HEADER OXIDOREDUCTASE 24-DEC-16 5UDA
TITLE CRYSTAL STRUCTURE OF CYP2B6 (Y226H/K262R) IN COMPLEX WITH A
TITLE 2 MONOTERPENE BORNANE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME P450 2B6;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: 1,4-CINEOLE 2-EXO-MONOOXYGENASE,CYPIIB6,CYTOCHROME P450
COMPND 5 IIB1;
COMPND 6 EC: 1.14.13.-;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CYP2B6;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: JM109
KEYWDS OXIDOREDUCTASE, CYTOCHROME P450, CYP2B6
EXPDTA X-RAY DIFFRACTION
AUTHOR M.B.SHAH,J.R.HALPERT
REVDAT 5 04-OCT-23 5UDA 1 REMARK
REVDAT 4 18-DEC-19 5UDA 1 REMARK
REVDAT 3 27-SEP-17 5UDA 1 REMARK
REVDAT 2 31-MAY-17 5UDA 1 JRNL REMARK
REVDAT 1 12-APR-17 5UDA 0
JRNL AUTH M.B.SHAH,J.LIU,Q.ZHANG,C.D.STOUT,J.R.HALPERT
JRNL TITL HALOGEN-PI INTERACTIONS IN THE CYTOCHROME P450 ACTIVE SITE:
JRNL TITL 2 STRUCTURAL INSIGHTS INTO HUMAN CYP2B6 SUBSTRATE SELECTIVITY.
JRNL REF ACS CHEM. BIOL. V. 12 1204 2017
JRNL REFN ESSN 1554-8937
JRNL PMID 28368100
JRNL DOI 10.1021/ACSCHEMBIO.7B00056
REMARK 2
REMARK 2 RESOLUTION. 1.93 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0072
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) : 1.93
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.43
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 3 NUMBER OF REFLECTIONS : 94042
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.175
REMARK 3 R VALUE (WORKING SET) : 0.173
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 4852
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) : 1.93
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.98
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7072
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.81
REMARK 3 BIN R VALUE (WORKING SET) : 0.2180
REMARK 3 BIN FREE R VALUE SET COUNT : 371
REMARK 3 BIN FREE R VALUE : 0.2840
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7416
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 222
REMARK 3 SOLVENT ATOMS : 481
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.46
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.64000
REMARK 3 B22 (A**2) : 0.64000
REMARK 3 B33 (A**2) : -0.96000
REMARK 3 B12 (A**2) : 0.32000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.126
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.123
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.082
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.804
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7891 ; 0.030 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10687 ; 2.199 ; 2.017
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 920 ; 6.071 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 366 ;35.032 ;22.869
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1313 ;14.659 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 59 ;20.160 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1147 ; 0.170 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5960 ; 0.012 ; 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): 4617 ; 1.424 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7482 ; 2.455 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3274 ; 3.719 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3205 ; 5.703 ; 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 5UDA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JAN-17.
