HEADER HYDROLASE/DNA 03-JUN-02 1LWS
TITLE CRYSTAL STRUCTURE OF THE INTEIN HOMING ENDONUCLEASE PI-SCEI
TITLE 2 BOUND TO ITS RECOGNITION SEQUENCE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PI-SCEI DNA RECOGNITION REGION TOP STRAND;
COMPND 3 CHAIN: B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: PI-SCEI DNA RECOGNITION REGION BOTTOM STRAND;
COMPND 7 CHAIN: C;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: ENDONUCLEASE PI-SCEI;
COMPND 11 CHAIN: A;
COMPND 12 SYNONYM: PI-SCEI, VMA-DERIVED ENDONUCLEASE, VDE, SCE VMA
COMPND 13 INTEIN;
COMPND 14 EC: 3.1.-.-;
COMPND 15 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 SYNTHETIC: YES;
SOURCE 5 MOL_ID: 3;
SOURCE 6 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 7 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 8 ORGANISM_TAXID: 4932;
SOURCE 9 GENE: VMA1;
SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 12 EXPRESSION_SYSTEM_STRAIN: DL41 (DE3);
SOURCE 13 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 14 EXPRESSION_SYSTEM_PLASMID: PT7PI-SCEI
KEYWDS HOMING ENDONUCLEASE, INTEIN, PROTEIN-DNA COMPLEX,
KEYWDS 2 ENDONUCLEASE, HYDROLASE/DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.M.MOURE,F.S.GIMBLE,F.A.QUIOCHO
REVDAT 2 24-FEB-09 1LWS 1 VERSN
REVDAT 1 27-SEP-02 1LWS 0
JRNL AUTH C.M.MOURE,F.S.GIMBLE,F.A.QUIOCHO
JRNL TITL CRYSTAL STRUCTURE OF THE INTEIN HOMING
JRNL TITL 2 ENDONUCLEASE PI-SCEI BOUND TO ITS RECOGNITION
JRNL TITL 3 SEQUENCE.
JRNL REF NAT.STRUCT.BIOL. V. 9 764 2002
JRNL REFN ISSN 1072-8368
JRNL PMID 12219083
JRNL DOI 10.1038/NSB840
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH X.DUAN,F.S.GIMBLE,F.A.QUIOCHO
REMARK 1 TITL CRYSTAL STRUCTURE OF PI-SCEI, A HOMING
REMARK 1 TITL 2 ENDONUCLEASE WITH PROTEIN SPLICING ACTIVITY
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 89 555 1997
REMARK 1 REFN ISSN 0092-8674
REMARK 1 DOI 10.1016/S0092-8674(00)80237-8
REMARK 2
REMARK 2 RESOLUTION. 3.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.92
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.6
REMARK 3 NUMBER OF REFLECTIONS : 11584
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 SET) : 0.287
REMARK 3 FREE R VALUE : 0.310
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 622
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.012
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.66
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1881
REMARK 3 BIN R VALUE (WORKING SET) : 0.3719
REMARK 3 BIN FREE R VALUE : 0.3945
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 124
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.043
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3360
REMARK 3 NUCLEIC ACID ATOMS : 1394
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 69.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 10.91000
REMARK 3 B22 (A**2) : 10.91000
REMARK 3 B33 (A**2) : -21.83000
REMARK 3 B12 (A**2) : 11.77000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.63
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.89
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.60
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.25
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : GROUP FOR PROTEIN ATOMS, OVERALL FOR
REMARK 3 DNA
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 8.580 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 13.300; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 7.640 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 11.130; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.21
REMARK 3 BSOL : 28.14
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 1LWS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUN-02.
