HEADER TRANSFERASE 29-JUN-14 4QQU
TITLE CRYSTAL STRUCTURE OF THE COBALAMIN-INDEPENDENT METHIONINE SYNTHASE
TITLE 2 ENZYME IN A CLOSED CONFORMATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5-METHYLTETRAHYDROPTEROYLTRIGLUTAMATE--HOMOCYSTEINE
COMPND 3 METHYLTRANSFERASE;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: COBALAMIN-INDEPENDENT METHIONINE SYNTHASE, METHIONINE
COMPND 6 SYNTHASE, VITAMIN-B12 INDEPENDENT ISOZYME;
COMPND 7 EC: 2.1.1.14;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CANDIDA ALBICANS;
SOURCE 3 ORGANISM_COMMON: YEAST;
SOURCE 4 ORGANISM_TAXID: 5476;
SOURCE 5 STRAIN: BWP17;
SOURCE 6 GENE: CAO19.10083, CAO19.2551, MET6;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4
KEYWDS COBALAMIN-INDEPENDENT, SURFACE ENTROPY REDUCTION, FUNGAL, DUAL TIM
KEYWDS 2 BARRELS, METHIONINE SYNTHASE, CLOSED CONFORMATION, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.K.UBHI,J.D.ROBERTUS
REVDAT 5 03-APR-24 4QQU 1 HETSYN
REVDAT 4 06-DEC-23 4QQU 1 REMARK
REVDAT 3 20-SEP-23 4QQU 1 REMARK SEQADV LINK
REVDAT 2 25-FEB-15 4QQU 1 JRNL
REVDAT 1 14-JAN-15 4QQU 0
JRNL AUTH D.K.UBHI,J.D.ROBERTUS
JRNL TITL THE COBALAMIN-INDEPENDENT METHIONINE SYNTHASE ENZYME
JRNL TITL 2 CAPTURED IN A SUBSTRATE-INDUCED CLOSED CONFORMATION.
JRNL REF J.MOL.BIOL. V. 427 901 2015
JRNL REFN ISSN 0022-2836
JRNL PMID 25545590
JRNL DOI 10.1016/J.JMB.2014.12.014
REMARK 2
REMARK 2 RESOLUTION. 2.98 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.98
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 71.71
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 15543
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) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.276
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 828
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.98
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.06
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1119
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.50
REMARK 3 BIN R VALUE (WORKING SET) : 0.2570
REMARK 3 BIN FREE R VALUE SET COUNT : 64
REMARK 3 BIN FREE R VALUE : 0.3610
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5888
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 69
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) : 31.67
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.19000
REMARK 3 B22 (A**2) : 2.53000
REMARK 3 B33 (A**2) : -1.34000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.519
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.405
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 47.155
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.940
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.844
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6082 ; 0.012 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 5660 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8279 ; 1.635 ; 1.972
REMARK 3 BOND ANGLES OTHERS (DEGREES): 13003 ; 0.832 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 764 ; 6.846 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 266 ;36.450 ;24.624
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 967 ;16.551 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 32 ;14.594 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 936 ; 0.079 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6942 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1354 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3064 ; 0.762 ; 1.942
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3064 ; 0.761 ; 1.942
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3825 ; 1.303 ; 2.910
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3821 ; 2.759 ; 4.696
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3018 ; 0.720 ; 2.017
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3000 ; 1.426 ; 3.191
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4430 ; 2.434 ; 4.744
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 7174 ; 4.234 ;24.772
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 7175 ; 4.234 ;24.771
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 379
REMARK 3 ORIGIN FOR THE GROUP (A): 7.9301 -20.2463 -31.1960
REMARK 3 T TENSOR
REMARK 3 T11: 0.1039 T22: 0.0316
REMARK 3 T33: 0.0408 T12: -0.0181
REMARK 3 T13: 0.0020 T23: -0.0335
REMARK 3 L TENSOR
REMARK 3 L11: 1.3510 L22: 0.8514
REMARK 3 L33: 1.1965 L12: -0.1491
REMARK 3 L13: -0.2227 L23: 0.0178
REMARK 3 S TENSOR
REMARK 3 S11: 0.1065 S12: -0.1089 S13: 0.1058
REMARK 3 S21: -0.1044 S22: -0.0133 S23: 0.0610
REMARK 3 S31: -0.0652 S32: 0.0595 S33: -0.0932
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 380 A 767
REMARK 3 ORIGIN FOR THE GROUP (A): 30.2596 -37.3515 -21.3185
REMARK 3 T TENSOR
REMARK 3 T11: 0.0499 T22: 0.2181
REMARK 3 T33: 0.0180 T12: 0.0224
REMARK 3 T13: 0.0021 T23: 0.0492
REMARK 3 L TENSOR
REMARK 3 L11: 1.0541 L22: 0.6083
REMARK 3 L33: 1.0945 L12: -0.0018
REMARK 3 L13: -0.4960 L23: -0.1722
REMARK 3 S TENSOR
REMARK 3 S11: 0.0141 S12: -0.3476 S13: -0.1280
REMARK 3 S21: -0.0361 S22: -0.0851 S23: -0.0374
REMARK 3 S31: -0.0226 S32: 0.4032 S33: 0.0710
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4QQU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JUL-14.
