HEADER ELECTRON TRANSPORT 10-JUL-08 3DR0
TITLE STRUCTURE OF REDUCED CYTOCHROME C6 FROM SYNECHOCOCCUS SP. PCC 7002
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C6;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: SOLUBLE CYTOCHROME F, CYTOCHROME C553, CYTOCHROME C-553;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SYNECHOCOCCUS SP. PCC 7002;
SOURCE 3 ORGANISM_COMMON: AGMENELLUM QUADRUPLICATUM;
SOURCE 4 ORGANISM_TAXID: 32049;
SOURCE 5 GENE: PETJ;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: DH5A;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PUC19
KEYWDS CYTOCHROME, PHOTOSYNTHESIS, CYANOBACTERIA, ELECTRON TRANSFER,
KEYWDS 2 ELECTRON TRANSPORT, HEME, IRON, METAL-BINDING, THYLAKOID, TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR W.BIALEK,S.KRZYWDA,M.JASKOLSKI,A.SZCZEPANIAK
REVDAT 4 01-NOV-23 3DR0 1 REMARK
REVDAT 3 25-APR-12 3DR0 1 JRNL VERSN
REVDAT 2 04-AUG-09 3DR0 1 JRNL
REVDAT 1 14-JUL-09 3DR0 0
JRNL AUTH W.BIALEK,S.KRZYWDA,M.JASKOLSKI,A.SZCZEPANIAK
JRNL TITL ATOMIC-RESOLUTION STRUCTURE OF REDUCED CYANOBACTERIAL
JRNL TITL 2 CYTOCHROME C6 WITH AN UNUSUAL SEQUENCE INSERTION
JRNL REF FEBS J. V. 276 4426 2009
JRNL REFN ISSN 1742-464X
JRNL PMID 19678839
JRNL DOI 10.1111/J.1742-4658.2009.07150.X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH W.BIALEK,M.NELSON,K.TAMIOLA,T.KALLAS,A.SZCZEPANIAK
REMARK 1 TITL DEEPLY BRANCHING C6-LIKE CYTOCHROMES OF CYANOBACTERIA
REMARK 1 REF BIOCHEMISTRY V. 47 5515 2008
REMARK 1 REFN ISSN 0006-2960
REMARK 1 PMID 18439023
REMARK 1 DOI 10.1021/BI701973G
REMARK 1 REFERENCE 2
REMARK 1 AUTH C.NOMURA,D.A.BRYANT
REMARK 1 TITL CYTOCHROME C6 FROM SYNECHOCOCCUS SP. PCC 7002
REMARK 1 REF THE PHOTOTROPHIC PROKARYOTES 269 1999
REMARK 1 REFN
REMARK 2
REMARK 2 RESOLUTION. 1.23 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0039
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) : 1.23
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.58
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 61634
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) : 0.108
REMARK 3 R VALUE (WORKING SET) : 0.107
REMARK 3 FREE R VALUE : 0.138
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1274
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) : 1.23
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3963
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.96
REMARK 3 BIN R VALUE (WORKING SET) : 0.2370
REMARK 3 BIN FREE R VALUE SET COUNT : 89
REMARK 3 BIN FREE R VALUE : 0.2430
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1986
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 139
REMARK 3 SOLVENT ATOMS : 523
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 7.47
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.19000
REMARK 3 B22 (A**2) : -0.19000
REMARK 3 B33 (A**2) : 0.29000
REMARK 3 B12 (A**2) : -0.10000
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): 0.036
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.036
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.026
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.302
