REMARK 2 REMARK 2 RESOLUTION. 3.52 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.2_869) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE- REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO, REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH, REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER REMARK 3 : ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.52 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.54 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 83.3 REMARK 3 NUMBER OF REFLECTIONS : 13608 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.375 REMARK 3 R VALUE (WORKING SET) : 0.373 REMARK 3 FREE R VALUE : 0.408 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.910 REMARK 3 FREE R VALUE TEST SET COUNT : 668 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 41.5426 - 6.0126 0.99 3230 160 0.3499 0.4081 REMARK 3 2 6.0126 - 4.7746 1.00 3111 163 0.3815 0.4093 REMARK 3 3 4.7746 - 4.1717 0.98 2977 170 0.3660 0.3912 REMARK 3 4 4.1717 - 3.7906 0.80 2423 131 0.4281 0.4247 REMARK 3 5 3.7906 - 3.5190 0.39 1199 44 0.4385 0.4479 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 REMARK 3 SHRINKAGE RADIUS : 0.86 REMARK 3 K_SOL : 0.30 REMARK 3 B_SOL : 130.54 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 1.430 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 44.130 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 113.52 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 126.43 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -6.95660 REMARK 3 B22 (A**2) : -0.06600 REMARK 3 B33 (A**2) : 2.12870 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 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.008 5645 REMARK 3 ANGLE : 1.377 7783 REMARK 3 CHIRALITY : 0.090 913 REMARK 3 PLANARITY : 0.006 1043 REMARK 3 DIHEDRAL : 15.303 1599 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : 2 REMARK 3 NCS GROUP : 1 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: chain 'D' and (resseq 1:113 or resseq REMARK 3 137:141 or resseq 143:244 ) REMARK 3 SELECTION : chain 'C' and (resseq 1:113 or resseq REMARK 3 137:141 or resseq 143:244 ) REMARK 3 ATOM PAIRS NUMBER : 1437 REMARK 3 RMSD : 0.050 REMARK 3 NCS GROUP : 2 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: chain 'A' and (resseq 1:181 or resseq REMARK 3 188:198 or resseq 200:213 ) REMARK 3 SELECTION : chain 'B' and (resseq 1:181 or resseq REMARK 3 188:198 or resseq 200:213 ) REMARK 3 ATOM PAIRS NUMBER : 1134 REMARK 3 RMSD : 0.054 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 4F9P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-MAY-12. REMARK 100 THE RCSB ID CODE IS RCSB072631. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 20-NOV-11 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.5 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) : 1.033 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL 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 : 16002 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.450 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.45 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.51 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6 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: PDB ENTRY 48F0, 3DIF, 1XGP REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 60.98 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.15 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES PH7.5, 1M SODIUM CHLORIDE, REMARK 280 15% PEG 8000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K 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 44.18000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 60.99500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 58.84000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 60.99500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 44.18000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 58.84000 REMARK 290 SMTRY3 4 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 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: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: D 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: C 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: C 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 ALA A -2 REMARK 465 ASP A -1 REMARK 465 LEU A 0 REMARK 465 ARG A 182 REMARK 465 GLY A 183 REMARK 465 SER A 184 REMARK 465 SER A 185 REMARK 465 GLY A 186 REMARK 465 GLU A 187 REMARK 465 ARG A 214 REMARK 465 SER A 215 REMARK 465 ALA A 216 REMARK 465 GLN A 217 REMARK 465 ALA B -2 REMARK 465 ASP B -1 REMARK 465 LEU B 0 REMARK 465 GLY B 183 REMARK 465 SER B 184 REMARK 465 SER B 185 REMARK 465 GLY B 186 REMARK 465 GLU B 187 REMARK 465 ARG B 214 REMARK 465 SER B 215 REMARK 465 ALA B 216 REMARK 465 GLN B 217 REMARK 465 ALA D 116 REMARK 465 GLY D 117 REMARK 465 GLY D 118 REMARK 465 GLY D 119 REMARK 465 GLY D 120 REMARK 465 SER D 121 REMARK 465 GLY D 122 REMARK 465 GLY D 123 REMARK 465 GLY D 124 REMARK 465 GLY D 125 REMARK 465 SER D 126 REMARK 465 GLY D 127 REMARK 465 GLY D 128 REMARK 465 GLY D 129 REMARK 465 GLY D 130 REMARK 465 SER D 131 REMARK 465 GLY D 132 REMARK 465 GLY D 133 REMARK 465 GLY D 134 REMARK 465 ARG D 244 REMARK 465 ALA D 245 REMARK 465 ASP D 246 REMARK 465 ALA D 247 REMARK 465 ALA D 248 REMARK 465 ALA D 249 REMARK 465 ALA D 250 REMARK 465 SER D 251 REMARK 465 GLY D 252 REMARK 465 ALA D 253 REMARK 465 ASP D 254 REMARK 465 SER C 114 REMARK 465 ALA C 115 REMARK 465 ALA C 116 REMARK 465 GLY C 117 REMARK 465 GLY C 118 REMARK 465 GLY C 119 REMARK 465 GLY C 120 REMARK 465 SER C 121 REMARK 465 GLY C 122 REMARK 465 GLY C 123 REMARK 465 GLY C 124 REMARK 465 GLY C 125 REMARK 465 SER C 126 REMARK 465 GLY C 127 REMARK 465 GLY C 128 REMARK 465 GLY C 129 REMARK 465 GLY C 130 REMARK 465 SER C 