HEADER ELECTRON TRANSPORT 14-JAN-08 3BXU
TITLE PPCB, A CYTOCHROME C7 FROM GEOBACTER SULFURREDUCENS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C3;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GEOBACTER SULFURREDUCENS;
SOURCE 3 GENE: CYD-1;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS MULTIHEME CYTOCHROMES, CYTOCHROME C7 GEOBACTER SULFURREDUCENS,
KEYWDS 2 ELECTRON TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR P.R.POKKULURI,M.SCHIFFER
REVDAT 4 21-FEB-24 3BXU 1 REMARK
REVDAT 3 24-FEB-09 3BXU 1 VERSN
REVDAT 2 02-SEP-08 3BXU 1 JRNL
REVDAT 1 01-JUL-08 3BXU 0
JRNL AUTH L.MORGADO,M.BRUIX,V.ORSHONSKY,Y.Y.LONDER,N.E.DUKE,X.YANG,
JRNL AUTH 2 P.R.POKKULURI,M.SCHIFFER,C.A.SALGUEIRO
JRNL TITL STRUCTURAL INSIGHTS INTO THE MODULATION OF THE REDOX
JRNL TITL 2 PROPERTIES OF TWO GEOBACTER SULFURREDUCENS HOMOLOGOUS
JRNL TITL 3 TRIHEME CYTOCHROMES.
JRNL REF BIOCHIM.BIOPHYS.ACTA V.1777 1157 2008
JRNL REFN ISSN 0006-3002
JRNL PMID 18534185
JRNL DOI 10.1016/J.BBABIO.2008.04.043
REMARK 2
REMARK 2 RESOLUTION. 1.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
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) : 1.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.07
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.0
REMARK 3 NUMBER OF REFLECTIONS : 27324
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) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.162
REMARK 3 FREE R VALUE : 0.186
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 3006
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) : 1.35
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.39
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1286
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2190
REMARK 3 BIN FREE R VALUE SET COUNT : 124
REMARK 3 BIN FREE R VALUE : 0.2480
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1068
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 263
REMARK 3 SOLVENT ATOMS : 201
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 7.75
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.05000
REMARK 3 B22 (A**2) : 0.06000
REMARK 3 B33 (A**2) : -0.01000
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): 0.078
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.063
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.038
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.931
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.956
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1406 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1109 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1963 ; 1.648 ; 2.508
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2609 ; 1.877 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 142 ; 6.201 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 150 ; 0.101 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1478 ; 0.015 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 190 ; 0.029 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 410 ; 0.404 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1368 ; 0.240 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 648 ; 0.092 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 140 ; 0.161 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 1 ; 0.016 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 22 ; 0.180 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 84 ; 0.235 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 41 ; 0.221 ; 0.200
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): 704 ; 0.944 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1123 ; 1.491 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 702 ; 1.968 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 838 ; 2.706 ; 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): 1406 ; 1.067 ; 2.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 201 ; 3.117 ; 2.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 1341 ; 1.741 ; 2.000
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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 74
REMARK 3 ORIGIN FOR THE GROUP (A): 7.3736 -0.9147 11.8341
REMARK 3 T TENSOR
REMARK 3 T11: 0.0214 T22: 0.0055
REMARK 3 T33: 0.0098 T12: 0.0030
REMARK 3 T13: -0.0017 T23: -0.0031
REMARK 3 L TENSOR
REMARK 3 L11: 2.0909 L22: 1.0526
REMARK 3 L33: 1.0900 L12: -0.3444
REMARK 3 L13: 0.0260 L23: -0.4231
REMARK 3 S TENSOR
REMARK 3 S11: -0.0176 S12: 0.0079 S13: -0.0056
REMARK 3 S21: -0.0306 S22: 0.0776 S23: -0.0035
REMARK 3 S31: 0.0108 S32: -0.0715 S33: -0.0600
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 74
REMARK 3 ORIGIN FOR THE GROUP (A): -7.7491 -0.6995 -10.1498
REMARK 3 T TENSOR
REMARK 3 T11: 0.0230 T22: 0.0060
REMARK 3 T33: 0.0179 T12: -0.0110
REMARK 3 T13: -0.0044 T23: 0.0057
REMARK 3 L TENSOR
REMARK 3 L11: 1.7063 L22: 0.6039
REMARK 3 L33: 1.4389 L12: -0.4625
REMARK 3 L13: -0.4148 L23: -0.0180
REMARK 3 S TENSOR
REMARK 3 S11: -0.0083 S12: -0.0176 S13: -0.0109
REMARK 3 S21: 0.0144 S22: 0.0321 S23: -0.0138
REMARK 3 S31: 0.0274 S32: -0.0276 S33: -0.0238
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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:
REMARK 3 THE NUMBER OF UNIQUE MEASURED REFLECTIONS IS TOO LARGE BECAUSE THE
REMARK 3 BIJVOET PAIRS ARE TREATED AS SEPARATE REFLECTIONS WITH THE SCALE
REMARK 3 ANOMALOUS OPTION IN HKL2000. THE FOLLOWING SIDE CHAIN ATOMS ARE IN
REMARK 3 WEAK DENSITY AND ARE PROBABLY
REMARK 3 DISORDERED.
