HEADER HYDROLASE 01-JUN-12 4FFS
TITLE CRYSTAL STRUCTURE OF 5'-METHYLTHIOADENOSINE/S-ADENOSYLHOMOCYSTEINE
TITLE 2 NUCLEOSIDASE FROM HELICOBACTER PYLORI WITH BUTYL-THIO-DADME-
TITLE 3 IMMUCILLIN-A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MTA/SAH NUCLEOSIDASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: 5'-METHYLTHIOADENOSINE NUCLEOSIDASE, S-ADENOSYLHOMOCYSTEINE
COMPND 5 NUCLEOSIDASE;
COMPND 6 EC: 3.2.2.9;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HELICOBACTER PYLORI;
SOURCE 3 ORGANISM_TAXID: 85963;
SOURCE 4 STRAIN: J99;
SOURCE 5 GENE: JHP_0082, MTN, MTNN, PFS;
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: PET32A
KEYWDS L-METHIONINE BIOSYNTHETIC PROCESS FROM S-ADENOSYLMETHIONINE, L-
KEYWDS 2 METHIONINE SALVAGE FROM METHYLTHIOADENOSINE, 5'-
KEYWDS 3 METHYLTHIOADENOSINE/S-ADENOSYLHOMOCYSTEINE NUCLEOSIDASE,
KEYWDS 4 ADENOSYLHOMOCYSTEINE NUCLEOSIDASE ACTIVITY, METHYLTHIOADENOSINE
KEYWDS 5 NUCLEOSIDASE ACTIVITY, HYDROLASE ACTIVITY, ACTING ON GLYCOSYL BONDS,
KEYWDS 6 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.M.HAAPALAINEN,A.RINALDO-MATTHIS,R.L.BROWN,G.E.NORRIS,S.C.ALMO,
AUTHOR 2 V.L.SCHRAMM
REVDAT 2 28-FEB-24 4FFS 1 REMARK SEQADV
REVDAT 1 26-SEP-12 4FFS 0
JRNL AUTH S.WANG,A.M.HAAPALAINEN,F.YAN,Q.DU,P.C.TYLER,G.B.EVANS,
JRNL AUTH 2 A.RINALDO-MATTHIS,R.L.BROWN,G.E.NORRIS,S.C.ALMO,V.L.SCHRAMM
JRNL TITL A PICOMOLAR TRANSITION STATE ANALOGUE INHIBITOR OF MTAN AS A
JRNL TITL 2 SPECIFIC ANTIBIOTIC FOR HELICOBACTER PYLORI.
JRNL REF BIOCHEMISTRY V. 51 6892 2012
JRNL REFN ISSN 0006-2960
JRNL PMID 22891633
JRNL DOI 10.1021/BI3009664
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0025
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.19
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 25229
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.163
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.192
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1320
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1815
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.1860
REMARK 3 BIN FREE R VALUE SET COUNT : 97
REMARK 3 BIN FREE R VALUE : 0.2560
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1779
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 229
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.02
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.109
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.106
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.068
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.281
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.954
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1881 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1854 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2544 ; 1.385 ; 1.978
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4295 ; 0.759 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 245 ; 5.694 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 78 ;34.879 ;25.769
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 346 ;13.163 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 3 ;14.130 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 295 ; 0.084 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2108 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 407 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4FFS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JUN-12.