REMARK 100 THE DEPOSITION ID IS D_1000225680.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-APR-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97946
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 98894
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.930
REMARK 200 RESOLUTION RANGE LOW (A) : 40.430
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.93
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.22900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4I91
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM CHLORIDE 0.1 M HEPES 25%
REMARK 280 W/V POLYETHYLENE GLYCOL 3350, PH 7.4, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 134.76667
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 67.38333
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 20
REMARK 465 ALA A 21
REMARK 465 LYS A 22
REMARK 465 LYS A 23
REMARK 465 THR A 24
REMARK 465 SER A 25
REMARK 465 SER A 26
REMARK 465 LYS A 27
REMARK 465 MET A 137
REMARK 465 GLY A 138
REMARK 465 LYS A 139
REMARK 465 HIS A 492
REMARK 465 HIS A 493
REMARK 465 HIS A 494
REMARK 465 HIS A 495
REMARK 465 MET B 20
REMARK 465 ALA B 21
REMARK 465 LYS B 22
REMARK 465 LYS B 23
REMARK 465 THR B 24
REMARK 465 SER B 25
REMARK 465 SER B 26
REMARK 465 LYS B 27
REMARK 465 PHE B 135
REMARK 465 GLY B 136
REMARK 465 MET B 137
REMARK 465 GLY B 138
REMARK 465 HIS B 492
REMARK 465 HIS B 493
REMARK 465 HIS B 494
REMARK 465 HIS B 495
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 LYS A 29 CE NZ
REMARK 470 ARG A 35 NE CZ NH1 NH2
REMARK 470 ARG A 48 CD NE CZ NH1 NH2
REMARK 470 ARG A 140 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 161 CE NZ
REMARK 470 LYS A 197 NZ
REMARK 470 GLU A 250 CG CD OE1 OE2
REMARK 470 ARG A 253 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 48 CZ NH1 NH2
REMARK 470 LYS B 139 CG CD CE NZ
REMARK 470 ARG B 140 CZ NH1 NH2
REMARK 470 LYS B 161 NZ
REMARK 470 LYS B 197 NZ
REMARK 470 LYS B 251 CE NZ
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 326 O HOH A 601 1.88
REMARK 500 OH TYR A 235 O HOH A 602 2.02
REMARK 500 ND1 HIS B 319 O HOH B 601 2.17
REMARK 500 NH2 ARG A 73 O GLU A 218 2.18
REMARK 500 ND1 HIS A 319 O HOH A 603 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 PHE A 296 CB PHE A 296 CG -0.147
REMARK 500 PHE B 296 CB PHE B 296 CG -0.145
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 B 158 CG - CD - NE ANGL. DEV. = -13.4 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 LYS A 29 -153.95 -124.34
REMARK 500 PRO A 31 153.18 -49.28
REMARK 500 LEU A 39 -48.98 71.79
REMARK 500 VAL A 89 -61.96 -96.73
REMARK 500 ASP A 263 -176.59 -174.88
