REMARK 2 REMARK 2 RESOLUTION. 2.58 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.2.0019 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.58 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.07 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9 REMARK 3 NUMBER OF REFLECTIONS : 231396 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 + TEST SET) : 0.230 REMARK 3 R VALUE (WORKING SET) : 0.227 REMARK 3 FREE R VALUE : 0.291 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 11664 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.58 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.64 REMARK 3 REFLECTION IN BIN (WORKING SET) : 13941 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.95 REMARK 3 BIN R VALUE (WORKING SET) : 0.3200 REMARK 3 BIN FREE R VALUE SET COUNT : 773 REMARK 3 BIN FREE R VALUE : 0.4170 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 37083 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 916 REMARK 3 SOLVENT ATOMS : 1036 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 53.00 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.07 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.29000 REMARK 3 B22 (A**2) : 0.39000 REMARK 3 B33 (A**2) : -0.10000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -0.04000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.467 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.322 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.252 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 23.221 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.906 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.843 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 38967 ; 0.012 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 53294 ; 1.439 ; 1.979 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 4952 ; 6.707 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1428 ;36.399 ;24.538 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 5714 ;17.200 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 127 ;19.334 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 6282 ; 0.093 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 28878 ; 0.004 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 13579 ; 0.208 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 25586 ; 0.303 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1357 ; 0.148 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 33 ; 0.145 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 5 ; 0.111 ; 0.200 REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 25370 ; 0.424 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 39910 ; 0.757 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 15519 ; 1.193 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 13384 ; 1.987 ; 4.500 REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 3B2U COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-DEC-07. REMARK 100 THE RCSB ID CODE IS RCSB045008. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 06-NOV-06 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : CHESS REMARK 200 BEAMLINE : F2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97950 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL REMARK 200 DATA SCALING SOFTWARE : HKL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 231454 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.570 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 200 DATA REDUNDANCY : 3.800 REMARK 200 R MERGE (I) : 0.09700 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.57 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0 REMARK 200 DATA REDUNDANCY IN SHELL : 3.30 REMARK 200 R MERGE FOR SHELL (I) : 0.45600 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.400 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 1YY9, 1CE1, AND 1DN0 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 63.18 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.34 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 12 % PEG 3350, 0.25 M AMMONIUM REMARK 280 ACETATE, 50 MM SODIUM ACETATE, PH 5.0, VAPOR DIFFUSION, REMARK 280 TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,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 69.56100 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 7100 ANGSTROM**2 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 6630 ANGSTROM**2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, C, B 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: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 7070 ANGSTROM**2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, F, 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: 4 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 7180 ANGSTROM**2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, J, I 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: 5 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 7470 ANGSTROM**2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: O, N, 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 350 REMARK 350 BIOMOLECULE: 6 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 6570 ANGSTROM**2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: R, Q, P 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: 7 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 6860 ANGSTROM**2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: U, T, S 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: 8 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 7000 ANGSTROM**2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: X, W, V 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 LYS H 137 REMARK 465 SER H 138 REMARK 465 THR H 139 REMARK 465 SER H 140 REMARK 465 GLY H 141 REMARK 465 SER H 223 REMARK 465 LEU A 307 REMARK 465 ARG A 503 REMARK 465 ASN A 504 REMARK 465 VAL A 505 REMARK 465 SER A 506 REMARK 465 ARG A 507 REMARK 465 GLY A 508 REMARK 465 ARG A 509 REMARK 465 GLU A 510 REMARK 465 CYS A 511 REMARK 465 VAL A 512 REMARK 465 ASP A 513 REMARK 465 LYS A 514 REMARK 465 HIS A 515 REMARK 465 HIS A 516 REMARK 465 HIS A 517 REMARK 465 HIS A 518 REMARK 465 HIS A 519 REMARK 465 HIS A 520 REMARK 465 SER C 135 REMARK 465 SER C 136 REMARK 465 LYS C 137 REMARK 465 SER C 138 REMARK 465 THR C 139 REMARK 465 SER C 140 REMARK 465 GLY C 141 REMARK 465 GLY C 142 REMARK 465 LYS C 222 REMARK 465 SER C 223 REMARK 465 LEU B 307 REMARK 465 GLU B 308 REMARK 465 ARG B 503 REMARK 465 ASN B 504 REMARK 465 VAL B 505 REMARK 465 SER B 506 REMARK 465 ARG B 507 