REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.25 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.1.24 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) : 2.25 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.98 REMARK 3 DATA CUTOFF (SIGMA(F)) : -3.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0 REMARK 3 NUMBER OF REFLECTIONS : 90709 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) : 0.220 REMARK 3 R VALUE (WORKING SET) : 0.218 REMARK 3 FREE R VALUE : 0.280 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.000 REMARK 3 FREE R VALUE TEST SET COUNT : 2819 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) : 2.25 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.31 REMARK 3 REFLECTION IN BIN (WORKING SET) : 6525 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.3690 REMARK 3 BIN FREE R VALUE SET COUNT : 194 REMARK 3 BIN FREE R VALUE : 0.4270 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 7956 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 883 REMARK 3 SOLVENT ATOMS : 554 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.27 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 OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.209 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.205 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.176 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.585 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.941 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.890 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9217 ; 0.031 ; 0.021 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12425 ; 2.683 ; 1.956 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1003 ; 8.795 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1419 ; 0.230 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6381 ; 0.014 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 5033 ; 0.264 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 598 ; 0.234 ; 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): 46 ; 0.323 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 8 ; 0.313 ; 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): 5040 ; 1.381 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8088 ; 2.407 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4134 ; 3.538 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4331 ; 5.166 ; 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 : BABINET MODEL WITH MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.40 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 3HB3 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-MAY-09. REMARK 100 THE RCSB ID CODE IS RCSB052916. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 04-OCT-05 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SLS REMARK 200 BEAMLINE : X10SA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9198 REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 90709 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250 REMARK 200 RESOLUTION RANGE LOW (A) : 111.800 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0 REMARK 200 DATA REDUNDANCY : 4.900 REMARK 200 R MERGE (I) : 0.12400 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 14.