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HEADER COMPLEX (HYDROLASE/COFACTOR) 13-SEP-95 1ETH
TITLE TRIACYLGLYCEROL LIPASE/COLIPASE COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRIACYLGLYCEROL ACYL-HYDROLASE;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: TRIACYLGLYCEROL LIPASE;
COMPND 5 EC: 3.1.1.3;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: COLIPASE;
COMPND 8 CHAIN: B, D
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGAN: PANCREAS;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 7 ORGANISM_COMMON: PIG
KEYWDS COMPLEX (HYDROLASE/COFACTOR), LIPID DEGRADATION
EXPDTA X-RAY DIFFRACTION
AUTHOR J.HERMOSO,D.PIGNOL,B.KERFELEC,I.CRENON,C.CHAPUS,
AUTHOR 2 J.C.FONTECILLA-CAMPS
REVDAT 1 07-DEC-96 1ETH 0
JRNL AUTH J.HERMOSO,D.PIGNOL,B.KERFELEC,I.CRENON,C.CHAPUS,
JRNL AUTH 2 J.C.FONTECILLA-CAMPS
JRNL TITL LIPASE ACTIVATION BY NON-IONIC DETERGENTS. THE
JRNL TITL 2 CRYSTAL STRUCTURE OF THE PORCINE
JRNL TITL 3 LIPASE-COLIPASE-TETRAETHYLENE GLYCOL MONOOCTYL
JRNL TITL 4 ETHER COMPLEX
JRNL REF J.BIOL.CHEM. V. 271 18007 1996
JRNL REFN ASTM JBCHA3 US ISSN 0021-9258 0071
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH H.VAN TILBEURGH,M.P.EGLOFF,C.MARTINEZ,N.RUGANI,
REMARK 1 AUTH 2 R.VERGER,C.CAMBILLAU
REMARK 1 TITL INTERFACIAL ACTIVATION OF THE LIPASE-PROCOLIPASE
REMARK 1 TITL 2 COMPLEX BY MIXED MICELLES REVEALED BY X-RAY
REMARK 1 TITL 3 CRYSTALLOGRAPHY
REMARK 1 REF NATURE V. 362 814 1993
REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 0006
REMARK 1 REFERENCE 2
REMARK 1 AUTH H.VAN TILBEURGH,L.SARDA,R.VERGER,C.CAMBILLAU
REMARK 1 TITL STRUCTURE OF THE PANCREATIC LIPASE-PROCOLIPASE
REMARK 1 TITL 2 COMPLEX
REMARK 1 REF NATURE V. 359 159 1992
REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 0006
REMARK 2
REMARK 2 RESOLUTION. 2.8 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.8
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 76.
REMARK 3 NUMBER OF REFLECTIONS : 33758
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.21
REMARK 3 FREE R VALUE : 0.29
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8340
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 272
REMARK 3 SOLVENT ATOMS : 357
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.73
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.44
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 27.26
REMARK 3 IMPROPER ANGLES (DEGREES) : 2.57
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 DESCRIPTION OF MODIFICATION: THE AUTHORS HAVE A PROBLEM
REMARK 3 WITH X-PLOR WHEN PRO 4 IS THE FIRST RESIDUE IN THE
REMARK 3 COLIPASE CHAIN. THEY HAVE OVERCOME THE DIFFICULTY BY
REMARK 3 GIVING THE ADJACENT RESIDUE ASP 3 AN OCCUPANCY OF ZERO.
REMARK 3 THE COORDINATE FILE FOR RUNNING X-PLOR PROGRAM IS
REMARK 3 LIPCOL_XPLOR.PDB.
REMARK 4
REMARK 4 1ETH COMPLIES WITH FORMAT V. 2.1, 25-OCT-1996
REMARK 6
REMARK 6 CRYST1
REMARK 6 UNUSUAL UNIT-CELL DATA: PSEUDOSYMMETRY P 23
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-12-1994
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : LURE
REMARK 200 BEAMLINE : W32
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.90
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42501
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.80
REMARK 200 RESOLUTION RANGE LOW (A) : 12.4
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 86.
REMARK 200 DATA REDUNDANCY : 4.
