HEADER OXIDOREDUCTASE 12-MAY-05 1ZO4
TITLE CRYSTAL STRUCTURE OF A328S MUTANT OF THE HEME DOMAIN OF P450BM-3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BIFUNCTIONAL P-450:NADPH-P450 REDUCTASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CYTOCHROME P450;
COMPND 5 EC: 1.14.14.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS MEGATERIUM;
SOURCE 3 ORGANISM_TAXID: 1404;
SOURCE 4 GENE: CYP102A1, CYP102;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: DH5ALPHA F'IQ;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PPROEX-1
KEYWDS CYTOCHROME P-450, HEMEPROTEIN A328S, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.HEGDA,B.CHEN,D.C.HAINES,M.BONDLELA,D.MULLIN,S.E.GRAHAM,
AUTHOR 2 D.R.TOMCHICK,M.MACHIUS,J.A.PETERSON
REVDAT 6 23-AUG-23 1ZO4 1 REMARK
REVDAT 5 20-OCT-21 1ZO4 1 REMARK SEQADV LINK
REVDAT 4 22-FEB-12 1ZO4 1 JRNL
REVDAT 3 13-JUL-11 1ZO4 1 VERSN
REVDAT 2 24-FEB-09 1ZO4 1 VERSN
REVDAT 1 01-AUG-06 1ZO4 0
JRNL AUTH D.C.HAINES,A.HEGDE,B.CHEN,W.ZHAO,M.BONDLELA,J.M.HUMPHREYS,
JRNL AUTH 2 D.A.MULLIN,D.R.TOMCHICK,M.MACHIUS,J.A.PETERSON
JRNL TITL A SINGLE ACTIVE-SITE MUTATION OF P450BM-3 DRAMATICALLY
JRNL TITL 2 ENHANCES SUBSTRATE BINDING AND RATE OF PRODUCT FORMATION.
JRNL REF BIOCHEMISTRY V. 50 8333 2011
JRNL REFN ISSN 0006-2960
JRNL PMID 21875028
JRNL DOI 10.1021/BI201099J
REMARK 2
REMARK 2 RESOLUTION. 1.46 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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.46
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.30
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.6
REMARK 3 NUMBER OF REFLECTIONS : 177454
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 SET) : 0.189
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 8896
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 7354
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 230
REMARK 3 SOLVENT ATOMS : 830
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.26
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.45000
REMARK 3 B22 (A**2) : 4.63000
REMARK 3 B33 (A**2) : -7.08000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -5.24000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.19
REMARK 3 ESD FROM SIGMAA (A) : 0.25
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) : 0.25
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.23
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.530
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.850
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
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 : NULL
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : LIGANDS_JAP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ZO4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000032944.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-APR-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.03320
