REMARK 2 REMARK 2 RESOLUTION. 2.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.5.0109 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) : 2.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.20 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7 REMARK 3 NUMBER OF REFLECTIONS : 77145 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) : 0.203 REMARK 3 R VALUE (WORKING SET) : 0.202 REMARK 3 FREE R VALUE : 0.252 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1533 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) : 2.10 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15 REMARK 3 REFLECTION IN BIN (WORKING SET) : 5221 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.81 REMARK 3 BIN R VALUE (WORKING SET) : 0.2680 REMARK 3 BIN FREE R VALUE SET COUNT : 90 REMARK 3 BIN FREE R VALUE : 0.3290 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 10196 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 39 REMARK 3 SOLVENT ATOMS : 492 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.43 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.00000 REMARK 3 B22 (A**2) : 0.01000 REMARK 3 B33 (A**2) : -0.01000 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): 0.248 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.203 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.161 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.442 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.932 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10583 ; 0.008 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14432 ; 1.123 ; 1.947 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1327 ; 5.973 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 444 ;34.084 ;24.414 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1674 ;13.923 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 35 ;17.485 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1605 ; 0.073 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8024 ; 0.004 ; 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): 6597 ; 0.376 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10709 ; 0.693 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3986 ; 1.061 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3715 ; 1.612 ; 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 : 10 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 : H 2 H 119 REMARK 3 ORIGIN FOR THE GROUP (A): -6.7421 9.4581 22.3345 REMARK 3 T TENSOR REMARK 3 T11: 0.1612 T22: 0.1339 REMARK 3 T33: 0.1742 T12: 0.1133 REMARK 3 T13: -0.0883 T23: -0.0374 REMARK 3 L TENSOR REMARK 3 L11: 0.9070 L22: 2.3955 REMARK 3 L33: 4.9262 L12: 0.3672 REMARK 3 L13: -0.3035 L23: -1.1474 REMARK 3 S TENSOR REMARK 3 S11: -0.1401 S12: -0.0670 S13: 0.1115 REMARK 3 S21: 0.1050 S22: 0.0865 S23: 0.1659 REMARK 3 S31: -0.4197 S32: -0.2523 S33: 0.0536 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 : H 120 H 219 REMARK 3 ORIGIN FOR THE GROUP (A): -4.4282 4.8885 -11.0162 REMARK 3 T TENSOR REMARK 3 T11: 0.0630 T22: 0.0402 REMARK 3 T33: 0.0691 T12: -0.0259 REMARK 3 T13: -0.0341 T23: 0.0298 REMARK 3 L TENSOR REMARK 3 L11: 2.2178 L22: 6.5080 REMARK 3 L33: 2.9263 L12: 0.0949 REMARK 3 L13: 0.0138 L23: 1.9120 REMARK 3 S TENSOR REMARK 3 S11: -0.0014 S12: 0.1166 S13: -0.2062 REMARK 3 S21: -0.1652 S22: -0.0773 S23: -0.0114 REMARK 3 S31: 0.1766 S32: 0.0420 S33: 0.0787 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : L 2 L 107 REMARK 3 ORIGIN FOR THE GROUP (A): 1.8329 -11.0569 21.0054 REMARK 3 T TENSOR REMARK 3 T11: 0.0945 