REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 3.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 7.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000000.000 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0010 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 78.1 REMARK 3 NUMBER OF REFLECTIONS : 34656 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) : 0.217 REMARK 3 FREE R VALUE : 0.285 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.600 REMARK 3 FREE R VALUE TEST SET COUNT : 889 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.010 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 6 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.00 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.17 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 55.10 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3983 REMARK 3 BIN R VALUE (WORKING SET) : 0.3090 REMARK 3 BIN FREE R VALUE : 0.4150 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 1.90 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 77 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.047 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 9834 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) : 42.40 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.20 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.18000 REMARK 3 B22 (A**2) : 1.68000 REMARK 3 B33 (A**2) : -1.50000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 5.05000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.35 REMARK 3 ESD FROM SIGMAA (A) : 0.59 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) : 0.52 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.85 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.017 REMARK 3 BOND ANGLES (DEGREES) : 2.20 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 27.90 REMARK 3 IMPROPER ANGLES (DEGREES) : 1.84 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : GROUP REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 4.280 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 6.910 ; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 6.830 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 10.320; 2.500 REMARK 3 REMARK 3 NCS MODEL : RESTRAINTS REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : 0.30 ; 0.1 REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 GROUP 2 POSITIONAL (A) : 0.29 ; 0.1 REMARK 3 GROUP 2 B-FACTOR (A**2) : NULL ; NULL REMARK 3 GROUP 3 POSITIONAL (A) : 0.40 ; 0.3 REMARK 3 GROUP 3 B-FACTOR (A**2) : NULL ; NULL REMARK 3 GROUP 4 POSITIONAL (A) : 0.40 ; 0.3 REMARK 3 GROUP 4 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : PARHCSDX.PRO REMARK 3 PARAMETER FILE 2 : NULL REMARK 3 PARAMETER FILE 3 : NULL REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO REMARK 3 TOPOLOGY FILE 2 : NULL REMARK 3 TOPOLOGY FILE 3 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1AHW 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 : MAY-94 REMARK 200 TEMPERATURE (KELVIN) : 297 REMARK 200 PH : 5.0-5.5 REMARK 200 NUMBER OF CRYSTALS USED : 4 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : ROTATING ANODE REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : ELLIOTT GX-18 REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : NI FILTER REMARK 200 OPTICS : COLLIMATOR REMARK 200 REMARK 200 DETECTOR TYPE : AREA DETECTOR REMARK 200 DETECTOR MANUFACTURER : SIEMENS REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XENGEN REMARK 200 DATA SCALING SOFTWARE : XENGEN REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42650 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000 REMARK 200 RESOLUTION RANGE LOW (A) : 47.