REMARK 2 REMARK 2 RESOLUTION. 4.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.7.0029 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) : 4.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.08 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 3 NUMBER OF REFLECTIONS : 11259 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) : 0.291 REMARK 3 R VALUE (WORKING SET) : 0.289 REMARK 3 FREE R VALUE : 0.349 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800 REMARK 3 FREE R VALUE TEST SET COUNT : 538 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 4.30 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 4.41 REMARK 3 REFLECTION IN BIN (WORKING SET) : 763 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00 REMARK 3 BIN R VALUE (WORKING SET) : 0.3320 REMARK 3 BIN FREE R VALUE SET COUNT : 46 REMARK 3 BIN FREE R VALUE : 0.4300 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4454 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 117 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) : 238.76 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.00000 REMARK 3 B22 (A**2) : 0.00000 REMARK 3 B33 (A**2) : 0.00000 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): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 0.998 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.857 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 157.305 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.885 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.831 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4698 ; 0.010 ; 0.019 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6387 ; 1.641 ; 1.985 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 557 ; 6.995 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 207 ;36.670 ;24.300 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 768 ;19.274 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 23 ;18.521 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 719 ; 0.104 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3497 ; 0.005 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL 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): NULL ; NULL ; NULL 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): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL 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): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL 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 : 6 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 : E 5 E 310 REMARK 3 RESIDUE RANGE : E 401 E 409 REMARK 3 ORIGIN FOR THE GROUP (A): 29.0110 20.6711 69.9892 REMARK 3 T TENSOR REMARK 3 T11: 0.9519 T22: 0.6100 REMARK 3 T33: 0.5631 T12: 0.0405 REMARK 3 T13: 0.1735 T23: 0.0883 REMARK 3 L TENSOR REMARK 3 L11: 1.9974 L22: 4.0538 REMARK 3 L33: 3.5253 L12: -0.5271 REMARK 3 L13: 1.0186 L23: -1.5577 REMARK 3 S TENSOR REMARK 3 S11: 0.0200 S12: -0.0233 S13: 0.2538 REMARK 3 S21: -0.0851 S22: -0.1329 S23: -0.3328 REMARK 3 S31: 0.1390 S32: 0.3646 S33: 0.1129 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 : C 1 C 116 REMARK 3 ORIGIN FOR THE GROUP (A): 23.7216 24.9254 110.2745 REMARK 3 T TENSOR REMARK 3 T11: 1.4186 T22: 1.3372 REMARK 3 T33: 0.5628 T12: 0.5296 REMARK 3 T13: -0.1709 T23: -0.4041 REMARK 3 L TENSOR REMARK 3 L11: 2.8479 L22: 11.0906 REMARK 3 L33: 9.7993 L12: -0.4492 REMARK 3 L13: 0.4127 L23: 0.7678 REMARK 3 S TENSOR REMARK 3 S11: -0.4002 S12: -1.2298 S13: 0.8319 REMARK 3 S21: 1.2423 S22: 0.6601 S23: -0.9499 REMARK 3 S31: -1.8834 S32: -0.2182 S33: -0.2598 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 : D 1 D 114 REMARK 3 ORIGIN FOR THE GROUP (A): 9.5930 9.7163 103.8221 REMARK 3 T TENSOR REMARK 3 T11: 1.0914 T22: 1.8360 REMARK 3 