T22: 0.0754 REMARK 3 T33: 0.1086 T12: 0.0445 REMARK 3 T13: -0.0352 T23: 0.0073 REMARK 3 L TENSOR REMARK 3 L11: 0.5623 L22: 2.9160 REMARK 3 L33: 3.2830 L12: -0.6921 REMARK 3 L13: -0.1747 L23: 2.5841 REMARK 3 S TENSOR REMARK 3 S11: -0.0923 S12: -0.1262 S13: -0.0468 REMARK 3 S21: 0.0486 S22: 0.0436 S23: 0.1399 REMARK 3 S31: 0.1514 S32: -0.0232 S33: 0.0487 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : L 108 L 212 REMARK 3 ORIGIN FOR THE GROUP (A): 10.1415 -1.8113 -13.6779 REMARK 3 T TENSOR REMARK 3 T11: 0.1190 T22: 0.1851 REMARK 3 T33: 0.2265 T12: 0.0190 REMARK 3 T13: 0.0567 T23: 0.0409 REMARK 3 L TENSOR REMARK 3 L11: 0.8180 L22: 6.9825 REMARK 3 L33: 5.1584 L12: 0.3047 REMARK 3 L13: -0.4913 L23: -3.8003 REMARK 3 S TENSOR REMARK 3 S11: 0.0623 S12: 0.0885 S13: 0.0668 REMARK 3 S21: -0.3707 S22: -0.3066 S23: -0.8466 REMARK 3 S31: 0.0168 S32: 0.6620 S33: 0.2443 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : X 2 X 236 REMARK 3 ORIGIN FOR THE GROUP (A): 3.9721 27.7818 98.6338 REMARK 3 T TENSOR REMARK 3 T11: 0.0704 T22: 0.2125 REMARK 3 T33: 0.0974 T12: -0.0054 REMARK 3 T13: 0.0305 T23: -0.0400 REMARK 3 L TENSOR REMARK 3 L11: 2.9997 L22: 3.3961 REMARK 3 L33: 3.5222 L12: 0.1430 REMARK 3 L13: -0.6989 L23: -0.3125 REMARK 3 S TENSOR REMARK 3 S11: 0.1048 S12: -0.2949 S13: 0.1729 REMARK 3 S21: 0.1255 S22: -0.1731 S23: 0.1083 REMARK 3 S31: -0.2395 S32: -0.1031 S33: 0.0683 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 2 A 119 REMARK 3 ORIGIN FOR THE GROUP (A): 13.6744 32.5197 71.1828 REMARK 3 T TENSOR REMARK 3 T11: 0.1647 T22: 0.0531 REMARK 3 T33: 0.0699 T12: 0.0654 REMARK 3 T13: 0.0141 T23: -0.0140 REMARK 3 L TENSOR REMARK 3 L11: 0.8645 L22: 2.5229 REMARK 3 L33: 3.8947 L12: 1.1325 REMARK 3 L13: -0.9160 L23: -2.1990 REMARK 3 S TENSOR REMARK 3 S11: 0.0463 S12: 0.0318 S13: 0.1210 REMARK 3 S21: 0.3520 S22: 0.0773 S23: 0.1700 REMARK 3 S31: -0.3892 S32: -0.2248 S33: -0.1235 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 120 A 219 REMARK 3 ORIGIN FOR THE GROUP (A): 18.7446 28.4500 38.3794 REMARK 3 T TENSOR REMARK 3 T11: 0.0445 T22: 0.0850 REMARK 3 T33: 0.0768 T12: -0.0312 REMARK 3 T13: -0.0383 T23: 0.0151 REMARK 3 L TENSOR REMARK 3 L11: 1.4753 L22: 7.5752 REMARK 3 L33: 1.9706 L12: 0.1506 REMARK 3 L13: -0.5481 L23: 2.0169 REMARK 3 S TENSOR REMARK 3 S11: -0.0519 S12: 0.2465 S13: -0.1635 REMARK 3 S21: -0.3334 S22: 0.0068 S23: 0.2892 REMARK 3 S31: 0.0841 S32: -0.1307 S33: 0.0450 REMARK 3 REMARK 3 TLS GROUP : 8 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 2 B 107 REMARK 3 ORIGIN FOR THE GROUP (A): 22.5244 12.2753 70.5238 REMARK 3 T TENSOR REMARK 3 T11: 0.0189 T22: 0.0219 REMARK 3 T33: 0.0514 T12: -0.0027 REMARK 3 T13: -0.0286 T23: 0.0082 REMARK 3 L TENSOR REMARK 3 L11: 0.7692 L22: 3.0469 REMARK 3 L33: 3.5912 L12: -0.3681 REMARK 3 L13: -0.7273 L23: 1.7018 REMARK 3 S TENSOR REMARK 3 S11: 0.0295 S12: -0.0227 S13: -0.1036 REMARK 3 S21: 0.0634 S22: 0.0034 S23: -0.0735 REMARK 3 S31: -0.0000 S32: 0.0189 S33: -0.0329 REMARK 3 REMARK 3 TLS GROUP : 9 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 108 B 212 REMARK 3 ORIGIN FOR THE GROUP (A): 33.2227 21.8514 36.4134 REMARK 3 T TENSOR REMARK 3 T11: 0.0553 T22: 0.1197 REMARK 3 T33: 0.0801 T12: -0.0020 REMARK 3 T13: 0.0214 T23: -0.0138 REMARK 3 L TENSOR REMARK 3 L11: 0.7992 L22: 5.1746 REMARK 3 L33: 4.2897 L12: 0.7330 REMARK 3 L13: -1.0873 L23: -3.5324 REMARK 3 S TENSOR REMARK 3 S11: 0.0718 S12: 0.0360 S13: 0.0004 REMARK 3 S21: -0.2686 S22: -0.2463 S23: -0.4195 REMARK 3 S31: -0.0249 S32: 0.4263 S33: 0.1745 REMARK 3 