HEADER OXIDOREDUCTASE 15-MAY-05 1ZOY
TITLE CRYSTAL STRUCTURE OF MITOCHONDRIAL RESPIRATORY COMPLEX II
TITLE 2 FROM PORCINE HEART AT 2.4 ANGSTROMS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FAD-BINDING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: FLAVOPROTEIN;
COMPND 5 EC: 1.3.5.1;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: IRON-SULFUR PROTEIN;
COMPND 8 CHAIN: B;
COMPND 9 EC: 1.3.5.1;
COMPND 10 MOL_ID: 3;
COMPND 11 MOLECULE: LARGE CYTOCHROME BINDING PROTEIN;
COMPND 12 CHAIN: C;
COMPND 13 MOL_ID: 4;
COMPND 14 MOLECULE: SMALL CYTOCHROME BINDING PROTEIN;
COMPND 15 CHAIN: D
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823;
SOURCE 5 TISSUE: PORCINE HEART;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 8 ORGANISM_COMMON: PIG;
SOURCE 9 ORGANISM_TAXID: 9823;
SOURCE 10 TISSUE: PORCINE HEART;
SOURCE 11 MOL_ID: 3;
SOURCE 12 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 13 ORGANISM_COMMON: PIG;
SOURCE 14 ORGANISM_TAXID: 9823;
SOURCE 15 TISSUE: PORCINE HEART;
SOURCE 16 MOL_ID: 4;
SOURCE 17 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 18 ORGANISM_COMMON: PIG;
SOURCE 19 ORGANISM_TAXID: 9823;
SOURCE 20 TISSUE: PORCINE HEART
KEYWDS SUCCINATE, UBIQUINONE OXIDOREDUCTASE, MITOCHONDRIAL
KEYWDS 2 RESPIRATORY COMPLEX II, MEMBRANE PROTEIN STRUCTURE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.SUN,X.HUO,Y.ZHAI,A.WANG,J.XU,D.SU,M.BARTLAM,Z.RAO
REVDAT 2 24-FEB-09 1ZOY 1 VERSN
REVDAT 1 12-JUL-05 1ZOY 0
JRNL AUTH F.SUN,X.HUO,Y.ZHAI,A.WANG,J.XU,D.SU,M.BARTLAM,Z.RAO
JRNL TITL CRYSTAL STRUCTURE OF MITOCHONDRIAL RESPIRATORY
JRNL TITL 2 MEMBRANE PROTEIN COMPLEX II
JRNL REF CELL(CAMBRIDGE,MASS.) V. 121 1043 2005
JRNL REFN ISSN 0092-8674
JRNL PMID 15989954
JRNL DOI 10.1016/J.CELL.2005.05.025
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 56559
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 SET) : 0.213
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.400
REMARK 3 FREE R VALUE TEST SET COUNT : 5757
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.49
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 43.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3730
REMARK 3 BIN FREE R VALUE : 0.3810
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 280
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8480
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 213
REMARK 3 SOLVENT ATOMS : 331
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 69.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.34
REMARK 3 ESD FROM SIGMAA (A) : 0.47
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.41
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.48
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.018
REMARK 3 BOND ANGLES (DEGREES) : 1.81
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.82
REMARK 3 IMPROPER ANGLES (DEGREES) : 4.83
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ZOY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-MAY-05.
