -2.660 1.00 23.52 C ANISOU 1482 CA GLY A 63 2998 2947 2992 -12 -12 0 C ATOM 1483 C GLY A 63 19.669 7.189 -3.486 1.00 23.99 C ANISOU 1483 C GLY A 63 3058 3026 3031 5 -17 -13 C ATOM 1484 O GLY A 63 19.357 7.026 -4.665 1.00 23.76 O ANISOU 1484 O GLY A 63 3136 2931 2961 16 -167 -64 O ATOM 1485 N ILE A 64 20.602 6.458 -2.872 1.00 24.09 N ANISOU 1485 N ILE A 64 3068 3031 3052 15 -23 13 N ATOM 1486 CA ILE A 64 21.394 5.440 -3.573 1.00 24.68 C ANISOU 1486 CA ILE A 64 3074 3131 3169 -6 -7 8 C ATOM 1487 C ILE A 64 21.075 3.982 -3.148 1.00 24.28 C ANISOU 1487 C ILE A 64 3014 3083 3126 19 0 -24 C ATOM 1488 O ILE A 64 21.758 3.057 -3.576 1.00 23.81 O ANISOU 1488 O ILE A 64 2844 3102 3100 62 127 -146 O ATOM 1489 CB ILE A 64 22.924 5.744 -3.402 1.00 25.42 C ANISOU 1489 CB ILE A 64 3216 3220 3221 -14 -19 28 C ATOM 1490 CG1 ILE A 64 23.389 5.556 -1.941 1.00 27.24 C ANISOU 1490 CG1 ILE A 64 3326 3476 3548 -15 -37 2 C ATOM 1491 CG2 ILE A 64 23.235 7.162 -3.864 1.00 25.75 C ANISOU 1491 CG2 ILE A 64 3249 3222 3312 -24 -37 14 C ATOM 1492 CD1 ILE A 64 24.923 5.677 -1.769 1.00 29.61 C ANISOU 1492 CD1 ILE A 64 3670 3666 3914 50 -145 9 C ATOM 1493 N LEU A 65 20.043 3.791 -2.322 1.00 23.31 N ANISOU 1493 N LEU A 65 2892 3004 2958 16 39 -13 N ATOM 1494 CA LEU A 65 19.637 2.467 -1.821 1.00 23.28 C ANISOU 1494 CA LEU A 65 2923 2952 2968 32 8 -24 C ATOM 1495 C LEU A 65 18.210 2.094 -2.192 1.00 23.17 C ANISOU 1495 C LEU A 65 2887 2930 2986 1 23 -17 C ATOM 1496 O LEU A 65 17.410 2.959 -2.543 1.00 23.67 O ANISOU 1496 O LEU A 65 2800 2962 3229 -31 37 -53 O ATOM 1497 CB LEU A 65 19.730 2.420 -0.287 1.00 23.13 C ANISOU 1497 CB LEU A 65 2915 2967 2903 15 26 5 C ATOM 1498 CG LEU A 65 21.032 2.934 0.327 1.00 23.66 C ANISOU 1498 CG LEU A 65 3052 3040 2898 10 -11 42 C ATOM 1499 CD1 LEU A 65 20.858 3.121 1.814 1.00 24.74 C ANISOU 1499 CD1 LEU A 65 3144 3136 3120 -78 -126 17 C ATOM 1500 CD2 LEU A 65 22.188 1.988 0.008 1.00 23.84 C ANISOU 1500 CD2 LEU A 65 3082 3101 2875 62 17 40 C ATOM 1501 N THR A 66 17.912 0.797 -2.128 1.00 22.95 N ANISOU 1501 N THR A 66 2904 2921 2895 6 55 -2 N ATOM 1502 CA THR A 66 16.537 0.301 -2.079 1.00 23.33 C ANISOU 1502 CA THR A 66 2953 2954 2955 8 56 17 C ATOM 1503 C THR A 66 16.315 -0.320 -0.702 1.00 22.92 C ANISOU 1503 C THR A 66 2893 2915 2898 13 65 46 C ATOM 1504 O THR A 66 17.223 -0.908 -0.093 1.00 22.73 O ANISOU 1504 O THR A 66 2820 2946 2870 102 153 107 O ATOM 1505 CB THR A 66 16.215 -0.760 -3.166 1.00 23.37 C ANISOU 1505 CB THR A 66 2972 2965 2940 1 80 21 C ATOM 1506 OG1 THR A 66 17.139 -1.851 -3.062 1.00 24.65 O ANISOU 1506 OG1 THR A 66 3258 2762 3344 -13 169 104 O ATOM 1507 CG2 THR A 66 16.393 -0.201 -4.603 1.00 24.45 C ANISOU 1507 CG2 THR A 66 3074 3095 3120 -47 1 -13 C ATOM 1508 N LEU A 67 15.095 -0.187 -0.215 1.00 22.33 N ANISOU 1508 N LEU A 67 2784 2839 2859 -5 36 38 N ATOM 1509 CA LEU A 67 14.792 -0.534 1.153 1.00 21.89 C ANISOU 1509 CA LEU A 67 2788 2765 2762 -11 6 -8 C ATOM 1510 C LEU A 67 13.931 -1.793 1.234 1.00 21.20 C ANISOU 1510 C LEU A 67 2717 2668 2669 -10 6 4 C ATOM 1511 O LEU A 67 13.135 -2.070 0.350 1.00 20.49 O ANISOU 1511 O LEU A 67 2747 2563 2473 -58 -60 -28 O ATOM 1512 CB LEU A 67 14.073 0.648 1.804 1.00 22.56 C ANISOU 1512 CB LEU A 67 2901 2791 2877 -19 -40 -33 C ATOM 1513 CG LEU A 67 14.838 1.986 1.709 1.00 23.42 C ANISOU 1513 CG LEU A 67 2917 2893 3088 -15 -82 12 C ATOM 1514 CD1 LEU A 67 14.058 3.038 2.471 1.00 23.68 C ANISOU 1514 CD1 LEU A 67 3134 2844 3018 77 -105 -123 C ATOM 1515 CD2 LEU A 67 16.246 1.884 2.263 1.00 24.84 C ANISOU 1515 CD2 LEU A 67 3147 2978 3313 13 -33 -72 C ATOM 1516 N LYS A 68 14.105 -2.522 2.332 1.00 20.19 N ANISOU 1516 N LYS A 68 2573 2517 2580 10 -5 60 N ATOM 1517 CA LYS A 68 13.298 -3.675 2.687 1.00 19.81 C ANISOU 1517 CA LYS A 68 2539 2492 2493 21 9 29 C ATOM 1518 C LYS A 68 12.851 -3.477 4.151 1.00 19.14 C ANISOU 1518 C LYS A 68 2457 2417 2396 20 36 0 C ATOM 1519 O LYS A 68 13.600 -2.914 4.973 1.00 19.41 O ANISOU 1519 O LYS A 68 2554 2513 2304 69 46 89 O ATOM 1520 CB LYS A 68 14.142 -4.955 2.568 1.00 19.90 C ANISOU 1520 CB LYS A 68 2590 2459 2509 -12 61 -21 C ATOM 1521 CG LYS A 68 14.367 -5.446 1.136 1.00 20.98 C ANISOU 1521 CG LYS A 68 2690 2631 2646 0 57 69 C ATOM 1522 CD LYS A 68 15.377 -6.595 1.072 1.00 20.89 C ANISOU 1522 CD LYS A 68 2656 2589 2692 -53 78 -25 C ATOM 1523 CE LYS A 68 14.783 -7.919 1.558 1.00 20.27 C ANISOU 1523 CE LYS A 68 2590 2609 2500 -44 192 37 C ATOM 1524 NZ LYS A 68 13.722 -8.442 0.649 1.00 18.45 N ANISOU 1524 NZ LYS A 68 2476 2399 2135 -405 188 -176 N ATOM 1525 N TYR A 69 11.647 -3.941 4.465 1.00 18.38 N ANISOU 1525 N TYR A 69 2340 2359 2281 56 29 12 N ATOM 1526 CA TYR A 69 11.065 -3.836 5.807 1.00 17.74 C ANISOU 1526 CA TYR A 69 2240 2299 2199 26 -12 -33 C ATOM 1527 C TYR A 69 10.902 -5.287 6.361 1.00 16.37 C ANISOU 1527 C TYR A 69 2047 2118 2053 14 -25 -7 C ATOM 1528 O TYR A 69 10.101 -6.095 5.831 1.00 14.82 O ANISOU 1528 O TYR A 69 1715 2152 1763 28 -80 -168 O ATOM 1529 CB TYR A 69 9.709 -3.104 5.749 1.00 18.02 C ANISOU 1529 CB TYR A 69 2370 2238 2237 26 -14 -25 C ATOM 1530 CG TYR A 69 9.776 -1.650 5.303 1.00 20.53 C ANISOU 1530 CG TYR A 69 2692 2574 2532 102 21 -57 C ATOM 1531 CD1 TYR A 69 10.059 -1.320 3.978 1.00 22.07 C ANISOU 1531 CD1 TYR A 69 3112 2577 2695 185 20 5 C ATOM 1532 CD2 TYR A 69 9.536 -0.603 6.211 1.00 22.15 C ANISOU 1532 CD2 TYR A 69 3134 2556 2726 -14 -132 -52 C ATOM 1533 CE1 TYR A 69 10.126 0.015 3.557 1.00 25.04 C ANISOU 1533 CE1 TYR A 69 3556 2918 3039 168 -22 -234 C ATOM 1534 CE2 TYR A 69 9.583 0.730 5.806 1.00 24.48 C ANISOU 1534 CE2 TYR A 69 3549 2894 2856 18 -62 -88 C ATOM 1535 CZ TYR A 69 9.886 1.031 4.476 1.00 25.40 C ANISOU 1535 CZ TYR A 69 3762 2864 3024 62 -61 -116 C ATOM 1536 OH TYR A 69 9.952 2.329 4.057 1.00 25.15 O ANISOU 1536 OH TYR A 69 3968 2643 2942 13 -205 -157 O ATOM 1537 N PRO A 70 11.690 -5.647 7.378 1.00 14.96 N ANISOU 1537 N PRO A 70 1872 1941 1871 -32 -54 -68 N ATOM 1538 CA PRO A 70 11.630 -7.002 7.935 1.00 14.33 C ANISOU 1538 CA PRO A 70 1800 1805 1837 27 -25 -40 C ATOM 1539 C PRO A 70 10.348 -7.369 8.686 1.00 13.46 C ANISOU 1539 C PRO A 70 1682 1682 1747 10 28 -66 C ATOM 1540 O PRO A 70 10.141 -8.553 8.918 1.00 13.24 O ANISOU 1540 O PRO A 70 1495 1744 1791 153 149 -153 O ATOM 1541 CB PRO A 70 12.849 -7.072 8.875 1.00 14.62 C ANISOU 1541 CB PRO A 70 1867 1814 1871 -24 -17 -71 C ATOM 1542 CG PRO A 70 13.191 -5.684 9.190 1.00 15.42 C ANISOU 1542 CG PRO A 70 1916 1987 1954 -44 -73 -20 C ATOM 1543 CD PRO A 70 12.708 -4.822 8.047 1.00 15.69 C ANISOU 1543 CD PRO A 70 1913 2053 1995 -6 -39 25 C ATOM 1544 N ILE A 71 9.543 -6.381 9.071 1.00 13.28 N ANISOU 1544 N ILE A 71 1699 1621 1726 -7 15 -17 N ATOM 1545 CA ILE A 71 8.285 -6.577 9.779 1.00 13.64 C ANISOU 1545 CA ILE A 71 1787 1659 1736 16 58 -52 C ATOM 1546 C ILE A 71 7.169 -6.063 8.900 1.00 13.46 C ANISOU 1546 C ILE A 71 1754 1635 1724 19 97 -42 C ATOM 1547 O ILE A 71 7.213 -4.910 8.456 1.00 14.10 O ANISOU 1547 O ILE A 71 1826 1636 1894 27 163 -107 O ATOM 1548 CB ILE A 71 8.297 -5.861 11.164 1.00 13.62 C ANISOU 1548 CB ILE A 71 1752 1684 1737 43 26 -35 C ATOM 1549 CG1 ILE A 71 9.347 -6.530 12.053 1.00 16.72 C ANISOU 1549 CG1 ILE A 71 2190 2125 2036 86 37 -76 C ATOM 1550 CG2 ILE A 71 6.915 -5.947 11.820 1.00 14.67 C ANISOU 1550 CG2 ILE A 71 2004 1777 1791 2 82 -11 C ATOM 1551 CD1 ILE A 71 9.493 -5.986 13.462 1.00 17.00 C ANISOU 1551 CD1 ILE A 71 2308 2094 2055 157 -126 -138 C ATOM 1552 N GLU A 72 6.200 -6.940 8.629 1.00 13.18 N ANISOU 1552 N GLU A 72 1716 1613 1675 -49 164 -19 N ATOM 1553 CA GLU A 72 5.028 -6.672 7.813 1.00 13.35 C ANISOU 1553 CA GLU A 72 1680 1677 1714 -54 103 -18 C ATOM 1554 C GLU A 72 3.758 -6.931 8.685 1.00 12.82 C ANISOU 1554 C GLU A 72 1660 1567 1642 -15 101 -11 C ATOM 1555 O GLU A 72 3.602 -8.003 9.265 1.00 11.55 O ANISOU 1555 O GLU A 72 1517 1294 1574 -79 139 -91 O ATOM 1556 CB GLU A 72 5.036 -7.611 6.571 1.00 14.43 C ANISOU 1556 CB GLU A 72 1806 1858 1816 -112 172 1 C ATOM 1557 CG GLU A 72 6.308 -7.518 5.693 1.00 19.75 C ANISOU 1557 CG GLU A 72 2583 2473 2447 -188 16 -114 C ATOM 1558 CD GLU A 72 6.348 -8.428 4.438 1.00 26.26 C ANISOU 1558 CD GLU A 72 3594 3338 3045 -678 183 -35 C ATOM 1559 OE1 GLU A 72 5.707 -9.507 4.427 1.00 27.96 O ANISOU 1559 OE1 GLU A 72 4294 3109 3221 -1414 25 -13 O ATOM 1560 OE2 GLU A 72 7.069 -8.068 3.439 1.00 32.43 O ANISOU 1560 OE2 GLU A 72 4319 3989 4012 -983 15 18 O ATOM 1561 N HIS A 73 2.861 -5.949 8.759 1.00 11.90 N ANISOU 1561 N HIS A 73 1500 1407 1614 24 128 13 N ATOM 1562 CA HIS A 73 1.650 -6.030 9.576 1.00 11.94 C ANISOU 1562 CA HIS A 73 1535 1452 1548 56 60 12 C ATOM 1563 C HIS A 73 1.902 -6.565 11.005 1.00 11.36 C ANISOU 1563 C HIS A 73 1426 1368 1521 72 45 -7 C ATOM 1564 O HIS A 73 1.128 -7.349 11.550 1.00 10.47 O ANISOU 1564 O HIS A 73 1319 1147 1512 64 123 10 O ATOM 1565 CB HIS A 73 0.632 -6.889 8.880 1.00 12.01 C ANISOU 1565 CB HIS A 73 1434 1554 1575 52 4 1 C ATOM 1566 CG HIS A 73 0.316 -6.465 7.476 1.00 15.02 C ANISOU 1566 CG HIS A 73 1834 2091 1782 130 127 103 C ATOM 1567 ND1 HIS A 73 -0.577 -5.453 7.188 1.00 17.72 N ANISOU 1567 ND1 HIS A 73 2184 2736 1810 344 -95 140 N ATOM 1568 CD2 HIS A 73 0.735 -6.949 6.279 1.00 18.76 C ANISOU 1568 CD2 HIS A 73 2417 2460 2248 327 38 31 C ATOM 1569 CE1 HIS A 73 -0.695 -5.332 5.871 1.00 20.81 C ANISOU 1569 CE1 HIS A 73 2561 2950 2393 428 200 105 C ATOM 1570 NE2 HIS A 73 0.092 -6.227 5.297 1.00 20.93 N ANISOU 1570 NE2 HIS A 73 2584 3020 2349 395 172 86 N ATOM 1571 N GLY A 74 3.007 -6.134 11.598 1.00 11.61 N ANISOU 1571 N GLY A 74 1490 1417 1503 31 46 16 N ATOM 1572 CA GLY A 74 3.326 -6.471 12.973 1.00 11.91 C ANISOU 1572 CA GLY A 74 1502 1497 1523 11 -11 -43 C ATOM 1573 C GLY A 74 4.086 -7.772 13.170 1.00 11.76 C ANISOU 1573 C GLY A 74 1497 1473 1496 26 2 -33 C ATOM 1574 O GLY A 74 4.544 -8.016 14.267 1.00 11.56 O ANISOU 1574 O GLY A 74 1573 1533 1284 40 3 -151 O ATOM 1575 N ILE A 75 4.226 -8.586 12.119 1.00 11.79 N ANISOU 1575 N ILE A 75 1516 1475 1487 -30 -49 -72 N ATOM 1576 CA ILE A 75 4.874 -9.914 12.183 1.00 11.98 C ANISOU 1576 CA ILE A 75 1630 1440 1480 -1 -14 -17 C ATOM 1577 C ILE A 75 6.249 -9.893 11.514 1.00 12.23 C ANISOU 1577 C ILE A 75 1654 1434 1557 -26 -47 -51 C ATOM 1578 O ILE A 75 6.392 -9.372 10.417 1.00 12.18 O ANISOU 1578 O ILE A 75 1940 1337 1350 -83 -5 -64 O ATOM 1579 CB ILE A 75 3.967 -10.956 11.458 1.00 12.03 C ANISOU 1579 CB ILE A 75 1560 1407 1604 -11 23 24 C ATOM 1580 CG1 ILE A 75 2.535 -10.925 12.009 1.00 12.78 C ANISOU 1580 CG1 ILE A 75 1838 1414 1601 59 102 -11 C ATOM 1581 CG2 ILE A 75 4.563 -12.351 11.525 1.00 12.45 C ANISOU 1581 CG2 ILE A 75 1657 1437 1634 72 127 17 C ATOM 1582 CD1 ILE A 75 2.448 -11.099 13.473 1.00 13.87 C ANISOU 1582 CD1 ILE A 75 1869 1638 1763 164 58 -17 C ATOM 1583 N ILE A 76 7.270 -10.453 12.157 1.00 12.93 N ANISOU 1583 N ILE A 76 1737 1512 1663 -14 -27 -32 N ATOM 1584 CA ILE A 76 8.601 -10.548 11.520 1.00 13.17 C ANISOU 1584 CA ILE A 76 1686 1624 1691 2 15 -7 C ATOM 1585 C ILE A 76 8.530 -11.551 10.345 1.00 13.28 C ANISOU 1585 C ILE A 76 1693 1639 1711 51 20 -7 C ATOM 1586 O ILE A 76 8.100 -12.692 10.531 1.00 13.60 O ANISOU 1586 O ILE A 76 1790 1640 1736 105 62 -58 O ATOM 1587 CB ILE A 76 9.679 -10.987 12.560 1.00 13.24 C ANISOU 1587 CB ILE A 76 1673 1670 1688 -34 11 -61 C ATOM 1588 CG1 ILE A 76 9.767 -9.966 13.700 1.00 15.22 C ANISOU 1588 CG1 ILE A 76 1916 1880 1984 -64 -61 83 C ATOM 1589 CG2 ILE A 76 11.045 -11.176 11.897 1.00 13.16 C ANISOU 1589 CG2 ILE A 76 1711 1662 1624 -22 -105 46 C ATOM 1590 CD1 ILE A 76 10.447 -10.505 14.936 1.00 17.91 C ANISOU 1590 CD1 ILE A 76 2153 2292 2359 -49 -28 -44 C ATOM 1591 N THR A 77 8.887 -11.109 9.138 1.00 13.37 N ANISOU 1591 N THR A 77 1683 1644 1751 101 48 6 N ATOM 1592 CA THR A 77 8.914 -11.981 7.959 1.00 14.35 C ANISOU 1592 CA THR A 77 1782 1838 1832 46 12 7 C ATOM 1593 C THR A 77 10.294 -12.110 7.289 1.00 14.33 C ANISOU 1593 C THR A 77 1771 1854 1819 19 39 -28 C ATOM 1594 O THR A 77 10.450 -12.882 6.361 1.00 16.39 O ANISOU 1594 O THR A 77 1925 2092 2209 58 62 -25 O ATOM 1595 CB THR A 77 7.872 -11.564 6.898 1.00 14.57 C ANISOU 1595 CB THR A 77 1782 1875 1876 48 31 9 C ATOM 1596 OG1 THR A 77 8.109 -10.226 6.452 1.00 14.29 O ANISOU 1596 OG1 THR A 77 1804 1840 1784 128 -5 8 O ATOM 1597 CG2 THR A 77 6.447 -11.547 7.471 1.00 16.03 C ANISOU 1597 CG2 THR A 77 2021 2116 1952 121 41 -13 C ATOM 1598 N ASN A 78 11.290 -11.376 7.745 1.00 14.18 N ANISOU 1598 N ASN A 78 1753 1793 1841 6 50 0 N ATOM 1599 CA ASN A 78 12.645 -11.523 7.203 1.00 13.86 C ANISOU 1599 CA ASN A 78 1743 1761 1762 -2 10 -6 C ATOM 1600 C ASN A 78 13.588 -11.570 8.399 1.00 13.68 C ANISOU 1600 C ASN A 78 1710 1767 1721 -4 13 -7 C ATOM 1601 O ASN A 78 13.954 -10.528 8.955 1.00 12.29 O ANISOU 1601 O ASN A 78 1629 1546 1492 -41 51 -160 O ATOM 1602 CB ASN A 78 12.991 -10.382 6.237 1.00 13.67 C ANISOU 1602 CB ASN A 78 1703 1756 1734 7 25 17 C ATOM 1603 CG ASN A 78 14.352 -10.570 5.545 1.00 14.51 C ANISOU 1603 CG ASN A 78 1709 1955 1847 -8 17 170 C ATOM 1604 OD1 ASN A 78 15.289 -11.138 6.115 1.00 13.20 O ANISOU 1604 OD1 ASN A 78 1383 1892 1740 50 2 466 O ATOM 1605 ND2 ASN A 78 14.458 -10.082 4.310 1.00 13.83 N ANISOU 1605 ND2 ASN A 78 1491 2037 1723 -73 -134 130 N ATOM 1606 N TRP A 79 13.947 -12.792 8.796 1.00 13.32 N ANISOU 1606 N TRP A 79 1677 1710 1674 1 13 -18 N ATOM 1607 CA TRP A 79 14.753 -13.014 9.991 1.00 13.79 C ANISOU 1607 CA TRP A 79 1713 1776 1751 -1 11 3 C ATOM 1608 C TRP A 79 16.199 -12.536 9.847 1.00 13.87 C ANISOU 1608 C TRP A 79 1717 1755 1796 -21 -17 23 C ATOM 1609 O TRP A 79 16.743 -12.038 10.806 1.00 13.18 O ANISOU 1609 O TRP A 79 1575 1705 1728 -122 -21 29 O ATOM 1610 CB TRP A 79 14.668 -14.473 10.452 1.00 13.84 C ANISOU 1610 CB TRP A 79 1716 1812 1729 -27 -13 50 C ATOM 1611 CG TRP A 79 13.294 -14.767 10.921 1.00 13.77 C ANISOU 1611 CG TRP A 79 1587 1968 1675 -2 0 84 C ATOM 1612 CD1 TRP A 79 12.292 -15.365 10.207 1.00 14.31 C ANISOU 1612 CD1 TRP A 79 1653 1880 1905 -167 46 233 C ATOM 1613 CD2 TRP A 79 12.727 -14.414 12.190 1.00 15.79 C ANISOU 1613 CD2 TRP A 79 1912 2050 2036 -131 -76 190 C ATOM 1614 NE1 TRP A 79 11.146 -15.414 10.965 1.00 14.14 N ANISOU 1614 NE1 TRP A 79 1544 1931 1894 -270 20 234 N ATOM 1615 CE2 TRP A 79 11.381 -14.828 12.180 1.00 14.23 C ANISOU 1615 CE2 TRP A 79 1645 1952 1809 -236 130 290 C ATOM 1616 CE3 TRP A 79 13.223 -13.794 13.343 1.00 14.77 C ANISOU 1616 CE3 TRP A 79 1926 1917 1768 29 -59 151 C ATOM 1617 CZ2 TRP A 79 10.531 -14.651 13.282 1.00 16.37 C ANISOU 1617 CZ2 TRP A 79 2133 1835 2252 51 -187 89 C ATOM 1618 CZ3 TRP A 79 12.388 -13.621 14.417 1.00 15.22 C ANISOU 1618 CZ3 TRP A 79 1967 1983 1830 58 -89 94 C ATOM 1619 CH2 TRP A 79 11.055 -14.050 14.385 1.00 15.69 C ANISOU 1619 CH2 TRP A 79 2237 1806 1916 -20 -48 4 C ATOM 1620 N ASP A 80 16.787 -12.643 8.653 1.00 14.11 N ANISOU 1620 N ASP A 80 1754 1727 1878 -5 20 1 N ATOM 1621 CA ASP A 80 18.142 -12.159 8.440 1.00 15.50 C ANISOU 1621 CA ASP A 80 1896 1992 1999 49 -13 -29 C ATOM 1622 C ASP A 80 18.260 -10.636 8.552 1.00 15.32 C ANISOU 1622 C ASP A 80 1874 1943 2004 47 -36 -4 C ATOM 1623 O ASP A 80 19.215 -10.115 9.172 1.00 16.53 O ANISOU 1623 O ASP A 80 1987 2160 2131 220 -92 -49 O ATOM 1624 CB ASP A 80 18.696 -12.655 7.103 1.00 15.80 C ANISOU 1624 CB ASP A 80 1930 2031 2039 37 -29 -24 C ATOM 1625 CG ASP A 80 18.982 -14.150 7.123 1.00 18.53 C ANISOU 1625 CG ASP A 80 2214 2568 2258 45 76 -80 C ATOM 1626 OD1 ASP A 80 19.025 -14.765 8.221 1.00 21.58 O ANISOU 1626 OD1 ASP A 80 2263 3095 2840 47 285 202 O ATOM 1627 OD2 ASP A 80 19.174 -14.804 6.093 1.00 23.52 O ANISOU 1627 OD2 ASP A 80 3007 3304 2623 -16 273 -273 O ATOM 1628 N ASP A 81 17.300 -9.912 7.984 1.00 14.47 N ANISOU 1628 N ASP A 81 1756 1863 1879 48 -40 5 N ATOM 1629 CA ASP A 81 17.289 -8.462 8.132 1.00 14.00 C ANISOU 1629 CA ASP A 81 1704 1807 1806 21 -37 22 C ATOM 1630 C ASP A 81 16.872 -8.058 9.553 1.00 13.16 C ANISOU 1630 C ASP A 81 1616 1716 1667 7 -48 39 C ATOM 1631 O ASP A 81 17.313 -7.034 10.059 1.00 12.47 O ANISOU 1631 O ASP A 81 1422 1698 1618 68 -74 99 O ATOM 1632 CB ASP A 81 16.369 -7.809 7.093 1.00 14.09 C ANISOU 1632 CB ASP A 81 1737 1822 1793 10 10 37 C ATOM 1633 CG ASP A 81 17.009 -7.725 5.713 1.00 15.01 C ANISOU 1633 CG ASP A 81 1802 2018 1882 98 12 -3 C ATOM 1634 OD1 ASP A 81 18.070 -8.342 5.498 1.00 15.96 O ANISOU 1634 OD1 ASP A 81 1647 2365 2050 94 280 -17 O ATOM 1635 OD2 ASP A 81 16.518 -7.070 4.781 1.00 16.14 O ANISOU 1635 OD2 ASP A 81 1865 2322 1945 269 3 54 O ATOM 1636 N MET A 82 16.014 -8.843 10.192 1.00 12.94 N ANISOU 1636 N MET A 82 1656 1619 1640 -14 -75 15 N ATOM 1637 CA MET A 82 15.646 -8.567 11.574 1.00 12.82 C ANISOU 1637 CA MET A 82 1618 1624 1629 -20 -2 38 C ATOM 1638 C MET A 82 16.896 -8.647 12.476 1.00 12.91 C ANISOU 1638 C MET A 82 1640 1635 1629 -24 26 93 C ATOM 1639 O MET A 82 17.072 -7.820 13.381 1.00 11.75 O ANISOU 1639 O MET A 82 1450 1557 1454 -88 -124 156 O ATOM 1640 CB MET A 82 14.529 -9.494 12.072 1.00 13.07 C ANISOU 1640 CB MET A 82 1665 1625 1676 13 1 -83 C ATOM 1641 CG MET A 82 13.841 -8.980 13.348 1.00 14.32 C ANISOU 1641 CG MET A 82 1786 1775 1879 15 13 56 C ATOM 1642 SD MET A 82 12.960 -7.423 13.050 1.00 16.51 S ANISOU 1642 SD MET A 82 1924 2083 2266 364 -23 -320 S ATOM 1643 CE MET A 82 13.191 -6.543 14.578 1.00 17.23 C ANISOU 1643 CE MET A 82 2102 2260 2183 186 -28 -108 C ATOM 1644 N GLU A 83 17.781 -9.601 12.200 1.00 13.14 N ANISOU 1644 N GLU A 83 1679 1616 1696 -36 43 80 N ATOM 1645 CA GLU A 83 19.029 -9.687 12.955 1.00 13.98 C ANISOU 1645 CA GLU A 83 1803 1738 1770 -31 -25 -3 C ATOM 1646 C GLU A 83 19.876 -8.421 12.768 1.00 13.04 C ANISOU 1646 C GLU A 83 1708 1581 1661 -66 -2 35 C ATOM 1647 O GLU A 83 20.494 -7.963 13.734 1.00 12.26 O ANISOU 1647 O GLU A 83 1693 1485 1477 -126 -23 52 O ATOM 1648 CB GLU A 83 19.869 -10.915 12.590 1.00 14.52 C ANISOU 1648 CB GLU A 83 1947 1748 1821 -14 20 -21 C ATOM 1649 CG GLU A 83 19.295 -12.219 13.125 1.00 19.00 C ANISOU 1649 CG GLU A 83 2381 2279 2559 15 1 -98 C ATOM 1650 CD GLU A 83 20.168 -13.441 12.830 1.00 24.01 C ANISOU 1650 CD GLU A 83 2842 2610 3669 20 107 -141 C ATOM 1651 OE1 GLU A 83 21.393 -13.281 12.640 1.00 25.94 O ANISOU 1651 OE1 GLU A 83 2543 2928 4382 84 188 -215 O ATOM 1652 OE2 GLU A 83 19.613 -14.571 12.774 1.00 29.52 O ANISOU 1652 OE2 GLU A 83 3827 2828 4560 147 389 -98 O ATOM 1653 N LYS A 84 19.885 -7.859 11.554 1.00 12.18 N ANISOU 1653 N LYS A 84 1597 1532 1496 -29 23 -69 N ATOM 1654 CA LYS A 84 20.605 -6.616 11.291 1.00 12.49 C ANISOU 1654 CA LYS A 84 1640 1567 1539 0 19 -25 C ATOM 1655 C LYS A 84 19.998 -5.450 12.077 1.00 12.18 C ANISOU 1655 C LYS A 84 1622 1513 1492 -35 22 -24 C ATOM 1656 O LYS A 84 20.723 -4.614 12.589 1.00 11.31 O ANISOU 1656 O LYS A 84 1444 1415 1438 -180 -41 -122 O ATOM 1657 CB LYS A 84 20.619 -6.268 9.798 1.00 12.65 C ANISOU 1657 CB LYS A 84 1665 1624 1516 52 10 -43 C ATOM 1658 CG LYS A 84 21.530 -7.149 8.960 1.00 14.88 C ANISOU 1658 CG LYS A 84 1922 1927 1803 -37 -29 -15 C ATOM 1659 CD LYS A 84 21.477 -6.724 7.492 1.00 17.06 C ANISOU 1659 CD LYS A 84 2157 2253 2069 55 -10 16 C ATOM 1660 CE LYS A 84 22.658 -7.226 6.690 1.00 18.77 C ANISOU 1660 CE LYS A 84 2481 2322 2328 66 -8 -23 C ATOM 1661 NZ LYS A 84 22.837 -8.698 6.810 1.00 19.56 N ANISOU 1661 NZ LYS A 84 2912 2179 2339 14 -159 -258 N ATOM 1662 N ILE A 85 18.677 -5.400 12.158 1.00 11.48 N ANISOU 1662 N ILE A 85 1477 1439 1445 -29 17 -7 N ATOM 1663 CA ILE A 85 17.996 -4.355 12.919 1.00 12.27 C ANISOU 1663 CA ILE A 85 1618 1524 1520 -34 14 22 C ATOM 1664 C ILE A 85 18.375 -4.435 14.399 1.00 11.73 C ANISOU 1664 C ILE A 85 1508 1494 1452 -28 10 26 C ATOM 1665 O ILE A 85 18.659 -3.403 15.039 1.00 12.04 O ANISOU 1665 O ILE A 85 1740 1440 1393 -3 101 23 O ATOM 1666 CB ILE A 85 16.481 -4.471 12.788 1.00 11.98 C ANISOU 1666 CB ILE A 85 1557 1552 1442 20 -14 -25 C ATOM 1667 CG1 ILE A 85 16.043 -4.198 11.346 1.00 14.99 C ANISOU 1667 CG1 ILE A 85 1973 1705 2017 30 38 24 C ATOM 1668 CG2 ILE A 85 15.781 -3.503 13.788 1.00 14.79 C ANISOU 1668 CG2 ILE A 85 1802 1893 1924 4 -7 100 C ATOM 1669 CD1 ILE A 85 15.792 -2.778 11.056 1.00 18.21 C ANISOU 1669 CD1 ILE A 85 2334 2267 2316 -37 10 111 C ATOM 1670 N TRP A 86 18.371 -5.652 14.943 1.00 11.31 N ANISOU 1670 N TRP A 86 1426 1445 1423 -5 1 42 N ATOM 1671 CA TRP A 86 18.690 -5.829 16.357 1.00 11.20 C ANISOU 1671 CA TRP A 86 1376 1449 1427 -5 5 32 C ATOM 1672 C TRP A 86 20.159 -5.494 16.608 1.00 11.49 C ANISOU 1672 C TRP A 86 1429 1465 1469 9 9 76 C ATOM 1673 O TRP A 86 20.493 -4.887 17.628 1.00 11.31 O ANISOU 1673 O TRP A 86 1367 1473 1457 -23 13 31 O ATOM 1674 CB TRP A 86 18.343 -7.247 16.839 1.00 10.68 C ANISOU 1674 CB TRP A 86 1275 1378 1402 13 30 28 C ATOM 1675 CG TRP A 86 16.873 -7.449 17.133 1.00 11.73 C ANISOU 1675 CG TRP A 86 1524 1380 1553 -146 21 -35 C ATOM 1676 CD1 TRP A 86 16.003 -6.537 17.647 1.00 13.41 C ANISOU 1676 CD1 TRP A 86 1586 1568 1939 -270 86 -4 C ATOM 1677 CD2 TRP A 86 16.110 -8.640 16.906 1.00 13.70 C ANISOU 1677 CD2 TRP A 86 1716 1744 1744 -148 17 -36 C ATOM 1678 NE1 TRP A 86 14.748 -7.086 17.763 1.00 13.80 N ANISOU 1678 NE1 TRP A 86 1827 1631 1785 -158 -37 35 N ATOM 1679 CE2 TRP A 86 14.786 -8.379 17.315 1.00 14.91 C ANISOU 1679 CE2 TRP A 86 1866 1898 1902 -334 -38 -87 C ATOM 1680 CE3 TRP A 86 16.414 -9.906 16.391 1.00 15.36 C ANISOU 1680 CE3 TRP A 86 1908 1845 2083 -168 -189 137 C ATOM 1681 CZ2 TRP A 86 13.765 -9.343 17.241 1.00 15.12 C ANISOU 1681 CZ2 TRP A 86 1946 1940 1856 -317 51 -47 C ATOM 1682 CZ3 TRP A 86 15.408 -10.857 16.320 1.00 15.21 C ANISOU 1682 CZ3 TRP A 86 1902 1889 1985 -267 -242 66 C ATOM 1683 CH2 TRP A 86 14.093 -10.559 16.736 1.00 14.65 C ANISOU 1683 CH2 TRP A 86 1852 1635 2078 -293 58 -38 C ATOM 1684 N HIS A 87 21.039 -5.869 15.684 1.00 11.77 N ANISOU 1684 N HIS A 87 1461 1546 1462 43 15 55 N ATOM 1685 CA HIS A 87 22.476 -5.547 15.843 1.00 12.31 C ANISOU 1685 CA HIS A 87 1493 1651 1530 31 -2 8 C ATOM 1686 C HIS A 87 22.682 -4.043 15.899 1.00 12.64 C ANISOU 1686 C HIS A 87 1530 1726 1547 20 -31 17 C ATOM 1687 O HIS A 87 23.425 -3.520 16.717 1.00 12.89 O ANISOU 1687 O HIS A 87 1515 1880 1503 109 -69 17 O ATOM 1688 CB HIS A 87 23.289 -6.154 14.696 1.00 12.62 C ANISOU 1688 CB HIS A 87 1524 1689 1580 41 -48 34 C ATOM 1689 CG HIS A 87 24.760 -5.905 14.792 1.00 13.36 C ANISOU 1689 CG HIS A 87 1535 1799 1739 43 34 -204 C ATOM 1690 ND1 HIS A 87 25.659 -6.898 15.107 1.00 15.90 N ANISOU 1690 ND1 HIS A 87 1685 2250 2104 26 -352 -124 N ATOM 1691 CD2 HIS A 87 25.491 -4.781 14.611 1.00 16.34 C ANISOU 1691 CD2 HIS A 87 1940 2105 2161 74 -71 -181 C ATOM 1692 CE1 HIS A 87 26.885 -6.398 15.103 1.00 17.34 C ANISOU 1692 CE1 HIS A 87 1915 2259 2413 -65 -222 -75 C ATOM 1693 NE2 HIS A 87 26.811 -5.114 14.810 1.00 16.12 N ANISOU 1693 NE2 HIS A 87 1536 2064 2525 132 -286 -158 N ATOM 1694 N HIS A 88 22.009 -3.344 15.003 1.00 13.49 N ANISOU 1694 N HIS A 88 1668 1753 1705 14 -32 -13 N ATOM 1695 CA HIS A 88 22.051 -1.899 14.943 1.00 13.66 C ANISOU 1695 CA HIS A 88 1721 1726 1741 -61 -15 -9 C ATOM 1696 C HIS A 88 21.503 -1.270 16.224 1.00 13.65 C ANISOU 1696 C HIS A 88 1747 1685 1754 -55 -35 -32 C ATOM 1697 O HIS A 88 22.039 -0.293 16.700 1.00 13.50 O ANISOU 1697 O HIS A 88 1743 1635 1749 -98 -137 -94 O ATOM 1698 CB HIS A 88 21.224 -1.445 13.755 1.00 13.94 C ANISOU 1698 CB HIS A 88 1797 1750 1748 -82 -25 50 C ATOM 1699 CG HIS A 88 21.293 0.019 13.494 1.00 15.50 C ANISOU 1699 CG HIS A 88 2124 1954 1811 -71 33 -54 C ATOM 1700 ND1 HIS A 88 22.309 0.589 12.762 1.00 17.67 N ANISOU 1700 ND1 HIS A 88 2450 2183 2080 -191 248 156 N ATOM 1701 CD2 HIS A 88 20.485 1.031 13.874 1.00 16.59 C ANISOU 1701 CD2 HIS A 88 2125 2096 2080 20 41 197 C ATOM 1702 CE1 HIS A 88 22.115 1.893 12.690 1.00 17.53 C ANISOU 1702 CE1 HIS A 88 2425 2080 2155 78 211 -21 C ATOM 1703 NE2 HIS A 88 21.015 2.186 13.358 1.00 18.09 N ANISOU 1703 NE2 HIS A 88 2434 2167 2270 -65 261 195 N ATOM 1704 N THR A 89 20.436 -1.839 16.775 1.00 13.49 N ANISOU 1704 N THR A 89 1729 1670 1723 -26 -2 -27 N ATOM 1705 CA THR A 89 19.849 -1.350 18.009 1.00 13.77 C ANISOU 1705 CA THR A 89 1746 1713 1771 -17 6 -24 C ATOM 1706 C THR A 89 20.849 -1.444 19.149 1.00 14.12 C ANISOU 1706 C THR A 89 1766 1786 1813 -59 38 -57 C ATOM 1707 O THR A 89 21.021 -0.486 19.883 1.00 13.93 O ANISOU 1707 O THR A 89 1696 1653 1943 -286 133 -158 O ATOM 1708 CB THR A 89 18.577 -2.135 18.360 1.00 13.69 C ANISOU 1708 CB THR A 89 1692 1797 1712 14 -7 -36 C ATOM 1709 OG1 THR A 89 17.617 -1.988 17.315 1.00 14.15 O ANISOU 1709 OG1 THR A 89 1557 2000 1817 72 195 -144 O ATOM 1710 CG2 THR A 89 17.876 -1.545 19.551 1.00 14.16 C ANISOU 1710 CG2 THR A 89 1750 1842 1787 130 -68 -91 C ATOM 1711 N PHE A 90 21.486 -2.603 19.304 1.00 14.38 N ANISOU 1711 N PHE A 90 1814 1841 1807 -5 33 -34 N ATOM 1712 CA PHE A 90 22.412 -2.831 20.412 1.00 14.48 C ANISOU 1712 CA PHE A 90 1800 1879 1821 -29 20 -52 C ATOM 1713 C PHE A 90 23.686 -2.034 20.264 1.00 14.95 C ANISOU 1713 C PHE A 90 1854 1949 1874 7 0 -72 C ATOM 1714 O PHE A 90 24.125 -1.375 21.204 1.00 13.79 O ANISOU 1714 O PHE A 90 1662 1908 1669 -36 45 -242 O ATOM 1715 CB PHE A 90 22.825 -4.302 20.483 1.00 14.87 C ANISOU 1715 CB PHE A 90 1891 1920 1837 1 -42 -54 C ATOM 1716 CG PHE A 90 21.733 -5.247 20.920 1.00 15.27 C ANISOU 1716 CG PHE A 90 1954 1954 1891 -50 182 -91 C ATOM 1717 CD1 PHE A 90 21.569 -6.470 20.266 1.00 15.76 C ANISOU 1717 CD1 PHE A 90 1926 2107 1952 86 216 -36 C ATOM 1718 CD2 PHE A 90 20.921 -4.961 22.008 1.00 17.54 C ANISOU 1718 CD2 PHE A 90 2214 2115 2333 -66 178 -246 C ATOM 1719 CE1 PHE A 90 20.605 -7.372 20.652 1.00 14.87 C ANISOU 1719 CE1 PHE A 90 1745 1912 1991 -21 270 -116 C ATOM 1720 CE2 PHE A 90 19.953 -5.863 22.423 1.00 18.08 C ANISOU 1720 CE2 PHE A 90 2346 2132 2390 -56 355 -251 C ATOM 1721 CZ PHE A 90 19.784 -7.072 21.742 1.00 19.32 C ANISOU 1721 CZ PHE A 90 2498 2380 2460 -123 217 -209 C ATOM 1722 N TYR A 91 24.301 -2.118 19.094 1.00 15.01 N ANISOU 1722 N TYR A 91 1953 1955 1793 21 -23 -100 N ATOM 1723 CA TYR A 91 25.661 -1.623 18.921 1.00 15.89 C ANISOU 1723 CA TYR A 91 2071 1989 1976 -18 -22 -46 C ATOM 1724 C TYR A 91 25.672 -0.166 18.509 1.00 16.98 C ANISOU 1724 C TYR A 91 2209 2132 2111 -48 -59 -45 C ATOM 1725 O TYR A 91 26.533 0.603 18.947 1.00 18.19 O ANISOU 1725 O TYR A 91 2490 2176 2243 -160 -268 -28 O ATOM 1726 CB TYR A 91 26.430 -2.492 17.912 1.00 16.32 C ANISOU 1726 CB TYR A 91 2111 2073 2015 -25 -66 -26 C ATOM 1727 CG TYR A 91 26.825 -3.821 18.518 1.00 16.67 C ANISOU 1727 CG TYR A 91 2148 1983 2203 24 -80 -131 C ATOM 1728 CD1 TYR A 91 26.061 -4.959 18.310 1.00 16.89 C ANISOU 1728 CD1 TYR A 91 1950 2197 2269 30 86 -57 C ATOM 1729 CD2 TYR A 91 27.936 -3.923 19.354 1.00 17.71 C ANISOU 1729 CD2 TYR A 91 2248 2137 2342 -28 -113 -162 C ATOM 1730 CE1 TYR A 91 26.408 -6.166 18.889 1.00 16.89 C ANISOU 1730 CE1 TYR A 91 2157 2074 2186 -45 13 100 C ATOM 1731 CE2 TYR A 91 28.293 -5.126 19.936 1.00 17.12 C ANISOU 1731 CE2 TYR A 91 2267 2048 2190 -63 -111 8 C ATOM 1732 CZ TYR A 91 27.522 -6.242 19.698 1.00 17.45 C ANISOU 1732 CZ TYR A 91 2208 2176 2245 -72 24 104 C ATOM 1733 OH TYR A 91 27.867 -7.438 20.265 1.00 17.63 O ANISOU 1733 OH TYR A 91 2255 2380 2062 -46 336 132 O ATOM 1734 N ASN A 92 24.730 0.224 17.669 1.00 16.70 N ANISOU 1734 N ASN A 92 2149 2097 2096 -31 -68 -19 N ATOM 1735 CA ASN A 92 24.752 1.574 17.118 1.00 17.86 C ANISOU 1735 CA ASN A 92 2274 2283 2226 -25 -31 -39 C ATOM 1736 C ASN A 92 23.916 2.610 17.859 1.00 16.89 C ANISOU 1736 C ASN A 92 2137 2171 2109 18 -55 -2 C ATOM 1737 O ASN A 92 24.349 3.754 18.009 1.00 15.89 O ANISOU 1737 O ASN A 92 1979 2060 1998 -119 -110 -20 O ATOM 1738 CB ASN A 92 24.422 1.532 15.622 1.00 18.55 C ANISOU 1738 CB ASN A 92 2379 2364 2304 -9 -29 -23 C ATOM 1739 CG ASN A 92 25.516 0.833 14.826 1.00 20.36 C ANISOU 1739 CG ASN A 92 2389 2646 2699 38 24 -238 C ATOM 1740 OD1 ASN A 92 25.266 -0.122 14.112 1.00 26.31 O ANISOU 1740 OD1 ASN A 92 3086 3297 3612 241 171 -413 O ATOM 1741 ND2 ASN A 92 26.744 1.304 14.979 1.00 26.14 N ANISOU 1741 ND2 ASN A 92 3132 3433 3365 310 45 -142 N ATOM 1742 N GLU A 93 22.747 2.210 18.341 1.00 16.31 N ANISOU 1742 N GLU A 93 2092 2087 2017 -55 -17 13 N ATOM 1743 CA GLU A 93 21.817 3.135 18.984 1.00 16.25 C ANISOU 1743 CA GLU A 93 2080 2053 2039 48 -14 -29 C ATOM 1744 C GLU A 93 21.960 3.131 20.505 1.00 15.82 C ANISOU 1744 C GLU A 93 2002 2031 1976 48 -27 -51 C ATOM 1745 O GLU A 93 22.147 4.188 21.115 1.00 16.10 O ANISOU 1745 O GLU A 93 2135 2010 1970 228 -43 -132 O ATOM 1746 CB GLU A 93 20.377 2.768 18.642 1.00 16.67 C ANISOU 1746 CB GLU A 93 2134 2111 2086 13 6 -18 C ATOM 1747 CG GLU A 93 19.973 3.001 17.202 1.00 19.11 C ANISOU 1747 CG GLU A 93 2486 2353 2420 52 103 -50 C ATOM 1748 CD GLU A 93 20.165 4.430 16.741 1.00 22.32 C ANISOU 1748 CD GLU A 93 3111 2711 2658 88 184 48 C ATOM 1749 OE1 GLU A 93 20.102 5.371 17.569 1.00 24.71 O ANISOU 1749 OE1 GLU A 93 3455 2863 3070 191 188 -5 O ATOM 1750 OE2 GLU A 93 20.393 4.606 15.536 1.00 27.93 O ANISOU 1750 OE2 GLU A 93 4237 3093 3281 81 -57 93 O ATOM 1751 N LEU A 94 21.873 1.952 21.116 1.00 14.64 N ANISOU 1751 N LEU A 94 1823 1900 1835 37 -46 -68 N ATOM 1752 CA LEU A 94 21.972 1.842 22.573 1.00 14.74 C ANISOU 1752 CA LEU A 94 1820 1929 1849 34 0 -50 C ATOM 1753 C LEU A 94 23.436 1.770 23.031 1.00 14.68 C ANISOU 1753 C LEU A 94 1814 1995 1768 24 -15 -70 C ATOM 1754 O LEU A 94 23.752 2.060 24.192 1.00 14.44 O ANISOU 1754 O LEU A 94 1835 1992 1657 4 135 -234 O ATOM 1755 CB LEU A 94 21.211 0.625 23.064 1.00 14.65 C ANISOU 1755 CB LEU A 94 1815 1902 1848 79 22 -96 C ATOM 1756 CG LEU A 94 19.699 0.664 22.844 1.00 15.22 C ANISOU 1756 CG LEU A 94 1913 1939 1931 31 -106 -123 C ATOM 1757 CD1 LEU A 94 19.087 -0.567 23.432 1.00 15.92 C ANISOU 1757 CD1 LEU A 94 2033 2326 1690 125 -66 33 C ATOM 1758 CD2 LEU A 94 19.081 1.906 23.466 1.00 16.61 C ANISOU 1758 CD2 LEU A 94 1970 2231 2108 148 -22 -94 C ATOM 1759 N ARG A 95 24.322 1.386 22.114 1.00 13.77 N ANISOU 1759 N ARG A 95 1684 1884 1662 39 -7 -113 N ATOM 1760 CA ARG A 95 25.750 1.316 22.383 1.00 14.00 C ANISOU 1760 CA ARG A 95 1723 1847 1747 -9 -8 -61 C ATOM 1761 C ARG A 95 26.060 0.508 23.649 1.00 13.64 C ANISOU 1761 C ARG A 95 1622 1830 1730 -3 9 -56 C ATOM 1762 O ARG A 95 26.734 0.978 24.564 1.00 12.62 O ANISOU 1762 O ARG A 95 1432 1756 1607 -149 13 -168 O ATOM 1763 CB ARG A 95 26.352 2.731 22.412 1.00 14.14 C ANISOU 1763 CB ARG A 95 1694 1903 1773 -51 -56 -26 C ATOM 1764 CG ARG A 95 26.233 3.464 21.051 1.00 16.16 C ANISOU 1764 CG ARG A 95 1923 2013 2205 -121 -153 -19 C ATOM 1765 CD ARG A 95 26.758 4.890 21.044 1.00 20.65 C ANISOU 1765 CD ARG A 95 2426 2677 2740 -8 -158 110 C ATOM 1766 NE ARG A 95 28.159 4.909 21.451 1.00 22.80 N ANISOU 1766 NE ARG A 95 2713 2859 3091 -221 -95 98 N ATOM 1767 CZ ARG A 95 28.718 5.846 22.199 1.00 25.12 C ANISOU 1767 CZ ARG A 95 3067 3199 3276 -48 -38 33 C ATOM 1768 NH1 ARG A 95 28.035 6.909 22.615 1.00 26.49 N ANISOU 1768 NH1 ARG A 95 3036 3436 3591 24 12 15 N ATOM 1769 NH2 ARG A 95 29.993 5.725 22.519 1.00 26.03 N ANISOU 1769 NH2 ARG A 95 3024 3441 3425 -76 -48 112 N ATOM 1770 N VAL A 96 25.585 -0.732 23.661 1.00 13.22 N ANISOU 1770 N VAL A 96 1480 1818 1724 -109 -22 -45 N ATOM 1771 CA VAL A 96 25.830 -1.676 24.742 1.00 14.28 C ANISOU 1771 CA VAL A 96 1690 1898 1837 -74 18 21 C ATOM 1772 C VAL A 96 26.455 -2.949 24.201 1.00 15.02 C ANISOU 1772 C VAL A 96 1795 2010 1901 -65 2 33 C ATOM 1773 O VAL A 96 26.460 -3.209 22.996 1.00 15.83 O ANISOU 1773 O VAL A 96 2002 2047 1965 -79 -20 74 O ATOM 1774 CB VAL A 96 24.498 -2.130 25.460 1.00 14.14 C ANISOU 1774 CB VAL A 96 1718 1869 1783 -68 3 13 C ATOM 1775 CG1 VAL A 96 23.711 -0.949 26.002 1.00 14.05 C ANISOU 1775 CG1 VAL A 96 1623 1943 1768 -96 20 71 C ATOM 1776 CG2 VAL A 96 23.634 -2.975 24.506 1.00 15.20 C ANISOU 1776 CG2 VAL A 96 1662 2078 2034 -140 114 71 C ATOM 1777 N ALA A 97 26.980 -3.754 25.112 1.00 16.31 N ANISOU 1777 N ALA A 97 2051 2114 2032 -81 39 43 N ATOM 1778 CA ALA A 97 27.348 -5.129 24.831 1.00 16.53 C ANISOU 1778 CA ALA A 97 2078 2094 2106 -36 27 0 C ATOM 1779 C ALA A 97 26.155 -5.996 25.268 1.00 16.88 C ANISOU 1779 C ALA A 97 2075 2169 2169 -66 12 3 C ATOM 1780 O ALA A 97 25.833 -6.043 26.451 1.00 16.31 O ANISOU 1780 O ALA A 97 1966 2165 2065 -124 21 36 O ATOM 1781 CB ALA A 97 28.579 -5.496 25.595 1.00 16.86 C ANISOU 1781 CB ALA A 97 2122 2141 2143 -80 19 12 C ATOM 1782 N PRO A 98 25.474 -6.639 24.323 1.00 17.45 N ANISOU 1782 N PRO A 98 2170 2226 2233 -47 5 2 N ATOM 1783 CA PRO A 98 24.219 -7.360 24.632 1.00 17.81 C ANISOU 1783 CA PRO A 98 2180 2303 2285 -50 13 0 C ATOM 1784 C PRO A 98 24.353 -8.491 25.664 1.00 17.90 C ANISOU 1784 C PRO A 98 2154 2264 2381 -32 -7 11 C ATOM 1785 O PRO A 98 23.437 -8.750 26.435 1.00 17.64 O ANISOU 1785 O PRO A 98 2101 2248 2353 -105 -68 53 O ATOM 1786 CB PRO A 98 23.778 -7.914 23.277 1.00 18.24 C ANISOU 1786 CB PRO A 98 2262 2305 2361 -67 -7 -8 C ATOM 1787 CG PRO A 98 24.552 -7.158 22.255 1.00 17.62 C ANISOU 1787 CG PRO A 98 2149 2324 2218 -48 -8 38 C ATOM 1788 CD PRO A 98 25.818 -6.700 22.893 1.00 17.67 C ANISOU 1788 CD PRO A 98 2211 2255 2247 -42 13 -30 C ATOM 1789 N GLU A 99 25.514 -9.130 25.702 1.00 18.44 N ANISOU 1789 N GLU A 99 2244 2309 2453 -47 11 -15 N ATOM 1790 CA GLU A 99 25.810 -10.155 26.694 1.00 18.45 C ANISOU 1790 CA GLU A 99 2212 2361 2434 2 9 20 C ATOM 1791 C GLU A 99 25.673 -9.677 28.160 1.00 18.14 C ANISOU 1791 C GLU A 99 2119 2307 2466 19 51 21 C ATOM 1792 O GLU A 99 25.578 -10.488 29.065 1.00 16.94 O ANISOU 1792 O GLU A 99 1870 2178 2389 64 108 57 O ATOM 1793 CB GLU A 99 27.222 -10.740 26.426 1.00 19.60 C ANISOU 1793 CB GLU A 99 2359 2478 2609 -40 63 52 C ATOM 1794 CG GLU A 99 28.353 -9.708 26.440 1.00 21.85 C ANISOU 1794 CG GLU A 99 2475 2909 2917 -105 19 35 C ATOM 1795 CD GLU A 99 28.754 -9.176 25.047 1.00 25.87 C ANISOU 1795 CD GLU A 99 2761 3659 3409 -211 85 -63 C ATOM 1796 OE1 GLU A 99 27.904 -9.093 24.133 1.00 23.95 O ANISOU 1796 OE1 GLU A 99 2181 3560 3357 -214 -145 -174 O ATOM 1797 OE2 GLU A 99 29.951 -8.806 24.866 1.00 31.02 O ANISOU 1797 OE2 GLU A 99 3415 4269 4099 -343 391 4 O ATOM 1798 N GLU A 100 25.635 -8.366 28.392 1.00 18.06 N ANISOU 1798 N GLU A 100 2156 2310 2395 -16 41 -12 N ATOM 1799 CA GLU A 100 25.577 -7.813 29.748 1.00 18.77 C ANISOU 1799 CA GLU A 100 2329 2347 2454 -5 12 22 C ATOM 1800 C GLU A 100 24.169 -7.456 30.211 1.00 17.51 C ANISOU 1800 C GLU A 100 2198 2221 2234 -28 52 13 C ATOM 1801 O GLU A 100 23.994 -7.097 31.362 1.00 17.89 O ANISOU 1801 O GLU A 100 2263 2379 2154 -10 -33 53 O ATOM 1802 CB GLU A 100 26.380 -6.512 29.792 1.00 19.57 C ANISOU 1802 CB GLU A 100 2428 2482 2523 -42 -49 -38 C ATOM 1803 CG GLU A 100 27.321 -6.396 30.946 1.00 24.87 C ANISOU 1803 CG GLU A 100 3251 2928 3269 -49 64 63 C ATOM 1804 CD GLU A 100 28.636 -7.011 30.608 1.00 29.39 C ANISOU 1804 CD GLU A 100 3837 3272 4058 -230 284 -44 C ATOM 1805 OE1 GLU A 100 28.647 -8.256 30.464 1.00 33.64 O ANISOU 1805 OE1 GLU A 100 4717 3302 4761 -564 276 -50 O ATOM 1806 OE2 GLU A 100 29.628 -6.250 30.462 1.00 32.96 O ANISOU 1806 OE2 GLU A 100 4660 3310 4551 -894 264 -28 O ATOM 1807 N HIS A 101 23.187 -7.483 29.318 1.00 15.54 N ANISOU 1807 N HIS A 101 1961 1980 1963 -6 -22 33 N ATOM 1808 CA HIS A 101 21.877 -6.883 29.619 1.00 14.83 C ANISOU 1808 CA HIS A 101 1904 1836 1891 13 13 14 C ATOM 1809 C HIS A 101 20.695 -7.805 29.317 1.00 14.19 C ANISOU 1809 C HIS A 101 1829 1728 1832 17 8 27 C ATOM 1810 O HIS A 101 20.543 -8.263 28.176 1.00 12.79 O ANISOU 1810 O HIS A 101 1854 1334 1670 -20 -33 55 O ATOM 1811 CB HIS A 101 21.679 -5.597 28.808 1.00 15.01 C ANISOU 1811 CB HIS A 101 1866 1890 1944 53 40 -3 C ATOM 1812 CG HIS A 101 22.764 -4.570 28.989 1.00 15.26 C ANISOU 1812 CG HIS A 101 1800 1821 2176 77 0 -78 C ATOM 1813 ND1 HIS A 101 22.609 -3.451 29.778 1.00 14.75 N ANISOU 1813 ND1 HIS A 101 1713 1763 2126 234 296 -176 N ATOM 1814 CD2 HIS A 101 24.011 -4.485 28.465 1.00 15.14 C ANISOU 1814 CD2 HIS A 101 2057 1856 1838 153 327 -72 C ATOM 1815 CE1 HIS A 101 23.719 -2.730 29.747 1.00 15.09 C ANISOU 1815 CE1 HIS A 101 1985 1663 2083 243 172 -60 C ATOM 1816 NE2 HIS A 101 24.588 -3.334 28.956 1.00 13.58 N ANISOU 1816 NE2 HIS A 101 1755 1456 1947 335 178 9 N ATOM 1817 N PRO A 102 19.842 -8.058 30.311 1.00 13.99 N ANISOU 1817 N PRO A 102 1823 1748 1742 -17 5 25 N ATOM 1818 CA PRO A 102 18.540 -8.697 30.055 1.00 13.67 C ANISOU 1818 CA PRO A 102 1750 1737 1706 -26 -22 0 C ATOM 1819 C PRO A 102 17.711 -7.899 29.059 1.00 13.42 C ANISOU 1819 C PRO A 102 1702 1689 1705 -17 3 -28 C ATOM 1820 O PRO A 102 17.704 -6.680 29.159 1.00 13.27 O ANISOU 1820 O PRO A 102 1812 1557 1669 36 -85 -84 O ATOM 1821 CB PRO A 102 17.851 -8.646 31.424 1.00 14.41 C ANISOU 1821 CB PRO A 102 1769 1872 1832 -9 0 -42 C ATOM 1822 CG PRO A 102 18.986 -8.653 32.425 1.00 15.14 C ANISOU 1822 CG PRO A 102 1954 2023 1774 -29 -18 -86 C ATOM 1823 CD PRO A 102 20.040 -7.788 31.752 1.00 14.20 C ANISOU 1823 CD PRO A 102 1799 1781 1813 -128 14 -9 C ATOM 1824 N THR A 103 17.001 -8.548 28.145 1.00 12.23 N ANISOU 1824 N THR A 103 1540 1541 1563 -22 0 -61 N ATOM 1825 CA THR A 103 16.359 -7.808 27.062 1.00 12.37 C ANISOU 1825 CA THR A 103 1580 1477 1642 -5 -6 -75 C ATOM 1826 C THR A 103 14.886 -8.159 26.961 1.00 11.71 C ANISOU 1826 C THR A 103 1464 1370 1615 11 -28 -57 C ATOM 1827 O THR A 103 14.542 -9.327 26.792 1.00 11.68 O ANISOU 1827 O THR A 103 1392 1236 1810 76 -11 -46 O ATOM 1828 CB THR A 103 17.113 -8.096 25.756 1.00 12.55 C ANISOU 1828 CB THR A 103 1586 1520 1661 -9 -1 8 C ATOM 1829 OG1 THR A 103 18.465 -7.605 25.872 1.00 13.43 O ANISOU 1829 OG1 THR A 103 1753 1617 1731 -117 -64 -173 O ATOM 1830 CG2 THR A 103 16.539 -7.332 24.586 1.00 13.82 C ANISOU 1830 CG2 THR A 103 1705 1803 1740 15 -31 -160 C ATOM 1831 N LEU A 104 14.019 -7.150 27.078 1.00 11.57 N ANISOU 1831 N LEU A 104 1541 1347 1506 -57 17 -38 N ATOM 1832 CA LEU A 104 12.586 -7.306 26.907 1.00 11.76 C ANISOU 1832 CA LEU A 104 1488 1419 1560 -13 30 -47 C ATOM 1833 C LEU A 104 12.211 -6.870 25.504 1.00 11.61 C ANISOU 1833 C LEU A 104 1501 1375 1533 -50 18 -63 C ATOM 1834 O LEU A 104 12.515 -5.751 25.080 1.00 10.04 O ANISOU 1834 O LEU A 104 1111 1166 1535 -148 19 -159 O ATOM 1835 CB LEU A 104 11.809 -6.503 27.966 1.00 12.42 C ANISOU 1835 CB LEU A 104 1619 1498 1600 -39 60 -51 C ATOM 1836 CG LEU A 104 10.272 -6.636 28.010 1.00 14.55 C ANISOU 1836 CG LEU A 104 1858 2019 1649 122 37 -82 C ATOM 1837 CD1 LEU A 104 9.721 -6.129 29.346 1.00 19.49 C ANISOU 1837 CD1 LEU A 104 2251 2711 2442 75 -28 -114 C ATOM 1838 CD2 LEU A 104 9.627 -5.840 26.985 1.00 18.57 C ANISOU 1838 CD2 LEU A 104 2315 2466 2272 -65 97 -19 C ATOM 1839 N LEU A 105 11.587 -7.788 24.763 1.00 12.31 N ANISOU 1839 N LEU A 105 1510 1471 1695 -74 27 28 N ATOM 1840 CA LEU A 105 11.091 -7.528 23.422 1.00 12.17 C ANISOU 1840 CA LEU A 105 1549 1491 1581 -56 33 49 C ATOM 1841 C LEU A 105 9.566 -7.557 23.448 1.00 12.38 C ANISOU 1841 C LEU A 105 1572 1520 1610 -3 62 66 C ATOM 1842 O LEU A 105 8.941 -8.078 24.389 1.00 11.70 O ANISOU 1842 O LEU A 105 1493 1302 1649 -101 178 230 O ATOM 1843 CB LEU A 105 11.603 -8.575 22.439 1.00 13.45 C ANISOU 1843 CB LEU A 105 1563 1773 1773 12 49 149 C ATOM 1844 CG LEU A 105 13.123 -8.771 22.361 1.00 16.45 C ANISOU 1844 CG LEU A 105 2075 2059 2115 -31 25 34 C ATOM 1845 CD1 LEU A 105 13.404 -9.985 21.503 1.00 20.16 C ANISOU 1845 CD1 LEU A 105 2498 2479 2680 -7 12 -61 C ATOM 1846 CD2 LEU A 105 13.761 -7.589 21.760 1.00 16.86 C ANISOU 1846 CD2 LEU A 105 1946 2157 2303 -196 -20 12 C ATOM 1847 N THR A 106 8.968 -6.967 22.428 1.00 12.08 N ANISOU 1847 N THR A 106 1542 1514 1533 -67 77 94 N ATOM 1848 CA THR A 106 7.522 -6.972 22.271 1.00 12.76 C ANISOU 1848 CA THR A 106 1610 1627 1609 39 17 26 C ATOM 1849 C THR A 106 7.071 -7.796 21.056 1.00 12.99 C ANISOU 1849 C THR A 106 1657 1660 1617 33 14 4 C ATOM 1850 O THR A 106 7.848 -8.068 20.148 1.00 13.87 O ANISOU 1850 O THR A 106 1895 1701 1673 87 32 -33 O ATOM 1851 CB THR A 106 6.981 -5.556 22.172 1.00 12.89 C ANISOU 1851 CB THR A 106 1616 1590 1691 -90 48 10 C ATOM 1852 OG1 THR A 106 7.290 -4.996 20.884 1.00 11.59 O ANISOU 1852 OG1 THR A 106 1535 1748 1118 15 -115 56 O ATOM 1853 CG2 THR A 106 7.628 -4.644 23.228 1.00 13.05 C ANISOU 1853 CG2 THR A 106 1446 1891 1620 148 8 -3 C ATOM 1854 N GLU A 107 5.809 -8.190 21.061 1.00 13.15 N ANISOU 1854 N GLU A 107 1696 1629 1669 1 0 2 N ATOM 1855 CA GLU A 107 5.235 -8.951 19.955 1.00 13.36 C ANISOU 1855 CA GLU A 107 1748 1704 1623 14 17 -36 C ATOM 1856 C GLU A 107 3.787 -8.547 19.678 1.00 13.24 C ANISOU 1856 C GLU A 107 1746 1651 1633 36 -16 -10 C ATOM 1857 O GLU A 107 3.078 -8.022 20.552 1.00 12.57 O ANISOU 1857 O GLU A 107 1769 1576 1428 55 58 -79 O ATOM 1858 CB GLU A 107 5.295 -10.447 20.257 1.00 13.06 C ANISOU 1858 CB GLU A 107 1669 