HEADER HYDROLASE 06-DEC-05 2C8O TITLE LYSOZYME (1SEC) AND UV LASR EXCITED FLUORESCENCE COMPND MOL_ID: 1; COMPND 2 MOLECULE: LYSOZYME C; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: 1,4-BETA-N-ACETYLMURAMIDASE C, ALLERGEN GAL D 4, COMPND 5 GAL D IV; COMPND 6 EC: 3.2.1.17 SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 ORGANISM_SCIENTIFIC: GALLUS GALLUS; SOURCE 4 ORGANISM_COMMON: CHICKEN; SOURCE 5 ORGANISM_TAXID: 9031; SOURCE 6 CELL_LINE: WHITE EGG; SOURCE 7 OTHER_DETAILS: SIGMA-ALDRICH KEYWDS LASER, UV, VISUALISATION, HYDROLASE, ALLERGEN, KEYWDS 2 ANTIMICROBIAL, BACTERIOLYTIC ENZYME EXPDTA X-RAY DIFFRACTION AUTHOR X.VERNEDE,B.LAVAULT,J.OHANA,D.NURIZZO,J.JOLY,L.JACQUAMET, AUTHOR 2 F.FELISAZ,F.CIPRIANI,D.BOURGEOIS REVDAT 2 24-FEB-09 2C8O 1 VERSN REVDAT 1 08-MAR-06 2C8O 0 JRNL AUTH X.VERNEDE,B.LAVAULT,J.OHANA,D.NURIZZO,J.JOLY, JRNL AUTH 2 L.JACQUAMET,F.FELISAZ,F.CIPRIANI,D.BOURGEOIS JRNL TITL UV LASER-EXCITED FLUORESCENCE AS A TOOL FOR THE JRNL TITL 2 VISUALIZATION OF PROTEIN CRYSTALS MOUNTED IN JRNL TITL 3 LOOPS. JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 62 253 2006 JRNL REFN ISSN 0907-4449 JRNL PMID 16510972 JRNL DOI 10.1107/S0907444905041429 REMARK 2 REMARK 2 RESOLUTION. 1.5 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.2.0005 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 55.64 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 18130 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) : 0.196 REMARK 3 R VALUE (WORKING SET) : 0.196 REMARK 3 FREE R VALUE : 0.208 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 984 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.50 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1309 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.1870 REMARK 3 BIN FREE R VALUE SET COUNT : 82 REMARK 3 BIN FREE R VALUE : 0.2490 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1000 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 133 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.67 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.19000 REMARK 3 B22 (A**2) : 0.19000 REMARK 3 B33 (A**2) : -0.38000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.086 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.080 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.047 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.195 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1024 ; 0.009 ; 0.021 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1387 ; 1.176 ; 1.901 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 128 ; 5.695 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 50 ;32.697 ;23.000 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 166 ;13.724 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 11 ;17.022 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 144 ; 0.084 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 790 ; 0.004 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 516 ; 0.201 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 717 ; 0.301 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 91 ; 0.140 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 34 ; 0.176 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 9 ; 0.104 ; 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): 649 ; 0.703 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1006 ; 1.249 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 445 ; 2.048 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 381 ; 3.331 ; 4.500 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 : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE REMARK 3 RIDING POSITIONS. REMARK 4 REMARK 4 2C8O COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-DEC-05. REMARK 100 THE PDBE ID CODE IS EBI-26705. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 24-MAY-05 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 4.50 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) : 0.9762 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA) REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19158 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500 REMARK 200 RESOLUTION RANGE LOW (A) : 40.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 10.400 REMARK 200 R MERGE (I) : 0.06000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 27.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.58 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 10.40 REMARK 200 R MERGE FOR SHELL (I) : 0.19000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 12.200 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 3LZT REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 38 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL 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 18.45800 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 39.36500 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 39.36500 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 27.68700 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 39.36500 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 39.36500 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 9.22900 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 39.36500 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 39.36500 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 27.68700 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 39.36500 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 39.36500 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 9.22900 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 18.45800 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 GENERATING THE BIOMOLECULE 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PQS 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 HOH A2057 LIES ON A SPECIAL POSITION. REMARK 375 HOH A2084 LIES ON A SPECIAL POSITION. 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 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 132L RELATED DB: PDB REMARK 900 LYSOZYME REMARK 900 RELATED ID: 193L RELATED DB: PDB REMARK 900 THE 1.33 A STRUCTURE OF TETRAGONAL HEN REMARK 900 EGG WHITE LYSOZYME REMARK 900 RELATED ID: 194L RELATED DB: PDB REMARK 900 THE 1.40 A STRUCTURE OF SPACEHAB-01 HEN REMARK 900 EGG WHITE LYSOZYME REMARK 900 RELATED ID: 1A2Y RELATED DB: PDB REMARK 900 HEN EGG WHITE LYSOZYME, D18A MUTANT, IN REMARK 900 COMPLEX WITH MOUSE MONOCLONAL ANTIBODY D1.3 REMARK 900 RELATED ID: 1AKI RELATED DB: PDB REMARK 900 THE STRUCTURE OF THE ORTHORHOMBIC FORM OF REMARK 900 HEN EGG-WHITE LYSOZYME AT 1.5 ANGSTROMS REMARK 900 RESOLUTION REMARK 900 RELATED ID: 1AT5 RELATED DB: PDB REMARK 900 HEN EGG WHITE LYSOZYME WITH A SUCCINIMIDE REMARK 900 RESIDUE REMARK 900 RELATED ID: 1AT6 RELATED DB: PDB REMARK 900 HEN EGG WHITE LYSOZYME WITH A ISOASPARTATE REMARK 900 RESIDUE REMARK 900 RELATED ID: 1AZF RELATED DB: PDB REMARK 900 CHICKEN EGG WHITE LYSOZYME CRYSTAL GROWN IN REMARK 900 BROMIDE SOLUTION REMARK 900 RELATED ID: 1B0D RELATED DB: PDB REMARK 900 STRUCTURAL EFFECTS OF MONOVALENT ANIONS ON REMARK 900 POLYMORPHIC LYSOZYME CRYSTALS REMARK 900 RELATED ID: 1B2K RELATED DB: PDB REMARK 900 STRUCTURAL EFFECTS OF MONOVALENT ANIONS ON REMARK 900 POLYMORPHIC LYSOZYME CRYSTALS REMARK 900 RELATED ID: 1BGI RELATED DB: PDB REMARK 900 ORTHORHOMBIC LYSOZYME CRYSTALLIZED AT HIGH REMARK 900 TEMPERATURE (310K) REMARK 900 RELATED ID: 1BHZ RELATED DB: PDB REMARK 900 LOW TEMPERATURE MIDDLE RESOLUTION STRUCTURE OF REMARK 900 HEN EGG WHITE LYSOZYME FROM MASC DATA REMARK 900 RELATED ID: 1BVK RELATED DB: PDB REMARK 900 HUMANIZED ANTI-LYSOZYME FV COMPLEXED WITH REMARK 900 LYSOZYME REMARK 900 RELATED ID: 1BVX RELATED DB: PDB REMARK 900 THE 1.8 A STRUCTURE OF GEL GROWN REMARK 900 TETRAGONAL HEN EGG WHITE LYSOZYME REMARK 900 RELATED ID: 1BWH RELATED DB: PDB REMARK 900 THE 1.8 A STRUCTURE OF GROUND CONTROL REMARK 900 GROWN TETRAGONAL HEN EGG WHITE LYSOZYME REMARK 900 RELATED ID: 1BWI RELATED DB: PDB REMARK 900 THE 1.8 A STRUCTURE OF MICROBATCH OIL REMARK 900 DROP GROWN TETRAGONAL HEN EGG WHITE LYSOZYME REMARK 900 RELATED ID: 1BWJ RELATED DB: PDB REMARK 900 THE 1.8 A STRUCTURE OF MICROGRAVITY GROWN REMARK 900 TETRAGONAL HEN EGG WHITE LYSOZYME REMARK 900 RELATED ID: 1C08 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HYHEL-10 FV-HEN REMARK 900 LYSOZYME COMPLEX REMARK 900 RELATED ID: 1C10 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HEW LYSOZYME UNDER REMARK 900 PRESSURE OF XENON (8 BAR) REMARK 900 RELATED ID: 1DPW RELATED DB: PDB REMARK 900 STRUCTURE OF HEN EGG-WHITE LYSOZYME IN REMARK 900 COMPLEX WITH MPD REMARK 900 RELATED ID: 1DPX RELATED DB: PDB REMARK 900 STRUCTURE OF HEN EGG-WHITE LYSOZYME REMARK 900 RELATED ID: 1DQJ RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE ANTI-LYSOZYME REMARK 900 ANTIBODY HYHEL-63 COMPLEXED WITH HEN EGG REMARK 900 WHITE LYSOZYME REMARK 900 RELATED ID: 1E8L RELATED DB: PDB REMARK 900 NMR SOLUTION STRUCTURE OF HEN LYSOZYME REMARK 900 RELATED ID: 1F0W RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF ORTHORHOMBIC LYSOZYME REMARK 900 GROWN AT PH 6.5 REMARK 900 RELATED ID: 1F10 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF ORTHORHOMBIC LYSOZYME REMARK 900 GROWN AT PH 6.5 AT 88% RELATIVE HUMIDITY REMARK 900 RELATED ID: 1F3J RELATED DB: PDB REMARK 900 HISTOCOMPATIBILITY ANTIGEN I-AG7 REMARK 900 RELATED ID: 1FDL RELATED DB: PDB REMARK 900 IGG1 FAB FRAGMENT (ANTI-LYSOZYME ANTIBODY D1.3, REMARK 900 KAPPA) - LYSOZYME COMPLEX REMARK 900 RELATED ID: 1FLQ RELATED DB: PDB REMARK 900 HEN EGG WHITE LYSOZYME MUTANT WITH ALANINE REMARK 900 SUBSTITUTED FORGLYCINE REMARK 900 RELATED ID: 1FLU RELATED DB: PDB REMARK 900 HEN EGG WHITE LYSOZYME MUTANT WITH ALANINE REMARK 900 SUBSTITUTED FORGLYCINE REMARK 900 RELATED ID: 1FLW RELATED DB: PDB REMARK 900 HEN EGG WHITE LYSOZYME MUTANT WITH ALANINE REMARK 900 SUBSTITUTED FORGLYCINE REMARK 900 RELATED ID: 1FLY RELATED DB: PDB REMARK 900 HEN EGG WHITE LYSOZYME MUTANT WITH ALANINE REMARK 900 SUBSTITUTED FORGLYCINE REMARK 900 RELATED ID: 1FN5 RELATED DB: PDB REMARK 900 HEN EGG WHITE LYSOZYME MUTANT WITH ALANINE REMARK 900 SUBSTITUTED FORGLYCINE REMARK 900 RELATED ID: 1G7H RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HEN EGG WHITE LYSOZYME REMARK 900 (HEL) COMPLEXEDWITH THE MUTANT ANTI-HEL REMARK 900 MONOCLONAL ANTIBODY D1.3(VLW92A) REMARK 900 RELATED ID: 1G7I RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HEN EGG WHITE LYSOZYME REMARK 900 (HEL) COMPLEXEDWITH THE MUTANT ANTI-HEL REMARK 900 MONOCLONAL ANTIBODY D1.3 (VLW92F) REMARK 900 RELATED ID: 1G7J RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HEN EGG WHITE LYSOZYME REMARK 900 (HEL) COMPLEXEDWITH THE MUTANT ANTI-HEL REMARK 900 MONOCLONAL ANTIBODY D1.3 (VLW92H) REMARK 900 RELATED ID: 1G7L RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HEN EGG WHITE LYSOZYME REMARK 900 (HEL) COMPLEXEDWITH THE MUTANT ANTI-HEL REMARK 900 MONOCLONAL ANTIBODY D1.3 (VLW92S) REMARK 900 RELATED ID: 1G7M RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HEN EGG WHITE LYSOZYME REMARK 900 (HEL) COMPLEXEDWITH THE MUTANT ANTI-HEL REMARK 900 MONOCLONAL ANTIBODY D1.3 (VLW92V) REMARK 900 RELATED ID: 1GPQ RELATED DB: PDB REMARK 900 STRUCTURE OF IVY COMPLEXED WITH ITS TARGET REMARK 900 , HEWL REMARK 900 RELATED ID: 1GWD RELATED DB: PDB REMARK 900 TRI-IODIDE DERIVATIVE OF HEN EGG-WHITE REMARK 900 LYSOZYME REMARK 900 RELATED ID: 1GXV RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF LYSOZYME AT LOW AND REMARK 900 HIGH PRESSURE REMARK 900 RELATED ID: 1GXX RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF LYSOZYME AT LOW AND REMARK 900 HIGH PRESSURE REMARK 900 RELATED ID: 1H6M RELATED DB: PDB REMARK 900 COVALENT GLYCOSYL-ENZYME INTERMEDIATE OF HEN REMARK 900 EGG WHITE LYSOZYME REMARK 900 RELATED ID: 1H87 RELATED DB: PDB REMARK 900 GADOLINIUM DERIVATIVE OF TETRAGONAL HEN EGG- REMARK 900 WHITE LYSOZYME AT 1.7 A RESOLUTION REMARK 900 RELATED ID: 1HC0 RELATED DB: PDB REMARK 900 STRUCTURE OF LYSOZYME WITH PERIODATE REMARK 900 RELATED ID: 1HEL RELATED DB: PDB REMARK 900 HEN EGG-WHITE LYSOZYME WILD TYPE REMARK 900 RELATED ID: 1HEM RELATED DB: PDB REMARK 900 LYSOZYME MUTANT WITH SER 91 REPLACED BY REMARK 900 THR (S91T) REMARK 900 RELATED ID: 1HEN RELATED DB: PDB REMARK 900 LYSOZYME MUTANT WITH ILE 55 REPLACED BY REMARK 900 VAL AND SER 91 REPLACED BY THR (I55V, REMARK 900 S91T) REMARK 900 RELATED ID: 1HEO RELATED DB: PDB REMARK 900 LYSOZYME MUTANT WITH ILE 55 REPLACED BY