REMARK 100 THE RCSB ID CODE IS RCSB032971.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-NOV-04; 10-FEB-05
REMARK 200 TEMPERATURE (KELVIN) : 100; 100
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : APS; APS
REMARK 200 BEAMLINE : 19-ID; 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.74101; 1.0322
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111);
REMARK 200 SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315; ADSC
REMARK 200 QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 60175
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 85.1
REMARK 200 DATA REDUNDANCY : 9.100
REMARK 200 R MERGE (I) : 0.12500
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) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 40.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.50100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SAD; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD COMBINED WITH MR
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1NEK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: N-NONYL-D-MALTOSIDE, N-DECYL-D-
REMARK 280 MALTOSIDE, HEPES, PEG 4000, 1,6-HEXANEDIOL, NACL, CACL2,
REMARK 280 SUCROSE, PH 7.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 290.0K
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 35.11900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 146.94800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.77850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 146.94800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.11900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.77850
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 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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 19430 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -155.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 SER A 1
REMARK 465 SER A 2
REMARK 465 ALA A 3
REMARK 465 LYS A 4
REMARK 465 VAL A 5
REMARK 465 SER A 6
REMARK 465 ASP A 7
REMARK 465 ALA A 8
REMARK 465 ILE A 9
REMARK 465 ALA B 1
REMARK 465 GLN B 2
REMARK 465 THR B 3
REMARK 465 ALA B 4
REMARK 465 ALA B 5
REMARK 465 ALA B 6
REMARK 465 THR B 7
REMARK 465 ALA B 8
REMARK 465 LYS B 248
REMARK 465 LYS B 249
REMARK 465 ALA B 250
REMARK 465 SER B 251
REMARK 465 VAL B 252
REMARK 465 LEU C 4
REMARK 465 GLY C 5
REMARK 465 ALA D 34
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS B 73 CB CYS B 73 SG -0.107
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 THR A 11 21.52 37.98
REMARK 500 ALA A 67 119.35 -173.41
REMARK 500 ALA A 68 59.27 -69.62
REMARK 500 LYS A 137 53.91 31.39
REMARK 500 ALA A 151 -117.42 50.28
REMARK 500 TYR A 217 44.03 -142.17
REMARK 500 ARG A 219 1.14 -62.57
REMARK 500 ASP A 247 37.93 38.56
REMARK 500 PHE A 250 93.31 -65.05
REMARK 500 ILE A 258 129.66 -39.14
