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HEADER OXIDOREDUCTASE 16-JUL-09 3IBT
TITLE STRUCTURE OF 1H-3-HYDROXY-4-OXOQUINOLINE 2,4-DIOXYGENASE
TITLE 2 (QDO)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 1H-3-HYDROXY-4-OXOQUINOLINE 2,4-DIOXYGENASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 1.13.11.47;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS PUTIDA;
SOURCE 3 ORGANISM_TAXID: 303;
SOURCE 4 GENE: QDO;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS QDO, DIOXYGENASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.J.OAKLEY
REVDAT 1 02-FEB-10 3IBT 0
JRNL AUTH R.A.STEINER,H.J.JANSSEN,P.ROVERSI,A.J.OAKLEY,
JRNL AUTH 2 S.FETZNER
JRNL TITL STRUCTURAL BASIS FOR COFACTOR-INDEPENDENT
JRNL TITL 2 DIOXYGENATION OF N-HETEROAROMATIC COMPOUNDS AT THE
JRNL TITL 3 ALPHA/BETA-HYDROLASE FOLD.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 107 657 2010
JRNL REFN ISSN 0027-8424
JRNL PMID 20080731
JRNL DOI 10.1073/PNAS.0909033107
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : -1.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 3 NUMBER OF REFLECTIONS : 11976
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) : 0.237
REMARK 3 R VALUE (WORKING SET) : 0.237
REMARK 3 FREE R VALUE : 0.279
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 617
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 696
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 78.94
REMARK 3 BIN R VALUE (WORKING SET) : 0.3750
REMARK 3 BIN FREE R VALUE SET COUNT : 31
REMARK 3 BIN FREE R VALUE : 0.3820
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2138
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 32
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 69.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 73.34
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.64000
REMARK 3 B22 (A**2) : 3.64000
REMARK 3 B33 (A**2) : -5.46000
REMARK 3 B12 (A**2) : 1.82000
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): 0.515
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.318
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.378
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 44.982
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.938
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.919
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2208 ; 0.019 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3009 ; 1.731 ; 1.917
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 262 ; 7.355 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 120 ;38.853 ;23.917
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 340 ;21.087 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 15 ;21.044 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 307 ; 0.110 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1765 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1081 ; 0.259 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1477 ; 0.327 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 84 ; 0.148 ; 0.200
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): 20 ; 0.226 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 4 ; 0.333 ; 0.200
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): 1340 ; 0.811 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2122 ; 1.191 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 991 ; 1.866 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 887 ; 2.892 ; 4.500
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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 263
REMARK 3 ORIGIN FOR THE GROUP (A): 10.1859 28.2735 59.9516
REMARK 3 T TENSOR
REMARK 3 T11: -0.3175 T22: 0.0821
REMARK 3 T33: -0.1445 T12: -0.2517
REMARK 3 T13: 0.0949 T23: -0.2725
REMARK 3 L TENSOR
REMARK 3 L11: 2.6800 L22: 3.1009
REMARK 3 L33: 6.6671 L12: -0.2956
REMARK 3 L13: -1.7753 L23: -0.8995
REMARK 3 S TENSOR
REMARK 3 S11: -0.4069 S12: 0.8380 S13: -0.5275
REMARK 3 S21: 0.1518 S22: 0.1578 S23: 0.3171
REMARK 3 S31: 0.7349 S32: -1.3361 S33: 0.2491
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: NULL
REMARK 4
REMARK 4 3IBT COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-JUL-09.
