| content |
HEADER HYDROLASE 14-DEC-11 3V48
TITLE CRYSTAL STRUCTURE OF THE PUTATIVE ALPHA/BETA HYDROLASE RUTD FROM
TITLE 2 E.COLI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE AMINOACRYLATE HYDROLASE RUTD;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: AMINOHYDROLASE;
COMPND 5 EC: 3.5.1.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI SE11;
SOURCE 3 ORGANISM_TAXID: 409438;
SOURCE 4 STRAIN: XL-1 BLUE;
SOURCE 5 GENE: ECSE_1071, RUTD;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21DE3RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B, MODIFIED FOR TEV CLEAVAGE
KEYWDS STRUCTURAL GENOMICS, PSI-BIOLOGY, NEW YORK STRUCTURAL GENOMICS
KEYWDS 2 RESEARCH CONSORTIUM, NYSGRC, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.A.KNAPIK,J.J.PETKOWSKI,Z.OTWINOWSKI,M.T.CYMBOROWSKI,D.G.COOPER,
AUTHOR 2 M.CHRUSZCZ,P.J.POREBSKI,E.NIEDZIALKOWSKA,S.C.ALMO,W.MINOR,NEW YORK
AUTHOR 3 STRUCTURAL GENOMICS RESEARCH CONSORTIUM (NYSGRC)
REVDAT 1 04-JAN-12 3V48 0
JRNL AUTH A.A.KNAPIK,J.J.PETKOWSKI,Z.OTWINOWSKI,M.T.CYMBOROWSKI,
JRNL AUTH 2 D.G.COOPER,K.A.MAJOREK,M.CHRUSZCZ,W.MINOR
JRNL TITL THE STRUCTURE OF RUTD, A MEMBER OF THE ALPHA/BETA HYDROLASE
JRNL TITL 2 SUPERFAMILY, AND A PUTATIVE AMINOACRYLATE HYDROLYTIC ENZYME
JRNL TITL 3 OF THE RUT URACIL DEGRADATION PATHWAY IN E.COLI
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.6
REMARK 3 NUMBER OF REFLECTIONS : 28021
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) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1471
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1686
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 78.34
REMARK 3 BIN R VALUE (WORKING SET) : 0.1900
REMARK 3 BIN FREE R VALUE SET COUNT : 68
REMARK 3 BIN FREE R VALUE : 0.2340
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4044
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 33
REMARK 3 SOLVENT ATOMS : 313
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.91
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.14000
REMARK 3 B22 (A**2) : -0.14000
REMARK 3 B33 (A**2) : 0.28000
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): 0.240
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.195
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.917
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4187 ; 0.013 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2724 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5709 ; 1.492 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6652 ; 4.291 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 535 ; 5.649 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 183 ;36.055 ;23.880
