HEADER SIGNALING PROTEIN 28-JUL-17 5OMA
TITLE CH3 CHIMERA OF HUMAN 14-3-3 SIGMA WITH THE STARD1 PEPTIDE INCLUDING
TITLE 2 SER57
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 14-3-3 PROTEIN SIGMA,STEROIDOGENIC ACUTE REGULATORY
COMPND 3 PROTEIN, MITOCHONDRIAL;
COMPND 4 CHAIN: A, B, C, D;
COMPND 5 SYNONYM: EPITHELIAL CELL MARKER PROTEIN 1,STRATIFIN,STAR,START
COMPND 6 DOMAIN-CONTAINING PROTEIN 1,STARD1;
COMPND 7 ENGINEERED: YES;
COMPND 8 OTHER_DETAILS: RESIDUES 75-77 WERE REPLACED BY ALANINES TO REDUCE
COMPND 9 SURFACE ENTROPY AND IMPROVE CRYSTALLIZATION;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: UNDETERMINED PEPTIDE;
COMPND 12 CHAIN: H;
COMPND 13 ENGINEERED: YES;
COMPND 14 OTHER_DETAILS: USED TO MODEL A PIECE OF THE DISORDERED PEPTIDE FUSED
COMPND 15 TO THE 14-3-3 PROTEIN CORE, OF UNDETERMINED SEQUENCE. MOST LIKELY
COMPND 16 CORRESPOND TO A CONTINUATION OF CHAIN D'.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: SFN, HME1, STAR, STARD1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS 14-3-3 PROTEINS, PROTEIN CHIMERA, PHOSPHOPEPTIDE-BINDING, SIGNALING
KEYWDS 2 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR N.N.SLUCHANKO,K.V.TUGAEVA,S.J.GREIVE,A.A.ANTSON
REVDAT 3 17-JAN-24 5OMA 1 REMARK
REVDAT 2 25-DEC-19 5OMA 1 REMARK
REVDAT 1 11-OCT-17 5OMA 0
JRNL AUTH N.N.SLUCHANKO,K.V.TUGAEVA,S.J.GREIVE,A.A.ANTSON
JRNL TITL CHIMERIC 14-3-3 PROTEINS FOR UNRAVELING INTERACTIONS WITH
JRNL TITL 2 INTRINSICALLY DISORDERED PARTNERS.
JRNL REF SCI REP V. 7 12014 2017
JRNL REFN ESSN 2045-2322
JRNL PMID 28931924
JRNL DOI 10.1038/S41598-017-12214-9
REMARK 2
REMARK 2 RESOLUTION. 3.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.3
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 11940
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 + TEST SET) : 0.212
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.960
REMARK 3 FREE R VALUE TEST SET COUNT : 951
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 : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 3.90
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 4.27
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2788
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2672
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2552
REMARK 3 BIN R VALUE (WORKING SET) : 0.2639
REMARK 3 BIN FREE R VALUE : 0.3041
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 8.46
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 236
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7266
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 18
REMARK 3 SOLVENT ATOMS : 1
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 136.6
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 198.7
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 15.96440
REMARK 3 B22 (A**2) : 15.96440
REMARK 3 B33 (A**2) : -31.92890
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) : 0.590
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.751
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.929
