HEADER OXIDOREDUCTASE(CYTOCHROME) 22-JAN-02 1GU2
TITLE CRYSTAL STRUCTURE OF OXIDIZED CYTOCHROME C'' FROM METHYLOPHILUS
TITLE 2 METHYLOTROPHUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C'';
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METHYLOPHILUS METHYLOTROPHUS;
SOURCE 3 ORGANISM_TAXID: 2327;
SOURCE 4 STRAIN: W3A1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS OXIDOREDUCTASE(CYTOCHROME), OXIDOREDUCTASE, ELECTRON TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR F.J.ENGUITA,E.POHL,A.RODRIGUES,H.SANTOS,M.A.CARRONDO
REVDAT 5 24-JUL-19 1GU2 1 REMARK
REVDAT 4 22-MAY-19 1GU2 1 REMARK LINK
REVDAT 3 22-MAR-17 1GU2 1 REMARK FORMUL
REVDAT 2 24-FEB-09 1GU2 1 VERSN
REVDAT 1 16-JAN-03 1GU2 0
JRNL AUTH F.J.ENGUITA,E.POHL,D.L.TURNER,H.SANTOS,M.A.CARRONDO
JRNL TITL STRUCTURAL EVIDENCE FOR A PROTON TRANSFER PATHWAY COUPLED
JRNL TITL 2 WITH HAEM REDUCTION OF CYTOCHROME C" FROM METHYLOPHILUS
JRNL TITL 3 METHYLOTROPHUS.
JRNL REF J.BIOL.INORG.CHEM. V. 11 189 2006
JRNL REFN ISSN 0949-8257
JRNL PMID 16341897
JRNL DOI 10.1007/S00775-005-0065-6
REMARK 2
REMARK 2 RESOLUTION. 1.19 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.19
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.2
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.148
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.186
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 100920
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.130
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.167
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 67489
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1911
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 86
REMARK 3 SOLVENT ATOMS : 357
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 2354.0
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 1887.0
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 6
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 21379
REMARK 3 NUMBER OF RESTRAINTS : 25807
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.014
REMARK 3 ANGLE DISTANCES (A) : 0.032
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.012
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.028
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.076
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.080
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.071
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.004
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.056
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.103
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1GU2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-JAN-02.
REMARK 100 THE DEPOSITION ID IS D_1290009196.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-SEP-01
REMARK 200 TEMPERATURE (KELVIN) : 110.0
REMARK 200 PH : 7.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8492
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 109062
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.190
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.05100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.19
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.26
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.48000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.950
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHELX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 0.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.00
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 29.26850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 39.19400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.05750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 39.19400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.26850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.05750
REMARK 290 SMTRY3 4 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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: PQS
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 LYS B 124
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 TYR A 10 CB - CG - CD1 ANGL. DEV. = -4.9 DEGREES
REMARK 500 ARG A 37 CD - NE - CZ ANGL. DEV. = 34.2 DEGREES
REMARK 500 ARG A 37 NE - CZ - NH2 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ASN A 55 O - C - N ANGL. DEV. = -10.1 DEGREES
REMARK 500 ASN A 56 C - N - CA ANGL. DEV. = 15.3 DEGREES
REMARK 500 ASN A 59 CB - CG - OD1 ANGL. DEV. = 16.8 DEGREES
REMARK 500 ARG A 76 NE - CZ - NH2 ANGL. DEV. = 3.8 DEGREES
REMARK 500 PHE A 92 CB - CG - CD1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 TYR B 10 CG - CD1 - CE1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 THR B 29 O - C - N ANGL. DEV. = -10.4 DEGREES
REMARK 500 ARG B 37 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ASN B 56 C - N - CA ANGL. DEV. = 16.2 DEGREES
