HEADER HYDROLASE INHIBITOR/HYDROLASE 26-AUG-09 3ISM
TITLE CRYSTAL STRUCTURE OF THE ENDOG/ENDOGI COMPLEX: MECHANISM OF ENDOG
TITLE 2 INHIBITION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CG8862;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 56-310;
COMPND 5 SYNONYM: ENDONUCLEASE G, ENDOG, LD35517P;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: CG4930;
COMPND 9 CHAIN: C;
COMPND 10 SYNONYM: ENDOGI, SD16985P;
COMPND 11 EC: 3.6.1.3;
COMPND 12 ENGINEERED: YES;
COMPND 13 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 3 ORGANISM_COMMON: FRUIT FLY;
SOURCE 4 ORGANISM_TAXID: 7227;
SOURCE 5 GENE: CG8862, DMEL_CG8862, ENDOG;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: C43(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21D;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 13 ORGANISM_COMMON: FRUIT FLY;
SOURCE 14 ORGANISM_TAXID: 7227;
SOURCE 15 GENE: ENDOGI, BG:DS07473.2, CG4930, DMEL_CG4930;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: C43(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET21D
KEYWDS ENDONUCLEASE, ENDONUCLEASE INHIBITOR COMPLEX, METAL COMPLEX,
KEYWDS 2 HYDROLASE, HYDROLASE INHIBITOR-HYDROLASE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR B.LOLL,M.GEBHARDT,E.WAHLE,A.MEINHART
REVDAT 5 01-NOV-23 3ISM 1 REMARK
REVDAT 4 10-NOV-21 3ISM 1 REMARK SEQADV LINK
REVDAT 3 13-JUL-11 3ISM 1 VERSN
REVDAT 2 02-FEB-11 3ISM 1 JRNL
REVDAT 1 08-SEP-09 3ISM 0
JRNL AUTH B.LOLL,M.GEBHARDT,E.WAHLE,A.MEINHART
JRNL TITL CRYSTAL STRUCTURE OF THE ENDOG/ENDOGI COMPLEX: MECHANISM OF
JRNL TITL 2 ENDOG INHIBITION.
JRNL REF NUCLEIC ACIDS RES. V. 37 7312 2009
JRNL REFN ISSN 0305-1048
JRNL PMID 19783821
JRNL DOI 10.1093/NAR/GKP770
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.23
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 45828
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) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2412
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3325
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2010
REMARK 3 BIN FREE R VALUE SET COUNT : 175
REMARK 3 BIN FREE R VALUE : 0.2310
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6299
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 328
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 38.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.91000
REMARK 3 B22 (A**2) : 0.37000
REMARK 3 B33 (A**2) : 0.54000
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): 0.248
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.192
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.128
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.380
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.946
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.926
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6611 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8994 ; 1.150 ; 1.941
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 818 ; 5.896 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 351 ;31.428 ;23.761
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1112 ;14.109 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 51 ;18.608 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 951 ; 0.086 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5184 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2975 ; 0.179 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4472 ; 0.304 ; 0.500
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 757 ; 0.167 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 2 ; 0.074 ; 0.500
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 41 ; 0.150 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 27 ; 0.236 ; 0.500