REMARK 900 VAL (I55V) REMARK 900 RELATED ID: 1HEP RELATED DB: PDB REMARK 900 LYSOZYME MUTANT WITH THR 40 REPLACED BY REMARK 900 SER, ILE 55 REPLACED BY VAL, AND SER 91 REMARK 900 REPLACED BY THR (T40S,I55V,S91T) REMARK 900 RELATED ID: 1HEQ RELATED DB: PDB REMARK 900 LYSOZYME MUTANT WITH THR 40 REPLACED BY REMARK 900 SER AND SER 91 REPLACED BY THR (T40S, REMARK 900 S91T) REMARK 900 RELATED ID: 1HER RELATED DB: PDB REMARK 900 LYSOZYME MUTANT WITH THR 40 REPLACED BY REMARK 900 SER (T40S) REMARK 900 RELATED ID: 1HEW RELATED DB: PDB REMARK 900 LYSOZYME COMPLEXED WITH THE INHIBITOR TRI-N REMARK 900 -ACETYLCHITOTRIOSE REMARK 900 RELATED ID: 1HF4 RELATED DB: PDB REMARK 900 STRUCTURAL EFFECTS OF MONOVALENT ANIONS ON REMARK 900 POLYMORPHIC LYSOZYME CRYSTALS REMARK 900 RELATED ID: 1HSW RELATED DB: PDB REMARK 900 LYSOZYME (MUCOPEPTIDE N-ACETYLMURAMYL HYDROLASE REMARK 900 ) REMARK 900 RELATED ID: 1HSX RELATED DB: PDB REMARK 900 LYSOZYME GROWN AT BASIC PH AND ITS LOW REMARK 900 HUMIDITY VARIANT REMARK 900 RELATED ID: 1IC4 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HYHEL-10 FV MUTANT( REMARK 900 HD32A)-HEN LYSOZYMECOMPLEX REMARK 900 RELATED ID: 1IC5 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HYHEL-10 FV MUTANT( REMARK 900 HD99A)-HEN LYSOZYMECOMPLEX REMARK 900 RELATED ID: 1IC7 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HYHEL-10 FV MUTANT( REMARK 900 HD32A99A)-HENLYSOZYME COMPLEX REMARK 900 RELATED ID: 1IEE RELATED DB: PDB REMARK 900 STRUCTURE OF TETRAGONAL HEN EGG WHITE REMARK 900 LYSOZYME AT 0.94 AFROM CRYSTALS GROWN BY REMARK 900 THE COUNTER-DIFFUSION METHOD REMARK 900 RELATED ID: 1IO5 RELATED DB: PDB REMARK 900 HYDROGEN AND HYDRATION OF HEN EGG-WHITE REMARK 900 LYSOZYME DETERMINEDBY NEUTRON DIFFRACTION REMARK 900 RELATED ID: 1IOQ RELATED DB: PDB REMARK 900 STABILIZATION OF HEN EGG WHITE LYSOZYME BY REMARK 900 A CAVITY-FILLINGMUTATION REMARK 900 RELATED ID: 1IOR RELATED DB: PDB REMARK 900 STABILIZATION OF HEN EGG WHITE LYSOZYME BY REMARK 900 A CAVITY-FILLINGMUTATION REMARK 900 RELATED ID: 1IOS RELATED DB: PDB REMARK 900 STABILIZATION OF HEN EGG WHITE LYSOZYME BY REMARK 900 A CAVITY-FILLINGMUTATION REMARK 900 RELATED ID: 1IOT RELATED DB: PDB REMARK 900 STABILIZATION OF HEN EGG WHITE LYSOZYME BY REMARK 900 A CAVITY-FILLINGMUTATION REMARK 900 RELATED ID: 1IR7 RELATED DB: PDB REMARK 900 IM MUTANT OF LYSOZYME REMARK 900 RELATED ID: 1IR8 RELATED DB: PDB REMARK 900 IM MUTANT OF LYSOZYME REMARK 900 RELATED ID: 1IR9 RELATED DB: PDB REMARK 900 IM MUTANT OF LYSOZYME REMARK 900 RELATED ID: 1J1O RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HYHEL-10 FV MUTANT REMARK 900 LY50F COMPLEXEDWITH HEN EGG WHITE LYSOZYME REMARK 900 RELATED ID: 1J1P RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HYHEL-10 FV MUTANT REMARK 900 LS91A COMPLEXEDWITH HEN EGG WHITE LYSOZYME REMARK 900 RELATED ID: 1J1X RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HYHEL-10 FV MUTANT REMARK 900 LS93A COMPLEXEDWITH HEN EGG WHITE LYSOZYME REMARK 900 RELATED ID: 1JA2 RELATED DB: PDB REMARK 900 BINDING OF N-ACETYLGLUCOSAMINE TO CHICKEN REMARK 900 EGG LYSOZYME: APOWDER DIFFRACTION STUDY REMARK 900 RELATED ID: 1JA4 RELATED DB: PDB REMARK 900 BINDING OF N-ACETYLGLUCOSAMINE TO CHICKEN REMARK 900 EGG LYSOZYME: APOWDER DIFFRACTION STUDY REMARK 900 RELATED ID: 1JA6 RELATED DB: PDB REMARK 900 BINDING OF N-ACETYLGLUCOSAMINE TO CHICKEN REMARK 900 EGG LYSOZYME: APOWDER DIFFRACTION STUDY REMARK 900 RELATED ID: 1JA7 RELATED DB: PDB REMARK 900 BINDING OF N-ACETYLGLUCOSAMINE TO CHICKEN REMARK 900 EGG LYSOZYME: APOWDER DIFFRACTION STUDY REMARK 900 RELATED ID: 1JIS RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF TETRAGONAL LYSOZYME GROWN REMARK 900 AT PH 4.6 REMARK 900 RELATED ID: 1JIT RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF TETRAGONAL LYSOZYME GROWN REMARK 900 IN PRESENCE30% TREHALOSE REMARK 900 RELATED ID: 1JIY RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF TETRAGONAL LYSOZYME GROWN REMARK 900 IN PRESENCE20% SORBITOL REMARK 900 RELATED ID: 1JJ0 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF TETRAGONAL LYSOZYME GROWN REMARK 900 IN PRESENCEOF 30% SUCROSE REMARK 900 RELATED ID: 1JJ1 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF ORTHORHOMBIC LYSOZYME REMARK 900 GROWN AT PH 4.6IN PRESENCE OF 5% REMARK 900 SORBITOL REMARK 900 RELATED ID: 1JJ3 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MONOCLINIC LYSOZYME GROWN REMARK 900 AT PH 4.6 REMARK 900 RELATED ID: 1JPO RELATED DB: PDB REMARK 900 LOW TEMPERATURE ORTHORHOMBIC LYSOZYME REMARK 900 RELATED ID: 1JTO RELATED DB: PDB REMARK 900 DEGENERATE INTERFACES IN ANTIGEN-ANTIBODY REMARK 900 COMPLEXES REMARK 900 RELATED ID: 1JTT RELATED DB: PDB REMARK 900 DEGENERATE INTERFACES IN ANTIGEN-ANTIBODY REMARK 900 COMPLEXES REMARK 900 RELATED ID: 1KIP RELATED DB: PDB REMARK 900 FV MUTANT Y(B 32)A (VH DOMAIN) OF REMARK 900 MOUSE MONOCLONAL ANTIBODY D1.3 COMPLEXED REMARK 900 WITH HEN EGG WHITE LYSOZYME REMARK 900 RELATED ID: 1KIQ RELATED DB: PDB REMARK 900 FV MUTANT Y(B 101)F (VH DOMAIN) OF REMARK 900 MOUSE MONOCLONAL ANTIBODY D1.3 COMPLEXED REMARK 900 WITH HEN EGG WHITE LYSOZYME REMARK 900 RELATED ID: 1KIR RELATED DB: PDB REMARK 900 FV MUTANT Y(A 50)S (VL DOMAIN) OF REMARK 900 MOUSE MONOCLONAL ANTIBODY D1.3 COMPLEXED REMARK 900 WITH HEN EGG WHITE LYSOZYME REMARK 900 RELATED ID: 1KXW RELATED DB: PDB REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN REMARK 900 LYSOZYME WITH THE HELIX DIPOLE AND CHARGED REMARK 900 SIDE CHAINS REMARK 900 RELATED ID: 1KXX RELATED DB: PDB REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN REMARK 900 LYSOZYME WITH THE HELIX DIPOLE AND CHARGED REMARK 900 SIDE CHAINS REMARK 900 RELATED ID: 1KXY RELATED DB: PDB REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN REMARK 900 LYSOZYME WITH THE HELIX DIPOLE AND CHARGED REMARK 900 SIDE CHAINS REMARK 900 RELATED ID: 1LCN RELATED DB: PDB REMARK 900 MONOCLINIC HEN EGG WHITE LYSOZYME, THIOCYANATE REMARK 900 COMPLEX REMARK 900 RELATED ID: 1LJ3 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MONOCLINIC LYSOZYME GROWN REMARK 900 AT PH 4.6 REMARK 900 RELATED ID: 1LJ4 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MONOCLINIC LYSOZYME GROWN REMARK 900 AT PH 4.6 REMARK 900 RELATED ID: 1LJE RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MONOCLINIC LYSOZYME GROWN REMARK 900 IN PRESENCEOF 10% SUCROSE REMARK 900 RELATED ID: 1LJF RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MONOCLINIC LYSOZYME GROWN REMARK 900 IN PRESENCEOF 10% SUCROSE REMARK 900 RELATED ID: 1LJG RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MONOCLINIC LYSOZYME GROWN REMARK 900 IN PRESENCEOF 5% GLYCEROL REMARK 900 RELATED ID: 1LJH RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MONOCLINIC LYSOZYME GROWN REMARK 900 IN PRESENCEOF 5% GLYCEROL REMARK 900 RELATED ID: 1LJI RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MONOCLINIC LYSOZYME GROWN REMARK 900 IN PRESENCE10% SORBITOL REMARK 900 RELATED ID: 1LJJ RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MONOCLINIC LYSOZYME GROWN REMARK 900 IN PRESENCEOF 10% TREHALOSE REMARK 900 RELATED ID: 1LJK RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MONOCLINIC LYSOZYME GROWN REMARK 900 IN PRESENCEOF 15% TREHALOSE REMARK 900 RELATED ID: 1LKR RELATED DB: PDB REMARK 900 MONOCLINIC HEN EGG WHITE LYSOZYME IODIDE REMARK 900 RELATED ID: 1LKS RELATED DB: PDB REMARK 900 HEN EGG WHITE LYSOZYME NITRATE REMARK 900 RELATED ID: 1LMA RELATED DB: PDB REMARK 900 LYSOZYME (88 PERCENT HUMIDITY) REMARK 900 RELATED ID: 1LPI RELATED DB: PDB REMARK 900 HEW LYSOZYME: TRP...NA CATION-PI INTERACTION REMARK 900 RELATED ID: 1LSA RELATED DB: PDB REMARK 900 LYSOZYME (120 K) REMARK 900 RELATED ID: 1LSB RELATED DB: PDB REMARK 900 LYSOZYME (180 K) REMARK 900 RELATED ID: 1LSC RELATED DB: PDB REMARK 900 LYSOZYME (250 K) REMARK 900 RELATED ID: 1LSD RELATED DB: PDB REMARK 900 LYSOZYME (280 K) REMARK 900 RELATED ID: 1LSE RELATED DB: PDB REMARK 900 LYSOZYME (295 K) REMARK 900 RELATED ID: 1LSF RELATED DB: PDB REMARK 900 LYSOZYME (95 K) REMARK 900 RELATED ID: 1LSG RELATED DB: PDB REMARK 900 MOL_ID: 1; MOLECULE: LYSOZYME MODIFIED WITH REMARK 900 HUMAN FIBRINOGEN GAMMA; CHAIN: NULL; REMARK 900 ENGINEERED; THE 14-RESIDUE C-TERMINUS ( REMARK 900 RESIDUES 398 - 411) OF THE HUMAN FIBRINOGEN REMARK 900 GAMMA CHAIN FUSED TO THE C-TERMINUS OF REMARK 900 CHICKEN EGG WHITE LYSOZYME; MUTATION: N-TERM REMARK 900 MET REMARK 900 RELATED ID: 1LSM RELATED DB: PDB REMARK 900 LYSOZYME MUTANT WITH ILE 55 REPLACED BY REMARK 900 LEU, SER 91 REPLACED BY THR, AND ASP 101 REMARK 900 REPLACED BY SER (I55L,S91T,D101S) REMARK 900 RELATED ID: 1LSN RELATED DB: PDB REMARK 900 LYSOZYME MUTANT WITH SER 91 REPLACED BY REMARK 900 ALA (S91A) REMARK 900 RELATED ID: 1LSY RELATED DB: PDB REMARK 900 LYSOZYME MUTANT WITH ASP 52 REPLACED BY REMARK 900 SER (D52S) REMARK 900 RELATED ID: 1LSZ RELATED DB: PDB REMARK 900 LYSOZYME MUTANT WITH ASP 52 REPLACED BY REMARK 900 SER (D52S) COMPLEXED WITH GLCNAC4 (TETRA-N- REMARK 900 ACETYL CHITOTETRAOSE) REMARK 900 RELATED ID: 1LYO RELATED DB: PDB REMARK 900 CROSS-LINKED LYSOZYME CRYSTAL IN NEAT WATER REMARK 900 RELATED ID: 1LYS RELATED DB: PDB REMARK 900 LYSOZYME REMARK 900 RELATED ID: 1LYZ RELATED DB: PDB REMARK 900 LYSOZYME REMARK 900 RELATED ID: 1LZ8 RELATED DB: PDB REMARK 900 LYSOZYME PHASED ON ANOMALOUS SIGNAL OF REMARK 900 SULFURS AND CHLORINES REMARK 900 RELATED ID: 1LZ9 RELATED DB: PDB REMARK 900 ANOMALOUS SIGNAL OF SOLVENT BROMINES USED REMARK 900 FOR PHASING OF LYSOZYME REMARK 900 RELATED ID: 1LZA RELATED DB: PDB REMARK 900 LYSOZYME REMARK 900 RELATED ID: 1LZB RELATED DB: PDB REMARK 900 LYSOZYME CO-CRYSTALLIZED WITH TRI-N-ACETYL- REMARK 900 CHITOTRIOSE (PH 4.7) REMARK 900 RELATED ID: 1LZC RELATED DB: PDB REMARK 900 LYSOZYME CO-CRYSTALLIZED WITH TETRA-N-ACETYL REMARK 900 -CHITOTETRAOSE (PH 4.7) REMARK 900 RELATED ID: 1LZD RELATED DB: PDB REMARK 900 LYSOZYME MUTANT WITH TRP 62 REPLACED BY REMARK 900 TYR (W62Y) REMARK 900 RELATED ID: 1LZE RELATED DB: PDB REMARK 900 LYSOZYME MUTANT WITH TRP 62 REPLACED BY REMARK 900 TYR (W62Y) CO-CRYSTALLIZED WITH TRI-N- REMARK 900 ACETYL-CHITOTRIOSE (PH 4.7) REMARK 900 RELATED ID: 1LZG RELATED DB: PDB REMARK 900 LYSOZYME MUTANT WITH TRP 62 REPLACED BY REMARK 900 PHE (W62F) CO-CRYSTALLIZED WITH TRI-N- REMARK 900 ACETYL-CHITOTRIOSE (PH 4.7) REMARK 900 RELATED ID: 1LZH RELATED DB: PDB REMARK 900 LYSOZYME (MONOCLINIC) REMARK 900 RELATED ID: 1LZN RELATED DB: PDB REMARK 900 NEUTRON STRUCTURE OF HEN EGG-WHITE LYSOZYME REMARK 900 RELATED ID: 1LZT RELATED DB: PDB REMARK 900 LYSOZYME , TRICLINIC CRYSTAL FORM REMARK 900 RELATED ID: 1MEL RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF A CAMEL SINGLE-DOMAIN REMARK 900 VH ANTIBODY FRAGMENT IN COMPLEX WITH REMARK 900 LYSOZYME REMARK 900 RELATED ID: 1MLC RELATED DB: PDB REMARK 900 MONOCLONAL ANTIBODY FAB D44.1 RAISED AGAINST REMARK 900 CHICKEN EGG-WHITE LYSOZYME COMPLEXED WITH REMARK 900 LYSOZYME REMARK 900 RELATED ID: 1N4F RELATED DB: PDB REMARK 900 PARA-ARSANILATE DERIVATIVE OF HEN EGG-WHITE REMARK 900 LYSOZYME REMARK 900 RELATED ID: 1NBY RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HYHEL-63 COMPLEXED WITH REMARK 900 HEL MUTANT K96A REMARK 900 RELATED ID: 1NBZ RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HYHEL-63 COMPLEXED WITH REMARK 900 HEL MUTANT K96A REMARK 900 RELATED ID: 1NDG RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF FAB FRAGMENT OF REMARK 900 ANTIBODY HYHEL-8COMPLEXED WITH ITS ANTIGEN REMARK 900 LYSOZYME REMARK 900 RELATED ID: 1NDM RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF FAB FRAGMENT OF REMARK 900 ANTIBODY HYHEL-26COMPLEXED WITH LYSOZYME REMARK 900 RELATED ID: 1P2C RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF AN ANTI- REMARK 900 LYSOZYME ANTIBODY REMARK 900 RELATED ID: 1PS5 RELATED DB: PDB REMARK 900 STRUCTURE OF THE MONOCLINIC C2 FORM OF HEN REMARK 900 EGG-WHITELYSOZYME AT 2.0 ANGSTROMS REMARK 900 RESOLUTION REMARK 900 RELATED ID: 1QIO RELATED DB: PDB REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE CAUSED REMARK 900 BY INTENSE SYNCHROTRON RADIATION TO HEN REMARK 900 EGG WHITE LYSOZYME REMARK 900 RELATED ID: 1QTK RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HEW LYSOZYME UNDER REMARK 900 PRESSURE OF KRYPTON (55 BAR) REMARK 900 RELATED ID: 1RCM RELATED DB: PDB REMARK 900 LYSOZYME (PARTIALLY REDUCED, CARBOXYMETHYLATED ( REMARK 900 6,127-RCM)) REMARK 900 RELATED ID: 1RFP RELATED DB: PDB REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN REMARK 900 LYSOZYME WITH THE HELIX DIPOLE AND CHARGED REMARK 900 SIDE CHAINS REMARK 900 RELATED ID: 1RI8 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE CAMELID SINGLE REMARK 900 DOMAIN ANTIBODY1D2L19 IN COMPLEX WITH HEN REMARK 900 EGG WHITE LYSOZYME REMARK 900 RELATED ID: 1RJC RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE CAMELID SINGLE REMARK 900 DOMAIN ANTIBODY CAB-LYS2 IN COMPLEX WITH REMARK 900 HEN EGG WHITE LYSOZYME REMARK 900 RELATED ID: 1SF4 RELATED DB: PDB REMARK 900 BINDING OF N,N'-DIACETYLCHITOBIOSE TO HEW REMARK 900 LYSOZYME: APOWDER DIFFRACTION STUDY REMARK 900 RELATED ID: 1SF6 RELATED DB: PDB REMARK 900 BINDING OF N,N',N"-TRIACETYLCHITOTRIOSE TO REMARK 900 HEW LYSOZYME: APOWDER DIFFRACTION STUDY REMARK 900 RELATED ID: 1SF7 RELATED DB: PDB REMARK 900 BINDING OF TETRA-N-ACETYLCHITOTETRAOSE TO REMARK 900 HEW LYSOZYME: APOWDER DIFFRACTION STUDY REMARK 900 RELATED ID: 1SFB RELATED DB: PDB REMARK 900 BINDING OF PENTA-N-ACETYLCHITOPENTAOSE TO REMARK 900 HEW LYSOZYME: APOWDER DIFFRACTION STUDY REMARK 900 RELATED ID: 1SFG RELATED DB: PDB REMARK 900 BINDING OF HEXA-N-ACETYLCHITOHEXAOSE: A REMARK 900 POWDER DIFFRACTIONSTUDY REMARK 900 RELATED ID: 1SQ2 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF THE NURSE REMARK 900 SHARK NEW ANTIGENRECEPTOR (NAR) VARIABLE REMARK 900 DOMAIN IN COMPLEX WITH LYXOZYME REMARK 900 RELATED ID: 1T3P RELATED DB: PDB REMARK 900 HALF-SANDWICH ARENE RUTHENIUM(II)-ENZYME REMARK 900 COMPLEX REMARK 900 RELATED ID: 1T6V RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF THE NURSE REMARK 900 SHARK NEW ANTIGENRECEPTOR (NAR) VARIABLE REMARK 900 DOMAIN IN COMPLEX WITH LYSOZYME REMARK 900 RELATED ID: 1UA6 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HYHEL-10 FV MUTANT REMARK 900 SFSF COMPLEXED WITHHEN EGG WHITE LYSOZYME REMARK 900 COMPLEX REMARK 900 RELATED ID: 1UC0 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF WILD-TYPE HEN-EGG REMARK 900 WHITE LYSOZYMESINGLY LABELED WITH 2',3'- REMARK 900 EPOXYPROPYL BETA-GLYCOSIDE OF N- REMARK 900 ACETYLLACTOSAMINE REMARK 900 RELATED ID: 1UCO RELATED DB: PDB REMARK 900 HEN EGG-WHITE LYSOZYME, LOW HUMIDITY FORM REMARK 900 RELATED ID: 1UIA RELATED DB: PDB REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN REMARK 900 LYSOZYME WITH THE HELIX DIPOLE AND CHARGED REMARK 900 SIDE CHAINS REMARK 900 RELATED ID: 1UIB RELATED DB: PDB REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN REMARK 900 LYSOZYME WITH THE HELIX DIPOLE AND CHARGED REMARK 900 SIDE CHAINS REMARK 900 RELATED ID: 1UIC RELATED DB: PDB REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN REMARK 900 LYSOZYME WITH THE HELIX DIPOLE AND CHARGED REMARK 900 SIDE CHAINS REMARK 900 RELATED ID: 1UID RELATED DB: PDB REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN REMARK 900 LYSOZYME WITH THE HELIX DIPOLE AND CHARGED REMARK 900 SIDE CHAINS REMARK 900 RELATED ID: 1UIE RELATED DB: PDB REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN REMARK 900 LYSOZYME WITH THE HELIX DIPOLE AND CHARGED REMARK 900 SIDE CHAINS REMARK 900 RELATED ID: 1UIF RELATED DB: PDB REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN REMARK 900 LYSOZYME WITH THE HELIX DIPOLE AND CHARGED REMARK 900 SIDE CHAINS REMARK 900 RELATED ID: 1UIG RELATED DB: PDB REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN REMARK 900 LYSOZYME WITH THE HELIX DIPOLE AND CHARGED REMARK 900 SIDE CHAINS REMARK 900 RELATED ID: 1UIH RELATED DB: PDB REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN REMARK 900 LYSOZYME WITH THE HELIX DIPOLE AND CHARGED REMARK 900 SIDE CHAINS REMARK 900 RELATED ID: 1UUZ RELATED DB: PDB REMARK 900 IVY:A NEW FAMILY OF PROTEIN REMARK 900 RELATED ID: 1V7S RELATED DB: PDB REMARK 900 TRICLINIC HEN LYSOZYME CRYSTALLIZED AT 313K REMARK 900 FROM A D2OSOLUTION REMARK 900 RELATED ID: 1V7T RELATED DB: PDB REMARK 900 TRICLINIC LYSOZYME WITH LOW SOLVENT CONTENT REMARK 900 OBTAINED BYPHASE TRANSITION REMARK 900 RELATED ID: 1VAT RELATED DB: PDB REMARK 900 IODINE DERIVATIVE OF HEN EGG-WHITE LYSOZYME REMARK 900 RELATED ID: 1VAU RELATED DB: PDB REMARK 900 XENON DERIVATIVE OF HEN EGG-WHITE LYSOZYME REMARK 900 RELATED ID: 1VDP RELATED DB: PDB REMARK 900 THE CRYSTAL STRUCTURE OF THE MONOCLINIC FORM REMARK 900 OF HEN EGGWHITE LYSOZYME AT 1.7 REMARK 900 ANGSTROMS RESOLUTION IN SPACE REMARK 900 RELATED ID: 1VDQ RELATED DB: PDB REMARK 900 THE CRYSTAL STRUCTURE OF THE ORTHORHOMBIC REMARK 900 FORM OF HEN EGGWHITE LYSOZYME AT 1.5 REMARK 900 ANGSTROMS RESOLUTION REMARK 900 RELATED ID: 1VDS RELATED DB: PDB REMARK 900 THE CRYSTAL STRUCTURE OF THE TETRAGONAL FORM REMARK 900 OF HEN EGGWHITE LYSOZYME AT 1.6 REMARK 900 ANGSTROMS RESOLUTION IN SPACE REMARK 900 RELATED ID: 1VDT RELATED DB: PDB REMARK 900 THE CRYSTAL STRUCTURE OF THE TETRAGONAL FORM REMARK 900 OF HEN EGGWHITE LYSOZYME AT 1.7 REMARK 900 ANGSTROMS RESOLUTION UNDER BASICCONDITIONS IN REMARK 900 SPACE REMARK 900 RELATED ID: 1VED RELATED DB: PDB REMARK 900 THE CRYSTAL STRUCTURE OF THE ORTHORHOMBIC REMARK 900 FORM OF HEN EGGWHITE LYSOZYME AT 1.9 REMARK 900 ANGSTROMS RESOLUTION IN SPACE REMARK 900 RELATED ID: 1VFB RELATED DB: PDB REMARK 900 FV FRAGMENT OF MOUSE MONOCLONAL ANTIBODY D1 REMARK 900 .3 COMPLEXED WITH HEN EGG LYSOZYME REMARK 900 RELATED ID: 1W6Z RELATED DB: PDB REMARK 900 HIGH ENERGY TATRAGONAL LYSOZYME X-RAY REMARK 900 STRUCTURE REMARK 900 RELATED ID: 1WTM RELATED DB: PDB REMARK 900 X-RAY STRUCTURE OF HEW LYSOZYME ORTHORHOMBIC REMARK 900 CRYSTAL FORMEDIN THE EARTH'S MAGNETIC REMARK 900 FIELD REMARK 900 RELATED ID: 1WTN RELATED DB: PDB REMARK 900 THE STRUCTURE OF HEW LYSOZYME ORTHORHOMBIC REMARK 900 CRYSTAL GROWTHUNDER A HIGH MAGNETIC FIELD REMARK 900 RELATED ID: 1XEI RELATED DB: PDB REMARK 900 THE CRYSTAL STRUCTURES OF LYSOZYME AT VERY REMARK 900 LOW LEVELS OF HYDRATION REMARK 900 RELATED ID: 1XEJ RELATED DB: PDB REMARK 900 THE CRYSTAL STRUCTURES OF LYSOZYME AT VERY REMARK 900 LOW LEVELS OF HYDRATION REMARK 900 RELATED ID: 1XEK RELATED DB: PDB REMARK 900 THE CRYSTAL STRUCTURES OF LYSOZYME AT VERY REMARK 900 LOW LEVELS OF HYDRATION REMARK 900 RELATED ID: 1XFP RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE CDR2 GERMLINE REMARK 900 REVERSION MUTANT OFCAB-LYS3 IN COMPLEX WITH REMARK 900 HEN EGG WHITE LYSOZYME REMARK 900 RELATED ID: 1XGP RELATED DB: PDB REMARK 900 STRUCTURE FOR ANTIBODY HYHEL-63 Y33A MUTANT REMARK 900 COMPLEXED WITHHEN EGG LYSOZYME REMARK 900 RELATED ID: 1XGQ RELATED DB: PDB REMARK 900 STRUCTURE FOR ANTIBODY HYHEL-63 Y33V MUTANT REMARK 900 COMPLEXED WITHHEN EGG LYSOZYME REMARK 900 RELATED ID: 1YIK RELATED DB: PDB REMARK 900 STRUCTURE OF HEN EGG WHITE LYSOZYME SOAKED REMARK 900 WITH CU-CYCLAM REMARK 900 RELATED ID: 1YIL RELATED DB: PDB REMARK 900 STRUCTURE OF HEN EGG WHITE LYSOZYME SOAKED REMARK 900 WITH CU2-XYLYLBICYCLAM REMARK 900 RELATED ID: 1YKX RELATED DB: PDB REMARK 900 EFFECT OF ALCOHOLS ON PROTEIN HYDRATION REMARK 900 RELATED ID: 1YKY RELATED DB: PDB REMARK 900 EFFECT OF ALCOHOLS ON PROTEIN HYDRATION REMARK 900 RELATED ID: 1YKZ RELATED DB: PDB REMARK 900 EFFECT OF ALCOHOLS ON PROTEIN HYDRATION REMARK 900 RELATED ID: 1YL0 RELATED DB: PDB REMARK 900 EFFECT OF ALCOHOLS ON PROTEIN HYDRATION REMARK 900 RELATED ID: 1YL1 RELATED DB: PDB REMARK 900 EFFECT OF ALCOHOLS ON PROTEIN HYDRATION REMARK 900 RELATED ID: 1YQV RELATED DB: PDB REMARK 900 THE CRYSTAL STRUCTURE OF THE ANTIBODY FAB REMARK 900 HYHEL5 COMPLEXWITH LYSOZYME AT 1.7A REMARK 900 RESOLUTION REMARK 900 RELATED ID: 1Z55 RELATED DB: PDB REMARK 900 EFFECT OF ALCOHOLS ON PROTEIN HYDRATION REMARK 900 RELATED ID: 1ZMY RELATED DB: PDB REMARK 900 CABBCII-10 VHH FRAMEWORK WITH CDR LOOPS OF REMARK 900 CABLYS3 GRAFTEDON IT AND IN COMPLEX WITH REMARK 900 HEN EGG WHITE LYSOZYME REMARK 900 RELATED ID: 2A7D RELATED DB: PDB REMARK 900 ON THE ROUTINE USE OF SOFT X-RAYS IN REMARK 900 MACROMOLECULARCRYSTALLOGRAPHY, PART III- THE REMARK 900 OPTIMAL DATA COLLECTIONWAVELENGTH REMARK 900 RELATED ID: 2A7F RELATED DB: PDB REMARK 900 ON THE ROUTINE USE OF SOFT X-RAYS IN REMARK 900 MACROMOLECULARCRYSTALLOGRAPHY, PART III- THE REMARK 900 OPTIMAL DATA COLLECTIONWAVELENGTH REMARK 900 RELATED ID: 2BLX RELATED DB: PDB REMARK 900 HEWL BEFORE A HIGH DOSE X-RAY "BURN" REMARK 900 RELATED ID: 2BLY RELATED DB: PDB REMARK 900 HEWL AFTER A HIGH DOSE X-RAY "BURN" REMARK 900 RELATED ID: 2BPU RELATED DB: PDB REMARK 900 THE KEDGE HOLMIUM DERIVATIVE OF HEN EGG- REMARK 900 WHITE LYSOZYME AT HIGH RESOLUTION FROM REMARK 900 SINGLE WAVELENGTH ANOMALOUS DIFFRACTION REMARK 900 RELATED ID: 2CDS RELATED DB: PDB REMARK 900 LYSOZYME REMARK 900 RELATED ID: 2D6B RELATED DB: PDB REMARK 900 NOVEL BROMATE SPECIES TRAPPED WITHIN A REMARK 900 PROTEIN CRYSTAL REMARK 900 RELATED ID: 2HFM RELATED DB: PDB REMARK 900 IGG1 FV FRAGMENT (HYHEL-10) AND LYSOZYME REMARK 900 COMPLEX (THEORETICAL MODEL) REMARK 900 RELATED ID: 2IFF RELATED DB: PDB REMARK 900 IGG1 FAB FRAGMENT (HYHEL-5) COMPLEXED WITH REMARK 900 LYSOZYME MUTANT WITH ARG 68 REPLACED BY REMARK 900 LYS (R68K) REMARK 900 RELATED ID: 2LYM RELATED DB: PDB REMARK 900 LYSOZYME (1 ATMOSPHERE, 1.4 M NACL) REMARK 900 RELATED ID: 2LYO RELATED DB: PDB REMARK 900 CROSS-LINKED CHICKEN LYSOZYME CRYSTAL IN 90 REMARK 900 % ACETONITRILE-WATER REMARK 900 RELATED ID: 2LYZ RELATED DB: PDB REMARK 900 LYSOZYME REMARK 900 RELATED ID: 2LZH RELATED DB: PDB REMARK 900 LYSOZYME (ORTHORHOMBIC) REMARK 900 RELATED ID: 2LZT RELATED DB: PDB REMARK 900 LYSOZYME , TRICLINIC CRYSTAL FORM REMARK 900 RELATED ID: 3HFM RELATED DB: PDB REMARK 900 IGG1 FAB FRAGMENT (HYHEL-10) AND LYSOZYME REMARK 900 COMPLEX REMARK 900 RELATED ID: 3LYM RELATED DB: PDB REMARK 900 LYSOZYME (1000 ATMOSPHERES, 1.4 M NACL) REMARK 900 RELATED ID: 3LYO RELATED DB: PDB REMARK 900 CROSS-LINKED CHICKEN LYSOZYME CRYSTAL IN 95 REMARK 900 % ACETONITRILE-WATER REMARK 900 RELATED ID: 3LYT RELATED DB: PDB REMARK 900 LYSOZYME (100 KELVIN) REMARK 900 RELATED ID: 3LYZ RELATED DB: PDB REMARK 900 LYSOZYME REMARK 900 RELATED ID: 3LZT RELATED DB: PDB REMARK 900 REFINEMENT OF TRICLINIC LYSOZYME AT ATOMIC REMARK 900 RESOLUTION REMARK 900 RELATED ID: 4LYM RELATED DB: PDB REMARK 900 LYSOZYME (MUCOPEPTIDE N-ACETYLMURAMYL HYDROLASE) REMARK 900 RELATED ID: 4LYO RELATED DB: PDB REMARK 900 CROSS-LINKED CHICKEN LYSOZYME CRYSTAL IN REMARK 900 NEAT ACETONITRILE, THEN BACK-SOAKED IN WATER REMARK 900 RELATED ID: 4LYT RELATED DB: PDB REMARK 900 LYSOZYME (298 KELVIN) REMARK 900 RELATED ID: 4LYZ RELATED DB: PDB REMARK 900 LYSOZYME REMARK 900 RELATED ID: 4LZT RELATED DB: PDB REMARK 900 ATOMIC RESOLUTION REFINEMENT OF TRICLINIC HEW REMARK 900 LYSOZYME AT 295K REMARK 900 RELATED ID: 5LYM RELATED DB: PDB REMARK 900 MOL_ID: 1; MOLECULE: LYSOZYME; CHAIN: A, B REMARK 900 ; EC: 3.2.1.17 REMARK 900 RELATED ID: 5LYT RELATED DB: PDB REMARK 900 LYSOZYME (100 KELVIN) REMARK 900 RELATED ID: 5LYZ RELATED DB: PDB REMARK 900 LYSOZYME REMARK 900 RELATED ID: 6LYT RELATED DB: PDB REMARK 900 LYSOZYME (298 KELVIN) REMARK 900 RELATED ID: 6LYZ RELATED DB: PDB REMARK 900 LYSOZYME REMARK 900 RELATED ID: 7LYZ RELATED DB: PDB REMARK 900 LYSOZYME TRICLINIC CRYSTAL FORM REMARK 900 RELATED ID: 8LYZ RELATED DB: PDB REMARK 900 LYSOZYME IODINE-INACTIVATED REMARK 900 RELATED ID: 2C8P RELATED DB: PDB REMARK 900 LYSOZYME (60SEC) AND UV LASER EXCITED REMARK 900 FLUORESCENCE DBREF 2C8O A 1 129 UNP P00698 LYSC_CHICK 19 147 SEQRES 1 A 129 LYS VAL PHE GLY ARG CYS GLU LEU ALA ALA ALA MET LYS SEQRES 2 A 129 ARG HIS GLY LEU ASP ASN TYR ARG GLY TYR SER LEU GLY SEQRES 3 A 129 ASN TRP VAL CYS ALA ALA LYS PHE GLU SER ASN PHE ASN SEQRES 4 A 129 THR GLN ALA THR ASN ARG ASN THR ASP GLY SER THR ASP SEQRES 5 A 129 TYR GLY ILE LEU GLN ILE ASN SER ARG TRP TRP CYS ASN SEQRES 6 A 129 ASP GLY ARG THR PRO GLY SER ARG ASN LEU CYS ASN ILE SEQRES 7 A 129 PRO CYS SER ALA LEU LEU SER SER ASP ILE THR ALA SER SEQRES 8 A 129 VAL ASN CYS ALA LYS LYS ILE VAL SER ASP GLY ASN GLY SEQRES 9 A 129 MET ASN ALA TRP VAL ALA TRP ARG ASN ARG CYS LYS GLY SEQRES 10 A 129 THR ASP VAL GLN ALA TRP ILE ARG GLY CYS ARG LEU FORMUL 2 HOH *133(H2 O1) HELIX 1 1 GLY A 4 HIS A 15 1 12 HELIX 2 2 SER A 24 ASN A 37 1 14 HELIX 3 3 CYS A 80 SER A 85 5 6 HELIX 4 4 ILE A 88 SER A 100 1 13 HELIX 5 5 ASN A 103 ALA A 107 5 5 HELIX 6 6 TRP A 108 CYS A 115 1 8 HELIX 7 7 ASP A 119 ARG A 125 5 7 SHEET 1 AA 3 THR A 43 ARG A 45 0 SHEET 2 AA 3 THR A 51 TYR A 53 -1 O ASP A 52 N ASN A 44 SHEET 3 AA 3 ILE A 58 ASN A 59 -1 O ILE A 58 N TYR A 53 SSBOND 1 CYS A 6 CYS A 127 1555 1555 2.03 SSBOND 2 CYS A 30 CYS A 115 1555 1555 2.06 