HEADER TRANSFERASE 29-APR-99 1WWA TITLE NGF BINDING DOMAIN OF HUMAN TRKA RECEPTOR COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN (NERVE GROWTH FACTOR RECEPTOR TRKA); COMPND 3 CHAIN: X, Y; COMPND 4 FRAGMENT: LIGAND BINDING DOMAIN; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI KEYWDS TRK RECEPTOR, RECEPTOR TYROSINE KINASE, 3D-DOMAIN SWAPPING EXPDTA X-RAY DIFFRACTION AUTHOR C.WIESMANN,M.H.ULTSCH,S.H.BASS,A.M.DE VOS REVDAT 2 01-APR-03 1WWA 1 JRNL REVDAT 1 07-JUL-99 1WWA 0 JRNL AUTH M.H.ULTSCH,C.WIESMANN,L.C.SIMMONS,J.HENRICH,M.YANG, JRNL AUTH 2 D.REILLY,S.H.BASS,A.M.DE VOS JRNL TITL CRYSTAL STRUCTURES OF THE NEUROTROPHIN-BINDING JRNL TITL 2 DOMAIN OF TRKA, TRKB AND TRKC. JRNL REF J.MOL.BIOL. V. 290 149 1999 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.50 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) : 2.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.200 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1000000.000 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0010 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 91.4 REMARK 3 NUMBER OF REFLECTIONS : 1404 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 : 0.258 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.300 REMARK 3 FREE R VALUE TEST SET COUNT : 659 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008 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) : 2.50 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.61 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.10 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1465 REMARK 3 BIN R VALUE (WORKING SET) : 0.3770 REMARK 3 BIN FREE R VALUE : 0.4090 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.50 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 67 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.005 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1634 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 66 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) : 12.72000 REMARK 3 B22 (A**2) : 12.72000 REMARK 3 B33 (A**2) : -24.70000 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) : 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) : 0.012 REMARK 3 BOND ANGLES (DEGREES) : 2.20 REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : NULL 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) : 2.225 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.744 ; 2.500 REMARK 3 SIDE-CHAIN BOND (A**2) : 4.123 ; 2.500 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 5.873 ; 3.000 REMARK 3 REMARK 3 NCS MODEL : RESTRAINED 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: NULL REMARK 4 REMARK 4 1WWA COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 4 REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY. REMARK 4 REMEDIATED DATA FILE REVISION 3.100 (2007-03-17) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB . REMARK 100 THE RCSB ID CODE IS RCSB000976. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : APR-1998 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 6.50 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRL REMARK 200 BEAMLINE : BL9-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.98 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : NULL REMARK 200 DETECTOR MANUFACTURER : NULL REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14884 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500 REMARK 200 RESOLUTION RANGE LOW (A) : 25.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 95.4 REMARK 200 DATA REDUNDANCY : 6.500 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.05100 REMARK 200 FOR THE DATA SET : 15.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59 REMARK 200 COMPLETENESS FOR SHELL (%) : 93.0 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.03700 REMARK 200 FOR SHELL : NULL 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: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 72.34 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.45 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.5 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,1/2+Z REMARK 290 3555 1/2-Y,1/2+X,1/4+Z REMARK 290 4555 1/2+Y,1/2-X,3/4+Z REMARK 290 5555 1/2-X,1/2+Y,1/4-Z REMARK 290 6555 1/2+X,1/2-Y,3/4-Z REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,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 37.99000 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 53.21000 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 53.21000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 18.99500 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 53.21000 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 53.21000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 56.98500 