HEADER IMMUNE SYSTEM 15-DEC-99 1DN0
TITLE STRUCTURE OF THE FAB FRAGMENT FROM A HUMAN IGM COLD AGGLUTININ
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IGM-KAPPA COLD AGGLUTININ (LIGHT CHAIN);
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: FAB FRAGMENT;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: IGM-KAPPA COLD AGGLUTININ (HEAVY CHAIN);
COMPND 7 CHAIN: B, D;
COMPND 8 FRAGMENT: FAB FRAGMENT
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 7 ORGANISM_COMMON: HUMAN;
SOURCE 8 ORGANISM_TAXID: 9606
KEYWDS FAB, IGM, ANTIBODY, COLD AGGLUTININ, HUMAN, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR A.CAUERHFF,B.BRADEN,J.G.CARVALHO,J.LEONI,I.POLIKARPOV,F.GOLDBAUM
REVDAT 4 31-JAN-18 1DN0 1 REMARK
REVDAT 3 24-FEB-09 1DN0 1 VERSN
REVDAT 2 01-APR-03 1DN0 1 JRNL
REVDAT 1 24-JAN-01 1DN0 0
JRNL AUTH A.CAUERHFF,B.C.BRADEN,J.G.CARVALHO,R.APARICIO,I.POLIKARPOV,
JRNL AUTH 2 J.LEONI,F.A.GOLDBAUM
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF THE FAB FROM A HUMAN IGM COLD
JRNL TITL 2 AGGLUTININ.
JRNL REF J.IMMUNOL. V. 165 6422 2000
JRNL REFN ISSN 0022-1767
JRNL PMID 11086081
REMARK 2
REMARK 2 RESOLUTION. 2.28 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.28
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 100.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 50825
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) : 0.180
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
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 : 6594
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 614
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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) : 0.023
REMARK 3 BOND ANGLES (DEGREES) : 2.410
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1DN0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-DEC-99.
REMARK 100 THE DEPOSITION ID IS D_1000010221.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : LNLS
REMARK 200 BEAMLINE : D03B-MX1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.3
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50825
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.280
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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) : 2.28
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.30
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 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 17%PEG 8,000, 0.1M NA HEPES., PH 7.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 4K, TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 56.92000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 113.84000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 113.84000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 56.92000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3360 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3430 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH D2239 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLU B 135
