HEADER CALCIUM-BINDING PROTEIN 17-JUN-99 1QIV TITLE CALMODULIN COMPLEXED WITH N-(3,3,-DIPHENYLPROPYL)-N'-[1-R-( TITLE 2 3,4-BIS-BUTOXYPHENYL)-ETHYL]-PROPYLENEDIAMINE (DPD), 1:2 TITLE 3 COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: CALMODULIN; COMPND 3 CHAIN: A SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 3 ORGANISM_COMMON: BOVINE; SOURCE 4 ORGAN: BRAIN; SOURCE 5 CELLULAR_LOCATION: CYTOPLASM KEYWDS CALCIUM-BINDING PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR V.HARMAT,Z.S.BOCSKEI,B.G.VERTESSY,G.NARAY-SZABO,J.OVADI REVDAT 1 28-MAR-00 1QIV 0 JRNL AUTH V.HARMAT,Z.S.BOCSKEI,G.NARAY-SZABO,I.BATA, JRNL AUTH 2 A.S.CSUTOR,I.HERMECZ,P.ARANYI,B.SZABO,K.LILIOM, JRNL AUTH 3 B.G.VERTESSY,J.OVADI JRNL TITL A NEW POTENT CALMODULIN ANTAGONIST WITH JRNL TITL 2 ARYLALKYLAMINE STRUCTURE: CRYSTALLOGRAPHIC, JRNL TITL 3 SPECTROSCOPIC AND FUNCTIONAL STUDIES JRNL REF J.MOL.BIOL. V. 297 747 2000 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH B.G.VERTESSY,V.HARMAT,Z.S.BOCSKEI,G.NARAY-SZABO, REMARK 1 AUTH 2 F.OROSZ,J.OVADI REMARK 1 TITL SIMULTANEOUS BINDING OF DRUGS WITH DIFFERENT REMARK 1 TITL 2 CHEMICAL STRUCTURES TO CA 2+ CALMODULIN: REMARK 1 TITL 3 CRYSTALLOGRAPHIC AND SPECTROSCOPIC STUDIES REMARK 1 REF BIOCHEMISTRY V. 37 15300 1998 REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 REMARK 1 REFERENCE 2 REMARK 1 AUTH B.G.VERTESSY,Z.S.BOCSKEI,V.HARMAT,G.NARAY-SZABO, REMARK 1 AUTH 2 J.OVADI REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY DIFFRACTION REMARK 1 TITL 2 ANALYSIS OF CA2+ CALMODULIN-DRUG AND REMARK 1 TITL 3 APOCALMODULIN-DRUG COMPLEXES REMARK 1 REF PROTEINS: STRUCT.,FUNCT., V. 28 131 1997 REMARK 1 REF 2 GENET. REMARK 1 REFN ASTM PSFGEY US ISSN 0887-3585 REMARK 1 REFERENCE 3 REMARK 1 AUTH M.VANDONSELAAR,R.A.HICKIE,J.W.QUAIL,L.T.J.DELBAERE REMARK 1 TITL TRIFLUOPERAZINE-INDUCED CONFORMATIONAL CHANGE IN CA REMARK 1 TITL 2 (2+)-CALMODULIN REMARK 1 REF NAT.STRUCT.BIOL. V. 1 795 1994 REMARK 1 REFN ASTM NSBIEW US ISSN 1072-8368 REMARK 1 REFERENCE 4 REMARK 1 AUTH W.J.COOK,L.J.WALTER,M.R.WALTER REMARK 1 TITL DRUG BINDING BY CALMODULIN: CRYSTAL STRUCTURE OF A REMARK 1 TITL 2 CALMODULIN-TRIFLUOPERAZINE COMPLEX REMARK 1 REF BIOCHEMISTRY V. 33 15259 1994 REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 REMARK 2 REMARK 2 RESOLUTION. 2.64 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.851 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.64 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.58 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1000000 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.001 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.3 REMARK 3 NUMBER OF REFLECTIONS : 4965 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) : 0.207 REMARK 3 FREE R VALUE : 0.301 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.1 REMARK 3 FREE R VALUE TEST SET COUNT : 259 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.010 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 8 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.64 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.76 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.3 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 473 REMARK 3 BIN R VALUE (WORKING SET) : 0.228 REMARK 3 BIN FREE R VALUE : 0.445 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.2 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 30 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.085 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1096 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 80 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 28.4 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.0 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.676 REMARK 3 B22 (A**2) : -0.676 REMARK 3 B33 (A**2) : -2.985 REMARK 3 B12 (A**2) : -1.466 REMARK 3 B13 (A**2) : 0.000 REMARK 3 B23 (A**2) : 0.000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.290 REMARK 3 ESD FROM SIGMAA (A) : 0.246 REMARK 3 LOW RESOLUTION CUTOFF (A) : 2.74 REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.431 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.526 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.006 REMARK 3 BOND ANGLES (DEGREES) : 1.358 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.234 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.566 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : GROUP 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 : PROTEIN_REP.PARAM REMARK 3 PARAMETER FILE 2 : CA.PAR REMARK 3 PARAMETER FILE 3 : AAA.PAR REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO REMARK 3 TOPOLOGY FILE 2 : CA.TOP REMARK 3 TOPOLOGY FILE 3 : AAA.TOP REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: DISORDERED SIDE CHAIN ATOMS OF REMARK 3 RESIDUES ARG 74 - THR 79 AND SER 81 OF THE CENTRAL REGION, REMARK 3 GLU 6, GLU 83, TRIMETHYL-LYSINE 115, GLU 123 AND GLU 127 REMARK 3 ARE NOT SEEN IN THE CRYSTAL STRUCTURE, AS WELL AS THE REMARK 3 N-TERMINAL ALA 1, ASP 2 AND C-TERMINAL ALA 147, LYS 148 REMARK 3 RESIDUES. REMARK 3 TEMPERATURE FACTORS FOR THE ATOMS IN RESIDUES 75 - 81 ARE REMARK 3 UNUSUALLY HIGH, INDICATING FLEXIBILITY IN THIS REGION. REMARK 3 THE C-TERMINAL RESIDUES WERE NOT SEEN IN THE DENSITY MAPS REMARK 4 REMARK 4 1QIV COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 17-JUN-1999. REMARK 100 THE EBI ID CODE IS EBI-2823. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-AUG-1997 REMARK 200 TEMPERATURE (KELVIN) : 93 REMARK 200 PH : 5.0 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 RU200 REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : GRAPHITE REMARK 200 OPTICS : NORMAL FOCUS 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 : 4969 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.63 REMARK 200 RESOLUTION RANGE LOW (A) : 24.58 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 92.7 REMARK 200 DATA REDUNDANCY : 4.3 REMARK 200 R MERGE (I) : 0.058 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.6 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.63 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.72 REMARK 200 COMPLETENESS FOR SHELL (%) : 76.2 REMARK 200 DATA REDUNDANCY IN SHELL : 2.3 REMARK 200 R MERGE FOR SHELL (I) : 0.123 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : 9.0 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: AMORE REMARK 200 STARTING MODEL: PDB ENTRY 1LIN REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 52 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.5 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED BY REMARK 280 HANGING DROP TECHNIQUE AT ROOM TEMPERATURE FROM 50 MM PH=5.0 REMARK 280 SODIUM CACODYLATE/HCL BUFFER, 10 MM MGCL2, 10 MM CACL2, REMARK 280 2MM DPD AND 28% PEG 8000. CRYSTAL GROWTH TOOK 2-3 WEEKS. REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 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+2/3 REMARK 290 3555 Y-X,-X,Z+1/3 REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,1/3-Z REMARK 290 6555 -X,Y-X,2/3-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 -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 115.87600 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 57.93800 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 57.93800 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 115.87600 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOLOGICAL UNIT: MONOMER 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 ALA A 1 REMARK 465 ASP A 2 REMARK 465 ALA A 147 REMARK 465 LYS A 148 