REMARK File generated by Swiss-PdbViewer 4.00b0 REMARK http://www.expasy.org/spdbv/ HEADER HYDROLASE (O-GLYCOSYL) 01-SEP-95 193L TITLE THE 1.33 A STRUCTURE OF TETRAGONAL HEN EGG WHITE LYSOZYME COMPND MOL_ID: 1; COMPND 2 MOLECULE: LYSOZYME; COMPND 3 CHAIN: A SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS; SOURCE 3 ORGANISM_COMMON: CHICKEN; SOURCE 4 ORGANISM_TAXID: 9031; SOURCE 5 CELLULAR_LOCATION: EGG WHITE KEYWDS HYDROLASE (O-GLYCOSYL) EXPDTA X-RAY DIFFRACTION AUTHOR M.C.VANEY,S.MAIGNAN,M.RIES-KAUTT,A.DUCRUIX REVDAT 2 24-FEB-09 193L 1 VERSN REVDAT 1 07-DEC-95 193L 0 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH M.M.RIES-KAUTT,I.BROUTIN,A.F.DUCRUIX,W.SHEPHARD, REMARK 1 AUTH 2 R.KAHN,B.LORBER,A.THEOBALD,R.GIEGE,N.CHAYEN,D.BLOW, REMARK 1 AUTH 3 K.PAAL,W.LITTKE REMARK 1 TITL EFFECT OF MICROGRAVITY ON RATE OF NUCLEATION, SIZE REMARK 1 TITL 2 AND QUALITY OF LYSOZYME CRYSTALS GROWN IN THE REMARK 1 TITL 3 ADVANCED PROTEIN CRYSTALLIZATION FACILITY ON REMARK 1 TITL 4 SPACEHAB-01 REMARK 1 REF TO BE PUBLISHED REMARK 1 REFN REMARK 1 REFERENCE 2 REMARK 1 AUTH A.C.M.YOUNG,R.F.TILTON,J.C.DEWAN REMARK 1 TITL THERMAL EXPANSION OF HEN-EGG-WHITE LYSOZYME. REMARK 1 TITL 2 COMPARISON OF THE 1.9 ANGSTROMS RESOLUTION REMARK 1 TITL 3 STRUCTURES OF THE TETRAGONAL FORM OF THE ENZYME AT REMARK 1 TITL 4 100K AND 298K REMARK 1 REF J.MOL.BIOL. V. 235 302 1994 REMARK 1 REFN ISSN 0022-2836 REMARK 1 REFERENCE 3 REMARK 1 AUTH R.BOSCH,P.LAUTENSCHLAGER,L.POTTHAST,J.STAPELMANN REMARK 1 TITL EXPERIMENT AND EQUIPMENT FOR PROTEIN REMARK 1 TITL 2 CRYSTALLIZATION IN MICROGRAM FACILITIES REMARK 1 REF J.CRYST.GROWTH V. 122 310 1992 REMARK 1 REFN ISSN 0022-0248 REMARK 2 REMARK 2 RESOLUTION. 1.33 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.33 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 7.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 23910 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING SET) : 0.184 REMARK 3 FREE R VALUE : 0.226 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000 REMARK 3 FREE R VALUE TEST SET COUNT : NULL REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : NULL REMARK 3 BIN FREE R VALUE : NULL REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1012 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 2 REMARK 3 SOLVENT ATOMS : 142 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.40 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.15 REMARK 3 ESD FROM SIGMAA (A) : NULL REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM C-V SIGMAA (A) : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.008 REMARK 3 BOND ANGLES (DEGREES) : 1.48 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.26 REMARK 3 IMPROPER ANGLES (DEGREES) : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 REMARK 3 NCS MODEL : NULL REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : NULL REMARK 3 TOPOLOGY FILE 1 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: SOME OF THE SIDE CHAIN ATOMS OF REMARK 3 RESIDUES ARG 21, ARG 61, TRP 62, ARG 73 ASN 77, LYS 97, ASP REMARK 3 101, ASN 103, GLN 121, ARG 125, AND LEU 129 HAVE A POORLY REMARK 3 DEFINED DENSITY. THESE ATOMS WERE BUILT USING STEREOCHEMICAL REMARK 3 CONSTRAINTS AND KEPT IN THE COORDINATE FILE. WATER MOLECULES REMARK 3 272 AND 273 ARE ON A TWO-FOLD AXIS AND HAVE BEEN MODELED WITH REMARK 3 50% OCCUPANCY. REMARK 4 REMARK 4 193L COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-SEP-93 REMARK 200 TEMPERATURE (KELVIN) : NULL REMARK 200 PH : 4.3 REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : LURE REMARK 200 BEAMLINE : DW32 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.901 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : NULL REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24111 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.330 REMARK 200 RESOLUTION RANGE LOW (A) : 15.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 87.1 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : 0.03100 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: NULL REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL REMARK 200 SOFTWARE USED: X-PLOR 3.1 REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 39.46 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PH 4.3 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4 REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4 REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4 REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4 REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 18.88500 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 39.27000 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 39.27000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 28.32750 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 39.27000 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 39.27000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 9.44250 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 39.27000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 39.27000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 28.32750 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 39.27000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 39.27000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 9.44250 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 18.88500 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: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH A 272 LIES ON A SPECIAL POSITION. REMARK 375 HOH A 273 LIES ON A SPECIAL POSITION. 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 ARG A 68 28.98 -141.69 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG A 125 0.13 SIDE_CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A 249 DISTANCE = 6.88 ANGSTROMS 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 NA A 131 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 SER A 60 O REMARK 620 2 CYS A 64 O 84.7 REMARK 620 3 SER A 72 OG 93.4 163.5 REMARK 620 4 ARG A 73 O 97.2 92.7 103.8 REMARK 620 5 HOH A 135 O 97.5 85.0 79.0 164.9 REMARK 620 6 HOH A 144 O 172.6 99.8 80.6 88.6 77.1 REMARK 620 N 1 2 3 4 5 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 130 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 131 DBREF 193L A 1 129 UNP P00698 LYSC_CHICK 19 147 CRYST1 78.540 78.540 37.770 90.00 90.00 90.00 P 43 21 2 8 ATOM 1 N LYS A 1 2.210 9.457 10.387 1.00 13.37 ATOM 2 CA LYS A 1 1.300 9.854 9.273 1.00 14.29 ATOM 3 C LYS A 1 1.331 11.365 9.051 1.00 14.29 ATOM 4 O LYS A 1 1.344 12.137 10.013 1.00 13.66 ATOM 5 CB LYS A 1 -0.140 9.415 9.591 1.00 15.13 ATOM 6 CG LYS A 1 -1.174 9.963 8.650 1.00 16.82 ATOM 7 CD LYS A 1 -2.566 9.469 8.985 0.45 17.79 ATOM 8 CE LYS A 1 -3.595 10.167 8.109 0.45 18.84 ATOM 9 NZ LYS A 1 -4.950 9.563 8.224 0.45 18.73 ATOM 10 N VAL A 2 1.379 11.780 7.791 1.00 13.97 ATOM 11 CA VAL A 2 1.370 13.199 7.462 1.00 14.71 ATOM 12 C VAL A 2 -0.047 13.501 6.989 1.00 15.34 ATOM 13 O VAL A 2 -0.502 12.952 5.990 1.00 17.30 ATOM 14 CB VAL A 2 2.413 13.567 6.374 1.00 14.07 ATOM 15 CG1 VAL A 2 2.282 15.052 5.993 1.00 15.84 ATOM 16 CG2 VAL A 2 3.823 13.299 6.894 1.00 14.87 ATOM 17 N PHE A 3 -0.782 14.278 7.769 1.00 14.09 ATOM 18 CA PHE A 3 -2.156 14.607 7.421 1.00 15.17 ATOM 19 C PHE A 3 -2.271 15.673 6.355 1.00 15.85 ATOM 20 O PHE A 3 -1.366 16.491 6.168 1.00 16.11 ATOM 21 CB PHE A 3 -2.905 15.129 8.649 1.00 14.49 ATOM 22 CG PHE A 3 -3.502 14.055 9.509 1.00 14.70 ATOM 23 CD1 PHE A 3 -2.722 13.390 10.461 1.00 13.85 ATOM 24 CD2 PHE A 3 -4.857 13.728 