REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.1 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) : 19.97 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 5660991.530 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.9 REMARK 3 NUMBER OF REFLECTIONS : 289871 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) : 0.225 REMARK 3 FREE R VALUE : 0.256 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 14494 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.002 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) : 2.50 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.66 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.10 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 40490 REMARK 3 BIN R VALUE (WORKING SET) : 0.3380 REMARK 3 BIN FREE R VALUE : 0.3600 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 2131 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.008 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 35355 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 904 REMARK 3 SOLVENT ATOMS : 548 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 36.90 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 57.90 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 18.67000 REMARK 3 B22 (A**2) : -9.65000 REMARK 3 B33 (A**2) : -9.02000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 4.94000 REMARK 3 B23 (A**2) : 0.00000 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) : 0.39 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.50 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.007 REMARK 3 BOND ANGLES (DEGREES) : 1.30 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.10 REMARK 3 IMPROPER ANGLES (DEGREES) : 1.22 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) : 1.340 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.280 ; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 1.860 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.760 ; 2.500 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : FLAT MODEL REMARK 3 KSOL : 0.32 REMARK 3 BSOL : 31.90 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_MOD.PARAM REMARK 3 PARAMETER FILE 3 : PARHCSDX.SOZANNEI202.BC1 REMARK 3 PARAMETER FILE 4 : NULL REMARK 3 PARAMETER FILE 5 : NULL REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP REMARK 3 TOPOLOGY FILE 2 : WATER.TOP REMARK 3 TOPOLOGY FILE 3 : TOPHCSDX.SOZANNEI202.BC1 REMARK 3 TOPOLOGY FILE 4 : PROTEIN.LINK REMARK 3 TOPOLOGY FILE 5 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 3CXH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-MAY-08. REMARK 100 THE RCSB ID CODE IS RCSB047332. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 09-MAY-04 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID14-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9340 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 289871 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500 REMARK 200 RESOLUTION RANGE LOW (A) : 20.