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HEADER HYDROLASE 05-JUN-08 3DD5
TITLE GLOMERELLA CINGULATA E600-CUTINASE COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CUTINASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 FRAGMENT: RESIDUES 31-224;
COMPND 5 SYNONYM: CUTIN HYDROLASE;
COMPND 6 EC: 3.1.1.74;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GLOMERELLA CINGULATA;
SOURCE 3 ORGANISM_COMMON: ANTHRACNOSE FUNGUS;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_STRAIN: ORIGAMI (DE3);
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET32B_CUTA
KEYWDS CATALYTIC TRIAD, HYDROLASE, SECRETED, SERINE ESTERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.P.NYON,D.W.RICE,J.M.BERRISFORD,A.M.HOUNSLOW,A.J.G.MOIR,
AUTHOR 2 H.HUANG,S.NATHAN,N.M.MAHADI,A.B.FARAH DIBA,C.J.CRAVEN
REVDAT 1 18-NOV-08 3DD5 0
JRNL AUTH M.P.NYON,D.W.RICE,J.M.BERRISFORD,A.M.HOUNSLOW,
JRNL AUTH 2 A.J.G.MOIR,H.HUANG,S.NATHAN,N.M.MAHADI,F.D.A.BAKAR,
JRNL AUTH 3 C.J.CRAVEN
JRNL TITL CATALYSIS BY GLOMERELLA CINGULATA CUTINASE
JRNL TITL 2 REQUIRES CONFORMATIONAL CYCLING BETWEEN THE ACTIVE
JRNL TITL 3 AND INACTIVE STATES OF ITS CATALYTIC TRIAD
JRNL REF J.MOL.BIOL. 2008
JRNL REFN ASTM JMOBAK UK ESSN 1089-8638
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 44886
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) : 0.219
REMARK 3 R VALUE (WORKING SET) : 0.215
REMARK 3 FREE R VALUE : 0.279
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2391
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3108
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.67
REMARK 3 BIN R VALUE (WORKING SET) : 0.3100
REMARK 3 BIN FREE R VALUE SET COUNT : 196
REMARK 3 BIN FREE R VALUE : 0.4020
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 11496
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 40.34
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.01000
REMARK 3 B22 (A**2) : 0.01000
REMARK 3 B33 (A**2) : -0.01000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.02000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.603
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.376
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.278
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.040
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.898
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.828
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 11716 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 15936 ; 1.477 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1539 ; 6.931 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 459 ;41.183 ;24.074
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1764 ;19.376 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 64 ;21.690 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1831 ; 0.107 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8884 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 5458 ; 0.231 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 8088 ; 0.313 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 389 ; 0.166 ; 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): 112 ; 0.196 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 9 ; 0.225 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 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: NULL
REMARK 4
REMARK 4 3DD5 COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ.
REMARK 100 THE RCSB ID CODE IS RCSB047889.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-AUG-2006
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : OSMIC VARIMAX
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47279
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 2.900
REMARK 200 R MERGE (I) : 0.12200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.40
REMARK 200 R MERGE FOR SHELL (I) : 0.41600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3DCN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MAGNESIUM ACETATE, 18% PEG
REMARK 280 3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,1/2+Y,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 58.68500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F
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 350
REMARK 350 BIOMOLECULE: 7
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G
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 350
REMARK 350 BIOMOLECULE: 8
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H
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 350
REMARK 350 BIOMOLECULE: 9
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4620 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 -1.000000 0.000000 0.000000 -22.34646
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 -58.68500
REMARK 350 BIOMT3 1 0.000000 0.000000 -1.000000 92.58128
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 51.12354
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -58.68500
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 92.58128
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, F
REMARK 350 BIOMT1 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 10
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 350 APPLY THE FOLLOWING TO CHAINS: G
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 -51.12354
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 -92.58128
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 -58.68500
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H
REMARK 350 BIOMT1 4 -1.000000 0.000000 0.000000 -73.47000
REMARK 350 BIOMT2 4 0.000000 1.000000 0.000000 -58.68500
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 11
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1310 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
