REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH S.C.YUHASZ,X.YSERN,M.STRAND,L.M.AMZEL REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY DIFFRACTION REMARK 1 TITL 2 STUDIES OF AN ANTI-4-HYDROXY-3-NITROPHENYLACETIC REMARK 1 TITL 3 ACID MONOCLONAL ANTIBODY FAB FRAGMENT COMPLEXED REMARK 1 TITL 4 WITH IMMUNIZING AND HETEROCLITIC HAPTENS REMARK 1 REF J.MOL.BIOL. V. 209 319 1989 REMARK 1 REFN ISSN 0022-2836 REMARK 2 REMARK 2 RESOLUTION. 3.00 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) : 3.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 10275 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) : 0.190 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 : 6350 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 44 REMARK 3 SOLVENT ATOMS : 5 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) : 0.30 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) : 0.017 REMARK 3 BOND ANGLES (DEGREES) : 4.08 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: REMARK 3 IN THE NUMBERING SCHEME USED IN THIS ENTRY, THE LIGHT REMARK 3 CHAIN RESIDUES FOR MOLECULE 1 ARE VL1 2 - 109, CL1 REMARK 3 110 - 212 AND THE HEAVY CHAIN RESIDUES ARE VH1 1 - 117, REMARK 3 CH1 118 - 218, RESPECTIVELY. MOLECULE 2 DEFINES THE LIGHT REMARK 3 CHAIN RESIDUES AS VL2 2 - 109, CL2 110 - 212, AND HEAVY REMARK 3 CHAIN RESIDUES AS VH2 1 - 117 AND CH2 118 - 218, REMARK 3 RESPECTIVELY. THE WATERS ARE NUMBERED 990 - 994 AND REMARK 3 THE 2 NITROPHENOL-EPSILON-AMINO CAPROIC MOLECULES REMARK 3 LABELED AS NP ARE NUMBERED 995 AND 996. REMARK 3 RESIDUES NUMBERED 132 - 140 OF H AND B CHAINS WERE NOT REMARK 3 FOUND IN THE ELECTRON DENSITY AND ARE PROBABLY DISORDERED. REMARK 4 REMARK 4 1YUH 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 : 01-JAN-00 REMARK 200 TEMPERATURE (KELVIN) : NULL REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : NULL REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : AREA DETECTOR REMARK 200 DETECTOR MANUFACTURER : SIEMENS REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XENGEN REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16470 REMARK 200 RESOLUTION RANGE HIGH (A) : NULL REMARK 200 RESOLUTION RANGE LOW (A) : NULL REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 70.3 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : 0.04700 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 (%): 50.93 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL 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 40.60000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 65.55000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.45000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 65.55000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 40.60000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.45000 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 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: 4580 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19250 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 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: 4850 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19240 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 