REMARK 200 R MERGE (I) : 0.13
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: F 2 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z,-X,-Y
REMARK 290 7555 -Z,-X,Y
REMARK 290 8555 -Z,X,-Y
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z,-X
REMARK 290 11555 Y,-Z,-X
REMARK 290 12555 -Y,-Z,X
REMARK 290 13555 X,1/2+Y,1/2+Z
REMARK 290 14555 -X,1/2-Y,1/2+Z
REMARK 290 15555 -X,1/2+Y,1/2-Z
REMARK 290 16555 X,1/2-Y,1/2-Z
REMARK 290 17555 Z,1/2+X,1/2+Y
REMARK 290 18555 Z,1/2-X,1/2-Y
REMARK 290 19555 -Z,1/2-X,1/2+Y
REMARK 290 20555 -Z,1/2+X,1/2-Y
REMARK 290 21555 Y,1/2+Z,1/2+X
REMARK 290 22555 -Y,1/2+Z,1/2-X
REMARK 290 23555 Y,1/2-Z,1/2-X
REMARK 290 24555 -Y,1/2-Z,1/2+X
REMARK 290 25555 1/2+X,Y,1/2+Z
REMARK 290 26555 1/2-X,-Y,1/2+Z
REMARK 290 27555 1/2-X,Y,1/2-Z
REMARK 290 28555 1/2+X,-Y,1/2-Z
REMARK 290 29555 1/2+Z,X,1/2+Y
REMARK 290 30555 1/2+Z,-X,1/2-Y
REMARK 290 31555 1/2-Z,-X,1/2+Y
REMARK 290 32555 1/2-Z,X,1/2-Y
REMARK 290 33555 1/2+Y,Z,1/2+X
REMARK 290 34555 1/2-Y,Z,1/2-X
REMARK 290 35555 1/2+Y,-Z,1/2-X
REMARK 290 36555 1/2-Y,-Z,1/2+X
REMARK 290 37555 1/2+X,1/2+Y,Z
REMARK 290 38555 1/2-X,1/2-Y,Z
REMARK 290 39555 1/2-X,1/2+Y,-Z
REMARK 290 40555 1/2+X,1/2-Y,-Z
REMARK 290 41555 1/2+Z,1/2+X,Y
REMARK 290 42555 1/2+Z,1/2-X,-Y
REMARK 290 43555 1/2-Z,1/2-X,Y
REMARK 290 44555 1/2-Z,1/2+X,-Y
REMARK 290 45555 1/2+Y,1/2+Z,X
REMARK 290 46555 1/2-Y,1/2+Z,-X
REMARK 290 47555 1/2+Y,1/2-Z,-X
REMARK 290 48555 1/2-Y,1/2-Z,X
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 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 144.55045
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 144.55045
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 144.55045
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 144.55045
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 144.55045
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 144.55045
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 144.55045
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 144.55045
REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 144.55045
REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 144.55045
REMARK 290 SMTRY1 18 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 18 -1.000000 0.000000 0.000000 144.55045
REMARK 290 SMTRY3 18 0.000000 -1.000000 0.000000 144.55045
REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 144.55045
REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 144.55045
REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 20 1.000000 0.000000 0.000000 144.55045
REMARK 290 SMTRY3 20 0.000000 -1.000000 0.000000 144.55045
REMARK 290 SMTRY1 21 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 144.55045
REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 144.55045
REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 22 0.000000 0.000000 1.000000 144.55045
REMARK 290 SMTRY3 22 -1.000000 0.000000 0.000000 144.55045
REMARK 290 SMTRY1 23 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 23 0.000000 0.000000 -1.000000 144.55045
REMARK 290 SMTRY3 23 -1.000000 0.000000 0.000000 144.55045
REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 144.55045
REMARK 290 SMTRY3 24 1.000000 0.000000 0.000000 144.55045
REMARK 290 SMTRY1 25 1.000000 0.000000 0.000000 144.55045
REMARK 290 SMTRY2 25 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 25 0.000000 0.000000 1.000000 144.55045
REMARK 290 SMTRY1 26 -1.000000 0.000000 0.000000 144.55045
REMARK 290 SMTRY2 26 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 26 0.000000 0.000000 1.000000 144.55045
REMARK 290 SMTRY1 27 -1.000000 0.000000 0.000000 144.55045
REMARK 290 SMTRY2 27 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 27 0.000000 0.000000 -1.000000 144.55045
REMARK 290 SMTRY1 28 1.000000 0.000000 0.000000 144.55045
REMARK 290 SMTRY2 28 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 28 0.000000 0.000000 -1.000000 144.55045
REMARK 290 SMTRY1 29 0.000000 0.000000 1.000000 144.55045