9.395 1.00 14.51 ATOM 25 CE1 PHE A 3 -3.284 12.418 11.286 1.00 15.14 ATOM 26 CE2 PHE A 3 -5.433 12.754 10.215 1.00 15.47 ATOM 27 CZ PHE A 3 -4.645 12.097 11.165 1.00 16.25 ATOM 28 N GLY A 4 -3.377 15.623 5.632 1.00 16.73 ATOM 29 CA GLY A 4 -3.684 16.709 4.718 1.00 15.55 ATOM 30 C GLY A 4 -4.375 17.763 5.540 1.00 14.64 ATOM 31 O GLY A 4 -4.902 17.446 6.618 1.00 13.76 ATOM 32 N ARG A 5 -4.391 19.001 5.103 1.00 14.62 ATOM 33 CA ARG A 5 -4.999 20.073 5.876 1.00 14.63 ATOM 34 C ARG A 5 -6.452 19.787 6.256 1.00 14.82 ATOM 35 O ARG A 5 -6.803 19.785 7.440 1.00 14.07 ATOM 36 CB ARG A 5 -4.896 21.383 5.103 1.00 14.87 ATOM 37 CG ARG A 5 -5.462 22.577 5.829 1.00 15.19 ATOM 38 CD ARG A 5 -5.241 23.849 5.036 1.00 18.00 ATOM 39 NE ARG A 5 -5.856 23.826 3.706 1.00 21.12 ATOM 40 CZ ARG A 5 -7.147 24.071 3.451 1.00 22.48 ATOM 41 NH1 ARG A 5 -8.002 24.358 4.431 1.00 21.31 ATOM 42 NH2 ARG A 5 -7.583 24.056 2.196 1.00 22.99 ATOM 43 N CYS A 6 -7.294 19.528 5.256 1.00 15.31 ATOM 44 CA CYS A 6 -8.713 19.242 5.517 1.00 15.61 ATOM 45 C CYS A 6 -8.939 17.904 6.212 1.00 14.43 ATOM 46 O CYS A 6 -9.877 17.747 6.988 1.00 14.93 ATOM 47 CB CYS A 6 -9.528 19.321 4.220 1.00 16.02 ATOM 48 SG CYS A 6 -9.531 20.985 3.490 1.00 17.40 ATOM 49 N GLU A 7 -8.052 16.945 5.967 1.00 14.47 ATOM 50 CA GLU A 7 -8.167 15.633 6.597 1.00 13.90 ATOM 51 C GLU A 7 -7.968 15.788 8.101 1.00 13.12 ATOM 52 O GLU A 7 -8.669 15.181 8.900 1.00 12.30 ATOM 53 CB GLU A 7 -7.110 14.683 6.044 1.00 15.30 ATOM 54 CG GLU A 7 -7.216 13.265 6.581 1.00 16.04 ATOM 55 CD GLU A 7 -6.026 12.402 6.206 1.00 17.22 ATOM 56 OE1 GLU A 7 -4.971 12.960 5.838 1.00 18.97 ATOM 57 OE2 GLU A 7 -6.123 11.157 6.310 1.00 18.13 ATOM 58 N LEU A 8 -6.999 16.613 8.476 1.00 12.65 ATOM 59 CA LEU A 8 -6.733 16.867 9.886 1.00 12.99 ATOM 60 C LEU A 8 -7.891 17.662 10.510 1.00 13.22 ATOM 61 O LEU A 8 -8.337 17.364 11.623 1.00 13.89 ATOM 62 CB LEU A 8 -5.419 17.636 10.049 1.00 12.73 ATOM 63 CG LEU A 8 -5.080 17.925 11.509 1.00 12.66 ATOM 64 CD1 LEU A 8 -4.903 16.606 12.291 1.00 12.97 ATOM 65 CD2 LEU A 8 -3.823 18.758 11.566 1.00 12.62 ATOM 66 N ALA A 9 -8.360 18.684 9.797 1.00 13.18 ATOM 67 CA ALA A 9 -9.481 19.503 10.263 1.00 13.55 ATOM 68 C ALA A 9 -10.674 18.601 10.590 1.00 12.97 ATOM 69 O ALA A 9 -11.261 18.697 11.667 1.00 13.63 ATOM 70 CB ALA A 9 -9.871 20.537 9.184 1.00 12.88 ATOM 71 N ALA A 10 -11.002 17.695 9.675 1.00 13.47 ATOM 72 CA ALA A 10 -12.118 16.779 9.882 1.00 14.09 ATOM 73 C ALA A 10 -11.884 15.876 11.093 1.00 14.14 ATOM 74 O ALA A 10 -12.776 15.670 11.910 1.00 14.67 ATOM 75 CB ALA A 10 -12.348 15.939 8.629 1.00 14.89 ATOM 76 N ALA A 11 -10.673 15.347 11.218 1.00 14.21 ATOM 77 CA ALA A 11 -10.344 14.475 12.337 1.00 13.56 ATOM 78 C ALA A 11 -10.448 15.222 13.669 1.00 14.33 ATOM 79 O ALA A 11 -10.957 14.681 14.655 1.00 14.05 ATOM 80 CB ALA A 11 -8.937 13.894 12.160 1.00 14.75 ATOM 81 N MET A 12 -9.963 16.463 13.697 1.00 13.39 ATOM 82 CA MET A 12 -10.001 17.259 14.911 1.00 13.27 ATOM 83 C MET A 12 -11.420 17.593 15.295 1.00 14.06 ATOM 84 O MET A 12 -11.778 17.532 16.475 1.00 15.18 ATOM 85 CB MET A 12 -9.194 18.527 14.729 1.00 11.79 ATOM 86 CG MET A 12 -7.708 18.270 14.750 1.00 13.16 ATOM 87 SD MET A 12 -6.768 19.779 14.548 1.00 14.24 ATOM 88 CE MET A 12 -5.295 19.399 15.529 1.00 14.01 ATOM 89 N LYS A 13 -12.234 17.901 14.290 1.00 15.13 ATOM 90 CA LYS A 13 -13.636 18.246 14.501 1.00 17.62 ATOM 91 C LYS A 13 -14.370 17.058 15.090 1.00 17.54 ATOM 92 O LYS A 13 -15.087 17.195 16.087 1.00 17.53 ATOM 93 CB LYS A 13 -14.277 18.666 13.177 1.00 19.34 ATOM 94 CG LYS A 13 -15.722 19.106 13.279 1.00 24.12 ATOM 95 CD LYS A 13 -16.054 20.016 12.109 1.00 27.22 ATOM 96 CE LYS A 13 -17.499 20.473 12.124 1.00 30.99 ATOM 97 NZ LYS A 13 -18.384 19.401 11.625 1.00 34.31 ATOM 98 N ARG A 14 -14.115 15.880 14.521 1.00 18.54 ATOM 99 CA ARG A 14 -14.739 14.640 14.970 1.00 19.34 ATOM 100 C ARG A 14 -14.347 14.352 16.410 1.00 18.83 ATOM 101 O ARG A 14 -15.136 13.800 17.176 1.00 18.28 ATOM 102 CB ARG A 14 -14.317 13.475 14.076 1.00 21.49 ATOM 103 CG ARG A 14 -15.440 12.496 13.805 1.00 28.11 ATOM 104 CD ARG A 14 -15.064 11.066 14.153 1.00 31.94 ATOM 105 NE ARG A 14 -13.726 10.691 13.705 1.00 35.42 ATOM 106 CZ ARG A 14 -13.091 9.597 14.124 1.00 36.74 ATOM 107 NH1 ARG A 14 -13.689 8.771 14.978 1.00 38.31 ATOM 108 NH2 ARG A 14 -11.852 9.342 13.719 1.00 38.45 ATOM 109 N HIS A 15 -13.126 14.747 16.779 1.00 17.87 ATOM 110 CA HIS A 15 -12.635 14.546 18.135 1.00 17.87 ATOM 111 C HIS A 15 -13.013 15.647 19.127 1.00 17.62 ATOM 112 O HIS A 15 -12.497 15.679 20.251 1.00 17.95 ATOM 113 CB HIS A 15 -11.134 14.286 18.133 1.00 18.14 ATOM 114 CG HIS A 15 -10.779 12.878 17.778 1.00 21.24 ATOM 115 ND1 HIS A 15 -10.472 12.489 16.492 1.00 21.64 ATOM 116 CD2 HIS A 15 -10.715 11.753 18.534 1.00 21.77 ATOM 117 CE1 HIS A 15 -10.232 11.184 16.471 1.00 22.34 ATOM 118 NE2 HIS A 15 -10.375 10.718 17.702 1.00 22.99 ATOM 119 N GLY A 16 -13.902 16.545 18.697 1.00 18.20 ATOM 120 CA GLY A 16 -14.409 17.607 19.557 1.00 18.44 ATOM 121 C GLY A 16 -13.568 18.840 19.822 1.00 19.98 ATOM 122 O GLY A 16 -13.802 19.556 20.804 1.00 19.75 ATOM 123 N LEU A 17 -12.593 19.100 18.962 1.00 19.58 ATOM 124 CA LEU A 17 -11.748 20.271 19.139 1.00 18.96 ATOM 125 C LEU A 17 -12.330 21.578 18.608 1.00 19.27 ATOM 126 O LEU A 17 -11.913 22.651 19.041 1.00 20.08 ATOM 127 CB LEU A 17 -10.365 20.033 18.531 1.00 17.97 ATOM 128 CG LEU A 17 -9.409 19.168 19.346 1.00 17.46 ATOM 129 CD1 LEU A 17 -8.046 19.186 18.653 1.00 18.90 ATOM 130 CD2 LEU A 17 -9.269 19.711 20.761 1.00 17.30 ATOM 131 N ASP A 18 -13.292 21.521 17.691 1.00 18.80 ATOM 132 CA ASP A 18 -13.852 22.766 17.165 1.00 19.86 ATOM 133 C ASP A 18 -14.545 23.517 18.295 1.00 19.44 ATOM 134 O ASP A 18 -15.488 23.017 18.914 1.00 19.72 ATOM 135 CB ASP A 18 -14.822 22.517 16.004 1.00 21.82 ATOM 136 CG ASP A 18 -15.301 23.819 15.321 1.00 24.65 ATOM 137 OD1 ASP A 18 -14.663 24.898 15.466 1.00 24.44 ATOM 138 OD2 ASP A 18 -16.339 23.757 14.616 1.00 27.71 ATOM 139 N ASN A 19 -14.012 24.692 18.598 1.00 18.59 ATOM 140 CA ASN A 19 -14.530 25.550 19.648 1.00 18.72 ATOM 141 C ASN A 19 -14.277 25.020 21.061 1.00 17.40 ATOM 142 O ASN A 19 -14.863 25.511 22.027 1.00 17.35 ATOM 143 CB ASN A 19 -16.015 25.844 19.418 1.00 23.30 ATOM 144 CG ASN A 19 -16.283 26.407 18.030 1.00 28.52 ATOM 145 OD1 ASN A 19 -15.817 27.500 17.687 1.00 31.85 ATOM 146 ND2 ASN A 19 -16.996 25.646 17.208 1.00 31.76 ATOM 147 N TYR A 20 -13.377 24.048 21.200 1.00 15.72 ATOM 148 CA TYR A 20 -13.057 23.531 22.520 1.00 14.39 ATOM 149 C TYR A 20 -12.366 24.665 23.287 1.00 15.42 ATOM 150 O TYR A 20 -11.381 25.230 22.814 1.00 14.26 ATOM 151 CB TYR A 20 -12.142 22.312 22.439 1.00 13.40 ATOM 152 CG TYR A 20 -11.980 21.658 23.784 1.00 14.68 ATOM 153 CD1 TYR A 20 -12.939 20.766 24.262 1.00 15.01 ATOM 154 CD2 TYR A 20 -10.904 21.979 24.611 1.00 14.49 ATOM 155 CE1 TYR A 20 -12.834 20.219 25.531 1.00 17.21 ATOM 156 CE2 TYR A 20 -10.789 21.444 25.880 1.00 15.61 ATOM 157 CZ TYR A 20 -11.755 20.565 26.335 1.00 17.85 ATOM 158 OH TYR A 20 -11.652 20.050 27.604 1.00 21.01 ATOM 159 N ARG A 21 -12.920 25.011 24.451 1.00 15.93 ATOM 160 CA ARG A 21 -12.426 26.112 25.299 1.00 17.50 ATOM 161 C ARG A 21 -12.459 27.427 24.535 1.00 15.51 ATOM 162 O ARG A 21 -11.653 28.319 24.800 1.00 16.42 ATOM 163 CB ARG A 21 -11.009 25.859 25.830 1.00 19.77 ATOM 164 CG ARG A 21 -10.902 24.720 26.803 1.00 26.43 ATOM 165 CD ARG A 21 -11.645 25.005 28.085 1.00 32.75 ATOM 166 NE ARG A 21 -11.995 23.759 28.759 1.00 38.98 ATOM 167 CZ ARG A 21 -12.064 23.607 30.076 1.00 42.00 ATOM 168 NH1 ARG