HEADER ELECTRON TRANSPORT 22-JUL-10 3O20
TITLE ELECTRON TRANSFER COMPLEXES:EXPERIMENTAL MAPPING OF THE REDOX-
TITLE 2 DEPENDENT CYTOCHROME C ELECTROSTATIC SURFACE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C;
COMPND 3 CHAIN: A, B, C
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: EQUUS CABALLUS;
SOURCE 3 ORGANISM_COMMON: DOMESTIC HORSE,EQUINE;
SOURCE 4 ORGANISM_TAXID: 9796
KEYWDS GLOBULAR PROTEIN, ELECTRON CARRIER, MITOCHONDRIAL RESPIRATION,
KEYWDS 2 ELECTRON TRASPORT CHAIN, ELECTRON TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR M.DE MARCH,R.DE ZORZI,A.CASINI,L.MESSORI,S.GEREMIA,N.DEMITRI,
AUTHOR 2 C.GABBIANI,A.GUERRI
REVDAT 3 20-MAR-19 3O20 1 JRNL LINK
REVDAT 2 07-MAR-18 3O20 1 REMARK
REVDAT 1 25-JAN-12 3O20 0
JRNL AUTH M.DE MARCH,N.DEMITRI,R.DE ZORZI,A.CASINI,C.GABBIANI,
JRNL AUTH 2 A.GUERRI,L.MESSORI,S.GEREMIA
JRNL TITL NITRATE AS A PROBE OF CYTOCHROME C SURFACE: CRYSTALLOGRAPHIC
JRNL TITL 2 IDENTIFICATION OF CRUCIAL "HOT SPOTS" FOR PROTEIN-PROTEIN
JRNL TITL 3 RECOGNITION.
JRNL REF J. INORG. BIOCHEM. V. 135 58 2014
JRNL REFN ISSN 1873-3344
JRNL PMID 24662464
JRNL DOI 10.1016/J.JINORGBIO.2014.02.015
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH E.SCHAFER,N.A.DENCHER,J.VONCK,D.N.PARCEJ
REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF THE RESPIRATORY CHAIN
REMARK 1 TITL 2 SUPERCOMPLEX I1III2IV1 FROM BOVINE HEART MITOCHONDRIA.
REMARK 1 REF BIOCHEMISTRY V. 46 12579 2007
REMARK 1 REFN ISSN 0006-2960
REMARK 1 PMID 17927210
REMARK 1 DOI 10.1021/BI700983H
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.HEINEMEYER,H.P.BRAUN,E.J.BOEKEMA,R.KOURIL
REMARK 1 TITL A STRUCTURAL MODEL OF THE CYTOCHROME C REDUCTASE/OXIDASE
REMARK 1 TITL 2 SUPERCOMPLEX FROM YEAST MITOCHONDRIA.
REMARK 1 REF J. BIOL. CHEM. V. 282 12240 2007
REMARK 1 REFN ISSN 0021-9258
REMARK 1 PMID 17322303
REMARK 1 DOI 10.1074/JBC.M610545200
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 65.09
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.3
REMARK 3 NUMBER OF REFLECTIONS : 21667
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) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.276
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1166
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1311
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 77.93
REMARK 3 BIN R VALUE (WORKING SET) : 0.2280
REMARK 3 BIN FREE R VALUE SET COUNT : 73
REMARK 3 BIN FREE R VALUE : 0.3030
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2478
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 201
REMARK 3 SOLVENT ATOMS : 365
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.27
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.26000
REMARK 3 B22 (A**2) : -1.31000
REMARK 3 B33 (A**2) : 2.53000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.36000
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): 0.204
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.146
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.879
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.931
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.863
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2748 ; 0.020 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3682 ; 1.794 ; 2.140
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 311 ; 6.279 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 102 ;34.061 ;25.294