REMARK 465 ASN B 136
REMARK 465 SER B 137
REMARK 465 PRO B 138
REMARK 465 SER B 139
REMARK 465 ASP B 140
REMARK 465 MET B 199
REMARK 465 ALA B 200
REMARK 465 GLY B 201
REMARK 465 ILE B 226
REMARK 465 ALA B 227
REMARK 465 GLU B 228
REMARK 465 LEU B 229
REMARK 465 PRO B 230
REMARK 465 PRO B 231
REMARK 465 LYS B 232
REMARK 465 GLU D 135
REMARK 465 ASN D 136
REMARK 465 SER D 137
REMARK 465 PRO D 138
REMARK 465 SER D 139
REMARK 465 ASP D 140
REMARK 465 THR D 141
REMARK 465 SER D 142
REMARK 465 ILE D 226
REMARK 465 ALA D 227
REMARK 465 GLU D 228
REMARK 465 LEU D 229
REMARK 465 PRO D 230
REMARK 465 PRO D 231
REMARK 465 LYS D 232
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O GLY C 213 N CYS C 215 2.09
REMARK 500 O LEU D 63 OG SER D 65 2.10
REMARK 500 ND2 ASN C 153 O HOH C 2599 2.15
REMARK 500
REMARK 500 REMARK: NULL
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. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH B 2132 O HOH B 2132 6555 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 46 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 46 NE - CZ - NH2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 LEU A 47 CA - CB - CG ANGL. DEV. = 16.4 DEGREES
REMARK 500 ARG A 62 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG A 109 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG B 66 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG B 66 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 VAL B 71 CB - CA - C ANGL. DEV. = -12.7 DEGREES
REMARK 500 ARG C 46 CG - CD - NE ANGL. DEV. = -15.0 DEGREES
REMARK 500 ARG C 46 NE - CZ - NH1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 ARG C 46 NE - CZ - NH2 ANGL. DEV. = -8.2 DEGREES
REMARK 500 ARG C 62 NE - CZ - NH1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG C 62 NE - CZ - NH2 ANGL. DEV. = -5.1 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 ALA A 52 -37.07 61.12
REMARK 500 ASP A 61 5.72 -66.11
REMARK 500 ARG A 78 88.22 -167.93
REMARK 500 ALA A 185 -73.70 -46.13
REMARK 500 LYS A 189 32.35 -76.16
REMARK 500 SER B 15 -17.20 88.52
REMARK 500 ASP B 31 -31.31 68.49
REMARK 500 SER B 103 -159.09 -141.71
REMARK 500 SER B 133 -179.75 -69.30
REMARK 500 SER B 172 59.38 -51.28
REMARK 500 PRO B 194 109.81 -50.10
REMARK 500 SER B 195 -59.76 -16.83
REMARK 500 LYS B 196 32.47 -69.72
REMARK 500 ASP B 197 76.59 -118.29
REMARK 500 PRO B 224 -136.49 -78.43
REMARK 500 SER C 31 13.73 55.01
REMARK 500 PRO C 41 118.40 -39.00
REMARK 500 ALA C 52 -43.43 70.46
REMARK 500 ARG C 78 60.14 39.42
REMARK 500 ALA C 85 -167.90 -170.29
REMARK 500 ASN C 153 -8.71 75.35
REMARK 500 ARG C 212 139.15 -34.58
REMARK 500 GLU C 214 39.99 -38.14
REMARK 500 SER D 15 -10.58 89.01
REMARK 500 ASP D 31 -34.27 73.20
REMARK 500 SER D 62 -3.34 -59.03
REMARK 500 LEU D 63 -87.71 -137.92
REMARK 500 LYS D 64 -48.37 49.29
REMARK 500 THR D 102 -65.36 -97.79
REMARK 500 SER D 103 171.33 -24.82
REMARK 500 ASN D 166 36.78 -83.94
REMARK 500 ASN D 167 9.46 39.76
REMARK 500 SER D 172 36.36 -165.87
REMARK 500 THR D 173 -169.54 -113.12
