HEADER OXIDOREDUCTASE, ELECTRON TRANSPORT 05-JAN-07 2OG7
TITLE CYSTAL STRUCTURE OF ASPARAGINE OXYGENASE IN COMPLEX WITH FE(II), 2S,
TITLE 2 3S-3-HYDROXYASPARAGINE AND SUCCINATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ASPARAGINE OXYGENASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PUTATIVE OXYGENASE;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES COELICOLOR A3(2);
SOURCE 3 ORGANISM_TAXID: 100226;
SOURCE 4 STRAIN: DSMZ 40783;
SOURCE 5 GENE: SCO3236 (ASNO);
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PQTEVMS01;
SOURCE 11 OTHER_DETAILS: EXPRESSION PLASMID ENCODES FOR N-TERMINAL HIS-7-TAG
SOURCE 12 FOR IMAC
KEYWDS NONRIBOSOMAL PEPTIDE SYNTHESIS; NON-HEME IRON(II); ALPHA-
KEYWDS 2 KETOGLUTARATE OXYGENASE; BETA-HYDROXYLATED AMINO ACID,
KEYWDS 3 OXIDOREDUCTASE, ELECTRON TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR L.-O.ESSEN,M.STRIEKER
REVDAT 6 30-AUG-23 2OG7 1 REMARK SEQADV LINK
REVDAT 5 18-OCT-17 2OG7 1 REMARK
REVDAT 4 13-JUL-11 2OG7 1 VERSN
REVDAT 3 24-FEB-09 2OG7 1 VERSN
REVDAT 2 10-APR-07 2OG7 1 JRNL
REVDAT 1 06-MAR-07 2OG7 0
JRNL AUTH M.STRIEKER,F.KOPP,C.MAHLERT,L.-O.ESSEN,M.A.MARAHIEL
JRNL TITL MECHANISTIC AND STRUCTURAL BASIS OF STEREOSPECIFIC
JRNL TITL 2 CBETA-HYDROXYLATION IN CALCIUM-DEPENDENT ANTIBIOTIC, A
JRNL TITL 3 DAPTOMYCIN-TYPE LIPOPEPTIDE
JRNL REF ACS CHEM.BIOL. V. 2 187 2007
JRNL REFN ISSN 1554-8929
JRNL PMID 17373765
JRNL DOI 10.1021/CB700012Y
REMARK 2
REMARK 2 RESOLUTION. 1.66 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) : 1.66
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 22.91
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 51776
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) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.184
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1582
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) : 1.66
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.70
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3535
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.98
REMARK 3 BIN R VALUE (WORKING SET) : 0.2600
REMARK 3 BIN FREE R VALUE SET COUNT : 95
REMARK 3 BIN FREE R VALUE : 0.2420
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2448
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 19
REMARK 3 SOLVENT ATOMS : 258
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 24.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.14
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.54000
REMARK 3 B22 (A**2) : 0.54000
REMARK 3 B33 (A**2) : -0.81000
REMARK 3 B12 (A**2) : 0.27000
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): 0.074
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.072
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.053
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.518
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.971
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.963
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2522 ; 0.008 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 1723 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3444 ; 1.178 ; 1.975
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4154 ; 0.871 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 318 ; 8.557 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 118 ;34.140 ;22.458
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 375 ;11.370 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 31 ;17.864 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 385 ; 0.061 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2866 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 529 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 512 ; 0.211 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1926 ; 0.208 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1235 ; 0.170 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1376 ; 0.083 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 176 ; 0.177 ; 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): 18 ; 0.129 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 70 ; 0.338 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 26 ; 0.195 ; 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): 2048 ; 0.775 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 636 ; 0.127 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2572 ; 0.845 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1041 ; 1.574 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 872 ; 2.408 ; 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 : 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 11 A 329
REMARK 3 ORIGIN FOR THE GROUP (A): -5.2883 62.4197 -12.4550
REMARK 3 T TENSOR
REMARK 3 T11: -0.0633 T22: -0.0460
REMARK 3 T33: -0.0881 T12: -0.0248
REMARK 3 T13: -0.0113 T23: -0.0063
REMARK 3 L TENSOR
REMARK 3 L11: 0.2002 L22: 2.9160
REMARK 3 L33: 0.5093 L12: 0.1254
REMARK 3 L13: -0.0722 L23: -0.3454
REMARK 3 S TENSOR
REMARK 3 S11: 0.1249 S12: -0.0433 S13: -0.0017
REMARK 3 S21: 0.0701 S22: -0.2363 S23: 0.0101
REMARK 3 S31: 0.0521 S32: -0.0208 S33: 0.1113
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2OG7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JAN-07.
