HEADER OXIDOREDUCTASE 15-JAN-11 2Y5N
TITLE STRUCTURE OF THE MIXED-FUNCTION P450 MYCG IN COMPLEX WITH MYCINAMICIN
TITLE 2 V IN P21 SPACE GROUP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: P-450-LIKE PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: MYCG;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MICROMONOSPORA GRISEORUBIDA;
SOURCE 3 ORGANISM_TAXID: 28040;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28B
KEYWDS OXIDOREDUCTASE, MYCINAMICIN BIOSYNTHESIS
EXPDTA X-RAY DIFFRACTION
AUTHOR S.LI,P.M.KELLS,D.H.SHERMAN,L.M.PODUST
REVDAT 6 20-DEC-23 2Y5N 1 REMARK LINK
REVDAT 5 08-MAY-19 2Y5N 1 REMARK
REVDAT 4 14-NOV-12 2Y5N 1 JRNL
REVDAT 3 19-SEP-12 2Y5N 1 JRNL
REVDAT 2 05-SEP-12 2Y5N 1 REMARK
REVDAT 1 01-FEB-12 2Y5N 0
JRNL AUTH S.LI,D.R.TIETZ,F.U.RUTAGANIRA,P.M.KELLS,Y.ANZAI,F.KATO,
JRNL AUTH 2 T.C.POCHAPSKY,D.H.SHERMAN,L.M.PODUST
JRNL TITL SUBSTRATE RECOGNITION BY THE MULTIFUNCTIONAL CYTOCHROME P450
JRNL TITL 2 MYCG IN MYCINAMICIN HYDROXYLATION AND EPOXIDATION REACTIONS.
JRNL REF J.BIOL.CHEM. V. 287 37880 2012
JRNL REFN ISSN 0021-9258
JRNL PMID 22952225
JRNL DOI 10.1074/JBC.M112.410340
REMARK 2
REMARK 2 RESOLUTION. 1.62 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.62
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 75.91
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 70.4
REMARK 3 NUMBER OF REFLECTIONS : 75373
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 + TEST SET) : 0.118
REMARK 3 R VALUE (WORKING SET) : 0.115
REMARK 3 FREE R VALUE : 0.188
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 4038
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) : 1.62
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.66
REMARK 3 REFLECTION IN BIN (WORKING SET) : 464
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 5.92
REMARK 3 BIN R VALUE (WORKING SET) : 0.3870
REMARK 3 BIN FREE R VALUE SET COUNT : 28
REMARK 3 BIN FREE R VALUE : 0.4080
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6233
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 265
REMARK 3 SOLVENT ATOMS : 1137
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.57
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.38000
REMARK 3 B22 (A**2) : 0.13000
REMARK 3 B33 (A**2) : -0.65000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.17000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.271
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.112
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.054
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.495
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.979
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6859 ; 0.023 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9369 ; 1.904 ; 2.041
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 836 ; 5.672 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 323 ;30.054 ;22.198
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1097 ;13.429 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 93 ;19.042 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1024 ; 0.122 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5326 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 4109 ; 1.702 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6652 ; 2.653 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2750 ; 4.357 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2717 ; 6.378 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 6859 ; 2.366 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 5 A 460 4
REMARK 3 1 B 5 B 460 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 3041 ; 0.27 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 B (A): 3041 ; 0.27 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 3041 ; 1.92 ; 2.00
REMARK 3 MEDIUM THERMAL 1 B (A**2): 3041 ; 1.92 ; 2.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 2Y5N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-JAN-11.