REMARK 100 THE RCSB ID CODE IS RCSB054216.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97929
REMARK 200 MONOCHROMATOR : BEAMLINE OPTICS
REMARK 200 OPTICS : BEAMLINE OPTICS
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
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 : 22906
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : 0.05500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.16800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 4.1-4.6M SODIUM FORMATE, PH 7.8,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 56.24500
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 112.49000
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 84.36750
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 140.61250
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 28.12250
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 56.24500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 112.49000
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 140.61250
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 84.36750
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 28.12250
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 ALA A 264
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 ARG A 56 NE ARG A 56 CZ 0.080
REMARK 500 ARG A 56 CZ ARG A 56 NH1 0.119
REMARK 500 ASP A 76 CG ASP A 76 OD1 0.203
REMARK 500 ASP A 76 CG ASP A 76 OD2 0.139
REMARK 500 GLU A 176 CD GLU A 176 OE1 0.079
REMARK 500 GLU A 176 CD GLU A 176 OE2 0.071
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 ASP A 33 CB - CG - OD1 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ARG A 56 NE - CZ - NH2 ANGL. DEV. = -3.8 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 GLN A 2 130.50 -32.19
REMARK 500 ASN A 7 -126.43 45.00
REMARK 500 THR A 9 -152.06 -146.63
REMARK 500 HIS A 20 56.75 -90.91
REMARK 500 ARG A 56 126.27 -27.06
REMARK 500 GLN A 62 77.52 22.25
REMARK 500 ASP A 64 -163.23 -77.95
REMARK 500 SER A 65 -179.80 137.71
REMARK 500 PHE A 80 -72.18 -85.15
REMARK 500 SER A 95 -123.08 52.86
REMARK 500 GLU A 155 -138.91 40.86
REMARK 500 THR A 156 32.78 -95.24
REMARK 500 ASN A 159 105.69 -59.59
REMARK 500 GLU A 169 -73.68 -82.29
REMARK 500 TYR A 212 144.26 -175.29
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY A 109 ALA A 110 149.74
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2WJ3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE COFACTOR-DEVOID 1-H-3-HYDROXY-4-
REMARK 900 OXOQUINALDINE 2,4-DIOXYGENASE (HOD) FROM ARTHROBACTER
REMARK 900 NITROGUAJACOLICUS RU61A
REMARK 900 RELATED ID: 2WJ4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE COFACTOR-DEVOID 1-H-3-HYDROXY-4-
REMARK 900 OXOQUINALDINE 2,4-DIOXYGENASE (HOD) FROM ARTHROBACTER
REMARK 900 NITROGUAJACOLICUS RU61A ANAEROBICALLY COMPLEXED WITH ITS
REMARK 900 NATURAL SUBSTRATE 1-H-3-HYDROXY-4-OXOQUINALDINE
REMARK 900 RELATED ID: 2WJ6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE COFACTOR-DEVOID 1-H-3-HYDROXY-4-
REMARK 900 OXOQUINALDINE 2,4-DIOXYGENASE (HOD) FROM ARTHROBACTER
REMARK 900 NITROGUAJACOLICUS RU61A COMPLEXED WITH ITS NATURAL
REMARK 900 SUBSTRATE N- ACETYLANTHRANILATE
REMARK 900 RELATED ID: 2WM2 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE COFACTOR-DEVOID 1-H-3-HYDROXY-4-
REMARK 900 OXOQUINALDINE 2,4-DIOXYGENASE (HOD) FROM ARTHROBACTER
REMARK 900 NITROGUAJACOLICUS RU61A IN COMPLEX WITH CHLORIDE
DBREF 3IBT A 1 264 UNP O33472 O33472_PSEPU 1 264
SEQADV 3IBT ILE A 118 UNP O33472 VAL 118 CONFLICT
SEQADV 3IBT ASP A 200 UNP O33472 GLU 200 CONFLICT
SEQADV 3IBT GLU A 226 UNP O33472 ASP 226 CONFLICT
