HEADER OXIDOREDUCTASE 11-NOV-10 3PKF
TITLE URATE OXIDASE UNDER 0.2 MPA / 2 BARS PRESSURE OF EQUIMOLAR MIXTURE OF
TITLE 2 XENON AND NITROUS OXIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: URICASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: URATE OXIDASE;
COMPND 5 EC: 1.7.3.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASPERGILLUS FLAVUS;
SOURCE 3 ORGANISM_TAXID: 5059;
SOURCE 4 GENE: UAZ, UOX;
SOURCE 5 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4932
KEYWDS T-FOLD, OXIDASE, PEROXISOME, TETRAMER, URIC ACID DEGRADATION,
KEYWDS 2 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.MARASSIO,N.COLLOC'H,T.PRANGE,J.H.ABRAINI
REVDAT 4 06-SEP-23 3PKF 1 REMARK SEQADV LINK
REVDAT 3 08-NOV-17 3PKF 1 REMARK
REVDAT 2 13-JUL-11 3PKF 1 JRNL
REVDAT 1 06-APR-11 3PKF 0
JRNL AUTH G.MARASSIO,T.PRANGE,H.N.DAVID,J.SOPKOVA-DE OLIVEIRA SANTOS,
JRNL AUTH 2 L.GABISON,N.DELCROIX,J.H.ABRAINI,N.COLLOC'H
JRNL TITL PRESSURE-RESPONSE ANALYSIS OF ANESTHETIC GASES XENON AND
JRNL TITL 2 NITROUS OXIDE ON URATE OXIDASE: A CRYSTALLOGRAPHIC STUDY.
JRNL REF FASEB J. V. 25 2266 2011
JRNL REFN ISSN 0892-6638
JRNL PMID 21421845
JRNL DOI 10.1096/FJ.11-183046
REMARK 2
REMARK 2 RESOLUTION. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.76
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 46152
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) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.181
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2460
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) : 1.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.69
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3420
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.67
REMARK 3 BIN R VALUE (WORKING SET) : 0.2620
REMARK 3 BIN FREE R VALUE SET COUNT : 172
REMARK 3 BIN FREE R VALUE : 0.2760
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2362
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 13
REMARK 3 SOLVENT ATOMS : 202
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.15
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): 0.076
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.073
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.049
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.449
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.972
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.970
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2458 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3336 ; 1.472 ; 1.934
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 296 ; 5.924 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 118 ;38.505 ;24.492
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 435 ;12.401 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;11.248 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 370 ; 0.096 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1850 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 1474 ; 0.845 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2407 ; 1.643 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 984 ; 2.452 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 928 ; 4.202 ; 4.500
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 : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3PKF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-NOV-10.
REMARK 100 THE DEPOSITION ID IS D_1000062480.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-SEP-10
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM30A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9797
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48685
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 4.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.32700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: RIGID BODY
