HEADER ALLERGEN 06-OCT-99 1QMR
TITLE BIRCH POLLEN ALLERGEN BET V 1 MUTANT N28T, K32Q, E45S, P108G
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MAJOR POLLEN ALLERGEN BET V 1-A;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: BET V 1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BETULA VERRUCOSA;
SOURCE 3 ORGANISM_COMMON: WHITE BIRCH;
SOURCE 4 ORGANISM_TAXID: 3505;
SOURCE 5 CELL: POLLEN;
SOURCE 6 CELLULAR_LOCATION: CYTOPLASM;
SOURCE 7 GENE: BET V 1 1.2801;
SOURCE 8 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 4922
KEYWDS ALLERGEN, PATHOGENESIS-RELATED PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.HENRIKSEN,J.O.HOLM,M.D.SPANGFORT,M.GAJHEDE
REVDAT 6 13-DEC-23 1QMR 1 REMARK
REVDAT 5 09-OCT-19 1QMR 1 JRNL
REVDAT 4 05-JUL-17 1QMR 1 REMARK
REVDAT 3 24-FEB-09 1QMR 1 VERSN
REVDAT 2 21-OCT-04 1QMR 1 JRNL
REVDAT 1 12-OCT-00 1QMR 0
JRNL AUTH J.HOLM,M.GAJHEDE,M.FERRERAS,A.HENRIKSEN,H.IPSEN,J.N.LARSEN,
JRNL AUTH 2 L.LUND,H.JACOBI,A.MILLNER,P.A.WURTZEN,M.D.SPANGFORT
JRNL TITL ALLERGY VACCINE ENGINEERING: EPITOPE MODULATION OF
JRNL TITL 2 RECOMBINANT BET V 1 REDUCES IGE BINDING BUT RETAINS PROTEIN
JRNL TITL 3 FOLDING PATTERN FOR INDUCTION OF PROTECTIVE
JRNL TITL 4 BLOCKING-ANTIBODY RESPONSES.
JRNL REF J IMMUNOL. V. 173 5258 2004
JRNL REFN ISSN 0022-1767
JRNL PMID 15470071
JRNL DOI 10.4049/JIMMUNOL.173.8.5258
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.GAJHEDE,P.OSMARK,F.M.POULSEN,H.IPSEN,J.N.LARSEN,
REMARK 1 AUTH 2 R.J.J.VAN NEERVEN,C.SCHOU,H.LOWENSTEIN,M.D.SPANGFORT
REMARK 1 TITL X-RAY AND NMR STRUCTURE OF BET V 1, THE ORIGIN OF BIRCH
REMARK 1 TITL 2 POLLEN ALLERGY
REMARK 1 REF NAT.STRUCT.BIOL. V. 3 1040 1996
REMARK 1 REFN ISSN 1072-8368
REMARK 1 PMID 8946858
REMARK 1 DOI 10.1038/NSB1296-1040
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.5
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) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 248643.490
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.2
REMARK 3 NUMBER OF REFLECTIONS : 7797
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 SET) : 0.196
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 407
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.012
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.28
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 78.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 981
REMARK 3 BIN R VALUE (WORKING SET) : 0.2030
REMARK 3 BIN FREE R VALUE : 0.2660
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.40
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 56
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.036
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1223
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 46
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 11.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.47000
REMARK 3 B22 (A**2) : -4.50000
REMARK 3 B33 (A**2) : 4.03000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.23
REMARK 3 ESD FROM SIGMAA (A) : 0.14
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.30
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.23
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.780
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
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 : FLAT MODEL
REMARK 3 KSOL : 0.33
REMARK 3 BSOL : 38.76
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1QMR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-OCT-99.