REMARK 100 THE DEPOSITION ID IS D_1000086397.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-FEB-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97648
REMARK 200 MONOCHROMATOR : ASYMMETRIC CUT SINGLE CRYSTAL
REMARK 200 SI(220)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16414
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.980
REMARK 200 RESOLUTION RANGE LOW (A) : 71.710
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.800
REMARK 200 R MERGE (I) : 0.17200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.98
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.60100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> 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: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 4L5Z
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM SODIUM IODIDE, 27% W/V PEG3350,
REMARK 280 0.25 MM BME, 0.15 MM ZINC SULFATE, 2 MM HOMOCYSTEINE, 5 MM 5-
REMARK 280 METHYLTETRAHYDROFOLATE TRIGLUTAMATE, 20 MM TRIS-CL, PH 7.4,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 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 37.48900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 51.95100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.55100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 51.95100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.48900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 49.55100
REMARK 290 SMTRY3 4 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 MET A -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 SER A -14
REMARK 465 SER A -13
REMARK 465 GLY A -12
REMARK 465 VAL A -11
REMARK 465 ASP A -10
REMARK 465 LEU A -9
REMARK 465 GLY A -8
REMARK 465 THR A -7
REMARK 465 GLU A -6
REMARK 465 ASN A -5
REMARK 465 LEU A -4
REMARK 465 TYR A -3
REMARK 465 PHE A -2
REMARK 465 GLN A -1
REMARK 465 SER A 0
REMARK 465 ALA A 107
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 MET A 1 CE
REMARK 470 LYS A 20 CD CE NZ
REMARK 470 LYS A 29 CE NZ
REMARK 470 LYS A 48 CE NZ
REMARK 470 LYS A 85 CE NZ
REMARK 470 THR A 106 OG1 CG2
REMARK 470 THR A 108 OG1 CG2
REMARK 470 GLN A 109 CG CD OE1 NE2
REMARK 470 VAL A 112 CG1 CG2
REMARK 470 LYS A 141 CE NZ
REMARK 470 LYS A 158 CE NZ
REMARK 470 ILE A 168 CD1
REMARK 470 ILE A 190 CD1
REMARK 470 LYS A 206 CE NZ
REMARK 470 GLN A 214 CG CD OE1 NE2
REMARK 470 LYS A 263 CG CD CE NZ
REMARK 470 SER A 289 OG
REMARK 470 ILE A 290 CD1
REMARK 470 LYS A 292 CD CE NZ
REMARK 470 ASP A 293 CG OD1 OD2
REMARK 470 LYS A 321 CE NZ
REMARK 470 LYS A 325 CE NZ