REMARK 465 GLY B 508 REMARK 465 ARG B 509 REMARK 465 GLU B 510 REMARK 465 CYS B 511 REMARK 465 VAL B 512 REMARK 465 ASP B 513 REMARK 465 LYS B 514 REMARK 465 HIS B 515 REMARK 465 HIS B 516 REMARK 465 HIS B 517 REMARK 465 HIS B 518 REMARK 465 HIS B 519 REMARK 465 HIS B 520 REMARK 465 SER F 136 REMARK 465 LYS F 137 REMARK 465 SER F 138 REMARK 465 THR F 139 REMARK 465 SER F 140 REMARK 465 GLY F 141 REMARK 465 LYS F 222 REMARK 465 SER F 223 REMARK 465 LEU E 307 REMARK 465 GLU E 308 REMARK 465 ARG E 503 REMARK 465 ASN E 504 REMARK 465 VAL E 505 REMARK 465 SER E 506 REMARK 465 ARG E 507 REMARK 465 GLY E 508 REMARK 465 ARG E 509 REMARK 465 GLU E 510 REMARK 465 CYS E 511 REMARK 465 VAL E 512 REMARK 465 ASP E 513 REMARK 465 LYS E 514 REMARK 465 HIS E 515 REMARK 465 HIS E 516 REMARK 465 HIS E 517 REMARK 465 HIS E 518 REMARK 465 HIS E 519 REMARK 465 HIS E 520 REMARK 465 LYS J 137 REMARK 465 SER J 138 REMARK 465 THR J 139 REMARK 465 SER J 140 REMARK 465 GLY J 141 REMARK 465 SER J 223 REMARK 465 LEU I 307 REMARK 465 GLU I 308 REMARK 465 GLU I 309 REMARK 465 ARG I 503 REMARK 465 ASN I 504 REMARK 465 VAL I 505 REMARK 465 SER I 506 REMARK 465 ARG I 507 REMARK 465 GLY I 508 REMARK 465 ARG I 509 REMARK 465 GLU I 510 REMARK 465 CYS I 511 REMARK 465 VAL I 512 REMARK 465 ASP I 513 REMARK 465 LYS I 514 REMARK 465 HIS I 515 REMARK 465 HIS I 516 REMARK 465 HIS I 517 REMARK 465 HIS I 518 REMARK 465 HIS I 519 REMARK 465 HIS I 520 REMARK 465 SER N 136 REMARK 465 LYS N 137 REMARK 465 SER N 138 REMARK 465 THR N 139 REMARK 465 SER N 140 REMARK 465 LEU M 307 REMARK 465 ARG M 503 REMARK 465 ASN M 504 REMARK 465 VAL M 505 REMARK 465 SER M 506 REMARK 465 ARG M 507 REMARK 465 GLY M 508 REMARK 465 ARG M 509 REMARK 465 GLU M 510 REMARK 465 CYS M 511 REMARK 465 VAL M 512 REMARK 465 ASP M 513 REMARK 465 LYS M 514 REMARK 465 HIS M 515 REMARK 465 HIS M 516 REMARK 465 HIS M 517 REMARK 465 HIS M 518 REMARK 465 HIS M 519 REMARK 465 HIS M 520 REMARK 465 LYS Q 137 REMARK 465 SER Q 138 REMARK 465 THR Q 139 REMARK 465 SER Q 140 REMARK 465 GLY Q 141 REMARK 465 SER Q 223 REMARK 465 LEU P 307 REMARK 465 GLU P 308 REMARK 465 GLU P 309 REMARK 465 ARG P 503 REMARK 465 ASN P 504 REMARK 465 VAL P 505 REMARK 465 SER P 506 REMARK 465 ARG P 507 REMARK 465 GLY P 508 REMARK 465 ARG P 509 REMARK 465 GLU P 510 REMARK 465 CYS P 511 REMARK 465 VAL P 512 REMARK 465 ASP P 513 REMARK 465 LYS P 514 REMARK 465 HIS P 515 REMARK 465 HIS P 516 REMARK 465 HIS P 517 REMARK 465 HIS P 518 REMARK 465 HIS P 519 REMARK 465 HIS P 520 REMARK 465 LYS T 137 REMARK 465 SER T 138 REMARK 465 THR T 139 REMARK 465 SER T 140 REMARK 465 GLY T 141 REMARK 465 GLY T 142 REMARK 465 SER T 223 REMARK 465 LEU S 307 REMARK 465 GLU S 308 REMARK 465 ARG S 503 REMARK 465 ASN S 504 REMARK 465 VAL S 505 REMARK 465 SER S 506 REMARK 465 ARG S 507 REMARK 465 GLY S 508 REMARK 465 ARG S 509 REMARK 465 GLU S 510 REMARK 465 CYS S 511 REMARK 465 VAL S 512 REMARK 465 ASP S 513 REMARK 465 LYS S 514 REMARK 465 HIS S 515 REMARK 465 HIS S 516 REMARK 465 HIS S 517 REMARK 465 HIS S 518 REMARK 465 HIS S 519 REMARK 465 HIS S 520 REMARK 465 SER W 136 REMARK 465 LYS W 137 REMARK 465 SER W 138 REMARK 465 THR W 139 REMARK 465 SER W 140 REMARK 465 GLY W 141 REMARK 465 SER W 223 REMARK 465 LEU V 307 REMARK 465 GLU V 308 REMARK 465 GLU