REMARK 2 REMARK 2 RESOLUTION. 3.70 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) : 3.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 10774 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) : 0.249 REMARK 3 R VALUE (WORKING SET) : 0.245 REMARK 3 FREE R VALUE : 0.323 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 574 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 10 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.70 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.90 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1517 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00 REMARK 3 BIN R VALUE (WORKING SET) : 0.3450 REMARK 3 BIN FREE R VALUE SET COUNT : 95 REMARK 3 BIN FREE R VALUE : 0.4050 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 7149 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 56 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 159.54 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -7.11000 REMARK 3 B22 (A**2) : 2.85000 REMARK 3 B33 (A**2) : -1.63000 REMARK 3 B12 (A**2) : -0.00000 REMARK 3 B13 (A**2) : -4.81000 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): 0.995 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.889 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 136.102 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.922 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.862 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7394 ; 0.008 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 4957 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10064 ; 1.119 ; 1.961 REMARK 3 BOND ANGLES OTHERS (DEGREES): 12092 ; 0.816 ; 3.000 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 931 ; 6.564 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 313 ;35.544 ;24.153 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1177 ;18.147 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 41 ;16.366 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1118 ; 0.058 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8251 ; 0.004 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): 1454 ; 0.001 ; 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): 235 ; 0.152 ; 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): 44 ; 0.166 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 5 ; 0.141 ; 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): 4644 ; 0.465 ; 1.000 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1894 ; 0.047 ; 1.000 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7504 ; 1.088 ; 3.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2750 ; 1.782 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2560 ; 3.154 ; 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 : 10 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 2 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : H 1 H 123 REMARK 3 RESIDUE RANGE : L 1 L 107 REMARK 3 ORIGIN FOR THE GROUP (A): 33.4708 32.8494 -9.0325 REMARK 3 T TENSOR REMARK 3 T11: 0.0793 T22: 0.0746 REMARK 3 T33: 0.1651 T12: -0.0220 REMARK 3 T13: 0.0992 T23: -0.0538 REMARK 3 L TENSOR REMARK 3 L11: 2.2195 L22: 6.3613 REMARK 3 L33: 7.4268 L12: -1.2679 REMARK 3 L13: 2.0905 L23: -0.4395 REMARK 3 S TENSOR REMARK 3 S11: -0.0161 S12: -0.0188 S13: -0.0975 REMARK 3 S21: -0.1337 S22: 0.0276 S23: 0.2719 REMARK 3 S31: 0.1598 S32: 0.5046 S33: -0.0115 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 : H 124 H 230 REMARK 3 RESIDUE RANGE : L 108 L 230 REMARK 3 ORIGIN FOR THE GROUP (A): 43.6656 29.9425 23.1522 REMARK 3 T TENSOR REMARK 3 T11: 0.1652 T22: 0.5362 REMARK 3 T33: 0.0389 T12: -0.0198 REMARK 3 T13: 0.0221 T23: 0.0833 REMARK 3 L TENSOR REMARK 3 L11: 4.7858 L22: 5.3219 REMARK 3 L33: 4.1845 L12: -1.8780 REMARK 3 L13: 0.8870 L23: 1.1314 REMARK 3 S TENSOR REMARK 3 S11: 0.2624 S12: -0.8561 S13: -0.2025 REMARK 3 S21: 0.0147 S22: -0.0749 S23: -0.2144 REMARK 3 S31: -0.2303 S32: 0.6103 S33: -0.1874 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 : A 1 A 190 REMARK 3 ORIGIN FOR THE GROUP (A): -14.3159 -8.5990 -86.2934 REMARK 3 T TENSOR REMARK 3 T11: 0.1571 T22: 0.6856 REMARK 3 T33: 0.3039 T12: -0.1726 REMARK 3 T13: 0.0114 T23: 0.1128 REMARK 3 L TENSOR REMARK 3 L11: 6.4936 L22: 