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 GLU A 6 CG CD OE1 OE2 REMARK 470 ARG A 74 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 75 CG CD CE NZ REMARK 470 MET A 76 CG SD CE REMARK 470 LYS A 77 CG CD CE NZ REMARK 470 ASP A 78 CG OD1 OD2 REMARK 470 THR A 79 CB OG1 CG2 REMARK 470 SER A 81 OG REMARK 470 GLU A 83 CD OE1 OE2 REMARK 470 LYS A 115 CG CD CE NZ REMARK 470 GLU A 123 CG CD OE1 OE2 REMARK 470 GLU A 127 CD OE1 OE2 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: CA1 REMARK 800 SITE_DESCRIPTION: CALCIUM BINDING SITE REMARK 800 REMARK 800 SITE_IDENTIFIER: CA2 REMARK 800 SITE_DESCRIPTION: CALCIUM BINDING SITE REMARK 800 REMARK 800 SITE_IDENTIFIER: CA3 REMARK 800 SITE_DESCRIPTION: CALCIUM BINDING SITE REMARK 800 REMARK 800 SITE_IDENTIFIER: CA4 REMARK 800 SITE_DESCRIPTION: CALCIUM BINDING SITE REMARK 800 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1LIN RELATED DB: PDB REMARK 900 RELATED ID: 1QIW RELATED DB: PDB REMARK 900 DBREF 1QIV A 1 148 SWS P02593 CALM_HUMAN 1 148 SEQRES 1 A 148 ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS SEQRES 2 A 148 GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR SEQRES 3 A 148 ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU SEQRES 4 A 148 GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE SEQRES 5 A 148 ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE SEQRES 6 A 148 PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP SEQRES 7 A 148 THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG VAL SEQRES 8 A 148 PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA GLU SEQRES 9 A 148 LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR SEQRES 10 A 148 ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP ILE SEQRES 11 A 148 ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL GLN SEQRES 12 A 148 MET MET THR ALA LYS HET CA A 149 1 HET CA A 150 1 HET CA A 151 1 HET CA A 152 1 HET DPD A 153 38 HET DPD A 154 38 HETNAM CA CALCIUM ION HETNAM DPD N-(3,3-DIPHENYLPROPYL)-N'-[1-R-(3,4-BIS-BUTOXYPHENYL)ETHYL]- HETNAM 2 DPD PROPYLENEDIAMINE FORMUL 2 CA 4(CA1 2+) FORMUL 3 DPD 2(C34 H48 N2 O2) HELIX 1 1 THR A 5 ASP A 20 1 16 HELIX 2 2 THR A 28 LEU A 39 1 12 HELIX 3 3 THR A 44 ASP A 56 1 13 HELIX 4 4 PHE A 65 ARG A 74 1 10 HELIX 5 5 SER A 81 ASP A 93 1 13 HELIX 6 6 SER A 101 LEU A 112 1 12 HELIX 7 7 THR A 117 ASP A 129 1 13 HELIX 8 8 ASN A 137 THR A 146 1 10 SHEET 1 A 2 THR A 26 ILE A 27 0 SHEET 2 A 2 ILE A 63 ASP A 64 -1 O ILE A 63 N ILE A 27 LINK CA CA A 149 O THR A 26 LINK CA CA A 149 OD1 ASP A 20 LINK CA CA A 149 OD1 ASP A 22 LINK CA CA A 149 OD1 ASP A 24 LINK CA CA A 149 OE1 GLU A 31 LINK CA CA A 149 OE2 GLU A 31 LINK CA CA A 150 O THR A 62 LINK CA CA A 150 OD1 ASN A 60 LINK CA CA A 150 OD1 ASP A 56 LINK CA CA A 150 OD1 ASP A 58 LINK CA CA A 150 OE1 GLU A 67 LINK CA CA A 150 OE2 GLU A 67 LINK CA CA A 151 O TYR A 99 LINK CA CA A 151 OD1 ASN A 97 LINK CA CA A 151 OD1 ASP A 93 LINK CA CA A 151 OD1 ASP A 95 LINK CA CA A 151 OD2 ASP A 95 LINK CA CA A 151 OE1 GLU A 104 LINK CA CA A 151 OE2 GLU A 104 LINK CA CA A 152 O GLN A 135 LINK CA CA A 152 OD1 ASP A 129 LINK CA CA A 152 OD1 ASP A 131 LINK CA CA A 152 OD1 ASP A 133 LINK CA CA A 152 OE1 GLU A 140 LINK CA CA A 152 OE2 GLU A 140 SITE 1 CA1 5 ASP A 20 ASP A 22 ASP A 24 THR A 26 SITE 2 CA1 5 GLU A 31 SITE 1 CA2 5 ASP A 56 ASP A 58 ASN A 60 THR A 62 SITE 2 CA2 5 GLU A 67 SITE 1 CA3 5 ASP A 93 ASP A 95 ASN A 97 TYR A 99 SITE 2 CA3 5 GLU A 104 SITE 1 CA4 5 ASP A 129 ASP A 131 ASP A 133 GLN A 135 SITE 2 CA4 5 GLU A 140 CRYST1 40.125 40.125 173.814 90.00 90.00 120.00 P 32 2 1 6 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 0.024922 0.014389 0.000000 0.00000 SCALE2 0.000000 0.028777 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005753 0.00000 (ATOM LINES ARE NOT SHOWN.) END