REMARK 290 SMTRY2 29 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 29 0.000000 1.000000 0.000000 144.55045
REMARK 290 SMTRY1 30 0.000000 0.000000 1.000000 144.55045
REMARK 290 SMTRY2 30 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 30 0.000000 -1.000000 0.000000 144.55045
REMARK 290 SMTRY1 31 0.000000 0.000000 -1.000000 144.55045
REMARK 290 SMTRY2 31 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 31 0.000000 1.000000 0.000000 144.55045
REMARK 290 SMTRY1 32 0.000000 0.000000 -1.000000 144.55045
REMARK 290 SMTRY2 32 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 32 0.000000 -1.000000 0.000000 144.55045
REMARK 290 SMTRY1 33 0.000000 1.000000 0.000000 144.55045
REMARK 290 SMTRY2 33 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 33 1.000000 0.000000 0.000000 144.55045
REMARK 290 SMTRY1 34 0.000000 -1.000000 0.000000 144.55045
REMARK 290 SMTRY2 34 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 34 -1.000000 0.000000 0.000000 144.55045
REMARK 290 SMTRY1 35 0.000000 1.000000 0.000000 144.55045
REMARK 290 SMTRY2 35 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 35 -1.000000 0.000000 0.000000 144.55045
REMARK 290 SMTRY1 36 0.000000 -1.000000 0.000000 144.55045
REMARK 290 SMTRY2 36 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 36 1.000000 0.000000 0.000000 144.55045
REMARK 290 SMTRY1 37 1.000000 0.000000 0.000000 144.55045
REMARK 290 SMTRY2 37 0.000000 1.000000 0.000000 144.55045
REMARK 290 SMTRY3 37 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 38 -1.000000 0.000000 0.000000 144.55045
REMARK 290 SMTRY2 38 0.000000 -1.000000 0.000000 144.55045
REMARK 290 SMTRY3 38 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 39 -1.000000 0.000000 0.000000 144.55045
REMARK 290 SMTRY2 39 0.000000 1.000000 0.000000 144.55045
REMARK 290 SMTRY3 39 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 40 1.000000 0.000000 0.000000 144.55045
REMARK 290 SMTRY2 40 0.000000 -1.000000 0.000000 144.55045
REMARK 290 SMTRY3 40 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 41 0.000000 0.000000 1.000000 144.55045
REMARK 290 SMTRY2 41 1.000000 0.000000 0.000000 144.55045
REMARK 290 SMTRY3 41 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 42 0.000000 0.000000 1.000000 144.55045
REMARK 290 SMTRY2 42 -1.000000 0.000000 0.000000 144.55045
REMARK 290 SMTRY3 42 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 43 0.000000 0.000000 -1.000000 144.55045
REMARK 290 SMTRY2 43 -1.000000 0.000000 0.000000 144.55045
REMARK 290 SMTRY3 43 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 44 0.000000 0.000000 -1.000000 144.55045
REMARK 290 SMTRY2 44 1.000000 0.000000 0.000000 144.55045
REMARK 290 SMTRY3 44 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 45 0.000000 1.000000 0.000000 144.55045
REMARK 290 SMTRY2 45 0.000000 0.000000 1.000000 144.55045
REMARK 290 SMTRY3 45 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 46 0.000000 -1.000000 0.000000 144.55045
REMARK 290 SMTRY2 46 0.000000 0.000000 1.000000 144.55045
REMARK 290 SMTRY3 46 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 47 0.000000 1.000000 0.000000 144.55045
REMARK 290 SMTRY2 47 0.000000 0.000000 -1.000000 144.55045
REMARK 290 SMTRY3 47 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 48 0.000000 -1.000000 0.000000 144.55045
REMARK 290 SMTRY2 48 0.000000 0.000000 -1.000000 144.55045
REMARK 290 SMTRY3 48 1.000000 0.000000 0.000000 0.00000
REMARK 290
REMARK 290 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 A 208 PRO A 209 0 245.70
REMARK 500 ALA A 333 SER A 334 0 232.31
REMARK 500 SER A 334 ASN A 335 0 125.45
REMARK 500 ASN A 405 VAL A 406 0 147.07
REMARK 500 ALA C 208 PRO C 209 0 246.00
REMARK 500 ALA C 333 SER C 334 0 232.99
REMARK 500 SER C 334 ASN C 335 0 127.23
REMARK 500 ASN C 405 VAL C 406 0 146.42
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. SOME OF THESE MAY BE ATOMS
REMARK 500 LOCATED ON SPECIAL POSITIONS IN THE CELL.
