REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH T.GALLAGHER,P.ALEXANDER,P.BRYAN,G.L.GILLILAND REMARK 1 TITL TWO CRYSTAL STRUCTURES OF THE B1 REMARK 1 TITL 2 IMMUNOGLOBULIN-BINDING DOMAIN OF STREPTOCOCCAL REMARK 1 TITL 3 PROTEIN G AND COMPARISON WITH NMR REMARK 1 REF BIOCHEMISTRY V. 33 4721 1994 REMARK 1 REFN ISSN 0006-2960 REMARK 1 REFERENCE 2 REMARK 1 AUTH J.P.DERRICK,D.B.WIGLEY REMARK 1 TITL CRYSTAL STRUCTURE OF A STREPTOCOCCAL PROTEIN G REMARK 1 TITL 2 DOMAIN BOUND TO AN FAB FRAGMENT REMARK 1 REF NATURE V. 359 752 1992 REMARK 1 REFN ISSN 0028-0836 REMARK 1 REFERENCE 3 REMARK 1 AUTH J.P.DERRICK,G.J.DAVIES,Z.DAUTER,K.S.WILSON, REMARK 1 AUTH 2 D.B.WIGLEY REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY ANALYSIS OF THE REMARK 1 TITL 2 COMPLEX BETWEEN A MOUSE FAB FRAGMENT AND A SINGLE REMARK 1 TITL 3 IGG-BINDING DOMAIN FROM STREPTOCOCCAL PROTEIN G REMARK 1 REF J.MOL.BIOL. V. 227 1253 1992 REMARK 1 REFN ISSN 0022-2836 REMARK 1 REFERENCE 4 REMARK 1 AUTH L.-Y.LIAN,J.P.DERRICK,M.J.SUTCLIFF,J.C.YANG, REMARK 1 AUTH 2 G.C.K.ROBERTS REMARK 1 TITL DETERMINATION OF THE SOLUTION STRUCTURES OF REMARK 1 TITL 2 DOMAINS II AND III OF PROTEIN G FROM STREPTOCOCCUS REMARK 1 TITL 3 BY 1H NUCLEAR MAGNETIC RESONANCE REMARK 1 REF J.MOL.BIOL. V. 228 1219 1992 REMARK 1 REFN ISSN 0022-2836 REMARK 1 REFERENCE 5 REMARK 1 AUTH A.ACHARI,S.P.HALE,A.J.HOWARD,G.M.CLORE, REMARK 1 AUTH 2 A.M.GRONENBORN,K.D.HARDMAN,M.WHITLOW REMARK 1 TITL 1.67 ANGSTROMS X-RAY STRUCTURE OF THE B2 REMARK 1 TITL 2 IMMUNOGLOBULIN-BINDING DOMAIN OF STREPTOCOCCAL REMARK 1 TITL 3 PROTEIN G AND COMPARISON TO THE NMR STRUCTURE OF REMARK 1 TITL 4 THE B1 DOMAIN REMARK 1 REF BIOCHEMISTRY V. 31 10449 1992 REMARK 1 REFN ISSN 0006-2960 REMARK 1 REFERENCE 6 REMARK 1 AUTH A.M.GRONENBORN,D.R.FILPULA,N.Z.ESSIG,A.ACHARI, REMARK 1 AUTH 2 M.WHITLOW,P.T.WINGFIELD,G.M.CLORE REMARK 1 TITL A NOVEL, HIGHLY STABLE FOLD OF THE IMMUNOGLOBULIN REMARK 1 TITL 2 BINDING DOMAIN OF STREPTOCOCCAL PROTEIN G REMARK 1 REF SCIENCE V. 253 657 1991 REMARK 1 REFN ISSN 0036-8075 REMARK 2 REMARK 2 RESOLUTION. 2.60 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PROLSQ, X-PLOR REMARK 3 AUTHORS : KONNERT,HENDRICKSON REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 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 + TEST SET) : 0.168 REMARK 3 R VALUE (WORKING SET) : NULL 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) : NULL 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 : 3772 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 345 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.80 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) : 0.015 ; 0.020 REMARK 3 ANGLE DISTANCE (A) : 0.056 ; 0.040 REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.077 ; 0.060 REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL REMARK 3 REMARK 3 PLANE RESTRAINT (A) : 0.012 ; 0.020 REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.133 ; 0.120 REMARK 3 REMARK 3 NON-BONDED CONTACT RESTRAINTS. REMARK 3 SINGLE TORSION (A) : 0.236 ; 0.500 REMARK 3 MULTIPLE TORSION (A) : 0.321 ; 0.500 REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL REMARK 3 H-BOND (X-H...Y) (A) : 0.286 ; 0.500 REMARK 3 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS. REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL REMARK 3 PLANAR (DEGREES) : 2.560 ; 5.000 REMARK 3 STAGGERED (DEGREES) : 25.040; 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) : 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 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1IGC 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 : APR-92 REMARK 200 TEMPERATURE (KELVIN) : NULL REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : EMBL/DESY HAMBURG 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) : 1.0 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 : 17204 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 (%) : 98.7 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : 0.07900 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 (%): 51.26 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52 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 32.25000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 60.05000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.25000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 60.05000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.25000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.25000 REMARK 290 SMTRY3 4 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, A 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 450 REMARK 450 SOURCE REMARK 450 REMARK 450 MOPC21 (IGG1 KAPPA) WAS ISOLATED FROM ASCITES FLUID, REMARK 450 GENERATED BY A MINERAL OIL-INDUCED PLASMACYTOMA. THE REMARK 450 PRODUCT WAS OBTAINED COMMERCIALLY (SIGMA PRODUCT NUMBER REMARK 450 M7894). FAB FRAGMENT WAS GENERATED BY PROTEOLYSIS OF REMARK 450 INTACT IGG1 AS DESCRIBED BY DERRICK ET AL., 1992 REMARK 450 (REFERENCE 3 ABOVE). PROTEIN G: SEE LIAN ET AL. 1992 REMARK 450 FOR DETAILS (REFERENCE 4 ABOVE). 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 MET A 1 REMARK 465 THR A 2 REMARK 465 PRO A 3 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 O TYR L 191 O SER L 207 1.80 REMARK 500 O ILE L 150 O SER L 190 1.84 REMARK 500 O VAL L 30 O SER L 67 1.89 REMARK 500 O GLY H 134 NH2 ARG H 195 2.07 REMARK 500 O VAL L 33 O GLY L 50 2.10 REMARK 500 NH2 ARG L 61 OD2 ASP L 82 2.12 REMARK 500 O SER H 119 O HOH H 237 2.14 REMARK 500 O HOH H 262 O HOH H 319 2.15 REMARK 500 O TRP H 99 O ALA H 106 2.15 REMARK 500 N ASP L 166 O THR L 171 2.19 