REMARK 2 REMARK 2 RESOLUTION. 2.86 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.5.0066 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) : 2.86 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 93.1 REMARK 3 NUMBER OF REFLECTIONS : 31669 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) : 0.255 REMARK 3 R VALUE (WORKING SET) : 0.253 REMARK 3 FREE R VALUE : 0.301 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1599 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) : 2.86 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.94 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1503 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 64.58 REMARK 3 BIN R VALUE (WORKING SET) : 0.3420 REMARK 3 BIN FREE R VALUE SET COUNT : 83 REMARK 3 BIN FREE R VALUE : 0.4340 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 8324 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 97 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 69.53 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 1.41000 REMARK 3 B22 (A**2) : -2.44000 REMARK 3 B33 (A**2) : 1.03000 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): 0.476 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.904 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.857 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8540 ; 0.007 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11613 ; 1.052 ; 1.948 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1072 ; 4.889 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 343 ;35.654 ;24.373 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1372 ;15.662 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 31 ;13.085 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1285 ; 0.067 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6437 ; 0.002 ; 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): 5405 ; 3.146 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8751 ; 4.920 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3135 ; 3.902 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2862 ; 4.827 ; 4.500 REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): 8540 ; 4.542 ; 3.000 REMARK 3 SPHERICITY; FREE ATOMS (A**2): 97 ; 1.457 ; 3.000 REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 8326 ; 1.559 ; 3.000 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 : NULL 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: NULL REMARK 4 REMARK 4 3NFP COMPLIES WITH FORMAT V. 3.20, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-JUN-10. REMARK 100 THE RCSB ID CODE IS RCSB059771. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-JAN-09 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRF REMARK 200 BEAMLINE : BL17U REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9796 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31671 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800 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 (%) : 95.5 REMARK 200 DATA REDUNDANCY : 4.600 REMARK 200 R MERGE (I) : 0.15800 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 7.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8 REMARK 200 DATA REDUNDANCY IN SHELL : 3.90 REMARK 200 R MERGE FOR SHELL (I) : 0.38400 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.900 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: CNS REMARK 200 STARTING MODEL: PDB ENTRY 3NFS REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 51.57 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS-HCL, 0.2M MGCL2, 10% PEG REMARK 280 8000, PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 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 -X,Y,-Z+1/2 REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 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 123.77750 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 