REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.0 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) : 2.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00 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) (%) : 92.5 REMARK 3 NUMBER OF REFLECTIONS : 145617 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) : 0.228 REMARK 3 FREE R VALUE : 0.252 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.500 REMARK 3 FREE R VALUE TEST SET COUNT : 3677 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 50 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.52 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 82.80 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2508 REMARK 3 BIN R VALUE (WORKING SET) : 0.4100 REMARK 3 BIN FREE R VALUE : 0.4110 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 2.20 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 67 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.050 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 17235 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 508 REMARK 3 SOLVENT ATOMS : 326 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 50.30 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 71.95 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) : 0.008 REMARK 3 BOND ANGLES (DEGREES) : 1.30 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 : CNS BULK SOLVENT MODEL USED REMARK 3 KSOL : 0.25 REMARK 3 BSOL : 31.44 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 : PROTEIN.PARAM REMARK 3 PARAMETER FILE 2 : WATER.1.PARAM REMARK 3 PARAMETER FILE 3 : 070303PARHCSDX_IUB.+LIP_TRUN.BC1 REMARK 3 PARAMETER FILE 4 : NULL REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP REMARK 3 TOPOLOGY FILE 2 : WATER_MOD.1.TOP REMARK 3 TOPOLOGY FILE 3 : 070303TOPHCSDX_IUB.+LIP_TRUN.BC1 REMARK 3 TOPOLOGY FILE 4 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1P84 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-MAY-03. REMARK 100 THE RCSB ID CODE IS RCSB019126. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 04-DEC-00 REMARK 200 TEMPERATURE (KELVIN) : 277 REMARK 200 PH : 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 7 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID14-3 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.93 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 149103 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500 REMARK 200 RESOLUTION RANGE LOW (A) : 25.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 92.4 REMARK 200 DATA REDUNDANCY : 2.500 REMARK 200 R MERGE (I) : 0.06600 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) : 2.50 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.56 REMARK 200 COMPLETENESS FOR SHELL (%) : 84.6 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.37400 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.200 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: POSITIONAL AND B-FACTOR REMARK 200 REFINEMENT REMARK 200 SOFTWARE USED: NULL REMARK 200 STARTING MODEL: PDB ENTRY 1KB9, PROTEIN ONLY REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 74.16 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.76 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000, PH 7.5, VAPOR DIFFUSION, REMARK 280 SITTING DROP, 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 107.49900 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 82.54550 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 107.49900 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 82.54550 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 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 BIOLOGICAL ASSEMBLY IS A DIMER. REMARK 