LinkDB: 3NC3 3NC5 3NC6 3NC7
Original site: 3NC3 3NC5 3NC6 3NC7
HEADER OXIDOREDUCTASE 04-JUN-10 3NC3 TITLE CYP134A1 STRUCTURE WITH A CLOSED SUBSTRATE BINDING LOOP COMPND MOL_ID: 1; COMPND 2 MOLECULE: CYTOCHROME P450 CYPX; COMPND 3 CHAIN: A, B; COMPND 4 EC: 1.14.-.-; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS; SOURCE 3 ORGANISM_TAXID: 1423; SOURCE 4 STRAIN: 168; SOURCE 5 GENE: BSU35060, CYP134, CYPB, CYPX; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A(+) KEYWDS CYTOCHROME P450 OXIDASE, HAEM PROTEIN, OXIDOREDUCTASE EXPDTA X-RAY DIFFRACTION AUTHOR M.J.CRYLE,I.SCHLICHTING REVDAT 3 21-FEB-24 3NC3 1 REMARK SEQADV LINK REVDAT 2 22-SEP-10 3NC3 1 JRNL REVDAT 1 11-AUG-10 3NC3 0 JRNL AUTH M.J.CRYLE,S.G.BELL,I.SCHLICHTING JRNL TITL STRUCTURAL AND BIOCHEMICAL CHARACTERIZATION OF THE JRNL TITL 2 CYTOCHROME P450 CYPX (CYP134A1) FROM BACILLUS SUBTILIS: A JRNL TITL 3 CYCLO-L-LEUCYL-L-LEUCYL DIPEPTIDE OXIDASE. JRNL REF BIOCHEMISTRY V. 49 7282 2010 JRNL REFN ISSN 0006-2960 JRNL PMID 20690619 JRNL DOI 10.1021/BI100910Y REMARK 2 REMARK 2 RESOLUTION. 2.66 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.5.0070 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.66 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.74 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 21929 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 + TEST SET) : 0.221 REMARK 3 R VALUE (WORKING SET) : 0.219 REMARK 3 FREE R VALUE : 0.273 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1064 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.66 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.73 REMARK 3 REFLECTION IN BIN (WORKING SET) : 744 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0 REMARK 3 BIN R VALUE (WORKING SET) : 0.3400 REMARK 3 BIN FREE R VALUE SET COUNT : 744 REMARK 3 BIN FREE R VALUE : 0.0000 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6037 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 104 REMARK 3 SOLVENT ATOMS : 46 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 62.90 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 56.33 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.37000 REMARK 3 B22 (A**2) : 1.59000 REMARK 3 B33 (A**2) : -1.21000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 0.365 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.330 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 33.933 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.880 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6293 ; 0.010 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8556 ; 1.327 ; 2.010 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 765 ; 6.209 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 295 ;34.420 ;23.932 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1067 ;17.541 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 47 ;19.092 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 948 ; 0.086 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4785 ; 0.006 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3832 ; 0.325 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6197 ; 0.633 ; 2.000 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2461 ; 1.042 ; 3.000 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2356 ; 1.772 ; 4.500 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 3 REMARK 3 REMARK 3 NCS GROUP NUMBER : 1 REMARK 3 CHAIN NAMES : A B REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 A 6 A 61 4 REMARK 3 1 B 6 B 61 4 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 MEDIUM POSITIONAL 1 A (A): 476 ; 0.35 ; 0.50 REMARK 3 MEDIUM THERMAL 1 A (A**2): 476 ; 0.30 ; 2.00 REMARK 3 REMARK 3 NCS GROUP NUMBER : 2 REMARK 3 CHAIN NAMES : A B REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 A 87 A 403 4 REMARK 3 1 B 87 B 403 4 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 MEDIUM POSITIONAL 2 A (A): 2405 ; 0.44 ; 0.50 REMARK 3 MEDIUM THERMAL 2 A (A**2): 2405 ; 0.37 ; 2.00 REMARK 3 REMARK 3 NCS GROUP NUMBER : 3 REMARK 3 CHAIN NAMES : A B REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 A 406 A 406 4 REMARK 3 1 B 406 B 406 4 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 MEDIUM POSITIONAL 3 A (A): 43 ; 0.17 ; 0.50 REMARK 3 MEDIUM THERMAL 3 A (A**2): 43 ; 0.62 ; 2.00 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 8 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 6 A 104 REMARK 3 ORIGIN FOR THE GROUP (A): 19.3148 -16.1746 -9.2263 REMARK 3 T TENSOR REMARK 3 T11: 0.4424 T22: 0.6923 REMARK 3 T33: 0.3129 T12: -0.1019 REMARK 3 T13: 0.1382 T23: -0.0691 REMARK 3 L TENSOR REMARK 3 L11: 6.3897 L22: 3.6331 REMARK 3 L33: 3.3027 L12: 0.7160 REMARK 3 L13: -0.8730 L23: 0.2301 REMARK 3 S TENSOR REMARK 3 S11: 0.0143 S12: 0.4746 S13: -0.5560 REMARK 3 S21: 0.2493 S22: -0.4959 S23: 0.6583 REMARK 3 S31: 0.7851 S32: -0.7253 S33: 0.4816 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 105 A 167 REMARK 3 ORIGIN FOR THE GROUP (A): 42.1265 -11.5409 -22.4682 REMARK 3 T TENSOR REMARK 3 T11: 0.1700 T22: 0.2473 REMARK 3 T33: 0.0526 T12: 0.0742 REMARK 3 T13: 0.0589 T23: 0.0796 REMARK 3 L TENSOR REMARK 3 L11: 6.2629 L22: 4.2041 REMARK 3 L33: 4.6538 L12: 1.9893 REMARK 3 L13: 0.0862 L23: 2.8140 REMARK 3 S TENSOR REMARK 3 S11: 0.0811 S12: 0.5506 S13: 0.2251 REMARK 3 S21: -0.1538 S22: 0.1724 S23: -0.0252 REMARK 3 S31: -0.2046 S32: 0.1438 S33: -0.2534 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 168 A 291 REMARK 3 ORIGIN FOR THE GROUP (A): 33.3330 -17.4162 -16.3930 REMARK 3 T TENSOR REMARK 3 T11: 0.2413 T22: 0.2706 REMARK 3 T33: 0.1495 T12: 0.0344 REMARK 3 T13: 0.0711 T23: 0.0223 REMARK 3 L TENSOR REMARK 3 L11: 1.6881 L22: 1.7017 REMARK 3 L33: 4.1786 L12: -0.1720 REMARK 3 L13: -0.2006 L23: 1.4753 REMARK 3 S TENSOR REMARK 3 S11: 0.0533 S12: 0.1401 S13: -0.3333 REMARK 3 S21: 0.1848 S22: -0.0933 S23: 0.1023 REMARK 3 S31: 0.6626 S32: -0.2432 S33: 0.0400 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 292 A 403 REMARK 3 ORIGIN FOR THE GROUP (A): 31.2045 -8.1324 -5.9849 REMARK 3 T TENSOR REMARK 3 T11: 0.2253 T22: 0.2370 REMARK 3 T33: 0.0416 T12: -0.0135 REMARK 3 T13: 0.0842 T23: -0.0051 REMARK 3 L TENSOR REMARK 3 L11: 5.8394 L22: 3.6433 REMARK 3 L33: 4.8442 L12: -0.1048 REMARK 3 L13: -0.5848 L23: 1.6478 REMARK 3 S TENSOR REMARK 3 S11: 0.1745 S12: -0.1794 S13: 0.0007 REMARK 3 S21: 0.4691 S22: -0.2215 S23: 0.2933 REMARK 3 S31: 0.3533 S32: -0.4560 S33: 0.0470 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 6 B 104 REMARK 3 ORIGIN FOR THE GROUP (A): 45.2896 8.7419 18.7716 REMARK 3 T TENSOR REMARK 3 T11: 0.2705 T22: 0.6030 REMARK 3 T33: 0.2167 T12: -0.0427 REMARK 3 T13: 0.0440 T23: -0.1138 REMARK 3 L TENSOR REMARK 3 L11: 6.0631 L22: 2.2700 REMARK 3 L33: 4.2700 L12: -0.6435 REMARK 3 L13: -0.7340 L23: 0.6402 REMARK 3 S TENSOR REMARK 3 S11: 0.0956 S12: -0.5123 S13: 0.0008 REMARK 3 S21: 0.1571 S22: 0.0385 S23: -0.4638 REMARK 3 S31: -0.1354 S32: 0.6617 S33: -0.1340 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 105 B 167 REMARK 3 ORIGIN FOR THE GROUP (A): 21.7025 11.9158 32.5903 REMARK 3 T TENSOR REMARK 3 T11: 0.1941 T22: 0.2937 REMARK 3 T33: 0.1228 T12: 0.0090 REMARK 3 T13: -0.0177 T23: -0.0724 REMARK 3 L TENSOR REMARK 3 L11: 4.8091 L22: 2.4611 REMARK 3 L33: 5.0745 L12: -1.5169 REMARK 3 L13: 0.8983 L23: -2.0752 REMARK 3 S TENSOR REMARK 3 S11: -0.0073 S12: -0.3698 S13: 0.3384 REMARK 3 S21: 0.3187 S22: 0.2927 S23: 0.0505 REMARK 3 S31: -0.3427 S32: -0.1331 S33: -0.2854 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 168 B 330 REMARK 3 ORIGIN FOR THE GROUP (A): 34.0617 7.7646 22.9676 REMARK 3 T TENSOR REMARK 3 T11: 0.1858 T22: 0.2560 REMARK 3 T33: 0.1483 T12: -0.0256 REMARK 3 T13: 0.0006 T23: -0.0702 REMARK 3 L TENSOR REMARK 3 L11: 2.4888 L22: 1.4935 REMARK 3 L33: 4.0537 L12: 0.1171 REMARK 3 L13: -0.5781 L23: -0.2731 REMARK 3 S TENSOR REMARK 3 S11: 0.1364 S12: -0.0273 S13: -0.0733 REMARK 3 S21: -0.2748 S22: 0.0357 S23: -0.1589 REMARK 3 S31: 0.0905 S32: 0.3745 S33: -0.1721 REMARK 3 REMARK 3 TLS GROUP : 8 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 331 B 404 REMARK 3 ORIGIN FOR THE GROUP (A): 27.2559 16.1199 18.9893 REMARK 3 T TENSOR REMARK 3 T11: 0.2809 T22: 0.2017 REMARK 3 T33: 0.1022 T12: -0.0276 REMARK 3 T13: 0.0343 T23: 0.0026 REMARK 3 L TENSOR REMARK 3 L11: 6.4674 L22: 2.8446 REMARK 3 L33: 4.6547 L12: -0.6756 REMARK 3 L13: -2.1140 L23: 0.9779 REMARK 3 S TENSOR REMARK 3 S11: 0.3436 S12: -0.1459 S13: 0.6697 REMARK 3 S21: -0.4236 S22: 0.0254 S23: 0.0658 REMARK 3 S31: -0.6721 S32: 0.2764 S33: -0.3689 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.40 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 3NC3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUN-10. REMARK 100 THE DEPOSITION ID IS D_1000059642. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 11-DEC-09 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SLS REMARK 200 BEAMLINE : X10SA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9790 REMARK 200 MONOCHROMATOR : SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS, XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21929 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.660 REMARK 200 RESOLUTION RANGE LOW (A) : 47.730 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 91.3 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : 0.14000 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.66 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.73 REMARK 200 COMPLETENESS FOR SHELL (%) : 80.8 REMARK 200 DATA REDUNDANCY IN SHELL : 3.90 REMARK 200 R MERGE FOR SHELL (I) : 0.58000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD REMARK 200 SOFTWARE USED: SHARP REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 53.67 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS, 0.1 M MGCL2, 12% (W/V) REMARK 280 POLYETHYLENE GLYCOL-3350, PH 6.5, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 293K 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 31.90000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 71.95000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.70000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 71.95000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.90000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 52.70000 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 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: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A 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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: B 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 -35 REMARK 465 GLY A -34 REMARK 465 SER A -33 REMARK 465 SER A -32 REMARK 465 HIS A -31 REMARK 465 HIS A -30 REMARK 465 HIS A -29 REMARK 465 HIS A -28 REMARK 465 HIS A -27 REMARK 465 HIS A -26 REMARK 465 SER A -25 REMARK 465 SER A -24 REMARK 465 GLY A -23 REMARK 465 LEU A -22 REMARK 465 VAL A -21 REMARK 465 PRO A -20 REMARK 465 ARG A -19 REMARK 465 GLY A -18 REMARK 465 SER A -17 REMARK 465 HIS A -16 REMARK 465 MET A -15 REMARK 465 ALA A -14 REMARK 465 SER A -13 REMARK 465 MET A -12 REMARK 465 THR A -11 REMARK 465 GLY A -10 REMARK 465 GLY A -9 REMARK 465 GLN A -8 REMARK 465 GLN A -7 REMARK 465 MET A -6 REMARK 465 GLY A -5 REMARK 465 ARG A -4 REMARK 465 GLY A -3 REMARK 465 SER A -2 REMARK 465 GLU A -1 REMARK 465 PHE A 0 REMARK 465 MET A 1 REMARK 465 SER A 2 REMARK 465 GLN A 3 REMARK 465 SER A 4 REMARK 465 GLY A 74 REMARK 465 PRO A 75 REMARK 465 VAL A 76 REMARK 465 LEU A 77 REMARK 465 ALA A 78 REMARK 465 GLN A 79 REMARK 465 MET A 80 REMARK 465 HIS A 81 REMARK 465 GLY A 82 REMARK 465 LYS A 83 REMARK 465 GLU A 84 REMARK 465 HIS A 85 REMARK 465 SER A 86 REMARK 465 SER A 211 REMARK 465 GLU A 212 REMARK 465 TYR A 213 REMARK 465 GLU A 214 REMARK 465 GLY A 215 REMARK 465 MET A 216 REMARK 465 GLY A 404 REMARK 465 ALA A 405 REMARK 465 MET B -35 REMARK 465 GLY B -34 REMARK 465 SER B -33 REMARK 465 SER B -32 REMARK 465 HIS B -31 REMARK 465 HIS B -30 REMARK 465 HIS B -29 REMARK 465 HIS B -28 REMARK 465 HIS B -27 REMARK 465 HIS B -26 REMARK 465 SER B -25 REMARK 465 SER B -24 REMARK 465 GLY B -23 REMARK 465 LEU B -22 REMARK 465 VAL B -21 REMARK 465 PRO B -20 REMARK 465 ARG B -19 REMARK 465 GLY B -18 REMARK 465 SER B -17 REMARK 465 HIS B -16 REMARK 465 MET B -15 REMARK 465 ALA B -14 REMARK 465 SER B -13 REMARK 465 MET B -12 REMARK 465 THR B -11 REMARK 465 GLY B -10 REMARK 465 GLY B -9 REMARK 465 GLN B -8 REMARK 465 GLN B -7 REMARK 465 MET B -6 REMARK 465 GLY B -5 REMARK 465 ARG B -4 REMARK 465 GLY B -3 REMARK 465 SER B -2 REMARK 465 GLU B -1 REMARK 465 PHE B 0 REMARK 465 MET B 1 REMARK 465 SER B 2 REMARK 465 GLN B 3 REMARK 465 SER B 4 REMARK 465 VAL B 76 REMARK 465 LEU B 77 REMARK 465 ALA B 78 REMARK 465 GLN B 79 REMARK 465 MET B 80 REMARK 465 HIS B 81 REMARK 465 GLY B 82 REMARK 465 LYS B 83 REMARK 465 GLU B 84 REMARK 465 HIS B 85 REMARK 465 GLU B 212 REMARK 465 TYR B 213 REMARK 465 GLU B 214 REMARK 465 GLY B 215 REMARK 465 MET B 216 REMARK 465 ALA B 405 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 ILE A 5 CG1 CG2 CD1 REMARK 470 LYS A 6 CG CD CE NZ REMARK 470 LEU A 7 CG CD1 CD2 REMARK 470 ILE B 5 CG1 CG2 CD1 REMARK 470 LYS B 6 CG CD CE NZ REMARK 470 LEU B 7 CG CD1 CD2 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 18 85.88 -151.17 REMARK 500 GLU A 28 -38.20 71.29 REMARK 500 ILE A 38 -167.32 -114.62 REMARK 500 ASP A 39 53.91 -107.20 REMARK 500 ARG A 67 119.83 -32.61 REMARK 500 GLU A 121 -49.69 80.80 REMARK 500 PHE A 131 -61.94 -149.03 REMARK 500 THR A 235 -72.78 -97.84 REMARK 500 ASP A 301 -6.31 62.08 REMARK 500 LYS A 334 -35.12 -38.13 REMARK 500 ALA A 340 55.16 -95.19 REMARK 500 HIS A 351 37.79 -96.18 REMARK 500 CYS A 353 121.03 -38.88 REMARK 500 LEU B 7 57.11 -99.22 REMARK 500 ASN B 18 89.14 -151.16 REMARK 500 ASP B 30 72.90 -118.91 REMARK 500 ILE B 38 -163.24 -105.08 REMARK 500 LEU B 101 -65.69 -22.57 REMARK 500 PHE B 131 -61.97 -133.77 REMARK 500 ASN B 199 74.63 -117.07 REMARK 500 THR B 235 -68.09 -99.56 REMARK 500 GLU B 236 -70.50 -45.93 REMARK 500 ASN B 252 71.87 -116.76 REMARK 500 HIS B 351 38.91 -96.28 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 A 406 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 353 SG REMARK 620 2 HEM A 406 NA 100.2 REMARK 620 3 HEM A 406 NB 91.3 92.1 REMARK 620 4 HEM A 406 NC 86.0 173.5 85.8 REMARK 620 5 