REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.97 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) : 2.97 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.64 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) (%) : 93.7 REMARK 3 NUMBER OF REFLECTIONS : 175444 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) : 0.229 REMARK 3 FREE R VALUE : 0.268 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900 REMARK 3 FREE R VALUE TEST SET COUNT : 17442 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 : 8 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.97 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.10 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 83.90 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 17625 REMARK 3 BIN R VALUE (WORKING SET) : 0.3930 REMARK 3 BIN FREE R VALUE : 0.3930 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 8.50 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 1983 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.009 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 35264 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 383 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 43.70 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 59.66 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 13.53000 REMARK 3 B22 (A**2) : -6.64000 REMARK 3 B33 (A**2) : -6.89000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 4.85000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.38 REMARK 3 ESD FROM SIGMAA (A) : 0.97 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) : 0.44 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.84 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.009 REMARK 3 BOND ANGLES (DEGREES) : 1.40 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 : 0.23 REMARK 3 BSOL : 10.00 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 1KYO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-02. REMARK 100 THE RCSB ID CODE IS RCSB015475. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 26-FEB-01 REMARK 200 TEMPERATURE (KELVIN) : 277 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 : ID14-3 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.931 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 : 175444 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.940 REMARK 200 RESOLUTION RANGE LOW (A) : 29.640 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 92.8 REMARK 200 DATA REDUNDANCY : 3.200 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.10600 REMARK 200 FOR THE DATA SET : 6.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.97 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.08 REMARK 200 COMPLETENESS FOR SHELL (%) : 76.5 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.39500 REMARK 200 FOR SHELL : 2.300 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 ENTRY 1EZV REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 73.33 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.61 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000, 20 MM TRIS, 0.05 % UNDECYL REMARK 280 -MALTOPYRANOSIDE, PH 7.5, VAPOR DIFFUSION, HANGING DROP, REMARK 280 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 82.76550 REMARK 290 SMTRY3 2 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: 