HEADER OXIDOREDUCTASE 17-AUG-12 4B7D
TITLE PIKC BOUND TO THE 10-DML ANALOG WITH THE 3-(N,N-DIMETHYLAMINO)
TITLE 2 PROPANOATE ANCHORING GROUP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME P450 HYDROXYLASE PIKC;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CYTOCHROME P450 MONOOXYGENASE;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: THIOLATE LINK BETWEEN C 354 AND HEM 1407
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES VENEZUELAE;
SOURCE 3 ORGANISM_TAXID: 54571;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: HMS174(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET28B
KEYWDS OXIDOREDUCTASE, MONOOXYGENASE, PIKROMYCIN BIOSYNTHESIS
EXPDTA X-RAY DIFFRACTION
AUTHOR L.M.PODUST
REVDAT 4 20-DEC-23 4B7D 1 REMARK LINK
REVDAT 3 08-MAY-19 4B7D 1 REMARK
REVDAT 2 04-DEC-13 4B7D 1 HETNAM HETSYN
REVDAT 1 28-AUG-13 4B7D 0
JRNL AUTH L.M.PODUST
JRNL TITL RECOGNITION OF SYNTHETIC SUBSTRATES BY P450 PIKC
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.89 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 1.89
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 93.37
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.9
REMARK 3 NUMBER OF REFLECTIONS : 55068
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) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2967
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) : 1.89
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.94
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3791
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.20
REMARK 3 BIN R VALUE (WORKING SET) : 0.2920
REMARK 3 BIN FREE R VALUE SET COUNT : 177
REMARK 3 BIN FREE R VALUE : 0.3310
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6083
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 160
REMARK 3 SOLVENT ATOMS : 446
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.07
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.00000
REMARK 3 B22 (A**2) : -1.33000
REMARK 3 B33 (A**2) : -1.87000
REMARK 3 B12 (A**2) : -0.91000
REMARK 3 B13 (A**2) : -0.17000
REMARK 3 B23 (A**2) : 0.88000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.191
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.177
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.144
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.947
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.921
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6430 ; 0.023 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8803 ; 2.046 ; 2.031
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 792 ; 6.184 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 283 ;33.633 ;22.226
