HEADER OXIDOREDUCTASE 09-AUG-06 2J18
TITLE CHLOROPEROXIDASE MIXTURE OF FERRIC AND FERROUS STATES (LOW DOSE DATA
TITLE 2 SET)
CAVEAT 2J18 MAN B 3 HAS WRONG CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHLOROPEROXIDASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 22-319;
COMPND 5 SYNONYM: CHLORIDE PEROXIDASE, CPO;
COMPND 6 EC: 1.11.1.10;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CALDARIOMYCES FUMAGO;
SOURCE 3 ORGANISM_TAXID: 5474;
SOURCE 4 EXPRESSION_SYSTEM: CALDARIOMYCES FUMAGO;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 5474
KEYWDS OXIDOREDUCTASE, PYRROLIDONE CARBOXYLIC ACID, GLYCOPROTEIN, METAL-
KEYWDS 2 BINDING, IRON, HEME, CHLORIDE, MANGANESE, PEROXIDASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.BEITLICH,K.KUHNEL,C.SCHULZE-BRIESE,R.L.SHOEMAN,I.SCHLICHTING
REVDAT 5 13-DEC-23 2J18 1 HETSYN
REVDAT 4 29-JUL-20 2J18 1 CAVEAT COMPND REMARK HETNAM
REVDAT 4 2 1 LINK SITE ATOM
REVDAT 3 11-MAR-20 2J18 1 CAVEAT SEQRES LINK
REVDAT 2 24-FEB-09 2J18 1 VERSN
REVDAT 1 18-DEC-06 2J18 0
JRNL AUTH T.BEITLICH,K.KUHNEL,C.SCHULZE-BRIESE,R.L.SHOEMAN,
JRNL AUTH 2 I.SCHLICHTING
JRNL TITL CRYORADIOLYTIC REDUCTION OF CRYSTALLINE HEME PROTEINS:
JRNL TITL 2 ANALYSIS BY UV-VIS SPECTROSCOPY AND X-RAY CRYSTALLOGRAPHY
JRNL REF J.SYNCHROTRON RADIAT. V. 14 11 2007
JRNL REFN ISSN 0909-0495
JRNL PMID 17211068
JRNL DOI 10.1107/S0909049506049806
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.75
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 3 NUMBER OF REFLECTIONS : 41005
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) : 0.175
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2158
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) : 1.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.79
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3021
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2050
REMARK 3 BIN FREE R VALUE SET COUNT : 158
REMARK 3 BIN FREE R VALUE : 0.2540
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2316
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 249
REMARK 3 SOLVENT ATOMS : 360
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.27
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.41000
REMARK 3 B22 (A**2) : -1.11000
REMARK 3 B33 (A**2) : 0.70000
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): 0.098
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.099
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.060
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.829
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.946
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.923
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2703 ; 0.012 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3734 ; 1.376 ; 2.082
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 306 ; 5.680 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 120 ;35.576 ;24.833
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 331 ;11.615 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;16.598 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 428 ; 0.088 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2037 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1425 ; 0.205 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1934 ; 0.314 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 293 ; 0.129 ; 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): 28 ; 0.198 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 14 ; 0.139 ; 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): 1552 ; 0.681 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2477 ; 1.114 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1276 ; 1.827 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1255 ; 2.852 ; 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 : 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. THERE IS AN ELONGATED DENSITY ABOVE THE HEME, WHICH
REMARK 3 WAS MODELLED AS A SINGLE WATER MOLECULE IN TWO POSITIONS
REMARK 4
REMARK 4 2J18 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-AUG-06.
REMARK 100 THE DEPOSITION ID IS D_1290029643.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 90.0
REMARK 200 PH : 3.40
REMARK 200 NUMBER OF CRYSTALS USED : 11
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9761
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 185512
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : 0.13000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.39000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1CPO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM KBR, 20% PEG3000, 0.1 M SODIUM
REMARK 280 CITRATE PH3.4, PH 3.40
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
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
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 50.37500
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 50.37500
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 28.86500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 75.23000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 28.86500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 75.23000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 50.37500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 28.86500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 75.23000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 50.37500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 28.86500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 75.23000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
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: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 A2014 LIES ON A SPECIAL POSITION.
REMARK 400
REMARK 400 COMPOUND
REMARK 400 CATALYZES PEROXIDATIVE HALOGENATIONS INVOLVED IN THE
REMARK 400 BIOSYNTHESIS OF CLARDARIOMYCIN (2,2-DICHLORO-1,3-CYCLO-
REMARK 400 PENTENEDIONE). THE ENZYME ALSO HAS POTENT CATALASE ACTIVITY AND IN
REMARK 400 THE ABSENCE OF HALIDE ION, ACTS AS A PEROXIDASE SIMILAR TO PLANT
REMARK 400 PEROXIDASES.
