REMARK 2 REMARK 2 RESOLUTION. 3.34 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.11.2 REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER, REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN, REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.34 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.20 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 92.6 REMARK 3 NUMBER OF REFLECTIONS : 19651 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) : 0.234 REMARK 3 R VALUE (WORKING SET) : 0.234 REMARK 3 FREE R VALUE : 0.233 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.110 REMARK 3 FREE R VALUE TEST SET COUNT : 1004 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 10 REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 3.34 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.52 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.62 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2769 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2475 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2635 REMARK 3 BIN R VALUE (WORKING SET) : 0.2460 REMARK 3 BIN FREE R VALUE : 0.2781 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.84 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 134 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 9082 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 76.24 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 110.97 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 1.54880 REMARK 3 B22 (A**2) : -6.36740 REMARK 3 B33 (A**2) : 4.81850 REMARK 3 B12 (A**2) : -8.62580 REMARK 3 B13 (A**2) : -8.96580 REMARK 3 B23 (A**2) : 16.79170 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.94 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL REMARK 3 REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797 REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.879 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.890 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 9302 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 12699 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 3005 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : 174 ; 2.000 ; HARMONIC REMARK 3 GENERAL PLANES : 1353 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 9302 ; 20.000 ; HARMONIC REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : 1242 ; 5.000 ; SEMIHARMONIC REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL REMARK 3 IDEAL-DIST CONTACT TERM : 10209 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.008 REMARK 3 BOND ANGLES (DEGREES) : 1.19 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.96 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 21.46 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 10 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: {A|1 - 123} REMARK 3 ORIGIN FOR THE GROUP (A): -5.8528 -8.0549 65.6961 REMARK 3 T TENSOR REMARK 3 T11: -0.0565 T22: -0.4174 REMARK 3 T33: 0.2337 T12: -0.0196 REMARK 3 T13: -0.0746 T23: 0.0079 REMARK 3 L TENSOR REMARK 3 L11: 8.1163 L22: 3.6032 REMARK 3 L33: 5.1577 L12: 0.2308 REMARK 3 L13: 1.6747 L23: 0.5947 REMARK 3 S TENSOR REMARK 3 S11: 0.1487 S12: -0.2225 S13: -0.3728 REMARK 3 S21: 0.2763 S22: -0.4463 S23: 0.3245 REMARK 3 S31: 0.1821 S32: -0.1336 S33: 0.2976 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: {A|124 - 224} REMARK 3 ORIGIN FOR THE GROUP (A): 15.6472 17.0931 60.6451 REMARK 3 T TENSOR REMARK 3 T11: 0.3081 T22: -0.2440 REMARK 3 T33: -0.1914 T12: 0.1431 REMARK 3 T13: 0.0554 T23: -0.0194 REMARK 3 L TENSOR REMARK 3 L11: 5.5100 L22: 4.9691 REMARK 3 L33: 1.9324 L12: -1.2686 REMARK 3 L13: 0.8239 L23: -3.0023 REMARK 3 S TENSOR REMARK 3 S11: 0.2379 S12: -0.1962 S13: 0.1505 REMARK 3 S21: -0.3120 S22: -0.0363 S23: 0.1347 REMARK 3 S31: -0.6114 S32: -0.0333 S33: -0.2015 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: {C|1 - 123} REMARK 3 ORIGIN FOR THE GROUP (A): -6.1585 -36.3010 8.6852 REMARK 3 T TENSOR REMARK 3 T11: -0.0884 T22: -0.3638 REMARK 3 T33: 0.0152 T12: 0.0125 REMARK 3 T13: -0.0575 T23: 0.0683 REMARK 3 L TENSOR REMARK 3 L11: 8.1033 L22: 4.2318 REMARK 3 L33: 7.7908 L12: -1.9239 REMARK 3 L13: -1.7567 L23: 1.3885 REMARK 3 S TENSOR REMARK 3 S11: 0.2308 S12: 0.0284 S13: 0.1363 REMARK 3 S21: -0.1734 S22: -0.4952 S23: 0.1667 REMARK 3 S31: -0.0535 S32: -0.0473 S33: 0.2644 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: {C|124 - 224} REMARK 3 ORIGIN FOR THE GROUP (A): 15.4538 -61.3629 13.7987 REMARK 3 T TENSOR REMARK 3 T11: 0.2753 T22: -0.2609 REMARK 3 T33: -0.2131 T12: 0.1045 REMARK 3 T13: -0.0684 T23: 0.0811 REMARK 3 L TENSOR REMARK 3 L11: 7.4969 L22: 5.4521 REMARK 3 L33: 2.6122 L12: -0.8769 REMARK 3 L13: 1.4540 L23: -2.3813 REMARK 3 S TENSOR REMARK 3 S11: 0.1449 S12: 0.1040 S13: -0.2805 REMARK 3 S21: 0.0939 S22: -0.0978 S23: -0.0519 REMARK 3 S31: 0.4370 S32: -0.4641 S33: -0.0471 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: {B|1 - 115} REMARK 3 ORIGIN FOR THE GROUP (A): -3.5084 -10.3966 44.5177 REMARK 3 T TENSOR REMARK 3 T11: -0.2102 T22: -0.0697 REMARK 3 T33: 0.0782 T12: 0.2259 REMARK 3 T13: -0.1301 T23: -0.1240 REMARK 3 L TENSOR REMARK 3 L11: 5.2730 L22: 3.4947 REMARK 3 L33: 5.6164 L12: 1.8776 REMARK 3 L13: -2.3656 L23: 0.2504 REMARK 3 S TENSOR REMARK 3 S11: -0.1877 S12: 0.6372 S13: -0.2001 REMARK 3 S21: -0.1502 S22: -0.2923 S23: 0.1856 REMARK 3 S31: 0.2812 S32: -0.1098 S33: 0.4800 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: {B|116 - 219} REMARK 3 ORIGIN FOR THE GROUP (A): 27.3521 12.3976 50.9139 REMARK 3 T TENSOR REMARK 3 T11: -0.0135 T22: -0.2736 REMARK 3 T33: -0.1205 T12: -0.0450 REMARK 3 T13: 0.0961 T23: 0.1858 REMARK 3 L TENSOR REMARK 3 L11: 6.4548 L22: 5.2161 REMARK 3 L33: 8.9339 L12: 0.1899 REMARK 3 L13: 2.5055 L23: 0.9064 REMARK 3 S TENSOR REMARK 3 S11: 0.2509 S12: -0.0798 S13: -0.1085 REMARK 3 S21: -0.0338 S22: -0.3233 S23: -0.1464 REMARK 3 S31: -0.2838 S32: 0.3569 S33: 0.0724 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: {D|1 - 115} REMARK 3 ORIGIN FOR THE GROUP (A): -3.5894 -33.6597 29.8124 REMARK 3 T TENSOR REMARK 3 T11: -0.2776 T22: -0.0981 REMARK 3 T33: 0.0433 T12: -0.1357 REMARK 3 T13: 0.0594 T23: -0.0461 REMARK 3 L TENSOR REMARK 3 L11: 3.8172 L22: 3.3999 REMARK 3 L33: 8.9825 L12: 0.9301 REMARK 3 L13: 2.1894 L23: 0.0012 REMARK 3 S TENSOR REMARK 3 S11: -0.0070 S12: -0.7482 S13: 0.3027 REMARK 3 S21: 0.1362 S22: -0.1572 S23: 0.2442 REMARK 3 S31: 0.0803 S32: 0.3002 S33: 0.1642 REMARK 3 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: {D|116 - 219} REMARK 3 ORIGIN FOR THE GROUP (A): 27.1767 -56.6172 23.3532 REMARK 3 T TENSOR REMARK 3 T11: -0.0170 T22: -0.1553 REMARK 3 T33: -0.1196 T12: 0.2462 REMARK 3 T13: -0.0063 T23: 0.1920 REMARK 3 L TENSOR REMARK 3 L11: 9.5569 L22: 3.3454 REMARK 3 L33: 6.8917 L12: -1.1865 REMARK 3 L13: -2.9122 L23: -0.1102 REMARK 3 S TENSOR REMARK 3 S11: 0.1254 S12: -0.0251 S13: -0.0370 REMARK 3 S21: -0.0534 S22: -0.1389 S23: -0.2237 REMARK 3 S31: 0.0922 S32: 0.5010 S33: 0.0135 REMARK 3 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: {E|4 - 151} REMARK 3 ORIGIN FOR THE GROUP (A): -35.6645 -23.0190 20.0986 REMARK 3 T TENSOR REMARK 3 T11: -0.4100 T22: -0.0926 REMARK 3 T33: 0.2674 T12: 0.1225 REMARK 3 T13: 0.0318 T23: -0.1609 REMARK 3 L TENSOR REMARK 3 L11: 5.5111 L22: 2.9597 REMARK 3 L33: 2.4854 L12: -4.1621 REMARK 3 L13: -2.3648 L23: 0.8174 REMARK 3 S TENSOR REMARK 3 S11: 0.1889 S12: -0.0998 S13: 0.2291 REMARK 3 S21: 0.0382 S22: 0.0059 S23: -0.0014 REMARK 3 S31: -0.1869 S32: -0.4332 S33: -0.1948 REMARK 3 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: {F|4 - 151} REMARK 3 ORIGIN FOR THE GROUP (A): -35.5085 -21.1849 54.3545 REMARK 3 T TENSOR REMARK 3 T11: -0.4233 T22: -0.0582 REMARK 3 T33: 0.2732 T12: 0.0313 REMARK 3 T13: 0.0096 T23: -0.1658 REMARK 3 L TENSOR REMARK 3 L11: 4.4414 L22: 4.0834 REMARK 3 L33: 1.1859 L12: 4.4144 REMARK 3 L13: 1.3269 L23: 1.6038 REMARK 3 S TENSOR REMARK 3 S11: 0.0872 S12: 0.0963 S13: -0.1498 REMARK 3 S21: 0.0496 S22: 0.0168 S23: -0.1529 REMARK 3 S31: 0.1282 S32: -0.5412 S33: -0.1040 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE ROBS, RWORK AND RFREE VALUES ARE REMARK 3 VERY CLOSE DUE TO THE USE OF TARGET RESTRAINTS DURING REFINEMENT REMARK 3 FOR THE FAB MOLECULES TO A PREVIOUSLY-DETERMINED HIGHER REMARK 3 RESOLUTION STRUCTURE (2.3 ANGSTROM; PDB ID 3V6F) (SMART ET AL., REMARK 3 2012) REMARK 4 REMARK 4 3V6Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JAN-12. REMARK 100 THE RCSB ID CODE IS RCSB069673. 