REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH N.BAN,C.ESCOBAR,R.GARCIA,K.HASEL,J.DAY,A.GREENWOOD, REMARK 1 AUTH 2 A.MCPHERSON REMARK 1 TITL CRYSTAL STRUCTURE OF AN IDIOTYPE-ANTI-IDIOTYPE FAB REMARK 1 TITL 2 COMPLEX REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 91 1604 1994 REMARK 1 REFN ISSN 0027-8424 REMARK 1 REFERENCE 2 REMARK 1 AUTH N.BAN,C.ESCOBAR,J.DAY,A.GREENWOOD,A.MCPHERSON REMARK 1 TITL PRELIMINARY CRYSTALLOGRAPHIC STUDY OF A COMPLEX REMARK 1 TITL 2 BETWEEN AN FAB OF A MONOCLONAL FELINE PERITONITIS REMARK 1 TITL 3 VIRUS NEUTRALIZING ANTIBODY AND ITS ANTI-IDIOTYPIC REMARK 1 TITL 4 FAB REMARK 1 REF J.MOL.BIOL. V. 234 894 1993 REMARK 1 REFN ISSN 0022-2836 REMARK 1 REFERENCE 3 REMARK 1 AUTH N.BAN,C.ESCOBAR,J.DAY,A.GREENWOOD,S.LARSON, REMARK 1 AUTH 2 A.MCPHERSON REMARK 1 TITL CHARACTERIZATION OF CRYSTALS OF AN FAB FRAGMENT OF REMARK 1 TITL 2 A MURINE MONOCLONAL ANTIBODY REMARK 1 REF J.MOL.BIOL. V. 222 445 1991 REMARK 1 REFN ISSN 0022-2836 REMARK 2 REMARK 2 RESOLUTION. 2.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 3.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 83.0 REMARK 3 NUMBER OF REFLECTIONS : NULL REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING SET) : 0.220 REMARK 3 FREE R VALUE : NULL REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : NULL 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) : NULL REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : NULL REMARK 3 BIN FREE R VALUE : NULL REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL 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 : 6662 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) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL 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) : 0.021 REMARK 3 BOND ANGLES (DEGREES) : 2.50 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 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 1AIF COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : NULL REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : NULL REMARK 200 RADIATION SOURCE : NULL REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL REMARK 200 WAVELENGTH OR RANGE (A) : NULL REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : NULL REMARK 200 DETECTOR MANUFACTURER : NULL REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL REMARK 200 RESOLUTION RANGE HIGH (A) : NULL REMARK 200 RESOLUTION RANGE LOW (A) : NULL REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : NULL 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) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL 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: NULL REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL REMARK 200 SOFTWARE USED: NULL REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 49.57 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,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 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3770 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20510 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, 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: 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: 3750 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20540 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 