1701 1591 43 -66 -15 C ATOM 1859 CG GLU A 107 4.279 -10.900 21.278 1.00 15.47 C ANISOU 1859 CG GLU A 107 2194 1966 1717 82 23 33 C ATOM 1860 CD GLU A 107 4.419 -12.353 21.689 1.00 19.06 C ANISOU 1860 CD GLU A 107 2791 2486 1964 234 182 2 C ATOM 1861 OE1 GLU A 107 4.985 -13.158 20.908 1.00 19.91 O ANISOU 1861 OE1 GLU A 107 2996 2764 1802 319 46 108 O ATOM 1862 OE2 GLU A 107 3.937 -12.696 22.811 1.00 21.95 O ANISOU 1862 OE2 GLU A 107 3246 2773 2319 5 566 134 O ATOM 1863 N ALA A 108 3.336 -8.816 18.467 1.00 13.62 N ANISOU 1863 N ALA A 108 1803 1718 1652 13 14 -60 N ATOM 1864 CA ALA A 108 1.934 -8.608 18.120 1.00 14.71 C ANISOU 1864 CA ALA A 108 1958 1853 1779 -40 -30 -16 C ATOM 1865 C ALA A 108 1.033 -9.599 18.860 1.00 15.22 C ANISOU 1865 C ALA A 108 2014 1895 1872 -92 -75 -117 C ATOM 1866 O ALA A 108 1.475 -10.676 19.261 1.00 14.31 O ANISOU 1866 O ALA A 108 1951 1714 1769 -202 -79 -76 O ATOM 1867 CB ALA A 108 1.737 -8.760 16.627 1.00 15.14 C ANISOU 1867 CB ALA A 108 1998 1936 1816 -74 -34 -106 C ATOM 1868 N PRO A 109 -0.213 -9.212 19.068 1.00 15.66 N ANISOU 1868 N PRO A 109 2056 1920 1973 -31 -76 -102 N ATOM 1869 CA PRO A 109 -1.256 -10.148 19.448 1.00 16.88 C ANISOU 1869 CA PRO A 109 2168 2126 2117 16 -46 -85 C ATOM 1870 C PRO A 109 -1.370 -11.220 18.352 1.00 17.17 C ANISOU 1870 C PRO A 109 2243 2129 2149 7 -55 -94 C ATOM 1871 O PRO A 109 -1.301 -10.896 17.151 1.00 18.23 O ANISOU 1871 O PRO A 109 2269 2322 2335 12 -24 -177 O ATOM 1872 CB PRO A 109 -2.523 -9.274 19.486 1.00 16.71 C ANISOU 1872 CB PRO A 109 2209 2020 2118 -16 -58 -118 C ATOM 1873 CG PRO A 109 -2.067 -7.911 19.534 1.00 16.38 C ANISOU 1873 CG PRO A 109 2097 2088 2039 19 -37 -36 C ATOM 1874 CD PRO A 109 -0.723 -7.843 18.947 1.00 16.83 C ANISOU 1874 CD PRO A 109 2216 2115 2061 -44 -104 -116 C ATOM 1875 N LEU A 110 -1.517 -12.466 18.764 1.00 17.73 N ANISOU 1875 N LEU A 110 2302 2202 2232 -6 -34 -21 N ATOM 1876 CA LEU A 110 -1.633 -13.618 17.844 1.00 17.38 C ANISOU 1876 CA LEU A 110 2296 2195 2112 30 -6 -53 C ATOM 1877 C LEU A 110 -0.357 -13.890 17.009 1.00 17.08 C ANISOU 1877 C LEU A 110 2284 2135 2069 34 -27 -28 C ATOM 1878 O LEU A 110 -0.422 -14.485 15.941 1.00 16.26 O ANISOU 1878 O LEU A 110 2343 2193 1642 131 -78 -121 O ATOM 1879 CB LEU A 110 -2.861 -13.482 16.933 1.00 17.88 C ANISOU 1879 CB LEU A 110 2327 2250 2215 24 20 -68 C ATOM 1880 CG LEU A 110 -4.182 -13.028 17.573 1.00 19.66 C ANISOU 1880 CG LEU A 110 2617 2415 2438 -26 -37 -80 C ATOM 1881 CD1 LEU A 110 -5.282 -12.774 16.524 1.00 21.37 C ANISOU 1881 CD1 LEU A 110 2768 2580 2770 -29 -38 -74 C ATOM 1882 CD2 LEU A 110 -4.642 -14.030 18.616 1.00 21.61 C ANISOU 1882 CD2 LEU A 110 2806 2668 2736 -54 103 -131 C ATOM 1883 N ASN A 111 0.800 -13.475 17.508 1.00 15.81 N ANISOU 1883 N ASN A 111 2059 2044 1903 24 -87 -33 N ATOM 1884 CA ASN A 111 2.065 -13.745 16.846 1.00 15.44 C ANISOU 1884 CA ASN A 111 2025 1975 1865 30 29 -9 C ATOM 1885 C ASN A 111 2.234 -15.247 16.721 1.00 15.17 C ANISOU 1885 C ASN A 111 2000 1961 1800 11 26 -35 C ATOM 1886 O ASN A 111 2.005 -15.953 17.689 1.00 14.53 O ANISOU 1886 O ASN A 111 1968 1883 1670 -12 228 -29 O ATOM 1887 CB ASN A 111 3.182 -13.172 17.708 1.00 15.55 C ANISOU 1887 CB ASN A 111 1984 2011 1912 80 19 -53 C ATOM 1888 CG ASN A 111 4.533 -13.175 17.031 1.00 16.13 C ANISOU 1888 CG ASN A 111 2135 2120 1874 131 97 27 C ATOM 1889 OD1 ASN A 111 4.639 -13.070 15.821 1.00 16.64 O ANISOU 1889 OD1 ASN A 111 2590 2090 1642 187 190 229 O ATOM 1890 ND2 ASN A 111 5.592 -13.250 17.845 1.00 16.24 N ANISOU 1890 ND2 ASN A 111 1871 1948 2352 574 178 141 N ATOM 1891 N PRO A 112 2.580 -15.767 15.542 1.00 15.26 N ANISOU 1891 N PRO A 112 2032 1930 1834 2 26 3 N ATOM 1892 CA PRO A 112 2.751 -17.230 15.390 1.00 15.07 C ANISOU 1892 CA PRO A 112 2026 1853 1844 2 41 11 C ATOM 1893 C PRO A 112 3.724 -17.865 16.400 1.00 14.68 C ANISOU 1893 C PRO A 112 1922 1814 1841 3 25 -2 C ATOM 1894 O PRO A 112 4.738 -17.277 16.756 1.00 13.94 O ANISOU 1894 O PRO A 112 1925 1604 1767 -80 78 70 O ATOM 1895 CB PRO A 112 3.255 -17.384 13.951 1.00 15.51 C ANISOU 1895 CB PRO A 112 2096 1879 1918 12 -7 4 C ATOM 1896 CG PRO A 112 2.684 -16.153 13.217 1.00 15.28 C ANISOU 1896 CG PRO A 112 2062 1875 1867 -11 4 28 C ATOM 1897 CD PRO A 112 2.690 -15.050 14.254 1.00 14.97 C ANISOU 1897 CD PRO A 112 2054 1824 1810 -45 91 1 C ATOM 1898 N LYS A 113 3.385 -19.051 16.882 1.00 14.81 N ANISOU 1898 N LYS A 113 1893 1816 1918 -70 -3 2 N ATOM 1899 CA LYS A 113 4.195 -19.741 17.876 1.00 15.79 C ANISOU 1899 CA LYS A 113 2012 1937 2051 -26 -26 14 C ATOM 1900 C LYS A 113 5.643 -19.918 17.425 1.00 14.90 C ANISOU 1900 C LYS A 113 1937 1786 1938 0 -2 12 C ATOM 1901 O LYS A 113 6.561 -19.719 18.206 1.00 14.59 O ANISOU 1901 O LYS A 113 1863 1661 2019 37 -89 18 O ATOM 1902 CB LYS A 113 3.577 -21.101 18.262 1.00 16.43 C ANISOU 1902 CB LYS A 113 2020 2097 2123 -59 15 9 C ATOM 1903 CG LYS A 113 2.219 -21.002 19.008 1.00 20.71 C ANISOU 1903 CG LYS A 113 2673 2555 2637 13 5 -26 C ATOM 1904 CD LYS A 113 1.972 -19.626 19.730 1.00 25.06 C ANISOU 1904 CD LYS A 113 3111 3235 3174 -96 -14 -45 C ATOM 1905 CE LYS A 113 0.669 -19.571 20.510 1.00 27.62 C ANISOU 1905 CE LYS A 113 3517 3551 3423 166 -30 -136 C ATOM 1906 NZ LYS A 113 0.709 -18.497 21.576 1.00 29.91 N ANISOU 1906 NZ LYS A 113 3770 3738 3855 232 -212 -233 N ATOM 1907 N ALA A 114 5.849 -20.266 16.166 1.00 14.92 N ANISOU 1907 N ALA A 114 1948 1765 1953 1 -49 65 N ATOM 1908 CA ALA A 114 7.197 -20.450 15.649 1.00 14.40 C ANISOU 1908 CA ALA A 114 1794 1796 1879 -25 -33 -5 C ATOM 1909 C ALA A 114 8.007 -19.147 15.703 1.00 14.21 C ANISOU 1909 C ALA A 114 1800 1672 1928 0 -61 -19 C ATOM 1910 O ALA A 114 9.228 -19.194 15.900 1.00 12.21 O ANISOU 1910 O ALA A 114 1365 1336 1936 -61 -171 -115 O ATOM 1911 CB ALA A 114 7.160 -21.004 14.216 1.00 15.36 C ANISOU 1911 CB ALA A 114 1910 1864 2059 -14 -21 -13 C ATOM 1912 N ASN A 115 7.343 -18.001 15.525 1.00 13.91 N ANISOU 1912 N ASN A 115 1712 1743 1827 15 -91 25 N ATOM 1913 CA ASN A 115 8.026 -16.700 15.587 1.00 13.88 C ANISOU 1913 CA ASN A 115 1730 1725 1816 29 -58 63 C ATOM 1914 C ASN A 115 8.523 -16.374 16.983 1.00 13.48 C ANISOU 1914 C ASN A 115 1687 1711 1722 42 -37 60 C ATOM 1915 O ASN A 115 9.587 -15.766 17.149 1.00 12.75 O ANISOU 1915 O ASN A 115 1464 1658 1721 50 -23 244 O ATOM 1916 CB ASN A 115 7.133 -15.552 15.072 1.00 13.85 C ANISOU 1916 CB ASN A 115 1731 1796 1732 43 -24 85 C ATOM 1917 CG ASN A 115 6.895 -15.648 13.594 1.00 15.15 C ANISOU 1917 CG ASN A 115 1958 1834 1961 46 -213 90 C ATOM 1918 OD1 ASN A 115 6.747 -16.757 13.067 1.00 18.74 O ANISOU 1918 OD1 ASN A 115 2703 2408 2008 450 -164 332 O ATOM 1919 ND2 ASN A 115 6.891 -14.501 12.894 1.00 16.07 N ANISOU 1919 ND2 ASN A 115 2208 1917 1980 96 -354 161 N ATOM 1920 N ARG A 116 7.751 -16.748 17.991 1.00 13.43 N ANISOU 1920 N ARG A 116 1641 1737 1722 -36 -29 78 N ATOM 1921 CA ARG A 116 8.154 -16.481 19.373 1.00 14.05 C ANISOU 1921 CA ARG A 116 1775 1835 1728 -11 -9 33 C ATOM 1922 C ARG A 116 9.394 -17.318 19.693 1.00 13.13 C ANISOU 1922 C ARG A 116 1675 1697 1615 26 -21 53 C ATOM 1923 O ARG A 116 10.286 -16.851 20.377 1.00 12.38 O ANISOU 1923 O ARG A 116 1715 1524 1465 128 -133 33 O ATOM 1924 CB ARG A 116 7.055 -16.808 20.410 1.00 14.47 C ANISOU 1924 CB ARG A 116 1757 2011 1728 47 -33 16 C ATOM 1925 CG ARG A 116 5.652 -16.486 20.045 1.00 16.79 C ANISOU 1925 CG ARG A 116 2235 2138 2003 37 46 -75 C ATOM 1926 CD ARG A 116 4.677 -16.842 21.130 1.00 18.07 C ANISOU 1926 CD ARG A 116 2329 2340 2197 24 77 -26 C ATOM 1927 NE ARG A 116 4.750 -15.823 22.161 1.00 18.39 N ANISOU 1927 NE ARG A 116 2530 2441 2017 143 3 -118 N ATOM 1928 CZ ARG A 116 4.836 -16.041 23.470 1.00 19.97 C ANISOU 1928 CZ ARG A 116 2821 2513 2252 3 -10 34 C ATOM 1929 NH1 ARG A 116 4.857 -17.280 23.974 1.00 19.21 N ANISOU 1929 NH1 ARG A 116 2654 2378 2264 -52 63 -57 N ATOM 1930 NH2 ARG A 116 4.902 -14.983 24.278 1.00 17.59 N ANISOU 1930 NH2 ARG A 116 2794 2245 1644 25 169 -129 N ATOM 1931 N GLU A 117 9.452 -18.539 19.165 1.00 13.30 N ANISOU 1931 N GLU A 117 1711 1763 1579 -30 -41 0 N ATOM 1932 CA GLU A 117 10.579 -19.430 19.407 1.00 13.69 C ANISOU 1932 CA GLU A 117 1743 1793 1665 -34 4 -50 C ATOM 1933 C GLU A 117 11.820 -18.909 18.709 1.00 13.72 C ANISOU 1933 C GLU A 117 1743 1817 1650 -29 40 -1 C ATOM 1934 O GLU A 117 12.890 -18.946 19.278 1.00 12.19 O ANISOU 1934 O GLU A 117 1377 1895 1357 37 29 41 O ATOM 1935 CB GLU A 117 10.283 -20.864 18.949 1.00 14.26 C ANISOU 1935 CB GLU A 117 1810 1878 1728 -114 -10 -27 C ATOM 1936 CG GLU A 117 9.218 -21.541 19.794 1.00 15.78 C ANISOU 1936 CG GLU A 117 2035 2064 1895 -233 136 -210 C ATOM 1937 CD GLU A 117 8.957 -22.961 19.367 1.00 20.38 C ANISOU 1937 CD GLU A 117 2610 2364 2770 -285 614 -442 C ATOM 1938 OE1 GLU A 117 9.811 -23.525 18.658 1.00 25.10 O ANISOU 1938 OE1 GLU A 117 3250 2841 3443 -621 969 -611 O ATOM 1939 OE2 GLU A 117 7.894 -23.525 19.738 1.00 23.49 O ANISOU 1939 OE2 GLU A 117 3230 2732 2963 -395 543 -1027 O ATOM 1940 N LYS A 118 11.652 -18.405 17.489 1.00 14.55 N ANISOU 1940 N LYS A 118 1848 1920 1758 3 -42 -35 N ATOM 1941 CA LYS A 118 12.758 -17.843 16.690 1.00 15.59 C ANISOU 1941 CA LYS A 118 1963 2042 1917 15 3 -6 C ATOM 1942 C LYS A 118 13.411 -16.615 17.353 1.00 14.98 C ANISOU 1942 C LYS A 118 1950 1928 1811 31 24 -5 C ATOM 1943 O LYS A 118 14.630 -16.477 17.386 1.00 13.59 O ANISOU 1943 O LYS A 118 1776 1858 1529 0 -20 -101 O ATOM 1944 CB LYS A 118 12.268 -17.455 15.282 1.00 16.43 C ANISOU 1944 CB LYS A 118 2097 2109 2036 80 45 -87 C ATOM 1945 CG LYS A 118 12.988 -18.130 14.141 1.00 22.32 C ANISOU 1945 CG LYS A 118 2752 2921 2805 47 8 39 C ATOM 1946 CD LYS A 118 14.481 -17.863 14.184 1.00 26.25 C ANISOU 1946 CD LYS A 118 3220 3379 3372 -146 52 -20 C ATOM 1947 CE LYS A 118 15.223 -18.440 12.959 1.00 29.03 C ANISOU 1947 CE LYS A 118 3599 3679 3751 31 50 -102 C ATOM 1948 NZ LYS A 118 16.617 -18.862 13.320 1.00 31.00 N ANISOU 1948 NZ LYS A 118 3518 4042 4215 -57 132 -61 N ATOM 1949 N MET A 119 12.583 -15.729 17.876 1.00 15.19 N ANISOU 1949 N MET A 119 1941 1938 1892 31 30 19 N ATOM 1950 CA MET A 119 13.039 -14.515 18.557 1.00 15.90 C ANISOU 1950 CA MET A 119 1988 2064 1987 10 13 1 C ATOM 1951 C MET A 119 13.908 -14.900 19.763 1.00 15.03 C ANISOU 1951 C MET A 119 1864 1935 1911 27 6 -8 C ATOM 1952 O MET A 119 14.994 -14.354 19.968 1.00 14.75 O ANISOU 1952 O MET A 119 1814 1972 1815 119 -145 -2 O ATOM 1953 CB MET A 119 11.798 -13.734 18.996 1.00 16.84 C ANISOU 1953 CB MET A 119 2185 2040 2173 17 0 -106 C ATOM 1954 CG MET A 119 11.932 -12.245 19.182 1.00 23.37 C ANISOU 1954 CG MET A 119 2739 2983 3155 118 201 70 C ATOM 1955 SD MET A 119 10.307 -11.548 19.843 1.00 32.79 S ANISOU 1955 SD MET A 119 3746 3970 4741 425 545 -98 S ATOM 1956 CE MET A 119 9.153 -12.395 18.682 1.00 23.51 C ANISOU 1956 CE MET A 119 2994 2760 3179 -12 95 -204 C ATOM 1957 N THR A 120 13.398 -15.841 20.552 1.00 13.95 N ANISOU 1957 N THR A 120 1775 1759 1766 31 -31 0 N ATOM 1958 CA THR A 120 14.091 -16.383 21.701 1.00 13.65 C ANISOU 1958 CA THR A 120 1736 1780 1671 -27 8 -1 C ATOM 1959 C THR A 120 15.437 -16.974 21.304 1.00 13.68 C ANISOU 1959 C THR A 120 1802 1747 1647 -19 -2 0 C ATOM 1960 O THR A 120 16.462 -16.672 21.926 1.00 12.29 O ANISOU 1960 O THR A 120 1628 1672 1368 -100 29 -23 O ATOM 1961 CB THR A 120 13.201 -17.447 22.350 1.00 13.81 C ANISOU 1961 CB THR A 120 1806 1787 1653 -8 -39 -3 C ATOM 1962 OG1 THR A 120 11.975 -16.839 22.765 1.00 12.71 O ANISOU 1962 OG1 THR A 120 1293 2081 1454 -86 89 230 O ATOM 1963 CG2 THR A 120 13.807 -17.989 23.642 1.00 14.90 C ANISOU 1963 CG2 THR A 120 1904 1873 1884 -101 -12 -40 C ATOM 1964 N GLN A 121 15.437 -17.789 20.248 1.00 13.56 N ANISOU 1964 N GLN A 121 1813 1684 1653 -22 3 -25 N ATOM 1965 CA GLN A 121 16.645 -18.455 19.778 1.00 14.35 C ANISOU 1965 CA GLN A 121 1859 1810 1781 4 -35 -72 C ATOM 1966 C GLN A 121 17.705 -17.468 19.317 1.00 13.58 C ANISOU 1966 C GLN A 121 1784 1703 1673 12 -32 -92 C ATOM 1967 O GLN A 121 18.893 -17.618 19.633 1.00 13.02 O ANISOU 1967 O GLN A 121 1663 1701 1583 73 -86 -129 O ATOM 1968 CB GLN A 121 16.307 -19.428 18.617 1.00 15.16 C ANISOU 1968 CB GLN A 121 1998 1894 1867 19 -10 -101 C ATOM 1969 CG GLN A 121 17.522 -20.056 17.951 1.00 17.23 C ANISOU 1969 CG GLN A 121 2285 2081 2181 -1 -135 -157 C ATOM 1970 CD GLN A 121 17.133 -21.186 17.007 1.00 21.94 C ANISOU 1970 CD GLN A 121 2976 2662 2695 300 -226 -331 C ATOM 1971 OE1 GLN A 121 16.101 -21.120 16.311 1.00 23.93 O ANISOU 1971 OE1 GLN A 121 3178 3099 2816 344 -470 -469 O ATOM 1972 NE2 GLN A 121 17.930 -22.226 17.000 1.00 23.39 N ANISOU 1972 NE2 GLN A 121 3290 2537 3058 511 -314 -426 N ATOM 1973 N ILE A 122 17.292 -16.456 18.565 1.00 12.87 N ANISOU 1973 N ILE A 122 1630 1691 1569 32 -90 -94 N ATOM 1974 CA ILE A 122 18.240 -15.473 18.069 1.00 13.02 C ANISOU 1974 CA ILE A 122 1626 1701 1618 -16 -30 10 C ATOM 1975 C ILE A 122 18.840 -14.665 19.235 1.00 12.34 C ANISOU 1975 C ILE A 122 1545 1650 1492 -45 -5 0 C ATOM 1976 O ILE A 122 20.055 -14.491 19.290 1.00 11.90 O ANISOU 1976 O ILE A 122 1468 1723 1330 -236 70 73 O ATOM 1977 CB ILE A 122 17.594 -14.587 16.985 1.00 14.13 C ANISOU 1977 CB ILE A 122 1783 1861 1723 -48 2 -42 C ATOM 1978 CG1 ILE A 122 17.425 -15.394 15.690 1.00 14.96 C ANISOU 1978 CG1 ILE A 122 1888 1910 1885 -75 -43 -29 C ATOM 1979 CG2 ILE A 122 18.428 -13.338 16.724 1.00 14.64 C ANISOU 1979 CG2 ILE A 122 1934 1794 1833 -81 -104 14 C ATOM 1980 CD1 ILE A 122 16.427 -14.772 14.713 1.00 15.45 C ANISOU 1980 CD1 ILE A 122 1918 2003 1946 -56 -102 122 C ATOM 1981 N MET A 123 18.023 -14.253 20.200 1.00 11.94 N ANISOU 1981 N MET A 123 1442 1570 1522 -15 -47 24 N ATOM 1982 CA MET A 123 18.507 -13.484 21.364 1.00 12.19 C ANISOU 1982 CA MET A 123 1545 1529 1558 28 7 15 C ATOM 1983 C MET A 123 19.604 -14.217 22.138 1.00 12.49 C ANISOU 1983 C MET A 123 1623 1576 1547 18 4 -14 C ATOM 1984 O MET A 123 20.654 -13.621 22.461 1.00 12.81 O ANISOU 1984 O MET A 123 1753 1511 1600 117 99 40 O ATOM 1985 CB MET A 123 17.341 -13.104 22.301 1.00 12.45 C ANISOU 1985 CB MET A 123 1642 1549 1537 -5 -14 50 C ATOM 1986 CG MET A 123 16.471 -11.935 21.747 1.00 13.35 C ANISOU 1986 CG MET A 123 1616 1720 1733 84 -28 38 C ATOM 1987 SD MET A 123 17.474 -10.433 21.500 1.00 14.88 S ANISOU 1987 SD MET A 123 2252 1741 1659 272 -155 246 S ATOM 1988 CE MET A 123 17.170 -9.944 19.793 1.00 15.77 C ANISOU 1988 CE MET A 123 1969 2089 1931 86 45 69 C ATOM 1989 N PHE A 124 19.387 -15.510 22.399 1.00 12.73 N ANISOU 1989 N PHE A 124 1631 1593 1610 12 7 15 N ATOM 1990 CA PHE A 124 20.333 -16.301 23.188 1.00 13.49 C ANISOU 1990 CA PHE A 124 1750 1637 1736 10 9 12 C ATOM 1991 C PHE A 124 21.523 -16.809 22.363 1.00 14.47 C ANISOU 1991 C PHE A 124 1843 1749 1905 6 -12 45 C ATOM 1992 O PHE A 124 22.656 -16.780 22.839 1.00 14.69 O ANISOU 1992 O PHE A 124 1752 1774 2056 72 -53 34 O ATOM 1993 CB PHE A 124 19.606 -17.463 23.885 1.00 13.24 C ANISOU 1993 CB PHE A 124 1757 1602 1669 4 52 27 C ATOM 1994 CG PHE A 124 18.771 -17.042 25.075 1.00 12.63 C ANISOU 1994 CG PHE A 124 1622 1532 1645 -11 -56 103 C ATOM 1995 CD1 PHE A 124 19.362 -16.453 26.179 1.00 12.28 C ANISOU 1995 CD1 PHE A 124 1666 1352 1645 -139 156 20 C ATOM 1996 CD2 PHE A 124 17.401 -17.251 25.090 1.00 13.15 C ANISOU 1996 CD2 PHE A 124 1962 1480 1552 -43 132 168 C ATOM 1997 CE1 PHE A 124 18.611 -16.067 27.264 1.00 13.32 C ANISOU 1997 CE1 PHE A 124 1762 1557 1742 -97 -26 128 C ATOM 1998 CE2 PHE A 124 16.633 -16.870 26.174 1.00 14.09 C ANISOU 1998 CE2 PHE A 124 1955 1608 1790 0 -43 206 C ATOM 1999 CZ PHE A 124 17.232 -16.277 27.268 1.00 13.54 C ANISOU 1999 CZ PHE A 124 1809 1540 1794 -175 -41 -10 C ATOM 2000 N GLU A 125 21.297 -17.237 21.123 1.00 15.68 N ANISOU 2000 N GLU A 125 1964 1938 2056 21 -8 46 N ATOM 2001 CA GLU A 125 22.363 -17.882 20.346 1.00 17.17 C ANISOU 2001 CA GLU A 125 2178 2152 2192 16 30 24 C ATOM 2002 C GLU A 125 23.193 -16.923 19.482 1.00 17.42 C ANISOU 2002 C GLU A 125 2170 2223 2224 38 29 49 C ATOM 2003 O GLU A 125 24.388 -17.113 19.334 1.00 17.79 O ANISOU 2003 O GLU A 125 2221 2300 2236 133 49 112 O ATOM 2004 CB GLU A 125 21.811 -19.025 19.484 1.00 17.99 C ANISOU 2004 CB GLU A 125 2231 2311 2292 -16 42 2 C ATOM 2005 CG GLU A 125 21.420 -20.249 20.296 1.00 19.01 C ANISOU 2005 CG GLU A 125 2477 2308 2437 127 74 -34 C ATOM 2006 CD GLU A 125 20.847 -21.379 19.449 1.00 23.04 C ANISOU 2006 CD GLU A 125 2903 3113 2737 -57 134 2 C ATOM 2007 OE1 GLU A 125 21.109 -21.433 18.215 1.00 23.55 O ANISOU 2007 OE1 GLU A 125 3282 3149 2515 293 413 -134 O ATOM 2008 OE2 GLU A 125 20.142 -22.236 20.036 1.00 24.46 O ANISOU 2008 OE2 GLU A 125 3006 3439 2846 -214 366 -8 O ATOM 2009 N THR A 126 22.555 -15.908 18.909 1.00 17.27 N ANISOU 2009 N THR A 126 2172 2186 2202 23 20 31 N ATOM 2010 CA THR A 126 23.248 -14.876 18.137 1.00 17.42 C ANISOU 2010 CA THR A 126 2159 2265 2194 24 38 -8 C ATOM 2011 C THR A 126 23.822 -13.776 19.043 1.00 16.50 C ANISOU 2011 C THR A 126 2051 2142 2077 -28 18 -10 C ATOM 2012 O THR A 126 25.004 -13.459 18.954 1.00 16.20 O ANISOU 2012 O THR A 126 1898 2159 2097 -59 35 1 O ATOM 2013 CB THR A 126 22.284 -14.271 17.082 1.00 17.37 C ANISOU 2013 CB THR A 126 2131 2279 2187 6 38 9 C ATOM 2014 OG1 THR A 126 21.949 -15.269 16.125 1.00 19.19 O ANISOU 2014 OG1 THR A 126 2414 2675 2202 90 97 -81 O ATOM 2015 CG2 THR A 126 22.935 -13.208 16.260 1.00 19.10 C ANISOU 2015 CG2 THR A 126 2399 2544 2311 89 64 -25 C ATOM 2016 N PHE A 127 22.996 -13.210 19.919 1.00 15.00 N ANISOU 2016 N PHE A 127 1863 1953 1880 -10 21 -1 N ATOM 2017 CA PHE A 127 23.416 -12.060 20.735 1.00 14.51 C ANISOU 2017 CA PHE A 127 1839 1859 1813 -63 0 18 C ATOM 2018 C PHE A 127 23.893 -12.400 22.162 1.00 14.26 C ANISOU 2018 C PHE A 127 1771 1887 1759 -79 -17 0 C ATOM 2019 O PHE A 127 24.361 -11.522 22.873 1.00 14.90 O ANISOU 2019 O PHE A 127 1811 2113 1737 -206 0 168 O ATOM 2020 CB PHE A 127 22.298 -11.017 20.751 1.00 13.59 C ANISOU 2020 CB PHE A 127 1700 1773 1689 -46 43 -53 C ATOM 2021 CG PHE A 127 22.002 -10.456 19.389 1.00 13.56 C ANISOU 2021 CG PHE A 127 1702 1599 1851 -42 -20 3 C ATOM 2022 CD1 PHE A 127 20.829 -10.773 18.732 1.00 12.25 C ANISOU 2022 CD1 PHE A 127 1684 1236 1734 -31 -91 -67 C ATOM 2023 CD2 PHE A 127 22.942 -9.652 18.738 1.00 15.25 C ANISOU 2023 CD2 PHE A 127 1819 1960 2012 -126 -66 59 C ATOM 2024 CE1 PHE A 127 20.571 -10.282 17.450 1.00 13.61 C ANISOU 2024 CE1 PHE A 127 1877 1456 1835 -161 -154 -148 C ATOM 2025 CE2 PHE A 127 22.708 -9.153 17.452 1.00 13.10 C ANISOU 2025 CE2 PHE A 127 1682 1612 1683 -15 -248 77 C ATOM 2026 CZ PHE A 127 21.504 -9.474 16.802 1.00 14.29 C ANISOU 2026 CZ PHE A 127 1795 1800 1831 -126 29 41 C ATOM 2027 N ASN A 128 23.740 -13.654 22.569 1.00 14.34 N ANISOU 2027 N ASN A 128 1772 1872 1803 7 -51 11 N ATOM 2028 CA ASN A 128 24.192 -14.153 23.868 1.00 14.83 C ANISOU 2028 CA ASN A 128 1832 1938 1864 -33 -32 -20 C ATOM 2029 C ASN A 128 23.693 -13.318 25.050 1.00 14.41 C ANISOU 2029 C ASN A 128 1789 1883 1801 10 -55 0 C ATOM 2030 O ASN A 128 24.437 -13.093 25.995 1.00 14.47 O ANISOU 2030 O ASN A 128 1690 2003 1802 51 -105 -132 O ATOM 2031 CB ASN A 128 25.745 -14.297 23.885 1.00 15.77 C ANISOU 2031 CB ASN A 128 2019 2003 1969 -22 -100 50 C ATOM 2032 CG ASN A 128 26.267 -15.154 25.069 1.00 19.36 C ANISOU 2032 CG ASN A 128 2329 2369 2658 -248 -99 -40 C ATOM 2033 OD1 ASN A 128 27.356 -14.905 25.610 1.00 23.51 O ANISOU 2033 OD1 ASN A 128 2723 2912 3298 -541 -85 -197 O ATOM 2034 ND2 ASN A 128 25.489 -16.163 25.468 1.00 22.85 N ANISOU 2034 ND2 ASN A 128 2613 2838 3228 -659 67 -57 N ATOM 2035 N VAL A 129 22.440 -12.860 25.005 1.00 13.14 N ANISOU 2035 N VAL A 129 1624 1784 1583 -9 -21 27 N ATOM 2036 CA VAL A 129 21.853 -12.168 26.144 1.00 13.22 C ANISOU 2036 CA VAL A 129 1663 1660 1699 12 -19 8 C ATOM 2037 C VAL A 129 21.846 -13.092 27.382 1.00 12.52 C ANISOU 2037 C VAL A 129 1568 1614 1572 28 -35 36 C ATOM 2038 O VAL A 129 21.736 -14.319 27.248 1.00 12.51 O ANISOU 2038 O VAL A 129 1536 1604 1613 -53 -118 11 O ATOM 2039 CB VAL A 129 20.397 -11.640 25.874 1.00 12.74 C ANISOU 2039 CB VAL A 129 1630 1649 1560 24 11 48 C ATOM 2040 CG1 VAL A 129 20.360 -10.670 24.705 1.00 14.62 C ANISOU 2040 CG1 VAL A 129 1763 1881 1911 132 13 1 C ATOM 2041 CG2 VAL A 129 19.411 -12.763 25.673 1.00 13.41 C ANISOU 2041 CG2 VAL A 129 1669 1833 1593 28 -10 -90 C ATOM 2042 N PRO A 130 21.969 -12.517 28.575 1.00 12.29 N ANISOU 2042 N PRO A 130 1510 1545 1613 3 -21 -4 N ATOM 2043 CA PRO A 130 21.901 -13.311 29.817 1.00 11.95 C ANISOU 2043 CA PRO A 130 1461 1513 1564 14 0 16 C ATOM 2044 C PRO A 130 20.456 -13.725 30.172 1.00 12.27 C ANISOU 2044 C PRO A 130 1488 1556 1616 -25 -16 15 C ATOM 2045 O PRO A 130 20.245 -14.682 30.921 1.00 11.81 O ANISOU 2045 O PRO A 130 1395 1528 1561 -136 -6 -37 O ATOM 2046 CB PRO A 130 22.447 -12.358 30.883 1.00 11.75 C ANISOU 2046 CB PRO A 130 1376 1520 1566 -4 -29 60 C ATOM 2047 CG PRO A 130 22.147 -10.951 30.344 1.00 12.49 C ANISOU 2047 CG PRO A 130 1534 1591 1621 19 34 -69 C ATOM 2048 CD PRO A 130 22.150 -11.071 28.838 1.00 12.60 C ANISOU 2048 CD PRO A 130 1577 1599 1609 59 -48 51 C ATOM 2049 N ALA A 131 19.485 -12.979 29.644 1.00 12.15 N ANISOU 2049 N ALA A 131 1469 1538 1608 8 -22 19 N ATOM 2050 CA ALA A 131 18.070 -13.164 29.979 1.00 12.51 C ANISOU 2050 CA ALA A 131 1533 1619 1599 35 -19 -20 C ATOM 2051 C ALA A 131 17.222 -12.419 28.983 1.00 12.66 C ANISOU 2051 C ALA A 131 1535 1613 1659 63 -6 -9 C ATOM 2052 O ALA A 131 17.685 -11.431 28.412 1.00 11.84 O ANISOU 2052 O ALA A 131 1277 1567 1652 171 -30 -33 O ATOM 2053 CB ALA A 131 17.764 -12.668 31.414 1.00 12.61 C ANISOU 2053 CB ALA A 131 1497 1679 1614 88 -34 -27 C ATOM 2054 N MET A 132 15.989 -12.895 28.770 1.00 12.95 N ANISOU 2054 N MET A 132 1580 1628 1713 -10 54 -17 N ATOM 2055 CA MET A 132 15.064 -12.301 27.805 1.00 13.46 C ANISOU 2055 CA MET A 132 1709 1711 1692 0 8 -27 C ATOM 2056 C MET A 132 13.595 -12.567 28.171 1.00 12.54 C ANISOU 2056 C MET A 132 1634 1554 1576 -103 -42 -55 C ATOM 2057 O MET A 132 13.302 -13.455 28.973 1.00 11.63 O ANISOU 2057 O MET A 132 1504 1437 1475 -220 -37 -84 O ATOM 2058 CB MET A 132 15.385 -12.759 26.362 1.00 15.22 C ANISOU 2058 CB MET A 132 1892 1891 1999 -128 -3 -63 C ATOM 2059 CG MET A 132 14.747 -14.075 25.879 1.00 20.03 C ANISOU 2059 CG MET A 132 2744 2467 2397 220 -48 -70 C ATOM 2060 SD MET A 132 13.608 -13.749 24.526 1.00 34.12 S ANISOU 2060 SD MET A 132 4439 3999 4523 -313 -120 -708 S ATOM 2061 CE MET A 132 12.187 -14.434 25.132 1.00 34.66 C ANISOU 2061 CE MET A 132 4569 4245 4354 -126 98 -78 C ATOM 2062 N TYR A 133 12.694 -11.748 27.630 1.00 11.47 N ANISOU 2062 N TYR A 133 1485 1436 1436 -52 -3 -5 N ATOM 2063 CA TYR A 133 11.252 -11.882 27.834 1.00 11.87 C ANISOU 2063 CA TYR A 133 1571 1438 1500 -14 -64 -34 C ATOM 2064 C TYR A 133 10.567 -11.308 26.604 1.00 12.00 C ANISOU 2064 C TYR A 133 1559 1504 1495 -34 -97 -30 C ATOM 2065 O TYR A 133 11.109 -10.411 25.956 1.00 12.34 O ANISOU 2065 O TYR A 133 1504 1669 1513 -201 -362 -72 O ATOM 2066 CB TYR A 133 10.819 -11.094 29.095 1.00 12.15 C ANISOU 2066 CB TYR A 133 1578 1566 1473 4 -38 115 C ATOM 2067 CG TYR A 133 9.445 -11.407 29.617 1.00 12.30 C ANISOU 2067 CG TYR A 133 1556 1511 1607 6 -82 102 C ATOM 2068 CD1 TYR A 133 8.344 -10.639 29.244 1.00 13.18 C ANISOU 2068 CD1 TYR A 133 1659 1470 1876 -139 23 -10 C ATOM 2069 CD2 TYR A 133 9.245 -12.458 30.516 1.00 14.57 C ANISOU 2069 CD2 TYR A 133 1868 1805 1863 -75 124 127 C ATOM 2070 CE1 TYR A 133 7.078 -10.925 29.727 1.00 13.85 C ANISOU 2070 CE1 TYR A 133 1844 1576 1840 51 99 220 C ATOM 2071 CE2 TYR A 133 7.977 -12.738 31.027 1.00 13.25 C ANISOU 2071 CE2 TYR A 133 1587 1563 1884 -27 -182 35 C ATOM 2072 CZ TYR A 133 6.909 -11.966 30.617 1.00 16.43 C ANISOU 2072 CZ TYR A 133 1923 2126 2191 -195 195 -135 C ATOM 2073 OH TYR A 133 5.664 -12.231 31.086 1.00 19.78 O ANISOU 2073 OH TYR A 133 2170 2727 2617 -755 87 90 O ATOM 2074 N VAL A 134 9.392 -11.827 26.269 1.00 12.49 N ANISOU 2074 N VAL A 134 1561 1514 1669 13 -62 -5 N ATOM 2075 CA VAL A 134 8.565 -11.260 25.204 1.00 13.67 C ANISOU 2075 CA VAL A 134 1707 1753 1732 -7 -19 4 C ATOM 2076 C VAL A 134 7.185 -10.935 25.772 1.00 12.79 C ANISOU 2076 C VAL A 134 1549 1625 1682 46 -17 12 C ATOM 2077 O VAL A 134 6.556 -11.801 26.388 1.00 12.03 O ANISOU 2077 O VAL A 134 1423 1550 1596 114 46 155 O ATOM 2078 CB VAL A 134 8.349 -12.238 24.022 1.00 14.47 C ANISOU 2078 CB VAL A 134 1775 1870 1853 139 -21 -44 C ATOM 2079 CG1 VAL A 134 7.787 -11.483 22.815 1.00 16.61 C ANISOU 2079 CG1 VAL A 134 2262 2117 1932 -2 35 -64 C ATOM 2080 CG2 VAL A 134 9.623 -12.912 23.625 1.00 17.54 C ANISOU 2080 CG2 VAL A 134 2230 2331 2100 -13 -51 98 C ATOM 2081 N ALA A 135 6.709 -9.710 25.546 1.00 12.12 N ANISOU 2081 N ALA A 135 1499 1470 1636 -47 2 58 N ATOM 2082 CA ALA A 135 5.377 -9.293 25.987 1.00 11.67 C ANISOU 2082 CA ALA A 135 1484 1448 1501 -19 20 9 C ATOM 2083 C ALA A 135 4.516 -8.806 24.830 1.00 10.90 C ANISOU 2083 C ALA A 135 1379 1358 1402 -45 -5 12 C ATOM 2084 O ALA A 135 5.032 -8.312 23.850 1.00 11.08 O ANISOU 2084 O ALA A 135 1276 1564 1370 26 -77 -64 O ATOM 2085 CB ALA A 135 5.494 -8.205 27.058 1.00 12.03 C ANISOU 2085 CB ALA A 135 1574 1436 1559 -57 -12 43 C ATOM 2086 N ILE A 136 3.197 -8.944 24.957 1.00 10.16 N ANISOU 2086 N ILE A 136 1273 1262 1324 15 44 26 N ATOM 2087 CA ILE A 136 2.257 -8.470 23.947 1.00 10.37 C ANISOU 2087 CA ILE A 136 1362 1313 1262 -32 32 -8 C ATOM 2088 C ILE A 136 2.126 -6.944 24.011 1.00 9.35 C ANISOU 2088 C ILE A 136 1205 1186 1158 33 38 -21 C ATOM 2089 O ILE A 136 1.899 -6.385 25.074 1.00 7.72 O ANISOU 2089 O ILE A 136 1009 1162 761 10 85 -71 O ATOM 2090 CB ILE A 136 0.879 -9.114 24.145 1.00 10.51 C ANISOU 2090 CB ILE A 136 1328 1289 1373 -25 -19 28 C ATOM 2091 CG1 ILE A 136 0.964 -10.635 23.951 1.00 13.02 C ANISOU 2091 CG1 ILE A 136 1567 1660 1718 -24 129 -91 C ATOM 2092 CG2 ILE A 136 -0.135 -8.536 23.175 1.00 13.10 C ANISOU 2092 CG2 ILE A 136 1860 1566 1550 -36 82 -25 C ATOM 2093 CD1 ILE A 136 -0.345 -11.385 24.326 1.00 14.01 C ANISOU 2093 CD1 ILE A 136 1803 1668 1850 -153 81 11 C ATOM 2094 N GLN A 137 2.295 -6.290 22.858 1.00 8.80 N ANISOU 2094 N GLN A 137 1190 1103 1050 59 12 -88 N ATOM 2095 CA GLN A 137 2.314 -4.833 22.743 1.00 9.35 C ANISOU 2095 CA GLN A 137 1234 1154 1163 21 40 0 C ATOM 2096 C GLN A 137 1.061 -4.181 23.369 1.00 9.20 C ANISOU 2096 C GLN A 137 1170 1094 1230 52 -8 6 C ATOM 2097 O GLN A 137 1.146 -3.307 24.239 1.00 8.41 O ANISOU 2097 O GLN A 137 1222 872 1100 38 83 3 O ATOM 2098 CB GLN A 137 2.448 -4.446 21.273 1.00 9.89 C ANISOU 2098 CB GLN A 137 1284 1198 1273 3 30 -14 C ATOM 2099 CG GLN A 137 3.831 -4.782 20.722 1.00 10.66 C ANISOU 2099 CG GLN A 137 1400 1246 1403 90 21 30 C ATOM 2100 CD GLN A 137 3.852 -5.178 19.259 1.00 11.49 C ANISOU 2100 CD GLN A 137 1636 1183 1545 240 -57 -42 C ATOM 2101 OE1 GLN A 137 2.826 -5.134 18.562 1.00 12.92 O ANISOU 2101 OE1 GLN A 137 1886 1229 1794 290 -238 -407 O ATOM 2102 NE2 GLN A 137 5.038 -5.556 18.780 1.00 9.60 N ANISOU 2102 NE2 GLN A 137 1402 725 1519 527 79 124 N ATOM 2103 N ALA A 138 -0.105 -4.653 22.976 1.00 9.25 N ANISOU 2103 N ALA A 138 1185 1094 1234 -4 -9 -14 N ATOM 2104 CA ALA A 138 -1.341 -4.020 23.442 1.00 9.64 C ANISOU 2104 CA ALA A 138 1194 1223 1243 -41 12 -71 C ATOM 2105 C ALA A 138 -1.457 -4.080 24.973 1.00 9.47 C ANISOU 2105 C ALA A 138 1188 1230 1180 -9 -41 -103 C ATOM 2106 O ALA A 138 -1.936 -3.107 25.622 1.00 8.98 O ANISOU 2106 O ALA A 138 1151 1158 1101 -116 -126 -415 O ATOM 2107 CB ALA A 138 -2.558 -4.677 22.773 1.00 10.38 C ANISOU 2107 CB ALA A 138 1269 1328 1347 -107 -9 6 C ATOM 2108 N VAL A 139 -1.039 -5.204 25.549 1.00 8.70 N ANISOU 2108 N VAL A 139 1074 1144 1086 -42 -4 -115 N ATOM 2109 CA VAL A 139 -1.149 -5.396 26.995 1.00 8.48 C ANISOU 2109 CA VAL A 139 1026 1100 1095 -7 33 -26 C ATOM 2110 C VAL A 139 -0.224 -4.425 27.722 1.00 7.68 C ANISOU 2110 C VAL A 139 1023 921 973 -29 61 25 C ATOM 2111 O VAL A 139 -0.620 -3.817 28.713 1.00 6.58 O ANISOU 2111 O VAL A 139 937 697 867 -1 162 181 O ATOM 2112 CB VAL A 139 -0.839 -6.853 27.395 1.00 8.90 C ANISOU 2112 CB VAL A 139 1139 1094 1146 -11 31 -96 C ATOM 2113 CG1 VAL A 139 -0.775 -7.021 28.890 1.00 10.07 C ANISOU 2113 CG1 VAL A 139 1342 1204 1279 -29 127 -134 C ATOM 2114 CG2 VAL A 139 -1.873 -7.838 26.772 1.00 8.38 C ANISOU 2114 CG2 VAL A 139 696 1210 1278 61 230 -188 C ATOM 2115 N LEU A 140 1.000 -4.253 27.217 1.00 7.27 N ANISOU 2115 N LEU A 140 915 902 945 -8 7 26 N ATOM 2116 CA LEU A 140 1.909 -3.232 27.757 1.00 7.60 C ANISOU 2116 CA LEU A 140 974 941 972 -2 30 -17 C ATOM 2117 C LEU A 140 1.298 -1.842 27.757 1.00 7.77 C ANISOU 2117 C LEU A 140 962 978 1009 -2 22 42 C ATOM 2118 O LEU A 140 1.482 -1.089 28.717 1.00 6.84 O ANISOU 2118 O LEU A 140 939 531 1129 58 188 -99 O ATOM 2119 CB LEU A 140 3.256 -3.218 27.007 1.00 6.88 C ANISOU 2119 CB LEU A 140 814 894 906 -40 -32 103 C ATOM 2120 CG LEU A 140 4.114 -4.470 27.221 1.00 7.71 C ANISOU 2120 CG LEU A 140 979 888 1061 -18 102 -124 C ATOM 2121 CD1 LEU A 140 5.434 -4.360 26.436 1.00 9.21 C ANISOU 2121 CD1 LEU A 140 1232 934 1332 1 103 12 C ATOM 2122 CD2 LEU A 140 4.411 -4.733 28.687 1.00 5.67 C ANISOU 2122 CD2 LEU A 140 948 462 744 71 104 -15 C ATOM 2123 N SER A 141 0.566 -1.505 26.692 1.00 8.92 N ANISOU 2123 N SER A 141 1167 1105 1117 -39 85 17 N ATOM 2124 CA SER A 141 -0.085 -0.213 26.601 1.00 9.71 C ANISOU 2124 CA SER A 141 1240 1275 1173 24 42 109 C ATOM 2125 C SER A 141 -1.150 -0.031 27.672 1.00 9.16 C ANISOU 2125 C SER A 141 1244 1186 1050 -4 99 88 C ATOM 2126 O SER A 141 -1.290 1.047 28.233 1.00 9.76 O ANISOU 2126 O SER A 141 1376 1389 941 -30 136 259 O ATOM 2127 CB SER A 141 -0.681 -0.012 25.203 1.00 9.88 C ANISOU 2127 CB SER A 141 1273 1331 1150 3 240 130 C ATOM 2128 OG SER A 141 0.381 0.348 24.376 1.00 16.06 O ANISOU 2128 OG SER A 141 2366 2035 1699 197 -101 461 O ATOM 2129 N LEU A 142 -1.886 -1.084 27.966 1.00 8.74 N ANISOU 2129 N LEU A 142 1112 1165 1041 -22 22 51 N ATOM 2130 CA LEU A 142 -2.911 -0.993 28.993 1.00 8.77 C ANISOU 2130 CA LEU A 142 1148 1110 1072 4 60 -12 C ATOM 2131 C LEU A 142 -2.254 -0.752 30.361 1.00 8.51 C ANISOU 2131 C LEU A 142 1082 1094 1057 -21 49 8 C ATOM 2132 O LEU A 142 -2.695 0.115 31.117 1.00 6.70 O ANISOU 2132 O LEU A 142 880 782 883 -36 203 -48 O ATOM 2133 CB LEU A 142 -3.773 -2.245 29.020 1.00 9.06 C ANISOU 2133 CB LEU A 142 1110 1235 1095 -55 29 -25 C ATOM 2134 CG LEU A 142 -4.992 -2.144 29.927 1.00 9.11 C ANISOU 2134 CG LEU A 142 1188 1175 1098 123 137 -26 C ATOM 2135 CD1 LEU A 142 -6.057 -1.267 29.318 1.00 10.14 C ANISOU 2135 CD1 LEU A 142 1239 1448 1164 -4 -113 -106 C ATOM 2136 CD2 LEU A 142 -5.552 -3.522 30.256 1.00 9.20 C ANISOU 2136 CD2 LEU A 142 1078 1198 1219 88 161 -252 C ATOM 2137 N TYR A 143 -1.183 -1.494 30.657 1.00 8.67 N ANISOU 2137 N TYR A 143 1126 1082 1085 1 102 -53 N ATOM 2138 CA TYR A 143 -0.433 -1.288 31.888 1.00 8.67 C ANISOU 2138 CA TYR A 143 1127 1126 1040 11 43 3 C ATOM 2139 C TYR A 143 0.119 0.147 32.027 1.00 8.79 C ANISOU 2139 C TYR A 143 1191 1103 1043 37 41 -16 C ATOM 2140 O TYR A 143 0.098 0.718 33.122 1.00 8.58 O ANISOU 2140 O TYR A 143 1254 1161 844 109 1 12 O ATOM 2141 CB TYR A 143 0.728 -2.273 32.017 1.00 9.36 C ANISOU 2141 CB TYR A 143 1291 1130 1135 28 88 -127 C ATOM 2142 CG TYR A 143 0.389 -3.741 32.132 1.00 10.06 C ANISOU 2142 CG TYR A 143 1266 1383 1173 62 110 116 C ATOM 2143 CD1 TYR A 143 1.372 -4.687 31.928 1.00 10.70 C ANISOU 2143 CD1 TYR A 143 1476 1335 1252 306 4 -101 C ATOM 2144 CD2 TYR A 143 -0.894 -4.183 32.421 1.00 12.95 C ANISOU 2144 CD2 TYR A 143 1800 1477 1642 186 147 -49 C ATOM 2145 CE1 TYR A 143 1.103 -6.022 32.035 1.00 13.65 C ANISOU 2145 CE1 TYR A 143 1475 1877 1833 100 240 35 C ATOM 2146 CE2 TYR A 143 -1.180 -5.515 32.514 1.00 13.94 C ANISOU 2146 CE2 TYR A 143 1801 1664 1830 289 202 114 C ATOM 2147 CZ TYR A 143 -0.175 -6.441 32.312 1.00 15.46 C ANISOU 2147 CZ TYR A 143 1786 2024 2061 289 160 102 C ATOM 2148 OH TYR A 143 -0.447 -7.789 32.405 1.00 16.11 O ANISOU 2148 OH TYR A 143 1530 1955 2635 574 172 161 O ATOM 2149 N ALA A 144 0.636 0.709 30.933 1.00 8.21 N ANISOU 2149 N ALA A 144 1127 1026 965 9 41 -28 N ATOM 2150 CA ALA A 144 1.146 2.067 30.940 1.00 8.63 C ANISOU 2150 CA ALA A 144 1066 1120 1092 -9 29 -18 C ATOM 2151 C ALA A 144 0.065 3.081 31.321 1.00 8.44 C ANISOU 2151 C ALA A 144 1039 1113 1055 -42 137 -79 C ATOM 2152 O ALA A 144 0.368 4.117 31.884 1.00 9.67 O ANISOU 2152 O ALA A 144 1025 1298 1350 -193 236 -192 O ATOM 2153 CB ALA A 144 1.763 2.420 29.581 1.00 7.82 C ANISOU 2153 CB ALA A 144 1013 1010 947 58 101 -49 C ATOM 2154 N SER A 145 -1.190 2.769 31.012 1.00 8.68 N ANISOU 2154 N SER A 145 1080 1104 1115 -15 33 -49 N ATOM 2155 CA SER A 145 -2.330 3.608 31.393 1.00 9.37 C ANISOU 2155 CA SER A 145 1135 1204 1220 -18 18 -16 C ATOM 2156 C SER A 145 -2.836 3.368 32.820 1.00 9.70 C ANISOU 2156 C SER A 145 1169 1199 1316 22 26 25 C ATOM 2157 O SER A 145 -3.828 3.978 33.243 1.00 9.07 O ANISOU 2157 O SER A 145 871 1185 1389 135 -39 -3 O ATOM 2158 CB SER A 145 -3.468 3.427 30.390 1.00 9.88 C ANISOU 2158 CB SER A 145 1104 1232 1418 50 104 -17 C ATOM 2159 OG SER A 145 -4.275 2.296 30.734 1.00 12.01 O ANISOU 2159 OG SER A 145 1315 1624 1623 -129 -38 203 O ATOM 2160 N GLY A 146 -2.151 2.506 33.574 1.00 9.83 N ANISOU 2160 N GLY A 146 1194 1258 1281 41 0 5 N ATOM 2161 CA GLY A 146 -2.557 2.177 34.940 1.00 9.66 C ANISOU 2161 CA GLY A 146 1220 1196 1255 18 -2 7 C ATOM 2162 C GLY A 146 -3.839 1.368 35.108 1.00 9.50 C ANISOU 2162 C GLY A 146 1176 1187 1243 34 -33 5 C ATOM 2163 O GLY A 146 -4.602 1.598 36.044 1.00 8.37 O ANISOU 2163 O GLY A 146 1082 922 1175 85 -12 -114 O ATOM 2164 N ARG A 147 -4.049 0.412 34.217 1.00 9.20 N ANISOU 2164 N ARG A 147 1195 1024 1276 24 -17 -73 N ATOM 2165 CA ARG A 147 -5.242 -0.441 34.184 1.00 9.96 C ANISOU 2165 CA ARG A 147 1223 1239 1319 -7 49 22 C ATOM 2166 C ARG A 147 -4.875 -1.932 34.010 1.00 8.77 C ANISOU 2166 C ARG A 147 1115 974 1244 -58 74 -23 C ATOM 2167 O ARG A 147 -3.907 -2.270 33.343 1.00 7.90 O ANISOU 2167 O ARG A 147 1055 778 1167 -96 166 -62 O ATOM 2168 CB ARG A 147 -6.079 -0.084 32.955 1.00 10.73 C ANISOU 2168 CB ARG A 147 1207 1448 1421 -11 126 45 C ATOM 2169 CG ARG A 147 -7.116 0.925 33.215 1.00 13.91 C ANISOU 2169 CG ARG A 147 1763 1700 1819 29 30 64 C ATOM 2170 CD ARG A 147 -7.751 1.499 32.004 1.00 15.05 C ANISOU 2170 CD ARG A 147 1845 2137 1734 -331 71 95 C ATOM 2171 NE ARG A 147 -7.023 2.705 31.841 1.00 19.96 N ANISOU 2171 NE ARG A 147 2711 2713 2158 -113 48 107 N ATOM 2172 CZ ARG A 147 -7.391 3.915 32.164 1.00 15.98 C ANISOU 2172 CZ ARG A 147 2169 2201 1700 257 173 133 C ATOM 2173 NH1 ARG A 147 -8.599 4.243 32.554 1.00 18.13 N ANISOU 2173 NH1 ARG A 147 1708 3414 1766 -182 -114 568 N ATOM 2174 NH2 ARG A 147 -6.484 4.837 32.023 1.00 15.38 N ANISOU 2174 NH2 ARG A 147 1916 1770 2157 -368 102 152 N ATOM 2175 N THR A 148 -5.706 -2.818 34.553 1.00 8.80 N ANISOU 2175 N THR A 148 1181 1033 1127 52 75 -44 N ATOM 2176 CA THR A 148 -5.598 -4.263 34.282 1.00 8.27 C ANISOU 2176 CA THR A 148 1049 968 1124 25 101 -53 C ATOM 2177 C THR A 148 -6.718 -4.776 33.389 1.00 8.33 C ANISOU 2177 C THR A 148 1019 1071 1075 46 31 -42 C ATOM 2178 O THR A 148 -6.653 -5.908 32.907 1.00 8.30 O ANISOU 2178 O THR A 148 923 1077 1152 151 11 -130 O ATOM 2179 CB THR A 148 -5.611 -5.072 35.579 1.00 7.54 C ANISOU 2179 CB THR A 148 998 865 1001 52 63 -40 C ATOM 2180 OG1 THR A 148 -6.884 -4.931 36.237 1.00 6.30 O ANISOU 2180 OG1 THR A 148 826 589 978 -194 247 -170 O ATOM 2181 CG2 THR A 148 -4.579 -4.546 36.563 1.00 7.81 C ANISOU 2181 CG2 THR A 148 893 903 1169 182 205 -75 C ATOM 2182 N THR A 149 -7.775 -3.981 33.235 1.00 8.70 N ANISOU 2182 N THR A 149 1154 1059 1089 32 29 -2 N ATOM 2183 CA THR A 149 -8.943 -4.390 32.450 1.00 8.39 C ANISOU 2183 CA THR A 149 1026 1082 1077 10 55 59 C ATOM 2184 C THR A 149 -9.298 -3.249 31.511 1.00 8.76 C ANISOU 2184 C THR A 149 1149 1061 1117 24 32 -1 C ATOM 2185 O THR A 149 -9.283 -2.117 31.908 1.00 9.69 O ANISOU 2185 O THR A 149 1335 1045 1300 45 65 67 O ATOM 2186 CB THR A 149 -10.145 -4.718 33.384 1.00 8.65 C ANISOU 2186 CB THR A 149 1142 1056 1089 8 -22 66 C ATOM 2187 OG1 THR A 149 -9.910 -5.965 34.052 1.00 7.10 O ANISOU 2187 OG1 THR A 149 806 1133 759 -90 268 130 O ATOM 2188 CG2 THR A 149 -11.399 -5.001 32.562 1.00 8.81 C ANISOU 2188 CG2 THR A 149 943 1030 1374 69 64 37 C ATOM 2189 N GLY A 150 -9.606 -3.568 30.261 1.00 8.80 N ANISOU 2189 N GLY A 150 1132 1065 1146 -2 0 13 N ATOM 2190 CA GLY A 150 -9.942 -2.585 29.263 1.00 8.08 C ANISOU 2190 CA GLY A 150 946 1069 1054 17 -17 33 C ATOM 2191 C GLY A 150 -9.809 -3.145 27.867 1.00 8.24 C ANISOU 2191 C GLY A 150 986 1107 1036 46 4 22 C ATOM 2192 O GLY A 150 -9.460 -4.326 27.666 1.00 8.02 O ANISOU 2192 O GLY A 150 921 1269 858 179 36 -36 O ATOM 2193 N ILE A 151 -10.137 -2.315 26.880 1.00 8.83 N ANISOU 2193 N ILE A 151 1057 1191 1107 61 30 -2 N ATOM 2194 CA ILE A 151 -9.934 -2.711 25.484 1.00 9.08 C ANISOU 2194 CA ILE A 151 1138 1173 1140 62 14 0 C ATOM 2195 C ILE A 151 -9.024 -1.712 24.796 1.00 9.17 C ANISOU 2195 C ILE A 151 1124 1178 1179 52 91 4 C ATOM 2196 O ILE A 151 -9.266 -0.499 24.781 1.00 9.93 O ANISOU 2196 O ILE A 151 1153 1273 1344 112 265 -17 O ATOM 2197 CB ILE A 151 -11.286 -2.954 24.744 1.00 9.11 C ANISOU 2197 CB ILE A 151 1100 1215 1143 16 48 -20 C ATOM 2198 CG1 ILE A 151 -11.035 -3.396 23.292 1.00 11.08 C ANISOU 2198 CG1 ILE A 151 1326 1499 1383 -51 -40 -2 C ATOM 2199 CG2 ILE A 151 -12.184 -1.725 24.794 1.00 7.54 C ANISOU 2199 CG2 ILE A 151 907 954 1002 53 -13 181 C ATOM 2200 CD1 ILE A 151 -12.278 -3.962 22.550 1.00 11.86 C ANISOU 2200 CD1 ILE A 151 1532 1499 1472 -93 39 147 C ATOM 2201 N VAL A 152 -7.945 -2.223 24.235 1.00 9.78 N ANISOU 2201 N VAL A 152 1254 1183 1278 41 47 -12 N ATOM 2202 CA VAL A 152 -6.938 -1.378 23.591 1.00 10.18 C ANISOU 2202 CA VAL A 152 1320 1207 1339 -2 55 -8 C ATOM 2203 C VAL A 152 -7.206 -1.318 22.096 1.00 11.00 C ANISOU 2203 C VAL A 152 1442 1331 1404 -34 106 4 C ATOM 2204 O VAL A 152 -7.489 -2.336 21.455 1.00 10.09 O ANISOU 2204 O VAL A 152 1511 1090 1231 -226 68 -87 O ATOM 2205 CB VAL A 152 -5.509 -1.895 23.894 1.00 10.07 C ANISOU 2205 CB VAL A 152 1308 1188 1329 -30 69 -7 C ATOM 2206 CG1 VAL A 152 -4.420 -1.114 23.108 1.00 10.91 C ANISOU 2206 CG1 VAL A 152 1273 1261 1609 56 28 -48 C ATOM 2207 CG2 VAL A 152 -5.258 -1.811 25.368 1.00 11.95 C ANISOU 2207 CG2 VAL A 152 1430 1471 1640 64 35 28 C ATOM 2208 N LEU A 153 -7.158 -0.106 21.552 1.00 11.57 N ANISOU 2208 N LEU A 153 1538 1400 1457 52 50 43 N ATOM 2209 CA LEU A 153 -7.026 0.074 20.118 1.00 12.58 C ANISOU 2209 CA LEU A 153 1644 1579 1554 34 9 16 C ATOM 2210 C LEU A 153 -5.590 0.468 19.843 1.00 12.53 C ANISOU 2210 C LEU A 153 1600 1586 1574 60 0 8 C ATOM 2211 O LEU A 153 -5.158 1.580 20.190 1.00 12.17 O ANISOU 2211 O LEU A 153 1584 1481 1559 124 74 -29 O ATOM 2212 CB LEU A 153 -7.985 1.157 19.619 1.00 12.82 C ANISOU 2212 CB LEU A 153 1718 1596 1555 -1 0 77 C ATOM 2213 CG LEU A 153 -7.866 1.476 18.120 1.00 15.95 C ANISOU 2213 CG LEU A 153 2116 1951 1993 111 -66 0 C ATOM 2214 CD1 LEU A 153 -8.447 0.381 17.316 1.00 15.54 C ANISOU 2214 CD1 LEU A 153 2173 1899 1831 -8 -15 -32 C ATOM 2215 CD2 LEU A 153 -8.566 2.794 17.804 1.00 18.87 C ANISOU 2215 CD2 LEU A 153 2519 2307 2341 122 -191 56 C ATOM 2216 N ASP A 154 -4.843 -0.460 19.247 1.00 12.80 N ANISOU 2216 N ASP A 154 1679 1606 1577 12 -17 -50 N ATOM 2217 CA ASP A 154 -3.426 -0.263 18.935 1.00 13.04 C ANISOU 2217 CA ASP A 154 1651 1674 1627 3 26 -13 C ATOM 2218 C ASP A 154 -3.307 -0.186 17.426 1.00 12.47 C ANISOU 2218 C ASP A 154 1634 1578 1525 -15 9 25 C ATOM 2219 O ASP A 154 -3.651 -1.143 16.743 1.00 13.26 O ANISOU 2219 O ASP A 154 1898 1638 1503 -11 118 29 O ATOM 2220 CB ASP A 154 -2.561 -1.423 19.508 1.00 13.06 C ANISOU 2220 CB ASP A 154 1670 1680 1612 31 54 72 C ATOM 2221 CG ASP A 154 -1.047 -1.067 19.600 1.00 16.45 C ANISOU 2221 CG ASP A 154 2179 1881 2191 130 -48 129 C ATOM 2222 OD1 ASP A 154 -0.177 -1.986 19.651 1.00 18.76 O ANISOU 2222 OD1 ASP A 154 2221 2254 2652 446 -13 377 O ATOM 2223 OD2 ASP A 154 -0.616 0.112 19.636 1.00 20.70 O ANISOU 2223 OD2 ASP A 154 2574 2082 3208 42 43 157 O ATOM 2224 N SER A 155 -2.891 0.963 16.898 1.00 12.29 N ANISOU 2224 N SER A 155 1523 1583 1562 -51 11 -42 N ATOM 2225 CA SER A 155 -2.795 1.179 15.447 1.00 11.07 C ANISOU 2225 CA SER A 155 1427 1454 1322 -19 -42 -31 C ATOM 2226 C SER A 155 -1.465 1.849 15.134 1.00 10.76 C ANISOU 2226 C SER A 155 1456 1393 1236 14 -44 -46 C ATOM 2227 O SER A 155 -1.210 2.956 15.587 1.00 10.51 O ANISOU 2227 O SER A 155 1436 1458 1097 63 -117 -111 O ATOM 2228 CB SER A 155 -3.945 2.068 14.991 1.00 12.06 C ANISOU 2228 CB SER A 155 1607 1509 1465 -125 -30 -53 C ATOM 2229 OG SER A 155 -3.991 2.220 13.577 1.00 