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 91.0 REMARK 200 DATA REDUNDANCY : 2.800 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.13500 REMARK 200 FOR THE DATA SET : 7.2000 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) : 3.19 REMARK 200 COMPLETENESS FOR SHELL (%) : 87.0 REMARK 200 DATA REDUNDANCY IN SHELL : 1.70 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.43000 REMARK 200 FOR SHELL : 0.900 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: NULL REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: TFFC, X-PLOR 3.1 REMARK 200 STARTING MODEL: TISSUE FACTOR (PDB ENTRY 1TFH) AND FAB 5G9 (PDB REMARK 200 ENTRY 1FGN) REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 64.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.70 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: TF-5G9 CRYSTAL WERE GROWN IN 1.7- REMARK 280 2.0M AMMONIUM SULFATE, 0.1M SODIUM CITRATE, PH 5.0-5.5, 0.2% REMARK 280 2-METHYL-2,4-PENTANE-DIOL (MPD), AND 2% PEG 600 AT AN REMARK 280 EQUIMOLAR 5G9:TF RATIO. THE CRYSTALS GREW EXTREMELY SLOWLY, REMARK 280 TAKING 6-9 MONTHS TO REACH A MAXIMAL SIZE OF 0.4 X 0.4 X 0.8 REMARK 280 MM3., PH 7.0 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 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 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 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 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: HEXAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, 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 SER C 1 REMARK 465 GLY C 2 REMARK 465 THR C 3 REMARK 465 VAL C 83 REMARK 465 GLU C 84 REMARK 465 SER C 85 REMARK 465 THR C 86 REMARK 465 GLY C 87 REMARK 465 SER C 88 REMARK 465 ALA C 89 REMARK 465 GLY C 90 REMARK 465 GLN C 212 REMARK 465 GLU C 213 REMARK 465 LYS C 214 REMARK 465 GLY C 215 REMARK 465 GLU C 216 REMARK 465 PHE C 217 REMARK 465 ARG C 218 REMARK 465 GLU C 219 REMARK 465 SER F 1 REMARK 465 GLY F 2 REMARK 465 THR F 3 REMARK 465 VAL F 83 REMARK 465 GLU F 84 REMARK 465 SER F 85 REMARK 465 THR F 86 REMARK 465 GLY F 87 REMARK 465 SER F 88 REMARK 465 ALA F 89 REMARK 465 GLY F 90 REMARK 465 GLN F 212 REMARK 465 GLU F 213 REMARK 465 LYS F 214 REMARK 465 GLY F 215 REMARK 465 GLU F 216 REMARK 465 PHE F 217 REMARK 465 ARG F 218 REMARK 465 GLU F 219 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 CYS A 134 CA - CB - SG ANGL. DEV. = 7.9 DEGREES REMARK 500 CYS D 134 CA - CB - SG ANGL. DEV. = 7.6 DEGREES REMARK 500 LEU E 81 CA - CB - CG ANGL. DEV. = 16.9 DEGREES REMARK 500 LYS E 213 N - CA - C ANGL. DEV. = -16.8 DEGREES REMARK 500 CYS F 57 CA - CB - SG ANGL. DEV. = 6.8 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 MET A 11 127.44 -170.57 REMARK 500 SER A 26 31.73 -79.57 REMARK 500 GLN A 27 144.40 165.40 REMARK 500 ASP A 28 116.05 -38.80 REMARK 500 TYR A 32 61.98 -103.53 REMARK 500 LEU A 47 -70.98 -64.54 REMARK 500 ALA A 51 -39.56 62.90 REMARK 500 ALA A 55 -157.64 -112.27 REMARK 500 ASP A 56 88.00 -32.67 REMARK 500 SER A 67 117.83 -169.05 REMARK 500 ASP A 81 45.94 -78.94 REMARK 500 HIS A 91 42.85 -141.49 REMARK 500 ASP A 110 154.00 -47.12 REMARK 500 PRO A 120 107.44 -45.09 REMARK 500 TYR A 140 129.76 -173.28 REMARK 500 ILE A 144 129.30 -170.11 REMARK 500 ASP A 151 79.09 67.30 REMARK 500 SER A 153 -37.16 -22.08 REMARK 500 GLU A 154 90.62 -53.93 REMARK 500 MET A 175 -160.50 -124.93 REMARK 500 SER A 176 110.87 -178.40 REMARK 500 ASP A 184 -73.48 -49.91 REMARK 500 LYS A 199 42.61 -79.79 REMARK 500 PRO A 204 145.40 -33.04 REMARK 500 ASN A 212 70.71 -116.60 REMARK 500 GLN B 3 145.24 -178.90 REMARK 500 SER B 7 -9.57 -43.28 REMARK 500 GLU B 10 110.53 -177.35 REMARK 500 GLN B 39 110.88 -160.50 REMARK 500 PRO B 41 -98.14 -11.92 REMARK 500 GLU B 42 32.45 -75.31 REMARK 500 GLU B 54 -73.92 -63.60 REMARK 500 ASN B 