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: 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 HIS L 97 NE2 HIS L 97 CD2 -0.076 REMARK 500 HIS L 200 NE2 HIS L 200 CD2 -0.074 REMARK 500 HIS H 35 NE2 HIS H 35 CD2 -0.072 REMARK 500 HIS H 169 NE2 HIS H 169 CD2 -0.068 REMARK 500 HIS H 204 NE2 HIS H 204 CD2 -0.069 REMARK 500 HIS A 191 NE2 HIS A 191 CD2 -0.074 REMARK 500 HIS A 200 NE2 HIS A 200 CD2 -0.070 REMARK 500 HIS A 203 NE2 HIS A 203 CD2 -0.068 REMARK 500 HIS B 35 NE2 HIS B 35 CD2 -0.069 REMARK 500 HIS B 169 NE2 HIS B 169 CD2 -0.072 REMARK 500 HIS B 204 NE2 HIS B 204 CD2 -0.070 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 THR L 5 CA - C - N ANGL. DEV. = -15.7 DEGREES REMARK 500 TRP L 37 CD1 - CG - CD2 ANGL. DEV. = 6.5 DEGREES REMARK 500 TRP L 37 CE2 - CD2 - CG ANGL. DEV. = -6.0 DEGREES REMARK 500 GLU L 40 CA - CB - CG ANGL. DEV. = 16.9 DEGREES REMARK 500 LEU L 45 CA - CB - CG ANGL. DEV. = 17.5 DEGREES REMARK 500 LEU L 49 CA - CB - CG ANGL. DEV. = 17.9 DEGREES REMARK 500 ARG L 56 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 TYR L 88 CB - CG - CD1 ANGL. DEV. = -4.1 DEGREES REMARK 500 TRP L 93 CD1 - CG - CD2 ANGL. DEV. = 6.3 DEGREES REMARK 500 TRP L 93 CE2 - CD2 - CG ANGL. DEV. = -5.7 DEGREES REMARK 500 TRP L 98 CD1 - CG - CD2 ANGL. DEV. = 6.4 DEGREES REMARK 500 TRP L 98 CE2 - CD2 - CG ANGL. DEV. = -6.3 DEGREES REMARK 500 TRP L 98 CG - CD2 - CE3 ANGL. DEV. = 5.5 DEGREES REMARK 500 VAL L 118 CG1 - CB - CG2 ANGL. DEV. = -9.6 DEGREES REMARK 500 TRP L 151 CB - CG - CD1 ANGL. DEV. = -8.3 DEGREES REMARK 500 TRP L 151 CE2 - CD2 - CG ANGL. DEV. = -6.1 DEGREES REMARK 500 TRP L 151 CG - CD2 - CE3 ANGL. DEV. = 5.5 DEGREES REMARK 500 MET L 176 CG - SD - CE ANGL. DEV. = -10.2 DEGREES REMARK 500 TRP L 188 CD1 - CG - CD2 ANGL. DEV. = 6.6 DEGREES REMARK 500 TRP L 188 CE2 - CD2 - CG ANGL. DEV. = -6.4 DEGREES REMARK 500 TRP L 188 CG - CD2 - CE3 ANGL. DEV. = 5.8 DEGREES REMARK 500 GLU L 189 N - CA - C ANGL. DEV. = 21.4 DEGREES REMARK 500 ARG L 190 NE - CZ - NH1 ANGL. DEV. = 5.3 DEGREES REMARK 500 ARG L 190 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES REMARK 500 SER L 195 N - CA - C ANGL. DEV. = 17.4 DEGREES REMARK 500 VAL L 198 CA - CB - CG2 ANGL. DEV. = -9.4 DEGREES REMARK 500 TRP H 36 CD1 - CG - CD2 ANGL. DEV. = 5.3 DEGREES REMARK 500 TRP H 36 CE2 - CD2 - CG ANGL. DEV. = -5.4 DEGREES REMARK 500 TRP H 47 CD1 - CG - CD2 ANGL. DEV. = 5.8 DEGREES REMARK 500 TRP H 47 CE2 - CD2 - CG ANGL. DEV. = -6.1 DEGREES REMARK 500 ILE H 51 CB - CA - C ANGL. DEV. = -13.4 DEGREES REMARK 500 LYS H 65 O - C - N ANGL. DEV. = -9.7 DEGREES REMARK 500 TYR H 80 CA - CB - CG ANGL. DEV. = 14.7 DEGREES REMARK 500 TYR H 80 CB - CG - CD2 ANGL. DEV. = -7.3 DEGREES REMARK 500 TYR H 80 CB - CG - CD1 ANGL. DEV. = 6.3 DEGREES REMARK 500 SER H 85 CA - C - N ANGL. DEV. = -15.6 DEGREES REMARK 500 ARG H 98 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES REMARK 500 TYR H 99 CB - CG - CD1 ANGL. DEV. = -6.3 DEGREES REMARK 500 ARG H 103 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES REMARK 500 TRP H 108 CB - CG - CD1 ANGL. DEV. = -8.4 DEGREES REMARK 500 TRP H 108 CE2 - CD2 - CG ANGL. DEV. = -5.9 DEGREES REMARK 500 TRP H 108 CG - CD2 - CE3 ANGL. DEV. = 8.5 DEGREES REMARK 500 GLN H 