REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.30 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) : 2.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00 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) (%) : 84.7 REMARK 3 NUMBER OF REFLECTIONS : 168517 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING SET) : 0.222 REMARK 3 FREE R VALUE : 0.254 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 4240 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) : NULL REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : NULL REMARK 3 BIN FREE R VALUE : NULL REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL 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 : 17222 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 213 REMARK 3 SOLVENT ATOMS : 346 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 52.10 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) : NULL REMARK 3 ESD FROM SIGMAA (A) : NULL REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM C-V SIGMAA (A) : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.007 REMARK 3 BOND ANGLES (DEGREES) : 0.90 REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : NULL 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 1EZV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-JUN-00. REMARK 100 THE RCSB ID CODE IS RCSB011071. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-FEB-99; 19-MAY-98 REMARK 200 TEMPERATURE (KELVIN) : 277; 277 REMARK 200 PH : 8.0 REMARK 200 NUMBER OF CRYSTALS USED : 17 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y; Y REMARK 200 RADIATION SOURCE : ESRF; EMBL/DESY, HAMBURG REMARK 200 BEAMLINE : ID14-3; X11 REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; NULL REMARK 200 WAVELENGTH OR RANGE (A) : 0.931; 0.906 REMARK 200 MONOCHROMATOR : NULL; NULL REMARK 200 OPTICS : NULL; NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD; IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH; MAR SCANNER 345 REMARK 200 MM PLATE REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300 REMARK 200 RESOLUTION RANGE LOW (A) : 15.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 84.9 REMARK 200 DATA REDUNDANCY : 6.270 REMARK 200 R MERGE (I) : 0.06500 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 15.00 REMARK 200 COMPLETENESS FOR SHELL (%) : 73.9 REMARK 200 DATA REDUNDANCY IN SHELL : 2.20 REMARK 200 R MERGE FOR SHELL (I) : 0.39000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; NULL REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL REMARK 200 SOFTWARE USED: DM, ARP/WARP REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 73.85 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.70 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 5 % PEG 4000, 100 MM TRIS, 0.05 % REMARK 280 UNDECYL-MALTOSIDE, 1 MICROMOLAR STIGMATELLIN, PH 8.0, REMARK 280 MICROSEEDING, TEMPERATURE 277K 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 107.23500 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 81.96000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 107.23500 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 81.96000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 300 REMARK: THE YEAST MITOCHONDRIAL CYTOCHROME BC1 COMPLEX CONSIST REMARK 300 OF 9 SUBUNITS (COR1, QCR2, COB, CYT1, RIP1, QCR6, QCR7, QCR8, REMARK 300 QCR9). THE BIOLOGICAL FUNCTIONAL UNIT IS A HOMODIMER. THE REMARK 300 SMALLEST SUBUNIT QCR10, WHICH IS NOT REQUIRED FOR A FUNCTIONAL REMARK 300 ENZYME, WAS NOT PRESENT IN THE PROTEIN PREPARATIONS. 