131 REMARK 465 GLY C 132 REMARK 465 GLY C 133 REMARK 465 GLY C 134 REMARK 465 GLY C 135 REMARK 465 SER C 136 REMARK 465 ARG C 244 REMARK 465 ALA C 245 REMARK 465 ASP C 246 REMARK 465 ALA C 247 REMARK 465 ALA C 248 REMARK 465 ALA C 249 REMARK 465 ALA C 250 REMARK 465 SER C 251 REMARK 465 GLY C 252 REMARK 465 ALA C 253 REMARK 465 ASP C 254 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 GLN A 1 CG CD OE1 NE2 REMARK 470 SER A 3 OG REMARK 470 ILE A 11 CG1 CG2 CD1 REMARK 470 LEU A 12 CG CD1 CD2 REMARK 470 MET A 14 CG SD CE REMARK 470 VAL A 15 CG1 CG2 REMARK 470 GLU A 17 CG CD OE1 OE2 REMARK 470 LEU A 21 CG CD1 CD2 REMARK 470 HIS A 24 CG ND1 CD2 CE1 NE2 REMARK 470 PHE A 26 CG CD1 CD2 CE1 CE2 CZ REMARK 470 THR A 28 OG1 CG2 REMARK 470 MET A 29 CG SD CE REMARK 470 SER A 30 OG REMARK 470 GLU A 32 CG CD OE1 OE2 REMARK 470 MET A 34 CG SD CE REMARK 470 GLU A 35 CG CD OE1 OE2 REMARK 470 LEU A 36 CG CD1 CD2 REMARK 470 LYS A 37 CG CD CE NZ REMARK 470 SER A 42 OG REMARK 470 LEU A 43 CG CD1 CD2 REMARK 470 GLN A 45 CG CD OE1 NE2 REMARK 470 VAL A 46 CG1 CG2 REMARK 470 LYS A 54 CG CD CE NZ REMARK 470 GLU A 55 CG CD OE1 OE2 REMARK 470 VAL A 56 CG1 CG2 REMARK 470 GLU A 57 CG CD OE1 OE2 REMARK 470 ARG A 59 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 65 CG CD NE CZ NH1 NH2 REMARK 470 SER A 69 OG REMARK 470 LEU A 71 CG CD1 CD2 REMARK 470 ARG A 72 CG CD NE CZ NH1 NH2 REMARK 470 THR A 76 OG1 CG2 REMARK 470 LYS A 79 CG CD CE NZ REMARK 470 ARG A 83 CG CD NE CZ NH1 NH2 REMARK 470 ILE A 84 CG1 CG2 CD1 REMARK 470 THR A 88 OG1 CG2 REMARK 470 SER A 92 OG REMARK 470 LYS A 94 CG CD CE NZ REMARK 470 LEU A 96 CG CD1 CD2 REMARK 470 ASP A 101 CG OD1 OD2 REMARK 470 ASP A 103 CG OD1 OD2 REMARK 470 GLU A 106 CG CD OE1 OE2 REMARK 470 LYS A 107 CG CD CE NZ REMARK 470 LEU A 109 CG CD1 CD2 REMARK 470 GLU A 111 CG CD OE1 OE2 REMARK 470 LEU A 112 CG CD1 CD2 REMARK 470 LYS A 113 CG CD CE NZ REMARK 470 VAL A 114 CG1 CG2 REMARK 470 SER A 119 OG REMARK 470 ASP A 120 CG OD1 OD2 REMARK 470 VAL A 123 CG1 CG2 REMARK 470 ASP A 124 CG OD1 OD2 REMARK 470 VAL A 125 CG1 CG2 REMARK 470 LYS A 126 CG CD CE NZ REMARK 470 LYS A 129 CG CD CE NZ REMARK 470 ASP A 130 CG OD1 OD2 REMARK 470 ILE A 133 CG1 CG2 CD1 REMARK 470 HIS A 134 CG ND1 CD2 CE1 NE2 REMARK 470 LEU A 135 CG CD1 CD2 REMARK 470 GLU A 136 CG CD OE1 OE2 REMARK 470 ARG A 138 CG CD NE CZ NH1 NH2 REMARK 470 SER A 139 OG REMARK 470 GLN A 145 CG CD OE1 NE2 REMARK 470 PRO A 146 CG CD REMARK 470 ILE A 148 CG1 CG2 CD1 REMARK 470 GLN A 149 CG CD OE1 NE2 REMARK 470 SER A 151 OG REMARK 470 ASN A 153 CG OD1 ND2 REMARK 470 LYS A 154 CG CD CE NZ REMARK 470 GLU A 156 CG CD OE1 OE2 REMARK 470 ILE A 158 CG1 CG2 CD1 REMARK 470 THR A 160 OG1 CG2 REMARK 470 VAL A 161 CG1 CG2 REMARK 470 GLU A 162 CG CD OE1 OE2 REMARK 470 VAL A 165 CG1 CG2 REMARK 470 VAL A 166 CG1 CG2 REMARK 470 ASP A 168 CG OD1 OD2 REMARK 470 VAL A 170 CG1 CG2 REMARK 470 LEU A 172 CG CD1 