123.77750 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 1.000000 0.000000 0.000000 51.08350 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 57.48650 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 51.08350 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 57.48650 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 123.77750 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 51.08350 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 57.48650 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 123.77750 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 51.08350 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 57.48650 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3080 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 21100 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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: 3080 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 21090 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350 REMARK 350 BIOMOLECULE: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: I 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: 4 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: K 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 SER A 130 REMARK 465 SER A 131 REMARK 465 LYS A 132 REMARK 465 SER H 130 REMARK 465 SER H 131 REMARK 465 ARG I 32 REMARK 465 GLY I 33 REMARK 465 PHE I 34 REMARK 465 ARG I 35 REMARK 465 ALA I 65 REMARK 465 THR I 66 REMARK 465 ARG I 67 REMARK 465 ASN I 68 REMARK 465 THR I 69 REMARK 465 THR I 70 REMARK 465 LYS I 71 REMARK 465 GLN I 72 REMARK 465 VAL I 73 REMARK 465 THR I 74 REMARK 465 PRO I 75 REMARK 465 GLN I 76 REMARK 465 PRO I 77 REMARK 465 GLU I 78 REMARK 465 GLU I 79 REMARK 465 GLN I 80 REMARK 465 LYS I 81 REMARK 465 GLU I 82 REMARK 465 ARG I 83 REMARK 465 LYS I 84 REMARK 465 THR I 85 REMARK 465 THR I 86 REMARK 465 GLU I 87 REMARK 465 MET I 88 REMARK 465 GLN I 89 REMARK 465 SER I 90 REMARK 465 PRO I 91 REMARK 465 MET I 92 REMARK 465 GLN I 93 REMARK 465 PRO I 94 REMARK 465 VAL I 95 REMARK 465 ASP I 96 REMARK 465 GLN I 97 REMARK 465 ALA I 98 REMARK 465 SER I 99 REMARK 465 LEU I 100 REMARK 465 GLY I 165 REMARK 465 GLU I 166 REMARK 465 MET I 167 REMARK 465 GLU I 168 REMARK 465 THR I 169 REMARK 465 SER I 170 REMARK 465 GLN I 171 REMARK 465 PHE I 172 REMARK 465 PRO I 173 REMARK 465 GLY I 174 REMARK 465 GLU I 175 REMARK 465 GLU I 176 REMARK 465 LYS I 177 REMARK 465 PRO I 178 REMARK 465 GLN I 179 REMARK 465 ALA I 180 REMARK 465 SER I 181 REMARK 465 PRO I 182 REMARK 465 GLU I 183 REMARK 465 GLY I 184 REMARK 465 ARG I 185 REMARK 465 PRO I 186 REMARK 465 GLU I 187 REMARK 465 SER I 188 REMARK 465 GLU I 189 REMARK 465 THR I 190 REMARK 465 SER I 191 REMARK 465 CYS I 192 REMARK 465 LEU I 193 REMARK 465 VAL I 194 REMARK 465 THR I 195 REMARK 465 THR I 196 REMARK 465 THR I 197 REMARK 465 ASP I 198 REMARK 465 PHE I 199 REMARK 465 GLN I 200 REMARK 465 ILE I 201 REMARK 465 GLN I 202 REMARK 465 THR I 203 REMARK 465 GLU I 204 REMARK 465 MET I 205 REMARK 465 ALA I 206 REMARK 465 ALA I 207 REMARK 465 THR I 208 REMARK 465 MET I 209 REMARK 465 GLU I 210 REMARK 465 THR I 211 REMARK 465 SER I 212 REMARK 465 ILE I 213 REMARK 465 PHE I 214 REMARK 465 THR I 215 REMARK 465 THR I 216 REMARK 465 GLU I 217 REMARK 465 HIS I 218 REMARK 465 HIS I 219 REMARK 465 HIS I 220 REMARK 465 HIS I 221 REMARK 465 HIS I 222 REMARK 465 HIS I 223 REMARK 465 LYS K 31 REMARK 465 ARG K 32 REMARK 465 GLY K 33 REMARK 465 PHE K 34 REMARK 465 ARG K 35 REMARK 465 ALA K 65 REMARK 465 THR K 66 REMARK 465 ARG K 67 REMARK 465 ASN K 68 REMARK 465 THR K 69 REMARK 465 THR K 70 REMARK 465 LYS K 71 REMARK 465 GLN K 72 REMARK 465 VAL K 73 REMARK 465 THR K 74 REMARK 465 PRO K 75 REMARK 465 GLN K 76 REMARK 465 PRO K 77 REMARK 465 GLU K 78 REMARK 465 GLU K 79 REMARK 465 GLN K 80 REMARK 465 LYS K 81 REMARK 465 GLU