HEADER TRANSFERASE 17-APR-02 1LIJ
TITLE STRUCTURE OF T. GONDII ADENOSINE KINASE BOUND TO PRODRUG 2 7-
TITLE 2 IODOTUBERCIDIN AND AMP-PCP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADENOSINE KINASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: AK, ADENOSINE 5'-PHOSPHOTRANSFERASE;
COMPND 5 EC: 2.7.1.20;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TOXOPLASMA GONDII;
SOURCE 3 ORGANISM_TAXID: 5811;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PBACE
KEYWDS ALPHA-BETA STRUCTURE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.A.SCHUMACHER,D.M.SCOTT,I.I.MATHEWS,S.E.EALICK,D.S.ROOS,B.ULLMAN,
AUTHOR 2 R.G.BRENNAN
REVDAT 4 14-FEB-24 1LIJ 1 REMARK SEQADV LINK
REVDAT 3 17-NOV-09 1LIJ 1 AUTHOR
REVDAT 2 24-FEB-09 1LIJ 1 VERSN
REVDAT 1 15-MAY-02 1LIJ 0
SPRSDE 15-MAY-02 1LIJ 1DH1
JRNL AUTH M.A.SCHUMACHER,D.M.SCOTT,I.I.MATHEWS,S.E.EALICK,D.S.ROOS,
JRNL AUTH 2 B.ULLMAN,R.G.BRENNAN
JRNL TITL CRYSTAL STRUCTURES OF TOXOPLASMA GONDII ADENOSINE KINASE
JRNL TITL 2 REVEAL A NOVEL CATALYTIC MECHANISM AND PRODRUG BINDING.
JRNL REF J.MOL.BIOL. V. 298 875 2000
JRNL REFN ISSN 0022-2836
JRNL PMID 10801355
JRNL DOI 10.1006/JMBI.2000.3753
REMARK 2
REMARK 2 RESOLUTION. 1.86 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TNT
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.86
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 32045
REMARK 3
REMARK 3 USING DATA ABOVE SIGMA CUTOFF.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2956
REMARK 3
REMARK 3 USING ALL DATA, NO SIGMA CUTOFF.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2433
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 53
REMARK 3 SOLVENT ATOMS : 145
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : 12.400
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : 0.011 ; NULL ; NULL
REMARK 3 BOND ANGLES (DEGREES) : 1.947 ; NULL ; NULL
REMARK 3 TORSION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES (A) : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES (A) : NULL ; NULL ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS (A) : NULL ; NULL ; NULL
REMARK 3
REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : 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 RESTRAINT LIBRARIES.
REMARK 3 STEREOCHEMISTRY : ENGH & HUBER
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1LIJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-APR-02.
REMARK 100 THE DEPOSITION ID IS D_1000015969.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-MAR-98
REMARK 200 TEMPERATURE (KELVIN) : 298.0
REMARK 200 PH : 6.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.08
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (TRUNCATE)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35168
