HEADER ELECTRON TRANSPORT 20-APR-09 3H4N
TITLE PPCD, A CYTOCHROME C7 FROM GEOBACTER SULFURREDUCENS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C7;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CYTOCHROME C3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GEOBACTER SULFURREDUCENS;
SOURCE 3 ORGANISM_TAXID: 35554;
SOURCE 4 GENE: CYD-4, GSU1024;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: JCB7123
KEYWDS CYTOCHROME C7, MULTIHEME CYTOCHROME, GEOBACTER SULFURREDUCENS,
KEYWDS 2 ELECTRON TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR P.R.POKKULURI,M.SCHIFFER
REVDAT 5 21-FEB-24 3H4N 1 REMARK
REVDAT 4 24-JUL-19 3H4N 1 REMARK
REVDAT 3 25-OCT-17 3H4N 1 REMARK
REVDAT 2 28-APR-10 3H4N 1 JRNL
REVDAT 1 29-DEC-09 3H4N 0
JRNL AUTH P.R.POKKULURI,Y.Y.LONDER,X.YANG,N.E.DUKE,J.ERICKSON,
JRNL AUTH 2 V.ORSHONSKY,G.JOHNSON,M.SCHIFFER
JRNL TITL STRUCTURAL CHARACTERIZATION OF A FAMILY OF CYTOCHROMES C(7)
JRNL TITL 2 INVOLVED IN FE(III) RESPIRATION BY GEOBACTER SULFURREDUCENS.
JRNL REF BIOCHIM.BIOPHYS.ACTA V.1797 222 2010
JRNL REFN ISSN 0006-3002
JRNL PMID 19857457
JRNL DOI 10.1016/J.BBABIO.2009.10.007
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) : 36.04
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 28548
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) : 0.152
REMARK 3 R VALUE (WORKING SET) : 0.149
REMARK 3 FREE R VALUE : 0.173
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.800
REMARK 3 FREE R VALUE TEST SET COUNT : 3111
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) : 1630
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.1320
REMARK 3 BIN FREE R VALUE SET COUNT : 163
REMARK 3 BIN FREE R VALUE : 0.1570
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1005
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 258
REMARK 3 SOLVENT ATOMS : 195
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 8.87
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.36000
REMARK 3 B22 (A**2) : 0.43000
REMARK 3 B33 (A**2) : -0.07000
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): 0.068
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.056
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.030
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.697
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.955
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1419 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1159 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1973 ; 1.413 ; 2.510
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2748 ; 0.865 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 136 ; 5.232 ; 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): 153 ; 0.081 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1457 ; 0.011 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 178 ; 0.018 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 380 ; 0.428 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1355 ; 0.244 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 637 ; 0.083 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 115 ; 0.176 ; 0.200
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): 15 ; 0.149 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 92 ; 0.246 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 27 ; 0.128 ; 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): 679 ; 0.891 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1089 ; 1.462 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 740 ; 1.696 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 883 ; 2.362 ; 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): 1419 ; 0.980 ; 2.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 195 ; 2.572 ; 2.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 1358 ; 1.413 ; 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 4 A 75
REMARK 3 ORIGIN FOR THE GROUP (A): 11.2871 3.4181 6.7204
REMARK 3 T TENSOR
REMARK 3 T11: 0.0183 T22: 0.0016
REMARK 3 T33: 0.0100 T12: -0.0053
REMARK 3 T13: -0.0045 T23: 0.0021
REMARK 3 L TENSOR
REMARK 3 L11: 1.3495 L22: 0.5571
REMARK 3 L33: 0.5731 L12: -0.2371
REMARK 3 L13: -0.4005 L23: 0.2346
REMARK 3 S TENSOR
REMARK 3 S11: 0.0046 S12: -0.0600 S13: 0.0116
REMARK 3 S21: 0.0193 S22: -0.0095 S23: 0.0023
REMARK 3 S31: 0.0008 S32: 0.0296 S33: 0.0048
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 4 B 75
REMARK 3 ORIGIN FOR THE GROUP (A): 4.4214 5.3074 31.3540
REMARK 3 T TENSOR
REMARK 3 T11: 0.0152 T22: 0.0183
REMARK 3 T33: 0.0023 T12: 0.0080
REMARK 3 T13: 0.0039 T23: 0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 1.2289 L22: 0.5850
REMARK 3 L33: 0.2710 L12: 0.1301
REMARK 3 L13: -0.1256 L23: -0.1562
REMARK 3 S TENSOR
REMARK 3 S11: 0.0353 S12: 0.1042 S13: 0.0324
REMARK 3 S21: -0.0140 S22: -0.0189 S23: 0.0007
REMARK 3 S31: -0.0040 S32: -0.0410 S33: -0.0164
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3H4N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-MAY-09.