REMARK 200 MONOCHROMATOR : SILICON SINGLE CRYSTAL
REMARK 200 MONOCHROMATORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : SBC-2
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 177454
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.460
REMARK 200 RESOLUTION RANGE LOW (A) : 29.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.1
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : 0.06500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.46
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.48
REMARK 200 COMPLETENESS FOR SHELL (%) : 60.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.30
REMARK 200 R MERGE FOR SHELL (I) : 0.74800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1FAG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, MES, MAGNESIUM CHLORIDE,
REMARK 280 GLYCEROL, PH 6.0, TEMPERATURE 277K, VAPOR DIFFUSION, HANGING DROP
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 76.60450
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
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 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 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A -2
REMARK 465 ALA A -1
REMARK 465 MET A 0
REMARK 465 GLY A 457
REMARK 465 ILE A 458
REMARK 465 PRO A 459
REMARK 465 SER A 460
REMARK 465 PRO A 461
REMARK 465 SER A 462
REMARK 465 THR A 463
REMARK 465 GLU A 464
REMARK 465 GLN A 465
REMARK 465 SER A 466
REMARK 465 ALA A 467
REMARK 465 LYS A 468
REMARK 465 LYS A 469
REMARK 465 VAL A 470
REMARK 465 GLY B -2
REMARK 465 ALA B -1
REMARK 465 MET B 0
REMARK 465 ILE B 458
REMARK 465 PRO B 459
REMARK 465 SER B 460
REMARK 465 PRO B 461
REMARK 465 SER B 462
REMARK 465 THR B 463
REMARK 465 GLU B 464
REMARK 465 GLN B 465
REMARK 465 SER B 466
REMARK 465 ALA B 467
REMARK 465 LYS B 468
REMARK 465 LYS B 469
REMARK 465 VAL B 470
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 SER A 328 N - CA - C ANGL. DEV. = -17.1 DEGREES
REMARK 500 SER B 328 N - CA - C ANGL. DEV. = -17.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LYS A 15 -124.58 63.88
REMARK 500 ASP A 84 40.11 -95.51
REMARK 500 PHE A 158 27.13 -147.03
REMARK 500 ASN A 192 77.25 -108.46
REMARK 500 ASP A 370 43.65 -80.90
REMARK 500 THR A 436 -129.34 -139.33
REMARK 500 LYS B 15 -128.91 52.87
REMARK 500 ASP B 84 42.03 -98.36
REMARK 500 PHE B 158 33.22 -148.30
REMARK 500 PRO B 193 -4.79 -58.54
REMARK 500 ASP B 231 40.59 -93.61
REMARK 500 HIS B 388 14.37 59.44
REMARK 500 THR B 436 -125.22 -134.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 471 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 400 SG
REMARK 620 2 HEM A 471 NA 98.4
REMARK 620 3 HEM A 471 NB 88.6 90.0
REMARK 620 4 HEM A 471 NC 86.9 174.7 90.6