REMARK 100 THE RCSB ID CODE IS RCSB016357.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL; NULL
REMARK 200 TEMPERATURE (KELVIN) : 200; NULL
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : APS; APS
REMARK 200 BEAMLINE : 14-BM-D; 14-BM-C
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792, 0.9789, 0.9611; 1.0
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; NULL
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4; NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12539
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.500
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 9.000
REMARK 200 R MERGE (I) : 0.05900
REMARK 200 R SYM (I) : 0.05900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.20100
REMARK 200 R SYM FOR SHELL (I) : 0.20100
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD; NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 200, NA HEPES, CALCIUM
REMARK 280 CHLORIDE, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 141.13333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 70.56667
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 105.85000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 35.28333
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 176.41667
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 141.13333
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 70.56667
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 35.28333
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 105.85000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 176.41667
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 APPLY THE FOLLOWING TO CHAINS: B, C, 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 DC B 1
REMARK 465 DG B 36
REMARK 465 DG B 37
REMARK 465 DG C 1
REMARK 465 DC C 2
REMARK 465 DC C 3
REMARK 465 GLU A 100
REMARK 465 TYR A 101
REMARK 465 GLU A 134
REMARK 465 GLY A 135
REMARK 465 GLU A 251
REMARK 465 TYR A 252
REMARK 465 LYS A 253
REMARK 465 ASP A 254
REMARK 465 ARG A 255
REMARK 465 LYS A 256
REMARK 465 GLU A 257
REMARK 465 PRO A 258
REMARK 465 GLN A 259
REMARK 465 LYS A 269
REMARK 465 VAL A 270
REMARK 465 VAL A 271
REMARK 465 ARG A 272
REMARK 465 GLY A 273
REMARK 465 ASN A 274
REMARK 465 GLY A 275
REMARK 465 ILE A 276
REMARK 465 ARG A 277
REMARK 465 ASN A 278
REMARK 465 ASN A 279
REMARK 465 LEU A 280
REMARK 465 ASN A 281
REMARK 465 THR A 282
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 DC B 3 O4' - C1' - N1 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DT C 6 N1 - C1' - C2' ANGL. DEV. = 8.5 DEGREES
REMARK 500 DC C 14 O4' - C1' - N1 ANGL. DEV. = 1.8 DEGREES
REMARK 500 DT C 21 O4' - C1' - N1 ANGL. DEV. = 2.6 DEGREES
REMARK 500 DC C 22 O4' - C1' - N1 ANGL. DEV. = 3.2 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 PHE A 2 -156.99 -104.44
REMARK 500 SER A 14 -166.15 -57.10
REMARK 500 GLU A 19 30.22 -67.76
REMARK 500 ASN A 20 -14.91 -150.48
REMARK 500 ILE A 38 -43.17 -135.98
REMARK 500 LEU A 40 76.61 -118.95
REMARK 500 GLU A 45 168.82 170.27
REMARK 500 GLN A 55 26.25 -67.32
REMARK 500 SER A 64 7.11 92.40
REMARK 500 LEU A 70 15.62 -149.79