REMARK 100 THE DEPOSITION ID IS D_1000052686.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-AUG-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) : 1.74041, 1.73818, 1.78832,
REMARK 200 1.69077, 1.0332
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 : 60576
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.340
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 (%) : 97.0
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.04700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 42.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.34
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.39
REMARK 200 COMPLETENESS FOR SHELL (%) : 79.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.14700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 8.400
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 (%): 47.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTAL OBTAINED FROM INDEX SCREEN-95
REMARK 280 (30% PEG MONOMETHYLETHER 2000, 0.1 M POTASSIUM THIOCYANATE), PH
REMARK 280 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 13.70000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 47.40000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.95000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 47.40000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 13.70000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 27.95000
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 300 REMARK: TWO MOLECULES PER ASYMMETRIC UNIT; MONOMER IN SOLUTION
REMARK 300 BASED ON SIZE EXCLUSION COLUMN CHROMATOGRAPHY AND DYNAMIC LIGHT
REMARK 300 SCATTERING
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 HIS A 0
REMARK 465 ASP A 1
REMARK 465 LYS A 2
REMARK 465 LYS A 71
REMARK 465 HIS B 0
REMARK 465 ASP B 1
REMARK 465 LYS B 71
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 A 65 CAB HEM A 74 1.91
REMARK 500 SG CYS B 51 CAB HEM B 73 1.92
REMARK 500 SG CYS A 51 CAB HEM A 73 1.92
REMARK 500 SG CYS A 27 CAB HEM A 72 1.93
REMARK 500 SG CYS B 65 CAB HEM B 74 1.94
REMARK 500 SG CYS A 30 CAC HEM A 72 1.94
REMARK 500 SG CYS A 54 CAC HEM A 73 1.94
REMARK 500 SG CYS B 27 CAB HEM B 72 1.94
REMARK 500 SG CYS B 30 CAC HEM B 72 1.97
REMARK 500 SG CYS B 54 CAC HEM B 73 2.01
REMARK 500 SG CYS A 68 CAC HEM A 74 2.02
REMARK 500 SD MET B 58 O HOH B 79 2.04
REMARK 500 SG CYS B 68 CAC HEM B 74 2.06
REMARK 500 OE2 GLU A 32 O HOH A 123 2.16
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 GLU A 26 -125.01 46.00
REMARK 500 GLU B 26 -132.14 50.16
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 91.4
REMARK 620 3 HEM A 72 NB 92.9 89.7
REMARK 620 4 HEM A 72 NC 90.2 178.4 89.6
REMARK 620 5 HEM A 72 ND 88.8 89.5 178.1 91.1
REMARK 620 6 HIS A 31 NE2 175.5 90.6 91.2 88.0 87.1
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 91.4
REMARK 620 3 HEM A 73 NB 90.0 89.5
REMARK 620 4 HEM A 73 NC 89.5 179.0 90.2