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): 4066 ; 0.533 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6429 ; 0.878 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2900 ; 1.378 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2542 ; 2.030 ; 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 : 6
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 67 A 90
REMARK 3 RESIDUE RANGE : B 65 B 90
REMARK 3 ORIGIN FOR THE GROUP (A): -36.6570 -37.5862 9.7591
REMARK 3 T TENSOR
REMARK 3 T11: -0.1299 T22: 0.0335
REMARK 3 T33: -0.0347 T12: -0.0248
REMARK 3 T13: -0.0231 T23: -0.0005
REMARK 3 L TENSOR
REMARK 3 L11: 0.8226 L22: 2.4607
REMARK 3 L33: 3.9245 L12: -0.1361
REMARK 3 L13: -0.1889 L23: -3.0449
REMARK 3 S TENSOR
REMARK 3 S11: 0.0391 S12: -0.1066 S13: -0.0711
REMARK 3 S21: -0.1113 S22: -0.0320 S23: 0.4865
REMARK 3 S31: 0.3028 S32: -0.0162 S33: -0.0071
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 91 A 311
REMARK 3 RESIDUE RANGE : B 91 B 311
REMARK 3 ORIGIN FOR THE GROUP (A): -21.9544 -37.8831 13.8288
REMARK 3 T TENSOR
REMARK 3 T11: -0.2317 T22: -0.1255
REMARK 3 T33: -0.1951 T12: -0.0005
REMARK 3 T13: -0.0163 T23: -0.0144
REMARK 3 L TENSOR
REMARK 3 L11: 0.8963 L22: 2.1689
REMARK 3 L33: 1.2657 L12: 0.4545
REMARK 3 L13: -0.2030 L23: -0.6744
REMARK 3 S TENSOR
REMARK 3 S11: -0.0022 S12: -0.0461 S13: -0.0495
REMARK 3 S21: 0.0373 S22: 0.0387 S23: 0.0114
REMARK 3 S31: 0.1234 S32: -0.0621 S33: -0.0365
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 : C 21 C 48
REMARK 3 ORIGIN FOR THE GROUP (A): -13.4390 -8.6385 38.5849
REMARK 3 T TENSOR
REMARK 3 T11: 0.0228 T22: 0.0331
REMARK 3 T33: 0.0151 T12: -0.0316
REMARK 3 T13: 0.0411 T23: 0.0270
REMARK 3 L TENSOR
REMARK 3 L11: 12.1000 L22: 11.6546
REMARK 3 L33: 9.1676 L12: 6.9412
REMARK 3 L13: 1.3458 L23: 1.0511
REMARK 3 S TENSOR
REMARK 3 S11: 0.4222 S12: -0.8898 S13: -0.4457
REMARK 3 S21: 0.8194 S22: -0.4351 S23: 0.4712
REMARK 3 S31: 0.4476 S32: -0.5885 S33: 0.0129
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 : C 49 C 174
REMARK 3 ORIGIN FOR THE GROUP (A): -6.3314 0.0046 23.1348
REMARK 3 T TENSOR
REMARK 3 T11: -0.0569 T22: -0.0918
REMARK 3 T33: -0.0467 T12: 0.0018
REMARK 3 T13: 0.0166 T23: -0.0311
REMARK 3 L TENSOR
REMARK 3 L11: 1.7572 L22: 2.2423
REMARK 3 L33: 1.8696 L12: 0.9993
REMARK 3 L13: 0.1975 L23: 0.1852
REMARK 3 S TENSOR
REMARK 3 S11: -0.0809 S12: 0.0278 S13: 0.0910
REMARK 3 S21: -0.1321 S22: 0.0726 S23: -0.1112
REMARK 3 S31: -0.2346 S32: 0.1284 S33: 0.0083
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 : C 219 C 274
REMARK 3 ORIGIN FOR THE GROUP (A): -8.3325 -75.1461 -0.3549
REMARK 3 T TENSOR
REMARK 3 T11: 0.2486 T22: 0.1945
REMARK 3 T33: 0.1520 T12: 0.0021
REMARK 3 T13: 0.0313 T23: -0.0471
REMARK 3 L TENSOR
REMARK 3 L11: 11.3852 L22: 26.3459
REMARK 3 L33: 14.7836 L12: -10.0861
REMARK 3 L13: 4.5175 L23: -4.5964
REMARK 3 S TENSOR
REMARK 3 S11: -0.0948 S12: 0.3209 S13: 0.0997
REMARK 3 S21: -0.5330 S22: -0.3902 S23: -0.7682
REMARK 3 S31: -0.5427 S32: 0.0560 S33: 0.4850
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 : C 275 C 354
REMARK 3 ORIGIN FOR THE GROUP (A): -12.1249 -79.3061 14.9819
REMARK 3 T TENSOR
REMARK 3 T11: 0.2398 T22: 0.0747
REMARK 3 T33: 0.1781 T12: -0.0619
REMARK 3 T13: -0.0635 T23: 0.0739
REMARK 3 L TENSOR
REMARK 3 L11: 2.1324 L22: 12.5569
REMARK 3 L33: 2.9862 L12: -2.4272
REMARK 3 L13: 1.1477 L23: 1.6759
REMARK 3 S TENSOR
REMARK 3 S11: 0.1757 S12: -0.1067 S13: -0.2258
REMARK 3 S21: 0.2185 S22: 0.0229 S23: -0.2127
REMARK 3 S31: 0.5108 S32: -0.2280 S33: -0.1986
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: NULL
REMARK 4
REMARK 4 3ISM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-AUG-09.
