REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH S.S.RAJAN,K.R.ELY,E.E.ABOLA,M.K.WOOD,P.M.COLMAN,R.J.ATHAY, REMARK 1 AUTH 2 A.B.EDMUNDSON REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF THE MCG IGG1 IMMUNOGLOBULIN REMARK 1 REF MOL.IMMUNOL. V. 20 787 1983 REMARK 1 REFN ISSN 0161-5890 REMARK 1 REFERENCE 2 REMARK 1 AUTH A.B.EDMUNDSON,K.R.ELY,E.E.ABOLA REMARK 1 TITL CONFORMATIONAL FLEXIBILITY IN IMMUNOGLOBULINS REMARK 1 REF CONTEMP.TOP.MOL.IMMUNOL. V. 7 95 1978 REMARK 1 REFN ISSN 0090-8800 REMARK 1 REFERENCE 3 REMARK 1 AUTH A.B.EDMUNDSON,M.K.WOOD,M.SCHIFFER,K.D.HARDMAN,C.F.AINSWORTH, REMARK 1 AUTH 2 K.R.ELY REMARK 1 TITL A CRYSTALLOGRAPHIC INVESTIGATION OF A HUMAN IGG REMARK 1 TITL 2 IMMUNOGLOBULIN REMARK 1 REF J.BIOL.CHEM. V. 245 2763 1970 REMARK 1 REFN ISSN 0021-9258 REMARK 2 REMARK 2 RESOLUTION. 3.20 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) : 3.20 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) : 0.232 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 : 4911 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 130 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) : 0.022 REMARK 3 BOND ANGLES (DEGREES) : NULL 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: NULL REMARK 4 REMARK 4 1MCO 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 (%): 62.18 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.25 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -X,Y,-Z+1/2 REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 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 93.35000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 93.35000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 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 44.20000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 55.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 44.20000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 55.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 93.35000 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 44.20000 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 55.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 93.35000 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 44.20000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 55.00000 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 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: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA,PQS REMARK 350 TOTAL BURIED SURFACE AREA: 19280 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 64440 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 1.0 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 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 280.05000 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 201 NE2 HIS L 201 CD2 -0.067 REMARK 500 LEU H 18 N LEU H 18 CA 0.132 REMARK 500 LEU H 84 CA LEU H 84 CB 0.166 REMARK 500 LEU H 84 CB LEU H 84 CG 0.175 REMARK 500 SER H 85 CA SER H 85 CB 0.116 REMARK 500 HIS H 204 NE2 HIS H 204 