HEADER OXIDOREDUCTASE 28-SEP-07 2RFB
TITLE CRYSTAL STRUCTURE OF A CYTOCHROME P450 FROM THE THERMOACIDOPHILIC
TITLE 2 ARCHAEON PICROPHILUS TORRIDUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME P450;
COMPND 3 CHAIN: A, B, C;
COMPND 4 EC: 1.14.14.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PICROPHILUS TORRIDUS;
SOURCE 3 ORGANISM_TAXID: 82076;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PCWORI
KEYWDS CYTOCHROME P450 THERMOPHILE, HEME, IRON, METAL-BINDING,
KEYWDS 2 MONOOXYGENASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.W.HO,H.LI,T.L.POULOS,C.R.NISHIDA,P.R.ORTIZ DE MONTELLANO
REVDAT 5 21-FEB-24 2RFB 1 REMARK
REVDAT 4 13-JUL-11 2RFB 1 VERSN
REVDAT 3 24-FEB-09 2RFB 1 VERSN
REVDAT 2 26-FEB-08 2RFB 1 JRNL
REVDAT 1 29-JAN-08 2RFB 0
JRNL AUTH W.W.HO,H.LI,C.R.NISHIDA,P.R.ORTIZ DE MONTELLANO,T.L.POULOS
JRNL TITL CRYSTAL STRUCTURE AND PROPERTIES OF CYP231A2 FROM THE
JRNL TITL 2 THERMOACIDOPHILIC ARCHAEON PICROPHILUS TORRIDUS.
JRNL REF BIOCHEMISTRY V. 47 2071 2008
JRNL REFN ISSN 0006-2960
JRNL PMID 18197710
JRNL DOI 10.1021/BI702240K
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.51
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 45855
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) : 0.214
REMARK 3 R VALUE (WORKING SET) : 0.211
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2414
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.56
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3327
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.24
REMARK 3 BIN R VALUE (WORKING SET) : 0.3020
REMARK 3 BIN FREE R VALUE SET COUNT : 152
REMARK 3 BIN FREE R VALUE : 0.3710
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8181
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 149
REMARK 3 SOLVENT ATOMS : 135
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 69.81
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.18000
REMARK 3 B22 (A**2) : 2.21000
REMARK 3 B33 (A**2) : -1.49000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.13000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.453
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.294
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.228
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.720
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.947
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.917
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8510 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11516 ; 1.619 ; 2.016
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1000 ; 6.558 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 408 ;36.575 ;24.412
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1557 ;19.580 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 49 ;19.976 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1231 ; 0.109 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6400 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3957 ; 0.236 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5759 ; 0.316 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 345 ; 0.182 ; 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): 63 ; 0.224 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 9 ; 0.264 ; 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): 5147 ; 0.727 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8128 ; 1.234 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3809 ; 1.733 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3382 ; 2.574 ; 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 : 3