REMARK 100 THE DEPOSITION ID IS D_1000054814.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-APR-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0075
REMARK 200 MONOCHROMATOR : SI(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 : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46364
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 43.230
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.18400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.5
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.20100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.200
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: 2O3B
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20%(W/V)PEG 2000 MME, PH 8.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 277K
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 35.39500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 60.54000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.57500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 60.54000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.39500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.57500
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 55
REMARK 465 LEU A 56
REMARK 465 ILE A 57
REMARK 465 PRO A 58
REMARK 465 ALA A 59
REMARK 465 GLN A 60
REMARK 465 GLU A 61
REMARK 465 ASN A 62
REMARK 465 ASN A 63
REMARK 465 VAL A 64
REMARK 465 SER A 65
REMARK 465 LEU A 66
REMARK 465 ALA A 312
REMARK 465 ALA A 313
REMARK 465 LEU A 314
REMARK 465 GLU A 315
REMARK 465 HIS A 316
REMARK 465 HIS A 317
REMARK 465 HIS A 318
REMARK 465 HIS A 319
REMARK 465 HIS A 320
REMARK 465 HIS A 321
REMARK 465 MET B 55
REMARK 465 LEU B 56
REMARK 465 ILE B 57
REMARK 465 PRO B 58
REMARK 465 ALA B 59
REMARK 465 GLN B 60
REMARK 465 GLU B 61
REMARK 465 ASN B 62
REMARK 465 ASN B 63
REMARK 465 VAL B 64
REMARK 465 ALA B 312
REMARK 465 ALA B 313
REMARK 465 LEU B 314
REMARK 465 GLU B 315
REMARK 465 HIS B 316
REMARK 465 HIS B 317
REMARK 465 HIS B 318
REMARK 465 HIS B 319
REMARK 465 HIS B 320
REMARK 465 HIS B 321
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 LYS C 3
REMARK 465 ARG C 4
REMARK 465 LYS C 5
REMARK 465 ALA C 6
REMARK 465 GLU C 7
REMARK 465 ASP C 8
REMARK 465 THR C 9
REMARK 465 GLN C 10
REMARK 465 SER C 11
REMARK 465 ASP C 12
REMARK 465 LYS C 13
REMARK 465 MET C 14
REMARK 465 ALA C 15
REMARK 465 THR C 16
REMARK 465 ALA C 17
REMARK 465 GLU C 18
REMARK 465 LYS C 19
REMARK 465 VAL C 20
REMARK 465 ALA C 175
REMARK 465 ALA C 176
REMARK 465 LEU C 177
REMARK 465 GLU C 178
