HEADER OXIDOREDUCTASE 04-MAR-11 3QZ1
TITLE CRYSTAL STRUCTURE OF BOVINE STEROID OF 21-HYDROXYLASE (P450C21)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: STEROID 21-HYDROXYLASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: 21-OHASE, CYTOCHROME P-450C21, CYTOCHROME P450 21,
COMPND 5 CYTOCHROME P450 XXI, CYTOCHROME P450-C21;
COMPND 6 EC: 1.14.99.10;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: BOVINE,COW,DOMESTIC CATTLE,DOMESTIC COW;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 GENE: CYP21, CYP21A1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 668369;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: DH5[ALPHA];
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PCWORI
KEYWDS P450 MONOOXYGENASE, 21-HYDROXYLASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.ZHAO,M.R.WATERMAN
REVDAT 3 21-FEB-24 3QZ1 1 REMARK SEQADV
REVDAT 2 08-NOV-17 3QZ1 1 REMARK
REVDAT 1 18-JAN-12 3QZ1 0
JRNL AUTH B.ZHAO,L.LEI,M.SUNDARAMOORTHY,N.KAGAWA,M.R.WATERMAN
JRNL TITL CRYSTAL STRUCTURE OF BOVINE STEROID OF 21-HYDROXYLASE
JRNL TITL 2 (P450C21)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1541.0
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 92.4
REMARK 3 NUMBER OF REFLECTIONS : 46235
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.282
REMARK 3 FREE R VALUE : 0.297
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.300
REMARK 3 FREE R VALUE TEST SET COUNT : 4666
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.11
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 81.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3697
REMARK 3 BIN R VALUE (WORKING SET) : 0.4024
REMARK 3 BIN FREE R VALUE : 0.4702
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 370
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 14064
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 364
REMARK 3 SOLVENT ATOMS : 97
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 119.1
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.35200
REMARK 3 B22 (A**2) : -0.51400
REMARK 3 B33 (A**2) : 0.16200
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.00800
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.54
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.508
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 139.6
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3QZ1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-MAR-11.
REMARK 100 THE DEPOSITION ID IS D_1000064282.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-FEB-11; 10-NOV-10
REMARK 200 TEMPERATURE (KELVIN) : 100; 100
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : APS; APS
REMARK 200 BEAMLINE : 21-ID-G; 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97; 1.5
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL; GRAPHITE
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE; IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 300 MM PLATE; MAR
REMARK 200 SCANNER 300 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47687
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.09200
REMARK 200 R SYM (I) : 0.06500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.53900
REMARK 200 R SYM FOR SHELL (I) : 0.67200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.210
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, TACSIMATE, PH 7.4, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 295K
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 83.99900
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, 4
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 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 VAL A 2
REMARK 465 LEU A 3
REMARK 465 ALA A 4
REMARK 465 GLY A 5
REMARK 465 LEU A 6
REMARK 465 LEU A 7
REMARK 465 LEU A 8
REMARK 465 LEU A 9
REMARK 465 LEU A 10
REMARK 465 THR A 11
REMARK 465 LEU A 12
REMARK 465 LEU A 13
REMARK 465 ALA A 14
REMARK 465 GLY A 15
REMARK 465 ALA A 16
REMARK 465 HIS A 17
REMARK 465 LEU A 18
REMARK 465 LEU A 19
REMARK 465 TRP A 20
REMARK 465 GLY A 21
REMARK 465 ARG A 22
REMARK 465 TRP A 23
REMARK 465 LYS A 24
REMARK 465 LEU A 25
REMARK 465 ARG A 26
REMARK 465 ASN A 27
REMARK 465 LEU A 28
REMARK 465 GLY A 131
REMARK 465 THR A 132
REMARK 465 GLU A 269
REMARK 465 GLU A 270
REMARK 465 GLY A 271
REMARK 465 PRO A 272
REMARK 465 GLY A 273
REMARK 465 GLU A 410
REMARK 465 PRO A 411
REMARK 465 GLY A 412
REMARK 465 GLY A 484
REMARK 465 VAL A 485
REMARK 465 GLU A 486
REMARK 465 ALA A 487
REMARK 465 GLY A 488
REMARK 465 ALA A 489
REMARK 465 TRP A 490
REMARK 465 GLU A 491
REMARK 465 SER A 492
REMARK 465 ALA A 493
REMARK 465 SER A 494
REMARK 465 ALA A 495
REMARK 465 GLN A 496
REMARK 465 MET B 1
REMARK 465 VAL B 2
REMARK 465 LEU B 3
REMARK 465 ALA B 4
REMARK 465 GLY B 5
REMARK 465 LEU B 6
REMARK 465 LEU B 7
REMARK 465 LEU B 8