REMARK 200 SOFTWARE USED: RIGID BODY
REMARK 200 STARTING MODEL: PDB ENTRY 2IBA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10-15 MG.ML-1 URATE OXIDASE, 2 MG/ML 8
REMARK 280 -AZAXANTHINE, 50 MM TRIS/HCL PH 8.5, 5-8 % PEG 8000, 0-0.05 M
REMARK 280 NACL, BATCH, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 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 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+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 1.000000 0.000000 0.000000 40.18700
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 48.15100
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 52.77100
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 40.18700
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 48.15100
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 52.77100
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 40.18700
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 48.15100
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 52.77100
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 40.18700
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 48.15100
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 52.77100
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 26740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -162.0 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 -1.000000 0.000000 0.000000 80.37400
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 96.30200
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 80.37400
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 105.54200
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 96.30200
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 105.54200
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 613 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 SER A 296
REMARK 465 LEU A 297
REMARK 465 LYS A 298
REMARK 465 SER A 299
REMARK 465 LYS A 300
REMARK 465 LEU A 301
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS A 290 CB CYS A 290 SG -0.109
REMARK 500
REMARK 500 REMARK: NULL
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 CYS A 290 CA - CB - SG ANGL. DEV. = 8.0 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 HIS A 118 26.39 -151.70
REMARK 500 SER A 124 156.78 90.40
REMARK 500 ASP A 175 110.00 -162.21
REMARK 500 SER A 226 164.11 175.70
REMARK 500 ASN A 270 21.36 -140.17
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 NA A 303 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE A 88 O
REMARK 620 2 TYR A 91 O 89.2
REMARK 620 3 ILE A 94 O 109.1 80.9
REMARK 620 4 GLU A 136 OE1 112.4 156.9 84.1
REMARK 620 5 HOH A 558 O 92.0 98.6 158.8 89.2
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZA A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 303
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3PJK RELATED DB: PDB
REMARK 900 RELATED ID: 3PK3 RELATED DB: PDB
REMARK 900 RELATED ID: 3PK4 RELATED DB: PDB
REMARK 900 RELATED ID: 3PK5 RELATED DB: PDB
REMARK 900 RELATED ID: 3PK6 RELATED DB: PDB
REMARK 900 RELATED ID: 3PK8 RELATED DB: PDB
REMARK 900 RELATED ID: 3PKG RELATED DB: PDB
REMARK 900 RELATED ID: 3PKH RELATED DB: PDB
REMARK 900 RELATED ID: 3PKK RELATED DB: PDB
REMARK 900 RELATED ID: 3PKL RELATED DB: PDB
REMARK 900 RELATED ID: 3PKS RELATED DB: PDB
REMARK 900 RELATED ID: 3PKT RELATED DB: PDB
REMARK 900 RELATED ID: 3PKU RELATED DB: PDB
REMARK 900 RELATED ID: 3PLE RELATED DB: PDB
REMARK 900 RELATED ID: 3PLG RELATED DB: PDB
REMARK 900 RELATED ID: 3PLH RELATED DB: PDB
REMARK 900 RELATED ID: 3PLI RELATED DB: PDB
REMARK 900 RELATED ID: 3PLJ RELATED DB: PDB
REMARK 900 RELATED ID: 3PLM RELATED DB: PDB
REMARK 900 RELATED ID: 2IC0 RELATED DB: PDB
REMARK 900 RELATED ID: 2ICQ RELATED DB: PDB
REMARK 900 RELATED ID: 2IBA RELATED DB: PDB
