HEADER TRANSFERASE/TRANSFERASE INHIBITOR 08-AUG-13 4M5I
TITLE THE IDENTIFICATION, ANALYSIS AND STRUCTURE-BASED DEVELOPMENT OF NOVEL
TITLE 2 INHIBITORS OF 6-HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 2-AMINO-4-HYDROXY-6-HYDROXYMETHYLDIHYDROPTERIDINE
COMPND 3 PYROPHOSPHOKINASE;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: 6-HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE, PPPK,
COMPND 6 7,8-DIHYDRO-6-HYDROXYMETHYLPTERIN-PYROPHOSPHOKINASE, HPPK;
COMPND 7 EC: 2.7.6.3;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: FOLK, B0142, JW0138;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET14B
KEYWDS FOLATE BIOSYNTHESIS, DIPHOSPHOTRANSFERASES, PTERIN, ATP BINDING,
KEYWDS 2 INHIBITOR, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.YUN,D.HOAGLAND,G.KUMAR,B.WADDELL,C.O.ROCK,R.E.LEE,S.W.WHITE
REVDAT 3 20-SEP-23 4M5I 1 REMARK SEQADV LINK
REVDAT 2 16-APR-14 4M5I 1 JRNL
REVDAT 1 02-APR-14 4M5I 0
JRNL AUTH M.K.YUN,D.HOAGLAND,G.KUMAR,M.B.WADDELL,C.O.ROCK,R.E.LEE,
JRNL AUTH 2 S.W.WHITE
JRNL TITL THE IDENTIFICATION, ANALYSIS AND STRUCTURE-BASED DEVELOPMENT
JRNL TITL 2 OF NOVEL INHIBITORS OF 6-HYDROXYMETHYL-7,8-DIHYDROPTERIN
JRNL TITL 3 PYROPHOSPHOKINASE.
JRNL REF BIOORG.MED.CHEM. V. 22 2157 2014
JRNL REFN ISSN 0968-0896
JRNL PMID 24613625
JRNL DOI 10.1016/J.BMC.2014.02.022
REMARK 2
REMARK 2 RESOLUTION. 1.08 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.3_928)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.08
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.66
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.3
REMARK 3 NUMBER OF REFLECTIONS : 56724
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.152
REMARK 3 R VALUE (WORKING SET) : 0.152
REMARK 3 FREE R VALUE : 0.167
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.510
REMARK 3 FREE R VALUE TEST SET COUNT : 1993
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 34.6620 - 2.6053 0.96 4107 148 0.1732 0.1829
REMARK 3 2 2.6053 - 2.0680 0.98 4133 155 0.1602 0.1579
REMARK 3 3 2.0680 - 1.8066 0.97 4060 148 0.1540 0.1683
REMARK 3 4 1.8066 - 1.6414 0.96 4047 144 0.1442 0.1597
REMARK 3 5 1.6414 - 1.5238 0.95 4004 145 0.1299 0.1529
REMARK 3 6 1.5238 - 1.4339 0.95 3966 141 0.1207 0.1470
REMARK 3 7 1.4339 - 1.3621 0.94 3934 149 0.1217 0.1431
REMARK 3 8 1.3621 - 1.3028 0.93 3922 136 0.1190 0.1427
REMARK 3 9 1.3028 - 1.2527 0.93 3881 145 0.1206 0.1456
REMARK 3 10 1.2527 - 1.2094 0.92 3855 134 0.1233 0.1642
REMARK 3 11 1.2094 - 1.1716 0.92 3821 149 0.1314 0.1494
REMARK 3 12 1.1716 - 1.1381 0.91 3802 135 0.1405 0.1686
REMARK 3 13 1.1381 - 1.1082 0.91 3786 145 0.1806 0.2235
REMARK 3 14 1.1082 - 1.0800 0.82 3413 119 0.2509 0.3036
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.47
REMARK 3 K_SOL : 0.46
REMARK 3 B_SOL : 55.76
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.120
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 13.400
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.44090
REMARK 3 B22 (A**2) : 1.02460
REMARK 3 B33 (A**2) : -0.58370
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.91000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.011 1382
REMARK 3 ANGLE : 1.352 1915
REMARK 3 CHIRALITY : 0.078 205
REMARK 3 PLANARITY : 0.005 238
REMARK 3 DIHEDRAL : 16.787 513
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4M5I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-SEP-13.
