HEADER OXIDOREDUCTASE 13-JAN-14 4OEK
TITLE CRYSTAL STRUCTURE OF THE COMPLEX OF GOAT LACTOPEROXIDASE WITH
TITLE 2 PHENYLETHYLAMINE AT 2.47 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LACTOPEROXIDASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 118-712;
COMPND 5 EC: 1.11.1.7
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CAPRA HIRCUS;
SOURCE 3 ORGANISM_COMMON: DOMESTIC GOAT,GOATS;
SOURCE 4 ORGANISM_TAXID: 9925
KEYWDS PEROXIDASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.KUMAR,R.P.SINGH,M.SINHA,A.BHUSHAN,P.KAUR,S.SHARMA,T.P.SINGH
REVDAT 3 20-SEP-23 4OEK 1 HETSYN
REVDAT 2 29-JUL-20 4OEK 1 COMPND REMARK HETNAM LINK
REVDAT 2 2 1 SITE ATOM
REVDAT 1 22-JAN-14 4OEK 0
JRNL AUTH M.KUMAR,R.P.SINGH,M.SINHA,A.BHUSHAN,P.KAUR,S.SHARMA,
JRNL AUTH 2 T.P.SINGH
JRNL TITL CRYSTAL STRUCTURE OF THE COMPLEX OF GOAT LACTOPEROXIDASE
JRNL TITL 2 WITH PHENYLETHYLAMINE AT 2.47 A
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.47 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 2.47
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 73.69
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.0
REMARK 3 NUMBER OF REFLECTIONS : 18577
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) : 0.208
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.281
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 995
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) : 2.47
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1100
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 72.70
REMARK 3 BIN R VALUE (WORKING SET) : 0.2610
REMARK 3 BIN FREE R VALUE SET COUNT : 69
REMARK 3 BIN FREE R VALUE : 0.3250
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4757
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 159
REMARK 3 SOLVENT ATOMS : 250
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.16
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.03000
REMARK 3 B22 (A**2) : -1.92000
REMARK 3 B33 (A**2) : 2.05000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.22000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.389
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.228
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 21.721
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.940
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.883
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5048 ; 0.012 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 3510 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6861 ; 1.841 ; 1.985
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8452 ; 3.072 ; 3.003
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 594 ; 6.323 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 240 ;37.677 ;23.750
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 804 ;16.103 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 38 ;18.634 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 727 ; 0.078 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5564 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1064 ; 0.007 ; 0.020
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 1 A 595
REMARK 3 ORIGIN FOR THE GROUP (A): 7.7372 -0.5141 21.9791
REMARK 3 T TENSOR
REMARK 3 T11: 0.0220 T22: 0.0316
REMARK 3 T33: 0.0258 T12: -0.0068
REMARK 3 T13: 0.0092 T23: 0.0073
REMARK 3 L TENSOR
REMARK 3 L11: 0.3919 L22: 0.7155
REMARK 3 L33: 0.1785 L12: 0.1675
REMARK 3 L13: 0.1289 L23: -0.1645
REMARK 3 S TENSOR
REMARK 3 S11: -0.0083 S12: 0.0194 S13: 0.0241
REMARK 3 S21: -0.0586 S22: 0.0311 S23: 0.0788
REMARK 3 S31: 0.0149 S32: 0.0016 S33: -0.0228
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
REMARK 4
REMARK 4 4OEK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JAN-14.