REMARK 465 LEU B 9
REMARK 465 LEU B 10
REMARK 465 THR B 11
REMARK 465 LEU B 12
REMARK 465 LEU B 13
REMARK 465 ALA B 14
REMARK 465 GLY B 15
REMARK 465 ALA B 16
REMARK 465 HIS B 17
REMARK 465 LEU B 18
REMARK 465 LEU B 19
REMARK 465 TRP B 20
REMARK 465 GLY B 21
REMARK 465 ARG B 22
REMARK 465 TRP B 23
REMARK 465 LYS B 24
REMARK 465 LEU B 25
REMARK 465 ARG B 26
REMARK 465 ASN B 27
REMARK 465 LEU B 28
REMARK 465 GLY B 131
REMARK 465 THR B 132
REMARK 465 ARG B 133
REMARK 465 SER B 134
REMARK 465 GLY B 264
REMARK 465 ARG B 265
REMARK 465 GLN B 266
REMARK 465 ARG B 267
REMARK 465 VAL B 268
REMARK 465 GLU B 269
REMARK 465 GLU B 270
REMARK 465 GLY B 271
REMARK 465 PRO B 272
REMARK 465 GLY B 273
REMARK 465 GLY B 327
REMARK 465 ALA B 328
REMARK 465 SER B 329
REMARK 465 CYS B 330
REMARK 465 SER B 331
REMARK 465 GLY B 484
REMARK 465 VAL B 485
REMARK 465 GLU B 486
REMARK 465 ALA B 487
REMARK 465 GLY B 488
REMARK 465 ALA B 489
REMARK 465 TRP B 490
REMARK 465 GLU B 491
REMARK 465 SER B 492
REMARK 465 ALA B 493
REMARK 465 SER B 494
REMARK 465 ALA B 495
REMARK 465 GLN B 496
REMARK 465 MET C 1
REMARK 465 VAL C 2
REMARK 465 LEU C 3
REMARK 465 ALA C 4
REMARK 465 GLY C 5
REMARK 465 LEU C 6
REMARK 465 LEU C 7
REMARK 465 LEU C 8
REMARK 465 LEU C 9
REMARK 465 LEU C 10
REMARK 465 THR C 11
REMARK 465 LEU C 12
REMARK 465 LEU C 13
REMARK 465 ALA C 14
REMARK 465 GLY C 15
REMARK 465 ALA C 16
REMARK 465 HIS C 17
REMARK 465 LEU C 18
REMARK 465 LEU C 19
REMARK 465 TRP C 20
REMARK 465 GLY C 21
REMARK 465 ARG C 22
REMARK 465 TRP C 23
REMARK 465 LYS C 24
REMARK 465 LEU C 25
REMARK 465 ARG C 26
REMARK 465 ASN C 27
REMARK 465 LEU C 28
REMARK 465 GLY C 131
REMARK 465 THR C 132
REMARK 465 GLY C 264
REMARK 465 ARG C 265
REMARK 465 GLN C 266
REMARK 465 ARG C 267
REMARK 465 VAL C 268
REMARK 465 GLU C 269
REMARK 465 GLU C 270
REMARK 465 GLY C 271
REMARK 465 PRO C 272
REMARK 465 GLY C 273
REMARK 465 GLY C 327
REMARK 465 ALA C 328
REMARK 465 SER C 329
REMARK 465 CYS C 330
REMARK 465 SER C 331
REMARK 465 ARG C 483
REMARK 465 GLY C 484
REMARK 465 VAL C 485
REMARK 465 GLU C 486
REMARK 465 ALA C 487
REMARK 465 GLY C 488
REMARK 465 ALA C 489
REMARK 465 TRP C 490
REMARK 465 GLU C 491
REMARK 465 SER C 492
REMARK 465 ALA C 493
REMARK 465 SER C 494
REMARK 465 ALA C 495
REMARK 465 GLN C 496
REMARK 465 MET D 1
REMARK 465 VAL D 2
REMARK 465 LEU D 3
REMARK 465 ALA D 4
REMARK 465 GLY D 5
REMARK 465 LEU D 6
REMARK 465 LEU D 7
REMARK 465 LEU D 8
REMARK 465 LEU D 9
REMARK 465 LEU D 10
REMARK 465 THR D 11
REMARK 465 LEU D 12
REMARK 465 LEU D 13
REMARK 465 ALA D 14
REMARK 465 GLY D 15
REMARK 465 ALA D 16
REMARK 465 HIS D 17
REMARK 465 LEU D 18
REMARK 465 LEU D 19
REMARK 465 TRP D 20
REMARK 465 GLY D 21
REMARK 465 ARG D 22
REMARK 465 TRP D 23
REMARK 465 LYS D 24
REMARK 465 LEU D 25
REMARK 465 ARG D 26
REMARK 465 ASN D 27
REMARK 465 LEU D 28
REMARK 465 GLY D 131
REMARK 465 THR D 132
REMARK 465 ARG D 133
REMARK 465 GLY D 264
REMARK 465 ARG D 265
REMARK 465 GLN D 266
REMARK 465 ARG D 267
REMARK 465 VAL D 268
REMARK 465 GLU D 269
REMARK 465 GLU D 270
REMARK 465 GLY D 271
REMARK 465 PRO D 272
REMARK 465 GLY D 273
REMARK 465 GLY D 327
REMARK 465 ALA D 328
REMARK 465 SER D 329
REMARK 465 CYS D 330
REMARK 465 SER D 331
REMARK 465 ARG D 332
REMARK 465 PRO D 482
REMARK 465 ARG D 483
REMARK 465 GLY D 484
REMARK 465 VAL D 485
REMARK 465 GLU D 486
REMARK 465 ALA D 487
REMARK 465 GLY D 488
REMARK 465 ALA D 489
REMARK 465 TRP D 490
REMARK 465 GLU D 491
REMARK 465 SER D 492
REMARK 465 ALA D 493
REMARK 465 SER D 494
REMARK 465 ALA D 495
REMARK 465 GLN D 496
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 HIS A 29 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 238 NZ
REMARK 470 HIS B 29 CG ND1 CD2 CE1 NE2
REMARK 470 HIS C 29 CG ND1 CD2 CE1 NE2
REMARK 470 ARG C 332 CG CD NE CZ NH1 NH2
REMARK 470 PRO C 411 CG CD
REMARK 470 HIS D 29 CG ND1 CD2 CE1 NE2
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 O GLY C 412 O HOH C 604 1.63
REMARK 500 ND2 ASN A 219 O HOH A 621 1.71
REMARK 500 OE2 GLU D 430 O HOH D 617 1.72
REMARK 500 N GLY C 179 OD1 ASP C 254 1.73
REMARK 500 NH2 ARG B 63 O HOH B 617 1.77
REMARK 500 O GLY D 111 NH2 ARG D 425 1.78
REMARK 500 O VAL B 284 CB PHE B 288 1.79
REMARK 500 OD1 ASN B 219 O HOH B 626 1.83
REMARK 500 O PRO A 463 CE1 TYR A 466 1.86
REMARK 500 NH1 ARG B 92 O PRO B 363 1.89
REMARK 500 OG SER A 102 O HOH A 610 1.89
REMARK 500 CG GLN A 42 O HOH A 613 1.89
REMARK 500 O ARG C 425 O HOH C 606 1.92
REMARK 500 O GLN A 446 NE2 GLN A 481 1.94
REMARK 500 OE1 GLN A 42 O HOH A 613 1.94
REMARK 500 O CYS D 105 O HOH D 604 1.96
REMARK 500 CG2 THR A 294 CAA 3QZ A 501 1.96
REMARK 500 O SER A 283 CD1 LEU A 287 1.96
REMARK 500 CG PRO D 463 CB LEU D 471 1.96
REMARK 500 OD2 ASP B 112 NH2 ARG B 365 1.97
REMARK 500 O GLY B 91 N ARG B 365 1.98
REMARK 500 ND2 ASN B 219 O HOH B 616 1.99
REMARK 500 CB PRO D 463 CG LEU D 471 1.99
REMARK 500 O SER A 246 NE1 TRP A 252 1.99
REMARK 500 CE1 PHE D 165 OE2 GLU D 293 1.99
REMARK 500 N GLN A 103 O HOH A 610 2.00
REMARK 500 O VAL B 284 N PHE B 288 2.01
REMARK 500 O GLN A 103 O HOH A 610 2.02
REMARK 500 CB CYS D 105 O HOH D 613 2.03
REMARK 500 CD2 LEU D 168 O THR D 292 2.04
REMARK 500 O PRO C 212 CE2 PHE C 216 2.04
REMARK 500 NH1 ARG D 232 OAE 3QZ D 501 2.06
REMARK 500 O SER A 171 CE1 TYR A 175 2.07
REMARK 500 OG1 THR C 449 O LEU C 480 2.08
REMARK 500 O ASP A 337 N ALA A 339 2.08
REMARK 500 OG SER B 74 OG1 THR B 77 2.08
REMARK 500 O ASP A 337 N ARG A 340 2.08
REMARK 500 CB GLN D 106 CE1 HIS D 279 2.11
REMARK 500 O THR B 169 CG1 ILE B 173 2.11
REMARK 500 OE1 GLN D 94 CE LYS D 99 2.12
REMARK 500 CB PRO A 475 NE2 GLN A 477 2.14
REMARK 500 CD GLN A 42 O HOH A 613 2.14
REMARK 500 O GLU D 164 CD1 LEU D 168 2.14
REMARK 500 CB GLN D 106 NE2 HIS D 279 2.15
REMARK 500 O PRO A 463 CD1 TYR A 466 2.16
REMARK 500 CE2 PHE B 189 CZ PHE B 288 2.16
REMARK 500 CG GLN D 106 NE2 HIS D 279 2.16
REMARK 500 CG2 THR B 294 CAA 3QZ B 501 2.17
REMARK 500 CE2 PHE B 178 CZ3 TRP B 252 2.18
REMARK 500 O SER D 370 O HOH D 606 2.18
REMARK 500
REMARK 500 THIS ENTRY HAS 52 CLOSE CONTACTS
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NH2 ARG B 404 O HOH A 618 2556 1.67
REMARK 500 NE2 HIS A 39 O PRO D 35 1556 2.07
REMARK 500 N LEU D 38 O HOH A 601 1554 2.13
REMARK 500 O PRO B 35 O PRO C 35 1556 2.14
REMARK 500 N LEU B 38 O HOH C 601 1556 2.14
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 PRO D 463 CA PRO D 463 CB -0.136
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 PRO A 359 C - N - CD ANGL. DEV. = -13.1 DEGREES
REMARK 500 CYS A 422 N - CA - C ANGL. DEV. = -19.1 DEGREES
REMARK 500 PRO B 43 C - N - CD ANGL. DEV. = -14.9 DEGREES
REMARK 500 PHE B 217 N - CA - C ANGL. DEV. = -17.4 DEGREES
REMARK 500 PRO B 218 C - N - CD ANGL. DEV. = -16.3 DEGREES
REMARK 500 TYR B 335 N - CA - C ANGL. DEV. = 18.3 DEGREES
REMARK 500 PRO B 359 C - N - CD ANGL. DEV. = -13.9 DEGREES
REMARK 500 PRO B 411 C - N - CD ANGL. DEV. = -14.6 DEGREES
REMARK 500 ARG B 425 N - CA - C ANGL. DEV. = -16.2 DEGREES
REMARK 500 ARG B 479 N - CA - C ANGL. DEV. = 20.3 DEGREES
REMARK 500 SER C 114 N - CA - C ANGL. DEV. = -17.6 DEGREES
REMARK 500 PRO C 411 N - CA - CB ANGL. DEV. = 7.2 DEGREES
REMARK 500 ARG C 479 N - CA - C ANGL. DEV. = 28.8 DEGREES
REMARK 500 SER D 114 N - CA - C ANGL. DEV. = -16.9 DEGREES
REMARK 500 ARG D 425 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 LEU D 471 CA - CB - CG ANGL. DEV. = 16.2 DEGREES
REMARK 500 ARG D 479 N - CA - C ANGL. DEV. = 21.0 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 GLN A 42 140.08 99.03
REMARK 500 ILE A 78 -7.23 -59.90
REMARK 500 TRP A 86 -57.01 62.57
REMARK 500 PRO A 96 2.06 -64.25
REMARK 500 GLN A 103 -124.14 57.09
REMARK 500 CYS A 105 156.37 102.97
REMARK 500 GLN A 106 155.84 90.50
REMARK 500 ASP A 107 179.72 146.79
REMARK 500 SER A 109 -91.79 78.40
REMARK 500 SER A 114 153.43 138.94
REMARK 500 LEU A 176 -31.49 -149.26
REMARK 500 PHE A 178 3.69 57.01
REMARK 500 LYS A 181 -25.08 63.58
REMARK 500 ASP A 201 68.88 -107.95
REMARK 500 VAL A 211 79.91 -116.84
REMARK 500 PHE A 213 3.20 -67.46
REMARK 500 ARG A 215 0.60 88.96
REMARK 500 TRP A 252 -165.13 -78.41
REMARK 500 LEU A 324 8.49 -163.64
REMARK 500 PRO A 326 -19.25 -49.70
REMARK 500 ARG A 332 -130.04 52.52
REMARK 500 TYR A 335 -88.78 7.67
REMARK 500 ARG A 338 -24.39 -22.12
REMARK 500 ALA A 361 -131.85 47.93
REMARK 500 PHE A 373 147.16 101.57
REMARK 500 VAL A 396 -27.00 -143.79
REMARK 500 ARG A 407 -28.60 -168.69
REMARK 500 VAL A 426 -95.08 26.86
REMARK 500 LEU A 450 80.67 78.66
REMARK 500 SER A 460 172.61 144.16
REMARK 500 LEU A 461 -18.78 104.12
REMARK 500 GLN A 462 126.42 92.84
REMARK 500 CYS A 467 -146.67 -119.56
REMARK 500 GLN B 42 155.68 104.85
REMARK 500 ASN B 44 54.87 72.20
REMARK 500 LEU B 56 -50.72 -126.49
REMARK 500 LEU B 66 -26.29 -143.90
REMARK 500 ILE B 78 -6.67 -59.38
REMARK 500 TRP B 86 -64.78 60.44
REMARK 500 PRO B 96 1.13 -63.75
REMARK 500 GLN B 103 -61.09 69.91
REMARK 500 CYS B 105 -178.20 80.50
REMARK 500 GLN B 106 -130.16 55.73
REMARK 500 ASP B 107 174.26 67.83
REMARK 500 SER B 109 -55.73 75.48
REMARK 500 SER B 114 163.39 148.43
REMARK 500 ALA B 155 -1.47 61.21
REMARK 500 LYS B 181 -8.19 69.36
REMARK 500 ASP B 183 -9.12 -59.29
REMARK 500 ASP B 201 69.27 -108.43
REMARK 500
REMARK 500 THIS ENTRY HAS 142 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG D 425 0.11 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 THE LIGAND 3QZ IN THE STRUCTURE IS 17-HYDROXYPROGESTERONE, WHICH IS
REMARK 600 VERY HYDROPHOBIC AND ITS SOLUBILITY IS POOR. THE AUTHORS COULD NOT
REMARK 600 ADD MORE LIGAND DURING CRYSTALLIZATION DUE TO THE POOR SOLUBILITY.
REMARK 600 THIS IS PROBABLY WHY THE LIGANDS (ESPECIALLY B502) SHOWED
REMARK 600 RELATIVELY HIGH REAL SPACE R VALUES. THE DISORDER IS ALSO ONE OF
REMARK 600 THE REASON TO BE CONSIDERED. THERE ARE FOUR MOLECULES IN ASYMMETRIC
REMARK 600 UNIT. THREE OF FOUR MOLECULES A, C, AND D CLEARLY SHOWED TWO
REMARK 600 MOLECULES IN THE ENZYME. MOLECULE B SHOWED TWO MOLECULES AS WELL
REMARK 600 EVEN THOUGH B502 IS MORE DISORDERED SOMEHOW. IN ADDITION, THE
REMARK 600 BIOCHEMICAL TITRATION DATA PROVIDE ADDITIONAL EVIDENCE TO SUPPORT
REMARK 600 TWO LIGANDS BOUND IN THE ENZYME AT SAME TIME
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 500 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 427 SG
REMARK 620 2 HEM A 500 NA 82.6
REMARK 620 3 HEM A 500 NB 97.9 91.1
REMARK 620 4 HEM A 500 NC 98.3 179.1 88.4
REMARK 620 5 HEM A 500 ND 83.7 90.7 177.7 89.7
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 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3QZ A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3QZ A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3QZ B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3QZ B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3QZ C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3QZ C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3QZ D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3QZ D 502
DBREF 3QZ1 A 1 496 UNP P00191 CP21A_BOVIN 1 496
DBREF 3QZ1 B 1 496 UNP P00191 CP21A_BOVIN 1 496
DBREF 3QZ1 C 1 496 UNP P00191 CP21A_BOVIN 1 496
DBREF 3QZ1 D 1 496 UNP P00191 CP21A_BOVIN 1 496
SEQADV 3QZ1 ARG A 241 UNP P00191 THR 241 ENGINEERED MUTATION
SEQADV 3QZ1 ALA A 442 UNP P00191 LEU 442 ENGINEERED MUTATION
SEQADV 3QZ1 ARG B 241 UNP P00191 THR 241 ENGINEERED MUTATION
SEQADV 3QZ1 ALA B 442 UNP P00191 LEU 442 ENGINEERED MUTATION
SEQADV 3QZ1 ARG C 241 UNP P00191 THR 241 ENGINEERED MUTATION
SEQADV 3QZ1 ALA C 442 UNP P00191 LEU 442 ENGINEERED MUTATION
SEQADV 3QZ1 ARG D 241 UNP P00191 THR 241 ENGINEERED MUTATION
SEQADV 3QZ1 ALA D 442 UNP P00191 LEU 442 ENGINEERED MUTATION
SEQRES 1 A 496 MET VAL LEU ALA GLY LEU LEU LEU LEU LEU THR LEU LEU
SEQRES 2 A 496 ALA GLY ALA HIS LEU LEU TRP GLY ARG TRP LYS LEU ARG
SEQRES 3 A 496 ASN LEU HIS LEU PRO PRO LEU VAL PRO GLY PHE LEU HIS
SEQRES 4 A 496 LEU LEU GLN PRO ASN LEU PRO ILE HIS LEU LEU SER LEU
SEQRES 5 A 496 THR GLN LYS LEU GLY PRO VAL TYR ARG LEU ARG LEU GLY
SEQRES 6 A 496 LEU GLN GLU VAL VAL VAL LEU ASN SER LYS ARG THR ILE
SEQRES 7 A 496 GLU GLU ALA MET ILE ARG LYS TRP VAL ASP PHE ALA GLY
SEQRES 8 A 496 ARG PRO GLN ILE PRO SER TYR LYS LEU VAL SER GLN ARG
SEQRES 9 A 496 CYS GLN ASP ILE SER LEU GLY ASP TYR SER LEU LEU TRP
SEQRES 10 A 496 LYS ALA HIS LYS LYS LEU THR ARG SER ALA LEU LEU LEU
SEQRES 11 A 496 GLY THR ARG SER SER MET GLU PRO TRP VAL ASP GLN LEU
SEQRES 12 A 496 THR GLN GLU PHE CYS GLU ARG MET ARG VAL GLN ALA GLY
SEQRES 13 A 496 ALA PRO VAL THR ILE GLN LYS GLU PHE SER LEU LEU THR
SEQRES 14 A 496 CYS SER ILE ILE CYS TYR LEU THR PHE GLY ASN LYS GLU
SEQRES 15 A 496 ASP THR LEU VAL HIS ALA PHE HIS ASP CYS VAL GLN ASP
SEQRES 16 A 496 LEU MET LYS THR TRP ASP HIS TRP SER ILE GLN ILE LEU
SEQRES 17 A 496 ASP MET VAL PRO PHE LEU ARG PHE PHE PRO ASN PRO GLY
SEQRES 18 A 496 LEU TRP ARG LEU LYS GLN ALA ILE GLU ASN ARG ASP HIS
SEQRES 19 A 496 MET VAL GLU LYS GLN LEU ARG ARG HIS LYS GLU SER MET
SEQRES 20 A 496 VAL ALA GLY GLN TRP ARG ASP MET THR ASP TYR MET LEU
SEQRES 21 A 496 GLN GLY VAL GLY ARG GLN ARG VAL GLU GLU GLY PRO GLY
SEQRES 22 A 496 GLN LEU LEU GLU GLY HIS VAL HIS MET SER VAL VAL ASP
SEQRES 23 A 496 LEU PHE ILE GLY GLY THR GLU THR THR ALA SER THR LEU
SEQRES 24 A 496 SER TRP ALA VAL ALA PHE LEU LEU HIS HIS PRO GLU ILE
SEQRES 25 A 496 GLN ARG ARG LEU GLN GLU GLU LEU ASP ARG GLU LEU GLY
SEQRES 26 A 496 PRO GLY ALA SER CYS SER ARG VAL THR TYR LYS ASP ARG
SEQRES 27 A 496 ALA ARG LEU PRO LEU LEU ASN ALA THR ILE ALA GLU VAL
SEQRES 28 A 496 LEU ARG LEU ARG PRO VAL VAL PRO LEU ALA LEU PRO HIS
SEQRES 29 A 496 ARG THR THR ARG PRO SER SER ILE PHE GLY TYR ASP ILE
SEQRES 30 A 496 PRO GLU GLY MET VAL VAL ILE PRO ASN LEU GLN GLY ALA
SEQRES 31 A 496 HIS LEU ASP GLU THR VAL TRP GLU GLN PRO HIS GLU PHE
SEQRES 32 A 496 ARG PRO ASP ARG PHE LEU GLU PRO GLY ALA ASN PRO SER
SEQRES 33 A 496 ALA LEU ALA PHE GLY CYS GLY ALA ARG VAL CYS LEU GLY
SEQRES 34 A 496 GLU SER LEU ALA ARG LEU GLU LEU PHE VAL VAL LEU ALA
SEQRES 35 A 496 ARG LEU LEU GLN ALA PHE THR LEU LEU PRO PRO PRO VAL
SEQRES 36 A 496 GLY ALA LEU PRO SER LEU GLN PRO ASP PRO TYR CYS GLY
SEQRES 37 A 496 VAL ASN LEU LYS VAL GLN PRO PHE GLN VAL ARG LEU GLN
SEQRES 38 A 496 PRO ARG GLY VAL GLU ALA GLY ALA TRP GLU SER ALA SER
SEQRES 39 A 496 ALA GLN
SEQRES 1 B 496 MET VAL LEU ALA GLY LEU LEU LEU LEU LEU THR LEU LEU
SEQRES 2 B 496 ALA GLY ALA HIS LEU LEU TRP GLY ARG TRP LYS LEU ARG
SEQRES 3 B 496 ASN LEU HIS LEU PRO PRO LEU VAL PRO GLY PHE LEU HIS
SEQRES 4 B 496 LEU LEU GLN PRO ASN LEU PRO ILE HIS LEU LEU SER LEU
SEQRES 5 B 496 THR GLN LYS LEU GLY PRO VAL TYR ARG LEU ARG LEU GLY
SEQRES 6 B 496 LEU GLN GLU VAL VAL VAL LEU ASN SER LYS ARG THR ILE
SEQRES 7 B 496 GLU GLU ALA MET ILE ARG LYS TRP VAL ASP PHE ALA GLY
SEQRES 8 B 496 ARG PRO GLN ILE PRO SER TYR LYS LEU VAL SER GLN ARG
SEQRES 9 B 496 CYS GLN ASP ILE SER LEU GLY ASP TYR SER LEU LEU TRP
SEQRES 10 B 496 LYS ALA HIS LYS LYS LEU THR ARG SER ALA LEU LEU LEU
SEQRES 11 B 496 GLY THR ARG SER SER MET GLU PRO TRP VAL ASP GLN LEU
SEQRES 12 B 496 THR GLN GLU PHE CYS GLU ARG MET ARG VAL GLN ALA GLY
SEQRES 13 B 496 ALA PRO VAL THR ILE GLN LYS GLU PHE SER LEU LEU THR
SEQRES 14 B 496 CYS SER ILE ILE CYS TYR LEU THR PHE GLY ASN LYS GLU
SEQRES 15 B 496 ASP THR LEU VAL HIS ALA PHE HIS ASP CYS VAL GLN ASP
SEQRES 16 B 496 LEU MET LYS THR TRP ASP HIS TRP SER ILE GLN ILE LEU
SEQRES 17 B 496 ASP MET VAL PRO PHE LEU ARG PHE PHE PRO ASN PRO GLY
SEQRES 18 B 496 LEU TRP ARG LEU LYS GLN ALA ILE GLU ASN ARG ASP HIS
SEQRES 19 B 496 MET VAL GLU LYS GLN LEU ARG ARG HIS LYS GLU SER MET
SEQRES 20 B 496 VAL ALA GLY GLN TRP ARG ASP MET THR ASP TYR MET LEU
SEQRES 21 B 496 GLN GLY VAL GLY ARG GLN ARG VAL GLU GLU GLY PRO GLY
SEQRES 22 B 496 GLN LEU LEU GLU GLY HIS VAL HIS MET SER VAL VAL ASP
SEQRES 23 B 496 LEU PHE ILE GLY GLY THR GLU THR THR ALA SER THR LEU
SEQRES 24 B 496 SER TRP ALA VAL ALA PHE LEU LEU HIS HIS PRO GLU ILE
SEQRES 25 B 496 GLN ARG ARG LEU GLN GLU GLU LEU ASP ARG GLU LEU GLY
SEQRES 26 B 496 PRO GLY ALA SER CYS SER ARG VAL THR TYR LYS ASP ARG
SEQRES 27 B 496 ALA ARG LEU PRO LEU LEU ASN ALA THR ILE ALA GLU VAL
SEQRES 28 B 496 LEU ARG LEU ARG PRO VAL VAL PRO LEU ALA LEU PRO HIS
SEQRES 29 B 496 ARG THR THR ARG PRO SER SER ILE PHE GLY TYR ASP ILE
SEQRES 30 B 496 PRO GLU GLY MET VAL VAL ILE PRO ASN LEU GLN GLY ALA
SEQRES 31 B 496 HIS LEU ASP GLU THR VAL TRP GLU GLN PRO HIS GLU PHE
SEQRES 32 B 496 ARG PRO ASP ARG PHE LEU GLU PRO GLY ALA ASN PRO SER
SEQRES 33 B 496 ALA LEU ALA PHE GLY CYS GLY ALA ARG VAL CYS LEU GLY
SEQRES 34 B 496 GLU SER LEU ALA ARG LEU GLU LEU PHE VAL VAL LEU ALA
SEQRES 35 B 496 ARG LEU LEU GLN ALA PHE THR LEU LEU PRO PRO PRO VAL
SEQRES 36 B 496 GLY ALA LEU PRO SER LEU GLN PRO ASP PRO TYR CYS GLY
SEQRES 37 B 496 VAL ASN LEU LYS VAL GLN PRO PHE GLN VAL ARG LEU GLN
SEQRES 38 B 496 PRO ARG GLY VAL GLU ALA GLY ALA TRP GLU SER ALA SER
SEQRES 39 B 496 ALA GLN
SEQRES 1 C 496 MET VAL LEU ALA GLY LEU LEU LEU LEU LEU THR LEU LEU
SEQRES 2 C 496 ALA GLY ALA HIS LEU LEU TRP GLY ARG TRP LYS LEU ARG
SEQRES 3 C 496 ASN LEU HIS LEU PRO PRO LEU VAL PRO GLY PHE LEU HIS
SEQRES 4 C 496 LEU LEU GLN PRO ASN LEU PRO ILE HIS LEU LEU SER LEU