REMARK 100 THE DEPOSITION ID IS D_1000081491.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-APR-13
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 : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : ROSENBAUM-ROCK DOUBLE-CRYSTAL
REMARK 200 MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 56757
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.080
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.3
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 33.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.08
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.31600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: PEB ENTRY 4M5G
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL, 0.2M CALCIUM CHLORIDE,
REMARK 280 25% PEG 4000, PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 291K
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 29.07350
REMARK 290 SMTRY3 2 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 GLY A -3
REMARK 465 SER A -2
REMARK 465 HIS A -1
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 154 CG CD CE NZ
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 SER A 13 78.02 65.55
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 203 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 26 O
REMARK 620 2 ILE A 28 O 101.0
REMARK 620 3 SER A 31 O 119.8 99.3
REMARK 620 4 HOH A 324 O 87.6 169.7 71.3
REMARK 620 5 HOH A 340 O 63.4 87.9 61.4 91.0
REMARK 620 6 HOH A 352 O 80.3 90.2 155.1 96.8 142.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 201 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 95 OD1
REMARK 620 2 ASP A 97 OD1 92.9
REMARK 620 3 APC A 204 O1A 94.7 169.7
REMARK 620 4 APC A 204 O1B 91.3 93.5 79.2
REMARK 620 5 HOH A 309 O 174.6 84.5 88.6 93.5
REMARK 620 6 HOH A 311 O 84.5 104.3 83.5 161.8 91.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 202 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 95 OD2
REMARK 620 2 ASP A 97 OD2 89.0
REMARK 620 3 APC A 204 O2G 167.3 92.5
REMARK 620 4 APC A 204 O1B 87.8 105.8 79.7
REMARK 620 5 HOH A 346 O 81.0 86.9 111.6 163.0
REMARK 620 6 HOH A 353 O 90.8 166.9 90.5 87.3 80.1
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 CA A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE APC A 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YH6 A 205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 206
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1Q0N RELATED DB: PDB
REMARK 900 RELATED ID: 1HKA RELATED DB: PDB
REMARK 900 RELATED ID: 1KBR RELATED DB: PDB
REMARK 900 RELATED ID: 4M5G RELATED DB: PDB
REMARK 900 RELATED ID: 4M5H RELATED DB: PDB
REMARK 900 RELATED ID: 4M5J RELATED DB: PDB
REMARK 900 RELATED ID: 4M5K RELATED DB: PDB
REMARK 900 RELATED ID: 4M5L RELATED DB: PDB
REMARK 900 RELATED ID: 4M5M RELATED DB: PDB
REMARK 900 RELATED ID: 4M5N RELATED DB: PDB
DBREF 4M5I A 0 158 UNP P26281 HPPK_ECOLI 1 159
SEQADV 4M5I GLY A -3 UNP P26281 EXPRESSION TAG
SEQADV 4M5I SER A -2 UNP P26281 EXPRESSION TAG
SEQADV 4M5I HIS A -1 UNP P26281 EXPRESSION TAG
SEQRES 1 A 162 GLY SER HIS MET THR VAL ALA TYR ILE ALA ILE GLY SER
SEQRES 2 A 162 ASN LEU ALA SER PRO LEU GLU GLN VAL ASN ALA ALA LEU
SEQRES 3 A 162 LYS ALA LEU GLY ASP ILE PRO GLU SER HIS ILE LEU THR
SEQRES 4 A 162 VAL SER SER PHE TYR ARG THR PRO PRO LEU GLY PRO GLN
SEQRES 5 A 162 ASP GLN PRO ASP TYR LEU ASN ALA ALA VAL ALA LEU GLU
SEQRES 6 A 162 THR SER LEU ALA PRO GLU GLU LEU LEU ASN HIS THR GLN