REMARK 500 THR A 266 144.92 -27.43
REMARK 500 GLU A 286 -18.26 174.97
REMARK 500 ALA A 289 87.80 -159.25
REMARK 500 LYS A 293 -139.93 50.73
REMARK 500 LEU A 295 64.07 -113.74
REMARK 500 SER A 304 -70.34 -67.26
REMARK 500 ARG A 313 39.49 -143.82
REMARK 500 PRO A 317 -74.44 -16.25
REMARK 500 HIS A 321 -162.96 -125.12
REMARK 500 VAL A 322 -161.08 -129.92
REMARK 500 LEU A 326 -18.20 -140.33
REMARK 500 LYS A 355 11.64 -143.20
REMARK 500 HIS A 365 -59.24 -142.60
REMARK 500 SER A 403 72.19 62.85
REMARK 500 ASN A 408 119.49 -166.84
REMARK 500 PRO A 444 -3.71 -57.16
REMARK 500 ALA A 482 -151.20 -87.22
REMARK 500 LEU A 504 -9.94 -52.61
REMARK 500 ARG A 512 16.76 -140.40
REMARK 500 TRP A 516 63.58 36.26
REMARK 500 LYS A 556 31.38 -80.53
REMARK 500 TYR A 564 0.43 -67.18
REMARK 500 GLN A 569 -58.38 166.10
REMARK 500 ASN A 608 104.46 -167.25
REMARK 500 SER A 621 141.66 -170.61
REMARK 500 TRP B 19 113.80 -174.36
REMARK 500 ASP B 22 32.14 -98.84
REMARK 500 THR B 24 132.02 -31.22
REMARK 500 SER B 64 -75.25 -166.44
REMARK 500 ALA B 74 112.86 -16.55
REMARK 500 LYS B 109 134.44 -178.40
REMARK 500 ASP B 110 -119.37 42.30
REMARK 500 TYR B 213 3.89 -61.32
REMARK 500 HIS C 29 -91.96 -131.84
REMARK 500 LEU C 80 38.98 -154.67
REMARK 500 CYS C 81 14.85 46.86
REMARK 500 LEU C 82 100.36 -25.75
REMARK 500 THR C 85 47.73 -83.41
REMARK 500 LEU C 86 -38.15 -160.26
REMARK 500 ALA C 141 1.78 -67.93
REMARK 500 LYS D 37 52.15 -108.56
REMARK 500 ALA D 96 -74.17 -42.71
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 EPH D 1306
REMARK 610 EPH D 1307
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 UQ1 B 1201
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 C1305 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 101 NE2
REMARK 620 2 HIS D 79 NE2 160.0
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 700
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES B 302
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B 303
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S B 304
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 1305
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPH D 1306
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPH D 1307
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UQ1 B 1201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ZP0 RELATED DB: PDB
REMARK 900 MITOCHONDRIAL RESPIRATORY COMPLEX II BOUND WITH 3-
REMARK 900 NITROPROPIONATE AND 2-THENOYLTRIFLUOROACETONE
DBREF 1ZOY A 17 557 UNP Q0QF01 Q0QF01_PIG 1 541
DBREF 1ZOY B 1 251 UNP Q007T0 DHSB_PIG 29 279
DBREF 1ZOY C 4 143 PDB 1ZOY 1ZOY 4 143
DBREF 1ZOY D 34 136 UNP A5GZW8 DHSD_PIG 57 159
SEQRES 1 A 622 SER SER ALA LYS VAL SER ASP ALA ILE SER THR GLN TYR
SEQRES 2 A 622 PRO VAL VAL ASP HIS GLU PHE ASP ALA VAL VAL VAL GLY
SEQRES 3 A 622 ALA GLY GLY ALA GLY LEU ARG ALA ALA PHE GLY LEU SER
SEQRES 4 A 622 GLU ALA GLY PHE ASN THR ALA CYS VAL THR LYS LEU PHE