HEM A 406 ND 94.4 89.2 173.8 92.1 REMARK 620 6 HOH A 428 O 166.7 68.5 82.4 105.1 92.4 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HEM B 406 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS B 353 SG REMARK 620 2 HEM B 406 NA 106.3 REMARK 620 3 HEM B 406 NB 88.4 90.6 REMARK 620 4 HEM B 406 NC 90.0 163.5 87.6 REMARK 620 5 HEM B 406 ND 105.0 88.7 166.3 89.2 REMARK 620 6 HOH B 431 O 162.3 80.5 75.1 83.2 91.3 REMARK 620 N 1 2 3 4 5 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 406 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 407 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 408 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 409 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 410 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 411 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 406 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 407 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 408 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 409 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3NC7 RELATED DB: PDB REMARK 900 RELATED ID: 3NC5 RELATED DB: PDB REMARK 900 RELATED ID: 3NC6 RELATED DB: PDB DBREF 3NC3 A 1 405 UNP O34926 CYPX_BACSU 1 405 DBREF 3NC3 B 1 405 UNP O34926 CYPX_BACSU 1 405 SEQADV 3NC3 MET A -35 UNP O34926 EXPRESSION TAG SEQADV 3NC3 GLY A -34 UNP O34926 EXPRESSION TAG SEQADV 3NC3 SER A -33 UNP O34926 EXPRESSION TAG SEQADV 3NC3 SER A -32 UNP O34926 EXPRESSION TAG SEQADV 3NC3 HIS A -31 UNP O34926 EXPRESSION TAG SEQADV 3NC3 HIS A -30 UNP O34926 EXPRESSION TAG SEQADV 3NC3 HIS A -29 UNP O34926 EXPRESSION TAG SEQADV 3NC3 HIS A -28 UNP O34926 EXPRESSION TAG SEQADV 3NC3 HIS A -27 UNP O34926 EXPRESSION TAG SEQADV 3NC3 HIS A -26 UNP O34926 EXPRESSION TAG SEQADV 3NC3 SER A -25 UNP O34926 EXPRESSION TAG SEQADV 3NC3 SER A -24 UNP O34926 EXPRESSION TAG SEQADV 3NC3 GLY A -23 UNP O34926 EXPRESSION TAG SEQADV 3NC3 LEU A -22 UNP O34926 EXPRESSION TAG SEQADV 3NC3 VAL A -21 UNP O34926 EXPRESSION TAG SEQADV 3NC3 PRO A -20 UNP O34926 EXPRESSION TAG SEQADV 3NC3 ARG A -19 UNP O34926 EXPRESSION TAG SEQADV 3NC3 GLY A -18 UNP O34926 EXPRESSION TAG SEQADV 3NC3 SER A -17 UNP O34926 EXPRESSION TAG SEQADV 3NC3 HIS A -16 UNP O34926 EXPRESSION TAG SEQADV 3NC3 MET A -15 UNP O34926 EXPRESSION TAG SEQADV 3NC3 ALA A -14 UNP O34926 EXPRESSION TAG SEQADV 3NC3 SER A -13 UNP O34926 EXPRESSION TAG SEQADV 3NC3 MET A -12 UNP O34926 EXPRESSION TAG SEQADV 3NC3 THR A -11 UNP O34926 EXPRESSION TAG SEQADV 3NC3 GLY A -10 UNP O34926 EXPRESSION TAG SEQADV 3NC3 GLY A -9 UNP O34926 EXPRESSION TAG SEQADV 3NC3 GLN A -8 UNP O34926 EXPRESSION TAG SEQADV 3NC3 GLN A -7 UNP O34926 EXPRESSION TAG SEQADV 3NC3 MET A -6 UNP O34926 EXPRESSION TAG SEQADV 3NC3 GLY A -5 UNP O34926 EXPRESSION TAG SEQADV 3NC3 ARG A -4 UNP O34926 EXPRESSION TAG SEQADV 3NC3 GLY A -3 UNP O34926 EXPRESSION TAG SEQADV 3NC3 SER A -2 UNP O34926 EXPRESSION TAG SEQADV 3NC3 GLU A -1 UNP O34926 EXPRESSION TAG SEQADV 3NC3 PHE A 0 UNP O34926 EXPRESSION TAG SEQADV 3NC3 THR A 356 UNP O34926 ALA 356 ENGINEERED MUTATION SEQADV 3NC3 MET B -35 UNP O34926 EXPRESSION TAG SEQADV 3NC3 GLY B -34 UNP O34926 EXPRESSION TAG SEQADV 3NC3 SER B -33 UNP O34926 EXPRESSION TAG SEQADV 3NC3 SER B -32 UNP O34926 EXPRESSION TAG SEQADV 3NC3 HIS B -31 UNP O34926 EXPRESSION TAG SEQADV 3NC3 HIS B -30 UNP O34926 EXPRESSION TAG SEQADV 3NC3 HIS B -29 UNP O34926 EXPRESSION TAG SEQADV 3NC3 HIS B -28 UNP O34926 EXPRESSION TAG SEQADV 3NC3 HIS B -27 UNP O34926 EXPRESSION TAG SEQADV 3NC3 HIS B -26 UNP O34926 EXPRESSION TAG SEQADV 3NC3 SER B -25 UNP O34926 EXPRESSION TAG SEQADV 3NC3 SER B -24 UNP O34926 EXPRESSION TAG SEQADV 3NC3 GLY B -23 UNP O34926 EXPRESSION TAG SEQADV 3NC3 LEU B -22 UNP O34926 EXPRESSION TAG SEQADV 3NC3 VAL B -21 UNP O34926 EXPRESSION TAG SEQADV 3NC3 PRO B -20 UNP O34926 EXPRESSION TAG SEQADV 3NC3 ARG B -19 UNP O34926 EXPRESSION TAG SEQADV 3NC3 GLY B -18 UNP O34926 EXPRESSION TAG SEQADV 3NC3 SER B -17 UNP O34926 EXPRESSION TAG SEQADV 3NC3 HIS B -16 UNP O34926 EXPRESSION TAG SEQADV 3NC3 MET B -15 UNP O34926 EXPRESSION TAG SEQADV 3NC3 ALA B -14 UNP O34926 EXPRESSION TAG SEQADV 3NC3 SER B -13 UNP O34926 EXPRESSION TAG SEQADV 3NC3 MET B -12 UNP O34926 EXPRESSION TAG SEQADV 3NC3 THR B -11 UNP O34926 EXPRESSION TAG SEQADV 3NC3 GLY B -10 UNP O34926 EXPRESSION TAG SEQADV 3NC3 GLY B -9 UNP O34926 EXPRESSION TAG SEQADV 3NC3 GLN B -8 UNP O34926 EXPRESSION TAG SEQADV 3NC3 GLN B -7 UNP O34926 EXPRESSION TAG SEQADV 3NC3 MET B -6 UNP O34926 EXPRESSION TAG SEQADV 3NC3 GLY B -5 UNP O34926 EXPRESSION TAG SEQADV 3NC3 ARG B -4 UNP O34926 EXPRESSION TAG SEQADV 3NC3 GLY B -3 UNP O34926 EXPRESSION TAG SEQADV 3NC3 SER B -2 UNP O34926 EXPRESSION TAG SEQADV 3NC3 GLU B -1 UNP O34926 EXPRESSION TAG SEQADV 3NC3 PHE B 0 UNP O34926 EXPRESSION TAG SEQADV 3NC3 THR B 356 UNP O34926 ALA 356 ENGINEERED MUTATION SEQRES 1 A 441 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY SEQRES 2 A 441 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY SEQRES 3 A 441 GLY GLN GLN MET GLY ARG GLY SER GLU PHE MET SER GLN SEQRES 4 A 441 SER ILE LYS LEU PHE SER VAL LEU SER ASP GLN PHE GLN SEQRES 5 A 441 ASN ASN PRO TYR ALA TYR PHE SER GLN LEU ARG GLU GLU SEQRES 6 A 441 ASP PRO VAL HIS TYR GLU GLU SER ILE ASP SER TYR PHE SEQRES 7 A 441 ILE SER ARG TYR HIS ASP VAL ARG TYR ILE LEU GLN HIS SEQRES 8 A 441 PRO ASP ILE PHE THR THR LYS SER LEU VAL GLU ARG ALA SEQRES 9 A 441 GLU PRO VAL MET ARG GLY PRO VAL LEU ALA GLN MET HIS SEQRES 10 A 441 GLY LYS GLU HIS SER ALA LYS ARG ARG ILE VAL VAL ARG SEQRES 11 A 441 SER PHE ILE GLY ASP ALA LEU ASP HIS LEU SER PRO LEU SEQRES 12 A 441 ILE LYS GLN ASN ALA GLU ASN LEU LEU ALA PRO TYR LEU SEQRES 13 A 441 GLU ARG GLY LYS SER ASP LEU VAL ASN ASP PHE GLY LYS SEQRES 14 A 441 THR PHE ALA VAL CYS VAL THR MET ASP MET LEU GLY LEU SEQRES 15 A 441 ASP LYS ARG ASP HIS GLU LYS ILE SER GLU TRP HIS SER SEQRES 16 A 441 GLY VAL ALA ASP PHE ILE THR SER ILE SER GLN SER PRO SEQRES 17 A 441 GLU ALA ARG ALA HIS SER LEU TRP CYS SER GLU GLN LEU SEQRES 18 A 441 SER GLN TYR LEU MET PRO VAL ILE LYS GLU ARG ARG VAL SEQRES 19 A 441 ASN PRO GLY SER ASP LEU ILE SER ILE LEU CYS THR SER SEQRES 20 A 441 GLU TYR GLU GLY MET ALA LEU SER ASP LYS ASP ILE LEU SEQRES 21 A 441 ALA LEU ILE LEU ASN VAL LEU LEU ALA ALA THR GLU PRO SEQRES 22 A 441 ALA ASP LYS THR LEU ALA LEU MET ILE TYR HIS LEU LEU SEQRES 23 A 441 ASN ASN PRO GLU GLN MET ASN ASP VAL LEU ALA ASP ARG SEQRES 24 A 441 SER LEU VAL PRO ARG ALA ILE ALA GLU THR LEU ARG TYR SEQRES 25 A 441 LYS PRO PRO VAL GLN LEU ILE PRO ARG GLN LEU SER GLN SEQRES 26 A 441 ASP THR VAL VAL GLY GLY MET GLU ILE LYS LYS ASP THR SEQRES 27 A 441 ILE VAL PHE CYS MET ILE GLY ALA ALA ASN ARG ASP PRO SEQRES 28 A 441 GLU ALA PHE GLU GLN PRO ASP VAL PHE ASN ILE HIS ARG SEQRES 29 A 441 GLU ASP LEU GLY ILE LYS SER ALA PHE SER GLY ALA ALA SEQRES 30 A 441 ARG HIS LEU ALA PHE GLY SER GLY ILE HIS ASN CYS VAL SEQRES 31 A 441 GLY THR ALA PHE ALA LYS ASN GLU ILE GLU ILE VAL ALA SEQRES 32 A 441 ASN ILE VAL LEU ASP LYS MET ARG ASN ILE ARG LEU GLU SEQRES 33 A 441 GLU ASP PHE CYS TYR ALA GLU SER GLY LEU TYR THR ARG SEQRES 34 A 441 GLY PRO VAL SER LEU LEU VAL ALA PHE ASP GLY ALA SEQRES 1 B 441 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY SEQRES 2 B 441 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY SEQRES 3 B 441 GLY GLN GLN MET GLY ARG GLY SER GLU PHE MET SER GLN SEQRES 4 B 441 SER ILE LYS LEU PHE SER VAL LEU SER ASP GLN PHE GLN SEQRES 5 B 441 ASN ASN PRO TYR ALA TYR PHE SER GLN LEU ARG GLU GLU SEQRES 6 B 441 ASP PRO VAL HIS TYR GLU GLU SER ILE ASP SER TYR PHE SEQRES 7 B 441 ILE SER ARG TYR HIS ASP VAL ARG TYR ILE LEU GLN HIS SEQRES 8 B 441 PRO ASP ILE PHE THR THR LYS SER LEU VAL GLU ARG ALA SEQRES 9 B 441 GLU PRO VAL MET ARG GLY PRO VAL LEU ALA GLN MET HIS SEQRES 10 B 441 GLY LYS GLU HIS SER ALA LYS ARG ARG ILE VAL VAL ARG SEQRES 11 B 441 SER PHE ILE GLY ASP ALA LEU ASP HIS LEU SER PRO LEU SEQRES 12 B 441 ILE LYS GLN ASN ALA GLU ASN LEU LEU ALA PRO TYR LEU SEQRES 13 B 441 GLU ARG GLY LYS SER ASP LEU VAL ASN ASP PHE GLY LYS SEQRES 14 B 441 THR PHE ALA VAL CYS VAL THR MET ASP MET LEU GLY LEU SEQRES 15 B 441 ASP LYS ARG ASP HIS GLU LYS ILE SER GLU TRP HIS SER SEQRES 16 B 441 GLY VAL ALA ASP PHE ILE THR SER ILE SER GLN SER PRO SEQRES 17 B 441 GLU ALA ARG ALA HIS SER LEU TRP CYS SER GLU GLN LEU SEQRES 18 B 441 SER GLN TYR LEU MET PRO VAL ILE LYS GLU ARG ARG VAL SEQRES 19 B 441 ASN PRO GLY SER ASP LEU ILE SER ILE LEU CYS THR SER SEQRES 20 B 441 GLU TYR GLU GLY MET ALA LEU SER ASP LYS ASP ILE LEU SEQRES 21 B 441 ALA LEU ILE LEU ASN VAL LEU LEU ALA ALA THR GLU PRO SEQRES 22 B 441 ALA ASP LYS THR LEU ALA LEU MET ILE TYR HIS LEU LEU SEQRES 23 B 441 ASN ASN PRO GLU GLN MET ASN ASP VAL LEU ALA ASP ARG SEQRES 24 B 441 SER LEU VAL PRO ARG ALA ILE ALA GLU THR LEU ARG TYR SEQRES 25 B 441 LYS PRO PRO VAL GLN LEU ILE PRO ARG GLN LEU SER GLN SEQRES 26 B 441 ASP THR VAL VAL GLY GLY MET GLU ILE LYS LYS ASP THR SEQRES 27 B 441 ILE VAL PHE CYS MET ILE GLY ALA ALA ASN ARG ASP PRO SEQRES 28 B 441 GLU ALA PHE GLU GLN PRO ASP VAL PHE ASN ILE HIS ARG SEQRES 29 B 441 GLU ASP LEU GLY ILE LYS SER ALA PHE SER GLY ALA ALA SEQRES 30 B 441 ARG HIS LEU ALA PHE GLY SER GLY ILE HIS ASN CYS VAL SEQRES 31 B 441 GLY THR ALA PHE ALA LYS ASN GLU ILE GLU ILE VAL ALA SEQRES 32 B 441 ASN ILE VAL LEU ASP LYS MET ARG ASN ILE ARG LEU GLU SEQRES 33 B 441 GLU ASP PHE CYS TYR ALA GLU SER GLY LEU TYR THR ARG SEQRES 34 B 441 GLY PRO VAL SER LEU LEU VAL ALA PHE ASP GLY ALA HET HEM A 406 43 HET GOL A 407 6 HET MG A 408 1 HET MG A 409 1 HET MG A 410 1 HET MG A 411 1 HET HEM B 406 43 HET GOL B 407 6 HET MG B 408 1 HET MG B 409 1 HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETNAM GOL GLYCEROL HETNAM MG MAGNESIUM ION HETSYN HEM HEME HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 3 HEM 2(C34 H32 FE N4 O4) FORMUL 4 GOL 2(C3 H8 O3) FORMUL 5 MG 6(MG 2+) FORMUL 13 HOH *46(H2 O) HELIX 1 1 SER A 12 ASN A 18 1 7 HELIX 2 2 PRO A 19 ALA A 21 5 3 HELIX 3 3 TYR A 22 ASP A 30 1 9 HELIX 4 4 ARG A 45 HIS A 55 1 11 HELIX 5 5 LYS A 88 ASP A 99 1 12 HELIX 6 6 ASP A 99 ALA A 117 1 19 HELIX 7 7 PHE A 131 LEU A 144 1 14 HELIX 8 8 ASP A 147 ARG A 149 5 3 HELIX 9 9 ASP A 150 SER A 167 1 18 HELIX 10 10 SER A 171 ARG A 197 1 27 HELIX 11 11 ASP A 203 CYS A 209 1 7 HELIX 12 12 SER A 219 ASN A 251 1 33 HELIX 13 13 ASN A 252 ASP A 262 1 11 HELIX 14 14 LEU A 265 LYS A 277 1 13 HELIX 15 15 ILE A 308 ARG A 313 1 6 HELIX 16 16 GLY A 332 ALA A 336 5 5 HELIX 17 17 SER A 348 ASN A 352 5 5 HELIX 18 18 GLY A 355 MET A 374 1 20 HELIX 19 19 SER B 12 ASN B 18 1 7 HELIX 20 20 PRO B 19 ALA B 21 5 3 HELIX 21 21 TYR B 22 ASP B 30 1 9 HELIX 22 22 ARG B 45 HIS B 55 1 11 HELIX 23 23 SER B 63 ALA B 68 1 6 HELIX 24 24 GLU B 69 MET B 72 5 4 HELIX 25 25 VAL B 93 ALA B 117 1 25 HELIX 26 26 PRO B 118 LEU B 120 5 3 HELIX 27 27 PHE B 131 LEU B 144 1 14 HELIX 28 28 ASP B 147 ARG B 149 5 3 HELIX 29 29 ASP B 150 THR B 166 1 17 HELIX 30 30 SER B 171 ASN B 199 1 29 HELIX 31 31 ASP B 203 THR B 210 1 8 HELIX 32 32 SER B 219 ASN B 252 1 34 HELIX 33 33 ASN B 252 ASP B 262 1 11 HELIX 34 34 LEU B 265 LYS B 277 1 13 HELIX 35 35 ILE B 308 ARG B 313 1 6 HELIX 36 36 ARG B 328 ALA B 336 5 9 HELIX 37 37 SER B 348 ASN B 352 5 5 HELIX 38 38 GLY B 355 MET B 374 1 20 SHEET 1 A 5 VAL A 32 GLU A 35 0 SHEET 2 A 5 SER A 40 ILE A 43 -1 O PHE A 42 N HIS A 33 SHEET 3 A 5 ILE A 303 MET A 307 1 O PHE A 305 N ILE A 43 SHEET 4 A 5 LEU A 282 LEU A 287 -1 N ILE A 283 O CYS A 306 SHEET 5 A 5 PHE A 59 THR A 60 -1 N THR A 60 O GLN A 286 SHEET 1 B 3 LYS A 124 ASP A 126 0 SHEET 2 B 3 LEU A 399 ALA A 401 -1 O VAL A 400 N SER A 125 SHEET 3 B 3 ARG A 378 LEU A 379 -1 N ARG A 378 O ALA A 401 SHEET 1 C 2 THR A 291 VAL A 292 0 SHEET 2 C 2 GLU A 297 ILE A 298 -1 O ILE A 298 N THR A 291 SHEET 1 D 2 GLU A 387 SER A 388 0 SHEET 2 D 2 GLY A 394 PRO A 395 -1 O GLY A 394 N SER A 388 SHEET 1 E 5 VAL B 32 GLU B 35 0 SHEET 2 E 5 SER B 40 ILE B 43 -1 O PHE B 42 N HIS B 33 SHEET 3 E 5 ILE B 303 MET B 307 1 O PHE B 305 N ILE B 43 SHEET 4 E 5 LEU B 282 LEU B 287 -1 N ARG B 285 O VAL B 304 SHEET 5 E 5 PHE B 59 THR B 61 -1 N THR B 60 O GLN B 286 SHEET 1 F 3 LYS B 124 ASP B 126 0 SHEET 2 F 3 LEU B 399 ALA B 401 -1 O VAL B 400 N SER B 125 SHEET 3 F 3 ARG B 378 LEU B 379 -1 N ARG B 378 O ALA B 401 SHEET 1 G 2 THR B 291 VAL B 293 0 SHEET 2 G 2 MET B 296 ILE B 298 -1 O ILE B 298 N THR B 291 SHEET 1 H 2 GLU B 387 SER B 388 0 SHEET 2 H 2 GLY B 394 PRO B 395 -1 O GLY B 394 N SER B 388 LINK O PRO A 172 MG MG A 410 1555 1555 2.69 LINK SG CYS A 353 FE HEM A 406 1555 1555 2.35 LINK FE HEM A 406 O HOH A 428 1555 1555 2.52 LINK OG SER B 63 MG MG B 409 1555 1555 2.75 LINK SG CYS B 353 FE HEM B 406 1555 1555 2.26 LINK FE HEM B 406 O HOH B 431 1555 1555 2.12 CISPEP 1 ARG B 90 ILE B 91 0 21.35 SITE 1 AC1 21 LYS A 62 ILE A 97 MET A 143 ASN A 229 SITE 2 AC1 21 ALA A 233 ALA A 234 PRO A 237 THR A 241 SITE 3 AC1 21 ILE A 283 ARG A 285 ALA A 345 PHE A 346 SITE 4 AC1 21 HIS A 351 CYS A 353 VAL A 354 GLY A 355 SITE 5 AC1 21 PHE A 358 ALA A 359 ILE A 363 GOL A 407 SITE 6 AC1 21 HOH A 428 SITE 1 AC2 4 ASN A 229 TYR A 391 HEM A 406 HOH A 428 SITE 1 AC3 3 ASN A 252 GLU A 254 ARG B 342 SITE 1 AC4 1 LYS A 277 SITE 1 AC5 3 PRO A 172 ARG A 175 ASN B 114 SITE 1 AC6 3 HIS A 248 ASN A 251 ASN A 252 SITE 1 AC7 20 SER B 63 LEU B 64 MET B 143 ASN B 229 SITE 2 AC7 20 ALA B 233 ALA B 234 PRO B 237 THR B 241 SITE 3 AC7 20 ILE B 283 ARG B 285 ALA B 345 HIS B 351 SITE 4 AC7 20 CYS B 353 VAL B 354 GLY B 355 PHE B 358 SITE 5 AC7 20 ALA B 359 ILE B 363 GOL B 407 HOH B 431 SITE 1 AC8 8 LEU B 64 ALA B 233 VAL B 280 TYR B 391 SITE 2 AC8 8 THR B 392 HEM B 406 HOH B 431 HOH B 432 SITE 1 AC9 3 HIS B 248 ASN B 251 ASN B 252 SITE 1 BC1 3 SER B 63 VAL B 65 ASN B 229 CRYST1 63.800 105.400 143.900 90.00 90.00 90.00 P 21 21 21 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.015674 0.000000 0.000000 0.00000 SCALE2 0.000000 0.009488 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006949 0.00000 (ATOM LINES ARE NOT SHOWN.) END
