HEADER STRUCTURAL PROTEIN 28-APR-04 1T44
TITLE STRUCTURAL BASIS OF ACTIN SEQUESTRATION BY THYMOSIN-B4: IMPLICATIONS
TITLE 2 FOR ARP2/3 ACTIVATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHIMERA OF GELSOLIN DOMAIN 1 AND C-TERMINAL DOMAIN OF
COMPND 3 THYMOSIN BETA-4;
COMPND 4 CHAIN: G;
COMPND 5 FRAGMENT: CHIMERA OF GELSOLIN DOMAIN 1 (RESIDUES 28-152) FROM HUMAN
COMPND 6 AND C-TERMINAL DOMAIN OF THYMOSIN BETA-4 FROM MOUSE (RESIDUES 153-
COMPND 7 171);
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: ACTIN, ALPHA;
COMPND 11 CHAIN: A;
COMPND 12 SYNONYM: ALPHA-ACTIN 1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HUMAN, HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 9606, 10090;
SOURCE 5 STRAIN: ,;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;
SOURCE 10 ORGANISM_COMMON: RABBIT;
SOURCE 11 ORGANISM_TAXID: 9986;
SOURCE 12 TISSUE: SKELETAL MUSCLE
KEYWDS STRUCTURAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR E.IROBI,A.H.AGUDA,M.LARSSON,L.D.BURTNICK,R.C.ROBINSON
REVDAT 5 23-AUG-23 1T44 1 REMARK SEQADV LINK
REVDAT 4 23-AUG-17 1T44 1 SOURCE
REVDAT 3 24-FEB-09 1T44 1 VERSN
REVDAT 2 21-SEP-04 1T44 1 JRNL
REVDAT 1 07-SEP-04 1T44 0
JRNL AUTH E.IROBI,A.H.AGUDA,M.LARSSON,C.GUERIN,H.L.YIN,L.D.BURTNICK,
JRNL AUTH 2 L.BLANCHOIN,R.C.ROBINSON
JRNL TITL STRUCTURAL BASIS OF ACTIN SEQUESTRATION BY THYMOSIN-BETA4:
JRNL TITL 2 IMPLICATIONS FOR WH2 PROTEINS.
JRNL REF EMBO J. V. 23 3599 2004
JRNL REFN ISSN 0261-4189
JRNL PMID 15329672
JRNL DOI 10.1038/SJ.EMBOJ.7600372
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 39223
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) : 0.147
REMARK 3 R VALUE (WORKING SET) : 0.144
REMARK 3 FREE R VALUE : 0.195
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2079
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2890
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.1270
REMARK 3 BIN FREE R VALUE SET COUNT : 140
REMARK 3 BIN FREE R VALUE : 0.1960
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3959
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 34
REMARK 3 SOLVENT ATOMS : 427
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.98
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.14000
REMARK 3 B22 (A**2) : -0.42000
REMARK 3 B33 (A**2) : -0.66000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.35000
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): 0.134
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.085
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.957
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.937