REMARK 620 5 HEM A 471 ND 98.0 89.0 173.4 89.8
REMARK 620 6 HOH A1867 O 171.9 77.2 84.7 97.6 88.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 471 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 400 SG
REMARK 620 2 HEM B 471 NA 98.5
REMARK 620 3 HEM B 471 NB 87.3 89.7
REMARK 620 4 HEM B 471 NC 86.4 175.1 89.9
REMARK 620 5 HEM B 471 ND 98.6 90.0 174.1 89.9
REMARK 620 6 HOH B1895 O 171.7 77.2 85.6 97.9 88.5
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 471
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 471
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES B 1490
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES A 1491
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1470
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1471
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1472
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1473
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1474
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1475
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1481
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1482
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1483
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1484
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1485
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1486
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1487
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1488
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1489
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JPZ RELATED DB: PDB
REMARK 900 N-PALMITOYLGLYCINE BOUND HEME DOMAIN OF P450BM-3
REMARK 900 RELATED ID: 2HPD RELATED DB: PDB
REMARK 900 ORIGINAL STRUCTURE OF THE HEME DOMAIN OF THE SAME PROTEIN
REMARK 900 RELATED ID: 1BU7 RELATED DB: PDB
REMARK 900 CRYOGENIC STRUCTURE OF THE HEME DOMAIN OF THE SAME PROTEIN
REMARK 900 RELATED ID: 1ZO9 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE WILD TYPE HEME DOMAIN OF THE SAME PROTEIN
REMARK 900 WITH N-PALMITOYLMETHIONINE
REMARK 900 RELATED ID: 1ZOA RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A328V MUTANT OF THE HEME DOMAIN OF THE SAME
REMARK 900 PROTEIN WITH N-PALMITOYLGLYCINE
DBREF 1ZO4 A 1 470 UNP P14779 CPXB_BACME 1 470
DBREF 1ZO4 B 1 470 UNP P14779 CPXB_BACME 1 470
SEQADV 1ZO4 GLY A -2 UNP P14779 EXPRESSION TAG
SEQADV 1ZO4 ALA A -1 UNP P14779 EXPRESSION TAG
SEQADV 1ZO4 MET A 0 UNP P14779 EXPRESSION TAG
SEQADV 1ZO4 SER A 328 UNP P14779 ALA 328 ENGINEERED MUTATION
SEQADV 1ZO4 GLY B -2 UNP P14779 EXPRESSION TAG
SEQADV 1ZO4 ALA B -1 UNP P14779 EXPRESSION TAG
SEQADV 1ZO4 MET B 0 UNP P14779 EXPRESSION TAG
SEQADV 1ZO4 SER B 328 UNP P14779 ALA 328 ENGINEERED MUTATION
SEQRES 1 A 473 GLY ALA MET THR ILE LYS GLU MET PRO GLN PRO LYS THR
