HEADER OXIDOREDUCTASE 24-JUL-09 3A51
TITLE STRUCTURE OF CYTOCHROME P450 VDH MUTANT (VDH-K1) OBTAINED BY DIRECTED
TITLE 2 EVOLUTION WITH BOUND 25-HYDROXYVITAMIN D3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VITAMIN D HYDROXYLASE;
COMPND 3 CHAIN: A, B, C, D, E;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDONOCARDIA AUTOTROPHICA;
SOURCE 3 ORGANISM_TAXID: 2074;
SOURCE 4 STRAIN: NBRC 12743;
SOURCE 5 GENE: VDH;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET22
KEYWDS CYTOCHROME P450, VITAMIN D3 HYDROXYLASE, HEMOPROTEIN, MONOOXYGENASE,
KEYWDS 2 DIRECTED EVOLUTION, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.YASUTAKE,Y.FUJII,W.K.CHEON,A.ARISAWA,T.TAMURA
REVDAT 3 01-NOV-23 3A51 1 REMARK SEQADV LINK
REVDAT 2 17-NOV-10 3A51 1 JRNL
REVDAT 1 28-JUL-10 3A51 0
JRNL AUTH Y.YASUTAKE,Y.FUJII,T.NISHIOKA,W.K.CHEON,A.ARISAWA,T.TAMURA
JRNL TITL STRUCTURAL EVIDENCE FOR ENHANCEMENT OF SEQUENTIAL VITAMIN D3
JRNL TITL 2 HYDROXYLATION ACTIVITIES BY DIRECTED EVOLUTION OF CYTOCHROME
JRNL TITL 3 P450 VITAMIN D3 HYDROXYLASE
JRNL REF J.BIOL.CHEM. V. 285 31193 2010
JRNL REFN ISSN 0021-9258
JRNL PMID 20667833
JRNL DOI 10.1074/JBC.M110.147009
REMARK 2
REMARK 2 RESOLUTION. 2.00 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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.60
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 161521
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) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 8447
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 11803
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.95
REMARK 3 BIN R VALUE (WORKING SET) : 0.2390
REMARK 3 BIN FREE R VALUE SET COUNT : 632
REMARK 3 BIN FREE R VALUE : 0.3100
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 15555
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 406
REMARK 3 SOLVENT ATOMS : 1319
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.42
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.53000
REMARK 3 B22 (A**2) : -0.23000
REMARK 3 B33 (A**2) : -0.29000
REMARK 3 B12 (A**2) : 0.00000
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): 0.173
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.156
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.110
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.887
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.932
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 16336 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 22304 ; 1.548 ; 2.040
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2007 ; 5.782 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 716 ;31.190 ;22.919
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2631 ;14.984 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 171 ;18.893 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2485 ; 0.102 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 12508 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 7994 ; 0.203 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 11205 ; 0.303 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1354 ; 0.139 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 6 ; 0.087 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 121 ; 0.162 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 24 ; 0.168 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): 4 ; 0.024 ; 0.200
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): 10372 ; 0.920 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 16207 ; 1.463 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 6686 ; 2.178 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 6085 ; 3.383 ; 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 : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3A51 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-JUL-09.
REMARK 100 THE DEPOSITION ID IS D_1000028819.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-DEC-08
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 : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NW12A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : SI(111) DOUBLE CRYSTAL
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 170383
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.400
REMARK 200 R MERGE (I) : 0.07700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 32.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.00
REMARK 200 R MERGE FOR SHELL (I) : 0.59400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.300
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 3A4G
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M CALCIUM ACETATE, 10.8% PEG3350,
REMARK 280 PH7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 38.58650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 94.57150
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 85.90000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 94.57150
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.58650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 85.90000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5