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 12 A 352
REMARK 3 ORIGIN FOR THE GROUP (A): -14.0786 33.2443 -42.8779
REMARK 3 T TENSOR
REMARK 3 T11: -0.4119 T22: -0.3348
REMARK 3 T33: -0.2694 T12: 0.0657
REMARK 3 T13: 0.0331 T23: 0.0242
REMARK 3 L TENSOR
REMARK 3 L11: 3.8558 L22: 1.5456
REMARK 3 L33: 2.7647 L12: 0.4318
REMARK 3 L13: -0.2203 L23: -0.0974
REMARK 3 S TENSOR
REMARK 3 S11: 0.0106 S12: -0.5086 S13: -0.1521
REMARK 3 S21: 0.1418 S22: -0.0488 S23: 0.0010
REMARK 3 S31: -0.0548 S32: 0.0309 S33: 0.0382
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 10 B 352
REMARK 3 ORIGIN FOR THE GROUP (A): -16.5130 54.8050 -83.8507
REMARK 3 T TENSOR
REMARK 3 T11: -0.0968 T22: -0.0220
REMARK 3 T33: -0.1361 T12: 0.0754
REMARK 3 T13: -0.0043 T23: -0.1001
REMARK 3 L TENSOR
REMARK 3 L11: 2.8836 L22: 2.4499
REMARK 3 L33: 7.5056 L12: -0.5370
REMARK 3 L13: 1.9868 L23: 0.5422
REMARK 3 S TENSOR
REMARK 3 S11: -0.1718 S12: -0.0945 S13: -0.0449
REMARK 3 S21: -0.2589 S22: -0.2141 S23: 0.2967
REMARK 3 S31: -0.3178 S32: -1.0376 S33: 0.3859
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 12 C 352
REMARK 3 ORIGIN FOR THE GROUP (A): 1.4523 81.3368 -40.9890
REMARK 3 T TENSOR
REMARK 3 T11: 0.3087 T22: -0.1587
REMARK 3 T33: 0.1292 T12: 0.1949
REMARK 3 T13: -0.3147 T23: -0.2454
REMARK 3 L TENSOR
REMARK 3 L11: 3.1681 L22: 3.9920
REMARK 3 L33: 2.3887 L12: 0.0407
REMARK 3 L13: -0.0734 L23: 0.9181
REMARK 3 S TENSOR
REMARK 3 S11: 0.0558 S12: 0.0775 S13: -0.0828
REMARK 3 S21: 0.3072 S22: 0.3010 S23: -0.1578
REMARK 3 S31: 0.3879 S32: 0.3977 S33: -0.3569
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 2RFB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-NOV-07.
REMARK 100 THE DEPOSITION ID IS D_1000044788.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-DEC-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL1-5
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.7400, 1.6475
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48305
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 48.510
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.05100
REMARK 200 R SYM (I) : 0.05100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 31.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.66100
REMARK 200 R SYM FOR SHELL (I) : 0.66100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M AMMONIUM SULFATE, 0.1M HEPES, 2%
REMARK 280 POLYETHYLENE GLYCOL 400, PH 7.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 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 84.23000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 350
REMARK 350 BIOMOLECULE: 3
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: C
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 10
REMARK 465 ARG A 11
REMARK 465 ASN A 50
REMARK 465 ALA A 51
REMARK 465 GLY A 52
REMARK 465 PRO B 44
REMARK 465 GLY B 45
REMARK 465 ASN B 46
REMARK 465 ARG B 47
REMARK 465 TYR B 48
