HEADER HYDROLASE/DNA 22-OCT-01 1K82
TITLE CRYSTAL STRUCTURE OF E.COLI FORMAMIDOPYRIMIDINE-DNA GLYCOSYLASE (FPG)
TITLE 2 COVALENTLY TRAPPED WITH DNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5'-D(*GP*GP*CP*TP*TP*CP*CP*TP*CP*CP*TP*GP*G)-3';
COMPND 3 CHAIN: E, F, G, H;
COMPND 4 SYNONYM: FAPY-DNA GLYCOSYLASE, FPG;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: 5'-D(*CP*CP*AP*GP*GP*AP*(PED)P*GP*AP*AP*GP*CP*C)-3';
COMPND 8 CHAIN: I, J, K, L;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 3;
COMPND 11 MOLECULE: FORMAMIDOPYRIMIDINE-DNA GLYCOSYLASE;
COMPND 12 CHAIN: A, B, C, D;
COMPND 13 EC: 3.2.2.23;
COMPND 14 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: ESCHERICHIA COLI;
SOURCE 7 ORGANISM_TAXID: 562;
SOURCE 8 GENE: FPG;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 11 EXPRESSION_SYSTEM_STRAIN: B834(DE3);
SOURCE 12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PET-13A
KEYWDS PROTEIN-DNA COMPLEX, DNA REPAIR, BETA SANDWICH, ZINC FINGER, HELIX
KEYWDS 2 TWO-TURNS HELIX, HYDROLASE-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR R.GILBOA,D.O.ZHARKOV,G.GOLAN,A.S.FERNANDES,S.E.GERCHMAN,E.MATZ,
AUTHOR 2 J.H.KYCIA,A.P.GROLLMAN,G.SHOHAM
REVDAT 3 16-AUG-23 1K82 1 REMARK LINK
REVDAT 2 24-FEB-09 1K82 1 VERSN
REVDAT 1 14-JUN-02 1K82 0
JRNL AUTH R.GILBOA,D.O.ZHARKOV,G.GOLAN,A.S.FERNANDES,S.E.GERCHMAN,
JRNL AUTH 2 E.MATZ,J.H.KYCIA,A.P.GROLLMAN,G.SHOHAM
JRNL TITL STRUCTURE OF FORMAMIDOPYRIMIDINE-DNA GLYCOSYLASE COVALENTLY
JRNL TITL 2 COMPLEXED TO DNA.
JRNL REF J.BIOL.CHEM. V. 277 19811 2002
JRNL REFN ISSN 0021-9258
JRNL PMID 11912217
JRNL DOI 10.1074/JBC.M202058200
REMARK 2
REMARK 2 RESOLUTION. 2.10 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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 84374
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.265
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 4191
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8149
REMARK 3 NUCLEIC ACID ATOMS : 2064
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 499
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 33.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.27
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) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.100
REMARK 3 BOND ANGLES (DEGREES) : 2.020
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1K82 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-NOV-01.
REMARK 100 THE DEPOSITION ID IS D_1000014677.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-APR-01
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X26C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 84396
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 34.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.8000
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) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.26500
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: GLRF
REMARK 200 STARTING MODEL: PDB ENTRY 1EE8 AND PDB ENTRY 1K3W
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, AMMONIUM SULFATE,
REMARK 280 CACODYLATE, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 298K
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 48.01650
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: E, I, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, J, 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, K, 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 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, D