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 92.7 REMARK 200 DATA REDUNDANCY : 3.200 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.66000 REMARK 200 FOR THE DATA SET : 12.7000 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) : 2.70 REMARK 200 COMPLETENESS FOR SHELL (%) : 77.5 REMARK 200 DATA REDUNDANCY IN SHELL : 2.80 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.38000 REMARK 200 FOR SHELL : 2.800 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 ENTRIES 1KB9 AND 1YEA REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 72.35 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.45 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 1M SUCROSE, 10% DMSO, 20MM TRIS PH REMARK 280 7.5, 80MM NACL, 0.05 % UM, 1 M STIGMATELLIN, 5% PEG 4000, REMARK 280 MICROBATCH (PARAFFIN OIL), TEMPERATURE 277K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,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 81.48500 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4 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: OCTADECAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTADECAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 92880 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 150440 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -685.8 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, REMARK 350 AND CHAINS: L, M, N, O, P, Q, R, S, T 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1910 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 11090 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.5 KCAL/MOL 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 REMARK 350 BIOMOLECULE: 3 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1980 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 10830 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.2 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: U, V 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: 4 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: W 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 ARG D 308 REMARK 465 LYS D 309 REMARK 465 GLY F 2 REMARK 465 MET F 3 REMARK 465 LEU F 4 REMARK 465 GLU F 5 REMARK 465 LEU F 6 REMARK 465 VAL F 7 REMARK 465 GLY F 8 REMARK 465 GLU F 9 REMARK 465 TYR F 10 REMARK 465 TRP F 11 REMARK 465 GLU F 12 REMARK 465 GLN F 13 REMARK 465 LEU F 14 REMARK 465 LYS F 15 REMARK 465 ILE F 16 REMARK 465 THR F 17 REMARK 465 VAL F 18 REMARK 465 VAL F 19 REMARK 465 PRO F 20 REMARK 465 VAL F 21 REMARK 465 VAL F 22 REMARK 465 ALA F 23 REMARK 465 ALA F 24 REMARK 465 ALA F 25 REMARK 465 GLU F 26 REMARK 465 ASP F 27 REMARK 465 ASP F 28 REMARK 465 ASP F 29 REMARK 465 ASN F 30 REMARK 465 GLU F 31 REMARK 465 GLN F 32 REMARK 465 HIS F 33 REMARK 465 GLU F 34 REMARK 465 GLU F 35 REMARK 465 LYS F 36 REMARK 465 ALA F 37 REMARK 465 ALA F 38 REMARK 465 GLU F 39 REMARK 465 GLY F 40 REMARK 465 GLU F 41 REMARK 465 GLU F 42 REMARK 465 LYS F 43 REMARK 465 GLU F 44 REMARK 465 GLU F 45 REMARK 465 GLU F 46 REMARK 465 ASN F 47 REMARK 465 GLY F 48 REMARK 465 ASP F 49 REMARK 465 GLU F 50 REMARK 465 ASP F 51 REMARK 465 GLU F 52 REMARK 465 ASP F 53 REMARK 465 GLU F 54 REMARK 465 ASP F 55 REMARK 465 GLU F 56 REMARK 465 ASP F 57 REMARK 465 GLU F 58 REMARK 465 ASP F 59 REMARK 465 ASP F 60 REMARK 465 ASP F 61 REMARK 465 ASP F 62 REMARK 465 ASP F 63 REMARK 465 ASP F 64 REMARK 465 ASP F 65 REMARK 465 GLU F 66 REMARK 465 ASP F 67 REMARK 465 GLU F 68 REMARK 465 GLU F 69 REMARK 465 GLU F 70 REMARK 465 GLU F 71 REMARK 465 GLU F 72 REMARK 465 GLU F 73 REMARK 465 PRO G 2 REMARK 465 SER I 2 REMARK 465 PHE I 3 REMARK 465 