REMARK 3 TLS GROUP : 10 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : C 3 C 235 REMARK 3 ORIGIN FOR THE GROUP (A): -11.9017 5.6961 51.0756 REMARK 3 T TENSOR REMARK 3 T11: 0.0579 T22: 0.3447 REMARK 3 T33: 0.1926 T12: 0.0589 REMARK 3 T13: 0.0071 T23: 0.0159 REMARK 3 L TENSOR REMARK 3 L11: 2.9688 L22: 5.0949 REMARK 3 L33: 5.2342 L12: -1.1291 REMARK 3 L13: 0.3033 L23: -0.6886 REMARK 3 S TENSOR REMARK 3 S11: 0.0587 S12: -0.2027 S13: -0.0622 REMARK 3 S21: 0.1029 S22: 0.0225 S23: 0.5980 REMARK 3 S31: -0.2398 S32: -0.5718 S33: -0.0811 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: REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS REMARK 3 U VALUES : WITH TLS ADDED REMARK 4 REMARK 4 4ETQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAY-12. REMARK 100 THE RCSB ID CODE IS RCSB072057. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-DEC-10 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRL REMARK 200 BEAMLINE : BL11-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.98 REMARK 200 MONOCHROMATOR : SIDE SCATTERING I-BEAM BENT REMARK 200 SINGLE CRYSTAL, ASYMMETRIC CUT REMARK 200 4.9650 DEGREES REMARK 200 OPTICS : SAMPLE TO DETECTOR DISTANCE: REMARK 200 185-650 MM, MAXIMUM VERTICAL REMARK 200 OFFSET: 208 MM REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 77173 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100 REMARK 200 RESOLUTION RANGE LOW (A) : 40.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8 REMARK 200 DATA REDUNDANCY : 3.100 REMARK 200 R MERGE (I) : 0.08600 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 10.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18 REMARK 200 COMPLETENESS FOR SHELL (%) : 93.2 REMARK 200 DATA REDUNDANCY IN SHELL : 3.00 REMARK 200 R MERGE FOR SHELL (I) : 0.45900 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: MOLREP REMARK 200 STARTING MODEL: PDB ENTRIES 1NSN AND 3JXF REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 43.70 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M POTASSIUM THIOCYANATE, 20% REMARK 280 PEG3350, VAPOR DIFFUSION, SITTING DROP, 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 45.57800 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 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: 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 APPLY THE FOLLOWING TO CHAINS: A, B, X 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 GLY H 136 REMARK 465 ASP H 137 REMARK 465 THR H 138 REMARK 465 THR H 139 REMARK 465 GLY H 221 REMARK 465 GLY H 222 REMARK 465 ASP A 137 REMARK 465 THR A 138 REMARK 465 THR A 139 REMARK 465 GLY A 222 REMARK 465 MET X 1 REMARK 465 SER X 206 REMARK 465 ASN X 207 REMARK 465 HIS X 208 REMARK 465 GLU X 209 REMARK 465 GLY X 210 REMARK 465 LYS X 211 REMARK 465 PRO X 212 REMARK 465 ILE X 237 REMARK 465 ILE X 238 REMARK 465 ARG X 239 REMARK 465 ALA X 240 REMARK 465 ALA X 241 REMARK 465 THR X 242 REMARK 465 THR X 243 REMARK 465 SER X 244 REMARK 465 PRO X 245 REMARK 465 ALA X 246 REMARK 465 ARG X 247 REMARK 465 GLU X 248 REMARK 465 ASN X 249 REMARK 465 TYR X 250 REMARK 465 PHE X 251 REMARK 465 MET X 252 REMARK 465 ARG X 253 REMARK 465 TRP X 254 REMARK 465 LEU X 255 REMARK 465 SER X 256 REMARK 465 ASP X 257 REMARK 465 LEU X 258 REMARK 465 ARG X 259 REMARK 465 GLU X 260 REMARK 465 THR X 261 REMARK 465 LEU X 262 REMARK 465 GLU X 263 REMARK 465 HIS X 264 REMARK 465 HIS X 265 REMARK 465 HIS X 266 REMARK 465 HIS X 267 REMARK 465 HIS X 268 REMARK 465 HIS X 269 REMARK 465 MET C 1 REMARK 465 PRO C 2 REMARK 465 SER C 206 REMARK 