REMARK 465 GLU C 179
REMARK 465 GLN C 180
REMARK 465 ALA C 181
REMARK 465 SER C 182
REMARK 465 LEU C 183
REMARK 465 ASP C 184
REMARK 465 GLN C 185
REMARK 465 ASP C 186
REMARK 465 GLY C 187
REMARK 465 PRO C 188
REMARK 465 ALA C 189
REMARK 465 THR C 190
REMARK 465 PRO C 191
REMARK 465 THR C 192
REMARK 465 THR C 193
REMARK 465 PRO C 194
REMARK 465 GLY C 195
REMARK 465 GLU C 196
REMARK 465 LEU C 197
REMARK 465 SER C 198
REMARK 465 ALA C 199
REMARK 465 ASP C 200
REMARK 465 ASP C 201
REMARK 465 ALA C 202
REMARK 465 ALA C 203
REMARK 465 ALA C 204
REMARK 465 LEU C 205
REMARK 465 SER C 206
REMARK 465 GLY C 207
REMARK 465 GLU C 208
REMARK 465 PHE C 209
REMARK 465 GLU C 210
REMARK 465 ALA C 211
REMARK 465 THR C 212
REMARK 465 LEU C 213
REMARK 465 THR C 214
REMARK 465 LYS C 215
REMARK 465 GLU C 216
REMARK 465 ASN C 217
REMARK 465 PRO C 218
REMARK 465 LEU C 231
REMARK 465 THR C 232
REMARK 465 LYS C 233
REMARK 465 GLY C 354
REMARK 465 PRO C 355
REMARK 465 VAL C 356
REMARK 465 ASN C 357
REMARK 465 ASP C 358
REMARK 465 ASP C 359
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 PHE A 186 -94.31 -147.15
REMARK 500 ASP A 189 -100.57 -131.45
REMARK 500 ASP A 222 -31.73 -37.29
REMARK 500 MET B 77 30.71 -94.08
REMARK 500 ASP B 92 11.76 -145.22
REMARK 500 PHE B 186 -91.11 -153.52
REMARK 500 ASP B 189 -102.65 -129.58
REMARK 500 ASP C 103 74.00 -166.24
REMARK 500 VAL C 130 -69.57 -103.90
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 MG A 1 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 2 O
REMARK 620 2 HOH A 3 O 97.4
REMARK 620 3 HOH A 4 O 164.6 97.6
REMARK 620 4 HOH A 5 O 91.0 86.9 86.4
REMARK 620 5 HOH A 6 O 84.5 178.1 80.5 92.7
REMARK 620 6 ASN A 187 OD1 99.3 86.4 85.1 168.4 93.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 1 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 2 O
REMARK 620 2 HOH B 3 O 101.3
REMARK 620 3 HOH B 4 O 166.4 88.7
REMARK 620 4 HOH B 5 O 99.7 89.3 89.6
REMARK 620 5 ASN B 187 OD1 87.9 77.3 85.2 165.7
REMARK 620 6 HOH C 360 O 85.1 172.7 84.5 93.1 99.6
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A 6989
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2O3B RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE COMPLEX OF NUCLEASE A (NUCA) WITH INTRA-CELLULAR
REMARK 900 INHIBITOR NUIA
REMARK 900 RELATED ID: 1ZM8 RELATED DB: PDB
REMARK 900 APO CRYSTAL STRUCTURE OF NUCLEASE A FROM ANABAENA SP.
REMARK 900 RELATED ID: 1QAE RELATED DB: PDB
REMARK 900 THE ACTIVE SITE OF SERRATIA ENDONUCLEASE CONTAINS A CONSERVED
REMARK 900 MAGNESIUM-WATER CLUSTER