REMARK 100 THE DEPOSITION ID IS D_1000084393.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-NOV-13
REMARK 200 TEMPERATURE (KELVIN) : 77
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM14
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18577
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.470
REMARK 200 RESOLUTION RANGE LOW (A) : 74.210
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.47
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.29900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.900
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 3SXV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM NITRATE, PEG , PH 6.8 , VAPOR
REMARK 280 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 39.94550
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
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 606 1.73
REMARK 500 OD2 ASP A 108 CMD HEM A 606 1.76
REMARK 500 O6 NAG B 2 O HOH A 761 1.99
REMARK 500 NA HEM A 606 O HOH A 950 2.12
REMARK 500 ND2 ASN A 95 O5 NAG A 601 2.16
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 ILE A 240 C ASN A 241 N 0.193
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 -116.34 -85.35
REMARK 500 VAL A 4 -55.19 -29.98
REMARK 500 ALA A 8 55.68 157.56
REMARK 500 PRO A 9 -158.51 -99.92
REMARK 500 GLU A 17 -28.60 92.64
REMARK 500 LEU A 55 -56.64 -137.24
REMARK 500 ALA A 56 -30.69 -146.92
REMARK 500 ILE A 82 -58.35 -125.13
REMARK 500 LEU A 119 15.10 36.70
REMARK 500 ASP A 137 -104.37 55.74
REMARK 500 ASN A 147 1.59 91.30
REMARK 500 CYS A 167 -95.89 87.42
REMARK 500 PRO A 170 -179.36 -65.68
REMARK 500 SER A 174 -83.93 -120.30
REMARK 500 ASP A 188 28.08 -142.60
REMARK 500 PRO A 209 32.73 -80.32
REMARK 500 ASP A 221 77.81 -115.23
REMARK 500 SER A 319 -1.68 -55.47
REMARK 500 GLU A 371 40.24 -106.99
REMARK 500 ASP A 389 45.39 -163.43
REMARK 500 THR A 425 -35.63 75.24
REMARK 500 ASN A 473 107.99 -168.95
REMARK 500 PRO A 589 0.48 -58.55
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 607 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 110 OD1
REMARK 620 2 ASP A 110 O 70.2
REMARK 620 3 THR A 184 O 136.3 78.4
REMARK 620 4 THR A 184 OG1 151.6 132.0 71.6
REMARK 620 5 PHE A 186 O 77.6 121.4 94.5 97.9
REMARK 620 6 ASP A 188 OD1 77.7 140.3 140.9 74.4 71.6
REMARK 620 7 SER A 190 OG 86.0 81.4 119.0 81.5 143.7 73.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 606 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 351 NE2
REMARK 620 2 HEM A 606 NA 111.6
REMARK 620 3 HEM A 606 NB 110.2 85.3
REMARK 620 4 HEM A 606 NC 103.4 144.3 89.0
REMARK 620 5 HEM A 606 ND 89.1 85.2 160.5 88.9
REMARK 620 6 HOH A 950 O 158.5 66.8 91.3 78.2 69.4
REMARK 620 N 1 2 3 4 5
DBREF 4OEK A 1 595 UNP A3F9D6 A3F9D6_CAPHI 118 712
SEQRES 1 A 595 SER TRP GLU VAL GLY CYS GLY ALA PRO VAL PRO LEU VAL
SEQRES 2 A 595 THR CYS ASP GLU GLN 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 VAL 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 SER GLU HIS SER LYS VAL GLN CYS GLU
SEQRES 11 A 595 GLU TYR CYS VAL GLN GLY ASP GLU 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 ASP 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 PRO PRO PHE ASN ASN VAL LYS PRO
SEQRES 19 A 595 SER PRO CYS GLU PHE ILE ASN THR THR ALA HIS VAL PRO
SEQRES 20 A 595 CYS PHE GLN ALA GLY ASP SER ARG ALA SER GLU GLN ILE
SEQRES 21 A 595 LEU LEU ALA THR VAL HIS THR LEU LEU LEU ARG GLU HIS
SEQRES 22 A 595 ASN ARG LEU ALA ARG GLU LEU LYS ARG LEU ASN PRO HIS
SEQRES 23 A 595 TRP ASP GLY GLU MET 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 ASN
SEQRES 32 A 595 SER LYS LEU MET ASN GLN ASN LYS MET VAL THR SER GLU
SEQRES 33 A 595 LEU ARG ASN LYS LEU PHE GLN PRO THR HIS LYS VAL 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 ALA VAL LEU LYS ASN LYS VAL LEU ALA LYS LYS LEU LEU