SSBOND 3 CYS A 64 CYS A 80 1555 1555 2.05 SSBOND 4 CYS A 76 CYS A 94 1555 1555 2.03 CRYST1 78.730 78.730 36.916 90.00 90.00 90.00 P 43 21 2 8 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 0.012702 0.000000 0.000000 0.00000 SCALE2 0.000000 0.012702 0.000000 0.00000 SCALE3 0.000000 0.000000 0.027089 0.00000 ATOM 1 N LYS A 1 3.128 10.145 10.078 1.00 13.61 N ATOM 2 CA LYS A 1 2.631 10.470 8.732 1.00 15.18 C ATOM 3 C LYS A 1 2.325 11.960 8.568 1.00 13.75 C ATOM 4 O LYS A 1 2.110 12.689 9.551 1.00 13.49 O ATOM 5 CB LYS A 1 1.446 9.608 8.435 1.00 16.90 C ATOM 6 CG LYS A 1 0.291 9.967 9.233 1.00 16.34 C ATOM 7 CD LYS A 1 -0.659 10.607 8.309 1.00 16.86 C ATOM 8 CE LYS A 1 -2.002 10.013 8.505 1.00 17.95 C ATOM 9 NZ LYS A 1 -2.976 10.775 7.702 1.00 19.81 N ATOM 10 N VAL A 2 2.342 12.402 7.317 1.00 13.21 N ATOM 11 CA VAL A 2 2.186 13.806 6.984 1.00 12.25 C ATOM 12 C VAL A 2 0.776 14.042 6.465 1.00 12.68 C ATOM 13 O VAL A 2 0.401 13.528 5.399 1.00 13.58 O ATOM 14 CB VAL A 2 3.260 14.275 5.958 1.00 11.97 C ATOM 15 CG1 VAL A 2 3.078 15.748 5.630 1.00 12.31 C ATOM 16 CG2 VAL A 2 4.693 14.018 6.495 1.00 11.30 C ATOM 17 N PHE A 3 -0.004 14.807 7.225 1.00 11.61 N ATOM 18 CA PHE A 3 -1.382 15.103 6.843 1.00 11.77 C ATOM 19 C PHE A 3 -1.417 16.183 5.796 1.00 12.56 C ATOM 20 O PHE A 3 -0.583 17.088 5.782 1.00 12.44 O ATOM 21 CB PHE A 3 -2.172 15.632 8.042 1.00 11.92 C ATOM 22 CG PHE A 3 -2.733 14.562 8.933 1.00 11.20 C ATOM 23 CD1 PHE A 3 -4.072 14.191 8.825 1.00 12.05 C ATOM 24 CD2 PHE A 3 -1.935 13.930 9.894 1.00 12.22 C ATOM 25 CE1 PHE A 3 -4.607 13.218 9.646 1.00 11.25 C ATOM 26 CE2 PHE A 3 -2.463 12.948 10.719 1.00 11.59 C ATOM 27 CZ PHE A 3 -3.811 12.591 10.602 1.00 12.89 C ATOM 28 N GLY A 4 -2.425 16.101 4.933 1.00 12.81 N ATOM 29 CA GLY A 4 -2.825 17.262 4.162 1.00 12.84 C ATOM 30 C GLY A 4 -3.536 18.275 5.042 1.00 12.64 C ATOM 31 O GLY A 4 -4.072 17.948 6.103 1.00 12.66 O ATOM 32 N ARG A 5 -3.547 19.519 4.594 1.00 13.27 N ATOM 33 CA ARG A 5 -4.208 20.591 5.323 1.00 12.99 C ATOM 34 C ARG A 5 -5.676 20.304 5.695 1.00 13.39 C ATOM 35 O ARG A 5 -6.063 20.378 6.870 1.00 13.55 O ATOM 36 CB ARG A 5 -4.094 21.886 4.518 1.00 13.37 C ATOM 37 CG ARG A 5 -4.707 23.095 5.187 1.00 13.46 C ATOM 38 CD ARG A 5 -4.528 24.360 4.323 1.00 13.99 C ATOM 39 NE ARG A 5 -5.115 24.278 2.978 1.00 16.99 N ATOM 40 CZ ARG A 5 -6.391 24.530 2.683 1.00 17.05 C ATOM 41 NH1 ARG A 5 -7.267 24.880 3.621 1.00 15.92 N ATOM 42 NH2 ARG A 5 -6.803 24.429 1.428 1.00 18.06 N ATOM 43 N CYS A 6 -6.495 20.004 4.681 1.00 13.88 N ATOM 44 CA CYS A 6 -7.915 19.719 4.905 1.00 14.40 C ATOM 45 C CYS A 6 -8.134 18.385 5.612 1.00 13.79 C ATOM 46 O CYS A 6 -9.055 18.234 6.415 1.00 14.30 O ATOM 47 CB CYS A 6 -8.710 19.768 3.593 1.00 15.06 C ATOM 48 SG CYS A 6 -8.832 21.431 2.897 1.00 17.35 S ATOM 49 N GLU A 7 -7.263 17.426 5.318 1.00 12.96 N ATOM 50 CA GLU A 7 -7.315 16.128 5.972 1.00 12.99 C ATOM 51 C GLU A 7 -7.133 16.285 7.489 1.00 12.66 C ATOM 52 O GLU A 7 -7.850 15.667 8.272 1.00 13.28 O ATOM 53 CB GLU A 7 -6.257 15.193 5.392 1.00 13.89 C ATOM 54 CG GLU A 7 -6.312 13.808 5.985 1.00 15.20 C ATOM 55 CD GLU A 7 -5.130 12.950 5.617 1.00 16.85 C ATOM 56 OE1 GLU A 7 -4.099 13.490 5.144 1.00 17.29 O ATOM 57 OE2 GLU A 7 -5.240 11.724 5.815 1.00 18.69 O ATOM 58 N LEU A 8 -6.180 17.126 7.897 1.00 11.90 N ATOM 59 CA LEU A 8 -5.974 17.377 9.324 1.00 11.65 C ATOM 60 C LEU A 8 -7.105 18.183 9.954 1.00 11.37 C ATOM 61 O LEU A 8 -7.506 17.891 11.083 1.00 11.26 O ATOM 62 CB LEU A 8 -4.621 18.063 9.584 1.00 11.58 C ATOM 63 CG LEU A 8 -4.253 18.270 11.062 1.00 10.33 C ATOM 64 CD1 LEU A 8 -4.173 16.950 11.805 1.00 10.50 C ATOM 65 CD2 LEU A 8 -2.934 19.016 11.167 1.00 11.88 C ATOM 66 N ALA A 9 -7.613 19.194 9.240 1.00 12.11 N ATOM 67 CA ALA A 9 -8.752 19.969 9.720 1.00 12.71 C ATOM 68 C ALA A 9 -9.920 19.042 10.039 1.00 12.70 C ATOM 69 O ALA A 9 -10.525 19.127 11.114 1.00 13.26 O ATOM 70 CB ALA A 9 -9.164 21.019 8.696 1.00 12.78 C ATOM 71 N ALA A 10 -10.213 18.138 9.105 1.00 13.54 N ATOM 72 CA ALA A 10 -11.295 17.164 9.282 1.00 13.67 C ATOM 73 C ALA A 10 -11.052 16.228 10.466 1.00 13.86 C ATOM 74 O ALA A 10 -11.953 15.980 11.265 1.00 14.90 O ATOM 75 CB ALA A 10 -11.495 16.370 7.999 1.00 14.09 C ATOM 76 N ALA A 11 -9.831 15.713 10.589 1.00 13.60 N ATOM 77 CA ALA A 11 -9.484 14.836 11.704 1.00 13.52 C ATOM 78 C ALA A 11 -9.588 15.571 13.046 1.00 13.54 C ATOM 79 O ALA A 11 -10.074 15.023 14.035 1.00 13.81 O ATOM 80 CB ALA A 11 -8.096 14.261 11.515 1.00 14.15 C ATOM 81 N MET A 12 -9.117 16.818 13.078 1.00 13.47 N ATOM 82 CA MET A 12 -9.202 17.622 14.291 1.00 13.11 C ATOM 83 C MET A 12 -10.641 17.885 14.709 1.00 13.90 C ATOM 84 O MET A 12 -10.956 17.860 15.899 1.00 13.92 O ATOM 85 CB MET A 12 -8.437 18.931 14.120 1.00 12.95 C ATOM 86 CG MET A 12 -6.942 18.758 14.262 1.00 11.63 C ATOM 87 SD MET A 12 -6.124 20.305 13.913 1.00 11.32 S ATOM 88 CE MET A 12 -4.547 19.997 14.715 1.00 11.30 C ATOM 89 N LYS A 13 -11.501 18.124 13.720 1.00 15.47 N ATOM 90 CA LYS A 13 -12.918 18.377 13.980 1.00 17.07 C ATOM 91 C LYS A 13 -13.584 17.113 14.497 1.00 17.59 C ATOM 92 O LYS A 13 -14.349 17.160 15.462 1.00 17.88 O ATOM 93 CB LYS A 13 -13.621 18.876 12.722 1.00 17.32 C ATOM 94 CG LYS A 13 -15.067 19.281 12.957 1.00 19.51 C ATOM 95 CD LYS A 13 -15.720 19.796 11.683 1.00 21.73 C ATOM 96 CE LYS A 13 -17.083 20.409 11.984 1.00 24.94 C ATOM 97 NZ LYS A 13 -17.937 19.502 12.804 1.00 26.73 N ATOM 98 N ARG A 14 -13.258 15.984 13.876 1.00 18.36 N ATOM 99 CA ARG A 14 -13.814 14.704 14.295 1.00 19.33 C ATOM 100 C ARG A 14 -13.420 14.387 15.754 1.00 19.34 C ATOM 101 O ARG A 14 -14.210 13.811 16.502 1.00 19.59 O ATOM 102 CB ARG A 14 -13.447 13.595 13.283 1.00 19.77 C ATOM 103 CG ARG A 14 -12.526 12.502 13.763 1.00 21.42 C ATOM 104 CD ARG A 14 -12.016 11.625 12.605 1.00 21.53 C ATOM 105 NE ARG A 14 -10.705 11.075 12.935 1.00 23.36 N ATOM 106 CZ ARG A 14 -10.502 9.933 13.594 1.00 20.10 C ATOM 107 NH1 ARG A 14 -11.520 9.151 13.984 1.00 21.10 N ATOM 108 NH2 ARG A 14 -9.267 9.572 13.863 1.00 6.03 N ATOM 109 N HIS A 15 -12.217 14.811 16.156 1.00 18.82 N ATOM 110 CA HIS A 15 -11.705 14.568 17.511 1.00 19.02 C ATOM 111 C HIS A 15 -12.059 15.667 18.518 1.00 18.54 C ATOM 112 O HIS A 15 -11.557 15.676 19.646 1.00 19.26 O ATOM 113 CB HIS A 15 -10.194 14.326 17.477 1.00 19.17 C ATOM 114 CG HIS A 15 -9.812 13.003 16.891 1.00 19.35 C ATOM 115 ND1 HIS A 15 -9.564 11.891 17.665 1.00 21.73 N ATOM 116 CD2 HIS A 15 -9.647 12.613 15.606 1.00 18.76 C ATOM 117 CE1 HIS A 15 -9.257 10.872 16.881 1.00 20.82 C ATOM 118 NE2 HIS A 15 -9.292 11.286 15.628 1.00 21.50 N ATOM 119 N GLY A 16 -12.924 16.591 18.107 1.00 18.25 N ATOM 120 CA GLY A 16 -13.531 17.562 19.020 1.00 17.87 C ATOM 121 C GLY A 16 -12.754 18.840 19.272 1.00 17.36 C ATOM 122 O GLY A 16 -13.016 19.547 20.241 1.00 17.43 O ATOM 123 N LEU A 17 -11.804 19.155 18.404 1.00 17.12 N ATOM 124 CA LEU A 17 -10.979 20.344 18.610 1.00 16.75 C ATOM 125 C LEU A 17 -11.597 21.636 18.061 1.00 17.50 C ATOM 126 O LEU A 17 -11.203 22.731 18.471 1.00 17.18 O ATOM 127 CB LEU A 17 -9.587 20.116 18.013 1.00 17.01 C ATOM 128 CG LEU A 17 -8.318 20.546 18.751 1.00 17.89 C ATOM 129 CD1 LEU A 17 -8.317 20.211 20.244 1.00 14.40 C ATOM 130 CD2 LEU A 17 -7.125 19.931 18.028 1.00 15.84 C ATOM 131 N ASP A 18 -12.572 21.513 17.152 1.00 17.86 N ATOM 132 CA ASP A 18 -13.216 22.692 16.560 1.00 18.50 C ATOM 133 C ASP A 18 -13.932 23.491 17.646 1.00 18.06 C ATOM 134 O ASP A 18 -14.868 23.008 18.276 1.00 18.14 O ATOM 135 CB ASP A 18 -14.193 22.306 15.434 1.00 19.67 C ATOM 136 CG ASP A 18 -14.725 23.523 14.656 1.00 22.29 C ATOM 137 OD1 ASP A 18 -14.253 24.668 14.876 1.00 26.34 O ATOM 138 OD2 ASP A 18 -15.617 23.322 13.793 1.00 27.34 O ATOM 139 N ASN A 19 -13.451 24.709 17.863 1.00 16.69 N ATOM 140 CA ASN A 19 -13.942 25.605 18.906 1.00 16.21 C ATOM 141 C ASN A 19 -13.706 25.131 20.347 1.00 14.99 C ATOM 142 O ASN A 19 -14.324 25.643 21.288 1.00 14.69 O ATOM 143 CB ASN A 19 -15.421 25.957 18.673 1.00 16.96 C ATOM 144 CG ASN A 19 -15.729 27.407 18.964 1.00 19.76 C ATOM 145 OD1 ASN A 19 -16.890 27.775 19.165 1.00 24.79 O ATOM 146 ND2 ASN A 19 -14.698 28.250 18.968 1.00 22.16 N ATOM 147 N TYR A 20 -12.786 24.181 20.528 1.00 14.39 N ATOM 148 CA TYR A 20 -12.433 23.740 21.867 1.00 13.33 C ATOM 149 C TYR A 20 -11.795 24.903 22.639 1.00 13.30 C ATOM 150 O TYR A 20 -10.865 25.551 22.143 1.00 13.19 O ATOM 151 CB TYR A 20 -11.492 22.524 21.829 1.00 13.73 C ATOM 152 CG TYR A 20 -11.337 21.893 23.196 1.00 13.00 C ATOM 153 CD1 TYR A 20 -12.221 20.903 23.635 1.00 13.24 C ATOM 154 CD2 TYR A 20 -10.332 22.308 24.072 1.00 12.24 C ATOM 155 CE1 TYR A 20 -12.105 20.342 24.910 1.00 13.79 C ATOM 156 CE2 TYR A 20 -10.209 21.751 25.349 1.00 13.85 C ATOM 157 CZ TYR A 20 -11.095 20.767 25.756 1.00 14.27 C ATOM 158 OH TYR A 20 -10.964 20.205 27.010 1.00 15.50 O ATOM 159 N ARG A 21 -12.321 25.183 23.834 1.00 12.92 N ATOM 160 CA ARG A 21 -11.905 26.346 24.632 1.00 12.50 C ATOM 161 C ARG A 21 -11.988 27.656 23.835 1.00 11.87 C ATOM 162 O ARG A 21 -11.236 28.596 24.074 1.00 12.12 O ATOM 163 CB ARG A 21 -10.509 26.151 25.229 1.00 13.64 C ATOM 164 CG ARG A 21 -10.450 25.151 26.379 1.00 17.02 C ATOM 165 CD ARG A 21 -10.803 25.798 27.711 1.00 21.67 C ATOM 166 NE ARG A 21 -11.071 24.787 28.735 1.00 26.76 N ATOM 167 CZ ARG A 21 -11.201 25.038 30.037 1.00 28.70 C ATOM 168 NH1 ARG A 21 -11.443 24.041 30.880 1.00 30.38 N ATOM 169 NH2 ARG A 21 -11.089 26.279 30.502 1.00 31.11 N ATOM 170 N GLY A 22 -12.898 27.663 22.865 1.00 11.36 N ATOM 171 CA GLY A 22 -13.174 28.834 22.043 1.00 11.30 C ATOM 172 C GLY A 22 -12.205 29.065 20.896 1.00 11.02 C ATOM 173 O GLY A 22 -12.250 30.108 20.253 1.00 11.58 O ATOM 174 N TYR A 23 -11.323 28.097 20.642 1.00 10.11 N ATOM 175 CA TYR A 23 -10.362 28.227 19.553 1.00 9.55 C ATOM 176 C TYR A 23 -10.878 27.534 18.306 1.00 9.83 C ATOM 177 O TYR A 23 -11.019 26.312 18.283 1.00 10.43 O ATOM 178 CB TYR A 23 -8.989 27.676 19.960 1.00 9.39 C ATOM 179 CG TYR A 23 -8.305 28.556 20.961 1.00 7.77 C ATOM 180 CD1 TYR A 23 -7.537 29.653 20.550 1.00 7.32 C ATOM 181 CD2 TYR A 23 -8.436 28.301 22.336 1.00 8.73 C ATOM 182 CE1 TYR A 23 -6.914 30.472 21.475 1.00 8.42 C ATOM 183 CE2 TYR A 23 -7.824 29.117 23.273 1.00 8.44 C ATOM 184 CZ TYR A 23 -7.056 30.194 22.836 1.00 9.36 C ATOM 185 OH TYR A 23 -6.423 31.006 23.742 1.00 9.67 O ATOM 186 N SER A 24 -11.180 28.329 17.284 1.00 10.34 N ATOM 187 CA SER A 24 -11.683 27.785 16.030 1.00 11.49 C ATOM 188 C SER A 24 -10.684 26.827 15.383 1.00 11.26 C ATOM 189 O SER A 24 -9.460 26.903 15.622 1.00 12.09 O ATOM 190 CB SER A 24 -11.970 28.913 15.055 1.00 11.75 C ATOM 191 OG SER A 24 -10.747 29.505 14.654 1.00 13.72 O ATOM 192 N LEU A 25 -11.207 25.945 14.539 1.00 11.83 N ATOM 193 CA LEU A 25 -10.407 24.947 13.848 1.00 11.63 C ATOM 194 C LEU A 25 -9.178 25.518 13.137 1.00 11.22 C ATOM 195 O LEU A 25 -8.118 24.889 13.140 1.00 10.68 O ATOM 196 CB LEU A 25 -11.276 24.195 12.849 1.00 11.89 C ATOM 197 CG LEU A 25 -10.778 22.875 12.276 1.00 12.52 C ATOM 198 CD1 LEU A 25 -10.406 21.862 13.355 1.00 15.29 C ATOM 199 CD2 LEU A 25 -11.873 22.311 11.368 1.00 12.94 C ATOM 200 N GLY A 26 -9.308 26.685 12.520 1.00 10.42 N ATOM 201 CA GLY A 26 -8.181 27.322 11.833 1.00 9.62 C ATOM 202 C GLY A 26 -7.001 27.605 12.747 1.00 9.10 C ATOM 203 O GLY A 26 -5.838 27.524 12.327 1.00 9.57 O ATOM 204 N ASN A 27 -7.287 27.938 13.998 1.00 8.78 N ATOM 205 CA ASN A 27 -6.205 28.136 14.976 1.00 8.44 C ATOM 206 C ASN A 27 -5.388 26.880 15.189 1.00 8.56 C ATOM 207 O ASN A 27 -4.156 26.932 15.238 1.00 8.51 O ATOM 208 CB ASN A 27 -6.745 28.605 16.322 1.00 9.60 C ATOM 209 CG ASN A 27 -7.092 30.061 16.311 1.00 8.30 C ATOM 210 OD1 ASN A 27 -6.201 30.917 16.367 1.00 9.36 O ATOM 211 ND2 ASN A 27 -8.385 30.360 16.202 1.00 10.15 N ATOM 212 N TRP A 28 -6.086 25.765 15.340 1.00 8.41 N ATOM 213 CA TRP A 28 -5.459 24.469 15.534 1.00 8.02 C ATOM 214 C TRP A 28 -4.670 24.008 14.330 1.00 8.28 C ATOM 215 O TRP A 28 -3.568 23.481 14.479 1.00 8.49 O ATOM 216 CB TRP A 28 -6.517 23.440 15.917 1.00 8.67 C ATOM 217 CG TRP A 28 -7.142 23.739 17.241 1.00 8.73 C ATOM 218 CD1 TRP A 28 -8.388 24.269 17.466 1.00 9.51 C ATOM 219 CD2 TRP A 28 -6.545 23.564 18.537 1.00 8.59 C ATOM 220 NE1 TRP A 28 -8.608 24.400 18.815 1.00 9.38 N ATOM 221 CE2 TRP A 28 -7.492 23.986 19.495 1.00 8.40 C ATOM 222 CE3 TRP A 28 -5.304 23.072 18.979 1.00 10.44 C ATOM 223 CZ2 TRP A 28 -7.249 23.930 20.870 1.00 9.41 C ATOM 224 CZ3 TRP A 28 -5.055 23.033 20.356 1.00 9.73 C ATOM 225 CH2 TRP A 28 -6.025 23.467 21.285 1.00 9.35 C