HEADER OXIDOREDUCTASE 28-JUN-10 3NPL
TITLE STRUCTURE OF RU(BPY)2(A-PHEN)(K97C) P450 BM3 HEME DOMAIN, A RUTHENIUM
TITLE 2 MODIFIED P450 BM3 MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BIFUNCTIONAL P-450/NADPH-P450 REDUCTASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 1-464;
COMPND 5 SYNONYM: CYTOCHROME P450(BM-3), CYTOCHROME P450BM-3, CYTOCHROME P450
COMPND 6 102, NADPH--CYTOCHROME P450 REDUCTASE;
COMPND 7 EC: 1.14.14.1;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS MEGATERIUM;
SOURCE 3 ORGANISM_TAXID: 1404;
SOURCE 4 GENE: CYP102, CYP102A1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PCWORI+
KEYWDS P450 BM3 HEME DOMAIN, MUTANT PROTEINS, ELECTRON TRANSFER,
KEYWDS 2 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.ENER,Y.-T.LEE,D.B.GOODIN,J.R.WINKLER,H.B.GRAY,L.CHERUZEL
REVDAT 2 06-SEP-23 3NPL 1 REMARK SEQADV LINK
REVDAT 1 25-AUG-10 3NPL 0
JRNL AUTH M.ENER,Y.-T.LEE,D.B.GOODIN,J.R.WINKLER,H.B.GRAY,L.CHERUZEL
JRNL TITL STRUCTURE OF RU(BPY)2(A-PHEN)(K97C) P450 BM3 HEME DOMAIN, A
JRNL TITL 2 RUTHENIUM MODIFIED P450 BM3 MUTANT
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 73020
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) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3677
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4745
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.90
REMARK 3 BIN R VALUE (WORKING SET) : 0.2730
REMARK 3 BIN FREE R VALUE SET COUNT : 226
REMARK 3 BIN FREE R VALUE : 0.3140
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7324
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 134
REMARK 3 SOLVENT ATOMS : 436
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.23000
REMARK 3 B22 (A**2) : 0.23000
REMARK 3 B33 (A**2) : -0.46000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.198
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.134
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.814
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.941
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.917
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7701 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10471 ; 1.375 ; 2.012
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 922 ; 5.885 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 374 ;36.786 ;24.759
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1353 ;15.510 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 43 ;11.669 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1102 ; 0.093 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5912 ; 0.006 ; 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): 4580 ; 0.642 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7404 ; 1.274 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3121 ; 1.893 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3061 ; 3.236 ; 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): NULL ; NULL ; NULL
