HEADER OXIDOREDUCTASE 07-JUL-09 3I6N
TITLE MODE OF BINDING OF THE TUBERCULOSIS PRODRUG ISONIAZID TO PEROXIDASES:
TITLE 2 CRYSTAL STRUCTURE OF BOVINE LACTOPEROXIDASE WITH ISONIAZID AT 2.7
TITLE 3 RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LACTOPEROXIDASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 118-712;
COMPND 5 SYNONYM: LPO;
COMPND 6 EC: 1.11.1.7
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: BOVINE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 OTHER_DETAILS: BOVINE
KEYWDS ANTIMICROBIAL ACTIVITY, HEME, OXIDATION, PEROXIDASE, OXIDOREDUCTASE,
KEYWDS 2 ANTIBIOTIC, ANTIMICROBIAL, CLEAVAGE ON PAIR OF BASIC RESIDUES,
KEYWDS 3 DISULFIDE BOND, GLYCOPROTEIN, HYDROGEN PEROXIDE, IRON, METAL-
KEYWDS 4 BINDING, SECRETED
EXPDTA X-RAY DIFFRACTION
AUTHOR A.K.SINGH,R.P.KUMAR,N.PANDEY,N.SINGH,M.SINHA,A.BHUSHAN,P.KAUR,
AUTHOR 2 S.SHARMA,T.P.SINGH
REVDAT 6 01-NOV-23 3I6N 1 HETSYN
REVDAT 5 29-JUL-20 3I6N 1 COMPND REMARK HETNAM LINK
REVDAT 5 2 1 SITE ATOM
REVDAT 4 31-JAN-18 3I6N 1 REMARK
REVDAT 3 13-JUL-11 3I6N 1 VERSN
REVDAT 2 07-APR-10 3I6N 1 JRNL
REVDAT 1 13-OCT-09 3I6N 0
JRNL AUTH A.K.SINGH,R.P.KUMAR,N.PANDEY,N.SINGH,M.SINHA,A.BHUSHAN,
JRNL AUTH 2 P.KAUR,S.SHARMA,T.P.SINGH
JRNL TITL MODE OF BINDING OF THE TUBERCULOSIS PRODRUG ISONIAZID TO
JRNL TITL 2 HEME PEROXIDASES: BINDING STUDIES AND CRYSTAL STRUCTURE OF
JRNL TITL 3 BOVINE LACTOPEROXIDASE WITH ISONIAZID AT 2.7 A RESOLUTION.
JRNL REF J.BIOL.CHEM. V. 285 1569 2010
JRNL REFN ISSN 0021-9258
JRNL PMID 19907057
JRNL DOI 10.1074/JBC.M109.060327
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 75.81
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.6
REMARK 3 NUMBER OF REFLECTIONS : 17002
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 828
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 : 4774
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 198
REMARK 3 SOLVENT ATOMS : 287
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 45.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.63
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.53400
REMARK 3 B22 (A**2) : 3.84500
REMARK 3 B33 (A**2) : -5.37900
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.94900
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
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) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.800
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 15.10
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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: HYDROGENS ADDED IN RIDING POSITIONS
REMARK 4
REMARK 4 3I6N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-JUL-09.
