REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.32 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) : 2.32 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.69 REMARK 3 DATA CUTOFF (SIGMA(F)) : -3.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 84230 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) : 0.206 REMARK 3 R VALUE (WORKING SET) : 0.205 REMARK 3 FREE R VALUE : 0.242 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.000 REMARK 3 FREE R VALUE TEST SET COUNT : 2623 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) : 2.32 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.38 REMARK 3 REFLECTION IN BIN (WORKING SET) : 5935 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00 REMARK 3 BIN R VALUE (WORKING SET) : 0.2240 REMARK 3 BIN FREE R VALUE SET COUNT : 157 REMARK 3 BIN FREE R VALUE : 0.3160 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 7954 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 703 REMARK 3 SOLVENT ATOMS : 379 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 51.50 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 60.15 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): 0.208 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.186 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.140 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.594 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.932 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.912 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8944 ; 0.027 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12142 ; 2.488 ; 2.020 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1003 ; 7.709 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 343 ;37.705 ;23.353 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1240 ;19.058 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 26 ;25.498 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1348 ; 0.182 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6376 ; 0.012 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4472 ; 0.251 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5956 ; 0.326 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 465 ; 0.197 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 3 ; 0.184 ; 0.200 REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 31 ; 0.277 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 5 ; 0.050 ; 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): 5189 ; 4.385 ; 4.000 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8089 ; 5.882 ; 6.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5284 ; 4.243 ; 4.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4049 ; 5.773 ; 6.000 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 : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: DUE TO A FEATURE IN THE REFINEMENT REMARK 3 PROGRAM, THE STRUCTURE WAS REFINED WITH OXT ON ONE OR MORE REMARK 3 RESIDUES THAT ARE NOT THE TERMINAL RESIDUES OF THE SEQUENCE. REMARK 3 IN ALL THESE INSTANCES THE OXT WAS CHANGED TO N OF THE NEXT REMARK 3 RESIDUE REMARK 4 REMARK 4 3EHB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-SEP-08. REMARK 100 THE RCSB ID CODE IS RCSB049322. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 16-NOV-06 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.3 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) : 0.92021 REMARK 200 MONOCHROMATOR : DOUBLE MIRROR 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 : 87146 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.320 REMARK 200 RESOLUTION RANGE LOW (A) : 20.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : 0.09000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 19.1400 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.32 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.40 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.0 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 3.930 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: DM REMARK 200 STARTING MODEL: PDB ENTRY 1AR1 REMARK 200 REMARK 200 REMARK: 25% (V/V) GLYCEROL WAS USED AS CRYOPROTECTANT TO FLASH REMARK 200 FREEZE IN A GASEOUS LIQUID NITROGEN COOLED STREAM REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 70.03 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.10 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: MPEG 2000 IS CONTAINED IN THE REMARK 280 CRYSTALLIZATION BUFFER PH 5.5, PH 7.3, VAPOR DIFFUSION, REMARK 280 HANGING DROP, TEMPERATURE 291K 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 42.23050 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 78.74350 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 75.66600 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 78.74350 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 42.23050 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 75.66600 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: 26240 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 38390 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -154.0 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 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 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 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 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 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 LEU A 546 CA C O CB CG CD1 CD2 REMARK 470 ASP B 253 CA C O CB CG OD1 OD2 REMARK 470 ALA C 119 CA C O CB REMARK 470 ARG D 109 CA C O CB CG CD NE REMARK 470 ARG D 109 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 MG MG A 562 O HOH A 582 1.68 REMARK 500 NH1 ARG A 208 O MET A 212 1.93 REMARK 500 NE2 HIS A 276 