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 PRO L 141 CD PRO L 141 N 0.098 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 ASN L 1 CA - CB - CG ANGL. DEV. = 15.8 DEGREES REMARK 500 SER L 12 CB - CA - C ANGL. DEV. = -12.7 DEGREES REMARK 500 SER L 12 N - CA - CB ANGL. DEV. = 10.8 DEGREES REMARK 500 CYS L 23 CB - CA - C ANGL. DEV. = 9.6 DEGREES REMARK 500 VAL L 30 CB - CA - C ANGL. DEV. = 13.1 DEGREES REMARK 500 GLN L 37 CA - CB - CG ANGL. DEV. = 13.7 DEGREES REMARK 500 GLU L 41 CA - C - O ANGL. DEV. = 14.0 DEGREES REMARK 500 GLU L 41 CA - C - N ANGL. DEV. = -13.9 DEGREES REMARK 500 GLN L 42 C - N - CA ANGL. DEV. = 16.2 DEGREES REMARK 500 GLY L 50 CA - C - O ANGL. DEV. = -11.6 DEGREES REMARK 500 GLY L 50 CA - C - N ANGL. DEV. = 15.1 DEGREES REMARK 500 ARG L 61 N - CA - CB ANGL. DEV. = 12.7 DEGREES REMARK 500 ARG L 61 CD - NE - CZ ANGL. DEV. = -10.8 DEGREES REMARK 500 SER L 77 O - C - N ANGL. DEV. = 10.1 DEGREES REMARK 500 ALA L 80 CB - CA - C ANGL. DEV. = 9.2 DEGREES REMARK 500 GLU L 81 CB - CG - CD ANGL. DEV. = 16.4 DEGREES REMARK 500 GLU L 81 CG - CD - OE1 ANGL. DEV. = 12.1 DEGREES REMARK 500 CYS L 88 CA - CB - SG ANGL. DEV. = 6.8 DEGREES REMARK 500 SER L 93 N - CA - CB ANGL. DEV. = -10.6 DEGREES REMARK 500 ARG L 108 CG - CD - NE ANGL. DEV. = -14.5 DEGREES REMARK 500 ASP L 110 CB - CG - OD1 ANGL. DEV. = -9.0 DEGREES REMARK 500 ASP L 110 CB - CG - OD2 ANGL. DEV. = 8.7 DEGREES REMARK 500 VAL L 133 CA - CB - CG1 ANGL. DEV. = 16.5 DEGREES REMARK 500 ASN L 137 CA - CB - CG ANGL. DEV. = 16.3 DEGREES REMARK 500 TYR L 140 CA - C - O ANGL. DEV. = -15.1 DEGREES REMARK 500 PRO L 141 CA - N - CD ANGL. DEV. = -23.7 DEGREES REMARK 500 PRO L 141 N - CA - CB ANGL. DEV. = 23.3 DEGREES REMARK 500 PRO L 141 N - CD - CG ANGL. DEV. = 17.2 DEGREES REMARK 500 TYR L 140 CA - C - N ANGL. DEV. = -17.5 DEGREES REMARK 500 TYR L 140 O - C - N ANGL. DEV. = 34.2 DEGREES REMARK 500 PRO L 141 C - N - CA ANGL. DEV. = 49.9 DEGREES REMARK 500 PRO L 141 C - N - CD ANGL. DEV. = -31.4 DEGREES REMARK 500 ASP L 151 CB - CA - C ANGL. DEV. = 12.3 DEGREES REMARK 500 SER L 152 N - CA - CB ANGL. DEV. = 12.6 DEGREES REMARK 500 ARG L 154 N - CA - CB ANGL. DEV. = -13.6 DEGREES REMARK 500 ARG L 154 CD - NE - CZ ANGL. DEV. = -9.6 DEGREES REMARK 500 ARG L 154 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES REMARK 500 ARG L 154 N - CA - C ANGL. DEV. = 19.5 DEGREES REMARK 500 ARG L 154 C - N - CA ANGL. DEV. = 23.9 DEGREES REMARK 500 GLN L 155 N - CA - C ANGL. DEV. = 18.5 DEGREES REMARK 500 ASP L 166 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES REMARK 500 ASP L 169 CB - CG - OD2 ANGL. DEV. = 6.4 DEGREES REMARK 500 SER L 173 N - CA - CB ANGL. DEV. = 10.2 DEGREES REMARK 500 MET L 174 CG - SD - CE ANGL. DEV. = -10.3 DEGREES REMARK 500 SER L 176 N - CA - CB ANGL. DEV. = 9.6 DEGREES REMARK 500 THR L 