REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH J.A.BECKINGHAM,S.P.BOTTOMLEY,R.HINTON,B.J.SUTTON, REMARK 1 AUTH 2 M.G.GORE REMARK 1 TITL INTERACTIONS BETWEEN A SINGLE IMMUNOGLOBULIN- REMARK 1 TITL 2 BINDING DOMAIN OF PROTEIN L FROM REMARK 1 TITL 3 PEPTOSTREPTOCOCCUS MAGNUS AND A HUMAN KAPPA LIGHT REMARK 1 TITL 4 CHAIN REMARK 1 REF BIOCHEM.J. V. 340 193 1999 REMARK 1 REFN ISSN 0264-6021 REMARK 1 PMID 10229674 REMARK 1 DOI 10.1042/0264-6021:3400193 REMARK 1 REFERENCE 2 REMARK 1 AUTH M.GRAILLE,E.A.STURA,A.L.CORPER,B.J.SUTTON, REMARK 1 AUTH 2 M.J.TAUSSIG,J.B.CHARBONNIER,G.J.SILVERMAN REMARK 1 TITL CRYSTAL STRUCTURE OF A STAPHYLOCOCCUS AUREUS REMARK 1 TITL 2 PROTEIN A DOMAIN COMPLEXED WITH THE FAB FRAGMENT REMARK 1 TITL 3 OF A HUMAN IGM ANTIBODY: STRUCTURAL BASIS FOR REMARK 1 TITL 4 RECOGNITION OF B-CELL RECEPTORS AND SUPERANTIGEN REMARK 1 TITL 5 ACTIVITY REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 97 5399 2000 REMARK 1 REFN ISSN 0027-8424 REMARK 1 PMID 10805799 REMARK 1 DOI 10.1073/PNAS.97.10.5399 REMARK 1 REFERENCE 3 REMARK 1 AUTH S.P.BOTTOMLEY,J.A.BECKINGHAM,J.P.MURPHY,M.ATKINSON, REMARK 1 AUTH 2 T.ATKINSON,R.J.HINTON,M.G.GORE REMARK 1 TITL CLONING, EXPRESSION AND PURIFICATION OF PPL-1, A REMARK 1 TITL 2 KAPPA-CHAIN BINDING PROTEIN, BASED UPON PROTEIN L REMARK 1 TITL 3 FROM PEPTOSTREPTOCOCCUS MAGNUS REMARK 1 REF BIOSEPARATION V. 5 359 1995 REMARK 1 REFN REMARK 1 PMID 8767928 REMARK 2 REMARK 2 RESOLUTION. 2.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.0 REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU, REMARK 3 : READ,RICE,SIMONSON,WARREN REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 2 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000 REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 84.5 REMARK 3 NUMBER OF REFLECTIONS : 24298 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING SET) : 0.215 REMARK 3 FREE R VALUE : 0.278 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0 REMARK 3 FREE R VALUE TEST SET COUNT : 1192 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 23 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.7 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.74 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 819 REMARK 3 BIN R VALUE (WORKING SET) : 0.3132 REMARK 3 BIN FREE R VALUE : 0.348 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 42 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 : 6936 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 10 REMARK 3 SOLVENT ATOMS : 112 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 59.53 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.5 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) : 0.34 REMARK 3 ESD FROM SIGMAA (A) : NULL REMARK 3 LOW RESOLUTION CUTOFF (A) : 6.00 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) : 0.0074 REMARK 3 BOND ANGLES (DEGREES) : 1.423 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 BULK SOLVENT MODELING. REMARK 3 METHOD USED : NULL REMARK 3 KSOL : 0.293557 REMARK 3 BSOL : 22.3753 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 : PROTEIN_REP.PARAM REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM REMARK 3 PARAMETER FILE 3 : IMIDAZOLE.PARAM REMARK 3 PARAMETER FILE 4 : NULL REMARK 3 TOPOLOGY FILE 1 : NULL REMARK 3 TOPOLOGY FILE 2 : NULL REMARK 3 TOPOLOGY FILE 3 : NULL REMARK 3 TOPOLOGY FILE 4 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: SIDE CHAIN ATOMS FROM RESIDUES LYS A REMARK 3 45, LYS A 169, GLU B 89, LEU C 54, LYS C 107, GLU D 89, GLN D REMARK 3 113, GLU D 136, ARG D 181, LYS E 833 AND LYS E 878 ARE NOT REMARK 3 DEFINED BY ELECTRONIC DENSITY REMARK 4 REMARK 4 1HEZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-NOV-00. REMARK 100 THE PDBE ID CODE IS EBI-5583. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-OCT-99 REMARK 200 TEMPERATURE (KELVIN) : 120.0 REMARK 200 PH : 8.50 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : LURE REMARK 200 BEAMLINE : DW32 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.962 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : 345 IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26811 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700 REMARK 200 RESOLUTION RANGE LOW (A) : 20.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 95.2 REMARK 200 DATA REDUNDANCY : 4.660 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.11200 REMARK 200 FOR THE DATA SET : 12.