REMARK 2 REMARK 2 RESOLUTION. 3.20 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) : 3.20 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.02 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 3 NUMBER OF REFLECTIONS : 24996 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) : 0.215 REMARK 3 R VALUE (WORKING SET) : 0.211 REMARK 3 FREE R VALUE : 0.292 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 1335 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) : 3.20 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.28 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1695 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.48 REMARK 3 BIN R VALUE (WORKING SET) : 0.2760 REMARK 3 BIN FREE R VALUE SET COUNT : 101 REMARK 3 BIN FREE R VALUE : 0.3380 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 7806 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 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) : 69.99 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 7.05000 REMARK 3 B22 (A**2) : -1.12000 REMARK 3 B33 (A**2) : -5.93000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 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): 0.532 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.388 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 51.060 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.928 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.863 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7988 ; 0.015 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10860 ; 1.701 ; 1.949 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1012 ; 8.677 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 322 ;36.282 ;24.472 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1310 ;22.717 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 34 ;22.725 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1218 ; 0.112 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6002 ; 0.006 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3774 ; 0.264 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5354 ; 0.318 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 307 ; 0.157 ; 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): 41 ; 0.215 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 1 ; 0.131 ; 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): 5154 ; 0.546 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8206 ; 0.984 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3258 ; 1.243 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2654 ; 2.122 ; 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 : 1 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 6 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : H 1 H 219 REMARK 3 RESIDUE RANGE : L 1 L 214 REMARK 3 RESIDUE RANGE : C 149 C 221 REMARK 3 RESIDUE RANGE : E 1 E 219 REMARK 3 RESIDUE RANGE : F 1 F 214 REMARK 3 RESIDUE RANGE : D 149 D 221 REMARK 3 ORIGIN FOR THE GROUP (A): 25.7373 -8.6688 -7.6906 REMARK 3 T TENSOR REMARK 3 T11: -0.2179 T22: -0.2037 REMARK 3 T33: -0.1324 T12: 0.0164 REMARK 3 T13: 0.0160 T23: 0.0038 REMARK 3 L TENSOR REMARK 3 L11: 0.2189 L22: 0.1475 REMARK 3 L33: 2.1656 L12: 0.0322 REMARK 3 L13: -0.0598 L23: 0.1250 REMARK 3 S TENSOR REMARK 3 S11: -0.0393 S12: -0.0404 S13: -0.0169 REMARK 3 S21: 0.0519 S22: 0.0145 S23: 0.0224 REMARK 3 S31: 0.1835 S32: 0.1986 S33: 0.0248 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 3VRL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-MAY-12. REMARK 100 THE RCSB ID CODE IS RCSB095413. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 08-JAN-11 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRF REMARK 200 BEAMLINE : BL17U REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24996 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 14.000 REMARK 200 R MERGE (I) : 0.12700 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) : 3.20 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.26 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.44800 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: MLPHARE REMARK 200 STARTING MODEL: PDB ENTRY 1E6J (FOR FAB CHAINS) REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 53.64 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, NABR, NACL, PH 7.0, VAPOR REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K 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 41.55450 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 75.41500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 62.02900 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 75.41500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 41.55450 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 62.02900 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, 3 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5570 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 23610 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5450 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 23540 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, 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 350 REMARK 350 BIOMOLECULE: 3 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 12570 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 45610 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -73.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, C, E, F, 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 ASP H 223 REMARK 465 CYS H 224 REMARK 465 PRO C 1 REMARK 465 ILE C 2 REMARK 465 VAL C 3 REMARK 465 GLN C 4 REMARK 465 ASN C 5 REMARK 465 LEU C 6 REMARK 465 GLN C 7 REMARK 465 GLY C 8 REMARK 465 GLN C 9 REMARK 465 MET C 10 REMARK 465 VAL C 11 REMARK 465 HIS C 12 REMARK 465 GLN C 13 REMARK 465 PRO C 14 REMARK 465 ILE C 15 REMARK 465 SER C 16 REMARK 465 PRO C 17 REMARK 465 ARG C 18 REMARK 465 THR C 19 REMARK 465 LEU C 20 REMARK 465 ASN C 21 REMARK 465 ALA C 22 REMARK 465 TRP C 23 REMARK 465 VAL C 24 REMARK 465 LYS C 25 REMARK 465 VAL C 26 REMARK 465 ILE C 27 REMARK 465 GLU C 28 REMARK 465 GLU C 29 REMARK 465 LYS C 30 REMARK 465 GLY C 31 REMARK 465 PHE C 32 REMARK 465 SER C 33 REMARK 465 PRO C 34 REMARK 465 GLU C 35 REMARK 465 VAL C 36 REMARK 465 ILE C 37 REMARK 465 PRO C 38 REMARK 465 MET C 39 REMARK 465 PHE C 40 REMARK 465 THR C 41 REMARK 465 ALA C 42 REMARK 465 LEU C 43 REMARK 465 SER C 44 REMARK 465 GLU C 45 REMARK 465 GLY C 46 REMARK 465 ALA C 47 REMARK 465 THR C 48 REMARK 465 PRO C 49 REMARK 465 GLN C 50 REMARK 465 ASP C 51 REMARK 465 LEU C 52 REMARK 465 ASN C 53 REMARK 465 THR C 54 REMARK 465 MET C 55 REMARK 465 LEU C 56 REMARK 465 ASN C 57 REMARK 465 THR C 58 REMARK 465 VAL C 59 REMARK 465 GLY C 60 REMARK 465 GLY C 61 REMARK 465 HIS C 62 REMARK 465 GLN C 63 REMARK 465 ALA C 64 REMARK 465 ALA C 65 REMARK 465 MET C 66 REMARK 465 GLN C 67 REMARK 465 MET C 68 REMARK 465 LEU C 69 REMARK 465 LYS C 70 REMARK 465 ASP C 71 REMARK 465 THR C 72 REMARK 465 ILE C 73 REMARK 465 ASN C 74 REMARK 465 GLU C 75 REMARK 465 GLU C 76 REMARK 465 ALA C 77 REMARK 465 ALA C 78 REMARK 465 GLU C 79 REMARK 465 TRP C 80 REMARK 465 ASP C 81 REMARK 465 ARG C 82 REMARK 465 LEU C 83 REMARK 465 HIS C 84 REMARK 465 PRO C 85 REMARK 465 VAL C 86 REMARK 465 GLN C 87 REMARK 465 ALA C 88 REMARK 465 GLY C 89 REMARK 465 PRO C 90 REMARK 465 VAL C 91 REMARK 465 ALA C 92 REMARK 465 PRO C 93 REMARK 465 GLY C 94 REMARK 465 GLN C 95 REMARK 465 MET C 96 REMARK 465 ARG C 97 REMARK 465 ASP C 98 REMARK 465 PRO C 99 REMARK 465 ARG C 100 REMARK 465 GLY C 101 REMARK 465 SER C 102 REMARK 465 ASP C 103 REMARK 