CD2 -0.067 REMARK 500 GLU H 243 CD GLU H 243 OE1 -0.072 REMARK 500 HIS H 253 NE2 HIS H 253 CD2 -0.068 REMARK 500 HIS H 295 NE2 HIS H 295 CD2 -0.080 REMARK 500 HIS H 414 NE2 HIS H 414 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 ASP L 28 CA - CB - CG ANGL. DEV. = 14.5 DEGREES REMARK 500 VAL L 29 CG1 - CB - CG2 ANGL. DEV. = -11.0 DEGREES REMARK 500 VAL L 35 CA - CB - CG1 ANGL. DEV. = 10.7 DEGREES REMARK 500 VAL L 35 CA - CB - CG2 ANGL. DEV. = -11.5 DEGREES REMARK 500 TRP L 37 CD1 - CG - CD2 ANGL. DEV. = 5.4 DEGREES REMARK 500 TRP L 37 CE2 - CD2 - CG ANGL. DEV. = -5.8 DEGREES REMARK 500 VAL L 53 CG1 - CB - CG2 ANGL. DEV. = -11.1 DEGREES REMARK 500 VAL L 53 CA - CB - CG1 ANGL. DEV. = 9.8 DEGREES REMARK 500 VAL L 53 CA - CB - CG2 ANGL. DEV. = -10.6 DEGREES REMARK 500 ARG L 56 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 VAL L 60 CA - CB - CG1 ANGL. DEV. = -9.0 DEGREES REMARK 500 TYR L 89 CA - CB - CG ANGL. DEV. = 15.1 DEGREES REMARK 500 CYS L 90 CA - CB - SG ANGL. DEV. = 8.3 DEGREES REMARK 500 VAL L 100 CG1 - CB - CG2 ANGL. DEV. = -10.6 DEGREES REMARK 500 THR L 103 CA - CB - CG2 ANGL. DEV. = 9.0 DEGREES REMARK 500 VAL L 109 CA - CB - CG2 ANGL. DEV. = 9.3 DEGREES REMARK 500 GLN L 112 N - CA - C ANGL. DEV. = 17.1 DEGREES REMARK 500 PRO L 113 C - N - CA ANGL. DEV. = 11.2 DEGREES REMARK 500 ASN L 116 CA - CB - CG ANGL. DEV. = 13.4 DEGREES REMARK 500 PRO L 117 CA - N - CD ANGL. DEV. = -8.7 DEGREES REMARK 500 PRO L 117 N - CA - C ANGL. DEV. = 23.6 DEGREES REMARK 500 ASN L 116 CA - C - N ANGL. DEV. = 18.9 DEGREES REMARK 500 THR L 118 N - CA - C ANGL. DEV. = 21.5 DEGREES REMARK 500 THR L 118 C - N - CA ANGL. DEV. = 16.9 DEGREES REMARK 500 PHE L 122 CA - CB - CG ANGL. DEV. = 14.7 DEGREES REMARK 500 PRO L 123 C - N - CA ANGL. DEV. = 10.7 DEGREES REMARK 500 LEU L 139 CB - CA - C ANGL. DEV. = -13.0 DEGREES REMARK 500 ILE L 140 CA - CB - CG2 ANGL. DEV. = -12.9 DEGREES REMARK 500 SER L 141 CA - C - N ANGL. DEV. = -14.2 DEGREES REMARK 500 SER L 141 O - C - N ANGL. DEV. = 9.6 DEGREES REMARK 500 TRP L 152 CE2 - CD2 - CG ANGL. DEV. = -4.9 DEGREES REMARK 500 HIS L 201 CA - CB - CG ANGL. DEV. = -10.4 DEGREES REMARK 500 VAL L 206 CG1 - CB - CG2 ANGL. DEV. = -9.7 DEGREES REMARK 500 SER L 216 N - CA - C ANGL. DEV. = 19.3 DEGREES REMARK 500 LEU H 2 CA - CB - CG ANGL. DEV. = 14.4 DEGREES REMARK 500 VAL H 3 CG1 - CB - CG2 ANGL. DEV. = -9.6 DEGREES REMARK 500 LEU H 11 CA - CB - CG ANGL. DEV. = 14.8 DEGREES REMARK 500 LEU H 11 CD1 - CG - CD2 ANGL. DEV. = -27.8 DEGREES REMARK 500 PRO H 14 N - CA - C ANGL. DEV. = 16.7 DEGREES REMARK 500 SER H 15 N - CA - C ANGL. DEV. = 20.8 DEGREES REMARK 500 SER H 15 C - N - CA ANGL. DEV. = 16.2 DEGREES REMARK 500 GLU H 16 N - CA - CB ANGL. DEV. = -11.6 DEGREES REMARK 500 GLU H 16 CA - CB - CG ANGL. DEV. = 14.8 DEGREES REMARK 500 ALA H 17 CB - CA - C ANGL. DEV. = 13.0 DEGREES REMARK 500 ALA H 17 N - CA - CB ANGL. DEV. = -21.1 DEGREES REMARK 500 GLU H 16 CA - C - N ANGL. DEV. = 19.9 DEGREES REMARK 500 GLU H 16 O - C - N ANGL. DEV. = -13.7 