REMARK 2 REMARK 2 RESOLUTION. 2.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.3.0037 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) : 2.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.88 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2 REMARK 3 NUMBER OF REFLECTIONS : 37032 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) : 0.230 REMARK 3 R VALUE (WORKING SET) : 0.229 REMARK 3 FREE R VALUE : 0.272 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.100 REMARK 3 FREE R VALUE TEST SET COUNT : 1191 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) : 2.50 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.56 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2593 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.39 REMARK 3 BIN R VALUE (WORKING SET) : 0.2670 REMARK 3 BIN FREE R VALUE SET COUNT : 81 REMARK 3 BIN FREE R VALUE : 0.3440 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6527 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 70 REMARK 3 SOLVENT ATOMS : 57 REMARK 3 REMARK 3 B VALUES. REMARK 3 B VALUE TYPE : LIKELY RESIDUAL REMARK 3 FROM WILSON PLOT (A**2) : 42.20 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 62.23 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.13000 REMARK 3 B22 (A**2) : 1.50000 REMARK 3 B33 (A**2) : -1.47000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -0.70000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.463 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.292 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.316 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 28.105 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.917 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.878 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6782 ; 0.018 ; 0.021 REMARK 3 BOND LENGTHS OTHERS (A): 4587 ; 0.003 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9213 ; 1.740 ; 1.950 REMARK 3 BOND ANGLES OTHERS (DEGREES): 11097 ; 1.110 ; 3.010 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 835 ; 7.848 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 293 ;37.001 ;24.403 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1097 ;18.315 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 31 ;19.280 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1003 ; 0.122 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7496 ; 0.006 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1321 ; 0.003 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1296 ; 0.227 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 4541 ; 0.213 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3036 ; 0.182 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): 3667 ; 0.096 ; 0.200 REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 181 ; 0.236 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): 1 ; 0.417 ; 0.200 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): 10 ; 0.135 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): 48 ; 0.184 ; 0.200 REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 3 ; 0.121 ; 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): 5317 ; 1.039 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1721 ; 0.166 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6778 ; 1.264 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3050 ; 2.001 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2435 ; 2.926 ; 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 : 4 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 2 B 41 REMARK 3 ORIGIN FOR THE GROUP (A): 54.0350 -46.9060 42.1430 REMARK 3 T TENSOR REMARK 3 T11: 0.4389 T22: 0.8800 REMARK 3 T33: 0.2227 T12: 0.1835 REMARK 3 T13: -0.0199 T23: -0.1026 REMARK 3 L TENSOR REMARK 3 L11: 15.7256 L22: 26.5061 REMARK 3 L33: 7.8644 L12: -0.4411 REMARK 3 L13: -4.6959 L23: -3.4339 REMARK 3 S TENSOR REMARK 3 S11: -0.7767 S12: 1.8843 S13: -0.7720 REMARK 3 S21: -1.9615 S22: 0.3062 S23: -3.7408 REMARK 3 S31: 2.5648 S32: 1.0052 S33: 0.4705 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 41 A 132 REMARK 3 ORIGIN FOR THE GROUP (A): 51.2840 -40.5410 78.7630 REMARK 3 T TENSOR REMARK 3 T11: 0.0711 T22: 0.0780 REMARK 3 T33: -0.2841 T12: -0.0007 REMARK 3 T13: -0.0029 T23: 0.4202 REMARK 3 L TENSOR REMARK 