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3 REMARK 200 DATA REDUNDANCY IN SHELL : 4.90 REMARK 200 R MERGE FOR SHELL (I) : 0.37900 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: EPMR REMARK 200 STARTING MODEL: PDB ENTRY 1AR1 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 69.41 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.02 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 25% GLYCEROL, PH 5.5, VAPOR REMARK 280 DIFFUSION, TEMPERATURE 277K 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 41.70150 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 78.59250 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 75.23650 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 78.59250 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 41.70150 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 75.23650 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 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: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 28690 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 37820 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -146.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 MET A 1 REMARK 465 ALA A 2 REMARK 465 ASP A 3 REMARK 465 ALA A 4 REMARK 465 ALA A 5 REMARK 465 VAL A 6 REMARK 465 HIS A 7 REMARK 465 GLY A 8 REMARK 465 HIS A 9 REMARK 465 GLY A 10 REMARK 465 ASP A 11 REMARK 465 HIS A 12 REMARK 465 HIS A 13 REMARK 465 ASP A 14 REMARK 465 THR A 15 REMARK 465 ARG A 16 REMARK 465 LEU A 546 REMARK 465 PRO A 547 REMARK 465 LYS A 548 REMARK 465 ARG A 549 REMARK 465 GLU A 550 REMARK 465 ASP A 551 REMARK 465 TRP A 552 REMARK 465 ASP A 553 REMARK 465 ARG A 554 REMARK 465 ALA A 555 REMARK 465 HIS A 556 REMARK 465 ALA A 557 REMARK 465 HIS A 558 REMARK 465 MET B -28 REMARK 465 MET B -27 REMARK 465 ALA B -26 REMARK 465 ILE B -25 REMARK 465 ALA B -24 REMARK 465 THR B -23 REMARK 465 LYS B -22 REMARK 465 ARG B -21 REMARK 465 ARG B -20 REMARK 465 GLY B -19 REMARK 465 VAL B -18 REMARK 465 ALA B -17 REMARK 465 ALA B -16 REMARK 465 VAL B -15 REMARK 465 MET B -14 REMARK 465 SER B -13 REMARK 465 LEU B -12 REMARK 465 GLY B -11 REMARK 465 VAL B -10 REMARK 465 ALA B -9 REMARK 465 THR B -8 REMARK 465 MET B -7 REMARK 465 THR B -6 REMARK 465 ALA B -5 REMARK 465 VAL B -4 REMARK 465 PRO B -3 REMARK 465 ALA B -2 REMARK 465 LEU B -1 REMARK 465 ALA B 0 REMARK 465 ASP B 253 REMARK 465 ALA B 254 REMARK 465 SER B 255 REMARK 465 ASP B 256 REMARK 465 TYR B 257 REMARK 465 LEU B 258 REMARK 465 PRO B 259 REMARK 465 ALA B 260 REMARK 465 SER B 261 REMARK 465 PRO B 262 REMARK 465 VAL B 263 REMARK 465 LYS B 264 REMARK 465 LEU B 265 REMARK 465 ALA B 266 REMARK 465 SER B 267 REMARK 465 ALA B 268 REMARK 465 GLU B 269 REMARK 465 ALA C 119 REMARK 465 TRP C 120 REMARK 465 ARG C 121 REMARK 465 HIS C 122 REMARK 465 PRO C 123 REMARK 465 GLN C 124 REMARK 465 PHE C 125 REMARK 465 GLY C 126 REMARK 465 GLY C 127 REMARK 465 ARG D 109 REMARK 465 GLU D 110 REMARK 465 GLN D 111 REMARK 465 LYS D 112 REMARK 465 LEU D 113 REMARK 465 ILE D 114 REMARK 465 SER D 115 REMARK 465 GLU D 116 REMARK 465 GLU D 117 REMARK 465 ASP D 118 REMARK 465 LEU D 119 REMARK 465 MET D 120 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 NE2 HIS A 276 CE2 TYR A 280 1.52 REMARK 500 N GLN B 1 O HOH B 1235 1.95 REMARK 500 OG SER C 31 O HOH C 1225 1.97 REMARK 500 O HOH B 569 O HOH C 883 2.01 REMARK 500 O HOH A 588 O HOH B 859 2.01 REMARK 500 ND1 HIS A 526 O HOH A 1314 2.02 REMARK 500 OD2 ASP B 135 O HOH B 1284 2.10 REMARK 500 ND2 ASN A 487 O6' LMT A 572 2.12 REMARK 500 OE1 GLN B 32 O HOH B 610 2.13 REMARK 500 O HOH B 328 O HOH B 1199 2.13 REMARK 500 O GLY C 109 OG SER D 43 2.14 REMARK 500 O ILE C 70 O HOH C 918 2.16 REMARK 500 O HOH B 865 O HOH B 1287 2.16 REMARK 500 OG SER C 35 OG SER C 50 2.17 REMARK 500 O HOH B 858 O HOH B 1291 2.17 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 VAL A 51 CB VAL A 51 CG2 0.130 REMARK 500 ILE A 367 CB ILE A 367 CG2 0.193 REMARK 500 TYR A 402 CD1 