SEQRES 5 A 622 PRO THR ARG SER HIS THR VAL ALA ALA GLN GLY GLY ILE
SEQRES 6 A 622 ASN ALA ALA LEU GLY ASN MET GLU GLU ASP ASN TRP ARG
SEQRES 7 A 622 TRP HIS PHE TYR ASP THR VAL LYS GLY SER ASP TRP LEU
SEQRES 8 A 622 GLY ASP GLN ASP ALA ILE HIS TYR MET THR GLU GLN ALA
SEQRES 9 A 622 PRO ALA SER VAL VAL GLU LEU GLU ASN TYR GLY MET PRO
SEQRES 10 A 622 PHE SER ARG THR GLU ASP GLY LYS ILE TYR GLN ARG ALA
SEQRES 11 A 622 PHE GLY GLY GLN SER LEU LYS PHE GLY LYS GLY GLY GLN
SEQRES 12 A 622 ALA HIS ARG CYS CYS CYS VAL ALA ASP ARG THR GLY HIS
SEQRES 13 A 622 SER LEU LEU HIS THR LEU TYR GLY ARG SER LEU ARG TYR
SEQRES 14 A 622 ASP THR SER TYR PHE VAL GLU TYR PHE ALA LEU ASP LEU
SEQRES 15 A 622 LEU MET GLU ASN GLY GLU CYS ARG GLY VAL ILE ALA LEU
SEQRES 16 A 622 CYS ILE GLU ASP GLY SER ILE HIS ARG ILE ARG ALA ARG
SEQRES 17 A 622 ASN THR VAL VAL ALA THR GLY GLY TYR GLY ARG THR TYR
SEQRES 18 A 622 PHE SER CYS THR SER ALA HIS THR SER THR GLY ASP GLY
SEQRES 19 A 622 THR ALA MET VAL THR ARG ALA GLY LEU PRO CYS GLN ASP
SEQRES 20 A 622 LEU GLU PHE VAL GLN PHE HIS PRO THR GLY ILE TYR GLY
SEQRES 21 A 622 ALA GLY CYS LEU ILE THR GLU GLY CYS ARG GLY GLU GLY
SEQRES 22 A 622 GLY ILE LEU ILE ASN SER GLN GLY GLU ARG PHE MET GLU
SEQRES 23 A 622 ARG TYR ALA PRO VAL ALA LYS ASP LEU ALA SER ARG ASP
SEQRES 24 A 622 VAL VAL SER ARG SER MET THR LEU GLU ILE ARG GLU GLY
SEQRES 25 A 622 ARG GLY CYS GLY PRO GLU LYS ASP HIS VAL TYR LEU GLN
SEQRES 26 A 622 LEU HIS HIS LEU PRO PRO GLU GLN LEU ALA VAL ARG LEU
SEQRES 27 A 622 PRO GLY ILE SER GLU THR ALA MET ILE PHE ALA GLY VAL
SEQRES 28 A 622 ASP VAL THR LYS GLU PRO ILE PRO VAL LEU PRO THR VAL
SEQRES 29 A 622 HIS TYR ASN MET GLY GLY ILE PRO THR ASN TYR LYS GLY
SEQRES 30 A 622 GLN VAL LEU ARG HIS VAL ASN GLY GLN ASP GLN VAL VAL
SEQRES 31 A 622 PRO GLY LEU TYR ALA CYS GLY GLU ALA ALA CYS ALA SER
SEQRES 32 A 622 VAL HIS GLY ALA ASN ARG LEU GLY ALA ASN SER LEU LEU
SEQRES 33 A 622 ASP LEU VAL VAL PHE GLY ARG ALA CYS ALA LEU SER ILE
SEQRES 34 A 622 ALA GLU SER CYS ARG PRO GLY ASP LYS VAL PRO SER ILE
SEQRES 35 A 622 LYS PRO ASN ALA GLY GLU GLU SER VAL MET ASN LEU ASP
SEQRES 36 A 622 LYS LEU ARG PHE ALA ASN GLY THR ILE ARG THR SER GLU
SEQRES 37 A 622 LEU ARG LEU SER MET GLN LYS SER MET GLN SER HIS ALA
SEQRES 38 A 622 ALA VAL PHE ARG VAL GLY SER VAL LEU GLN GLU GLY CYS
SEQRES 39 A 622 GLU LYS ILE LEU ARG LEU TYR GLY ASP LEU GLN HIS LEU
SEQRES 40 A 622 LYS THR PHE ASP ARG GLY MET VAL TRP ASN THR ASP LEU
SEQRES 41 A 622 VAL GLU THR LEU GLU LEU GLN ASN LEU MET LEU CYS ALA
SEQRES 42 A 622 LEU GLN THR ILE TYR GLY ALA GLU ALA ARG LYS GLU SER
SEQRES 43 A 622 ARG GLY ALA HIS ALA ARG GLU ASP PHE LYS GLU ARG VAL
SEQRES 44 A 622 ASP GLU TYR ASP TYR SER LYS PRO ILE GLN GLY GLN GLN
SEQRES 45 A 622 LYS LYS PRO PHE GLN GLU HIS TRP ARG LYS HIS THR LEU