REMARK 500
REMARK 500 DISTANCE CUTOFF: 2.2 ANGSTROMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 2H HOH D 310 HE ARG A 413 18555 1.74
REMARK 500 HE ARG A 413 2H HOH D 310 48555 1.74
REMARK 500 2H HOH D 310 2HH1 ARG A 438 18555 1.77
REMARK 500 2HH1 ARG A 438 2H HOH D 310 48555 1.77
REMARK 500 1H HOH D 310 1HH2 ARG A 413 18555 1.86
REMARK 500 1HH2 ARG A 413 1H HOH D 310 48555 1.86
REMARK 500 1H HOH D 216 CG2 VAL D 76 19655 1.95
REMARK 500 CG2 VAL D 76 1H HOH D 216 46546 1.95
REMARK 500 2H HOH D 28 3H SER A 1 21545 2.00
REMARK 500 3H SER A 1 2H HOH D 28 29455 2.00
REMARK 500 H CYS C 4 O GLN A 434 18555 2.01
REMARK 500 O GLN A 434 H CYS C 4 48555 2.01
REMARK 500 H THR C 116 OD2 ASP D 72 19655 2.02
REMARK 500 OD2 ASP D 72 H THR C 116 46546 2.02
REMARK 500 2HH1 ARG A 438 1H HOH D 310 48555 2.05
REMARK 500 1H HOH D 310 2HH1 ARG A 438 18555 2.05
REMARK 500 OD2 ASP B 72 H THR A 116 23555 2.06
REMARK 500 H THR A 116 OD2 ASP B 72 32555 2.06
REMARK 500 O ASN B 81 1H HOH D 251 23555 2.08
REMARK 500 O HOH D 28 3H SER A 1 21545 2.08
REMARK 500 1H HOH D 251 O ASN B 81 32555 2.08
REMARK 500 3H SER A 1 O HOH D 28 29455 2.08
REMARK 500 H CYS A 4 O GLN C 434 29455 2.14
REMARK 500 O GLN C 434 H CYS A 4 21545 2.14
REMARK 500 2H HOH D 251 CE1 TYR B 59 32555 2.16
REMARK 500 CE1 TYR B 59 2H HOH D 251 23555 2.16
REMARK 850
REMARK 850 CORRECTION BEFORE RELEASE
REMARK 850 ORIGINAL DEPOSITION REVISED PRIOR TO RELEASE
REMARK 850 DATE REVISED: 20-DEC-1995 TRACKING NUMBER: T7138
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 1ETH B SWS P02703 1 - 3 NOT IN ATOMS LIST
REMARK 999 1ETH B SWS P02703 91 - 95 NOT IN ATOMS LIST
REMARK 999 1ETH D SWS P02703 1 - 3 NOT IN ATOMS LIST
REMARK 999 1ETH D SWS P02703 91 - 95 NOT IN ATOMS LIST
REMARK 999
REMARK 999 PART OF THE DISCREPANCIES IN SEQUENCE IS EXPLAINED AS
REMARK 999 FOLLOWS:
REMARK 999 CHAIN A AND C; MODIFICATIONS ABOUT RESIDUE 30 ARE
REMARK 999 EXPLAINED BY PROTEIN SEQUENCING AND ELECTRON DENSITY MAP.
REMARK 999 MAP. ASN 405 AND ASN 406 WERE NOT FOUND IN THE ELECTRON
REMARK 999 DENSITY MAP.
REMARK 999 CHAINS B AND D: MUTATION AT LEU 37 (SWISSPROT) TO SER 37
REMARK 999 IS MADE AFTER EGLOFF ET AL. (PDB ENTRY 1LPB) ON THE BASIS
REMARK 999 OF MASS SPECTROSCOPY.
DBREF 1ETH A 1 448 SWS P00591 LIPP_PIG 1 449
DBREF 1ETH B 4 90 SWS P02703 COL2_PIG 4 90
DBREF 1ETH C 1 448 SWS P00591 LIPP_PIG 1 449
DBREF 1ETH D 4 90 SWS P02703 COL2_PIG 4 90
SEQADV 1ETH TRP A 30 SWS P00591 MISSING FROM SWS
SEQADV 1ETH SER A 31 SWS P00591 PRO 30 CONFLICT
SEQADV 1ETH PRO A 32 SWS P00591 ASP 31 CONFLICT
SEQADV 1ETH A SWS P00591 ASN 405 GAP IN PDB ENTRY
SEQADV 1ETH A SWS P00591 ASN 406 GAP IN PDB ENTRY
SEQADV 1ETH TRP C 30 SWS P00591 MISSING FROM SWS
SEQADV 1ETH SER C 31 SWS P00591 PRO 30 CONFLICT
SEQADV 1ETH PRO C 32 SWS P00591 ASP 31 CONFLICT
SEQADV 1ETH C SWS P00591 ASN 405 GAP IN PDB ENTRY