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 517 ;16.915 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 6 ;26.403 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 352 ; 0.099 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2038 ; 0.011 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1503 ; 0.207 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1763 ; 0.305 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 292 ; 0.215 ; 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): 101 ; 0.247 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 59 ; 0.268 ; 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): 1665 ; 1.085 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2478 ; 1.471 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1296 ; 2.379 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1197 ; 3.302 ; 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 : 16
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 7 1
REMARK 3 1 B 1 B 7 1
REMARK 3 1 C 1 C 7 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 50 ; 0.08 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 B (A): 50 ; 0.06 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 C (A): 50 ; 0.08 ; 0.05
REMARK 3 TIGHT THERMAL 1 A (A**2): 50 ; 0.19 ; 0.50
REMARK 3 TIGHT THERMAL 1 B (A**2): 50 ; 0.21 ; 0.50
REMARK 3 TIGHT THERMAL 1 C (A**2): 50 ; 0.25 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 8 A 8 3
REMARK 3 1 B 8 B 8 3
REMARK 3 1 C 8 C 8 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 A (A): 3 ; 0.01 ; 0.05
REMARK 3 TIGHT POSITIONAL 2 B (A): 3 ; 0.01 ; 0.05
REMARK 3 TIGHT POSITIONAL 2 C (A): 3 ; 0.01 ; 0.05
REMARK 3 TIGHT THERMAL 2 A (A**2): 3 ; 0.13 ; 0.50
REMARK 3 TIGHT THERMAL 2 B (A**2): 3 ; 0.45 ; 0.50
REMARK 3 TIGHT THERMAL 2 C (A**2): 3 ; 0.39 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : A B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 9 A 11 1
REMARK 3 1 B 9 B 11 1
REMARK 3 1 C 9 C 11 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 3 A (A): 26 ; 0.05 ; 0.05
REMARK 3 TIGHT POSITIONAL 3 B (A): 26 ; 0.05 ; 0.05
REMARK 3 TIGHT POSITIONAL 3 C (A): 26 ; 0.05 ; 0.05
REMARK 3 TIGHT THERMAL 3 A (A**2): 26 ; 0.39 ; 0.50
REMARK 3 TIGHT THERMAL 3 B (A**2): 26 ; 0.31 ; 0.50
REMARK 3 TIGHT THERMAL 3 C (A**2): 26 ; 0.43 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 4
REMARK 3 CHAIN NAMES : A B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 12 A 12 3
REMARK 3 1 B 12 B 12 3
REMARK 3 1 C 12 C 12 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 4 A (A): 4 ; 0.02 ; 0.05
REMARK 3 TIGHT POSITIONAL 4 B (A): 4 ; 0.02 ; 0.05
REMARK 3 TIGHT POSITIONAL 4 C (A): 4 ; 0.02 ; 0.05
REMARK 3 LOOSE POSITIONAL 4 A (A): 5 ; 1.61 ; 5.00
REMARK 3 LOOSE POSITIONAL 4 B (A): 5 ; 2.52 ; 5.00
REMARK 3 LOOSE POSITIONAL 4 C (A): 5 ; 1.70 ; 5.00
REMARK 3 TIGHT THERMAL 4 A (A**2): 4 ; 0.16 ; 0.50
REMARK 3 TIGHT THERMAL 4 B (A**2): 4 ; 0.22 ; 0.50
REMARK 3 TIGHT THERMAL 4 C (A**2): 4 ; 0.11 ; 0.50
REMARK 3 LOOSE THERMAL 4 A (A**2): 5 ; 2.76 ; 10.00
REMARK 3 LOOSE THERMAL 4 B (A**2): 5 ; 4.21 ; 10.00
REMARK 3 LOOSE THERMAL 4 C (A**2): 5 ; 2.13 ; 10.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 5
REMARK 3 CHAIN NAMES : A B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 13 A 15 1
REMARK 3 1 B 13 B 15 1
REMARK 3 1 C 13 C 15 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 5 A (A): 20 ; 0.07 ; 0.05
REMARK 3 TIGHT POSITIONAL 5 B (A): 20 ; 0.07 ; 0.05
REMARK 3 TIGHT POSITIONAL 5 C (A): 20 ; 0.07 ; 0.05
REMARK 3 TIGHT THERMAL 5 A (A**2): 20 ; 0.35 ; 0.50
REMARK 3 TIGHT THERMAL 5 B (A**2): 20 ; 0.21 ; 0.50
REMARK 3 TIGHT THERMAL 5 C (A**2): 20 ; 0.46 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 6
REMARK 3 CHAIN NAMES : A B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 16 A 16 3
REMARK 3 1 B 16 B 16 3
REMARK 3 1 C 16 C 16 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 6 A (A): 4 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 6 B (A): 4 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 6 C (A): 4 ; 0.02 ; 0.05
REMARK 3 LOOSE POSITIONAL 6 A (A): 5 ; 0.64 ; 5.00
REMARK 3 LOOSE POSITIONAL 6 B (A): 5 ; 1.36 ; 5.00
REMARK 3 LOOSE POSITIONAL 6 C (A): 5 ; 0.74 ; 5.00
REMARK 3 TIGHT THERMAL 6 A (A**2): 4 ; 0.35 ; 0.50