V 309 REMARK 465 ARG V 503 REMARK 465 ASN V 504 REMARK 465 VAL V 505 REMARK 465 SER V 506 REMARK 465 ARG V 507 REMARK 465 GLY V 508 REMARK 465 ARG V 509 REMARK 465 GLU V 510 REMARK 465 CYS V 511 REMARK 465 VAL V 512 REMARK 465 ASP V 513 REMARK 465 LYS V 514 REMARK 465 HIS V 515 REMARK 465 HIS V 516 REMARK 465 HIS V 517 REMARK 465 HIS V 518 REMARK 465 HIS V 519 REMARK 465 HIS V 520 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 L 126 CG CD CE NZ REMARK 470 LYS L 145 CG CD CE NZ REMARK 470 GLN H 5 CG CD OE1 NE2 REMARK 470 SER H 136 OG REMARK 470 LYS H 209 CG CD CE NZ REMARK 470 LYS H 217 CG CD CE NZ REMARK 470 LYS H 218 CG CD CE NZ REMARK 470 LYS H 222 CG CD CE NZ REMARK 470 GLU A 308 CG CD OE1 OE2 REMARK 470 GLU A 309 CG CD OE1 OE2 REMARK 470 LYS A 310 CG CD CE NZ REMARK 470 LYS A 333 CG CD CE NZ REMARK 470 LYS A 336 CG CD CE NZ REMARK 470 GLN A 366 CG CD OE1 NE2 REMARK 470 LYS A 430 CG CD CE NZ REMARK 470 LYS A 454 CG CD CE NZ REMARK 470 LYS A 476 CG CD CE NZ REMARK 470 LEU A 485 CG CD1 CD2 REMARK 470 GLU A 489 CG CD OE1 OE2 REMARK 470 ARG A 497 CG CD NE CZ NH1 NH2 REMARK 470 LYS D 126 CG CD CE NZ REMARK 470 GLN D 147 CG CD OE1 NE2 REMARK 470 LYS D 169 CG CD CE NZ REMARK 470 LYS D 183 CG CD CE NZ REMARK 470 LYS C 83 CG CD CE NZ REMARK 470 THR C 143 OG1 CG2 REMARK 470 LYS C 151 CG CD CE NZ REMARK 470 GLN C 200 CG CD OE1 NE2 REMARK 470 ASN C 207 CG OD1 REMARK 470 LYS C 209 CG CD CE NZ REMARK 470 LYS C 214 CG CD CE NZ REMARK 470 ASP C 216 CG OD1 OD2 REMARK 470 LYS C 217 CG CD CE NZ REMARK 470 LYS C 218 CG CD CE NZ REMARK 470 GLU B 309 CG CD OE1 OE2 REMARK 470 LYS B 310 CG CD CE NZ REMARK 470 LYS B 322 CG CD CE NZ REMARK 470 LYS B 333 CG CD CE NZ REMARK 470 LYS B 336 CG CD CE NZ REMARK 470 LYS B 375 CG CD CE NZ REMARK 470 GLU B 400 CG CD OE1 OE2 REMARK 470 ARG B 427 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 430 CG CD CE NZ REMARK 470 LYS B 454 CG CD CE NZ REMARK 470 LYS B 455 CG CD CE NZ REMARK 470 GLU B 472 CG CD OE1 OE2 REMARK 470 LYS B 476 CG CD CE NZ REMARK 470 GLU B 489 CG CD OE1 OE2 REMARK 470 GLU B 495 CG CD OE1 OE2 REMARK 470 ARG B 497 CG CD NE CZ NH1 NH2 REMARK 470 ARG G 45 CG CD NE CZ NH1 NH2 REMARK 470 ASP G 122 CG OD1 OD2 REMARK 470 GLU G 123 CG CD OE1 OE2 REMARK 470 LYS G 126 CG CD CE NZ REMARK 470 LYS G 169 CG CD CE NZ REMARK 470 LYS F 83 CG CD CE NZ REMARK 470 LYS F 125 CG CD CE NZ REMARK 470 GLU F 156 CG CD OE1 OE2 REMARK 470 ILE F 203 CG1 CG2 CD1 REMARK 470 ASN F 207 CG OD1 REMARK 470 LYS F 209 CG CD CE NZ REMARK 470 LYS F 214 CG CD CE NZ REMARK 470 LYS F 218 CG CD CE NZ REMARK 470 GLU E 309 CG CD OE1 OE2 REMARK 470 LYS E 310 CG CD CE NZ REMARK 470 LYS E 322 CG CD CE NZ REMARK 470 LYS E 333 CG CD CE NZ REMARK 470 GLU E 367 CG CD OE1 OE2 REMARK 470 ARG E 405 CG CD NE CZ NH1 NH2 REMARK 470 LYS E 454 CG CD CE NZ REMARK 470 LYS E 455 CG CD CE NZ REMARK 470 LYS E 465 CG CD CE NZ REMARK 470 LEU E 485 CG CD1 CD2 REMARK 470 GLU E 489 CG CD OE1 OE2 REMARK 470 ARG E 497 CG CD NE CZ NH1 NH2 REMARK 470 ARG K 24 CG CD NE CZ NH1 NH2 REMARK 470 LYS K 126 CG CD CE NZ REMARK 470 ARG K 142 CG CD NE CZ NH1 NH2 REMARK 470 LYS K 145 CG CD CE NZ REMARK 470 LYS K 169 CG CD CE NZ REMARK 470 GLN J 113 CG CD OE1 NE2 REMARK 470 LYS J 125 CG CD CE NZ REMARK 470 ILE J 203 CG1 CG2 CD1 REMARK 470 ASN J 212 