REMARK 2 REMARK 2 RESOLUTION. 2.90 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) : 2.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 33988 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) : 0.222 REMARK 3 R VALUE (WORKING SET) : 0.236 REMARK 3 FREE R VALUE : 0.277 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1711 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) : 2.90 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.96 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1850 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.36 REMARK 3 BIN R VALUE (WORKING SET) : 0.3760 REMARK 3 BIN FREE R VALUE SET COUNT : 102 REMARK 3 BIN FREE R VALUE : 0.4050 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 7770 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 40 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) : 57.13 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.48000 REMARK 3 B22 (A**2) : -4.19000 REMARK 3 B33 (A**2) : 4.67000 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): 1.776 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.407 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.304 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 34.265 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.927 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.886 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8024 ; 0.009 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 5412 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10937 ; 1.210 ; 1.958 REMARK 3 BOND ANGLES OTHERS (DEGREES): 13133 ; 0.846 ; 3.008 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1005 ; 6.756 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 348 ;36.357 ;24.138 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1253 ;15.444 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 44 ;14.469 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1208 ; 0.070 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8949 ; 0.003 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1568 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1530 ; 0.207 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 5586 ; 0.185 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3800 ; 0.176 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): 4331 ; 0.083 ; 0.200 REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 149 ; 0.138 ; 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): 9 ; 0.189 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): 15 ; 0.164 ; 0.200 REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 2 ; 0.296 ; 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): 5401 ; 2.728 ; 2.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2052 ; 0.464 ; 2.500 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8131 ; 4.227 ; 5.