REMARK 3 TIGHT THERMAL 6 B (A**2): 4 ; 0.40 ; 0.50
REMARK 3 TIGHT THERMAL 6 C (A**2): 4 ; 0.13 ; 0.50
REMARK 3 LOOSE THERMAL 6 A (A**2): 5 ; 1.46 ; 10.00
REMARK 3 LOOSE THERMAL 6 B (A**2): 5 ; 1.20 ; 10.00
REMARK 3 LOOSE THERMAL 6 C (A**2): 5 ; 2.27 ; 10.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 7
REMARK 3 CHAIN NAMES : A B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 17 A 24 1
REMARK 3 1 B 17 B 24 1
REMARK 3 1 C 17 C 24 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 7 A (A): 56 ; 0.06 ; 0.05
REMARK 3 TIGHT POSITIONAL 7 B (A): 56 ; 0.05 ; 0.05
REMARK 3 TIGHT POSITIONAL 7 C (A): 56 ; 0.05 ; 0.05
REMARK 3 TIGHT THERMAL 7 A (A**2): 56 ; 0.22 ; 0.50
REMARK 3 TIGHT THERMAL 7 B (A**2): 56 ; 0.25 ; 0.50
REMARK 3 TIGHT THERMAL 7 C (A**2): 56 ; 0.24 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 8
REMARK 3 CHAIN NAMES : A B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 25 A 25 3
REMARK 3 1 B 25 B 25 3
REMARK 3 1 C 25 C 25 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 8 A (A): 4 ; 0.02 ; 0.05
REMARK 3 TIGHT POSITIONAL 8 B (A): 4 ; 0.02 ; 0.05
REMARK 3 TIGHT POSITIONAL 8 C (A): 4 ; 0.02 ; 0.05
REMARK 3 LOOSE POSITIONAL 8 A (A): 5 ; 1.15 ; 5.00
REMARK 3 LOOSE POSITIONAL 8 B (A): 5 ; 1.21 ; 5.00
REMARK 3 LOOSE POSITIONAL 8 C (A): 5 ; 1.92 ; 5.00
REMARK 3 TIGHT THERMAL 8 A (A**2): 4 ; 0.19 ; 0.50
REMARK 3 TIGHT THERMAL 8 B (A**2): 4 ; 0.17 ; 0.50
REMARK 3 TIGHT THERMAL 8 C (A**2): 4 ; 0.23 ; 0.50
REMARK 3 LOOSE THERMAL 8 A (A**2): 5 ; 2.31 ; 10.00
REMARK 3 LOOSE THERMAL 8 B (A**2): 5 ; 2.93 ; 10.00
REMARK 3 LOOSE THERMAL 8 C (A**2): 5 ; 1.70 ; 10.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 9
REMARK 3 CHAIN NAMES : A B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 26 A 68 1
REMARK 3 1 B 26 B 68 1
REMARK 3 1 C 26 C 68 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 9 A (A): 342 ; 0.06 ; 0.05
REMARK 3 TIGHT POSITIONAL 9 B (A): 342 ; 0.06 ; 0.05
REMARK 3 TIGHT POSITIONAL 9 C (A): 342 ; 0.06 ; 0.05
REMARK 3 TIGHT THERMAL 9 A (A**2): 342 ; 0.25 ; 0.50
REMARK 3 TIGHT THERMAL 9 B (A**2): 342 ; 0.26 ; 0.50
REMARK 3 TIGHT THERMAL 9 C (A**2): 342 ; 0.31 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 10
REMARK 3 CHAIN NAMES : A B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 69 A 69 3
REMARK 3 1 B 69 B 69 3
REMARK 3 1 C 69 C 69 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 10 A (A): 4 ; 0.01 ; 0.05
REMARK 3 TIGHT POSITIONAL 10 B (A): 4 ; 0.03 ; 0.05
REMARK 3 TIGHT POSITIONAL 10 C (A): 4 ; 0.02 ; 0.05
REMARK 3 LOOSE POSITIONAL 10 A (A): 5 ; 0.99 ; 5.00
REMARK 3 LOOSE POSITIONAL 10 B (A): 5 ; 0.48 ; 5.00
REMARK 3 LOOSE POSITIONAL 10 C (A): 5 ; 0.53 ; 5.00
REMARK 3 TIGHT THERMAL 10 A (A**2): 4 ; 0.19 ; 0.50
REMARK 3 TIGHT THERMAL 10 B (A**2): 4 ; 0.21 ; 0.50
REMARK 3 TIGHT THERMAL 10 C (A**2): 4 ; 0.11 ; 0.50
REMARK 3 LOOSE THERMAL 10 A (A**2): 5 ; 3.94 ; 10.00
REMARK 3 LOOSE THERMAL 10 B (A**2): 5 ; 5.78 ; 10.00
REMARK 3 LOOSE THERMAL 10 C (A**2): 5 ; 1.90 ; 10.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 11
REMARK 3 CHAIN NAMES : A B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 70 A 85 1
REMARK 3 1 B 70 B 85 1
REMARK 3 1 C 70 C 85 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 11 A (A): 124 ; 0.06 ; 0.05
REMARK 3 TIGHT POSITIONAL 11 B (A): 124 ; 0.06 ; 0.05
REMARK 3 TIGHT POSITIONAL 11 C (A): 124 ; 0.06 ; 0.05
REMARK 3 TIGHT THERMAL 11 A (A**2): 124 ; 0.28 ; 0.50
REMARK 3 TIGHT THERMAL 11 B (A**2): 124 ; 0.28 ; 0.50
REMARK 3 TIGHT THERMAL 11 C (A**2): 124 ; 0.36 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 12
REMARK 3 CHAIN NAMES : A B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 86 A 88 3
REMARK 3 1 B 86 B 88 3
REMARK 3 1 C 86 C 88 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 12 A (A): 12 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 12 B (A): 12 ; 0.06 ; 0.05