110 CA - CB - CG ANGL. DEV. = 14.0 DEGREES REMARK 500 LEU H 146 CA - CB - CG ANGL. DEV. = 20.0 DEGREES REMARK 500 TRP H 159 CD1 - CG - CD2 ANGL. DEV. = 7.4 DEGREES REMARK 500 TRP H 159 CE2 - CD2 - CG ANGL. DEV. = -6.7 DEGREES REMARK 500 TRP H 159 CG - CD2 - CE3 ANGL. DEV. = 6.5 DEGREES REMARK 500 SER H 166 N - CA - C ANGL. DEV. = 16.8 DEGREES REMARK 500 LEU H 175 CA - CB - CG ANGL. DEV. = 17.5 DEGREES REMARK 500 TRP H 193 CD1 - CG - CD2 ANGL. DEV. = 6.9 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 115 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 GLN L 6 -162.45 -68.11 REMARK 500 PRO L 14 109.86 -55.13 REMARK 500 VAL L 29 77.71 -63.65 REMARK 500 ALA L 35 124.00 -20.05 REMARK 500 LYS L 41 -157.40 -149.44 REMARK 500 PRO L 42 99.93 -27.95 REMARK 500 ASP L 43 77.11 51.30 REMARK 500 ARG L 44 -5.01 57.61 REMARK 500 THR L 53 -36.01 63.11 REMARK 500 PRO L 58 82.51 -63.44 REMARK 500 ARG L 63 -50.95 -125.93 REMARK 500 LEU L 68 91.68 -67.38 REMARK 500 THR L 82 -18.23 -44.42 REMARK 500 SER L 95 -66.27 54.83 REMARK 500 HIS L 97 138.21 174.92 REMARK 500 PRO L 112 154.27 -10.55 REMARK 500 SER L 125 -38.59 -34.12 REMARK 500 VAL L 146 78.79 -114.04 REMARK 500 ASP L 154 80.43 169.23 REMARK 500 THR L 156 99.87 -38.63 REMARK 500 PRO L 167 82.64 -7.95 REMARK 500 SER L 171 -41.21 13.99 REMARK 500 ASN L 173 27.26 81.08 REMARK 500 TRP L 188 -81.68 -75.93 REMARK 500 GLU L 189 -57.70 -26.47 REMARK 500 ALA L 192 -70.01 -89.01 REMARK 500 GLU L 201 16.22 57.43 REMARK 500 LEU L 209 -161.91 -127.30 REMARK 500 ARG L 211 -41.30 -138.57 REMARK 500 GLN H 3 -161.47 -109.85 REMARK 500 PHE H 4 53.76 -175.32 REMARK 500 SER H 7 -161.38 -59.36 REMARK 500 PRO H 14 108.53 -39.38 REMARK 500 PHE H 29 -67.11 -15.74 REMARK 500 SER H 31 40.51 -100.93 REMARK 500 PRO H 41 89.63 -49.30 REMARK 500 VAL H 56 -31.55 75.87 REMARK 500 SER H 77 43.26 33.45 REMARK 500 SER H 85 91.06 -19.22 REMARK 500 ASP H 90 48.06 -144.09 REMARK 500 ALA H 92 -153.40 -144.91 REMARK 500 ALA H 100 -119.43 -74.51 REMARK 500 CYS H 102 87.71 27.63 REMARK 500 THR H 121 105.51 -24.49 REMARK 500 PRO H 131 73.75 -56.20 REMARK 500 ALA H 135 127.30 169.40 REMARK 500 THR H 137 92.44 -45.75 REMARK 500 SER H 139 -82.33 18.42 REMARK 500 PRO H 154 90.08 -54.18 REMARK 500 TRP H 159 -86.62 -79.47 REMARK 500 SER H 161 -9.76 53.41 REMARK 500 SER H 166 61.66 -66.19 REMARK 500 SER H 177 74.02 39.77 REMARK 500 ASP H 178 -29.70 62.55 REMARK 500 ALA H 190 -48.28 -26.84 REMARK 500 THR H 192 -80.94 -160.12 REMARK 500 SER H 195 -75.80 -50.79 REMARK 500 PRO H 205 -72.81 -44.18 REMARK 500 ALA H 206 -72.81 -30.22 REMARK 500 SER H 208 106.89 -34.85 REMARK 500 GLU A 7 154.09 -39.36 REMARK 500 PRO A 14 108.48 -53.46 REMARK 500 THR A 31 -8.07 -58.26 REMARK 500 ASN A 33 -4.04 -54.81 REMARK 500 TRP A 37 76.29 -116.52 REMARK 500 LYS A 41 -144.97 -113.52 REMARK 500 PRO A 42 121.06 -34.68 REMARK 500 ASP A 43 92.61 21.64 REMARK 500 ARG A 44 11.97 54.13 REMARK 500 THR A 47 103.03 10.51 REMARK 500 THR A 53 -26.58 67.02 REMARK 500 ASN A 54 -17.92 -163.55 REMARK 500 ASN A 55 94.11 -63.97 REMARK 500 PRO A 58 39.83 -61.37 REMARK 500 LEU A 68 80.00 -68.41 REMARK 500 ALA A 80 132.39 -33.91 REMARK 500 SER A 95 -80.56 55.35 REMARK 500 PRO A 112 116.91 4.02 REMARK 500 GLU