SEQRES 1 A 264 MSE GLN SER LEU ASN VAL ASN GLY THR LEU MSE THR TYR
SEQRES 2 A 264 SER GLU SER GLY ASP PRO HIS ALA PRO THR LEU PHE LEU
SEQRES 3 A 264 LEU SER GLY TRP CYS GLN ASP HIS ARG LEU PHE LYS ASN
SEQRES 4 A 264 LEU ALA PRO LEU LEU ALA ARG ASP PHE HIS VAL ILE CYS
SEQRES 5 A 264 PRO ASP TRP ARG GLY HIS ASP ALA LYS GLN THR ASP SER
SEQRES 6 A 264 GLY ASP PHE ASP SER GLN THR LEU ALA GLN ASP LEU LEU
SEQRES 7 A 264 ALA PHE ILE ASP ALA LYS GLY ILE ARG ASP PHE GLN MSE
SEQRES 8 A 264 VAL SER THR SER HIS GLY CYS TRP VAL ASN ILE ASP VAL
SEQRES 9 A 264 CYS GLU GLN LEU GLY ALA ALA ARG LEU PRO LYS THR ILE
SEQRES 10 A 264 ILE ILE ASP TRP LEU LEU GLN PRO HIS PRO GLY PHE TRP
SEQRES 11 A 264 GLN GLN LEU ALA GLU GLY GLN HIS PRO THR GLU TYR VAL
SEQRES 12 A 264 ALA GLY ARG GLN SER PHE PHE ASP GLU TRP ALA GLU THR
SEQRES 13 A 264 THR ASP ASN ALA ASP VAL LEU ASN HIS LEU ARG ASN GLU
SEQRES 14 A 264 MSE PRO TRP PHE HIS GLY GLU MSE TRP GLN ARG ALA CYS
SEQRES 15 A 264 ARG GLU ILE GLU ALA ASN TYR ARG THR TRP GLY SER PRO
SEQRES 16 A 264 LEU ASP ARG MSE ASP SER LEU PRO GLN LYS PRO GLU ILE
SEQRES 17 A 264 CYS HIS ILE TYR SER GLN PRO LEU SER GLN ASP TYR ARG
SEQRES 18 A 264 GLN LEU GLN LEU GLU PHE ALA ALA GLY HIS SER TRP PHE
SEQRES 19 A 264 HIS PRO ARG HIS ILE PRO GLY ARG THR HIS PHE PRO SER
SEQRES 20 A 264 LEU GLU ASN PRO VAL ALA VAL ALA GLN ALA ILE ARG GLU
SEQRES 21 A 264 PHE LEU GLN ALA
MODRES 3IBT MSE A 1 MET SELENOMETHIONINE
MODRES 3IBT MSE A 11 MET SELENOMETHIONINE
MODRES 3IBT MSE A 91 MET SELENOMETHIONINE
MODRES 3IBT MSE A 170 MET SELENOMETHIONINE
MODRES 3IBT MSE A 177 MET SELENOMETHIONINE
MODRES 3IBT MSE A 199 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 11 8
HET MSE A 91 8
HET MSE A 170 8
HET MSE A 177 8
HET MSE A 199 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 6(C5 H11 N O2 SE)
FORMUL 2 HOH *32(H2 O)
HELIX 1 1 ASP A 33 LYS A 38 5 6
HELIX 2 2 ASN A 39 ALA A 45 1 7
HELIX 3 3 ASP A 69 LYS A 84 1 16
HELIX 4 4 HIS A 96 LEU A 108 1 13
HELIX 5 5 HIS A 126 GLY A 136 1 11
HELIX 6 6 GLU A 141 GLU A 155 1 15
HELIX 7 7 ASN A 159 GLU A 169 1 11
HELIX 8 8 MSE A 170 PHE A 173 5 4
HELIX 9 9 HIS A 174 GLY A 193 1 20
HELIX 10 10 SER A 194 SER A 201 1 8
HELIX 11 11 SER A 217 HIS A 231 1 15
HELIX 12 12 PHE A 245 ASN A 250 1 6
HELIX 13 13 ASN A 250 LEU A 262 1 13
SHEET 1 A 2 ASN A 5 VAL A 6 0
SHEET 2 A 2 THR A 9 LEU A 10 -1 O THR A 9 N VAL A 6
SHEET 1 B 7 TYR A 13 SER A 16 0
SHEET 2 B 7 HIS A 49 PRO A 53 -1 O CYS A 52 N SER A 14
SHEET 3 B 7 THR A 23 LEU A 27 1 N LEU A 26 O ILE A 51
SHEET 4 B 7 PHE A 89 THR A 94 1 O VAL A 92 N LEU A 27
SHEET 5 B 7 LYS A 115 ILE A 119 1 O ILE A 117 N SER A 93
SHEET 6 B 7 GLU A 207 TYR A 212 1 O ILE A 211 N ILE A 118
SHEET 7 B 7 PHE A 234 HIS A 238 1 O ARG A 237 N HIS A 210
LINK C MSE A 1 N GLN A 2 1555 1555 1.34
LINK C LEU A 10 N MSE A 11 1555 1555 1.33
LINK C MSE A 11 N THR A 12 1555 1555 1.37
LINK C GLN A 90 N MSE A 91 1555 1555 1.34
LINK C MSE A 91 N VAL A 92 1555 1555 1.32
LINK C GLU A 169 N MSE A 170 1555 1555 1.33
LINK C MSE A 170 N PRO A 171 1555 1555 1.35
LINK C GLU A 176 N MSE A 177 1555 1555 1.32
LINK C MSE A 177 N TRP A 178 1555 1555 1.33
LINK C ARG A 198 N MSE A 199 1555 1555 1.34
LINK C MSE A 199 N ASP A 200 1555 1555 1.32
CISPEP 1 GLN A 214 PRO A 215 0 -3.17
CRYST1 90.138 90.138 168.735 90.00 90.00 120.00 P 61 2 2 12
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 0.011094 0.006405 0.000000 0.00000
SCALE2 0.000000 0.012810 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005926 0.00000
TER 2139 GLN A 263
MASTER 395 0 6 13 9 0 0 6 2170 1 59 21
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