REMARK 500 TYR A 317 69.49 -117.60
REMARK 500 SER A 430 -163.60 68.99
REMARK 500 LYS B 29 -141.26 -119.92
REMARK 500 LEU B 39 -51.63 73.18
REMARK 500 VAL B 89 -60.14 -98.32
REMARK 500 ASP B 263 -175.39 -171.57
REMARK 500 TYR B 317 70.82 -118.70
REMARK 500 LYS B 384 131.85 -38.86
REMARK 500 SER B 430 -164.30 69.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 CM5 A 503
REMARK 610 CM5 A 505
REMARK 610 CM5 B 503
REMARK 610 CM5 B 505
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 501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 436 SG
REMARK 620 2 HEM A 501 NA 104.0
REMARK 620 3 HEM A 501 NB 92.5 91.1
REMARK 620 4 HEM A 501 NC 89.0 167.0 88.7
REMARK 620 5 HEM A 501 ND 103.1 88.4 164.1 88.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 436 SG
REMARK 620 2 HEM B 501 NA 104.0
REMARK 620 3 HEM B 501 NB 92.0 89.9
REMARK 620 4 HEM B 501 NC 89.1 167.0 89.6
REMARK 620 5 HEM B 501 ND 103.8 87.4 164.1 89.6
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 HEM A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CAE A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CM5 A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CM5 A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CM5 A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CAE B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CM5 B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CM5 B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CM5 B 505
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5UEC RELATED DB: PDB
DBREF 5UDA A 21 491 UNP P20813 CP2B6_HUMAN 21 491
DBREF 5UDA B 21 491 UNP P20813 CP2B6_HUMAN 21 491
SEQADV 5UDA MET A 20 UNP P20813 INITIATING METHIONINE
SEQADV 5UDA ALA A 21 UNP P20813 GLN 21 ENGINEERED MUTATION
SEQADV 5UDA LYS A 22 UNP P20813 ARG 22 ENGINEERED MUTATION
SEQADV 5UDA LYS A 23 UNP P20813 HIS 23 ENGINEERED MUTATION
SEQADV 5UDA THR A 24 UNP P20813 PRO 24 ENGINEERED MUTATION
SEQADV 5UDA SER A 25 UNP P20813 ASN 25 ENGINEERED MUTATION
SEQADV 5UDA SER A 26 UNP P20813 THR 26 ENGINEERED MUTATION
SEQADV 5UDA LYS A 27 UNP P20813 HIS 27 ENGINEERED MUTATION
SEQADV 5UDA GLY A 28 UNP P20813 ASP 28 ENGINEERED MUTATION
SEQADV 5UDA LYS A 29 UNP P20813 ARG 29 ENGINEERED MUTATION
SEQADV 5UDA HIS A 226 UNP P20813 TYR 226 ENGINEERED MUTATION
SEQADV 5UDA ARG A 262 UNP P20813 LYS 262 ENGINEERED MUTATION
SEQADV 5UDA HIS A 492 UNP P20813 EXPRESSION TAG
SEQADV 5UDA HIS A 493 UNP P20813 EXPRESSION TAG
SEQADV 5UDA HIS A 494 UNP P20813 EXPRESSION TAG
SEQADV 5UDA HIS A 495 UNP P20813 EXPRESSION TAG
SEQADV 5UDA MET B 20 UNP P20813 INITIATING METHIONINE