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.988
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.984
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2289 ; 0.019 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1375 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3135 ; 1.687 ; 2.109
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3370 ; 1.633 ; 3.004
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 279 ; 6.331 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 96 ;40.289 ;26.562
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 319 ;11.107 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 3 ;19.982 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 311 ; 0.106 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2610 ; 0.011 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 402 ; 0.001 ; 0.020
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): 1402 ; 1.619 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 582 ; 0.578 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2186 ; 2.269 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 887 ; 3.315 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 949 ; 4.306 ; 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): 3664 ; 1.418 ; 1.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 523 ;12.667 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 3597 ; 4.407 ; 5.000
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 : 8
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 16
REMARK 3 ORIGIN FOR THE GROUP (A): 30.3078 -18.0786 -7.9964
REMARK 3 T TENSOR
REMARK 3 T11: 0.0791 T22: 0.0679
REMARK 3 T33: 0.0999 T12: 0.0122
REMARK 3 T13: -0.0164 T23: -0.0110
REMARK 3 L TENSOR
REMARK 3 L11: 2.9043 L22: 2.9646
REMARK 3 L33: 3.5448 L12: 0.4475
REMARK 3 L13: -0.0728 L23: 0.5572
REMARK 3 S TENSOR
REMARK 3 S11: -0.0397 S12: 0.0880 S13: 0.0822
REMARK 3 S21: -0.0978 S22: -0.0124 S23: -0.0695
REMARK 3 S31: -0.1801 S32: 0.0489 S33: 0.0522
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 : A 17 A 70
REMARK 3 ORIGIN FOR THE GROUP (A): 26.3122 -32.0445 -10.1208
REMARK 3 T TENSOR
REMARK 3 T11: 0.0643 T22: 0.0576
REMARK 3 T33: 0.0754 T12: -0.0080
REMARK 3 T13: 0.0068 T23: 0.0048
REMARK 3 L TENSOR
REMARK 3 L11: 1.2156 L22: 1.2653
REMARK 3 L33: 1.3290 L12: -0.2179
REMARK 3 L13: 0.0798 L23: 0.1018
REMARK 3 S TENSOR
REMARK 3 S11: -0.0174 S12: -0.0145 S13: -0.1193
REMARK 3 S21: 0.0239 S22: 0.0190 S23: 0.0237
REMARK 3 S31: 0.0827 S32: -0.0273 S33: -0.0016
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 71 A 93
REMARK 3 ORIGIN FOR THE GROUP (A): 30.4577 -22.5080 -12.5056
REMARK 3 T TENSOR
REMARK 3 T11: 0.0507 T22: 0.0224
REMARK 3 T33: 0.0292 T12: -0.0027
REMARK 3 T13: -0.0130 T23: 0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 4.8728 L22: 2.9524
REMARK 3 L33: 0.8024 L12: -2.6969
REMARK 3 L13: -0.6644 L23: 0.8287
REMARK 3 S TENSOR
REMARK 3 S11: -0.0777 S12: -0.0106 S13: 0.0801
REMARK 3 S21: -0.0044 S22: 0.0324 S23: -0.0360
REMARK 3 S31: -0.0512 S32: 0.0136 S33: 0.0453
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 16