SEQRES 46 A 622 SER TYR VAL ASP VAL LYS THR GLY LYS VAL SER LEU GLU
SEQRES 47 A 622 TYR ARG PRO VAL ILE ASP LYS THR LEU ASN GLU ALA ASP
SEQRES 48 A 622 CYS ALA THR VAL PRO PRO ALA ILE ARG SER TYR
SEQRES 1 B 252 ALA GLN THR ALA ALA ALA THR ALA PRO ARG ILE LYS LYS
SEQRES 2 B 252 PHE ALA ILE TYR ARG TRP ASP PRO ASP LYS THR GLY ASP
SEQRES 3 B 252 LYS PRO HIS MET GLN THR TYR GLU ILE ASP LEU ASN ASN
SEQRES 4 B 252 CYS GLY PRO MET VAL LEU ASP ALA LEU ILE LYS ILE LYS
SEQRES 5 B 252 ASN GLU ILE ASP SER THR LEU THR PHE ARG ARG SER CYS
SEQRES 6 B 252 ARG GLU GLY ILE CYS GLY SER CYS ALA MET ASN ILE ASN
SEQRES 7 B 252 GLY GLY ASN THR LEU ALA CYS THR ARG ARG ILE ASP THR
SEQRES 8 B 252 ASN LEU ASP LYS VAL SER LYS ILE TYR PRO LEU PRO HIS
SEQRES 9 B 252 MET TYR VAL ILE LYS ASP LEU VAL PRO ASP LEU SER ASN
SEQRES 10 B 252 PHE TYR ALA GLN TYR LYS SER ILE GLU PRO TYR LEU LYS
SEQRES 11 B 252 LYS LYS ASP GLU SER GLN GLU GLY LYS GLN GLN TYR LEU
SEQRES 12 B 252 GLN SER ILE GLU GLU ARG GLU LYS LEU ASP GLY LEU TYR
SEQRES 13 B 252 GLU CYS ILE LEU CYS ALA CYS CYS SER THR SER CYS PRO
SEQRES 14 B 252 SER TYR TRP TRP ASN GLY ASP LYS TYR LEU GLY PRO ALA
SEQRES 15 B 252 VAL LEU MET GLN ALA TYR ARG TRP MET ILE ASP SER ARG
SEQRES 16 B 252 ASP ASP PHE THR GLU GLU ARG LEU ALA LYS LEU GLN ASP
SEQRES 17 B 252 PRO PHE SER LEU TYR ARG CYS HIS THR ILE MET ASN CYS
SEQRES 18 B 252 THR GLY THR CYS PRO LYS GLY LEU ASN PRO GLY LYS ALA
SEQRES 19 B 252 ILE ALA GLU ILE LYS LYS MET MET ALA THR TYR LYS GLU
SEQRES 20 B 252 LYS LYS ALA SER VAL
SEQRES 1 C 140 LEU GLY THR THR ALA LYS GLU GLU MET GLU ARG PHE TRP
SEQRES 2 C 140 ASN LYS ASN LEU GLY SER ASN ARG PRO LEU SER PRO HIS
SEQRES 3 C 140 ILE THR ILE TYR ARG TRP SER LEU PRO MET ALA MET SER
SEQRES 4 C 140 ILE CYS HIS ARG GLY THR GLY ILE ALA LEU SER ALA GLY
SEQRES 5 C 140 VAL SER LEU PHE GLY LEU SER ALA LEU LEU LEU PRO GLY
SEQRES 6 C 140 ASN PHE GLU SER HIS LEU GLU LEU VAL LYS SER LEU CYS
SEQRES 7 C 140 LEU GLY PRO THR LEU ILE TYR THR ALA LYS PHE GLY ILE
SEQRES 8 C 140 VAL PHE PRO LEU MET TYR HIS THR TRP ASN GLY ILE ARG
SEQRES 9 C 140 HIS LEU ILE TRP ASP LEU GLY LYS GLY LEU THR ILE PRO
SEQRES 10 C 140 GLN LEU THR GLN SER GLY VAL VAL VAL LEU ILE LEU THR
SEQRES 11 C 140 VAL LEU SER SER VAL GLY LEU ALA ALA MET
SEQRES 1 D 103 ALA SER SER LYS ALA ALA SER LEU HIS TRP THR GLY GLU
SEQRES 2 D 103 ARG VAL VAL SER VAL LEU LEU LEU GLY LEU LEU PRO ALA
SEQRES 3 D 103 ALA TYR LEU ASN PRO CYS SER ALA MET ASP TYR SER LEU
SEQRES 4 D 103 ALA ALA ALA LEU THR LEU HIS GLY HIS TRP GLY ILE GLY
SEQRES 5 D 103 GLN VAL VAL THR ASP TYR VAL ARG GLY ASP ALA LEU GLN
SEQRES 6 D 103 LYS ALA ALA LYS ALA GLY LEU LEU ALA LEU SER ALA PHE
SEQRES 7 D 103 THR PHE ALA GLY LEU CYS TYR PHE ASN TYR HIS ASP VAL
SEQRES 8 D 103 GLY ILE CYS LYS ALA VAL ALA MET LEU TRP LYS LEU
HET FAD A 700 53
HET FES B 302 4
HET SF4 B 303 8
HET F3S B 304 7
HET HEM C1305 43
HET EPH D1306 44