GLY I 59 REMARK 465 ASP I 60 REMARK 465 GLY I 61 REMARK 465 ASP I 62 REMARK 465 ASP I 63 REMARK 465 ASP I 64 REMARK 465 ASP I 65 REMARK 465 GLU I 66 REMARK 465 ARG O 308 REMARK 465 LYS O 309 REMARK 465 GLY Q 2 REMARK 465 MET Q 3 REMARK 465 LEU Q 4 REMARK 465 GLU Q 5 REMARK 465 LEU Q 6 REMARK 465 VAL Q 7 REMARK 465 GLY Q 8 REMARK 465 GLU Q 9 REMARK 465 TYR Q 10 REMARK 465 TRP Q 11 REMARK 465 GLU Q 12 REMARK 465 GLN Q 13 REMARK 465 LEU Q 14 REMARK 465 LYS Q 15 REMARK 465 ILE Q 16 REMARK 465 THR Q 17 REMARK 465 VAL Q 18 REMARK 465 VAL Q 19 REMARK 465 PRO Q 20 REMARK 465 VAL Q 21 REMARK 465 VAL Q 22 REMARK 465 ALA Q 23 REMARK 465 ALA Q 24 REMARK 465 ALA Q 25 REMARK 465 GLU Q 26 REMARK 465 ASP Q 27 REMARK 465 ASP Q 28 REMARK 465 ASP Q 29 REMARK 465 ASN Q 30 REMARK 465 GLU Q 31 REMARK 465 GLN Q 32 REMARK 465 HIS Q 33 REMARK 465 GLU Q 34 REMARK 465 GLU Q 35 REMARK 465 LYS Q 36 REMARK 465 ALA Q 37 REMARK 465 ALA Q 38 REMARK 465 GLU Q 39 REMARK 465 GLY Q 40 REMARK 465 GLU Q 41 REMARK 465 GLU Q 42 REMARK 465 LYS Q 43 REMARK 465 GLU Q 44 REMARK 465 GLU Q 45 REMARK 465 GLU Q 46 REMARK 465 ASN Q 47 REMARK 465 GLY Q 48 REMARK 465 ASP Q 49 REMARK 465 GLU Q 50 REMARK 465 ASP Q 51 REMARK 465 GLU Q 52 REMARK 465 ASP Q 53 REMARK 465 GLU Q 54 REMARK 465 ASP Q 55 REMARK 465 GLU Q 56 REMARK 465 ASP Q 57 REMARK 465 GLU Q 58 REMARK 465 ASP Q 59 REMARK 465 ASP Q 60 REMARK 465 ASP Q 61 REMARK 465 ASP Q 62 REMARK 465 ASP Q 63 REMARK 465 ASP Q 64 REMARK 465 ASP Q 65 REMARK 465 GLU Q 66 REMARK 465 ASP Q 67 REMARK 465 GLU Q 68 REMARK 465 GLU Q 69 REMARK 465 GLU Q 70 REMARK 465 GLU Q 71 REMARK 465 GLU Q 72 REMARK 465 GLU Q 73 REMARK 465 PRO R 2 REMARK 465 SER T 2 REMARK 465 PHE T 3 REMARK 465 GLY T 59 REMARK 465 ASP T 60 REMARK 465 GLY T 61 REMARK 465 ASP T 62 REMARK 465 ASP T 63 REMARK 465 ASP T 64 REMARK 465 ASP T 65 REMARK 465 GLU T 66 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 N MET C 1 O HOH C 5260 2.18 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 ILE B 87 N - CA - C ANGL. DEV. = -16.6 DEGREES REMARK 500 LEU P 65 CA - CB - CG ANGL. DEV. = 14.7 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 18.01 -154.27 REMARK 500 ALA A 46 -62.28 -157.80 REMARK 500 HIS A 47 -18.65 86.23 REMARK 500 SER A 98 -163.73 -112.74 REMARK 500 ILE A 125 -35.92 -147.21 REMARK 500 GLN A 126 -80.49 -98.17 REMARK 500 GLN A 127 15.00 -67.22 REMARK 500 ASN A 227 -111.11 -131.21 REMARK 500 LEU A 228 -158.63 55.84 REMARK 500 SER A 229 -58.53 -156.34 REMARK 500 LEU A 230 85.22 55.36 REMARK 500 LYS A 239 -145.87 -155.06 REMARK 500 LEU A 251 65.30 -102.16 REMARK 500 ASN A 271 79.12 55.94 REMARK 500 GLN A 310 73.41 44.06 REMARK 500 SER A 357 23.75 -151.43 REMARK 500 GLU A 379 41.14 -100.23 REMARK 500 ILE A 396 -66.31 -94.77 REMARK 500 ALA B 21 135.07 -170.39 REMARK 500 PRO B 25 41.16 -82.18 REMARK 500 GLN B 57 -168.18 -79.71 REMARK 500 LYS B 79 147.57 -176.99 REMARK 500 LYS B 95 -53.62 -27.28 REMARK 500 LYS B 111 56.78 -142.83 REMARK 500 SER B 122 -51.75 -121.43 REMARK 500 ARG B 152 17.03 -38.86 REMARK 500 LYS B 153 -5.61 160.66 REMARK 500 LYS B 213 -121.46 -98.01 REMARK 500 SER B 214 99.24 172.32 REMARK 500 GLU B 266 23.60 -78.11 REMARK 500 LEU B 267 21.71 -146.01 REMARK 500 LYS B 310 43.56 -92.32 REMARK 500 ASP B 313 -76.76 -158.75 REMARK 500 VAL B 327 38.03 -75.38 REMARK 