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4082 ; 0.014 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 3627 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5535 ; 1.434 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8473 ; 0.868 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 499 ; 5.574 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 603 ; 0.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4512 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 809 ; 0.004 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 784 ; 0.203 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 4127 ; 0.245 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 2242 ; 0.086 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 304 ; 0.162 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 15 ; 0.078 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 3 ; 0.068 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 42 ; 0.252 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 19 ; 0.106 ; 0.200
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): 2494 ; 0.969 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4025 ; 1.629 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1588 ; 2.950 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1510 ; 4.545 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : 7
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 4
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 6 A 32
REMARK 3 RESIDUE RANGE : A 71 A 136
REMARK 3 RESIDUE RANGE : A 337 A 375
REMARK 3 RESIDUE RANGE : A 700 A 700
REMARK 3 ORIGIN FOR THE GROUP (A): 13.2700 -8.4420 23.0340
REMARK 3 T TENSOR
REMARK 3 T11: 0.0634 T22: 0.1292
REMARK 3 T33: 0.1194 T12: -0.0043
REMARK 3 T13: 0.0115 T23: -0.0121
REMARK 3 L TENSOR
REMARK 3 L11: 0.5605 L22: 1.1180
REMARK 3 L33: 1.1494 L12: 0.1648
REMARK 3 L13: -0.2891 L23: 0.1821
REMARK 3 S TENSOR
REMARK 3 S11: -0.0190 S12: -0.0111 S13: -0.0442
REMARK 3 S21: -0.0277 S22: 0.0356 S23: -0.1174
REMARK 3 S31: 0.0297 S32: 0.0954 S33: -0.0166
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 33 A 70
REMARK 3 ORIGIN FOR THE GROUP (A): 18.5280 1.1990 3.7080
REMARK 3 T TENSOR
REMARK 3 T11: 0.0516 T22: 0.1358
REMARK 3 T33: 0.0745 T12: -0.0136
REMARK 3 T13: 0.0600 T23: -0.0263
REMARK 3 L TENSOR
REMARK 3 L11: 3.4305 L22: 8.0116
REMARK 3 L33: 2.9583 L12: 1.4418
REMARK 3 L13: -0.6866 L23: -1.3148
REMARK 3 S TENSOR
REMARK 3 S11: 0.1536 S12: 0.1717 S13: 0.0814
REMARK 3 S21: -0.1824 S22: -0.0247 S23: -0.3562
REMARK 3 S31: 0.0883 S32: 0.2529 S33: -0.1289
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 137 A 180
REMARK 3 RESIDUE RANGE : A 274 A 336
REMARK 3 ORIGIN FOR THE GROUP (A): -10.5150 -0.4510 22.7710
REMARK 3 T TENSOR
REMARK 3 T11: 0.0833 T22: 0.1425
REMARK 3 T33: 0.1016 T12: -0.0118
REMARK 3 T13: 0.0025 T23: 0.0092
REMARK 3 L TENSOR
REMARK 3 L11: 0.8275 L22: 0.7237
REMARK 3 L33: 1.2282 L12: -0.0942