REMARK 100 THE DEPOSITION ID IS D_1290047021.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUL-09
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.11587
REMARK 200 MONOCHROMATOR : SI (111) DOUBLE CRYSTAL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 79430
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.610
REMARK 200 RESOLUTION RANGE LOW (A) : 93.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 70.4
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.04000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.61
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 11.1
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : 0.30000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
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 2Y4H
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 7% PEG 4000, 0.025 M MG ACETATE, 23
REMARK 280 DEGREES C, PH 7.0, TEMPERATURE 296K
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 28.71400
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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: PISA
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 MET A -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 THR A 2
REMARK 465 SER A 3
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -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 GLN B 215 CG CD OE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 NH1 ARG B 75 OE2 GLU B 77 1.82
REMARK 500 O HOH A 2103 O HOH A 2251 2.01
REMARK 500 O HOH A 2134 O HOH A 2305 2.11
REMARK 500 O HOH B 2232 O HOH B 2450 2.16
REMARK 500 O HOH A 2047 O HOH A 2449 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 ARG A 95 CB ARG A 95 CG -0.180
REMARK 500 GLU A 200 CD GLU A 200 OE1 0.071
REMARK 500 SER A 238 CB SER A 238 OG 0.089
REMARK 500 GLU B 28 CG GLU B 28 CD 0.107
REMARK 500 GLU B 28 CD GLU B 28 OE1 0.081
REMARK 500 GLU B 120 CG GLU B 120 CD 0.092
REMARK 500 ARG B 353 CZ ARG B 353 NH2 -0.084
REMARK 500
REMARK 500 REMARK: NULL
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 ARG A 213 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 LEU A 250 CA - CB - CG ANGL. DEV. = -21.2 DEGREES
REMARK 500 ARG A 353 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG B 53 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG B 53 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG B 115 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG B 353 CD - NE - CZ ANGL. DEV. = 10.5 DEGREES
REMARK 500 ARG B 353 NE - CZ - NH1 ANGL. DEV. = 12.6 DEGREES
REMARK 500 ARG B 353 NE - CZ - NH2 ANGL. DEV. = -11.7 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 PHE A 138 -63.26 -130.85
REMARK 500 THR A 202 -158.19 -133.81
REMARK 500 GLN A 215 -108.74 51.38
REMARK 500 TYR A 236 -75.15 -93.81
REMARK 500 PHE B 138 -64.58 -129.46
REMARK 500 THR B 202 -163.63 -122.91
REMARK 500 GLN B 215 -114.51 49.85
REMARK 500 TYR B 236 -73.40 -93.48
REMARK 500 THR B 284 69.57 -150.37
REMARK 500 ALA B 285 -173.29 -62.93
REMARK 500 ALA B 285 159.98 -49.69
REMARK 500 MET B 385 4.55 81.70
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 A2029 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH A2030 DISTANCE = 7.91 ANGSTROMS
REMARK 525 HOH A2073 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH A2084 DISTANCE = 6.81 ANGSTROMS
REMARK 525 HOH B2021 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH B2025 DISTANCE = 6.79 ANGSTROMS
REMARK 525 HOH B2050 DISTANCE = 5.92 ANGSTROMS
REMARK 525 HOH B2073 DISTANCE = 6.97 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 PROTOPORPHYRIN IX CONTAINING FE (HEM): HEME-THIOLATE BOND
REMARK 600 TO CYS 346
REMARK 600 MYCINAMICIN V (MV): NATIVE MYCG SUBSTRATE
REMARK 600 GLYCEROL (GOL): PART OF CRYO-PROTECTANT
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 450 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 346 SG
REMARK 620 2 HEM A 450 NA 95.7
REMARK 620 3 HEM A 450 NB 90.1 90.5
REMARK 620 4 HEM A 450 NC 87.9 176.3 88.8
REMARK 620 5 HEM A 450 ND 94.0 90.1 175.8 90.3
REMARK 620 6 HOH A2397 O 176.1 86.6 86.7 89.7 89.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1406 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A2103 O
REMARK 620 2 HOH A2260 O 94.7
REMARK 620 3 HOH A2263 O 112.0 77.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 450 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 346 SG
REMARK 620 2 HEM B 450 NA 96.5
REMARK 620 3 HEM B 450 NB 88.6 90.0
REMARK 620 4 HEM B 450 NC 87.1 176.5 90.2
REMARK 620 5 HEM B 450 ND 95.7 89.7 175.7 89.8
REMARK 620 6 HOH B2381 O 175.3 87.8 89.4 88.6 86.3
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 450
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MYV A 460
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1398
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1399
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1404
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1405
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1406
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 450
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MYV B 460
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1398
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1399
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1400
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1401
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2Y4H RELATED DB: PDB
REMARK 900 STRUCTURE OF THE MIXED-FUNCTION P450 MYCG IN COMPLEX WITH
REMARK 900 MYCINAMICIN IV IN P21212 SPACE GROUP
REMARK 900 RELATED ID: 2Y46 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE MIXED-FUNCTION P450 MYCG IN COMPLEX WITH
REMARK 900 MYCINAMICIN IV
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE 6XHIS TAG AND THROMBIN CLEAVAGE SITE ARE ENGINEERED AT
REMARK 999 THE N-TERMINUS.