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3291 ; 2.402 ; 2.500 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2806 ; 3.741 ; 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 : H 1 H 114 REMARK 3 ORIGIN FOR THE GROUP (A): 29.7944 -19.4991 86.4199 REMARK 3 T TENSOR REMARK 3 T11: 0.2173 T22: -0.0205 REMARK 3 T33: -0.1547 T12: 0.0147 REMARK 3 T13: -0.0039 T23: 0.0388 REMARK 3 L TENSOR REMARK 3 L11: 3.1396 L22: 1.2177 REMARK 3 L33: 3.0757 L12: -0.4194 REMARK 3 L13: 2.1476 L23: 0.3570 REMARK 3 S TENSOR REMARK 3 S11: -0.2968 S12: 0.2112 S13: 0.1829 REMARK 3 S21: -0.2307 S22: 0.1503 S23: 0.1922 REMARK 3 S31: -0.3832 S32: 0.0143 S33: 0.1465 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 : H 115 H 215 REMARK 3 ORIGIN FOR THE GROUP (A): 30.9774 11.1172 96.6333 REMARK 3 T TENSOR REMARK 3 T11: 0.6142 T22: -0.4985 REMARK 3 T33: 0.5217 T12: 0.1456 REMARK 3 T13: -0.4472 T23: -0.0329 REMARK 3 L TENSOR REMARK 3 L11: 5.3815 L22: 3.3279 REMARK 3 L33: 1.2477 L12: 4.2304 REMARK 3 L13: 1.4682 L23: 1.1094 REMARK 3 S TENSOR REMARK 3 S11: -0.6556 S12: -0.2077 S13: 0.9928 REMARK 3 S21: -0.3479 S22: -0.0627 S23: 0.7108 REMARK 3 S31: -0.9371 S32: 0.0292 S33: 0.7184 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 : L 1 L 109 REMARK 3 ORIGIN FOR THE GROUP (A): 43.8698 -21.1832 103.6787 REMARK 3 T TENSOR REMARK 3 T11: 0.1548 T22: 0.0196 REMARK 3 T33: -0.1747 T12: -0.0009 REMARK 3 T13: 0.0723 T23: 0.0085 REMARK 3 L TENSOR REMARK 3 L11: 2.1178 L22: 2.8866 REMARK 3 L33: 3.2055 L12: 0.9418 REMARK 3 L13: 2.0106 L23: 1.8968 REMARK 3 S TENSOR REMARK 3 S11: 0.1894 S12: 0.0139 S13: -0.0446 REMARK 3 S21: 0.0792 S22: 0.0134 S23: 0.0244 REMARK 3 S31: -0.1064 S32: 0.1430 S33: -0.2028 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 : L 110 L 212 REMARK 3 ORIGIN FOR THE GROUP (A): 29.7138 12.3864 113.4280 REMARK 3 T TENSOR REMARK 3 T11: 0.5511 T22: -0.1081 REMARK 3 T33: 0.5100 T12: 0.3969 REMARK 3 T13: -0.2773 T23: -0.5922 REMARK 3 L TENSOR REMARK 3 L11: 0.3428 L22: 3.3432 REMARK 3 L33: 1.0378 L12: -1.0705 REMARK 3 L13: 0.5964 L23: -1.8627 REMARK 3 S TENSOR REMARK 3 S11: -0.2965 S12: -0.1750 S13: 0.3310 REMARK 3 S21: 0.2064 S22: -0.0493 S23: 0.6930 REMARK 3 S31: -0.4743 S32: -0.1829 S33: 0.3458 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 1 A 195 REMARK 3 ORIGIN FOR THE GROUP (A): -22.0268 -24.8261 39.5992 REMARK 3 T TENSOR REMARK 3 T11: -0.0267 T22: 0.0288 REMARK 3 T33: 0.0788 T12: -0.0207 REMARK 3 T13: -0.0119 T23: 0.0310 REMARK 3 L TENSOR REMARK 3 L11: 2.0876 L22: 1.0365 REMARK 3 L33: 0.1507 L12: 0.0911 REMARK 3 L13: 0.3419 L23: 0.0411 REMARK 3 S TENSOR REMARK 3 S11: -0.0603 S12: 0.2082 S13: -0.0122 REMARK 3 S21: -0.0185 S22: 0.0617 S23: -0.0109 REMARK 3 S31: -0.0251 S32: 0.0205 S33: -0.0014 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 : A 196 A 320 REMARK 3 RESIDUE RANGE : A 1001 A 1001 REMARK 3 ORIGIN FOR THE GROUP (A): -7.9660 -7.3859 57.0914 REMARK 3 T TENSOR REMARK 3 T11: -0.0197 T22: -0.0150 REMARK 3 T33: 0.1375 T12: 0.0231 REMARK 3 T13: 0.0062 T23: 0.0016 REMARK 3 L TENSOR REMARK 3 L11: 0.3893 L22: 2.0757 REMARK 3 L33: 0.2710 L12: -0.1593 REMARK 3 L13: 0.2549 L23: 0.3531 REMARK 3 S TENSOR REMARK 3 S11: -0.0912 S12: 0.0055 S13: 0.0691 REMARK 3 S21: 0.2203 S22: 0.0844 S23: 0.0127 REMARK 3 S31: -0.0053 S32: -0.0222 S33: 0.0068 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 321 A 488 REMARK 3 ORIGIN FOR THE GROUP (A): 7.0973 -38.7217 51.6103 REMARK 3 T TENSOR REMARK 3 T11: -0.0124 T22: -0.0328 REMARK 3 T33: 0.1244 T12: 0.0100 REMARK 3 T13: -0.0567 T23: -0.0245 REMARK 3 L TENSOR REMARK 3 L11: 1.3097 L22: 1.1772 REMARK 3 L33: 0.5752 L12: 0.3309 REMARK 3 L13: -0.1491 L23: -0.1827 REMARK 3 S