REMARK 100 THE DEPOSITION ID IS D_1000054030.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-JAN-09
REMARK 200 TEMPERATURE (KELVIN) : 283
REMARK 200 PH : 6.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5414
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17002
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 75.810
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.13800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.2000
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) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.42000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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 3GC1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM IODIDE, PEG3350, PH6.2,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 40.27500
REMARK 290 SMTRY3 2 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: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, 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 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 OE2 GLU A 258 CMB HEM A 605 1.54
REMARK 500 OD2 ASP A 108 CMD HEM A 605 1.58
REMARK 500
REMARK 500 REMARK: NULL
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 MET A 352 CG MET A 352 SD -0.159
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 VAL A 10 CB - CA - C ANGL. DEV. = 14.6 DEGREES
REMARK 500 ASP A 108 CA - CB - CG ANGL. DEV. = 21.1 DEGREES
REMARK 500 ASN A 147 CA - CB - CG ANGL. DEV. = 13.3 DEGREES
REMARK 500 CYS A 167 CB - CA - C ANGL. DEV. = 7.5 DEGREES
REMARK 500 PRO A 170 C - N - CA ANGL. DEV. = 11.4 DEGREES
REMARK 500 GLN A 173 N - CA - CB ANGL. DEV. = 11.3 DEGREES
REMARK 500 CYS A 441 CA - CB - SG ANGL. DEV. = 8.1 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 TRP A 2 102.83 87.37
REMARK 500 GLU A 3 -70.12 -100.37
REMARK 500 VAL A 4 -22.15 61.25
REMARK 500 CYS A 6 122.57 -22.41
REMARK 500 PRO A 9 101.65 -55.03
REMARK 500 VAL A 10 -116.35 -75.84
REMARK 500 GLU A 17 -12.48 70.18
REMARK 500 ALA A 56 -11.61 -157.76
REMARK 500 PHE A 113 117.04 -166.05
REMARK 500 GLU A 118 -95.88 -95.52
REMARK 500 LEU A 119 18.58 49.60
REMARK 500 ASN A 122 42.25 95.47
REMARK 500 ASP A 137 -129.94 49.33
REMARK 500 CYS A 167 -124.15 59.06
REMARK 500 PRO A 168 -115.17 -46.57
REMARK 500 THR A 169 -48.88 166.19
REMARK 500 PRO A 170 -175.39 -32.23
REMARK 500 PRO A 171 -84.72 -36.59
REMARK 500 TYR A 172 173.51 78.50
REMARK 500 SER A 174 -131.46 75.26
REMARK 500 LEU A 175 -174.69 -66.72
REMARK 500 PRO A 209 41.30 -100.14
REMARK 500 ASN A 241 81.75 -159.46
REMARK 500 ILE A 260 -39.15 -36.06
REMARK 500 GLU A 371 54.34 -113.39
REMARK 500 ASP A 389 43.02 -143.33
REMARK 500 MET A 412 -72.12 -74.86
REMARK 500 PRO A 424 -9.65 -54.96
REMARK 500 ASN A 473 115.94 -162.60
REMARK 500 LYS A 485 -24.53 55.46
REMARK 500 ASP A 583 115.17 -38.21