HEADER OXIDOREDUCTASE 04-JUN-10 3NC5 TITLE CYP134A1 STRUCTURE WITH AN OPEN SUBSTRATE BINDING LOOP COMPND MOL_ID: 1; COMPND 2 MOLECULE: CYTOCHROME P450 CYPX; COMPND 3 CHAIN: A, B; COMPND 4 EC: 1.14.-.-; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS; SOURCE 3 ORGANISM_TAXID: 1423; SOURCE 4 STRAIN: 168; SOURCE 5 GENE: BSU35060, CYP134, CYPB, CYPX; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A(+) KEYWDS CYTOCHROME P450 OXIDASE, HAEM PROTEIN, OXIDOREDUCTASE EXPDTA X-RAY DIFFRACTION AUTHOR M.J.CRYLE,I.SCHLICHTING REVDAT 3 21-FEB-24 3NC5 1 REMARK SEQADV LINK REVDAT 2 22-SEP-10 3NC5 1 JRNL REVDAT 1 11-AUG-10 3NC5 0 JRNL AUTH M.J.CRYLE,S.G.BELL,I.SCHLICHTING JRNL TITL STRUCTURAL AND BIOCHEMICAL CHARACTERIZATION OF THE JRNL TITL 2 CYTOCHROME P450 CYPX (CYP134A1) FROM BACILLUS SUBTILIS: A JRNL TITL 3 CYCLO-L-LEUCYL-L-LEUCYL DIPEPTIDE OXIDASE. JRNL REF BIOCHEMISTRY V. 49 7282 2010 JRNL REFN ISSN 0006-2960 JRNL PMID 20690619 JRNL DOI 10.1021/BI100910Y REMARK 2 REMARK 2 RESOLUTION. 2.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.5.0070 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.62 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 21929 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 + TEST SET) : 0.235 REMARK 3 R VALUE (WORKING SET) : 0.231 REMARK 3 FREE R VALUE : 0.306 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1091 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.90 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1497 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0 REMARK 3 BIN R VALUE (WORKING SET) : 0.2910 REMARK 3 BIN FREE R VALUE SET COUNT : 78 REMARK 3 BIN FREE R VALUE : 0.4040 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6003 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 101 REMARK 3 SOLVENT ATOMS : 32 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 68.50 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 58.32 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.00000 REMARK 3 B22 (A**2) : 0.00000 REMARK 3 B33 (A**2) : 0.00000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 0.491 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.393 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 39.311 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.921 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.858 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6233 ; 0.009 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8468 ; 1.254 ; 2.012 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 751 ; 6.093 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 292 ;35.634 ;24.075 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1067 ;17.186 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 44 ;18.525 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 940 ; 0.087 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4722 ; 0.005 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3784 ; 0.276 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6123 ; 0.536 ; 2.000 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2449 ; 0.878 ; 3.000 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2345 ; 1.479 ; 4.500 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 3 REMARK 3 REMARK 3 NCS GROUP NUMBER : 1 REMARK 3 CHAIN NAMES : A B REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 A 6 A 61 5 REMARK 3 1 B 6 B 61 5 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 MEDIUM POSITIONAL 1 A (A): 224 ; 0.230 ; 0.500 REMARK 3 LOOSE POSITIONAL 1 A (A): 264 ; 0.380 ; 5.000 REMARK 3 MEDIUM THERMAL 1 A (A**2): 224 ; 0.260 ; 2.000 REMARK 3 LOOSE THERMAL 1 A (A**2): 264 ; 0.280 ;10.000 REMARK 3 REMARK 3 NCS GROUP NUMBER : 2 REMARK 3 CHAIN NAMES : A B REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 A 90 A 403 5 REMARK 3 1 B 90 B 403 5 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 MEDIUM POSITIONAL 2 A (A): 1240 ; 0.270 ; 0.500 REMARK 3 LOOSE POSITIONAL 2 A (A): 1173 ; 0.590 ; 5.000 REMARK 3 MEDIUM THERMAL 2 A (A**2): 1240 ; 1.110 ; 2.000 REMARK 3 LOOSE THERMAL 2 A (A**2): 1173 ; 1.370 ;10.000 REMARK 3 REMARK 3 NCS GROUP NUMBER : 3 REMARK 3 CHAIN NAMES : A B REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 A 1 A 406 4 REMARK 3 1 B 1 B 406 4 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 MEDIUM POSITIONAL 3 A (A): 43 ; 0.150 ; 0.500 REMARK 3 MEDIUM THERMAL 3 A (A**2): 43 ; 0.640 ; 2.000 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 10 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 6 A 10 REMARK 3 ORIGIN FOR THE GROUP (A): 7.1752 -3.3903 -11.1383 REMARK 3 T TENSOR REMARK 3 T11: 0.2235 T22: 0.8562 REMARK 3 T33: 0.7740 T12: -0.0031 REMARK 3 T13: 0.0097 T23: 0.0149 REMARK 3 L TENSOR REMARK 3 L11: 13.1961 L22: 8.0833 REMARK 3 L33: 14.6244 L12: 1.0953 REMARK 3 L13: -0.2745 L23: -6.5809 REMARK 3 S TENSOR REMARK 3 S11: -0.1037 S12: 0.4940 S13: 0.3235 REMARK 3 S21: -0.2217 S22: 0.0877 S23: 0.8036 REMARK 3 S31: 0.1879 S32: -0.8559 S33: 0.0160 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 11 A 109 REMARK 3 ORIGIN FOR THE GROUP (A): 21.8630 -17.2719 -9.3896 REMARK 3 T TENSOR REMARK 3 T11: 0.4131 T22: 0.7068 REMARK 3 T33: 0.2193 T12: -0.0101 REMARK 3 T13: 0.0521 T23: 0.0389 REMARK 3 L TENSOR REMARK 3 L11: 6.8692 L22: 2.2704 REMARK 3 L33: 2.7887 L12: 0.5141 REMARK 3 L13: -1.1922 L23: 1.0801 REMARK 3 S TENSOR REMARK 3 S11: -0.0196 S12: 0.5255 S13: -0.3886 REMARK 3 S21: 0.1120 S22: -0.1803 S23: 0.5515 REMARK 3 S31: 0.5547 S32: -0.3540 S33: 0.1999 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 110 A 154 REMARK 3 ORIGIN FOR THE GROUP (A): 45.2793 -9.8815 -21.9719 REMARK 3 T TENSOR REMARK 3 T11: 0.3034 T22: 0.4958 REMARK 3 T33: 0.2471 T12: 0.0707 REMARK 3 T13: 0.0923 T23: 0.1122 REMARK 3 L TENSOR REMARK 3 L11: 5.4453 L22: 13.0808 REMARK 3 L33: 5.4602 L12: -1.6873 REMARK 3 L13: 1.0851 L23: 3.2390 REMARK 3 S TENSOR REMARK 3 S11: 0.1097 S12: 0.4357 S13: 0.4981 REMARK 3 S21: -0.8590 S22: 0.1772 S23: -0.3272 REMARK 3 S31: -0.3874 S32: 0.1428 S33: -0.2869 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 155 A 290 REMARK 3 ORIGIN FOR THE GROUP (A): 33.3419 -17.7076 -17.0733 REMARK 3 T TENSOR REMARK 3 T11: 0.2861 T22: 0.5204 REMARK 3 T33: 0.1126 T12: 0.0455 REMARK 3 T13: 0.0548 T23: 0.1151 REMARK 3 L TENSOR REMARK 3 L11: 2.1509 L22: 2.1368 REMARK 3 L33: 4.6660 L12: -0.6223 REMARK 3 L13: -0.2802 L23: 2.3008 REMARK 3 S TENSOR REMARK 3 S11: 0.0519 S12: 0.1288 S13: -0.3489 REMARK 3 S21: 0.0263 S22: 0.0030 S23: 0.0604 REMARK 3 S31: 0.4359 S32: -0.0279 S33: -0.0549 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 291 A 403 REMARK 3 ORIGIN FOR THE GROUP (A): 30.4956 -8.6009 -5.6263 REMARK 3 T TENSOR REMARK 3 T11: 0.2287 T22: 0.5102 REMARK 3 T33: 0.0430 T12: 0.0720 REMARK 3 T13: 0.0909 T23: 0.0547 REMARK 3 L TENSOR REMARK 3 L11: 5.2634 L22: 4.2474 REMARK 3 L33: 4.9849 L12: -0.1292 REMARK 3 L13: -0.8062 L23: 1.2450 REMARK 3 S TENSOR REMARK 3 S11: 0.1654 S12: -0.0282 S13: 0.0656 REMARK 3 S21: 0.3524 S22: -0.0966 S23: 0.1701 REMARK 3 S31: 0.2217 S32: -0.2690 S33: -0.0688 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 6 B 10 REMARK 3 ORIGIN FOR THE GROUP (A): 57.1249 19.9255 23.0175 REMARK 3 T TENSOR REMARK 3 T11: 0.4053 T22: 1.1640 REMARK 3 T33: 0.9196 T12: -0.0582 REMARK 3 T13: 0.0208 T23: -0.0419 REMARK 3 L TENSOR REMARK 3 L11: 20.3185 L22: 9.7697 REMARK 3 L33: 26.2359 L12: 2.0822 REMARK 3 L13: -18.7562 L23: 2.1866 REMARK 3 S TENSOR REMARK 3 S11: 0.2413 S12: -0.6789 S13: 0.0660 REMARK 3 S21: 0.0118 S22: -0.6054 S23: -0.4009 REMARK 3 S31: 0.7227 S32: 0.6461 S33: 0.3641 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 11 B 116 REMARK 3 ORIGIN FOR THE GROUP (A): 40.1292 7.8758 20.5786 REMARK 3 T TENSOR REMARK 3 T11: 0.3675 T22: 0.7835 REMARK 3 T33: 0.2839 T12: -0.0201 REMARK 3 T13: -0.0032 T23: -0.0746 REMARK 3 L TENSOR REMARK 3 L11: 6.6336 L22: 1.4109 REMARK 3 L33: 3.3177 L12: -1.3063 REMARK 3 L13: -3.1048 L23: 0.7440 REMARK 3 S TENSOR REMARK 3 S11: 0.0186 S12: -0.6061 S13: 0.0958 REMARK 3 S21: 0.0472 S22: 0.2257 S23: -0.4916 REMARK 3 S31: 0.0551 S32: 0.7830 S33: -0.2443 REMARK 3 REMARK 3 TLS GROUP : 8 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 117 B 186 REMARK 3 ORIGIN FOR THE GROUP (A): 27.4269 10.8335 36.9149 REMARK 3 T TENSOR REMARK 3 T11: 0.3416 T22: 0.6437 REMARK 3 T33: 0.1182 T12: 0.0414 REMARK 3 T13: -0.0450 T23: -0.1519 REMARK 3 L TENSOR REMARK 3 L11: 5.3440 L22: 1.6495 REMARK 3 L33: 4.5610 L12: 1.5197 REMARK 3 L13: 2.4961 L23: -1.2977 REMARK 3 S TENSOR REMARK 3 S11: 0.1049 S12: -0.0944 S13: 0.2493 REMARK 3 S21: 0.3712 S22: -0.0277 S23: 0.1293 REMARK 3 S31: -0.4279 S32: 0.0978 S33: -0.0772 REMARK 3 REMARK 3 TLS GROUP : 9 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 187 B 336 REMARK 3 ORIGIN FOR THE GROUP (A): 33.3587 7.9204 19.9016 REMARK 3 T TENSOR REMARK 3 T11: 0.3124 T22: 0.5259 REMARK 3 T33: 0.2271 T12: 0.0044 REMARK 3 T13: 0.0246 T23: -0.1632 REMARK 3 L TENSOR REMARK 3 L11: 3.7741 L22: 1.3856 REMARK 3 L33: 4.7194 L12: 0.5342 REMARK 3 L13: -1.1543 L23: -0.1515 REMARK 3 S TENSOR REMARK 3 S11: 0.1388 S12: 0.0970 S13: -0.1013 REMARK 3 S21: -0.3893 S22: 0.0463 S23: -0.3416 REMARK 3 S31: -0.0057 S32: 0.4499 S33: -0.1851 REMARK 3 REMARK 3 TLS GROUP : 10 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 337 B 403 REMARK 3 ORIGIN FOR THE GROUP (A): 27.1740 17.0449 20.4390 REMARK 3 T TENSOR REMARK 3 T11: 0.4008 T22: 0.5129 REMARK 3 T33: 0.1683 T12: -0.0408 REMARK 3 T13: 0.0486 T23: -0.0158 REMARK 3 L TENSOR REMARK 3 L11: 5.3431 L22: 4.1780 REMARK 3 L33: 3.5034 L12: -0.5033 REMARK 3 L13: -0.6334 L23: 2.0682 REMARK 3 S TENSOR REMARK 3 S11: 0.3239 S12: -0.3954 S13: 0.7049 REMARK 3 S21: -0.3627 S22: 0.1148 S23: -0.1271 REMARK 3 S31: -0.7487 S32: 0.2369 S33: -0.4387 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.40 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 3NC5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUN-10. REMARK 100 THE DEPOSITION ID IS D_1000059644. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 30-APR-09 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SLS REMARK 200 BEAMLINE : X10SA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000 REMARK 200 MONOCHROMATOR : SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS, XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21929 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900 REMARK 200 RESOLUTION RANGE LOW (A) : 40.620 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 95.8 REMARK 200 DATA REDUNDANCY : 3.900 REMARK 200 R MERGE (I) : 0.12000 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.98 REMARK 200 COMPLETENESS FOR SHELL (%) : 90.3 REMARK 200 DATA REDUNDANCY IN SHELL : 4.00 REMARK 200 R MERGE FOR SHELL (I) : 0.34000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.100 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD REMARK 200 SOFTWARE USED: SHARP REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 53.67 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS, 0.1 M MGCL2, 12% (W/V) REMARK 280 POLYETHYLENE GLYCOL-3350, PH 6.5, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 293K 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 31.90000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 71.95000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.70000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 71.95000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.90000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 52.70000 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 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: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A 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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: B 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 -35 REMARK 465 GLY A -34 REMARK 465 SER A -33 REMARK 465 SER A -32 REMARK 465 HIS A -31 REMARK 465 HIS A -30 REMARK 465 HIS A -29 REMARK 465 HIS A -28 REMARK 465 HIS A -27 REMARK 465 HIS A -26 REMARK 465 SER A -25 REMARK 465 SER A -24 REMARK 465 GLY A -23 REMARK 465 LEU A -22 REMARK 465 VAL A -21 REMARK 465 PRO A -20 REMARK 465 ARG A -19 REMARK 465 GLY A -18 REMARK 465 SER A -17 REMARK 465 HIS A -16 REMARK 465 MET A -15 REMARK 465 ALA A -14 REMARK 465 SER A -13 REMARK 465 MET A -12 REMARK 465 THR A -11 REMARK 465 GLY A -10 REMARK 465 GLY A -9 REMARK 465 GLN A -8 REMARK 465 GLN A -7 REMARK 465 MET A -6 REMARK 465 GLY A -5 REMARK 465 ARG A -4 REMARK 465 GLY A -3 REMARK 465 SER A -2 REMARK 465 GLU A -1 REMARK 465 PHE A 0 REMARK 465 MET A 1 REMARK 465 SER A 2 REMARK 465 GLN A 3 REMARK 465 SER A 4 REMARK 465 ILE A 5 REMARK 465 GLY A 74 REMARK 465 PRO A 75 REMARK 465 VAL A 76 REMARK 465 LEU A 77 REMARK 465 ALA A 78 REMARK 465 GLN A 79 REMARK 465 MET A 80 REMARK 465 HIS A 81 REMARK 465 GLY A 82 REMARK 465 LYS A 83 REMARK 465 GLU A 84 REMARK 465 HIS A 85 REMARK 465 GLU A 214 REMARK 465 GLY A 215 REMARK 465 GLY A 404 REMARK 465 ALA A 405 REMARK 465 MET B -35 REMARK 465 GLY B -34 REMARK 465 SER B -33 REMARK 465 SER B -32 REMARK 465 HIS B -31 REMARK 465 HIS B -30 REMARK 465 HIS B -29 REMARK 465 HIS B -28 REMARK 465 HIS B -27 REMARK 465 HIS B -26 REMARK 465 SER B -25 REMARK 465 SER B -24 REMARK 465 GLY B -23 REMARK 465 LEU B -22 REMARK 465 VAL B -21 REMARK 465 PRO B -20 REMARK 465 ARG B -19 REMARK 465 GLY B -18 REMARK 465 SER B -17 REMARK 465 HIS B -16 REMARK 465 MET B -15 REMARK 465 ALA B -14 REMARK 465 SER B -13 REMARK 465 MET B -12 REMARK 465 THR B -11 REMARK 465 GLY B -10 REMARK 465 GLY B -9 REMARK 465 GLN B -8 REMARK 465 GLN B -7 REMARK 465 MET B -6 REMARK 465 GLY B -5 REMARK 465 ARG B -4 REMARK 465 GLY B -3 REMARK 465 SER B -2 REMARK 465 GLU B -1 REMARK 465 PHE B 0 REMARK 465 MET B 1 REMARK 465 SER B 2 REMARK 465 GLN B 3 REMARK 465 SER B 4 REMARK 465 ILE B 5 REMARK 465 GLU B 69 REMARK 465 PRO B 70 REMARK 465 VAL B 71 REMARK 465 MET B 72 REMARK 465 ARG B 73 REMARK 465 GLY B 74 REMARK 465 PRO B 75 REMARK 465 VAL B 76 REMARK 465 LEU B 77 REMARK 465 ALA B 78 REMARK 465 GLN B 79 REMARK 465 MET B 80 REMARK 465 HIS B 81 REMARK 465 GLY B 82 REMARK 465 LYS B 83 REMARK 465 GLU B 84 REMARK 465 HIS B 85 REMARK 465 SER B 86 REMARK 465 ALA B 87 REMARK 465 LYS B 88 REMARK 465 ARG B 89 REMARK 465 TYR B 213 REMARK 465 GLU B 214 REMARK 465 GLY B 215 REMARK 465 MET B 216 REMARK 465 GLY B 404 REMARK 465 ALA B 405 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 OE1 GLU A 319 O HOH A 420 2.18 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 18 82.65 -154.86 REMARK 500 ASP A 30 61.43 -152.60 REMARK 500 PHE A 131 -48.64 -142.15 REMARK 500 SER A 211 -116.85 54.82 REMARK 500 THR A 235 -67.45 -104.83 REMARK 500 LYS