13.24 O ANISOU 2229 OG SER A 155 1639 1879 1511 -4 -69 -15 O ATOM 2230 N GLY A 156 -0.610 1.162 14.377 1.00 10.06 N ANISOU 2230 N GLY A 156 1345 1294 1183 71 -92 -84 N ATOM 2231 CA GLY A 156 0.681 1.669 13.975 1.00 9.36 C ANISOU 2231 CA GLY A 156 1199 1193 1162 -3 -49 -24 C ATOM 2232 C GLY A 156 0.801 1.979 12.493 1.00 10.34 C ANISOU 2232 C GLY A 156 1291 1332 1304 35 -53 -62 C ATOM 2233 O GLY A 156 -0.114 2.530 11.893 1.00 10.63 O ANISOU 2233 O GLY A 156 1352 1460 1223 151 -41 37 O ATOM 2234 N ASP A 157 1.950 1.660 11.901 1.00 10.75 N ANISOU 2234 N ASP A 157 1380 1362 1342 16 -58 -41 N ATOM 2235 CA ASP A 157 2.170 1.888 10.480 1.00 10.76 C ANISOU 2235 CA ASP A 157 1403 1302 1381 -13 -19 -48 C ATOM 2236 C ASP A 157 1.663 0.738 9.604 1.00 10.71 C ANISOU 2236 C ASP A 157 1443 1289 1334 0 -89 -46 C ATOM 2237 O ASP A 157 1.350 0.947 8.421 1.00 9.58 O ANISOU 2237 O ASP A 157 1377 1106 1155 55 -124 -81 O ATOM 2238 CB ASP A 157 3.652 2.084 10.221 1.00 11.65 C ANISOU 2238 CB ASP A 157 1538 1377 1510 -14 -35 -34 C ATOM 2239 CG ASP A 157 3.934 2.611 8.824 1.00 13.16 C ANISOU 2239 CG ASP A 157 1683 1559 1756 -47 57 -19 C ATOM 2240 OD1 ASP A 157 3.385 3.669 8.434 1.00 15.78 O ANISOU 2240 OD1 ASP A 157 1512 1889 2592 -199 -12 15 O ATOM 2241 OD2 ASP A 157 4.697 2.028 8.048 1.00 16.04 O ANISOU 2241 OD2 ASP A 157 2025 1825 2242 22 223 -77 O ATOM 2242 N GLY A 158 1.612 -0.461 10.191 1.00 9.69 N ANISOU 2242 N GLY A 158 1262 1222 1196 -27 -81 -6 N ATOM 2243 CA GLY A 158 1.376 -1.705 9.476 1.00 9.83 C ANISOU 2243 CA GLY A 158 1270 1194 1270 40 -48 39 C ATOM 2244 C GLY A 158 0.083 -2.435 9.836 1.00 9.56 C ANISOU 2244 C GLY A 158 1274 1121 1234 36 -54 75 C ATOM 2245 O GLY A 158 -0.495 -3.138 9.002 1.00 10.15 O ANISOU 2245 O GLY A 158 1421 1088 1346 132 -134 106 O ATOM 2246 N VAL A 159 -0.385 -2.284 11.069 1.00 9.43 N ANISOU 2246 N VAL A 159 1188 1119 1273 76 -35 21 N ATOM 2247 CA VAL A 159 -1.529 -3.071 11.506 1.00 9.28 C ANISOU 2247 CA VAL A 159 1233 1099 1193 -5 -38 30 C ATOM 2248 C VAL A 159 -2.323 -2.405 12.603 1.00 8.69 C ANISOU 2248 C VAL A 159 1136 1071 1093 -14 -41 74 C ATOM 2249 O VAL A 159 -1.806 -1.589 13.345 1.00 8.14 O ANISOU 2249 O VAL A 159 1070 1115 906 16 -144 -7 O ATOM 2250 CB VAL A 159 -1.078 -4.476 11.913 1.00 10.10 C ANISOU 2250 CB VAL A 159 1297 1230 1307 -28 -21 23 C ATOM 2251 CG1 VAL A 159 -0.266 -4.456 13.206 1.00 10.42 C ANISOU 2251 CG1 VAL A 159 1452 1197 1309 -36 -60 23 C ATOM 2252 CG2 VAL A 159 -2.289 -5.429 12.019 1.00 11.26 C ANISOU 2252 CG2 VAL A 159 1282 1417 1578 -26 72 -12 C ATOM 2253 N THR A 160 -3.606 -2.711 12.661 1.00 8.92 N ANISOU 2253 N THR A 160 1202 1068 1120 -89 -98 -5 N ATOM 2254 CA THR A 160 -4.481 -2.232 13.736 1.00 9.37 C ANISOU 2254 CA THR A 160 1197 1166 1196 -43 -87 36 C ATOM 2255 C THR A 160 -5.110 -3.435 14.472 1.00 9.06 C ANISOU 2255 C THR A 160 1224 1076 1143 -51 -63 33 C ATOM 2256 O THR A 160 -5.572 -4.393 13.834 1.00 9.01 O ANISOU 2256 O THR A 160 1259 994 1168 -186 -96 144 O ATOM 2257 CB THR A 160 -5.575 -1.302 13.142 1.00 10.11 C ANISOU 2257 CB THR A 160 1352 1221 1267 -93 -68 30 C ATOM 2258 OG1 THR A 160 -4.973 -0.132 12.574 1.00 11.95 O ANISOU 2258 OG1 THR A 160 1547 1491 1502 -196 -392 447 O ATOM 2259 CG2 THR A 160 -6.479 -0.751 14.220 1.00 10.10 C ANISOU 2259 CG2 THR A 160 1218 1298 1319 85 -116 -52 C ATOM 2260 N HIS A 161 -5.138 -3.387 15.800 1.00 8.62 N ANISOU 2260 N HIS A 161 1154 1039 1080 -18 -49 2 N ATOM 2261 CA HIS A 161 -5.832 -4.399 16.595 1.00 9.25 C ANISOU 2261 CA HIS A 161 1163 1180 1169 -47 -44 -46 C ATOM 2262 C HIS A 161 -6.782 -3.806 17.631 1.00 9.18 C ANISOU 2262 C HIS A 161 1153 1196 1138 -50 -21 -26 C ATOM 2263 O HIS A 161 -6.507 -2.762 18.223 1.00 9.45 O ANISOU 2263 O HIS A 161 1161 1327 1103 -134 -64 -52 O ATOM 2264 CB HIS A 161 -4.855 -5.257 17.390 1.00 9.06 C ANISOU 2264 CB HIS A 161 1126 1251 1064 0 -54 -39 C ATOM 2265 CG HIS A 161 -4.032 -6.195 16.571 1.00 11.15 C ANISOU 2265 CG HIS A 161 1227 1492 1517 -69 -230 -140 C ATOM 2266 ND1 HIS A 161 -2.713 -5.948 16.284 1.00 13.23 N ANISOU 2266 ND1 HIS A 161 1214 1729 2084 0 -87 -161 N ATOM 2267 CD2 HIS A 161 -4.328 -7.377 15.983 1.00 14.47 C ANISOU 2267 CD2 HIS A 161 1400 1819 2279 5 75 75 C ATOM 2268 CE1 HIS A 161 -2.225 -6.941 15.566 1.00 14.13 C ANISOU 2268 CE1 HIS A 161 1419 1804 2144 -86 -72 -160 C ATOM 2269 NE2 HIS A 161 -3.190 -7.815 15.356 1.00 14.60 N ANISOU 2269 NE2 HIS A 161 1541 1736 2269 156 -208 145 N ATOM 2270 N ASN A 162 -7.879 -4.506 17.880 1.00 9.58 N ANISOU 2270 N ASN A 162 1216 1239 1185 -87 -90 -26 N ATOM 2271 CA ASN A 162 -8.672 -4.314 19.090 1.00 9.66 C ANISOU 2271 CA ASN A 162 1253 1260 1155 -55 -19 -7 C ATOM 2272 C ASN A 162 -8.323 -5.493 20.014 1.00 9.45 C ANISOU 2272 C ASN A 162 1279 1158 1154 -68 -50 21 C ATOM 2273 O ASN A 162 -8.488 -6.656 19.629 1.00 9.82 O ANISOU 2273 O ASN A 162 1218 1399 1113 -96 -103 94 O ATOM 2274 CB ASN A 162 -10.168 -4.324 18.806 1.00 10.45 C ANISOU 2274 CB ASN A 162 1373 1386 1208 -52 -50 44 C ATOM 2275 CG ASN A 162 -10.594 -3.297 17.775 1.00 12.98 C ANISOU 2275 CG ASN A 162 1737 1492 1702 -100 55 -5 C ATOM 2276 OD1 ASN A 162 -10.854 -3.623 16.615 1.00 18.20 O ANISOU 2276 OD1 ASN A 162 2232 2494 2189 -117 88 610 O ATOM 2277 ND2 ASN A 162 -10.700 -2.076 18.192 1.00 18.01 N ANISOU 2277 ND2 ASN A 162 2230 1993 2618 243 230 -157 N ATOM 2278 N VAL A 163 -7.808 -5.203 21.205 1.00 9.12 N ANISOU 2278 N VAL A 163 1217 1068 1179 -49 -42 38 N ATOM 2279 CA VAL A 163 -7.407 -6.231 22.158 1.00 9.13 C ANISOU 2279 CA VAL A 163 1107 1157 1202 20 -32 28 C ATOM 2280 C VAL A 163 -8.121 -6.066 23.494 1.00 8.90 C ANISOU 2280 C VAL A 163 1124 1081 1173 -22 -60 18 C ATOM 2281 O VAL A 163 -7.734 -5.241 24.303 1.00 8.38 O ANISOU 2281 O VAL A 163 1088 928 1168 -20 -130 -37 O ATOM 2282 CB VAL A 163 -5.870 -6.219 22.394 1.00 9.24 C ANISOU 2282 CB VAL A 163 1216 1162 1131 0 -30 8 C ATOM 2283 CG1 VAL A 163 -5.471 -7.427 23.223 1.00 9.47 C ANISOU 2283 CG1 VAL A 163 943 1243 1411 128 -4 56 C ATOM 2284 CG2 VAL A 163 -5.129 -6.202 21.055 1.00 10.55 C ANISOU 2284 CG2 VAL A 163 1130 1373 1502 9 62 25 C ATOM 2285 N PRO A 164 -9.173 -6.843 23.747 1.00 8.45 N ANISOU 2285 N PRO A 164 1051 1039 1120 -20 -51 19 N ATOM 2286 CA PRO A 164 -9.806 -6.793 25.066 1.00 8.24 C ANISOU 2286 CA PRO A 164 1061 1007 1060 -5 -20 9 C ATOM 2287 C PRO A 164 -8.998 -7.593 26.104 1.00 7.64 C ANISOU 2287 C PRO A 164 1030 927 945 43 -16 0 C ATOM 2288 O PRO A 164 -8.456 -8.642 25.831 1.00 8.04 O ANISOU 2288 O PRO A 164 1166 930 957 7 -69 40 O ATOM 2289 CB PRO A 164 -11.224 -7.343 24.812 1.00 8.54 C ANISOU 2289 CB PRO A 164 1142 1050 1052 21 10 33 C ATOM 2290 CG PRO A 164 -11.088 -8.216 23.634 1.00 8.84 C ANISOU 2290 CG PRO A 164 1135 1038 1184 -95 -32 -71 C ATOM 2291 CD PRO A 164 -9.877 -7.747 22.820 1.00 8.41 C ANISOU 2291 CD PRO A 164 1107 938 1147 4 9 33 C ATOM 2292 N ILE A 165 -8.894 -7.037 27.291 1.00 7.62 N ANISOU 2292 N ILE A 165 977 920 997 25 -25 18 N ATOM 2293 CA ILE A 165 -8.023 -7.533 28.351 1.00 7.19 C ANISOU 2293 CA ILE A 165 938 843 950 49 5 0 C ATOM 2294 C ILE A 165 -8.791 -7.524 29.670 1.00 7.29 C ANISOU 2294 C ILE A 165 948 871 948 35 42 10 C ATOM 2295 O ILE A 165 -9.471 -6.544 30.003 1.00 6.55 O ANISOU 2295 O ILE A 165 877 734 875 -14 71 0 O ATOM 2296 CB ILE A 165 -6.746 -6.632 28.448 1.00 6.88 C ANISOU 2296 CB ILE A 165 837 860 915 63 -12 -40 C ATOM 2297 CG1 ILE A 165 -5.960 -6.664 27.149 1.00 6.59 C ANISOU 2297 CG1 ILE A 165 802 894 808 -57 -158 60 C ATOM 2298 CG2 ILE A 165 -5.846 -7.044 29.616 1.00 7.50 C ANISOU 2298 CG2 ILE A 165 1068 899 882 106 139 -26 C ATOM 2299 CD1 ILE A 165 -5.062 -5.452 26.943 1.00 8.04 C ANISOU 2299 CD1 ILE A 165 971 870 1213 -106 0 29 C ATOM 2300 N TYR A 166 -8.676 -8.618 30.415 1.00 7.53 N ANISOU 2300 N TYR A 166 1013 846 1002 -10 71 -52 N ATOM 2301 CA TYR A 166 -9.341 -8.761 31.692 1.00 8.38 C ANISOU 2301 CA TYR A 166 1090 1005 1088 -40 42 -37 C ATOM 2302 C TYR A 166 -8.382 -9.250 32.753 1.00 7.92 C ANISOU 2302 C TYR A 166 1029 952 1024 -55 67 -45 C ATOM 2303 O TYR A 166 -7.773 -10.294 32.597 1.00 6.61 O ANISOU 2303 O TYR A 166 979 755 776 -51 154 -161 O ATOM 2304 CB TYR A 166 -10.529 -9.734 31.586 1.00 8.87 C ANISOU 2304 CB TYR A 166 1157 1082 1128 -60 -6 -42 C ATOM 2305 CG TYR A 166 -11.336 -9.840 32.866 1.00 11.95 C ANISOU 2305 CG TYR A 166 1531 1499 1510 -84 26 -18 C ATOM 2306 CD1 TYR A 166 -11.241 -10.970 33.687 1.00 16.44 C ANISOU 2306 CD1 TYR A 166 2029 2245 1969 -6 19 -35 C ATOM 2307 CD2 TYR A 166 -12.189 -8.810 33.265 1.00 13.05 C ANISOU 2307 CD2 TYR A 166 1541 1728 1687 -128 -60 -91 C ATOM 2308 CE1 TYR A 166 -11.992 -11.072 34.875 1.00 17.16 C ANISOU 2308 CE1 TYR A 166 2032 2456 2032 -155 -128 -121 C ATOM 2309 CE2 TYR A 166 -12.932 -8.906 34.446 1.00 14.97 C ANISOU 2309 CE2 TYR A 166 1812 2017 1856 -140 -307 -193 C ATOM 2310 CZ TYR A 166 -12.831 -10.029 35.235 1.00 16.40 C ANISOU 2310 CZ TYR A 166 1849 2469 1911 -243 -162 -261 C ATOM 2311 OH TYR A 166 -13.571 -10.102 36.384 1.00 19.54 O ANISOU 2311 OH TYR A 166 1730 3306 2386 -338 -347 -391 O ATOM 2312 N GLU A 167 -8.264 -8.484 33.841 1.00 7.78 N ANISOU 2312 N GLU A 167 1021 894 1039 -67 54 -88 N ATOM 2313 CA GLU A 167 -7.444 -8.840 34.983 1.00 7.79 C ANISOU 2313 CA GLU A 167 982 943 1032 -51 7 -47 C ATOM 2314 C GLU A 167 -6.004 -9.233 34.551 1.00 7.71 C ANISOU 2314 C GLU A 167 999 901 1028 -23 -10 -103 C ATOM 2315 O GLU A 167 -5.402 -10.171 35.063 1.00 7.08 O ANISOU 2315 O GLU A 167 723 948 1017 -25 -177 -127 O ATOM 2316 CB GLU A 167 -8.144 -9.882 35.889 1.00 8.57 C ANISOU 2316 CB GLU A 167 1042 1039 1173 -1 34 -82 C ATOM 2317 CG GLU A 167 -9.328 -9.314 36.685 1.00 8.62 C ANISOU 2317 CG GLU A 167 1130 1081 1062 -92 93 -110 C ATOM 2318 CD GLU A 167 -9.787 -10.164 37.889 1.00 9.84 C ANISOU 2318 CD GLU A 167 1201 1236 1301 -69 54 -98 C ATOM 2319 OE1 GLU A 167 -9.348 -11.342 38.066 1.00 8.86 O ANISOU 2319 OE1 GLU A 167 1112 1064 1187 -151 63 -329 O ATOM 2320 OE2 GLU A 167 -10.619 -9.635 38.675 1.00 8.34 O ANISOU 2320 OE2 GLU A 167 787 1168 1211 -162 -38 -188 O ATOM 2321 N GLY A 168 -5.485 -8.460 33.600 1.00 7.78 N ANISOU 2321 N GLY A 168 992 951 1013 -28 -10 -66 N ATOM 2322 CA GLY A 168 -4.106 -8.522 33.166 1.00 8.29 C ANISOU 2322 CA GLY A 168 1010 1026 1114 0 -29 -91 C ATOM 2323 C GLY A 168 -3.854 -9.259 31.871 1.00 8.93 C ANISOU 2323 C GLY A 168 1069 1137 1184 -8 5 -64 C ATOM 2324 O GLY A 168 -2.754 -9.166 31.328 1.00 9.38 O ANISOU 2324 O GLY A 168 946 1159 1458 48 37 -238 O ATOM 2325 N TYR A 169 -4.853 -9.961 31.345 1.00 9.16 N ANISOU 2325 N TYR A 169 1058 1193 1227 -23 -41 -57 N ATOM 2326 CA TYR A 169 -4.611 -10.875 30.229 1.00 9.19 C ANISOU 2326 CA TYR A 169 1098 1216 1176 23 -27 -15 C ATOM 2327 C TYR A 169 -5.588 -10.687 29.103 1.00 9.21 C ANISOU 2327 C TYR A 169 1137 1188 1172 13 -14 26 C ATOM 2328 O TYR A 169 -6.801 -10.580 29.313 1.00 8.77 O ANISOU 2328 O TYR A 169 1072 1159 1102 20 -90 81 O ATOM 2329 CB TYR A 169 -4.683 -12.313 30.723 1.00 9.90 C ANISOU 2329 CB TYR A 169 1195 1344 1221 31 -13 7 C ATOM 2330 CG TYR A 169 -3.574 -12.611 31.700 1.00 11.57 C ANISOU 2330 CG TYR A 169 1365 1632 1398 72 -83 4 C ATOM 2331 CD1 TYR A 169 -3.813 -12.664 33.072 1.00 11.49 C ANISOU 2331 CD1 TYR A 169 1586 1467 1310 176 33 -8 C ATOM 2332 CD2 TYR A 169 -2.279 -12.810 31.243 1.00 15.91 C ANISOU 2332 CD2 TYR A 169 1941 2371 1732 58 -141 224 C ATOM 2333 CE1 TYR A 169 -2.767 -12.892 33.968 1.00 13.97 C ANISOU 2333 CE1 TYR A 169 1813 1922 1571 260 123 7 C ATOM 2334 CE2 TYR A 169 -1.227 -13.054 32.121 1.00 18.25 C ANISOU 2334 CE2 TYR A 169 2145 2872 1914 38 -50 200 C ATOM 2335 CZ TYR A 169 -1.474 -13.093 33.480 1.00 17.92 C ANISOU 2335 CZ TYR A 169 2134 2886 1785 87 -54 187 C ATOM 2336 OH TYR A 169 -0.409 -13.343 34.318 1.00 19.22 O ANISOU 2336 OH TYR A 169 2117 3441 1742 301 31 388 O ATOM 2337 N ALA A 170 -5.052 -10.664 27.901 1.00 9.51 N ANISOU 2337 N ALA A 170 1130 1259 1222 30 -40 -8 N ATOM 2338 CA ALA A 170 -5.841 -10.583 26.682 1.00 10.47 C ANISOU 2338 CA ALA A 170 1297 1376 1305 31 -9 20 C ATOM 2339 C ALA A 170 -6.773 -11.772 26.556 1.00 10.88 C ANISOU 2339 C ALA A 170 1396 1375 1362 22 -57 0 C ATOM 2340 O ALA A 170 -6.462 -12.874 27.041 1.00 11.30 O ANISOU 2340 O ALA A 170 1379 1525 1389 25 -94 65 O ATOM 2341 CB ALA A 170 -4.927 -10.512 25.501 1.00 10.91 C ANISOU 2341 CB ALA A 170 1420 1497 1225 52 -68 -1 C ATOM 2342 N LEU A 171 -7.927 -11.528 25.938 1.00 11.46 N ANISOU 2342 N LEU A 171 1527 1401 1426 26 -39 42 N ATOM 2343 CA LEU A 171 -8.920 -12.548 25.622 1.00 12.11 C ANISOU 2343 CA LEU A 171 1570 1503 1527 13 -29 21 C ATOM 2344 C LEU A 171 -8.742 -12.903 24.136 1.00 12.34 C ANISOU 2344 C LEU A 171 1634 1508 1547 34 -23 -52 C ATOM 2345 O LEU A 171 -9.255 -12.196 23.272 1.00 12.62 O ANISOU 2345 O LEU A 171 1733 1413 1649 15 -47 -168 O ATOM 2346 CB LEU A 171 -10.323 -11.990 25.917 1.00 12.08 C ANISOU 2346 CB LEU A 171 1632 1467 1490 -16 -43 -30 C ATOM 2347 CG LEU A 171 -10.554 -11.566 27.369 1.00 15.21 C ANISOU 2347 CG LEU A 171 1966 1844 1969 110 97 121 C ATOM 2348 CD1 LEU A 171 -11.665 -10.534 27.491 1.00 18.71 C ANISOU 2348 CD1 LEU A 171 2422 2482 2204 175 47 116 C ATOM 2349 CD2 LEU A 171 -10.900 -12.733 28.214 1.00 18.84 C ANISOU 2349 CD2 LEU A 171 2420 2317 2417 75 83 -46 C ATOM 2350 N PRO A 172 -7.991 -13.960 23.817 1.00 13.48 N ANISOU 2350 N PRO A 172 1804 1656 1659 34 -12 -18 N ATOM 2351 CA PRO A 172 -7.592 -14.226 22.418 1.00 13.96 C ANISOU 2351 CA PRO A 172 1867 1735 1700 63 -23 -21 C ATOM 2352 C PRO A 172 -8.758 -14.365 21.425 1.00 13.96 C ANISOU 2352 C PRO A 172 1843 1733 1727 17 -39 -27 C ATOM 2353 O PRO A 172 -8.679 -13.834 20.328 1.00 12.06 O ANISOU 2353 O PRO A 172 1852 1458 1270 -14 -113 -105 O ATOM 2354 CB PRO A 172 -6.826 -15.571 22.493 1.00 14.47 C ANISOU 2354 CB PRO A 172 1939 1841 1715 91 -56 -9 C ATOM 2355 CG PRO A 172 -6.506 -15.785 23.923 1.00 15.51 C ANISOU 2355 CG PRO A 172 2030 1994 1870 112 2 23 C ATOM 2356 CD PRO A 172 -7.468 -14.979 24.739 1.00 14.08 C ANISOU 2356 CD PRO A 172 1852 1805 1692 120 15 -76 C ATOM 2357 N HIS A 173 -9.811 -15.073 21.822 1.00 14.21 N ANISOU 2357 N HIS A 173 1840 1747 1811 -23 -7 37 N ATOM 2358 CA HIS A 173 -10.983 -15.315 20.980 1.00 14.87 C ANISOU 2358 CA HIS A 173 1848 1893 1906 -33 -11 2 C ATOM 2359 C HIS A 173 -11.664 -13.999 20.532 1.00 13.91 C ANISOU 2359 C HIS A 173 1697 1816 1771 -51 -6 5 C ATOM 2360 O HIS A 173 -12.313 -13.952 19.493 1.00 13.13 O ANISOU 2360 O HIS A 173 1544 1867 1576 -115 -116 -28 O ATOM 2361 CB HIS A 173 -11.999 -16.202 21.750 1.00 16.21 C ANISOU 2361 CB HIS A 173 1975 2041 2140 -41 -2 -23 C ATOM 2362 CG HIS A 173 -12.889 -15.422 22.664 1.00 19.89 C ANISOU 2362 CG HIS A 173 2290 2517 2748 -35 67 -195 C ATOM 2363 ND1 HIS A 173 -12.416 -14.779 23.789 1.00 26.21 N ANISOU 2363 ND1 HIS A 173 2895 3585 3479 209 -87 -168 N ATOM 2364 CD2 HIS A 173 -14.209 -15.115 22.584 1.00 25.50 C ANISOU 2364 CD2 HIS A 173 2973 3291 3425 -35 57 -118 C ATOM 2365 CE1 HIS A 173 -13.406 -14.123 24.374 1.00 27.10 C ANISOU 2365 CE1 HIS A 173 3098 3736 3462 -10 33 -222 C ATOM 2366 NE2 HIS A 173 -14.506 -14.311 23.665 1.00 25.29 N ANISOU 2366 NE2 HIS A 173 2771 3346 3492 -90 80 -296 N ATOM 2367 N ALA A 174 -11.511 -12.938 21.322 1.00 12.80 N ANISOU 2367 N ALA A 174 1534 1682 1645 -26 -15 -17 N ATOM 2368 CA ALA A 174 -12.116 -11.629 21.027 1.00 12.74 C ANISOU 2368 CA ALA A 174 1583 1637 1618 -15 -11 16 C ATOM 2369 C ALA A 174 -11.227 -10.579 20.318 1.00 11.91 C ANISOU 2369 C ALA A 174 1407 1590 1528 -37 25 18 C ATOM 2370 O ALA A 174 -11.698 -9.494 19.988 1.00 10.45 O ANISOU 2370 O ALA A 174 1122 1398 1447 -81 33 37 O ATOM 2371 CB ALA A 174 -12.703 -11.030 22.316 1.00 12.61 C ANISOU 2371 CB ALA A 174 1662 1596 1531 47 46 40 C ATOM 2372 N ILE A 175 -9.956 -10.892 20.090 1.00 12.48 N ANISOU 2372 N ILE A 175 1539 1611 1591 10 17 -2 N ATOM 2373 CA ILE A 175 -9.051 -9.977 19.382 1.00 12.19 C ANISOU 2373 CA ILE A 175 1504 1515 1611 -37 14 26 C ATOM 2374 C ILE A 175 -9.449 -9.804 17.916 1.00 12.72 C ANISOU 2374 C ILE A 175 1623 1577 1633 -16 42 9 C ATOM 2375 O ILE A 175 -9.756 -10.781 17.233 1.00 12.10 O ANISOU 2375 O ILE A 175 1507 1381 1707 -120 48 16 O ATOM 2376 CB ILE A 175 -7.581 -10.474 19.478 1.00 12.44 C ANISOU 2376 CB ILE A 175 1575 1524 1625 16 43 3 C ATOM 2377 CG1 ILE A 175 -7.079 -10.437 20.923 1.00 11.85 C ANISOU 2377 CG1 ILE A 175 1406 1497 1599 -42 -52 45 C ATOM 2378 CG2 ILE A 175 -6.650 -9.636 18.597 1.00 11.90 C ANISOU 2378 CG2 ILE A 175 1394 1537 1587 -11 112 231 C ATOM 2379 CD1 ILE A 175 -5.730 -11.169 21.123 1.00 12.32 C ANISOU 2379 CD1 ILE A 175 1642 1419 1618 25 -21 50 C ATOM 2380 N MET A 176 -9.477 -8.555 17.444 1.00 13.84 N ANISOU 2380 N MET A 176 1749 1777 1732 -93 47 -17 N ATOM 2381 CA MET A 176 -9.697 -8.251 16.018 1.00 15.03 C ANISOU 2381 CA MET A 176 1897 1922 1891 -43 30 24 C ATOM 2382 C MET A 176 -8.435 -7.672 15.421 1.00 14.76 C ANISOU 2382 C MET A 176 1842 1912 1853 -74 29 39 C ATOM 2383 O MET A 176 -7.797 -6.821 16.023 1.00 14.70 O ANISOU 2383 O MET A 176 1886 1938 1759 -161 161 61 O ATOM 2384 CB MET A 176 -10.817 -7.228 15.811 1.00 15.36 C ANISOU 2384 CB MET A 176 1910 1955 1970 -60 103 25 C ATOM 2385 CG MET A 176 -12.102 -7.563 16.521 1.00 18.80 C ANISOU 2385 CG MET A 176 2379 2333 2428 -36 -7 -57 C ATOM 2386 SD MET A 176 -13.042 -8.813 15.664 1.00 23.23 S ANISOU 2386 SD MET A 176 2759 2830 3236 -348 131 22 S ATOM 2387 CE MET A 176 -14.015 -9.480 17.058 1.00 24.85 C ANISOU 2387 CE MET A 176 3147 3060 3233 26 174 30 C ATOM 2388 N ARG A 177 -8.085 -8.138 14.233 1.00 15.46 N ANISOU 2388 N ARG A 177 1911 1990 1972 -104 -7 10 N ATOM 2389 CA ARG A 177 -6.954 -7.612 13.489 1.00 16.42 C ANISOU 2389 CA ARG A 177 2070 2126 2041 -91 -25 -17 C ATOM 2390 C ARG A 177 -7.482 -6.962 12.224 1.00 16.66 C ANISOU 2390 C ARG A 177 2088 2177 2062 -125 12 0 C ATOM 2391 O ARG A 177 -8.266 -7.571 11.512 1.00 15.48 O ANISOU 2391 O ARG A 177 1936 2085 1860 -416 -97 -40 O ATOM 2392 CB ARG A 177 -5.990 -8.745 13.139 1.00 17.45 C ANISOU 2392 CB ARG A 177 2165 2265 2199 -90 -39 0 C ATOM 2393 CG ARG A 177 -4.716 -8.260 12.453 1.00 19.53 C ANISOU 2393 CG ARG A 177 2482 2578 2358 -122 -50 -25 C ATOM 2394 CD ARG A 177 -4.360 -8.945 11.194 1.00 25.42 C ANISOU 2394 CD ARG A 177 3108 3112 3438 63 -199 39 C ATOM 2395 NE ARG A 177 -3.045 -9.550 11.290 1.00 29.63 N ANISOU 2395 NE ARG A 177 3487 3661 4108 38 -250 32 N ATOM 2396 CZ ARG A 177 -2.182 -9.712 10.290 1.00 29.20 C ANISOU 2396 CZ ARG A 177 3662 3860 3570 -61 -95 64 C ATOM 2397 NH1 ARG A 177 -2.428 -9.274 9.075 1.00 30.57 N ANISOU 2397 NH1 ARG A 177 3902 3580 4132 -57 -453 64 N ATOM 2398 NH2 ARG A 177 -1.032 -10.310 10.528 1.00 30.91 N ANISOU 2398 NH2 ARG A 177 3810 4082 3851 136 -4 151 N ATOM 2399 N LEU A 178 -7.048 -5.732 11.950 1.00 16.65 N ANISOU 2399 N LEU A 178 2079 2136 2111 -116 20 -35 N ATOM 2400 CA LEU A 178 -7.425 -4.984 10.746 1.00 17.88 C ANISOU 2400 CA LEU A 178 2225 2296 2270 -98 32 -26 C ATOM 2401 C LEU A 178 -6.131 -4.565 10.002 1.00 17.42 C ANISOU 2401 C LEU A 178 2151 2316 2150 -96 86 13 C ATOM 2402 O LEU A 178 -5.292 -3.879 10.591 1.00 15.27 O ANISOU 2402 O LEU A 178 1806 2208 1784 -235 199 112 O ATOM 2403 CB LEU A 178 -8.145 -3.711 11.193 1.00 18.85 C ANISOU 2403 CB LEU A 178 2219 2462 2482 -35 -29 -11 C ATOM 2404 CG LEU A 178 -9.542 -3.286 10.781 1.00 24.20 C ANISOU 2404 CG LEU A 178 3088 3069 3037 3 21 -71 C ATOM 2405 CD1 LEU A 178 -10.068 -2.282 11.822 1.00 26.59 C ANISOU 2405 CD1 LEU A 178 3338 3378 3384 12 87 -121 C ATOM 2406 CD2 LEU A 178 -9.524 -2.661 9.406 1.00 25.50 C ANISOU 2406 CD2 LEU A 178 3310 3188 3188 -62 102 191 C ATOM 2407 N ASP A 179 -5.969 -4.966 8.740 1.00 17.65 N ANISOU 2407 N ASP A 179 2194 2301 2210 -93 40 27 N ATOM 2408 CA ASP A 179 -4.824 -4.537 7.918 1.00 18.95 C ANISOU 2408 CA ASP A 179 2466 2435 2299 32 21 18 C ATOM 2409 C ASP A 179 -5.139 -3.220 7.212 1.00 19.11 C ANISOU 2409 C ASP A 179 2525 2432 2303 12 39 35 C ATOM 2410 O ASP A 179 -5.282 -3.164 5.978 1.00 20.89 O ANISOU 2410 O ASP A 179 2774 2740 2421 7 70 99 O ATOM 2411 CB ASP A 179 -4.482 -5.601 6.870 1.00 19.32 C ANISOU 2411 CB ASP A 179 2530 2399 2409 35 30 -20 C ATOM 2412 CG ASP A 179 -3.760 -6.780 7.461 1.00 21.52 C ANISOU 2412 CG ASP A 179 2975 2608 2591 155 50 -118 C ATOM 2413 OD1 ASP A 179 -3.644 -7.820 6.759 1.00 22.58 O ANISOU 2413 OD1 ASP A 179 3503 2593 2483 -191 377 -306 O ATOM 2414 OD2 ASP A 179 -3.275 -6.752 8.625 1.00 22.48 O ANISOU 2414 OD2 ASP A 179 3211 2313 3017 607 78 -293 O ATOM 2415 N LEU A 180 -5.341 -2.200 8.022 1.00 18.42 N ANISOU 2415 N LEU A 180 2426 2345 2227 -21 -20 37 N ATOM 2416 CA LEU A 180 -5.565 -0.831 7.602 1.00 17.91 C ANISOU 2416 CA LEU A 180 2269 2302 2232 -20 -22 3 C ATOM 2417 C LEU A 180 -4.875 -0.072 8.717 1.00 16.37 C ANISOU 2417 C LEU A 180 2067 2131 2020 -39 -38 0 C ATOM 2418 O LEU A 180 -5.308 -0.106 9.853 1.00 16.18 O ANISOU 2418 O LEU A 180 2003 2221 1923 -184 -170 56 O ATOM 2419 CB LEU A 180 -7.057 -0.493 7.553 1.00 18.67 C ANISOU 2419 CB LEU A 180 2421 2335 2336 16 -79 -25 C ATOM 2420 CG LEU A 180 -7.499 0.981 7.555 1.00 20.88 C ANISOU 2420 CG LEU A 180 2583 2672 2676 31 7 18 C ATOM 2421 CD1 LEU A 180 -6.641 1.880 6.712 1.00 23.02 C ANISOU 2421 CD1 LEU A 180 2859 2916 2971 75 -29 50 C ATOM 2422 CD2 LEU A 180 -8.921 1.077 7.068 1.00 22.83 C ANISOU 2422 CD2 LEU A 180 2898 2803 2974 -41 -167 -93 C ATOM 2423 N ALA A 181 -3.779 0.577 8.382 1.00 14.91 N ANISOU 2423 N ALA A 181 1845 1963 1857 -19 -31 25 N ATOM 2424 CA ALA A 181 -3.005 1.314 9.343 1.00 14.26 C ANISOU 2424 CA ALA A 181 1786 1810 1821 9 25 -13 C ATOM 2425 C ALA A 181 -2.268 2.470 8.653 1.00 14.26 C ANISOU 2425 C ALA A 181 1757 1823 1838 -3 31 -36 C ATOM 2426 O ALA A 181 -2.674 2.937 7.565 1.00 12.71 O ANISOU 2426 O ALA A 181 1517 1568 1742 51 118 -80 O ATOM 2427 CB ALA A 181 -2.059 0.353 10.078 1.00 14.21 C ANISOU 2427 CB ALA A 181 1679 1877 1842 -86 -27 -34 C ATOM 2428 N GLY A 182 -1.219 2.957 9.300 1.00 14.71 N ANISOU 2428 N GLY A 182 1832 1852 1903 0 39 33 N ATOM 2429 CA GLY A 182 -0.577 4.191 8.900 1.00 15.74 C ANISOU 2429 CA GLY A 182 1980 1964 2035 1 -8 0 C ATOM 2430 C GLY A 182 -0.108 4.227 7.465 1.00 15.59 C ANISOU 2430 C GLY A 182 1985 1962 1973 -9 15 13 C ATOM 2431 O GLY A 182 -0.319 5.218 6.785 1.00 16.34 O ANISOU 2431 O GLY A 182 2033 2054 2119 48 52 11 O ATOM 2432 N ARG A 183 0.502 3.147 6.991 1.00 16.48 N ANISOU 2432 N ARG A 183 2096 2108 2058 -13 -25 67 N ATOM 2433 CA ARG A 183 0.997 3.092 5.618 1.00 17.52 C ANISOU 2433 CA ARG A 183 2243 2205 2207 8 36 21 C ATOM 2434 C ARG A 183 -0.151 3.216 4.591 1.00 16.50 C ANISOU 2434 C ARG A 183 2079 2117 2072 3 33 35 C ATOM 2435 O ARG A 183 -0.013 3.888 3.582 1.00 15.88 O ANISOU 2435 O ARG A 183 1943 2051 2040 12 68 23 O ATOM 2436 CB ARG A 183 1.805 1.813 5.377 1.00 18.56 C ANISOU 2436 CB ARG A 183 2371 2370 2311 10 44 84 C ATOM 2437 CG ARG A 183 2.911 1.953 4.346 1.00 23.36 C ANISOU 2437 CG ARG A 183 3014 2843 3019 92 36 37 C ATOM 2438 CD ARG A 183 3.760 0.709 4.126 1.00 29.21 C ANISOU 2438 CD ARG A 183 3688 3771 3636 112 -36 51 C ATOM 2439 NE ARG A 183 4.489 0.371 5.346 1.00 33.04 N ANISOU 2439 NE ARG A 183 4106 4302 4143 134 -219 59 N ATOM 2440 CZ ARG A 183 5.686 -0.205 5.400 1.00 35.17 C ANISOU 2440 CZ ARG A 183 4324 4566 4472 23 -32 -15 C ATOM 2441 NH1 ARG A 183 6.334 -0.537 4.289 1.00 35.74 N ANISOU 2441 NH1 ARG A 183 4565 4646 4365 -10 -8 -140 N ATOM 2442 NH2 ARG A 183 6.234 -0.457 6.603 1.00 35.80 N ANISOU 2442 NH2 ARG A 183 4424 4575 4603 -66 -186 57 N ATOM 2443 N ASP A 184 -1.274 2.560 4.846 1.00 16.31 N ANISOU 2443 N ASP A 184 2142 2058 1995 26 59 19 N ATOM 2444 CA ASP A 184 -2.444 2.669 3.976 1.00 16.10 C ANISOU 2444 CA ASP A 184 2119 2045 1950 36 35 18 C ATOM 2445 C ASP A 184 -2.989 4.095 3.943 1.00 15.86 C ANISOU 2445 C ASP A 184 2075 2006 1944 32 20 -39 C ATOM 2446 O ASP A 184 -3.441 4.580 2.896 1.00 14.79 O ANISOU 2446 O ASP A 184 1992 1862 1762 115 70 29 O ATOM 2447 CB ASP A 184 -3.540 1.707 4.420 1.00 16.67 C ANISOU 2447 CB ASP A 184 2262 2043 2026 51 16 -12 C ATOM 2448 CG ASP A 184 -3.051 0.271 4.494 1.00 19.51 C ANISOU 2448 CG ASP A 184 2848 2363 2200 35 117 111 C ATOM 2449 OD1 ASP A 184 -3.066 -0.329 5.591 1.00 22.77 O ANISOU 2449 OD1 ASP A 184 3550 2570 2532 -254 474 604 O ATOM 2450 OD2 ASP A 184 -2.570 -0.317 3.511 1.00 21.25 O ANISOU 2450 OD2 ASP A 184 3672 2290 2109 -30 144 -38 O ATOM 2451 N LEU A 185 -2.937 4.764 5.087 1.00 15.74 N ANISOU 2451 N LEU A 185 2078 2013 1889 91 57 -49 N ATOM 2452 CA LEU A 185 -3.403 6.147 5.191 1.00 15.80 C ANISOU 2452 CA LEU A 185 2081 2000 1919 10 7 -39 C ATOM 2453 C LEU A 185 -2.482 7.064 4.405 1.00 14.83 C ANISOU 2453 C LEU A 185 1988 1884 1762 56 63 -86 C ATOM 2454 O LEU A 185 -2.946 7.911 3.646 1.00 13.48 O ANISOU 2454 O LEU A 185 1999 1536 1586 143 126 -66 O ATOM 2455 CB LEU A 185 -3.483 6.579 6.661 1.00 16.52 C ANISOU 2455 CB LEU A 185 2083 2130 2061 85 108 -75 C ATOM 2456 CG LEU A 185 -4.841 6.426 7.354 1.00 19.31 C ANISOU 2456 CG LEU A 185 2452 2420 2463 -82 50 12 C ATOM 2457 CD1 LEU A 185 -5.785 5.415 6.694 1.00 20.09 C ANISOU 2457 CD1 LEU A 185 2784 2394 2452 -191 139 -246 C ATOM 2458 CD2 LEU A 185 -4.657 6.145 8.806 1.00 19.34 C ANISOU 2458 CD2 LEU A 185 2496 2409 2441 -110 0 98 C ATOM 2459 N THR A 186 -1.180 6.866 4.558 1.00 13.74 N ANISOU 2459 N THR A 186 1798 1766 1653 52 -14 -81 N ATOM 2460 CA THR A 186 -0.219 7.603 3.755 1.00 13.87 C ANISOU 2460 CA THR A 186 1821 1716 1733 3 -12 -6 C ATOM 2461 C THR A 186 -0.449 7.421 2.246 1.00 13.99 C ANISOU 2461 C THR A 186 1875 1679 1761 -31 -36 -47 C ATOM 2462 O THR A 186 -0.440 8.398 1.485 1.00 12.94 O ANISOU 2462 O THR A 186 1899 1333 1682 -108 -44 -24 O ATOM 2463 CB THR A 186 1.224 7.216 4.152 1.00 14.22 C ANISOU 2463 CB THR A 186 1828 1816 1757 -46 -2 13 C ATOM 2464 OG1 THR A 186 1.501 7.720 5.468 1.00 13.58 O ANISOU 2464 OG1 THR A 186 1777 1837 1543 -90 -85 98 O ATOM 2465 CG2 THR A 186 2.277 7.905 3.225 1.00 14.54 C ANISOU 2465 CG2 THR A 186 1852 1857 1813 52 11 108 C ATOM 2466 N ASP A 187 -0.664 6.182 1.802 1.00 14.45 N ANISOU 2466 N ASP A 187 1946 1723 1820 -20 -21 -4 N ATOM 2467 CA ASP A 187 -0.851 5.917 0.361 1.00 14.83 C ANISOU 2467 CA ASP A 187 1969 1822 1844 10 -49 -10 C ATOM 2468 C ASP A 187 -2.136 6.592 -0.158 1.00 14.64 C ANISOU 2468 C ASP A 187 1928 1827 1806 -11 -32 -26 C ATOM 2469 O ASP A 187 -2.161 7.112 -1.260 1.00 14.25 O ANISOU 2469 O ASP A 187 2054 1735 1625 42 -62 118 O ATOM 2470 CB ASP A 187 -0.874 4.408 0.063 1.00 14.91 C ANISOU 2470 CB ASP A 187 1934 1890 1838 22 -59 -54 C ATOM 2471 CG ASP A 187 0.488 3.729 0.287 1.00 16.88 C ANISOU 2471 CG ASP A 187 2221 2044 2146 -10 14 20 C ATOM 2472 OD1 ASP A 187 1.528 4.421 0.366 1.00 19.27 O ANISOU 2472 OD1 ASP A 187 2139 2773 2408 68 -179 86 O ATOM 2473 OD2 ASP A 187 0.619 2.495 0.388 1.00 20.57 O ANISOU 2473 OD2 ASP A 187 2731 2591 2494 234 231 370 O ATOM 2474 N TYR A 188 -3.186 6.602 0.655 1.00 14.61 N ANISOU 2474 N TYR A 188 1917 1847 1787 8 10 -62 N ATOM 2475 CA TYR A 188 -4.465 7.196 0.278 1.00 14.33 C ANISOU 2475 CA TYR A 188 1833 1794 1814 9 -8 -19 C ATOM 2476 C TYR A 188 -4.356 8.717 0.205 1.00 14.57 C ANISOU 2476 C TYR A 188 1816 1875 1846 32 -3 -21 C ATOM 2477 O TYR A 188 -4.859 9.335 -0.736 1.00 14.20 O ANISOU 2477 O TYR A 188 1688 1844 1861 123 -80 47 O ATOM 2478 CB TYR A 188 -5.555 6.775 1.279 1.00 14.43 C ANISOU 2478 CB TYR A 188 1888 1791 1800 31 24 -74 C ATOM 2479 CG TYR A 188 -6.923 7.276 0.924 1.00 14.94 C ANISOU 2479 CG TYR A 188 1866 1807 2000 -45 8 -45 C ATOM 2480 CD1 TYR A 188 -7.501 6.963 -0.303 1.00 15.71 C ANISOU 2480 CD1 TYR A 188 2124 1905 1938 72 89 -85 C ATOM 2481 CD2 TYR A 188 -7.642 8.100 1.807 1.00 16.55 C ANISOU 2481 CD2 TYR A 188 2183 2161 1944 -69 63 24 C ATOM 2482 CE1 TYR A 188 -8.792 7.429 -0.650 1.00 16.50 C ANISOU 2482 CE1 TYR A 188 2206 2022 2041 138 -37 28 C ATOM 2483 CE2 TYR A 188 -8.923 8.586 1.473 1.00 16.93 C ANISOU 2483 CE2 TYR A 188 2184 2084 2162 12 -111 -16 C ATOM 2484 CZ TYR A 188 -9.485 8.249 0.236 1.00 17.58 C ANISOU 2484 CZ TYR A 188 2245 2231 2201 111 -47 245 C ATOM 2485 OH TYR A 188 -10.736 8.697 -0.095 1.00 17.53 O ANISOU 2485 OH TYR A 188 2204 2246 2207 464 -476 481 O ATOM 2486 N LEU A 189 -3.658 9.323 1.164 1.00 14.51 N ANISOU 2486 N LEU A 189 1807 1882 1825 40 43 4 N ATOM 2487 CA LEU A 189 -3.448 10.766 1.120 1.00 14.46 C ANISOU 2487 CA LEU A 189 1803 1810 1879 53 11 6 C ATOM 2488 C LEU A 189 -2.698 11.124 -0.172 1.00 14.64 C ANISOU 2488 C LEU A 189 1859 1825 1878 85 26 9 C ATOM 2489 O LEU A 189 -3.045 12.073 -0.866 1.00 13.81 O ANISOU 2489 O LEU A 189 1761 1550 1934 114 1 12 O ATOM 2490 CB LEU A 189 -2.685 11.258 2.343 1.00 14.53 C ANISOU 2490 CB LEU A 189 1842 1839 1837 91 55 12 C ATOM 2491 CG LEU A 189 -2.466 12.772 2.406 1.00 14.71 C ANISOU 2491 CG LEU A 189 1748 1921 1917 31 49 -56 C ATOM 2492 CD1 LEU A 189 -3.786 13.580 2.374 1.00 16.18 C ANISOU 2492 CD1 LEU A 189 2130 2067 1951 -44 -21 -60 C ATOM 2493 CD2 LEU A 189 -1.604 13.127 3.634 1.00 16.32 C ANISOU 2493 CD2 LEU A 189 2148 2104 1946 187 99 -6 C ATOM 2494 N MET A 190 -1.694 10.320 -0.511 1.00 15.00 N ANISOU 2494 N MET A 190 1873 1935 1891 41 -14 68 N ATOM 2495 CA MET A 190 -0.951 10.511 -1.737 1.00 15.70 C ANISOU 2495 CA MET A 190 1973 2000 1990 39 12 26 C ATOM 2496 C MET A 190 -1.871 10.411 -2.968 1.00 15.04 C ANISOU 2496 C MET A 190 1860 1942 1911 35 22 14 C ATOM 2497 O MET A 190 -1.740 11.195 -3.893 1.00 14.22 O ANISOU 2497 O MET A 190 1686 1892 1824 102 83 27 O ATOM 2498 CB MET A 190 0.198 9.511 -1.830 1.00 16.12 C ANISOU 2498 CB MET A 190 2024 2009 2090 63 42 56 C ATOM 2499 CG MET A 190 1.132 9.781 -2.957 1.00 19.32 C ANISOU 2499 CG MET A 190 2440 2382 2518 140 -18 22 C ATOM 2500 SD MET A 190 2.495 8.584 -3.060 1.00 27.55 S ANISOU 2500 SD MET A 190 3315 3560 3592 305 -94 -255 S ATOM 2501 CE MET A 190 3.679 9.376 -2.151 1.00 28.48 C ANISOU 2501 CE MET A 190 3500 3577 3744 121 -44 -191 C ATOM 2502 N LYS A 191 -2.799 9.460 -2.962 1.00 15.52 N ANISOU 2502 N LYS A 191 1954 2004 1937 46 22 49 N ATOM 2503 CA LYS A 191 -3.736 9.270 -4.072 1.00 15.68 C ANISOU 2503 CA LYS A 191 1963 2007 1985 6 41 7 C ATOM 2504 C LYS A 191 -4.600 10.517 -4.252 1.00 15.68 C ANISOU 2504 C LYS A 191 1952 2028 1978 21 55 25 C ATOM 2505 O LYS A 191 -4.703 11.053 -5.352 1.00 15.12 O ANISOU 2505 O LYS A 191 1845 2098 1798 16 255 13 O ATOM 2506 CB LYS A 191 -4.625 8.052 -3.813 1.00 16.23 C ANISOU 2506 CB LYS A 191 2109 1982 2075 56 -11 33 C ATOM 2507 CG LYS A 191 -5.552 7.689 -4.953 1.00 17.35 C ANISOU 2507 CG LYS A 191 2234 2081 2277 14 -104 35 C ATOM 2508 CD LYS A 191 -6.217 6.356 -4.709 1.00 22.45 C ANISOU 2508 CD LYS A 191 2681 2928 2920 6 -155 23 C ATOM 2509 CE LYS A 191 -7.135 5.989 -5.864 1.00 24.21 C ANISOU 2509 CE LYS A 191 2977 3063 3159 50 -159 -77 C ATOM 2510 NZ LYS A 191 -8.411 6.733 -5.701 1.00 27.13 N ANISOU 2510 NZ LYS A 191 3133 3594 3581 157 -218 -47 N ATOM 2511 N ILE A 192 -5.199 10.999 -3.167 1.00 14.98 N ANISOU 2511 N ILE A 192 1913 1943 1833 0 115 -11 N ATOM 2512 CA ILE A 192 -6.149 12.119 -3.285 1.00 15.30 C ANISOU 2512 CA ILE A 192 1951 1967 1894 -10 34 36 C ATOM 2513 C ILE A 192 -5.477 13.479 -3.491 1.00 15.48 C ANISOU 2513 C ILE A 192 1953 2008 1917 -6 46 59 C ATOM 2514 O ILE A 192 -6.065 14.359 -4.121 1.00 14.74 O ANISOU 2514 O ILE A 192 1937 1984 1678 -8 43 220 O ATOM 2515 CB ILE A 192 -7.179 12.147 -2.118 1.00 15.10 C ANISOU 2515 CB ILE A 192 1925 1914 1896 12 35 4 C ATOM 2516 CG1 ILE A 192 -6.485 12.376 -0.779 1.00 15.84 C ANISOU 2516 CG1 ILE A 192 2070 1981 1964 5 119 -27 C ATOM 2517 CG2 ILE A 192 -7.995 10.828 -2.118 1.00 15.86 C ANISOU 2517 CG2 ILE A 192 1943 2111 1970 -31 112 41 C ATOM 2518 CD1 ILE A 192 -7.415 12.280 0.396 1.00 17.75 C ANISOU 2518 CD1 ILE A 192 2295 2103 2346 43 -15 -3 C ATOM 2519 N LEU A 193 -4.251 13.637 -2.987 1.00 15.61 N ANISOU 2519 N LEU A 193 2061 2016 1850 -58 -13 37 N ATOM 2520 CA LEU A 193 -3.449 14.826 -3.257 1.00 16.25 C ANISOU 2520 CA LEU A 193 2123 2055 1995 -41 -29 36 C ATOM 2521 C LEU A 193 -3.004 14.830 -4.726 1.00 15.82 C ANISOU 2521 C LEU A 193 2096 2013 1899 -83 -19 -45 C ATOM 2522 O LEU A 193 -2.937 15.886 -5.375 1.00 15.12 O ANISOU 2522 O LEU A 193 2201 1992 1549 -161 -89 -42 O ATOM 2523 CB LEU A 193 -2.227 14.879 -2.343 1.00 16.60 C ANISOU 2523 CB LEU A 193 2175 2020 2110 -73 -43 -52 C ATOM 2524 CG LEU A 193 -2.149 15.920 -1.217 1.00 20.19 C ANISOU 2524 CG LEU A 193 2512 2680 2478 0 16 43 C ATOM 2525 CD1 LEU A 193 -3.456 16.502 -0.716 1.00 20.00 C ANISOU 2525 CD1 LEU A 193 2416 2737 2446 23 28 65 C ATOM 2526 CD2 LEU A 193 -1.336 15.391 -0.084 1.00 20.83 C ANISOU 2526 CD2 LEU A 193 2849 2622 2444 115 -25 232 C ATOM 2527 N THR A 194 -2.707 13.647 -5.248 1.00 16.56 N ANISOU 2527 N THR A 194 2125 2155 2010 -103 4 40 N ATOM 2528 CA THR A 194 -2.467 13.497 -6.680 1.00 17.10 C ANISOU 2528 CA THR A 194 2158 2222 2115 -117 36 13 C ATOM 2529 C THR A 194 -3.700 13.902 -7.506 1.00 18.01 C ANISOU 2529 C THR A 194 2270 2312 2259 -72 37 7 C ATOM 2530 O THR A 194 -3.570 14.543 -8.539 1.00 17.87 O ANISOU 2530 O THR A 194 2254 2315 2217 -157 98 12 O ATOM 2531 CB THR A 194 -1.994 12.074 -7.011 1.00 16.87 C ANISOU 2531 CB THR A 194 2150 2165 2095 -107 42 56 C ATOM 2532 OG1 THR A 194 -0.730 11.820 -6.366 1.00 15.41 O ANISOU 2532 OG1 THR A 194 1897 2199 1757 -554 66 218 O ATOM 2533 CG2 THR A 194 -1.701 11.907 -8.537 1.00 16.80 C ANISOU 2533 CG2 THR A 194 2091 2197 2094 -103 16 68 C ATOM 2534 N GLU A 195 -4.895 13.554 -7.041 1.00 19.12 N ANISOU 2534 N GLU A 195 2403 2427 2435 -76 27 13 N ATOM 2535 CA GLU A 195 -6.135 13.943 -7.731 1.00 20.22 C ANISOU 2535 CA GLU A 195 2551 2553 2578 -41 -34 33 C ATOM 2536 C GLU A 195 -6.328 15.474 -7.766 1.00 20.48 C ANISOU 2536 C GLU A 195 2606 2583 2592 -28 -60 24 C ATOM 2537 O GLU A 195 -6.897 16.022 -8.705 1.00 19.38 O ANISOU 2537 O GLU A 195 2562 2551 2249 0 -147 123 O ATOM 2538 CB GLU A 195 -7.360 13.237 -7.088 1.00 20.48 C ANISOU 2538 CB GLU A 195 2562 2606 2612 -74 2 66 C ATOM 2539 CG GLU A 195 -7.374 11.735 -7.382 1.00 22.45 C ANISOU 2539 CG GLU A 195 2770 2819 2939 -240 11 61 C ATOM 2540 CD GLU A 195 -8.499 10.955 -6.708 1.00 26.63 C ANISOU 2540 CD GLU A 195 3426 3124 3567 -384 52 -71 C ATOM 2541 OE1 GLU A 195 -8.710 9.786 -7.127 1.00 30.05 O ANISOU 2541 OE1 GLU A 195 3816 3509 4091 -641 13 0 O ATOM 2542 OE2 GLU A 195 -9.163 11.476 -5.770 1.00 28.15 O ANISOU 2542 OE2 GLU A 195 3527 3277 3891 -697 193 -68 O ATOM 2543 N ARG A 196 -5.850 16.145 -6.723 1.00 20.97 N ANISOU 2543 N ARG A 196 2669 2648 2649 24 -104 9 N ATOM 2544 CA ARG A 196 -5.865 17.602 -6.631 1.00 21.35 C ANISOU 2544 CA ARG A 196 2720 2680 2712 24 -51 31 C ATOM 2545 C ARG A 196 -4.875 18.300 -7.591 1.00 21.11 C ANISOU 2545 C ARG A 196 2682 2642 2695 22 -59 7 C ATOM 2546 O ARG A 196 -4.973 19.499 -7.819 1.00 20.84 O ANISOU 2546 O ARG A 196 2759 2452 2707 37 -64 147 O ATOM 2547 CB ARG A 196 -5.582 17.986 -5.183 1.00 21.76 C ANISOU 2547 CB ARG A 196 2747 2724 2793 14 -59 -23 C ATOM 2548 CG ARG A 196 -5.575 19.431 -4.881 1.00 23.76 C ANISOU 2548 CG ARG A 196 2992 2994 3041 73 -46 51 C ATOM 2549 CD ARG A 196 -5.769 19.727 -3.401 1.00 25.48 C ANISOU 2549 CD ARG A 196 3319 3145 3218 -4 -167 32 C ATOM 2550 NE ARG A 196 -6.220 21.090 -3.238 1.00 28.95 N ANISOU 2550 NE ARG A 196 3608 3785 3604 -33 -140 -157 N ATOM 2551 CZ ARG A 196 -7.281 21.488 -2.556 1.00 31.62 C ANISOU 2551 CZ ARG A 196 4031 3987 3995 -64 -86 -95 C ATOM 2552 NH1 ARG A 196 -8.072 20.642 -1.896 1.00 31.61 N ANISOU 2552 NH1 ARG A 196 4236 3788 3983 -88 -177 133 N ATOM 2553 NH2 ARG A 196 -7.552 22.781 -2.531 1.00 33.56 N ANISOU 2553 NH2 ARG A 196 4384 4032 4333 -113 -92 50 N ATOM 2554 N GLY A 197 -3.932 17.552 -8.154 1.00 20.83 N ANISOU 2554 N GLY A 197 2632 2632 2650 15 -70 18 N ATOM 2555 CA GLY A 197 -3.043 18.070 -9.193 1.00 20.43 C ANISOU 2555 CA GLY A 197 2609 2591 2561 31 -59 70 C ATOM 2556 C GLY A 197 -1.564 17.880 -8.913 1.00 20.38 C ANISOU 2556 C GLY A 197 2602 2588 2552 25 -54 69 C ATOM 2557 O GLY A 197 -0.720 18.187 -9.752 1.00 19.36 O ANISOU 2557 O GLY A 197 2612 2354 2388 31 -172 352 O ATOM 2558 N TYR A 198 -1.237 17.331 -7.748 1.00 20.03 N ANISOU 2558 N TYR A 198 2603 2576 2430 29 -58 76 N ATOM 2559 CA TYR A 198 0.163 17.181 -7.352 1.00 20.78 C ANISOU 2559 CA TYR A 198 2671 2660 2562 35 -13 25 C ATOM 2560 C TYR A 198 0.737 15.831 -7.816 1.00 21.39 C ANISOU 2560 C TYR A 198 2757 2732 2636 24 -26 19 C ATOM 2561 O TYR A 198 0.011 14.980 -8.323 1.00 21.28 O ANISOU 2561 O TYR A 198 2811 2705 2568 90 -8 -27 O ATOM 2562 CB TYR A 198 0.293 17.368 -5.832 1.00 20.56 C ANISOU 2562 CB TYR A 198 2624 2652 2536 46 -80 51 C ATOM 2563 CG TYR A 198 -0.325 18.660 -5.323 1.00 20.91 C ANISOU 2563 CG TYR A 198 2789 2641 2512 79 -11 18 C ATOM 2564 CD1 TYR A 198 -1.194 18.649 -4.236 1.00 22.06 C ANISOU 2564 CD1 TYR A 198 3023 2706 2651 224 -206 252 C ATOM 2565 CD2 TYR A 198 -0.063 19.902 -5.943 1.00 23.62 C ANISOU 2565 CD2 TYR A 198 3145 2924 2903 196 -37 -67 C ATOM 2566 CE1 TYR A 198 -1.774 19.827 -3.745 1.00 22.43 C ANISOU 2566 CE1 TYR A 198 3206 2836 2478 103 -106 0 C ATOM 2567 CE2 TYR A 198 -0.657 21.108 -5.449 1.00 24.11 C ANISOU 2567 CE2 TYR A 198 3322 2840 2997 101 -58 62 C ATOM 2568 CZ TYR A 198 -1.511 21.042 -4.352 1.00 23.25 C ANISOU 2568 CZ TYR A 198 3294 2780 2759 234 -114 -31 C ATOM 2569 OH TYR A 198 -2.111 22.157 -3.821 1.00 26.11 O ANISOU 2569 OH TYR A 198 3991 3107 2821 281 -216 97 O ATOM 2570 N SER A 199 2.041 15.648 -7.639 1.00 22.50 N ANISOU 2570 N SER A 199 2883 2867 2796 37 8 -12 N ATOM 2571 CA SER A 199 2.716 14.449 -8.103 1.00 23.67 C ANISOU 2571 CA SER A 199 2997 3013 2980 -13 -11 23 C ATOM 2572 C SER A 199 3.857 14.003 -7.158 1.00 24.46 C ANISOU 2572 C SER A 199 3095 3108 3087 -41 -65 14 C ATOM 2573 O SER A 199 4.751 14.787 -6.827 1.00 25.06 O ANISOU 2573 O SER A 199 3121 3196 3202 -108 -85 34 O ATOM 2574 CB SER A 199 3.259 14.684 -9.515 1.00 23.70 C ANISOU 2574 CB SER A 199 3015 3036 2951 18 -5 -42 C ATOM 2575 OG SER A 199 3.794 13.483 -10.008 1.00 24.06 O ANISOU 2575 OG SER A 199 3044 3042 3054 7 114 32 O ATOM 2576 N PHE A 200 3.811 12.736 -6.754 1.00 24.78 N ANISOU 2576 N PHE A 200 3138 3143 3132 -21 -80 25 N ATOM 2577 CA PHE A 200 4.753 12.150 -5.812 1.00 25.16 C ANISOU 2577 CA PHE A 200 3189 3202 3166 -17 -60 2 C ATOM 2578 C PHE A 200 5.247 10.790 -6.339 1.00 25.66 C ANISOU 2578 C PHE A 200 3256 3275 3216 13 -67 1 C ATOM 2579 O PHE A 200 4.778 9.717 -5.918 1.00 25.37 O ANISOU 2579 O PHE A 200 3223 3242 3173 -13 -161 40 O ATOM 2580 CB PHE A 200 4.077 11.988 -4.447 1.00 25.06 C ANISOU 2580 CB PHE A 200 3170 3215 3136 -16 -55 4 C ATOM 2581 CG PHE A 200 3.509 13.262 -3.891 1.00 24.84 C ANISOU 2581 CG PHE A 200 3151 3263 3022 33 -36 28 C ATOM 2582 CD1 PHE A 200 2.158 13.561 -4.034 1.00 24.68 C ANISOU 2582 CD1 PHE A 200 3179 3311 2885 61 -97 -17 C ATOM 2583 CD2 PHE A 200 4.325 14.152 -3.190 1.00 24.90 C ANISOU 2583 CD2 PHE A 200 3209 3189 3063 18 -30 134 C ATOM 2584 CE1 PHE A 200 1.628 14.751 -3.508 1.00 24.94 C ANISOU 2584 CE1 PHE A 200 3048 3356 3071 -5 -42 61 C ATOM 2585 CE2 PHE A 200 3.809 15.328 -2.650 1.00 25.50 C ANISOU 2585 CE2 PHE A 200 3293 3380 3013 58 -63 70 C ATOM 2586 CZ PHE A 200 2.446 15.633 -2.810 1.00 25.03 C ANISOU 2586 CZ PHE A 200 3104 3361 3046 -7 43 39 C ATOM 2587 N VAL A 201 6.218 10.849 -7.246 1.00 26.39 N ANISOU 2587 N VAL A 201 3367 3323 3334 44 -60 -3 N ATOM 2588 CA VAL A 201 6.581 9.688 -8.069 1.00 27.33 C ANISOU 2588 CA VAL A 201 3493 3428 3460 33 -58 -8 C ATOM 2589 C VAL A 201 7.621 8.761 -7.412 1.00 26.89 C ANISOU 2589 C VAL A 201 3479 3327 3411 55 -87 -20 C ATOM 2590 O VAL A 201 7.654 7.586 -7.743 1.00 27.60 O ANISOU 2590 O VAL A 201 3612 3340 3534 53 -222 -62 O ATOM 2591 CB VAL A 201 7.084 10.104 -9.492 1.00 27.80 C ANISOU 2591 CB VAL A 201 3590 3461 3509 54 -30 -40 C ATOM 2592 CG1 VAL A 201 7.089 8.896 -10.445 1.00 29.54 C ANISOU 2592 CG1 VAL A 201 3735 3702 3787 -25 -25 -9 C ATOM 2593 CG2 VAL A 201 6.223 11.234 -10.100 1.00 28.77 C ANISOU 2593 CG2 VAL A 201 3629 3608 3694 63 -84 -2 C ATOM 2594 N THR A 202 8.444 9.271 -6.488 1.00 25.74 N ANISOU 2594 N THR A 202 3299 3225 3254 9 -53 -20 N ATOM 2595 CA THR A 202 9.448 8.441 -5.795 1.00 25.11 C ANISOU 2595 CA THR A 202 3225 3179 3136 -11 -6 -39 C ATOM 2596 C THR A 202 8.968 7.828 -4.459 1.00 24.49 C ANISOU 2596 C THR A 202 3104 3125 3073 -7 -47 -40 C ATOM 2597 O THR A 202 8.074 8.373 -3.792 1.00 23.95 O ANISOU 2597 O THR A 202 2997 3161 2943 10 -99 -27 O ATOM 2598 CB THR A 202 10.735 9.265 -5.537 1.00 25.39 C ANISOU 2598 CB THR A 202 3279 3197 3170 -10 9 -38 C ATOM 2599 OG1 THR A 202 10.448 10.354 -4.648 1.00 26.28 O ANISOU 2599 OG1 THR A 202 3587 3223 3172 -121 90 0 O ATOM 2600 CG2 THR A 202 11.245 9.949 -6.824 1.00 25.20 C ANISOU 2600 CG2 THR A 202 3307 3180 3087 21 88 -1 C ATOM 2601 N THR A 203 9.590 6.715 -4.048 1.00 23.60 N ANISOU 2601 N THR A 203 3022 3000 2943 -12 -7 -60 N ATOM 2602 CA THR A 203 9.364 6.178 -2.701 1.00 23.40 C ANISOU 2602 CA THR A 203 2957 2992 2942 -28 -7 -34 C ATOM 2603 C THR A 203 9.792 7.229 -1.653 1.00 23.26 C ANISOU 2603 C THR A 203 2935 2969 2932 -41 -13 -31 C ATOM 2604 O THR A 203 9.197 7.320 -0.586 1.00 21.87 O ANISOU 2604 O THR A 203 2694 2940 2673 -201 51 47 O ATOM 2605 CB THR A 203 10.103 4.820 -2.443 1.00 23.18 C ANISOU 2605 CB THR A 203 2956 2936 2914 -24 26 -70 C ATOM 2606 OG1 THR A 203 11.532 5.007 -2.481 1.00 22.80 O ANISOU 2606 OG1 THR A 203 3057 2845 2761 45 15 -153 O ATOM 2607 CG2 THR A 203 9.831 3.816 -3.540 1.00 23.85 C ANISOU 2607 CG2 THR A 203 2980 2955 3126 -114 -32 -39 C ATOM 2608 N ALA A 204 10.806 8.036 -1.973 1.00 23.48 N ANISOU 2608 N ALA A 204 2938 3026 2957 -63 27 -35 N ATOM 2609 CA ALA A 204 11.247 9.102 -1.062 1.00 24.45 C ANISOU 2609 CA ALA A 204 3069 3116 3103 -56 28 -34 C ATOM 2610 C ALA A 204 10.139 10.107 -0.812 1.00 24.64 C ANISOU 2610 C ALA A 204 3065 3128 3166 -56 1 -39 C ATOM 2611 O ALA A 204 9.963 10.594 0.297 1.00 24.42 O ANISOU 2611 O ALA A 204 2922 3236 3118 -120 84 -34 O ATOM 2612 CB ALA A 204 12.471 9.811 -1.599 1.00 24.53 C ANISOU 2612 CB ALA A 204 3128 3091 3100 -49 -5 -40 C ATOM 2613 N GLU A 205 9.377 10.416 -1.841 1.00 25.48 N ANISOU 2613 N GLU A 205 3237 3190 3251 -54 26 -37 N ATOM 2614 CA GLU A 205 8.271 11.345 -1.666 1.00 26.43 C ANISOU 2614 CA GLU A 205 3363 3294 3385 -33 16 -26 C ATOM 2615 C GLU A 205 7.119 10.832 -0.799 1.00 26.68 C ANISOU 2615 C GLU A 205 3371 3319 3446 -15 17 -59 C ATOM 2616 O GLU A 205 6.372 11.641 -0.255 1.00 26.67 O ANISOU 2616 O GLU A 205 3409 3242 3482 -36 63 -149 O ATOM 2617 CB GLU A 205 7.793 11.859 -3.015 1.00 26.91 C ANISOU 2617 CB GLU A 205 3440 3326 3456 -29 2 -61 C ATOM 2618 CG GLU A 205 8.713 12.975 -3.470 1.00 28.24 C ANISOU 2618 CG GLU A 205 3573 3542 3616 -40 28 -32 C ATOM 2619 CD GLU A 205 8.651 13.251 -4.939 1.00 29.54 C ANISOU 2619 CD GLU A 205 3686 3728 3807 -43 -74 -42 C ATOM 2620 OE1 GLU A 205 8.243 14.389 -5.285 1.00 30.29 O ANISOU 2620 OE1 GLU A 205 3550 3799 4160 -94 -125 -92 O ATOM 2621 OE2 GLU A 205 9.043 12.351 -5.721 1.00 30.50 O ANISOU 2621 OE2 GLU A 205 3951 3348 4287 95 -60 -225 O ATOM 2622 N ARG A 206 6.978 9.511 -0.654 1.00 26.56 N ANISOU 2622 N ARG A 206 3388 3291 3411 -13 33 -23 N ATOM 2623 CA ARG A 206 6.023 8.954 0.308 1.00 26.57 C ANISOU 2623 CA ARG A 206 3348 3339 3408 15 20 -50 C ATOM 2624 C ARG A 206 6.330 9.454 1.699 1.00 25.02 C ANISOU 2624 C ARG A 206 3158 3133 3211 -1 25 -83 C ATOM 2625 O ARG A 206 5.417 9.649 2.493 1.00 24.16 O ANISOU 2625 O ARG A 206 2921 3065 3193 69 156 -228 O ATOM 2626 CB ARG A 206 6.049 7.415 0.359 1.00 27.42 C ANISOU 2626 CB ARG A 206 3486 3431 3498 -26 -4 -67 C ATOM 2627 CG ARG A 206 5.316 6.719 -0.767 1.00 31.09 C ANISOU 2627 CG ARG A 206 3954 3866 3991 19 -58 -36 C ATOM 2628 CD ARG A 206 5.243 5.210 -0.587 1.00 34.73 C ANISOU 2628 CD ARG A 206 4419 4374 4402 -116 10 56 C ATOM 2629 NE ARG A 206 4.210 4.869 0.389 1.00 37.88 N ANISOU 2629 NE ARG A 206 4690 4965 4737 -60 -28 -58 N ATOM 2630 CZ ARG A 206 4.404 4.662 1.696 1.00 40.19 C ANISOU 2630 CZ ARG A 206 4961 5247 5059 -46 4 -28 C ATOM 2631 NH1 ARG A 206 5.615 4.754 2.260 1.00 42.08 N ANISOU 2631 NH1 ARG A 206 5139 5479 5367 58 23 0 N ATOM 2632 NH2 ARG A 206 3.368 4.366 2.465 1.00 40.10 N ANISOU 2632 NH2 ARG A 206 4945 5169 5119 -34 27 -63 N ATOM 2633 N GLU A 207 7.613 9.610 2.016 1.00 22.91 N ANISOU 2633 N GLU A 207 2868 2887 2946 13 30 -42 N ATOM 2634 CA GLU A 207 7.974 10.073 3.344 1.00 22.08 C ANISOU 2634 CA GLU A 207 2774 2769 2843 -19 -9 20 C ATOM 2635 C GLU A 207 7.501 11.515 3.529 1.00 20.24 C ANISOU 2635 C GLU A 207 2530 2553 2608 -14 -46 47 C ATOM 2636 O GLU A 207 7.108 11.893 4.627 1.00 18.70 O ANISOU 2636 O GLU A 207 2300 2416 2386 -50 -145 183 O ATOM 2637 CB GLU A 207 9.475 9.916 3.620 1.00 22.70 C ANISOU 2637 CB GLU A 207 2869 2862 2890 7 11 41 C ATOM 2638 CG GLU A 207 9.990 8.476 3.506 1.00 24.02 C ANISOU 2638 CG GLU A 207 3278 2799 3046 -45 13 -28 C ATOM 2639 CD GLU A 207 9.338 7.523 4.500 1.00 27.30 C ANISOU 2639 CD GLU A 207 4111 2980 3280 -133 8 -125 C ATOM 2640 OE1 GLU A 207 9.176 7.900 5.681 1.00 26.45 O ANISOU 2640 OE1 GLU A 207 4209 2708 3131 70 -118 -299 O ATOM 2641 OE2 GLU A 207 8.984 6.383 4.101 1.00 30.78 O ANISOU 2641 OE2 GLU A 207 5083 3017 3595 -286 129 -40 O ATOM 2642 N ILE A 208 7.515 12.305 2.447 1.00 18.76 N ANISOU 2642 N ILE A 208 2376 2349 2403 -32 -33 23 N ATOM 2643 CA ILE A 208 6.961 13.657 2.491 1.00 17.61 C ANISOU 2643 CA ILE A 208 2238 2201 2251 -2 -10 54 C ATOM 2644 C ILE A 208 5.459 13.639 2.731 1.00 16.08 C ANISOU 2644 C ILE A 208 2053 2024 2031 -55 2 75 C ATOM 2645 O ILE A 208 4.957 14.419 3.518 1.00 15.52 O ANISOU 2645 O ILE A 208 2020 1858 2016 -90 -21 13 O ATOM 2646 CB ILE A 208 7.282 14.460 1.205 1.00 17.39 C ANISOU 2646 CB ILE A 208 2165 2220 2223 -36 32 18 C ATOM 2647 CG1 ILE A 208 8.807 14.577 1.008 1.00 19.20 C ANISOU 2647 CG1 ILE A 208 2474 2404 2416 3 -6 -43 C ATOM 2648 CG2 ILE A 208 6.653 15.870 1.284 1.00 17.02 C ANISOU 2648 CG2 ILE A 208 2078 2183 2205 43 10 169 C ATOM 2649 CD1 ILE A 208 9.538 15.258 2.141 1.00 20.07 C ANISOU 2649 CD1 ILE A 208 2442 2595 2588 -80 -40 71 C ATOM 2650 N VAL A 209 4.739 12.763 2.046 1.00 15.34 N ANISOU 2650 N VAL A 209 1986 1889 1953 -21 48 36 N ATOM 2651 CA VAL A 209 3.274 12.692 2.206 1.00 15.05 C ANISOU 2651 CA VAL A 209 1937 1848 1932 -15 27 50 C ATOM 2652 C VAL A 209 2.979 12.206 3.643 1.00 14.48 C ANISOU 2652 C VAL A 209 1857 1805 1837 -6 6 65 C ATOM 2653 O VAL A 209 2.065 12.679 4.301 1.00 14.43 O ANISOU 2653 O VAL A 209 1890 1725 1869 98 -45 137 O ATOM 2654 CB VAL A 209 2.622 11.796 1.122 1.00 14.68 C ANISOU 2654 CB VAL A 209 1875 1853 1850 -2 8 62 C ATOM 2655 CG1 VAL A 209 1.134 11.575 1.372 1.00 14.87 C ANISOU 2655 CG1 VAL A 209 1894 1814 1942 32 84 100 C ATOM 2656 CG2 VAL A 209 2.816 12.387 -0.262 1.00 15.52 C ANISOU 2656 CG2 VAL A 209 1946 1860 2091 -100 66 17 C ATOM 2657 N ARG A 210 3.796 11.301 4.151 1.00 14.10 N ANISOU 2657 N ARG A 210 1839 1722 1794 41 6 9 N ATOM 2658 CA ARG A 210 3.652 10.863 5.544 1.00 14.58 C ANISOU 2658 CA ARG A 210 1866 1816 1855 16 -6 5 C ATOM 2659 C ARG A 210 3.760 12.070 6.495 1.00 14.57 C ANISOU 2659 C ARG A 210 1884 1782 1869 41 2 -5 C ATOM 2660 O ARG A 210 2.980 12.202 7.446 1.00 14.91 O ANISOU 2660 O ARG A 210 1844 1834 1987 4 -16 72 O ATOM 2661 CB ARG A 210 4.727 9.840 5.913 1.00 14.34 C ANISOU 2661 CB ARG A 210 1863 1752 1831 2 -24 18 C ATOM 2662 CG ARG A 210 4.632 9.401 7.347 1.00 15.20 C ANISOU 2662 CG ARG A 210 1952 1923 1898 36 -25 -8 C ATOM 2663 CD ARG A 210 5.675 8.406 7.752 1.00 17.46 C ANISOU 2663 CD ARG A 210 2292 2217 2122 -4 8 32 C ATOM 2664 NE ARG A 210 7.030 8.877 7.494 1.00 18.80 N ANISOU 2664 NE ARG A 210 2352 2543 2245 156 31 15 N ATOM 2665 CZ ARG A 210 7.681 9.799 8.203 1.00 19.52 C ANISOU 2665 CZ ARG A 210 2459 2470 2487 -75 55 -101 C ATOM 2666 NH1 ARG A 210 7.118 10.418 9.232 1.00 19.71 N ANISOU 2666 NH1 ARG A 210 2555 2647 2285 -204 0 -89 N ATOM 2667 NH2 ARG A 210 8.913 10.115 7.862 1.00 21.69 N ANISOU 2667 NH2 ARG A 210 2664 2859 2717 -78 44 -35 N ATOM 2668 N ASP A 211 4.746 12.926 6.249 1.00 14.22 N ANISOU 2668 N ASP A 211 1819 1713 1869 2 -15 -18 N ATOM 2669 CA ASP A 211 4.906 14.137 7.053 1.00 14.67 C ANISOU 2669 CA ASP A 211 1882 1856 1835 5 -6 -37 C ATOM 2670 C ASP A 211 3.681 15.058 6.994 1.00 14.45 C ANISOU 2670 C ASP A 211 1817 1857 1814 21 18 -62 C ATOM 2671 O ASP A 211 3.305 15.617 8.000 1.00 14.31 O ANISOU 2671 O ASP A 211 1836 1923 1677 -25 14 -18 O ATOM 2672 CB ASP A 211 6.122 14.919 6.582 1.00 14.66 C ANISOU 2672 CB ASP A 211 1837 1861 1871 -11 14 -116 C ATOM 2673 CG ASP A 211 6.539 15.995 7.554 1.00 15.88 C ANISOU 2673 CG ASP A 211 2087 1923 2023 48 87 -169 C ATOM 2674 OD1 ASP A 211 6.751 17.142 7.100 1.00 15.43 O ANISOU 2674 OD1 ASP A 211 2110 1527 2223 -296 377 -212 O ATOM 2675 OD2 ASP A 211 6.671 15.779 8.781 1.00 16.74 O ANISOU 2675 OD2 ASP A 211 2467 1934 1959 57 -124 -267 O ATOM 2676 N ILE A 212 3.103 15.247 5.808 1.00 14.68 N ANISOU 2676 N ILE A 212 1839 1902 1833 44 -2 -29 N ATOM 2677 CA ILE A 212 1.901 16.077 5.639 1.00 15.19 C ANISOU 2677 CA ILE A 212 1955 1942 1874 -15 -9 17 C ATOM 2678 C ILE A 212 0.789 15.503 6.495 1.00 15.37 C ANISOU 2678 C ILE A 212 1897 1962 1980 -24 -33 -6 C ATOM 2679 O ILE A 212 0.102 16.223 7.239 1.00 15.24 O ANISOU 2679 O ILE A 212 1836 1913 2041 -5 -156 54 O ATOM 2680 CB ILE A 212 1.446 16.110 4.161 1.00 15.24 C ANISOU 2680 CB ILE A 212 1925 1941 1922 -44 -42 19 C ATOM 2681 CG1 ILE A 212 2.512 16.783 3.286 1.00 16.17 C ANISOU 2681 CG1 ILE A 212 2063 2144 1937 -87 -49 62 C ATOM 2682 CG2 ILE A 212 0.136 16.860 4.033 1.00 15.03 C ANISOU 2682 CG2 ILE A 212 1993 1895 1821 -45 95 51 C ATOM 2683 CD1 ILE A 212 2.272 16.652 1.768 1.00 17.58 C ANISOU 2683 CD1 ILE A 212 2423 2044 2211 -36 37 -59 C ATOM 2684 N LYS A 213 0.640 14.188 6.393 1.00 15.21 N ANISOU 2684 N LYS A 213 1924 1906 1949 -17 -42 -7 N ATOM 2685 CA LYS A 213 -0.360 13.453 7.158 1.00 15.19 C ANISOU 2685 CA LYS A 213 1907 1972 1892 -24 31 -11 C ATOM 2686 C LYS A 213 -0.210 13.727 8.665 1.00 15.56 C ANISOU 2686 C LYS A 213 1952 2034 1925 -23 1 -18 C ATOM 2687 O LYS A 213 -1.180 14.088 9.335 1.00 15.84 O ANISOU 2687 O LYS A 213 1993 2193 1831 -33 -27 -69 O ATOM 2688 CB LYS A 213 -0.263 11.950 6.839 1.00 14.84 C ANISOU 2688 CB LYS A 213 1848 1925 1865 -20 79 -16 C ATOM 2689 CG LYS A 213 -1.192 11.009 7.621 1.00 15.41 C ANISOU 2689 CG LYS A 213 1984 1877 1993 -33 118 -36 C ATOM 2690 CD LYS A 213 -0.793 9.544 7.422 1.00 13.76 C ANISOU 2690 CD LYS A 213 1723 1669 1835 -43 152 -89 C ATOM 2691 CE LYS A 213 0.305 9.084 8.363 1.00 13.83 C ANISOU 2691 CE LYS A 213 1760 1705 1790 -94 241 -84 C ATOM 2692 NZ LYS A 213 0.574 7.592 8.309 1.00 12.20 N ANISOU 2692 NZ LYS A 213 1125 1327 2183 4 642 16 N ATOM 2693 N GLU A 214 1.007 13.602 9.176 1.00 15.86 N ANISOU 2693 N GLU A 214 1950 2084 1990 -11 19 40 N ATOM 2694 CA GLU A 214 1.265 13.757 10.605 1.00 16.55 C ANISOU 2694 CA GLU A 214 2068 2118 2103 15 26 -34 C ATOM 2695 C GLU A 214 1.060 15.192 11.068 1.00 17.31 C ANISOU 2695 C GLU A 214 2192 2194 2188 54 46 5 C ATOM 2696 O GLU A 214 0.749 15.428 12.212 1.00 17.85 O ANISOU 2696 O GLU A 214 2264 2303 2215 192 157 -76 O ATOM 2697 CB GLU A 214 2.696 13.291 10.961 1.00 16.53 C ANISOU 2697 CB GLU A 214 2064 2113 2101 38 5 22 C ATOM 2698 CG GLU A 214 2.925 11.790 10.738 1.00 16.46 C ANISOU 2698 CG GLU A 214 1985 2224 2045 31 40 -72 C ATOM 2699 CD GLU A 214 4.350 11.322 11.025 1.00 17.96 C ANISOU 2699 CD GLU A 214 2473 2376 1974 17 209 -101 C ATOM 2700 OE1 GLU A 214 5.179 12.127 11.526 1.00 19.26 O ANISOU 2700 OE1 GLU A 214 2468 2907 1943 -75 102 -192 O ATOM 2701 OE2 GLU A 214 4.650 10.139 10.742 1.00 15.36 O ANISOU 2701 OE2 GLU A 214 2254 2037 1546 367 505 -635 O ATOM 2702 N LYS A 215 1.276 16.155 10.199 1.00 17.60 N ANISOU 2702 N LYS A 215 2231 2240 2216 78 -36 31 N ATOM 2703 CA LYS A 215 1.243 17.559 10.616 1.00 18.01 C ANISOU 2703 CA LYS A 215 2262 2250 2330 14 -57 -1 C ATOM 2704 C LYS A 215 -0.134 18.239 10.407 1.00 17.23 C ANISOU 2704 C LYS A 215 2163 2106 2277 21 -30 15 C ATOM 2705 O LYS A 215 -0.501 19.131 11.154 1.00 16.71 O ANISOU 2705 O LYS A 215 2125 1952 2272 47 -49 -44 O ATOM 2706 CB LYS A 215 2.346 18.343 9.895 1.00 18.64 C ANISOU 2706 CB LYS A 215 2330 2390 2360 24 -36 28 C ATOM 2707 CG LYS A 215 3.765 17.971 10.342 1.00 21.28 C ANISOU 2707 CG LYS A 215 2646 2590 2848 -48 -8 -11 C ATOM 2708 CD LYS A 215 4.786 18.867 9.681 1.00 24.64 C ANISOU 2708 CD LYS A 215 3093 3135 3134 16 -6 67 C ATOM 2709 CE LYS A 215 6.184 18.729 10.305 1.00 27.51 C ANISOU 2709 CE LYS A 215 3528 3342 3580 0 -167 116 C ATOM 2710 NZ LYS A 215 6.397 17.443 11.058 1.00 27.43 N ANISOU 2710 NZ LYS A 215 3843 3001 3576 -160 -78 240 N ATOM 2711 N LEU A 216 -0.894 17.785 9.417 1.00 16.19 N ANISOU 2711 N LEU A 216 2057 1929 2163 -15 -78 70 N ATOM 2712 CA LEU A 216 -2.095 18.498 8.990 1.00 16.52 C ANISOU 2712 CA LEU A 216 2062 2053 2160 -30 0 -9 C ATOM 2713 C LEU A 216 -3.415 17.699 9.004 1.00 15.93 C ANISOU 2713 C LEU A 216 1986 1997 2067 -11 5 2 C ATOM 2714 O LEU A 216 -4.503 18.293 8.918 1.00 15.36 O ANISOU 2714 O LEU A 216 1806 1886 2145 45 72 12 O ATOM 2715 CB LEU A 216 -1.849 19.046 7.591 1.00 16.50 C ANISOU 2715 CB LEU A 216 2153 1975 2138 12 0 59 C ATOM 2716 CG LEU A 216 -1.338 20.478 7.381 1.00 19.23 C ANISOU 2716 CG LEU A 216 2375 2458 2473 -72 -21 -35 C ATOM 2717 CD1 LEU A 216 -0.886 21.251 8.600 1.00 19.75 C ANISOU 2717 CD1 LEU A 216 2463 2608 2431 -28 -16 43 C ATOM 2718 CD2 LEU A 216 -0.282 20.475 6.309 1.00 18.86 C ANISOU 2718 CD2 LEU A 216 2090 2299 2776 -57 151 -151 C ATOM 2719 N CYS A 217 -3.357 16.378 9.097 1.00 14.79 N ANISOU 2719 N CYS A 217 1839 1846 1932 -15 -13 22 N ATOM 2720 CA CYS A 217 -4.601 15.619 9.042 1.00 15.02 C ANISOU 2720 CA CYS A 217 1827 1911 1968 -19 16 10 C ATOM 2721 C CYS A 217 -5.298 15.657 10.391 1.00 14.61 C ANISOU 2721 C CYS A 217 1813 1847 1890 -52 -34 27 C ATOM 2722 O CYS A 217 -4.660 15.880 11.399 1.00 14.45 O ANISOU 2722 O CYS A 217 1672 1834 1982 -201 -71 68 O ATOM 2723 CB CYS A 217 -4.357 14.191 8.581 1.00 15.21 C ANISOU 2723 CB CYS A 217 1837 1953 1987 -61 20 -3 C ATOM 2724 SG CYS A 217 -4.021 14.076 6.811 1.00 17.56 S ANISOU 2724 SG CYS A 217 1950 2523 2196 53 37 -255 S ATOM 2725 N TYR A 218 -6.621 15.488 10.381 1.00 14.03 N ANISOU 2725 N TYR A 218 1644 1813 1873 -29 -4 11 N ATOM 2726 CA TYR A 218 -7.426 15.353 11.592 1.00 13.89 C ANISOU 2726 CA TYR A 218 1760 1777 1739 -41 15 81 C ATOM 2727 C TYR A 218 -8.719 14.582 11.333 1.00 13.05 C ANISOU 2727 C TYR A 218 1564 1753 1642 -66 -21 69 C ATOM 2728 O TYR A 218 -9.146 14.445 10.199 1.00 12.78 O ANISOU 2728 O TYR A 218 1454 1798 1604 -202 103 151 O ATOM 2729 CB TYR A 218 -7.803 16.704 12.191 1.00 14.55 C ANISOU 2729 CB TYR A 218 1793 1848 1887 -61 -11 44 C ATOM 2730 CG TYR A 218 -8.748 17.551 11.336 1.00 15.36 C ANISOU 2730 CG TYR A 218 1945 2058 1831 5 38 107 C ATOM 2731 CD1 TYR A 218 -10.118 17.591 11.593 1.00 14.94 C ANISOU 2731 CD1 TYR A 218 2021 1815 1841 -17 -56 -39 C ATOM 2732 CD2 TYR A 218 -8.259 18.318 10.278 1.00 16.45 C ANISOU 2732 CD2 TYR A 218 2118 1879 2251 -208 77 193 C ATOM 2733 CE1 TYR A 218 -10.978 18.367 10.809 1.00 16.19 C ANISOU 2733 CE1 TYR A 218 2096 1926 2127 -100 17 33 C ATOM 2734 CE2 TYR A 218 -9.105 19.092 9.495 1.00 15.41 C ANISOU 2734 CE2 TYR A 218 2015 1914 1926 -220 0 153 C ATOM 2735 CZ TYR A 218 -10.462 19.117 9.759 1.00 15.71 C ANISOU 2735 CZ TYR A 218 2068 1996 1905 -18 160 80 C ATOM 2736 OH TYR A 218 -11.293 19.883 8.985 1.00 15.94 O ANISOU 2736 OH TYR A 218 1958 1920 2176 23 94 318 O ATOM 2737 N VAL A 219 -9.333 14.084 12.407 1.00 13.06 N ANISOU 2737 N VAL A 219 1587 1711 1663 -22 -35 12 N ATOM 2738 CA VAL A 219 -10.567 13.332 12.316 1.00 13.31 C ANISOU 2738 CA VAL A 219 1643 1686 1728 -24 17 61 C ATOM 2739 C VAL A 219 -11.740 14.258 12.596 1.00 13.53 C ANISOU 2739 C VAL A 219 1693 1688 1757 5 -35 50 C ATOM 2740 O VAL A 219 -11.834 14.874 13.654 1.00 13.12 O ANISOU 2740 O VAL A 219 1574 1626 1784 -61 -99 113 O ATOM 2741 CB VAL A 219 -10.605 12.116 13.276 1.00 13.20 C ANISOU 2741 CB VAL A 219 1593 1672 1749 43 -23 49 C ATOM 2742 CG1 VAL A 219 -11.985 11.458 13.233 1.00 13.90 C ANISOU 2742 CG1 VAL A 219 1895 1492 1895 31 90 241 C ATOM 2743 CG2 VAL A 219 -9.535 11.092 12.887 1.00 14.74 C ANISOU 2743 CG2 VAL A 219 1981 1829 1790 -65 6 91 C ATOM 2744 N ALA A 220 -12.643 14.328 11.625 1.00 14.65 N ANISOU 2744 N ALA A 220 1840 1822 1902 -24 36 29 N ATOM 2745 CA ALA A 220 -13.839 15.139 11.731 1.00 15.04 C ANISOU 2745 CA ALA A 220 1892 1869 1952 -8 -22 42 C ATOM 2746 C ALA A 220 -14.829 14.522 12.714 1.00 15.60 C ANISOU 2746 C ALA A 220 1985 1985 1956 36 28 18 C ATOM 2747 O ALA A 220 -15.053 13.307 12.699 1.00 15.67 O ANISOU 2747 O ALA A 220 2026 2046 1881 1 73 29 O ATOM 2748 CB ALA A 220 -14.467 15.247 10.370 1.00 15.61 C ANISOU 2748 CB ALA A 220 2017 1977 1937 -11 55 10 C ATOM 2749 N LEU A 221 -15.426 15.341 13.569 1.00 16.43 N ANISOU 2749 N LEU A 221 2165 1980 2095 12 -46 7 N ATOM 2750 CA LEU A 221 -16.493 14.861 14.452 1.00 16.95 C ANISOU 2750 CA LEU A 221 2173 2135 2129 4 -3 7 C ATOM 2751 C LEU A 221 -17.709 14.347 13.667 1.00 17.26 C ANISOU 2751 C LEU A 221 2207 2192 2157 0 -12 13 C ATOM 2752 O LEU A 221 -18.235 13.260 13.969 1.00 16.79 O ANISOU 2752 O LEU A 221 2176 2164 2039 -84 -35 111 O ATOM 2753 CB LEU A 221 -16.920 15.950 15.435 1.00 17.63 C ANISOU 2753 CB LEU A 221 2259 2166 2271 36 -36 21 C ATOM 2754 CG LEU A 221 -17.866 15.537 16.567 1.00 18.92 C ANISOU 2754 CG LEU A 221 2445 2352 2389 79 -29 48 C ATOM 2755 CD1 LEU A 221 -17.332 14.299 17.340 1.00 21.87 C ANISOU 2755 CD1 LEU A 221 2783 2762 2762 -94 1 -30 C ATOM 2756 CD2 LEU A 221 -18.110 16.739 17.519 1.00 21.12 C ANISOU 2756 CD2 LEU A 221 2700 2706 2616 -4 -37 -14 C ATOM 2757 N ASP A 222 -18.143 15.126 12.671 1.00 17.23 N ANISOU 2757 N ASP A 222 2196 2175 2173 6 18 31 N ATOM 2758 CA ASP A 222 -19.197 14.721 11.722 1.00 18.00 C ANISOU 2758 CA ASP A 222 2279 2307 2251 -36 7 42 C ATOM 2759 C ASP A 222 -18.687 14.896 10.294 1.00 17.77 C ANISOU 2759 C ASP A 222 2217 2281 2254 -25 -34 93 C ATOM 2760 O ASP A 222 -18.547 16.030 9.804 1.00 17.40 O ANISOU 2760 O ASP A 222 2066 2325 2220 -35 -94 279 O ATOM 2761 CB ASP A 222 -20.494 15.520 11.924 1.00 18.38 C ANISOU 2761 CB ASP A 222 2310 2345 2327 -23 -70 34 C ATOM 2762 CG ASP A 222 -21.665 14.988 11.063 1.00 21.16 C ANISOU 2762 CG ASP A 222 2761 2746 2531 -196 98 -27 C ATOM 2763 OD1 ASP A 222 -21.611 15.077 9.823 1.00 22.25 O ANISOU 2763 OD1 ASP A 222 3131 3133 2186 -339 -33 -38 O ATOM 2764 OD2 ASP A 222 -22.688 14.454 11.534 1.00 26.04 O ANISOU 2764 OD2 ASP A 222 3154 3560 3178 -229 115 -319 O ATOM 2765 N PHE A 223 -18.390 13.777 9.640 1.00 17.21 N ANISOU 2765 N PHE A 223 2156 2228 2154 2 -23 100 N ATOM 2766 CA PHE A 223 -17.717 13.809 8.347 1.00 17.30 C ANISOU 2766 CA PHE A 223 2156 2223 2194 7 -32 78 C ATOM 2767 C PHE A 223 -18.508 14.599 7.285 1.00 17.73 C ANISOU 2767 C PHE A 223 2199 2271 2266 12 -35 119 C ATOM 2768 O PHE A 223 -17.939 15.433 6.568 1.00 16.56 O ANISOU 2768 O PHE A 223 1966 2057 2268 -76 -61 252 O ATOM 2769 CB PHE A 223 -17.474 12.399 7.828 1.00 16.82 C ANISOU 2769 CB PHE A 223 2088 2104 2196 35 -47 81 C ATOM 2770 CG PHE A 223 -16.805 12.377 6.494 1.00 16.70 C ANISOU 2770 CG PHE A 223 2182 2045 2118 38 -14 -6 C ATOM 2771 CD1 PHE A 223 -15.481 12.781 6.367 1.00 15.50 C ANISOU 2771 CD1 PHE A 223 1952 2049 1887 83 107 10 C ATOM 2772 CD2 PHE A 223 -17.506 12.016 5.358 1.00 17.50 C ANISOU 2772 CD2 PHE A 223 2245 2085 2319 89 54 63 C ATOM 2773 CE1 PHE A 223 -14.853 12.781 5.117 1.00 17.54 C ANISOU 2773 CE1 PHE A 223 2273 2116 2274 -69 -64 -25 C ATOM 2774 CE2 PHE A 223 -16.892 12.011 4.115 1.00 18.05 C ANISOU 2774 CE2 PHE A 223 2251 2244 2362 143 123 3 C ATOM 2775 CZ PHE A 223 -15.559 12.409 3.996 1.00 17.60 C ANISOU 2775 CZ PHE A 223 2250 2211 2225 13 53 -25 C ATOM 2776 N GLU A 224 -19.803 14.321 7.171 1.00 17.96 N ANISOU 2776 N GLU A 224 2190 2310 2321 -57 -27 123 N ATOM 2777 CA GLU A 224 -20.619 14.979 6.142 1.00 19.32 C ANISOU 2777 CA GLU A 224 2364 2467 2510 -27 -37 17 C ATOM 2778 C GLU A 224 -20.747 16.496 6.374 1.00 18.41 C ANISOU 2778 C GLU A 224 2217 2371 2406 -12 -43 16 C ATOM 2779 O GLU A 224 -20.703 17.248 5.421 1.00 17.81 O ANISOU 2779 O GLU A 224 2025 2392 2350 -45 -47 -10 O ATOM 2780 CB GLU A 224 -22.003 14.303 5.975 1.00 20.19 C ANISOU 2780 CB GLU A 224 2517 2534 2618 -45 -12 23 C ATOM 2781 CG GLU A 224 -21.980 12.944 5.236 1.00 23.71 C ANISOU 2781 CG GLU A 224 3098 2843 3066 -10 52 -66 C ATOM 2782 CD GLU A 224 -21.299 12.923 3.849 1.00 29.45 C ANISOU 2782 CD GLU A 224 4101 3201 3886 109 -29 -164 C ATOM 2783 OE1 GLU A 224 -21.152 13.974 3.174 1.00 33.65 O ANISOU 2783 OE1 GLU A 224 4877 3596 4311 33 0 -243 O ATOM 2784 OE2 GLU A 224 -20.902 11.810 3.402 1.00 33.49 O ANISOU 2784 OE2 GLU A 224 4469 3833 4422 263 -91 -500 O ATOM 2785 N ASN A 225 -20.871 16.940 7.624 1.00 18.28 N ANISOU 2785 N ASN A 225 2217 2373 2356 15 -9 3 N ATOM 2786 CA ASN A 225 -20.865 18.376 7.922 1.00 18.50 C ANISOU 2786 CA ASN A 225 2273 2434 2322 34 19 -11 C ATOM 2787 C ASN A 225 -19.523 19.028 7.582 1.00 17.86 C ANISOU 2787 C ASN A 225 2221 2338 2224 44 51 0 C ATOM 2788 O ASN A 225 -19.504 20.166 7.132 1.00 15.72 O ANISOU 2788 O ASN A 225 1896 2149 1928 182 132 -53 O ATOM 2789 CB ASN A 225 -21.146 18.672 9.402 1.00 19.07 C ANISOU 2789 CB ASN A 225 2298 2577 2368 27 88 -4 C ATOM 2790 CG ASN A 225 -22.612 18.522 9.787 1.00 22.62 C ANISOU 2790 CG ASN A 225 2759 3219 2615 191 90 -261 C ATOM 2791 OD1 ASN A 225 -22.979 18.839 10.921 1.00 27.90 O ANISOU 2791 OD1 ASN A 225 3374 4154 3071 240 451 -467 O ATOM 2792 ND2 ASN A 225 -23.446 18.015 8.879 1.00 26.02 N ANISOU 2792 ND2 ASN A 225 2954 3972 2960 182 181 -512 N ATOM 2793 N GLU A 226 -18.408 18.330 7.840 1.00 17.76 N ANISOU 2793 N GLU A 226 2245 2237 2263 64 47 53 N ATOM 2794 CA GLU A 226 -17.091 18.894 7.581 1.00 18.55 C ANISOU 2794 CA GLU A 226 2369 2302 2376 37 -12 8 C ATOM 2795 C GLU A 226 -16.891 19.037 6.090 1.00 17.55 C ANISOU 2795 C GLU A 226 2265 2192 2208 33 4 31 C ATOM 2796 O GLU A 226 -16.230 19.975 5.678 1.00 17.54 O ANISOU 2796 O GLU A 226 2385 2098 2182 -39 26 33 O ATOM 2797 CB GLU A 226 -15.922 18.036 8.095 1.00 19.11 C ANISOU 2797 CB GLU A 226 2569 2328 2361 117 -2 24 C ATOM 2798 CG GLU A 226 -15.435 18.196 9.519 1.00 23.22 C ANISOU 2798 CG GLU A 226 3032 2648 3140 70 -113 27 C ATOM 2799 CD GLU A 226 -15.171 19.592 10.019 1.00 24.62 C ANISOU 2799 CD GLU A 226 3253 2482 3617 113 11 78 C ATOM 2800 OE1 GLU A 226 -16.101 20.106 10.637 1.00 28.37 O ANISOU 2800 OE1 GLU A 226 3755 3104 3920 -281 241 -223 O ATOM 2801 OE2 GLU A 226 -14.031 20.121 9.874 1.00 25.19 O ANISOU 2801 OE2 GLU A 226 3417 2503 3650 30 210 615 O ATOM 2802 N MET A 227 -17.424 18.097 5.292 1.00 16.66 N ANISOU 2802 N MET A 227 2166 2034 2130 17 0 64 N ATOM 2803 CA MET A 227 -17.307 18.169 3.841 1.00 16.31 C ANISOU 2803 CA MET A 227 2068 2045 2082 22 3 -2 C ATOM 2804 C MET A 227 -18.050 19.429 3.337 1.00 16.58 C ANISOU 2804 C MET A 227 2145 2069 2086 7 3 44 C ATOM 2805 O MET A 227 -17.578 20.136 2.439 1.00 15.78 O ANISOU 2805 O MET A 227 2109 2007 1877 -55 96 57 O ATOM 2806 CB MET A 227 -17.878 16.908 3.165 1.00 16.12 C ANISOU 2806 CB MET A 227 2041 2007 2076 27 24 29 C ATOM 2807 CG MET A 227 -16.963 15.687 3.159 1.00 15.36 C ANISOU 2807 CG MET A 227 1996 1964 1875 -22 54 -26 C ATOM 2808 SD MET A 227 -15.378 15.901 2.290 1.00 16.93 S ANISOU 2808 SD MET A 227 2399 2123 1910 160 312 -119 S ATOM 2809 CE MET A 227 -15.962 15.542 0.601 1.00 17.70 C ANISOU 2809 CE MET A 227 2270 2314 2139 112 108 -149 C ATOM 2810 N ALA A 228 -19.190 19.713 3.960 1.00 16.38 N ANISOU 2810 N ALA A 228 2117 2067 2038 22 16 6 N ATOM 2811 CA ALA A 228 -20.005 20.863 3.592 1.00 17.07 C ANISOU 2811 CA ALA A 228 2216 2158 2110 5 -11 10 C ATOM 2812 C ALA A 228 -19.290 22.171 3.952 1.00 17.55 C ANISOU 2812 C ALA A 228 2287 2216 2165 -1 -52 25 C ATOM 2813 O ALA A 228 -19.355 23.153 3.205 1.00 17.32 O ANISOU 2813 O ALA A 228 2382 2212 1986 17 -97 98 O ATOM 2814 CB ALA A 228 -21.368 20.788 4.269 1.00 17.27 C ANISOU 2814 CB ALA A 228 2244 2191 2123 -36 10 24 C ATOM 2815 N THR A 229 -18.609 22.182 5.099 1.00 17.42 N ANISOU 2815 N THR A 229 2287 2197 2134 37 -86 58 N ATOM 2816 CA THR A 229 -17.790 23.322 5.489 1.00 17.39 C ANISOU 2816 CA THR A 229 2237 2192 2178 4 -50 28 C ATOM 2817 C THR A 229 -16.681 23.549 4.466 1.00 17.40 C ANISOU 2817 C THR A 229 2253 2184 2171 29 -70 1 C ATOM 2818 O THR A 229 -16.457 24.678 4.036 1.00 17.72 O ANISOU 2818 O THR A 229 2344 2172 2217 123 -126 2 O ATOM 2819 CB THR A 229 -17.187 23.120 6.904 1.00 17.84 C ANISOU 2819 CB THR A 229 2293 2225 2260 -12 -23 2 C ATOM 2820 OG1 THR A 229 -18.231 23.045 7.870 1.00 17.18 O ANISOU 2820 OG1 THR A 229 2248 2181 2097 -175 149 189 O ATOM 2821 CG2 THR A 229 -16.379 24.347 7.353 1.00 18.95 C ANISOU 2821 CG2 THR A 229 2441 2348 2409 -75 -69 -79 C ATOM 2822 N ALA A 230 -15.994 22.485 4.050 1.00 16.90 N ANISOU 2822 N ALA A 230 2161 2134 2123 47 -49 27 N ATOM 2823 CA ALA A 230 -14.884 22.649 3.111 1.00 17.07 C ANISOU 2823 CA ALA A 230 2185 2136 2162 2 -23 -13 C ATOM 2824 C ALA A 230 -15.386 23.183 1.781 1.00 16.90 C ANISOU 2824 C ALA A 230 2196 2086 2137 -5 15 23 C ATOM 2825 O ALA A 230 -14.641 23.849 1.063 1.00 17.21 O ANISOU 2825 O ALA A 230 2229 1999 2310 -65 -3 -74 O ATOM 2826 CB ALA A 230 -14.139 21.338 2.905 1.00 16.83 C ANISOU 2826 CB ALA A 230 2141 2079 2175 24 -8 -2 C ATOM 2827 N ALA A 231 -16.641 22.877 1.456 1.00 16.62 N ANISOU 2827 N ALA A 231 2146 2080 2089 -19 48 43 N ATOM 2828 CA ALA A 231 -17.216 23.256 0.187 1.00 17.37 C ANISOU 2828 CA ALA A 231 2188 2204 2206 -9 15 0 C ATOM 2829 C ALA A 231 -17.737 24.693 0.200 1.00 17.89 C ANISOU 2829 C ALA A 231 2268 2271 2256 -24 41 -8 C ATOM 2830 O ALA A 231 -17.895 25.304 -0.855 1.00 17.98 O ANISOU 2830 O ALA A 231 2296 2308 2226 -74 128 33 O ATOM 2831 CB ALA A 231 -18.326 22.286 -0.194 1.00 17.47 C ANISOU 2831 CB ALA A 231 2244 2185 2208 -1 50 48 C ATOM 2832 N SER A 232 -18.026 25.230 1.384 1.00 18.40 N ANISOU 2832 N SER A 232 2331 2340 2318 -15 42 -15 N ATOM 2833 CA SER A 232 -18.647 26.554 1.474 1.00 18.87 C ANISOU 2833 CA SER A 232 2366 2409 2392 -1 54 -27 C ATOM 2834 C SER A 232 -17.708 27.650 2.018 1.00 19.26 C ANISOU 2834 C SER A 232 2403 2469 2443 16 63 -43 C ATOM 2835 O SER A 232 -18.075 28.829 2.046 1.00 19.81 O ANISOU 2835 O SER A 232 2402 2592 2532 -8 89 -25 O ATOM 2836 CB SER A 232 -19.940 26.470 2.294 1.00 18.82 C ANISOU 2836 CB SER A 232 2368 2409 2375 23 49 -12 C ATOM 2837 OG SER A 232 -19.660 26.286 3.649 1.00 18.80 O ANISOU 2837 OG SER A 232 2502 2289 2350 14 257 -102 O ATOM 2838 N SER A 233 -16.496 27.260 2.406 1.00 19.32 N ANISOU 2838 N SER A 233 2366 2525 2447 21 45 -56 N ATOM 2839 CA SER A 233 -15.519 28.164 2.998 1.00 19.53 C ANISOU 2839 CA SER A 233 2398 2532 2487 21 27 -64 C ATOM 2840 C SER A 233 -14.075 27.668 2.662 1.00 19.35 C ANISOU 2840 C SER A 233 2357 2492 2501 0 44 -109 C ATOM 2841 O SER A 233 -13.879 26.514 2.294 1.00 19.07 O ANISOU 2841 O SER A 233 2181 2545 2518 28 93 -169 O ATOM 2842 CB SER A 233 -15.803 28.219 4.516 1.00 19.96 C ANISOU 2842 CB SER A 233 2396 2615 2571 -9 45 -112 C ATOM 2843 OG SER A 233 -14.703 28.647 5.304 1.00 21.37 O ANISOU 2843 OG SER A 233 2640 2814 2663 157 108 -189 O ATOM 2844 N SER A 234 -13.073 28.536 2.778 1.00 19.44 N ANISOU 2844 N SER A 234 2369 2494 2522 46 43 -104 N ATOM 2845 CA SER A 234 -11.666 28.122 2.644 1.00 19.46 C ANISOU 2845 CA SER A 234 2404 2492 2495 6 -45 -66 C ATOM 2846 C SER A 234 -10.959 27.954 4.000 1.00 19.29 C ANISOU 2846 C SER A 234 2427 2464 2437 -6 -40 -51 C ATOM 2847 O SER A 234 -9.763 27.705 4.056 1.00 19.61 O ANISOU 2847 O SER A 234 2492 2503 2455 -80 -133 -130 O ATOM 2848 CB SER A 234 -10.901 29.124 1.792 1.00 18.69 C ANISOU 2848 CB SER A 234 2314 2374 2411 6 -49 -31 C ATOM 2849 OG SER A 234 -10.897 30.391 2.415 1.00 19.07 O ANISOU 2849 OG SER A 234 2176 2551 2518 52 -231 69 O ATOM 2850 N SER A 235 -11.706 28.071 5.080 1.00 19.70 N ANISOU 2850 N SER A 235 2492 2494 2498 -29 -27 -43 N ATOM 2851 CA SER A 235 -11.140 28.138 6.431 1.00 20.21 C ANISOU 2851 CA SER A 235 2558 2573 2546 -31 -23 -27 C ATOM 2852 C SER A 235 -10.485 26.838 6.914 1.00 20.27 C ANISOU 2852 C SER A 235 2596 2577 2526 -52 -37 -23 C ATOM 2853 O SER A 235 -9.734 26.860 7.879 1.00 20.86 O ANISOU 2853 O SER A 235 2703 2631 2591 -130 -128 -85 O ATOM 2854 CB SER A 235 -12.228 28.538 7.417 1.00 20.27 C ANISOU 2854 CB SER A 235 2596 2613 2490 -56 18 -52 C ATOM 2855 OG SER A 235 -13.216 27.512 7.488 1.00 20.93 O ANISOU 2855 OG SER A 235 2704 2774 2473 -80 98 -153 O ATOM 2856 N LEU A 236 -10.782 25.710 6.267 1.00 19.69 N ANISOU 2856 N LEU A 236 2520 2485 2476 -56 22 4 N ATOM 2857 CA LEU A 236 -10.130 24.437 6.600 1.00 19.75 C ANISOU 2857 CA LEU A 236 2498 2518 2488 -1 11 -24 C ATOM 2858 C LEU A 236 -8.829 24.195 5.820 1.00 19.08 C ANISOU 2858 C LEU A 236 2454 2427 2368 21 50 -41 C ATOM 2859 O LEU A 236 -8.118 23.254 6.115 1.00 18.18 O ANISOU 2859 O LEU A 236 2366 2315 2226 99 133 -96 O ATOM 2860 CB LEU A 236 -11.086 23.260 6.362 1.00 19.70 C ANISOU 2860 CB LEU A 236 2563 2463 2460 -17 15 32 C ATOM 2861 CG LEU A 236 -12.075 22.837 7.446 1.00 22.03 C ANISOU 2861 CG LEU A 236 2780 2743 2847 42 -28 -77 C ATOM 2862 CD1 LEU A 236 -12.225 23.788 8.647 1.00 22.59 C ANISOU 2862 CD1 LEU A 236 2865 2831 2886 87 48 -144 C ATOM 2863 CD2 LEU A 236 -13.400 22.546 6.813 1.00 21.98 C ANISOU 2863 CD2 LEU A 236 2671 2932 2749 186 -119 -54 C ATOM 2864 N GLU A 237 -8.508 25.059 4.860 1.00 18.81 N ANISOU 2864 N GLU A 237 2367 2401 2378 3 32 -67 N ATOM 2865 CA GLU A 237 -7.330 24.869 4.014 1.00 18.90 C ANISOU 2865 CA GLU A 237 2391 2424 2365 18 -12 -44 C ATOM 2866 C GLU A 237 -6.010 25.240 4.728 1.00 18.52 C ANISOU 2866 C GLU A 237 2304 2394 2338 13 -38 -46 C ATOM 2867 O GLU A 237 -5.956 26.172 5.523 1.00 18.08 O ANISOU 2867 O GLU A 237 2150 2378 2341 -2 -149 -100 O ATOM 2868 CB GLU A 237 -7.500 25.652 2.712 1.00 19.29 C ANISOU 2868 CB GLU A 237 2423 2512 2392 49 -7 -73 C ATOM 2869 CG GLU A 237 -8.700 25.135 1.925 1.00 21.23 C ANISOU 2869 CG GLU A 237 2649 2931 2486 136 -40 -39 C ATOM 2870 CD GLU A 237 -8.857 25.737 0.536 1.00 23.42 C ANISOU 2870 CD GLU A 237 3059 3253 2584 132 -93 62 C ATOM 2871 OE1 GLU A 237 -9.912 25.459 -0.101 1.00 24.25 O ANISOU 2871 OE1 GLU A 237 3220 3623 2369 652 -541 74 O ATOM 2872 OE2 GLU A 237 -7.948 26.460 0.081 1.00 23.78 O ANISOU 2872 OE2 GLU A 237 3188 3633 2213 -3 182 -143 O ATOM 2873 N LYS A 238 -4.964 24.480 4.451 1.00 17.87 N ANISOU 2873 N LYS A 238 2273 2295 2220 35 -33 -22 N ATOM 2874 CA LYS A 238 -3.654 24.709 5.046 1.00 18.68 C ANISOU 2874 CA LYS A 238 2379 2350 2366 41 8 -34 C ATOM 2875 C LYS A 238 -2.580 24.605 3.975 1.00 18.89 C ANISOU 2875 C LYS A 238 2425 2401 2349 15 -12 -22 C ATOM 2876 O LYS A 238 -2.801 23.979 2.942 1.00 19.96 O ANISOU 2876 O LYS A 238 2536 2511 2534 90 39 -146 O ATOM 2877 CB LYS A 238 -3.399 23.671 6.130 1.00 18.91 C ANISOU 2877 CB LYS A 238 2369 2490 2323 45 -20 6 C ATOM 2878 CG LYS A 238 -4.311 23.783 7.357 1.00 20.75 C ANISOU 2878 CG LYS A 238 2566 2655 2661 35 26 -55 C ATOM 2879 CD LYS A 238 -3.847 24.889 8.309 1.00 23.57 C ANISOU 2879 CD LYS A 238 2977 3087 2892 -44 61 -153 C ATOM 2880 CE LYS A 238 -4.838 25.081 9.442 1.00 26.53 C ANISOU 2880 CE LYS A 238 3518 3349 3210 -122 60 -221 C ATOM 2881 NZ LYS A 238 -4.539 26.333 10.220 1.00 28.29 N ANISOU 2881 NZ LYS A 238 4033 3343 3372 -180 186 -489 N ATOM 2882 N SER A 239 -1.421 25.205 4.230 1.00 18.52 N ANISOU 2882 N SER A 239 2362 2331 2344 7 -32 -5 N ATOM 2883 CA SER A 239 -0.293 25.217 3.300 1.00 18.67 C ANISOU 2883 CA SER A 239 2397 2374 2323 -12 -5 16 C ATOM 2884 C SER A 239 0.810 24.311 3.807 1.00 17.98 C ANISOU 2884 C SER A 239 2260 2306 2265 -20 -13 -13 C ATOM 2885 O SER A 239 0.981 24.177 5.001 1.00 17.82 O ANISOU 2885 O SER A 239 2246 2411 2112 79 -113 -10 O ATOM 2886 CB SER A 239 0.262 26.641 3.180 1.00 18.90 C ANISOU 2886 CB SER A 239 2405 2389 2384 33 28 32 C ATOM 2887 OG SER A 239 -0.733 27.515 2.673 1.00 21.91 O ANISOU 2887 OG SER A 239 2857 2864 2603 -112 42 140 O ATOM 2888 N TYR A 240 1.557 23.686 2.907 1.00 17.73 N ANISOU 2888 N TYR A 240 2236 2284 2215 -65 -33 -10 N ATOM 2889 CA TYR A 240 2.668 22.822 3.295 1.00 17.40 C ANISOU 2889 CA TYR A 240 2203 2192 2215 -41 16 -7 C ATOM 2890 C TYR A 240 3.805 23.058 2.301 1.00 18.17 C ANISOU 2890 C TYR A 240 2332 2284 2289 -50 0 -9 C ATOM 2891 O TYR A 240 3.563 23.088 1.117 1.00 16.91 O ANISOU 2891 O TYR A 240 2203 2119 2103 -48 -55 79 O ATOM 2892 CB TYR A 240 2.246 21.345 3.296 1.00 17.43 C ANISOU 2892 CB TYR A 240 2240 2269 2114 -27 33 47 C ATOM 2893 CG TYR A 240 3.375 20.405 3.644 1.00 16.99 C ANISOU 2893 CG TYR A 240 2214 2026 2212 -22 84 -20 C ATOM 2894 CD1 TYR A 240 4.208 19.894 2.664 1.00 16.69 C ANISOU 2894 CD1 TYR A 240 2300 2005 2034 -96 153 73 C ATOM 2895 CD2 TYR A 240 3.629 20.061 4.968 1.00 16.21 C ANISOU 2895 CD2 TYR A 240 2200 1995 1962 93 199 179 C ATOM 2896 CE1 TYR A 240 5.265 19.027 2.986 1.00 15.42 C ANISOU 2896 CE1 TYR A 240 1933 2010 1916 33 -5 70 C ATOM 2897 CE2 TYR A 240 4.664 19.213 5.306 1.00 18.09 C ANISOU 2897 CE2 TYR A 240 2197 2375 2299 0 76 -47 C ATOM 2898 CZ TYR A 240 5.489 18.698 4.308 1.00 17.62 C ANISOU 2898 CZ TYR A 240 2273 2196 2224 111 137 -13 C ATOM 2899 OH TYR A 240 6.534 17.872 4.646 1.00 17.19 O ANISOU 2899 OH TYR A 240 2392 1876 2261 109 -156 -68 O ATOM 2900 N GLU A 241 5.037 23.209 2.798 1.00 19.13 N ANISOU 2900 N GLU A 241 2385 2443 2437 -26 0 4 N ATOM 2901 CA GLU A 241 6.208 23.511 1.966 1.00 20.23 C ANISOU 2901 CA GLU A 241 2508 2539 2640 -68 0 -3 C ATOM 2902 C GLU A 241 6.990 22.242 1.655 1.00 20.19 C ANISOU 2902 C GLU A 241 2457 2527 2686 -93 -6 -2 C ATOM 2903 O GLU A 241 7.457 21.571 2.564 1.00 20.67 O ANISOU 2903 O GLU A 241 2360 2503 2989 -227 -37 -145 O ATOM 2904 CB GLU A 241 7.131 24.509 2.656 1.00 20.52 C ANISOU 2904 CB GLU A 241 2525 2597 2671 -61 28 -1 C ATOM 2905 CG GLU A 241 8.295 24.920 1.752 1.00 23.64 C ANISOU 2905 CG GLU A 241 2888 2917 3177 -119 2 -33 C ATOM 2906 CD GLU A 241 9.161 26.033 2.321 1.00 27.10 C ANISOU 2906 CD GLU A 241 3118 3373 3805 -205 5 -269 C ATOM 2907 OE1 GLU A 241 8.639 26.942 3.003 1.00 31.35 O ANISOU 2907 OE1 GLU A 241 3647 3875 4388 -466 -92 -399 O ATOM 2908 OE2 GLU A 241 10.383 26.002 2.060 1.00 31.17 O ANISOU 2908 OE2 GLU A 241 3688 3681 4473 -382 -84 -296 O ATOM 2909 N LEU A 242 7.105 21.925 0.372 1.00 21.00 N ANISOU 2909 N LEU A 242 2585 2584 2808 -86 28 -7 N ATOM 2910 CA LEU A 242 7.834 20.746 -0.121 1.00 21.75 C ANISOU 2910 CA LEU A 242 2704 2713 2845 -65 21 26 C ATOM 2911 C LEU A 242 9.357 20.980 -0.028 1.00 22.30 C ANISOU 2911 C LEU A 242 2767 2799 2904 -92 49 23 C ATOM 2912 O LEU A 242 9.785 22.129 0.113 1.00 22.61 O ANISOU 2912 O LEU A 242 2774 2801 3013 -189 134 -21 O ATOM 2913 CB LEU A 242 7.423 20.428 -1.576 1.00 21.09 C ANISOU 2913 CB LEU A 242 2693 2590 2728 -68 -11 69 C ATOM 2914 CG LEU A 242 6.302 19.411 -1.916 1.00 23.04 C ANISOU 2914 CG LEU A 242 2934 2923 2895 12 -31 18 C ATOM 2915 CD1 LEU A 242 5.487 18.914 -0.732 1.00 22.04 C ANISOU 2915 CD1 LEU A 242 2603 2935 2833 -101 72 -29 C ATOM 2916 CD2 LEU A 242 5.363 19.880 -3.038 1.00 21.87 C ANISOU 2916 CD2 LEU A 242 2655 2671 2982 84 -53 160 C ATOM 2917 N PRO A 243 10.165 19.919 -0.078 1.00 22.49 N ANISOU 2917 N PRO A 243 2801 2837 2905 -50 33 45 N ATOM 2918 CA PRO A 243 11.629 20.063 0.006 1.00 23.26 C ANISOU 2918 CA PRO A 243 2931 2951 2955 -49 50 57 C ATOM 2919 C PRO A 243 12.240 20.989 -1.047 1.00 23.58 C ANISOU 2919 C PRO A 243 2960 3030 2967 -49 56 79 C ATOM 2920 O PRO A 243 13.210 21.661 -0.723 1.00 23.17 O ANISOU 2920 O PRO A 243 2908 3063 2832 -123 146 188 O ATOM 2921 CB PRO A 243 12.150 18.627 -0.179 1.00 23.35 C ANISOU 2921 CB PRO A 243 2923 2974 2973 -40 29 41 C ATOM 2922 CG PRO A 243 11.024 17.752 0.267 1.00 22.92 C ANISOU 2922 CG PRO A 243 2868 2902 2939 -52 39 62 C ATOM 2923 CD PRO A 243 9.764 18.500 -0.148 1.00 23.12 C ANISOU 2923 CD PRO A 243 2880 2971 2930 2 19 18 C ATOM 2924 N ASP A 244 11.678 21.040 -2.252 1.00 24.19 N ANISOU 2924 N ASP A 244 3055 3106 3027 -31 83 36 N ATOM 2925 CA ASP A 244 12.170 21.963 -3.282 1.00 25.41 C ANISOU 2925 CA ASP A 244 3191 3298 3165 21 28 0 C ATOM 2926 C ASP A 244 11.634 23.391 -3.158 1.00 25.01 C ANISOU 2926 C ASP A 244 3190 3174 3139 0 59 9 C ATOM 2927 O ASP A 244 11.946 24.229 -3.990 1.00 25.29 O ANISOU 2927 O ASP A 244 3206 3306 3095 8 126 70 O ATOM 2928 CB ASP A 244 11.911 21.405 -4.695 1.00 26.08 C ANISOU 2928 CB ASP A 244 3278 3431 3201 44 23 -30 C ATOM 2929 CG ASP A 244 10.452 21.503 -5.116 1.00 27.59 C ANISOU 2929 CG ASP A 244 3300 3924 3258 69 36 -49 C ATOM 2930 OD1 ASP A 244 10.169 21.238 -6.308 1.00 30.90 O ANISOU 2930 OD1 ASP A 244 3541 4770 3426 58 238 -178 O ATOM 2931 OD2 ASP A 244 9.524 21.821 -4.335 1.00 29.50 O ANISOU 2931 OD2 ASP A 244 3547 4398 3262 396 142 -115 O ATOM 2932 N GLY A 245 10.822 23.658 -2.138 1.00 24.49 N ANISOU 2932 N GLY A 245 3107 3104 3094 -13 62 14 N ATOM 2933 CA GLY A 245 10.374 25.009 -1.837 1.00 24.17 C ANISOU 2933 CA GLY A 245 3067 3060 3057 -15 38 -10 C ATOM 2934 C GLY A 245 8.946 25.312 -2.251 1.00 23.81 C ANISOU 2934 C GLY A 245 3000 3029 3017 -12 49 -12 C ATOM 2935 O GLY A 245 8.382 26.317 -1.795 1.00 23.67 O ANISOU 2935 O GLY A 245 3015 2974 3001 -80 40 -11 O ATOM 2936 N GLN A 246 8.372 24.475 -3.123 1.00 23.24 N ANISOU 2936 N GLN A 246 2907 2943 2981 -23 80 -33 N ATOM 2937 CA GLN A 246 6.984 24.624 -3.550 1.00 23.38 C ANISOU 2937 CA GLN A 246 2983 2961 2937 -13 28 -16 C ATOM 2938 C GLN A 246 6.029 24.469 -2.351 1.00 22.78 C ANISOU 2938 C GLN A 246 2873 2913 2870 -42 65 -6 C ATOM 2939 O GLN A 246 6.128 23.521 -1.568 1.00 22.14 O ANISOU 2939 O GLN A 246 2792 2943 2674 -117 86 -53 O ATOM 2940 CB GLN A 246 6.602 23.608 -4.637 1.00 23.49 C ANISOU 2940 CB GLN A 246 2992 2980 2952 25 19 -32 C ATOM 2941 CG GLN A 246 5.154 23.757 -5.155 1.00 24.75 C ANISOU 2941 CG GLN A 246 3148 3152 3103 44 -16 -22 C ATOM 2942 CD GLN A 246 4.693 22.645 -6.106 1.00 26.24 C ANISOU 2942 CD GLN A 246 3181 3622 3165 114 -182 -60 C ATOM 2943 OE1 GLN A 246 3.531 22.629 -6.509 1.00 29.79 O ANISOU 2943 OE1 GLN A 246 3737 4107 3475 137 -177 -84 O ATOM 2944 NE2 GLN A 246 5.578 21.716 -6.441 1.00 25.26 N ANISOU 2944 NE2 GLN A 246 2797 3852 2945 404 -95 -505 N ATOM 2945 N VAL A 247 5.106 25.411 -2.256 1.00 22.60 N ANISOU 2945 N VAL A 247 2866 2860 2860 -47 60 26 N ATOM 2946 CA VAL A 247 4.067 25.425 -1.249 1.00 22.33 C ANISOU 2946 CA VAL A 247 2831 2850 2801 -5 59 38 C ATOM 2947 C VAL A 247 2.805 24.886 -1.910 1.00 22.05 C ANISOU 2947 C VAL A 247 2793 2810 2774 24 44 25 C ATOM 2948 O VAL A 247 2.384 25.391 -2.953 1.00 21.30 O ANISOU 2948 O VAL A 247 2743 2650 2699 99 71 219 O ATOM 2949 CB VAL A 247 3.800 26.840 -0.726 1.00 22.50 C ANISOU 2949 CB VAL A 247 2844 2877 2825 -27 35 35 C ATOM 2950 CG1 VAL A 247 2.653 26.824 0.319 1.00 22.73 C ANISOU 2950 CG1 VAL A 247 2906 2919 2811 27 35 -32 C ATOM 2951 CG2 VAL A 247 5.069 27.450 -0.135 1.00 23.05 C ANISOU 2951 CG2 VAL A 247 2951 2979 2827 -51 100 74 C ATOM 2952 N ILE A 248 2.221 23.847 -1.312 1.00 21.40 N ANISOU 2952 N ILE A 248 2755 2680 2694 35 34 71 N ATOM 2953 CA ILE A 248 0.968 23.283 -1.797 1.00 21.67 C ANISOU 2953 CA ILE A 248 2782 2751 2699 1 -19 17 C ATOM 2954 C ILE A 248 -0.151 23.472 -0.794 1.00 21.47 C ANISOU 2954 C ILE A 248 2725 2736 2694 5 0 -1 C ATOM 2955 O ILE A 248 0.099 23.697 0.394 1.00 21.08 O ANISOU 2955 O ILE A 248 2677 2803 2527 0 38 -2 O ATOM 2956 CB ILE A 248 1.123 21.789 -2.136 1.00 22.10 C ANISOU 2956 CB ILE A 248 2793 2839 2762 -3 -31 35 C ATOM 2957 CG1 ILE A 248 1.522 20.963 -0.915 1.00 23.74 C ANISOU 2957 CG1 ILE A 248 3086 2854 3078 -13 -97 21 C ATOM 2958 CG2 ILE A 248 2.130 21.607 -3.268 1.00 23.16 C ANISOU 2958 CG2 ILE A 248 2984 2870 2942 -1 -49 -6 C ATOM 2959 CD1 ILE A 248 1.201 19.478 -1.075 1.00 25.55 C ANISOU 2959 CD1 ILE A 248 3286 3161 3258 -115 -184 18 C ATOM 2960 N THR A 249 -1.378 23.357 -1.283 1.00 21.16 N ANISOU 2960 N THR A 249 2680 2716 2640 40 -42 0 N ATOM 2961 CA THR A 249 -2.583 23.492 -0.466 1.00 21.36 C ANISOU 2961 CA THR A 249 2706 2715 2695 66 -30 -24 C ATOM 2962 C THR A 249 -3.253 22.143 -0.167 1.00 20.87 C ANISOU 2962 C THR A 249 2605 2663 2660 54 -46 -52 C ATOM 2963 O THR A 249 -3.435 21.323 -1.073 1.00 21.25 O ANISOU 2963 O THR A 249 2710 2696 2666 75 -58 -170 O ATOM 2964 CB THR A 249 -3.602 24.408 -1.195 1.00 21.94 C ANISOU 2964 CB THR A 249 2726 2800 2807 43 -22 -15 C ATOM 2965 OG1 THR A 249 -3.056 25.721 -1.382 1.00 21.94 O ANISOU 2965 OG1 THR A 249 2868 2867 2600 242 -43 68 O ATOM 2966 CG2 THR A 249 -4.829 24.648 -0.312 1.00 22.95 C ANISOU 2966 CG2 THR A 249 2878 2944 2897 116 97 -30 C ATOM 2967 N ILE A 250 -3.631 21.927 1.091 1.00 19.75 N ANISOU 2967 N ILE A 250 2451 2535 2515 56 -28 -65 N ATOM 2968 CA ILE A 250 -4.360 20.736 1.523 1.00 19.74 C ANISOU 2968 CA ILE A 250 2474 2494 2530 -8 -47 -39 C ATOM 2969 C ILE A 250 -5.720 21.202 2.050 1.00 18.59 C ANISOU 2969 C ILE A 250 2296 2353 2413 -44 -59 -9 C ATOM 2970 O ILE A 250 -5.783 22.031 2.966 1.00 17.98 O ANISOU 2970 O ILE A 250 2137 2134 2561 -119 -145 -134 O ATOM 2971 CB ILE A 250 -3.569 19.983 2.635 1.00 20.70 C ANISOU 2971 CB ILE A 250 2521 2596 2748 0 45 2 C ATOM 2972 CG1 ILE A 250 -2.076 19.968 2.320 1.00 23.89 C ANISOU 2972 CG1 ILE A 250 3015 2859 3203 -62 -142 66 C ATOM 2973 CG2 ILE A 250 -4.021 18.512 2.783 1.00 21.79 C ANISOU 2973 CG2 ILE A 250 2674 2809 2793 -43 -8 -62 C ATOM 2974 CD1 ILE A 250 -1.332 21.031 3.006 1.00 27.27 C ANISOU 2974 CD1 ILE A 250 3494 3390 3477 89 -101 29 C ATOM 2975 N GLY A 251 -6.809 20.690 1.472 1.00 17.54 N ANISOU 2975 N GLY A 251 2259 2167 2238 -47 -85 10 N ATOM 2976 CA GLY A 251 -8.163 21.028 1.924 1.00 16.91 C ANISOU 2976 CA GLY A 251 2168 2114 2142 -61 -92 13 C ATOM 2977 C GLY A 251 -8.855 19.895 2.673 1.00 17.09 C ANISOU 2977 C GLY A 251 2210 2164 2116 -39 -102 1 C ATOM 2978 O GLY A 251 -8.370 19.469 3.721 1.00 17.00 O ANISOU 2978 O GLY A 251 2228 2121 2109 -14 -322 23 O ATOM 2979 N ASN A 252 -9.973 19.395 2.122 1.00 16.26 N ANISOU 2979 N ASN A 252 2016 2077 2082 -6 -89 33 N ATOM 2980 CA ASN A 252 -10.763 18.302 2.722 1.00 15.48 C ANISOU 2980 CA ASN A 252 1945 1979 1955 -22 0 33 C ATOM 2981 C ASN A 252 -10.000 16.968 2.804 1.00 14.82 C ANISOU 2981 C ASN A 252 1862 1877 1892 -82 13 -39 C ATOM 2982 O ASN A 252 -10.365 16.074 3.568 1.00 13.99 O ANISOU 2982 O ASN A 252 1778 1835 1701 -99 64 14 O ATOM 2983 CB ASN A 252 -12.161 18.148 2.052 1.00 15.71 C ANISOU 2983 CB ASN A 252 2019 2003 1946 -24 47 16 C ATOM 2984 CG ASN A 252 -12.093 17.828 0.563 1.00 16.76 C ANISOU 2984 CG ASN A 252 2119 2080 2169 53 46 19 C ATOM 2985 OD1 ASN A 252 -11.033 17.504 0.035 1.00 17.57 O ANISOU 2985 OD1 ASN A 252 2349 2169 2157 253 289 -40 O ATOM 2986 ND2 ASN A 252 -13.237 17.937 -0.126 1.00 17.73 N ANISOU 2986 ND2 ASN A 252 2283 2135 2317 -169 168 -267 N ATOM 2987 N GLU A 253 -8.890 16.876 2.077 1.00 14.42 N ANISOU 2987 N GLU A 253 1857 1832 1788 -57 60 -35 N ATOM 2988 CA GLU A 253 -7.947 15.761 2.213 1.00 14.22 C ANISOU 2988 CA GLU A 253 1792 1767 1843 -55 34 24 C ATOM 2989 C GLU A 253 -7.443 15.606 3.642 1.00 14.46 C ANISOU 2989 C GLU A 253 1731 1788 1975 -47 45 44 C ATOM 2990 O GLU A 253 -7.176 14.497 4.081 1.00 14.10 O ANISOU 2990 O GLU A 253 1664 1654 2038 -163 114 309 O ATOM 2991 CB GLU A 253 -6.764 15.944 1.266 1.00 14.77 C ANISOU 2991 CB GLU A 253 1918 1832 1861 7 16 -41 C ATOM 2992 CG GLU A 253 -7.159 16.024 -0.200 1.00 15.34 C ANISOU 2992 CG GLU A 253 1994 1959 1874 0 2 -1 C ATOM 2993 CD GLU A 253 -7.321 17.446 -0.744 1.00 17.18 C ANISOU 2993 CD GLU A 253 2562 2165 1800 -43 -13 -14 C ATOM 2994 OE1 GLU A 253 -7.460 17.555 -1.974 1.00 19.56 O ANISOU 2994 OE1 GLU A 253 3458 2330 1643 -116 351 114 O ATOM 2995 OE2 GLU A 253 -7.349 18.450 0.022 1.00 15.49 O ANISOU 2995 OE2 GLU A 253 2601 1784 1498 83 181 -45 O ATOM 2996 N ARG A 254 -7.335 16.723 4.364 1.00 14.44 N ANISOU 2996 N ARG A 254 1755 1804 1926 -85 37 15 N ATOM 2997 CA ARG A 254 -6.920 16.739 5.759 1.00 14.46 C ANISOU 2997 CA ARG A 254 1827 1805 1861 -20 11 40 C ATOM 2998 C ARG A 254 -7.741 15.757 6.609 1.00 14.58 C ANISOU 2998 C ARG A 254 1809 1774 1955 -37 -15 35 C ATOM 2999 O ARG A 254 -7.194 15.033 7.433 1.00 13.72 O ANISOU 2999 O ARG A 254 1837 1550 1824 4 -6 93 O ATOM 3000 CB ARG A 254 -7.089 18.159 6.347 1.00 14.35 C ANISOU 3000 CB ARG A 254 1770 1819 1862 -67 14 0 C ATOM 3001 CG ARG A 254 -6.106 19.221 5.840 1.00 15.13 C ANISOU 3001 CG ARG A 254 1989 1879 1881 33 -36 8 C ATOM 3002 CD ARG A 254 -6.282 20.588 6.499 1.00 15.73 C ANISOU 3002 CD ARG A 254 1956 2062 1956 -14 9 67 C ATOM 3003 NE ARG A 254 -5.904 20.573 7.918 1.00 15.77 N ANISOU 3003 NE ARG A 254 1932 1972 2088 -159 -145 -141 N ATOM 3004 CZ ARG A 254 -6.433 21.353 8.867 1.00 16.70 C ANISOU 3004 CZ ARG A 254 2036 2244 2063 -50 0 4 C ATOM 3005 NH1 ARG A 254 -7.372 22.245 8.591 1.00 16.34 N ANISOU 3005 NH1 ARG A 254 2210 2037 1960 146 -1 -168 N ATOM 3006 NH2 ARG A 254 -6.000 21.249 10.118 1.00 17.48 N ANISOU 3006 NH2 ARG A 254 2159 2269 2209 10 -253 -55 N ATOM 3007 N PHE A 255 -9.058 15.750 6.429 1.00 15.08 N ANISOU 3007 N PHE A 255 1886 1845 1997 46 6 42 N ATOM 3008 CA PHE A 255 -9.933 14.853 7.214 1.00 14.70 C ANISOU 3008 CA PHE A 255 1859 1776 1950 7 11 23 C ATOM 3009 C PHE A 255 -10.496 13.652 6.449 1.00 14.99 C ANISOU 3009 C PHE A 255 1874 1845 1975 30 7 8 C ATOM 3010 O PHE A 255 -10.960 12.698 7.063 1.00 14.12 O ANISOU 3010 O PHE A 255 1779 1500 2085 -8 -67 64 O ATOM 3011 CB PHE A 255 -11.065 15.629 7.905 1.00 14.56 C ANISOU 3011 CB PHE A 255 1894 1788 1849 16 -2 16 C ATOM 3012 CG PHE A 255 -11.964 16.367 6.968 1.00 14.63 C ANISOU 3012 CG PHE A 255 1770 1823 1964 22 19 -46 C ATOM 3013 CD1 PHE A 255 -13.048 15.737 6.378 1.00 14.30 C ANISOU 3013 CD1 PHE A 255 1619 1924 1888 -48 -8 54 C ATOM 3014 CD2 PHE A 255 -11.735 17.706 6.680 1.00 14.63 C ANISOU 3014 CD2 PHE A 255 1811 1836 1909 -27 -105 28 C ATOM 3015 CE1 PHE A 255 -13.890 16.425 5.533 1.00 13.75 C ANISOU 3015 CE1 PHE A 255 1653 1944 1625 -125 -84 131 C ATOM 3016 CE2 PHE A 255 -12.574 18.386 5.831 1.00 15.13 C ANISOU 3016 CE2 PHE A 255 1884 1938 1924 123 -228 10 C ATOM 3017 CZ PHE A 255 -13.669 17.723 5.261 1.00 13.28 C ANISOU 3017 CZ PHE A 255 1651 1707 1685 -68 -219 31 C ATOM 3018 N ARG A 256 -10.429 13.692 5.128 1.00 15.42 N ANISOU 3018 N ARG A 256 1968 1858 2030 56 -33 37 N ATOM 3019 CA ARG A 256 -10.794 12.555 4.301 1.00 15.64 C ANISOU 3019 CA ARG A 256 1974 1936 2029 37 -10 -7 C ATOM 3020 C ARG A 256 -9.815 11.408 4.466 1.00 15.72 C ANISOU 3020 C ARG A 256 2001 1926 2042 70 14 -26 C ATOM 3021 O ARG A 256 -10.220 10.251 4.392 1.00 15.68 O ANISOU 3021 O ARG A 256 2046 1891 2021 140 94 -36 O ATOM 3022 CB ARG A 256 -10.826 12.940 2.834 1.00 15.88 C ANISOU 3022 CB ARG A 256 1995 1946 2092 68 7 -3 C ATOM 3023 CG ARG A 256 -12.106 13.562 2.389 1.00 17.98 C ANISOU 3023 CG ARG A 256 2223 2329 2279 -74 -163 -189 C ATOM 3024 CD ARG A 256 -12.398 13.222 0.963 1.00 22.41 C ANISOU 3024 CD ARG A 256 2743 2886 2887 99 -103 206 C ATOM 3025 NE ARG A 256 -11.666 14.115 0.154 1.00 20.83 N ANISOU 3025 NE ARG A 256 2354 2482 3079 -178 -147 504 N ATOM 3026 CZ ARG A 256 -11.092 13.879 -1.023 1.00 20.03 C ANISOU 3026 CZ ARG A 256 2560 2431 2618 -29 -49 -91 C ATOM 3027 NH1 ARG A 256 -11.109 12.709 -1.661 1.00 19.79 N ANISOU 3027 NH1 ARG A 256 2352 2080 3087 -334 -312 369 N ATOM 3028 NH2 ARG A 256 -10.469 14.896 -1.574 1.00 19.17 N ANISOU 3028 NH2 ARG A 256 2595 2231 2455 -423 146 224 N ATOM 3029 N CYS A 257 -8.541 11.726 4.680 1.00 15.38 N ANISOU 3029 N CYS A 257 1919 1905 2019 57 3 -19 N ATOM 3030 CA CYS A 257 -7.524 10.694 4.827 1.00 16.24 C ANISOU 3030 CA CYS A 257 2009 2045 2113 57 0 -1 C ATOM 3031 C CYS A 257 -7.800 9.754 6.023 1.00 15.61 C ANISOU 3031 C CYS A 257 1896 1995 2039 88 -31 -5 C ATOM 3032 O CYS A 257 -7.985 8.549 5.817 1.00 15.21 O ANISOU 3032 O CYS A 257 1629 2019 2128 234 -18 42 O ATOM 3033 CB CYS A 257 -6.113 11.302 4.848 1.00 16.53 C ANISOU 3033 CB CYS A 257 2069 2065 2144 126 -59 7 C ATOM 3034 SG CYS A 257 -4.826 10.186 5.448 1.00 20.16 S ANISOU 3034 SG CYS A 257 2586 2434 2636 282 139 177 S ATOM 3035 N PRO A 258 -7.834 10.265 7.253 1.00 15.34 N ANISOU 3035 N PRO A 258 1827 1958 2043 64 -24 13 N ATOM 3036 CA PRO A 258 -8.163 9.422 8.406 1.00 15.09 C ANISOU 3036 CA PRO A 258 1830 1942 1960 9 -8 1 C ATOM 3037 C PRO A 258 -9.633 8.981 8.540 1.00 14.81 C ANISOU 3037 C PRO A 258 1812 1880 1933 3 46 -22 C ATOM 3038 O PRO A 258 -9.885 8.056 9.306 1.00 14.49 O ANISOU 3038 O PRO A 258 1631 1858 2014 -89 111 -74 O ATOM 3039 CB PRO A 258 -7.753 10.274 9.603 1.00 15.36 C ANISOU 3039 CB PRO A 258 1934 1923 1979 50 -28 -51 C ATOM 3040 CG PRO A 258 -7.682 11.634 9.143 1.00 15.12 C ANISOU 3040 CG PRO A 258 1867 1939 1938 58 7 102 C ATOM 3041 CD PRO A 258 -7.459 11.623 7.672 1.00 15.50 C ANISOU 3041 CD PRO A 258 1905 1942 2042 129 -16 -10 C ATOM 3042 N GLU A 259 -10.563 9.612 7.835 1.00 14.05 N ANISOU 3042 N GLU A 259 1661 1817 1857 -38 1 -41 N ATOM 3043 CA GLU A 259 -11.934 9.107 7.787 1.00 14.41 C ANISOU 3043 CA GLU A 259 1824 1788 1861 25 45 -11 C ATOM 3044 C GLU A 259 -11.950 7.639 7.365 1.00 13.92 C ANISOU 3044 C GLU A 259 1763 1718 1806 21 76 -43 C ATOM 3045 O GLU A 259 -12.834 6.885 7.754 1.00 12.85 O ANISOU 3045 O GLU A 259 1690 1512 1679 153 147 -28 O ATOM 3046 CB GLU A 259 -12.759 9.933 6.811 1.00 14.49 C ANISOU 3046 CB GLU A 259 1783 1844 1879 17 -59 0 C ATOM 3047 CG GLU A 259 -14.231 9.558 6.767 1.00 15.38 C ANISOU 3047 CG GLU A 259 1951 1860 2031 26 70 -23 C ATOM 3048 CD GLU A 259 -14.956 9.773 8.078 1.00 17.47 C ANISOU 3048 CD GLU A 259 2312 2213 2112 -105 -112 107 C ATOM 3049 OE1 GLU A 259 -14.440 10.517 8.938 1.00 18.31 O ANISOU 3049 OE1 GLU A 259 2599 2348 2009 -121 -312 -203 O ATOM 3050 OE2 GLU A 259 -16.068 9.208 8.230 1.00 16.82 O ANISOU 3050 OE2 GLU A 259 1868 2301 2219 -80 288 218 O ATOM 3051 N THR A 260 -10.946 7.251 6.579 1.00 13.84 N ANISOU 3051 N THR A 260 1796 1700 1762 11 92 7 N ATOM 3052 CA THR A 260 -10.754 5.871 6.127 1.00 13.78 C ANISOU 3052 CA THR A 260 1824 1722 1689 1 88 21 C ATOM 3053 C THR A 260 -10.759 4.825 7.268 1.00 13.90 C ANISOU 3053 C THR A 260 1851 1722 1709 -9 67 20 C ATOM 3054 O THR A 260 -11.207 3.688 7.077 1.00 13.83 O ANISOU 3054 O THR A 260 1945 1707 1602 -31 123 51 O ATOM 3055 CB THR A 260 -9.431 5.798 5.375 1.00 13.72 C ANISOU 3055 CB THR A 260 1840 1719 1653 23 61 11 C ATOM 3056 OG1 THR A 260 -9.477 6.677 4.238 1.00 14.74 O ANISOU 3056 OG1 THR A 260 1976 1802 1820 -11 332 -175 O ATOM 3057 CG2 THR A 260 -9.217 4.449 4.795 1.00 13.88 C ANISOU 3057 CG2 THR A 260 1878 1710 1685 -25 105 42 C ATOM 3058 N LEU A 261 -10.271 5.214 8.439 1.00 13.39 N ANISOU 3058 N LEU A 261 1743 1728 1616 -37 -23 24 N ATOM 3059 CA LEU A 261 -10.315 4.338 9.614 1.00 13.34 C ANISOU 3059 CA LEU A 261 1737 1670 1662 -45 -15 6 C ATOM 3060 C LEU A 261 -11.740 3.985 10.010 1.00 13.32 C ANISOU 3060 C LEU A 261 1783 1685 1593 -16 5 0 C ATOM 3061 O LEU A 261 -11.975 2.884 10.478 1.00 13.58 O ANISOU 3061 O LEU A 261 1874 1713 1573 -27 -23 -1 O ATOM 3062 CB LEU A 261 -9.608 4.974 10.804 1.00 13.55 C ANISOU 3062 CB LEU A 261 1757 1707 1684 -17 14 11 C ATOM 3063 CG LEU A 261 -8.121 5.261 10.617 1.00 13.46 C ANISOU 3063 CG LEU A 261 1682 1673 1758 -36 -22 -15 C ATOM 3064 CD1 LEU A 261 -7.653 6.202 11.704 1.00 13.50 C ANISOU 3064 CD1 LEU A 261 1702 1738 1687 -150 26 -64 C ATOM 3065 CD2 LEU A 261 -7.351 3.968 10.677 1.00 15.43 C ANISOU 3065 CD2 LEU A 261 1840 1978 2044 -80 -125 -110 C ATOM 3066 N PHE A 262 -12.679 4.912 9.823 1.00 13.85 N ANISOU 3066 N PHE A 262 1852 1728 1680 -47 0 62 N ATOM 3067 CA PHE A 262 -14.097 4.680 10.101 1.00 14.29 C ANISOU 3067 CA PHE A 262 1840 1812 1776 9 -12 21 C ATOM 3068 C PHE A 262 -14.882 4.154 8.898 1.00 14.72 C ANISOU 3068 C PHE A 262 1859 1879 1855 -26 -8 19 C ATOM 3069 O PHE A 262 -15.887 3.471 9.090 1.00 14.95 O ANISOU 3069 O PHE A 262 1802 1864 2013 28 -69 -62 O ATOM 3070 CB PHE A 262 -14.733 5.953 10.661 1.00 14.44 C ANISOU 3070 CB PHE A 262 1924 1813 1748 7 22 57 C ATOM 3071 CG PHE A 262 -14.051 6.448 11.909 1.00 14.64 C ANISOU 3071 CG PHE A 262 1866 1842 1854 7 -12 36 C ATOM 3072 CD1 PHE A 262 -14.472 6.014 13.155 1.00 13.89 C ANISOU 3072 CD1 PHE A 262 1861 1683 1733 112 10 21 C ATOM 3073 CD2 PHE A 262 -12.946 7.303 11.839 1.00 14.72 C ANISOU 3073 CD2 PHE A 262 1893 1858 1842 9 81 -85 C ATOM 3074 CE1 PHE A 262 -13.826 6.439 14.312 1.00 13.96 C ANISOU 3074 CE1 PHE A 262 1924 1636 1743 74 -143 141 C ATOM 3075 CE2 PHE A 262 -12.298 7.706 12.989 1.00 13.42 C ANISOU 3075 CE2 PHE A 262 1859 1674 1563 -33 -3 16 C ATOM 3076 CZ PHE A 262 -12.758 7.266 14.231 1.00 13.06 C ANISOU 3076 CZ PHE A 262 1695 1545 1721 67 -147 24 C ATOM 3077 N GLN A 263 -14.415 4.457 7.678 1.00 14.86 N ANISOU 3077 N GLN A 263 1806 1957 1881 0 12 -44 N ATOM 3078 CA GLN A 263 -15.040 3.994 6.436 1.00 14.45 C ANISOU 3078 CA GLN A 263 1777 1911 1799 14 17 -28 C ATOM 3079 C GLN A 263 -13.985 3.372 5.519 1.00 14.29 C ANISOU 3079 C GLN A 263 1685 1958 1786 -15 -13 -7 C ATOM 3080 O GLN A 263 -13.512 4.033 4.572 1.00 14.26 O ANISOU 3080 O GLN A 263 1560 2115 1742 0 104 -39 O ATOM 3081 CB GLN A 263 -15.743 5.142 5.700 1.00 14.69 C ANISOU 3081 CB GLN A 263 1839 1939 1802 1 24 -12 C ATOM 3082 CG GLN A 263 -16.755 5.908 6.515 1.00 15.54 C ANISOU 3082 CG GLN A 263 1900 2136 1866 127 -51 -48 C ATOM 3083 CD GLN A 263 -17.619 6.843 5.667 1.00 16.54 C ANISOU 3083 CD GLN A 263 2111 2343 1830 129 -99 -70 C ATOM 3084 OE1 GLN A 263 -18.353 6.381 4.797 1.00 16.07 O ANISOU 3084 OE1 GLN A 263 2070 2465 1569 514 -581 -181 O ATOM 3085 NE2 GLN A 263 -17.542 8.148 5.928 1.00 14.54 N ANISOU 3085 NE2 GLN A 263 1841 2278 1404 254 228 -381 N ATOM 3086 N PRO A 264 -13.584 2.131 5.801 1.00 13.48 N ANISOU 3086 N PRO A 264 1648 1754 1718 -8 1 -27 N ATOM 3087 CA PRO A 264 -12.576 1.456 4.973 1.00 14.23 C ANISOU 3087 CA PRO A 264 1777 1798 1831 22 -59 2 C ATOM 3088 C PRO A 264 -12.970 1.314 3.482 1.00 15.03 C ANISOU 3088 C PRO A 264 1883 1895 1931 45 -11 39 C ATOM 3089 O PRO A 264 -12.086 1.068 2.664 1.00 14.40 O ANISOU 3089 O PRO A 264 1721 1747 2003 76 -137 69 O ATOM 3090 CB PRO A 264 -12.405 0.098 5.674 1.00 14.79 C ANISOU 3090 CB PRO A 264 1810 1938 1869 -7 20 3 C ATOM 3091 CG PRO A 264 -12.824 0.369 7.130 1.00 13.42 C ANISOU 3091 CG PRO A 264 1671 1730 1696 56 -63 -75 C ATOM 3092 CD PRO A 264 -13.992 1.304 6.951 1.00 13.86 C ANISOU 3092 CD PRO A 264 1696 1790 1777 64 27 -70 C ATOM 3093 N SER A 265 -14.252 1.497 3.132 1.00 15.36 N ANISOU 3093 N SER A 265 1951 1923 1959 -9 -45 66 N ATOM 3094 CA SER A 265 -14.660 1.537 1.727 1.00 16.39 C ANISOU 3094 CA SER A 265 2048 2084 2094 19 11 56 C ATOM 3095 C SER A 265 -13.958 2.649 0.911 1.00 16.68 C ANISOU 3095 C SER A 265 2118 2124 2094 -15 -12 86 C ATOM 3096 O SER A 265 -13.892 2.556 -0.317 1.00 16.63 O ANISOU 3096 O SER A 265 2144 2183 1990 -60 59 108 O ATOM 3097 CB SER A 265 -16.185 1.688 1.603 1.00 16.85 C ANISOU 3097 CB SER A 265 2098 2120 2183 4 39 73 C ATOM 3098 OG SER A 265 -16.614 2.916 2.188 1.00 17.20 O ANISOU 3098 OG SER A 265 2091 2164 2278 214 132 51 O ATOM 3099 N PHE A 266 -13.445 3.684 1.574 1.00 16.97 N ANISOU 3099 N PHE A 266 2201 2180 2066 28 -21 78 N ATOM 3100 CA PHE A 266 -12.621 4.709 0.903 1.00 17.83 C ANISOU 3100 CA PHE A 266 2256 2283 2232 0 -9 4 C ATOM 3101 C PHE A 266 -11.407 4.138 0.115 1.00 18.94 C ANISOU 3101 C PHE A 266 2404 2423 2369 -9 -17 13 C ATOM 3102 O PHE A 266 -10.981 4.731 -0.878 1.00 18.71 O ANISOU 3102 O PHE A 266 2367 2488 2253 -23 -93 -38 O ATOM 3103 CB PHE A 266 -12.104 5.725 1.920 1.00 18.07 C ANISOU 3103 CB PHE A 266 2347 2332 2185 2 6 38 C ATOM 3104 CG PHE A 266 -13.111 6.779 2.346 1.00 16.88 C ANISOU 3104 CG PHE A 266 2250 2212 1950 19 21 98 C ATOM 3105 CD1 PHE A 266 -12.659 7.974 2.912 1.00 17.85 C ANISOU 3105 CD1 PHE A 266 2501 2399 1882 185 131 103 C ATOM 3106 CD2 PHE A 266 -14.468 6.592 2.217 1.00 18.07 C ANISOU 3106 CD2 PHE A 266 2414 2436 2013 36 94 34 C ATOM 3107 CE1 PHE A 266 -13.555 8.958 3.316 1.00 17.89 C ANISOU 3107 CE1 PHE A 266 2405 2296 2097 78 -2 -17 C ATOM 3108 CE2 PHE A 266 -15.369 7.579 2.626 1.00 19.45 C ANISOU 3108 CE2 PHE A 266 2690 2347 2352 -56 8 -46 C ATOM 3109 CZ PHE A 266 -14.911 8.752 3.175 1.00 18.78 C ANISOU 3109 CZ PHE A 266 2655 2397 2082 -20 81 -8 C ATOM 3110 N ILE A 267 -10.849 3.011 0.565 1.00 20.06 N ANISOU 3110 N ILE A 267 2509 2595 2517 42 -31 -8 N ATOM 3111 CA ILE A 267 -9.743 2.324 -0.150 1.00 21.00 C ANISOU 3111 CA ILE A 267 2636 2722 2620 17 5 -13 C ATOM 3112 C ILE A 267 -10.096 0.900 -0.651 1.00 21.88 C ANISOU 3112 C ILE A 267 2756 2844 2712 63 9 -38 C ATOM 3113 O ILE A 267 -9.213 0.093 -0.904 1.00 22.30 O ANISOU 3113 O ILE A 267 2759 3000 2714 136 -12 -73 O ATOM 3114 CB ILE A 267 -8.448 2.306 0.722 1.00 20.61 C ANISOU 3114 CB ILE A 267 2560 2665 2602 37 38 13 C ATOM 3115 CG1 ILE A 267 -8.684 1.600 2.060 1.00 21.67 C ANISOU 3115 CG1 ILE A 267 2694 2830 2710 52 -64 -66 C ATOM 3116 CG2 ILE A 267 -7.981 3.708 0.980 1.00 20.75 C ANISOU 3116 CG2 ILE A 267 2532 2708 2644 42 5 -9 C ATOM 3117 CD1 ILE A 267 -7.424 1.242 2.788 1.00 22.66 C ANISOU 3117 CD1 ILE A 267 2809 2988 2812 142 43 0 C ATOM 3118 N GLY A 268 -11.388 0.600 -0.791 1.00 22.62 N ANISOU 3118 N GLY A 268 2848 2925 2819 4 4 -59 N ATOM 3119 CA GLY A 268 -11.832 -0.639 -1.400 1.00 23.19 C ANISOU 3119 CA GLY A 268 2974 2958 2879 -8 23 -3 C ATOM 3120 C GLY A 268 -12.022 -1.810 -0.449 1.00 23.97 C ANISOU 3120 C GLY A 268 3081 3050 2974 -3 -22 -19 C ATOM 3121 O GLY A 268 -12.376 -2.901 -0.902 1.00 23.59 O ANISOU 3121 O GLY A 268 3193 2990 2778 -23 -76 -106 O ATOM 3122 N MET A 269 -11.809 -1.603 0.856 1.00 24.00 N ANISOU 3122 N MET A 269 3048 3091 2979 -26 -22 -48 N ATOM 3123 CA MET A 269 -11.950 -2.692 1.822 1.00 24.75 C ANISOU 3123 CA MET A 269 3133 3170 3099 12 -24 -34 C ATOM 3124 C MET A 269 -13.373 -2.823 2.285 1.00 24.33 C ANISOU 3124 C MET A 269 3050 3118 3076 -15 0 -27 C ATOM 3125 O MET A 269 -14.015 -1.828 2.574 1.00 23.98 O ANISOU 3125 O MET A 269 2995 3039 3075 -15 2 -30 O ATOM 3126 CB MET A 269 -11.111 -2.441 3.061 1.00 25.04 C ANISOU 3126 CB MET A 269 3148 3235 3129 15 -24 -66 C ATOM 3127 CG MET A 269 -9.673 -2.301 2.793 1.00 26.88 C ANISOU 3127 CG MET A 269 3380 3497 3334 1 -94 -29 C ATOM 3128 SD MET A 269 -8.840 -2.054 4.330 1.00 31.31 S ANISOU 3128 SD MET A 269 3638 4244 4015 102 -251 -332 S ATOM 3129 CE MET A 269 -7.104 -2.125 3.718 1.00 32.74 C ANISOU 3129 CE MET A 269 4063 4272 4104 44 -13 -157 C ATOM 3130 N GLU A 270 -13.840 -4.057 2.418 1.00 24.80 N ANISOU 3130 N GLU A 270 3144 3166 3112 31 -2 -60 N ATOM 3131 CA GLU A 270 -15.204 -4.329 2.872 1.00 25.23 C ANISOU 3131 CA GLU A 270 3152 3216 3215 -10 8 -37 C ATOM 3132 C GLU A 270 -15.299 -4.444 4.404 1.00 24.66 C ANISOU 3132 C GLU A 270 3081 3162 3128 -19 3 -25 C ATOM 3133 O GLU A 270 -16.373 -4.669 4.959 1.00 24.49 O ANISOU 3133 O GLU A 270 2952 3242 3110 -14 93 -17 O ATOM 3134 CB GLU A 270 -15.729 -5.608 2.224 1.00 25.92 C ANISOU 3134 CB GLU A 270 3234 3295 3320 28 -27 -77 C ATOM 3135 CG GLU A 270 -15.975 -5.486 0.731 1.00 28.94 C ANISOU 3135 CG GLU A 270 3506 3631 3857 11 -32 -132 C ATOM 3136 CD GLU A 270 -17.058 -6.440 0.237 1.00 32.12 C ANISOU 3136 CD GLU A 270 3545 4040 4618 -21 -115 -406 C ATOM 3137 OE1 GLU A 270 -16.704 -7.508 -0.306 1.00 34.59 O ANISOU 3137 OE1 GLU A 270 3580 4296 5266 46 -113 -565 O ATOM 3138 OE2 GLU A 270 -18.263 -6.120 0.401 1.00 35.14 O ANISOU 3138 OE2 GLU A 270 3637 4570 5143 30 -148 -507 O ATOM 3139 N SER A 271 -14.175 -4.261 5.078 1.00 23.59 N ANISOU 3139 N SER A 271 2926 3029 3009 10 -8 -14 N ATOM 3140 CA SER A 271 -14.113 -4.341 6.526 1.00 23.13 C ANISOU 3140 CA SER A 271 2873 2989 2924 23 -10 -55 C ATOM 3141 C SER A 271 -14.926 -3.258 7.238 1.00 21.32 C ANISOU 3141 C SER A 271 2717 2733 2649 -17 -62 -70 C ATOM 3142 O SER A 271 -15.144 -2.164 6.720 1.00 20.87 O ANISOU 3142 O SER A 271 2724 2729 2474 -52 -162 -246 O ATOM 3143 CB SER A 271 -12.651 -4.230 6.962 1.00 23.92 C ANISOU 3143 CB SER A 271 2932 3082 3073 30 15 -66 C ATOM 3144 OG SER A 271 -11.822 -5.037 6.102 1.00 27.25 O ANISOU 3144 OG SER A 271 3145 3579 3627 50 63 -176 O ATOM 3145 N ALA A 272 -15.364 -3.577 8.443 1.00 19.55 N ANISOU 3145 N ALA A 272 2501 2498 2428 -28 14 -62 N ATOM 3146 CA ALA A 272 -15.963 -2.588 9.322 1.00 18.90 C ANISOU 3146 CA ALA A 272 2454 2412 2313 -17 18 25 C ATOM 3147 C ALA A 272 -14.872 -1.594 9.756 1.00 17.15 C ANISOU 3147 C ALA A 272 2242 2246 2029 -1 -2 4 C ATOM 3148 O ALA A 272 -13.694 -1.935 9.784 1.00 16.77 O ANISOU 3148 O ALA A 272 2296 2233 1841 42 -31 97 O ATOM 3149 CB ALA A 272 -16.595 -3.289 10.523 1.00 19.61 C ANISOU 3149 CB ALA A 272 2523 2540 2385 16 46 -88 C ATOM 3150 N GLY A 273 -15.264 -0.357 10.051 1.00 16.11 N ANISOU 3150 N GLY A 273 2064 2102 1954 3 -25 47 N ATOM 3151 CA GLY A 273 -14.350 0.654 10.562 1.00 14.98 C ANISOU 3151 CA GLY A 273 1919 1923 1847 0 -5 -14 C ATOM 3152 C GLY A 273 -14.004 0.408 12.025 1.00 14.17 C ANISOU 3152 C GLY A 273 1806 1834 1742 0 -14 23 C ATOM 3153 O GLY A 273 -14.590 -0.439 12.677 1.00 13.05 O ANISOU 3153 O GLY A 273 1651 1721 1585 -34 -32 27 O ATOM 3154 N ILE A 274 -13.052 1.168 12.545 1.00 13.51 N ANISOU 3154 N ILE A 274 1719 1746 1665 -38 32 29 N ATOM 3155 CA ILE A 274 -12.474 0.886 13.864 1.00 13.87 C ANISOU 3155 CA ILE A 274 1760 1776 1731 -11 17 18 C ATOM 3156 C ILE A 274 -13.461 0.998 15.040 1.00 13.46 C ANISOU 3156 C ILE A 274 1705 1712 1696 39 55 -32 C ATOM 3157 O ILE A 274 -13.278 0.367 16.089 1.00 13.88 O ANISOU 3157 O ILE A 274 1795 1760 1715 70 123 -19 O ATOM 3158 CB ILE A 274 -11.206 1.734 14.113 1.00 13.66 C ANISOU 3158 CB ILE A 274 1732 1746 1710 -22 25 13 C ATOM 3159 CG1 ILE A 274 -11.474 3.239 13.938 1.00 14.39 C ANISOU 3159 CG1 ILE A 274 1756 1861 1848 3 14 -53 C ATOM 3160 CG2 ILE A 274 -10.071 1.261 13.174 1.00 14.04 C ANISOU 3160 CG2 ILE A 274 1853 1751 1730 -27 -92 -9 C ATOM 3161 CD1 ILE A 274 -10.322 4.116 14.436 1.00 14.92 C ANISOU 3161 CD1 ILE A 274 1972 1809 1887 -22 53 3 C ATOM 3162 N HIS A 275 -14.498 1.792 14.863 1.00 13.67 N ANISOU 3162 N HIS A 275 1722 1718 1751 55 48 -20 N ATOM 3163 CA HIS A 275 -15.569 1.912 15.875 1.00 13.57 C ANISOU 3163 CA HIS A 275 1695 1707 1752 68 74 -34 C ATOM 3164 C HIS A 275 -16.381 0.638 15.971 1.00 13.28 C ANISOU 3164 C HIS A 275 1564 1717 1762 135 71 -32 C ATOM 3165 O HIS A 275 -16.661 0.166 17.069 1.00 12.39 O ANISOU 3165 O HIS A 275 1357 1585 1763 247 219 -55 O ATOM 3166 CB HIS A 275 -16.477 3.119 15.594 1.00 13.37 C ANISOU 3166 CB HIS A 275 1642 1694 1741 102 49 -18 C ATOM 3167 CG HIS A 275 -17.154 3.080 14.259 1.00 14.88 C ANISOU 3167 CG HIS A 275 1924 1880 1850 250 -6 -257 C ATOM 3168 ND1 HIS A 275 -16.504 2.714 13.103 1.00 16.75 N ANISOU 3168 ND1 HIS A 275 2188 2284 1891 368 12 -157 N ATOM 3169 CD2 HIS A 275 -18.429 3.358 13.900 1.00 17.28 C ANISOU 3169 CD2 HIS A 275 2259 2410 1894 250 28 -234 C ATOM 3170 CE1 HIS A 275 -17.358 2.727 12.095 1.00 17.17 C ANISOU 3170 CE1 HIS A 275 2123 2433 1967 536 118 -101 C ATOM 3171 NE2 HIS A 275 -18.527 3.144 12.547 1.00 19.20 N ANISOU 3171 NE2 HIS A 275 2452 2666 2173 140 37 -316 N ATOM 3172 N GLU A 276 -16.712 0.070 14.812 1.00 13.82 N ANISOU 3172 N GLU A 276 1643 1769 1837 81 15 -32 N ATOM 3173 CA GLU A 276 -17.490 -1.153 14.722 1.00 14.47 C ANISOU 3173 CA GLU A 276 1786 1836 1875 11 -28 -2 C ATOM 3174 C GLU A 276 -16.682 -2.391 15.128 1.00 13.88 C ANISOU 3174 C GLU A 276 1704 1765 1805 8 -34 -39 C ATOM 3175 O GLU A 276 -17.235 -3.282 15.753 1.00 12.32 O ANISOU 3175 O GLU A 276 1381 1409 1890 -85 -119 -20 O ATOM 3176 CB GLU A 276 -18.091 -1.334 13.314 1.00 15.18 C ANISOU 3176 CB GLU A 276 1867 1928 1971 -75 -2 -48 C ATOM 3177 CG GLU A 276 -19.073 -2.505 13.258 1.00 19.43 C ANISOU 3177 CG GLU A 276 2460 2445 2476 19 -205 -65 C ATOM 3178 CD GLU A 276 -20.117 -2.423 12.139 1.00 24.49 C ANISOU 3178 CD GLU A 276 2901 3067 3334 -140 -492 24 C ATOM 3179 OE1 GLU A 276 -20.887 -3.409 12.000 1.00 26.83 O ANISOU 3179 OE1 GLU A 276 3072 3324 3797 -301 -769 -274 O ATOM 3180 OE2 GLU A 276 -20.170 -1.405 11.405 1.00 28.66 O ANISOU 3180 OE2 GLU A 276 3641 3452 3797 -124 -687 117 O ATOM 3181 N THR A 277 -15.384 -2.443 14.825 1.00 13.69 N ANISOU 3181 N THR A 277 1693 1753 1754 -21 -17 3 N ATOM 3182 CA THR A 277 -14.570 -3.577 15.297 1.00 14.41 C ANISOU 3182 CA THR A 277 1794 1816 1865 -16 21 -22 C ATOM 3183 C THR A 277 -14.361 -3.539 16.815 1.00 13.35 C ANISOU 3183 C THR A 277 1708 1676 1686 -9 -20 -53 C ATOM 3184 O THR A 277 -14.236 -4.585 17.439 1.00 12.85 O ANISOU 3184 O THR A 277 1768 1549 1562 -89 44 -182 O ATOM 3185 CB THR A 277 -13.186 -3.721 14.551 1.00 15.23 C ANISOU 3185 CB THR A 277 1956 1916 1915 11 13 -1 C ATOM 3186 OG1 THR A 277 -12.356 -2.578 14.768 1.00 14.90 O ANISOU 3186 OG1 THR A 277 1886 1739 2034 -203 43 107 O ATOM 3187 CG2 THR A 277 -13.361 -3.796 13.044 1.00 16.70 C ANISOU 3187 CG2 THR A 277 2200 2104 2038 50 -23 -21 C ATOM 3188 N THR A 278 -14.312 -2.338 17.401 1.00 13.09 N ANISOU 3188 N THR A 278 1604 1682 1688 27 -3 -11 N ATOM 3189 CA THR A 278 -14.220 -2.191 18.850 1.00 12.42 C ANISOU 3189 CA THR A 278 1478 1604 1636 30 -61 -13 C ATOM 3190 C THR A 278 -15.489 -2.801 19.473 1.00 12.28 C ANISOU 3190 C THR A 278 1411 1628 1626 8 -48 11 C ATOM 3191 O THR A 278 -15.423 -3.623 20.399 1.00 11.22 O ANISOU 3191 O THR A 278 1058 1604 1598 92 -120 -50 O ATOM 3192 CB THR A 278 -14.083 -0.700 19.245 1.00 12.47 C ANISOU 3192 CB THR A 278 1511 1642 1582 -15 -82 29 C ATOM 3193 OG1 THR A 278 -12.826 -0.182 18.781 1.00 12.52 O ANISOU 3193 OG1 THR A 278 1333 1674 1748 -72 -225 -110 O ATOM 3194 CG2 THR A 278 -14.012 -0.529 20.738 1.00 12.69 C ANISOU 3194 CG2 THR A 278 1400 1636 1787 74 -51 -15 C ATOM 3195 N TYR A 279 -16.644 -2.408 18.933 1.00 12.36 N ANISOU 3195 N TYR A 279 1452 1623 1620 24 -12 32 N ATOM 3196 CA TYR A 279 -17.933 -2.948 19.382 1.00 12.43 C ANISOU 3196 CA TYR A 279 1464 1632 1627 12 -26 29 C ATOM 3197 C TYR A 279 -18.032 -4.464 19.172 1.00 12.53 C ANISOU 3197 C TYR A 279 1441 1679 1638 5 -40 41 C ATOM 3198 O TYR A 279 -18.417 -5.204 20.092 1.00 11.96 O ANISOU 3198 O TYR A 279 1311 1580 1652 -29 0 155 O ATOM 3199 CB TYR A 279 -19.081 -2.210 18.691 1.00 12.63 C ANISOU 3199 CB TYR A 279 1542 1696 1559 16 -5 36 C ATOM 3200 CG TYR A 279 -20.448 -2.794 18.946 1.00 13.24 C ANISOU 3200 CG TYR A 279 1559 1776 1693 -23 -115 13 C ATOM 3201 CD1 TYR A 279 -21.120 -2.545 20.139 1.00 12.42 C ANISOU 3201 CD1 TYR A 279 1472 1601 1642 81 -34 151 C ATOM 3202 CD2 TYR A 279 -21.080 -3.570 17.984 1.00 16.09 C ANISOU 3202 CD2 TYR A 279 1981 2109 2021 -86 -1 -64 C ATOM 3203 CE1 TYR A 279 -22.377 -3.077 20.380 1.00 15.41 C ANISOU 3203 CE1 TYR A 279 1794 2166 1894 -7 -80 -227 C ATOM 3204 CE2 TYR A 279 -22.351 -4.109 18.215 1.00 16.50 C ANISOU 3204 CE2 TYR A 279 1818 2462 1987 -59 -34 -174 C ATOM 3205 CZ TYR A 279 -22.994 -3.853 19.415 1.00 17.22 C ANISOU 3205 CZ TYR A 279 1997 2476 2068 -75 26 -238 C ATOM 3206 OH TYR A 279 -24.253 -4.371 19.648 1.00 18.89 O ANISOU 3206 OH TYR A 279 2121 2949 2108 -63 -16 -552 O ATOM 3207 N ASN A 280 -17.652 -4.927 17.985 1.00 12.23 N ANISOU 3207 N ASN A 280 1446 1622 1575 28 -23 16 N ATOM 3208 CA ASN A 280 -17.669 -6.350 17.690 1.00 12.99 C ANISOU 3208 CA ASN A 280 1606 1659 1669 1 -17 41 C ATOM 3209 C ASN A 280 -16.787 -7.128 18.672 1.00 12.58 C ANISOU 3209 C ASN A 280 1558 1601 1621 29 -48 41 C ATOM 3210 O ASN A 280 -17.184 -8.203 19.125 1.00 13.12 O ANISOU 3210 O ASN A 280 1539 1631 1812 90 -81 126 O ATOM 3211 CB ASN A 280 -17.187 -6.657 16.261 1.00 13.13 C ANISOU 3211 CB ASN A 280 1647 1729 1610 5 -68 -3 C ATOM 3212 CG ASN A 280 -18.148 -6.195 15.194 1.00 14.49 C ANISOU 3212 CG ASN A 280 2018 1785 1701 3 -28 -1 C ATOM 3213 OD1 ASN A 280 -17.771 -6.074 14.021 1.00 19.17 O ANISOU 3213 OD1 ASN A 280 2826 2521 1934 253 58 -59 O ATOM 3214 ND2 ASN A 280 -19.380 -5.954 15.571 1.00 12.37 N ANISOU 3214 ND2 ASN A 280 1890 1538 1270 274 -87 -198 N ATOM 3215 N SER A 281 -15.609 -6.592 18.992 1.00 11.96 N ANISOU 3215 N SER A 281 1501 1459 1582 -19 -3 15 N ATOM 3216 CA SER A 281 -14.682 -7.244 19.927 1.00 12.03 C ANISOU 3216 CA SER A 281 1505 1476 1586 -37 -42 -3 C ATOM 3217 C SER A 281 -15.302 -7.365 21.337 1.00 12.24 C ANISOU 3217 C SER A 281 1581 1528 1541 -24 -115 -50 C ATOM 3218 O SER A 281 -15.282 -8.436 21.961 1.00 11.99 O ANISOU 3218 O SER A 281 1525 1489 1539 -112 -97 -148 O ATOM 3219 CB SER A 281 -13.349 -6.503 19.962 1.00 12.52 C ANISOU 3219 CB SER A 281 1602 1502 1650 22 -72 38 C ATOM 3220 OG SER A 281 -12.462 -7.051 20.918 1.00 12.90 O ANISOU 3220 OG SER A 281 1553 1530 1816 -47 -169 60 O ATOM 3221 N ILE A 282 -15.877 -6.269 21.812 1.00 12.53 N ANISOU 3221 N ILE A 282 1539 1611 1609 10 -70 -18 N ATOM 3222 CA ILE A 282 -16.541 -6.214 23.106 1.00 13.36 C ANISOU 3222 CA ILE A 282 1707 1697 1670 -7 -8 18 C ATOM 3223 C ILE A 282 -17.684 -7.235 23.156 1.00 13.73 C ANISOU 3223 C ILE A 282 1731 1777 1707 0 -16 -19 C ATOM 3224 O ILE A 282 -17.860 -7.933 24.150 1.00 14.54 O ANISOU 3224 O ILE A 282 1830 1789 1906 -70 46 -68 O ATOM 3225 CB ILE A 282 -17.047 -4.771 23.375 1.00 13.06 C ANISOU 3225 CB ILE A 282 1638 1704 1619 11 -12 0 C ATOM 3226 CG1 ILE A 282 -15.847 -3.836 23.627 1.00 14.21 C ANISOU 3226 CG1 ILE A 282 1894 1712 1790 2 19 55 C ATOM 3227 CG2 ILE A 282 -17.988 -4.723 24.585 1.00 14.49 C ANISOU 3227 CG2 ILE A 282 1784 1956 1763 10 10 119 C ATOM 3228 CD1 ILE A 282 -16.237 -2.389 23.868 1.00 15.38 C ANISOU 3228 CD1 ILE A 282 2112 1920 1812 41 -83 -35 C ATOM 3229 N MET A 283 -18.422 -7.362 22.065 1.00 15.17 N ANISOU 3229 N MET A 283 1888 1970 1905 10 19 15 N ATOM 3230 CA MET A 283 -19.570 -8.268 22.009 1.00 15.69 C ANISOU 3230 CA MET A 283 1960 2038 1963 -16 -22 11 C ATOM 3231 C MET A 283 -19.167 -9.722 21.982 1.00 16.09 C ANISOU 3231 C MET A 283 2000 2124 1988 0 -54 23 C ATOM 3232 O MET A 283 -19.983 -10.587 22.269 1.00 16.09 O ANISOU 3232 O MET A 283 1743 2210 2160 -62 -140 91 O ATOM 3233 CB MET A 283 -20.470 -7.936 20.812 1.00 16.28 C ANISOU 3233 CB MET A 283 1999 2080 2106 0 -9 -7 C ATOM 3234 CG MET A 283 -21.210 -6.612 20.976 1.00 16.93 C ANISOU 3234 CG MET A 283 2114 2058 2260 31 -22 16 C ATOM 3235 SD MET A 283 -22.304 -6.497 22.420 1.00 18.73 S ANISOU 3235 SD MET A 283 2539 1789 2789 -141 265 -78 S ATOM 3236 CE MET A 283 -23.516 -7.809 22.088 1.00 20.35 C ANISOU 3236 CE MET A 283 2370 2440 2919 8 80 -132 C ATOM 3237 N LYS A 284 -17.919 -10.008 21.631 1.00 16.75 N ANISOU 3237 N LYS A 284 2058 2216 2089 -46 -56 15 N ATOM 3238 CA LYS A 284 -17.393 -11.380 21.730 1.00 17.48 C ANISOU 3238 CA LYS A 284 2263 2216 2159 1 -35 3 C ATOM 3239 C LYS A 284 -17.010 -11.766 23.161 1.00 17.21 C ANISOU 3239 C LYS A 284 2270 2161 2105 2 -37 -6 C ATOM 3240 O LYS A 284 -16.730 -12.927 23.421 1.00 16.91 O ANISOU 3240 O LYS A 284 2399 2046 1979 91 -63 -70 O ATOM 3241 CB LYS A 284 -16.172 -11.565 20.834 1.00 17.88 C ANISOU 3241 CB LYS A 284 2290 2267 2234 -17 -50 18 C ATOM 3242 CG LYS A 284 -16.471 -11.434 19.333 1.00 21.28 C ANISOU 3242 CG LYS A 284 2884 2606 2594 2 -58 -7 C ATOM 3243 CD LYS A 284 -15.819 -12.526 18.525 1.00 25.62 C ANISOU 3243 CD LYS A 284 3278 3387 3068 125 -121 -62 C ATOM 3244 CE LYS A 284 -16.219 -12.460 17.030 1.00 29.33 C ANISOU 3244 CE LYS A 284 3785 3757 3599 75 -190 -95 C ATOM 3245 NZ LYS A 284 -16.774 -13.781 16.547 1.00 31.55 N ANISOU 3245 NZ LYS A 284 4234 3897 3855 -64 -361 -206 N ATOM 3246 N CYS A 285 -16.963 -10.800 24.077 1.00 16.93 N ANISOU 3246 N CYS A 285 2212 2121 2099 15 -10 -15 N ATOM 3247 CA CYS A 285 -16.620 -11.086 25.472 1.00 16.41 C ANISOU 3247 CA CYS A 285 2102 2088 2044 -35 14 -22 C ATOM 3248 C CYS A 285 -17.878 -11.310 26.300 1.00 17.56 C ANISOU 3248 C CYS A 285 2222 2259 2190 -51 18 -23 C ATOM 3249 O CYS A 285 -18.965 -10.857 25.944 1.00 17.13 O ANISOU 3249 O CYS A 285 2076 2270 2163 -114 193 -59 O ATOM 3250 CB CYS A 285 -15.810 -9.946 26.088 1.00 16.19 C ANISOU 3250 CB CYS A 285 2060 2089 2001 4 -6 -22 C ATOM 3251 SG CYS A 285 -14.329 -9.461 25.180 1.00 13.51 S ANISOU 3251 SG CYS A 285 1770 1683 1679 -189 -89 45 S ATOM 3252 N ASP A 286 -17.677 -11.995 27.418 1.00 18.71 N ANISOU 3252 N ASP A 286 2341 2380 2388 -86 40 46 N ATOM 3253 CA ASP A 286 -18.691 -12.267 28.434 1.00 20.15 C ANISOU 3253 CA ASP A 286 2511 2607 2535 -37 1 12 C ATOM 3254 C ASP A 286 -19.447 -10.994 28.775 1.00 19.89 C ANISOU 3254 C ASP A 286 2476 2584 2497 -48 22 27 C ATOM 3255 O ASP A 286 -18.831 -9.960 29.082 1.00 18.20 O ANISOU 3255 O ASP A 286 2120 2500 2292 -233 45 54 O ATOM 3256 CB ASP A 286 -17.980 -12.832 29.675 1.00 20.86 C ANISOU 3256 CB ASP A 286 2604 2724 2595 -48 33 88 C ATOM 3257 CG ASP A 286 -18.937 -13.272 30.784 1.00 25.48 C ANISOU 3257 CG ASP A 286 3007 3411 3260 8 -182 191 C ATOM 3258 OD1 ASP A 286 -20.160 -12.992 30.718 1.00 31.67 O ANISOU 3258 OD1 ASP A 286 3458 4246 4326 83 -467 242 O ATOM 3259 OD2 ASP A 286 -18.534 -13.912 31.782 1.00 30.26 O ANISOU 3259 OD2 ASP A 286 3869 4001 3624 25 -363 599 O ATOM 3260 N ILE A 287 -20.776 -11.062 28.719 1.00 19.73 N ANISOU 3260 N ILE A 287 2439 2545 2510 -84 -2 1 N ATOM 3261 CA ILE A 287 -21.610 -9.889 29.005 1.00 20.74 C ANISOU 3261 CA ILE A 287 2555 2694 2629 -37 -24 -45 C ATOM 3262 C ILE A 287 -21.266 -9.224 30.357 1.00 20.46 C ANISOU 3262 C ILE A 287 2512 2670 2589 -43 -16 -59 C ATOM 3263 O ILE A 287 -21.411 -8.020 30.496 1.00 21.13 O ANISOU 3263 O ILE A 287 2534 2896 2599 -74 -155 -162 O ATOM 3264 CB ILE A 287 -23.157 -10.203 28.879 1.00 20.60 C ANISOU 3264 CB ILE A 287 2572 2644 2610 -23 7 -64 C ATOM 3265 CG1 ILE A 287 -23.961 -8.886 28.902 1.00 22.46 C ANISOU 3265 CG1 ILE A 287 2702 2986 2843 -48 -42 -24 C ATOM 3266 CG2 ILE A 287 -23.612 -11.129 29.962 1.00 21.56 C ANISOU 3266 CG2 ILE A 287 2708 2705 2778 -61 9 -67 C ATOM 3267 CD1 ILE A 287 -25.344 -8.920 28.218 1.00 23.90 C ANISOU 3267 CD1 ILE A 287 3060 3027 2992 -48 41 3 C ATOM 3268 N ASP A 288 -20.768 -10.000 31.315 1.00 20.67 N ANISOU 3268 N ASP A 288 2563 2684 2603 -73 5 -36 N ATOM 3269 CA ASP A 288 -20.463 -9.497 32.657 1.00 21.23 C ANISOU 3269 CA ASP A 288 2665 2704 2696 -73 7 -22 C ATOM 3270 C ASP A 288 -19.216 -8.601 32.746 1.00 19.96 C ANISOU 3270 C ASP A 288 2464 2586 2531 -100 31 -50 C ATOM 3271 O ASP A 288 -18.991 -7.956 33.775 1.00 20.31 O ANISOU 3271 O ASP A 288 2485 2695 2537 -226 101 -110 O ATOM 3272 CB ASP A 288 -20.334 -10.673 33.648 1.00 22.05 C ANISOU 3272 CB ASP A 288 2749 2790 2838 -57 17 -23 C ATOM 3273 CG ASP A 288 -21.686 -11.312 33.972 1.00 25.21 C ANISOU 3273 CG ASP A 288 3144 3145 3290 8 12 -11 C ATOM 3274 OD1 ASP A 288 -21.750 -12.547 34.221 1.00 30.13 O ANISOU 3274 OD1 ASP A 288 4027 3609 3811 35 -48 -15 O ATOM 3275 OD2 ASP A 288 -22.749 -10.643 33.997 1.00 30.07 O ANISOU 3275 OD2 ASP A 288 3315 4032 4078 58 90 -38 O ATOM 3276 N ILE A 289 -18.395 -8.574 31.706 1.00 18.15 N ANISOU 3276 N ILE A 289 2299 2351 2245 -93 8 -17 N ATOM 3277 CA ILE A 289 -17.235 -7.676 31.690 1.00 17.21 C ANISOU 3277 CA ILE A 289 2155 2231 2152 -36 15 -27 C ATOM 3278 C ILE A 289 -17.357 -6.533 30.678 1.00 15.84 C ANISOU 3278 C ILE A 289 1952 2030 2037 -7 -9 39 C ATOM 3279 O ILE A 289 -16.487 -5.675 30.626 1.00 15.07 O ANISOU 3279 O ILE A 289 1685 2043 1995 -39 -45 80 O ATOM 3280 CB ILE A 289 -15.903 -8.452 31.468 1.00 16.76 C ANISOU 3280 CB ILE A 289 2117 2172 2079 40 23 0 C ATOM 3281 CG1 ILE A 289 -15.750 -8.859 29.991 1.00 17.26 C ANISOU 3281 CG1 ILE A 289 2117 2186 2252 38 44 -17 C ATOM 3282 CG2 ILE A 289 -15.807 -9.659 32.416 1.00 16.90 C ANISOU 3282 CG2 ILE A 289 2126 2089 2205 -25 71 -120 C ATOM 3283 CD1 ILE A 289 -14.307 -9.096 29.584 1.00 18.33 C ANISOU 3283 CD1 ILE A 289 2247 2405 2310 -56 -2 75 C ATOM 3284 N ARG A 290 -18.426 -6.504 29.889 1.00 14.88 N ANISOU 3284 N ARG A 290 1838 1947 1867 -132 5 -9 N ATOM 3285 CA ARG A 290 -18.553 -5.488 28.848 1.00 15.06 C ANISOU 3285 CA ARG A 290 1857 1938 1925 -49 -59 -40 C ATOM 3286 C ARG A 290 -18.607 -4.078 29.398 1.00 15.22 C ANISOU 3286 C ARG A 290 1875 2003 1902 -31 -103 -52 C ATOM 3287 O ARG A 290 -18.030 -3.154 28.821 1.00 14.36 O ANISOU 3287 O ARG A 290 1806 1881 1767 -152 -136 -109 O ATOM 3288 CB ARG A 290 -19.763 -5.735 27.962 1.00 14.83 C ANISOU 3288 CB ARG A 290 1807 1946 1880 -81 -20 -48 C ATOM 3289 CG ARG A 290 -19.643 -6.979 27.150 1.00 14.70 C ANISOU 3289 CG ARG A 290 1748 1986 1851 -174 -46 -53 C ATOM 3290 CD ARG A 290 -20.872 -7.229 26.288 1.00 16.00 C ANISOU 3290 CD ARG A 290 1956 2085 2036 -188 -15 -49 C ATOM 3291 NE ARG A 290 -20.877 -8.602 25.812 1.00 14.90 N ANISOU 3291 NE ARG A 290 1761 2000 1897 -280 -27 -322 N ATOM 3292 CZ ARG A 290 -21.965 -9.225 25.373 1.00 17.94 C ANISOU 3292 CZ ARG A 290 2123 2282 2410 -128 -3 -259 C ATOM 3293 NH1 ARG A 290 -23.130 -8.588 25.323 1.00 18.59 N ANISOU 3293 NH1 ARG A 290 2068 2397 2598 -347 -301 -217 N ATOM 3294 NH2 ARG A 290 -21.884 -10.486 24.983 1.00 18.65 N ANISOU 3294 NH2 ARG A 290 2248 2294 2544 -403 -40 -522 N ATOM 3295 N LYS A 291 -19.288 -3.905 30.511 1.00 15.50 N ANISOU 3295 N LYS A 291 1917 2046 1926 -60 -32 -48 N ATOM 3296 CA LYS A 291 -19.366 -2.584 31.115 1.00 16.90 C ANISOU 3296 CA LYS A 291 2154 2136 2131 -54 24 7 C ATOM 3297 C LYS A 291 -17.945 -2.017 31.385 1.00 15.67 C ANISOU 3297 C LYS A 291 1952 2039 1961 -67 27 4 C ATOM 3298 O LYS A 291 -17.672 -0.867 31.069 1.00 14.86 O ANISOU 3298 O LYS A 291 1870 1894 1880 -173 5 27 O ATOM 3299 CB LYS A 291 -20.216 -2.645 32.389 1.00 17.78 C ANISOU 3299 CB LYS A 291 2286 2214 2253 -51 109 -50 C ATOM 3300 CG LYS A 291 -20.456 -1.310 33.077 1.00 22.89 C ANISOU 3300 CG LYS A 291 2907 2799 2990 -2 78 31 C ATOM 3301 CD LYS A 291 -21.931 -1.095 33.566 1.00 26.48 C ANISOU 3301 CD LYS A 291 3297 3305 3456 41 -31 108 C ATOM 3302 CE LYS A 291 -22.696 -0.005 32.715 1.00 28.52 C ANISOU 3302 CE LYS A 291 3704 3512 3616 67 -87 122 C ATOM 3303 NZ LYS A 291 -21.861 1.196 32.244 1.00 25.49 N ANISOU 3303 NZ LYS A 291 3377 3350 2957 -31 -46 423 N ATOM 3304 N ASP A 292 -17.053 -2.835 31.934 1.00 15.07 N ANISOU 3304 N ASP A 292 1901 1948 1873 -42 66 48 N ATOM 3305 CA ASP A 292 -15.673 -2.405 32.220 1.00 15.36 C ANISOU 3305 CA ASP A 292 1976 1976 1883 -46 0 26 C ATOM 3306 C ASP A 292 -14.846 -2.164 30.951 1.00 14.56 C ANISOU 3306 C ASP A 292 1806 1911 1814 -68 0 -22 C ATOM 3307 O ASP A 292 -13.928 -1.348 30.929 1.00 16.36 O ANISOU 3307 O ASP A 292 2164 2234 1817 -239 17 -76 O ATOM 3308 CB ASP A 292 -14.958 -3.421 33.125 1.00 15.84 C ANISOU 3308 CB ASP A 292 2057 1999 1960 -38 53 34 C ATOM 3309 CG ASP A 292 -15.464 -3.369 34.568 1.00 18.90 C ANISOU 3309 CG ASP A 292 2750 2255 2173 158 21 61 C ATOM 3310 OD1 ASP A 292 -15.280 -4.358 35.305 1.00 23.59 O ANISOU 3310 OD1 ASP A 292 3872 2491 2599 -34 59 83 O ATOM 3311 OD2 ASP A 292 -16.068 -2.380 35.055 1.00 23.61 O ANISOU 3311 OD2 ASP A 292 3358 3123 2489 295 411 -136 O ATOM 3312 N LEU A 293 -15.158 -2.883 29.894 1.00 12.91 N ANISOU 3312 N LEU A 293 1592 1686 1627 -47 3 -67 N ATOM 3313 CA LEU A 293 -14.492 -2.679 28.632 1.00 12.65 C ANISOU 3313 CA LEU A 293 1498 1647 1661 5 12 -57 C ATOM 3314 C LEU A 293 -14.880 -1.314 28.020 1.00 11.58 C ANISOU 3314 C LEU A 293 1393 1477 1527 23 53 -86 C ATOM 3315 O LEU A 293 -14.015 -0.558 27.606 1.00 11.30 O ANISOU 3315 O LEU A 293 1308 1437 1547 87 156 -110 O ATOM 3316 CB LEU A 293 -14.842 -3.828 27.691 1.00 12.53 C ANISOU 3316 CB LEU A 293 1480 1669 1609 47 101 -188 C ATOM 3317 CG LEU A 293 -13.874 -4.995 27.466 1.00 15.71 C ANISOU 3317 CG LEU A 293 2037 1958 1975 44 -102 -27 C ATOM 3318 CD1 LEU A 293 -12.861 -5.319 28.538 1.00 15.03 C ANISOU 3318 CD1 LEU A 293 2297 1780 1631 160 -114 -7 C ATOM 3319 CD2 LEU A 293 -14.654 -6.206 27.066 1.00 14.30 C ANISOU 3319 CD2 LEU A 293 1593 1701 2137 -164 117 74 C ATOM 3320 N TYR A 294 -16.177 -0.983 28.029 1.00 10.81 N ANISOU 3320 N TYR A 294 1319 1360 1426 11 -49 -53 N ATOM 3321 CA TYR A 294 -16.681 0.263 27.443 1.00 10.34 C ANISOU 3321 CA TYR A 294 1257 1301 1370 13 -30 -25 C ATOM 3322 C TYR A 294 -16.128 1.478 28.192 1.00 10.08 C ANISOU 3322 C TYR A 294 1222 1248 1360 55 -6 30 C ATOM 3323 O TYR A 294 -15.863 2.533 27.600 1.00 10.12 O ANISOU 3323 O TYR A 294 1232 1206 1407 188 -162 207 O ATOM 3324 CB TYR A 294 -18.203 0.282 27.519 1.00 10.99 C ANISOU 3324 CB TYR A 294 1453 1338 1382 92 -115 -50 C ATOM 3325 CG TYR A 294 -18.958 -0.439 26.413 1.00 11.33 C ANISOU 3325 CG TYR A 294 1339 1425 1538 8 -192 9 C ATOM 3326 CD1 TYR A 294 -18.857 -0.010 25.096 1.00 11.57 C ANISOU 3326 CD1 TYR A 294 1423 1460 1513 24 -122 -68 C ATOM 3327 CD2 TYR A 294 -19.825 -1.498 26.701 1.00 11.67 C ANISOU 3327 CD2 TYR A 294 1395 1364 1672 191 -174 75 C ATOM 3328 CE1 TYR A 294 -19.571 -0.616 24.083 1.00 11.68 C ANISOU 3328 CE1 TYR A 294 1671 1380 1386 13 -132 67 C ATOM 3329 CE2 TYR A 294 -20.555 -2.124 25.683 1.00 10.61 C ANISOU 3329 CE2 TYR A 294 1327 1297 1404 198 -20 -2 C ATOM 3330 CZ TYR A 294 -20.426 -1.663 24.378 1.00 12.52 C ANISOU 3330 CZ TYR A 294 1601 1549 1604 64 -90 -118 C ATOM 3331 OH TYR A 294 -21.123 -2.237 23.349 1.00 14.09 O ANISOU 3331 OH TYR A 294 2051 1851 1450 -22 -285 0 O ATOM 3332 N ALA A 295 -15.941 1.325 29.494 1.00 9.09 N ANISOU 3332 N ALA A 295 1125 1086 1240 37 -59 48 N ATOM 3333 CA ALA A 295 -15.448 2.414 30.328 1.00 9.18 C ANISOU 3333 CA ALA A 295 1131 1137 1220 58 -10 18 C ATOM 3334 C ALA A 295 -13.929 2.568 30.259 1.00 9.33 C ANISOU 3334 C ALA A 295 1151 1125 1266 59 -46 -19 C ATOM 3335 O ALA A 295 -13.402 3.491 30.855 1.00 9.74 O ANISOU 3335 O ALA A 295 1094 1202 1404 186 34 -136 O ATOM 3336 CB ALA A 295 -15.906 2.228 31.762 1.00 9.75 C ANISOU 3336 CB ALA A 295 1208 1160 1335 8 -120 -81 C ATOM 3337 N ASN A 296 -13.230 1.678 29.535 1.00 9.77 N ANISOU 3337 N ASN A 296 1182 1248 1282 60 2 5 N ATOM 3338 CA ASN A 296 -11.762 1.653 29.540 1.00 9.67 C ANISOU 3338 CA ASN A 296 1196 1160 1316 32 -35 20 C ATOM 3339 C ASN A 296 -11.167 1.343 28.159 1.00 9.95 C ANISOU 3339 C ASN A 296 1170 1229 1382 -1 -77 -6 C ATOM 3340 O ASN A 296 -10.394 0.390 28.000 1.00 9.23 O ANISOU 3340 O ASN A 296 1171 1023 1310 69 -159 -15 O ATOM 3341 CB ASN A 296 -11.256 0.645 30.602 1.00 9.86 C ANISOU 3341 CB ASN A 296 1202 1243 1299 101 0 1 C ATOM 3342 CG ASN A 296 -11.590 1.057 32.006 1.00 10.70 C ANISOU 3342 CG ASN A 296 1251 1405 1409 -12 -167 167 C ATOM 3343 OD1 ASN A 296 -10.875 