HEADER OXIDOREDUCTASE 31-MAR-05 1Z8Q
TITLE FERROUS DIOXYGEN COMPLEX OF THE A245T CYTOCHROME P450ERYF
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 6-DEOXYERYTHRONOLIDE B HYDROXYLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: 6-DEB HYDROXYLASE, ERYTHOMYCIN A BIOSYNTHESIS HYDROLASE,
COMPND 5 CYTOCHROME P450 107A1, CYPCVIIA1, P450ERYF;
COMPND 6 EC: 1.-.-.-;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROPOLYSPORA ERYTHRAEA;
SOURCE 3 ORGANISM_TAXID: 1836;
SOURCE 4 GENE: ERYF, CYP107A1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HEME, CYP, P450, ERYTHROMYCIN, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.NAGANO,J.R.CUPP-VICKERY,T.L.POULOS
REVDAT 5 23-AUG-23 1Z8Q 1 REMARK
REVDAT 4 20-OCT-21 1Z8Q 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1Z8Q 1 VERSN
REVDAT 2 28-JUN-05 1Z8Q 1 JRNL
REVDAT 1 12-APR-05 1Z8Q 0
JRNL AUTH S.NAGANO,J.R.CUPP-VICKERY,T.L.POULOS
JRNL TITL CRYSTAL STRUCTURES OF THE FERROUS DIOXYGEN COMPLEX OF
JRNL TITL 2 WILD-TYPE CYTOCHROME P450ERYF AND ITS MUTANTS, A245S AND
JRNL TITL 3 A245T: INVESTIGATION OF THE PROTON TRANSFER SYSTEM IN
JRNL TITL 4 P450ERYF.
JRNL REF J.BIOL.CHEM. V. 280 22102 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 15824115
JRNL DOI 10.1074/JBC.M501732200
REMARK 2
REMARK 2 RESOLUTION. 2.00 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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.05
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 161821.860
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 89.3
REMARK 3 NUMBER OF REFLECTIONS : 25476
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) : 0.201
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1237
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.03
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 79.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1050
REMARK 3 BIN R VALUE (WORKING SET) : 0.2460
REMARK 3 BIN FREE R VALUE : 0.3480
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.50
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 50
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.049
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3177
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 72
REMARK 3 SOLVENT ATOMS : 173
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.89000
REMARK 3 B22 (A**2) : -2.20000
REMARK 3 B33 (A**2) : 3.10000
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) : 0.23
REMARK 3 ESD FROM SIGMAA (A) : 0.15
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) : 0.29
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.23
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.900
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) : 1.990 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.680 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.190 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.060 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 39.22
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 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : HETERO.PARAM
REMARK 3 PARAMETER FILE 4 : DEB.PARAM
REMARK 3 PARAMETER FILE 5 : ION.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : HETERO.TOP
REMARK 3 TOPOLOGY FILE 4 : DEB.TOP
