HEADER TRANSFERASE 27-NOV-07 3BGS
TITLE STRUCTURE OF HUMAN PURINE NUCLEOSIDE PHOSPHORYLASE WITH L-DADME-IMMH
TITLE 2 AND PHOSPHATE
CAVEAT 3BGS DIH A 301 HAS WRONG CHIRALITY AT ATOM C4' DIH A 301 HAS
CAVEAT 2 3BGS WRONG CHIRALITY AT ATOM C3'
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
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 STRAIN: BL21(DE3);
SOURCE 6 GENE: NP, PNP;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PCR-T7/CT-TOPO
KEYWDS PNP, TRANSITION STATE ANALOGUE, L-ENANTIOMER, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.S.MURKIN,U.A.RAMAGOPAL,S.C.ALMO,V.L.SCHRAMM
REVDAT 6 30-AUG-23 3BGS 1 REMARK SEQADV
REVDAT 5 12-DEC-18 3BGS 1 CAVEAT COMPND HETNAM HETSYN
REVDAT 5 2 1 FORMUL
REVDAT 4 25-OCT-17 3BGS 1 REMARK
REVDAT 3 24-FEB-09 3BGS 1 VERSN
REVDAT 2 26-FEB-08 3BGS 1 JRNL
REVDAT 1 08-JAN-08 3BGS 0
JRNL AUTH A.RINALDO-MATTHIS,A.S.MURKIN,U.A.RAMAGOPAL,K.CLINCH,S.P.MEE,
JRNL AUTH 2 G.B.EVANS,P.C.TYLER,R.H.FURNEAUX,S.C.ALMO,V.L.SCHRAMM
JRNL TITL L-ENANTIOMERS OF TRANSITION STATE ANALOGUE INHIBITORS BOUND
JRNL TITL 2 TO HUMAN PURINE NUCLEOSIDE PHOSPHORYLASE
JRNL REF J.AM.CHEM.SOC. V. 130 842 2008
JRNL REFN ISSN 0002-7863
JRNL PMID 18154341
JRNL DOI 10.1021/JA710733G
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 99.50
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 38395
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) : 0.219
REMARK 3 R VALUE (WORKING SET) : 0.218
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1922
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2639
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.39
REMARK 3 BIN R VALUE (WORKING SET) : 0.3100
REMARK 3 BIN FREE R VALUE SET COUNT : 133
REMARK 3 BIN FREE R VALUE : 0.4070
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2238
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 34
REMARK 3 SOLVENT ATOMS : 101
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 56.15
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.06000
REMARK 3 B22 (A**2) : 0.06000
REMARK 3 B33 (A**2) : -0.10000
REMARK 3 B12 (A**2) : 0.03000
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): 0.140
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.137
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.115
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.415
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.948
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2393 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3252 ; 1.639 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 301 ; 4.891 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 113 ;32.793 ;23.451
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 400 ;14.493 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 19 ;17.455 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 346 ; 0.114 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1847 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1031 ; 0.239 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1621 ; 0.327 ; 0.500
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 199 ; 0.211 ; 0.500
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): 52 ; 0.172 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 24 ; 0.191 ; 0.500
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): 1493 ; 3.392 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2346 ; 4.711 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1020 ; 3.301 ; 2.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 902 ; 4.634 ; 3.000
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 : 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 3BGS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-DEC-07.