ATOM 226 N VAL A 29 -5.221 24.218 13.139 1.00 8.19 N ATOM 227 CA VAL A 29 -4.529 23.853 11.897 1.00 8.04 C ATOM 228 C VAL A 29 -3.284 24.720 11.694 1.00 8.10 C ATOM 229 O VAL A 29 -2.213 24.209 11.354 1.00 8.28 O ATOM 230 CB VAL A 29 -5.485 23.903 10.679 1.00 8.38 C ATOM 231 CG1 VAL A 29 -4.754 23.584 9.386 1.00 7.98 C ATOM 232 CG2 VAL A 29 -6.623 22.915 10.858 1.00 9.35 C ATOM 233 N CYS A 30 -3.426 26.026 11.892 1.00 8.03 N ATOM 234 CA CYS A 30 -2.291 26.948 11.830 1.00 8.00 C ATOM 235 C CYS A 30 -1.183 26.547 12.823 1.00 8.27 C ATOM 236 O CYS A 30 -0.006 26.531 12.465 1.00 7.53 O ATOM 237 CB CYS A 30 -2.773 28.380 12.108 1.00 8.16 C ATOM 238 SG CYS A 30 -1.501 29.611 11.893 1.00 9.25 S ATOM 239 N ALA A 31 -1.557 26.224 14.058 1.00 7.71 N ATOM 240 CA ALA A 31 -0.568 25.825 15.059 1.00 7.33 C ATOM 241 C ALA A 31 0.163 24.564 14.599 1.00 7.16 C ATOM 242 O ALA A 31 1.392 24.482 14.659 1.00 8.18 O ATOM 243 CB ALA A 31 -1.246 25.606 16.417 1.00 7.92 C ATOM 244 N ALA A 32 -0.589 23.583 14.105 1.00 6.80 N ATOM 245 CA ALA A 32 0.029 22.340 13.637 1.00 6.55 C ATOM 246 C ALA A 32 0.955 22.589 12.442 1.00 6.78 C ATOM 247 O ALA A 32 2.033 21.992 12.346 1.00 7.67 O ATOM 248 CB ALA A 32 -1.014 21.312 13.288 1.00 6.89 C ATOM 249 N LYS A 33 0.553 23.475 11.532 1.00 7.82 N ATOM 250 CA LYS A 33 1.394 23.798 10.391 1.00 8.03 C ATOM 251 C LYS A 33 2.787 24.264 10.818 1.00 7.85 C ATOM 252 O LYS A 33 3.806 23.752 10.331 1.00 8.24 O ATOM 253 CB LYS A 33 0.735 24.888 9.529 1.00 8.47 C ATOM 254 CG LYS A 33 1.661 25.425 8.430 1.00 9.76 C ATOM 255 CD LYS A 33 1.822 24.412 7.310 1.00 11.54 C ATOM 256 CE LYS A 33 2.656 24.995 6.177 1.00 14.27 C ATOM 257 NZ LYS A 33 2.908 23.979 5.121 1.00 17.52 N ATOM 258 N PHE A 34 2.835 25.218 11.740 1.00 8.63 N ATOM 259 CA PHE A 34 4.121 25.801 12.116 1.00 8.68 C ATOM 260 C PHE A 34 4.864 25.014 13.182 1.00 8.91 C ATOM 261 O PHE A 34 6.097 25.103 13.283 1.00 9.71 O ATOM 262 CB PHE A 34 3.960 27.280 12.461 1.00 9.36 C ATOM 263 CG PHE A 34 3.475 28.100 11.297 1.00 9.07 C ATOM 264 CD1 PHE A 34 4.160 28.064 10.084 1.00 10.16 C ATOM 265 CD2 PHE A 34 2.335 28.884 11.401 1.00 11.45 C ATOM 266 CE1 PHE A 34 3.723 28.802 9.001 1.00 9.43 C ATOM 267 CE2 PHE A 34 1.897 29.623 10.319 1.00 13.19 C ATOM 268 CZ PHE A 34 2.586 29.581 9.125 1.00 10.82 C ATOM 269 N GLU A 35 4.136 24.232 13.967 1.00 8.48 N ATOM 270 CA GLU A 35 4.808 23.360 14.924 1.00 8.31 C ATOM 271 C GLU A 35 5.477 22.166 14.250 1.00 8.57 C ATOM 272 O GLU A 35 6.615 21.824 14.570 1.00 8.44 O ATOM 273 CB GLU A 35 3.820 22.847 15.971 1.00 8.36 C ATOM 274 CG GLU A 35 3.315 23.903 16.943 1.00 7.91 C ATOM 275 CD GLU A 35 4.402 24.492 17.834 1.00 8.69 C ATOM 276 OE1 GLU A 35 5.549 23.995 17.815 1.00 9.74 O ATOM 277 OE2 GLU A 35 4.093 25.458 18.567 1.00 9.28 O ATOM 278 N SER A 36 4.775 21.518 13.308 1.00 7.95 N ATOM 279 CA SER A 36 5.232 20.223 12.774 1.00 8.00 C ATOM 280 C SER A 36 5.180 20.088 11.260 1.00 8.34 C ATOM 281 O SER A 36 5.548 19.040 10.737 1.00 8.62 O ATOM 282 CB SER A 36 4.375 19.104 13.352 1.00 8.33 C ATOM 283 OG SER A 36 3.059 19.233 12.824 1.00 8.13 O ATOM 284 N ASN A 37 4.679 21.113 10.559 1.00 8.81 N ATOM 285 CA ASN A 37 4.375 20.995 9.122 1.00 9.10 C ATOM 286 C ASN A 37 3.460 19.800 8.829 1.00 8.43 C ATOM 287 O ASN A 37 3.586 19.140 7.797 1.00 9.43 O ATOM 288 CB ASN A 37 5.643 20.962 8.250 1.00 9.44 C ATOM 289 CG ASN A 37 5.386 21.446 6.835 1.00 12.12 C ATOM 290 OD1 ASN A 37 4.360 22.060 6.553 1.00 14.21 O ATOM 291 ND2 ASN A 37 6.329 21.168 5.939 1.00 16.12 N ATOM 292 N PHE A 38 2.569 19.522 9.778 1.00 8.21 N ATOM 293 CA PHE A 38 1.533 18.472 9.667 1.00 8.12 C ATOM 294 C PHE A 38 2.084 17.038 9.740 1.00 8.34 C ATOM 295 O PHE A 38 1.391 16.071 9.385 1.00 8.70 O ATOM 296 CB PHE A 38 0.703 18.616 8.376 1.00 8.31 C ATOM 297 CG PHE A 38 -0.005 19.942 8.212 1.00 8.17 C ATOM 298 CD1 PHE A 38 -0.545 20.641 9.294 1.00 8.62 C ATOM 299 CD2 PHE A 38 -0.186 20.460 6.932 1.00 10.34 C ATOM 300 CE1 PHE A 38 -1.232 21.853 9.094 1.00 9.33 C ATOM 301 CE2 PHE A 38 -0.857 21.669 6.727 1.00 10.63 C ATOM 302 CZ PHE A 38 -1.392 22.361 7.812 1.00 10.23 C ATOM 303 N ASN A 39 3.317 16.916 10.225 1.00 7.81 N ATOM 304 CA ASN A 39 3.983 15.631 10.367 1.00 7.58 C ATOM 305 C ASN A 39 3.841 15.073 11.780 1.00 8.05 C ATOM 306 O ASN A 39 4.400 15.633 12.730 1.00 8.20 O ATOM 307 CB ASN A 39 5.459 15.786 9.980 1.00 7.97 C ATOM 308 CG ASN A 39 6.188 14.464 9.881 1.00 8.72 C ATOM 309 OD1 ASN A 39 5.677 13.425 10.270 1.00 8.37 O ATOM 310 ND2 ASN A 39 7.409 14.511 9.350 1.00 13.88 N ATOM 311 N THR A 40 3.108 13.968 11.919 1.00 8.73 N ATOM 312 CA THR A 40 2.931 13.359 13.244 1.00 8.89 C ATOM 313 C THR A 40 4.243 12.897 13.879 1.00 8.70 C ATOM 314 O THR A 40 4.313 12.794 15.096 1.00 9.10 O ATOM 315 CB THR A 40 1.954 12.163 13.245 1.00 8.76 C ATOM 316 OG1 THR A 40 2.548 11.048 12.572 1.00 9.77 O ATOM 317 CG2 THR A 40 0.646 12.525 12.569 1.00 9.75 C ATOM 318 N GLN A 41 5.265 12.628 13.066 1.00 9.02 N ATOM 319 CA GLN A 41 6.511 12.069 13.588 1.00 8.81 C ATOM 320 C GLN A 41 7.536 13.120 13.968 1.00 9.06 C ATOM 321 O GLN A 41 8.644 12.761 14.367 1.00 10.29 O ATOM 322 CB GLN A 41 7.120 11.077 12.594 1.00 9.30 C ATOM 323 CG GLN A 41 6.217 9.884 12.328 1.00 9.37 C ATOM 324 CD GLN A 41 6.930 8.758 11.632 1.00 9.82 C ATOM 325 OE1 GLN A 41 6.828 8.587 10.399 1.00 12.03 O ATOM 326 NE2 GLN A 41 7.684 7.995 12.397 1.00 8.64 N ATOM 327 N ALA A 42 7.171 14.398 13.875 1.00 8.29 N ATOM 328 CA ALA A 42 8.067 15.497 14.204 1.00 8.57 C ATOM 329 C ALA A 42 8.538 15.431 15.663 1.00 8.40 C ATOM 330 O ALA A 42 7.734 15.274 16.577 1.00 7.79 O ATOM 331 CB ALA A 42 7.366 16.815 13.953 1.00 8.52 C ATOM 332 N THR A 43 9.844 15.571 15.864 1.00 8.51 N ATOM 333 CA THR A 43 10.408 15.717 17.207 1.00 9.61 C ATOM 334 C THR A 43 11.413 16.860 17.175 1.00 10.21 C ATOM 335 O THR A 43 12.043 17.109 16.153 1.00 11.03 O ATOM 336 CB THR A 43 11.153 14.443 17.688 1.00 9.45 C ATOM 337 OG1 THR A 43 12.236 14.157 16.792 1.00 11.23 O ATOM 338 CG2 THR A 43 10.220 13.240 17.774 1.00 9.45 C ATOM 339 N ASN A 44 11.581 17.553 18.292 1.00 9.86 N ATOM 340 CA ASN A 44 12.588 18.597 18.383 1.00 10.90 C ATOM 341 C ASN A 44 13.072 18.696 19.816 1.00 10.58 C ATOM 342 O ASN A 44 12.282 18.794 20.739 1.00 10.15 O ATOM 343 CB ASN A 44 12.034 19.936 17.883 1.00 11.61 C ATOM 344 CG ASN A 44 11.924 19.991 16.362 1.00 14.85 C ATOM 345 OD1 ASN A 44 12.934 20.045 15.643 1.00 19.30 O ATOM 346 ND2 ASN A 44 10.695 19.957 15.863 1.00 18.88 N ATOM 347 N ARG A 45 14.385 18.673 19.991 1.00 11.96 N ATOM 348 CA ARG A 45 14.992 18.770 21.309 1.00 13.09 C ATOM 349 C ARG A 45 15.097 20.231 21.735 1.00 13.69 C ATOM 350 O ARG A 45 15.566 21.078 20.959 1.00 14.36 O ATOM 351 CB ARG A 45 16.379 18.128 21.269 1.00 13.41 C ATOM 352 CG ARG A 45 16.997 17.878 22.647 1.00 17.00 C ATOM 353 CD ARG A 45 16.513 16.551 23.204 1.00 20.98 C ATOM 354 NE ARG A 45 17.524 15.491 23.137 1.00 27.82 N ATOM 355 CZ ARG A 45 18.062 14.900 24.209 1.00 27.90 C ATOM 356 NH1 ARG A 45 17.688 15.237 25.445 1.00 28.88 N ATOM 357 NH2 ARG A 45 18.960 13.941 24.046 1.00 30.86 N ATOM 358 N ASN A 46 14.677 20.502 22.969 1.00 14.23 N ATOM 359 CA ASN A 46 14.784 21.835 23.574 1.00 15.67 C ATOM 360 C ASN A 46 16.119 21.988 24.290 1.00 17.19 C ATOM 361 O ASN A 46 16.738 20.995 24.684 1.00 17.56 O ATOM 362 CB ASN A 46 13.623 22.061 24.546 1.00 15.78 C ATOM 363 CG ASN A 46 12.254 21.886 23.878 1.00 14.54 C ATOM 364 OD1 ASN A 46 11.362 21.227 24.420 1.00 18.44 O ATOM 365 ND2 ASN A 46 12.096 22.471 22.696 1.00 17.89 N ATOM 366 N THR A 47 16.560 23.237 24.457 1.00 19.17 N ATOM 367 CA THR A 47 17.852 23.536 25.088 1.00 20.64 C ATOM 368 C THR A 47 17.991 22.932 26.497 1.00 20.15 C ATOM 369 O THR A 47 19.085 22.521 26.904 1.00 20.92 O ATOM 370 CB THR A 47 18.127 25.069 25.123 1.00 20.83 C ATOM 371 OG1 THR A 47 16.990 25.761 25.657 1.00 23.95 O ATOM 372 CG2 THR A 47 18.392 25.589 23.718 1.00 22.19 C ATOM 373 N ASP A 48 16.865 22.849 27.204 1.00 19.64 N ATOM 374 CA ASP A 48 16.819 22.340 28.576 1.00 18.94 C ATOM 375 C ASP A 48 16.815 20.816 28.683 1.00 18.50 C ATOM 376 O ASP A 48 16.776 20.270 29.790 1.00 18.75 O ATOM 377 CB ASP A 48 15.624 22.940 29.339 1.00 19.27 C ATOM 378 CG ASP A 48 14.267 22.394 28.874 1.00 20.05 C ATOM 379 OD1 ASP A 48 14.194 21.654 27.874 1.00 19.82 O ATOM 380 OD2 ASP A 48 13.253 22.696 29.532 1.00 24.52 O ATOM 381 N GLY A 49 16.826 20.143 27.534 1.00 16.97 N ATOM 382 CA GLY A 49 16.893 18.684 27.470 1.00 15.53 C ATOM 383 C GLY A 49 15.547 18.003 27.269 1.00 13.82 C ATOM 384 O GLY A 49 15.503 16.793 27.018 1.00 14.83 O ATOM 385 N SER A 50 14.453 18.759 27.398 1.00 12.41 N ATOM 386 CA SER A 50 13.119 18.230 27.110 1.00 10.90 C ATOM 387 C SER A 50 13.006 18.102 25.593 1.00 10.02 C ATOM 388 O SER A 50 13.859 18.615 24.861 1.00 9.78 O ATOM 389 CB SER A 50 12.010 19.130 27.676 1.00 10.60 C ATOM 390 OG SER A 50 12.023 20.396 27.035 1.00 12.30 O ATOM 391 N THR A 51 11.965 17.405 25.144 1.00 8.18 N ATOM 392 CA THR A 51 11.744 17.167 23.713 1.00 7.38 C ATOM 393 C THR A 51 10.278 17.437 23.414 1.00 6.84 C ATOM 394 O THR A 51 9.408 17.154 24.239 1.00 6.39 O ATOM 395 CB THR A 51 12.131 15.727 23.328 1.00 7.23 C ATOM 396 OG1 THR A 51 13.504 15.525 23.654 1.00 7.89 O ATOM 397 CG2 THR A 51 11.963 15.449 21.829 1.00 8.86 C ATOM 398 N ASP A 52 10.024 18.004 22.233 1.00 7.17 N ATOM 399 CA ASP A 52 8.663 18.263 21.737 1.00 8.02 C ATOM 400 C ASP A 52 8.296 17.175 20.728 1.00 7.54 C ATOM 401 O ASP A 52 9.130 16.793 19.897 1.00 7.85 O ATOM 402 CB ASP A 52 8.590 19.619 21.037 1.00 8.77 C ATOM 403 CG ASP A 52 8.699 20.805 21.992 1.00 12.45 C ATOM 404 OD1 ASP A 52 8.745 20.624 23.223 1.00 13.61 O ATOM 405 OD2 ASP A 52 8.693 21.954 21.492 1.00 17.94 O ATOM 406 N TYR A 53 7.053 16.689 20.795 1.00 7.20 N ATOM 407 CA TYR A 53 6.622 15.522 20.015 1.00 6.96 C ATOM 408 C TYR A 53 5.324 15.748 19.269 1.00 6.97 C ATOM 409 O TYR A 53 4.347 16.234 19.840 1.00 7.74 O ATOM 410 CB TYR A 53 6.406 14.302 20.925 1.00 7.38 C ATOM 411 CG TYR A 53 7.633 13.825 21.649 1.00 7.28 C ATOM 412 CD1 TYR A 53 8.389 12.771 21.143 1.00 6.67 C ATOM 413 CD2 TYR A 53 8.025 14.410 22.862 1.00 7.13 C ATOM 414 CE1 TYR A 53 9.542 12.317 21.818 1.00 6.78 C ATOM 415 CE2 TYR A 53 9.160 13.980 23.531 1.00 6.65 C ATOM 416 CZ TYR A 53 9.909 12.934 23.012 1.00 6.56 C ATOM 417 OH TYR A 53 11.028 12.483 23.679 1.00 7.94 O ATOM 418 N GLY A 54 5.333 15.359 18.000 1.00 6.90 N ATOM 419 CA GLY A 54 4.096 15.216 17.239 1.00 7.40 C ATOM 420 C GLY A 54 3.592 16.478 16.566 1.00 7.73 C ATOM 421 O GLY A 54 4.288 17.498 16.491 1.00 7.08 O ATOM 422 N ILE A 55 2.356 16.393 16.072 1.00 8.54 N ATOM 423 CA ILE A 55 1.782 17.454 15.241 1.00 10.69 C ATOM 424 C ILE A 55 1.680 18.796 15.945 1.00 9.81 C ATOM 425 O ILE A 55 1.731 19.835 15.295 1.00 9.58 O ATOM 426 CB ILE A 55 0.385 17.108 14.648 1.00 11.68 C ATOM 427 CG1 ILE A 55 -0.640 16.770 15.737 1.00 12.12 C ATOM 428 CG2 ILE A 55 0.495 16.037 13.609 1.00 13.31 C ATOM 429 CD1 ILE A 55 -2.120 16.808 15.268 1.00 13.21 C ATOM 430 N LEU A 56 1.522 18.759 17.268 1.00 9.28 N ATOM 431 CA LEU A 56 1.440 19.969 18.066 1.00 9.22 C ATOM 432 C LEU A 56 2.643 20.153 19.003 1.00 8.47 C ATOM 433 O LEU A 56 2.638 20.988 19.909 1.00 9.02 O ATOM 434 CB LEU A 56 0.112 20.025 18.825 1.00 9.32 C ATOM 435 CG LEU A 56 -1.084 20.358 17.917 1.00 9.84 C ATOM 436 CD1 LEU A 56 -2.384 20.071 18.654 1.00 11.38 C ATOM 437 CD2 LEU A 56 -1.043 21.826 17.471 1.00 12.73 C ATOM 438 N GLN A 57 3.691 19.365 18.765 1.00 8.25 N ATOM 439 CA GLN A 57 4.983 19.586 19.425 1.00 8.09 C ATOM 440 C GLN A 57 4.842 19.723 20.951 1.00 8.71 C ATOM 441 O GLN A 57 5.308 20.685 21.578 1.00 9.82 O ATOM 442 CB GLN A 57 5.715 20.773 18.785 1.00 7.75 C ATOM 443 CG GLN A 57 6.212 20.404 17.395 1.00 6.70 C ATOM 444 CD GLN A 57 7.312 19.372 17.449 1.00 7.52 C ATOM 445 OE1 GLN A 57 7.080 18.164 17.217 1.00 9.80 O ATOM 446 NE2 GLN A 57 8.516 19.825 17.760 1.00 7.33 N ATOM 447 N ILE A 58 4.192 18.720 21.531 1.00 8.36 N ATOM 448 CA ILE A 58 3.910 18.674 22.962 1.00 9.28 C ATOM 449 C ILE A 58 5.177 18.267 23.721 1.00 9.43 C ATOM 450 O ILE A 58 5.891 17.349 23.329 1.00 9.17 O ATOM 451 CB ILE A 58 2.703 17.767 23.218 1.00 9.59 C ATOM 452 CG1 ILE A 58 1.448 18.469 22.666 1.00 9.68 C ATOM 453 CG2 ILE A 58 2.589 17.417 24.697 1.00 10.20 C ATOM 454 CD1 ILE A 58 0.202 17.631 22.712 1.00 12.14 C ATOM 455 N ASN A 59 5.454 18.999 24.799 1.00 10.81 N ATOM 456 CA ASN A 59 6.744 19.004 25.470 1.00 12.14 C ATOM 457 C ASN A 59 6.803 18.000 26.619 1.00 11.72 C ATOM 458 O ASN A 59 5.893 17.946 27.448 1.00 12.68 O ATOM 