REMARK 2 REMARK 2 RESOLUTION. 2.19 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.2.0019 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) : 2.19 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8 REMARK 3 NUMBER OF REFLECTIONS : 62930 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) : 0.227 REMARK 3 R VALUE (WORKING SET) : 0.222 REMARK 3 FREE R VALUE : 0.271 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000 REMARK 3 FREE R VALUE TEST SET COUNT : 6979 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 25 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.19 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.23 REMARK 3 REFLECTION IN BIN (WORKING SET) : 3061 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 81.91 REMARK 3 BIN R VALUE (WORKING SET) : 0.2950 REMARK 3 BIN FREE R VALUE SET COUNT : 322 REMARK 3 BIN FREE R VALUE : 0.3620 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 9986 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 39 REMARK 3 SOLVENT ATOMS : 81 REMARK 3 REMARK 3 B VALUES. REMARK 3 B VALUE TYPE : LIKELY RESIDUAL REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.28 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -1.92000 REMARK 3 B22 (A**2) : 0.40000 REMARK 3 B33 (A**2) : 1.51000 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): 0.341 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.248 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.209 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.318 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.927 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.898 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10292 ; 0.008 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 6840 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14012 ; 1.139 ; 1.941 REMARK 3 BOND ANGLES OTHERS (DEGREES): 16619 ; 0.821 ; 3.006 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1302 ; 5.872 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 451 ;35.236 ;24.568 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1590 ;15.618 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 43 ;17.149 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1534 ; 0.066 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11599 ; 0.003 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 2072 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2043 ; 0.188 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 6794 ; 0.185 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4950 ; 0.174 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): 5539 ; 0.082 ; 0.200 REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 247 ; 0.140 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 19 ; 0.119 ; 0.200 REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 67 ; 0.190 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): 140 ; 0.197 ; 0.200 REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 17 ; 0.159 ; 0.200 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): 6708 ; 2.397 ; 2.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2654 ; 0.570 ; 2.500 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10463 ; 3.579 ; 5.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4187 ; 2.202 ; 2.500 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3548 ; 3.199 ; 5.000 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 : 5 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 1 A 107 4 REMARK 3 1 L 1 L 107 4 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 MEDIUM POSITIONAL 1 A (A): 1373 ; 0.42 ; 0.50 REMARK 3 MEDIUM THERMAL 1 A (A**2): 1373 ; 0.56 ; 2.00 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 1 B 111 4 REMARK 3 1 H 1 H 111 4 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 MEDIUM POSITIONAL 2 B (A): 1542 ; 0.39 ; 0.50 REMARK 3 MEDIUM THERMAL 2 B (A**2): 1542 ; 0.60 ; 2.00 REMARK 3 REMARK 3 NCS GROUP NUMBER : 3 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 108 A 212 4 REMARK 3 1 L 108 L 212 4 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 