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.964
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 7383 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 9939 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2693 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 219 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1050 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 7383 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 952 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 8242 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.11
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.57
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 22.13
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|1 - A|235 }
REMARK 3 ORIGIN FOR THE GROUP (A): -26.0815 -11.7876 -21.6359
REMARK 3 T TENSOR
REMARK 3 T11: -0.1995 T22: 0.0132
REMARK 3 T33: -0.1407 T12: 0.2030
REMARK 3 T13: 0.1140 T23: 0.2310
REMARK 3 L TENSOR
REMARK 3 L11: 9.3315 L22: 4.8791
REMARK 3 L33: 5.0586 L12: -1.5594
REMARK 3 L13: -3.7593 L23: 1.2533
REMARK 3 S TENSOR
REMARK 3 S11: -0.2284 S12: -0.3149 S13: -0.6308
REMARK 3 S21: -0.3241 S22: 0.0128 S23: 0.2008
REMARK 3 S31: 0.4329 S32: 0.5986 S33: 0.2156
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { C|2 - C|231 }
REMARK 3 ORIGIN FOR THE GROUP (A): -25.3873 28.4016 -21.6784
REMARK 3 T TENSOR
REMARK 3 T11: 0.3827 T22: -0.1104
REMARK 3 T33: 0.4593 T12: 0.1152
REMARK 3 T13: 0.3040 T23: -0.0375
REMARK 3 L TENSOR
REMARK 3 L11: 11.1851 L22: 15.2875
REMARK 3 L33: 2.1468 L12: 5.8208
REMARK 3 L13: -1.5959 L23: 0.1159
REMARK 3 S TENSOR
REMARK 3 S11: -0.0123 S12: -0.6557 S13: 0.2733
REMARK 3 S21: 0.3576 S22: 0.2767 S23: -0.5646
REMARK 3 S31: -0.6620 S32: 0.3725 S33: -0.2644
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { B|0 - B|236 }
REMARK 3 ORIGIN FOR THE GROUP (A): -52.2355 -8.2802 5.5157
REMARK 3 T TENSOR
REMARK 3 T11: 0.0876 T22: -0.2798
REMARK 3 T33: 0.1739 T12: 0.0793
REMARK 3 T13: 0.0118 T23: -0.0427
REMARK 3 L TENSOR
REMARK 3 L11: 3.4674 L22: 4.0461
REMARK 3 L33: 3.4637 L12: 0.4314
REMARK 3 L13: 0.4336 L23: -1.8176
REMARK 3 S TENSOR
REMARK 3 S11: 0.2381 S12: 0.1814 S13: 0.1587
REMARK 3 S21: 0.4511 S22: -0.0844 S23: 0.5519
REMARK 3 S31: -0.4584 S32: -0.4811 S33: -0.1538
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: { D|2 - D|231 }
REMARK 3 ORIGIN FOR THE GROUP (A): -53.1374 -45.3796 23.7714
REMARK 3 T TENSOR
REMARK 3 T11: -0.0961 T22: -0.2080
REMARK 3 T33: 0.2918 T12: -0.1686
REMARK 3 T13: -0.2898 T23: 0.2519
REMARK 3 L TENSOR
REMARK 3 L11: 3.5063 L22: 6.8191
REMARK 3 L33: 3.2157 L12: -0.7438
REMARK 3 L13: -0.0433 L23: -1.7075
REMARK 3 S TENSOR
REMARK 3 S11: 0.2996 S12: -0.4516 S13: -0.6503
REMARK 3 S21: 0.4617 S22: -0.0614 S23: 0.5645
REMARK 3 S31: 0.3002 S32: -0.3084 S33: -0.2382
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5OMA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-JUL-17.
