HEADER TRANSFERASE 16-OCT-03 1V2H
TITLE CRYSTAL STRUCTURE OF HUMAN PNP COMPLEXED WITH GUANINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PURINE NUCLEOSIDE PHOSPHORYLASE;
COMPND 3 CHAIN: E;
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 GENE: PNP;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET23A
KEYWDS PURINE NUCLEOSIDE PHOSPHORYLASE, DRUG DESIGN, SYNCHROTRON, GUANINE,
KEYWDS 2 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.F.DE AZEVEDO JR.,F.CANDURI,J.H.PEREIRA,D.M.DOS SANTOS,M.V.BERTACINE
AUTHOR 2 DIAS,R.G.SILVA,M.S.PALMA,L.A.BASSO,D.S.SANTOS
REVDAT 5 25-OCT-23 1V2H 1 REMARK
REVDAT 4 13-JUL-11 1V2H 1 VERSN
REVDAT 3 24-FEB-09 1V2H 1 VERSN
REVDAT 2 20-JAN-04 1V2H 1 SOURCE
REVDAT 1 13-JAN-04 1V2H 0
JRNL AUTH W.F.DE AZEVEDO JR.,F.CANDURI,D.M.DOS SANTOS,J.H.PEREIRA,
JRNL AUTH 2 M.V.BERTACINE DIAS,R.G.SILVA,M.A.MENDES,L.A.BASSO,M.S.PALMA,
JRNL AUTH 3 D.S.SANTOS
JRNL TITL CRYSTAL STRUCTURE OF HUMAN PNP COMPLEXED WITH GUANINE.
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 312 767 2003
JRNL REFN ISSN 0006-291X
JRNL PMID 14680831
JRNL DOI 10.1016/J.BBRC.2003.10.190
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH W.F.DE AZEVEDO JR.,F.CANDURI,D.M.DOS SANTOS,R.G.SILVA,
REMARK 1 AUTH 2 J.S.DE OLIVEIRA,L.P.DE CARVALHO,L.A.BASSO,M.A.MENDES,
REMARK 1 AUTH 3 M.S.PALMA,D.S.SANTOS
REMARK 1 TITL CRYSTAL STRUCTURE OF HUMAN PURINE NUCLEOSIDE PHOSPHORYLASE
REMARK 1 TITL 2 AT 2.3A RESOLUTION
REMARK 1 REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 308 545 2003
REMARK 1 REFN ISSN 0006-291X
REMARK 1 PMID 12914785
REMARK 1 DOI 10.1016/S0006-291X(03)01431-1
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 16195
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) : 0.218
REMARK 3 FREE R VALUE : 0.293
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1618
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) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2251
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 31
REMARK 3 SOLVENT ATOMS : 38
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.82
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.36
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : 8.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.013
REMARK 3 BOND ANGLES (DEGREES) : 1.790
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.540
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 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 1V2H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-OCT-03.