23-MERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, REMARK 350 AND CHAINS: J, K, L, M, N, O, P, Q, R, REMARK 350 AND CHAINS: S, T, U, V, 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 PRO D 307 REMARK 465 ARG D 308 REMARK 465 LYS D 309 REMARK 465 PRO G 2 REMARK 465 SER I 2 REMARK 465 PHE I 3 REMARK 465 ALA I 57 REMARK 465 ALA I 58 REMARK 465 PRO O 307 REMARK 465 ARG O 308 REMARK 465 LYS O 309 REMARK 465 PRO R 2 REMARK 465 SER T 2 REMARK 465 PHE T 3 REMARK 465 ALA T 57 REMARK 465 ALA T 58 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LYS D 306 CG CD CE NZ REMARK 470 LYS O 306 CG CD CE NZ 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 PHE B 340 N - CA - C ANGL. DEV. = -17.2 DEGREES REMARK 500 GLY J 32 N - CA - C ANGL. DEV. = 17.5 DEGREES REMARK 500 PHE M 340 N - CA - C ANGL. DEV. = -17.1 DEGREES REMARK 500 GLY U 32 N - CA - C ANGL. DEV. = 20.7 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 GLU A 28 -148.13 77.04 REMARK 500 VAL A 29 86.01 91.58 REMARK 500 ASN A 34 -74.50 -130.94 REMARK 500 ILE A 36 -144.02 -127.45 REMARK 500 PRO A 44 92.33 -41.18 REMARK 500 ALA A 45 -110.24 -110.65 REMARK 500 PRO A 63 -16.88 -47.36 REMARK 500 SER A 97 -159.20 -134.80 REMARK 500 PRO A 109 -39.14 -38.70 REMARK 500 SER A 111 24.56 -78.22 REMARK 500 ILE A 124 -62.27 -145.29 REMARK 500 GLN A 126 21.77 -75.23 REMARK 500 LEU A 130 -48.81 67.41 REMARK 500 SER A 134 -9.40 68.25 REMARK 500 ASN A 212 1.07 -154.19 REMARK 500 ASN A 226 -128.32 -63.22 REMARK 500 LEU A 227 -173.17 70.07 REMARK 500 SER A 228 -56.21 -147.49 REMARK 500 LEU A 229 91.02 67.62 REMARK 500 LYS A 238 -125.33 -161.92 REMARK 500 LYS A 257 -159.74 -113.70 REMARK 500 ASN A 270 67.40 64.20 REMARK 500 ALA A 289 -31.49 -37.47 REMARK 500 ASN A 313 149.87 177.82 REMARK 500 SER A 398 163.90 176.55 REMARK 500 ALA B 21 -156.22 -176.12 REMARK 500 ARG B 22 -76.47 -170.40 REMARK 500 ASP B 23 157.53 81.96 REMARK 500 PRO B 25 44.06 -82.60 REMARK 500 HIS B 36 75.21 -69.80 REMARK 500 ASP B 45 92.17 -45.95 REMARK 500 GLN B 57 -138.98 -87.39 REMARK 500 LYS B 79 138.76 -170.89 REMARK 500 ASP B 83 -167.99 -100.45 REMARK 500 LEU B 89 76.24 -107.46 REMARK 500 ALA B 91 85.83 -151.12 REMARK 500 LYS B 95 -63.33 34.06 REMARK 500 SER B 122 -62.32 -120.74 REMARK 500 THR B 150 -72.55 -77.20 REMARK 500 ARG B 152 -84.92 -15.05 REMARK 500 GLU B 203 -3.09 61.91 REMARK 500 LYS B 222 153.17 61.39 REMARK 500 PHE B 223 -62.68 -122.17 REMARK 500 PHE B 224 123.75 68.37 REMARK 500 LEU B 267 48.17 -109.76 REMARK 500 ASP B 281 13.12 -149.49 REMARK 500 ASP B 291 -113.82 -147.56 REMARK 500 GLN B 292 -70.52 -149.22 REMARK 500 ASP B 313 -82.56 -161.49 REMARK 500 LEU B 314 -15.01 68.61 REMARK 500 TYR B 320 -50.47 176.74 REMARK 500 GLU B 330 -12.36 -167.52 REMARK 500 SER B 331 46.46 -87.24 REMARK 500 VAL B 332 64.40 33.88 REMARK 500 SER B 333 132.22 -172.02 REMARK 500 SER B 334 63.29 -157.98 REMARK 500 PRO B 335 -127.92 -65.97 REMARK 500 ILE B 336 -123.22 13.50 REMARK 500 GLU B 337 -154.38 63.20 REMARK 500 LEU B 338 -59.42 53.75 REMARK 500 ASP B 341 18.04 80.35 REMARK 500 ALA B 342 -122.79 -124.98 REMARK 500 LYS B 344 48.61 -147.40 REMARK 500 LYS B 347 -152.02 -103.37 REMARK 500 TYR B 364 -169.66 -101.93 REMARK 500 GLU B 367 -157.43 -66.98 REMARK 500 ILE C 18 -63.21 -108.64 REMARK 500 ALA C 61 -77.41 -45.32 REMARK 500 ARG C 107 -146.60 -87.39 REMARK 500 SER C 108 -146.13 59.72 REMARK 500 ARG C 110 22.24 -79.16 REMARK 500 PRO C 155 -73.41 -21.28 REMARK 500 PHE C 156 -61.41 -102.90 REMARK 500 ASN C 215 -23.04 -36.55 REMARK 500 SER C 223 37.88 71.34 REMARK 500 TYR C 224 -72.34 -162.71 REMARK 500 SER C 247 48.40 -153.96 REMARK 500 ASN C 256 25.35 -76.58 REMARK 500 PRO C 286 44.14 -80.92 REMARK 500 VAL C 301 -8.66 -59.76 REMARK 500 VAL C 346 -50.69 -26.77 REMARK 500 ILE C 365 -58.40 -123.74 REMARK 500 ARG C 382 -1.06 -151.99 REMARK 500 LEU D 107 50.99 -145.76 REMARK 500 ASP D 139 -168.72 -76.49 REMARK 500 ALA D 226 -164.00 -77.62 REMARK 500 PRO D 241 109.90 -57.25 REMARK 500 HIS D 263 -85.62 -20.51 REMARK 500 PRO E 37 176.41 -52.79 REMARK 500 ASN E 47 -8.30 -154.21 REMARK 500 ALA E 84 127.57 -37.37 REMARK 500 PRO E 102 -171.91 -67.45 REMARK 500 LEU E 103 -89.63 -72.63 REMARK 500 GLN E 141 137.45 -176.39 REMARK 500 PRO E 150 -14.06 -43.93 REMARK 500 HIS E 161 -72.99 -82.32 REMARK 500 PHE E 173 20.15 -142.12 REMARK 500 ASP E 208 58.10 -154.19 REMARK 500 ASP E 210 33.94 -81.17 REMARK 500 ASN F 87 54.45 -96.89 REMARK 500 PRO F 112 91.20 -62.64 REMARK 500 LEU F 117 -23.27 -147.56 REMARK 500 HIS F 119 21.62 -163.87 REMARK 500 PRO G 19 -17.45 -46.81 REMARK 500 ARG G 90 -39.17 -34.28 REMARK 500 ALA G 96 -27.95 -34.43 REMARK 500 ASP G 99 55.52 -65.76 REMARK 500 THR H 8 -164.63 -121.21 REMARK 500 TRP H 13 123.47 -36.25 REMARK 500 HIS H 15 47.38 -149.31 REMARK 500 PRO H 36 87.01 -46.76 REMARK 500 LEU H 37 90.18 25.99 REMARK 500 GLN H 38 -141.47 -120.97 REMARK 500 PHE H 41 152.95 73.30 REMARK 500 HIS H 42 -52.60 74.05 REMARK 500 PHE H 52 16.87 83.36 REMARK 500 PHE H 56 -18.16 -46.03 REMARK 500 ARG H 86 -18.37 -49.53 REMARK 500 ASN H 93 -92.88 -61.31 REMARK 500 LYS I 12 72.89 49.95 REMARK 500 ARG I 13 19.35 45.97 REMARK 500 ALA J 9 99.77 -51.02 REMARK 500 TYR J 27 148.00 -177.24 REMARK 500 TYR J 33 -112.23 -99.87 REMARK 500 SER J 63 -72.91 -61.40 REMARK 500 LYS J 65 -25.38 -34.36 REMARK 500 ASN J 77 70.66 60.68 REMARK 500 SER J 85 77.25 44.64 REMARK 500 ALA J 108 117.55 173.35 REMARK 500 SER K 10 63.42 31.69 REMARK 500 ALA K 13 -165.71 -162.08 REMARK 500 SER K 14 -156.32 -92.43 REMARK 500 LEU K 15 45.91 -107.27 REMARK 500 GLN K 27 -160.99 -112.75 REMARK 500 ASN K 30 -97.33 59.92 REMARK 500 ASN K 31 -0.82 -141.09 REMARK 500 PHE K 32 75.35 -65.63 REMARK 500 THR K 51 -55.22 66.34 REMARK 500 LEU K 78 8.40 -61.35 REMARK 500 GLU K 81 14.46 -64.54 REMARK 500 HIS K 91 40.26 -168.41 REMARK 500 GLU L 28 -131.61 80.39 REMARK 500 VAL L 29 96.37 67.15 REMARK 500 ASN L 34 -83.82 -178.61 REMARK 500 PRO L 44 98.35 -36.43 REMARK 500 ALA L 45 -124.99 -131.69 REMARK 500 HIS L 46 -101.22 -95.36 REMARK 500 SER L 111 24.34 -73.00 REMARK 500 ILE L 124 -61.16 -146.94 REMARK 500 GLN L 126 30.98 -86.98 REMARK 500 LEU L 130 -62.06 64.33 REMARK 500 LEU L 131 0.45 -63.04 REMARK 500 SER L 133 171.92 -53.91 REMARK 500 SER L 134 -21.80 78.47 REMARK 500 ASN L 226 -125.76 -65.27 REMARK 500 LEU L 227 -179.25 67.52 REMARK 500 SER L 228 -62.42 -132.51 REMARK 500 LEU L 229 84.86 75.68 REMARK 500 LYS L 238 -131.20 -145.76 REMARK 500 ASN L 270 54.61 70.58 REMARK 500 GLN L 309 80.35 44.43 REMARK 500 SER L 324 -150.18 -147.12 REMARK 500 ILE L 395 -50.99 -130.19 REMARK 500 SER L 398 147.84 172.77 REMARK 500 ALA M 21 -172.83 -171.91 REMARK 500 ARG M 22 -61.33 -158.62 REMARK 500 ASP M 23 140.05 