CD2 REMARK 470 VAL A 175 CG1 CG2 REMARK 470 SER A 178 OG REMARK 470 VAL A 179 CG1 CG2 REMARK 470 ILE A 180 CG1 CG2 CD1 REMARK 470 MET A 181 CG SD CE REMARK 470 VAL A 189 CG1 CG2 REMARK 470 SER A 190 OG REMARK 470 ILE A 193 CG1 CG2 CD1 REMARK 470 ARG A 194 CG CD NE CZ NH1 NH2 REMARK 470 SER A 195 OG REMARK 470 LEU A 198 CG CD1 CD2 REMARK 470 LEU A 200 CG CD1 CD2 REMARK 470 GLU A 201 CG CD OE1 OE2 REMARK 470 LYS A 202 CG CD CE NZ REMARK 470 THR A 203 OG1 CG2 REMARK 470 ILE A 206 CG1 CG2 CD1 REMARK 470 SER A 207 OG REMARK 470 ILE A 208 CG1 CG2 CD1 REMARK 470 ASP A 210 CG OD1 OD2 REMARK 470 PRO A 211 CG CD REMARK 470 PHE A 213 CG CD1 CD2 CE1 CE2 CZ REMARK 470 PHE B 2 CG CD1 CD2 CE1 CE2 CZ REMARK 470 SER B 3 OG REMARK 470 LEU B 5 CG CD1 CD2 REMARK 470 SER B 8 OG REMARK 470 LEU B 12 CG CD1 CD2 REMARK 470 VAL B 15 CG1 CG2 REMARK 470 GLU B 17 CG CD OE1 OE2 REMARK 470 LEU B 25 CG CD1 CD2 REMARK 470 PHE B 26 CG CD1 CD2 CE1 CE2 CZ REMARK 470 MET B 29 CG SD CE REMARK 470 SER B 30 OG REMARK 470 GLU B 35 CG CD OE1 OE2 REMARK 470 LEU B 36 CG CD1 CD2 REMARK 470 LYS B 37 CG CD CE NZ REMARK 470 VAL B 39 CG1 CG2 REMARK 470 SER B 41 OG REMARK 470 SER B 42 OG REMARK 470 LEU B 43 CG CD1 CD2 REMARK 470 GLN B 45 CG CD OE1 NE2 REMARK 470 VAL B 46 CG1 CG2 REMARK 470 VAL B 47 CG1 CG2 REMARK 470 ASN B 48 CG OD1 ND2 REMARK 470 VAL B 49 CG1 CG2 REMARK 470 TYR B 50 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ASP B 52 CG OD1 OD2 REMARK 470 LYS B 54 CG CD CE NZ REMARK 470 GLU B 55 CG CD OE1 OE2 REMARK 470 VAL B 56 CG1 CG2 REMARK 470 GLU B 57 CG CD OE1 OE2 REMARK 470 GLN B 60 CG CD OE1 NE2 REMARK 470 TYR B 64 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ARG B 65 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 67 CG CD NE CZ NH1 NH2 REMARK 470 THR B 68 OG1 CG2 REMARK 470 SER B 69 OG REMARK 470 LEU B 71 CG CD1 CD2 REMARK 470 ARG B 72 CG CD NE CZ NH1 NH2 REMARK 470 ILE B 75 CG1 CG2 CD1 REMARK 470 LYS B 79 CG CD CE NZ REMARK 470 LEU B 82 CG CD1 CD2 REMARK 470 ARG B 83 CG CD NE CZ NH1 NH2 REMARK 470 ILE B 84 CG1 CG2 CD1 REMARK 470 VAL B 87 CG1 CG2 REMARK 470 LYS B 94 CG CD CE NZ REMARK 470 LEU B 96 CG CD1 CD2 REMARK 470 ASP B 103 CG OD1 OD2 REMARK 470 PHE B 104 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLU B 106 CG CD OE1 OE2 REMARK 470 LYS B 107 CG CD CE NZ REMARK 470 LEU B 109 CG CD1 CD2 REMARK 470 GLU B 111 CG CD OE1 OE2 REMARK 470 LYS B 113 CG CD CE NZ REMARK 470 SER B 119 OG REMARK 470 LEU B 121 CG CD1 CD2 REMARK 470 HIS B 122 CG ND1 CD2 CE1 NE2 REMARK 470 VAL B 125 CG1 CG2 REMARK 470 LYS B 126 CG CD CE NZ REMARK 470 LYS B 129 CG CD CE NZ REMARK 470 ASP B 130 CG OD1 OD2 REMARK 470 ILE B 133 CG1 CG2 CD1 REMARK 470 HIS B 134 CG ND1 CD2 CE1 NE2 REMARK 470 LEU B 135 CG CD1 CD2 REMARK 470 ARG B 138 CG CD NE CZ NH1 NH2 REMARK 470 SER B 139 OG REMARK 470 GLN B 147 CG CD OE1 NE2 REMARK 470 GLN B 149 CG CD OE1 NE2 REMARK 470 SER B 151 OG REMARK 470 ASN B 152 CG OD1 ND2 REMARK 470 ASN B 153 CG OD1 ND2 REMARK 470 LYS B 154 CG CD CE NZ REMARK 470 GLU B 156 CG CD OE1 OE2 REMARK 470 ASN B 157 CG OD1 ND2 REMARK 470 GLU B 162 CG CD OE1 OE2 REMARK 470 VAL B 165 CG1 CG2 REMARK 470 VAL B 166 CG1 CG2 REMARK 470 ASP B 168 CG OD1 OD2 REMARK 470 VAL B 170 CG1 CG2 REMARK 470 VAL B 175 CG1 CG2 REMARK 470 SER B 178 OG REMARK 470 VAL B 179 CG1 CG2 REMARK 470 ILE B 180 CG1 CG2 CD1 REMARK 470 MET B 181 CG SD CE REMARK 470 ARG B 182 CG CD NE CZ NH1 NH2 REMARK 470 VAL B 189 CG1 CG2 REMARK 470 THR B 192 OG1 CG2 REMARK 470 ARG B 194 CG CD NE CZ NH1 NH2 REMARK 470 SER B 196 OG REMARK 470 LEU B 197 CG CD1 CD2 REMARK 470 LEU B 198 CG CD1 CD2 REMARK 470 LEU B 200 CG CD1 CD2 REMARK 470 LYS B 202 CG CD CE NZ REMARK 470 THR B 203 OG1 CG2 REMARK 470 SER B 205 OG REMARK 470 ILE B 206 CG1 CG2 CD1 REMARK 470 ILE B 208 CG1 CG2 CD1 REMARK 470 ASP B 210 CG OD1 OD2 REMARK 470 PRO B 211 CG CD REMARK 470 PHE B 212 CG CD1 CD2 CE1 CE2 CZ REMARK 470 PHE B 213 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLN D 1 CG CD OE1 NE2 REMARK 470 GLN D 3 CG CD OE1 NE2 REMARK 470 GLN D 5 CG CD OE1 NE2 REMARK 470 GLU D 10 CG CD OE1 OE2 REMARK 470 VAL D 12 CG1 CG2 REMARK 470 ARG D 13 CG CD NE CZ NH1 NH2 REMARK 470 LYS D 19 CG CD CE NZ REMARK 470 LYS D 23 CG CD CE NZ REMARK 470 TYR D 27 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS D 38 CG CD CE NZ REMARK 470 ARG D 40 CG CD NE CZ NH1 NH2 REMARK 470 GLN D 43 CG CD OE1 NE2 REMARK 470 ILE D 51 CG1 CG2 CD1 REMARK 470 ASN D 52 CG OD1 ND2 REMARK 470 ARG D 54 CG CD NE CZ NH1 NH2 REMARK 470 SER D 58 OG REMARK 470 GLU D 62 CG CD OE1 OE2 REMARK 470 LYS D 63 CG CD CE NZ REMARK 470 LYS D 65 CG CD CE NZ REMARK 470 ARG D 67 CG CD NE CZ NH1 NH2 REMARK 470 THR D 68 OG1 CG2 REMARK 470 SER D 75 OG REMARK 470 SER D 76 OG REMARK 470 MET D 81 CG SD CE REMARK 470 GLN D 82 CG CD OE1 NE2 REMARK 470 LEU D 83 CG CD1 CD2 REMARK 470 ARG D 98 CG CD NE CZ NH1 NH2 REMARK 470 SER D 99 OG REMARK 470 ASP D 100 CG OD1 OD2 REMARK 470 LEU D 140 CG CD1 CD2 REMARK 470 SER D 148 OG REMARK 470 SER D 154 OG REMARK 470 SER D 158 OG REMARK 470 ARG D 160 CG CD NE CZ NH1 NH2 REMARK 470 GLN D 163 CG CD OE1 NE2 REMARK 470 ARG D 173 CG CD NE CZ NH1 NH2 REMARK 470 LYS D 175 CG CD CE NZ REMARK 470 GLU D 178 CG CD OE1 OE2 REMARK 470 ARG D 181 CG CD NE CZ NH1 NH2 REMARK 470 LYS D 185 CG CD CE NZ REMARK 470 SER D 188 OG REMARK 470 GLN D 189 CG CD OE1 NE2 REMARK 470 SER D 201 OG REMARK 470 THR D 216 OG1 CG2 REMARK 470 GLU D 217 CG CD OE1 OE2 REMARK 470 GLN D 226 CG CD OE1 NE2 REMARK 470 SER D 227 OG REMARK 470 LYS D 239 CG CD CE NZ REMARK 470 GLU D 241 CG CD OE1 OE2 REMARK 470 LYS D 243 CG CD CE NZ REMARK 470 GLN C 1 CG CD OE1 NE2 REMARK 470 LEU C 4 CG CD1 CD2 REMARK 470 SER C 7 OG REMARK 470 VAL C 12 CG1 CG2 REMARK 470 ARG C 13 CG CD NE CZ NH1 NH2 REMARK 470 LYS C 19 CG CD CE NZ REMARK 470 LYS C 23 CG CD CE NZ REMARK 470 SER C 25 OG REMARK 470 PHE C 29 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS C 38 CG CD CE NZ REMARK 470 GLN C 39 CG CD OE1 NE2 REMARK 470 ARG C 40 CG CD NE CZ NH1 NH2 REMARK 470 GLN C 43 CG CD OE1 NE2 REMARK 470 ILE C 48 CG1 CG2 CD1 REMARK 470 ASN C 52 CG OD1 ND2 REMARK 470 ARG C 54 CG CD NE CZ NH1 NH2 REMARK 470 GLU C 62 CG CD OE1 OE2 REMARK 470 LYS C 63 CG CD CE NZ REMARK 470 LYS C 65 CG CD CE NZ REMARK 470 ARG C 67 CG CD NE CZ NH1 NH2 REMARK 470 THR C 68 OG1 CG2 REMARK 470 THR C 69 OG1 CG2 REMARK 470 ASP C 73 CG OD1 OD2 REMARK 470 GLN C 74 CG CD OE1 NE2 REMARK 470 GLN C 82 CG CD OE1 NE2 REMARK 470 SER C 84 OG REMARK 470 LEU C 86 CG CD1 CD2 REMARK 470 SER C 88 OG REMARK 470 SER C 91 OG REMARK 470 ARG C 98 CG CD NE CZ NH1 NH2 REMARK 470 ASP C 100 CG OD1 OD2 REMARK 470 TYR C 101 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 VAL C 145 CG1 CG2 REMARK 470 THR C 146 OG1 CG2 REMARK 470 LEU C 147 CG CD1 CD2 REMARK 470 SER C 148 OG REMARK 470 VAL C 149 CG1 CG2 REMARK 470 LEU C 157 CG CD1 CD2 REMARK 470 SER C 158 OG REMARK 470 ARG C 160 CG CD NE CZ NH1 NH2 REMARK 470 GLN C 163 CG CD OE1 NE2 REMARK 470 SER C 164 OG REMARK 470 ARG C 173 CG CD NE CZ NH1 NH2 REMARK 470 LYS C 175 CG CD CE NZ REMARK 470 SER C 176 OG REMARK 470 GLU C 178 CG CD OE1 OE2 REMARK 470 ARG C 181 CG CD NE CZ NH1 NH2 REMARK 470 LEU C 182 CG CD1 CD2 REMARK 470 LEU C 183 CG CD1 CD2 REMARK 470 LYS C 185 CG CD CE NZ REMARK 470 GLN C 189 CG CD OE1 NE2 REMARK 470 ILE C 191 CG1 CG2 CD1 REMARK 470 ILE C 194 CG1 CG2 CD1 REMARK 470 SER C 201 OG REMARK 470 GLU C 206 CG CD OE1 OE2 REMARK 470 LEU C 209 CG CD1 CD2 REMARK 470 SER C 210 OG REMARK 470 ILE C 211 CG1 CG2 CD1 REMARK 470 SER C 213 OG REMARK 470 ILE C 221 CG1 CG2 CD1 REMARK 470 THR C 238 OG1 CG2 REMARK 470 LYS C 239 CG CD CE NZ REMARK 470 GLU C 241 CG CD OE1 OE2 REMARK 470 LEU C 242 CG CD1 CD2 REMARK 470 LYS C 243 CG CD CE NZ 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 PRO B 146 C - N - CD ANGL. DEV. = -18.4 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 SER A 42 -62.49 -100.34 REMARK 500 SER B 42 -63.23 -96.64 REMARK 500 ILE B 75 -56.55 68.81 REMARK 500 LEU B 197 -72.75 -71.62 REMARK 500 ILE D 48 -160.11 -101.47 REMARK 500 ARG D 54 -5.27 83.86 REMARK 500 ASP D 100 -11.43 73.48 REMARK 500 ILE D 138 136.55 -35.46 REMARK 500 SER D 162 -71.56 -69.31 REMARK 500 SER D 166 -126.54 60.67 REMARK 500 LEU D 183 -64.00 -97.52 REMARK 500 TYR D 186 -6.37 85.53 REMARK 500 ALA D 187 -3.76 81.29 REMARK 500 SER D 188 -51.25 -122.89 REMARK 500 SER D 213 72.71 57.98 REMARK 500 ASN D 228 -71.56 -73.73 REMARK 500 ARG C 54 3.59 86.01 REMARK 500 SER C 85 71.22 54.64 REMARK 500 ASP C 100 -5.60 83.32 REMARK 500 SER C 166 -125.94 60.53 REMARK 500 LEU C 183 -60.47 -96.59 REMARK 500 ALA C 187 0.70 59.63 REMARK 500 SER C 188 -66.35 -136.11 REMARK 500 SER C 213 71.87 58.44 REMARK 500 ASN C 228 -71.52 -73.96 REMARK 500 REMARK 500 REMARK: NULL