REMARK 3 TIGHT POSITIONAL 12 C (A): 12 ; 0.05 ; 0.05
REMARK 3 LOOSE POSITIONAL 12 A (A): 15 ; 0.42 ; 5.00
REMARK 3 LOOSE POSITIONAL 12 B (A): 15 ; 0.54 ; 5.00
REMARK 3 LOOSE POSITIONAL 12 C (A): 15 ; 0.43 ; 5.00
REMARK 3 TIGHT THERMAL 12 A (A**2): 12 ; 0.21 ; 0.50
REMARK 3 TIGHT THERMAL 12 B (A**2): 12 ; 0.26 ; 0.50
REMARK 3 TIGHT THERMAL 12 C (A**2): 12 ; 0.25 ; 0.50
REMARK 3 LOOSE THERMAL 12 A (A**2): 15 ; 2.41 ; 10.00
REMARK 3 LOOSE THERMAL 12 B (A**2): 15 ; 3.66 ; 10.00
REMARK 3 LOOSE THERMAL 12 C (A**2): 15 ; 2.75 ; 10.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 13
REMARK 3 CHAIN NAMES : A B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 89 A 99 1
REMARK 3 1 B 89 B 99 1
REMARK 3 1 C 89 C 99 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 13 A (A): 94 ; 0.07 ; 0.05
REMARK 3 TIGHT POSITIONAL 13 B (A): 94 ; 0.07 ; 0.05
REMARK 3 TIGHT POSITIONAL 13 C (A): 94 ; 0.07 ; 0.05
REMARK 3 TIGHT THERMAL 13 A (A**2): 94 ; 0.27 ; 0.50
REMARK 3 TIGHT THERMAL 13 B (A**2): 94 ; 0.26 ; 0.50
REMARK 3 TIGHT THERMAL 13 C (A**2): 94 ; 0.28 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 14
REMARK 3 CHAIN NAMES : A B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 100 A 100 3
REMARK 3 1 B 100 B 100 3
REMARK 3 1 C 100 C 100 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 14 A (A): 4 ; 0.03 ; 0.05
REMARK 3 TIGHT POSITIONAL 14 B (A): 4 ; 0.03 ; 0.05
REMARK 3 TIGHT POSITIONAL 14 C (A): 4 ; 0.01 ; 0.05
REMARK 3 LOOSE POSITIONAL 14 A (A): 5 ; 1.24 ; 5.00
REMARK 3 LOOSE POSITIONAL 14 B (A): 5 ; 0.65 ; 5.00
REMARK 3 LOOSE POSITIONAL 14 C (A): 5 ; 0.84 ; 5.00
REMARK 3 TIGHT THERMAL 14 A (A**2): 4 ; 0.35 ; 0.50
REMARK 3 TIGHT THERMAL 14 B (A**2): 4 ; 0.21 ; 0.50
REMARK 3 TIGHT THERMAL 14 C (A**2): 4 ; 0.47 ; 0.50
REMARK 3 LOOSE THERMAL 14 A (A**2): 5 ; 1.49 ; 10.00
REMARK 3 LOOSE THERMAL 14 B (A**2): 5 ; 0.50 ; 10.00
REMARK 3 LOOSE THERMAL 14 C (A**2): 5 ; 1.84 ; 10.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 15
REMARK 3 CHAIN NAMES : A B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 101 A 102 1
REMARK 3 1 B 101 B 102 1
REMARK 3 1 C 101 C 102 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 15 A (A): 12 ; 0.05 ; 0.05
REMARK 3 TIGHT POSITIONAL 15 B (A): 12 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 15 C (A): 12 ; 0.04 ; 0.05
REMARK 3 TIGHT THERMAL 15 A (A**2): 12 ; 0.19 ; 0.50
REMARK 3 TIGHT THERMAL 15 B (A**2): 12 ; 0.30 ; 0.50
REMARK 3 TIGHT THERMAL 15 C (A**2): 12 ; 0.23 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 16
REMARK 3 CHAIN NAMES : A B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 103 A 104 3
REMARK 3 1 B 103 B 104 3
REMARK 3 1 C 103 C 104 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 16 A (A): 8 ; 0.08 ; 0.05
REMARK 3 TIGHT POSITIONAL 16 B (A): 8 ; 0.07 ; 0.05
REMARK 3 TIGHT POSITIONAL 16 C (A): 8 ; 0.04 ; 0.05
REMARK 3 LOOSE POSITIONAL 16 A (A): 10 ; 0.61 ; 5.00
REMARK 3 LOOSE POSITIONAL 16 B (A): 10 ; 0.42 ; 5.00
REMARK 3 LOOSE POSITIONAL 16 C (A): 10 ; 0.42 ; 5.00
REMARK 3 TIGHT THERMAL 16 A (A**2): 8 ; 0.12 ; 0.50
REMARK 3 TIGHT THERMAL 16 B (A**2): 8 ; 0.14 ; 0.50
REMARK 3 TIGHT THERMAL 16 C (A**2): 8 ; 0.10 ; 0.50
REMARK 3 LOOSE THERMAL 16 A (A**2): 10 ; 2.40 ; 10.00
REMARK 3 LOOSE THERMAL 16 B (A**2): 10 ; 0.86 ; 10.00
REMARK 3 LOOSE THERMAL 16 C (A**2): 10 ; 2.72 ; 10.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3O20 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUL-10.
REMARK 100 THE DEPOSITION ID IS D_1000060564.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : SEALED TUBE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : OXFORD DIFFRACTION ENHANCE ULTRA
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21667
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 65.090