REMARK 100 THE DEPOSITION ID IS D_1290004195.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-SEP-99
REMARK 200 TEMPERATURE (KELVIN) : 287.0
REMARK 200 PH : 6.00
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 RUH2R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU IMAGE PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 7832
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 37.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 34.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.23
REMARK 200 COMPLETENESS FOR SHELL (%) : 78.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.13500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 9.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS 0.5
REMARK 200 STARTING MODEL: PDB ENTRY 1BV1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.00
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 59.77400
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 59.77400
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 1.000000 0.000000 0.000000 16.17350
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 37.09800
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 16.17350
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 37.09800
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 59.77400
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 16.17350
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 37.09800
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 59.77400
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 16.17350
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 37.09800
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 74.19600
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 400
REMARK 400 COMPOUND
REMARK 400 CHAIN A ENGINEERED MUTATION ASN28THR, LYS32GLN, GLU45SER,
REMARK 400 PRO108GLY
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 ILE A 23 -61.86 -96.39
REMARK 500 ASP A 93 -84.17 43.47
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BTV RELATED DB: PDB
REMARK 900 STRUCTURE OF BET V 1, NMR, 20 STRUCTURES
REMARK 900 RELATED ID: 1BV1 RELATED DB: PDB
REMARK 900 BIRCH POLLEN ALLERGEN BET V 1
REMARK 900 RELATED ID: 1B6F RELATED DB: PDB
REMARK 900 BIRCH POLLEN ALLERGEN BET V 1
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE LEU 62 SWS P15494 PHE 62 CONFLICT IS A KNOWN
REMARK 999 VARIANT FROM THE SWISSPROT SEQUENCE TAKEN FROM
REMARK 999 REFERENCE:
REMARK 999 BREITENEDER H.,PETTENBURGER K.,BITO A.,VALENTA R.,
REMARK 999 KRAFT D.,RUMPOLD H.,SCHEINER O.,BREITENBACH M.
REMARK 999 EMBO J. 8:1935-1938(1989).
DBREF 1QMR A 1 159 UNP P15494 BV1A_BETVE 1 159
SEQADV 1QMR THR A 28 UNP P15494 ASN 28 ENGINEERED MUTATION
SEQADV 1QMR GLN A 32 UNP P15494 LYS 32 ENGINEERED MUTATION
SEQADV 1QMR SER A 45 UNP P15494 GLU 45 ENGINEERED MUTATION
SEQADV 1QMR GLY A 108 UNP P15494 PRO 108 ENGINEERED MUTATION
SEQADV 1QMR LEU A 62 UNP P15494 PHE 62 CONFLICT
SEQRES 1 A 159 GLY VAL PHE ASN TYR GLU THR GLU THR THR SER VAL ILE
SEQRES 2 A 159 PRO ALA ALA ARG LEU PHE LYS ALA PHE ILE LEU ASP GLY
SEQRES 3 A 159 ASP THR LEU PHE PRO GLN VAL ALA PRO GLN ALA ILE SER
SEQRES 4 A 159 SER VAL GLU ASN ILE SER GLY ASN GLY GLY PRO GLY THR
SEQRES 5 A 159 ILE LYS LYS ILE SER PHE PRO GLU GLY LEU PRO PHE LYS
SEQRES 6 A 159 TYR VAL LYS ASP ARG VAL ASP GLU VAL ASP HIS THR ASN
SEQRES 7 A 159 PHE LYS TYR ASN TYR SER VAL ILE GLU GLY GLY PRO ILE
SEQRES 8 A 159 GLY ASP THR LEU GLU LYS ILE SER ASN GLU ILE LYS ILE
SEQRES 9 A 159 VAL ALA THR GLY ASP GLY GLY SER ILE LEU LYS ILE SER
SEQRES 10 A 159 ASN LYS TYR HIS THR LYS GLY ASP HIS GLU VAL LYS ALA
SEQRES 11 A 159 GLU GLN VAL LYS ALA SER LYS GLU MET GLY GLU THR LEU
SEQRES 12 A 159 LEU ARG ALA VAL GLU SER TYR LEU LEU ALA HIS SER ASP
SEQRES 13 A 159 ALA TYR ASN
FORMUL 2 HOH *46(H2 O)
HELIX 1 1 PRO A 14 ILE A 23 1 10
HELIX 2 2 ASP A 25 ALA A 34 1 10
HELIX 3 3 LYS A 129 HIS A 154 1 26
SHEET 1 A 5 VAL A 2 SER A 11 0
SHEET 2 A 5 SER A 112 THR A 122 -1 N TYR A 120 O PHE A 3
SHEET 3 A 5 LEU A 95 ALA A 106 -1 N VAL A 105 O ILE A 113
SHEET 4 A 5 LYS A 80 VAL A 85 -1 N VAL A 85 O ILE A 98
SHEET 5 A 5 GLU A 73 ASP A 75 -1 N ASP A 75 O LYS A 80
SHEET 1 B 4 SER A 40 SER A 45 0
SHEET 2 B 4 ILE A 53 SER A 57 -1 N SER A 57 O SER A 40
SHEET 3 B 4 TYR A 66 VAL A 71 -1 N ASP A 69 O LYS A 54
SHEET 4 B 4 TYR A 83 GLY A 88 -1 N GLU A 87 O LYS A 68
CRYST1 32.347 74.196 119.548 90.00 90.00 90.00 C 2 2 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.030915 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013478 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008365 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