REMARK 620 5 HEM A 73 ND 90.3 91.0 179.5 89.3
REMARK 620 6 HIS A 55 NE2 178.4 90.1 90.5 89.0 89.2
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 89.0
REMARK 620 3 HEM A 74 NB 87.2 89.2
REMARK 620 4 HEM A 74 NC 92.4 178.4 91.7
REMARK 620 5 HEM A 74 ND 94.8 90.1 178.0 88.9
REMARK 620 6 HIS A 69 NE2 176.1 88.8 89.5 89.8 88.5
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 89.4
REMARK 620 3 HEM B 72 NB 89.8 90.7
REMARK 620 4 HEM B 72 NC 91.3 179.2 89.6
REMARK 620 5 HEM B 72 ND 91.6 88.5 178.3 91.2
REMARK 620 6 HIS B 31 NE2 177.5 88.7 88.6 90.5 90.0
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 90.0
REMARK 620 3 HEM B 73 NB 91.4 89.2
REMARK 620 4 HEM B 73 NC 90.0 179.6 91.1
REMARK 620 5 HEM B 73 ND 89.2 90.2 179.2 89.4
REMARK 620 6 HIS B 55 NE2 175.9 94.1 88.2 85.9 91.3
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 92.3
REMARK 620 3 HEM B 74 NB 87.4 90.2
REMARK 620 4 HEM B 74 NC 87.8 178.8 90.9
REMARK 620 5 HEM B 74 ND 93.2 89.7 179.5 89.2
REMARK 620 6 HIS B 69 NE2 177.5 87.8 90.1 92.2 89.4
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 HEM A 72
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 73
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 74
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 72
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 73
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
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 FROM GEOBACTER SULFURREDUCENS
REMARK 900 RELATED ID: 3BXU RELATED DB: PDB
REMARK 900 CYTOCHROME C7 FROM GEOBACTER SULFURREDUCENS
REMARK 900 RELATED ID: 3H33 RELATED DB: PDB
REMARK 900 CYTOCHROME C7 FROM GEOBACTER SULFURREDUCENS
REMARK 900 RELATED ID: 3H34 RELATED DB: PDB
REMARK 900 CYTOCHROME C7 FROM GEOBACTER SULFURREDUCENS
DBREF 3H4N A 0 71 UNP Q74ED8 Q74ED8_GEOSL 21 92
DBREF 3H4N B 0 71 UNP Q74ED8 Q74ED8_GEOSL 21 92
SEQRES 1 A 72 HIS ASP LYS VAL VAL VAL LEU GLU ALA LYS ASN GLY ASN
SEQRES 2 A 72 VAL THR PHE ASP HIS LYS LYS HIS ALA GLY VAL LYS GLY
SEQRES 3 A 72 GLU CYS LYS ALA CYS HIS GLU THR GLU ALA GLY GLY LYS
SEQRES 4 A 72 ILE ALA GLY MET GLY LYS ASP TRP ALA HIS LYS THR CYS
SEQRES 5 A 72 THR GLY CYS HIS LYS GLU MET GLY LYS GLY PRO THR LYS
SEQRES 6 A 72 CYS GLY GLU CYS HIS LYS LYS
SEQRES 1 B 72 HIS ASP LYS VAL VAL VAL LEU GLU ALA LYS ASN GLY ASN
SEQRES 2 B 72 VAL THR PHE ASP HIS LYS LYS HIS ALA GLY VAL LYS GLY
SEQRES 3 B 72 GLU CYS LYS ALA CYS HIS GLU THR GLU ALA GLY GLY LYS
SEQRES 4 B 72 ILE ALA GLY MET GLY LYS ASP TRP ALA HIS LYS THR CYS
SEQRES 5 B 72 THR GLY CYS HIS LYS GLU MET GLY LYS GLY PRO THR LYS
SEQRES 6 B 72 CYS GLY GLU CYS HIS LYS LYS
HET HEM A 72 43
HET HEM A 73 48
HET HEM A 74 46
HET HEM B 72 43
HET HEM B 73 43
HET HEM B 74 43
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN HEM HEME
FORMUL 3 HEM 6(C34 H32 FE N4 O4)
FORMUL 9 HOH *195(H2 O)
HELIX 1 1 ASP A 16 ALA A 21 5 6