TYR A 402 CE1 0.093 REMARK 500 GLU A 481 CD GLU A 481 OE2 -0.072 REMARK 500 VAL B 9 CB VAL B 9 CG2 -0.161 REMARK 500 TYR B 122 CD1 TYR B 122 CE1 0.117 REMARK 500 TYR B 127 CE1 TYR B 127 CZ -0.082 REMARK 500 TYR B 149 CZ TYR B 149 CE2 0.079 REMARK 500 TRP B 203 CB TRP B 203 CG 0.119 REMARK 500 PHE B 204 CE2 PHE B 204 CD2 0.124 REMARK 500 TYR B 212 CG TYR B 212 CD1 0.084 REMARK 500 GLU B 218 C GLU B 218 O 0.189 REMARK 500 TYR B 226 CD1 TYR B 226 CE1 0.092 REMARK 500 TYR B 239 CD1 TYR B 239 CE1 0.096 REMARK 500 TYR D 32 CG TYR D 32 CD1 0.085 REMARK 500 TYR D 32 CD1 TYR D 32 CE1 0.093 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 ARG A 54 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 ARG A 54 NE - CZ - NH2 ANGL. DEV. = -7.3 DEGREES REMARK 500 MET A 55 CG - SD - CE ANGL. DEV. = -11.1 DEGREES REMARK 500 ARG A 71 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES REMARK 500 ARG A 71 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES REMARK 500 MET A 90 CG - SD - CE ANGL. DEV. = -9.7 DEGREES REMARK 500 MET A 99 CG - SD - CE ANGL. DEV. = -12.1 DEGREES REMARK 500 ASP A 124 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES REMARK 500 PHE A 215 CB - CA - C ANGL. DEV. = 12.1 DEGREES REMARK 500 ASP A 257 CB - CG - OD2 ANGL. DEV. = 7.4 DEGREES REMARK 500 LEU A 310 CB - CG - CD1 ANGL. DEV. = -15.3 DEGREES REMARK 500 LEU A 380 CB - CG - CD1 ANGL. DEV. = 10.5 DEGREES REMARK 500 LEU A 380 CB - CG - CD2 ANGL. DEV. = -12.4 DEGREES REMARK 500 THR A 389 CA - CB - CG2 ANGL. DEV. = 8.5 DEGREES REMARK 500 ASP A 399 CB - CG - OD2 ANGL. DEV. = 6.4 DEGREES REMARK 500 ARG A 468 CG - CD - NE ANGL. DEV. = -15.5 DEGREES REMARK 500 ARG A 468 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES REMARK 500 ARG A 473 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 ARG A 473 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES REMARK 500 ASP A 477 CB - CG - OD2 ANGL. DEV. = 8.5 DEGREES REMARK 500 ASP B 2 CB - CG - OD2 ANGL. DEV. = 6.8 DEGREES REMARK 500 ASP B 35 CB - CG - OD2 ANGL. DEV. = 6.1 DEGREES REMARK 500 ARG B 59 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES REMARK 500 PRO B 66 N - CA - C ANGL. DEV. = -16.1 DEGREES REMARK 500 ARG B 70 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES REMARK 500 ASP B 111 CB - CG - OD2 ANGL. DEV. = 7.1 DEGREES REMARK 500 ASP B 130 CB - CG - OD2 ANGL. DEV. = 6.4 DEGREES REMARK 500 ASP B 135 CB - CG - OD1 ANGL. DEV. = 7.7 DEGREES REMARK 500 LEU B 137 CB - CG - CD2 ANGL. DEV. = 10.5 DEGREES REMARK 500 ASP B 146 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES REMARK 500 ASP B 152 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES REMARK 500 TYR B 154 O - C - N ANGL. DEV. = -10.7 DEGREES REMARK 500 LEU B 155 C - N - CA ANGL. DEV. = -22.8 DEGREES REMARK 500 VAL B 166 CB - CA - C ANGL. DEV. = -16.7 DEGREES REMARK 500 VAL B 179 CG1 - CB - CG2 ANGL. DEV. = 10.9 DEGREES REMARK 500 THR B 184 OG1 - CB - CG2 ANGL. DEV. = -15.0 DEGREES REMARK 500 MET B 227 CG - SD - CE ANGL. DEV. = -10.6 DEGREES REMARK 500 THR C 33 N - CA - C ANGL. DEV. = -16.3 DEGREES REMARK 500 ASP C 90 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES REMARK 500 ASP D 1 CB - CG - OD2 ANGL. DEV. = 5.5 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 PHE A 19 -48.25 -1.51 REMARK 500 TRP A 22 -71.08 -128.88 REMARK 500 HIS A 28 -33.63 -38.07 REMARK 500 MET A 53 -57.83 -29.26 REMARK 500 TYR A 64 -52.61 -133.98 REMARK 500 GLU A 68 -5.72 -54.57 REMARK 500 LEU A 72 -33.29 -134.65 REMARK 500 GLU A 79 122.23 -29.90 REMARK 500 VAL A 102 -92.27 -116.70 REMARK 500 GLU A 174 151.32 -44.63 REMARK 500 ASP A 248 -37.26 -34.59 REMARK 500 ASN A 250 -21.78 -141.38 REMARK 500 ALA A 259 -17.53 -48.22 REMARK 500 LYS A 299 61.86 81.42 REMARK 500 LYS A 300 124.23 175.18 REMARK 500 MET A 327 19.74 -143.80 REMARK 500 ARG A 474 27.34 82.00 REMARK 500 PHE A 482 16.10 -65.58 REMARK 500 ALA A 513 22.44 -149.18 REMARK 500 TRP A 523 -80.36 -94.46 REMARK 500 ASN A 524 172.34 177.56 REMARK 500 ALA A 527 90.36 -69.67 REMARK 500 PHE A 543 75.45 51.73 REMARK 500 GLU A 544 -97.37 -41.60 REMARK 500 LEU B 4 7.15 -66.94 REMARK 500 ILE B 10 -53.85 -123.40 REMARK 500 VAL B 67 90.17 77.24 REMARK 500 HIS B 73 -179.69 172.30 REMARK 500 ASN B 74 86.08 164.81 REMARK 500 ASP B 152 11.01 -66.45 REMARK 500 ASP B 178 -63.08 -107.33 REMARK 500 HIS B 181 -164.17 -126.19 REMARK 500 CYS B 220 19.02 -143.71 REMARK 500 HIS B 224 -54.86 -26.39 REMARK 500 MET B 227 52.05 -172.57 REMARK 500 PRO B 228 -168.89 -71.14 REMARK 500 SER B 235 156.58 -35.58 REMARK 500 LYS B 238 -60.12 -28.51 REMARK 500 VAL C 12 -174.50 -29.48 REMARK 500 LEU C 18 147.30 -177.09 REMARK 500 LEU C 86 108.22 -57.82 REMARK 500 ASP C 90 0.76 -60.25 REMARK 500 TYR C 102 -107.56 64.74 REMARK 500 ALA C 104 -177.43 -62.29 REMARK 500 TYR D 30 -125.60 76.85 REMARK 500 ASN D 50 48.66 39.68 REMARK 500 ALA D 51 -34.46 54.15 REMARK 500 THR D 69 -32.88 -137.97 REMARK 500 SER D 77 85.51 19.80 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 GLY C 8 GLY C 9 39.75 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 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: (11X,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 SER A 46 23.7 L L OUTSIDE RANGE REMARK 500 VAL A 165 24.3 L L OUTSIDE RANGE REMARK 500 PHE A 215 20.8 L L OUTSIDE RANGE REMARK 500 HIS A 276 23.2 L L OUTSIDE RANGE REMARK 500 VAL A 408 22.6 L L OUTSIDE RANGE REMARK 500 PHE A 460 24.4 L L OUTSIDE RANGE REMARK 500 PHE A 508 23.9 L L OUTSIDE RANGE REMARK 500 THR A 545 24.5 L L OUTSIDE RANGE REMARK 500 VAL B 9 23.1 L L OUTSIDE RANGE REMARK 500 ARG B 62 23.1 L L OUTSIDE RANGE REMARK 500 PRO B 66 47.6 L L OUTSIDE RANGE REMARK 500 VAL B 67 21.2 L L OUTSIDE RANGE REMARK 500 THR B 75 24.8 L L OUTSIDE RANGE REMARK 500 TYR B 154 22.0 L L OUTSIDE RANGE REMARK 500 LEU B 155 23.6 L L OUTSIDE RANGE REMARK 500 VAL B 163 21.4 L L OUTSIDE RANGE REMARK 500 VAL B 174 24.1 L L OUTSIDE RANGE REMARK 500 VAL C 12 23.9 L L OUTSIDE RANGE REMARK 500 ASP C 106 23.8 L L OUTSIDE RANGE REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH C 675 DISTANCE = 6.97 ANGSTROMS REMARK 525 HOH A 610 DISTANCE = 7.47 ANGSTROMS REMARK 525 HOH A 629 DISTANCE = 7.57 ANGSTROMS REMARK 525 HOH D1263 DISTANCE = 6.10 ANGSTROMS REMARK 525 HOH D1264 DISTANCE = 7.54 ANGSTROMS REMARK 525 HOH D1271 DISTANCE = 9.18 ANGSTROMS REMARK 525 HOH A 763 DISTANCE = 7.44 ANGSTROMS REMARK 525 HOH D1272 DISTANCE = 15.64 ANGSTROMS REMARK 525 HOH A 804 DISTANCE = 7.76 ANGSTROMS REMARK 525 HOH C1207 DISTANCE = 9.62 ANGSTROMS REMARK 525 HOH B 758 DISTANCE = 6.61 ANGSTROMS REMARK 525 HOH B 769 DISTANCE = 5.96 ANGSTROMS REMARK 525 HOH A1230 DISTANCE = 5.18 ANGSTROMS REMARK 525 HOH A1255 DISTANCE = 6.08 ANGSTROMS REMARK 525 HOH A1260 DISTANCE = 5.67 ANGSTROMS REMARK 525 HOH A1304 DISTANCE = 6.93 ANGSTROMS REMARK 525 HOH B1220 DISTANCE = 5.43 ANGSTROMS 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 CA A 563 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU A 56 O REMARK 620 2 GLU A 56 OE2 88.2 REMARK 620 3 HIS A 59 O 84.9 171.3 REMARK 620 4 GLY A 61 O 153.3 95.6 88.2 REMARK 620 5 GLN A 63 OE1 134.3 75.2 113.5 71.8 REMARK 620 6 HOH A 851 O 76.3 89.4 83.8 77.3 143.7 REMARK 620 7 HOH A 965 O 60.3 94.6 86.8 144.9 78.5 136.3 