REMARK 465 SER B 49
REMARK 465 ASN B 50
REMARK 465 ALA B 51
REMARK 465 MET C 10
REMARK 465 ARG C 11
REMARK 465 PRO C 44
REMARK 465 GLY C 45
REMARK 465 ASN C 46
REMARK 465 ARG C 47
REMARK 465 TYR C 48
REMARK 465 SER C 49
REMARK 465 ASN C 50
REMARK 465 ALA C 51
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 ARG B 11 CG CD NE CZ NH1 NH2
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 O2 SO4 C 910 O HOH C 931 1.44
REMARK 500 S SO4 C 910 O HOH C 931 1.53
REMARK 500 O4 SO4 C 910 O HOH C 931 1.78
REMARK 500 O3 SO4 C 910 O HOH C 931 2.03
REMARK 500 O LEU B 177 N ASN B 179 2.17
REMARK 500 OD2 ASP A 331 NZ LYS A 334 2.18
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 ASP B 221 CG ASP B 221 OD1 0.300
REMARK 500 ASP B 221 CG ASP B 221 OD2 0.203
REMARK 500 ASP B 222 CG ASP B 222 OD1 0.174
REMARK 500 LYS B 225 CD LYS B 225 CE 0.283
REMARK 500 LYS B 287 CD LYS B 287 CE 0.498
REMARK 500 LYS B 287 CE LYS B 287 NZ 0.281
REMARK 500 ARG B 290 NE ARG B 290 CZ 0.091
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 236 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 ASP B 221 CB - CG - OD1 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ASP B 222 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 LYS B 287 CG - CD - CE ANGL. DEV. = -18.5 DEGREES
REMARK 500 LYS B 287 CD - CE - NZ ANGL. DEV. = -14.6 DEGREES
REMARK 500 PRO C 62 C - N - CA ANGL. DEV. = -12.0 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 ASN A 36 64.45 -108.61
REMARK 500 PRO A 44 -158.06 -55.06
REMARK 500 ASN A 46 -100.24 -163.22
REMARK 500 TYR A 48 -20.03 -153.61
REMARK 500 SER A 55 -141.76 55.58
REMARK 500 ASN A 97 53.48 -151.62
REMARK 500 ASP A 99 136.40 -39.17
REMARK 500 ASN A 100 -5.19 77.60
REMARK 500 TYR A 107 -56.98 -131.58
REMARK 500 ASN A 145 -8.61 -52.35
REMARK 500 SER A 163 -148.79 -77.26
REMARK 500 SER A 165 -157.31 -142.18
REMARK 500 LYS A 178 91.25 53.68
REMARK 500 ARG A 180 129.92 175.31
REMARK 500 ASN A 199 -73.57 -78.65
REMARK 500 ASN A 226 77.72 -151.27
REMARK 500 ASN A 256 48.44 35.17
REMARK 500 CYS A 304 114.97 -36.76
REMARK 500 ARG B 11 1.85 -160.56
REMARK 500 LEU B 12 128.73 44.58
REMARK 500 ASN B 36 62.70 -108.49
REMARK 500 SER B 55 -129.21 63.52
REMARK 500 THR B 58 42.33 -109.04
REMARK 500 ASN B 61 -65.74 -19.96
REMARK 500 GLU B 66 -38.22 -176.88
REMARK 500 LEU B 94 -7.64 -58.62
REMARK 500 ASN B 97 78.73 -119.60
REMARK 500 ILE B 98 -49.95 -135.42
REMARK 500 ASP B 99 137.26 -37.77
REMARK 500 ASN B 100 -45.38 74.35
REMARK 500 ILE B 104 -70.72 -59.49
REMARK 500 TYR B 107 -54.64 -144.27
REMARK 500 SER B 176 -143.23 -159.07
REMARK 500 LEU B 177 -168.32 161.14
REMARK 500 LYS B 178 0.76 26.61
REMARK 500 ASN B 179 61.97 97.83
REMARK 500 ARG B 180 118.50 178.92
REMARK 500 THR B 183 156.92 -49.94
REMARK 500 ASN B 199 -70.37 -70.16
REMARK 500 ASP B 218 69.42 -114.97
REMARK 500 ASP B 221 -70.02 -48.10
REMARK 500 HIS B 246 63.65 -110.87
REMARK 500 ASN B 256 73.02 18.99
REMARK 500 ASN B 257 -5.07 84.68
REMARK 500 GLU B 282 75.80 42.15
REMARK 500 ASP B 284 41.23 -101.22
REMARK 500 CYS B 304 117.19 -35.82
REMARK 500 ARG B 327 128.17 177.37
REMARK 500 ASN B 340 117.54 -31.68
REMARK 500 LEU B 351 -80.98 -98.53
REMARK 500
REMARK 500 THIS ENTRY HAS 72 RAMACHANDRAN OUTLIERS.