SEQRES 7 A 162 ARG ILE GLU LEU GLN GLN GLY ARG VAL ARG LYS ALA GLU
SEQRES 8 A 162 ARG TRP GLY PRO ARG THR LEU ASP LEU ASP ILE MET LEU
SEQRES 9 A 162 PHE GLY ASN GLU VAL ILE ASN THR GLU ARG LEU THR VAL
SEQRES 10 A 162 PRO HIS TYR ASP MET LYS ASN ARG GLY PHE MET LEU TRP
SEQRES 11 A 162 PRO LEU PHE GLU ILE ALA PRO GLU LEU VAL PHE PRO ASP
SEQRES 12 A 162 GLY GLU MET LEU ARG GLN ILE LEU HIS THR ARG ALA PHE
SEQRES 13 A 162 ASP LYS LEU ASN LYS TRP
HET CA A 201 1
HET CA A 202 1
HET CA A 203 1
HET APC A 204 31
HET YH6 A 205 22
HET CL A 206 1
HETNAM CA CALCIUM ION
HETNAM APC DIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER
HETNAM YH6 2-AMINO-8-{[2-(4-METHYLPHENYL)-2-OXOETHYL]SULFANYL}-1,
HETNAM 2 YH6 7-DIHYDRO-6H-PURIN-6-ONE
HETNAM CL CHLORIDE ION
HETSYN APC ALPHA,BETA-METHYLENEADENOSINE-5'-TRIPHOSPHATE
FORMUL 2 CA 3(CA 2+)
FORMUL 5 APC C11 H18 N5 O12 P3
FORMUL 6 YH6 C14 H13 N5 O2 S
FORMUL 7 CL CL 1-
FORMUL 8 HOH *188(H2 O)
HELIX 1 1 SER A 13 ASP A 27 1 15
HELIX 2 2 ALA A 65 GLN A 80 1 16
HELIX 3 3 ASP A 117 ASN A 120 5 4
HELIX 4 4 ARG A 121 ALA A 132 1 12
HELIX 5 5 MET A 142 ARG A 150 1 9
SHEET 1 A 4 SER A 31 VAL A 36 0
SHEET 2 A 4 TYR A 53 THR A 62 -1 O ALA A 59 N LEU A 34
SHEET 3 A 4 THR A 1 SER A 9 -1 N ALA A 3 O LEU A 60
SHEET 4 A 4 ASP A 95 PHE A 101 -1 O ASP A 97 N ALA A 6
SHEET 1 B 4 SER A 31 VAL A 36 0
SHEET 2 B 4 TYR A 53 THR A 62 -1 O ALA A 59 N LEU A 34
SHEET 3 B 4 TYR A 40 THR A 42 -1 N THR A 42 O TYR A 53
SHEET 4 B 4 ASN A 156 LYS A 157 -1 O ASN A 156 N ARG A 41
SHEET 1 C 2 ILE A 106 ASN A 107 0
SHEET 2 C 2 THR A 112 VAL A 113 -1 O VAL A 113 N ILE A 106
LINK O GLY A 26 CA CA A 203 1555 1555 2.50
LINK O ILE A 28 CA CA A 203 1555 1555 2.34
LINK O SER A 31 CA CA A 203 1555 1555 2.37
LINK OD1 ASP A 95 CA CA A 201 1555 1555 2.29
LINK OD2 ASP A 95 CA CA A 202 1555 1555 2.39
LINK OD1 ASP A 97 CA CA A 201 1555 1555 2.29
LINK OD2 ASP A 97 CA CA A 202 1555 1555 2.24
LINK CA CA A 201 O1A APC A 204 1555 1555 2.34
LINK CA CA A 201 O1B APC A 204 1555 1555 2.35
LINK CA CA A 201 O HOH A 309 1555 1555 2.34
LINK CA CA A 201 O HOH A 311 1555 1555 2.35
LINK CA CA A 202 O2G APC A 204 1555 1555 2.36
LINK CA CA A 202 O1B APC A 204 1555 1555 2.39
LINK CA CA A 202 O HOH A 346 1555 1555 2.51
LINK CA CA A 202 O HOH A 353 1555 1555 2.30
LINK CA CA A 203 O HOH A 324 1555 1555 2.42
LINK CA CA A 203 O HOH A 340 1555 1555 2.57
LINK CA CA A 203 O HOH A 352 1555 1555 2.32
CISPEP 1 VAL A 113 PRO A 114 0 -2.63
SITE 1 AC1 5 ASP A 95 ASP A 97 APC A 204 HOH A 309
SITE 2 AC1 5 HOH A 311
SITE 1 AC2 5 ASP A 95 ASP A 97 APC A 204 HOH A 346
SITE 2 AC2 5 HOH A 353
SITE 1 AC3 6 GLY A 26 ILE A 28 SER A 31 HOH A 324
SITE 2 AC3 6 HOH A 340 HOH A 352
SITE 1 AC4 26 GLN A 74 ARG A 82 ARG A 84 TRP A 89
SITE 2 AC4 26 ARG A 92 ASP A 95 ASP A 97 ILE A 98
SITE 3 AC4 26 ARG A 110 LEU A 111 THR A 112 HIS A 115
SITE 4 AC4 26 TYR A 116 ARG A 121 GLN A 145 HIS A 148
SITE 5 AC4 26 CA A 201 CA A 202 HOH A 305 HOH A 309
SITE 6 AC4 26 HOH A 404 HOH A 415 HOH A 423 HOH A 472
SITE 7 AC4 26 HOH A 487 HOH A 488
SITE 1 AC5 11 THR A 42 PRO A 43 PRO A 44 LEU A 45
SITE 2 AC5 11 TYR A 53 ASN A 55 TRP A 89 ARG A 121
SITE 3 AC5 11 PHE A 123 HOH A 327 HOH A 353
SITE 1 AC6 5 LEU A 64 ALA A 65 GLU A 68 HOH A 391
SITE 2 AC6 5 HOH A 477
CRYST1 35.918 58.147 38.443 90.00 115.63 90.00 P 1 21 1 2
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 0.027841 0.000000 0.013355 0.00000
SCALE2 0.000000 0.017198 0.000000 0.00000
SCALE3 0.000000 0.000000 0.028850 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