A 300 -122.37 53.47 REMARK 500 GLN A 320 64.24 35.62 REMARK 500 ASP A 322 40.72 -95.81 REMARK 500 LYS A 334 -18.28 -44.15 REMARK 500 ASN A 352 -179.29 -67.36 REMARK 500 MET A 374 67.17 -110.66 REMARK 500 LEU B 7 47.47 -94.59 REMARK 500 VAL B 32 66.16 -101.59 REMARK 500 SER B 37 -117.65 66.83 REMARK 500 ASP B 39 13.93 86.26 REMARK 500 HIS B 55 70.20 -117.03 REMARK 500 VAL B 128 -63.33 -95.48 REMARK 500 PHE B 131 -60.38 -102.42 REMARK 500 ASN B 199 69.82 -119.59 REMARK 500 SER B 211 -122.98 64.15 REMARK 500 THR B 235 -72.88 -101.93 REMARK 500 ASN B 252 75.99 -115.16 REMARK 500 LYS B 277 59.66 -141.20 REMARK 500 ASN B 325 87.19 -157.71 REMARK 500 MET B 374 73.00 -102.97 REMARK 500 ASP B 382 -8.29 65.52 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 LYS B 300 ASP B 301 31.21 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 MG A 408 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 163 OD1 REMARK 620 2 THR A 166 OG1 107.3 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HEM A 406 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 353 SG REMARK 620 2 HEM A 406 NA 105.4 REMARK 620 3 HEM A 406 NB 89.2 88.8 REMARK 620 4 HEM A 406 NC 85.4 168.9 94.1 REMARK 620 5 HEM A 406 ND 97.9 87.1 172.5 88.8 REMARK 620 6 HOH A 427 O 155.4 69.8 66.9 101.4 105.7 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HEM B 406 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS B 353 SG REMARK 620 2 HEM B 406 NA 99.3 REMARK 620 3 HEM B 406 NB 85.2 80.9 REMARK 620 4 HEM B 406 NC 91.4 164.5 89.0 REMARK 620 5 HEM B 406 ND 105.7 95.9 169.1 91.9 REMARK 620 6 HOH B 422 O 154.8 74.3 69.8 91.3 99.3 REMARK 620 N 1 2 3 4 5 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 406 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 407 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 408 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 409 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 406 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 407 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 408 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3NC3 RELATED DB: PDB REMARK 900 RELATED ID: 3NC7 RELATED DB: PDB REMARK 900 RELATED ID: 3NC6 RELATED DB: PDB DBREF 3NC5 A 1 405 UNP O34926 CYPX_BACSU 1 405 DBREF 3NC5 B 1 405 UNP O34926 CYPX_BACSU 1 405 SEQADV 3NC5 MET A -35 UNP O34926 EXPRESSION TAG SEQADV 3NC5 GLY A -34 UNP O34926 EXPRESSION TAG SEQADV 3NC5 SER A -33 UNP O34926 EXPRESSION TAG SEQADV 3NC5 SER A -32 UNP O34926 EXPRESSION TAG SEQADV 3NC5 HIS A -31 UNP O34926 EXPRESSION TAG SEQADV 3NC5 HIS A -30 UNP O34926 EXPRESSION TAG SEQADV 3NC5 HIS A -29 UNP O34926 EXPRESSION TAG SEQADV 3NC5 HIS A -28 UNP O34926 EXPRESSION TAG SEQADV 3NC5 HIS A -27 UNP O34926 EXPRESSION TAG SEQADV 3NC5 HIS A -26 UNP O34926 EXPRESSION TAG SEQADV 3NC5 SER A -25 UNP O34926 EXPRESSION TAG SEQADV 3NC5 SER A -24 UNP O34926 EXPRESSION TAG SEQADV 3NC5 GLY A -23 UNP O34926 EXPRESSION TAG SEQADV 3NC5 LEU A -22 UNP O34926 EXPRESSION TAG SEQADV 3NC5 VAL A -21 UNP O34926 EXPRESSION TAG SEQADV 3NC5 PRO A -20 UNP O34926 EXPRESSION TAG SEQADV 3NC5 ARG A -19 UNP O34926 EXPRESSION TAG SEQADV 3NC5 GLY A -18 UNP O34926 EXPRESSION TAG SEQADV 3NC5 SER A -17 UNP O34926 EXPRESSION TAG SEQADV 3NC5 HIS A -16 UNP O34926 EXPRESSION TAG SEQADV 3NC5 MET A -15 UNP O34926 EXPRESSION TAG SEQADV 3NC5 ALA A -14 UNP O34926 EXPRESSION TAG SEQADV 3NC5 SER A -13 UNP O34926 EXPRESSION TAG SEQADV 3NC5 MET A -12 UNP O34926 EXPRESSION TAG SEQADV 3NC5 THR A -11 UNP O34926 EXPRESSION TAG SEQADV 3NC5 GLY A -10 UNP O34926 EXPRESSION TAG SEQADV 3NC5 GLY A -9 UNP O34926 EXPRESSION TAG SEQADV 3NC5 GLN A -8 UNP O34926 EXPRESSION TAG SEQADV 3NC5 GLN A -7 UNP O34926 EXPRESSION TAG SEQADV 3NC5 MET A -6 UNP O34926 EXPRESSION TAG SEQADV 3NC5 GLY A -5 UNP O34926 EXPRESSION TAG SEQADV 3NC5 ARG A -4 UNP O34926 EXPRESSION TAG SEQADV 3NC5 GLY A -3 UNP O34926 EXPRESSION TAG SEQADV 3NC5 SER A -2 UNP O34926 EXPRESSION TAG SEQADV 3NC5 GLU A -1 UNP O34926 EXPRESSION TAG SEQADV 3NC5 PHE A 0 UNP O34926 EXPRESSION TAG SEQADV 3NC5 THR A 356 UNP O34926 ALA 356 ENGINEERED MUTATION SEQADV 3NC5 MET B -35 UNP O34926 EXPRESSION TAG SEQADV 3NC5 GLY B -34 UNP O34926 EXPRESSION TAG SEQADV 3NC5 SER B -33 UNP O34926 EXPRESSION TAG SEQADV 3NC5 SER B -32 UNP O34926 EXPRESSION TAG SEQADV 3NC5 HIS B -31 UNP O34926 EXPRESSION TAG SEQADV 3NC5 HIS B -30 UNP O34926 EXPRESSION TAG SEQADV 3NC5 HIS B -29 UNP O34926 EXPRESSION TAG SEQADV 3NC5 HIS B -28 UNP O34926 EXPRESSION TAG SEQADV 3NC5 HIS B -27 UNP O34926 EXPRESSION TAG SEQADV 3NC5 HIS B -26 UNP O34926 EXPRESSION TAG SEQADV 3NC5 SER B -25 UNP O34926 EXPRESSION TAG SEQADV 3NC5 SER B -24 UNP O34926 EXPRESSION TAG SEQADV 3NC5 GLY B -23 UNP O34926 EXPRESSION TAG SEQADV 3NC5 LEU B -22 UNP O34926 EXPRESSION TAG SEQADV 3NC5 VAL B -21 UNP O34926 EXPRESSION TAG SEQADV 3NC5 PRO B -20 UNP O34926 EXPRESSION TAG SEQADV 3NC5 ARG B -19 UNP O34926 EXPRESSION TAG SEQADV 3NC5 GLY B -18 UNP O34926 EXPRESSION TAG SEQADV 3NC5 SER B -17 UNP O34926 EXPRESSION TAG SEQADV 3NC5 HIS B -16 UNP O34926 EXPRESSION TAG SEQADV 3NC5 MET B -15 UNP O34926 EXPRESSION TAG SEQADV 3NC5 ALA B -14 UNP O34926 EXPRESSION TAG SEQADV 3NC5 SER B -13 UNP O34926 EXPRESSION TAG SEQADV 3NC5 MET B -12 UNP O34926 EXPRESSION TAG SEQADV 3NC5 THR B -11 UNP O34926 EXPRESSION TAG SEQADV 3NC5 GLY B -10 UNP O34926 EXPRESSION TAG SEQADV 3NC5 GLY B -9 UNP O34926 EXPRESSION TAG SEQADV 3NC5 GLN B -8 UNP O34926 EXPRESSION TAG SEQADV 3NC5 GLN B -7 UNP O34926 EXPRESSION TAG SEQADV 3NC5 MET B -6 UNP O34926 EXPRESSION TAG SEQADV 3NC5 GLY B -5 UNP O34926 EXPRESSION TAG SEQADV 3NC5 ARG B -4 UNP O34926 EXPRESSION TAG SEQADV 3NC5 GLY B -3 UNP O34926 EXPRESSION TAG SEQADV 3NC5 SER B -2 UNP O34926 EXPRESSION TAG SEQADV 3NC5 GLU B -1 UNP O34926 EXPRESSION TAG SEQADV 3NC5 PHE B 0 UNP O34926 EXPRESSION TAG SEQADV 3NC5 THR B 356 UNP O34926 ALA 356 ENGINEERED MUTATION SEQRES 1 A 441 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY SEQRES 2 A 441 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY SEQRES 3 A 441 GLY GLN GLN MET GLY ARG GLY SER GLU PHE MET SER GLN SEQRES 4 A 441 SER ILE LYS LEU PHE SER VAL LEU SER ASP GLN PHE GLN SEQRES 5 A 441 ASN ASN PRO TYR ALA TYR PHE SER GLN LEU ARG GLU GLU SEQRES 6 A 441 ASP PRO VAL HIS TYR GLU GLU SER ILE ASP SER TYR PHE SEQRES 7 A 441 ILE SER ARG TYR HIS ASP VAL ARG TYR ILE LEU GLN HIS SEQRES 8 A 441 PRO ASP ILE PHE THR THR LYS SER LEU VAL GLU ARG ALA SEQRES 9 A 441 GLU PRO VAL MET ARG GLY PRO VAL LEU ALA GLN MET HIS SEQRES 10 A 441 GLY LYS GLU HIS SER ALA LYS ARG ARG ILE VAL VAL ARG SEQRES 11 A 441 SER PHE ILE GLY ASP ALA LEU ASP HIS LEU SER PRO LEU SEQRES 12 A 441 ILE LYS GLN ASN ALA GLU ASN LEU LEU ALA PRO TYR LEU SEQRES 13 A 441 GLU ARG GLY LYS SER ASP LEU VAL ASN ASP PHE GLY LYS SEQRES 14 A 441 THR PHE ALA VAL CYS VAL THR MET ASP MET LEU GLY LEU SEQRES 15 A 441 ASP LYS ARG ASP HIS GLU LYS ILE SER GLU TRP HIS SER SEQRES 16 A 441 GLY VAL ALA ASP PHE ILE THR SER ILE SER GLN SER PRO SEQRES 17 A 441 GLU ALA ARG ALA HIS SER LEU TRP CYS SER GLU GLN LEU SEQRES 18 A 441 SER GLN TYR LEU MET PRO VAL ILE LYS GLU ARG ARG VAL SEQRES 19 A 441 ASN PRO GLY SER ASP LEU ILE SER ILE LEU CYS THR SER SEQRES 20 A 441 GLU TYR GLU GLY MET ALA LEU SER ASP LYS ASP ILE LEU SEQRES 21 A 441 ALA LEU ILE LEU ASN VAL LEU LEU ALA ALA THR GLU PRO SEQRES 22 A 441 ALA ASP LYS THR LEU ALA LEU MET ILE TYR HIS LEU LEU SEQRES 23 A 441 ASN ASN PRO GLU GLN MET ASN ASP VAL LEU ALA ASP ARG SEQRES 24 A 441 SER LEU VAL PRO ARG ALA ILE ALA GLU THR LEU ARG TYR SEQRES 25 A 441 LYS PRO PRO VAL GLN LEU ILE PRO ARG GLN LEU SER GLN SEQRES 26 A 441 ASP THR VAL VAL GLY GLY MET GLU ILE LYS LYS ASP THR SEQRES 27 A 441 ILE VAL PHE CYS MET ILE GLY ALA ALA ASN ARG ASP PRO SEQRES 28 A 441 GLU ALA PHE GLU GLN PRO ASP VAL PHE ASN ILE HIS ARG SEQRES 29 A 441 GLU ASP LEU GLY ILE LYS SER ALA PHE SER GLY ALA ALA SEQRES 30 A 441 ARG HIS LEU ALA PHE GLY SER GLY ILE HIS ASN CYS VAL SEQRES 31 A 441 GLY THR ALA PHE ALA LYS ASN GLU ILE GLU ILE VAL ALA SEQRES 32 A 441 ASN ILE VAL LEU ASP LYS MET ARG ASN ILE ARG LEU GLU SEQRES 33 A 441 GLU ASP PHE CYS TYR ALA GLU SER GLY LEU TYR THR ARG SEQRES 34 A 441 GLY PRO VAL SER LEU LEU VAL ALA PHE ASP GLY ALA SEQRES 1 B 441 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY SEQRES 2 B 441 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY SEQRES 3 B 441 GLY GLN GLN MET GLY ARG GLY SER GLU PHE MET SER GLN SEQRES 4 B 441 SER ILE LYS LEU PHE SER VAL LEU SER ASP GLN PHE GLN SEQRES 5 B 441 ASN ASN PRO TYR ALA TYR PHE SER GLN LEU ARG GLU GLU SEQRES 6 B 441 ASP PRO VAL HIS TYR GLU GLU SER ILE ASP SER TYR PHE SEQRES 7 B 441 ILE SER ARG TYR HIS ASP VAL ARG TYR ILE LEU GLN HIS SEQRES 8 B 441 PRO ASP ILE PHE THR THR LYS SER LEU VAL GLU ARG ALA SEQRES 9 B 441 GLU PRO VAL MET ARG GLY PRO VAL LEU ALA GLN MET HIS SEQRES 10 B 441 GLY LYS GLU HIS SER ALA LYS ARG ARG ILE VAL VAL ARG SEQRES 11 B 441 SER PHE ILE GLY ASP ALA LEU ASP HIS LEU SER PRO LEU SEQRES 12 B 441 ILE LYS GLN ASN ALA GLU ASN LEU LEU ALA PRO TYR LEU SEQRES 13 B 441 GLU ARG GLY LYS SER ASP LEU VAL ASN ASP PHE GLY LYS SEQRES 14 B 441 THR PHE ALA VAL CYS VAL THR MET ASP MET LEU GLY LEU SEQRES 15 B 441 ASP LYS ARG ASP HIS GLU LYS ILE SER GLU TRP HIS SER SEQRES 16 B 441 GLY VAL ALA ASP PHE ILE THR SER ILE SER GLN SER PRO SEQRES 17 B 441 GLU ALA ARG ALA HIS SER LEU TRP CYS SER GLU GLN LEU SEQRES 18 B 441 SER GLN TYR LEU MET PRO VAL ILE LYS GLU ARG ARG VAL SEQRES 19 B 441 ASN PRO GLY SER ASP LEU ILE SER ILE LEU CYS THR SER SEQRES 20 B 441 GLU TYR GLU GLY MET ALA LEU SER ASP LYS ASP ILE LEU SEQRES 21 B 441 ALA LEU ILE LEU ASN VAL LEU LEU ALA ALA THR GLU PRO SEQRES 22 B 441 ALA ASP LYS THR LEU ALA LEU MET ILE TYR HIS LEU LEU SEQRES 23 B 441 ASN ASN PRO GLU GLN MET ASN ASP VAL LEU ALA ASP ARG SEQRES 24 B 441 SER LEU VAL PRO ARG ALA ILE ALA GLU THR LEU ARG TYR SEQRES 25 B 441 LYS PRO PRO VAL GLN LEU ILE PRO ARG GLN LEU SER GLN SEQRES 26 B 441 ASP THR VAL VAL GLY GLY MET GLU ILE LYS LYS ASP THR SEQRES 27 B 441 ILE VAL PHE CYS MET ILE GLY ALA ALA ASN ARG ASP PRO SEQRES 28 B 441 GLU ALA PHE GLU GLN PRO ASP VAL PHE ASN ILE HIS ARG SEQRES 29 B 441 GLU ASP LEU GLY ILE LYS SER ALA PHE SER GLY ALA ALA SEQRES 30 B 441 ARG HIS LEU ALA PHE GLY SER GLY ILE HIS ASN CYS VAL SEQRES 31 B 441 GLY THR ALA PHE ALA LYS ASN GLU ILE GLU ILE VAL ALA SEQRES 32 B 441 ASN ILE VAL LEU ASP LYS MET ARG ASN ILE ARG LEU GLU SEQRES 33 B 441 GLU ASP PHE CYS TYR ALA GLU SER GLY LEU TYR THR ARG SEQRES 34 B 441 GLY PRO VAL SER LEU LEU VAL ALA PHE ASP GLY ALA HET HEM A 406 43 HET GOL A 407 6 HET MG A 408 1 HET MG A 409 1 HET HEM B 406 43 HET GOL B 407 6 HET MG B 408 1 HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETNAM GOL GLYCEROL HETNAM MG MAGNESIUM ION HETSYN HEM HEME HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 3 HEM 2(C34 H32 FE N4 O4) FORMUL 4 GOL 2(C3 H8 O3) FORMUL 5 MG 3(MG 2+) FORMUL 10 HOH *32(H2 O) HELIX 1 1 SER A 12 ASN A 18 1 7 HELIX 2 2 PRO A 19 ALA A 21 5 3 HELIX 3 3 TYR A 22 ASP A 30 1 9 HELIX 4 4 ARG A 45 HIS A 55 1 11 HELIX 5 5 LYS A 88 ALA A 117 1 30 HELIX 6 6 PHE A 131 GLY A 145 1 15 HELIX 7 7 ASP A 147 ARG A 149 5 3 HELIX 8 8 ASP A 150 SER A 167 1 18 HELIX 9 9 SER A 171 ASN A 199 1 29 HELIX 10 10 ASP A 203 THR A 210 1 8 HELIX 11 11 SER A 219 ALA A 234 1 16 HELIX 12 12 THR A 235 ASN A 252 1 18 HELIX 13 13 ASN A 252 ASP A 262 1 11 HELIX 14 14 LEU A 265 LYS A 277 1 13 HELIX 15 15 ILE A 308 ARG A 313 1 6 HELIX 16 16 GLY A 332 ALA A 336 5 5 HELIX 17 17 GLY A 355 MET A 374 1 20 HELIX 18 18 SER B 12 ASN B 18 1 7 HELIX 19 19 PRO B 19 ALA B 21 5 3 HELIX 20 20 TYR B 22 ASP B 30 1 9 HELIX 21 21 ARG B 45 HIS B 55 1 11 HELIX 22 22 VAL B 92 LEU B 104 1 13 HELIX 23 23 LEU B 104 ALA B 117 1 14 HELIX 24 24 PHE B 131 GLY B 145 1 15 HELIX 25 25 ASP B 147 ARG B 149 5 3 HELIX 26 26 ASP B 150 SER B 167 1 18 HELIX 27 27 SER B 171 ASN B 199 1 29 HELIX 28 28 ASP B 203 CYS B 209 1 7 HELIX 29 29 SER B 219 ASN B 252 1 34 HELIX 30 30 ASN B 252 ASP B 262 1 11 HELIX 31 31 LEU B 265 LYS B 277 1 13 HELIX 32 32 ILE B 308 ARG B 313 1 6 HELIX 33 33 GLY B 332 ALA B 336 5 5 HELIX 34 34 SER B 348 ASN B 352 5 5 HELIX 35 35 GLY B 355 MET B 374 1 20 SHEET 1 A 5 VAL A 32 TYR A 34 0 SHEET 2 A 5 SER A 40 ILE A 43 -1 O PHE A 42 N HIS A 33 SHEET 3 A 5 ILE A 303 MET A 307 1 O PHE A 305 N TYR A 41 SHEET 4 A 5 LEU A 282 LEU A 287 -1 N ARG A 285 O VAL A 304 SHEET 5 A 5 PHE A 59 THR A 60 -1 N THR A 60 O GLN A 286 SHEET 1 B 3 LYS A 124 ASP A 126 0 SHEET 2 B 3 LEU A 399 ALA A 401 -1 O VAL A 400 N SER A 125 SHEET 3 B 3 ARG A 378 LEU A 379 -1 N ARG A 378 O ALA A 401 SHEET 1 C 2 THR A 291 VAL A 293 0 SHEET 2 C 2 MET A 296 ILE A 298 -1 O MET A 296 N VAL A 293 SHEET 1 D 2 GLU A 387 SER A 388 0 SHEET 2 D 2 GLY A 394 PRO A 395 -1 O GLY A 394 N SER A 388 SHEET 1 E 5 VAL B 32 TYR B 34 0 SHEET 2 E 5 TYR B 41 ILE B 43 -1 O PHE B 42 N HIS B 33 SHEET 3 E 5 ILE B 303 MET B 307 1 O PHE B 305 N TYR B 41 SHEET 4 E 5 LEU B 282 LEU B 287 -1 N ARG B 285 O VAL B 304 SHEET 5 E 5 PHE B 59 THR B 60 -1 N THR B 60 O GLN B 286 SHEET 1 F 3 LYS B 124 ASP B 126 0 SHEET 2 F 3 LEU B 399 ALA B 401 -1 O VAL B 400 N SER B 125 SHEET 3 F 3 ARG B 378 LEU B 379 -1 N ARG B 378 O ALA B 401 SHEET 1 G 2 GLU B 387 SER B 388 0 SHEET 2 G 2 GLY B 394 PRO B 395 -1 O GLY B 394 N SER B 388 LINK OD1 ASP A 163 MG MG A 408 1555 1555 2.68 LINK OG1 THR A 166 MG MG A 408 1555 1555 2.54 LINK O GLN A 281 MG MG A 409 1555 1555 2.63 LINK SG CYS A 353 FE HEM A 406 1555 1555 2.33 LINK FE HEM A 406 O HOH A 427 1555 1555 2.25 LINK SG CYS B 353 FE HEM B 406 1555 1555 2.21 LINK O VAL B 354 MG MG B 408 1555 1555 2.96 LINK FE HEM B 406 O HOH B 422 1555 1555 2.04 CISPEP 1 ILE A 38 ASP A 39 0 29.57 CISPEP 2 SER A 211 GLU A 212 0 0.59 CISPEP 3 ILE B 38 ASP B 39 0 20.94 CISPEP 4 VAL B 65 GLU B 66 0 -18.89 CISPEP 5 ARG B 90 ILE B 91 0 -0.15 CISPEP 6 SER B 211 GLU B 212 0 -10.70 SITE 1 AC1 15 LEU A 64 ASN A 229 ALA A 233 ALA A 234 SITE 2 AC1 15 PRO A 237 THR A 241 ARG A 285 ALA A 345 SITE 3 AC1 15 PHE A 346 HIS A 351 CYS A 353 GLY A 355 SITE 4 AC1 15 PHE A 358 GOL A 407 HOH A 427 SITE 1 AC2 5 PRO A 237 VAL A 280 TYR A 391 HEM A 406 SITE 2 AC2 5 HOH A 427 SITE 1 AC3 3 ASP A 163 THR A 166 SER A 167 SITE 1 AC4 4 GLN A 281 MET A 307 ILE A 308 GLY A 309 SITE 1 AC5 16 GLU B 66 ILE B 97 ASN B 229 ALA B 233 SITE 2 AC5 16 ALA B 234 PRO B 237 LEU B 274 ILE B 283 SITE 3 AC5 16 ARG B 285 ALA B 345 PHE B 346 HIS B 351 SITE 4 AC5 16 CYS B 353 GLU B 362 ILE B 363 HOH B 422 SITE 1 AC6 4 ALA B 233 PRO B 237 TYR B 391 HOH B 422 SITE 1 AC7 6 ILE B 97 VAL B 354 GLY B 355 THR B 356 SITE 2 AC7 6 ALA B 357 PHE B 358 CRYST1 63.800 105.400 143.900 90.00 90.00 90.00 P 21 21 21 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.015674 0.000000 0.000000 0.00000 SCALE2 0.000000 0.009488 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006949 0.00000 (ATOM LINES ARE NOT SHOWN.) END
