HEADER GROWTH FACTOR 03-APR-00 1E0O
TITLE CRYSTAL STRUCTURE OF A TERNARY FGF1-FGFR2-HEPARIN COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FIBROBLAST GROWTH FACTOR 1;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: ACIDIC FIBROBLAST GROWTH FACTOR;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: FIBROBLAST GROWTH FACTOR RECEPTOR 2;
COMPND 8 CHAIN: B, D;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET14A;
SOURCE 8 OTHER_DETAILS: RECOMBINANT;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 15 EXPRESSION_SYSTEM_PLASMID: PET3A;
SOURCE 16 OTHER_DETAILS: RECOMBINANT
KEYWDS GROWTH FACTOR, RECEPTOR TYROSINE KINASE, HEPARIN, TERNARY COMPLEX,
KEYWDS 2 SIGNAL TRANSDUCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR L.PELLEGRINI,D.F.BURKE,F.VON DELFT,B.MULLOY,T.L.BLUNDELL
REVDAT 6 29-JUL-20 1E0O 1 COMPND REMARK HETNAM LINK
REVDAT 6 2 1 SITE ATOM
REVDAT 5 13-DEC-17 1E0O 1 SOURCE AUTHOR JRNL
REVDAT 4 27-APR-11 1E0O 1 VERSN
REVDAT 3 24-FEB-09 1E0O 1 VERSN
REVDAT 2 11-NOV-00 1E0O 1 JRNL
REVDAT 1 23-OCT-00 1E0O 0
JRNL AUTH L.PELLEGRINI,D.F.BURKE,F.VON DELFT,B.MULLOY,T.L.BLUNDELL
JRNL TITL CRYSTAL STRUCTURE OF FIBROBLAST GROWTH FACTOR RECEPTOR
JRNL TITL 2 ECTODOMAIN BOUND TO LIGAND AND HEPARIN
JRNL REF NATURE V. 407 1029 2000
JRNL REFN ISSN 0028-0836
JRNL PMID 11069186
JRNL DOI 10.1038/35039551
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.9
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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.20
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 36348
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) : 0.274
REMARK 3 FREE R VALUE : 0.309
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1804
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 : 5001
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 205
REMARK 3 SOLVENT ATOMS : 41
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 69.10
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) : 0.49
REMARK 3 ESD FROM SIGMAA (A) : 0.67
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) : 0.55
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.64
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.520
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) : 4.360 ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 7.110 ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : 6.150 ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 8.960 ; 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 : RESTRAINTS
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 1E0O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-APR-00.
REMARK 100 THE DEPOSITION ID IS D_1290004815.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUL-99
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ELETTRA
REMARK 200 BEAMLINE : 5.2R
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
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 : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36342