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 597 ;14.439 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 25 ;21.201 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 646 ; 0.077 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4721 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 828 ; 0.009 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED 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 : 10
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 14
REMARK 3 ORIGIN FOR THE GROUP (A): 28.9830 16.4210 73.0990
REMARK 3 T TENSOR
REMARK 3 T11: 0.2035 T22: 0.2770
REMARK 3 T33: 0.0561 T12: 0.0644
REMARK 3 T13: -0.0148 T23: -0.0504
REMARK 3 L TENSOR
REMARK 3 L11: 13.4294 L22: 4.0091
REMARK 3 L33: 1.2260 L12: 2.2698
REMARK 3 L13: -2.0179 L23: -0.7701
REMARK 3 S TENSOR
REMARK 3 S11: 0.1693 S12: -0.8162 S13: -0.1324
REMARK 3 S21: 0.6266 S22: -0.1096 S23: -0.2656
REMARK 3 S31: -0.2507 S32: 0.1654 S33: -0.0597
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 15 A 116
REMARK 3 ORIGIN FOR THE GROUP (A): 33.3480 12.6130 61.3370
REMARK 3 T TENSOR
REMARK 3 T11: 0.0366 T22: 0.1289
REMARK 3 T33: 0.0248 T12: 0.0306
REMARK 3 T13: -0.0078 T23: 0.0032
REMARK 3 L TENSOR
REMARK 3 L11: 2.0215 L22: 1.2332
REMARK 3 L33: 2.0641 L12: -0.3068
REMARK 3 L13: -0.6026 L23: 0.0258
REMARK 3 S TENSOR
REMARK 3 S11: -0.0502 S12: -0.2293 S13: 0.0030
REMARK 3 S21: 0.0730 S22: 0.0489 S23: -0.0288
REMARK 3 S31: 0.0727 S32: 0.2110 S33: 0.0014
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 117 A 172
REMARK 3 ORIGIN FOR THE GROUP (A): 36.0340 25.7450 44.6980
REMARK 3 T TENSOR
REMARK 3 T11: 0.1270 T22: 0.1899
REMARK 3 T33: 0.1126 T12: -0.0495
REMARK 3 T13: 0.0328 T23: -0.0434
REMARK 3 L TENSOR
REMARK 3 L11: 1.4491 L22: 0.1766
REMARK 3 L33: 1.3395 L12: -0.2471
REMARK 3 L13: 0.2365 L23: -0.2915
REMARK 3 S TENSOR
REMARK 3 S11: 0.0676 S12: -0.1131 S13: 0.2333
REMARK 3 S21: 0.0137 S22: 0.0270 S23: -0.0701
REMARK 3 S31: -0.1953 S32: 0.2575 S33: -0.0946
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 173 A 258
REMARK 3 ORIGIN FOR THE GROUP (A): 27.1480 10.9370 51.0370
REMARK 3 T TENSOR
REMARK 3 T11: 0.0495 T22: 0.0763
REMARK 3 T33: 0.0436 T12: -0.0050
REMARK 3 T13: 0.0107 T23: 0.0112
REMARK 3 L TENSOR
REMARK 3 L11: 1.4018 L22: 1.0238
REMARK 3 L33: 1.6226 L12: -0.3145
REMARK 3 L13: -0.3697 L23: -0.1626
REMARK 3 S TENSOR
REMARK 3 S11: -0.0589 S12: 0.0764 S13: -0.0778
REMARK 3 S21: -0.0365 S22: 0.0873 S23: 0.1074
REMARK 3 S31: 0.0659 S32: 0.0233 S33: -0.0284
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 259 A 266
REMARK 3 ORIGIN FOR THE GROUP (A): 16.4230 0.5340 66.3160
REMARK 3 T TENSOR
REMARK 3 T11: 0.2567 T22: 0.2010
REMARK 3 T33: 0.0442 T12: -0.0687
REMARK 3 T13: 0.0180 T23: 0.0509
REMARK 3 L TENSOR
REMARK 3 L11: 0.7426 L22: 57.8914
REMARK 3 L33: 27.3041 L12: -1.5482
REMARK 3 L13: 4.4694 L23: -12.9583
REMARK 3 S TENSOR
REMARK 3 S11: 0.1334 S12: -0.0403 S13: -0.0094
REMARK 3 S21: 0.0736 S22: -0.0635 S23: 0.5798
