REMARK 2 REMARK 2 RESOLUTION. 3.0 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.1 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 : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00 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) (%) : 95.3 REMARK 3 NUMBER OF REFLECTIONS : 35995 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) : 0.2234 REMARK 3 FREE R VALUE : 0.2877 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.8 REMARK 3 FREE R VALUE TEST SET COUNT : 2563 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 : 9819 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 292 REMARK 3 SOLVENT ATOMS : 84 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) : -37.928 REMARK 3 B22 (A**2) : 15.850 REMARK 3 B33 (A**2) : 22.078 REMARK 3 B12 (A**2) : 0.000 REMARK 3 B13 (A**2) : 6.472 REMARK 3 B23 (A**2) : 0.000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.434 REMARK 3 ESD FROM SIGMAA (A) : NULL REMARK 3 LOW RESOLUTION CUTOFF (A) : 25.0 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) : 0.007422 REMARK 3 BOND ANGLES (DEGREES) : 1.36901 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.6 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.95 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 : 0.249712 REMARK 3 BSOL : 26.6436 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 : CARBOHYDRATE.PARAM REMARK 3 PARAMETER FILE 3 : ION.PARAM REMARK 3 PARAMETER FILE 4 : WATER.PARAM REMARK 3 PARAMETER FILE 5 : CACO.PAR REMARK 3 PARAMETER FILE 6 : 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 TOPOLOGY FILE 5 : NULL REMARK 3 TOPOLOGY FILE 6 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2J6E COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-SEP-06. REMARK 100 THE PDBE ID CODE IS EBI-30026. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 6.50 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID14-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.934 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36545 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000 REMARK 200 RESOLUTION RANGE LOW (A) : 25.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9 REMARK 200 DATA REDUNDANCY : 3.600 REMARK 200 R MERGE (I) : 0.08000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 14.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.11 REMARK 200 COMPLETENESS FOR SHELL (%) : 93.8 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.42000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 3.200 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: PDB ENTRIES 1DN2, 2FB4 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 52.1 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.28 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 10% MPEG 5000, 3 MM REMARK 280 ZINCACETATE, 3 MM CDCL2, 100 MM SODIUMCACODYLATE PH 6.5 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 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 X+1/2,Y+1/2,Z 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 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 1.000000 0.000000 