HEADER OXIDOREDUCTASE 11-AUG-05 2ANZ
TITLE CYTOCHROME C PEROXIDASE IN COMPLEX WITH 2,6-DIAMINOPYRIDINE
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;
COMPND 7 MUTATION: 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;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PT7CCP
KEYWDS OXIDOREDUCTASE, PEROXIDASE, MODEL BINDING SITE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.BRENK,S.W.VETTER,S.E.BOYCE,D.B.GOODIN,B.K.SHOICHET
REVDAT 4 23-AUG-23 2ANZ 1 REMARK
REVDAT 3 20-OCT-21 2ANZ 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 2ANZ 1 VERSN
REVDAT 1 11-APR-06 2ANZ 0
JRNL AUTH R.BRENK,S.W.VETTER,S.E.BOYCE,D.B.GOODIN,B.K.SHOICHET
JRNL TITL PROBING MOLECULAR DOCKING IN A CHARGED MODEL BINDING SITE.
JRNL REF J.MOL.BIOL. V. 357 1449 2006
JRNL REFN ISSN 0022-2836
JRNL PMID 16490206
JRNL DOI 10.1016/J.JMB.2006.01.034
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.33
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 262020.120
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 92.6
REMARK 3 NUMBER OF REFLECTIONS : 39296
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) : 0.192
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1978
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.86
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5963
REMARK 3 BIN R VALUE (WORKING SET) : 0.2590
REMARK 3 BIN FREE R VALUE : 0.2730
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 321
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.015
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2328
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 51
REMARK 3 SOLVENT ATOMS : 317
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.76000
REMARK 3 B22 (A**2) : 3.12000
REMARK 3 B33 (A**2) : -3.87000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.19
REMARK 3 ESD FROM SIGMAA (A) : 0.14
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) : 0.21
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.15
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.210
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 0.970 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.390 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.680 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.330 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.38
REMARK 3 BSOL : 59.00
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 : HEME.PAR
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : 26D.PAR
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : HEME.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : 26D.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2ANZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-AUG-05.
REMARK 100 THE DEPOSITION ID IS D_1000034113.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-MAY-05
REMARK 200 TEMPERATURE (KELVIN) : 200.0
REMARK 200 PH : 6.0
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) : 1.5418
REMARK 200 MONOCHROMATOR : YALE MIRRORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39610
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.81
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.39500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.500
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: 1AC4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MES, MPD, PH 6.0, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 310K
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 25.42000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 53.54000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.08500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 53.54000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.42000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.08500
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 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 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 LYS A 2
REMARK 465 THR A 3
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 GLU A 17 CG CD OE1 OE2
REMARK 470 LYS A 183 CG CD CE NZ
REMARK 470 LYS A 278 CG CD CE NZ
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 TYR A 39 OH
REMARK 480 LYS A 74 CD CE NZ
REMARK 480 LYS A 90 CD CE NZ
REMARK 480 LYS A 97 CE NZ
REMARK 480 LYS A 212 NZ
REMARK 480 LYS A 226 CG CD CE NZ
REMARK 480 LYS A 264 CE NZ
REMARK 480 LYS A 287 CE NZ
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 12 112.67 -36.21
REMARK 500 ASP A 148 30.99 -99.54
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 400 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 175 NE2
REMARK 620 2 HEM A 400 NA 95.5
REMARK 620 3 HEM A 400 NB 82.8 87.5
REMARK 620 4 HEM A 400 NC 90.4 173.9 91.7
REMARK 620 5 HEM A 400 ND 104.6 87.1 171.3 92.8
REMARK 620 6 HOH A1415 O 168.4 83.5 85.6 90.3 86.9
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 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 26D A 500
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AA4 RELATED DB: PDB
REMARK 900 APO-STRUCTURE
DBREF 2ANZ A 4 294 UNP P00431 CCPR_YEAST 71 361
SEQADV 2ANZ MET A 1 UNP P00431 CLONING ARTIFACT
SEQADV 2ANZ LYS A 2 UNP P00431 CLONING ARTIFACT
SEQADV 2ANZ THR A 3 UNP P00431 CLONING ARTIFACT
SEQADV 2ANZ ILE A 53 UNP P00431 THR 120 CONFLICT
SEQADV 2ANZ GLY A 152 UNP P00431 ASP 219 CONFLICT
SEQADV 2ANZ GLY A 191 UNP P00431 TRP 258 ENGINEERED MUTATION
SEQADV 2ANZ ASP A 272 UNP P00431 ASN 339 CONFLICT
SEQRES 1 A 294 MET LYS THR 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 ILE 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 GLY 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 GLY 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 ASP 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 HEM A 400 43
HET 26D A 500 8
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM 26D PYRIDINE-2,6-DIAMINE
HETSYN HEM HEME
FORMUL 2 HEM C34 H32 FE N4 O4
FORMUL 3 26D C5 H7 N3
FORMUL 4 HOH *317(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 GLY A 84 5 6
HELIX 7 7 LEU A 85 PHE A 99 1 15
HELIX 8 8 SER A 103 MET A 119 1 17
HELIX 9 9 PRO A 134 THR A 138 5 5
HELIX 10 10 ASP A 150 ARG A 160 1 11
HELIX 11 11 ASN A 164 GLY A 173 1 10
HELIX 12 12 ALA A 174 LEU A 177 5 4
HELIX 13 13 HIS A 181 GLY A 186 1 6
HELIX 14 14 ASN A 200 GLU A 209 1 10
HELIX 15 15 LEU A 232 ASP A 241 1 10
HELIX 16 16 ASP A 241 ASN A 253 1 13
HELIX 17 17 ASP A 254 ASP A 272 1 19
HELIX 18 18 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 LYS A 212 LYS A 215 0
SHEET 2 C 3 GLU A 221 ASP A 224 -1 O GLN A 222 N GLU A 214
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 HEM A 400 1555 1555 2.16
LINK FE HEM A 400 O HOH A1415 1555 1555 2.25
SITE 1 AC1 25 PRO A 44 VAL A 45 ARG A 48 TRP A 51
SITE 2 AC1 25 PRO A 145 ASP A 146 ALA A 147 LEU A 171
SITE 3 AC1 25 MET A 172 ALA A 174 HIS A 175 LEU A 177
SITE 4 AC1 25 GLY A 178 LYS A 179 THR A 180 HIS A 181
SITE 5 AC1 25 ASN A 184 SER A 185 LEU A 232 THR A 234
SITE 6 AC1 25 26D A 500 HOH A1121 HOH A1136 HOH A1161
SITE 7 AC1 25 HOH A1415
SITE 1 AC2 10 HIS A 175 LEU A 177 GLY A 178 LYS A 179
SITE 2 AC2 10 THR A 180 GLY A 191 MET A 230 ASP A 235
SITE 3 AC2 10 HEM A 400 HOH A1000
CRYST1 50.840 76.170 107.080 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 0.019670 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013129 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009339 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