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 : NULL
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 : 1.20
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 U VALUES: REFINED INDIVIDUALLY
REMARK 4
REMARK 4 3NPL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUN-10.
REMARK 100 THE DEPOSITION ID IS D_1000060120.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-MAR-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97946
REMARK 200 MONOCHROMATOR : SIDE SCATTERING I-BEAM BENT
REMARK 200 SINGLE CRYSTAL
REMARK 200 OPTICS : RH COATED FLAT MIRROR
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 3.2.25
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 74965
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 42.525
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 10.60
REMARK 200 R MERGE (I) : 0.12600
REMARK 200 R SYM (I) : 0.12600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 10.70
REMARK 200 R MERGE FOR SHELL (I) : 0.82700
REMARK 200 R SYM FOR SHELL (I) : 0.82700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.900
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 2UWH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 71.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M (NH4)2SO4, PH 8.4, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 136.92500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 58.53900
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 58.53900
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 68.46250
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 58.53900
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 58.53900
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 205.38750
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 58.53900
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 58.53900
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 68.46250
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 58.53900
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 58.53900
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 205.38750
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 136.92500
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 0
REMARK 465 THR A 1
REMARK 465 ILE A 2
REMARK 465 LYS A 3
REMARK 465 GLU A 4
REMARK 465 PRO A 461
REMARK 465 SER A 462
REMARK 465 THR A 463
REMARK 465 HIS A 464
REMARK 465 HIS A 465
REMARK 465 HIS A 466
REMARK 465 HIS A 467
REMARK 465 HIS A 468
REMARK 465 HIS A 469
REMARK 465 MET B 0
REMARK 465 THR B 1
REMARK 465 ILE B 2
REMARK 465 LYS B 3
REMARK 465 GLU B 4
REMARK 465 PRO B 461
REMARK 465 SER B 462
REMARK 465 THR B 463
REMARK 465 HIS B 464
REMARK 465 HIS B 465
REMARK 465 HIS B 466
REMARK 465 HIS B 467
REMARK 465 HIS B 468
REMARK 465 HIS B 469
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 15 -124.70 51.64
REMARK 500 PRO A 196 -11.00 -45.53
REMARK 500 HIS A 266 -43.58 -144.82
REMARK 500 LYS A 349 123.34 -36.97