0.000000 120.99000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.80500 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 120.99000 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 37.80500 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 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PQS REMARK 350 TOTAL BURIED SURFACE AREA: 14400 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 70770 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -78.3 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, H, I, L, M 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 A 216 REMARK 465 PRO A 217 REMARK 465 LYS A 218 REMARK 465 SER A 219 REMARK 465 CYS A 220 REMARK 465 ASP A 221 REMARK 465 LYS A 222 REMARK 465 THR A 223 REMARK 465 HIS A 224 REMARK 465 THR A 225 REMARK 465 CYS A 226 REMARK 465 PRO A 227 REMARK 465 PRO A 228 REMARK 465 CYS A 229 REMARK 465 PRO A 230 REMARK 465 ALA A 231 REMARK 465 PRO A 232 REMARK 465 GLU A 233 REMARK 465 LEU A 234 REMARK 465 LEU A 235 REMARK 465 GLY A 446 REMARK 465 LYS A 447 REMARK 465 GLU B 216 REMARK 465 PRO B 217 REMARK 465 LYS B 218 REMARK 465 SER B 219 REMARK 465 CYS B 220 REMARK 465 ASP B 221 REMARK 465 LYS B 222 REMARK 465 THR B 223 REMARK 465 HIS B 224 REMARK 465 THR B 225 REMARK 465 CYS B 226 REMARK 465 PRO B 227 REMARK 465 PRO B 228 REMARK 465 CYS B 229 REMARK 465 PRO B 230 REMARK 465 ALA B 231 REMARK 465 PRO B 232 REMARK 465 GLU B 233 REMARK 465 LEU B 234 REMARK 465 LEU B 235 REMARK 465 GLY B 236 REMARK 465 GLY B 237 REMARK 465 LYS B 447 REMARK 465 LEU H -10 REMARK 465 LEU H -9 REMARK 465 LEU H -8 REMARK 465 VAL H -7 REMARK 465 ALA H -6 REMARK 465 ALA H -5 REMARK 465 PRO H -4 REMARK 465 ARG H -3 REMARK 465 TRP H -2 REMARK 465 LEU H -1 REMARK 465 SER H 0 REMARK 465 SER H 130 REMARK 465 CYS H 131 REMARK 465 ASP H 132 REMARK 465 THR H 133 REMARK 465 LEU I -10 REMARK 465 LEU I -9 REMARK 465 LEU I -8 REMARK 465 VAL I -7 REMARK 465 ALA I -6 REMARK 465 ALA I -5 REMARK 465 PRO I -4 REMARK 465 ARG I -3 REMARK 465 TRP I -2 REMARK 465 LEU I -1 REMARK 465 SER I 0 REMARK 465 MET L -18 REMARK 465 ALA L -17 REMARK 465 GLY L -16 REMARK 465 PHE L -15 REMARK 465 PRO L -14 REMARK 465 LEU L -13 REMARK 465 LEU L -12 REMARK 465 LEU L -11 REMARK 465 THR L -10 REMARK 465 LEU L -9 REMARK 465 LEU L -8 REMARK 465 THR L -7 REMARK 465 HIS L -6 REMARK 465 CYS L -5 REMARK 465 ALA L -4 REMARK 465 GLY L -3 REMARK 465 SER L -2 REMARK 465 TRP L -1 REMARK 465 ALA L 0 REMARK 465 CYS L 211 REMARK 465 MET M -18 REMARK 465 ALA M -17 REMARK 465 GLY M -16 REMARK 465 PHE M -15 REMARK 465 PRO M -14 REMARK 465 LEU M -13 REMARK 465 LEU M -12 REMARK 465 LEU M -11 REMARK 465 THR M -10 REMARK 465 LEU M -9 REMARK 465 LEU M -8 REMARK 465 THR M -7 REMARK 465 HIS M -6 REMARK 465 CYS M -5 REMARK 465 ALA M -4 REMARK 465 GLY M -3 REMARK 465 SER M -2 REMARK 465 TRP M -1 REMARK 465 ALA M 0 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 PRO A 445 CA C O CB CG CD REMARK 470 PRO B 238 CG CD REMARK 470 GLY B 446 CA C O REMARK 470 GLU L 210 CA C O CB CG CD OE1 OE2 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 N GLY H 96 - O GLY H 