REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.851 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000000.000 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0010 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.1 REMARK 3 NUMBER OF REFLECTIONS : 57373 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) : 0.207 REMARK 3 FREE R VALUE : 0.261 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 2910 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 6 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.70 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 81.50 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 7839 REMARK 3 BIN R VALUE (WORKING SET) : 0.3570 REMARK 3 BIN FREE R VALUE : 0.3670 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 419 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.018 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 7926 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 266 REMARK 3 SOLVENT ATOMS : 52 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 44.20 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 59.70 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) : 0.36 REMARK 3 ESD FROM SIGMAA (A) : 0.55 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) : 0.42 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.54 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.012 REMARK 3 BOND ANGLES (DEGREES) : 1.60 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.40 REMARK 3 IMPROPER ANGLES (DEGREES) : 2.47 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 3.180 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 5.080 ; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 4.530 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 6.440 ; 2.500 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 : PARHCSDX.PRO REMARK 3 PARAMETER FILE 2 : PARAM19.SOL REMARK 3 PARAMETER FILE 3 : NULL REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO REMARK 3 TOPOLOGY FILE 2 : TOPH19.SOL REMARK 3 TOPOLOGY FILE 3 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1AR1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 31-JAN-97 REMARK 200 TEMPERATURE (KELVIN) : 277 REMARK 200 PH : 5.5 REMARK 200 NUMBER OF CRYSTALS USED : 10 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : BM14 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.078 REMARK 200 MONOCHROMATOR : SI(111) REMARK 200 OPTICS : COLLIMATING AND FOCUSSING REMARK 200 MIRROR REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : PRINCETON 2K REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57373 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 93.8 REMARK 200 DATA REDUNDANCY : 3.400 REMARK 200 R MERGE (I) : 0.06800 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 13.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80 REMARK 200 COMPLETENESS FOR SHELL (%) : 79.7 REMARK 200 DATA REDUNDANCY IN SHELL : 2.50 REMARK 200 R MERGE FOR SHELL (I) : 0.33200 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 4.000 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: NULL REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: X-PLOR 3.851 REMARK 200 STARTING MODEL: FOUR PROTEIN SUBUNITS CONTAINING CYTOCHROME C REMARK 200 OXIDASE FROM PARACOCCUS DENITRIFICANS (NATURE 376: 660-669) REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 72.