DEGREES REMARK 500 ALA H 17 C - N - CA ANGL. DEV. = 19.1 DEGREES REMARK 500 LEU H 18 CA - CB - CG ANGL. DEV. = 21.4 DEGREES REMARK 500 LEU H 18 CA - C - O ANGL. DEV. = 13.7 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 179 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 CYS L 22 103.89 -167.95 REMARK 500 SER L 26 -65.74 -3.01 REMARK 500 SER L 27 -6.08 -58.89 REMARK 500 ASP L 28 -97.91 -123.92 REMARK 500 ALA L 42 88.67 -56.98 REMARK 500 GLU L 52 20.17 33.54 REMARK 500 VAL L 53 102.43 64.99 REMARK 500 PRO L 57 -129.14 -90.78 REMARK 500 SER L 67 -138.70 -151.63 REMARK 500 LEU L 80 156.23 -49.50 REMARK 500 TYR L 93 -165.37 -77.25 REMARK 500 GLU L 94 -21.95 -147.14 REMARK 500 SER L 96 -70.96 47.39 REMARK 500 ASP L 97 -43.37 -137.96 REMARK 500 THR L 118 135.90 58.45 REMARK 500 PRO L 123 -175.98 -30.96 REMARK 500 GLN L 130 -74.49 -55.44 REMARK 500 ASN L 132 102.23 9.95 REMARK 500 LYS L 133 143.57 177.47 REMARK 500 ASP L 142 126.54 58.31 REMARK 500 TYR L 144 58.06 -142.49 REMARK 500 ASP L 155 18.39 80.13 REMARK 500 ALA L 161 159.54 161.39 REMARK 500 LYS L 167 139.01 -36.85 REMARK 500 LYS L 170 142.26 -32.04 REMARK 500 GLN L 171 -169.49 -103.72 REMARK 500 HIS L 201 87.49 -171.98 REMARK 500 LYS L 208 -108.08 -78.97 REMARK 500 THR L 209 119.51 53.36 REMARK 500 PRO L 212 33.11 -95.24 REMARK 500 THR L 213 -169.69 117.21 REMARK 500 CYS L 215 -163.10 25.25 REMARK 500 PRO H 14 116.72 -31.96 REMARK 500 SER H 15 38.76 136.20 REMARK 500 GLU H 16 -112.67 -151.03 REMARK 500 ILE H 29 -92.09 162.37 REMARK 500 ASN H 30 -71.85 80.12 REMARK 500 THR H 31 -47.28 -131.72 REMARK 500 ILE H 32 98.08 -67.92 REMARK 500 LEU H 33 -43.77 142.08 REMARK 500 TYR H 34 -130.98 -143.41 REMARK 500 PRO H 43 90.32 -66.20 REMARK 500 TYR H 55 -38.48 -33.10 REMARK 500 SER H 56 95.34 151.50 REMARK 500 SER H 58 97.19 -162.62 REMARK 500 PRO H 63 -12.26 -43.11 REMARK 500 SER H 64 -76.03 -84.72 REMARK 500 LEU H 65 36.08 -85.40 REMARK 500 SER H 67 -34.65 83.44 REMARK 500 ARG H 68 -78.99 -65.46 REMARK 500 REMARK 500 THIS ENTRY HAS 110 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 TYR L 144 PRO L 145 90.42 REMARK 500 PHE H 150 PRO H 151 -124.25 REMARK 500 GLN H 152 PRO H 153 -112.98 REMARK 500 TYR H 358 PRO H 359 -81.28 REMARK 500 PRO H 380 PRO H 381 -138.98 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 L 144 0.09 SIDE CHAIN REMARK 500 TYR H 54 0.08 SIDE CHAIN REMARK 500 TYR H 96 0.07 SIDE CHAIN REMARK 500 PHE H 126 0.08 SIDE CHAIN REMARK 500 TYR H 334 0.09 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 SER H 15 -12.39 REMARK 500 ALA H 17 16.72 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 GLU L 52 24.6 L L OUTSIDE RANGE REMARK 500 GLN L 112 24.4 L L OUTSIDE RANGE REMARK 500 PRO L 117 21.7 L L OUTSIDE RANGE REMARK 500 THR L 118 20.6 L L OUTSIDE RANGE REMARK 500 LEU L 139 24.9 L L OUTSIDE RANGE REMARK 500 THR L 209 23.1 L L OUTSIDE RANGE REMARK 500 SER L 216 23.3 L L OUTSIDE RANGE REMARK 500 SER H 15 19.6 L L OUTSIDE RANGE REMARK 500 LEU H 84 52.4 L L OUTSIDE RANGE REMARK 500 