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 980 ;16.863 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 74 ;20.988 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 979 ; 0.137 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4984 ; 0.011 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 3968 ; 1.150 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6381 ; 1.907 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2462 ; 3.305 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2422 ; 4.823 ; 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 : 1.40
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 4B7D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-AUG-12.
REMARK 100 THE DEPOSITION ID IS D_1290053788.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JUL-12
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.11587
REMARK 200 MONOCHROMATOR : SI (111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59193
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.880
REMARK 200 RESOLUTION RANGE LOW (A) : 93.370
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.400
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.2
REMARK 200 DATA REDUNDANCY : 1.800
REMARK 200 R MERGE (I) : 0.04000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.88
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.98
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.8
REMARK 200 DATA REDUNDANCY IN SHELL : 1.30
REMARK 200 R MERGE FOR SHELL (I) : 0.83000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.400
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 2BVJ
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.05 M AMMONIUM SULFATE,
REMARK 280 0.1 M TRIS HCL, PH 6.5, 23 DEGREES C, TEMPERATURE 296K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
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: 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 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 -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 ARG A 2
REMARK 465 ARG A 3
REMARK 465 THR A 4
REMARK 465 GLN A 5
REMARK 465 GLN A 6
REMARK 465 GLY A 7
REMARK 465 THR A 8
REMARK 465 THR A 9
REMARK 465 ALA A 10
REMARK 465 SER A 11
REMARK 465 PRO A 12
REMARK 465 PRO A 13
REMARK 465 ARG A 407
REMARK 465 GLY A 408
REMARK 465 ARG A 409
REMARK 465 GLU A 410
REMARK 465 ALA A 411
REMARK 465 GLY A 412
REMARK 465 ARG A 413
REMARK 465 ARG A 414
REMARK 465 THR A 415
REMARK 465 GLY A 416
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 ARG B 2
REMARK 465 ARG B 3
REMARK 465 THR B 4
REMARK 465 GLN B 5
REMARK 465 GLN B 6
REMARK 465 GLY B 7
REMARK 465 THR B 8
REMARK 465 THR B 9
REMARK 465 ALA B 10
REMARK 465 SER B 11
REMARK 465 PRO B 12
REMARK 465 PRO B 13
REMARK 465 ARG B 407