HET EPH D1307 36
HET UQ1 B1201 18
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM FES FE2/S2 (INORGANIC) CLUSTER
HETNAM SF4 IRON/SULFUR CLUSTER
HETNAM F3S FE3-S4 CLUSTER
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM EPH L-ALPHA-PHOSPHATIDYL-BETA-OLEOYL-GAMMA-PALMITOYL-
HETNAM 2 EPH PHOSPHATIDYLETHANOLAMINE
HETNAM UQ1 UBIQUINONE-1
HETSYN HEM HEME
FORMUL 5 FAD C27 H33 N9 O15 P2
FORMUL 6 FES FE2 S2
FORMUL 7 SF4 FE4 S4
FORMUL 8 F3S FE3 S4
FORMUL 9 HEM C34 H32 FE N4 O4
FORMUL 10 EPH 2(C39 H68 N O8 P)
FORMUL 12 UQ1 C14 H18 O4
FORMUL 13 HOH *331(H2 O)
HELIX 1 1 GLY A 28 ALA A 41 1 14
HELIX 2 2 PHE A 52 ALA A 61 5 10
HELIX 3 3 ASN A 76 SER A 88 1 13
HELIX 4 4 ASP A 93 GLY A 115 1 23
HELIX 5 5 ARG A 153 LEU A 167 1 15
HELIX 6 6 TYR A 217 TYR A 221 5 5
HELIX 7 7 GLY A 232 ALA A 241 1 10
HELIX 8 8 GLU A 267 GLY A 273 1 7
HELIX 9 9 SER A 297 GLY A 312 1 16
HELIX 10 10 GLU A 332 ARG A 337 1 6
HELIX 11 11 LEU A 338 GLY A 350 1 13
HELIX 12 12 ASN A 413 CYS A 433 1 21
HELIX 13 13 GLY A 447 PHE A 459 1 13
HELIX 14 14 THR A 466 ALA A 481 1 16
HELIX 15 15 VAL A 486 LEU A 504 1 19
HELIX 16 16 ASN A 517 ARG A 543 1 27
HELIX 17 17 PRO A 575 HIS A 579 5 5
HELIX 18 18 ASN B 38 CYS B 40 5 3
HELIX 19 19 MET B 43 GLU B 54 1 12
HELIX 20 20 LEU B 115 ILE B 125 1 11
HELIX 21 21 SER B 145 LYS B 151 1 7
HELIX 22 22 CYS B 164 SER B 167 5 4
HELIX 23 23 CYS B 168 GLY B 175 1 8
HELIX 24 24 LEU B 179 ILE B 192 1 14
HELIX 25 25 PHE B 198 LYS B 205 1 8
HELIX 26 26 CYS B 221 CYS B 225 5 5
HELIX 27 27 ASN B 230 ALA B 243 1 14
HELIX 28 28 THR C 7 GLY C 21 1 15
HELIX 29 29 SER C 36 LEU C 66 1 31
HELIX 30 30 ASN C 69 SER C 79 1 11
HELIX 31 31 GLY C 83 LEU C 113 1 31
HELIX 32 32 THR C 118 ALA C 141 1 24
HELIX 33 33 LYS D 37 ASN D 63 1 27
HELIX 34 34 CYS D 65 VAL D 92 1 28
HELIX 35 35 GLY D 94 HIS D 122 1 29
HELIX 36 36 GLY D 125 LYS D 135 1 11
SHEET 1 A 4 VAL A 15 GLU A 19 0
SHEET 2 A 4 ILE A 202 ARG A 206 1 O ILE A 202 N VAL A 16
SHEET 3 A 4 GLU A 188 CYS A 196 -1 N ALA A 194 O HIS A 203
SHEET 4 A 4 TYR A 177 GLU A 185 -1 N LEU A 183 O GLY A 191
SHEET 1 B 6 SER A 172 VAL A 175 0
SHEET 2 B 6 THR A 45 THR A 49 1 N THR A 45 O SER A 172
SHEET 3 B 6 ALA A 22 VAL A 25 1 N VAL A 24 O VAL A 48
SHEET 4 B 6 ASN A 209 VAL A 212 1 O VAL A 211 N VAL A 25
SHEET 5 B 6 GLN A 386 ALA A 395 1 O TYR A 394 N THR A 210
SHEET 6 B 6 GLN A 378 VAL A 383 -1 N VAL A 383 O GLN A 386
SHEET 1 C 3 ILE A 65 ASN A 66 0
SHEET 2 C 3 GLN A 143 CYS A 148 -1 O CYS A 148 N ILE A 65
SHEET 3 C 3 GLN A 128 SER A 135 -1 N GLN A 134 O ALA A 144
SHEET 1 D 3 CYS A 245 GLN A 246 0
SHEET 2 D 3 HIS A 583 VAL A 588 -1 O SER A 586 N CYS A 245
SHEET 3 D 3 VAL A 595 ARG A 600 -1 O GLU A 598 N LEU A 585
SHEET 1 E 2 VAL A 251 HIS A 254 0
SHEET 2 E 2 THR A 363 ASN A 367 -1 O TYR A 366 N GLN A 252
SHEET 1 F 2 ILE A 275 ILE A 277 0
SHEET 2 F 2 TYR A 323 GLN A 325 -1 O GLN A 325 N ILE A 275
