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 STRUCTURES 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 P.M.COLMAN,W.R.TULIP,J.N.VARGHESE,P.A.TULLOCH,A.T.BAKER, REMARK 1 AUTH 2 W.G.LAVER,G.M.AIR,R.G.WEBSTER REMARK 1 TITL THREE DIMENSIONAL STRUCTURES OF INFLUENZA VIRUS REMARK 1 TITL 2 NEURAMINIDASE-ANTIBODY COMPLEXES REMARK 1 REF PHILOS.TRANS.R.SOC.LONDON, V. 323 511 1989 REMARK 1 REF 2 SER.B REMARK 1 REFN ISSN 0080-4622 REMARK 1 REFERENCE 3 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 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) : NULL 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 : NULL 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) : 0.200 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 : 4777 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 86 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) : 0.014 REMARK 3 BOND ANGLES (DEGREES) : 3.50 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 NO SOLVENT ATOMS AND NO CALCIUM ATOM. THE REFERENCE REMARK 3 STRUCTURE FOR THE CALCIUM ATOM IS THE N9 MUTANT S370L (PDB REMARK 3 ENTRY 2NN9). REMARK 4 REMARK 4 1NMA 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 : 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 (%): 71.09 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.25 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 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,X,Z REMARK 290 4555 Y,-X,Z REMARK 290 5555 -X,Y,-Z REMARK 290 6555 X,-Y,-Z REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-Z REMARK 290 9555 X+1/2,Y+1/2,Z+1/2 REMARK 290 10555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 11555 -Y+1/2,X+1/2,Z+1/2 REMARK 290 12555 Y+1/2,-X+1/2,Z+1/2 REMARK 290 13555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 14555 X+1/2,-Y+1/2,-Z+1/2 REMARK 290 15555 Y+1/2,X+1/2,-Z+1/2 REMARK 290 16555 -Y+1/2,-X+1/2,-Z+1/2 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 0.00000 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000 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 SMTRY1 9 1.000000 0.000000 0.000000 85.75000 REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 85.75000 REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 80.10000 REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 85.75000 REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 85.75000 REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 80.10000 REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 85.75000 REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 85.75000 REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 80.10000 REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 85.75000 REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 85.75000 REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 80.10000 REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 85.75000 REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 85.75000 REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 80.10000 REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 85.75000 REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 85.75000 REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 80.10000 REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 85.75000 REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 85.75000 REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 80.10000 REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 85.75000 REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 85.75000 REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 80.10000 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 200A - 200F DO NOT REMARK 300 REQUIRE TRANSFORMATION TO APPEAR AS PART OF THE EPITOPE. REMARK 300 THIS CARBOHYDRATE IS COVALENTLY ATTACHED TO THE REMARK 300 NEURAMINIDASE SUBUNIT WHICH IS NEIGHBORING TO THE ONE IN REMARK 300 THIS FILE. 