REMARK 500 ARG D 174 104.71 174.66
REMARK 500 ALA D 200 51.46 -160.06
REMARK 500 THR D 202 43.76 -92.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR A 33 0.09 SIDE CHAIN
REMARK 500 TYR A 141 0.06 SIDE CHAIN
REMARK 500 TYR C 33 0.09 SIDE CHAIN
REMARK 500 TYR C 141 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1DN0 A 1 215 PIR A23746 A23746 1 215
DBREF 1DN0 B 2 232 PIR B23746 B23746 1 231
DBREF 1DN0 C 1 215 PIR A23746 A23746 1 215
DBREF 1DN0 D 2 232 PIR B23746 B23746 1 231
SEQADV 1DN0 CYS A 23 PIR A23746 GLY 23 CONFLICT
SEQADV 1DN0 CYS A 89 PIR A23746 GLY 89 CONFLICT
SEQADV 1DN0 CYS A 215 PIR A23746 GLY 215 CONFLICT
SEQADV 1DN0 GLU B 1 PIR B23746 CONFLICT
SEQADV 1DN0 ALA B 200 PIR B23746 GLN 199 CONFLICT
SEQADV 1DN0 CYS C 23 PIR A23746 GLY 23 CONFLICT
SEQADV 1DN0 CYS C 89 PIR A23746 GLY 89 CONFLICT
SEQADV 1DN0 CYS C 215 PIR A23746 GLY 215 CONFLICT
SEQADV 1DN0 GLU D 1 PIR B23746 CONFLICT
SEQADV 1DN0 ALA D 200 PIR B23746 GLN 199 CONFLICT
SEQRES 1 A 215 GLU ILE VAL LEU THR GLN SER PRO ALA THR LEU SER LEU
SEQRES 2 A 215 SER PRO GLY GLU ARG ALA THR LEU SER CYS GLY ALA SER
SEQRES 3 A 215 GLN SER VAL SER SER ASN TYR LEU ALA TRP TYR GLN GLN
SEQRES 4 A 215 LYS PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR ASP ALA
SEQRES 5 A 215 SER SER ARG ALA THR GLY ILE PRO ASP ARG PHE SER GLY
SEQRES 6 A 215 SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER ARG
SEQRES 7 A 215 LEU GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN
SEQRES 8 A 215 TYR GLY SER SER PRO LEU THR PHE GLY GLY GLY THR LYS
SEQRES 9 A 215 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE
SEQRES 10 A 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR
SEQRES 11 A 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG
SEQRES 12 A 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN
SEQRES 13 A 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER
SEQRES 14 A 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU
SEQRES 15 A 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS
SEQRES 16 A 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS
SEQRES 17 A 215 SER PHE ASN ARG GLY GLU CYS
SEQRES 1 B 232 GLU VAL GLN LEU GLN GLN TRP GLY ALA GLY LEU LEU LYS
SEQRES 2 B 232 PRO SER GLU THR LEU SER LEU THR CYS ALA VAL TYR GLY
SEQRES 3 B 232 GLY SER PHE SER ASP TYR TYR TRP SER TRP ILE ARG GLN
SEQRES 4 B 232 PRO PRO GLY LYS GLY LEU GLU TRP ILE GLY GLU ILE ASN
SEQRES 5 B 232 HIS SER GLY SER THR ASN TYR ASN PRO SER LEU LYS SER
SEQRES 6 B 232 ARG VAL THR ILE SER VAL ASP THR SER LYS ASN GLN PHE
SEQRES 7 B 232 SER LEU LYS LEU SER SER VAL THR ALA ALA ASP THR ALA
SEQRES 8 B 232 VAL TYR TYR CYS ALA ARG PRO PRO HIS ASP THR SER GLY
SEQRES 9 B 232 HIS TYR TRP ASN TYR TRP GLY GLN GLY THR LEU VAL THR
SEQRES 10 B 232 VAL SER SER GLY SER ALA SER ALA PRO THR LEU PHE PRO
SEQRES 11 B 232 LEU VAL SER CYS GLU ASN SER PRO SER ASP THR SER SER
SEQRES 12 B 232 VAL ALA VAL GLY CYS LEU ALA GLN ASP PHE LEU PRO ASP
SEQRES 13 B 232 SER ILE THR PHE SER TRP LYS TYR LYS ASN ASN SER ASP