SEQRES 2 A 473 PHE GLY GLU LEU LYS ASN LEU PRO LEU LEU ASN THR ASP
SEQRES 3 A 473 LYS PRO VAL GLN ALA LEU MET LYS ILE ALA ASP GLU LEU
SEQRES 4 A 473 GLY GLU ILE PHE LYS PHE GLU ALA PRO GLY ARG VAL THR
SEQRES 5 A 473 ARG TYR LEU SER SER GLN ARG LEU ILE LYS GLU ALA CYS
SEQRES 6 A 473 ASP GLU SER ARG PHE ASP LYS ASN LEU SER GLN ALA LEU
SEQRES 7 A 473 LYS PHE VAL ARG ASP PHE ALA GLY ASP GLY LEU PHE THR
SEQRES 8 A 473 SER TRP THR HIS GLU LYS ASN TRP LYS LYS ALA HIS ASN
SEQRES 9 A 473 ILE LEU LEU PRO SER PHE SER GLN GLN ALA MET LYS GLY
SEQRES 10 A 473 TYR HIS ALA MET MET VAL ASP ILE ALA VAL GLN LEU VAL
SEQRES 11 A 473 GLN LYS TRP GLU ARG LEU ASN ALA ASP GLU HIS ILE GLU
SEQRES 12 A 473 VAL PRO GLU ASP MET THR ARG LEU THR LEU ASP THR ILE
SEQRES 13 A 473 GLY LEU CYS GLY PHE ASN TYR ARG PHE ASN SER PHE TYR
SEQRES 14 A 473 ARG ASP GLN PRO HIS PRO PHE ILE THR SER MET VAL ARG
SEQRES 15 A 473 ALA LEU ASP GLU ALA MET ASN LYS LEU GLN ARG ALA ASN
SEQRES 16 A 473 PRO ASP ASP PRO ALA TYR ASP GLU ASN LYS ARG GLN PHE
SEQRES 17 A 473 GLN GLU ASP ILE LYS VAL MET ASN ASP LEU VAL ASP LYS
SEQRES 18 A 473 ILE ILE ALA ASP ARG LYS ALA SER GLY GLU GLN SER ASP
SEQRES 19 A 473 ASP LEU LEU THR HIS MET LEU ASN GLY LYS ASP PRO GLU
SEQRES 20 A 473 THR GLY GLU PRO LEU ASP ASP GLU ASN ILE ARG TYR GLN
SEQRES 21 A 473 ILE ILE THR PHE LEU ILE ALA GLY HIS GLU THR THR SER
SEQRES 22 A 473 GLY LEU LEU SER PHE ALA LEU TYR PHE LEU VAL LYS ASN
SEQRES 23 A 473 PRO HIS VAL LEU GLN LYS ALA ALA GLU GLU ALA ALA ARG
SEQRES 24 A 473 VAL LEU VAL ASP PRO VAL PRO SER TYR LYS GLN VAL LYS
SEQRES 25 A 473 GLN LEU LYS TYR VAL GLY MET VAL LEU ASN GLU ALA LEU
SEQRES 26 A 473 ARG LEU TRP PRO THR SER PRO ALA PHE SER LEU TYR ALA
SEQRES 27 A 473 LYS GLU ASP THR VAL LEU GLY GLY GLU TYR PRO LEU GLU
SEQRES 28 A 473 LYS GLY ASP GLU LEU MET VAL LEU ILE PRO GLN LEU HIS
SEQRES 29 A 473 ARG ASP LYS THR ILE TRP GLY ASP ASP VAL GLU GLU PHE
SEQRES 30 A 473 ARG PRO GLU ARG PHE GLU ASN PRO SER ALA ILE PRO GLN
SEQRES 31 A 473 HIS ALA PHE LYS PRO PHE GLY ASN GLY GLN ARG ALA CYS
SEQRES 32 A 473 ILE GLY GLN GLN PHE ALA LEU HIS GLU ALA THR LEU VAL
SEQRES 33 A 473 LEU GLY MET MET LEU LYS HIS PHE ASP PHE GLU ASP HIS
SEQRES 34 A 473 THR ASN TYR GLU LEU ASP ILE LYS GLU THR LEU THR LEU
SEQRES 35 A 473 LYS PRO GLU GLY PHE VAL VAL LYS ALA LYS SER LYS LYS
SEQRES 36 A 473 ILE PRO LEU GLY GLY ILE PRO SER PRO SER THR GLU GLN
SEQRES 37 A 473 SER ALA LYS LYS VAL
SEQRES 1 B 473 GLY ALA MET THR ILE LYS GLU MET PRO GLN PRO LYS THR
SEQRES 2 B 473 PHE GLY GLU LEU LYS ASN LEU PRO LEU LEU ASN THR ASP
SEQRES 3 B 473 LYS PRO VAL GLN ALA LEU MET LYS ILE ALA ASP GLU LEU
SEQRES 4 B 473 GLY GLU ILE PHE LYS PHE GLU ALA PRO GLY ARG VAL THR
SEQRES 5 B 473 ARG TYR LEU SER SER GLN ARG LEU ILE LYS GLU ALA CYS
SEQRES 6 B 473 ASP GLU SER ARG PHE ASP LYS ASN LEU SER GLN ALA LEU