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 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 -22.34646
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -58.68500
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 92.58128
REMARK 350
REMARK 350 BIOMOLECULE: 12
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1360 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 51.12354
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 58.68500
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 92.58128
REMARK 350
REMARK 350 BIOMOLECULE: 13
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1360 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 350 APPLY THE FOLLOWING TO CHAINS: E
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -58.68500
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 14
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15270 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G
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 350 APPLY THE FOLLOWING TO CHAINS: H
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 -22.34646
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -58.68500
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 92.58128
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSEQI
REMARK 465 ALA A 24
REMARK 465 MET A 25
REMARK 465 ALA A 26
REMARK 465 ILE A 27
REMARK 465 SER A 28
REMARK 465 ASP A 29
REMARK 465 PRO A 30
REMARK 465 ALA B 24
REMARK 465 MET B 25
REMARK 465 ALA B 26
REMARK 465 ILE B 27
REMARK 465 SER B 28
REMARK 465 ASP B 29
REMARK 465 PRO B 30
REMARK 465 ALA C 24
REMARK 465 MET C 25
REMARK 465 ALA C 26
REMARK 465 ILE C 27
REMARK 465 SER C 28
REMARK 465 ASP C 29
REMARK 465 PRO C 30
REMARK 465 GLN C 31
REMARK 465 ALA D 24
REMARK 465 MET D 25
REMARK 465 ALA D 26
REMARK 465 ILE D 27
REMARK 465 SER D 28
REMARK 465 ASP D 29
REMARK 465 PRO D 30
REMARK 465 ALA E 24
REMARK 465 MET E 25
REMARK 465 ALA E 26
REMARK 465 ILE E 27
REMARK 465 SER E 28
REMARK 465 ASP E 29
REMARK 465 PRO E 30
REMARK 465 GLN E 31
REMARK 465 ALA F 24
REMARK 465 MET F 25
REMARK 465 ALA F 26
REMARK 465 ILE F 27
REMARK 465 SER F 28
REMARK 465 ASP F 29
REMARK 465 PRO F 30
REMARK 465 GLN F 31
REMARK 465 ALA G 24
REMARK 465 MET G 25
REMARK 465 ALA G 26
REMARK 465 ILE G 27
REMARK 465 SER G 28
REMARK 465 ASP G 29
REMARK 465 PRO G 30
REMARK 465 GLN G 31
REMARK 465 ALA H 24
REMARK 465 MET H 25
REMARK 465 ALA H 26
REMARK 465 ILE H 27
REMARK 465 SER H 28
REMARK 465 ASP H 29
REMARK 465 PRO H 30
REMARK 465 GLN H 31
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 THR A 58 OG1
REMARK 470 GLY A 224 C O
REMARK 470 THR G 58 CG2
REMARK 470 THR H 40 CG2
REMARK 470 THR H 58 OG1
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG D 174 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 THR A 58 -23.20 97.38
REMARK 500 SER A 66 -111.36 -112.46
REMARK 500 SER A 136 -118.21 57.77
REMARK 500 VAL A 213 -73.24 -114.15
REMARK 500 SER B 43 1.05 -63.33
REMARK 500 THR B 58 -25.51 85.38
REMARK 500 SER B 66 -92.43 -111.09
REMARK 500 PRO B 92 1.56 -65.52
REMARK 500 CYS B 125 88.66 -153.17
REMARK 500 SER B 136 -118.72 62.80
REMARK 500 TYR B 165 104.10 -56.38
REMARK 500 HIS B 204 -177.47 -170.93
REMARK 500 VAL B 213 -59.37 -124.60
REMARK 500 SER C 43 2.92 -69.72
REMARK 500 ALA C 45 63.83 -109.77
REMARK 500 THR C 58 -23.53 86.82
REMARK 500 SER C 66 -105.03 -125.22
REMARK 500 PRO C 92 -37.53 -39.89
REMARK 500 TYR C 93 94.76 -65.18
REMARK 500 SER C 136 -106.19 63.40
REMARK 500 LEU C 201 128.29 173.32
REMARK 500 SER D 32 20.30 -76.68
REMARK 500 THR D 58 -23.23 73.38
REMARK 500 SER D 66 -105.21 -110.48
REMARK 500 SER D 136 -110.87 68.73
REMARK 500 THR D 197 -166.77 -129.35
REMARK 500 ILE D 200 70.36 85.86
REMARK 500 LEU D 201 115.81 172.36
REMARK 500 ALA E 45 61.39 -154.67
REMARK 500 SER E 66 -101.18 -142.77
REMARK 500 ASN E 82 22.35 -64.90
REMARK 500 ASP E 83 11.73 -157.53
REMARK 500 SER E 136 -120.41 62.33
REMARK 500 SER E 147 -15.08 -44.89
REMARK 500 SER E 150 161.43 -47.46
REMARK 500 PRO E 176 130.21 -34.49
REMARK 500 PRO E 202 131.85 -37.52
REMARK 500 ALA F 45 49.69 -156.97
REMARK 500 SER F 66 -124.76 -117.26
REMARK 500 VAL F 89 93.48 -69.87
REMARK 500 PRO F 92 -6.67 -59.01
REMARK 500 SER F 136 -115.70 64.14
REMARK 500 SER F 147 -34.29 -38.46
REMARK 500 LYS F 167 36.27 -93.39
REMARK 500 SER G 44 24.72 -67.22
REMARK 500 ALA G 45 56.29 -170.75
REMARK 500 THR G 58 -24.52 68.79
REMARK 500 SER G 66 -97.63 -125.32
REMARK 500 THR G 106 -166.29 -171.40
REMARK 500 SER G 136 -113.89 65.39
REMARK 500 LEU G 172 35.28 76.70
REMARK 500 VAL G 213 -69.99 -121.02
REMARK 500 ALA H 45 58.03 -142.12
REMARK 500 THR H 58 -19.11 75.99
REMARK 500 SER H 66 -99.26 -124.13
REMARK 500 PRO H 92 5.90 -60.60
REMARK 500 SER H 136 -109.66 72.10
REMARK 500 GLU H 179 118.38 -27.44
REMARK 500 ASP H 191 91.72 -56.64
REMARK 500 ALA H 203 60.56 99.97
REMARK 500 VAL H 213 -58.96 -122.88
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ALA G 203 HIS G 204 -149.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DEP A 401
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DEP B 402
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DEP C 403
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DEP D 404
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DEP E 405
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DEP F 406
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DEP G 407
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DEP H 408
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3DCN RELATED DB: PDB
REMARK 900 APO CUTINASE
REMARK 900 RELATED ID: 3DEA RELATED DB: PDB
REMARK 900 PETFP-CUTINASE COMPLEX
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE IS BASED ON REFERENCE 2 IN THE DATABASE,
REMARK 999 CUTI_COLGL.
