REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 3.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7 REMARK 3 NUMBER OF REFLECTIONS : 40441 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : OTHER REMARK 3 R VALUE (WORKING + TEST SET) : 0.282 REMARK 3 R VALUE (WORKING SET) : 0.281 REMARK 3 FREE R VALUE : 0.309 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 2154 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) : 3.30 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.38 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2495 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 82.50 REMARK 3 BIN R VALUE (WORKING SET) : 0.3780 REMARK 3 BIN FREE R VALUE SET COUNT : 127 REMARK 3 BIN FREE R VALUE : 0.3940 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 13218 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 2 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 109.00 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 128.44 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -4.20000 REMARK 3 B22 (A**2) : 5.73000 REMARK 3 B33 (A**2) : -1.79000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -0.20000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.543 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.597 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.921 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.902 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; NULL ; NULL REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL 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): NULL ; NULL ; NULL REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL 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): NULL ; NULL ; NULL 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): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL 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): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL 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 : 1 REMARK 3 REMARK 3 NCS GROUP NUMBER : 1 REMARK 3 CHAIN NAMES : A B REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 A 18 A 458 2 REMARK 3 1 B 18 B 458 2 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT 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: NULL REMARK 4 REMARK 4 2HLF COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JUL-06. REMARK 100 THE RCSB ID CODE IS RCSB038480. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 24-JUN-05 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 9.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SLS REMARK 200 BEAMLINE : X06SA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.91921 REMARK 200 MONOCHROMATOR : LN2 COOLED FIXED-EXIT REMARK 200 SI(111) MONOCHROMATOR REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42596 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300 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 (%) : 95.8 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.42 REMARK 200 COMPLETENESS FOR SHELL (%) : 81.7 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 : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: CNS REMARK 200 STARTING MODEL: 1OTS REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 68.26 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.87 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 34% PEG 200/300 1:2, 50MM GLYCIN, REMARK 280 150MM NABR, PH 9.