REMARK 500 LEU A 71 104.61 77.95
REMARK 500 ILE A 96 -150.55 -98.56
REMARK 500 LYS A 97 -0.43 -42.93
REMARK 500 GLU A 103 165.12 176.86
REMARK 500 ARG A 118 124.74 -28.95
REMARK 500 LEU A 122 -178.20 172.50
REMARK 500 LYS A 128 108.23 -170.96
REMARK 500 ARG A 138 -79.56 -55.52
REMARK 500 LEU A 142 -5.73 -54.27
REMARK 500 SER A 150 163.43 171.94
REMARK 500 ASN A 151 -60.44 -102.00
REMARK 500 LYS A 152 140.33 -34.32
REMARK 500 ARG A 162 -15.05 -46.24
REMARK 500 GLN A 177 -166.64 -104.80
REMARK 500 SER A 196 -155.84 -152.16
REMARK 500 LYS A 197 147.81 -0.00
REMARK 500 PHE A 198 74.46 -67.64
REMARK 500 ILE A 202 -21.24 98.00
REMARK 500 GLU A 203 2.22 -158.64
REMARK 500 LYS A 206 -80.31 -70.97
REMARK 500 SER A 221 24.81 -71.24
REMARK 500 ASP A 222 -6.90 -144.02
REMARK 500 ALA A 224 65.11 -63.47
REMARK 500 ASN A 247 46.86 79.38
REMARK 500 ASP A 288 43.63 -74.75
REMARK 500 ALA A 289 -55.27 -151.51
REMARK 500 VAL A 291 -61.68 -102.33
REMARK 500 ASN A 302 129.24 179.23
REMARK 500 PHE A 306 -44.22 -21.76
REMARK 500 ASN A 311 121.80 -22.73
REMARK 500 ILE A 312 -70.18 -49.46
REMARK 500 HIS A 333 44.80 -107.67
REMARK 500 THR A 341 154.41 149.40
REMARK 500 ARG A 347 -79.59 -43.52
REMARK 500 ALA A 409 -78.64 -48.84
REMARK 500 ALA A 410 -152.54 -99.18
REMARK 500 SER A 437 135.41 -13.47
REMARK 500 ASP A 438 41.86 -64.24
REMARK 500 ASP A 439 64.57 -177.84
REMARK 500 GLN A 449 11.56 84.36
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 DA B 24 0.07 SIDE_CHAIN
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 A 501 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 326 OD2
REMARK 620 2 ASP A 326 OD1 51.5
REMARK 620 3 ASP A 218 OD1 70.5 65.9
REMARK 620 4 GLY A 217 O 69.2 118.8 83.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 502 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 325 O
REMARK 620 2 ASP A 218 OD1 100.8
REMARK 620 3 ASP A 218 OD2 62.2 47.9
REMARK 620 4 ASP A 326 OD1 73.6 68.9 85.2
REMARK 620 N 1 2 3
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 501
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1VDE RELATED DB: PDB
REMARK 900 PI-SCEI, A HOMING ENDONUCLEASE WITH PROTEIN SPLICING
REMARK 900 ACTIVITY
REMARK 900 RELATED ID: 1LWT RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE INTEIN HOMING ENDONUCLEASE PI_SCEI
REMARK 900 BOUND TO ITS SUBSTRATE DNA (CA2+ FREE)
DBREF 1LWS A 1 454 UNP P17255 VATA_YEAST 284 737
DBREF 1LWS B 1 37 PDB 1LWS 1LWS 1 37
DBREF 1LWS C 1 37 PDB 1LWS 1LWS 1 37
SEQADV 1LWS MSE A 10 UNP P17255 MET 293 MODIFIED RESIDUE
SEQADV 1LWS MSE A 28 UNP P17255 MET 311 MODIFIED RESIDUE
SEQADV 1LWS MSE A 47 UNP P17255 MET 330 MODIFIED RESIDUE
SEQADV 1LWS MSE A 109 UNP P17255 MET 392 MODIFIED RESIDUE
SEQADV 1LWS MSE A 193 UNP P17255 MET 476 MODIFIED RESIDUE
SEQADV 1LWS MSE A 236 UNP P17255 MET 519 MODIFIED RESIDUE
SEQADV 1LWS MSE A 372 UNP P17255 MET 655 MODIFIED RESIDUE
SEQADV 1LWS MSE A 385 UNP P17255 MET 668 MODIFIED RESIDUE
SEQRES 1 B 37 DC DT DC DT DA DT DG DT DC DG DG DG DT
SEQRES 2 B 37 DG DC DG DG DA DG DA DA DA DG DA DG DG
SEQRES 3 B 37 DT DA DA DT DG DA DA DA DT DG DG
SEQRES 1 C 37 DG DC DC DA DT DT DT DC DA DT DT DA DC