DBREF 3DD5 A 31 224 UNP P11373 CUTI_COLGL 31 224
DBREF 3DD5 B 31 224 UNP P11373 CUTI_COLGL 31 224
DBREF 3DD5 C 31 224 UNP P11373 CUTI_COLGL 31 224
DBREF 3DD5 D 31 224 UNP P11373 CUTI_COLGL 31 224
DBREF 3DD5 E 31 224 UNP P11373 CUTI_COLGL 31 224
DBREF 3DD5 F 31 224 UNP P11373 CUTI_COLGL 31 224
DBREF 3DD5 G 31 224 UNP P11373 CUTI_COLGL 31 224
DBREF 3DD5 H 31 224 UNP P11373 CUTI_COLGL 31 224
SEQADV 3DD5 ALA A 24 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 MET A 25 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 ALA A 26 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 ILE A 27 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 SER A 28 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 ASP A 29 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 PRO A 30 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 ALA B 24 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 MET B 25 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 ALA B 26 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 ILE B 27 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 SER B 28 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 ASP B 29 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 PRO B 30 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 ALA C 24 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 MET C 25 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 ALA C 26 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 ILE C 27 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 SER C 28 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 ASP C 29 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 PRO C 30 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 ALA D 24 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 MET D 25 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 ALA D 26 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 ILE D 27 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 SER D 28 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 ASP D 29 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 PRO D 30 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 ALA E 24 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 MET E 25 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 ALA E 26 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 ILE E 27 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 SER E 28 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 ASP E 29 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 PRO E 30 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 ALA F 24 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 MET F 25 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 ALA F 26 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 ILE F 27 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 SER F 28 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 ASP F 29 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 PRO F 30 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 ALA G 24 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 MET G 25 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 ALA G 26 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 ILE G 27 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 