DBREF 3ISM A 56 310 UNP Q7JXB9 Q7JXB9_DROME 56 310
DBREF 3ISM B 56 310 UNP Q7JXB9 Q7JXB9_DROME 56 310
DBREF 3ISM C 1 359 UNP Q9V3V9 Q9V3V9_DROME 1 359
SEQADV 3ISM MET A 55 UNP Q7JXB9 INITIATING METHIONINE
SEQADV 3ISM ALA A 311 UNP Q7JXB9 EXPRESSION TAG
SEQADV 3ISM ALA A 312 UNP Q7JXB9 EXPRESSION TAG
SEQADV 3ISM ALA A 313 UNP Q7JXB9 EXPRESSION TAG
SEQADV 3ISM LEU A 314 UNP Q7JXB9 EXPRESSION TAG
SEQADV 3ISM GLU A 315 UNP Q7JXB9 EXPRESSION TAG
SEQADV 3ISM HIS A 316 UNP Q7JXB9 EXPRESSION TAG
SEQADV 3ISM HIS A 317 UNP Q7JXB9 EXPRESSION TAG
SEQADV 3ISM HIS A 318 UNP Q7JXB9 EXPRESSION TAG
SEQADV 3ISM HIS A 319 UNP Q7JXB9 EXPRESSION TAG
SEQADV 3ISM HIS A 320 UNP Q7JXB9 EXPRESSION TAG
SEQADV 3ISM HIS A 321 UNP Q7JXB9 EXPRESSION TAG
SEQADV 3ISM MET B 55 UNP Q7JXB9 INITIATING METHIONINE
SEQADV 3ISM ALA B 311 UNP Q7JXB9 EXPRESSION TAG
SEQADV 3ISM ALA B 312 UNP Q7JXB9 EXPRESSION TAG
SEQADV 3ISM ALA B 313 UNP Q7JXB9 EXPRESSION TAG
SEQADV 3ISM LEU B 314 UNP Q7JXB9 EXPRESSION TAG
SEQADV 3ISM GLU B 315 UNP Q7JXB9 EXPRESSION TAG
SEQADV 3ISM HIS B 316 UNP Q7JXB9 EXPRESSION TAG
SEQADV 3ISM HIS B 317 UNP Q7JXB9 EXPRESSION TAG
SEQADV 3ISM HIS B 318 UNP Q7JXB9 EXPRESSION TAG
SEQADV 3ISM HIS B 319 UNP Q7JXB9 EXPRESSION TAG
SEQADV 3ISM HIS B 320 UNP Q7JXB9 EXPRESSION TAG
SEQADV 3ISM HIS B 321 UNP Q7JXB9 EXPRESSION TAG
SEQADV 3ISM ALA C 2 UNP Q9V3V9 SER 2 ENGINEERED MUTATION
SEQRES 1 A 267 MET LEU ILE PRO ALA GLN GLU ASN ASN VAL SER LEU THR
SEQRES 2 A 267 ALA THR PRO SER ARG ILE GLY GLN ILE MET LYS TYR GLY
SEQRES 3 A 267 PHE PRO GLY LEU ASP HIS VAL ARG SER HIS SER ASP TYR
SEQRES 4 A 267 VAL LEU SER TYR ASP ARG ARG ASN ARG VAL PRO HIS TRP
SEQRES 5 A 267 VAL PHE GLU HIS LEU THR ALA GLU SER VAL ALA LYS ASN
SEQRES 6 A 267 ASP ALA VAL ASP ARG SER LYS CYS ASP PHE LYS GLN ASP
SEQRES 7 A 267 GLU SER ILE HIS PRO PHE PHE ARG SER GLN ASN THR ASP
SEQRES 8 A 267 TYR ARG ARG SER GLY TYR ASP ARG GLY HIS MET ALA ALA
SEQRES 9 A 267 ALA GLY ASN HIS ARG LEU HIS GLN LYS HIS CYS ASP GLU
SEQRES 10 A 267 THR PHE TYR LEU SER ASN MET ALA PRO GLN VAL GLY GLN
SEQRES 11 A 267 GLY PHE ASN ARG ASP ALA TRP ASN THR LEU GLU ALA HIS
SEQRES 12 A 267 VAL ARG ARG LEU THR LYS THR TYR SER ASN VAL TYR VAL
SEQRES 13 A 267 CYS THR GLY PRO LEU TYR LEU PRO HIS LYS GLU ASP ASP
SEQRES 14 A 267 GLY LYS SER TYR VAL LYS TYR GLU VAL ILE GLY ALA ASN
SEQRES 15 A 267 THR VAL ALA VAL PRO THR HIS PHE TYR LYS VAL ILE VAL
SEQRES 16 A 267 GLY GLU SER ALA ASP HIS LYS LEU HIS MET GLU SER TYR
SEQRES 17 A 267 VAL MET PRO ASN GLN VAL ILE SER ASN ASP THR PRO ILE