5.5502 REMARK 3 L33: 3.5300 L12: -0.5985 REMARK 3 L13: 1.1239 L23: 1.3045 REMARK 3 S TENSOR REMARK 3 S11: 0.1657 S12: 0.1047 S13: -0.8740 REMARK 3 S21: -0.0471 S22: -0.1439 S23: 0.4533 REMARK 3 S31: 0.2090 S32: -0.3294 S33: -0.0218 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 : A 191 A 207 REMARK 3 ORIGIN FOR THE GROUP (A): -27.5654 16.4310 -95.3811 REMARK 3 T TENSOR REMARK 3 T11: 1.9166 T22: 1.8474 REMARK 3 T33: 1.1446 T12: 0.1789 REMARK 3 T13: 0.2014 T23: 0.0543 REMARK 3 L TENSOR REMARK 3 L11: 5.3929 L22: 7.3001 REMARK 3 L33: 1.2004 L12: 6.2644 REMARK 3 L13: -2.5282 L23: -2.9516 REMARK 3 S TENSOR REMARK 3 S11: -0.6728 S12: 0.6400 S13: 1.3305 REMARK 3 S21: -1.2998 S22: 0.9663 S23: 1.4809 REMARK 3 S31: 0.5788 S32: -0.3656 S33: -0.2935 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 : A 208 A 225 REMARK 3 ORIGIN FOR THE GROUP (A): -26.3442 13.2410 -84.5845 REMARK 3 T TENSOR REMARK 3 T11: 0.4569 T22: 0.8228 REMARK 3 T33: 0.4555 T12: 0.1446 REMARK 3 T13: -0.0690 T23: 0.0651 REMARK 3 L TENSOR REMARK 3 L11: 5.0472 L22: 22.8370 REMARK 3 L33: 18.3072 L12: -0.3602 REMARK 3 L13: -7.3472 L23: -0.8940 REMARK 3 S TENSOR REMARK 3 S11: 0.2935 S12: -0.0154 S13: 0.8031 REMARK 3 S21: 0.3342 S22: 0.0356 S23: 1.3201 REMARK 3 S31: 0.0316 S32: -0.2352 S33: -0.3292 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 : A 226 A 238 REMARK 3 ORIGIN FOR THE GROUP (A): -20.3791 14.2688 -77.1534 REMARK 3 T TENSOR REMARK 3 T11: 0.6054 T22: 1.1475 REMARK 3 T33: 0.5108 T12: -0.0062 REMARK 3 T13: -0.0236 T23: -0.0636 REMARK 3 L TENSOR REMARK 3 L11: 24.8193 L22: 29.4460 REMARK 3 L33: 0.1632 L12: 21.8677 REMARK 3 L13: 1.4054 L23: 2.1574 REMARK 3 S TENSOR REMARK 3 S11: -0.0588 S12: -2.7977 S13: 1.1016 REMARK 3 S21: -1.2214 S22: -0.0438 S23: 0.2291 REMARK 3 S31: -0.1129 S32: 0.0592 S33: 0.1026 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 239 A 269 REMARK 3 ORIGIN FOR THE GROUP (A): -20.5613 22.8784 -63.3953 REMARK 3 T TENSOR REMARK 3 T11: 1.4800 T22: 1.4576 REMARK 3 T33: 1.3025 T12: -0.1538 REMARK 3 T13: 0.3557 T23: -0.0490 REMARK 3 L TENSOR REMARK 3 L11: 10.3261 L22: 0.9108 REMARK 3 L33: 3.3067 L12: 1.9941 REMARK 3 L13: 4.4026 L23: 0.0079 REMARK 3 S TENSOR REMARK 3 S11: 0.3886 S12: -0.9577 S13: 2.0415 REMARK 3 S21: 0.9359 S22: -0.5622 S23: 0.6911 REMARK 3 S31: -1.1503 S32: -0.3949 S33: 0.1736 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 270 A 284 REMARK 3 ORIGIN FOR THE GROUP (A): -9.5711 9.5911 -62.7529 REMARK 3 T TENSOR REMARK 3 T11: 1.2162 T22: 0.6257 REMARK 3 T33: 0.6649 T12: -0.1108 REMARK 3 T13: -0.3786 T23: -0.1530 REMARK 3 L TENSOR REMARK 3 L11: 30.8784 L22: 42.2115 REMARK 3 L33: 12.6943 L12: 4.3442 REMARK 3 L13: -17.5735 L23: -13.0406 REMARK 3 S TENSOR REMARK 3 S11: -1.4558 S12: -2.2993 S13: -0.3221 REMARK 3 S21: 1.6618 S22: 1.5801 S23: 1.0470 REMARK 3 S31: 0.4144 S32: 0.7688 S33: -0.1243 REMARK 3 REMARK 3 TLS GROUP : 9 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 285 A 303 REMARK 3 ORIGIN FOR THE GROUP (A): -5.5736 16.3477 -56.4016 REMARK 3 T TENSOR REMARK 3 T11: 0.7021 T22: 1.0974 REMARK 3 T33: 0.9540 T12: -0.1740 REMARK 3 T13: -0.2533 T23: -0.3845 REMARK 3 L TENSOR REMARK 3 L11: 3.5789 L22: 21.0423 REMARK 3 L33: 6.4188 L12: -8.6108 REMARK 3 L13: -3.3967 L23: 9.1792 REMARK 3 S TENSOR REMARK 3 S11: -0.5939 S12: -0.2616 S13: -0.3947 REMARK 3 S21: 1.2068 S22: 0.3729 S23: 0.9523 REMARK 3 S31: -0.1453 S32: -0.2690 S33: 0.2210 REMARK 3 REMARK 3 TLS GROUP : 10 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 304 A 513 REMARK 3 ORIGIN FOR THE GROUP (A): 20.1072 25.9959 -39.4263 REMARK 3 T TENSOR REMARK 3 T11: 0.1702 T22: 0.2293 REMARK 3 T33: 0.0545 T12: -0.1817 REMARK 3 T13: 0.0413 T23: -0.0675 REMARK 3 L TENSOR REMARK 3 L11: 4.8626 L22: 8.2437 REMARK 3 L33: 6.9601 L12: -0.3208 REMARK 3 L13: 0.7599 L23: 0.1142 REMARK 3 S TENSOR REMARK 3 S11: -0.2240 S12: 0.1361 S13: -0.3162 REMARK 3 S21: -0.3851 S22: 0.3266 S23: 0.1520 REMARK 3 S31: 0.2421 S32: -0.2721 S33: -0.1026 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 3P11 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-OCT-10. REMARK 100 THE RCSB ID CODE IS RCSB061822. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 24-JUN-09 REMARK 200 TEMPERATURE (KELVIN) : 110 REMARK 200 PH : 9 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) : 1.0 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : SI REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13436 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.500 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -2.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 3.500 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.11000 REMARK 200 FOR THE DATA SET : 12.0000 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: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 50.22 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 1500, PH 9, VAPOR DIFFUSION, REMARK 280 SITTING DROP, TEMPERATURE 295K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z 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 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 104.19600 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 24.19850 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 104.19600 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 24.19850 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 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 APPLY THE FOLLOWING TO CHAINS: H, L, A 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 H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 SER H 132 REMARK 465 GLY H 133 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 GLY L 212 REMARK 465 GLU L 213 REMARK 465 CYS L 214 REMARK 465 SER A 1 REMARK 465 GLU A 2 REMARK 465 VAL A 3 REMARK 465 GLY A 4 REMARK 465 ASN A 5 REMARK 465 SER A 6 REMARK 465 GLN A 7 REMARK 465 GLY A 514 REMARK 465 ASN A 515 REMARK 465 SER A 516 REMARK 465 HIS A 517 REMARK 465 HIS A 518 REMARK 465 HIS A 519 REMARK 465 HIS A 520 REMARK 465 HIS A 521 REMARK 465 HIS A 522 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 A 36 N - CA - C ANGL. DEV. = -18.3 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 H 30 112.47 -26.23 REMARK 500 ILE H 51 116.48 -165.55 REMARK 500 ALA H 53 -70.44 -74.45 REMARK 500 SER H 62 -4.95 -51.05 REMARK 500 VAL H 63 -18.39 -150.34 REMARK 500 LYS H 64 98.53 -52.89 REMARK 500 THR H 87 108.64 -55.32 REMARK 500 ALA H 93 130.04 -170.67 REMARK 500 SER H 99 148.23 106.40 REMARK 500 PRO H 126 -167.02 -78.24 REMARK 500 SER H 127 -56.32 84.04 REMARK 500 ASP H 144 84.88 62.34 REMARK 500 GLU H 148 156.53 -49.05 REMARK 500 ASP L 28 109.59 -46.22 REMARK 500 ALA L 30 -89.61 46.25 REMARK 500 PRO L 40 104.27 -45.83 REMARK 500 ALA L 51 -18.59 62.83 REMARK 500 SER L 52 -10.29 -150.78 REMARK 500 GLU L 92 -72.07 -63.22 REMARK 500 ASN L 138 80.25 45.57 REMARK 500 ASN L 152 -5.16 58.29 REMARK 500 GLU L 187 35.55 -72.66 REMARK 500 LYS L 188 27.27 -148.08 REMARK 500 TYR A 34 40.67 -81.72 REMARK 500 GLU A 35 -85.39 -39.01 REMARK 500 LEU A 55 81.07 -49.49 REMARK 500 PHE A 75 159.74 -48.83 REMARK 500 ASP A 93 -41.03 59.72 REMARK 500 ASN A 103 79.07 -111.62 REMARK 500 HIS A 138 -8.62 75.40 REMARK 500 ASN A 160 -132.09 -117.22 REMARK 500 GLN A 206 37.77 -88.91 REMARK 500 PRO A 219 37.23 -86.44 REMARK 500 HIS A 229 -91.67 -136.31 REMARK 500 PRO A 255 99.04 -59.19 REMARK 500 PRO A 272 167.09 -49.97 REMARK 500 GLN A 279 -49.56 45.08 REMARK 500 THR A 280 -50.91 -130.62 REMARK 500 ARG A 284 -75.76 -53.44 REMARK 500 PRO A 288 -5.88 -59.11 REMARK 500 PRO A 309 89.83 -63.83 REMARK 500 LYS A 310 82.72 -67.55 REMARK 500 SER A 327 60.20 -100.68 REMARK 500 ASN A 328 -51.28 -171.73 REMARK 500 THR A 336 -67.02 -103.35 REMARK 500 PHE A 344 74.75 -116.01 REMARK 500 VAL A 367 -39.14 -34.40 REMARK 500 PRO A 384 101.82 -56.85 REMARK 500 PHE A 390 47.07 -91.39 REMARK 500 TYR A 405 -92.00 -105.71 REMARK 500 REMARK 500 THIS ENTRY HAS 56 RAMACHANDRAN OUTLIERS. 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 LYS A 188 THR A 189 144.68 REMARK 500 ILE A 190 CYS A 191 -144.04 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 623 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 624 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 625 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 627 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3P0V RELATED DB: PDB REMARK 900 FAB DL11 ALONE REMARK 900 RELATED ID: 3P0Y RELATED DB: PDB REMARK 900 FAB DL11 WITH EGFR