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 LYS A 217
REMARK 465 ASP A 218
REMARK 465 PHE A 219
REMARK 465 LEU A 220
REMARK 465 GLN A 221
REMARK 465 SER A 222
REMARK 465 ASP A 223
REMARK 465 GLY A 224
REMARK 465 LYS B 217
REMARK 465 ASP B 218
REMARK 465 PHE B 219
REMARK 465 LEU B 220
REMARK 465 GLN B 221
REMARK 465 SER B 222
REMARK 465 ASP B 223
REMARK 465 GLY B 224
REMARK 465 LYS C 217
REMARK 465 ASP C 218
REMARK 465 PHE C 219
REMARK 465 LEU C 220
REMARK 465 GLN C 221
REMARK 465 SER C 222
REMARK 465 ASP C 223
REMARK 465 GLY C 224
REMARK 465 LYS D 217
REMARK 465 ASP D 218
REMARK 465 PHE D 219
REMARK 465 LEU D 220
REMARK 465 GLN D 221
REMARK 465 SER D 222
REMARK 465 ASP D 223
REMARK 465 GLY D 224
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 GLU A 82 CB CG CD OE1 OE2
REMARK 470 LYS A 117 CG CD CE NZ
REMARK 470 GLU A 120 CG CD OE1 OE2
REMARK 470 LYS A 225 CG CD CE NZ
REMARK 470 TYR A 228 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU B 82 CG CD OE1 OE2
REMARK 470 GLU B 83 CG CD OE1 OE2
REMARK 470 LYS B 117 CG CD CE NZ
REMARK 470 HIS B 127 CG ND1 CD2 CE1 NE2
REMARK 470 GLN B 211 CG CD OE1 NE2
REMARK 470 LYS B 225 CG CD CE NZ
REMARK 470 TYR B 228 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS C 117 CG CD CE NZ
REMARK 470 HIS C 127 CG ND1 CD2 CE1 NE2
REMARK 470 LYS C 225 CG CD CE NZ
REMARK 470 TYR C 228 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU D 82 CG CD OE1 OE2
REMARK 470 LYS D 117 CG CD CE NZ
REMARK 470 GLU D 120 CG CD OE1 OE2
REMARK 470 LYS D 225 CG CD CE NZ
REMARK 470 TYR D 228 CG CD1 CD2 CE1 CE2 CZ OH
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 OE1 GLN D 211 OE2 GLU D 232 1.76
REMARK 500 ND1 HIS C 122 O ASN C 123 1.76
REMARK 500 O HIS D 122 OG1 THR D 126 1.82
REMARK 500 C HIS D 122 OG1 THR D 126 2.07
REMARK 500 O HIS C 122 OG1 THR C 126 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 DG E 402 C4 DG E 402 C5 0.043
REMARK 500 DT E 404 C2 DT E 404 N3 0.089
REMARK 500 DT E 404 C5 DT E 404 C7 0.109
REMARK 500 DT E 405 C2 DT E 405 N3 0.082
REMARK 500 DT E 405 C5 DT E 405 C7 0.102
REMARK 500 DT E 408 C2 DT E 408 N3 0.089
REMARK 500 DT E 408 C5 DT E 408 C7 0.101
REMARK 500 DT E 411 C2 DT E 411 N3 0.083
REMARK 500 DT E 411 C5 DT E 411 C7 0.101
REMARK 500 DG E 412 C4 DG E 412 C5 0.042
REMARK 500 DG E 413 C4 DG E 413 C5 0.042
REMARK 500 DG F 402 C4 DG F 402 C5 0.044
REMARK 500 DT F 404 C2 DT F 404 N3 0.087
REMARK 500 DT F 404 C5 DT F 404 C7 0.101
REMARK 500 DT F 405 C2 DT F 405 N3 0.084
REMARK 500 DT F 405 C5 DT F 405 C7 0.099
REMARK 500 DT F 408 C2 DT F 408 N3 0.085
REMARK 500 DT F 408 C5 DT F 408 C7 0.098
REMARK 500 DT F 411 C2 DT F 411 N3 0.089
REMARK 500 DT F 411 C5 DT F 411 C7 0.104
REMARK 500 DT G 404 C2 DT G 404 N3 0.090
REMARK 500 DT G 404 C5 DT G 404 C7 0.102
REMARK 500 DT G 405 C2 DT G 405 N3 0.080
REMARK 500 DT G 405 C5 DT G 405 C7 0.096
REMARK 500 DT G 408 C2 DT G 408 N3 0.084
REMARK 500 DT G 408 C5 DT G 408 C7 0.101
REMARK 500 DT G 411 C2 DT G 411 N3 0.088
REMARK 500 DT G 411 C5 DT G 411 C7 0.104
REMARK 500 DT H 404 C2 DT H 404 N3 0.081
REMARK 500 DT H 404 C5 DT H 404 C7 0.097
REMARK 500 DT H 405 C2 DT H 405 N3 0.088
REMARK 500 DT H 405 C5 DT H 405 C7 0.097
REMARK 500 DT H 408 C2 DT H 408 N3 0.083
REMARK 500 DT H 408 C5 DT H 408 C7 0.099
REMARK 500 DT H 411 C2 DT H 411 N3 0.089