500 GLU B 330 -32.38 -148.56 REMARK 500 SER B 333 55.22 -167.43 REMARK 500 PRO B 335 -163.10 -48.37 REMARK 500 GLU B 337 -76.90 -88.59 REMARK 500 LEU B 338 4.33 -57.72 REMARK 500 ALA B 342 -144.78 -84.87 REMARK 500 VAL B 343 139.63 -18.95 REMARK 500 ILE C 18 -66.17 -107.88 REMARK 500 PHE C 156 -71.37 69.03 REMARK 500 ASP C 217 87.06 -155.79 REMARK 500 SER C 223 -70.69 92.96 REMARK 500 SER C 247 53.39 -149.95 REMARK 500 PRO C 286 26.44 -71.81 REMARK 500 VAL C 346 -71.89 -9.18 REMARK 500 ILE C 365 -54.10 -124.71 REMARK 500 ARG C 382 -39.96 -153.42 REMARK 500 VAL D 100 -37.77 -130.60 REMARK 500 CYS D 104 -30.50 -132.46 REMARK 500 SER D 119 -9.68 -143.09 REMARK 500 ASP D 139 -175.78 -66.60 REMARK 500 PRO D 210 115.24 -37.39 REMARK 500 PRO D 241 105.17 -53.71 REMARK 500 HIS D 263 -70.91 -28.24 REMARK 500 ASN E 46 47.07 -65.65 REMARK 500 ASN E 47 -82.89 -84.00 REMARK 500 ALA E 84 130.56 -36.79 REMARK 500 ALA E 92 -162.28 -78.72 REMARK 500 PRO E 102 -144.46 -61.99 REMARK 500 LEU E 103 -115.40 -76.77 REMARK 500 HIS E 161 -77.65 -82.19 REMARK 500 ILE E 187 4.72 -67.10 REMARK 500 ASP E 208 79.41 -157.08 REMARK 500 ASP F 116 76.50 -113.20 REMARK 500 GLU F 118 -25.93 70.50 REMARK 500 HIS F 119 49.23 -105.01 REMARK 500 THR H 8 -164.02 -117.79 REMARK 500 HIS H 15 57.41 -154.17 REMARK 500 PRO H 36 47.29 -46.05 REMARK 500 LEU H 37 18.68 38.89 REMARK 500 HIS H 42 -34.83 76.31 REMARK 500 ALA H 44 41.08 -148.99 REMARK 500 PHE H 49 -38.91 68.88 REMARK 500 PHE H 52 43.58 -93.82 REMARK 500 ASN H 93 -94.87 -61.58 REMARK 500 LYS I 12 63.72 36.51 REMARK 500 ARG I 13 -4.00 68.47 REMARK 500 ARG I 55 -80.81 -56.39 REMARK 500 ALA I 57 83.27 -67.65 REMARK 500 LEU J 11 111.30 -171.05 REMARK 500 TYR J 33 -131.18 -115.58 REMARK 500 ASN J 44 83.10 51.96 REMARK 500 LYS J 65 -38.43 -28.65 REMARK 500 SER J 85 68.74 37.34 REMARK 500 ALA J 108 114.31 -164.87 REMARK 500 HIS J 126 107.31 -58.90 REMARK 500 SER K 10 130.11 72.12 REMARK 500 LEU K 11 140.23 -170.99 REMARK 500 ASN K 30 -100.30 51.86 REMARK 500 THR K 51 -36.10 54.11 REMARK 500 SER K 63 -121.81 -89.86 REMARK 500 SER K 65 -145.54 -123.58 REMARK 500 PRO K 80 -59.23 -121.95 REMARK 500 GLU K 81 20.77 -75.84 REMARK 500 ASP K 82 -4.62 -58.71 REMARK 500 ILE K 83 108.55 -59.31 REMARK 500 HIS K 91 53.50 -162.63 REMARK 500 THR L 30 119.50 -160.26 REMARK 500 ASN L 34 25.83 -161.39 REMARK 500 HIS L 47 -13.39 82.85 REMARK 500 SER L 98 -163.18 -121.68 REMARK 500 ILE L 125 37.51 -144.48 REMARK 500 GLN L 126 -37.59 -174.76 REMARK 500 GLN L 127 46.77 -90.99 REMARK 500 GLU L 217 49.51 -71.79 REMARK 500 ASP L 218 -34.07 -156.24 REMARK 500 ASN L 227 -123.20 -158.93 REMARK 500 LEU L 228 -176.78 54.58 REMARK 500 SER L 229 19.04 -160.10 REMARK 500 GLN L 231 69.75 77.82 REMARK 500 LYS L 239 -154.23 -162.02 REMARK 500 LEU L 251 61.36 -110.30 REMARK 500 ASN L 271 9.44 88.25 REMARK 500 GLN L 310 71.17 50.79 REMARK 500 SER L 357 10.01 -143.53 REMARK 500 SER L 399 135.95 -176.99 REMARK 500 TRP L 427 108.69 -54.19 REMARK 500 ASP L 451 5.21 -66.04 REMARK 500 GLN M 57 -160.18 -79.03 REMARK 500 LYS M 95 -56.66 -21.97 REMARK 500 SER M 122 -60.92 -120.98 REMARK 500 LYS M 153 -12.83 179.09 REMARK 500 ASP M 313 -53.33 -172.52 REMARK 500 LEU M 314 -20.15 62.53 REMARK 500 SER M 315 32.94 76.40 REMARK 500 VAL M 327 28.61 -77.68 REMARK 500 GLN M 328 65.19 -105.86 REMARK 500 SER M 333 47.38 -162.59 REMARK 500 PRO M 335 -158.86 -55.10 REMARK 500 GLU M 337 -66.07 -96.95 REMARK 500 LEU M 338 -20.46 -36.62 REMARK 500 ALA M 342 -162.54 -172.96 REMARK 500 VAL M 343 116.23 34.59 REMARK 500 LYS M 347 -114.69 -98.93 REMARK 500 LEU M 348 101.79 155.74 REMARK 500 GLU M 367 30.28 -98.89 REMARK 500 PHE N 156 -76.03 76.32 REMARK 500 ASP N 217 84.81 -156.00 REMARK 500 SER N 223 -71.72 92.32 REMARK 500 SER N 247 56.17 -153.83 REMARK 500 PRO N 286 25.43 -69.95 REMARK 500 VAL N 346 -65.83 -21.97 REMARK 500 ILE N 365 -66.20 -124.03 REMARK 500 ARG N 382 -54.24 -148.50 REMARK 500 LEU O 107 55.38 -140.80 REMARK 500 ASP O 139 -178.41 -62.37 REMARK 500 ASN O 169 29.60 -144.12 REMARK 500 ASN P 46 77.70 -66.63 REMARK 500 ALA P 84 121.68 -37.82 REMARK 500 PRO P 102 -159.36 -60.05 REMARK 500 LEU P 103 -116.51 -67.61 REMARK 500 HIS P 161 -77.94 -79.54 REMARK 500 ILE P 187 -1.74 -57.42 REMARK 500 ASP P 208 74.22 -166.56 REMARK 500 GLU Q 118 21.00 40.67 REMARK 500 HIS Q 119 40.60 -147.46 REMARK 500 ASN R 91 0.17 -64.80 REMARK 500 HIS S 15 54.02 -157.22 REMARK 500 PRO S 36 100.71 -47.30 REMARK 500 LEU S 37 105.95 -7.38 REMARK 500 HIS S 42 -51.13 -145.91 REMARK 500 ARG S 91 -73.90 -70.59 REMARK 500 ASN S 93 -88.60 -75.63 REMARK 500 LYS T 12 84.54 42.56 REMARK 500 ARG T 13 -1.09 53.17 REMARK 500 ILE T 56 94.98 -66.36 REMARK 500 LEU U 11 116.81 -166.46 REMARK 500 SER U 15 -22.26 96.42 REMARK 500 TYR U 33 -157.64 -95.42 REMARK 500 PRO U 42 98.85 -63.30 REMARK 500 ASN U 44 90.85 52.40 REMARK 500 LYS U 45 107.90 -164.80 REMARK 500 SER U 85 71.49 39.89 REMARK 500 VAL V 9 105.78 -54.89 REMARK 500 SER V 10 96.69 71.31 REMARK 500 LEU V 15 99.49 -66.19 REMARK 500 ASN V 30 -77.02 -45.94 REMARK 500 ASN V 31 13.51 -158.29 REMARK 500 THR V 51 -52.75 59.67 REMARK 500 ARG V 61 25.28 -72.92 REMARK 500 THR V 69 -14.99 -145.82 REMARK 500 SER V 76 -36.40 -141.04 REMARK 500 HIS V 91 28.12 -160.61 REMARK 500 SER W 4 4.89 -151.34 REMARK 500 THR W 5 -161.79 -112.40 REMARK 500 CYS W 23 -41.47 -134.12 REMARK 500 LYS W 36 -134.27 -127.94 REMARK 500 ASN W 65 72.06 39.23 REMARK 500 ASN W 79 85.93 -160.78 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 C 279 0.07 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 HEM C4001 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS C 82 NE2 REMARK 620 2 HIS C 183 NE2 175.0 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HEM C4002 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS C 96 NE2 REMARK 620 2 HIS C 197 NE2 176.3 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HEM D4003 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS D 105 NE2 REMARK 620 2 MET D 225 SD 172.6 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 FES E4004 FE1 REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS E 159 SG REMARK 620 2 CYS E 178 SG 108.6 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 FES E4004 FE2 REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS E 161 ND1 REMARK 620 2 HIS E 181 ND1 94.9 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HEM N4021 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS N 82 NE2 REMARK 620 2 HIS N 183 NE2 175.4 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HEM N4022 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS N 96 NE2 