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 A 410 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 304 SG
REMARK 620 2 HEM A 410 NA 102.2
REMARK 620 3 HEM A 410 NB 90.1 82.0
REMARK 620 4 HEM A 410 NC 87.4 168.9 92.5
REMARK 620 5 HEM A 410 ND 102.5 92.7 167.1 90.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 410 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 304 SG
REMARK 620 2 HEM B 410 NA 104.9
REMARK 620 3 HEM B 410 NB 90.9 88.4
REMARK 620 4 HEM B 410 NC 83.7 170.5 87.5
REMARK 620 5 HEM B 410 ND 98.8 92.0 169.8 90.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM C 410 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 304 SG
REMARK 620 2 HEM C 410 NA 99.5
REMARK 620 3 HEM C 410 NB 88.4 84.7
REMARK 620 4 HEM C 410 NC 88.7 170.7 91.3
REMARK 620 5 HEM C 410 ND 98.2 92.7 173.2 90.3
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 SO4 A 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 910
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 920
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 910
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 410
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2RFC RELATED DB: PDB
DBREF 2RFB A 10 352 UNP Q6KZ68 Q6KZ68_PICTO 1 343
DBREF 2RFB B 10 352 UNP Q6KZ68 Q6KZ68_PICTO 1 343
DBREF 2RFB C 10 352 UNP Q6KZ68 Q6KZ68_PICTO 1 343
SEQRES 1 A 343 MET ARG LEU ASN ASP PRO VAL HIS TYR ASP GLY ALA TRP
SEQRES 2 A 343 HIS VAL TYR LYS TYR SER ASP VAL LYS HIS VAL LEU MET
SEQRES 3 A 343 ASN ASP LYS ILE PHE SER SER ASN PRO GLY ASN ARG TYR
SEQRES 4 A 343 SER ASN ALA GLY GLY ILE SER PHE ILE THR MET ASP ASN
SEQRES 5 A 343 PRO GLU HIS LYS GLU PHE ARG ASP ILE SER ALA PRO TYR
SEQRES 6 A 343 PHE LEU PRO SER LYS ILE ASN ASP TYR LYS ASP PHE ILE
SEQRES 7 A 343 GLU GLU THR SER ASN ASP LEU ILE LYS ASN ILE ASP ASN
SEQRES 8 A 343 LYS ASP ILE ILE SER GLU TYR ALA VAL ARG LEU PRO VAL
SEQRES 9 A 343 ASN ILE ILE SER LYS ILE LEU GLY ILE PRO ASP SER ASP
SEQRES 10 A 343 MET PRO LEU PHE LYS LEU TRP SER ASP TYR ILE ILE GLY
SEQRES 11 A 343 ASN LYS ARG ASP GLU ASN PHE ASN TYR VAL ASN ASN ARG
SEQRES 12 A 343 MET VAL SER ARG LEU LEU GLU ILE PHE LYS SER ASP SER
SEQRES 13 A 343 HIS GLY ILE ILE ASN VAL LEU ALA GLY SER SER LEU LYS
SEQRES 14 A 343 ASN ARG LYS LEU THR MET ASP GLU LYS ILE LYS TYR ILE