REMARK 3
REMARK 3 ON CHAIN A,
REMARK 3 ASP2: OD1;
REMARK 3 LYS9: CD, CE, NZ;
REMARK 3 LYS18: CD, CE, NZ;
REMARK 3 LYS19: CD, CE, NZ;
REMARK 3 LYS33: CD, CE, NZ;
REMARK 3 LYS49: CD, CE, NZ;
REMARK 3 LYS52: NZ;
REMARK 3 GLU56: CD, OE1, OE2;
REMARK 3 LYS60: CD, CE, NZ;
REMARK 3 LYS70: CG, CD, CE, NZ;
REMARK 3 LYS71: CB, CG, CD, CE, NZ;
REMARK 3
REMARK 3 ON CHAIN B,
REMARK 3 LYS9: CG, CD, CE, NZ;
REMARK 3 LSY18: NZ;
REMARK 3 LYS33: CE, NZ;
REMARK 3 LYS37: CE, NZ;
REMARK 3 MET58: SD, CE;
REMARK 3 LYS60: CG, CD, CE, NZ.
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
REMARK 4
REMARK 4 3BXU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JAN-08.
REMARK 100 THE DEPOSITION ID IS D_1000046091.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-DEC-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.73766, 1.73859, 1.78875
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : CUSTOM-MADE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58322
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.350
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.0
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.08900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 62.0
REMARK 200 DATA REDUNDANCY IN SHELL : 1.60
REMARK 200 R MERGE FOR SHELL (I) : 0.34200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 45% JEFFAMINE ED-2001 0.2 M AMMONIUM
REMARK 280 IODIDE, PH 7.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
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 17.10000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 44.45000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 23.75000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 44.45000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 17.10000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 23.75000
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 300 REMARK: BIOLOGICAL UNIT OF PPCB IS UNKNOWN. IT APPEARS TO BE A
REMARK 300 DIMER IN THE CRYSTAL WITH A BURIED SURFACE AREA OF 1190 SQUARE
REMARK 300 ANGSTROM CALCULATED WITH THE PROGRAM SURFACE (CCP4).
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8270 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8660 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -152.7 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 SG CYS B 51 CAB HEM B 73 1.81
REMARK 500 SG CYS A 51 CAB HEM A 73 1.87
REMARK 500 O HOH B 119 O HOH B 172 1.90
REMARK 500 SG CYS B 65 CAB HEM B 74 1.91
REMARK 500 SG CYS A 27 CAB HEM A 72 1.94
REMARK 500 SG CYS B 54 CAC HEM B 73 1.94
REMARK 500 SG CYS B 68 CAC HEM B 74 1.97
REMARK 500 SG CYS A 30 CAC HEM A 72 1.97
REMARK 500 SG CYS B 27 CAB HEM B 72 1.98
REMARK 500 O HOH A 178 O HOH B 86 2.00
REMARK 500 SG CYS A 54 CAC HEM A 73 2.01
REMARK 500 SG CYS B 30 CAC HEM B 72 2.06
REMARK 500 SG CYS A 65 CAB HEM A 74 2.07
REMARK 500 SG CYS A 68 CAC HEM A 74 2.08
REMARK 500 O HOH B 86 O HOH B 112 2.12
REMARK 500 O HOH A 99 O HOH A 175 2.16
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 ASP A 26 CB - CG - OD2 ANGL. DEV. = 7.7 DEGREES
REMARK 500 GLU A 56 CA - CB - CG ANGL. DEV. = 15.9 DEGREES