REMARK 100 THE DEPOSITION ID IS D_1200006029.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-JUN-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9282
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12047
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.890
REMARK 200 RESOLUTION RANGE LOW (A) : 47.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 12.71
REMARK 200 R MERGE (I) : 0.26500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.8800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.89
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.13
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : 12.66
REMARK 200 R MERGE FOR SHELL (I) : 2.88500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.970
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 5LU1 (MONOMER)
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRISPROPANE PH 6.5, 0.2 M
REMARK 280 AMMONIUM SULFATE, 25% PEG 3350, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
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,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 81.22350
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 61.62550
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 61.62550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 40.61175
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 61.62550
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 61.62550
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 121.83525
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 61.62550
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 61.62550
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 40.61175
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 61.62550
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 61.62550
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 121.83525
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 81.22350
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, H
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: 2490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23270 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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 GLY A -2
REMARK 465 PRO A -1
REMARK 465 HIS A 0
REMARK 465 ALA A 75
REMARK 465 ALA A 76
REMARK 465 ALA A 77
REMARK 465 LEU A 236
REMARK 465 ARG A 237
REMARK 465 ARG A 238
REMARK 465 SER A 239
REMARK 465 SEP A 240
REMARK 465 LEU A 241
REMARK 465 LEU A 242
REMARK 465 GLY A 243
REMARK 465 SER A 244
REMARK 465 ARG A 245
REMARK 465 GLY B -2
REMARK 465 PRO B -1
REMARK 465 ALA B 75
REMARK 465 ALA B 76
REMARK 465 ALA B 77
REMARK 465 SER B 239
REMARK 465 SEP B 240
REMARK 465 LEU B 241
REMARK 465 LEU B 242
REMARK 465 GLY B 243
REMARK 465 SER B 244
REMARK 465 ARG B 245
REMARK 465 GLY C -2
REMARK 465 PRO C -1
REMARK 465 HIS C 0
REMARK 465 MET C 1
REMARK 465 GLY C 73
REMARK 465 SER C 74
REMARK 465 ALA C 75
REMARK 465 GLY C 232
REMARK 465 SER C 233
REMARK 465 GLY C 234
REMARK 465 SEP C 235
REMARK 465 LEU C 236
REMARK 465 ARG C 237
REMARK 465 ARG C 238
REMARK 465 SER C 239
REMARK 465 SEP C 240