SEQADV 5UDA ALA B 21 UNP P20813 GLN 21 ENGINEERED MUTATION
SEQADV 5UDA LYS B 22 UNP P20813 ARG 22 ENGINEERED MUTATION
SEQADV 5UDA LYS B 23 UNP P20813 HIS 23 ENGINEERED MUTATION
SEQADV 5UDA THR B 24 UNP P20813 PRO 24 ENGINEERED MUTATION
SEQADV 5UDA SER B 25 UNP P20813 ASN 25 ENGINEERED MUTATION
SEQADV 5UDA SER B 26 UNP P20813 THR 26 ENGINEERED MUTATION
SEQADV 5UDA LYS B 27 UNP P20813 HIS 27 ENGINEERED MUTATION
SEQADV 5UDA GLY B 28 UNP P20813 ASP 28 ENGINEERED MUTATION
SEQADV 5UDA LYS B 29 UNP P20813 ARG 29 ENGINEERED MUTATION
SEQADV 5UDA HIS B 226 UNP P20813 TYR 226 ENGINEERED MUTATION
SEQADV 5UDA ARG B 262 UNP P20813 LYS 262 ENGINEERED MUTATION
SEQADV 5UDA HIS B 492 UNP P20813 EXPRESSION TAG
SEQADV 5UDA HIS B 493 UNP P20813 EXPRESSION TAG
SEQADV 5UDA HIS B 494 UNP P20813 EXPRESSION TAG
SEQADV 5UDA HIS B 495 UNP P20813 EXPRESSION TAG
SEQRES 1 A 476 MET ALA LYS LYS THR SER SER LYS GLY LYS LEU PRO PRO
SEQRES 2 A 476 GLY PRO ARG PRO LEU PRO LEU LEU GLY ASN LEU LEU GLN
SEQRES 3 A 476 MET ASP ARG ARG GLY LEU LEU LYS SER PHE LEU ARG PHE
SEQRES 4 A 476 ARG GLU LYS TYR GLY ASP VAL PHE THR VAL HIS LEU GLY
SEQRES 5 A 476 PRO ARG PRO VAL VAL MET LEU CYS GLY VAL GLU ALA ILE
SEQRES 6 A 476 ARG GLU ALA LEU VAL ASP LYS ALA GLU ALA PHE SER GLY
SEQRES 7 A 476 ARG GLY LYS ILE ALA MET VAL ASP PRO PHE PHE ARG GLY
SEQRES 8 A 476 TYR GLY VAL ILE PHE ALA ASN GLY ASN ARG TRP LYS VAL
SEQRES 9 A 476 LEU ARG ARG PHE SER VAL THR THR MET ARG ASP PHE GLY
SEQRES 10 A 476 MET GLY LYS ARG SER VAL GLU GLU ARG ILE GLN GLU GLU
SEQRES 11 A 476 ALA GLN CYS LEU ILE GLU GLU LEU ARG LYS SER LYS GLY
SEQRES 12 A 476 ALA LEU MET ASP PRO THR PHE LEU PHE GLN SER ILE THR
SEQRES 13 A 476 ALA ASN ILE ILE CYS SER ILE VAL PHE GLY LYS ARG PHE
SEQRES 14 A 476 HIS TYR GLN ASP GLN GLU PHE LEU LYS MET LEU ASN LEU
SEQRES 15 A 476 PHE TYR GLN THR PHE SER LEU ILE SER SER VAL PHE GLY
SEQRES 16 A 476 GLN LEU PHE GLU LEU PHE SER GLY PHE LEU LYS HIS PHE
SEQRES 17 A 476 PRO GLY ALA HIS ARG GLN VAL TYR LYS ASN LEU GLN GLU
SEQRES 18 A 476 ILE ASN ALA TYR ILE GLY HIS SER VAL GLU LYS HIS ARG
SEQRES 19 A 476 GLU THR LEU ASP PRO SER ALA PRO ARG ASP LEU ILE ASP
SEQRES 20 A 476 THR TYR LEU LEU HIS MET GLU LYS GLU LYS SER ASN ALA
SEQRES 21 A 476 HIS SER GLU PHE SER HIS GLN ASN LEU ASN LEU ASN THR
SEQRES 22 A 476 LEU SER LEU PHE PHE ALA GLY THR GLU THR THR SER THR
SEQRES 23 A 476 THR LEU ARG TYR GLY PHE LEU LEU MET LEU LYS TYR PRO
SEQRES 24 A 476 HIS VAL ALA GLU ARG VAL TYR ARG GLU ILE GLU GLN VAL
SEQRES 25 A 476 ILE GLY PRO HIS ARG PRO PRO GLU LEU HIS ASP ARG ALA
SEQRES 26 A 476 LYS MET PRO TYR THR GLU ALA VAL ILE TYR GLU ILE GLN