SEQRES 7 B 473 LYS PHE VAL ARG ASP PHE ALA GLY ASP GLY LEU PHE THR
SEQRES 8 B 473 SER TRP THR HIS GLU LYS ASN TRP LYS LYS ALA HIS ASN
SEQRES 9 B 473 ILE LEU LEU PRO SER PHE SER GLN GLN ALA MET LYS GLY
SEQRES 10 B 473 TYR HIS ALA MET MET VAL ASP ILE ALA VAL GLN LEU VAL
SEQRES 11 B 473 GLN LYS TRP GLU ARG LEU ASN ALA ASP GLU HIS ILE GLU
SEQRES 12 B 473 VAL PRO GLU ASP MET THR ARG LEU THR LEU ASP THR ILE
SEQRES 13 B 473 GLY LEU CYS GLY PHE ASN TYR ARG PHE ASN SER PHE TYR
SEQRES 14 B 473 ARG ASP GLN PRO HIS PRO PHE ILE THR SER MET VAL ARG
SEQRES 15 B 473 ALA LEU ASP GLU ALA MET ASN LYS LEU GLN ARG ALA ASN
SEQRES 16 B 473 PRO ASP ASP PRO ALA TYR ASP GLU ASN LYS ARG GLN PHE
SEQRES 17 B 473 GLN GLU ASP ILE LYS VAL MET ASN ASP LEU VAL ASP LYS
SEQRES 18 B 473 ILE ILE ALA ASP ARG LYS ALA SER GLY GLU GLN SER ASP
SEQRES 19 B 473 ASP LEU LEU THR HIS MET LEU ASN GLY LYS ASP PRO GLU
SEQRES 20 B 473 THR GLY GLU PRO LEU ASP ASP GLU ASN ILE ARG TYR GLN
SEQRES 21 B 473 ILE ILE THR PHE LEU ILE ALA GLY HIS GLU THR THR SER
SEQRES 22 B 473 GLY LEU LEU SER PHE ALA LEU TYR PHE LEU VAL LYS ASN
SEQRES 23 B 473 PRO HIS VAL LEU GLN LYS ALA ALA GLU GLU ALA ALA ARG
SEQRES 24 B 473 VAL LEU VAL ASP PRO VAL PRO SER TYR LYS GLN VAL LYS
SEQRES 25 B 473 GLN LEU LYS TYR VAL GLY MET VAL LEU ASN GLU ALA LEU
SEQRES 26 B 473 ARG LEU TRP PRO THR SER PRO ALA PHE SER LEU TYR ALA
SEQRES 27 B 473 LYS GLU ASP THR VAL LEU GLY GLY GLU TYR PRO LEU GLU
SEQRES 28 B 473 LYS GLY ASP GLU LEU MET VAL LEU ILE PRO GLN LEU HIS
SEQRES 29 B 473 ARG ASP LYS THR ILE TRP GLY ASP ASP VAL GLU GLU PHE
SEQRES 30 B 473 ARG PRO GLU ARG PHE GLU ASN PRO SER ALA ILE PRO GLN
SEQRES 31 B 473 HIS ALA PHE LYS PRO PHE GLY ASN GLY GLN ARG ALA CYS
SEQRES 32 B 473 ILE GLY GLN GLN PHE ALA LEU HIS GLU ALA THR LEU VAL
SEQRES 33 B 473 LEU GLY MET MET LEU LYS HIS PHE ASP PHE GLU ASP HIS
SEQRES 34 B 473 THR ASN TYR GLU LEU ASP ILE LYS GLU THR LEU THR LEU
SEQRES 35 B 473 LYS PRO GLU GLY PHE VAL VAL LYS ALA LYS SER LYS LYS
SEQRES 36 B 473 ILE PRO LEU GLY GLY ILE PRO SER PRO SER THR GLU GLN
SEQRES 37 B 473 SER ALA LYS LYS VAL
HET HEM A 471 43
HET MES A1491 12
HET GOL A1471 6
HET GOL A1472 6
HET GOL A1473 6
HET GOL A1476 6
HET GOL A1481 6
HET GOL A1482 6
HET GOL A1484 6
HET GOL A1485 6
HET GOL A1486 6
HET GOL A1487 6
HET GOL A1489 6
HET HEM B 471 43
HET MES B1490 12
HET GOL B1470 6
HET GOL B1474 6
HET GOL B1475 6
HET GOL B1477 6
HET GOL B1478 6
HET GOL B1479 6
HET GOL B1480 6
HET GOL B1483 6
HET GOL B1488 6
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETNAM GOL GLYCEROL
HETSYN HEM HEME
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 4 MES 2(C6 H13 N O4 S)
FORMUL 5 GOL 20(C3 H8 O3)
FORMUL 27 HOH *830(H2 O)
HELIX 1 1 PHE A 11 LYS A 15 5 5
HELIX 2 2 ASN A 16 ASN A 21 5 6
HELIX 3 3 LYS A 24 GLY A 37 1 14
HELIX 4 4 SER A 54 CYS A 62 1 9