DBREF 2Y5N A 1 397 UNP Q59523 Q59523_MICGR 1 397
DBREF 2Y5N B 1 397 UNP Q59523 Q59523_MICGR 1 397
SEQADV 2Y5N MET A -19 UNP Q59523 EXPRESSION TAG
SEQADV 2Y5N GLY A -18 UNP Q59523 EXPRESSION TAG
SEQADV 2Y5N SER A -17 UNP Q59523 EXPRESSION TAG
SEQADV 2Y5N SER A -16 UNP Q59523 EXPRESSION TAG
SEQADV 2Y5N HIS A -15 UNP Q59523 EXPRESSION TAG
SEQADV 2Y5N HIS A -14 UNP Q59523 EXPRESSION TAG
SEQADV 2Y5N HIS A -13 UNP Q59523 EXPRESSION TAG
SEQADV 2Y5N HIS A -12 UNP Q59523 EXPRESSION TAG
SEQADV 2Y5N HIS A -11 UNP Q59523 EXPRESSION TAG
SEQADV 2Y5N HIS A -10 UNP Q59523 EXPRESSION TAG
SEQADV 2Y5N SER A -9 UNP Q59523 EXPRESSION TAG
SEQADV 2Y5N SER A -8 UNP Q59523 EXPRESSION TAG
SEQADV 2Y5N GLY A -7 UNP Q59523 EXPRESSION TAG
SEQADV 2Y5N LEU A -6 UNP Q59523 EXPRESSION TAG
SEQADV 2Y5N VAL A -5 UNP Q59523 EXPRESSION TAG
SEQADV 2Y5N PRO A -4 UNP Q59523 EXPRESSION TAG
SEQADV 2Y5N ARG A -3 UNP Q59523 EXPRESSION TAG
SEQADV 2Y5N GLY A -2 UNP Q59523 EXPRESSION TAG
SEQADV 2Y5N SER A -1 UNP Q59523 EXPRESSION TAG
SEQADV 2Y5N HIS A 0 UNP Q59523 EXPRESSION TAG
SEQADV 2Y5N MET B -19 UNP Q59523 EXPRESSION TAG
SEQADV 2Y5N GLY B -18 UNP Q59523 EXPRESSION TAG
SEQADV 2Y5N SER B -17 UNP Q59523 EXPRESSION TAG
SEQADV 2Y5N SER B -16 UNP Q59523 EXPRESSION TAG
SEQADV 2Y5N HIS B -15 UNP Q59523 EXPRESSION TAG
SEQADV 2Y5N HIS B -14 UNP Q59523 EXPRESSION TAG
SEQADV 2Y5N HIS B -13 UNP Q59523 EXPRESSION TAG
SEQADV 2Y5N HIS B -12 UNP Q59523 EXPRESSION TAG
SEQADV 2Y5N HIS B -11 UNP Q59523 EXPRESSION TAG
SEQADV 2Y5N HIS B -10 UNP Q59523 EXPRESSION TAG
SEQADV 2Y5N SER B -9 UNP Q59523 EXPRESSION TAG
SEQADV 2Y5N SER B -8 UNP Q59523 EXPRESSION TAG
SEQADV 2Y5N GLY B -7 UNP Q59523 EXPRESSION TAG
SEQADV 2Y5N LEU B -6 UNP Q59523 EXPRESSION TAG
SEQADV 2Y5N VAL B -5 UNP Q59523 EXPRESSION TAG
SEQADV 2Y5N PRO B -4 UNP Q59523 EXPRESSION TAG
SEQADV 2Y5N ARG B -3 UNP Q59523 EXPRESSION TAG
SEQADV 2Y5N GLY B -2 UNP Q59523 EXPRESSION TAG
SEQADV 2Y5N SER B -1 UNP Q59523 EXPRESSION TAG
SEQADV 2Y5N HIS B 0 UNP Q59523 EXPRESSION TAG
SEQRES 1 A 417 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 417 LEU VAL PRO ARG GLY SER HIS MET THR SER ALA GLU PRO
