REMARK 2 REMARK 2 RESOLUTION. 3.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.2 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) : 3.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 96.1 REMARK 3 NUMBER OF REFLECTIONS : 68755 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) : 0.292 REMARK 3 R VALUE (WORKING SET) : 0.291 REMARK 3 FREE R VALUE : 0.312 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 3496 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) : 3.50 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.57 REMARK 3 REFLECTION IN BIN (WORKING SET) : 3622 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.47 REMARK 3 BIN R VALUE (WORKING SET) : 0.3410 REMARK 3 BIN FREE R VALUE SET COUNT : 187 REMARK 3 BIN FREE R VALUE : 0.3410 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 32356 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 0 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) : 65.48 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 4.80000 REMARK 3 B22 (A**2) : 0.36000 REMARK 3 B33 (A**2) : -5.27000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -3.56000 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): 0.793 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.675 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 95.462 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.840 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.821 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 33204 ; 0.007 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 28664 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 45152 ; 1.037 ; 1.955 REMARK 3 BOND ANGLES OTHERS (DEGREES): 67260 ; 0.712 ; 3.000 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 4168 ; 5.494 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1356 ;35.478 ;24.218 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 5340 ;18.479 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 128 ;12.205 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 4976 ; 0.058 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 36912 ; 0.002 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 6608 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 5177 ; 0.193 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 27180 ; 0.181 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 15655 ; 0.177 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): 19536 ; 0.082 ; 0.200 REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 644 ; 0.149 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): 3 ; 0.005 ; 0.200 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): 93 ; 0.337 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): 177 ; 0.380 ; 0.200 REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 10 ; 0.277 ; 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): 26696 ; 2.959 ; 2.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 8488 ; 0.105 ; 2.500 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 33936 ; 3.626 ; 5.