REMARK 3 L13: 0.0683 L23: -0.1121
REMARK 3 S TENSOR
REMARK 3 S11: -0.0133 S12: 0.0317 S13: 0.0173
REMARK 3 S21: -0.0227 S22: 0.0288 S23: 0.0389
REMARK 3 S31: 0.0466 S32: -0.0964 S33: -0.0155
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 181 A 273
REMARK 3 RESIDUE RANGE : A 900 A 900
REMARK 3 ORIGIN FOR THE GROUP (A): -4.7810 13.5290 3.1250
REMARK 3 T TENSOR
REMARK 3 T11: 0.1104 T22: 0.1341
REMARK 3 T33: 0.0662 T12: -0.0016
REMARK 3 T13: 0.0049 T23: 0.0351
REMARK 3 L TENSOR
REMARK 3 L11: 0.9088 L22: 1.1919
REMARK 3 L33: 1.0628 L12: -0.1035
REMARK 3 L13: -0.3906 L23: -0.3899
REMARK 3 S TENSOR
REMARK 3 S11: 0.0332 S12: 0.0584 S13: 0.0367
REMARK 3 S21: -0.1388 S22: -0.0017 S23: -0.0331
REMARK 3 S31: -0.0100 S32: -0.0762 S33: -0.0315
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 28 G 152
REMARK 3 RESIDUE RANGE : G 701 G 702
REMARK 3 ORIGIN FOR THE GROUP (A): -2.8120 -1.7860 47.4380
REMARK 3 T TENSOR
REMARK 3 T11: 0.1344 T22: 0.1038
REMARK 3 T33: 0.0792 T12: 0.0056
REMARK 3 T13: 0.0027 T23: 0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 0.6797 L22: 1.5906
REMARK 3 L33: 0.9111 L12: 0.4544
REMARK 3 L13: -0.2006 L23: -0.0675
REMARK 3 S TENSOR
REMARK 3 S11: 0.0099 S12: -0.0591 S13: -0.0098
REMARK 3 S21: 0.1737 S22: 0.0096 S23: 0.0193
REMARK 3 S31: 0.0130 S32: 0.0458 S33: -0.0195
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 153 G 171
REMARK 3 ORIGIN FOR THE GROUP (A): 15.5960 12.6590 3.6640
REMARK 3 T TENSOR
REMARK 3 T11: 0.0940 T22: 0.0756
REMARK 3 T33: 0.1570 T12: 0.0203
REMARK 3 T13: 0.0962 T23: 0.0520
REMARK 3 L TENSOR
REMARK 3 L11: 1.0654 L22: 0.9998
REMARK 3 L33: 32.7026 L12: 0.3132
REMARK 3 L13: -1.0000 L23: -4.8265
REMARK 3 S TENSOR
REMARK 3 S11: 0.1943 S12: 0.1473 S13: 0.3959
REMARK 3 S21: 0.0083 S22: -0.0160 S23: -0.2443
REMARK 3 S31: -0.0383 S32: 0.3091 S33: -0.1783
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 901 A 1175
REMARK 3 ORIGIN FOR THE GROUP (A): -1.0040 1.3470 25.0510
REMARK 3 T TENSOR
REMARK 3 T11: 0.1027 T22: 0.1280
REMARK 3 T33: 0.1012 T12: -0.0148
REMARK 3 T13: -0.0028 T23: 0.0088
REMARK 3 L TENSOR
REMARK 3 L11: 0.0662 L22: 0.2688
REMARK 3 L33: 0.3065 L12: -0.0219
REMARK 3 L13: -0.1275 L23: -0.0315
REMARK 3 S TENSOR
REMARK 3 S11: 0.0024 S12: 0.0201 S13: 0.0092
REMARK 3 S21: 0.0119 S22: 0.0066 S23: -0.0100
REMARK 3 S31: 0.0121 S32: -0.0104 S33: -0.0090
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 1T44 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAY-04.
REMARK 100 THE DEPOSITION ID IS D_1000022287.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0052
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 : 39223
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.11400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.10