300 THERE IS A MONOMER IN THE ASYMMETRIC UNIT. REMARK 300 THE SECOND PART OF THE BIOLOGICAL ASSEMBLY IS GENERATED REMARK 300 BY SYMMETRY OPERATORS FOR SPACE GROUP: C 2 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: OCTADECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, 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 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: J, K 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 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 H 38 REMARK 475 GLY H 39 REMARK 475 ILE H 40 REMARK 475 PHE H 41 REMARK 475 HIS H 42 REMARK 475 ASN H 43 REMARK 475 ALA H 44 REMARK 475 VAL H 45 REMARK 475 PHE H 46 REMARK 475 ASN H 47 REMARK 475 SER H 48 REMARK 475 PHE H 49 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 O ASN C 173 O HOH C 809 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES 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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) 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 ATM2 ATM3 REMARK 500 GLY J 32 N - CA - C ANGL. DEV. = 16.4 DEGREES 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 ASN A 34 -54.33 -120.12 REMARK 500 PRO A 44 -81.42 -34.46 REMARK 500 ALA A 46 -32.25 -150.56 REMARK 500 HIS A 47 -36.45 79.45 REMARK 500 SER A 98 -169.67 -127.98 REMARK 500 ILE A 125 -54.00 -138.32 REMARK 500 LYS A 128 23.85 -78.77 REMARK 500 ALA A 129 -13.30 -152.93 REMARK 500 LEU A 132 43.12 -102.06 REMARK 500 ASN A 154 -33.79 -135.69 REMARK 500 GLN A 170 141.52 -36.98 REMARK 500 PRO A 173 -57.09 -28.99 REMARK 500 PHE A 201 40.36 -79.25 REMARK 500 ASN A 213 -24.75 -146.59 REMARK 500 ASN A 227 -137.98 -78.54 REMARK 500 LEU A 228 121.03 68.70 REMARK 500 LEU A 230 92.01 60.39 REMARK 500 GLN A 231 62.18 62.08 REMARK 500 LYS A 239 -147.48 -157.83 REMARK 500 LEU A 251 60.97 -103.94 REMARK 500 ASN A 271 52.26 74.24 REMARK 500 GLN A 310 72.42 51.82 REMARK 500 SER A 325 -169.51 -161.11 REMARK 500 LEU A 443 174.78 -58.09 REMARK 500 ALA B 21 -165.74 -166.21 REMARK 500 ARG B 22 102.91 167.67 REMARK 500 GLN B 57 -136.72 -76.79 REMARK 500 LYS B 79 144.60 -171.43 REMARK 500 ASP B 96 3.83 -66.55 REMARK 500 LYS B 111 56.84 -145.91 REMARK 500 ARG B 152 -1.91 -42.95 REMARK 500 LYS B 153 2.23 -175.68 REMARK 500 SER B 204 -159.83 -94.71 REMARK 500 PRO B 210 88.32 -59.64 REMARK 500 ALA B 211 101.95 -56.64 REMARK 500 THR B 261 53.32 -103.80 REMARK 500 PHE B 279 -162.68 -116.31 REMARK 500 LYS B 310 52.15 -111.70 REMARK 500 ASP B 313 -69.40 -156.66 REMARK 500 SER B 331 46.66 -104.02 REMARK 500 SER B 333 21.34 -166.49 REMARK 500 PRO B 335 -124.01 -57.04 REMARK 500 ALA B 342 -101.68 -145.50 REMARK 500 LYS B 344 21.47 -146.10 REMARK 500 LYS B 347 -144.97 -118.90 REMARK 500 LEU B 348 88.10 -167.40 REMARK 500 ASP B 366 -70.24 -52.06 REMARK 500 GLU B 367 1.07 -59.95 REMARK 500 ILE C 18 -60.48 -105.17 REMARK 500 PRO C 109 30.35 -92.34 REMARK 500 PHE C 156 -74.99 76.61 REMARK 500 SER C 172 -159.14 -142.76 REMARK 500 ASP C 217 83.86 -155.19 REMARK 500 SER C 223 -71.14 98.68 REMARK 500 SER C 247 52.81 -153.61 REMARK 500 PRO C 286 25.91 -66.83 REMARK 500 ILE C 365 -58.35 -124.81 REMARK 500 ASN C 384 55.34 -102.37 REMARK 500 LEU D 107 47.98 -144.41 REMARK 500 ARG D 147 148.16 -173.45 REMARK 500 ILE D 180 -39.48 -39.19 REMARK 500 GLU E 45 98.54 -64.16 REMARK 500 ASN E 46 86.49 -59.77 REMARK 500 ASP E 50 49.66 -88.17 REMARK 500 LEU E 89 37.35 -87.53 REMARK 500 PRO E 102 -162.18 -61.52 REMARK 500 LEU E 103 -96.32 -75.62 REMARK 500 PRO E 150 -17.46 -44.70 REMARK 500 HIS E 161 -82.84 -78.22 REMARK 500 ASP E 208 74.43 -155.96 REMARK 500 LEU F 117 -28.01 -149.63 REMARK 500 HIS F 119 22.35 -158.35 REMARK 500 ARG G 90 -34.92 -39.78 