1.869 32.585 1.00 9.80 O ANISOU 3343 OD1 ASN A 296 865 1419 1436 -46 -280 347 O ATOM 3344 ND2 ASN A 296 -12.712 0.524 32.569 1.00 7.46 N ANISOU 3344 ND2 ASN A 296 479 1350 1003 90 84 164 N ATOM 3345 N ASN A 297 -11.544 2.147 27.163 1.00 10.07 N ANISOU 3345 N ASN A 297 1223 1144 1459 -41 -50 51 N ATOM 3346 CA ASN A 297 -11.018 2.048 25.803 1.00 11.42 C ANISOU 3346 CA ASN A 297 1389 1346 1601 10 4 -41 C ATOM 3347 C ASN A 297 -9.754 2.871 25.687 1.00 10.97 C ANISOU 3347 C ASN A 297 1289 1278 1598 1 31 -4 C ATOM 3348 O ASN A 297 -9.841 4.087 25.595 1.00 12.24 O ANISOU 3348 O ASN A 297 1215 1476 1959 -14 71 -38 O ATOM 3349 CB ASN A 297 -11.947 2.703 24.789 1.00 12.55 C ANISOU 3349 CB ASN A 297 1557 1511 1700 -21 -35 -63 C ATOM 3350 CG ASN A 297 -13.163 1.922 24.495 1.00 16.76 C ANISOU 3350 CG ASN A 297 2134 2082 2152 29 76 -255 C ATOM 3351 OD1 ASN A 297 -14.189 2.033 25.204 1.00 26.53 O ANISOU 3351 OD1 ASN A 297 3540 3360 3177 15 -47 -573 O ATOM 3352 ND2 ASN A 297 -13.123 1.183 23.389 1.00 23.90 N ANISOU 3352 ND2 ASN A 297 2854 3611 2615 249 11 -575 N ATOM 3353 N VAL A 298 -8.601 2.222 25.632 1.00 10.37 N ANISOU 3353 N VAL A 298 1240 1285 1415 16 1 11 N ATOM 3354 CA VAL A 298 -7.310 2.905 25.582 1.00 9.61 C ANISOU 3354 CA VAL A 298 1221 1161 1270 30 -2 -30 C ATOM 3355 C VAL A 298 -6.764 2.875 24.159 1.00 10.01 C ANISOU 3355 C VAL A 298 1268 1208 1327 0 7 -33 C ATOM 3356 O VAL A 298 -6.650 1.800 23.551 1.00 10.58 O ANISOU 3356 O VAL A 298 1476 1166 1377 -117 80 -133 O ATOM 3357 CB VAL A 298 -6.315 2.220 26.555 1.00 9.31 C ANISOU 3357 CB VAL A 298 1147 1254 1135 19 4 -59 C ATOM 3358 CG1 VAL A 298 -4.944 2.875 26.474 1.00 9.97 C ANISOU 3358 CG1 VAL A 298 1281 1503 1002 -82 -208 105 C ATOM 3359 CG2 VAL A 298 -6.839 2.266 27.969 1.00 9.62 C ANISOU 3359 CG2 VAL A 298 1159 1195 1299 75 -58 183 C ATOM 3360 N MET A 299 -6.397 4.037 23.638 1.00 9.88 N ANISOU 3360 N MET A 299 1329 1112 1312 62 15 -61 N ATOM 3361 CA MET A 299 -5.784 4.160 22.321 1.00 10.71 C ANISOU 3361 CA MET A 299 1362 1315 1389 15 -15 -21 C ATOM 3362 C MET A 299 -4.263 4.193 22.403 1.00 10.23 C ANISOU 3362 C MET A 299 1336 1244 1304 -14 -46 -15 C ATOM 3363 O MET A 299 -3.701 4.935 23.206 1.00 9.78 O ANISOU 3363 O MET A 299 1312 1097 1304 -55 -8 -148 O ATOM 3364 CB MET A 299 -6.268 5.437 21.644 1.00 11.03 C ANISOU 3364 CB MET A 299 1318 1441 1432 -4 -48 -49 C ATOM 3365 CG MET A 299 -7.719 5.333 21.191 1.00 15.86 C ANISOU 3365 CG MET A 299 1940 2012 2074 199 171 168 C ATOM 3366 SD MET A 299 -8.201 6.838 20.404 1.00 22.82 S ANISOU 3366 SD MET A 299 2315 3475 2880 476 16 22 S ATOM 3367 CE MET A 299 -9.681 6.293 19.883 1.00 23.52 C ANISOU 3367 CE MET A 299 2857 3162 2918 20 77 -139 C ATOM 3368 N SER A 300 -3.597 3.390 21.582 1.00 9.94 N ANISOU 3368 N SER A 300 1393 1173 1210 -73 -72 -47 N ATOM 3369 CA SER A 300 -2.149 3.457 21.479 1.00 10.90 C ANISOU 3369 CA SER A 300 1547 1272 1319 -35 -20 2 C ATOM 3370 C SER A 300 -1.668 3.328 20.061 1.00 10.67 C ANISOU 3370 C SER A 300 1430 1315 1306 -71 -36 -47 C ATOM 3371 O SER A 300 -2.365 2.768 19.196 1.00 11.16 O ANISOU 3371 O SER A 300 1428 1590 1222 -212 76 -19 O ATOM 3372 CB SER A 300 -1.450 2.434 22.385 1.00 12.34 C ANISOU 3372 CB SER A 300 1830 1356 1499 -169 -47 -39 C ATOM 3373 OG SER A 300 -1.719 1.124 21.984 1.00 15.77 O ANISOU 3373 OG SER A 300 3091 1210 1689 44 -1 63 O ATOM 3374 N GLY A 301 -0.477 3.880 19.822 1.00 9.55 N ANISOU 3374 N GLY A 301 1283 1176 1168 -76 -16 -18 N ATOM 3375 CA GLY A 301 0.171 3.817 18.535 1.00 9.20 C ANISOU 3375 CA GLY A 301 1207 1158 1126 -1 -28 -11 C ATOM 3376 C GLY A 301 0.017 5.101 17.751 1.00 8.90 C ANISOU 3376 C GLY A 301 1203 1108 1070 3 -36 5 C ATOM 3377 O GLY A 301 -0.889 5.900 18.004 1.00 8.55 O ANISOU 3377 O GLY A 301 1231 1095 922 33 -180 104 O ATOM 3378 N GLY A 302 0.905 5.262 16.777 1.00 9.28 N ANISOU 3378 N GLY A 302 1229 1100 1197 22 -77 19 N ATOM 3379 CA GLY A 302 1.035 6.470 15.989 1.00 9.45 C ANISOU 3379 CA GLY A 302 1191 1169 1230 -36 -9 44 C ATOM 3380 C GLY A 302 -0.203 6.854 15.215 1.00 9.67 C ANISOU 3380 C GLY A 302 1229 1174 1269 -14 -14 64 C ATOM 3381 O GLY A 302 -0.501 8.038 15.092 1.00 8.83 O ANISOU 3381 O GLY A 302 1057 922 1376 -18 96 88 O ATOM 3382 N THR A 303 -0.922 5.857 14.701 1.00 9.26 N ANISOU 3382 N THR A 303 1194 1132 1190 -31 5 42 N ATOM 3383 CA THR A 303 -2.094 6.109 13.894 1.00 9.83 C ANISOU 3383 CA THR A 303 1273 1248 1215 15 -22 51 C ATOM 3384 C THR A 303 -3.317 6.525 14.736 1.00 10.33 C ANISOU 3384 C THR A 303 1304 1374 1247 74 -53 53 C ATOM 3385 O THR A 303 -4.295 6.980 14.191 1.00 11.16 O ANISOU 3385 O THR A 303 1329 1586 1324 173 -130 37 O ATOM 3386 CB THR A 303 -2.339 4.899 12.944 1.00 9.92 C ANISOU 3386 CB THR A 303 1270 1269 1226 48 -25 77 C ATOM 3387 OG1 THR A 303 -1.308 4.892 11.951 1.00 11.53 O ANISOU 3387 OG1 THR A 303 1650 1475 1254 36 -114 -75 O ATOM 3388 CG2 THR A 303 -3.622 5.008 12.118 1.00 10.54 C ANISOU 3388 CG2 THR A 303 1383 1250 1368 -31 -15 9 C ATOM 3389 N THR A 304 -3.245 6.425 16.062 1.00 10.72 N ANISOU 3389 N THR A 304 1299 1513 1260 93 -44 43 N ATOM 3390 CA THR A 304 -4.260 7.041 16.923 1.00 10.96 C ANISOU 3390 CA THR A 304 1415 1470 1278 99 -45 64 C ATOM 3391 C THR A 304 -3.963 8.473 17.285 1.00 10.71 C ANISOU 3391 C THR A 304 1405 1424 1237 61 -93 103 C ATOM 3392 O THR A 304 -4.700 9.066 18.072 1.00 11.38 O ANISOU 3392 O THR A 304 1615 1515 1193 98 -171 151 O ATOM 3393 CB THR A 304 -4.478 6.235 18.246 1.00 11.04 C ANISOU 3393 CB THR A 304 1416 1494 1284 57 -32 85 C ATOM 3394 OG1 THR A 304 -3.351 6.392 19.135 1.00 9.94 O ANISOU 3394 OG1 THR A 304 1147 1381 1248 283 -4 31 O ATOM 3395 CG2 THR A 304 -4.615 4.742 17.960 1.00 10.68 C ANISOU 3395 CG2 THR A 304 1518 1406 1131 102 35 77 C ATOM 3396 N MET A 305 -2.937 9.061 16.690 1.00 11.16 N ANISOU 3396 N MET A 305 1370 1546 1325 153 -127 44 N ATOM 3397 CA MET A 305 -2.533 10.415 17.058 1.00 11.83 C ANISOU 3397 CA MET A 305 1509 1553 1432 60 -84 39 C ATOM 3398 C MET A 305 -3.318 11.567 16.406 1.00 11.65 C ANISOU 3398 C MET A 305 1490 1481 1454 63 -123 16 C ATOM 3399 O MET A 305 -3.101 12.705 16.773 1.00 12.12 O ANISOU 3399 O MET A 305 1532 1519 1554 78 -291 3 O ATOM 3400 CB MET A 305 -1.037 10.617 16.797 1.00 12.53 C ANISOU 3400 CB MET A 305 1612 1701 1446 53 -97 67 C ATOM 3401 CG MET A 305 -0.098 9.910 17.778 1.00 15.07 C ANISOU 3401 CG MET A 305 1959 1920 1847 142 3 39 C ATOM 3402 SD MET A 305 -0.294 10.405 19.500 1.00 19.83 S ANISOU 3402 SD MET A 305 2681 2658 2196 206 -174 440 S ATOM 3403 CE MET A 305 -0.371 12.111 19.392 1.00 24.98 C ANISOU 3403 CE MET A 305 3297 3254 2939 132 -52 34 C ATOM 3404 N TYR A 306 -4.221 11.293 15.471 1.00 11.55 N ANISOU 3404 N TYR A 306 1490 1456 1440 70 -83 -13 N ATOM 3405 CA TYR A 306 -4.976 12.357 14.786 1.00 11.25 C ANISOU 3405 CA TYR A 306 1427 1461 1384 29 -15 14 C ATOM 3406 C TYR A 306 -5.775 13.188 15.780 1.00 11.93 C ANISOU 3406 C TYR A 306 1524 1519 1488 32 -43 0 C ATOM 3407 O TYR A 306 -6.517 12.612 16.614 1.00 12.32 O ANISOU 3407 O TYR A 306 1496 1765 1419 137 73 -79 O ATOM 3408 CB TYR A 306 -5.960 11.749 13.773 1.00 11.22 C ANISOU 3408 CB TYR A 306 1443 1402 1417 95 -32 20 C ATOM 3409 CG TYR A 306 -5.273 11.044 12.635 1.00 11.37 C ANISOU 3409 CG TYR A 306 1472 1474 1372 35 25 32 C ATOM 3410 CD1 TYR A 306 -4.763 11.755 11.552 1.00 11.94 C ANISOU 3410 CD1 TYR A 306 1725 1269 1543 67 104 108 C ATOM 3411 CD2 TYR A 306 -5.097 9.672 12.659 1.00 9.69 C ANISOU 3411 CD2 TYR A 306 1290 1078 1313 92 -33 -47 C ATOM 3412 CE1 TYR A 306 -4.112 11.106 10.512 1.00 11.61 C ANISOU 3412 CE1 TYR A 306 1624 1337 1447 54 115 -6 C ATOM 3413 CE2 TYR A 306 -4.460 9.014 11.629 1.00 11.28 C ANISOU 3413 CE2 TYR A 306 1354 1510 1419 43 50 93 C ATOM 3414 CZ TYR A 306 -3.962 9.727 10.562 1.00 12.59 C ANISOU 3414 CZ TYR A 306 1828 1464 1489 121 95 36 C ATOM 3415 OH TYR A 306 -3.306 9.052 9.545 1.00 14.71 O ANISOU 3415 OH TYR A 306 2433 1472 1683 82 368 0 O ATOM 3416 N PRO A 307 -5.668 14.515 15.716 1.00 12.41 N ANISOU 3416 N PRO A 307 1575 1599 1541 -12 4 -4 N ATOM 3417 CA PRO A 307 -6.590 15.361 16.483 1.00 12.24 C ANISOU 3417 CA PRO A 307 1553 1559 1538 -29 46 -5 C ATOM 3418 C PRO A 307 -8.019 14.991 16.148 1.00 12.10 C ANISOU 3418 C PRO A 307 1522 1565 1508 5 31 36 C ATOM 3419 O PRO A 307 -8.311 14.710 14.977 1.00 11.85 O ANISOU 3419 O PRO A 307 1466 1477 1559 -71 183 -82 O ATOM 3420 CB PRO A 307 -6.269 16.771 15.996 1.00 12.80 C ANISOU 3420 CB PRO A 307 1650 1639 1573 11 2 7 C ATOM 3421 CG PRO A 307 -4.809 16.696 15.557 1.00 12.78 C ANISOU 3421 CG PRO A 307 1608 1653 1595 54 37 12 C ATOM 3422 CD PRO A 307 -4.708 15.321 14.930 1.00 12.24 C ANISOU 3422 CD PRO A 307 1582 1525 1542 -40 -9 -72 C ATOM 3423 N GLY A 308 -8.880 14.922 17.164 1.00 11.70 N ANISOU 3423 N GLY A 308 1461 1522 1460 16 66 20 N ATOM 3424 CA GLY A 308 -10.284 14.592 16.965 1.00 11.79 C ANISOU 3424 CA GLY A 308 1482 1521 1477 -29 20 37 C ATOM 3425 C GLY A 308 -10.652 13.107 17.072 1.00 11.98 C ANISOU 3425 C GLY A 308 1498 1529 1524 -5 25 52 C ATOM 3426 O GLY A 308 -11.848 12.767 17.167 1.00 11.40 O ANISOU 3426 O GLY A 308 1325 1530 1476 -38 31 152 O ATOM 3427 N ILE A 309 -9.673 12.209 17.046 1.00 11.41 N ANISOU 3427 N ILE A 309 1397 1483 1452 38 34 79 N ATOM 3428 CA ILE A 309 -10.015 10.788 16.987 1.00 12.13 C ANISOU 3428 CA ILE A 309 1495 1563 1547 35 38 9 C ATOM 3429 C ILE A 309 -10.721 10.301 18.252 1.00 12.02 C ANISOU 3429 C ILE A 309 1489 1507 1570 56 51 38 C ATOM 3430 O ILE A 309 -11.631 9.490 18.146 1.00 11.95 O ANISOU 3430 O ILE A 309 1336 1642 1563 241 198 59 O ATOM 3431 CB ILE A 309 -8.793 9.875 16.602 1.00 12.45 C ANISOU 3431 CB ILE A 309 1568 1546 1616 2 12 8 C ATOM 3432 CG1 ILE A 309 -9.295 8.488 16.222 1.00 14.99 C ANISOU 3432 CG1 ILE A 309 1782 1886 2028 50 92 -62 C ATOM 3433 CG2 ILE A 309 -7.799 9.758 17.713 1.00 12.08 C ANISOU 3433 CG2 ILE A 309 1486 1495 1606 -1 48 95 C ATOM 3434 CD1 ILE A 309 -8.247 7.590 15.604 1.00 16.78 C ANISOU 3434 CD1 ILE A 309 2017 2155 2204 142 208 -77 C ATOM 3435 N ALA A 310 -10.346 10.810 19.422 1.00 12.63 N ANISOU 3435 N ALA A 310 1586 1605 1608 24 33 39 N ATOM 3436 CA ALA A 310 -10.965 10.359 20.683 1.00 13.55 C ANISOU 3436 CA ALA A 310 1714 1726 1707 -15 -23 -23 C ATOM 3437 C ALA A 310 -12.420 10.766 20.736 1.00 13.79 C ANISOU 3437 C ALA A 310 1768 1765 1704 -27 -6 -42 C ATOM 3438 O ALA A 310 -13.270 9.969 21.076 1.00 13.34 O ANISOU 3438 O ALA A 310 1704 1766 1598 -130 -52 -113 O ATOM 3439 CB ALA A 310 -10.240 10.920 21.907 1.00 14.64 C ANISOU 3439 CB ALA A 310 1857 1862 1843 42 -30 38 C ATOM 3440 N ASP A 311 -12.692 12.019 20.392 1.00 14.21 N ANISOU 3440 N ASP A 311 1802 1804 1792 -12 -41 -4 N ATOM 3441 CA ASP A 311 -14.054 12.543 20.396 1.00 14.65 C ANISOU 3441 CA ASP A 311 1857 1828 1880 -49 -30 -39 C ATOM 3442 C ASP A 311 -14.927 11.822 19.359 1.00 13.39 C ANISOU 3442 C ASP A 311 1746 1726 1612 -19 -34 -63 C ATOM 3443 O ASP A 311 -16.099 11.554 19.619 1.00 11.17 O ANISOU 3443 O ASP A 311 1382 1536 1324 -56 -81 -197 O ATOM 3444 CB ASP A 311 -14.043 14.057 20.164 1.00 15.73 C ANISOU 3444 CB ASP A 311 2032 1952 1990 -35 -74 -43 C ATOM 3445 CG ASP A 311 -13.556 14.834 21.406 1.00 19.11 C ANISOU 3445 CG ASP A 311 2565 2271 2425 -167 -162 15 C ATOM 3446 OD1 ASP A 311 -13.233 16.035 21.281 1.00 25.33 O ANISOU 3446 OD1 ASP A 311 3374 2642 3607 -159 -262 -65 O ATOM 3447 OD2 ASP A 311 -13.454 14.317 22.544 1.00 23.73 O ANISOU 3447 OD2 ASP A 311 3340 3016 2658 -329 -271 121 O ATOM 3448 N ARG A 312 -14.340 11.460 18.215 1.00 13.15 N ANISOU 3448 N ARG A 312 1638 1664 1692 -54 19 -17 N ATOM 3449 CA ARG A 312 -15.067 10.712 17.204 1.00 12.22 C ANISOU 3449 CA ARG A 312 1582 1577 1484 -29 6 -7 C ATOM 3450 C ARG A 312 -15.385 9.299 17.702 1.00 12.31 C ANISOU 3450 C ARG A 312 1584 1629 1463 -59 40 17 C ATOM 3451 O ARG A 312 -16.506 8.846 17.557 1.00 12.28 O ANISOU 3451 O ARG A 312 1582 1656 1426 -62 165 99 O ATOM 3452 CB ARG A 312 -14.276 10.628 15.919 1.00 12.51 C ANISOU 3452 CB ARG A 312 1566 1610 1574 -70 -33 48 C ATOM 3453 CG ARG A 312 -15.006 9.930 14.763 1.00 12.67 C ANISOU 3453 CG ARG A 312 1672 1543 1599 -98 60 -18 C ATOM 3454 CD ARG A 312 -16.323 10.557 14.273 1.00 12.92 C ANISOU 3454 CD ARG A 312 1719 1474 1713 -52 40 -35 C ATOM 3455 NE ARG A 312 -16.838 9.746 13.172 1.00 12.48 N ANISOU 3455 NE ARG A 312 1729 1650 1361 6 -186 102 N ATOM 3456 CZ ARG A 312 -16.397 9.793 11.917 1.00 14.39 C ANISOU 3456 CZ ARG A 312 1772 1925 1768 -123 -163 137 C ATOM 3457 NH1 ARG A 312 -16.911 8.960 11.013 1.00 13.52 N ANISOU 3457 NH1 ARG A 312 2004 1635 1497 -93 -1 85 N ATOM 3458 NH2 ARG A 312 -15.492 10.685 11.539 1.00 14.95 N ANISOU 3458 NH2 ARG A 312 1628 2232 1818 -143 -311 38 N ATOM 3459 N MET A 313 -14.402 8.619 18.286 1.00 11.95 N ANISOU 3459 N MET A 313 1491 1622 1428 -34 120 21 N ATOM 3460 CA MET A 313 -14.614 7.284 18.833 1.00 12.95 C ANISOU 3460 CA MET A 313 1647 1668 1603 -7 28 -30 C ATOM 3461 C MET A 313 -15.683 7.286 19.925 1.00 12.83 C ANISOU 3461 C MET A 313 1669 1637 1568 -39 57 58 C ATOM 3462 O MET A 313 -16.534 6.431 19.930 1.00 13.38 O ANISOU 3462 O MET A 313 1709 1700 1672 -94 105 143 O ATOM 3463 CB MET A 313 -13.322 6.680 19.362 1.00 13.32 C ANISOU 3463 CB MET A 313 1731 1786 1542 -34 0 -80 C ATOM 3464 CG MET A 313 -12.420 6.199 18.251 1.00 17.14 C ANISOU 3464 CG MET A 313 2140 2131 2241 22 -142 -83 C ATOM 3465 SD MET A 313 -12.795 4.565 17.546 1.00 25.62 S ANISOU 3465 SD MET A 313 3508 3201 3023 60 -377 -536 S ATOM 3466 CE MET A 313 -13.955 3.965 18.534 1.00 19.61 C ANISOU 3466 CE MET A 313 2495 2504 2449 -20 104 9 C ATOM 3467 N GLN A 314 -15.643 8.278 20.810 1.00 12.74 N ANISOU 3467 N GLN A 314 1637 1652 1551 -12 46 78 N ATOM 3468 CA GLN A 314 -16.626 8.414 21.874 1.00 12.81 C ANISOU 3468 CA GLN A 314 1630 1620 1614 6 63 77 C ATOM 3469 C GLN A 314 -18.036 8.479 21.264 1.00 12.63 C ANISOU 3469 C GLN A 314 1614 1585 1598 30 70 100 C ATOM 3470 O GLN A 314 -18.930 7.774 21.701 1.00 11.06 O ANISOU 3470 O GLN A 314 1334 1314 1554 -22 159 273 O ATOM 3471 CB GLN A 314 -16.340 9.662 22.727 1.00 13.38 C ANISOU 3471 CB GLN A 314 1739 1740 1602 -27 85 95 C ATOM 3472 CG GLN A 314 -17.426 9.979 23.783 1.00 16.01 C ANISOU 3472 CG GLN A 314 2030 2035 2018 52 259 6 C ATOM 3473 CD GLN A 314 -17.294 9.139 25.052 1.00 17.79 C ANISOU 3473 CD GLN A 314 2053 2447 2260 147 434 44 C ATOM 3474 OE1 GLN A 314 -16.185 8.706 25.399 1.00 21.10 O ANISOU 3474 OE1 GLN A 314 2415 3095 2507 119 1141 -71 O ATOM 3475 NE2 GLN A 314 -18.419 8.926 25.767 1.00 19.00 N ANISOU 3475 NE2 GLN A 314 2084 2530 2602 27 757 14 N ATOM 3476 N LYS A 315 -18.205 9.308 20.231 1.00 11.71 N ANISOU 3476 N LYS A 315 1584 1440 1423 53 72 121 N ATOM 3477 CA LYS A 315 -19.487 9.473 19.577 1.00 12.08 C ANISOU 3477 CA LYS A 315 1618 1490 1481 12 45 69 C ATOM 3478 C LYS A 315 -19.959 8.179 18.923 1.00 11.57 C ANISOU 3478 C LYS A 315 1582 1361 1453 34 36 167 C ATOM 3479 O LYS A 315 -21.108 7.783 19.073 1.00 11.01 O ANISOU 3479 O LYS A 315 1473 1289 1420 19 9 201 O ATOM 3480 CB LYS A 315 -19.382 10.592 18.512 1.00 12.39 C ANISOU 3480 CB LYS A 315 1700 1469 1539 62 25 78 C ATOM 3481 CG LYS A 315 -20.649 10.857 17.735 1.00 15.28 C ANISOU 3481 CG LYS A 315 2022 1856 1927 -46 2 25 C ATOM 3482 CD LYS A 315 -20.492 12.139 16.893 1.00 18.90 C ANISOU 3482 CD LYS A 315 2501 2376 2303 51 -140 -39 C ATOM 3483 CE LYS A 315 -21.605 12.290 15.881 1.00 22.25 C ANISOU 3483 CE LYS A 315 2956 2770 2726 21 -93 -168 C ATOM 3484 NZ LYS A 315 -21.227 11.579 14.631 1.00 25.10 N ANISOU 3484 NZ LYS A 315 3240 3271 3025 172 -410 -463 N ATOM 3485 N GLU A 316 -19.070 7.530 18.185 1.00 11.26 N ANISOU 3485 N GLU A 316 1586 1332 1361 11 26 127 N ATOM 3486 CA GLU A 316 -19.449 6.347 17.418 1.00 12.02 C ANISOU 3486 CA GLU A 316 1580 1500 1487 -43 6 67 C ATOM 3487 C GLU A 316 -19.758 5.144 18.317 1.00 12.06 C ANISOU 3487 C GLU A 316 1602 1495 1483 -20 14 45 C ATOM 3488 O GLU A 316 -20.749 4.425 18.105 1.00 11.57 O ANISOU 3488 O GLU A 316 1619 1385 1390 -198 4 97 O ATOM 3489 CB GLU A 316 -18.353 5.989 16.403 1.00 11.93 C ANISOU 3489 CB GLU A 316 1568 1512 1452 -17 -25 33 C ATOM 3490 CG GLU A 316 -18.114 7.024 15.306 1.00 13.00 C ANISOU 3490 CG GLU A 316 1551 1628 1760 -140 -27 96 C ATOM 3491 CD GLU A 316 -19.306 7.334 14.428 1.00 16.82 C ANISOU 3491 CD GLU A 316 2203 2054 2133 -283 -168 480 C ATOM 3492 OE1 GLU A 316 -19.191 8.266 13.599 1.00 18.12 O ANISOU 3492 OE1 GLU A 316 2727 1975 2182 -284 -251 970 O ATOM 3493 OE2 GLU A 316 -20.360 6.672 14.549 1.00 18.75 O ANISOU 3493 OE2 GLU A 316 2115 2584 2425 -498 -572 827 O ATOM 3494 N ILE A 317 -18.942 4.942 19.341 1.00 12.14 N ANISOU 3494 N ILE A 317 1565 1517 1530 23 25 35 N ATOM 3495 CA ILE A 317 -19.189 3.825 20.243 1.00 12.56 C ANISOU 3495 CA ILE A 317 1563 1585 1622 -2 22 46 C ATOM 3496 C ILE A 317 -20.478 4.044 21.032 1.00 12.50 C ANISOU 3496 C ILE A 317 1552 1557 1638 -7 14 22 C ATOM 3497 O ILE A 317 -21.233 3.104 21.242 1.00 12.35 O ANISOU 3497 O ILE A 317 1335 1544 1812 -47 29 2 O ATOM 3498 CB ILE A 317 -17.975 3.554 21.138 1.00 12.96 C ANISOU 3498 CB ILE A 317 1654 1646 1623 -21 38 39 C ATOM 3499 CG1 ILE A 317 -16.851 2.988 20.261 1.00 15.05 C ANISOU 3499 CG1 ILE A 317 1840 1977 1901 9 -138 105 C ATOM 3500 CG2 ILE A 317 -18.345 2.555 22.283 1.00 12.96 C ANISOU 3500 CG2 ILE A 317 1646 1618 1659 76 73 104 C ATOM 3501 CD1 ILE A 317 -15.524 2.965 20.905 1.00 18.84 C ANISOU 3501 CD1 ILE A 317 2348 2353 2457 -29 -51 144 C ATOM 3502 N THR A 318 -20.729 5.281 21.451 1.00 12.54 N ANISOU 3502 N THR A 318 1523 1552 1688 -15 25 16 N ATOM 3503 CA THR A 318 -21.983 5.641 22.115 1.00 12.54 C ANISOU 3503 CA THR A 318 1611 1540 1612 -104 74 -6 C ATOM 3504 C THR A 318 -23.192 5.298 21.260 1.00 12.73 C ANISOU 3504 C THR A 318 1624 1531 1681 -15 50 -26 C ATOM 3505 O THR A 318 -24.206 4.802 21.773 1.00 12.63 O ANISOU 3505 O THR A 318 1637 1302 1860 -207 0 -97 O ATOM 3506 CB THR A 318 -21.974 7.146 22.472 1.00 12.56 C ANISOU 3506 CB THR A 318 1571 1562 1637 -55 88 -11 C ATOM 3507 OG1 THR A 318 -20.945 7.390 23.452 1.00 12.10 O ANISOU 3507 OG1 THR A 318 1798 1714 1083 -486 177 135 O ATOM 3508 CG2 THR A 318 -23.287 7.584 23.135 1.00 12.91 C ANISOU 3508 CG2 THR A 318 1863 1589 1451 -259 72 4 C ATOM 3509 N ALA A 319 -23.087 5.559 19.968 1.00 13.45 N ANISOU 3509 N ALA A 319 1685 1643 1781 -24 73 -19 N ATOM 3510 CA ALA A 319 -24.161 5.259 19.032 1.00 13.81 C ANISOU 3510 CA ALA A 319 1714 1748 1782 -24 22 2 C ATOM 3511 C ALA A 319 -24.434 3.752 18.890 1.00 14.01 C ANISOU 3511 C ALA A 319 1765 1740 1818 0 17 4 C ATOM 3512 O ALA A 319 -25.581 3.359 18.650 1.00 14.32 O ANISOU 3512 O ALA A 319 1734 1744 1962 -83 45 3 O ATOM 3513 CB ALA A 319 -23.880 5.895 17.659 1.00 14.51 C ANISOU 3513 CB ALA A 319 1808 1783 1922 10 55 -1 C ATOM 3514 N LEU A 320 -23.411 2.909 19.037 1.00 14.10 N ANISOU 3514 N LEU A 320 1760 1825 1771 -44 -21 25 N ATOM 3515 CA LEU A 320 -23.589 1.440 18.933 1.00 14.08 C ANISOU 3515 CA LEU A 320 1827 1784 1737 -14 -7 16 C ATOM 3516 C LEU A 320 -23.999 0.721 20.236 1.00 13.77 C ANISOU 3516 C LEU A 320 1779 1727 1724 -25 -31 49 C ATOM 3517 O LEU A 320 -24.681 -0.321 20.203 1.00 13.21 O ANISOU 3517 O LEU A 320 1855 1531 1631 -121 -92 127 O ATOM 3518 CB LEU A 320 -22.310 0.785 18.391 1.00 14.36 C ANISOU 3518 CB LEU A 320 1731 1920 1802 -33 -22 31 C ATOM 3519 CG LEU A 320 -21.942 1.081 16.932 1.00 15.41 C ANISOU 3519 CG LEU A 320 1875 2060 1917 -38 -12 4 C ATOM 3520 CD1 LEU A 320 -20.486 0.674 16.658 1.00 16.42 C ANISOU 3520 CD1 LEU A 320 2165 2159 1913 39 92 179 C ATOM 3521 CD2 LEU A 320 -22.883 0.370 15.960 1.00 17.80 C ANISOU 3521 CD2 LEU A 320 2341 2307 2115 33 86 34 C ATOM 3522 N ALA A 321 -23.587 1.279 21.368 1.00 13.16 N ANISOU 3522 N ALA A 321 1717 1636 1646 -42 -25 23 N ATOM 3523 CA ALA A 321 -23.780 0.653 22.677 1.00 12.73 C ANISOU 3523 CA ALA A 321 1632 1592 1612 -14 -8 48 C ATOM 3524 C ALA A 321 -25.155 0.962 23.230 1.00 13.00 C ANISOU 3524 C ALA A 321 1640 1641 1656 -37 -24 32 C ATOM 3525 O ALA A 321 -25.785 1.932 22.804 1.00 12.57 O ANISOU 3525 O ALA A 321 1466 1610 1700 -22 -6 80 O ATOM 3526 CB ALA A 321 -22.732 1.158 23.644 1.00 12.41 C ANISOU 3526 CB ALA A 321 1574 1527 1614 -69 50 91 C ATOM 3527 N PRO A 322 -25.619 0.165 24.195 1.00 13.69 N ANISOU 3527 N PRO A 322 1728 1729 1742 -30 -8 24 N ATOM 3528 CA PRO A 322 -26.866 0.491 24.902 1.00 14.37 C ANISOU 3528 CA PRO A 322 1784 1826 1850 -1 -26 11 C ATOM 3529 C PRO A 322 -26.738 1.872 25.567 1.00 15.56 C ANISOU 3529 C PRO A 322 1940 1965 2005 -25 -24 25 C ATOM 3530 O PRO A 322 -25.637 2.273 25.951 1.00 15.45 O ANISOU 3530 O PRO A 322 1881 2005 1981 22 -134 5 O ATOM 3531 CB PRO A 322 -27.032 -0.655 25.929 1.00 13.93 C ANISOU 3531 CB PRO A 322 1715 1807 1770 -11 -15 7 C ATOM 3532 CG PRO A 322 -26.150 -1.764 25.432 1.00 13.76 C ANISOU 3532 CG PRO A 322 1775 1685 1768 -89 -59 53 C ATOM 3533 CD PRO A 322 -25.009 -1.084 24.695 1.00 13.78 C ANISOU 3533 CD PRO A 322 1706 1782 1745 10 7 32 C ATOM 3534 N SER A 323 -27.842 2.604 25.656 1.00 16.72 N ANISOU 3534 N SER A 323 2044 2111 2197 -35 43 0 N ATOM 3535 CA SER A 323 -27.787 4.044 25.902 1.00 18.57 C ANISOU 3535 CA SER A 323 2279 2358 2418 10 13 -38 C ATOM 3536 C SER A 323 -27.478 4.425 27.351 1.00 19.81 C ANISOU 3536 C SER A 323 2440 2505 2580 14 2 -50 C ATOM 3537 O SER A 323 -27.241 5.595 27.653 1.00 20.63 O ANISOU 3537 O SER A 323 2462 2591 2785 12 -102 -168 O ATOM 3538 CB SER A 323 -29.090 4.703 25.439 1.00 18.81 C ANISOU 3538 CB SER A 323 2335 2367 2443 -20 32 -31 C ATOM 3539 OG SER A 323 -30.154 4.279 26.232 1.00 19.36 O ANISOU 3539 OG SER A 323 2210 2362 2783 -42 102 -137 O ATOM 3540 N THR A 324 -27.470 3.435 28.234 1.00 20.71 N ANISOU 3540 N THR A 324 2550 2678 2638 42 0 -51 N ATOM 3541 CA THR A 324 -27.096 3.636 29.624 1.00 21.78 C ANISOU 3541 CA THR A 324 2719 2811 2743 23 28 -69 C ATOM 3542 C THR A 324 -25.627 3.244 29.896 1.00 21.39 C ANISOU 3542 C THR A 324 2649 2812 2665 25 55 -61 C ATOM 3543 O THR A 324 -25.154 3.341 31.021 1.00 21.07 O ANISOU 3543 O THR A 324 2710 2907 2388 2 199 -122 O ATOM 3544 CB THR A 324 -28.000 2.776 30.506 1.00 21.90 C ANISOU 3544 CB THR A 324 2737 2786 2797 -21 9 -41 C ATOM 3545 OG1 THR A 324 -28.039 1.443 29.967 1.00 24.53 O ANISOU 3545 OG1 THR A 324 3054 3076 3187 -68 -23 -277 O ATOM 3546 CG2 THR A 324 -29.424 3.236 30.438 1.00 22.46 C ANISOU 3546 CG2 THR A 324 2865 2828 2841 83 109 -131 C ATOM 3547 N MET A 325 -24.908 2.781 28.874 1.00 21.10 N ANISOU 3547 N MET A 325 2648 2754 2612 17 54 -33 N ATOM 3548 CA MET A 325 -23.512 2.381 29.062 1.00 20.68 C ANISOU 3548 CA MET A 325 2617 2652 2586 30 36 -11 C ATOM 3549 C MET A 325 -22.647 3.613 29.272 1.00 20.17 C ANISOU 3549 C MET A 325 2543 2575 2543 10 6 -20 C ATOM 3550 O MET A 325 -22.829 4.610 28.579 1.00 19.01 O ANISOU 3550 O MET A 325 2442 2366 2413 83 -58 46 O ATOM 3551 CB MET A 325 -23.021 1.627 27.827 1.00 21.08 C ANISOU 3551 CB MET A 325 2672 2676 2659 5 36 -1 C ATOM 3552 CG MET A 325 -21.835 0.767 28.064 1.00 21.82 C ANISOU 3552 CG MET A 325 2776 2836 2679 92 81 46 C ATOM 3553 SD MET A 325 -22.122 -0.560 29.256 1.00 25.28 S ANISOU 3553 SD MET A 325 3433 3310 2859 328 195 395 S ATOM 3554 CE MET A 325 -23.120 -1.673 28.364 1.00 23.85 C ANISOU 3554 CE MET A 325 2955 3152 2954 95 112 42 C ATOM 3555 N LYS A 326 -21.716 3.541 30.228 1.00 19.96 N ANISOU 3555 N LYS A 326 2586 2486 2511 26 0 20 N ATOM 3556 CA LYS A 326 -20.701 4.579 30.416 1.00 20.25 C ANISOU 3556 CA LYS A 326 2555 2569 2570 45 -8 -31 C ATOM 3557 C LYS A 326 -19.537 4.273 29.489 1.00 19.26 C ANISOU 3557 C LYS A 326 2471 2422 2424 30 -42 -55 C ATOM 3558 O LYS A 326 -18.905 3.224 29.590 1.00 19.14 O ANISOU 3558 O LYS A 326 2390 2479 2402 205 -57 -95 O ATOM 3559 CB LYS A 326 -20.219 4.649 31.871 1.00 21.00 C ANISOU 3559 CB LYS A 326 2694 2606 2679 8 17 -75 C ATOM 3560 CG LYS A 326 -19.532 5.988 32.238 1.00 25.95 C ANISOU 3560 CG LYS A 326 3231 3287 3340 84 113 -85 C ATOM 3561 CD LYS A 326 -20.477 6.971 33.008 1.00 31.41 C ANISOU 3561 CD LYS A 326 4144 3763 4025 12 26 -68 C ATOM 3562 CE LYS A 326 -20.039 8.469 32.859 1.00 33.91 C ANISOU 3562 CE LYS A 326 4444 4098 4339 61 -37 -123 C ATOM 3563 NZ LYS A 326 -20.696 9.359 33.900 1.00 34.88 N ANISOU 3563 NZ LYS A 326 4704 3939 4608 214 121 -125 N ATOM 3564 N ILE A 327 -19.277 5.190 28.575 1.00 18.19 N ANISOU 3564 N ILE A 327 2316 2278 2316 35 -3 -27 N ATOM 3565 CA ILE A 327 -18.211 5.050 27.600 1.00 17.64 C ANISOU 3565 CA ILE A 327 2198 2237 2267 -5 -26 -27 C ATOM 3566 C ILE A 327 -17.111 6.087 27.849 1.00 15.82 C ANISOU 3566 C ILE A 327 1935 2039 2037 -40 -3 -14 C ATOM 3567 O ILE A 327 -17.384 7.265 28.050 1.00 14.92 O ANISOU 3567 O ILE A 327 1583 2040 2043 -76 -54 11 O ATOM 3568 CB ILE A 327 -18.818 5.125 26.193 1.00 18.07 C ANISOU 3568 CB ILE A 327 2254 2275 2336 -36 -8 -33 C ATOM 3569 CG1 ILE A 327 -19.677 3.855 25.966 1.00 19.71 C ANISOU 3569 CG1 ILE A 327 2403 2569 2514 -10 -81 -27 C ATOM 3570 CG2 ILE A 327 -17.755 5.201 25.109 1.00 18.70 C ANISOU 3570 CG2 ILE A 327 2357 2391 2357 -140 -81 -25 C ATOM 3571 CD1 ILE A 327 -20.811 4.103 25.194 1.00 20.34 C ANISOU 3571 CD1 ILE A 327 2506 2720 2500 -62 -53 -67 C ATOM 3572 N LYS A 328 -15.868 5.617 27.879 1.00 14.89 N ANISOU 3572 N LYS A 328 1872 1897 1889 -28 -5 1 N ATOM 3573 CA LYS A 328 -14.716 6.484 28.050 1.00 14.20 C ANISOU 3573 CA LYS A 328 1762 1840 1793 -50 -23 -2 C ATOM 3574 C LYS A 328 -13.546 6.066 27.143 1.00 13.16 C ANISOU 3574 C LYS A 328 1641 1680 1680 -53 -39 -32 C ATOM 3575 O LYS A 328 -13.111 4.920 27.158 1.00 12.35 O ANISOU 3575 O LYS A 328 1479 1684 1529 -250 -20 -119 O ATOM 3576 CB LYS A 328 -14.300 6.466 29.513 1.00 15.29 C ANISOU 3576 CB LYS A 328 1941 1942 1924 -74 11 21 C ATOM 3577 CG LYS A 328 -13.087 7.301 29.870 1.00 17.89 C ANISOU 3577 CG LYS A 328 2320 2373 2105 0 28 -56 C ATOM 3578 CD LYS A 328 -13.053 7.594 31.387 1.00 24.03 C ANISOU 3578 CD LYS A 328 3108 3053 2969 -44 -57 12 C ATOM 3579 CE LYS A 328 -11.710 8.179 31.841 1.00 25.29 C ANISOU 3579 CE LYS A 328 3235 3282 3092 -168 -73 -62 C ATOM 3580 NZ LYS A 328 -11.583 8.186 33.344 1.00 26.99 N ANISOU 3580 NZ LYS A 328 3586 3632 3035 -234 151 44 N ATOM 3581 N ILE A 329 -13.023 7.024 26.384 1.00 12.26 N ANISOU 3581 N ILE A 329 1508 1604 1543 25 18 22 N ATOM 3582 CA ILE A 329 -11.831 6.848 25.564 1.00 12.24 C ANISOU 3582 CA ILE A 329 1484 1569 1598 50 13 9 C ATOM 3583 C ILE A 329 -10.632 7.518 26.250 1.00 11.80 C ANISOU 3583 C ILE A 329 1401 1469 1614 67 34 0 C ATOM 3584 O ILE A 329 -10.691 8.677 26.610 1.00 10.99 O ANISOU 3584 O ILE A 329 1154 1353 1665 124 122 -3 O ATOM 3585 CB ILE A 329 -12.039 7.510 24.179 1.00 12.06 C ANISOU 3585 CB ILE A 329 1429 1608 1543 92 28 -5 C ATOM 3586 CG1 ILE A 329 -13.391 7.090 23.558 1.00 14.43 C ANISOU 3586 CG1 ILE A 329 1830 1765 1886 50 34 12 C ATOM 3587 CG2 ILE A 329 -10.883 7.195 23.277 1.00 14.13 C ANISOU 3587 CG2 ILE A 329 1946 1737 1686 21 15 164 C ATOM 3588 CD1 ILE A 329 -13.664 5.599 23.480 1.00 14.90 C ANISOU 3588 CD1 ILE A 329 1870 1877 1912 -7 136 -45 C ATOM 3589 N ILE A 330 -9.539 6.775 26.414 1.00 11.45 N ANISOU 3589 N ILE A 330 1363 1443 1543 55 12 12 N ATOM 3590 CA ILE A 330 -8.334 7.282 27.036 1.00 10.82 C ANISOU 3590 CA ILE A 330 1362 1341 1407 40 19 13 C ATOM 3591 C ILE A 330 -7.282 7.334 25.929 1.00 11.04 C ANISOU 3591 C ILE A 330 1405 1373 1414 31 53 19 C ATOM 3592 O ILE A 330 -6.936 6.316 25.327 1.00 9.60 O ANISOU 3592 O ILE A 330 1259 1200 1187 0 230 -142 O ATOM 3593 CB ILE A 330 -7.912 6.359 28.197 1.00 11.30 C ANISOU 3593 CB ILE A 330 1418 1512 1362 40 0 1 C ATOM 3594 CG1 ILE A 330 -9.012 6.327 29.280 1.00 12.60 C ANISOU 3594 CG1 ILE A 330 1537 1558 1690 -78 -162 198 C ATOM 3595 CG2 ILE A 330 -6.560 6.838 28.800 1.00 11.06 C ANISOU 3595 CG2 ILE A 330 1311 1569 1322 -106 -31 140 C ATOM 3596 CD1 ILE A 330 -9.740 5.021 29.382 1.00 15.38 C ANISOU 3596 CD1 ILE A 330 1897 2040 1904 47 -146 -85 C ATOM 3597 N ALA A 331 -6.809 8.538 25.658 1.00 11.65 N ANISOU 3597 N ALA A 331 1481 1457 1486 64 78 -17 N ATOM 3598 CA ALA A 331 -5.873 8.812 24.592 1.00 12.68 C ANISOU 3598 CA ALA A 331 1616 1605 1593 55 48 47 C ATOM 3599 C ALA A 331 -4.748 9.649 25.162 1.00 13.12 C ANISOU 3599 C ALA A 331 1674 1663 1646 48 73 68 C ATOM 3600 O ALA A 331 -4.736 10.850 25.018 1.00 13.70 O ANISOU 3600 O ALA A 331 1893 1576 1736 177 205 82 O ATOM 3601 CB ALA A 331 -6.569 9.557 23.477 1.00 13.11 C ANISOU 3601 CB ALA A 331 1639 1766 1575 120 10 36 C ATOM 3602 N PRO A 332 -3.795 9.007 25.820 1.00 13.63 N ANISOU 3602 N PRO A 332 1646 1723 1808 -10 61 72 N ATOM 3603 CA PRO A 332 -2.675 9.719 26.452 1.00 13.77 C ANISOU 3603 CA PRO A 332 1692 1772 1765 22 -11 39 C ATOM 3604 C PRO A 332 -1.825 10.487 25.394 1.00 12.67 C ANISOU 3604 C PRO A 332 1500 1594 1718 -41 -15 53 C ATOM 3605 O PRO A 332 -1.653 9.954 24.285 1.00 11.33 O ANISOU 3605 O PRO A 332 1161 1505 1640 -62 -115 60 O ATOM 3606 CB PRO A 332 -1.849 8.590 27.061 1.00 14.02 C ANISOU 3606 CB PRO A 332 1740 1783 1802 -50 24 131 C ATOM 3607 CG PRO A 332 -2.670 7.380 26.971 1.00 14.84 C ANISOU 3607 CG PRO A 332 1809 1967 1859 57 -73 17 C ATOM 3608 CD PRO A 332 -3.679 7.547 25.931 1.00 13.91 C ANISOU 3608 CD PRO A 332 1673 1854 1756 33 39 83 C ATOM 3609 N PRO A 333 -1.302 11.677 25.701 1.00 12.50 N ANISOU 3609 N PRO A 333 1571 1585 1593 8 -37 -21 N ATOM 3610 CA PRO A 333 -0.442 12.393 24.742 1.00 11.92 C ANISOU 3610 CA PRO A 333 1501 1471 1553 -23 -25 -20 C ATOM 3611 C PRO A 333 0.770 11.599 24.283 1.00 11.48 C ANISOU 3611 C PRO A 333 1501 1384 1476 -22 -20 -41 C ATOM 3612 O PRO A 333 1.191 11.761 23.142 1.00 9.85 O ANISOU 3612 O PRO A 333 1421 1118 1201 -99 12 67 O ATOM 3613 CB PRO A 333 0.025 13.650 25.510 1.00 12.24 C ANISOU 3613 CB PRO A 333 1519 1551 1580 26 -8 -69 C ATOM 3614 CG PRO A 333 -0.811 13.720 26.734 1.00 13.37 C ANISOU 3614 CG PRO A 333 1773 1643 1663 -11 16 -42 C ATOM 3615 CD PRO A 333 -1.513 12.429 26.950 1.00 13.26 C ANISOU 3615 CD PRO A 333 1631 1602 1805 -27 -20 -57 C ATOM 3616 N GLU A 334 1.302 10.753 25.167 1.00 11.58 N ANISOU 3616 N GLU A 334 1517 1469 1411 2 0 -51 N ATOM 3617 CA GLU A 334 2.519 9.965 24.907 1.00 12.08 C ANISOU 3617 CA GLU A 334 1596 1504 1489 12 -45 -51 C ATOM 3618 C GLU A 334 2.261 8.636 24.182 1.00 11.66 C ANISOU 3618 C GLU A 334 1577 1460 1392 68 -40 -69 C ATOM 3619 O GLU A 334 3.128 7.780 24.171 1.00 11.24 O ANISOU 3619 O GLU A 334 1564 1452 1255 95 -89 -254 O ATOM 3620 CB GLU A 334 3.275 9.700 26.227 1.00 12.78 C ANISOU 3620 CB GLU A 334 1737 1540 1576 4 19 -33 C ATOM 3621 CG GLU A 334 2.704 8.627 27.168 1.00 14.88 C ANISOU 3621 CG GLU A 334 1874 1988 1791 33 100 2 C ATOM 3622 CD GLU A 334 1.475 9.056 27.940 1.00 17.77 C ANISOU 3622 CD GLU A 334 2601 2277 1874 9 268 40 C ATOM 3623 OE1 GLU A 334 1.022 10.205 27.781 1.00 20.30 O ANISOU 3623 OE1 GLU A 334 2938 2950 1824 269 634 184 O ATOM 3624 OE2 GLU A 334 0.939 8.220 28.708 1.00 20.71 O ANISOU 3624 OE2 GLU A 334 2585 2957 2325 -227 224 -76 O ATOM 3625 N ARG A 335 1.089 8.468 23.575 1.00 10.85 N ANISOU 3625 N ARG A 335 1478 1360 1281 23 -47 -21 N ATOM 3626 CA ARG A 335 0.672 7.147 23.125 1.00 10.96 C ANISOU 3626 CA ARG A 335 1430 1387 1346 26 -30 13 C ATOM 3627 C ARG A 335 1.440 6.491 21.967 1.00 11.53 C ANISOU 3627 C ARG A 335 1500 1416 1465 46 -101 20 C ATOM 3628 O ARG A 335 1.289 5.291 21.743 1.00 11.68 O ANISOU 3628 O ARG A 335 1466 1424 1548 288 -214 90 O ATOM 3629 CB ARG A 335 -0.827 7.109 22.893 1.00 11.13 C ANISOU 3629 CB ARG A 335 1539 1305 1384 62 -110 -6 C ATOM 3630 CG ARG A 335 -1.393 8.020 21.825 1.00 10.88 C ANISOU 3630 CG ARG A 335 1456 1392 1285 3 -77 10 C ATOM 3631 CD ARG A 335 -2.908 8.020 21.903 1.00 9.04 C ANISOU 3631 CD ARG A 335 1039 1106 1288 -108 0 -69 C ATOM 3632 NE ARG A 335 -3.565 8.920 20.968 1.00 8.70 N ANISOU 3632 NE ARG A 335 868 1216 1221 -88 -374 -159 N ATOM 3633 CZ ARG A 335 -3.697 10.222 21.133 1.00 11.46 C ANISOU 3633 CZ ARG A 335 1354 1512 1486 2 -178 -47 C ATOM 3634 NH1 ARG A 335 -4.352 10.947 20.226 1.00 13.04 N ANISOU 3634 NH1 ARG A 335 1727 1607 1618 -53 -121 98 N ATOM 3635 NH2 ARG A 335 -3.195 10.819 22.206 1.00 12.21 N ANISOU 3635 NH2 ARG A 335 1402 1585 1652 64 -234 -143 N ATOM 3636 N LYS A 336 2.243 7.273 21.244 1.00 12.07 N ANISOU 3636 N LYS A 336 1516 1554 1514 66 -43 22 N ATOM 3637 CA LYS A 336 3.235 6.758 20.301 1.00 12.63 C ANISOU 3637 CA LYS A 336 1643 1592 1561 5 -6 -13 C ATOM 3638 C LYS A 336 4.237 5.845 21.000 1.00 11.65 C ANISOU 3638 C LYS A 336 1559 1427 1438 8 33 28 C ATOM 3639 O LYS A 336 4.841 4.964 20.366 1.00 12.16 O ANISOU 3639 O LYS A 336 1886 1492 1240 -38 66 -15 O ATOM 3640 CB LYS A 336 4.020 7.922 19.676 1.00 13.21 C ANISOU 3640 CB LYS A 336 1755 1651 1612 62 15 38 C ATOM 3641 CG LYS A 336 3.249 8.669 18.610 1.00 17.66 C ANISOU 3641 CG LYS A 336 2286 2168 2254 -11 -92 -19 C ATOM 3642 CD LYS A 336 3.829 10.066 18.253 1.00 23.17 C ANISOU 3642 CD LYS A 336 2926 2899 2976 -19 39 26 C ATOM 3643 CE LYS A 336 5.287 10.042 17.849 1.00 25.88 C ANISOU 3643 CE LYS A 336 3319 3177 3336 -19 68 19 C ATOM 3644 NZ LYS A 336 5.908 11.422 17.731 1.00 29.14 N ANISOU 3644 NZ LYS A 336 4002 3448 3619 0 43 -151 N ATOM 3645 N TYR A 337 4.466 6.085 22.289 1.00 9.74 N ANISOU 3645 N TYR A 337 1279 1253 1167 -64 33 -20 N ATOM 3646 CA TYR A 337 5.435 5.296 23.052 1.00 9.62 C ANISOU 3646 CA TYR A 337 1217 1184 1254 -29 18 5 C ATOM 3647 C TYR A 337 4.835 4.480 24.207 1.00 9.59 C ANISOU 3647 C TYR A 337 1200 1183 1260 -4 1 -14 C ATOM 3648 O TYR A 337 5.589 3.980 25.023 1.00 8.69 O ANISOU 3648 O TYR A 337 1059 961 1280 73 39 -2 O ATOM 3649 CB TYR A 337 6.532 6.230 23.638 1.00 10.00 C ANISOU 3649 CB TYR A 337 1222 1305 1272 14 12 91 C ATOM 3650 CG TYR A 337 7.290 7.083 22.637 1.00 11.79 C ANISOU 3650 CG TYR A 337 1424 1419 1635 -103 45 89 C ATOM 3651 CD1 TYR A 337 7.472 6.681 21.306 1.00 11.53 C ANISOU 3651 CD1 TYR A 337 1482 1451 1444 27 32 164 C ATOM 3652 CD2 TYR A 337 7.882 8.265 23.036 1.00 13.67 C ANISOU 3652 CD2 TYR A 337 1782 1576 1834 -138 109 63 C ATOM 3653 CE1 TYR A 337 8.193 7.479 20.392 1.00 13.58 C ANISOU 3653 CE1 TYR A 337 1612 1652 1896 -139 208 -43 C ATOM 3654 CE2 TYR A 337 8.606 9.064 22.117 1.00 15.60 C ANISOU 3654 CE2 TYR A 337 1931 2027 1967 -294 347 91 C ATOM 3655 CZ TYR A 337 8.741 8.665 20.806 1.00 15.22 C ANISOU 3655 CZ TYR A 337 1875 1918 1987 -327 291 76 C ATOM 3656 OH TYR A 337 9.465 9.454 19.916 1.00 17.55 O ANISOU 3656 OH TYR A 337 2439 1789 2438 -250 225 420 O ATOM 3657 N SER A 338 3.504 4.354 24.290 1.00 9.89 N ANISOU 3657 N SER A 338 1204 1249 1302 -48 48 31 N ATOM 3658 CA SER A 338 2.854 3.673 25.419 1.00 10.88 C ANISOU 3658 CA SER A 338 1325 1433 1375 -38 8 32 C ATOM 3659 C SER A 338 3.305 2.228 25.585 1.00 10.51 C ANISOU 3659 C SER A 338 1293 1354 1346 0 39 -8 C ATOM 3660 O SER A 338 3.495 1.754 26.705 1.00 10.64 O ANISOU 3660 O SER A 338 1251 1416 1375 -12 118 54 O ATOM 3661 CB SER A 338 1.323 3.667 25.267 1.00 10.20 C ANISOU 3661 CB SER A 338 1201 1294 1381 -12 117 65 C ATOM 3662 OG SER A 338 0.827 4.968 25.352 1.00 13.72 O ANISOU 3662 OG SER A 338 1432 2131 1649 -267 113 45 O ATOM 3663 N VAL A 339 3.456 1.526 24.466 1.00 10.91 N ANISOU 3663 N VAL A 339 1307 1449 1387 -44 13 53 N ATOM 3664 CA VAL A 339 3.897 0.150 24.495 1.00 10.28 C ANISOU 3664 CA VAL A 339 1268 1297 1341 2 24 1 C ATOM 3665 C VAL A 339 5.278 0.096 25.155 1.00 9.75 C ANISOU 3665 C VAL A 339 1259 1244 1201 38 -6 9 C ATOM 3666 O VAL A 339 5.528 -0.708 26.068 1.00 10.00 O ANISOU 3666 O VAL A 339 1445 1253 1100 62 108 44 O ATOM 3667 CB VAL A 339 3.968 -0.475 23.063 1.00 10.97 C ANISOU 3667 CB VAL A 339 1351 1455 1361 27 -62 46 C ATOM 3668 CG1 VAL A 339 4.695 -1.797 23.097 1.00 11.92 C ANISOU 3668 CG1 VAL A 339 1560 1402 1565 81 -30 23 C ATOM 3669 CG2 VAL A 339 2.550 -0.672 22.438 1.00 9.37 C ANISOU 3669 CG2 VAL A 339 1007 1216 1337 -289 -45 -33 C ATOM 3670 N TRP A 340 6.169 0.946 24.670 1.00 8.37 N ANISOU 3670 N TRP A 340 1013 1012 1155 14 7 48 N ATOM 3671 CA TRP A 340 7.545 0.988 25.167 1.00 8.69 C ANISOU 3671 CA TRP A 340 1076 1089 1134 0 -32 31 C ATOM 3672 C TRP A 340 7.565 1.304 26.657 1.00 8.31 C ANISOU 3672 C TRP A 340 984 1086 1085 -3 40 2 C ATOM 3673 O TRP A 340 8.279 0.641 27.429 1.00 7.62 O ANISOU 3673 O TRP A 340 653 1128 1111 46 -81 56 O ATOM 3674 CB TRP A 340 8.415 1.997 24.398 1.00 8.52 C ANISOU 3674 CB TRP A 340 977 1136 1122 -15 29 5 C ATOM 3675 CG TRP A 340 9.846 1.871 24.812 1.00 7.31 C ANISOU 3675 CG TRP A 340 837 970 969 159 -62 50 C ATOM 3676 CD1 TRP A 340 10.787 1.114 24.219 1.00 7.59 C ANISOU 3676 CD1 TRP A 340 617 1199 1068 -40 -20 -138 C ATOM 3677 CD2 TRP A 340 10.460 2.443 25.968 1.00 6.86 C ANISOU 3677 CD2 TRP A 340 638 696 1269 92 50 -84 C ATOM 3678 NE1 TRP A 340 11.962 1.177 24.924 1.00 8.38 N ANISOU 3678 NE1 TRP A 340 804 1156 1224 128 -55 -137 N ATOM 3679 CE2 TRP A 340 11.784 1.992 26.006 1.00 8.20 C ANISOU 3679 CE2 TRP A 340 817 1073 1224 -9 63 -116 C ATOM 3680 CE3 TRP A 340 10.016 3.273 26.997 1.00 8.71 C ANISOU 3680 CE3 TRP A 340 946 1140 1223 74 137 5 C ATOM 3681 CZ2 TRP A 340 12.666 2.363 27.007 1.00 7.91 C ANISOU 3681 CZ2 TRP A 340 907 878 1218 124 -90 11 C ATOM 3682 CZ3 TRP A 340 10.885 3.642 27.973 1.00 5.09 C ANISOU 3682 CZ3 TRP A 340 537 471 925 -248 40 -3 C ATOM 3683 CH2 TRP A 340 12.191 3.177 27.990 1.00 6.51 C ANISOU 3683 CH2 TRP A 340 815 736 920 -27 192 6 C ATOM 3684 N ILE A 341 6.767 2.289 27.066 1.00 8.24 N ANISOU 3684 N ILE A 341 1033 985 1112 -30 9 38 N ATOM 3685 CA ILE A 341 6.742 2.711 28.480 1.00 8.20 C ANISOU 3685 CA ILE A 341 1066 1039 1011 48 0 -42 C ATOM 3686 C ILE A 341 6.237 1.600 29.395 1.00 8.14 C ANISOU 3686 C ILE A 341 1038 1078 975 57 -34 -61 C ATOM 3687 O ILE A 341 6.755 1.401 30.484 1.00 7.94 O ANISOU 3687 O ILE A 341 987 1222 807 159 -13 -171 O ATOM 3688 CB ILE A 341 5.886 3.989 28.658 1.00 8.07 C ANISOU 3688 CB ILE A 341 948 1122 993 58 -75 -15 C ATOM 3689 CG1 ILE A 341 6.526 5.162 27.909 1.00 8.46 C ANISOU 3689 CG1 ILE A 341 1066 1021 1124 107 -118 30 C ATOM 3690 CG2 ILE A 341 5.757 4.351 30.127 1.00 9.81 C ANISOU 3690 CG2 ILE A 341 1161 1329 1234 139 105 -137 C ATOM 3691 CD1 ILE A 341 5.581 6.316 27.694 1.00 10.68 C ANISOU 3691 CD1 ILE A 341 1359 1437 1259 172 -107 164 C ATOM 3692 N GLY A 342 5.239 0.858 28.943 1.00 8.38 N ANISOU 3692 N GLY A 342 1062 1080 1042 35 -26 15 N ATOM 3693 CA GLY A 342 4.739 -0.279 29.690 1.00 8.48 C ANISOU 3693 CA GLY A 342 1118 1083 1020 28 -66 -20 C ATOM 3694 C GLY A 342 5.812 -1.325 29.912 1.00 8.06 C ANISOU 3694 C GLY A 342 1110 975 977 26 -65 -19 C ATOM 3695 O GLY A 342 5.882 -1.905 30.981 1.00 8.28 O ANISOU 3695 O GLY A 342 1323 809 1012 25 -90 1 O ATOM 3696 N GLY A 343 6.615 -1.585 28.890 1.00 7.55 N ANISOU 3696 N GLY A 343 965 980 922 -35 -22 88 N ATOM 3697 CA GLY A 343 7.735 -2.484 28.998 1.00 7.84 C ANISOU 3697 CA GLY A 343 928 1053 995 -23 -34 -28 C ATOM 3698 C GLY A 343 8.822 -1.982 29.965 1.00 8.25 C ANISOU 3698 C GLY A 343 994 1145 993 -12 -88 -5 C ATOM 3699 O GLY A 343 9.417 -2.780 30.677 1.00 9.70 O ANISOU 3699 O GLY A 343 1032 1535 1116 -143 -227 -176 O ATOM 3700 N SER A 344 9.086 -0.686 29.959 1.00 8.10 N ANISOU 3700 N SER A 344 907 1160 1009 0 -32 -84 N ATOM 3701 CA SER A 344 10.057 -0.065 30.853 1.00 9.12 C ANISOU 3701 CA SER A 344 1127 1198 1138 27 18 5 C ATOM 3702 C SER A 344 9.663 -0.262 32.310 1.00 9.29 C ANISOU 3702 C SER A 344 1087 1305 1136 84 -5 -53 C ATOM 3703 O SER A 344 10.509 -0.560 33.170 1.00 8.88 O ANISOU 3703 O SER A 344 793 1383 1197 277 -29 -61 O ATOM 3704 CB SER A 344 10.178 1.436 30.529 1.00 9.43 C ANISOU 3704 CB SER A 344 1175 1220 1187 44 26 -23 C ATOM 3705 OG SER A 344 11.081 2.085 31.421 1.00 9.26 O ANISOU 3705 OG SER A 344 1374 998 1147 -115 27 190 O ATOM 3706 N ILE A 345 8.374 -0.092 32.580 1.00 8.78 N ANISOU 3706 N ILE A 345 949 1277 1110 40 -62 -18 N ATOM 3707 CA ILE A 345 7.815 -0.271 33.919 1.00 8.81 C ANISOU 3707 CA ILE A 345 1013 1247 1087 45 -21 0 C ATOM 3708 C ILE A 345 7.893 -1.747 34.334 1.00 9.02 C ANISOU 3708 C ILE A 345 1109 1210 1107 -80 -14 26 C ATOM 3709 O ILE A 345 8.469 -2.061 35.376 1.00 8.56 O ANISOU 3709 O ILE A 345 1048 1427 777 -136 74 58 O ATOM 3710 CB ILE A 345 6.361 0.243 33.990 1.00 8.46 C ANISOU 3710 CB ILE A 345 923 1203 1086 34 -27 -15 C ATOM 3711 CG1 ILE A 345 6.314 1.746 33.708 1.00 7.34 C ANISOU 3711 CG1 ILE A 345 757 1149 881 142 -5 48 C ATOM 3712 CG2 ILE A 345 5.752 -0.083 35.353 1.00 7.94 C ANISOU 3712 CG2 ILE A 345 833 1094 1087 92 -10 -21 C ATOM 3713 CD1 ILE A 345 4.866 2.332 33.626 1.00 9.01 C ANISOU 3713 CD1 ILE A 345 1092 1287 1041 -66 89 291 C ATOM 3714 N LEU A 346 7.363 -2.645 33.498 1.00 10.03 N ANISOU 3714 N LEU A 346 1270 1351 1189 -11 5 67 N ATOM 3715 CA LEU A 346 7.395 -4.101 33.761 1.00 9.88 C ANISOU 3715 CA LEU A 346 1253 1230 1269 -35 -41 -23 C ATOM 3716 C LEU A 346 8.803 -4.603 34.068 1.00 10.41 C ANISOU 3716 C LEU A 346 