REMARK 2 REMARK 2 RESOLUTION. 1.95 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) : 1.95 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9 REMARK 3 NUMBER OF REFLECTIONS : NULL 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) : 0.200 REMARK 3 R VALUE (WORKING SET) : 0.198 REMARK 3 FREE R VALUE : 0.245 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 6188 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) : 1.94 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.99 REMARK 3 REFLECTION IN BIN (WORKING SET) : 7724 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.27 REMARK 3 BIN R VALUE (WORKING SET) : 0.2790 REMARK 3 BIN FREE R VALUE SET COUNT : 410 REMARK 3 BIN FREE R VALUE : 0.3180 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 12561 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 66 REMARK 3 SOLVENT ATOMS : 802 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.31 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 3.84000 REMARK 3 B22 (A**2) : -2.56000 REMARK 3 B33 (A**2) : -0.79000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 1.28000 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): 0.165 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.132 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.587 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.947 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 12901 ; 0.019 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 17570 ; 1.741 ; 1.956 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1677 ; 7.303 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 463 ;33.199 ;24.039 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1974 ;16.174 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 52 ;22.390 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1993 ; 0.129 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9652 ; 0.009 ; 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): 8391 ; 1.106 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 13530 ; 1.935 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4510 ; 3.039 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4040 ; 4.773 ; 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 : 8 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 1 H 212 REMARK 3 ORIGIN FOR THE GROUP (A): 27.9193 49.6122 15.7269 REMARK 3 T TENSOR REMARK 3 T11: 0.0217 T22: 0.1242 REMARK 3 T33: 0.1493 T12: 0.0055 REMARK 3 T13: -0.0414 T23: -0.0002 REMARK 3 L TENSOR REMARK 3 L11: 0.2892 L22: 0.0241 REMARK 3 L33: 0.5196 L12: -0.0820 REMARK 3 L13: -0.1335 L23: 0.0229 REMARK 3 S TENSOR REMARK 3 S11: -0.0245 S12: 0.0102 S13: -0.0099 REMARK 3 S21: 0.0108 S22: -0.0024 S23: -0.0026 REMARK 3 S31: -0.0356 S32: -0.0050 S33: 0.0269 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 : L 4 L 210 REMARK 3 ORIGIN FOR THE GROUP (A): 34.3225 65.2480 22.7566 REMARK 3 T TENSOR REMARK 3 T11: 0.0616 T22: 0.1272 REMARK 3 T33: 0.1179 T12: -0.0107 REMARK 3 T13: -0.0257 T23: -0.0047 REMARK 3 L TENSOR REMARK 3 L11: 0.0322 L22: 0.2824 REMARK 3 L33: 0.4964 L12: 0.0481 REMARK 3 L13: -0.1052 L23: -0.2786 REMARK 3 S TENSOR REMARK 3 S11: 0.0211 S12: 0.0261 S13: 0.0030 REMARK 3 S21: 0.0981 S22: 0.0095 S23: -0.0247 REMARK 3 S31: -0.0841 S32: 0.0093 S33: -0.0307 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 : A 1 A 213 REMARK 3 ORIGIN FOR THE GROUP (A): 19.2304 24.2048 51.6113 REMARK 3 T TENSOR REMARK 3 T11: 0.0875 T22: 0.1331 REMARK 3 T33: 0.0909 T12: 0.0173 REMARK 3 T13: 0.0161 T23: -0.0261 REMARK 3 L TENSOR REMARK 3 L11: 0.0119 L22: 0.3835 REMARK 3 L33: 0.8131 L12: -0.0169 REMARK 3 L13: 0.0491 L23: -0.1066 REMARK 3 S TENSOR REMARK 3 S11: -0.0115 S12: 0.0288 S13: -0.0136 REMARK 3 S21: 0.1209 S22: 0.0209 S23: 0.0676 REMARK 