REMARK 2 REMARK 2 RESOLUTION. 2.95 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.4.0069 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) : 2.95 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8 REMARK 3 NUMBER OF REFLECTIONS : 17200 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) : 0.225 REMARK 3 R VALUE (WORKING SET) : 0.222 REMARK 3 FREE R VALUE : 0.287 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 927 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) : 2.95 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.03 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1246 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.95 REMARK 3 BIN R VALUE (WORKING SET) : 0.2950 REMARK 3 BIN FREE R VALUE SET COUNT : 72 REMARK 3 BIN FREE R VALUE : 0.4800 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4995 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 99 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) : 77.24 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -1.23000 REMARK 3 B22 (A**2) : -1.23000 REMARK 3 B33 (A**2) : 2.46000 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): 0.473 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.358 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 42.292 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.928 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.875 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5217 ; 0.006 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 3452 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7109 ; 1.061 ; 1.968 REMARK 3 BOND ANGLES OTHERS (DEGREES): 8421 ; 1.303 ; 3.003 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 644 ; 6.138 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 211 ;34.308 ;24.408 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 844 ;15.482 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;16.668 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 829 ; 0.066 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5696 ; 0.003 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): 994 ; 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): 145 ; 0.131 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): 1 ; 0.025 ; 0.200 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): 38 ; 0.132 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): 105 ; 0.150 ; 0.200 REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 11 ; 0.120 ; 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): 3219 ; 0.606 ; 3.000 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1310 ; 0.071 ; 3.000 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5231 ; 1.217 ; 5.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1998 ; 1.982 ; 7.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1878 ; 3.516 ;11.000 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 : 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 : A 8 A 121 REMARK 3 RESIDUE RANGE : A 301 A 506 REMARK 3 ORIGIN FOR THE GROUP (A): -12.5149 -56.1071 -16.8211 REMARK 3 T TENSOR REMARK 3 T11: -0.3665 T22: -0.1701 REMARK 3 T33: -0.1724 T12: 0.0280 REMARK 3 T13: 0.1070 T23: 0.1443 REMARK 3 L TENSOR REMARK 3 L11: 1.5050 L22: 2.4240 REMARK 3 L33: 10.2021 L12: 0.5942 REMARK 3 L13: 0.9868 L23: 1.1792 REMARK 3 S TENSOR REMARK 3 S11: -0.0529 S12: 0.0418 S13: 0.1473 REMARK 3 S21: 0.0031 S22: -0.0079 S23: 0.1462 REMARK 3 S31: -0.1466 S32: -0.2387 S33: 0.0608 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 122 A 236 REMARK 3 ORIGIN FOR THE GROUP (A): -5.6331 -33.7413 0.5488 REMARK 3 T TENSOR REMARK 3 T11: -0.0436 T22: -0.2858 REMARK 3 T33: -0.0688 T12: 0.1246 REMARK 3 T13: 0.3070 T23: 0.1071 REMARK 3 L TENSOR REMARK 3 L11: 2.6507 L22: 3.3178 REMARK 3 L33: 9.8766 L12: 0.5765 REMARK 3 L13: -0.0901 L23: 1.6832 REMARK 3 S TENSOR REMARK 3 S11: 0.0128 S12: -0.1190 S13: 0.6009 REMARK 3 S21: 0.5917 S22: 0.2106 S23: 0.2432 REMARK 3 S31: -0.6346 S32: -0.5688 S33: -0.2234 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 2 L 108 REMARK 3 ORIGIN FOR THE GROUP (A): 17.2230 -32.6237 -15.4424 REMARK 3 T TENSOR REMARK 3 T11: -0.1259 T22: -0.4429 REMARK 3 T33: -0.2979 T12: -0.0557 REMARK 3 T13: 0.0436 T23: 0.1665 REMARK 3 L TENSOR REMARK 3 L11: 9.8096 L22: 5.7129 REMARK 3 L33: 4.1553 L12: -0.6537 REMARK 3 L13: -0.5405 L23: 1.6498 REMARK 3 S TENSOR REMARK 3 S11: 0.3146 S12: 0.0910 S13: 0.2245 REMARK 3 S21: 0.9550 S22: -0.1948 S23: -0.4588 REMARK 3 S31: -0.2309 S32: 0.2154 S33: -0.1198 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 109 L 212 REMARK 3 ORIGIN FOR THE GROUP (A): 37.3773 -44.5855 -46.8504 REMARK 3 T TENSOR REMARK 3 T11: -0.0998 T22: 0.0049 REMARK 3 T33: 0.2463 T12: -0.2063 REMARK 3 T13: -0.0456 T23: -0.2318 REMARK 3 L TENSOR REMARK 3 L11: 4.1748 L22: 3.1922 REMARK 3 L33: 10.7383 L12: -1.1067 REMARK 3 L13: 0.9896 L23: 0.2780 REMARK 3 S TENSOR REMARK 3 S11: -0.2815 S12: 0.3348 S13: 0.0557 REMARK 3 S21: 0.0747 S22: 0.2846 S23: -0.7796 REMARK 3 S31: 0.0447 S32: 0.4010 S33: -0.0031 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 : H 1 H 113 REMARK 3 ORIGIN FOR THE GROUP (A): 3.8831 -28.0776 -32.5630 REMARK 3 T TENSOR REMARK 3 T11: -0.3827 T22: -0.0704 REMARK 3 T33: -0.1319 T12: 0.0968 REMARK 3 T13: 0.0882 T23: 0.1896 REMARK 3 L TENSOR REMARK 3 L11: 5.2108 L22: 2.7162 REMARK 3 L33: 9.9330 L12: 0.4218 REMARK 3 L13: -2.2213 L23: -2.1499 REMARK 3 S TENSOR REMARK 3 S11: -0.1844 S12: 0.9078 S13: 0.3616 REMARK 3 S21: 0.0830 S22: 0.4035 S23: 0.4913 REMARK 3 S31: -0.2921 S32: -0.4859 S33: -0.2191 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 : H 114 H 228 REMARK 3 ORIGIN FOR THE GROUP (A): 21.3906 -47.0282 -48.0561 REMARK 3 T TENSOR REMARK 3 T11: -0.1260 T22: 0.3302 REMARK 3 T33: -0.2074 T12: -0.2723 REMARK 3 T13: -0.0708 T23: -0.0431 REMARK 3 L TENSOR REMARK 3 L11: 4.1028 L22: 10.0859 REMARK 3 L33: 4.0864 L12: -1.8901 REMARK 3 L13: 0.5612 L23: -0.2781 REMARK 3 S TENSOR REMARK 3 S11: 0.0692 S12: 0.1445 S13: -0.5480 REMARK 3 S21: -0.1619 S22: 0.2135 S23: -0.2191 REMARK 3 S31: 0.3971 S32: -0.2934 S33: -0.2827 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 3MJ9 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-APR-10. REMARK 100 THE RCSB ID CODE IS RCSB058613. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 22-OCT-06 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 6.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-D REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793 REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL CRYO-COOLED REMARK 200 SI(111) REMARK 200 OPTICS : SI(111) DOUBLE CRYSTAL REMARK 200 MONOCHROMATOR. ADJUSTABLE REMARK 200 FOCUSING MIRRORS IN K-B GEOMETRY REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18365 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.950 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7 REMARK 200 DATA REDUNDANCY : 3.100 REMARK 200 R MERGE (I) : 0.12200 REMARK 200 R SYM (I) : 0.12200 REMARK 200 FOR THE DATA SET : 6.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.95 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.06 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.61700 REMARK 200 R SYM FOR SHELL (I) : 0.61700 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: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 55.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2-1.4 M NA-MALONATE, PH 6.0, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 295K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4 REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4 REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4 REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4 REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-Z+1/2 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 53.91950 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 62.51000 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 62.51000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 80.87925 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 62.51000 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 62.51000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 26.95975 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 62.51000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 62.51000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 80.87925 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 62.51000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 62.51000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 26.95975 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 53.91950 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 7600 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 30250 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 ARG A -1 REMARK 465 SER A 0 REMARK 465 GLN A 1 REMARK 465 GLY A 2 REMARK 465 LEU A 3 REMARK 465 PRO A 4 REMARK 465 GLY A 5 REMARK 465 LEU A 6 REMARK 465 THR A 7 REMARK 465 GLU A 237 REMARK 465 PHE A 238 REMARK 465 GLN A 239 REMARK 465 ARG A 240 REMARK 465 THR A 241 REMARK 465 ILE A 242 REMARK 465 SER A 243 REMARK 465 PRO A 244 REMARK 465 THR A 245 REMARK 465 PRO A 246 REMARK 465 PRO A 247 REMARK 465 THR A 248 REMARK 465 ASP A 249 REMARK 465 LYS A 250 REMARK 465 GLY A 251 REMARK 465 GLN A 252 REMARK 465 GLN A 253 REMARK 465 GLY A 254 REMARK 465 ILE A 255 REMARK 465 LEU A 256 REMARK 465 ASN A 257 REMARK 465 GLY A 258 REMARK 465 ASN A 259 REMARK 465 GLN A 260 REMARK 465 HIS A 261 REMARK 465 HIS A 262 REMARK 465 HIS A 263 REMARK 465 HIS A 264 REMARK 465 HIS A 265 REMARK 465 HIS A 266 REMARK 465 SER L 1 REMARK 465 ALA L 213 REMARK 465 CYS L 214 REMARK 465 SER L 215 REMARK 465 CYS H 128 REMARK 465 ASP H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 THR H 132 REMARK 465 SER H 133 REMARK 465 THR H 134 REMARK 465 THR H 135 REMARK 465 ASP H 229 REMARK 465 GLY H 230 REMARK 465 SER H 231 REMARK 465 GLY H 232 REMARK 465 CYS H 233 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 9 110.83 -160.95 REMARK 500 CYS A 25 84.56 -160.24 REMARK 500 GLN A 28 116.42 -39.49 REMARK 500 ASP A 45 -156.39 -133.31 REMARK 500 GLU A 106 -9.01 83.08 REMARK 500 ARG A 124 -4.62 78.26 REMARK 500 LYS A 150 140.18 -170.90 REMARK 500 SER A 156 103.07 -160.72 REMARK 500 ASN A 186 -14.95 75.42 REMARK 500 VAL L 13 130.57 -176.76 REMARK 500 ASP L 51 -55.21 66.29 REMARK 500 SER L 90 -154.18 -164.89 REMARK 500 THR L 94 -76.64 -97.83 REMARK 500 ALA L 142 47.36 -84.63 REMARK 500 ALA L 150 102.07 -160.32 REMARK 500 THR L 156 -60.64 -106.92 REMARK 500 ASN L 190 -78.18 -49.71 REMARK 500 ASP H 31 13.69 -140.64 REMARK 500 SER H 65 14.11 93.95 REMARK 500 GLN H 83 -161.05 -113.03 REMARK 500 TYR H 97 -90.72 43.55 REMARK 500 ALA H 214 -71.96 -48.82 REMARK 500 SER H 216 30.26 71.21 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 L 166 SER L 168 145.65 REMARK 500 GLU H 85 ASP H 86 148.66 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 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 401 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 501 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 502 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 503 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 504 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 505 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC A 506 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3MJ6 RELATED DB: PDB REMARK 900 RELATED ID: 3MJ7 RELATED DB: PDB