SEQADV 1ETH C SWS P00591 ASN 406 GAP IN PDB ENTRY
SEQRES 1 A 448 SER GLU VAL CYS PHE PRO ARG LEU GLY CYS PHE SER ASP
SEQRES 2 A 448 ASP ALA PRO TRP ALA GLY ILE VAL GLN ARG PRO LEU LYS
SEQRES 3 A 448 ILE LEU PRO TRP SER PRO LYS ASP VAL ASP THR ARG PHE
SEQRES 4 A 448 LEU LEU TYR THR ASN GLN ASN GLN ASN ASN TYR GLN GLU
SEQRES 5 A 448 LEU VAL ALA ASP PRO SER THR ILE THR ASN SER ASN PHE
SEQRES 6 A 448 ARG MET ASP ARG LYS THR ARG PHE ILE ILE HIS GLY PHE
SEQRES 7 A 448 ILE ASP LYS GLY GLU GLU ASP TRP LEU SER ASN ILE CYS
SEQRES 8 A 448 LYS ASN LEU PHE LYS VAL GLU SER VAL ASN CYS ILE CYS
SEQRES 9 A 448 VAL ASP TRP LYS GLY GLY SER ARG THR GLY TYR THR GLN
SEQRES 10 A 448 ALA SER GLN ASN ILE ARG ILE VAL GLY ALA GLU VAL ALA
SEQRES 11 A 448 TYR PHE VAL GLU VAL LEU LYS SER SER LEU GLY TYR SER
SEQRES 12 A 448 PRO SER ASN VAL HIS VAL ILE GLY HIS SER LEU GLY SER
SEQRES 13 A 448 HIS ALA ALA GLY GLU ALA GLY ARG ARG THR ASN GLY THR
SEQRES 14 A 448 ILE GLU ARG ILE THR GLY LEU ASP PRO ALA GLU PRO CYS
SEQRES 15 A 448 PHE GLN GLY THR PRO GLU LEU VAL ARG LEU ASP PRO SER
SEQRES 16 A 448 ASP ALA LYS PHE VAL ASP VAL ILE HIS THR ASP ALA ALA
SEQRES 17 A 448 PRO ILE ILE PRO ASN LEU GLY PHE GLY MET SER GLN THR
SEQRES 18 A 448 VAL GLY HIS LEU ASP PHE PHE PRO ASN GLY GLY LYS GLN
SEQRES 19 A 448 MET PRO GLY CYS GLN LYS ASN ILE LEU SER GLN ILE VAL
SEQRES 20 A 448 ASP ILE ASP GLY ILE TRP GLU GLY THR ARG ASP PHE VAL
SEQRES 21 A 448 ALA CYS ASN HIS LEU ARG SER TYR LYS TYR TYR ALA ASP
SEQRES 22 A 448 SER ILE LEU ASN PRO ASP GLY PHE ALA GLY PHE PRO CYS
SEQRES 23 A 448 ASP SER TYR ASN VAL PHE THR ALA ASN LYS CYS PHE PRO
SEQRES 24 A 448 CYS PRO SER GLU GLY CYS PRO GLN MET GLY HIS TYR ALA
SEQRES 25 A 448 ASP ARG PHE PRO GLY LYS THR ASN GLY VAL SER GLN VAL
SEQRES 26 A 448 PHE TYR LEU ASN THR GLY ASP ALA SER ASN PHE ALA ARG
SEQRES 27 A 448 TRP ARG TYR LYS VAL SER VAL THR LEU SER GLY LYS LYS
SEQRES 28 A 448 VAL THR GLY HIS ILE LEU VAL SER LEU PHE GLY ASN GLU
SEQRES 29 A 448 GLY ASN SER ARG GLN TYR GLU ILE TYR LYS GLY THR LEU
SEQRES 30 A 448 GLN PRO ASP ASN THR HIS SER ASP GLU PHE ASP SER ASP
SEQRES 31 A 448 VAL GLU VAL GLY ASP LEU GLN LYS VAL LYS PHE ILE TRP
SEQRES 32 A 448 TYR ASN VAL ILE ASN PRO THR LEU PRO ARG VAL GLY ALA
SEQRES 33 A 448 SER LYS ILE THR VAL GLU ARG ASN ASP GLY LYS VAL TYR
SEQRES 34 A 448 ASP PHE CYS SER GLN GLU THR VAL ARG GLU GLU VAL LEU
SEQRES 35 A 448 LEU THR LEU ASN PRO CYS
SEQRES 1 B 95 VAL PRO ASP PRO ARG GLY ILE ILE ILE ASN LEU ASP GLU
SEQRES 2 B 95 GLY GLU LEU CYS LEU ASN SER ALA GLN CYS LYS SER ASN
SEQRES 3 B 95 CYS CYS GLN HIS ASP THR ILE LEU SER LEU SER ARG CYS
SEQRES 4 B 95 ALA LEU LYS ALA ARG GLU ASN SER GLU CYS SER ALA PHE
SEQRES 5 B 95 THR LEU TYR GLY VAL TYR TYR LYS CYS PRO CYS GLU ARG
SEQRES 6 B 95 GLY LEU THR CYS GLU GLY ASP LYS SER LEU VAL GLY SER