A 21 -11.739 24.612 30.891 1.00 42.87 ATOM 169 NH2 ARG A 21 -12.398 22.421 30.580 1.00 44.67 ATOM 170 N GLY A 22 -13.366 27.519 23.569 1.00 13.94 ATOM 171 CA GLY A 22 -13.498 28.722 22.769 1.00 14.18 ATOM 172 C GLY A 22 -12.545 28.869 21.588 1.00 13.69 ATOM 173 O GLY A 22 -12.527 29.920 20.933 1.00 14.16 ATOM 174 N TYR A 23 -11.750 27.841 21.296 1.00 13.04 ATOM 175 CA TYR A 23 -10.812 27.924 20.173 1.00 11.72 ATOM 176 C TYR A 23 -11.382 27.246 18.950 1.00 11.64 ATOM 177 O TYR A 23 -11.540 26.032 18.926 1.00 11.49 ATOM 178 CB TYR A 23 -9.466 27.307 20.536 1.00 10.94 ATOM 179 CG TYR A 23 -8.732 28.112 21.575 1.00 9.56 ATOM 180 CD1 TYR A 23 -7.905 29.166 21.199 1.00 9.66 ATOM 181 CD2 TYR A 23 -8.861 27.821 22.936 1.00 9.70 ATOM 182 CE1 TYR A 23 -7.216 29.910 22.152 1.00 9.56 ATOM 183 CE2 TYR A 23 -8.176 28.565 23.897 1.00 10.01 ATOM 184 CZ TYR A 23 -7.351 29.609 23.491 1.00 9.39 ATOM 185 OH TYR A 23 -6.624 30.329 24.410 1.00 10.65 ATOM 186 N SER A 24 -11.658 28.039 17.921 1.00 12.38 ATOM 187 CA SER A 24 -12.227 27.502 16.696 1.00 12.92 ATOM 188 C SER A 24 -11.249 26.543 16.042 1.00 13.28 ATOM 189 O SER A 24 -10.037 26.611 16.282 1.00 12.29 ATOM 190 CB SER A 24 -12.600 28.624 15.740 1.00 13.26 ATOM 191 OG SER A 24 -11.476 29.427 15.414 1.00 15.80 ATOM 192 N LEU A 25 -11.786 25.673 15.200 1.00 13.55 ATOM 193 CA LEU A 25 -11.008 24.664 14.510 1.00 12.98 ATOM 194 C LEU A 25 -9.772 25.190 13.800 1.00 12.15 ATOM 195 O LEU A 25 -8.721 24.543 13.818 1.00 11.55 ATOM 196 CB LEU A 25 -11.911 23.935 13.522 1.00 14.24 ATOM 197 CG LEU A 25 -11.513 22.545 13.046 1.00 14.22 ATOM 198 CD1 LEU A 25 -11.300 21.634 14.237 1.00 15.56 ATOM 199 CD2 LEU A 25 -12.615 21.999 12.148 1.00 14.68 ATOM 200 N GLY A 26 -9.883 26.354 13.169 1.00 11.53 ATOM 201 CA GLY A 26 -8.741 26.919 12.466 1.00 11.04 ATOM 202 C GLY A 26 -7.525 27.115 13.357 1.00 10.33 ATOM 203 O GLY A 26 -6.396 27.004 12.904 1.00 11.77 ATOM 204 N ASN A 27 -7.756 27.401 14.633 1.00 9.22 ATOM 205 CA ASN A 27 -6.656 27.598 15.577 1.00 9.74 ATOM 206 C ASN A 27 -5.871 26.309 15.763 1.00 9.99 ATOM 207 O ASN A 27 -4.645 26.309 15.774 1.00 10.32 ATOM 208 CB ASN A 27 -7.181 28.054 16.937 1.00 10.93 ATOM 209 CG ASN A 27 -7.538 29.513 16.952 1.00 11.10 ATOM 210 OD1 ASN A 27 -6.665 30.363 17.008 1.00 11.18 ATOM 211 ND2 ASN A 27 -8.827 29.814 16.864 1.00 12.48 ATOM 212 N TRP A 28 -6.594 25.206 15.897 1.00 9.30 ATOM 213 CA TRP A 28 -5.983 23.903 16.097 1.00 9.65 ATOM 214 C TRP A 28 -5.228 23.431 14.873 1.00 9.67 ATOM 215 O TRP A 28 -4.145 22.858 14.990 1.00 10.34 ATOM 216 CB TRP A 28 -7.053 22.892 16.495 1.00 9.50 ATOM 217 CG TRP A 28 -7.680 23.248 17.788 1.00 9.24 ATOM 218 CD1 TRP A 28 -8.902 23.821 17.981 1.00 10.46 ATOM 219 CD2 TRP A 28 -7.113 23.058 19.091 1.00 10.54 ATOM 220 NE1 TRP A 28 -9.137 23.995 19.325 1.00 10.25 ATOM 221 CE2 TRP A 28 -8.056 23.536 20.030 1.00 10.50 ATOM 222 CE3 TRP A 28 -5.895 22.526 19.557 1.00 11.51 ATOM 223 CZ2 TRP A 28 -7.827 23.493 21.410 1.00 12.28 ATOM 224 CZ3 TRP A 28 -5.669 22.484 20.929 1.00 13.13 ATOM 225 CH2 TRP A 28 -6.630 22.969 21.840 1.00 13.31 ATOM 226 N VAL A 29 -5.793 23.673 13.698 1.00 9.43 ATOM 227 CA VAL A 29 -5.144 23.261 12.461 1.00 9.34 ATOM 228 C VAL A 29 -3.891 24.096 12.243 1.00 8.98 ATOM 229 O VAL A 29 -2.838 23.575 11.891 1.00 10.02 ATOM 230 CB VAL A 29 -6.107 23.374 11.258 1.00 11.07 ATOM 231 CG1 VAL A 29 -5.358 23.048 9.947 1.00 12.02 ATOM 232 CG2 VAL A 29 -7.303 22.426 11.462 1.00 10.22 ATOM 233 N CYS A 30 -3.996 25.386 12.500 1.00 8.26 ATOM 234 CA CYS A 30 -2.856 26.270 12.356 1.00 9.10 ATOM 235 C CYS A 30 -1.743 25.846 13.330 1.00 9.20 ATOM 236 O CYS A 30 -0.566 25.804 12.963 1.00 9.57 ATOM 237 CB CYS A 30 -3.285 27.708 12.641 1.00 9.73 ATOM 238 SG CYS A 30 -1.961 28.925 12.425 1.00 11.14 ATOM 239 N ALA A 31 -2.120 25.520 14.565 1.00 9.01 ATOM 240 CA ALA A 31 -1.141 25.099 15.561 1.00 10.45 ATOM 241 C ALA A 31 -0.431 23.828 15.089 1.00 10.35 ATOM 242 O ALA A 31 0.800 23.749 15.132 1.00 11.31 ATOM 243 CB ALA A 31 -1.811 24.865 16.905 1.00 10.58 ATOM 244 N ALA A 32 -1.199 22.863 14.589 1.00 9.56 ATOM 245 CA ALA A 32 -0.622 21.614 14.111 1.00 9.32 ATOM 246 C ALA A 32 0.314 21.865 12.933 1.00 9.93 ATOM 247 O ALA A 32 1.380 21.253 12.834 1.00 10.53 ATOM 248 CB ALA A 32 -1.721 20.634 13.718 1.00 8.67 ATOM 249 N LYS A 33 -0.082 22.754 12.034 1.00 9.58 ATOM 250 CA LYS A 33 0.744 23.066 10.875 1.00 10.82 ATOM 251 C LYS A 33 2.121 23.554 11.290 1.00 11.40 ATOM 252 O LYS A 33 3.149 23.047 10.828 1.00 12.21 ATOM 253 CB LYS A 33 0.086 24.151 10.020 1.00 12.47 ATOM 254 CG LYS A 33 0.992 24.714 8.930 1.00 14.14 ATOM 255 CD LYS A 33 1.343 23.664 7.896 1.00 17.39 ATOM 256 CE LYS A 33 2.257 24.242 6.833 1.00 19.47 ATOM 257 NZ LYS A 33 2.566 23.218 5.808 1.00 22.35 ATOM 258 N PHE A 34 2.139 24.541 12.172 1.00 10.96 ATOM 259 CA PHE A 34 3.400 25.106 12.583 1.00 11.15 ATOM 260 C PHE A 34 4.165 24.345 13.624 1.00 11.12 ATOM 261 O PHE A 34 5.369 24.515 13.729 1.00 13.10 ATOM 262 CB PHE A 34 3.233 26.585 12.919 1.00 11.71 ATOM 263 CG PHE A 34 2.808 27.400 11.728 1.00 11.01 ATOM 264 CD1 PHE A 34 3.532 27.321 10.530 1.00 10.99 ATOM 265 CD2 PHE A 34 1.664 28.186 11.772 1.00 12.03 ATOM 266 CE1 PHE A 34 3.110 28.013 9.385 1.00 13.03 ATOM 267 CE2 PHE A 34 1.232 28.882 10.637 1.00 14.31 ATOM 268 CZ PHE A 34 1.959 28.796 9.440 1.00 12.81 ATOM 269 N GLU A 35 3.493 23.490 14.373 1.00 9.43 ATOM 270 CA GLU A 35 4.191 22.705 15.374 1.00 10.08 ATOM 271 C GLU A 35 4.851 21.473 14.773 1.00 10.99 ATOM 272 O GLU A 35 6.003 21.184 15.066 1.00 11.00 ATOM 273 CB GLU A 35 3.227 22.245 16.470 1.00 9.70 ATOM 274 CG GLU A 35 2.787 23.347 17.437 1.00 10.97 ATOM 275 CD GLU A 35 3.912 23.832 18.350 1.00 12.32 ATOM 276 OE1 GLU A 35 4.977 23.182 18.388 1.00 12.78 ATOM 277 OE2 GLU A 35 3.735 24.854 19.042 1.00 13.36 ATOM 278 N SER A 36 4.139 20.780 13.886 1.00 10.28 ATOM 279 CA SER A 36 4.638 19.520 13.331 1.00 10.77 ATOM 280 C SER A 36 4.566 19.345 11.824 1.00 11.17 ATOM 281 O SER A 36 4.933 18.284 11.312 1.00 10.95 ATOM 282 CB SER A 36 3.799 18.396 13.926 1.00 10.55 ATOM 283 OG SER A 36 2.472 18.471 13.412 1.00 10.56 ATOM 284 N ASN A 37 4.039 20.349 11.127 1.00 11.35 ATOM 285 CA ASN A 37 3.837 20.289 9.684 1.00 13.06 ATOM 286 C ASN A 37 2.880 19.131 9.374 1.00 11.81 ATOM 287 O ASN A 37 3.021 18.441 8.373 1.00 11.83 ATOM 288 CB ASN A 37 5.160 20.155 8.915 1.00 16.57 ATOM 289 CG ASN A 37 5.057 20.687 7.502 1.00 19.26 ATOM 290 OD1 ASN A 37 4.190 21.511 7.194 1.00 21.93 ATOM 291 ND2 ASN A 37 5.949 20.236 6.633 1.00 22.36 ATOM 292 N PHE A 38 1.931 18.921 10.284 1.00 10.80 ATOM 293 CA PHE A 38 0.899 17.891 10.181 1.00 11.05 ATOM 294 C PHE A 38 1.433 16.460 10.249 1.00 11.23 ATOM 295 O PHE A 38 0.749 15.525 9.832 1.00 11.64 ATOM 296 CB PHE A 38 0.107 18.044 8.875 1.00 11.84 ATOM 297 CG PHE A 38 -0.604 19.357 8.721 1.00 11.03 ATOM 298 CD1 PHE A 38 -1.157 20.007 9.813 1.00 10.74 ATOM 299 CD2 PHE A 38 -0.767 19.907 7.452 1.00 11.96 ATOM 300 CE1 PHE A 38 -1.885 21.184 9.645 1.00 12.02 ATOM 301 CE2 PHE A 38 -1.486 21.074 7.268 1.00 12.63 ATOM 302 CZ PHE A 38 -2.046 21.715 8.372 1.00 11.53 ATOM 303 N ASN A 39 2.637 16.289 10.780 1.00 10.53 ATOM 304 CA ASN A 39 3.260 14.968 10.871 1.00 10.57 ATOM 305 C ASN A 39 3.118 14.427 12.286 1.00 9.87 ATOM 306 O ASN A 39 3.695 14.979 13.227 1.00 10.36 ATOM 307 CB ASN A 39 4.741 15.088 10.498 1.00 10.33 ATOM 308 CG ASN A 39 5.462 13.751 10.459 1.00 11.53 ATOM 309 OD1 ASN A 39 4.882 12.683 10.699 1.00 11.65 ATOM 310 ND2 ASN A 39 6.747 13.807 10.142 1.00 14.65 ATOM 311 N THR A 40 2.394 13.322 12.429 1.00 10.06 ATOM 312 