REMARK 3 ORIGIN FOR THE GROUP (A): 10.4548 7.0679 -2.0158
REMARK 3 T TENSOR
REMARK 3 T11: 0.0662 T22: 0.0611
REMARK 3 T33: 0.0925 T12: -0.0062
REMARK 3 T13: -0.0019 T23: 0.0129
REMARK 3 L TENSOR
REMARK 3 L11: 2.7036 L22: 2.2036
REMARK 3 L33: 4.9799 L12: -0.7579
REMARK 3 L13: 0.5589 L23: -0.3811
REMARK 3 S TENSOR
REMARK 3 S11: -0.0754 S12: -0.0939 S13: 0.1152
REMARK 3 S21: 0.0598 S22: -0.0314 S23: 0.0004
REMARK 3 S31: -0.2278 S32: -0.0397 S33: 0.1067
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 17 B 93
REMARK 3 ORIGIN FOR THE GROUP (A): 14.1377 -3.4194 1.1614
REMARK 3 T TENSOR
REMARK 3 T11: 0.0551 T22: 0.0692
REMARK 3 T33: 0.0519 T12: 0.0084
REMARK 3 T13: 0.0014 T23: 0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 0.9815 L22: 1.3109
REMARK 3 L33: 1.0202 L12: 0.0291
REMARK 3 L13: 0.0600 L23: -0.1027
REMARK 3 S TENSOR
REMARK 3 S11: -0.0008 S12: 0.0074 S13: 0.0128
REMARK 3 S21: 0.0008 S22: -0.0156 S23: -0.0826
REMARK 3 S31: -0.0118 S32: 0.0854 S33: 0.0164
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 1 C 40
REMARK 3 ORIGIN FOR THE GROUP (A): 30.6261 21.4571 -14.0271
REMARK 3 T TENSOR
REMARK 3 T11: 0.0595 T22: 0.0688
REMARK 3 T33: 0.0703 T12: -0.0029
REMARK 3 T13: 0.0020 T23: 0.0102
REMARK 3 L TENSOR
REMARK 3 L11: 1.5831 L22: 2.0052
REMARK 3 L33: 0.6002 L12: -0.8684
REMARK 3 L13: -0.6106 L23: 0.7647
REMARK 3 S TENSOR
REMARK 3 S11: 0.0585 S12: 0.0697 S13: 0.0757
REMARK 3 S21: -0.0958 S22: -0.0535 S23: -0.0302
REMARK 3 S31: -0.0406 S32: -0.0401 S33: -0.0049
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 41 C 72
REMARK 3 ORIGIN FOR THE GROUP (A): 22.4197 16.3696 -9.1192
REMARK 3 T TENSOR
REMARK 3 T11: 0.0393 T22: 0.0511
REMARK 3 T33: 0.0569 T12: -0.0071
REMARK 3 T13: -0.0051 T23: 0.0070
REMARK 3 L TENSOR
REMARK 3 L11: 1.6036 L22: 2.2777
REMARK 3 L33: 2.5005 L12: 0.0933
REMARK 3 L13: -0.0015 L23: 0.9943
REMARK 3 S TENSOR
REMARK 3 S11: 0.0014 S12: 0.0336 S13: -0.0097
REMARK 3 S21: 0.0043 S22: -0.0433 S23: 0.1267
REMARK 3 S31: 0.0288 S32: -0.1554 S33: 0.0419
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 73 C 93
REMARK 3 ORIGIN FOR THE GROUP (A): 34.2732 17.2052 -7.7044
REMARK 3 T TENSOR
REMARK 3 T11: 0.0473 T22: 0.0540
REMARK 3 T33: 0.0545 T12: 0.0105
REMARK 3 T13: 0.0088 T23: 0.0025
REMARK 3 L TENSOR
REMARK 3 L11: 2.0323 L22: 6.6957
REMARK 3 L33: 0.6696 L12: 2.0866
REMARK 3 L13: 0.0541 L23: 0.6187
REMARK 3 S TENSOR
REMARK 3 S11: -0.0445 S12: -0.0300 S13: -0.0122
REMARK 3 S21: 0.0220 S22: 0.0329 S23: -0.1093
REMARK 3 S31: 0.0209 S32: 0.0272 S33: 0.0115
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 3DR0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-JUL-08.
REMARK 100 THE DEPOSITION ID IS D_1000048380.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-DEC-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8170
REMARK 200 MONOCHROMATOR : SI [111], HORIZONTALLY FOCUSSING
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 62908
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.220