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 : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I24 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : NULL 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 : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19664 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.340 REMARK 200 RESOLUTION RANGE LOW (A) : 46.200 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 92.6 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL 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: NULL REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 57.05 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,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 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 300 REMARK: HEPATITIS B VIRUS E-ANTIGEN (HBEAG) IS COMPRISED OF CHAINS REMARK 300 E AND F 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: 5800 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 27150 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5820 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 27140 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, E 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 A 137 REMARK 465 CYS A 138 REMARK 465 GLY A 139 REMARK 465 GLY C 137 REMARK 465 CYS C 138 REMARK 465 GLY C 139 REMARK 465 SER E 1 REMARK 465 LYS E 2 REMARK 465 LEU E 3 REMARK 465 THR E 152 REMARK 465 LEU E 153 REMARK 465 PRO E 154 REMARK 465 GLU E 155 REMARK 465 THR E 156 REMARK 465 THR E 157 REMARK 465 VAL E 158 REMARK 465 VAL E 159 REMARK 465 SER F 1 REMARK 465 LYS F 2 REMARK 465 LEU F 3 REMARK 465 THR F 152 REMARK 465 LEU F 153 REMARK 465 PRO F 154 REMARK 465 GLU F 155 REMARK 465 THR F 156 REMARK 465 THR F 157 REMARK 465 VAL F 158 REMARK 465 VAL F 159 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 LEU A 11 CD1 - CG - CD2 ANGL. DEV. = -19.0 DEGREES REMARK 500 LEU C 11 CD1 - CG - CD2 ANGL. DEV. = -20.0 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 B 32 -25.21 75.04 REMARK 500 ALA B 57 -27.32 65.07 REMARK 500 SER B 100 -15.41 65.82 REMARK 500 MET B 102 77.37 -160.30 REMARK 500 LYS B 176 -70.37 -76.20 REMARK 500 SER D 32 -25.22 74.91 REMARK 500 ALA D 57 -27.27 65.24 REMARK 500 SER D 100 -15.52 65.79 REMARK 500 MET D 102 77.69 -160.22 REMARK 500 LYS D 176 -70.45 -76.08 REMARK 500 LEU E 5 -72.70 -70.96 REMARK 500 PRO E 35 -169.09 -78.26 REMARK 500 HIS E 57 6.25 -150.68 REMARK 500 ALA E 58 87.42 -64.55 REMARK 500 THR E 84 -54.05 -138.15 REMARK 500 LEU E 86 -147.15 -117.69 REMARK 500 SER E 91 -34.96 -153.07 REMARK 500 PRO E 140 154.83 -49.63 REMARK 500 ALA E 141 -45.02 80.95 REMARK 500 LEU F 5 -72.62 -71.13 REMARK 500 PRO F 35 -169.01 -78.40 REMARK 500 HIS F 57 6.25 -150.63 REMARK 500 ALA F 58 87.37 -64.52 REMARK 500 THR F 84 -53.97 -138.10 REMARK 500 LEU F 86 -147.08 -117.77 REMARK 500 SER F 91 -34.96 -153.17 REMARK 500 PRO F 140 154.64 -49.54 REMARK 500 ALA F 141 -44.95 80.97 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CHIRAL CENTERS REMARK 500 REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16) REMARK 500 REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS REMARK 500 SER A 171 21.9 L L OUTSIDE RANGE REMARK 500 THR B 59 24.4 L L OUTSIDE RANGE REMARK 500 SER C 171 21.8 L L OUTSIDE RANGE REMARK 500 THR D 59 24.3 L L OUTSIDE RANGE REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3V6F RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF FAB E6