1365 1263 1327 -30 -38 18 C ATOM 3717 O LEU A 346 9.035 -5.267 35.100 1.00 9.46 O ANISOU 3717 O LEU A 346 1369 773 1450 -146 -145 62 O ATOM 3718 CB LEU A 346 6.835 -4.857 32.560 1.00 10.44 C ANISOU 3718 CB LEU A 346 1286 1371 1307 14 8 -15 C ATOM 3719 CG LEU A 346 6.689 -6.372 32.693 1.00 9.94 C ANISOU 3719 CG LEU A 346 1227 1240 1310 48 -24 -22 C ATOM 3720 CD1 LEU A 346 5.722 -6.734 33.764 1.00 10.82 C ANISOU 3720 CD1 LEU A 346 1257 1398 1453 70 -89 -133 C ATOM 3721 CD2 LEU A 346 6.284 -6.984 31.337 1.00 10.55 C ANISOU 3721 CD2 LEU A 346 1229 1231 1547 76 -28 -35 C ATOM 3722 N ALA A 347 9.753 -4.231 33.206 1.00 10.68 N ANISOU 3722 N ALA A 347 1409 1287 1359 -7 -98 -10 N ATOM 3723 CA ALA A 347 11.128 -4.688 33.346 1.00 10.92 C ANISOU 3723 CA ALA A 347 1354 1389 1402 18 -74 -7 C ATOM 3724 C ALA A 347 11.815 -4.156 34.603 1.00 11.35 C ANISOU 3724 C ALA A 347 1395 1469 1448 71 -106 -5 C ATOM 3725 O ALA A 347 12.786 -4.738 35.028 1.00 11.40 O ANISOU 3725 O ALA A 347 1297 1539 1493 178 -237 138 O ATOM 3726 CB ALA A 347 11.946 -4.339 32.134 1.00 10.99 C ANISOU 3726 CB ALA A 347 1455 1350 1369 12 -126 -28 C ATOM 3727 N SER A 348 11.331 -3.046 35.163 1.00 11.47 N ANISOU 3727 N SER A 348 1370 1506 1482 38 -97 19 N ATOM 3728 CA SER A 348 11.947 -2.418 36.329 1.00 10.98 C ANISOU 3728 CA SER A 348 1331 1442 1398 -6 -21 60 C ATOM 3729 C SER A 348 11.457 -2.923 37.668 1.00 10.92 C ANISOU 3729 C SER A 348 1337 1387 1425 61 -45 94 C ATOM 3730 O SER A 348 12.047 -2.603 38.695 1.00 10.17 O ANISOU 3730 O SER A 348 1247 1340 1275 122 -54 196 O ATOM 3731 CB SER A 348 11.715 -0.916 36.291 1.00 11.11 C ANISOU 3731 CB SER A 348 1346 1435 1438 16 -8 50 C ATOM 3732 OG SER A 348 12.280 -0.351 35.123 1.00 10.85 O ANISOU 3732 OG SER A 348 1321 1423 1377 -326 -40 181 O ATOM 3733 N LEU A 349 10.368 -3.677 37.665 1.00 10.56 N ANISOU 3733 N LEU A 349 1275 1355 1383 -11 -31 155 N ATOM 3734 CA LEU A 349 9.729 -4.082 38.921 1.00 11.54 C ANISOU 3734 CA LEU A 349 1403 1468 1512 16 -58 34 C ATOM 3735 C LEU A 349 10.581 -5.096 39.680 1.00 11.18 C ANISOU 3735 C LEU A 349 1354 1419 1473 10 -120 83 C ATOM 3736 O LEU A 349 11.136 -6.014 39.083 1.00 11.04 O ANISOU 3736 O LEU A 349 1165 1426 1601 18 -258 106 O ATOM 3737 CB LEU A 349 8.364 -4.706 38.646 1.00 10.33 C ANISOU 3737 CB LEU A 349 1170 1406 1347 -1 -30 67 C ATOM 3738 CG LEU A 349 7.357 -3.812 37.937 1.00 12.24 C ANISOU 3738 CG LEU A 349 1509 1550 1589 -12 34 -19 C ATOM 3739 CD1 LEU A 349 6.062 -4.626 37.791 1.00 13.17 C ANISOU 3739 CD1 LEU A 349 1446 1805 1750 -108 -166 116 C ATOM 3740 CD2 LEU A 349 7.128 -2.494 38.707 1.00 11.02 C ANISOU 3740 CD2 LEU A 349 1520 1307 1358 83 -43 -3 C ATOM 3741 N SER A 350 10.656 -4.931 40.992 1.00 12.31 N ANISOU 3741 N SER A 350 1536 1489 1652 -12 -104 22 N ATOM 3742 CA SER A 350 11.388 -5.865 41.847 1.00 13.28 C ANISOU 3742 CA SER A 350 1696 1619 1729 -28 -64 -10 C ATOM 3743 C SER A 350 10.870 -7.310 41.646 1.00 14.27 C ANISOU 3743 C SER A 350 1801 1696 1922 -24 -100 -44 C ATOM 3744 O SER A 350 11.626 -8.274 41.778 1.00 15.00 O ANISOU 3744 O SER A 350 1789 1747 2160 -125 -250 -106 O ATOM 3745 CB SER A 350 11.230 -5.454 43.313 1.00 13.62 C ANISOU 3745 CB SER A 350 1726 1737 1709 -52 -76 -32 C ATOM 3746 OG SER A 350 9.847 -5.419 43.675 1.00 12.52 O ANISOU 3746 OG SER A 350 1622 1508 1625 205 -70 -18 O ATOM 3747 N THR A 351 9.589 -7.448 41.321 1.00 14.37 N ANISOU 3747 N THR A 351 1778 1768 1913 -39 -88 -24 N ATOM 3748 CA THR A 351 8.974 -8.768 41.130 1.00 15.62 C ANISOU 3748 CA THR A 351 1943 1969 2022 5 -74 32 C ATOM 3749 C THR A 351 9.300 -9.432 39.822 1.00 16.15 C ANISOU 3749 C THR A 351 2060 1992 2085 -2 -117 -11 C ATOM 3750 O THR A 351 8.959 -10.606 39.645 1.00 17.88 O ANISOU 3750 O THR A 351 2319 2181 2292 18 -144 -18 O ATOM 3751 CB THR A 351 7.451 -8.663 41.202 1.00 15.31 C ANISOU 3751 CB THR A 351 1857 1970 1990 -24 -105 16 C ATOM 3752 OG1 THR A 351 7.015 -7.522 40.438 1.00 14.91 O ANISOU 3752 OG1 THR A 351 1694 1993 1978 -87 -160 260 O ATOM 3753 CG2 THR A 351 7.007 -8.385 42.631 1.00 16.36 C ANISOU 3753 CG2 THR A 351 1893 2088 2232 15 -23 139 C ATOM 3754 N PHE A 352 9.875 -8.685 38.891 1.00 16.31 N ANISOU 3754 N PHE A 352 2002 2065 2129 -44 -84 27 N ATOM 3755 CA PHE A 352 10.142 -9.178 37.554 1.00 16.93 C ANISOU 3755 CA PHE A 352 2185 2118 2130 -1 -86 25 C ATOM 3756 C PHE A 352 11.433 -9.970 37.442 1.00 18.30 C ANISOU 3756 C PHE A 352 2354 2318 2280 -14 -83 63 C ATOM 3757 O PHE A 352 11.629 -10.697 36.470 1.00 17.19 O ANISOU 3757 O PHE A 352 2274 2203 2054 -1 -179 168 O ATOM 3758 CB PHE A 352 10.150 -8.021 36.529 1.00 17.54 C ANISOU 3758 CB PHE A 352 2254 2183 2224 -27 -22 -19 C ATOM 3759 CG PHE A 352 9.918 -8.478 35.111 1.00 15.93 C ANISOU 3759 CG PHE A 352 2143 1982 1926 113 -61 57 C ATOM 3760 CD1 PHE A 352 8.686 -8.952 34.729 1.00 14.27 C ANISOU 3760 CD1 PHE A 352 1756 1803 1861 230 7 -20 C ATOM 3761 CD2 PHE A 352 10.950 -8.489 34.190 1.00 15.80 C ANISOU 3761 CD2 PHE A 352 2169 1986 1848 103 10 71 C ATOM 3762 CE1 PHE A 352 8.461 -9.414 33.427 1.00 14.54 C ANISOU 3762 CE1 PHE A 352 1901 1815 1806 303 38 114 C ATOM 3763 CE2 PHE A 352 10.734 -8.938 32.886 1.00 16.72 C ANISOU 3763 CE2 PHE A 352 2127 2174 2051 53 -21 -31 C ATOM 3764 CZ PHE A 352 9.491 -9.410 32.515 1.00 15.22 C ANISOU 3764 CZ PHE A 352 1951 2075 1754 114 -6 120 C ATOM 3765 N GLN A 353 12.294 -9.877 38.454 1.00 20.07 N ANISOU 3765 N GLN A 353 2566 2530 2529 -32 -104 -7 N ATOM 3766 CA GLN A 353 13.600 -10.564 38.432 1.00 22.39 C ANISOU 3766 CA GLN A 353 2845 2834 2826 -17 -33 -19 C ATOM 3767 C GLN A 353 13.502 -12.062 38.135 1.00 22.48 C ANISOU 3767 C GLN A 353 2855 2854 2829 3 -51 -17 C ATOM 3768 O GLN A 353 14.319 -12.583 37.402 1.00 22.87 O ANISOU 3768 O GLN A 353 2942 2865 2880 19 -13 -87 O ATOM 3769 CB GLN A 353 14.360 -10.366 39.761 1.00 23.23 C ANISOU 3769 CB GLN A 353 2887 2946 2993 -52 -87 -17 C ATOM 3770 CG GLN A 353 15.448 -9.281 39.724 1.00 28.08 C ANISOU 3770 CG GLN A 353 3448 3525 3694 -51 -5 7 C ATOM 3771 CD GLN A 353 14.914 -7.846 39.535 1.00 33.58 C ANISOU 3771 CD GLN A 353 3858 4208 4691 -244 7 -198 C ATOM 3772 OE1 GLN A 353 13.734 -7.629 39.195 1.00 36.25 O ANISOU 3772 OE1 GLN A 353 3930 4744 5100 -397 -296 -412 O ATOM 3773 NE2 GLN A 353 15.796 -6.861 39.747 1.00 38.32 N ANISOU 3773 NE2 GLN A 353 4187 4760 5610 -464 31 -124 N ATOM 3774 N GLN A 354 12.515 -12.753 38.696 1.00 22.71 N ANISOU 3774 N GLN A 354 2949 2888 2789 5 -8 41 N ATOM 3775 CA GLN A 354 12.392 -14.205 38.472 1.00 23.67 C ANISOU 3775 CA GLN A 354 3055 3012 2926 -12 14 42 C ATOM 3776 C GLN A 354 11.515 -14.597 37.255 1.00 22.56 C ANISOU 3776 C GLN A 354 2910 2818 2842 -13 8 40 C ATOM 3777 O GLN A 354 11.365 -15.777 36.937 1.00 22.38 O ANISOU 3777 O GLN A 354 3002 2620 2879 41 29 15 O ATOM 3778 CB GLN A 354 11.960 -14.936 39.775 1.00 24.93 C ANISOU 3778 CB GLN A 354 3140 3195 3136 -8 43 44 C ATOM 3779 CG GLN A 354 10.457 -15.014 40.048 1.00 29.10 C ANISOU 3779 CG GLN A 354 3762 3790 3503 -6 153 62 C ATOM 3780 CD GLN A 354 9.897 -13.711 40.591 1.00 34.09 C ANISOU 3780 CD GLN A 354 4570 4376 4004 45 168 323 C ATOM 3781 OE1 GLN A 354 9.857 -12.719 39.869 1.00 38.20 O ANISOU 3781 OE1 GLN A 354 5116 5123 4272 -43 157 616 O ATOM 3782 NE2 GLN A 354 9.463 -13.708 41.862 1.00 36.34 N ANISOU 3782 NE2 GLN A 354 5080 5166 3561 -23 439 259 N ATOM 3783 N MET A 355 10.972 -13.607 36.553 1.00 20.77 N ANISOU 3783 N MET A 355 2678 2595 2615 5 21 26 N ATOM 3784 CA MET A 355 10.120 -13.888 35.410 1.00 19.84 C ANISOU 3784 CA MET A 355 2542 2484 2513 -4 25 13 C ATOM 3785 C MET A 355 10.863 -13.981 34.074 1.00 17.63 C ANISOU 3785 C MET A 355 2289 2156 2252 42 14 -12 C ATOM 3786 O MET A 355 10.321 -14.520 33.116 1.00 16.23 O ANISOU 3786 O MET A 355 2143 1887 2134 85 18 7 O ATOM 3787 CB MET A 355 9.009 -12.870 35.347 1.00 20.56 C ANISOU 3787 CB MET A 355 2613 2626 2570 -32 43 22 C ATOM 3788 CG MET A 355 7.895 -13.175 36.386 1.00 25.89 C ANISOU 3788 CG MET A 355 3330 3347 3157 219 -73 -141 C ATOM 3789 SD MET A 355 6.794 -11.823 36.367 1.00 36.94 S ANISOU 3789 SD MET A 355 4628 5012 4393 43 -118 -502 S ATOM 3790 CE MET A 355 5.722 -12.298 34.858 1.00 37.28 C ANISOU 3790 CE MET A 355 4677 4906 4580 -17 -112 -77 C ATOM 3791 N TRP A 356 12.082 -13.451 34.010 1.00 15.53 N ANISOU 3791 N TRP A 356 1992 1907 2002 39 8 -53 N ATOM 3792 CA TRP A 356 12.891 -13.530 32.805 1.00 14.82 C ANISOU 3792 CA TRP A 356 1902 1855 1873 30 16 -33 C ATOM 3793 C TRP A 356 13.182 -14.974 32.474 1.00 14.08 C ANISOU 3793 C TRP A 356 1777 1774 1795 50 65 -41 C ATOM 3794 O TRP A 356 13.359 -15.797 33.381 1.00 12.96 O ANISOU 3794 O TRP A 356 1717 1757 1447 171 138 -112 O ATOM 3795 CB TRP A 356 14.271 -12.895 32.990 1.00 14.87 C ANISOU 3795 CB TRP A 356 1866 1870 1912 -30 -5 -67 C ATOM 3796 CG TRP A 356 14.328 -11.421 33.275 1.00 15.03 C ANISOU 3796 CG TRP A 356 1921 1849 1938 84 -37 -39 C ATOM 3797 CD1 TRP A 356 14.539 -10.829 34.493 1.00 15.13 C ANISOU 3797 CD1 TRP A 356 1937 2003 1806 32 -97 -71 C ATOM 3798 CD2 TRP A 356 14.248 -10.354 32.324 1.00 14.47 C ANISOU 3798 CD2 TRP A 356 2012 1811 1672 -67 -55 47 C ATOM 3799 NE1 TRP A 356 14.585 -9.461 34.355 1.00 14.16 N ANISOU 3799 NE1 TRP A 356 2099 1552 1726 139 -29 -18 N ATOM 3800 CE2 TRP A 356 14.384 -9.141 33.037 1.00 14.76 C ANISOU 3800 CE2 TRP A 356 2245 1715 1649 -81 -37 18 C ATOM 3801 CE3 TRP A 356 14.053 -10.294 30.935 1.00 14.74 C ANISOU 3801 CE3 TRP A 356 2069 1836 1692 0 -167 45 C ATOM 3802 CZ2 TRP A 356 14.336 -7.887 32.409 1.00 15.08 C ANISOU 3802 CZ2 TRP A 356 2318 1739 1673 37 -242 -2 C ATOM 3803 CZ3 TRP A 356 14.013 -9.043 30.313 1.00 14.49 C ANISOU 3803 CZ3 TRP A 356 2020 1856 1627 3 -294 12 C ATOM 3804 CH2 TRP A 356 14.153 -7.863 31.047 1.00 14.38 C ANISOU 3804 CH2 TRP A 356 2102 1693 1667 -7 -210 56 C ATOM 3805 N ILE A 357 13.278 -15.268 31.180 1.00 13.06 N ANISOU 3805 N ILE A 357 1705 1671 1585 56 13 -12 N ATOM 3806 CA ILE A 357 13.946 -16.485 30.724 1.00 13.04 C ANISOU 3806 CA ILE A 357 1665 1643 1643 11 32 -19 C ATOM 3807 C ILE A 357 15.457 -16.279 30.835 1.00 13.22 C ANISOU 3807 C ILE A 357 1713 1666 1644 68 54 -26 C ATOM 3808 O ILE A 357 15.998 -15.375 30.220 1.00 12.71 O ANISOU 3808 O ILE A 357 1606 1544 1680 124 146 162 O ATOM 3809 CB ILE A 357 13.558 -16.816 29.271 1.00 12.74 C ANISOU 3809 CB ILE A 357 1572 1652 1614 33 31 -41 C ATOM 3810 CG1 ILE A 357 12.048 -17.003 29.155 1.00 13.72 C ANISOU 3810 CG1 ILE A 357 1753 1773 1683 -32 -18 -7 C ATOM 3811 CG2 ILE A 357 14.254 -18.108 28.823 1.00 12.85 C ANISOU 3811 CG2 ILE A 357 1613 1507 1760 -198 -48 -70 C ATOM 3812 CD1 ILE A 357 11.531 -16.891 27.752 1.00 14.08 C ANISOU 3812 CD1 ILE A 357 1661 1806 1880 -19 -115 -81 C ATOM 3813 N THR A 358 16.135 -17.097 31.629 1.00 13.39 N ANISOU 3813 N THR A 358 1752 1669 1665 82 34 10 N ATOM 3814 CA THR A 358 17.600 -17.006 31.751 1.00 14.36 C ANISOU 3814 CA THR A 358 1870 1775 1811 30 38 29 C ATOM 3815 C THR A 358 18.260 -17.868 30.682 1.00 14.31 C ANISOU 3815 C THR A 358 1804 1824 1808 74 11 3 C ATOM 3816 O THR A 358 17.641 -18.779 30.141 1.00 12.55 O ANISOU 3816 O THR A 358 1491 1638 1638 110 -44 -52 O ATOM 3817 CB THR A 358 18.120 -17.480 33.134 1.00 14.81 C ANISOU 3817 CB THR A 358 1908 1884 1832 40 17 -37 C ATOM 3818 OG1 THR A 358 17.713 -18.836 33.376 1.00 14.72 O ANISOU 3818 OG1 THR A 358 2060 1815 1717 -51 86 111 O ATOM 3819 CG2 THR A 358 17.516 -16.670 34.308 1.00 16.87 C ANISOU 3819 CG2 THR A 358 2195 2074 2142 51 80 -1 C ATOM 3820 N LYS A 359 19.534 -17.583 30.426 1.00 15.23 N ANISOU 3820 N LYS A 359 1913 1919 1952 8 -35 14 N ATOM 3821 CA LYS A 359 20.363 -18.363 29.515 1.00 16.18 C ANISOU 3821 CA LYS A 359 2023 2093 2031 1 -8 -5 C ATOM 3822 C LYS A 359 20.440 -19.837 29.978 1.00 16.45 C ANISOU 3822 C LYS A 359 2092 2098 2058 10 -12 71 C ATOM 3823 O LYS A 359 20.372 -20.749 29.166 1.00 15.90 O ANISOU 3823 O LYS A 359 2074 2010 1956 17 -14 93 O ATOM 3824 CB LYS A 359 21.769 -17.722 29.376 1.00 16.69 C ANISOU 3824 CB LYS A 359 2142 2106 2090 -20 0 40 C ATOM 3825 CG LYS A 359 22.765 -18.464 28.434 1.00 18.16 C ANISOU 3825 CG LYS A 359 2228 2403 2269 24 51 -3 C ATOM 3826 CD LYS A 359 22.130 -18.853 27.082 1.00 22.35 C ANISOU 3826 CD LYS A 359 2624 2958 2907 93 57 39 C ATOM 3827 CE LYS A 359 23.122 -19.110 25.921 1.00 23.69 C ANISOU 3827 CE LYS A 359 2949 3118 2932 78 258 34 C ATOM 3828 NZ LYS A 359 24.247 -20.049 26.294 1.00 26.03 N ANISOU 3828 NZ LYS A 359 3048 3605 3236 102 407 172 N ATOM 3829 N GLN A 360 20.541 -20.074 31.280 1.00 17.56 N ANISOU 3829 N GLN A 360 2204 2260 2208 -2 17 42 N ATOM 3830 CA GLN A 360 20.564 -21.458 31.793 1.00 18.39 C ANISOU 3830 CA GLN A 360 2345 2313 2329 23 -24 22 C ATOM 3831 C GLN A 360 19.257 -22.203 31.478 1.00 17.78 C ANISOU 3831 C GLN A 360 2210 2243 2303 41 -16 17 C ATOM 3832 O GLN A 360 19.284 -23.335 31.016 1.00 16.91 O ANISOU 3832 O GLN A 360 1957 2145 2324 102 -80 39 O ATOM 3833 CB GLN A 360 20.815 -21.481 33.309 1.00 19.48 C ANISOU 3833 CB GLN A 360 2470 2439 2490 17 9 39 C ATOM 3834 CG GLN A 360 20.604 -22.859 33.984 1.00 22.75 C ANISOU 3834 CG GLN A 360 3044 2763 2834 30 -57 30 C ATOM 3835 CD GLN A 360 21.107 -22.904 35.414 1.00 27.28 C ANISOU 3835 CD GLN A 360 3906 3067 3389 0 -69 66 C ATOM 3836 OE1 GLN A 360 21.483 -21.874 35.986 1.00 31.35 O ANISOU 3836 OE1 GLN A 360 4446 3621 3846 61 -63 66 O ATOM 3837 NE2 GLN A 360 21.120 -24.101 36.001 1.00 30.53 N ANISOU 3837 NE2 GLN A 360 4352 3462 3785 27 -59 59 N ATOM 3838 N GLU A 361 18.118 -21.563 31.744 1.00 17.72 N ANISOU 3838 N GLU A 361 2254 2224 2254 25 -19 34 N ATOM 3839 CA GLU A 361 16.808 -22.121 31.412 1.00 17.53 C ANISOU 3839 CA GLU A 361 2232 2170 2258 -10 18 42 C ATOM 3840 C GLU A 361 16.687 -22.422 29.911 1.00 17.05 C ANISOU 3840 C GLU A 361 2179 2148 2148 -5 3 38 C ATOM 3841 O GLU A 361 16.149 -23.457 29.522 1.00 16.39 O ANISOU 3841 O GLU A 361 2117 2091 2018 -117 -19 73 O ATOM 3842 CB GLU A 361 15.674 -21.173 31.846 1.00 17.85 C ANISOU 3842 CB GLU A 361 2256 2254 2269 13 74 44 C ATOM 3843 CG GLU A 361 15.405 -21.142 33.343 1.00 18.72 C ANISOU 3843 CG GLU A 361 2371 2325 2415 78 97 112 C ATOM 3844 CD GLU A 361 14.322 -20.132 33.731 1.00 20.89 C ANISOU 3844 CD GLU A 361 2652 2602 2680 262 416 301 C ATOM 3845 OE1 GLU A 361 13.555 -20.429 34.666 1.00 23.20 O ANISOU 3845 OE1 GLU A 361 3144 2876 2793 491 564 550 O ATOM 3846 OE2 GLU A 361 14.216 -19.046 33.104 1.00 19.49 O ANISOU 3846 OE2 GLU A 361 2429 2159 2815 209 637 348 O ATOM 3847 N TYR A 362 17.205 -21.529 29.075 1.00 16.62 N ANISOU 3847 N TYR A 362 2116 2069 2130 -24 0 40 N ATOM 3848 CA TYR A 362 17.189 -21.728 27.626 1.00 17.08 C ANISOU 3848 CA TYR A 362 2190 2115 2185 0 -3 -14 C ATOM 3849 C TYR A 362 18.060 -22.931 27.225 1.00 17.90 C ANISOU 3849 C TYR A 362 2296 2216 2289 18 -18 18 C ATOM 3850 O TYR A 362 17.661 -23.738 26.383 1.00 16.58 O ANISOU 3850 O TYR A 362 2159 1931 2210 26 -76 -81 O ATOM 3851 CB TYR A 362 17.659 -20.463 26.868 1.00 16.83 C ANISOU 3851 CB TYR A 362 2190 2121 2081 47 -21 -1 C ATOM 3852 CG TYR A 362 17.728 -20.679 25.367 1.00 16.84 C ANISOU 3852 CG TYR A 362 2180 2049 2168 40 12 24 C ATOM 3853 CD1 TYR A 362 16.581 -20.584 24.580 1.00 14.84 C ANISOU 3853 CD1 TYR A 362 1992 1763 1881 76 -49 114 C ATOM 3854 CD2 TYR A 362 18.929 -21.046 24.747 1.00 15.45 C ANISOU 3854 CD2 TYR A 362 1966 1934 1969 -12 -22 107 C ATOM 3855 CE1 TYR A 362 16.635 -20.818 23.214 1.00 16.51 C ANISOU 3855 CE1 TYR A 362 2145 1908 2218 -3 27 55 C ATOM 3856 CE2 TYR A 362 18.994 -21.290 23.391 1.00 15.23 C ANISOU 3856 CE2 TYR A 362 1920 1903 1963 -111 134 116 C ATOM 3857 CZ TYR A 362 17.849 -21.158 22.625 1.00 15.68 C ANISOU 3857 CZ TYR A 362 1885 2039 2031 -82 119 22 C ATOM 3858 OH TYR A 362 17.903 -21.393 21.284 1.00 17.33 O ANISOU 3858 OH TYR A 362 1846 2531 2205 -153 310 248 O ATOM 3859 N ASP A 363 19.245 -23.040 27.824 1.00 19.14 N ANISOU 3859 N ASP A 363 2429 2404 2437 -31 -18 -15 N ATOM 3860 CA ASP A 363 20.165 -24.141 27.534 1.00 20.29 C ANISOU 3860 CA ASP A 363 2568 2538 2601 5 -1 -38 C ATOM 3861 C ASP A 363 19.559 -25.501 27.878 1.00 21.00 C ANISOU 3861 C ASP A 363 2666 2624 2687 24 0 -17 C ATOM 3862 O ASP A 363 19.830 -26.483 27.192 1.00 21.12 O ANISOU 3862 O ASP A 363 2678 2487 2857 82 65 -120 O ATOM 3863 CB ASP A 363 21.490 -23.981 28.280 1.00 20.72 C ANISOU 3863 CB ASP A 363 2658 2591 2621 -14 22 -22 C ATOM 3864 CG ASP A 363 22.360 -22.884 27.706 1.00 23.31 C ANISOU 3864 CG ASP A 363 2853 3118 2884 -53 -6 -19 C ATOM 3865 OD1 ASP A 363 23.295 -22.441 28.419 1.00 27.36 O ANISOU 3865 OD1 ASP A 363 3133 3801 3461 -147 -18 -93 O ATOM 3866 OD2 ASP A 363 22.181 -22.390 26.566 1.00 26.15 O ANISOU 3866 OD2 ASP A 363 3176 3649 3110 -126 148 0 O ATOM 3867 N GLU A 364 18.727 -25.558 28.912 1.00 21.44 N ANISOU 3867 N GLU A 364 2711 2692 2743 52 -8 -33 N ATOM 3868 CA GLU A 364 18.149 -26.824 29.367 1.00 22.42 C ANISOU 3868 CA GLU A 364 2814 2836 2867 12 -22 -11 C ATOM 3869 C GLU A 364 16.894 -27.180 28.592 1.00 21.47 C ANISOU 3869 C GLU A 364 2662 2695 2800 9 -62 -19 C ATOM 3870 O GLU A 364 16.681 -28.337 28.284 1.00 21.44 O ANISOU 3870 O GLU A 364 2577 2602 2968 51 -98 -17 O ATOM 3871 CB GLU A 364 17.823 -26.774 30.859 1.00 23.15 C ANISOU 3871 CB GLU A 364 2895 2969 2930 16 -47 17 C ATOM 3872 CG GLU A 364 19.050 -26.543 31.729 1.00 27.47 C ANISOU 3872 CG GLU A 364 3443 3626 3368 -72 2 70 C ATOM 3873 CD GLU A 364 18.756 -26.603 33.226 1.00 32.40 C ANISOU 3873 CD GLU A 364 3793 4675 3841 -166 69 97 C ATOM 3874 OE1 GLU A 364 17.590 -26.879 33.594 1.00 35.38 O ANISOU 3874 OE1 GLU A 364 3651 5427 4364 -218 254 272 O ATOM 3875 OE2 GLU A 364 19.704 -26.377 34.032 1.00 34.89 O ANISOU 3875 OE2 GLU A 364 3939 5264 4051 -140 -196 178 O ATOM 3876 N ALA A 365 16.097 -26.175 28.248 1.00 20.30 N ANISOU 3876 N ALA A 365 2541 2526 2647 11 -54 -16 N ATOM 3877 CA ALA A 365 14.745 -26.377 27.713 1.00 19.84 C ANISOU 3877 CA ALA A 365 2460 2494 2582 -3 -23 3 C ATOM 3878 C ALA A 365 14.593 -26.109 26.210 1.00 18.85 C ANISOU 3878 C ALA A 365 2325 2353 2484 -10 -83 -15 C ATOM 3879 O ALA A 365 13.716 -26.665 25.568 1.00 19.27 O ANISOU 3879 O ALA A 365 2307 2284 2731 -3 -153 -13 O ATOM 3880 CB ALA A 365 13.758 -25.502 28.495 1.00 19.60 C ANISOU 3880 CB ALA A 365 2476 2398 2573 24 -64 -34 C ATOM 3881 N GLY A 366 15.435 -25.245 25.656 1.00 17.52 N ANISOU 3881 N GLY A 366 2125 2242 2287 -8 -62 20 N ATOM 3882 CA GLY A 366 15.327 -24.844 24.269 1.00 16.66 C ANISOU 3882 CA GLY A 366 2024 2151 2153 -20 -48 -15 C ATOM 3883 C GLY A 366 14.272 -23.749 24.111 1.00 16.10 C ANISOU 3883 C GLY A 366 1934 2109 2073 -15 -36 2 C ATOM 3884 O GLY A 366 13.637 -23.334 25.086 1.00 15.45 O ANISOU 3884 O GLY A 366 1715 2144 2010 59 -36 -82 O ATOM 3885 N PRO A 367 14.095 -23.277 22.883 1.00 15.39 N ANISOU 3885 N PRO A 367 1857 2000 1987 -37 -29 -6 N ATOM 3886 CA PRO A 367 13.204 -22.145 22.587 1.00 15.01 C ANISOU 3886 CA PRO A 367 1844 1937 1919 -11 -21 13 C ATOM 3887 C PRO A 367 11.729 -22.289 23.012 1.00 14.57 C ANISOU 3887 C PRO A 367 1822 1896 1816 0 -13 19 C ATOM 3888 O PRO A 367 11.049 -21.274 23.277 1.00 13.87 O ANISOU 3888 O PRO A 367 1826 1815 1626 39 -48 106 O ATOM 3889 CB PRO A 367 13.286 -22.027 21.064 1.00 15.25 C ANISOU 3889 CB PRO A 367 1842 1975 1974 38 -10 6 C ATOM 3890 CG PRO A 367 14.456 -22.812 20.630 1.00 16.47 C ANISOU 3890 CG PRO A 367 2001 2119 2135 -35 15 38 C ATOM 3891 CD PRO A 367 14.787 -23.784 21.681 1.00 15.42 C ANISOU 3891 CD PRO A 367 1874 1978 2007 -53 -47 83 C ATOM 3892 N SER A 368 11.234 -23.520 23.050 1.00 14.11 N ANISOU 3892 N SER A 368 1714 1844 1803 17 12 19 N ATOM 3893 CA SER A 368 9.847 -23.776 23.465 1.00 14.56 C ANISOU 3893 CA SER A 368 1845 1832 1853 -6 -39 4 C ATOM 3894 C SER A 368 9.554 -23.251 24.881 1.00 13.47 C ANISOU 3894 C SER A 368 1704 1736 1674 3 -3 8 C ATOM 3895 O SER A 368 8.406 -23.143 25.261 1.00 13.81 O ANISOU 3895 O SER A 368 1773 1808 1664 41 -163 -21 O ATOM 3896 CB SER A 368 9.492 -25.272 23.351 1.00 14.74 C ANISOU 3896 CB SER A 368 1845 1856 1897 -26 -53 -2 C ATOM 3897 OG SER A 368 9.991 -26.020 24.445 1.00 15.41 O ANISOU 3897 OG SER A 368 2002 1681 2169 -90 -120 11 O ATOM 3898 N ILE A 369 10.590 -22.901 25.643 1.00 12.42 N ANISOU 3898 N ILE A 369 1582 1593 1543 38 -28 54 N ATOM 3899 CA ILE A 369 10.397 -22.308 26.960 1.00 12.09 C ANISOU 3899 CA ILE A 369 1560 1488 1544 39 0 37 C ATOM 3900 C ILE A 369 9.558 -21.036 26.934 1.00 11.56 C ANISOU 3900 C ILE A 369 1429 1525 1435 61 -6 24 C ATOM 3901 O ILE A 369 8.884 -20.737 27.908 1.00 11.52 O ANISOU 3901 O ILE A 369 1512 1586 1278 145 -98 72 O ATOM 3902 CB ILE A 369 11.754 -22.074 27.668 1.00 11.88 C ANISOU 3902 CB ILE A 369 1504 1465 1543 82 30 -44 C ATOM 3903 CG1 ILE A 369 11.560 -21.724 29.148 1.00 14.68 C ANISOU 3903 CG1 ILE A 369 1933 1637 2005 38 4 30 C ATOM 3904 CG2 ILE A 369 12.501 -20.984 27.025 1.00 12.42 C ANISOU 3904 CG2 ILE A 369 1446 1512 1759 153 29 20 C ATOM 3905 CD1 ILE A 369 11.379 -22.834 30.040 1.00 16.83 C ANISOU 3905 CD1 ILE A 369 2151 1880 2361 165 143 -39 C ATOM 3906 N VAL A 370 9.603 -20.307 25.822 1.00 10.69 N ANISOU 3906 N VAL A 370 1382 1330 1349 45 -1 44 N ATOM 3907 CA VAL A 370 8.889 -19.053 25.674 1.00 11.52 C ANISOU 3907 CA VAL A 370 1514 1434 1430 5 33 13 C ATOM 3908 C VAL A 370 7.380 -19.192 25.867 1.00 11.10 C ANISOU 3908 C VAL A 370 1510 1346 1360 17 42 90 C ATOM 3909 O VAL A 370 6.752 -18.309 26.436 1.00 11.65 O ANISOU 3909 O VAL A 370 1651 1147 1629 -23 154 203 O ATOM 3910 CB VAL A 370 9.265 -18.352 24.332 1.00 11.40 C ANISOU 3910 CB VAL A 370 1494 1414 1422 78 -20 54 C ATOM 3911 CG1 VAL A 370 8.691 -19.088 23.154 1.00 13.28 C ANISOU 3911 CG1 VAL A 370 1878 1480 1688 57 16 -5 C ATOM 3912 CG2 VAL A 370 8.829 -16.901 24.315 1.00 12.84 C ANISOU 3912 CG2 VAL A 370 1740 1557 1581 -52 -33 -151 C ATOM 3913 N HIS A 371 6.809 -20.329 25.502 1.00 10.85 N ANISOU 3913 N HIS A 371 1459 1411 1252 -30 28 24 N ATOM 3914 CA HIS A 371 5.364 -20.528 25.664 1.00 11.92 C ANISOU 3914 CA HIS A 371 1583 1513 1432 21 11 3 C ATOM 3915 C HIS A 371 4.910 -20.792 27.087 1.00 11.97 C ANISOU 3915 C HIS A 371 1570 1493 1484 -6 55 57 C ATOM 3916 O HIS A 371 3.720 -20.738 27.369 1.00 12.30 O ANISOU 3916 O HIS A 371 1683 1581 1408 44 3 206 O ATOM 3917 CB HIS A 371 4.913 -21.701 24.835 1.00 12.69 C ANISOU 3917 CB HIS A 371 1552 1678 1590 -20 8 -7 C ATOM 3918 CG HIS A 371 5.394 -21.646 23.434 1.00 12.75 C ANISOU 3918 CG HIS A 371 1613 1765 1465 34 10 -84 C ATOM 3919 ND1 HIS A 371 6.131 -22.664 22.866 1.00 14.40 N ANISOU 3919 ND1 HIS A 371 1643 2146 1682 142 -153 -158 N ATOM 3920 CD2 HIS A 371 5.279 -20.683 22.494 1.00 12.85 C ANISOU 3920 CD2 HIS A 371 1404 1750 1727 121 -38 -101 C ATOM 3921 CE1 HIS A 371 6.426 -22.334 21.623 1.00 14.75 C ANISOU 3921 CE1 HIS A 371 1796 1907 1898 145 165 -129 C ATOM 3922 NE2 HIS A 371 5.913 -21.145 21.368 1.00 14.84 N ANISOU 3922 NE2 HIS A 371 1804 2026 1808 133 -73 76 N ATOM 3923 N ARG A 372 5.850 -21.120 27.957 1.00 11.53 N ANISOU 3923 N ARG A 372 1525 1438 1418 3 -42 -13 N ATOM 3924 CA ARG A 372 5.544 -21.430 29.349 1.00 12.72 C ANISOU 3924 CA ARG A 372 1647 1558 1626 -14 40 -117 C ATOM 3925 C ARG A 372 5.883 -20.235 30.255 1.00 14.06 C ANISOU 3925 C ARG A 372 1855 1738 1747 -65 40 -168 C ATOM 3926 O ARG A 372 5.190 -19.995 31.207 1.00 14.91 O ANISOU 3926 O ARG A 372 2116 1808 1740 -147 83 -514 O ATOM 3927 CB ARG A 372 6.283 -22.694 29.798 1.00 12.02 C ANISOU 3927 CB ARG A 372 1532 1502 1532 -14 46 -83 C ATOM 3928 CG ARG A 372 5.859 -23.926 28.978 1.00 13.09 C ANISOU 3928 CG ARG A 372 1743 1461 1768 71 56 -158 C ATOM 3929 CD ARG A 372 6.527 -25.256 29.374 1.00 14.80 C ANISOU 3929 CD ARG A 372 1990 1697 1934 -94 -134 -131 C ATOM 3930 NE ARG A 372 7.986 -25.221 29.518 1.00 15.93 N ANISOU 3930 NE ARG A 372 2160 1536 2355 41 306 -182 N ATOM 3931 CZ ARG A 372 8.861 -25.621 28.600 1.00 18.73 C ANISOU 3931 CZ ARG A 372 2542 2159 2413 -133 -13 -104 C ATOM 3932 NH1 ARG A 372 10.145 -25.569 28.863 1.00 18.62 N ANISOU 3932 NH1 ARG A 372 2246 2452 2377 -74 -77 -179 N ATOM 3933 NH2 ARG A 372 8.479 -26.065 27.411 1.00 22.14 N ANISOU 3933 NH2 ARG A 372 2864 2568 2977 -121 14 149 N ATOM 3934 N LYS A 373 6.905 -19.470 29.921 1.00 15.70 N ANISOU 3934 N LYS A 373 2035 1904 2025 -25 -21 -119 N ATOM 3935 CA LYS A 373 7.317 -18.318 30.743 1.00 17.40 C ANISOU 3935 CA LYS A 373 2246 2125 2238 6 -14 -33 C ATOM 3936 C LYS A 373 6.666 -16.988 30.329 1.00 18.89 C ANISOU 3936 C LYS A 373 2463 2264 2449 -12 4 -74 C ATOM 3937 O LYS A 373 6.546 -16.103 31.164 1.00 18.87 O ANISOU 3937 O LYS A 373 2609 2154 2405 30 5 -90 O ATOM 3938 CB LYS A 373 8.836 -18.167 30.676 1.00 17.76 C ANISOU 3938 CB LYS A 373 2296 2141 2310 -43 -12 -46 C ATOM 3939 CG LYS A 373 9.617 -19.323 31.269 1.00 19.11 C ANISOU 3939 CG LYS A 373 2396 2393 2470 74 32 -7 C ATOM 3940 CD LYS A 373 9.905 -19.163 32.752 1.00 21.86 C ANISOU 3940 CD LYS A 373 2824 2774 2707 29 -19 -54 C ATOM 3941 CE LYS A 373 10.852 -17.999 33.060 1.00 22.14 C ANISOU 3941 CE LYS A 373 2862 2768 2780 -108 99 115 C ATOM 3942 NZ LYS A 373 11.595 -18.136 34.378 1.00 22.85 N ANISOU 3942 NZ LYS A 373 3217 2928 2535 -89 217 26 N ATOM 3943 N CYS A 374 6.252 -16.869 29.061 1.00 20.25 N ANISOU 3943 N CYS A 374 2665 2458 2568 -1 11 -9 N ATOM 3944 CA CYS A 374 5.716 -15.630 28.487 1.00 22.12 C ANISOU 3944 CA CYS A 374 2841 2774 2790 -22 7 -24 C ATOM 3945 C CYS A 374 4.329 -15.815 27.879 1.00 24.60 C ANISOU 3945 C CYS A 374 3161 3073 3111 35 24 -48 C ATOM 3946 O CYS A 374 4.203 -16.341 26.787 1.00 24.11 O ANISOU 3946 O CYS A 374 3123 3051 2984 146 82 -127 O ATOM 3947 CB CYS A 374 6.662 -15.109 27.374 1.00 22.17 C ANISOU 3947 CB CYS A 374 2848 2764 2810 24 -6 -3 C ATOM 3948 SG CYS A 374 8.378 -14.755 27.885 1.00 21.06 S ANISOU 3948 SG CYS A 374 2728 2620 2651 -369 -144 58 S ATOM 3949 N PHE A 375 3.272 -15.364 28.553 1.00 27.67 N ANISOU 3949 N PHE A 375 3597 3472 3442 -9 -24 -38 N ATOM 3950 CA PHE A 375 1.962 -15.275 27.887 1.00 30.13 C ANISOU 3950 CA PHE A 375 3918 3770 3759 -41 -43 44 C ATOM 3951 C PHE A 375 1.957 -14.223 26.745 1.00 31.73 C ANISOU 3951 C PHE A 375 4222 3897 3937 -98 -124 22 C ATOM 3952 O PHE A 375 2.491 -13.105 26.872 1.00 32.57 O ANISOU 3952 O PHE A 375 4326 3956 4091 -282 -169 -8 O ATOM 3953 CB PHE A 375 0.846 -14.974 28.884 1.00 30.48 C ANISOU 3953 CB PHE A 375 3963 3841 3777 -78 0 74 C ATOM 3954 CG PHE A 375 0.250 -16.217 29.490 1.00 32.69 C ANISOU 3954 CG PHE A 375 4208 4156 4055 -113 -56 142 C ATOM 3955 CD1 PHE A 375 0.758 -16.738 30.678 1.00 34.08 C ANISOU 3955 CD1 PHE A 375 4387 4336 4224 -66 -100 245 C ATOM 3956 CD2 PHE A 375 -0.786 -16.887 28.854 1.00 32.94 C ANISOU 3956 CD2 PHE A 375 4388 4103 4024 -180 -106 107 C ATOM 3957 CE1 PHE A 375 0.215 -17.890 31.236 1.00 32.95 C ANISOU 3957 CE1 PHE A 375 4346 4008 4164 -38 -80 113 C ATOM 3958 CE2 PHE A 375 -1.336 -18.036 29.411 1.00 32.76 C ANISOU 3958 CE2 PHE A 375 4419 3944 4081 -41 -81 37 C ATOM 3959 CZ PHE A 375 -0.833 -18.531 30.608 1.00 32.50 C ANISOU 3959 CZ PHE A 375 4337 3818 4192 -16 -46 31 C ATOM 3960 OXT PHE A 375 1.410 -14.447 25.638 1.00 33.14 O ANISOU 3960 OXT PHE A 375 4545 3974 4072 -38 -264 82 O TER 3961 PHE A 375 HETATM 3962 CA CA G 701 -8.628 -12.961 39.545 1.00 19.67 CA ANISOU 3962 CA CA G 701 2591 2622 2260 59 -28 -97 CA HETATM 3963 CA CA G 702 4.705 9.684 43.909 1.00 19.95 CA ANISOU 3963 CA CA G 702 2517 2622 2439 -162 -153 -194 CA HETATM 3964 CA CA A 700 3.648 -1.183 17.205 1.00 21.94 CA ANISOU 3964 CA CA A 700 2654 3248 2432 -299 -139 157 CA HETATM 3965 PG ATP A 900 2.812 -1.410 13.787 1.00 21.50 P ANISOU 3965 PG ATP A 900 2531 2655 2982 -535 317 247 P HETATM 3966 O1G ATP A 900 3.601 -2.634 13.542 1.00 20.46 O ANISOU 3966 O1G ATP A 900 2904 2096 2772 -344 214 -4 O HETATM 3967 O2G ATP A 900 1.654 -1.315 12.785 1.00 22.27 O ANISOU 3967 O2G ATP A 900 2955 2825 2679 -722 366 41 O HETATM 3968 O3G ATP A 900 2.281 -1.350 15.232 1.00 20.84 O ANISOU 3968 O3G ATP A 900 2622 2717 2579 -315 322 -176 O HETATM 3969 PB ATP A 900 4.714 0.703 14.385 1.00 19.48 P ANISOU 3969 PB ATP A 900 2349 2629 2422 -237 404 84 P HETATM 3970 O1B ATP A 900 5.962 0.960 13.658 1.00 17.99 O ANISOU 3970 O1B ATP A 900 2126 2576 2133 -632 -23 -243 O HETATM 3971 O2B ATP A 900 4.931 0.027 15.731 1.00 19.37 O ANISOU 3971 O2B ATP A 900 2216 3155 1987 -384 197 34 O HETATM 3972 O3B ATP A 900 3.790 -0.167 13.420 1.00 21.42 O ANISOU 3972 O3B ATP A 900 2740 2660 2739 -511 299 104 O HETATM 3973 PA ATP A 900 3.950 3.283 15.472 1.00 21.38 P ANISOU 3973 PA ATP A 900 2804 2980 2336 -234 -39 111 P HETATM 3974 O1A ATP A 900 3.021 3.080 16.595 1.00 21.61 O ANISOU 3974 O1A ATP A 900 2401 3378 2431 139 -142 -47 O HETATM 3975 O2A ATP A 900 5.407 3.481 15.904 1.00 22.48 O ANISOU 3975 O2A ATP A 900 3110 3269 2160 -332 -116 -76 O HETATM 3976 O3A ATP A 900 3.819 2.042 14.444 1.00 22.38 O ANISOU 3976 O3A ATP A 900 2800 3129 2571 -381 354 184 O HETATM 3977 O5' ATP A 900 3.388 4.498 14.568 1.00 23.75 O ANISOU 3977 O5' ATP A 900 2979 3201 2842 -153 32 69 O HETATM 3978 C5' ATP A 900 3.927 4.841 13.303 1.00 23.62 C ANISOU 3978 C5' ATP A 900 2897 3181 2893 -12 91 50 C HETATM 3979 C4' ATP A 900 2.791 5.314 12.402 1.00 24.25 C ANISOU 3979 C4' ATP A 900 3004 3143 3065 -159 100 118 C HETATM 3980 O4' ATP A 900 2.077 6.367 13.032 1.00 24.88 O ANISOU 3980 O4' ATP A 900 2894 3469 3087 -118 311 137 O HETATM 3981 C3' ATP A 900 3.226 5.858 11.050 1.00 25.01 C ANISOU 3981 C3' ATP A 900 3188 3391 2923 -58 107 12 C HETATM 3982 O3' ATP A 900 2.313 5.414 10.045 1.00 26.51 O ANISOU 3982 O3' ATP A 900 3440 3404 3227 -382 343 177 O HETATM 3983 C2' ATP A 900 3.165 7.356 11.253 1.00 23.04 C ANISOU 3983 C2' ATP A 900 3024 3070 2657 -127 55 13 C HETATM 3984 O2' ATP A 900 3.039 8.128 10.093 1.00 24.78 O ANISOU 3984 O2' ATP A 900 3153 3140 3121 -100 105 -142 O HETATM 3985 C1' ATP A 900 1.943 7.464 12.152 1.00 22.99 C ANISOU 3985 C1' ATP A 900 2721 3044 2969 -101 64 134 C HETATM 3986 N9 ATP A 900 1.924 8.707 12.918 1.00 23.37 N ANISOU 3986 N9 ATP A 900 2638 3328 2910 22 87 220 N HETATM 3987 C8 ATP A 900 2.896 9.177 13.771 1.00 24.03 C ANISOU 3987 C8 ATP A 900 2756 3405 2967 84 -76 249 C HETATM 3988 N7 ATP A 900 2.494 10.359 14.289 1.00 21.59 N ANISOU 3988 N7 ATP A 900 2514 2877 2810 -18 -9 207 N HETATM 3989 C5 ATP A 900 1.282 10.661 13.758 1.00 23.02 C ANISOU 3989 C5 ATP A 900 2624 3180 2942 -44 61 201 C HETATM 3990 C6 ATP A 900 0.418 11.749 13.911 1.00 22.15 C ANISOU 3990 C6 ATP A 900 2577 2830 3009 -8 -60 266 C HETATM 3991 N6 ATP A 900 0.738 12.808 14.651 1.00 24.04 N ANISOU 3991 N6 ATP A 900 2538 3110 3482 -341 38 113 N HETATM 3992 N1 ATP A 900 -0.775 11.757 13.243 1.00 21.26 N ANISOU 3992 N1 ATP A 900 2613 2657 2808 67 -156 402 N HETATM 3993 C2 ATP A 900 -1.110 10.721 12.411 1.00 22.17 C ANISOU 3993 C2 ATP A 900 2692 2819 2911 113 -180 314 C HETATM 3994 N3 ATP A 900 -0.255 9.645 12.221 1.00 23.03 N ANISOU 3994 N3 ATP A 900 2293 3286 3168 -3 -145 389 N HETATM 3995 C4 ATP A 900 0.915 9.620 12.905 1.00 22.97 C ANISOU 3995 C4 ATP A 900 2574 3221 2930 22 4 357 C HETATM 3996 O HOH G 703 3.518 5.510 44.727 1.00 9.48 O ANISOU 3996 O HOH G 703 1247 1713 641 568 -225 118 O HETATM 3997 O HOH G 704 4.776 11.883 44.640 1.00 7.70 O ANISOU 3997 O HOH G 704 1159 937 829 -417 80 -353 O HETATM 3998 O HOH G 705 -1.728 11.134 38.189 1.00 14.56 O ANISOU 3998 O HOH G 705 2277 2136 1119 -1 -353 610 O HETATM 3999 O HOH G 706 -5.024 -9.136 53.366 1.00 9.55 O ANISOU 3999 O HOH G 706 1594 1369 663 83 508 282 O HETATM 4000 O HOH G 707 -4.455 -10.050 55.918 1.00 15.16 O ANISOU 4000 O HOH G 707 1580 1650 2530 554 -62 -354 O HETATM 4001 O HOH G 708 -11.717 -14.524 46.305 1.00 13.75 O ANISOU 4001 O HOH G 708 2070 1815 1338 -1178 642 410 O HETATM 4002 O HOH G 709 -12.096 -7.313 38.262 1.00 13.27 O ANISOU 4002 O HOH G 709 1424 2107 1510 -492 -390 94 O HETATM 4003 O HOH G 710 -3.091 3.768 53.790 1.00 14.14 O ANISOU 4003 O HOH G 710 3218 783 1369 -853 -439 673 O HETATM 4004 O HOH G 711 -0.689 5.466 34.075 1.00 15.31 O ANISOU 4004 O HOH G 711 2216 1089 2510 -151 90 -78 O HETATM 4005 O HOH G 712 -6.937 -13.552 37.954 1.00 13.76 O ANISOU 4005 O HOH G 712 2035 2065 1126 341 554 138 O HETATM 4006 O HOH G 713 -13.527 9.356 54.264 1.00 15.64 O ANISOU 4006 O HOH G 713 2412 1329 2202 39 444 714 O HETATM 4007 O HOH G 714 0.588 15.448 45.761 1.00 10.45 O ANISOU 4007 O HOH G 714 1906 415 1647 300 754 -198 O HETATM 4008 O HOH G 715 -2.422 -12.072 55.586 1.00 12.97 O ANISOU 4008 O HOH G 715 2292 1462 1173 -945 -298 553 O HETATM 4009 O HOH G 716 -0.323 8.214 36.943 1.00 11.17 O ANISOU 4009 O HOH G 716 1947 1480 814 632 154 413 O HETATM 4010 O HOH G 717 12.613 6.744 -4.225 1.00 34.92 O ANISOU 4010 O HOH G 717 3382 5099 4784 955 2394 2682 O HETATM 4011 O HOH G 718 3.175 -6.645 54.846 1.00 18.57 O ANISOU 4011 O HOH G 718 1981 2589 2484 -550 416 551 O HETATM 4012 O HOH G 719 1.359 -3.138 56.062 1.00 14.37 O ANISOU 4012 O HOH G 719 2254 2171 1036 -303 -378 180 O HETATM 4013 O HOH G 720 -12.422 -9.792 50.338 1.00 16.47 O ANISOU 4013 O HOH G 720 2468 2310 1479 -228 204 -501 O HETATM 4014 O HOH G 721 7.796 5.849 43.262 1.00 15.23 O ANISOU 4014 O HOH G 721 1208 2775 1804 -224 -388 -372 O HETATM 4015 O HOH G 722 -13.872 -7.225 50.478 1.00 16.56 O ANISOU 4015 O HOH G 722 2311 2103 1877 -617 584 -996 O HETATM 4016 O HOH G 723 -12.230 -1.796 38.434 1.00 20.13 O ANISOU 4016 O HOH G 723 3063 1635 2951 -1104 377 1229 O HETATM 4017 O HOH G 724 -9.751 -14.452 37.718 1.00 21.20 O ANISOU 4017 O HOH G 724 5116 1209 1728 1332 -293 393 O HETATM 4018 O HOH G 725 7.871 3.771 41.181 1.00 18.95 O ANISOU 4018 O HOH G 725 2247 2675 2278 656 659 10 O HETATM 4019 O HOH G 726 18.007 13.309 2.139 1.00 24.22 O ANISOU 4019 O HOH G 726 3627 3638 1936 1483 850 912 O HETATM 4020 O HOH G 727 -6.218 -6.105 59.386 1.00 26.22 O ANISOU 4020 O HOH G 727 5069 3532 1360 -1360 -385 711 O HETATM 4021 O HOH G 728 1.372 5.923 53.134 1.00 17.85 O ANISOU 4021 O HOH G 728 3018 2612 1153 -583 175 405 O HETATM 4022 O HOH G 729 -10.964 -13.570 39.674 1.00 15.95 O ANISOU 4022 O HOH G 729 1331 1482 3245 702 2 63 O HETATM 4023 O HOH G 730 5.484 10.380 41.831 1.00 12.53 O ANISOU 4023 O HOH G 730 1119 2116 1525 214 -428 238 O HETATM 4024 O HOH G 731 -18.840 -1.058 46.113 1.00 21.01 O ANISOU 4024 O HOH G 731 2430 3187 2366 -1374 -504 -934 O HETATM 4025 O HOH G 732 -4.060 5.469 35.480 1.00 23.26 O ANISOU 4025 O HOH G 732 4057 2832 1949 874 79 -770 O HETATM 4026 O HOH G 733 1.223 -4.736 53.937 1.00 16.42 O ANISOU 4026 O HOH G 733 1951 1944 2342 698 -126 750 O HETATM 4027 O HOH G 734 -10.978 -3.517 56.836 1.00 26.64 O ANISOU 4027 O HOH G 734 2934 2971 4215 698 1114 1126 O HETATM 4028 O HOH G 735 -16.232 -2.708 52.897 1.00 19.31 O ANISOU 4028 O HOH G 735 2506 2012 2816 -540 1061 -357 O HETATM 4029 O HOH G 736 -14.494 9.412 47.545 1.00 22.40 O ANISOU 4029 O HOH G 736 2540 1792 4177 632 -1831 -234 O HETATM 4030 O HOH G 737 8.705 12.682 41.299 1.00 19.60 O ANISOU 4030 O HOH G 737 3095 1990 2361 281 -139 -383 O HETATM 4031 O HOH G 738 -14.742 -11.146 46.833 1.00 29.52 O ANISOU 4031 O HOH G 738 5150 3124 2940 -1056 -1348 226 O HETATM 4032 O HOH G 739 2.845 -13.673 40.056 1.00 15.85 O ANISOU 4032 O HOH G 739 1854 1780 2385 384 -564 749 O HETATM 4033 O HOH G 740 -12.626 4.435 41.087 1.00 16.52 O ANISOU 4033 O HOH G 740 944 2276 3055 22 -1130 45 O HETATM 4034 O HOH G 741 -3.350 18.849 43.830 1.00 17.52 O ANISOU 4034 O HOH G 741 1485 883 4288 -194 -717 348 O HETATM 4035 O HOH G 742 -5.267 15.771 45.387 1.00 17.33 O ANISOU 4035 O HOH G 742 2811 1623 2147 -269 164 815 O HETATM 4036 O HOH G 743 -1.965 17.513 52.892 1.00 14.74 O ANISOU 4036 O HOH G 743 2230 1527 1843 376 905 -1016 O HETATM 4037 O HOH G 744 -3.192 7.477 36.974 1.00 20.92 O ANISOU 4037 O HOH G 744 1551 3192 3204 -38 -549 -138 O HETATM 4038 O HOH G 745 -13.766 5.562 53.961 1.00 15.72 O ANISOU 4038 O HOH G 745 1653 1934 2384 128 418 -762 O HETATM 4039 O HOH G 746 3.801 -9.758 35.114 1.00 30.44 O ANISOU 4039 O HOH G 746 3877 4130 3557 -89 951 -779 O HETATM 4040 O HOH G 747 15.688 20.114 0.427 1.00 25.98 O ANISOU 4040 O HOH G 747 3181 2558 4132 532 1106 45 O HETATM 4041 O HOH G 748 12.301 -1.016 48.002 1.00 26.47 O ANISOU 4041 O HOH G 748 2521 4868 2669 -267 -821 669 O HETATM 4042 O HOH G 749 18.549 5.838 -9.976 1.00 42.41 O ANISOU 4042 O HOH G 749 4457 5915 5741 158 1068 -1261 O HETATM 4043 O HOH G 750 10.993 10.552 47.396 1.00 18.14 O ANISOU 4043 O HOH G 750 1723 2271 2896 -729 -474 196 O HETATM 4044 O HOH G 751 -11.466 -10.032 57.204 1.00 14.32 O ANISOU 4044 O HOH G 751 1643 1206 2591 261 94 -657 O HETATM 4045 O HOH G 752 -9.105 -18.452 40.131 1.00 20.77 O ANISOU 4045 O HOH G 752 3193 1172 3524 -710 537 683 O HETATM 4046 O HOH G 753 -6.046 9.339 40.172 1.00 17.80 O ANISOU 4046 O HOH G 753 1985 1731 3044 355 63 122 O HETATM 4047 O HOH G 754 -10.121 9.730 59.320 1.00 25.17 O ANISOU 4047 O HOH G 754 2813 6364 384 861 -46 -696 O HETATM 4048 O HOH G 755 9.383 9.305 12.100 1.00 24.43 O ANISOU 4048 O HOH G 755 2950 3760 2572 160 186 596 O HETATM 4049 O HOH G 756 -9.058 -17.246 37.884 1.00 16.72 O ANISOU 4049 O HOH G 756 2577 1288 2485 -257 -841 -1086 O HETATM 4050 O HOH G 757 -10.037 4.051 59.194 1.00 24.81 O ANISOU 4050 O HOH G 757 2900 2719 3805 462 -531 733 O HETATM 4051 O HOH G 758 5.282 2.701 52.769 1.00 18.68 O ANISOU 4051 O HOH G 758 443 3345 3307 -494 -436 -791 O HETATM 4052 O HOH G 759 3.324 13.657 42.529 1.00 20.87 O ANISOU 4052 O HOH G 759 2260 1594 4075 675 -244 -601 O HETATM 4053 O HOH G 760 -7.455 11.820 39.803 1.00 27.37 O ANISOU 4053 O HOH G 760 2025 3480 4892 552 -1131 -72 O HETATM 4054 O HOH G 761 -18.781 2.518 52.208 1.00 17.12 O ANISOU 4054 O HOH G 761 2492 1413 2599 -341 314 757 O HETATM 4055 O HOH G 762 3.757 4.601 53.653 1.00 15.03 O ANISOU 4055 O HOH G 762 1440 2444 1826 253 120 -248 O HETATM 4056 O HOH G 763 -8.592 -20.390 50.580 1.00 25.46 O ANISOU 4056 O HOH G 763 5287 2818 1568 1799 789 -294 O HETATM 4057 O HOH G 764 20.372 14.830 -6.692 1.00 30.40 O ANISOU 4057 O HOH G 764 5317 2689 3543 0 135 139 O HETATM 4058 O HOH G 765 -4.015 9.165 38.483 1.00 29.32 O ANISOU 4058 O HOH G 765 4355 3701 3083 -83 13 -446 O HETATM 4059 O HOH G 766 2.029 7.686 55.070 1.00 27.72 O ANISOU 4059 O HOH G 766 4627 2687 3218 450 -678 1153 O HETATM 4060 O HOH G 767 -1.920 -14.363 63.582 1.00 23.27 O ANISOU 4060 O HOH G 767 3593 1953 3291 -135 67 321 O HETATM 4061 O HOH G 768 4.212 10.626 34.994 1.00 26.42 O ANISOU 4061 O HOH G 768 4764 2869 2405 -2390 -208 -764 O HETATM 4062 O HOH G 769 -16.308 7.709 46.077 1.00 20.24 O ANISOU 4062 O HOH G 769 3381 1660 2650 480 1112 -211 O HETATM 4063 O HOH G 770 -11.530 2.881 37.314 1.00 29.71 O ANISOU 4063 O HOH G 770 2966 4051 4271 458 229 -563 O HETATM 4064 O HOH G 771 0.574 16.676 53.139 1.00 15.15 O ANISOU 4064 O HOH G 771 2828 1637 1289 205 -73 -228 O HETATM 4065 O HOH G 772 15.205 4.350 36.748 1.00 24.20 O ANISOU 4065 O HOH G 772 3602 2772 2818 958 -1243 -106 O HETATM 4066 O HOH G 773 14.464 10.264 3.812 1.00 27.31 O ANISOU 4066 O HOH G 773 4098 2721 3555 1465 -659 476 O HETATM 4067 O HOH G 774 15.868 11.940 35.845 1.00 23.16 O ANISOU 4067 O HOH G 774 3870 2538 2391 -1768 -567 501 O HETATM 4068 O HOH G 775 -0.406 19.360 43.971 1.00 29.23 O ANISOU 4068 O HOH G 775 3494 3326 4284 861 521 -303 O HETATM 4069 O HOH G 776 6.950 13.407 45.572 1.00 23.60 O ANISOU 4069 O HOH G 776 3525 2054 3386 -380 -73 -102 O HETATM 4070 O HOH G 777 -8.046 -13.432 34.873 1.00 39.78 O ANISOU 4070 O HOH G 777 6450 3431 5234 -470 -2484 -64 O HETATM 4071 O HOH G 778 1.926 -10.141 33.757 1.00 35.39 O ANISOU 4071 O HOH G 778 2640 6340 4467 -538 596 235 O HETATM 4072 O HOH G 779 -10.110 14.381 44.885 1.00 25.55 O ANISOU 4072 O HOH G 779 3087 1979 4643 1497 915 196 O HETATM 4073 O HOH G 780 7.129 7.739 16.740 1.00 25.15 O ANISOU 4073 O HOH G 780 3620 2854 3082 187 -436 -596 O HETATM 4074 O HOH G 781 -15.506 -4.200 54.840 1.00 30.39 O ANISOU 4074 O HOH G 781 3038 4300 4208 -1568 1719 1575 O HETATM 4075 O HOH G 782 -18.735 4.843 46.115 1.00 25.98 O ANISOU 4075 O HOH G 782 1582 2691 5597 -906 -1199 79 O HETATM 4076 O HOH G 783 -1.886 -5.676 57.953 1.00 31.42 O ANISOU 4076 O HOH G 783 5053 4833 2052 1460 338 -317 O HETATM 4077 O HOH G 784 -14.823 -7.088 52.932 1.00 24.76 O ANISOU 4077 O HOH G 784 2887 1387 5133 -29 357 705 O HETATM 4078 O HOH G 785 -19.610 1.761 44.894 1.00 24.29 O ANISOU 4078 O HOH G 785 546 4613 4067 -1071 -467 582 O HETATM 4079 O HOH G 786 -10.197 -9.448 59.731 1.00 35.21 O ANISOU 4079 O HOH G 786 3312 4858 5205 -121 549 -103 O HETATM 4080 O HOH G 787 3.134 9.884 30.965 1.00 37.76 O ANISOU 4080 O HOH G 787 5788 2394 6162 179 -29 961 O HETATM 4081 O HOH G 788 -12.911 -12.324 57.781 1.00 23.46 O ANISOU 4081 O HOH G 788 3910 4020 981 -1766 1111 -351 O HETATM 4082 O HOH G 789 -0.939 10.426 57.845 1.00 27.49 O ANISOU 4082 O HOH G 789 4377 3194 