REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH T.SIMON,K.RAJEWSKY REMARK 1 TITL A FUNCTIONAL ANTIBODY MUTANT WITH AN INSERTION IN REMARK 1 TITL 2 THE FRAMEWORK REGION 3 LOOP OF THE VH DOMAIN: REMARK 1 TITL 3 IMPLICATIONS FOR ANTIBODY ENGINEERING REMARK 1 REF PROTEIN ENG. V. 5 229 1992 REMARK 1 REFN ISSN 0269-2139 REMARK 2 REMARK 2 RESOLUTION. 1.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PROLSQ REMARK 3 AUTHORS : KONNERT,HENDRICKSON REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 59954 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 + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.296 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 REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA. REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.2960 REMARK 3 FREE R VALUE (NO CUTOFF) : NULL REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 5236 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 88 REMARK 3 SOLVENT ATOMS : 478 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 14.90 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.80 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 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA REMARK 3 BOND LENGTH (A) : 0.012 ; 0.020 REMARK 3 ANGLE DISTANCE (A) : 0.040 ; 0.030 REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL REMARK 3 REMARK 3 PLANE RESTRAINT (A) : 0.010 ; 0.020 REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.148 ; 0.150 REMARK 3 REMARK 3 NON-BONDED CONTACT RESTRAINTS. REMARK 3 SINGLE TORSION (A) : NULL ; NULL REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL REMARK 3 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS. REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL REMARK 3 PLANAR (DEGREES) : 1.800 ; 3.000 REMARK 3 STAGGERED (DEGREES) : 22.500; 15.000 REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 1.400 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.100 ; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 1.900 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.300 ; 3.000 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE HAS THREE MOLECULES REMARK 3 PER EQUIVALENT POSITION ARRANGED AS A TRANSLATION ALONG THE Z- REMARK 3 AXIS SUCH THAT OVERALL THE DIFFRACTION DATA SHOWS WEAK REMARK 3 INTENSITIES FOR HKL, L=2N AND THIS TRANSLATIONAL NON- REMARK 3 CRYSTALLOGRAPHIC SYMMETRY IS ON CLEARLY BROKEN BY THE REMARK 3 DIFFERENT CONFORMATION OF THE TAIL O HAPTEN LIGAND ADOPTED IN REMARK 3 EACH OF THE THREE INDEPENDENTLY DETERMINED MOLECULES. THERE REMARK 3 ARE ALSO TWO CONFORMATIONS FOUND FOR THE HAPTEN BOUND TO REMARK 3 CHAINS L AND H. REMARK 4 REMARK 4 1A6V 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 : AUG-95 REMARK 200 TEMPERATURE (KELVIN) : 269 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SRS REMARK 200 BEAMLINE : PX9.6 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.87 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : AGROVATA, ROTAVATA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 367775 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.740 REMARK 200 RESOLUTION RANGE LOW (A) : 9.200 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 94.8 REMARK 200 DATA REDUNDANCY : 5.900 REMARK 200 R MERGE (I) : 0.05900 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) : 1.