MEDIUM POSITIONAL 3 A (A): 1366 ; 0.41 ; 0.50 REMARK 3 MEDIUM THERMAL 3 A (A**2): 1366 ; 0.30 ; 2.00 REMARK 3 REMARK 3 NCS GROUP NUMBER : 4 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 112 B 214 4 REMARK 3 1 H 112 H 214 4 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 MEDIUM POSITIONAL 4 B (A): 1224 ; 0.42 ; 0.50 REMARK 3 MEDIUM THERMAL 4 B (A**2): 1224 ; 0.39 ; 2.00 REMARK 3 REMARK 3 NCS GROUP NUMBER : 5 REMARK 3 CHAIN NAMES : X Y REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 X 1461 X 1721 6 REMARK 3 1 Y 1461 Y 1721 6 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 LOOSE POSITIONAL 5 X (A): 2697 ; 0.59 ; 5.00 REMARK 3 LOOSE THERMAL 5 X (A**2): 2697 ; 3.22 ; 10.00 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 6 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 : X 1447 X 1727 REMARK 3 ORIGIN FOR THE GROUP (A): -12.1002 -25.4332 1.3977 REMARK 3 T TENSOR REMARK 3 T11: -0.1362 T22: -0.1808 REMARK 3 T33: -0.0868 T12: -0.0023 REMARK 3 T13: 0.0086 T23: -0.0140 REMARK 3 L TENSOR REMARK 3 L11: 1.4419 L22: 1.1034 REMARK 3 L33: 0.7321 L12: -0.2074 REMARK 3 L13: 0.2254 L23: 0.3498 REMARK 3 S TENSOR REMARK 3 S11: 0.0340 S12: 0.0943 S13: 0.1010 REMARK 3 S21: -0.0582 S22: -0.0498 S23: 0.0322 REMARK 3 S31: -0.0816 S32: 0.0048 S33: 0.0158 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 2 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 1 A 106 REMARK 3 RESIDUE RANGE : B 1 B 111 REMARK 3 ORIGIN FOR THE GROUP (A): -4.0428 -30.9795 28.4490 REMARK 3 T TENSOR REMARK 3 T11: -0.1511 T22: -0.1338 REMARK 3 T33: -0.2433 T12: -0.0029 REMARK 3 T13: 0.0028 T23: -0.0159 REMARK 3 L TENSOR REMARK 3 L11: 3.7199 L22: 0.6112 REMARK 3 L33: 1.1723 L12: 0.3945 REMARK 3 L13: 0.3381 L23: 0.0323 REMARK 3 S TENSOR REMARK 3 S11: 0.0168 S12: -0.4188 S13: -0.0273 REMARK 3 S21: 0.0456 S22: -0.0514 S23: -0.0075 REMARK 3 S31: -0.0447 S32: -0.0127 S33: 0.0347 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 2 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 107 A 212 REMARK 3 RESIDUE RANGE : B 112 B 214 REMARK 3 ORIGIN FOR THE GROUP (A): -2.5366 -30.8855 63.3461 REMARK 3 T TENSOR REMARK 3 T11: 0.0121 T22: -0.0027 REMARK 3 T33: -0.1758 T12: 0.0959 REMARK 3 T13: 0.0371 T23: -0.0180 REMARK 3 L TENSOR REMARK 3 L11: 3.4399 L22: 1.6613 REMARK 3 L33: 5.4864 L12: 1.7021 REMARK 3 L13: -1.5726 L23: -1.8068 REMARK 3 S TENSOR REMARK 3 S11: -0.0091 S12: -0.0024 S13: 0.1996 REMARK 3 S21: 0.2154 S22: 0.2959 S23: -0.0378 REMARK 3 S31: -0.5495 S32: -0.6572 S33: -0.2868 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 : Y 1461 Y 1726 REMARK 3 ORIGIN FOR THE GROUP (A): -18.4883 20.1126 16.4180 REMARK 3 T TENSOR REMARK 3 T11: -0.0593 T22: -0.1216 REMARK 3 T33: 0.0171 T12: -0.0017 REMARK 3 T13: -0.0276 T23: -0.0808 REMARK 3 L TENSOR REMARK 3 L11: 1.7346 L22: 1.2211 REMARK 3 L33: 1.3379 L12: -0.3479 REMARK 3 L13: -0.2312 L23: 0.2572 REMARK 3 S TENSOR REMARK 3 S11: -0.0369 S12: -0.2490 S13: 0.0204 REMARK 3 S21: -0.0798 S22: -0.0147 S23: 0.0208 REMARK 3 S31: -0.0384 S32: -0.0030 S33: 0.0516 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 NUMBER OF COMPONENTS GROUP : 2 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : L 1 L 106 REMARK 3 RESIDUE RANGE : H 1 H 111 REMARK 3 ORIGIN FOR THE GROUP (A): -26.1848 9.2761 43.0114 REMARK 3 T TENSOR REMARK 3 T11: 0.0690 T22: 0.2230 REMARK 3 T33: 0.0234 T12: 0.1143 REMARK 3 T13: 0.0622 T23: 0.0002 REMARK 3 L TENSOR REMARK 3 L11: 2.7095 L22: 3.2052 REMARK 3 L33: 5.2128 L12: 0.6681 REMARK 3 L13: 1.0891 L23: -0.5049 REMARK 3 S TENSOR REMARK 3 S11: -0.1650 S12: -0.5337 S13: -0.3404 REMARK 3 S21: 0.0524 S22: 0.0125 S23: -0.2646 REMARK 3 S31: 0.6946 S32: -0.1282 S33: 0.1525 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 NUMBER OF COMPONENTS GROUP : 2 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : L 107 L 212 REMARK 3 RESIDUE RANGE : H 112 H 213 REMARK 3 ORIGIN FOR THE GROUP (A): -28.6178 -2.0566 74.9825 REMARK 3 T TENSOR REMARK 3 T11: 0.6264 T22: 0.2958 REMARK 3 T33: 0.1061 T12: 0.3322 REMARK 3 T13: 0.0379 T23: -0.0646 REMARK 3 L TENSOR REMARK 3 L11: 4.5629 L22: 2.5132 REMARK 3 L33: 9.0204 L12: 2.8562 REMARK 3 L13: -1.8259 L23: -2.3299 REMARK 3 S TENSOR REMARK 3 S11: -0.1107 S12: 0.1923 S13: -0.1970 REMARK 3 S21: -0.2396 S22: -0.2474 S23: -0.2052 REMARK 3 S31: 1.4866 S32: -0.3169 S33: 0.3581 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 3L95 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JAN-10. REMARK 100 THE RCSB ID CODE IS RCSB056989. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 30-APR-08 REMARK 200 TEMPERATURE (KELVIN) : 93 REMARK 200 PH : 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ALS REMARK 200 BEAMLINE : 5.0.2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.000 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 69923 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.190 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4 REMARK 200 DATA REDUNDANCY : 6.600 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.09800 REMARK 200 FOR THE DATA SET : 14.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.19 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32 REMARK 200 COMPLETENESS FOR SHELL (%) : 88.5 REMARK 200 DATA REDUNDANCY IN SHELL : 5.50 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.49600 REMARK 200 FOR SHELL : 4.200 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 2OO4, FAB FRAGMENT REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 45.63 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: EQUAL VOLUMES OF PROTEIN AND WELL REMARK 280 SOLUTIONS. PROTEIN: 6 MG/ML IN 150 MM NACL, 20 MM BIS-TRIS PH REMARK 280 6.5. WELL SOLUTION: 300 MM DI-AMMONIUM SULFATE, 20% PEG 5000 MME, REMARK 280 100 MM TRIS PH 7.5, VAPOR DIFFUSION, TEMPERATURE 292K 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 23.12700 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 89.81000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 81.96700 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 89.81000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.12700 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 81.96700 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: PENTAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 6330 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 28910 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: X, B, H, A, Y 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: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5680 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 27960 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: Y, X, 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 GLU A 213 REMARK 465 CYS A 214 REMARK 465 SER B 215 REMARK 465 CYS B 216 REMARK 465 ASP B 217 REMARK 465 LYS B 218 REMARK 465 THR B 219 REMARK 465 HIS B 220 REMARK 465 THR B 221 REMARK 465 GLN X 1688 REMARK 465 ALA X 1689 REMARK 465 SER X 1690 REMARK 465 GLU X 1728 REMARK 465 PRO X 1729 REMARK 465 ALA X 1730 REMARK 465 ASN X 1731 REMARK 465 SER X 1732 REMARK 465 HIS X 1733 REMARK 465 HIS X 1734 REMARK 465 HIS X 1735 REMARK 465 HIS X 1736 REMARK 465 HIS X 1737 REMARK 465 HIS X 1738 REMARK 465 GLU L 213 REMARK 465 CYS L 214 REMARK 465 LYS H 214 REMARK 465 SER H 215 REMARK 465 CYS H 216 REMARK 465 ASP H 217 REMARK 465 LYS H 218 REMARK 465 THR H 219 REMARK 465 HIS H 220 REMARK 465 THR H 221 REMARK 465 GLY Y 1447 REMARK 465 SER Y 1448 REMARK 465 ALA Y 1449 REMARK 465 CYS Y 1450 REMARK 465 GLU Y 1451 REMARK 465 LEU Y 1452 REMARK 465 PRO Y 1453 REMARK 465 GLU Y 1454 REMARK 465 CYS Y 1455 REMARK 465 GLN Y 1456 REMARK 465 GLU Y 1457 REMARK 465 ASP Y 1458 REMARK 465 ALA Y 1459 REMARK 465 GLY Y 1460 REMARK 465 ARG Y 1524 REMARK 465 ALA Y 1525 REMARK 465 GLU Y 1526 REMARK 465 VAL Y 1727 REMARK 465 GLU Y 1728 REMARK 465 PRO Y 1729 REMARK 465 ALA Y 1730 REMARK 465 ASN Y 1731 REMARK 465 SER Y 1732 REMARK 465 HIS Y 1733 REMARK 465 HIS Y 1734 REMARK 465 HIS Y 1735 REMARK 465 HIS Y 1736 REMARK 465 HIS Y 1737 REMARK 465 HIS Y 1738 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LYS B 214 CG CD CE NZ 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 