SER G 28 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 ASP G 29 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 PRO G 30 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 ALA H 24 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 MET H 25 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 ALA H 26 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 ILE H 27 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 SER H 28 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 ASP H 29 UNP P11373 EXPRESSION TAG
SEQADV 3DD5 PRO H 30 UNP P11373 EXPRESSION TAG
SEQRES 1 A 201 ALA MET ALA ILE SER ASP PRO GLN SER SER THR ARG ASN
SEQRES 2 A 201 GLU LEU GLU THR GLY SER SER SER ALA CYS PRO LYS VAL
SEQRES 3 A 201 ILE TYR ILE PHE ALA ARG ALA SER THR GLU PRO GLY ASN
SEQRES 4 A 201 MET GLY ILE SER ALA GLY PRO ILE VAL ALA ASP ALA LEU
SEQRES 5 A 201 GLU ARG ILE TYR GLY ALA ASN ASP VAL TRP VAL GLN GLY
SEQRES 6 A 201 VAL GLY GLY PRO TYR LEU ALA ASP LEU ALA SER ASN PHE
SEQRES 7 A 201 LEU PRO ASP GLY THR SER SER ALA ALA ILE ASN GLU ALA
SEQRES 8 A 201 ARG ARG LEU PHE THR LEU ALA ASN THR LYS CYS PRO ASN
SEQRES 9 A 201 ALA ALA ILE VAL SER GLY GLY TYR SER GLN GLY THR ALA
SEQRES 10 A 201 VAL MET ALA GLY SER ILE SER GLY LEU SER THR THR ILE
SEQRES 11 A 201 LYS ASN GLN ILE LYS GLY VAL VAL LEU PHE GLY TYR THR
SEQRES 12 A 201 LYS ASN LEU GLN ASN LEU GLY ARG ILE PRO ASN PHE GLU
SEQRES 13 A 201 THR SER LYS THR GLU VAL TYR CYS ASP ILE ALA ASP ALA
SEQRES 14 A 201 VAL CYS TYR GLY THR LEU PHE ILE LEU PRO ALA HIS PHE
SEQRES 15 A 201 LEU TYR GLN THR ASP ALA ALA VAL ALA ALA PRO ARG PHE
SEQRES 16 A 201 LEU GLN ALA ARG ILE GLY
SEQRES 1 B 201 ALA MET ALA ILE SER ASP PRO GLN SER SER THR ARG ASN
SEQRES 2 B 201 GLU LEU GLU THR GLY SER SER SER ALA CYS PRO LYS VAL
SEQRES 3 B 201 ILE TYR ILE PHE ALA ARG ALA SER THR GLU PRO GLY ASN
SEQRES 4 B 201 MET GLY ILE SER ALA GLY PRO ILE VAL ALA ASP ALA LEU
SEQRES 5 B 201 GLU ARG ILE TYR GLY ALA ASN ASP VAL TRP VAL GLN GLY
SEQRES 6 B 201 VAL GLY GLY PRO TYR LEU ALA ASP LEU ALA SER ASN PHE
SEQRES 7 B 201 LEU PRO ASP GLY THR SER SER ALA ALA ILE ASN GLU ALA
SEQRES 8 B 201 ARG ARG LEU PHE THR LEU ALA ASN THR LYS CYS PRO ASN
SEQRES 9 B 201 ALA ALA ILE VAL SER GLY GLY TYR SER GLN GLY THR ALA
SEQRES 10 B 201 VAL MET ALA GLY SER ILE SER GLY LEU SER THR THR ILE
SEQRES 11 B 201 LYS ASN GLN ILE LYS GLY VAL VAL LEU PHE GLY TYR THR
SEQRES 12 B 201 LYS ASN LEU GLN ASN LEU GLY ARG ILE PRO ASN PHE GLU
SEQRES 13 B 201 THR SER LYS THR GLU VAL TYR CYS ASP ILE ALA ASP ALA
SEQRES 14 B 201 VAL CYS TYR GLY THR LEU PHE ILE LEU PRO ALA HIS PHE
SEQRES 15 B 201 LEU TYR GLN THR ASP ALA ALA VAL ALA ALA PRO ARG PHE
SEQRES 16 B 201 LEU GLN ALA ARG ILE GLY
SEQRES 1 C 201 ALA MET ALA ILE SER ASP PRO GLN SER SER THR ARG ASN
SEQRES 2 C 201 GLU LEU GLU THR GLY SER SER SER ALA CYS PRO LYS VAL
SEQRES 3 C 201 ILE TYR ILE PHE ALA ARG ALA SER THR GLU PRO GLY ASN
SEQRES 4 C 201 MET GLY ILE SER ALA GLY PRO ILE VAL ALA ASP ALA LEU
SEQRES 5 C 201 GLU ARG ILE TYR GLY ALA ASN ASP VAL TRP VAL GLN GLY
SEQRES 6 C 201 VAL GLY GLY PRO TYR LEU ALA ASP LEU ALA SER ASN PHE
SEQRES 7 C 201 LEU PRO ASP GLY THR SER SER ALA ALA ILE ASN GLU ALA
SEQRES 8 C 201 ARG ARG LEU PHE THR LEU ALA ASN THR LYS CYS PRO ASN
SEQRES 9 C 201 ALA ALA ILE VAL SER GLY GLY TYR SER GLN GLY THR ALA