REMARK 465 GLY B 408
REMARK 465 ARG B 409
REMARK 465 GLU B 410
REMARK 465 ALA B 411
REMARK 465 GLY B 412
REMARK 465 ARG B 413
REMARK 465 ARG B 414
REMARK 465 THR B 415
REMARK 465 GLY B 416
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 51 CG CD OE1 OE2
REMARK 470 GLU A 83 CG CD OE1 OE2
REMARK 470 ARG A 109 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 165 CD OE1 OE2
REMARK 470 GLU A 211 CG CD OE1 OE2
REMARK 470 GLU A 300 CG CD OE1 OE2
REMARK 470 ILE A 395 CD1
REMARK 470 ARG A 406 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 203 CG OD1 OD2
REMARK 470 ARG B 206 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 300 CG CD OE1 OE2
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 NH2 ARG A 219 O HOH A 2152 2.04
REMARK 500 O HOH A 2119 O HOH A 2129 2.17
REMARK 500 OG1 THR A 46 O HOH A 2039 2.18
REMARK 500 O HOH A 2058 O HOH A 2211 2.18
REMARK 500 C ARG B 406 O HOH B 2219 2.18
REMARK 500 NH1 ARG A 104 O2D HEM A 1407 2.18
REMARK 500 O HOH A 2207 O HOH A 2210 2.19
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 GLU A 287 CB GLU A 287 CG 0.122
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 ARG A 285 NE - CZ - NH1 ANGL. DEV. = 6.7 DEGREES
REMARK 500 ARG A 285 NE - CZ - NH2 ANGL. DEV. = -8.9 DEGREES
REMARK 500 LEU B 161 CB - CG - CD1 ANGL. DEV. = -10.3 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 ALA A 108 -64.70 -27.27
REMARK 500 ALA A 136 -6.59 -48.57
REMARK 500 LEU A 148 -47.08 -143.17
REMARK 500 HIS A 245 -73.25 -106.15
REMARK 500 ASP A 305 52.87 39.31
REMARK 500 ASN A 392 109.15 -42.62
REMARK 500 LEU B 148 -53.07 -138.89
REMARK 500 ASP B 212 -177.71 -66.08
REMARK 500 ASP B 224 79.29 -102.95
REMARK 500 LEU B 228 103.16 -162.09
REMARK 500 LEU B 228 103.16 -162.39
REMARK 500 HIS B 245 -95.99 -107.15
REMARK 500 GLU B 287 43.13 -141.77
REMARK 500 ASP B 305 50.84 38.46
REMARK 500 CYS B 354 113.74 -32.43
REMARK 500 PRO B 384 -61.81 -29.98
REMARK 500 PRO B 384 -61.81 -24.89
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 PROTOPORPHYRIN IX CONTAINING FE (HEM): THIOLATE BOND
REMARK 600 BETWEEN FE AND C 354
REMARK 600 GLYCEROL (GOL): CRYO-PROTECTANT
REMARK 600 (3R,4S,5S,7R,11R,12R,E)-12-ETHYL-3,5,7,11-TETRAMETHYL-2,
REMARK 600 8-DIOXOOXACYCLODODEC-9-EN-4-YL 3-(DIMETHYLAMINO)PROPANOATE
REMARK 600 (QLE): SYNTHETIC SUBSTRATE ANALOG
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 A1407 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 354 SG
REMARK 620 2 HEM A1407 NA 95.7
REMARK 620 3 HEM A1407 NB 86.6 89.9
REMARK 620 4 HEM A1407 NC 91.2 173.1 89.8
REMARK 620 5 HEM A1407 ND 99.2 90.2 174.1 89.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B1407 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 354 SG
