HEADER TRANSFERASE 17-JUN-05 2A0Y
TITLE STRUCTURE OF HUMAN PURINE NUCLEOSIDE PHOSPHORYLASE H257D MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PURINE NUCLEOSIDE PHOSPHORYLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: INOSINE PHOSPHORYLASE, PNP;
COMPND 5 EC: 2.4.2.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: NP, PNP;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PURINE NUCLEOSIDE PHOSPHORYLASE, TRANSITION STATE INHIBITOR, MUTANT,
KEYWDS 2 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.S.MURKIN,W.SHI,V.L.SCHRAMM
REVDAT 7 23-AUG-23 2A0Y 1 REMARK
REVDAT 6 20-OCT-21 2A0Y 1 REMARK SEQADV
REVDAT 5 12-DEC-18 2A0Y 1 COMPND HETNAM HETSYN FORMUL
REVDAT 4 13-JUL-11 2A0Y 1 VERSN
REVDAT 3 02-MAR-10 2A0Y 1 JRNL
REVDAT 2 24-FEB-09 2A0Y 1 VERSN
REVDAT 1 06-JUN-06 2A0Y 0
JRNL AUTH A.S.MURKIN,M.R.BIRCK,A.RINALDO-MATTHIS,W.SHI,E.A.TAYLOR,
JRNL AUTH 2 S.C.ALMO,V.L.SCHRAMM
JRNL TITL NEIGHBORING GROUP PARTICIPATION IN THE TRANSITION STATE OF
JRNL TITL 2 HUMAN PURINE NUCLEOSIDE PHOSPHORYLASE.
JRNL REF BIOCHEMISTRY V. 46 5038 2007
JRNL REFN ISSN 0006-2960
JRNL PMID 17407325
JRNL DOI 10.1021/BI700147B
REMARK 2
REMARK 2 RESOLUTION. 2.28 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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) : 2.28
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.0
REMARK 3 NUMBER OF REFLECTIONS : 28222
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.243
REMARK 3 FREE R VALUE : 0.266
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2804
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) : 2.28
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.42
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 69.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3040
REMARK 3 BIN FREE R VALUE : 0.3370
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 350
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.018
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2204
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 29
REMARK 3 SOLVENT ATOMS : 46
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 41.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.42000
REMARK 3 B22 (A**2) : 2.42000
REMARK 3 B33 (A**2) : -4.85000
REMARK 3 B12 (A**2) : 6.72000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.33
REMARK 3 ESD FROM SIGMAA (A) : 0.33
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.38
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.36
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.800
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
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 2A0Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JUN-05.
REMARK 100 THE DEPOSITION ID IS D_1000033354.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-NOV-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
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) : 1.1
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29445
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.280
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 : 8.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 43.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.28
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.36
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.56400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1RSZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 76.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NA CITRATE, AMMONIUM SULFATE, PH 5.6,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 71.23350
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 41.12668
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 55.34300
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 71.23350
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 41.12668
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 55.34300
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 71.23350
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 41.12668
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 55.34300
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 71.23350
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 41.12668
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 55.34300
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 71.23350
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 41.12668
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 55.34300
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 71.23350
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 41.12668
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 55.34300
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 82.25336
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 110.68600
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 82.25336
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 110.68600
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 82.25336
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 110.68600
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 82.25336
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 110.68600
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 82.25336