459 CB ASN A 59 6.960 20.425 26.014 1.00 12.83 C ATOM 460 CG ASN A 59 8.391 20.714 26.435 1.00 16.31 C ATOM 461 OD1 ASN A 59 9.177 19.812 26.691 1.00 20.98 O ATOM 462 ND2 ASN A 59 8.729 22.005 26.515 1.00 20.31 N ATOM 463 N SER A 60 7.891 17.230 26.675 1.00 10.78 N ATOM 464 CA SER A 60 8.096 16.242 27.721 1.00 10.85 C ATOM 465 C SER A 60 8.337 16.847 29.106 1.00 11.42 C ATOM 466 O SER A 60 8.308 16.108 30.071 1.00 11.93 O ATOM 467 CB SER A 60 9.268 15.335 27.349 1.00 10.93 C ATOM 468 OG SER A 60 10.485 16.077 27.313 1.00 9.26 O ATOM 469 N ARG A 61 8.578 18.157 29.187 1.00 12.50 N ATOM 470 CA ARG A 61 8.813 18.849 30.465 1.00 13.71 C ATOM 471 C ARG A 61 7.597 18.715 31.384 1.00 13.54 C ATOM 472 O ARG A 61 7.748 18.525 32.585 1.00 13.41 O ATOM 473 CB ARG A 61 9.181 20.321 30.219 1.00 14.57 C ATOM 474 CG ARG A 61 9.300 21.215 31.465 1.00 18.65 C ATOM 475 CD ARG A 61 10.370 20.747 32.438 1.00 24.56 C ATOM 476 NE ARG A 61 11.706 20.702 31.847 1.00 28.69 N ATOM 477 CZ ARG A 61 12.696 19.934 32.294 1.00 29.71 C ATOM 478 NH1 ARG A 61 12.507 19.133 33.341 1.00 29.31 N ATOM 479 NH2 ARG A 61 13.874 19.959 31.682 1.00 30.74 N ATOM 480 N TRP A 62 6.399 18.744 30.804 1.00 12.97 N ATOM 481 CA TRP A 62 5.155 18.694 31.557 1.00 12.88 C ATOM 482 C TRP A 62 4.194 17.584 31.187 1.00 11.88 C ATOM 483 O TRP A 62 3.457 17.096 32.038 1.00 11.37 O ATOM 484 CB TRP A 62 4.394 20.014 31.406 1.00 14.95 C ATOM 485 CG TRP A 62 5.060 21.148 32.070 1.00 17.12 C ATOM 486 CD1 TRP A 62 5.733 22.169 31.469 1.00 19.68 C ATOM 487 CD2 TRP A 62 5.132 21.381 33.474 1.00 20.41 C ATOM 488 NE1 TRP A 62 6.209 23.045 32.420 1.00 21.85 N ATOM 489 CE2 TRP A 62 5.851 22.580 33.660 1.00 20.75 C ATOM 490 CE3 TRP A 62 4.648 20.697 34.597 1.00 20.57 C ATOM 491 CZ2 TRP A 62 6.104 23.109 34.927 1.00 21.02 C ATOM 492 CZ3 TRP A 62 4.904 21.225 35.864 1.00 20.47 C ATOM 493 CH2 TRP A 62 5.621 22.421 36.011 1.00 19.51 C ATOM 494 N TRP A 63 4.159 17.199 29.912 1.00 10.45 N ATOM 495 CA TRP A 63 2.947 16.571 29.390 1.00 10.01 C ATOM 496 C TRP A 63 3.005 15.088 29.091 1.00 9.71 C ATOM 497 O TRP A 63 1.982 14.417 29.113 1.00 9.85 O ATOM 498 CB TRP A 63 2.443 17.334 28.152 1.00 10.08 C ATOM 499 CG TRP A 63 2.259 18.791 28.456 1.00 9.84 C ATOM 500 CD1 TRP A 63 3.056 19.831 28.046 1.00 10.57 C ATOM 501 CD2 TRP A 63 1.255 19.368 29.300 1.00 10.88 C ATOM 502 NE1 TRP A 63 2.598 21.015 28.566 1.00 11.34 N ATOM 503 CE2 TRP A 63 1.497 20.761 29.343 1.00 9.72 C ATOM 504 CE3 TRP A 63 0.166 18.844 30.017 1.00 11.14 C ATOM 505 CZ2 TRP A 63 0.685 21.640 30.075 1.00 10.62 C ATOM 506 CZ3 TRP A 63 -0.638 19.720 30.747 1.00 11.97 C ATOM 507 CH2 TRP A 63 -0.374 21.101 30.761 1.00 11.00 C ATOM 508 N CYS A 64 4.193 14.579 28.787 1.00 9.43 N ATOM 509 CA CYS A 64 4.334 13.174 28.433 1.00 9.51 C ATOM 510 C CYS A 64 5.622 12.626 29.014 1.00 8.83 C ATOM 511 O CYS A 64 6.518 13.389 29.371 1.00 9.70 O ATOM 512 CB CYS A 64 4.281 12.976 26.912 1.00 9.31 C ATOM 513 SG CYS A 64 5.597 13.786 25.965 1.00 9.04 S ATOM 514 N ASN A 65 5.694 11.305 29.126 1.00 8.60 N ATOM 515 CA ASN A 65 6.916 10.670 29.584 1.00 8.85 C ATOM 516 C ASN A 65 7.777 10.130 28.459 1.00 8.26 C ATOM 517 O ASN A 65 7.317 9.318 27.658 1.00 8.55 O ATOM 518 CB ASN A 65 6.627 9.519 30.541 1.00 9.50 C ATOM 519 CG ASN A 65 7.909 8.860 30.986 1.00 10.41 C ATOM 520 OD1 ASN A 65 8.785 9.531 31.502 1.00 11.97 O ATOM 521 ND2 ASN A 65 8.061 7.565 30.694 1.00 13.23 N ATOM 522 N ASP A 66 9.035 10.576 28.433 1.00 8.30 N ATOM 523 CA ASP A 66 10.020 10.008 27.510 1.00 9.14 C ATOM 524 C ASP A 66 11.217 9.367 28.213 1.00 10.07 C ATOM 525 O ASP A 66 12.129 8.893 27.546 1.00 10.38 O ATOM 526 CB ASP A 66 10.471 11.015 26.430 1.00 8.24 C ATOM 527 CG ASP A 66 11.272 12.198 26.985 1.00 7.81 C ATOM 528 OD1 ASP A 66 11.659 12.236 28.186 1.00 8.13 O ATOM 529 OD2 ASP A 66 11.527 13.131 26.188 1.00 8.37 O ATOM 530 N GLY A 67 11.202 9.369 29.544 1.00 11.34 N ATOM 531 CA GLY A 67 12.251 8.732 30.340 1.00 12.09 C ATOM 532 C GLY A 67 13.603 9.420 30.366 1.00 12.74 C ATOM 533 O GLY A 67 14.559 8.888 30.953 1.00 13.79 O ATOM 534 N ARG A 68 13.711 10.589 29.735 1.00 11.88 N ATOM 535 CA ARG A 68 14.990 11.282 29.623 1.00 12.04 C ATOM 536 C ARG A 68 14.861 12.800 29.831 1.00 12.16 C ATOM 537 O ARG A 68 15.670 13.593 29.327 1.00 13.20 O ATOM 538 CB ARG A 68 15.658 10.951 28.284 1.00 11.81 C ATOM 539 CG ARG A 68 14.906 11.485 27.076 1.00 12.44 C ATOM 540 CD ARG A 68 15.849 11.603 25.921 1.00 14.52 C ATOM 541 NE ARG A 68 15.412 12.589 24.949 1.00 16.81 N ATOM 542 CZ ARG A 68 15.860 12.627 23.697 1.00 16.70 C ATOM 543 NH1 ARG A 68 16.752 11.728 23.307 1.00 18.91 N ATOM 544 NH2 ARG A 68 15.423 13.550 22.835 1.00 15.92 N ATOM 545 N THR A 69 13.846 13.203 30.592 1.00 11.25 N ATOM 546 CA THR A 69 13.667 14.612 30.917 1.00 11.76 C ATOM 547 C THR A 69 13.621 14.763 32.438 1.00 12.20 C ATOM 548 O THR A 69 12.548 14.734 33.025 1.00 12.63 O ATOM 549 CB THR A 69 12.401 15.216 30.260 1.00 11.37 C ATOM 550 OG1 THR A 69 12.369 14.869 28.860 1.00 10.67 O ATOM 551 CG2 THR A 69 12.398 16.731 30.398 1.00 10.97 C ATOM 552 N PRO A 70 14.797 14.900 33.072 1.00 13.21 N ATOM 553 CA PRO A 70 14.833 14.991 34.534 1.00 14.07 C ATOM 554 C PRO A 70 13.940 16.037 35.171 1.00 15.08 C ATOM 555 O PRO A 70 13.924 17.201 34.747 1.00 16.49 O ATOM 556 CB PRO A 70 16.310 15.292 34.823 1.00 14.50 C ATOM 557 CG PRO A 70 17.026 14.612 33.731 1.00 14.30 C ATOM 558 CD PRO A 70 16.161 14.899 32.509 1.00 13.81 C ATOM 559 N GLY A 71 13.201 15.610 36.194 1.00 15.08 N ATOM 560 CA GLY A 71 12.393 16.516 36.994 1.00 15.74 C ATOM 561 C GLY A 71 11.078 16.845 36.337 1.00 16.27 C ATOM 562 O GLY A 71 10.298 17.634 36.862 1.00 17.71 O ATOM 563 N SER A 72 10.826 16.234 35.182 1.00 16.29 N ATOM 564 CA SER A 72 9.621 16.519 34.410 1.00 15.93 C ATOM 565 C SER A 72 8.377 15.844 34.980 1.00 16.07 C ATOM 566 O SER A 72 8.458 15.020 35.898 1.00 16.25 O ATOM 567 CB SER A 72 9.821 16.110 32.944 1.00 16.00 C ATOM 568 OG SER A 72 9.823 14.693 32.785 1.00 15.90 O ATOM 569 N ARG A 73 7.227 16.221 34.434 1.00 15.03 N ATOM 570 CA ARG A 73 5.974 15.551 34.719 1.00 14.47 C ATOM 571 C ARG A 73 5.416 14.865 33.476 1.00 13.90 C ATOM 572 O ARG A 73 5.992 14.966 32.381 1.00 13.91 O ATOM 573 CB ARG A 73 4.958 16.562 35.259 1.00 14.83 C ATOM 574 CG ARG A 73 5.422 17.252 36.531 1.00 16.57 C ATOM 575 CD ARG A 73 5.374 16.301 37.736 1.00 19.14 C ATOM 576 NE ARG A 73 4.000 16.062 38.177 1.00 20.62 N ATOM 577 CZ ARG A 73 3.312 16.876 38.974 1.00 21.27 C ATOM 578 NH1 ARG A 73 3.863 17.986 39.450 1.00 22.80 N ATOM 579 NH2 ARG A 73 2.067 16.569 39.302 1.00 22.74 N ATOM 580 N ASN A 74 4.307 14.164 33.667 1.00 13.58 N ATOM 581 CA ASN A 74 3.613 13.440 32.616 1.00 12.89 C ATOM 582 C ASN A 74 2.103 13.636 32.815 1.00 13.13 C ATOM 583 O ASN A 74 1.357 12.682 33.070 1.00 12.88 O ATOM 584 CB ASN A 74 3.997 11.948 32.672 1.00 12.63 C ATOM 585 CG ASN A 74 3.280 11.099 31.625 1.00 12.22 C ATOM 586 OD1 ASN A 74 2.656 11.619 30.699 1.00 11.78 O ATOM 587 ND2 ASN A 74 3.362 9.774 31.777 1.00 13.05 N ATOM 588 N LEU A 75 1.666 14.887 32.667 1.00 13.16 N ATOM 589 CA LEU A 75 0.298 15.275 33.026 1.00 14.15 C ATOM 590 C LEU A 75 -0.767 14.691 32.106 1.00 13.92 C ATOM 591 O LEU A 75 -1.917 14.510 32.517 1.00 15.02 O ATOM 592 CB LEU A 75 0.175 16.798 33.132 1.00 14.29 C ATOM 593 CG LEU A 75 1.000 17.439 34.252 1.00 15.55 C ATOM 594 CD1 LEU A 75 0.913 18.954 34.183 1.00 16.29 C ATOM 595 CD2 LEU A 75 0.529 16.921 35.620 1.00 17.75 C ATOM 596 N CYS A 76 -0.378 14.355 30.873 1.00 13.47 N ATOM 597 CA CYS A 76 -1.291 13.683 29.961 1.00 12.87 C ATOM 598 C CYS A 76 -1.316 12.165 30.147 1.00 12.84 C ATOM 599 O CYS A 76 -2.087 11.472 29.487 1.00 13.23 O ATOM 600 CB CYS A 76 -0.959 14.058 28.512 1.00 12.36 C ATOM 601 SG CYS A 76 -1.373 15.785 28.186 1.00 12.35 S ATOM 602 N ASN A 77 -0.444 11.665 31.034 1.00 13.18 N ATOM 603 CA ASN A 77 -0.357 10.236 31.365 1.00 14.23 C ATOM 604 C ASN A 77 -0.186 9.348 30.136 1.00 13.81 C ATOM 605 O ASN A 77 -0.918 8.380 29.935 1.00 14.60 O ATOM 606 CB ASN A 77 -1.570 9.804 32.209 1.00 14.86 C ATOM 607 CG ASN A 77 -1.723 10.640 33.467 1.00 17.42 C ATOM 608 OD1 ASN A 77 -2.705 11.374 33.621 1.00 22.63 O ATOM 609 ND2 ASN A 77 -0.743 10.561 34.360 1.00 22.57 N ATOM 610 N ILE A 78 0.801 9.697 29.315 1.00 13.05 N ATOM 611 CA ILE A 78 1.103 8.964 28.095 1.00 12.52 C ATOM 612 C ILE A 78 2.598 8.936 27.825 1.00 11.64 C ATOM 613 O ILE A 78 3.324 9.865 28.212 1.00 10.68 O ATOM 614 CB ILE A 78 0.449 9.610 26.834 1.00 12.61 C ATOM 615 CG1 ILE A 78 0.687 11.123 26.822 1.00 12.45 C ATOM 616 CG2 ILE A 78 -1.040 9.229 26.715 1.00 14.07 C ATOM 617 CD1 ILE A 78 0.398 11.785 25.491 1.00 13.86 C ATOM 618 N PRO A 79 3.060 7.881 27.141 1.00 11.26 N ATOM 619 CA PRO A 79 4.425 7.933 26.625 1.00 10.96 C ATOM 620 C PRO A 79 4.468 8.956 25.500 1.00 9.90 C ATOM 621 O PRO A 79 3.520 9.056 24.708 1.00 9.59 O ATOM 622 CB PRO A 79 4.656 6.521 26.081 1.00 10.68 C ATOM 623 CG PRO A 79 3.296 5.968 25.815 1.00 12.10 C ATOM 624 CD PRO A 79 2.362 6.628 26.783 1.00 11.54 C ATOM 625 N CYS A 80 5.543 9.733 25.438 1.00 8.91 N ATOM 626 CA CYS A 80 5.664 10.750 24.393 1.00 8.47 C ATOM 627 C CYS A 80 5.562 10.131 22.990 1.00 8.84 C ATOM 628 O CYS A 80 5.104 10.781 22.044 1.00 8.85 O ATOM 629 CB CYS A 80 6.981 11.499 24.545 1.00 8.56 C ATOM 630 SG CYS A 80 7.148 12.452 26.064 1.00 8.17 S ATOM 631 N SER A 81 5.990 8.878 22.853 1.00 9.20 N ATOM 632 CA SER A 81 5.868 8.163 21.582 1.00 10.19 C ATOM 633 C SER A 81 4.436 8.086 21.042 1.00 10.48 C ATOM 634 O SER A 81 4.228 8.031 19.830 1.00 11.61 O ATOM 635 CB SER A 81 6.480 6.773 21.709 1.00 10.80 C ATOM 636 OG SER A 81 5.723 5.982 22.614 1.00 11.27 O ATOM 637 N ALA A 82 3.455 8.084 21.946 1.00 10.85 N ATOM 638 CA ALA A 82 2.041 8.086 21.542 1.00 10.75 C ATOM 639 C ALA A 82 1.685 9.315 20.728 1.00 11.13 C ATOM 640 O ALA A 82 0.718 9.309 19.951 1.00 11.59 O ATOM 641 CB ALA A 82 1.134 8.001 22.750 1.00 11.08 C ATOM 642 N LEU A 83 2.450 10.379 20.932 1.00 10.22 N ATOM 643 CA LEU A 83 2.223 11.639 20.242 1.00 10.74 C ATOM 644 C LEU A 83 2.746 11.619 18.806 1.00 10.66 C ATOM 645 O LEU A 83 2.594 12.605 18.080 1.00 10.95 O ATOM 646 CB LEU A 83 2.851 12.782 21.042 1.00 10.46 C ATOM 647 CG LEU A 83 2.266 13.000 22.440 1.00 11.12 C ATOM 648 CD1 LEU A 83 3.099 14.008 23.217 1.00 11.21 C ATOM 649 CD2 LEU A 83 0.816 13.497 22.329 1.00 11.54 C ATOM 650 N LEU A 84 3.360 10.504 18.398 1.00 10.94 N ATOM 651 CA LEU A 84 3.958 10.389 17.059 1.00 10.65 C ATOM 652 C LEU A 84 3.126 9.514 16.125 1.00 10.87 C ATOM 653 O LEU A 84 3.450 9.364 14.947 1.00 11.23 O ATOM 654 CB LEU A 84 5.395 9.837 17.143 1.00 10.70 C ATOM 655 CG LEU A 84 6.375 10.647 18.002 1.00 10.61 C ATOM 656 CD1 LEU A 84 7.724 9.998 17.904 1.00 12.88 C ATOM 657 CD2 LEU A 84 6.471 12.111 17.600 1.00 10.49 C ATOM 658 N SER A 85 2.049 8.955 16.665 1.00 11.49 N ATOM 659 CA SER A 85 1.191 8.031 15.935 1.00 12.08 C ATOM 660 C SER A 85 0.495 8.667 14.726 1.00 12.62 C ATOM 661 O SER A 85 0.218 9.868 14.718 1.00 12.49 O ATOM 662 CB SER A 85 0.137 7.474 16.889 1.00 12.34 C ATOM 663 OG SER A 85 -0.733 6.607 16.194 1.00 14.51 O ATOM 664 N SER A 86 0.206 7.858 13.706 1.00 13.05 N ATOM 665 CA SER A 86 -0.660 8.322 12.614 1.00 14.00 C ATOM 666 C SER A 86 -2.077 8.683 13.119 1.00 14.14 C ATOM 667 O SER A 86 -2.765 9.519 12.523 1.00 15.27 O ATOM 668 CB SER A 86 -0.732 7.269 11.507 1.00 14.06 C ATOM 669 OG SER A 86 -1.158 6.021 12.022 1.00 17.13 O ATOM 670 N ASP A 87 -2.487 8.052 14.215 1.00 13.76 N ATOM 671 CA ASP A 87 -3.750 8.330 14.896 1.00 14.43 C ATOM 672 C ASP A 87 -3.537 9.527 15.826 1.00 13.67 C ATOM 673 O ASP A 87 -2.727 9.448 16.751 1.00 14.25 O ATOM 674 CB ASP A 87 -4.166 7.086 15.707 1.00 15.62 C ATOM 675 CG ASP A 87 -5.542 7.225 16.370 1.00 17.73 C ATOM 676 OD1 ASP A 87 -5.931 8.329 16.799 1.00 18.41 O ATOM 677 OD2 ASP A 87 -6.247 6.191 16.477 1.00 23.10 O ATOM 678 N ILE A 88 -4.262 10.621 15.595 1.00 12.86 N ATOM 679 CA ILE A 88 -4.014 11.856 16.365 1.00 12.73 C ATOM 680 C ILE A 88 -4.713 11.938 17.728 1.00 12.51 C ATOM 681 O ILE A 88 -4.589 12.956 18.413 1.00 12.14 O ATOM 682 CB ILE A 88 -4.311 13.146 15.539 1.00 12.29 C ATOM 683 CG1 ILE A 88 -5.818 13.327 15.278 1.00 13.07 C ATOM 684 CG2 ILE A 88 -3.507 13.130 14.230 1.00 13.12 C ATOM 685 CD1 ILE A 88 -6.185 14.721 14.790 1.00 13.52 C ATOM 686 N THR A 89 -5.412 10.877 18.137 1.00 12.64 N ATOM 687 CA THR A 89 -6.185 10.893 19.386 1.00 12.73 C ATOM 688 C THR A 89 -5.360 11.347 20.593 1.00 12.12 C ATOM 689 O THR A 89 -5.775 12.249 21.314 1.00 11.91 O ATOM 690 CB THR A 89 -6.836 9.511 