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 350
REMARK 350 BIOMOLECULE: 4
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: D
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: 5
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: E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 1
REMARK 465 LEU A 404
REMARK 465 GLU A 405
REMARK 465 HIS A 406
REMARK 465 HIS A 407
REMARK 465 HIS A 408
REMARK 465 HIS A 409
REMARK 465 HIS A 410
REMARK 465 HIS A 411
REMARK 465 MET B 1
REMARK 465 LEU B 404
REMARK 465 GLU B 405
REMARK 465 HIS B 406
REMARK 465 HIS B 407
REMARK 465 HIS B 408
REMARK 465 HIS B 409
REMARK 465 HIS B 410
REMARK 465 HIS B 411
REMARK 465 MET C 1
REMARK 465 ALA C 403
REMARK 465 LEU C 404
REMARK 465 GLU C 405
REMARK 465 HIS C 406
REMARK 465 HIS C 407
REMARK 465 HIS C 408
REMARK 465 HIS C 409
REMARK 465 HIS C 410
REMARK 465 HIS C 411
REMARK 465 MET D 1
REMARK 465 LEU D 404
REMARK 465 GLU D 405
REMARK 465 HIS D 406
REMARK 465 HIS D 407
REMARK 465 HIS D 408
REMARK 465 HIS D 409
REMARK 465 HIS D 410
REMARK 465 HIS D 411
REMARK 465 MET E 1
REMARK 465 ALA E 403
REMARK 465 LEU E 404
REMARK 465 GLU E 405
REMARK 465 HIS E 406
REMARK 465 HIS E 407
REMARK 465 HIS E 408
REMARK 465 HIS E 409
REMARK 465 HIS E 410
REMARK 465 HIS E 411
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 ASP A 33 61.12 -155.35
REMARK 500 ASP A 74 -17.82 -40.75
REMARK 500 TYR A 141 -60.98 -147.50
REMARK 500 ASP A 173 -168.20 -114.39
REMARK 500 ASP A 174 23.01 -77.73
REMARK 500 ASP A 217 87.48 -155.74
REMARK 500 THR A 240 -73.36 -120.48
REMARK 500 ASP A 280 70.77 -151.03
REMARK 500 HIS A 342 138.49 -172.29
REMARK 500 CYS A 347 113.89 -37.53
REMARK 500 ASP B 33 68.09 -153.60
REMARK 500 TYR B 141 -61.96 -147.92
REMARK 500 ASP B 173 -164.60 -100.54
REMARK 500 PRO B 176 151.56 -49.69
REMARK 500 ASP B 217 95.48 -163.34
REMARK 500 THR B 240 -71.22 -121.67
REMARK 500 ASP B 280 68.80 -154.08
REMARK 500 ASP B 333 60.39 -104.91
REMARK 500 HIS B 342 137.69 -172.10
REMARK 500 CYS B 347 113.21 -35.64
REMARK 500 ASP C 33 67.77 -156.14
REMARK 500 MET C 138 -70.74 -57.91
REMARK 500 TYR C 141 -65.24 -146.37
REMARK 500 THR C 240 -73.57 -124.56
REMARK 500 ARG C 332 136.96 -38.19
REMARK 500 ASP C 333 77.74 -109.04
REMARK 500 HIS C 342 136.64 177.50
REMARK 500 ASP D 33 65.09 -153.55
REMARK 500 PRO D 41 -71.48 -53.03
REMARK 500 MET D 138 -73.18 -58.22
REMARK 500 TYR D 141 -67.09 -140.20
REMARK 500 ASP D 174 21.73 -68.65
REMARK 500 THR D 240 -73.44 -123.76
REMARK 500 ASP D 333 67.89 -102.75
REMARK 500 HIS D 342 132.68 -175.25
REMARK 500 CYS D 347 118.03 -35.87
REMARK 500 TYR E 141 -57.24 -150.33
REMARK 500 THR E 240 -74.22 -123.85
REMARK 500 HIS E 342 131.32 -176.82
REMARK 500 CYS E 347 118.19 -37.29
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A2505 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 128 O
REMARK 620 2 HOH A 593 O 87.3
REMARK 620 3 HOH A 905 O 73.7 93.0
REMARK 620 4 HOH A 929 O 99.1 173.6 89.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A2501 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 204 OD1
REMARK 620 2 HOH A 528 O 73.7
REMARK 620 3 HOH A 579 O 102.4 81.0
REMARK 620 4 HOH A 926 O 105.8 75.1 135.7
REMARK 620 5 GOL A3002 O3 89.9 140.2 138.6 75.0
REMARK 620 6 GOL A3002 O2 87.3 142.8 72.1 141.8 69.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A2506 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 320 O
REMARK 620 2 ASP D 320 O 165.2
REMARK 620 3 HOH D 933 O 109.7 59.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 412 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 347 SG
REMARK 620 2 HEM A 412 NA 100.1
REMARK 620 3 HEM A 412 NB 88.5 89.5
REMARK 620 4 HEM A 412 NC 89.6 170.2 89.1
REMARK 620 5 HEM A 412 ND 102.5 88.0 169.0 91.5
REMARK 620 6 VDY A6178 O1 174.4 82.6 86.6 87.5 82.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 412 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 347 SG
REMARK 620 2 HEM B 412 NA 99.0
REMARK 620 3 HEM B 412 NB 87.1 85.7
REMARK 620 4 HEM B 412 NC 90.1 170.5 92.2
REMARK 620 5 HEM B 412 ND 103.0 91.2 169.8 89.2
REMARK 620 6 VDY B6178 O1 171.5 80.8 84.4 89.8 85.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C2503 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 204 OD1
REMARK 620 2 HOH C 482 O 86.7
REMARK 620 3 HOH C 703 O 77.9 76.8
REMARK 620 4 ACT C4004 OXT 95.1 126.9 155.3
REMARK 620 5 ACT C4004 O 81.0 80.3 149.5 48.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM C 412 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 347 SG
REMARK 620 2 HEM C 412 NA 100.0
REMARK 620 3 HEM C 412 NB 88.2 87.9
REMARK 620 4 HEM C 412 NC 87.3 172.0 89.1
REMARK 620 5 HEM C 412 ND 100.1 89.3 171.6 92.6
REMARK 620 6 VDY C6178 O1 171.6 85.3 85.5 87.1 86.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D2502 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 204 OD1