T33: 0.1749 T12: 0.2528 REMARK 3 T13: -0.0641 T23: 0.4602 REMARK 3 L TENSOR REMARK 3 L11: 6.4346 L22: 7.1817 REMARK 3 L33: 1.6695 L12: 3.1292 REMARK 3 L13: -0.3488 L23: 2.3949 REMARK 3 S TENSOR REMARK 3 S11: -0.0542 S12: -0.5603 S13: 0.3559 REMARK 3 S21: 0.8683 S22: 0.2457 S23: 0.3608 REMARK 3 S31: 0.3066 S32: -0.6527 S33: -0.1915 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 1 A 21 REMARK 3 ORIGIN FOR THE GROUP (A): 22.1987 36.5549 42.7027 REMARK 3 T TENSOR REMARK 3 T11: 0.9512 T22: 0.7076 REMARK 3 T33: 1.0784 T12: 0.3682 REMARK 3 T13: 0.6285 T23: 0.0262 REMARK 3 L TENSOR REMARK 3 L11: 36.1603 L22: 21.9651 REMARK 3 L33: 32.0445 L12: 10.5898 REMARK 3 L13: 12.7605 L23: -19.0556 REMARK 3 S TENSOR REMARK 3 S11: 0.0521 S12: 0.1126 S13: 3.0663 REMARK 3 S21: 0.0796 S22: 0.7400 S23: 2.4276 REMARK 3 S31: 0.0060 S32: -0.8875 S33: -0.7921 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 : B 7 B 21 REMARK 3 ORIGIN FOR THE GROUP (A): 31.7255 32.2463 43.2281 REMARK 3 T TENSOR REMARK 3 T11: 2.3177 T22: 3.4397 REMARK 3 T33: 0.8610 T12: 1.6314 REMARK 3 T13: 0.4305 T23: 0.3113 REMARK 3 L TENSOR REMARK 3 L11: 14.8872 L22: 3.0510 REMARK 3 L33: 3.0429 L12: -6.5429 REMARK 3 L13: 6.5144 L23: -2.7385 REMARK 3 S TENSOR REMARK 3 S11: 1.7280 S12: 1.6628 S13: 0.3947 REMARK 3 S21: -1.2128 S22: -1.5249 S23: -0.2527 REMARK 3 S31: 0.5470 S32: 0.1764 S33: -0.2031 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 : F 705 F 715 REMARK 3 ORIGIN FOR THE GROUP (A): 22.7019 27.5001 51.7357 REMARK 3 T TENSOR REMARK 3 T11: 1.6323 T22: 0.9297 REMARK 3 T33: 0.8640 T12: 0.1313 REMARK 3 T13: 0.0973 T23: 0.2564 REMARK 3 L TENSOR REMARK 3 L11: 12.5839 L22: 7.0083 REMARK 3 L33: 27.2169 L12: 5.9820 REMARK 3 L13: -11.3383 L23: 3.0172 REMARK 3 S TENSOR REMARK 3 S11: 1.2487 S12: -0.0612 S13: -0.8971 REMARK 3 S21: -0.0382 S22: -0.0288 S23: -1.3790 REMARK 3 S31: -2.2847 S32: 0.0373 S33: -1.2199 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: U VALUES: WITH TLS ADDED REMARK 4 REMARK 4 3W12 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-NOV-12. REMARK 100 THE RCSB ID CODE IS RCSB095751. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 20-MAR-12 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 : 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) : 0.9686 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11280 REMARK 200 RESOLUTION RANGE HIGH (A) : 4.301 REMARK 200 RESOLUTION RANGE LOW (A) : 169.488 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 200 DATA REDUNDANCY : 8.800 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.18800 REMARK 200 FOR THE DATA SET : 7.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.53 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 8.80 REMARK 200 R MERGE FOR SHELL (I) : 2.69700 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.000 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: 3LOH, 2WRW REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 79.75 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 6.07 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.9-1.1M TRI-SODIUM CITRATE, 0.1M REMARK 280 IMIDAZOLE-HCL, 0.02% SODIUM AZIDE, PH 8.0 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 3 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,Y,-Z REMARK 290 4555 X,-Y,-Z REMARK 290 5555 Z,X,Y REMARK 290 6555 Z,-X,-Y REMARK 290 7555 -Z,-X,Y REMARK 290 8555 -Z,X,-Y REMARK 290 9555 Y,Z,X REMARK 290 10555 -Y,Z,-X REMARK 290 11555 Y,-Z,-X REMARK 290 12555 -Y,-Z,X 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 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 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: HEXAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 8640 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 