CA THR A 40 2.180 12.717 13.737 1.00 10.33 ATOM 313 C THR A 40 3.460 12.197 14.366 1.00 9.50 ATOM 314 O THR A 40 3.528 12.050 15.569 1.00 9.75 ATOM 315 CB THR A 40 1.194 11.535 13.675 1.00 10.60 ATOM 316 OG1 THR A 40 1.741 10.484 12.869 1.00 11.46 ATOM 317 CG2 THR A 40 -0.136 11.979 13.092 1.00 11.39 ATOM 318 N GLN A 41 4.471 11.934 13.542 1.00 9.67 ATOM 319 CA GLN A 41 5.727 11.372 14.036 1.00 9.89 ATOM 320 C GLN A 41 6.797 12.381 14.421 1.00 10.85 ATOM 321 O GLN A 41 7.903 12.008 14.811 1.00 11.99 ATOM 322 CB GLN A 41 6.289 10.385 13.005 1.00 10.94 ATOM 323 CG GLN A 41 5.371 9.197 12.724 1.00 10.65 ATOM 324 CD GLN A 41 6.096 8.070 12.023 1.00 12.26 ATOM 325 OE1 GLN A 41 6.862 7.329 12.643 1.00 14.95 ATOM 326 NE2 GLN A 41 5.902 7.965 10.721 1.00 12.26 ATOM 327 N ALA A 42 6.464 13.659 14.346 1.00 10.56 ATOM 328 CA ALA A 42 7.428 14.698 14.672 1.00 11.45 ATOM 329 C ALA A 42 7.862 14.678 16.136 1.00 10.35 ATOM 330 O ALA A 42 7.044 14.492 17.042 1.00 9.67 ATOM 331 CB ALA A 42 6.853 16.071 14.317 1.00 11.14 ATOM 332 N THR A 43 9.165 14.809 16.349 1.00 9.71 ATOM 333 CA THR A 43 9.721 14.885 17.685 1.00 10.65 ATOM 334 C THR A 43 10.774 15.972 17.655 1.00 10.48 ATOM 335 O THR A 43 11.438 16.191 16.640 1.00 11.99 ATOM 336 CB THR A 43 10.403 13.575 18.138 1.00 11.80 ATOM 337 OG1 THR A 43 11.423 13.215 17.195 1.00 13.27 ATOM 338 CG2 THR A 43 9.402 12.443 18.281 1.00 11.63 ATOM 339 N ASN A 44 10.922 16.670 18.768 1.00 10.86 ATOM 340 CA ASN A 44 11.930 17.707 18.870 1.00 12.02 ATOM 341 C ASN A 44 12.405 17.792 20.308 1.00 11.65 ATOM 342 O ASN A 44 11.596 17.855 21.221 1.00 11.37 ATOM 343 CB ASN A 44 11.363 19.040 18.397 1.00 15.07 ATOM 344 CG ASN A 44 11.119 19.065 16.884 1.00 17.60 ATOM 345 OD1 ASN A 44 9.990 18.931 16.415 1.00 20.46 ATOM 346 ND2 ASN A 44 12.191 19.200 16.121 1.00 17.83 ATOM 347 N ARG A 45 13.723 17.748 20.500 1.00 12.62 ATOM 348 CA ARG A 45 14.322 17.811 21.835 1.00 14.02 ATOM 349 C ARG A 45 14.471 19.259 22.270 1.00 14.67 ATOM 350 O ARG A 45 14.826 20.119 21.465 1.00 15.70 ATOM 351 CB ARG A 45 15.716 17.170 21.829 1.00 16.53 ATOM 352 CG ARG A 45 16.269 16.846 23.211 1.00 18.27 ATOM 353 CD ARG A 45 15.759 15.500 23.633 1.00 22.98 ATOM 354 NE ARG A 45 16.007 15.193 25.037 1.00 26.61 ATOM 355 CZ ARG A 45 16.969 14.379 25.476 1.00 25.91 ATOM 356 NH1 ARG A 45 17.797 13.800 24.618 1.00 26.21 ATOM 357 NH2 ARG A 45 17.018 14.048 26.760 1.00 24.84 ATOM 358 N ASN A 46 14.214 19.516 23.546 1.00 15.32 ATOM 359 CA ASN A 46 14.334 20.852 24.113 1.00 17.33 ATOM 360 C ASN A 46 15.641 20.901 24.884 1.00 17.85 ATOM 361 O ASN A 46 16.170 19.863 25.268 1.00 18.68 ATOM 362 CB ASN A 46 13.151 21.136 25.036 1.00 18.35 ATOM 363 CG ASN A 46 11.807 21.014 24.321 1.00 18.89 ATOM 364 OD1 ASN A 46 10.889 20.342 24.796 1.00 21.71 ATOM 365 ND2 ASN A 46 11.694 21.653 23.170 1.00 20.89 ATOM 366 N THR A 47 16.145 22.102 25.154 1.00 20.72 ATOM 367 CA THR A 47 17.421 22.268 25.870 1.00 22.40 ATOM 368 C THR A 47 17.402 21.716 27.283 1.00 21.60 ATOM 369 O THR A 47 18.430 21.252 27.777 1.00 23.34 ATOM 370 CB THR A 47 17.871 23.748 25.921 1.00 23.96 ATOM 371 OG1 THR A 47 16.857 24.544 26.546 1.00 27.12 ATOM 372 CG2 THR A 47 18.107 24.262 24.522 1.00 24.96 ATOM 373 N ASP A 48 16.243 21.759 27.931 1.00 20.29 ATOM 374 CA ASP A 48 16.130 21.238 29.283 1.00 19.93 ATOM 375 C ASP A 48 16.109 19.707 29.304 1.00 19.44 ATOM 376 O ASP A 48 15.982 19.105 30.374 1.00 21.00 ATOM 377 CB ASP A 48 14.895 21.805 29.991 1.00 19.87 ATOM 378 CG ASP A 48 13.604 21.393 29.342 1.00 21.86 ATOM 379 OD1 ASP A 48 13.626 20.745 28.284 1.00 23.77 ATOM 380 OD2 ASP A 48 12.538 21.722 29.881 1.00 24.18 ATOM 381 N GLY A 49 16.185 19.077 28.132 1.00 17.49 ATOM 382 CA GLY A 49 16.194 17.630 28.080 1.00 15.16 ATOM 383 C GLY A 49 14.849 16.985 27.802 1.00 14.92 ATOM 384 O GLY A 49 14.775 15.775 27.559 1.00 15.53 ATOM 385 N SER A 50 13.777 17.766 27.865 1.00 13.01 ATOM 386 CA SER A 50 12.459 17.230 27.584 1.00 11.88 ATOM 387 C SER A 50 12.344 17.118 26.061 1.00 11.11 ATOM 388 O SER A 50 13.212 17.601 25.331 1.00 11.91 ATOM 389 CB SER A 50 11.390 18.165 28.124 1.00 12.17 ATOM 390 OG SER A 50 11.453 19.413 27.461 1.00 13.80 ATOM 391 N THR A 51 11.294 16.471 25.580 1.00 10.21 ATOM 392 CA THR A 51 11.106 16.308 24.142 1.00 10.41 ATOM 393 C THR A 51 9.640 16.578 23.839 1.00 10.15 ATOM 394 O THR A 51 8.785 16.314 24.689 1.00 10.32 ATOM 395 CB THR A 51 11.465 14.867 23.700 1.00 11.09 ATOM 396 OG1 THR A 51 12.839 14.590 24.029 1.00 10.36 ATOM 397 CG2 THR A 51 11.256 14.678 22.193 1.00 11.19 ATOM 398 N ASP A 52 9.379 17.176 22.676 1.00 9.24 ATOM 399 CA ASP A 52 8.025 17.475 22.214 1.00 10.05 ATOM 400 C ASP A 52 7.655 16.363 21.253 1.00 9.60 ATOM 401 O ASP A 52 8.472 15.974 20.416 1.00 9.31 ATOM 402 CB ASP A 52 7.983 18.814 21.504 1.00 10.93 ATOM 403 CG ASP A 52 8.250 19.960 22.431 1.00 13.72 ATOM 404 OD1 ASP A 52 8.063 19.815 23.648 1.00 14.45 ATOM 405 OD2 ASP A 52 8.640 21.033 21.940 1.00 20.90 ATOM 406 N TYR A 53 6.412 15.898 21.345 1.00 9.77 ATOM 407 CA TYR A 53 5.944 14.770 20.557 1.00 9.16 ATOM 408 C TYR A 53 4.666 14.966 19.809 1.00 9.89 ATOM 409 O TYR A 53 3.691 15.498 20.342 1.00 10.43 ATOM 410 CB TYR A 53 5.671 13.584 21.480 1.00 9.20 ATOM 411 CG TYR A 53 6.881 13.041 22.170 1.00 9.57 ATOM 412 CD1 TYR A 53 7.336 13.601 23.363 1.00 9.84 ATOM 413 CD2 TYR A 53 7.596 11.977 21.621 1.00 9.56 ATOM 414 CE1 TYR A 53 8.473 13.119 23.989 1.00 9.68 ATOM 415 CE2 TYR A 53 8.731 11.488 22.239 1.00 10.81 ATOM 416 CZ TYR A 53 9.157 12.068 23.421 1.00 10.34 ATOM 417 OH TYR A 53 10.277 11.595 24.039 1.00 11.24 ATOM 418 N GLY A 54 4.660 14.461 18.590 1.00 10.05 ATOM 419 CA GLY A 54 3.451 14.465 17.811 1.00 10.60 ATOM 420 C GLY A 54 3.030 15.696 17.072 1.00 9.45 ATOM 421 O GLY A 54 3.702 16.727 17.047 1.00 9.58 ATOM 422 N ILE A 55 1.829 15.574 16.538 1.00 10.35 ATOM 423 CA ILE A 55 1.223 16.588 15.727 1.00 11.34 ATOM 424 C ILE A 55 1.076 17.928 16.456 1.00 10.64 ATOM 425 O ILE A 55 1.178 18.982 15.832 1.00 11.19 ATOM 426 CB ILE A 55 -0.102 16.037 15.121 1.00 13.92 ATOM 427 CG1 ILE A 55 -0.467 16.823 13.865 1.00 16.20 ATOM 428 CG2 ILE A 55 -1.208 15.989 16.178 1.00 13.61 ATOM 429 CD1 ILE A 55 -1.389 16.089 12.943 1.00 19.40 ATOM 430 N LEU A 56 0.905 17.890 17.774 1.00 10.04 ATOM 431 CA LEU A 56 0.777 19.110 18.544 1.00 10.90 ATOM 432 C LEU A 56 1.982 19.355 19.422 1.00 10.87 ATOM 433 O LEU A 56 1.945 20.184 20.329 1.00 10.72 ATOM 434 CB LEU A 56 -0.520 19.115 19.353 1.00 13.20 ATOM 435 CG LEU A 56 -1.768 19.342 18.497 1.00 14.34 ATOM 436 CD1 LEU A 56 -3.019 19.127 19.330 1.00 15.08 ATOM 437 CD2 LEU A 56 -1.719 20.746 17.898 1.00 15.46 ATOM 438 N GLN A 57 3.043 18.589 19.188 1.00 9.95 ATOM 439 CA GLN A 57 4.285 18.767 19.927 1.00 9.90 ATOM 440 C GLN A 57 4.104 18.898 21.441 1.00 9.80 ATOM 441 O GLN A 57 4.550 19.867 22.047 1.00 11.12 ATOM 442 CB GLN A 57 5.030 19.983 19.361 1.00 9.56 ATOM 443 CG GLN A 57 5.595 19.730 17.964 1.00 10.26 ATOM 444 CD GLN A 57 6.714 18.715 17.989 1.00 10.58 ATOM 445 OE1 GLN A 57 7.860 19.063 18.252 1.00 10.26 ATOM 446 NE2 GLN A 57 6.379 17.442 17.758 1.00 10.79 ATOM 447 N ILE A 58 3.474 17.895 22.037 1.00 10.17 ATOM 448 CA ILE A 58 3.222 17.874 23.464 1.00 11.03 ATOM 449 C ILE A 58 4.509 17.517 24.209 1.00 11.94 ATOM 450 O ILE A 58 5.229 16.568 23.857 1.00 10.74 ATOM 451 CB ILE A 58 2.052 16.943 23.769 1.00 12.23 ATOM 452 CG1 ILE A 58 0.768 17.602 23.257 1.00 10.94 ATOM 453 CG2 ILE A 58 1.980 16.621 25.256 1.00 13.33 ATOM 454 CD1 ILE A 58 -0.440 16.713 23.315 1.00 12.00 ATOM 455 N ASN A 59 4.802 18.322 25.219 1.00 12.31 ATOM 456 CA ASN