REMARK 200 RESOLUTION RANGE LOW (A) : 71.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.07500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.22
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.26
REMARK 200 COMPLETENESS FOR SHELL (%) : 73.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.37300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
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 ID 1CTJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10MM HEPES, 2.2M AMMONIUM SULFATE, PH
REMARK 280 6.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 18.85133
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 9.42567
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 A 14 CAB HEM A 94 1.80
REMARK 500 SG CYS C 14 CAB HEM C 94 1.82
REMARK 500 SG CYS B 14 CAB HEM B 94 1.84
REMARK 500 SG CYS A 17 CAC HEM A 94 1.85
REMARK 500 SG CYS C 17 CAC HEM C 94 1.87
REMARK 500 SG CYS B 17 CAC HEM B 94 1.87
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 GLN B 62 100.66 -161.84
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 94 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 18 NE2
REMARK 620 2 HEM A 94 NA 92.3
REMARK 620 3 HEM A 94 NB 90.3 90.5
REMARK 620 4 HEM A 94 NC 87.9 179.4 90.0
REMARK 620 5 HEM A 94 ND 89.5 89.8 179.6 89.7
REMARK 620 6 MET A 65 SD 170.1 96.5 85.0 83.4 95.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 94 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 18 NE2
REMARK 620 2 HEM B 94 NA 91.6
REMARK 620 3 HEM B 94 NB 89.3 91.1
REMARK 620 4 HEM B 94 NC 87.8 178.9 89.8
REMARK 620 5 HEM B 94 ND 90.2 87.8 178.8 91.2
REMARK 620 6 MET B 65 SD 170.4 97.2 86.9 83.4 93.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM C 94 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 18 NE2
REMARK 620 2 HEM C 94 NA 92.8
REMARK 620 3 HEM C 94 NB 88.3 88.4
REMARK 620 4 HEM C 94 NC 89.3 177.6 90.5
REMARK 620 5 HEM C 94 ND 90.1 89.8 177.6 91.3
REMARK 620 6 MET C 65 SD 171.3 94.9 87.8 82.9 94.0
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 B 96
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 95
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 94
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 94
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 94
DBREF 3DR0 A 1 93 UNP O30881 CYC6_SYNP2 25 117
DBREF 3DR0 B 1 93 UNP O30881 CYC6_SYNP2 25 117
DBREF 3DR0 C 1 93 UNP O30881 CYC6_SYNP2 25 117
SEQRES 1 A 93 ALA ASP ALA ALA ALA GLY ALA GLN VAL PHE ALA ALA ASN
SEQRES 2 A 93 CYS ALA ALA CYS HIS ALA GLY GLY ASN ASN ALA VAL MET
SEQRES 3 A 93 PRO THR LYS THR LEU LYS ALA ASP ALA LEU LYS THR TYR
SEQRES 4 A 93 LEU ALA GLY TYR LYS ASP GLY SER LYS SER LEU GLU GLU
SEQRES 5 A 93 ALA VAL ALA TYR GLN VAL THR ASN GLY GLN GLY ALA MET
SEQRES 6 A 93 PRO ALA PHE GLY GLY ARG LEU SER ASP ALA ASP ILE ALA
SEQRES 7 A 93 ASN VAL ALA ALA TYR ILE ALA ASP GLN ALA GLU ASN ASN
SEQRES 8 A 93 LYS TRP
SEQRES 1 B 93 ALA ASP ALA ALA ALA GLY ALA GLN VAL PHE ALA ALA ASN
SEQRES 2 B 93 CYS ALA ALA CYS HIS ALA GLY GLY ASN ASN ALA VAL MET
SEQRES 3 B 93 PRO THR LYS THR LEU LYS ALA ASP ALA LEU LYS THR TYR
SEQRES 4 B 93 LEU ALA GLY TYR LYS ASP GLY SER LYS SER LEU GLU GLU
