REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 3.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU, REMARK 3 : READ,RICE,SIMONSON,WARREN REMARK 3 REMARK 3 REFINEMENT TARGET : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 18.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 86.0 REMARK 3 NUMBER OF REFLECTIONS : 21346 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 SET) : 0.250 REMARK 3 FREE R VALUE : 0.319 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 1091 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.00 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.05 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.3510 REMARK 3 BIN FREE R VALUE : 0.3870 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : 38 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 8432 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 85 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 69.10 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.60 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM SIGMAA (A) : NULL REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM C-V SIGMAA (A) : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.012 REMARK 3 BOND ANGLES (DEGREES) : 1.66 REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : NULL REMARK 3 KSOL : NULL REMARK 3 BSOL : NULL REMARK 3 REMARK 3 NCS MODEL : NULL REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : NULL REMARK 3 TOPOLOGY FILE 1 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1PKQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-JUN-03. REMARK 100 THE RCSB ID CODE IS RCSB019395. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 10-NOV-02 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : MPG/DESY, HAMBURG REMARK 200 BEAMLINE : BW6 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0500 REMARK 200 MONOCHROMATOR : SI(111) DOUBLE CRYSTAL, NON REMARK 200 DISPERSIVE REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22442 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000 REMARK 200 RESOLUTION RANGE LOW (A) : 18.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 86.7 REMARK 200 DATA REDUNDANCY : 2.300 REMARK 200 R MERGE (I) : 0.09400 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 5.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.09 REMARK 200 COMPLETENESS FOR SHELL (%) : 73.0 REMARK 200 DATA REDUNDANCY IN SHELL : 1.90 REMARK 200 R MERGE FOR SHELL (I) : 0.35100 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.000 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: AMORE, BEAST REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 53.55 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS/HCL, MOPS, NACL, PEG8000, PH REMARK 280 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,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 20.