REMARK 2 REMARK 2 RESOLUTION. 3.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.8.0 REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER, REMARK 3 : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK, REMARK 3 : MATTHEWS,TEN EYCK,TRONRUD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 9210 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) : 0.243 REMARK 3 R VALUE (WORKING SET) : 0.235 REMARK 3 FREE R VALUE : 0.308 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.170 REMARK 3 FREE R VALUE TEST SET COUNT : 937 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 : 5 REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.91 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2578 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2422 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2316 REMARK 3 BIN R VALUE (WORKING SET) : 0.2344 REMARK 3 BIN FREE R VALUE : 0.3103 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.16 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 262 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 : 3211 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 27 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 45.69 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 79.94 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 33.17150 REMARK 3 B22 (A**2) : 2.97070 REMARK 3 B33 (A**2) : -36.14220 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 4.32750 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.75 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) : NULL 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 : 0.838 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.724 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 3321 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 4521 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 1095 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : 64 ; 2.000 ; HARMONIC REMARK 3 GENERAL PLANES : 482 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 3292 ; 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 : 447 ; 5.000 ; NULL REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL REMARK 3 IDEAL-DIST CONTACT TERM : 3945 ; 4.000 ; NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.010 REMARK 3 BOND ANGLES (DEGREES) : 1.22 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.57 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 25.21 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 3P0G COMPLIES WITH FORMAT V. 3.20, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-OCT-10. REMARK 100 THE RCSB ID CODE IS RCSB061801. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 10-MAR-10; 25-MAR-10 REMARK 200 TEMPERATURE (KELVIN) : 78; 78 REMARK 200 PH : 8.0 REMARK 200 NUMBER OF CRYSTALS USED : 23 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y; Y REMARK 200 RADIATION SOURCE : APS; APS REMARK 200 BEAMLINE : 23-ID-B; 23-ID-B REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0332; 1.0332 REMARK 200 MONOCHROMATOR : DOUBLE-CRYSTAL; DOUBLE-CRYSTAL REMARK 200 OPTICS : MIRRORS; MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : CCD; CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD; MARMOSAIC REMARK 200 300 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9308 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.500 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 94.8 REMARK 200 DATA REDUNDANCY : 3.500 REMARK 200 R MERGE (I) : 0.20000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 4.