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 24.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.47400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHARP, SHELX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 72.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS WERE GROWN FROM: 1.0M LI2SO4,
REMARK 280 0.1M TRISCL PH=8.5, 10MM NISO4, PH 8.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62
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 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+2/3
REMARK 290 6555 X-Y,X,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 45.90667
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 22.95333
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 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 45.90667
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 22.95333
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 4810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.3 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E
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 PHE A 1
REMARK 465 ASN A 2
REMARK 465 LEU A 3
REMARK 465 PRO A 4
REMARK 465 PRO A 5
REMARK 465 GLY A 6
REMARK 465 ASN A 7
REMARK 465 TYR A 8
REMARK 465 LYS A 9
REMARK 465 SER A 139
REMARK 465 ASP A 140
REMARK 465 SER B 148
REMARK 465 VAL B 294
REMARK 465 GLU B 295
REMARK 465 LYS B 296
REMARK 465 ASN B 297
REMARK 465 GLY B 298
REMARK 465 SER B 299
REMARK 465 LYS B 300
REMARK 465 TYR B 301
REMARK 465 GLY B 302
REMARK 465 PRO B 303
REMARK 465 ASP B 304
REMARK 465 GLY B 305
REMARK 465 LEU B 306
REMARK 465 PRO B 307
REMARK 465 TYR B 308
REMARK 465 PRO B 361
REMARK 465 ALA B 362
REMARK 465 PRO B 363
REMARK 465 GLY B 364
REMARK 465 ARG B 365
REMARK 465 GLU B 366
REMARK 465 PHE C 1
REMARK 465 ASN C 2
REMARK 465 LEU C 3
REMARK 465 PRO C 4
REMARK 465 PRO C 5
REMARK 465 GLY C 6
REMARK 465 ASN C 7
REMARK 465 TYR C 8
REMARK 465 SER C 139
REMARK 465 ASP C 140
REMARK 465 SER D 148
REMARK 465 VAL D 294
REMARK 465 GLU D 295
REMARK 465 LYS D 296
REMARK 465 ASN D 297
REMARK 465 GLY D 298
REMARK 465 SER D 299
REMARK 465 LYS D 300
REMARK 465 TYR D 301
REMARK 465 GLY D 302
REMARK 465 PRO D 303
REMARK 465 ASP D 304
REMARK 465 GLY D 305
REMARK 465 LEU D 306
REMARK 465 PRO D 307
REMARK 465 TYR D 308
REMARK 465 LEU D 309
REMARK 465 PRO D 361
REMARK 465 ALA D 362
REMARK 465 PRO D 363
REMARK 465 GLY D 364
REMARK 465 ARG D 365
REMARK 465 GLU D 366
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 LYS A 10 CG CD CE NZ
REMARK 470 ASP A 28 CG OD1 OD2
REMARK 470 ASP A 36 CG OD1 OD2
REMARK 470 GLN A 40 CG CD OE1 NE2
REMARK 470 GLN A 45 CG CD OE1 NE2
REMARK 470 LYS A 57 CG CD CE NZ
REMARK 470 ASP A 70 CG OD1 OD2
REMARK 470 GLN A 77 CG CD OE1 NE2
REMARK 470 GLU A 81 CG CD OE1 OE2
REMARK 470 GLU A 82 CG CD OE1 OE2
REMARK 470 LYS A 101 CG CD CE NZ
REMARK 470 GLU A 104 CG CD OE1 OE2
REMARK 470 LYS A 105 CG CD CE NZ