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 110.68600
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 82.25336
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 110.68600
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A TRIMER GENERATED FROM THE
REMARK 300 MONOMER IN THE ASYMMETRIC UNIT BY THE CRYSTALLOGRAPHIC 3-FOLD
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 10970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -124.0 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 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 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 GLU A 2
REMARK 465 PRO A 285
REMARK 465 ASP A 286
REMARK 465 LYS A 287
REMARK 465 ALA A 288
REMARK 465 SER A 289
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 ASN A 55 -0.75 71.82
REMARK 500 SER A 59 87.84 -49.37
REMARK 500 THR A 60 -90.94 -34.71
REMARK 500 VAL A 61 34.48 -144.28
REMARK 500 PHE A 159 71.57 -119.06
REMARK 500 ASP A 167 113.02 -28.52
REMARK 500 GLN A 184 -72.24 -52.47
REMARK 500 SER A 220 -156.43 -152.62
REMARK 500 THR A 221 -60.82 68.68
REMARK 500 LEU A 252 43.03 -107.33
REMARK 500 ALA A 268 -85.58 -42.64
REMARK 500 PRO A 283 -153.38 -59.71
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 SO4 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIH A 300
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2A0W RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE SAME PROTEIN H257G MUTANT
REMARK 900 RELATED ID: 2A0X RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE SAME PROTEIN H257F MUTANT
DBREF 2A0Y A 1 289 UNP P00491 PNPH_HUMAN 1 289
SEQADV 2A0Y ASP A 257 UNP P00491 HIS 257 ENGINEERED MUTATION
SEQRES 1 A 289 MET GLU ASN GLY TYR THR TYR GLU ASP TYR LYS ASN THR
SEQRES 2 A 289 ALA GLU TRP LEU LEU SER HIS THR LYS HIS ARG PRO GLN
SEQRES 3 A 289 VAL ALA ILE ILE CYS GLY SER GLY LEU GLY GLY LEU THR
SEQRES 4 A 289 ASP LYS LEU THR GLN ALA GLN ILE PHE ASP TYR SER GLU
SEQRES 5 A 289 ILE PRO ASN PHE PRO ARG SER THR VAL PRO GLY HIS ALA
SEQRES 6 A 289 GLY ARG LEU VAL PHE GLY PHE LEU ASN GLY ARG ALA CYS
SEQRES 7 A 289 VAL MET MET GLN GLY ARG PHE HIS MET TYR GLU GLY TYR
SEQRES 8 A 289 PRO LEU TRP LYS VAL THR PHE PRO VAL ARG VAL PHE HIS
SEQRES 9 A 289 LEU LEU GLY VAL ASP THR LEU VAL VAL THR ASN ALA ALA
SEQRES 10 A 289 GLY GLY LEU ASN PRO LYS PHE GLU VAL GLY ASP ILE MET
SEQRES 11 A 289 LEU ILE ARG ASP HIS ILE ASN LEU PRO GLY PHE SER GLY
SEQRES 12 A 289 GLN ASN PRO LEU ARG GLY PRO ASN ASP GLU ARG PHE GLY
SEQRES 13 A 289 ASP ARG PHE PRO ALA MET SER ASP ALA TYR ASP ARG THR
SEQRES 14 A 289 MET ARG GLN ARG ALA LEU SER THR TRP LYS GLN MET GLY
SEQRES 15 A 289 GLU GLN ARG GLU LEU GLN GLU GLY THR TYR VAL MET VAL
SEQRES 16 A 289 ALA GLY PRO SER PHE GLU THR VAL ALA GLU CYS ARG VAL
SEQRES 17 A 289 LEU GLN LYS LEU GLY ALA ASP ALA VAL GLY MET SER THR
SEQRES 18 A 289 VAL PRO GLU VAL ILE VAL ALA ARG HIS CYS GLY LEU ARG
SEQRES 19 A 289 VAL PHE GLY PHE SER LEU ILE THR ASN LYS VAL ILE MET
SEQRES 20 A 289 ASP TYR GLU SER LEU GLU LYS ALA ASN ASP GLU GLU VAL
SEQRES 21 A 289 LEU ALA ALA GLY LYS GLN ALA ALA GLN LYS LEU GLU GLN
SEQRES 22 A 289 PHE VAL SER ILE LEU MET ALA SER ILE PRO LEU PRO ASP
SEQRES 23 A 289 LYS ALA SER
HET SO4 A 401 5
HET SO4 A 402 5
HET DIH A 300 19
HETNAM SO4 SULFATE ION
HETNAM DIH 7-[[(3R,4R)-3-(HYDROXYMETHYL)-4-OXIDANYL-PYRROLIDIN-1-
HETNAM 2 DIH IUM-1-YL]METHYL]-3,5-DIHYDROPYRROLO[3,2-D]PYRIMIDIN-4-
HETNAM 3 DIH ONE
FORMUL 2 SO4 2(O4 S 2-)
FORMUL 4 DIH C12 H17 N4 O3 1+
FORMUL 5 HOH *46(H2 O)
HELIX 1 1 THR A 6 SER A 19 1 14
HELIX 2 2 LEU A 35 ASP A 40 5 6
HELIX 3 3 SER A 51 ILE A 53 5 3
HELIX 4 4 HIS A 86 GLY A 90 5 5
HELIX 5 5 PRO A 92 THR A 97 1 6
HELIX 6 6 THR A 97 LEU A 106 1 10
HELIX 7 7 LEU A 138 SER A 142 1 5
HELIX 8 8 ASP A 167 GLY A 182 1 16
HELIX 9 9 THR A 202 LEU A 212 1 11
HELIX 10 10 THR A 221 CYS A 231 1 11
HELIX 11 11 ASN A 256 ALA A 267 1 12
HELIX 12 12 ALA A 267 ALA A 280 1 14
SHEET 1 A10 THR A 43 ASP A 49 0
SHEET 2 A10 ARG A 67 LEU A 73 -1 O LEU A 68 N PHE A 48
SHEET 3 A10 ARG A 76 GLN A 82 -1 O MET A 80 N VAL A 69
SHEET 4 A10 VAL A 27 CYS A 31 1 N ILE A 29 O VAL A 79
SHEET 5 A10 THR A 110 GLY A 119 1 O VAL A 112 N ILE A 30
SHEET 6 A10 ARG A 234 LYS A 244 1 O ASN A 243 N GLY A 119
SHEET 7 A10 ILE A 129 ASN A 137 -1 N MET A 130 O SER A 239
SHEET 8 A10 GLN A 188 MET A 194 1 O GLY A 190 N ARG A 133
SHEET 9 A10 ALA A 216 GLY A 218 1 O ALA A 216 N VAL A 193
SHEET 10 A10 THR A 110 GLY A 119 -1 N GLY A 118 O VAL A 217
CISPEP 1 GLY A 197 PRO A 198 0 0.37
SITE 1 AC1 10 GLY A 32 SER A 33 ARG A 84 HIS A 86
SITE 2 AC1 10 ASN A 115 ALA A 116 SER A 220 DIH A 300
SITE 3 AC1 10 HOH A 501 HOH A 505
SITE 1 AC2 5 PRO A 92 GLN A 144 ARG A 148 HOH A 504
SITE 2 AC2 5 HOH A 538
SITE 1 AC3 16 TYR A 88 ALA A 116 GLY A 118 PHE A 159
SITE 2 AC3 16 PHE A 200 GLU A 201 VAL A 217 GLY A 218
SITE 3 AC3 16 MET A 219 ASN A 243 VAL A 245 ASP A 257
SITE 4 AC3 16 VAL A 260 SO4 A 401 HOH A 501 HOH A 532
CRYST1 142.467 142.467 166.029 90.00 90.00 120.00 H 3 2 18
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 0.007019 0.004053 0.000000 0.00000
SCALE2 0.000000 0.008105 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006023 0.00000
(ATOM LINES ARE NOT SHOWN.)
END