REMARK 3 S31: 0.9081 S32: -0.1514 S33: -0.0699
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 : B 0 B 14
REMARK 3 ORIGIN FOR THE GROUP (A): 19.6460 27.3230 4.1680
REMARK 3 T TENSOR
REMARK 3 T11: 0.2138 T22: 0.3674
REMARK 3 T33: 0.0445 T12: -0.0114
REMARK 3 T13: 0.0017 T23: 0.0604
REMARK 3 L TENSOR
REMARK 3 L11: 22.4299 L22: 4.0508
REMARK 3 L33: 2.9507 L12: 6.4726
REMARK 3 L13: 3.3891 L23: 2.5614
REMARK 3 S TENSOR
REMARK 3 S11: -0.2733 S12: 2.2731 S13: 0.2667
REMARK 3 S21: -0.4261 S22: 0.4229 S23: -0.0245
REMARK 3 S31: -0.5918 S32: 0.2682 S33: -0.1495
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 : B 15 B 116
REMARK 3 ORIGIN FOR THE GROUP (A): 24.1590 33.0410 14.6920
REMARK 3 T TENSOR
REMARK 3 T11: 0.1768 T22: 0.0612
REMARK 3 T33: 0.0347 T12: -0.0058
REMARK 3 T13: 0.0241 T23: 0.0217
REMARK 3 L TENSOR
REMARK 3 L11: 2.1026 L22: 1.4020
REMARK 3 L33: 3.1669 L12: -0.1677
REMARK 3 L13: 0.5711 L23: -0.2655
REMARK 3 S TENSOR
REMARK 3 S11: 0.0575 S12: 0.1123 S13: 0.1226
REMARK 3 S21: -0.1365 S22: 0.0175 S23: -0.0494
REMARK 3 S31: -0.5330 S32: 0.0044 S33: -0.0751
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 117 B 172
REMARK 3 ORIGIN FOR THE GROUP (A): 34.9870 22.5140 29.9960
REMARK 3 T TENSOR
REMARK 3 T11: 0.0942 T22: 0.1427
REMARK 3 T33: 0.0763 T12: -0.0372
REMARK 3 T13: 0.0057 T23: -0.0239
REMARK 3 L TENSOR
REMARK 3 L11: 1.1298 L22: 0.4410
REMARK 3 L33: 3.0282 L12: 0.4394
REMARK 3 L13: -0.2300 L23: -0.1335
REMARK 3 S TENSOR
REMARK 3 S11: 0.0315 S12: 0.0259 S13: -0.0350
REMARK 3 S21: -0.1093 S22: 0.0352 S23: -0.0814
REMARK 3 S31: -0.2174 S32: 0.4311 S33: -0.0668
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 173 B 198
REMARK 3 ORIGIN FOR THE GROUP (A): 30.2750 40.4370 23.3960
REMARK 3 T TENSOR
REMARK 3 T11: 0.4168 T22: 0.1250
REMARK 3 T33: 0.1115 T12: -0.1899
REMARK 3 T13: 0.0656 T23: -0.0204
REMARK 3 L TENSOR
REMARK 3 L11: 7.1798 L22: 1.9096
REMARK 3 L33: 2.7078 L12: -1.9345
REMARK 3 L13: -2.4575 L23: 1.0725
REMARK 3 S TENSOR
REMARK 3 S11: 0.1454 S12: -0.2798 S13: 0.7229
REMARK 3 S21: -0.0761 S22: 0.1588 S23: -0.1778
REMARK 3 S31: -0.8914 S32: 0.5310 S33: -0.3042
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 199 B 262
REMARK 3 ORIGIN FOR THE GROUP (A): 14.3350 29.4550 26.7560
REMARK 3 T TENSOR
REMARK 3 T11: 0.1179 T22: 0.1307
REMARK 3 T33: 0.0825 T12: 0.0570
REMARK 3 T13: 0.0121 T23: 0.0253
REMARK 3 L TENSOR
REMARK 3 L11: 1.0913 L22: 1.5746
REMARK 3 L33: 2.3355 L12: -0.1171
REMARK 3 L13: -0.0184 L23: -0.4076
REMARK 3 S TENSOR
REMARK 3 S11: 0.0783 S12: -0.0393 S13: 0.0109
REMARK 3 S21: -0.0659 S22: 0.0682 S23: 0.1462
REMARK 3 S31: -0.2444 S32: -0.4257 S33: -0.1465
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 : 1.20
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 3V48 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-DEC-11.