REMARK 500 LEU A 437 -45.37 66.80
REMARK 500 LYS B 15 -123.63 43.68
REMARK 500 ASP B 84 44.68 -106.26
REMARK 500 HIS B 266 -36.54 -143.26
REMARK 500 THR B 436 57.13 -140.92
REMARK 500 LEU B 437 -25.59 68.87
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY B 46 ARG B 47 -149.63
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 500 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 400 SG
REMARK 620 2 HEM A 500 NA 99.7
REMARK 620 3 HEM A 500 NB 87.0 88.0
REMARK 620 4 HEM A 500 NC 84.2 176.0 91.2
REMARK 620 5 HEM A 500 ND 96.3 91.2 176.7 89.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 500 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 400 SG
REMARK 620 2 HEM B 500 NA 101.7
REMARK 620 3 HEM B 500 NB 86.1 91.3
REMARK 620 4 HEM B 500 NC 82.5 175.8 88.6
REMARK 620 5 HEM B 500 ND 96.9 89.1 176.8 90.7
REMARK 620 N 1 2 3 4
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 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 550
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RU8 B 501
DBREF 3NPL A 0 463 UNP P14779 CPXB_BACME 1 464
DBREF 3NPL B 0 463 UNP P14779 CPXB_BACME 1 464
SEQADV 3NPL ALA A 62 UNP P14779 CYS 63 ENGINEERED MUTATION
SEQADV 3NPL CYS A 97 UNP P14779 LYS 98 ENGINEERED MUTATION
SEQADV 3NPL SER A 156 UNP P14779 CYS 157 ENGINEERED MUTATION
SEQADV 3NPL HIS A 464 UNP P14779 EXPRESSION TAG
SEQADV 3NPL HIS A 465 UNP P14779 EXPRESSION TAG
SEQADV 3NPL HIS A 466 UNP P14779 EXPRESSION TAG
SEQADV 3NPL HIS A 467 UNP P14779 EXPRESSION TAG
SEQADV 3NPL HIS A 468 UNP P14779 EXPRESSION TAG
SEQADV 3NPL HIS A 469 UNP P14779 EXPRESSION TAG
SEQADV 3NPL ALA B 62 UNP P14779 CYS 63 ENGINEERED MUTATION
SEQADV 3NPL CYS B 97 UNP P14779 LYS 98 ENGINEERED MUTATION
SEQADV 3NPL SER B 156 UNP P14779 CYS 157 ENGINEERED MUTATION
SEQADV 3NPL HIS B 464 UNP P14779 EXPRESSION TAG
SEQADV 3NPL HIS B 465 UNP P14779 EXPRESSION TAG
SEQADV 3NPL HIS B 466 UNP P14779 EXPRESSION TAG
SEQADV 3NPL HIS B 467 UNP P14779 EXPRESSION TAG
SEQADV 3NPL HIS B 468 UNP P14779 EXPRESSION TAG
SEQADV 3NPL HIS B 469 UNP P14779 EXPRESSION TAG
SEQRES 1 A 470 MET THR ILE LYS GLU MET PRO GLN PRO LYS THR PHE GLY
SEQRES 2 A 470 GLU LEU LYS ASN LEU PRO LEU LEU ASN THR ASP LYS PRO
SEQRES 3 A 470 VAL GLN ALA LEU MET LYS ILE ALA ASP GLU LEU GLY GLU
SEQRES 4 A 470 ILE PHE LYS PHE GLU ALA PRO GLY ARG VAL THR ARG TYR
SEQRES 5 A 470 LEU SER SER GLN ARG LEU ILE LYS GLU ALA ALA ASP GLU
SEQRES 6 A 470 SER ARG PHE ASP LYS ASN LEU SER GLN ALA LEU LYS PHE
SEQRES 7 A 470 VAL ARG ASP PHE ALA GLY ASP GLY LEU PHE THR SER TRP
SEQRES 8 A 470 THR HIS GLU LYS ASN TRP CYS LYS ALA HIS ASN ILE LEU
SEQRES 9 A 470 LEU PRO SER PHE SER GLN GLN ALA MET LYS GLY TYR HIS
SEQRES 10 A 470 ALA MET MET VAL ASP ILE ALA VAL GLN LEU VAL GLN LYS
SEQRES 11 A 470 TRP GLU ARG LEU ASN ALA ASP GLU HIS ILE GLU VAL PRO
SEQRES 12 A 470 GLU ASP MET THR ARG LEU THR LEU ASP THR ILE GLY LEU
SEQRES 13 A 470 SER GLY PHE ASN TYR ARG PHE ASN SER PHE TYR ARG ASP