465 ASN C 207 REMARK 465 HIS C 208 REMARK 465 GLU C 209 REMARK 465 GLY C 210 REMARK 465 LYS C 211 REMARK 465 PRO C 212 REMARK 465 HIS C 213 REMARK 465 GLU C 236 REMARK 465 ILE C 237 REMARK 465 ILE C 238 REMARK 465 ARG C 239 REMARK 465 ALA C 240 REMARK 465 ALA C 241 REMARK 465 THR C 242 REMARK 465 THR C 243 REMARK 465 SER C 244 REMARK 465 PRO C 245 REMARK 465 ALA C 246 REMARK 465 ARG C 247 REMARK 465 GLU C 248 REMARK 465 ASN C 249 REMARK 465 TYR C 250 REMARK 465 PHE C 251 REMARK 465 MET C 252 REMARK 465 ARG C 253 REMARK 465 TRP C 254 REMARK 465 LEU C 255 REMARK 465 SER C 256 REMARK 465 ASP C 257 REMARK 465 LEU C 258 REMARK 465 ARG C 259 REMARK 465 GLU C 260 REMARK 465 THR C 261 REMARK 465 LEU C 262 REMARK 465 GLU C 263 REMARK 465 HIS C 264 REMARK 465 HIS C 265 REMARK 465 HIS C 266 REMARK 465 HIS C 267 REMARK 465 HIS C 268 REMARK 465 HIS C 269 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 GLN H 2 CG CD OE1 NE2 REMARK 470 LYS H 66 CG CD CE NZ REMARK 470 GLN L 2 CG CD OE1 NE2 REMARK 470 PRO X 2 CG CD REMARK 470 LYS X 13 CG CD CE NZ REMARK 470 LYS X 32 CG CD CE NZ REMARK 470 LYS X 48 CG CD CE NZ REMARK 470 ARG X 142 CG CD NE CZ NH1 NH2 REMARK 470 LYS X 198 CG CD CE NZ REMARK 470 LYS X 224 CG CD CE NZ REMARK 470 GLN C 3 CG CD OE1 NE2 REMARK 470 ASN C 18 CG OD1 ND2 REMARK 470 LYS C 32 CG CD CE NZ REMARK 470 LYS C 108 CG CD CE NZ REMARK 470 LYS C 127 CG CD CE NZ REMARK 470 VAL C 129 CG1 CG2 REMARK 470 TYR C 130 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ILE C 134 CG1 CG2 CD1 REMARK 470 ASP C 139 CG OD1 OD2 REMARK 470 SER C 140 OG REMARK 470 ASN C 145 CG OD1 ND2 REMARK 470 LYS C 198 CG CD CE NZ REMARK 470 LEU C 203 CG CD1 CD2 REMARK 470 TYR C 214 CG CD1 CD2 CE1 CE2 CZ OH 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 PRO H 42 -33.14 -38.06 REMARK 500 SER H 86 64.02 36.98 REMARK 500 SER H 141 -33.64 81.17 REMARK 500 THR L 51 -53.23 73.27 REMARK 500 ARG L 77 75.57 89.27 REMARK 500 ASN L 212 51.86 -113.59 REMARK 500 LYS A 68 -51.87 -126.41 REMARK 500 SER A 86 58.26 34.53 REMARK 500 SER A 119 142.94 -171.54 REMARK 500 VAL A 134 152.09 -48.85 REMARK 500 CYS A 135 -80.05 -50.16 REMARK 500 THR B 51 -45.78 79.81 REMARK 500 ARG B 77 67.59 78.76 REMARK 500 HIS X 27 75.34 -112.36 REMARK 500 THR X 34 -74.73 -102.07 REMARK 500 ASN X 59 -166.70 -162.99 REMARK 500 TYR X 76 85.20 -155.14 REMARK 500 ASP X 125 41.79 -87.75 REMARK 500 SER X 152 -166.25 68.27 REMARK 500 ASN X 218 11.34 -146.89 REMARK 500 ALA C 19 41.68 -97.67 REMARK 500 THR C 34 -70.03 -86.16 REMARK 500 TYR C 76 90.72 -160.56 REMARK 500 ASN C 79 -61.95 -92.56 REMARK 500 ASP C 125 59.17 -95.45 REMARK 500 LYS C 133 -16.37 -47.78 REMARK 500 ILE C 215 78.06 -100.41 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 L 466 DISTANCE = 6.50 ANGSTROMS REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 SCN A 303 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN H 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL L 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN L 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN A 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN A 303 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN B 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN X 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 301 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4EBQ RELATED DB: PDB REMARK 900 FAB STRUCTURE OF ANTI-VACCINIA VIRUS D8L ANTIGEN MICE IGG2A REMARK 900 LA5 REMARK 900 RELATED ID: 4E9O RELATED DB: PDB REMARK 900 VACCINIA D8L ECTODOMAIN STRUCTURE