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1HRC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: EXCESS OF NANO3 AND 10% OF DITIONITE,
REMARK 280 PH 7.4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 300K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 45.04600
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 26.01450
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 45.04600
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 26.01450
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, 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 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 350
REMARK 350 BIOMOLECULE: 3
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: 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 OE2 GLU A 69 O HOH A 185 2.07
REMARK 500 O HOH B 359 O HOH C 123 2.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 135 O HOH B 355 2555 2.08
REMARK 500 O HOH A 121 O HOH C 325 2655 2.13
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 LYS A 27 -125.02 -112.65
REMARK 500 ASN A 70 77.80 -170.66
REMARK 500 PHE A 82 118.03 -171.90
REMARK 500 LYS B 27 -120.49 -112.34
REMARK 500 ASN B 70 79.56 -169.58
REMARK 500 LYS C 27 -121.90 -99.49
REMARK 500 ASN C 70 80.76 -173.71
REMARK 500 PHE C 82 121.25 -173.83
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 HEC B 105 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 18 NE2
REMARK 620 2 HEC B 105 NA 90.7
REMARK 620 3 HEC B 105 NB 93.8 89.9
REMARK 620 4 HEC B 105 NC 90.1 179.1 89.7
REMARK 620 5 HEC B 105 ND 89.3 89.3 176.8 91.1
REMARK 620 6 MET B 80 SD 172.4 84.8 92.3 94.5 84.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC C 105 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 18 NE2
REMARK 620 2 HEC C 105 NA 83.3
REMARK 620 3 HEC C 105 NB 88.3 88.4
REMARK 620 4 HEC C 105 NC 90.8 174.1 91.0
REMARK 620 5 HEC C 105 ND 84.6 87.1 172.0 92.7
REMARK 620 6 MET C 80 SD 170.2 87.4 94.7 98.5 91.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC A 105 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 18 NE2
REMARK 620 2 HEC A 105 NA 86.6
REMARK 620 3 HEC A 105 NB 91.5 90.8
REMARK 620 4 HEC A 105 NC 86.2 172.2 86.3
REMARK 620 5 HEC A 105 ND 83.0 85.8 173.7 96.3
REMARK 620 6 MET A 80 SD 173.4 87.3 91.1 100.0 94.1
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 HEC A 105
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 106
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 107
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 108
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 109
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 110
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 111
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 112
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC B 105
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 B 106
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 B 107
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 B 108
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 B 109
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 B 110
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 B 111
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 B 112
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 B 113
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC C 105
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 C 106
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 C 107
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 C 108
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KYO RELATED DB: PDB
REMARK 900 YEAST CYTOCHROME BC1 COMPLEX WITH BOUND SUBSTRATE CYTOCHROME C
REMARK 900 RELATED ID: 2PCC RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A COMPLEX BETWEEN ELECTRON TRANSFER PARTNERS,
REMARK 900 CYTOCHROME C PEROXIDASE AND CYTOCHROME C.
