REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH S.B.LARSON,Y.G.KUZNETSOV,J.DAY,J.ZHOU,S.GLASER, REMARK 1 AUTH 2 G.BRASLAWSKY,A.MCPHERSON REMARK 1 TITL COMBINED USE OF AFM AND X-RAY DIFFRACTION TO REMARK 1 TITL 2 ANALYZE CRYSTALS OF AN ENGINEERED, DOMAIN-DELETED REMARK 1 TITL 3 ANTIBODY REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 61 416 2005 REMARK 1 REFN ISSN 0907-4449 REMARK 1 PMID 15805596 REMARK 1 DOI 10.1107/S0907444905001216 REMARK 2 REMARK 2 RESOLUTION. 2.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.1 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) : 2.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.13 REMARK 3 DATA CUTOFF (SIGMA(F)) : 4.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 38542.320 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.5 REMARK 3 NUMBER OF REFLECTIONS : 76662 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) : 0.246 REMARK 3 FREE R VALUE : 0.296 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.700 REMARK 3 FREE R VALUE TEST SET COUNT : 5924 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 10 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.80 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.90 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.00 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6992 REMARK 3 BIN R VALUE (WORKING SET) : 0.3830 REMARK 3 BIN FREE R VALUE : 0.4050 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 6.10 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 452 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.019 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 16740 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 22.70 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.40 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 16.32000 REMARK 3 B22 (A**2) : -3.31000 REMARK 3 B33 (A**2) : -13.01000 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 COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.38 REMARK 3 ESD FROM SIGMAA (A) : 0.72 REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00 REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.48 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.80 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.013 REMARK 3 BOND ANGLES (DEGREES) : 1.88 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 27.30 REMARK 3 IMPROPER ANGLES (DEGREES) : 1.32 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 1.380 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.420 ; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 1.520 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.390 ; 2.500 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : FLAT MODEL REMARK 3 KSOL : 0.33 REMARK 3 BSOL : 29.13 REMARK 3 REMARK 3 NCS MODEL : RESTRAINED REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : 0.087 ; 210 REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; 6.000 REMARK 3 GROUP 2 POSITIONAL (A) : 0.148 ; 150 REMARK 3 GROUP 2 B-FACTOR (A**2) : NULL ; 12.000 REMARK 3 GROUP 3 POSITIONAL (A) : 0.085 ; 210 REMARK 3 GROUP 3 B-FACTOR (A**2) : NULL ; 6.000 REMARK 3 GROUP 4 POSITIONAL (A) : 0.093 ; 210 REMARK 3 GROUP 4 B-FACTOR (A**2) : NULL ; 6.000 REMARK 3 GROUP 5 POSITIONAL (A) : 0.109 ; 150 REMARK 3 GROUP 5 B-FACTOR (A**2) : NULL ; 12.000 REMARK 3 GROUP 6 POSITIONAL (A) : 0.110 ; 150 REMARK 3 GROUP 6 B-FACTOR (A**2) : NULL ; 12.000 REMARK 3 GROUP 7 POSITIONAL (A) : 0.109 ; 210 REMARK 3 GROUP 7 B-FACTOR (A**2) : NULL ; 6.000 REMARK 3 GROUP 8 POSITIONAL (A) : 0.136 ; 210 REMARK 3 GROUP 8 B-FACTOR (A**2) : NULL ; 6.000 REMARK 3 REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM REMARK 3 PARAMETER FILE 2 : NULL REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP REMARK 3 TOPOLOGY FILE 2 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: USED NCS RESTRAINTS FOR EQUIVALENT REMARK 3 CHAINS REMARK 4 REMARK 4 1ZA6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-APR-05. REMARK 100 THE RCSB ID CODE IS RCSB032491. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 04-OCT-03 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 7.20 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ALS REMARK 200 BEAMLINE : 5.0.2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9194 REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL, SI(1 1 1) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK V. 9.0 REMARK 200 DATA SCALING SOFTWARE : D*TREK V. 9.0 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 76662 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800 REMARK 200 RESOLUTION RANGE LOW (A) : 45.130 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 9.060 REMARK 200 R MERGE (I) : 0.15200 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 10.9000 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 (%) : 98.0 REMARK 200 DATA REDUNDANCY IN SHELL : 7.62 REMARK 200 R MERGE FOR SHELL (I) : 0.36500 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 5.000 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: CNS 1.1 REMARK 200 STARTING MODEL: PDB ENTRY 1BBJ; PDB ENTRY 1FC1 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 62.30 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.29 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 4 M SODIUM FORMATE, 1.5 MM TRITON X REMARK 280 -100 DETERGENT, PH 7.2, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 290K, PH 7.20 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2 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 41.27000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 112.10000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 41.27000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 112.10000 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 300 REMARK: CHAINS A, B, C, D ARE THE PRESUMED BIOLOGICAL UNIT 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: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 10260 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 48510 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -65.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 10570 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 48180 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -59.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, 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 350 REMARK 350 BIOMOLECULE: 3 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXADECAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 62170 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 172860 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -263.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 82.54000 REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 224.20000 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 4 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 23910 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 93610 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -137.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, 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 ASP B 219 REMARK 465 LYS B 220 REMARK 465 THR B 221 REMARK 465 HIS B 222 REMARK 465 THR B 223 REMARK 465 CYS B 224 REMARK 465 PRO B 225 REMARK 465 PRO B 226 REMARK 465 CYS B 227 REMARK 465 GLY B 228 REMARK 465 GLY B 229 REMARK 465 GLY B 230 REMARK 465 SER B 231 REMARK 465 SER B 232 REMARK 465 GLY B 233 REMARK 465 GLY B 234 REMARK 465 GLY B 235 REMARK 465 SER B 236 REMARK 465 GLY B 237 REMARK 465 GLY B 238 REMARK 465 ASP D 219 REMARK 465 LYS D 220 REMARK 465 THR D 221 REMARK 465 HIS D 222 REMARK 465 THR D 223 REMARK 465 