SEQRES 14 A 470 GLN PRO HIS PRO PHE ILE THR SER MET VAL ARG ALA LEU
SEQRES 15 A 470 ASP GLU ALA MET ASN LYS LEU GLN ARG ALA ASN PRO ASP
SEQRES 16 A 470 ASP PRO ALA TYR ASP GLU ASN LYS ARG GLN PHE GLN GLU
SEQRES 17 A 470 ASP ILE LYS VAL MET ASN ASP LEU VAL ASP LYS ILE ILE
SEQRES 18 A 470 ALA ASP ARG LYS ALA SER GLY GLU GLN SER ASP ASP LEU
SEQRES 19 A 470 LEU THR HIS MET LEU ASN GLY LYS ASP PRO GLU THR GLY
SEQRES 20 A 470 GLU PRO LEU ASP ASP GLU ASN ILE ARG TYR GLN ILE ILE
SEQRES 21 A 470 THR PHE LEU ILE ALA GLY HIS GLU THR THR SER GLY LEU
SEQRES 22 A 470 LEU SER PHE ALA LEU TYR PHE LEU VAL LYS ASN PRO HIS
SEQRES 23 A 470 VAL LEU GLN LYS ALA ALA GLU GLU ALA ALA ARG VAL LEU
SEQRES 24 A 470 VAL ASP PRO VAL PRO SER TYR LYS GLN VAL LYS GLN LEU
SEQRES 25 A 470 LYS TYR VAL GLY MET VAL LEU ASN GLU ALA LEU ARG LEU
SEQRES 26 A 470 TRP PRO THR ALA PRO ALA PHE SER LEU TYR ALA LYS GLU
SEQRES 27 A 470 ASP THR VAL LEU GLY GLY GLU TYR PRO LEU GLU LYS GLY
SEQRES 28 A 470 ASP GLU LEU MET VAL LEU ILE PRO GLN LEU HIS ARG ASP
SEQRES 29 A 470 LYS THR ILE TRP GLY ASP ASP VAL GLU GLU PHE ARG PRO
SEQRES 30 A 470 GLU ARG PHE GLU ASN PRO SER ALA ILE PRO GLN HIS ALA
SEQRES 31 A 470 PHE LYS PRO PHE GLY ASN GLY GLN ARG ALA CYS ILE GLY
SEQRES 32 A 470 GLN GLN PHE ALA LEU HIS GLU ALA THR LEU VAL LEU GLY
SEQRES 33 A 470 MET MET LEU LYS HIS PHE ASP PHE GLU ASP HIS THR ASN
SEQRES 34 A 470 TYR GLU LEU ASP ILE LYS GLU THR LEU THR LEU LYS PRO
SEQRES 35 A 470 GLU GLY PHE VAL VAL LYS ALA LYS SER LYS LYS ILE PRO
SEQRES 36 A 470 LEU GLY GLY ILE PRO SER PRO SER THR HIS HIS HIS HIS
SEQRES 37 A 470 HIS HIS
SEQRES 1 B 470 MET THR ILE LYS GLU MET PRO GLN PRO LYS THR PHE GLY
SEQRES 2 B 470 GLU LEU LYS ASN LEU PRO LEU LEU ASN THR ASP LYS PRO
SEQRES 3 B 470 VAL GLN ALA LEU MET LYS ILE ALA ASP GLU LEU GLY GLU
SEQRES 4 B 470 ILE PHE LYS PHE GLU ALA PRO GLY ARG VAL THR ARG TYR
SEQRES 5 B 470 LEU SER SER GLN ARG LEU ILE LYS GLU ALA ALA ASP GLU
SEQRES 6 B 470 SER ARG PHE ASP LYS ASN LEU SER GLN ALA LEU LYS PHE
SEQRES 7 B 470 VAL ARG ASP PHE ALA GLY ASP GLY LEU PHE THR SER TRP
SEQRES 8 B 470 THR HIS GLU LYS ASN TRP CYS LYS ALA HIS ASN ILE LEU
SEQRES 9 B 470 LEU PRO SER PHE SER GLN GLN ALA MET LYS GLY TYR HIS
SEQRES 10 B 470 ALA MET MET VAL ASP ILE ALA VAL GLN LEU VAL GLN LYS
SEQRES 11 B 470 TRP GLU ARG LEU ASN ALA ASP GLU HIS ILE GLU VAL PRO
SEQRES 12 B 470 GLU ASP MET THR ARG LEU THR LEU ASP THR ILE GLY LEU
SEQRES 13 B 470 SER GLY PHE ASN TYR ARG PHE ASN SER PHE TYR ARG ASP
SEQRES 14 B 470 GLN PRO HIS PRO PHE ILE THR SER MET VAL ARG ALA LEU
SEQRES 15 B 470 ASP GLU ALA MET ASN LYS LEU GLN ARG ALA ASN PRO ASP
SEQRES 16 B 470 ASP PRO ALA TYR ASP GLU ASN LYS ARG GLN PHE GLN GLU
SEQRES 17 B 470 ASP ILE LYS VAL MET ASN ASP LEU VAL ASP LYS ILE ILE
SEQRES 18 B 470 ALA ASP ARG LYS ALA SER GLY GLU GLN SER ASP ASP LEU
SEQRES 19 B 470 LEU THR HIS MET LEU ASN GLY LYS ASP PRO GLU THR GLY
SEQRES 20 B 470 GLU PRO LEU ASP ASP GLU ASN ILE ARG TYR GLN ILE ILE