SER H 86 21.6 L L OUTSIDE RANGE REMARK 500 SER H 116 25.0 L L OUTSIDE RANGE REMARK 500 LEU H 220 22.9 L L OUTSIDE RANGE REMARK 500 ASP H 265 20.9 L L OUTSIDE RANGE REMARK 500 ASN H 282 24.2 L L OUTSIDE RANGE REMARK 500 VAL H 290 24.7 L L OUTSIDE RANGE REMARK 500 ARG H 329 16.1 L L OUTSIDE RANGE REMARK 500 GLU H 415 19.5 L L OUTSIDE RANGE REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: LC1 REMARK 800 EVIDENCE_CODE: AUTHOR REMARK 800 SITE_DESCRIPTION: ANTIGEN COMBINING SITE 1 IN CHAIN L REMARK 800 REMARK 800 SITE_IDENTIFIER: LC2 REMARK 800 EVIDENCE_CODE: AUTHOR REMARK 800 SITE_DESCRIPTION: ANTIGEN COMBINING SITE 2 IN CHAIN L REMARK 800 REMARK 800 SITE_IDENTIFIER: LC3 REMARK 800 EVIDENCE_CODE: AUTHOR REMARK 800 SITE_DESCRIPTION: ANTIGEN COMBINING SITE 3 IN CHAIN L REMARK 800 REMARK 800 SITE_IDENTIFIER: HC1 REMARK 800 EVIDENCE_CODE: AUTHOR REMARK 800 SITE_DESCRIPTION: ANTIGEN COMBINING SITE 1 IN CHAIN H REMARK 800 REMARK 800 SITE_IDENTIFIER: HC2 REMARK 800 EVIDENCE_CODE: AUTHOR REMARK 800 SITE_DESCRIPTION: ANTIGEN COMBINING SITE 2 IN CHAIN H REMARK 800 REMARK 800 SITE_IDENTIFIER: HC3 REMARK 800 EVIDENCE_CODE: AUTHOR REMARK 800 SITE_DESCRIPTION: ANTIGEN COMBINING SITE 3 IN CHAIN H REMARK 800 REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG H 429 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUL H 430 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG H 431 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA H 432 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN H 433 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG H 434 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL H 435 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA H 436 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GUP H 437 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG H 438 REMARK 999 REMARK 999 SEQUENCE REMARK 999 THE FOLLOWING TABLE MAY BE USED TO RELATE THE ENTRIES REMARK 999 SEQUENCE NUMBERING TO THE NUMBERING SYSTEM OF E.KABAT REMARK 999 (E.A.KABAT,T.T.WU,M.REID-MILLER,H.M.PERRY,K.S.GOTTESMAN, REMARK 999 SEQUENCES OF PROTEINS OF IMMUNOLOGICAL INTEREST, 4TH ED., REMARK 999 (1987), NATIONAL INSTITUTE OF HEALTH,BETHESDA,MD.). REMARK 999 REMARK 999 LIGHT CHAIN HEAVY CHAIN REMARK 999 REMARK 999 COMPUTER KABAT COMPUTER KABAT REMARK 999 FILE NUMBER FILE NUMBER REMARK 999 NUMBER NUMBER REMARK 999 REMARK 999 1-9 1-9 1-35 1-35 REMARK 999 10-26 11-27 36 35A REMARK 999 27 27A 37 35B REMARK 999 28 27B 38-84 36-82 REMARK 999 29 27C 85 82A REMARK 999 30-97 28-95 86 82B REMARK 999 110 106A 87 82C REMARK 999 111-172 107-168 88-103 83-98 REMARK 999 173-203 170-200 104 100K REMARK 999 204 203-215 105-134 101-130 REMARK 999 135-156 133-154 REMARK 999 157-158 158-159 REMARK 999 159-166 162-169 REMARK 999 167-177 171-181 REMARK 999 178-191 183-196 REMARK 999 192-194 198-200 REMARK 999 195-199 202-206 REMARK 999 200-216 208-224 REMARK 999 217-222 231-237 REMARK 999 (EU REMARK 999 NUMBERING) REMARK 999 223-428 238-443 REMARK 999 (EU REMARK 999 NUMBERING)