SEQRES 2 C 37 DC DT DC DT DT DT DC DT DC DC DG DC DA
SEQRES 3 C 37 DC DC DC DG DA DC DA DT DA DG DA
SEQRES 1 A 454 CYS PHE ALA LYS GLY THR ASN VAL LEU MSE ALA ASP GLY
SEQRES 2 A 454 SER ILE GLU CYS ILE GLU ASN ILE GLU VAL GLY ASN LYS
SEQRES 3 A 454 VAL MSE GLY LYS ASP GLY ARG PRO ARG GLU VAL ILE LYS
SEQRES 4 A 454 LEU PRO ARG GLY ARG GLU THR MSE TYR SER VAL VAL GLN
SEQRES 5 A 454 LYS SER GLN HIS ARG ALA HIS LYS SER ASP SER SER ARG
SEQRES 6 A 454 GLU VAL PRO GLU LEU LEU LYS PHE THR CYS ASN ALA THR
SEQRES 7 A 454 HIS GLU LEU VAL VAL ARG THR PRO ARG SER VAL ARG ARG
SEQRES 8 A 454 LEU SER ARG THR ILE LYS GLY VAL GLU TYR PHE GLU VAL
SEQRES 9 A 454 ILE THR PHE GLU MSE GLY GLN LYS LYS ALA PRO ASP GLY
SEQRES 10 A 454 ARG ILE VAL GLU LEU VAL LYS GLU VAL SER LYS SER TYR
SEQRES 11 A 454 PRO ILE SER GLU GLY PRO GLU ARG ALA ASN GLU LEU VAL
SEQRES 12 A 454 GLU SER TYR ARG LYS ALA SER ASN LYS ALA TYR PHE GLU
SEQRES 13 A 454 TRP THR ILE GLU ALA ARG ASP LEU SER LEU LEU GLY SER
SEQRES 14 A 454 HIS VAL ARG LYS ALA THR TYR GLN THR TYR ALA PRO ILE
SEQRES 15 A 454 LEU TYR GLU ASN ASP HIS PHE PHE ASP TYR MSE GLN LYS
SEQRES 16 A 454 SER LYS PHE HIS LEU THR ILE GLU GLY PRO LYS VAL LEU
SEQRES 17 A 454 ALA TYR LEU LEU GLY LEU TRP ILE GLY ASP GLY LEU SER
SEQRES 18 A 454 ASP ARG ALA THR PHE SER VAL ASP SER ARG ASP THR SER
SEQRES 19 A 454 LEU MSE GLU ARG VAL THR GLU TYR ALA GLU LYS LEU ASN
SEQRES 20 A 454 LEU CYS ALA GLU TYR LYS ASP ARG LYS GLU PRO GLN VAL
SEQRES 21 A 454 ALA LYS THR VAL ASN LEU TYR SER LYS VAL VAL ARG GLY
SEQRES 22 A 454 ASN GLY ILE ARG ASN ASN LEU ASN THR GLU ASN PRO LEU
SEQRES 23 A 454 TRP ASP ALA ILE VAL GLY LEU GLY PHE LEU LYS ASP GLY
SEQRES 24 A 454 VAL LYS ASN ILE PRO SER PHE LEU SER THR ASP ASN ILE
SEQRES 25 A 454 GLY THR ARG GLU THR PHE LEU ALA GLY LEU ILE ASP SER
SEQRES 26 A 454 ASP GLY TYR VAL THR ASP GLU HIS GLY ILE LYS ALA THR
SEQRES 27 A 454 ILE LYS THR ILE HIS THR SER VAL ARG ASP GLY LEU VAL
SEQRES 28 A 454 SER LEU ALA ARG SER LEU GLY LEU VAL VAL SER VAL ASN
SEQRES 29 A 454 ALA GLU PRO ALA LYS VAL ASP MSE ASN GLY THR LYS HIS
SEQRES 30 A 454 LYS ILE SER TYR ALA ILE TYR MSE SER GLY GLY ASP VAL
SEQRES 31 A 454 LEU LEU ASN VAL LEU SER LYS CYS ALA GLY SER LYS LYS
SEQRES 32 A 454 PHE ARG PRO ALA PRO ALA ALA ALA PHE ALA ARG GLU CYS
SEQRES 33 A 454 ARG GLY PHE TYR PHE GLU LEU GLN GLU LEU LYS GLU ASP
SEQRES 34 A 454 ASP TYR TYR GLY ILE THR LEU SER ASP ASP SER ASP HIS
SEQRES 35 A 454 GLN PHE LEU LEU ALA ASN GLN VAL VAL VAL HIS ASN
MODRES 1LWS MSE A 10 MET SELENOMETHIONINE
MODRES 1LWS MSE A 28 MET SELENOMETHIONINE
MODRES 1LWS MSE A 47 MET SELENOMETHIONINE
MODRES 1LWS MSE A 109 MET SELENOMETHIONINE
MODRES 1LWS MSE A 193 MET SELENOMETHIONINE
MODRES 1LWS MSE A 236 MET SELENOMETHIONINE
MODRES 1LWS MSE A 372 MET SELENOMETHIONINE
MODRES 1LWS MSE A 385 MET SELENOMETHIONINE
HET MSE A 10 8
HET MSE A 28 8
HET MSE A 47 8
HET MSE A 109 8
HET MSE A 193 8
HET MSE A 236 8
HET MSE A 372 8
HET MSE A 385 8
HET CA A 501 1
HET CA A 502 1
HETNAM MSE SELENOMETHIONINE
HETNAM CA CALCIUM ION
FORMUL 3 MSE 8(C5 H11 N O2 SE)
FORMUL 4 CA 2(CA 2+)
HELIX 1 1 GLU A 19 ILE A 21 5 3