SEQRES 14 B 232 ILE SER SER THR ARG GLY PHE PRO SER VAL LEU ARG GLY
SEQRES 15 B 232 GLY LYS TYR ALA ALA THR SER GLN VAL LEU LEU PRO SER
SEQRES 16 B 232 LYS ASP VAL MET ALA GLY THR ASP GLU HIS VAL VAL CYS
SEQRES 17 B 232 LYS VAL GLN HIS PRO ASN GLY ASN LYS GLU LYS ASN VAL
SEQRES 18 B 232 PRO LEU PRO VAL ILE ALA GLU LEU PRO PRO LYS
SEQRES 1 C 215 GLU ILE VAL LEU THR GLN SER PRO ALA THR LEU SER LEU
SEQRES 2 C 215 SER PRO GLY GLU ARG ALA THR LEU SER CYS GLY ALA SER
SEQRES 3 C 215 GLN SER VAL SER SER ASN TYR LEU ALA TRP TYR GLN GLN
SEQRES 4 C 215 LYS PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR ASP ALA
SEQRES 5 C 215 SER SER ARG ALA THR GLY ILE PRO ASP ARG PHE SER GLY
SEQRES 6 C 215 SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER ARG
SEQRES 7 C 215 LEU GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN
SEQRES 8 C 215 TYR GLY SER SER PRO LEU THR PHE GLY GLY GLY THR LYS
SEQRES 9 C 215 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE
SEQRES 10 C 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR
SEQRES 11 C 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG
SEQRES 12 C 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN
SEQRES 13 C 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER
SEQRES 14 C 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU
SEQRES 15 C 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS
SEQRES 16 C 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS
SEQRES 17 C 215 SER PHE ASN ARG GLY GLU CYS
SEQRES 1 D 232 GLU VAL GLN LEU GLN GLN TRP GLY ALA GLY LEU LEU LYS
SEQRES 2 D 232 PRO SER GLU THR LEU SER LEU THR CYS ALA VAL TYR GLY
SEQRES 3 D 232 GLY SER PHE SER ASP TYR TYR TRP SER TRP ILE ARG GLN
SEQRES 4 D 232 PRO PRO GLY LYS GLY LEU GLU TRP ILE GLY GLU ILE ASN
SEQRES 5 D 232 HIS SER GLY SER THR ASN TYR ASN PRO SER LEU LYS SER
SEQRES 6 D 232 ARG VAL THR ILE SER VAL ASP THR SER LYS ASN GLN PHE
SEQRES 7 D 232 SER LEU LYS LEU SER SER VAL THR ALA ALA ASP THR ALA
SEQRES 8 D 232 VAL TYR TYR CYS ALA ARG PRO PRO HIS ASP THR SER GLY
SEQRES 9 D 232 HIS TYR TRP ASN TYR TRP GLY GLN GLY THR LEU VAL THR
SEQRES 10 D 232 VAL SER SER GLY SER ALA SER ALA PRO THR LEU PHE PRO
SEQRES 11 D 232 LEU VAL SER CYS GLU ASN SER PRO SER ASP THR SER SER
SEQRES 12 D 232 VAL ALA VAL GLY CYS LEU ALA GLN ASP PHE LEU PRO ASP
SEQRES 13 D 232 SER ILE THR PHE SER TRP LYS TYR LYS ASN ASN SER ASP
SEQRES 14 D 232 ILE SER SER THR ARG GLY PHE PRO SER VAL LEU ARG GLY
SEQRES 15 D 232 GLY LYS TYR ALA ALA THR SER GLN VAL LEU LEU PRO SER
SEQRES 16 D 232 LYS ASP VAL MET ALA GLY THR ASP GLU HIS VAL VAL CYS
SEQRES 17 D 232 LYS VAL GLN HIS PRO ASN GLY ASN LYS GLU LYS ASN VAL
SEQRES 18 D 232 PRO LEU PRO VAL ILE ALA GLU LEU PRO PRO LYS
FORMUL 5 HOH *614(H2 O)
HELIX 1 1 VAL A 29 ASN A 32 5 4
HELIX 2 2 GLU A 80 PHE A 84 5 5
HELIX 3 3 SER A 122 SER A 128 1 7
HELIX 4 4 LYS A 184 LYS A 189 1 6
HELIX 5 5 THR B 86 THR B 90 5 5
HELIX 6 6 VAL C 29 ASN C 32 5 4
HELIX 7 7 GLU C 80 PHE C 84 5 5
HELIX 8 8 SER C 122 SER C 128 1 7
HELIX 9 9 LYS C 184 LYS C 189 1 6