REMARK 620 2 HEM B1407 NA 96.3
REMARK 620 3 HEM B1407 NB 90.5 88.6
REMARK 620 4 HEM B1407 NC 89.1 174.5 90.6
REMARK 620 5 HEM B1407 ND 96.2 90.8 173.3 89.4
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 1407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE QLE A 1408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 1407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE QLE B 1408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1409
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2BVJ RELATED DB: PDB
REMARK 900 LIGAND-FREE STRUCTURE OF CYTOCHROME P450 PIKC (CYP107L1)
REMARK 900 RELATED ID: 2C6H RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF YC-17-BOUND CYTOCHROME P450 PIKC (CYP107L1)
REMARK 900 RELATED ID: 2C7X RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF NARBOMYCIN-BOUND CYTOCHROME P450 PIKC
REMARK 900 (CYP107L1)
REMARK 900 RELATED ID: 2CA0 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF YC-17-BOUND CYTOCHROME P450 PIKC (CYP107L1)
REMARK 900 RELATED ID: 2CD8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF YC-17-BOUND CYTOCHROME P450 PIKC (CYP107L1)
REMARK 900 RELATED ID: 2VZ7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE YC-17-BOUND PIKC D50N MUTANT
REMARK 900 RELATED ID: 2VZM RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE NARBOMYCIN-BOUND PIKC D50N MUTANT
REMARK 900 RELATED ID: 2WHW RELATED DB: PDB
REMARK 900 SELECTIVE OXIDATION OF CARBOLIDE C-H BONDS BY ENGINEERED MACROLIDE
REMARK 900 P450 MONOOXYGENASE
REMARK 900 RELATED ID: 2WI9 RELATED DB: PDB
REMARK 900 SELECTIVE OXIDATION OF CARBOLIDE C-H BONDS BY ENGINEERED MACROLIDE
REMARK 900 P450 MONOOXYGENASE
REMARK 900 RELATED ID: 4B7S RELATED DB: PDB
REMARK 900 PIKC D50N MUTANT BOUND TO THE 10-DML ANALOG WITH THE 3-(N,N-
REMARK 900 DIMETHYLAMINO)PROPANOATE ANCHORING GROUP
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 FIRST 20 RESIDUES INCLUDING 6X HIS-TAG AND THROMBIN
REMARK 999 CLEAVAGE SITE ARE FROM THE CLONING VECTOR PET28A
DBREF 4B7D A 1 416 UNP O87605 O87605_9ACTO 1 416
DBREF 4B7D B 1 416 UNP O87605 O87605_9ACTO 1 416
SEQADV 4B7D MET A -19 UNP O87605 EXPRESSION TAG
SEQADV 4B7D GLY A -18 UNP O87605 EXPRESSION TAG
SEQADV 4B7D SER A -17 UNP O87605 EXPRESSION TAG
SEQADV 4B7D SER A -16 UNP O87605 EXPRESSION TAG
SEQADV 4B7D HIS A -15 UNP O87605 EXPRESSION TAG
SEQADV 4B7D HIS A -14 UNP O87605 EXPRESSION TAG
SEQADV 4B7D HIS A -13 UNP O87605 EXPRESSION TAG
SEQADV 4B7D HIS A -12 UNP O87605 EXPRESSION TAG
SEQADV 4B7D HIS A -11 UNP O87605 EXPRESSION TAG
SEQADV 4B7D HIS A -10 UNP O87605 EXPRESSION TAG
SEQADV 4B7D SER A -9 UNP O87605 EXPRESSION TAG
SEQADV 4B7D SER A -8 UNP O87605 EXPRESSION TAG
SEQADV 4B7D GLY A -7 UNP O87605 EXPRESSION TAG