REMARK 500 GLU A 594 -77.45 -50.52
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 TYR A 172 GLN A 173 -143.80
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 CA A 615 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 110 O
REMARK 620 2 ASP A 110 OD1 66.9
REMARK 620 3 THR A 184 O 75.9 128.3
REMARK 620 4 THR A 184 OG1 125.2 158.1 73.6
REMARK 620 5 PHE A 186 O 120.4 79.9 90.0 103.9
REMARK 620 6 ASP A 188 OD1 141.4 87.5 140.7 72.3 79.8
REMARK 620 7 SER A 190 OG 70.8 85.2 115.3 82.9 154.6 79.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 605 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 351 NE2
REMARK 620 2 HEM A 605 NA 89.4
REMARK 620 3 HEM A 605 NB 89.3 85.5
REMARK 620 4 HEM A 605 NC 79.5 167.9 89.6
REMARK 620 5 HEM A 605 ND 76.0 95.8 165.1 86.2
REMARK 620 6 HOH A 617 O 169.0 98.0 83.2 92.4 111.2
REMARK 620 N 1 2 3 4 5
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3GC1 RELATED DB: PDB
REMARK 900 NATIVE LACTOPEROXIDASE
DBREF 3I6N A 1 595 UNP P80025 PERL_BOVIN 118 712
SEQRES 1 A 595 SER TRP GLU VAL GLY CYS GLY ALA PRO VAL PRO LEU VAL
SEQRES 2 A 595 LYS CYS ASP GLU ASN SER PRO TYR ARG THR ILE THR GLY
SEQRES 3 A 595 ASP CYS ASN ASN ARG ARG SER PRO ALA LEU GLY ALA ALA
SEQRES 4 A 595 ASN ARG ALA LEU ALA ARG TRP LEU PRO ALA GLU TYR GLU
SEQRES 5 A 595 ASP GLY LEU ALA LEU PRO PHE GLY TRP THR GLN ARG LYS
SEQRES 6 A 595 THR ARG ASN GLY PHE ARG VAL PRO LEU ALA ARG GLU VAL
SEQRES 7 A 595 SER ASN LYS ILE VAL GLY TYR LEU ASP GLU GLU GLY VAL
SEQRES 8 A 595 LEU ASP GLN ASN ARG SER LEU LEU PHE MET GLN TRP GLY
SEQRES 9 A 595 GLN ILE VAL ASP HIS ASP LEU ASP PHE ALA PRO GLU THR
SEQRES 10 A 595 GLU LEU GLY SER ASN GLU HIS SER LYS THR GLN CYS GLU
SEQRES 11 A 595 GLU TYR CYS ILE GLN GLY ASP ASN CYS PHE PRO ILE MET
SEQRES 12 A 595 PHE PRO LYS ASN ASP PRO LYS LEU LYS THR GLN GLY LYS
SEQRES 13 A 595 CYS MET PRO PHE PHE ARG ALA GLY PHE VAL CYS PRO THR
SEQRES 14 A 595 PRO PRO TYR GLN SER LEU ALA ARG GLU GLN ILE ASN ALA
SEQRES 15 A 595 VAL THR SER PHE LEU ASP ALA SER LEU VAL TYR GLY SER
SEQRES 16 A 595 GLU PRO SEP LEU ALA SER ARG LEU ARG ASN LEU SER SER
SEQRES 17 A 595 PRO LEU GLY LEU MET ALA VAL ASN GLN GLU ALA TRP ASP
SEQRES 18 A 595 HIS GLY LEU ALA TYR LEU PRO PHE ASN ASN LYS LYS PRO
SEQRES 19 A 595 SER PRO CYS GLU PHE ILE ASN THR THR ALA ARG VAL PRO
SEQRES 20 A 595 CYS PHE LEU ALA GLY ASP PHE ARG ALA SER GLU GLN ILE
SEQRES 21 A 595 LEU LEU ALA THR ALA HIS THR LEU LEU LEU ARG GLU HIS
SEQRES 22 A 595 ASN ARG LEU ALA ARG GLU LEU LYS LYS LEU ASN PRO HIS
SEQRES 23 A 595 TRP ASN GLY GLU LYS LEU TYR GLN GLU ALA ARG LYS ILE
SEQRES 24 A 595 LEU GLY ALA PHE ILE GLN ILE ILE THR PHE ARG ASP TYR
SEQRES 25 A 595 LEU PRO ILE VAL LEU GLY SER GLU MET GLN LYS TRP ILE
SEQRES 26 A 595 PRO PRO TYR GLN GLY TYR ASN ASN SER VAL ASP PRO ARG
SEQRES 27 A 595 ILE SER ASN VAL PHE THR PHE ALA PHE ARG PHE GLY HIS
SEQRES 28 A 595 MET GLU VAL PRO SER THR VAL SER ARG LEU ASP GLU ASN
SEQRES 29 A 595 TYR GLN PRO TRP GLY PRO GLU ALA GLU LEU PRO LEU HIS
SEQRES 30 A 595 THR LEU PHE PHE ASN THR TRP ARG ILE ILE LYS ASP GLY
SEQRES 31 A 595 GLY ILE ASP PRO LEU VAL ARG GLY LEU LEU ALA LYS LYS
SEQRES 32 A 595 SER LYS LEU MET ASN GLN ASP LYS MET VAL THR SER GLU
SEQRES 33 A 595 LEU ARG ASN LYS LEU PHE GLN PRO THR HIS LYS ILE HIS
SEQRES 34 A 595 GLY PHE ASP LEU ALA ALA ILE ASN LEU GLN ARG CYS ARG
SEQRES 35 A 595 ASP HIS GLY MET PRO GLY TYR ASN SER TRP ARG GLY PHE
SEQRES 36 A 595 CYS GLY LEU SER GLN PRO LYS THR LEU LYS GLY LEU GLN
SEQRES 37 A 595 THR VAL LEU LYS ASN LYS ILE LEU ALA LYS LYS LEU MET
SEQRES 38 A 595 ASP LEU TYR LYS THR PRO ASP ASN ILE ASP ILE TRP ILE
SEQRES 39 A 595 GLY GLY ASN ALA GLU PRO MET VAL GLU ARG GLY ARG VAL
SEQRES 40 A 595 GLY PRO LEU LEU ALA CYS LEU LEU GLY ARG GLN PHE GLN
SEQRES 41 A 595 GLN ILE ARG ASP GLY ASP ARG PHE TRP TRP GLU ASN PRO
SEQRES 42 A 595 GLY VAL PHE THR GLU LYS GLN ARG ASP SER LEU GLN LYS
SEQRES 43 A 595 VAL SER PHE SER ARG LEU ILE CYS ASP ASN THR HIS ILE
SEQRES 44 A 595 THR LYS VAL PRO LEU HIS ALA PHE GLN ALA ASN ASN TYR
SEQRES 45 A 595 PRO HIS ASP PHE VAL ASP CYS SER THR VAL ASP LYS LEU
SEQRES 46 A 595 ASP LEU SER PRO TRP ALA SER ARG GLU ASN
MODRES 3I6N ASN A 95 ASN GLYCOSYLATION SITE
MODRES 3I6N ASN A 205 ASN GLYCOSYLATION SITE
MODRES 3I6N ASN A 241 ASN GLYCOSYLATION SITE
MODRES 3I6N ASN A 332 ASN GLYCOSYLATION SITE
MODRES 3I6N SEP A 198 SER PHOSPHOSERINE
HET SEP A 198 10
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 NAG D 1 14
HET NAG D 2 14
HET MAN D 3 11
HET NAG E 1 14
HET NAG E 2 14
HET HEM A 605 43
HET ISZ A 607 10
HET IOD A 608 1
HET IOD A 609 1
HET IOD A 610 1
HET IOD A 611 1
HET IOD A 612 1
HET IOD A 613 1
HET IOD A 614 1
HET CA A 615 1
HET SCN A 616 3
HETNAM SEP PHOSPHOSERINE
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM ISZ 4-(DIAZENYLCARBONYL)PYRIDINE
HETNAM IOD IODIDE ION
HETNAM CA CALCIUM ION
HETNAM SCN THIOCYANATE ION
HETSYN SEP PHOSPHONOSERINE
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
HETSYN ISZ ISONIAZID; TUBAZID; RIMITSID; ISONICOTINYLHYDRAZINE;
HETSYN 2 ISZ LANIZID; NYDRAZID
FORMUL 1 SEP C3 H8 N O6 P
FORMUL 2 NAG 8(C8 H15 N O6)
FORMUL 2 MAN 2(C6 H12 O6)
FORMUL 6 HEM C34 H32 FE N4 O4
FORMUL 7 ISZ C6 H5 N3 O
FORMUL 8 IOD 7(I 1-)
FORMUL 15 CA CA 2+
FORMUL 16 SCN C N S 1-
FORMUL 17 HOH *287(H2 O)
HELIX 1 1 LEU A 74 ILE A 82 1 9
HELIX 2 2 LEU A 98 ASP A 112 1 15
HELIX 3 3 ALA A 189 GLY A 194 1 6
HELIX 4 4 GLU A 196 LEU A 203 1 8
HELIX 5 5 SER A 235 ILE A 240 1 6
HELIX 6 6 GLN A 259 ASN A 284 1 26
HELIX 7 7 ASN A 288 ASP A 311 1 24
HELIX 8 8 LEU A 313 GLY A 318 1 6
HELIX 9 9 SER A 319 MET A 321 5 3
HELIX 10 10 VAL A 342 PHE A 347 1 6
HELIX 11 11 ARG A 348 VAL A 354 5 7