REMARK 100 THE RCSB ID CODE IS RCSB069574.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-NOV-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9787
REMARK 200 MONOCHROMATOR : C 111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31045
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 10.200
REMARK 200 R MERGE (I) : 0.35200
REMARK 200 R SYM (I) : 0.35200
REMARK 200 FOR THE DATA SET : 11.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: HKL-3000:SHELXC/D/E, MLPHARE, DM, ARP/WARP, SOLVE,
REMARK 200 RESOLVE, CCP4
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.15 M MALIC ACID 20% PEG 3350, PH
REMARK 280 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 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+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
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 80.87650
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 39.79850
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 39.79850
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 121.31475
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 39.79850
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 39.79850
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 40.43825
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 39.79850
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 39.79850
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 121.31475
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 39.79850
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 39.79850
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 40.43825
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 80.87650
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: 4570 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20090 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 B -1
REMARK 465 GLU B 263
REMARK 465 ALA B 264
REMARK 465 ALA B 265
REMARK 465 LEU B 266
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 ARG A 187 CZ NH1 NH2
REMARK 470 ARG B 187 CZ NH1 NH2
REMARK 470 ARG B 196 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 198 CG CD NE CZ NH1 NH2
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 53 56.63 -118.44
REMARK 500 ALA A 88 -115.02 55.65
REMARK 500 ALA A 238 51.27 -92.94
REMARK 500 ASN B 53 55.65 -118.87
REMARK 500 ALA B 88 -111.56 56.32
REMARK 500 ALA B 238 49.96 -92.38
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 GOL A 267
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 268
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN A 269
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN A 270