19.696 1.00 12.87 C ATOM 691 OG1 THR A 89 -7.619 9.092 18.577 1.00 14.69 O ATOM 692 CG2 THR A 89 -7.722 9.582 20.951 1.00 14.65 C ATOM 693 N ALA A 90 -4.187 10.744 20.798 1.00 11.48 N ATOM 694 CA ALA A 90 -3.356 11.124 21.949 1.00 10.83 C ATOM 695 C ALA A 90 -2.905 12.586 21.907 1.00 10.28 C ATOM 696 O ALA A 90 -3.005 13.297 22.920 1.00 10.87 O ATOM 697 CB ALA A 90 -2.166 10.188 22.106 1.00 11.63 C ATOM 698 N SER A 91 -2.459 13.052 20.743 1.00 9.79 N ATOM 699 CA SER A 91 -2.122 14.471 20.605 1.00 9.64 C ATOM 700 C SER A 91 -3.293 15.408 20.876 1.00 9.52 C ATOM 701 O SER A 91 -3.128 16.425 21.549 1.00 10.02 O ATOM 702 CB SER A 91 -1.523 14.772 19.236 1.00 9.75 C ATOM 703 OG SER A 91 -0.188 14.296 19.163 1.00 9.37 O ATOM 704 N VAL A 92 -4.465 15.071 20.352 1.00 9.91 N ATOM 705 CA VAL A 92 -5.643 15.910 20.556 1.00 10.80 C ATOM 706 C VAL A 92 -6.047 15.945 22.024 1.00 11.10 C ATOM 707 O VAL A 92 -6.265 17.020 22.592 1.00 11.45 O ATOM 708 CB VAL A 92 -6.840 15.441 19.698 1.00 10.91 C ATOM 709 CG1 VAL A 92 -8.114 16.183 20.100 1.00 11.31 C ATOM 710 CG2 VAL A 92 -6.546 15.663 18.227 1.00 12.20 C ATOM 711 N ASN A 93 -6.127 14.768 22.642 1.00 11.50 N ATOM 712 CA ASN A 93 -6.522 14.683 24.033 1.00 12.27 C ATOM 713 C ASN A 93 -5.573 15.447 24.943 1.00 11.51 C ATOM 714 O ASN A 93 -6.013 16.111 25.877 1.00 12.23 O ATOM 715 CB ASN A 93 -6.647 13.222 24.483 1.00 13.29 C ATOM 716 CG ASN A 93 -7.825 12.515 23.831 1.00 16.18 C ATOM 717 OD1 ASN A 93 -8.645 13.141 23.159 1.00 18.74 O ATOM 718 ND2 ASN A 93 -7.895 11.202 24.007 1.00 19.08 N ATOM 719 N CYS A 94 -4.274 15.342 24.674 1.00 11.11 N ATOM 720 CA CYS A 94 -3.298 16.060 25.487 1.00 10.99 C ATOM 721 C CYS A 94 -3.367 17.570 25.222 1.00 10.77 C ATOM 722 O CYS A 94 -3.298 18.379 26.156 1.00 10.61 O ATOM 723 CB CYS A 94 -1.898 15.508 25.201 1.00 10.97 C ATOM 724 SG CYS A 94 -0.633 16.101 26.320 1.00 11.21 S ATOM 725 N ALA A 95 -3.506 17.946 23.948 1.00 10.72 N ATOM 726 CA ALA A 95 -3.713 19.351 23.580 1.00 10.00 C ATOM 727 C ALA A 95 -4.918 19.983 24.293 1.00 10.01 C ATOM 728 O ALA A 95 -4.864 21.134 24.694 1.00 9.95 O ATOM 729 CB ALA A 95 -3.844 19.498 22.070 1.00 10.16 C ATOM 730 N LYS A 96 -5.996 19.225 24.456 1.00 9.96 N ATOM 731 CA LYS A 96 -7.149 19.735 25.211 1.00 10.78 C ATOM 732 C LYS A 96 -6.783 20.084 26.664 1.00 11.17 C ATOM 733 O LYS A 96 -7.217 21.108 27.206 1.00 12.04 O ATOM 734 CB LYS A 96 -8.301 18.723 25.163 1.00 10.77 C ATOM 735 CG LYS A 96 -8.925 18.579 23.784 1.00 11.14 C ATOM 736 CD LYS A 96 -10.034 17.532 23.792 1.00 11.84 C ATOM 737 CE LYS A 96 -10.676 17.424 22.423 1.00 13.14 C ATOM 738 NZ LYS A 96 -11.602 16.266 22.327 1.00 16.39 N ATOM 739 N LYS A 97 -5.972 19.236 27.297 1.00 11.34 N ATOM 740 CA LYS A 97 -5.490 19.531 28.646 1.00 12.02 C ATOM 741 C LYS A 97 -4.601 20.776 28.665 1.00 11.73 C ATOM 742 O LYS A 97 -4.740 21.637 29.530 1.00 12.10 O ATOM 743 CB LYS A 97 -4.720 18.336 29.217 1.00 13.07 C ATOM 744 CG LYS A 97 -5.568 17.167 29.642 1.00 16.94 C ATOM 745 CD LYS A 97 -4.717 16.163 30.419 1.00 22.11 C ATOM 746 CE LYS A 97 -5.449 14.837 30.607 1.00 24.91 C ATOM 747 NZ LYS A 97 -5.531 14.063 29.331 1.00 28.28 N ATOM 748 N ILE A 98 -3.711 20.878 27.679 1.00 11.07 N ATOM 749 CA ILE A 98 -2.768 21.987 27.614 1.00 11.30 C ATOM 750 C ILE A 98 -3.515 23.307 27.464 1.00 11.07 C ATOM 751 O ILE A 98 -3.258 24.246 28.196 1.00 11.55 O ATOM 752 CB ILE A 98 -1.743 21.813 26.476 1.00 11.44 C ATOM 753 CG1 ILE A 98 -0.867 20.597 26.738 1.00 11.97 C ATOM 754 CG2 ILE A 98 -0.879 23.070 26.333 1.00 11.45 C ATOM 755 CD1 ILE A 98 -0.023 20.180 25.560 1.00 12.77 C ATOM 756 N VAL A 99 -4.443 23.356 26.511 1.00 11.19 N ATOM 757 CA VAL A 99 -5.160 24.591 26.211 1.00 11.96 C ATOM 758 C VAL A 99 -6.113 25.012 27.337 1.00 13.48 C ATOM 759 O VAL A 99 -6.539 26.167 27.389 1.00 13.30 O ATOM 760 CB VAL A 99 -5.858 24.483 24.841 1.00 11.52 C ATOM 761 CG1 VAL A 99 -7.113 23.618 24.925 1.00 11.67 C ATOM 762 CG2 VAL A 99 -6.181 25.868 24.279 1.00 11.31 C ATOM 763 N SER A 100 -6.410 24.082 28.244 1.00 14.49 N ATOM 764 CA SER A 100 -7.239 24.366 29.418 1.00 16.04 C ATOM 765 C SER A 100 -6.436 24.833 30.631 1.00 17.12 C ATOM 766 O SER A 100 -7.015 25.128 31.681 1.00 17.71 O ATOM 767 CB SER A 100 -8.049 23.122 29.792 1.00 15.73 C ATOM 768 OG SER A 100 -8.828 22.664 28.702 1.00 16.59 O ATOM 769 N ASP A 101 -5.115 24.896 30.480 1.00 18.17 N ATOM 770 CA ASP A 101 -4.168 25.051 31.599 1.00 19.20 C ATOM 771 C ASP A 101 -4.134 26.467 32.161 1.00 19.13 C ATOM 772 O ASP A 101 -3.631 26.685 33.263 1.00 19.58 O ATOM 773 CB ASP A 101 -2.757 24.633 31.148 1.00 19.98 C ATOM 774 CG ASP A 101 -1.794 24.413 32.306 1.00 23.18 C ATOM 775 OD1 ASP A 101 -2.077 23.567 33.183 1.00 26.81 O ATOM 776 OD2 ASP A 101 -0.737 25.078 32.321 1.00 26.56 O ATOM 777 N GLY A 102 -4.673 27.424 31.411 1.00 18.62 N ATOM 778 CA GLY A 102 -4.699 28.816 31.875 1.00 18.15 C ATOM 779 C GLY A 102 -4.331 29.878 30.848 1.00 17.60 C ATOM 780 O GLY A 102 -4.930 30.954 30.831 1.00 18.14 O ATOM 781 N ASN A 103 -3.353 29.587 29.987 1.00 16.83 N ATOM 782 CA ASN A 103 -2.885 30.578 29.010 1.00 15.25 C ATOM 783 C ASN A 103 -3.388 30.307 27.597 1.00 13.53 C ATOM 784 O ASN A 103 -2.943 30.928 26.632 1.00 12.73 O ATOM 785 CB ASN A 103 -1.365 30.723 29.038 1.00 16.33 C ATOM 786 CG ASN A 103 -0.848 31.166 30.398 1.00 18.31 C ATOM 787 OD1 ASN A 103 0.174 30.678 30.873 1.00 24.95 O ATOM 788 ND2 ASN A 103 -1.569 32.068 31.041 1.00 20.80 N ATOM 789 N GLY A 104 -4.353 29.404 27.497 1.00 12.22 N ATOM 790 CA GLY A 104 -4.936 29.077 26.220 1.00 10.92 C ATOM 791 C GLY A 104 -3.883 28.603 25.243 1.00 10.74 C ATOM 792 O GLY A 104 -2.948 27.888 25.613 1.00 10.34 O ATOM 793 N MET A 105 -4.021 29.033 23.999 1.00 9.90 N ATOM 794 CA MET A 105 -3.118 28.555 22.961 1.00 9.06 C ATOM 795 C MET A 105 -1.770 29.254 22.994 1.00 9.48 C ATOM 796 O MET A 105 -0.870 28.891 22.245 1.00 9.04 O ATOM 797 CB MET A 105 -3.758 28.631 21.571 1.00 9.10 C ATOM 798 CG MET A 105 -4.809 27.562 21.334 1.00 8.65 C ATOM 799 SD MET A 105 -5.226 27.359 19.569 1.00 9.26 S ATOM 800 CE MET A 105 -3.806 26.417 18.968 1.00 8.86 C ATOM 801 N ASN A 106 -1.606 30.237 23.876 1.00 9.58 N ATOM 802 CA ASN A 106 -0.288 30.843 24.056 1.00 9.68 C ATOM 803 C ASN A 106 0.766 29.835 24.527 1.00 10.24 C ATOM 804 O ASN A 106 1.962 30.116 24.418 1.00 10.92 O ATOM 805 CB ASN A 106 -0.352 32.037 25.009 1.00 9.76 C ATOM 806 CG ASN A 106 -1.209 33.163 24.469 1.00 10.32 C ATOM 807 OD1 ASN A 106 -0.836 33.865 23.513 1.00 10.54 O ATOM 808 ND2 ASN A 106 -2.367 33.353 25.090 1.00 12.13 N ATOM 809 N ALA A 107 0.329 28.675 25.034 1.00 10.66 N ATOM 810 CA ALA A 107 1.258 27.597 25.392 1.00 11.06 C ATOM 811 C ALA A 107 2.107 27.176 24.195 1.00 10.93 C ATOM 812 O ALA A 107 3.243 26.722 24.358 1.00 12.49 O ATOM 813 CB ALA A 107 0.500 26.408 25.944 1.00 11.59 C ATOM 814 N TRP A 108 1.545 27.299 22.994 1.00 10.69 N ATOM 815 CA TRP A 108 2.276 27.041 21.760 1.00 10.65 C ATOM 816 C TRP A 108 2.899 28.342 21.287 1.00 11.89 C ATOM 817 O TRP A 108 2.233 29.198 20.717 1.00 11.21 O ATOM 818 CB TRP A 108 1.343 26.440 20.700 1.00 9.89 C ATOM 819 CG TRP A 108 0.933 25.033 20.997 1.00 8.94 C ATOM 820 CD1 TRP A 108 1.633 23.890 20.683 1.00 9.46 C ATOM 821 CD2 TRP A 108 -0.241 24.601 21.696 1.00 8.01 C ATOM 822 NE1 TRP A 108 0.955 22.784 21.126 1.00 9.08 N ATOM 823 CE2 TRP A 108 -0.196 23.184 21.755 1.00 8.83 C ATOM 824 CE3 TRP A 108 -1.335 25.271 22.282 1.00 7.85 C ATOM 825 CZ2 TRP A 108 -1.192 22.424 22.367 1.00 8.50 C ATOM 826 CZ3 TRP A 108 -2.336 24.511 22.891 1.00 8.93 C ATOM 827 CH2 TRP A 108 -2.257 23.098 22.925 1.00 8.89 C ATOM 828 N VAL A 109 4.188 28.507 21.545 1.00 13.25 N ATOM 829 CA VAL A 109 4.857 29.748 21.177 1.00 14.45 C ATOM 830 C VAL A 109 4.715 30.065 19.672 1.00 13.78 C ATOM 831 O VAL A 109 4.484 31.230 19.324 1.00 13.76 O ATOM 832 CB VAL A 109 6.319 29.794 21.701 1.00 15.08 C ATOM 833 CG1 VAL A 109 7.064 31.002 21.151 1.00 17.20 C ATOM 834 CG2 VAL A 109 6.319 29.835 23.242 1.00 16.62 C ATOM 835 N ALA A 110 4.784 29.043 18.815 1.00 13.58 N ATOM 836 CA ALA A 110 4.586 29.226 17.361 1.00 12.82 C ATOM 837 C ALA A 110 3.175 29.725 17.043 1.00 12.35 C ATOM 838 O ALA A 110 2.994 30.509 16.109 1.00 12.80 O ATOM 839 CB ALA A 110 4.910 27.969 16.579 1.00 13.55 C ATOM 840 N TRP A 111 2.172 29.263 17.792 1.00 11.13 N ATOM 841 CA TRP A 111 0.831 29.842 17.631 1.00 10.12 C ATOM 842 C TRP A 111 0.815 31.328 17.991 1.00 10.26 C ATOM 843 O TRP A 111 0.301 32.147 17.231 1.00 9.95 O ATOM 844 CB TRP A 111 -0.232 29.090 18.444 1.00 9.94 C ATOM 845 CG TRP A 111 -1.595 29.734 18.327 1.00 8.54 C ATOM 846 CD1 TRP A 111 -2.520 29.507 17.351 1.00 10.12 C ATOM 847 CD2 TRP A 111 -2.175 30.720 19.204 1.00 8.73 C ATOM 848 NE1 TRP A 111 -3.627 30.291 17.556 1.00 10.21 N ATOM 849 CE2 TRP A 111 -3.447 31.039 18.685 1.00 8.34 C ATOM 850 CE3 TRP A 111 -1.738 31.370 20.368 1.00 8.82 C ATOM 851 CZ2 TRP A 111 -4.297 31.969 19.294 1.00 9.14 C ATOM 852 CZ3 TRP A 111 -2.580 32.285 20.973 1.00 9.86 C ATOM 853 CH2 TRP A 111 -3.849 32.584 20.434 1.00 9.74 C ATOM 854 N ARG A 112 1.375 31.683 19.148 1.00 11.60 N ATOM 855 CA ARG A 112 1.414 33.080 19.552 1.00 12.63 C ATOM 856 C ARG A 112 2.131 33.922 18.499 1.00 11.70 C ATOM 857 O ARG A 112 1.657 34.984 18.140 1.00 12.29 O ATOM 858 CB ARG A 112 2.070 33.249 20.929 1.00 12.82 C ATOM 859 CG ARG A 112 2.109 34.679 21.420 1.00 15.21 C ATOM 860 CD ARG A 112 2.587 34.770 22.868 1.00 16.13 C ATOM 861 NE ARG A 112 3.852 34.062 23.075 1.00 22.04 N ATOM 862 CZ ARG A 112 5.058 34.516 22.729 1.00 24.36 C ATOM 863 NH1 ARG A 112 5.203 35.696 22.134 1.00 24.98 N ATOM 864 NH2 ARG A 112 6.130 33.773 22.971 1.00 25.68 N ATOM 865 N ASN A 113 3.253 33.420 17.997 1.00 11.64 N ATOM 866 CA ASN A 113 4.089 34.228 17.107 1.00 11.89 C ATOM 867 C ASN A 113 3.643 34.252 15.651 1.00 11.77 C ATOM 868 O ASN A 113 3.962 35.201 14.931 1.00 11.85 O ATOM 869 CB ASN A 113 5.561 33.820 17.223 1.00 11.65 C ATOM 870 CG ASN A 113 6.170 34.210 18.557 1.00 12.28 C ATOM 871 OD1 ASN A 113 5.780 35.207 19.172 1.00 14.10 O ATOM 872 ND2 ASN A 113 7.159 33.431 18.993 1.00 12.16 N ATOM 873 N ARG A 114 2.903 33.233 15.206 1.00 11.21 N ATOM 874 CA ARG A 114 2.626 33.103 13.775 1.00 11.59 C ATOM 875 C ARG A 114 1.159 32.973 13.414 1.00 11.95 C ATOM 876 O ARG A 114 0.801 33.178 12.255 1.00 12.88 O ATOM 877 CB ARG A 114 3.432 31.949 13.192 1.00 11.21 C ATOM 878 CG ARG A 114 4.927 32.091 13.486 1.00 11.34 C ATOM 879 CD ARG A 114 5.706 30.914 13.007 1.00 11.57 C ATOM 880 NE ARG A 114 5.863 30.933 11.549 1.00 9.79 N ATOM 881 CZ ARG A 114 6.655 30.096 10.896 1.00 10.89 C ATOM 882 NH1 ARG A 114 7.357 29.196 11.573 1.00 10.29 N ATOM 883 NH2 ARG A 114 6.765 30.167 9.573 1.00 11.90 N ATOM 884 N CYS A 115 0.315 32.664 14.398 1.00 11.12 N ATOM 885 CA CYS A 115 -1.105 32.408 14.136 1.00 10.87 C ATOM 886 C CYS A 115 -2.025 33.403 14.816 1.00 10.93 C ATOM 887 O CYS A 115 -3.004 33.871 14.225 1.00 11.36 O ATOM 888 CB CYS A 115 -1.492 31.003 14.602 1.00 10.02 C ATOM 889 SG CYS A 115 -0.603 29.692 13.743 1.00 9.95 S ATOM 890 N LYS A 116 -1.730 33.694 16.077 1.00 10.92 N ATOM 891 CA LYS A 116 -2.542 34.581 16.878 1.00 11.70 C ATOM 892 C LYS A 116 -2.806 35.914 16.168 1.00 11.61 C ATOM 893 O LYS A 116 -1.881 36.598 15.714 1.00 11.95 O ATOM 894 CB LYS A 116 -1.844 34.798 18.210 1.00 11.24 C ATOM 895 CG LYS A 116 -2.641 35.582 19.218 1.00 11.59 C ATOM 896 CD LYS A 116 -1.820 35.808 20.466 1.00 11.41 C ATOM 897 CE LYS A 116 -2.649 36.428 21.580 1.00 11.72 C ATOM 898 NZ LYS A 116 -1.808 36.604 22.817 1.00 11.76 N ATOM 899 N GLY A 117 -4.086 36.247 16.057 1.00 12.41 N ATOM 900 CA GLY A 117 -4.503 37.506 15.452 1.00 13.01 C ATOM 901 C GLY A 117 -4.574 37.532 13.940 1.00 13.67 C ATOM 902 O GLY A 117 -5.042 38.512 13.365 1.00 15.07 O ATOM 903 N THR A 118 -4.101 36.473 13.292 1.00 12.94 N ATOM 904 CA THR A 118 -4.108 36.412 11.836 1.00 12.33 C ATOM 905 C THR A 118 -5.419 35.833 11.319 1.00 12.74 C ATOM 906 O THR A 118 -6.264 35.370 12.096 1.00 12.04 O ATOM 907 CB THR A 118 -2.933 35.563 11.306 1.00 12.18 C ATOM 908 OG1 THR A 118 -3.188 34.185 11.592 1.00 11.24 O ATOM 909 CG2 THR A 118 -1.619 35.990 11.946 1.00 11.38 C ATOM 910 N ASP A 119 -5.584 35.847 9.998 1.00 13.48 N ATOM 911 CA ASP A 119 -6.746 35.253 9.365 1.00 14.55 C ATOM 912 C ASP A 119 -6.624 33.725 9.353 1.00 14.38 C ATOM 913 O ASP A 119 -6.421 33.101 8.309 1.00 14.56 O ATOM 914 CB ASP A 119 -6.903 35.823 7.940 1.00 15.20 C ATOM 915 CG ASP A 119 -8.144 35.309 7.224 1.00 18.60 C ATOM 916 OD1 ASP A 119 -9.096 34.839 7.885 1.00 20.81 O ATOM 