SEQRES 18 A 267 SER VAL PHE GLN VAL PRO PRO GLU SER VAL GLU ARG SER
SEQRES 19 A 267 ALA GLY LEU LEU PHE PHE ASP GLN ILE ASN ARG LYS GLN
SEQRES 20 A 267 LEU THR THR ILE ASN GLY LYS LYS VAL ALA ALA ALA LEU
SEQRES 21 A 267 GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 267 MET LEU ILE PRO ALA GLN GLU ASN ASN VAL SER LEU THR
SEQRES 2 B 267 ALA THR PRO SER ARG ILE GLY GLN ILE MET LYS TYR GLY
SEQRES 3 B 267 PHE PRO GLY LEU ASP HIS VAL ARG SER HIS SER ASP TYR
SEQRES 4 B 267 VAL LEU SER TYR ASP ARG ARG ASN ARG VAL PRO HIS TRP
SEQRES 5 B 267 VAL PHE GLU HIS LEU THR ALA GLU SER VAL ALA LYS ASN
SEQRES 6 B 267 ASP ALA VAL ASP ARG SER LYS CYS ASP PHE LYS GLN ASP
SEQRES 7 B 267 GLU SER ILE HIS PRO PHE PHE ARG SER GLN ASN THR ASP
SEQRES 8 B 267 TYR ARG ARG SER GLY TYR ASP ARG GLY HIS MET ALA ALA
SEQRES 9 B 267 ALA GLY ASN HIS ARG LEU HIS GLN LYS HIS CYS ASP GLU
SEQRES 10 B 267 THR PHE TYR LEU SER ASN MET ALA PRO GLN VAL GLY GLN
SEQRES 11 B 267 GLY PHE ASN ARG ASP ALA TRP ASN THR LEU GLU ALA HIS
SEQRES 12 B 267 VAL ARG ARG LEU THR LYS THR TYR SER ASN VAL TYR VAL
SEQRES 13 B 267 CYS THR GLY PRO LEU TYR LEU PRO HIS LYS GLU ASP ASP
SEQRES 14 B 267 GLY LYS SER TYR VAL LYS TYR GLU VAL ILE GLY ALA ASN
SEQRES 15 B 267 THR VAL ALA VAL PRO THR HIS PHE TYR LYS VAL ILE VAL
SEQRES 16 B 267 GLY GLU SER ALA ASP HIS LYS LEU HIS MET GLU SER TYR
SEQRES 17 B 267 VAL MET PRO ASN GLN VAL ILE SER ASN ASP THR PRO ILE
SEQRES 18 B 267 SER VAL PHE GLN VAL PRO PRO GLU SER VAL GLU ARG SER
SEQRES 19 B 267 ALA GLY LEU LEU PHE PHE ASP GLN ILE ASN ARG LYS GLN
SEQRES 20 B 267 LEU THR THR ILE ASN GLY LYS LYS VAL ALA ALA ALA LEU
SEQRES 21 B 267 GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 C 359 MET ALA LYS ARG LYS ALA GLU ASP THR GLN SER ASP LYS
SEQRES 2 C 359 MET ALA THR ALA GLU LYS VAL ALA GLN ASN ASP TYR THR
SEQRES 3 C 359 ILE GLY LEU VAL ASP PRO VAL LYS ASP TYR GLN LYS LEU
SEQRES 4 C 359 ILE GLU THR ARG VAL GLN VAL ASP GLU ILE VAL ASP ASP
SEQRES 5 C 359 ASP VAL THR LYS GLU ASN PHE ASP ARG THR ALA ALA ALA
SEQRES 6 C 359 ALA ARG ASP VAL ILE TRP ARG LEU LEU PHE ASP GLU ALA
SEQRES 7 C 359 GLY THR SER GLN SER ASN THR GLU LYS ALA SER GLN LEU
SEQRES 8 C 359 LEU GLU GLU TYR ARG GLY ASP ALA CYS PHE TYR ASP PRO
SEQRES 9 C 359 THR PRO TYR ASN GLU TRP ILE VAL LYS LEU ARG ASP GLU
SEQRES 10 C 359 VAL LEU LYS LYS GLU LEU LEU ASP PHE TRP ARG ASP VAL
SEQRES 11 C 359 LEU VAL LYS LYS GLN LEU GLY PRO CYS TRP SER ARG ASP
SEQRES 12 C 359 SER ASP LEU PHE ASP SER ASP ASP THR PRO PRO LEU GLU
SEQRES 13 C 359 PHE TYR ALA HIS ALA GLY CYS THR ALA PRO PHE ALA ALA