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 0.00000 REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 171.50000 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 171.50000 REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 4 -1.000000 0.000000 0.000000 171.50000 REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 171.50000 REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000 REMARK 400 REMARK 400 COMPOUND REMARK 400 NEURAMINIDASE RESIDUES 458 - 468 ARE INCORRECT, ALL BEING REMARK 400 ONE RESIDUE OUT OF REGISTER. THEY ARE NOT PART OF ANTIBODY REMARK 400 BINDING SITE. 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 PRO N 459 REMARK 465 ASP N 460 REMARK 465 GLY N 461 REMARK 465 ALA N 462 REMARK 465 LYS N 463 REMARK 465 ILE N 464 REMARK 465 GLU N 465 REMARK 465 TYR N 466 REMARK 465 PHE N 467 REMARK 465 LEU N 468 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 ND2 ASN N 200 C1 NAG N 469A 3655 1.49 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 HIS N 98 NE2 HIS N 98 CD2 -0.081 REMARK 500 HIS N 144 NE2 HIS N 144 CD2 -0.067 REMARK 500 HIS N 184 NE2 HIS N 184 CD2 -0.075 REMARK 500 HIS N 274 NE2 HIS N 274 CD2 -0.071 REMARK 500 HIS N 312 NE2 HIS N 312 CD2 -0.072 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 N 88 N - CA - CB ANGL. DEV. = -12.2 DEGREES REMARK 500 TRP N 97 CD1 - CG - CD2 ANGL. DEV. = 6.7 DEGREES REMARK 500 TRP N 97 CE2 - CD2 - CG ANGL. DEV. = -6.2 DEGREES REMARK 500 GLU N 119 CA - CB - CG ANGL. DEV. = 13.2 DEGREES REMARK 500 ARG N 152 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES REMARK 500 TRP N 161 CD1 - CG - CD2 ANGL. DEV. = 6.1 DEGREES REMARK 500 TRP N 161 CE2 - CD2 - CG ANGL. DEV. = -5.8 DEGREES REMARK 500 TRP N 161 CG - CD2 - CE3 ANGL. DEV. = 5.6 DEGREES REMARK 500 ARG N 172 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES REMARK 500 ARG N 172 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES REMARK 500 TRP N 178 CD1 - CG - CD2 ANGL. DEV. = 6.1 DEGREES REMARK 500 TRP N 178 CE2 - CD2 - CG ANGL. DEV. = -5.6 DEGREES REMARK 500 ARG N 187 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES REMARK 500 ARG N 187 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES REMARK 500 TRP N 206 CD1 - CG - CD2 ANGL. DEV. = 6.5 DEGREES REMARK 500 TRP N 206 CE2 - CD2 - CG ANGL. DEV. = -5.3 DEGREES REMARK 500 ARG N 210 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES REMARK 500 TRP N 218 CD1 - CG - CD2 ANGL. DEV. = 7.2 DEGREES REMARK 500 TRP N 218 CE2 - CD2 - CG ANGL. DEV. = -6.2 DEGREES REMARK 500 ARG N 224 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 GLN N 226 N - CA - C ANGL. DEV. = 16.9 DEGREES REMARK 500 TYR N 256 CB - CG - CD1 ANGL. DEV. = -3.8 DEGREES REMARK 500 TRP N 265 CD1 - CG - CD2 ANGL. DEV. = 7.7 DEGREES REMARK 500 TRP N 265 CB - CG - CD1 ANGL. DEV. = -9.1 DEGREES REMARK 500 TRP N 265 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES REMARK 500 TRP N 265 CE2 - CD2 - CG ANGL. DEV. = -6.3 DEGREES REMARK 500 TRP N 265 CG - CD2 - CE3 ANGL. DEV. = 6.4 DEGREES REMARK 500 TRP N 295 CD1 - CG - CD2 ANGL. DEV. = 6.1 DEGREES REMARK 500 TRP N 295 CE2 - CD2 - CG ANGL. DEV. = -5.9 DEGREES REMARK 500 ARG N 300 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES REMARK 500 TRP N 361 CD1 - CG - CD2 ANGL. DEV. = 6.9 DEGREES REMARK 500 