3 S31: -0.1432 S32: -0.0601 S33: -0.0094 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 : B 4 B 210 REMARK 3 ORIGIN FOR THE GROUP (A): 29.0500 9.7401 48.1163 REMARK 3 T TENSOR REMARK 3 T11: 0.1024 T22: 0.1007 REMARK 3 T33: 0.0871 T12: 0.0100 REMARK 3 T13: 0.0277 T23: -0.0048 REMARK 3 L TENSOR REMARK 3 L11: 0.0200 L22: 0.1390 REMARK 3 L33: 1.8558 L12: 0.0200 REMARK 3 L13: -0.1406 L23: -0.2916 REMARK 3 S TENSOR REMARK 3 S11: -0.0120 S12: 0.0118 S13: 0.0176 REMARK 3 S21: 0.0263 S22: -0.0110 S23: 0.0205 REMARK 3 S31: 0.1100 S32: 0.0757 S33: 0.0230 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 : C 1 C 213 REMARK 3 ORIGIN FOR THE GROUP (A): 56.5167 3.9904 51.5650 REMARK 3 T TENSOR REMARK 3 T11: 0.1032 T22: 0.0985 REMARK 3 T33: 0.0875 T12: 0.0432 REMARK 3 T13: 0.0572 T23: -0.0073 REMARK 3 L TENSOR REMARK 3 L11: 0.0810 L22: 0.5720 REMARK 3 L33: 1.0671 L12: 0.1331 REMARK 3 L13: -0.0726 L23: 0.4510 REMARK 3 S TENSOR REMARK 3 S11: 0.0141 S12: 0.0094 S13: 0.0175 REMARK 3 S21: 0.0435 S22: -0.0643 S23: 0.0909 REMARK 3 S31: -0.0343 S32: -0.0537 S33: 0.0502 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 : D 4 D 210 REMARK 3 ORIGIN FOR THE GROUP (A): 65.7399 -10.9954 47.8814 REMARK 3 T TENSOR REMARK 3 T11: 0.1362 T22: 0.1047 REMARK 3 T33: 0.0715 T12: 0.0252 REMARK 3 T13: 0.0134 T23: 0.0151 REMARK 3 L TENSOR REMARK 3 L11: 0.0417 L22: 0.3042 REMARK 3 L33: 1.4081 L12: 0.0858 REMARK 3 L13: -0.1524 L23: -0.2601 REMARK 3 S TENSOR REMARK 3 S11: -0.0197 S12: 0.0220 S13: 0.0069 REMARK 3 S21: 0.0687 S22: -0.0277 S23: -0.0021 REMARK 3 S31: 0.0964 S32: -0.0007 S33: 0.0475 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 : E 1 E 211 REMARK 3 ORIGIN FOR THE GROUP (A): 64.4579 28.5476 15.6435 REMARK 3 T TENSOR REMARK 3 T11: 0.0291 T22: 0.1289 REMARK 3 T33: 0.1473 T12: 0.0049 REMARK 3 T13: -0.0473 T23: 0.0046 REMARK 3 L TENSOR REMARK 3 L11: 0.1207 L22: 0.0033 REMARK 3 L33: 0.5180 L12: -0.0025 REMARK 3 L13: -0.1217 L23: -0.0168 REMARK 3 S TENSOR REMARK 3 S11: -0.0147 S12: 0.0077 S13: 0.0008 REMARK 3 S21: 0.0048 S22: 0.0117 S23: 0.0032 REMARK 3 S31: -0.0191 S32: -0.0124 S33: 0.0030 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 : F 4 F 210 REMARK 3 ORIGIN FOR THE GROUP (A): 70.8773 44.4447 22.4067 REMARK 3 T TENSOR REMARK 3 T11: 0.0755 T22: 0.1191 REMARK 3 T33: 0.1214 T12: -0.0084 REMARK 3 T13: -0.0277 T23: -0.0048 REMARK 3 L TENSOR REMARK 3 L11: 0.0573 L22: 0.1410 REMARK 3 L33: 0.4011 L12: 0.0775 REMARK 3 L13: -0.1163 L23: -0.1646 REMARK 3 S TENSOR REMARK 3 S11: 0.0346 S12: 0.0338 S13: 0.0115 REMARK 3 S21: 0.0869 S22: 0.0052 S23: -0.0035 REMARK 3 S31: -0.0417 S32: 0.0266 S33: -0.0398 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: NULL REMARK 4 REMARK 4 3TNN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-SEP-11. REMARK 100 THE RCSB ID CODE IS RCSB067694. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 29-APR-11 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 : BL7-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : AREA DETECTOR REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 115389 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950 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 (%) : 93.3 REMARK 200 DATA REDUNDANCY : 3.400 REMARK 200 R MERGE (I) : 0.11300 REMARK 200 R SYM (I) : 0.08200 REMARK 200 FOR THE DATA SET : 12.