100D 2.16 REMARK 500 REMARK 500 REMARK: NULL 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 CYS H 92 CA - CB - SG ANGL. DEV. = 6.7 DEGREES REMARK 500 CYS I 92 CA - CB - SG ANGL. DEV. = 8.9 DEGREES 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 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 253 -31.81 -37.90 REMARK 500 ASP A 265 40.64 72.06 REMARK 500 ASN A 297 38.15 -95.37 REMARK 500 SER A 337 158.63 167.04 REMARK 500 LYS A 338 152.05 -47.79 REMARK 500 PRO A 352 170.07 -57.93 REMARK 500 PRO A 387 -164.23 -71.72 REMARK 500 LYS A 414 -39.71 -37.79 REMARK 500 GLU B 258 143.95 -171.60 REMARK 500 ASP B 265 77.64 63.58 REMARK 500 SER B 267 170.49 -53.14 REMARK 500 GLU B 269 -78.50 -54.68 REMARK 500 GLU B 272 120.06 -37.33 REMARK 500 VAL B 282 155.24 -46.23 REMARK 500 ASN B 286 88.69 177.70 REMARK 500 ALA B 287 81.95 -153.33 REMARK 500 LYS B 288 147.85 -36.95 REMARK 500 GLU B 293 108.38 -57.20 REMARK 500 ASN B 297 57.16 -156.09 REMARK 500 HIS B 310 -77.09 -37.14 REMARK 500 ALA B 327 26.35 -67.40 REMARK 500 ALA B 330 73.98 -110.01 REMARK 500 PRO B 331 100.31 -29.92 REMARK 500 ILE B 332 138.45 -38.90 REMARK 500 GLN B 342 108.06 -48.31 REMARK 500 TYR B 436 130.98 -170.99 REMARK 500 SER B 442 148.74 -175.84 REMARK 500 PRO H 14 151.16 -37.92 REMARK 500 SER H 15 -17.42 64.61 REMARK 500 GLU H 16 -165.14 -67.90 REMARK 500 ASN H 56 121.23 -37.84 REMARK 500 LEU H 63 27.83 -151.47 REMARK 500 THR H 83 -158.81 -124.02 REMARK 500 ASP H 86 28.66 -57.38 REMARK 500 ALA H 88 -168.33 -167.18 REMARK 500 SER H 115 146.63 85.80 REMARK 500 ALA H 116 178.40 -56.00 REMARK 500 SER H 117 134.89 177.30 REMARK 500 SER H 135 68.17 74.40 REMARK 500 LEU H 141 174.59 -50.23 REMARK 500 ALA H 142 116.54 -178.22 REMARK 500 GLN H 143 -160.14 -115.51 REMARK 500 ASP H 144 -58.58 80.94 REMARK 500 LEU H 146 -64.29 -102.91 REMARK 500 SER H 149 70.51 164.62 REMARK 500 THR H 151 78.87 -66.31 REMARK 500 SER H 153 174.47 173.45 REMARK 500 TYR H 156 -163.73 -58.24 REMARK 500 LYS H 157 -78.20 -60.78 REMARK 500 ASN H 158 40.39 -71.42 REMARK 500 ASN H 159 78.15 54.99 REMARK 500 SER H 163 16.62 -65.39 REMARK 500 ALA H 178 111.49 -175.69 REMARK 500 THR H 180 -155.43 -101.85 REMARK 500 SER H 181 104.21 169.57 REMARK 500 PRO H 186 -133.57 -55.38 REMARK 500 LYS H 188 66.64 146.27 REMARK 500 ASP H 189 -71.99 -143.13 REMARK 500 VAL H 190 -155.37 42.60 REMARK 500 THR H 194 -102.15 -63.30 REMARK 500 ASP H 195 -16.38 -166.17 REMARK 500 HIS H 197 -170.97 43.08 REMARK 500 HIS H 204 142.38 172.57 REMARK 500 SER I 15 -23.13 72.12 REMARK 500 LEU I 63 26.29 -166.90 REMARK 500 ALA I 84 -30.77 -36.87 REMARK 500 ALA I 88 -169.55 -173.25 REMARK 500 SER I 115 156.17 52.17 REMARK 500 ALA I 116 164.23 -42.70 REMARK 500 SER I 117 -169.39 -178.20 REMARK 500 VAL I 125 -115.22 -53.05 REMARK 500 SER I 126 -35.47 -172.47 REMARK 500 SER I 134 85.12 -68.69 REMARK 500 SER I 135 97.67 79.46 REMARK 500 ASP I 144 -16.77 64.89 REMARK 500 LEU I 146 -95.19 -99.87 REMARK 500 SER I 149 19.77 -168.60 REMARK 500 ILE I 150 173.58 -55.45 REMARK 500 THR I 151 99.43 -165.59 REMARK 500 TYR I 156 -161.52 -68.38 REMARK 500 ASN