REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH T.FISCHMANN,H.SOUCHON,M.-M.RIOTTOT,D.TELLO, REMARK 1 AUTH 2 R.J.POLJAK REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY DIFFRACTION REMARK 1 TITL 2 STUDIES OF TWO ANTIGEN-ANTIBODY (LYSOZYME-FAB) REMARK 1 TITL 3 COMPLEXES REMARK 1 REF J.MOL.BIOL. V. 203 527 1988 REMARK 1 REFN ISSN 0022-2836 REMARK 2 REMARK 2 RESOLUTION. 2.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PROLSQ REMARK 3 AUTHORS : KONNERT,HENDRICKSON REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 7.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000 REMARK 3 COMPLETENESS FOR RANGE (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 42713 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) : 0.184 REMARK 3 R VALUE (WORKING SET) : NULL REMARK 3 FREE R VALUE : 0.282 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 : 8582 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 210 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.10 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) : 0.016 ; 0.020 REMARK 3 ANGLE DISTANCE (A) : 0.041 ; 0.030 REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.051 ; 0.050 REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL REMARK 3 REMARK 3 PLANE RESTRAINT (A) : 0.010 ; 0.020 REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 167.000; 0.150 REMARK 3 REMARK 3 NON-BONDED CONTACT RESTRAINTS. REMARK 3 SINGLE TORSION (A) : 0.220 ; 0.400 REMARK 3 MULTIPLE TORSION (A) : 0.270 ; 0.400 REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL REMARK 3 H-BOND (X-H...Y) (A) : 0.230 ; 0.400 REMARK 3 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS. REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL REMARK 3 PLANAR (DEGREES) : 5.400 ; 3.000 REMARK 3 STAGGERED (DEGREES) : 23.100; 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) : 0.860 ; 1.000 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.560 ; 1.500 REMARK 3 SIDE-CHAIN BOND (A**2) : 1.270 ; 1.500 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.040 ; 2.000 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: D44.1-HEL COMPLEX CRYSTALS HAVE TWO REMARK 3 FAB-HEL COMPLEXES IN THE ASYMMETRIC UNIT. COMPLEX NUMBER 1 REMARK 3 INCLUDES CHAIN A (VL AND CL DOMAINS), CHAIN B (VH AND CH1 REMARK 3 DOMAINS) AND CHAIN E (HEL). COMPLEX NUMBER 2 INCLUDES CHAIN C REMARK 3 (VL AND CL DOMAINS) CHAIN D (VH AND CH1 DOMAINS) AND CHAIN F REMARK 3 (HEL). THE CL C-TERMINAL RESIDUE CYS 214 OF COMPLEX NUMBER 1, REMARK 3 THE CL C-TERMINAL RESIDUES LYS 213 AND CYS 214 AND CH1 REMARK 3 RESIDUES GLY 130 - ASN 136, THR 195, AND VAL 214 HAVE NO REMARK 3 ELECTRON DENSITY AND HAVE BEEN ASSIGNED OCCUPANCIES OF 0.01. REMARK 3 IN ADDITION, THE 14 C-TERMINAL RESIDUES OF THE HEL OF COMPLEX REMARK 3 NUMBER 1 ARE POORLY RESOLVED. ATOMIC POSITIONS FOR ATOMS OF REMARK 3 THESE RESIDUES SHOULD BE CONSIDERED ARBITRARY. REMARK 4 REMARK 4 1MLC 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 : 1 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) : NULL 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 : XDS REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44729 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 (%) : 94.0 REMARK 200 DATA REDUNDANCY : 4.000 REMARK 200 R MERGE (I) : 0.10000 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 (%): 57.39 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.89 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 49.85000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 42.35000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 83.65000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 