SEQRES 21 B 470 THR PHE LEU ILE ALA GLY HIS GLU THR THR SER GLY LEU
SEQRES 22 B 470 LEU SER PHE ALA LEU TYR PHE LEU VAL LYS ASN PRO HIS
SEQRES 23 B 470 VAL LEU GLN LYS ALA ALA GLU GLU ALA ALA ARG VAL LEU
SEQRES 24 B 470 VAL ASP PRO VAL PRO SER TYR LYS GLN VAL LYS GLN LEU
SEQRES 25 B 470 LYS TYR VAL GLY MET VAL LEU ASN GLU ALA LEU ARG LEU
SEQRES 26 B 470 TRP PRO THR ALA PRO ALA PHE SER LEU TYR ALA LYS GLU
SEQRES 27 B 470 ASP THR VAL LEU GLY GLY GLU TYR PRO LEU GLU LYS GLY
SEQRES 28 B 470 ASP GLU LEU MET VAL LEU ILE PRO GLN LEU HIS ARG ASP
SEQRES 29 B 470 LYS THR ILE TRP GLY ASP ASP VAL GLU GLU PHE ARG PRO
SEQRES 30 B 470 GLU ARG PHE GLU ASN PRO SER ALA ILE PRO GLN HIS ALA
SEQRES 31 B 470 PHE LYS PRO PHE GLY ASN GLY GLN ARG ALA CYS ILE GLY
SEQRES 32 B 470 GLN GLN PHE ALA LEU HIS GLU ALA THR LEU VAL LEU GLY
SEQRES 33 B 470 MET MET LEU LYS HIS PHE ASP PHE GLU ASP HIS THR ASN
SEQRES 34 B 470 TYR GLU LEU ASP ILE LYS GLU THR LEU THR LEU LYS PRO
SEQRES 35 B 470 GLU GLY PHE VAL VAL LYS ALA LYS SER LYS LYS ILE PRO
SEQRES 36 B 470 LEU GLY GLY ILE PRO SER PRO SER THR HIS HIS HIS HIS
SEQRES 37 B 470 HIS HIS
HET HEM A 500 43
HET SO4 A 550 5
HET HEM B 500 43
HET RU8 B 501 43
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM SO4 SULFATE ION
HETNAM RU8 BIS(2,2'-BIPYRIDINE-KAPPA~2~N~1~,N~1'~)[2-IODO-N-(1,10-
HETNAM 2 RU8 PHENANTHROLIN-5-YL-KAPPA~2~N~1~,N~10~)
HETNAM 3 RU8 ACETAMIDE]RUTHENIUM(2+)
HETSYN HEM HEME
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 4 SO4 O4 S 2-
FORMUL 6 RU8 C34 H26 I N7 O RU 2+
FORMUL 7 HOH *436(H2 O)
HELIX 1 1 PHE A 11 LYS A 15 5 5
HELIX 2 2 ASN A 16 ASN A 21 5 6
HELIX 3 3 LYS A 24 GLY A 37 1 14
HELIX 4 4 SER A 54 ALA A 62 1 9
HELIX 5 5 SER A 72 GLY A 83 1 12
HELIX 6 6 GLU A 93 LEU A 104 1 12
HELIX 7 7 PRO A 105 PHE A 107 5 3
HELIX 8 8 SER A 108 ARG A 132 1 25
HELIX 9 9 VAL A 141 ASN A 159 1 19
HELIX 10 10 ASN A 163 ARG A 167 5 5
HELIX 11 11 HIS A 171 ARG A 190 1 20
HELIX 12 12 ASP A 195 ALA A 197 5 3
HELIX 13 13 TYR A 198 ALA A 225 1 28
HELIX 14 14 ASP A 232 GLY A 240 1 9
HELIX 15 15 ASP A 250 GLY A 265 1 16
HELIX 16 16 HIS A 266 LYS A 282 1 17
HELIX 17 17 ASN A 283 LEU A 298 1 16
HELIX 18 18 SER A 304 GLN A 310 1 7
HELIX 19 19 LEU A 311 TRP A 325 1 15
HELIX 20 20 ILE A 357 HIS A 361 1 5
HELIX 21 21 ASP A 363 GLY A 368 1 6
HELIX 22 22 ARG A 375 GLU A 380 5 6
HELIX 23 23 ASN A 381 ILE A 385 5 5
HELIX 24 24 ASN A 395 ALA A 399 5 5
HELIX 25 25 GLY A 402 HIS A 420 1 19
HELIX 26 26 PHE B 11 LYS B 15 5 5
HELIX 27 27 ASN B 16 ASN B 21 5 6
HELIX 28 28 LYS B 24 GLY B 37 1 14
HELIX 29 29 SER B 54 ALA B 62 1 9
HELIX 30 30 SER B 72 GLY B 83 1 12
HELIX 31 31 GLU B 93 LEU B 104 1 12
HELIX 32 32 PRO B 105 PHE B 107 5 3
HELIX 33 33 SER B 108 ARG B 132 1 25
HELIX 34 34 VAL B 141 ASN B 159 1 19
HELIX 35 35 ASN B 163 ARG B 167 5 5
HELIX 36 36 HIS B 171 LEU B 188 1 18
HELIX 37 37 ASP B 195 ALA B 197 5 3
HELIX 38 38 TYR B 198 ALA B 225 1 28