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HEA A 559 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 94 NE2 REMARK 620 2 HIS A 413 NE2 174.6 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CU1 A 561 CU REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 276 ND1 REMARK 620 2 HIS A 325 NE2 100.8 REMARK 620 3 HIS A 326 NE2 138.8 94.5 REMARK 620 4 PEO A 576 O2 110.7 88.0 107.8 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MN A 562 MN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 404 OD1 REMARK 620 2 GLU B 218 OE1 113.6 REMARK 620 3 HOH B 285 O 166.7 71.3 REMARK 620 4 HOH A 578 O 72.3 98.6 120.1 REMARK 620 5 HOH B 884 O 86.4 79.7 82.2 156.1 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HEA A 560 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 411 NE2 REMARK 620 2 PEO A 576 O1 169.8 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CU1 B 270 CU REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU B 218 O REMARK 620 2 HIS B 224 ND1 87.2 REMARK 620 N 1 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEA A 559 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEA A 560 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 A 561 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 562 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 563 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LDA A 564 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LDA A 565 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LDA A 566 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LDA A 567 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT A 568 REMARK 800 SITE_IDENTIFIER: BC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT A 569 REMARK 800 SITE_IDENTIFIER: BC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT A 570 REMARK 800 SITE_IDENTIFIER: BC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT A 571 REMARK 800 SITE_IDENTIFIER: BC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT A 572 REMARK 800 SITE_IDENTIFIER: BC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT A 573 REMARK 800 SITE_IDENTIFIER: BC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT A 574 REMARK 800 SITE_IDENTIFIER: BC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT A 575 REMARK 800 SITE_IDENTIFIER: BC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEO A 576 REMARK 800 SITE_IDENTIFIER: CC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 B 270 REMARK 800 SITE_IDENTIFIER: CC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 B 271 REMARK 800 SITE_IDENTIFIER: CC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LDA B 272 REMARK 800 SITE_IDENTIFIER: CC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LDA B 273 REMARK 800 SITE_IDENTIFIER: CC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LDA B 274 REMARK 800 SITE_IDENTIFIER: CC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LDA B 275 REMARK 800 SITE_IDENTIFIER: CC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LDA B 276 REMARK 800 SITE_IDENTIFIER: CC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT B 278 REMARK 800 SITE_IDENTIFIER: CC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT B 279 REMARK 800 SITE_IDENTIFIER: DC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT B 280 REMARK 800 SITE_IDENTIFIER: DC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT B 281 REMARK 800 SITE_IDENTIFIER: DC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT B 282 REMARK 800 SITE_IDENTIFIER: DC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT B 283 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1AR1 RELATED DB: PDB