REMARK 100 THE DEPOSITION ID IS D_1000041095.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-JUN-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X13
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8080
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51815
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 23.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 3.690
REMARK 200 R MERGE (I) : 0.05200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.1000
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 (%) : 98.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.49
REMARK 200 R MERGE FOR SHELL (I) : 0.53900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1DRY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.5 M SODIUM ACETATE, 0.1 M HEPES, PH
REMARK 280 4.6, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
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 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 30.28900
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 60.57800
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 60.57800
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 30.28900
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 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 A7218 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 MET A -23
REMARK 465 LYS A -22
REMARK 465 HIS A -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 SER A -14
REMARK 465 ASP A -13
REMARK 465 TYR A -12
REMARK 465 ASP A -11
REMARK 465 ILE A -10
REMARK 465 PRO A -9
REMARK 465 THR A -8
REMARK 465 THR A -7
REMARK 465 GLU A -6
REMARK 465 ASN A -5
REMARK 465 LEU A -4
REMARK 465 TYR A -3
REMARK 465 PHE A -2
REMARK 465 GLN A -1
REMARK 465 GLY A 0
REMARK 465 SER A 1
REMARK 465 ALA A 2
REMARK 465 ALA A 3
REMARK 465 ASN A 4
REMARK 465 ALA A 5
REMARK 465 ALA A 6
REMARK 465 GLY A 7
REMARK 465 PRO A 8
REMARK 465 ALA A 9
REMARK 465 SER A 10
REMARK 465 PRO A 330
REMARK 465 GLN A 331
REMARK 465 PRO A 332
REMARK 465 ALA A 333
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 7023 O HOH A 7211 1.69
REMARK 500 O HOH A 7018 O HOH A 7172 1.96
REMARK 500 O HOH A 7103 O HOH A 7174 2.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 7104 O HOH A 7104 5674 2.12
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 PHE A 216 GLN A 217 119.94
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 FE2 A5001 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 155 NE2
REMARK 620 2 GLU A 157 OE1 102.5
REMARK 620 3 HIS A 287 NE2 85.0 86.2
REMARK 620 4 SIN A6001 O2 156.3 99.8 88.6
REMARK 620 5 SIN A6001 O1 97.7 157.8 86.4 59.2
REMARK 620 6 AHB A7002 OB 93.0 93.2 177.8 93.6 95.0
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 A 5001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIN A 6001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AHB A 7002
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2OG5 RELATED DB: PDB
REMARK 900 APO FORM OF ASPARAGINE OXYGENASE