181 N - CA - CB ANGL. DEV. = 12.2 DEGREES REMARK 500 ARG L 187 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES REMARK 500 SER L 190 N - CA - CB ANGL. DEV. = 10.7 DEGREES REMARK 500 THR L 196 N - CA - CB ANGL. DEV. = 15.8 DEGREES REMARK 500 SER L 207 N - CA - C ANGL. DEV. = 16.4 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 LYS L 9 -33.75 123.89 REMARK 500 MET L 11 139.50 -174.32 REMARK 500 VAL L 30 -121.89 48.58 REMARK 500 PRO L 40 111.81 -38.44 REMARK 500 GLU L 41 91.03 20.69 REMARK 500 LEU L 47 -50.80 -122.63 REMARK 500 ASP L 60 9.01 -54.43 REMARK 500 SER L 67 -69.22 -134.24 REMARK 500 ASP L 82 8.43 -42.83 REMARK 500 ALA L 84 -173.81 179.78 REMARK 500 ASN L 138 61.63 62.45 REMARK 500 PHE L 139 -127.30 -91.81 REMARK 500 TYR L 140 110.56 129.38 REMARK 500 PRO L 141 140.47 144.03 REMARK 500 ILE L 150 -80.28 -42.43 REMARK 500 SER L 152 37.08 -174.58 REMARK 500 GLN L 155 -149.10 -127.34 REMARK 500 ASN L 156 -14.18 -154.27 REMARK 500 ASP L 169 73.91 -114.91 REMARK 500 SER L 170 39.20 -20.42 REMARK 500 GLU L 184 -62.83 -175.47 REMARK 500 GLU L 186 -72.19 -58.30 REMARK 500 ARG L 187 34.31 -66.10 REMARK 500 ASN L 189 -45.95 -149.24 REMARK 500 LYS L 198 16.54 -52.79 REMARK 500 SER L 207 -119.27 -55.15 REMARK 500 PHE L 208 107.34 47.01 REMARK 500 ARG L 210 103.67 -43.63 REMARK 500 ASN L 211 68.37 -105.83 REMARK 500 PHE H 29 -79.30 -20.16 REMARK 500 SER H 30 11.70 -55.62 REMARK 500 LYS H 43 -174.13 139.31 REMARK 500 LYS H 76 41.23 -104.75 REMARK 500 ASN H 77 62.99 21.48 REMARK 500 THR H 84 55.93 -154.98 REMARK 500 SER H 85 32.55 178.60 REMARK 500 LEU H 86 122.72 -38.65 REMARK 500 TRP H 99 -85.90 -66.19 REMARK 500 TYR H 104 96.19 -61.54 REMARK 500 TYR H 105 58.80 -118.80 REMARK 500 SER H 135 88.41 -161.48 REMARK 500 ALA H 136 97.19 177.70 REMARK 500 ALA H 137 98.17 -44.75 REMARK 500 SER H 141 -20.59 167.74 REMARK 500 PHE H 153 131.88 -176.09 REMARK 500 SER H 168 -85.73 -35.98 REMARK 500 PRO H 174 151.77 -46.35 REMARK 500 SER H 179 84.33 -159.79 REMARK 500 SER H 193 -81.25 -40.28 REMARK 500 HIS H 206 86.03 -151.82 REMARK 500 ARG H 220 31.84 -81.00 REMARK 500 ASP H 221 86.14 -38.55 REMARK 500 THR A 6 115.32 159.19 REMARK 500 VAL A 26 -74.82 -87.17 REMARK 500 TYR A 50 127.22 -171.00 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 A 63 DISTANCE = 5.13 ANGSTROMS REMARK 525 HOH A 74 DISTANCE = 6.72 ANGSTROMS REMARK 525 HOH L 228 DISTANCE = 5.33 ANGSTROMS REMARK 525 HOH L 229 DISTANCE = 9.19 ANGSTROMS REMARK 525 HOH A 78 DISTANCE = 6.52 ANGSTROMS REMARK 525 HOH H 246 DISTANCE = 6.59 ANGSTROMS REMARK 525 HOH L 237 DISTANCE = 5.53 ANGSTROMS REMARK 525 HOH L 238 DISTANCE = 6.51 ANGSTROMS REMARK 525 HOH A 88 DISTANCE = 5.35 ANGSTROMS REMARK 525 HOH L 240 DISTANCE = 5.34 ANGSTROMS REMARK 525 HOH L 243 DISTANCE = 6.35 ANGSTROMS REMARK 525 HOH H 258 DISTANCE = 