27370 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, C, D, 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 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 HIS E 1 REMARK 465 LEU E 2 REMARK 465 TYR E 3 REMARK 465 PRO E 4 REMARK 465 PRO E 160 REMARK 465 GLY E 161 REMARK 465 THR E 162 REMARK 465 ALA E 163 REMARK 465 LYS E 164 REMARK 465 GLY E 165 REMARK 465 LYS E 166 REMARK 465 THR E 167 REMARK 465 CYS E 266 REMARK 465 LYS E 267 REMARK 465 ASN E 268 REMARK 465 SER E 269 REMARK 465 ARG E 270 REMARK 465 ARG E 271 REMARK 465 GLN E 272 REMARK 465 GLY E 273 REMARK 465 CYS E 274 REMARK 465 HIS E 275 REMARK 465 PHE B 1 REMARK 465 VAL B 2 REMARK 465 ASN B 3 REMARK 465 GLN B 4 REMARK 465 HIS B 5 REMARK 465 LEU B 6 REMARK 465 ARG B 22 REMARK 465 GLY B 23 REMARK 465 PHE B 24 REMARK 465 PHE B 25 REMARK 465 PR9 B 26 REMARK 465 THR F 704 REMARK 465 PRO F 716 REMARK 465 ARG F 717 REMARK 465 PRO F 718 REMARK 465 SER F 719 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 CG2 ILE D 2 OG SER D 26 2.08 REMARK 500 O SER E 198 O LEU E 213 2.10 REMARK 500 CD ARG D 67 O SER D 82 2.11 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 CYS E 259 CA - CB - SG ANGL. DEV. = 6.8 DEGREES REMARK 500 CYS E 308 CA - CB - SG ANGL. DEV. = 7.9 DEGREES REMARK 500 CYS D 94 CA - CB - SG ANGL. DEV. = 6.8 DEGREES REMARK 500 VAL F 715 CG1 - CB - CG2 ANGL. DEV. = -10.4 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 ASN E 15 -80.84 71.24 REMARK 500 ASP E 59 -92.26 -101.84 REMARK 500 PHE E 89 -103.08 58.73 REMARK 500 GLU E 97 51.51 36.39 REMARK 500 HIS E 100 -19.46 103.20 REMARK 500 ARG E 114 -101.81 65.24 REMARK 500 GLU E 124 -28.15 92.99 REMARK 500 CYS E 126 -162.34 -118.42 REMARK 500 GLU E 153 7.51 46.71 REMARK 500 GLU E 154 70.37 -119.88 REMARK 500 ASN E 175 -128.87 -103.93 REMARK 500 LYS E 197 -130.18 54.53 REMARK 500 LEU E 213 -86.67 -95.06 REMARK 500 ALA E 227 108.10 -164.30 REMARK 500 ASN E 230 -90.29 -93.46 REMARK 500 GLN E 249 19.64 59.53 REMARK 500 TRP E 251 -20.42 -157.39 REMARK 500 HIS E 264 92.37 -69.02 REMARK 500 LEU E 299 -1.74 62.32 REMARK 500 PRO C 14 153.62 -48.06 REMARK 500 SER C 15 -8.51 74.06 REMARK 500 LYS C 43 -169.29 -107.95 REMARK 500 SER C 84 73.01 39.15 REMARK 500 TYR C 100 -59.80 -22.66 REMARK 500 PRO C 104 -94.85 -92.34 REMARK 500 TYR C 107 115.86 72.69 REMARK 500 ILE D 2 -169.71 -76.11 REMARK 500 SER D 33 -6.85 -59.53 REMARK 500 ASN D 34 -6.86 -150.25 REMARK 500 GLN D 35 33.74 70.76 REMARK 500 ALA D 57 -3.27 50.44 REMARK 500 SER D 58 -11.76 -141.85 REMARK 500 SER D 83 90.94 72.09 REMARK 500 TYR D 100 -134.50 60.81 REMARK 500 CYS A 7 -68.34 -105.76 REMARK 500 SER A 12 112.01 -161.44 REMARK 500 LEU A 13 -88.84 36.10 REMARK 500 ASN F 711 -28.83 -39.84 REMARK 500 PHE F 714 106.09 -161.09 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 ALA D 114 23.6 L L OUTSIDE RANGE 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 E 401 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG E 406 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR LINKED RESIDUES E 402 TO 405 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR LINKED RESIDUES E 407 TO 409 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2DTG RELATED DB: PDB REMARK 900 RELATED ID: 3LOH RELATED DB: PDB REMARK 900 RELATED ID: 2WRW RELATED DB: PDB REMARK 900 RELATED ID: 3W11 RELATED DB: PDB REMARK 900 RELATED ID: 3W13 RELATED DB: PDB REMARK 900 RELATED ID: 3W14 RELATED DB: PDB REMARK 999 REMARK 999 SEQUENCE REMARK 999 HIS E 144 IS NATURAL VARIANT RS1051692. THE SEQUENCE OF CHIAN F IS REMARK 999 ISOFORM SHORT OF INSULIN RECEPTOR, P06213-2. B26 TYR MUTATED TO D- REMARK 999 PRO; B27-B30 ARE DELETED; B26 C-TERMINUS IS FINISHED WITH CONH2 REMARK 999 (CARBOXYAMIDE) NOT A COOH GROUP.