ND2 ASN X 1588 O HOH X 19 2.16 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 CYS X1529 CA - CB - SG ANGL. DEV. = 6.6 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 SER A 30 -107.86 30.14 REMARK 500 ALA A 51 -52.26 78.30 REMARK 500 GLU A 81 0.22 -67.06 REMARK 500 ALA A 84 173.23 172.50 REMARK 500 ASN A 152 -22.12 75.58 REMARK 500 SER B 96 -166.52 -101.29 REMARK 500 SER B 132 71.71 -119.27 REMARK 500 SER X1481 51.83 -113.69 REMARK 500 ASP X1486 107.39 -33.35 REMARK 500 ALA X1563 46.54 -174.44 REMARK 500 PRO X1716 15.17 -69.46 REMARK 500 SER L 30 -117.16 47.46 REMARK 500 ALA L 51 -50.08 72.41 REMARK 500 ALA L 84 154.21 173.00 REMARK 500 PRO L 95 94.66 -63.08 REMARK 500 VAL L 110 97.64 -62.21 REMARK 500 ASN L 138 73.57 54.10 REMARK 500 ASN L 152 -2.40 68.36 REMARK 500 SER H 7 177.05 172.69 REMARK 500 SER H 96 -165.94 -78.51 REMARK 500 PHE H 98 97.98 -69.83 REMARK 500 SER H 112 -153.06 -142.03 REMARK 500 ASP H 144 85.18 59.80 REMARK 500 THR H 191 -61.25 -93.59 REMARK 500 LYS Y1462 -28.31 72.15 REMARK 500 ASP Y1486 94.59 28.52 REMARK 500 CYS Y1522 59.70 -100.11 REMARK 500 ALA Y1563 42.27 -154.59 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 CA X2001 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 VAL X1463 O REMARK 620 2 ASN X1461 OD1 91.8 REMARK 620 3 ASP X1476 OD2 81.3 148.7 REMARK 620 4 ASP X1479 OD2 82.4 75.0 73.8 REMARK 620 5 ASP X1458 O 161.0 72.7 106.2 83.0 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA X2003 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS X1545 O REMARK 620 2 ASP X1547 OD2 83.4 REMARK 620 3 ASP X1561 OD2 85.0 168.0 REMARK 620 4 HIS X1540 O 157.3 96.0 95.9 REMARK 620 5 ASP X1543 OD1 84.5 113.2 68.7 74.9 REMARK 620 6 ASP X1558 OD1 125.1 91.0 93.0 77.6 144.8 REMARK 620 7 ASP X1558 OD2 77.9 85.3 89.1 124.8 152.8 47.2 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA Y2002 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP Y1507 OD2 REMARK 620 2 ASP Y1503 OD1 100.1 REMARK 620 3 HIS Y1505 O 82.4 88.0 REMARK 620 4 TYR Y1500 O 98.6 72.2 160.1 REMARK 620 5 ASP Y1518 OD1 91.0 150.7 120.5 79.4 REMARK 620 6 ASP Y1521 OD2 159.1 69.4 79.2 95.3 107.0 REMARK 620 7 ASP Y1518 OD2 90.8 154.3 70.3 129.4 50.6 92.4 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA X2002 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS X1505 O REMARK 620 2 ASP X1507 OD2 78.2 REMARK 620 3 TYR X1500 O 159.3 99.7 REMARK 620 4 ASP X1521 OD2 90.8 168.2 89.2 REMARK 620 5 ASP X1503 OD1 83.6 94.4 76.0 80.2 REMARK 620 6 ASP X1518 OD2 77.2 93.0 123.5 88.5 157.6 REMARK 620 7 ASP X1518 OD1 126.3 94.0 74.2 95.8 150.0 49.9 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA Y2001 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 VAL Y1463 O REMARK 620 2 SER Y1465 OG 103.6 REMARK 620 3 ASP Y1476 OD2 69.6 74.2 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA Y2003 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS Y1545 O REMARK 620 2 HIS Y1540 O 155.5 REMARK 620 3 ASP Y1547 OD2 88.7 93.3 REMARK 620 4 ASP Y1558 OD2 76.8 127.3 94.0 REMARK 620 5 ASP Y1561 OD2 87.1 91.4 175.3 82.9 REMARK 620 6 ASP Y1543 OD1 79.5 76.3 104.7 149.3 76.6 REMARK 620 7 ASP Y1558 OD1 127.2 77.1 92.6 50.4 88.3 149.0 REMARK 620 N 1 2 3 4 5 6 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 222 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA X 2001 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA X 2002 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA X 2003 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG X 2004 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG X 2005 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA Y 2001 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA Y 2002 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA Y 2003 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3ETO RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE S1-CLEAVED NOTCH1 NEGATIVE REMARK 900 REGULATORY REGION (NRR) REMARK 900 RELATED ID: 2OO4 RELATED DB: PDB REMARK 900 STRUCTURE OF LNR-HD (NEGATIVE REGULATORY REGION) FROM HUMAN REMARK 900 NOTCH2