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 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 ASN B 31 O ASN B 54 2.10 REMARK 500 OD1 ASN H 31 O ASN H 54 2.17 REMARK 500 O LEU B 53 N SER B 55 2.17 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) 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 RES CSSEQI ATM2 DEVIATION REMARK 500 GLU H 64 CB GLU H 64 CG 0.124 REMARK 500 THR H 194 CA THR H 194 CB 0.157 REMARK 500 TRP A 149 CB TRP A 149 CG -0.111 REMARK 500 GLU B 64 CB GLU B 64 CG 0.143 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 LEU L 34 CA - CB - CG ANGL. DEV. = 15.4 DEGREES REMARK 500 ARG L 212 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 ARG L 212 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES REMARK 500 THR H 28 N - CA - C ANGL. DEV. = -20.4 DEGREES REMARK 500 LEU H 103 CA - CB - CG ANGL. DEV. = -14.1 DEGREES REMARK 500 PRO H 134 N - CA - C ANGL. DEV. = 21.8 DEGREES REMARK 500 PHE H 154 N - CA - C ANGL. DEV. = 18.3 DEGREES REMARK 500 PRO H 155 C - N - CA ANGL. DEV. = -11.9 DEGREES REMARK 500 PRO H 197 N - CA - C ANGL. DEV. = -20.2 DEGREES REMARK 500 SER H 210 N - CA - C ANGL. DEV. = 16.6 DEGREES REMARK 500 LEU A 34 CA - CB - CG ANGL. DEV. = 14.4 DEGREES REMARK 500 THR B 28 N - CA - C ANGL. DEV. = -22.1 DEGREES REMARK 500 LEU B 83 CA - CB - CG ANGL. DEV. = -16.5 DEGREES REMARK 500 PRO B 134 N - CA - C ANGL. DEV. = 18.9 DEGREES REMARK 500 PHE B 154 N - CA - C ANGL. DEV. = 16.2 DEGREES REMARK 500 PRO B 155 C - N - CA ANGL. DEV. = -11.3 DEGREES REMARK 500 PRO B 197 N - CA - C ANGL. DEV. = -20.5 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 L 28 99.28 -59.17 REMARK 500 SER L 31 -62.39 -28.08 REMARK 500 SER L 32 40.84 -68.23 REMARK 500 ASN L 33 25.29 -159.12 REMARK 500 SER L 41 136.93 -22.36 REMARK 500 PRO L 47 108.37 -42.40 REMARK 500 TRP L 48 -63.15 -97.07 REMARK 500 SER L 57 103.45 -36.44 REMARK 500 SER L 68 123.67 -175.36 REMARK 500 SER L 77 -82.15 -47.29 REMARK 500 ALA L 84 22.85 -59.71 REMARK 500 ASN L 93 -70.93 -78.92 REMARK 500 PRO L 121 165.36 -43.89 REMARK 500 GLU L 124 -71.33 -38.77 REMARK 500 ASP L 152 79.23 51.25 REMARK 500 SER L 154 103.42 -57.05 REMARK 500 VAL L 160 103.02 -39.73 REMARK 500 GLN L 167 146.69 -34.48 REMARK 500 SER L 172 56.09 72.87 REMARK 500 ARG L 189 -4.29 -45.54 REMARK 500 ASN L 191 -62.87 -131.42 REMARK 500 SER L 192 100.03 -58.40 REMARK 500 CYS L 195 72.78 -114.09 REMARK 500 LYS L 200 -29.50 -12.94 REMARK 500 THR L 201 32.67 -92.37 REMARK 500 SER L 202 93.52 163.76 REMARK 500 PRO L 205 174.33 -28.94 REMARK 500 VAL L 207 47.89 -141.29 REMARK 500 ARG L 212 118.61 -167.16 REMARK 500 GLU L 214 -76.95 -69.40 REMARK 500 LYS H 3 98.68 -165.64 REMARK 500 LYS H 19 81.13 -162.40 REMARK 500 CYS H 22 140.60 178.54 REMARK 500 THR H 28 74.22 -160.20 REMARK 500 ASN H 30 -64.89 -0.57 REMARK 500 TYR H 32 -159.82 -131.51 REMARK 500 VAL H 48 -70.61 -86.90 REMARK 500 ALA H 49 -164.95 -125.48 REMARK 500 GLU H 50 113.58 171.00 REMARK 500 ASN H 54 -29.65 -18.62 REMARK 500 SER H 55 -25.75 151.86 REMARK 500 ASN H 57 -74.83 -36.13 REMARK 500 TYR H 62 -158.51 -122.05 REMARK 500 GLU H 64 -54.03 -15.03 REMARK 500 VAL H 66 -37.31 -158.80 REMARK 500 ARG H 74 129.39 -171.70 REMARK 500 SER H 79 -3.85 78.59 REMARK 500 GLU H 91 -46.63 -27.81 REMARK 500 LEU H 103 47.19 -88.77 REMARK 500 ALA H 107 -154.06 178.60 REMARK 500 THR H 115 143.92 -170.20 