REMARK 2 REMARK 2 RESOLUTION. 5.65 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.2_869) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE- REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO, REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH, REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER REMARK 3 : ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 5.65 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.93 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 3 NUMBER OF REFLECTIONS : 12713 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.308 REMARK 3 R VALUE (WORKING SET) : 0.306 REMARK 3 FREE R VALUE : 0.324 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.980 REMARK 3 FREE R VALUE TEST SET COUNT : 1269 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 48.9334 - 11.7055 0.98 1254 135 0.3488 0.4085 REMARK 3 2 11.7055 - 9.3120 0.99 1267 147 0.2479 0.2413 REMARK 3 3 9.3120 - 8.1410 1.00 1272 144 0.2628 0.2802 REMARK 3 4 8.1410 - 7.3994 1.00 1279 142 0.3047 0.2907 REMARK 3 5 7.3994 - 6.8706 1.00 1262 136 0.3088 0.3796 REMARK 3 6 6.8706 - 6.4665 1.00 1292 145 0.3435 0.3392 REMARK 3 7 6.4665 - 6.1433 1.00 1274 144 0.3347 0.3464 REMARK 3 8 6.1433 - 5.8763 1.00 1258 133 0.3385 0.2963 REMARK 3 9 5.8763 - 5.6500 1.00 1286 143 0.3547 0.3762 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 REMARK 3 SHRINKAGE RADIUS : 0.86 REMARK 3 K_SOL : 0.33 REMARK 3 B_SOL : 49.62 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 2.250 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 35.910 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) : 219.41090 REMARK 3 B22 (A**2) : 219.41090 REMARK 3 B33 (A**2) : 269.94020 REMARK 3 B12 (A**2) : -0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.015 14401 REMARK 3 ANGLE : 1.587 19527 REMARK 3 CHIRALITY : 0.088 2246 REMARK 3 PLANARITY : 0.009 2473 REMARK 3 DIHEDRAL : 15.286 5275 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : 4 REMARK 3 NCS GROUP : 1 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: chain 'A' and (resseq 1:6 or resseq 10: REMARK 3 340 ) REMARK 3 SELECTION : chain 'C' and (resseq 1:6 or resseq 10: REMARK 3 340 ) REMARK 3 ATOM PAIRS NUMBER : 2555 REMARK 3 RMSD : 0.041 REMARK 3 NCS GROUP : 2 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: chain 'L' and (resseq 3:7 or resseq 10: REMARK 3 110 or resseq 113:115 or resseq 121:215 ) REMARK 3 SELECTION : chain 'F' and (resseq 3:7 or resseq 10: REMARK 3 110 or resseq 113:115 or resseq 121:215 ) REMARK 3 ATOM PAIRS NUMBER : 1528 REMARK 3 RMSD : 0.039 REMARK 3 NCS GROUP : 3 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: chain 'B' and (resseq 368:459 or resseq REMARK 3 463:513 ) REMARK 3 SELECTION : chain 'D' and (resseq 368:459 or resseq REMARK 3 463:513 ) REMARK 3 ATOM PAIRS NUMBER : 1043 REMARK 3 RMSD : 0.155 REMARK 3 NCS GROUP : 4 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: chain 'H' and (resseq 2:99 ) REMARK 3 SELECTION : chain 'E' and (resseq 2:99 ) REMARK 3 ATOM PAIRS NUMBER : 797 REMARK 3 RMSD : 0.001 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 4FQK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JUL-12. REMARK 100 THE RCSB ID CODE IS RCSB073230. 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 : 4.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRL REMARK 200 BEAMLINE : BL11-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : NULL REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12751 REMARK 200 RESOLUTION RANGE HIGH (A) : 5.650 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 200 DATA REDUNDANCY : 6.000 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.08000 REMARK 200 FOR THE DATA SET : 16.