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.19800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1P8Z
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, SODIUM ACETATE, CALCIUM
REMARK 280 CHLORIDE, PH 6.5, MICROBATCH, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
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
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 34.66750
REMARK 290 SMTRY3 2 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5310 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -59.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, 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 GLY G 25
REMARK 465 SER G 26
REMARK 465 HIS G 27
REMARK 465 ARG A 39
REMARK 465 HIS A 40
REMARK 465 GLN A 41
REMARK 465 GLY A 42
REMARK 465 VAL A 43
REMARK 465 MET A 44
REMARK 465 VAL A 45
REMARK 465 GLY A 46
REMARK 465 MET A 47
REMARK 465 GLY A 48
REMARK 465 GLN A 49
REMARK 465 LYS A 50
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 GLN G 171 O HOH G 749 2.17
REMARK 500
REMARK 500 REMARK: NULL
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 PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 51 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ARG A 147 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG A 147 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 ASP A 222 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG A 256 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 ARG A 256 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
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 LEU G 112 30.42 -86.37
REMARK 500 PHE G 125 27.13 -141.50
REMARK 500 LYS G 157 77.47 -101.83
REMARK 500 ALA A 181 -159.45 -151.97
REMARK 500 ASN A 296 55.73 -141.84
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 CA G 702 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY G 65 O
REMARK 620 2 ASP G 66 OD2 79.8
REMARK 620 3 GLU G 97 OE2 121.7 86.2
REMARK 620 4 GLU G 97 OE1 75.4 100.1 51.8
REMARK 620 5 VAL G 145 O 149.9 88.5 84.7 134.4
REMARK 620 6 HOH G 704 O 80.1 100.6 158.1 144.4 74.8
REMARK 620 7 HOH G 730 O 103.5 170.0 84.1 72.1 92.7 89.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA G 701 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP G 109 OD1
REMARK 620 2 ASP G 109 OD2 49.1
REMARK 620 3 GLY G 114 O 70.9 119.2
REMARK 620 4 ALA G 116 O 79.4 83.7 95.8
REMARK 620 5 HOH G 712 O 78.6 72.9 88.2 154.9
REMARK 620 6 HOH G 724 O 137.1 140.9 77.1 132.6 72.4
REMARK 620 7 HOH G 729 O 138.0 152.3 80.0 74.0 130.9 58.5
REMARK 620 8 GLU A 167 OE1 131.0 81.9 156.3 97.4 88.1 79.5 84.8
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 700 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ATP A 900 O2B
REMARK 620 2 ATP A 900 O3G 80.1