REMARK 470 ASN B 149 CG OD1 ND2
REMARK 470 LYS B 196 CG CD CE NZ
REMARK 470 LYS B 199 CG CD CE NZ
REMARK 470 GLN B 212 CG CD OE1 NE2
REMARK 470 LYS B 226 CG CD CE NZ
REMARK 470 LYS B 279 CG CD CE NZ
REMARK 470 LYS B 292 CG CD CE NZ
REMARK 470 HIS B 293 CG ND1 CD2 CE1 NE2
REMARK 470 LYS B 313 CG CD CE NZ
REMARK 470 LYS B 322 CG CD CE NZ
REMARK 470 GLU B 323 CG CD OE1 OE2
REMARK 470 GLU B 325 CG CD OE1 OE2
REMARK 470 ARG B 330 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 335 CG CD OE1 OE2
REMARK 470 LYS C 10 CG CD CE NZ
REMARK 470 GLN C 40 CG CD OE1 NE2
REMARK 470 LYS C 100 CG CD CE NZ
REMARK 470 LYS C 101 CG CD CE NZ
REMARK 470 GLU C 104 CG CD OE1 OE2
REMARK 470 GLU D 160 CG CD OE1 OE2
REMARK 470 LYS D 196 CG CD CE NZ
REMARK 470 LYS D 199 CG CD CE NZ
REMARK 470 GLU D 201 CG CD OE1 OE2
REMARK 470 LYS D 226 CG CD CE NZ
REMARK 470 GLN D 285 CG CD OE1 NE2
REMARK 470 LYS D 292 CG CD CE NZ
REMARK 470 HIS D 293 CG ND1 CD2 CE1 NE2
REMARK 470 LYS D 310 CG CD CE NZ
REMARK 470 LYS D 313 CG CD CE NZ
REMARK 470 LYS D 322 CG CD CE NZ
REMARK 470 ARG D 330 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 335 CG CD OE1 OE2
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 LEU A 14 65.75 -111.71
REMARK 500 ASP A 28 0.27 -69.57
REMARK 500 ASP A 32 -143.49 -124.80
REMARK 500 THR A 34 -166.63 -117.13
REMARK 500 ARG A 35 -6.32 -141.41
REMARK 500 HIS A 41 35.76 -76.42
REMARK 500 GLN A 43 64.85 -60.56
REMARK 500 GLU A 49 -83.25 -77.71
REMARK 500 THR A 59 14.36 -69.98
REMARK 500 GLU A 60 -68.30 -121.43
REMARK 500 ASP A 68 -171.51 -65.38
REMARK 500 GLU A 81 -34.46 -33.10
REMARK 500 GLU A 91 -39.63 -35.79
REMARK 500 ASN A 106 53.27 95.64
REMARK 500 LEU A 111 137.40 -177.73
REMARK 500 LYS A 113 -16.60 -34.59
REMARK 500 CYS A 117 151.40 -44.05
REMARK 500 ARG A 119 117.50 -24.17
REMARK 500 PRO A 136 174.32 -47.03
REMARK 500 ARG B 152 110.74 -176.24
REMARK 500 PRO B 154 135.26 -35.97
REMARK 500 ASN B 158 66.55 -177.71
REMARK 500 ALA B 172 -13.61 94.97
REMARK 500 SER B 220 62.43 37.01
REMARK 500 ALA B 260 156.11 -48.03
REMARK 500 SER B 267 142.41 -174.93
REMARK 500 VAL B 270 126.52 -36.58
REMARK 500 ALA B 284 -158.60 -134.88
REMARK 500 VAL B 317 -89.01 -60.15
REMARK 500 ILE B 329 77.28 -150.58
REMARK 500 VAL B 332 -176.23 -50.56
REMARK 500 ASP B 336 -8.24 -53.82
REMARK 500 PHE B 352 140.77 -171.72
REMARK 500 ASN C 18 -76.70 -33.82
REMARK 500 HIS C 41 27.96 -66.04
REMARK 500 GLU C 49 -95.46 -74.22
REMARK 500 THR C 59 23.93 -72.48
REMARK 500 GLU C 60 -74.46 -129.45
REMARK 500 ASP C 68 -166.28 -67.20
REMARK 500 HIS C 93 25.11 81.53
REMARK 500 ASN C 106 61.57 69.97
REMARK 500 LYS C 113 -13.78 -44.98
REMARK 500 CYS C 117 148.76 -38.89
REMARK 500 ARG C 122 50.19 -103.62
REMARK 500 PRO C 136 156.50 -46.29
REMARK 500 ASN D 150 32.43 -96.01
REMARK 500 PRO D 154 132.79 -32.44
REMARK 500 LYS D 164 99.19 -66.70
REMARK 500 ALA D 172 -24.65 82.08
REMARK 500 ASN D 194 63.98 36.94
REMARK 500
REMARK 500 THIS ENTRY HAS 59 RAMACHANDRAN OUTLIERS.