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 267
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 268
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN B 269
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: NYSGRC-490004 RELATED DB: TARGETDB
DBREF 3V48 A 1 266 UNP B6I985 RUTD_ECOSE 1 266
DBREF 3V48 B 1 266 UNP B6I985 RUTD_ECOSE 1 266
SEQADV 3V48 GLY A -1 UNP B6I985 EXPRESSION TAG
SEQADV 3V48 HIS A 0 UNP B6I985 EXPRESSION TAG
SEQADV 3V48 GLY B -1 UNP B6I985 EXPRESSION TAG
SEQADV 3V48 HIS B 0 UNP B6I985 EXPRESSION TAG
SEQRES 1 A 268 GLY HIS MSE LYS LEU SER LEU SER PRO PRO PRO TYR ALA
SEQRES 2 A 268 ASP ALA PRO VAL VAL VAL LEU ILE SER GLY LEU GLY GLY
SEQRES 3 A 268 SER GLY SER TYR TRP LEU PRO GLN LEU ALA VAL LEU GLU
SEQRES 4 A 268 GLN GLU TYR GLN VAL VAL CYS TYR ASP GLN ARG GLY THR
SEQRES 5 A 268 GLY ASN ASN PRO ASP THR LEU ALA GLU ASP TYR SER ILE
SEQRES 6 A 268 ALA GLN MSE ALA ALA GLU LEU HIS GLN ALA LEU VAL ALA
SEQRES 7 A 268 ALA GLY ILE GLU HIS TYR ALA VAL VAL GLY HIS ALA LEU
SEQRES 8 A 268 GLY ALA LEU VAL GLY MSE GLN LEU ALA LEU ASP TYR PRO
SEQRES 9 A 268 ALA SER VAL THR VAL LEU ILE SER VAL ASN GLY TRP LEU
SEQRES 10 A 268 ARG ILE ASN ALA HIS THR ARG ARG CYS PHE GLN VAL ARG
SEQRES 11 A 268 GLU ARG LEU LEU TYR SER GLY GLY ALA GLN ALA TRP VAL
SEQRES 12 A 268 GLU ALA GLN PRO LEU PHE LEU TYR PRO ALA ASP TRP MSE
SEQRES 13 A 268 ALA ALA ARG ALA PRO ARG LEU GLU ALA GLU ASP ALA LEU
SEQRES 14 A 268 ALA LEU ALA HIS PHE GLN GLY LYS ASN ASN LEU LEU ARG
SEQRES 15 A 268 ARG LEU ASN ALA LEU LYS ARG ALA ASP PHE SER HIS HIS
SEQRES 16 A 268 ALA ASP ARG ILE ARG CYS PRO VAL GLN ILE ILE CYS ALA
SEQRES 17 A 268 SER ASP ASP LEU LEU VAL PRO THR ALA CYS SER SER GLU
SEQRES 18 A 268 LEU HIS ALA ALA LEU PRO ASP SER GLN LYS MSE VAL MSE
SEQRES 19 A 268 PRO TYR GLY GLY HIS ALA CYS ASN VAL THR ASP PRO GLU
SEQRES 20 A 268 THR PHE ASN ALA LEU LEU LEU ASN GLY LEU ALA SER LEU
SEQRES 21 A 268 LEU HIS HIS ARG GLU ALA ALA LEU
SEQRES 1 B 268 GLY HIS MSE LYS LEU SER LEU SER PRO PRO PRO TYR ALA
SEQRES 2 B 268 ASP ALA PRO VAL VAL VAL LEU ILE SER GLY LEU GLY GLY
SEQRES 3 B 268 SER GLY SER TYR TRP LEU PRO GLN LEU ALA VAL LEU GLU
SEQRES 4 B 268 GLN GLU TYR GLN VAL VAL CYS TYR ASP GLN ARG GLY THR
SEQRES 5 B 268 GLY ASN ASN PRO ASP THR LEU ALA GLU ASP TYR SER ILE
SEQRES 6 B 268 ALA GLN MSE ALA ALA GLU LEU HIS GLN ALA LEU VAL ALA
SEQRES 7 B 268 ALA GLY ILE GLU HIS TYR ALA VAL VAL GLY HIS ALA LEU
SEQRES 8 B 268 GLY ALA LEU VAL GLY MSE GLN LEU ALA LEU ASP TYR PRO
SEQRES 9 B 268 ALA SER VAL THR VAL LEU ILE SER VAL ASN GLY TRP LEU
SEQRES 10 B 268 ARG ILE ASN ALA HIS THR ARG ARG CYS PHE GLN VAL ARG
SEQRES 11 B 268 GLU ARG LEU LEU TYR SER GLY GLY ALA GLN ALA TRP VAL