CE2 TYR A 280 1.96 REMARK 500 OE2 GLU C 1 O GLY C 26 2.13 REMARK 500 NH2 ARG A 468 OD2 ASP B 35 2.19 REMARK 500 OH TYR A 440 OE1 GLU A 442 2.19 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 TYR A 407 CE2 TYR A 407 CD2 0.112 REMARK 500 PHE A 460 CZ PHE A 460 CE2 0.123 REMARK 500 TYR B 125 CZ TYR B 125 CE2 0.099 REMARK 500 ALA B 182 CA ALA B 182 CB 0.136 REMARK 500 CYS D 23 CB CYS D 23 SG -0.141 REMARK 500 ALA D 51 CA ALA D 51 CB 0.130 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. = 4.5 DEGREES REMARK 500 ARG A 54 NE - CZ - NH2 ANGL. DEV. = -8.3 DEGREES REMARK 500 GLY A 61 N - CA - C ANGL. DEV. = -16.4 DEGREES REMARK 500 ASP A 124 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES REMARK 500 ARG A 249 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES REMARK 500 ASP A 263 CB - CG - OD1 ANGL. DEV. = 8.0 DEGREES REMARK 500 ASP A 263 CB - CG - OD2 ANGL. DEV. = -6.5 DEGREES REMARK 500 LEU A 271 CA - CB - CG ANGL. DEV. = -15.5 DEGREES REMARK 500 VAL A 388 CG1 - CB - CG2 ANGL. DEV. = 11.0 DEGREES REMARK 500 ARG A 400 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES REMARK 500 VAL A 408 CG1 - CB - CG2 ANGL. DEV. = 10.1 DEGREES REMARK 500 ARG A 468 CG - CD - NE ANGL. DEV. = -13.1 DEGREES REMARK 500 ARG A 468 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES REMARK 500 ARG A 468 NE - CZ - NH2 ANGL. DEV. = -7.5 DEGREES REMARK 500 PRO B 66 N - CA - C ANGL. DEV. = -17.0 DEGREES REMARK 500 LEU B 137 CB - CG - CD1 ANGL. DEV. = -12.4 DEGREES REMARK 500 LEU B 137 CB - CG - CD2 ANGL. DEV. = 13.4 DEGREES REMARK 500 LEU B 155 C - N - CA ANGL. DEV. = -18.2 DEGREES REMARK 500 VAL B 163 CG1 - CB - CG2 ANGL. DEV. = 10.8 DEGREES REMARK 500 VAL B 166 CB - CA - C ANGL. DEV. = -12.2 DEGREES REMARK 500 LYS B 238 CD - CE - NZ ANGL. DEV. = -15.0 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 18 112.52 -39.93 REMARK 500 TYR A 64 -54.71 -136.22 REMARK 500 ALA A 76 30.16 -78.12 REMARK 500 SER A 77 15.56 -143.04 REMARK 500 GLU A 79 124.37 -16.78 REMARK 500 VAL A 102 -82.11 -127.71 REMARK 500 MET A 207 21.06 -142.41 REMARK 500 LYS A 299 62.16 74.32 REMARK 500 LYS A 300 134.60 -176.37 REMARK 500 MET A 327 19.75 -145.36 REMARK 500 ALA A 396 -48.87 -25.42 REMARK 500 ALA A 420 -32.23 -37.59 REMARK 500 PRO A 479 150.27 -40.44 REMARK 500 VAL A 517 83.79 -153.32 REMARK 500 TRP A 523 -81.85 -111.76 REMARK 500 PHE A 543 71.97 48.04 REMARK 500 GLU A 544 -81.93 -70.46 REMARK 500 ASP B 2 -64.15 -99.94 REMARK 500 ILE B 10 -50.37 -120.47 REMARK 500 VAL B 67 83.35 72.64 REMARK 500 PHE B 71 154.35 -47.53 REMARK 500 HIS B 73 -176.82 -179.26 REMARK 500 ASN B 74 96.45 159.14 REMARK 500 MET B 227 67.29 -152.26 REMARK 500 SER B 235 158.39 -43.24 REMARK 500 LEU C 18 144.39 -172.34 REMARK 500 LYS C 43 21.78 82.68 REMARK 500 ASN C 77 45.93 71.62 REMARK 500 TYR C 102 -115.94 71.11 REMARK 500 SER C 118 70.63 -53.87 REMARK 500 TYR D 30 -117.13 57.34 REMARK 500 LEU D 47 -55.52 -120.18 REMARK 500 ALA D 51 -42.88 72.31 REMARK 500 SER D 77 81.59 35.62 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 60.53 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 D 141 DISTANCE = 7.77 ANGSTROMS REMARK 525 HOH C 152 DISTANCE = 7.32 ANGSTROMS REMARK 525 HOH A 604 DISTANCE = 7.67 ANGSTROMS REMARK 525 HOH C 158 DISTANCE = 5.33 ANGSTROMS REMARK 525 HOH D 153 DISTANCE = 6.10 ANGSTROMS REMARK 525 HOH C 161 DISTANCE = 7.02 ANGSTROMS REMARK 525 HOH A 623 DISTANCE = 5.44 ANGSTROMS REMARK 525 HOH A 631 DISTANCE = 5.30 ANGSTROMS REMARK 525 HOH B 345 DISTANCE = 5.92 ANGSTROMS REMARK 525 HOH A 643 DISTANCE = 8.11 ANGSTROMS REMARK 525 HOH A 644 DISTANCE = 6.84 ANGSTROMS REMARK 525 HOH A 650 DISTANCE = 5.27 ANGSTROMS REMARK 525 HOH A 651 DISTANCE = 6.70 ANGSTROMS REMARK 525 HOH A 654 DISTANCE = 7.14 ANGSTROMS REMARK 525 HOH B 361 DISTANCE = 5.38 ANGSTROMS REMARK 525 HOH A 663 DISTANCE = 6.50 ANGSTROMS REMARK 525 HOH A 664 DISTANCE = 5.04 ANGSTROMS REMARK 525 HOH B 367 DISTANCE = 7.26 ANGSTROMS REMARK 525 HOH A 667 DISTANCE = 5.74 ANGSTROMS REMARK 525 HOH B 371 DISTANCE = 5.91 ANGSTROMS REMARK 525 HOH B 374 DISTANCE = 5.55 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 85.7 REMARK 620 3 HIS A 59 O 91.0 175.2 REMARK 620 4 GLY A 61 O 159.7 103.4 80.8 REMARK 620 5 GLN A 63 OE1 130.3 75.1 104.6 69.9 REMARK 620 6 HOH A 669 O 74.5 85.5 97.1 88.1 145.7 REMARK 620 N 1 2 3 4 5 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 176.1 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CU A 561 CU REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 276 ND1 REMARK 620 2 HIS A 325 NE2 106.4 REMARK 620 3 HIS A 326 NE2 135.4 97.1 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MG A 562 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 403 NE2 REMARK 620 2 ASP A 404 OD1 82.2 REMARK 620 3 GLU B 218 OE1 172.9 104.8 REMARK 620 4 HOH A 684 O 98.7 68.7 84.0 REMARK 620 N 1 2 3 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 PER A 576 O2 166.6 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 CU A 561 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 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 PER A 576 REMARK 800 SITE_IDENTIFIER: CC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU B 270 REMARK 800 SITE_IDENTIFIER: CC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU 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 277 REMARK 800 SITE_IDENTIFIER: CC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT B 278 REMARK 800 SITE_IDENTIFIER: DC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT B 279 REMARK 800 SITE_IDENTIFIER: DC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT D 121 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1AR1 RELATED DB: PDB REMARK 900 WILD TYPE, ROOM TEMPERATURE