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 14698 ; 1.602 ; 2.500 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 11216 ; 2.611 ; 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 : 3 REMARK 3 REMARK 3 NCS GROUP NUMBER : 1 REMARK 3 CHAIN NAMES : A E G K M Q S W REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 A 1 A 90 1 REMARK 3 1 E 1 E 90 1 REMARK 3 1 G 1 G 90 1 REMARK 3 1 K 1 K 90 1 REMARK 3 1 M 1 M 90 1 REMARK 3 1 Q 1 Q 90 1 REMARK 3 1 S 1 S 90 1 REMARK 3 1 W 1 W 90 1 REMARK 3 2 A 106 A 211 1 REMARK 3 2 E 106 E 211 1 REMARK 3 2 G 106 G 211 1 REMARK 3 2 K 106 K 211 1 REMARK 3 2 M 106 M 211 1 REMARK 3 2 Q 106 Q 211 1 REMARK 3 2 S 106 S 211 1 REMARK 3 2 W 106 W 211 1 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 TIGHT POSITIONAL 1 A (A): 2839 ; 0.010 ; 0.050 REMARK 3 TIGHT POSITIONAL 1 E (A): 2839 ; 0.010 ; 0.050 REMARK 3 TIGHT POSITIONAL 1 G (A): 2839 ; 0.010 ; 0.050 REMARK 3 TIGHT POSITIONAL 1 K (A): 2839 ; 0.010 ; 0.050 REMARK 3 TIGHT POSITIONAL 1 M (A): 2839 ; 0.010 ; 0.050 REMARK 3 TIGHT POSITIONAL 1 Q (A): 2839 ; 0.010 ; 0.050 REMARK 3 TIGHT POSITIONAL 1 S (A): 2839 ; 0.010 ; 0.050 REMARK 3 TIGHT POSITIONAL 1 W (A): 2839 ; 0.010 ; 0.050 REMARK 3 TIGHT THERMAL 1 A (A**2): 2839 ; 0.020 ; 0.500 REMARK 3 TIGHT THERMAL 1 E (A**2): 2839 ; 0.020 ; 0.500 REMARK 3 TIGHT THERMAL 1 G (A**2): 2839 ; 0.030 ; 0.500 REMARK 3 TIGHT THERMAL 1 K (A**2): 2839 ; 0.020 ; 0.500 REMARK 3 TIGHT THERMAL 1 M (A**2): 2839 ; 0.020 ; 0.500 REMARK 3 TIGHT THERMAL 1 Q (A**2): 2839 ; 0.030 ; 0.500 REMARK 3 TIGHT THERMAL 1 S (A**2): 2839 ; 0.030 ; 0.500 REMARK 3 TIGHT THERMAL 1 W (A**2): 2839 ; 0.030 ; 0.500 REMARK 3 REMARK 3 NCS GROUP NUMBER : 2 REMARK 3 CHAIN NAMES : B F H L N R T X REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 B 1 B 113 1 REMARK 3 1 F 1 F 113 1 REMARK 3 1 H 1 H 113 1 REMARK 3 1 L 1 L 113 1 REMARK 3 1 N 1 N 113 1 REMARK 3 1 R 1 R 113 1 REMARK 3 1 T 1 T 113 1 REMARK 3 1 X 1 X 113 1 REMARK 3 2 B 114 B 216 1 REMARK 3 2 F 114 F 216 1 REMARK 3 2 H 114 H 216 1 REMARK 3 2 L 114 L 216 1 REMARK 3 2 N 114 N 216 1 REMARK 3 2 R 114 R 216 1 REMARK 3 2 T 114 T 216 1 REMARK 3 2 X 114 X 216 1 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 TIGHT POSITIONAL 2 B (A): 3047 ; 0.010 ; 0.050 REMARK 3 TIGHT POSITIONAL 2 F (A): 3047 ; 0.010 ; 0.050 REMARK 3 TIGHT POSITIONAL 2 H (A): 3047 ; 0.020 ; 0.050 REMARK 3 TIGHT POSITIONAL 2 L (A): 3047 ; 0.010 ; 0.050 REMARK 3 TIGHT POSITIONAL 2 N (A): 3047 ; 0.010 ; 0.050 REMARK 3 TIGHT POSITIONAL 2 R (A): 3047 ; 0.020 ; 0.050 REMARK 3 TIGHT POSITIONAL 2 T (A): 3047 ; 0.010 ; 0.050 REMARK 3 TIGHT POSITIONAL 2 X (A): 3047 ; 0.010 ; 0.050 REMARK 3 TIGHT THERMAL 2 B (A**2): 3047 ; 0.020 ; 0.500 REMARK 3 TIGHT THERMAL 2 F (A**2): 3047 ; 0.020 ; 0.500 REMARK 3 TIGHT THERMAL 2 H (A**2): 3047 ; 0.030 ; 0.500 REMARK 3 TIGHT THERMAL 2 L (A**2): 3047 ; 0.020 ; 0.500 REMARK 3 TIGHT THERMAL 2 N (A**2): 3047 ; 0.020 ; 0.500 REMARK 3 TIGHT THERMAL 2 R (A**2): 3047 ; 0.030 ; 0.500 REMARK 3 TIGHT THERMAL 2 T (A**2): 3047 ; 0.030 ; 0.500 REMARK 3 TIGHT THERMAL 2 X (A**2): 3047 ; 0.030 ; 0.500 REMARK 3 REMARK 3 NCS GROUP NUMBER : 3 REMARK 3 CHAIN NAMES : C D I J O P U V REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 C 13 C 107 1 REMARK 3 1 D 13 D 109 1 REMARK 3 1 I 13 I 107 1 REMARK 3 1 J 13 J 109 1 REMARK 3 1 O 13 O 107 1 REMARK 3 1 P 13 P 109 1 REMARK 3 1 U 13 U 107 1 REMARK 3 1 V 13 V 109 1 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 TIGHT POSITIONAL 3 C (A): 1457 ; 0.010 ; 0.050 REMARK 3 TIGHT POSITIONAL 3 D (A): 1457 ; 0.010 ; 0.050 REMARK 3 TIGHT POSITIONAL 3 I (A): 1457 ; 0.010 ; 0.050 REMARK 3 TIGHT POSITIONAL 3 J (A): 1457 ; 0.010 ; 0.050 REMARK 3 TIGHT POSITIONAL 3 O (A): 1457 ; 0.010 ; 0.050 REMARK 3 TIGHT POSITIONAL 3 P (A): 1457 ; 0.010 ; 0.050 REMARK 3 TIGHT POSITIONAL 3 U (A): 1457 ; 0.010 ; 0.050 REMARK 3 TIGHT POSITIONAL 3 V (A): 1457 ; 0.010 ; 0.050 REMARK 3 TIGHT THERMAL 3 C (A**2): 1457 ; 0.020 ; 0.500 REMARK 3 TIGHT THERMAL 3 D (A**2): 1457 ; 0.020 ; 0.500 REMARK 3 TIGHT THERMAL 3 I (A**2): 