HELIX 5 5 SER A 72 GLY A 83 1 12
HELIX 6 6 GLU A 93 LEU A 104 1 12
HELIX 7 7 PRO A 105 SER A 108 5 4
HELIX 8 8 GLN A 109 GLN A 110 5 2
HELIX 9 9 ALA A 111 ARG A 132 1 22
HELIX 10 10 VAL A 141 ASN A 159 1 19
HELIX 11 11 ASN A 163 ARG A 167 5 5
HELIX 12 12 HIS A 171 LYS A 187 1 17
HELIX 13 13 LEU A 188 ARG A 190 5 3
HELIX 14 14 ASP A 195 ALA A 197 5 3
HELIX 15 15 TYR A 198 GLY A 227 1 30
HELIX 16 16 ASP A 232 GLY A 240 1 9
HELIX 17 17 ASP A 250 ASN A 283 1 34
HELIX 18 18 ASN A 283 LEU A 298 1 16
HELIX 19 19 SER A 304 LEU A 311 1 8
HELIX 20 20 LEU A 311 TRP A 325 1 15
HELIX 21 21 ILE A 357 HIS A 361 1 5
HELIX 22 22 ASP A 363 GLY A 368 1 6
HELIX 23 23 ARG A 375 GLU A 380 5 6
HELIX 24 24 ASN A 381 ILE A 385 5 5
HELIX 25 25 ASN A 395 ALA A 399 5 5
HELIX 26 26 GLY A 402 HIS A 420 1 19
HELIX 27 27 PHE B 11 LYS B 15 5 5
HELIX 28 28 ASN B 16 ASN B 21 5 6
HELIX 29 29 LYS B 24 GLY B 37 1 14
HELIX 30 30 SER B 54 CYS B 62 1 9
HELIX 31 31 SER B 72 GLY B 83 1 12
HELIX 32 32 GLU B 93 LEU B 104 1 12
HELIX 33 33 PRO B 105 SER B 108 5 4
HELIX 34 34 GLN B 109 GLN B 110 5 2
HELIX 35 35 ALA B 111 ARG B 132 1 22
HELIX 36 36 VAL B 141 ASN B 159 1 19
HELIX 37 37 ASN B 163 ARG B 167 5 5
HELIX 38 38 HIS B 171 LYS B 187 1 17
HELIX 39 39 LEU B 188 ARG B 190 5 3
HELIX 40 40 ASP B 195 ALA B 197 5 3
HELIX 41 41 TYR B 198 GLY B 227 1 30
HELIX 42 42 ASP B 232 GLY B 240 1 9
HELIX 43 43 ASP B 250 ASN B 283 1 34
HELIX 44 44 ASN B 283 LEU B 298 1 16
HELIX 45 45 SER B 304 GLN B 310 1 7
HELIX 46 46 LEU B 311 TRP B 325 1 15
HELIX 47 47 ILE B 357 HIS B 361 1 5
HELIX 48 48 ASP B 363 GLY B 368 1 6
HELIX 49 49 ARG B 375 GLU B 380 5 6
HELIX 50 50 ASN B 381 ILE B 385 5 5
HELIX 51 51 ASN B 395 ALA B 399 5 5
HELIX 52 52 GLY B 402 HIS B 420 1 19
SHEET 1 A 5 ILE A 39 ALA A 44 0
SHEET 2 A 5 ARG A 47 LEU A 52 -1 O THR A 49 N PHE A 42
SHEET 3 A 5 GLU A 352 LEU A 356 1 O MET A 354 N LEU A 52
SHEET 4 A 5 ALA A 330 ALA A 335 -1 N PHE A 331 O VAL A 355
SHEET 5 A 5 PHE A 67 LYS A 69 -1 N ASP A 68 O TYR A 334
SHEET 1 B 3 ILE A 139 GLU A 140 0
SHEET 2 B 3 VAL A 445 SER A 450 -1 O VAL A 446 N ILE A 139
SHEET 3 B 3 PHE A 421 GLU A 424 -1 N GLU A 424 O LYS A 447
SHEET 1 C 2 THR A 339 LEU A 341 0
SHEET 2 C 2 TYR A 345 LEU A 347 -1 O LEU A 347 N THR A 339
SHEET 1 D 2 ILE A 433 GLU A 435 0
SHEET 2 D 2 LEU A 439 PRO A 441 -1 O LYS A 440 N LYS A 434
SHEET 1 E 5 ILE B 39 ALA B 44 0
SHEET 2 E 5 ARG B 47 LEU B 52 -1 O TYR B 51 N PHE B 40
SHEET 3 E 5 GLU B 352 LEU B 356 1 O MET B 354 N LEU B 52
SHEET 4 E 5 ALA B 330 ALA B 335 -1 N PHE B 331 O VAL B 355
SHEET 5 E 5 PHE B 67 LYS B 69 -1 N ASP B 68 O TYR B 334
SHEET 1 F 3 ILE B 139 GLU B 140 0
SHEET 2 F 3 VAL B 445 SER B 450 -1 O VAL B 446 N ILE B 139
SHEET 3 F 3 PHE B 421 GLU B 424 -1 N GLU B 424 O LYS B 447
SHEET 1 G 2 THR B 339 LEU B 341 0