K 82 REMARK 465 ARG K 83 REMARK 465 LYS K 84 REMARK 465 THR K 85 REMARK 465 THR K 86 REMARK 465 GLU K 87 REMARK 465 MET K 88 REMARK 465 GLN K 89 REMARK 465 SER K 90 REMARK 465 PRO K 91 REMARK 465 MET K 92 REMARK 465 GLN K 93 REMARK 465 PRO K 94 REMARK 465 VAL K 95 REMARK 465 ASP K 96 REMARK 465 GLN K 97 REMARK 465 ALA K 98 REMARK 465 SER K 99 REMARK 465 LEU K 100 REMARK 465 PRO K 101 REMARK 465 GLN K 130 REMARK 465 CYS K 131 REMARK 465 VAL K 132 REMARK 465 LEU K 138 REMARK 465 HIS K 139 REMARK 465 ARG K 140 REMARK 465 GLY K 141 REMARK 465 PRO K 142 REMARK 465 ILE K 162 REMARK 465 CYS K 163 REMARK 465 THR K 164 REMARK 465 GLY K 165 REMARK 465 GLU K 166 REMARK 465 MET K 167 REMARK 465 GLU K 168 REMARK 465 THR K 169 REMARK 465 SER K 170 REMARK 465 GLN K 171 REMARK 465 PHE K 172 REMARK 465 PRO K 173 REMARK 465 GLY K 174 REMARK 465 GLU K 175 REMARK 465 GLU K 176 REMARK 465 LYS K 177 REMARK 465 PRO K 178 REMARK 465 GLN K 179 REMARK 465 ALA K 180 REMARK 465 SER K 181 REMARK 465 PRO K 182 REMARK 465 GLU K 183 REMARK 465 GLY K 184 REMARK 465 ARG K 185 REMARK 465 PRO K 186 REMARK 465 GLU K 187 REMARK 465 SER K 188 REMARK 465 GLU K 189 REMARK 465 THR K 190 REMARK 465 SER K 191 REMARK 465 CYS K 192 REMARK 465 LEU K 193 REMARK 465 VAL K 194 REMARK 465 THR K 195 REMARK 465 THR K 196 REMARK 465 THR K 197 REMARK 465 ASP K 198 REMARK 465 PHE K 199 REMARK 465 GLN K 200 REMARK 465 ILE K 201 REMARK 465 GLN K 202 REMARK 465 THR K 203 REMARK 465 GLU K 204 REMARK 465 MET K 205 REMARK 465 ALA K 206 REMARK 465 ALA K 207 REMARK 465 THR K 208 REMARK 465 MET K 209 REMARK 465 GLU K 210 REMARK 465 THR K 211 REMARK 465 SER K 212 REMARK 465 ILE K 213 REMARK 465 PHE K 214 REMARK 465 THR K 215 REMARK 465 THR K 216 REMARK 465 GLU K 217 REMARK 465 HIS K 218 REMARK 465 HIS K 219 REMARK 465 HIS K 220 REMARK 465 HIS K 221 REMARK 465 HIS K 222 REMARK 465 HIS K 223 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 LYS A 63 -55.80 -142.80 REMARK 500 PHE A 64 30.10 -99.12 REMARK 500 ASP A 104 -47.06 -141.45 REMARK 500 THR A 134 41.23 -71.74 REMARK 500 THR B 49 65.58 36.93 REMARK 500 THR B 50 -33.85 64.18 REMARK 500 SER B 51 -11.62 -143.48 REMARK 500 ALA B 83 -161.83 -176.07 REMARK 500 ARG B 90 43.12 -153.67 REMARK 500 ARG B 107 -169.78 -117.49 REMARK 500 ASN B 137 76.49 39.70 REMARK 500 PRO B 140 -177.50 -69.72 REMARK 500 GLU B 142 99.13 -61.15 REMARK 500 ASN B 157 -1.64 -142.57 REMARK 500 SER B 167 14.57 -68.92 REMARK 500 LYS B 168 -30.33 -133.85 REMARK 500 LYS B 189 -63.12 -105.35 REMARK 500 SER H 16 -159.37 -92.48 REMARK 500 PRO H 41 120.79 -32.56 REMARK 500 ILE H 48 -60.65 -93.58 REMARK 500 GLU H 89 -6.57 -55.95 REMARK 500 SER H 133 165.02 -48.48 REMARK 500 THR H 134 -23.23 103.76 REMARK 500 ASP H 147 83.59 54.40 REMARK 500 PRO H 205 -9.42 -53.34 REMARK 500 LEU L 46 -73.59 -102.54 REMARK 500 THR L 50 -41.43 81.29 REMARK 500 ALA L 83 -162.35 -177.49 REMARK 500 LYS L 125 42.35 -84.68 REMARK 500 ASN L 137 75.92 52.54 REMARK 500 ASN L 157 25.23 -150.61 REMARK 500 PRO I 11 117.79 -39.90 REMARK 500 ILE I 37 -127.70 -133.35 REMARK 500 LYS I 38 145.05 133.88 REMARK 500 SER I 41 -162.82 60.25 REMARK 500 LEU I 42 -35.19 -133.44 REMARK 500 ASN I 49 -112.98 -76.75 REMARK 500 ASP I 56 -77.01 -70.64 REMARK 500 THR I 62 -132.96 -125.25 REMARK 500 GLU I 116 146.13 -179.00 REMARK 500 VAL I 122 -158.50 -88.07 REMARK 500 VAL I 123 -82.57 -73.26 REMARK 500 GLN I 133 -153.72 58.10 REMARK 500 THR I 150 -92.16 -122.94 REMARK 500 HIS I 151 49.65 -86.36 REMARK 500 GLN I 160 78.79 84.39 REMARK 500 LEU K 2 110.89 -171.23 REMARK 500 PRO K 8 -176.42 -66.53 REMARK 500 PRO K 11 106.84 -54.13 REMARK 500 HIS K 12 96.87 72.86 REMARK 500 REMARK 500 THIS ENTRY HAS 60 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A 226 DISTANCE = 7.12 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3IU3 RELATED DB: PDB REMARK 900 RELATED ID: 3NFS RELATED DB: PDB