REMARK 465 LEU C 241
REMARK 465 LEU C 242
REMARK 465 GLY C 243
REMARK 465 SER C 244
REMARK 465 ARG C 245
REMARK 465 GLY D -2
REMARK 465 PRO D -1
REMARK 465 HIS D 0
REMARK 465 MET D 1
REMARK 465 GLY D 73
REMARK 465 SER D 74
REMARK 465 ALA D 75
REMARK 465 ALA D 76
REMARK 465 ALA D 77
REMARK 465 GLY D 232
REMARK 465 SER D 233
REMARK 465 GLY D 234
REMARK 465 SEP D 235
REMARK 465 LEU D 236
REMARK 465 ARG D 237
REMARK 465 ARG D 238
REMARK 465 SER D 239
REMARK 465 SEP D 240
REMARK 465 LEU D 241
REMARK 465 LEU D 242
REMARK 465 GLY D 243
REMARK 465 SER D 244
REMARK 465 ARG D 245
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 72 CG CD OE1 OE2
REMARK 470 LYS A 214 CD CE NZ
REMARK 470 GLU B 72 CG CD OE1 OE2
REMARK 470 LYS B 214 CD CE NZ
REMARK 470 LYS C 214 CD CE NZ
REMARK 470 GLU D 72 CG CD OE1 OE2
REMARK 470 LYS D 214 CD CE NZ
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 ASN C 70 OE2 GLU C 72 1.84
REMARK 500 O ASN C 70 CD GLU C 72 2.06
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 ARG A 18 78.12 -104.73
REMARK 500 HIS A 106 53.82 -157.51
REMARK 500 SER A 233 -130.72 -82.85
REMARK 500 GLU B 2 131.22 -28.14
REMARK 500 ARG B 3 -35.64 -36.22
REMARK 500 ARG B 18 77.77 -105.62
REMARK 500 HIS B 106 24.74 -153.79
REMARK 500 THR B 136 -40.10 -134.17
REMARK 500 ILE B 183 -63.00 -91.30
REMARK 500 THR B 231 -71.00 -76.19
REMARK 500 ARG C 18 77.65 -105.93
REMARK 500 ALA C 77 -92.14 -78.39
REMARK 500 ASP C 104 -64.17 -101.51
REMARK 500 LEU C 107 -54.30 -149.63
REMARK 500 THR C 136 -33.61 -132.85
REMARK 500 ILE C 183 -63.34 -91.26
REMARK 500 ARG D 18 78.00 -105.79
REMARK 500 LEU D 107 -46.88 -160.08
REMARK 500 THR D 136 -38.09 -133.65
REMARK 500 ILE D 183 -61.99 -91.03
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 301
DBREF 5OMA A 1 231 UNP P31947 1433S_HUMAN 1 231
DBREF 5OMA A 237 245 UNP P49675 STAR_HUMAN 54 62
DBREF 5OMA B 1 231 UNP P31947 1433S_HUMAN 1 231
DBREF 5OMA B 237 245 UNP P49675 STAR_HUMAN 54 62
DBREF 5OMA C 1 231 UNP P31947 1433S_HUMAN 1 231
DBREF 5OMA C 237 245 UNP P49675 STAR_HUMAN 54 62
DBREF 5OMA D 1 231 UNP P31947 1433S_HUMAN 1 231
DBREF 5OMA D 237 245 UNP P49675 STAR_HUMAN 54 62
DBREF 5OMA H 1 4 PDB 5OMA 5OMA 1 4
SEQADV 5OMA GLY A -2 UNP P31947 EXPRESSION TAG
SEQADV 5OMA PRO A -1 UNP P31947 EXPRESSION TAG
SEQADV 5OMA HIS A 0 UNP P31947 EXPRESSION TAG
SEQADV 5OMA ALA A 75 UNP P31947 GLU 75 ENGINEERED MUTATION
SEQADV 5OMA ALA A 76 UNP P31947 GLU 76 ENGINEERED MUTATION
SEQADV 5OMA ALA A 77 UNP P31947 LYS 77 ENGINEERED MUTATION
SEQADV 5OMA GLY A 232 UNP P31947 LINKER
SEQADV 5OMA SER A 233 UNP P31947 LINKER
SEQADV 5OMA GLY A 234 UNP P31947 LINKER
SEQADV 5OMA SEP A 235 UNP P31947 LINKER
SEQADV 5OMA LEU A 236 UNP P31947 LINKER
SEQADV 5OMA GLY B -2 UNP P31947 EXPRESSION TAG
SEQADV 5OMA PRO B -1 UNP P31947 EXPRESSION TAG
SEQADV 5OMA HIS B 0 UNP P31947 EXPRESSION TAG
SEQADV 5OMA ALA B 75 UNP P31947 GLU 75 ENGINEERED MUTATION
SEQADV 5OMA ALA B 76 UNP P31947 GLU 76 ENGINEERED MUTATION
SEQADV 5OMA ALA B 77 UNP P31947 LYS 77 ENGINEERED MUTATION