SEQADV 4B7D LEU A -6 UNP O87605 EXPRESSION TAG
SEQADV 4B7D VAL A -5 UNP O87605 EXPRESSION TAG
SEQADV 4B7D PRO A -4 UNP O87605 EXPRESSION TAG
SEQADV 4B7D ARG A -3 UNP O87605 EXPRESSION TAG
SEQADV 4B7D GLY A -2 UNP O87605 EXPRESSION TAG
SEQADV 4B7D SER A -1 UNP O87605 EXPRESSION TAG
SEQADV 4B7D HIS A 0 UNP O87605 EXPRESSION TAG
SEQADV 4B7D MET B -19 UNP O87605 EXPRESSION TAG
SEQADV 4B7D GLY B -18 UNP O87605 EXPRESSION TAG
SEQADV 4B7D SER B -17 UNP O87605 EXPRESSION TAG
SEQADV 4B7D SER B -16 UNP O87605 EXPRESSION TAG
SEQADV 4B7D HIS B -15 UNP O87605 EXPRESSION TAG
SEQADV 4B7D HIS B -14 UNP O87605 EXPRESSION TAG
SEQADV 4B7D HIS B -13 UNP O87605 EXPRESSION TAG
SEQADV 4B7D HIS B -12 UNP O87605 EXPRESSION TAG
SEQADV 4B7D HIS B -11 UNP O87605 EXPRESSION TAG
SEQADV 4B7D HIS B -10 UNP O87605 EXPRESSION TAG
SEQADV 4B7D SER B -9 UNP O87605 EXPRESSION TAG
SEQADV 4B7D SER B -8 UNP O87605 EXPRESSION TAG
SEQADV 4B7D GLY B -7 UNP O87605 EXPRESSION TAG
SEQADV 4B7D LEU B -6 UNP O87605 EXPRESSION TAG
SEQADV 4B7D VAL B -5 UNP O87605 EXPRESSION TAG
SEQADV 4B7D PRO B -4 UNP O87605 EXPRESSION TAG
SEQADV 4B7D ARG B -3 UNP O87605 EXPRESSION TAG
SEQADV 4B7D GLY B -2 UNP O87605 EXPRESSION TAG
SEQADV 4B7D SER B -1 UNP O87605 EXPRESSION TAG
SEQADV 4B7D HIS B 0 UNP O87605 EXPRESSION TAG
SEQRES 1 A 436 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 436 LEU VAL PRO ARG GLY SER HIS MET ARG ARG THR GLN GLN
SEQRES 3 A 436 GLY THR THR ALA SER PRO PRO VAL LEU ASP LEU GLY ALA
SEQRES 4 A 436 LEU GLY GLN ASP PHE ALA ALA ASP PRO TYR PRO THR TYR
SEQRES 5 A 436 ALA ARG LEU ARG ALA GLU GLY PRO ALA HIS ARG VAL ARG
SEQRES 6 A 436 THR PRO GLU GLY ASP GLU VAL TRP LEU VAL VAL GLY TYR
SEQRES 7 A 436 ASP ARG ALA ARG ALA VAL LEU ALA ASP PRO ARG PHE SER
SEQRES 8 A 436 LYS ASP TRP ARG ASN SER THR THR PRO LEU THR GLU ALA
SEQRES 9 A 436 GLU ALA ALA LEU ASN HIS ASN MET LEU GLU SER ASP PRO
SEQRES 10 A 436 PRO ARG HIS THR ARG LEU ARG LYS LEU VAL ALA ARG GLU
SEQRES 11 A 436 PHE THR MET ARG ARG VAL GLU LEU LEU ARG PRO ARG VAL
SEQRES 12 A 436 GLN GLU ILE VAL ASP GLY LEU VAL ASP ALA MET LEU ALA
SEQRES 13 A 436 ALA PRO ASP GLY ARG ALA ASP LEU MET GLU SER LEU ALA
SEQRES 14 A 436 TRP PRO LEU PRO ILE THR VAL ILE SER GLU LEU LEU GLY
SEQRES 15 A 436 VAL PRO GLU PRO ASP ARG ALA ALA PHE ARG VAL TRP THR
SEQRES 16 A 436 ASP ALA PHE VAL PHE PRO ASP ASP PRO ALA GLN ALA GLN
SEQRES 17 A 436 THR ALA MET ALA GLU MET SER GLY TYR LEU SER ARG LEU
SEQRES 18 A 436 ILE ASP SER LYS ARG GLY GLN ASP GLY GLU ASP LEU LEU
SEQRES 19 A 436 SER ALA LEU VAL ARG THR SER ASP GLU ASP GLY SER ARG
SEQRES 20 A 436 LEU THR SER GLU GLU LEU LEU GLY MET ALA HIS ILE LEU
SEQRES 21 A 436 LEU VAL ALA GLY HIS GLU THR THR VAL ASN LEU ILE ALA
