REMARK 2 REMARK 2 RESOLUTION. 2.22 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.11.2 REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER, REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN, REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.22 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.35 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 85.8 REMARK 3 NUMBER OF REFLECTIONS : 78809 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 + TEST SET) : 0.198 REMARK 3 R VALUE (WORKING SET) : 0.196 REMARK 3 FREE R VALUE : 0.236 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070 REMARK 3 FREE R VALUE TEST SET COUNT : 3996 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 : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.22 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.28 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.79 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 4634 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2261 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4414 REMARK 3 BIN R VALUE (WORKING SET) : 0.2238 REMARK 3 BIN FREE R VALUE : 0.2730 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.75 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 220 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 : 13189 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 301 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 41.25 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.42 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 6.96460 REMARK 3 B22 (A**2) : 5.19300 REMARK 3 B33 (A**2) : -12.15770 REMARK 3 B12 (A**2) : -0.97090 REMARK 3 B13 (A**2) : -0.72980 REMARK 3 B23 (A**2) : -0.78570 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.28 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.34 REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL REMARK 3 REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797 REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.925 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.906 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 13594 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 18551 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 4461 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : 282 ; 2.000 ; HARMONIC REMARK 3 GENERAL PLANES : 2006 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 13594 ; 20.000 ; HARMONIC REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : 1804 ; 5.000 ; SEMIHARMONIC REMARK 3 SUM OF OCCUPANCIES : 7 ; 1.000 ; HARMONIC REMARK 3 UTILITY DISTANCES : 7 ; 1.000 ; HARMONIC REMARK 3 UTILITY ANGLES : 14 ; 1.000 ; HARMONIC REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL REMARK 3 IDEAL-DIST CONTACT TERM : 14455 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.010 REMARK 3 BOND ANGLES (DEGREES) : 1.18 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.43 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 18.19 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 4JZO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-APR-13. REMARK 100 THE RCSB ID CODE IS RCSB078706. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 28-FEB-12 REMARK 200 TEMPERATURE (KELVIN) : 110 REMARK 200 PH : 8.