REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 3.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.5.0044 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) : 3.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.64 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4 REMARK 3 NUMBER OF REFLECTIONS : 23953 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) : 0.279 REMARK 3 R VALUE (WORKING SET) : 0.275 REMARK 3 FREE R VALUE : 0.351 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200 REMARK 3 FREE R VALUE TEST SET COUNT : 1316 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) : 3.39 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1638 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.37 REMARK 3 BIN R VALUE (WORKING SET) : 0.3430 REMARK 3 BIN FREE R VALUE SET COUNT : 95 REMARK 3 BIN FREE R VALUE : 0.4190 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 8955 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 36 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 114.49 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 3.00000 REMARK 3 B22 (A**2) : 1.36000 REMARK 3 B33 (A**2) : -5.07000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -1.23000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 0.725 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.664 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 39.752 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.861 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.844 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9222 ; 0.011 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12561 ; 1.492 ; 1.961 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1149 ; 8.068 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 345 ;35.766 ;23.797 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1477 ;23.161 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 36 ;15.443 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1420 ; 0.105 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6856 ; 0.007 ; 0.021 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): 5778 ; 0.495 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9343 ; 0.923 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3444 ; 0.845 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3218 ; 1.527 ; 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 : 1.40 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 2ZUQ COMPLIES WITH FORMAT V. 3.20, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-OCT-08. REMARK 100 THE RCSB ID CODE IS RCSB028449. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 19-MAY-08 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SPRING-8 REMARK 200 BEAMLINE : BL44XU REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.90 REMARK 200 MONOCHROMATOR : SI(111)DOUBLE CRYSTAL REMARK 200 OPTICS : LH-COATED MIRROR REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : MACSCIENCE REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25296 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300 REMARK 200 RESOLUTION RANGE LOW (A) : 47.510 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 200 DATA REDUNDANCY : 3.700 REMARK 200 R MERGE (I) : 0.08600 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.7000 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) : 3.48 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.0 