SEQRES 27 A 476 ARG PHE SER ASP LEU LEU PRO MET GLY VAL PRO HIS ILE
SEQRES 28 A 476 VAL THR GLN HIS THR SER PHE ARG GLY TYR ILE ILE PRO
SEQRES 29 A 476 LYS ASP THR GLU VAL PHE LEU ILE LEU SER THR ALA LEU
SEQRES 30 A 476 HIS ASP PRO HIS TYR PHE GLU LYS PRO ASP ALA PHE ASN
SEQRES 31 A 476 PRO ASP HIS PHE LEU ASP ALA ASN GLY ALA LEU LYS LYS
SEQRES 32 A 476 THR GLU ALA PHE ILE PRO PHE SER LEU GLY LYS ARG ILE
SEQRES 33 A 476 CYS LEU GLY GLU GLY ILE ALA ARG ALA GLU LEU PHE LEU
SEQRES 34 A 476 PHE PHE THR THR ILE LEU GLN ASN PHE SER MET ALA SER
SEQRES 35 A 476 PRO VAL ALA PRO GLU ASP ILE ASP LEU THR PRO GLN GLU
SEQRES 36 A 476 CYS GLY VAL GLY LYS ILE PRO PRO THR TYR GLN ILE ARG
SEQRES 37 A 476 PHE LEU PRO ARG HIS HIS HIS HIS
SEQRES 1 B 476 MET ALA LYS LYS THR SER SER LYS GLY LYS LEU PRO PRO
SEQRES 2 B 476 GLY PRO ARG PRO LEU PRO LEU LEU GLY ASN LEU LEU GLN
SEQRES 3 B 476 MET ASP ARG ARG GLY LEU LEU LYS SER PHE LEU ARG PHE
SEQRES 4 B 476 ARG GLU LYS TYR GLY ASP VAL PHE THR VAL HIS LEU GLY
SEQRES 5 B 476 PRO ARG PRO VAL VAL MET LEU CYS GLY VAL GLU ALA ILE
SEQRES 6 B 476 ARG GLU ALA LEU VAL ASP LYS ALA GLU ALA PHE SER GLY
SEQRES 7 B 476 ARG GLY LYS ILE ALA MET VAL ASP PRO PHE PHE ARG GLY
SEQRES 8 B 476 TYR GLY VAL ILE PHE ALA ASN GLY ASN ARG TRP LYS VAL
SEQRES 9 B 476 LEU ARG ARG PHE SER VAL THR THR MET ARG ASP PHE GLY
SEQRES 10 B 476 MET GLY LYS ARG SER VAL GLU GLU ARG ILE GLN GLU GLU
SEQRES 11 B 476 ALA GLN CYS LEU ILE GLU GLU LEU ARG LYS SER LYS GLY
SEQRES 12 B 476 ALA LEU MET ASP PRO THR PHE LEU PHE GLN SER ILE THR
SEQRES 13 B 476 ALA ASN ILE ILE CYS SER ILE VAL PHE GLY LYS ARG PHE
SEQRES 14 B 476 HIS TYR GLN ASP GLN GLU PHE LEU LYS MET LEU ASN LEU
SEQRES 15 B 476 PHE TYR GLN THR PHE SER LEU ILE SER SER VAL PHE GLY
SEQRES 16 B 476 GLN LEU PHE GLU LEU PHE SER GLY PHE LEU LYS HIS PHE
SEQRES 17 B 476 PRO GLY ALA HIS ARG GLN VAL TYR LYS ASN LEU GLN GLU
SEQRES 18 B 476 ILE ASN ALA TYR ILE GLY HIS SER VAL GLU LYS HIS ARG
SEQRES 19 B 476 GLU THR LEU ASP PRO SER ALA PRO ARG ASP LEU ILE ASP
SEQRES 20 B 476 THR TYR LEU LEU HIS MET GLU LYS GLU LYS SER ASN ALA
SEQRES 21 B 476 HIS SER GLU PHE SER HIS GLN ASN LEU ASN LEU ASN THR
SEQRES 22 B 476 LEU SER LEU PHE PHE ALA GLY THR GLU THR THR SER THR
SEQRES 23 B 476 THR LEU ARG TYR GLY PHE LEU LEU MET LEU LYS TYR PRO
SEQRES 24 B 476 HIS VAL ALA GLU ARG VAL TYR ARG GLU ILE GLU GLN VAL
SEQRES 25 B 476 ILE GLY PRO HIS ARG PRO PRO GLU LEU HIS ASP ARG ALA
SEQRES 26 B 476 LYS MET PRO TYR THR GLU ALA VAL ILE TYR GLU ILE GLN
SEQRES 27 B 476 ARG PHE SER ASP LEU LEU PRO MET GLY VAL PRO HIS ILE
SEQRES 28 B 476 VAL THR GLN HIS THR SER PHE ARG GLY TYR ILE ILE PRO