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SLS REMARK 200 BEAMLINE : X06SA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000 REMARK 200 MONOCHROMATOR : LN2 COOLED FIXED-EXIT SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 78908 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.220 REMARK 200 RESOLUTION RANGE LOW (A) : 41.350 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 85.9 REMARK 200 DATA REDUNDANCY : 1.600 REMARK 200 R MERGE (I) : 0.08200 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.22 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34 REMARK 200 COMPLETENESS FOR SHELL (%) : 71.0 REMARK 200 DATA REDUNDANCY IN SHELL : 1.30 REMARK 200 R MERGE FOR SHELL (I) : 0.18400 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: PHASER REMARK 200 STARTING MODEL: 2XZA AND 3QOT REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 46.25 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 23% PEG 3350 250MM SODIUM REMARK 280 THIOCYANATE, PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE REMARK 280 293K 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, 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: THE ASYMETRIC UNIT CONTAINS FOUR FAB MOLECULES EACH REMARK 300 REPRESENTING A HETERODIMER OF HEAVY AND LIGHT CHAIN. EACH FAB REMARK 300 MOLECULE BINDS ONE SYNTHETIC PEPTIDE. 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4850 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19570 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: J, 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4670 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19210 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, C, 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 350 REMARK 350 BIOMOLECULE: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4700 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19470 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, D, 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: 4 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4990 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19120 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, 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 SER A 134 REMARK 465 LYS A 135 REMARK 465 SER A 136 REMARK 465 THR A 137 REMARK 465 LYS A 220 REMARK 465 SER A 221 REMARK 465 CYS A 222 REMARK 465 ASP A 223 REMARK 465 LYS A 224 REMARK 465 LEU A 225 REMARK 465 GLU A 226 REMARK 465 ASP A 227 REMARK 465 ASP A 228 REMARK 465 ASP A 229 REMARK 465 ASP A 230 REMARK 465 LYS A 231 REMARK 465 ALA A 232 REMARK 465 GLY A 233 REMARK 465 TRP A 234 REMARK 465 SER A 235 REMARK 465 HIS A 236 REMARK 465 PRO A 237 REMARK 465 GLN A 238 REMARK 465 PHE A 239 REMARK 465 GLU A 240 REMARK 465 LYS A 241 REMARK 465 GLY A 242 REMARK 465 GLY A 243 REMARK 465 GLY A 244 REMARK 465 SER A 245 REMARK 465 GLY A 246 REMARK 465 GLY A 247 REMARK 465 GLY A 248 REMARK 465 SER A 249 REMARK 465 GLY A 250 REMARK 465 GLY A 251 REMARK 465 GLY A 252 REMARK 465 SER A 253 REMARK 465 TRP A 254 REMARK 465 SER A 255 REMARK 465 HIS A 256 REMARK 465 PRO A 257 REMARK 465 GLN A 258 REMARK 465 PHE A 259 REMARK 465 GLU A 260 REMARK 465 LYS A 261 REMARK 465 ARG B -1 REMARK 465 SER B 0 REMARK 465 GLU B 212 REMARK 465 CYS B 213 REMARK 465 GLN C 1 REMARK 465 SER C 134 REMARK 465 LYS C 135 REMARK 465 SER C 136 REMARK 465 THR C 137 REMARK 465 LYS C 220 REMARK 465 SER C 221 REMARK 465 CYS C 222 REMARK 465 ASP C 223 REMARK 465 LYS C 224 REMARK 465 LEU C 225 REMARK 465 GLU C 226 REMARK 465 ASP C 227 REMARK 465 ASP C 228 REMARK 465 ASP C 229 REMARK 465 ASP C 230 REMARK 465 LYS C 231 REMARK 465 ALA C 232 REMARK 465 GLY C 233 REMARK 465 TRP C 234 REMARK 465 SER C 235 REMARK 465 HIS C 236 REMARK 465 PRO C 237 REMARK 465 GLN C 238 REMARK 465 PHE C 239 REMARK 465 GLU C 240 REMARK 465 LYS C 241 REMARK 465 GLY C 242 REMARK 465 GLY C 243 REMARK 465 GLY C 244 REMARK 465 SER C 245 REMARK 465 GLY C 246 REMARK 465 GLY C 247 REMARK 465 GLY C 248 REMARK 465 SER C 249 REMARK 465 GLY C 250 REMARK 465 GLY C 251 REMARK 465 GLY C 252 REMARK 465 SER C 253 REMARK 465 TRP C 254 REMARK 465 SER C 255 REMARK 465 HIS C 256 REMARK 465 PRO C 257 REMARK 465 GLN C 258 REMARK 465 PHE C 259 REMARK 465 GLU C 260 REMARK 465 LYS C 261 REMARK 465 SER D 134 REMARK 465 LYS D 135 REMARK 465 SER D 136 REMARK 465 THR D 137 REMARK 465 SER D 138 REMARK 465 LYS D 