SEQRES 7 B 95 ILE THR ASN THR ASN PHE GLY ILE CYS HIS ASN VAL GLY
SEQRES 8 B 95 ARG SER ASP SER
SEQRES 1 C 448 SER GLU VAL CYS PHE PRO ARG LEU GLY CYS PHE SER ASP
SEQRES 2 C 448 ASP ALA PRO TRP ALA GLY ILE VAL GLN ARG PRO LEU LYS
SEQRES 3 C 448 ILE LEU PRO TRP SER PRO LYS ASP VAL ASP THR ARG PHE
SEQRES 4 C 448 LEU LEU TYR THR ASN GLN ASN GLN ASN ASN TYR GLN GLU
SEQRES 5 C 448 LEU VAL ALA ASP PRO SER THR ILE THR ASN SER ASN PHE
SEQRES 6 C 448 ARG MET ASP ARG LYS THR ARG PHE ILE ILE HIS GLY PHE
SEQRES 7 C 448 ILE ASP LYS GLY GLU GLU ASP TRP LEU SER ASN ILE CYS
SEQRES 8 C 448 LYS ASN LEU PHE LYS VAL GLU SER VAL ASN CYS ILE CYS
SEQRES 9 C 448 VAL ASP TRP LYS GLY GLY SER ARG THR GLY TYR THR GLN
SEQRES 10 C 448 ALA SER GLN ASN ILE ARG ILE VAL GLY ALA GLU VAL ALA
SEQRES 11 C 448 TYR PHE VAL GLU VAL LEU LYS SER SER LEU GLY TYR SER
SEQRES 12 C 448 PRO SER ASN VAL HIS VAL ILE GLY HIS SER LEU GLY SER
SEQRES 13 C 448 HIS ALA ALA GLY GLU ALA GLY ARG ARG THR ASN GLY THR
SEQRES 14 C 448 ILE GLU ARG ILE THR GLY LEU ASP PRO ALA GLU PRO CYS
SEQRES 15 C 448 PHE GLN GLY THR PRO GLU LEU VAL ARG LEU ASP PRO SER
SEQRES 16 C 448 ASP ALA LYS PHE VAL ASP VAL ILE HIS THR ASP ALA ALA
SEQRES 17 C 448 PRO ILE ILE PRO ASN LEU GLY PHE GLY MET SER GLN THR
SEQRES 18 C 448 VAL GLY HIS LEU ASP PHE PHE PRO ASN GLY GLY LYS GLN
SEQRES 19 C 448 MET PRO GLY CYS GLN LYS ASN ILE LEU SER GLN ILE VAL
SEQRES 20 C 448 ASP ILE ASP GLY ILE TRP GLU GLY THR ARG ASP PHE VAL
SEQRES 21 C 448 ALA CYS ASN HIS LEU ARG SER TYR LYS TYR TYR ALA ASP
SEQRES 22 C 448 SER ILE LEU ASN PRO ASP GLY PHE ALA GLY PHE PRO CYS
SEQRES 23 C 448 ASP SER TYR ASN VAL PHE THR ALA ASN LYS CYS PHE PRO
SEQRES 24 C 448 CYS PRO SER GLU GLY CYS PRO GLN MET GLY HIS TYR ALA
SEQRES 25 C 448 ASP ARG PHE PRO GLY LYS THR ASN GLY VAL SER GLN VAL
SEQRES 26 C 448 PHE TYR LEU ASN THR GLY ASP ALA SER ASN PHE ALA ARG
SEQRES 27 C 448 TRP ARG TYR LYS VAL SER VAL THR LEU SER GLY LYS LYS
SEQRES 28 C 448 VAL THR GLY HIS ILE LEU VAL SER LEU PHE GLY ASN GLU
SEQRES 29 C 448 GLY ASN SER ARG GLN TYR GLU ILE TYR LYS GLY THR LEU
SEQRES 30 C 448 GLN PRO ASP ASN THR HIS SER ASP GLU PHE ASP SER ASP
SEQRES 31 C 448 VAL GLU VAL GLY ASP LEU GLN LYS VAL LYS PHE ILE TRP
SEQRES 32 C 448 TYR ASN VAL ILE ASN PRO THR LEU PRO ARG VAL GLY ALA
SEQRES 33 C 448 SER LYS ILE THR VAL GLU ARG ASN ASP GLY LYS VAL TYR
SEQRES 34 C 448 ASP PHE CYS SER GLN GLU THR VAL ARG GLU GLU VAL LEU
SEQRES 35 C 448 LEU THR LEU ASN PRO CYS
SEQRES 1 D 95 VAL PRO ASP PRO ARG GLY ILE ILE ILE ASN LEU ASP GLU
SEQRES 2 D 95 GLY GLU LEU CYS LEU ASN SER ALA GLN CYS LYS SER ASN
SEQRES 3 D 95 CYS CYS GLN HIS ASP THR ILE LEU SER LEU SER ARG CYS
SEQRES 4 D 95 ALA LEU LYS ALA ARG GLU ASN SER GLU CYS SER ALA PHE
SEQRES 5 D 95 THR LEU TYR GLY VAL TYR TYR LYS CYS PRO CYS GLU ARG
SEQRES 6 D 95 GLY LEU THR CYS GLU GLY ASP LYS SER LEU VAL GLY SER