I 159 41.42 28.93 REMARK 500 PRO I 186 -70.99 -49.56 REMARK 500 SER I 187 -52.95 -172.99 REMARK 500 LYS I 188 18.53 -166.52 REMARK 500 ASP I 189 -121.69 -73.26 REMARK 500 VAL I 190 -125.75 37.88 REMARK 500 MET I 191 -81.48 -135.21 REMARK 500 THR I 194 -129.74 -57.76 REMARK 500 ASP I 195 44.26 -154.53 REMARK 500 HIS I 197 -174.01 25.06 REMARK 500 HIS I 204 139.06 178.23 REMARK 500 ALA L 10 -74.39 -138.74 REMARK 500 GLN L 16 -160.57 -72.26 REMARK 500 ASN L 27A -100.13 -143.87 REMARK 500 ASN L 51 -49.62 74.06 REMARK 500 ASN L 52 29.21 -152.97 REMARK 500 LEU L 78 148.18 -39.14 REMARK 500 GLU L 81 24.59 -72.90 REMARK 500 LYS L 103 -75.60 -64.66 REMARK 500 LEU L 104 113.88 65.17 REMARK 500 GLN L 109 74.07 33.87 REMARK 500 PRO L 120 168.07 -44.95 REMARK 500 GLN L 126 32.33 -77.52 REMARK 500 ALA L 127 32.26 -169.39 REMARK 500 ASN L 128 72.10 41.98 REMARK 500 LYS L 129 105.39 -163.69 REMARK 500 SER L 137 -125.04 -68.06 REMARK 500 PHE L 139 119.51 172.18 REMARK 500 ALA L 143 119.75 -173.83 REMARK 500 THR L 145 68.88 -106.29 REMARK 500 LYS L 156 -98.31 -48.42 REMARK 500 THR L 162 -152.74 -82.54 REMARK 500 PRO L 164 171.85 -55.58 REMARK 500 SER L 165 111.02 -167.90 REMARK 500 SER L 179 -111.53 -85.59 REMARK 500 LEU L 180 121.71 63.36 REMARK 500 THR L 181 147.72 -39.40 REMARK 500 GLU L 183 32.93 -84.07 REMARK 500 SER L 190 123.04 60.94 REMARK 500 SER L 200 106.81 -56.58 REMARK 500 THR L 201 55.20 -97.94 REMARK 500 PRO L 208 12.92 -64.03 REMARK 500 SER M 2 21.25 -141.78 REMARK 500 ALA M 10 -117.87 -139.12 REMARK 500 GLN M 16 160.00 -49.87 REMARK 500 ASN M 27A -102.86 -131.31 REMARK 500 PRO M 44 157.89 -45.96 REMARK 500 ASN M 51 -52.94 65.30 REMARK 500 ASN M 52 42.42 -156.12 REMARK 500 SER M 65 141.53 -170.80 REMARK 500 THR M 69 38.69 -145.73 REMARK 500 LEU M 78 138.10 -30.42 REMARK 500 GLU M 81 32.09 -76.73 REMARK 500 ALA M 84 -173.82 177.90 REMARK 500 SER M 95A 46.55 73.72 REMARK 500 PRO M 110 41.65 -76.58 REMARK 500 ALA M 112 58.93 -108.78 REMARK 500 PRO M 113 73.43 -55.30 REMARK 500 SER M 114 75.52 -66.56 REMARK 500 ALA M 127 16.74 -64.09 REMARK 500 ASN M 128 30.72 72.97 REMARK 500 ALA M 130 49.06 -157.65 REMARK 500 ILE M 136 95.36 -66.13 REMARK 500 SER M 137 -140.41 -53.48 REMARK 500 PHE M 139 -161.89 -167.90 REMARK 500 PHE M 140 136.25 178.07 REMARK 500 ALA M 143 131.12 169.37 REMARK 500 VAL M 144 -155.95 -151.04 REMARK 500 ALA M 147 114.72 -165.39 REMARK 500 LYS M 156 -136.03 -63.81 REMARK 500 VAL M 159 60.92 -108.62 REMARK 500 GLN M 167 -168.05 -119.75 REMARK 500 SER M 179 -106.19 -57.79 REMARK 500 LEU M 180 133.26 64.56 REMARK 500 LYS M 186 -5.68 -57.73 REMARK 500 SER M 187 -85.25 -99.17 REMARK 500 HIS M 188 168.84 -38.19 REMARK 500 SER M 190 139.57 63.63 REMARK 500 THR M 201 57.87 -91.51 REMARK 500 PRO M 208 14.61 -67.86 REMARK 500 GLU M 210 43.85 -85.81 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 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CD A1445 CD REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU A 294 OE1 REMARK 620 2 GLU A 294 OE2 50.4 REMARK 620 3 HIS A 435 NE2 111.5 150.4 REMARK 620 4 HIS A 310 NE2 108.4 96.0 113.1 