HELIX 39 39 ASP B 232 GLY B 240 1 9
HELIX 40 40 ASP B 250 GLY B 265 1 16
HELIX 41 41 HIS B 266 ASN B 283 1 18
HELIX 42 42 ASN B 283 LEU B 298 1 16
HELIX 43 43 SER B 304 GLN B 310 1 7
HELIX 44 44 LEU B 311 TRP B 325 1 15
HELIX 45 45 ILE B 357 HIS B 361 1 5
HELIX 46 46 ASP B 363 GLY B 368 1 6
HELIX 47 47 ARG B 375 GLU B 380 5 6
HELIX 48 48 ASN B 381 ILE B 385 5 5
HELIX 49 49 ASN B 395 ALA B 399 5 5
HELIX 50 50 GLY B 402 HIS B 420 1 19
SHEET 1 A 5 ILE A 39 ALA A 44 0
SHEET 2 A 5 ARG A 47 LEU A 52 -1 O THR A 49 N PHE A 42
SHEET 3 A 5 GLU A 352 LEU A 356 1 O MET A 354 N LEU A 52
SHEET 4 A 5 ALA A 330 ALA A 335 -1 N PHE A 331 O VAL A 355
SHEET 5 A 5 PHE A 67 LYS A 69 -1 N ASP A 68 O TYR A 334
SHEET 1 B 3 ILE A 139 GLU A 140 0
SHEET 2 B 3 VAL A 445 SER A 450 -1 O VAL A 446 N ILE A 139
SHEET 3 B 3 PHE A 421 GLU A 424 -1 N ASP A 422 O LYS A 449
SHEET 1 C 2 THR A 339 LEU A 341 0
SHEET 2 C 2 TYR A 345 LEU A 347 -1 O LEU A 347 N THR A 339
SHEET 1 D 2 ILE A 433 GLU A 435 0
SHEET 2 D 2 LEU A 439 PRO A 441 -1 O LYS A 440 N LYS A 434
SHEET 1 E 5 ILE B 39 ALA B 44 0
SHEET 2 E 5 ARG B 47 LEU B 52 -1 O THR B 49 N PHE B 42
SHEET 3 E 5 GLU B 352 LEU B 356 1 O MET B 354 N LEU B 52
SHEET 4 E 5 ALA B 330 ALA B 335 -1 N PHE B 331 O VAL B 355
SHEET 5 E 5 PHE B 67 ASN B 70 -1 N ASN B 70 O SER B 332
SHEET 1 F 3 ILE B 139 GLU B 140 0
SHEET 2 F 3 VAL B 445 SER B 450 -1 O VAL B 446 N ILE B 139
SHEET 3 F 3 PHE B 421 GLU B 424 -1 N ASP B 422 O LYS B 449
SHEET 1 G 2 THR B 339 LEU B 341 0
SHEET 2 G 2 TYR B 345 LEU B 347 -1 O LEU B 347 N THR B 339
SHEET 1 H 2 ILE B 433 GLU B 435 0
SHEET 2 H 2 LEU B 439 PRO B 441 -1 O LYS B 440 N LYS B 434
LINK SG CYS B 97 C49 RU8 B 501 1555 1555 1.80
LINK SG CYS A 400 FE HEM A 500 1555 1555 2.18
LINK SG CYS B 400 FE HEM B 500 1555 1555 2.32
SITE 1 AC1 24 LYS A 69 LEU A 86 PHE A 87 TRP A 96
SITE 2 AC1 24 ALA A 264 GLY A 265 THR A 268 THR A 269
SITE 3 AC1 24 THR A 327 PHE A 331 PRO A 392 PHE A 393
SITE 4 AC1 24 GLY A 394 ARG A 398 ALA A 399 CYS A 400
SITE 5 AC1 24 ILE A 401 GLY A 402 HOH A 601 HOH A 603
SITE 6 AC1 24 HOH A 626 HOH A 630 HOH A 661 HOH A 694
SITE 1 AC2 3 LYS A 41 ARG A 50 HOH A 664
SITE 1 AC3 25 LYS B 69 LEU B 86 PHE B 87 TRP B 96
SITE 2 AC3 25 ALA B 264 GLY B 265 THR B 268 THR B 269
SITE 3 AC3 25 THR B 327 PHE B 331 PRO B 392 PHE B 393
SITE 4 AC3 25 GLY B 394 ARG B 398 ALA B 399 CYS B 400
SITE 5 AC3 25 ILE B 401 GLY B 402 ALA B 406 HOH B 602
SITE 6 AC3 25 HOH B 611 HOH B 655 HOH B 680 HOH B 749
SITE 7 AC3 25 HOH B 759
SITE 1 AC4 11 ASN A 70 TRP A 90 TYR A 334 LYS A 336
SITE 2 AC4 11 GLY A 350 GLU A 352 TRP B 96 CYS B 97
SITE 3 AC4 11 ASN B 101 GLU B 244 HOH B 717
CRYST1 117.078 117.078 273.850 90.00 90.00 90.00 P 41 21 2 16
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 0.008541 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008541 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003652 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