REMARK 500 DT H 411 C5 DT H 411 C7 0.101
REMARK 500 DG H 412 C4 DG H 412 C5 0.043
REMARK 500 DG H 413 C4 DG H 413 C5 0.044
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 DG E 401 O4' - C1' - N9 ANGL. DEV. = 2.5 DEGREES
REMARK 500 DG E 401 C6 - N1 - C2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 DG E 401 C2 - N3 - C4 ANGL. DEV. = 8.5 DEGREES
REMARK 500 DG E 401 N3 - C4 - C5 ANGL. DEV. = -9.4 DEGREES
REMARK 500 DG E 401 C5 - C6 - N1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 DG E 401 C5 - N7 - C8 ANGL. DEV. = -6.8 DEGREES
REMARK 500 DG E 401 N7 - C8 - N9 ANGL. DEV. = 9.4 DEGREES
REMARK 500 DG E 401 C8 - N9 - C4 ANGL. DEV. = -6.0 DEGREES
REMARK 500 DG E 401 N3 - C4 - N9 ANGL. DEV. = 8.1 DEGREES
REMARK 500 DG E 401 C5 - C6 - O6 ANGL. DEV. = -7.5 DEGREES
REMARK 500 DG E 402 C6 - N1 - C2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 DG E 402 C2 - N3 - C4 ANGL. DEV. = 8.5 DEGREES
REMARK 500 DG E 402 N3 - C4 - C5 ANGL. DEV. = -9.7 DEGREES
REMARK 500 DG E 402 C5 - C6 - N1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 DG E 402 C5 - N7 - C8 ANGL. DEV. = -6.7 DEGREES
REMARK 500 DG E 402 N7 - C8 - N9 ANGL. DEV. = 10.4 DEGREES
REMARK 500 DG E 402 C8 - N9 - C4 ANGL. DEV. = -7.2 DEGREES
REMARK 500 DG E 402 N3 - C4 - N9 ANGL. DEV. = 7.5 DEGREES
REMARK 500 DG E 402 C5 - C6 - O6 ANGL. DEV. = -5.3 DEGREES
REMARK 500 DC E 403 C2 - N3 - C4 ANGL. DEV. = 7.7 DEGREES
REMARK 500 DC E 403 N3 - C4 - C5 ANGL. DEV. = -6.5 DEGREES
REMARK 500 DC E 403 C5 - C6 - N1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 DC E 403 N3 - C4 - N4 ANGL. DEV. = 5.3 DEGREES
REMARK 500 DT E 404 N1 - C1' - C2' ANGL. DEV. = 10.3 DEGREES
REMARK 500 DT E 404 O4' - C1' - N1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 DT E 404 N1 - C2 - N3 ANGL. DEV. = 5.6 DEGREES
REMARK 500 DT E 404 C2 - N3 - C4 ANGL. DEV. = -7.5 DEGREES
REMARK 500 DT E 404 C4 - C5 - C6 ANGL. DEV. = 4.7 DEGREES
REMARK 500 DT E 404 N3 - C2 - O2 ANGL. DEV. = -8.7 DEGREES
REMARK 500 DT E 404 C6 - C5 - C7 ANGL. DEV. = -7.0 DEGREES
REMARK 500 DT E 405 O4' - C1' - N1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 DT E 405 N1 - C2 - N3 ANGL. DEV. = 5.3 DEGREES
REMARK 500 DT E 405 C2 - N3 - C4 ANGL. DEV. = -6.9 DEGREES
REMARK 500 DT E 405 C4 - C5 - C6 ANGL. DEV. = 5.8 DEGREES
REMARK 500 DT E 405 C5 - C6 - N1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 DT E 405 N3 - C2 - O2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 DT E 405 C6 - C5 - C7 ANGL. DEV. = -6.4 DEGREES
REMARK 500 DC E 406 O4' - C1' - N1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 DC E 406 C2 - N3 - C4 ANGL. DEV. = 8.4 DEGREES
REMARK 500 DC E 406 N3 - C4 - C5 ANGL. DEV. = -6.2 DEGREES
REMARK 500 DC E 406 C5 - C6 - N1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 DC E 407 O4' - C1' - N1 ANGL. DEV. = 1.8 DEGREES
REMARK 500 DC E 407 C2 - N3 - C4 ANGL. DEV. = 8.0 DEGREES
REMARK 500 DC E 407 N3 - C4 - C5 ANGL. DEV. = -5.7 DEGREES
REMARK 500 DT E 408 O4' - C1' - N1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 DT E 408 N1 - C2 - N3 ANGL. DEV. = 4.5 DEGREES
REMARK 500 DT E 408 C2 - N3 - C4 ANGL. DEV. = -5.5 DEGREES
REMARK 500 DT E 408 C4 - C5 - C6 ANGL. DEV. = 4.7 DEGREES
REMARK 500 DT E 408 N3 - C2 - O2 ANGL. DEV. = -8.1 DEGREES
REMARK 500 DT E 408 C6 - C5 - C7 ANGL. DEV. = -5.7 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 630 ANGLE DEVIATIONS.