REMARK 620 5 HIS A 268 NE2 116.2 79.0 93.5 113.6 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A1446 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU A 272 OE1 REMARK 620 2 GLU A 345 OE2 69.7 REMARK 620 3 CAC A1447 O1 101.8 86.3 REMARK 620 4 GLU A 272 OE2 66.3 129.8 80.3 REMARK 620 5 GLU A 345 OE1 118.1 56.0 102.1 174.0 REMARK 620 6 HIS A 433 NE2 103.3 129.7 141.6 83.7 91.1 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CAC A1447 AS REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CAC A1447 O1 REMARK 620 2 CAC A1447 O2 117.0 REMARK 620 N 1 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 NAG A1453 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUL A1454 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1455 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A1456 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A1457 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG A1458 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL A1459 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A1460 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1461 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B1450 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUL B1451 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B1452 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA B1453 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B1454 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B1455 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL B1456 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA B1457 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B1458 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A1445 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A1446 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAC A1447 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A1451 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A1452 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B1446 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B1449 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT H1215 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A1448 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A1449 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A1450 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B1447 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B1448 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD M1212 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1AJ7 RELATED DB: PDB REMARK 900 IMMUNOGLOBULIN 48G7 GERMLINE FAB ANTIBODY REMARK 900 COMPLEXED WITH HAPTEN 5-(PARA-NITROPHENYL REMARK 900 PHOSPHONATE)-PENTANOIC ACID. AFFINITY MATURATION REMARK 900 OF AN ESTEROLYTIC ANTIBODY REMARK 900 RELATED ID: 1AQK RELATED DB: PDB REMARK 900 THREE-DIMENSIONAL STRUCTURE OF A HUMAN FAB REMARK 900 WITH HIGH AFFINITY FOR TETANUS TOXOID REMARK 900 RELATED ID: 1D5B RELATED DB: PDB REMARK 900 UNLIGANDED MATURE OXY-COPE CATALYTIC ANTIBODY REMARK 900 RELATED ID: 1D5I RELATED DB: PDB REMARK 900 UNLIGANDED GERMLINE PRECURSOR OF