HEADER OXIDOREDUCTASE 04-JUN-10 3NC6 TITLE CYP134A1 1-PHENYLIMIDAZOLE BOUND STRUCTURE COMPND MOL_ID: 1; COMPND 2 MOLECULE: CYTOCHROME P450 CYPX; COMPND 3 CHAIN: A, B; COMPND 4 EC: 1.14.-.-; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS; SOURCE 3 ORGANISM_TAXID: 1423; SOURCE 4 STRAIN: 168; SOURCE 5 GENE: BSU35060, CYP134, CYPB, CYPX; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PLASMID KEYWDS CYTOCHROME P450 OXIDASE, HAEM PROTEIN, OXIDOREDUCTASE EXPDTA X-RAY DIFFRACTION AUTHOR M.J.CRYLE,I.SCHLICHTING REVDAT 3 21-FEB-24 3NC6 1 REMARK SEQADV LINK REVDAT 2 22-SEP-10 3NC6 1 JRNL REVDAT 1 11-AUG-10 3NC6 0 JRNL AUTH M.J.CRYLE,S.G.BELL,I.SCHLICHTING JRNL TITL STRUCTURAL AND BIOCHEMICAL CHARACTERIZATION OF THE JRNL TITL 2 CYTOCHROME P450 CYPX (CYP134A1) FROM BACILLUS SUBTILIS: A JRNL TITL 3 CYCLO-L-LEUCYL-L-LEUCYL DIPEPTIDE OXIDASE. JRNL REF BIOCHEMISTRY V. 49 7282 2010 JRNL REFN ISSN 0006-2960 JRNL PMID 20690619 JRNL DOI 10.1021/BI100910Y REMARK 2 REMARK 2 RESOLUTION. 3.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.5.0070 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.84 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 18488 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 + TEST SET) : 0.217 REMARK 3 R VALUE (WORKING SET) : 0.214 REMARK 3 FREE R VALUE : 0.278 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900 REMARK 3 FREE R VALUE TEST SET COUNT : 912 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.10 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.18 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1260 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0 REMARK 3 BIN R VALUE (WORKING SET) : 0.2290 REMARK 3 BIN FREE R VALUE SET COUNT : 64 REMARK 3 BIN FREE R VALUE : 0.3230 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6029 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 109 REMARK 3 SOLVENT ATOMS : 5 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 72.80 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 62.57 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.00000 REMARK 3 B22 (A**2) : 0.00000 REMARK 3 B33 (A**2) : 0.00000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 0.519 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.419 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 45.503 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.929 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.879 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6281 ; 0.011 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8537 ; 1.490 ; 2.011 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 760 ; 6.485 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 294 ;30.439 ;24.014 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1064 ;18.571 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 45 ;20.406 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 944 ; 0.099 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4783 ; 0.006 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3814 ; 0.300 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6164 ; 0.586 ; 2.000 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2467 ; 1.069 ; 3.000 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2372 ; 1.873 ; 4.500 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 2 REMARK 3 REMARK 3 NCS GROUP NUMBER : 1 REMARK 3 CHAIN NAMES : A B REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 A 5 A 403 4 REMARK 3 1 B 5 B 403 4 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 MEDIUM POSITIONAL 1 A (A): 2946 ; 0.52 ; 0.50 REMARK 3 MEDIUM THERMAL 1 A (A**2): 2946 ; 0.49 ; 2.00 REMARK 3 REMARK 3 NCS GROUP NUMBER : 2 REMARK 3 CHAIN NAMES : A B REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 C 1 A 406 4 REMARK 3 1 D 1 B 406 4 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 MEDIUM POSITIONAL 2 A (A): 43 ; 0.27 ; 0.50 REMARK 3 MEDIUM THERMAL 2 A (A**2): 43 ; 1.12 ; 2.00 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 10 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 5 A 102 REMARK 3 ORIGIN FOR THE GROUP (A): 18.9921 -15.9982 -8.8502 REMARK 3 T TENSOR REMARK 3 T11: 0.6375 T22: 0.9696 REMARK 3 T33: 0.2337 T12: -0.1658 REMARK 3 T13: 0.2725 T23: -0.0808 REMARK 3 L TENSOR REMARK 3 L11: 6.1361 L22: 4.1960 REMARK 3 L33: 3.4230 L12: 1.1831 REMARK 3 L13: 0.7804 L23: 0.0755 REMARK 3 S TENSOR REMARK 3 S11: -0.0319 S12: 0.0356 S13: -0.4811 REMARK 3 S21: 0.2795 S22: -0.2797 S23: 0.5078 REMARK 3 S31: 0.7170 S32: -0.7524 S33: 0.3115 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 103 A 150 REMARK 3 ORIGIN FOR THE GROUP (A): 46.4533 -11.0145 -20.1869 REMARK 3 T TENSOR REMARK 3 T11: 0.2373 T22: 0.5994 REMARK 3 T33: 0.0691 T12: 0.0682 REMARK 3 T13: 0.0773 T23: 0.0144 REMARK 3 L TENSOR REMARK 3 L11: 3.5670 L22: 9.6384 REMARK 3 L33: 3.4500 L12: -0.0694 REMARK 3 L13: 2.7483 L23: 3.0048 REMARK 3 S TENSOR REMARK 3 S11: 0.1856 S12: 0.2266 S13: -0.2428 REMARK 3 S21: -0.2766 S22: 0.2543 S23: -0.4705 REMARK 3 S31: -0.2028 S32: 0.1502 S33: -0.4398 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 151 A 290 REMARK 3 ORIGIN FOR THE GROUP (A): 33.4093 -17.3314 -17.9062 REMARK 3 T TENSOR REMARK 3 T11: 0.4028 T22: 0.6180 REMARK 3 T33: 0.1989 T12: -0.0117 REMARK 3 T13: 0.0166 T23: -0.0245 REMARK 3 L TENSOR REMARK 3 L11: 2.0054 L22: 1.6486 REMARK 3 L33: 3.6100 L12: -0.1221 REMARK 3 L13: -0.0282 L23: 1.4418 REMARK 3 S TENSOR REMARK 3 S11: 0.1096 S12: 0.1293 S13: -0.5582 REMARK 3 S21: 0.1513 S22: -0.1104 S23: 0.2149 REMARK 3 S31: 0.5629 S32: -0.2276 S33: 0.0008 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 291 A 353 REMARK 3 ORIGIN FOR THE GROUP (A): 23.0773 -13.6452 -0.6439 REMARK 3 T TENSOR REMARK 3 T11: 0.7586 T22: 0.8269 REMARK 3 T33: 0.2977 T12: -0.2793 REMARK 3 T13: 0.2364 T23: 0.0001 REMARK 3 L TENSOR REMARK 3 L11: 6.2246 L22: 7.2836 REMARK 3 L33: 5.0004 L12: 1.0034 REMARK 3 L13: 0.7701 L23: 3.5931 REMARK 3 S TENSOR REMARK 3 S11: 0.0525 S12: -0.5829 S13: -0.5673 REMARK 3 S21: 1.1711 S22: -0.3794 S23: 1.1498 REMARK 3 S31: 1.2430 S32: -0.8394 S33: 0.3269 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 354 A 403 REMARK 3 ORIGIN FOR THE GROUP (A): 39.1435 -3.2194 -12.5642 REMARK 3 T TENSOR REMARK 3 T11: 0.2575 T22: 0.5516 REMARK 3 T33: 0.0733 T12: 0.0218 REMARK 3 T13: 0.0608 T23: -0.0165 REMARK 3 L TENSOR REMARK 3 L11: 9.0022 L22: 5.4909 REMARK 3 L33: 7.0963 L12: 1.1705 REMARK 3 L13: 1.6643 L23: 0.2163 REMARK 3 S TENSOR REMARK 3 S11: 0.1766 S12: -0.0512 S13: 0.5687 REMARK 3 S21: 0.3438 S22: -0.2302 S23: -0.2129 REMARK 3 S31: -0.3728 S32: -0.1277 S33: 0.0536 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 4 B 66 REMARK 3 ORIGIN FOR THE GROUP (A): 50.6451 11.6638 18.5635 REMARK 3 T TENSOR REMARK 3 T11: 0.4251 T22: 0.8431 REMARK 3 T33: 0.5088 T12: -0.1014 REMARK 3 T13: -0.0077 T23: 0.0681 REMARK 3 L TENSOR REMARK 3 L11: 7.1593 L22: 1.4971 REMARK 3 L33: 4.8130 L12: 0.0380 REMARK 3 L13: -0.9605 L23: 2.3825 REMARK 3 S TENSOR REMARK 3 S11: 0.1512 S12: -0.3019 S13: 0.3508 REMARK 3 S21: 0.0323 S22: 0.1691 S23: -0.5035 REMARK 3 S31: -0.1305 S32: 0.6313 S33: -0.3202 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 67 B 104 REMARK 3 ORIGIN FOR THE GROUP (A): 27.7255 -4.4354 21.7263 REMARK 3 T TENSOR REMARK 3 T11: 0.6697 T22: 0.7610 REMARK 3 T33: 0.6800 T12: -0.0730 REMARK 3 T13: 0.0472 T23: 0.0404 REMARK 3 L TENSOR REMARK 3 L11: 0.1069 L22: 8.5388 REMARK 3 L33: 4.8669 L12: -0.0465 REMARK 3 L13: -0.1242 L23: 1.2448 REMARK 3 S TENSOR REMARK 3 S11: -0.0615 S12: -0.0637 S13: -0.2488 REMARK 3 S21: -1.1103 S22: 0.3698 S23: 0.1478 REMARK 3 S31: 0.5978 S32: 0.0300 S33: -0.3082 REMARK 3 REMARK 3 TLS GROUP : 8 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 105 B 168 REMARK 3 ORIGIN FOR THE GROUP (A): 23.1153 12.5545 32.2909 REMARK 3 T TENSOR REMARK 3 T11: 0.3071 T22: 0.6107 REMARK 3 T33: 0.0736 T12: 0.0358 REMARK 3 T13: 0.0722 T23: 0.0279 REMARK 3 L TENSOR REMARK 3 L11: 4.6690 L22: 3.6850 REMARK 3 L33: 3.7962 L12: 0.2522 REMARK 3 L13: 0.8943 L23: -1.1702 REMARK 3 S TENSOR REMARK 3 S11: -0.0129 S12: -0.4094 S13: 0.1152 REMARK 3 S21: 0.4604 S22: 0.3678 S23: 0.4523 REMARK 3 S31: -0.4506 S32: -0.2709 S33: -0.3548 REMARK 3 REMARK 3 TLS GROUP : 9 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 169 B 290 REMARK 3 ORIGIN FOR THE GROUP (A): 31.1176 6.5107 26.4935 REMARK 3 T TENSOR REMARK 3 T11: 0.3236 T22: 0.5759 REMARK 3 T33: 0.1074 T12: 0.0049 REMARK 3 T13: -0.0270 T23: 0.0375 REMARK 3 L TENSOR REMARK 3 L11: 2.9024 L22: 1.4200 REMARK 3 L33: 3.4355 L12: 0.1918 REMARK 3 L13: -0.5767 L23: -0.4045 REMARK 3 S TENSOR REMARK 3 S11: 0.0874 S12: 0.0063 S13: -0.4084 REMARK 3 S21: -0.0393 S22: 0.2026 S23: 0.1221 REMARK 3 S31: 0.1638 S32: -0.1468 S33: -0.2900 REMARK 3 REMARK 3 TLS GROUP : 10 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 291 B 404 REMARK 3 ORIGIN FOR THE GROUP (A): 34.6344 15.1640 16.0611 REMARK 3 T TENSOR REMARK 3 T11: 0.3584 T22: 0.5613 REMARK 3 T33: 0.0436 T12: -0.0245 REMARK 3 T13: 0.0617 T23: 0.0042 REMARK 3 L TENSOR REMARK 3 L11: 6.3630 L22: 4.0797 REMARK 3 L33: 3.5795 L12: -0.7311 REMARK 3 L13: -0.2596 L23: 0.1023 REMARK 3 S TENSOR REMARK 3 S11: 0.1739 S12: -0.0178 S13: 0.3562 REMARK 3 S21: -0.5787 S22: 0.0935 S23: -0.0249 REMARK 3 S31: -0.2876 S32: 0.3171 S33: -0.2674 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.40 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 3NC6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUN-10. REMARK 100 THE DEPOSITION ID IS D_1000059645. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 11-DEC-09 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SLS REMARK 200 BEAMLINE : X10SA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9790 REMARK 200 MONOCHROMATOR : SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS, XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18488 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100 REMARK 200 RESOLUTION RANGE LOW (A) : 48.060 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 94.3 REMARK 200 DATA REDUNDANCY : 4.800 REMARK 200 R MERGE (I) : 0.11000 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.18 REMARK 200 COMPLETENESS FOR SHELL (%) : 86.1 REMARK 200 DATA REDUNDANCY IN SHELL : 4.90 REMARK 200 R MERGE FOR SHELL (I) : 0.43000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.000 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD REMARK 200 SOFTWARE USED: SHARP REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.83 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS, 0.1 M MGCL2, 12% (W/V) REMARK 280 POLYETHYLENE GLYCOL-3350, PH 6.5, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 293K 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 32.47500 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 71.46500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 53.45000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 71.46500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.47500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 53.45000 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 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: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A 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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: B 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 -35 REMARK 465 GLY A -34 REMARK 465 SER A -33 REMARK 465 SER A -32 REMARK 465 HIS A -31 REMARK 465 HIS A -30 REMARK 465 HIS A -29 REMARK 465 HIS A -28 REMARK 465 HIS A -27 REMARK 465 HIS A -26 REMARK 465 SER A -25 REMARK 465 SER A -24 REMARK 465 GLY A -23 REMARK 465 LEU A -22 REMARK 465 VAL A -21 REMARK 465 PRO A -20 REMARK 465 ARG A -19 REMARK 465 GLY A -18 REMARK 465 SER A -17 REMARK 465 HIS A -16 REMARK 465 MET A -15 REMARK 465 ALA A -14 REMARK 465 SER A -13 REMARK 465 MET A -12 REMARK 465 THR A -11 REMARK 465 GLY A -10 REMARK 465 GLY A -9 REMARK 465 GLN A -8 REMARK 465 GLN A -7 REMARK 465 MET A -6 REMARK 465 GLY A -5 REMARK 465 ARG A -4 REMARK 465 GLY A -3 REMARK 465 SER A -2 REMARK 465 GLU A -1 REMARK 465 PHE A 0 REMARK 465 MET A 1 REMARK 465 SER A 2 REMARK 465 GLN A 3 REMARK 465 SER A 4 REMARK 465 GLU A 69 REMARK 465 PRO A 70 REMARK 465 VAL A 71 REMARK 465 MET A 72 REMARK 465 ARG A 73 REMARK 465 GLY A 74 REMARK 465 PRO A 75 REMARK 465 VAL A 76 REMARK 465 LEU A 77 REMARK 465 ALA A 78 REMARK 465 GLN A 79 REMARK 465 MET A 80 REMARK 465 HIS A 81 REMARK 465 GLY A 82 REMARK 465 LYS A 83 REMARK 465 GLU A 84 REMARK 465 HIS A 85 REMARK 465 SER A 86 REMARK 465 SER A 211 REMARK 465 GLU A 212 REMARK 465 TYR A 213 REMARK 465 GLU A 214 REMARK 465 GLY A 215 REMARK 465 MET A 216 REMARK 465 ALA A 217 REMARK 465 GLY A 404 REMARK 465 ALA A 405 REMARK 465 MET B -35 REMARK 465 GLY B -34 REMARK 465 SER B -33 REMARK 465 SER B -32 REMARK 465 HIS B -31 REMARK 465 HIS B -30 REMARK 465 HIS B -29 REMARK 465 HIS B -28 REMARK 465 HIS B -27 REMARK 465 HIS B -26 REMARK 465 SER B -25 REMARK 465 SER B -24 REMARK 465 GLY B -23 REMARK 465 LEU B -22 REMARK 465 VAL B -21 REMARK 465 PRO B -20 REMARK 465 ARG B -19 REMARK 465 GLY B -18 REMARK 465 SER B -17 REMARK 465 HIS B -16 REMARK 465 MET B -15 REMARK 465 ALA B -14 REMARK 465 SER B -13 REMARK 465 MET B -12 REMARK 465 THR B -11 REMARK 465 GLY B -10 REMARK 465 GLY B -9 REMARK 465 GLN B -8 REMARK 465 GLN B -7 REMARK 465 MET B -6 REMARK 465 GLY B -5 REMARK 465 ARG B -4 REMARK 465 GLY B -3 REMARK 465 SER B -2 REMARK 465 GLU B -1 REMARK 465 PHE B 0 REMARK 465 MET B 1 REMARK 465 SER B 2 REMARK 465 GLN B 3 REMARK 465 GLY B 74 REMARK 465 PRO B 75 REMARK 465 VAL B 76 REMARK 465 LEU B 77 REMARK 465 ALA B 78 REMARK 465 GLN B 79 REMARK 465 MET B 80 REMARK 465 HIS B 81 REMARK 465 GLY B 82 REMARK 465 LYS B 83 REMARK 465 GLU B 84 REMARK 465 HIS B 85 REMARK 465 ALA B 405 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 