REMARK 900 RELATED ID: 2PCB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A COMPLEX BETWEEN ELECTRON TRANSFER PARTNERS,
REMARK 900 CYTOCHROME C PEROXIDASE AND CYTOCHROME C.
REMARK 900 RELATED ID: 1L9J RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF THE CYTOCHROME-C(2)-PHOTOSYNTHETIC REACTION
REMARK 900 CENTER ELECTRON TRANSFER COMPLEX FROM RHODOBACTER SPHAEROIDES IN
REMARK 900 TYPE I CO-CRYSTALS
DBREF 3O20 A 1 104 UNP P00004 CYC_HORSE 2 105
DBREF 3O20 B 1 104 UNP P00004 CYC_HORSE 2 105
DBREF 3O20 C 1 104 UNP P00004 CYC_HORSE 2 105
SEQADV 3O20 ACE A 0 UNP P00004 ACETYLATION
SEQADV 3O20 ACE B 0 UNP P00004 ACETYLATION
SEQADV 3O20 ACE C 0 UNP P00004 ACETYLATION
SEQRES 1 A 105 ACE GLY ASP VAL GLU LYS GLY LYS LYS ILE PHE VAL GLN
SEQRES 2 A 105 LYS CYS ALA GLN CYS HIS THR VAL GLU LYS GLY GLY LYS
SEQRES 3 A 105 HIS LYS THR GLY PRO ASN LEU HIS GLY LEU PHE GLY ARG
SEQRES 4 A 105 LYS THR GLY GLN ALA PRO GLY PHE THR TYR THR ASP ALA
SEQRES 5 A 105 ASN LYS ASN LYS GLY ILE THR TRP LYS GLU GLU THR LEU
SEQRES 6 A 105 MET GLU TYR LEU GLU ASN PRO LYS LYS TYR ILE PRO GLY
SEQRES 7 A 105 THR LYS MET ILE PHE ALA GLY ILE LYS LYS LYS THR GLU
SEQRES 8 A 105 ARG GLU ASP LEU ILE ALA TYR LEU LYS LYS ALA THR ASN
SEQRES 9 A 105 GLU
SEQRES 1 B 105 ACE GLY ASP VAL GLU LYS GLY LYS LYS ILE PHE VAL GLN
SEQRES 2 B 105 LYS CYS ALA GLN CYS HIS THR VAL GLU LYS GLY GLY LYS
SEQRES 3 B 105 HIS LYS THR GLY PRO ASN LEU HIS GLY LEU PHE GLY ARG
SEQRES 4 B 105 LYS THR GLY GLN ALA PRO GLY PHE THR TYR THR ASP ALA
SEQRES 5 B 105 ASN LYS ASN LYS GLY ILE THR TRP LYS GLU GLU THR LEU
SEQRES 6 B 105 MET GLU TYR LEU GLU ASN PRO LYS LYS TYR ILE PRO GLY
SEQRES 7 B 105 THR LYS MET ILE PHE ALA GLY ILE LYS LYS LYS THR GLU
SEQRES 8 B 105 ARG GLU ASP LEU ILE ALA TYR LEU LYS LYS ALA THR ASN
SEQRES 9 B 105 GLU
SEQRES 1 C 105 ACE GLY ASP VAL GLU LYS GLY LYS LYS ILE PHE VAL GLN
SEQRES 2 C 105 LYS CYS ALA GLN CYS HIS THR VAL GLU LYS GLY GLY LYS
SEQRES 3 C 105 HIS LYS THR GLY PRO ASN LEU HIS GLY LEU PHE GLY ARG
SEQRES 4 C 105 LYS THR GLY GLN ALA PRO GLY PHE THR TYR THR ASP ALA
SEQRES 5 C 105 ASN LYS ASN LYS GLY ILE THR TRP LYS GLU GLU THR LEU
SEQRES 6 C 105 MET GLU TYR LEU GLU ASN PRO LYS LYS TYR ILE PRO GLY
SEQRES 7 C 105 THR LYS MET ILE PHE ALA GLY ILE LYS LYS LYS THR GLU
SEQRES 8 C 105 ARG GLU ASP LEU ILE ALA TYR LEU LYS LYS ALA THR ASN
SEQRES 9 C 105 GLU
HET ACE A 0 3