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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 APPLY THE FOLLOWING TO CHAINS: A, B, 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: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, G, J 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 MET A -20 REMARK 465 LYS A -19 REMARK 465 GLN A -18 REMARK 465 SER A -17 REMARK 465 THR A -16 REMARK 465 ILE A -15 REMARK 465 ALA A -14 REMARK 465 LEU A -13 REMARK 465 ALA A -12 REMARK 465 LEU A -11 REMARK 465 LEU A -10 REMARK 465 PRO A -9 REMARK 465 LEU A -8 REMARK 465 LEU A -7 REMARK 465 PHE A -6 REMARK 465 THR A -5 REMARK 465 PRO A -4 REMARK 465 VAL A -3 REMARK 465 THR A -2 REMARK 465 LYS A -1 REMARK 465 ALA A 0 REMARK 465 CYS A 214 REMARK 465 MET B -20 REMARK 465 LYS B -19 REMARK 465 LYS B -18 REMARK 465 THR B -17 REMARK 465 ALA B -16 REMARK 465 ILE B -15 REMARK 465 ALA B -14 REMARK 465 ILE B -13 REMARK 465 ALA B -12 REMARK 465 VAL B -11 REMARK 465 ALA B -10 REMARK 465 LEU B -9 REMARK 465 ALA B -8 REMARK 465 GLY B -7 REMARK 465 PHE B -6 REMARK 465 ALA B -5 REMARK 465 THR B -4 REMARK 465 VAL B -3 REMARK 465 ALA B -2 REMARK 465 GLN B -1 REMARK 465 ALA B 0 REMARK 465 SER B 217 REMARK 465 ALA B 218 REMARK 465 TRP B 219 REMARK 465 SER B 220 REMARK 465 HIS B 221 REMARK 465 PRO B 222 REMARK 465 GLN B 223 REMARK 465 PHE B 224 REMARK 465 GLU B 225 REMARK 465 LYS B 226 REMARK 465 MET E -1 REMARK 465 ARG E 0 REMARK 465 TYR E 120 REMARK 465 TRP E 121 REMARK 465 ILE E 122 REMARK 465 ASN E 123 REMARK 465 PRO E 124 REMARK 465 GLY E 125 REMARK 465 ARG E 126 REMARK 465 SER E 127 REMARK 465 ARG E 128 REMARK 465 SER E 129 REMARK 465 HIS E 130 REMARK 465 HIS E 131 REMARK 465 HIS E 132 REMARK 465 HIS E 133 REMARK 465 HIS E 134 REMARK 465 HIS E 135 REMARK 465 MET F -20 REMARK 465 LYS F -19 REMARK 465 GLN F -18 REMARK 465 SER F -17 REMARK 465 THR F -16 REMARK 465 ILE F -15 REMARK 465 ALA F -14 REMARK 465 LEU F -13 REMARK 465 ALA F -12 REMARK 465 LEU F -11 REMARK 465 LEU F -10 REMARK 465 PRO F -9 REMARK 465 LEU F -8 REMARK 465 LEU F -7 REMARK 465 PHE F -6 REMARK 465 THR F -5 REMARK 465 PRO F -4 REMARK 465 VAL F -3 REMARK 465 THR F -2 REMARK 465 LYS F -1 REMARK 465 ALA F 0 REMARK 465 ARG F 211 REMARK 465 GLY F 212 REMARK 465 GLU F 213 REMARK 465 CYS F 214 REMARK 465 MET G -20 REMARK 465 LYS G -19 REMARK 465 LYS G -18 REMARK 465 THR G -17 REMARK 465 ALA G -16 REMARK 465 ILE G -15 REMARK 465 ALA G -14 REMARK 465 ILE G -13 REMARK 465 ALA G -12 REMARK 465 VAL G -11 REMARK 465 ALA G -10 REMARK 465 LEU G -9 REMARK 465 ALA G -8 REMARK 465 GLY G -7 REMARK 465 PHE G -6 REMARK 465 ALA G -5 REMARK 465 THR G -4 REMARK 465 VAL G -3 REMARK 465 ALA G -2 REMARK 465 GLN G -1 REMARK 465 ALA G 0 REMARK 465 LYS G 129 REMARK 465 SER G 130 REMARK 465 THR G 131 REMARK 465 SER G 132 REMARK 465 LYS G 214 REMARK 465 SER G 215 REMARK 465 CYS G 216 REMARK 465 SER G 217 REMARK 465 ALA G 218 REMARK 465 TRP G 219 REMARK 