SEQRES 3 A 417 ARG ALA TYR PRO PHE ASN ASP VAL HIS GLY LEU THR LEU
SEQRES 4 A 417 ALA GLY ARG TYR GLY GLU LEU GLN GLU THR GLU PRO VAL
SEQRES 5 A 417 SER ARG VAL ARG PRO PRO TYR GLY GLU GLU ALA TRP LEU
SEQRES 6 A 417 VAL THR ARG TYR GLU ASP VAL ARG ALA VAL LEU GLY ASP
SEQRES 7 A 417 GLY ARG PHE VAL ARG GLY PRO SER MET THR ARG ASP GLU
SEQRES 8 A 417 PRO ARG THR ARG PRO GLU MET VAL LYS GLY GLY LEU LEU
SEQRES 9 A 417 SER MET ASP PRO PRO GLU HIS SER ARG LEU ARG ARG LEU
SEQRES 10 A 417 VAL VAL LYS ALA PHE THR ALA ARG ARG ALA GLU SER LEU
SEQRES 11 A 417 ARG PRO ARG ALA ARG GLU ILE ALA HIS GLU LEU VAL ASP
SEQRES 12 A 417 GLN MET ALA ALA THR GLY GLN PRO ALA ASP LEU VAL ALA
SEQRES 13 A 417 MET PHE ALA ARG GLN LEU PRO VAL ARG VAL ILE CYS GLU
SEQRES 14 A 417 LEU LEU GLY VAL PRO SER ALA ASP HIS ASP ARG PHE THR
SEQRES 15 A 417 ARG TRP SER GLY ALA PHE LEU SER THR ALA GLU VAL THR
SEQRES 16 A 417 ALA GLU GLU MET GLN GLU ALA ALA GLU GLN ALA TYR ALA
SEQRES 17 A 417 TYR MET GLY ASP LEU ILE ASP ARG ARG ARG LYS GLU PRO
SEQRES 18 A 417 THR ASP ASP LEU VAL SER ALA LEU VAL GLN ALA ARG ASP
SEQRES 19 A 417 GLN GLN ASP SER LEU SER GLU GLN GLU LEU LEU ASP LEU
SEQRES 20 A 417 ALA ILE GLY LEU LEU VAL ALA GLY TYR GLU SER THR THR
SEQRES 21 A 417 THR GLN ILE ALA ASP PHE VAL TYR LEU LEU MET THR ARG
SEQRES 22 A 417 PRO GLU LEU ARG ARG GLN LEU LEU ASP ARG PRO GLU LEU
SEQRES 23 A 417 ILE PRO SER ALA VAL GLU GLU LEU THR ARG TRP VAL PRO
SEQRES 24 A 417 LEU GLY VAL GLY THR ALA PHE PRO ARG TYR ALA VAL GLU
SEQRES 25 A 417 ASP VAL THR LEU ARG GLY VAL THR ILE ARG ALA GLY GLU
SEQRES 26 A 417 PRO VAL LEU ALA SER THR GLY ALA ALA ASN ARG ASP GLN
SEQRES 27 A 417 ALA GLN PHE PRO ASP ALA ASP ARG ILE ASP VAL ASP ARG
SEQRES 28 A 417 THR PRO ASN GLN HIS LEU GLY PHE GLY HIS GLY VAL HIS
SEQRES 29 A 417 HIS CYS LEU GLY ALA PRO LEU ALA ARG VAL GLU LEU GLN
SEQRES 30 A 417 VAL ALA LEU GLU VAL LEU LEU GLN ARG LEU PRO GLY ILE
SEQRES 31 A 417 ARG LEU GLY ILE PRO GLU THR GLN LEU ARG TRP SER GLU
SEQRES 32 A 417 GLY MET LEU LEU ARG GLY PRO LEU GLU LEU PRO VAL VAL
SEQRES 33 A 417 TRP