SEQRES 5 B 93 ALA VAL ALA TYR GLN VAL THR ASN GLY GLN GLY ALA MET
SEQRES 6 B 93 PRO ALA PHE GLY GLY ARG LEU SER ASP ALA ASP ILE ALA
SEQRES 7 B 93 ASN VAL ALA ALA TYR ILE ALA ASP GLN ALA GLU ASN ASN
SEQRES 8 B 93 LYS TRP
SEQRES 1 C 93 ALA ASP ALA ALA ALA GLY ALA GLN VAL PHE ALA ALA ASN
SEQRES 2 C 93 CYS ALA ALA CYS HIS ALA GLY GLY ASN ASN ALA VAL MET
SEQRES 3 C 93 PRO THR LYS THR LEU LYS ALA ASP ALA LEU LYS THR TYR
SEQRES 4 C 93 LEU ALA GLY TYR LYS ASP GLY SER LYS SER LEU GLU GLU
SEQRES 5 C 93 ALA VAL ALA TYR GLN VAL THR ASN GLY GLN GLY ALA MET
SEQRES 6 C 93 PRO ALA PHE GLY GLY ARG LEU SER ASP ALA ASP ILE ALA
SEQRES 7 C 93 ASN VAL ALA ALA TYR ILE ALA ASP GLN ALA GLU ASN ASN
SEQRES 8 C 93 LYS TRP
HET HEM A 94 43
HET SO4 B 96 5
HET SO4 B 95 5
HET HEM B 94 43
HET HEM C 94 43
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM SO4 SULFATE ION
HETSYN HEM HEME
FORMUL 4 HEM 3(C34 H32 FE N4 O4)
FORMUL 5 SO4 2(O4 S 2-)
FORMUL 9 HOH *523(H2 O)
HELIX 1 1 ASP A 2 CYS A 14 1 13
HELIX 2 2 CYS A 14 ALA A 19 1 6
HELIX 3 3 GLY A 20 ASN A 22 5 3
HELIX 4 4 LYS A 32 LEU A 40 1 9
HELIX 5 5 SER A 49 GLY A 61 1 13
HELIX 6 6 SER A 73 ASN A 90 1 18
HELIX 7 7 ASP B 2 CYS B 14 1 13
HELIX 8 8 CYS B 14 ALA B 19 1 6
HELIX 9 9 GLY B 20 ASN B 22 5 3
HELIX 10 10 LYS B 32 LEU B 40 1 9
HELIX 11 11 SER B 49 GLY B 61 1 13
HELIX 12 12 SER B 73 ASN B 90 1 18
HELIX 13 13 ASP C 2 CYS C 14 1 13
HELIX 14 14 CYS C 14 ALA C 19 1 6
HELIX 15 15 GLY C 20 ASN C 22 5 3
HELIX 16 16 LYS C 32 LEU C 40 1 9
HELIX 17 17 SER C 49 GLY C 61 1 13
HELIX 18 18 SER C 73 ASN C 90 1 18
LINK NE2 HIS A 18 FE HEM A 94 1555 1555 2.05
LINK SD MET A 65 FE HEM A 94 1555 1555 2.33
LINK NE2 HIS B 18 FE HEM B 94 1555 1555 2.07
LINK SD MET B 65 FE HEM B 94 1555 1555 2.33
LINK NE2 HIS C 18 FE HEM C 94 1555 1555 2.05
LINK SD MET C 65 FE HEM C 94 1555 1555 2.31
SITE 1 AC1 4 HOH B 198 HOH B 232 HOH B 233 ARG C 71
SITE 1 AC2 6 PRO B 66 ALA B 67 HOH B 117 HOH B 262
SITE 2 AC2 6 SER C 73 ASP C 74
SITE 1 AC3 20 ASN A 13 CYS A 14 CYS A 17 HIS A 18
SITE 2 AC3 20 ASN A 23 MET A 26 LYS A 29 THR A 30
SITE 3 AC3 20 LEU A 31 TYR A 39 GLN A 57 VAL A 58
SITE 4 AC3 20 GLN A 62 MET A 65 PRO A 66 PHE A 68
SITE 5 AC3 20 ILE A 84 HOH A 103 HOH A 105 HOH A 106
SITE 1 AC4 23 ASN B 13 CYS B 14 CYS B 17 HIS B 18
SITE 2 AC4 23 ASN B 23 VAL B 25 MET B 26 LYS B 29
SITE 3 AC4 23 THR B 30 LEU B 31 LEU B 36 TYR B 39
SITE 4 AC4 23 GLN B 57 VAL B 58 GLN B 62 MET B 65
SITE 5 AC4 23 PHE B 68 ILE B 84 HOH B 104 HOH B 116
SITE 6 AC4 23 HOH B 224 HOH B 279 HOH B 283
SITE 1 AC5 22 ASN C 13 CYS C 14 CYS C 17 HIS C 18
SITE 2 AC5 22 ASN C 23 MET C 26 LYS C 29 THR C 30
SITE 3 AC5 22 LEU C 31 ALA C 35 TYR C 39 GLN C 57
SITE 4 AC5 22 VAL C 58 GLN C 62 MET C 65 PRO C 66
SITE 5 AC5 22 PHE C 68 ILE C 84 HOH C 99 HOH C 102
SITE 6 AC5 22 HOH C 112 HOH C 129
CRYST1 82.879 82.879 28.277 90.00 90.00 120.00 P 32 9
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 0.012066 0.006966 0.000000 0.00000
SCALE2 0.000000 0.013932 0.000000 0.00000
SCALE3 0.000000 0.000000 0.035364 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