REMARK 500 ASP B 26 CB - CG - OD2 ANGL. DEV. = 5.8 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 ASP A 2 -46.04 159.20
REMARK 500 CYS A 51 -77.87 -136.84
REMARK 500 PRO B 25 27.85 -78.77
REMARK 500 PRO B 25 47.29 -86.46
REMARK 500 CYS B 51 -77.56 -138.73
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 72 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 17 NE2
REMARK 620 2 HEM A 72 NA 90.4
REMARK 620 3 HEM A 72 NB 92.0 90.9
REMARK 620 4 HEM A 72 NC 90.8 178.7 89.5
REMARK 620 5 HEM A 72 ND 89.6 88.3 178.3 91.2
REMARK 620 6 HIS A 31 NE2 179.5 89.5 88.5 89.4 89.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 73 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 20 NE2
REMARK 620 2 HEM A 73 NA 88.1
REMARK 620 3 HEM A 73 NB 91.9 89.6
REMARK 620 4 HEM A 73 NC 91.4 179.5 90.4
REMARK 620 5 HEM A 73 ND 88.5 90.1 179.5 89.9
REMARK 620 6 HIS A 55 NE2 179.0 92.8 88.0 87.7 91.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 74 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 47 NE2
REMARK 620 2 HEM A 74 NA 89.4
REMARK 620 3 HEM A 74 NB 85.2 90.0
REMARK 620 4 HEM A 74 NC 89.8 178.6 88.8
REMARK 620 5 HEM A 74 ND 96.0 89.8 178.8 91.5
REMARK 620 6 HIS A 69 NE2 170.4 94.3 85.9 86.3 92.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 72 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 17 NE2
REMARK 620 2 HEM B 72 NA 90.8
REMARK 620 3 HEM B 72 NB 90.0 91.5
REMARK 620 4 HEM B 72 NC 91.0 178.2 88.3
REMARK 620 5 HEM B 72 ND 91.1 89.4 178.6 90.7
REMARK 620 6 HIS B 31 NE2 179.0 89.5 89.0 88.8 89.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 73 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 20 NE2
REMARK 620 2 HEM B 73 NA 89.8
REMARK 620 3 HEM B 73 NB 89.7 88.9
REMARK 620 4 HEM B 73 NC 91.3 178.5 90.0
REMARK 620 5 HEM B 73 ND 90.3 90.3 179.2 90.7
REMARK 620 6 HIS B 55 NE2 177.0 89.3 93.1 89.6 86.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 74 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 47 NE2
REMARK 620 2 HEM B 74 NA 89.4
REMARK 620 3 HEM B 74 NB 85.4 89.0
REMARK 620 4 HEM B 74 NC 90.1 179.4 90.8
REMARK 620 5 HEM B 74 ND 94.6 91.0 180.0 89.2
REMARK 620 6 HIS B 69 NE2 175.0 89.1 89.8 91.5 90.2
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 SO4 A 75
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 72
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 73
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 74
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 72
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 73
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 74
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1OS6 RELATED DB: PDB
REMARK 900 CYTOCHROME C7 (PPCA) FROM GEOBACTER SULFURREDUCENS
DBREF 3BXU A 1 71 UNP Q74G83 Q74G83_GEOSL 21 91
DBREF 3BXU B 1 71 UNP Q74G83 Q74G83_GEOSL 21 91
SEQRES 1 A 71 ALA ASP THR MET THR PHE THR ALA LYS ASN GLY ASN VAL
SEQRES 2 A 71 THR PHE ASP HIS LYS LYS HIS GLN THR ILE VAL PRO ASP
SEQRES 3 A 71 CYS ALA VAL CYS HIS GLY LYS THR PRO GLY LYS ILE GLU
SEQRES 4 A 71 GLY PHE GLY LYS GLU MET ALA HIS GLY LYS SER CYS LYS