SEQRES 1 B 417 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 417 LEU VAL PRO ARG GLY SER HIS MET THR SER ALA GLU PRO
SEQRES 3 B 417 ARG ALA TYR PRO PHE ASN ASP VAL HIS GLY LEU THR LEU
SEQRES 4 B 417 ALA GLY ARG TYR GLY GLU LEU GLN GLU THR GLU PRO VAL
SEQRES 5 B 417 SER ARG VAL ARG PRO PRO TYR GLY GLU GLU ALA TRP LEU
SEQRES 6 B 417 VAL THR ARG TYR GLU ASP VAL ARG ALA VAL LEU GLY ASP
SEQRES 7 B 417 GLY ARG PHE VAL ARG GLY PRO SER MET THR ARG ASP GLU
SEQRES 8 B 417 PRO ARG THR ARG PRO GLU MET VAL LYS GLY GLY LEU LEU
SEQRES 9 B 417 SER MET ASP PRO PRO GLU HIS SER ARG LEU ARG ARG LEU
SEQRES 10 B 417 VAL VAL LYS ALA PHE THR ALA ARG ARG ALA GLU SER LEU
SEQRES 11 B 417 ARG PRO ARG ALA ARG GLU ILE ALA HIS GLU LEU VAL ASP
SEQRES 12 B 417 GLN MET ALA ALA THR GLY GLN PRO ALA ASP LEU VAL ALA
SEQRES 13 B 417 MET PHE ALA ARG GLN LEU PRO VAL ARG VAL ILE CYS GLU
SEQRES 14 B 417 LEU LEU GLY VAL PRO SER ALA ASP HIS ASP ARG PHE THR
SEQRES 15 B 417 ARG TRP SER GLY ALA PHE LEU SER THR ALA GLU VAL THR
SEQRES 16 B 417 ALA GLU GLU MET GLN GLU ALA ALA GLU GLN ALA TYR ALA
SEQRES 17 B 417 TYR MET GLY ASP LEU ILE ASP ARG ARG ARG LYS GLU PRO
SEQRES 18 B 417 THR ASP ASP LEU VAL SER ALA LEU VAL GLN ALA ARG ASP
SEQRES 19 B 417 GLN GLN ASP SER LEU SER GLU GLN GLU LEU LEU ASP LEU
SEQRES 20 B 417 ALA ILE GLY LEU LEU VAL ALA GLY TYR GLU SER THR THR
SEQRES 21 B 417 THR GLN ILE ALA ASP PHE VAL TYR LEU LEU MET THR ARG
SEQRES 22 B 417 PRO GLU LEU ARG ARG GLN LEU LEU ASP ARG PRO GLU LEU
SEQRES 23 B 417 ILE PRO SER ALA VAL GLU GLU LEU THR ARG TRP VAL PRO
SEQRES 24 B 417 LEU GLY VAL GLY THR ALA PHE PRO ARG TYR ALA VAL GLU
SEQRES 25 B 417 ASP VAL THR LEU ARG GLY VAL THR ILE ARG ALA GLY GLU
SEQRES 26 B 417 PRO VAL LEU ALA SER THR GLY ALA ALA ASN ARG ASP GLN
SEQRES 27 B 417 ALA GLN PHE PRO ASP ALA ASP ARG ILE ASP VAL ASP ARG
SEQRES 28 B 417 THR PRO ASN GLN HIS LEU GLY PHE GLY HIS GLY VAL HIS
SEQRES 29 B 417 HIS CYS LEU GLY ALA PRO LEU ALA ARG VAL GLU LEU GLN
SEQRES 30 B 417 VAL ALA LEU GLU VAL LEU LEU GLN ARG LEU PRO GLY ILE
SEQRES 31 B 417 ARG LEU GLY ILE PRO GLU THR GLN LEU ARG TRP SER GLU
SEQRES 32 B 417 GLY MET LEU LEU ARG GLY PRO LEU GLU LEU PRO VAL VAL
SEQRES 33 B 417 TRP