REMARK 500 ASP B 86 CB - CG - OD1 ANGL. DEV. = 8.0 DEGREES
REMARK 500 ASP B 98 CB - CG - OD2 ANGL. DEV. = -5.7 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 THR A 54 173.80 69.97
REMARK 500 THR B 54 172.12 69.25
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2006 DISTANCE = 7.02 ANGSTROMS
REMARK 525 HOH A2029 DISTANCE = 6.24 ANGSTROMS
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 HEC A 125 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 53 NE2
REMARK 620 2 HEC A 125 NA 91.7
REMARK 620 3 HEC A 125 NB 91.2 89.7
REMARK 620 4 HEC A 125 NC 87.7 179.4 90.6
REMARK 620 5 HEC A 125 ND 90.8 89.7 177.9 90.1
REMARK 620 6 HIS A 95 NE2 178.4 88.8 90.3 91.7 87.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC B 125 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 53 NE2
REMARK 620 2 HEC B 125 NA 90.8
REMARK 620 3 HEC B 125 NB 92.1 89.6
REMARK 620 4 HEC B 125 NC 88.8 179.7 90.4
REMARK 620 5 HEC B 125 ND 89.6 90.4 178.4 89.6
REMARK 620 6 HIS B 95 NE2 177.8 88.3 90.0 92.1 88.4
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 HEC A 125
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC B 125
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1E8E RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF METHYLOPHILUS METHYLOTROPHUS CYTOCHROME C'':
REMARK 900 INSIGHTS INTO THE STRUCTURAL BASIS OF HAEM-LIGAND DETACHMENT
DBREF 1GU2 A 1 124 UNP Q9RQB9 CYCA_METME 21 144
DBREF 1GU2 B 1 124 UNP Q9RQB9 CYCA_METME 21 144
SEQRES 1 A 124 ASP VAL THR ASN ALA GLU LYS LEU VAL TYR LYS TYR THR
SEQRES 2 A 124 ASN ILE ALA HIS SER ALA ASN PRO MET TYR GLU ALA PRO
SEQRES 3 A 124 SER ILE THR ASP GLY LYS ILE PHE PHE ASN ARG LYS PHE
SEQRES 4 A 124 LYS THR PRO SER GLY LYS GLU ALA ALA CYS ALA SER CYS
SEQRES 5 A 124 HIS THR ASN ASN PRO ALA ASN VAL GLY LYS ASN ILE VAL
SEQRES 6 A 124 THR GLY LYS GLU ILE PRO PRO LEU ALA PRO ARG VAL ASN
SEQRES 7 A 124 THR LYS ARG PHE THR ASP ILE ASP LYS VAL GLU ASP GLU
SEQRES 8 A 124 PHE THR LYS HIS CYS ASN ASP ILE LEU GLY ALA ASP CYS
SEQRES 9 A 124 SER PRO SER GLU LYS ALA ASN PHE ILE ALA TYR LEU LEU
SEQRES 10 A 124 THR GLU THR LYS PRO THR LYS
SEQRES 1 B 124 ASP VAL THR ASN ALA GLU LYS LEU VAL TYR LYS TYR THR
SEQRES 2 B 124 ASN ILE ALA HIS SER ALA ASN PRO MET TYR GLU ALA PRO
SEQRES 3 B 124 SER ILE THR ASP GLY LYS ILE PHE PHE ASN ARG LYS PHE
SEQRES 4 B 124 LYS THR PRO SER GLY LYS GLU ALA ALA CYS ALA SER CYS
SEQRES 5 B 124 HIS THR ASN ASN PRO ALA ASN VAL GLY LYS ASN ILE VAL
SEQRES 6 B 124 THR GLY LYS GLU ILE PRO PRO LEU ALA PRO ARG VAL ASN
SEQRES 7 B 124 THR LYS ARG PHE THR ASP ILE ASP LYS VAL GLU ASP GLU
SEQRES 8 B 124 PHE THR LYS HIS CYS ASN ASP ILE LEU GLY ALA ASP CYS
SEQRES 9 B 124 SER PRO SER GLU LYS ALA ASN PHE ILE ALA TYR LEU LEU
SEQRES 10 B 124 THR GLU THR LYS PRO THR LYS
HET HEC A 125 43
HET HEC B 125 43
HETNAM HEC HEME C
FORMUL 3 HEC 2(C34 H34 FE N4 O4)
FORMUL 5 HOH *357(H2 O)
HELIX 1 1 ASP A 1 ASN A 20 1 20
HELIX 2 2 SER A 27 ARG A 37 1 11
HELIX 3 3 ALA A 48 THR A 54 1 7
HELIX 4 4 ASP A 84 GLY A 101 1 18
HELIX 5 5 SER A 105 GLU A 119 1 15
HELIX 6 6 ASP B 1 ASN B 20 1 20
HELIX 7 7 SER B 27 ARG B 37 1 11
HELIX 8 8 ALA B 48 THR B 54 1 7
HELIX 9 9 ASP B 84 GLY B 101 1 18
HELIX 10 10 SER B 105 LEU B 117 1 13
SHEET 1 AA 2 PHE A 39 LYS A 40 0
SHEET 2 AA 2 GLU A 46 ALA A 47 -1 O ALA A 47 N PHE A 39
SHEET 1 AB 2 GLY A 61 LYS A 62 0
SHEET 2 AB 2 GLU A 69 ILE A 70 -1 O ILE A 70 N GLY A 61
SHEET 1 BA 2 PHE B 39 LYS B 40 0
SHEET 2 BA 2 GLU B 46 ALA B 47 -1 O ALA B 47 N PHE B 39
SHEET 1 BB 2 GLY B 61 LYS B 62 0
SHEET 2 BB 2 GLU B 69 ILE B 70 -1 O ILE B 70 N GLY B 61
SSBOND 1 CYS A 96 CYS A 104 1555 1555 2.06
SSBOND 2 CYS B 96 CYS B 104 1555 1555 2.09
LINK SG CYS A 49 CAB HEC A 125 1555 1555 1.83
LINK SG CYS A 52 CAC HEC A 125 1555 1555 1.85
LINK NE2 HIS A 53 FE HEC A 125 1555 1555 2.02
LINK NE2 HIS A 95 FE HEC A 125 1555 1555 2.01
LINK SG CYS B 49 CAB HEC B 125 1555 1555 1.82
LINK SG CYS B 52 CAC HEC B 125 1555 1555 1.83
LINK NE2 HIS B 53 FE HEC B 125 1555 1555 2.01
LINK NE2 HIS B 95 FE HEC B 125 1555 1555 2.02
SITE 1 AC1 18 PHE A 34 ALA A 48 CYS A 49 CYS A 52
SITE 2 AC1 18 HIS A 53 ASN A 63 PRO A 71 LEU A 73
SITE 3 AC1 18 ARG A 81 GLU A 91 HIS A 95 ILE A 99
SITE 4 AC1 18 HOH A2185 HOH A2186 HOH A2187 HOH A2188
SITE 5 AC1 18 HOH A2189 HOH A2190
SITE 1 AC2 16 PHE B 34 CYS B 49 CYS B 52 HIS B 53
SITE 2 AC2 16 ASN B 63 PRO B 71 LEU B 73 ARG B 81
SITE 3 AC2 16 VAL B 88 HIS B 95 ILE B 99 HOH B2120
SITE 4 AC2 16 HOH B2164 HOH B2165 HOH B2166 HOH B2167
CRYST1 58.537 74.115 78.388 90.00 90.00 90.00 P 21 21 21 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 0.017083 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013492 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012757 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