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 CE2 TYR A 288 O HOH A 2317 2.11
REMARK 500 O HOH A 2043 O HOH A 2314 2.15
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 ALA A 102 -110.49 -144.13
REMARK 500 PRO A 220 44.06 -78.61
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 HEM A1300 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 29 SG
REMARK 620 2 HEM A1300 NA 100.1
REMARK 620 3 HEM A1300 NB 98.7 88.1
REMARK 620 4 HEM A1300 NC 91.6 168.4 90.2
REMARK 620 5 HEM A1300 ND 94.2 88.7 167.1 90.4
REMARK 620 6 HOH A2336 O 170.1 71.6 76.1 96.8 91.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A1299 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 104 OE2
REMARK 620 2 HIS A 105 O 82.9
REMARK 620 3 SER A 108 OG 175.0 100.1
REMARK 620 4 HEM A1300 O1A 104.7 88.4 79.5
REMARK 620 5 HOH A2333 O 88.3 90.6 87.6 166.7
REMARK 620 6 HOH A2334 O 85.5 167.5 91.8 90.1 93.7
REMARK 620 N 1 2 3 4 5
REMARK 630
REMARK 630 MOLECULE TYPE: OLIGOSACCHARIDE METABOLISM
REMARK 630 MOLECULE NAME: ALPHA-D-MANNOPYRANOSE
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 630 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 630
REMARK 630 M RES C SSSEQI
REMARK 630 MAN A 1307
REMARK 630 MAN A 1308
REMARK 630 MAN A 1309
REMARK 630 MAN A 1310
REMARK 630 MAN A 1311
REMARK 630 MAN A 1312
REMARK 630 MAN A 1313
REMARK 630 MAN A 1314
REMARK 630 MAN A 1317
REMARK 630 SOURCE: NULL
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP: NULL
REMARK 630 DETAILS: OLIGOSACCHARIDE
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CPO RELATED DB: PDB
REMARK 900 CHLOROPEROXIDASE
REMARK 900 RELATED ID: 2CIV RELATED DB: PDB
REMARK 900 CHLOROPEROXIDASE BROMIDE COMPLEX
REMARK 900 RELATED ID: 2CIW RELATED DB: PDB
REMARK 900 CHLOROPEROXIDASE IODIDE COMPLEX
REMARK 900 RELATED ID: 2CIX RELATED DB: PDB
REMARK 900 CHLOROPEROXIDASE COMPLEXED WITH CYCLOPENTANEDIONE
REMARK 900 RELATED ID: 2CIY RELATED DB: PDB
REMARK 900 CHLOROPEROXIDASE COMPLEXED WITH CYANIDE AND DMSO
REMARK 900 RELATED ID: 2CIZ RELATED DB: PDB
REMARK 900 CHLOROPEROXIDASE COMPLEXED WITH ACETATE
REMARK 900 RELATED ID: 2CJ0 RELATED DB: PDB
REMARK 900 CHLOROPEROXIDASE COMPLEXED WITH NITRATE
REMARK 900 RELATED ID: 2CJ1 RELATED DB: PDB
REMARK 900 CHLOROPEROXIDASE COMPLEXED WITH FORMATE ( ETHYLENE GLYCOL
REMARK 900 CRYOPROTECTANT)
REMARK 900 RELATED ID: 2CJ2 RELATED DB: PDB
REMARK 900 CHLOROPEROXIDASE COMPLEXED WITH FORMATE (SUGAR CRYOPROTECTANT)
REMARK 900 RELATED ID: 2CPO RELATED DB: PDB
REMARK 900 CHLOROPEROXIDASE
REMARK 900 RELATED ID: 2J19 RELATED DB: PDB
REMARK 900 FERROUS CHLOROPEROXIDASE (HIGH DOSE DATA SET)
DBREF 2J18 A 0 0 PDB 2J18 2J18 0 0
DBREF 2J18 A 1 298 UNP P04963 PRXC_CALFU 22 319
SEQRES 1 A 299 PCA GLU PRO GLY SER GLY ILE GLY TYR PRO TYR ASP ASN