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 10.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.08700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.24400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: EPMR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 83.85000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 23.48500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 83.85000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 23.48500
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 MET A 1
REMARK 465 ALA A 2
REMARK 465 VAL A 3
REMARK 465 ASP A 4
REMARK 465 SER A 5
REMARK 465 SER A 6
REMARK 465 ASN A 7
REMARK 465 SER A 8
REMARK 465 ALA A 9
REMARK 465 THR A 10
REMARK 465 ALA A 238
REMARK 465 ALA A 239
REMARK 465 GLU A 240
REMARK 465 GLU A 254
REMARK 465 VAL A 255
REMARK 465 CYS A 256
REMARK 465 THR A 257
REMARK 465 GLY A 258
REMARK 465 ALA A 259
REMARK 465 LEU A 260
REMARK 465 ARG A 261
REMARK 465 LEU A 262
REMARK 465 LEU A 263
REMARK 465 THR A 264
REMARK 465 ALA A 265
REMARK 465 GLY A 266
REMARK 465 GLN A 267
REMARK 465 ASN A 268
REMARK 465 THR A 359
REMARK 465 SER A 360
REMARK 465 LEU A 361
REMARK 465 PRO A 362
REMARK 465 CYS A 363
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 LYS A 241 CG CD CE NZ
REMARK 470 VAL A 242 CG1 CG2
REMARK 470 LEU A 244 CG CD1 CD2
REMARK 470 SER A 245 OG
REMARK 470 VAL A 246 CG1 CG2
REMARK 470 ASN A 248 CG OD1 ND2
REMARK 470 LYS A 249 CG CD CE NZ
REMARK 470 GLU A 250 CG CD OE1 OE2
REMARK 470 HIS A 251 CG ND1 CD2 CE1 NE2
REMARK 470 VAL A 253 CG1 CG2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 1030 O HOH A 1107 2.18
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 THR A 137 C LEU A 138 N -0.253
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 PRO A 12 C - N - CD ANGL. DEV. = -23.5 DEGREES
REMARK 500 VAL A 75 CG1 - CB - CG2 ANGL. DEV. = 10.6 DEGREES
REMARK 500 LEU A 130 CB - CA - C ANGL. DEV. = 12.7 DEGREES
REMARK 500 ARG A 136 O - C - N ANGL. DEV. = -12.1 DEGREES
REMARK 500 THR A 137 O - C - N ANGL. DEV. = -12.7 DEGREES
REMARK 500 HIS A 234 CB - CA - C ANGL. DEV. = 12.2 DEGREES
REMARK 500 LYS A 249 CB - CA - C ANGL. DEV. = 13.4 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 PRO A 12 -80.41 -30.09
REMARK 500 ARG A 83 -55.71 60.85
REMARK 500 ASP A 96 40.59 -99.10
REMARK 500 GLU A 133 -109.74 69.27
REMARK 500 THR A 174 138.74 176.33
REMARK 500 ASN A 190 1.29 80.37
REMARK 500 SER A 198 -49.12 57.80
REMARK 500 TYR A 206 44.25 -109.75
REMARK 500 HIS A 234 -145.73 -99.56
REMARK 500 ASN A 235 -103.28 -94.41
REMARK 500 LEU A 236 -55.03 21.28
REMARK 500 LEU A 356 49.00 -103.56
REMARK 500 SER A 357 -90.48 -85.66
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 999 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ACP A 799 O1B
REMARK 620 2 ACP A 799 O3A 60.4
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 899