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: EICOSAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, H, F, G, I 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 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, H, F, G, I, REMARK 350 AND CHAINS: X, Y REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000 REMARK 475 REMARK 475 ZERO OCCUPANCY RESIDUES REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY. REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE) REMARK 475 M RES C SSEQI REMARK 475 GLN G 38 REMARK 475 GLY G 39 REMARK 475 ILE G 40 REMARK 475 PHE G 41 REMARK 475 HIS G 42 REMARK 475 ASN G 43 REMARK 475 ALA G 44 REMARK 475 VAL G 45 REMARK 475 PHE G 46 REMARK 475 ASN G 47 REMARK 475 SER G 48 REMARK 475 PHE G 49 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 ASN A 34 -95.63 -94.53 REMARK 500 PRO A 44 99.78 -49.00 REMARK 500 ALA A 45 -84.77 -119.73 REMARK 500 HIS A 46 -60.48 -161.76 REMARK 500 SER A 97 -164.60 -121.32 REMARK 500 ILE A 124 -52.30 -141.05 REMARK 500 LEU A 131 48.87 -92.00 REMARK 500 ASN A 153 -32.09 -132.80 REMARK 500 PHE A 200 40.49 -80.11 REMARK 500 ASN A 212 -7.66 -140.37 REMARK 500 ASN A 226 -128.73 -89.70 REMARK 500 LEU A 227 107.83 61.77 REMARK 500 LEU A 229 99.05 63.37 REMARK 500 PRO A 235 -155.62 -70.06 REMARK 500 LYS A 238 -143.90 -146.14 REMARK 500 SER A 246 -178.59 -173.39 REMARK 500 LEU A 250 58.53 -101.62 REMARK 500 GLN A 309 76.24 52.10 REMARK 500 SER A 356 13.50 -149.15 REMARK 500 ALA B 21 -175.16 -170.51 REMARK 500 ARG B 22 115.59 177.15 REMARK 500 PRO B 25 33.74 -85.61 REMARK 500 GLN B 57 -154.04 -69.99 REMARK 500 LYS B 79 135.83 175.73 REMARK 500 LYS B 111 58.28 -150.75 REMARK 500 THR B 150 -77.33 -66.92 REMARK 500 LYS B 153 20.49 -165.03 REMARK 500 GLU B 203 75.86 -100.38 REMARK 500 SER B 204 -159.99 -172.12 REMARK 500 LEU B 215 41.01 -105.36 REMARK 500 THR B 261 48.01 -108.07 REMARK 500 LEU B 267 30.55 -99.04 REMARK 500 PHE B 279 -160.44 -116.92 REMARK 500 ASP B 281 55.27 -147.14 REMARK 500 LYS B 310 54.59 -101.25 REMARK 500 ASP B 313 -72.44 178.87 REMARK 500 GLN B 328 41.10 -88.45 REMARK 500 ASN B 329 -49.79 -22.14 REMARK 500 SER B 333 35.45 90.13 REMARK 500 ILE B 336 131.03 -15.37 REMARK 500 GLU B 337 -70.21 -111.37 REMARK 500 LEU B 338 27.49 -73.34 REMARK 500 ALA B 342 -82.94 -146.24 REMARK 500 LYS B 347 -140.76 -89.22 REMARK 500 LEU B 348 100.16 -166.87 REMARK 500 ASP B 358 84.12 -69.41 REMARK 500 PHE C 156 -60.13 52.25 REMARK 500 VAL C 157 30.68 -95.44 REMARK 500 ASP C 217 85.03 -155.90 REMARK 500 SER C 223 -76.78 76.48 REMARK 500 SER C 247 54.37 -154.72 REMARK 500 PRO C 286 31.55 -75.59 REMARK 500 SER C 311 164.52 -48.90 REMARK 500 ILE C 365 -58.51 -129.78 REMARK 500 ASN C 384 54.15 -112.31 REMARK 500 LEU D 107 58.50 -145.82 REMARK 500 ASP D 139 -175.26 -67.63 REMARK 500 ASN D 169 41.06 -141.37 REMARK 500 GLU E 45 94.18 -55.84 REMARK 500 ASP E 50 53.39 -96.61 REMARK 500 PRO E 102 -175.46 -62.33 REMARK 500 HIS E 161 -82.35 -67.80 REMARK 500 GLU H 118 35.85 38.51 REMARK 500 HIS H 119 37.28 -160.97 REMARK 500 PRO G 4 -159.12 -57.69 REMARK 500 THR G 8 -168.63 -121.93 REMARK 500 HIS G 15 58.88 -149.17 REMARK 500 PHE G 41 150.84 93.94 REMARK 500 HIS G 42 -46.95 69.93 REMARK 500 VAL G 45 -22.84 -152.29 REMARK 500 ASN G 47 -74.36 -64.90 REMARK 