TRP N 361 CE2 - CD2 - CG ANGL. DEV. = -5.8 DEGREES REMARK 500 ARG N 364 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES REMARK 500 ARG N 364 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES REMARK 500 ARG N 371 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 ARG N 371 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES REMARK 500 THR N 401 N - CA - CB ANGL. DEV. = -14.3 DEGREES REMARK 500 TRP N 403 CD1 - CG - CD2 ANGL. DEV. = 5.5 DEGREES REMARK 500 TRP N 403 CB - CG - CD1 ANGL. DEV. = -8.6 DEGREES REMARK 500 TRP N 403 CE2 - CD2 - CG ANGL. DEV. = -5.9 DEGREES REMARK 500 TRP N 403 CG - CD2 - CE3 ANGL. DEV. = 6.7 DEGREES REMARK 500 TYR N 406 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES REMARK 500 TRP N 412B CD1 - CG - CD2 ANGL. DEV. = 6.5 DEGREES REMARK 500 TRP N 412B CE2 - CD2 - CG ANGL. DEV. = -6.3 DEGREES REMARK 500 ARG N 430 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES REMARK 500 TRP N 437 CD1 - CG - CD2 ANGL. DEV. = 6.6 DEGREES REMARK 500 TRP N 437 CE2 - CD2 - CG ANGL. DEV. = -5.7 DEGREES REMARK 500 TRP N 438 CD1 - CG - CD2 ANGL. DEV. = 5.1 DEGREES REMARK 500 TRP N 438 CE2 - CD2 - CG ANGL. DEV. = -5.4 DEGREES REMARK 500 TRP N 456 CE2 - CD2 - CG ANGL. DEV. = -5.1 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 76 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 GLU N 83 129.80 -172.46 REMARK 500 TYR N 100 -62.89 -124.64 REMARK 500 ASN N 104 38.62 -91.62 REMARK 500 ALA N 105 -51.99 -29.68 REMARK 500 ASP N 111 45.93 -148.77 REMARK 500 THR N 117 -164.49 -122.52 REMARK 500 ARG N 118 172.21 171.89 REMARK 500 GLU N 119 87.36 35.52 REMARK 500 PRO N 126 5.30 -60.02 REMARK 500 ASP N 127 11.58 -151.56 REMARK 500 ASN N 146 104.11 -57.70 REMARK 500 ARG N 152 112.09 -160.96 REMARK 500 PRO N 167 82.85 -64.30 REMARK 500 ASN N 170 -59.25 172.23 REMARK 500 THR N 181 145.94 -179.85 REMARK 500 ARG N 187 -63.83 -92.12 REMARK 500 ASN N 200 43.64 -157.97 REMARK 500 ASN N 208 71.87 60.72 REMARK 500 ARG N 209 -9.50 61.59 REMARK 500 THR N 217 104.45 -38.80 REMARK 500 ARG N 220 50.89 18.28 REMARK 500 ILE N 222 95.94 38.62 REMARK 500 THR N 225 -157.40 -127.93 REMARK 500 GLU N 227 32.54 75.30 REMARK 500 THR N 247 54.25 -91.93 REMARK 500 LYS N 264 173.06 164.99 REMARK 500 GLU N 277 98.80 55.71 REMARK 500 GLU N 283 -70.60 -138.03 REMARK 500 ALA N 285 5.77 58.42 REMARK 500 CYS N 291 -153.82 -125.22 REMARK 500 TRP N 295 -79.27 -62.14 REMARK 500 GLN N 315 -168.91 -173.42 REMARK 500 SER N 319 156.62 -49.06 REMARK 500 ASP N 330 108.26 -58.84 REMARK 500 ASN N 346 16.47 86.31 REMARK 500 ASP N 356 64.63 -118.92 REMARK 500 SER N 404 -130.83 -122.58 REMARK 500 ASP N 434 1.12 -63.81 REMARK 500 THR L 8 144.24 64.74 REMARK 500 ALA L 13 137.77 -171.99 REMARK 500 SER L 14 31.54 -87.78 REMARK 500 LEU L 15 89.78 59.09 REMARK 500 ILE L 29 34.48 -85.47 REMARK 500 SER L 30 -105.14 36.45 REMARK 500 ASN L 31 33.71 -143.50 REMARK 500 PRO L 40 -36.27 -33.61 REMARK 500 THR L 43 106.36 -8.29 REMARK 500 THR L 51 -49.04 61.29 REMARK 500 HIS L 55 -167.86 -77.73 REMARK 500 SER L 60 -22.60 -36.07 REMARK 500 REMARK 500 THIS ENTRY HAS 62 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 -145.49 REMARK 500 ARG N 327 PRO N 328 146.03 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 ARG L 107 0.28 SIDE CHAIN REMARK 500 ARG L 108 0.08 SIDE CHAIN REMARK 500 TYR H 90 0.07 SIDE CHAIN REMARK 500 ARG H 100 0.21 SIDE CHAIN 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 ARG N 220 24.9 L L OUTSIDE RANGE REMARK 500 GLN N 226 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 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