REMARK 200 DATA REDUNDANCY IN SHELL : 3.60 REMARK 200 R MERGE FOR SHELL (I) : 0.86500 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.700 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: 1IGT REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 58.66 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG3350, PH 7, VAPOR DIFFUSION, REMARK 280 TEMPERATURE 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 134.65350 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.74000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 134.65350 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 25.74000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C 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 APPLY THE FOLLOWING TO CHAINS: 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 MET A 1 REMARK 465 LEU A 2 REMARK 465 ARG A 3 REMARK 465 PHE A 4 REMARK 465 LEU A 5 REMARK 465 ASN A 6 REMARK 465 GLN A 7 REMARK 465 ALA A 8 REMARK 465 SER A 9 REMARK 465 ARG A 109 REMARK 465 PHE A 110 REMARK 465 PRO A 111 REMARK 465 GLU A 112 REMARK 465 TRP A 113 REMARK 465 SER A 163 REMARK 465 GLN A 164 REMARK 465 PRO A 165 REMARK 465 PHE A 166 REMARK 465 LYS A 167 REMARK 465 ALA A 168 REMARK 465 LYS A 169 REMARK 465 LYS A 170 REMARK 465 ARG A 171 REMARK 465 ASP A 172 REMARK 465 LEU A 173 REMARK 465 PHE A 174 REMARK 465 GLY A 175 REMARK 465 ARG A 176 REMARK 465 MET B 1 REMARK 465 ASP B 2 REMARK 465 SER B 3 REMARK 465 GLN B 4 REMARK 465 ALA B 5 REMARK 465 GLN B 6 REMARK 465 VAL B 7 REMARK 465 LEU B 8 REMARK 465 ILE B 9 REMARK 465 LEU B 10 REMARK 465 LEU B 11 REMARK 465 LEU B 12 REMARK 465 LEU B 13 REMARK 465 TRP B 14 REMARK 465 VAL B 15 REMARK 465 SER B 16 REMARK 465 GLY B 17 REMARK 465 THR B 18 REMARK 465 CYS B 19 REMARK 465 GLY B 20 REMARK 465 ARG B 133 REMARK 465 TYR C 101 REMARK 465 ARG C 102 REMARK 465 SER C 103 REMARK 465 TYR C 104 REMARK 465 ALA C 120 REMARK 465 MET D 1 REMARK 465 LEU D 2 REMARK 465 ARG D 3 REMARK 465 PHE D 4 REMARK 465 LEU D 5 REMARK 465 ASN D 6 REMARK 465 GLN D 7 REMARK 465 ALA D 8 REMARK 465 SER D 9 REMARK 465 ARG D 109 REMARK 465 PHE D 110 REMARK 465 PRO D 111 REMARK 465 GLU D 112 REMARK 465 TRP D 113 REMARK 465 SER D 163 REMARK 465 GLN D 164 REMARK 465 PRO D 165 REMARK 465 PHE D 166 REMARK 465 LYS D 167 REMARK 465 ALA D 168 REMARK 465 LYS D 169 REMARK 465 LYS D 170 REMARK 465 ARG D 171 REMARK 465 ASP D 172 REMARK 465 LEU D 173 REMARK 465 PHE D 174 REMARK 465 GLY D 175 REMARK 465 ARG D 176 REMARK 465 MET E 1 REMARK 465 ASP E 2 REMARK 465 SER E 3 REMARK 465 GLN E 4 REMARK 465 ALA E 5 REMARK 465 GLN E 6 REMARK 465 VAL E 7 REMARK 465 LEU E 8 REMARK 465 ILE E 9 REMARK 465 LEU E 10 REMARK 465 LEU E 11 REMARK 465 LEU E 12 REMARK 465 LEU E 13 REMARK 465 TRP E 14 REMARK 465 VAL E 15 REMARK 465 SER E 16 REMARK 465 GLY E 17 REMARK 465 THR E 18 REMARK 465 CYS E 19 REMARK 465 GLY E 20 REMARK 465 ARG E 133 REMARK 465 ALA F 120 REMARK 465 ILE F 216 REMARK 465 GLU F 217 REMARK 465 PRO F 218 REMARK 465 ARG F 219 REMARK 465 GLY F 220 REMARK 465 PRO F 221 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 NZ LYS B 44 OD1 ASP B 96 1.85 REMARK 500 O ALA C 28 OG SER C 31 2.14 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 C 134 CA - CB - SG ANGL. DEV. = 6.7 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 ALA A 14 7.63 -56.01 REMARK 500 TRP A 15 -59.68 -126.46 REMARK 500 ALA A 24 27.97 -78.77 REMARK 500 LEU A 25 -56.34 -150.08 