A 126 -71.37 -78.06 REMARK 500 GLU A 127 -28.05 -29.64 REMARK 500 ILE A 139 78.91 -115.29 REMARK 500 ASP A 141 85.25 75.37 REMARK 500 PRO A 144 132.18 -31.38 REMARK 500 PRO A 157 107.24 -24.11 REMARK 500 MET A 162 96.23 -55.50 REMARK 500 PRO A 167 98.63 -21.35 REMARK 500 LYS A 169 73.57 -48.46 REMARK 500 SER A 171 -56.89 32.56 REMARK 500 ALA A 192 -31.30 -156.25 REMARK 500 TYR A 194 40.48 -80.53 REMARK 500 LEU A 209 -82.61 -126.05 REMARK 500 SER A 210 169.30 121.11 REMARK 500 ARG A 211 -57.35 -129.52 REMARK 500 SER B 7 -93.23 -66.42 REMARK 500 PRO B 41 70.29 -62.84 REMARK 500 ARG B 43 -77.73 -142.45 REMARK 500 ASN B 55 42.73 -168.94 REMARK 500 VAL B 56 -40.90 55.80 REMARK 500 VAL B 57 104.77 10.38 REMARK 500 THR B 58 71.15 -117.05 REMARK 500 LYS B 67 -32.33 -138.17 REMARK 500 SER B 85 15.51 52.07 REMARK 500 THR B 87 -157.08 -98.75 REMARK 500 GLU B 89 34.96 -89.50 REMARK 500 ASP B 90 21.12 -151.87 REMARK 500 TYR B 101 131.63 -173.72 REMARK 500 CYS B 102 100.22 2.64 REMARK 500 GLN B 110 -32.32 -35.73 REMARK 500 THR B 121 64.45 -28.98 REMARK 500 PRO B 124 -159.55 -74.75 REMARK 500 SER B 125 93.99 -161.70 REMARK 500 PRO B 128 104.21 -49.36 REMARK 500 PRO B 131 64.58 -60.40 REMARK 500 SER B 133 -146.68 -103.44 REMARK 500 ALA B 135 144.06 -175.32 REMARK 500 THR B 137 80.64 -46.35 REMARK 500 SER B 139 -31.52 -19.39 REMARK 500 GLU B 153 -46.07 -16.32 REMARK 500 THR B 156 72.66 -100.84 REMARK 500 ASN B 160 63.17 -3.85 REMARK 500 SER B 161 71.94 24.52 REMARK 500 SER B 166 69.13 -45.23 REMARK 500 GLN B 176 74.38 -56.99 REMARK 500 SER B 177 94.50 57.17 REMARK 500 ASP B 178 -33.48 56.17 REMARK 500 PRO B 189 125.53 -38.47 REMARK 500 ALA B 190 -56.11 -14.78 REMARK 500 SER B 191 -15.06 -21.46 REMARK 500 THR B 192 -80.95 -129.90 REMARK 500 PRO B 194 -33.36 -28.18 REMARK 500 PRO B 205 -96.14 -57.88 REMARK 500 SER B 208 86.20 -64.10 REMARK 500 ALA B 210 13.12 -158.24 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 TRP H 193 PRO H 194 -30.52 REMARK 500 LYS A 41 PRO A 42 131.55 REMARK 500 PRO A 122 PRO A 123 145.12 REMARK 500 TYR A 143 PRO A 144 -31.37 REMARK 500 THR A 156 PRO A 157 145.83 REMARK 500 ARG B 103 PRO B 104 126.32 REMARK 500 PHE B 151 PRO B 152 -31.27 REMARK 500 PHE B 171 PRO B 172 149.66 REMARK 500 VAL B 188 PRO B 189 148.45 REMARK 500 TRP B 193 PRO B 194 -41.11 REMARK 500 VAL B 216 PRO B 217 142.50 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 99 0.09 SIDE_CHAIN REMARK 500 TYR A 180 0.08 SIDE_CHAIN REMARK 500 TYR A 194 0.09 SIDE_CHAIN 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 NP H 995 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NP B 996 REMARK 999 REMARK 999 SEQUENCE REMARK 999 REMARK 999 IN THE NUMBERING SCHEME USED IN THIS ENTRY, THE LIGHT REMARK 999 CHAIN RESIDUES FOR MOLECULE 1 ARE VL1 2 - 109, CL1 REMARK 999 110 - 212 AND THE HEAVY CHAIN RESIDUES ARE VH1 1 - 117, REMARK 999 CH1 118 - 218, RESPECTIVELY. MOLECULE 2 DEFINES THE LIGHT REMARK 999 CHAIN RESIDUES AS VL2 2 - 109, CL2 110 - 212, AND HEAVY REMARK 999 CHAIN RESIDUES AS VH2 1 - 117 AND CH2 118 - 218, REMARK 999 RESPECTIVELY. THE WATERS ARE NUMBERED 990 - 994 AND REMARK 999 THE 2 NITROPHENOL-EPSILON-AMINO CAPROIC MOLECULES REMARK 999 LABELED AS NP ARE NUMBERED 995 AND 996.