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 15 0.06 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 IDS E 10
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI A 201 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 93 NE2
REMARK 620 2 HOH A 307 O 108.7
REMARK 620 3 HIS B 254 NE2 85.7 122.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI B 401 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 245 NE2
REMARK 620 2 ASP B 247 OD1 82.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI B 402 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 287 NE2
REMARK 620 2 HOH B 512 O 125.9
REMARK 620 3 HIS D 287 NE2 62.4 154.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI C 203 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 93 NE2
REMARK 620 2 HIS D 254 NE2 81.3
REMARK 620 3 HOH D 507 O 78.1 74.2
REMARK 620 4 HOH D 515 O 107.4 91.9 164.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI D 404 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 245 NE2
REMARK 620 2 ASP D 247 OD1 82.3
REMARK 620 3 HOH D 504 O 79.2 105.6
REMARK 620 N 1 2
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AXM RELATED DB: PDB
REMARK 900 HEPARIN-LINKED BIOLOGICALLY-ACTIVE DIMER OF FIBROBLAST
REMARK 900 RELATED ID: 2AXM RELATED DB: PDB
REMARK 900 HEPARIN-LINKED BIOLOGICALLY-ACTIVE DIMER OF FIBROBLAST
REMARK 900 RELATED ID: 1DJS RELATED DB: PDB
REMARK 900 LIGAND-BINDING PORTION OF FIBROBLAST GROWTH FACTOR RECEPTOR
REMARK 900 RELATED ID: 1CVS RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A DIMERIC FGF2-FGFR1 COMPLEX
DBREF 1E0O A 1 140 UNP P05230 FGF1_HUMAN 16 155
DBREF 1E0O B 148 366 UNP P21802 FGR2_HUMAN 148 366
DBREF 1E0O C 1 140 UNP P05230 FGF1_HUMAN 16 155
DBREF 1E0O D 148 366 UNP P21802 FGR2_HUMAN 148 366
SEQRES 1 A 140 PHE ASN LEU PRO PRO GLY ASN TYR LYS LYS PRO LYS LEU
SEQRES 2 A 140 LEU TYR CYS SER ASN GLY GLY HIS PHE LEU ARG ILE LEU
SEQRES 3 A 140 PRO ASP GLY THR VAL ASP GLY THR ARG ASP ARG SER ASP
SEQRES 4 A 140 GLN HIS ILE GLN LEU GLN LEU SER ALA GLU SER VAL GLY
SEQRES 5 A 140 GLU VAL TYR ILE LYS SER THR GLU THR GLY GLN TYR LEU
SEQRES 6 A 140 ALA MET ASP THR ASP GLY LEU LEU TYR GLY SER GLN THR
SEQRES 7 A 140 PRO ASN GLU GLU CYS LEU PHE LEU GLU ARG LEU GLU GLU
SEQRES 8 A 140 ASN HIS TYR ASN THR TYR ILE SER LYS LYS HIS ALA GLU
SEQRES 9 A 140 LYS ASN TRP PHE VAL GLY LEU LYS LYS ASN GLY SER CYS