A 59 6.038 18.219 25.988 1.00 13.31 ATOM 457 C ASN A 59 6.086 17.160 27.098 1.00 12.82 ATOM 458 O ASN A 59 5.164 17.049 27.921 1.00 13.86 ATOM 459 CB ASN A 59 6.378 19.619 26.511 1.00 13.27 ATOM 460 CG ASN A 59 7.725 19.677 27.156 0.60 12.47 ATOM 461 OD1 ASN A 59 7.823 19.603 28.368 0.60 13.45 ATOM 462 ND2 ASN A 59 8.773 19.792 26.358 0.60 11.68 ATOM 463 N SER A 60 7.201 16.423 27.144 1.00 12.04 ATOM 464 CA SER A 60 7.420 15.362 28.125 1.00 12.68 ATOM 465 C SER A 60 7.713 15.865 29.547 1.00 13.25 ATOM 466 O SER A 60 7.677 15.085 30.498 1.00 14.56 ATOM 467 CB SER A 60 8.561 14.454 27.657 1.00 11.12 ATOM 468 OG SER A 60 9.794 15.157 27.647 1.00 10.97 ATOM 469 N ARG A 61 8.027 17.151 29.683 1.00 15.55 ATOM 470 CA ARG A 61 8.310 17.749 30.993 1.00 18.96 ATOM 471 C ARG A 61 7.070 17.708 31.877 1.00 19.09 ATOM 472 O ARG A 61 7.177 17.516 33.093 1.00 19.40 ATOM 473 CB ARG A 61 8.785 19.202 30.829 1.00 21.73 ATOM 474 CG ARG A 61 8.944 20.011 32.108 1.00 28.83 ATOM 475 CD ARG A 61 10.148 19.577 32.931 1.00 34.29 ATOM 476 NE ARG A 61 11.411 19.688 32.193 1.00 38.44 ATOM 477 CZ ARG A 61 12.490 18.949 32.445 1.00 40.31 ATOM 478 NH1 ARG A 61 12.469 18.041 33.422 1.00 42.44 ATOM 479 NH2 ARG A 61 13.589 19.112 31.720 1.00 40.12 ATOM 480 N TRP A 62 5.891 17.786 31.263 1.00 17.60 ATOM 481 CA TRP A 62 4.660 17.792 32.036 1.00 17.89 ATOM 482 C TRP A 62 3.578 16.830 31.639 1.00 15.84 ATOM 483 O TRP A 62 2.852 16.325 32.488 1.00 16.61 ATOM 484 CB TRP A 62 3.985 19.167 31.945 1.00 21.38 ATOM 485 CG TRP A 62 4.877 20.328 32.129 1.00 27.10 ATOM 486 CD1 TRP A 62 5.433 21.101 31.143 1.00 29.12 ATOM 487 CD2 TRP A 62 5.334 20.856 33.368 1.00 30.06 ATOM 488 NE1 TRP A 62 6.214 22.080 31.707 1.00 31.44 ATOM 489 CE2 TRP A 62 6.174 21.953 33.070 1.00 31.95 ATOM 490 CE3 TRP A 62 5.121 20.507 34.709 1.00 32.47 ATOM 491 CZ2 TRP A 62 6.805 22.711 34.069 1.00 35.33 ATOM 492 CZ3 TRP A 62 5.747 21.257 35.704 1.00 35.27 ATOM 493 CH2 TRP A 62 6.580 22.348 35.377 1.00 36.06 ATOM 494 N TRP A 63 3.512 16.488 30.341 1.00 14.85 ATOM 495 CA TRP A 63 2.264 15.847 29.901 1.00 13.36 ATOM 496 C TRP A 63 2.381 14.361 29.574 1.00 12.94 ATOM 497 O TRP A 63 1.349 13.663 29.581 1.00 13.25 ATOM 498 CB TRP A 63 1.752 16.564 28.679 1.00 13.58 ATOM 499 CG TRP A 63 1.642 18.055 28.963 1.00 13.12 ATOM 500 CD1 TRP A 63 2.467 19.017 28.521 1.00 13.22 ATOM 501 CD2 TRP A 63 0.635 18.669 29.765 1.00 13.06 ATOM 502 NE1 TRP A 63 2.005 20.253 29.044 1.00 13.99 ATOM 503 CE2 TRP A 63 0.920 20.033 29.783 1.00 13.92 ATOM 504 CE3 TRP A 63 -0.482 18.188 30.477 1.00 14.71 ATOM 505 CZ2 TRP A 63 0.140 20.966 30.495 1.00 13.93 ATOM 506 CZ3 TRP A 63 -1.256 19.130 31.183 1.00 14.08 ATOM 507 CH2 TRP A 63 -0.955 20.463 31.191 1.00 14.50 ATOM 508 N CYS A 64 3.543 13.817 29.270 1.00 12.89 ATOM 509 CA CYS A 64 3.643 12.409 28.949 1.00 12.23 ATOM 510 C CYS A 64 4.958 11.870 29.478 1.00 12.59 ATOM 511 O CYS A 64 5.878 12.633 29.806 1.00 12.56 ATOM 512 CB CYS A 64 3.527 12.194 27.435 1.00 11.52 ATOM 513 SG CYS A 64 4.830 13.015 26.447 1.00 11.13 ATOM 514 N ASN A 65 5.024 10.553 29.595 1.00 12.38 ATOM 515 CA ASN A 65 6.219 9.901 30.088 1.00 13.32 ATOM 516 C ASN A 65 7.053 9.294 28.961 1.00 12.06 ATOM 517 O ASN A 65 6.545 8.467 28.195 1.00 11.74 ATOM 518 CB ASN A 65 5.850 8.794 31.078 1.00 14.47 ATOM 519 CG ASN A 65 7.080 8.142 31.696 1.00 18.78 ATOM 520 OD1 ASN A 65 8.044 8.828 32.058 1.00 20.93 ATOM 521 ND2 ASN A 65 7.072 6.819 31.787 1.00 23.44 ATOM 522 N ASP A 66 8.310 9.721 28.842 1.00 10.62 ATOM 523 CA ASP A 66 9.192 9.145 27.838 1.00 10.53 ATOM 524 C ASP A 66 10.367 8.420 28.474 1.00 11.72 ATOM 525 O ASP A 66 11.277 7.968 27.786 1.00 12.86 ATOM 526 CB ASP A 66 9.673 10.181 26.824 1.00 10.93 ATOM 527 CG ASP A 66 10.513 11.287 27.433 1.00 9.90 ATOM 528 OD1 ASP A 66 10.837 11.271 28.642 1.00 11.50 ATOM 529 OD2 ASP A 66 10.843 12.214 26.669 1.00 11.14 ATOM 530 N GLY A 67 10.339 8.319 29.796 1.00 13.28 ATOM 531 CA GLY A 67 11.393 7.640 30.518 1.00 14.79 ATOM 532 C GLY A 67 12.751 8.320 30.538 1.00 16.79 ATOM 533 O GLY A 67 13.710 7.734 31.047 1.00 19.34 ATOM 534 N ARG A 68 12.861 9.542 30.021 1.00 14.67 ATOM 535 CA ARG A 68 14.153 10.219 30.017 1.00 15.96 ATOM 536 C ARG A 68 14.094 11.716 30.297 1.00 16.42 ATOM 537 O ARG A 68 14.949 12.479 29.825 1.00 18.56 ATOM 538 CB ARG A 68 14.877 9.979 28.697 1.00 16.01 ATOM 539 CG ARG A 68 14.207 10.623 27.513 1.00 16.77 ATOM 540 CD ARG A 68 15.172 10.676 26.368 1.00 18.38 ATOM 541 NE ARG A 68 14.747 11.614 25.343 1.00 19.34 ATOM 542 CZ ARG A 68 15.198 11.598 24.090 1.00 21.03 ATOM 543 NH1 ARG A 68 16.100 10.683 23.726 1.00 22.09 ATOM 544 NH2 ARG A 68 14.750 12.490 23.205 1.00 18.80 ATOM 545 N THR A 69 13.100 12.144 31.058 1.00 15.95 ATOM 546 CA THR A 69 12.973 13.550 31.410 1.00 15.73 ATOM 547 C THR A 69 12.854 13.543 32.933 1.00 18.25 ATOM 548 O THR A 69 11.754 13.521 33.483 1.00 18.98 ATOM 549 CB THR A 69 11.710 14.185 30.775 1.00 14.99 ATOM 550 OG1 THR A 69 11.670 13.875 29.374 1.00 13.15 ATOM 551 CG2 THR A 69 11.721 15.697 30.953 1.00 13.34 ATOM 552 N PRO A 70 13.991 13.446 33.630 1.00 20.66 ATOM 553 CA PRO A 70 14.054 13.418 35.093 1.00 22.70 ATOM 554 C PRO A 70 13.197 14.479 35.754 1.00 24.41 ATOM 555 O PRO A 70 13.196 15.646 35.341 1.00 25.64 ATOM 556 CB PRO A 70 15.525 13.670 35.359 1.00 23.89 ATOM 557 CG PRO A 70 16.175 12.939 34.221 1.00 23.95 ATOM 558 CD PRO A 70 15.340 13.377 33.047 1.00 21.45 ATOM 559 N GLY A 71 12.442 14.050 36.758 1.00 26.11 ATOM 560 CA GLY A 71 11.579 14.964 37.484 1.00 27.95 ATOM 561 C GLY A 71 10.475 15.589 36.647 1.00 28.58 ATOM 562 O GLY A 71 10.124 16.751 36.853 1.00 31.57 ATOM 563 N SER A 72 9.970 14.850 35.673 1.00 27.25 ATOM 564 CA SER A 72 8.899 15.352 34.833 1.00 26.60 ATOM 565 C SER A 72 7.588 14.724 35.297 1.00 26.38 ATOM 566 O SER A 72 7.574 13.711 36.006 1.00 26.04 ATOM 567 CB SER A 72 9.153 15.016 33.361 1.00 26.71 ATOM 568 OG SER A 72 8.970 13.632 33.096 1.00 26.87 ATOM 569 N ARG A 73 6.491 15.364 34.931 1.00 25.01 ATOM 570 CA ARG A 73 5.176 14.875 35.289 1.00 24.81 ATOM 571 C ARG A 73 4.638 14.167 34.062 1.00 22.85 ATOM 572 O ARG A 73 5.227 14.235 32.969 1.00 23.08 ATOM 573 CB ARG A 73 4.263 16.038 35.684 1.00 27.11 ATOM 574 CG ARG A 73 4.716 16.773 36.942 1.00 32.46 ATOM 575 CD ARG A 73 3.880 16.377 38.161 1.00 38.66 ATOM 576 NE ARG A 73 2.615 17.120 38.225 1.00 43.30 ATOM 577 CZ ARG A 73 1.599 16.826 39.039 1.00 45.78 ATOM 578 NH1 ARG A 73 1.673 15.791 39.871 1.00 45.60 ATOM 579 NH2 ARG A 73 0.501 17.573 39.023 1.00 47.05 ATOM 580 N ASN A 74 3.542 13.454 34.253 1.00 19.91 ATOM 581 CA ASN A 74 2.888 12.726 33.181 1.00 18.07 ATOM 582 C ASN A 74 1.409 13.025 33.383 1.00 16.98 ATOM 583 O ASN A 74 0.603 12.129 33.625 1.00 16.26 ATOM 584 CB ASN A 74 3.170 11.228 33.306 1.00 17.12 ATOM 585 CG ASN A 74 2.523 10.415 32.203 1.00 16.21 ATOM 586 OD1 ASN A 74 1.913 10.959 31.286 1.00 16.86 ATOM 587 ND2 ASN A 74 2.633 9.100 32.304 1.00 16.39 ATOM 588 N LEU A 75 1.068 14.305 33.283 1.00 16.89 ATOM 589 CA LEU A 75 -0.303 14.754 33.494 1.00 16.97 ATOM 590 C LEU A 75 -1.351 14.135 32.585 1.00 16.37 ATOM 591 O LEU A 75 -2.513 14.034 32.972 1.00 18.12 ATOM 592 CB LEU A 75 -0.376 16.281 33.469 1.00 18.64 ATOM 593 CG LEU A 75 0.406 16.917 34.620 1.00 20.53 ATOM 594 CD1 LEU A 75 0.425 18.435 34.496 1.00 21.00 ATOM 595 CD2 LEU A 75 -0.229 16.483 35.941 1.00 22.48 ATOM 596 N CYS A 76 -0.963 13.700 31.394 1.00 15.03 ATOM 597 CA CYS A 76 -1.929 13.063 30.512 1.00 14.77 ATOM 598 C CYS A 76 -1.965 11.555 30.715 1.00 15.66 ATOM 599 O CYS A 76 -2.769 10.861 30.096 1.00 15.99 ATOM 600 CB CYS A 76 -1.659 