HET ACE B 0 3
HET ACE C 0 3
HET HEC A 105 43
HET NO3 A 106 4
HET NO3 A 107 4
HET NO3 A 108 4
HET NO3 A 109 4
HET NO3 A 110 4
HET NO3 A 111 4
HET NO3 A 112 4
HET HEC B 105 43
HET NO3 B 106 4
HET NO3 B 107 4
HET NO3 B 108 4
HET NO3 B 109 4
HET NO3 B 110 4
HET NO3 B 111 4
HET NO3 B 112 4
HET NO3 B 113 4
HET HEC C 105 43
HET NO3 C 106 4
HET NO3 C 107 4
HET NO3 C 108 4
HETNAM ACE ACETYL GROUP
HETNAM HEC HEME C
HETNAM NO3 NITRATE ION
FORMUL 1 ACE 3(C2 H4 O)
FORMUL 4 HEC 3(C34 H34 FE N4 O4)
FORMUL 5 NO3 18(N O3 1-)
FORMUL 25 HOH *365(H2 O)
HELIX 1 1 ASP A 2 CYS A 14 1 13
HELIX 2 2 THR A 49 ASN A 54 1 6
HELIX 3 3 LYS A 60 ASN A 70 1 11
HELIX 4 4 ASN A 70 ILE A 75 1 6
HELIX 5 5 LYS A 87 THR A 102 1 16
HELIX 6 6 ASP B 2 CYS B 14 1 13
HELIX 7 7 THR B 49 ASN B 54 1 6
HELIX 8 8 LYS B 60 ASN B 70 1 11
HELIX 9 9 ASN B 70 ILE B 75 1 6
HELIX 10 10 LYS B 87 THR B 102 1 16
HELIX 11 11 ASP C 2 CYS C 14 1 13
HELIX 12 12 THR C 49 ASN C 54 1 6
HELIX 13 13 LYS C 60 ASN C 70 1 11
HELIX 14 14 ASN C 70 ILE C 75 1 6
HELIX 15 15 LYS C 87 THR C 102 1 16
LINK NE2 HIS B 18 FE HEC B 105 1555 1555 2.00
LINK NE2 HIS C 18 FE HEC C 105 1555 1555 2.04
LINK NE2 HIS A 18 FE HEC A 105 1555 1555 2.05
LINK SD MET C 80 FE HEC C 105 1555 1555 2.28
LINK SD MET A 80 FE HEC A 105 1555 1555 2.36
LINK SD MET B 80 FE HEC B 105 1555 1555 2.36
LINK SG CYS A 14 CAB HEC A 105 1555 1555 1.83
LINK SG CYS B 14 CAB HEC B 105 1555 1555 1.88
LINK SG CYS C 14 CAB HEC C 105 1555 1555 1.84
LINK SG CYS A 17 CAC HEC A 105 1555 1555 1.98
LINK SG CYS B 17 CAC HEC B 105 1555 1555 2.08
LINK SG CYS C 17 CAC HEC C 105 1555 1555 2.06
LINK C ACE A 0 N GLY A 1 1555 1555 1.33
LINK C ACE B 0 N GLY B 1 1555 1555 1.34
LINK C ACE C 0 N GLY C 1 1555 1555 1.34
SITE 1 AC1 24 LYS A 13 CYS A 14 CYS A 17 HIS A 18
SITE 2 AC1 24 THR A 28 GLY A 29 PRO A 30 THR A 40
SITE 3 AC1 24 GLY A 41 TYR A 48 THR A 49 ASN A 52
SITE 4 AC1 24 TRP A 59 LEU A 64 TYR A 67 LEU A 68
SITE 5 AC1 24 THR A 78 LYS A 79 MET A 80 ILE A 81
SITE 6 AC1 24 PHE A 82 LEU A 94 HOH A 131 HOH A 211
SITE 1 AC2 6 VAL A 11 HOH A 141 HOH A 168 PHE C 82
SITE 2 AC2 6 ALA C 83 GLY C 84
SITE 1 AC3 7 PHE A 82 ALA A 83 GLY A 84 HOH A 179
SITE 2 AC3 7 LYS B 8 VAL B 11 GLN B 12
SITE 1 AC4 5 LYS A 13 GLY A 84 LYS A 86 LYS A 87
SITE 2 AC4 5 GLU A 90
SITE 1 AC5 7 THR A 19 VAL A 20 GLU A 21 HOH A 236
SITE 2 AC5 7 THR C 28 ILE C 81 HOH C 124