CYS D 224 REMARK 465 PRO D 225 REMARK 465 PRO D 226 REMARK 465 CYS D 227 REMARK 465 GLY D 228 REMARK 465 GLY D 229 REMARK 465 GLY D 230 REMARK 465 SER D 231 REMARK 465 SER D 232 REMARK 465 GLY D 233 REMARK 465 GLY D 234 REMARK 465 GLY D 235 REMARK 465 SER D 236 REMARK 465 GLY D 237 REMARK 465 GLY D 238 REMARK 465 ASP F 219 REMARK 465 LYS F 220 REMARK 465 THR F 221 REMARK 465 HIS F 222 REMARK 465 THR F 223 REMARK 465 CYS F 224 REMARK 465 PRO F 225 REMARK 465 PRO F 226 REMARK 465 CYS F 227 REMARK 465 GLY F 228 REMARK 465 GLY F 229 REMARK 465 GLY F 230 REMARK 465 SER F 231 REMARK 465 SER F 232 REMARK 465 GLY F 233 REMARK 465 GLY F 234 REMARK 465 GLY F 235 REMARK 465 SER F 236 REMARK 465 GLY F 237 REMARK 465 GLY F 238 REMARK 465 ASP H 219 REMARK 465 LYS H 220 REMARK 465 THR H 221 REMARK 465 HIS H 222 REMARK 465 THR H 223 REMARK 465 CYS H 224 REMARK 465 PRO H 225 REMARK 465 PRO H 226 REMARK 465 CYS H 227 REMARK 465 GLY H 228 REMARK 465 GLY H 229 REMARK 465 GLY H 230 REMARK 465 SER H 231 REMARK 465 SER H 232 REMARK 465 GLY H 233 REMARK 465 GLY H 234 REMARK 465 GLY H 235 REMARK 465 SER H 236 REMARK 465 GLY H 237 REMARK 465 GLY H 238 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 A 119 CA - N - CD ANGL. DEV. = -17.2 DEGREES REMARK 500 PRO A 147 C - N - CA ANGL. DEV. = 15.5 DEGREES REMARK 500 LEU B 86 CA - CB - CG ANGL. DEV. = -14.2 DEGREES REMARK 500 ASN B 258 N - CA - C ANGL. DEV. = -17.4 DEGREES REMARK 500 LEU C 142 CA - CB - CG ANGL. DEV. = 14.8 DEGREES REMARK 500 CYS D 22 CA - CB - SG ANGL. DEV. = 6.7 DEGREES REMARK 500 CYS D 96 CA - CB - SG ANGL. DEV. = 7.7 DEGREES REMARK 500 SER E 120 N - CA - C ANGL. DEV. = -17.5 DEGREES REMARK 500 PRO E 147 C - N - CA ANGL. DEV. = -14.7 DEGREES REMARK 500 PRO E 147 C - N - CD ANGL. DEV. = 15.0 DEGREES REMARK 500 CYS F 96 CA - CB - SG ANGL. DEV. = 8.0 DEGREES REMARK 500 CYS H 22 CA - CB - SG ANGL. DEV. = 7.5 DEGREES REMARK 500 PRO H 271 C - N - CA ANGL. DEV. = -23.4 DEGREES REMARK 500 PRO H 271 C - N - CD ANGL. DEV. = 20.2 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 PRO A 46 119.40 -17.66 REMARK 500 PRO A 50 153.74 -40.83 REMARK 500 ALA A 57 -28.66 64.69 REMARK 500 SER A 58 24.12 -154.96 REMARK 500 SER A 62 -59.51 -28.17 REMARK 500 ASP A 88 -3.91 -57.54 REMARK 500 ALA A 90 -164.50 -173.37 REMARK 500 THR A 115 135.29 113.82 REMARK 500 ASN A 144 75.93 53.79 REMARK 500 TYR A 146 132.64 -170.17 REMARK 500 ASN A 158 39.63 32.81 REMARK 500 SER A 177 50.20 38.60 REMARK 500 SER A 188 154.92 -48.75 REMARK 500 ARG A 217 -72.36 -26.03 REMARK 500 GLU A 219 130.49 -22.04 REMARK 500 PHE B 29 -31.92 -31.19 REMARK 500 THR B 30 30.32 -98.44 REMARK 500 GLN B 43 165.29 -2.32 REMARK 500 SER B 77 35.78 78.41 REMARK 500 SER B 85 65.10 38.34 REMARK 500 ALA B 92 178.35 173.37 REMARK 500 SER B 99 167.05 81.23 REMARK 500 ALA B 116 153.14 -47.34 REMARK 500 SER B 130 156.93 172.20 REMARK 500 SER B 132 -24.95 62.49 REMARK 500 ASP B 146 82.22 54.37 REMARK 500 PHE B 148 140.73 -170.78 REMARK 500 ASN B 157 47.07 35.83 REMARK 500 SER B 158 70.32 44.17 REMARK 500 PRO B 215 146.19 -39.10 REMARK 500 GLN B 259 101.95 85.19 REMARK 500 SER B 280 -98.66 -114.34 REMARK 500 ASN B 281 -138.64 -69.70 REMARK 500 SER B 297 -7.61 -50.48 REMARK 500 ASN B 331 25.15 -142.41 REMARK 500 THR B 334 148.88 -173.68 REMARK 500 PRO B 342 82.88 -69.10 REMARK 500 GLU C 17 176.76 -50.17 REMARK 500 PRO C 46 120.74 -31.18 REMARK 500 PRO C 50 161.10 -47.13 REMARK 500 ALA C 57 -22.82 54.24 REMARK 500 SER C 58 30.94 -160.07 REMARK 500 VAL C 84 153.41 -48.93 REMARK 500 ALA C 90 -161.24 179.12 REMARK 500 TYR C 146 -114.39 -96.51 REMARK 500 PRO C 147 113.05 -16.16 REMARK 500 GLU C 149 128.33 -36.13 REMARK 500 LYS C 175 -57.48 -121.52 REMARK 500 PHE D 29 -44.81 -29.22 REMARK 500 PRO D 41 104.39 -31.29 REMARK 500 GLN D 43 -139.84 -66.77 REMARK 500 ARG D 44 143.63 -32.13 REMARK 500 SER D 85 63.20 25.17 REMARK 500 SER D 88 -52.17 -28.94 REMARK 500 ALA D 92 178.43 176.71 REMARK 500 SER D 99 173.72 66.48 REMARK 500 MET D 102 65.57 -67.80 REMARK 500 ALA D 116 152.49 -46.27 REMARK 500 SER D 130 -161.39 128.72 REMARK 500 SER D 132 16.58 35.21 REMARK 500 SER D 134 -32.34 -138.67 REMARK 500 ASP D 146 75.34 35.35 REMARK 500 ASN D 157 50.51 31.35 REMARK 500 THR D 162 -39.27 -140.04 REMARK 500 ASN D 206 48.82 34.73 REMARK 500 ASP D 210 41.48 -146.17 REMARK 500 LYS D 216 -170.35 52.21 REMARK 500 SER D 217 81.96 -179.87 REMARK 500 GLN D 259 100.14 77.46 REMARK 500 SER D 272 14.54 -65.07 REMARK 500 GLU D 279 142.90 179.52 REMARK 500 SER D 280 -89.55 -96.42 REMARK 500 ASN D 281 -131.82 -82.04 REMARK 500 SER D 297 -3.82 -59.94 REMARK 500 HIS D 326 149.39 -175.73 REMARK 500 HIS D 332 8.95 59.37 REMARK 500 GLU E 17 177.14 -56.75 REMARK 500 PRO E 46 126.18 -30.04 REMARK 500 LEU E 53 -64.45 -103.70 REMARK 500 ALA E 57 -32.37 67.40 REMARK 500 SER E 58 15.03 -150.63 REMARK 500 SER E 62 -57.97 -28.89 REMARK 500 ARG E 67 -5.80 -59.82 REMARK 500 VAL E 84 161.64 -49.06 REMARK 500 ASP E 88 -5.85 -56.18 REMARK 500 ALA E 90 -162.25 -169.87 REMARK 500 THR E 115 136.62 137.82 REMARK 500 TYR E 146 -92.35 -103.59 REMARK 500 ARG E 217 88.68 -50.28 REMARK 500 PHE F 29 -36.50 -34.05 REMARK 500 ASN F 40 -159.48 -75.08 REMARK 500 PRO F 41 -106.10 -65.95 REMARK 500 ARG F 44 -160.00 -60.40 REMARK 500 SER F 85 66.42 31.09 REMARK 500 ALA F 92 178.17 179.53 REMARK 500 SER F 99 173.34 72.52 REMARK 500 PRO F 128 175.63 -48.52 REMARK 500 SER F 132 -10.59 56.93 REMARK 500 LEU F 191 102.80 -34.08 REMARK 500 GLN F 259 104.81 84.81 REMARK 500 SER F 272 -8.31 -54.70 REMARK 500 SER F 280 -93.99 -111.38 REMARK 500 ASN F 281 -143.33 -83.13 REMARK 500 SER F 297 -9.07 -56.32 REMARK 500 ASN F 318 119.44 21.04 REMARK 500 GLU G 17 172.07 -53.76 REMARK 500 SER G 32 -34.00 -35.81 REMARK 500 PRO G 46 120.28 -30.49 REMARK 500 PRO G 50 153.30 -42.65 REMARK 500 LEU G 53 -68.88 -96.05 REMARK 500 ALA G 57 -25.94 57.66 REMARK 500 SER G 58 23.44 -156.25 REMARK 500 SER G 62 -37.83 -32.95 REMARK 500 ARG G 67 -7.67 -54.86 REMARK 500 VAL G 84 161.53 -47.54 REMARK 500 ALA G 90 -163.23 174.72 REMARK 500 GLU G 149 126.03 -39.73 REMARK 500 ASN G 164 24.56 -149.71 REMARK 500 LYS G 175 -68.02 -102.63 REMARK 500 ALA G 190 -73.40 -61.19 REMARK 500 PRO G 210 129.10 -33.30 REMARK 500 ARG G 217 -120.89 167.75 REMARK 500 GLU G 219 -50.97 -154.99 REMARK 500 PRO H 41 62.74 -14.46 REMARK 500 GLN H 43 -124.50 -85.27 REMARK 500 ARG H 44 120.99 -27.04 REMARK 500 SER H 77 31.29 73.70 REMARK 500 SER H 85 60.97 38.25 REMARK 500 ALA H 92 -177.60 -175.01 REMARK 500 SER H 99 169.32 69.99 REMARK 500 ALA H 116 156.91 -48.52 REMARK 500 PRO H 128 -160.51 -49.86 REMARK 500 LYS H 131 -77.20 -62.83 REMARK 500 PRO H 149 -166.86 -100.40 REMARK 500 THR H 162 -37.30 -137.39 REMARK 500 LEU H 191 102.42 -51.61 REMARK 500 GLU H 214 140.94 -170.91 REMARK 500 LEU H 255 25.89 -75.92 REMARK 500 GLN H 259 103.66 78.32 REMARK 500 TYR H 270 -75.35 -96.48 REMARK 500 SER H 272 2.21 -59.42 REMARK 500 SER H 280 -92.35 -101.65 REMARK 500 ASN H 281 -126.02 -75.33 REMARK 500 PRO H 293 154.37 -49.67 REMARK 500 SER H 297 10.81 -59.59 REMARK 500 ASN H 318 149.98 49.77 REMARK 500 HIS H 326 142.50 -176.05 REMARK 500 HIS H 330 -39.58 -36.77 REMARK 500 PRO H 342 82.85 -69.89 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 TYR B 304 0.07 SIDE_CHAIN REMARK 500 TYR C 92 0.07 SIDE_CHAIN REMARK 500 TYR C 146 0.07 SIDE_CHAIN REMARK 500 TYR G 92 0.08 SIDE_CHAIN REMARK 500 TYR G 98 0.06 SIDE_CHAIN REMARK 500 TYR G 146 0.08 SIDE_CHAIN REMARK 500 TYR H 270 0.07 SIDE_CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 999 REMARK 999 SEQUENCE REMARK 999 THERE WAS NO SUITABLE SEQUENCE DATABASE MATCH REMARK 999 AT TIME OF PROCESSING.