CG OD1 REMARK 470 LYS J 214 CG CD CE NZ REMARK 470 ASP J 216 CG OD1 OD2 REMARK 470 LYS J 218 CG CD CE NZ REMARK 470 GLU J 220 CG CD OE1 OE2 REMARK 470 LYS J 222 CG CD CE NZ REMARK 470 LYS I 322 CG CD CE NZ REMARK 470 LYS I 333 CG CD CE NZ REMARK 470 ASN I 452 CG OD1 REMARK 470 LYS I 454 CG CD CE NZ REMARK 470 LYS I 455 CG CD CE NZ REMARK 470 LYS I 476 CG CD CE NZ REMARK 470 ARG I 497 CG CD NE CZ NH1 NH2 REMARK 470 LYS O 126 CG CD CE NZ REMARK 470 GLU O 143 CG CD OE1 OE2 REMARK 470 LYS O 149 CG CD CE NZ REMARK 470 LYS O 169 CG CD CE NZ REMARK 470 LYS N 77 CG CD CE NZ REMARK 470 LYS N 125 CG CD CE NZ REMARK 470 SER N 195 OG REMARK 470 LYS N 209 CG CD CE NZ REMARK 470 LYS N 214 CG CD CE NZ REMARK 470 LYS N 218 CG CD CE NZ REMARK 470 LYS N 222 CG CD CE NZ REMARK 470 GLU M 308 CG CD OE1 OE2 REMARK 470 GLU M 309 CG CD OE1 OE2 REMARK 470 LYS M 310 CG CD CE NZ REMARK 470 LYS M 322 CG CD CE NZ REMARK 470 LYS M 333 CG CD CE NZ REMARK 470 LYS M 336 CG CD CE NZ REMARK 470 LYS M 375 CG CD CE NZ REMARK 470 ASN M 452 CG OD1 REMARK 470 LYS M 454 CG CD CE NZ REMARK 470 LYS M 455 CG CD CE NZ REMARK 470 LYS M 476 CG CD CE NZ REMARK 470 GLU M 489 CG CD OE1 OE2 REMARK 470 GLU M 495 CG CD OE1 OE2 REMARK 470 ARG M 497 CG CD NE CZ NH1 NH2 REMARK 470 LYS R 103 CG CD CE NZ REMARK 470 LYS R 126 CG CD CE NZ REMARK 470 LYS R 169 CG CD CE NZ REMARK 470 GLN Q 1 CG CD OE1 NE2 REMARK 470 LYS Q 83 CG CD CE NZ REMARK 470 SER Q 136 OG REMARK 470 THR Q 199 OG1 CG2 REMARK 470 LYS Q 209 CG CD CE NZ REMARK 470 ASN Q 212 CG OD1 REMARK 470 LYS Q 214 CG CD CE NZ REMARK 470 LYS Q 218 CG CD CE NZ REMARK 470 LYS Q 222 CG CD CE NZ REMARK 470 LYS P 322 CG CD CE NZ REMARK 470 LYS P 333 CG CD CE NZ REMARK 470 LYS P 336 CG CD CE NZ REMARK 470 LYS P 430 CG CD CE NZ REMARK 470 LYS P 454 CG CD CE NZ REMARK 470 LYS P 455 CG CD CE NZ REMARK 470 GLU P 472 CG CD OE1 OE2 REMARK 470 LYS P 476 CG CD CE NZ REMARK 470 GLU P 489 CG CD OE1 OE2 REMARK 470 ARG P 497 CG CD NE CZ NH1 NH2 REMARK 470 GLU U 123 CG CD OE1 OE2 REMARK 470 GLN T 1 CG CD OE1 NE2 REMARK 470 GLN T 200 CG CD OE1 NE2 REMARK 470 ASN T 207 CG OD1 REMARK 470 LYS T 209 CG CD CE NZ REMARK 470 ASN T 212 CG OD1 REMARK 470 LYS T 214 CG CD CE NZ REMARK 470 LYS T 217 CG CD CE NZ REMARK 470 LYS T 218 CG CD CE NZ REMARK 470 LYS T 222 CG CD CE NZ REMARK 470 GLU S 309 CG CD OE1 OE2 REMARK 470 LYS S 310 CG CD CE NZ REMARK 470 ILE S 318 CG1 CG2 CD1 REMARK 470 LYS S 333 CG CD CE NZ REMARK 470 LYS S 336 CG CD CE NZ REMARK 470 PHE S 357 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG S 390 CG CD NE CZ NH1 NH2 REMARK 470 GLU S 400 CG CD OE1 OE2 REMARK 470 GLU S 431 CG CD OE1 OE2 REMARK 470 LYS S 454 CG CD CE NZ REMARK 470 LYS S 455 CG CD CE NZ REMARK 470 LEU S 456 CG CD1 CD2 REMARK 470 LYS S 463 CG CD CE NZ REMARK 470 LYS S 476 CG CD CE NZ REMARK 470 LEU S 485 CG CD1 CD2 REMARK 470 GLU S 489 CG CD OE1 OE2 REMARK 470 ARG X 45 CG CD NE CZ NH1 NH2 REMARK 470 LYS X 126 CG CD CE NZ REMARK 470 LYS W 209 CG CD CE NZ REMARK 470 ASN W 212 CG OD1 REMARK 470 LYS W 214 CG CD CE NZ REMARK 470 LYS W 217 CG CD CE NZ REMARK 470 LYS W 218 CG CD CE NZ REMARK 470 LYS W 222 CG CD CE NZ REMARK 470 LYS V 310 CG CD CE NZ REMARK 470 LYS V 322 CG CD CE NZ REMARK 470 LYS V 333 CG CD CE NZ REMARK 470 ARG V 353 CG CD NE CZ NH1 NH2 REMARK 470 GLU