ILE A 5 CG1 CG2 CD1 REMARK 470 LYS A 6 CG CD CE NZ REMARK 470 SER B 4 OG REMARK 470 ILE B 5 CG1 CG2 CD1 REMARK 470 LYS B 6 CG CD CE NZ REMARK 470 LEU B 7 CG CD1 CD2 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 PRO B 19 C - N - CD ANGL. DEV. = -16.5 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 LYS A 6 91.33 -68.12 REMARK 500 VAL A 10 21.02 -79.58 REMARK 500 ASN A 18 85.19 -171.00 REMARK 500 LEU A 64 4.82 -64.63 REMARK 500 GLU A 66 -72.77 -139.44 REMARK 500 THR A 235 -61.34 -98.74 REMARK 500 ASP A 301 -6.49 78.93 REMARK 500 GLN A 320 56.72 39.25 REMARK 500 ASN A 376 30.17 74.18 REMARK 500 LEU A 390 -34.88 -138.13 REMARK 500 SER A 397 157.11 176.16 REMARK 500 ILE B 5 -158.99 -178.11 REMARK 500 TYR B 20 3.35 -69.78 REMARK 500 MET B 72 -133.21 -108.45 REMARK 500 ALA B 87 22.82 -73.81 REMARK 500 LYS B 88 69.46 -100.26 REMARK 500 ILE B 91 -53.81 127.69 REMARK 500 GLU B 212 -81.04 -97.45 REMARK 500 TYR B 213 -53.84 71.21 REMARK 500 MET B 216 -73.34 -89.42 REMARK 500 ASP B 301 -5.18 80.31 REMARK 500 ASP B 382 15.99 58.47 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 A 406 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 353 SG REMARK 620 2 HEM A 406 NA 98.4 REMARK 620 3 HEM A 406 NB 86.6 87.6 REMARK 620 4 HEM A 406 NC 80.3 177.6 90.3 REMARK 620 5 HEM A 406 ND 93.1 91.6 179.1 90.5 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HEM B 406 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS B 353 SG REMARK 620 2 HEM B 406 NA 100.1 REMARK 620 3 HEM B 406 NB 97.6 89.2 REMARK 620 4 HEM B 406 NC 82.8 176.4 88.3 REMARK 620 5 HEM B 406 ND 85.0 91.2 177.2 91.1 REMARK 620 N 1 2 3 4 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 406 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 406 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PIW A 407 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PIW B 407 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3NC3 RELATED DB: PDB REMARK 900 RELATED ID: 3NC5 RELATED DB: PDB REMARK 900 RELATED ID: 3NC7 RELATED DB: PDB DBREF 3NC6 A 1 405 UNP O34926 CYPX_BACSU 1 405 DBREF 3NC6 B 1 405 UNP O34926 CYPX_BACSU 1 405 SEQADV 3NC6 MET A -35 UNP O34926 EXPRESSION TAG SEQADV 3NC6 GLY A -34 UNP O34926 EXPRESSION TAG SEQADV 3NC6 SER A -33 UNP O34926 EXPRESSION TAG SEQADV 3NC6 SER A -32 UNP O34926 EXPRESSION TAG SEQADV 3NC6 HIS A -31 UNP O34926 EXPRESSION TAG SEQADV 3NC6 HIS A -30 UNP O34926 EXPRESSION TAG SEQADV 3NC6 HIS A -29 UNP O34926 EXPRESSION TAG SEQADV 3NC6 HIS A -28 UNP O34926 EXPRESSION TAG SEQADV 3NC6 HIS A -27 UNP O34926 EXPRESSION TAG SEQADV 3NC6 HIS A -26 UNP O34926 EXPRESSION TAG SEQADV 3NC6 SER A -25 UNP O34926 EXPRESSION TAG SEQADV 3NC6 SER A -24 UNP O34926 EXPRESSION TAG SEQADV 3NC6 GLY A -23 UNP O34926 EXPRESSION TAG SEQADV 3NC6 LEU A -22 UNP O34926 EXPRESSION TAG SEQADV 3NC6 VAL A -21 UNP O34926 EXPRESSION TAG SEQADV 3NC6 PRO A -20 UNP O34926 EXPRESSION TAG SEQADV 3NC6 ARG A -19 UNP O34926 EXPRESSION TAG SEQADV 3NC6 GLY A -18 UNP O34926 EXPRESSION TAG SEQADV 3NC6 SER A -17 UNP O34926 EXPRESSION TAG SEQADV 3NC6 HIS A -16 UNP O34926 EXPRESSION TAG SEQADV 3NC6 MET A -15 UNP O34926 EXPRESSION TAG SEQADV 3NC6 ALA A -14 UNP O34926 EXPRESSION TAG SEQADV 3NC6 SER A -13 UNP O34926 EXPRESSION TAG SEQADV 3NC6 MET A -12 UNP O34926 EXPRESSION TAG SEQADV 3NC6 THR A -11 UNP O34926 EXPRESSION TAG SEQADV 3NC6 GLY A -10 UNP O34926 EXPRESSION TAG SEQADV 3NC6 GLY A -9 UNP O34926 EXPRESSION TAG SEQADV 3NC6 GLN A -8 UNP O34926 EXPRESSION TAG SEQADV 3NC6 GLN A -7 UNP O34926 EXPRESSION TAG SEQADV 3NC6 MET A -6 UNP O34926 EXPRESSION TAG SEQADV 3NC6 GLY A -5 UNP O34926 EXPRESSION TAG SEQADV 3NC6 ARG A -4 UNP O34926 EXPRESSION TAG SEQADV 3NC6 GLY A -3 UNP O34926 EXPRESSION TAG SEQADV 3NC6 SER A -2 UNP O34926 EXPRESSION TAG SEQADV 3NC6 GLU A -1 UNP O34926 EXPRESSION TAG SEQADV 3NC6 PHE A 0 UNP O34926 EXPRESSION TAG SEQADV 3NC6 THR A 356 UNP O34926 ALA 356 ENGINEERED MUTATION SEQADV 3NC6 MET B -35 UNP O34926 EXPRESSION TAG SEQADV 3NC6 GLY B -34 UNP O34926 EXPRESSION TAG SEQADV 3NC6 SER B -33 UNP O34926 EXPRESSION TAG SEQADV 3NC6 SER B -32 UNP O34926 EXPRESSION TAG SEQADV 3NC6 HIS B -31 UNP O34926 EXPRESSION TAG SEQADV 3NC6 HIS B -30 UNP O34926 EXPRESSION TAG SEQADV 3NC6 HIS B -29 UNP O34926 EXPRESSION TAG SEQADV 3NC6 HIS B -28 UNP O34926 EXPRESSION TAG SEQADV 3NC6 HIS B -27 UNP O34926 EXPRESSION TAG SEQADV 3NC6 HIS B -26 UNP O34926 EXPRESSION TAG SEQADV 3NC6 SER B -25 UNP O34926 EXPRESSION TAG SEQADV 3NC6 SER B -24 UNP O34926 EXPRESSION TAG SEQADV 3NC6 GLY B -23 UNP O34926 EXPRESSION TAG SEQADV 3NC6 LEU B -22 UNP O34926 EXPRESSION TAG SEQADV 3NC6 VAL B -21 UNP O34926 EXPRESSION TAG SEQADV 3NC6 PRO B -20 UNP O34926 EXPRESSION TAG SEQADV 3NC6 ARG B -19 UNP O34926 EXPRESSION TAG SEQADV 3NC6 GLY B -18 UNP O34926 EXPRESSION TAG SEQADV 3NC6 SER B -17 UNP O34926 EXPRESSION TAG SEQADV 3NC6 HIS B -16 UNP O34926 EXPRESSION TAG SEQADV 3NC6 MET B -15 UNP O34926 EXPRESSION TAG SEQADV 3NC6 ALA B -14 UNP O34926 EXPRESSION TAG SEQADV 3NC6 SER B -13 UNP O34926 EXPRESSION TAG SEQADV 3NC6 MET B -12 UNP O34926 EXPRESSION TAG SEQADV 3NC6 THR B -11 UNP O34926 EXPRESSION TAG SEQADV 3NC6 GLY B -10 UNP O34926 EXPRESSION TAG SEQADV 3NC6 GLY B -9 UNP O34926 EXPRESSION TAG SEQADV 3NC6 GLN B -8 UNP O34926 EXPRESSION TAG SEQADV 3NC6 GLN B -7 UNP O34926 EXPRESSION TAG SEQADV 3NC6 MET B -6 UNP O34926 EXPRESSION TAG SEQADV 3NC6 GLY B -5 UNP O34926 EXPRESSION TAG SEQADV 3NC6 ARG B -4 UNP O34926 EXPRESSION TAG SEQADV 3NC6 GLY B -3 UNP O34926 EXPRESSION TAG SEQADV 3NC6 SER B -2 UNP O34926 EXPRESSION TAG SEQADV 3NC6 GLU B -1 UNP O34926 EXPRESSION TAG SEQADV 3NC6 PHE B 0 UNP O34926 EXPRESSION TAG SEQADV 3NC6 THR B 356 UNP O34926 ALA 356 ENGINEERED MUTATION SEQRES 1 A 441 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY SEQRES 2 A 441 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY SEQRES 3 A 441 GLY GLN GLN MET GLY ARG GLY SER GLU PHE MET SER GLN SEQRES 4 A 441 SER ILE LYS LEU PHE SER VAL LEU SER ASP GLN PHE GLN SEQRES 5 A 441 ASN ASN PRO TYR ALA TYR PHE SER GLN LEU ARG GLU GLU SEQRES 6 A 441 ASP PRO VAL HIS TYR GLU GLU SER ILE ASP SER TYR PHE SEQRES 7 A 441 ILE SER ARG TYR HIS ASP VAL ARG TYR ILE LEU GLN HIS SEQRES 8 A 441 PRO ASP ILE PHE THR THR LYS SER LEU VAL GLU ARG ALA SEQRES 9 A 441 GLU PRO VAL MET ARG GLY PRO VAL LEU ALA GLN MET HIS SEQRES 10 A 441 GLY LYS GLU HIS SER ALA LYS ARG ARG ILE VAL VAL ARG SEQRES 11 A 441 SER PHE ILE GLY ASP ALA LEU ASP HIS LEU SER PRO LEU SEQRES 12 A 441 ILE LYS GLN ASN ALA GLU ASN LEU LEU ALA PRO TYR LEU SEQRES 13 A 441 GLU ARG GLY LYS SER ASP LEU VAL ASN ASP PHE GLY LYS SEQRES 14 A 441 THR PHE ALA VAL CYS VAL THR MET ASP MET LEU GLY LEU SEQRES 15 A 441 ASP LYS ARG ASP HIS GLU LYS ILE SER GLU TRP HIS SER SEQRES 16 A 441 GLY VAL ALA ASP PHE ILE THR SER ILE SER GLN SER PRO SEQRES 17 A 441 GLU ALA ARG ALA HIS SER LEU TRP CYS SER GLU GLN LEU SEQRES 18 A 441 SER GLN TYR LEU MET PRO VAL ILE LYS GLU ARG ARG VAL SEQRES 19 A 441 ASN PRO GLY SER ASP LEU ILE SER ILE LEU CYS THR SER SEQRES 20 A 441 GLU TYR GLU GLY MET ALA LEU SER ASP LYS ASP ILE LEU SEQRES 21 A 441 ALA LEU ILE LEU ASN VAL LEU LEU ALA ALA THR GLU PRO SEQRES 22 A 441 ALA ASP LYS THR LEU ALA LEU MET ILE TYR HIS LEU LEU SEQRES 23 A 441 ASN ASN PRO GLU GLN MET ASN ASP VAL LEU ALA ASP ARG SEQRES 24 A 441 SER LEU VAL PRO ARG ALA ILE ALA GLU THR LEU ARG TYR SEQRES 25 A 441 LYS PRO PRO VAL GLN LEU ILE PRO ARG GLN LEU SER GLN SEQRES 26 A 441 ASP THR VAL VAL GLY GLY MET GLU ILE LYS LYS ASP THR SEQRES 27 A 441 ILE VAL PHE CYS MET ILE GLY ALA ALA ASN ARG ASP PRO SEQRES 28 A 441 GLU ALA PHE GLU GLN PRO ASP VAL PHE ASN ILE HIS ARG SEQRES 29 A 441 GLU ASP LEU GLY ILE LYS SER ALA PHE SER GLY ALA ALA SEQRES 30 A 441 ARG HIS LEU ALA PHE GLY SER GLY ILE HIS ASN CYS VAL SEQRES 31 A 441 GLY THR ALA PHE ALA LYS ASN GLU ILE GLU ILE VAL ALA SEQRES 32 A 441 ASN ILE VAL LEU ASP LYS MET ARG ASN ILE ARG LEU GLU SEQRES 33 A 441 GLU ASP PHE CYS TYR ALA GLU SER GLY LEU TYR THR ARG SEQRES 34 A 441 GLY PRO VAL SER LEU LEU VAL ALA PHE ASP GLY ALA SEQRES 1 B 441 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY SEQRES 2 B 441 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY SEQRES 3 B 441 GLY GLN GLN MET GLY ARG GLY SER GLU PHE MET SER GLN SEQRES 4 B 441 SER ILE LYS LEU PHE SER VAL LEU SER ASP GLN PHE GLN SEQRES 5 B 441 ASN ASN PRO TYR ALA TYR PHE SER GLN LEU ARG GLU GLU SEQRES 6 B 441 ASP PRO VAL HIS TYR GLU GLU SER ILE ASP SER TYR PHE SEQRES 7 B 441 ILE SER ARG TYR HIS ASP VAL ARG TYR ILE LEU GLN HIS SEQRES 8 B 441 PRO ASP ILE PHE THR THR LYS SER LEU VAL GLU ARG ALA SEQRES 9 B 441 GLU PRO VAL MET ARG GLY PRO VAL LEU ALA GLN MET HIS SEQRES 10 B 441 GLY LYS GLU HIS SER ALA LYS ARG ARG ILE VAL VAL ARG SEQRES 11 B 441 SER PHE ILE GLY ASP ALA LEU ASP HIS LEU SER PRO LEU SEQRES 12 B 441 ILE LYS GLN ASN ALA GLU ASN LEU LEU ALA PRO TYR LEU SEQRES 13 B 441 GLU ARG GLY LYS SER ASP LEU VAL ASN ASP PHE GLY LYS SEQRES 14 B 441 THR PHE ALA VAL CYS VAL THR MET ASP MET LEU GLY LEU SEQRES 15 B 441 ASP LYS ARG ASP HIS GLU LYS ILE SER GLU TRP HIS SER SEQRES 16 B 441 GLY VAL ALA ASP PHE ILE THR SER ILE SER GLN SER PRO SEQRES 17 B 441 GLU ALA ARG ALA HIS SER LEU TRP CYS SER GLU GLN LEU SEQRES 18 B 441 SER GLN TYR LEU MET PRO VAL ILE LYS GLU ARG ARG VAL SEQRES 19 B 441 ASN PRO GLY SER ASP LEU ILE SER ILE LEU CYS THR SER SEQRES 20 B 441 GLU TYR GLU GLY MET ALA LEU SER ASP LYS ASP ILE LEU SEQRES 21 B 441 ALA LEU ILE LEU ASN VAL LEU LEU ALA ALA THR GLU PRO SEQRES 22 B 441 ALA ASP LYS THR LEU ALA LEU MET ILE TYR HIS LEU LEU SEQRES 23 B 441 ASN ASN PRO GLU GLN MET ASN ASP VAL LEU ALA ASP ARG SEQRES 24 B 441 SER LEU VAL PRO ARG ALA ILE ALA GLU THR LEU ARG TYR SEQRES 25 B 441 LYS PRO PRO VAL GLN LEU ILE PRO ARG GLN LEU SER GLN SEQRES 26 B 441 ASP THR VAL VAL GLY GLY MET GLU ILE LYS LYS ASP THR SEQRES 27 B 441 ILE VAL PHE CYS MET ILE GLY ALA ALA ASN ARG ASP PRO SEQRES 28 B 441 GLU ALA PHE GLU GLN PRO ASP VAL PHE ASN ILE HIS ARG SEQRES 29 B 441 GLU ASP LEU GLY ILE LYS SER ALA PHE SER GLY ALA ALA SEQRES 30 B 441 ARG HIS LEU ALA PHE GLY SER GLY ILE HIS ASN CYS VAL SEQRES 31 B 441 GLY THR ALA PHE ALA LYS ASN GLU ILE GLU ILE VAL ALA SEQRES 32 B 441 ASN ILE VAL LEU ASP LYS MET ARG ASN ILE ARG LEU GLU SEQRES 33 B 441 GLU ASP PHE CYS TYR ALA GLU SER GLY LEU TYR THR ARG SEQRES 34 B 441 GLY PRO VAL SER LEU LEU VAL ALA PHE ASP GLY ALA HET HEM A 406 43 HET PIW A 407 11 HET MG A 408 1 HET HEM B 406 43 HET PIW B 407 11 HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETNAM PIW 1-PHENYL-1H-IMIDAZOLE HETNAM MG MAGNESIUM ION HETSYN HEM HEME FORMUL 3 HEM 2(C34 H32 FE N4 O4) FORMUL 4 PIW 2(C9 H8 N2) FORMUL 5 MG MG 2+ FORMUL 8 HOH *5(H2 O) HELIX 1 1 SER A 12 ASN A 17 1 6 HELIX 2 2 ASN A 18 ALA A 21 5 4 HELIX 3 3 TYR A 22 ASP A 30 1 9 HELIX 4 4 ARG A 45 GLN A 54 1 10 HELIX 5 5 ARG A 89 ALA A 117 1 29 HELIX 6 6 PRO A 118 LEU A 120 5 3 HELIX 7 7 PHE A 131 GLY A 145 1 15 HELIX 8 8 ASP A 147 ARG A 149 5 3 HELIX 9 9 ASP A 150 SER A 167 1 18 HELIX 10 10 SER A 171 ASN A 199 1 29 HELIX 11 11 ASP A 203 CYS A 209 1 7 HELIX 12 12 SER A 219 ASN A 252 1 34 HELIX 13 13 ASN A 252 ASP A 262 1 11 HELIX 14 14 LEU A 265 LYS A 277 1 13 HELIX 15 15 ILE A 308 ARG A 313 1 6 HELIX 16 16 GLY A 355 MET A 374 1 20 HELIX 17 17 SER B 12 ASN B 18 1 7 HELIX 18 18 TYR B 22 ASP B 30 1 9 HELIX 19 19 ARG B 45 GLN B 54 1 10 HELIX 20 20 SER B 63 ALA B 68 1 6 HELIX 21 21 VAL B 92 LEU B 104 1 13 HELIX 22 22 LEU B 104 ALA B 117 1 14 HELIX 23 23 PRO B 118 LEU B 120 5 3 HELIX 24 24 PHE B 131 GLY B 145 1 15 HELIX 25 25 ASP B 147 ARG B 149 5 3 HELIX 26 26 ASP B 150 SER B 167 1 18 HELIX 27 27 SER B 171 ASN B 199 1 29 HELIX 28 28 ASP B 203 SER B 211 1 9 HELIX 29 29 SER B 219 ASN B 251 1 33 HELIX 30 30 ASN B 252 ALA B 261 1 10 HELIX 31 31 LEU B 265 LYS B 277 1 13 HELIX 32 32 ILE B 308 ARG B 313 1 6 HELIX 33 33 ARG B 328 ALA B 336 5 9 HELIX 34 34 SER B 348 ASN B 352 5 5 HELIX 35 35 GLY B 355 MET B 374 1 20 SHEET 1 A 4 VAL A 32 TYR A 34 0 SHEET 2 A 4 SER A 40 ILE A 43 -1 O PHE A 42 N HIS A 33 SHEET 3 A 4 ILE A 303 MET A 307 1 O PHE A 305 N TYR A 41 SHEET 4 A 4 LEU A 282 GLN A 286 -1 N ARG A 285 O VAL A 304 SHEET 1 B 3 LYS A 124 ASP A 126 0 SHEET 2 B 3 LEU A 399 ALA A 401 -1 O VAL A 400 N SER A 125 SHEET 3 B 3 ARG A 378 LEU A 379 -1 N ARG A 378 O ALA A 401 SHEET 1 C 2 THR A 291 VAL A 292 0 SHEET 2 C 2 GLU A 297 ILE A 298 -1 O ILE A 298 N THR A 291 SHEET 1 D 2 GLU A 387 GLY A 389 0 SHEET 2 D 2 ARG A 393 PRO A 395 -1 O GLY A 394 N SER A 388 SHEET 1 E 5 VAL B 32 GLU B 35 0 SHEET 2 E 5 SER B 40 ILE B 43 -1 O PHE B 42 N HIS B 33 SHEET 3 E 5 ILE B 303 MET B 307 1 O PHE B 305 N TYR B 41 SHEET 4 E 5 LEU B 282 LEU B 287 -1 N ARG B 285 O VAL B 304 SHEET 5 E 5 PHE B 59 THR B 60 -1 N THR B 60 O GLN B 286 SHEET 1 F 3 LYS B 124 ASP B 126 0 SHEET 2 F 3 LEU B 399 ALA B 401 -1 O VAL B 400 N SER B 125 SHEET 3 F 3 ARG B 378 LEU B 379 -1 N ARG B 378 O ALA B 401 SHEET 1 G 2 THR B 291 VAL B 293 0 SHEET 2 G 2 MET B 296 ILE B 298 -1 O ILE B 298 N THR B 291 SHEET 1 H 2 GLU B 387 SER B 388 0 SHEET 2 H 2 GLY B 394 PRO B 395 -1 O GLY B 394 N SER B 388 LINK SG CYS A 353 FE HEM A 406 1555 1555 2.49 LINK SG CYS B 353 FE HEM B 406 1555 1555 2.17 CISPEP 1 ILE B 5 LYS B 6 0 -15.01 CISPEP 2 ARG B 90 ILE B 91 0 16.88 SITE 1 AC1 20 SER A 63 LEU A 64 ILE A 97 MET A 143 SITE 2 AC1 20 ASN A 229 ALA A 233 ALA A 234 PRO A 237 SITE 3 AC1 20 THR A 241 VAL A 280 ILE A 283 ARG A 285 SITE 4 AC1 20 ALA A 345 PHE A 346 HIS A 351 CYS A 353 SITE 5 AC1 20 VAL A 354 GLY A 355 PHE A 358 PIW A 407 SITE 1 AC2 18 SER B 63 LEU B 64 ILE B 97 ASN B 229 SITE 2 AC2 18 ALA B 233 ALA B 234 PRO B 237 THR B 241 SITE 3 AC2 18 ILE B 283 ARG B 285 ALA B 345 PHE B 346 SITE 4 AC2 18 HIS B 351 CYS B 353 GLY B 355 PHE B 358 SITE 5 AC2 18 GLU B 362 PIW B 407 SITE 1 AC3 4 LEU A 64 LEU A 232 GLU A 236 HEM A 406 SITE 1 AC4 4 LEU B 64 GLU B 236 THR B 392 HEM B 406 CRYST1 64.950 106.900 142.930 90.00 90.00 90.00 P 21 21 21 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.015396 0.000000 0.000000 0.00000 SCALE2 0.000000 0.009355 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006996 0.00000 (ATOM LINES ARE NOT SHOWN.) END