SEQRES 29 B 476 LYS ASP THR GLU VAL PHE LEU ILE LEU SER THR ALA LEU
SEQRES 30 B 476 HIS ASP PRO HIS TYR PHE GLU LYS PRO ASP ALA PHE ASN
SEQRES 31 B 476 PRO ASP HIS PHE LEU ASP ALA ASN GLY ALA LEU LYS LYS
SEQRES 32 B 476 THR GLU ALA PHE ILE PRO PHE SER LEU GLY LYS ARG ILE
SEQRES 33 B 476 CYS LEU GLY GLU GLY ILE ALA ARG ALA GLU LEU PHE LEU
SEQRES 34 B 476 PHE PHE THR THR ILE LEU GLN ASN PHE SER MET ALA SER
SEQRES 35 B 476 PRO VAL ALA PRO GLU ASP ILE ASP LEU THR PRO GLN GLU
SEQRES 36 B 476 CYS GLY VAL GLY LYS ILE PRO PRO THR TYR GLN ILE ARG
SEQRES 37 B 476 PHE LEU PRO ARG HIS HIS HIS HIS
HET HEM A 501 43
HET CAE A 502 20
HET CM5 A 503 12
HET CM5 A 504 34
HET CM5 A 505 12
HET HEM B 501 43
HET CAE B 502 20
HET CM5 B 503 12
HET CM5 B 504 34
HET CM5 B 505 12
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM CAE CAMPHANE
HETNAM CM5 5-CYCLOHEXYL-1-PENTYL-BETA-D-MALTOSIDE
HETSYN HEM HEME
HETSYN CM5 5-CYCLOHEXYLPENTYL 4-O-ALPHA-D-GLUCOPYRANOSYL-BETA-D-
HETSYN 2 CM5 GLUCOPYRANOSIDE; CYMAL-5
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 4 CAE 2(C10 H18)
FORMUL 5 CM5 6(C23 H42 O11)
FORMUL 13 HOH *481(H2 O)
HELIX 1 AA1 ASN A 42 MET A 46 5 5
HELIX 2 AA2 GLY A 50 GLY A 63 1 14
HELIX 3 AA3 GLY A 80 VAL A 89 1 10
HELIX 4 AA4 LYS A 91 SER A 96 1 6
HELIX 5 AA5 VAL A 104 ARG A 109 1 6
HELIX 6 AA6 ASN A 117 PHE A 135 1 19
HELIX 7 AA7 SER A 141 SER A 160 1 20
HELIX 8 AA8 PRO A 167 PHE A 184 1 18
HELIX 9 AA9 ASP A 192 SER A 211 1 20
HELIX 10 AB1 SER A 211 LYS A 225 1 15
HELIX 11 AB2 GLY A 229 LEU A 256 1 28
HELIX 12 AB3 ASP A 263 GLU A 275 1 13
HELIX 13 AB4 SER A 284 TYR A 317 1 34
HELIX 14 AB5 TYR A 317 ILE A 332 1 16
HELIX 15 AB6 GLU A 339 LYS A 345 5 7
HELIX 16 AB7 MET A 346 ASP A 361 1 16
HELIX 17 AB8 ILE A 391 HIS A 397 1 7
HELIX 18 AB9 ASN A 409 LEU A 414 5 6
HELIX 19 AC1 GLY A 438 ASN A 456 1 19
HELIX 20 AC2 ALA A 464 ILE A 468 5 5
HELIX 21 AC3 ASN B 42 MET B 46 5 5
HELIX 22 AC4 GLY B 50 GLY B 63 1 14
HELIX 23 AC5 GLY B 80 VAL B 89 1 10
HELIX 24 AC6 LYS B 91 SER B 96 1 6
HELIX 25 AC7 VAL B 104 ARG B 109 1 6
HELIX 26 AC8 ASN B 117 ASP B 134 1 18
HELIX 27 AC9 SER B 141 SER B 160 1 20
HELIX 28 AD1 PRO B 167 PHE B 184 1 18
HELIX 29 AD2 ASP B 192 SER B 211 1 20
HELIX 30 AD3 SER B 211 LYS B 225 1 15
HELIX 31 AD4 GLY B 229 LEU B 256 1 28
HELIX 32 AD5 ASP B 263 GLU B 275 1 13
HELIX 33 AD6 SER B 284 TYR B 317 1 34
HELIX 34 AD7 TYR B 317 ILE B 332 1 16
HELIX 35 AD8 GLU B 339 LYS B 345 5 7
HELIX 36 AD9 MET B 346 ASP B 361 1 16
HELIX 37 AE1 ILE B 391 HIS B 397 1 7
HELIX 38 AE2 ASN B 409 LEU B 414 5 6
HELIX 39 AE3 GLY B 438 ASN B 456 1 19
HELIX 40 AE4 ALA B 464 ILE B 468 5 5