HET HEM A 450 43
HET MYV A 460 50
HET GOL A1398 6
HET GOL A1399 6
HET GOL A1400 6
HET GOL A1401 6
HET GOL A1402 6
HET GOL A1403 6
HET GOL A1404 6
HET GOL A1405 6
HET MG A1406 1
HET HEM B 450 43
HET MYV B 460 50
HET GOL B1398 6
HET GOL B1399 6
HET GOL B1400 6
HET GOL B1401 6
HET GOL B1402 6
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM MYV MYCINAMICIN V
HETNAM GOL GLYCEROL
HETNAM MG MAGNESIUM ION
HETSYN HEM HEME
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 4 MYV 2(C37 H61 N O12)
FORMUL 5 GOL 13(C3 H8 O3)
FORMUL 13 MG MG 2+
FORMUL 21 HOH *1137(H2 O)
HELIX 1 1 ALA A 20 GLU A 30 1 11
HELIX 2 2 ARG A 48 GLY A 57 1 10
HELIX 3 3 ARG A 63 THR A 68 5 6
HELIX 4 4 GLY A 82 MET A 86 5 5
HELIX 5 5 PRO A 89 PHE A 102 1 14
HELIX 6 6 THR A 103 LEU A 110 1 8
HELIX 7 7 LEU A 110 GLY A 129 1 20
HELIX 8 8 LEU A 134 PHE A 138 1 5
HELIX 9 9 GLN A 141 GLY A 152 1 12
HELIX 10 10 PRO A 154 ALA A 156 5 3
HELIX 11 11 ASP A 157 ALA A 167 1 11
HELIX 12 12 THR A 175 GLU A 200 1 26
HELIX 13 13 ASP A 204 ALA A 212 1 9
HELIX 14 14 SER A 220 ARG A 263 1 44
HELIX 15 15 LEU A 266 VAL A 278 1 13
HELIX 16 16 SER A 310 ASN A 315 1 6
HELIX 17 17 GLY A 348 LEU A 367 1 20
HELIX 18 18 PRO A 375 LEU A 379 5 5
HELIX 19 19 ALA B 20 GLU B 30 1 11
HELIX 20 20 ARG B 48 ASP B 58 1 11
HELIX 21 21 ARG B 63 THR B 68 5 6
HELIX 22 22 GLY B 82 MET B 86 5 5
HELIX 23 23 PRO B 89 PHE B 102 1 14
HELIX 24 24 THR B 103 LEU B 110 1 8
HELIX 25 25 LEU B 110 GLY B 129 1 20
HELIX 26 26 LEU B 134 PHE B 138 1 5
HELIX 27 27 GLN B 141 GLY B 152 1 12
HELIX 28 28 PRO B 154 ALA B 156 5 3
HELIX 29 29 ASP B 157 ALA B 167 1 11
HELIX 30 30 THR B 175 GLU B 200 1 26
HELIX 31 31 ASP B 204 ALA B 212 1 9
HELIX 32 32 SER B 220 GLY B 235 1 16
HELIX 33 33 TYR B 236 ARG B 253 1 18
HELIX 34 34 ARG B 253 ARG B 263 1 11
HELIX 35 35 LEU B 266 VAL B 278 1 13
HELIX 36 36 SER B 310 ASN B 315 1 6
HELIX 37 37 GLY B 348 LEU B 367 1 20
HELIX 38 38 PRO B 375 LEU B 379 5 5
SHEET 1 AA 6 ARG A 7 ALA A 8 0
SHEET 2 AA 6 VAL A 32 ARG A 36 1 O ARG A 34 N ARG A 7
SHEET 3 AA 6 ALA A 43 VAL A 46 -1 O ALA A 43 N VAL A 35
SHEET 4 AA 6 PRO A 306 ALA A 309 1 O PRO A 306 N TRP A 44