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 GLU A 2 -168.85 -108.54
REMARK 500 LEU A 32 -151.62 -98.04
REMARK 500 ALA A 55 -127.43 53.91
REMARK 500 GLU A 82 -130.67 -173.28
REMARK 500 ASP A 106 89.48 -162.29
REMARK 500 HIS A 122 -118.35 -126.34
REMARK 500 ASN A 123 171.33 53.94
REMARK 500 VAL A 124 -8.20 -53.09
REMARK 500 PRO A 226 -163.09 -49.69
REMARK 500 VAL A 235 -37.38 -133.26
REMARK 500 THR A 253 -157.92 -140.69
REMARK 500 GLU B 2 -168.66 -112.73
REMARK 500 LEU B 32 -148.92 -99.81
REMARK 500 ALA B 55 -121.90 52.79
REMARK 500 ASP B 106 91.88 -164.50
REMARK 500 ASN B 123 -90.42 153.49
REMARK 500 PRO B 226 -168.04 -70.12
REMARK 500 VAL B 235 -31.57 -141.32
REMARK 500 GLU C 2 -166.34 -112.94
REMARK 500 LEU C 32 -152.24 -99.28
REMARK 500 ALA C 55 -126.71 53.78
REMARK 500 ASP C 106 88.93 -161.67
REMARK 500 VAL C 124 -30.13 91.03
REMARK 500 PRO C 226 -162.73 -65.45
REMARK 500 VAL C 235 -40.17 -134.84
REMARK 500 GLU D 2 -167.72 -110.10
REMARK 500 ARG D 31 68.92 -106.13
REMARK 500 LEU D 32 -152.90 -91.46
REMARK 500 ALA D 55 -124.64 60.78
REMARK 500 ASP D 106 89.71 -160.07
REMARK 500 HIS D 122 -100.66 -130.20
REMARK 500 ASN D 123 -174.96 68.37
REMARK 500 THR D 126 -75.75 -45.77
REMARK 500 PRO D 226 -165.64 -70.43
REMARK 500 VAL D 235 -34.23 -134.77
REMARK 500 THR D 253 -158.93 -144.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 450 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 243 SG
REMARK 620 2 CYS A 246 SG 108.6
REMARK 620 3 CYS A 263 SG 110.4 104.0
REMARK 620 4 CYS A 266 SG 113.3 111.1 109.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 450 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 243 SG
REMARK 620 2 CYS B 246 SG 109.0
REMARK 620 3 CYS B 263 SG 114.5 104.3
REMARK 620 4 CYS B 266 SG 110.2 109.5 109.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 450 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 243 SG
REMARK 620 2 CYS C 246 SG 109.6
REMARK 620 3 CYS C 263 SG 112.6 104.0
REMARK 620 4 CYS C 266 SG 109.6 112.3 108.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 450 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 243 SG
REMARK 620 2 CYS D 246 SG 107.6
REMARK 620 3 CYS D 263 SG 110.7 105.2
REMARK 620 4 CYS D 266 SG 110.7 111.2 111.2
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 ZN A 450
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 450
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 450
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 450
DBREF 1K82 A 1 268 UNP P05523 FPG_ECOLI 2 269
DBREF 1K82 B 1 268 UNP P05523 FPG_ECOLI 2 269
DBREF 1K82 C 1 268 UNP P05523 FPG_ECOLI 2 269
DBREF 1K82 D 1 268 UNP P05523 FPG_ECOLI 2 269
DBREF 1K82 E 401 413 PDB 1K82 1K82 401 413
DBREF 1K82 I 421 433 PDB 1K82 1K82 421 433
DBREF 1K82 F 401 413 PDB 1K82 1K82 401 413
DBREF 1K82 J 421 433 PDB 1K82 1K82 421 433
DBREF 1K82 G 401 413 PDB 1K82 1K82 401 413
