REMARK 2 REMARK 2 RESOLUTION. 1.95 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.2.0005 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) : 1.95 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7 REMARK 3 NUMBER OF REFLECTIONS : 57365 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) : 0.192 REMARK 3 R VALUE (WORKING SET) : 0.189 REMARK 3 FREE R VALUE : 0.221 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100 REMARK 3 FREE R VALUE TEST SET COUNT : 6425 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) : 1.95 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.99 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2938 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 84.14 REMARK 3 BIN R VALUE (WORKING SET) : 0.2330 REMARK 3 BIN FREE R VALUE SET COUNT : 324 REMARK 3 BIN FREE R VALUE : 0.2750 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6389 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 150 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) : 36.25 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 1.36000 REMARK 3 B22 (A**2) : 0.10000 REMARK 3 B33 (A**2) : -1.02000 REMARK 3 B12 (A**2) : 0.33000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.57000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.176 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.152 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.108 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.739 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.942 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6535 ; 0.008 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 5725 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8900 ; 1.192 ; 1.952 REMARK 3 BOND ANGLES OTHERS (DEGREES): 13408 ; 0.721 ; 3.000 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 842 ; 6.021 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 247 ;35.667 ;24.372 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1026 ;15.204 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 26 ;20.308 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1019 ; 0.074 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7284 ; 0.003 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1268 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 949 ; 0.185 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 5289 ; 0.180 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2994 ; 0.172 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): 3994 ; 0.080 ; 0.200 REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 208 ; 0.140 ; 0.200 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): 15 ; 0.179 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): 72 ; 0.233 ; 0.200 REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 5 ; 0.419 ; 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): 5387 ; 2.616 ; 2.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1725 ; 0.471 ; 2.500 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6835 ; 3.331 ; 5.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2748 ; 2.462 ; 2.500 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2065 ; 3.519 ; 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 : NULL 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 2 A 109 REMARK 3 ORIGIN FOR THE GROUP (A): 5.6325 -9.0664 -15.0378 REMARK 3 T TENSOR REMARK 3 T11: -0.0448 T22: -0.0907 REMARK 3 T33: -0.1282 T12: -0.0065 REMARK 3 T13: -0.0032 T23: 0.0005 REMARK 3 L TENSOR REMARK 3 L11: 1.2399 L22: 2.6145 REMARK 3 L33: 6.0470 L12: -0.6953 REMARK 3 L13: 1.2377 