REMARK 100 THE DEPOSITION ID IS D_1000072846.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-FEB-06
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 : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.10010
REMARK 200 MONOCHROMATOR : SI III
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26569
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : 0.09900
REMARK 200 R SYM (I) : 0.09900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.10
REMARK 200 R MERGE FOR SHELL (I) : 0.61500
REMARK 200 R SYM FOR SHELL (I) : 0.61500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRI-SODIUM CITRATE, 0.1M TRIS, PH
REMARK 280 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 3 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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z,-X,-Y
REMARK 290 7555 -Z,-X,Y
REMARK 290 8555 -Z,X,-Y
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z,-X
REMARK 290 11555 Y,-Z,-X
REMARK 290 12555 -Y,-Z,X
REMARK 290 13555 Y,X,-Z
REMARK 290 14555 -Y,-X,-Z
REMARK 290 15555 Y,-X,Z
REMARK 290 16555 -Y,X,Z
REMARK 290 17555 X,Z,-Y
REMARK 290 18555 -X,Z,Y
REMARK 290 19555 -X,-Z,-Y
REMARK 290 20555 X,-Z,Y
REMARK 290 21555 Z,Y,-X
REMARK 290 22555 Z,-Y,X
REMARK 290 23555 -Z,Y,X
REMARK 290 24555 -Z,-Y,-X
REMARK 290 25555 X+1/2,Y+1/2,Z+1/2
REMARK 290 26555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 27555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 28555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 29555 Z+1/2,X+1/2,Y+1/2
REMARK 290 30555 Z+1/2,-X+1/2,-Y+1/2
REMARK 290 31555 -Z+1/2,-X+1/2,Y+1/2
REMARK 290 32555 -Z+1/2,X+1/2,-Y+1/2
REMARK 290 33555 Y+1/2,Z+1/2,X+1/2
REMARK 290 34555 -Y+1/2,Z+1/2,-X+1/2
REMARK 290 35555 Y+1/2,-Z+1/2,-X+1/2
REMARK 290 36555 -Y+1/2,-Z+1/2,X+1/2
REMARK 290 37555 Y+1/2,X+1/2,-Z+1/2
REMARK 290 38555 -Y+1/2,-X+1/2,-Z+1/2
REMARK 290 39555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 40555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 41555 X+1/2,Z+1/2,-Y+1/2
REMARK 290 42555 -X+1/2,Z+1/2,Y+1/2
REMARK 290 43555 -X+1/2,-Z+1/2,-Y+1/2
REMARK 290 44555 X+1/2,-Z+1/2,Y+1/2
REMARK 290 45555 Z+1/2,Y+1/2,-X+1/2
REMARK 290 46555 Z+1/2,-Y+1/2,X+1/2
REMARK 290 47555 -Z+1/2,Y+1/2,X+1/2
REMARK 290 48555 -Z+1/2,-Y+1/2,-X+1/2
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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
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 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 13 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 14 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 14 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 15 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 16 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 16 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 17 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 18 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 18 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 18 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 19 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 19 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 19 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 20 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 20 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 20 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 21 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 21 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 21 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 22 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 22 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 22 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 23 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 23 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 23 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 24 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 24 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 24 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 25 1.000000 0.000000 0.000000 78.86600
REMARK 290 SMTRY2 25 0.000000 1.000000 0.000000 78.86600
REMARK 290 SMTRY3 25 0.000000 0.000000 1.000000 78.86600
REMARK 290 SMTRY1 26 -1.000000 0.000000 0.000000 78.86600