HELIX 10 10 THR D 86 THR D 90 5 5
HELIX 11 11 PRO D 194 MET D 199 1 6
SHEET 1 A 4 LEU A 4 SER A 7 0
SHEET 2 A 4 ALA A 19 ALA A 25 -1 N SER A 22 O SER A 7
SHEET 3 A 4 ASP A 71 ILE A 76 -1 N PHE A 72 O CYS A 23
SHEET 4 A 4 PHE A 63 SER A 68 -1 O SER A 64 N THR A 75
SHEET 1 B 5 SER A 54 ARG A 55 0
SHEET 2 B 5 ARG A 46 TYR A 50 -1 N TYR A 50 O SER A 54
SHEET 3 B 5 LEU A 34 GLN A 39 -1 O TRP A 36 N LEU A 48
SHEET 4 B 5 VAL A 86 GLN A 91 -1 O VAL A 86 N GLN A 39
SHEET 5 B 5 THR A 98 PHE A 99 -1 O THR A 98 N GLN A 91
SHEET 1 B1 6 SER A 54 ARG A 55 0
SHEET 2 B1 6 ARG A 46 TYR A 50 -1 N TYR A 50 O SER A 54
SHEET 3 B1 6 LEU A 34 GLN A 39 -1 O TRP A 36 N LEU A 48
SHEET 4 B1 6 VAL A 86 GLN A 91 -1 O VAL A 86 N GLN A 39
SHEET 5 B1 6 THR A 103 ILE A 107 -1 N THR A 103 O TYR A 87
SHEET 6 B1 6 THR A 10 LEU A 13 1 O LEU A 11 N GLU A 106
SHEET 1 C 4 SER A 115 PHE A 119 0
SHEET 2 C 4 THR A 130 PHE A 140 -1 O VAL A 134 N PHE A 119
SHEET 3 C 4 TYR A 174 SER A 183 -1 N TYR A 174 O PHE A 140
SHEET 4 C 4 SER A 160 VAL A 164 -1 O GLN A 161 N THR A 179
SHEET 1 D 4 ALA A 154 GLN A 156 0
SHEET 2 D 4 LYS A 146 VAL A 151 -1 O TRP A 149 N GLN A 156
SHEET 3 D 4 VAL A 192 THR A 198 -1 O ALA A 194 N LYS A 150
SHEET 4 D 4 VAL A 206 ASN A 211 -1 O VAL A 206 N VAL A 197
SHEET 1 E 4 GLN B 3 TRP B 7 0
SHEET 2 E 4 LEU B 18 TYR B 25 -1 N THR B 21 O TRP B 7
SHEET 3 E 4 GLN B 77 LEU B 82 -1 O PHE B 78 N CYS B 22
SHEET 4 E 4 VAL B 67 ASP B 72 -1 O THR B 68 N LYS B 81
SHEET 1 F 5 THR B 57 TYR B 59 0
SHEET 2 F 5 GLU B 46 ILE B 51 -1 O GLU B 50 N ASN B 58
SHEET 3 F 5 TRP B 34 GLN B 39 -1 N TRP B 34 O ILE B 51
SHEET 4 F 5 ALA B 91 ARG B 97 -1 N VAL B 92 O GLN B 39
SHEET 5 F 5 TYR B 109 TRP B 110 -1 O TYR B 109 N ARG B 97
SHEET 1 F1 6 THR B 57 TYR B 59 0
SHEET 2 F1 6 GLU B 46 ILE B 51 -1 O GLU B 50 N ASN B 58
SHEET 3 F1 6 TRP B 34 GLN B 39 -1 N TRP B 34 O ILE B 51
SHEET 4 F1 6 ALA B 91 ARG B 97 -1 N VAL B 92 O GLN B 39
SHEET 5 F1 6 THR B 114 VAL B 118 -1 O THR B 114 N TYR B 93
SHEET 6 F1 6 LEU B 11 LEU B 12 1 N LEU B 12 O THR B 117
SHEET 1 G 4 THR B 127 VAL B 132 0
SHEET 2 G 4 VAL B 144 PHE B 153 -1 O GLY B 147 N LEU B 131
SHEET 3 G 4 LYS B 184 LEU B 193 -1 N TYR B 185 O PHE B 153
SHEET 4 G 4 THR B 173 GLY B 175 -1 N ARG B 174 O GLN B 190
SHEET 1 G1 4 THR B 127 VAL B 132 0
SHEET 2 G1 4 VAL B 144 PHE B 153 -1 O GLY B 147 N LEU B 131
SHEET 3 G1 4 LYS B 184 LEU B 193 -1 N TYR B 185 O PHE B 153
SHEET 4 G1 4 VAL B 179 ARG B 181 -1 N VAL B 179 O ALA B 186
SHEET 1 H 4 ASP B 169 ILE B 170 0
SHEET 2 H 4 THR B 159 TYR B 164 -1 O TRP B 162 N ILE B 170
SHEET 3 H 4 HIS B 205 GLN B 211 -1 N VAL B 207 O LYS B 163
SHEET 4 H 4 LYS B 217 PRO B 222 -1 O LYS B 217 N VAL B 210
SHEET 1 I 4 LEU C 4 SER C 7 0
SHEET 2 I 4 ALA C 19 ALA C 25 -1 N SER C 22 O SER C 7
SHEET 3 I 4 ASP C 71 ILE C 76 -1 O PHE C 72 N CYS C 23
SHEET 4 I 4 PHE C 63 SER C 68 -1 O SER C 64 N THR C 75
SHEET 1 J 5 SER C 54 ARG C 55 0
SHEET 2 J 5 ARG C 46 TYR C 50 -1 N TYR C 50 O SER C 54
SHEET 3 J 5 LEU C 34 GLN C 39 -1 O TRP C 36 N LEU C 48
SHEET 4 J 5 VAL C 86 GLN C 91 -1 O VAL C 86 N GLN C 39