DBREF 1K82 K 421 433 PDB 1K82 1K82 421 433
DBREF 1K82 H 401 413 PDB 1K82 1K82 401 413
DBREF 1K82 L 421 433 PDB 1K82 1K82 421 433
SEQRES 1 E 13 DG DG DC DT DT DC DC DT DC DC DT DG DG
SEQRES 1 I 13 DC DC DA DG DG DA PED DG DA DA DG DC DC
SEQRES 1 F 13 DG DG DC DT DT DC DC DT DC DC DT DG DG
SEQRES 1 J 13 DC DC DA DG DG DA PED DG DA DA DG DC DC
SEQRES 1 G 13 DG DG DC DT DT DC DC DT DC DC DT DG DG
SEQRES 1 K 13 DC DC DA DG DG DA PED DG DA DA DG DC DC
SEQRES 1 H 13 DG DG DC DT DT DC DC DT DC DC DT DG DG
SEQRES 1 L 13 DC DC DA DG DG DA PED DG DA DA DG DC DC
SEQRES 1 A 268 PRO GLU LEU PRO GLU VAL GLU THR SER ARG ARG GLY ILE
SEQRES 2 A 268 GLU PRO HIS LEU VAL GLY ALA THR ILE LEU HIS ALA VAL
SEQRES 3 A 268 VAL ARG ASN GLY ARG LEU ARG TRP PRO VAL SER GLU GLU
SEQRES 4 A 268 ILE TYR ARG LEU SER ASP GLN PRO VAL LEU SER VAL GLN
SEQRES 5 A 268 ARG ARG ALA LYS TYR LEU LEU LEU GLU LEU PRO GLU GLY
SEQRES 6 A 268 TRP ILE ILE ILE HIS LEU GLY MET SER GLY SER LEU ARG
SEQRES 7 A 268 ILE LEU PRO GLU GLU LEU PRO PRO GLU LYS HIS ASP HIS
SEQRES 8 A 268 VAL ASP LEU VAL MET SER ASN GLY LYS VAL LEU ARG TYR
SEQRES 9 A 268 THR ASP PRO ARG ARG PHE GLY ALA TRP LEU TRP THR LYS
SEQRES 10 A 268 GLU LEU GLU GLY HIS ASN VAL LEU THR HIS LEU GLY PRO
SEQRES 11 A 268 GLU PRO LEU SER ASP ASP PHE ASN GLY GLU TYR LEU HIS
SEQRES 12 A 268 GLN LYS CYS ALA LYS LYS LYS THR ALA ILE LYS PRO TRP
SEQRES 13 A 268 LEU MET ASP ASN LYS LEU VAL VAL GLY VAL GLY ASN ILE
SEQRES 14 A 268 TYR ALA SER GLU SER LEU PHE ALA ALA GLY ILE HIS PRO
SEQRES 15 A 268 ASP ARG LEU ALA SER SER LEU SER LEU ALA GLU CYS GLU
SEQRES 16 A 268 LEU LEU ALA ARG VAL ILE LYS ALA VAL LEU LEU ARG SER
SEQRES 17 A 268 ILE GLU GLN GLY GLY THR THR LEU LYS ASP PHE LEU GLN
SEQRES 18 A 268 SER ASP GLY LYS PRO GLY TYR PHE ALA GLN GLU LEU GLN
SEQRES 19 A 268 VAL TYR GLY ARG LYS GLY GLU PRO CYS ARG VAL CYS GLY
SEQRES 20 A 268 THR PRO ILE VAL ALA THR LYS HIS ALA GLN ARG ALA THR
SEQRES 21 A 268 PHE TYR CYS ARG GLN CYS GLN LYS
SEQRES 1 B 268 PRO GLU LEU PRO GLU VAL GLU THR SER ARG ARG GLY ILE
SEQRES 2 B 268 GLU PRO HIS LEU VAL GLY ALA THR ILE LEU HIS ALA VAL
SEQRES 3 B 268 VAL ARG ASN GLY ARG LEU ARG TRP PRO VAL SER GLU GLU
SEQRES 4 B 268 ILE TYR ARG LEU SER ASP GLN PRO VAL LEU SER VAL GLN
SEQRES 5 B 268 ARG ARG ALA LYS TYR LEU LEU LEU GLU LEU PRO GLU GLY
SEQRES 6 B 268 TRP ILE ILE ILE HIS LEU GLY MET SER GLY SER LEU ARG
SEQRES 7 B 268 ILE LEU PRO GLU GLU LEU PRO PRO GLU LYS HIS ASP HIS
SEQRES 8 B 268 VAL ASP LEU VAL MET SER ASN GLY LYS VAL LEU ARG TYR
SEQRES 9 B 268 THR ASP PRO ARG ARG PHE GLY ALA TRP LEU TRP THR LYS
SEQRES 10 B 268 GLU LEU GLU GLY HIS ASN VAL LEU THR HIS LEU GLY PRO
SEQRES 11 B 268 GLU PRO LEU SER ASP ASP PHE ASN GLY GLU TYR LEU HIS
SEQRES 12 B 268 GLN LYS CYS ALA LYS LYS LYS THR ALA ILE LYS PRO TRP
SEQRES 13 B 268 LEU MET ASP ASN LYS LEU VAL VAL GLY VAL GLY ASN ILE
SEQRES 14 B 268 TYR ALA SER GLU SER LEU PHE ALA ALA GLY ILE HIS PRO