REMARK 500 VAL A 35 -61.86 -99.26 REMARK 500 LEU A 37 100.17 -25.90 REMARK 500 LEU A 38 77.85 55.04 REMARK 500 PRO A 40 165.12 -36.59 REMARK 500 SER A 41 -62.15 -138.44 REMARK 500 VAL A 42 -126.82 55.92 REMARK 500 LEU A 55 -77.13 -42.55 REMARK 500 ALA A 62 -89.65 -88.12 REMARK 500 ALA A 64 74.01 49.23 REMARK 500 PRO A 65 -78.57 -31.92 REMARK 500 LYS A 66 -54.96 -126.73 REMARK 500 THR A 67 -24.18 -166.12 REMARK 500 TYR A 79 -71.34 -61.48 REMARK 500 LEU A 94 12.03 -62.17 REMARK 500 LEU A 96 9.05 -66.29 REMARK 500 TYR A 97 73.40 177.45 REMARK 500 PRO A 100 -18.86 -34.05 REMARK 500 ALA A 102 -155.17 55.39 REMARK 500 THR A 103 -60.25 -175.15 REMARK 500 CYS A 104 60.98 76.63 REMARK 500 PHE A 106 -106.75 -142.63 REMARK 500 MET A 107 -166.70 48.32 REMARK 500 LEU A 116 -75.65 -68.88 REMARK 500 TRP A 119 9.43 -61.45 REMARK 500 VAL A 123 -6.30 -143.19 REMARK 500 SER A 127 65.06 -114.13 REMARK 500 CYS A 130 85.32 61.16 REMARK 500 TRP A 135 43.52 -92.38 REMARK 500 LEU A 138 33.07 77.33 REMARK 500 TRP A 145 -74.35 -58.59 REMARK 500 LEU A 146 -36.37 -35.70 REMARK 500 VAL A 156 -91.63 -70.09 REMARK 500 ALA A 157 -71.73 -7.49 REMARK 500 VAL A 158 -79.75 -73.87 REMARK 500 VAL A 161 -80.37 -134.22 REMARK 500 ALA B 35 93.34 -55.06 REMARK 500 THR B 54 126.28 62.23 REMARK 500 ARG B 55 101.82 -54.72 REMARK 500 LEU B 73 -51.99 -128.35 REMARK 500 TRP B 76 -44.45 55.54 REMARK 500 ALA B 77 -35.34 158.96 REMARK 500 SER B 82 101.79 -25.14 REMARK 500 ASP B 86 -26.94 -38.16 REMARK 500 SER B 93 135.05 175.61 REMARK 500 VAL B 104 100.92 -53.71 REMARK 500 LEU B 120 -170.25 63.56 REMARK 500 THR B 139 76.32 -115.68 REMARK 500 SER B 141 115.57 -169.13 REMARK 500 PRO B 145 162.38 -46.82 REMARK 500 SER B 147 -59.51 -24.92 REMARK 500 LEU B 161 74.37 -119.82 REMARK 500 TYR B 165 131.66 -174.10 REMARK 500 ASP B 176 -25.01 50.10 REMARK 500 GLN B 181 -41.05 -131.18 REMARK 500 ASN B 182 101.05 -47.72 REMARK 500 SER B 187 125.63 -170.47 REMARK 500 GLN B 191 129.87 -20.32 REMARK 500 TYR B 198 177.20 -51.60 REMARK 500 HIS B 214 -167.85 -119.38 REMARK 500 ASN B 215 -61.52 -121.76 REMARK 500 THR B 222 -0.50 -153.47 REMARK 500 HIS B 223 130.46 -33.42 REMARK 500 LYS B 224 48.54 -77.26 REMARK 500 THR B 227 45.33 -73.91 REMARK 500 PRO B 229 95.11 -59.02 REMARK 500 ARG B 236 -92.41 -35.41 REMARK 500 ASN B 237 -69.50 11.88 REMARK 500 LEU C 18 136.54 163.74 REMARK 500 ALA C 28 77.79 -59.32 REMARK 500 LYS C 43 1.76 83.80 REMARK 500 ASN C 77 8.17 59.17 REMARK 500 SER C 84 -144.29 -120.27 REMARK 500 SER C 85 67.74 -12.01 REMARK 500 THR C 91 100.98 -44.76 REMARK 500 MET C 106 106.01 -58.93 REMARK 500 GLN C 111 -18.34 -157.26 REMARK 500 PRO C 132 -179.84 -68.47 REMARK 500 VAL C 133 124.96 -38.70 REMARK 500 THR C 137 88.58 -27.22 REMARK 500 SER C 140 -52.56 -143.67 REMARK 500 SER C 178 -101.37 57.45 REMARK 500 ASP C 179 38.52 -162.11 REMARK 500 VAL C 189 149.39 178.13 REMARK 500 TRP C 194 -144.29 -79.37 REMARK 500 PRO C 195 -54.94 -11.90 REMARK 500 ALA C 207 4.82 -62.23 REMARK 500 SER C 208 -5.29 -143.36 REMARK 500 SER C 209 95.45 55.46 REMARK 500 LYS C 211 59.98 -111.43 REMARK 500 PRO C 218 -157.80 -59.38 REMARK 500 ARG D 12 -63.94 7.89 REMARK 500 MET D 18 -70.89 -66.90 REMARK 500 ALA D 19 -33.41 -38.69 REMARK 500 HIS D 34 -62.34 -120.85 REMARK 500 LEU D 37 82.95 54.71 REMARK 500 LEU D 38 96.02 63.30 REMARK 500 SER D 41 -44.38 -160.34 REMARK 500 VAL D 42 -128.33 29.63 REMARK 500 CYS D 44 -22.83 -39.82 REMARK 500 