SHEET 5 J 5 THR C 98 PHE C 99 -1 O THR C 98 N GLN C 91
SHEET 1 J1 6 SER C 54 ARG C 55 0
SHEET 2 J1 6 ARG C 46 TYR C 50 -1 N TYR C 50 O SER C 54
SHEET 3 J1 6 LEU C 34 GLN C 39 -1 O TRP C 36 N LEU C 48
SHEET 4 J1 6 VAL C 86 GLN C 91 -1 O VAL C 86 N GLN C 39
SHEET 5 J1 6 THR C 103 ILE C 107 -1 O THR C 103 N TYR C 87
SHEET 6 J1 6 THR C 10 LEU C 13 1 O LEU C 11 N GLU C 106
SHEET 1 K 4 SER C 115 PHE C 119 0
SHEET 2 K 4 THR C 130 PHE C 140 -1 O VAL C 134 N PHE C 119
SHEET 3 K 4 TYR C 174 SER C 183 -1 N TYR C 174 O PHE C 140
SHEET 4 K 4 SER C 160 VAL C 164 -1 O GLN C 161 N THR C 179
SHEET 1 L 4 ALA C 154 LEU C 155 0
SHEET 2 L 4 LYS C 146 VAL C 151 -1 N VAL C 151 O ALA C 154
SHEET 3 L 4 VAL C 192 THR C 198 -1 N ALA C 194 O LYS C 150
SHEET 4 L 4 VAL C 206 ASN C 211 -1 O VAL C 206 N VAL C 197
SHEET 1 M 4 GLN D 3 TRP D 7 0
SHEET 2 M 4 LEU D 18 TYR D 25 -1 N THR D 21 O TRP D 7
SHEET 3 M 4 GLN D 77 LEU D 82 -1 O PHE D 78 N CYS D 22
SHEET 4 M 4 VAL D 67 ASP D 72 -1 N THR D 68 O LYS D 81
SHEET 1 N 5 THR D 57 TYR D 59 0
SHEET 2 N 5 GLU D 46 ILE D 51 -1 O GLU D 50 N ASN D 58
SHEET 3 N 5 TRP D 34 GLN D 39 -1 N TRP D 34 O ILE D 51
SHEET 4 N 5 ALA D 91 ARG D 97 -1 N VAL D 92 O GLN D 39
SHEET 5 N 5 TYR D 109 TRP D 110 -1 O TYR D 109 N ARG D 97
SHEET 1 N1 6 THR D 57 TYR D 59 0
SHEET 2 N1 6 GLU D 46 ILE D 51 -1 O GLU D 50 N ASN D 58
SHEET 3 N1 6 TRP D 34 GLN D 39 -1 N TRP D 34 O ILE D 51
SHEET 4 N1 6 ALA D 91 ARG D 97 -1 N VAL D 92 O GLN D 39
SHEET 5 N1 6 THR D 114 VAL D 118 -1 N THR D 114 O TYR D 93
SHEET 6 N1 6 LEU D 11 LEU D 12 1 N LEU D 12 O THR D 117
SHEET 1 O 4 THR D 127 VAL D 132 0
SHEET 2 O 4 VAL D 144 PHE D 153 -1 O GLY D 147 N LEU D 131
SHEET 3 O 4 LYS D 184 LEU D 193 -1 N TYR D 185 O PHE D 153
SHEET 4 O 4 VAL D 179 ARG D 181 -1 N VAL D 179 O ALA D 186
SHEET 1 P 4 ASP D 169 ILE D 170 0
SHEET 2 P 4 THR D 159 TYR D 164 -1 O TRP D 162 N ILE D 170
SHEET 3 P 4 HIS D 205 GLN D 211 -1 N VAL D 207 O LYS D 163
SHEET 4 P 4 LYS D 217 PRO D 222 -1 N LYS D 217 O VAL D 210
SSBOND 1 CYS A 23 CYS A 89 1555 1555 2.06
SSBOND 2 CYS A 135 CYS A 195 1555 1555 2.05
SSBOND 3 CYS A 215 CYS B 134 1555 1555 2.94
SSBOND 4 CYS B 22 CYS B 95 1555 1555 2.07
SSBOND 5 CYS B 148 CYS B 208 1555 1555 2.04
SSBOND 6 CYS C 23 CYS C 89 1555 1555 2.09
SSBOND 7 CYS C 135 CYS C 195 1555 1555 2.02
SSBOND 8 CYS C 215 CYS D 134 1555 1555 2.73
SSBOND 9 CYS D 22 CYS D 95 1555 1555 2.05
SSBOND 10 CYS D 148 CYS D 208 1555 1555 2.20
CISPEP 1 SER A 7 PRO A 8 0 -0.95
CISPEP 2 SER A 95 PRO A 96 0 0.22
CISPEP 3 TYR A 141 PRO A 142 0 0.41
CISPEP 4 LEU B 154 PRO B 155 0 -0.22
CISPEP 5 SER C 7 PRO C 8 0 -1.02
CISPEP 6 SER C 95 PRO C 96 0 -0.25
CISPEP 7 TYR C 141 PRO C 142 0 0.43
CISPEP 8 LEU D 154 PRO D 155 0 0.01
CRYST1 110.880 110.880 170.760 90.00 90.00 120.00 P 31 2 1 12
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 0.009019 0.005207 0.000000 0.00000
SCALE2 0.000000 0.010414 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005856 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