AN OXY-COPE REMARK 900 CATALYTIC ANTIBODY REMARK 900 RELATED ID: 1D6V RELATED DB: PDB REMARK 900 CONFORMATION EFFECTS IN BIOLOGICAL CATALYSIS REMARK 900 INTRODUCED BY OXY-COPE ANTIBODY MATURATION REMARK 900 RELATED ID: 1DN2 RELATED DB: PDB REMARK 900 FC FRAGMENT OF HUMAN IGG1 IN COMPLEX WITH REMARK 900 AN ENGINEERED 13 RESIDUE PEPTIDE REMARK 900 DCAWHLGELVWCT-NH2 REMARK 900 RELATED ID: 1E4K RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF SOLUBLE HUMAN IGG1 FC REMARK 900 FRAGMENT-FC-GAMMA RECEPTOR III COMPLEX REMARK 900 RELATED ID: 1FC1 RELATED DB: PDB REMARK 900 FC FRAGMENT (IGG1 CLASS) REMARK 900 RELATED ID: 1FC2 RELATED DB: PDB REMARK 900 RELATED ID: 1FCC RELATED DB: PDB REMARK 900 RELATED ID: 1H3T RELATED DB: PDB REMARK 900 STRUCTURAL ANALYSIS OF HUMAN IGG-FC REMARK 900 GLYCOFORMS REVEALS A CORRELATION BETWEEN REMARK 900 GLYCOSYLATION AND STRUCTURAL INTEGRITY REMARK 900 RELATED ID: 1H3U RELATED DB: PDB REMARK 900 STRUCTURAL ANALYSIS OF HUMAN IGG-FC REMARK 900 GLYCOFORMS REVEALS A CORRELATION BETWEEN REMARK 900 GLYCOSYLATION AND STRUCTURAL INTEGRITY REMARK 900 RELATED ID: 1H3V RELATED DB: PDB REMARK 900 STRUCTURAL ANALYSIS OF HUMAN IGG-FC REMARK 900 GLYCOFORMS REVEALS A CORRELATION BETWEEN REMARK 900 GLYCOSYLATION AND STRUCTURAL INTEGRITY REMARK 900 RELATED ID: 1H3W RELATED DB: PDB REMARK 900 STRUCTURAL ANALYSIS OF HUMAN IGG-FC REMARK 900 GLYCOFORMS REVEALS A CORRELATION BETWEEN REMARK 900 GLYCOSYLATION AND STRUCTURAL INTEGRITY REMARK 900 RELATED ID: 1H3Y RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF A HUMAN IGG1 FC- REMARK 900 FRAGMENT,HIGH SALTCONDITION REMARK 900 RELATED ID: 1HZH RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE INTACT HUMAN IGG REMARK 900 B12 WITH BROADAND POTENT ACTIVITY AGAINST REMARK 900 PRIMARY HIV-1 ISOLATES: ATEMPLATE FOR HIV REMARK 900 VACCINE DESIGN REMARK 900 RELATED ID: 1I7Z RELATED DB: PDB REMARK 900 ANTIBODY GNC92H2 BOUND TO LIGAND REMARK 900 RELATED ID: 1IIS RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF A HUMAN FCG RECEPTOR REMARK 900 IN COMPLEX WITHAN FC FRAGMENT OF IGG1 ( REMARK 900 ORTHORHOMBIC) REMARK 900 RELATED ID: 1IIX RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF A HUMAN FCG RECEPTOR REMARK 900 IN COMPLEX WITHAN FC FRAGMENT OF IGG1 ( REMARK 900 HEXAGONAL) REMARK 900 RELATED ID: 1L6X RELATED DB: PDB REMARK 900 FC FRAGMENT OF RITUXIMAB BOUND TO A REMARK 900 MINIMIZED VERSION OFTHE B-DOMAIN FROM REMARK 900 PROTEIN A CALLED Z34C REMARK 900 RELATED ID: 1N7M RELATED DB: PDB REMARK 900 GERMLINE 7G12 WITH N-METHYLMESOPORPHYRIN REMARK 900 RELATED ID: 1OQX RELATED DB: PDB REMARK 900 G-2 GLYCOVARIANT OF HUMAN IGG FC BOUND REMARK 900 TO MINIMIZED VERSIONOF PROTEIN A CALLED Z34C REMARK 900 RELATED ID: 1T83 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF A HUMAN TYPE III FC REMARK 900 GAMMA RECEPTOR INCOMPLEX WITH AN FC FRAGMENT REMARK 900 OF IGG1 (ORTHORHOMBIC) REMARK 900 RELATED ID: 2IWG RELATED DB: PDB REMARK 900 T.B.C REMARK 900 RELATED ID: 2RCS RELATED DB: PDB REMARK 900 IMMUNOGLOBULIN 48G7 GERMLINE FAB - AFFINITY REMARK 900 MATURATION OF AN ESTEROLYTIC ANTIBODY