REMARK 500 ASP G 99 61.99 -69.54 REMARK 500 HIS H 15 49.99 -154.50 REMARK 500 LEU H 37 99.25 -44.95 REMARK 500 GLN H 38 -20.69 -166.34 REMARK 500 ILE H 40 47.61 -83.28 REMARK 500 HIS H 42 -44.76 73.75 REMARK 500 VAL H 45 -48.25 -145.69 REMARK 500 PHE H 49 -7.72 67.21 REMARK 500 ARG H 51 29.59 -75.58 REMARK 500 PHE H 52 -13.22 -146.44 REMARK 500 ASN H 93 -97.70 -51.48 REMARK 500 LYS I 12 85.59 45.93 REMARK 500 ARG I 13 8.60 48.42 REMARK 500 LEU J 11 122.83 -170.55 REMARK 500 SER J 15 -3.31 76.66 REMARK 500 TYR J 27 146.18 -179.88 REMARK 500 TYR J 33 -142.88 -82.17 REMARK 500 LYS J 65 -37.48 -32.19 REMARK 500 ASN J 77 66.10 60.21 REMARK 500 ASP J 90 23.61 -71.93 REMARK 500 ALA J 108 131.63 -173.65 REMARK 500 ASN K 31 3.60 -170.83 REMARK 500 PHE K 32 76.22 -65.24 REMARK 500 THR K 51 -25.36 58.05 REMARK 500 SER K 52 -2.42 -152.56 REMARK 500 ARG K 61 11.43 -66.83 REMARK 500 LEU K 73 84.80 -159.01 REMARK 500 LEU K 78 23.21 -69.02 REMARK 500 GLU K 81 38.44 -97.00 REMARK 500 ALA K 84 -179.33 -172.82 REMARK 500 HIS K 91 34.01 -152.93 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 D 94 0.07 SIDE_CHAIN 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 E 725 DISTANCE = 11.03 ANGSTROMS REMARK 525 HOH D 774 DISTANCE = 7.81 ANGSTROMS REMARK 525 HOH C 797 DISTANCE = 9.99 ANGSTROMS REMARK 525 HOH C 803 DISTANCE = 11.68 ANGSTROMS REMARK 525 HOH C 804 DISTANCE = 8.61 ANGSTROMS REMARK 525 HOH C 805 DISTANCE = 8.64 ANGSTROMS REMARK 525 HOH C 810 DISTANCE = 8.67 ANGSTROMS 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 3PE C 710 REMARK 610 3PE C 711 REMARK 610 3PH A 713 REMARK 610 3PH D 714 REMARK 610 PC1 D 715 REMARK 610 CDL D 731 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 C 701 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS C 183 NE2 REMARK 620 2 HIS C 82 NE2 174.3 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HEM C 702 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS C 96 NE2 REMARK 620 2 HIS C 197 NE2 177.4 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HEM D 703 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS D 105 NE2 REMARK 620 2 MET D 225 SD 177.0 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 FES E 704 FE2 REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS E 181 ND1 REMARK 620 2 HIS E 161 ND1 98.1 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 701 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 702 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 703 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES E 704 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DBT C 705 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UQ6 C 706 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3PE C 710 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3PE C 711 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3PH A 713 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3PH D 714 REMARK 800 SITE_IDENTIFIER: BC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PC1 D 715 REMARK 800 SITE_IDENTIFIER: BC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UMQ A 721 REMARK 800 SITE_IDENTIFIER: BC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CDL D 731 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1KB9 RELATED DB: PDB REMARK 900 TIGHTLY BOUND PHOSPHOLIPIDS IN STIGMATELLIN INHIBITED REMARK 900 CYTOCHROME BC1 COMPLEX, UBIQUINONE AT QI SITE, FV FRAGMENT REMARK 900 RELATED ID: 1EZV RELATED DB: PDB REMARK 900 STIGMATELLIN INHIBITED CYTOCHROME BC1 COMPLEX, UBIQUINONE REMARK 900 AT QI SITE, FV FRAGMENT REMARK 900 RELATED ID: 1KYO RELATED DB: PDB REMARK 900 CYTOCHROME C BOUND TO YEAST CYTOCHROME BC1 COMPLEX, FV REMARK 900 FRAGMENT