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE REMARK 280 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z REMARK 290 4555 -X+1/2,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 116.41750 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.79650 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 116.41750 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 48.79650 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: HEXAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 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 ARG B 17 REMARK 465 GLU B 459 REMARK 465 GLN B 460 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 O ALA B 187 N ALA B 189 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 THR D 68 CB THR D 68 CG2 -0.294 REMARK 500 MET D 77 SD MET D 77 CE -0.421 REMARK 500 GLU D 78 CD GLU D 78 OE1 -0.144 REMARK 500 GLU D 78 CD GLU D 78 OE2 -0.121 REMARK 500 ASP D 81 CG ASP D 81 OD2 -0.143 REMARK 500 LYS D 141 CD LYS D 141 CE -0.280 REMARK 500 LYS D 141 CE LYS D 141 NZ -0.165 REMARK 500 THR F 68 CB THR F 68 CG2 -0.284 REMARK 500 TRP F 90 CG TRP F 90 CD1 -0.089 REMARK 500 LYS F 141 CD LYS F 141 CE -0.243 REMARK 500 LYS F 141 CE LYS F 141 NZ -0.159 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 LEU A 78 CA - CB - CG ANGL. DEV. = 16.6 DEGREES REMARK 500 LEU B 78 CA - CB - CG ANGL. DEV. = 16.3 DEGREES REMARK 500 ASP D 17 CB - CG - OD2 ANGL. DEV. = 6.4 DEGREES REMARK 500 ARG D 60 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES REMARK 500 ARG D 60 NE - CZ - NH2 ANGL. DEV. = -4.4 DEGREES REMARK 500 THR D 68 OG1 - CB - CG2 ANGL. DEV. = -15.3 DEGREES REMARK 500 GLU D 78 OE1 - CD - OE2 ANGL. DEV. = -19.0 DEGREES REMARK 500 ASP D 81 OD1 - CG - OD2 ANGL. DEV. = -17.2 DEGREES REMARK 500 ASP D 81 CB - CG - OD1 ANGL. DEV. = 11.9 DEGREES REMARK 500 TYR D 139 CB - CG - CD2 ANGL. DEV. = 8.8 DEGREES REMARK 500 TYR D 139 CB - CG - CD1 ANGL. DEV. = -5.8 DEGREES REMARK 500 PRO D 140 C - N - CA ANGL. DEV. = -37.8 DEGREES REMARK 500 PRO D 140 C - N - CD ANGL. DEV. = 19.9 DEGREES REMARK 500 ASP D 166 CB - CG - OD1 ANGL. DEV. = 7.9 DEGREES REMARK 500 ASP F 17 CB - CG - OD2 ANGL. DEV. = 10.1 DEGREES REMARK 500 ARG F 60 NE - CZ - NH2 ANGL. DEV. = 7.0 DEGREES REMARK 500 THR F 68 OG1 - CB - CG2 ANGL. DEV. = -14.6 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 ASP A 73 -99.11 -79.65 REMARK 500 ASN A 74 87.61 -32.40 REMARK 500 TYR A 94 -38.59 -38.96 REMARK 500 ALA A 101 67.14 -178.94 REMARK 500 PRO A 102 -18.93 -47.35 REMARK 500 ALA A 104 9.99 -63.47 REMARK 500 SER A 107 -88.28 -45.40 REMARK 500 VAL A 122 75.52 -119.19 REMARK 500 ARG A 126 -73.30 -109.80 REMARK 500 LEU A 128 -71.33 -42.47 REMARK 500 PHE A 132 -78.90 -56.71 REMARK 500 GLU A 148 -72.13 -35.99 REMARK 500 LEU A 177 -6.56 -57.82 REMARK 500 ALA A 188 -2.91 -53.58 REMARK 500 ILE A 201 24.05 -71.64 REMARK 500 GLU A 202 -8.24 -149.06 REMARK 500 GLU A 203 -71.19 -144.02 REMARK 500 PRO A 206 104.61 -49.03 REMARK 500 LEU A 212 47.93 -93.06 REMARK 500 ILE A 223 -71.64 -41.79 REMARK 500 VAL A 236 91.03 -161.81 REMARK 500 SER A 245 -162.49 -70.69 REMARK 500 VAL A 283 -37.27 -36.76 REMARK 500 PHE A 307 -17.02 179.69 REMARK 500 ALA A 309 66.85 159.59 REMARK 500 ALA A 311 -4.05 -57.48 REMARK 500 SER A 313 -164.18 -104.96 REMARK 500 LEU A 333 -72.40 -62.60 REMARK 500 THR A 344 -75.23 -58.95 REMARK 500 ARG A 403 28.29 48.00 REMARK 500 ALA A 404 61.76 -117.55 REMARK 500 LEU A 413 -70.60 -39.39 REMARK 500 GLU A 414 -17.61 -41.05 REMARK 500 ASN A 418 58.02 -102.36 REMARK 500 PRO A 443 97.35 -48.36 REMARK 500 ALA A 458 -34.67 -35.04 REMARK 500 VAL B 42 -71.00 -58.01 REMARK 500 ASP B 73 -96.48 -75.56 REMARK 500 ASN B 74 92.41 -35.23 REMARK 500 LEU B 96 -19.53 -45.35 REMARK 500 ALA B 101 65.42 175.10 REMARK 500 PRO B 102 -16.52 -48.12 REMARK 