SEQRES 15 B 268 ASP ARG LEU ALA SER SER LEU SER LEU ALA GLU CYS GLU
SEQRES 16 B 268 LEU LEU ALA ARG VAL ILE LYS ALA VAL LEU LEU ARG SER
SEQRES 17 B 268 ILE GLU GLN GLY GLY THR THR LEU LYS ASP PHE LEU GLN
SEQRES 18 B 268 SER ASP GLY LYS PRO GLY TYR PHE ALA GLN GLU LEU GLN
SEQRES 19 B 268 VAL TYR GLY ARG LYS GLY GLU PRO CYS ARG VAL CYS GLY
SEQRES 20 B 268 THR PRO ILE VAL ALA THR LYS HIS ALA GLN ARG ALA THR
SEQRES 21 B 268 PHE TYR CYS ARG GLN CYS GLN LYS
SEQRES 1 C 268 PRO GLU LEU PRO GLU VAL GLU THR SER ARG ARG GLY ILE
SEQRES 2 C 268 GLU PRO HIS LEU VAL GLY ALA THR ILE LEU HIS ALA VAL
SEQRES 3 C 268 VAL ARG ASN GLY ARG LEU ARG TRP PRO VAL SER GLU GLU
SEQRES 4 C 268 ILE TYR ARG LEU SER ASP GLN PRO VAL LEU SER VAL GLN
SEQRES 5 C 268 ARG ARG ALA LYS TYR LEU LEU LEU GLU LEU PRO GLU GLY
SEQRES 6 C 268 TRP ILE ILE ILE HIS LEU GLY MET SER GLY SER LEU ARG
SEQRES 7 C 268 ILE LEU PRO GLU GLU LEU PRO PRO GLU LYS HIS ASP HIS
SEQRES 8 C 268 VAL ASP LEU VAL MET SER ASN GLY LYS VAL LEU ARG TYR
SEQRES 9 C 268 THR ASP PRO ARG ARG PHE GLY ALA TRP LEU TRP THR LYS
SEQRES 10 C 268 GLU LEU GLU GLY HIS ASN VAL LEU THR HIS LEU GLY PRO
SEQRES 11 C 268 GLU PRO LEU SER ASP ASP PHE ASN GLY GLU TYR LEU HIS
SEQRES 12 C 268 GLN LYS CYS ALA LYS LYS LYS THR ALA ILE LYS PRO TRP
SEQRES 13 C 268 LEU MET ASP ASN LYS LEU VAL VAL GLY VAL GLY ASN ILE
SEQRES 14 C 268 TYR ALA SER GLU SER LEU PHE ALA ALA GLY ILE HIS PRO
SEQRES 15 C 268 ASP ARG LEU ALA SER SER LEU SER LEU ALA GLU CYS GLU
SEQRES 16 C 268 LEU LEU ALA ARG VAL ILE LYS ALA VAL LEU LEU ARG SER
SEQRES 17 C 268 ILE GLU GLN GLY GLY THR THR LEU LYS ASP PHE LEU GLN
SEQRES 18 C 268 SER ASP GLY LYS PRO GLY TYR PHE ALA GLN GLU LEU GLN
SEQRES 19 C 268 VAL TYR GLY ARG LYS GLY GLU PRO CYS ARG VAL CYS GLY
SEQRES 20 C 268 THR PRO ILE VAL ALA THR LYS HIS ALA GLN ARG ALA THR
SEQRES 21 C 268 PHE TYR CYS ARG GLN CYS GLN LYS
SEQRES 1 D 268 PRO GLU LEU PRO GLU VAL GLU THR SER ARG ARG GLY ILE
SEQRES 2 D 268 GLU PRO HIS LEU VAL GLY ALA THR ILE LEU HIS ALA VAL
SEQRES 3 D 268 VAL ARG ASN GLY ARG LEU ARG TRP PRO VAL SER GLU GLU
SEQRES 4 D 268 ILE TYR ARG LEU SER ASP GLN PRO VAL LEU SER VAL GLN
SEQRES 5 D 268 ARG ARG ALA LYS TYR LEU LEU LEU GLU LEU PRO GLU GLY
SEQRES 6 D 268 TRP ILE ILE ILE HIS LEU GLY MET SER GLY SER LEU ARG
SEQRES 7 D 268 ILE LEU PRO GLU GLU LEU PRO PRO GLU LYS HIS ASP HIS
SEQRES 8 D 268 VAL ASP LEU VAL MET SER ASN GLY LYS VAL LEU ARG TYR
SEQRES 9 D 268 THR ASP PRO ARG ARG PHE GLY ALA TRP LEU TRP THR LYS
SEQRES 10 D 268 GLU LEU GLU GLY HIS ASN VAL LEU THR HIS LEU GLY PRO
SEQRES 11 D 268 GLU PRO LEU SER ASP ASP PHE ASN GLY GLU TYR LEU HIS
SEQRES 12 D 268 GLN LYS CYS ALA LYS LYS LYS THR ALA ILE LYS PRO TRP
SEQRES 13 D 268 LEU MET ASP ASN LYS LEU VAL VAL GLY VAL GLY ASN ILE
SEQRES 14 D 268 TYR ALA SER GLU SER LEU PHE ALA ALA GLY ILE HIS PRO
SEQRES 15 D 268 ASP ARG LEU ALA SER SER LEU SER LEU ALA GLU CYS GLU