REMARK 620 3 HOH A 909 O 171.1 91.2
REMARK 620 4 HOH A 911 O 94.0 77.7 82.4
REMARK 620 5 HOH A 915 O 95.6 70.3 82.9 144.4
REMARK 620 6 HOH A 918 O 91.2 134.1 96.2 148.1 65.8
REMARK 620 7 HOH A 970 O 86.8 152.1 100.3 78.7 136.0 70.2
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA G 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA G 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 900
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1P8Z RELATED DB: PDB
REMARK 900 A HYBRID OF THIS PROTEIN WITH THE C-TERMINAL HALF OF THYMOSIN B4
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 FUSION OF GELSOLIN DOMAIN 1 FROM HUMAN WITH
REMARK 999 C-TERMINAL DOMAIN OF THYMOSIN B4 FROM MOUSE
REMARK 999 (SEQUENCE:ETQEKNPLPSKETIEQEKQ)
DBREF 1T44 G 28 152 UNP P06396 GELS_HUMAN 55 179
DBREF 1T44 G 153 171 UNP P20065 TYB4_MOUSE 28 46
DBREF 1T44 A 6 375 UNP P02568 ACTS_HUMAN 8 377
SEQADV 1T44 GLY G 25 UNP P06396 CLONING ARTIFACT
SEQADV 1T44 SER G 26 UNP P06396 CLONING ARTIFACT
SEQADV 1T44 HIS G 27 UNP P06396 CLONING ARTIFACT
SEQRES 1 G 147 GLY SER HIS GLU HIS PRO GLU PHE LEU LYS ALA GLY LYS
SEQRES 2 G 147 GLU PRO GLY LEU GLN ILE TRP ARG VAL GLU LYS PHE ASP
SEQRES 3 G 147 LEU VAL PRO VAL PRO THR ASN LEU TYR GLY ASP PHE PHE
SEQRES 4 G 147 THR GLY ASP ALA TYR VAL ILE LEU LYS THR VAL GLN LEU
SEQRES 5 G 147 ARG ASN GLY ASN LEU GLN TYR ASP LEU HIS TYR TRP LEU
SEQRES 6 G 147 GLY ASN GLU CYS SER GLN ASP GLU SER GLY ALA ALA ALA
SEQRES 7 G 147 ILE PHE THR VAL GLN LEU ASP ASP TYR LEU ASN GLY ARG
SEQRES 8 G 147 ALA VAL GLN HIS ARG GLU VAL GLN GLY PHE GLU SER ALA
SEQRES 9 G 147 THR PHE LEU GLY TYR PHE LYS SER GLY LEU LYS TYR LYS
SEQRES 10 G 147 LYS GLY GLY VAL ALA SER GLY PHE LYS HIS VAL GLU THR
SEQRES 11 G 147 GLN GLU LYS ASN PRO LEU PRO SER LYS GLU THR ILE GLU
SEQRES 12 G 147 GLN GLU LYS GLN
SEQRES 1 A 370 THR ALA LEU VAL CYS ASP ASN GLY SER GLY LEU VAL LYS
SEQRES 2 A 370 ALA GLY PHE ALA GLY ASP ASP ALA PRO ARG ALA VAL PHE
SEQRES 3 A 370 PRO SER ILE VAL GLY ARG PRO ARG HIS GLN GLY VAL MET
SEQRES 4 A 370 VAL GLY MET GLY GLN LYS ASP SER TYR VAL GLY ASP GLU
SEQRES 5 A 370 ALA GLN SER LYS ARG GLY ILE LEU THR LEU LYS TYR PRO
SEQRES 6 A 370 ILE GLU HIS GLY ILE ILE THR ASN TRP ASP ASP MET GLU
SEQRES 7 A 370 LYS ILE TRP HIS HIS THR PHE TYR ASN GLU LEU ARG VAL
SEQRES 8 A 370 ALA PRO GLU GLU HIS PRO THR LEU LEU THR GLU ALA PRO
SEQRES 9 A 370 LEU ASN PRO LYS ALA ASN ARG GLU LYS MET THR GLN ILE
SEQRES 10 A 370 MET PHE GLU THR PHE ASN VAL PRO ALA MET TYR VAL ALA
SEQRES 11 A 370 ILE GLN ALA VAL LEU SER LEU TYR ALA SER GLY ARG THR
SEQRES 12 A 370 THR GLY ILE VAL LEU ASP SER GLY ASP GLY VAL THR HIS
SEQRES 13 A 370 ASN VAL PRO ILE TYR GLU GLY TYR ALA LEU PRO HIS ALA
SEQRES 14 A 370 ILE MET ARG LEU ASP LEU ALA GLY ARG ASP LEU THR ASP