SEQRES 12 B 268 GLU ALA GLN PRO LEU PHE LEU TYR PRO ALA ASP TRP MSE
SEQRES 13 B 268 ALA ALA ARG ALA PRO ARG LEU GLU ALA GLU ASP ALA LEU
SEQRES 14 B 268 ALA LEU ALA HIS PHE GLN GLY LYS ASN ASN LEU LEU ARG
SEQRES 15 B 268 ARG LEU ASN ALA LEU LYS ARG ALA ASP PHE SER HIS HIS
SEQRES 16 B 268 ALA ASP ARG ILE ARG CYS PRO VAL GLN ILE ILE CYS ALA
SEQRES 17 B 268 SER ASP ASP LEU LEU VAL PRO THR ALA CYS SER SER GLU
SEQRES 18 B 268 LEU HIS ALA ALA LEU PRO ASP SER GLN LYS MSE VAL MSE
SEQRES 19 B 268 PRO TYR GLY GLY HIS ALA CYS ASN VAL THR ASP PRO GLU
SEQRES 20 B 268 THR PHE ASN ALA LEU LEU LEU ASN GLY LEU ALA SER LEU
SEQRES 21 B 268 LEU HIS HIS ARG GLU ALA ALA LEU
MODRES 3V48 MSE A 1 MET SELENOMETHIONINE
MODRES 3V48 MSE A 66 MET SELENOMETHIONINE
MODRES 3V48 MSE A 95 MET SELENOMETHIONINE
MODRES 3V48 MSE A 154 MET SELENOMETHIONINE
MODRES 3V48 MSE A 230 MET SELENOMETHIONINE
MODRES 3V48 MSE A 232 MET SELENOMETHIONINE
MODRES 3V48 MSE B 1 MET SELENOMETHIONINE
MODRES 3V48 MSE B 66 MET SELENOMETHIONINE
MODRES 3V48 MSE B 95 MET SELENOMETHIONINE
MODRES 3V48 MSE B 154 MET SELENOMETHIONINE
MODRES 3V48 MSE B 230 MET SELENOMETHIONINE
MODRES 3V48 MSE B 232 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 66 8
HET MSE A 95 8
HET MSE A 154 8
HET MSE A 230 8
HET MSE A 232 8
HET MSE B 1 8
HET MSE B 66 8
HET MSE B 95 8
HET MSE B 154 8
HET MSE B 230 8
HET MSE B 232 8
HET GOL A 267 6
HET GOL A 268 6
HET SCN A 269 3
HET SCN A 270 3
HET GOL B 267 6
HET GOL B 268 6
HET SCN B 269 3
HETNAM MSE SELENOMETHIONINE
HETNAM GOL GLYCEROL
HETNAM SCN THIOCYANATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MSE 12(C5 H11 N O2 SE)
FORMUL 3 GOL 4(C3 H8 O3)
FORMUL 5 SCN 3(C N S 1-)
FORMUL 10 HOH *313(H2 O)
HELIX 1 1 SER A 25 TYR A 28 5 4
HELIX 2 2 TRP A 29 GLN A 38 1 10
HELIX 3 3 SER A 62 ALA A 77 1 16
HELIX 4 4 ALA A 88 TYR A 101 1 14
HELIX 5 5 ASN A 118 TYR A 149 1 32
HELIX 6 6 PRO A 150 ALA A 156 1 7
HELIX 7 7 ARG A 157 HIS A 171 1 15
HELIX 8 8 GLY A 174 ALA A 188 1 15
HELIX 9 9 HIS A 193 ILE A 197 5 5
HELIX 10 10 THR A 214 LEU A 224 1 11
HELIX 11 11 ALA A 238 ASP A 243 1 6
HELIX 12 12 ASP A 243 LEU A 266 1 24
HELIX 13 13 SER B 25 TYR B 28 5 4
HELIX 14 14 TRP B 29 GLN B 38 1 10
HELIX 15 15 SER B 62 ALA B 77 1 16
HELIX 16 16 ALA B 88 TYR B 101 1 14
HELIX 17 17 ASN B 118 GLN B 144 1 27
HELIX 18 18 PRO B 145 LEU B 148 5 4
HELIX 19 19 PRO B 150 ALA B 156 1 7
HELIX 20 20 ARG B 157 HIS B 171 1 15
HELIX 21 21 GLY B 174 ALA B 188 1 15
HELIX 22 22 HIS B 193 ILE B 197 5 5
HELIX 23 23 THR B 214 LEU B 224 1 11
HELIX 24 24 ALA B 238 ASP B 243 1 6
HELIX 25 25 ASP B 243 HIS B 261 1 19
SHEET 1 A 7 SER A 4 LEU A 5 0
SHEET 2 A 7 GLN A 41 CYS A 44 -1 O CYS A 44 N SER A 4