SEQRES 10 A 140 LYS ARG GLY PRO ARG THR HIS TYR GLY GLN LYS ALA ILE
SEQRES 11 A 140 LEU PHE LEU PRO LEU PRO VAL SER SER ASP
SEQRES 1 B 219 SER ASN ASN LYS ARG ALA PRO TYR TRP THR ASN THR GLU
SEQRES 2 B 219 LYS MET GLU LYS ARG LEU HIS ALA VAL PRO ALA ALA ASN
SEQRES 3 B 219 THR VAL LYS PHE ARG CYS PRO ALA GLY GLY ASN PRO MET
SEQRES 4 B 219 PRO THR MET ARG TRP LEU LYS ASN GLY LYS GLU PHE LYS
SEQRES 5 B 219 GLN GLU HIS ARG ILE GLY GLY TYR LYS VAL ARG ASN GLN
SEQRES 6 B 219 HIS TRP SER LEU ILE MET GLU SER VAL VAL PRO SER ASP
SEQRES 7 B 219 LYS GLY ASN TYR THR CYS VAL VAL GLU ASN GLU TYR GLY
SEQRES 8 B 219 SER ILE ASN HIS THR TYR HIS LEU ASP VAL VAL GLU ARG
SEQRES 9 B 219 SER PRO HIS ARG PRO ILE LEU GLN ALA GLY LEU PRO ALA
SEQRES 10 B 219 ASN ALA SER THR VAL VAL GLY GLY ASP VAL GLU PHE VAL
SEQRES 11 B 219 CYS LYS VAL TYR SER ASP ALA GLN PRO HIS ILE GLN TRP
SEQRES 12 B 219 ILE LYS HIS VAL GLU LYS ASN GLY SER LYS TYR GLY PRO
SEQRES 13 B 219 ASP GLY LEU PRO TYR LEU LYS VAL LEU LYS ALA ALA GLY
SEQRES 14 B 219 VAL ASN THR THR ASP LYS GLU ILE GLU VAL LEU TYR ILE
SEQRES 15 B 219 ARG ASN VAL THR PHE GLU ASP ALA GLY GLU TYR THR CYS
SEQRES 16 B 219 LEU ALA GLY ASN SER ILE GLY ILE SER PHE HIS SER ALA
SEQRES 17 B 219 TRP LEU THR VAL LEU PRO ALA PRO GLY ARG GLU
SEQRES 1 C 140 PHE ASN LEU PRO PRO GLY ASN TYR LYS LYS PRO LYS LEU
SEQRES 2 C 140 LEU TYR CYS SER ASN GLY GLY HIS PHE LEU ARG ILE LEU
SEQRES 3 C 140 PRO ASP GLY THR VAL ASP GLY THR ARG ASP ARG SER ASP
SEQRES 4 C 140 GLN HIS ILE GLN LEU GLN LEU SER ALA GLU SER VAL GLY
SEQRES 5 C 140 GLU VAL TYR ILE LYS SER THR GLU THR GLY GLN TYR LEU
SEQRES 6 C 140 ALA MET ASP THR ASP GLY LEU LEU TYR GLY SER GLN THR
SEQRES 7 C 140 PRO ASN GLU GLU CYS LEU PHE LEU GLU ARG LEU GLU GLU
SEQRES 8 C 140 ASN HIS TYR ASN THR TYR ILE SER LYS LYS HIS ALA GLU
SEQRES 9 C 140 LYS ASN TRP PHE VAL GLY LEU LYS LYS ASN GLY SER CYS
SEQRES 10 C 140 LYS ARG GLY PRO ARG THR HIS TYR GLY GLN LYS ALA ILE
SEQRES 11 C 140 LEU PHE LEU PRO LEU PRO VAL SER SER ASP
SEQRES 1 D 219 SER ASN ASN LYS ARG ALA PRO TYR TRP THR ASN THR GLU
SEQRES 2 D 219 LYS MET GLU LYS ARG LEU HIS ALA VAL PRO ALA ALA ASN
SEQRES 3 D 219 THR VAL LYS PHE ARG CYS PRO ALA GLY GLY ASN PRO MET
SEQRES 4 D 219 PRO THR MET ARG TRP LEU LYS ASN GLY LYS GLU PHE LYS
SEQRES 5 D 219 GLN GLU HIS ARG ILE GLY GLY TYR LYS VAL ARG ASN GLN
SEQRES 6 D 219 HIS TRP SER LEU ILE MET GLU SER VAL VAL PRO SER ASP