465 ILE C 104 REMARK 465 ALA C 105 REMARK 465 GLY C 106 REMARK 465 THR C 107 REMARK 465 THR C 108 REMARK 465 SER C 109 REMARK 465 THR C 110 REMARK 465 LEU C 111 REMARK 465 GLN C 112 REMARK 465 GLU C 113 REMARK 465 GLN C 114 REMARK 465 ILE C 115 REMARK 465 GLY C 116 REMARK 465 TRP C 117 REMARK 465 MET C 118 REMARK 465 THR C 119 REMARK 465 HIS C 120 REMARK 465 ASN C 121 REMARK 465 PRO C 122 REMARK 465 PRO C 123 REMARK 465 ILE C 124 REMARK 465 PRO C 125 REMARK 465 VAL C 126 REMARK 465 GLY C 127 REMARK 465 ASP C 128 REMARK 465 ILE C 129 REMARK 465 TYR C 130 REMARK 465 LYS C 131 REMARK 465 ARG C 132 REMARK 465 TRP C 133 REMARK 465 ILE C 134 REMARK 465 ILE C 135 REMARK 465 LEU C 136 REMARK 465 GLY C 137 REMARK 465 LEU C 138 REMARK 465 ASN C 139 REMARK 465 LYS C 140 REMARK 465 ILE C 141 REMARK 465 VAL C 142 REMARK 465 ARG C 143 REMARK 465 MET C 144 REMARK 465 TYR C 145 REMARK 465 SER C 146 REMARK 465 PRO C 147 REMARK 465 VAL C 148 REMARK 465 GLY C 222 REMARK 465 GLY C 223 REMARK 465 PRO C 224 REMARK 465 SER C 225 REMARK 465 HIS C 226 REMARK 465 LYS C 227 REMARK 465 ALA C 228 REMARK 465 ARG C 229 REMARK 465 VAL C 230 REMARK 465 LEU C 231 REMARK 465 ASP E 223 REMARK 465 CYS E 224 REMARK 465 PRO D 1 REMARK 465 ILE D 2 REMARK 465 VAL D 3 REMARK 465 GLN D 4 REMARK 465 ASN D 5 REMARK 465 LEU D 6 REMARK 465 GLN D 7 REMARK 465 GLY D 8 REMARK 465 GLN D 9 REMARK 465 MET D 10 REMARK 465 VAL D 11 REMARK 465 HIS D 12 REMARK 465 GLN D 13 REMARK 465 PRO D 14 REMARK 465 ILE D 15 REMARK 465 SER D 16 REMARK 465 PRO D 17 REMARK 465 ARG D 18 REMARK 465 THR D 19 REMARK 465 LEU D 20 REMARK 465 ASN D 21 REMARK 465 ALA D 22 REMARK 465 TRP D 23 REMARK 465 VAL D 24 REMARK 465 LYS D 25 REMARK 465 VAL D 26 REMARK 465 ILE D 27 REMARK 465 GLU D 28 REMARK 465 GLU D 29 REMARK 465 LYS D 30 REMARK 465 GLY D 31 REMARK 465 PHE D 32 REMARK 465 SER D 33 REMARK 465 PRO D 34 REMARK 465 GLU D 35 REMARK 465 VAL D 36 REMARK 465 ILE D 37 REMARK 465 PRO D 38 REMARK 465 MET D 39 REMARK 465 PHE D 40 REMARK 465 THR D 41 REMARK 465 ALA D 42 REMARK 465 LEU D 43 REMARK 465 SER D 44 REMARK 465 GLU D 45 REMARK 465 GLY D 46 REMARK 465 ALA D 47 REMARK 465 THR D 48 REMARK 465 PRO D 49 REMARK 465 GLN D 50 REMARK 465 ASP D 51 REMARK 465 LEU D 52 REMARK 465 ASN D 53 REMARK 465 THR D 54 REMARK 465 MET D 55 REMARK 465 LEU D 56 REMARK 465 ASN D 57 REMARK 465 THR D 58 REMARK 465 VAL D 59 REMARK 465 GLY D 60 REMARK 465 GLY D 61 REMARK 465 HIS D 62 REMARK 465 GLN D 63 REMARK 465 ALA D 64 REMARK 465 ALA D 65 REMARK 465 MET D 66 REMARK 465 GLN D 67 REMARK 465 MET D 68 REMARK 465 LEU D 69 REMARK 465 LYS D 70 REMARK 465 ASP D 71 REMARK 465 THR D 72 REMARK 465 ILE D 73 REMARK 465 ASN D 74 REMARK 465 GLU D 75 REMARK 465 GLU D 76 REMARK 465 ALA D 77 REMARK 465 ALA D 78 REMARK 465 GLU D 79 REMARK 465 TRP D 80 REMARK 465 ASP D 81 REMARK 465 ARG D 82 REMARK 465 LEU D 83 REMARK 465 HIS D 84 REMARK 465 PRO D 85 REMARK 465 VAL D 86 REMARK 465 GLN D 87 REMARK 465 ALA D 88 REMARK 465 GLY D 89 REMARK 465 PRO D 90 REMARK 465 VAL D 91 REMARK 465 ALA D 92 REMARK 465 PRO D 93 REMARK 465 GLY D 94 REMARK 465 GLN D 95 REMARK 465 MET D 96 REMARK 465 ARG D 97 REMARK 465 ASP D 98 REMARK 465 PRO D 99 REMARK 465 ARG D 100 REMARK 465 GLY D 101 REMARK 465 SER D 102 REMARK 465 ASP D 103 REMARK 465 ILE D 104 REMARK 465 ALA D 105 REMARK 465 GLY D 106 REMARK 465 THR D 107 REMARK 465 THR D 108 REMARK 465 SER D 109 REMARK 465 THR D 110 REMARK 465 LEU D 111 REMARK 465 GLN D 112 REMARK 465 GLU D 113 REMARK 465 GLN D 114 REMARK 465 ILE D 115 REMARK 465 GLY D 116 REMARK 465 TRP D 117 REMARK 465 MET D 118 REMARK 465 THR D 119 REMARK 465 HIS D 120 REMARK 465 ASN D 121 REMARK 465 PRO D 122 REMARK 465 PRO D 123 REMARK 465 ILE D 124 REMARK 465 PRO D 125 REMARK 465 VAL D 126 REMARK 465 GLY D 127 REMARK 465 ASP D 128 REMARK 