3 L11: 9.8112 L22: 8.7012 REMARK 3 L33: 4.6745 L12: -1.2009 REMARK 3 L13: -1.6517 L23: 5.1144 REMARK 3 S TENSOR REMARK 3 S11: 0.5181 S12: 0.2417 S13: 0.8900 REMARK 3 S21: -0.3670 S22: -0.3248 S23: -1.2106 REMARK 3 S31: -0.6866 S32: 0.8789 S33: -0.1934 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 2 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : U 1 U 80 REMARK 3 RESIDUE RANGE : A 9 A 40 REMARK 3 ORIGIN FOR THE GROUP (A): 32.4850 -38.1400 60.3870 REMARK 3 T TENSOR REMARK 3 T11: -0.0382 T22: -0.1934 REMARK 3 T33: -0.5517 T12: 0.0749 REMARK 3 T13: -0.1130 T23: 0.2814 REMARK 3 L TENSOR REMARK 3 L11: 6.1447 L22: 5.9408 REMARK 3 L33: 6.0103 L12: 2.0134 REMARK 3 L13: 0.3447 L23: -2.6643 REMARK 3 S TENSOR REMARK 3 S11: -0.0910 S12: -0.1513 S13: -0.1966 REMARK 3 S21: 0.1904 S22: 0.0273 S23: -0.0426 REMARK 3 S31: -0.0607 S32: 0.2014 S33: 0.0637 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 NUMBER OF COMPONENTS GROUP : 4 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : L 1 L 212 REMARK 3 RESIDUE RANGE : H 1 H 208 REMARK 3 RESIDUE RANGE : U 87 U 185 REMARK 3 RESIDUE RANGE : U 186 U 275 REMARK 3 ORIGIN FOR THE GROUP (A): 18.8100 -7.0670 18.9510 REMARK 3 T TENSOR REMARK 3 T11: -0.4237 T22: -0.3873 REMARK 3 T33: -0.4443 T12: -0.0247 REMARK 3 T13: 0.0117 T23: -0.0373 REMARK 3 L TENSOR REMARK 3 L11: 0.7195 L22: 1.7667 REMARK 3 L33: 2.1140 L12: 0.0287 REMARK 3 L13: 0.3308 L23: -1.4249 REMARK 3 S TENSOR REMARK 3 S11: 0.0931 S12: -0.0707 S13: 0.1554 REMARK 3 S21: 0.1367 S22: -0.2159 S23: -0.0153 REMARK 3 S31: 0.0124 S32: 0.2226 S33: 0.1228 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 3BT2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-JAN-08. REMARK 100 THE RCSB ID CODE IS RCSB045933. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL; NULL REMARK 200 TEMPERATURE (KELVIN) : 100; 100 REMARK 200 PH : 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 2 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y; Y REMARK 200 RADIATION SOURCE : APS; NSLS REMARK 200 BEAMLINE : 24-ID-C; X12C REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0; 1.0 REMARK 200 MONOCHROMATOR : NULL; NULL REMARK 200 OPTICS : NULL; NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD; CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315; ADSC QUANTUM REMARK 200 210 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38381 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2 REMARK 200 DATA REDUNDANCY : 5.300 REMARK 200 R MERGE (I) : 0.07700 REMARK 200 R SYM (I) : 0.07700 REMARK 200 FOR THE DATA SET : 24.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59 REMARK 200 COMPLETENESS FOR SHELL (%) : 96.0 REMARK 200 DATA REDUNDANCY IN SHELL : 4.10 REMARK 200 R MERGE FOR SHELL (I) : 0.35600 REMARK 200 R SYM FOR SHELL (I) : 0.35600 REMARK 200 FOR SHELL : 2.800 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: AMORE REMARK 200 STARTING MODEL: PDB ENTRY 2FD6 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 57.25 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG 4000, 2.5% ETHANOL, 0.05% REMARK 280 SODIUM AZIDE, 50MM CACODYLATE PH 6.5, PH 7.5, MICRODIALYSIS, REMARK 280 TEMPERATURE 295K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,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 43.60250 REMARK 290 SMTRY3 2 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: PENTAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, L, H, U 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 7200 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 38680 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.3 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, L, H, U 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: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: B 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 A -1 REMARK 465 SER A 0 REMARK 465 SER A 1 REMARK 465 ASN A 2 REMARK 465 GLU A 3 REMARK 465 LEU A 4 REMARK 465 HIS A 5 REMARK 465 GLN A 6 REMARK 465 VAL A 7 REMARK 465 PRO A 8 REMARK 465 ASP A 133 REMARK 465 CYS L 213 REMARK 465 GLY H 127 REMARK 465 GLY H 209 REMARK 465 ARG U 0 REMARK 465 SER U 81 REMARK 465 GLY U 82 REMARK 465 ARG U 83 REMARK 465 ALA U 84 REMARK 465 VAL U 85 REMARK 465 THR U 86 REMARK 465 GLN U 131 REMARK 465 GLU U 132 