SEQRES 15 A 343 MET LEU LEU ILE ILE GLY GLY ASN GLU THR THR THR ASN
SEQRES 16 A 343 LEU ILE GLY ASN MET ILE ARG VAL ILE ASP GLU ASN PRO
SEQRES 17 A 343 ASP ILE ILE ASP ASP ALA LEU LYS ASN ARG SER GLY PHE
SEQRES 18 A 343 VAL GLU GLU THR LEU ARG TYR TYR SER PRO ILE GLN PHE
SEQRES 19 A 343 LEU PRO HIS ARG PHE ALA ALA GLU ASP SER TYR ILE ASN
SEQRES 20 A 343 ASN LYS LYS ILE LYS LYS GLY ASP GLN VAL ILE VAL TYR
SEQRES 21 A 343 LEU GLY SER ALA ASN ARG ASP GLU THR PHE PHE ASP GLU
SEQRES 22 A 343 PRO ASP LEU PHE LYS ILE GLY ARG ARG GLU MET HIS LEU
SEQRES 23 A 343 ALA PHE GLY ILE GLY ILE HIS MET CYS LEU GLY ALA PRO
SEQRES 24 A 343 LEU ALA ARG LEU GLU ALA SER ILE ALA LEU ASN ASP ILE
SEQRES 25 A 343 LEU ASN HIS PHE LYS ARG ILE LYS ILE ASP TYR LYS LYS
SEQRES 26 A 343 SER ARG LEU LEU ASP ASN LYS MET VAL LEU GLY TYR ASP
SEQRES 27 A 343 LYS LEU PHE LEU SER
SEQRES 1 B 343 MET ARG LEU ASN ASP PRO VAL HIS TYR ASP GLY ALA TRP
SEQRES 2 B 343 HIS VAL TYR LYS TYR SER ASP VAL LYS HIS VAL LEU MET
SEQRES 3 B 343 ASN ASP LYS ILE PHE SER SER ASN PRO GLY ASN ARG TYR
SEQRES 4 B 343 SER ASN ALA GLY GLY ILE SER PHE ILE THR MET ASP ASN
SEQRES 5 B 343 PRO GLU HIS LYS GLU PHE ARG ASP ILE SER ALA PRO TYR
SEQRES 6 B 343 PHE LEU PRO SER LYS ILE ASN ASP TYR LYS ASP PHE ILE
SEQRES 7 B 343 GLU GLU THR SER ASN ASP LEU ILE LYS ASN ILE ASP ASN
SEQRES 8 B 343 LYS ASP ILE ILE SER GLU TYR ALA VAL ARG LEU PRO VAL
SEQRES 9 B 343 ASN ILE ILE SER LYS ILE LEU GLY ILE PRO ASP SER ASP
SEQRES 10 B 343 MET PRO LEU PHE LYS LEU TRP SER ASP TYR ILE ILE GLY
SEQRES 11 B 343 ASN LYS ARG ASP GLU ASN PHE ASN TYR VAL ASN ASN ARG
SEQRES 12 B 343 MET VAL SER ARG LEU LEU GLU ILE PHE LYS SER ASP SER
SEQRES 13 B 343 HIS GLY ILE ILE ASN VAL LEU ALA GLY SER SER LEU LYS
SEQRES 14 B 343 ASN ARG LYS LEU THR MET ASP GLU LYS ILE LYS TYR ILE
SEQRES 15 B 343 MET LEU LEU ILE ILE GLY GLY ASN GLU THR THR THR ASN
SEQRES 16 B 343 LEU ILE GLY ASN MET ILE ARG VAL ILE ASP GLU ASN PRO
SEQRES 17 B 343 ASP ILE ILE ASP ASP ALA LEU LYS ASN ARG SER GLY PHE
SEQRES 18 B 343 VAL GLU GLU THR LEU ARG TYR TYR SER PRO ILE GLN PHE
SEQRES 19 B 343 LEU PRO HIS ARG PHE ALA ALA GLU ASP SER TYR ILE ASN
SEQRES 20 B 343 ASN LYS LYS ILE LYS LYS GLY ASP GLN VAL ILE VAL TYR
SEQRES 21 B 343 LEU GLY SER ALA ASN ARG ASP GLU THR PHE PHE ASP GLU
SEQRES 22 B 343 PRO ASP LEU PHE LYS ILE GLY ARG ARG GLU MET HIS LEU