SITE 1 AC6 7 THR A 28 ILE A 81 HOH A 178 PHE B 10
SITE 2 AC6 7 THR B 19 VAL B 20 GLU B 21
SITE 1 AC7 8 GLY A 77 HOH A 132 HOH A 261 LYS C 39
SITE 2 AC7 8 ILE C 57 THR C 58 LYS C 60 THR C 63
SITE 1 AC8 6 GLY A 45 PHE A 46 THR A 47 HOH A 118
SITE 2 AC8 6 HOH A 180 LYS B 53
SITE 1 AC9 25 LYS B 13 CYS B 14 GLN B 16 CYS B 17
SITE 2 AC9 25 HIS B 18 THR B 28 GLY B 29 PRO B 30
SITE 3 AC9 25 THR B 40 GLY B 41 TYR B 48 THR B 49
SITE 4 AC9 25 ASN B 52 TRP B 59 LEU B 64 TYR B 67
SITE 5 AC9 25 LEU B 68 THR B 78 LYS B 79 MET B 80
SITE 6 AC9 25 ILE B 81 PHE B 82 LEU B 94 HOH B 119
SITE 7 AC9 25 HOH B 135
SITE 1 BC1 7 LYS A 53 HIS B 26 GLY B 45 PHE B 46
SITE 2 BC1 7 THR B 47 HOH B 276 LYS C 25
SITE 1 BC2 5 LYS B 27 THR B 28 NO3 B 111 LYS C 25
SITE 2 BC2 5 LYS C 27
SITE 1 BC3 6 PHE B 82 ALA B 83 GLY B 84 HOH B 147
SITE 2 BC3 6 HOH B 332 VAL C 11
SITE 1 BC4 6 LYS B 13 GLY B 84 ILE B 85 LYS B 86
SITE 2 BC4 6 HOH B 163 LYS C 8
SITE 1 BC5 10 LYS B 39 GLY B 56 ILE B 57 THR B 58
SITE 2 BC5 10 LYS B 60 THR B 63 HOH B 194 HOH B 355
SITE 3 BC5 10 GLY C 77 HOH C 196
SITE 1 BC6 9 LYS A 25 HIS A 26 LYS A 27 THR A 28
SITE 2 BC6 9 HOH A 347 LYS B 25 LYS B 27 NO3 B 107
SITE 3 BC6 9 HOH B 133
SITE 1 BC7 6 LYS A 100 PHE B 36 LYS B 60 GLU B 61
SITE 2 BC7 6 LYS B 99 HOH B 136
SITE 1 BC8 9 LYS A 39 GLY A 56 ILE A 57 THR A 58
SITE 2 BC8 9 LYS A 60 HOH A 142 GLY B 77 HOH B 263
SITE 3 BC8 9 HOH B 354
SITE 1 BC9 26 ALA A 15 LYS C 13 CYS C 14 CYS C 17
SITE 2 BC9 26 HIS C 18 THR C 28 GLY C 29 PRO C 30
SITE 3 BC9 26 THR C 40 GLY C 41 PHE C 46 TYR C 48
SITE 4 BC9 26 THR C 49 ASN C 52 TRP C 59 TYR C 67
SITE 5 BC9 26 LEU C 68 THR C 78 LYS C 79 MET C 80
SITE 6 BC9 26 ILE C 81 PHE C 82 LEU C 98 HOH C 121
SITE 7 BC9 26 HOH C 124 HOH C 136
SITE 1 CC1 4 GLU A 4 LYS A 7 LYS C 72 ALA C 83
SITE 1 CC2 7 THR B 28 ILE B 81 THR C 19 VAL C 20
SITE 2 CC2 7 GLU C 21 HOH C 117 HOH C 318
SITE 1 CC3 7 LYS A 8 HOH A 351 LYS C 13 GLY C 84
SITE 2 CC3 7 ILE C 85 LYS C 86 HOH C 345
CRYST1 90.092 52.029 77.749 90.00 123.07 90.00 C 1 2 1 12
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 0.011100 0.000000 0.007227 0.00000
SCALE2 0.000000 0.019220 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015348 0.00000
HETATM 1 C ACE A 0 4.683 -4.418 30.244 1.00 27.27 C
HETATM 2 O ACE A 0 5.586 -4.825 31.008 1.00 29.08 O
HETATM 3 CH3 ACE A 0 3.453 -3.823 30.831 1.00 26.82 C
(ATOM LINES ARE NOT SHOWN.)
END