SEQRES 14 C 359 SER LEU LYS VAL ARG ALA ALA LEU GLU GLU GLN ALA SER
SEQRES 15 C 359 LEU ASP GLN ASP GLY PRO ALA THR PRO THR THR PRO GLY
SEQRES 16 C 359 GLU LEU SER ALA ASP ASP ALA ALA ALA LEU SER GLY GLU
SEQRES 17 C 359 PHE GLU ALA THR LEU THR LYS GLU ASN PRO LEU GLU GLU
SEQRES 18 C 359 TYR ARG THR LEU MET LYS ARG PHE VAL LEU THR LYS ILE
SEQRES 19 C 359 ILE VAL PRO ASP SER VAL HIS GLN ALA SER VAL LYS LYS
SEQRES 20 C 359 ILE ALA ALA ALA ALA ARG GLU ILE ILE TRP LYS LEU LEU
SEQRES 21 C 359 PHE ASP GLY THR PRO SER ALA GLU ASP GLN ASN LYS ALA
SEQRES 22 C 359 ALA GLU LEU LEU GLN GLU TYR LYS GLY ASP ALA GLY PHE
SEQRES 23 C 359 TYR GLY PRO ASP ASP TYR ASN SER TRP ILE PHE ASN LEU
SEQRES 24 C 359 ARG ASP GLU VAL LEU THR LYS GLU LEU LEU ASP PHE TRP
SEQRES 25 C 359 ARG ASP LYS MET VAL LYS MET GLU LEU GLY PRO SER CYS
SEQRES 26 C 359 ALA ARG ASP SER ASP TYR TYR ASP ASN GLU ASP PRO LEU
SEQRES 27 C 359 PRO PHE GLU PHE TYR GLU LYS ALA GLY CYS LYS ALA PRO
SEQRES 28 C 359 PHE GLU GLY PRO VAL ASN ASP ASP
HET MG A 1 1
HET TRS A6989 8
HET MG B 1 1
HETNAM MG MAGNESIUM ION
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETSYN TRS TRIS BUFFER
FORMUL 4 MG 2(MG 2+)
FORMUL 5 TRS C4 H12 N O3 1+
FORMUL 7 HOH *328(H2 O)
HELIX 1 1 SER A 71 MET A 77 1 7
HELIX 2 2 ASP A 123 CYS A 127 5 5
HELIX 3 3 HIS A 136 ARG A 140 5 5
HELIX 4 4 GLN A 142 ARG A 147 1 6
HELIX 5 5 ALA A 158 HIS A 162 5 5
HELIX 6 6 HIS A 165 GLU A 171 1 7
HELIX 7 7 THR A 172 SER A 176 5 5
HELIX 8 8 ASP A 189 LEU A 201 1 13
HELIX 9 9 THR A 202 THR A 204 5 3
HELIX 10 10 PRO A 274 GLN A 279 5 6
HELIX 11 11 PRO A 281 GLY A 290 1 10
HELIX 12 12 THR B 69 MET B 77 1 9
HELIX 13 13 THR B 112 ALA B 117 1 6
HELIX 14 14 ASP B 123 CYS B 127 5 5
HELIX 15 15 HIS B 136 ARG B 140 5 5
HELIX 16 16 GLN B 142 ARG B 147 1 6
HELIX 17 17 ALA B 158 HIS B 162 5 5
HELIX 18 18 HIS B 165 GLU B 171 1 7
HELIX 19 19 THR B 172 SER B 176 5 5
HELIX 20 20 ASP B 189 LEU B 201 1 13
HELIX 21 21 THR B 202 THR B 204 5 3
HELIX 22 22 PRO B 274 GLN B 279 5 6
HELIX 23 23 PRO B 281 GLY B 290 1 10
HELIX 24 24 ASN B 298 LEU B 302 5 5
HELIX 25 25 ASP C 31 VAL C 44 1 14
HELIX 26 26 ASP C 51 ASP C 76 1 26
HELIX 27 27 THR C 80 ASP C 103 1 24
HELIX 28 28 ASP C 103 LYS C 121 1 19
HELIX 29 29 LEU C 123 VAL C 130 1 8
HELIX 30 30 LEU C 155 ALA C 159 5 5
HELIX 31 31 PHE C 167 ARG C 174 1 8
HELIX 32 32 LEU C 219 VAL C 230 1 12
HELIX 33 33 PRO C 237 ASP C 262 1 26
HELIX 34 34 SER C 266 GLY C 288 1 23
HELIX 35 35 PRO C 289 LYS C 306 1 18
HELIX 36 36 LEU C 308 LYS C 315 1 8
HELIX 37 37 PRO C 339 GLU C 344 1 6