42.35000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 49.85000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 83.65000 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, F 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 400 REMARK 400 COMPOUND REMARK 400 REMARK 400 VL RESIDUE SER 30 IS IN THE SECOND POSITION OF A II'-TYPE REMARK 400 TURN. VL RESIDUE VAL 51 IS THE SECOND RESIDUE (I+1) OF A REMARK 400 MODIFIED GAMMA TURN (CLASS 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 SER D 189 OG SER D 193 2.15 REMARK 500 O ASP D 90 OH TYR D 94 2.16 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 GLY B 101 N GLY B 101 CA 0.099 REMARK 500 GLY D 101 N GLY D 101 CA 0.108 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 A 17 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES REMARK 500 ASN A 31 N - CA - CB ANGL. DEV. = -11.5 DEGREES REMARK 500 LEU A 33 CB - CG - CD2 ANGL. DEV. = -11.0 DEGREES REMARK 500 TYR A 36 CB - CG - CD2 ANGL. DEV. = 3.7 DEGREES REMARK 500 TYR A 36 CB - CG - CD1 ANGL. DEV. = -4.4 DEGREES REMARK 500 ARG A 45 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 ARG A 45 NE - CZ - NH2 ANGL. DEV. = -4.4 DEGREES REMARK 500 LEU A 46 CA - CB - CG ANGL. DEV. = 13.9 DEGREES REMARK 500 ARG A 61 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES REMARK 500 ASP A 82 CB - CG - OD1 ANGL. DEV. = -8.7 DEGREES REMARK 500 ARG A 96 NE - CZ - NH2 ANGL. DEV. = 4.5 DEGREES REMARK 500 LYS A 103 N - CA - CB ANGL. DEV. = -11.1 DEGREES REMARK 500 ARG A 108 NE - CZ - NH1 ANGL. DEV. = 5.3 DEGREES REMARK 500 ARG A 108 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES REMARK 500 ASP A 110 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES REMARK 500 ARG A 155 NE - CZ - NH2 ANGL. DEV. = 3.7 DEGREES REMARK 500 ASP A 165 CA - CB - CG ANGL. DEV. = 13.3 DEGREES REMARK 500 TYR A 186 CB - CG - CD2 ANGL. DEV. = 3.8 DEGREES REMARK 500 ARG A 188 NE - CZ - NH2 ANGL. DEV. = -6.5 DEGREES REMARK 500 GLU A 195 OE1 - CD - OE2 ANGL. DEV. = 10.5 DEGREES REMARK 500 ARG A 211 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES REMARK 500 ARG A 211 NE - CZ - NH2 ANGL. DEV. = -8.4 DEGREES REMARK 500 TYR B 27 CB - CG - CD2 ANGL. DEV. = -4.8 DEGREES REMARK 500 TYR B 27 CB - CG - CD1 ANGL. DEV. = 3.7 DEGREES REMARK 500 ARG B 40 NE - CZ - NH1 ANGL. DEV. = 10.2 DEGREES REMARK 500 ARG B 40 NE - CZ - NH2 ANGL. DEV. = -7.2 DEGREES REMARK 500 TYR B 59 CB - CG - CD2 ANGL. DEV. = 4.8 DEGREES REMARK 500 TYR B 59 CB - CG - CD1 ANGL. DEV. = -5.2 DEGREES REMARK 500 LEU B 83 CA - CB - CG ANGL. DEV. = 17.2 DEGREES REMARK 500 ARG B 98 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES REMARK 500 GLY B 101 N - CA - C ANGL. DEV. = -15.3 DEGREES REMARK 500 GLU B 151 OE1 - CD - OE2 ANGL. DEV. = 9.4 DEGREES REMARK 500 ASP B 176 CB - CG - OD1 ANGL. DEV. = -6.4 DEGREES REMARK 500 ARG B 216 NE - CZ - NH1 ANGL. DEV. = -6.9 DEGREES REMARK 500 ARG B 216 NE - CZ - NH2 ANGL. DEV. = 5.7 DEGREES REMARK 500 ASP B 217 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES REMARK 500 ASP C 17 CA - CB - CG ANGL. DEV. = 18.6 DEGREES REMARK 500 ASP C 17 CB - CG - OD1 ANGL. DEV. = 12.2 DEGREES REMARK 500 ASP C 17 CB - CG - OD2 ANGL. DEV. = -6.5 DEGREES REMARK 500 ASN C 31 CB - CA - C ANGL. DEV. = 12.9 DEGREES REMARK 500 ARG C 45 CD - NE - CZ ANGL. DEV. = -8.9 DEGREES REMARK 500 ARG C 45 NE - CZ - NH1 ANGL. DEV. = -6.7 DEGREES REMARK 500 ARG C 45 NE - CZ - NH2 ANGL. DEV. = 3.3 DEGREES REMARK 500 SER C 54 N - CA - CB ANGL. DEV. = 10.0 DEGREES REMARK 500 GLU C 79 OE1 - CD - OE2 ANGL. DEV. = 7.7 DEGREES REMARK 500 ARG C 96 CD - NE - CZ ANGL. DEV. = -9.1 DEGREES REMARK 