SEQRES 23 B 343 ALA PHE GLY ILE GLY ILE HIS MET CYS LEU GLY ALA PRO
SEQRES 24 B 343 LEU ALA ARG LEU GLU ALA SER ILE ALA LEU ASN ASP ILE
SEQRES 25 B 343 LEU ASN HIS PHE LYS ARG ILE LYS ILE ASP TYR LYS LYS
SEQRES 26 B 343 SER ARG LEU LEU ASP ASN LYS MET VAL LEU GLY TYR ASP
SEQRES 27 B 343 LYS LEU PHE LEU SER
SEQRES 1 C 343 MET ARG LEU ASN ASP PRO VAL HIS TYR ASP GLY ALA TRP
SEQRES 2 C 343 HIS VAL TYR LYS TYR SER ASP VAL LYS HIS VAL LEU MET
SEQRES 3 C 343 ASN ASP LYS ILE PHE SER SER ASN PRO GLY ASN ARG TYR
SEQRES 4 C 343 SER ASN ALA GLY GLY ILE SER PHE ILE THR MET ASP ASN
SEQRES 5 C 343 PRO GLU HIS LYS GLU PHE ARG ASP ILE SER ALA PRO TYR
SEQRES 6 C 343 PHE LEU PRO SER LYS ILE ASN ASP TYR LYS ASP PHE ILE
SEQRES 7 C 343 GLU GLU THR SER ASN ASP LEU ILE LYS ASN ILE ASP ASN
SEQRES 8 C 343 LYS ASP ILE ILE SER GLU TYR ALA VAL ARG LEU PRO VAL
SEQRES 9 C 343 ASN ILE ILE SER LYS ILE LEU GLY ILE PRO ASP SER ASP
SEQRES 10 C 343 MET PRO LEU PHE LYS LEU TRP SER ASP TYR ILE ILE GLY
SEQRES 11 C 343 ASN LYS ARG ASP GLU ASN PHE ASN TYR VAL ASN ASN ARG
SEQRES 12 C 343 MET VAL SER ARG LEU LEU GLU ILE PHE LYS SER ASP SER
SEQRES 13 C 343 HIS GLY ILE ILE ASN VAL LEU ALA GLY SER SER LEU LYS
SEQRES 14 C 343 ASN ARG LYS LEU THR MET ASP GLU LYS ILE LYS TYR ILE
SEQRES 15 C 343 MET LEU LEU ILE ILE GLY GLY ASN GLU THR THR THR ASN
SEQRES 16 C 343 LEU ILE GLY ASN MET ILE ARG VAL ILE ASP GLU ASN PRO
SEQRES 17 C 343 ASP ILE ILE ASP ASP ALA LEU LYS ASN ARG SER GLY PHE
SEQRES 18 C 343 VAL GLU GLU THR LEU ARG TYR TYR SER PRO ILE GLN PHE
SEQRES 19 C 343 LEU PRO HIS ARG PHE ALA ALA GLU ASP SER TYR ILE ASN
SEQRES 20 C 343 ASN LYS LYS ILE LYS LYS GLY ASP GLN VAL ILE VAL TYR
SEQRES 21 C 343 LEU GLY SER ALA ASN ARG ASP GLU THR PHE PHE ASP GLU
SEQRES 22 C 343 PRO ASP LEU PHE LYS ILE GLY ARG ARG GLU MET HIS LEU
SEQRES 23 C 343 ALA PHE GLY ILE GLY ILE HIS MET CYS LEU GLY ALA PRO
SEQRES 24 C 343 LEU ALA ARG LEU GLU ALA SER ILE ALA LEU ASN ASP ILE
SEQRES 25 C 343 LEU ASN HIS PHE LYS ARG ILE LYS ILE ASP TYR LYS LYS
SEQRES 26 C 343 SER ARG LEU LEU ASP ASN LYS MET VAL LEU GLY TYR ASP
SEQRES 27 C 343 LYS LEU PHE LEU SER
HET SO4 A 900 5
HET SO4 A 910 5
HET SO4 A 920 5
HET HEM A 410 43
HET HEM B 410 43
HET SO4 C 910 5
HET HEM C 410 43
HETNAM SO4 SULFATE ION
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN HEM HEME