SHEET 1 G 2 ILE A 371 PRO A 372 0
SHEET 2 G 2 ALA A 400 CYS A 401 1 O CYS A 401 N ILE A 371
SHEET 1 H 2 ILE A 464 ARG A 465 0
SHEET 2 H 2 LEU A 507 LYS A 508 1 O LYS A 508 N ILE A 464
SHEET 1 I 5 HIS B 29 ASP B 36 0
SHEET 2 I 5 ILE B 11 ARG B 18 -1 N PHE B 14 O TYR B 33
SHEET 3 I 5 VAL B 96 TYR B 100 1 O SER B 97 N ALA B 15
SHEET 4 I 5 MET B 75 ILE B 77 -1 N ASN B 76 O TYR B 100
SHEET 5 I 5 GLY B 80 THR B 82 -1 O GLY B 80 N ILE B 77
SHEET 1 J 2 VAL B 107 LYS B 109 0
SHEET 2 J 2 VAL B 112 PRO B 113 -1 O VAL B 112 N ILE B 108
LINK C8M FAD A 700 NE2 HIS A 57 1555 1555 1.71
LINK FE2 FES B 302 SG CYS B 65 1555 1555 2.31
LINK FE2 FES B 302 SG CYS B 70 1555 1555 2.19
LINK FE1 FES B 302 SG CYS B 73 1555 1555 2.33
LINK FE1 FES B 302 SG CYS B 85 1555 1555 2.49
LINK FE2 SF4 B 303 SG CYS B 158 1555 1555 2.24
LINK FE4 SF4 B 303 SG CYS B 161 1555 1555 2.40
LINK FE1 SF4 B 303 SG CYS B 164 1555 1555 2.28
LINK FE3 SF4 B 303 SG CYS B 225 1555 1555 2.44
LINK FE4 F3S B 304 SG CYS B 168 1555 1555 2.45
LINK FE1 F3S B 304 SG CYS B 215 1555 1555 2.36
LINK FE3 F3S B 304 SG CYS B 221 1555 1555 2.19
LINK FE HEM C1305 NE2 HIS C 101 1555 1555 2.23
LINK FE HEM C1305 NE2 HIS D 79 1555 1555 2.18
SITE 1 AC1 43 GLY A 26 ALA A 27 GLY A 28 GLY A 29
SITE 2 AC1 43 ALA A 30 VAL A 48 THR A 49 LYS A 50
SITE 3 AC1 43 LEU A 51 SER A 56 HIS A 57 THR A 58
SITE 4 AC1 43 ALA A 60 ALA A 61 GLN A 62 GLY A 63
SITE 5 AC1 43 GLY A 64 TYR A 177 PHE A 178 ALA A 179
SITE 6 AC1 43 ALA A 213 THR A 214 GLY A 215 THR A 225
SITE 7 AC1 43 ASP A 233 LEU A 264 HIS A 365 TYR A 366
SITE 8 AC1 43 GLY A 397 GLU A 398 ARG A 409 ALA A 412
SITE 9 AC1 43 ASN A 413 SER A 414 LEU A 415 LEU A 418
SITE 10 AC1 43 HOH A 703 HOH A 705 HOH A 769 HOH A 790
SITE 11 AC1 43 HOH A 796 HOH A 847 HOH A 886
SITE 1 AC2 8 SER B 64 CYS B 65 ARG B 66 GLY B 68
SITE 2 AC2 8 CYS B 70 GLY B 71 CYS B 73 CYS B 85
SITE 1 AC3 6 CYS B 158 CYS B 161 ALA B 162 CYS B 164
SITE 2 AC3 6 CYS B 225 PRO B 226
SITE 1 AC4 9 CYS B 168 TYR B 178 PRO B 181 CYS B 215
SITE 2 AC4 9 HIS B 216 MET B 219 ASN B 220 CYS B 221
SITE 3 AC4 9 HOH B1260
SITE 1 AC5 16 HOH B1211 HOH B1249 ARG C 46 GLY C 49
SITE 2 AC5 16 LEU C 52 SER C 53 HIS C 101 THR C 102
SITE 3 AC5 16 GLY C 105 HIS C 108 LEU D 53 LEU D 57
SITE 4 AC5 16 HIS D 79 GLY D 83 VAL D 87 HOH D1309
SITE 1 AC6 6 ALA D 60 TYR D 61 PRO D 64 LEU D 72
SITE 2 AC6 6 TRP D 134 HOH D1326
SITE 1 AC7 7 LEU C 135 GLY C 139 ALA C 142 MET C 143
SITE 2 AC7 7 LYS D 99 ALA D 103 HOH D1324
SITE 1 AC8 6 TRP B 173 ILE B 218 HOH B1272 TRP C 35
SITE 2 AC8 6 ILE C 43 TYR D 91
CRYST1 70.238 83.557 293.896 90.00 90.00 90.00 P 21 21 21 4
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 0.014237 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011968 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003403 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