500 ALA B 104 16.61 -64.11 REMARK 500 SER B 107 -80.38 -49.42 REMARK 500 VAL B 122 76.14 -111.60 REMARK 500 TRP B 125 -12.71 -49.64 REMARK 500 LEU B 128 -75.48 -39.01 REMARK 500 PHE B 132 -84.45 -51.08 REMARK 500 GLN B 153 -71.38 -67.92 REMARK 500 ILE B 154 -30.26 -39.35 REMARK 500 ALA B 187 -77.34 -66.51 REMARK 500 ALA B 188 -3.94 -41.49 REMARK 500 ASN B 191 44.42 38.92 REMARK 500 ILE B 201 20.19 -73.95 REMARK 500 GLU B 202 -14.91 -143.04 REMARK 500 GLU B 203 -79.97 -134.99 REMARK 500 PRO B 206 99.61 -48.13 REMARK 500 LEU B 212 49.59 -96.64 REMARK 500 ILE B 223 -76.56 -37.76 REMARK 500 VAL B 236 92.36 -165.50 REMARK 500 SER B 245 -163.42 -67.08 REMARK 500 VAL B 283 -32.41 -36.20 REMARK 500 PHE B 307 -15.21 -176.91 REMARK 500 ALA B 309 61.31 158.27 REMARK 500 SER B 313 -159.70 -97.72 REMARK 500 LEU B 333 -72.64 -64.23 REMARK 500 THR B 344 -75.59 -61.27 REMARK 500 MET B 394 -40.44 -26.00 REMARK 500 SER B 401 -68.41 -98.69 REMARK 500 ARG B 403 29.19 45.43 REMARK 500 ALA B 404 63.58 -116.54 REMARK 500 LEU B 413 -76.65 -36.14 REMARK 500 GLU B 414 -16.17 -36.23 REMARK 500 ASN B 418 58.94 -101.52 REMARK 500 PRO B 443 96.29 -50.25 REMARK 500 LEU B 444 -37.69 -36.75 REMARK 500 GLU B 457 44.32 -91.64 REMARK 500 SER C 30 -169.02 -68.50 REMARK 500 ARG C 31 -18.71 61.26 REMARK 500 PRO C 41 125.42 -37.86 REMARK 500 PRO C 62 109.77 -53.86 REMARK 500 LYS C 65 -63.00 -29.29 REMARK 500 TRP C 106 154.09 -47.50 REMARK 500 ASP C 109 -73.71 -50.90 REMARK 500 SER C 136 32.78 -68.48 REMARK 500 ALA C 137 24.28 -150.98 REMARK 500 ALA C 140 89.12 -41.79 REMARK 500 PHE C 154 134.23 -170.80 REMARK 500 PRO C 155 -163.44 -102.12 REMARK 500 LEU C 167 79.90 -107.64 REMARK 500 SER D 7 -92.67 -44.98 REMARK 500 SER D 27 -160.53 -119.81 REMARK 500 TRP D 46 -66.22 -105.61 REMARK 500 THR D 50 -35.69 69.97 REMARK 500 SER D 51 -1.10 -145.43 REMARK 500 THR D 76 88.41 74.81 REMARK 500 GLU D 80 21.45 -66.51 REMARK 500 ALA D 83 -176.33 177.13 REMARK 500 TRP D 90 22.86 -162.62 REMARK 500 ILE D 105 91.29 -63.04 REMARK 500 THR D 125 48.04 -83.03 REMARK 500 SER D 126 0.24 -169.25 REMARK 500 TYR D 139 -118.63 -108.15 REMARK 500 PRO D 140 179.08 -40.99 REMARK 500 LYS D 168 18.20 -146.26 REMARK 500 ASP D 169 -6.71 178.42 REMARK 500 LYS D 198 -39.12 -34.80 REMARK 500 THR D 199 2.36 -63.61 REMARK 500 SER D 200 144.60 -170.50 REMARK 500 SER E 30 -169.89 -67.56 REMARK 500 ARG E 31 -14.63 59.91 REMARK 500 PRO E 41 123.50 -37.81 REMARK 500 PRO E 62 102.37 -52.06 REMARK 500 SER E 63 -130.54 -125.23 REMARK 500 LEU E 64 -125.86 -135.82 REMARK 500 LYS E 65 -82.74 -70.60 REMARK 500 ALA E 92 178.46 178.99 REMARK 500 TYR E 100 -168.29 -160.20 REMARK 500 ALA E 122 -164.93 -59.36 REMARK 500 SER E 136 34.96 -69.61 REMARK 500 ALA E 137 25.07 -151.93 REMARK 500 ALA E 140 88.66 -39.11 REMARK 500 GLN E 179 119.25 -164.52 REMARK 500 SER F 7 -92.69 -42.66 REMARK 500 SER F 27 -159.42 -114.85 REMARK 500 TRP F 46 -65.51 -101.17 REMARK 500 ASP F 49 43.33 39.87 REMARK 500 THR F 50 -37.09 73.28 REMARK 500 THR F 76 91.04 79.94 REMARK 500 ALA F 83 -171.62 -176.03 REMARK 500 TRP F 90 24.23 -161.88 REMARK 500 THR F 125 43.99 -81.32 REMARK 500 SER F 126 -2.51 -165.15 REMARK 500 PRO F 140 178.72 -58.34 REMARK 500 LYS F 198 -32.71 -39.31 REMARK 500 PRO F 203 155.00 -49.84 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 TYR D 139 PRO D 140 -130.34 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 TYR F 139 0.07 SIDE_CHAIN 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 BR A 1 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 2 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1OTS RELATED DB: PDB