55 72.11 -111.44 REMARK 500 SER B 69 104.50 -173.75 REMARK 500 LEU B 81 107.70 -161.44 REMARK 500 ALA B 92 -173.75 -171.02 REMARK 500 SER B 101 -50.44 96.86 REMARK 500 PRO B 122 152.81 -46.72 REMARK 500 SER B 132 145.98 164.10 REMARK 500 THR B 136 -58.67 -147.65 REMARK 500 PHE B 150 139.82 173.92 REMARK 500 LEU B 163 90.44 -62.99 REMARK 500 GLN B 175 84.19 -159.99 REMARK 500 SER B 176 66.85 77.34 REMARK 500 ASP B 177 -18.45 57.72 REMARK 500 SER B 190 0.62 -66.79 REMARK 500 ASN C 5 114.63 160.79 REMARK 500 ASN C 11 44.98 76.52 REMARK 500 ASN C 18 52.79 38.08 REMARK 500 THR C 40 -133.22 -80.21 REMARK 500 SER C 42 81.79 52.57 REMARK 500 ASP C 44 108.04 -54.39 REMARK 500 LYS C 48 -44.22 -138.26 REMARK 500 CYS C 49 77.03 -103.85 REMARK 500 TYR C 51 44.00 22.87 REMARK 500 THR C 55 34.12 -97.40 REMARK 500 ASP C 66 85.40 -162.41 REMARK 500 SER C 115 174.37 173.41 REMARK 500 PHE C 116 121.54 -172.46 REMARK 500 ASN C 124 101.00 -52.92 REMARK 500 GLU C 130 144.64 -23.54 REMARK 500 ASN C 137 -148.31 53.81 REMARK 500 ASN C 138 37.03 -96.35 REMARK 500 ASP C 150 42.99 -91.46 REMARK 500 SER C 160 -47.90 -24.73 REMARK 500 THR C 172 -147.80 -138.65 REMARK 500 SER C 188 139.35 -174.66 REMARK 500 VAL C 198 -81.89 -138.85 REMARK 500 MET C 210 -136.62 -97.04 REMARK 500 MET D 11 115.80 -160.34 REMARK 500 LEU D 15 153.31 -46.78 REMARK 500 SER D 26 5.81 -67.20 REMARK 500 ALA D 51 -56.60 64.59 REMARK 500 ALA D 55 -157.31 -114.40 REMARK 500 ASP D 56 63.28 -26.56 REMARK 500 SER D 67 114.02 -168.82 REMARK 500 ASP D 81 49.99 -78.74 REMARK 500 ALA D 84 -166.81 -167.59 REMARK 500 HIS D 91 47.83 -148.69 REMARK 500 GLU D 93 144.32 -175.20 REMARK 500 ASP D 110 161.63 -42.57 REMARK 500 ASP D 151 88.88 69.42 REMARK 500 SER D 153 -37.59 -18.13 REMARK 500 GLU D 154 85.32 -55.41 REMARK 500 GLN D 166 121.11 -36.76 REMARK 500 SER D 171 16.50 59.82 REMARK 500 THR D 180 77.22 -115.24 REMARK 500 ASP D 184 -77.96 -47.09 REMARK 500 ASN D 190 -38.45 -130.34 REMARK 500 LYS D 199 22.53 -75.82 REMARK 500 ASN D 212 65.60 -107.18 REMARK 500 GLN E 3 144.74 -177.93 REMARK 500 GLU E 10 71.52 171.56 REMARK 500 PRO E 41 -86.56 -39.01 REMARK 500 GLU E 54 -78.44 -52.12 REMARK 500 ASN E 55 64.67 -105.54 REMARK 500 SER E 84 153.08 175.81 REMARK 500 SER E 101 -52.06 103.75 REMARK 500 GLN E 109 172.33 -53.62 REMARK 500 PRO E 122 151.96 -47.50 REMARK 500 THR E 136 -49.42 -156.13 REMARK 500 SER E 165 -76.14 -37.42 REMARK 500 PRO E 171 150.61 -42.42 REMARK 500 GLN E 175 81.63 -160.30 REMARK 500 SER E 176 80.76 65.89 REMARK 500 ASP E 177 -27.34 58.50 REMARK 500 THR E 180 118.24 -165.09 REMARK 500 SER E 190 3.76 -69.31 REMARK 500 SER E 207 38.40 38.08 REMARK 500 ASN F 5 101.12 -174.58 REMARK 500 ALA F 8 -163.27 -78.12 REMARK 500 ASN F 11 58.01 71.48 REMARK 500 PHE F 19 -9.72 67.16 REMARK 500 THR F 40 -139.46 -76.46 REMARK 500 SER F 42 87.47 41.40 REMARK 500 ASP F 44 91.62 -48.22 REMARK 500 LYS F 48 -70.27 -126.08 REMARK 500 TYR F 51 43.42 39.53 REMARK 500 ASP F 66 89.65 -165.68 REMARK 500 PHE F 116 102.60 -175.78 REMARK 500 VAL F 119 50.04 -109.62 REMARK 500 ASN F 137 -153.19 62.08 REMARK 500 LEU F 151 95.46 -163.52 REMARK 500 SER F 160 -55.42 -18.71 REMARK 500 SER F 161 -45.99 -28.94 REMARK 500 THR F 172 -150.84 -154.17 REMARK 500 LYS F 181 119.04 -32.47 REMARK 500 SER F 188 108.42 -170.74 REMARK 500 VAL F 198 -75.08 -133.71 REMARK 500 MET F 210 -122.83 -92.87 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 A 12 0.06 SIDE_CHAIN REMARK 500 TYR E 94 0.07 SIDE_CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: BSC REMARK 800 EVIDENCE_CODE: UNKNOWN REMARK 800 SITE_DESCRIPTION: KEY TF EPITOPE RESIDUES FOR 5G9. REMARK 800 SITE_IDENTIFIER: BSF REMARK 800 EVIDENCE_CODE: UNKNOWN REMARK 800 SITE_DESCRIPTION: KEY TF EPITOPE RESIDUES FOR 5G9.