V 376 CG CD OE1 OE2 REMARK 470 ARG V 390 CG CD NE CZ NH1 NH2 REMARK 470 ARG V 405 CG CD NE CZ NH1 NH2 REMARK 470 LYS V 454 CG CD CE NZ REMARK 470 LYS V 455 CG CD CE NZ REMARK 470 LYS V 476 CG CD CE NZ REMARK 470 HIS V 483 CG ND1 CD2 CE1 NE2 REMARK 470 GLU V 489 CG CD OE1 OE2 REMARK 470 ARG V 497 CG CD NE CZ NH1 NH2 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 O3 BMA A 3283 O5 MAN A 3284 1.85 REMARK 500 O6 NAG I 3891 O HOH I 4242 2.09 REMARK 500 O3 BMA I 3283 O6 MAN I 3284 2.11 REMARK 500 O HOH I 4215 O HOH K 277 2.12 REMARK 500 ND2 ASN B 337 C2 NAG B 3371 2.14 REMARK 500 O4 NAG M 3282 O5 BMA M 3283 2.14 REMARK 500 ND2 ASN M 337 C2 NAG M 3371 2.15 REMARK 500 O GLY I 471 O HOH I 4213 2.16 REMARK 500 O3 BMA A 3283 C2 MAN A 3284 2.19 REMARK 500 O HOH I 4205 O HOH I 4222 2.19 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 L 88 CA - CB - SG ANGL. DEV. = 7.0 DEGREES REMARK 500 PRO C 157 C - N - CA ANGL. DEV. = -10.4 DEGREES REMARK 500 CYS B 338 CA - CB - SG ANGL. DEV. = 7.6 DEGREES REMARK 500 PRO J 193 C - N - CA ANGL. DEV. = 9.6 DEGREES REMARK 500 LEU X 21 CA - CB - CG ANGL. DEV. = 14.1 DEGREES REMARK 500 LEU W 18 CA - CB - CG ANGL. DEV. = 14.3 DEGREES REMARK 500 CYS W 97 CA - CB - SG ANGL. DEV. = 7.8 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 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 L 30 -127.90 51.92 REMARK 500 ALA L 51 -44.52 111.01 REMARK 500 SER L 52 -73.37 163.81 REMARK 500 SER L 77 116.21 -163.51 REMARK 500 ALA L 84 -173.11 171.42 REMARK 500 ASP L 151 42.85 39.44 REMARK 500 ASN L 152 -6.60 79.06 REMARK 500 SER H 15 -4.68 80.74 REMARK 500 ALA H 90 -7.65 -59.66 REMARK 500 ALA H 93 151.76 179.56 REMARK 500 ASP H 109 -72.79 -107.20 REMARK 500 SER H 135 152.09 169.16 REMARK 500 ASP H 152 63.11 67.69 REMARK 500 THR H 168 -33.12 66.88 REMARK 500 SER H 195 -50.32 -21.15 REMARK 500 SER H 196 45.37 -102.89 REMARK 500 GLU A 309 -84.22 -116.05 REMARK 500 LEU A 393 59.09 -93.25 REMARK 500 TYR A 447 -27.21 91.97 REMARK 500 PRO A 488 2.13 -59.72 REMARK 500 ARG A 497 2.09 -66.06 REMARK 500 VAL A 500 -72.94 -70.44 REMARK 500 SER D 30 -102.98 39.94 REMARK 500 ALA D 51 -44.86 69.29 REMARK 500 ASP D 151 52.28 35.31 REMARK 500 ASN D 152 -1.90 76.49 REMARK 500 SER D 171 9.76 81.78 REMARK 500 SER C 15 -12.52 80.10 REMARK 500 ILE C 50 -63.76 -98.93 REMARK 500 ASP C 152 62.73 70.31 REMARK 500 ASN C 163 -67.01 71.20 REMARK 500 SER C 164 16.17 -161.99 REMARK 500 THR C 199 -165.36 -70.63 REMARK 500 GLN C 200 84.65 -5.06 REMARK 500 ASN B 337 -10.95 83.96 REMARK 500 GLN B 411 -35.67 -135.18 REMARK 500 TYR B 447 -38.05 76.10 REMARK 500 ASN B 473 -71.01 -46.58 REMARK 500 PRO B 488 -3.18 -55.90 REMARK 500 SER B 501 -72.08 129.83 REMARK 500 SER G 30 -119.11 48.34 REMARK 500 ALA G 51 -45.47 74.16 REMARK 500 ALA G 84 -160.60 -161.60 REMARK 500 ASN G 152 -13.77 80.01 REMARK 500 SER F 15 -1.32 98.80 REMARK 500 SER F 30 44.87 -100.32 REMARK 500 ASN F 163 -43.16 57.50 REMARK 500 SER F 164 10.15 167.38 REMARK 500 SER F 195 35.06 -87.28 REMARK 500 TYR E 447 -23.58 75.75 REMARK 500 REMARK 500 THIS ENTRY HAS 152 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 ALA L 51 SER L 52 -55.35 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CHIRAL CENTERS REMARK 500 REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16) REMARK 