SEQRES 7 D 95 ILE THR ASN THR ASN PHE GLY ILE CYS HIS ASN VAL GLY
SEQRES 8 D 95 ARG SER ASP SER
HET CA A 449 1
HET NAG A 450 27
HET NAG A 451 27
HET BMA A 452 20
HET BMA A 453 22
HET BMA A 454 22
HET C8E A 455 55
HET C8E A 456 55
HET BME A 456 4
HET CA C 449 1
HET NAG C 450 27
HET NAG C 451 27
HET BMA C 452 20
HET BMA C 453 22
HET BMA C 454 22
HET C8E C 455 55
HET C8E C 456 55
HET BME C 456 4
HETNAM CA CALCIUM ION
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM BMA BETA-D-MANNOSE
HETNAM C8E (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE
HETNAM BME BETA-MERCAPTOETHANOL
FORMUL 5 CA 2(CA1 2+)
FORMUL 6 NAG 4(C8 H15 N1 O6)
FORMUL 7 BMA 6(C6 H12 O6)
FORMUL 8 C8E 4(C16 H34 O5)
FORMUL 9 BME 2(C2 H6 O1 S1)
FORMUL 10 HOH *357(H2 O1)
HELIX 1 1 PRO A 32 VAL A 35 1 4
HELIX 2 2 ASN A 44 ASN A 46 5 3
HELIX 3 3 SER A 58 ASN A 62 1 5
HELIX 4 4 ASP A 85 VAL A 97 1 13
HELIX 5 5 LYS A 108 ARG A 112 1 5
HELIX 6 6 TYR A 115 SER A 138 1 24
HELIX 7 7 PRO A 144 ASN A 146 5 3
HELIX 8 8 SER A 153 ARG A 164 5 12
HELIX 9 9 PRO A 194 ASP A 196 5 3
HELIX 10 10 PRO A 229 GLY A 231 5 3
HELIX 11 11 ILE A 242 ILE A 246 1 5
HELIX 12 12 ILE A 252 ILE A 275 1 24
HELIX 13 13 ASN A 290 THR A 293 1 4
HELIX 14 14 GLY A 309 ARG A 314 5 6
HELIX 15 15 LEU B 75 ILE B 79 1 5
HELIX 16 16 PRO C 6 LEU C 8 5 3
HELIX 17 17 ASN C 44 ASN C 46 5 3
HELIX 18 18 PRO C 57 THR C 61 1 5
HELIX 19 19 ASP C 85 VAL C 97 5 13
HELIX 20 20 GLY C 110 ARG C 112 5 3
HELIX 21 21 TYR C 115 LEU C 140 1 26
HELIX 22 22 PRO C 144 ASN C 146 5 3
HELIX 23 23 SER C 153 THR C 166 5 14
HELIX 24 24 PRO C 194 ASP C 196 5 3
HELIX 25 25 ILE C 210 ASN C 213 1 4
HELIX 26 26 PRO C 229 GLY C 232 5 4
HELIX 27 27 ILE C 242 ILE C 246 1 5
HELIX 28 28 ILE C 252 ALA C 261 1 10
HELIX 29 29 ASN C 263 LEU C 276 1 14
HELIX 30 30 TYR C 289 ALA C 294 1 6
HELIX 31 31 ALA C 312 ARG C 314 5 3
HELIX 32 32 LEU D 75 ILE D 79 1 5
SHEET 1 A 2 GLU A 2 PHE A 5 0
SHEET 2 A 2 GLY A 9 SER A 12 -1 N PHE A 11 O VAL A 3
SHEET 1 B 6 ARG A 38 THR A 43 0
SHEET 2 B 6 ASN A 101 ASP A 106 -1 N ASP A 106 O ARG A 38
SHEET 3 B 6 THR A 71 ILE A 75 1 N ARG A 72 O ASN A 101
SHEET 4 B 6 VAL A 147 SER A 153 1 N HIS A 148 O THR A 71
SHEET 5 B 6 ILE A 173 PRO A 178 1 N THR A 174 O VAL A 149
SHEET 6 B 6 VAL A 200 ILE A 203 1 N ASP A 201 O ILE A 173
SHEET 1 C 2 LEU A 225 PRO A 229 0
SHEET 2 C 2 GLN A 324 LEU A 328 1 N GLN A 324 O ASP A 226
SHEET 1 D 4 THR A 382 SER A 389 0
SHEET 2 D 4 TRP A 339 LEU A 347 -1 N VAL A 345 O HIS A 383
SHEET 3 D 4 ALA A 416 ARG A 423 -1 N GLU A 422 O LYS A 342
SHEET 4 D 4 VAL A 428 CYS A 432 -1 N PHE A 431 O ILE A 419
SHEET 1 E 4 LEU A 443 LEU A 445 0
SHEET 2 E 4 VAL A 399 TYR A 404 -1 N PHE A 401 O LEU A 443
SHEET 3 E 4 VAL A 352 LEU A 360 -1 N SER A 359 O LYS A 400
SHEET 4 E 4 TYR A 370 LEU A 377 -1 N LEU A 377 O VAL A 352
SHEET 1 F 2 LEU B 67 GLY B 71 0