917 OD2 ASP A 119 -8.160 35.395 5.974 1.00 22.56 O ATOM 918 N VAL A 120 -6.773 33.129 10.532 1.00 13.61 N ATOM 919 CA VAL A 120 -6.625 31.674 10.684 1.00 13.18 C ATOM 920 C VAL A 120 -7.679 30.845 9.926 1.00 13.34 C ATOM 921 O VAL A 120 -7.465 29.665 9.648 1.00 12.61 O ATOM 922 CB VAL A 120 -6.597 31.254 12.177 1.00 12.94 C ATOM 923 CG1 VAL A 120 -5.352 31.825 12.884 1.00 13.22 C ATOM 924 CG2 VAL A 120 -7.905 31.675 12.872 1.00 12.84 C ATOM 925 N GLN A 121 -8.813 31.453 9.578 1.00 14.17 N ATOM 926 CA GLN A 121 -9.841 30.734 8.835 1.00 14.90 C ATOM 927 C GLN A 121 -9.334 30.306 7.450 1.00 13.79 C ATOM 928 O GLN A 121 -9.831 29.320 6.876 1.00 14.08 O ATOM 929 CB GLN A 121 -11.106 31.586 8.729 1.00 16.04 C ATOM 930 CG GLN A 121 -12.329 30.856 8.201 1.00 20.98 C ATOM 931 CD GLN A 121 -13.629 31.513 8.635 1.00 26.07 C ATOM 932 OE1 GLN A 121 -14.665 30.850 8.752 1.00 30.08 O ATOM 933 NE2 GLN A 121 -13.580 32.821 8.885 1.00 28.41 N ATOM 934 N ALA A 122 -8.332 31.021 6.934 1.00 13.52 N ATOM 935 CA ALA A 122 -7.714 30.653 5.658 1.00 13.36 C ATOM 936 C ALA A 122 -7.199 29.210 5.686 1.00 13.06 C ATOM 937 O ALA A 122 -7.126 28.545 4.656 1.00 13.23 O ATOM 938 CB ALA A 122 -6.587 31.615 5.306 1.00 13.58 C ATOM 939 N TRP A 123 -6.861 28.715 6.875 1.00 13.06 N ATOM 940 CA TRP A 123 -6.315 27.356 7.009 1.00 12.80 C ATOM 941 C TRP A 123 -7.335 26.245 6.771 1.00 13.47 C ATOM 942 O TRP A 123 -6.967 25.107 6.501 1.00 13.08 O ATOM 943 CB TRP A 123 -5.627 27.174 8.371 1.00 12.46 C ATOM 944 CG TRP A 123 -4.369 27.951 8.408 1.00 12.12 C ATOM 945 CD1 TRP A 123 -4.172 29.159 8.997 1.00 13.17 C ATOM 946 CD2 TRP A 123 -3.136 27.603 7.767 1.00 13.17 C ATOM 947 NE1 TRP A 123 -2.888 29.584 8.782 1.00 12.99 N ATOM 948 CE2 TRP A 123 -2.228 28.657 8.020 1.00 12.79 C ATOM 949 CE3 TRP A 123 -2.716 26.510 6.995 1.00 12.93 C ATOM 950 CZ2 TRP A 123 -0.909 28.642 7.546 1.00 13.57 C ATOM 951 CZ3 TRP A 123 -1.403 26.498 6.504 1.00 12.85 C ATOM 952 CH2 TRP A 123 -0.521 27.571 6.784 1.00 12.79 C ATOM 953 N ILE A 124 -8.618 26.580 6.875 1.00 14.55 N ATOM 954 CA ILE A 124 -9.662 25.581 6.640 1.00 16.21 C ATOM 955 C ILE A 124 -10.493 25.907 5.398 1.00 16.61 C ATOM 956 O ILE A 124 -11.454 25.196 5.080 1.00 17.14 O ATOM 957 CB ILE A 124 -10.560 25.350 7.895 1.00 16.20 C ATOM 958 CG1 ILE A 124 -11.299 26.630 8.302 1.00 17.03 C ATOM 959 CG2 ILE A 124 -9.714 24.787 9.039 1.00 16.99 C ATOM 960 CD1 ILE A 124 -12.461 26.393 9.276 1.00 17.83 C ATOM 961 N ARG A 125 -10.096 26.965 4.700 1.00 17.73 N ATOM 962 CA ARG A 125 -10.838 27.469 3.539 1.00 19.34 C ATOM 963 C ARG A 125 -10.879 26.410 2.460 1.00 19.77 C ATOM 964 O ARG A 125 -9.857 25.816 2.124 1.00 19.90 O ATOM 965 CB ARG A 125 -10.181 28.740 3.008 1.00 19.61 C ATOM 966 CG ARG A 125 -11.024 29.541 2.014 1.00 21.75 C ATOM 967 CD ARG A 125 -10.487 30.961 1.895 1.00 25.70 C ATOM 968 NE ARG A 125 -10.609 31.699 3.158 1.00 28.19 N ATOM 969 CZ ARG A 125 -9.832 32.721 3.509 1.00 29.98 C ATOM 970 NH1 ARG A 125 -8.861 33.134 2.701 1.00 32.01 N ATOM 971 NH2 ARG A 125 -10.014 33.326 4.678 1.00 31.25 N ATOM 972 N GLY A 126 -12.078 26.151 1.939 1.00 20.38 N ATOM 973 CA GLY A 126 -12.247 25.178 0.870 1.00 21.14 C ATOM 974 C GLY A 126 -12.382 23.736 1.323 1.00 21.54 C ATOM 975 O GLY A 126 -12.726 22.869 0.523 1.00 21.85 O ATOM 976 N CYS A 127 -12.112 23.474 2.600 1.00 21.37 N ATOM 977 CA CYS A 127 -12.167 22.112 3.132 1.00 21.83 C ATOM 978 C CYS A 127 -13.592 21.636 3.379 1.00 23.05 C ATOM 979 O CYS A 127 -14.407 22.362 3.948 1.00 23.05 O ATOM 980 CB CYS A 127 -11.385 22.009 4.446 1.00 21.24 C ATOM 981 SG CYS A 127 -9.649 22.534 4.394 1.00 17.61 S ATOM 982 N ARG A 128 -13.869 20.399 2.972 1.00 24.53 N ATOM 983 CA ARG A 128 -15.147 19.767 3.262 1.00 26.59 C ATOM 984 C ARG A 128 -15.109 19.291 4.710 1.00 26.85 C ATOM 985 O ARG A 128 -14.392 18.349 5.034 1.00 27.50 O ATOM 986 CB ARG A 128 -15.406 18.605 2.298 1.00 26.54 C ATOM 987 CG ARG A 128 -16.820 18.042 2.365 1.00 27.91 C ATOM 988 CD ARG A 128 -17.010 16.877 1.409 1.00 28.63 C ATOM 989 NE ARG A 128 -17.056 17.293 0.010 1.00 33.85 N ATOM 990 CZ ARG A 128 -16.129 17.000 -0.900 1.00 35.25 C ATOM 991 NH1 ARG A 128 -15.068 16.270 -0.574 1.00 36.53 N ATOM 992 NH2 ARG A 128 -16.272 17.431 -2.147 1.00 37.05 N ATOM 993 N LEU A 129 -15.856 19.966 5.580 1.00 27.78 N ATOM 994 CA LEU A 129 -15.852 19.657 7.014 1.00 28.54 C ATOM 995 C LEU A 129 -17.264 19.379 7.510 1.00 29.05 C ATOM 996 O LEU A 129 -18.228 19.974 7.016 1.00 30.03 O ATOM 997 CB LEU A 129 -15.242 20.810 7.821 1.00 28.59 C ATOM 998 CG LEU A 129 -13.875 21.371 7.401 1.00 28.76 C ATOM 999 CD1 LEU A 129 -13.629 22.717 8.070 1.00 29.53 C ATOM 1000 CD2 LEU A 129 -12.728 20.407 7.695 1.00 28.97 C TER 1001 LEU A 129 HETATM 1002 O HOH A2001 2.889 7.444 10.779 1.00 16.91 O HETATM 1003 O HOH A2002 2.443 10.238 5.221 1.00 19.67 O HETATM 1004 O HOH A2003 -1.743 12.007 4.631 1.00 26.85 O HETATM 1005 O HOH A2004 0.725 18.467 4.011 1.00 14.13 O HETATM 1006 O HOH A2005 -2.435 24.008 1.431 1.00 29.75 O HETATM 1007 O HOH A2006 2.239 28.340 4.272 1.00 33.61 O HETATM 1008 O HOH A2007 -5.645 20.071 1.736 1.00 19.36 O HETATM 1009 O HOH A2008 -9.187 13.202 7.933 1.00 24.85 O HETATM 1010 O HOH A2009 -7.378 10.934 8.114 1.00 38.89 O HETATM 1011 O HOH A2010 -5.898 17.384 2.595 1.00 19.20 O HETATM 1012 O HOH A2011 -14.704 19.633 16.575 1.00 26.72 O HETATM 1013 O HOH A2012 0.214 26.915 3.126 1.00 28.47 O HETATM 1014 O HOH A2013 9.765 24.086 15.877 1.00 29.11 O HETATM 1015 O HOH A2014 9.964 30.618 23.504 1.00 33.04 O HETATM 1016 O HOH A2015 -2.961 29.237 4.017 1.00 30.48 O HETATM 1017 O HOH A2016 18.998 18.801 18.563 0.50 29.28 O HETATM 1018 O HOH A2017 12.142 24.479 26.344 1.00 42.75 O HETATM 1019 O HOH A2018 -14.080 30.409 17.539 1.00 24.40 O HETATM 1020 O HOH A2019 -16.825 26.179 22.450 1.00 32.80 O HETATM 1021 O HOH A2020 -12.593 17.992 27.478 1.00 30.75 O HETATM 1022 O HOH A2021 -14.615 23.749 25.084 1.00 21.31 O HETATM 1023 O HOH A2022 -10.619 31.278 23.720 1.00 13.00 O HETATM 1024 O HOH A2023 -14.033 24.472 32.292 1.00 33.28 O HETATM 1025 O HOH A2024 -8.319 31.564 25.968 1.00 5.09 O HETATM 1026 O HOH A2025 -11.754 32.671 14.882 1.00 19.01 O HETATM 1027 O HOH A2026 -11.132 29.065 11.726 1.00 8.43 O HETATM 1028 O HOH A2027 -11.861 31.370 12.569 1.00 36.34 O HETATM 1029 O HOH A2028 -6.028 33.753 16.623 1.00 13.71 O HETATM 1030 O HOH A2029 -9.129 33.279 15.757 1.00 14.83 O HETATM 1031 O HOH A2030 2.458 4.523 16.349 1.00 21.98 O HETATM 1032 O HOH A2031 1.178 4.190 23.337 1.00 37.64 O HETATM 1033 O HOH A2032 -0.332 23.844 3.905 1.00 12.26 O HETATM 1034 O HOH A2033 5.846 24.621 8.666 1.00 18.35 O HETATM 1035 O HOH A2034 -4.761 9.608 25.166 1.00 27.12 O HETATM 1036 O HOH A2035 7.603 24.911 11.077 1.00 17.94 O HETATM 1037 O HOH A2036 7.638 26.161 15.366 1.00 16.61 O HETATM 1038 O HOH A2037 7.554 24.161 19.541 1.00 20.92 O HETATM 1039 O HOH A2038 8.835 20.658 13.485 1.00 22.54 O HETATM 1040 O HOH A2039 7.888 26.552 18.066 1.00 22.66 O HETATM 1041 O HOH A2040 5.893 26.789 19.814 1.00 18.98 O HETATM 1042 O HOH A2041 -15.677 19.729 23.881 1.00 31.28 O HETATM 1043 O HOH A2042 8.139 18.126 10.449 1.00 19.48 O HETATM 1044 O HOH A2043 5.769 17.641 6.873 1.00 20.64 O HETATM 1045 O HOH A2044 6.153 22.235 2.922 1.00 25.56 O HETATM 1046 O HOH A2045 3.007 19.643 5.041 1.00 16.12 O HETATM 1047 O HOH A2046 9.121 21.142 7.602 1.00 30.57 O HETATM 1048 O HOH A2047 8.109 17.206 7.861 1.00 19.37 O HETATM 1049 O HOH A2048 5.622 10.959 9.072 1.00 9.76 O HETATM 1050 O HOH A2049 8.647 27.279 23.267 1.00 45.58 O HETATM 1051 O HOH A2050 -0.802 39.099 19.140 1.00 19.58 O HETATM 1052 O HOH A2051 -0.068 32.045 8.113 1.00 18.56 O HETATM 1053 O HOH A2052 -3.895 41.361 16.536 1.00 25.17 O HETATM 1054 O HOH A2053 -8.435 37.815 15.116 1.00 21.23 O HETATM 1055 O HOH A2054 -2.878 31.559 5.127 1.00 24.69 O HETATM 1056 O HOH A2055 -2.511 39.245 9.887 1.00 27.09 O HETATM 1057 O HOH A2056 11.357 13.251 14.437 1.00 8.63 O HETATM 1058 O HOH A2057 14.408 14.403 18.454 0.50 16.77 O HETATM 1059 O HOH A2058 10.607 22.671 13.857 1.00 44.63 O HETATM 1060 O HOH A2059 16.120 18.472 17.633 1.00 20.92 O HETATM 1061 O HOH A2060 20.762 14.240 26.180 1.00 34.75 O HETATM 1062 O HOH A2061 11.499 22.704 20.124 1.00 28.45 O HETATM 1063 O HOH A2062 19.625 19.649 24.580 1.00 37.10 O HETATM 1064 O HOH A2063 14.804 24.595 26.566 1.00 29.00 O HETATM 1065 O HOH A2064 10.976 23.250 28.238 1.00 32.50 O HETATM 1066 O HOH A2065 11.925 24.742 30.746 1.00 31.13 O HETATM 1067 O HOH A2066 16.203 17.842 30.631 1.00 33.65 O HETATM 1068 O HOH A2067 1.574 16.646 19.291 1.00 8.98 O HETATM 1069 O HOH A2068 9.201 22.392 18.328 1.00 14.89 O HETATM 1070 O HOH A2069 3.869 21.538 25.182 1.00 18.09 O HETATM 1071 O HOH A2070 7.946 14.137 31.209 1.00 7.05 O HETATM 1072 O HOH A2071 8.087 20.211 35.097 1.00 29.56 O HETATM 1073 O HOH A2072 3.381 23.690 28.312 1.00 30.47 O HETATM 1074 O HOH A2073 10.473 5.692 30.771 1.00 12.00 O HETATM 1075 O HOH A2074 7.753 12.118 32.509 1.00 14.37 O HETATM 1076 O HOH A2075 10.499 8.702 33.598 1.00 25.69 O HETATM 1077 O HOH A2076 5.452 5.963 29.598 1.00 11.15 O HETATM 1078 O HOH A2077 9.686 12.715 30.214 1.00 9.94 O HETATM 1079 O HOH A2078 14.751 7.397 33.166 1.00 23.67 O HETATM 1080 O HOH A2079 18.544 9.958 24.502 1.00 21.03 O HETATM 1081 O HOH A2080 17.409 15.737 29.426 1.00 28.85 O HETATM 1082 O HOH A2081 11.746 11.649 32.384 1.00 5.17 O HETATM 1083 O HOH A2082 14.356 11.474 34.098 1.00 22.47 O HETATM 1084 O HOH A2083 8.249 19.172 37.196 1.00 36.68 O HETATM 1085 O HOH A2084 12.816 12.817 36.917 0.50 18.87 O HETATM 1086 O HOH A2085 10.676 12.741 35.190 1.00 27.00 O HETATM 1087 O HOH A2086 6.543 17.543 41.252 1.00 27.56 O HETATM 1088 O HOH A2087 6.577 19.507 39.023 1.00 30.49 O HETATM 1089 O HOH A2088 2.880 13.671 36.369 1.00 20.01 O HETATM 1090 O HOH A2089 2.811 7.039 30.510 1.00 19.21 O HETATM 1091 O HOH A2090 5.259 8.786 33.995 1.00 22.28 O HETATM 1092 O HOH A2091 3.265 4.756 21.713 1.00 18.98 O HETATM 1093 O HOH A2092 4.233 6.160 17.857 1.00 20.24 O HETATM 1094 O HOH A2093 7.185 3.878 23.604 1.00 14.41 O HETATM 1095 O HOH A2094 -1.272 11.054 18.717 1.00 13.28 O HETATM 1096 O HOH A2095 -1.099 6.983 20.106 1.00 23.59 O HETATM 1097 O HOH A2096 0.975 13.955 16.569 1.00 13.43 O HETATM 1098 O HOH A2097 -0.623 11.994 16.158 1.00 12.32 O HETATM 1099 O HOH A2098 1.563 5.206 13.690 1.00 21.43 O HETATM 1100 O HOH A2099 -4.587 9.060 10.627 1.00 24.92 O HETATM 1101 O HOH A2100 -3.313 8.330 19.336 1.00 16.99 O HETATM 1102 O HOH A2101 -10.048 7.929 19.074 1.00 29.52 O HETATM 1103 O HOH A2102 -3.186 11.950 25.355 1.00 20.57 O HETATM 1104 O HOH A2103 -8.004 15.541 27.550 1.00 26.28 O HETATM 1105 O HOH A2104 -9.299 12.671 20.440 1.00 25.41 O HETATM 1106 O HOH A2105 -10.264 9.591 23.421 1.00 35.33 O HETATM 1107 O HOH A2106 -11.018 14.125 24.050 1.00 33.26 O HETATM 1108 O HOH A2107 -14.031 17.234 23.906 1.00 32.45 O HETATM 1109 O HOH A2108 -3.982 12.752 27.838 1.00 21.19 O HETATM 1110 O HOH A2109 -5.170 21.602 32.227 1.00 27.00 O HETATM 1111 O HOH A2110 -2.376 26.967 28.272 1.00 16.07 O HETATM 1112 O HOH A2111 -6.397 28.088 29.185 1.00 17.70 O HETATM 1113 O HOH A2112 3.851 31.891 24.506 1.00 32.36 O HETATM 1114 O HOH A2113 5.072 27.573 26.350 1.00 31.82 O HETATM 1115 O HOH A2114 2.808 23.716 25.354 1.00 31.66 O HETATM 1116 O HOH A2115 5.839 26.481 22.517 1.00 20.94 O HETATM 1117 O HOH A2116 1.424 37.687 18.582 1.00 28.82 O HETATM 1118 O HOH A2117 8.115 27.989 8.264 1.00 14.29 O HETATM 1119 O HOH A2118 1.729 33.586 9.812 1.00 15.24 O HETATM 1120 O HOH A2119 4.545 32.909 9.882 1.00 11.36 O HETATM 1121 O HOH A2120 0.952 36.056 15.401 1.00 15.41 O HETATM 1122 O HOH A2121 0.092 38.514 21.878 1.00 18.31 O HETATM 1123 O HOH A2122 -1.296 38.996 14.651 1.00 24.58 O HETATM 1124 O HOH A2123 -0.294 36.701 25.385 1.00 25.86 O HETATM 1125 O HOH A2124 -3.395 39.098 18.141 1.00 16.37 O HETATM 1126 O HOH A2125 -7.291 35.295 14.632 1.00 16.30 O HETATM 1127 O HOH A2126 -2.582 32.439 9.481 1.00 13.79 O HETATM 1128 O HOH A2127 -3.857 37.369 8.304 1.00 18.60 O HETATM 1129 O HOH A2128 -3.873 33.237 7.234 1.00 23.44 O HETATM 1130 O HOH A2129 -17.383 29.318 7.800 1.00 43.28 O HETATM 1131 O HOH A2130 -6.663 29.165 2.095 1.00 32.28 O HETATM 1132 O HOH A2131 -11.599 18.900 1.297 1.00 29.75 O HETATM 1133 O HOH A2132 -15.208 16.447 6.214 1.00 26.66 O HETATM 1134 O HOH A2133 -20.064 17.181 0.460 1.00 49.15 O CONECT 48 981 CONECT 238 889 CONECT 513 630 CONECT 601 724 CONECT 630 513 CONECT 724 601 CONECT 889 238 CONECT 981 48 MASTER 943 0 0 7 3 0 0 6 1133 1 8 10 END