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 5.65 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 5.80 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8 REMARK 200 DATA REDUNDANCY IN SHELL : 6.70 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.86000 REMARK 200 FOR SHELL : 2.100 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: PDB ENTRIES 4FQM AND 4FQJ REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 76.42 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.22 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.8 M SODIUM PHOSPHATE MONOBASIC, 1.2 REMARK 280 M POTASSIUM PHOSPHATE DIBASIC, 0.1 M SODIUM ACETATE, PH 4.5, REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z REMARK 290 3555 -X+Y,-X,Z REMARK 290 4555 X+2/3,Y+1/3,Z+1/3 REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3 REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3 REMARK 290 7555 X+1/3,Y+2/3,Z+2/3 REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3 REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 94.60000 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 54.61734 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 106.43667 REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 94.60000 REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 54.61734 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 106.43667 REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 94.60000 REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 54.61734 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 106.43667 REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 109.23467 REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 212.87333 REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 109.23467 REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 212.87333 REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 109.23467 REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 212.87333 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: DODECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, H, L 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 -0.500000 -0.866025 0.000000 -189.20000 REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 -94.60000 REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 -163.85201 REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DODECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, E, 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 350 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 350 BIOMT3 3 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 ILE A 7 REMARK 465 THR A 8 REMARK 465 SER A 9 REMARK 465 THR A 27 REMARK 465 LYS A 339 REMARK 465 LEU A 340 REMARK 465 LEU A 341 REMARK 465 LYS A 342 REMARK 465 GLU A 343 REMARK 465 ARG A 344 REMARK 465 GLY B 348 REMARK 465 PHE B 349 REMARK 465 PHE B 350 REMARK 465 GLY B 351 REMARK 465 ALA B 352 REMARK 465 ILE B 353 REMARK 465 ALA B 354 REMARK 465 GLY B 355 REMARK 465 PHE B 356 REMARK 465 LEU B 357 REMARK 465 GLU B 358 REMARK 465 GLY B 359 REMARK 465 GLY B 360 REMARK 465 TRP B 361 REMARK 465 GLU B 362 REMARK 465 GLY B 363 REMARK 465 MET B 364 REMARK 465 ILE B 365 REMARK 465 ALA B 366 REMARK 465 GLY B 367 REMARK 465 TRP B 368 REMARK 465 ILE B 392 REMARK 465 ASN B 393 REMARK 465 LYS B 394 REMARK 465 ASP B 459 REMARK 465 GLU B 460 REMARK 465 HIS B 461 REMARK 465 LEU B 462 REMARK 465 ASP B 515 REMARK 465 SER B 516 REMARK 465 LEU B 517 REMARK 465 ASN B 518 REMARK 465 ILE B 519 REMARK 465 THR B 520 REMARK 465 ALA B 521 REMARK 465 ALA B 522 REMARK 465 SER B 523 REMARK 465 SER B 524 REMARK 465 GLY B 525 REMARK 465 ARG B 526 REMARK 465 ILE C 7 REMARK 465 THR C 8 REMARK 465 SER C 9 REMARK 465 THR C 27 REMARK 465 LYS C 339 REMARK 465 LEU C 340 REMARK 465 LEU C 341 REMARK 465 LYS C 342 REMARK 465 GLU C 343 REMARK 465 ARG C 344 REMARK 465 GLY D 348 REMARK 465 PHE D 349 REMARK 465 PHE D 350 REMARK 465 GLY D 351 REMARK 465 ALA D 352 REMARK 465 ILE D 353 REMARK 465 ALA D 354 REMARK 465 GLY D 355 REMARK 465 PHE D 356 REMARK 465 LEU D 357 REMARK 465 GLU D 358 REMARK 465 GLY D 359 REMARK 465 GLY D 360 REMARK 465 TRP D 361 REMARK 465 GLU D 362 REMARK 465 GLY D 363 REMARK 465 MET D 364 REMARK 465 ILE D 365 REMARK 465 ALA D 366 REMARK 465 GLY D 367 REMARK 465 TRP D 368 REMARK 465 ILE D 392 REMARK 465 ASN D 393 REMARK 465 LYS D 394 REMARK 465 ASP D 459 REMARK 465 GLU D 460 REMARK 465 HIS D 461 REMARK 465 ASP D 515 REMARK 465 SER D 516 REMARK 465 LEU D 517 REMARK 465 ASN D 518 REMARK 465 ILE D 519 REMARK 465 THR D 520 REMARK 465 ALA D 521 REMARK 