500 REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS REMARK 500 ALA L 51 23.5 L L OUTSIDE RANGE REMARK 500 PHE C 130 24.8 L L OUTSIDE RANGE REMARK 500 GLU C 156 22.5 L L OUTSIDE RANGE REMARK 500 CYS B 338 23.6 L L OUTSIDE RANGE REMARK 500 HIS I 394 20.6 L L OUTSIDE RANGE REMARK 500 ARG M 497 23.6 L L OUTSIDE RANGE REMARK 500 ASP Q 109 24.6 L L OUTSIDE RANGE 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 3281 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3282 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 3283 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 3284 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3371 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3891 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 4201 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 4202 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3281 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3282 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA B 3283 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3371 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3891 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 4201 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 4202 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG E 3281 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG E 3282 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA E 3283 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN E 3284 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG E 3371 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG E 3891 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG E 4201 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG E 4202 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG I 3281 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG I 3282 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA I 3283 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN I 3284 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG I 3371 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG I 3891 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG I 3892 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA I 3893 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG I 4201 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG I 4202 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG M 3281 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG M 3282 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA M 3283 REMARK 800 REMARK 800 SITE_IDENTIFIER: EC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN M 3284 REMARK 800 REMARK 800 SITE_IDENTIFIER: EC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN M 3285 REMARK 800 REMARK 800 SITE_IDENTIFIER: EC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG M 3371 REMARK 800 REMARK 800 SITE_IDENTIFIER: EC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG M 3891 REMARK 800 REMARK 800 SITE_IDENTIFIER: EC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG M 3892 REMARK 800 REMARK 800 SITE_IDENTIFIER: EC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA M 3893 REMARK 800 REMARK 800 SITE_IDENTIFIER: EC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG M 4201 REMARK 800 REMARK 800 SITE_IDENTIFIER: EC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG M 4202 REMARK 800 REMARK 800 SITE_IDENTIFIER: EC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA M 4203 REMARK 800 REMARK 800 SITE_IDENTIFIER: FC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG P 3281 REMARK 800 REMARK 800 SITE_IDENTIFIER: FC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG P 3282 REMARK 800 REMARK 800 SITE_IDENTIFIER: FC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA P 3283 REMARK 800 REMARK 800 SITE_IDENTIFIER: FC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG P 3371 REMARK 800 REMARK 800 SITE_IDENTIFIER: FC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG P 3891 REMARK 800 REMARK 800 SITE_IDENTIFIER: FC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG P 4201 REMARK 800 REMARK 800 SITE_IDENTIFIER: FC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG P 4202 REMARK 800 REMARK 800 SITE_IDENTIFIER: FC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG S 3281 REMARK 800 REMARK 800 SITE_IDENTIFIER: FC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG S 3282 REMARK 800 REMARK 800 SITE_IDENTIFIER: GC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA S 3283 REMARK 800 REMARK 800 SITE_IDENTIFIER: GC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG S 3371 REMARK 800 REMARK 800 SITE_IDENTIFIER: GC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG S 3891 REMARK 800 REMARK 800 SITE_IDENTIFIER: GC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG S 4201 REMARK 800 REMARK 800 SITE_IDENTIFIER: GC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG S 4202 REMARK 800 REMARK 800 SITE_IDENTIFIER: GC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG V 3281 REMARK 800 REMARK 800 SITE_IDENTIFIER: GC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG V 3282 REMARK 800 REMARK 800 SITE_IDENTIFIER: GC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA V 3283 REMARK 800 REMARK 800 SITE_IDENTIFIER: GC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG V 3371 REMARK 800 REMARK 800 SITE_IDENTIFIER: HC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG V 3891 REMARK 800 REMARK 800 SITE_IDENTIFIER: HC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG V 4201 REMARK 800 REMARK 800 SITE_IDENTIFIER: HC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG V 4202 REMARK 800 REMARK 800 SITE_IDENTIFIER: HC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1 REMARK 800 REMARK 800 SITE_IDENTIFIER: HC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 G 214 REMARK 800 REMARK 800 SITE_IDENTIFIER: HC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 1 REMARK 800 REMARK 800 SITE_IDENTIFIER: HC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 K 214 REMARK 800 REMARK 800 SITE_IDENTIFIER: HC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 O 214 REMARK 800 REMARK 800 SITE_IDENTIFIER: HC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 U 214 REMARK 800 REMARK 800 SITE_IDENTIFIER: IC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 X 214 REMARK 800 REMARK 800 SITE_IDENTIFIER: IC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 V 1 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3B2V RELATED DB: PDB