220 REMARK 465 SER D 221 REMARK 465 CYS D 222 REMARK 465 ASP D 223 REMARK 465 LYS D 224 REMARK 465 LEU D 225 REMARK 465 GLU D 226 REMARK 465 ASP D 227 REMARK 465 ASP D 228 REMARK 465 ASP D 229 REMARK 465 ASP D 230 REMARK 465 LYS D 231 REMARK 465 ALA D 232 REMARK 465 GLY D 233 REMARK 465 TRP D 234 REMARK 465 SER D 235 REMARK 465 HIS D 236 REMARK 465 PRO D 237 REMARK 465 GLN D 238 REMARK 465 PHE D 239 REMARK 465 GLU D 240 REMARK 465 LYS D 241 REMARK 465 GLY D 242 REMARK 465 GLY D 243 REMARK 465 GLY D 244 REMARK 465 SER D 245 REMARK 465 GLY D 246 REMARK 465 GLY D 247 REMARK 465 GLY D 248 REMARK 465 SER D 249 REMARK 465 GLY D 250 REMARK 465 GLY D 251 REMARK 465 GLY D 252 REMARK 465 SER D 253 REMARK 465 TRP D 254 REMARK 465 SER D 255 REMARK 465 HIS D 256 REMARK 465 PRO D 257 REMARK 465 GLN D 258 REMARK 465 PHE D 259 REMARK 465 GLU D 260 REMARK 465 LYS D 261 REMARK 465 ARG E -1 REMARK 465 SER E 0 REMARK 465 GLU E 212 REMARK 465 CYS E 213 REMARK 465 ARG F -1 REMARK 465 SER F 0 REMARK 465 SER F 1 REMARK 465 GLU F 212 REMARK 465 CYS F 213 REMARK 465 GLN G 1 REMARK 465 THR G 76 REMARK 465 LYS G 220 REMARK 465 SER G 221 REMARK 465 CYS G 222 REMARK 465 ASP G 223 REMARK 465 LYS G 224 REMARK 465 LEU G 225 REMARK 465 GLU G 226 REMARK 465 ASP G 227 REMARK 465 ASP G 228 REMARK 465 ASP G 229 REMARK 465 ASP G 230 REMARK 465 LYS G 231 REMARK 465 ALA G 232 REMARK 465 GLY G 233 REMARK 465 TRP G 234 REMARK 465 SER G 235 REMARK 465 HIS G 236 REMARK 465 PRO G 237 REMARK 465 GLN G 238 REMARK 465 PHE G 239 REMARK 465 GLU G 240 REMARK 465 LYS G 241 REMARK 465 GLY G 242 REMARK 465 GLY G 243 REMARK 465 GLY G 244 REMARK 465 SER G 245 REMARK 465 GLY G 246 REMARK 465 GLY G 247 REMARK 465 GLY G 248 REMARK 465 SER G 249 REMARK 465 GLY G 250 REMARK 465 GLY G 251 REMARK 465 GLY G 252 REMARK 465 SER G 253 REMARK 465 TRP G 254 REMARK 465 SER G 255 REMARK 465 HIS G 256 REMARK 465 PRO G 257 REMARK 465 GLN G 258 REMARK 465 PHE G 259 REMARK 465 GLU G 260 REMARK 465 LYS G 261 REMARK 465 ARG H -1 REMARK 465 SER H 0 REMARK 465 SER H 1 REMARK 465 GLU H 212 REMARK 465 CYS H 213 REMARK 465 ASN I 434 REMARK 465 THR I 435 REMARK 465 ASN J 434 REMARK 465 THR J 435 REMARK 465 ASN K 434 REMARK 465 THR K 435 REMARK 465 ASN L 434 REMARK 465 THR L 435 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 ASP B 50 -43.23 67.22 REMARK 500 LYS B 168 -62.83 -101.61 REMARK 500 LYS B 189 -64.63 -100.34 REMARK 500 ARG C 56 42.20 36.91 REMARK 500 ASP C 150 67.54 60.18 REMARK 500 ASP E 50 -42.31 64.31 REMARK 500 LYS E 189 -66.57 -99.32 REMARK 500 ASP F 50 -44.32 70.61 REMARK 500 ALA F 83 177.40 179.28 REMARK 500 LYS F 189 -64.07 -100.78 REMARK 500 LEU G 29 -36.41 67.11 REMARK 500 SER G 102 4.57 58.98 REMARK 500 ASP H 50 -48.27 71.35 REMARK 500 ALA H 83 178.53 176.03 REMARK 500 LYS H 189 -64.63 -100.80 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CHIRAL CENTERS REMARK 500 REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16) REMARK 500 REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS REMARK 500 ASP B 25 24.9 L L OUTSIDE RANGE REMARK 500 ASP B 169 23.2 L L OUTSIDE RANGE REMARK 500 ILE E 57 24.8 L L OUTSIDE RANGE REMARK 500 THR G 28 23.2 L L OUTSIDE RANGE REMARK 500 HIS L 445 23.9 L L OUTSIDE RANGE REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN I OF ENVELOPE REMARK 800 GLYCOPROTEIN E2 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN J OF ENVELOPE REMARK 800 GLYCOPROTEIN E2 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN K OF ENVELOPE REMARK 800 GLYCOPROTEIN E2 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN L OF ENVELOPE REMARK 800 GLYCOPROTEIN E2 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4JZN RELATED DB: PDB REMARK 900 THREE DIMENSIONAL STRUCTURE OF BROADLY NEUTRALIZING HUMAN REMARK 900 ANTI - HEPATITIS C VIRUS (HCV) GLYCOPROTEIN E2 FAB FRAGMENT REMARK 900 HC84-1