SEQRES 7 D 219 LYS GLY ASN TYR THR CYS VAL VAL GLU ASN GLU TYR GLY
SEQRES 8 D 219 SER ILE ASN HIS THR TYR HIS LEU ASP VAL VAL GLU ARG
SEQRES 9 D 219 SER PRO HIS ARG PRO ILE LEU GLN ALA GLY LEU PRO ALA
SEQRES 10 D 219 ASN ALA SER THR VAL VAL GLY GLY ASP VAL GLU PHE VAL
SEQRES 11 D 219 CYS LYS VAL TYR SER ASP ALA GLN PRO HIS ILE GLN TRP
SEQRES 12 D 219 ILE LYS HIS VAL GLU LYS ASN GLY SER LYS TYR GLY PRO
SEQRES 13 D 219 ASP GLY LEU PRO TYR LEU LYS VAL LEU LYS ALA ALA GLY
SEQRES 14 D 219 VAL ASN THR THR ASP LYS GLU ILE GLU VAL LEU TYR ILE
SEQRES 15 D 219 ARG ASN VAL THR PHE GLU ASP ALA GLY GLU TYR THR CYS
SEQRES 16 D 219 LEU ALA GLY ASN SER ILE GLY ILE SER PHE HIS SER ALA
SEQRES 17 D 219 TRP LEU THR VAL LEU PRO ALA PRO GLY ARG GLU
HET SGN E 1 20
HET IDS E 2 16
HET SGN E 3 19
HET IDS E 4 16
HET SGN E 5 19
HET IDS E 6 16
HET SGN E 7 19
HET IDS E 8 16
HET SGN E 9 19
HET IDS E 10 15
HET NI A 201 1
HET NI B 401 1
HET NI B 402 1
HET SO4 C 201 5
HET SO4 C 202 5
HET NI C 203 1
HET SO4 D 401 5
HET SO4 D 402 5
HET SO4 D 403 5
HET NI D 404 1
HETNAM SGN 2-DEOXY-6-O-SULFO-2-(SULFOAMINO)-ALPHA-D-GLUCOPYRANOSE
HETNAM IDS 2-O-SULFO-ALPHA-L-IDOPYRANURONIC ACID
HETNAM NI NICKEL (II) ION
HETNAM SO4 SULFATE ION
HETSYN IDS O2-SULFO-GLUCURONIC ACID
FORMUL 5 SGN 5(C6 H13 N O11 S2)
FORMUL 5 IDS 5(C6 H10 O10 S)
FORMUL 6 NI 5(NI 2+)
FORMUL 9 SO4 5(O4 S 2-)
FORMUL 16 HOH *41(H2 O)
HELIX 1 AA1 ASN A 80 CYS A 83 5 4
HELIX 2 AA2 ASN B 158 GLU B 163 5 6
HELIX 3 AA3 LYS B 199 ARG B 203 5 5
HELIX 4 AA4 ASN B 211 HIS B 213 5 3
HELIX 5 AA5 VAL B 222 LYS B 226 5 5
HELIX 6 AA6 THR B 320 GLU B 325 1 6
HELIX 7 AA7 ASN C 80 CYS C 83 5 4
HELIX 8 AA8 HIS C 102 ASN C 106 5 5
HELIX 9 AA9 ARG C 119 THR C 123 5 5
HELIX 10 AB1 LYS D 199 ARG D 203 5 5
HELIX 11 AB2 VAL D 222 LYS D 226 5 5
HELIX 12 AB3 THR D 320 GLU D 325 1 6
SHEET 1 AA1 2 LEU A 13 CYS A 16 0
SHEET 2 AA1 2 PHE A 132 LEU A 135 -1 O LEU A 135 N LEU A 13
SHEET 1 AA2 2 PHE A 22 ILE A 25 0
SHEET 2 AA2 2 VAL A 31 THR A 34 -1 O THR A 34 N PHE A 22
SHEET 1 AA3 4 LEU A 44 ALA A 48 0
SHEET 2 AA3 4 GLU A 53 SER A 58 -1 O TYR A 55 N SER A 47
SHEET 3 AA3 4 PHE A 85 LEU A 89 -1 O PHE A 85 N VAL A 54
SHEET 4 AA3 4 ASN A 95 SER A 99 -1 O THR A 96 N ARG A 88
SHEET 1 AA4 2 TYR A 64 MET A 67 0
SHEET 2 AA4 2 LEU A 73 SER A 76 -1 O TYR A 74 N ALA A 66
SHEET 1 AA5 2 ARG B 152 TRP B 156 0