2871 -1369 814 -345 O HETATM 4083 O HOH G 790 2.496 -13.336 37.404 1.00 22.39 O ANISOU 4083 O HOH G 790 2863 3541 2103 -366 1034 56 O HETATM 4084 O HOH G 791 -12.841 5.522 38.470 1.00 29.31 O ANISOU 4084 O HOH G 791 1630 5867 3636 4 -1344 -2143 O HETATM 4085 O HOH G 792 2.331 13.542 38.443 1.00 31.81 O ANISOU 4085 O HOH G 792 3941 4603 3542 -79 976 736 O HETATM 4086 O HOH G 793 10.254 11.689 10.292 1.00 30.66 O ANISOU 4086 O HOH G 793 2360 4028 5259 -297 1935 184 O HETATM 4087 O HOH G 794 11.282 19.180 3.728 1.00 27.81 O ANISOU 4087 O HOH G 794 2431 3005 5131 1470 573 -656 O HETATM 4088 O HOH G 795 1.065 -15.880 50.842 1.00 24.31 O ANISOU 4088 O HOH G 795 2780 2784 3672 -827 980 -1816 O HETATM 4089 O HOH G 796 -17.253 -9.870 51.723 1.00 29.57 O ANISOU 4089 O HOH G 796 2848 3678 4709 193 425 -917 O HETATM 4090 O HOH G 797 5.208 15.041 41.439 1.00 28.74 O ANISOU 4090 O HOH G 797 3876 4317 2726 310 -256 187 O HETATM 4091 O HOH G 798 -12.248 -14.723 42.025 1.00 21.66 O ANISOU 4091 O HOH G 798 3765 1584 2878 1080 724 20 O HETATM 4092 O HOH G 799 1.409 -8.179 56.292 1.00 21.07 O ANISOU 4092 O HOH G 799 2730 2700 2575 89 -814 381 O HETATM 4093 O HOH G 800 -3.158 16.622 55.398 1.00 37.41 O ANISOU 4093 O HOH G 800 4514 3163 6535 990 2308 -1427 O HETATM 4094 O HOH G 801 2.870 1.102 62.698 1.00 40.63 O ANISOU 4094 O HOH G 801 6465 5044 3927 511 -37 -446 O HETATM 4095 O HOH G 802 -7.524 15.330 37.836 1.00 35.07 O ANISOU 4095 O HOH G 802 4328 2884 6112 -716 -952 310 O HETATM 4096 O HOH G 803 13.401 17.798 3.274 1.00 26.05 O ANISOU 4096 O HOH G 803 1773 5180 2942 -34 -802 -516 O HETATM 4097 O HOH G 804 9.353 -4.435 49.610 1.00 23.84 O ANISOU 4097 O HOH G 804 3842 1779 3436 2251 -304 345 O HETATM 4098 O HOH G 805 11.751 9.937 6.729 1.00 35.46 O ANISOU 4098 O HOH G 805 4817 3828 4826 1089 -346 -890 O HETATM 4099 O HOH G 806 11.202 2.889 49.411 1.00 26.02 O ANISOU 4099 O HOH G 806 3379 3101 3405 -149 -1722 -967 O HETATM 4100 O HOH G 807 -19.867 5.809 48.620 1.00 25.17 O ANISOU 4100 O HOH G 807 1151 3306 5106 1326 -604 -532 O HETATM 4101 O HOH G 808 0.492 -6.592 58.127 1.00 24.85 O ANISOU 4101 O HOH G 808 4217 2984 2238 1461 -755 465 O HETATM 4102 O HOH G 809 -1.807 12.735 58.031 1.00 33.33 O ANISOU 4102 O HOH G 809 5866 3978 2819 1272 1578 -636 O HETATM 4103 O HOH G 810 -13.604 -24.296 47.115 1.00 34.05 O ANISOU 4103 O HOH G 810 3005 3607 6323 981 -337 982 O HETATM 4104 O HOH G 811 6.138 8.866 14.601 1.00 29.28 O ANISOU 4104 O HOH G 811 4042 3004 4078 1302 389 718 O HETATM 4105 O HOH G 812 -8.777 -17.288 60.845 1.00 38.41 O ANISOU 4105 O HOH G 812 6878 2585 5131 6 1006 1824 O HETATM 4106 O HOH G 813 10.488 -2.845 51.861 1.00 34.94 O ANISOU 4106 O HOH G 813 4936 3359 4979 2126 -491 49 O HETATM 4107 O HOH G 814 2.505 15.452 44.335 1.00 30.69 O ANISOU 4107 O HOH G 814 2144 5724 3790 -1792 -953 -2492 O HETATM 4108 O HOH G 815 -13.921 1.515 41.760 1.00 28.56 O ANISOU 4108 O HOH G 815 1589 6638 2623 -987 -750 -311 O HETATM 4109 O HOH G 816 -16.072 3.986 56.534 1.00 30.45 O ANISOU 4109 O HOH G 816 1945 5747 3876 -1082 -800 -272 O HETATM 4110 O HOH G 817 -15.379 11.864 46.979 1.00 35.00 O ANISOU 4110 O HOH G 817 5939 3570 3789 -372 -296 -794 O HETATM 4111 O HOH G 818 -10.983 -21.854 43.381 1.00 40.70 O ANISOU 4111 O HOH G 818 7573 2909 4982 1563 528 740 O HETATM 4112 O HOH G 819 14.845 12.860 12.600 1.00 30.49 O ANISOU 4112 O HOH G 819 3902 4007 3673 -328 -926 -1500 O HETATM 4113 O HOH G 820 -16.124 -15.131 47.550 1.00 30.60 O ANISOU 4113 O HOH G 820 2816 5300 3510 -1047 -278 -789 O HETATM 4114 O HOH G 821 12.371 11.111 40.473 1.00 24.81 O ANISOU 4114 O HOH G 821 3157 2908 3361 -1079 1244 129 O HETATM 4115 O HOH G 822 8.364 -12.738 53.779 1.00 26.32 O ANISOU 4115 O HOH G 822 4673 3327 2000 1102 1001 1771 O HETATM 4116 O HOH G 823 -10.364 6.808 35.715 1.00 31.71 O ANISOU 4116 O HOH G 823 4492 3049 4506 931 434 -563 O HETATM 4117 O HOH G 824 -14.620 -14.302 42.907 1.00 28.07 O ANISOU 4117 O HOH G 824 3123 3229 4312 -848 -684 624 O HETATM 4118 O HOH G 825 4.538 4.956 61.561 1.00 36.33 O ANISOU 4118 O HOH G 825 4518 5650 3633 192 -1472 -389 O HETATM 4119 O HOH G 826 -13.973 -8.535 57.139 1.00 35.84 O ANISOU 4119 O HOH G 826 4606 5858 3152 -1096 117 -308 O HETATM 4120 O HOH G 827 4.625 -6.005 57.071 1.00 25.32 O ANISOU 4120 O HOH G 827 2718 3545 3357 752 741 1578 O HETATM 4121 O HOH G 828 -14.266 -13.298 45.561 1.00 31.52 O ANISOU 4121 O HOH G 828 4807 4531 2635 1302 740 551 O HETATM 4122 O HOH G 829 -3.234 -8.677 58.036 1.00 21.71 O ANISOU 4122 O HOH G 829 4015 2151 2080 -774 -42 73 O HETATM 4123 O HOH G 830 -8.004 7.978 35.578 1.00 38.25 O ANISOU 4123 O HOH G 830 6819 5055 2655 1537 -1622 553 O HETATM 4124 O HOH G 831 -8.579 6.249 58.086 1.00 30.15 O ANISOU 4124 O HOH G 831 3698 4912 2843 293 1102 -1113 O HETATM 4125 O HOH G 832 -6.201 7.123 59.035 1.00 35.97 O ANISOU 4125 O HOH G 832 4346 4940 4380 -569 528 -821 O HETATM 4126 O HOH G 833 2.860 12.610 56.282 1.00 28.37 O ANISOU 4126 O HOH G 833 3219 4064 3494 -559 -157 -1698 O HETATM 4127 O HOH G 834 -15.960 -8.646 45.267 1.00 38.39 O ANISOU 4127 O HOH G 834 4604 6312 3670 1297 874 -888 O HETATM 4128 O HOH G 835 1.033 -12.763 56.463 1.00 24.26 O ANISOU 4128 O HOH G 835 3849 2582 2786 -313 -404 -83 O HETATM 4129 O HOH G 836 9.499 3.499 52.804 1.00 29.94 O ANISOU 4129 O HOH G 836 4307 4051 3016 -1362 139 -359 O HETATM 4130 O HOH G 837 12.831 -1.695 43.272 1.00 33.87 O ANISOU 4130 O HOH G 837 3691 4358 4818 359 -479 -123 O HETATM 4131 O HOH G 838 14.454 14.048 18.653 1.00 37.39 O ANISOU 4131 O HOH G 838 4891 3698 5618 1212 -2214 484 O HETATM 4132 O HOH G 839 18.782 11.860 27.753 1.00 33.44 O ANISOU 4132 O HOH G 839 4584 5279 2843 -2482 -13 1498 O HETATM 4133 O HOH G 840 -15.564 -11.948 57.943 1.00 33.51 O ANISOU 4133 O HOH G 840 4436 4718 3575 -1110 544 -690 O HETATM 4134 O HOH G 841 -0.865 -18.796 46.868 1.00 30.48 O ANISOU 4134 O HOH G 841 4967 1882 4729 228 415 933 O HETATM 4135 O HOH G 842 5.889 14.426 50.159 1.00 25.99 O ANISOU 4135 O HOH G 842 1898 3131 4844 536 -600 -2236 O HETATM 4136 O HOH G 843 -4.359 -0.324 61.021 1.00 30.01 O ANISOU 4136 O HOH G 843 5098 4344 1961 -274 164 352 O HETATM 4137 O HOH G 844 6.561 9.768 51.616 1.00 32.34 O ANISOU 4137 O HOH G 844 5419 3004 3862 -965 -1059 -419 O HETATM 4138 O HOH G 845 -3.771 -4.582 59.961 1.00 37.38 O ANISOU 4138 O HOH G 845 4883 4555 4764 722 159 1807 O HETATM 4139 O HOH G 846 19.899 10.065 28.955 1.00 34.39 O ANISOU 4139 O HOH G 846 3036 4985 5045 -1084 989 -159 O HETATM 4140 O HOH G 847 -18.521 0.989 42.473 1.00 31.61 O ANISOU 4140 O HOH G 847 3346 4824 3839 -1283 -803 590 O HETATM 4141 O HOH G 848 15.423 19.438 2.847 1.00 35.54 O ANISOU 4141 O HOH G 848 3588 5531 4383 -1247 204 69 O HETATM 4142 O HOH G 849 7.530 -0.193 55.700 1.00 32.14 O ANISOU 4142 O HOH G 849 5049 3077 4085 886 -1828 317 O HETATM 4143 O HOH G 850 11.945 1.308 46.865 1.00 28.25 O ANISOU 4143 O HOH G 850 3997 3112 3622 197 -1722 -448 O HETATM 4144 O HOH G 851 19.922 22.708 -0.302 1.00 37.96 O ANISOU 4144 O HOH G 851 4684 3331 6407 -1641 1128 88 O HETATM 4145 O HOH G 852 1.271 15.372 55.396 1.00 27.09 O ANISOU 4145 O HOH G 852 3852 3644 2793 297 170 -1188 O HETATM 4146 O HOH G 853 -19.484 4.708 51.058 1.00 31.14 O ANISOU 4146 O HOH G 853 3563 3226 5040 -411 -213 -267 O HETATM 4147 O HOH G 854 14.120 2.656 46.557 1.00 33.35 O ANISOU 4147 O HOH G 854 4454 3432 4784 -1212 -675 1777 O HETATM 4148 O HOH A 901 9.823 -3.362 9.198 1.00 12.37 O ANISOU 4148 O HOH A 901 1690 1267 1743 -209 -196 -42 O HETATM 4149 O HOH A 902 6.073 2.205 21.867 1.00 10.41 O ANISOU 4149 O HOH A 902 1357 1504 1091 -493 -396 -110 O HETATM 4150 O HOH A 903 15.509 4.679 27.429 1.00 12.77 O ANISOU 4150 O HOH A 903 1809 573 2467 -607 312 300 O HETATM 4151 O HOH A 904 -1.330 7.420 10.489 1.00 11.59 O ANISOU 4151 O HOH A 904 1294 1704 1404 133 206 508 O HETATM 4152 O HOH A 905 -12.933 10.512 0.057 1.00 24.64 O ANISOU 4152 O HOH A 905 4828 1235 3296 408 -374 161 O HETATM 4153 O HOH A 906 -19.413 1.218 31.165 1.00 12.82 O ANISOU 4153 O HOH A 906 637 3491 744 171 188 -364 O HETATM 4154 O HOH A 907 -12.540 12.539 9.282 1.00 16.01 O ANISOU 4154 O HOH A 907 2515 2039 1529 686 188 630 O HETATM 4155 O HOH A 908 -13.521 14.484 15.967 1.00 16.88 O ANISOU 4155 O HOH A 908 2064 1385 2963 431 63 432 O HETATM 4156 O HOH A 909 2.057 -2.421 18.473 1.00 13.43 O ANISOU 4156 O HOH A 909 1019 3209 875 -463 -203 344 O HETATM 4157 O HOH A 910 2.771 10.252 21.522 1.00 20.45 O ANISOU 4157 O HOH A 910 1918 2545 3307 -1531 23 -640 O HETATM 4158 O HOH A 911 2.039 0.610 17.538 1.00 13.97 O ANISOU 4158 O HOH A 911 2741 1739 828 1103 -70 -52 O HETATM 4159 O HOH A 912 8.667 18.955 3.065 1.00 23.88 O ANISOU 4159 O HOH A 912 2800 2825 3448 806 -179 -404 O HETATM 4160 O HOH A 913 5.089 -9.833 16.486 1.00 15.10 O ANISOU 4160 O HOH A 913 2754 1685 1295 281 174 -109 O HETATM 4161 O HOH A 914 10.096 -6.070 19.894 1.00 15.73 O ANISOU 4161 O HOH A 914 798 2347 2829 604 371 482 O HETATM 4162 O HOH A 915 4.064 -3.616 15.992 1.00 15.95 O ANISOU 4162 O HOH A 915 1709 2912 1438 -135 -245 467 O HETATM 4163 O HOH A 916 -2.336 -11.459 27.597 1.00 15.53 O ANISOU 4163 O HOH A 916 1803 2888 1208 -633 919 150 O HETATM 4164 O HOH A 917 17.601 -3.810 1.325 1.00 19.58 O ANISOU 4164 O HOH A 917 1133 3121 3186 598 -78 152 O HETATM 4165 O HOH A 918 5.552 -2.340 17.988 1.00 12.70 O ANISOU 4165 O HOH A 918 1500 1476 1849 526 -354 -1373 O HETATM 4166 O HOH A 919 -1.391 -2.183 6.271 1.00 21.45 O ANISOU 4166 O HOH A 919 3572 1268 3310 172 372 15 O HETATM 4167 O HOH A 920 -1.377 3.745 27.695 1.00 9.27 O ANISOU 4167 O HOH A 920 953 1294 1274 615 -225 -99 O HETATM 4168 O HOH A 921 11.180 -7.248 1.342 1.00 18.70 O ANISOU 4168 O HOH A 921 3553 1453 2096 336 270 -768 O HETATM 4169 O HOH A 922 -16.854 1.685 4.859 1.00 17.17 O ANISOU 4169 O HOH A 922 1524 2627 2373 223 -187 -528 O HETATM 4170 O HOH A 923 -10.634 1.001 22.764 1.00 27.98 O ANISOU 4170 O HOH A 923 2972 4551 3106 -1535 -162 2460 O HETATM 4171 O HOH A 924 6.767 -12.041 14.588 1.00 16.03 O ANISOU 4171 O HOH A 924 1847 2134 2108 342 796 -288 O HETATM 4172 O HOH A 925 6.836 -14.870 9.907 1.00 19.82 O ANISOU 4172 O HOH A 925 3224 1942 2364 -1462 -444 -500 O HETATM 4173 O HOH A 926 -11.777 -5.851 35.948 1.00 21.03 O ANISOU 4173 O HOH A 926 2849 2635 2505 1267 732 -119 O HETATM 4174 O HOH A 927 2.503 2.767 21.760 1.00 11.47 O ANISOU 4174 O HOH A 927 890 1897 1571 209 -261 798 O HETATM 4175 O HOH A 928 -4.388 3.134 0.729 1.00 14.17 O ANISOU 4175 O HOH A 928 2779 1358 1246 911 659 250 O HETATM 4176 O HOH A 929 -4.567 9.926 -7.879 1.00 21.16 O ANISOU 4176 O HOH A 929 2620 3548 1871 -51 1173 7 O HETATM 4177 O HOH A 930 -1.776 4.401 25.172 1.00 15.33 O ANISOU 4177 O HOH A 930 1551 2564 1708 -307 14 584 O HETATM 4178 O HOH A 931 -11.730 23.673 1.276 1.00 16.73 O ANISOU 4178 O HOH A 931 2516 1946 1892 -610 -710 -798 O HETATM 4179 O HOH A 932 -15.862 19.401 0.433 1.00 11.75 O ANISOU 4179 O HOH A 932 717 1933 1814 134 27 -223 O HETATM 4180 O HOH A 933 -23.400 9.162 19.571 1.00 14.72 O ANISOU 4180 O HOH A 933 1299 2130 2163 1094 254 986 O HETATM 4181 O HOH A 934 -12.650 -11.412 38.816 1.00 14.94 O ANISOU 4181 O HOH A 934 2294 1051 2331 -505 210 0 O HETATM 4182 O HOH A 935 -27.024 2.639 20.800 1.00 25.34 O ANISOU 4182 O HOH A 935 3019 3622 2988 426 -1504 -37 O HETATM 4183 O HOH A 936 23.462 -16.102 26.695 1.00 32.22 O ANISOU 4183 O HOH A 936 956 4142 7143 1088 1522 1443 O HETATM 4184 O HOH A 937 -0.809 -4.486 19.822 1.00 17.44 O ANISOU 4184 O HOH A 937 1847 3698 1079 258 -318 -22 O HETATM 4185 O HOH A 938 13.864 -6.786 5.455 1.00 23.41 O ANISOU 4185 O HOH A 938 4418 3602 872 1017 -231 -3 O HETATM 4186 O HOH A 939 2.124 25.159 -5.564 1.00 25.05 O ANISOU 4186 O HOH A 939 5180 2232 2104 1211 -409 1465 O HETATM 4187 O HOH A 940 -23.017 -3.972 23.952 1.00 26.03 O ANISOU 4187 O HOH A 940 4065 2882 2941 1943 -1471 -149 O HETATM 4188 O HOH A 941 -10.492 14.071 20.185 1.00 18.40 O ANISOU 4188 O HOH A 941 2390 1329 3272 -746 398 154 O HETATM 4189 O HOH A 942 -24.414 4.343 24.423 1.00 16.62 O ANISOU 4189 O HOH A 942 3346 1814 1155 -109 -463 343 O HETATM 4190 O HOH A 943 3.360 -3.533 7.281 1.00 16.04 O ANISOU 4190 O HOH A 943 3418 1151 1526 -242 428 126 O HETATM 4191 O HOH A 944 -21.377 4.234 15.363 1.00 12.93 O ANISOU 4191 O HOH A 944 748 2233 1930 -308 -355 88 O HETATM 4192 O HOH A 945 21.662 -11.032 9.303 1.00 24.38 O ANISOU 4192 O HOH A 945 1479 4731 3051 351 259 -1062 O HETATM 4193 O HOH A 946 -18.386 -0.054 10.378 1.00 38.10 O ANISOU 4193 O HOH A 946 4886 7337 2252 627 -1405 -655 O HETATM 4194 O HOH A 947 11.102 -3.027 14.200 1.00 23.91 O ANISOU 4194 O HOH A 947 3498 3096 2488 368 -431 295 O HETATM 4195 O HOH A 948 7.706 -15.654 33.374 1.00 20.80 O ANISOU 4195 O HOH A 948 2832 3940 1128 399 702 772 O HETATM 4196 O HOH A 949 6.209 5.400 17.818 1.00 20.63 O ANISOU 4196 O HOH A 949 2905 2705 2228 -1060 375 -561 O HETATM 4197 O HOH A 950 5.411 -18.281 11.192 1.00 16.08 O ANISOU 4197 O HOH A 950 2292 2344 1470 201 144 -1138 O HETATM 4198 O HOH A 951 -14.118 9.870 26.634 1.00 18.64 O ANISOU 4198 O HOH A 951 776 1517 4788 572 604 -70 O HETATM 4199 O HOH A 952 15.774 -14.336 5.957 1.00 26.85 O ANISOU 4199 O HOH A 952 4580 2998 2622 -141 314 -756 O HETATM 4200 O HOH A 953 9.849 -8.832 5.212 1.00 23.65 O ANISOU 4200 O HOH A 953 3720 2955 2311 -200 106 699 O HETATM 4201 O HOH A 954 -19.469 11.228 10.473 1.00 19.56 O ANISOU 4201 O HOH A 954 1145 3183 3101 -85 -315 1531 O HETATM 4202 O HOH A 955 -10.980 20.981 -0.082 1.00 17.16 O ANISOU 4202 O HOH A 955 1747 2272 2499 450 61 1673 O HETATM 4203 O HOH A 956 17.096 -2.781 34.681 1.00 24.03 O ANISOU 4203 O HOH A 956 3382 4190 1556 -862 -584 -824 O HETATM 4204 O HOH A 957 6.091 -3.113 6.828 1.00 19.68 O ANISOU 4204 O HOH A 957 2964 1854 2657 1368 587 1342 O HETATM 4205 O HOH A 958 21.724 -18.083 33.231 1.00 17.54 O ANISOU 4205 O HOH A 958 2288 1655 2719 480 -876 48 O HETATM 4206 O HOH A 959 -4.359 -14.552 27.449 1.00 17.94 O ANISOU 4206 O HOH A 959 1544 2638 2632 432 -657 579 O HETATM 4207 O HOH A 960 -25.576 -3.738 22.016 1.00 32.22 O ANISOU 4207 O HOH A 960 1877 7837 2524 -1675 404 -1734 O HETATM 4208 O HOH A 961 19.890 9.994 0.282 1.00 21.35 O ANISOU 4208 O HOH A 961 2301 2663 3146 -333 1469 -626 O HETATM 4209 O HOH A 962 -4.045 14.307 -11.667 1.00 14.72 O ANISOU 4209 O HOH A 962 1301 2288 2001 -546 -746 718 O HETATM 4210 O HOH A 963 -18.981 -9.648 17.737 1.00 16.58 O ANISOU 4210 O HOH A 963 2733 957 2610 -73 -356 -87 O HETATM 4211 O HOH A 964 -10.287 13.606 -4.780 1.00 22.20 O ANISOU 4211 O HOH A 964 2898 3597 1939 -755 343 1065 O HETATM 4212 O HOH A 965 9.402 3.598 8.474 1.00 25.48 O ANISOU 4212 O HOH A 965 3171 3745 2764 -617 -210 1456 O HETATM 4213 O HOH A 966 13.379 -15.017 6.982 1.00 20.82 O ANISOU 4213 O HOH A 966 3053 1302 3553 -737 155 409 O HETATM 4214 O HOH A 967 -20.192 11.386 22.249 1.00 31.41 O ANISOU 4214 O HOH A 967 4495 3515 3922 1475 628 -98 O HETATM 4215 O HOH A 968 2.159 -10.285 27.409 1.00 20.84 O ANISOU 4215 O HOH A 968 3276 2199 2443 -664 -1295 1152 O HETATM 4216 O HOH A 969 24.002 1.065 9.035 1.00 24.70 O ANISOU 4216 O HOH A 969 3594 4503 1288 -738 -1 -1316 O HETATM 4217 O HOH A 970 4.696 0.069 18.939 1.00 14.03 O ANISOU 4217 O HOH A 970 2021 1840 1468 -336 -291 -129 O HETATM 4218 O HOH A 971 -17.563 18.159 12.040 1.00 25.02 O ANISOU 4218 O HOH A 971 2268 2750 4488 -791 -469 22 O HETATM 4219 O HOH A 972 1.587 10.983 -7.516 1.00 22.94 O ANISOU 4219 O HOH A 972 3115 4099 1499 -1371 -73 -10 O HETATM 4220 O HOH A 973 -17.404 24.432 -3.397 1.00 15.28 O ANISOU 4220 O HOH A 973 927 3287 1589 -230 644 778 O HETATM 4221 O HOH A 974 8.159 -5.782 3.831 1.00 20.04 O ANISOU 4221 O HOH A 974 2168 2571 2874 -294 273 -1170 O HETATM 4222 O HOH A 975 -4.719 -11.891 37.191 1.00 15.05 O ANISOU 4222 O HOH A 975 2531 1058 2129 615 1317 46 O HETATM 4223 O HOH A 976 8.159 -8.076 17.352 1.00 23.22 O ANISOU 4223 O HOH A 976 2984 3487 2349 -242 -127 -1158 O HETATM 4224 O HOH A 977 -9.362 -1.309 34.623 1.00 16.20 O ANISOU 4224 O HOH A 977 2665 1576 1912 -850 316 -45 O HETATM 4225 O HOH A 978 12.605 -26.376 23.292 1.00 25.58 O ANISOU 4225 O HOH A 978 3318 2175 4223 837 391 -826 O HETATM 4226 O HOH A 979 26.429 -9.333 19.731 1.00 21.71 O ANISOU 4226 O HOH A 979 1567 4669 2011 -1419 252 403 O HETATM 4227 O HOH A 980 5.225 23.642 5.611 1.00 26.87 O ANISOU 4227 O HOH A 980 2973 3169 4068 -2132 -114 -1502 O HETATM 4228 O HOH A 981 -7.393 10.680 27.503 1.00 25.88 O ANISOU 4228 O HOH A 981 5059 1883 2890 -364 1077 -1060 O HETATM 4229 O HOH A 982 -1.266 26.845 6.594 1.00 23.82 O ANISOU 4229 O HOH A 982 4028 3838 1184 -2623 516 -599 O HETATM 4230 O HOH A 983 -7.586 -14.216 29.128 1.00 21.49 O ANISOU 4230 O HOH A 983 3145 2325 2695 109 201 841 O HETATM 4231 O HOH A 984 17.351 4.805 -4.797 1.00 26.25 O ANISOU 4231 O HOH A 984 3322 3203 3449 -853 -1750 108 O HETATM 4232 O HOH A 985 16.555 -12.947 3.777 1.00 22.39 O ANISOU 4232 O HOH A 985 1736 4064 2706 -483 -869 -957 O HETATM 4233 O HOH A 986 -2.772 -12.136 13.301 1.00 30.45 O ANISOU 4233 O HOH A 986 4697 4169 2700 422 468 -359 O HETATM 4234 O HOH A 987 3.656 -21.142 14.274 1.00 15.59 O ANISOU 4234 O HOH A 987 1099 1250 3574 -807 -310 786 O HETATM 4235 O HOH A 988 -17.863 12.851 21.202 1.00 19.20 O ANISOU 4235 O HOH A 988 1101 1568 4624 -80 -712 715 O HETATM 4236 O HOH A 989 -18.628 6.552 10.878 1.00 28.47 O ANISOU 4236 O HOH A 989 2097 2476 6243 -1682 1300 390 O HETATM 4237 O HOH A 990 5.476 16.726 -5.331 1.00 41.85 O ANISOU 4237 O HOH A 990 5937 4993 4969 -532 -478 -2677 O HETATM 4238 O HOH A 991 3.397 5.855 6.359 1.00 21.54 O ANISOU 4238 O HOH A 991 1693 2915 3576 -32 321 490 O HETATM 4239 O HOH A 992 -0.229 -1.734 15.858 1.00 19.25 O ANISOU 4239 O HOH A 992 2183 2206 2922 -977 -434 334 O HETATM 4240 O HOH A 993 -18.296 -5.247 33.470 1.00 34.10 O ANISOU 4240 O HOH A 993 5591 3990 3374 771 603 1399 O HETATM 4241 O HOH A 994 -1.260 6.101 -3.454 1.00 20.06 O ANISOU 4241 O HOH A 994 2824 2890 1907 1533 -641 31 O HETATM 4242 O HOH A 995 -14.463 21.339 -1.185 1.00 21.43 O ANISOU 4242 O HOH A 995 4187 1171 2783 -554 1401 -246 O HETATM 4243 O HOH A 996 27.009 -2.553 27.803 1.00 18.22 O ANISOU 4243 O HOH A 996 1775 3200 1946 94 406 -296 O HETATM 4244 O HOH A 997 -20.960 -5.840 32.005 1.00 22.70 O ANISOU 4244 O HOH A 997 2564 2747 3312 -504 2140 -875 O HETATM 4245 O HOH A 998 13.321 -2.906 41.281 1.00 27.52 O ANISOU 4245 O HOH A 998 2577 3908 3969 -186 -1425 -307 O HETATM 4246 O HOH A 999 3.826 2.702 19.089 1.00 20.38 O ANISOU 4246 O HOH A 999 3327 2277 2136 -785 349 -181 O HETATM 4247 O HOH A1000 -1.501 14.884 -10.917 1.00 21.66 O ANISOU 4247 O HOH A1000 2736 4064 1429 -844 -494 -377 O HETATM 4248 O HOH A1001 12.053 -8.236 3.688 1.00 20.29 O ANISOU 4248 O HOH A1001 2599 3173 1938 -485 913 447 O HETATM 4249 O HOH A1002 25.350 -13.330 28.805 1.00 24.50 O ANISOU 4249 O HOH A1002 1782 3317 4209 1125 701 527 O HETATM 4250 O HOH A1003 -7.992 12.707 20.164 1.00 21.64 O ANISOU 4250 O HOH A1003 2035 3429 2757 -946 -1558 726 O HETATM 4251 O HOH A1004 11.443 -27.937 27.040 1.00 24.63 O ANISOU 4251 O HOH A1004 4344 2941 2071 -1195 -160 83 O HETATM 4252 O HOH A1005 13.408 -5.966 37.493 1.00 35.84 O ANISOU 4252 O HOH A1005 2516 5479 5620 -807 -311 -1308 O HETATM 4253 O HOH A1006 -21.532 23.173 1.331 1.00 27.65 O ANISOU 4253 O HOH A1006 1969 5132 3402 939 531 1909 O HETATM 4254 O HOH A1007 -2.394 8.163 -7.658 1.00 23.22 O ANISOU 4254 O HOH A1007 4266 2320 2237 392 576 454 O HETATM 4255 O HOH A1008 29.690 -7.626 22.313 1.00 25.26 O ANISOU 4255 O HOH A1008 1657 3403 4535 696 -349 -1224 O HETATM 4256 O HOH A1009 7.603 21.775 5.378 1.00 27.42 O ANISOU 4256 O HOH A1009 4591 3657 2168 -1162 -1423 -331 O HETATM 4257 O HOH A1010 1.752 -20.405 26.040 1.00 25.29 O ANISOU 4257 O HOH A1010 2670 3945 2994 -1091 -549 -192 O HETATM 4258 O HOH A1011 -23.814 5.836 26.527 1.00 17.10 O ANISOU 4258 O HOH A1011 1205 1915 3374 676 346 624 O HETATM 4259 O HOH A1012 0.685 -15.332 33.906 1.00 33.62 O ANISOU 4259 O HOH A1012 4986 2840 4947 1281 -842 324 O HETATM 4260 O HOH A1013 -21.157 -7.633 17.144 1.00 29.18 O ANISOU 4260 O HOH A1013 2477 4578 4033 -1047 -892 -1048 O HETATM 4261 O HOH A1014 7.533 -17.267 35.271 1.00 31.19 O ANISOU 4261 O HOH A1014 3588 4386 3876 39 2088 128 O HETATM 4262 O HOH A1015 6.678 8.856 12.084 1.00 29.90 O ANISOU 4262 O HOH A1015 3437 4284 3640 559 671 632 O HETATM 4263 O HOH A1016 7.656 -10.484 16.912 1.00 29.30 O ANISOU 4263 O HOH A1016 3158 5871 2104 -1121 -341 422 O HETATM 4264 O HOH A1017 15.017 -0.388 36.025 1.00 31.41 O ANISOU 4264 O HOH A1017 2820 3694 5419 -1045 -1889 1492 O HETATM 4265 O HOH A1018 -9.157 -15.858 27.804 1.00 19.19 O ANISOU 4265 O HOH A1018 2000 3122 2169 -320 253 998 O HETATM 4266 O HOH A1019 -21.844 7.914 26.250 1.00 25.03 O ANISOU 4266 O HOH A1019 2340 3384 3783 184 701 -820 O HETATM 4267 O HOH A1020 0.322 12.088 30.203 1.00 36.38 O ANISOU 4267 O HOH A1020 5977 5232 2613 547 -1813 579 O HETATM 4268 O HOH A1021 4.493 -23.849 14.890 1.00 29.00 O ANISOU 4268 O HOH A1021 3934 3498 3585 -761 -3 -527 O HETATM 4269 O HOH A1022 -2.326 14.136 12.527 1.00 23.60 O ANISOU 4269 O HOH A1022 2110 2897 3958 -201 -277 -1067 O HETATM 4270 O HOH A1023 1.226 -20.536 15.300 1.00 24.45 O ANISOU 4270 O HOH A1023 2574 3784 2930 -1574 -51 298 O HETATM 4271 O HOH A1024 -21.551 -4.819 14.429 1.00 31.46 O ANISOU 4271 O HOH A1024 3784 4117 4052 610 150 454 O HETATM 4272 O HOH A1025 -8.346 -12.804 31.662 1.00 21.58 O ANISOU 4272 O HOH A1025 2492 2545 3162 -183 -488 -1176 O HETATM 4273 O HOH A1026 31.782 -10.730 24.073 1.00 29.30 O ANISOU 4273 O HOH A1026 1860 5683 3587 -1130 1499 -621 O HETATM 4274 O HOH A1027 21.828 -15.466 32.860 1.00 25.02 O ANISOU 4274 O HOH A1027 4322 3139 2045 340 -1424 -181 O HETATM 4275 O HOH A1028 9.870 18.449 -3.720 1.00 25.35 O ANISOU 4275 O HOH A1028 4133 3284 2213 658 101 904 O HETATM 4276 O HOH A1029 -0.590 7.926 -5.568 1.00 20.46 O ANISOU 4276 O HOH A1029 2685 2338 2748 1187 465 -10 O HETATM 4277 O HOH A1030 28.687 -1.450 22.190 1.00 24.00 O ANISOU 4277 O HOH A1030 3619 3320 2177 -1771 583 -1101 O HETATM 4278 O HOH A1031 -22.290 20.854 0.326 1.00 31.18 O ANISOU 4278 O HOH A1031 4581 3969 3294 348 -1299 1141 O HETATM 4279 O HOH A1032 -21.038 3.390 11.131 1.00 28.88 O ANISOU 4279 O HOH A1032 3700 4038 3234 -149 -1173 973 O HETATM 4280 O HOH A1033 -19.761 -5.384 11.738 1.00 30.28 O ANISOU 4280 O HOH A1033 4783 4401 2320 -91 -1518 1684 O HETATM 4281 O HOH A1034 0.088 -8.165 13.803 1.00 27.47 O ANISOU 4281 O HOH A1034 4739 3065 2631 297 442 -508 O HETATM 4282 O HOH A1035 9.379 6.422 8.087 1.00 26.99 O ANISOU 4282 O HOH A1035 4438 2409 3405 -386 -743 -1248 O HETATM 4283 O HOH A1036 -2.766 16.935 12.368 1.00 28.15 O ANISOU 4283 O HOH A1036 3250 5037 2407 -2119 -714 165 O HETATM 4284 O HOH A1037 7.088 13.716 -7.686 1.00 37.26 O ANISOU 4284 O HOH A1037 4396 5580 4180 -805 487 748 O HETATM 4285 O HOH A1038 -4.834 19.368 12.093 1.00 25.44 O ANISOU 4285 O HOH A1038 3902 1875 3886 666 -179 -411 O HETATM 4286 O HOH A1039 -20.442 11.188 24.770 1.00 26.08 O ANISOU 4286 O HOH A1039 2971 4423 2512 6 425 15 O HETATM 4287 O HOH A1040 20.474 -9.924 6.141 1.00 31.24 O ANISOU 4287 O HOH A1040 4468 3389 4011 813 -437 1196 O HETATM 4288 O HOH A1041 0.175 -11.044 28.873 1.00 26.40 O ANISOU 4288 O HOH A1041 3987 3172 2870 -850 -343 1778 O HETATM 4289 O HOH A1042 -10.782 -9.136 13.084 1.00 35.07 O ANISOU 4289 O HOH A1042 4478 6737 2108 -759 706 311 O HETATM 4290 O HOH A1043 9.796 16.209 -6.655 1.00 30.75 O ANISOU 4290 O HOH A1043 4801 2841 4039 -32 490 457 O HETATM 4291 O HOH A1044 -20.824 7.754 28.611 1.00 20.73 O ANISOU 4291 O HOH A1044 3234 2079 2563 -82 664 651 O HETATM 4292 O HOH A1045 -7.812 7.807 32.697 1.00 32.27 O ANISOU 4292 O HOH A1045 5079 3198 3982 -723 383 -850 O HETATM 4293 O HOH A1046 -8.511 15.622 -3.698 1.00 22.16 O ANISOU 4293 O HOH A1046 2567 3208 2644 655 -1337 329 O HETATM 4294 O HOH A1047 -6.675 28.489 0.721 1.00 32.20 O ANISOU 4294 O HOH A1047 5125 3601 3508 -1242 -87 44 O HETATM 4295 O HOH A1048 3.563 18.223 -6.927 1.00 27.07 O ANISOU 4295 O HOH A1048 3477 2684 4122 323 324 879 O HETATM 4296 O HOH A1049 -0.974 -4.042 17.049 1.00 21.00 O ANISOU 4296 O HOH A1049 3110 2412 2454 338 988 -174 O HETATM 4297 O HOH A1050 -5.022 4.396 -1.646 1.00 20.92 O ANISOU 4297 O HOH A1050 3706 2583 1657 -151 -504 -460 O HETATM 4298 O HOH A1051 13.180 1.516 -1.712 1.00 25.74 O ANISOU 4298 O HOH A1051 4766 2227 2787 -733 130 -727 O HETATM 4299 O HOH A1052 5.821 -6.296 16.065 1.00 21.27 O ANISOU 4299 O HOH A1052 4586 1516 1980 57 912 -886 O HETATM 4300 O HOH A1053 -4.852 11.460 -10.207 1.00 32.01 O ANISOU 4300 O HOH A1053 4412 3727 4023 412 820 325 O HETATM 4301 O HOH A1054 -25.667 8.308 20.407 1.00 26.96 O ANISOU 4301 O HOH A1054 2990 3137 4116 974 1263 348 O HETATM 4302 O HOH A1055 6.337 -4.003 4.105 1.00 27.96 O ANISOU 4302 O HOH A1055 2156 4601 3865 202 872 475 O HETATM 4303 O HOH A1056 1.879 8.644 -6.403 1.00 29.86 O ANISOU 4303 O HOH A1056 2677 4544 4123 1333 72 1638 O HETATM 4304 O HOH A1057 7.297 -12.806 43.481 1.00 33.45 O ANISOU 4304 O HOH A1057 3707 3208 5791 317 -419 -669 O HETATM 4305 O HOH A1058 -11.654 17.372 14.799 1.00 31.27 O ANISOU 4305 O HOH A1058 6774 2632 2474 38 1048 147 O HETATM 4306 O HOH A1059 -8.888 -3.278 36.597 1.00 27.42 O ANISOU 4306 O HOH A1059 2920 4306 3189 1313 -435 -117 O HETATM 4307 O HOH A1060 9.419 -15.201 5.613 1.00 38.18 O ANISOU 4307 O HOH A1060 4677 3334 6493 336 195 -1342 O HETATM 4308 O HOH A1061 -16.111 -1.102 4.165 1.00 26.89 O ANISOU 4308 O HOH A1061 4547 1860 3807 51 1165 835 O HETATM 4309 O HOH A1062 -22.762 11.311 20.985 1.00 33.23 O ANISOU 4309 O HOH A1062 3755 4366 4505 970 -645 -457 O HETATM 4310 O HOH A1063 26.948 -10.679 21.998 1.00 26.69 O ANISOU 4310 O HOH A1063 3180 3068 3893 -166 1125 -149 O HETATM 4311 O HOH A1064 -8.094 16.434 19.427 1.00 24.19 O ANISOU 4311 O HOH A1064 4308 3592 1289 -564 -120 22 O HETATM 4312 O HOH A1065 4.373 -12.375 28.081 1.00 24.70 O ANISOU 4312 O HOH A1065 1755 3219 4409 -1310 103 -134 O HETATM 4313 O HOH A1066 4.105 -12.368 25.281 1.00 30.16 O ANISOU 4313 O HOH A1066 4831 2516 4112 601 1018 453 O HETATM 4314 O HOH A1067 -1.672 -10.266 14.666 1.00 37.26 O ANISOU 4314 O HOH A1067 5472 2218 6464 -690 913 1359 O HETATM 4315 O HOH A1068 -16.920 31.013 1.149 1.00 21.50 O ANISOU 4315 O HOH A1068 1307 4195 2667 133 -315 -205 O HETATM 4316 O HOH A1069 -26.313 -0.298 29.949 1.00 34.31 O ANISOU 4316 O HOH A1069 2742 4284 6009 -662 62 548 O HETATM 4317 O HOH A1070 -0.086 -12.661 9.156 1.00 30.97 O ANISOU 4317 O HOH A1070 4532 4058 3174 425 351 -190 O HETATM 4318 O HOH A1071 18.705 -13.758 3.595 1.00 27.28 O ANISOU 4318 O HOH A1071 3763 3265 3338 -639 -53 -317 O HETATM 4319 O HOH A1072 -2.691 20.808 12.093 1.00 31.62 O ANISOU 4319 O HOH A1072 2884 4178 4949 -346 -562 1760 O HETATM 4320 O HOH A1073 -6.509 19.863 14.004 1.00 28.72 O ANISOU 4320 O HOH A1073 4661 2996 3254 814 -132 1049 O HETATM 4321 O HOH A1074 -11.065 -14.011 31.500 1.00 30.47 O ANISOU 4321 O HOH A1074 4139 3325 4111 314 619 -135 O HETATM 4322 O HOH A1075 -7.144 3.371 -2.923 1.00 26.65 O ANISOU 4322 O HOH A1075 4487 4751 885 -92 859 36 O HETATM 4323 O HOH A1076 14.164 -3.226 -2.097 1.00 30.10 O ANISOU 4323 O HOH A1076 3656 3613 4167 -1371 -594 634 O HETATM 4324 O HOH A1077 0.609 5.665 28.022 1.00 33.23 O ANISOU 4324 O HOH A1077 4677 2807 5140 358 -1598 235 O HETATM 4325 O HOH A1078 16.725 10.968 2.963 1.00 26.93 O ANISOU 4325 O HOH A1078 2308 3046 4878 548 489 712 O HETATM 4326 O HOH A1079 11.418 17.565 -5.127 1.00 25.82 O ANISOU 4326 O HOH A1079 3034 3537 3237 -552 664 -1141 O HETATM 4327 O HOH A1080 6.561 8.595 30.492 1.00 20.80 O ANISOU 4327 O HOH A1080 2508 1724 3671 181 -776 -552 O HETATM 4328 O HOH A1081 -12.115 24.937 3.574 1.00 19.56 O ANISOU 4328 O HOH A1081 1667 2327 3434 -504 -571 777 O HETATM 4329 O HOH A1082 10.806 -21.411 15.244 1.00 26.57 O ANISOU 4329 O HOH A1082 4129 3000 2966 1303 -688 -418 O HETATM 4330 O HOH A1083 6.887 3.353 7.514 1.00 31.21 O ANISOU 4330 O HOH A1083 3509 5951 2397 323 239 1587 O HETATM 4331 O HOH A1084 -15.652 -6.497 9.011 1.00 35.15 O ANISOU 4331 O HOH A1084 6226 3362 3766 43 -626 833 O HETATM 4332 O HOH A1085 -30.114 0.390 27.846 1.00 27.80 O ANISOU 4332 O HOH A1085 3356 4455 2750 419 200 -1375 O HETATM 4333 O HOH A1086 14.369 -1.378 38.742 1.00 25.49 O ANISOU 4333 O HOH A1086 2766 3569 3349 -923 -192 247 O HETATM 4334 O HOH A1087 -15.088 11.949 -0.023 1.00 35.65 O ANISOU 4334 O HOH A1087 5675 3687 4181 658 481 193 O HETATM 4335 O HOH A1088 5.519 7.542 -4.777 1.00 41.56 O ANISOU 4335 O HOH A1088 3138 5354 7296 -438 828 -294 O HETATM 4336 O HOH A1089 -2.251 -13.712 26.194 1.00 38.79 O ANISOU 4336 O HOH A1089 4086 5311 5339 -630 1308 -289 O HETATM 4337 O HOH A1090 1.903 11.205 -10.217 1.00 29.11 O ANISOU 4337 O HOH A1090 3088 3670 4300 -587 -612 -1265 O HETATM 4338 O HOH A1091 7.461 13.448 9.890 1.00 34.00 O ANISOU 4338 O HOH A1091 5103 3808 4006 604 -1387 534 O HETATM 4339 O HOH A1092 31.695 -4.845 27.995 1.00 26.60 O ANISOU 4339 O HOH A1092 3227 3772 3107 640 103 -216 O HETATM 4340 O HOH A1093 -22.071 -13.550 27.753 1.00 26.22 O ANISOU 4340 O HOH A1093 2209 4047 3704 -676 -202 -1371 O HETATM 4341 O HOH A1094 14.857 -7.652 36.670 1.00 30.84 O ANISOU 4341 O HOH A1094 5254 2245 4216 -1690 352 -301 O HETATM 4342 O HOH A1095 16.723 3.714 33.783 1.00 23.77 O ANISOU 4342 O HOH A1095 1745 4472 2812 -530 -868 541 O HETATM 4343 O HOH A1096 -0.191 12.197 -11.700 1.00 25.83 O ANISOU 4343 O HOH A1096 3634 4394 1786 780 433 167 O HETATM 4344 O HOH A1097 17.406 -13.241 35.630 1.00 37.37 O ANISOU 4344 O HOH A1097 4589 5343 4266 1238 -1864 -533 O HETATM 4345 O HOH A1098 -5.282 -6.686 3.863 1.00 29.10 O ANISOU 4345 O HOH A1098 5649 1614 3791 -810 2149 -415 O HETATM 4346 O HOH A1099 -26.238 -1.090 18.094 1.00 30.35 O ANISOU 4346 O HOH A1099 4098 3820 3611 -1181 -568 1288 O HETATM 4347 O HOH A1100 24.185 -0.607 11.476 1.00 34.50 O ANISOU 4347 O HOH A1100 1635 6637 4835 17 806 485 O HETATM 4348 O HOH A1101 7.081 6.464 10.474 1.00 31.05 O ANISOU 4348 O HOH A1101 4619 5023 2153 2197 -697 847 O HETATM 4349 O HOH A1102 -27.774 4.901 18.198 1.00 32.82 O ANISOU 4349 O HOH A1102 4023 3962 4484 -804 -1480 -289 O HETATM 4350 O HOH A1103 18.136 -19.846 35.702 1.00 32.57 O ANISOU 4350 O HOH A1103 6263 2618 3493 -571 55 1799 O HETATM 4351 O HOH A1104 11.470 -12.098 3.640 1.00 31.24 O ANISOU 4351 O HOH A1104 4903 5108 1857 1564 811 -1786 O HETATM 4352 O HOH A1105 -17.489 22.308 10.283 1.00 33.41 O ANISOU 4352 O HOH A1105 3938 4760 3993 -406 573 347 O HETATM 4353 O HOH A1106 -15.081 -6.694 34.693 1.00 42.88 O ANISOU 4353 O HOH A1106 5969 5925 4398 -134 -1323 177 O HETATM 4354 O HOH A1107 -0.149 -18.455 12.891 1.00 38.09 O ANISOU 4354 O HOH A1107 3860 3934 6676 -584 -828 -1187 O HETATM 4355 O HOH A1108 10.150 -4.848 2.063 1.00 23.26 O ANISOU 4355 O HOH A1108 2846 2599 3393 -426 -1171 -488 O HETATM 4356 O HOH A1109 -9.876 10.410 28.928 1.00 35.43 O ANISOU 4356 O HOH A1109 6703 4470 2286 51 826 -671 O HETATM 4357 O HOH A1110 1.101 -12.791 20.916 1.00 44.29 O ANISOU 4357 O HOH A1110 5131 5464 6232 244 -830 18 O HETATM 4358 O HOH A1111 -13.677 16.645 17.527 1.00 26.58 O ANISOU 4358 O HOH A1111 3965 3417 2717 282 -422 84 O HETATM 4359 O HOH A1112 10.859 1.515 -0.216 1.00 28.16 O ANISOU 4359 O HOH A1112 2329 4752 3616 101 -402 25 O HETATM 4360 O HOH A1113 -9.394 4.676 -2.934 1.00 27.53 O ANISOU 4360 O HOH A1113 4224 4106 2128 -351 54 -151 O HETATM 4361 O HOH A1114 9.717 23.670 5.508 1.00 39.11 O ANISOU 4361 O HOH A1114 4732 4780 5346 599 -419 -1919 O HETATM 4362 O HOH A1115 10.254 -2.480 0.197 1.00 33.76 O ANISOU 4362 O HOH A1115 4729 5262 2835 861 -2387 -48 O HETATM 4363 O HOH A1116 -9.360 18.662 15.409 1.00 39.53 O ANISOU 4363 O HOH A1116 4947 5956 4116 1831 -329 -1544 O HETATM 4364 O HOH A1117 -7.890 13.394 22.780 1.00 31.68 O ANISOU 4364 O HOH A1117 3764 4734 3539 -631 -364 -1144 O HETATM 4365 O HOH A1118 26.570 -11.715 31.348 1.00 36.12 O ANISOU 4365 O HOH A1118 3054 5490 5177 -1480 418 821 O HETATM 4366 O HOH A1119 -15.911 -1.633 -0.295 1.00 31.73 O ANISOU 4366 O HOH A1119 5862 3371 2821 -244 -1121 -1152 O HETATM 4367 O HOH A1120 18.223 9.642 23.621 1.00 32.51 O ANISOU 4367 O HOH A1120 4879 2306 5168 -809 -848 1266 O HETATM 4368 O HOH A1121 -17.776 -14.821 21.643 1.00 40.08 O ANISOU 4368 O HOH A1121 5773 4624 4830 -224 -429 314 O HETATM 4369 O HOH A1122 -14.609 13.790 -2.282 1.00 33.23 O ANISOU 4369 O HOH A1122 3836 5282 3507 1276 -1416 -834 O HETATM 4370 O HOH A1123 -3.269 -13.616 22.918 1.00 33.64 O ANISOU 4370 O HOH A1123 2290 3891 6599 259 524 -228 O HETATM 4371 O HOH A1124 17.880 -11.331 37.167 1.00 36.17 O ANISOU 4371 O HOH A1124 3561 3969 6211 -1796 -482 312 O HETATM 4372 O HOH A1125 -13.965 -13.059 30.765 1.00 33.92 O ANISOU 4372 O HOH A1125 3570 4335 4980 457 739 -280 O HETATM 4373 O HOH A1126 -6.732 8.133 -8.601 1.00 31.32 O ANISOU 4373 O HOH A1126 4023 4205 3671 148 -216 684 O HETATM 4374 O HOH A1127 -5.597 -19.456 22.869 1.00 30.95 O ANISOU 4374 O HOH A1127 4741 5065 1953 916 1165 487 O HETATM 4375 O HOH A1128 -3.158 13.868 21.972 1.00 31.86 O ANISOU 4375 O HOH A1128 4839 2483 4783 1859 -1274 -580 O HETATM 4376 O HOH A1129 1.550 -5.202 16.232 1.00 29.58 O ANISOU 4376 O HOH A1129 3387 4995 2856 -843 -1200 -329 O HETATM 4377 O HOH A1130 -12.251 -12.134 17.321 1.00 26.71 O ANISOU 4377 O HOH A1130 4295 4048 1805 -124 -586 -475 O HETATM 4378 O HOH A1131 16.507 -19.084 37.387 1.00 35.70 O ANISOU 4378 O HOH A1131 3559 4884 5121 190 1405 1292 O HETATM 4379 O HOH A1132 16.916 -6.710 35.338 1.00 32.58 O ANISOU 4379 O HOH A1132 2597 5253 4528 -392 789 508 O HETATM 4380 O HOH A1133 -5.815 13.013 19.171 1.00 33.69 O ANISOU 4380 O HOH A1133 5620 4248 2930 1119 973 503 O HETATM 4381 O HOH A1134 -24.440 11.163 23.751 1.00 37.83 O ANISOU 4381 O HOH A1134 5764 4713 3895 1406 -1102 681 O HETATM 4382 O HOH A1135 -11.572 1.744 20.434 1.00 34.79 O ANISOU 4382 O HOH A1135 3637 5550 4030 -975 -686 -1621 O HETATM 4383 O HOH A1136 7.897 16.560 -3.594 1.00 34.87 O ANISOU 4383 O HOH A1136 4586 2979 5683 1687 1273 101 O HETATM 4384 O HOH A1137 3.054 1.360 0.435 1.00 32.80 O ANISOU 4384 O HOH A1137 3632 4419 4412 331 -57 -132 O HETATM 4385 O HOH A1138 8.681 17.293 13.110 1.00 43.80 O ANISOU 4385 O HOH A1138 3711 5818 7114 370 -1408 -792 O HETATM 4386 O HOH A1139 23.269 -4.255 11.570 1.00 29.55 O ANISOU 4386 O HOH A1139 3609 3795 3822 -2181 -171 -179 O HETATM 4387 O HOH A1140 -20.907 9.627 6.766 1.00 27.47 O ANISOU 4387 O HOH A1140 2104 4878 3454 -154 -841 313 O HETATM 4388 O HOH A1141 -9.586 24.126 -2.442 1.00 28.49 O ANISOU 4388 O HOH A1141 3984 1266 5573 469 1489 -1352 O HETATM 4389 O HOH A1142 21.862 -23.759 23.946 1.00 39.65 O ANISOU 4389 O HOH A1142 3130 4926 7007 885 924 -714 O HETATM 4390 O HOH A1143 9.060 -18.359 12.124 1.00 31.16 O ANISOU 4390 O HOH A1143 2274 4552 5012 -1713 -878 -1264 O HETATM 4391 O HOH A1144 28.356 0.373 20.291 1.00 31.13 O ANISOU 4391 O HOH A1144 1248 4686 5893 -1755 302 -201 O HETATM 4392 O HOH A1145 -25.053 -6.350 18.153 1.00 41.29 O ANISOU 4392 O HOH A1145 6832 4635 4222 -1245 404 189 O HETATM 4393 O HOH A1146 -7.902 21.950 12.601 1.00 42.26 O ANISOU 4393 O HOH A1146 6260 6082 3712 -276 915 -250 O HETATM 4394 O HOH A1147 -32.919 4.615 28.311 1.00 33.25 O ANISOU 4394 O HOH A1147 4976 3453 4202 -951 545 -1427 O HETATM 4395 O HOH A1148 -3.237 -16.341 21.732 1.00 37.11 O ANISOU 4395 O HOH A1148 2824 5043 6233 1366 -419 -59 O HETATM 4396 O HOH A1149 -21.956 -5.483 34.262 1.00 35.14 O ANISOU 4396 O HOH A1149 5472 5680 2197 502 1069 -526 O HETATM 4397 O HOH A1150 -12.324 20.455 -2.333 1.00 29.90 O ANISOU 4397 O HOH A1150 4840 4027 2491 -399 1339 -71 O HETATM 4398 O HOH A1151 1.412 1.261 20.090 1.00 44.89 O ANISOU 4398 O HOH A1151 7106 3464 6486 811 -603 -90 O HETATM 4399 O HOH A1152 -3.306 4.174 -3.547 1.00 26.87 O ANISOU 4399 O HOH A1152 4228 3675 2305 290 -688 186 O HETATM 4400 O HOH A1153 29.345 7.488 18.528 1.00 31.17 O ANISOU 4400 O HOH A1153 2156 4070 5614 2178 -862 143 O HETATM 4401 O HOH A1154 9.164 11.372 33.817 1.00 35.88 O ANISOU 4401 O HOH A1154 4193 3453 5988 230 1790 772 O HETATM 4402 O HOH A1155 -16.992 4.776 0.132 1.00 31.59 O ANISOU 4402 O HOH A1155 4357 3571 4073 -130 -617 -1045 O HETATM 4403 O HOH A1156 -4.033 27.647 2.737 1.00 36.18 O ANISOU 4403 O HOH A1156 4488 3329 5928 163 573 -226 O HETATM 4404 O HOH A1157 -15.093 -12.872 33.195 1.00 41.86 O ANISOU 4404 O HOH A1157 5984 3864 6055 1215 -870 451 O HETATM 4405 O HOH A1158 3.093 -9.407 29.616 1.00 41.87 O ANISOU 4405 O HOH A1158 4889 6238 4781 -1041 1530 118 O HETATM 4406 O HOH A1159 21.315 12.495 3.024 1.00 36.00 O ANISOU 4406 O HOH A1159 4856 3272 5551 -1274 -792 1364 O HETATM 4407 O HOH A1160 1.518 -14.419 22.940 1.00 35.49 O ANISOU 4407 O HOH A1160 4505 3573 5406 2061 -161 -1641 O HETATM 4408 O HOH A1161 -10.305 19.024 -2.365 1.00 42.95 O ANISOU 4408 O HOH A1161 5602 4509 6205 2061 -279 791 O HETATM 4409 O HOH A1162 14.414 -17.602 36.999 1.00 33.99 O ANISOU 4409 O HOH A1162 4627 3599 4685 -765 -870 53 O HETATM 4410 O HOH A1163 -8.653 14.123 -10.659 1.00 31.58 O ANISOU 4410 O HOH A1163 3916 5058 3022 -353 229 502 O HETATM 4411 O HOH A1164 5.138 22.285 -9.799 1.00 41.02 O ANISOU 4411 O HOH A1164 5768 5679 4137 -667 -248 135 O HETATM 4412 O HOH A1165 18.858 -24.942 24.128 1.00 27.51 O ANISOU 4412 O HOH A1165 2449 3457 4544 1111 -83 973 O HETATM 4413 O HOH A1166 -14.634 -7.778 38.174 1.00 27.67 O ANISOU 4413 O HOH A1166 2445 5181 2885 -544 -389 1468 O HETATM 4414 O HOH A1167 -3.465 7.473 30.399 1.00 31.22 O ANISOU 4414 O HOH A1167 4151 2998 4713 -2440 1475 682 O HETATM 4415 O HOH A1168 -13.650 -14.411 34.791 1.00 36.87 O ANISOU 4415 O HOH A1168 4627 3602 5777 569 -143 -327 O HETATM 4416 O HOH A1169 -21.527 16.916 2.989 1.00 32.85 O ANISOU 4416 O HOH A1169 3819 4577 4086 2280 -772 1017 O HETATM 4417 O HOH A1170 -1.089 7.967 30.405 1.00 30.79 O ANISOU 4417 O HOH A1170 4473 4642 2582 595 444 322 O HETATM 4418 O HOH A1171 -10.330 -1.540 20.351 1.00 22.65 O ANISOU 4418 O HOH A1171 2172 3485 2949 176 408 -30 O HETATM 4419 O HOH A1172 24.344 -0.283 32.070 1.00 40.31 O ANISOU 4419 O HOH A1172 4233 5724 5359 315 930 -846 O HETATM 4420 O HOH A1173 -10.617 -16.022 24.670 1.00 32.50 O ANISOU 4420 O HOH A1173 5678 3580 3089 1727 -221 920 O HETATM 4421 O HOH A1174 13.180 -11.107 1.782 1.00 27.26 O ANISOU 4421 O HOH A1174 3541 5076 1737 634 -78 -452 O HETATM 4422 O HOH A1175 3.664 27.197 4.074 1.00 38.69 O ANISOU 4422 O HOH A1175 5050 6234 3415 107 83 -997 O CONECT 311 3963 CONECT 319 3963 CONECT 577 3963 CONECT 578 3963 CONECT 660 3962 CONECT 661 3962 CONECT 701 3962 CONECT 716 3962 CONECT 945 3963 CONECT 2319 3962 CONECT 3962 660 661 701 716 CONECT 3962 2319 4005 4017 4022 CONECT 3963 311 319 577 578 CONECT 3963 945 3997 4023 CONECT 3964 3968 3971 4156 4158 CONECT 3964 4162 4165 4217 CONECT 3965 3966 3967 3968 3972 CONECT 3966 3965 CONECT 3967 3965 CONECT 3968 3964 3965 CONECT 3969 3970 3971 3972 3976 CONECT 3970 3969 CONECT 3971 3964 3969 CONECT 3972 3965 3969 CONECT 3973 3974 3975 3976 3977 CONECT 3974 3973 CONECT 3975 3973 CONECT 3976 3969 3973 CONECT 3977 3973 3978 CONECT 3978 3977 3979 CONECT 3979 3978 3980 3981 CONECT 3980 3979 3985 CONECT 3981 3979 3982 3983 CONECT 3982 3981 CONECT 3983 3981 3984 3985 CONECT 3984 3983 CONECT 3985 3980 3983 3986 CONECT 3986 3985 3987 3995 CONECT 3987 3986 3988 CONECT 3988 3987 3989 CONECT 3989 3988 3990 3995 CONECT 3990 3989 3991 3992 CONECT 3991 3990 CONECT 3992 3990 3993 CONECT 3993 3992 3994 CONECT 3994 3993 3995 CONECT 3995 3986 3989 3994 CONECT 3997 3963 CONECT 4005 3962 CONECT 4017 3962 CONECT 4022 3962 CONECT 4023 3963 CONECT 4156 3964 CONECT 4158 3964 CONECT 4162 3964 CONECT 4165 3964 CONECT 4217 3964 MASTER 507 0 4 27 29 0 13 6 4420 2 57 41 END
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Entry Information
PDB ID
1t44
Complex Type
Protein-Protein
PDBbind Subset
general set
Protein Name
chimera of gelsolin domain 1 and c-terminal
Ligand Name
protein
EC.Number
E.C.-.-.-.-
Resolution
2(Å)
Affinity (Kd/Ki/IC50)
Kd=1uM
Release Year
2004
Protein/NA Sequence
Check fasta file
Primary Reference
Embo J. v23 pp. 3599-608, 2004
Links to External Databases
RCSB PDB
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PDBsum
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Pubchem
Comprehensive collection of chemical and biological data
UniProtKB AC
UniProt accession number (AC):
P06396
P20065
P68135
Entrez Gene ID
NCBI Entrez Gene ID:
2934
19241
ASD
Information of known allosteric effects of PDB entries
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