64.60 REMARK 500 HIS M 36 85.67 -59.45 REMARK 500 TYR M 41 56.41 -106.86 REMARK 500 ASP M 45 88.28 -58.74 REMARK 500 LEU M 89 65.32 -106.91 REMARK 500 ASP M 97 27.21 -71.45 REMARK 500 SER M 122 -54.57 -126.18 REMARK 500 PRO M 138 -15.77 -48.35 REMARK 500 THR M 150 -72.42 -79.14 REMARK 500 ARG M 152 -85.98 55.22 REMARK 500 ASN M 191 41.37 71.29 REMARK 500 GLU M 203 17.53 162.89 REMARK 500 LYS M 222 120.48 14.63 REMARK 500 PHE M 224 95.08 58.70 REMARK 500 ALA M 248 -34.56 -132.29 REMARK 500 THR M 261 40.06 -107.27 REMARK 500 LEU M 267 28.74 -151.57 REMARK 500 ASP M 313 -84.63 162.83 REMARK 500 LEU M 314 -2.78 76.30 REMARK 500 TYR M 320 -50.71 -129.53 REMARK 500 LEU M 323 -45.78 -139.89 REMARK 500 VAL M 332 36.19 28.01 REMARK 500 SER M 333 102.71 -162.02 REMARK 500 PRO M 335 -119.29 -74.60 REMARK 500 ILE M 336 -112.96 34.03 REMARK 500 GLU M 337 -153.92 50.73 REMARK 500 LEU M 338 -62.09 39.18 REMARK 500 PHE M 340 138.76 165.88 REMARK 500 ASP M 341 -22.92 82.53 REMARK 500 ALA M 342 -76.92 -101.53 REMARK 500 LYS M 344 56.82 -156.51 REMARK 500 LYS M 347 -127.39 -138.38 REMARK 500 LEU M 348 96.56 -174.87 REMARK 500 ASP M 358 80.50 -68.65 REMARK 500 GLU M 367 -105.67 -73.70 REMARK 500 ILE N 18 -55.15 -127.88 REMARK 500 ARG N 107 -156.38 -85.15 REMARK 500 SER N 108 -108.78 32.48 REMARK 500 PRO N 155 -73.73 -32.94 REMARK 500 SER N 207 -153.44 -90.08 REMARK 500 PRO N 220 151.23 -48.84 REMARK 500 SER N 223 68.51 66.63 REMARK 500 TYR N 224 -69.25 172.51 REMARK 500 SER N 247 48.60 -158.29 REMARK 500 PRO N 286 7.33 -68.71 REMARK 500 VAL N 346 -76.37 17.25 REMARK 500 ARG N 382 3.59 -152.81 REMARK 500 PRO O 81 -15.49 -46.90 REMARK 500 ALA O 102 -4.66 -49.76 REMARK 500 CYS O 104 -17.30 -141.12 REMARK 500 LEU O 107 44.56 -140.48 REMARK 500 GLU O 130 1.01 -67.82 REMARK 500 ASP O 139 -168.40 -60.30 REMARK 500 PRO O 203 152.95 -47.42 REMARK 500 MET O 233 5.30 -66.53 REMARK 500 THR O 240 131.38 -38.75 REMARK 500 GLU O 260 60.07 -119.60 REMARK 500 HIS O 263 -79.58 -12.10 REMARK 500 ASP P 50 32.24 -84.91 REMARK 500 LEU P 89 46.30 -78.32 REMARK 500 THR P 160 1.48 -69.06 REMARK 500 HIS P 161 -73.59 -83.57 REMARK 500 ASP P 208 70.03 -161.90 REMARK 500 ASN Q 87 46.99 -103.53 REMARK 500 GLN Q 111 155.54 -38.04 REMARK 500 PRO Q 112 106.76 -50.19 REMARK 500 LEU Q 117 -26.44 -157.12 REMARK 500 HIS Q 119 -11.27 -151.10 REMARK 500 LYS Q 120 118.76 -28.34 REMARK 500 LEU Q 142 -58.75 -29.75 REMARK 500 ARG R 90 -31.95 -39.32 REMARK 500 ASP R 99 60.57 -66.25 REMARK 500 MET S 10 112.69 -165.67 REMARK 500 HIS S 15 52.44 -162.41 REMARK 500 PRO S 36 65.71 -42.62 REMARK 500 LEU S 37 81.89 41.68 REMARK 500 GLN S 38 -108.32 -102.29 REMARK 500 PHE S 41 115.54 74.81 REMARK 500 HIS S 42 -37.18 91.28 REMARK 500 ASN S 43 -50.27 -122.07 REMARK 500 PHE S 49 -15.04 60.93 REMARK 500 ARG S 51 47.91 -98.01 REMARK 500 PHE S 52 24.29 172.69 REMARK 500 TYR S 81 47.73 -98.86 REMARK 500 ASN S 93 -82.42 -83.63 REMARK 500 LYS T 8 -7.51 -59.47 REMARK 500 LYS T 12 83.63 43.78 REMARK 500 ARG T 13 16.78 54.83 REMARK 500 SER U 15 -2.87 71.13 REMARK 500 TYR U 27 120.27 176.80 REMARK 500 TYR U 33 -145.54 -88.73 REMARK 500 LYS U 65 -18.47 -42.77 REMARK 500 SER U 69 100.16 -165.30 REMARK 500 SER U 85 74.32 39.64 REMARK 500 THR U 91 97.74 -62.00 REMARK 500 ALA U 108 123.59 -171.42 REMARK 500 ARG U 125 -24.18 -145.69 REMARK 500 HIS U 126 