SEQRES 22 A 436 ASN GLY MET TYR ALA LEU LEU SER HIS PRO ASP GLN LEU
SEQRES 23 A 436 ALA ALA LEU ARG ALA ASP MET THR LEU LEU ASP GLY ALA
SEQRES 24 A 436 VAL GLU GLU MET LEU ARG TYR GLU GLY PRO VAL GLU SER
SEQRES 25 A 436 ALA THR TYR ARG PHE PRO VAL GLU PRO VAL ASP LEU ASP
SEQRES 26 A 436 GLY THR VAL ILE PRO ALA GLY ASP THR VAL LEU VAL VAL
SEQRES 27 A 436 LEU ALA ASP ALA HIS ARG THR PRO GLU ARG PHE PRO ASP
SEQRES 28 A 436 PRO HIS ARG PHE ASP ILE ARG ARG ASP THR ALA GLY HIS
SEQRES 29 A 436 LEU ALA PHE GLY HIS GLY ILE HIS PHE CYS ILE GLY ALA
SEQRES 30 A 436 PRO LEU ALA ARG LEU GLU ALA ARG ILE ALA VAL ARG ALA
SEQRES 31 A 436 LEU LEU GLU ARG CYS PRO ASP LEU ALA LEU ASP VAL SER
SEQRES 32 A 436 PRO GLY GLU LEU VAL TRP TYR PRO ASN PRO MET ILE ARG
SEQRES 33 A 436 GLY LEU LYS ALA LEU PRO ILE ARG TRP ARG ARG GLY ARG
SEQRES 34 A 436 GLU ALA GLY ARG ARG THR GLY
SEQRES 1 B 436 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 436 LEU VAL PRO ARG GLY SER HIS MET ARG ARG THR GLN GLN
SEQRES 3 B 436 GLY THR THR ALA SER PRO PRO VAL LEU ASP LEU GLY ALA
SEQRES 4 B 436 LEU GLY GLN ASP PHE ALA ALA ASP PRO TYR PRO THR TYR
SEQRES 5 B 436 ALA ARG LEU ARG ALA GLU GLY PRO ALA HIS ARG VAL ARG
SEQRES 6 B 436 THR PRO GLU GLY ASP GLU VAL TRP LEU VAL VAL GLY TYR
SEQRES 7 B 436 ASP ARG ALA ARG ALA VAL LEU ALA ASP PRO ARG PHE SER
SEQRES 8 B 436 LYS ASP TRP ARG ASN SER THR THR PRO LEU THR GLU ALA
SEQRES 9 B 436 GLU ALA ALA LEU ASN HIS ASN MET LEU GLU SER ASP PRO
SEQRES 10 B 436 PRO ARG HIS THR ARG LEU ARG LYS LEU VAL ALA ARG GLU
SEQRES 11 B 436 PHE THR MET ARG ARG VAL GLU LEU LEU ARG PRO ARG VAL
SEQRES 12 B 436 GLN GLU ILE VAL ASP GLY LEU VAL ASP ALA MET LEU ALA
SEQRES 13 B 436 ALA PRO ASP GLY ARG ALA ASP LEU MET GLU SER LEU ALA
SEQRES 14 B 436 TRP PRO LEU PRO ILE THR VAL ILE SER GLU LEU LEU GLY
SEQRES 15 B 436 VAL PRO GLU PRO ASP ARG ALA ALA PHE ARG VAL TRP THR
SEQRES 16 B 436 ASP ALA PHE VAL PHE PRO ASP ASP PRO ALA GLN ALA GLN
SEQRES 17 B 436 THR ALA MET ALA GLU MET SER GLY TYR LEU SER ARG LEU
SEQRES 18 B 436 ILE ASP SER LYS ARG GLY GLN ASP GLY GLU ASP LEU LEU
SEQRES 19 B 436 SER ALA LEU VAL ARG THR SER ASP GLU ASP GLY SER ARG
SEQRES 20 B 436 LEU THR SER GLU GLU LEU LEU GLY MET ALA HIS ILE LEU
SEQRES 21 B 436 LEU VAL ALA GLY HIS GLU THR THR VAL ASN LEU ILE ALA
SEQRES 22 B 436 ASN GLY MET TYR ALA LEU LEU SER HIS PRO ASP GLN LEU
SEQRES 23 B 436 ALA ALA LEU ARG ALA ASP MET THR LEU LEU ASP GLY ALA
SEQRES 24 B 436 VAL GLU GLU MET LEU ARG TYR GLU GLY PRO VAL GLU SER
SEQRES 25 B 436 ALA THR TYR ARG PHE PRO VAL GLU PRO VAL ASP LEU ASP
SEQRES 26 B 436 GLY THR VAL ILE PRO ALA GLY ASP THR VAL LEU VAL VAL
SEQRES 27 B 436 LEU ALA ASP ALA HIS ARG THR PRO GLU ARG PHE PRO ASP
SEQRES 28 B 436 PRO HIS ARG PHE ASP ILE ARG ARG ASP THR ALA GLY HIS