SEQADV 5OMA GLY B 232 UNP P31947 LINKER
SEQADV 5OMA SER B 233 UNP P31947 LINKER
SEQADV 5OMA GLY B 234 UNP P31947 LINKER
SEQADV 5OMA SEP B 235 UNP P31947 LINKER
SEQADV 5OMA LEU B 236 UNP P31947 LINKER
SEQADV 5OMA GLY C -2 UNP P31947 EXPRESSION TAG
SEQADV 5OMA PRO C -1 UNP P31947 EXPRESSION TAG
SEQADV 5OMA HIS C 0 UNP P31947 EXPRESSION TAG
SEQADV 5OMA ALA C 75 UNP P31947 GLU 75 ENGINEERED MUTATION
SEQADV 5OMA ALA C 76 UNP P31947 GLU 76 ENGINEERED MUTATION
SEQADV 5OMA ALA C 77 UNP P31947 LYS 77 ENGINEERED MUTATION
SEQADV 5OMA GLY C 232 UNP P31947 LINKER
SEQADV 5OMA SER C 233 UNP P31947 LINKER
SEQADV 5OMA GLY C 234 UNP P31947 LINKER
SEQADV 5OMA SEP C 235 UNP P31947 LINKER
SEQADV 5OMA LEU C 236 UNP P31947 LINKER
SEQADV 5OMA GLY D -2 UNP P31947 EXPRESSION TAG
SEQADV 5OMA PRO D -1 UNP P31947 EXPRESSION TAG
SEQADV 5OMA HIS D 0 UNP P31947 EXPRESSION TAG
SEQADV 5OMA ALA D 75 UNP P31947 GLU 75 ENGINEERED MUTATION
SEQADV 5OMA ALA D 76 UNP P31947 GLU 76 ENGINEERED MUTATION
SEQADV 5OMA ALA D 77 UNP P31947 LYS 77 ENGINEERED MUTATION
SEQADV 5OMA GLY D 232 UNP P31947 LINKER
SEQADV 5OMA SER D 233 UNP P31947 LINKER
SEQADV 5OMA GLY D 234 UNP P31947 LINKER
SEQADV 5OMA SEP D 235 UNP P31947 LINKER
SEQADV 5OMA LEU D 236 UNP P31947 LINKER
SEQRES 1 A 248 GLY PRO HIS MET GLU ARG ALA SER LEU ILE GLN LYS ALA
SEQRES 2 A 248 LYS LEU ALA GLU GLN ALA GLU ARG TYR GLU ASP MET ALA
SEQRES 3 A 248 ALA PHE MET LYS GLY ALA VAL GLU LYS GLY GLU GLU LEU
SEQRES 4 A 248 SER CYS GLU GLU ARG ASN LEU LEU SER VAL ALA TYR LYS
SEQRES 5 A 248 ASN VAL VAL GLY GLY GLN ARG ALA ALA TRP ARG VAL LEU
SEQRES 6 A 248 SER SER ILE GLU GLN LYS SER ASN GLU GLU GLY SER ALA
SEQRES 7 A 248 ALA ALA GLY PRO GLU VAL ARG GLU TYR ARG GLU LYS VAL
SEQRES 8 A 248 GLU THR GLU LEU GLN GLY VAL CYS ASP THR VAL LEU GLY
SEQRES 9 A 248 LEU LEU ASP SER HIS LEU ILE LYS GLU ALA GLY ASP ALA
SEQRES 10 A 248 GLU SER ARG VAL PHE TYR LEU LYS MET LYS GLY ASP TYR
SEQRES 11 A 248 TYR ARG TYR LEU ALA GLU VAL ALA THR GLY ASP ASP LYS
SEQRES 12 A 248 LYS ARG ILE ILE ASP SER ALA ARG SER ALA TYR GLN GLU
SEQRES 13 A 248 ALA MET ASP ILE SER LYS LYS GLU MET PRO PRO THR ASN
SEQRES 14 A 248 PRO ILE ARG LEU GLY LEU ALA LEU ASN PHE SER VAL PHE
SEQRES 15 A 248 HIS TYR GLU ILE ALA ASN SER PRO GLU GLU ALA ILE SER
SEQRES 16 A 248 LEU ALA LYS THR THR PHE ASP GLU ALA MET ALA ASP LEU
SEQRES 17 A 248 HIS THR LEU SER GLU ASP SER TYR LYS ASP SER THR LEU
SEQRES 18 A 248 ILE MET GLN LEU LEU ARG ASP ASN LEU THR LEU TRP THR
SEQRES 19 A 248 GLY SER GLY SEP LEU ARG ARG SER SEP LEU LEU GLY SER
SEQRES 20 A 248 ARG
SEQRES 1 B 248 GLY PRO HIS MET GLU ARG ALA SER LEU ILE GLN LYS ALA
SEQRES 2 B 248 LYS LEU ALA GLU GLN ALA GLU ARG TYR GLU ASP MET ALA
SEQRES 3 B 248 ALA PHE MET LYS GLY ALA VAL GLU LYS GLY GLU GLU LEU
SEQRES 4 B 248 SER CYS GLU GLU ARG ASN LEU LEU SER VAL ALA TYR LYS
SEQRES 5 B 248 ASN VAL VAL GLY GLY GLN ARG ALA ALA TRP ARG VAL LEU
SEQRES 6 B 248 SER SER ILE GLU GLN LYS SER ASN GLU GLU GLY SER ALA
SEQRES 7 B 248 ALA ALA GLY PRO GLU VAL ARG GLU TYR ARG GLU LYS VAL