SHEET 1 AA1 5 VAL A 65 LEU A 70 0
SHEET 2 AA1 5 ARG A 73 LEU A 78 -1 O MET A 77 N PHE A 66
SHEET 3 AA1 5 GLU A 387 LEU A 390 1 O PHE A 389 N LEU A 78
SHEET 4 AA1 5 HIS A 369 ILE A 370 -1 N HIS A 369 O VAL A 388
SHEET 5 AA1 5 GLY A 97 ARG A 98 -1 N GLY A 97 O ILE A 370
SHEET 1 AA2 2 THR A 375 PHE A 377 0
SHEET 2 AA2 2 TYR A 380 ILE A 382 -1 O ILE A 382 N THR A 375
SHEET 1 AA3 2 PHE A 457 ALA A 460 0
SHEET 2 AA3 2 ARG A 487 PRO A 490 -1 O LEU A 489 N SER A 458
SHEET 1 AA4 2 GLU A 474 CYS A 475 0
SHEET 2 AA4 2 LYS A 479 ILE A 480 -1 O ILE A 480 N GLU A 474
SHEET 1 AA5 5 VAL B 65 LEU B 70 0
SHEET 2 AA5 5 ARG B 73 LEU B 78 -1 O MET B 77 N PHE B 66
SHEET 3 AA5 5 GLU B 387 LEU B 390 1 O PHE B 389 N VAL B 76
SHEET 4 AA5 5 HIS B 369 ILE B 370 -1 N HIS B 369 O VAL B 388
SHEET 5 AA5 5 GLY B 97 ARG B 98 -1 N GLY B 97 O ILE B 370
SHEET 1 AA6 3 LEU B 164 MET B 165 0
SHEET 2 AA6 3 ILE B 486 PRO B 490 -1 O ILE B 486 N MET B 165
SHEET 3 AA6 3 PHE B 457 ALA B 460 -1 N SER B 458 O LEU B 489
SHEET 1 AA7 2 THR B 375 PHE B 377 0
SHEET 2 AA7 2 TYR B 380 ILE B 382 -1 O ILE B 382 N THR B 375
SHEET 1 AA8 2 GLU B 474 CYS B 475 0
SHEET 2 AA8 2 LYS B 479 ILE B 480 -1 O ILE B 480 N GLU B 474
LINK SG CYS A 436 FE HEM A 501 1555 1555 2.33
LINK SG CYS B 436 FE HEM B 501 1555 1555 2.29
SITE 1 AC1 22 ARG A 98 VAL A 113 TRP A 121 ARG A 125
SITE 2 AC1 22 MET A 132 THR A 302 THR A 303 THR A 306
SITE 3 AC1 22 LEU A 362 LEU A 363 VAL A 367 HIS A 369
SITE 4 AC1 22 LEU A 392 PRO A 428 PHE A 429 SER A 430
SITE 5 AC1 22 ARG A 434 CYS A 436 LEU A 437 GLY A 438
SITE 6 AC1 22 ALA A 442 HOH A 718
SITE 1 AC2 3 ILE A 101 ILE A 114 PHE A 206
SITE 1 AC3 1 PHE A 223
SITE 1 AC4 8 PHE A 188 GLU A 194 MET A 198 PHE A 202
SITE 2 AC4 8 ALA A 243 TYR A 244 PHE A 296 LYS B 384
SITE 1 AC5 3 ASP A 47 ARG A 48 VAL A 212
SITE 1 AC6 25 ARG B 98 VAL B 113 ILE B 114 TRP B 121
SITE 2 AC6 25 ARG B 125 MET B 132 ALA B 298 GLY B 299
SITE 3 AC6 25 THR B 302 THR B 303 THR B 306 LEU B 362
SITE 4 AC6 25 LEU B 363 VAL B 367 HIS B 369 LEU B 392
SITE 5 AC6 25 PRO B 428 PHE B 429 SER B 430 ARG B 434
SITE 6 AC6 25 CYS B 436 LEU B 437 GLY B 438 ALA B 442
SITE 7 AC6 25 HOH B 762
SITE 1 AC7 4 ILE B 101 ILE B 114 PHE B 206 VAL B 477
SITE 1 AC8 1 PHE B 223
SITE 1 AC9 7 LYS A 384 GLU B 194 MET B 198 PHE B 202
SITE 2 AC9 7 ILE B 241 TYR B 244 PHE B 296
SITE 1 AD1 2 ARG B 48 LEU B 51
CRYST1 77.490 77.490 202.150 90.00 90.00 120.00 P 32 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 0.012905 0.007451 0.000000 0.00000
SCALE2 0.000000 0.014901 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004947 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