13.406 29.048 1.00 14.03 ATOM 601 SG CYS A 76 -2.078 15.137 28.693 1.00 14.62 ATOM 602 N ASN A 77 -1.082 11.049 31.567 1.00 16.88 ATOM 603 CA ASN A 77 -1.026 9.623 31.862 1.00 19.32 ATOM 604 C ASN A 77 -0.882 8.745 30.646 1.00 18.27 ATOM 605 O ASN A 77 -1.657 7.808 30.434 1.00 17.31 ATOM 606 CB ASN A 77 -2.254 9.189 32.653 1.00 24.82 ATOM 607 CG ASN A 77 -1.954 9.057 34.116 1.00 31.15 ATOM 608 OD1 ASN A 77 -1.164 8.190 34.520 1.00 35.64 ATOM 609 ND2 ASN A 77 -2.527 9.943 34.923 1.00 33.62 ATOM 610 N ILE A 78 0.134 9.037 29.849 1.00 16.63 ATOM 611 CA ILE A 78 0.382 8.267 28.643 1.00 17.42 ATOM 612 C ILE A 78 1.850 8.287 28.273 1.00 15.92 ATOM 613 O ILE A 78 2.595 9.192 28.671 1.00 14.28 ATOM 614 CB ILE A 78 -0.332 8.856 27.380 1.00 17.73 ATOM 615 CG1 ILE A 78 -0.091 10.365 27.292 1.00 19.40 ATOM 616 CG2 ILE A 78 -1.785 8.439 27.311 1.00 19.99 ATOM 617 CD1 ILE A 78 -0.387 10.960 25.930 1.00 21.82 ATOM 618 N PRO A 79 2.314 7.219 27.610 1.00 15.02 ATOM 619 CA PRO A 79 3.720 7.225 27.206 1.00 14.04 ATOM 620 C PRO A 79 3.736 8.220 26.035 1.00 12.15 ATOM 621 O PRO A 79 2.757 8.330 25.284 1.00 11.36 ATOM 622 CB PRO A 79 3.956 5.787 26.738 1.00 14.78 ATOM 623 CG PRO A 79 2.582 5.294 26.342 1.00 17.53 ATOM 624 CD PRO A 79 1.691 5.900 27.396 1.00 16.32 ATOM 625 N CYS A 80 4.807 8.985 25.911 1.00 10.92 ATOM 626 CA CYS A 80 4.888 9.966 24.838 1.00 10.10 ATOM 627 C CYS A 80 4.757 9.320 23.462 1.00 10.86 ATOM 628 O CYS A 80 4.253 9.944 22.515 1.00 11.57 ATOM 629 CB CYS A 80 6.188 10.756 24.942 1.00 9.50 ATOM 630 SG CYS A 80 6.354 11.676 26.504 1.00 10.22 ATOM 631 N SER A 81 5.174 8.063 23.351 1.00 10.65 ATOM 632 CA SER A 81 5.079 7.357 22.080 1.00 12.62 ATOM 633 C SER A 81 3.634 7.292 21.574 1.00 12.61 ATOM 634 O SER A 81 3.399 7.293 20.363 1.00 13.63 ATOM 635 CB SER A 81 5.656 5.951 22.205 1.00 12.42 ATOM 636 OG SER A 81 4.979 5.228 23.213 1.00 15.19 ATOM 637 N ALA A 82 2.666 7.281 22.489 1.00 12.80 ATOM 638 CA ALA A 82 1.246 7.245 22.106 1.00 14.49 ATOM 639 C ALA A 82 0.873 8.479 21.275 1.00 14.62 ATOM 640 O ALA A 82 -0.052 8.440 20.445 1.00 15.98 ATOM 641 CB ALA A 82 0.366 7.162 23.347 1.00 14.40 ATOM 642 N LEU A 83 1.611 9.566 21.481 1.00 12.74 ATOM 643 CA LEU A 83 1.381 10.816 20.777 1.00 13.12 ATOM 644 C LEU A 83 1.894 10.840 19.339 1.00 12.97 ATOM 645 O LEU A 83 1.696 11.826 18.633 1.00 14.41 ATOM 646 CB LEU A 83 2.023 11.961 21.562 1.00 12.67 ATOM 647 CG LEU A 83 1.474 12.134 22.975 1.00 14.90 ATOM 648 CD1 LEU A 83 2.310 13.160 23.734 1.00 15.18 ATOM 649 CD2 LEU A 83 0.004 12.538 22.910 1.00 14.31 ATOM 650 N LEU A 84 2.521 9.759 18.885 1.00 12.83 ATOM 651 CA LEU A 84 3.062 9.720 17.536 1.00 12.53 ATOM 652 C LEU A 84 2.231 8.876 16.598 1.00 13.86 ATOM 653 O LEU A 84 2.524 8.797 15.394 1.00 14.90 ATOM 654 CB LEU A 84 4.497 9.170 17.553 1.00 13.21 ATOM 655 CG LEU A 84 5.470 9.907 18.481 1.00 14.73 ATOM 656 CD1 LEU A 84 6.822 9.236 18.416 1.00 16.65 ATOM 657 CD2 LEU A 84 5.600 11.360 18.063 1.00 13.66 ATOM 658 N SER A 85 1.196 8.252 17.154 1.00 14.76 ATOM 659 CA SER A 85 0.279 7.391 16.406 1.00 14.93 ATOM 660 C SER A 85 -0.436 8.089 15.259 1.00 14.90 ATOM 661 O SER A 85 -0.653 9.290 15.300 1.00 14.93 ATOM 662 CB SER A 85 -0.773 6.816 17.359 1.00 14.94 ATOM 663 OG SER A 85 -1.758 6.100 16.637 1.00 18.96 ATOM 664 N SER A 86 -0.809 7.326 14.240 1.00 15.54 ATOM 665 CA SER A 86 -1.547 7.873 13.115 1.00 15.99 ATOM 666 C SER A 86 -2.946 8.260 13.583 1.00 16.76 ATOM 667 O SER A 86 -3.623 9.066 12.956 1.00 18.90 ATOM 668 CB SER A 86 -1.609 6.843 11.983 0.50 15.96 ATOM 669 OG SER A 86 -2.018 5.580 12.449 0.50 14.50 ATOM 670 N ASP A 87 -3.365 7.685 14.703 1.00 17.23 ATOM 671 CA ASP A 87 -4.663 7.964 15.313 1.00 17.67 ATOM 672 C ASP A 87 -4.371 9.124 16.264 1.00 16.66 ATOM 673 O ASP A 87 -3.579 8.983 17.200 1.00 16.78 ATOM 674 CB ASP A 87 -5.135 6.745 16.108 1.00 19.69 ATOM 675 CG ASP A 87 -6.560 6.898 16.639 1.00 23.88 ATOM 676 OD1 ASP A 87 -6.963 8.023 16.976 1.00 23.56 ATOM 677 OD2 ASP A 87 -7.291 5.890 16.696 1.00 27.63 ATOM 678 N ILE A 88 -5.010 10.265 16.036 1.00 15.47 ATOM 679 CA ILE A 88 -4.749 11.446 16.861 1.00 13.80 ATOM 680 C ILE A 88 -5.473 11.510 18.189 1.00 13.36 ATOM 681 O ILE A 88 -5.298 12.466 18.939 1.00 12.60 ATOM 682 CB ILE A 88 -5.016 12.759 16.099 1.00 14.07 ATOM 683 CG1 ILE A 88 -6.509 12.912 15.778 1.00 13.80 ATOM 684 CG2 ILE A 88 -4.150 12.810 14.830 1.00 14.79 ATOM 685 CD1 ILE A 88 -6.860 14.235 15.150 1.00 15.66 ATOM 686 N THR A 89 -6.282 10.507 18.495 1.00 13.19 ATOM 687 CA THR A 89 -7.034 10.504 19.740 1.00 13.53 ATOM 688 C THR A 89 -6.229 10.884 20.991 1.00 13.15 ATOM 689 O THR A 89 -6.648 11.755 21.757 1.00 13.37 ATOM 690 CB THR A 89 -7.728 9.147 19.945 1.00 14.76 ATOM 691 OG1 THR A 89 -8.570 8.880 18.827 1.00 16.97 ATOM 692 CG2 THR A 89 -8.583 9.180 21.181 1.00 16.63 ATOM 693 N ALA A 90 -5.079 10.253 21.200 1.00 11.72 ATOM 694 CA ALA A 90 -4.281 10.539 22.391 1.00 12.59 ATOM 695 C ALA A 90 -3.818 11.981 22.381 1.00 12.13 ATOM 696 O ALA A 90 -3.863 12.650 23.415 1.00 13.81 ATOM 697 CB ALA A 90 -3.081 9.590 22.484 1.00 12.59 ATOM 698 N SER A 91 -3.350 12.451 21.227 1.00 10.91 ATOM 699 CA SER A 91 -2.891 13.835 21.107 1.00 11.30 ATOM 700 C SER A 91 -4.018 14.827 21.420 1.00 11.49 ATOM 701 O SER A 91 -3.828 15.808 22.148 1.00 11.81 ATOM 702 CB SER A 91 -2.315 14.095 19.709 1.00 11.03 ATOM 703 OG SER A 91 -0.981 13.623 19.623 1.00 12.25 ATOM 704 N VAL A 92 -5.198 14.556 20.882 1.00 11.69 ATOM 705 CA VAL A 92 -6.339 15.425 21.113 1.00 12.56 ATOM 706 C VAL A 92 -6.766 15.420 22.580 1.00 13.16 ATOM 707 O VAL A 92 -6.981 16.484 23.162 1.00 13.01 ATOM 708 CB VAL A 92 -7.520 15.041 20.200 1.00 14.13 ATOM 709 CG1 VAL A 92 -8.793 15.819 20.609 1.00 15.03 ATOM 710 CG2 VAL A 92 -7.151 15.338 18.757 1.00 14.65 ATOM 711 N ASN A 93 -6.878 14.238 23.186 1.00 12.31 ATOM 712 CA ASN A 93 -7.283 14.148 24.588 1.00 14.39 ATOM 713 C ASN A 93 -6.320 14.878 25.502 1.00 13.98 ATOM 714 O ASN A 93 -6.739 15.543 26.449 1.00 14.45 ATOM 715 CB ASN A 93 -7.415 12.694 25.048 1.00 17.41 ATOM 716 CG ASN A 93 -8.573 11.976 24.378 1.00 22.45 ATOM 717 OD1 ASN A 93 -9.461 12.609 23.801 1.00 22.91 ATOM 718 ND2 ASN A 93 -8.565 10.639 24.450 1.00 24.80 ATOM 719 N CYS A 94 -5.028 14.748 25.225 1.00 12.45 ATOM 720 CA CYS A 94 -4.029 15.419 26.033 1.00 11.63 ATOM 721 C CYS A 94 -4.070 16.927 25.778 1.00 11.22 ATOM 722 O CYS A 94 -3.972 17.722 26.711 1.00 11.31 ATOM 723 CB CYS A 94 -2.649 14.848 25.730 1.00 12.21 ATOM 724 SG CYS A 94 -1.336 15.446 26.832 1.00 13.98 ATOM 725 N ALA A 95 -4.251 17.320 24.517 1.00 11.06 ATOM 726 CA ALA A 95 -4.324 18.735 24.152 1.00 10.91 ATOM 727 C ALA A 95 -5.489 19.411 24.893 1.00 11.63 ATOM 728 O ALA A 95 -5.393 20.566 25.303 1.00 12.10 ATOM 729 CB ALA A 95 -4.487 18.888 22.651 1.00 10.27 ATOM 730 N LYS A 96 -6.591 18.691 25.068 1.00 12.04 ATOM 731 CA LYS A 96 -7.735 19.243 25.783 1.00 12.85 ATOM 732 C LYS A 96 -7.346 19.579 27.218 1.00 13.35 ATOM 733 O LYS A 96 -7.781 20.583 27.751 1.00 15.40 ATOM 734 CB LYS A 96 -8.903 18.251 25.773 1.00 13.82 ATOM 735 CG LYS A 96 -9.578 18.141 24.429 1.00 14.05 ATOM 736 CD LYS A 96 -10.698 17.122 24.451 1.00 16.31 ATOM 737 CE LYS A 96 -11.324 17.021 23.063 1.00 18.36 ATOM 738 NZ LYS A 96 -12.267 15.881 22.934 1.00 18.93 ATOM 739 N LYS A 97 -6.534 18.737 27.849 1.00 13.79 ATOM 740 CA LYS A 97 -6.117 19.007 29.226 1.00 15.84 ATOM 741 C LYS A 97 -5.184 20.212 29.260 1.00 14.71 ATOM 742 O LYS A 97 -5.279 21.067 30.134 1.00 14.56 ATOM 743 CB LYS A 97 -5.409 17.796 29.850 1.00 18.79 ATOM 744 CG LYS A 97 -6.302 16.573 30.037 1.00 25.83 ATOM 745 