REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH W.R.TULIP,J.N.VARGHESE,W.G.LAVER,R.G.WEBSTER,P.M.COLMAN REMARK 1 TITL REFINED CRYSTAL STRUCTURE OF THE INFLUENZA VIRUS N9 REMARK 1 TITL 2 NEURAMINIDASE-NC41 FAB COMPLEX REMARK 1 REF J.MOL.BIOL. V. 227 122 1992 REMARK 1 REFN ISSN 0022-2836 REMARK 1 REFERENCE 2 REMARK 1 AUTH W.R.TULIP,J.N.VARGHESE,R.G.WEBSTER,G.M.AIR,W.G.LAVER, REMARK 1 AUTH 2 P.M.COLMAN REMARK 1 TITL CRYSTAL STRUCTURES OF NEURAMINIDASE-ANTIBODY COMPLEXES REMARK 1 REF COLD SPRING HARBOR V. 54 257 1989 REMARK 1 REF 2 SYMP.QUANT.BIOL. REMARK 1 REFN ISSN 0091-7451 REMARK 1 REFERENCE 3 REMARK 1 AUTH P.M.COLMAN,W.G.LAVER,J.N.VARGHESE,A.T.BAKER,P.A.TULLOCH, REMARK 1 AUTH 2 G.M.AIR,R.G.WEBSTER REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF A COMPLEX OF ANTIBODY WITH REMARK 1 TITL 2 INFLUENZA VIRUS NEURAMINIDASE REMARK 1 REF NATURE V. 326 358 1987 REMARK 1 REFN ISSN 0028-0836 REMARK 2 REMARK 2 RESOLUTION. 2.50 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) : 2.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL 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 : 29288 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) : 0.212 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 : 6407 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 101 REMARK 3 SOLVENT ATOMS : 0 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) : NULL 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) : 0.019 REMARK 3 BOND ANGLES (DEGREES) : 3.80 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: THE COORDINATES OF THE CALCIUM ATOM ARE REMARK 3 NOT WELL DETERMINED. THE REFERENCE STRUCTURE FOR THE CALCIUM ATOM REMARK 3 IS THE N9 MUTANT S370L (PDB ENTRY 2NN9) REMARK 4 REMARK 4 1NCC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 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 : NULL REMARK 200 TEMPERATURE (KELVIN) : NULL REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : NULL REMARK 200 RADIATION SOURCE : NULL REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL REMARK 200 WAVELENGTH OR RANGE (A) : NULL REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : NULL REMARK 200 DETECTOR MANUFACTURER : NULL REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL 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 (%) : NULL REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL 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: X-PLOR REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 74.03 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.74 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 21 2 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 -Y+1/2,X+1/2,Z REMARK 290 4555 Y+1/2,-X+1/2,Z REMARK 290 5555 -X+1/2,Y+1/2,-Z REMARK 290 6555 X+1/2,-Y+1/2,-Z REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-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 0.000000 -1.000000 0.000000 83.50000 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 83.50000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 83.50000 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 83.50000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 83.50000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 83.50000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 83.50000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 83.50000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 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 300 REMARK: THE COORDINATES OF THE CARBOHYDRATE IN THE EPITOPE CAN BE REMARK 300 GENERATED FORM THE COORDINATES OF RESIDUES C 200A-C 200F BY REMARK 300 APPLYING THE FOLLOWING TRANSFORMATION: REMARK 300 REMARK 300 0.0 1.0 0.0 83.5 REMARK 300 -1.0 0.0 0.0 83.5 REMARK 300 0.0 0.0 1.0 0.0 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: DODECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: N, 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 BIOMT1 2 0.000000 1.000000 0.000000 83.50000 REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 83.50000 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 83.50000 REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 -83.50000 REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 4 -1.000000 0.000000 0.000000 167.00000 REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 350 BIOMT3 4 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 TRP N 97 CG TRP N 97 CD2 -0.107 REMARK 500 HIS N 98 NE2 HIS N 98 CD2 -0.093 REMARK 500 HIS N 150 NE2 HIS N 150 CD2 -0.074 REMARK 500 HIS N 184 NE2 HIS N 184 CD2 -0.081 REMARK 500 HIS N 233 NE2 HIS N 233 CD2 -0.077 REMARK 500 HIS N 274 NE2 HIS N 274 CD2 -0.070 REMARK 500 HIS N 312 NE2 HIS N 312 CD2 -0.077 REMARK 500 HIS L 91 NE2 HIS L 91 CD2 -0.069 REMARK 500 HIS L 189 NE2 HIS L 189 CD2 -0.074 REMARK 500 HIS L 198 NE2 HIS L 198 CD2 -0.069 REMARK 500 HIS H 212 NE2 HIS H 212 CD2 -0.079 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 TRP N 97 CD1 - CG - CD2 ANGL. DEV. = 5.5 DEGREES REMARK 500 TRP N 97 CE2 - CD2 - CE3 ANGL. DEV. = 7.9 DEGREES REMARK 500 TRP N 97 CE2 - CD2 - CG ANGL. DEV. = -5.5 DEGREES REMARK 500 TRP N 97 CD2 - CE3 - CZ3 ANGL. DEV. = -8.7 DEGREES REMARK 500 ASP N 103 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES REMARK 500 ARG N 107 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES REMARK 500 ASP N 111 CA - C - N ANGL. DEV. = 14.1 DEGREES REMARK 500 ASP N 111 O - C - N ANGL. DEV. = -12.4 DEGREES REMARK 500 TYR N 121 CA - CB - CG ANGL. DEV. = 12.6 DEGREES REMARK 500 ARG N 130 NE - CZ - NH2 ANGL. DEV. = -5.2 DEGREES REMARK 500 ARG N 152 CG - CD - NE ANGL. DEV. = -13.4 DEGREES REMARK 500 ARG N 152 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES REMARK 500 TRP N 161 CD1 - CG - CD2 ANGL. DEV. = 4.9 DEGREES REMARK 500 TRP N 161 CE2 - CD2 - CG ANGL. DEV. = -5.4 DEGREES REMARK 500 LEU N 163 CA - CB - CG ANGL. DEV. = 16.4 DEGREES REMARK 500 LEU N 163 CB - CG - CD2 ANGL. DEV. = -11.8 DEGREES REMARK 500 TYR N 169A CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES REMARK 500 ARG N 172 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES REMARK 500 TRP N 178 CD1 - CG - CD2 ANGL. DEV. = 5.4 DEGREES REMARK 500 TRP N 178 CE2 - CD2 - CG ANGL. DEV. = -5.5 DEGREES REMARK 500 HIS N 184 CA - C - N ANGL. DEV. = 14.1 DEGREES REMARK 500 ARG N 189 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES REMARK 500 ASN N 198 CB - CG - ND2 ANGL. DEV. = 15.0 DEGREES REMARK 500 TRP N 206 CE2 - CD2 - CG ANGL. DEV. = -5.1 DEGREES REMARK 500 ARG N 210 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES REMARK 500 TRP N 218 CD1 - CG - CD2 ANGL. DEV. = 8.2 DEGREES REMARK 500 TRP N 218 CG - CD1 - NE1 ANGL. DEV. = -6.7 DEGREES REMARK 500 TRP N 218 CE2 - CD2 - CG ANGL. DEV. = -6.9 DEGREES REMARK 500 GLN N 226 N - CA - C ANGL. DEV. = 18.3 DEGREES REMARK 500 ARG N 253 N - CA - CB ANGL. DEV. = -14.1 DEGREES REMARK 500 ARG N 253 CA - CB - CG ANGL. DEV. = 15.7 DEGREES REMARK 500 TYR N 255 CB - CG - CD2 ANGL. DEV. = -4.1 DEGREES REMARK 500 TRP N 265 CD1 - CG - CD2 ANGL. DEV. = 6.7 DEGREES REMARK 500 TRP N 265 CE2 - CD2 - CG ANGL. DEV. = -5.6 DEGREES REMARK 500 ARG N 284 CD - NE - CZ ANGL. DEV. = -16.0 DEGREES REMARK 500 ARG N 292 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES REMARK 500 VAL N 302 CG1 - CB - CG2 ANGL. DEV. = -12.3 DEGREES REMARK 500 ASP N 306 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES REMARK 500 HIS N 312 CB - CG - CD2 ANGL. DEV. = -9.9 DEGREES REMARK 500 THR N 313 CA - CB - CG2 ANGL. DEV. = -8.4 DEGREES REMARK 500 ARG N 327 N - CA - CB ANGL. DEV. = -12.5 DEGREES REMARK 500 ARG N 327 NE - CZ - NH1 ANGL. DEV. = -4.1 DEGREES REMARK 500 TRP