REMARK 465 GLY U 133 REMARK 465 GLU U 134 REMARK 465 GLU U 135 REMARK 465 GLY U 136 REMARK 465 ARG U 137 REMARK 465 PRO U 138 REMARK 465 HIS U 249 REMARK 465 ALA U 250 REMARK 465 HIS U 251 REMARK 465 LEU U 276 REMARK 465 ASP U 277 REMARK 465 VAL U 278 REMARK 465 GLN U 279 REMARK 465 TYR U 280 REMARK 465 ARG U 281 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 OE1 GLU L 105 OH TYR L 172 1.83 REMARK 500 NE2 HIS U 128 OE2 GLU U 183 1.92 REMARK 500 NE2 HIS U 143 OE2 GLU U 183 1.96 REMARK 500 O HIS U 273 N ASP U 275 1.99 REMARK 500 O ALA L 25 OG1 THR L 69 2.00 REMARK 500 O TYR L 93 N PHE L 96 2.01 REMARK 500 OH TYR A 58 O LYS A 61 2.01 REMARK 500 OD2 ASP A 12 NE2 HIS A 41 2.03 REMARK 500 CG1 VAL H 131 O VAL H 178 2.12 REMARK 500 OD2 ASP A 12 NE2 HIS A 29 2.13 REMARK 500 O TYR L 93 CD2 PHE L 96 2.19 REMARK 500 OE2 GLU L 50 ND1 HIS H 98 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 GLY A 38 C GLY A 38 O 0.132 REMARK 500 HIS A 41 CG HIS A 41 CD2 0.073 REMARK 500 CYS L 193 CB CYS L 193 SG -0.128 REMARK 500 LYS U 7 C LYS U 7 O 0.193 REMARK 500 GLU U 183 CB GLU U 183 CG 0.263 REMARK 500 GLU U 183 CD GLU U 183 OE2 0.077 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 88 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 LYS B 40 N - CA - C ANGL. DEV. = 17.3 DEGREES REMARK 500 TYR L 93 CB - CG - CD2 ANGL. DEV. = 4.0 DEGREES REMARK 500 TYR L 93 CB - CG - CD1 ANGL. DEV. = -4.6 DEGREES REMARK 500 PRO L 94 C - N - CA ANGL. DEV. = -10.9 DEGREES REMARK 500 ARG L 187 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 ARG L 187 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES REMARK 500 ASP H 101 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES REMARK 500 ARG U 192 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 ARG U 192 NE - CZ - NH2 ANGL. DEV. = -5.3 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 ASN A 10 -124.30 -70.15 REMARK 500 CYS A 11 74.86 57.51 REMARK 500 ASP A 12 1.55 -68.05 REMARK 500 ASN A 15 -131.98 66.58 REMARK 500 GLU A 52 -140.82 -84.63 REMARK 500 LYS A 61 -141.47 -90.12 REMARK 500 ALA A 62 101.01 79.80 REMARK 500 THR A 66 -36.93 -35.28 REMARK 500 ASN A 104 57.40 -162.21 REMARK 500 VAL A 128 124.58 -30.58 REMARK 500 LYS B 6 -49.50 177.51 REMARK 500 ARG B 8 -34.90 84.02 REMARK 500 THR B 10 48.80 -150.93 REMARK 500 CYS B 19 136.57 58.17 REMARK 500 GLU B 38 -90.13 -87.88 REMARK 500 LYS B 40 -99.16 -76.49 REMARK 500 ILE L 2 108.08 -10.69 REMARK 500 SER L 26 -29.40 -35.63 REMARK 500 TRP L 47 -57.54 -123.41 REMARK 500 GLU L 50 47.80 33.62 REMARK 500 ILE L 51 -52.64 90.41 REMARK 500 ALA L 84 -179.98 -175.63 REMARK 500 TYR L 93 -93.08 -17.74 REMARK 500 PRO L 94 -10.62 -36.89 REMARK 500 PHE L 96 32.97 38.65 REMARK 500 HIS H 52A -59.16 75.28 REMARK 500 SER H 82B 60.31 60.11 REMARK 500 SER H 129 -41.49 38.70 REMARK 500 MET H 130 8.82 -168.60 REMARK 500 VAL H 131 89.30 73.02 REMARK 500 SER H 155 -46.59 -140.69 REMARK 500 GLU U 34 -127.80 45.46 REMARK 500 ASP U 74 111.60 125.35 REMARK 500 SER U 88 83.50 79.65 REMARK 500 ARG U 89 -72.87 -130.06 REMARK 500 TYR U 92 -107.74 -113.37 REMARK 500 CYS U 153 -70.72 -79.45 REMARK 500 PRO U 154 102.81 -49.71 REMARK 500 ASN U 161 -158.68 -149.06 REMARK 500 GLU U 230 173.60 67.57 REMARK 500 PRO U 231 -83.56 -38.80 REMARK 500 LYS U 232 -169.77 -67.07 REMARK 500 ASN U 233 49.83 -84.44 REMARK 500 ASN U 259 -86.74 -131.63 REMARK 500 ASN U 272 -22.23 -25.11 REMARK 500 PRO U 274 33.34 -38.84 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 LYS A 61 ALA A 62 -138.66 REMARK 500 MET H 130 VAL H 131 143.58 REMARK 500 CYS U 271 ASN U 272 144.37 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 LYS B 40 3.3 L L EXPECTING SP3 REMARK 500 SER H 129 23.7 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 NAG U 1172 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG U 1200 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2FD6 RELATED DB: PDB REMARK 900 STRUCTURE OF UROKINASE RECEPTOR IN COMPLEX WITH UROKINASE REMARK 900 RELATED ID: 3BT1 RELATED DB: PDB REMARK 900 THE SAME PROTEIN COMPLEX WITHOUT FAB FRAGMENTS REMARK 999 REMARK 999 SEQUENCE REMARK 999 THIS COORDINATES IN CHAINS L AND H ARE USED NON-SEQUENTIAL REMARK 999 RESIDUE NUMBERING. IT IS DUE TO KABAT-WU NUMBERING, WHICH IS REMARK 999 TYPICAL FOR ANTIBODY.