SHEET 5 AA 6 ARG A 288 ALA A 290 -1 O ARG A 288 N VAL A 307
SHEET 6 AA 6 PHE A 61 VAL A 62 -1 O VAL A 62 N TYR A 289
SHEET 1 AB 3 ALA A 132 ASP A 133 0
SHEET 2 AB 3 PRO A 394 VAL A 396 -1 O VAL A 395 N ALA A 132
SHEET 3 AB 3 ARG A 371 LEU A 372 -1 O ARG A 371 N VAL A 396
SHEET 1 AC 2 VAL A 294 LEU A 296 0
SHEET 2 AC 2 VAL A 299 ILE A 301 -1 O VAL A 299 N LEU A 296
SHEET 1 BA 6 ARG B 7 ALA B 8 0
SHEET 2 BA 6 VAL B 32 ARG B 36 1 O ARG B 34 N ARG B 7
SHEET 3 BA 6 ALA B 43 VAL B 46 -1 O ALA B 43 N VAL B 35
SHEET 4 BA 6 PRO B 306 ALA B 309 1 O PRO B 306 N TRP B 44
SHEET 5 BA 6 ARG B 288 ALA B 290 -1 O ARG B 288 N VAL B 307
SHEET 6 BA 6 PHE B 61 VAL B 62 -1 O VAL B 62 N TYR B 289
SHEET 1 BB 3 ALA B 132 ASP B 133 0
SHEET 2 BB 3 PRO B 394 VAL B 396 -1 O VAL B 395 N ALA B 132
SHEET 3 BB 3 ARG B 371 LEU B 372 -1 O ARG B 371 N VAL B 396
SHEET 1 BC 2 VAL B 294 LEU B 296 0
SHEET 2 BC 2 VAL B 299 ILE B 301 -1 O VAL B 299 N LEU B 296
LINK SG CYS A 346 FE HEM A 450 1555 1555 2.34
LINK FE HEM A 450 O HOH A2397 1555 1555 2.22
LINK MG MG A1406 O HOH A2103 1555 1555 2.87
LINK MG MG A1406 O HOH A2260 1555 1555 2.68
LINK MG MG A1406 O HOH A2263 1555 1555 2.56
LINK SG CYS B 346 FE HEM B 450 1555 1555 2.34
LINK FE HEM B 450 O HOH B2381 1555 1555 2.25
CISPEP 1 TYR A 9 PRO A 10 0 7.42
CISPEP 2 PRO A 88 PRO A 89 0 3.88
CISPEP 3 GLN A 130 PRO A 131 0 -8.10
CISPEP 4 THR A 332 PRO A 333 0 -9.15
CISPEP 5 TYR B 9 PRO B 10 0 5.29
CISPEP 6 PRO B 88 PRO B 89 0 6.54
CISPEP 7 GLN B 130 PRO B 131 0 -3.43
CISPEP 8 THR B 332 PRO B 333 0 -10.71
SITE 1 AC1 24 LEU A 83 LEU A 84 HIS A 91 ARG A 95
SITE 2 AC1 24 PHE A 102 ALA A 234 GLY A 235 SER A 238
SITE 3 AC1 24 THR A 239 GLN A 242 PHE A 286 ARG A 288
SITE 4 AC1 24 GLY A 338 PHE A 339 GLY A 340 HIS A 344
SITE 5 AC1 24 CYS A 346 LEU A 347 GLY A 348 ALA A 352
SITE 6 AC1 24 MYV A 460 HOH A2397 HOH A2566 HOH A2567
SITE 1 AC2 17 ARG A 75 VAL A 79 GLY A 81 GLY A 82
SITE 2 AC2 17 LEU A 84 PHE A 168 VAL A 174 MET A 179
SITE 3 AC2 17 VAL A 233 ALA A 234 LEU A 386 HEM A 450
SITE 4 AC2 17 HOH A2313 HOH A2399 HOH A2569 HOH A2570
SITE 5 AC2 17 HOH A2571