5.40 ANGSTROMS REMARK 525 HOH L 254 DISTANCE = 5.18 ANGSTROMS REMARK 525 HOH L 256 DISTANCE = 5.52 ANGSTROMS REMARK 525 HOH L 257 DISTANCE = 8.69 ANGSTROMS REMARK 525 HOH L 262 DISTANCE = 7.28 ANGSTROMS REMARK 525 HOH H 278 DISTANCE = 7.03 ANGSTROMS REMARK 525 HOH L 271 DISTANCE = 5.65 ANGSTROMS REMARK 525 HOH H 288 DISTANCE = 5.79 ANGSTROMS REMARK 525 HOH H 292 DISTANCE = 5.48 ANGSTROMS REMARK 525 HOH L 283 DISTANCE = 5.34 ANGSTROMS REMARK 525 HOH H 297 DISTANCE = 7.07 ANGSTROMS REMARK 525 HOH H 300 DISTANCE = 5.26 ANGSTROMS REMARK 525 HOH L 292 DISTANCE = 5.72 ANGSTROMS REMARK 525 HOH H 302 DISTANCE = 5.59 ANGSTROMS REMARK 525 HOH L 293 DISTANCE = 7.70 ANGSTROMS REMARK 525 HOH L 294 DISTANCE = 7.67 ANGSTROMS REMARK 525 HOH H 306 DISTANCE = 6.99 ANGSTROMS REMARK 525 HOH H 308 DISTANCE = 5.70 ANGSTROMS REMARK 525 HOH H 310 DISTANCE = 5.32 ANGSTROMS REMARK 525 HOH H 311 DISTANCE = 5.16 ANGSTROMS REMARK 525 HOH H 315 DISTANCE = 8.89 ANGSTROMS REMARK 525 HOH H 317 DISTANCE = 7.98 ANGSTROMS REMARK 525 HOH H 320 DISTANCE = 7.60 ANGSTROMS REMARK 525 HOH H 321 DISTANCE = 7.73 ANGSTROMS REMARK 525 HOH L 312 DISTANCE = 5.05 ANGSTROMS REMARK 525 HOH H 323 DISTANCE = 7.22 ANGSTROMS REMARK 525 HOH L 320 DISTANCE = 8.19 ANGSTROMS REMARK 525 HOH H 330 DISTANCE = 5.53 ANGSTROMS REMARK 525 HOH L 322 DISTANCE = 6.69 ANGSTROMS REMARK 525 HOH H 336 DISTANCE = 5.79 ANGSTROMS REMARK 525 HOH L 327 DISTANCE = 5.93 ANGSTROMS REMARK 525 HOH H 337 DISTANCE = 7.31 ANGSTROMS REMARK 525 HOH H 338 DISTANCE = 5.96 ANGSTROMS REMARK 525 HOH H 341 DISTANCE = 8.24 ANGSTROMS REMARK 525 HOH L 333 DISTANCE = 7.85 ANGSTROMS REMARK 525 HOH L 334 DISTANCE = 6.82 ANGSTROMS REMARK 525 HOH L 335 DISTANCE = 9.42 ANGSTROMS REMARK 525 HOH L 336 DISTANCE = 6.30 ANGSTROMS REMARK 525 HOH H 346 DISTANCE = 5.97 ANGSTROMS REMARK 525 HOH L 342 DISTANCE = 8.63 ANGSTROMS REMARK 525 HOH H 352 DISTANCE = 6.16 ANGSTROMS REMARK 525 HOH L 352 DISTANCE = 5.88 ANGSTROMS REMARK 525 HOH L 353 DISTANCE = 5.59 ANGSTROMS REMARK 525 HOH L 357 DISTANCE = 6.77 ANGSTROMS REMARK 525 HOH H 367 DISTANCE = 5.01 ANGSTROMS REMARK 525 HOH L 361 DISTANCE = 7.30 ANGSTROMS REMARK 525 HOH L 364 DISTANCE = 5.32 ANGSTROMS REMARK 525 HOH L 365 DISTANCE = 8.21 ANGSTROMS REMARK 525 HOH L 366 DISTANCE = 6.83 ANGSTROMS REMARK 525 HOH L 375 DISTANCE = 5.99 ANGSTROMS REMARK 999 REMARK 999 SEQUENCE REMARK 999 REMARK 999 THERE ARE NO RESIDUES MISSING FROM THE LIGHT CHAIN. THERE REMARK 999 ARE NO RESIDUES MISSING FROM THE N TERMINUS OF THE HEAVY REMARK 999 CHAIN. THE SITE OF PROTEOLYSIS AT THE C TERMINUS OF THE REMARK 999 HEAVY CHAIN IS UNDEFINED, SO IT IS NOT KNOWN WHETHER THERE REMARK 999 ARE ANY RESIDUES MISSING THERE. THE FIRST THREE RESIDUES REMARK 999 ARE MISSING FROM THE N TERMINUS OF PROTEIN G DOMAIN III: REMARK 999 MET A 1, THR A 2, AND PRO A 3.