REMARK 290 SMTRY2 26 0.000000 -1.000000 0.000000 78.86600
REMARK 290 SMTRY3 26 0.000000 0.000000 1.000000 78.86600
REMARK 290 SMTRY1 27 -1.000000 0.000000 0.000000 78.86600
REMARK 290 SMTRY2 27 0.000000 1.000000 0.000000 78.86600
REMARK 290 SMTRY3 27 0.000000 0.000000 -1.000000 78.86600
REMARK 290 SMTRY1 28 1.000000 0.000000 0.000000 78.86600
REMARK 290 SMTRY2 28 0.000000 -1.000000 0.000000 78.86600
REMARK 290 SMTRY3 28 0.000000 0.000000 -1.000000 78.86600
REMARK 290 SMTRY1 29 0.000000 0.000000 1.000000 78.86600
REMARK 290 SMTRY2 29 1.000000 0.000000 0.000000 78.86600
REMARK 290 SMTRY3 29 0.000000 1.000000 0.000000 78.86600
REMARK 290 SMTRY1 30 0.000000 0.000000 1.000000 78.86600
REMARK 290 SMTRY2 30 -1.000000 0.000000 0.000000 78.86600
REMARK 290 SMTRY3 30 0.000000 -1.000000 0.000000 78.86600
REMARK 290 SMTRY1 31 0.000000 0.000000 -1.000000 78.86600
REMARK 290 SMTRY2 31 -1.000000 0.000000 0.000000 78.86600
REMARK 290 SMTRY3 31 0.000000 1.000000 0.000000 78.86600
REMARK 290 SMTRY1 32 0.000000 0.000000 -1.000000 78.86600
REMARK 290 SMTRY2 32 1.000000 0.000000 0.000000 78.86600
REMARK 290 SMTRY3 32 0.000000 -1.000000 0.000000 78.86600
REMARK 290 SMTRY1 33 0.000000 1.000000 0.000000 78.86600
REMARK 290 SMTRY2 33 0.000000 0.000000 1.000000 78.86600
REMARK 290 SMTRY3 33 1.000000 0.000000 0.000000 78.86600
REMARK 290 SMTRY1 34 0.000000 -1.000000 0.000000 78.86600
REMARK 290 SMTRY2 34 0.000000 0.000000 1.000000 78.86600
REMARK 290 SMTRY3 34 -1.000000 0.000000 0.000000 78.86600
REMARK 290 SMTRY1 35 0.000000 1.000000 0.000000 78.86600
REMARK 290 SMTRY2 35 0.000000 0.000000 -1.000000 78.86600
REMARK 290 SMTRY3 35 -1.000000 0.000000 0.000000 78.86600
REMARK 290 SMTRY1 36 0.000000 -1.000000 0.000000 78.86600
REMARK 290 SMTRY2 36 0.000000 0.000000 -1.000000 78.86600
REMARK 290 SMTRY3 36 1.000000 0.000000 0.000000 78.86600
REMARK 290 SMTRY1 37 0.000000 1.000000 0.000000 78.86600
REMARK 290 SMTRY2 37 1.000000 0.000000 0.000000 78.86600
REMARK 290 SMTRY3 37 0.000000 0.000000 -1.000000 78.86600
REMARK 290 SMTRY1 38 0.000000 -1.000000 0.000000 78.86600
REMARK 290 SMTRY2 38 -1.000000 0.000000 0.000000 78.86600
REMARK 290 SMTRY3 38 0.000000 0.000000 -1.000000 78.86600
REMARK 290 SMTRY1 39 0.000000 1.000000 0.000000 78.86600
REMARK 290 SMTRY2 39 -1.000000 0.000000 0.000000 78.86600
REMARK 290 SMTRY3 39 0.000000 0.000000 1.000000 78.86600
REMARK 290 SMTRY1 40 0.000000 -1.000000 0.000000 78.86600
REMARK 290 SMTRY2 40 1.000000 0.000000 0.000000 78.86600
REMARK 290 SMTRY3 40 0.000000 0.000000 1.000000 78.86600
REMARK 290 SMTRY1 41 1.000000 0.000000 0.000000 78.86600
REMARK 290 SMTRY2 41 0.000000 0.000000 1.000000 78.86600
REMARK 290 SMTRY3 41 0.000000 -1.000000 0.000000 78.86600
REMARK 290 SMTRY1 42 -1.000000 0.000000 0.000000 78.86600
REMARK 290 SMTRY2 42 0.000000 0.000000 1.000000 78.86600
REMARK 290 SMTRY3 42 0.000000 1.000000 0.000000 78.86600
REMARK 290 SMTRY1 43 -1.000000 0.000000 0.000000 78.86600
REMARK 290 SMTRY2 43 0.000000 0.000000 -1.000000 78.86600
REMARK 290 SMTRY3 43 0.000000 -1.000000 0.000000 78.86600
REMARK 290 SMTRY1 44 1.000000 0.000000 0.000000 78.86600
REMARK 290 SMTRY2 44 0.000000 0.000000 -1.000000 78.86600
REMARK 290 SMTRY3 44 0.000000 1.000000 0.000000 78.86600
REMARK 290 SMTRY1 45 0.000000 0.000000 1.000000 78.86600
REMARK 290 SMTRY2 45 0.000000 1.000000 0.000000 78.86600
REMARK 290 SMTRY3 45 -1.000000 0.000000 0.000000 78.86600
REMARK 290 SMTRY1 46 0.000000 0.000000 1.000000 78.86600
REMARK 290 SMTRY2 46 0.000000 -1.000000 0.000000 78.86600
REMARK 290 SMTRY3 46 1.000000 0.000000 0.000000 78.86600
REMARK 290 SMTRY1 47 0.000000 0.000000 -1.000000 78.86600
REMARK 290 SMTRY2 47 0.000000 1.000000 0.000000 78.86600
REMARK 290 SMTRY3 47 1.000000 0.000000 0.000000 78.86600
REMARK 290 SMTRY1 48 0.000000 0.000000 -1.000000 78.86600
REMARK 290 SMTRY2 48 0.000000 -1.000000 0.000000 78.86600
REMARK 290 SMTRY3 48 -1.000000 0.000000 0.000000 78.86600
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17660 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL
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 350 BIOMT1 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 520 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 610 LIES ON A SPECIAL POSITION.