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.56 REMARK 200 COMPLETENESS FOR SHELL (%) : 93.7 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: SINGLE WAVELENGTH; SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: PDB ENTRIES 2RH1 AND 3DWT REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 53.97 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 36-44% PEG 400, 100 MM TRIS PH 8.0, 4% REMARK 280 DMSO, 1% 1,2,3-HEPTANETRIOL, TWIN-SYRINGE MIXING METHOD, REMARK 280 TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 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 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 118.34300 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 22.83000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 118.34300 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 22.83000 REMARK 290 SMTRY3 4 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2130 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20570 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 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 400 REMARK 400 COMPOUND REMARK 400 THE T4 LYSOZYME IS NOT VISIBLE IN THE STRUCTURE 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 A -7 REMARK 465 TYR A -6 REMARK 465 LYS A -5 REMARK 465 ASP A -4 REMARK 465 ASP A -3 REMARK 465 ASP A -2 REMARK 465 ASP A -1 REMARK 465 ALA A 0 REMARK 465 MET A 1 REMARK 465 GLY A 2 REMARK 465 GLN A 3 REMARK 465 PRO A 4 REMARK 465 GLY A 5 REMARK 465 ASN A 6 REMARK 465 GLY A 7 REMARK 465 SER A 8 REMARK 465 ALA A 9 REMARK 465 PHE A 10 REMARK 465 LEU A 11 REMARK 465 LEU A 12 REMARK 465 ALA A 13 REMARK 465 PRO A 14 REMARK 465 ASN A 15 REMARK 465 ARG A 16 REMARK 465 SER A 17 REMARK 465 HIS A 18 REMARK 465 ALA A 19 REMARK 465 PRO A 20 REMARK 465 ASP A 21 REMARK 465 HIS A 22 REMARK 465 ARG A 227A REMARK 465 GLN A 227B REMARK 465 LEU A 227C REMARK 465 ASN A 227D REMARK 465 ILE A 227E REMARK 465 PHE A 227F REMARK 465 GLU A 227G REMARK 465 MET A 227H REMARK 465 LEU A 227I REMARK 465 ARG A 227J REMARK 465 ILE A 227K REMARK 465 ASP A 227L REMARK 465 GLU A 227M REMARK 465 GLY A 227N REMARK 465 LEU A 227O REMARK 465 ARG A 227P REMARK 465 LEU A 227Q REMARK 465 LYS A 227R REMARK 465 ILE A 227S REMARK 465 TYR A 227T REMARK 465 LYS A 227U REMARK 465 ASP A 227V REMARK 465 THR A 227W REMARK 465 GLU A 227X REMARK 465 GLY A 227Y REMARK 465 TYR A 227Z REMARK 465 TYR A 228A REMARK 465 THR A 228B REMARK 465 ILE A 228C REMARK 465 GLY A 228D REMARK 465 ILE A 228E REMARK 465 GLY A 228F REMARK 465 HIS A 228G REMARK 465 LEU A 228H REMARK 465 LEU A 228I REMARK 465 THR A 228J REMARK 465 LYS A 228K REMARK 465 SER A 228L REMARK 465 PRO A 228M REMARK 465 SER A 228N REMARK 465 LEU A 228O REMARK 465 ASN A 228P REMARK 465 ALA A 228Q REMARK 465 ALA A 228R REMARK 465 LYS A 228S REMARK 465 SER A 228T REMARK 465 GLU A 228U REMARK 465 LEU A 228V REMARK 465 ASP A 228W REMARK 465 LYS A 228X REMARK 465 ALA A 228Y REMARK 465 ILE A 228Z REMARK 465 GLY A 229A REMARK 465 ARG A 229B REMARK 465 ASN A 229C REMARK 465 THR A 229D REMARK 465 ASN A 229E REMARK 465 GLY A 229F REMARK 465 VAL A 229G REMARK 465 ILE A 229H REMARK 465 THR A 229I REMARK 465 LYS A 229J REMARK 465 ASP A 229K REMARK 465 GLU A 229L REMARK 465 ALA A 229M REMARK 465 GLU A 229N REMARK 465 LYS A 229O REMARK 465 LEU A 229P REMARK 465 PHE A 229Q REMARK 465 ASN A 229R REMARK 465 GLN A 229S REMARK 465 ASP A 229T REMARK 465 VAL A 229U REMARK 465 ASP A 229V REMARK 465 ALA A 229W REMARK 465 ALA A 229X REMARK 465 VAL A 229Y REMARK 465 ARG A 229Z REMARK 465 GLY A 230A REMARK 465 ILE A 230B REMARK 465 LEU A 230C REMARK 465 ARG A 230D REMARK 465 ASN A 230E REMARK 465 ALA A 230F REMARK 465 LYS A 230G REMARK 465 LEU A 230H REMARK 465 LYS A 230I REMARK 465 PRO A 230J