REMARK 620 2 HOH D 601 O 86.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM D 412 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 347 SG
REMARK 620 2 HEM D 412 NA 102.5
REMARK 620 3 HEM D 412 NB 88.1 89.5
REMARK 620 4 HEM D 412 NC 88.5 168.5 87.7
REMARK 620 5 HEM D 412 ND 103.3 88.9 168.6 91.6
REMARK 620 6 VDY D6178 O1 176.2 76.6 88.2 92.1 80.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E2504 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 204 OD1
REMARK 620 2 HOH E 565 O 119.9
REMARK 620 3 HOH E 576 O 87.7 138.4
REMARK 620 4 HOH E 652 O 152.8 82.2 83.8
REMARK 620 5 ACT E4005 O 76.8 133.9 79.1 76.2
REMARK 620 6 ACT E4005 OXT 88.5 91.1 122.2 74.6 44.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM E 412 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E 347 SG
REMARK 620 2 HEM E 412 NA 100.0
REMARK 620 3 HEM E 412 NB 89.1 88.6
REMARK 620 4 HEM E 412 NC 89.6 170.3 90.7
REMARK 620 5 HEM E 412 ND 101.8 86.7 168.8 92.3
REMARK 620 6 VDY E6178 O1 174.2 79.4 85.1 90.8 84.0
REMARK 620 N 1 2 3 4 5
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 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VDY A 6178
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 3001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 4006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 3002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VDY B 6178
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 4009
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VDY C 6178
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 2503
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 4004
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 4007
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VDY D 6178
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 2502
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT D 4001
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM E 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VDY E 6178
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 2504
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT E 4005
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT E 4008
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3A4G RELATED DB: PDB
REMARK 900 WILD-TYPE VDH
REMARK 900 RELATED ID: 3A4H RELATED DB: PDB
REMARK 900 WILD-TYPE VDH
REMARK 900 RELATED ID: 3A4Z RELATED DB: PDB
REMARK 900 RELATED ID: 3A50 RELATED DB: PDB
DBREF 3A51 A 1 403 UNP C4B644 C4B644_9PSEU 1 403
DBREF 3A51 B 1 403 UNP C4B644 C4B644_9PSEU 1 403
DBREF 3A51 C 1 403 UNP C4B644 C4B644_9PSEU 1 403
DBREF 3A51 D 1 403 UNP C4B644 C4B644_9PSEU 1 403
DBREF 3A51 E 1 403 UNP C4B644 C4B644_9PSEU 1 403
SEQADV 3A51 ARG A 70 UNP C4B644 THR 70 ENGINEERED MUTATION
SEQADV 3A51 LEU A 156 UNP C4B644 VAL 156 ENGINEERED MUTATION
SEQADV 3A51 MET A 216 UNP C4B644 GLU 216 ENGINEERED MUTATION
SEQADV 3A51 ARG A 384 UNP C4B644 GLU 384 ENGINEERED MUTATION
SEQADV 3A51 LEU A 404 UNP C4B644 EXPRESSION TAG
SEQADV 3A51 GLU A 405 UNP C4B644 EXPRESSION TAG
SEQADV 3A51 HIS A 406 UNP C4B644 EXPRESSION TAG
SEQADV 3A51 HIS A 407 UNP C4B644 EXPRESSION TAG
SEQADV 3A51 HIS A 408 UNP C4B644 EXPRESSION TAG
SEQADV 3A51 HIS A 409 UNP C4B644 EXPRESSION TAG
SEQADV 3A51 HIS A 410 UNP C4B644 EXPRESSION TAG
SEQADV 3A51 HIS A 411 UNP C4B644 EXPRESSION TAG
SEQADV 3A51 ARG B 70 UNP C4B644 THR 70 ENGINEERED MUTATION
SEQADV 3A51 LEU B 156 UNP C4B644 VAL 156 ENGINEERED MUTATION
SEQADV 3A51 MET B 216 UNP C4B644 GLU 216 ENGINEERED MUTATION
SEQADV 3A51 ARG B 384 UNP C4B644 GLU 384 ENGINEERED MUTATION
SEQADV 3A51 LEU B 404 UNP C4B644 EXPRESSION TAG
SEQADV 3A51 GLU B 405 UNP C4B644 EXPRESSION TAG
SEQADV 3A51 HIS B 406 UNP C4B644 EXPRESSION TAG
SEQADV 3A51 HIS B 407 UNP C4B644 EXPRESSION TAG
SEQADV 3A51 HIS B 408 UNP C4B644 EXPRESSION TAG
SEQADV 3A51 HIS B 409 UNP C4B644 EXPRESSION TAG
SEQADV 3A51 HIS B 410 UNP C4B644 EXPRESSION TAG
SEQADV 3A51 HIS B 411 UNP C4B644 EXPRESSION TAG
SEQADV 3A51 ARG C 70 UNP C4B644 THR 70 ENGINEERED MUTATION
SEQADV 3A51 LEU C 156 UNP C4B644 VAL 156 ENGINEERED MUTATION
SEQADV 3A51 MET C 216 UNP C4B644 GLU 216 ENGINEERED MUTATION
SEQADV 3A51 ARG C 384 UNP C4B644 GLU 384 ENGINEERED MUTATION
SEQADV 3A51 LEU C 404 UNP C4B644 EXPRESSION TAG
SEQADV 3A51 GLU C 405 UNP C4B644 EXPRESSION TAG
SEQADV 3A51 HIS C 406 UNP C4B644 EXPRESSION TAG
SEQADV 3A51 HIS C 407 UNP C4B644 EXPRESSION TAG
SEQADV 3A51 HIS C 408 UNP C4B644 EXPRESSION TAG
SEQADV 3A51 HIS C 409 UNP C4B644 EXPRESSION TAG
SEQADV 3A51 HIS C 410 UNP C4B644 EXPRESSION TAG
SEQADV 3A51 HIS C 411 UNP C4B644 EXPRESSION TAG
SEQADV 3A51 ARG D 70 UNP C4B644 THR 70 ENGINEERED MUTATION
SEQADV 3A51 LEU D 156 UNP C4B644 VAL 156 ENGINEERED MUTATION
SEQADV 3A51 MET D 216 UNP C4B644 GLU 216 ENGINEERED MUTATION
SEQADV 3A51 ARG D 384 UNP C4B644 GLU 384 ENGINEERED MUTATION
SEQADV 3A51 LEU D 404 UNP C4B644 EXPRESSION TAG
SEQADV 3A51 GLU D 405 UNP C4B644 EXPRESSION TAG
SEQADV 3A51 HIS D 406 UNP C4B644 EXPRESSION TAG
SEQADV 3A51 HIS D 407 UNP C4B644 EXPRESSION TAG
SEQADV 3A51 HIS D 408 UNP C4B644 EXPRESSION TAG