REMARK 100 THE DEPOSITION ID IS D_1000006123.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-APR-03
REMARK 200 TEMPERATURE (KELVIN) : 104.0
REMARK 200 PH : 5.30
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : LNLS
REMARK 200 BEAMLINE : D03B-MX1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.4310
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA, CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18226
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 56.381
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.0
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.37100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1M73
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 74.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 5.30, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 292K
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 70.53500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 40.72340
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 54.12333
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 70.53500
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 40.72340
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 54.12333
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 70.53500
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 40.72340
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 54.12333
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 70.53500
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 40.72340
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 54.12333
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 70.53500
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 40.72340
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 54.12333
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 70.53500
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 40.72340
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 54.12333
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 81.44680
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 108.24667
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 81.44680
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 108.24667
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 81.44680
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 108.24667
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 81.44680
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 108.24667
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 81.44680
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 108.24667
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 81.44680
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 108.24667
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 11320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -233.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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 70.53500
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 122.17020
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 -70.53500
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 122.17020
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
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 E 283 C - N - CA ANGL. DEV. = 9.1 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 ASN E 3 143.49 -11.00
REMARK 500 PRO E 54 -121.63 -33.93
REMARK 500 ASN E 55 7.10 -51.60
REMARK 500 VAL E 61 -54.09 -143.38
REMARK 500 PRO E 62 -85.32 -41.26
REMARK 500 ALA E 65 23.11 152.78
REMARK 500 ASN E 74 52.47 26.32
REMARK 500 PHE E 159 74.08 -112.45
REMARK 500 ASP E 167 120.29 -36.75
REMARK 500 GLN E 184 -74.01 -67.92
REMARK 500 ALA E 196 -70.79 -87.10
REMARK 500 SER E 220 -157.02 -155.07
REMARK 500 THR E 221 -64.22 70.37
REMARK 500 ASN E 243 -166.44 -176.08
REMARK 500 LYS E 244 142.55 179.72
REMARK 500 ILE E 246 40.27 166.15
REMARK 500 TYR E 249 77.84 -54.75
REMARK 500 GLU E 250 80.78 65.69
REMARK 500 LEU E 252 -6.87 65.06
REMARK 500 LYS E 254 -13.20 -159.06
REMARK 500 ALA E 255 172.51 77.81