TENSOR REMARK 3 S11: -0.0255 S12: 0.0520 S13: -0.0633 REMARK 3 S21: 0.1222 S22: 0.0517 S23: -0.0810 REMARK 3 S31: 0.0235 S32: -0.0049 S33: -0.0262 REMARK 3 REMARK 3 TLS GROUP : 8 REMARK 3 NUMBER OF COMPONENTS GROUP : 2 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 489 A 607 REMARK 3 RESIDUE RANGE : A 1002 A 1002 REMARK 3 ORIGIN FOR THE GROUP (A): 28.3618 -45.0651 82.0399 REMARK 3 T TENSOR REMARK 3 T11: 0.1732 T22: 0.0523 REMARK 3 T33: -0.0850 T12: 0.1355 REMARK 3 T13: -0.0948 T23: -0.1061 REMARK 3 L TENSOR REMARK 3 L11: 2.5972 L22: 0.7191 REMARK 3 L33: 2.4049 L12: 0.7931 REMARK 3 L13: 2.4935 L23: 0.8339 REMARK 3 S TENSOR REMARK 3 S11: 0.1291 S12: 0.2237 S13: -0.1703 REMARK 3 S21: 0.2505 S22: 0.2294 S23: 0.0561 REMARK 3 S31: 0.2136 S32: 0.2414 S33: -0.3585 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 3BE1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-NOV-07. REMARK 100 THE RCSB ID CODE IS RCSB045402. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 13-JUL-06 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.0 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) : 1.00 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : AREA DETECTOR REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL REMARK 200 DATA SCALING SOFTWARE : HKL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34149 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900 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 (%) : 100.0 REMARK 200 DATA REDUNDANCY : 5.700 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.09500 REMARK 200 FOR THE DATA SET : 18.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 5.80 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.65800 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: PDB ENTRY 3BDY REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 61.34 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.18 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS OF THE FAB/HER2 COMPLEX WERE REMARK 280 OBTAINED BY MIXING PROTEIN SOLUTION (11 MG/ML PROTEIN, 25 MM TRIS REMARK 280 -HCL PH 8 AND 150 MM SODIUM CHLORIDE) WITH CRYSTALLIZATION BUFFER REMARK 280 CONTAINING 25% W/V PEG2000, 0.1M MES PH 6.5. BEFORE DATA REMARK 280 COLLECTION THE CRYSTALS WERE FLASH FROZEN IN LIQUID NITROGEN WITH REMARK 280 20% ETHYLENE GLYCOL AS CRYO-PROTECTANT, PH 8.0, VAPOR DIFFUSION, REMARK 280 HANGING DROP, 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 31.16200 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 104.08550 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 57.52800 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 104.08550 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.16200 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 57.52800 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: A, H, 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 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 LEU A 101 REMARK 465 ASN A 102 REMARK 465 ASN A 103 REMARK 465 THR A 104 REMARK 465 THR A 105 REMARK 465 PRO A 106 REMARK 465 VAL A 107 REMARK 465 THR A 108 REMARK 465 GLY A 109 REMARK 465 ALA A 110 REMARK 465 ASP A 362 REMARK 465 PRO A 363 REMARK 465 ALA A 364 REMARK 465 SER A 365 REMARK 465 GLY A 581 REMARK 465 VAL A 582 REMARK 465 