HEADER OXIDOREDUCTASE 28-JAN-04 1S73
TITLE CRYSTAL STRUCTURE OF MESOPONE CYTOCHROME C PEROXIDASE (R-ISOMER)
TITLE 2 [MPCCP-R]
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C PEROXIDASE, MITOCHONDRIAL;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CCP;
COMPND 5 EC: 1.11.1.5;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: CCP1, CCP, CPO, YKR066C;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) STAR;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: T7 PROMOTER;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: POULOS VECTOR
KEYWDS BIFUNCTIONAL CATALYST, PROXIMAL LOOP, TRP191 RADICAL, MESOPORPHYRIN,
KEYWDS 2 NITRITE REDUCTASE, CYCTOCHROME C PEROXIDASE, CYTOCHORME OXIDASE,
KEYWDS 3 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.BHASKAR,C.E.IMMOOS,F.SULC,M.S.CHOEN,P.J.FARMER,T.L.POULOS
REVDAT 4 03-APR-24 1S73 1 REMARK
REVDAT 3 14-FEB-24 1S73 1 REMARK LINK
REVDAT 2 24-FEB-09 1S73 1 VERSN
REVDAT 1 14-JUN-05 1S73 0
JRNL AUTH B.BHASKAR,C.E.IMMOOS,F.SULC,M.S.CHOEN,P.J.FARMER,T.L.POULOS
JRNL TITL CRYSTAL STRUCTURES OF REDUCED, RESTING AND NO-BOUND STATES
JRNL TITL 2 OF MESOPONE CYTOCHORME C PEROXIDASE (MPCCP) (R-ISOMER)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.53 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) : 1.53
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
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) (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 62085
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) : 0.183
REMARK 3 FREE R VALUE : 0.202
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 3095
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) : 1.53
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.58
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 7.69
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3846
REMARK 3 BIN FREE R VALUE : 0.3908
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 245
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 : 2374
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 44
REMARK 3 SOLVENT ATOMS : 706
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.18
REMARK 3 ESD FROM SIGMAA (A) : 0.11
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) : 0.20
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1S73 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-FEB-04.
REMARK 100 THE DEPOSITION ID IS D_1000021449.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-SEP-02
REMARK 200 TEMPERATURE (KELVIN) : 115
REMARK 200 PH : 6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 62259
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.530
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 (%) : 97.2
REMARK 200 DATA REDUNDANCY : 13.10
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : 0.05200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 50.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.53
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.56
REMARK 200 COMPLETENESS FOR SHELL (%) : 73.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.75
REMARK 200 R MERGE FOR SHELL (I) : 0.17100
REMARK 200 R SYM FOR SHELL (I) : 0.14600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.830
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: WTCCP - ULTRA-HIGH RESOLUTION STRUCTURE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS-PHOSPHATE BUFFER, 2-METHYL-2,4
REMARK 280 -PENTANEDIOL, PH 6, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 277K
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 53.49000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 25.57750
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.07450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 25.57750
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 53.49000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.07450
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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 300 REMARK: HELICAL BUNDLE PROTEIN WITH A DISTINCT DISTAL AND PROXIMAL
REMARK 300 DOMAINS SEPARATED BY HEME. PROXIMAL HEME DOMAIN ALSO COMNTAINS THE
REMARK 300 LOOP COMPRISING RESIDUES (189-195) WHICH FORM THE LOOP. TRP191 OF
REMARK 300 THIS PROXIMAL LOOP FORMS THE RADICAL DURING CATALYSIS AND ELECTRON
REMARK 300 TRANSFER.
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 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 LYS A 123 CD - CE - NZ ANGL. DEV. = 14.2 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 12 113.07 -36.87