FORMUL 4 SO4 4(O4 S 2-)
FORMUL 7 HEM 3(C34 H32 FE N4 O4)
FORMUL 11 HOH *135(H2 O)
HELIX 1 1 LYS A 26 ASN A 36 1 11
HELIX 2 2 ILE A 54 MET A 59 5 6
HELIX 3 3 ASP A 60 LEU A 76 1 17
HELIX 4 4 LEU A 76 ASN A 81 1 6
HELIX 5 5 TYR A 83 LYS A 96 1 14
HELIX 6 6 ASP A 102 TYR A 107 1 6
HELIX 7 7 VAL A 109 GLY A 121 1 13
HELIX 8 8 PRO A 123 SER A 125 5 3
HELIX 9 9 ASP A 126 ILE A 138 1 13
HELIX 10 10 GLU A 144 SER A 163 1 20
HELIX 11 11 GLY A 167 GLY A 174 1 8
HELIX 12 12 THR A 183 ASN A 216 1 34
HELIX 13 13 ILE A 219 ASN A 226 1 8
HELIX 14 14 ASN A 226 TYR A 238 1 13
HELIX 15 15 TYR A 269 ASN A 274 1 6
HELIX 16 16 GLY A 306 PHE A 325 1 20
HELIX 17 17 LYS B 26 ASN B 36 1 11
HELIX 18 18 ILE B 54 MET B 59 5 6
HELIX 19 19 ASP B 60 LEU B 76 1 17
HELIX 20 20 LEU B 76 LEU B 94 1 19
HELIX 21 21 ASP B 102 TYR B 107 1 6
HELIX 22 22 VAL B 109 GLY B 121 1 13
HELIX 23 23 PRO B 123 SER B 125 5 3
HELIX 24 24 ASP B 126 ILE B 138 1 13
HELIX 25 25 ASN B 145 SER B 163 1 19
HELIX 26 26 GLY B 167 GLY B 174 1 8
HELIX 27 27 THR B 183 ASN B 216 1 34
HELIX 28 28 ILE B 219 ASN B 226 1 8
HELIX 29 29 ASN B 226 TYR B 238 1 13
HELIX 30 30 LEU B 270 ASN B 274 1 5
HELIX 31 31 GLY B 306 PHE B 325 1 20
HELIX 32 32 LYS C 26 ASN C 36 1 11
HELIX 33 33 ILE C 54 MET C 59 5 6
HELIX 34 34 HIS C 64 ALA C 72 1 9
HELIX 35 35 PRO C 73 PHE C 75 5 3
HELIX 36 36 LEU C 76 ASP C 82 1 7
HELIX 37 37 TYR C 83 LYS C 96 1 14
HELIX 38 38 ASP C 102 TYR C 107 1 6
HELIX 39 39 VAL C 109 GLY C 121 1 13
HELIX 40 40 PRO C 123 SER C 125 5 3
HELIX 41 41 ASP C 126 ILE C 138 1 13
HELIX 42 42 ASN C 145 SER C 163 1 19
HELIX 43 43 HIS C 166 GLY C 174 1 9
HELIX 44 44 THR C 183 ASN C 216 1 34
HELIX 45 45 ILE C 219 ASN C 226 1 8
HELIX 46 46 ASN C 226 TYR C 238 1 13
HELIX 47 47 LEU C 270 ASN C 274 1 5
HELIX 48 48 GLY C 306 PHE C 325 1 20
SHEET 1 A 3 VAL A 16 TYR A 18 0
SHEET 2 A 3 ALA A 21 VAL A 24 -1 O HIS A 23 N VAL A 16
SHEET 3 A 3 GLN A 265 VAL A 268 1 O ILE A 267 N TRP A 22
SHEET 1 B 2 PHE A 40 SER A 41 0
SHEET 2 B 2 PHE A 248 ALA A 249 -1 O PHE A 248 N SER A 41
SHEET 1 C 2 SER A 253 ILE A 255 0
SHEET 2 C 2 LYS A 258 ILE A 260 -1 O ILE A 260 N SER A 253
SHEET 1 D 2 ARG A 336 LEU A 337 0
SHEET 2 D 2 TYR A 346 LYS A 348 -1 O ASP A 347 N ARG A 336
SHEET 1 E 5 VAL B 16 TYR B 18 0
SHEET 2 E 5 ALA B 21 VAL B 24 -1 O ALA B 21 N TYR B 18