SEQRES 5 A 71 GLY CYS HIS GLU GLU MET LYS LYS GLY PRO THR LYS CYS
SEQRES 6 A 71 GLY GLU CYS HIS LYS LYS
SEQRES 1 B 71 ALA ASP THR MET THR PHE THR ALA LYS ASN GLY ASN VAL
SEQRES 2 B 71 THR PHE ASP HIS LYS LYS HIS GLN THR ILE VAL PRO ASP
SEQRES 3 B 71 CYS ALA VAL CYS HIS GLY LYS THR PRO GLY LYS ILE GLU
SEQRES 4 B 71 GLY PHE GLY LYS GLU MET ALA HIS GLY LYS SER CYS LYS
SEQRES 5 B 71 GLY CYS HIS GLU GLU MET LYS LYS GLY PRO THR LYS CYS
SEQRES 6 B 71 GLY GLU CYS HIS LYS LYS
HET SO4 A 75 5
HET HEM A 72 43
HET HEM A 73 43
HET HEM A 74 43
HET HEM B 72 43
HET HEM B 73 43
HET HEM B 74 43
HETNAM SO4 SULFATE ION
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN HEM HEME
FORMUL 3 SO4 O4 S 2-
FORMUL 4 HEM 6(C34 H32 FE N4 O4)
FORMUL 10 HOH *201(H2 O)
HELIX 1 1 ASP A 16 VAL A 24 1 9
HELIX 2 2 CYS A 27 GLY A 32 1 6
HELIX 3 3 GLY A 42 GLY A 48 1 7
HELIX 4 4 CYS A 51 LYS A 59 1 9
HELIX 5 5 LYS A 64 CYS A 68 1 5
HELIX 6 6 HIS B 17 VAL B 24 1 8
HELIX 7 7 CYS B 27 GLY B 32 1 6
HELIX 8 8 GLY B 42 GLY B 48 1 7
HELIX 9 9 CYS B 51 LYS B 59 1 9
HELIX 10 10 LYS B 64 HIS B 69 1 6
SHEET 1 A 3 MET A 4 PHE A 6 0
SHEET 2 A 3 ASN A 12 PHE A 15 -1 O VAL A 13 N PHE A 6
SHEET 3 A 3 HIS A 69 LYS A 70 -1 O LYS A 70 N ASN A 12
SHEET 1 B 2 THR B 3 PHE B 6 0
SHEET 2 B 2 VAL B 13 ASP B 16 -1 O PHE B 15 N MET B 4
LINK NE2 HIS A 17 FE HEM A 72 1555 1555 2.02
LINK NE2 HIS A 20 FE HEM A 73 1555 1555 2.06
LINK NE2 HIS A 31 FE HEM A 72 1555 1555 2.02
LINK NE2 HIS A 47 FE HEM A 74 1555 1555 2.01
LINK NE2 HIS A 55 FE HEM A 73 1555 1555 2.03
LINK NE2 HIS A 69 FE HEM A 74 1555 1555 1.97
LINK NE2 HIS B 17 FE HEM B 72 1555 1555 2.05
LINK NE2 HIS B 20 FE HEM B 73 1555 1555 2.05
LINK NE2 HIS B 31 FE HEM B 72 1555 1555 2.01
LINK NE2 HIS B 47 FE HEM B 74 1555 1555 1.99
LINK NE2 HIS B 55 FE HEM B 73 1555 1555 2.01
LINK NE2 HIS B 69 FE HEM B 74 1555 1555 2.04
SITE 1 AC1 2 GLY A 42 LYS A 43
SITE 1 AC2 12 MET A 4 HIS A 17 GLN A 21 CYS A 27
SITE 2 AC2 12 CYS A 30 HIS A 31 PRO A 35 GLY A 36
SITE 3 AC2 12 LYS A 37 ILE A 38 ASN B 12 GLN B 21
SITE 1 AC3 11 PHE A 15 LYS A 19 HIS A 20 ILE A 23
SITE 2 AC3 11 SER A 50 CYS A 51 CYS A 54 HIS A 55
SITE 3 AC3 11 LYS A 60 PRO A 62 LYS B 19
SITE 1 AC4 13 PHE A 6 THR A 7 ALA A 8 LYS A 9
SITE 2 AC4 13 ASN A 10 LYS A 43 ALA A 46 HIS A 47
SITE 3 AC4 13 THR A 63 LYS A 64 CYS A 65 CYS A 68
SITE 4 AC4 13 HIS A 69
SITE 1 AC5 13 ASN A 12 GLN A 21 MET B 4 PHE B 15
SITE 2 AC5 13 HIS B 17 GLN B 21 CYS B 27 CYS B 30
SITE 3 AC5 13 HIS B 31 PRO B 35 GLY B 36 LYS B 37
SITE 4 AC5 13 ILE B 38
SITE 1 AC6 11 LYS A 60 THR B 14 PHE B 15 LYS B 19
SITE 2 AC6 11 HIS B 20 SER B 50 CYS B 51 CYS B 54
SITE 3 AC6 11 HIS B 55 LYS B 60 PRO B 62
SITE 1 AC7 16 THR A 7 GLY A 40 MET A 45 PHE B 6
SITE 2 AC7 16 THR B 7 ALA B 8 LYS B 9 ASN B 10
SITE 3 AC7 16 GLY B 42 LYS B 43 ALA B 46 HIS B 47
SITE 4 AC7 16 LYS B 64 CYS B 65 CYS B 68 HIS B 69
CRYST1 34.200 47.500 88.900 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 0.029240 0.000000 0.000000 0.00000
SCALE2 0.000000 0.021053 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011249 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