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.78 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.6 REMARK 200 DATA REDUNDANCY IN SHELL : 5.00 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.37400 REMARK 200 FOR SHELL : 2.900 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: AMORE REMARK 200 STARTING MODEL: 1DEE REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 63.1 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 13-16% MPEG 5000, REMARK 280 100MM IMIDAZOLE MALATE, PH8.5 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 27.59250 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 105.26900 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.66750 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 105.26900 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.59250 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.66750 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 GENERATING THE BIOMOLECULE 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC REMARK 350 SOFTWARE USED: PQS REMARK 350 TOTAL BURIED SURFACE AREA: 11780 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 48480 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -69.6 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, C, D 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 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 GLU B 136 REMARK 465 ASN B 137 REMARK 465 SER B 138 REMARK 465 ASN B 139 REMARK 465 PRO B 140 REMARK 465 SER B 141 REMARK 465 SER B 142 REMARK 465 THR B 143 REMARK 465 LYS B 196 REMARK 465 ASP B 197 REMARK 465 VAL B 198 REMARK 465 ALA B 199 REMARK 465 GLN B 200 REMARK 465 GLY B 201 REMARK 465 THR B 202 REMARK 465 ASN B 203 REMARK 465 GLU B 204 REMARK 465 SER D 138 REMARK 465 ASN D 139 REMARK 465 PRO D 140 REMARK 465 SER D 141 REMARK 465 LYS D 196 REMARK 465 ASP D 197 REMARK 465 VAL D 198 REMARK 465 ALA D 199 REMARK 465 GLN D 200 REMARK 465 GLY D 201 REMARK 465 THR D 202 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LYS A 45 CG CD CE NZ REMARK 470 LYS A 169 CG CD CE NZ REMARK 470 GLU B 89 CG CD OE1 OE2 REMARK 470 LEU C 154 CG CD1 CD2 REMARK 470 LYS C 207 CG CD CE NZ REMARK 470 GLU D 89 CG CD OE1 OE2 REMARK 470 GLN D 113 CG CD OE1 NE2 REMARK 470 GLU D 136 CG CD OE1 OE2 REMARK 470 ARG D 181 CG CD NE CZ NH1 NH2 REMARK 470 LYS E 833 CG CD CE NZ REMARK 470 LYS E 878 CG CD CE NZ 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 PRO B 224 C - N - CA ANGL. DEV. = 9.8 DEGREES REMARK 500 PRO D 222 C - N - CA ANGL. DEV. = 9.3 DEGREES 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 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 ILE A 29 15.86 -141.94 REMARK 500 SER A 30 -109.04 59.75 REMARK 500 ALA A 51 -29.91 70.23 REMARK 500 SER A 60 -9.82 -43.70 REMARK 500 ALA A 84 -162.12 -178.81 REMARK 500 ARG A 108 -161.24 -129.11 REMARK 500 ASN A 138 84.93 22.78 REMARK 500 PRO A 141 -179.64 -68.48 REMARK 500 ASN A 158 15.59 -149.64 REMARK 500 PHE A 209 125.15 -179.36 REMARK 500 ARG B 16 -162.99 -65.38 REMARK 500 ALA B 49 -176.88 176.31 REMARK 500 ASN B 77 66.97 32.80 REMARK 500 GLU B 89 -8.28 -59.86 REMARK 500 ALA B 106 142.16 -39.23 REMARK 500 SER B 134 -176.56 -65.07 REMARK 500 ASP B 152 73.28 36.24 REMARK 500 SER B 157 76.15 -153.67 REMARK 500 ASN B 167 86.33 -16.95 REMARK 500 SER B 172 63.48 -62.73 REMARK 500 CYS C 23 115.54 -170.84 REMARK 500 SER C 30 -108.42 63.12 REMARK 500 ALA C 51 -30.45 71.45 REMARK 500 SER C 52 11.17 -148.68 REMARK 500 PRO C 59 148.92 -35.80 REMARK 500 PRO C 80 -35.41 -38.67 REMARK 500 ALA C 84 -156.08 -170.23 REMARK 500 PRO C 141 -155.67 -59.01 REMARK 500 SER C 171 17.74 49.44 REMARK 500 LYS C 190 -60.39 -107.75 REMARK 500 ALA D 92 177.50 176.07 REMARK 500 GLU D 136 159.02 164.58 REMARK 500 SER D 157 76.05 -154.46 REMARK 500 ASN D 166 27.62 -77.99 REMARK 500 ASN D 167 28.07 46.08 REMARK 500 ASP D 169 133.44 -33.65 REMARK 500 SER D 172 23.82 -161.26 REMARK 500 PRO D 194 -141.14 -83.34 REMARK 500 VAL E 860 -4.00 -148.31 REMARK 500 GLU E 863 157.95 -49.51 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 700 REMARK 700 SHEET REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, REMARK 700 TWO SHEETS ARE DEFINED. REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 401 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD C 401