SEQRES 16 D 268 LEU LEU ALA ARG VAL ILE LYS ALA VAL LEU LEU ARG SER
SEQRES 17 D 268 ILE GLU GLN GLY GLY THR THR LEU LYS ASP PHE LEU GLN
SEQRES 18 D 268 SER ASP GLY LYS PRO GLY TYR PHE ALA GLN GLU LEU GLN
SEQRES 19 D 268 VAL TYR GLY ARG LYS GLY GLU PRO CYS ARG VAL CYS GLY
SEQRES 20 D 268 THR PRO ILE VAL ALA THR LYS HIS ALA GLN ARG ALA THR
SEQRES 21 D 268 PHE TYR CYS ARG GLN CYS GLN LYS
HET PED I 427 11
HET PED J 427 11
HET PED K 427 11
HET PED L 427 11
HET ZN A 450 1
HET ZN B 450 1
HET ZN C 450 1
HET ZN D 450 1
HETNAM PED PENTANE-3,4-DIOL-5-PHOSPHATE
HETNAM ZN ZINC ION
HETSYN PED OPEN FORM OF 1'-2'-DIDEOXYRIBOFURANOSE-5'-PHOSPHATE
FORMUL 2 PED 4(C5 H13 O6 P)
FORMUL 13 ZN 4(ZN 2+)
FORMUL 17 HOH *499(H2 O)
HELIX 1 1 GLU A 2 VAL A 18 1 17
HELIX 2 2 SER A 37 LEU A 43 1 7
HELIX 3 3 HIS A 122 THR A 126 5 5
HELIX 4 4 ASN A 138 ALA A 147 1 10
HELIX 5 5 ALA A 152 MET A 158 1 7
HELIX 6 6 GLY A 167 GLY A 179 1 13
HELIX 7 7 LEU A 185 LEU A 189 5 5
HELIX 8 8 SER A 190 GLN A 211 1 22
HELIX 9 9 PHE A 229 LEU A 233 5 5
HELIX 10 10 GLU B 2 VAL B 18 1 17
HELIX 11 11 SER B 37 ARG B 42 1 6
HELIX 12 12 ASN B 138 ALA B 147 1 10
HELIX 13 13 ALA B 152 MET B 158 1 7
HELIX 14 14 GLY B 167 GLY B 179 1 13
HELIX 15 15 LEU B 185 LEU B 189 5 5
HELIX 16 16 SER B 190 GLN B 211 1 22
HELIX 17 17 GLY B 227 LEU B 233 5 7
HELIX 18 18 GLU C 2 VAL C 18 1 17
HELIX 19 19 SER C 37 ARG C 42 1 6
HELIX 20 20 ASN C 138 ALA C 147 1 10
HELIX 21 21 ALA C 152 MET C 158 1 7
HELIX 22 22 GLY C 167 GLY C 179 1 13
HELIX 23 23 LEU C 185 LEU C 189 5 5
HELIX 24 24 SER C 190 GLN C 211 1 22
HELIX 25 25 TYR C 228 LEU C 233 5 6
HELIX 26 26 GLU D 2 VAL D 18 1 17
HELIX 27 27 SER D 37 ARG D 42 1 6
HELIX 28 28 ASN D 138 ALA D 147 1 10
HELIX 29 29 ALA D 152 MET D 158 1 7
HELIX 30 30 GLY D 167 GLY D 179 1 13
HELIX 31 31 LEU D 185 LEU D 189 5 5
HELIX 32 32 SER D 190 GLN D 211 1 22
HELIX 33 33 TYR D 228 LEU D 233 5 6
SHEET 1 A 5 GLN A 46 PRO A 47 0
SHEET 2 A 5 THR A 21 VAL A 27 -1 N ILE A 22 O GLN A 46
SHEET 3 A 5 VAL A 92 MET A 96 -1 O ASP A 93 N VAL A 26
SHEET 4 A 5 VAL A 101 THR A 105 -1 O TYR A 104 N VAL A 92
SHEET 5 A 5 SER A 76 LEU A 80 -1 N ARG A 78 O ARG A 103
SHEET 1 B 4 SER A 50 ARG A 54 0
SHEET 2 B 4 TYR A 57 GLU A 61 -1 O LEU A 59 N GLN A 52
SHEET 3 B 4 TRP A 66 HIS A 70 -1 O ILE A 69 N LEU A 58
SHEET 4 B 4 ALA A 112 THR A 116 -1 O LEU A 114 N ILE A 68
SHEET 1 C 2 VAL A 251 HIS A 255 0
SHEET 2 C 2 ARG A 258 TYR A 262 -1 O THR A 260 N THR A 253
SHEET 1 D 5 SER B 44 PRO B 47 0
SHEET 2 D 5 THR B 21 VAL B 27 -1 N ILE B 22 O GLN B 46
SHEET 3 D 5 ASP B 90 MET B 96 -1 O VAL B 95 N HIS B 24
SHEET 4 D 5 VAL B 101 THR B 105 -1 O TYR B 104 N VAL B 92
SHEET 5 D 5 SER B 76 LEU B 80 -1 N LEU B 80 O VAL B 101
SHEET 1 E 4 SER B 50 ARG B 54 0
SHEET 2 E 4 TYR B 57 LEU B 62 -1 O TYR B 57 N ARG B 54
SHEET 3 E 4 GLY B 65 HIS B 70 -1 O ILE B 69 N LEU B 58
SHEET 4 E 4 ALA B 112 THR B 116 -1 O THR B 116 N TRP B 66
SHEET 1 F 2 VAL B 251 HIS B 255 0