HELIX 2 2 ARG A 57 ASP A 62 1 6
HELIX 3 3 PRO A 136 LYS A 148 1 13
HELIX 4 4 ARG A 162 LEU A 167 5 6
HELIX 5 5 SER A 169 THR A 175 1 7
HELIX 6 6 PHE A 189 LYS A 195 1 7
HELIX 7 7 GLU A 203 ASP A 218 1 16
HELIX 8 8 ASP A 232 ASN A 247 1 16
HELIX 9 9 LEU A 286 VAL A 291 1 6
HELIX 10 10 SER A 305 ASP A 310 5 6
HELIX 11 11 ASN A 311 ASP A 326 1 16
HELIX 12 12 HIS A 343 LEU A 357 1 15
HELIX 13 13 GLY A 388 SER A 396 1 9
SHEET 1 A 2 ASN A 7 VAL A 8 0
SHEET 2 A 2 GLU A 16 CYS A 17 -1 O GLU A 16 N VAL A 8
SHEET 1 B 3 LYS A 26 MSE A 28 0
SHEET 2 B 3 PRO A 34 LYS A 39 -1 O ARG A 35 N VAL A 27
SHEET 3 B 3 THR A 435 LEU A 436 -1 O THR A 435 N LYS A 39
SHEET 1 C 3 LYS A 72 ASN A 76 0
SHEET 2 C 3 ARG A 42 GLN A 52 -1 N VAL A 50 O PHE A 73
SHEET 3 C 3 PHE A 421 TYR A 432 -1 O TYR A 431 N GLY A 43
SHEET 1 D 2 GLU A 80 PRO A 86 0
SHEET 2 D 2 TYR A 154 GLU A 160 -1 O ILE A 159 N LEU A 81
SHEET 1 E 3 VAL A 89 ARG A 90 0
SHEET 2 E 3 ILE A 105 LYS A 113 -1 O ILE A 105 N ARG A 90
SHEET 3 E 3 ILE A 119 VAL A 126 -1 O VAL A 126 N THR A 106
SHEET 1 F 2 GLN A 177 TYR A 179 0
SHEET 2 F 2 ARG A 417 PHE A 419 -1 O PHE A 419 N GLN A 177
SHEET 1 G 2 THR A 225 ASP A 229 0
SHEET 2 G 2 ALA A 261 ASN A 265 -1 O LYS A 262 N VAL A 228
SHEET 1 H 2 LEU A 296 LYS A 297 0
SHEET 2 H 2 VAL A 300 LYS A 301 -1 O VAL A 300 N LYS A 297
SHEET 1 I 4 GLY A 327 THR A 330 0
SHEET 2 I 4 LYS A 336 ILE A 339 -1 O THR A 338 N TYR A 328
SHEET 3 I 4 SER A 380 SER A 386 -1 O ILE A 383 N ILE A 339
SHEET 4 I 4 VAL A 360 GLU A 366 -1 N GLU A 366 O SER A 380
SHEET 1 J 2 VAL A 370 ASP A 371 0
SHEET 2 J 2 THR A 375 LYS A 376 -1 O THR A 375 N ASP A 371
SHEET 1 K 2 GLN A 443 LEU A 445 0
SHEET 2 K 2 VAL A 451 HIS A 453 -1 O VAL A 452 N PHE A 444
LINK C LEU A 9 N MSE A 10 1555 1555 1.33
LINK C MSE A 10 N ALA A 11 1555 1555 1.34
LINK C VAL A 27 N MSE A 28 1555 1555 1.34
LINK C MSE A 28 N GLY A 29 1555 1555 1.34
LINK C THR A 46 N MSE A 47 1555 1555 1.33
LINK C MSE A 47 N TYR A 48 1555 1555 1.33
LINK C GLU A 108 N MSE A 109 1555 1555 1.32
LINK C MSE A 109 N GLY A 110 1555 1555 1.33
LINK C TYR A 192 N MSE A 193 1555 1555 1.33
LINK C MSE A 193 N GLN A 194 1555 1555 1.34
LINK C LEU A 235 N MSE A 236 1555 1555 1.33
LINK C MSE A 236 N GLU A 237 1555 1555 1.33
LINK C ASP A 371 N MSE A 372 1555 1555 1.33
LINK C MSE A 372 N ASN A 373 1555 1555 1.33
LINK C TYR A 384 N MSE A 385 1555 1555 1.33
LINK C MSE A 385 N SER A 386 1555 1555 1.33
LINK CA CA A 501 OD2 ASP A 326 1555 1555 2.06
LINK CA CA A 501 OD1 ASP A 326 1555 1555 2.74
LINK CA CA A 501 OD1 ASP A 218 1555 1555 2.65
LINK CA CA A 501 O GLY A 217 1555 1555 2.78
LINK CA CA A 502 O SER A 325 1555 1555 2.85
LINK CA CA A 502 OD1 ASP A 218 1555 1555 2.85
LINK CA CA A 502 OD2 ASP A 218 1555 1555 2.61
LINK CA CA A 502 OD1 ASP A 326 1555 1555 2.26
SITE 1 AC1 3 GLY A 217 ASP A 218 ASP A 326
SITE 1 AC2 3 ASP A 218 SER A 325 ASP A 326
CRYST1 123.000 123.000 211.700 90.00 90.00 120.00 P 65 2 2 12
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 0.008130 0.004694 0.000000 0.00000
SCALE2 0.000000 0.009388 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004724 0.00000
(ATOM LINES ARE NOT SHOWN.)
END