SEQRES 8 B 248 GLU THR GLU LEU GLN GLY VAL CYS ASP THR VAL LEU GLY
SEQRES 9 B 248 LEU LEU ASP SER HIS LEU ILE LYS GLU ALA GLY ASP ALA
SEQRES 10 B 248 GLU SER ARG VAL PHE TYR LEU LYS MET LYS GLY ASP TYR
SEQRES 11 B 248 TYR ARG TYR LEU ALA GLU VAL ALA THR GLY ASP ASP LYS
SEQRES 12 B 248 LYS ARG ILE ILE ASP SER ALA ARG SER ALA TYR GLN GLU
SEQRES 13 B 248 ALA MET ASP ILE SER LYS LYS GLU MET PRO PRO THR ASN
SEQRES 14 B 248 PRO ILE ARG LEU GLY LEU ALA LEU ASN PHE SER VAL PHE
SEQRES 15 B 248 HIS TYR GLU ILE ALA ASN SER PRO GLU GLU ALA ILE SER
SEQRES 16 B 248 LEU ALA LYS THR THR PHE ASP GLU ALA MET ALA ASP LEU
SEQRES 17 B 248 HIS THR LEU SER GLU ASP SER TYR LYS ASP SER THR LEU
SEQRES 18 B 248 ILE MET GLN LEU LEU ARG ASP ASN LEU THR LEU TRP THR
SEQRES 19 B 248 GLY SER GLY SEP LEU ARG ARG SER SEP LEU LEU GLY SER
SEQRES 20 B 248 ARG
SEQRES 1 C 248 GLY PRO HIS MET GLU ARG ALA SER LEU ILE GLN LYS ALA
SEQRES 2 C 248 LYS LEU ALA GLU GLN ALA GLU ARG TYR GLU ASP MET ALA
SEQRES 3 C 248 ALA PHE MET LYS GLY ALA VAL GLU LYS GLY GLU GLU LEU
SEQRES 4 C 248 SER CYS GLU GLU ARG ASN LEU LEU SER VAL ALA TYR LYS
SEQRES 5 C 248 ASN VAL VAL GLY GLY GLN ARG ALA ALA TRP ARG VAL LEU
SEQRES 6 C 248 SER SER ILE GLU GLN LYS SER ASN GLU GLU GLY SER ALA
SEQRES 7 C 248 ALA ALA GLY PRO GLU VAL ARG GLU TYR ARG GLU LYS VAL
SEQRES 8 C 248 GLU THR GLU LEU GLN GLY VAL CYS ASP THR VAL LEU GLY
SEQRES 9 C 248 LEU LEU ASP SER HIS LEU ILE LYS GLU ALA GLY ASP ALA
SEQRES 10 C 248 GLU SER ARG VAL PHE TYR LEU LYS MET LYS GLY ASP TYR
SEQRES 11 C 248 TYR ARG TYR LEU ALA GLU VAL ALA THR GLY ASP ASP LYS
SEQRES 12 C 248 LYS ARG ILE ILE ASP SER ALA ARG SER ALA TYR GLN GLU
SEQRES 13 C 248 ALA MET ASP ILE SER LYS LYS GLU MET PRO PRO THR ASN
SEQRES 14 C 248 PRO ILE ARG LEU GLY LEU ALA LEU ASN PHE SER VAL PHE
SEQRES 15 C 248 HIS TYR GLU ILE ALA ASN SER PRO GLU GLU ALA ILE SER
SEQRES 16 C 248 LEU ALA LYS THR THR PHE ASP GLU ALA MET ALA ASP LEU
SEQRES 17 C 248 HIS THR LEU SER GLU ASP SER TYR LYS ASP SER THR LEU
SEQRES 18 C 248 ILE MET GLN LEU LEU ARG ASP ASN LEU THR LEU TRP THR
SEQRES 19 C 248 GLY SER GLY SEP LEU ARG ARG SER SEP LEU LEU GLY SER
SEQRES 20 C 248 ARG
SEQRES 1 D 248 GLY PRO HIS MET GLU ARG ALA SER LEU ILE GLN LYS ALA
SEQRES 2 D 248 LYS LEU ALA GLU GLN ALA GLU ARG TYR GLU ASP MET ALA
SEQRES 3 D 248 ALA PHE MET LYS GLY ALA VAL GLU LYS GLY GLU GLU LEU
SEQRES 4 D 248 SER CYS GLU GLU ARG ASN LEU LEU SER VAL ALA TYR LYS
SEQRES 5 D 248 ASN VAL VAL GLY GLY GLN ARG ALA ALA TRP ARG VAL LEU
SEQRES 6 D 248 SER SER ILE GLU GLN LYS SER ASN GLU GLU GLY SER ALA
SEQRES 7 D 248 ALA ALA GLY PRO GLU VAL ARG GLU TYR ARG GLU LYS VAL
SEQRES 8 D 248 GLU THR GLU LEU GLN GLY VAL CYS ASP THR VAL LEU GLY
SEQRES 9 D 248 LEU LEU ASP SER HIS LEU ILE LYS GLU ALA GLY ASP ALA
SEQRES 10 D 248 GLU SER ARG VAL PHE TYR LEU LYS MET LYS GLY ASP TYR
SEQRES 11 D 248 TYR ARG TYR LEU ALA GLU VAL ALA THR GLY ASP ASP LYS
SEQRES 12 D 248 LYS ARG ILE ILE ASP SER ALA ARG SER ALA TYR GLN GLU
SEQRES 13 D 248 ALA MET ASP ILE SER LYS LYS GLU MET PRO PRO THR ASN