HELIX 2 2 GLY A 25 CYS A 30 5 6
HELIX 3 3 GLY A 42 GLY A 59 1 17
HELIX 4 4 LYS A 64 HIS A 69 1 6
HELIX 5 5 HIS B 17 ALA B 21 5 5
HELIX 6 6 GLY B 25 CYS B 30 5 6
HELIX 7 7 GLY B 42 GLY B 59 1 17
HELIX 8 8 LYS B 64 HIS B 69 1 6
SHEET 1 A 2 VAL A 4 LEU A 6 0
SHEET 2 A 2 VAL A 13 PHE A 15 -1 O VAL A 13 N LEU A 6
SHEET 1 B 2 VAL B 4 LEU B 6 0
SHEET 2 B 2 VAL B 13 PHE B 15 -1 O VAL B 13 N LEU B 6
LINK NE2 HIS A 17 FE HEM A 72 1555 1555 2.06
LINK NE2 HIS A 20 FE HEM A 73 1555 1555 2.03
LINK NE2 HIS A 31 FE HEM A 72 1555 1555 2.05
LINK NE2 HIS A 47 FE HEM A 74 1555 1555 2.08
LINK NE2 HIS A 55 FE HEM A 73 1555 1555 2.02
LINK NE2 HIS A 69 FE HEM A 74 1555 1555 2.05
LINK NE2 HIS B 17 FE HEM B 72 1555 1555 2.03
LINK NE2 HIS B 20 FE HEM B 73 1555 1555 2.04
LINK NE2 HIS B 31 FE HEM B 72 1555 1555 2.01
LINK NE2 HIS B 47 FE HEM B 74 1555 1555 2.05
LINK NE2 HIS B 55 FE HEM B 73 1555 1555 2.07
LINK NE2 HIS B 69 FE HEM B 74 1555 1555 2.03
SITE 1 AC1 22 LYS A 9 PHE A 15 HIS A 17 HIS A 20
SITE 2 AC1 22 GLU A 26 CYS A 27 CYS A 30 HIS A 31
SITE 3 AC1 22 GLU A 33 ALA A 34 GLY A 35 GLY A 36
SITE 4 AC1 22 LYS A 37 ILE A 38 LYS A 43 HEM A 73
SITE 5 AC1 22 HEM A 74 HOH A 84 HOH A 109 HOH A 112
SITE 6 AC1 22 HOH A 133 HOH A 142
SITE 1 AC2 23 VAL A 13 THR A 14 ASP A 16 LYS A 19
SITE 2 AC2 23 HIS A 20 THR A 49A CYS A 51 CYS A 54
SITE 3 AC2 23 HIS A 55 MET A 58 PRO A 62 HEM A 72
SITE 4 AC2 23 HOH A 77 HOH A 78 HOH A 116 HOH A 127
SITE 5 AC2 23 HOH A 161 HOH A 172 GLY B 59 LYS B 60
SITE 6 AC2 23 GLY B 61 HOH B 100 HOH B 181
SITE 1 AC3 21 LEU A 6 GLU A 7 ALA A 8 LYS A 9
SITE 2 AC3 21 ASN A 10 LYS A 37 MET A 41 GLY A 42
SITE 3 AC3 21 LYS A 43 ALA A 46 HIS A 47 THR A 52
SITE 4 AC3 21 PRO A 62 THR A 63 LYS A 64 CYS A 65
SITE 5 AC3 21 CYS A 68 HIS A 69 HEM A 72 HOH A 87
SITE 6 AC3 21 HOH A 113
SITE 1 AC4 22 PHE B 15 HIS B 17 HIS B 20 VAL B 23
SITE 2 AC4 22 GLU B 26 CYS B 27 CYS B 30 HIS B 31
SITE 3 AC4 22 GLU B 33 GLY B 35 GLY B 36 LYS B 37
SITE 4 AC4 22 ILE B 38 MET B 41 LYS B 43 HEM B 73
SITE 5 AC4 22 HEM B 74 HOH B 80 HOH B 92 HOH B 107
SITE 6 AC4 22 HOH B 131 HOH B 168
SITE 1 AC5 18 GLU A 67 LYS A 70 THR B 14 PHE B 15
SITE 2 AC5 18 LYS B 19 HIS B 20 VAL B 23 THR B 49A
SITE 3 AC5 18 CYS B 51 CYS B 54 HIS B 55 LYS B 60
SITE 4 AC5 18 PRO B 62 HEM B 72 HOH B 109 HOH B 112
SITE 5 AC5 18 HOH B 126 HOH B 179
SITE 1 AC6 23 LYS A 24 LEU B 6 GLU B 7 ALA B 8
SITE 2 AC6 23 LYS B 9 ASN B 10 HIS B 17 GLY B 42
SITE 3 AC6 23 LYS B 43 ALA B 46 HIS B 47 THR B 52
SITE 4 AC6 23 PRO B 62 THR B 63 LYS B 64 CYS B 65
SITE 5 AC6 23 CYS B 68 HIS B 69 HEM B 72 HOH B 102
SITE 6 AC6 23 HOH B 138 HOH B 193 HOH B 197
CRYST1 27.400 55.900 94.800 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 0.036496 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017889 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010549 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