REMARK 900 RELATED ID: 2OG6 RELATED DB: PDB
REMARK 900 ASPARAGINE OXYGENASE WITH FE(II)
DBREF 2OG7 A -23 333 UNP Q9Z4Z5 Q9Z4Z5_STRCO 1 333
SEQADV 2OG7 LYS A -22 UNP Q9Z4Z5 EXPRESSION TAG
SEQADV 2OG7 HIS A -21 UNP Q9Z4Z5 EXPRESSION TAG
SEQADV 2OG7 HIS A -20 UNP Q9Z4Z5 EXPRESSION TAG
SEQADV 2OG7 HIS A -19 UNP Q9Z4Z5 EXPRESSION TAG
SEQADV 2OG7 HIS A -18 UNP Q9Z4Z5 EXPRESSION TAG
SEQADV 2OG7 HIS A -17 UNP Q9Z4Z5 EXPRESSION TAG
SEQADV 2OG7 HIS A -16 UNP Q9Z4Z5 EXPRESSION TAG
SEQADV 2OG7 HIS A -15 UNP Q9Z4Z5 EXPRESSION TAG
SEQADV 2OG7 SER A -14 UNP Q9Z4Z5 CLONING ARTIFACT
SEQADV 2OG7 ASP A -13 UNP Q9Z4Z5 CLONING ARTIFACT
SEQADV 2OG7 TYR A -12 UNP Q9Z4Z5 CLONING ARTIFACT
SEQADV 2OG7 ASP A -11 UNP Q9Z4Z5 CLONING ARTIFACT
SEQADV 2OG7 ILE A -10 UNP Q9Z4Z5 CLONING ARTIFACT
SEQADV 2OG7 PRO A -9 UNP Q9Z4Z5 CLONING ARTIFACT
SEQADV 2OG7 THR A -8 UNP Q9Z4Z5 CLONING ARTIFACT
SEQADV 2OG7 THR A -7 UNP Q9Z4Z5 CLONING ARTIFACT
SEQADV 2OG7 GLU A -6 UNP Q9Z4Z5 CLONING ARTIFACT
SEQADV 2OG7 ASN A -5 UNP Q9Z4Z5 CLONING ARTIFACT
SEQADV 2OG7 LEU A -4 UNP Q9Z4Z5 CLONING ARTIFACT
SEQADV 2OG7 TYR A -3 UNP Q9Z4Z5 CLONING ARTIFACT
SEQADV 2OG7 PHE A -2 UNP Q9Z4Z5 CLONING ARTIFACT
SEQADV 2OG7 GLN A -1 UNP Q9Z4Z5 CLONING ARTIFACT
SEQADV 2OG7 GLY A 0 UNP Q9Z4Z5 CLONING ARTIFACT
SEQADV 2OG7 SER A 1 UNP Q9Z4Z5 CLONING ARTIFACT
SEQRES 1 A 357 MET LYS HIS HIS HIS HIS HIS HIS HIS SER ASP TYR ASP
SEQRES 2 A 357 ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY SER ALA
SEQRES 3 A 357 ALA ASN ALA ALA GLY PRO ALA SER ARG TYR ASP VAL THR
SEQRES 4 A 357 LEU ASP GLN SER ASP ALA GLU LEU VAL GLU GLU ILE ALA
SEQRES 5 A 357 TRP LYS LEU ALA THR GLN ALA THR GLY ARG PRO ASP ASP
SEQRES 6 A 357 ALA GLU TRP VAL GLU ALA ALA ARG ASN ALA TRP HIS ALA
SEQRES 7 A 357 TRP PRO ALA THR LEU ARG ARG ASP LEU ALA GLY PHE ARG
SEQRES 8 A 357 ARG ASP SER GLY PRO ASP GLY ALA ILE VAL LEU ARG GLY
SEQRES 9 A 357 LEU PRO VAL ASP SER MET GLY LEU PRO PRO THR PRO ARG
SEQRES 10 A 357 VAL ASN GLY SER VAL GLN ARG GLU ALA SER LEU GLY ALA
SEQRES 11 A 357 ALA VAL LEU LEU MET THR ALA CYS GLY LEU GLY ASP PRO
SEQRES 12 A 357 GLY ALA PHE LEU PRO GLU LYS ASN GLY ALA LEU VAL GLN
SEQRES 13 A 357 ASP VAL VAL PRO VAL PRO GLY MET GLU GLU PHE GLN GLY
SEQRES 14 A 357 ASN ALA GLY SER THR LEU LEU THR PHE HIS ASN GLU ASN
SEQRES 15 A 357 ALA PHE HIS GLU HIS ARG PRO ASP PHE VAL MET LEU LEU
SEQRES 16 A 357 CYS LEU ARG ALA ASP PRO THR GLY ARG ALA GLY LEU ARG
SEQRES 17 A 357 THR ALA CYS VAL ARG ARG VAL LEU PRO LEU LEU SER ASP
SEQRES 18 A 357 SER THR VAL ASP ALA LEU TRP ALA PRO GLU PHE ARG THR
SEQRES 19 A 357 ALA PRO PRO PRO SER PHE GLN LEU SER GLY PRO GLU GLU
SEQRES 20 A 357 ALA PRO ALA PRO VAL LEU LEU GLY ASP ARG SER ASP PRO
SEQRES 21 A 357 ASP LEU ARG VAL ASP LEU ALA ALA THR GLU PRO VAL THR
SEQRES 22 A 357 GLU ARG ALA ALA GLU ALA LEU ARG GLU LEU GLN ALA HIS
SEQRES 23 A 357 PHE ASP ALA THR ALA VAL THR HIS ARG LEU LEU PRO GLY
SEQRES 24 A 357 GLU LEU ALA ILE VAL ASP ASN ARG VAL THR VAL HIS GLY
SEQRES 25 A 357 ARG THR GLU PHE THR PRO ARG TYR ASP GLY THR ASP ARG
SEQRES 26 A 357 TRP LEU GLN ARG THR PHE VAL LEU THR ASP LEU ARG ARG
SEQRES 27 A 357 SER ARG ALA MET ARG PRO ALA ASP GLY TYR VAL LEU GLY
SEQRES 28 A 357 ALA ALA PRO GLN PRO ALA
HET FE2 A5001 1
HET SIN A6001 8
HET AHB A7002 10
HETNAM FE2 FE (II) ION
HETNAM SIN SUCCINIC ACID
HETNAM AHB BETA-HYDROXYASPARAGINE
FORMUL 2 FE2 FE 2+
FORMUL 3 SIN C4 H6 O4
FORMUL 4 AHB C4 H8 N2 O4
FORMUL 5 HOH *258(H2 O)
HELIX 1 1 ASP A 17 ALA A 35 1 19
HELIX 2 2 ASP A 41 HIS A 53 1 13
HELIX 3 3 PRO A 56 ASP A 69 1 14
HELIX 4 4 SER A 103 GLY A 117 1 15
HELIX 5 5 GLU A 125 ALA A 129 5 5
HELIX 6 6 VAL A 188 LEU A 192 1 5
HELIX 7 7 PRO A 193 LEU A 195 5 3
HELIX 8 8 SER A 196 TRP A 204 1 9
HELIX 9 9 THR A 249 ALA A 267 1 19
HELIX 10 10 ASP A 311 GLY A 323 5 13
SHEET 1 A 6 ASP A 13 THR A 15 0
SHEET 2 A 6 ALA A 75 ARG A 79 1 O ARG A 79 N VAL A 14
SHEET 3 A 6 LEU A 277 ASP A 281 -1 O ILE A 279 N ILE A 76
SHEET 4 A 6 PHE A 167 ARG A 174 -1 N VAL A 168 O VAL A 280
SHEET 5 A 6 TRP A 302 LEU A 309 -1 O GLN A 304 N LEU A 171
SHEET 6 A 6 GLN A 132 VAL A 134 -1 N VAL A 134 O LEU A 303
SHEET 1 B 7 ASP A 13 THR A 15 0
SHEET 2 B 7 ALA A 75 ARG A 79 1 O ARG A 79 N VAL A 14
SHEET 3 B 7 LEU A 277 ASP A 281 -1 O ILE A 279 N ILE A 76
SHEET 4 B 7 PHE A 167 ARG A 174 -1 N VAL A 168 O VAL A 280
SHEET 5 B 7 TRP A 302 LEU A 309 -1 O GLN A 304 N LEU A 171
SHEET 6 B 7 ASP A 118 PHE A 122 -1 N ASP A 118 O LEU A 309
SHEET 7 B 7 VAL A 325 LEU A 326 1 O LEU A 326 N ALA A 121
SHEET 1 C 4 LEU A 152 HIS A 155 0
SHEET 2 C 4 THR A 285 ARG A 289 -1 O ARG A 289 N LEU A 152
SHEET 3 C 4 LEU A 183 CYS A 187 -1 N ALA A 186 O VAL A 286
SHEET 4 C 4 VAL A 268 HIS A 270 -1 O HIS A 270 N LEU A 183
SHEET 1 D 2 PHE A 208 THR A 210 0
SHEET 2 D 2 THR A 245 PRO A 247 -1 O GLU A 246 N ARG A 209
SHEET 1 E 2 LEU A 229 GLY A 231 0
SHEET 2 E 2 PRO A 236 LEU A 238 -1 O ASP A 237 N LEU A 230
LINK NE2 HIS A 155 FE FE2 A5001 1555 1555 2.23
LINK OE1 GLU A 157 FE FE2 A5001 1555 1555 2.00
LINK NE2 HIS A 287 FE FE2 A5001 1555 1555 2.15
LINK FE FE2 A5001 O2 SIN A6001 1555 1555 2.34
LINK FE FE2 A5001 O1 SIN A6001 1555 1555 2.12
LINK FE FE2 A5001 OB AHB A7002 1555 1555 2.14
SITE 1 AC1 5 HIS A 155 GLU A 157 HIS A 287 SIN A6001
SITE 2 AC1 5 AHB A7002
SITE 1 AC2 13 VAL A 134 LEU A 152 HIS A 155 GLU A 157
SITE 2 AC2 13 LEU A 183 HIS A 287 ARG A 289 ARG A 301
SITE 3 AC2 13 ARG A 305 FE2 A5001 AHB A7002 HOH A7003
SITE 4 AC2 13 HOH A7229
SITE 1 AC3 15 GLU A 125 GLY A 145 ASN A 146 HIS A 155
SITE 2 AC3 15 GLU A 157 ASN A 158 PRO A 213 SER A 215
SITE 3 AC3 15 ASP A 241 ARG A 305 FE2 A5001 SIN A6001
SITE 4 AC3 15 HOH A7004 HOH A7005 HOH A7229
CRYST1 91.308 91.308 90.867 90.00 90.00 120.00 P 31 2 1 6
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 0.010952 0.006323 0.000000 0.00000
SCALE2 0.000000 0.012646 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011005 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