SEQRES 10 C 201 VAL MET ALA GLY SER ILE SER GLY LEU SER THR THR ILE
SEQRES 11 C 201 LYS ASN GLN ILE LYS GLY VAL VAL LEU PHE GLY TYR THR
SEQRES 12 C 201 LYS ASN LEU GLN ASN LEU GLY ARG ILE PRO ASN PHE GLU
SEQRES 13 C 201 THR SER LYS THR GLU VAL TYR CYS ASP ILE ALA ASP ALA
SEQRES 14 C 201 VAL CYS TYR GLY THR LEU PHE ILE LEU PRO ALA HIS PHE
SEQRES 15 C 201 LEU TYR GLN THR ASP ALA ALA VAL ALA ALA PRO ARG PHE
SEQRES 16 C 201 LEU GLN ALA ARG ILE GLY
SEQRES 1 D 201 ALA MET ALA ILE SER ASP PRO GLN SER SER THR ARG ASN
SEQRES 2 D 201 GLU LEU GLU THR GLY SER SER SER ALA CYS PRO LYS VAL
SEQRES 3 D 201 ILE TYR ILE PHE ALA ARG ALA SER THR GLU PRO GLY ASN
SEQRES 4 D 201 MET GLY ILE SER ALA GLY PRO ILE VAL ALA ASP ALA LEU
SEQRES 5 D 201 GLU ARG ILE TYR GLY ALA ASN ASP VAL TRP VAL GLN GLY
SEQRES 6 D 201 VAL GLY GLY PRO TYR LEU ALA ASP LEU ALA SER ASN PHE
SEQRES 7 D 201 LEU PRO ASP GLY THR SER SER ALA ALA ILE ASN GLU ALA
SEQRES 8 D 201 ARG ARG LEU PHE THR LEU ALA ASN THR LYS CYS PRO ASN
SEQRES 9 D 201 ALA ALA ILE VAL SER GLY GLY TYR SER GLN GLY THR ALA
SEQRES 10 D 201 VAL MET ALA GLY SER ILE SER GLY LEU SER THR THR ILE
SEQRES 11 D 201 LYS ASN GLN ILE LYS GLY VAL VAL LEU PHE GLY TYR THR
SEQRES 12 D 201 LYS ASN LEU GLN ASN LEU GLY ARG ILE PRO ASN PHE GLU
SEQRES 13 D 201 THR SER LYS THR GLU VAL TYR CYS ASP ILE ALA ASP ALA
SEQRES 14 D 201 VAL CYS TYR GLY THR LEU PHE ILE LEU PRO ALA HIS PHE
SEQRES 15 D 201 LEU TYR GLN THR ASP ALA ALA VAL ALA ALA PRO ARG PHE
SEQRES 16 D 201 LEU GLN ALA ARG ILE GLY
SEQRES 1 E 201 ALA MET ALA ILE SER ASP PRO GLN SER SER THR ARG ASN
SEQRES 2 E 201 GLU LEU GLU THR GLY SER SER SER ALA CYS PRO LYS VAL
SEQRES 3 E 201 ILE TYR ILE PHE ALA ARG ALA SER THR GLU PRO GLY ASN
SEQRES 4 E 201 MET GLY ILE SER ALA GLY PRO ILE VAL ALA ASP ALA LEU
SEQRES 5 E 201 GLU ARG ILE TYR GLY ALA ASN ASP VAL TRP VAL GLN GLY
SEQRES 6 E 201 VAL GLY GLY PRO TYR LEU ALA ASP LEU ALA SER ASN PHE
SEQRES 7 E 201 LEU PRO ASP GLY THR SER SER ALA ALA ILE ASN GLU ALA
SEQRES 8 E 201 ARG ARG LEU PHE THR LEU ALA ASN THR LYS CYS PRO ASN
SEQRES 9 E 201 ALA ALA ILE VAL SER GLY GLY TYR SER GLN GLY THR ALA
SEQRES 10 E 201 VAL MET ALA GLY SER ILE SER GLY LEU SER THR THR ILE
SEQRES 11 E 201 LYS ASN GLN ILE LYS GLY VAL VAL LEU PHE GLY TYR THR
SEQRES 12 E 201 LYS ASN LEU GLN ASN LEU GLY ARG ILE PRO ASN PHE GLU
SEQRES 13 E 201 THR SER LYS THR GLU VAL TYR CYS ASP ILE ALA ASP ALA
SEQRES 14 E 201 VAL CYS TYR GLY THR LEU PHE ILE LEU PRO ALA HIS PHE
SEQRES 15 E 201 LEU TYR GLN THR ASP ALA ALA VAL ALA ALA PRO ARG PHE
SEQRES 16 E 201 LEU GLN ALA ARG ILE GLY
SEQRES 1 F 201 ALA MET ALA ILE SER ASP PRO GLN SER SER THR ARG ASN
SEQRES 2 F 201 GLU LEU GLU THR GLY SER SER SER ALA CYS PRO LYS VAL
SEQRES 3 F 201 ILE TYR ILE PHE ALA ARG ALA SER THR GLU PRO GLY ASN
SEQRES 4 F 201 MET GLY ILE SER ALA GLY PRO ILE VAL ALA ASP ALA LEU
SEQRES 5 F 201 GLU ARG ILE TYR GLY ALA ASN ASP VAL TRP VAL GLN GLY
SEQRES 6 F 201 VAL GLY GLY PRO TYR LEU ALA ASP LEU ALA SER ASN PHE
SEQRES 7 F 201 LEU PRO ASP GLY THR SER SER ALA ALA ILE ASN GLU ALA
SEQRES 8 F 201 ARG ARG LEU PHE THR LEU ALA ASN THR LYS CYS PRO ASN
SEQRES 9 F 201 ALA ALA ILE VAL SER GLY GLY TYR SER GLN GLY THR ALA
SEQRES 10 F 201 VAL MET ALA GLY SER ILE SER GLY LEU SER THR THR ILE
SEQRES 11 F 201 LYS ASN GLN ILE LYS GLY VAL VAL LEU PHE GLY TYR THR
