REMARK 2 REMARK 2 RESOLUTION. 2.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.5.0109 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.74 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 93.3 REMARK 3 NUMBER OF REFLECTIONS : 27360 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) : 0.186 REMARK 3 R VALUE (WORKING SET) : 0.184 REMARK 3 FREE R VALUE : 0.239 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 1477 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) : 2.50 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.57 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1794 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 83.56 REMARK 3 BIN R VALUE (WORKING SET) : 0.2640 REMARK 3 BIN FREE R VALUE SET COUNT : 92 REMARK 3 BIN FREE R VALUE : 0.3400 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6695 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 11 REMARK 3 SOLVENT ATOMS : 294 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 40.60 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.85 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 1.17000 REMARK 3 B22 (A**2) : 0.48000 REMARK 3 B33 (A**2) : -1.55000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.11000 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): 0.315 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.199 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.676 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.936 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.894 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6872 ; 0.010 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 4556 ; 0.002 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9370 ; 1.461 ; 1.966 REMARK 3 BOND ANGLES OTHERS (DEGREES): 11162 ; 1.469 ; 3.000 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 847 ; 5.233 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 266 ;33.536 ;24.135 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1081 ;14.917 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 26 ;15.954 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1066 ; 0.086 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7562 ; 0.006 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): 1368 ; 0.003 ; 0.020 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): 4253 ; 1.368 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1714 ; 0.145 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6940 ; 2.716 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2619 ; 3.965 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2430 ; 6.806 ; 4.500 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 L REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 A 5 A 207 5 REMARK 3 1 L 5 L 207 5 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 MEDIUM POSITIONAL 1 A (A): 1222 ; 0.09 ; 0.50 REMARK 3 LOOSE POSITIONAL 1 A (A): 1518 ; 0.53 ; 5.00 REMARK 3 MEDIUM THERMAL 1 A (A**2): 1222 ; 1.38 ; 2.00 REMARK 3 LOOSE THERMAL 1 A (A**2): 1518 ; 1.30 ; 10.00 REMARK 3 REMARK 3 NCS GROUP NUMBER : 2 REMARK 3 CHAIN NAMES : B H REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 B 5 B 110 5 REMARK 3 1 H 5 H 110 5 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 MEDIUM POSITIONAL 2 H (A): 622 ; 0.06 ; 0.50 REMARK 3 LOOSE POSITIONAL 2 H (A): 804 ; 0.52 ; 5.00 REMARK 3 MEDIUM THERMAL 2 H (A**2): 622 ; 2.28 ; 2.00 REMARK 3 LOOSE THERMAL 2 H (A**2): 804 ; 1.95 ; 10.00 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 : H 1 H 114 REMARK 3 ORIGIN FOR THE GROUP (A): 10.7486 14.2940 32.4472 REMARK 3 T TENSOR REMARK 3 T11: 0.0686 T22: 0.0189 REMARK 3 T33: 0.0709 T12: 0.0048 REMARK 3 T13: 0.0291 T23: 0.0145 REMARK 3 L TENSOR REMARK 3 L11: 0.0278 L22: 0.3546 REMARK 3 L33: 1.0327 L12: -0.0575 REMARK 3 L13: 0.0354 L23: 0.3046 REMARK 3 S TENSOR REMARK 3 S11: 0.0067 S12: 0.0036 S13: 0.0210 REMARK 3 S21: 0.0217 S22: 0.0127 S23: 0.0006 REMARK 3 S31: -0.0006 S32: -0.0212 S33: -0.0195 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 : H 115 H 227 REMARK 3 ORIGIN FOR THE GROUP (A): -3.3083 -7.8853 7.3240 REMARK 3 T TENSOR REMARK 3 T11: 0.0339 T22: 0.1025 REMARK 3 T33: 0.0436 T12: 0.0067 REMARK 3 T13: -0.0096 T23: -0.0108 REMARK 3 L TENSOR REMARK 3 L11: 0.5274 L22: 0.5645 REMARK 3 L33: 0.1388 L12: -0.3713 REMARK 3 L13: -0.0297 L23: 0.2151 REMARK 3 S TENSOR REMARK 3 S11: 0.0005 S12: -0.0240 S13: -0.0207 REMARK 3 S21: 0.0255 S22: 0.0349 S23: -0.0514 REMARK 3 S31: 0.0110 S32: -0.0252 S33: -0.0354 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 : L 1 L 107 REMARK 3 ORIGIN FOR THE GROUP (A): 24.0056 -3.9266 34.6123 REMARK 3 T TENSOR REMARK 3 T11: 0.0946 T22: 0.0536 REMARK 3 T33: 0.0318 T12: 0.0437 REMARK 3 T13: 0.0079 T23: -0.0156 REMARK 3 L TENSOR REMARK 3 L11: 0.0983 L22: 1.2906 REMARK 3 L33: 0.6015 L12: 0.2145 REMARK 3 L13: -0.0460 L23: 0.5786 REMARK 3 S TENSOR REMARK 3 S11: -0.0581 S12: -0.0248 S13: 0.0193 REMARK 3 S21: 0.0707 S22: 0.0685 S23: 0.0644 REMARK 3 S31: 0.1512 S32: 0.1352 S33: -0.0103 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 : L 108 L 212 REMARK 3 ORIGIN FOR THE GROUP (A): 11.4722 -9.8633 1.3782 REMARK 3 T TENSOR REMARK 3 T11: 0.1074 T22: 0.0642 REMARK 3 T33: 0.0307 T12: 0.0240 REMARK 3 T13: -0.0036 T23: -0.0096 REMARK 3 L TENSOR REMARK 3 L11: 0.5114 L22: 0.0509 REMARK 3 L33: 0.9669 L12: -0.0258 REMARK 3 L13: 0.2968 L23: -0.2053 REMARK 3 S TENSOR REMARK 3 S11: -0.0479 S12: 0.1146 S13: -0.0577 REMARK 3 S21: 0.0185 S22: 0.0338 S23: -0.0112 REMARK 3 S31: -0.0163 S32: -0.0456 S33: 0.0141 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 1 B 114 REMARK 3 ORIGIN FOR THE GROUP (A): 17.1249 2.0797 -31.7602 REMARK 3 T TENSOR REMARK 3 T11: 0.0203 T22: 0.1692 REMARK 3 T33: 0.0498 T12: 0.0508 REMARK 3 T13: 0.0137 T23: -0.0067 REMARK 3 L TENSOR REMARK 3 L11: 0.0193 L22: 0.1423 REMARK 3 L33: 1.0699 L12: 0.0368 REMARK 3 L13: -0.0662 L23: 0.1193 REMARK 3 S TENSOR REMARK 3 S11: -0.0096 S12: 0.0037 S13: -0.0291 REMARK 3 S21: -0.0322 S22: -0.0252 S23: -0.0749 REMARK 3 S31: -0.0426 S32: -0.1489 S33: 0.0348 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 115 B 222 REMARK 3 ORIGIN FOR THE GROUP (A): 37.5576 12.2483 -4.1447 REMARK 3 T TENSOR REMARK 3 T11: 0.1081 T22: 0.0162 REMARK 3 T33: 0.0528 T12: 0.0015 REMARK 3 T13: 0.0344 T23: 0.0008 REMARK 3 L TENSOR REMARK 3 L11: 0.4168 L22: 0.5392 REMARK 3 L33: 0.7031 L12: -0.2660 REMARK 3 L13: 0.5200 L23: -0.4083 REMARK 3 S TENSOR REMARK 3 S11: 0.0397 S12: -0.0159 S13: -0.0429 REMARK 3 S21: -0.0221 S22: 0.0233 S23: -0.0156 REMARK 3 S31: -0.0210 S32: -0.0206 S33: -0.0630 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 : A 1 A 108 REMARK 3 ORIGIN FOR THE GROUP (A): 25.1410 -17.9631 -24.0379 REMARK 3 T TENSOR REMARK 3 T11: 0.0941 T22: 0.0549 REMARK 3 T33: 0.0385 T12: -0.0261 REMARK 3 T13: 0.0224 T23: -0.0162 REMARK 3 L TENSOR REMARK 3 L11: 0.8252 L22: 0.1030 REMARK 3 L33: 1.2737 L12: -0.1752 REMARK 3 L13: 0.5593 L23: 0.1229 REMARK 3 S TENSOR REMARK 3 S11: -0.0124 S12: 0.0523 S13: 0.0528 REMARK 3 S21: 0.0674 S22: -0.0035 S23: -0.0184 REMARK 3 S31: 0.2343 S32: 0.0357 S33: 0.0158 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 : A 109 A 212 REMARK 3 ORIGIN FOR THE GROUP (A): 29.8144 1.6172 5.7419 REMARK 3 T TENSOR REMARK 3 T11: 0.0730 T22: 0.0188 REMARK 3 T33: 0.1039 T12: -0.0106 REMARK 3 T13: -0.0005 T23: 0.0035 REMARK 3 L TENSOR REMARK 3 L11: 0.2487 L22: 0.4948 REMARK 3 L33: 0.6999 L12: -0.1829 REMARK 3 L13: -0.3903 L23: 0.1972 REMARK 3 S TENSOR REMARK 3 S11: 0.0616 S12: 0.0379 S13: -0.0013 REMARK 3 S21: -0.0126 S22: -0.0270 S23: -0.0204 REMARK 3 S31: -0.0445 S32: -0.0775 S33: -0.0345 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 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 3QG6 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-FEB-11. REMARK 100 THE RCSB ID CODE IS RCSB063603. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 05-JUN-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 : APS REMARK 200 BEAMLINE : 23-ID-B REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.98 REMARK 200 MONOCHROMATOR : SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29017 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500 REMARK 200 RESOLUTION RANGE LOW (A) : 39.740 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 94.3 REMARK 200 DATA REDUNDANCY : 2.900 REMARK 200 R MERGE (I) : 0.16800 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59 REMARK 200 COMPLETENESS FOR SHELL (%) : 90.7 REMARK 200 DATA REDUNDANCY IN SHELL : 2.40 REMARK 200 R MERGE FOR SHELL (I) : 0.43100 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.600 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: PDB ENTRY 15C8 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 47.64 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 29MM ZINC CHLORIDE, 20% PEG 4000, 0.1M REMARK 280 SODIUM CACODYLATE. CRYOPROTECTION IN 20% GLYCEROL, PH 6.5, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 49.24900 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4540 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20030 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, A, 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4580 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19850 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, L, H 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 GLY B 131 REMARK 465 ASP B 132 REMARK 465 THR B 133 REMARK 465 THR B 134 REMARK 465 GLY H 131 REMARK 465 ASP H 132 REMARK 465 THR H 133 REMARK 465 THR H 134 REMARK 465 SER H 228 REMARK 465 TYR C 1 REMARK 465 SER C 2 REMARK 465 TYR D 1 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 LEU A 47 -66.03 -102.83 REMARK 500 LEU A 51 -52.90 73.60 REMARK 500 ALA A 130 108.72 -161.04 REMARK 500 SER B 15 -12.50 85.20 REMARK 500 ASN B 32 -56.61 68.99 REMARK 500 ARG B 94 -90.32 -85.53 REMARK 500 SER H 15 -10.38 87.92 REMARK 500 ASN H 32 -55.83 69.79 REMARK 500 ASN H 43 1.75 80.34 REMARK 500 ARG H 94 -88.71 -87.86 REMARK 500 ASP H 183 -1.87 70.69 REMARK 500 LEU L 47 -62.66 -103.65 REMARK 500 LEU L 51 -54.60 78.22 REMARK 500 ALA L 130 110.42 -160.56 REMARK 500 SER L 171 17.83 59.89 REMARK 500 PHE C 6 -89.27 -113.16 REMARK 500 PHE D 6 -88.81 -110.64 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 SER H 17 LEU H 18 -142.75 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 ZN A 216 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 189 NE2 REMARK 620 2 GLU H 85 OE2 103.4 REMARK 620 3 GLU A 185 OE2 104.4 83.0 REMARK 620 4 GLU H 85 OE1 95.1 54.8 136.8 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN L 218 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP L 1 N REMARK 620 2 ASP L 1 O 77.6 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN B 229 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP B 72 OD1 REMARK 620 2 SER B 74 OG 87.4 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN L 215 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU B 85 OE2 REMARK 620 2 HIS L 189 NE2 117.2 REMARK 620 3 GLU L 185 OE2 83.7 102.2 REMARK 620 4 GLU B 85 OE1 55.9 91.2 138.8 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 217 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 93 ND1 REMARK 620 2 HOH A 271 O 132.5 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 214 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 1 O REMARK 620 2 ASP A 1 N 74.3 REMARK 620 N 1 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 214 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 216 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 217 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 229 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H 229 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN L 215 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN L 216 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN L 217 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN L 218 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN C OF AGR AUTOINDUCING REMARK 800 PEPTIDE REMARK 800 REMARK 800 SITE_IDENTIFIER: BC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN D OF AGR AUTOINDUCING REMARK 800 PEPTIDE REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3QG7 RELATED DB: PDB