REMARK 100 THE DEPOSITION ID IS D_1000045501.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-NOV-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
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) : 0.9793
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38397
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.099
REMARK 200 RESOLUTION RANGE LOW (A) : 99.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 12.50
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : 0.07600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.6000
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.70
REMARK 200 R MERGE FOR SHELL (I) : 0.71400
REMARK 200 R SYM FOR SHELL (I) : 0.62700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 1RR6
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 74.27
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CITRATE PH 5.0, 2.3 M
REMARK 280 AMMONIUM DIHYDROGENPHOSPHATE, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 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 71.40050
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 41.22310
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 55.78267
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 71.40050
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 41.22310
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 55.78267
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 71.40050
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 41.22310
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 55.78267
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 71.40050
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 41.22310
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 55.78267
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 71.40050
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 41.22310
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 55.78267
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 71.40050
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 41.22310
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 55.78267
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 82.44620
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 111.56533
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 82.44620
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 111.56533
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 82.44620
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 111.56533
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 82.44620
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 111.56533
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 82.44620
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 111.56533
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 82.44620
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 111.56533
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11390 ANGSTROM**2
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 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 LEU A 35 14.90 -141.56
REMARK 500 ASN A 55 -4.67 74.74
REMARK 500 ASN A 74 55.70 33.99
REMARK 500 ASP A 167 108.83 -45.31
REMARK 500 SER A 176 -74.09 -49.32
REMARK 500 THR A 177 -34.65 -36.32
REMARK 500 THR A 221 -54.62 78.04
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 PO4 A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIH A 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1RR6 RELATED DB: PDB
REMARK 900 RELATED ID: 1RT9 RELATED DB: PDB
REMARK 900 RELATED ID: 1RSZ RELATED DB: PDB
DBREF 3BGS A 1 289 UNP P00491 PNPH_HUMAN 1 289
SEQADV 3BGS SER A 51 UNP P00491 GLY 51 VARIANT
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 HIS 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 PO4 A 302 5
HET PO4 A 303 5
HET PO4 A 304 5
HET DIH A 301 19
HETNAM PO4 PHOSPHATE 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 PO4 3(O4 P 3-)
FORMUL 5 DIH C12 H17 N4 O3 1+
FORMUL 6 HOH *101(H2 O)
HELIX 1 1 THR A 6 THR A 21 1 16
HELIX 2 2 LEU A 35 LEU A 42 5 8
HELIX 3 3 SER A 51 ILE A 53 5 3
HELIX 4 4 VAL A 61 ALA A 65 5 5
HELIX 5 5 HIS A 86 GLY A 90 5 5
HELIX 6 6 PRO A 92 THR A 97 1 6
HELIX 7 7 THR A 97 LEU A 106 1 10
HELIX 8 8 LEU A 138 SER A 142 1 5
HELIX 9 9 ASP A 167 MET A 181 1 15
HELIX 10 10 THR A 202 LEU A 212 1 11
HELIX 11 11 THR A 221 CYS A 231 1 11
HELIX 12 12 ASN A 256 ALA A 267 1 12
HELIX 13 13 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 ARG A 76 N LEU A 73
SHEET 4 A10 VAL A 27 CYS A 31 1 N ILE A 29 O MET A 81
SHEET 5 A10 THR A 110 GLY A 119 1 O VAL A 112 N ALA A 28
SHEET 6 A10 ARG A 234 LYS A 244 1 O ARG A 234 N LEU A 111
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 GLN A 188 N LEU A 131
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 5.50
SITE 1 AC1 5 GLU A 153 ASP A 157 ARG A 158 HIS A 257
SITE 2 AC1 5 HOH A 318
SITE 1 AC2 10 GLY A 32 SER A 33 ARG A 84 HIS A 86
SITE 2 AC2 10 ASN A 115 ALA A 116 SER A 220 DIH A 301
SITE 3 AC2 10 HOH A 346 HOH A 376
SITE 1 AC3 5 PRO A 92 GLN A 144 ARG A 148 HOH A 317
SITE 2 AC3 5 HOH A 373
SITE 1 AC4 16 TYR A 88 ALA A 116 ALA A 117 GLY A 118
SITE 2 AC4 16 PHE A 159 PHE A 200 GLU A 201 VAL A 217
SITE 3 AC4 16 GLY A 218 MET A 219 THR A 242 ASN A 243
SITE 4 AC4 16 HIS A 257 VAL A 260 PO4 A 303 HOH A 335
CRYST1 142.801 142.801 167.348 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 0.007003 0.004043 0.000000 0.00000
SCALE2 0.000000 0.008086 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005976 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