REMARK 500 ASN E 256 -62.78 -173.02
REMARK 500 HIS E 257 -31.29 173.62
REMARK 500 LEU E 261 -37.11 -130.39
REMARK 500 LYS E 265 -69.05 -29.96
REMARK 500 ASP E 286 -15.38 -49.19
REMARK 500 LYS E 287 -37.44 94.74
REMARK 500 ALA E 288 65.36 39.73
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 E 291
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 292
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 293
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 294
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GUN E 290
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1M73 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN AT 2.3 ANGSTROM.
REMARK 900 RELATED ID: 1PF7 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH IMMUCILLIN H.
DBREF 1V2H E 2 289 UNP P00491 PNPH_HUMAN 2 289
SEQRES 1 E 288 GLU ASN GLY TYR THR TYR GLU ASP TYR LYS ASN THR ALA
SEQRES 2 E 288 GLU TRP LEU LEU SER HIS THR LYS HIS ARG PRO GLN VAL
SEQRES 3 E 288 ALA ILE ILE CYS GLY SER GLY LEU GLY GLY LEU THR ASP
SEQRES 4 E 288 LYS LEU THR GLN ALA GLN ILE PHE ASP TYR SER GLU ILE
SEQRES 5 E 288 PRO ASN PHE PRO ARG SER THR VAL PRO GLY HIS ALA GLY
SEQRES 6 E 288 ARG LEU VAL PHE GLY PHE LEU ASN GLY ARG ALA CYS VAL
SEQRES 7 E 288 MET MET GLN GLY ARG PHE HIS MET TYR GLU GLY TYR PRO
SEQRES 8 E 288 LEU TRP LYS VAL THR PHE PRO VAL ARG VAL PHE HIS LEU
SEQRES 9 E 288 LEU GLY VAL ASP THR LEU VAL VAL THR ASN ALA ALA GLY
SEQRES 10 E 288 GLY LEU ASN PRO LYS PHE GLU VAL GLY ASP ILE MET LEU
SEQRES 11 E 288 ILE ARG ASP HIS ILE ASN LEU PRO GLY PHE SER GLY GLN
SEQRES 12 E 288 ASN PRO LEU ARG GLY PRO ASN ASP GLU ARG PHE GLY ASP
SEQRES 13 E 288 ARG PHE PRO ALA MET SER ASP ALA TYR ASP ARG THR MET
SEQRES 14 E 288 ARG GLN ARG ALA LEU SER THR TRP LYS GLN MET GLY GLU
SEQRES 15 E 288 GLN ARG GLU LEU GLN GLU GLY THR TYR VAL MET VAL ALA
SEQRES 16 E 288 GLY PRO SER PHE GLU THR VAL ALA GLU CYS ARG VAL LEU
SEQRES 17 E 288 GLN LYS LEU GLY ALA ASP ALA VAL GLY MET SER THR VAL
SEQRES 18 E 288 PRO GLU VAL ILE VAL ALA ARG HIS CYS GLY LEU ARG VAL
SEQRES 19 E 288 PHE GLY PHE SER LEU ILE THR ASN LYS VAL ILE MET ASP
SEQRES 20 E 288 TYR GLU SER LEU GLU LYS ALA ASN HIS GLU GLU VAL LEU
SEQRES 21 E 288 ALA ALA GLY LYS GLN ALA ALA GLN LYS LEU GLU GLN PHE
SEQRES 22 E 288 VAL SER ILE LEU MET ALA SER ILE PRO LEU PRO ASP LYS
SEQRES 23 E 288 ALA SER
HET SO4 E 291 5
HET SO4 E 292 5
HET SO4 E 293 5
HET SO4 E 294 5
HET GUN E 290 11
HETNAM SO4 SULFATE ION
HETNAM GUN GUANINE
FORMUL 2 SO4 4(O4 S 2-)
FORMUL 6 GUN C5 H5 N5 O
FORMUL 7 HOH *38(H2 O)
HELIX 1 1 THR E 6 SER E 19 1 14
HELIX 2 2 LEU E 35 LEU E 42 5 8
HELIX 3 3 HIS E 86 GLY E 90 5 5
HELIX 4 4 PRO E 92 THR E 97 1 6
HELIX 5 5 THR E 97 GLY E 107 1 11
HELIX 6 6 LEU E 138 SER E 142 1 5
HELIX 7 7 ASP E 167 MET E 181 1 15
HELIX 8 8 THR E 202 LEU E 212 1 11
HELIX 9 9 THR E 221 CYS E 231 1 11
HELIX 10 10 ALA E 263 LEU E 278 1 16
SHEET 1 A10 THR E 43 ASP E 49 0
SHEET 2 A10 ARG E 67 LEU E 73 -1 O LEU E 68 N PHE E 48
SHEET 3 A10 ARG E 76 GLN E 82 -1 O GLN E 82 N ARG E 67
SHEET 4 A10 VAL E 27 CYS E 31 1 N ILE E 29 O MET E 81
SHEET 5 A10 THR E 110 GLY E 119 1 O THR E 114 N ILE E 30
SHEET 6 A10 ARG E 234 LYS E 244 1 O LEU E 240 N ASN E 115
SHEET 7 A10 ILE E 129 ASN E 137 -1 N MET E 130 O SER E 239
SHEET 8 A10 GLN E 188 MET E 194 1 O TYR E 192 N ASP E 134
SHEET 9 A10 ALA E 216 GLY E 218 1 O ALA E 216 N VAL E 193
SHEET 10 A10 THR E 110 GLY E 119 -1 N GLY E 118 O VAL E 217
SITE 1 AC1 4 PRO E 92 GLN E 144 ARG E 148 HOH E 304
SITE 1 AC2 8 GLY E 32 SER E 33 ARG E 84 HIS E 86
SITE 2 AC2 8 ASN E 115 ALA E 116 SER E 220 HOH E 295
SITE 1 AC3 5 GLY E 34 LEU E 35 GLY E 36 GLN E 82
SITE 2 AC3 5 HOH E 307
SITE 1 AC4 4 SER E 33 TYR E 88 PHE E 159 GUN E 290
SITE 1 AC5 9 ALA E 116 ALA E 117 GLY E 118 GLU E 201
SITE 2 AC5 9 VAL E 217 MET E 219 THR E 242 ASN E 243
SITE 3 AC5 9 SO4 E 294
CRYST1 141.070 141.070 162.370 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 0.007090 0.004090 0.000000 0.00000
SCALE2 0.000000 0.008190 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006160 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