465 ILE D 129 REMARK 465 TYR D 130 REMARK 465 LYS D 131 REMARK 465 ARG D 132 REMARK 465 TRP D 133 REMARK 465 ILE D 134 REMARK 465 ILE D 135 REMARK 465 LEU D 136 REMARK 465 GLY D 137 REMARK 465 LEU D 138 REMARK 465 ASN D 139 REMARK 465 LYS D 140 REMARK 465 ILE D 141 REMARK 465 VAL D 142 REMARK 465 ARG D 143 REMARK 465 MET D 144 REMARK 465 TYR D 145 REMARK 465 SER D 146 REMARK 465 PRO D 147 REMARK 465 VAL D 148 REMARK 465 GLY D 222 REMARK 465 GLY D 223 REMARK 465 PRO D 224 REMARK 465 SER D 225 REMARK 465 HIS D 226 REMARK 465 LYS D 227 REMARK 465 ALA D 228 REMARK 465 ARG D 229 REMARK 465 VAL D 230 REMARK 465 LEU D 231 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 NH1 ARG H 98 OD2 ASP H 110 2.18 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 LYS H 87 CD LYS H 87 CE 0.176 REMARK 500 CYS F 214 C CYS F 214 O 0.265 REMARK 500 LYS D 158 CE LYS D 158 NZ 0.164 REMARK 500 LYS D 182 CE LYS D 182 NZ 0.193 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 LYS H 87 CD - CE - NZ ANGL. DEV. = 14.3 DEGREES REMARK 500 LEU H 186 CA - CB - CG ANGL. DEV. = 16.5 DEGREES REMARK 500 PRO L 141 C - N - CA ANGL. DEV. = 15.6 DEGREES REMARK 500 PRO L 141 C - N - CD ANGL. DEV. = -16.1 DEGREES REMARK 500 PRO E 156 C - N - CA ANGL. DEV. = 12.5 DEGREES REMARK 500 PRO E 198 C - N - CA ANGL. DEV. = -10.3 DEGREES REMARK 500 PRO F 95 C - N - CA ANGL. DEV. = -13.1 DEGREES REMARK 500 CYS F 214 CA - C - O ANGL. DEV. = -12.9 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 LYS H 43 12.97 105.72 REMARK 500 ASP H 110 -74.72 4.67 REMARK 500 SER H 137 77.16 21.84 REMARK 500 ALA H 138 167.37 147.71 REMARK 500 ALA H 139 -149.49 53.24 REMARK 500 GLN H 140 -35.06 88.60 REMARK 500 ASN H 142 152.95 -49.38 REMARK 500 ASN H 164 73.33 31.31 REMARK 500 SER H 165 19.53 46.63 REMARK 500 SER H 167 22.52 -77.27 REMARK 500 LEU H 168 56.79 -147.99 REMARK 500 SER H 169 -77.23 -69.87 REMARK 500 SER H 181 103.04 30.13 REMARK 500 ASP H 182 -6.99 72.91 REMARK 500 TRP H 197 -132.53 -86.60 REMARK 500 PRO H 198 -60.91 -26.66 REMARK 500 SER H 199 15.84 -59.83 REMARK 500 ILE H 219 63.12 -113.76 REMARK 500 PRO H 221 -178.83 -66.29 REMARK 500 HIS L 30 52.58 36.79 REMARK 500 LEU L 47 -34.77 -132.13 REMARK 500 ALA L 51 -38.48 71.91 REMARK 500 SER L 77 88.90 33.74 REMARK 500 GLU L 81 1.72 -64.93 REMARK 500 TRP L 92 -77.60 -88.47 REMARK 500 ASN L 138 75.32 53.58 REMARK 500 PRO L 141 138.20 10.41 REMARK 500 ASP L 151 -38.54 76.49 REMARK 500 GLU L 154 170.64 -56.20 REMARK 500 ASN L 157 -70.74 -72.31 REMARK 500 GLU L 187 28.00 -78.80 REMARK 500 ASN L 190 -70.72 -113.82 REMARK 500 ARG L 211 5.53 -65.04 REMARK 500 GLU L 213 38.25 -90.97 REMARK 500 SER E 25 119.27 -161.85 REMARK 500 LYS E 43 11.92 91.97 REMARK 500 ALA E 49 141.97 -175.35 REMARK 500 SER E 63 -8.67 -57.79 REMARK 500 LYS E 65 107.87 -30.99 REMARK 500 SER E 85 57.42 39.38 REMARK 500 GLU E 89 -33.07 -38.18 REMARK 500 VAL E 106 113.47 -36.30 REMARK 500 PRO E 135 161.42 -45.20 REMARK 500 ALA E 138 -113.74 -125.07 REMARK 500 ALA E 139 85.97 -63.66 REMARK 500 THR E 141 22.30 -65.96 REMARK 500 LEU E 147 -166.20 -118.66 REMARK 500 PRO E 156 155.04 -14.89 REMARK 500 ASN E 164 71.94 47.32 REMARK 500 SER E 165 38.59 18.43 REMARK 500 REMARK 500 THIS ENTRY HAS 74 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 TRP H 197 PRO H 198 -133.91 REMARK 500 TYR L 140 PRO L 141 -109.10 REMARK 500 PHE E 155 PRO E 156 -121.79 REMARK 500 SER F 7 PRO F 8 -123.57 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CHIRAL CENTERS REMARK 500 REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16) REMARK 500 REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS REMARK 500 THR L 94 24.5 L L OUTSIDE RANGE REMARK 500 TRP E 197 22.8 L L OUTSIDE RANGE REMARK 500 THR F 94 24.3 L L OUTSIDE RANGE REMARK 500 REMARK 500 REMARK: NULL