N 361 CE2 - CD2 - CG ANGL. DEV. = -5.7 DEGREES REMARK 500 ARG N 364 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 ARG N 368 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 TRP N 403 CD1 - CG - CD2 ANGL. DEV. = 6.9 DEGREES REMARK 500 TRP N 403 CG - CD1 - NE1 ANGL. DEV. = -6.4 DEGREES REMARK 500 TRP N 403 CE2 - CD2 - CG ANGL. DEV. = -6.0 DEGREES REMARK 500 TRP N 412B CD1 - CG - CD2 ANGL. DEV. = 6.4 DEGREES REMARK 500 TRP N 412B CE2 - CD2 - CG ANGL. DEV. = -5.3 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 104 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 ARG N 82 5.25 -61.28 REMARK 500 SER N 96 -163.71 -161.50 REMARK 500 ASP N 111 -13.59 -142.01 REMARK 500 GLU N 119 74.32 44.22 REMARK 500 ALA N 133 163.65 178.96 REMARK 500 GLN N 154 31.72 -81.78 REMARK 500 THR N 181 139.25 177.90 REMARK 500 LYS N 187 -76.01 -82.92 REMARK 500 THR N 188 -163.10 -129.13 REMARK 500 ASN N 200 34.09 -153.15 REMARK 500 VAL N 212 -32.63 -131.87 REMARK 500 ALA N 219 10.48 -154.33 REMARK 500 ILE N 222 72.50 36.76 REMARK 500 THR N 225 -169.11 -125.85 REMARK 500 ALA N 246 50.27 -97.02 REMARK 500 THR N 247 -36.27 -155.20 REMARK 500 GLU N 259 27.75 42.32 REMARK 500 ARG N 284 55.11 32.95 REMARK 500 CYS N 291 -158.97 -139.18 REMARK 500 TRP N 295 -82.44 -69.70 REMARK 500 GLN N 315 -169.89 -161.98 REMARK 500 PRO N 331 171.01 -51.47 REMARK 500 ASN N 346 70.88 23.19 REMARK 500 ASN N 347 148.41 -172.76 REMARK 500 SER N 353 145.67 -171.46 REMARK 500 ASN N 359 73.65 -108.50 REMARK 500 GLN N 392 142.89 -179.75 REMARK 500 GLN N 395 115.06 -164.18 REMARK 500 SER N 404 -149.95 -124.35 REMARK 500 TYR N 412A -34.36 -38.88 REMARK 500 GLU N 433 65.43 -109.36 REMARK 500 ILE N 464 -6.73 -54.38 REMARK 500 THR L 31 -3.75 67.52 REMARK 500 ALA L 51 -4.62 55.37 REMARK 500 SER L 52 -18.27 -144.44 REMARK 500 ASP L 60 -33.55 -35.31 REMARK 500 SER L 67 176.32 172.90 REMARK 500 VAL L 78 104.86 -47.17 REMARK 500 ALA L 84 174.14 177.32 REMARK 500 HIS L 91 31.75 -143.84 REMARK 500 GLU L 154 93.00 -51.58 REMARK 500 ASN L 157 -168.58 -103.51 REMARK 500 GLU L 187 1.62 -61.09 REMARK 500 ASN L 190 -36.29 -147.85 REMARK 500 THR L 200 21.28 -77.19 REMARK 500 THR L 202 -61.16 -100.30 REMARK 500 ASN L 212 158.42 179.51 REMARK 500 PRO H 14 129.22 -37.95 REMARK 500 GLU H 16 -168.36 -60.28 REMARK 500 THR H 52A 35.65 -70.02 REMARK 500 REMARK 500 THIS ENTRY HAS 68 RAMACHANDRAN OUTLIERS. 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 GLY N 248 PRO N 249 129.96 REMARK 500 PRO L 94 PRO L 95 -30.20 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 N 155 0.09 SIDE CHAIN REMARK 500 TYR N 255 0.08 SIDE CHAIN REMARK 500 ARG N 284 0.27 SIDE CHAIN REMARK 500 ARG N 327 0.23 SIDE CHAIN REMARK 500 TYR L 87 0.07 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 ASP N 457 11.10 REMARK 500 ILE L 56 10.38 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 GLN N 226 23.5 L L OUTSIDE RANGE REMARK 500 THR L 20 47.8 L L OUTSIDE RANGE REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA N 1 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASN N 347 O REMARK 620 2 ASP N 324 OD2 127.0 REMARK 620 3 ASP N 324 OD1 90.5 39.9 REMARK 620 4 GLY N 297 O 125.0 105.6 130.5 REMARK 620 5 ASP N 293 O 89.5 117.7 142.3 77.9 REMARK 620 N 1 2 3 4 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG N 469A REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG N 470B REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA N 471C REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN N 472D REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN N 473E REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN N 474F REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG N 475A REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG N 476A REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA N 1