SHEET 2 F 2 GLY B 85 ASN B 89 -1 N HIS B 88 O THR B 68
SHEET 1 G 2 GLU C 2 PHE C 5 0
SHEET 2 G 2 GLY C 9 SER C 12 -1 N PHE C 11 O VAL C 3
SHEET 1 H 7 GLN C 51 LEU C 53 0
SHEET 2 H 7 THR C 37 LEU C 41 -1 N LEU C 41 O GLN C 51
SHEET 3 H 7 ASN C 101 TRP C 107 -1 N ASP C 106 O ARG C 38
SHEET 4 H 7 THR C 71 ILE C 75 1 N ARG C 72 O ASN C 101
SHEET 5 H 7 VAL C 147 HIS C 152 1 N HIS C 148 O THR C 71
SHEET 6 H 7 ARG C 172 LEU C 176 1 N ARG C 172 O VAL C 149
SHEET 7 H 7 VAL C 200 ILE C 203 1 N ASP C 201 O ILE C 173
SHEET 1 I 2 LEU C 225 PHE C 227 0
SHEET 2 I 2 GLN C 324 PHE C 326 1 N GLN C 324 O ASP C 226
SHEET 1 J 4 THR C 382 SER C 389 0
SHEET 2 J 4 TRP C 339 GLY C 349 -1 N VAL C 345 O HIS C 383
SHEET 3 J 4 VAL C 414 ARG C 423 -1 N GLU C 422 O LYS C 342
SHEET 4 J 4 VAL C 428 CYS C 432 -1 N PHE C 431 O ILE C 419
SHEET 1 K 2 GLU D 48 SER D 50 0
SHEET 2 K 2 PHE D 84 ILE D 86 -1 N GLY D 85 O CYS D 49
SHEET 1 L 2 LEU D 67 CYS D 69 0
SHEET 2 L 2 CYS D 87 ASN D 89 -1 N HIS D 88 O THR D 68
SHEET 1 M 2 HIS C 355 VAL C 358 0
SHEET 2 M 2 TYR C 370 LYS C 374 -1 N TYR C 373 O ILE C 356
SHEET 1 N 2 SER C 359 GLY C 362 0
SHEET 2 N 2 LEU C 396 LYS C 400 -1 N LYS C 400 O SER C 359
SSBOND 1 CYS A 4 CYS A 10
SSBOND 2 CYS A 91 CYS A 102
SSBOND 3 CYS A 238 CYS A 262
SSBOND 4 CYS A 286 CYS A 297
SSBOND 5 CYS A 300 CYS A 305
SSBOND 6 CYS A 432 CYS A 448
SSBOND 7 CYS B 17 CYS B 28
SSBOND 8 CYS B 23 CYS B 39
SSBOND 9 CYS B 27 CYS B 61
SSBOND 10 CYS B 49 CYS B 69
SSBOND 11 CYS B 63 CYS B 87
SSBOND 12 CYS C 4 CYS C 10
SSBOND 13 CYS C 91 CYS C 102
SSBOND 14 CYS C 238 CYS C 262
SSBOND 15 CYS C 286 CYS C 297
SSBOND 16 CYS C 300 CYS C 305
SSBOND 17 CYS C 432 CYS C 448
SSBOND 18 CYS D 17 CYS D 28
SSBOND 19 CYS D 23 CYS D 39
SSBOND 20 CYS D 27 CYS D 61
SSBOND 21 CYS D 49 CYS D 69
SSBOND 22 CYS D 63 CYS D 87
LINK CA CA A 449 O GLU A 188
LINK CA CA A 449 O ARG A 191
LINK CA CA A 449 OD2 ASP A 196
LINK C1 NAG A 450 CG ASN C 167
LINK C1 NAG A 450 ND2 ASN C 167
LINK O4 NAG A 450 C1 NAG A 451
LINK O5 NAG A 450 OD1 ASN C 167
LINK O5 NAG A 450 ND2 ASN C 167
LINK O4 NAG A 451 C1 BMA A 452
LINK O3 BMA A 452 C1 BMA A 454
LINK O6 BMA A 452 C1 BMA A 453
LINK CA CA C 449 O GLU C 188
LINK CA CA C 449 O ARG C 191
LINK C1 NAG C 450 ND2 ASN A 167
LINK O4 NAG C 450 C1 NAG C 451
LINK O4 NAG C 451 C1 BMA C 452
LINK O3 BMA C 452 C1 BMA C 454
LINK O6 BMA C 452 C1 BMA C 453
CISPEP 1 ALA A 15 PRO A 16 0 5.56
CISPEP 2 ILE A 211 PRO A 212 0 -12.40
CISPEP 3 PHE A 298 PRO A 299 0 -15.97
CISPEP 4 ALA C 15 PRO C 16 0 4.55
CISPEP 5 ILE C 211 PRO C 212 0 -12.68
CISPEP 6 PHE C 298 PRO C 299 0 -14.32
CRYST1 289.100 289.100 289.100 90.00 90.00 90.00 F 2 3 96
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 0.003459 0.000000 0.000000 0.00000
SCALE2 0.000000 0.003459 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003459 0.00000 |