500 GLU C 105 CA - CB - CG ANGL. DEV. = 13.6 DEGREES REMARK 500 ARG C 108 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES REMARK 500 ARG C 108 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES REMARK 500 ASP C 110 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 105 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 SER A 30 -116.48 59.16 REMARK 500 ASN A 32 52.27 -114.29 REMARK 500 HIS A 41 -56.99 101.49 REMARK 500 VAL A 51 -29.86 67.67 REMARK 500 SER A 52 8.00 -160.71 REMARK 500 SER A 67 147.44 164.38 REMARK 500 SER A 77 94.36 58.62 REMARK 500 SER A 201 129.37 -177.82 REMARK 500 ALA B 16 -168.07 -78.72 REMARK 500 THR B 28 97.19 -68.24 REMARK 500 ALA B 92 -176.05 -171.32 REMARK 500 ALA B 132 178.15 64.73 REMARK 500 ALA B 133 -73.97 68.72 REMARK 500 GLN B 134 -81.36 -14.99 REMARK 500 ASN B 136 -165.93 -69.83 REMARK 500 ASP B 176 -20.57 89.61 REMARK 500 PRO B 190 -79.16 -61.72 REMARK 500 ALA B 204 -15.54 -41.29 REMARK 500 SER B 205 21.30 -150.64 REMARK 500 SER B 206 -7.78 67.12 REMARK 500 SER C 28 82.24 -64.26 REMARK 500 SER C 30 -122.16 61.75 REMARK 500 ASN C 32 73.73 -103.67 REMARK 500 SER C 40 117.73 -32.03 REMARK 500 HIS C 41 16.08 80.11 REMARK 500 VAL C 51 -43.14 71.25 REMARK 500 SER C 52 10.15 -145.11 REMARK 500 SER C 67 106.89 117.41 REMARK 500 SER C 77 64.40 68.04 REMARK 500 SER C 116 100.21 -163.67 REMARK 500 PRO C 120 153.42 -34.15 REMARK 500 ASN C 138 71.13 45.17 REMARK 500 ILE C 144 135.95 -171.12 REMARK 500 ASP C 151 63.37 16.78 REMARK 500 GLN C 156 -46.53 -141.41 REMARK 500 SER C 171 11.26 52.41 REMARK 500 ASN C 190 -50.78 -125.46 REMARK 500 THR C 193 130.00 -27.43 REMARK 500 THR C 202 6.23 -159.66 REMARK 500 SER C 203 128.84 -177.51 REMARK 500 GLU C 213 96.28 159.84 REMARK 500 ALA D 9 129.64 -29.92 REMARK 500 HIS D 43 -164.74 -120.49 REMARK 500 ASP D 73 68.98 -162.74 REMARK 500 ASN D 77 33.56 38.09 REMARK 500 GLU D 89 -5.51 -59.66 REMARK 500 ALA D 92 178.23 174.26 REMARK 500 THR D 120 107.29 -172.42 REMARK 500 PRO D 129 97.52 -40.09 REMARK 500 SER D 131 -60.86 90.88 REMARK 500 ALA D 133 102.21 -31.15 REMARK 500 THR D 135 49.42 -75.27 REMARK 500 PRO D 150 -151.58 -85.37 REMARK 500 ASN D 158 -59.61 71.19 REMARK 500 SER D 159 156.69 160.29 REMARK 500 LEU D 162 79.58 -53.01 REMARK 500 SER D 164 -103.76 -61.95 REMARK 500 GLN D 174 -71.17 -75.31 REMARK 500 SER D 175 72.53 -154.81 REMARK 500 ASP D 176 -10.56 89.03 REMARK 500 GLU D 194 -144.70 -103.81 REMARK 500 HIS D 202 78.01 -153.96 REMARK 500 SER D 206 85.18 41.36 REMARK 500 ARG D 216 96.31 -20.54 REMARK 500 ALA E 9 -37.94 -29.76 REMARK 500 ASN E 19 17.18 58.95 REMARK 500 GLU E 35 -85.97 -75.71 REMARK 500 THR E 47 42.82 -108.87 REMARK 500 ASN E 77 70.96 24.31 REMARK 500 ILE E 88 13.90 -51.48 REMARK 500 SER E 100 -41.52 -18.55 REMARK 500 ASP E 101 28.93 -69.56 REMARK 500 MET E 105 1.12 -69.35 REMARK 500 VAL E 109 -60.10 -20.62 REMARK 500 ASN E 113 -12.44 168.59 REMARK 500 ARG E 114 -14.19 -140.93 REMARK 500 CYS E 115 46.00 -148.51 REMARK 500 THR E 118 -110.48 35.79 REMARK 500 ASP E 119 41.67 -164.18 REMARK 500 VAL E 120 -27.59 -37.16 REMARK 500 ARG F 21 22.67 45.06 REMARK 500 GLU F 35 -71.43 -68.08 REMARK 500 PHE F 38 29.53 47.82 REMARK 500 ASN F 46 -158.80 -103.62 REMARK 500 ARG F 68 10.80 -154.93 REMARK 500 ASN F 77 85.52 38.35 REMARK 500 ILE F 78 133.46 -179.39 REMARK 500 SER F 100 1.87 -68.67 REMARK 500 ASN F 103 13.19 -149.69 REMARK 500 THR F 118 164.09 -35.43 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 A 108 0.10 SIDE_CHAIN REMARK 500 ARG E 68 0.12 SIDE_CHAIN REMARK 500 ARG F 5 0.10 SIDE_CHAIN 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 B1701 DISTANCE = 5.46 ANGSTROMS