HEADER OXIDOREDUCTASE 04-JUN-10 3NC7 TITLE CYP134A1 2-PHENYLIMIDAZOLE BOUND STRUCTURE COMPND MOL_ID: 1; COMPND 2 MOLECULE: CYTOCHROME P450 CYPX; COMPND 3 CHAIN: A, B; COMPND 4 EC: 1.14.-.-; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS; SOURCE 3 ORGANISM_TAXID: 1423; SOURCE 4 STRAIN: 168; SOURCE 5 GENE: BSU35060, CYP134, CYPB, CYPX; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A(+) KEYWDS CYTOCHROME P450 OXIDASE, HAEM PROTEIN, OXIDOREDUCTASE EXPDTA X-RAY DIFFRACTION AUTHOR M.J.CRYLE,I.SCHLICHTING REVDAT 3 21-FEB-24 3NC7 1 REMARK SEQADV LINK REVDAT 2 22-SEP-10 3NC7 1 JRNL REVDAT 1 11-AUG-10 3NC7 0 JRNL AUTH M.J.CRYLE,S.G.BELL,I.SCHLICHTING JRNL TITL STRUCTURAL AND BIOCHEMICAL CHARACTERIZATION OF THE JRNL TITL 2 CYTOCHROME P450 CYPX (CYP134A1) FROM BACILLUS SUBTILIS: A JRNL TITL 3 CYCLO-L-LEUCYL-L-LEUCYL DIPEPTIDE OXIDASE. JRNL REF BIOCHEMISTRY V. 49 7282 2010 JRNL REFN ISSN 0006-2960 JRNL PMID 20690619 JRNL DOI 10.1021/BI100910Y REMARK 2 REMARK 2 RESOLUTION. 3.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.5.0070 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.55 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 15206 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 + TEST SET) : 0.215 REMARK 3 R VALUE (WORKING SET) : 0.211 REMARK 3 FREE R VALUE : 0.286 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900 REMARK 3 FREE R VALUE TEST SET COUNT : 751 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.30 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.39 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1047 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0 REMARK 3 BIN R VALUE (WORKING SET) : 0.2410 REMARK 3 BIN FREE R VALUE SET COUNT : 56 REMARK 3 BIN FREE R VALUE : 0.3290 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6021 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 110 REMARK 3 SOLVENT ATOMS : 2 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 55.90 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.11 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.03000 REMARK 3 B22 (A**2) : 0.65000 REMARK 3 B33 (A**2) : -0.62000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 0.626 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.486 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 58.921 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.916 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.850 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6270 ; 0.010 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8523 ; 1.253 ; 2.012 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 759 ; 5.925 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 293 ;34.353 ;24.061 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1060 ;17.802 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 45 ;18.369 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 944 ; 0.085 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4777 ; 0.006 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3815 ; 0.232 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6167 ; 0.468 ; 2.000 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2455 ; 0.780 ; 3.000 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2355 ; 1.409 ; 4.500 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 2 REMARK 3 REMARK 3 NCS GROUP NUMBER : 1 REMARK 3 CHAIN NAMES : A B REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 A 4 A 404 4 REMARK 3 1 B 4 B 404 4 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 MEDIUM POSITIONAL 1 A (A): 2982 ; 0.660 ; 0.500 REMARK 3 MEDIUM THERMAL 1 A (A**2): 2982 ; 0.300 ; 2.000 REMARK 3 REMARK 3 NCS GROUP NUMBER : 2 REMARK 3 CHAIN NAMES : A B REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 C 1 A 406 4 REMARK 3 1 D 1 B 406 4 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 MEDIUM POSITIONAL 2 A (A): 43 ; 0.360 ; 0.500 REMARK 3 MEDIUM THERMAL 2 A (A**2): 43 ; 0.600 ; 2.000 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 10 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 5 A 57 REMARK 3 ORIGIN FOR THE GROUP (A): 13.3781 -10.2119 -7.4582 REMARK 3 T TENSOR REMARK 3 T11: 0.2628 T22: 0.8515 REMARK 3 T33: 0.2651 T12: -0.1132 REMARK 3 T13: 0.0983 T23: -0.1580 REMARK 3 L TENSOR REMARK 3 L11: 7.6722 L22: 9.1505 REMARK 3 L33: 4.0745 L12: -1.1856 REMARK 3 L13: 2.1487 L23: -0.5148 REMARK 3 S TENSOR REMARK 3 S11: -0.3619 S12: 0.0899 S13: 0.1721 REMARK 3 S21: 0.1220 S22: 0.1648 S23: 1.0312 REMARK 3 S31: 0.4201 S32: -1.3515 S33: 0.1970 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 58 A 107 REMARK 3 ORIGIN FOR THE GROUP (A): 31.7932 -27.2083 -12.7890 REMARK 3 T TENSOR REMARK 3 T11: 0.7568 T22: 0.6923 REMARK 3 T33: 0.8228 T12: 0.0087 REMARK 3 T13: 0.1110 T23: 0.1536 REMARK 3 L TENSOR REMARK 3 L11: 5.1786 L22: 6.8671 REMARK 3 L33: 2.9388 L12: 4.7089 REMARK 3 L13: -2.3718 L23: 0.0159 REMARK 3 S TENSOR REMARK 3 S11: 0.0809 S12: 0.2247 S13: -0.3384 REMARK 3 S21: 0.1923 S22: -0.3114 S23: -0.0333 REMARK 3 S31: 0.0684 S32: -0.5342 S33: 0.2305 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 108 A 200 REMARK 3 ORIGIN FOR THE GROUP (A): 38.3086 -16.1711 -25.7741 REMARK 3 T TENSOR REMARK 3 T11: 0.1658 T22: 0.3532 REMARK 3 T33: 0.0209 T12: 0.0604 REMARK 3 T13: 0.0097 T23: 0.0403 REMARK 3 L TENSOR REMARK 3 L11: 3.7849 L22: 3.1041 REMARK 3 L33: 3.0636 L12: 0.1817 REMARK 3 L13: 1.2086 L23: 2.1631 REMARK 3 S TENSOR REMARK 3 S11: 0.1762 S12: 0.4514 S13: -0.1396 REMARK 3 S21: -0.3744 S22: -0.0397 S23: -0.0729 REMARK 3 S31: 0.0887 S32: 0.0342 S33: -0.1364 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 201 A 296 REMARK 3 ORIGIN FOR THE GROUP (A): 32.3134 -15.0218 -9.9718 REMARK 3 T TENSOR REMARK 3 T11: 0.2261 T22: 0.2402 REMARK 3 T33: 0.0965 T12: -0.0115 REMARK 3 T13: 0.0261 T23: 0.0184 REMARK 3 L TENSOR REMARK 3 L11: 3.3257 L22: 4.1549 REMARK 3 L33: 3.5094 L12: -0.1463 REMARK 3 L13: -0.5424 L23: 2.2306 REMARK 3 S TENSOR REMARK 3 S11: -0.0306 S12: 0.0189 S13: -0.5245 REMARK 3 S21: 0.1828 S22: -0.1309 S23: 0.2146 REMARK 3 S31: 0.5538 S32: -0.2473 S33: 0.1615 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 297 A 403 REMARK 3 ORIGIN FOR THE GROUP (A): 31.9124 -8.0631 -6.1811 REMARK 3 T TENSOR REMARK 3 T11: 0.1291 T22: 0.1637 REMARK 3 T33: 0.0107 T12: -0.0083 REMARK 3 T13: 0.0279 T23: -0.0148 REMARK 3 L TENSOR REMARK 3 L11: 6.4400 L22: 4.9924 REMARK 3 L33: 4.6707 L12: 0.2995 REMARK 3 L13: -1.3220 L23: 0.4633 REMARK 3 S TENSOR REMARK 3 S11: 0.1486 S12: -0.1237 S13: -0.0514 REMARK 3 S21: 0.5516 S22: -0.1692 S23: 0.1838 REMARK 3 S31: 0.2634 S32: -0.2521 S33: 0.0206 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 6 B 101 REMARK 3 ORIGIN FOR THE GROUP (A): 46.0787 8.1548 19.1412 REMARK 3 T TENSOR REMARK 3 T11: 0.2843 T22: 0.4948 REMARK 3 T33: 0.0569 T12: -0.0114 REMARK 3 T13: 0.0357 T23: -0.0345 REMARK 3 L TENSOR REMARK 3 L11: 4.8072 L22: 1.4800 REMARK 3 L33: 3.9352 L12: -0.1381 REMARK 3 L13: -0.6473 L23: 0.4500 REMARK 3 S TENSOR REMARK 3 S11: 0.0361 S12: -0.1910 S13: -0.1913 REMARK 3 S21: 0.1503 S22: -0.0488 S23: -0.1777 REMARK 3 S31: 0.0676 S32: 0.5354 S33: 0.0126 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 102 B 167 REMARK 3 ORIGIN FOR THE GROUP (A): 21.8322 11.8644 31.3775 REMARK 3 T TENSOR REMARK 3 T11: 0.1786 T22: 0.2333 REMARK 3 T33: 0.0406 T12: 0.0173 REMARK 3 T13: 0.0270 T23: -0.0270 REMARK 3 L TENSOR REMARK 3 L11: 6.4980 L22: 4.1494 REMARK 3 L33: 4.4434 L12: -2.9959 REMARK 3 L13: 1.6352 L23: -1.1502 REMARK 3 S TENSOR REMARK 3 S11: 0.0011 S12: -0.2802 S13: 0.3102 REMARK 3 S21: 0.1651 S22: 0.1496 S23: 0.0101 REMARK 3 S31: -0.0418 S32: -0.3623 S33: -0.1508 REMARK 3 REMARK 3 TLS GROUP : 8 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 168 B 290 REMARK 3 ORIGIN FOR THE GROUP (A): 30.8932 6.5613 26.2923 REMARK 3 T TENSOR REMARK 3 T11: 0.0710 T22: 0.2208 REMARK 3 T33: 0.0469 T12: -0.0115 REMARK 3 T13: -0.0253 T23: -0.0020 REMARK 3 L TENSOR REMARK 3 L11: 2.2801 L22: 1.5408 REMARK 3 L33: 3.8327 L12: 0.5259 REMARK 3 L13: -0.6558 L23: -0.3323 REMARK 3 S TENSOR REMARK 3 S11: 0.1565 S12: -0.1517 S13: -0.2157 REMARK 3 S21: -0.0922 S22: 0.0543 S23: 0.0257 REMARK 3 S31: 0.0888 S32: 0.0015 S33: -0.2108 REMARK 3 REMARK 3 TLS GROUP : 9 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 291 B 391 REMARK 3 ORIGIN FOR THE GROUP (A): 34.7701 14.0831 14.2204 REMARK 3 T TENSOR REMARK 3 T11: 0.1515 T22: 0.1948 REMARK 3 T33: 0.0185 T12: -0.0073 REMARK 3 T13: 0.0385 T23: 0.0111 REMARK 3 L TENSOR REMARK 3 L11: 6.2614 L22: 3.5612 REMARK 3 L33: 3.0769 L12: -0.3094 REMARK 3 L13: -0.3443 L23: 0.1325 REMARK 3 S TENSOR REMARK 3 S11: 0.1242 S12: 0.0391 S13: 0.1959 REMARK 3 S21: -0.4894 S22: 0.0103 S23: -0.0845 REMARK 3 S31: -0.2383 S32: 0.3234 S33: -0.1346 REMARK 3 REMARK 3 TLS GROUP : 10 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 392 B 404 REMARK 3 ORIGIN FOR THE GROUP (A): 31.5395 21.6667 25.8510 REMARK 3 T TENSOR REMARK 3 T11: 0.2373 T22: 0.3360 REMARK 3 T33: 0.1822 T12: -0.0617 REMARK 3 T13: 0.1308 T23: 0.0625 REMARK 3 L TENSOR REMARK 3 L11: 8.2478 L22: 6.2696 REMARK 3 L33: 8.0298 L12: -6.9519 REMARK 3 L13: -2.0513 L23: 3.4612 REMARK 3 S TENSOR REMARK 3 S11: -0.4428 S12: -0.7823 S13: -0.1607 REMARK 3 S21: 0.3536 S22: 0.8529 S23: 0.0535 REMARK 3 S31: -0.0722 S32: 0.6877 S33: -0.4101 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.40 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 3NC7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUN-10. REMARK 100 THE DEPOSITION ID IS D_1000059646. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 11-DEC-09 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SLS REMARK 200 BEAMLINE : X10SA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9790 REMARK 200 MONOCHROMATOR : SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS, XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15206 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300 REMARK 200 RESOLUTION RANGE LOW (A) : 47.670 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 95.8 REMARK 200 DATA REDUNDANCY : 4.800 REMARK 200 R MERGE (I) : 0.12000 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.39 REMARK 200 COMPLETENESS FOR SHELL (%) : 89.4 REMARK 200 DATA REDUNDANCY IN SHELL : 5.00 REMARK 200 R MERGE FOR SHELL (I) : 0.39000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.600 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD REMARK 200 SOFTWARE USED: SHARP REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.10 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS, 0.1 M MGCL2, 12% (W/V) REMARK 280 POLYETHYLENE GLYCOL-3350, PH 6.5, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 293K 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 32.18000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 71.04500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 53.39500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 71.04500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.18000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 53.39500 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 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: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A 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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: B 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 -35 REMARK 465 GLY A -34 REMARK 465 SER A -33 REMARK 465 SER A -32 REMARK 465 HIS A -31 REMARK 465 HIS A -30 REMARK 465 HIS A -29 REMARK 465 HIS A -28 REMARK 465 HIS A -27 REMARK 465 HIS A -26 REMARK 465 SER A -25 REMARK 465 SER A -24 REMARK 465 GLY A -23 REMARK 465 LEU A -22 REMARK 465 VAL A -21 REMARK 465 PRO A -20 REMARK 465 ARG A -19 REMARK 465 GLY A -18 REMARK 465 SER A -17 REMARK 465 HIS A -16 REMARK 465 MET A -15 REMARK 465 ALA A -14 REMARK 465 SER A -13 REMARK 465 MET A -12 REMARK 465 THR A -11 REMARK 465 GLY A -10 REMARK 465 GLY A -9 REMARK 465 GLN A -8 REMARK 465 GLN A -7 REMARK 465 MET A -6 REMARK 465 GLY A -5 REMARK 465 ARG A -4 REMARK 465 GLY A -3 REMARK 465 SER A -2 REMARK 465 GLU A -1 REMARK 465 PHE A 0 REMARK 465 MET A 1 REMARK 465 SER A 2 REMARK 465 GLN A 3 REMARK 465 SER A 4 REMARK 465 MET A 72 REMARK 465 ARG A 73 REMARK 465 GLY A 74 REMARK 465 PRO A 75 REMARK 465 VAL A 76 REMARK 465 LEU A 77 REMARK 465 ALA A 78 REMARK 465 GLN A 79 REMARK 465 MET A 80 REMARK 465 HIS A 81 REMARK 465 GLY A 82 REMARK 465 LYS A 83 REMARK 465 GLU A 84 REMARK 465 HIS A 85 REMARK 465 SER A 86 REMARK 465 GLU A 212 REMARK 465 TYR A 213 REMARK 465 GLU A 214 REMARK 465 GLY A 215 REMARK 465 MET A 216 REMARK 465 GLY A 404 REMARK 465 ALA A 405 REMARK 465 MET B -35 REMARK 465 GLY B -34 REMARK 465 SER B -33 REMARK 465 SER B -32 REMARK 465 HIS B -31 REMARK 465 HIS B -30 REMARK 465 HIS B -29 REMARK 465 HIS B -28 REMARK 465 HIS B -27 REMARK 465 HIS B -26 REMARK 465 SER B -25 REMARK 465 SER B -24 REMARK 465 GLY B -23 REMARK 465 LEU B -22 REMARK 465 VAL B -21 REMARK 465 PRO B -20 REMARK 465 ARG B -19 REMARK 465 GLY B -18 REMARK 465 SER B -17 REMARK 465 HIS B -16 REMARK 465 MET B -15 REMARK 465 ALA B -14 REMARK 465 SER B -13 REMARK 465 MET B -12 REMARK 465 THR B -11 REMARK 465 GLY B -10 REMARK 465 GLY B -9 REMARK 465 GLN B -8 REMARK 465 GLN B -7 REMARK 465 MET B -6 REMARK 465 GLY B -5 REMARK 465 ARG B -4 REMARK 465 GLY B -3 REMARK 465 SER B -2 REMARK 465 GLU B -1 REMARK 465 PHE B 0 REMARK 465 MET B 1 REMARK 465 SER B 2 REMARK 465 GLN B 3 REMARK 465 SER B 4 REMARK 465 ILE B 5 REMARK 465 PRO B 75 REMARK 465 VAL B 76 REMARK 465 LEU B 77 REMARK 465 ALA B 78 REMARK 465 GLN B 79 REMARK 465 MET B 80 REMARK 465 HIS B 81 REMARK 465 GLY B 82 REMARK 465 LYS B 83 REMARK 465 GLU B 84 REMARK 465 HIS B 85 REMARK 465 TYR B 213 REMARK 465 GLU B 214 REMARK 465 GLY B 215 REMARK 465 MET B 216 REMARK 465 ALA B 405 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 ILE A 5 CG1 CG2 CD1 REMARK 470 LYS A 6 CG CD CE NZ REMARK 470 LEU A 7 CG CD1 CD2 REMARK 470 LYS B 6 CG CD CE NZ REMARK 470 LEU B 7 CG CD1 CD2 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 ALA A 317 NH2 ARG A 342 2.13 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 PRO B 19 C - N - CD ANGL. DEV. = -15.0 DEGREES REMARK 500 VAL B 92 CB - CA - C ANGL. DEV. = -12.2 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 18 89.30 -177.10 REMARK 500 GLU A 28 -5.16 73.03 REMARK 500 GLU A 29 -53.43 -144.88 REMARK 500 ASP A 39 75.67 -103.05 REMARK 500 ARG A 67 141.10 -39.64 REMARK 500 PRO A 70 117.27 -34.97 REMARK 500 GLU A 121 -55.39 66.15 REMARK 500 PHE A 131 -54.26 -133.90 REMARK 500 ASP A 239 -66.87 -28.58 REMARK 