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 53.21000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 53.21000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 18.99500 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 53.21000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 53.21000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 56.98500 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 37.99000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). REMARK 350 REMARK 350 GENERATING THE BIOMOLECULE 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 APPLY THE FOLLOWING TO CHAINS: X 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 BIOMOLECULE: 2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: Y 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 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 VAL X 278 REMARK 465 GLN X 279 REMARK 465 VAL X 280 REMARK 465 ASN X 281 REMARK 465 PHE Y 383 REMARK 465 GLU Y 384 REMARK 465 PHE Y 385 REMARK 465 ASN Y 386 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 MET Y 296 SD MET Y 296 CE 0.105 REMARK 500 PRO Y 382 CB PRO Y 382 CG 0.078 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: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 SER X 283 N - CA - C ANGL. DEV. = 14.4 DEGREES REMARK 500 LEU X 346 CA - CB - CG ANGL. DEV. =-11.8 DEGREES REMARK 500 LEU X 346 N - CA - C ANGL. DEV. =-20.8 DEGREES REMARK 500 ILE Y 301 N - CA - C ANGL. DEV. =-11.4 DEGREES REMARK 500 GLU Y 339 N - CA - C ANGL. DEV. =-13.9 DEGREES REMARK 500 LEU Y 346 N - CA - C ANGL. DEV. =-22.7 DEGREES REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1WWB RELATED DB: PDB REMARK 900 TRKB REMARK 900 RELATED ID: 1WWC RELATED DB: PDB REMARK 900 TRKC DBREF 1WWA X 278 386 UNP P04629 NTRK1_HUMAN 278 408 DBREF 1WWA Y 278 386 UNP P04629 NTRK1_HUMAN 278 408 SEQADV 1WWA X UNP P04629 VAL 393 SEE REMARK 999 SEQADV 1WWA X UNP P04629 SER 394 SEE REMARK 999 SEQADV 1WWA X UNP P04629 PHE 395 SEE REMARK 999 SEQADV 1WWA X UNP P04629 SER 396 SEE REMARK 999 SEQADV 1WWA X UNP P04629 PRO 397 SEE REMARK 999 SEQADV 1WWA X UNP P04629 VAL 398 SEE REMARK 999 SEQADV 1WWA Y UNP P04629 VAL 393 SEE REMARK 999 SEQADV 1WWA Y UNP P04629 SER 394 SEE REMARK 999 SEQADV 1WWA Y UNP P04629 PHE 395 SEE REMARK 999 SEQADV 1WWA Y UNP P04629 SER 396 SEE REMARK 999 SEQADV 1WWA Y UNP P04629 PRO 397 SEE REMARK 999 SEQADV 1WWA Y UNP P04629 VAL 398 SEE REMARK 999 SEQRES 1 X 109 VAL GLN VAL ASN VAL SER PHE PRO ALA SER VAL GLN LEU SEQRES 2 X 109 HIS THR ALA VAL GLU MET HIS HIS TRP CYS ILE PRO PHE SEQRES 3 X 109 SER VAL ASP GLY GLN PRO ALA PRO SER LEU ARG TRP LEU SEQRES 4 X 109 PHE ASN GLY SER VAL LEU ASN GLU THR SER PHE ILE PHE SEQRES 5 X 109 THR GLU PHE LEU GLU PRO ALA ALA ASN GLU THR VAL ARG SEQRES 6 X 109 HIS GLY CYS LEU ARG LEU ASN GLN PRO THR HIS VAL ASN SEQRES 7 X 109 ASN GLY ASN TYR THR LEU LEU ALA ALA ASN PRO PHE GLY SEQRES 8 X 109 GLN ALA SER ALA SER ILE MET ALA ALA PHE MET ASP ASN SEQRES 9 X 109 PRO PHE GLU PHE ASN SEQRES 1 Y 109 VAL GLN VAL ASN VAL SER PHE PRO ALA SER VAL GLN LEU SEQRES 2 Y 109 HIS THR ALA VAL GLU MET HIS HIS TRP CYS ILE PRO PHE SEQRES 3 Y 109 SER VAL ASP GLY GLN PRO ALA PRO SER LEU ARG TRP LEU SEQRES 4 Y 109 PHE ASN GLY SER VAL LEU ASN GLU THR SER PHE ILE PHE SEQRES 5 Y 109 THR GLU PHE LEU GLU PRO ALA ALA ASN GLU THR VAL ARG SEQRES 6 Y 109 HIS GLY CYS LEU ARG LEU ASN GLN PRO THR HIS VAL ASN SEQRES 7 Y 109 ASN GLY ASN TYR THR LEU LEU ALA ALA ASN PRO PHE GLY SEQRES 8 Y 109 GLN ALA SER ALA SER ILE MET ALA ALA PHE MET ASP ASN SEQRES 9 Y 109 PRO PHE GLU PHE ASN FORMUL 3 HOH *66(H2 O) HELIX 1 1 HIS X 353 ASN X 355 5 3 HELIX 2 2 HIS Y 353 ASN Y 355 5 3 SHEET 1 A 3 TRP X 299 VAL X 305 0 SHEET 2 A 3 ARG X 342 LEU X 348 -1 N LEU X 348 O TRP X 299 SHEET 3 A 3 ILE X 328 PHE X 332 -1 N GLU X 331 O CYS X 345 SHEET 1 B 3 SER X 312 PHE X 317 0 SHEET 2 B 3 GLY X 357 ASN X 365 -1 N ALA X 364 O SER X 312 SHEET 3 B 3 GLY X 368 ALA X 376 -1 N ALA X 376 O GLY X 357 SHEET 1 C 3 HIS Y 298 VAL Y 305 0 SHEET 2 C 3 ARG Y 342 ASN Y 349 -1 N LEU Y 348 O TRP Y 299 SHEET 3 C 3 ILE Y 328 PHE Y 332 -1 N GLU Y 331 O CYS Y 345 SHEET 1 D 3 SER Y 312 PHE Y 317 0 SHEET 2 D 3 GLY Y 357 ASN Y 365 -1 N ALA Y 364 O SER Y 312 SHEET 3 D 3 GLY Y 368 ALA Y 376 -1 N ALA Y 376 O GLY Y 357 SSBOND 1 CYS X 300 CYS X 345 SSBOND 2 CYS Y 300 CYS Y 345 CISPEP 1 GLN X 308 PRO X 309 0 0.27 CISPEP 2 GLN Y 308 PRO Y 309 0 0.04 CRYST1 106.420 106.420 75.980 90.00 90.00 90.00 P 41 21 2 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 0.009397 0.000000 0.000000 0.00000 SCALE2 0.000000 0.009397 0.000000 0.00000 SCALE3 0.000000 0.000000 0.013161 0.00000 MTRIX1 1 -0.999900 0.004000 0.015800 -17.96480 1 MTRIX2 1 0.011600 -0.514100 0.857700 96.75570 1 MTRIX3 1 0.011500 0.857700 0.514000 -54.58860 1