SHEET 2 AA5 2 ALA B 181 ASN B 184 -1 O GLY B 182 N TYR B 155
SHEET 1 AA6 5 LEU B 166 PRO B 170 0
SHEET 2 AA6 5 GLY B 238 VAL B 249 1 O HIS B 245 N HIS B 167
SHEET 3 AA6 5 GLY B 227 ASN B 235 -1 N TYR B 229 O TYR B 244
SHEET 4 AA6 5 THR B 188 LYS B 193 -1 N LEU B 192 O THR B 230
SHEET 5 AA6 5 LYS B 196 GLU B 197 -1 O LYS B 196 N LYS B 193
SHEET 1 AA7 3 VAL B 175 ARG B 178 0
SHEET 2 AA7 3 SER B 215 MET B 218 -1 O MET B 218 N VAL B 175
SHEET 3 AA7 3 LYS B 208 ARG B 210 -1 N LYS B 208 O ILE B 217
SHEET 1 AA8 2 ILE B 257 LEU B 258 0
SHEET 2 AA8 2 VAL B 280 TYR B 281 -1 O TYR B 281 N ILE B 257
SHEET 1 AA9 5 ALA B 266 VAL B 269 0
SHEET 2 AA9 5 GLY B 349 LEU B 360 1 O TRP B 356 N ALA B 266
SHEET 3 AA9 5 GLY B 338 ASN B 346 -1 N CYS B 342 O HIS B 353
SHEET 4 AA9 5 HIS B 287 LYS B 292 -1 N HIS B 287 O GLY B 345
SHEET 5 AA9 5 LYS B 310 ALA B 314 -1 O LYS B 310 N LYS B 292
SHEET 1 AB1 2 VAL B 274 VAL B 277 0
SHEET 2 AB1 2 VAL B 326 ILE B 329 -1 O LEU B 327 N PHE B 276
SHEET 1 AB2 4 VAL C 31 THR C 34 0
SHEET 2 AB2 4 HIS C 21 ILE C 25 -1 N PHE C 22 O THR C 34
SHEET 3 AB2 4 LEU C 13 CYS C 16 -1 N CYS C 16 O HIS C 21
SHEET 4 AB2 4 PHE C 132 LEU C 135 -1 O LEU C 135 N LEU C 13
SHEET 1 AB3 4 LEU C 44 SER C 47 0
SHEET 2 AB3 4 GLU C 53 SER C 58 -1 O TYR C 55 N SER C 47
SHEET 3 AB3 4 PHE C 85 LEU C 89 -1 O PHE C 85 N VAL C 54
SHEET 4 AB3 4 ASN C 95 SER C 99 -1 O ILE C 98 N LEU C 86
SHEET 1 AB4 2 TYR C 64 MET C 67 0
SHEET 2 AB4 2 LEU C 73 SER C 76 -1 O TYR C 74 N ALA C 66
SHEET 1 AB5 2 LEU C 111 LYS C 112 0
SHEET 2 AB5 2 SER C 116 CYS C 117 -1 O SER C 116 N LYS C 112
SHEET 1 AB6 2 ARG D 152 TRP D 156 0
SHEET 2 AB6 2 ALA D 181 ASN D 184 -1 O GLY D 182 N TYR D 155
SHEET 1 AB7 5 LEU D 166 PRO D 170 0
SHEET 2 AB7 5 GLY D 238 VAL D 249 1 O HIS D 245 N HIS D 167
SHEET 3 AB7 5 GLY D 227 ASN D 235 -1 N TYR D 229 O TYR D 244
SHEET 4 AB7 5 THR D 188 LYS D 193 -1 N LEU D 192 O THR D 230
SHEET 5 AB7 5 LYS D 196 GLU D 197 -1 O LYS D 196 N LYS D 193
SHEET 1 AB8 3 VAL D 175 ARG D 178 0
SHEET 2 AB8 3 SER D 215 MET D 218 -1 O MET D 218 N VAL D 175
SHEET 3 AB8 3 LYS D 208 ARG D 210 -1 N LYS D 208 O ILE D 217
SHEET 1 AB9 2 ILE D 257 LEU D 258 0
SHEET 2 AB9 2 VAL D 280 TYR D 281 -1 O TYR D 281 N ILE D 257
SHEET 1 AC1 5 ALA D 266 VAL D 269 0
SHEET 2 AC1 5 GLY D 349 LEU D 360 1 O LEU D 360 N THR D 268
SHEET 3 AC1 5 GLY D 338 ASN D 346 -1 N ASN D 346 O GLY D 349