465 ALA D 522 REMARK 465 SER D 523 REMARK 465 SER D 524 REMARK 465 GLY D 525 REMARK 465 ARG D 526 REMARK 465 SER E 112 REMARK 465 SER E 128 REMARK 465 LYS E 129 REMARK 465 SER E 130 REMARK 465 THR E 131 REMARK 465 SER E 132 REMARK 465 GLY E 133 REMARK 465 CYS E 216 REMARK 465 HIS E 217 REMARK 465 HIS E 218 REMARK 465 HIS E 219 REMARK 465 HIS E 220 REMARK 465 HIS E 221 REMARK 465 HIS E 222 REMARK 465 LEU F 106A REMARK 465 CYS F 211 REMARK 465 SER F 212 REMARK 465 SER H 112 REMARK 465 SER H 128 REMARK 465 LYS H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 SER H 132 REMARK 465 GLY H 133 REMARK 465 HIS H 217 REMARK 465 HIS H 218 REMARK 465 HIS H 219 REMARK 465 HIS H 220 REMARK 465 HIS H 221 REMARK 465 HIS H 222 REMARK 465 LEU L 106A REMARK 465 SER L 212 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 A 45 -75.01 -39.30 REMARK 500 LYS A 56 -4.34 69.33 REMARK 500 CYS A 57 74.45 -100.38 REMARK 500 LYS A 71 -11.93 72.14 REMARK 500 CYS A 94 -157.95 57.38 REMARK 500 ARG A 112 -38.65 -38.73 REMARK 500 HIS A 122 -141.51 53.65 REMARK 500 ILE A 125 141.62 -170.71 REMARK 500 SER A 142 -12.35 70.45 REMARK 500 ILE A 146 -44.13 -29.18 REMARK 500 THR A 147 -89.49 -76.07 REMARK 500 ASN A 148 150.80 157.83 REMARK 500 ALA A 159 91.42 -67.99 REMARK 500 LYS A 162 -123.77 46.14 REMARK 500 LYS A 163B -125.06 42.32 REMARK 500 THR A 165 -179.21 -171.20 REMARK 500 ILE A 177 -19.68 68.48 REMARK 500 GLU A 180 -123.92 36.85 REMARK 500 ASN A 194 150.82 -49.94 REMARK 500 LEU A 201 -70.91 -61.39 REMARK 500 ASN A 215 66.74 37.29 REMARK 500 ILE A 225 -60.32 -98.23 REMARK 500 LYS A 251 -175.50 -47.62 REMARK 500 GLN A 261 -167.18 -123.89 REMARK 500 GLN A 268 -84.12 -112.74 REMARK 500 SER A 303 -68.02 -109.97 REMARK 500 LEU B 410 73.15 62.88 REMARK 500 ALA B 416 -71.42 -44.61 REMARK 500 MET B 417 83.59 67.04 REMARK 500 LEU B 473 -63.39 -146.40 REMARK 500 PRO B 475 49.07 -80.92 REMARK 500 LYS C 45 -75.06 -39.24 REMARK 500 LYS C 56 -4.21 69.33 REMARK 500 CYS C 57 74.52 -100.42 REMARK 500 LYS C 71 -12.04 72.19 REMARK 500 CYS C 94 -157.97 57.34 REMARK 500 ARG C 112 -38.65 -38.72 REMARK 500 HIS C 122 -141.53 53.65 REMARK 500 ILE C 125 141.58 -170.81 REMARK 500 SER C 142 -12.28 70.43 REMARK 500 ILE C 146 -44.50 -29.18 REMARK 500 THR C 147 -89.65 -75.61 REMARK 500 ASN C 148 150.95 157.95 REMARK 500 ALA C 159 91.51 -67.96 REMARK 500 LYS C 162 -123.80 46.18 REMARK 500 LYS C 163B -125.10 42.33 REMARK 500 THR C 165 -179.25 -171.20 REMARK 500 ILE C 177 -19.69 68.51 REMARK 500 GLU C 180 -123.87 36.89 REMARK 500 LEU C 201 -70.87 -61.36 REMARK 500 REMARK 500 THIS ENTRY HAS 86 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 401 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 402 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 403 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 404 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 405 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 406 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 407 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 408 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 409 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 410 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 401 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 402 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA C 403 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 404 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 405 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 406 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 407 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 408 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 409 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 410 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4FNK RELATED DB: PDB REMARK 900 RELATED ID: 4FQH RELATED DB: PDB REMARK 900 RELATED ID: 4FQI RELATED DB: PDB REMARK 900 RELATED ID: 4FQJ RELATED DB: PDB REMARK 900 RELATED ID: 4FQL RELATED DB: PDB REMARK 900 RELATED ID: 4FQM RELATED DB: PDB REMARK 900 RELATED ID: 4FQV RELATED DB: PDB REMARK 900 RELATED ID: 4FQY RELATED DB: PDB