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 FMI A 296 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 175 NE2
REMARK 620 2 FMI A 296 NA 99.4
REMARK 620 3 FMI A 296 NB 95.7 88.8
REMARK 620 4 FMI A 296 NC 93.9 166.7 91.2
REMARK 620 5 FMI A 296 ND 95.7 89.0 168.6 88.4
REMARK 620 6 HOH A 468 O 178.8 80.3 83.1 86.5 85.5
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 FMI A 296
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2CYP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF WTCCP FROM SACCHAROMYCES CEREVISIAE
REMARK 900 RELATED ID: 1KOK RELATED DB: PDB
REMARK 900 MESOPONE CYTOCHROME C PEROXIDASE (S-ISOMER): FUNCTIONAL MODEL OF
REMARK 900 HEME OXYGENATED OXIDASES
REMARK 900 RELATED ID: 1SBM RELATED DB: PDB
REMARK 900 FERROUS STATE OF (4-MESOPORPHYRINONE)- R-ISOMER INCORPORATED INTO
REMARK 900 APO-WTCCP
REMARK 900 RELATED ID: 1SDQ RELATED DB: PDB
REMARK 900 NO BOUND FERROUS STATE OF 4-MESOPORPHYRINONE (R-ISOMER)
REMARK 900 INCORPORATED INTO APO-WTCCP
DBREF 1S73 A 1 294 UNP P00431 CCPR_YEAST 68 361
SEQRES 1 A 294 THR THR PRO LEU VAL HIS VAL ALA SER VAL GLU LYS GLY
SEQRES 2 A 294 ARG SER TYR GLU ASP PHE GLN LYS VAL TYR ASN ALA ILE
SEQRES 3 A 294 ALA LEU LYS LEU ARG GLU ASP ASP GLU TYR ASP ASN TYR
SEQRES 4 A 294 ILE GLY TYR GLY PRO VAL LEU VAL ARG LEU ALA TRP HIS
SEQRES 5 A 294 THR SER GLY THR TRP ASP LYS HIS ASP ASN THR GLY GLY
SEQRES 6 A 294 SER TYR GLY GLY THR TYR ARG PHE LYS LYS GLU PHE ASN
SEQRES 7 A 294 ASP PRO SER ASN ALA GLY LEU GLN ASN GLY PHE LYS PHE
SEQRES 8 A 294 LEU GLU PRO ILE HIS LYS GLU PHE PRO TRP ILE SER SER
SEQRES 9 A 294 GLY ASP LEU PHE SER LEU GLY GLY VAL THR ALA VAL GLN
SEQRES 10 A 294 GLU MET GLN GLY PRO LYS ILE PRO TRP ARG CYS GLY ARG
SEQRES 11 A 294 VAL ASP THR PRO GLU ASP THR THR PRO ASP ASN GLY ARG
SEQRES 12 A 294 LEU PRO ASP ALA ASP LYS ASP ALA ASP TYR VAL ARG THR
SEQRES 13 A 294 PHE PHE GLN ARG LEU ASN MET ASN ASP ARG GLU VAL VAL
SEQRES 14 A 294 ALA LEU MET GLY ALA HIS ALA LEU GLY LYS THR HIS LEU
SEQRES 15 A 294 LYS ASN SER GLY TYR GLU GLY PRO TRP GLY ALA ALA ASN
SEQRES 16 A 294 ASN VAL PHE THR ASN GLU PHE TYR LEU ASN LEU LEU ASN
SEQRES 17 A 294 GLU ASP TRP LYS LEU GLU LYS ASN ASP ALA ASN ASN GLU
SEQRES 18 A 294 GLN TRP ASP SER LYS SER GLY TYR MET MET LEU PRO THR
SEQRES 19 A 294 ASP TYR SER LEU ILE GLN ASP PRO LYS TYR LEU SER ILE
SEQRES 20 A 294 VAL LYS GLU TYR ALA ASN ASP GLN ASP LYS PHE PHE LYS
SEQRES 21 A 294 ASP PHE SER LYS ALA PHE GLU LYS LEU LEU GLU ASN GLY
SEQRES 22 A 294 ILE THR PHE PRO LYS ASP ALA PRO SER PRO PHE ILE PHE
SEQRES 23 A 294 LYS THR LEU GLU GLU GLN GLY LEU
HET FMI A 296 44
HETNAM FMI FE-(4-MESOPORPHYRINONE)-R-ISOMER
FORMUL 2 FMI C34 H36 FE N4 O5 2+
FORMUL 3 HOH *706(H2 O)
HELIX 1 1 SER A 15 ASP A 33 1 19
HELIX 2 2 GLU A 35 ILE A 40 1 6
HELIX 3 3 TYR A 42 GLY A 55 1 14
HELIX 4 4 GLY A 69 ARG A 72 5 4
HELIX 5 5 PHE A 73 ASN A 78 1 6
HELIX 6 6 ASP A 79 ALA A 83 5 5
HELIX 7 7 GLY A 84 GLY A 84 5 1
HELIX 8 8 LEU A 85 PHE A 99 1 15
HELIX 9 9 SER A 103 MET A 119 1 17
HELIX 10 10 PRO A 134 THR A 138 5 5
HELIX 11 11 ASP A 150 ARG A 160 1 11
HELIX 12 12 ASN A 164 GLY A 173 1 10
HELIX 13 13 ALA A 174 LEU A 177 5 4
HELIX 14 14 HIS A 181 GLY A 186 1 6
HELIX 15 15 ASN A 200 GLU A 209 1 10
HELIX 16 16 LEU A 232 ASP A 241 1 10
HELIX 17 17 ASP A 241 ASN A 253 1 13
HELIX 18 18 ASP A 254 ASN A 272 1 19
HELIX 19 19 THR A 288 GLY A 293 1 6
SHEET 1 A 2 HIS A 6 VAL A 7 0
SHEET 2 A 2 ILE A 274 THR A 275 1 O THR A 275 N HIS A 6
SHEET 1 B 2 LYS A 179 THR A 180 0
SHEET 2 B 2 GLY A 189 PRO A 190 -1 O GLY A 189 N THR A 180
SHEET 1 C 3 TRP A 211 LYS A 215 0
SHEET 2 C 3 GLU A 221 SER A 225 -1 O ASP A 224 N LYS A 212
SHEET 3 C 3 MET A 230 MET A 231 -1 O MET A 231 N TRP A 223
LINK NE2 HIS A 175 FE FMI A 296 1555 1555 2.09
LINK FE FMI A 296 O HOH A 468 1555 1555 2.18
SITE 1 AC1 23 PRO A 44 VAL A 45 TRP A 51 PRO A 145
SITE 2 AC1 23 LEU A 171 MET A 172 ALA A 174 HIS A 175
SITE 3 AC1 23 LEU A 177 GLY A 178 LYS A 179 THR A 180
SITE 4 AC1 23 HIS A 181 ASN A 184 SER A 185 TRP A 191
SITE 5 AC1 23 LEU A 232 THR A 234 HOH A 330 HOH A 343
SITE 6 AC1 23 HOH A 358 HOH A 468 HOH A 797
CRYST1 106.980 76.149 51.155 90.00 90.00 90.00 P 21 21 21 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 0.009348 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013132 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019548 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