500 SER A 288 -81.31 -64.02 REMARK 500 ASP A 322 33.66 -98.61 REMARK 500 CYS A 353 120.85 -32.63 REMARK 500 LEU B 7 59.26 -100.87 REMARK 500 ALA B 87 47.17 -85.40 REMARK 500 ARG B 89 34.89 -70.72 REMARK 500 VAL B 92 8.08 87.14 REMARK 500 VAL B 93 -43.46 -132.04 REMARK 500 PHE B 131 -71.05 -135.11 REMARK 500 LYS B 148 -9.51 -53.94 REMARK 500 GLU B 152 -79.83 -53.89 REMARK 500 LYS B 153 -63.40 -25.48 REMARK 500 SER B 211 179.86 173.93 REMARK 500 ALA B 238 -39.54 -39.33 REMARK 500 SER B 264 2.62 -65.67 REMARK 500 ASN B 376 56.48 70.58 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 MG A 408 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ALA A 136 O REMARK 620 2 GLU A 362 OE1 109.0 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HEM A 406 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 353 SG REMARK 620 2 HEM A 406 NA 103.0 REMARK 620 3 HEM A 406 NB 82.3 90.6 REMARK 620 4 HEM A 406 NC 78.6 174.8 84.7 REMARK 620 5 HEM A 406 ND 98.4 95.3 173.8 89.4 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MG B 408 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ALA B 136 O REMARK 620 2 GLU B 362 OE1 119.4 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HEM B 406 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS B 353 SG REMARK 620 2 HEM B 406 NA 111.6 REMARK 620 3 HEM B 406 NB 94.1 91.2 REMARK 620 4 HEM B 406 NC 80.3 167.9 85.5 REMARK 620 5 HEM B 406 ND 94.4 92.1 169.1 89.1 REMARK 620 N 1 2 3 4 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 406 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PIY A 407 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 408 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 406 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PIY B 407 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 408 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3NC3 RELATED DB: PDB REMARK 900 RELATED ID: 3NC5 RELATED DB: PDB REMARK 900 RELATED ID: 3NC6 RELATED DB: PDB DBREF 3NC7 A 1 405 UNP O34926 CYPX_BACSU 1 405 DBREF 3NC7 B 1 405 UNP O34926 CYPX_BACSU 1 405 SEQADV 3NC7 MET A -35 UNP O34926 EXPRESSION TAG SEQADV 3NC7 GLY A -34 UNP O34926 EXPRESSION TAG SEQADV 3NC7 SER A -33 UNP O34926 EXPRESSION TAG SEQADV 3NC7 SER A -32 UNP O34926 EXPRESSION TAG SEQADV 3NC7 HIS A -31 UNP O34926 EXPRESSION TAG SEQADV 3NC7 HIS A -30 UNP O34926 EXPRESSION TAG SEQADV 3NC7 HIS A -29 UNP O34926 EXPRESSION TAG SEQADV 3NC7 HIS A -28 UNP O34926 EXPRESSION TAG SEQADV 3NC7 HIS A -27 UNP O34926 EXPRESSION TAG SEQADV 3NC7 HIS A -26 UNP O34926 EXPRESSION TAG SEQADV 3NC7 SER A -25 UNP O34926 EXPRESSION TAG SEQADV 3NC7 SER A -24 UNP O34926 EXPRESSION TAG SEQADV 3NC7 GLY A -23 UNP O34926 EXPRESSION TAG SEQADV 3NC7 LEU A -22 UNP O34926 EXPRESSION TAG SEQADV 3NC7 VAL A -21 UNP O34926 EXPRESSION TAG SEQADV 3NC7 PRO A -20 UNP O34926 EXPRESSION TAG SEQADV 3NC7 ARG A -19 UNP O34926 EXPRESSION TAG SEQADV 3NC7 GLY A -18 UNP O34926 EXPRESSION TAG SEQADV 3NC7 SER A -17 UNP O34926 EXPRESSION TAG SEQADV 3NC7 HIS A -16 UNP O34926 EXPRESSION TAG SEQADV 3NC7 MET A -15 UNP O34926 EXPRESSION TAG SEQADV 3NC7 ALA A -14 UNP O34926 EXPRESSION TAG SEQADV 3NC7 SER A -13 UNP O34926 EXPRESSION TAG SEQADV 3NC7 MET A -12 UNP O34926 EXPRESSION TAG SEQADV 3NC7 THR A -11 UNP O34926 EXPRESSION TAG SEQADV 3NC7 GLY A -10 UNP O34926 EXPRESSION TAG SEQADV 3NC7 GLY A -9 UNP O34926 EXPRESSION TAG SEQADV 3NC7 GLN A -8 UNP O34926 EXPRESSION TAG SEQADV 3NC7 GLN A -7 UNP O34926 EXPRESSION TAG SEQADV 3NC7 MET A -6 UNP O34926 EXPRESSION TAG SEQADV 3NC7 GLY A -5 UNP O34926 EXPRESSION TAG SEQADV 3NC7 ARG A -4 UNP O34926 EXPRESSION TAG SEQADV 3NC7 GLY A -3 UNP O34926 EXPRESSION TAG SEQADV 3NC7 SER A -2 UNP O34926 EXPRESSION TAG SEQADV 3NC7 GLU A -1 UNP O34926 EXPRESSION TAG SEQADV 3NC7 PHE A 0 UNP O34926 EXPRESSION TAG SEQADV 3NC7 THR A 356 UNP O34926 ALA 356 ENGINEERED MUTATION SEQADV 3NC7 MET B -35 UNP O34926 EXPRESSION TAG SEQADV 3NC7 GLY B -34 UNP O34926 EXPRESSION TAG SEQADV 3NC7 SER B -33 UNP O34926 EXPRESSION TAG SEQADV 3NC7 SER B -32 UNP O34926 EXPRESSION TAG SEQADV 3NC7 HIS B -31 UNP O34926 EXPRESSION TAG SEQADV 3NC7 HIS B -30 UNP O34926 EXPRESSION TAG SEQADV 3NC7 HIS B -29 UNP O34926 EXPRESSION TAG SEQADV 3NC7 HIS B -28 UNP O34926 EXPRESSION TAG SEQADV 3NC7 HIS B -27 UNP O34926 EXPRESSION TAG SEQADV 3NC7 HIS B -26 UNP O34926 EXPRESSION TAG SEQADV 3NC7 SER B -25 UNP O34926 EXPRESSION TAG SEQADV 3NC7 SER B -24 UNP O34926 EXPRESSION TAG SEQADV 3NC7 GLY B -23 UNP O34926 EXPRESSION TAG SEQADV 3NC7 LEU B -22 UNP O34926 EXPRESSION TAG SEQADV 3NC7 VAL B -21 UNP O34926 EXPRESSION TAG SEQADV 3NC7 PRO B -20 UNP O34926 EXPRESSION TAG SEQADV 3NC7 ARG B -19 UNP O34926 EXPRESSION TAG SEQADV 3NC7 GLY B -18 UNP O34926 EXPRESSION TAG SEQADV 3NC7 SER B -17 UNP O34926 EXPRESSION TAG SEQADV 3NC7 HIS B -16 UNP O34926 EXPRESSION TAG SEQADV 3NC7 MET B -15 UNP O34926 EXPRESSION TAG SEQADV 3NC7 ALA B -14 UNP O34926 EXPRESSION TAG SEQADV 3NC7 SER B -13 UNP O34926 EXPRESSION TAG SEQADV 3NC7 MET B -12 UNP O34926 EXPRESSION TAG SEQADV 3NC7 THR B -11 UNP O34926 EXPRESSION TAG SEQADV 3NC7 GLY B -10 UNP O34926 EXPRESSION TAG SEQADV 3NC7 GLY B -9 UNP O34926 EXPRESSION TAG SEQADV 3NC7 GLN B -8 UNP O34926 EXPRESSION TAG SEQADV 3NC7 GLN B -7 UNP O34926 EXPRESSION TAG SEQADV 3NC7 MET B -6 UNP O34926 EXPRESSION TAG SEQADV 3NC7 GLY B -5 UNP O34926 EXPRESSION TAG SEQADV 3NC7 ARG B -4 UNP O34926 EXPRESSION TAG SEQADV 3NC7 GLY B -3 UNP O34926 EXPRESSION TAG SEQADV 3NC7 SER B -2 UNP O34926 EXPRESSION TAG SEQADV 3NC7 GLU B -1 UNP O34926 EXPRESSION TAG SEQADV 3NC7 PHE B 0 UNP O34926 EXPRESSION TAG SEQADV 3NC7 THR B 356 UNP O34926 ALA 356 ENGINEERED MUTATION SEQRES 1 A 441 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY SEQRES 2 A 441 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY SEQRES 3 A 441 GLY GLN GLN MET GLY ARG GLY SER GLU PHE MET SER GLN SEQRES 4 A 441 SER ILE LYS LEU PHE SER VAL LEU SER ASP GLN PHE GLN SEQRES 5 A 441 ASN ASN PRO TYR ALA TYR PHE SER GLN LEU ARG GLU GLU SEQRES 6 A 441 ASP PRO VAL HIS TYR GLU GLU SER ILE ASP SER TYR PHE SEQRES 7 A 441 ILE SER ARG TYR HIS ASP VAL ARG TYR ILE LEU GLN HIS SEQRES 8 A 441 PRO ASP ILE PHE THR THR LYS SER LEU VAL GLU ARG ALA SEQRES 9 A 441 GLU PRO VAL MET ARG GLY PRO VAL LEU ALA GLN MET HIS SEQRES 10 A 441 GLY LYS GLU HIS SER ALA LYS ARG ARG ILE VAL VAL ARG SEQRES 11 A 441 SER PHE ILE GLY ASP ALA LEU ASP HIS LEU SER PRO LEU SEQRES 12 A 441 ILE LYS GLN ASN ALA GLU ASN LEU LEU ALA PRO TYR LEU SEQRES 13 A 441 GLU ARG GLY LYS SER ASP LEU VAL ASN ASP PHE GLY LYS SEQRES 14 A 441 THR PHE ALA VAL CYS VAL THR MET ASP MET LEU GLY LEU SEQRES 15 A 441 ASP LYS ARG ASP HIS GLU LYS ILE SER GLU TRP HIS SER SEQRES 16 A 441 GLY VAL ALA ASP PHE ILE THR SER ILE SER GLN SER PRO SEQRES 17 A 441 GLU ALA ARG ALA HIS SER LEU TRP CYS SER GLU GLN LEU SEQRES 18 A 441 SER GLN TYR LEU MET PRO VAL ILE LYS GLU ARG ARG VAL SEQRES 19 A 441 ASN PRO GLY SER ASP LEU ILE SER ILE LEU CYS THR SER SEQRES 20 A 441 GLU TYR GLU GLY MET ALA LEU SER ASP LYS ASP ILE LEU SEQRES 21 A 441 ALA LEU ILE LEU ASN VAL LEU LEU ALA ALA THR GLU PRO SEQRES 22 A 441 ALA ASP LYS THR LEU ALA LEU MET ILE TYR HIS LEU LEU SEQRES 23 A 441 ASN ASN PRO GLU GLN MET ASN ASP VAL LEU ALA ASP ARG SEQRES 24 A 441 SER LEU VAL PRO ARG ALA ILE ALA GLU THR LEU ARG TYR SEQRES 25 A 441 LYS PRO PRO VAL GLN LEU ILE PRO ARG GLN LEU SER GLN SEQRES 26 A 441 ASP THR VAL VAL GLY GLY MET GLU ILE LYS LYS ASP THR SEQRES 27 A 441 ILE VAL PHE CYS MET ILE GLY ALA ALA ASN ARG ASP PRO SEQRES 28 A 441 GLU ALA PHE GLU GLN PRO ASP VAL PHE ASN ILE HIS ARG SEQRES 29 A 441 GLU ASP LEU GLY ILE LYS SER ALA PHE SER GLY ALA ALA SEQRES 30 A 441 ARG HIS LEU ALA PHE GLY SER GLY ILE HIS ASN CYS VAL SEQRES 31 A 441 GLY THR ALA PHE ALA LYS ASN GLU ILE GLU ILE VAL ALA SEQRES 32 A 441 ASN ILE VAL LEU ASP LYS MET ARG ASN ILE ARG LEU GLU SEQRES 33 A 441 GLU ASP PHE CYS TYR ALA GLU SER GLY LEU TYR THR ARG SEQRES 34 A 441 GLY PRO VAL SER LEU LEU VAL ALA PHE ASP GLY ALA SEQRES 1 B 441 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY SEQRES 2 B 441 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY SEQRES 3 B 441 GLY GLN GLN MET GLY ARG GLY SER GLU PHE MET SER GLN SEQRES 4 B 441 SER ILE LYS LEU PHE SER VAL LEU SER ASP GLN PHE GLN SEQRES 5 B 441 ASN ASN PRO TYR ALA TYR PHE SER GLN LEU ARG GLU GLU SEQRES 6 B 441 ASP PRO VAL HIS TYR GLU GLU SER ILE ASP SER TYR PHE SEQRES 7 B 441 ILE SER ARG TYR HIS ASP VAL ARG TYR ILE LEU GLN HIS SEQRES 8 B 441 PRO ASP ILE PHE THR THR LYS SER LEU VAL GLU ARG ALA SEQRES 9 B 441 GLU PRO VAL MET ARG GLY PRO VAL LEU ALA GLN MET HIS SEQRES 10 B 441 GLY LYS GLU HIS SER ALA LYS ARG ARG ILE VAL VAL ARG SEQRES 11 B 441 SER PHE ILE GLY ASP ALA LEU ASP HIS LEU SER PRO LEU SEQRES 12 B 441 ILE LYS GLN ASN ALA GLU ASN LEU LEU ALA PRO TYR LEU SEQRES 13 B 441 GLU ARG GLY LYS SER ASP LEU VAL ASN ASP PHE GLY LYS SEQRES 14 B 441 THR PHE ALA VAL CYS VAL THR MET ASP MET LEU GLY LEU SEQRES 15 B 441 ASP LYS ARG ASP HIS GLU LYS ILE SER GLU TRP HIS SER SEQRES 16 B 441 GLY VAL ALA ASP PHE ILE THR SER ILE SER GLN SER PRO SEQRES 17 B 441 GLU ALA ARG ALA HIS SER LEU TRP CYS SER GLU GLN LEU SEQRES 18 B 441 SER GLN TYR LEU MET PRO VAL ILE LYS GLU ARG ARG VAL SEQRES 19 B 441 ASN PRO GLY SER ASP LEU ILE SER ILE LEU CYS THR SER SEQRES 20 B 441 GLU TYR GLU GLY MET ALA LEU SER ASP LYS ASP ILE LEU SEQRES 21 B 441 ALA LEU ILE LEU ASN VAL LEU LEU ALA ALA THR GLU PRO SEQRES 22 B 441 ALA ASP LYS THR LEU ALA LEU MET ILE TYR HIS LEU LEU SEQRES 23 B 441 ASN ASN PRO GLU GLN MET ASN ASP VAL LEU ALA ASP ARG SEQRES 24 B 441 SER LEU VAL PRO ARG ALA ILE ALA GLU THR LEU ARG TYR SEQRES 25 B 441 LYS PRO PRO VAL GLN LEU ILE PRO ARG GLN LEU SER GLN SEQRES 26 B 441 ASP THR VAL VAL GLY GLY MET GLU ILE LYS LYS ASP THR SEQRES 27 B 441 ILE VAL PHE CYS MET ILE GLY ALA ALA ASN ARG ASP PRO SEQRES 28 B 441 GLU ALA PHE GLU GLN PRO ASP VAL PHE ASN ILE HIS ARG SEQRES 29 B 441 GLU ASP LEU GLY ILE LYS SER ALA PHE SER GLY ALA ALA SEQRES 30 B 441 ARG HIS LEU ALA PHE GLY SER GLY ILE HIS ASN CYS VAL SEQRES 31 B 441 GLY THR ALA PHE ALA LYS ASN GLU ILE GLU ILE VAL ALA SEQRES 32 B 441 ASN ILE VAL LEU ASP LYS MET ARG ASN ILE ARG LEU GLU SEQRES 33 B 441 GLU ASP PHE CYS TYR ALA GLU SER GLY LEU TYR THR ARG SEQRES 34 B 441 GLY PRO VAL SER LEU LEU VAL ALA PHE ASP GLY ALA HET HEM A 406 43 HET PIY A 407 11 HET MG A 408 1 HET HEM B 406 43 HET PIY B 407 11 HET MG B 408 1 HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETNAM PIY 2-PHENYL-1H-IMIDAZOLE HETNAM MG MAGNESIUM ION HETSYN HEM HEME FORMUL 3 HEM 2(C34 H32 FE N4 O4) FORMUL 4 PIY 2(C9 H8 N2) FORMUL 5 MG 2(MG 2+) FORMUL 9 HOH *2(H2 O) HELIX 1 1 SER A 12 ASN A 17 1 6 HELIX 2 2 ASN A 18 ALA A 21 5 4 HELIX 3 3 TYR A 22 ARG A 27 1 6 HELIX 4 4 ARG A 45 HIS A 55 1 11 HELIX 5 5 LYS A 88 ASP A 99 1 12 HELIX 6 6 LEU A 104 ALA A 117 1 14 HELIX 7 7 PHE A 131 GLY A 145 1 15 HELIX 8 8 ASP A 147 ARG A 149 5 3 HELIX 9 9 ASP A 150 SER A 167 1 18 HELIX 10 10 SER A 171 ASN A 199 1 29 HELIX 11 11 ASP A 203 CYS A 209 1 7 HELIX 12 12 SER A 219 ASN A 251 1 33 HELIX 13 13 ASN A 252 ASP A 262 1 11 HELIX 14 14 LEU A 265 LYS A 277 1 13 HELIX 15 15 ILE A 308 ARG A 313 1 6 HELIX 16 16 SER A 348 ASN A 352 5 5 HELIX 17 17 GLY A 355 MET A 374 1 20 HELIX 18 18 SER B 12 ASN B 18 1 7 HELIX 19 19 TYR B 22 ASP B 30 1 9 HELIX 20 20 ARG B 45 GLN B 54 1 10 HELIX 21 21 SER B 63 ALA B 68 1 6 HELIX 22 22 VAL B 93 LEU B 104 1 12 HELIX 23 23 LEU B 104 ALA B 117 1 14 HELIX 24 24 PHE B 131 GLY B 145 1 15 HELIX 25 25 ASP B 147 ARG B 149 5 3 HELIX 26 26 ASP B 150 SER B 167 1 18 HELIX 27 27 SER B 171 ASN B 199 1 29 HELIX 28 28 ASP B 203 CYS B 209 1 7 HELIX 29 29 SER B 219 ASN B 252 1 34 HELIX 30 30 ASN B 252 ASP B 262 1 11 HELIX 31 31 LEU B 265 LYS B 277 1 13 HELIX 32 32 ILE B 308 ARG B 313 1 6 HELIX 33 33 GLY B 355 MET B 374 1 20 SHEET 1 A 5 VAL A 32 GLU A 35 0 SHEET 2 A 5 SER A 40 ILE A 43 -1 O PHE A 42 N HIS A 33 SHEET 3 A 5 ILE A 303 MET A 307 1 O PHE A 305 N TYR A 41 SHEET 4 A 5 LEU A 282 LEU A 287 -1 N ILE A 283 O CYS A 306 SHEET 5 A 5 PHE A 59 THR A 60 -1 N THR A 60 O GLN A 286 SHEET 1 B 3 LYS A 124 ASP A 126 0 SHEET 2 B 3 LEU A 399 ALA A 401 -1 O VAL A 400 N SER A 125 SHEET 3 B 3 ARG A 378 LEU A 379 -1 N ARG A 378 O ALA A 401 SHEET 1 C 2 VAL A 292 VAL A 293 0 SHEET 2 C 2 MET A 296 GLU A 297 -1 O MET A 296 N VAL A 293 SHEET 1 D 2 GLU A 387 SER A 388 0 SHEET 2 D 2 GLY A 394 PRO A 395 -1 O GLY A 394 N SER A 388 SHEET 1 E 5 VAL B 32 GLU B 35 0 SHEET 2 E 5 SER B 40 ILE B 43 -1 O PHE B 42 N HIS B 33 SHEET 3 E 5 ILE B 303 MET B 307 1 O PHE B 305 N ILE B 43 SHEET 4 E 5 LEU B 282 LEU B 287 -1 N ARG B 285 O VAL B 304 SHEET 5 E 5 PHE B 59 THR B 60 -1 N THR B 60 O GLN B 286 SHEET 1 F 3 LYS B 124 ASP B 126 0 SHEET 2 F 3 LEU B 399 ALA B 401 -1 O VAL B 400 N SER B 125 SHEET 3 F 3 ARG B 378 LEU B 379 -1 N ARG B 378 O ALA B 401 SHEET 1 G 2 THR B 291 VAL B 293 0 SHEET 2 G 2 MET B 296 ILE B 298 -1 O MET B 296 N VAL B 293 SHEET 1 H 2 GLY B 347 SER B 348 0 SHEET 2 H 2 HIS B 351 ASN B 352 -1 O HIS B 351 N SER B 348 SHEET 1 I 2 GLU B 387 SER B 388 0 SHEET 2 I 2 GLY B 394 PRO B 395 -1 O GLY B 394 N SER B 388 LINK O ALA A 136 MG MG A 408 1555 1555 2.81 LINK SG CYS A 353 FE HEM A 406 1555 1555 2.48 LINK OE1 GLU A 362 MG MG A 408 1555 1555 2.73 LINK O ALA B 136 MG MG B 408 1555 1555 2.86 LINK SG CYS B 353 FE HEM B 406 1555 1555 2.45 LINK OE1 GLU B 362 MG MG B 408 1555 1555 2.81 SITE 1 AC1 19 LEU A 64 ILE A 97 MET A 143 ASN A 229 SITE 2 AC1 19 ALA A 233 ALA A 234 PRO A 237 THR A 241 SITE 3 AC1 19 ILE A 283 ARG A 285 ALA A 345 PHE A 346 SITE 4 AC1 19 GLY A 347 HIS A 351 CYS A 353 VAL A 354 SITE 5 AC1 19 PHE A 358 ALA A 359 PIY A 407 SITE 1 AC2 4 LEU A 232 GLU A 236 TYR A 391 HEM A 406 SITE 1 AC3 4 ALA A 136 THR A 140 ALA A 234 GLU A 362 SITE 1 AC4 18 SER B 63 LEU B 64 MET B 143 ASN B 229 SITE 2 AC4 18 ALA B 233 ALA B 234 PRO B 237 ILE B 283 SITE 3 AC4 18 ARG B 285 ALA B 345 PHE B 346 HIS B 351 SITE 4 AC4 18 CYS B 353 GLY B 355 PHE B 358 ALA B 359 SITE 5 AC4 18 ILE B 363 PIY B 407 SITE 1 AC5 3 ILE B 165 GLU B 236 HEM B 406 SITE 1 AC6 5 ALA B 136 THR B 140 ALA B 234 ALA B 238 SITE 2 AC6 5 GLU B 362 CRYST1 64.360 106.790 142.090 90.00 90.00 90.00 P 21 21 21 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.015538 0.000000 0.000000 0.00000 SCALE2 0.000000 0.009364 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007038 0.00000 (ATOM LINES ARE NOT SHOWN.) END