SHEET 2 F 2 ARG B 258 TYR B 262 -1 O THR B 260 N THR B 253
SHEET 1 G 5 SER C 44 PRO C 47 0
SHEET 2 G 5 THR C 21 VAL C 27 -1 N ILE C 22 O GLN C 46
SHEET 3 G 5 VAL C 92 MET C 96 -1 O ASP C 93 N VAL C 26
SHEET 4 G 5 VAL C 101 THR C 105 -1 O TYR C 104 N VAL C 92
SHEET 5 G 5 SER C 76 LEU C 80 -1 N ARG C 78 O ARG C 103
SHEET 1 H 4 SER C 50 ARG C 54 0
SHEET 2 H 4 TYR C 57 LEU C 62 -1 O LEU C 59 N GLN C 52
SHEET 3 H 4 GLY C 65 HIS C 70 -1 O ILE C 69 N LEU C 58
SHEET 4 H 4 ALA C 112 THR C 116 -1 O LEU C 114 N ILE C 68
SHEET 1 I 2 VAL C 251 HIS C 255 0
SHEET 2 I 2 ARG C 258 TYR C 262 -1 O TYR C 262 N VAL C 251
SHEET 1 J 5 SER D 44 PRO D 47 0
SHEET 2 J 5 THR D 21 VAL D 27 -1 N ILE D 22 O GLN D 46
SHEET 3 J 5 VAL D 92 MET D 96 -1 O ASP D 93 N VAL D 26
SHEET 4 J 5 VAL D 101 THR D 105 -1 O TYR D 104 N VAL D 92
SHEET 5 J 5 SER D 76 LEU D 80 -1 N LEU D 80 O VAL D 101
SHEET 1 K 4 SER D 50 ARG D 54 0
SHEET 2 K 4 TYR D 57 GLU D 61 -1 O LEU D 59 N GLN D 52
SHEET 3 K 4 TRP D 66 HIS D 70 -1 O ILE D 69 N LEU D 58
SHEET 4 K 4 ALA D 112 THR D 116 -1 O LEU D 114 N ILE D 68
SHEET 1 L 2 VAL D 251 HIS D 255 0
SHEET 2 L 2 ARG D 258 TYR D 262 -1 O TYR D 262 N VAL D 251
LINK O3' DA I 426 P PED I 427 1555 1555 1.62
LINK O3' PED I 427 P DG I 428 1555 1555 1.63
LINK C1' PED I 427 N PRO A 1 1555 1555 1.39
LINK O3' DA J 426 P PED J 427 1555 1555 1.62
LINK O3' PED J 427 P DG J 428 1555 1555 1.62
LINK C1' PED J 427 N PRO B 1 1555 1555 1.40
LINK O3' DA K 426 P PED K 427 1555 1555 1.62
LINK O3' PED K 427 P DG K 428 1555 1555 1.64
LINK C1' PED K 427 N PRO C 1 1555 1555 1.40
LINK O3' DA L 426 P PED L 427 1555 1555 1.63
LINK O3' PED L 427 P DG L 428 1555 1555 1.62
LINK C1' PED L 427 N PRO D 1 1555 1555 1.40
LINK SG CYS A 243 ZN ZN A 450 1555 1555 2.33
LINK SG CYS A 246 ZN ZN A 450 1555 1555 2.39
LINK SG CYS A 263 ZN ZN A 450 1555 1555 2.37
LINK SG CYS A 266 ZN ZN A 450 1555 1555 2.33
LINK SG CYS B 243 ZN ZN B 450 1555 1555 2.32
LINK SG CYS B 246 ZN ZN B 450 1555 1555 2.38
LINK SG CYS B 263 ZN ZN B 450 1555 1555 2.35
LINK SG CYS B 266 ZN ZN B 450 1555 1555 2.36
LINK SG CYS C 243 ZN ZN C 450 1555 1555 2.33
LINK SG CYS C 246 ZN ZN C 450 1555 1555 2.37
LINK SG CYS C 263 ZN ZN C 450 1555 1555 2.36
LINK SG CYS C 266 ZN ZN C 450 1555 1555 2.34
LINK SG CYS D 243 ZN ZN D 450 1555 1555 2.34
LINK SG CYS D 246 ZN ZN D 450 1555 1555 2.38
LINK SG CYS D 263 ZN ZN D 450 1555 1555 2.34
LINK SG CYS D 266 ZN ZN D 450 1555 1555 2.32
SITE 1 AC1 4 CYS A 243 CYS A 246 CYS A 263 CYS A 266
SITE 1 AC2 4 CYS B 243 CYS B 246 CYS B 263 CYS B 266
SITE 1 AC3 4 CYS C 243 CYS C 246 CYS C 263 CYS C 266
SITE 1 AC4 4 CYS D 243 CYS D 246 CYS D 263 CYS D 266
CRYST1 80.704 96.033 96.228 90.00 96.80 90.00 P 1 21 1 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 0.012392 0.000000 0.001478 0.00000
SCALE2 0.000000 0.010413 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010465 0.00000
(ATOM LINES ARE NOT SHOWN.)
END