SHEET 3 A 7 VAL A 15 ILE A 19 1 N LEU A 18 O VAL A 43
SHEET 4 A 7 TYR A 82 HIS A 87 1 O VAL A 85 N ILE A 19
SHEET 5 A 7 VAL A 105 VAL A 111 1 O ILE A 109 N GLY A 86
SHEET 6 A 7 VAL A 201 ALA A 206 1 O ILE A 204 N SER A 110
SHEET 7 A 7 SER A 227 MSE A 232 1 O MSE A 232 N CYS A 205
SHEET 1 B 7 SER B 4 LEU B 5 0
SHEET 2 B 7 GLN B 41 CYS B 44 -1 O CYS B 44 N SER B 4
SHEET 3 B 7 VAL B 15 ILE B 19 1 N LEU B 18 O VAL B 43
SHEET 4 B 7 TYR B 82 HIS B 87 1 O ALA B 83 N VAL B 17
SHEET 5 B 7 VAL B 105 VAL B 111 1 O VAL B 111 N GLY B 86
SHEET 6 B 7 VAL B 201 ALA B 206 1 O ILE B 204 N SER B 110
SHEET 7 B 7 SER B 227 MSE B 232 1 O MSE B 232 N CYS B 205
LINK C HIS A 0 N MSE A 1 1555 1555 1.33
LINK C MSE A 1 N LYS A 2 1555 1555 1.33
LINK C GLN A 65 N MSE A 66 1555 1555 1.33
LINK C MSE A 66 N ALA A 67 1555 1555 1.32
LINK C GLY A 94 N MSE A 95 1555 1555 1.33
LINK C MSE A 95 N GLN A 96 1555 1555 1.32
LINK C TRP A 153 N MSE A 154 1555 1555 1.32
LINK C MSE A 154 N ALA A 155 1555 1555 1.32
LINK C LYS A 229 N MSE A 230 1555 1555 1.33
LINK C MSE A 230 N VAL A 231 1555 1555 1.31
LINK C VAL A 231 N MSE A 232 1555 1555 1.32
LINK C MSE A 232 N PRO A 233 1555 1555 1.35
LINK C HIS B 0 N MSE B 1 1555 1555 1.32
LINK C MSE B 1 N LYS B 2 1555 1555 1.35
LINK C GLN B 65 N MSE B 66 1555 1555 1.33
LINK C MSE B 66 N ALA B 67 1555 1555 1.32
LINK C GLY B 94 N MSE B 95 1555 1555 1.33
LINK C MSE B 95 N GLN B 96 1555 1555 1.33
LINK C TRP B 153 N MSE B 154 1555 1555 1.33
LINK C MSE B 154 N ALA B 155 1555 1555 1.31
LINK C LYS B 229 N MSE B 230 1555 1555 1.33
LINK C MSE B 230 N VAL B 231 1555 1555 1.33
LINK C VAL B 231 N MSE B 232 1555 1555 1.33
LINK C MSE B 232 N PRO B 233 1555 1555 1.34
SITE 1 AC1 7 GLY A 23 HIS A 87 LEU A 148 SCN A 270
SITE 2 AC1 7 HOH A 296 HOH A 349 HOH A 407
SITE 1 AC2 9 MSE A 154 ALA A 155 ALA A 158 LEU A 161
SITE 2 AC2 9 HOH A 357 HOH A 415 HIS B 120 ARG B 123
SITE 3 AC2 9 HOH B 449
SITE 1 AC3 5 GLY A 23 ARG A 128 TRP A 140 GLN A 144
SITE 2 AC3 5 HOH A 294
SITE 1 AC4 8 LEU A 22 ALA A 88 LEU A 89 LEU A 185
SITE 2 AC4 8 LEU A 211 HIS A 237 GOL A 267 HOH A 294
SITE 1 AC5 7 GLY B 21 LEU B 22 GLY B 23 HIS B 87
SITE 2 AC5 7 HOH B 270 HOH B 283 HOH B 416
SITE 1 AC6 5 HIS A 120 ARG A 123 MSE B 154 ALA B 155
SITE 2 AC6 5 ALA B 158
SITE 1 AC7 5 HIS A 0 ARG A 48 ARG B 157 PRO B 159
SITE 2 AC7 5 ARG B 160
CRYST1 79.597 79.597 161.753 90.00 90.00 90.00 P 43 21 2 16
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.012563 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012563 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006182 0.00000
TER 2053 LEU A 266
TER 4062 ARG B 262
MASTER 507 0 19 25 14 0 15 6 4390 2 153 42
END |