465 SER G 220 REMARK 465 HIS G 221 REMARK 465 PRO G 222 REMARK 465 GLN G 223 REMARK 465 PHE G 224 REMARK 465 GLU G 225 REMARK 465 LYS G 226 REMARK 465 MET J -3 REMARK 465 ARG J -2 REMARK 465 GLY J -1 REMARK 465 SER J 0 REMARK 465 PHE J 119 REMARK 465 TYR J 120 REMARK 465 TRP J 121 REMARK 465 ILE J 122 REMARK 465 ASN J 123 REMARK 465 PRO J 124 REMARK 465 GLY J 125 REMARK 465 ARG J 126 REMARK 465 SER J 127 REMARK 465 ARG J 128 REMARK 465 SER J 129 REMARK 465 HIS J 130 REMARK 465 HIS J 131 REMARK 465 HIS J 132 REMARK 465 HIS J 133 REMARK 465 HIS J 134 REMARK 465 HIS J 135 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 GLU B 1 CG CD OE1 OE2 REMARK 470 LYS B 210 CG CD CE NZ REMARK 470 LYS B 214 CG CD CE NZ REMARK 470 SER B 215 OG REMARK 470 CYS B 216 SG REMARK 470 PHE E 119 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLU G 1 CG CD OE1 OE2 REMARK 470 LYS G 210 CG CD CE NZ REMARK 480 REMARK 480 ZERO OCCUPANCY ATOM REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 480 M RES C SSEQI ATOMS REMARK 480 LYS A 18 CE NZ REMARK 480 LYS A 24 CE NZ REMARK 480 GLN A 30E CG CD OE1 NE2 REMARK 480 LYS A 30F CE NZ REMARK 480 LYS A 149 CE NZ REMARK 480 LYS A 169 CE NZ REMARK 480 LYS A 188 CG CD CE NZ REMARK 480 LYS A 190 CE NZ REMARK 480 LYS B 23 CD CE NZ REMARK 480 LYS B 64 CG CD CE NZ REMARK 480 LYS B 117 CE NZ REMARK 480 LYS B 129 CB CG CD CE NZ REMARK 480 LYS B 201 CB CG CD CE NZ REMARK 480 LYS B 206 CG CD CE NZ REMARK 480 LYS E 55 CG CD CE NZ REMARK 480 ARG E 66 CD NE CZ NH1 NH2 REMARK 480 GLU E 74 CG CD OE1 OE2 REMARK 480 LYS E 80 CE NZ REMARK 480 GLU E 93 CG CD OE1 OE2 REMARK 480 LYS F 18 CE NZ REMARK 480 LYS F 24 CG CD CE NZ REMARK 480 GLN F 30E CG CD OE1 NE2 REMARK 480 LYS F 149 CE NZ REMARK 480 LYS F 169 CE NZ REMARK 480 LYS F 183 CG CD NZ REMARK 480 LYS F 188 CG CD CE NZ REMARK 480 LYS F 190 CE NZ REMARK 480 LYS G 23 CD CE NZ REMARK 480 LYS G 64 CG CD CE NZ REMARK 480 LYS G 117 CG CD CE NZ REMARK 480 LYS G 201 CB CG CD CE NZ REMARK 480 LYS G 206 CG CD CE NZ REMARK 480 GLU J 19 CD OE1 OE2 REMARK 480 LYS J 55 CG CD CE NZ REMARK 480 ARG J 66 CD NE CZ NH1 NH2 REMARK 480 GLU J 74 CD OE1 OE2 REMARK 480 LYS J 80 CE NZ REMARK 480 ASN J 87 CG OD1 ND2 REMARK 480 PHE J 90 CG CD1 CD2 CE1 CE2 CZ REMARK 480 GLU J 93 CG CD OE1 OE2 REMARK 480 LYS J 114 CG CD CE NZ 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 OG SER B 130 O ALA B 137 2.17 REMARK 500 OG SER G 203 OG1 THR G 205 2.18 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 SER B 120 N - CA - C ANGL. DEV. = -16.9 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 10 145.36 178.39 REMARK 500 ALA A 51 -29.59 70.38 REMARK 500 SER A 52 65.99 -161.24 REMARK 500 SER A 67 170.98 172.36 REMARK 500 VAL A 78 150.86 -47.28 REMARK 500 ALA A 84 -172.55 175.55 REMARK 500 HIS A 92 -31.49 -135.82 REMARK 500 ARG A 108 -159.40 -147.97 REMARK 500 LYS A 126 -15.78 -49.10 REMARK 500 ASN A 