SEQADV 3A51 HIS D 409 UNP C4B644 EXPRESSION TAG
SEQADV 3A51 HIS D 410 UNP C4B644 EXPRESSION TAG
SEQADV 3A51 HIS D 411 UNP C4B644 EXPRESSION TAG
SEQADV 3A51 ARG E 70 UNP C4B644 THR 70 ENGINEERED MUTATION
SEQADV 3A51 LEU E 156 UNP C4B644 VAL 156 ENGINEERED MUTATION
SEQADV 3A51 MET E 216 UNP C4B644 GLU 216 ENGINEERED MUTATION
SEQADV 3A51 ARG E 384 UNP C4B644 GLU 384 ENGINEERED MUTATION
SEQADV 3A51 LEU E 404 UNP C4B644 EXPRESSION TAG
SEQADV 3A51 GLU E 405 UNP C4B644 EXPRESSION TAG
SEQADV 3A51 HIS E 406 UNP C4B644 EXPRESSION TAG
SEQADV 3A51 HIS E 407 UNP C4B644 EXPRESSION TAG
SEQADV 3A51 HIS E 408 UNP C4B644 EXPRESSION TAG
SEQADV 3A51 HIS E 409 UNP C4B644 EXPRESSION TAG
SEQADV 3A51 HIS E 410 UNP C4B644 EXPRESSION TAG
SEQADV 3A51 HIS E 411 UNP C4B644 EXPRESSION TAG
SEQRES 1 A 411 MET ALA LEU THR THR THR GLY THR GLU GLN HIS ASP LEU
SEQRES 2 A 411 PHE SER GLY THR PHE TRP GLN ASN PRO HIS PRO ALA TYR
SEQRES 3 A 411 ALA ALA LEU ARG ALA GLU ASP PRO VAL ARG LYS LEU ALA
SEQRES 4 A 411 LEU PRO ASP GLY PRO VAL TRP LEU LEU THR ARG TYR ALA
SEQRES 5 A 411 ASP VAL ARG GLU ALA PHE VAL ASP PRO ARG LEU SER LYS
SEQRES 6 A 411 ASP TRP ARG HIS ARG LEU PRO GLU ASP GLN ARG ALA ASP
SEQRES 7 A 411 MET PRO ALA THR PRO THR PRO MET MET ILE LEU MET ASP
SEQRES 8 A 411 PRO PRO ASP HIS THR ARG LEU ARG LYS LEU VAL GLY ARG
SEQRES 9 A 411 SER PHE THR VAL ARG ARG MET ASN GLU LEU GLU PRO ARG
SEQRES 10 A 411 ILE THR GLU ILE ALA ASP GLY LEU LEU ALA GLY LEU PRO
SEQRES 11 A 411 THR ASP GLY PRO VAL ASP LEU MET ARG GLU TYR ALA PHE
SEQRES 12 A 411 GLN ILE PRO VAL GLN VAL ILE CYS GLU LEU LEU GLY LEU
SEQRES 13 A 411 PRO ALA GLU ASP ARG ASP ASP PHE SER ALA TRP SER SER
SEQRES 14 A 411 VAL LEU VAL ASP ASP SER PRO ALA ASP ASP LYS ASN ALA
SEQRES 15 A 411 ALA MET GLY LYS LEU HIS GLY TYR LEU SER ASP LEU LEU
SEQRES 16 A 411 GLU ARG LYS ARG THR GLU PRO ASP ASP ALA LEU LEU SER
SEQRES 17 A 411 SER LEU LEU ALA VAL SER ASP MET ASP GLY ASP ARG LEU
SEQRES 18 A 411 SER GLN GLU GLU LEU VAL ALA MET ALA MET LEU LEU LEU
SEQRES 19 A 411 ILE ALA GLY HIS GLU THR THR VAL ASN LEU ILE GLY ASN
SEQRES 20 A 411 GLY VAL LEU ALA LEU LEU THR HIS PRO ASP GLN ARG LYS
SEQRES 21 A 411 LEU LEU ALA GLU ASP PRO SER LEU ILE SER SER ALA VAL
SEQRES 22 A 411 GLU GLU PHE LEU ARG PHE ASP SER PRO VAL SER GLN ALA
SEQRES 23 A 411 PRO ILE ARG PHE THR ALA GLU ASP VAL THR TYR SER GLY
SEQRES 24 A 411 VAL THR ILE PRO ALA GLY GLU MET VAL MET LEU GLY LEU
SEQRES 25 A 411 ALA ALA ALA ASN ARG ASP ALA ASP TRP MET PRO GLU PRO
SEQRES 26 A 411 ASP ARG LEU ASP ILE THR ARG ASP ALA SER GLY GLY VAL
SEQRES 27 A 411 PHE PHE GLY HIS GLY ILE HIS PHE CYS LEU GLY ALA GLN
SEQRES 28 A 411 LEU ALA ARG LEU GLU GLY ARG VAL ALA ILE GLY ARG LEU
SEQRES 29 A 411 PHE ALA ASP ARG PRO GLU LEU ALA LEU ALA VAL GLY LEU
SEQRES 30 A 411 ASP GLU LEU VAL TYR ARG ARG SER THR LEU VAL ARG GLY
SEQRES 31 A 411 LEU SER ARG MET PRO VAL THR MET GLY PRO ARG SER ALA
SEQRES 32 A 411 LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 411 MET ALA LEU THR THR THR GLY THR GLU GLN HIS ASP LEU
SEQRES 2 B 411 PHE SER GLY THR PHE TRP GLN ASN PRO HIS PRO ALA TYR
SEQRES 3 B 411 ALA ALA LEU ARG ALA GLU ASP PRO VAL ARG LYS LEU ALA
SEQRES 4 B 411 LEU PRO ASP GLY PRO VAL TRP LEU LEU THR ARG TYR ALA
SEQRES 5 B 411 ASP VAL ARG GLU ALA PHE VAL ASP PRO ARG LEU SER LYS
SEQRES 6 B 411 ASP TRP ARG HIS ARG LEU PRO GLU ASP GLN ARG ALA ASP
SEQRES 7 B 411 MET PRO ALA THR PRO THR PRO MET MET ILE LEU MET ASP
SEQRES 8 B 411 PRO PRO ASP HIS THR ARG LEU ARG LYS LEU VAL GLY ARG
SEQRES 9 B 411 SER PHE THR VAL ARG ARG MET ASN GLU LEU GLU PRO ARG
SEQRES 10 B 411 ILE THR GLU ILE ALA ASP GLY LEU LEU ALA GLY LEU PRO
SEQRES 11 B 411 THR ASP GLY PRO VAL ASP LEU MET ARG GLU TYR ALA PHE
SEQRES 12 B 411 GLN ILE PRO VAL GLN VAL ILE CYS GLU LEU LEU GLY LEU
SEQRES 13 B 411 PRO ALA GLU ASP ARG ASP ASP PHE SER ALA TRP SER SER
SEQRES 14 B 411 VAL LEU VAL ASP ASP SER PRO ALA ASP ASP LYS ASN ALA
SEQRES 15 B 411 ALA MET GLY LYS LEU HIS GLY TYR LEU SER ASP LEU LEU
SEQRES 16 B 411 GLU ARG LYS ARG THR GLU PRO ASP ASP ALA LEU LEU SER
SEQRES 17 B 411 SER LEU LEU ALA VAL SER ASP MET ASP GLY ASP ARG LEU
SEQRES 18 B 411 SER GLN GLU GLU LEU VAL ALA MET ALA MET LEU LEU LEU
SEQRES 19 B 411 ILE ALA GLY HIS GLU THR THR VAL ASN LEU ILE GLY ASN
SEQRES 20 B 411 GLY VAL LEU ALA LEU LEU THR HIS PRO ASP GLN ARG LYS
SEQRES 21 B 411 LEU LEU ALA GLU ASP PRO SER LEU ILE SER SER ALA VAL
SEQRES 22 B 411 GLU GLU PHE LEU ARG PHE ASP SER PRO VAL SER GLN ALA
SEQRES 23 B 411 PRO ILE ARG PHE THR ALA GLU ASP VAL THR TYR SER GLY
SEQRES 24 B 411 VAL THR ILE PRO ALA GLY GLU MET VAL MET LEU GLY LEU
SEQRES 25 B 411 ALA ALA ALA ASN ARG ASP ALA ASP TRP MET PRO GLU PRO
SEQRES 26 B 411 ASP ARG LEU ASP ILE THR ARG ASP ALA SER GLY GLY VAL
SEQRES 27 B 411 PHE PHE GLY HIS GLY ILE HIS PHE CYS LEU GLY ALA GLN
SEQRES 28 B 411 LEU ALA ARG LEU GLU GLY ARG VAL ALA ILE GLY ARG LEU
SEQRES 29 B 411 PHE ALA ASP ARG PRO GLU LEU ALA LEU ALA VAL GLY LEU
SEQRES 30 B 411 ASP GLU LEU VAL TYR ARG ARG SER THR LEU VAL ARG GLY
SEQRES 31 B 411 LEU SER ARG MET PRO VAL THR MET GLY PRO ARG SER ALA
SEQRES 32 B 411 LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 C 411 MET ALA LEU THR THR THR GLY THR GLU GLN HIS ASP LEU
SEQRES 2 C 411 PHE SER GLY THR PHE TRP GLN ASN PRO HIS PRO ALA TYR
SEQRES 3 C 411 ALA ALA LEU ARG ALA GLU ASP PRO VAL ARG LYS LEU ALA
SEQRES 4 C 411 LEU PRO ASP GLY PRO VAL TRP LEU LEU THR ARG TYR ALA
SEQRES 5 C 411 ASP VAL ARG GLU ALA PHE VAL ASP PRO ARG LEU SER LYS
SEQRES 6 C 411 ASP TRP ARG HIS ARG LEU PRO GLU ASP GLN ARG ALA ASP
SEQRES 7 C 411 MET PRO ALA THR PRO THR PRO MET MET ILE LEU MET ASP
SEQRES 8 C 411 PRO PRO ASP HIS THR ARG LEU ARG LYS LEU VAL GLY ARG
SEQRES 9 C 411 SER PHE THR VAL ARG ARG MET ASN GLU LEU GLU PRO ARG
SEQRES 10 C 411 ILE THR GLU ILE ALA ASP GLY LEU LEU ALA GLY LEU PRO
SEQRES 11 C 411 THR ASP GLY PRO VAL ASP LEU MET ARG GLU TYR ALA PHE
SEQRES 12 C 411 GLN ILE PRO VAL GLN VAL ILE CYS GLU LEU LEU GLY LEU
SEQRES 13 C 411 PRO ALA GLU ASP ARG ASP ASP PHE SER ALA TRP SER SER
SEQRES 14 C 411 VAL LEU VAL ASP ASP SER PRO ALA ASP ASP LYS ASN ALA
SEQRES 15 C 411 ALA MET GLY LYS LEU HIS GLY TYR LEU SER ASP LEU LEU
SEQRES 16 C 411 GLU ARG LYS ARG THR GLU PRO ASP ASP ALA LEU LEU SER
SEQRES 17 C 411 SER LEU LEU ALA VAL SER ASP MET ASP GLY ASP ARG LEU
SEQRES 18 C 411 SER GLN GLU GLU LEU VAL ALA MET ALA MET LEU LEU LEU
SEQRES 19 C 411 ILE ALA GLY HIS GLU THR THR VAL ASN LEU ILE GLY ASN
SEQRES 20 C 411 GLY VAL LEU ALA LEU LEU THR HIS PRO ASP GLN ARG LYS
SEQRES 21 C 411 LEU LEU ALA GLU ASP PRO SER LEU ILE SER SER ALA VAL
SEQRES 22 C 411 GLU GLU PHE LEU ARG PHE ASP SER PRO VAL SER GLN ALA
SEQRES 23 C 411 PRO ILE ARG PHE THR ALA GLU ASP VAL THR TYR SER GLY
SEQRES 24 C 411 VAL THR ILE PRO ALA GLY GLU MET VAL MET LEU GLY LEU
SEQRES 25 C 411 ALA ALA ALA ASN ARG ASP ALA ASP TRP MET PRO GLU PRO
SEQRES 26 C 411 ASP ARG LEU ASP ILE THR ARG ASP ALA SER GLY GLY VAL
SEQRES 27 C 411 PHE PHE GLY HIS GLY ILE HIS PHE CYS LEU GLY ALA GLN
SEQRES 28 C 411 LEU ALA ARG LEU GLU GLY ARG VAL ALA ILE GLY ARG LEU
SEQRES 29 C 411 PHE ALA ASP ARG PRO GLU LEU ALA LEU ALA VAL GLY LEU
SEQRES 30 C 411 ASP GLU LEU VAL TYR ARG ARG SER THR LEU VAL ARG GLY
SEQRES 31 C 411 LEU SER ARG MET PRO VAL THR MET GLY PRO ARG SER ALA
SEQRES 32 C 411 LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 D 411 MET ALA LEU THR THR THR GLY THR GLU GLN HIS ASP LEU
SEQRES 2 D 411 PHE SER GLY THR PHE TRP GLN ASN PRO HIS PRO ALA TYR
SEQRES 3 D 411 ALA ALA LEU ARG ALA GLU ASP PRO VAL ARG LYS LEU ALA
SEQRES 4 D 411 LEU PRO ASP GLY PRO VAL TRP LEU LEU THR ARG TYR ALA
SEQRES 5 D 411 ASP VAL ARG GLU ALA PHE VAL ASP PRO ARG LEU SER LYS
SEQRES 6 D 411 ASP TRP ARG HIS ARG LEU PRO GLU ASP GLN ARG ALA ASP
SEQRES 7 D 411 MET PRO ALA THR PRO THR PRO MET MET ILE LEU MET ASP
SEQRES 8 D 411 PRO PRO ASP HIS THR ARG LEU ARG LYS LEU VAL GLY ARG
SEQRES 9 D 411 SER PHE THR VAL ARG ARG MET ASN GLU LEU GLU PRO ARG
SEQRES 10 D 411 ILE THR GLU ILE ALA ASP GLY LEU LEU ALA GLY LEU PRO
SEQRES 11 D 411 THR ASP GLY PRO VAL ASP LEU MET ARG GLU TYR ALA PHE
SEQRES 12 D 411 GLN ILE PRO VAL GLN VAL ILE CYS GLU LEU LEU GLY LEU
SEQRES 13 D 411 PRO ALA GLU ASP ARG ASP ASP PHE SER ALA TRP SER SER
SEQRES 14 D 411 VAL LEU VAL ASP ASP SER PRO ALA ASP ASP LYS ASN ALA
SEQRES 15 D 411 ALA MET GLY LYS LEU HIS GLY TYR LEU SER ASP LEU LEU
SEQRES 16 D 411 GLU ARG LYS ARG THR GLU PRO ASP ASP ALA LEU LEU SER
SEQRES 17 D 411 SER LEU LEU ALA VAL SER ASP MET ASP GLY ASP ARG LEU
SEQRES 18 D 411 SER GLN GLU GLU LEU VAL ALA MET ALA MET LEU LEU LEU
SEQRES 19 D 411 ILE ALA GLY HIS GLU THR THR VAL ASN LEU ILE GLY ASN
SEQRES 20 D 411 GLY VAL LEU ALA LEU LEU THR HIS PRO ASP GLN ARG LYS
SEQRES 21 D 411 LEU LEU ALA GLU ASP PRO SER LEU ILE SER SER ALA VAL
SEQRES 22 D 411 GLU GLU PHE LEU ARG PHE ASP SER PRO VAL SER GLN ALA
SEQRES 23 D 411 PRO ILE ARG PHE THR ALA GLU ASP VAL THR TYR SER GLY
SEQRES 24 D 411 VAL THR ILE PRO ALA GLY GLU MET VAL MET LEU GLY LEU
SEQRES 25 D 411 ALA ALA ALA ASN ARG ASP ALA ASP TRP MET PRO GLU PRO
SEQRES 26 D 411 ASP ARG LEU ASP ILE THR ARG ASP ALA SER GLY GLY VAL
SEQRES 27 D 411 PHE PHE GLY HIS GLY ILE HIS PHE CYS LEU GLY ALA GLN
SEQRES 28 D 411 LEU ALA ARG LEU GLU GLY ARG VAL ALA ILE GLY ARG LEU
SEQRES 29 D 411 PHE ALA ASP ARG PRO GLU LEU ALA LEU ALA VAL GLY LEU
SEQRES 30 D 411 ASP GLU LEU VAL TYR ARG ARG SER THR LEU VAL ARG GLY
SEQRES 31 D 411 LEU SER ARG MET PRO VAL THR MET GLY PRO ARG SER ALA
SEQRES 32 D 411 LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 E 411 MET ALA LEU THR THR THR GLY THR GLU GLN HIS ASP LEU
SEQRES 2 E 411 PHE SER GLY THR PHE TRP GLN ASN PRO HIS PRO ALA TYR
SEQRES 3 E 411 ALA ALA LEU ARG ALA GLU ASP PRO VAL ARG LYS LEU ALA
SEQRES 4 E 411 LEU PRO ASP GLY PRO VAL TRP LEU LEU THR ARG TYR ALA
SEQRES 5 E 411 ASP VAL ARG GLU ALA PHE VAL ASP PRO ARG LEU SER LYS
SEQRES 6 E 411 ASP TRP ARG HIS ARG LEU PRO GLU ASP GLN ARG ALA ASP
SEQRES 7 E 411 MET PRO ALA THR PRO THR PRO MET MET ILE LEU MET ASP
SEQRES 8 E 411 PRO PRO ASP HIS THR ARG LEU ARG LYS LEU VAL GLY ARG
SEQRES 9 E 411 SER PHE THR VAL ARG ARG MET ASN GLU LEU GLU PRO ARG
SEQRES 10 E 411 ILE THR GLU ILE ALA ASP GLY LEU LEU ALA GLY LEU PRO
SEQRES 11 E 411 THR ASP GLY PRO VAL ASP LEU MET ARG GLU TYR ALA PHE
SEQRES 12 E 411 GLN ILE PRO VAL GLN VAL ILE CYS GLU LEU LEU GLY LEU
SEQRES 13 E 411 PRO ALA GLU ASP ARG ASP ASP PHE SER ALA TRP SER SER
SEQRES 14 E 411 VAL LEU VAL ASP ASP SER PRO ALA ASP ASP LYS ASN ALA
SEQRES 15 E 411 ALA MET GLY LYS LEU HIS GLY TYR LEU SER ASP LEU LEU
SEQRES 16 E 411 GLU ARG LYS ARG THR GLU PRO ASP ASP ALA LEU LEU SER
SEQRES 17 E 411 SER LEU LEU ALA VAL SER ASP MET ASP GLY ASP ARG LEU
SEQRES 18 E 411 SER GLN GLU GLU LEU VAL ALA MET ALA MET LEU LEU LEU
SEQRES 19 E 411 ILE ALA GLY HIS GLU THR THR VAL ASN LEU ILE GLY ASN
SEQRES 20 E 411 GLY VAL LEU ALA LEU LEU THR HIS PRO ASP GLN ARG LYS
SEQRES 21 E 411 LEU LEU ALA GLU ASP PRO SER LEU ILE SER SER ALA VAL
SEQRES 22 E 411 GLU GLU PHE LEU ARG PHE ASP SER PRO VAL SER GLN ALA
SEQRES 23 E 411 PRO ILE ARG PHE THR ALA GLU ASP VAL THR TYR SER GLY
SEQRES 24 E 411 VAL THR ILE PRO ALA GLY GLU MET VAL MET LEU GLY LEU
SEQRES 25 E 411 ALA ALA ALA ASN ARG ASP ALA ASP TRP MET PRO GLU PRO
SEQRES 26 E 411 ASP ARG LEU ASP ILE THR ARG ASP ALA SER GLY GLY VAL
SEQRES 27 E 411 PHE PHE GLY HIS GLY ILE HIS PHE CYS LEU GLY ALA GLN
SEQRES 28 E 411 LEU ALA ARG LEU GLU GLY ARG VAL ALA ILE GLY ARG LEU
SEQRES 29 E 411 PHE ALA ASP ARG PRO GLU LEU ALA LEU ALA VAL GLY LEU
SEQRES 30 E 411 ASP GLU LEU VAL TYR ARG ARG SER THR LEU VAL ARG GLY
SEQRES 31 E 411 LEU SER ARG MET PRO VAL THR MET GLY PRO ARG SER ALA
SEQRES 32 E 411 LEU GLU HIS HIS HIS HIS HIS HIS
HET HEM A 412 43
HET VDY A6178 29
HET CA A2501 1
HET CA A2505 1
HET CA A2506 1
HET GOL A3001 6
HET ACT A4006 4
HET GOL A3002 6
HET HEM B 412 43
HET VDY B6178 29
HET ACT B4009 4
HET HEM C 412 43
HET VDY C6178 29
HET CA C2503 1
HET ACT C4004 4
HET ACT C4007 4
HET HEM D 412 43
HET VDY D6178 29
HET CA D2502 1
HET ACT D4001 4
HET HEM E 412 43
HET VDY E6178 29
HET CA E2504 1
HET ACT E4005 4
HET ACT E4008 4
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM VDY 3-{2-[1-(5-HYDROXY-1,5-DIMETHYL-HEXYL)-7A-METHYL-
HETNAM 2 VDY OCTAHYDRO-INDEN-4-YLIDENE]-ETHYLIDENE}-4-METHYLENE-
HETNAM 3 VDY CYCLOHEXANOL
HETNAM CA CALCIUM ION
HETNAM GOL GLYCEROL
HETNAM ACT ACETATE ION
HETSYN HEM HEME
HETSYN VDY 25-HYDROXYVITAMIN D3
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 6 HEM 5(C34 H32 FE N4 O4)
FORMUL 7 VDY 5(C27 H44 O2)
FORMUL 8 CA 6(CA 2+)
FORMUL 11 GOL 2(C3 H8 O3)
FORMUL 12 ACT 7(C2 H3 O2 1-)
FORMUL 31 HOH *1319(H2 O)
HELIX 1 1 SER A 15 GLN A 20 5 6
HELIX 2 2 PRO A 22 ASP A 33 1 12
HELIX 3 3 ARG A 50 PHE A 58 1 9
HELIX 4 4 ASP A 66 LEU A 71 5 6
HELIX 5 5 PRO A 72 ARG A 76 5 5
HELIX 6 6 MET A 86 MET A 90 5 5
HELIX 7 7 PRO A 93 ARG A 104 1 12
HELIX 8 8 THR A 107 GLU A 113 1 7
HELIX 9 9 LEU A 114 GLY A 128 1 15
HELIX 10 10 LEU A 137 TYR A 141 1 5
HELIX 11 11 PHE A 143 GLY A 155 1 13
HELIX 12 12 PRO A 157 GLU A 159 5 3
HELIX 13 13 ASP A 160 ASP A 173 1 14
HELIX 14 14 PRO A 176 GLU A 201 1 26
HELIX 15 15 ALA A 205 ASP A 217 1 13
HELIX 16 16 SER A 222 THR A 240 1 19
HELIX 17 17 THR A 240 HIS A 255 1 16
HELIX 18 18 HIS A 255 ASP A 265 1 11
HELIX 19 19 LEU A 268 ASP A 280 1 13
HELIX 20 20 GLY A 311 ASN A 316 1 6
HELIX 21 21 HIS A 342 PHE A 346 5 5
HELIX 22 22 GLY A 349 ARG A 368 1 20
HELIX 23 23 GLY A 376 LEU A 380 5 5
HELIX 24 24 SER B 15 TRP B 19 5 5
HELIX 25 25 PRO B 22 ASP B 33 1 12
HELIX 26 26 ARG B 50 PHE B 58 1 9
HELIX 27 27 ASP B 66 LEU B 71 5 6
HELIX 28 28 PRO B 72 ALA B 77 1 6
HELIX 29 29 MET B 86 MET B 90 5 5
HELIX 30 30 PRO B 93 ARG B 104 1 12
HELIX 31 31 THR B 107 GLU B 113 1 7
HELIX 32 32 LEU B 114 LEU B 129 1 16
HELIX 33 33 LEU B 137 TYR B 141 1 5
HELIX 34 34 PHE B 143 GLY B 155 1 13
HELIX 35 35 PRO B 157 GLU B 159 5 3
HELIX 36 36 ASP B 160 ASP B 173 1 14
HELIX 37 37 PRO B 176 GLU B 201 1 26
HELIX 38 38 ALA B 205 ASP B 217 1 13
HELIX 39 39 SER B 222 THR B 240 1 19
HELIX 40 40 THR B 240 HIS B 255 1 16
HELIX 41 41 HIS B 255 ASP B 265 1 11
HELIX 42 42 LEU B 268 ASP B 280 1 13
HELIX 43 43 GLY B 311 ASN B 316 1 6
HELIX 44 44 GLY B 349 ARG B 368 1 20
HELIX 45 45 GLY B 376 LEU B 380 5 5
HELIX 46 46 SER C 15 GLN C 20 5 6
HELIX 47 47 PRO C 22 ASP C 33 1 12
HELIX 48 48 ARG C 50 VAL C 59 1 10
HELIX 49 49 ASP C 66 LEU C 71 5 6
HELIX 50 50 PRO C 72 ARG C 76 5 5
HELIX 51 51 MET C 86 MET C 90 5 5
HELIX 52 52 PRO C 93 ARG C 104 1 12
HELIX 53 53 THR C 107 GLU C 113 1 7
HELIX 54 54 LEU C 114 LEU C 129 1 16
HELIX 55 55 LEU C 137 TYR C 141 1 5
HELIX 56 56 PHE C 143 GLY C 155 1 13
HELIX 57 57 PRO C 157 GLU C 159 5 3
HELIX 58 58 ASP C 160 ASP C 173 1 14
HELIX 59 59 PRO C 176 GLU C 201 1 26
HELIX 60 60 ALA C 205 ASP C 217 1 13
HELIX 61 61 SER C 222 THR C 240 1 19
HELIX 62 62 THR C 240 HIS C 255 1 16
HELIX 63 63 HIS C 255 ASP C 265 1 11
HELIX 64 64 LEU C 268 ASP C 280 1 13
HELIX 65 65 GLY C 311 ASN C 316 1 6
HELIX 66 66 GLY C 349 ARG C 368 1 20
HELIX 67 67 GLY C 376 LEU C 380 5 5
HELIX 68 68 SER D 15 TRP D 19 5 5
HELIX 69 69 PRO D 22 ASP D 33 1 12
HELIX 70 70 ARG D 50 ASP D 60 1 11
HELIX 71 71 ASP D 66 LEU D 71 5 6
HELIX 72 72 PRO D 72 ARG D 76 5 5
HELIX 73 73 MET D 86 MET D 90 5 5
HELIX 74 74 PRO D 93 ARG D 104 1 12
HELIX 75 75 THR D 107 GLU D 113 1 7
HELIX 76 76 LEU D 114 GLY D 128 1 15
HELIX 77 77 LEU D 137 TYR D 141 1 5
HELIX 78 78 PHE D 143 GLY D 155 1 13
HELIX 79 79 PRO D 157 GLU D 159 5 3
HELIX 80 80 ASP D 160 ASP D 173 1 14
HELIX 81 81 PRO D 176 GLU D 201 1 26
HELIX 82 82 ALA D 205 ASP D 217 1 13
HELIX 83 83 SER D 222 THR D 240 1 19
HELIX 84 84 THR D 240 THR D 254 1 15
HELIX 85 85 HIS D 255 ASP D 265 1 11
HELIX 86 86 LEU D 268 ASP D 280 1 13
HELIX 87 87 GLY D 311 ASN D 316 1 6
HELIX 88 88 GLY D 349 ARG D 368 1 20
HELIX 89 89 GLY D 376 LEU D 380 5 5
HELIX 90 90 SER E 15 TRP E 19 5 5
HELIX 91 91 PRO E 22 ASP E 33 1 12
HELIX 92 92 ARG E 50 PHE E 58 1 9
HELIX 93 93 ASP E 66 LEU E 71 5 6
HELIX 94 94 PRO E 72 ARG E 76 5 5
HELIX 95 95 MET E 86 MET E 90 5 5
HELIX 96 96 PRO E 93 ARG E 104 1 12
HELIX 97 97 THR E 107 GLU E 113 1 7
HELIX 98 98 LEU E 114 LEU E 129 1 16
HELIX 99 99 LEU E 137 TYR E 141 1 5
HELIX 100 100 PHE E 143 GLY E 155 1 13
HELIX 101 101 PRO E 157 GLU E 159 5 3
HELIX 102 102 ASP E 160 ASP E 173 1 14
HELIX 103 103 PRO E 176 GLU E 201 1 26
HELIX 104 104 ALA E 205 ASP E 217 1 13
HELIX 105 105 SER E 222 THR E 240 1 19
HELIX 106 106 THR E 240 THR E 254 1 15
HELIX 107 107 HIS E 255 ASP E 265 1 11
HELIX 108 108 LEU E 268 ASP E 280 1 13
HELIX 109 109 GLY E 311 ASN E 316 1 6
HELIX 110 110 GLY E 349 ARG E 368 1 20
HELIX 111 111 GLY E 376 LEU E 380 5 5
SHEET 1 A 2 LEU A 3 THR A 4 0
SHEET 2 A 2 ASP A 12 LEU A 13 -1 O LEU A 13 N LEU A 3
SHEET 1 B 5 VAL A 35 LEU A 40 0
SHEET 2 B 5 GLY A 43 LEU A 48 -1 O VAL A 45 N LEU A 38
SHEET 3 B 5 MET A 307 LEU A 310 1 O MET A 309 N TRP A 46
SHEET 4 B 5 ARG A 289 THR A 291 -1 N ARG A 289 O VAL A 308
SHEET 5 B 5 LEU A 63 SER A 64 -1 N SER A 64 O PHE A 290
SHEET 1 C 3 VAL A 135 ASP A 136 0
SHEET 2 C 3 PRO A 395 THR A 397 -1 O VAL A 396 N VAL A 135
SHEET 3 C 3 ALA A 372 LEU A 373 -1 N ALA A 372 O THR A 397
SHEET 1 D 2 VAL A 295 TYR A 297 0
SHEET 2 D 2 VAL A 300 ILE A 302 -1 O ILE A 302 N VAL A 295
SHEET 1 E 2 LEU B 3 THR B 4 0
SHEET 2 E 2 ASP B 12 LEU B 13 -1 O LEU B 13 N LEU B 3
SHEET 1 F 5 VAL B 35 LEU B 38 0
SHEET 2 F 5 VAL B 45 LEU B 48 -1 O VAL B 45 N LEU B 38
SHEET 3 F 5 MET B 307 LEU B 310 1 O MET B 309 N TRP B 46
SHEET 4 F 5 ARG B 289 THR B 291 -1 N ARG B 289 O VAL B 308
SHEET 5 F 5 LEU B 63 SER B 64 -1 N SER B 64 O PHE B 290
SHEET 1 G 3 PRO B 134 ASP B 136 0
SHEET 2 G 3 PRO B 395 THR B 397 -1 O VAL B 396 N VAL B 135
SHEET 3 G 3 ALA B 372 LEU B 373 -1 N ALA B 372 O THR B 397
SHEET 1 H 2 VAL B 295 TYR B 297 0
SHEET 2 H 2 VAL B 300 ILE B 302 -1 O ILE B 302 N VAL B 295
SHEET 1 I 2 LEU C 3 THR C 4 0
SHEET 2 I 2 ASP C 12 LEU C 13 -1 O LEU C 13 N LEU C 3
SHEET 1 J 5 VAL C 35 LEU C 40 0
SHEET 2 J 5 GLY C 43 LEU C 48 -1 O VAL C 45 N LEU C 38
SHEET 3 J 5 MET C 307 LEU C 310 1 O MET C 309 N TRP C 46
SHEET 4 J 5 ARG C 289 THR C 291 -1 N ARG C 289 O VAL C 308
SHEET 5 J 5 LEU C 63 SER C 64 -1 N SER C 64 O PHE C 290
SHEET 1 K 3 PRO C 134 ASP C 136 0
SHEET 2 K 3 PRO C 395 THR C 397 -1 O VAL C 396 N VAL C 135
SHEET 3 K 3 ALA C 372 LEU C 373 -1 N ALA C 372 O THR C 397
SHEET 1 L 2 VAL C 295 TYR C 297 0
SHEET 2 L 2 VAL C 300 ILE C 302 -1 O VAL C 300 N TYR C 297
SHEET 1 M 2 LEU D 3 THR D 4 0
SHEET 2 M 2 ASP D 12 LEU D 13 -1 O LEU D 13 N LEU D 3
SHEET 1 N 5 VAL D 35 LEU D 40 0
SHEET 2 N 5 GLY D 43 LEU D 48 -1 O VAL D 45 N LEU D 38
SHEET 3 N 5 MET D 307 LEU D 310 1 O MET D 309 N TRP D 46
SHEET 4 N 5 ARG D 289 THR D 291 -1 N ARG D 289 O VAL D 308
SHEET 5 N 5 LEU D 63 SER D 64 -1 N SER D 64 O PHE D 290
SHEET 1 O 3 VAL D 135 ASP D 136 0
SHEET 2 O 3 PRO D 395 THR D 397 -1 O VAL D 396 N VAL D 135
SHEET 3 O 3 ALA D 372 LEU D 373 -1 N ALA D 372 O THR D 397
SHEET 1 P 2 VAL D 295 TYR D 297 0
SHEET 2 P 2 VAL D 300 ILE D 302 -1 O ILE D 302 N VAL D 295
SHEET 1 Q 2 LEU E 3 THR E 4 0
SHEET 2 Q 2 ASP E 12 LEU E 13 -1 O LEU E 13 N LEU E 3
SHEET 1 R 5 VAL E 35 LEU E 38 0
SHEET 2 R 5 VAL E 45 LEU E 48 -1 O LEU E 47 N ARG E 36
SHEET 3 R 5 MET E 307 LEU E 310 1 O MET E 309 N TRP E 46
SHEET 4 R 5 ARG E 289 THR E 291 -1 N ARG E 289 O VAL E 308
SHEET 5 R 5 LEU E 63 SER E 64 -1 N SER E 64 O PHE E 290
SHEET 1 S 3 VAL E 135 ASP E 136 0
SHEET 2 S 3 PRO E 395 THR E 397 -1 O VAL E 396 N VAL E 135
SHEET 3 S 3 ALA E 372 LEU E 373 -1 N ALA E 372 O THR E 397
SHEET 1 T 2 VAL E 295 TYR E 297 0
SHEET 2 T 2 VAL E 300 ILE E 302 -1 O ILE E 302 N VAL E 295
LINK O GLY A 128 CA CA A2505 1555 1555 2.25
LINK OD1 ASP A 204 CA CA A2501 1555 1555 2.47
LINK O ASP A 320 CA CA A2506 1555 1555 2.61
LINK SG CYS A 347 FE HEM A 412 1555 1555 2.27
LINK FE HEM A 412 O1 VDY A6178 1555 1555 2.41
LINK O HOH A 528 CA CA A2501 1555 1555 2.64
LINK O HOH A 579 CA CA A2501 1555 1555 2.64
LINK O HOH A 593 CA CA A2505 1555 1555 2.38
LINK O HOH A 905 CA CA A2505 1555 1555 2.56
LINK O HOH A 926 CA CA A2501 1555 1555 2.51
LINK O HOH A 929 CA CA A2505 1555 1555 2.48
LINK CA CA A2501 O3 GOL A3002 1555 1555 2.47
LINK CA CA A2501 O2 GOL A3002 1555 1555 2.44
LINK CA CA A2506 O ASP D 320 1555 1555 2.96
LINK CA CA A2506 O HOH D 933 1555 1555 2.33
LINK SG CYS B 347 FE HEM B 412 1555 1555 2.14
LINK FE HEM B 412 O1 VDY B6178 1555 1555 2.42
LINK OD1 ASP C 204 CA CA C2503 1555 1555 2.43
LINK SG CYS C 347 FE HEM C 412 1555 1555 2.39
LINK FE HEM C 412 O1 VDY C6178 1555 1555 2.69
LINK O HOH C 482 CA CA C2503 1555 1555 2.51
LINK O HOH C 703 CA CA C2503 1555 1555 2.59
LINK CA CA C2503 OXT ACT C4004 1555 1555 2.75
LINK CA CA C2503 O ACT C4004 1555 1555 2.55
LINK OD1 ASP D 204 CA CA D2502 1555 1555 2.35
LINK SG CYS D 347 FE HEM D 412 1555 1555 2.37
LINK FE HEM D 412 O1 VDY D6178 1555 1555 2.58
LINK O HOH D 601 CA CA D2502 1555 1555 2.54
LINK OD1 ASP E 204 CA CA E2504 1555 1555 2.78
LINK SG CYS E 347 FE HEM E 412 1555 1555 2.39
LINK FE HEM E 412 O1 VDY E6178 1555 1555 2.43
LINK O HOH E 565 CA CA E2504 1555 1555 2.41
LINK O HOH E 576 CA CA E2504 1555 1555 2.37
LINK O HOH E 652 CA CA E2504 1555 1555 2.53
LINK CA CA E2504 O ACT E4005 1555 1555 2.88
LINK CA CA E2504 OXT ACT E4005 1555 1555 2.92
CISPEP 1 PRO A 92 PRO A 93 0 -1.14
CISPEP 2 PRO B 92 PRO B 93 0 9.76
CISPEP 3 PRO C 92 PRO C 93 0 0.14
CISPEP 4 PRO D 92 PRO D 93 0 2.22
CISPEP 5 PRO E 92 PRO E 93 0 1.79
SITE 1 AC1 25 PHE A 58 LYS A 65 ILE A 88 HIS A 95
SITE 2 AC1 25 ARG A 99 PHE A 106 LEU A 232 LEU A 233
SITE 3 AC1 25 ALA A 236 THR A 240 THR A 241 VAL A 283
SITE 4 AC1 25 PRO A 287 ARG A 289 LEU A 312 PHE A 339
SITE 5 AC1 25 PHE A 340 GLY A 341 ILE A 344 HIS A 345
SITE 6 AC1 25 CYS A 347 GLY A 349 ALA A 353 HOH A 421
SITE 7 AC1 25 VDY A6178
SITE 1 AC2 8 LYS A 180 ASN A 181 LEU A 232 ILE A 235
SITE 2 AC2 8 THR A 240 VAL A 283 PRO A 287 HEM A 412
SITE 1 AC3 6 ASP A 204 HOH A 528 HOH A 579 HOH A 926
SITE 2 AC3 6 GOL A3002 HOH E 469
SITE 1 AC4 6 GLY A 128 HOH A 593 HOH A 905 HOH A 929
SITE 2 AC4 6 HOH B 415 HOH B 467
SITE 1 AC5 3 ASP A 320 ASP D 320 HOH D 933
SITE 1 AC6 8 ASP A 53 GLU A 56 HOH A 474 HOH A 600
SITE 2 AC6 8 HOH A 922 HOH A1250 ARG D 55 HOH D 490
SITE 1 AC7 6 HIS A 342 GLY A 343 PHE A 346 HOH A 576
SITE 2 AC7 6 HOH A1012 HOH D 483
SITE 1 AC8 9 ASP A 204 HOH A 506 HOH A 579 HOH A 926
SITE 2 AC8 9 CA A2501 ARG E 70 PRO E 72 ALA E 304
SITE 3 AC8 9 HOH E 847
SITE 1 AC9 25 PHE B 58 LYS B 65 ILE B 88 HIS B 95
SITE 2 AC9 25 ARG B 99 PHE B 106 LEU B 233 ALA B 236
SITE 3 AC9 25 THR B 240 THR B 241 VAL B 283 ALA B 286
SITE 4 AC9 25 PRO B 287 ARG B 289 LEU B 312 PHE B 339
SITE 5 AC9 25 PHE B 340 GLY B 341 ILE B 344 HIS B 345
SITE 6 AC9 25 CYS B 347 GLY B 349 ALA B 353 HOH B 442
SITE 7 AC9 25 VDY B6178
SITE 1 BC1 9 PRO B 83 MET B 86 LYS B 180 ASN B 181
SITE 2 BC1 9 ILE B 235 THR B 240 VAL B 283 LEU B 387
SITE 3 BC1 9 HEM B 412
SITE 1 BC2 5 ASN B 21 ASP B 280 ARG B 317 ARG B 389
SITE 2 BC2 5 HOH B 662
SITE 1 BC3 25 PHE C 58 LYS C 65 MET C 87 ILE C 88
SITE 2 BC3 25 HIS C 95 ARG C 99 PHE C 106 ALA C 236
SITE 3 BC3 25 THR C 240 THR C 241 ALA C 286 PRO C 287
SITE 4 BC3 25 ARG C 289 LEU C 312 PHE C 339 PHE C 340
SITE 5 BC3 25 GLY C 341 ILE C 344 HIS C 345 CYS C 347
SITE 6 BC3 25 LEU C 348 GLY C 349 ALA C 353 HOH C 418
SITE 7 BC3 25 VDY C6178
SITE 1 BC4 7 LYS C 180 ASN C 181 ILE C 235 THR C 240
SITE 2 BC4 7 VAL C 283 PRO C 287 HEM C 412
SITE 1 BC5 6 HOH A 505 HOH A 553 ASP C 204 HOH C 482
SITE 2 BC5 6 HOH C 703 ACT C4004
SITE 1 BC6 5 ARG A 70 HOH A 553 ASP C 204 HOH C 725
SITE 2 BC6 5 CA C2503
SITE 1 BC7 3 HIS C 342 GLY C 343 HOH C1305
SITE 1 BC8 26 PHE D 58 LYS D 65 MET D 87 ILE D 88
SITE 2 BC8 26 HIS D 95 ARG D 99 PHE D 106 LEU D 232
SITE 3 BC8 26 ALA D 236 THR D 240 THR D 241 VAL D 283
SITE 4 BC8 26 PRO D 287 ARG D 289 LEU D 312 PHE D 339
SITE 5 BC8 26 PHE D 340 GLY D 341 ILE D 344 HIS D 345
SITE 6 BC8 26 CYS D 347 LEU D 348 GLY D 349 ALA D 353
SITE 7 BC8 26 HOH D 416 VDY D6178
SITE 1 BC9 9 LYS D 180 ASN D 181 MET D 184 ILE D 235
SITE 2 BC9 9 THR D 240 VAL D 283 PRO D 287 LEU D 387
SITE 3 BC9 9 HEM D 412
SITE 1 CC1 4 HOH B1159 HOH B1160 ASP D 204 HOH D 601
SITE 1 CC2 5 HIS D 342 GLY D 343 PHE D 346 HOH D 443
SITE 2 CC2 5 HOH D 459
SITE 1 CC3 25 PHE E 58 LYS E 65 MET E 87 ILE E 88
SITE 2 CC3 25 HIS E 95 ARG E 99 PHE E 106 ALA E 236
SITE 3 CC3 25 THR E 240 THR E 241 VAL E 283 ALA E 286
SITE 4 CC3 25 PRO E 287 ARG E 289 LEU E 312 PHE E 339
SITE 5 CC3 25 PHE E 340 GLY E 341 ILE E 344 HIS E 345
SITE 6 CC3 25 CYS E 347 GLY E 349 ALA E 353 HOH E 449
SITE 7 CC3 25 VDY E6178
SITE 1 CC4 9 MET E 86 LYS E 180 ASN E 181 LEU E 232
SITE 2 CC4 9 ILE E 235 THR E 240 VAL E 283 PRO E 287
SITE 3 CC4 9 HEM E 412
SITE 1 CC5 5 ASP E 204 HOH E 565 HOH E 576 HOH E 652
SITE 2 CC5 5 ACT E4005
SITE 1 CC6 4 ARG C 70 ASP E 204 HOH E 448 CA E2504
SITE 1 CC7 3 HIS E 342 GLY E 343 PHE E 346
CRYST1 77.173 171.800 189.143 90.00 90.00 90.00 P 21 21 21 20
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 0.012958 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005821 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005287 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