REMARK 620 2 HIS N 197 NE2 174.1 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HEM O4023 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS O 105 NE2 REMARK 620 2 MET O 225 SD 176.9 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 FES P4024 FE1 REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS P 159 SG REMARK 620 2 CYS P 178 SG 117.3 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 FES P4024 FE2 REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS P 161 ND1 REMARK 620 2 HIS P 181 ND1 100.2 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HEM W4026 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS W 27 NE2 REMARK 620 2 MET W 89 SD 179.2 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 SUC O 4146 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 4001 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 4002 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 4003 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES E 4004 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SMA C 4005 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 8PE C 4010 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 9PE N 4011 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 6PH E 4013 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 7PH D 4014 REMARK 800 SITE_IDENTIFIER: BC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UMQ A 4021 REMARK 800 SITE_IDENTIFIER: BC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CN6 C 4031 REMARK 800 SITE_IDENTIFIER: BC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM N 4021 REMARK 800 SITE_IDENTIFIER: BC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM N 4022 REMARK 800 SITE_IDENTIFIER: BC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM O 4023 REMARK 800 SITE_IDENTIFIER: BC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES P 4024 REMARK 800 SITE_IDENTIFIER: BC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SMA N 4025 REMARK 800 SITE_IDENTIFIER: BC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 8PE N 4110 REMARK 800 SITE_IDENTIFIER: CC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 9PE C 4111 REMARK 800 SITE_IDENTIFIER: CC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 6PH L 4113 REMARK 800 SITE_IDENTIFIER: CC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 7PH O 4114 REMARK 800 SITE_IDENTIFIER: CC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UMQ L 4121 REMARK 800 SITE_IDENTIFIER: CC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CN6 N 4131 REMARK 800 SITE_IDENTIFIER: CC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM W 4026 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3CX5 RELATED DB: PDB REMARK 900 STRUCTURE OF COMPLEX III WITH BOUND CYTOCHROME C IN REDUCED REMARK 900 STATE AND DEFINITION OF A MINIMAL CORE INTERFACE FOR REMARK 900 ELECTRON TRANSFER. REMARK 900 RELATED ID: 1KYO RELATED DB: PDB REMARK 900 YEAST CYTOCHROME BC1 COMPLEX WITH BOUND SUBSTRATE REMARK 900 CYTOCHROME C REMARK 900 RELATED ID: 1KB9 RELATED DB: PDB REMARK 900 PHOSPHOLIPID-BINDING IN THE YEAST CYTOCHROME BC1 COMPLEX REMARK 900 CRYSTALLIZED WITH AN ANTIBODY FV FRAGMENT REMARK 900 RELATED ID: 1EZV RELATED DB: PDB REMARK 900 YEAST CYTOCHROME BC1 COMPLEX CRYSTALLIZED WITH AN ANTIBODY REMARK 900 FV FRAGMENT