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 999
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RPP A 699
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACP A 799
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1LII RELATED DB: PDB
REMARK 900 STRUCTURE OF T. GONDII ADENOSINE KINASE BOUND TO ADENOSINE 2 AND
REMARK 900 AMP-PCP
REMARK 900 RELATED ID: 1LIK RELATED DB: PDB
REMARK 900 STRUCTURE OF T. GONDII ADENOSINE KINASE BOUND TO ADENOSINE
REMARK 900 RELATED ID: 1LIO RELATED DB: PDB
REMARK 900 STRUCTURE OF APO T. GONDII ADENOSINE KINASE
DBREF 1LIJ A 1 363 UNP Q9TVW2 ADK_TOXGO 1 363
SEQADV 1LIJ THR A 126 UNP Q9TVW2 VAL 126 CONFLICT
SEQADV 1LIJ ILE A 150 UNP Q9TVW2 LEU 150 CONFLICT
SEQADV 1LIJ ASN A 153 UNP Q9TVW2 ASP 153 CONFLICT
SEQADV 1LIJ VAL A 242 UNP Q9TVW2 THR 242 CONFLICT
SEQADV 1LIJ VAL A 246 UNP Q9TVW2 THR 246 CONFLICT
SEQADV 1LIJ GLY A 327 UNP Q9TVW2 ALA 327 CONFLICT
SEQRES 1 A 363 MET ALA VAL ASP SER SER ASN SER ALA THR GLY PRO MET
SEQRES 2 A 363 ARG VAL PHE ALA ILE GLY ASN PRO ILE LEU ASP LEU VAL
SEQRES 3 A 363 ALA GLU VAL PRO SER SER PHE LEU ASP GLU PHE PHE LEU
SEQRES 4 A 363 LYS ARG GLY ASP ALA THR LEU ALA THR PRO GLU GLN MET
SEQRES 5 A 363 ARG ILE TYR SER THR LEU ASP GLN PHE ASN PRO THR SER
SEQRES 6 A 363 LEU PRO GLY GLY SER ALA LEU ASN SER VAL ARG VAL VAL
SEQRES 7 A 363 GLN LYS LEU LEU ARG LYS PRO GLY SER ALA GLY TYR MET
SEQRES 8 A 363 GLY ALA ILE GLY ASP ASP PRO ARG GLY GLN VAL LEU LYS
SEQRES 9 A 363 GLU LEU CYS ASP LYS GLU GLY LEU ALA THR ARG PHE MET
SEQRES 10 A 363 VAL ALA PRO GLY GLN SER THR GLY THR CYS ALA VAL LEU
SEQRES 11 A 363 ILE ASN GLU LYS GLU ARG THR LEU CYS THR HIS LEU GLY
SEQRES 12 A 363 ALA CYS GLY SER PHE ARG ILE PRO GLU ASN TRP THR THR
SEQRES 13 A 363 PHE ALA SER GLY ALA LEU ILE PHE TYR ALA THR ALA TYR
SEQRES 14 A 363 THR LEU THR ALA THR PRO LYS ASN ALA LEU GLU VAL ALA
SEQRES 15 A 363 GLY TYR ALA HIS GLY ILE PRO ASN ALA ILE PHE THR LEU
SEQRES 16 A 363 ASN LEU SER ALA PRO PHE CYS VAL GLU LEU TYR LYS ASP
SEQRES 17 A 363 ALA MET GLN SER LEU LEU LEU HIS THR ASN ILE LEU PHE
SEQRES 18 A 363 GLY ASN GLU GLU GLU PHE ALA HIS LEU ALA LYS VAL HIS
SEQRES 19 A 363 ASN LEU VAL ALA ALA GLU LYS VAL ALA LEU SER VAL ALA
SEQRES 20 A 363 ASN LYS GLU HIS ALA VAL GLU VAL CYS THR GLY ALA LEU
SEQRES 21 A 363 ARG LEU LEU THR ALA GLY GLN ASN THR GLY ALA THR LYS
SEQRES 22 A 363 LEU VAL VAL MET THR ARG GLY HIS ASN PRO VAL ILE ALA
SEQRES 23 A 363 ALA GLU GLN THR ALA ASP GLY THR VAL VAL VAL HIS GLU
SEQRES 24 A 363 VAL GLY VAL PRO VAL VAL ALA ALA GLU LYS ILE VAL ASP
SEQRES 25 A 363 THR ASN GLY ALA GLY ASP ALA PHE VAL GLY GLY PHE LEU
SEQRES 26 A 363 TYR GLY LEU SER GLN GLY LYS THR VAL LYS GLN CYS ILE
SEQRES 27 A 363 MET CYS GLY ASN ALA CYS ALA GLN ASP VAL ILE GLN HIS