SEQRES 5 C 496 THR GLN LYS LEU GLY PRO VAL TYR ARG LEU ARG LEU GLY
SEQRES 6 C 496 LEU GLN GLU VAL VAL VAL LEU ASN SER LYS ARG THR ILE
SEQRES 7 C 496 GLU GLU ALA MET ILE ARG LYS TRP VAL ASP PHE ALA GLY
SEQRES 8 C 496 ARG PRO GLN ILE PRO SER TYR LYS LEU VAL SER GLN ARG
SEQRES 9 C 496 CYS GLN ASP ILE SER LEU GLY ASP TYR SER LEU LEU TRP
SEQRES 10 C 496 LYS ALA HIS LYS LYS LEU THR ARG SER ALA LEU LEU LEU
SEQRES 11 C 496 GLY THR ARG SER SER MET GLU PRO TRP VAL ASP GLN LEU
SEQRES 12 C 496 THR GLN GLU PHE CYS GLU ARG MET ARG VAL GLN ALA GLY
SEQRES 13 C 496 ALA PRO VAL THR ILE GLN LYS GLU PHE SER LEU LEU THR
SEQRES 14 C 496 CYS SER ILE ILE CYS TYR LEU THR PHE GLY ASN LYS GLU
SEQRES 15 C 496 ASP THR LEU VAL HIS ALA PHE HIS ASP CYS VAL GLN ASP
SEQRES 16 C 496 LEU MET LYS THR TRP ASP HIS TRP SER ILE GLN ILE LEU
SEQRES 17 C 496 ASP MET VAL PRO PHE LEU ARG PHE PHE PRO ASN PRO GLY
SEQRES 18 C 496 LEU TRP ARG LEU LYS GLN ALA ILE GLU ASN ARG ASP HIS
SEQRES 19 C 496 MET VAL GLU LYS GLN LEU ARG ARG HIS LYS GLU SER MET
SEQRES 20 C 496 VAL ALA GLY GLN TRP ARG ASP MET THR ASP TYR MET LEU
SEQRES 21 C 496 GLN GLY VAL GLY ARG GLN ARG VAL GLU GLU GLY PRO GLY
SEQRES 22 C 496 GLN LEU LEU GLU GLY HIS VAL HIS MET SER VAL VAL ASP
SEQRES 23 C 496 LEU PHE ILE GLY GLY THR GLU THR THR ALA SER THR LEU
SEQRES 24 C 496 SER TRP ALA VAL ALA PHE LEU LEU HIS HIS PRO GLU ILE
SEQRES 25 C 496 GLN ARG ARG LEU GLN GLU GLU LEU ASP ARG GLU LEU GLY
SEQRES 26 C 496 PRO GLY ALA SER CYS SER ARG VAL THR TYR LYS ASP ARG
SEQRES 27 C 496 ALA ARG LEU PRO LEU LEU ASN ALA THR ILE ALA GLU VAL
SEQRES 28 C 496 LEU ARG LEU ARG PRO VAL VAL PRO LEU ALA LEU PRO HIS
SEQRES 29 C 496 ARG THR THR ARG PRO SER SER ILE PHE GLY TYR ASP ILE
SEQRES 30 C 496 PRO GLU GLY MET VAL VAL ILE PRO ASN LEU GLN GLY ALA
SEQRES 31 C 496 HIS LEU ASP GLU THR VAL TRP GLU GLN PRO HIS GLU PHE
SEQRES 32 C 496 ARG PRO ASP ARG PHE LEU GLU PRO GLY ALA ASN PRO SER
SEQRES 33 C 496 ALA LEU ALA PHE GLY CYS GLY ALA ARG VAL CYS LEU GLY
SEQRES 34 C 496 GLU SER LEU ALA ARG LEU GLU LEU PHE VAL VAL LEU ALA
SEQRES 35 C 496 ARG LEU LEU GLN ALA PHE THR LEU LEU PRO PRO PRO VAL
SEQRES 36 C 496 GLY ALA LEU PRO SER LEU GLN PRO ASP PRO TYR CYS GLY
SEQRES 37 C 496 VAL ASN LEU LYS VAL GLN PRO PHE GLN VAL ARG LEU GLN
SEQRES 38 C 496 PRO ARG GLY VAL GLU ALA GLY ALA TRP GLU SER ALA SER
SEQRES 39 C 496 ALA GLN
SEQRES 1 D 496 MET VAL LEU ALA GLY LEU LEU LEU LEU LEU THR LEU LEU
SEQRES 2 D 496 ALA GLY ALA HIS LEU LEU TRP GLY ARG TRP LYS LEU ARG
SEQRES 3 D 496 ASN LEU HIS LEU PRO PRO LEU VAL PRO GLY PHE LEU HIS
SEQRES 4 D 496 LEU LEU GLN PRO ASN LEU PRO ILE HIS LEU LEU SER LEU
SEQRES 5 D 496 THR GLN LYS LEU GLY PRO VAL TYR ARG LEU ARG LEU GLY
SEQRES 6 D 496 LEU GLN GLU VAL VAL VAL LEU ASN SER LYS ARG THR ILE
SEQRES 7 D 496 GLU GLU ALA MET ILE ARG LYS TRP VAL ASP PHE ALA GLY
SEQRES 8 D 496 ARG PRO GLN ILE PRO SER TYR LYS LEU VAL SER GLN ARG
SEQRES 9 D 496 CYS GLN ASP ILE SER LEU GLY ASP TYR SER LEU LEU TRP
SEQRES 10 D 496 LYS ALA HIS LYS LYS LEU THR ARG SER ALA LEU LEU LEU
SEQRES 11 D 496 GLY THR ARG SER SER MET GLU PRO TRP VAL ASP GLN LEU
SEQRES 12 D 496 THR GLN GLU PHE CYS GLU ARG MET ARG VAL GLN ALA GLY
SEQRES 13 D 496 ALA PRO VAL THR ILE GLN LYS GLU PHE SER LEU LEU THR
SEQRES 14 D 496 CYS SER ILE ILE CYS TYR LEU THR PHE GLY ASN LYS GLU
SEQRES 15 D 496 ASP THR LEU VAL HIS ALA PHE HIS ASP CYS VAL GLN ASP
SEQRES 16 D 496 LEU MET LYS THR TRP ASP HIS TRP SER ILE GLN ILE LEU
SEQRES 17 D 496 ASP MET VAL PRO PHE LEU ARG PHE PHE PRO ASN PRO GLY
SEQRES 18 D 496 LEU TRP ARG LEU LYS GLN ALA ILE GLU ASN ARG ASP HIS
SEQRES 19 D 496 MET VAL GLU LYS GLN LEU ARG ARG HIS LYS GLU SER MET
SEQRES 20 D 496 VAL ALA GLY GLN TRP ARG ASP MET THR ASP TYR MET LEU
SEQRES 21 D 496 GLN GLY VAL GLY ARG GLN ARG VAL GLU GLU GLY PRO GLY
SEQRES 22 D 496 GLN LEU LEU GLU GLY HIS VAL HIS MET SER VAL VAL ASP