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.88 REMARK 200 COMPLETENESS FOR SHELL (%) : 95.8 REMARK 200 DATA REDUNDANCY IN SHELL : 3.80 REMARK 200 R MERGE FOR SHELL (I) : 0.36100 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: MIR REMARK 200 SOFTWARE USED: MLPHARE REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 33.20 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS WERE GROWN USING AMMONIUM REMARK 280 SULPHATE AS PRECIPITANT REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 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 35.88000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 55.75550 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.09500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 55.75550 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.88000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.09500 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 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: 3250 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 9660 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 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: 2460 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 10140 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, I 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2440 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 9960 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: N, J 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 H 419 REMARK 465 SER H 420 REMARK 465 GLU M 110 REMARK 465 SER I 420 REMARK 465 GLU N 110 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 GLN L 1 CB CG CD OE1 NE2 REMARK 470 ARG L 23 CG CD NE CZ NH1 NH2 REMARK 470 SER L 24 OG REMARK 470 LYS L 105 CG CD CE NZ REMARK 470 GLU L 110 CB CG CD OE1 OE2 REMARK 470 GLN N 1 CB CG CD OE1 NE2 REMARK 470 PRO N 58 CB CG CD REMARK 470 ASN N 96 CG OD1 ND2 REMARK 470 LYS J 313 CG CD CE NZ REMARK 470 SER J 404 OG REMARK 470 ASP J 408 CG OD1 OD2 REMARK 470 SER J 420 CB OG 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 C3 NPC H 430 C3 NPC H 431 0.56 REMARK 500 N3 NPC H 430 N3 NPC H 431 0.58 REMARK 500 O3A NPC H 430 O3A NPC H 431 0.60 REMARK 500 O3B NPC H 430 O3B NPC H 431 0.60 REMARK 500 C4 NPC H 430 C4 NPC H 431 0.62 REMARK 500 O4 NPC H 430 O4 NPC H 431 0.69 REMARK 500 N3 NPC H 430 O3B NPC H 431 0.74 REMARK 500 C4 NPC H 430 O4 NPC H 431 0.82 REMARK 500 C3 NPC H 430 C2 NPC H 431 2.07 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 THR N 82 C THR N 82 O 0.122 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 ASP L 43 C - N - CA ANGL. DEV. = 16.0 DEGREES REMARK 500 ARG L 63 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES REMARK 500 ARG L 63 NE - CZ - NH2 ANGL. DEV. = -6.8 DEGREES REMARK 500 ALA L 91 N - CA - CB ANGL. DEV. = 9.5 DEGREES REMARK 500 VAL H 318 CA - CB - CG1 ANGL. DEV. = 9.9 DEGREES REMARK 500 MET H 334 CG - SD - CE ANGL. DEV. = 11.9 DEGREES REMARK 500 ARG H 340 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES REMARK 500 ARG H 343 N - CA - CB ANGL. DEV. = 14.1 DEGREES REMARK 500 ARG H 343 CA - CB - CG ANGL. DEV. = 14.8 DEGREES REMARK 500 ARG H 343 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES REMARK 500 ARG H 343 NE - CZ - NH2 ANGL. DEV. = -7.7 DEGREES REMARK 500 ARG H 343 C - N - CA ANGL. DEV. = 16.4 DEGREES REMARK 500 GLU H 346 N - CA - CB ANGL. DEV. = 11.3 DEGREES REMARK 500 ARG H 350 CA - CB - CG ANGL. DEV. = 17.8 DEGREES REMARK 500 ARG H 350 CG - CD - NE ANGL. DEV. = 13.0 DEGREES REMARK 500 ARG H 350 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES REMARK 500 LYS H 359 CA - CB - CG ANGL. DEV. = 23.4 DEGREES REMARK 500 ASP H 373 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES REMARK 500 SER H 388 N - CA - CB ANGL. DEV. = 9.9 DEGREES REMARK 500 GLU H 389 CA - C - O ANGL. DEV. = 14.0 DEGREES REMARK 500 ASP H 390 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES REMARK 500 ASP H 390 C - N - CA ANGL. DEV. = 29.6 DEGREES REMARK 500 GLY H 403 N - CA - C ANGL. DEV. = 26.0 DEGREES REMARK 500 TYR H 406 CA - CB - CG ANGL. DEV. = 11.9 DEGREES REMARK 500 ASP H 408 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES REMARK 500 ALA M 2 N - CA - C ANGL. DEV. = -16.9 DEGREES REMARK 500 GLU M 16 CA - CB - CG ANGL. DEV. = 15.8 DEGREES REMARK 500 GLU M 16 OE1 - CD - OE2 ANGL. DEV. = -7.8 DEGREES REMARK 500 ARG M 23 CA - CB - CG ANGL. DEV. = 13.6 DEGREES REMARK 500 ARG M 23 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 ASP M 43 CB - CG - OD1 ANGL. DEV. = 7.0 DEGREES REMARK 500 LEU M 45 CB - CA - C ANGL. DEV. = 14.6 DEGREES REMARK 500 ARG M 56 CA - CB - CG ANGL. DEV. = 17.1 DEGREES REMARK 500 ARG M 56 CD - NE - CZ ANGL. DEV. = 13.2 DEGREES REMARK 500 ARG M 56 NE - CZ - NH1 ANGL. DEV. = 6.0 DEGREES REMARK 500 ARG M 63 NE - CZ - NH1 ANGL. DEV. = 6.0 DEGREES REMARK 500 GLN M 81 CB - CG - CD ANGL. DEV. = 15.9 DEGREES REMARK 500 CYS M 90 N - CA - CB ANGL. DEV. = 9.5 DEGREES REMARK 500 ALA M 91 N - CA - CB ANGL. DEV. = -9.4 DEGREES REMARK 500 ARG I 340 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES REMARK 500 ARG I 340 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES REMARK 500 ARG I 350 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES REMARK 500 GLU I 389 CA - CB - CG ANGL. DEV. = 16.7 DEGREES REMARK 500 TYR I 395 CB - CG - CD1 ANGL. DEV. = -3.8 DEGREES REMARK 500 ASP I 408 CB - CG - OD1 ANGL. DEV. = 9.3 DEGREES REMARK 500 THR I 415 CA - CB - CG2 ANGL. DEV. = 9.2 DEGREES REMARK 500 VAL N 4 CA - CB - CG1 ANGL. DEV. = 9.6 DEGREES REMARK 500 VAL N 18 N - CA - CB ANGL. DEV. = 13.9 DEGREES REMARK 500 LEU N 20 CB - CA - C ANGL. DEV. = 12.7 DEGREES REMARK 500 ARG N 23 CD - NE - CZ ANGL. DEV. = 11.7 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 90 ANGLE DEVIATIONS. 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 ASP L 43 73.17 72.65 REMARK 500 HIS L 44 29.28 41.10 REMARK 500 THR L 53 -54.73 61.24 REMARK 500 SER L 67 -171.74 170.16 REMARK 500 ALA L 80 121.60 -39.74 REMARK 500 ALA L 86 178.04 175.76 REMARK 500 SER L 95 -98.61 34.97 REMARK 500 LEU L 109 88.00 60.87 REMARK 500 PHE H 329 -77.86 -38.61 REMARK 500 ARG H 340 110.55 174.66 REMARK 500 PRO H 341 137.38 -23.50 REMARK 500 ARG H 343 -60.63 148.80 REMARK 500 LYS H 367 -76.85 -119.77 REMARK 500 SER H 384 -88.59 -67.35 REMARK 500 LEU H 386 91.68 -61.69 REMARK 500 SER H 388 58.08 119.81 REMARK 500 ASP H 390 -21.35 -30.54 REMARK 500 SER H 391 91.14 -59.74 REMARK 500 TYR H 402 41.16 -99.89 REMARK 500 TYR M 34 57.07 37.52 REMARK 500 PRO M 42 115.56 -20.61 REMARK 500 ASP M 43 59.92 70.50 REMARK 500 HIS M 44 73.51 31.36 REMARK 500 THR M 53 -49.56 78.82 REMARK 500 ASN M 54 19.21 -142.52 REMARK 500 ALA M 62 -7.85 -39.82 REMARK 500 ALA M 86 -170.60 175.22 REMARK 500 TYR M 94 55.78 -116.23 REMARK 500 SER M 95 -8.22 65.39 REMARK 500 ASN M 96 4.37 -166.78 REMARK 500 ARG I 343 -93.10 -21.14 REMARK 500 SER I 366 -7.77 163.55 REMARK 500 SER I 385 52.45 35.02 REMARK 500 SER I 404 -16.18 -46.50 REMARK 500 ALA N 2 107.39 -173.57 REMARK 500 THR N 12 -158.68 -111.23 REMARK 500 PRO N 14 130.67 -35.85 REMARK 500 THR N 30 -154.12 -92.82 REMARK 500 SER N 32 2.31 -65.96 REMARK 500 TYR N 34 89.29 16.07 REMARK 500 ASP N 43 32.00 100.60 REMARK 500 THR N 53 -44.58 66.37 REMARK 500 ALA N 57 121.33 -23.81 REMARK 500 PRO N 58 136.46 -33.88 REMARK 500 VAL N 60 123.49 -39.24 REMARK 500 ALA N 62 -0.49 -53.38 REMARK 500 ALA N 80 140.49 -27.91 REMARK 500 THR N 82 -19.17 -40.33 REMARK 500 ALA N 86 -166.39 176.78 REMARK 500 SER N 95 -27.60 49.32 REMARK 500 VAL J 312 146.70 -174.93 REMARK 500 ALA J 316 34.81 -166.72 REMARK 500 SER J 317 135.77 24.78 REMARK 500 THR J 328 -110.41 -57.99 REMARK 500 PHE J 329 -14.35 147.83 REMARK 500 SER J 331 -170.47 85.96 REMARK 500 TYR J 332 106.05 69.31 REMARK 500 PRO J 353 -72.29 -85.57 REMARK 500 SER J 355 92.47 89.83 REMARK 500 LYS J 365 -58.35 -15.18 REMARK 500 THR J 369 124.41 169.10 REMARK 500 LEU J 370 -148.83 -87.32 REMARK 500 THR J 371 117.41 140.42 REMARK 500 SER J 377 71.51 35.95 REMARK 500 SER J 384 -119.08 -91.29 REMARK 500 SER J 385 79.65 -61.82 REMARK 500 ASP J 400 78.07 -54.42 REMARK 500 SER J 404 36.59 -95.32 REMARK 500 SER J 405 94.24 24.45 REMARK 500 SER J 419 141.80 30.42 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH M 111 DISTANCE = 7.42 ANGSTROMS REMARK 525 HOH N 150 DISTANCE = 5.11 ANGSTROMS REMARK 525 HOH I 434 DISTANCE = 6.74 ANGSTROMS REMARK 525 HOH M 119 DISTANCE = 10.28 ANGSTROMS REMARK 525 HOH M 120 DISTANCE = 7.07 ANGSTROMS REMARK 525 HOH I 476 DISTANCE = 5.56 ANGSTROMS REMARK 525 HOH N 456 DISTANCE = 11.05 ANGSTROMS REMARK 525 HOH L 184 DISTANCE = 5.19 ANGSTROMS REMARK 525 HOH L 185 DISTANCE = 7.46 ANGSTROMS REMARK 525 HOH I 515 DISTANCE = 5.23 ANGSTROMS REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: HA1 REMARK 800 EVIDENCE_CODE: UNKNOWN REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR THE HAPTEN, NPC, (4-HYDROXY- REMARK 800 3-NITROPHENYL) ACETATE BOUND TO A LIPID CARRIER BOUND TO FV REMARK 800 FRAGMENT FOR CHAINS L AND H, CONFORMATION 1 REMARK 800 SITE_IDENTIFIER: HA2 REMARK 800 EVIDENCE_CODE: UNKNOWN REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR THE HAPTEN, NPC, (4-HYDROXY- REMARK 800 3-NITROPHENYL) ACETATE BOUND TO A LIPID CARRIER BOUND TO FV REMARK 800 FRAGMENT FOR CHAINS L AND H, CONFORMATION 2 REMARK 800 SITE_IDENTIFIER: HA3 REMARK 800 EVIDENCE_CODE: UNKNOWN REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR THE HAPTEN, NPC, (4-HYDROXY- REMARK 800 3-NITROPHENYL) ACETATE BOUND TO A LIPID CARRIER BOUND TO FV REMARK 800 FRAGMENT FOR CHAINS M AND I REMARK 800 SITE_IDENTIFIER: HA4 REMARK 800 EVIDENCE_CODE: UNKNOWN REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR THE HAPTEN, NPC, (4-HYDROXY- REMARK 800 3-NITROPHENYL) ACETATE BOUND TO A LIPID CARRIER BOUND TO FV REMARK 800 FRAGMENT FOR CHAINS N AND J REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NPC H 430 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NPC H 431 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NPC I 430 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NPC J 430