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.80 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PH 5.5 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 46.75000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 78.35000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 75.50000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 78.35000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 46.75000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 75.50000 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 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 MET A 1 REMARK 465 ALA A 2 REMARK 465 ASP A 3 REMARK 465 ALA A 4 REMARK 465 ALA A 5 REMARK 465 VAL A 6 REMARK 465 HIS A 7 REMARK 465 GLY A 8 REMARK 465 HIS A 9 REMARK 465 GLY A 10 REMARK 465 ASP A 11 REMARK 465 HIS A 12 REMARK 465 HIS A 13 REMARK 465 ASP A 14 REMARK 465 THR A 15 REMARK 465 ARG A 16 REMARK 465 LEU A 546 REMARK 465 PRO A 547 REMARK 465 LYS A 548 REMARK 465 ARG A 549 REMARK 465 GLU A 550 REMARK 465 ASP A 551 REMARK 465 TRP A 552 REMARK 465 ASP A 553 REMARK 465 ARG A 554 REMARK 465 ALA A 555 REMARK 465 HIS A 556 REMARK 465 ALA A 557 REMARK 465 HIS A 558 REMARK 465 MET B -28 REMARK 465 MET B -27 REMARK 465 ALA B -26 REMARK 465 ILE B -25 REMARK 465 ALA B -24 REMARK 465 THR B -23 REMARK 465 LYS B -22 REMARK 465 ARG B -21 REMARK 465 ARG B -20 REMARK 465 GLY B -19 REMARK 465 VAL B -18 REMARK 465 ALA B -17 REMARK 465 ALA B -16 REMARK 465 VAL B -15 REMARK 465 MET B -14 REMARK 465 SER B -13 REMARK 465 LEU B -12 REMARK 465 GLY B -11 REMARK 465 VAL B -10 REMARK 465 ALA B -9 REMARK 465 THR B -8 REMARK 465 MET B -7 REMARK 465 THR B -6 REMARK 465 ALA B -5 REMARK 465 VAL B -4 REMARK 465 PRO B -3 REMARK 465 ALA B -2 REMARK 465 LEU B -1 REMARK 465 ALA B 0 REMARK 465 ASP B 253 REMARK 465 ALA B 254 REMARK 465 SER B 255 REMARK 465 ASP B 256 REMARK 465 TYR B 257 REMARK 465 LEU B 258 REMARK 465 PRO B 259 REMARK 465 ALA B 260 REMARK 465 SER B 261 REMARK 465 PRO B 262 REMARK 465 VAL B 263 REMARK 465 LYS B 264 REMARK 465 LEU B 265 REMARK 465 ALA B 266 REMARK 465 SER B 267 REMARK 465 ALA B 268 REMARK 465 GLU B 269 REMARK 465 ALA C 119 REMARK 465 TRP C 120 REMARK 465 ARG C 121 REMARK 465 HIS C 122 REMARK 465 PRO C 123 REMARK 465 GLN C 124 REMARK 465 PHE C 125 REMARK 465 GLY C 126 REMARK 465 GLY C 127 REMARK 465 ARG D 109 REMARK 465 GLU D 110 REMARK 465 GLN D 111 REMARK 465 LYS D 112 REMARK 465 LEU D 113 REMARK 465 ILE D 114 REMARK 465 SER D 115 REMARK 465 GLU D 116 REMARK 465 GLU D 117 REMARK 465 ASP D 118 REMARK 465 LEU D 119 REMARK 465 MET D 120 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 PHE A 18 107.52 -50.75 REMARK 500 TRP A 22 -79.61 -100.09 REMARK 500 TYR A 64 -51.66 -126.47 REMARK 500 ASN A 83 78.32 -109.75 REMARK 500 VAL A 102 -67.22 -140.91 REMARK 500 LEU A 166 73.82 47.19 REMARK 500 THR A 172 46.26 -87.98 REMARK 500 THR A 173 -11.25 -155.54 REMARK 500 ALA A 175 -83.10 -53.92 REMARK 500 MET A 207 23.15 -60.94 REMARK 500 PHE A 215 30.47 -87.61 REMARK 500 VAL A 322 27.20 -141.37 REMARK 500 ALA A 324 3.70 -65.25 REMARK 500 SER A 366 89.74 48.49 REMARK 500 ARG A 474 31.55 73.37 REMARK 500 TRP A 523 -93.10 -93.46 REMARK 500 ASP A 528 40.41 -102.63 REMARK 500 LEU A 530 -34.22 -39.30 REMARK 500 ILE B 10 -73.38 -100.61 REMARK 500 HIS B 73 155.95 171.27 REMARK 500 ASN B 74 47.61 -159.40 REMARK 500 THR B 75 -45.07 -17.24 REMARK 500 TRP B 81 22.98 -74.62 REMARK 500 GLN B 120 84.19 -51.26 REMARK 500 TRP B 121 34.88 87.32 REMARK 500 TYR B 127 79.47 -103.63 REMARK 500 TYR B 154 -83.32 -42.91 REMARK 500 LEU B 155 4.96 -64.58 REMARK 500 ASP B 178 -80.64 -101.55 REMARK 500 PHE B 204 167.44 178.03 REMARK 500 GLU B 218 116.88 -168.30 REMARK 500 LEU B 219 120.85 -39.42 REMARK 500 PRO B 228 -179.25 -68.30 REMARK 500 LEU C 18 145.69 -179.81 REMARK 500 SER C 25 142.30 -172.35 REMARK 500 LYS C 43 13.39 81.53 REMARK 500 TYR C 102 -102.10 71.81 REMARK 500 ILE D 2 -149.63 -82.34 REMARK 500 TYR D 30 -103.22 63.64 REMARK 500 LEU D 47 -61.06 -103.72 REMARK 500 ALA D 51 -41.12 71.96 REMARK 500 LYS D 52 15.09 -143.19 REMARK 500 SER D 77 87.77 40.60 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 TYR A 280 0.09 SIDE_CHAIN REMARK 500 TYR A 339 0.06 SIDE_CHAIN 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 CA A 561 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU A 56 O REMARK 620 2 GLU A 56 OE2 81.5 REMARK 620 3 HIS A 59 O 72.4 131.5 REMARK 620 4 GLY A 61 O 140.7 81.4 93.6 REMARK 620 5 GLN A 63 OE1 73.1 66.3 67.3 67.6 REMARK 620 6 ASP A 477 OD1 139.9 125.6 99.6 77.6 141.2 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HEA A 562 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 94 NE2 REMARK 620 2 HIS A 413 NE2 178.0 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CU A 559 CU REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 276 ND1 REMARK 620 2 HIS A 325 NE2 85.9 REMARK 620 3 HIS A 326 NE2 137.2 83.8 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MG A 560 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 403 NE2 REMARK 620 2 ASP A 404 OD1 77.7 REMARK 620 3 GLU B 218 OE1 132.0 134.6 REMARK 620 4 HOH A 574 O 65.9 137.8 68.1 REMARK 620 5 GLU B 218 OE2 136.1 90.0 44.6 101.4 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CU B 271 CU REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS B 181 ND1 REMARK 620 2 CYS B 216 SG 126.4 REMARK 620 3 MET B 227 SD 102.3 105.2 REMARK 620 4 CYS B 220 SG 112.5 108.8 96.8 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CU B 270 CU REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS B 224 ND1 REMARK 620 2 CYS B 220 SG 116.0 REMARK 620 3 CU B 271 CU 171.2 55.9 REMARK 620 4 GLU B 218 O 73.3 101.6 103.8 REMARK 620 5 CYS B 216 SG 132.4 111.2 55.4 92.6 REMARK 620 N 1 2 3 4 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: CUA REMARK 800 EVIDENCE_CODE: UNKNOWN REMARK 800 SITE_DESCRIPTION: CU A BINDING SITE. REMARK 800 SITE_IDENTIFIER: HMA REMARK 800 EVIDENCE_CODE: UNKNOWN REMARK 800 SITE_DESCRIPTION: AXIAL HEME A LIGANDS. REMARK 800 SITE_IDENTIFIER: HM3 REMARK 800 EVIDENCE_CODE: UNKNOWN REMARK 800 SITE_DESCRIPTION: AXIAL HEME A3 LIGAND. REMARK 800 SITE_IDENTIFIER: CUB REMARK 800 EVIDENCE_CODE: UNKNOWN REMARK 800 SITE_DESCRIPTION: CU B BINDING SITE. REMARK 800 SITE_IDENTIFIER: MM REMARK 800 EVIDENCE_CODE: UNKNOWN REMARK 800 SITE_DESCRIPTION: NON REDOX ACTIVE MN/MG BINDING SITE. REMARK 800 SITE_IDENTIFIER: CA REMARK 800 EVIDENCE_CODE: UNKNOWN REMARK 800 SITE_DESCRIPTION: NON REDOX ACTIVE CA BINDING SITE. REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU B 270 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU B 271 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 559 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 560 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 561 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEA A 562 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEA A 563 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LDA B 272 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LDA B 273 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LDA A 564 REMARK 800 SITE_IDENTIFIER: BC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LDA A 565 REMARK 800 SITE_IDENTIFIER: BC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LDA A 566 REMARK 800 SITE_IDENTIFIER: BC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LDA A 568 REMARK 800 SITE_IDENTIFIER: BC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LDA B 274 REMARK 800 SITE_IDENTIFIER: BC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LDA A 569