REMARK 3 TOPOLOGY FILE 5 : ION.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1Z8Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-APR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032439.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-JUN-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.92
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25476
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 36.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.3
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1JIO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS, SODIUM ACETATE, PEG 4000 , PH
REMARK 280 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 288K
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 26.97500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 48.46500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.28000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 48.46500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.97500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.28000
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 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 HIS A 13 -0.15 -143.11
REMARK 500 PHE A 144 -67.22 -153.90
REMARK 500 MET A 177 69.43 -112.89
REMARK 500 SER A 272 9.20 -56.30
REMARK 500 VAL A 334 -8.28 -56.37
REMARK 500 CYS A 351 128.33 -38.96
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 410 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 351 SG
REMARK 620 2 HEM A 410 NA 96.6
REMARK 620 3 HEM A 410 NB 83.1 90.5
REMARK 620 4 HEM A 410 NC 88.1 175.2 89.2
REMARK 620 5 HEM A 410 ND 99.4 89.7 177.4 90.3
REMARK 620 6 OXY A 417 O1 169.2 88.4 87.3 86.8 90.1
REMARK 620 7 OXY A 417 O2 150.4 104.4 76.1 70.9 101.3 19.6
REMARK 620 N 1 2 3 4 5 6
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 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OXY A 417
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DEB A 420
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1Z8O RELATED DB: PDB
REMARK 900 RELATED ID: 1Z8P RELATED DB: PDB
DBREF 1Z8Q A 1 404 UNP Q00441 CPXJ_SACER 1 404
SEQADV 1Z8Q THR A 245 UNP Q00441 ALA 245 ENGINEERED MUTATION
SEQRES 1 A 404 MET THR THR VAL PRO ASP LEU GLU SER ASP SER PHE HIS
SEQRES 2 A 404 VAL ASP TRP TYR ARG THR TYR ALA GLU LEU ARG GLU THR
SEQRES 3 A 404 ALA PRO VAL THR PRO VAL ARG PHE LEU GLY GLN ASP ALA
SEQRES 4 A 404 TRP LEU VAL THR GLY TYR ASP GLU ALA LYS ALA ALA LEU
SEQRES 5 A 404 SER ASP LEU ARG LEU SER SER ASP PRO LYS LYS LYS TYR
SEQRES 6 A 404 PRO GLY VAL GLU VAL GLU PHE PRO ALA TYR LEU GLY PHE
SEQRES 7 A 404 PRO GLU ASP VAL ARG ASN TYR PHE ALA THR ASN MET GLY
SEQRES 8 A 404 THR SER ASP PRO PRO THR HIS THR ARG LEU ARG LYS LEU
SEQRES 9 A 404 VAL SER GLN GLU PHE THR VAL ARG ARG VAL GLU ALA MET
SEQRES 10 A 404 ARG PRO ARG VAL GLU GLN ILE THR ALA GLU LEU LEU ASP
SEQRES 11 A 404 GLU VAL GLY ASP SER GLY VAL VAL ASP ILE VAL ASP ARG
SEQRES 12 A 404 PHE ALA HIS PRO LEU PRO ILE LYS VAL ILE CYS GLU LEU
SEQRES 13 A 404 LEU GLY VAL ASP GLU LYS TYR ARG GLY GLU PHE GLY ARG
SEQRES 14 A 404 TRP SER SER GLU ILE LEU VAL MET ASP PRO GLU ARG ALA
SEQRES 15 A 404 GLU GLN ARG GLY GLN ALA ALA ARG GLU VAL VAL ASN PHE
SEQRES 16 A 404 ILE LEU ASP LEU VAL GLU ARG ARG ARG THR GLU PRO GLY
SEQRES 17 A 404 ASP ASP LEU LEU SER ALA LEU ILE ARG VAL GLN ASP ASP
SEQRES 18 A 404 ASP ASP GLY ARG LEU SER ALA ASP GLU LEU THR SER ILE
SEQRES 19 A 404 ALA LEU VAL LEU LEU LEU ALA GLY PHE GLU THR SER VAL
SEQRES 20 A 404 SER LEU ILE GLY ILE GLY THR TYR LEU LEU LEU THR HIS