105.39 75.92 REMARK 500 SER V 10 64.06 27.38 REMARK 500 GLN V 27 -144.95 -116.86 REMARK 500 ASN V 30 -86.35 58.07 REMARK 500 ASN V 31 11.21 -161.92 REMARK 500 THR V 51 -42.17 70.33 REMARK 500 SER V 63 -145.10 -100.80 REMARK 500 SER V 65 -146.17 -128.34 REMARK 500 LEU V 73 77.19 -173.41 REMARK 500 LEU V 78 1.30 -62.59 REMARK 500 HIS V 91 39.49 -156.21 REMARK 500 PHE V 98 -159.18 -93.99 REMARK 500 THR V 102 98.78 -165.14 REMARK 500 CYS W 19 -45.18 -131.63 REMARK 500 GLN W 21 28.05 -72.79 REMARK 500 CYS W 22 -27.93 -167.34 REMARK 500 LYS W 32 -133.75 -117.74 REMARK 500 LEU W 37 41.11 -101.75 REMARK 500 ASN W 75 84.59 -162.61 REMARK 500 PRO W 81 -1.81 -51.83 REMARK 500 ALA W 106 -57.25 -124.29 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 N 224 0.08 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 D 503 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS D 105 NE2 REMARK 620 2 MET D 225 SD 175.4 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HEM O 523 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS O 105 NE2 REMARK 620 2 MET O 225 SD 173.1 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HEM C 501 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS C 183 NE2 REMARK 620 2 HIS C 82 NE2 176.3 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HEM N 521 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS N 82 NE2 REMARK 620 2 HIS N 183 NE2 178.6 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HEM C 502 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS C 96 NE2 REMARK 620 2 HIS C 197 NE2 173.6 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HEM N 522 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS N 197 NE2 REMARK 620 2 HIS N 96 NE2 179.1 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HEM W 526 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS W 23 NE2 REMARK 620 2 MET W 85 SD 176.0 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 FES E 504 FE2 REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS E 161 ND1 REMARK 620 2 HIS E 181 ND1 85.9 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 FES P 524 FE2 REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS P 181 ND1 REMARK 620 2 HIS P 161 ND1 104.7 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 501 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 502 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 503 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES E 504 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 HEM N 521 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM N 522 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM O 523 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES P 524 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SMA N 525 REMARK 800 SITE_IDENTIFIER: BC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM W 526 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1EZV RELATED DB: PDB REMARK 900 YEAST CYTOCHROME BC1 COMPLEX CRYSTALLIZED WITH AN ANTIBODY REMARK 900 FV FRAGMENT REMARK 900 RELATED ID: 1KB9 RELATED DB: PDB REMARK 900 PHOSPHOLIPID-BINDING IN THE YEAST CYTOCHROME BC1 COMPLEX REMARK 900 RYSTALLIZED WITH AN ANTIBODY FV FRAGMENT REMARK 999 REMARK 999 SEQUENCE REMARK 999 RESIDUE 270 (CHAINS C AND N) IS IN CONFLICT IN REMARK 999 SWISSPROT ENTRY P00163 AS BEING EITHER ASP OR VAL.