HELIX 12 12 HIS A 377 LEU A 379 5 3
HELIX 13 13 THR A 383 ASP A 389 1 7
HELIX 14 14 ILE A 392 LYS A 402 1 11
HELIX 15 15 THR A 414 ASN A 419 1 6
HELIX 16 16 ASP A 432 HIS A 444 1 13
HELIX 17 17 GLY A 448 CYS A 456 1 9
HELIX 18 18 THR A 463 LYS A 472 1 10
HELIX 19 19 ASN A 473 LYS A 485 1 13
HELIX 20 20 THR A 486 ILE A 490 5 5
HELIX 21 21 ASP A 491 GLU A 499 1 9
HELIX 22 22 GLY A 508 GLY A 525 1 18
HELIX 23 23 THR A 537 GLN A 545 1 9
HELIX 24 24 SER A 548 THR A 557 1 10
HELIX 25 25 SER A 580 VAL A 582 5 3
HELIX 26 26 LEU A 587 ALA A 591 5 5
SHEET 1 A 2 ARG A 41 ALA A 42 0
SHEET 2 A 2 ILE A 180 ASN A 181 -1 O ASN A 181 N ARG A 41
SHEET 1 B 2 LEU A 92 SER A 97 0
SHEET 2 B 2 LYS A 403 LYS A 405 -1 O SER A 404 N ARG A 96
SHEET 1 C 2 ILE A 142 MET A 143 0
SHEET 2 C 2 CYS A 157 MET A 158 -1 O MET A 158 N ILE A 142
SHEET 1 D 2 THR A 357 SER A 359 0
SHEET 2 D 2 GLU A 373 PRO A 375 -1 O LEU A 374 N VAL A 358
SHEET 1 E 2 LEU A 421 PHE A 422 0
SHEET 2 E 2 HIS A 429 PHE A 431 -1 O PHE A 431 N LEU A 421
SHEET 1 F 2 LYS A 561 PRO A 563 0
SHEET 2 F 2 PHE A 576 ASP A 578 -1 O VAL A 577 N VAL A 562
SSBOND 1 CYS A 6 CYS A 167 1555 1555 2.12
SSBOND 2 CYS A 15 CYS A 28 1555 1555 2.03
SSBOND 3 CYS A 129 CYS A 139 1555 1555 1.87
SSBOND 4 CYS A 133 CYS A 157 1555 1555 2.03
SSBOND 5 CYS A 237 CYS A 248 1555 1555 2.03
SSBOND 6 CYS A 456 CYS A 513 1555 1555 2.03
SSBOND 7 CYS A 554 CYS A 579 1555 1555 2.04
LINK ND2 ASN A 95 C1 NAG B 1 1555 1555 1.46
LINK C PRO A 197 N SEP A 198 1555 1555 1.33
LINK C SEP A 198 N LEU A 199 1555 1555 1.34
LINK ND2 ASN A 205 C1 NAG C 1 1555 1555 1.44
LINK ND2 ASN A 241 C1 NAG D 1 1555 1555 1.45
LINK ND2 ASN A 332 C1 NAG E 1 1555 1555 1.46
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.41
LINK O4 NAG B 2 C1 MAN B 3 1555 1555 1.41
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.39
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.44
LINK O4 NAG D 2 C1 MAN D 3 1555 1555 1.44
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.41
LINK O ASP A 110 CA CA A 615 1555 1555 2.48
LINK OD1 ASP A 110 CA CA A 615 1555 1555 2.61
LINK O THR A 184 CA CA A 615 1555 1555 2.64
LINK OG1 THR A 184 CA CA A 615 1555 1555 2.62
LINK O PHE A 186 CA CA A 615 1555 1555 2.43
LINK OD1 ASP A 188 CA CA A 615 1555 1555 2.62
LINK OG SER A 190 CA CA A 615 1555 1555 2.66
LINK NE2 HIS A 351 FE HEM A 605 1555 1555 2.48
LINK FE HEM A 605 O HOH A 617 1555 1555 2.55
CISPEP 1 VAL A 10 PRO A 11 0 -2.01
CISPEP 2 LYS A 233 PRO A 234 0 -0.08
CISPEP 3 TYR A 572 PRO A 573 0 6.58
CRYST1 54.490 80.550 77.780 90.00 102.66 90.00 P 1 21 1 2
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 0.018352 0.000000 0.004122 0.00000
SCALE2 0.000000 0.012415 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013177 0.00000
(ATOM LINES ARE NOT SHOWN.)
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