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 -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
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 LYS A 51 161.02 80.69
REMARK 500 ASN A 89 -14.36 82.35
REMARK 500 SER A 117 -148.25 -135.52
REMARK 500 HIS A 155 47.25 -154.47
REMARK 500 GLU A 175 -26.20 -141.20
REMARK 500 ASP A 201 -163.52 -120.87
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BIG A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 302
DBREF 4FFS A 1 230 UNP Q9ZMY2 MTNN_HELPJ 1 230
SEQADV 4FFS MET A -8 UNP Q9ZMY2 INITIATING METHIONINE
SEQADV 4FFS HIS A -7 UNP Q9ZMY2 EXPRESSION TAG
SEQADV 4FFS HIS A -6 UNP Q9ZMY2 EXPRESSION TAG
SEQADV 4FFS HIS A -5 UNP Q9ZMY2 EXPRESSION TAG
SEQADV 4FFS HIS A -4 UNP Q9ZMY2 EXPRESSION TAG
SEQADV 4FFS HIS A -3 UNP Q9ZMY2 EXPRESSION TAG
SEQADV 4FFS HIS A -2 UNP Q9ZMY2 EXPRESSION TAG
SEQADV 4FFS GLU A -1 UNP Q9ZMY2 EXPRESSION TAG
SEQADV 4FFS PHE A 0 UNP Q9ZMY2 EXPRESSION TAG
SEQRES 1 A 239 MET HIS HIS HIS HIS HIS HIS GLU PHE MET GLN LYS ILE
SEQRES 2 A 239 GLY ILE LEU GLY ALA MET ARG GLU GLU ILE THR PRO ILE
SEQRES 3 A 239 LEU GLU LEU PHE GLY VAL ASP PHE GLU GLU ILE PRO LEU
SEQRES 4 A 239 GLY GLY ASN VAL PHE HIS LYS GLY VAL TYR HIS ASN LYS
SEQRES 5 A 239 GLU ILE ILE VAL ALA TYR SER LYS ILE GLY LYS VAL HIS
SEQRES 6 A 239 SER THR LEU THR THR THR SER MET ILE LEU ALA PHE GLY
SEQRES 7 A 239 VAL GLN LYS VAL LEU PHE SER GLY VAL ALA GLY SER LEU
SEQRES 8 A 239 VAL LYS ASP LEU LYS ILE ASN ASP LEU LEU VAL ALA THR
SEQRES 9 A 239 GLN LEU VAL GLN HIS ASP VAL ASP LEU SER ALA PHE ASP
SEQRES 10 A 239 HIS PRO LEU GLY PHE ILE PRO GLU SER ALA ILE PHE ILE
SEQRES 11 A 239 GLU THR SER GLY SER LEU ASN ALA LEU ALA LYS LYS ILE
SEQRES 12 A 239 ALA ASN GLU GLN HIS ILE ALA LEU LYS GLU GLY VAL ILE
SEQRES 13 A 239 ALA SER GLY ASP GLN PHE VAL HIS SER LYS GLU ARG LYS
SEQRES 14 A 239 GLU PHE LEU VAL SER GLU PHE LYS ALA SER ALA VAL GLU
SEQRES 15 A 239 MET GLU GLY ALA SER VAL ALA PHE VAL CYS GLN LYS PHE
SEQRES 16 A 239 GLY VAL PRO CYS CYS VAL LEU ARG SER ILE SER ASP ASN
SEQRES 17 A 239 ALA ASP GLU LYS ALA GLY MET SER PHE ASP GLU PHE LEU