SITE 1 AC3 6 ARG A 113 GLU A 120 ARG A 145 SER A 155
SITE 2 AC3 6 HIS A 158 HOH A2572
SITE 1 AC4 5 THR A 18 LEU A 19 ALA A 20 GLY A 21
SITE 2 AC4 5 HOH A2573
SITE 1 AC5 3 GLU A 292 HOH A2575 HOH A2576
SITE 1 AC6 4 GLY A 191 ASP A 195 HOH A2346 HOH A2578
SITE 1 AC7 8 ARG A 140 THR A 240 THR A 241 ALA A 244
SITE 2 AC7 8 GLY A 389 PRO A 390 LEU A 391 HOH A2579
SITE 1 AC8 7 ARG A 140 THR A 171 LEU A 391 HOH A2311
SITE 2 AC8 7 HOH A2561 HOH A2581 HOH A2582
SITE 1 AC9 3 ASP A 325 HOH A2483 HOH A2485
SITE 1 BC1 10 ARG A 73 THR A 74 VAL A 282 GLY A 283
SITE 2 BC1 10 ALA A 285 MET A 385 LEU A 386 HOH A2439
SITE 3 BC1 10 HOH A2583 HOH A2584
SITE 1 BC2 4 HOH A2103 HOH A2251 HOH A2260 HOH A2263
SITE 1 BC3 21 LEU B 83 LEU B 84 HIS B 91 ARG B 95
SITE 2 BC3 21 PHE B 102 ALA B 234 GLY B 235 SER B 238
SITE 3 BC3 21 THR B 239 ALA B 285 PHE B 286 ARG B 288
SITE 4 BC3 21 GLY B 338 PHE B 339 GLY B 340 HIS B 344
SITE 5 BC3 21 CYS B 346 GLY B 348 MYV B 460 HOH B2381
SITE 6 BC3 21 HOH B2543
SITE 1 BC4 18 ARG B 75 GLU B 77 VAL B 79 GLY B 81
SITE 2 BC4 18 GLY B 82 LEU B 83 LEU B 84 PHE B 168
SITE 3 BC4 18 SER B 170 VAL B 174 MET B 179 VAL B 233
SITE 4 BC4 18 ALA B 234 LEU B 386 HEM B 450 HOH B2545
SITE 5 BC4 18 HOH B2546 HOH B2547
SITE 1 BC5 5 ARG B 253 GLU B 255 ILE B 327 HOH B2464
SITE 2 BC5 5 HOH B2469
SITE 1 BC6 8 ARG B 140 THR B 240 THR B 241 ALA B 244
SITE 2 BC6 8 GLY B 389 PRO B 390 LEU B 391 HOH B2548
SITE 1 BC7 9 LEU B 56 GLY B 57 GLY B 59 PHE B 61
SITE 2 BC7 9 PRO B 88 GLY B 342 VAL B 343 HOH B2201
SITE 3 BC7 9 HOH B2549
SITE 1 BC8 9 THR B 2 ARG B 34 GLU B 41 GLU B 42
SITE 2 BC8 9 ALA B 43 TRP B 44 GLU B 305 PRO B 306
SITE 3 BC8 9 HOH B2551
SITE 1 BC9 6 TYR B 248 THR B 252 ARG B 253 GLU B 376
SITE 2 BC9 6 HOH B2552 HOH B2553
CRYST1 82.752 57.428 101.929 90.00 113.47 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 0.012084 0.000000 0.005247 0.00000
SCALE2 0.000000 0.017413 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010696 0.00000
MTRIX1 1 0.832400 -0.008577 -0.554100 35.78000 1
MTRIX2 1 0.003232 0.999900 -0.010620 17.34000 1
MTRIX3 1 0.554200 0.007051 0.832400 -4.55600 1
(ATOM LINES ARE NOT SHOWN.)
END