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 ALA VAL ASP LYS LEU
SEQRES 46 A 595 ASP LEU SER PRO TRP ALA SER ARG GLU ASN
MODRES 4OEK ASN A 241 ASN GLYCOSYLATION SITE
MODRES 4OEK ASN A 332 ASN GLYCOSYLATION SITE
MODRES 4OEK ASN A 95 ASN GLYCOSYLATION SITE
MODRES 4OEK ASN A 205 ASN GLYCOSYLATION SITE
MODRES 4OEK SEP A 198 SER PHOSPHOSERINE
HET SEP A 198 10
HET NAG B 1 14
HET NAG B 2 14
HET NAG A 601 14
HET NAG A 602 14
HET NAG A 605 14
HET HEM A 606 43
HET CA A 607 1
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 IOD A 615 1
HET IOD A 616 1
HET IOD A 617 1
HET IOD A 618 1
HET IOD A 619 1
HET IOD A 620 1
HET SCN A 621 3
HET EDO A 622 4
HET EDO A 623 4
HET EDO A 624 4
HET EDO A 625 4
HET EDO A 626 4
HET PEA A 627 9
HETNAM SEP PHOSPHOSERINE
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM CA CALCIUM ION
HETNAM IOD IODIDE ION
HETNAM SCN THIOCYANATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PEA 2-PHENYLETHYLAMINE
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 HEM HEME
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 SEP C3 H8 N O6 P
FORMUL 2 NAG 5(C8 H15 N O6)
FORMUL 6 HEM C34 H32 FE N4 O4
FORMUL 7 CA CA 2+
FORMUL 8 IOD 13(I 1-)
FORMUL 21 SCN C N S 1-
FORMUL 22 EDO 5(C2 H6 O2)
FORMUL 27 PEA C8 H12 N 1+
FORMUL 28 HOH *250(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 GLU A 123 GLU A 131 1 9
HELIX 4 4 LYS A 150 GLY A 155 1 6
HELIX 5 5 ALA A 189 GLY A 194 1 6
HELIX 6 6 GLU A 196 ARG A 204 1 9
HELIX 7 7 SER A 235 ILE A 240 1 6
HELIX 8 8 ARG A 255 GLU A 258 5 4
HELIX 9 9 GLN A 259 ASN A 284 1 26
HELIX 10 10 ASP A 288 ASP A 311 1 24
HELIX 11 11 TYR A 312 GLY A 318 1 7
HELIX 12 12 GLU A 320 ILE A 325 1 6
HELIX 13 13 SER A 340 PHE A 347 1 8
HELIX 14 14 ARG A 348 VAL A 354 5 7
HELIX 15 15 HIS A 377 PHE A 380 5 4
HELIX 16 16 THR A 383 LYS A 388 1 6
HELIX 17 17 GLY A 391 LYS A 402 1 12
HELIX 18 18 THR A 414 ASN A 419 1 6
HELIX 19 19 ASP A 432 HIS A 444 1 13
HELIX 20 20 GLY A 448 CYS A 456 1 9
HELIX 21 21 THR A 463 LYS A 472 1 10
HELIX 22 22 ASN A 473 TYR A 484 1 12
HELIX 23 23 THR A 486 ILE A 490 5 5
HELIX 24 24 ASP A 491 GLU A 499 1 9
HELIX 25 25 GLY A 508 GLY A 525 1 18
HELIX 26 26 THR A 537 GLN A 545 1 9
HELIX 27 27 SER A 548 THR A 557 1 10
HELIX 28 28 SER A 580 VAL A 582 5 3
HELIX 29 29 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 ASN A 403 LYS A 405 -1 O SER A 404 N ASP A 93
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 2.02
SSBOND 2 CYS A 15 CYS A 28 1555 1555 2.05
SSBOND 3 CYS A 129 CYS A 139 1555 1555 2.03
SSBOND 4 CYS A 133 CYS A 157 1555 1555 2.04
SSBOND 5 CYS A 237 CYS A 248 1555 1555 2.02
SSBOND 6 CYS A 456 CYS A 513 1555 1555 2.04
SSBOND 7 CYS A 554 CYS A 579 1555 1555 2.03
LINK ND2 ASN A 95 C1 NAG A 601 1555 1555 1.45
LINK C PRO A 197 N SEP A 198 1555 1555 1.33
LINK C SEP A 198 N LEU A 199 1555 1555 1.31
LINK ND2 ASN A 205 C1 NAG A 602 1555 1555 1.45
LINK ND2 ASN A 241 C1 NAG B 1 1555 1555 1.44
LINK ND2 ASN A 332 C1 NAG A 605 1555 1555 1.44
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.45
LINK OD1 ASP A 110 CA CA A 607 1555 1555 2.10
LINK O ASP A 110 CA CA A 607 1555 1555 2.19
LINK O THR A 184 CA CA A 607 1555 1555 2.44
LINK OG1 THR A 184 CA CA A 607 1555 1555 2.54
LINK O PHE A 186 CA CA A 607 1555 1555 2.36
LINK OD1 ASP A 188 CA CA A 607 1555 1555 2.61
LINK OG SER A 190 CA CA A 607 1555 1555 2.52
LINK NE2 HIS A 351 FE HEM A 606 1555 1555 2.13
LINK FE HEM A 606 O HOH A 950 1555 1555 1.84
CISPEP 1 LYS A 233 PRO A 234 0 10.67
CISPEP 2 TYR A 572 PRO A 573 0 1.67
CRYST1 53.166 79.891 75.284 90.00 101.80 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 0.018809 0.000000 0.003929 0.00000
SCALE2 0.000000 0.012517 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013570 0.00000
(ATOM LINES ARE NOT SHOWN.)
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