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.98 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.5 REMARK 200 DATA REDUNDANCY IN SHELL : 3.50 REMARK 200 R MERGE FOR SHELL (I) : 0.76500 REMARK 200 R SYM FOR SHELL (I) : 0.61300 REMARK 200 FOR SHELL : 2.000 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: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 47.24 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM SULFATE, 30% PEG 4000, REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K 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 42.25250 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, 4 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3230 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18860 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3160 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18870 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350 REMARK 350 BIOMOLECULE: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3090 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18760 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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: 4 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3070 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18730 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 SER H 127 REMARK 465 SER H 128 REMARK 465 LYS H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 SER H 132 REMARK 465 GLY H 133 REMARK 465 PRO H 213 REMARK 465 LYS H 214 REMARK 465 SER H 215 REMARK 465 CYS H 216 REMARK 465 ASP H 217 REMARK 465 LYS H 218 REMARK 465 THR H 219 REMARK 465 HIS H 220 REMARK 465 GLN L 2 REMARK 465 SER L 3 REMARK 465 GLU L 211 REMARK 465 CYS L 212 REMARK 465 SER L 213 REMARK 465 SER A 127 REMARK 465 SER A 128 REMARK 465 LYS A 129 REMARK 465 SER A 130 REMARK 465 THR A 131 REMARK 465 SER A 132 REMARK 465 GLY A 133 REMARK 465 LYS A 214 REMARK 465 SER A 215 REMARK 465 CYS A 216 REMARK 465 ASP A 217 REMARK 465 LYS A 218 REMARK 465 THR A 219 REMARK 465 HIS A 220 REMARK 465 GLN B 2 REMARK 465 SER B 3 REMARK 465 GLU B 211 REMARK 465 CYS B 212 REMARK 465 SER B 213 REMARK 465 SER C 127 REMARK 465 SER C 128 REMARK 465 LYS C 129 REMARK 465 SER C 130 REMARK 465 THR C 131 REMARK 465 SER C 132 REMARK 465 GLY C 133 REMARK 465 LYS C 214 REMARK 465 SER C 215 REMARK 465 CYS C 216 REMARK 465 ASP C 217 REMARK 465 LYS C 218 REMARK 465 THR C 219 REMARK 465 HIS C 220 REMARK 465 GLN D 2 REMARK 465 SER D 3 REMARK 465 GLU D 211 REMARK 465 CYS D 212 REMARK 465 SER D 213 REMARK 465 SER E 127 REMARK 465 SER E 128 REMARK 465 LYS E 129 REMARK 465 SER E 130 REMARK 465 THR E 131 REMARK 465 SER E 132 REMARK 465 GLY E 133 REMARK 465 GLU E 212 REMARK 465 PRO E 213 REMARK 465 LYS E 214 REMARK 465 SER E 215 REMARK 465 CYS E 216 REMARK 465 ASP E 217 REMARK 465 LYS E 218 REMARK 465 THR E 219 REMARK 465 HIS E 220 REMARK 465 GLN F 2 REMARK 465 SER F 3 REMARK 465 GLU F 211 REMARK 465 CYS F 212 REMARK 465 SER F 213 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 OE1 GLU H 1 O HOH E 471 2655 1.79 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 SER D 10 C VAL D 11 N 0.155 REMARK 500 TYR E 90 CE2 TYR E 90 CD2 0.096 REMARK 500 GLU E 148 CD GLU E 148 OE2 0.068 REMARK 500 TYR F 49 CD1 TYR F 49 CE1 0.112 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 H 66 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES REMARK 500 ARG H 66 NE - CZ - NH2 ANGL. DEV. = -6.0 DEGREES REMARK 500 ARG L 54 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES REMARK 500 ARG L 54 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES REMARK 500 LEU B 181 CA - CB - CG ANGL. DEV. = 14.2 DEGREES REMARK 500 ARG C 66 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES REMARK 500 ARG C 66 NE - CZ - NH2 ANGL. DEV. = -4.4 DEGREES REMARK 500 ARG E 66 NE - CZ - NH1 ANGL. DEV. = 5.6 DEGREES REMARK 500 ARG E 66 NE - CZ - NH2 ANGL. DEV. = -7.6 DEGREES REMARK 500 VAL E 169 CB - CA - C ANGL. DEV. = -13.1 DEGREES REMARK 500 ARG F 54 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 ARG F 54 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES REMARK 500 SER F 169 N - CA - C