1457 ; 0.020 ; 0.500 REMARK 3 TIGHT THERMAL 3 J (A**2): 1457 ; 0.020 ; 0.500 REMARK 3 TIGHT THERMAL 3 O (A**2): 1457 ; 0.020 ; 0.500 REMARK 3 TIGHT THERMAL 3 P (A**2): 1457 ; 0.020 ; 0.500 REMARK 3 TIGHT THERMAL 3 U (A**2): 1457 ; 0.020 ; 0.500 REMARK 3 TIGHT THERMAL 3 V (A**2): 1457 ; 0.020 ; 0.500 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 40 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 1 A 105 REMARK 3 RESIDUE RANGE : A 106 A 211 REMARK 3 RESIDUE RANGE : B 1 B 113 REMARK 3 RESIDUE RANGE : B 114 B 216 REMARK 3 RESIDUE RANGE : C 13 C 107 REMARK 3 RESIDUE RANGE : D 13 D 107 REMARK 3 RESIDUE RANGE : E 1 E 105 REMARK 3 RESIDUE RANGE : E 106 E 211 REMARK 3 RESIDUE RANGE : F 1 F 113 REMARK 3 RESIDUE RANGE : F 114 F 216 REMARK 3 RESIDUE RANGE : G 1 G 105 REMARK 3 RESIDUE RANGE : G 106 G 211 REMARK 3 RESIDUE RANGE : H 1 H 113 REMARK 3 RESIDUE RANGE : H 114 H 216 REMARK 3 RESIDUE RANGE : I 13 I 107 REMARK 3 RESIDUE RANGE : J 13 J 107 REMARK 3 RESIDUE RANGE : K 1 K 105 REMARK 3 RESIDUE RANGE : K 106 K 211 REMARK 3 RESIDUE RANGE : L 1 L 113 REMARK 3 RESIDUE RANGE : L 114 L 216 REMARK 3 RESIDUE RANGE : M 1 M 105 REMARK 3 RESIDUE RANGE : M 106 M 211 REMARK 3 RESIDUE RANGE : N 1 N 113 REMARK 3 RESIDUE RANGE : N 114 N 216 REMARK 3 RESIDUE RANGE : O 13 O 107 REMARK 3 RESIDUE RANGE : P 13 P 107 REMARK 3 RESIDUE RANGE : Q 1 Q 105 REMARK 3 RESIDUE RANGE : Q 106 Q 211 REMARK 3 RESIDUE RANGE : R 1 R 113 REMARK 3 RESIDUE RANGE : R 114 R 216 REMARK 3 RESIDUE RANGE : S 1 S 105 REMARK 3 RESIDUE RANGE : S 106 S 211 REMARK 3 RESIDUE RANGE : T 1 T 113 REMARK 3 RESIDUE RANGE : T 114 T 216 REMARK 3 RESIDUE RANGE : U 13 U 107 REMARK 3 RESIDUE RANGE : V 13 V 107 REMARK 3 RESIDUE RANGE : W 1 W 105 REMARK 3 RESIDUE RANGE : W 106 W 211 REMARK 3 RESIDUE RANGE : X 1 X 113 REMARK 3 RESIDUE RANGE : X 114 X 216 REMARK 3 ORIGIN FOR THE GROUP (A): -38.4554 60.4287 19.4604 REMARK 3 T TENSOR REMARK 3 T11: 0.0000 T22: 0.0000 REMARK 3 T33: 0.0000 T12: 0.0000 REMARK 3 T13: 0.0000 T23: 0.0000 REMARK 3 L TENSOR REMARK 3 L11: 0.0632 L22: 0.0679 REMARK 3 L33: 0.1053 L12: 0.0204 REMARK 3 L13: 0.0135 L23: 0.0836 REMARK 3 S TENSOR REMARK 3 S11: 0.0196 S12: -0.0349 S13: -0.0028 REMARK 3 S21: 0.0537 S22: -0.0021 S23: 0.0118 REMARK 3 S31: 0.0530 S32: -0.0138 S33: -0.0175 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 2QR0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-JUL-07. REMARK 100 THE RCSB ID CODE IS RCSB043946. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : NULL REMARK 200 PH : NULL 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 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : NULL REMARK 200 DETECTOR MANUFACTURER : NULL REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL REMARK 200 DATA SCALING SOFTWARE : HKL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 71940 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.500 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.1 REMARK 200 DATA REDUNDANCY : 3.300 REMARK 200 R MERGE (I) : 0.09700 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 10.