SEQRES 2 A 299 ASN THR LEU PRO TYR VAL ALA PRO GLY PRO THR ASP SER
SEQRES 3 A 299 ARG ALA PRO CYS PRO ALA LEU ASN ALA LEU ALA ASN HIS
SEQRES 4 A 299 GLY TYR ILE PRO HIS ASP GLY ARG ALA ILE SER ARG GLU
SEQRES 5 A 299 THR LEU GLN ASN ALA PHE LEU ASN HIS MET GLY ILE ALA
SEQRES 6 A 299 ASN SER VAL ILE GLU LEU ALA LEU THR ASN ALA PHE VAL
SEQRES 7 A 299 VAL CYS GLU TYR VAL THR GLY SER ASP CYS GLY ASP SER
SEQRES 8 A 299 LEU VAL ASN LEU THR LEU LEU ALA GLU PRO HIS ALA PHE
SEQRES 9 A 299 GLU HIS ASP HIS SER PHE SER ARG LYS ASP TYR LYS GLN
SEQRES 10 A 299 GLY VAL ALA ASN SER ASN ASP PHE ILE ASP ASN ARG ASN
SEQRES 11 A 299 PHE ASP ALA GLU THR PHE GLN THR SER LEU ASP VAL VAL
SEQRES 12 A 299 ALA GLY LYS THR HIS PHE ASP TYR ALA ASP MET ASN GLU
SEQRES 13 A 299 ILE ARG LEU GLN ARG GLU SER LEU SER ASN GLU LEU ASP
SEQRES 14 A 299 PHE PRO GLY TRP PHE THR GLU SER LYS PRO ILE GLN ASN
SEQRES 15 A 299 VAL GLU SER GLY PHE ILE PHE ALA LEU VAL SER ASP PHE
SEQRES 16 A 299 ASN LEU PRO ASP ASN ASP GLU ASN PRO LEU VAL ARG ILE
SEQRES 17 A 299 ASP TRP TRP LYS TYR TRP PHE THR ASN GLU SER PHE PRO
SEQRES 18 A 299 TYR HIS LEU GLY TRP HIS PRO PRO SER PRO ALA ARG GLU
SEQRES 19 A 299 ILE GLU PHE VAL THR SER ALA SER SER ALA VAL LEU ALA
SEQRES 20 A 299 ALA SER VAL THR SER THR PRO SER SER LEU PRO SER GLY
SEQRES 21 A 299 ALA ILE GLY PRO GLY ALA GLU ALA VAL PRO LEU SER PHE
SEQRES 22 A 299 ALA SER THR MET THR PRO PHE LEU LEU ALA THR ASN ALA
SEQRES 23 A 299 PRO TYR TYR ALA GLN ASP PRO THR LEU GLY PRO ASN ASP
MODRES 2J18 ASN A 12 ASN GLYCOSYLATION SITE
MODRES 2J18 ASN A 93 ASN GLYCOSYLATION SITE
MODRES 2J18 ASN A 216 ASN GLYCOSYLATION SITE
MODRES 2J18 THR A 238 THR GLYCOSYLATION SITE
MODRES 2J18 SER A 239 SER GLYCOSYLATION SITE
MODRES 2J18 SER A 241 SER GLYCOSYLATION SITE
MODRES 2J18 SER A 242 SER GLYCOSYLATION SITE
MODRES 2J18 SER A 248 SER GLYCOSYLATION SITE
MODRES 2J18 THR A 250 THR GLYCOSYLATION SITE
MODRES 2J18 SER A 251 SER GLYCOSYLATION SITE
MODRES 2J18 THR A 252 THR GLYCOSYLATION SITE
MODRES 2J18 THR A 283 THR GLYCOSYLATION SITE
MODRES 2J18 THR A 293 THR GLYCOSYLATION SITE
MODRES 2J18 PCA A 0 GLU PYROGLUTAMIC ACID
HET PCA A 0 8
HET NAG B 1 14
HET NAG B 2 14
HET MAN B 3 11
HET NAG C 1 14
HET NAG C 2 14
HET MAN D 1 11
HET MAN D 2 11
HET MN A1299 1
HET HEM A1300 43
HET NAG A1301 14
HET MAN A1307 11
HET MAN A1308 11
HET MAN A1309 11
HET MAN A1310 11
HET MAN A1311 11
HET MAN A1312 11
HET MAN A1313 11
HET MAN A1314 11
HET MAN A1317 11
HET BR A1318 1
HET BR A1319 1
HET BR A1320 1
HETNAM PCA PYROGLUTAMIC ACID
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM MN MANGANESE (II) ION
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM BR BROMIDE ION
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN HEM HEME
FORMUL 1 PCA C5 H7 N O3
FORMUL 2 NAG 5(C8 H15 N O6)
FORMUL 2 MAN 12(C6 H12 O6)
FORMUL 5 MN MN 2+
FORMUL 6 HEM C34 H32 FE N4 O4
FORMUL 17 BR 3(BR 1-)
FORMUL 20 HOH *360(H2 O)
HELIX 1 1 GLU A 1 GLY A 5 5 5
HELIX 2 2 CYS A 29 HIS A 38 1 10
HELIX 3 3 SER A 49 GLY A 62 1 14
HELIX 4 4 ALA A 64 VAL A 67 5 4
HELIX 5 5 ILE A 68 GLY A 84 1 17
HELIX 6 6 THR A 95 GLU A 99 5 5
HELIX 7 7 ASP A 131 ASP A 140 1 10
HELIX 8 8 VAL A 141 ALA A 143 5 3
HELIX 9 9 ASP A 149 ASP A 168 1 20
HELIX 10 10 SER A 176 SER A 192 1 17
HELIX 11 11 ILE A 207 GLU A 217 1 11
HELIX 12 12 PRO A 220 GLY A 224 5 5
HELIX 13 13 GLU A 233 ALA A 247 1 15
SHEET 1 AA 2 ARG A 46 ILE A 48 0
SHEET 2 AA 2 LEU A 91 ASN A 93 -1 O LEU A 91 N ILE A 48
SHEET 1 AB 2 HIS A 147 PHE A 148 0
SHEET 2 AB 2 VAL A 205 ARG A 206 -1 O VAL A 205 N PHE A 148
SSBOND 1 CYS A 79 CYS A 87 1555 1555 2.06
LINK C PCA A 0 N AGLU A 1 1555 1555 1.33
LINK C PCA A 0 N BGLU A 1 1555 1555 1.33
LINK ND2 ASN A 12 C1 NAG A1301 1555 1555 1.44
LINK ND2 ASN A 93 C1 NAG B 1 1555 1555 1.44
LINK ND2 ASN A 216 C1 NAG C 1 1555 1555 1.45
LINK OG1 THR A 238 C1 MAN A1307 1555 1555 1.45
LINK OG SER A 239 C1 MAN A1308 1555 1555 1.44
LINK OG SER A 241 C1 MAN A1309 1555 1555 1.44
LINK OG SER A 242 C1 MAN A1310 1555 1555 1.45
LINK OG SER A 248 C1 MAN A1311 1555 1555 1.44
LINK OG1 THR A 250 C1 MAN A1312 1555 1555 1.45
LINK OG SER A 251 C1 MAN A1313 1555 1555 1.45
LINK OG1 THR A 252 C1 MAN A1314 1555 1555 1.45
LINK OG1 THR A 283 C1 MAN D 1 1555 1555 1.44
LINK OG1 THR A 293 C1 MAN A1317 1555 1555 1.45
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.44
LINK O4 NAG B 2 C1 MAN B 3 1555 1555 1.44
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44
LINK O2 MAN D 1 C1 MAN D 2 1555 1555 1.44
LINK SG CYS A 29 FE HEM A1300 1555 1555 2.33
LINK OE2 GLU A 104 MN MN A1299 1555 1555 1.98
LINK O HIS A 105 MN MN A1299 1555 1555 1.98
LINK OG SER A 108 MN MN A1299 1555 1555 2.00
LINK MN MN A1299 O1A HEM A1300 1555 1555 1.98
LINK MN MN A1299 O HOH A2333 1555 1555 2.34
LINK MN MN A1299 O HOH A2334 1555 1555 2.38
LINK FE HEM A1300 O BHOH A2336 1555 1555 2.64
CISPEP 1 TYR A 8 PRO A 9 0 1.14
CISPEP 2 SER A 229 PRO A 230 0 -2.33
CISPEP 3 ASP A 291 PRO A 292 0 3.52
CRYST1 57.730 150.460 100.750 90.00 90.00 90.00 C 2 2 21 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 0.017322 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006646 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009926 0.00000
HETATM 1 N PCA A 0 7.189 15.620 17.886 1.00 10.67 N
HETATM 2 CA PCA A 0 7.479 15.853 19.296 1.00 10.74 C
HETATM 3 CB PCA A 0 6.433 16.830 19.843 1.00 11.33 C
HETATM 4 CG PCA A 0 5.964 17.636 18.627 1.00 11.78 C
HETATM 5 CD PCA A 0 6.426 16.778 17.467 1.00 10.87 C
HETATM 6 OE PCA A 0 6.184 17.027 16.275 1.00 10.98 O
HETATM 7 C PCA A 0 7.467 14.515 20.040 1.00 10.84 C
HETATM 8 O PCA A 0 7.045 13.501 19.485 1.00 9.58 O
(ATOM LINES ARE NOT SHOWN.)
END