ANGL. DEV. = -20.1 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 H 144 63.71 69.88 REMARK 500 THR H 160 -32.07 -131.15 REMARK 500 THR H 191 -59.05 -127.91 REMARK 500 ASP L 27B -82.77 -142.20 REMARK 500 ASN L 31 51.28 -100.12 REMARK 500 VAL L 51 -42.29 70.50 REMARK 500 ALA L 84 168.09 171.50 REMARK 500 PHE L 95B -60.08 69.53 REMARK 500 PRO L 142 -175.36 -68.40 REMARK 500 ASP L 152 -106.31 55.90 REMARK 500 ASN L 171 -2.12 85.62 REMARK 500 GLU L 199 70.34 54.36 REMARK 500 ASP A 144 76.36 67.68 REMARK 500 SER A 156 28.39 49.50 REMARK 500 THR A 160 -36.77 -130.69 REMARK 500 ASP B 27B -88.13 -133.38 REMARK 500 ASN B 31 49.56 -98.60 REMARK 500 VAL B 51 -39.13 68.01 REMARK 500 ALA B 84 174.70 173.25 REMARK 500 PHE B 95B -73.41 70.99 REMARK 500 ASP B 152 -116.40 55.90 REMARK 500 ASN B 171 -5.43 76.06 REMARK 500 ALA C 88 158.57 178.88 REMARK 500 ASP C 144 68.56 62.68 REMARK 500 SER C 187 -8.77 -47.24 REMARK 500 LEU C 189 -80.07 -35.27 REMARK 500 ASP D 27B -82.77 -135.30 REMARK 500 ASN D 31 58.68 -104.18 REMARK 500 VAL D 51 -39.93 69.89 REMARK 500 ALA D 84 176.90 179.50 REMARK 500 PHE D 95B -61.90 74.85 REMARK 500 ASP D 152 -114.30 47.16 REMARK 500 ASN D 171 -10.10 71.92 REMARK 500 ALA E 88 161.85 179.40 REMARK 500 ASP E 144 61.95 65.07 REMARK 500 ASP F 27B -85.64 -129.43 REMARK 500 ASN F 31 51.66 -93.56 REMARK 500 VAL F 51 -39.25 69.44 REMARK 500 PHE F 95B -72.80 68.27 REMARK 500 ASP F 152 -114.40 53.20 REMARK 500 ALA F 158 109.38 74.66 REMARK 500 GLN F 168 -115.72 -86.58 REMARK 500 SER F 169 -117.25 -68.59 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 VAL B 106 ARG B 107 -147.49 REMARK 500 GLY D 108 GLN D 109 -138.95 REMARK 500 VAL F 156 LYS F 157 148.01 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 VAL L 51 23.9 L L OUTSIDE RANGE REMARK 500 VAL B 51 23.7 L L OUTSIDE RANGE REMARK 500 VAL D 51 22.0 L L OUTSIDE RANGE REMARK 500 VAL F 51 20.6 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 SO4 H 221 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 L 214 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 214 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 214 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 215 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 214 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 215 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 H 222 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL H 223 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL L 215 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 1 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL L 216 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 221 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 221 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL F 216 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 222 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL F 217 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 215 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 223 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 216 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL H 224 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL L 217 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL H 225 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3QEH RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HUMAN N12-I15 FAB, AN ADCC AND NON- REMARK 900 NEUTRALIZING ANTI-HIV-1 ENV ANTIBODY REMARK 900 RELATED ID: 3TNM RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF A32 FAB, AN ADCC ANTI-HIV-1 ENV REMARK 900 ANTIBODY REMARK 900 RELATED ID: 3QEG RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HUMAN N12-I2 FAB, AN ADCC AND REMARK 900 NEUTRALIZING ANTI-HIV-1 ENV ANTIBODY