DBREF 3PKF A 1 301 UNP Q00511 URIC_ASPFL 2 302
SEQADV 3PKF ACE A 0 UNP Q00511 ACETYLATION
SEQRES 1 A 302 ACE SER ALA VAL LYS ALA ALA ARG TYR GLY LYS ASP ASN
SEQRES 2 A 302 VAL ARG VAL TYR LYS VAL HIS LYS ASP GLU LYS THR GLY
SEQRES 3 A 302 VAL GLN THR VAL TYR GLU MET THR VAL CYS VAL LEU LEU
SEQRES 4 A 302 GLU GLY GLU ILE GLU THR SER TYR THR LYS ALA ASP ASN
SEQRES 5 A 302 SER VAL ILE VAL ALA THR ASP SER ILE LYS ASN THR ILE
SEQRES 6 A 302 TYR ILE THR ALA LYS GLN ASN PRO VAL THR PRO PRO GLU
SEQRES 7 A 302 LEU PHE GLY SER ILE LEU GLY THR HIS PHE ILE GLU LYS
SEQRES 8 A 302 TYR ASN HIS ILE HIS ALA ALA HIS VAL ASN ILE VAL CYS
SEQRES 9 A 302 HIS ARG TRP THR ARG MET ASP ILE ASP GLY LYS PRO HIS
SEQRES 10 A 302 PRO HIS SER PHE ILE ARG ASP SER GLU GLU LYS ARG ASN
SEQRES 11 A 302 VAL GLN VAL ASP VAL VAL GLU GLY LYS GLY ILE ASP ILE
SEQRES 12 A 302 LYS SER SER LEU SER GLY LEU THR VAL LEU LYS SER THR
SEQRES 13 A 302 ASN SER GLN PHE TRP GLY PHE LEU ARG ASP GLU TYR THR
SEQRES 14 A 302 THR LEU LYS GLU THR TRP ASP ARG ILE LEU SER THR ASP
SEQRES 15 A 302 VAL ASP ALA THR TRP GLN TRP LYS ASN PHE SER GLY LEU
SEQRES 16 A 302 GLN GLU VAL ARG SER HIS VAL PRO LYS PHE ASP ALA THR
SEQRES 17 A 302 TRP ALA THR ALA ARG GLU VAL THR LEU LYS THR PHE ALA
SEQRES 18 A 302 GLU ASP ASN SER ALA SER VAL GLN ALA THR MET TYR LYS
SEQRES 19 A 302 MET ALA GLU GLN ILE LEU ALA ARG GLN GLN LEU ILE GLU
SEQRES 20 A 302 THR VAL GLU TYR SER LEU PRO ASN LYS HIS TYR PHE GLU
SEQRES 21 A 302 ILE ASP LEU SER TRP HIS LYS GLY LEU GLN ASN THR GLY
SEQRES 22 A 302 LYS ASN ALA GLU VAL PHE ALA PRO GLN SER ASP PRO ASN
SEQRES 23 A 302 GLY LEU ILE LYS CYS THR VAL GLY ARG SER SER LEU LYS
SEQRES 24 A 302 SER LYS LEU
HET ACE A 0 3
HET AZA A 302 11
HET NA A 303 1
HET XE A 801 1
HETNAM ACE ACETYL GROUP
HETNAM AZA 8-AZAXANTHINE
HETNAM NA SODIUM ION
HETNAM XE XENON
FORMUL 1 ACE C2 H4 O
FORMUL 2 AZA C4 H3 N5 O2
FORMUL 3 NA NA 1+
FORMUL 4 XE XE
FORMUL 5 HOH *202(H2 O)
HELIX 1 1 ILE A 42 LYS A 48 1 7
HELIX 2 2 ASP A 50 ILE A 54 5 5
HELIX 3 3 ALA A 56 ASN A 71 1 16
HELIX 4 4 PRO A 75 TYR A 91 1 17
HELIX 5 5 GLY A 193 HIS A 200 1 8
HELIX 6 6 HIS A 200 ASP A 222 1 23
HELIX 7 7 SER A 226 GLN A 242 1 17
HELIX 8 8 THR A 271 ALA A 275 5 5
SHEET 1 A 8 TYR A 8 LYS A 20 0
SHEET 2 A 8 GLN A 27 GLY A 40 -1 O LEU A 38 N TYR A 8
SHEET 3 A 8 ILE A 94 HIS A 104 -1 O HIS A 98 N LEU A 37
SHEET 4 A 8 LYS A 127 VAL A 135 -1 O VAL A 132 N VAL A 99
SHEET 5 A 8 GLY A 139 LYS A 153 -1 O ASP A 141 N ASP A 133
SHEET 6 A 8 LEU A 178 TRP A 188 -1 O VAL A 182 N LEU A 149
SHEET 7 A 8 ILE A 245 ASN A 254 -1 O GLU A 246 N GLN A 187
SHEET 8 A 8 GLY A 286 GLY A 293 -1 O VAL A 292 N VAL A 248
SHEET 1 B 2 THR A 107 ILE A 111 0
SHEET 2 B 2 LYS A 114 ILE A 121 -1 O HIS A 116 N MET A 109
SHEET 1 C 2 TYR A 257 GLU A 259 0
SHEET 2 C 2 PHE A 278 PRO A 280 -1 O ALA A 279 N PHE A 258
LINK C ACE A 0 N SER A 1 1555 1555 1.34
LINK O ILE A 88 NA NA A 303 1555 1555 2.34
LINK O TYR A 91 NA NA A 303 1555 1555 2.70
LINK O ILE A 94 NA NA A 303 1555 1555 2.46
LINK OE1 GLU A 136 NA NA A 303 1555 1555 2.71
LINK NA NA A 303 O HOH A 558 1555 1555 2.35
CISPEP 1 THR A 74 PRO A 75 0 -9.26
CISPEP 2 ASP A 283 PRO A 284 0 -8.60
SITE 1 AC1 10 ILE A 54 ALA A 56 THR A 57 PHE A 159
SITE 2 AC1 10 ARG A 176 SER A 226 VAL A 227 GLN A 228
SITE 3 AC1 10 ASN A 254 HOH A 409
SITE 1 AC2 6 ILE A 88 TYR A 91 ASN A 92 ILE A 94
SITE 2 AC2 6 GLU A 136 HOH A 558
CRYST1 80.374 96.302 105.542 90.00 90.00 90.00 I 2 2 2 8
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 0.012442 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010384 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009475 0.00000
HETATM 1 C ACE A 0 62.088 57.713 20.050 1.00 38.18 C
HETATM 2 O ACE A 0 61.567 56.671 19.631 1.00 39.12 O
HETATM 3 CH3 ACE A 0 63.425 58.192 19.547 1.00 38.74 C
(ATOM LINES ARE NOT SHOWN.)
END