PHE D 52 -5.08 -56.29 REMARK 500 LEU D 55 -81.25 -68.22 REMARK 500 ALA D 57 -70.63 -29.84 REMARK 500 ILE D 63 96.91 -56.94 REMARK 500 ALA D 64 64.19 70.69 REMARK 500 PRO D 65 -52.29 -19.67 REMARK 500 THR D 67 -36.25 -156.06 REMARK 500 ILE D 76 15.32 -63.09 REMARK 500 TYR D 97 56.73 -144.85 REMARK 500 PRO D 100 7.10 -66.62 REMARK 500 ALA D 102 159.06 68.12 REMARK 500 THR D 103 -65.67 -143.62 REMARK 500 MET D 107 -165.75 143.06 REMARK 500 LEU D 116 -77.19 -87.11 REMARK 500 PRO D 121 -87.25 -82.36 REMARK 500 PHE D 124 72.19 -108.77 REMARK 500 CYS D 130 61.65 77.83 REMARK 500 LEU D 138 29.36 45.15 REMARK 500 VAL D 156 18.86 -61.95 REMARK 500 ALA D 157 -90.64 -114.20 REMARK 500 VAL D 160 -93.70 -126.61 REMARK 500 GLU E 37 -162.35 -79.60 REMARK 500 ARG E 55 98.65 -44.84 REMARK 500 ASN E 57 68.97 -174.28 REMARK 500 TYR E 58 34.54 88.56 REMARK 500 PRO E 66 150.21 -48.16 REMARK 500 ALA E 77 -41.23 64.19 REMARK 500 SER E 78 -79.50 -92.14 REMARK 500 PRO E 85 156.43 -40.62 REMARK 500 THR E 89 90.30 -162.35 REMARK 500 ASP E 96 76.34 -157.92 REMARK 500 SER E 103 18.31 52.32 REMARK 500 VAL E 104 101.18 -19.42 REMARK 500 GLU E 107 46.10 -88.37 REMARK 500 ALA E 110 171.52 179.40 REMARK 500 LEU E 120 -157.45 57.52 REMARK 500 SER E 147 -56.18 -19.30 REMARK 500 ASN E 163 77.41 53.00 REMARK 500 ASP E 168 93.04 -55.18 REMARK 500 ASP E 176 92.67 20.79 REMARK 500 GLU E 179 79.94 -113.51 REMARK 500 GLN E 191 142.41 -29.15 REMARK 500 LYS E 208 -59.23 -27.89 REMARK 500 ASN E 215 -54.81 -121.38 REMARK 500 THR E 222 40.91 -155.51 REMARK 500 LYS E 232 98.79 -165.54 REMARK 500 ARG E 236 -73.63 -40.11 REMARK 500 ASN E 237 -77.28 9.77 REMARK 500 PRO F 14 102.01 -50.47 REMARK 500 LYS F 19 79.19 -102.07 REMARK 500 ALA F 28 23.08 -67.98 REMARK 500 PHE F 29 -88.29 29.86 REMARK 500 SER F 30 -19.37 -43.12 REMARK 500 SER F 31 -71.45 -45.96 REMARK 500 SER F 52 -169.51 -67.37 REMARK 500 LYS F 65 100.01 -47.69 REMARK 500 ARG F 67 -5.23 -147.54 REMARK 500 ASN F 74 -18.58 -43.83 REMARK 500 ALA F 75 -72.87 -80.86 REMARK 500 SER F 85 64.94 39.70 REMARK 500 ALA F 92 160.82 167.06 REMARK 500 TYR F 101 -64.43 -14.40 REMARK 500 TYR F 104 -6.84 62.54 REMARK 500 MET F 106 91.51 -62.59 REMARK 500 THR F 122 127.22 -34.84 REMARK 500 PRO F 132 -149.98 -64.02 REMARK 500 CYS F 134 -54.96 -26.89 REMARK 500 THR F 137 30.50 -154.62 REMARK 500 THR F 138 89.93 -33.09 REMARK 500 SER F 140 -46.07 -161.39 REMARK 500 CYS F 146 115.41 -162.96 REMARK 500 PHE F 152 140.33 -170.55 REMARK 500 PRO F 153 -165.22 -105.00 REMARK 500 PRO F 155 -152.70 -101.73 REMARK 500 SER F 162 -25.24 63.66 REMARK 500 SER F 166 -62.97 -145.07 REMARK 500 SER F 167 87.77 -35.02 REMARK 500 SER F 178 -126.09 44.71 REMARK 500 TRP F 194 -142.80 -86.73 REMARK 500 PRO F 195 -77.25 19.01 REMARK 500 SER F 196 -87.97 -31.56 REMARK 500 SER F 209 68.19 85.98 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 TRP C 194 PRO C 195 -136.66 REMARK 500 ASN E 57 TYR E 58 49.02 REMARK 500 TRP F 194 PRO F 195 -138.66 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 LEU A 38 24.2 L L OUTSIDE RANGE REMARK 500 ASN B 57 23.5 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 UQ1 A 177 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UQ1 D 177 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2HI7 RELATED DB: PDB REMARK 900 THE SAME PROTEIN COMPLEXED WITH DSBA REMARK 900 RELATED ID: 2ZUP RELATED DB: PDB REMARK 900 THE SAME PROTEIN COMPLEXED WITH DSBA