REMARK 470 LYS A 328 CE NZ
REMARK 470 ILE A 356 CD1
REMARK 470 LYS A 375 CG CD CE NZ
REMARK 470 LYS A 384 CE NZ
REMARK 470 LYS A 394 CE NZ
REMARK 470 SER A 400 OG
REMARK 470 ILE A 401 CG1 CG2 CD1
REMARK 470 LYS A 406 CG CD CE NZ
REMARK 470 GLU A 416 CG CD OE1 OE2
REMARK 470 LYS A 422 CG CD CE NZ
REMARK 470 GLU A 427 CG CD OE1 OE2
REMARK 470 LYS A 433 CE NZ
REMARK 470 ASP A 454 OD1 OD2
REMARK 470 ILE A 457 CD1
REMARK 470 LYS A 461 CE NZ
REMARK 470 LYS A 464 CG CD CE NZ
REMARK 470 THR A 468 CG2
REMARK 470 GLU A 473 CG CD OE1 OE2
REMARK 470 LYS A 478 CD CE NZ
REMARK 470 GLU A 489 CD OE1 OE2
REMARK 470 ILE A 490 CD1
REMARK 470 THR A 520 OG1 CG2
REMARK 470 ASN A 521 CG OD1 ND2
REMARK 470 LYS A 550 CE NZ
REMARK 470 LYS A 586 NZ
REMARK 470 ILE A 587 CD1
REMARK 470 LEU A 594 CG CD1 CD2
REMARK 470 ILE A 618 CD1
REMARK 470 VAL A 648 CG1 CG2
REMARK 470 SER A 651 OG
REMARK 470 ILE A 654 CG1 CG2 CD1
REMARK 470 ASN A 666 OD1 ND2
REMARK 470 ILE A 668 CD1
REMARK 470 LEU A 671 CG CD1 CD2
REMARK 470 GLN A 690 CG CD OE1 NE2
REMARK 470 SER A 693 OG
REMARK 470 GLU A 694 CG CD OE1 OE2
REMARK 470 SER A 713 OG
REMARK 470 LYS A 714 NZ
REMARK 470 VAL A 727 CG1 CG2
REMARK 470 LYS A 732 NZ
REMARK 470 GLU A 758 CD OE1 OE2
REMARK 470 LYS A 761 CE NZ
REMARK 470 LYS A 766 CE NZ
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 ASN A 61 -4.57 75.94
REMARK 500 TYR A 66 -55.84 -159.43
REMARK 500 ASN A 77 17.96 84.31
REMARK 500 LYS A 85 38.87 -81.66
REMARK 500 PHE A 123 -124.13 49.60
REMARK 500 SER A 184 49.18 -155.60
REMARK 500 GLU A 228 -39.89 -37.46
REMARK 500 PHE A 255 -7.75 78.92
REMARK 500 ASN A 267 53.51 -144.96
REMARK 500 VAL A 270 170.49 -55.37
REMARK 500 VAL A 344 -70.32 -74.47
REMARK 500 ASP A 353 126.83 -37.47
REMARK 500 THR A 445 -162.13 -126.48
REMARK 500 THR A 520 -68.83 -101.39
REMARK 500 ASN A 521 34.33 -94.77
REMARK 500 ASP A 672 46.88 35.31
REMARK 500 PHE A 680 -39.43 -142.77
REMARK 500 ASP A 684 48.53 -98.07
REMARK 500 ARG A 710 132.63 -39.54
REMARK 500 SER A 731 0.07 -67.45
REMARK 500 CYS A 739 -159.53 -163.97
REMARK 500
REMARK 500 REMARK: NULL
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 ZN A 802 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 657 NE2
REMARK 620 2 CYS A 659 SG 113.8
REMARK 620 3 CYS A 739 SG 101.8 125.8
REMARK 620 4 HCS A 801 SD 108.9 109.6 94.6
REMARK 620 N 1 2 3
REMARK 630
REMARK 630 MOLECULE TYPE: PEPTIDE-LIKE UNKNOWN
REMARK 630 MOLECULE NAME: N-[4-({[(6S)-2-AMINO-4-OXO-3,4,5,6,7,8-
REMARK 630 HEXAHYDROPTERIDIN-6-YL]METHYL}AMINO)BENZOYL]-L-GAMMA-GLUTAMYL-L-
REMARK 630 GAMMA-GLUTAMYL-L-GLUTAMIC ACID
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 630 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 630
REMARK 630 M RES C SSSEQI
REMARK 630 39S A 805
REMARK 630 SOURCE: NULL
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP: 40Q GGL GGL GLU
REMARK 630 DETAILS: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HCS A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 39S A 805
DBREF 4QQU A 1 767 UNP P82610 METE_CANAL 1 767
SEQADV 4QQU MET A -21 UNP P82610 EXPRESSION TAG
SEQADV 4QQU HIS A -20 UNP P82610 EXPRESSION TAG
SEQADV 4QQU HIS A -19 UNP P82610 EXPRESSION TAG
SEQADV 4QQU HIS A -18 UNP P82610 EXPRESSION TAG
SEQADV 4QQU HIS A -17 UNP P82610 EXPRESSION TAG
SEQADV 4QQU HIS A -16 UNP P82610 EXPRESSION TAG
SEQADV 4QQU HIS A -15 UNP P82610 EXPRESSION TAG
SEQADV 4QQU SER A -14 UNP P82610 EXPRESSION TAG
SEQADV 4QQU SER A -13 UNP P82610 EXPRESSION TAG
SEQADV 4QQU GLY A -12 UNP P82610 EXPRESSION TAG
SEQADV 4QQU VAL A -11 UNP P82610 EXPRESSION TAG
SEQADV 4QQU ASP A -10 UNP P82610 EXPRESSION TAG
SEQADV 4QQU LEU A -9 UNP P82610 EXPRESSION TAG
SEQADV 4QQU GLY A -8 UNP P82610 EXPRESSION TAG
SEQADV 4QQU THR A -7 UNP P82610 EXPRESSION TAG
SEQADV 4QQU GLU A -6 UNP P82610 EXPRESSION TAG
SEQADV 4QQU ASN A -5 UNP P82610 EXPRESSION TAG
SEQADV 4QQU LEU A -4 UNP P82610 EXPRESSION TAG
SEQADV 4QQU TYR A -3 UNP P82610 EXPRESSION TAG
SEQADV 4QQU PHE A -2 UNP P82610 EXPRESSION TAG
SEQADV 4QQU GLN A -1 UNP P82610 EXPRESSION TAG
SEQADV 4QQU SER A 0 UNP P82610 EXPRESSION TAG
SEQADV 4QQU ALA A 103 UNP P82610 LYS 103 ENGINEERED MUTATION
SEQADV 4QQU ALA A 104 UNP P82610 LYS 104 ENGINEERED MUTATION
SEQADV 4QQU ALA A 107 UNP P82610 GLU 107 ENGINEERED MUTATION
SEQRES 1 A 789 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 789 GLY THR GLU ASN LEU TYR PHE GLN SER MET VAL GLN SER
SEQRES 3 A 789 SER VAL LEU GLY PHE PRO ARG ILE GLY GLY GLN ARG GLU
SEQRES 4 A 789 LEU LYS LYS ILE THR GLU ALA TYR TRP SER GLY LYS ALA
SEQRES 5 A 789 THR VAL GLU GLU LEU LEU ALA LYS GLY LYS GLU LEU ARG
SEQRES 6 A 789 GLU HIS ASN TRP LYS LEU GLN GLN LYS ALA GLY VAL ASP
SEQRES 7 A 789 ILE ILE PRO SER ASN ASP PHE SER TYR TYR ASP GLN VAL
SEQRES 8 A 789 LEU ASP LEU SER LEU LEU PHE ASN ALA ILE PRO GLU ARG
SEQRES 9 A 789 TYR THR LYS PHE ASP LEU ALA PRO ILE ASP VAL LEU PHE
SEQRES 10 A 789 ALA MET GLY ARG GLY LEU GLN ALA ALA ALA THR ALA THR
SEQRES 11 A 789 GLN ALA ALA VAL ASP VAL THR ALA LEU GLU MET VAL LYS
SEQRES 12 A 789 TRP PHE ASP SER ASN TYR HIS TYR VAL ARG PRO THR PHE
SEQRES 13 A 789 SER HIS SER THR GLU PHE LYS LEU ASN THR ALA ALA GLY
SEQRES 14 A 789 ILE LYS PRO VAL ASP GLU PHE ASN GLU ALA LYS ALA LEU
SEQRES 15 A 789 GLY VAL GLN THR ARG PRO VAL ILE LEU GLY PRO VAL SER
SEQRES 16 A 789 TYR LEU TYR LEU GLY LYS ALA ASP LYS ASP SER LEU ASP
SEQRES 17 A 789 LEU GLU PRO ILE SER LEU LEU PRO LYS ILE LEU PRO VAL
SEQRES 18 A 789 TYR LYS GLU LEU LEU GLN LYS LEU LYS GLU ALA GLY ALA
SEQRES 19 A 789 GLU GLN VAL GLN ILE ASP GLU PRO VAL LEU VAL LEU ASP
SEQRES 20 A 789 LEU PRO GLU ALA VAL GLN SER LYS PHE LYS GLU ALA TYR
SEQRES 21 A 789 ASP ALA LEU VAL GLY ALA ASP VAL PRO GLU LEU ILE LEU
SEQRES 22 A 789 THR THR TYR PHE GLY ASP VAL ARG PRO ASN LEU LYS ALA
SEQRES 23 A 789 ILE GLU ASN LEU PRO VAL ALA GLY PHE HIS PHE ASP PHE
SEQRES 24 A 789 VAL ARG VAL PRO GLU GLN LEU ASP GLU VAL ALA SER ILE
SEQRES 25 A 789 LEU LYS ASP GLY GLN THR LEU SER ALA GLY VAL VAL ASP
SEQRES 26 A 789 GLY ARG ASN ILE TRP LYS THR ASP PHE ALA LYS ALA SER
SEQRES 27 A 789 ALA VAL VAL GLN LYS ALA ILE GLU LYS VAL GLY LYS ASP
SEQRES 28 A 789 LYS VAL VAL VAL ALA THR SER SER SER LEU LEU HIS THR
SEQRES 29 A 789 PRO VAL ASP LEU GLU SER GLU THR LYS LEU ASP ALA VAL
SEQRES 30 A 789 ILE LYS ASP TRP PHE SER PHE ALA THR GLN LYS LEU ASP
SEQRES 31 A 789 GLU VAL VAL VAL ILE ALA LYS ASN VAL SER GLY GLU ASP
SEQRES 32 A 789 VAL SER LYS GLN LEU GLU ALA ASN ALA ALA SER ILE LYS
SEQRES 33 A 789 ALA ARG SER GLU SER SER ILE THR ASN ASP PRO LYS VAL
SEQRES 34 A 789 GLN GLU ARG LEU THR THR ILE ASN GLU ALA LEU ALA THR
SEQRES 35 A 789 ARG LYS ALA ALA PHE PRO GLU ARG LEU THR GLU GLN LYS
SEQRES 36 A 789 ALA LYS TYR ASN LEU PRO LEU PHE PRO THR THR THR ILE
SEQRES 37 A 789 GLY SER PHE PRO GLN THR LYS ASP ILE ARG ILE ASN ARG
SEQRES 38 A 789 ASN LYS PHE ALA LYS GLY GLN ILE THR ALA GLU GLU TYR
SEQRES 39 A 789 GLU ALA PHE ILE ASN LYS GLU ILE GLU THR VAL VAL ARG
SEQRES 40 A 789 PHE GLN GLU GLU ILE GLY LEU ASP VAL LEU VAL HIS GLY
SEQRES 41 A 789 GLU PRO GLU ARG ASN ASP MET VAL GLN TYR PHE GLY GLU
SEQRES 42 A 789 GLN LEU ASN GLY PHE ALA PHE THR THR ASN GLY TRP VAL
SEQRES 43 A 789 GLN SER TYR GLY SER ARG TYR VAL ARG PRO PRO ILE ILE
SEQRES 44 A 789 VAL GLY ASP VAL SER ARG PRO LYS ALA MET THR VAL LYS
SEQRES 45 A 789 GLU SER VAL TYR ALA GLN SER ILE THR SER LYS PRO MET
SEQRES 46 A 789 LYS GLY MET LEU THR GLY PRO VAL THR ILE LEU ARG TRP
SEQRES 47 A 789 SER PHE PRO ARG ASP ASP VAL SER GLY LYS ILE GLN ALA
SEQRES 48 A 789 LEU GLN LEU GLY LEU ALA LEU ARG ASP GLU VAL ASN ASP
SEQRES 49 A 789 LEU GLU GLY ALA GLY ILE THR VAL ILE GLN VAL ASP GLU
SEQRES 50 A 789 PRO ALA ILE ARG GLU GLY LEU PRO LEU ARG ALA GLY LYS
SEQRES 51 A 789 GLU ARG SER ASP TYR LEU ASN TRP ALA ALA GLN SER PHE
SEQRES 52 A 789 ARG VAL ALA THR SER GLY VAL GLU ASN SER THR GLN ILE
SEQRES 53 A 789 HIS SER HIS PHE CYS TYR SER ASP LEU ASP PRO ASN HIS
SEQRES 54 A 789 ILE LYS ALA LEU ASP ALA ASP VAL VAL SER ILE GLU PHE
SEQRES 55 A 789 SER LYS LYS ASP ASP PRO ASN TYR ILE GLN GLU PHE SER
SEQRES 56 A 789 GLU TYR PRO ASN HIS ILE GLY LEU GLY LEU PHE ASP ILE
SEQRES 57 A 789 HIS SER PRO ARG ILE PRO SER LYS GLN GLU PHE VAL SER
SEQRES 58 A 789 ARG ILE GLU GLU ILE LEU LYS VAL TYR PRO ALA SER LYS
SEQRES 59 A 789 PHE TRP VAL ASN PRO ASP CYS GLY LEU LYS THR ARG GLY
SEQRES 60 A 789 TRP PRO GLU VAL LYS GLU SER LEU THR ASN MET VAL GLU
SEQRES 61 A 789 ALA ALA LYS GLU PHE ARG ALA LYS TYR
HET HCS A 801 8
HET ZN A 802 1
HET PO4 A 803 5
HET PO4 A 804 5
HET 39S A 805 50
HETNAM HCS 2-AMINO-4-MERCAPTO-BUTYRIC ACID
HETNAM ZN ZINC ION
HETNAM PO4 PHOSPHATE ION
HETNAM 39S N-[4-({[(6S)-2-AMINO-4-OXO-3,4,5,6,7,8-
HETNAM 2 39S HEXAHYDROPTERIDIN-6-YL]METHYL}AMINO)BENZOYL]-L-GAMMA-
HETNAM 3 39S GLUTAMYL-L-GAMMA-GLUTAMYL-L-GLUTAMIC ACID
HETSYN HCS L-HOMOCYSTEINE
FORMUL 2 HCS C4 H9 N O2 S
FORMUL 3 ZN ZN 2+
FORMUL 4 PO4 2(O4 P 3-)
FORMUL 6 39S C29 H37 N9 O12
FORMUL 7 HOH *41(H2 O)
HELIX 1 1 ARG A 16 SER A 27 1 12
HELIX 2 2 THR A 31 GLY A 54 1 24
HELIX 3 3 ASP A 67 PHE A 76 1 10
HELIX 4 4 PRO A 80 THR A 84 5 5
HELIX 5 5 ALA A 89 GLY A 100 1 12
HELIX 6 6 ILE A 148 ALA A 159 1 12
HELIX 7 7 GLY A 170 GLY A 178 1 9
HELIX 8 8 LYS A 182 LEU A 185 5 4
HELIX 9 9 GLU A 188 SER A 191 5 4
HELIX 10 10 LEU A 192 GLY A 211 1 20
HELIX 11 11 PRO A 220 LEU A 224 5 5
HELIX 12 12 PRO A 227 SER A 232 1 6
HELIX 13 13 SER A 232 VAL A 242 1 11
HELIX 14 14 VAL A 258 PRO A 260 5 3
HELIX 15 15 ASN A 261 GLU A 266 1 6
HELIX 16 16 VAL A 280 GLU A 282 5 3
HELIX 17 17 GLN A 283 ILE A 290 1 8
HELIX 18 18 ASP A 311 GLY A 327 1 17
HELIX 19 19 SER A 338 THR A 342 5 5
HELIX 20 20 ASP A 345 GLU A 349 5 5
HELIX 21 21 ASP A 353 ASP A 358 1 6
HELIX 22 22 PHE A 362 SER A 378 1 17
HELIX 23 23 VAL A 382 GLU A 398 1 17
HELIX 24 24 ASP A 404 LEU A 411 1 8
HELIX 25 25 THR A 412 ILE A 414 5 3
HELIX 26 26 GLU A 416 THR A 420 5 5
HELIX 27 27 ALA A 424 ASN A 437 1 14
HELIX 28 28 THR A 452 LYS A 464 1 13
HELIX 29 29 THR A 468 GLY A 491 1 24
HELIX 30 30 VAL A 506 GLU A 511 1 6
HELIX 31 31 THR A 548 ILE A 558 1 11
HELIX 32 32 GLY A 569 TRP A 576 1 8
HELIX 33 33 SER A 584 ALA A 606 1 23
HELIX 34 34 GLY A 627 SER A 646 1 20
HELIX 35 35 ASP A 664 LEU A 671 1 8
HELIX 36 36 ASN A 687 PHE A 692 1 6
HELIX 37 37 SER A 713 LYS A 726 1 14
HELIX 38 38 GLY A 745 TYR A 767 1 23
SHEET 1 A 8 GLN A 3 SER A 5 0
SHEET 2 A 8 VAL A 331 THR A 335 1 O VAL A 333 N SER A 5
SHEET 3 A 8 THR A 296 VAL A 302 1 N ALA A 299 O VAL A 332
SHEET 4 A 8 GLY A 272 ASP A 276 1 N PHE A 275 O GLY A 300
SHEET 5 A 8 GLU A 248 THR A 252 1 N LEU A 251 O GLY A 272
SHEET 6 A 8 GLN A 214 ASP A 218 1 N VAL A 215 O ILE A 250
SHEET 7 A 8 THR A 164 LEU A 169 1 N PRO A 166 O GLN A 216
SHEET 8 A 8 ILE A 58 SER A 60 1 N ILE A 58 O ARG A 165
SHEET 1 B 2 LEU A 101 ALA A 103 0
SHEET 2 B 2 VAL A 112 VAL A 114 -1 O VAL A 114 N LEU A 101
SHEET 1 C 2 MET A 119 LYS A 121 0
SHEET 2 C 2 HIS A 128 VAL A 130 -1 O TYR A 129 N VAL A 120
SHEET 1 D 2 THR A 133 PHE A 134 0
SHEET 2 D 2 LYS A 179 ALA A 180 1 O LYS A 179 N PHE A 134
SHEET 1 E 2 ASN A 514 ALA A 517 0
SHEET 2 E 2 ILE A 536 SER A 542 -1 O VAL A 538 N GLY A 515
SHEET 1 F 2 VAL A 524 TYR A 527 0
SHEET 2 F 2 ARG A 530 VAL A 532 -1 O VAL A 532 N VAL A 524
SHEET 1 G 5 LYS A 564 THR A 568 0
SHEET 2 G 5 VAL A 610 ASP A 614 1 O GLN A 612 N LEU A 567
SHEET 3 G 5 GLN A 653 PHE A 658 1 O HIS A 655 N VAL A 613
SHEET 4 G 5 VAL A 675 ILE A 678 1 O VAL A 675 N SER A 656
SHEET 5 G 5 GLY A 700 LEU A 701 1 O GLY A 700 N VAL A 676
LINK NE2 HIS A 657 ZN ZN A 802 1555 1555 2.21
LINK SG CYS A 659 ZN ZN A 802 1555 1555 2.18
LINK SG CYS A 739 ZN ZN A 802 1555 1555 2.36
LINK SD HCS A 801 ZN ZN A 802 1555 1555 1.94
SITE 1 AC1 13 ILE A 446 GLY A 447 SER A 448 GLU A 499
SITE 2 AC1 13 MET A 505 MET A 566 ASP A 614 HIS A 657
SITE 3 AC1 13 CYS A 659 CYS A 739 GLY A 740 ZN A 802
SITE 4 AC1 13 39S A 805
SITE 1 AC2 4 HIS A 657 CYS A 659 CYS A 739 HCS A 801
SITE 1 AC3 6 ARG A 99 TYR A 527 ARG A 530 HIS A 707
SITE 2 AC3 6 THR A 743 ARG A 744
SITE 1 AC4 6 PRO A 665 ASN A 666 LYS A 669 GLU A 694
SITE 2 AC4 6 TYR A 695 PRO A 696
SITE 1 AC5 21 ARG A 16 LYS A 19 ASN A 126 LYS A 330
SITE 2 AC5 21 GLN A 451 LYS A 453 ARG A 456 ARG A 459
SITE 3 AC5 21 ASN A 503 ASP A 504 MET A 505 TRP A 523
SITE 4 AC5 21 SER A 526 ARG A 530 TYR A 531 VAL A 532
SITE 5 AC5 21 TRP A 576 THR A 743 HCS A 801 HOH A 915
SITE 6 AC5 21 HOH A 923
CRYST1 74.978 99.102 103.902 90.00 90.00 90.00 P 21 21 21 4
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 0.013337 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010091 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009624 0.00000
(ATOM LINES ARE NOT SHOWN.)
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