SEQRES 29 B 436 LEU ALA PHE GLY HIS GLY ILE HIS PHE CYS ILE GLY ALA
SEQRES 30 B 436 PRO LEU ALA ARG LEU GLU ALA ARG ILE ALA VAL ARG ALA
SEQRES 31 B 436 LEU LEU GLU ARG CYS PRO ASP LEU ALA LEU ASP VAL SER
SEQRES 32 B 436 PRO GLY GLU LEU VAL TRP TYR PRO ASN PRO MET ILE ARG
SEQRES 33 B 436 GLY LEU LYS ALA LEU PRO ILE ARG TRP ARG ARG GLY ARG
SEQRES 34 B 436 GLU ALA GLY ARG ARG THR GLY
HET GOL A1406 6
HET HEM A1407 43
HET QLE A1408 28
HET GOL B1406 6
HET HEM B1407 43
HET QLE B1408 28
HET GOL B1409 6
HETNAM GOL GLYCEROL
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM QLE [(3R,4S,5S,7R,9E,11R,12R)-12-ETHYL-3,5,7,11-
HETNAM 2 QLE TETRAMETHYL-2,8-BIS(OXIDANYLIDENE)-1-OXACYCLODODEC-9-
HETNAM 3 QLE EN-4-YL] 3-(DIMETHYLAMINO)PROPANOATE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN HEM HEME
FORMUL 3 GOL 3(C3 H8 O3)
FORMUL 4 HEM 2(C34 H32 FE N4 O4)
FORMUL 5 QLE 2(C22 H37 N O5)
FORMUL 10 HOH *446(H2 O)
HELIX 1 1 LEU A 17 ASP A 27 1 11
HELIX 2 2 PRO A 28 GLY A 39 1 12
HELIX 3 3 GLY A 57 ASP A 67 1 11
HELIX 4 4 ASP A 73 SER A 77 5 5
HELIX 5 5 THR A 82 ALA A 87 1 6
HELIX 6 6 ASN A 91 SER A 95 5 5
HELIX 7 7 PRO A 98 ALA A 108 1 11
HELIX 8 8 ARG A 109 PHE A 111 5 3
HELIX 9 9 THR A 112 LEU A 118 1 7
HELIX 10 10 LEU A 119 ALA A 136 1 18
HELIX 11 11 LEU A 144 LEU A 148 1 5
HELIX 12 12 TRP A 150 GLY A 162 1 13
HELIX 13 13 PRO A 164 PRO A 166 5 3
HELIX 14 14 ASP A 167 PHE A 180 1 14
HELIX 15 15 ASP A 183 ARG A 206 1 24
HELIX 16 16 ASP A 212 ASP A 224 1 13
HELIX 17 17 THR A 229 HIS A 245 1 17
HELIX 18 18 HIS A 245 SER A 261 1 17
HELIX 19 19 HIS A 262 ASP A 272 1 11
HELIX 20 20 LEU A 275 GLY A 288 1 14
HELIX 21 21 VAL A 318 HIS A 323 1 6
HELIX 22 22 GLY A 356 CYS A 375 1 20
HELIX 23 23 SER A 383 LEU A 387 5 5
HELIX 24 24 LEU B 17 ASP B 27 1 11
HELIX 25 25 PRO B 28 GLY B 39 1 12
HELIX 26 26 GLY B 57 ASP B 67 1 11
HELIX 27 27 ASP B 73 SER B 77 5 5
HELIX 28 28 THR B 82 ALA B 87 1 6
HELIX 29 29 ASN B 91 SER B 95 5 5
HELIX 30 30 PRO B 98 VAL B 107 1 10
HELIX 31 31 ALA B 108 PHE B 111 5 4
HELIX 32 32 THR B 112 LEU B 119 1 8
HELIX 33 33 LEU B 119 LEU B 135 1 17
HELIX 34 34 LEU B 144 LEU B 148 1 5
HELIX 35 35 TRP B 150 LEU B 161 1 12
HELIX 36 36 PRO B 164 ASP B 167 5 4
HELIX 37 37 ARG B 168 PHE B 180 1 13
HELIX 38 38 ASP B 183 ASP B 209 1 27
HELIX 39 39 ASP B 212 ASP B 224 1 13
HELIX 40 40 THR B 229 HIS B 245 1 17
HELIX 41 41 HIS B 245 HIS B 262 1 18
HELIX 42 42 HIS B 262 ASP B 272 1 11
HELIX 43 43 LEU B 275 GLY B 288 1 14
HELIX 44 44 VAL B 318 HIS B 323 1 6
HELIX 45 45 GLY B 356 CYS B 375 1 20
HELIX 46 46 SER B 383 LEU B 387 5 5
SHEET 1 AA 4 LEU A 15 ASP A 16 0
SHEET 2 AA 4 ALA A 41 ARG A 45 1 O ARG A 43 N LEU A 15
SHEET 3 AA 4 GLU A 51 VAL A 55 -1 O VAL A 52 N VAL A 44