SEQRES 18 A 239 GLU LYS SER ALA HIS THR SER ALA LYS PHE LEU LYS SER
SEQRES 19 A 239 MET VAL ASP GLU LEU
HET BIG A 301 23
HET CL A 302 1
HETNAM BIG (3R,4S)-1-[(4-AMINO-5H-PYRROLO[3,2-D]PYRIMIDIN-7-YL)
HETNAM 2 BIG METHYL]-4-[(BUTYLSULFANYL)METHYL]PYRROLIDIN-3-OL
HETNAM CL CHLORIDE ION
HETSYN BIG BUTYLTHIO-DADME-IMMUCILLIN A
FORMUL 2 BIG C16 H25 N5 O S
FORMUL 3 CL CL 1-
FORMUL 4 HOH *229(H2 O)
HELIX 1 1 MET A 10 GLY A 22 1 13
HELIX 2 2 GLY A 53 GLY A 69 1 17
HELIX 3 3 LEU A 104 ASP A 108 5 5
HELIX 4 4 SER A 124 GLN A 138 1 15
HELIX 5 5 SER A 156 LYS A 168 1 13
HELIX 6 6 GLU A 175 PHE A 186 1 12
HELIX 7 7 LYS A 203 GLU A 229 1 27
SHEET 1 A 9 GLU A 26 LEU A 30 0
SHEET 2 A 9 ASN A 33 TYR A 40 -1 O PHE A 35 N ILE A 28
SHEET 3 A 9 LYS A 43 TYR A 49 -1 O VAL A 47 N HIS A 36
SHEET 4 A 9 GLN A 2 GLY A 8 1 N ILE A 6 O ILE A 46
SHEET 5 A 9 LYS A 72 SER A 81 1 O SER A 76 N LEU A 7
SHEET 6 A 9 ALA A 169 GLU A 173 -1 O VAL A 172 N GLY A 80
SHEET 7 A 9 LEU A 142 SER A 149 1 N VAL A 146 O SER A 170
SHEET 8 A 9 LEU A 91 GLN A 99 1 N VAL A 98 O SER A 149
SHEET 9 A 9 PHE A 120 GLU A 122 -1 O ILE A 121 N LEU A 97
SHEET 1 B 8 GLU A 26 LEU A 30 0
SHEET 2 B 8 ASN A 33 TYR A 40 -1 O PHE A 35 N ILE A 28
SHEET 3 B 8 LYS A 43 TYR A 49 -1 O VAL A 47 N HIS A 36
SHEET 4 B 8 GLN A 2 GLY A 8 1 N ILE A 6 O ILE A 46
SHEET 5 B 8 LYS A 72 SER A 81 1 O SER A 76 N LEU A 7
SHEET 6 B 8 CYS A 190 ASP A 198 1 O CYS A 191 N PHE A 75
SHEET 7 B 8 LEU A 91 GLN A 99 -1 N LEU A 92 O ARG A 194
SHEET 8 B 8 PHE A 120 GLU A 122 -1 O ILE A 121 N LEU A 97
SITE 1 AC1 17 ALA A 9 MET A 10 ILE A 52 VAL A 78
SITE 2 AC1 17 ALA A 79 GLY A 80 LEU A 104 PHE A 153
SITE 3 AC1 17 VAL A 154 VAL A 172 GLU A 173 MET A 174
SITE 4 AC1 17 GLU A 175 SER A 197 ASP A 198 PHE A 208
SITE 5 AC1 17 HOH A 565
SITE 1 AC2 5 VAL A 23 ASP A 24 LYS A 185 HOH A 409
SITE 2 AC2 5 HOH A 607
CRYST1 157.732 157.732 157.732 90.00 90.00 90.00 I 4 3 2 48
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 0.006340 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006340 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006340 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