138 80.81 38.64 REMARK 500 PRO A 141 -171.05 -66.18 REMARK 500 ALA B 9 129.99 -28.79 REMARK 500 PRO B 14 153.70 -48.07 REMARK 500 ALA B 16 -155.60 -120.33 REMARK 500 PHE B 29 -34.39 -37.27 REMARK 500 PRO B 41 -58.67 -24.42 REMARK 500 ALA B 88 -172.86 -174.66 REMARK 500 MET B 100A 48.04 83.01 REMARK 500 SER B 112 136.41 -176.71 REMARK 500 SER B 113 48.95 -84.82 REMARK 500 SER B 127 -168.96 -170.68 REMARK 500 LEU B 138 -160.17 -125.27 REMARK 500 ALA B 158 10.43 -64.79 REMARK 500 THR B 160 -48.63 -146.70 REMARK 500 ALA B 168 177.45 -51.86 REMARK 500 LEU B 189 -39.37 -36.86 REMARK 500 PRO B 202 6.46 -52.55 REMARK 500 SER B 203 -12.67 -143.35 REMARK 500 ASN B 204 -8.99 85.46 REMARK 500 LYS B 214 -172.46 178.87 REMARK 500 SER B 215 37.22 -143.05 REMARK 500 VAL E 16 157.95 -46.62 REMARK 500 ASP E 18 -164.82 -107.28 REMARK 500 ASN E 31 92.18 -59.86 REMARK 500 ALA E 32 37.69 -86.77 REMARK 500 MET E 35 171.19 -55.27 REMARK 500 SER E 42 -60.27 -12.93 REMARK 500 PRO E 43 -77.79 -45.65 REMARK 500 GLU E 70 151.35 179.55 REMARK 500 ASN E 87 54.02 39.06 REMARK 500 VAL E 88 151.87 -47.82 REMARK 500 SER E 91 -0.43 -55.46 REMARK 500 HIS E 103 -83.50 60.40 REMARK 500 GLN E 106 118.48 -165.59 REMARK 500 SER F 7 139.68 -173.77 REMARK 500 SER F 10 144.13 178.41 REMARK 500 ALA F 51 -29.43 69.05 REMARK 500 SER F 52 66.27 -160.31 REMARK 500 SER F 67 178.21 176.68 REMARK 500 VAL F 78 152.92 -45.81 REMARK 500 ALA F 84 -172.83 173.35 REMARK 500 HIS F 92 -30.64 -134.49 REMARK 500 ARG F 108 -158.76 -148.74 REMARK 500 ASP F 122 -74.75 -16.45 REMARK 500 GLU F 123 -36.71 -35.77 REMARK 500 ASN F 138 81.64 37.93 REMARK 500 PRO F 141 -171.56 -66.56 REMARK 500 LEU F 154 150.03 -49.77 REMARK 500 ALA G 9 130.00 -28.15 REMARK 500 PRO G 14 156.14 -47.19 REMARK 500 ALA G 16 -156.37 -119.07 REMARK 500 TYR G 27 170.40 179.06 REMARK 500 THR G 28 83.53 -69.56 REMARK 500 PHE G 29 -34.44 -39.72 REMARK 500 ALA G 88 -170.84 -172.72 REMARK 500 MET G 100A 47.15 84.47 REMARK 500 SER G 127 -168.14 -169.72 REMARK 500 LEU G 138 -160.62 -123.94 REMARK 500 SER G 156 15.64 57.77 REMARK 500 ALA G 158 9.74 -66.65 REMARK 500 THR G 160 -49.86 -148.13 REMARK 500 ALA G 168 177.72 -52.95 REMARK 500 SER G 172 -9.71 -57.22 REMARK 500 PRO G 202 4.52 -52.40 REMARK 500 SER G 203 -12.70 -141.65 REMARK 500 ASN G 204 -8.81 85.68 REMARK 500 VAL G 211 31.94 -140.50 REMARK 500 GLU G 212 -175.77 -60.05 REMARK 500 VAL J 16 159.31 -46.77 REMARK 500 ASP J 18 -164.30 -109.52 REMARK 500 ASN J 31 94.21 -59.98 REMARK 500 ALA J 32 37.10 -89.84 REMARK 500 MET J 35 171.58 -56.66 REMARK 500 SER J 42 -58.07 -14.33 REMARK 500 PRO J 43 -75.95 -47.62 REMARK 500 GLU J 70 150.02 179.74 REMARK 500 LEU J 72 102.72 -52.93 REMARK 500 GLU J 74 -91.54 -22.65 REMARK 500 SER J 91 6.71 -66.62 REMARK 500 HIS J 103 -93.84 58.65 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1PKO RELATED DB: PDB REMARK 900 MYELIN OLIGODENDROCYTE PROTEIN