SHEET 4 AA 4 VAL A 315 VAL A 317 1 O LEU A 316 N VAL A 55
SHEET 1 AB 2 PHE A 70 SER A 71 0
SHEET 2 AB 2 PHE A 297 PRO A 298 -1 O PHE A 297 N SER A 71
SHEET 1 AC 3 ARG A 141 ASP A 143 0
SHEET 2 AC 3 PRO A 402 ARG A 404 -1 O ILE A 403 N ALA A 142
SHEET 3 AC 3 ALA A 379 LEU A 380 -1 O ALA A 379 N ARG A 404
SHEET 1 AD 2 VAL A 302 LEU A 304 0
SHEET 2 AD 2 THR A 307 ILE A 309 -1 O THR A 307 N LEU A 304
SHEET 1 BA 4 LEU B 15 ASP B 16 0
SHEET 2 BA 4 ALA B 41 ARG B 45 1 O ARG B 43 N LEU B 15
SHEET 3 BA 4 GLU B 51 VAL B 55 -1 O VAL B 52 N VAL B 44
SHEET 4 BA 4 VAL B 315 VAL B 317 1 O LEU B 316 N VAL B 55
SHEET 1 BB 2 PHE B 70 SER B 71 0
SHEET 2 BB 2 PHE B 297 PRO B 298 -1 O PHE B 297 N SER B 71
SHEET 1 BC 3 ARG B 141 ASP B 143 0
SHEET 2 BC 3 PRO B 402 ARG B 404 -1 O ILE B 403 N ALA B 142
SHEET 3 BC 3 ALA B 379 LEU B 380 -1 O ALA B 379 N ARG B 404
SHEET 1 BD 2 VAL B 302 LEU B 304 0
SHEET 2 BD 2 THR B 307 ILE B 309 -1 O THR B 307 N LEU B 304
LINK SG CYS A 354 FE HEM A1407 1555 1555 2.31
LINK SG CYS B 354 FE HEM B1407 1555 1555 2.24
CISPEP 1 PRO A 97 PRO A 98 0 9.75
CISPEP 2 PRO B 97 PRO B 98 0 -1.40
SITE 1 AC1 6 TRP A 74 THR A 294 TYR A 295 QLE A1408
SITE 2 AC1 6 HOH A2075 HOH A2226
SITE 1 AC2 27 LYS A 72 MET A 92 LEU A 93 HIS A 100
SITE 2 AC2 27 ARG A 104 PHE A 111 LEU A 240 ALA A 243
SITE 3 AC2 27 GLY A 244 THR A 247 THR A 248 LEU A 251
SITE 4 AC2 27 PRO A 289 ALA A 293 THR A 294 ARG A 296
SITE 5 AC2 27 ALA A 346 PHE A 347 GLY A 348 ILE A 351
SITE 6 AC2 27 HIS A 352 CYS A 354 ILE A 355 GLY A 356
SITE 7 AC2 27 ALA A 360 QLE A1408 HOH A2212
SITE 1 AC3 10 GLU A 85 LEU A 93 GLU A 94 HIS A 238
SITE 2 AC3 10 ILE A 239 VAL A 242 ALA A 243 MET A 394
SITE 3 AC3 10 GOL A1406 HEM A1407
SITE 1 AC4 5 THR B 294 TYR B 295 MET B 394 QLE B1408
SITE 2 AC4 5 HOH B2068
SITE 1 AC5 26 LYS B 72 MET B 92 LEU B 93 HIS B 100
SITE 2 AC5 26 ARG B 104 ILE B 157 ILE B 239 LEU B 240
SITE 3 AC5 26 ALA B 243 GLY B 244 THR B 247 THR B 248
SITE 4 AC5 26 LEU B 251 PRO B 289 ALA B 293 THR B 294
SITE 5 AC5 26 ARG B 296 ALA B 346 PHE B 347 ILE B 351
SITE 6 AC5 26 HIS B 352 CYS B 354 ILE B 355 ALA B 360
SITE 7 AC5 26 QLE B1408 HOH B2204
SITE 1 AC6 12 TRP B 74 GLU B 85 LEU B 93 GLU B 94
SITE 2 AC6 12 HIS B 238 VAL B 242 ALA B 243 THR B 247
SITE 3 AC6 12 MET B 394 ILE B 395 GOL B1406 HEM B1407
SITE 1 AC7 10 ASP B 182 THR B 341 ALA B 342 GLY B 343
SITE 2 AC7 10 HIS B 344 PHE B 353 ARG B 361 HOH B2170
SITE 3 AC7 10 HOH B2202 HOH B2220
CRYST1 36.766 58.042 96.415 79.96 79.52 88.73 P 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 0.027199 -0.000603 -0.005002 0.00000
SCALE2 0.000000 0.017233 -0.003031 0.00000
SCALE3 0.000000 0.000000 0.010710 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