SHEET 1 A 8 VAL A 87 SER A 89 0
SHEET 2 A 8 VAL A 94 ASP A 98 -1 O LEU A 95 N ARG A 88
SHEET 3 A 8 VAL A 103 LEU A 111 -1 O TRP A 106 N SER A 96
SHEET 4 A 8 ASN A 207 LEU A 215 -1 O VAL A 208 N LEU A 111
SHEET 5 A 8 HIS A 243 GLU A 251 -1 O VAL A 249 N TYR A 209
SHEET 6 A 8 LEU A 257 PRO A 265 -1 O GLU A 260 N ILE A 248
SHEET 7 A 8 THR A 304 ILE A 305 1 O THR A 304 N MET A 259
SHEET 8 A 8 LYS A 308 LYS A 309 -1 O LYS A 308 N ILE A 305
SHEET 1 B 2 ASP A 152 HIS A 155 0
SHEET 2 B 2 MET A 178 GLN A 181 -1 O GLN A 181 N ASP A 152
SHEET 1 C 4 PRO A 218 LYS A 220 0
SHEET 2 C 4 SER A 226 ILE A 233 -1 O TYR A 227 N HIS A 219
SHEET 3 C 4 SER B 226 ILE B 233 -1 O VAL B 228 N TYR A 230
SHEET 4 C 4 HIS B 219 LYS B 220 -1 N HIS B 219 O TYR B 227
SHEET 1 D 4 VAL A 238 ALA A 239 0
SHEET 2 D 4 SER A 226 ILE A 233 -1 N ILE A 233 O VAL A 238
SHEET 3 D 4 SER B 226 ILE B 233 -1 O VAL B 228 N TYR A 230
SHEET 4 D 4 VAL B 238 ALA B 239 -1 O VAL B 238 N ILE B 233
SHEET 1 E 8 VAL B 87 SER B 89 0
SHEET 2 E 8 VAL B 94 ASP B 98 -1 O LEU B 95 N ARG B 88
SHEET 3 E 8 VAL B 103 LEU B 111 -1 O HIS B 105 N SER B 96
SHEET 4 E 8 ASN B 207 LEU B 215 -1 O VAL B 208 N LEU B 111
SHEET 5 E 8 HIS B 243 GLU B 251 -1 O VAL B 249 N TYR B 209
SHEET 6 E 8 LEU B 257 PRO B 265 -1 O GLU B 260 N ILE B 248
SHEET 7 E 8 THR B 304 ILE B 305 1 O THR B 304 N MET B 259
SHEET 8 E 8 LYS B 308 LYS B 309 -1 O LYS B 308 N ILE B 305
SHEET 1 F 2 ASP B 152 HIS B 155 0
SHEET 2 F 2 MET B 178 GLN B 181 -1 O GLN B 181 N ASP B 152
LINK MG MG A 1 O HOH A 2 1555 1555 2.12
LINK MG MG A 1 O HOH A 3 1555 1555 2.09
LINK MG MG A 1 O HOH A 4 1555 1555 2.14
LINK MG MG A 1 O HOH A 5 1555 1555 2.01
LINK MG MG A 1 O HOH A 6 1555 1555 2.19
LINK MG MG A 1 OD1 ASN A 187 1555 1555 2.00
LINK MG MG B 1 O HOH B 2 1555 1555 1.96
LINK MG MG B 1 O HOH B 3 1555 1555 2.13
LINK MG MG B 1 O HOH B 4 1555 1555 2.20
LINK MG MG B 1 O HOH B 5 1555 1555 1.89
LINK MG MG B 1 OD1 ASN B 187 1555 1555 2.17
LINK MG MG B 1 O HOH C 360 1555 1555 2.11
SITE 1 AC1 6 HOH A 2 HOH A 3 HOH A 4 HOH A 5
SITE 2 AC1 6 HOH A 6 ASN A 187
SITE 1 AC2 8 SER A 125 CYS A 127 ASP A 128 LYS C 56
SITE 2 AC2 8 ASP C 103 PRO C 104 THR C 105 LEU C 146
SITE 1 AC3 6 HOH B 2 HOH B 3 HOH B 4 HOH B 5
SITE 2 AC3 6 ASN B 187 HOH C 360
CRYST1 70.790 109.150 121.080 90.00 90.00 90.00 P 21 21 21 8
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 0.014126 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009162 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008259 0.00000
(ATOM LINES ARE NOT SHOWN.)
END