SHEET 3 E 5 GLN B 265 TYR B 269 1 O ILE B 267 N VAL B 24
SHEET 4 E 5 PHE B 243 ALA B 249 -1 N ARG B 247 O VAL B 266
SHEET 5 E 5 PHE B 40 SER B 41 -1 N SER B 41 O PHE B 248
SHEET 1 F 2 SER B 253 ILE B 255 0
SHEET 2 F 2 LYS B 258 ILE B 260 -1 O LYS B 258 N ILE B 255
SHEET 1 G 2 ARG B 336 LEU B 337 0
SHEET 2 G 2 TYR B 346 LYS B 348 -1 O ASP B 347 N ARG B 336
SHEET 1 H 5 VAL C 16 HIS C 17 0
SHEET 2 H 5 TRP C 22 VAL C 24 -1 O HIS C 23 N VAL C 16
SHEET 3 H 5 GLN C 265 TYR C 269 1 O ILE C 267 N TRP C 22
SHEET 4 H 5 PHE C 243 ALA C 249 -1 N LEU C 244 O VAL C 268
SHEET 5 H 5 PHE C 40 SER C 41 -1 N SER C 41 O PHE C 248
SHEET 1 I 2 SER C 253 ILE C 255 0
SHEET 2 I 2 LYS C 258 ILE C 260 -1 O ILE C 260 N SER C 253
SHEET 1 J 2 ARG C 336 LEU C 337 0
SHEET 2 J 2 TYR C 346 LYS C 348 -1 O ASP C 347 N ARG C 336
LINK SG CYS A 304 FE HEM A 410 1555 1555 2.33
LINK SG CYS B 304 FE HEM B 410 1555 1555 2.11
LINK SG CYS C 304 FE HEM C 410 1555 1555 2.34
SITE 1 AC1 3 ASP A 99 PHE A 325 LYS A 326
SITE 1 AC2 3 PHE A 280 ASP A 281 ARG A 290
SITE 1 AC3 3 ILE A 54 SER A 55 LYS A 189
SITE 1 AC4 5 PHE C 280 ASP C 281 ARG C 290 ARG C 291
SITE 2 AC4 5 HOH C 931
SITE 1 AC5 20 PHE A 56 ILE A 57 HIS A 64 ARG A 68
SITE 2 AC5 20 LEU A 194 GLY A 197 GLY A 198 THR A 201
SITE 3 AC5 20 ILE A 241 ARG A 247 LEU A 270 ALA A 296
SITE 4 AC5 20 PHE A 297 GLY A 298 ILE A 301 HIS A 302
SITE 5 AC5 20 CYS A 304 GLY A 306 HOH A 944 HOH A 946
SITE 1 AC6 25 PHE B 56 ILE B 57 HIS B 64 ARG B 68
SITE 2 AC6 25 PHE B 75 LEU B 193 LEU B 194 GLY B 197
SITE 3 AC6 25 GLY B 198 THR B 201 HIS B 246 ARG B 247
SITE 4 AC6 25 LEU B 270 ALA B 296 PHE B 297 GLY B 298
SITE 5 AC6 25 ILE B 301 HIS B 302 CYS B 304 GLY B 306
SITE 6 AC6 25 LEU B 309 ALA B 310 HOH B 412 HOH B 419
SITE 7 AC6 25 HOH B 420
SITE 1 AC7 19 PHE C 56 ILE C 57 HIS C 64 ARG C 68
SITE 2 AC7 19 LEU C 194 GLY C 197 GLY C 198 THR C 201
SITE 3 AC7 19 LEU C 205 LEU C 235 LEU C 244 ARG C 247
SITE 4 AC7 19 ALA C 296 PHE C 297 GLY C 298 ILE C 301
SITE 5 AC7 19 HIS C 302 CYS C 304 GLY C 306
CRYST1 48.790 168.460 88.230 90.00 96.25 90.00 P 1 21 1 6
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.020496 0.000000 0.002245 0.00000
SCALE2 0.000000 0.005936 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011402 0.00000
(ATOM LINES ARE NOT SHOWN.)
END