SHEET 2 G 2 TYR B 345 LEU B 347 -1 O LEU B 347 N THR B 339
SHEET 1 H 2 ILE B 433 GLU B 435 0
SHEET 2 H 2 LEU B 439 PRO B 441 -1 O LYS B 440 N LYS B 434
LINK SG CYS A 400 FE HEM A 471 1555 1555 2.34
LINK FE HEM A 471 O AHOH A1867 1555 1555 2.33
LINK SG CYS B 400 FE HEM B 471 1555 1555 2.35
LINK FE HEM B 471 O AHOH B1895 1555 1555 2.43
SITE 1 AC1 26 LYS A 69 LEU A 86 PHE A 87 TRP A 96
SITE 2 AC1 26 PHE A 107 ALA A 264 GLY A 265 THR A 268
SITE 3 AC1 26 THR A 269 LEU A 272 THR A 327 PHE A 331
SITE 4 AC1 26 PRO A 392 PHE A 393 GLY A 394 ARG A 398
SITE 5 AC1 26 ALA A 399 CYS A 400 ILE A 401 HOH A1494
SITE 6 AC1 26 HOH A1499 HOH A1502 HOH A1504 HOH A1517
SITE 7 AC1 26 HOH A1796 HOH A1867
SITE 1 AC2 27 LYS B 69 LEU B 86 PHE B 87 TRP B 96
SITE 2 AC2 27 PHE B 107 ALA B 264 GLY B 265 THR B 268
SITE 3 AC2 27 THR B 269 LEU B 272 THR B 327 PHE B 331
SITE 4 AC2 27 PRO B 392 PHE B 393 GLY B 394 ARG B 398
SITE 5 AC2 27 ALA B 399 CYS B 400 ILE B 401 ALA B 406
SITE 6 AC2 27 HOH B1493 HOH B1494 HOH B1496 HOH B1499
SITE 7 AC2 27 HOH B1500 HOH B1540 HOH B1895
SITE 1 AC3 5 HIS B 285 ARG B 375 GLU B 377 HOH B1546
SITE 2 AC3 5 HOH B1871
SITE 1 AC4 8 ILE A 366 TRP A 367 ARG A 375 GLU A 377
SITE 2 AC4 8 ARG A 378 ALA A 384 ILE A 385 PRO A 386
SITE 1 AC5 4 GLN A 128 ARG A 132 ASP B 121 ARG B 161
SITE 1 AC6 4 ASP A 338 GLU A 348 HOH A1702 HOH A1810
SITE 1 AC7 8 TYR A 166 ARG A 167 HOH A1550 LYS B 129
SITE 2 AC7 8 LEU B 133 ASP B 168 HOH B1645 HOH B1718
SITE 1 AC8 3 ARG A 79 HOH A1790 HOH A1856
SITE 1 AC9 9 PHE B 390 LYS B 391 PRO B 392 PHE B 393
SITE 2 AC9 9 GLY B 394 GLN B 403 GOL B1475 HOH B1559
SITE 3 AC9 9 HOH B1835
SITE 1 BC1 6 LYS B 391 GLY B 394 ASN B 395 GLY B 396
SITE 2 BC1 6 GLN B 403 GOL B1474
SITE 1 BC2 5 GLY B 83 ASP B 84 GLU B 252 TYR B 256
SITE 2 BC2 5 HOH B1678
SITE 1 BC3 4 GLU B 247 LYS B 282 HOH B1676 HOH B1879
SITE 1 BC4 4 ARG A 132 ASP B 121 VAL B 124 HOH B1668
SITE 1 BC5 5 HIS A 285 LYS A 289 GLU A 377 HOH A1690
SITE 2 BC5 5 HOH A1853
SITE 1 BC6 5 LYS A 289 TYR A 313 MET A 316 GLU A 380
SITE 2 BC6 5 HOH A1731
SITE 1 BC7 3 GLY B 240 LYS B 241 HOH B1908
SITE 1 BC8 4 MET A 5 LYS A 41 ARG A 50 HOH A1597
SITE 1 BC9 4 SER A 108 GOL A1487 HOH A1521 HOH A1528
SITE 1 CC1 9 TRP A 130 GLU A 131 LEU A 133 ASN A 134
SITE 2 CC1 9 ALA A 448 LYS A 449 SER A 450 HOH A1586
SITE 3 CC1 9 HOH A1676
SITE 1 CC2 7 HIS A 100 GLY A 396 GLN A 397 GOL A1485
SITE 2 CC2 7 HOH A1567 HOH A1658 HOH A1735
SITE 1 CC3 5 VAL B 302 PRO B 303 SER B 304 HOH B1622
SITE 2 CC3 5 HOH B1868
SITE 1 CC4 4 PRO A 25 VAL A 26 LEU A 29 TYR A 51
CRYST1 58.827 153.209 61.583 90.00 94.33 90.00 P 1 21 1 4
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 0.016999 0.000000 0.001287 0.00000
SCALE2 0.000000 0.006527 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016285 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