SEQRES 15 A 370 TYR LEU MET LYS ILE LEU THR GLU ARG GLY TYR SER PHE
SEQRES 16 A 370 VAL THR THR ALA GLU ARG GLU ILE VAL ARG ASP ILE LYS
SEQRES 17 A 370 GLU LYS LEU CYS TYR VAL ALA LEU ASP PHE GLU ASN GLU
SEQRES 18 A 370 MET ALA THR ALA ALA SER SER SER SER LEU GLU LYS SER
SEQRES 19 A 370 TYR GLU LEU PRO ASP GLY GLN VAL ILE THR ILE GLY ASN
SEQRES 20 A 370 GLU ARG PHE ARG CYS PRO GLU THR LEU PHE GLN PRO SER
SEQRES 21 A 370 PHE ILE GLY MET GLU SER ALA GLY ILE HIS GLU THR THR
SEQRES 22 A 370 TYR ASN SER ILE MET LYS CYS ASP ILE ASP ILE ARG LYS
SEQRES 23 A 370 ASP LEU TYR ALA ASN ASN VAL MET SER GLY GLY THR THR
SEQRES 24 A 370 MET TYR PRO GLY ILE ALA ASP ARG MET GLN LYS GLU ILE
SEQRES 25 A 370 THR ALA LEU ALA PRO SER THR MET LYS ILE LYS ILE ILE
SEQRES 26 A 370 ALA PRO PRO GLU ARG LYS TYR SER VAL TRP ILE GLY GLY
SEQRES 27 A 370 SER ILE LEU ALA SER LEU SER THR PHE GLN GLN MET TRP
SEQRES 28 A 370 ILE THR LYS GLN GLU TYR ASP GLU ALA GLY PRO SER ILE
SEQRES 29 A 370 VAL HIS ARG LYS CYS PHE
HET CA G 701 1
HET CA G 702 1
HET CA A 700 1
HET ATP A 900 31
HETNAM CA CALCIUM ION
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
FORMUL 3 CA 3(CA 2+)
FORMUL 6 ATP C10 H16 N5 O13 P3
FORMUL 7 HOH *427(H2 O)
HELIX 1 1 HIS G 29 ALA G 35 1 7
HELIX 2 2 PRO G 55 TYR G 59 5 5
HELIX 3 3 SER G 94 LEU G 112 1 19
HELIX 4 4 SER G 127 GLY G 132 1 6
HELIX 5 5 SER G 162 GLN G 171 1 10
HELIX 6 6 GLY A 55 LYS A 61 1 7
HELIX 7 7 ARG A 62 LEU A 65 5 4
HELIX 8 8 ASN A 78 ASN A 92 1 15
HELIX 9 9 ALA A 97 HIS A 101 5 5
HELIX 10 10 PRO A 112 THR A 126 1 15
HELIX 11 11 GLN A 137 SER A 145 1 9
HELIX 12 12 PRO A 172 ILE A 175 5 4
HELIX 13 13 ALA A 181 ARG A 196 1 16
HELIX 14 14 THR A 202 CYS A 217 1 16
HELIX 15 15 ASP A 222 SER A 233 1 12
HELIX 16 16 ASN A 252 THR A 260 1 9
HELIX 17 17 LEU A 261 PHE A 262 5 2
HELIX 18 18 GLN A 263 GLY A 268 5 6
HELIX 19 19 GLY A 273 LYS A 284 1 12
HELIX 20 20 ASP A 286 ALA A 295 1 10
HELIX 21 21 GLY A 301 MET A 305 5 5
HELIX 22 22 GLY A 308 ALA A 321 1 14
HELIX 23 23 GLU A 334 LYS A 336 5 3
HELIX 24 24 TYR A 337 LEU A 349 1 13
HELIX 25 25 SER A 350 GLN A 353 5 4
HELIX 26 26 LYS A 359 GLY A 366 1 8
HELIX 27 27 ILE A 369 CYS A 374 1 6
SHEET 1 A 5 ASP G 50 PRO G 53 0
SHEET 2 A 5 GLY G 40 GLU G 47 -1 N ARG G 45 O VAL G 52
SHEET 3 A 5 ALA G 67 GLN G 75 -1 O VAL G 69 N TRP G 44
SHEET 4 A 5 LEU G 81 LEU G 89 -1 O GLN G 82 N VAL G 74
SHEET 5 A 5 VAL G 117 VAL G 122 1 O GLU G 121 N TYR G 87
SHEET 1 B 2 ASP G 61 PHE G 63 0
SHEET 2 B 2 LYS G 139 LYS G 141 1 O LYS G 139 N PHE G 62
SHEET 1 C 7 GLN G 155 GLU G 156 0
SHEET 2 C 7 ALA A 29 PRO A 32 1 O VAL A 30 N GLN G 155
SHEET 3 C 7 LEU A 16 PHE A 21 -1 N VAL A 17 O PHE A 31
SHEET 4 C 7 LEU A 8 ASN A 12 -1 N ASP A 11 O LYS A 18
SHEET 5 C 7 THR A 103 GLU A 107 1 O LEU A 104 N LEU A 8