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.63 REMARK 200 COMPLETENESS FOR SHELL (%) : 93.4 REMARK 200 DATA REDUNDANCY IN SHELL : 2.90 REMARK 200 R MERGE FOR SHELL (I) : 0.44400 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL 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: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 59.96 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.07 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL 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 45.10900 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F 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: HEXAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, I, J, K, L REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, N, O, P, Q, R REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 4 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: S, T, U, V, W, X 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 LYS B 129 REMARK 465 SER B 130 REMARK 465 THR B 131 REMARK 465 SER B 132 REMARK 465 GLY B 133 REMARK 465 LYS C 108 REMARK 465 ASP C 109 REMARK 465 LYS F 129 REMARK 465 SER F 130 REMARK 465 THR F 131 REMARK 465 SER F 132 REMARK 465 GLY F 133 REMARK 465 LYS H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 SER H 132 REMARK 465 GLY H 133 REMARK 465 LYS I 108 REMARK 465 ASP I 109 REMARK 465 LYS L 129 REMARK 465 SER L 130 REMARK 465 THR L 131 REMARK 465 SER L 132 REMARK 465 GLY L 133 REMARK 465 LYS N 129 REMARK 465 SER N 130 REMARK 465 THR N 131 REMARK 465 SER N 132 REMARK 465 GLY N 133 REMARK 465 LYS O 108 REMARK 465 ASP O 109 REMARK 465 LYS R 129 REMARK 465 SER R 130 REMARK 465 THR R 131 REMARK 465 SER R 132 REMARK 465 GLY R 133 REMARK 465 LYS T 129 REMARK 465 SER T 130 REMARK 465 THR T 131 REMARK 465 SER T 132 REMARK 465 GLY T 133 REMARK 465 LYS U 108 REMARK 465 ASP U 109 REMARK 465 LYS X 129 REMARK 465 SER X 130 REMARK 465 THR X 131 REMARK 465 SER X 132 REMARK 465 GLY X 133 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 NE2 GLN K 90 OG1 THR K 97 2.07 REMARK 500 OH TYR P 45 OH TYR R 54 2.08 REMARK 500 NE2 GLN Q 90 OG1 THR Q 97 2.15 REMARK 500 OH TYR I 39 O SER I 95 2.15 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 LEU A 11 129.72 -177.66 REMARK 500 SER A 30 -160.10 69.80 REMARK 500 SER A 31 52.78 -94.34 REMARK 500 ALA A 32 62.30 -119.38 REMARK 500 SER A 50 41.23 37.58 REMARK 500 ALA A 51 -36.70 72.29 REMARK 500 SER A 52 -31.20 -131.83 REMARK 500 THR A 69 -34.16 152.77 REMARK 500 TYR A 91 -152.90 -123.08 REMARK 500 SER A 92 65.97 85.94 REMARK 500 TYR A 93 127.89 -15.73 REMARK 500 TYR A 94 59.20 -161.62 REMARK 500 TYR A 94A -56.41 97.98 REMARK 500 ASN A 138 70.35 50.77 REMARK 500 GLU A 143 93.38 -55.40 REMARK 500 LEU A 154 173.16 -59.81 REMARK 500 PRO A 204 105.10 -41.09 REMARK 500 VAL B 48 -65.21 -103.63 REMARK 500 SER B 55 46.57 37.26 REMARK 500 ALA B 100 157.41 69.25 REMARK 500 SER B 127 -123.76 -113.67 REMARK 500 ASP B 144 77.26 58.90 REMARK 500 SER B 215 -73.60 -15.08 REMARK 500 CYS C 26 105.72 -43.22 REMARK 500 ASP C 63 127.52 -177.08 REMARK 500 THR C 71 -54.39 -121.21 REMARK 500 GLN C 87 -77.12 -142.30 REMARK 500 CYS D 26 105.94 -43.28 REMARK 500 ASP D 63 127.67 -176.96 REMARK 500 THR D 71 -53.93 -121.47 REMARK 500 GLN D 87 -76.30 -141.55 REMARK 500 LEU E 11 130.90 -177.56 REMARK 500 SER E 30 -160.69 69.16 REMARK 500 SER E 31 53.13 -94.28 REMARK 500 SER E 50 42.38 37.81 REMARK 500 ALA E 51 -35.56 70.97 REMARK 500 SER E 52 -31.36 -132.12 REMARK 500 SER E 67 59.69 -143.22 REMARK 500 THR E 69 -33.73 152.59 REMARK 500 TYR E 91 -119.48 -115.16 REMARK 500 SER E 92 100.49 57.61 REMARK 500 TYR E 94 -67.63 -132.89 REMARK 500 TYR E 94A -50.76 -121.06 REMARK 500 ASN E 138 71.14 50.05 REMARK 500 GLU E 143 93.52 -56.12 REMARK 500 LEU E 154 173.10 -59.79 REMARK 500 PRO E 204 105.29 -41.07 REMARK 500 SER F 31 32.32 -91.37 REMARK 500 VAL F 48 -65.69 -103.52 REMARK 500 SER F 55 44.46 36.86 REMARK 500 REMARK 500 THIS ENTRY HAS 211 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL