REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE) 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) : 2.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.75 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.050 REMARK 3 COMPLETENESS FOR RANGE (%) : 87.7 REMARK 3 NUMBER OF REFLECTIONS : 58690 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.201 REMARK 3 R VALUE (WORKING SET) : 0.195 REMARK 3 FREE R VALUE : 0.260 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100 REMARK 3 FREE R VALUE TEST SET COUNT : 5927 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 29.7540 - 7.7240 0.98 2010 234 0.2080 0.2350 REMARK 3 2 7.7240 - 6.1490 0.98 2013 214 0.1840 0.2430 REMARK 3 3 6.1490 - 5.3770 0.99 2005 222 0.1640 0.2210 REMARK 3 4 5.3770 - 4.8870 0.98 1989 205 0.1410 0.1980 REMARK 3 5 4.8870 - 4.5380 0.99 1997 243 0.1420 0.1820 REMARK 3 6 4.5380 - 4.2720 0.98 1975 231 0.1320 0.1880 REMARK 3 7 4.2720 - 4.0580 0.99 1985 204 0.1500 0.2090 REMARK 3 8 4.0580 - 3.8820 0.99 1973 254 0.1540 0.1990 REMARK 3 9 3.8820 - 3.7330 0.99 1982 213 0.1590 0.2200 REMARK 3 10 3.7330 - 3.6040 0.99 1970 205 0.1700 0.2430 REMARK 3 11 3.6040 - 3.4920 0.99 1981 222 0.1640 0.2220 REMARK 3 12 3.4920 - 3.3920 0.98 1997 185 0.1670 0.2330 REMARK 3 13 3.3920 - 3.3030 0.97 1926 240 0.1870 0.2730 REMARK 3 14 3.3030 - 3.2220 0.97 1982 191 0.2010 0.2830 REMARK 3 15 3.2220 - 3.1490 0.97 1958 240 0.2100 0.2810 REMARK 3 16 3.1490 - 3.0820 0.96 1894 219 0.2080 0.2620 REMARK 3 17 3.0820 - 3.0210 0.96 1899 229 0.2060 0.2850 REMARK 3 18 3.0210 - 2.9640 0.95 1876 216 0.2070 0.2740 REMARK 3 19 2.9640 - 2.9110 0.93 1879 219 0.2190 0.3280 REMARK 3 20 2.9110 - 2.8620 0.91 1806 196 0.2230 0.3030 REMARK 3 21 2.8620 - 2.8150 0.87 1737 200 0.2320 0.3290 REMARK 3 22 2.8150 - 2.7720 0.82 1667 181 0.2490 0.3220 REMARK 3 23 2.7720 - 2.7310 0.78 1527 171 0.2530 0.4070 REMARK 3 24 2.7310 - 2.6930 0.74 1485 171 0.2580 0.3460 REMARK 3 25 2.6930 - 2.6570 0.72 1420 175 0.2850 0.3790 REMARK 3 26 2.6570 - 2.6220 0.66 1301 161 0.2850 0.3630 REMARK 3 27 2.6220 - 2.5890 0.62 1250 125 0.2810 0.3670 REMARK 3 28 2.5890 - 2.5580 0.61 1204 126 0.2730 0.3450 REMARK 3 29 2.5580 - 2.5280 0.56 1148 129 0.2730 0.3350 REMARK 3 30 2.5280 - 2.5000 0.48 927 106 0.2950 0.3540 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : 0.33 REMARK 3 B_SOL : 22.86 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 2.500 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.64 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -2.98800 REMARK 3 B22 (A**2) : -3.97600 REMARK 3 B33 (A**2) : 6.96400 REMARK 3 B12 (A**2) : -0.00000 REMARK 3 B13 (A**2) : -0.22900 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 : 0.009 11302 REMARK 3 ANGLE : 1.192 15312 REMARK 3 CHIRALITY : 0.078 1599 REMARK 3 PLANARITY : 0.005 1981 REMARK 3 DIHEDRAL : 16.113 3890 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 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 3JUY COMPLIES WITH FORMAT V. 3.20, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-SEP-09. REMARK 100 THE RCSB ID CODE IS RCSB055191. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 08-OCT-07 REMARK 200 TEMPERATURE (KELVIN) : 100 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) : 1.0332 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 REMARK 200 DATA SCALING SOFTWARE : HKL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 61604 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 92.3 REMARK 200 DATA REDUNDANCY : 2.700 REMARK 200 R MERGE (I) : 0.12400 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59 REMARK 200 COMPLETENESS FOR SHELL (%) : 65.8 REMARK 200 DATA REDUNDANCY IN SHELL : 1.50 REMARK 200 R MERGE FOR SHELL (I) : 0.41100 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: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 57.89 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 20% W/V PEG-8000, 0.1 M MES, 0.2 M REMARK 280 CALCIUM ACETATE, PH 6.0, SITTING DROP, TEMPERATURE 292K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 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+1/2,Y+1/2,Z 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 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 99.58600 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 57.56500 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 99.58600 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 57.56500 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, 5, 6 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: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A 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: 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: 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: 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: 5 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: E 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: 6 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: F 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 B -5 REMARK 465 HIS B -4 REMARK 465 HIS B -3 REMARK 465 HIS B -2 REMARK 465 HIS B -1 REMARK 465 HIS B 0 REMARK 465 SER B 132 REMARK 465 GLY B 133 REMARK 465 GLY B 134 REMARK 465 GLY B 135 REMARK 465 GLY B 136 REMARK 465 SER B 137 REMARK 465 GLY B 138 REMARK 465 GLY B 139 REMARK 465 GLY B 140 REMARK 465 GLY B 141 REMARK 465 HIS A -5 REMARK 465 HIS A -4 REMARK 465 HIS A -3 REMARK 465 HIS A -2 REMARK 465 HIS A -1 REMARK 465 HIS A 0 REMARK 465 SER A 127 REMARK 465 GLY A 128 REMARK 465 GLY A 129 REMARK 465 GLY A 130 REMARK 465 GLY A 131 REMARK 465 SER A 132 REMARK 465 GLY A 133 REMARK 465 GLY A 134 REMARK 465 GLY A 135 REMARK 465 GLY A 136 REMARK 465 SER A 137 REMARK 465 GLY A 138 REMARK 465 GLY A 139 REMARK 465 GLY A 140 REMARK 465 GLY A 141 REMARK 465 SER A 142 REMARK 465 LYS A 250 REMARK 465 HIS C -5 REMARK 465 HIS C -4 REMARK 465 HIS C -3 REMARK 465 HIS C -2 REMARK 465 HIS C -1 REMARK 465 HIS C 0 REMARK 465 GLY C 128 REMARK 465 GLY C 129 REMARK 465 GLY C 130 REMARK 465 GLY C 131 REMARK 465 SER C 132 REMARK 465 GLY C 133 REMARK 465 GLY C 134 REMARK 465 GLY C 135 REMARK 465 GLY C 136 REMARK 465 SER C 137 REMARK 465 GLY C 138 REMARK 465 GLY C 139 REMARK 465 GLY C 140 REMARK 465 GLY C 141 REMARK 465 HIS E -5 REMARK 465 HIS E -4 REMARK 465 HIS E -3 REMARK 465 HIS E -2 REMARK 465 HIS E -1 REMARK 465 HIS E 0 REMARK 465 GLY E 128 REMARK 465 GLY E 129 REMARK 465 GLY E 130 REMARK 465 GLY E 131 REMARK 465 SER E 132 REMARK 465 GLY E 133 REMARK 465 GLY E 134 REMARK 465 GLY E 135 REMARK 465 GLY E 136 REMARK 465 SER E 137 REMARK 465 GLY E 138 REMARK 465 GLY E 139 REMARK 465 GLY E 140 REMARK 465 GLY E 141 REMARK 465 SER E 142 REMARK 465 LYS E 250 REMARK 465 HIS F -5 REMARK 465 HIS F -4 REMARK 465 HIS F -3 REMARK 465 HIS F -2 REMARK 465 HIS F -1 REMARK 465 HIS F 0 REMARK 465 GLY F 128 REMARK 465 GLY F 129 REMARK 465 GLY F 130 REMARK 465 GLY F 131 REMARK 465 SER F 132 REMARK 465 GLY F 133 REMARK 465 GLY F 134 REMARK 465 GLY F 135 REMARK 465 GLY F 136 REMARK 465 SER F 137 REMARK 465 GLY F 138 REMARK 465 GLY F 139 REMARK 465 GLY F 140 REMARK 465 GLY F 141 REMARK 465 SER F 142 REMARK 465 LYS F 250 REMARK 465 HIS D -5 REMARK 465 HIS D -4 REMARK 465 HIS D -3 REMARK 465 HIS D -2 REMARK 465 HIS D -1 REMARK 465 HIS D 0 REMARK 465 GLY D 128 REMARK 465 GLY D 129 REMARK 465 GLY D 130 REMARK 465 GLY D 131 REMARK 465 SER D 132 REMARK 465 GLY D 133 REMARK 465 GLY D 134 REMARK 465 GLY D 135 REMARK 465 GLY D 136 REMARK 465 SER D 137 REMARK 465 GLY D 138 REMARK 465 GLY D 139 REMARK 465 GLY D 140 REMARK 465 GLY D 141 REMARK 465 SER D 142 REMARK 465 LYS D 250 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 TRP B 104 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP B 104 CZ3 CH2 REMARK 470 ASP B 105 CG OD1 OD2 REMARK 470 ASP B 203 CG OD1 OD2 REMARK 470 SER B 210 OG REMARK 470 LYS B 250 CG CD CE NZ REMARK 470 ASP A 105 CG OD1 OD2 REMARK 470 GLN C 1 CG CD OE1 NE2 REMARK 470 TRP C 104 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP C 104 CZ3 CH2 REMARK 470 GLU C 143 CG CD OE1 OE2 REMARK 470 LYS C 250 CG CD CE NZ REMARK 470 TRP E 104 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP E 104 CZ3 CH2 REMARK 470 ASP E 105 CG OD1 OD2 REMARK 470 ASP E 203 CG OD1 OD2 REMARK 470 ARG E 220 CG CD NE CZ NH1 NH2 REMARK 470 TRP F 104 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP F 104 CZ3 CH2 REMARK 470 ASP F 105 CG OD1 OD2 REMARK 470 GLU F 143 CG CD OE1 OE2 REMARK 470 SER F 237 OG REMARK 470 SER F 238 OG REMARK 470 TRP D 104 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP D 104 CZ3 CH2 REMARK 470 SER D 156 OG REMARK 470 ARG D 172 CG CD NE CZ NH1 NH2 REMARK 470 ASP D 203 CG OD1 OD2 REMARK 470 ARG D 220 CG CD NE CZ NH1 NH2 REMARK 470 SER D 237 OG REMARK 470 SER D 238 OG 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 OD1 ASP F 66 OH TYR D 112 2.19 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 B 127 -159.81 -153.08 REMARK 500 PRO B 157 108.95 -45.33 REMARK 500 GLU B 159 -170.95 -62.02 REMARK 500 ILE B 171 77.86 -100.61 REMARK 500 VAL B 194 -47.20 72.41 REMARK 500 PRO A 41 127.30 -36.08 REMARK 500 ALA A 89 8.50 -69.19 REMARK 500 TYR A 109 6.88 85.31 REMARK 500 LEU A 153 103.17 -161.32 REMARK 500 ARG A 175 70.62 -101.38 REMARK 500 VAL A 194 -45.48 69.91 REMARK 500 ALA C 89 3.69 -69.35 REMARK 500 ASP C 105 72.57 -105.24 REMARK 500 TYR C 109 8.00 80.71 REMARK 500 TYR C 112 31.82 -88.89 REMARK 500 SER C 126 89.16 -66.70 REMARK 500 SER C 154 63.17 -105.52 REMARK 500 PRO C 157 138.07 -35.26 REMARK 500 ILE C 171 77.41 -114.95 REMARK 500 PRO C 183 127.69 -36.28 REMARK 500 PRO C 187 151.11 -47.88 REMARK 500 VAL C 194 -50.57 76.20 REMARK 500 ALA C 227 -172.08 -170.51 REMARK 500 TRP E 104 -34.05 -35.11 REMARK 500 ASP E 105 80.85 -159.90 REMARK 500 VAL E 194 -50.26 73.71 REMARK 500 SER E 199 123.26 -39.62 REMARK 500 ASP E 203 -8.88 -59.81 REMARK 500 GLU E 224 36.11 -71.82 REMARK 500 ALA E 227 170.07 177.49 REMARK 500 SER E 237 27.02 -152.17 REMARK 500 CYS F 22 88.61 -160.42 REMARK 500 TYR F 109 -6.94 73.30 REMARK 500 VAL F 194 -56.50 67.55 REMARK 500 SER F 210 167.71 168.84 REMARK 500 ALA F 227 -166.64 -170.53 REMARK 500 SER F 237 17.81 -150.78 REMARK 500 ALA D 92 -179.80 -176.84 REMARK 500 TYR D 112 30.35 -86.64 REMARK 500 SER D 126 -166.92 -72.27 REMARK 500 PRO D 183 129.09 -36.74 REMARK 500 VAL D 194 -62.95 62.84 REMARK 500 SER D 237 -10.21 -151.38 REMARK 500 REMARK 500 REMARK: NULL