REMARK 500 ALA H 122 -160.13 -60.93 REMARK 500 ALA H 133 -174.82 -63.70 REMARK 500 ALA H 137 114.28 177.41 REMARK 500 THR H 140 91.31 -34.40 REMARK 500 ASN H 141 -179.19 56.72 REMARK 500 MET H 143 165.25 159.10 REMARK 500 PHE H 154 -55.37 -121.40 REMARK 500 ASN H 163 82.75 60.98 REMARK 500 SER H 164 45.50 32.94 REMARK 500 SER H 169 84.54 -44.52 REMARK 500 SER H 180 63.96 91.10 REMARK 500 ASP H 181 51.84 29.52 REMARK 500 SER H 193 -45.82 -13.52 REMARK 500 SER H 198 -22.83 -39.96 REMARK 500 GLU H 199 -36.37 -27.34 REMARK 500 PRO H 208 -36.52 -35.24 REMARK 500 SER H 210 0.54 84.89 REMARK 500 THR H 212 95.04 -176.71 REMARK 500 LYS H 213 -152.97 -86.68 REMARK 500 VAL H 214 172.78 179.53 REMARK 500 SER A 28 96.93 -64.90 REMARK 500 SER A 31 -64.25 -24.36 REMARK 500 SER A 32 39.03 -65.76 REMARK 500 ASN A 33 24.72 -156.43 REMARK 500 SER A 41 135.61 -21.04 REMARK 500 PRO A 47 103.90 -41.05 REMARK 500 TRP A 48 -66.79 -93.40 REMARK 500 SER A 57 101.65 -35.49 REMARK 500 SER A 66 149.69 -175.17 REMARK 500 SER A 68 124.32 -172.77 REMARK 500 SER A 77 -77.63 -49.20 REMARK 500 ALA A 84 21.66 -62.06 REMARK 500 ASN A 93 -73.87 -77.34 REMARK 500 PRO A 121 164.91 -41.88 REMARK 500 SER A 123 -65.34 -27.41 REMARK 500 GLU A 124 -71.37 -40.46 REMARK 500 ASP A 152 79.31 51.47 REMARK 500 VAL A 160 104.24 -33.71 REMARK 500 GLN A 167 146.90 -34.29 REMARK 500 SER A 172 52.57 72.22 REMARK 500 ARG A 189 -0.70 -46.08 REMARK 500 ASN A 191 -61.92 -142.02 REMARK 500 SER A 192 99.62 -58.55 REMARK 500 CYS A 195 76.18 -111.57 REMARK 500 LYS A 200 -26.57 -20.92 REMARK 500 THR A 201 41.09 -91.26 REMARK 500 SER A 202 87.05 157.08 REMARK 500 THR A 203 -3.31 -58.75 REMARK 500 PRO A 205 164.67 -28.54 REMARK 500 VAL A 207 54.25 -145.35 REMARK 500 ARG A 212 118.71 -167.09 REMARK 500 GLU A 214 -74.80 -65.84 REMARK 500 LYS B 3 97.05 -163.89 REMARK 500 LYS B 19 82.95 -156.73 REMARK 500 CYS B 22 140.94 -179.57 REMARK 500 THR B 28 76.46 -164.80 REMARK 500 ASN B 30 -62.40 -2.34 REMARK 500 VAL B 48 -68.05 -91.30 REMARK 500 ALA B 49 -165.74 -123.19 REMARK 500 GLU B 50 116.80 170.85 REMARK 500 ASN B 54 -33.36 -2.99 REMARK 500 SER B 55 -29.25 158.14 REMARK 500 ASN B 57 -75.53 -31.81 REMARK 500 TYR B 62 -153.75 -125.15 REMARK 500 GLU B 64 -59.93 -8.37 REMARK 500 VAL B 66 -33.62 -154.12 REMARK 500 ARG B 74 127.47 -171.88 REMARK 500 LEU B 103 42.46 -88.87 REMARK 500 ALA B 107 -158.67 -174.25 REMARK 500 THR B 115 142.60 -174.09 REMARK 500 ALA B 122 -155.75 -88.34 REMARK 500 ALA B 133 -178.68 -58.91 REMARK 500 ALA B 137 104.34 -178.36 REMARK 500 THR B 140 87.75 -30.36 REMARK 500 ASN B 141 -172.84 56.55 REMARK 500 MET B 143 165.23 163.91 REMARK 500 ASN B 163 83.00 51.13 REMARK 500 SER B 164 48.19 31.44 REMARK 500 SER B 169 82.25 -39.10 REMARK 500 SER B 180 61.73 88.22 REMARK 500 ASP B 181 51.71 33.55 REMARK 500 SER B 188 137.81 -171.70 REMARK 500 VAL B 191 -155.60 -83.47 REMARK 500 SER B 193 -51.09 -15.60 REMARK 500 GLU B 199 -33.13 -28.43 REMARK 500 SER B 210 5.51 86.09 REMARK 500 THR B 212 93.95 -172.11 REMARK 500 LYS B 213 -158.50 -90.30 REMARK 500 ASP B 215 -169.74 -163.21 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 H 32 0.07 SIDE_CHAIN REMARK 500 TYR A 88 0.11 SIDE_CHAIN REMARK 500 TYR B 32 0.09 SIDE_CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 ARG H 196 10.13 REMARK 500 THR B 28 10.39 REMARK 500 REMARK 500 REMARK: NULL