LYS A 583 REMARK 465 PRO A 584 REMARK 465 ASP A 585 REMARK 465 LEU A 586 REMARK 465 SER A 587 REMARK 465 TYR A 588 REMARK 465 MET A 589 REMARK 465 PRO A 590 REMARK 465 CYS A 608 REMARK 465 THR A 609 REMARK 465 HIS A 610 REMARK 465 SER A 611 REMARK 465 CYS A 612 REMARK 465 VAL A 613 REMARK 465 ASP A 614 REMARK 465 LEU A 615 REMARK 465 ASP A 616 REMARK 465 ASP A 617 REMARK 465 LYS A 618 REMARK 465 GLY A 619 REMARK 465 CYS A 620 REMARK 465 PRO A 621 REMARK 465 ALA A 622 REMARK 465 GLU A 623 REMARK 465 GLN A 624 REMARK 465 GLU H -2 REMARK 465 ILE H -1 REMARK 465 SER H 0 REMARK 465 SER H 129 REMARK 465 SER H 130 REMARK 465 LYS H 131 REMARK 465 SER H 132 REMARK 465 THR H 133 REMARK 465 SER H 134 REMARK 465 GLY H 135 REMARK 465 LYS H 216 REMARK 465 SER H 217 REMARK 465 CYS H 218 REMARK 465 ASP H 219 REMARK 465 LYS H 220 REMARK 465 THR H 221 REMARK 465 HIS H 222 REMARK 465 GLU L 213 REMARK 465 CYS L 214 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 ARG L 27D CG CD NE CZ NH1 NH2 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 OE1 GLU A 125 O ALA A 219 1.96 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 ASP A 8 78.23 -156.16 REMARK 500 LYS A 10 -123.99 49.30 REMARK 500 THR A 45 -50.61 -19.58 REMARK 500 LEU A 74 40.42 -106.15 REMARK 500 ASN A 89 -40.80 -155.87 REMARK 500 TYR A 141 -12.57 72.13 REMARK 500 LYS A 178 -84.17 -10.74 REMARK 500 ARG A 195 -47.02 -132.33 REMARK 500 CYS A 213 125.85 -6.13 REMARK 500 HIS A 215 154.92 -31.94 REMARK 500 HIS A 235 -76.36 -137.06 REMARK 500 VAL A 286 -8.19 -58.86 REMARK 500 VAL A 292 128.08 -179.66 REMARK 500 LEU A 295 153.91 -45.20 REMARK 500 GLU A 326 -122.12 38.67 REMARK 500 ALA A 343 115.48 -39.49 REMARK 500 PHE A 359 -93.75 -93.12 REMARK 500 ASP A 360 77.28 -41.37 REMARK 500 LEU A 400 42.43 -106.31 REMARK 500 ALA A 418 -51.09 -121.47 REMARK 500 ARG A 495 -2.17 61.16 REMARK 500 GLN A 511 -99.10 -101.34 REMARK 500 HIS A 567 -101.66 -126.03 REMARK 500 GLU A 598 34.28 -87.76 REMARK 500 SER H 25 137.36 -174.23 REMARK 500 ARG H 66 -46.28 -148.03 REMARK 500 ASP H 146 78.73 62.06 REMARK 500 PRO H 151 -159.67 -101.84 REMARK 500 SER H 155 111.52 -164.03 REMARK 500 ASN H 157 -161.96 72.88 REMARK 500 SER H 158 -78.72 -66.23 REMARK 500 SER H 190 -59.08 -164.36 REMARK 500 LEU H 191 -84.41 22.73 REMARK 500 THR H 193 -58.03 -142.56 REMARK 500 GLN H 194 -87.28 -85.85 REMARK 500 THR H 195 145.01 165.52 REMARK 500 ASN H 206 5.00 56.52 REMARK 500 PRO L 27C -78.51 -72.59 REMARK 500 ARG L 27D -113.38 62.57 REMARK 500 SER L 28 95.76 -164.41 REMARK 500 SER L 30 -68.84 -18.68 REMARK 500 SER L 77 76.23 -151.16 REMARK 500 ALA L 84 -179.94 178.77 REMARK 500 THR L 109 127.33 -39.17 REMARK 500 SER L 127 -60.65 -160.73 REMARK 500 ASN L 138 67.57 34.56 REMARK 500 ASP L 151 -80.04 60.87 REMARK 500 LYS L 169 -67.14 -108.66 REMARK 500 SER L 182 -161.20 -75.85 REMARK 500 ALA L 184 -71.20 -58.41 REMARK 500 REMARK 500 THIS ENTRY HAS 52 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 GLY A 427 ILE A 428 144.51 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 1001 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES L 215 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3BDY RELATED DB: PDB REMARK 900 RELATED ID: 2JPA RELATED DB: PDB REMARK 900 RELATED ID: 2JP9 RELATED DB: PDB