SHEET 6 C 7 ALA A 131 ILE A 136 1 O TYR A 133 N LEU A 105
SHEET 7 C 7 ILE A 357 THR A 358 -1 O ILE A 357 N MET A 132
SHEET 1 D 3 TYR A 53 VAL A 54 0
SHEET 2 D 3 VAL A 35 ARG A 37 -1 N GLY A 36 O TYR A 53
SHEET 3 D 3 THR A 66 LYS A 68 -1 O THR A 66 N ARG A 37
SHEET 1 E 2 ILE A 71 GLU A 72 0
SHEET 2 E 2 ILE A 75 ILE A 76 -1 O ILE A 75 N GLU A 72
SHEET 1 F 3 TYR A 169 ALA A 170 0
SHEET 2 F 3 THR A 160 TYR A 166 -1 N TYR A 166 O TYR A 169
SHEET 3 F 3 MET A 176 LEU A 178 -1 O LEU A 178 N THR A 160
SHEET 1 G 5 TYR A 169 ALA A 170 0
SHEET 2 G 5 THR A 160 TYR A 166 -1 N TYR A 166 O TYR A 169
SHEET 3 G 5 GLY A 150 SER A 155 -1 N GLY A 150 O ILE A 165
SHEET 4 G 5 ASN A 297 SER A 300 1 O SER A 300 N LEU A 153
SHEET 5 G 5 ILE A 329 ILE A 330 1 O ILE A 330 N ASN A 297
SHEET 1 H 2 LYS A 238 GLU A 241 0
SHEET 2 H 2 VAL A 247 ILE A 250 -1 O ILE A 248 N TYR A 240
LINK O GLY G 65 CA CA G 702 1555 1555 2.33
LINK OD2 ASP G 66 CA CA G 702 1555 1555 2.34
LINK OE2 GLU G 97 CA CA G 702 1555 1555 2.46
LINK OE1 GLU G 97 CA CA G 702 1555 1555 2.53
LINK OD1 ASP G 109 CA CA G 701 1555 1555 2.75
LINK OD2 ASP G 109 CA CA G 701 1555 1555 2.36
LINK O GLY G 114 CA CA G 701 1555 1555 2.43
LINK O ALA G 116 CA CA G 701 1555 1555 2.31
LINK O VAL G 145 CA CA G 702 1555 1555 2.34
LINK CA CA G 701 O HOH G 712 1555 1555 2.40
LINK CA CA G 701 O HOH G 724 1555 1555 2.61
LINK CA CA G 701 O HOH G 729 1555 1555 2.42
LINK CA CA G 701 OE1 GLU A 167 1555 1555 2.31
LINK CA CA G 702 O HOH G 704 1555 1555 2.32
LINK CA CA G 702 O HOH G 730 1555 1555 2.33
LINK CA CA A 700 O2B ATP A 900 1555 1555 2.30
LINK CA CA A 700 O3G ATP A 900 1555 1555 2.41
LINK CA CA A 700 O HOH A 909 1555 1555 2.38
LINK CA CA A 700 O HOH A 911 1555 1555 2.43
LINK CA CA A 700 O HOH A 915 1555 1555 2.75
LINK CA CA A 700 O HOH A 918 1555 1555 2.36
LINK CA CA A 700 O HOH A 970 1555 1555 2.38
SITE 1 AC1 6 ATP A 900 HOH A 909 HOH A 911 HOH A 915
SITE 2 AC1 6 HOH A 918 HOH A 970
SITE 1 AC2 7 GLU A 167 ASP G 109 GLY G 114 ALA G 116
SITE 2 AC2 7 HOH G 712 HOH G 724 HOH G 729
SITE 1 AC3 6 GLY G 65 ASP G 66 GLU G 97 VAL G 145
SITE 2 AC3 6 HOH G 704 HOH G 730
SITE 1 AC4 26 GLY A 13 SER A 14 GLY A 15 LEU A 16
SITE 2 AC4 26 LYS A 18 GLY A 156 ASP A 157 GLY A 158
SITE 3 AC4 26 VAL A 159 GLY A 182 ARG A 210 LYS A 213
SITE 4 AC4 26 GLU A 214 GLY A 301 GLY A 302 THR A 303
SITE 5 AC4 26 MET A 305 TYR A 306 CA A 700 HOH A 904
SITE 6 AC4 26 HOH A 911 HOH A 915 HOH A 949 HOH A 992
SITE 7 AC4 26 HOH A 999 HOH A1022
CRYST1 56.850 69.335 80.233 90.00 94.93 90.00 P 1 21 1 2
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 0.017590 0.000000 0.001517 0.00000
SCALE2 0.000000 0.014423 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012510 0.00000
(ATOM LINES ARE NOT SHOWN.)
END