CD LYS A 97 -5.646 15.529 30.938 1.00 29.52 ATOM 746 CE LYS A 97 -6.530 14.279 31.090 1.00 32.80 ATOM 747 NZ LYS A 97 -6.720 13.515 29.816 1.00 34.72 ATOM 748 N ILE A 98 -4.276 20.272 28.295 1.00 12.66 ATOM 749 CA ILE A 98 -3.315 21.371 28.222 1.00 12.46 ATOM 750 C ILE A 98 -4.020 22.717 28.059 1.00 11.57 ATOM 751 O ILE A 98 -3.788 23.628 28.828 1.00 11.64 ATOM 752 CB ILE A 98 -2.292 21.151 27.051 1.00 12.77 ATOM 753 CG1 ILE A 98 -1.459 19.890 27.302 1.00 11.74 ATOM 754 CG2 ILE A 98 -1.383 22.366 26.873 1.00 10.79 ATOM 755 CD1 ILE A 98 -0.588 19.510 26.136 1.00 11.33 ATOM 756 N VAL A 99 -4.923 22.816 27.096 1.00 12.30 ATOM 757 CA VAL A 99 -5.616 24.067 26.832 1.00 13.12 ATOM 758 C VAL A 99 -6.550 24.508 27.971 1.00 16.42 ATOM 759 O VAL A 99 -6.960 25.673 28.033 1.00 16.19 ATOM 760 CB VAL A 99 -6.366 24.006 25.482 1.00 12.64 ATOM 761 CG1 VAL A 99 -7.608 23.132 25.591 1.00 12.40 ATOM 762 CG2 VAL A 99 -6.703 25.393 25.000 1.00 13.89 ATOM 763 N SER A 100 -6.871 23.582 28.870 1.00 17.46 ATOM 764 CA SER A 100 -7.726 23.877 30.017 1.00 21.00 ATOM 765 C SER A 100 -6.870 24.265 31.224 1.00 23.39 ATOM 766 O SER A 100 -7.390 24.703 32.249 1.00 25.23 ATOM 767 CB SER A 100 -8.549 22.646 30.373 1.00 18.66 ATOM 768 OG SER A 100 -9.430 22.309 29.324 1.00 21.02 ATOM 769 N ASP A 101 -5.558 24.118 31.067 1.00 26.52 ATOM 770 CA ASP A 101 -4.554 24.379 32.096 1.00 28.88 ATOM 771 C ASP A 101 -4.454 25.812 32.611 1.00 29.40 ATOM 772 O ASP A 101 -3.757 26.072 33.595 1.00 30.68 ATOM 773 CB ASP A 101 -3.194 23.936 31.562 1.00 31.42 ATOM 774 CG ASP A 101 -2.164 23.784 32.642 1.00 36.61 ATOM 775 OD1 ASP A 101 -2.441 23.077 33.639 1.00 38.56 ATOM 776 OD2 ASP A 101 -1.057 24.348 32.474 1.00 39.69 ATOM 777 N GLY A 102 -5.110 26.753 31.941 1.00 29.00 ATOM 778 CA GLY A 102 -5.046 28.134 32.403 1.00 27.72 ATOM 779 C GLY A 102 -4.479 29.153 31.428 1.00 26.86 ATOM 780 O GLY A 102 -4.918 30.313 31.440 1.00 27.10 ATOM 781 N ASN A 103 -3.516 28.752 30.594 1.00 24.06 ATOM 782 CA ASN A 103 -2.935 29.679 29.621 1.00 21.43 ATOM 783 C ASN A 103 -3.519 29.515 28.225 1.00 17.05 ATOM 784 O ASN A 103 -3.088 30.173 27.277 1.00 15.51 ATOM 785 CB ASN A 103 -1.424 29.531 29.580 1.00 26.15 ATOM 786 CG ASN A 103 -0.804 29.724 30.937 1.00 31.78 ATOM 787 OD1 ASN A 103 -0.893 30.807 31.520 1.00 34.10 ATOM 788 ND2 ASN A 103 -0.217 28.659 31.484 1.00 33.86 ATOM 789 N GLY A 104 -4.511 28.647 28.105 1.00 14.35 ATOM 790 CA GLY A 104 -5.141 28.428 26.822 1.00 13.38 ATOM 791 C GLY A 104 -4.154 27.915 25.789 1.00 12.58 ATOM 792 O GLY A 104 -3.222 27.184 26.110 1.00 13.41 ATOM 793 N MET A 105 -4.317 28.354 24.547 1.00 11.47 ATOM 794 CA MET A 105 -3.437 27.891 23.483 1.00 10.45 ATOM 795 C MET A 105 -2.062 28.522 23.485 1.00 10.76 ATOM 796 O MET A 105 -1.207 28.161 22.678 1.00 9.59 ATOM 797 CB MET A 105 -4.108 28.025 22.122 1.00 9.50 ATOM 798 CG MET A 105 -5.170 26.955 21.903 1.00 9.98 ATOM 799 SD MET A 105 -5.687 26.815 20.194 1.00 11.98 ATOM 800 CE MET A 105 -4.293 25.878 19.516 1.00 12.53 ATOM 801 N ASN A 106 -1.845 29.466 24.397 1.00 11.19 ATOM 802 CA ASN A 106 -0.541 30.116 24.509 1.00 11.66 ATOM 803 C ASN A 106 0.508 29.090 24.920 1.00 11.33 ATOM 804 O ASN A 106 1.706 29.347 24.786 1.00 12.07 ATOM 805 CB ASN A 106 -0.580 31.289 25.488 1.00 11.51 ATOM 806 CG ASN A 106 -1.429 32.438 24.973 1.00 12.32 ATOM 807 OD1 ASN A 106 -1.116 33.062 23.945 1.00 12.90 ATOM 808 ND2 ASN A 106 -2.528 32.704 25.662 1.00 13.37 ATOM 809 N ALA A 107 0.046 27.926 25.392 1.00 11.49 ATOM 810 CA ALA A 107 0.933 26.830 25.774 1.00 11.72 ATOM 811 C ALA A 107 1.733 26.354 24.551 1.00 12.37 ATOM 812 O ALA A 107 2.809 25.766 24.689 1.00 14.97 ATOM 813 CB ALA A 107 0.127 25.685 26.352 1.00 12.50 ATOM 814 N TRP A 108 1.193 26.586 23.358 1.00 10.58 ATOM 815 CA TRP A 108 1.861 26.215 22.113 1.00 10.77 ATOM 816 C TRP A 108 2.537 27.453 21.556 1.00 11.45 ATOM 817 O TRP A 108 1.876 28.367 21.055 1.00 10.55 ATOM 818 CB TRP A 108 0.872 25.642 21.099 1.00 10.66 ATOM 819 CG TRP A 108 0.459 24.255 21.456 1.00 10.57 ATOM 820 CD1 TRP A 108 1.149 23.104 21.183 1.00 10.72 ATOM 821 CD2 TRP A 108 -0.724 23.858 22.158 1.00 9.61 ATOM 822 NE1 TRP A 108 0.463 22.023 21.665 1.00 10.63 ATOM 823 CE2 TRP A 108 -0.691 22.452 22.265 1.00 10.63 ATOM 824 CE3 TRP A 108 -1.810 24.552 22.708 1.00 10.13 ATOM 825 CZ2 TRP A 108 -1.702 21.719 22.907 1.00 9.41 ATOM 826 CZ3 TRP A 108 -2.816 23.822 23.348 1.00 10.10 ATOM 827 CH2 TRP A 108 -2.751 22.420 23.436 1.00 9.14 ATOM 828 N VAL A 109 3.863 27.461 21.628 1.00 12.11 ATOM 829 CA VAL A 109 4.647 28.596 21.171 1.00 12.51 ATOM 830 C VAL A 109 4.386 28.976 19.708 1.00 11.98 ATOM 831 O VAL A 109 4.225 30.162 19.399 1.00 12.63 ATOM 832 CB VAL A 109 6.169 28.333 21.368 0.52 13.76 ATOM 833 CG1 VAL A 109 6.992 29.504 20.830 0.52 14.99 ATOM 834 CG2 VAL A 109 6.475 28.104 22.845 0.52 13.71 ATOM 835 N ALA A 110 4.271 27.991 18.823 1.00 12.24 ATOM 836 CA ALA A 110 4.029 28.298 17.414 1.00 12.15 ATOM 837 C ALA A 110 2.646 28.914 17.221 1.00 11.62 ATOM 838 O ALA A 110 2.451 29.742 16.342 1.00 12.10 ATOM 839 CB ALA A 110 4.192 27.059 16.545 1.00 12.77 ATOM 840 N TRP A 111 1.679 28.493 18.028 1.00 11.10 ATOM 841 CA TRP A 111 0.346 29.064 17.919 1.00 9.78 ATOM 842 C TRP A 111 0.426 30.532 18.325 1.00 10.54 ATOM 843 O TRP A 111 -0.095 31.413 17.633 1.00 9.84 ATOM 844 CB TRP A 111 -0.661 28.353 18.827 1.00 8.55 ATOM 845 CG TRP A 111 -1.997 29.024 18.771 1.00 8.60 ATOM 846 CD1 TRP A 111 -2.944 28.886 17.792 1.00 10.22 ATOM 847 CD2 TRP A 111 -2.511 30.003 19.687 1.00 9.43 ATOM 848 NE1 TRP A 111 -4.007 29.722 18.038 1.00 9.55 ATOM 849 CE2 TRP A 111 -3.773 30.413 19.196 1.00 8.80 ATOM 850 CE3 TRP A 111 -2.032 30.572 20.882 1.00 9.16 ATOM 851 CZ2 TRP A 111 -4.559 31.365 19.856 1.00 9.82 ATOM 852 CZ3 TRP A 111 -2.816 31.514 21.537 1.00 9.24 ATOM 853 CH2 TRP A 111 -4.064 31.901 21.019 1.00 9.18 ATOM 854 N ARG A 112 1.068 30.791 19.457 1.00 10.37 ATOM 855 CA ARG A 112 1.195 32.150 19.950 1.00 12.97 ATOM 856 C ARG A 112 1.924 33.065 18.952 1.00 12.98 ATOM 857 O ARG A 112 1.482 34.185 18.669 1.00 13.20 ATOM 858 CB ARG A 112 1.947 32.143 21.277 1.00 15.14 ATOM 859 CG ARG A 112 1.786 33.417 22.056 1.00 22.83 ATOM 860 CD ARG A 112 2.788 33.489 23.193 1.00 28.76 ATOM 861 NE ARG A 112 3.030 32.168 23.765 1.00 34.42 ATOM 862 CZ ARG A 112 4.238 31.641 23.932 1.00 36.49 ATOM 863 NH1 ARG A 112 5.317 32.335 23.571 1.00 36.88 ATOM 864 NH2 ARG A 112 4.365 30.415 24.428 1.00 37.65 ATOM 865 N ASN A 113 3.005 32.561 18.374 1.00 11.96 ATOM 866 CA ASN A 113 3.792 33.363 17.455 1.00 12.28 ATOM 867 C ASN A 113 3.349 33.404 16.018 1.00 11.88 ATOM 868 O ASN A 113 3.635 34.378 15.324 1.00 12.86 ATOM 869 CB ASN A 113 5.252 32.926 17.511 1.00 11.92 ATOM 870 CG ASN A 113 5.892 33.255 18.836 1.00 12.85 ATOM 871 OD1 ASN A 113 5.539 34.253 19.466 1.00 14.71 ATOM 872 ND2 ASN A 113 6.824 32.427 19.272 1.00 12.40 ATOM 873 N ARG A 114 2.593 32.406 15.579 1.00 11.23 ATOM 874 CA ARG A 114 2.209 32.327 14.182 1.00 12.02 ATOM 875 C ARG A 114 0.732 32.200 13.848 1.00 12.65 ATOM 876 O ARG A 114 0.355 32.384 12.694 1.00 14.37 ATOM 877 CB ARG A 114 2.990 31.181 13.548 1.00 11.74 ATOM 878 CG ARG A 114 4.476 31.272 13.875 1.00 12.79 ATOM 879 CD ARG A 114 5.249 30.119 13.327 1.00 12.82 ATOM 880 NE ARG A 114 5.374 30.175 11.875 1.00 13.88 ATOM 881 CZ ARG A 114 6.094 29.306 11.172 1.00 13.81 ATOM 882 NH1 ARG A 114 6.738 28.333 11.802 1.00 13.91 ATOM 883 NH2 ARG A 114 6.161 29.405 9.851 1.00 14.55 ATOM 884 N CYS A 115 -0.098 31.899 14.839 1.00 11.03 ATOM 885 CA CYS A 115 -1.528 31.742 14.605 1.00 10.74 ATOM 886 C CYS A 115 -2.368 32.779 15.312 1.00 11.14 ATOM 887 O CYS A 115 -3.336 33.286 14.748 1.00 12.82 ATOM 888 CB CYS A 115 -1.986 30.368 15.068 1.00 9.77 ATOM 889 SG CYS A 115 -1.085 29.030 14.254 1.00 11.03 ATOM 890 N LYS A 116 -2.022 33.047 16.565 1.00 11.12 ATOM 891 CA LYS A 116 -2.734 34.005 17.397 1.00 11.96 ATOM 892 C LYS A 116 -2.921 35.330 16.679 1.00 13.58 ATOM 893 O LYS A 116 -1.951 35.923 16.189 1.00 13.52 ATOM 894 CB LYS A 116 -1.959 34.239 18.694 1.00 11.59 ATOM 895 CG LYS A 116 -2.724 35.019 19.748 1.00 10.89 ATOM 896 CD LYS A 116 -1.907 35.143 21.029 1.00 11.25 ATOM 897 CE LYS A 116 -2.739 35.716 22.178 1.00 12.12 ATOM 898 NZ LYS A 116 -1.988 35.717 23.474 1.00 13.02 ATOM 899 N GLY A 117 -4.179 35.765 16.608 1.00 16.63 ATOM 900 CA GLY A 117 -4.515 37.032 15.984 1.00 18.20 ATOM 901 C GLY A 117 -4.486 37.071 14.471 1.00 19.75 ATOM 902 O GLY A 117 -4.563 38.151 13.882 1.00 22.16 ATOM 903 N THR A 118 -4.299 35.922 13.831 1.00 18.08 ATOM 904 CA THR A 118 -4.279 35.866 12.376 1.00 16.65 ATOM 905 C THR A 118 -5.634 35.344 11.917 1.00 17.02 ATOM 906 O THR A 118 -6.480 34.981 12.734 1.00 15.42 ATOM 907 CB THR A 118 -3.170 34.918 11.853 1.00 16.90 ATOM 908 OG1 THR A 118 -3.508 33.559 12.162 1.00 15.39 ATOM 909 CG2 THR A 118 -1.809 35.286 12.477 1.00 15.82 ATOM 910 N ASP A 119 -5.851 35.307 10.611 1.00 17.74 ATOM 911 CA ASP A 119 -7.110 34.810 10.091 1.00 19.48 ATOM 912 C ASP A 119 -7.025 33.293 10.091 1.00 18.72 ATOM 913 O ASP A 119 -6.726 32.685 9.062 1.00 19.46 ATOM 914 CB ASP A 119 -7.335 35.327 8.668 1.00 24.27 ATOM 915 CG ASP A 119 -8.622 34.795 8.044 1.00 28.86 ATOM 916 OD1 ASP A 119 -9.612 34.557 8.779 1.00 31.95 ATOM 917 OD2 ASP A 119 -8.636 34.609 6.808 1.00 33.26 ATOM 918 N VAL A 120 -7.298 32.680 11.238 1.00 16.86 ATOM 919 CA VAL A 120 -7.200 31.229 11.354 1.00 16.73 ATOM 920 C VAL A 120 -8.260 30.440 10.594 1.00 17.55 ATOM 921 O VAL A 120 -8.073 29.253 10.318 1.00 16.60 ATOM 922 CB VAL A 120 -7.112 30.760 12.833 1.00 16.21 ATOM 923 CG1 VAL A 120 -5.797 31.224 13.455 1.00 15.89 ATOM 924 CG2 VAL A 120 -8.278 31.281 13.624 1.00 17.06 ATOM 925 N GLN A 121 -9.360 31.092 10.232 1.00 18.39 ATOM 926 CA GLN A 121 -10.423 30.432 9.483 1.00 19.26 ATOM 927 C GLN A 121 -9.878 29.942 8.127 1.00 18.49 ATOM 928 O GLN A 121 -10.363 28.952 7.566 1.00 18.52 ATOM 929 CB GLN A 121 -11.601 31.406 9.295 1.00 23.56 ATOM 930 CG GLN A 121 -12.906 30.781 8.773 1.00 30.73 ATOM 931 CD GLN A 121 -12.936 30.595 7.248 1.00 35.86 ATOM 932 OE1 GLN A 121 -12.496 31.471 6.494 1.00 38.72 ATOM 933 NE2 GLN A 121 -13.482 29.459 6.791 1.00 36.92 ATOM 934 N ALA A 122 -8.849 30.614 7.617 1.00 17.79 ATOM 935 CA ALA A 122 -8.233 30.241 6.347 1.00 16.60 ATOM 936 C ALA A 122 -7.706 28.808 6.358 1.00 17.29 ATOM 937 O ALA A 122 -7.619 28.167 5.312 1.00 16.84 ATOM 938 CB ALA A 122 -7.111 31.194 6.014 1.00 17.47 ATOM 939 N TRP A 123 -7.352 28.298 7.536 1.00 16.19 ATOM 940 CA TRP A 123 -6.838 26.931 7.649 1.00 16.77 ATOM 941 C TRP A 123 -7.886 25.865 7.379 1.00 17.15 ATOM 942 O TRP A 123 -7.558 24.716 7.090 1.00 17.34 ATOM 943 CB TRP A 123 -6.184 26.707 9.017 1.00 15.57 ATOM 944 CG TRP A 123 -4.914 27.451 9.100 1.00 16.00 ATOM 945 CD1 TRP A 123 -4.707 28.655 9.712 1.00 15.58 ATOM 946 CD2 TRP A 123 -3.693 27.122 8.434 1.00 15.77 ATOM 947 NE1 TRP A 123 -3.436 29.104 9.455 1.00 15.14 ATOM 948 CE2 TRP A 123 -2.789 28.183 8.672 1.00 15.83 ATOM 949 CE3 TRP A 123 -3.274 26.036 7.649 1.00 16.29 ATOM 950 CZ2 TRP A 123 -1.492 28.193 8.150 1.00 15.55 ATOM 951 CZ3 TRP A 123 -1.983 26.047 7.125 1.00 16.02 ATOM 952 CH2 TRP A 123 -1.110 27.123 7.382 1.00 16.65 ATOM 953 N ILE A 124 -9.155 26.237 7.467 1.00 17.21 ATOM 954 CA ILE A 124 -10.204 25.270 7.209 1.00 18.26 ATOM 955 C ILE A 124 -11.001 25.624 5.958 1.00 19.22 ATOM 956 O ILE A 124 -11.932 24.905 5.588 1.00 19.00 ATOM 957 CB ILE A 124 -11.132 25.108 8.423 1.00 18.76 ATOM 958 CG1 ILE A 124 -11.747 26.451 8.804 1.00 18.50 ATOM 959 CG2 ILE A 124 -10.347 24.516 9.601 1.00 18.86 ATOM 960 CD1 ILE A 124 -12.844 26.335 9.824 1.00 24.04 ATOM 961 N ARG A 125 -10.591 26.685 5.270 1.00 20.13 ATOM 962 CA ARG A 125 -11.304 27.085 4.067 1.00 23.33 ATOM 963 C ARG A 125 -11.248 25.997 3.007 1.00 22.94 ATOM 964 O ARG A 125 -10.230 25.332 2.839 1.00 23.32 ATOM 965 CB ARG A 125 -10.800 28.435 3.524 1.00 27.58 ATOM 966 CG ARG A 125 -9.342 28.506 3.049 1.00 33.92 ATOM 967 CD ARG A 125 -9.146 27.959 1.642 1.00 39.02 ATOM 968 NE ARG A 125 -7.809 28.194 1.092 1.00 42.84 ATOM 969 CZ ARG A 125 -6.670 27.729 1.608 1.00 43.90 ATOM 970 NH1 ARG A 125 -6.554 27.511 2.911 1.00 44.69 ATOM 971 NH2 ARG A 125 -5.632 27.505 0.822 1.00 45.95 ATOM 972 N GLY A 126 -12.393 25.759 2.377 1.00 23.41 ATOM 973 CA GLY A 126 -12.487 24.762 1.331 1.00 22.97 ATOM 974 C GLY A 126 -12.746 23.353 1.807 1.00 22.82 ATOM 975 O GLY A 126 -13.025 22.463 0.994 1.00 24.18 ATOM 976 N CYS A 127 -12.667 23.125 3.109 1.00 21.83 ATOM 977 CA CYS A 127 -12.878 21.780 3.626 1.00 21.42 ATOM 978 C CYS A 127 -14.340 21.437 3.832 1.00 22.48 ATOM 979 O CYS A 127 -15.145 22.298 4.161 1.00 23.37 ATOM 980 CB CYS A 127 -12.132 21.584 4.945 1.00 19.29 ATOM 981 SG CYS A 127 -10.393 22.107 4.933 1.00 18.84 ATOM 982 N ARG A 128 -14.676 20.169 3.645 1.00 24.51 ATOM 983 CA ARG A 128 -16.035 19.698 3.852 1.00 27.48 ATOM 984 C ARG A 128 -15.978 19.120 5.265 1.00 28.87 ATOM 985 O ARG A 128 -15.402 18.049 5.464 1.00 30.25 ATOM 986 CB ARG A 128 -16.357 18.623 2.810 1.00 29.11 ATOM 987 CG ARG A 128 -17.777 18.068 2.880 1.00 32.94 ATOM 988 CD ARG A 128 -18.132 17.287 1.622 1.00 34.85 ATOM 989 NE ARG A 128 -17.027 16.444 1.173 1.00 39.35 ATOM 990 CZ ARG A 128 -16.581 16.395 -0.082 1.00 41.19 ATOM 991 NH1 ARG A 128 -17.152 17.138 -1.028 1.00 42.18 ATOM 992 NH2 ARG A 128 -15.547 15.615 -0.388 1.00 43.01 ATOM 993 N LEU A 129 -16.511 19.851 6.245 1.00 30.47 ATOM 994 CA LEU A 129 -16.455 19.422 7.653 1.00 32.89 ATOM 995 C LEU A 129 -17.697 18.776 8.286 1.00 34.37 ATOM 996 O LEU A 129 -17.702 17.538 8.421 1.00 35.24 ATOM 997 CB LEU A 129 -15.978 20.569 8.554 1.00 32.71 ATOM 998 CG LEU A 129 -14.497 20.939 8.679 1.00 33.56 ATOM 999 CD1 LEU A 129 -13.643 19.702 8.604 1.00 33.22 ATOM 1000 CD2 LEU A 129 -14.106 21.920 7.613 1.00 35.05 ATOM 1001 OXT LEU A 129 -18.621 19.504 8.723 1.00 35.18 TER 1002 LEU A 129 HETATM 1003 CL CL A 130 -8.436 30.896 26.764 1.00 21.43 HETATM 1004 NA NA A 131 7.238 13.287 31.697 1.00 20.97 CONECT 1004 466 568 572 SPDBVT 0.9993997812 -0.0318865068 -0.0135378586 SPDBVT 0.0320954882 0.9993644357 0.0155109940 SPDBVT 0.0130346632 -0.0159361884 0.9997880459 SPDBVT -0.6729249954 20.4601001740 18.9810924530 SPDBVT -1.3507167101 19.8263416290 19.2501831055 SPDBVV default; SPDBVV 16.035906410723 2404.623491517909 20.000000000000 SPDBVV -0.6005035792 -0.4588317819 0.6548807886 SPDBVV -0.7611170224 0.0769000994 -0.6440397915 SPDBVV 0.2451455274 -0.8851891157 -0.3954034645 SPDBVV 1.1950000525 22.8390007019 17.3005008698 SPDBVV 0.0000000000 0.0000000000 0.0000000000 SPDBVf 32 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 SPDBVf 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 SPDBVf 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 SPDBVf 48 48 48 48 48 48 48 48 48 32 32 32 32 48 48 48 48 48 48 48 SPDBVf 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 SPDBVf 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 SPDBVf 48 48 48 48 48 48 32 32 32 32 32 32 SPDBVo 1004d NA SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 SPDBVb 0.00 0.00 0.20 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 SPDBVi 2 1 1 0 1 0 1 1 0 1 0 1 1 0 0 SPDBVp 9031 END