SHEET 4 AC1 5 HIS D 287 LYS D 292 -1 N GLN D 289 O LEU D 343
SHEET 5 AC1 5 VAL D 311 ALA D 314 -1 O LYS D 313 N TRP D 290
SHEET 1 AC2 2 VAL D 274 VAL D 277 0
SHEET 2 AC2 2 VAL D 326 ILE D 329 -1 O LEU D 327 N PHE D 276
SSBOND 1 CYS B 179 CYS B 231 1555 1555 2.04
SSBOND 2 CYS B 278 CYS B 342 1555 1555 2.02
SSBOND 3 CYS D 179 CYS D 231 1555 1555 2.05
SSBOND 4 CYS D 278 CYS D 342 1555 1555 2.03
LINK O4 SGN E 1 C1 IDS E 2 1555 1555 1.43
LINK O4 IDS E 2 C1 SGN E 3 1555 1555 1.44
LINK O4 SGN E 3 C1 IDS E 4 1555 1555 1.44
LINK O4 IDS E 4 C1 SGN E 5 1555 1555 1.42
LINK O4 SGN E 5 C1 IDS E 6 1555 1555 1.38
LINK O4 IDS E 6 C1 SGN E 7 1555 1555 1.37
LINK O4 SGN E 7 C1 IDS E 8 1555 1555 1.38
LINK O4 IDS E 8 C1 SGN E 9 1555 1555 1.42
LINK O4 SGN E 9 C1 IDS E 10 1555 1555 1.40
LINK NE2 HIS A 93 NI NI A 201 1555 1555 2.14
LINK NI NI A 201 O HOH A 307 1555 1555 1.96
LINK NI NI A 201 NE2 HIS B 254 1555 1555 2.41
LINK NE2 HIS B 245 NI NI B 401 1555 1555 2.40
LINK OD1 ASP B 247 NI NI B 401 1555 1555 2.38
LINK NE2 HIS B 287 NI NI B 402 1555 1555 2.06
LINK NI NI B 402 O HOH B 512 1555 1555 1.95
LINK NI NI B 402 NE2 HIS D 287 5564 1555 2.11
LINK NE2 HIS C 93 NI NI C 203 1555 1555 2.37
LINK NI NI C 203 NE2 HIS D 254 1555 1555 2.35
LINK NI NI C 203 O HOH D 507 1555 1555 2.22
LINK NI NI C 203 O HOH D 515 1555 1555 2.07
LINK NE2 HIS D 245 NI NI D 404 1555 1555 2.38
LINK OD1 ASP D 247 NI NI D 404 1555 1555 2.14
LINK NI NI D 404 O HOH D 504 1555 1555 2.11
CISPEP 1 ASN B 184 PRO B 185 0 1.68
CISPEP 2 SER B 252 PRO B 253 0 3.69
CISPEP 3 LEU B 262 PRO B 263 0 0.18
CISPEP 4 ASN D 184 PRO D 185 0 -0.08
CISPEP 5 SER D 252 PRO D 253 0 0.83
CISPEP 6 LEU D 262 PRO D 263 0 0.22
CRYST1 195.900 195.900 68.860 90.00 90.00 120.00 P 62 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 0.005105 0.002947 0.000000 0.00000
SCALE2 0.000000 0.005894 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014522 0.00000
MTRIX1 1 0.610700 0.789217 -0.064666 -92.51000 1
MTRIX2 1 0.774890 -0.612432 -0.156434 182.22301 1
MTRIX3 1 -0.163064 0.045426 -0.985569 33.63400 1
MTRIX1 2 0.565035 0.824776 0.021913 -93.16200 1
MTRIX2 2 0.799169 -0.540504 -0.263028 173.12801 1
MTRIX3 2 -0.205095 0.166132 -0.964539 41.46000 1
MTRIX1 3 0.704223 0.669179 -0.237213 -69.99780 1
MTRIX2 3 0.551295 -0.725933 -0.411212 197.39650 1
MTRIX3 3 -0.447375 0.158811 -0.880133 66.43880 1
(ATOM LINES ARE NOT SHOWN.)
END