REMARK 465 VAL A 230K REMARK 465 TYR A 230L REMARK 465 ASP A 230M REMARK 465 SER A 230N REMARK 465 LEU A 230O REMARK 465 ASP A 230P REMARK 465 ALA A 230Q REMARK 465 VAL A 230R REMARK 465 ARG A 230S REMARK 465 ARG A 230T REMARK 465 ALA A 230U REMARK 465 ALA A 230V REMARK 465 LEU A 230W REMARK 465 ILE A 230X REMARK 465 ASN A 230Y REMARK 465 MET A 230Z REMARK 465 VAL A 231A REMARK 465 PHE A 231B REMARK 465 GLN A 231C REMARK 465 MET A 231D REMARK 465 GLY A 231E REMARK 465 GLU A 231F REMARK 465 THR A 231G REMARK 465 GLY A 231H REMARK 465 VAL A 231I REMARK 465 ALA A 231J REMARK 465 GLY A 231K REMARK 465 PHE A 231L REMARK 465 THR A 231M REMARK 465 ASN A 231N REMARK 465 SER A 231O REMARK 465 LEU A 231P REMARK 465 ARG A 231Q REMARK 465 MET A 231R REMARK 465 LEU A 231S REMARK 465 GLN A 231T REMARK 465 GLN A 231U REMARK 465 LYS A 231V REMARK 465 ARG A 231W REMARK 465 TRP A 231X REMARK 465 ASP A 231Y REMARK 465 GLU A 231Z REMARK 465 ALA A 232A REMARK 465 ALA A 232B REMARK 465 VAL A 232C REMARK 465 ASN A 232D REMARK 465 LEU A 232E REMARK 465 ALA A 232F REMARK 465 LYS A 232G REMARK 465 SER A 232H REMARK 465 ARG A 232I REMARK 465 TRP A 232J REMARK 465 TYR A 232K REMARK 465 ASN A 232L REMARK 465 GLN A 232M REMARK 465 THR A 232N REMARK 465 PRO A 232O REMARK 465 ASN A 232P REMARK 465 ARG A 232Q REMARK 465 ALA A 232R REMARK 465 LYS A 232S REMARK 465 ARG A 232T REMARK 465 VAL A 232U REMARK 465 ILE A 232V REMARK 465 THR A 232W REMARK 465 THR A 232X REMARK 465 PHE A 232Y REMARK 465 ARG A 232Z REMARK 465 THR A 233A REMARK 465 GLY A 233B REMARK 465 THR A 233C REMARK 465 TRP A 233D REMARK 465 ASP A 233E REMARK 465 ALA A 233F REMARK 465 TYR A 233G REMARK 465 LYS A 233H REMARK 465 PHE A 233I REMARK 465 CYS A 233J REMARK 465 SER A 345 REMARK 465 SER A 346 REMARK 465 LEU A 347 REMARK 465 LYS A 348 REMARK 465 ALA A 349 REMARK 465 TYR A 350 REMARK 465 GLY A 351 REMARK 465 ASN A 352 REMARK 465 GLY A 353 REMARK 465 TYR A 354 REMARK 465 SER A 355 REMARK 465 SER A 356 REMARK 465 ASN A 357 REMARK 465 GLY A 358 REMARK 465 ASN A 359 REMARK 465 THR A 360 REMARK 465 GLY A 361 REMARK 465 GLU A 362 REMARK 465 GLN A 363 REMARK 465 SER A 364 REMARK 465 GLY A 365 REMARK 465 GLN B 1 REMARK 465 HIS B 123 REMARK 465 HIS B 124 REMARK 465 HIS B 125 REMARK 465 HIS B 126 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 THR A 25 -159.51 -115.79 REMARK 500 GLU A 30 6.02 -67.08 REMARK 500 ARG A 63 -7.84 -56.04 REMARK 500 ALA A 92 -76.14 -48.29 REMARK 500 THR A 136 -70.40 -66.55 REMARK 500 LEU A 145 93.35 -68.97 REMARK 500 CYS A 191 50.50 -140.23 REMARK 500 PHE A 208 -56.23 -131.31 REMARK 500 ILE A 298 -93.14 -73.64 REMARK 500 LEU A 302 -4.24 -144.88 REMARK 500 PRO B 41 97.00 -42.10 REMARK 500 LYS B 43 -144.82 -118.72 REMARK 500 SER B 56 141.30 -173.53 REMARK 500 ASN B 58 79.03 -169.01 REMARK 500 ASN B 61 -29.11 -34.52 REMARK 500 ARG B 66 -74.28 -85.74 REMARK 500 ASN B 76 70.07 67.77 REMARK 500 LEU B 85 98.83 -46.89 REMARK 500 PRO B 87 5.32 -68.67 REMARK 500 ALA B 102 108.36 -33.08 REMARK 500 VAL B 103 -2.42 -58.02 REMARK 500 SER B 120 51.23 -118.82 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 VAL A 24 24.1 L L OUTSIDE RANGE REMARK 500 ILE A 121 24.8 L L OUTSIDE RANGE REMARK 500 CYS A 191 25.0 L L OUTSIDE RANGE REMARK 500 PHE A 208 24.9 L L OUTSIDE RANGE REMARK 500 PHE A 217 23.9 L L OUTSIDE RANGE REMARK 500 TRP A 286 23.6 L L OUTSIDE RANGE REMARK 500 ARG B 38 23.7 L L OUTSIDE RANGE REMARK 500 ASN B 61 24.1 L L OUTSIDE RANGE REMARK 500 VAL B 103 23.6 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 RESIDUE P0G A 366 REMARK 999 REMARK 999 SEQUENCE REMARK 999 SEQUENCE CONFLICT AT THESE POSITION IN UNP ENTRY P07550