SEQRES 28 A 363 VAL GLY PHE SER LEU SER PHE THR SER LEU PRO CYS
HET CL A 899 1
HET MG A 999 1
HET RPP A 699 20
HET ACP A 799 31
HETNAM CL CHLORIDE ION
HETNAM MG MAGNESIUM ION
HETNAM RPP 2-RIBOFURANOSYL-3-IODO-2,3-DIHYDRO-1H-PYRAZOLO[3,4-
HETNAM 2 RPP D]PYRIMIDIN-4-YLAMINE
HETNAM ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER
HETSYN ACP ADENOSINE-5'-[BETA, GAMMA-METHYLENE]TRIPHOSPHATE
FORMUL 2 CL CL 1-
FORMUL 3 MG MG 2+
FORMUL 4 RPP C10 H14 I N5 O4
FORMUL 5 ACP C11 H18 N5 O12 P3
FORMUL 6 HOH *145(H2 O)
HELIX 1 1 PRO A 30 PHE A 37 1 8
HELIX 2 2 THR A 48 MET A 52 5 5
HELIX 3 3 ARG A 53 LEU A 58 1 6
HELIX 4 4 ASP A 59 ASN A 62 5 4
HELIX 5 5 GLY A 69 ARG A 83 1 15
HELIX 6 6 ASP A 97 GLU A 110 1 14
HELIX 7 7 LEU A 142 PHE A 148 5 7
HELIX 8 8 ASN A 153 ALA A 158 1 6
HELIX 9 9 TYR A 169 ALA A 173 5 5
HELIX 10 10 PRO A 175 GLY A 187 1 13
HELIX 11 11 ALA A 199 TYR A 206 1 8
HELIX 12 12 TYR A 206 HIS A 216 1 11
HELIX 13 13 GLU A 224 HIS A 234 1 11
HELIX 14 14 LYS A 241 VAL A 253 1 13
HELIX 15 15 ALA A 306 ILE A 310 5 5
HELIX 16 16 GLY A 315 GLN A 330 1 16
HELIX 17 17 THR A 333 ILE A 349 1 17
SHEET 1 A 9 ALA A 113 ALA A 119 0
SHEET 2 A 9 ALA A 88 GLY A 95 1 N GLY A 92 O MET A 117
SHEET 3 A 9 VAL A 15 ILE A 18 1 N VAL A 15 O GLY A 89
SHEET 4 A 9 ILE A 163 THR A 167 1 O TYR A 165 N PHE A 16
SHEET 5 A 9 ILE A 192 ASN A 196 1 O THR A 194 N PHE A 164
SHEET 6 A 9 ILE A 219 ASN A 223 1 O PHE A 221 N LEU A 195
SHEET 7 A 9 LEU A 274 ARG A 279 1 O VAL A 276 N LEU A 220
SHEET 8 A 9 ASN A 282 GLN A 289 -1 O ILE A 285 N MET A 277
SHEET 9 A 9 VAL A 295 VAL A 300 -1 O VAL A 296 N GLU A 288
SHEET 1 B 5 ALA A 44 LEU A 46 0
SHEET 2 B 5 GLU A 135 HIS A 141 1 O THR A 140 N THR A 45
SHEET 3 B 5 GLY A 125 ASN A 132 -1 N ALA A 128 O CYS A 139
SHEET 4 B 5 ILE A 22 GLU A 28 1 N LEU A 25 O VAL A 129
SHEET 5 B 5 THR A 64 GLY A 68 -1 O GLY A 68 N ILE A 22
LINK O1B ACP A 799 MG MG A 999 1555 1555 2.03
LINK O3A ACP A 799 MG MG A 999 1555 1555 2.93
SITE 1 AC1 5 GLY A 19 ASN A 20 ALA A 71 THR A 167
SITE 2 AC1 5 RPP A 699
SITE 1 AC2 1 ACP A 799
SITE 1 AC3 16 ASN A 20 ASP A 24 THR A 45 LEU A 46
SITE 2 AC3 16 GLY A 68 GLY A 69 SER A 70 ASN A 73
SITE 3 AC3 16 THR A 140 TYR A 169 ASN A 314 ASP A 318
SITE 4 AC3 16 ACP A 799 CL A 899 HOH A1005 HOH A1015
SITE 1 AC4 21 ARG A 136 ASN A 223 THR A 278 GLY A 280
SITE 2 AC4 21 HIS A 281 VAL A 284 VAL A 302 THR A 313
SITE 3 AC4 21 ASN A 314 GLY A 315 ALA A 316 GLY A 317
SITE 4 AC4 21 ASN A 342 ALA A 345 GLN A 346 RPP A 699
SITE 5 AC4 21 MG A 999 HOH A1000 HOH A1004 HOH A1095
SITE 6 AC4 21 HOH A1122
CRYST1 167.700 46.970 44.090 90.00 90.00 90.00 P 21 21 2 4
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 0.005963 0.000000 0.000000 0.00000
SCALE2 0.000000 0.021290 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022681 0.00000
(ATOM LINES ARE NOT SHOWN.)
END