SEQRES 23 D 496 LEU PHE ILE GLY GLY THR GLU THR THR ALA SER THR LEU
SEQRES 24 D 496 SER TRP ALA VAL ALA PHE LEU LEU HIS HIS PRO GLU ILE
SEQRES 25 D 496 GLN ARG ARG LEU GLN GLU GLU LEU ASP ARG GLU LEU GLY
SEQRES 26 D 496 PRO GLY ALA SER CYS SER ARG VAL THR TYR LYS ASP ARG
SEQRES 27 D 496 ALA ARG LEU PRO LEU LEU ASN ALA THR ILE ALA GLU VAL
SEQRES 28 D 496 LEU ARG LEU ARG PRO VAL VAL PRO LEU ALA LEU PRO HIS
SEQRES 29 D 496 ARG THR THR ARG PRO SER SER ILE PHE GLY TYR ASP ILE
SEQRES 30 D 496 PRO GLU GLY MET VAL VAL ILE PRO ASN LEU GLN GLY ALA
SEQRES 31 D 496 HIS LEU ASP GLU THR VAL TRP GLU GLN PRO HIS GLU PHE
SEQRES 32 D 496 ARG PRO ASP ARG PHE LEU GLU PRO GLY ALA ASN PRO SER
SEQRES 33 D 496 ALA LEU ALA PHE GLY CYS GLY ALA ARG VAL CYS LEU GLY
SEQRES 34 D 496 GLU SER LEU ALA ARG LEU GLU LEU PHE VAL VAL LEU ALA
SEQRES 35 D 496 ARG LEU LEU GLN ALA PHE THR LEU LEU PRO PRO PRO VAL
SEQRES 36 D 496 GLY ALA LEU PRO SER LEU GLN PRO ASP PRO TYR CYS GLY
SEQRES 37 D 496 VAL ASN LEU LYS VAL GLN PRO PHE GLN VAL ARG LEU GLN
SEQRES 38 D 496 PRO ARG GLY VAL GLU ALA GLY ALA TRP GLU SER ALA SER
SEQRES 39 D 496 ALA GLN
HET HEM A 500 43
HET 3QZ A 501 24
HET 3QZ A 502 24
HET HEM B 500 43
HET 3QZ B 501 24
HET 3QZ B 502 24
HET HEM C 500 43
HET 3QZ C 501 24
HET 3QZ C 502 24
HET HEM D 500 43
HET 3QZ D 501 24
HET 3QZ D 502 24
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM 3QZ (9BETA)-17-HYDROXYPREGN-4-ENE-3,20-DIONE
HETSYN HEM HEME
FORMUL 5 HEM 4(C34 H32 FE N4 O4)
FORMUL 6 3QZ 8(C21 H30 O3)
FORMUL 17 HOH *97(H2 O)
HELIX 1 1 ASN A 44 LEU A 52 1 9
HELIX 2 2 THR A 53 LYS A 55 5 3
HELIX 3 3 ARG A 76 ALA A 81 1 6
HELIX 4 4 SER A 114 LEU A 130 1 17
HELIX 5 5 MET A 136 VAL A 153 1 18
HELIX 6 6 VAL A 159 SER A 166 1 8
HELIX 7 7 SER A 166 ILE A 173 1 8
HELIX 8 8 GLU A 182 ASP A 195 1 14
HELIX 9 9 HIS A 202 VAL A 211 1 10
HELIX 10 10 PRO A 212 ARG A 215 5 4
HELIX 11 11 ASN A 219 SER A 246 1 28
HELIX 12 12 MET A 255 LEU A 260 1 6
HELIX 13 13 GLU A 277 HIS A 309 1 33
HELIX 14 14 HIS A 309 GLY A 325 1 17
HELIX 15 15 LYS A 336 ARG A 340 5 5
HELIX 16 16 LEU A 341 ARG A 355 1 15
HELIX 17 17 ASN A 386 HIS A 391 1 6
HELIX 18 18 GLY A 429 PHE A 448 1 20
HELIX 19 19 ASN B 44 LEU B 52 1 9
HELIX 20 20 THR B 53 LYS B 55 5 3
HELIX 21 21 ARG B 76 ALA B 81 1 6
HELIX 22 22 SER B 114 LEU B 130 1 17
HELIX 23 23 MET B 136 VAL B 153 1 18
HELIX 24 24 VAL B 159 SER B 166 1 8
HELIX 25 25 LEU B 168 THR B 177 1 10
HELIX 26 26 GLU B 182 ASP B 195 1 14
HELIX 27 27 HIS B 202 VAL B 211 1 10
HELIX 28 28 PRO B 212 ARG B 215 5 4
HELIX 29 29 ASN B 219 GLU B 245 1 27
HELIX 30 30 MET B 255 VAL B 263 1 9
HELIX 31 31 GLU B 277 HIS B 309 1 33
HELIX 32 32 HIS B 309 GLY B 325 1 17
HELIX 33 33 LEU B 341 ARG B 355 1 15
HELIX 34 34 ASN B 386 HIS B 391 1 6
HELIX 35 35 GLY B 429 PHE B 448 1 20
HELIX 36 36 ASN C 44 GLY C 57 1 14
HELIX 37 37 ARG C 76 ALA C 81 1 6
HELIX 38 38 TRP C 86 ALA C 90 5 5
HELIX 39 39 SER C 114 ALA C 127 1 14
HELIX 40 40 GLU C 137 VAL C 153 1 17
HELIX 41 41 VAL C 159 TYR C 175 1 17
HELIX 42 42 GLU C 182 ASP C 195 1 14
HELIX 43 43 HIS C 202 VAL C 211 1 10
HELIX 44 44 ASN C 219 GLU C 245 1 27
HELIX 45 45 MET C 255 VAL C 263 1 9
HELIX 46 46 GLU C 277 ILE C 289 1 13
HELIX 47 47 GLY C 290 HIS C 309 1 20
HELIX 48 48 HIS C 309 GLY C 325 1 17
HELIX 49 49 THR C 334 ARG C 338 5 5
HELIX 50 50 LEU C 341 ARG C 355 1 15
HELIX 51 51 ASN C 386 HIS C 391 1 6
HELIX 52 52 GLY C 429 PHE C 448 1 20
HELIX 53 53 ASN D 44 GLY D 57 1 14
HELIX 54 54 SER D 74 ALA D 81 1 8
HELIX 55 55 LYS D 85 ALA D 90 5 6
HELIX 56 56 ILE D 95 LEU D 100 1 6
HELIX 57 57 SER D 114 ALA D 127 1 14
HELIX 58 58 MET D 136 VAL D 153 1 18
HELIX 59 59 VAL D 159 SER D 166 1 8
HELIX 60 60 SER D 166 TYR D 175 1 10
HELIX 61 61 GLU D 182 ASP D 195 1 14
HELIX 62 62 HIS D 202 VAL D 211 1 10