500 PHE G 52 -3.32 169.33 REMARK 500 ASN G 93 -98.25 -58.50 REMARK 500 LYS I 12 71.10 51.87 REMARK 500 ARG I 13 -5.46 61.81 REMARK 500 ALA I 57 111.90 -161.03 REMARK 500 LEU X 11 109.41 -167.42 REMARK 500 TYR X 27 134.11 178.34 REMARK 500 TYR X 33 -129.59 -110.46 REMARK 500 ASN X 77 62.18 63.44 REMARK 500 SER X 85 71.41 37.96 REMARK 500 ASP X 90 30.85 -81.32 REMARK 500 ARG X 125 -152.92 -105.47 REMARK 500 SER Y 14 -158.69 -100.22 REMARK 500 ASN Y 30 -91.16 -68.48 REMARK 500 SER Y 52 -22.74 -174.40 REMARK 500 SER Y 63 -148.26 -110.72 REMARK 500 THR Y 69 -13.69 -145.98 REMARK 500 SER Y 76 -76.16 -87.56 REMARK 500 GLU Y 81 31.66 -94.34 REMARK 500 HIS Y 91 33.93 -146.99 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 LEU A 108 PRO A 109 -114.46 REMARK 500 VAL B 332 SER B 333 -121.77 REMARK 500 ILE G 40 PHE G 41 -149.99 REMARK 500 GLU Y 79 PRO Y 80 -51.46 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG A 249 0.10 SIDE_CHAIN REMARK 500 ARG A 446 0.13 SIDE_CHAIN REMARK 500 ARG A 448 0.09 SIDE_CHAIN REMARK 500 ARG B 69 0.09 SIDE_CHAIN REMARK 500 ARG C 79 0.17 SIDE_CHAIN REMARK 500 ARG C 218 0.09 SIDE_CHAIN REMARK 500 TYR C 279 0.08 SIDE_CHAIN REMARK 500 ARG C 314 0.13 SIDE_CHAIN REMARK 500 TYR D 94 0.11 SIDE_CHAIN REMARK 500 TYR D 97 0.06 SIDE_CHAIN REMARK 500 ARG D 109 0.13 SIDE_CHAIN REMARK 500 TYR D 154 0.06 SIDE_CHAIN REMARK 500 ARG E 192 0.09 SIDE_CHAIN REMARK 500 TYR H 98 0.09 SIDE_CHAIN REMARK 500 ARG F 71 0.11 SIDE_CHAIN REMARK 500 TYR X 60 0.07 SIDE_CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 HIS C 222 -12.65 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH F 137 DISTANCE = 7.04 ANGSTROMS REMARK 525 HOH E 232 DISTANCE = 5.30 ANGSTROMS REMARK 525 HOH E 233 DISTANCE = 5.31 ANGSTROMS REMARK 525 HOH C 541 DISTANCE = 7.31 ANGSTROMS REMARK 525 HOH A 492 DISTANCE = 7.78 ANGSTROMS REMARK 525 HOH C 546 DISTANCE = 5.99 ANGSTROMS 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 D 3 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 MET D 225 SD REMARK 620 2 HIS D 105 NE2 175.1 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HEM C 401 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS C 183 NE2 REMARK 620 2 HIS C 82 NE2 174.7 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HEM C 402 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS C 197 NE2 REMARK 620 2 HIS C 96 NE2 175.7 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 HEM C 401 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 402 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 3 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES E 4 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SMA C 505 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UQ6 C 506 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1QCR RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF BOVINE MITOCHONDRIAL CYTOCHROME BC1 REMARK 900 COMPLEX REMARK 900 RELATED ID: 3BCC RELATED DB: PDB REMARK 900 STIGMATELLIN AND ANTIMYCIN BOUND CYTOCHROME BC1 COMPLEX REMARK 900 FROM CHICKEN REMARK 900 RELATED ID: 1BCC RELATED DB: PDB REMARK 900 CYTOCHROME BC1 COMPLEX FROM CHICKEN REMARK 900 RELATED ID: 2BCC RELATED DB: PDB REMARK 900 STIGMATELLIN BOUND CYTOCHROME BC1 COMPLEX FROM CHICKEN REMARK 900 RELATED ID: 1BE3 RELATED DB: PDB REMARK 900 CYTOCHROME BC1 COMPLEX FROM BOVINE REMARK 900 RELATED ID: 1BGY RELATED DB: PDB REMARK 900 CYTOCHROME BC1 COMPLEX FROM BOVINE