L23: -2.0703 REMARK 3 S TENSOR REMARK 3 S11: 0.0222 S12: 0.1704 S13: -0.0151 REMARK 3 S21: -0.1710 S22: -0.0840 S23: -0.0352 REMARK 3 S31: 0.0855 S32: 0.1385 S33: 0.0618 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 110 A 212 REMARK 3 ORIGIN FOR THE GROUP (A): -4.7040 21.9189 0.8153 REMARK 3 T TENSOR REMARK 3 T11: -0.1524 T22: -0.1683 REMARK 3 T33: 0.0175 T12: 0.0350 REMARK 3 T13: 0.0312 T23: 0.0189 REMARK 3 L TENSOR REMARK 3 L11: 1.1331 L22: 4.9068 REMARK 3 L33: 3.9785 L12: -0.0175 REMARK 3 L13: 0.1744 L23: 1.5132 REMARK 3 S TENSOR REMARK 3 S11: 0.1058 S12: 0.0214 S13: 0.1288 REMARK 3 S21: -0.0449 S22: 0.0181 S23: -0.1660 REMARK 3 S31: -0.1260 S32: 0.0220 S33: -0.1240 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 : B 1 B 114 REMARK 3 ORIGIN FOR THE GROUP (A): 7.7129 -16.6993 6.0880 REMARK 3 T TENSOR REMARK 3 T11: -0.1914 T22: -0.1846 REMARK 3 T33: -0.1223 T12: 0.0080 REMARK 3 T13: 0.0117 T23: -0.0118 REMARK 3 L TENSOR REMARK 3 L11: 1.1030 L22: 2.3107 REMARK 3 L33: 2.3675 L12: 0.2334 REMARK 3 L13: 0.0970 L23: 0.3346 REMARK 3 S TENSOR REMARK 3 S11: -0.0335 S12: 0.0221 S13: -0.0469 REMARK 3 S21: -0.2689 S22: 0.0060 S23: -0.0300 REMARK 3 S31: 0.0162 S32: -0.0346 S33: 0.0275 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 : B 115 B 214 REMARK 3 ORIGIN FOR THE GROUP (A): -11.7546 9.7820 9.5830 REMARK 3 T TENSOR REMARK 3 T11: -0.1416 T22: -0.1571 REMARK 3 T33: 0.0030 T12: 0.0163 REMARK 3 T13: 0.0300 T23: 0.0186 REMARK 3 L TENSOR REMARK 3 L11: 2.7404 L22: 2.8330 REMARK 3 L33: 3.5011 L12: -1.1734 REMARK 3 L13: 2.1125 L23: -1.4562 REMARK 3 S TENSOR REMARK 3 S11: -0.0150 S12: -0.0384 S13: -0.0276 REMARK 3 S21: 0.0284 S22: 0.2355 S23: 0.3239 REMARK 3 S31: -0.0491 S32: -0.1895 S33: -0.2204 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 : L 1 L 109 REMARK 3 ORIGIN FOR THE GROUP (A): -9.3810 -32.4069 45.4477 REMARK 3 T TENSOR REMARK 3 T11: 0.0416 T22: -0.0354 REMARK 3 T33: -0.1193 T12: 0.0409 REMARK 3 T13: 0.0043 T23: 0.0516 REMARK 3 L TENSOR REMARK 3 L11: 2.0718 L22: 1.8007 REMARK 3 L33: 5.5883 L12: -0.1807 REMARK 3 L13: 0.3809 L23: -0.8969 REMARK 3 S TENSOR REMARK 3 S11: -0.1233 S12: -0.2651 S13: -0.0634 REMARK 3 S21: 0.1986 S22: 0.0263 S23: 0.0030 REMARK 3 S31: -0.0335 S32: 0.1448 S33: 0.0970 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 : L 110 L 210 REMARK 3 ORIGIN FOR THE GROUP (A): 0.6021 1.5534 54.6155 REMARK 3 T TENSOR REMARK 3 T11: 0.5001 T22: 0.3126 REMARK 3 T33: 0.0398 T12: -0.1668 REMARK 3 T13: 0.1479 T23: -0.2792 REMARK 3 L TENSOR REMARK 3 L11: 2.8344 L22: 9.6017 REMARK 3 L33: 8.5364 L12: 1.2488 REMARK 3 L13: -0.3572 L23: -5.5825 REMARK 3 S TENSOR REMARK 3 S11: 0.3803 S12: -0.7333 S13: 0.5947 REMARK 3 S21: 1.3227 S22: -0.0936 S23: 0.6253 REMARK 3 S31: -1.9370 S32: 0.1934 S33: -0.2868 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 : H 1 H 114 REMARK 3 ORIGIN FOR THE GROUP (A): -11.2526 -23.6052 24.7486 REMARK 3 T TENSOR REMARK 3 T11: -0.1812 T22: -0.1155 REMARK 3 T33: -0.1161 T12: -0.0224 REMARK 3 T13: -0.0070 T23: 0.0184 REMARK 3 L TENSOR REMARK 3 L11: 1.5164 L22: 3.2770 REMARK 3 L33: 2.2228 L12: -0.5327 REMARK 3 L13: -0.1534 L23: -0.1377 REMARK 3 S TENSOR REMARK 3 S11: -0.0279 S12: -0.0602 S13: -0.0952 REMARK 3 S21: 0.2165 S22: -0.0939 S23: -0.1050 REMARK 3 S31: 0.2027 S32: 0.1127 S33: 0.1218 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 : H 115 H 213 REMARK 3 ORIGIN FOR THE GROUP (A): 7.9358 -2.0092 40.1021 REMARK 3 T TENSOR REMARK 3 T11: -0.0472 T22: 0.1759 REMARK 3 T33: -0.0507 T12: -0.1454 REMARK 3 T13: 0.0019 T23: -0.0762 REMARK 3 L TENSOR REMARK 3 L11: 2.7200 L22: 2.0267 REMARK 3 L33: 9.7750 L12: -0.2193 REMARK 3 L13: 1.9191 L23: -1.5350 REMARK 3 S TENSOR REMARK 3 S11: 0.1234 S12: -0.3692 S13: 0.3378 REMARK 3 S21: 0.2762 S22: -0.1526 S23: 0.0390 REMARK 3 S31: -0.5230 S32: 1.2129 S33: 0.0293 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 2HFF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUN-06. REMARK 100 THE RCSB ID CODE IS RCSB038287. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 12-JUN-04 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 19-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9804 REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SAGITTALLY REMARK 200 FOCUSED MONOCHROMATOR REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : CUSTOM-MADE REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63805 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0 REMARK 200 DATA REDUNDANCY : 3.400 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.07400 REMARK 200 FOR THE DATA SET : 6.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02 REMARK 200 COMPLETENESS FOR SHELL (%) : 91.8 REMARK 200 DATA REDUNDANCY IN SHELL : 2.50 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.36600 REMARK 200 FOR SHELL : 1.800 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: AMORE REMARK 200 STARTING MODEL: CHAINS A,B FROM PDB 2HG9 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 49.21 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS WERE GROWN IN HANGING DROPS REMARK 280 WITH 1:1 RATIO OF PROTEIN TO WELL SOLUTION CONSISTING OF 100 MM REMARK 280 HEPES, PH 7.5, 20% PEG 10K, AND THEN FROZEN IN MOTHER LIQUOR WITH REMARK 280 25% PEG 400 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: THE CRYSATLLOGRAPHIC ASSYMMETRIC UNIT CONTAINS TWO REMARK 300 BIOLOGICALLY RELEVANT ASSEMBLIES COMPOSED OF CHAINS A,B AND H,L REMARK 300 RESPECTIVELY 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3280 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19020 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3270 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18870 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 ASP A 1 REMARK 465 ASN B 98A REMARK 465 ARG B 98B REMARK 465 LEU B 98C REMARK 465 GLY B 98D REMARK 465 VAL B 98E REMARK 465 CYS B 98F REMARK 465 SER B 128 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 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 GLY L 211 REMARK 465 GLU L 212 REMARK 465 CYS L 213 REMARK 465 TYR H 97A REMARK 465 ASN H 97B REMARK 465 ARG H 97C REMARK 465 LEU H 97D REMARK 465 GLY H 97E REMARK 465 VAL H 97F REMARK 465 CYS H 97G REMARK 465 SER H 128 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 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 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 470 CYS H 97 SG REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH A 232 O HOH L 221 1554 1.85 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 ARG B 95 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 ARG B 95 NE - CZ - NH2 ANGL. DEV. = -3.1 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 -112.75 45.44 REMARK 500 ALA A 51 -38.99 73.38 REMARK 500 SER A 155 -87.78 -102.86 REMARK 500 ASN A 157 23.37 -141.78 REMARK 500 GLU A 212 65.22 33.69 REMARK 500 ALA B 88 162.75 178.81 REMARK 500 SER L 30 -126.00 58.54 REMARK 500 ALA L 51 -42.77 77.61 REMARK 500 ALA L 84 174.76 178.66 REMARK 500 ASN L 137 74.23 55.27 REMARK 500 SER L 155 -81.94 -69.78 REMARK 500 THR H 191 -60.20 -128.50 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2HFG RELATED DB: PDB