HELIX 63 63 PRO D 212 ARG D 215 5 4
HELIX 64 64 ASN D 219 SER D 246 1 28
HELIX 65 65 MET D 255 LEU D 260 1 6
HELIX 66 66 LEU D 276 HIS D 309 1 34
HELIX 67 67 HIS D 309 ARG D 322 1 14
HELIX 68 68 THR D 334 ARG D 340 5 7
HELIX 69 69 LEU D 341 ARG D 355 1 15
HELIX 70 70 GLY D 389 ASP D 393 5 5
HELIX 71 71 GLY D 429 LEU D 445 1 17
SHEET 1 A 4 VAL A 59 LEU A 62 0
SHEET 2 A 4 VAL A 69 LEU A 72 -1 O VAL A 69 N LEU A 62
SHEET 3 A 4 VAL A 382 PRO A 385 1 O ILE A 384 N VAL A 70
SHEET 4 A 4 HIS A 364 ARG A 365 -1 N HIS A 364 O VAL A 383
SHEET 1 B 2 SER A 370 SER A 371 0
SHEET 2 B 2 ASP A 376 ILE A 377 -1 O ILE A 377 N SER A 370
SHEET 1 C 4 VAL B 59 LEU B 62 0
SHEET 2 C 4 VAL B 69 LEU B 72 -1 O VAL B 69 N LEU B 62
SHEET 3 C 4 VAL B 382 PRO B 385 1 O ILE B 384 N VAL B 70
SHEET 4 C 4 HIS B 364 ARG B 365 -1 N HIS B 364 O VAL B 383
SHEET 1 D 2 SER B 370 SER B 371 0
SHEET 2 D 2 ASP B 376 ILE B 377 -1 O ILE B 377 N SER B 370
SHEET 1 E 5 LEU C 33 VAL C 34 0
SHEET 2 E 5 VAL C 59 LEU C 62 1 O ARG C 61 N VAL C 34
SHEET 3 E 5 VAL C 69 LEU C 72 -1 O VAL C 69 N LEU C 62
SHEET 4 E 5 VAL C 382 PRO C 385 1 O ILE C 384 N VAL C 70
SHEET 5 E 5 HIS C 364 ARG C 365 -1 N HIS C 364 O VAL C 383
SHEET 1 F 2 SER C 370 SER C 371 0
SHEET 2 F 2 ASP C 376 ILE C 377 -1 O ILE C 377 N SER C 370
SHEET 1 G 4 VAL D 59 LEU D 62 0
SHEET 2 G 4 VAL D 69 LEU D 72 -1 O VAL D 71 N TYR D 60
SHEET 3 G 4 VAL D 382 PRO D 385 1 O ILE D 384 N VAL D 70
SHEET 4 G 4 HIS D 364 ARG D 365 -1 N HIS D 364 O VAL D 383
LINK SG CYS A 427 FE HEM A 500 1555 1555 2.67
CISPEP 1 GLU D 410 PRO D 411 0 -0.89
SITE 1 AC1 23 ARG A 92 ILE A 108 SER A 109 TRP A 117
SITE 2 AC1 23 LEU A 128 GLY A 291 THR A 294 THR A 295
SITE 3 AC1 23 THR A 298 LEU A 352 ALA A 361 LEU A 362
SITE 4 AC1 23 HIS A 364 LEU A 387 ALA A 419 PHE A 420
SITE 5 AC1 23 ARG A 425 VAL A 426 CYS A 427 LEU A 428
SITE 6 AC1 23 GLY A 429 ALA A 433 3QZ A 501
SITE 1 AC2 8 LEU A 110 LEU A 196 TRP A 200 ARG A 232
SITE 2 AC2 8 GLY A 290 THR A 294 VAL A 358 HEM A 500
SITE 1 AC3 5 LEU A 64 GLN A 67 ILE A 95 GLN A 206
SITE 2 AC3 5 VAL A 382
SITE 1 AC4 22 ARG B 92 ILE B 108 SER B 109 TRP B 117
SITE 2 AC4 22 LYS B 121 LEU B 128 GLY B 291 THR B 294
SITE 3 AC4 22 THR B 295 THR B 298 VAL B 358 LEU B 362
SITE 4 AC4 22 HIS B 364 LEU B 387 ALA B 419 PHE B 420
SITE 5 AC4 22 ARG B 425 CYS B 427 LEU B 428 GLY B 429
SITE 6 AC4 22 ALA B 433 3QZ B 501
SITE 1 AC5 11 SER B 109 LEU B 110 LEU B 196 TRP B 200
SITE 2 AC5 11 ILE B 229 ARG B 232 GLY B 290 THR B 294
SITE 3 AC5 11 VAL B 358 VAL B 469 HEM B 500
SITE 1 AC6 5 LEU B 40 LEU B 64 GLN B 206 MET B 210
SITE 2 AC6 5 LEU B 360
SITE 1 AC7 20 ARG C 92 ILE C 108 SER C 109 GLY C 291
SITE 2 AC7 20 THR C 294 THR C 295 THR C 298 LEU C 352
SITE 3 AC7 20 VAL C 358 HIS C 364 LEU C 387 ALA C 419
SITE 4 AC7 20 PHE C 420 ARG C 425 CYS C 427 LEU C 428
SITE 5 AC7 20 GLY C 429 ALA C 433 3QZ C 501 HOH C 606
SITE 1 AC8 9 VAL C 101 SER C 109 LEU C 196 TRP C 200
SITE 2 AC8 9 ILE C 229 ARG C 232 ASP C 286 THR C 294
SITE 3 AC8 9 HEM C 500
SITE 1 AC9 5 GLN C 206 LEU C 360 ALA C 361 CYS C 467
SITE 2 AC9 5 GLY C 468
SITE 1 BC1 20 ARG D 92 SER D 109 TRP D 117 LYS D 121
SITE 2 BC1 20 GLY D 291 THR D 294 THR D 295 THR D 298
SITE 3 BC1 20 VAL D 358 ALA D 361 HIS D 364 LEU D 387
SITE 4 BC1 20 ALA D 419 PHE D 420 ARG D 425 VAL D 426
SITE 5 BC1 20 CYS D 427 LEU D 428 GLY D 429 3QZ D 501
SITE 1 BC2 7 SER D 109 LEU D 196 TRP D 200 ARG D 232
SITE 2 BC2 7 ASP D 286 THR D 294 HEM D 500
SITE 1 BC3 6 LEU D 64 GLY D 65 GLN D 206 LEU D 360
SITE 2 BC3 6 ALA D 361 CYS D 467
CRYST1 67.871 167.998 111.843 90.00 90.09 90.00 P 1 21 1 8
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 0.014734 0.000000 0.000023 0.00000
SCALE2 0.000000 0.005952 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008941 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