SEQRES 12 F 201 LYS ASN LEU GLN ASN LEU GLY ARG ILE PRO ASN PHE GLU
SEQRES 13 F 201 THR SER LYS THR GLU VAL TYR CYS ASP ILE ALA ASP ALA
SEQRES 14 F 201 VAL CYS TYR GLY THR LEU PHE ILE LEU PRO ALA HIS PHE
SEQRES 15 F 201 LEU TYR GLN THR ASP ALA ALA VAL ALA ALA PRO ARG PHE
SEQRES 16 F 201 LEU GLN ALA ARG ILE GLY
SEQRES 1 G 201 ALA MET ALA ILE SER ASP PRO GLN SER SER THR ARG ASN
SEQRES 2 G 201 GLU LEU GLU THR GLY SER SER SER ALA CYS PRO LYS VAL
SEQRES 3 G 201 ILE TYR ILE PHE ALA ARG ALA SER THR GLU PRO GLY ASN
SEQRES 4 G 201 MET GLY ILE SER ALA GLY PRO ILE VAL ALA ASP ALA LEU
SEQRES 5 G 201 GLU ARG ILE TYR GLY ALA ASN ASP VAL TRP VAL GLN GLY
SEQRES 6 G 201 VAL GLY GLY PRO TYR LEU ALA ASP LEU ALA SER ASN PHE
SEQRES 7 G 201 LEU PRO ASP GLY THR SER SER ALA ALA ILE ASN GLU ALA
SEQRES 8 G 201 ARG ARG LEU PHE THR LEU ALA ASN THR LYS CYS PRO ASN
SEQRES 9 G 201 ALA ALA ILE VAL SER GLY GLY TYR SER GLN GLY THR ALA
SEQRES 10 G 201 VAL MET ALA GLY SER ILE SER GLY LEU SER THR THR ILE
SEQRES 11 G 201 LYS ASN GLN ILE LYS GLY VAL VAL LEU PHE GLY TYR THR
SEQRES 12 G 201 LYS ASN LEU GLN ASN LEU GLY ARG ILE PRO ASN PHE GLU
SEQRES 13 G 201 THR SER LYS THR GLU VAL TYR CYS ASP ILE ALA ASP ALA
SEQRES 14 G 201 VAL CYS TYR GLY THR LEU PHE ILE LEU PRO ALA HIS PHE
SEQRES 15 G 201 LEU TYR GLN THR ASP ALA ALA VAL ALA ALA PRO ARG PHE
SEQRES 16 G 201 LEU GLN ALA ARG ILE GLY
SEQRES 1 H 201 ALA MET ALA ILE SER ASP PRO GLN SER SER THR ARG ASN
SEQRES 2 H 201 GLU LEU GLU THR GLY SER SER SER ALA CYS PRO LYS VAL
SEQRES 3 H 201 ILE TYR ILE PHE ALA ARG ALA SER THR GLU PRO GLY ASN
SEQRES 4 H 201 MET GLY ILE SER ALA GLY PRO ILE VAL ALA ASP ALA LEU
SEQRES 5 H 201 GLU ARG ILE TYR GLY ALA ASN ASP VAL TRP VAL GLN GLY
SEQRES 6 H 201 VAL GLY GLY PRO TYR LEU ALA ASP LEU ALA SER ASN PHE
SEQRES 7 H 201 LEU PRO ASP GLY THR SER SER ALA ALA ILE ASN GLU ALA
SEQRES 8 H 201 ARG ARG LEU PHE THR LEU ALA ASN THR LYS CYS PRO ASN
SEQRES 9 H 201 ALA ALA ILE VAL SER GLY GLY TYR SER GLN GLY THR ALA
SEQRES 10 H 201 VAL MET ALA GLY SER ILE SER GLY LEU SER THR THR ILE
SEQRES 11 H 201 LYS ASN GLN ILE LYS GLY VAL VAL LEU PHE GLY TYR THR
SEQRES 12 H 201 LYS ASN LEU GLN ASN LEU GLY ARG ILE PRO ASN PHE GLU
SEQRES 13 H 201 THR SER LYS THR GLU VAL TYR CYS ASP ILE ALA ASP ALA
SEQRES 14 H 201 VAL CYS TYR GLY THR LEU PHE ILE LEU PRO ALA HIS PHE
SEQRES 15 H 201 LEU TYR GLN THR ASP ALA ALA VAL ALA ALA PRO ARG PHE
SEQRES 16 H 201 LEU GLN ALA ARG ILE GLY
HET DEP A 401 8
HET DEP B 402 8
HET DEP C 403 8
HET DEP D 404 8
HET DEP E 405 8
HET DEP F 406 8
HET DEP G 407 8
HET DEP H 408 8
HETNAM DEP DIETHYL PHOSPHONATE
FORMUL 9 DEP 8(C4 H11 O3 P)
FORMUL 17 HOH *4(H2 O)
HELIX 1 1 SER A 66 GLY A 80 1 15
HELIX 2 2 ASP A 96 LEU A 102 5 7
HELIX 3 3 SER A 107 CYS A 125 1 19
HELIX 4 4 SER A 136 GLY A 148 1 13
HELIX 5 5 SER A 150 ASN A 155 1 6
HELIX 6 6 LYS A 167 LEU A 172 1 6
HELIX 7 7 GLU A 179 SER A 181 5 3
HELIX 8 8 ASP A 191 GLY A 196 5 6
HELIX 9 9 TYR A 207 VAL A 213 1 7
HELIX 10 10 VAL A 213 ILE A 223 1 11
HELIX 11 11 SER B 66 GLY B 80 1 15
HELIX 12 12 LEU B 97 LEU B 102 5 6
HELIX 13 13 SER B 107 CYS B 125 1 19
HELIX 14 14 SER B 136 SER B 147 1 12
HELIX 15 15 SER B 150 ASN B 155 1 6
HELIX 16 16 GLU B 179 SER B 181 5 3
HELIX 17 17 ASP B 191 GLY B 196 5 6
HELIX 18 18 TYR B 207 VAL B 213 1 7
HELIX 19 19 VAL B 213 GLY B 224 1 12
HELIX 20 20 ASN C 36 GLY C 41 1 6
HELIX 21 21 SER C 66 GLY C 80 1 15
HELIX 22 22 ASP C 96 LEU C 102 5 7
HELIX 23 23 SER C 107 CYS C 125 1 19
HELIX 24 24 GLN C 137 GLY C 148 1 12
HELIX 25 25 SER C 150 GLN C 156 1 7
HELIX 26 26 GLU C 179 SER C 181 5 3
HELIX 27 27 ASP C 191 GLY C 196 5 6
HELIX 28 28 TYR C 207 VAL C 213 1 7
HELIX 29 29 VAL C 213 GLY C 224 1 12
HELIX 30 30 SER D 66 GLY D 80 1 15
HELIX 31 31 ASP D 96 LEU D 102 5 7
HELIX 32 32 SER D 107 CYS D 125 1 19
HELIX 33 33 SER D 136 GLY D 148 1 13
HELIX 34 34 SER D 150 ASN D 155 1 6
HELIX 35 35 ASP D 191 GLY D 196 5 6
HELIX 36 36 TYR D 207 VAL D 213 1 7
HELIX 37 37 VAL D 213 GLY D 224 1 12
HELIX 38 38 ASN E 36 GLY E 41 1 6
HELIX 39 39 SER E 66 GLY E 80 1 15
HELIX 40 40 LEU E 97 LEU E 102 5 6
HELIX 41 41 SER E 107 CYS E 125 1 19
HELIX 42 42 SER E 136 SER E 147 1 12
HELIX 43 43 SER E 150 GLN E 156 1 7
HELIX 44 44 GLU E 179 SER E 181 5 3
HELIX 45 45 ASP E 191 GLY E 196 5 6
HELIX 46 46 TYR E 207 VAL E 213 1 7
HELIX 47 47 VAL E 213 GLY E 224 1 12
HELIX 48 48 ASN F 36 GLY F 41 1 6
HELIX 49 49 SER F 66 GLY F 80 1 15
HELIX 50 50 LEU F 97 LEU F 102 5 6
HELIX 51 51 SER F 107 CYS F 125 1 19
HELIX 52 52 SER F 136 GLY F 148 1 13
HELIX 53 53 SER F 150 GLN F 156 1 7
HELIX 54 54 GLU F 179 SER F 181 5 3
HELIX 55 55 ASP F 191 GLY F 196 5 6
HELIX 56 56 TYR F 207 VAL F 213 1 7
HELIX 57 57 VAL F 213 GLY F 224 1 12
HELIX 58 58 SER G 42 CYS G 46 5 5
HELIX 59 59 SER G 66 GLY G 80 1 15
HELIX 60 60 ASP G 96 LEU G 102 5 7
HELIX 61 61 SER G 107 CYS G 125 1 19
HELIX 62 62 GLN G 137 SER G 147 1 11
HELIX 63 63 SER G 150 GLN G 156 1 7
HELIX 64 64 LYS G 167 LEU G 172 1 6
HELIX 65 65 ASP G 191 TYR G 195 5 5
HELIX 66 66 TYR G 207 VAL G 213 1 7
HELIX 67 67 VAL G 213 GLY G 224 1 12
HELIX 68 68 ASN H 36 GLY H 41 1 6
HELIX 69 69 SER H 66 GLY H 80 1 15
HELIX 70 70 ASP H 96 LEU H 102 5 7
HELIX 71 71 SER H 107 CYS H 125 1 19
HELIX 72 72 SER H 136 SER H 147 1 12
HELIX 73 73 SER H 150 GLN H 156 1 7
HELIX 74 74 GLU H 179 SER H 181 5 3
HELIX 75 75 ASP H 191 TYR H 195 5 5
HELIX 76 76 TYR H 207 VAL H 213 1 7
HELIX 77 77 VAL H 213 GLY H 224 1 12
SHEET 1 A 5 VAL A 84 GLY A 88 0
SHEET 2 A 5 VAL A 49 ALA A 54 1 N TYR A 51 O TRP A 85
SHEET 3 A 5 ALA A 129 TYR A 135 1 O VAL A 131 N ILE A 50
SHEET 4 A 5 ILE A 157 PHE A 163 1 O LYS A 158 N ILE A 130
SHEET 5 A 5 THR A 183 TYR A 186 1 O TYR A 186 N LEU A 162
SHEET 1 B 5 VAL B 84 GLY B 88 0
SHEET 2 B 5 VAL B 49 ALA B 54 1 N TYR B 51 O GLN B 87
SHEET 3 B 5 ALA B 129 TYR B 135 1 O VAL B 131 N ILE B 50
SHEET 4 B 5 ILE B 157 PHE B 163 1 O PHE B 163 N GLY B 134
SHEET 5 B 5 THR B 183 TYR B 186 1 O TYR B 186 N LEU B 162
SHEET 1 C 5 VAL C 84 GLY C 88 0
SHEET 2 C 5 VAL C 49 ALA C 54 1 N TYR C 51 O GLN C 87
SHEET 3 C 5 ALA C 129 TYR C 135 1 O ALA C 129 N ILE C 50
SHEET 4 C 5 ILE C 157 PHE C 163 1 O LYS C 158 N ILE C 130
SHEET 5 C 5 THR C 183 TYR C 186 1 O TYR C 186 N LEU C 162
SHEET 1 D 5 VAL D 84 GLY D 88 0
SHEET 2 D 5 VAL D 49 ALA D 54 1 N TYR D 51 O TRP D 85
SHEET 3 D 5 ALA D 129 TYR D 135 1 O ALA D 129 N ILE D 50
SHEET 4 D 5 ILE D 157 PHE D 163 1 O LYS D 158 N ILE D 130
SHEET 5 D 5 THR D 183 TYR D 186 1 O TYR D 186 N LEU D 162
SHEET 1 E 5 VAL E 84 GLY E 88 0
SHEET 2 E 5 VAL E 49 ALA E 54 1 N TYR E 51 O TRP E 85
SHEET 3 E 5 ALA E 129 TYR E 135 1 O VAL E 131 N ILE E 50
SHEET 4 E 5 ILE E 157 PHE E 163 1 O PHE E 163 N GLY E 134
SHEET 5 E 5 THR E 183 TYR E 186 1 O TYR E 186 N LEU E 162
SHEET 1 F 5 VAL F 84 GLY F 88 0
SHEET 2 F 5 VAL F 49 ALA F 54 1 N TYR F 51 O GLN F 87
SHEET 3 F 5 ALA F 129 TYR F 135 1 O VAL F 131 N ILE F 50
SHEET 4 F 5 ILE F 157 PHE F 163 1 O LYS F 158 N ILE F 130
SHEET 5 F 5 THR F 183 TYR F 186 1 O TYR F 186 N LEU F 162
SHEET 1 G 5 VAL G 84 GLY G 88 0
SHEET 2 G 5 VAL G 49 ALA G 54 1 N TYR G 51 O GLN G 87
SHEET 3 G 5 ALA G 129 TYR G 135 1 O ALA G 129 N ILE G 50
SHEET 4 G 5 ILE G 157 PHE G 163 1 O PHE G 163 N GLY G 134
SHEET 5 G 5 THR G 183 TYR G 186 1 O GLU G 184 N LEU G 162
SHEET 1 H 5 VAL H 84 GLY H 88 0
SHEET 2 H 5 VAL H 49 ALA H 54 1 N TYR H 51 O TRP H 85
SHEET 3 H 5 ALA H 129 TYR H 135 1 O ALA H 129 N ILE H 50
SHEET 4 H 5 ILE H 157 PHE H 163 1 O PHE H 163 N GLY H 134
SHEET 5 H 5 THR H 183 TYR H 186 1 O TYR H 186 N LEU H 162
SSBOND 1 CYS A 46 CYS A 125 1555 1555 2.06
SSBOND 2 CYS A 187 CYS A 194 1555 1555 2.10
SSBOND 3 CYS B 46 CYS B 125 1555 1555 2.05
SSBOND 4 CYS B 187 CYS B 194 1555 1555 2.13
SSBOND 5 CYS C 46 CYS C 125 1555 1555 2.07
SSBOND 6 CYS C 187 CYS C 194 1555 1555 2.10
SSBOND 7 CYS D 46 CYS D 125 1555 1555 2.06
SSBOND 8 CYS D 187 CYS D 194 1555 1555 2.09
SSBOND 9 CYS E 46 CYS E 125 1555 1555 2.07
SSBOND 10 CYS E 187 CYS E 194 1555 1555 2.09
SSBOND 11 CYS F 46 CYS F 125 1555 1555 2.09
SSBOND 12 CYS F 187 CYS F 194 1555 1555 2.11
SSBOND 13 CYS G 46 CYS G 125 1555 1555 2.06
SSBOND 14 CYS G 187 CYS G 194 1555 1555 2.13
SSBOND 15 CYS H 46 CYS H 125 1555 1555 2.07
SSBOND 16 CYS H 187 CYS H 194 1555 1555 2.10
LINK OG SER A 136 P DEP A 401 1555 1555 1.87
LINK OG SER B 136 P DEP B 402 1555 1555 1.91
LINK OG SER C 136 P DEP C 403 1555 1555 1.83
LINK OG SER D 136 P DEP D 404 1555 1555 2.00
LINK OG SER E 136 P DEP E 405 1555 1555 1.93
LINK OG SER F 136 P DEP F 406 1555 1555 1.74
LINK OG SER G 136 P DEP G 407 1555 1555 2.19
LINK OG SER H 136 P DEP H 408 1555 1555 1.73
CISPEP 1 ILE A 223 GLY A 224 0 0.65
CISPEP 2 PHE D 199 ILE D 200 0 -8.02
CISPEP 3 TYR G 195 GLY G 196 0 -16.87
CISPEP 4 PRO H 202 ALA H 203 0 -6.48
SITE 1 AC1 5 ALA A 56 SER A 57 ASN A 100 SER A 136
SITE 2 AC1 5 GLN A 137
SITE 1 AC2 4 SER B 57 ASN B 100 SER B 136 GLN B 137
SITE 1 AC3 5 ALA C 56 SER C 57 SER C 136 GLN C 137
SITE 2 AC3 5 PHE C 199
SITE 1 AC4 8 ALA D 56 SER D 57 ASN D 100 TYR D 135
SITE 2 AC4 8 SER D 136 GLN D 137 VAL D 193 PHE D 199
SITE 1 AC5 7 ALA E 56 SER E 57 ASN E 100 TYR E 135
SITE 2 AC5 7 SER E 136 GLN E 137 VAL E 193
SITE 1 AC6 8 ALA F 56 SER F 57 ASN F 100 TYR F 135
SITE 2 AC6 8 SER F 136 GLN F 137 VAL F 193 LEU F 198
SITE 1 AC7 7 ALA G 56 SER G 57 ASN G 100 TYR G 135
SITE 2 AC7 7 SER G 136 GLN G 137 LEU G 201
SITE 1 AC8 7 ALA H 56 SER H 57 TYR H 135 SER H 136
SITE 2 AC8 7 GLN H 137 VAL H 193 PHE H 199
CRYST1 73.470 117.370 95.240 90.00 103.57 90.00 P 1 21 1 16
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 0.013610 0.000000 0.003286 0.00000
SCALE2 0.000000 0.008520 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010801 0.00000
TER 1432 GLY A 224
TER 2868 GLY B 224
TER 4295 GLY C 224
TER 5731 GLY D 224
TER 7158 GLY E 224
TER 8585 GLY F 224
TER 10011 GLY G 224
TER 11436 GLY H 224
MASTER 584 0 8 77 40 0 15 611496 8 104 128
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