SEQRES 14 D 248 PRO ILE ARG LEU GLY LEU ALA LEU ASN PHE SER VAL PHE
SEQRES 15 D 248 HIS TYR GLU ILE ALA ASN SER PRO GLU GLU ALA ILE SER
SEQRES 16 D 248 LEU ALA LYS THR THR PHE ASP GLU ALA MET ALA ASP LEU
SEQRES 17 D 248 HIS THR LEU SER GLU ASP SER TYR LYS ASP SER THR LEU
SEQRES 18 D 248 ILE MET GLN LEU LEU ARG ASP ASN LEU THR LEU TRP THR
SEQRES 19 D 248 GLY SER GLY SEP LEU ARG ARG SER SEP LEU LEU GLY SER
SEQRES 20 D 248 ARG
SEQRES 1 H 4 UNK UNK UNK UNK
HET SEP A 235 10
HET SEP B 235 10
HET TRS B 301 8
HET PO4 C 301 5
HET SO4 D 301 5
HETNAM SEP PHOSPHOSERINE
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETNAM PO4 PHOSPHATE ION
HETNAM SO4 SULFATE ION
HETSYN SEP PHOSPHONOSERINE
HETSYN TRS TRIS BUFFER
FORMUL 1 SEP 2(C3 H8 N O6 P)
FORMUL 6 TRS C4 H12 N O3 1+
FORMUL 7 PO4 O4 P 3-
FORMUL 8 SO4 O4 S 2-
FORMUL 9 HOH *(H2 O)
HELIX 1 AA1 MET A 1 ALA A 16 1 16
HELIX 2 AA2 ARG A 18 GLU A 31 1 14
HELIX 3 AA3 SER A 37 ASN A 70 1 34
HELIX 4 AA4 PRO A 79 SER A 105 1 27
HELIX 5 AA5 ASP A 113 ALA A 135 1 23
HELIX 6 AA6 ASP A 138 MET A 162 1 25
HELIX 7 AA7 ASN A 166 ILE A 183 1 18
HELIX 8 AA8 SER A 186 ASP A 204 1 19
HELIX 9 AA9 LEU A 205 LEU A 208 5 4
HELIX 10 AB1 SER A 209 THR A 231 1 23
HELIX 11 AB2 GLU B 2 GLU B 17 1 16
HELIX 12 AB3 ARG B 18 GLU B 31 1 14
HELIX 13 AB4 SER B 37 ASN B 70 1 34
HELIX 14 AB5 PRO B 79 LEU B 107 1 29
HELIX 15 AB6 ASP B 113 ALA B 135 1 23
HELIX 16 AB7 ASP B 138 MET B 162 1 25
HELIX 17 AB8 ASN B 166 ILE B 183 1 18
HELIX 18 AB9 SER B 186 ASP B 204 1 19
HELIX 19 AC1 LEU B 205 LEU B 208 5 4
HELIX 20 AC2 SER B 209 SER B 233 1 25
HELIX 21 AC3 ARG C 3 GLU C 17 1 15
HELIX 22 AC4 ARG C 18 GLU C 31 1 14
HELIX 23 AC5 SER C 37 GLU C 71 1 35
HELIX 24 AC6 PRO C 79 LEU C 103 1 25
HELIX 25 AC7 ASP C 113 ALA C 135 1 23
HELIX 26 AC8 ASP C 138 LYS C 160 1 23
HELIX 27 AC9 ASN C 166 GLU C 182 1 17
HELIX 28 AD1 SER C 186 ASP C 204 1 19
HELIX 29 AD2 LEU C 205 LEU C 208 5 4
HELIX 30 AD3 SER C 209 THR C 231 1 23
HELIX 31 AD4 ARG D 3 GLU D 17 1 15
HELIX 32 AD5 ARG D 18 GLU D 31 1 14
HELIX 33 AD6 SER D 37 ASN D 70 1 34
HELIX 34 AD7 PRO D 79 SER D 105 1 27
HELIX 35 AD8 ASP D 113 ALA D 135 1 23
HELIX 36 AD9 ASP D 138 MET D 162 1 25
HELIX 37 AE1 ASN D 166 ILE D 183 1 18
HELIX 38 AE2 SER D 186 ASP D 204 1 19
HELIX 39 AE3 LEU D 205 LEU D 208 5 4
HELIX 40 AE4 SER D 209 THR D 231 1 23
LINK C GLY A 234 N SEP A 235 1555 1555 1.36
LINK C GLY B 234 N SEP B 235 1555 1555 1.33
LINK C SEP B 235 N LEU B 236 1555 1555 1.36
CISPEP 1 SER A 105 HIS A 106 0 17.71
CISPEP 2 GLU C 71 GLU C 72 0 8.70
CISPEP 3 SER C 105 HIS C 106 0 -2.30
CISPEP 4 SER D 105 HIS D 106 0 -7.25
SITE 1 AC1 4 ASP B 97 LEU B 131 ASP B 139 ILE B 143
SITE 1 AC2 3 ARG C 56 ARG C 129 TYR C 130
SITE 1 AC3 3 ARG D 56 ARG D 129 TYR D 130
CRYST1 123.251 123.251 162.447 90.00 90.00 90.00 P 41 21 2 32
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 0.008114 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008114 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006156 0.00000
(ATOM LINES ARE NOT SHOWN.)
END