SEQRES 21 A 404 PRO ASP GLN LEU ALA LEU VAL ARG ARG ASP PRO SER ALA
SEQRES 22 A 404 LEU PRO ASN ALA VAL GLU GLU ILE LEU ARG TYR ILE ALA
SEQRES 23 A 404 PRO PRO GLU THR THR THR ARG PHE ALA ALA GLU GLU VAL
SEQRES 24 A 404 GLU ILE GLY GLY VAL ALA ILE PRO GLN TYR SER THR VAL
SEQRES 25 A 404 LEU VAL ALA ASN GLY ALA ALA ASN ARG ASP PRO LYS GLN
SEQRES 26 A 404 PHE PRO ASP PRO HIS ARG PHE ASP VAL THR ARG ASP THR
SEQRES 27 A 404 ARG GLY HIS LEU SER PHE GLY GLN GLY ILE HIS PHE CYS
SEQRES 28 A 404 MET GLY ARG PRO LEU ALA LYS LEU GLU GLY GLU VAL ALA
SEQRES 29 A 404 LEU ARG ALA LEU PHE GLY ARG PHE PRO ALA LEU SER LEU
SEQRES 30 A 404 GLY ILE ASP ALA ASP ASP VAL VAL TRP ARG ARG SER LEU
SEQRES 31 A 404 LEU LEU ARG GLY ILE ASP HIS LEU PRO VAL ARG LEU ASP
SEQRES 32 A 404 GLY
HET HEM A 410 43
HET OXY A 417 2
HET DEB A 420 27
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM OXY OXYGEN MOLECULE
HETNAM DEB 6-DEOXYERYTHRONOLIDE B
HETSYN HEM HEME
FORMUL 2 HEM C34 H32 FE N4 O4
FORMUL 3 OXY O2
FORMUL 4 DEB C21 H38 O6
FORMUL 5 HOH *173(H2 O)
HELIX 1 1 SER A 9 HIS A 13 5 5
HELIX 2 2 ASP A 15 ALA A 27 1 13
HELIX 3 3 GLY A 44 ASP A 54 1 11
HELIX 4 4 PHE A 72 LEU A 76 5 5
HELIX 5 5 PRO A 79 ALA A 87 1 9
HELIX 6 6 ASN A 89 SER A 93 5 5
HELIX 7 7 PRO A 96 GLN A 107 1 12
HELIX 8 8 THR A 110 MET A 117 1 8
HELIX 9 9 MET A 117 GLU A 131 1 15
HELIX 10 10 ILE A 140 PHE A 144 1 5
HELIX 11 11 HIS A 146 LEU A 157 1 12
HELIX 12 12 ASP A 160 ARG A 164 5 5
HELIX 13 13 GLU A 166 VAL A 176 1 11
HELIX 14 14 ASP A 178 GLU A 180 5 3
HELIX 15 15 ARG A 181 GLU A 206 1 26
HELIX 16 16 ASP A 210 VAL A 218 1 9
HELIX 17 17 SER A 227 THR A 259 1 33
HELIX 18 18 HIS A 260 ASP A 270 1 11
HELIX 19 19 ALA A 273 ILE A 285 1 13
HELIX 20 20 ALA A 315 ASN A 320 1 6
HELIX 21 21 GLY A 353 PHE A 372 1 20
HELIX 22 22 ASP A 380 VAL A 384 5 5
SHEET 1 A 5 VAL A 29 PHE A 34 0
SHEET 2 A 5 GLN A 37 VAL A 42 -1 O LEU A 41 N THR A 30
SHEET 3 A 5 THR A 311 VAL A 314 1 O LEU A 313 N TRP A 40
SHEET 4 A 5 THR A 291 ALA A 295 -1 N ARG A 293 O VAL A 312
SHEET 5 A 5 LEU A 57 SER A 58 -1 N SER A 58 O PHE A 294
SHEET 1 B 3 VAL A 137 ASP A 139 0
SHEET 2 B 3 PRO A 399 ARG A 401 -1 O VAL A 400 N VAL A 138
SHEET 3 B 3 SER A 376 LEU A 377 -1 N SER A 376 O ARG A 401
SHEET 1 C 2 GLN A 219 ASP A 220 0
SHEET 2 C 2 GLY A 224 ARG A 225 -1 O GLY A 224 N ASP A 220
SHEET 1 D 2 VAL A 299 ILE A 301 0
SHEET 2 D 2 VAL A 304 ILE A 306 -1 O ILE A 306 N VAL A 299
LINK SG CYS A 351 FE HEM A 410 1555 1555 2.31
LINK FE HEM A 410 O1 OXY A 417 1555 1555 1.77
LINK FE HEM A 410 O2 OXY A 417 1555 1555 2.78
CISPEP 1 PRO A 95 PRO A 96 0 0.12
SITE 1 AC1 21 MET A 90 GLY A 91 HIS A 98 ARG A 102
SITE 2 AC1 21 PHE A 109 ALA A 241 GLY A 242 THR A 245
SITE 3 AC1 21 ARG A 293 SER A 343 GLY A 345 ILE A 348
SITE 4 AC1 21 HIS A 349 CYS A 351 ALA A 357 OXY A 417
SITE 5 AC1 21 DEB A 420 HOH A 425 HOH A 431 HOH A 440
SITE 6 AC1 21 HOH A 463
SITE 1 AC2 4 ALA A 241 THR A 245 HEM A 410 DEB A 420
SITE 1 AC3 13 ALA A 74 GLY A 91 THR A 92 ILE A 174
SITE 2 AC3 13 LEU A 175 VAL A 237 THR A 245 LEU A 391
SITE 3 AC3 13 LEU A 392 HEM A 410 OXY A 417 HOH A 422
SITE 4 AC3 13 HOH A 433
CRYST1 53.950 78.560 96.930 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 0.018536 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012729 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010317 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
